data_4YWT
# 
_entry.id   4YWT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4YWT         
WWPDB D_1000208211 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          4ad7 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        4YWT 
_pdbx_database_status.recvd_initial_deposition_date   2015-03-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Awad, W.'    1 
'Mani, K.'    2 
'Logan, D.T.' 3 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary J.Biol.Chem.                             JBCHA3 0071 1083-351X ? ? 290 ? 22991 23008 
'Structural Aspects of N-Glycosylations and the C-terminal Region in Human Glypican-1.' 2015 ? 10.1074/jbc.M115.660878   26203194 
? 
? ? ? ? ? ? ? US ? ? 1       'Acta Crystallogr. D Biol. Crystallogr.' ABCRE6 ?    1399-0047 ? ? 69  ? 2524  2533  
'Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration.' 2013 ? 
10.1107/S0907444913025250 24311593 ? 
? ? ? ? ? ? ? US ? ? 2       'J. Biol. Chem.'                         JBCHA3 0071 1083-351X ? ? 287 ? 14040 14051 
;Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1.
;
2012 ? 10.1074/jbc.M111.322487   22351761 ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Awad, W.'              1  
primary 'Adamczyk, B.'          2  
primary 'Ornros, J.'            3  
primary 'Karlsson, N.G.'        4  
primary 'Mani, K.'              5  
primary 'Logan, D.T.'           6  
1       'Awad, W.'              7  
1       'Svensson Birkedal, G.' 8  
1       'Thunnissen, M.M.'      9  
1       'Mani, K.'              10 
1       'Logan, D.T.'           11 
2       'Svensson, G.'          12 
2       'Awad, W.'              13 
2       'Hakansson, M.'         14 
2       'Mani, K.'              15 
2       'Logan, D.T.'           16 
# 
_cell.entry_id           4YWT 
_cell.length_a           46.780 
_cell.length_b           166.590 
_cell.length_c           137.700 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.38 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4YWT 
_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     man Glypican-1             58506.973 4   ? 'S486A, S488A and S490A' 'UNP residues 24-527' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   4   ? ?                        ?                     ? 
3 non-polymer syn 'CALCIUM ION'          40.078    9   ? ?                        ?                     ? 
4 water       nat water                  18.015    284 ? ?                        ?                     ? 
# 
_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       
;APQLHHHHHHDLYENLYFQGKLDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRS
HAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEE
TLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVP
LGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWL
AEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLC
SEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDA
SDDGAGAGAGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;APQLHHHHHHDLYENLYFQGKLDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRS
HAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEE
TLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVP
LGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWL
AEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLC
SEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDA
SDDGAGAGAGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   ALA n 
1 2   PRO n 
1 3   GLN n 
1 4   LEU n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  ASP n 
1 12  LEU n 
1 13  TYR n 
1 14  GLU n 
1 15  ASN n 
1 16  LEU n 
1 17  TYR n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  LYS n 
1 22  LEU n 
1 23  ASP n 
1 24  PRO n 
1 25  ALA n 
1 26  SER n 
1 27  LYS n 
1 28  SER n 
1 29  ARG n 
1 30  SER n 
1 31  CYS n 
1 32  GLY n 
1 33  GLU n 
1 34  VAL n 
1 35  ARG n 
1 36  GLN n 
1 37  ILE n 
1 38  TYR n 
1 39  GLY n 
1 40  ALA n 
1 41  LYS n 
1 42  GLY n 
1 43  PHE n 
1 44  SER n 
1 45  LEU n 
1 46  SER n 
1 47  ASP n 
1 48  VAL n 
1 49  PRO n 
1 50  GLN n 
1 51  ALA n 
1 52  GLU n 
1 53  ILE n 
1 54  SER n 
1 55  GLY n 
1 56  GLU n 
1 57  HIS n 
1 58  LEU n 
1 59  ARG n 
1 60  ILE n 
1 61  CYS n 
1 62  PRO n 
1 63  GLN n 
1 64  GLY n 
1 65  TYR n 
1 66  THR n 
1 67  CYS n 
1 68  CYS n 
1 69  THR n 
1 70  SER n 
1 71  GLU n 
1 72  MET n 
1 73  GLU n 
1 74  GLU n 
1 75  ASN n 
1 76  LEU n 
1 77  ALA n 
1 78  ASN n 
1 79  ARG n 
1 80  SER n 
1 81  HIS n 
1 82  ALA n 
1 83  GLU n 
1 84  LEU n 
1 85  GLU n 
1 86  THR n 
1 87  ALA n 
1 88  LEU n 
1 89  ARG n 
1 90  ASP n 
1 91  SER n 
1 92  SER n 
1 93  ARG n 
1 94  VAL n 
1 95  LEU n 
1 96  GLN n 
1 97  ALA n 
1 98  MET n 
1 99  LEU n 
1 100 ALA n 
1 101 THR n 
1 102 GLN n 
1 103 LEU n 
1 104 ARG n 
1 105 SER n 
1 106 PHE n 
1 107 ASP n 
1 108 ASP n 
1 109 HIS n 
1 110 PHE n 
1 111 GLN n 
1 112 HIS n 
1 113 LEU n 
1 114 LEU n 
1 115 ASN n 
1 116 ASP n 
1 117 SER n 
1 118 GLU n 
1 119 ARG n 
1 120 THR n 
1 121 LEU n 
1 122 GLN n 
1 123 ALA n 
1 124 THR n 
1 125 PHE n 
1 126 PRO n 
1 127 GLY n 
1 128 ALA n 
1 129 PHE n 
1 130 GLY n 
1 131 GLU n 
1 132 LEU n 
1 133 TYR n 
1 134 THR n 
1 135 GLN n 
1 136 ASN n 
1 137 ALA n 
1 138 ARG n 
1 139 ALA n 
1 140 PHE n 
1 141 ARG n 
1 142 ASP n 
1 143 LEU n 
1 144 TYR n 
1 145 SER n 
1 146 GLU n 
1 147 LEU n 
1 148 ARG n 
1 149 LEU n 
1 150 TYR n 
1 151 TYR n 
1 152 ARG n 
1 153 GLY n 
1 154 ALA n 
1 155 ASN n 
1 156 LEU n 
1 157 HIS n 
1 158 LEU n 
1 159 GLU n 
1 160 GLU n 
1 161 THR n 
1 162 LEU n 
1 163 ALA n 
1 164 GLU n 
1 165 PHE n 
1 166 TRP n 
1 167 ALA n 
1 168 ARG n 
1 169 LEU n 
1 170 LEU n 
1 171 GLU n 
1 172 ARG n 
1 173 LEU n 
1 174 PHE n 
1 175 LYS n 
1 176 GLN n 
1 177 LEU n 
1 178 HIS n 
1 179 PRO n 
1 180 GLN n 
1 181 LEU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 ASP n 
1 186 ASP n 
1 187 TYR n 
1 188 LEU n 
1 189 ASP n 
1 190 CYS n 
1 191 LEU n 
1 192 GLY n 
1 193 LYS n 
1 194 GLN n 
1 195 ALA n 
1 196 GLU n 
1 197 ALA n 
1 198 LEU n 
1 199 ARG n 
1 200 PRO n 
1 201 PHE n 
1 202 GLY n 
1 203 GLU n 
1 204 ALA n 
1 205 PRO n 
1 206 ARG n 
1 207 GLU n 
1 208 LEU n 
1 209 ARG n 
1 210 LEU n 
1 211 ARG n 
1 212 ALA n 
1 213 THR n 
1 214 ARG n 
1 215 ALA n 
1 216 PHE n 
1 217 VAL n 
1 218 ALA n 
1 219 ALA n 
1 220 ARG n 
1 221 SER n 
1 222 PHE n 
1 223 VAL n 
1 224 GLN n 
1 225 GLY n 
1 226 LEU n 
1 227 GLY n 
1 228 VAL n 
1 229 ALA n 
1 230 SER n 
1 231 ASP n 
1 232 VAL n 
1 233 VAL n 
1 234 ARG n 
1 235 LYS n 
1 236 VAL n 
1 237 ALA n 
1 238 GLN n 
1 239 VAL n 
1 240 PRO n 
1 241 LEU n 
1 242 GLY n 
1 243 PRO n 
1 244 GLU n 
1 245 CYS n 
1 246 SER n 
1 247 ARG n 
1 248 ALA n 
1 249 VAL n 
1 250 MET n 
1 251 LYS n 
1 252 LEU n 
1 253 VAL n 
1 254 TYR n 
1 255 CYS n 
1 256 ALA n 
1 257 HIS n 
1 258 CYS n 
1 259 LEU n 
1 260 GLY n 
1 261 VAL n 
1 262 PRO n 
1 263 GLY n 
1 264 ALA n 
1 265 ARG n 
1 266 PRO n 
1 267 CYS n 
1 268 PRO n 
1 269 ASP n 
1 270 TYR n 
1 271 CYS n 
1 272 ARG n 
1 273 ASN n 
1 274 VAL n 
1 275 LEU n 
1 276 LYS n 
1 277 GLY n 
1 278 CYS n 
1 279 LEU n 
1 280 ALA n 
1 281 ASN n 
1 282 GLN n 
1 283 ALA n 
1 284 ASP n 
1 285 LEU n 
1 286 ASP n 
1 287 ALA n 
1 288 GLU n 
1 289 TRP n 
1 290 ARG n 
1 291 ASN n 
1 292 LEU n 
1 293 LEU n 
1 294 ASP n 
1 295 SER n 
1 296 MET n 
1 297 VAL n 
1 298 LEU n 
1 299 ILE n 
1 300 THR n 
1 301 ASP n 
1 302 LYS n 
1 303 PHE n 
1 304 TRP n 
1 305 GLY n 
1 306 THR n 
1 307 SER n 
1 308 GLY n 
1 309 VAL n 
1 310 GLU n 
1 311 SER n 
1 312 VAL n 
1 313 ILE n 
1 314 GLY n 
1 315 SER n 
1 316 VAL n 
1 317 HIS n 
1 318 THR n 
1 319 TRP n 
1 320 LEU n 
1 321 ALA n 
1 322 GLU n 
1 323 ALA n 
1 324 ILE n 
1 325 ASN n 
1 326 ALA n 
1 327 LEU n 
1 328 GLN n 
1 329 ASP n 
1 330 ASN n 
1 331 ARG n 
1 332 ASP n 
1 333 THR n 
1 334 LEU n 
1 335 THR n 
1 336 ALA n 
1 337 LYS n 
1 338 VAL n 
1 339 ILE n 
1 340 GLN n 
1 341 GLY n 
1 342 CYS n 
1 343 GLY n 
1 344 ASN n 
1 345 PRO n 
1 346 LYS n 
1 347 VAL n 
1 348 ASN n 
1 349 PRO n 
1 350 GLN n 
1 351 GLY n 
1 352 PRO n 
1 353 GLY n 
1 354 PRO n 
1 355 GLU n 
1 356 GLU n 
1 357 LYS n 
1 358 ARG n 
1 359 ARG n 
1 360 ARG n 
1 361 GLY n 
1 362 LYS n 
1 363 LEU n 
1 364 ALA n 
1 365 PRO n 
1 366 ARG n 
1 367 GLU n 
1 368 ARG n 
1 369 PRO n 
1 370 PRO n 
1 371 SER n 
1 372 GLY n 
1 373 THR n 
1 374 LEU n 
1 375 GLU n 
1 376 LYS n 
1 377 LEU n 
1 378 VAL n 
1 379 SER n 
1 380 GLU n 
1 381 ALA n 
1 382 LYS n 
1 383 ALA n 
1 384 GLN n 
1 385 LEU n 
1 386 ARG n 
1 387 ASP n 
1 388 VAL n 
1 389 GLN n 
1 390 ASP n 
1 391 PHE n 
1 392 TRP n 
1 393 ILE n 
1 394 SER n 
1 395 LEU n 
1 396 PRO n 
1 397 GLY n 
1 398 THR n 
1 399 LEU n 
1 400 CYS n 
1 401 SER n 
1 402 GLU n 
1 403 LYS n 
1 404 MET n 
1 405 ALA n 
1 406 LEU n 
1 407 SER n 
1 408 THR n 
1 409 ALA n 
1 410 SER n 
1 411 ASP n 
1 412 ASP n 
1 413 ARG n 
1 414 CYS n 
1 415 TRP n 
1 416 ASN n 
1 417 GLY n 
1 418 MET n 
1 419 ALA n 
1 420 ARG n 
1 421 GLY n 
1 422 ARG n 
1 423 TYR n 
1 424 LEU n 
1 425 PRO n 
1 426 GLU n 
1 427 VAL n 
1 428 MET n 
1 429 GLY n 
1 430 ASP n 
1 431 GLY n 
1 432 LEU n 
1 433 ALA n 
1 434 ASN n 
1 435 GLN n 
1 436 ILE n 
1 437 ASN n 
1 438 ASN n 
1 439 PRO n 
1 440 GLU n 
1 441 VAL n 
1 442 GLU n 
1 443 VAL n 
1 444 ASP n 
1 445 ILE n 
1 446 THR n 
1 447 LYS n 
1 448 PRO n 
1 449 ASP n 
1 450 MET n 
1 451 THR n 
1 452 ILE n 
1 453 ARG n 
1 454 GLN n 
1 455 GLN n 
1 456 ILE n 
1 457 MET n 
1 458 GLN n 
1 459 LEU n 
1 460 LYS n 
1 461 ILE n 
1 462 MET n 
1 463 THR n 
1 464 ASN n 
1 465 ARG n 
1 466 LEU n 
1 467 ARG n 
1 468 SER n 
1 469 ALA n 
1 470 TYR n 
1 471 ASN n 
1 472 GLY n 
1 473 ASN n 
1 474 ASP n 
1 475 VAL n 
1 476 ASP n 
1 477 PHE n 
1 478 GLN n 
1 479 ASP n 
1 480 ALA n 
1 481 SER n 
1 482 ASP n 
1 483 ASP n 
1 484 GLY n 
1 485 ALA n 
1 486 GLY n 
1 487 ALA n 
1 488 GLY n 
1 489 ALA n 
1 490 GLY n 
1 491 ASP n 
1 492 GLY n 
1 493 CYS n 
1 494 LEU n 
1 495 ASP n 
1 496 ASP n 
1 497 LEU n 
1 498 CYS n 
1 499 SER n 
1 500 ARG n 
1 501 LYS n 
1 502 VAL n 
1 503 SER n 
1 504 ARG n 
1 505 LYS n 
1 506 SER n 
1 507 SER n 
1 508 SER n 
1 509 SER n 
1 510 ARG n 
1 511 THR n 
1 512 PRO n 
1 513 LEU n 
1 514 THR n 
1 515 HIS n 
1 516 ALA n 
1 517 LEU n 
1 518 PRO n 
1 519 GLY n 
1 520 LEU n 
1 521 SER n 
1 522 GLU n 
1 523 GLN n 
1 524 GLU n 
1 525 GLY n 
1 526 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   526 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GPC1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               Human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            HEK-293 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GPC1_HUMAN 
_struct_ref.pdbx_db_accession          P35052 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSHAELETALRDSSRVLQAMLATQ
LRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLL
LPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVP
GARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGC
GNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGR
YLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKV
SRKSSSSRTPLTHALPGLSEQEGQ
;
_struct_ref.pdbx_align_begin           24 
# 
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 4YWT A 23 ? 526 ? P35052 24 ? 527 ? 24 527 
2 1 4YWT B 23 ? 526 ? P35052 24 ? 527 ? 24 527 
3 1 4YWT C 23 ? 526 ? P35052 24 ? 527 ? 24 527 
4 1 4YWT D 23 ? 526 ? P35052 24 ? 527 ? 24 527 
# 
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 4YWT ALA A 1   ? UNP P35052 ?   ?   'expression tag'      2   1   
1 4YWT PRO A 2   ? UNP P35052 ?   ?   'expression tag'      3   2   
1 4YWT GLN A 3   ? UNP P35052 ?   ?   'expression tag'      4   3   
1 4YWT LEU A 4   ? UNP P35052 ?   ?   'expression tag'      5   4   
1 4YWT HIS A 5   ? UNP P35052 ?   ?   'expression tag'      6   5   
1 4YWT HIS A 6   ? UNP P35052 ?   ?   'expression tag'      7   6   
1 4YWT HIS A 7   ? UNP P35052 ?   ?   'expression tag'      8   7   
1 4YWT HIS A 8   ? UNP P35052 ?   ?   'expression tag'      9   8   
1 4YWT HIS A 9   ? UNP P35052 ?   ?   'expression tag'      10  9   
1 4YWT HIS A 10  ? UNP P35052 ?   ?   'expression tag'      11  10  
1 4YWT ASP A 11  ? UNP P35052 ?   ?   'expression tag'      12  11  
1 4YWT LEU A 12  ? UNP P35052 ?   ?   'expression tag'      13  12  
1 4YWT TYR A 13  ? UNP P35052 ?   ?   'expression tag'      14  13  
1 4YWT GLU A 14  ? UNP P35052 ?   ?   'expression tag'      15  14  
1 4YWT ASN A 15  ? UNP P35052 ?   ?   'expression tag'      16  15  
1 4YWT LEU A 16  ? UNP P35052 ?   ?   'expression tag'      17  16  
1 4YWT TYR A 17  ? UNP P35052 ?   ?   'expression tag'      18  17  
1 4YWT PHE A 18  ? UNP P35052 ?   ?   'expression tag'      19  18  
1 4YWT GLN A 19  ? UNP P35052 ?   ?   'expression tag'      20  19  
1 4YWT GLY A 20  ? UNP P35052 ?   ?   'expression tag'      21  20  
1 4YWT LYS A 21  ? UNP P35052 ?   ?   'expression tag'      22  21  
1 4YWT LEU A 22  ? UNP P35052 ?   ?   'expression tag'      23  22  
1 4YWT ALA A 485 ? UNP P35052 SER 486 'engineered mutation' 486 23  
1 4YWT ALA A 487 ? UNP P35052 SER 488 'engineered mutation' 488 24  
1 4YWT ALA A 489 ? UNP P35052 SER 490 'engineered mutation' 490 25  
2 4YWT ALA B 1   ? UNP P35052 ?   ?   'expression tag'      2   26  
2 4YWT PRO B 2   ? UNP P35052 ?   ?   'expression tag'      3   27  
2 4YWT GLN B 3   ? UNP P35052 ?   ?   'expression tag'      4   28  
2 4YWT LEU B 4   ? UNP P35052 ?   ?   'expression tag'      5   29  
2 4YWT HIS B 5   ? UNP P35052 ?   ?   'expression tag'      6   30  
2 4YWT HIS B 6   ? UNP P35052 ?   ?   'expression tag'      7   31  
2 4YWT HIS B 7   ? UNP P35052 ?   ?   'expression tag'      8   32  
2 4YWT HIS B 8   ? UNP P35052 ?   ?   'expression tag'      9   33  
2 4YWT HIS B 9   ? UNP P35052 ?   ?   'expression tag'      10  34  
2 4YWT HIS B 10  ? UNP P35052 ?   ?   'expression tag'      11  35  
2 4YWT ASP B 11  ? UNP P35052 ?   ?   'expression tag'      12  36  
2 4YWT LEU B 12  ? UNP P35052 ?   ?   'expression tag'      13  37  
2 4YWT TYR B 13  ? UNP P35052 ?   ?   'expression tag'      14  38  
2 4YWT GLU B 14  ? UNP P35052 ?   ?   'expression tag'      15  39  
2 4YWT ASN B 15  ? UNP P35052 ?   ?   'expression tag'      16  40  
2 4YWT LEU B 16  ? UNP P35052 ?   ?   'expression tag'      17  41  
2 4YWT TYR B 17  ? UNP P35052 ?   ?   'expression tag'      18  42  
2 4YWT PHE B 18  ? UNP P35052 ?   ?   'expression tag'      19  43  
2 4YWT GLN B 19  ? UNP P35052 ?   ?   'expression tag'      20  44  
2 4YWT GLY B 20  ? UNP P35052 ?   ?   'expression tag'      21  45  
2 4YWT LYS B 21  ? UNP P35052 ?   ?   'expression tag'      22  46  
2 4YWT LEU B 22  ? UNP P35052 ?   ?   'expression tag'      23  47  
2 4YWT ALA B 485 ? UNP P35052 SER 486 'engineered mutation' 486 48  
2 4YWT ALA B 487 ? UNP P35052 SER 488 'engineered mutation' 488 49  
2 4YWT ALA B 489 ? UNP P35052 SER 490 'engineered mutation' 490 50  
3 4YWT ALA C 1   ? UNP P35052 ?   ?   'expression tag'      2   51  
3 4YWT PRO C 2   ? UNP P35052 ?   ?   'expression tag'      3   52  
3 4YWT GLN C 3   ? UNP P35052 ?   ?   'expression tag'      4   53  
3 4YWT LEU C 4   ? UNP P35052 ?   ?   'expression tag'      5   54  
3 4YWT HIS C 5   ? UNP P35052 ?   ?   'expression tag'      6   55  
3 4YWT HIS C 6   ? UNP P35052 ?   ?   'expression tag'      7   56  
3 4YWT HIS C 7   ? UNP P35052 ?   ?   'expression tag'      8   57  
3 4YWT HIS C 8   ? UNP P35052 ?   ?   'expression tag'      9   58  
3 4YWT HIS C 9   ? UNP P35052 ?   ?   'expression tag'      10  59  
3 4YWT HIS C 10  ? UNP P35052 ?   ?   'expression tag'      11  60  
3 4YWT ASP C 11  ? UNP P35052 ?   ?   'expression tag'      12  61  
3 4YWT LEU C 12  ? UNP P35052 ?   ?   'expression tag'      13  62  
3 4YWT TYR C 13  ? UNP P35052 ?   ?   'expression tag'      14  63  
3 4YWT GLU C 14  ? UNP P35052 ?   ?   'expression tag'      15  64  
3 4YWT ASN C 15  ? UNP P35052 ?   ?   'expression tag'      16  65  
3 4YWT LEU C 16  ? UNP P35052 ?   ?   'expression tag'      17  66  
3 4YWT TYR C 17  ? UNP P35052 ?   ?   'expression tag'      18  67  
3 4YWT PHE C 18  ? UNP P35052 ?   ?   'expression tag'      19  68  
3 4YWT GLN C 19  ? UNP P35052 ?   ?   'expression tag'      20  69  
3 4YWT GLY C 20  ? UNP P35052 ?   ?   'expression tag'      21  70  
3 4YWT LYS C 21  ? UNP P35052 ?   ?   'expression tag'      22  71  
3 4YWT LEU C 22  ? UNP P35052 ?   ?   'expression tag'      23  72  
3 4YWT ALA C 485 ? UNP P35052 SER 486 'engineered mutation' 486 73  
3 4YWT ALA C 487 ? UNP P35052 SER 488 'engineered mutation' 488 74  
3 4YWT ALA C 489 ? UNP P35052 SER 490 'engineered mutation' 490 75  
4 4YWT ALA D 1   ? UNP P35052 ?   ?   'expression tag'      2   76  
4 4YWT PRO D 2   ? UNP P35052 ?   ?   'expression tag'      3   77  
4 4YWT GLN D 3   ? UNP P35052 ?   ?   'expression tag'      4   78  
4 4YWT LEU D 4   ? UNP P35052 ?   ?   'expression tag'      5   79  
4 4YWT HIS D 5   ? UNP P35052 ?   ?   'expression tag'      6   80  
4 4YWT HIS D 6   ? UNP P35052 ?   ?   'expression tag'      7   81  
4 4YWT HIS D 7   ? UNP P35052 ?   ?   'expression tag'      8   82  
4 4YWT HIS D 8   ? UNP P35052 ?   ?   'expression tag'      9   83  
4 4YWT HIS D 9   ? UNP P35052 ?   ?   'expression tag'      10  84  
4 4YWT HIS D 10  ? UNP P35052 ?   ?   'expression tag'      11  85  
4 4YWT ASP D 11  ? UNP P35052 ?   ?   'expression tag'      12  86  
4 4YWT LEU D 12  ? UNP P35052 ?   ?   'expression tag'      13  87  
4 4YWT TYR D 13  ? UNP P35052 ?   ?   'expression tag'      14  88  
4 4YWT GLU D 14  ? UNP P35052 ?   ?   'expression tag'      15  89  
4 4YWT ASN D 15  ? UNP P35052 ?   ?   'expression tag'      16  90  
4 4YWT LEU D 16  ? UNP P35052 ?   ?   'expression tag'      17  91  
4 4YWT TYR D 17  ? UNP P35052 ?   ?   'expression tag'      18  92  
4 4YWT PHE D 18  ? UNP P35052 ?   ?   'expression tag'      19  93  
4 4YWT GLN D 19  ? UNP P35052 ?   ?   'expression tag'      20  94  
4 4YWT GLY D 20  ? UNP P35052 ?   ?   'expression tag'      21  95  
4 4YWT LYS D 21  ? UNP P35052 ?   ?   'expression tag'      22  96  
4 4YWT LEU D 22  ? UNP P35052 ?   ?   'expression tag'      23  97  
4 4YWT ALA D 485 ? UNP P35052 SER 486 'engineered mutation' 486 98  
4 4YWT ALA D 487 ? UNP P35052 SER 488 'engineered mutation' 488 99  
4 4YWT ALA D 489 ? UNP P35052 SER 490 'engineered mutation' 490 100 
# 
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 
CA  non-polymer         . 'CALCIUM ION'          ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
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 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? '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.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   4YWT 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.29 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         46.31 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 6000, Tris-HCl and CaCl2' 
_exptl_crystal_grow.pdbx_pH_range   8 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-05-08 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'double crystal, Si[111]' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'MAX II BEAMLINE I911-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
# 
_reflns.B_iso_Wilson_estimate            38.7 
_reflns.entry_id                         4YWT 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.38 
_reflns.d_resolution_low                 43.22 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       82475 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             97.9 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.6 
_reflns.pdbx_Rmerge_I_obs                0.1076 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            7.44 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.38 
_reflns_shell.d_res_low                   2.47 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.62 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        97.11 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.69 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.7 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4YWT 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     82387 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             43.223 
_refine.ls_d_res_high                            2.380 
_refine.ls_percent_reflns_obs                    97.80 
_refine.ls_R_factor_obs                          0.2398 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2390 
_refine.ls_R_factor_R_free                       0.2728 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.40 
_refine.ls_number_reflns_R_free                  1981 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      4bwe 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.34 
_refine.pdbx_overall_phase_error                 32.91 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        12704 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.number_atoms_solvent             284 
_refine_hist.number_atoms_total               13053 
_refine_hist.d_res_high                       2.380 
_refine_hist.d_res_low                        43.223 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.004  ? ? 13139 'X-RAY DIFFRACTION' ? 
f_angle_d          0.856  ? ? 17763 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 14.965 ? ? 4775  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.046  ? ? 2019  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 2335  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.3800 2.4395  5731 0.3383 98.00  0.3243 . . 136 . . . . 
'X-RAY DIFFRACTION' . 2.4395 2.5055  5730 0.3279 98.00  0.3494 . . 146 . . . . 
'X-RAY DIFFRACTION' . 2.5055 2.5792  5752 0.3086 98.00  0.2948 . . 135 . . . . 
'X-RAY DIFFRACTION' . 2.5792 2.6624  5707 0.3043 98.00  0.3899 . . 140 . . . . 
'X-RAY DIFFRACTION' . 2.6624 2.7576  5736 0.2962 97.00  0.3237 . . 141 . . . . 
'X-RAY DIFFRACTION' . 2.7576 2.8680  5786 0.2915 100.00 0.3142 . . 143 . . . . 
'X-RAY DIFFRACTION' . 2.8680 2.9985  5703 0.2754 98.00  0.3193 . . 142 . . . . 
'X-RAY DIFFRACTION' . 2.9985 3.1565  5809 0.2701 98.00  0.3233 . . 142 . . . . 
'X-RAY DIFFRACTION' . 3.1565 3.3542  5771 0.2574 98.00  0.2900 . . 140 . . . . 
'X-RAY DIFFRACTION' . 3.3542 3.6130  5729 0.2374 98.00  0.2847 . . 147 . . . . 
'X-RAY DIFFRACTION' . 3.6130 3.9764  5680 0.2103 97.00  0.2502 . . 135 . . . . 
'X-RAY DIFFRACTION' . 3.9764 4.5513  5792 0.1922 98.00  0.2511 . . 143 . . . . 
'X-RAY DIFFRACTION' . 4.5513 5.7320  5801 0.2023 98.00  0.2162 . . 145 . . . . 
'X-RAY DIFFRACTION' . 5.7320 43.2302 5679 0.1960 95.00  0.2202 . . 146 . . . . 
# 
_struct.entry_id                     4YWT 
_struct.title                        
'Crystal structure of full-length glypican-1 core protein after controlled crystal dehydration to 87% relative humidity' 
_struct.pdbx_descriptor              'Glypican-1 core protein' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4YWT 
_struct_keywords.text            'glypican-1, diffraction quality, controlled dehydration, HC1b, membrane protein' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
S N N 4 ? 
T N N 4 ? 
U N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 CYS A 31  ? ALA A 40  ? CYS A 32  ALA A 41  1 ? 10 
HELX_P HELX_P2  AA2 SER A 44  ? VAL A 48  ? SER A 45  VAL A 49  5 ? 5  
HELX_P HELX_P3  AA3 THR A 69  ? GLY A 130 ? THR A 70  GLY A 131 1 ? 62 
HELX_P HELX_P4  AA4 GLY A 130 ? GLN A 135 ? GLY A 131 GLN A 136 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 136 ? GLY A 153 ? ASN A 137 GLY A 154 1 ? 18 
HELX_P HELX_P6  AA6 HIS A 157 ? HIS A 178 ? HIS A 158 HIS A 179 1 ? 22 
HELX_P HELX_P7  AA7 GLU A 203 ? ALA A 237 ? GLU A 204 ALA A 238 1 ? 35 
HELX_P HELX_P8  AA8 GLY A 242 ? TYR A 254 ? GLY A 243 TYR A 255 1 ? 13 
HELX_P HELX_P9  AA9 TYR A 254 ? LEU A 259 ? TYR A 255 LEU A 260 1 ? 6  
HELX_P HELX_P10 AB1 CYS A 267 ? LEU A 279 ? CYS A 268 LEU A 280 1 ? 13 
HELX_P HELX_P11 AB2 LEU A 279 ? ASP A 284 ? LEU A 280 ASP A 285 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 285 ? THR A 300 ? LEU A 286 THR A 301 1 ? 16 
HELX_P HELX_P13 AB4 ASP A 301 ? TRP A 304 ? ASP A 302 TRP A 305 5 ? 4  
HELX_P HELX_P14 AB5 SER A 311 ? GLY A 314 ? SER A 312 GLY A 315 5 ? 4  
HELX_P HELX_P15 AB6 SER A 315 ? ASP A 329 ? SER A 316 ASP A 330 1 ? 15 
HELX_P HELX_P16 AB7 ASN A 330 ? THR A 335 ? ASN A 331 THR A 336 1 ? 6  
HELX_P HELX_P17 AB8 GLY A 372 ? VAL A 388 ? GLY A 373 VAL A 389 1 ? 17 
HELX_P HELX_P18 AB9 ASP A 390 ? LYS A 403 ? ASP A 391 LYS A 404 1 ? 14 
HELX_P HELX_P19 AC1 LEU A 432 ? ILE A 436 ? LEU A 433 ILE A 437 5 ? 5  
HELX_P HELX_P20 AC2 ASP A 449 ? GLY A 472 ? ASP A 450 GLY A 473 1 ? 24 
HELX_P HELX_P21 AC3 CYS B 31  ? LYS B 41  ? CYS B 32  LYS B 42  1 ? 11 
HELX_P HELX_P22 AC4 SER B 44  ? VAL B 48  ? SER B 45  VAL B 49  5 ? 5  
HELX_P HELX_P23 AC5 THR B 69  ? PHE B 125 ? THR B 70  PHE B 126 1 ? 57 
HELX_P HELX_P24 AC6 PHE B 125 ? GLY B 130 ? PHE B 126 GLY B 131 1 ? 6  
HELX_P HELX_P25 AC7 GLY B 130 ? GLN B 135 ? GLY B 131 GLN B 136 1 ? 6  
HELX_P HELX_P26 AC8 ASN B 136 ? ARG B 152 ? ASN B 137 ARG B 153 1 ? 17 
HELX_P HELX_P27 AC9 HIS B 157 ? LEU B 177 ? HIS B 158 LEU B 178 1 ? 21 
HELX_P HELX_P28 AD1 PRO B 184 ? GLN B 194 ? PRO B 185 GLN B 195 1 ? 11 
HELX_P HELX_P29 AD2 GLU B 203 ? ALA B 237 ? GLU B 204 ALA B 238 1 ? 35 
HELX_P HELX_P30 AD3 GLY B 242 ? TYR B 254 ? GLY B 243 TYR B 255 1 ? 13 
HELX_P HELX_P31 AD4 TYR B 254 ? LEU B 259 ? TYR B 255 LEU B 260 1 ? 6  
HELX_P HELX_P32 AD5 CYS B 267 ? LEU B 279 ? CYS B 268 LEU B 280 1 ? 13 
HELX_P HELX_P33 AD6 LEU B 279 ? ASP B 284 ? LEU B 280 ASP B 285 1 ? 6  
HELX_P HELX_P34 AD7 LEU B 285 ? THR B 300 ? LEU B 286 THR B 301 1 ? 16 
HELX_P HELX_P35 AD8 ASP B 301 ? TRP B 304 ? ASP B 302 TRP B 305 5 ? 4  
HELX_P HELX_P36 AD9 GLY B 308 ? SER B 315 ? GLY B 309 SER B 316 1 ? 8  
HELX_P HELX_P37 AE1 SER B 315 ? ASN B 330 ? SER B 316 ASN B 331 1 ? 16 
HELX_P HELX_P38 AE2 ASN B 330 ? GLY B 343 ? ASN B 331 GLY B 344 1 ? 14 
HELX_P HELX_P39 AE3 GLY B 372 ? VAL B 388 ? GLY B 373 VAL B 389 1 ? 17 
HELX_P HELX_P40 AE4 ASP B 390 ? LYS B 403 ? ASP B 391 LYS B 404 1 ? 14 
HELX_P HELX_P41 AE5 LEU B 432 ? ILE B 436 ? LEU B 433 ILE B 437 5 ? 5  
HELX_P HELX_P42 AE6 ASP B 449 ? GLY B 472 ? ASP B 450 GLY B 473 1 ? 24 
HELX_P HELX_P43 AE7 CYS C 31  ? LYS C 41  ? CYS C 32  LYS C 42  1 ? 11 
HELX_P HELX_P44 AE8 SER C 44  ? VAL C 48  ? SER C 45  VAL C 49  5 ? 5  
HELX_P HELX_P45 AE9 THR C 69  ? GLY C 130 ? THR C 70  GLY C 131 1 ? 62 
HELX_P HELX_P46 AF1 GLY C 130 ? GLN C 135 ? GLY C 131 GLN C 136 1 ? 6  
HELX_P HELX_P47 AF2 ASN C 136 ? ARG C 152 ? ASN C 137 ARG C 153 1 ? 17 
HELX_P HELX_P48 AF3 HIS C 157 ? HIS C 178 ? HIS C 158 HIS C 179 1 ? 22 
HELX_P HELX_P49 AF4 GLU C 203 ? GLN C 238 ? GLU C 204 GLN C 239 1 ? 36 
HELX_P HELX_P50 AF5 GLY C 242 ? TYR C 254 ? GLY C 243 TYR C 255 1 ? 13 
HELX_P HELX_P51 AF6 TYR C 254 ? LEU C 259 ? TYR C 255 LEU C 260 1 ? 6  
HELX_P HELX_P52 AF7 CYS C 267 ? LEU C 279 ? CYS C 268 LEU C 280 1 ? 13 
HELX_P HELX_P53 AF8 LEU C 279 ? ASP C 284 ? LEU C 280 ASP C 285 1 ? 6  
HELX_P HELX_P54 AF9 LEU C 285 ? THR C 300 ? LEU C 286 THR C 301 1 ? 16 
HELX_P HELX_P55 AG1 ASP C 301 ? TRP C 304 ? ASP C 302 TRP C 305 5 ? 4  
HELX_P HELX_P56 AG2 SER C 311 ? GLY C 314 ? SER C 312 GLY C 315 5 ? 4  
HELX_P HELX_P57 AG3 SER C 315 ? ASN C 330 ? SER C 316 ASN C 331 1 ? 16 
HELX_P HELX_P58 AG4 ASN C 330 ? ALA C 336 ? ASN C 331 ALA C 337 1 ? 7  
HELX_P HELX_P59 AG5 GLY C 372 ? VAL C 388 ? GLY C 373 VAL C 389 1 ? 17 
HELX_P HELX_P60 AG6 ASP C 390 ? LYS C 403 ? ASP C 391 LYS C 404 1 ? 14 
HELX_P HELX_P61 AG7 LEU C 432 ? ILE C 436 ? LEU C 433 ILE C 437 5 ? 5  
HELX_P HELX_P62 AG8 ASP C 449 ? GLY C 472 ? ASP C 450 GLY C 473 1 ? 24 
HELX_P HELX_P63 AG9 CYS D 31  ? LYS D 41  ? CYS D 32  LYS D 42  1 ? 11 
HELX_P HELX_P64 AH1 THR D 69  ? PHE D 129 ? THR D 70  PHE D 130 1 ? 61 
HELX_P HELX_P65 AH2 GLY D 130 ? GLN D 135 ? GLY D 131 GLN D 136 1 ? 6  
HELX_P HELX_P66 AH3 ASN D 136 ? ARG D 152 ? ASN D 137 ARG D 153 1 ? 17 
HELX_P HELX_P67 AH4 HIS D 157 ? HIS D 178 ? HIS D 158 HIS D 179 1 ? 22 
HELX_P HELX_P68 AH5 PRO D 184 ? ARG D 199 ? PRO D 185 ARG D 200 1 ? 16 
HELX_P HELX_P69 AH6 GLU D 203 ? ALA D 237 ? GLU D 204 ALA D 238 1 ? 35 
HELX_P HELX_P70 AH7 GLY D 242 ? TYR D 254 ? GLY D 243 TYR D 255 1 ? 13 
HELX_P HELX_P71 AH8 TYR D 254 ? LEU D 259 ? TYR D 255 LEU D 260 1 ? 6  
HELX_P HELX_P72 AH9 CYS D 267 ? LEU D 279 ? CYS D 268 LEU D 280 1 ? 13 
HELX_P HELX_P73 AI1 LEU D 279 ? ASP D 284 ? LEU D 280 ASP D 285 1 ? 6  
HELX_P HELX_P74 AI2 LEU D 285 ? THR D 300 ? LEU D 286 THR D 301 1 ? 16 
HELX_P HELX_P75 AI3 ASP D 301 ? TRP D 304 ? ASP D 302 TRP D 305 5 ? 4  
HELX_P HELX_P76 AI4 GLY D 308 ? GLY D 314 ? GLY D 309 GLY D 315 1 ? 7  
HELX_P HELX_P77 AI5 SER D 315 ? GLY D 343 ? SER D 316 GLY D 344 1 ? 29 
HELX_P HELX_P78 AI6 GLY D 372 ? VAL D 388 ? GLY D 373 VAL D 389 1 ? 17 
HELX_P HELX_P79 AI7 SER D 394 ? LYS D 403 ? SER D 395 LYS D 404 1 ? 10 
HELX_P HELX_P80 AI8 LEU D 432 ? ILE D 436 ? LEU D 433 ILE D 437 5 ? 5  
HELX_P HELX_P81 AI9 ASP D 449 ? GLY D 472 ? ASP D 450 GLY D 473 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 31  SG  ? ? ? 1_555 A CYS 67  SG ? ? A CYS 32  A CYS 68  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf2  disulf ?   ? A CYS 61  SG  ? ? ? 1_555 A CYS 255 SG ? ? A CYS 62  A CYS 256 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf3  disulf ?   ? A CYS 68  SG  ? ? ? 1_555 A CYS 258 SG ? ? A CYS 69  A CYS 259 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf4  disulf ?   ? A CYS 245 SG  ? ? ? 1_555 A CYS 278 SG ? ? A CYS 246 A CYS 279 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf5  disulf ?   ? A CYS 267 SG  A ? ? 1_555 A CYS 414 SG ? ? A CYS 268 A CYS 415 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf6  disulf ?   ? A CYS 271 SG  ? ? ? 1_555 A CYS 400 SG ? ? A CYS 272 A CYS 401 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf7  disulf ?   ? B CYS 31  SG  ? ? ? 1_555 B CYS 67  SG ? ? B CYS 32  B CYS 68  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf8  disulf ?   ? B CYS 61  SG  ? ? ? 1_555 B CYS 255 SG ? ? B CYS 62  B CYS 256 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf9  disulf ?   ? B CYS 68  SG  ? ? ? 1_555 B CYS 258 SG ? ? B CYS 69  B CYS 259 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf10 disulf ?   ? B CYS 190 SG  ? ? ? 1_555 B CYS 342 SG ? ? B CYS 191 B CYS 343 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf11 disulf ?   ? B CYS 245 SG  ? ? ? 1_555 B CYS 278 SG ? ? B CYS 246 B CYS 279 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf12 disulf ?   ? B CYS 267 SG  A ? ? 1_555 B CYS 414 SG ? ? B CYS 268 B CYS 415 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf13 disulf ?   ? B CYS 271 SG  ? ? ? 1_555 B CYS 400 SG ? ? B CYS 272 B CYS 401 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf14 disulf ?   ? C CYS 31  SG  ? ? ? 1_555 C CYS 67  SG ? ? C CYS 32  C CYS 68  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf15 disulf ?   ? C CYS 61  SG  ? ? ? 1_555 C CYS 255 SG ? ? C CYS 62  C CYS 256 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf16 disulf ?   ? C CYS 68  SG  ? ? ? 1_555 C CYS 258 SG ? ? C CYS 69  C CYS 259 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf17 disulf ?   ? C CYS 245 SG  ? ? ? 1_555 C CYS 278 SG ? ? C CYS 246 C CYS 279 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf18 disulf ?   ? C CYS 267 SG  ? ? ? 1_555 C CYS 414 SG ? ? C CYS 268 C CYS 415 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf19 disulf ?   ? C CYS 271 SG  ? ? ? 1_555 C CYS 400 SG ? ? C CYS 272 C CYS 401 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf20 disulf ?   ? D CYS 31  SG  A ? ? 1_555 D CYS 67  SG A ? D CYS 32  D CYS 68  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf21 disulf ?   ? D CYS 61  SG  ? ? ? 1_555 D CYS 255 SG ? ? D CYS 62  D CYS 256 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf22 disulf ?   ? D CYS 68  SG  ? ? ? 1_555 D CYS 258 SG ? ? D CYS 69  D CYS 259 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf23 disulf ?   ? D CYS 190 SG  ? ? ? 1_555 D CYS 342 SG ? ? D CYS 191 D CYS 343 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf24 disulf ?   ? D CYS 245 SG  ? ? ? 1_555 D CYS 278 SG ? ? D CYS 246 D CYS 279 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf25 disulf ?   ? D CYS 267 SG  A ? ? 1_555 D CYS 414 SG ? ? D CYS 268 D CYS 415 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf26 disulf ?   ? D CYS 271 SG  ? ? ? 1_555 D CYS 400 SG ? ? D CYS 272 D CYS 401 1_555 ? ? ? ? ? ? ? 2.032 ? 
covale1  covale one ? A ASN 115 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 116 A NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? 
metalc1  metalc ?   ? A ASP 387 O   ? ? ? 1_555 F CA  .   CA ? ? A ASP 388 A CA  602 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc2  metalc ?   ? A ASP 390 OD1 ? ? ? 1_555 F CA  .   CA ? ? A ASP 391 A CA  602 1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc3  metalc ?   ? A ASP 390 OD2 ? ? ? 1_555 F CA  .   CA ? ? A ASP 391 A CA  602 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc4  metalc ?   ? A ILE 436 O   ? ? ? 1_555 G CA  .   CA ? ? A ILE 437 A CA  603 1_555 ? ? ? ? ? ? ? 2.381 ? 
covale2  covale one ? B ASN 115 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 116 B NAG 601 1_555 ? ? ? ? ? ? ? 1.443 ? 
metalc5  metalc ?   ? B ASP 387 O   ? ? ? 1_555 J CA  .   CA ? ? B ASP 388 B CA  603 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc6  metalc ?   ? B ASP 390 OD1 ? ? ? 1_555 J CA  .   CA ? ? B ASP 391 B CA  603 1_555 ? ? ? ? ? ? ? 2.358 ? 
metalc7  metalc ?   ? B ASP 390 OD2 ? ? ? 1_555 J CA  .   CA ? ? B ASP 391 B CA  603 1_555 ? ? ? ? ? ? ? 2.364 ? 
metalc8  metalc ?   ? B ILE 436 O   ? ? ? 1_555 I CA  .   CA ? ? B ILE 437 B CA  602 1_555 ? ? ? ? ? ? ? 2.381 ? 
metalc9  metalc ?   ? B GLU 442 OE1 ? ? ? 1_555 I CA  .   CA ? ? B GLU 443 B CA  602 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc10 metalc ?   ? B GLU 442 OE2 ? ? ? 1_555 I CA  .   CA ? ? B GLU 443 B CA  602 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc11 metalc ?   ? C ASP 47  OD1 ? ? ? 1_555 L CA  .   CA ? ? C ASP 48  C CA  602 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc12 metalc ?   ? C GLU 71  OE1 ? ? ? 1_555 L CA  .   CA ? ? C GLU 72  C CA  602 1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc13 metalc ?   ? C GLU 71  OE2 ? ? ? 1_555 L CA  .   CA ? ? C GLU 72  C CA  602 1_555 ? ? ? ? ? ? ? 2.364 ? 
covale3  covale one ? C ASN 115 ND2 ? ? ? 1_555 K NAG .   C1 ? ? C ASN 116 C NAG 601 1_555 ? ? ? ? ? ? ? 1.440 ? 
metalc14 metalc ?   ? C ASP 387 O   ? ? ? 1_555 N CA  .   CA ? ? C ASP 388 C CA  604 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc15 metalc ?   ? C ASP 390 OD1 ? ? ? 1_555 N CA  .   CA ? ? C ASP 391 C CA  604 1_555 ? ? ? ? ? ? ? 2.361 ? 
metalc16 metalc ?   ? C ASP 390 OD2 ? ? ? 1_555 N CA  .   CA ? ? C ASP 391 C CA  604 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc17 metalc ?   ? C ILE 436 O   ? ? ? 1_555 M CA  .   CA ? ? C ILE 437 C CA  603 1_555 ? ? ? ? ? ? ? 2.382 ? 
metalc18 metalc ?   ? C GLU 442 OE2 ? ? ? 1_555 M CA  .   CA ? ? C GLU 443 C CA  603 1_555 ? ? ? ? ? ? ? 2.361 ? 
covale4  covale one ? D ASN 115 ND2 ? ? ? 1_555 O NAG .   C1 ? ? D ASN 116 D NAG 601 1_555 ? ? ? ? ? ? ? 1.436 ? 
metalc19 metalc ?   ? D ASP 387 O   ? ? ? 1_555 Q CA  .   CA ? ? D ASP 388 D CA  603 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc20 metalc ?   ? D ASP 390 OD1 ? ? ? 1_555 Q CA  .   CA ? ? D ASP 391 D CA  603 1_555 ? ? ? ? ? ? ? 2.360 ? 
metalc21 metalc ?   ? D ASP 390 OD2 ? ? ? 1_555 Q CA  .   CA ? ? D ASP 391 D CA  603 1_555 ? ? ? ? ? ? ? 2.363 ? 
metalc22 metalc ?   ? D ILE 436 O   ? ? ? 1_555 P CA  .   CA ? ? D ILE 437 D CA  602 1_555 ? ? ? ? ? ? ? 2.385 ? 
metalc23 metalc ?   ? D GLU 442 OE1 ? ? ? 1_555 P CA  .   CA ? ? D GLU 443 D CA  602 1_555 ? ? ? ? ? ? ? 2.364 ? 
metalc24 metalc ?   ? F CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  602 A HOH 741 1_555 ? ? ? ? ? ? ? 2.389 ? 
metalc25 metalc ?   ? F CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  602 A HOH 787 1_555 ? ? ? ? ? ? ? 2.392 ? 
metalc26 metalc ?   ? F CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  602 A HOH 731 1_555 ? ? ? ? ? ? ? 2.392 ? 
metalc27 metalc ?   ? G CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  603 A HOH 766 1_555 ? ? ? ? ? ? ? 2.389 ? 
metalc28 metalc ?   ? G CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  603 A HOH 770 1_555 ? ? ? ? ? ? ? 2.392 ? 
metalc29 metalc ?   ? G CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? A CA  603 A HOH 780 1_555 ? ? ? ? ? ? ? 2.390 ? 
metalc30 metalc ?   ? I CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  602 B HOH 707 1_555 ? ? ? ? ? ? ? 2.393 ? 
metalc31 metalc ?   ? I CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  602 B HOH 716 1_555 ? ? ? ? ? ? ? 2.392 ? 
metalc32 metalc ?   ? J CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  603 B HOH 702 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc33 metalc ?   ? J CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  603 B HOH 731 1_555 ? ? ? ? ? ? ? 2.390 ? 
metalc34 metalc ?   ? J CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  603 B HOH 741 1_555 ? ? ? ? ? ? ? 2.390 ? 
metalc35 metalc ?   ? J CA  .   CA  ? ? ? 1_555 S HOH .   O  ? ? B CA  603 B HOH 776 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc36 metalc ?   ? L CA  .   CA  ? ? ? 1_555 T HOH .   O  ? ? C CA  602 C HOH 703 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc37 metalc ?   ? M CA  .   CA  ? ? ? 1_555 T HOH .   O  ? ? C CA  603 C HOH 720 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc38 metalc ?   ? M CA  .   CA  ? ? ? 1_555 T HOH .   O  ? ? C CA  603 C HOH 724 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc39 metalc ?   ? N CA  .   CA  ? ? ? 1_555 T HOH .   O  ? ? C CA  604 C HOH 717 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc40 metalc ?   ? P CA  .   CA  ? ? ? 1_555 U HOH .   O  ? ? D CA  602 D HOH 712 1_555 ? ? ? ? ? ? ? 2.390 ? 
metalc41 metalc ?   ? Q CA  .   CA  ? ? ? 1_555 U HOH .   O  ? ? D CA  603 D HOH 738 1_555 ? ? ? ? ? ? ? 2.391 ? 
metalc42 metalc ?   ? A GLU 164 OE1 ? ? ? 1_555 L CA  .   CA ? ? A GLU 165 C CA  602 2_656 ? ? ? ? ? ? ? 2.363 ? 
metalc43 metalc ?   ? L CA  .   CA  ? ? ? 1_555 R HOH .   O  ? ? C CA  602 A HOH 782 2_646 ? ? ? ? ? ? ? 2.390 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           368 
_struct_mon_prot_cis.label_asym_id          D 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ARG 
_struct_mon_prot_cis.auth_seq_id            369 
_struct_mon_prot_cis.auth_asym_id           D 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    369 
_struct_mon_prot_cis.pdbx_label_asym_id_2   D 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     370 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    D 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -21.87 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 CYS A 414 ? TRP A 415 ? CYS A 415 TRP A 416 
AA1 2 ARG A 420 ? GLY A 421 ? ARG A 421 GLY A 422 
AA2 1 CYS B 414 ? TRP B 415 ? CYS B 415 TRP B 416 
AA2 2 ARG B 420 ? GLY B 421 ? ARG B 421 GLY B 422 
AA3 1 CYS C 414 ? TRP C 415 ? CYS C 415 TRP C 416 
AA3 2 ARG C 420 ? GLY C 421 ? ARG C 421 GLY C 422 
AA4 1 CYS D 414 ? TRP D 415 ? CYS D 415 TRP D 416 
AA4 2 ARG D 420 ? GLY D 421 ? ARG D 421 GLY D 422 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N CYS A 414 ? N CYS A 415 O GLY A 421 ? O GLY A 422 
AA2 1 2 N CYS B 414 ? N CYS B 415 O GLY B 421 ? O GLY B 422 
AA3 1 2 N CYS C 414 ? N CYS C 415 O GLY C 421 ? O GLY C 422 
AA4 1 2 N CYS D 414 ? N CYS D 415 O GLY D 421 ? O GLY D 422 
# 
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 A CA  602 ? 5 'binding site for residue CA A 602'                             
AC2 Software A CA  603 ? 5 'binding site for residue CA A 603'                             
AC3 Software B CA  602 ? 4 'binding site for residue CA B 602'                             
AC4 Software B CA  603 ? 6 'binding site for residue CA B 603'                             
AC5 Software C CA  602 ? 3 'binding site for residue CA C 602'                             
AC6 Software C CA  603 ? 4 'binding site for residue CA C 603'                             
AC7 Software C CA  604 ? 3 'binding site for residue CA C 604'                             
AC8 Software D CA  602 ? 3 'binding site for residue CA D 602'                             
AC9 Software D CA  603 ? 3 'binding site for residue CA D 603'                             
AD1 Software A NAG 601 ? 3 'binding site for Mono-Saccharide NAG A 601 bound to ASN A 116' 
AD2 Software B NAG 601 ? 3 'binding site for Mono-Saccharide NAG B 601 bound to ASN B 116' 
AD3 Software C NAG 601 ? 2 'binding site for Mono-Saccharide NAG C 601 bound to ASN C 116' 
AD4 Software D NAG 601 ? 4 'binding site for Mono-Saccharide NAG D 601 bound to ASN D 116' 
# 
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 5 ASP A 387 ? ASP A 388 . ? 1_555 ? 
2  AC1 5 ASP A 390 ? ASP A 391 . ? 1_555 ? 
3  AC1 5 HOH R .   ? HOH A 731 . ? 1_555 ? 
4  AC1 5 HOH R .   ? HOH A 741 . ? 1_555 ? 
5  AC1 5 HOH R .   ? HOH A 787 . ? 1_555 ? 
6  AC2 5 ILE A 436 ? ILE A 437 . ? 1_555 ? 
7  AC2 5 GLU A 442 ? GLU A 443 . ? 1_555 ? 
8  AC2 5 HOH R .   ? HOH A 766 . ? 1_555 ? 
9  AC2 5 HOH R .   ? HOH A 770 . ? 1_555 ? 
10 AC2 5 HOH R .   ? HOH A 780 . ? 1_555 ? 
11 AC3 4 ILE B 436 ? ILE B 437 . ? 1_555 ? 
12 AC3 4 GLU B 442 ? GLU B 443 . ? 1_555 ? 
13 AC3 4 HOH S .   ? HOH B 707 . ? 1_555 ? 
14 AC3 4 HOH S .   ? HOH B 716 . ? 1_555 ? 
15 AC4 6 ASP B 387 ? ASP B 388 . ? 1_555 ? 
16 AC4 6 ASP B 390 ? ASP B 391 . ? 1_555 ? 
17 AC4 6 HOH S .   ? HOH B 702 . ? 1_555 ? 
18 AC4 6 HOH S .   ? HOH B 731 . ? 1_555 ? 
19 AC4 6 HOH S .   ? HOH B 741 . ? 1_555 ? 
20 AC4 6 HOH S .   ? HOH B 776 . ? 1_555 ? 
21 AC5 3 ASP C 47  ? ASP C 48  . ? 1_555 ? 
22 AC5 3 GLU C 71  ? GLU C 72  . ? 1_555 ? 
23 AC5 3 HOH T .   ? HOH C 703 . ? 1_555 ? 
24 AC6 4 ILE C 436 ? ILE C 437 . ? 1_555 ? 
25 AC6 4 GLU C 442 ? GLU C 443 . ? 1_555 ? 
26 AC6 4 HOH T .   ? HOH C 720 . ? 1_555 ? 
27 AC6 4 HOH T .   ? HOH C 724 . ? 1_555 ? 
28 AC7 3 ASP C 387 ? ASP C 388 . ? 1_555 ? 
29 AC7 3 ASP C 390 ? ASP C 391 . ? 1_555 ? 
30 AC7 3 HOH T .   ? HOH C 717 . ? 1_555 ? 
31 AC8 3 ILE D 436 ? ILE D 437 . ? 1_555 ? 
32 AC8 3 GLU D 442 ? GLU D 443 . ? 1_555 ? 
33 AC8 3 HOH U .   ? HOH D 712 . ? 1_555 ? 
34 AC9 3 ASP D 387 ? ASP D 388 . ? 1_555 ? 
35 AC9 3 ASP D 390 ? ASP D 391 . ? 1_555 ? 
36 AC9 3 HOH U .   ? HOH D 738 . ? 1_555 ? 
37 AD1 3 GLN A 111 ? GLN A 112 . ? 1_555 ? 
38 AD1 3 HIS A 112 ? HIS A 113 . ? 1_555 ? 
39 AD1 3 ASN A 115 ? ASN A 116 . ? 1_555 ? 
40 AD2 3 GLN B 111 ? GLN B 112 . ? 1_555 ? 
41 AD2 3 HIS B 112 ? HIS B 113 . ? 1_555 ? 
42 AD2 3 ASN B 115 ? ASN B 116 . ? 1_555 ? 
43 AD3 2 GLN C 111 ? GLN C 112 . ? 1_555 ? 
44 AD3 2 ASN C 115 ? ASN C 116 . ? 1_555 ? 
45 AD4 4 GLN D 111 ? GLN D 112 . ? 1_555 ? 
46 AD4 4 HIS D 112 ? HIS D 113 . ? 1_555 ? 
47 AD4 4 ASN D 115 ? ASN D 116 . ? 1_555 ? 
48 AD4 4 ARG D 148 ? ARG D 149 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4YWT 
_atom_sites.fract_transf_matrix[1][1]   0.021377 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000141 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006003 
_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]   0.007262 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . PRO A 1 24  ? 16.273  -22.753 92.219  1.00 101.81 ? 25  PRO A N   1 
ATOM   2     C  CA  . PRO A 1 24  ? 15.227  -23.775 92.099  1.00 104.69 ? 25  PRO A CA  1 
ATOM   3     C  C   . PRO A 1 24  ? 14.371  -23.669 90.834  1.00 106.06 ? 25  PRO A C   1 
ATOM   4     O  O   . PRO A 1 24  ? 13.153  -23.500 90.911  1.00 107.67 ? 25  PRO A O   1 
ATOM   5     C  CB  . PRO A 1 24  ? 14.372  -23.567 93.355  1.00 102.31 ? 25  PRO A CB  1 
ATOM   6     C  CG  . PRO A 1 24  ? 15.178  -22.699 94.254  1.00 103.64 ? 25  PRO A CG  1 
ATOM   7     C  CD  . PRO A 1 24  ? 16.100  -21.907 93.407  1.00 99.69  ? 25  PRO A CD  1 
ATOM   8     N  N   . ALA A 1 25  ? 15.018  -23.788 89.680  1.00 109.91 ? 26  ALA A N   1 
ATOM   9     C  CA  . ALA A 1 25  ? 14.322  -23.924 88.410  1.00 111.94 ? 26  ALA A CA  1 
ATOM   10    C  C   . ALA A 1 25  ? 14.743  -25.251 87.791  1.00 116.59 ? 26  ALA A C   1 
ATOM   11    O  O   . ALA A 1 25  ? 15.472  -26.017 88.422  1.00 119.45 ? 26  ALA A O   1 
ATOM   12    C  CB  . ALA A 1 25  ? 14.633  -22.760 87.485  1.00 109.52 ? 26  ALA A CB  1 
ATOM   13    N  N   . SER A 1 26  ? 14.283  -25.521 86.572  1.00 115.48 ? 27  SER A N   1 
ATOM   14    C  CA  . SER A 1 26  ? 14.573  -26.783 85.888  1.00 116.52 ? 27  SER A CA  1 
ATOM   15    C  C   . SER A 1 26  ? 14.114  -27.989 86.709  1.00 117.91 ? 27  SER A C   1 
ATOM   16    O  O   . SER A 1 26  ? 14.897  -28.898 86.992  1.00 121.69 ? 27  SER A O   1 
ATOM   17    C  CB  . SER A 1 26  ? 16.069  -26.901 85.563  1.00 113.50 ? 27  SER A CB  1 
ATOM   18    O  OG  . SER A 1 26  ? 16.843  -27.105 86.733  1.00 112.96 ? 27  SER A OG  1 
ATOM   19    N  N   . LYS A 1 27  ? 12.841  -27.962 87.098  1.00 117.75 ? 28  LYS A N   1 
ATOM   20    C  CA  . LYS A 1 27  ? 12.163  -29.079 87.759  1.00 118.18 ? 28  LYS A CA  1 
ATOM   21    C  C   . LYS A 1 27  ? 12.699  -29.438 89.148  1.00 115.94 ? 28  LYS A C   1 
ATOM   22    O  O   . LYS A 1 27  ? 12.699  -30.609 89.529  1.00 120.52 ? 28  LYS A O   1 
ATOM   23    C  CB  . LYS A 1 27  ? 12.212  -30.323 86.864  1.00 120.30 ? 28  LYS A CB  1 
ATOM   24    N  N   . SER A 1 28  ? 13.158  -28.442 89.900  1.00 107.33 ? 29  SER A N   1 
ATOM   25    C  CA  . SER A 1 28  ? 13.444  -28.641 91.321  1.00 100.11 ? 29  SER A CA  1 
ATOM   26    C  C   . SER A 1 28  ? 13.041  -27.414 92.134  1.00 91.89  ? 29  SER A C   1 
ATOM   27    O  O   . SER A 1 28  ? 13.389  -26.295 91.777  1.00 91.57  ? 29  SER A O   1 
ATOM   28    C  CB  . SER A 1 28  ? 14.925  -28.953 91.537  1.00 99.74  ? 29  SER A CB  1 
ATOM   29    O  OG  . SER A 1 28  ? 15.206  -29.136 92.913  1.00 99.24  ? 29  SER A OG  1 
ATOM   30    N  N   . ARG A 1 29  ? 12.288  -27.615 93.210  1.00 88.82  ? 30  ARG A N   1 
ATOM   31    C  CA  . ARG A 1 29  ? 11.910  -26.503 94.084  1.00 78.92  ? 30  ARG A CA  1 
ATOM   32    C  C   . ARG A 1 29  ? 12.787  -26.378 95.330  1.00 76.57  ? 30  ARG A C   1 
ATOM   33    O  O   . ARG A 1 29  ? 12.532  -25.529 96.186  1.00 77.00  ? 30  ARG A O   1 
ATOM   34    C  CB  . ARG A 1 29  ? 10.439  -26.627 94.476  1.00 83.02  ? 30  ARG A CB  1 
ATOM   35    C  CG  . ARG A 1 29  ? 9.597   -27.086 93.313  1.00 82.74  ? 30  ARG A CG  1 
ATOM   36    C  CD  . ARG A 1 29  ? 8.110   -27.016 93.571  1.00 82.86  ? 30  ARG A CD  1 
ATOM   37    N  NE  . ARG A 1 29  ? 7.380   -27.041 92.307  1.00 81.79  ? 30  ARG A NE  1 
ATOM   38    C  CZ  . ARG A 1 29  ? 6.059   -27.124 92.203  1.00 81.61  ? 30  ARG A CZ  1 
ATOM   39    N  NH1 . ARG A 1 29  ? 5.310   -27.230 93.291  1.00 74.35  ? 30  ARG A NH1 1 
ATOM   40    N  NH2 . ARG A 1 29  ? 5.490   -27.146 91.005  1.00 77.18  ? 30  ARG A NH2 1 
ATOM   41    N  N   . SER A 1 30  ? 13.794  -27.238 95.447  1.00 78.30  ? 31  SER A N   1 
ATOM   42    C  CA  . SER A 1 30  ? 14.694  -27.208 96.597  1.00 79.87  ? 31  SER A CA  1 
ATOM   43    C  C   . SER A 1 30  ? 15.431  -25.875 96.685  1.00 76.51  ? 31  SER A C   1 
ATOM   44    O  O   . SER A 1 30  ? 15.990  -25.398 95.699  1.00 70.88  ? 31  SER A O   1 
ATOM   45    C  CB  . SER A 1 30  ? 15.697  -28.362 96.525  1.00 85.62  ? 31  SER A CB  1 
ATOM   46    O  OG  . SER A 1 30  ? 16.716  -28.097 95.578  1.00 86.92  ? 31  SER A OG  1 
ATOM   47    N  N   . CYS A 1 31  ? 15.427  -25.281 97.875  1.00 75.85  ? 32  CYS A N   1 
ATOM   48    C  CA  . CYS A 1 31  ? 16.013  -23.960 98.086  1.00 73.66  ? 32  CYS A CA  1 
ATOM   49    C  C   . CYS A 1 31  ? 17.490  -24.030 98.458  1.00 73.41  ? 32  CYS A C   1 
ATOM   50    O  O   . CYS A 1 31  ? 18.025  -23.100 99.060  1.00 73.82  ? 32  CYS A O   1 
ATOM   51    C  CB  . CYS A 1 31  ? 15.251  -23.213 99.184  1.00 73.74  ? 32  CYS A CB  1 
ATOM   52    S  SG  . CYS A 1 31  ? 13.570  -22.727 98.747  1.00 69.60  ? 32  CYS A SG  1 
ATOM   53    N  N   . GLY A 1 32  ? 18.142  -25.130 98.092  1.00 81.50  ? 33  GLY A N   1 
ATOM   54    C  CA  . GLY A 1 32  ? 19.514  -25.394 98.493  1.00 85.68  ? 33  GLY A CA  1 
ATOM   55    C  C   . GLY A 1 32  ? 20.525  -24.301 98.194  1.00 84.66  ? 33  GLY A C   1 
ATOM   56    O  O   . GLY A 1 32  ? 21.269  -23.877 99.081  1.00 87.67  ? 33  GLY A O   1 
ATOM   57    N  N   . GLU A 1 33  ? 20.556  -23.844 96.947  1.00 85.31  ? 34  GLU A N   1 
ATOM   58    C  CA  . GLU A 1 33  ? 21.532  -22.844 96.528  1.00 81.71  ? 34  GLU A CA  1 
ATOM   59    C  C   . GLU A 1 33  ? 21.259  -21.489 97.173  1.00 77.52  ? 34  GLU A C   1 
ATOM   60    O  O   . GLU A 1 33  ? 22.187  -20.794 97.592  1.00 74.34  ? 34  GLU A O   1 
ATOM   61    C  CB  . GLU A 1 33  ? 21.541  -22.717 95.004  1.00 87.16  ? 34  GLU A CB  1 
ATOM   62    C  CG  . GLU A 1 33  ? 21.602  -24.057 94.289  1.00 96.02  ? 34  GLU A CG  1 
ATOM   63    C  CD  . GLU A 1 33  ? 22.188  -23.953 92.896  1.00 100.35 ? 34  GLU A CD  1 
ATOM   64    O  OE1 . GLU A 1 33  ? 22.125  -22.857 92.301  1.00 98.74  ? 34  GLU A OE1 1 
ATOM   65    O  OE2 . GLU A 1 33  ? 22.712  -24.971 92.395  1.00 104.10 ? 34  GLU A OE2 1 
ATOM   66    N  N   . VAL A 1 34  ? 19.985  -21.121 97.254  1.00 73.75  ? 35  VAL A N   1 
ATOM   67    C  CA  . VAL A 1 34  ? 19.587  -19.897 97.937  1.00 70.44  ? 35  VAL A CA  1 
ATOM   68    C  C   . VAL A 1 34  ? 19.972  -19.985 99.410  1.00 72.29  ? 35  VAL A C   1 
ATOM   69    O  O   . VAL A 1 34  ? 20.414  -19.005 100.005 1.00 70.02  ? 35  VAL A O   1 
ATOM   70    C  CB  . VAL A 1 34  ? 18.073  -19.638 97.799  1.00 67.15  ? 35  VAL A CB  1 
ATOM   71    C  CG1 . VAL A 1 34  ? 17.630  -18.494 98.701  1.00 62.27  ? 35  VAL A CG1 1 
ATOM   72    C  CG2 . VAL A 1 34  ? 17.722  -19.352 96.350  1.00 61.41  ? 35  VAL A CG2 1 
ATOM   73    N  N   . ARG A 1 35  ? 19.820  -21.175 99.983  1.00 75.02  ? 36  ARG A N   1 
ATOM   74    C  CA  . ARG A 1 35  ? 20.200  -21.416 101.370 1.00 80.31  ? 36  ARG A CA  1 
ATOM   75    C  C   . ARG A 1 35  ? 21.694  -21.199 101.579 1.00 86.26  ? 36  ARG A C   1 
ATOM   76    O  O   . ARG A 1 35  ? 22.104  -20.468 102.483 1.00 86.94  ? 36  ARG A O   1 
ATOM   77    C  CB  . ARG A 1 35  ? 19.815  -22.835 101.795 1.00 72.33  ? 36  ARG A CB  1 
ATOM   78    N  N   . GLN A 1 36  ? 22.503  -21.834 100.735 1.00 91.30  ? 37  GLN A N   1 
ATOM   79    C  CA  . GLN A 1 36  ? 23.954  -21.737 100.847 1.00 96.11  ? 37  GLN A CA  1 
ATOM   80    C  C   . GLN A 1 36  ? 24.447  -20.308 100.629 1.00 89.82  ? 37  GLN A C   1 
ATOM   81    O  O   . GLN A 1 36  ? 25.326  -19.836 101.348 1.00 92.49  ? 37  GLN A O   1 
ATOM   82    C  CB  . GLN A 1 36  ? 24.635  -22.683 99.853  1.00 102.51 ? 37  GLN A CB  1 
ATOM   83    C  CG  . GLN A 1 36  ? 25.929  -22.135 99.265  1.00 105.92 ? 37  GLN A CG  1 
ATOM   84    C  CD  . GLN A 1 36  ? 26.646  -23.138 98.387  1.00 111.38 ? 37  GLN A CD  1 
ATOM   85    O  OE1 . GLN A 1 36  ? 26.292  -24.316 98.352  1.00 115.29 ? 37  GLN A OE1 1 
ATOM   86    N  NE2 . GLN A 1 36  ? 27.662  -22.673 97.668  1.00 111.03 ? 37  GLN A NE2 1 
ATOM   87    N  N   . ILE A 1 37  ? 23.878  -19.621 99.642  1.00 85.88  ? 38  ILE A N   1 
ATOM   88    C  CA  . ILE A 1 37  ? 24.282  -18.250 99.342  1.00 80.63  ? 38  ILE A CA  1 
ATOM   89    C  C   . ILE A 1 37  ? 23.888  -17.303 100.475 1.00 79.37  ? 38  ILE A C   1 
ATOM   90    O  O   . ILE A 1 37  ? 24.684  -16.467 100.902 1.00 78.40  ? 38  ILE A O   1 
ATOM   91    C  CB  . ILE A 1 37  ? 23.667  -17.760 98.015  1.00 75.56  ? 38  ILE A CB  1 
ATOM   92    C  CG1 . ILE A 1 37  ? 24.275  -18.526 96.838  1.00 75.32  ? 38  ILE A CG1 1 
ATOM   93    C  CG2 . ILE A 1 37  ? 23.895  -16.269 97.833  1.00 75.90  ? 38  ILE A CG2 1 
ATOM   94    C  CD1 . ILE A 1 37  ? 23.673  -18.170 95.498  1.00 73.10  ? 38  ILE A CD1 1 
ATOM   95    N  N   . TYR A 1 38  ? 22.664  -17.455 100.969 1.00 78.66  ? 39  TYR A N   1 
ATOM   96    C  CA  . TYR A 1 38  ? 22.160  -16.640 102.071 1.00 80.63  ? 39  TYR A CA  1 
ATOM   97    C  C   . TYR A 1 38  ? 22.944  -16.892 103.356 1.00 87.57  ? 39  TYR A C   1 
ATOM   98    O  O   . TYR A 1 38  ? 23.084  -16.001 104.193 1.00 89.22  ? 39  TYR A O   1 
ATOM   99    C  CB  . TYR A 1 38  ? 20.671  -16.923 102.288 1.00 75.19  ? 39  TYR A CB  1 
ATOM   100   C  CG  . TYR A 1 38  ? 20.018  -16.150 103.411 1.00 72.57  ? 39  TYR A CG  1 
ATOM   101   C  CD1 . TYR A 1 38  ? 19.666  -14.817 103.250 1.00 68.55  ? 39  TYR A CD1 1 
ATOM   102   C  CD2 . TYR A 1 38  ? 19.723  -16.763 104.621 1.00 71.60  ? 39  TYR A CD2 1 
ATOM   103   C  CE1 . TYR A 1 38  ? 19.057  -14.112 104.271 1.00 69.11  ? 39  TYR A CE1 1 
ATOM   104   C  CE2 . TYR A 1 38  ? 19.110  -16.069 105.644 1.00 72.83  ? 39  TYR A CE2 1 
ATOM   105   C  CZ  . TYR A 1 38  ? 18.779  -14.744 105.465 1.00 72.84  ? 39  TYR A CZ  1 
ATOM   106   O  OH  . TYR A 1 38  ? 18.173  -14.048 106.486 1.00 76.08  ? 39  TYR A OH  1 
ATOM   107   N  N   . GLY A 1 39  ? 23.457  -18.111 103.501 1.00 95.70  ? 40  GLY A N   1 
ATOM   108   C  CA  . GLY A 1 39  ? 24.214  -18.491 104.680 1.00 100.10 ? 40  GLY A CA  1 
ATOM   109   C  C   . GLY A 1 39  ? 25.657  -18.025 104.644 1.00 102.42 ? 40  GLY A C   1 
ATOM   110   O  O   . GLY A 1 39  ? 26.204  -17.589 105.657 1.00 106.05 ? 40  GLY A O   1 
ATOM   111   N  N   . ALA A 1 40  ? 26.275  -18.111 103.469 1.00 100.10 ? 41  ALA A N   1 
ATOM   112   C  CA  . ALA A 1 40  ? 27.655  -17.673 103.286 1.00 96.39  ? 41  ALA A CA  1 
ATOM   113   C  C   . ALA A 1 40  ? 27.752  -16.153 103.346 1.00 92.20  ? 41  ALA A C   1 
ATOM   114   O  O   . ALA A 1 40  ? 28.845  -15.586 103.330 1.00 94.38  ? 41  ALA A O   1 
ATOM   115   C  CB  . ALA A 1 40  ? 28.206  -18.189 101.965 1.00 95.46  ? 41  ALA A CB  1 
ATOM   116   N  N   . LYS A 1 41  ? 26.597  -15.500 103.414 1.00 88.64  ? 42  LYS A N   1 
ATOM   117   C  CA  . LYS A 1 41  ? 26.531  -14.050 103.500 1.00 81.32  ? 42  LYS A CA  1 
ATOM   118   C  C   . LYS A 1 41  ? 26.310  -13.582 104.936 1.00 82.84  ? 42  LYS A C   1 
ATOM   119   O  O   . LYS A 1 41  ? 25.982  -12.421 105.176 1.00 84.48  ? 42  LYS A O   1 
ATOM   120   C  CB  . LYS A 1 41  ? 25.425  -13.518 102.588 1.00 79.43  ? 42  LYS A CB  1 
ATOM   121   C  CG  . LYS A 1 41  ? 25.807  -13.501 101.118 1.00 75.83  ? 42  LYS A CG  1 
ATOM   122   C  CD  . LYS A 1 41  ? 24.670  -12.993 100.251 1.00 75.12  ? 42  LYS A CD  1 
ATOM   123   C  CE  . LYS A 1 41  ? 25.181  -12.538 98.895  1.00 73.82  ? 42  LYS A CE  1 
ATOM   124   N  NZ  . LYS A 1 41  ? 26.105  -11.374 99.018  1.00 73.73  ? 42  LYS A NZ  1 
ATOM   125   N  N   . GLY A 1 42  ? 26.487  -14.493 105.888 1.00 85.12  ? 43  GLY A N   1 
ATOM   126   C  CA  . GLY A 1 42  ? 26.447  -14.142 107.296 1.00 84.01  ? 43  GLY A CA  1 
ATOM   127   C  C   . GLY A 1 42  ? 25.060  -14.062 107.907 1.00 83.21  ? 43  GLY A C   1 
ATOM   128   O  O   . GLY A 1 42  ? 24.842  -13.324 108.867 1.00 83.19  ? 43  GLY A O   1 
ATOM   129   N  N   . PHE A 1 43  ? 24.122  -14.823 107.356 1.00 83.75  ? 44  PHE A N   1 
ATOM   130   C  CA  . PHE A 1 43  ? 22.768  -14.869 107.896 1.00 85.50  ? 44  PHE A CA  1 
ATOM   131   C  C   . PHE A 1 43  ? 22.398  -16.298 108.283 1.00 87.49  ? 44  PHE A C   1 
ATOM   132   O  O   . PHE A 1 43  ? 23.022  -17.252 107.820 1.00 89.48  ? 44  PHE A O   1 
ATOM   133   C  CB  . PHE A 1 43  ? 21.761  -14.316 106.889 1.00 81.57  ? 44  PHE A CB  1 
ATOM   134   C  CG  . PHE A 1 43  ? 22.036  -12.904 106.462 1.00 77.68  ? 44  PHE A CG  1 
ATOM   135   C  CD1 . PHE A 1 43  ? 21.896  -11.855 107.357 1.00 78.69  ? 44  PHE A CD1 1 
ATOM   136   C  CD2 . PHE A 1 43  ? 22.414  -12.621 105.160 1.00 74.88  ? 44  PHE A CD2 1 
ATOM   137   C  CE1 . PHE A 1 43  ? 22.145  -10.553 106.965 1.00 78.16  ? 44  PHE A CE1 1 
ATOM   138   C  CE2 . PHE A 1 43  ? 22.661  -11.322 104.761 1.00 76.07  ? 44  PHE A CE2 1 
ATOM   139   C  CZ  . PHE A 1 43  ? 22.525  -10.286 105.664 1.00 74.68  ? 44  PHE A CZ  1 
ATOM   140   N  N   . SER A 1 44  ? 21.386  -16.439 109.136 1.00 93.01  ? 45  SER A N   1 
ATOM   141   C  CA  . SER A 1 44  ? 20.983  -17.748 109.643 1.00 95.52  ? 45  SER A CA  1 
ATOM   142   C  C   . SER A 1 44  ? 20.484  -18.670 108.536 1.00 93.55  ? 45  SER A C   1 
ATOM   143   O  O   . SER A 1 44  ? 19.629  -18.291 107.737 1.00 93.53  ? 45  SER A O   1 
ATOM   144   C  CB  . SER A 1 44  ? 19.897  -17.596 110.711 1.00 100.16 ? 45  SER A CB  1 
ATOM   145   O  OG  . SER A 1 44  ? 20.425  -17.063 111.912 1.00 103.02 ? 45  SER A OG  1 
ATOM   146   N  N   . LEU A 1 45  ? 21.023  -19.885 108.498 1.00 91.15  ? 46  LEU A N   1 
ATOM   147   C  CA  . LEU A 1 45  ? 20.568  -20.897 107.552 1.00 90.56  ? 46  LEU A CA  1 
ATOM   148   C  C   . LEU A 1 45  ? 19.177  -21.390 107.935 1.00 90.16  ? 46  LEU A C   1 
ATOM   149   O  O   . LEU A 1 45  ? 18.444  -21.926 107.104 1.00 91.73  ? 46  LEU A O   1 
ATOM   150   C  CB  . LEU A 1 45  ? 21.547  -22.075 107.498 1.00 88.13  ? 46  LEU A CB  1 
ATOM   151   C  CG  . LEU A 1 45  ? 22.823  -21.931 106.662 1.00 85.55  ? 46  LEU A CG  1 
ATOM   152   C  CD1 . LEU A 1 45  ? 23.817  -20.981 107.314 1.00 82.48  ? 46  LEU A CD1 1 
ATOM   153   C  CD2 . LEU A 1 45  ? 23.457  -23.294 106.425 1.00 79.12  ? 46  LEU A CD2 1 
ATOM   154   N  N   . SER A 1 46  ? 18.826  -21.201 109.203 1.00 93.70  ? 47  SER A N   1 
ATOM   155   C  CA  . SER A 1 46  ? 17.531  -21.623 109.723 1.00 95.69  ? 47  SER A CA  1 
ATOM   156   C  C   . SER A 1 46  ? 16.391  -20.806 109.124 1.00 92.22  ? 47  SER A C   1 
ATOM   157   O  O   . SER A 1 46  ? 15.257  -21.279 109.039 1.00 92.79  ? 47  SER A O   1 
ATOM   158   C  CB  . SER A 1 46  ? 17.509  -21.508 111.249 1.00 98.17  ? 47  SER A CB  1 
ATOM   159   O  OG  . SER A 1 46  ? 17.735  -20.171 111.661 1.00 97.51  ? 47  SER A OG  1 
ATOM   160   N  N   . ASP A 1 47  ? 16.697  -19.581 108.707 1.00 91.31  ? 48  ASP A N   1 
ATOM   161   C  CA  . ASP A 1 47  ? 15.686  -18.694 108.144 1.00 88.87  ? 48  ASP A CA  1 
ATOM   162   C  C   . ASP A 1 47  ? 15.251  -19.128 106.749 1.00 87.82  ? 48  ASP A C   1 
ATOM   163   O  O   . ASP A 1 47  ? 14.225  -18.672 106.244 1.00 86.99  ? 48  ASP A O   1 
ATOM   164   C  CB  . ASP A 1 47  ? 16.196  -17.251 108.093 1.00 92.50  ? 48  ASP A CB  1 
ATOM   165   C  CG  . ASP A 1 47  ? 16.446  -16.671 109.470 1.00 96.18  ? 48  ASP A CG  1 
ATOM   166   O  OD1 . ASP A 1 47  ? 15.618  -16.908 110.373 1.00 96.51  ? 48  ASP A OD1 1 
ATOM   167   O  OD2 . ASP A 1 47  ? 17.453  -15.951 109.641 1.00 98.04  ? 48  ASP A OD2 1 
ATOM   168   N  N   . VAL A 1 48  ? 16.029  -20.007 106.126 1.00 82.43  ? 49  VAL A N   1 
ATOM   169   C  CA  . VAL A 1 48  ? 15.731  -20.450 104.770 1.00 72.61  ? 49  VAL A CA  1 
ATOM   170   C  C   . VAL A 1 48  ? 14.757  -21.621 104.750 1.00 84.68  ? 49  VAL A C   1 
ATOM   171   O  O   . VAL A 1 48  ? 15.034  -22.674 105.325 1.00 77.09  ? 49  VAL A O   1 
ATOM   172   C  CB  . VAL A 1 48  ? 17.004  -20.862 104.014 1.00 72.02  ? 49  VAL A CB  1 
ATOM   173   C  CG1 . VAL A 1 48  ? 16.647  -21.353 102.617 1.00 71.13  ? 49  VAL A CG1 1 
ATOM   174   C  CG2 . VAL A 1 48  ? 17.977  -19.700 103.943 1.00 71.27  ? 49  VAL A CG2 1 
ATOM   175   N  N   . PRO A 1 49  ? 13.608  -21.437 104.085 1.00 80.83  ? 50  PRO A N   1 
ATOM   176   C  CA  . PRO A 1 49  ? 12.639  -22.521 103.916 1.00 79.59  ? 50  PRO A CA  1 
ATOM   177   C  C   . PRO A 1 49  ? 13.238  -23.710 103.176 1.00 79.66  ? 50  PRO A C   1 
ATOM   178   O  O   . PRO A 1 49  ? 14.003  -23.543 102.224 1.00 75.59  ? 50  PRO A O   1 
ATOM   179   C  CB  . PRO A 1 49  ? 11.513  -21.872 103.100 1.00 79.45  ? 50  PRO A CB  1 
ATOM   180   C  CG  . PRO A 1 49  ? 12.114  -20.648 102.501 1.00 77.31  ? 50  PRO A CG  1 
ATOM   181   C  CD  . PRO A 1 49  ? 13.138  -20.180 103.482 1.00 76.86  ? 50  PRO A CD  1 
ATOM   182   N  N   . GLN A 1 50  ? 12.878  -24.901 103.639 1.00 83.17  ? 51  GLN A N   1 
ATOM   183   C  CA  . GLN A 1 50  ? 13.371  -26.165 103.108 1.00 86.10  ? 51  GLN A CA  1 
ATOM   184   C  C   . GLN A 1 50  ? 13.112  -26.297 101.612 1.00 78.86  ? 51  GLN A C   1 
ATOM   185   O  O   . GLN A 1 50  ? 13.991  -26.707 100.855 1.00 78.55  ? 51  GLN A O   1 
ATOM   186   C  CB  . GLN A 1 50  ? 12.733  -27.345 103.857 1.00 92.34  ? 51  GLN A CB  1 
ATOM   187   C  CG  . GLN A 1 50  ? 11.231  -27.214 104.175 1.00 94.05  ? 51  GLN A CG  1 
ATOM   188   C  CD  . GLN A 1 50  ? 10.904  -26.124 105.188 1.00 94.14  ? 51  GLN A CD  1 
ATOM   189   O  OE1 . GLN A 1 50  ? 11.574  -25.989 106.212 1.00 95.14  ? 51  GLN A OE1 1 
ATOM   190   N  NE2 . GLN A 1 50  ? 9.879   -25.330 104.894 1.00 91.43  ? 51  GLN A NE2 1 
ATOM   191   N  N   . ALA A 1 51  ? 11.901  -25.952 101.191 1.00 78.01  ? 52  ALA A N   1 
ATOM   192   C  CA  . ALA A 1 51  ? 11.566  -25.958 99.775  1.00 76.48  ? 52  ALA A CA  1 
ATOM   193   C  C   . ALA A 1 51  ? 10.904  -24.645 99.380  1.00 74.02  ? 52  ALA A C   1 
ATOM   194   O  O   . ALA A 1 51  ? 10.688  -23.771 100.219 1.00 73.60  ? 52  ALA A O   1 
ATOM   195   C  CB  . ALA A 1 51  ? 10.659  -27.134 99.444  1.00 78.35  ? 52  ALA A CB  1 
ATOM   196   N  N   . GLU A 1 52  ? 10.582  -24.518 98.098  1.00 72.56  ? 53  GLU A N   1 
ATOM   197   C  CA  . GLU A 1 52  ? 9.996   -23.296 97.565  1.00 75.66  ? 53  GLU A CA  1 
ATOM   198   C  C   . GLU A 1 52  ? 8.610   -23.061 98.161  1.00 75.71  ? 53  GLU A C   1 
ATOM   199   O  O   . GLU A 1 52  ? 7.745   -23.934 98.098  1.00 79.62  ? 53  GLU A O   1 
ATOM   200   C  CB  . GLU A 1 52  ? 9.929   -23.384 96.039  1.00 74.87  ? 53  GLU A CB  1 
ATOM   201   C  CG  . GLU A 1 52  ? 9.591   -22.096 95.321  1.00 66.54  ? 53  GLU A CG  1 
ATOM   202   C  CD  . GLU A 1 52  ? 9.904   -22.179 93.839  1.00 69.72  ? 53  GLU A CD  1 
ATOM   203   O  OE1 . GLU A 1 52  ? 8.986   -21.974 93.018  1.00 66.60  ? 53  GLU A OE1 1 
ATOM   204   O  OE2 . GLU A 1 52  ? 11.073  -22.458 93.497  1.00 65.17  ? 53  GLU A OE2 1 
ATOM   205   N  N   . ILE A 1 53  ? 8.400   -21.880 98.736  1.00 69.92  ? 54  ILE A N   1 
ATOM   206   C  CA  . ILE A 1 53  ? 7.145   -21.580 99.422  1.00 70.77  ? 54  ILE A CA  1 
ATOM   207   C  C   . ILE A 1 53  ? 6.358   -20.472 98.727  1.00 72.03  ? 54  ILE A C   1 
ATOM   208   O  O   . ILE A 1 53  ? 6.786   -19.942 97.703  1.00 70.72  ? 54  ILE A O   1 
ATOM   209   C  CB  . ILE A 1 53  ? 7.386   -21.167 100.889 1.00 71.73  ? 54  ILE A CB  1 
ATOM   210   C  CG1 . ILE A 1 53  ? 8.137   -19.835 100.954 1.00 78.44  ? 54  ILE A CG1 1 
ATOM   211   C  CG2 . ILE A 1 53  ? 8.140   -22.257 101.635 1.00 73.86  ? 54  ILE A CG2 1 
ATOM   212   C  CD1 . ILE A 1 53  ? 8.238   -19.254 102.349 1.00 77.04  ? 54  ILE A CD1 1 
ATOM   213   N  N   . SER A 1 54  ? 5.206   -20.128 99.298  1.00 71.75  ? 55  SER A N   1 
ATOM   214   C  CA  . SER A 1 54  ? 4.343   -19.094 98.736  1.00 69.74  ? 55  SER A CA  1 
ATOM   215   C  C   . SER A 1 54  ? 4.898   -17.702 99.027  1.00 70.03  ? 55  SER A C   1 
ATOM   216   O  O   . SER A 1 54  ? 5.486   -17.464 100.082 1.00 71.01  ? 55  SER A O   1 
ATOM   217   C  CB  . SER A 1 54  ? 2.921   -19.228 99.285  1.00 71.59  ? 55  SER A CB  1 
ATOM   218   O  OG  . SER A 1 54  ? 1.990   -18.554 98.457  1.00 73.44  ? 55  SER A OG  1 
ATOM   219   N  N   . GLY A 1 55  ? 4.698   -16.785 98.087  1.00 71.38  ? 56  GLY A N   1 
ATOM   220   C  CA  . GLY A 1 55  ? 5.346   -15.485 98.126  1.00 71.68  ? 56  GLY A CA  1 
ATOM   221   C  C   . GLY A 1 55  ? 4.514   -14.310 98.601  1.00 73.60  ? 56  GLY A C   1 
ATOM   222   O  O   . GLY A 1 55  ? 4.817   -13.170 98.253  1.00 75.12  ? 56  GLY A O   1 
ATOM   223   N  N   . GLU A 1 56  ? 3.457   -14.576 99.365  1.00 77.21  ? 57  GLU A N   1 
ATOM   224   C  CA  . GLU A 1 56  ? 2.567   -13.517 99.845  1.00 78.17  ? 57  GLU A CA  1 
ATOM   225   C  C   . GLU A 1 56  ? 3.314   -12.368 100.527 1.00 71.34  ? 57  GLU A C   1 
ATOM   226   O  O   . GLU A 1 56  ? 2.976   -11.200 100.340 1.00 68.36  ? 57  GLU A O   1 
ATOM   227   C  CB  . GLU A 1 56  ? 1.515   -14.087 100.814 1.00 83.74  ? 57  GLU A CB  1 
ATOM   228   C  CG  . GLU A 1 56  ? 2.073   -14.546 102.159 1.00 89.59  ? 57  GLU A CG  1 
ATOM   229   C  CD  . GLU A 1 56  ? 1.211   -14.139 103.343 1.00 95.65  ? 57  GLU A CD  1 
ATOM   230   O  OE1 . GLU A 1 56  ? 0.039   -14.568 103.429 1.00 98.60  ? 57  GLU A OE1 1 
ATOM   231   O  OE2 . GLU A 1 56  ? 1.715   -13.365 104.186 1.00 95.23  ? 57  GLU A OE2 1 
ATOM   232   N  N   . HIS A 1 57  ? 4.339   -12.710 101.299 1.00 74.47  ? 58  HIS A N   1 
ATOM   233   C  CA  . HIS A 1 57  ? 4.942   -11.788 102.251 1.00 78.19  ? 58  HIS A CA  1 
ATOM   234   C  C   . HIS A 1 57  ? 5.890   -10.778 101.624 1.00 75.63  ? 58  HIS A C   1 
ATOM   235   O  O   . HIS A 1 57  ? 6.234   -9.776  102.255 1.00 72.09  ? 58  HIS A O   1 
ATOM   236   C  CB  . HIS A 1 57  ? 5.686   -12.588 103.315 1.00 80.04  ? 58  HIS A CB  1 
ATOM   237   C  CG  . HIS A 1 57  ? 6.731   -13.498 102.752 1.00 83.62  ? 58  HIS A CG  1 
ATOM   238   N  ND1 . HIS A 1 57  ? 6.421   -14.647 102.058 1.00 85.90  ? 58  HIS A ND1 1 
ATOM   239   C  CD2 . HIS A 1 57  ? 8.083   -13.417 102.762 1.00 85.25  ? 58  HIS A CD2 1 
ATOM   240   C  CE1 . HIS A 1 57  ? 7.537   -15.242 101.674 1.00 86.66  ? 58  HIS A CE1 1 
ATOM   241   N  NE2 . HIS A 1 57  ? 8.559   -14.515 102.088 1.00 84.71  ? 58  HIS A NE2 1 
ATOM   242   N  N   . LEU A 1 58  ? 6.311   -11.045 100.391 1.00 78.90  ? 59  LEU A N   1 
ATOM   243   C  CA  . LEU A 1 58  ? 7.347   -10.240 99.761  1.00 82.34  ? 59  LEU A CA  1 
ATOM   244   C  C   . LEU A 1 58  ? 6.907   -8.788  99.620  1.00 83.40  ? 59  LEU A C   1 
ATOM   245   O  O   . LEU A 1 58  ? 5.884   -8.492  99.001  1.00 87.43  ? 59  LEU A O   1 
ATOM   246   C  CB  . LEU A 1 58  ? 7.693   -10.815 98.385  1.00 77.76  ? 59  LEU A CB  1 
ATOM   247   C  CG  . LEU A 1 58  ? 7.945   -12.323 98.289  1.00 75.10  ? 59  LEU A CG  1 
ATOM   248   C  CD1 . LEU A 1 58  ? 8.058   -12.747 96.832  1.00 73.45  ? 59  LEU A CD1 1 
ATOM   249   C  CD2 . LEU A 1 58  ? 9.189   -12.725 99.066  1.00 74.31  ? 59  LEU A CD2 1 
ATOM   250   N  N   . ARG A 1 59  ? 7.691   -7.887  100.203 1.00 84.71  ? 60  ARG A N   1 
ATOM   251   C  CA  . ARG A 1 59  ? 7.471   -6.454  100.054 1.00 83.83  ? 60  ARG A CA  1 
ATOM   252   C  C   . ARG A 1 59  ? 8.086   -5.903  98.770  1.00 77.48  ? 60  ARG A C   1 
ATOM   253   O  O   . ARG A 1 59  ? 7.532   -4.998  98.148  1.00 77.35  ? 60  ARG A O   1 
ATOM   254   C  CB  . ARG A 1 59  ? 8.015   -5.705  101.272 1.00 95.12  ? 60  ARG A CB  1 
ATOM   255   C  CG  . ARG A 1 59  ? 7.292   -6.046  102.570 1.00 103.95 ? 60  ARG A CG  1 
ATOM   256   C  CD  . ARG A 1 59  ? 5.892   -5.432  102.625 1.00 108.99 ? 60  ARG A CD  1 
ATOM   257   N  NE  . ARG A 1 59  ? 5.920   -3.972  102.706 1.00 111.07 ? 60  ARG A NE  1 
ATOM   258   C  CZ  . ARG A 1 59  ? 4.843   -3.196  102.629 1.00 111.44 ? 60  ARG A CZ  1 
ATOM   259   N  NH1 . ARG A 1 59  ? 3.641   -3.734  102.470 1.00 113.03 ? 60  ARG A NH1 1 
ATOM   260   N  NH2 . ARG A 1 59  ? 4.966   -1.878  102.715 1.00 111.57 ? 60  ARG A NH2 1 
ATOM   261   N  N   . ILE A 1 60  ? 9.236   -6.449  98.384  1.00 68.06  ? 61  ILE A N   1 
ATOM   262   C  CA  . ILE A 1 60  ? 10.000  -5.911  97.260  1.00 59.13  ? 61  ILE A CA  1 
ATOM   263   C  C   . ILE A 1 60  ? 9.941   -6.798  96.018  1.00 55.29  ? 61  ILE A C   1 
ATOM   264   O  O   . ILE A 1 60  ? 9.415   -6.388  94.983  1.00 55.64  ? 61  ILE A O   1 
ATOM   265   C  CB  . ILE A 1 60  ? 11.478  -5.693  97.641  1.00 57.37  ? 61  ILE A CB  1 
ATOM   266   C  CG1 . ILE A 1 60  ? 11.584  -4.790  98.871  1.00 55.33  ? 61  ILE A CG1 1 
ATOM   267   C  CG2 . ILE A 1 60  ? 12.249  -5.098  96.472  1.00 52.19  ? 61  ILE A CG2 1 
ATOM   268   C  CD1 . ILE A 1 60  ? 12.885  -4.937  99.626  1.00 49.61  ? 61  ILE A CD1 1 
ATOM   269   N  N   . CYS A 1 61  ? 10.503  -8.000  96.121  1.00 55.12  ? 62  CYS A N   1 
ATOM   270   C  CA  . CYS A 1 61  ? 10.506  -8.946  95.009  1.00 56.34  ? 62  CYS A CA  1 
ATOM   271   C  C   . CYS A 1 61  ? 9.088   -9.226  94.528  1.00 57.85  ? 62  CYS A C   1 
ATOM   272   O  O   . CYS A 1 61  ? 8.163   -9.297  95.339  1.00 52.23  ? 62  CYS A O   1 
ATOM   273   C  CB  . CYS A 1 61  ? 11.192  -10.254 95.414  1.00 51.43  ? 62  CYS A CB  1 
ATOM   274   S  SG  . CYS A 1 61  ? 12.914  -10.072 95.930  1.00 88.10  ? 62  CYS A SG  1 
ATOM   275   N  N   . PRO A 1 62  ? 8.914   -9.375  93.204  1.00 56.43  ? 63  PRO A N   1 
ATOM   276   C  CA  . PRO A 1 62  ? 7.602   -9.674  92.621  1.00 59.46  ? 63  PRO A CA  1 
ATOM   277   C  C   . PRO A 1 62  ? 6.984   -10.898 93.276  1.00 63.89  ? 63  PRO A C   1 
ATOM   278   O  O   . PRO A 1 62  ? 7.666   -11.910 93.438  1.00 65.96  ? 63  PRO A O   1 
ATOM   279   C  CB  . PRO A 1 62  ? 7.920   -9.937  91.148  1.00 53.60  ? 63  PRO A CB  1 
ATOM   280   C  CG  . PRO A 1 62  ? 9.170   -9.175  90.896  1.00 48.49  ? 63  PRO A CG  1 
ATOM   281   C  CD  . PRO A 1 62  ? 9.958   -9.250  92.172  1.00 48.86  ? 63  PRO A CD  1 
ATOM   282   N  N   . GLN A 1 63  ? 5.718   -10.802 93.665  1.00 70.86  ? 64  GLN A N   1 
ATOM   283   C  CA  . GLN A 1 63  ? 5.100   -11.871 94.431  1.00 77.25  ? 64  GLN A CA  1 
ATOM   284   C  C   . GLN A 1 63  ? 4.879   -13.110 93.572  1.00 78.44  ? 64  GLN A C   1 
ATOM   285   O  O   . GLN A 1 63  ? 4.239   -13.064 92.522  1.00 82.19  ? 64  GLN A O   1 
ATOM   286   C  CB  . GLN A 1 63  ? 3.789   -11.392 95.054  1.00 84.24  ? 64  GLN A CB  1 
ATOM   287   C  CG  . GLN A 1 63  ? 4.001   -10.677 96.383  1.00 89.54  ? 64  GLN A CG  1 
ATOM   288   C  CD  . GLN A 1 63  ? 2.882   -9.719  96.735  1.00 92.69  ? 64  GLN A CD  1 
ATOM   289   O  OE1 . GLN A 1 63  ? 1.868   -9.646  96.041  1.00 96.61  ? 64  GLN A OE1 1 
ATOM   290   N  NE2 . GLN A 1 63  ? 3.062   -8.976  97.822  1.00 92.35  ? 64  GLN A NE2 1 
ATOM   291   N  N   . GLY A 1 64  ? 5.431   -14.218 94.051  1.00 75.40  ? 65  GLY A N   1 
ATOM   292   C  CA  . GLY A 1 64  ? 5.425   -15.485 93.349  1.00 72.94  ? 65  GLY A CA  1 
ATOM   293   C  C   . GLY A 1 64  ? 6.149   -16.462 94.249  1.00 72.15  ? 65  GLY A C   1 
ATOM   294   O  O   . GLY A 1 64  ? 6.634   -16.073 95.310  1.00 69.90  ? 65  GLY A O   1 
ATOM   295   N  N   . TYR A 1 65  ? 6.237   -17.722 93.841  1.00 68.94  ? 66  TYR A N   1 
ATOM   296   C  CA  . TYR A 1 65  ? 6.831   -18.736 94.702  1.00 70.59  ? 66  TYR A CA  1 
ATOM   297   C  C   . TYR A 1 65  ? 8.317   -18.475 94.918  1.00 61.71  ? 66  TYR A C   1 
ATOM   298   O  O   . TYR A 1 65  ? 9.082   -18.315 93.966  1.00 60.41  ? 66  TYR A O   1 
ATOM   299   C  CB  . TYR A 1 65  ? 6.591   -20.127 94.120  1.00 64.02  ? 66  TYR A CB  1 
ATOM   300   C  CG  . TYR A 1 65  ? 5.151   -20.552 94.267  1.00 65.41  ? 66  TYR A CG  1 
ATOM   301   C  CD1 . TYR A 1 65  ? 4.618   -20.829 95.518  1.00 67.12  ? 66  TYR A CD1 1 
ATOM   302   C  CD2 . TYR A 1 65  ? 4.314   -20.640 93.163  1.00 66.95  ? 66  TYR A CD2 1 
ATOM   303   C  CE1 . TYR A 1 65  ? 3.299   -21.204 95.667  1.00 68.48  ? 66  TYR A CE1 1 
ATOM   304   C  CE2 . TYR A 1 65  ? 2.990   -21.012 93.301  1.00 69.41  ? 66  TYR A CE2 1 
ATOM   305   C  CZ  . TYR A 1 65  ? 2.489   -21.294 94.556  1.00 68.09  ? 66  TYR A CZ  1 
ATOM   306   O  OH  . TYR A 1 65  ? 1.173   -21.667 94.704  1.00 83.12  ? 66  TYR A OH  1 
ATOM   307   N  N   . THR A 1 66  ? 8.711   -18.433 96.187  1.00 62.56  ? 67  THR A N   1 
ATOM   308   C  CA  . THR A 1 66  ? 10.026  -17.938 96.568  1.00 67.60  ? 67  THR A CA  1 
ATOM   309   C  C   . THR A 1 66  ? 10.711  -18.787 97.632  1.00 69.18  ? 67  THR A C   1 
ATOM   310   O  O   . THR A 1 66  ? 10.058  -19.497 98.396  1.00 65.52  ? 67  THR A O   1 
ATOM   311   C  CB  . THR A 1 66  ? 9.932   -16.492 97.094  1.00 69.46  ? 67  THR A CB  1 
ATOM   312   O  OG1 . THR A 1 66  ? 11.215  -16.072 97.576  1.00 73.82  ? 67  THR A OG1 1 
ATOM   313   C  CG2 . THR A 1 66  ? 8.920   -16.406 98.227  1.00 61.84  ? 67  THR A CG2 1 
ATOM   314   N  N   . CYS A 1 67  ? 12.038  -18.712 97.663  1.00 68.82  ? 68  CYS A N   1 
ATOM   315   C  CA  . CYS A 1 67  ? 12.830  -19.343 98.711  1.00 64.64  ? 68  CYS A CA  1 
ATOM   316   C  C   . CYS A 1 67  ? 13.166  -18.355 99.823  1.00 64.70  ? 68  CYS A C   1 
ATOM   317   O  O   . CYS A 1 67  ? 13.891  -18.688 100.758 1.00 66.72  ? 68  CYS A O   1 
ATOM   318   C  CB  . CYS A 1 67  ? 14.114  -19.937 98.133  1.00 64.58  ? 68  CYS A CB  1 
ATOM   319   S  SG  . CYS A 1 67  ? 13.857  -21.452 97.193  1.00 110.62 ? 68  CYS A SG  1 
ATOM   320   N  N   . CYS A 1 68  ? 12.652  -17.135 99.707  1.00 64.88  ? 69  CYS A N   1 
ATOM   321   C  CA  . CYS A 1 68  ? 12.971  -16.080 100.663 1.00 64.63  ? 69  CYS A CA  1 
ATOM   322   C  C   . CYS A 1 68  ? 11.836  -15.802 101.643 1.00 71.78  ? 69  CYS A C   1 
ATOM   323   O  O   . CYS A 1 68  ? 10.669  -15.737 101.256 1.00 72.50  ? 69  CYS A O   1 
ATOM   324   C  CB  . CYS A 1 68  ? 13.332  -14.788 99.924  1.00 59.98  ? 69  CYS A CB  1 
ATOM   325   S  SG  . CYS A 1 68  ? 14.934  -14.818 99.090  1.00 81.47  ? 69  CYS A SG  1 
ATOM   326   N  N   . THR A 1 69  ? 12.190  -15.639 102.914 1.00 74.60  ? 70  THR A N   1 
ATOM   327   C  CA  . THR A 1 69  ? 11.239  -15.188 103.921 1.00 78.88  ? 70  THR A CA  1 
ATOM   328   C  C   . THR A 1 69  ? 11.387  -13.682 104.101 1.00 77.48  ? 70  THR A C   1 
ATOM   329   O  O   . THR A 1 69  ? 12.207  -13.053 103.432 1.00 78.73  ? 70  THR A O   1 
ATOM   330   C  CB  . THR A 1 69  ? 11.442  -15.903 105.272 1.00 75.91  ? 70  THR A CB  1 
ATOM   331   O  OG1 . THR A 1 69  ? 12.727  -15.568 105.810 1.00 68.08  ? 70  THR A OG1 1 
ATOM   332   C  CG2 . THR A 1 69  ? 11.339  -17.412 105.100 1.00 74.69  ? 70  THR A CG2 1 
ATOM   333   N  N   . SER A 1 70  ? 10.591  -13.106 104.997 1.00 81.56  ? 71  SER A N   1 
ATOM   334   C  CA  . SER A 1 70  ? 10.646  -11.672 105.264 1.00 84.16  ? 71  SER A CA  1 
ATOM   335   C  C   . SER A 1 70  ? 12.030  -11.256 105.757 1.00 78.94  ? 71  SER A C   1 
ATOM   336   O  O   . SER A 1 70  ? 12.622  -10.298 105.251 1.00 77.60  ? 71  SER A O   1 
ATOM   337   C  CB  . SER A 1 70  ? 9.579   -11.278 106.288 1.00 94.66  ? 71  SER A CB  1 
ATOM   338   O  OG  . SER A 1 70  ? 9.524   -9.872  106.455 1.00 99.53  ? 71  SER A OG  1 
ATOM   339   N  N   . GLU A 1 71  ? 12.538  -11.992 106.742 1.00 76.39  ? 72  GLU A N   1 
ATOM   340   C  CA  . GLU A 1 71  ? 13.869  -11.751 107.284 1.00 78.95  ? 72  GLU A CA  1 
ATOM   341   C  C   . GLU A 1 71  ? 14.929  -11.871 106.193 1.00 76.84  ? 72  GLU A C   1 
ATOM   342   O  O   . GLU A 1 71  ? 15.863  -11.069 106.130 1.00 76.25  ? 72  GLU A O   1 
ATOM   343   C  CB  . GLU A 1 71  ? 14.169  -12.728 108.423 1.00 78.95  ? 72  GLU A CB  1 
ATOM   344   C  CG  . GLU A 1 71  ? 13.294  -12.532 109.653 1.00 82.59  ? 72  GLU A CG  1 
ATOM   345   C  CD  . GLU A 1 71  ? 13.321  -13.728 110.588 1.00 87.65  ? 72  GLU A CD  1 
ATOM   346   O  OE1 . GLU A 1 71  ? 14.354  -14.428 110.629 1.00 88.74  ? 72  GLU A OE1 1 
ATOM   347   O  OE2 . GLU A 1 71  ? 12.312  -13.965 111.286 1.00 88.84  ? 72  GLU A OE2 1 
ATOM   348   N  N   . MET A 1 72  ? 14.771  -12.872 105.332 1.00 75.90  ? 73  MET A N   1 
ATOM   349   C  CA  . MET A 1 72  ? 15.687  -13.079 104.217 1.00 70.68  ? 73  MET A CA  1 
ATOM   350   C  C   . MET A 1 72  ? 15.669  -11.902 103.249 1.00 63.62  ? 73  MET A C   1 
ATOM   351   O  O   . MET A 1 72  ? 16.720  -11.389 102.866 1.00 61.72  ? 73  MET A O   1 
ATOM   352   C  CB  . MET A 1 72  ? 15.345  -14.369 103.468 1.00 71.71  ? 73  MET A CB  1 
ATOM   353   C  CG  . MET A 1 72  ? 15.604  -15.641 104.255 1.00 76.65  ? 73  MET A CG  1 
ATOM   354   S  SD  . MET A 1 72  ? 15.250  -17.121 103.289 1.00 67.67  ? 73  MET A SD  1 
ATOM   355   C  CE  . MET A 1 72  ? 16.386  -16.907 101.920 1.00 63.67  ? 73  MET A CE  1 
ATOM   356   N  N   . GLU A 1 73  ? 14.469  -11.482 102.859 1.00 58.59  ? 74  GLU A N   1 
ATOM   357   C  CA  . GLU A 1 73  ? 14.305  -10.380 101.918 1.00 62.43  ? 74  GLU A CA  1 
ATOM   358   C  C   . GLU A 1 73  ? 14.914  -9.095  102.470 1.00 61.15  ? 74  GLU A C   1 
ATOM   359   O  O   . GLU A 1 73  ? 15.659  -8.399  101.773 1.00 66.37  ? 74  GLU A O   1 
ATOM   360   C  CB  . GLU A 1 73  ? 12.823  -10.167 101.593 1.00 56.47  ? 74  GLU A CB  1 
ATOM   361   C  CG  . GLU A 1 73  ? 12.568  -9.527  100.234 1.00 54.47  ? 74  GLU A CG  1 
ATOM   362   C  CD  . GLU A 1 73  ? 11.140  -9.037  100.076 1.00 54.61  ? 74  GLU A CD  1 
ATOM   363   O  OE1 . GLU A 1 73  ? 10.478  -8.787  101.105 1.00 64.79  ? 74  GLU A OE1 1 
ATOM   364   O  OE2 . GLU A 1 73  ? 10.678  -8.905  98.923  1.00 53.58  ? 74  GLU A OE2 1 
ATOM   365   N  N   . GLU A 1 74  ? 14.600  -8.792  103.727 1.00 61.99  ? 75  GLU A N   1 
ATOM   366   C  CA  . GLU A 1 74  ? 15.137  -7.606  104.387 1.00 63.40  ? 75  GLU A CA  1 
ATOM   367   C  C   . GLU A 1 74  ? 16.663  -7.650  104.463 1.00 62.00  ? 75  GLU A C   1 
ATOM   368   O  O   . GLU A 1 74  ? 17.342  -6.681  104.102 1.00 61.71  ? 75  GLU A O   1 
ATOM   369   C  CB  . GLU A 1 74  ? 14.544  -7.460  105.790 1.00 70.64  ? 75  GLU A CB  1 
ATOM   370   C  CG  . GLU A 1 74  ? 13.080  -7.047  105.805 1.00 76.27  ? 75  GLU A CG  1 
ATOM   371   C  CD  . GLU A 1 74  ? 12.507  -6.976  107.208 1.00 85.13  ? 75  GLU A CD  1 
ATOM   372   O  OE1 . GLU A 1 74  ? 13.141  -7.514  108.140 1.00 88.89  ? 75  GLU A OE1 1 
ATOM   373   O  OE2 . GLU A 1 74  ? 11.424  -6.377  107.380 1.00 85.49  ? 75  GLU A OE2 1 
ATOM   374   N  N   . ASN A 1 75  ? 17.193  -8.779  104.928 1.00 61.79  ? 76  ASN A N   1 
ATOM   375   C  CA  . ASN A 1 75  ? 18.636  -8.967  105.042 1.00 61.68  ? 76  ASN A CA  1 
ATOM   376   C  C   . ASN A 1 75  ? 19.358  -8.779  103.710 1.00 63.07  ? 76  ASN A C   1 
ATOM   377   O  O   . ASN A 1 75  ? 20.368  -8.075  103.633 1.00 61.11  ? 76  ASN A O   1 
ATOM   378   C  CB  . ASN A 1 75  ? 18.947  -10.354 105.607 1.00 63.63  ? 76  ASN A CB  1 
ATOM   379   C  CG  . ASN A 1 75  ? 18.747  -10.431 107.109 1.00 67.79  ? 76  ASN A CG  1 
ATOM   380   O  OD1 . ASN A 1 75  ? 18.922  -9.443  107.822 1.00 72.74  ? 76  ASN A OD1 1 
ATOM   381   N  ND2 . ASN A 1 75  ? 18.383  -11.611 107.599 1.00 68.31  ? 76  ASN A ND2 1 
ATOM   382   N  N   . LEU A 1 76  ? 18.833  -9.408  102.664 1.00 62.56  ? 77  LEU A N   1 
ATOM   383   C  CA  . LEU A 1 76  ? 19.421  -9.299  101.334 1.00 61.05  ? 77  LEU A CA  1 
ATOM   384   C  C   . LEU A 1 76  ? 19.321  -7.873  100.796 1.00 57.41  ? 77  LEU A C   1 
ATOM   385   O  O   . LEU A 1 76  ? 20.219  -7.403  100.093 1.00 56.07  ? 77  LEU A O   1 
ATOM   386   C  CB  . LEU A 1 76  ? 18.750  -10.280 100.371 1.00 57.23  ? 77  LEU A CB  1 
ATOM   387   C  CG  . LEU A 1 76  ? 19.075  -11.756 100.608 1.00 58.18  ? 77  LEU A CG  1 
ATOM   388   C  CD1 . LEU A 1 76  ? 18.263  -12.644 99.678  1.00 55.16  ? 77  LEU A CD1 1 
ATOM   389   C  CD2 . LEU A 1 76  ? 20.565  -12.012 100.432 1.00 54.61  ? 77  LEU A CD2 1 
ATOM   390   N  N   . ALA A 1 77  ? 18.229  -7.189  101.131 1.00 58.72  ? 78  ALA A N   1 
ATOM   391   C  CA  . ALA A 1 77  ? 18.064  -5.787  100.756 1.00 56.78  ? 78  ALA A CA  1 
ATOM   392   C  C   . ALA A 1 77  ? 19.168  -4.933  101.378 1.00 60.54  ? 78  ALA A C   1 
ATOM   393   O  O   . ALA A 1 77  ? 19.879  -4.200  100.674 1.00 57.35  ? 78  ALA A O   1 
ATOM   394   C  CB  . ALA A 1 77  ? 16.695  -5.281  101.178 1.00 59.55  ? 78  ALA A CB  1 
ATOM   395   N  N   . ASN A 1 78  ? 19.303  -5.039  102.700 1.00 61.05  ? 79  ASN A N   1 
ATOM   396   C  CA  . ASN A 1 78  ? 20.377  -4.372  103.430 1.00 59.99  ? 79  ASN A CA  1 
ATOM   397   C  C   . ASN A 1 78  ? 21.740  -4.660  102.812 1.00 62.80  ? 79  ASN A C   1 
ATOM   398   O  O   . ASN A 1 78  ? 22.562  -3.754  102.625 1.00 61.09  ? 79  ASN A O   1 
ATOM   399   C  CB  . ASN A 1 78  ? 20.374  -4.806  104.898 1.00 65.95  ? 79  ASN A CB  1 
ATOM   400   C  CG  . ASN A 1 78  ? 19.728  -3.782  105.811 1.00 67.22  ? 79  ASN A CG  1 
ATOM   401   O  OD1 . ASN A 1 78  ? 18.507  -3.629  105.828 1.00 68.61  ? 79  ASN A OD1 1 
ATOM   402   N  ND2 . ASN A 1 78  ? 20.549  -3.081  106.586 1.00 66.94  ? 79  ASN A ND2 1 
ATOM   403   N  N   . ARG A 1 79  ? 21.963  -5.930  102.485 1.00 61.73  ? 80  ARG A N   1 
ATOM   404   C  CA  . ARG A 1 79  ? 23.222  -6.364  101.894 1.00 63.56  ? 80  ARG A CA  1 
ATOM   405   C  C   . ARG A 1 79  ? 23.508  -5.657  100.573 1.00 58.66  ? 80  ARG A C   1 
ATOM   406   O  O   . ARG A 1 79  ? 24.552  -5.025  100.418 1.00 56.49  ? 80  ARG A O   1 
ATOM   407   C  CB  . ARG A 1 79  ? 23.221  -7.877  101.680 1.00 70.13  ? 80  ARG A CB  1 
ATOM   408   C  CG  . ARG A 1 79  ? 24.525  -8.402  101.111 1.00 74.17  ? 80  ARG A CG  1 
ATOM   409   C  CD  . ARG A 1 79  ? 25.687  -8.006  102.006 1.00 79.38  ? 80  ARG A CD  1 
ATOM   410   N  NE  . ARG A 1 79  ? 25.506  -8.492  103.370 1.00 86.34  ? 80  ARG A NE  1 
ATOM   411   C  CZ  . ARG A 1 79  ? 25.870  -9.701  103.780 1.00 93.34  ? 80  ARG A CZ  1 
ATOM   412   N  NH1 . ARG A 1 79  ? 26.447  -10.538 102.930 1.00 93.61  ? 80  ARG A NH1 1 
ATOM   413   N  NH2 . ARG A 1 79  ? 25.669  -10.070 105.037 1.00 96.17  ? 80  ARG A NH2 1 
ATOM   414   N  N   . SER A 1 80  ? 22.578  -5.766  99.629  1.00 57.28  ? 81  SER A N   1 
ATOM   415   C  CA  . SER A 1 80  ? 22.750  -5.159  98.311  1.00 53.91  ? 81  SER A CA  1 
ATOM   416   C  C   . SER A 1 80  ? 22.937  -3.644  98.403  1.00 49.46  ? 81  SER A C   1 
ATOM   417   O  O   . SER A 1 80  ? 23.773  -3.064  97.695  1.00 47.40  ? 81  SER A O   1 
ATOM   418   C  CB  . SER A 1 80  ? 21.554  -5.491  97.414  1.00 47.68  ? 81  SER A CB  1 
ATOM   419   O  OG  . SER A 1 80  ? 20.332  -5.158  98.046  1.00 46.22  ? 81  SER A OG  1 
ATOM   420   N  N   . HIS A 1 81  ? 22.165  -3.011  99.284  1.00 50.54  ? 82  HIS A N   1 
ATOM   421   C  CA  . HIS A 1 81  ? 22.285  -1.573  99.509  1.00 45.99  ? 82  HIS A CA  1 
ATOM   422   C  C   . HIS A 1 81  ? 23.691  -1.198  99.984  1.00 48.40  ? 82  HIS A C   1 
ATOM   423   O  O   . HIS A 1 81  ? 24.352  -0.321  99.402  1.00 45.25  ? 82  HIS A O   1 
ATOM   424   C  CB  . HIS A 1 81  ? 21.241  -1.107  100.525 1.00 48.01  ? 82  HIS A CB  1 
ATOM   425   C  CG  . HIS A 1 81  ? 21.360  0.338   100.897 1.00 58.06  ? 82  HIS A CG  1 
ATOM   426   N  ND1 . HIS A 1 81  ? 22.120  0.772   101.961 1.00 59.09  ? 82  HIS A ND1 1 
ATOM   427   C  CD2 . HIS A 1 81  ? 20.814  1.448   100.346 1.00 60.38  ? 82  HIS A CD2 1 
ATOM   428   C  CE1 . HIS A 1 81  ? 22.036  2.087   102.050 1.00 60.69  ? 82  HIS A CE1 1 
ATOM   429   N  NE2 . HIS A 1 81  ? 21.251  2.522   101.082 1.00 60.97  ? 82  HIS A NE2 1 
ATOM   430   N  N   . ALA A 1 82  ? 24.143  -1.876  101.037 1.00 47.10  ? 83  ALA A N   1 
ATOM   431   C  CA  . ALA A 1 82  ? 25.478  -1.653  101.583 1.00 49.88  ? 83  ALA A CA  1 
ATOM   432   C  C   . ALA A 1 82  ? 26.555  -1.866  100.521 1.00 52.34  ? 83  ALA A C   1 
ATOM   433   O  O   . ALA A 1 82  ? 27.546  -1.132  100.467 1.00 52.36  ? 83  ALA A O   1 
ATOM   434   C  CB  . ALA A 1 82  ? 25.721  -2.567  102.773 1.00 51.40  ? 83  ALA A CB  1 
ATOM   435   N  N   . GLU A 1 83  ? 26.347  -2.870  99.675  1.00 49.36  ? 84  GLU A N   1 
ATOM   436   C  CA  . GLU A 1 83  ? 27.289  -3.188  98.608  1.00 46.91  ? 84  GLU A CA  1 
ATOM   437   C  C   . GLU A 1 83  ? 27.378  -2.051  97.588  1.00 49.12  ? 84  GLU A C   1 
ATOM   438   O  O   . GLU A 1 83  ? 28.480  -1.630  97.204  1.00 54.06  ? 84  GLU A O   1 
ATOM   439   C  CB  . GLU A 1 83  ? 26.890  -4.502  97.929  1.00 47.47  ? 84  GLU A CB  1 
ATOM   440   C  CG  . GLU A 1 83  ? 27.164  -5.734  98.788  1.00 51.15  ? 84  GLU A CG  1 
ATOM   441   C  CD  . GLU A 1 83  ? 26.433  -6.975  98.305  1.00 58.67  ? 84  GLU A CD  1 
ATOM   442   O  OE1 . GLU A 1 83  ? 25.472  -6.841  97.518  1.00 57.87  ? 84  GLU A OE1 1 
ATOM   443   O  OE2 . GLU A 1 83  ? 26.819  -8.089  98.718  1.00 57.04  ? 84  GLU A OE2 1 
ATOM   444   N  N   . LEU A 1 84  ? 26.221  -1.548  97.160  1.00 42.82  ? 85  LEU A N   1 
ATOM   445   C  CA  . LEU A 1 84  ? 26.193  -0.402  96.252  1.00 43.48  ? 85  LEU A CA  1 
ATOM   446   C  C   . LEU A 1 84  ? 26.896  0.806   96.874  1.00 44.30  ? 85  LEU A C   1 
ATOM   447   O  O   . LEU A 1 84  ? 27.669  1.502   96.199  1.00 41.53  ? 85  LEU A O   1 
ATOM   448   C  CB  . LEU A 1 84  ? 24.755  -0.037  95.875  1.00 43.11  ? 85  LEU A CB  1 
ATOM   449   C  CG  . LEU A 1 84  ? 24.609  1.214   95.004  1.00 45.49  ? 85  LEU A CG  1 
ATOM   450   C  CD1 . LEU A 1 84  ? 25.416  1.084   93.722  1.00 46.67  ? 85  LEU A CD1 1 
ATOM   451   C  CD2 . LEU A 1 84  ? 23.150  1.488   94.686  1.00 47.62  ? 85  LEU A CD2 1 
ATOM   452   N  N   . GLU A 1 85  ? 26.632  1.045   98.158  1.00 48.93  ? 86  GLU A N   1 
ATOM   453   C  CA  . GLU A 1 85  ? 27.312  2.118   98.884  1.00 43.67  ? 86  GLU A CA  1 
ATOM   454   C  C   . GLU A 1 85  ? 28.832  1.963   98.825  1.00 52.49  ? 86  GLU A C   1 
ATOM   455   O  O   . GLU A 1 85  ? 29.559  2.920   98.523  1.00 57.78  ? 86  GLU A O   1 
ATOM   456   C  CB  . GLU A 1 85  ? 26.854  2.159   100.343 1.00 47.37  ? 86  GLU A CB  1 
ATOM   457   C  CG  . GLU A 1 85  ? 25.556  2.915   100.570 1.00 56.10  ? 86  GLU A CG  1 
ATOM   458   C  CD  . GLU A 1 85  ? 25.266  3.140   102.042 1.00 68.34  ? 86  GLU A CD  1 
ATOM   459   O  OE1 . GLU A 1 85  ? 25.938  2.507   102.885 1.00 71.52  ? 86  GLU A OE1 1 
ATOM   460   O  OE2 . GLU A 1 85  ? 24.375  3.956   102.356 1.00 70.86  ? 86  GLU A OE2 1 
ATOM   461   N  N   . THR A 1 86  ? 29.301  0.750   99.110  1.00 50.28  ? 87  THR A N   1 
ATOM   462   C  CA  . THR A 1 86  ? 30.728  0.448   99.100  1.00 49.86  ? 87  THR A CA  1 
ATOM   463   C  C   . THR A 1 86  ? 31.345  0.719   97.732  1.00 44.57  ? 87  THR A C   1 
ATOM   464   O  O   . THR A 1 86  ? 32.386  1.380   97.631  1.00 49.30  ? 87  THR A O   1 
ATOM   465   C  CB  . THR A 1 86  ? 30.992  -1.019  99.499  1.00 50.34  ? 87  THR A CB  1 
ATOM   466   O  OG1 . THR A 1 86  ? 30.683  -1.201  100.886 1.00 55.35  ? 87  THR A OG1 1 
ATOM   467   C  CG2 . THR A 1 86  ? 32.450  -1.386  99.266  1.00 45.64  ? 87  THR A CG2 1 
ATOM   468   N  N   . ALA A 1 87  ? 30.698  0.216   96.682  1.00 36.98  ? 88  ALA A N   1 
ATOM   469   C  CA  . ALA A 1 87  ? 31.177  0.447   95.320  1.00 43.30  ? 88  ALA A CA  1 
ATOM   470   C  C   . ALA A 1 87  ? 31.293  1.944   95.020  1.00 44.91  ? 88  ALA A C   1 
ATOM   471   O  O   . ALA A 1 87  ? 32.358  2.441   94.599  1.00 43.87  ? 88  ALA A O   1 
ATOM   472   C  CB  . ALA A 1 87  ? 30.255  -0.224  94.317  1.00 35.90  ? 88  ALA A CB  1 
ATOM   473   N  N   . LEU A 1 88  ? 30.193  2.655   95.261  1.00 44.64  ? 89  LEU A N   1 
ATOM   474   C  CA  . LEU A 1 88  ? 30.125  4.089   95.000  1.00 44.15  ? 89  LEU A CA  1 
ATOM   475   C  C   . LEU A 1 88  ? 31.246  4.853   95.704  1.00 40.75  ? 89  LEU A C   1 
ATOM   476   O  O   . LEU A 1 88  ? 32.006  5.597   95.065  1.00 33.21  ? 89  LEU A O   1 
ATOM   477   C  CB  . LEU A 1 88  ? 28.764  4.641   95.431  1.00 47.12  ? 89  LEU A CB  1 
ATOM   478   C  CG  . LEU A 1 88  ? 28.455  6.081   95.015  1.00 53.88  ? 89  LEU A CG  1 
ATOM   479   C  CD1 . LEU A 1 88  ? 28.227  6.173   93.513  1.00 54.03  ? 89  LEU A CD1 1 
ATOM   480   C  CD2 . LEU A 1 88  ? 27.256  6.623   95.778  1.00 53.82  ? 89  LEU A CD2 1 
ATOM   481   N  N   . ARG A 1 89  ? 31.364  4.657   97.016  1.00 47.45  ? 90  ARG A N   1 
ATOM   482   C  CA  . ARG A 1 89  ? 32.355  5.405   97.781  1.00 54.63  ? 90  ARG A CA  1 
ATOM   483   C  C   . ARG A 1 89  ? 33.779  4.971   97.439  1.00 57.49  ? 90  ARG A C   1 
ATOM   484   O  O   . ARG A 1 89  ? 34.726  5.734   97.633  1.00 60.10  ? 90  ARG A O   1 
ATOM   485   C  CB  . ARG A 1 89  ? 32.115  5.266   99.285  1.00 63.58  ? 90  ARG A CB  1 
ATOM   486   C  CG  . ARG A 1 89  ? 32.683  6.437   100.080 1.00 72.56  ? 90  ARG A CG  1 
ATOM   487   C  CD  . ARG A 1 89  ? 32.704  6.175   101.574 1.00 80.30  ? 90  ARG A CD  1 
ATOM   488   N  NE  . ARG A 1 89  ? 31.684  5.217   101.982 1.00 87.22  ? 90  ARG A NE  1 
ATOM   489   C  CZ  . ARG A 1 89  ? 30.631  5.521   102.735 1.00 92.57  ? 90  ARG A CZ  1 
ATOM   490   N  NH1 . ARG A 1 89  ? 30.454  6.764   103.163 1.00 94.72  ? 90  ARG A NH1 1 
ATOM   491   N  NH2 . ARG A 1 89  ? 29.754  4.581   103.058 1.00 93.34  ? 90  ARG A NH2 1 
ATOM   492   N  N   . ASP A 1 90  ? 33.932  3.752   96.929  1.00 57.00  ? 91  ASP A N   1 
ATOM   493   C  CA  . ASP A 1 90  ? 35.236  3.309   96.438  1.00 54.26  ? 91  ASP A CA  1 
ATOM   494   C  C   . ASP A 1 90  ? 35.641  4.099   95.196  1.00 52.97  ? 91  ASP A C   1 
ATOM   495   O  O   . ASP A 1 90  ? 36.747  4.663   95.134  1.00 53.47  ? 91  ASP A O   1 
ATOM   496   C  CB  . ASP A 1 90  ? 35.226  1.809   96.128  1.00 61.18  ? 91  ASP A CB  1 
ATOM   497   C  CG  . ASP A 1 90  ? 35.534  0.959   97.347  1.00 65.00  ? 91  ASP A CG  1 
ATOM   498   O  OD1 . ASP A 1 90  ? 35.418  1.471   98.481  1.00 66.74  ? 91  ASP A OD1 1 
ATOM   499   O  OD2 . ASP A 1 90  ? 35.903  -0.221  97.170  1.00 68.97  ? 91  ASP A OD2 1 
ATOM   500   N  N   . SER A 1 91  ? 34.743  4.145   94.213  1.00 46.36  ? 92  SER A N   1 
ATOM   501   C  CA  . SER A 1 91  ? 35.005  4.916   92.995  1.00 48.69  ? 92  SER A CA  1 
ATOM   502   C  C   . SER A 1 91  ? 35.309  6.383   93.332  1.00 33.22  ? 92  SER A C   1 
ATOM   503   O  O   . SER A 1 91  ? 36.310  6.975   92.859  1.00 29.48  ? 92  SER A O   1 
ATOM   504   C  CB  . SER A 1 91  ? 33.812  4.819   92.041  1.00 45.48  ? 92  SER A CB  1 
ATOM   505   O  OG  . SER A 1 91  ? 34.198  5.097   90.706  1.00 50.91  ? 92  SER A OG  1 
ATOM   506   N  N   . SER A 1 92  ? 34.447  6.954   94.173  1.00 32.89  ? 93  SER A N   1 
ATOM   507   C  CA  . SER A 1 92  ? 34.638  8.313   94.662  1.00 42.11  ? 93  SER A CA  1 
ATOM   508   C  C   . SER A 1 92  ? 36.013  8.485   95.302  1.00 43.63  ? 93  SER A C   1 
ATOM   509   O  O   . SER A 1 92  ? 36.682  9.492   95.083  1.00 34.58  ? 93  SER A O   1 
ATOM   510   C  CB  . SER A 1 92  ? 33.549  8.683   95.669  1.00 40.55  ? 93  SER A CB  1 
ATOM   511   O  OG  . SER A 1 92  ? 33.794  9.963   96.225  1.00 47.59  ? 93  SER A OG  1 
ATOM   512   N  N   . ARG A 1 93  ? 36.431  7.495   96.083  1.00 47.34  ? 94  ARG A N   1 
ATOM   513   C  CA  . ARG A 1 93  ? 37.729  7.545   96.750  1.00 47.75  ? 94  ARG A CA  1 
ATOM   514   C  C   . ARG A 1 93  ? 38.873  7.569   95.744  1.00 45.59  ? 94  ARG A C   1 
ATOM   515   O  O   . ARG A 1 93  ? 39.852  8.303   95.921  1.00 44.68  ? 94  ARG A O   1 
ATOM   516   C  CB  . ARG A 1 93  ? 37.888  6.361   97.703  1.00 51.08  ? 94  ARG A CB  1 
ATOM   517   C  CG  . ARG A 1 93  ? 37.703  6.731   99.163  1.00 60.14  ? 94  ARG A CG  1 
ATOM   518   C  CD  . ARG A 1 93  ? 37.485  5.506   100.035 1.00 69.95  ? 94  ARG A CD  1 
ATOM   519   N  NE  . ARG A 1 93  ? 37.180  5.882   101.413 1.00 76.80  ? 94  ARG A NE  1 
ATOM   520   C  CZ  . ARG A 1 93  ? 36.803  5.028   102.358 1.00 86.06  ? 94  ARG A CZ  1 
ATOM   521   N  NH1 . ARG A 1 93  ? 36.676  3.738   102.079 1.00 86.05  ? 94  ARG A NH1 1 
ATOM   522   N  NH2 . ARG A 1 93  ? 36.549  5.466   103.584 1.00 88.25  ? 94  ARG A NH2 1 
ATOM   523   N  N   . VAL A 1 94  ? 38.748  6.768   94.688  1.00 39.96  ? 95  VAL A N   1 
ATOM   524   C  CA  . VAL A 1 94  ? 39.732  6.801   93.609  1.00 38.16  ? 95  VAL A CA  1 
ATOM   525   C  C   . VAL A 1 94  ? 39.837  8.207   93.005  1.00 42.75  ? 95  VAL A C   1 
ATOM   526   O  O   . VAL A 1 94  ? 40.938  8.800   92.944  1.00 42.96  ? 95  VAL A O   1 
ATOM   527   C  CB  . VAL A 1 94  ? 39.386  5.788   92.500  1.00 35.45  ? 95  VAL A CB  1 
ATOM   528   C  CG1 . VAL A 1 94  ? 40.258  6.014   91.273  1.00 29.98  ? 95  VAL A CG1 1 
ATOM   529   C  CG2 . VAL A 1 94  ? 39.540  4.365   93.016  1.00 32.99  ? 95  VAL A CG2 1 
ATOM   530   N  N   . LEU A 1 95  ? 38.693  8.748   92.580  1.00 40.72  ? 96  LEU A N   1 
ATOM   531   C  CA  . LEU A 1 95  ? 38.692  10.081  91.963  1.00 36.86  ? 96  LEU A CA  1 
ATOM   532   C  C   . LEU A 1 95  ? 39.308  11.145  92.883  1.00 34.04  ? 96  LEU A C   1 
ATOM   533   O  O   . LEU A 1 95  ? 40.157  11.951  92.465  1.00 38.08  ? 96  LEU A O   1 
ATOM   534   C  CB  . LEU A 1 95  ? 37.269  10.488  91.577  1.00 38.63  ? 96  LEU A CB  1 
ATOM   535   C  CG  . LEU A 1 95  ? 37.113  11.875  90.949  1.00 33.59  ? 96  LEU A CG  1 
ATOM   536   C  CD1 . LEU A 1 95  ? 37.954  11.993  89.689  1.00 34.53  ? 96  LEU A CD1 1 
ATOM   537   C  CD2 . LEU A 1 95  ? 35.654  12.159  90.643  1.00 31.25  ? 96  LEU A CD2 1 
ATOM   538   N  N   . GLN A 1 96  ? 38.878  11.120  94.140  1.00 39.02  ? 97  GLN A N   1 
ATOM   539   C  CA  . GLN A 1 96  ? 39.339  12.050  95.164  1.00 39.48  ? 97  GLN A CA  1 
ATOM   540   C  C   . GLN A 1 96  ? 40.849  11.963  95.353  1.00 40.76  ? 97  GLN A C   1 
ATOM   541   O  O   . GLN A 1 96  ? 41.530  12.986  95.471  1.00 45.36  ? 97  GLN A O   1 
ATOM   542   C  CB  . GLN A 1 96  ? 38.623  11.764  96.486  1.00 46.09  ? 97  GLN A CB  1 
ATOM   543   C  CG  . GLN A 1 96  ? 38.478  12.960  97.407  1.00 55.53  ? 97  GLN A CG  1 
ATOM   544   C  CD  . GLN A 1 96  ? 37.681  12.631  98.655  1.00 63.20  ? 97  GLN A CD  1 
ATOM   545   O  OE1 . GLN A 1 96  ? 36.738  11.840  98.611  1.00 63.20  ? 97  GLN A OE1 1 
ATOM   546   N  NE2 . GLN A 1 96  ? 38.054  13.239  99.776  1.00 67.82  ? 97  GLN A NE2 1 
ATOM   547   N  N   . ALA A 1 97  ? 41.364  10.737  95.380  1.00 40.90  ? 98  ALA A N   1 
ATOM   548   C  CA  . ALA A 1 97  ? 42.801  10.515  95.485  1.00 38.40  ? 98  ALA A CA  1 
ATOM   549   C  C   . ALA A 1 97  ? 43.527  11.155  94.307  1.00 36.93  ? 98  ALA A C   1 
ATOM   550   O  O   . ALA A 1 97  ? 44.527  11.868  94.492  1.00 33.13  ? 98  ALA A O   1 
ATOM   551   C  CB  . ALA A 1 97  ? 43.109  9.026   95.554  1.00 35.97  ? 98  ALA A CB  1 
ATOM   552   N  N   . MET A 1 98  ? 43.015  10.910  93.101  1.00 30.31  ? 99  MET A N   1 
ATOM   553   C  CA  . MET A 1 98  ? 43.617  11.497  91.901  1.00 35.95  ? 99  MET A CA  1 
ATOM   554   C  C   . MET A 1 98  ? 43.694  13.026  91.999  1.00 35.00  ? 99  MET A C   1 
ATOM   555   O  O   . MET A 1 98  ? 44.779  13.626  91.860  1.00 34.62  ? 99  MET A O   1 
ATOM   556   C  CB  . MET A 1 98  ? 42.831  11.084  90.653  1.00 31.13  ? 99  MET A CB  1 
ATOM   557   C  CG  . MET A 1 98  ? 43.507  11.429  89.327  1.00 33.87  ? 99  MET A CG  1 
ATOM   558   S  SD  . MET A 1 98  ? 43.222  13.122  88.757  1.00 48.46  ? 99  MET A SD  1 
ATOM   559   C  CE  . MET A 1 98  ? 41.482  13.056  88.346  1.00 40.39  ? 99  MET A CE  1 
ATOM   560   N  N   . LEU A 1 99  ? 42.545  13.651  92.251  1.00 33.75  ? 100 LEU A N   1 
ATOM   561   C  CA  . LEU A 1 99  ? 42.487  15.109  92.353  1.00 36.65  ? 100 LEU A CA  1 
ATOM   562   C  C   . LEU A 1 99  ? 43.420  15.647  93.440  1.00 38.39  ? 100 LEU A C   1 
ATOM   563   O  O   . LEU A 1 99  ? 44.073  16.677  93.255  1.00 33.24  ? 100 LEU A O   1 
ATOM   564   C  CB  . LEU A 1 99  ? 41.055  15.573  92.623  1.00 32.62  ? 100 LEU A CB  1 
ATOM   565   C  CG  . LEU A 1 99  ? 40.027  15.322  91.519  1.00 35.43  ? 100 LEU A CG  1 
ATOM   566   C  CD1 . LEU A 1 99  ? 38.638  15.714  91.995  1.00 30.92  ? 100 LEU A CD1 1 
ATOM   567   C  CD2 . LEU A 1 99  ? 40.396  16.078  90.250  1.00 24.16  ? 100 LEU A CD2 1 
ATOM   568   N  N   . ALA A 1 100 ? 43.484  14.942  94.566  1.00 39.69  ? 101 ALA A N   1 
ATOM   569   C  CA  . ALA A 1 100 ? 44.336  15.354  95.679  1.00 30.63  ? 101 ALA A CA  1 
ATOM   570   C  C   . ALA A 1 100 ? 45.813  15.338  95.290  1.00 38.43  ? 101 ALA A C   1 
ATOM   571   O  O   . ALA A 1 100 ? 46.547  16.306  95.545  1.00 37.48  ? 101 ALA A O   1 
ATOM   572   C  CB  . ALA A 1 100 ? 44.099  14.461  96.886  1.00 30.19  ? 101 ALA A CB  1 
ATOM   573   N  N   . THR A 1 101 ? 46.247  14.242  94.670  1.00 35.66  ? 102 THR A N   1 
ATOM   574   C  CA  . THR A 1 101 ? 47.639  14.144  94.237  1.00 37.33  ? 102 THR A CA  1 
ATOM   575   C  C   . THR A 1 101 ? 47.969  15.227  93.210  1.00 32.18  ? 102 THR A C   1 
ATOM   576   O  O   . THR A 1 101 ? 49.041  15.844  93.272  1.00 28.58  ? 102 THR A O   1 
ATOM   577   C  CB  . THR A 1 101 ? 47.967  12.759  93.642  1.00 33.39  ? 102 THR A CB  1 
ATOM   578   O  OG1 . THR A 1 101 ? 47.157  12.524  92.484  1.00 43.11  ? 102 THR A OG1 1 
ATOM   579   C  CG2 . THR A 1 101 ? 47.722  11.666  94.670  1.00 32.96  ? 102 THR A CG2 1 
ATOM   580   N  N   . GLN A 1 102 ? 47.047  15.466  92.278  1.00 32.43  ? 103 GLN A N   1 
ATOM   581   C  CA  . GLN A 1 102 ? 47.230  16.561  91.323  1.00 28.77  ? 103 GLN A CA  1 
ATOM   582   C  C   . GLN A 1 102 ? 47.433  17.899  92.038  1.00 39.67  ? 103 GLN A C   1 
ATOM   583   O  O   . GLN A 1 102 ? 48.370  18.652  91.733  1.00 35.18  ? 103 GLN A O   1 
ATOM   584   C  CB  . GLN A 1 102 ? 46.035  16.656  90.371  1.00 28.76  ? 103 GLN A CB  1 
ATOM   585   C  CG  . GLN A 1 102 ? 45.966  15.540  89.341  1.00 31.34  ? 103 GLN A CG  1 
ATOM   586   C  CD  . GLN A 1 102 ? 47.144  15.558  88.384  1.00 35.80  ? 103 GLN A CD  1 
ATOM   587   O  OE1 . GLN A 1 102 ? 47.730  16.608  88.120  1.00 34.89  ? 103 GLN A OE1 1 
ATOM   588   N  NE2 . GLN A 1 102 ? 47.497  14.390  87.858  1.00 36.40  ? 103 GLN A NE2 1 
ATOM   589   N  N   . LEU A 1 103 ? 46.554  18.176  92.997  1.00 34.23  ? 104 LEU A N   1 
ATOM   590   C  CA  . LEU A 1 103 ? 46.593  19.423  93.752  1.00 37.61  ? 104 LEU A CA  1 
ATOM   591   C  C   . LEU A 1 103 ? 47.936  19.616  94.453  1.00 34.35  ? 104 LEU A C   1 
ATOM   592   O  O   . LEU A 1 103 ? 48.591  20.658  94.295  1.00 38.28  ? 104 LEU A O   1 
ATOM   593   C  CB  . LEU A 1 103 ? 45.456  19.455  94.776  1.00 36.68  ? 104 LEU A CB  1 
ATOM   594   C  CG  . LEU A 1 103 ? 45.294  20.746  95.576  1.00 33.15  ? 104 LEU A CG  1 
ATOM   595   C  CD1 . LEU A 1 103 ? 45.238  21.925  94.632  1.00 35.55  ? 104 LEU A CD1 1 
ATOM   596   C  CD2 . LEU A 1 103 ? 44.039  20.689  96.429  1.00 31.99  ? 104 LEU A CD2 1 
ATOM   597   N  N   . ARG A 1 104 ? 48.338  18.604  95.219  1.00 33.80  ? 105 ARG A N   1 
ATOM   598   C  CA  . ARG A 1 104 ? 49.623  18.635  95.912  1.00 34.47  ? 105 ARG A CA  1 
ATOM   599   C  C   . ARG A 1 104 ? 50.767  18.885  94.934  1.00 33.02  ? 105 ARG A C   1 
ATOM   600   O  O   . ARG A 1 104 ? 51.602  19.768  95.154  1.00 25.83  ? 105 ARG A O   1 
ATOM   601   C  CB  . ARG A 1 104 ? 49.858  17.329  96.672  1.00 27.12  ? 105 ARG A CB  1 
ATOM   602   N  N   . SER A 1 105 ? 50.782  18.119  93.845  1.00 25.82  ? 106 SER A N   1 
ATOM   603   C  CA  . SER A 1 105 ? 51.828  18.242  92.833  1.00 38.22  ? 106 SER A CA  1 
ATOM   604   C  C   . SER A 1 105 ? 51.949  19.663  92.283  1.00 34.34  ? 106 SER A C   1 
ATOM   605   O  O   . SER A 1 105 ? 53.036  20.247  92.295  1.00 33.83  ? 106 SER A O   1 
ATOM   606   C  CB  . SER A 1 105 ? 51.574  17.263  91.684  1.00 31.62  ? 106 SER A CB  1 
ATOM   607   O  OG  . SER A 1 105 ? 51.743  15.923  92.112  1.00 39.82  ? 106 SER A OG  1 
ATOM   608   N  N   . PHE A 1 106 ? 50.837  20.222  91.813  1.00 27.50  ? 107 PHE A N   1 
ATOM   609   C  CA  . PHE A 1 106 ? 50.879  21.548  91.200  1.00 31.80  ? 107 PHE A CA  1 
ATOM   610   C  C   . PHE A 1 106 ? 51.198  22.658  92.199  1.00 27.10  ? 107 PHE A C   1 
ATOM   611   O  O   . PHE A 1 106 ? 52.019  23.534  91.911  1.00 28.66  ? 107 PHE A O   1 
ATOM   612   C  CB  . PHE A 1 106 ? 49.562  21.853  90.487  1.00 23.45  ? 107 PHE A CB  1 
ATOM   613   C  CG  . PHE A 1 106 ? 49.499  21.312  89.089  1.00 29.09  ? 107 PHE A CG  1 
ATOM   614   C  CD1 . PHE A 1 106 ? 49.058  20.019  88.849  1.00 23.69  ? 107 PHE A CD1 1 
ATOM   615   C  CD2 . PHE A 1 106 ? 49.894  22.093  88.014  1.00 23.29  ? 107 PHE A CD2 1 
ATOM   616   C  CE1 . PHE A 1 106 ? 49.004  19.518  87.562  1.00 23.80  ? 107 PHE A CE1 1 
ATOM   617   C  CE2 . PHE A 1 106 ? 49.844  21.598  86.724  1.00 23.45  ? 107 PHE A CE2 1 
ATOM   618   C  CZ  . PHE A 1 106 ? 49.397  20.307  86.498  1.00 23.70  ? 107 PHE A CZ  1 
ATOM   619   N  N   . ASP A 1 107 ? 50.555  22.625  93.365  1.00 28.62  ? 108 ASP A N   1 
ATOM   620   C  CA  . ASP A 1 107 ? 50.819  23.636  94.388  1.00 30.89  ? 108 ASP A CA  1 
ATOM   621   C  C   . ASP A 1 107 ? 52.302  23.628  94.768  1.00 38.35  ? 108 ASP A C   1 
ATOM   622   O  O   . ASP A 1 107 ? 53.001  24.661  94.694  1.00 38.93  ? 108 ASP A O   1 
ATOM   623   C  CB  . ASP A 1 107 ? 49.947  23.390  95.622  1.00 26.40  ? 108 ASP A CB  1 
ATOM   624   C  CG  . ASP A 1 107 ? 49.981  24.547  96.602  1.00 35.60  ? 108 ASP A CG  1 
ATOM   625   O  OD1 . ASP A 1 107 ? 49.937  25.711  96.148  1.00 37.82  ? 108 ASP A OD1 1 
ATOM   626   O  OD2 . ASP A 1 107 ? 50.047  24.295  97.823  1.00 38.01  ? 108 ASP A OD2 1 
ATOM   627   N  N   . ASP A 1 108 ? 52.775  22.442  95.147  1.00 33.68  ? 109 ASP A N   1 
ATOM   628   C  CA  . ASP A 1 108 ? 54.167  22.251  95.531  1.00 37.72  ? 109 ASP A CA  1 
ATOM   629   C  C   . ASP A 1 108 ? 55.129  22.675  94.431  1.00 32.97  ? 109 ASP A C   1 
ATOM   630   O  O   . ASP A 1 108 ? 56.181  23.240  94.719  1.00 35.37  ? 109 ASP A O   1 
ATOM   631   C  CB  . ASP A 1 108 ? 54.429  20.789  95.905  1.00 39.09  ? 109 ASP A CB  1 
ATOM   632   C  CG  . ASP A 1 108 ? 53.934  20.443  97.296  1.00 42.11  ? 109 ASP A CG  1 
ATOM   633   O  OD1 . ASP A 1 108 ? 53.160  21.238  97.871  1.00 47.27  ? 109 ASP A OD1 1 
ATOM   634   O  OD2 . ASP A 1 108 ? 54.319  19.373  97.814  1.00 46.81  ? 109 ASP A OD2 1 
ATOM   635   N  N   . HIS A 1 109 ? 54.778  22.410  93.175  1.00 25.21  ? 110 HIS A N   1 
ATOM   636   C  CA  . HIS A 1 109 ? 55.694  22.735  92.086  1.00 30.55  ? 110 HIS A CA  1 
ATOM   637   C  C   . HIS A 1 109 ? 55.728  24.229  91.776  1.00 35.84  ? 110 HIS A C   1 
ATOM   638   O  O   . HIS A 1 109 ? 56.777  24.759  91.422  1.00 30.38  ? 110 HIS A O   1 
ATOM   639   C  CB  . HIS A 1 109 ? 55.347  21.966  90.815  1.00 25.13  ? 110 HIS A CB  1 
ATOM   640   C  CG  . HIS A 1 109 ? 56.292  22.237  89.686  1.00 35.56  ? 110 HIS A CG  1 
ATOM   641   N  ND1 . HIS A 1 109 ? 57.641  21.966  89.768  1.00 30.68  ? 110 HIS A ND1 1 
ATOM   642   C  CD2 . HIS A 1 109 ? 56.091  22.773  88.459  1.00 34.87  ? 110 HIS A CD2 1 
ATOM   643   C  CE1 . HIS A 1 109 ? 58.229  22.316  88.639  1.00 36.83  ? 110 HIS A CE1 1 
ATOM   644   N  NE2 . HIS A 1 109 ? 57.310  22.807  87.826  1.00 39.43  ? 110 HIS A NE2 1 
ATOM   645   N  N   . PHE A 1 110 ? 54.590  24.905  91.889  1.00 30.40  ? 111 PHE A N   1 
ATOM   646   C  CA  . PHE A 1 110 ? 54.568  26.353  91.697  1.00 32.28  ? 111 PHE A CA  1 
ATOM   647   C  C   . PHE A 1 110 ? 55.395  27.024  92.793  1.00 37.43  ? 111 PHE A C   1 
ATOM   648   O  O   . PHE A 1 110 ? 56.281  27.868  92.519  1.00 35.31  ? 111 PHE A O   1 
ATOM   649   C  CB  . PHE A 1 110 ? 53.130  26.878  91.696  1.00 23.52  ? 111 PHE A CB  1 
ATOM   650   C  CG  . PHE A 1 110 ? 52.381  26.586  90.425  1.00 27.42  ? 111 PHE A CG  1 
ATOM   651   C  CD1 . PHE A 1 110 ? 52.997  26.737  89.193  1.00 31.50  ? 111 PHE A CD1 1 
ATOM   652   C  CD2 . PHE A 1 110 ? 51.068  26.146  90.462  1.00 24.62  ? 111 PHE A CD2 1 
ATOM   653   C  CE1 . PHE A 1 110 ? 52.313  26.468  88.021  1.00 23.15  ? 111 PHE A CE1 1 
ATOM   654   C  CE2 . PHE A 1 110 ? 50.380  25.869  89.294  1.00 22.85  ? 111 PHE A CE2 1 
ATOM   655   C  CZ  . PHE A 1 110 ? 51.003  26.030  88.072  1.00 22.92  ? 111 PHE A CZ  1 
ATOM   656   N  N   . GLN A 1 111 ? 55.117  26.624  94.033  1.00 24.54  ? 112 GLN A N   1 
ATOM   657   C  CA  . GLN A 1 111 ? 55.867  27.149  95.169  1.00 35.64  ? 112 GLN A CA  1 
ATOM   658   C  C   . GLN A 1 111 ? 57.368  26.876  95.022  1.00 40.60  ? 112 GLN A C   1 
ATOM   659   O  O   . GLN A 1 111 ? 58.194  27.743  95.321  1.00 38.53  ? 112 GLN A O   1 
ATOM   660   C  CB  . GLN A 1 111 ? 55.335  26.559  96.475  1.00 34.66  ? 112 GLN A CB  1 
ATOM   661   C  CG  . GLN A 1 111 ? 53.994  27.144  96.896  1.00 38.31  ? 112 GLN A CG  1 
ATOM   662   C  CD  . GLN A 1 111 ? 53.490  26.576  98.206  1.00 50.32  ? 112 GLN A CD  1 
ATOM   663   O  OE1 . GLN A 1 111 ? 52.366  26.082  98.291  1.00 50.58  ? 112 GLN A OE1 1 
ATOM   664   N  NE2 . GLN A 1 111 ? 54.322  26.644  99.239  1.00 51.47  ? 112 GLN A NE2 1 
ATOM   665   N  N   . HIS A 1 112 ? 57.717  25.684  94.539  1.00 34.13  ? 113 HIS A N   1 
ATOM   666   C  CA  A HIS A 1 112 ? 59.120  25.340  94.346  0.59 35.31  ? 113 HIS A CA  1 
ATOM   667   C  CA  B HIS A 1 112 ? 59.112  25.312  94.323  0.41 35.77  ? 113 HIS A CA  1 
ATOM   668   C  C   . HIS A 1 112 ? 59.758  26.155  93.232  1.00 35.80  ? 113 HIS A C   1 
ATOM   669   O  O   . HIS A 1 112 ? 60.915  26.522  93.330  1.00 33.97  ? 113 HIS A O   1 
ATOM   670   C  CB  A HIS A 1 112 ? 59.300  23.856  94.035  0.59 26.76  ? 113 HIS A CB  1 
ATOM   671   C  CB  B HIS A 1 112 ? 59.229  23.831  93.956  0.41 26.71  ? 113 HIS A CB  1 
ATOM   672   C  CG  A HIS A 1 112 ? 60.668  23.520  93.528  0.59 30.05  ? 113 HIS A CG  1 
ATOM   673   C  CG  B HIS A 1 112 ? 59.259  22.913  95.138  0.41 30.95  ? 113 HIS A CG  1 
ATOM   674   N  ND1 A HIS A 1 112 ? 60.941  23.338  92.189  0.59 34.04  ? 113 HIS A ND1 1 
ATOM   675   N  ND1 B HIS A 1 112 ? 58.563  21.724  95.175  0.41 27.61  ? 113 HIS A ND1 1 
ATOM   676   C  CD2 A HIS A 1 112 ? 61.846  23.366  94.177  0.59 34.41  ? 113 HIS A CD2 1 
ATOM   677   C  CD2 B HIS A 1 112 ? 59.912  23.004  96.321  0.41 32.11  ? 113 HIS A CD2 1 
ATOM   678   C  CE1 A HIS A 1 112 ? 62.226  23.069  92.037  0.59 36.41  ? 113 HIS A CE1 1 
ATOM   679   C  CE1 B HIS A 1 112 ? 58.779  21.126  96.333  0.41 28.42  ? 113 HIS A CE1 1 
ATOM   680   N  NE2 A HIS A 1 112 ? 62.798  23.082  93.227  0.59 36.37  ? 113 HIS A NE2 1 
ATOM   681   N  NE2 B HIS A 1 112 ? 59.594  21.882  97.047  0.41 31.91  ? 113 HIS A NE2 1 
ATOM   682   N  N   . LEU A 1 113 ? 59.006  26.428  92.172  1.00 32.95  ? 114 LEU A N   1 
ATOM   683   C  CA  . LEU A 1 113 ? 59.531  27.233  91.078  1.00 32.25  ? 114 LEU A CA  1 
ATOM   684   C  C   . LEU A 1 113 ? 59.863  28.624  91.590  1.00 36.43  ? 114 LEU A C   1 
ATOM   685   O  O   . LEU A 1 113 ? 60.963  29.140  91.348  1.00 36.61  ? 114 LEU A O   1 
ATOM   686   C  CB  . LEU A 1 113 ? 58.536  27.311  89.919  1.00 31.70  ? 114 LEU A CB  1 
ATOM   687   C  CG  . LEU A 1 113 ? 58.484  26.098  88.986  1.00 34.11  ? 114 LEU A CG  1 
ATOM   688   C  CD1 . LEU A 1 113 ? 57.370  26.259  87.963  1.00 35.60  ? 114 LEU A CD1 1 
ATOM   689   C  CD2 . LEU A 1 113 ? 59.826  25.889  88.294  1.00 25.83  ? 114 LEU A CD2 1 
ATOM   690   N  N   . LEU A 1 114 ? 58.920  29.218  92.320  1.00 29.78  ? 115 LEU A N   1 
ATOM   691   C  CA  . LEU A 1 114 ? 59.153  30.551  92.876  1.00 36.79  ? 115 LEU A CA  1 
ATOM   692   C  C   . LEU A 1 114 ? 60.356  30.564  93.833  1.00 37.13  ? 115 LEU A C   1 
ATOM   693   O  O   . LEU A 1 114 ? 61.284  31.381  93.690  1.00 32.72  ? 115 LEU A O   1 
ATOM   694   C  CB  . LEU A 1 114 ? 57.898  31.053  93.594  1.00 32.89  ? 115 LEU A CB  1 
ATOM   695   C  CG  . LEU A 1 114 ? 57.877  32.538  93.956  1.00 39.14  ? 115 LEU A CG  1 
ATOM   696   C  CD1 . LEU A 1 114 ? 58.123  33.386  92.718  1.00 38.76  ? 115 LEU A CD1 1 
ATOM   697   C  CD2 . LEU A 1 114 ? 56.555  32.915  94.609  1.00 41.73  ? 115 LEU A CD2 1 
ATOM   698   N  N   . ASN A 1 115 ? 60.338  29.643  94.794  1.00 31.90  ? 116 ASN A N   1 
ATOM   699   C  CA  . ASN A 1 115 ? 61.402  29.532  95.790  1.00 36.89  ? 116 ASN A CA  1 
ATOM   700   C  C   . ASN A 1 115 ? 62.785  29.323  95.168  1.00 39.61  ? 116 ASN A C   1 
ATOM   701   O  O   . ASN A 1 115 ? 63.777  29.909  95.609  1.00 33.94  ? 116 ASN A O   1 
ATOM   702   C  CB  . ASN A 1 115 ? 61.088  28.386  96.758  1.00 37.27  ? 116 ASN A CB  1 
ATOM   703   C  CG  . ASN A 1 115 ? 59.963  28.726  97.723  1.00 44.31  ? 116 ASN A CG  1 
ATOM   704   O  OD1 . ASN A 1 115 ? 59.261  29.722  97.551  1.00 40.79  ? 116 ASN A OD1 1 
ATOM   705   N  ND2 . ASN A 1 115 ? 59.788  27.893  98.745  1.00 49.49  ? 116 ASN A ND2 1 
ATOM   706   N  N   . ASP A 1 116 ? 62.833  28.488  94.138  1.00 36.89  ? 117 ASP A N   1 
ATOM   707   C  CA  . ASP A 1 116 ? 64.068  28.159  93.437  1.00 32.95  ? 117 ASP A CA  1 
ATOM   708   C  C   . ASP A 1 116 ? 64.556  29.361  92.649  1.00 37.68  ? 117 ASP A C   1 
ATOM   709   O  O   . ASP A 1 116 ? 65.760  29.590  92.532  1.00 35.97  ? 117 ASP A O   1 
ATOM   710   C  CB  . ASP A 1 116 ? 63.858  26.965  92.504  1.00 40.13  ? 117 ASP A CB  1 
ATOM   711   C  CG  . ASP A 1 116 ? 65.129  26.175  92.268  1.00 53.98  ? 117 ASP A CG  1 
ATOM   712   O  OD1 . ASP A 1 116 ? 65.453  25.309  93.108  1.00 56.35  ? 117 ASP A OD1 1 
ATOM   713   O  OD2 . ASP A 1 116 ? 65.801  26.417  91.242  1.00 59.05  ? 117 ASP A OD2 1 
ATOM   714   N  N   . SER A 1 117 ? 63.615  30.120  92.096  1.00 36.21  ? 118 SER A N   1 
ATOM   715   C  CA  . SER A 1 117 ? 63.963  31.372  91.438  1.00 33.95  ? 118 SER A CA  1 
ATOM   716   C  C   . SER A 1 117 ? 64.639  32.299  92.443  1.00 32.24  ? 118 SER A C   1 
ATOM   717   O  O   . SER A 1 117 ? 65.697  32.878  92.162  1.00 27.69  ? 118 SER A O   1 
ATOM   718   C  CB  . SER A 1 117 ? 62.724  32.037  90.837  1.00 33.83  ? 118 SER A CB  1 
ATOM   719   O  OG  . SER A 1 117 ? 63.090  33.051  89.917  1.00 37.79  ? 118 SER A OG  1 
ATOM   720   N  N   . GLU A 1 118 ? 64.036  32.416  93.624  1.00 33.82  ? 119 GLU A N   1 
ATOM   721   C  CA  . GLU A 1 118 ? 64.593  33.279  94.664  1.00 33.08  ? 119 GLU A CA  1 
ATOM   722   C  C   . GLU A 1 118 ? 65.991  32.829  95.106  1.00 34.06  ? 119 GLU A C   1 
ATOM   723   O  O   . GLU A 1 118 ? 66.893  33.655  95.263  1.00 35.92  ? 119 GLU A O   1 
ATOM   724   C  CB  . GLU A 1 118 ? 63.658  33.338  95.874  1.00 31.39  ? 119 GLU A CB  1 
ATOM   725   C  CG  . GLU A 1 118 ? 63.985  34.468  96.842  1.00 30.96  ? 119 GLU A CG  1 
ATOM   726   C  CD  . GLU A 1 118 ? 63.068  34.496  98.049  1.00 42.96  ? 119 GLU A CD  1 
ATOM   727   O  OE1 . GLU A 1 118 ? 62.186  33.616  98.150  1.00 45.48  ? 119 GLU A OE1 1 
ATOM   728   O  OE2 . GLU A 1 118 ? 63.225  35.403  98.894  1.00 44.22  ? 119 GLU A OE2 1 
ATOM   729   N  N   . ARG A 1 119 ? 66.170  31.525  95.301  1.00 36.49  ? 120 ARG A N   1 
ATOM   730   C  CA  . ARG A 1 119 ? 67.465  30.988  95.716  1.00 36.68  ? 120 ARG A CA  1 
ATOM   731   C  C   . ARG A 1 119 ? 68.530  31.204  94.645  1.00 34.92  ? 120 ARG A C   1 
ATOM   732   O  O   . ARG A 1 119 ? 69.677  31.544  94.951  1.00 34.58  ? 120 ARG A O   1 
ATOM   733   C  CB  . ARG A 1 119 ? 67.353  29.499  96.047  1.00 38.06  ? 120 ARG A CB  1 
ATOM   734   C  CG  . ARG A 1 119 ? 66.783  29.212  97.426  1.00 48.70  ? 120 ARG A CG  1 
ATOM   735   C  CD  . ARG A 1 119 ? 66.854  27.730  97.761  1.00 54.54  ? 120 ARG A CD  1 
ATOM   736   N  NE  . ARG A 1 119 ? 65.569  27.210  98.220  1.00 60.50  ? 120 ARG A NE  1 
ATOM   737   C  CZ  . ARG A 1 119 ? 64.736  26.503  97.464  1.00 63.18  ? 120 ARG A CZ  1 
ATOM   738   N  NH1 . ARG A 1 119 ? 65.052  26.223  96.206  1.00 64.15  ? 120 ARG A NH1 1 
ATOM   739   N  NH2 . ARG A 1 119 ? 63.587  26.071  97.966  1.00 63.51  ? 120 ARG A NH2 1 
ATOM   740   N  N   . THR A 1 120 ? 68.142  31.002  93.390  1.00 33.76  ? 121 THR A N   1 
ATOM   741   C  CA  . THR A 1 120 ? 69.036  31.232  92.262  1.00 37.62  ? 121 THR A CA  1 
ATOM   742   C  C   . THR A 1 120 ? 69.475  32.690  92.222  1.00 42.99  ? 121 THR A C   1 
ATOM   743   O  O   . THR A 1 120 ? 70.653  32.993  92.005  1.00 49.00  ? 121 THR A O   1 
ATOM   744   C  CB  . THR A 1 120 ? 68.372  30.856  90.924  1.00 34.00  ? 121 THR A CB  1 
ATOM   745   O  OG1 . THR A 1 120 ? 67.875  29.514  90.995  1.00 41.27  ? 121 THR A OG1 1 
ATOM   746   C  CG2 . THR A 1 120 ? 69.369  30.967  89.779  1.00 30.15  ? 121 THR A CG2 1 
ATOM   747   N  N   . LEU A 1 121 ? 68.519  33.590  92.442  1.00 40.71  ? 122 LEU A N   1 
ATOM   748   C  CA  . LEU A 1 121 ? 68.825  35.012  92.506  1.00 40.58  ? 122 LEU A CA  1 
ATOM   749   C  C   . LEU A 1 121 ? 69.827  35.298  93.622  1.00 39.40  ? 122 LEU A C   1 
ATOM   750   O  O   . LEU A 1 121 ? 70.867  35.910  93.386  1.00 37.09  ? 122 LEU A O   1 
ATOM   751   C  CB  . LEU A 1 121 ? 67.548  35.832  92.712  1.00 41.92  ? 122 LEU A CB  1 
ATOM   752   C  CG  . LEU A 1 121 ? 67.710  37.348  92.865  1.00 40.12  ? 122 LEU A CG  1 
ATOM   753   C  CD1 . LEU A 1 121 ? 66.591  38.070  92.136  1.00 44.03  ? 122 LEU A CD1 1 
ATOM   754   C  CD2 . LEU A 1 121 ? 67.728  37.756  94.331  1.00 38.41  ? 122 LEU A CD2 1 
ATOM   755   N  N   . GLN A 1 122 ? 69.509  34.847  94.833  1.00 36.64  ? 123 GLN A N   1 
ATOM   756   C  CA  . GLN A 1 122 ? 70.370  35.082  95.990  1.00 35.35  ? 123 GLN A CA  1 
ATOM   757   C  C   . GLN A 1 122 ? 71.778  34.528  95.793  1.00 43.51  ? 123 GLN A C   1 
ATOM   758   O  O   . GLN A 1 122 ? 72.747  35.078  96.315  1.00 48.14  ? 123 GLN A O   1 
ATOM   759   C  CB  . GLN A 1 122 ? 69.755  34.470  97.249  1.00 34.12  ? 123 GLN A CB  1 
ATOM   760   C  CG  . GLN A 1 122 ? 68.504  35.170  97.741  1.00 47.30  ? 123 GLN A CG  1 
ATOM   761   C  CD  . GLN A 1 122 ? 67.942  34.529  98.994  1.00 54.11  ? 123 GLN A CD  1 
ATOM   762   O  OE1 . GLN A 1 122 ? 67.112  35.117  99.687  1.00 57.52  ? 123 GLN A OE1 1 
ATOM   763   N  NE2 . GLN A 1 122 ? 68.394  33.317  99.293  1.00 58.09  ? 123 GLN A NE2 1 
ATOM   764   N  N   . ALA A 1 123 ? 71.888  33.442  95.037  1.00 45.05  ? 124 ALA A N   1 
ATOM   765   C  CA  . ALA A 1 123 ? 73.178  32.792  94.843  1.00 50.70  ? 124 ALA A CA  1 
ATOM   766   C  C   . ALA A 1 123 ? 74.009  33.433  93.729  1.00 33.14  ? 124 ALA A C   1 
ATOM   767   O  O   . ALA A 1 123 ? 75.233  33.516  93.836  1.00 34.11  ? 124 ALA A O   1 
ATOM   768   C  CB  . ALA A 1 123 ? 72.978  31.315  94.558  1.00 32.97  ? 124 ALA A CB  1 
ATOM   769   N  N   . THR A 1 124 ? 73.350  33.885  92.665  1.00 41.82  ? 125 THR A N   1 
ATOM   770   C  CA  . THR A 1 124 ? 74.077  34.354  91.485  1.00 32.92  ? 125 THR A CA  1 
ATOM   771   C  C   . THR A 1 124 ? 74.248  35.874  91.410  1.00 43.20  ? 125 THR A C   1 
ATOM   772   O  O   . THR A 1 124 ? 75.246  36.360  90.879  1.00 33.62  ? 125 THR A O   1 
ATOM   773   C  CB  . THR A 1 124 ? 73.386  33.887  90.192  1.00 32.53  ? 125 THR A CB  1 
ATOM   774   O  OG1 . THR A 1 124 ? 72.061  34.429  90.133  1.00 31.48  ? 125 THR A OG1 1 
ATOM   775   C  CG2 . THR A 1 124 ? 73.313  32.369  90.148  1.00 41.14  ? 125 THR A CG2 1 
ATOM   776   N  N   . PHE A 1 125 ? 73.277  36.617  91.934  1.00 42.41  ? 126 PHE A N   1 
ATOM   777   C  CA  . PHE A 1 125 ? 73.290  38.080  91.841  1.00 36.43  ? 126 PHE A CA  1 
ATOM   778   C  C   . PHE A 1 125 ? 74.496  38.794  92.480  1.00 40.30  ? 126 PHE A C   1 
ATOM   779   O  O   . PHE A 1 125 ? 75.000  39.753  91.897  1.00 39.63  ? 126 PHE A O   1 
ATOM   780   C  CB  . PHE A 1 125 ? 72.000  38.652  92.438  1.00 32.67  ? 126 PHE A CB  1 
ATOM   781   C  CG  . PHE A 1 125 ? 70.897  38.833  91.433  1.00 40.28  ? 126 PHE A CG  1 
ATOM   782   C  CD1 . PHE A 1 125 ? 70.653  37.867  90.470  1.00 41.60  ? 126 PHE A CD1 1 
ATOM   783   C  CD2 . PHE A 1 125 ? 70.105  39.970  91.450  1.00 39.11  ? 126 PHE A CD2 1 
ATOM   784   C  CE1 . PHE A 1 125 ? 69.641  38.032  89.542  1.00 42.62  ? 126 PHE A CE1 1 
ATOM   785   C  CE2 . PHE A 1 125 ? 69.091  40.140  90.525  1.00 41.92  ? 126 PHE A CE2 1 
ATOM   786   C  CZ  . PHE A 1 125 ? 68.858  39.169  89.570  1.00 40.24  ? 126 PHE A CZ  1 
ATOM   787   N  N   . PRO A 1 126 ? 74.955  38.357  93.673  1.00 43.17  ? 127 PRO A N   1 
ATOM   788   C  CA  . PRO A 1 126 ? 76.111  39.067  94.241  1.00 45.39  ? 127 PRO A CA  1 
ATOM   789   C  C   . PRO A 1 126 ? 77.346  39.047  93.342  1.00 46.82  ? 127 PRO A C   1 
ATOM   790   O  O   . PRO A 1 126 ? 78.103  40.015  93.326  1.00 51.99  ? 127 PRO A O   1 
ATOM   791   C  CB  . PRO A 1 126 ? 76.385  38.312  95.550  1.00 41.90  ? 127 PRO A CB  1 
ATOM   792   C  CG  . PRO A 1 126 ? 75.648  37.016  95.425  1.00 43.43  ? 127 PRO A CG  1 
ATOM   793   C  CD  . PRO A 1 126 ? 74.447  37.334  94.603  1.00 41.68  ? 127 PRO A CD  1 
ATOM   794   N  N   . GLY A 1 127 ? 77.538  37.965  92.596  1.00 52.97  ? 128 GLY A N   1 
ATOM   795   C  CA  . GLY A 1 127 ? 78.658  37.874  91.679  1.00 54.95  ? 128 GLY A CA  1 
ATOM   796   C  C   . GLY A 1 127 ? 78.484  38.763  90.461  1.00 57.02  ? 128 GLY A C   1 
ATOM   797   O  O   . GLY A 1 127 ? 79.430  39.409  90.010  1.00 61.82  ? 128 GLY A O   1 
ATOM   798   N  N   . ALA A 1 128 ? 77.264  38.804  89.937  1.00 54.29  ? 129 ALA A N   1 
ATOM   799   C  CA  . ALA A 1 128 ? 76.983  39.505  88.689  1.00 56.19  ? 129 ALA A CA  1 
ATOM   800   C  C   . ALA A 1 128 ? 76.860  41.016  88.863  1.00 53.51  ? 129 ALA A C   1 
ATOM   801   O  O   . ALA A 1 128 ? 77.150  41.774  87.938  1.00 56.19  ? 129 ALA A O   1 
ATOM   802   C  CB  . ALA A 1 128 ? 75.710  38.952  88.059  1.00 49.06  ? 129 ALA A CB  1 
ATOM   803   N  N   . PHE A 1 129 ? 76.431  41.455  90.043  1.00 49.59  ? 130 PHE A N   1 
ATOM   804   C  CA  . PHE A 1 129 ? 76.104  42.863  90.247  1.00 51.45  ? 130 PHE A CA  1 
ATOM   805   C  C   . PHE A 1 129 ? 76.737  43.463  91.502  1.00 53.41  ? 130 PHE A C   1 
ATOM   806   O  O   . PHE A 1 129 ? 76.861  44.683  91.615  1.00 55.08  ? 130 PHE A O   1 
ATOM   807   C  CB  . PHE A 1 129 ? 74.585  43.038  90.302  1.00 44.19  ? 130 PHE A CB  1 
ATOM   808   C  CG  . PHE A 1 129 ? 73.863  42.422  89.138  1.00 43.03  ? 130 PHE A CG  1 
ATOM   809   C  CD1 . PHE A 1 129 ? 74.106  42.858  87.846  1.00 40.75  ? 130 PHE A CD1 1 
ATOM   810   C  CD2 . PHE A 1 129 ? 72.940  41.408  89.336  1.00 37.96  ? 130 PHE A CD2 1 
ATOM   811   C  CE1 . PHE A 1 129 ? 73.444  42.292  86.772  1.00 42.81  ? 130 PHE A CE1 1 
ATOM   812   C  CE2 . PHE A 1 129 ? 72.274  40.840  88.267  1.00 34.97  ? 130 PHE A CE2 1 
ATOM   813   C  CZ  . PHE A 1 129 ? 72.526  41.283  86.983  1.00 37.43  ? 130 PHE A CZ  1 
ATOM   814   N  N   . GLY A 1 130 ? 77.128  42.611  92.446  1.00 55.06  ? 131 GLY A N   1 
ATOM   815   C  CA  . GLY A 1 130 ? 77.797  43.068  93.652  1.00 53.48  ? 131 GLY A CA  1 
ATOM   816   C  C   . GLY A 1 130 ? 76.950  43.916  94.586  1.00 54.20  ? 131 GLY A C   1 
ATOM   817   O  O   . GLY A 1 130 ? 75.856  43.516  94.998  1.00 50.33  ? 131 GLY A O   1 
ATOM   818   N  N   . GLU A 1 131 ? 77.470  45.094  94.922  1.00 48.57  ? 132 GLU A N   1 
ATOM   819   C  CA  . GLU A 1 131 ? 76.813  46.001  95.859  1.00 49.52  ? 132 GLU A CA  1 
ATOM   820   C  C   . GLU A 1 131 ? 75.462  46.477  95.335  1.00 43.20  ? 132 GLU A C   1 
ATOM   821   O  O   . GLU A 1 131 ? 74.590  46.865  96.115  1.00 44.43  ? 132 GLU A O   1 
ATOM   822   C  CB  . GLU A 1 131 ? 77.712  47.202  96.159  1.00 47.33  ? 132 GLU A CB  1 
ATOM   823   N  N   . LEU A 1 132 ? 75.302  46.452  94.015  1.00 35.04  ? 133 LEU A N   1 
ATOM   824   C  CA  . LEU A 1 132 ? 74.030  46.788  93.388  1.00 39.66  ? 133 LEU A CA  1 
ATOM   825   C  C   . LEU A 1 132 ? 72.914  45.905  93.931  1.00 45.64  ? 133 LEU A C   1 
ATOM   826   O  O   . LEU A 1 132 ? 71.823  46.384  94.241  1.00 48.69  ? 133 LEU A O   1 
ATOM   827   C  CB  . LEU A 1 132 ? 74.115  46.642  91.869  1.00 34.44  ? 133 LEU A CB  1 
ATOM   828   C  CG  . LEU A 1 132 ? 74.693  47.811  91.074  1.00 42.78  ? 133 LEU A CG  1 
ATOM   829   C  CD1 . LEU A 1 132 ? 74.357  47.656  89.602  1.00 46.26  ? 133 LEU A CD1 1 
ATOM   830   C  CD2 . LEU A 1 132 ? 74.183  49.139  91.609  1.00 44.91  ? 133 LEU A CD2 1 
ATOM   831   N  N   . TYR A 1 133 ? 73.196  44.611  94.047  1.00 41.37  ? 134 TYR A N   1 
ATOM   832   C  CA  . TYR A 1 133 ? 72.220  43.680  94.594  1.00 41.31  ? 134 TYR A CA  1 
ATOM   833   C  C   . TYR A 1 133 ? 72.269  43.623  96.115  1.00 42.00  ? 134 TYR A C   1 
ATOM   834   O  O   . TYR A 1 133 ? 71.236  43.742  96.774  1.00 40.52  ? 134 TYR A O   1 
ATOM   835   C  CB  . TYR A 1 133 ? 72.424  42.268  94.040  1.00 41.39  ? 134 TYR A CB  1 
ATOM   836   C  CG  . TYR A 1 133 ? 71.772  41.224  94.919  1.00 44.42  ? 134 TYR A CG  1 
ATOM   837   C  CD1 . TYR A 1 133 ? 70.390  41.100  94.969  1.00 44.30  ? 134 TYR A CD1 1 
ATOM   838   C  CD2 . TYR A 1 133 ? 72.535  40.383  95.720  1.00 41.68  ? 134 TYR A CD2 1 
ATOM   839   C  CE1 . TYR A 1 133 ? 69.786  40.164  95.781  1.00 40.09  ? 134 TYR A CE1 1 
ATOM   840   C  CE2 . TYR A 1 133 ? 71.937  39.441  96.536  1.00 43.23  ? 134 TYR A CE2 1 
ATOM   841   C  CZ  . TYR A 1 133 ? 70.562  39.336  96.560  1.00 40.36  ? 134 TYR A CZ  1 
ATOM   842   O  OH  . TYR A 1 133 ? 69.957  38.401  97.368  1.00 43.03  ? 134 TYR A OH  1 
ATOM   843   N  N   . THR A 1 134 ? 73.466  43.428  96.665  1.00 33.50  ? 135 THR A N   1 
ATOM   844   C  CA  . THR A 1 134 ? 73.611  43.125  98.090  1.00 51.04  ? 135 THR A CA  1 
ATOM   845   C  C   . THR A 1 134 ? 73.049  44.212  99.008  1.00 48.43  ? 135 THR A C   1 
ATOM   846   O  O   . THR A 1 134 ? 72.639  43.926  100.132 1.00 53.22  ? 135 THR A O   1 
ATOM   847   C  CB  . THR A 1 134 ? 75.086  42.886  98.469  1.00 49.81  ? 135 THR A CB  1 
ATOM   848   O  OG1 . THR A 1 134 ? 75.864  44.039  98.131  1.00 50.99  ? 135 THR A OG1 1 
ATOM   849   C  CG2 . THR A 1 134 ? 75.638  41.672  97.734  1.00 34.76  ? 135 THR A CG2 1 
ATOM   850   N  N   . GLN A 1 135 ? 73.025  45.452  98.530  1.00 49.82  ? 136 GLN A N   1 
ATOM   851   C  CA  . GLN A 1 135 ? 72.488  46.555  99.322  1.00 53.10  ? 136 GLN A CA  1 
ATOM   852   C  C   . GLN A 1 135 ? 71.025  46.830  98.991  1.00 50.56  ? 136 GLN A C   1 
ATOM   853   O  O   . GLN A 1 135 ? 70.447  47.815  99.450  1.00 47.69  ? 136 GLN A O   1 
ATOM   854   C  CB  . GLN A 1 135 ? 73.321  47.821  99.115  1.00 62.78  ? 136 GLN A CB  1 
ATOM   855   C  CG  . GLN A 1 135 ? 74.740  47.704  99.640  1.00 73.77  ? 136 GLN A CG  1 
ATOM   856   C  CD  . GLN A 1 135 ? 74.785  47.517  101.145 1.00 82.19  ? 136 GLN A CD  1 
ATOM   857   O  OE1 . GLN A 1 135 ? 74.948  46.400  101.638 1.00 84.49  ? 136 GLN A OE1 1 
ATOM   858   N  NE2 . GLN A 1 135 ? 74.637  48.611  101.883 1.00 84.73  ? 136 GLN A NE2 1 
ATOM   859   N  N   . ASN A 1 136 ? 70.431  45.947  98.195  1.00 49.16  ? 137 ASN A N   1 
ATOM   860   C  CA  . ASN A 1 136 ? 69.022  46.053  97.841  1.00 47.58  ? 137 ASN A CA  1 
ATOM   861   C  C   . ASN A 1 136 ? 68.343  44.692  97.907  1.00 40.63  ? 137 ASN A C   1 
ATOM   862   O  O   . ASN A 1 136 ? 67.272  44.494  97.336  1.00 36.75  ? 137 ASN A O   1 
ATOM   863   C  CB  . ASN A 1 136 ? 68.865  46.653  96.443  1.00 48.57  ? 137 ASN A CB  1 
ATOM   864   C  CG  . ASN A 1 136 ? 69.460  48.043  96.335  1.00 48.16  ? 137 ASN A CG  1 
ATOM   865   O  OD1 . ASN A 1 136 ? 69.164  48.923  97.143  1.00 48.28  ? 137 ASN A OD1 1 
ATOM   866   N  ND2 . ASN A 1 136 ? 70.315  48.243  95.341  1.00 46.48  ? 137 ASN A ND2 1 
ATOM   867   N  N   . ALA A 1 137 ? 68.977  43.760  98.613  1.00 41.40  ? 138 ALA A N   1 
ATOM   868   C  CA  . ALA A 1 137 ? 68.493  42.387  98.710  1.00 39.49  ? 138 ALA A CA  1 
ATOM   869   C  C   . ALA A 1 137 ? 67.097  42.310  99.319  1.00 39.39  ? 138 ALA A C   1 
ATOM   870   O  O   . ALA A 1 137 ? 66.275  41.489  98.905  1.00 35.79  ? 138 ALA A O   1 
ATOM   871   C  CB  . ALA A 1 137 ? 69.468  41.543  99.521  1.00 38.28  ? 138 ALA A CB  1 
ATOM   872   N  N   . ARG A 1 138 ? 66.829  43.169  100.298 1.00 34.46  ? 139 ARG A N   1 
ATOM   873   C  CA  . ARG A 1 138 ? 65.534  43.158  100.965 1.00 39.47  ? 139 ARG A CA  1 
ATOM   874   C  C   . ARG A 1 138 ? 64.424  43.559  100.002 1.00 40.87  ? 139 ARG A C   1 
ATOM   875   O  O   . ARG A 1 138 ? 63.286  43.132  100.158 1.00 41.76  ? 139 ARG A O   1 
ATOM   876   C  CB  . ARG A 1 138 ? 65.521  44.086  102.182 1.00 39.90  ? 139 ARG A CB  1 
ATOM   877   C  CG  . ARG A 1 138 ? 64.263  43.922  103.022 1.00 46.02  ? 139 ARG A CG  1 
ATOM   878   C  CD  . ARG A 1 138 ? 64.043  45.059  103.997 1.00 49.97  ? 139 ARG A CD  1 
ATOM   879   N  NE  . ARG A 1 138 ? 62.668  45.052  104.487 1.00 54.97  ? 139 ARG A NE  1 
ATOM   880   C  CZ  . ARG A 1 138 ? 62.198  45.867  105.425 1.00 56.03  ? 139 ARG A CZ  1 
ATOM   881   N  NH1 . ARG A 1 138 ? 62.996  46.762  105.991 1.00 58.18  ? 139 ARG A NH1 1 
ATOM   882   N  NH2 . ARG A 1 138 ? 60.929  45.781  105.801 1.00 56.56  ? 139 ARG A NH2 1 
ATOM   883   N  N   . ALA A 1 139 ? 64.754  44.380  99.011  1.00 41.32  ? 140 ALA A N   1 
ATOM   884   C  CA  . ALA A 1 139 ? 63.776  44.773  98.004  1.00 42.11  ? 140 ALA A CA  1 
ATOM   885   C  C   . ALA A 1 139 ? 63.323  43.555  97.203  1.00 42.22  ? 140 ALA A C   1 
ATOM   886   O  O   . ALA A 1 139 ? 62.125  43.333  97.007  1.00 46.31  ? 140 ALA A O   1 
ATOM   887   C  CB  . ALA A 1 139 ? 64.352  45.835  97.083  1.00 32.89  ? 140 ALA A CB  1 
ATOM   888   N  N   . PHE A 1 140 ? 64.290  42.760  96.755  1.00 43.82  ? 141 PHE A N   1 
ATOM   889   C  CA  . PHE A 1 140 ? 64.004  41.561  95.975  1.00 43.95  ? 141 PHE A CA  1 
ATOM   890   C  C   . PHE A 1 140 ? 63.282  40.508  96.813  1.00 42.61  ? 141 PHE A C   1 
ATOM   891   O  O   . PHE A 1 140 ? 62.312  39.891  96.357  1.00 44.01  ? 141 PHE A O   1 
ATOM   892   C  CB  . PHE A 1 140 ? 65.298  40.985  95.396  1.00 40.59  ? 141 PHE A CB  1 
ATOM   893   C  CG  . PHE A 1 140 ? 66.012  41.922  94.463  1.00 37.61  ? 141 PHE A CG  1 
ATOM   894   C  CD1 . PHE A 1 140 ? 65.526  42.152  93.186  1.00 32.16  ? 141 PHE A CD1 1 
ATOM   895   C  CD2 . PHE A 1 140 ? 67.168  42.572  94.860  1.00 41.97  ? 141 PHE A CD2 1 
ATOM   896   C  CE1 . PHE A 1 140 ? 66.179  43.014  92.323  1.00 33.62  ? 141 PHE A CE1 1 
ATOM   897   C  CE2 . PHE A 1 140 ? 67.825  43.436  94.002  1.00 41.95  ? 141 PHE A CE2 1 
ATOM   898   C  CZ  . PHE A 1 140 ? 67.330  43.656  92.732  1.00 30.21  ? 141 PHE A CZ  1 
ATOM   899   N  N   . ARG A 1 141 ? 63.757  40.311  98.040  1.00 37.79  ? 142 ARG A N   1 
ATOM   900   C  CA  . ARG A 1 141 ? 63.128  39.379  98.972  1.00 40.99  ? 142 ARG A CA  1 
ATOM   901   C  C   . ARG A 1 141 ? 61.667  39.760  99.207  1.00 40.48  ? 142 ARG A C   1 
ATOM   902   O  O   . ARG A 1 141 ? 60.775  38.904  99.204  1.00 39.91  ? 142 ARG A O   1 
ATOM   903   C  CB  . ARG A 1 141 ? 63.901  39.348  100.293 1.00 47.28  ? 142 ARG A CB  1 
ATOM   904   C  CG  . ARG A 1 141 ? 63.276  38.494  101.384 1.00 51.34  ? 142 ARG A CG  1 
ATOM   905   C  CD  . ARG A 1 141 ? 64.282  38.218  102.494 1.00 61.63  ? 142 ARG A CD  1 
ATOM   906   N  NE  . ARG A 1 141 ? 65.342  37.316  102.051 1.00 69.85  ? 142 ARG A NE  1 
ATOM   907   C  CZ  . ARG A 1 141 ? 66.456  37.071  102.734 1.00 75.82  ? 142 ARG A CZ  1 
ATOM   908   N  NH1 . ARG A 1 141 ? 66.667  37.668  103.899 1.00 79.39  ? 142 ARG A NH1 1 
ATOM   909   N  NH2 . ARG A 1 141 ? 67.363  36.233  102.250 1.00 77.34  ? 142 ARG A NH2 1 
ATOM   910   N  N   . ASP A 1 142 ? 61.435  41.057  99.391  1.00 44.16  ? 143 ASP A N   1 
ATOM   911   C  CA  . ASP A 1 142 ? 60.089  41.593  99.555  1.00 45.17  ? 143 ASP A CA  1 
ATOM   912   C  C   . ASP A 1 142 ? 59.245  41.339  98.315  1.00 39.36  ? 143 ASP A C   1 
ATOM   913   O  O   . ASP A 1 142 ? 58.077  40.968  98.421  1.00 34.96  ? 143 ASP A O   1 
ATOM   914   C  CB  . ASP A 1 142 ? 60.134  43.094  99.856  1.00 52.66  ? 143 ASP A CB  1 
ATOM   915   C  CG  . ASP A 1 142 ? 60.486  43.391  101.301 1.00 60.86  ? 143 ASP A CG  1 
ATOM   916   O  OD1 . ASP A 1 142 ? 60.153  42.566  102.178 1.00 63.43  ? 143 ASP A OD1 1 
ATOM   917   O  OD2 . ASP A 1 142 ? 61.094  44.451  101.561 1.00 65.38  ? 143 ASP A OD2 1 
ATOM   918   N  N   . LEU A 1 143 ? 59.834  41.540  97.139  1.00 32.83  ? 144 LEU A N   1 
ATOM   919   C  CA  . LEU A 1 143 ? 59.122  41.276  95.893  1.00 35.14  ? 144 LEU A CA  1 
ATOM   920   C  C   . LEU A 1 143 ? 58.677  39.817  95.816  1.00 42.95  ? 144 LEU A C   1 
ATOM   921   O  O   . LEU A 1 143 ? 57.534  39.527  95.456  1.00 41.79  ? 144 LEU A O   1 
ATOM   922   C  CB  . LEU A 1 143 ? 59.989  41.629  94.683  1.00 27.82  ? 144 LEU A CB  1 
ATOM   923   C  CG  . LEU A 1 143 ? 59.332  41.378  93.323  1.00 35.92  ? 144 LEU A CG  1 
ATOM   924   C  CD1 . LEU A 1 143 ? 57.971  42.056  93.249  1.00 37.10  ? 144 LEU A CD1 1 
ATOM   925   C  CD2 . LEU A 1 143 ? 60.229  41.848  92.191  1.00 35.58  ? 144 LEU A CD2 1 
ATOM   926   N  N   . TYR A 1 144 ? 59.578  38.901  96.165  1.00 39.15  ? 145 TYR A N   1 
ATOM   927   C  CA  . TYR A 1 144 ? 59.243  37.480  96.148  1.00 37.34  ? 145 TYR A CA  1 
ATOM   928   C  C   . TYR A 1 144 ? 58.163  37.136  97.170  1.00 34.63  ? 145 TYR A C   1 
ATOM   929   O  O   . TYR A 1 144 ? 57.277  36.327  96.890  1.00 31.64  ? 145 TYR A O   1 
ATOM   930   C  CB  . TYR A 1 144 ? 60.488  36.627  96.391  1.00 31.05  ? 145 TYR A CB  1 
ATOM   931   C  CG  . TYR A 1 144 ? 61.285  36.366  95.134  1.00 31.79  ? 145 TYR A CG  1 
ATOM   932   C  CD1 . TYR A 1 144 ? 62.372  37.160  94.799  1.00 34.56  ? 145 TYR A CD1 1 
ATOM   933   C  CD2 . TYR A 1 144 ? 60.938  35.332  94.274  1.00 26.16  ? 145 TYR A CD2 1 
ATOM   934   C  CE1 . TYR A 1 144 ? 63.099  36.927  93.648  1.00 34.09  ? 145 TYR A CE1 1 
ATOM   935   C  CE2 . TYR A 1 144 ? 61.659  35.092  93.120  1.00 26.14  ? 145 TYR A CE2 1 
ATOM   936   C  CZ  . TYR A 1 144 ? 62.739  35.893  92.813  1.00 33.54  ? 145 TYR A CZ  1 
ATOM   937   O  OH  . TYR A 1 144 ? 63.463  35.663  91.667  1.00 37.40  ? 145 TYR A OH  1 
ATOM   938   N  N   . SER A 1 145 ? 58.233  37.746  98.350  1.00 32.15  ? 146 SER A N   1 
ATOM   939   C  CA  . SER A 1 145 ? 57.198  37.537  99.359  1.00 37.94  ? 146 SER A CA  1 
ATOM   940   C  C   . SER A 1 145 ? 55.836  38.015  98.853  1.00 39.99  ? 146 SER A C   1 
ATOM   941   O  O   . SER A 1 145 ? 54.814  37.358  99.075  1.00 32.57  ? 146 SER A O   1 
ATOM   942   C  CB  . SER A 1 145 ? 57.559  38.252  100.663 1.00 35.32  ? 146 SER A CB  1 
ATOM   943   O  OG  . SER A 1 145 ? 58.603  37.575  101.342 1.00 39.60  ? 146 SER A OG  1 
ATOM   944   N  N   . GLU A 1 146 ? 55.833  39.155  98.167  1.00 42.16  ? 147 GLU A N   1 
ATOM   945   C  CA  . GLU A 1 146 ? 54.613  39.709  97.587  1.00 42.80  ? 147 GLU A CA  1 
ATOM   946   C  C   . GLU A 1 146 ? 54.042  38.792  96.511  1.00 36.92  ? 147 GLU A C   1 
ATOM   947   O  O   . GLU A 1 146 ? 52.832  38.561  96.462  1.00 29.66  ? 147 GLU A O   1 
ATOM   948   C  CB  . GLU A 1 146 ? 54.877  41.101  97.005  1.00 50.98  ? 147 GLU A CB  1 
ATOM   949   C  CG  . GLU A 1 146 ? 54.930  42.213  98.042  1.00 63.31  ? 147 GLU A CG  1 
ATOM   950   C  CD  . GLU A 1 146 ? 53.555  42.761  98.378  1.00 69.35  ? 147 GLU A CD  1 
ATOM   951   O  OE1 . GLU A 1 146 ? 52.970  43.467  97.530  1.00 74.70  ? 147 GLU A OE1 1 
ATOM   952   O  OE2 . GLU A 1 146 ? 53.055  42.483  99.487  1.00 73.58  ? 147 GLU A OE2 1 
ATOM   953   N  N   . LEU A 1 147 ? 54.915  38.279  95.647  1.00 30.57  ? 148 LEU A N   1 
ATOM   954   C  CA  . LEU A 1 147 ? 54.513  37.315  94.627  1.00 28.19  ? 148 LEU A CA  1 
ATOM   955   C  C   . LEU A 1 147 ? 53.903  36.075  95.268  1.00 32.66  ? 148 LEU A C   1 
ATOM   956   O  O   . LEU A 1 147 ? 52.923  35.516  94.772  1.00 36.36  ? 148 LEU A O   1 
ATOM   957   C  CB  . LEU A 1 147 ? 55.708  36.915  93.760  1.00 33.31  ? 148 LEU A CB  1 
ATOM   958   C  CG  . LEU A 1 147 ? 56.196  37.894  92.692  1.00 31.75  ? 148 LEU A CG  1 
ATOM   959   C  CD1 . LEU A 1 147 ? 57.445  37.353  92.020  1.00 32.54  ? 148 LEU A CD1 1 
ATOM   960   C  CD2 . LEU A 1 147 ? 55.108  38.130  91.665  1.00 30.99  ? 148 LEU A CD2 1 
ATOM   961   N  N   . ARG A 1 148 ? 54.497  35.657  96.380  1.00 39.40  ? 149 ARG A N   1 
ATOM   962   C  CA  . ARG A 1 148 ? 54.063  34.472  97.107  1.00 42.42  ? 149 ARG A CA  1 
ATOM   963   C  C   . ARG A 1 148 ? 52.659  34.671  97.680  1.00 40.87  ? 149 ARG A C   1 
ATOM   964   O  O   . ARG A 1 148 ? 51.770  33.831  97.490  1.00 39.36  ? 149 ARG A O   1 
ATOM   965   C  CB  . ARG A 1 148 ? 55.071  34.154  98.214  1.00 39.46  ? 149 ARG A CB  1 
ATOM   966   C  CG  . ARG A 1 148 ? 55.015  32.743  98.755  1.00 41.06  ? 149 ARG A CG  1 
ATOM   967   C  CD  . ARG A 1 148 ? 56.297  32.418  99.508  1.00 36.76  ? 149 ARG A CD  1 
ATOM   968   N  NE  . ARG A 1 148 ? 57.438  32.290  98.604  1.00 41.11  ? 149 ARG A NE  1 
ATOM   969   C  CZ  . ARG A 1 148 ? 58.615  32.880  98.790  1.00 40.39  ? 149 ARG A CZ  1 
ATOM   970   N  NH1 . ARG A 1 148 ? 58.813  33.652  99.850  1.00 39.70  ? 149 ARG A NH1 1 
ATOM   971   N  NH2 . ARG A 1 148 ? 59.594  32.702  97.912  1.00 36.73  ? 149 ARG A NH2 1 
ATOM   972   N  N   . LEU A 1 149 ? 52.465  35.792  98.371  1.00 42.82  ? 150 LEU A N   1 
ATOM   973   C  CA  . LEU A 1 149 ? 51.150  36.165  98.887  1.00 44.11  ? 150 LEU A CA  1 
ATOM   974   C  C   . LEU A 1 149 ? 50.119  36.248  97.768  1.00 41.02  ? 150 LEU A C   1 
ATOM   975   O  O   . LEU A 1 149 ? 48.971  35.835  97.933  1.00 33.50  ? 150 LEU A O   1 
ATOM   976   C  CB  . LEU A 1 149 ? 51.220  37.504  99.621  1.00 43.38  ? 150 LEU A CB  1 
ATOM   977   C  CG  . LEU A 1 149 ? 51.609  37.471  101.098 1.00 49.75  ? 150 LEU A CG  1 
ATOM   978   C  CD1 . LEU A 1 149 ? 51.925  38.872  101.592 1.00 47.21  ? 150 LEU A CD1 1 
ATOM   979   C  CD2 . LEU A 1 149 ? 50.494  36.849  101.921 1.00 46.70  ? 150 LEU A CD2 1 
ATOM   980   N  N   . TYR A 1 150 ? 50.544  36.788  96.631  1.00 38.80  ? 151 TYR A N   1 
ATOM   981   C  CA  . TYR A 1 150 ? 49.682  36.917  95.463  1.00 39.16  ? 151 TYR A CA  1 
ATOM   982   C  C   . TYR A 1 150 ? 49.255  35.556  94.930  1.00 41.87  ? 151 TYR A C   1 
ATOM   983   O  O   . TYR A 1 150 ? 48.114  35.380  94.506  1.00 43.51  ? 151 TYR A O   1 
ATOM   984   C  CB  . TYR A 1 150 ? 50.393  37.710  94.366  1.00 43.90  ? 151 TYR A CB  1 
ATOM   985   C  CG  . TYR A 1 150 ? 49.531  37.994  93.159  1.00 47.78  ? 151 TYR A CG  1 
ATOM   986   C  CD1 . TYR A 1 150 ? 48.437  38.842  93.249  1.00 50.71  ? 151 TYR A CD1 1 
ATOM   987   C  CD2 . TYR A 1 150 ? 49.816  37.420  91.928  1.00 53.22  ? 151 TYR A CD2 1 
ATOM   988   C  CE1 . TYR A 1 150 ? 47.649  39.106  92.148  1.00 54.99  ? 151 TYR A CE1 1 
ATOM   989   C  CE2 . TYR A 1 150 ? 49.032  37.680  90.820  1.00 59.09  ? 151 TYR A CE2 1 
ATOM   990   C  CZ  . TYR A 1 150 ? 47.949  38.526  90.937  1.00 62.37  ? 151 TYR A CZ  1 
ATOM   991   O  OH  . TYR A 1 150 ? 47.160  38.793  89.843  1.00 65.67  ? 151 TYR A OH  1 
ATOM   992   N  N   . TYR A 1 151 ? 50.176  34.597  94.951  1.00 39.29  ? 152 TYR A N   1 
ATOM   993   C  CA  . TYR A 1 151 ? 49.860  33.242  94.518  1.00 45.71  ? 152 TYR A CA  1 
ATOM   994   C  C   . TYR A 1 151 ? 48.909  32.566  95.496  1.00 43.83  ? 152 TYR A C   1 
ATOM   995   O  O   . TYR A 1 151 ? 47.980  31.873  95.085  1.00 45.09  ? 152 TYR A O   1 
ATOM   996   C  CB  . TYR A 1 151 ? 51.127  32.394  94.367  1.00 38.48  ? 152 TYR A CB  1 
ATOM   997   C  CG  . TYR A 1 151 ? 50.835  30.912  94.246  1.00 33.62  ? 152 TYR A CG  1 
ATOM   998   C  CD1 . TYR A 1 151 ? 50.410  30.364  93.042  1.00 29.09  ? 152 TYR A CD1 1 
ATOM   999   C  CD2 . TYR A 1 151 ? 50.973  30.063  95.338  1.00 29.49  ? 152 TYR A CD2 1 
ATOM   1000  C  CE1 . TYR A 1 151 ? 50.136  29.015  92.927  1.00 25.05  ? 152 TYR A CE1 1 
ATOM   1001  C  CE2 . TYR A 1 151 ? 50.700  28.712  95.233  1.00 28.14  ? 152 TYR A CE2 1 
ATOM   1002  C  CZ  . TYR A 1 151 ? 50.282  28.193  94.025  1.00 31.03  ? 152 TYR A CZ  1 
ATOM   1003  O  OH  . TYR A 1 151 ? 50.009  26.849  93.915  1.00 25.20  ? 152 TYR A OH  1 
ATOM   1004  N  N   . ARG A 1 152 ? 49.144  32.765  96.790  1.00 50.03  ? 153 ARG A N   1 
ATOM   1005  C  CA  . ARG A 1 152 ? 48.342  32.092  97.808  1.00 49.48  ? 153 ARG A CA  1 
ATOM   1006  C  C   . ARG A 1 152 ? 46.908  32.614  97.864  1.00 54.65  ? 153 ARG A C   1 
ATOM   1007  O  O   . ARG A 1 152 ? 46.055  32.032  98.536  1.00 57.59  ? 153 ARG A O   1 
ATOM   1008  C  CB  . ARG A 1 152 ? 49.002  32.221  99.182  1.00 55.52  ? 153 ARG A CB  1 
ATOM   1009  C  CG  . ARG A 1 152 ? 50.273  31.402  99.325  1.00 58.60  ? 153 ARG A CG  1 
ATOM   1010  C  CD  . ARG A 1 152 ? 50.681  31.257  100.781 1.00 65.12  ? 153 ARG A CD  1 
ATOM   1011  N  NE  . ARG A 1 152 ? 51.968  30.581  100.921 1.00 71.68  ? 153 ARG A NE  1 
ATOM   1012  C  CZ  . ARG A 1 152 ? 53.060  31.150  101.420 1.00 76.84  ? 153 ARG A CZ  1 
ATOM   1013  N  NH1 . ARG A 1 152 ? 53.023  32.410  101.832 1.00 77.36  ? 153 ARG A NH1 1 
ATOM   1014  N  NH2 . ARG A 1 152 ? 54.189  30.460  101.511 1.00 77.90  ? 153 ARG A NH2 1 
ATOM   1015  N  N   . GLY A 1 153 ? 46.642  33.707  97.158  1.00 52.58  ? 154 GLY A N   1 
ATOM   1016  C  CA  . GLY A 1 153 ? 45.285  34.203  97.030  1.00 54.63  ? 154 GLY A CA  1 
ATOM   1017  C  C   . GLY A 1 153 ? 45.000  35.492  97.774  1.00 61.44  ? 154 GLY A C   1 
ATOM   1018  O  O   . GLY A 1 153 ? 43.923  36.068  97.617  1.00 57.95  ? 154 GLY A O   1 
ATOM   1019  N  N   . ALA A 1 154 ? 45.954  35.939  98.588  1.00 62.23  ? 155 ALA A N   1 
ATOM   1020  C  CA  . ALA A 1 154 ? 45.824  37.212  99.290  1.00 72.34  ? 155 ALA A CA  1 
ATOM   1021  C  C   . ALA A 1 154 ? 45.575  38.307  98.264  1.00 86.46  ? 155 ALA A C   1 
ATOM   1022  O  O   . ALA A 1 154 ? 46.162  38.284  97.182  1.00 80.80  ? 155 ALA A O   1 
ATOM   1023  C  CB  . ALA A 1 154 ? 47.068  37.509  100.110 1.00 64.98  ? 155 ALA A CB  1 
ATOM   1024  N  N   . ASN A 1 155 ? 44.732  39.281  98.594  1.00 108.01 ? 156 ASN A N   1 
ATOM   1025  C  CA  . ASN A 1 155 ? 44.218  40.142  97.542  1.00 110.65 ? 156 ASN A CA  1 
ATOM   1026  C  C   . ASN A 1 155 ? 45.121  41.343  97.336  1.00 109.67 ? 156 ASN A C   1 
ATOM   1027  O  O   . ASN A 1 155 ? 45.211  42.252  98.159  1.00 112.28 ? 156 ASN A O   1 
ATOM   1028  C  CB  . ASN A 1 155 ? 42.794  40.598  97.863  1.00 113.83 ? 156 ASN A CB  1 
ATOM   1029  N  N   . LEU A 1 156 ? 45.779  41.300  96.188  1.00 92.06  ? 157 LEU A N   1 
ATOM   1030  C  CA  . LEU A 1 156 ? 46.795  42.239  95.755  1.00 83.89  ? 157 LEU A CA  1 
ATOM   1031  C  C   . LEU A 1 156 ? 46.784  42.078  94.249  1.00 79.39  ? 157 LEU A C   1 
ATOM   1032  O  O   . LEU A 1 156 ? 46.173  41.131  93.752  1.00 78.42  ? 157 LEU A O   1 
ATOM   1033  C  CB  . LEU A 1 156 ? 48.181  41.910  96.323  1.00 78.30  ? 157 LEU A CB  1 
ATOM   1034  C  CG  . LEU A 1 156 ? 48.431  41.627  97.807  1.00 72.60  ? 157 LEU A CG  1 
ATOM   1035  C  CD1 . LEU A 1 156 ? 49.582  40.645  97.943  1.00 70.67  ? 157 LEU A CD1 1 
ATOM   1036  C  CD2 . LEU A 1 156 ? 48.737  42.902  98.571  1.00 73.52  ? 157 LEU A CD2 1 
ATOM   1037  N  N   . HIS A 1 157 ? 47.400  42.992  93.508  1.00 81.39  ? 158 HIS A N   1 
ATOM   1038  C  CA  . HIS A 1 157 ? 47.778  42.629  92.145  1.00 85.92  ? 158 HIS A CA  1 
ATOM   1039  C  C   . HIS A 1 157 ? 49.159  43.209  91.829  1.00 80.26  ? 158 HIS A C   1 
ATOM   1040  O  O   . HIS A 1 157 ? 49.603  44.174  92.459  1.00 78.56  ? 158 HIS A O   1 
ATOM   1041  C  CB  . HIS A 1 157 ? 46.698  43.062  91.134  1.00 95.93  ? 158 HIS A CB  1 
ATOM   1042  C  CG  . HIS A 1 157 ? 47.098  42.908  89.695  1.00 103.12 ? 158 HIS A CG  1 
ATOM   1043  N  ND1 . HIS A 1 157 ? 48.076  43.666  89.092  1.00 107.44 ? 158 HIS A ND1 1 
ATOM   1044  C  CD2 . HIS A 1 157 ? 46.707  42.001  88.768  1.00 104.95 ? 158 HIS A CD2 1 
ATOM   1045  C  CE1 . HIS A 1 157 ? 48.231  43.273  87.840  1.00 108.27 ? 158 HIS A CE1 1 
ATOM   1046  N  NE2 . HIS A 1 157 ? 47.413  42.263  87.619  1.00 107.91 ? 158 HIS A NE2 1 
ATOM   1047  N  N   . LEU A 1 158 ? 49.835  42.579  90.871  1.00 75.86  ? 159 LEU A N   1 
ATOM   1048  C  CA  . LEU A 1 158 ? 51.223  42.862  90.519  1.00 74.66  ? 159 LEU A CA  1 
ATOM   1049  C  C   . LEU A 1 158 ? 51.494  44.210  89.872  1.00 72.87  ? 159 LEU A C   1 
ATOM   1050  O  O   . LEU A 1 158 ? 52.595  44.697  89.959  1.00 74.08  ? 159 LEU A O   1 
ATOM   1051  C  CB  . LEU A 1 158 ? 51.731  41.775  89.575  1.00 74.77  ? 159 LEU A CB  1 
ATOM   1052  C  CG  . LEU A 1 158 ? 51.436  40.389  90.130  1.00 74.00  ? 159 LEU A CG  1 
ATOM   1053  C  CD1 . LEU A 1 158 ? 51.731  39.316  89.109  1.00 75.19  ? 159 LEU A CD1 1 
ATOM   1054  C  CD2 . LEU A 1 158 ? 52.259  40.184  91.384  1.00 73.05  ? 159 LEU A CD2 1 
ATOM   1055  N  N   . GLU A 1 159 ? 50.525  44.805  89.195  1.00 65.40  ? 160 GLU A N   1 
ATOM   1056  C  CA  . GLU A 1 159 ? 50.796  46.037  88.457  1.00 64.17  ? 160 GLU A CA  1 
ATOM   1057  C  C   . GLU A 1 159 ? 51.306  47.153  89.359  1.00 60.45  ? 160 GLU A C   1 
ATOM   1058  O  O   . GLU A 1 159 ? 52.373  47.732  89.136  1.00 60.37  ? 160 GLU A O   1 
ATOM   1059  C  CB  . GLU A 1 159 ? 49.539  46.507  87.734  1.00 61.93  ? 160 GLU A CB  1 
ATOM   1060  N  N   . GLU A 1 160 ? 50.517  47.433  90.384  1.00 60.32  ? 161 GLU A N   1 
ATOM   1061  C  CA  . GLU A 1 160 ? 50.801  48.475  91.347  1.00 60.19  ? 161 GLU A CA  1 
ATOM   1062  C  C   . GLU A 1 160 ? 52.009  48.096  92.206  1.00 59.22  ? 161 GLU A C   1 
ATOM   1063  O  O   . GLU A 1 160 ? 52.874  48.929  92.471  1.00 64.55  ? 161 GLU A O   1 
ATOM   1064  C  CB  . GLU A 1 160 ? 49.560  48.725  92.212  1.00 68.40  ? 161 GLU A CB  1 
ATOM   1065  C  CG  . GLU A 1 160 ? 48.206  48.641  91.475  1.00 78.98  ? 161 GLU A CG  1 
ATOM   1066  C  CD  . GLU A 1 160 ? 47.727  47.211  91.213  1.00 88.85  ? 161 GLU A CD  1 
ATOM   1067  O  OE1 . GLU A 1 160 ? 48.576  46.313  91.022  1.00 90.40  ? 161 GLU A OE1 1 
ATOM   1068  O  OE2 . GLU A 1 160 ? 46.500  46.980  91.225  1.00 92.35  ? 161 GLU A OE2 1 
ATOM   1069  N  N   . THR A 1 161 ? 52.070  46.832  92.618  1.00 54.91  ? 162 THR A N   1 
ATOM   1070  C  CA  . THR A 1 161 ? 53.140  46.333  93.486  1.00 48.09  ? 162 THR A CA  1 
ATOM   1071  C  C   . THR A 1 161 ? 54.517  46.411  92.823  1.00 43.38  ? 162 THR A C   1 
ATOM   1072  O  O   . THR A 1 161 ? 55.499  46.849  93.429  1.00 41.12  ? 162 THR A O   1 
ATOM   1073  C  CB  . THR A 1 161 ? 52.864  44.875  93.903  1.00 45.09  ? 162 THR A CB  1 
ATOM   1074  O  OG1 . THR A 1 161 ? 51.729  44.838  94.776  1.00 46.77  ? 162 THR A OG1 1 
ATOM   1075  C  CG2 . THR A 1 161 ? 54.064  44.275  94.622  1.00 49.81  ? 162 THR A CG2 1 
ATOM   1076  N  N   . LEU A 1 162 ? 54.563  45.967  91.572  1.00 31.94  ? 163 LEU A N   1 
ATOM   1077  C  CA  . LEU A 1 162 ? 55.748  46.014  90.727  1.00 40.13  ? 163 LEU A CA  1 
ATOM   1078  C  C   . LEU A 1 162 ? 56.084  47.451  90.368  1.00 37.12  ? 163 LEU A C   1 
ATOM   1079  O  O   . LEU A 1 162 ? 57.247  47.810  90.312  1.00 40.67  ? 163 LEU A O   1 
ATOM   1080  C  CB  . LEU A 1 162 ? 55.539  45.192  89.446  1.00 39.48  ? 163 LEU A CB  1 
ATOM   1081  C  CG  . LEU A 1 162 ? 55.393  43.667  89.547  1.00 36.19  ? 163 LEU A CG  1 
ATOM   1082  C  CD1 . LEU A 1 162 ? 54.860  43.076  88.242  1.00 27.92  ? 163 LEU A CD1 1 
ATOM   1083  C  CD2 . LEU A 1 162 ? 56.710  43.020  89.920  1.00 36.34  ? 163 LEU A CD2 1 
ATOM   1084  N  N   . ALA A 1 163 ? 55.065  48.268  90.108  1.00 40.53  ? 164 ALA A N   1 
ATOM   1085  C  CA  . ALA A 1 163 ? 55.289  49.683  89.819  1.00 36.80  ? 164 ALA A CA  1 
ATOM   1086  C  C   . ALA A 1 163 ? 56.025  50.341  90.985  1.00 43.84  ? 164 ALA A C   1 
ATOM   1087  O  O   . ALA A 1 163 ? 57.053  51.003  90.801  1.00 50.64  ? 164 ALA A O   1 
ATOM   1088  C  CB  . ALA A 1 163 ? 53.972  50.392  89.546  1.00 42.64  ? 164 ALA A CB  1 
ATOM   1089  N  N   . GLU A 1 164 ? 55.494  50.130  92.186  1.00 39.80  ? 165 GLU A N   1 
ATOM   1090  C  CA  . GLU A 1 164 ? 56.109  50.617  93.414  1.00 43.83  ? 165 GLU A CA  1 
ATOM   1091  C  C   . GLU A 1 164 ? 57.534  50.086  93.553  1.00 50.27  ? 165 GLU A C   1 
ATOM   1092  O  O   . GLU A 1 164 ? 58.477  50.849  93.802  1.00 51.00  ? 165 GLU A O   1 
ATOM   1093  C  CB  . GLU A 1 164 ? 55.266  50.201  94.624  1.00 49.17  ? 165 GLU A CB  1 
ATOM   1094  C  CG  . GLU A 1 164 ? 55.880  50.545  95.971  1.00 51.35  ? 165 GLU A CG  1 
ATOM   1095  C  CD  . GLU A 1 164 ? 55.783  52.024  96.299  1.00 61.40  ? 165 GLU A CD  1 
ATOM   1096  O  OE1 . GLU A 1 164 ? 55.015  52.743  95.622  1.00 62.82  ? 165 GLU A OE1 1 
ATOM   1097  O  OE2 . GLU A 1 164 ? 56.477  52.470  97.237  1.00 60.75  ? 165 GLU A OE2 1 
ATOM   1098  N  N   . PHE A 1 165 ? 57.669  48.773  93.377  1.00 46.43  ? 166 PHE A N   1 
ATOM   1099  C  CA  . PHE A 1 165 ? 58.955  48.085  93.441  1.00 45.94  ? 166 PHE A CA  1 
ATOM   1100  C  C   . PHE A 1 165 ? 60.013  48.739  92.557  1.00 38.73  ? 166 PHE A C   1 
ATOM   1101  O  O   . PHE A 1 165 ? 61.129  48.999  93.001  1.00 36.72  ? 166 PHE A O   1 
ATOM   1102  C  CB  . PHE A 1 165 ? 58.781  46.615  93.043  1.00 34.91  ? 166 PHE A CB  1 
ATOM   1103  C  CG  . PHE A 1 165 ? 60.066  45.932  92.668  1.00 33.38  ? 166 PHE A CG  1 
ATOM   1104  C  CD1 . PHE A 1 165 ? 60.955  45.512  93.644  1.00 29.74  ? 166 PHE A CD1 1 
ATOM   1105  C  CD2 . PHE A 1 165 ? 60.384  45.710  91.337  1.00 30.53  ? 166 PHE A CD2 1 
ATOM   1106  C  CE1 . PHE A 1 165 ? 62.137  44.886  93.300  1.00 34.47  ? 166 PHE A CE1 1 
ATOM   1107  C  CE2 . PHE A 1 165 ? 61.566  45.087  90.987  1.00 31.14  ? 166 PHE A CE2 1 
ATOM   1108  C  CZ  . PHE A 1 165 ? 62.444  44.673  91.970  1.00 36.72  ? 166 PHE A CZ  1 
ATOM   1109  N  N   . TRP A 1 166 ? 59.646  49.004  91.308  1.00 42.84  ? 167 TRP A N   1 
ATOM   1110  C  CA  . TRP A 1 166 ? 60.554  49.578  90.327  1.00 39.60  ? 167 TRP A CA  1 
ATOM   1111  C  C   . TRP A 1 166 ? 60.861  51.030  90.646  1.00 46.06  ? 167 TRP A C   1 
ATOM   1112  O  O   . TRP A 1 166 ? 61.987  51.484  90.447  1.00 45.91  ? 167 TRP A O   1 
ATOM   1113  C  CB  . TRP A 1 166 ? 59.972  49.465  88.914  1.00 40.46  ? 167 TRP A CB  1 
ATOM   1114  C  CG  . TRP A 1 166 ? 59.970  48.068  88.381  1.00 44.45  ? 167 TRP A CG  1 
ATOM   1115  C  CD1 . TRP A 1 166 ? 58.883  47.322  88.032  1.00 42.49  ? 167 TRP A CD1 1 
ATOM   1116  C  CD2 . TRP A 1 166 ? 61.115  47.242  88.145  1.00 45.44  ? 167 TRP A CD2 1 
ATOM   1117  N  NE1 . TRP A 1 166 ? 59.279  46.083  87.592  1.00 38.78  ? 167 TRP A NE1 1 
ATOM   1118  C  CE2 . TRP A 1 166 ? 60.646  46.009  87.651  1.00 36.08  ? 167 TRP A CE2 1 
ATOM   1119  C  CE3 . TRP A 1 166 ? 62.492  47.427  88.302  1.00 38.15  ? 167 TRP A CE3 1 
ATOM   1120  C  CZ2 . TRP A 1 166 ? 61.503  44.967  87.311  1.00 35.39  ? 167 TRP A CZ2 1 
ATOM   1121  C  CZ3 . TRP A 1 166 ? 63.342  46.390  87.965  1.00 39.58  ? 167 TRP A CZ3 1 
ATOM   1122  C  CH2 . TRP A 1 166 ? 62.844  45.176  87.476  1.00 37.55  ? 167 TRP A CH2 1 
ATOM   1123  N  N   . ALA A 1 167 ? 59.860  51.758  91.133  1.00 44.96  ? 168 ALA A N   1 
ATOM   1124  C  CA  . ALA A 1 167 ? 60.080  53.136  91.560  1.00 42.10  ? 168 ALA A CA  1 
ATOM   1125  C  C   . ALA A 1 167 ? 61.152  53.195  92.648  1.00 41.94  ? 168 ALA A C   1 
ATOM   1126  O  O   . ALA A 1 167 ? 62.209  53.827  92.476  1.00 46.52  ? 168 ALA A O   1 
ATOM   1127  C  CB  . ALA A 1 167 ? 58.782  53.753  92.056  1.00 42.75  ? 168 ALA A CB  1 
ATOM   1128  N  N   . ARG A 1 168 ? 60.881  52.513  93.758  1.00 44.33  ? 169 ARG A N   1 
ATOM   1129  C  CA  . ARG A 1 168 ? 61.791  52.521  94.900  1.00 46.78  ? 169 ARG A CA  1 
ATOM   1130  C  C   . ARG A 1 168 ? 63.168  51.967  94.537  1.00 52.74  ? 169 ARG A C   1 
ATOM   1131  O  O   . ARG A 1 168 ? 64.196  52.494  94.979  1.00 52.30  ? 169 ARG A O   1 
ATOM   1132  C  CB  . ARG A 1 168 ? 61.191  51.726  96.061  1.00 44.71  ? 169 ARG A CB  1 
ATOM   1133  C  CG  . ARG A 1 168 ? 59.779  52.149  96.459  1.00 52.62  ? 169 ARG A CG  1 
ATOM   1134  C  CD  . ARG A 1 168 ? 59.739  53.538  97.095  1.00 55.14  ? 169 ARG A CD  1 
ATOM   1135  N  NE  . ARG A 1 168 ? 59.729  54.615  96.107  1.00 55.92  ? 169 ARG A NE  1 
ATOM   1136  C  CZ  . ARG A 1 168 ? 58.639  55.050  95.482  1.00 55.38  ? 169 ARG A CZ  1 
ATOM   1137  N  NH1 . ARG A 1 168 ? 57.460  54.503  95.739  1.00 52.77  ? 169 ARG A NH1 1 
ATOM   1138  N  NH2 . ARG A 1 168 ? 58.728  56.036  94.599  1.00 51.69  ? 169 ARG A NH2 1 
ATOM   1139  N  N   . LEU A 1 169 ? 63.187  50.913  93.725  1.00 47.81  ? 170 LEU A N   1 
ATOM   1140  C  CA  . LEU A 1 169 ? 64.449  50.314  93.306  1.00 48.15  ? 170 LEU A CA  1 
ATOM   1141  C  C   . LEU A 1 169 ? 65.265  51.287  92.463  1.00 49.50  ? 170 LEU A C   1 
ATOM   1142  O  O   . LEU A 1 169 ? 66.484  51.356  92.598  1.00 45.46  ? 170 LEU A O   1 
ATOM   1143  C  CB  . LEU A 1 169 ? 64.213  49.022  92.525  1.00 44.36  ? 170 LEU A CB  1 
ATOM   1144  C  CG  . LEU A 1 169 ? 65.496  48.268  92.169  1.00 41.55  ? 170 LEU A CG  1 
ATOM   1145  C  CD1 . LEU A 1 169 ? 66.233  47.852  93.434  1.00 37.63  ? 170 LEU A CD1 1 
ATOM   1146  C  CD2 . LEU A 1 169 ? 65.203  47.063  91.291  1.00 44.35  ? 170 LEU A CD2 1 
ATOM   1147  N  N   . LEU A 1 170 ? 64.591  52.035  91.594  1.00 52.71  ? 171 LEU A N   1 
ATOM   1148  C  CA  . LEU A 1 170 ? 65.267  53.038  90.781  1.00 47.06  ? 171 LEU A CA  1 
ATOM   1149  C  C   . LEU A 1 170 ? 65.839  54.133  91.673  1.00 51.62  ? 171 LEU A C   1 
ATOM   1150  O  O   . LEU A 1 170 ? 66.973  54.578  91.472  1.00 48.21  ? 171 LEU A O   1 
ATOM   1151  C  CB  . LEU A 1 170 ? 64.317  53.638  89.742  1.00 44.59  ? 171 LEU A CB  1 
ATOM   1152  C  CG  . LEU A 1 170 ? 64.875  54.806  88.924  1.00 44.54  ? 171 LEU A CG  1 
ATOM   1153  C  CD1 . LEU A 1 170 ? 66.121  54.386  88.157  1.00 45.52  ? 171 LEU A CD1 1 
ATOM   1154  C  CD2 . LEU A 1 170 ? 63.821  55.351  87.974  1.00 45.44  ? 171 LEU A CD2 1 
ATOM   1155  N  N   . GLU A 1 171 ? 65.053  54.556  92.663  1.00 55.56  ? 172 GLU A N   1 
ATOM   1156  C  CA  . GLU A 1 171 ? 65.535  55.529  93.643  1.00 53.96  ? 172 GLU A CA  1 
ATOM   1157  C  C   . GLU A 1 171 ? 66.824  55.059  94.317  1.00 57.18  ? 172 GLU A C   1 
ATOM   1158  O  O   . GLU A 1 171 ? 67.860  55.730  94.239  1.00 61.44  ? 172 GLU A O   1 
ATOM   1159  C  CB  . GLU A 1 171 ? 64.472  55.802  94.710  1.00 55.77  ? 172 GLU A CB  1 
ATOM   1160  C  CG  . GLU A 1 171 ? 63.179  56.394  94.182  1.00 58.22  ? 172 GLU A CG  1 
ATOM   1161  C  CD  . GLU A 1 171 ? 62.173  56.661  95.287  1.00 62.85  ? 172 GLU A CD  1 
ATOM   1162  O  OE1 . GLU A 1 171 ? 62.290  56.034  96.361  1.00 65.21  ? 172 GLU A OE1 1 
ATOM   1163  O  OE2 . GLU A 1 171 ? 61.268  57.496  95.082  1.00 65.65  ? 172 GLU A OE2 1 
ATOM   1164  N  N   . ARG A 1 172 ? 66.753  53.900  94.970  1.00 54.29  ? 173 ARG A N   1 
ATOM   1165  C  CA  . ARG A 1 172 ? 67.894  53.354  95.706  1.00 53.48  ? 173 ARG A CA  1 
ATOM   1166  C  C   . ARG A 1 172 ? 69.122  53.140  94.820  1.00 51.83  ? 173 ARG A C   1 
ATOM   1167  O  O   . ARG A 1 172 ? 70.236  53.532  95.179  1.00 49.82  ? 173 ARG A O   1 
ATOM   1168  C  CB  . ARG A 1 172 ? 67.507  52.035  96.379  1.00 56.68  ? 173 ARG A CB  1 
ATOM   1169  C  CG  . ARG A 1 172 ? 66.522  52.188  97.527  1.00 61.37  ? 173 ARG A CG  1 
ATOM   1170  C  CD  . ARG A 1 172 ? 66.163  50.841  98.133  1.00 65.40  ? 173 ARG A CD  1 
ATOM   1171  N  NE  . ARG A 1 172 ? 67.335  50.150  98.664  1.00 70.34  ? 173 ARG A NE  1 
ATOM   1172  C  CZ  . ARG A 1 172 ? 67.824  50.336  99.886  1.00 73.20  ? 173 ARG A CZ  1 
ATOM   1173  N  NH1 . ARG A 1 172 ? 67.242  51.195  100.712 1.00 76.05  ? 173 ARG A NH1 1 
ATOM   1174  N  NH2 . ARG A 1 172 ? 68.894  49.661  100.283 1.00 71.64  ? 173 ARG A NH2 1 
ATOM   1175  N  N   . LEU A 1 173 ? 68.912  52.520  93.663  1.00 50.06  ? 174 LEU A N   1 
ATOM   1176  C  CA  . LEU A 1 173 ? 70.002  52.241  92.736  1.00 52.32  ? 174 LEU A CA  1 
ATOM   1177  C  C   . LEU A 1 173 ? 70.655  53.525  92.233  1.00 55.33  ? 174 LEU A C   1 
ATOM   1178  O  O   . LEU A 1 173 ? 71.878  53.590  92.091  1.00 56.77  ? 174 LEU A O   1 
ATOM   1179  C  CB  . LEU A 1 173 ? 69.503  51.405  91.554  1.00 49.11  ? 174 LEU A CB  1 
ATOM   1180  C  CG  . LEU A 1 173 ? 69.283  49.917  91.840  1.00 44.54  ? 174 LEU A CG  1 
ATOM   1181  C  CD1 . LEU A 1 173 ? 68.684  49.213  90.636  1.00 38.03  ? 174 LEU A CD1 1 
ATOM   1182  C  CD2 . LEU A 1 173 ? 70.587  49.257  92.243  1.00 45.12  ? 174 LEU A CD2 1 
ATOM   1183  N  N   . PHE A 1 174 ? 69.845  54.548  91.972  1.00 58.26  ? 175 PHE A N   1 
ATOM   1184  C  CA  . PHE A 1 174 ? 70.393  55.817  91.508  1.00 59.98  ? 175 PHE A CA  1 
ATOM   1185  C  C   . PHE A 1 174 ? 71.174  56.510  92.618  1.00 58.08  ? 175 PHE A C   1 
ATOM   1186  O  O   . PHE A 1 174 ? 72.218  57.110  92.364  1.00 59.40  ? 175 PHE A O   1 
ATOM   1187  C  CB  . PHE A 1 174 ? 69.293  56.741  90.990  1.00 61.93  ? 175 PHE A CB  1 
ATOM   1188  C  CG  . PHE A 1 174 ? 69.817  57.950  90.270  1.00 63.44  ? 175 PHE A CG  1 
ATOM   1189  C  CD1 . PHE A 1 174 ? 70.270  57.849  88.965  1.00 63.28  ? 175 PHE A CD1 1 
ATOM   1190  C  CD2 . PHE A 1 174 ? 69.864  59.185  90.897  1.00 61.53  ? 175 PHE A CD2 1 
ATOM   1191  C  CE1 . PHE A 1 174 ? 70.758  58.957  88.296  1.00 65.55  ? 175 PHE A CE1 1 
ATOM   1192  C  CE2 . PHE A 1 174 ? 70.351  60.296  90.234  1.00 61.45  ? 175 PHE A CE2 1 
ATOM   1193  C  CZ  . PHE A 1 174 ? 70.796  60.181  88.931  1.00 61.40  ? 175 PHE A CZ  1 
ATOM   1194  N  N   . LYS A 1 175 ? 70.664  56.431  93.845  1.00 61.93  ? 176 LYS A N   1 
ATOM   1195  C  CA  . LYS A 1 175 ? 71.394  56.959  94.993  1.00 63.72  ? 176 LYS A CA  1 
ATOM   1196  C  C   . LYS A 1 175 ? 72.748  56.274  95.140  1.00 70.01  ? 176 LYS A C   1 
ATOM   1197  O  O   . LYS A 1 175 ? 73.758  56.928  95.406  1.00 69.30  ? 176 LYS A O   1 
ATOM   1198  C  CB  . LYS A 1 175 ? 70.592  56.791  96.285  1.00 61.11  ? 176 LYS A CB  1 
ATOM   1199  C  CG  . LYS A 1 175 ? 69.411  57.733  96.429  1.00 63.78  ? 176 LYS A CG  1 
ATOM   1200  C  CD  . LYS A 1 175 ? 68.776  57.586  97.803  1.00 65.96  ? 176 LYS A CD  1 
ATOM   1201  C  CE  . LYS A 1 175 ? 69.817  57.712  98.908  1.00 68.57  ? 176 LYS A CE  1 
ATOM   1202  N  NZ  . LYS A 1 175 ? 69.203  57.629  100.263 1.00 70.23  ? 176 LYS A NZ  1 
ATOM   1203  N  N   . GLN A 1 176 ? 72.764  54.956  94.960  1.00 76.93  ? 177 GLN A N   1 
ATOM   1204  C  CA  . GLN A 1 176 ? 73.982  54.175  95.152  1.00 79.06  ? 177 GLN A CA  1 
ATOM   1205  C  C   . GLN A 1 176 ? 74.989  54.411  94.030  1.00 77.54  ? 177 GLN A C   1 
ATOM   1206  O  O   . GLN A 1 176 ? 76.198  54.386  94.258  1.00 81.60  ? 177 GLN A O   1 
ATOM   1207  C  CB  . GLN A 1 176 ? 73.653  52.684  95.261  1.00 84.59  ? 177 GLN A CB  1 
ATOM   1208  C  CG  . GLN A 1 176 ? 74.812  51.838  95.768  1.00 91.47  ? 177 GLN A CG  1 
ATOM   1209  C  CD  . GLN A 1 176 ? 74.494  50.355  95.803  1.00 94.76  ? 177 GLN A CD  1 
ATOM   1210  O  OE1 . GLN A 1 176 ? 73.523  49.899  95.200  1.00 94.48  ? 177 GLN A OE1 1 
ATOM   1211  N  NE2 . GLN A 1 176 ? 75.310  49.596  96.526  1.00 96.58  ? 177 GLN A NE2 1 
ATOM   1212  N  N   . LEU A 1 177 ? 74.489  54.641  92.819  1.00 72.70  ? 178 LEU A N   1 
ATOM   1213  C  CA  . LEU A 1 177 ? 75.360  54.985  91.699  1.00 71.60  ? 178 LEU A CA  1 
ATOM   1214  C  C   . LEU A 1 177 ? 76.051  56.323  91.932  1.00 73.60  ? 178 LEU A C   1 
ATOM   1215  O  O   . LEU A 1 177 ? 77.192  56.522  91.517  1.00 74.28  ? 178 LEU A O   1 
ATOM   1216  C  CB  . LEU A 1 177 ? 74.576  55.031  90.384  1.00 71.50  ? 178 LEU A CB  1 
ATOM   1217  C  CG  . LEU A 1 177 ? 74.726  53.838  89.436  1.00 71.50  ? 178 LEU A CG  1 
ATOM   1218  C  CD1 . LEU A 1 177 ? 74.103  52.580  90.021  1.00 72.77  ? 178 LEU A CD1 1 
ATOM   1219  C  CD2 . LEU A 1 177 ? 74.139  54.153  88.065  1.00 73.05  ? 178 LEU A CD2 1 
ATOM   1220  N  N   . HIS A 1 178 ? 75.354  57.238  92.598  1.00 70.55  ? 179 HIS A N   1 
ATOM   1221  C  CA  . HIS A 1 178 ? 75.885  58.577  92.826  1.00 69.42  ? 179 HIS A CA  1 
ATOM   1222  C  C   . HIS A 1 178 ? 75.952  58.937  94.309  1.00 67.97  ? 179 HIS A C   1 
ATOM   1223  O  O   . HIS A 1 178 ? 75.087  59.651  94.816  1.00 64.41  ? 179 HIS A O   1 
ATOM   1224  C  CB  . HIS A 1 178 ? 75.036  59.614  92.087  1.00 70.11  ? 179 HIS A CB  1 
ATOM   1225  C  CG  . HIS A 1 178 ? 74.905  59.353  90.619  1.00 71.34  ? 179 HIS A CG  1 
ATOM   1226  N  ND1 . HIS A 1 178 ? 75.849  58.654  89.897  1.00 71.29  ? 179 HIS A ND1 1 
ATOM   1227  C  CD2 . HIS A 1 178 ? 73.935  59.692  89.738  1.00 72.57  ? 179 HIS A CD2 1 
ATOM   1228  C  CE1 . HIS A 1 178 ? 75.468  58.577  88.635  1.00 71.58  ? 179 HIS A CE1 1 
ATOM   1229  N  NE2 . HIS A 1 178 ? 74.309  59.199  88.511  1.00 71.98  ? 179 HIS A NE2 1 
ATOM   1230  N  N   . PRO A 1 179 ? 76.979  58.435  95.013  1.00 68.73  ? 180 PRO A N   1 
ATOM   1231  C  CA  . PRO A 1 179 ? 77.212  58.835  96.405  1.00 76.21  ? 180 PRO A CA  1 
ATOM   1232  C  C   . PRO A 1 179 ? 77.667  60.289  96.489  1.00 86.50  ? 180 PRO A C   1 
ATOM   1233  O  O   . PRO A 1 179 ? 77.459  60.950  97.508  1.00 88.57  ? 180 PRO A O   1 
ATOM   1234  C  CB  . PRO A 1 179 ? 78.324  57.885  96.871  1.00 72.26  ? 180 PRO A CB  1 
ATOM   1235  C  CG  . PRO A 1 179 ? 78.371  56.789  95.847  1.00 69.47  ? 180 PRO A CG  1 
ATOM   1236  C  CD  . PRO A 1 179 ? 77.955  57.430  94.565  1.00 69.59  ? 180 PRO A CD  1 
ATOM   1237  N  N   . GLN A 1 180 ? 78.287  60.768  95.414  1.00 93.95  ? 181 GLN A N   1 
ATOM   1238  C  CA  . GLN A 1 180 ? 78.813  62.127  95.351  1.00 98.45  ? 181 GLN A CA  1 
ATOM   1239  C  C   . GLN A 1 180 ? 77.722  63.171  95.557  1.00 100.67 ? 181 GLN A C   1 
ATOM   1240  O  O   . GLN A 1 180 ? 77.894  64.117  96.326  1.00 104.64 ? 181 GLN A O   1 
ATOM   1241  C  CB  . GLN A 1 180 ? 79.512  62.362  94.009  1.00 101.26 ? 181 GLN A CB  1 
ATOM   1242  N  N   . LEU A 1 181 ? 76.600  62.994  94.869  1.00 97.34  ? 182 LEU A N   1 
ATOM   1243  C  CA  . LEU A 1 181 ? 75.495  63.938  94.966  1.00 95.24  ? 182 LEU A CA  1 
ATOM   1244  C  C   . LEU A 1 181 ? 74.441  63.470  95.962  1.00 92.00  ? 182 LEU A C   1 
ATOM   1245  O  O   . LEU A 1 181 ? 73.912  62.364  95.847  1.00 93.75  ? 182 LEU A O   1 
ATOM   1246  C  CB  . LEU A 1 181 ? 74.854  64.154  93.593  1.00 94.26  ? 182 LEU A CB  1 
ATOM   1247  N  N   . LEU A 1 182 ? 74.144  64.315  96.943  1.00 93.74  ? 183 LEU A N   1 
ATOM   1248  C  CA  . LEU A 1 182 ? 73.052  64.047  97.868  1.00 92.85  ? 183 LEU A CA  1 
ATOM   1249  C  C   . LEU A 1 182 ? 71.746  64.435  97.186  1.00 92.28  ? 183 LEU A C   1 
ATOM   1250  O  O   . LEU A 1 182 ? 71.613  65.549  96.680  1.00 92.49  ? 183 LEU A O   1 
ATOM   1251  C  CB  . LEU A 1 182 ? 73.243  64.812  99.178  1.00 94.97  ? 183 LEU A CB  1 
ATOM   1252  C  CG  . LEU A 1 182 ? 73.039  64.001  100.460 1.00 95.49  ? 183 LEU A CG  1 
ATOM   1253  C  CD1 . LEU A 1 182 ? 73.713  62.640  100.350 1.00 93.19  ? 183 LEU A CD1 1 
ATOM   1254  C  CD2 . LEU A 1 182 ? 73.565  64.764  101.666 1.00 95.91  ? 183 LEU A CD2 1 
ATOM   1255  N  N   . LEU A 1 183 ? 70.787  63.514  97.167  1.00 91.02  ? 184 LEU A N   1 
ATOM   1256  C  CA  . LEU A 1 183 ? 69.596  63.681  96.338  1.00 90.00  ? 184 LEU A CA  1 
ATOM   1257  C  C   . LEU A 1 183 ? 68.285  63.656  97.122  1.00 90.08  ? 184 LEU A C   1 
ATOM   1258  O  O   . LEU A 1 183 ? 67.680  62.598  97.297  1.00 89.26  ? 184 LEU A O   1 
ATOM   1259  C  CB  . LEU A 1 183 ? 69.561  62.598  95.257  1.00 84.99  ? 184 LEU A CB  1 
ATOM   1260  N  N   . PRO A 1 184 ? 67.844  64.832  97.597  1.00 95.32  ? 185 PRO A N   1 
ATOM   1261  C  CA  . PRO A 1 184 ? 66.523  65.017  98.206  1.00 98.17  ? 185 PRO A CA  1 
ATOM   1262  C  C   . PRO A 1 184 ? 65.415  64.990  97.155  1.00 102.27 ? 185 PRO A C   1 
ATOM   1263  O  O   . PRO A 1 184 ? 65.713  65.091  95.964  1.00 103.98 ? 185 PRO A O   1 
ATOM   1264  C  CB  . PRO A 1 184 ? 66.629  66.396  98.859  1.00 96.53  ? 185 PRO A CB  1 
ATOM   1265  C  CG  . PRO A 1 184 ? 67.626  67.116  98.028  1.00 96.12  ? 185 PRO A CG  1 
ATOM   1266  C  CD  . PRO A 1 184 ? 68.628  66.079  97.602  1.00 93.17  ? 185 PRO A CD  1 
ATOM   1267  N  N   . ASP A 1 185 ? 64.168  64.832  97.593  1.00 105.16 ? 186 ASP A N   1 
ATOM   1268  C  CA  . ASP A 1 185 ? 63.015  64.800  96.693  1.00 106.59 ? 186 ASP A CA  1 
ATOM   1269  C  C   . ASP A 1 185 ? 63.000  65.979  95.722  1.00 107.68 ? 186 ASP A C   1 
ATOM   1270  O  O   . ASP A 1 185 ? 63.165  65.803  94.515  1.00 106.27 ? 186 ASP A O   1 
ATOM   1271  C  CB  . ASP A 1 185 ? 61.713  64.787  97.497  1.00 109.08 ? 186 ASP A CB  1 
ATOM   1272  C  CG  . ASP A 1 185 ? 61.826  63.991  98.780  1.00 110.18 ? 186 ASP A CG  1 
ATOM   1273  O  OD1 . ASP A 1 185 ? 62.475  62.924  98.765  1.00 109.59 ? 186 ASP A OD1 1 
ATOM   1274  O  OD2 . ASP A 1 185 ? 61.264  64.432  99.805  1.00 111.37 ? 186 ASP A OD2 1 
ATOM   1275  N  N   . GLY A 1 192 ? 60.851  62.853  93.208  1.00 87.08  ? 193 GLY A N   1 
ATOM   1276  C  CA  . GLY A 1 192 ? 60.123  63.189  91.998  1.00 88.77  ? 193 GLY A CA  1 
ATOM   1277  C  C   . GLY A 1 192 ? 60.994  63.112  90.761  1.00 87.79  ? 193 GLY A C   1 
ATOM   1278  O  O   . GLY A 1 192 ? 61.393  64.139  90.213  1.00 88.59  ? 193 GLY A O   1 
ATOM   1279  N  N   . LYS A 1 193 ? 61.343  61.897  90.346  1.00 91.25  ? 194 LYS A N   1 
ATOM   1280  C  CA  . LYS A 1 193 ? 62.131  61.739  89.133  1.00 95.46  ? 194 LYS A CA  1 
ATOM   1281  C  C   . LYS A 1 193 ? 61.208  61.134  88.080  1.00 101.35 ? 194 LYS A C   1 
ATOM   1282  O  O   . LYS A 1 193 ? 60.876  59.949  88.139  1.00 94.12  ? 194 LYS A O   1 
ATOM   1283  C  CB  . LYS A 1 193 ? 63.367  60.837  89.354  1.00 94.16  ? 194 LYS A CB  1 
ATOM   1284  C  CG  . LYS A 1 193 ? 64.047  60.797  90.759  1.00 89.26  ? 194 LYS A CG  1 
ATOM   1285  C  CD  . LYS A 1 193 ? 63.923  62.055  91.615  1.00 91.12  ? 194 LYS A CD  1 
ATOM   1286  C  CE  . LYS A 1 193 ? 64.156  61.737  93.084  1.00 90.62  ? 194 LYS A CE  1 
ATOM   1287  N  NZ  . LYS A 1 193 ? 63.978  62.924  93.962  1.00 92.08  ? 194 LYS A NZ  1 
ATOM   1288  N  N   . GLN A 1 194 ? 60.793  61.947  87.115  1.00 107.77 ? 195 GLN A N   1 
ATOM   1289  C  CA  . GLN A 1 194 ? 59.899  61.465  86.069  1.00 113.07 ? 195 GLN A CA  1 
ATOM   1290  C  C   . GLN A 1 194 ? 60.678  61.123  84.795  1.00 115.48 ? 195 GLN A C   1 
ATOM   1291  O  O   . GLN A 1 194 ? 60.093  60.801  83.761  1.00 117.41 ? 195 GLN A O   1 
ATOM   1292  C  CB  . GLN A 1 194 ? 58.783  62.480  85.797  1.00 115.53 ? 195 GLN A CB  1 
ATOM   1293  C  CG  . GLN A 1 194 ? 57.601  61.928  84.978  1.00 117.71 ? 195 GLN A CG  1 
ATOM   1294  C  CD  . GLN A 1 194 ? 56.890  60.725  85.601  1.00 118.41 ? 195 GLN A CD  1 
ATOM   1295  O  OE1 . GLN A 1 194 ? 57.088  60.386  86.770  1.00 118.98 ? 195 GLN A OE1 1 
ATOM   1296  N  NE2 . GLN A 1 194 ? 56.067  60.062  84.797  1.00 118.82 ? 195 GLN A NE2 1 
ATOM   1297  N  N   . ALA A 1 195 ? 62.004  61.225  84.864  1.00 118.99 ? 196 ALA A N   1 
ATOM   1298  C  CA  . ALA A 1 195 ? 62.864  60.836  83.746  1.00 118.52 ? 196 ALA A CA  1 
ATOM   1299  C  C   . ALA A 1 195 ? 62.601  59.384  83.347  1.00 115.17 ? 196 ALA A C   1 
ATOM   1300  O  O   . ALA A 1 195 ? 62.933  58.969  82.239  1.00 120.55 ? 196 ALA A O   1 
ATOM   1301  C  CB  . ALA A 1 195 ? 64.325  61.037  84.104  1.00 122.18 ? 196 ALA A CB  1 
ATOM   1302  N  N   . GLU A 1 196 ? 61.980  58.629  84.248  1.00 103.27 ? 197 GLU A N   1 
ATOM   1303  C  CA  . GLU A 1 196 ? 61.525  57.281  83.949  1.00 98.42  ? 197 GLU A CA  1 
ATOM   1304  C  C   . GLU A 1 196 ? 60.470  57.351  82.851  1.00 100.51 ? 197 GLU A C   1 
ATOM   1305  O  O   . GLU A 1 196 ? 59.863  58.398  82.634  1.00 99.65  ? 197 GLU A O   1 
ATOM   1306  C  CB  . GLU A 1 196 ? 60.967  56.600  85.197  1.00 93.52  ? 197 GLU A CB  1 
ATOM   1307  N  N   . ALA A 1 197 ? 60.268  56.224  82.174  1.00 108.59 ? 198 ALA A N   1 
ATOM   1308  C  CA  . ALA A 1 197 ? 59.663  56.151  80.843  1.00 109.85 ? 198 ALA A CA  1 
ATOM   1309  C  C   . ALA A 1 197 ? 60.587  56.805  79.817  1.00 108.17 ? 198 ALA A C   1 
ATOM   1310  O  O   . ALA A 1 197 ? 60.150  57.267  78.763  1.00 111.26 ? 198 ALA A O   1 
ATOM   1311  C  CB  . ALA A 1 197 ? 58.272  56.791  80.812  1.00 111.88 ? 198 ALA A CB  1 
ATOM   1312  N  N   . LEU A 1 198 ? 61.874  56.843  80.154  1.00 98.19  ? 199 LEU A N   1 
ATOM   1313  C  CA  . LEU A 1 198 ? 62.929  56.745  79.157  1.00 90.49  ? 199 LEU A CA  1 
ATOM   1314  C  C   . LEU A 1 198 ? 63.287  55.266  79.184  1.00 81.47  ? 199 LEU A C   1 
ATOM   1315  O  O   . LEU A 1 198 ? 64.132  54.788  78.426  1.00 83.12  ? 199 LEU A O   1 
ATOM   1316  C  CB  . LEU A 1 198 ? 64.133  57.650  79.465  1.00 88.18  ? 199 LEU A CB  1 
ATOM   1317  C  CG  . LEU A 1 198 ? 65.160  57.348  80.566  1.00 84.86  ? 199 LEU A CG  1 
ATOM   1318  C  CD1 . LEU A 1 198 ? 66.260  56.404  80.095  1.00 82.23  ? 199 LEU A CD1 1 
ATOM   1319  C  CD2 . LEU A 1 198 ? 65.782  58.646  81.060  1.00 85.24  ? 199 LEU A CD2 1 
ATOM   1320  N  N   . ARG A 1 199 ? 62.599  54.561  80.082  1.00 75.78  ? 200 ARG A N   1 
ATOM   1321  C  CA  . ARG A 1 199 ? 62.786  53.136  80.332  1.00 66.77  ? 200 ARG A CA  1 
ATOM   1322  C  C   . ARG A 1 199 ? 64.228  52.789  80.689  1.00 63.48  ? 200 ARG A C   1 
ATOM   1323  O  O   . ARG A 1 199 ? 64.931  52.152  79.904  1.00 62.30  ? 200 ARG A O   1 
ATOM   1324  C  CB  . ARG A 1 199 ? 62.317  52.322  79.126  1.00 71.74  ? 200 ARG A CB  1 
ATOM   1325  C  CG  . ARG A 1 199 ? 60.811  52.107  79.103  1.00 76.24  ? 200 ARG A CG  1 
ATOM   1326  C  CD  . ARG A 1 199 ? 60.266  52.036  77.689  1.00 82.31  ? 200 ARG A CD  1 
ATOM   1327  N  NE  . ARG A 1 199 ? 58.887  51.555  77.667  1.00 88.00  ? 200 ARG A NE  1 
ATOM   1328  C  CZ  . ARG A 1 199 ? 58.277  51.082  76.586  1.00 93.94  ? 200 ARG A CZ  1 
ATOM   1329  N  NH1 . ARG A 1 199 ? 58.922  51.030  75.428  1.00 96.74  ? 200 ARG A NH1 1 
ATOM   1330  N  NH2 . ARG A 1 199 ? 57.021  50.664  76.660  1.00 96.09  ? 200 ARG A NH2 1 
ATOM   1331  N  N   . PRO A 1 200 ? 64.672  53.212  81.885  1.00 56.33  ? 201 PRO A N   1 
ATOM   1332  C  CA  . PRO A 1 200 ? 66.036  52.938  82.347  1.00 56.13  ? 201 PRO A CA  1 
ATOM   1333  C  C   . PRO A 1 200 ? 66.293  51.448  82.549  1.00 54.25  ? 201 PRO A C   1 
ATOM   1334  O  O   . PRO A 1 200 ? 67.427  51.001  82.385  1.00 56.89  ? 201 PRO A O   1 
ATOM   1335  C  CB  . PRO A 1 200 ? 66.114  53.691  83.680  1.00 54.17  ? 201 PRO A CB  1 
ATOM   1336  C  CG  . PRO A 1 200 ? 64.703  53.789  84.142  1.00 51.74  ? 201 PRO A CG  1 
ATOM   1337  C  CD  . PRO A 1 200 ? 63.882  53.936  82.898  1.00 53.84  ? 201 PRO A CD  1 
ATOM   1338  N  N   . PHE A 1 201 ? 65.256  50.694  82.902  1.00 51.86  ? 202 PHE A N   1 
ATOM   1339  C  CA  . PHE A 1 201 ? 65.395  49.256  83.117  1.00 48.45  ? 202 PHE A CA  1 
ATOM   1340  C  C   . PHE A 1 201 ? 65.125  48.457  81.844  1.00 56.51  ? 202 PHE A C   1 
ATOM   1341  O  O   . PHE A 1 201 ? 65.145  47.225  81.861  1.00 57.70  ? 202 PHE A O   1 
ATOM   1342  C  CB  . PHE A 1 201 ? 64.455  48.781  84.226  1.00 49.02  ? 202 PHE A CB  1 
ATOM   1343  C  CG  . PHE A 1 201 ? 64.819  49.283  85.594  1.00 40.99  ? 202 PHE A CG  1 
ATOM   1344  C  CD1 . PHE A 1 201 ? 66.015  48.915  86.188  1.00 41.89  ? 202 PHE A CD1 1 
ATOM   1345  C  CD2 . PHE A 1 201 ? 63.951  50.101  86.298  1.00 39.00  ? 202 PHE A CD2 1 
ATOM   1346  C  CE1 . PHE A 1 201 ? 66.347  49.370  87.452  1.00 46.34  ? 202 PHE A CE1 1 
ATOM   1347  C  CE2 . PHE A 1 201 ? 64.276  50.557  87.563  1.00 42.79  ? 202 PHE A CE2 1 
ATOM   1348  C  CZ  . PHE A 1 201 ? 65.475  50.192  88.140  1.00 44.51  ? 202 PHE A CZ  1 
ATOM   1349  N  N   . GLY A 1 202 ? 64.863  49.158  80.746  1.00 54.17  ? 203 GLY A N   1 
ATOM   1350  C  CA  . GLY A 1 202 ? 64.574  48.506  79.482  1.00 59.83  ? 203 GLY A CA  1 
ATOM   1351  C  C   . GLY A 1 202 ? 63.142  48.011  79.393  1.00 60.54  ? 203 GLY A C   1 
ATOM   1352  O  O   . GLY A 1 202 ? 62.227  48.626  79.943  1.00 64.82  ? 203 GLY A O   1 
ATOM   1353  N  N   . GLU A 1 203 ? 62.948  46.896  78.697  1.00 59.03  ? 204 GLU A N   1 
ATOM   1354  C  CA  . GLU A 1 203 ? 61.614  46.341  78.489  1.00 58.40  ? 204 GLU A CA  1 
ATOM   1355  C  C   . GLU A 1 203 ? 61.254  45.323  79.566  1.00 49.63  ? 204 GLU A C   1 
ATOM   1356  O  O   . GLU A 1 203 ? 60.118  44.853  79.634  1.00 49.74  ? 204 GLU A O   1 
ATOM   1357  C  CB  . GLU A 1 203 ? 61.515  45.686  77.109  1.00 67.89  ? 204 GLU A CB  1 
ATOM   1358  C  CG  . GLU A 1 203 ? 62.528  46.197  76.098  1.00 80.15  ? 204 GLU A CG  1 
ATOM   1359  C  CD  . GLU A 1 203 ? 62.396  45.513  74.750  1.00 89.34  ? 204 GLU A CD  1 
ATOM   1360  O  OE1 . GLU A 1 203 ? 61.501  45.900  73.969  1.00 92.72  ? 204 GLU A OE1 1 
ATOM   1361  O  OE2 . GLU A 1 203 ? 63.184  44.584  74.473  1.00 92.54  ? 204 GLU A OE2 1 
ATOM   1362  N  N   . ALA A 1 204 ? 62.232  44.990  80.402  1.00 41.07  ? 205 ALA A N   1 
ATOM   1363  C  CA  . ALA A 1 204 ? 62.069  43.956  81.422  1.00 44.25  ? 205 ALA A CA  1 
ATOM   1364  C  C   . ALA A 1 204 ? 60.925  44.205  82.422  1.00 40.93  ? 205 ALA A C   1 
ATOM   1365  O  O   . ALA A 1 204 ? 60.218  43.261  82.773  1.00 49.39  ? 205 ALA A O   1 
ATOM   1366  C  CB  . ALA A 1 204 ? 63.385  43.759  82.172  1.00 40.18  ? 205 ALA A CB  1 
ATOM   1367  N  N   . PRO A 1 205 ? 60.742  45.456  82.898  1.00 38.79  ? 206 PRO A N   1 
ATOM   1368  C  CA  . PRO A 1 205 ? 59.596  45.660  83.797  1.00 41.61  ? 206 PRO A CA  1 
ATOM   1369  C  C   . PRO A 1 205 ? 58.242  45.349  83.153  1.00 40.87  ? 206 PRO A C   1 
ATOM   1370  O  O   . PRO A 1 205 ? 57.357  44.808  83.820  1.00 40.55  ? 206 PRO A O   1 
ATOM   1371  C  CB  . PRO A 1 205 ? 59.690  47.147  84.149  1.00 40.32  ? 206 PRO A CB  1 
ATOM   1372  C  CG  . PRO A 1 205 ? 61.130  47.467  84.013  1.00 42.96  ? 206 PRO A CG  1 
ATOM   1373  C  CD  . PRO A 1 205 ? 61.607  46.651  82.849  1.00 42.30  ? 206 PRO A CD  1 
ATOM   1374  N  N   . ARG A 1 206 ? 58.089  45.686  81.877  1.00 37.84  ? 207 ARG A N   1 
ATOM   1375  C  CA  . ARG A 1 206 ? 56.839  45.437  81.167  1.00 42.91  ? 207 ARG A CA  1 
ATOM   1376  C  C   . ARG A 1 206 ? 56.625  43.943  80.927  1.00 37.28  ? 207 ARG A C   1 
ATOM   1377  O  O   . ARG A 1 206 ? 55.550  43.404  81.214  1.00 30.31  ? 207 ARG A O   1 
ATOM   1378  C  CB  . ARG A 1 206 ? 56.819  46.196  79.838  1.00 38.26  ? 207 ARG A CB  1 
ATOM   1379  C  CG  . ARG A 1 206 ? 55.602  45.902  78.978  1.00 47.44  ? 207 ARG A CG  1 
ATOM   1380  C  CD  . ARG A 1 206 ? 55.603  46.741  77.712  1.00 55.70  ? 207 ARG A CD  1 
ATOM   1381  N  NE  . ARG A 1 206 ? 54.542  46.340  76.794  1.00 64.66  ? 207 ARG A NE  1 
ATOM   1382  C  CZ  . ARG A 1 206 ? 54.751  45.904  75.556  1.00 75.04  ? 207 ARG A CZ  1 
ATOM   1383  N  NH1 . ARG A 1 206 ? 55.987  45.818  75.082  1.00 78.30  ? 207 ARG A NH1 1 
ATOM   1384  N  NH2 . ARG A 1 206 ? 53.726  45.557  74.790  1.00 78.27  ? 207 ARG A NH2 1 
ATOM   1385  N  N   . GLU A 1 207 ? 57.653  43.285  80.397  1.00 34.41  ? 208 GLU A N   1 
ATOM   1386  C  CA  . GLU A 1 207 ? 57.627  41.842  80.181  1.00 38.44  ? 208 GLU A CA  1 
ATOM   1387  C  C   . GLU A 1 207 ? 57.259  41.113  81.467  1.00 41.12  ? 208 GLU A C   1 
ATOM   1388  O  O   . GLU A 1 207 ? 56.362  40.261  81.480  1.00 37.23  ? 208 GLU A O   1 
ATOM   1389  C  CB  . GLU A 1 207 ? 58.983  41.350  79.666  1.00 44.65  ? 208 GLU A CB  1 
ATOM   1390  C  CG  . GLU A 1 207 ? 59.265  41.695  78.214  1.00 51.19  ? 208 GLU A CG  1 
ATOM   1391  C  CD  . GLU A 1 207 ? 58.370  40.941  77.250  1.00 61.82  ? 208 GLU A CD  1 
ATOM   1392  O  OE1 . GLU A 1 207 ? 58.135  41.448  76.133  1.00 66.25  ? 208 GLU A OE1 1 
ATOM   1393  O  OE2 . GLU A 1 207 ? 57.906  39.837  77.608  1.00 63.77  ? 208 GLU A OE2 1 
ATOM   1394  N  N   . LEU A 1 208 ? 57.948  41.468  82.548  1.00 41.62  ? 209 LEU A N   1 
ATOM   1395  C  CA  . LEU A 1 208 ? 57.672  40.892  83.856  1.00 45.12  ? 209 LEU A CA  1 
ATOM   1396  C  C   . LEU A 1 208 ? 56.235  41.164  84.281  1.00 36.73  ? 209 LEU A C   1 
ATOM   1397  O  O   . LEU A 1 208 ? 55.567  40.277  84.807  1.00 27.07  ? 209 LEU A O   1 
ATOM   1398  C  CB  . LEU A 1 208 ? 58.638  41.439  84.909  1.00 41.13  ? 209 LEU A CB  1 
ATOM   1399  C  CG  . LEU A 1 208 ? 58.465  40.839  86.305  1.00 38.27  ? 209 LEU A CG  1 
ATOM   1400  C  CD1 . LEU A 1 208 ? 58.636  39.324  86.258  1.00 33.82  ? 209 LEU A CD1 1 
ATOM   1401  C  CD2 . LEU A 1 208 ? 59.435  41.462  87.295  1.00 27.53  ? 209 LEU A CD2 1 
ATOM   1402  N  N   . ARG A 1 209 ? 55.763  42.387  84.047  1.00 39.48  ? 210 ARG A N   1 
ATOM   1403  C  CA  . ARG A 1 209 ? 54.395  42.752  84.406  1.00 35.92  ? 210 ARG A CA  1 
ATOM   1404  C  C   . ARG A 1 209 ? 53.387  41.829  83.730  1.00 37.71  ? 210 ARG A C   1 
ATOM   1405  O  O   . ARG A 1 209 ? 52.617  41.137  84.401  1.00 34.37  ? 210 ARG A O   1 
ATOM   1406  C  CB  . ARG A 1 209 ? 54.094  44.205  84.030  1.00 41.55  ? 210 ARG A CB  1 
ATOM   1407  C  CG  . ARG A 1 209 ? 52.746  44.694  84.548  1.00 42.27  ? 210 ARG A CG  1 
ATOM   1408  C  CD  . ARG A 1 209 ? 52.417  46.110  84.083  1.00 50.46  ? 210 ARG A CD  1 
ATOM   1409  N  NE  . ARG A 1 209 ? 51.864  46.141  82.731  1.00 54.13  ? 210 ARG A NE  1 
ATOM   1410  C  CZ  . ARG A 1 209 ? 52.505  46.615  81.668  1.00 57.59  ? 210 ARG A CZ  1 
ATOM   1411  N  NH1 . ARG A 1 209 ? 53.728  47.110  81.794  1.00 57.08  ? 210 ARG A NH1 1 
ATOM   1412  N  NH2 . ARG A 1 209 ? 51.920  46.600  80.478  1.00 59.08  ? 210 ARG A NH2 1 
ATOM   1413  N  N   . LEU A 1 210 ? 53.410  41.820  82.400  1.00 32.54  ? 211 LEU A N   1 
ATOM   1414  C  CA  . LEU A 1 210 ? 52.481  41.015  81.616  1.00 34.58  ? 211 LEU A CA  1 
ATOM   1415  C  C   . LEU A 1 210 ? 52.562  39.534  81.985  1.00 35.64  ? 211 LEU A C   1 
ATOM   1416  O  O   . LEU A 1 210 ? 51.555  38.915  82.370  1.00 40.69  ? 211 LEU A O   1 
ATOM   1417  C  CB  . LEU A 1 210 ? 52.758  41.196  80.122  1.00 33.27  ? 211 LEU A CB  1 
ATOM   1418  C  CG  . LEU A 1 210 ? 52.472  42.581  79.538  1.00 42.15  ? 211 LEU A CG  1 
ATOM   1419  C  CD1 . LEU A 1 210 ? 53.081  42.715  78.151  1.00 44.94  ? 211 LEU A CD1 1 
ATOM   1420  C  CD2 . LEU A 1 210 ? 50.975  42.846  79.497  1.00 39.78  ? 211 LEU A CD2 1 
ATOM   1421  N  N   . ARG A 1 211 ? 53.768  38.981  81.879  1.00 29.96  ? 212 ARG A N   1 
ATOM   1422  C  CA  . ARG A 1 211 ? 53.980  37.557  82.113  1.00 34.43  ? 212 ARG A CA  1 
ATOM   1423  C  C   . ARG A 1 211 ? 53.551  37.124  83.510  1.00 40.67  ? 212 ARG A C   1 
ATOM   1424  O  O   . ARG A 1 211 ? 52.836  36.134  83.657  1.00 40.26  ? 212 ARG A O   1 
ATOM   1425  C  CB  . ARG A 1 211 ? 55.446  37.191  81.877  1.00 27.90  ? 212 ARG A CB  1 
ATOM   1426  C  CG  . ARG A 1 211 ? 55.847  37.231  80.414  1.00 27.59  ? 212 ARG A CG  1 
ATOM   1427  C  CD  . ARG A 1 211 ? 57.301  36.845  80.214  1.00 31.79  ? 212 ARG A CD  1 
ATOM   1428  N  NE  . ARG A 1 211 ? 57.656  36.836  78.798  1.00 35.10  ? 212 ARG A NE  1 
ATOM   1429  C  CZ  . ARG A 1 211 ? 57.479  35.796  77.990  1.00 43.06  ? 212 ARG A CZ  1 
ATOM   1430  N  NH1 . ARG A 1 211 ? 57.830  35.879  76.714  1.00 44.57  ? 212 ARG A NH1 1 
ATOM   1431  N  NH2 . ARG A 1 211 ? 56.949  34.672  78.457  1.00 45.41  ? 212 ARG A NH2 1 
ATOM   1432  N  N   . ALA A 1 212 ? 53.972  37.863  84.532  1.00 31.87  ? 213 ALA A N   1 
ATOM   1433  C  CA  . ALA A 1 212 ? 53.610  37.509  85.901  1.00 34.25  ? 213 ALA A CA  1 
ATOM   1434  C  C   . ALA A 1 212 ? 52.104  37.624  86.107  1.00 34.91  ? 213 ALA A C   1 
ATOM   1435  O  O   . ALA A 1 212 ? 51.484  36.744  86.718  1.00 37.49  ? 213 ALA A O   1 
ATOM   1436  C  CB  . ALA A 1 212 ? 54.351  38.379  86.898  1.00 25.63  ? 213 ALA A CB  1 
ATOM   1437  N  N   . THR A 1 213 ? 51.525  38.707  85.589  1.00 35.12  ? 214 THR A N   1 
ATOM   1438  C  CA  . THR A 1 213 ? 50.089  38.939  85.706  1.00 37.31  ? 214 THR A CA  1 
ATOM   1439  C  C   . THR A 1 213 ? 49.288  37.771  85.142  1.00 40.51  ? 214 THR A C   1 
ATOM   1440  O  O   . THR A 1 213 ? 48.374  37.270  85.794  1.00 32.54  ? 214 THR A O   1 
ATOM   1441  C  CB  . THR A 1 213 ? 49.659  40.230  84.988  1.00 38.98  ? 214 THR A CB  1 
ATOM   1442  O  OG1 . THR A 1 213 ? 50.260  41.360  85.634  1.00 49.74  ? 214 THR A OG1 1 
ATOM   1443  C  CG2 . THR A 1 213 ? 48.148  40.380  85.026  1.00 44.20  ? 214 THR A CG2 1 
ATOM   1444  N  N   . ARG A 1 214 ? 49.637  37.334  83.937  1.00 30.37  ? 215 ARG A N   1 
ATOM   1445  C  CA  . ARG A 1 214 ? 48.957  36.192  83.329  1.00 37.45  ? 215 ARG A CA  1 
ATOM   1446  C  C   . ARG A 1 214 ? 49.208  34.884  84.095  1.00 37.35  ? 215 ARG A C   1 
ATOM   1447  O  O   . ARG A 1 214 ? 48.271  34.222  84.577  1.00 33.90  ? 215 ARG A O   1 
ATOM   1448  C  CB  . ARG A 1 214 ? 49.399  36.041  81.871  1.00 34.71  ? 215 ARG A CB  1 
ATOM   1449  C  CG  . ARG A 1 214 ? 49.100  34.683  81.262  1.00 32.28  ? 215 ARG A CG  1 
ATOM   1450  C  CD  . ARG A 1 214 ? 49.573  34.601  79.816  1.00 27.30  ? 215 ARG A CD  1 
ATOM   1451  N  NE  . ARG A 1 214 ? 50.944  35.077  79.646  1.00 29.05  ? 215 ARG A NE  1 
ATOM   1452  C  CZ  . ARG A 1 214 ? 52.028  34.409  80.032  1.00 36.18  ? 215 ARG A CZ  1 
ATOM   1453  N  NH1 . ARG A 1 214 ? 53.231  34.928  79.829  1.00 41.99  ? 215 ARG A NH1 1 
ATOM   1454  N  NH2 . ARG A 1 214 ? 51.914  33.229  80.627  1.00 31.09  ? 215 ARG A NH2 1 
ATOM   1455  N  N   . ALA A 1 215 ? 50.485  34.536  84.221  1.00 29.93  ? 216 ALA A N   1 
ATOM   1456  C  CA  . ALA A 1 215 ? 50.897  33.228  84.715  1.00 33.50  ? 216 ALA A CA  1 
ATOM   1457  C  C   . ALA A 1 215 ? 50.516  32.960  86.169  1.00 34.88  ? 216 ALA A C   1 
ATOM   1458  O  O   . ALA A 1 215 ? 50.128  31.841  86.508  1.00 26.00  ? 216 ALA A O   1 
ATOM   1459  C  CB  . ALA A 1 215 ? 52.398  33.063  84.539  1.00 27.33  ? 216 ALA A CB  1 
ATOM   1460  N  N   . PHE A 1 216 ? 50.628  33.966  87.033  1.00 26.56  ? 217 PHE A N   1 
ATOM   1461  C  CA  . PHE A 1 216 ? 50.380  33.726  88.453  1.00 29.71  ? 217 PHE A CA  1 
ATOM   1462  C  C   . PHE A 1 216 ? 48.891  33.545  88.761  1.00 32.48  ? 217 PHE A C   1 
ATOM   1463  O  O   . PHE A 1 216 ? 48.516  32.670  89.552  1.00 39.20  ? 217 PHE A O   1 
ATOM   1464  C  CB  . PHE A 1 216 ? 50.978  34.851  89.300  1.00 30.44  ? 217 PHE A CB  1 
ATOM   1465  C  CG  . PHE A 1 216 ? 52.438  34.657  89.606  1.00 32.16  ? 217 PHE A CG  1 
ATOM   1466  C  CD1 . PHE A 1 216 ? 52.836  33.852  90.661  1.00 36.69  ? 217 PHE A CD1 1 
ATOM   1467  C  CD2 . PHE A 1 216 ? 53.413  35.262  88.828  1.00 27.17  ? 217 PHE A CD2 1 
ATOM   1468  C  CE1 . PHE A 1 216 ? 54.177  33.662  90.943  1.00 35.46  ? 217 PHE A CE1 1 
ATOM   1469  C  CE2 . PHE A 1 216 ? 54.755  35.077  89.104  1.00 24.32  ? 217 PHE A CE2 1 
ATOM   1470  C  CZ  . PHE A 1 216 ? 55.138  34.275  90.163  1.00 36.56  ? 217 PHE A CZ  1 
ATOM   1471  N  N   . VAL A 1 217 ? 48.040  34.347  88.126  1.00 31.12  ? 218 VAL A N   1 
ATOM   1472  C  CA  . VAL A 1 217 ? 46.604  34.178  88.310  1.00 36.79  ? 218 VAL A CA  1 
ATOM   1473  C  C   . VAL A 1 217 ? 46.154  32.895  87.611  1.00 30.66  ? 218 VAL A C   1 
ATOM   1474  O  O   . VAL A 1 217 ? 45.227  32.225  88.075  1.00 23.57  ? 218 VAL A O   1 
ATOM   1475  C  CB  . VAL A 1 217 ? 45.790  35.396  87.793  1.00 39.34  ? 218 VAL A CB  1 
ATOM   1476  C  CG1 . VAL A 1 217 ? 45.844  35.502  86.278  1.00 40.28  ? 218 VAL A CG1 1 
ATOM   1477  C  CG2 . VAL A 1 217 ? 44.345  35.309  88.267  1.00 38.24  ? 218 VAL A CG2 1 
ATOM   1478  N  N   . ALA A 1 218 ? 46.825  32.538  86.514  1.00 26.48  ? 219 ALA A N   1 
ATOM   1479  C  CA  . ALA A 1 218 ? 46.549  31.261  85.860  1.00 31.21  ? 219 ALA A CA  1 
ATOM   1480  C  C   . ALA A 1 218 ? 46.799  30.099  86.822  1.00 27.38  ? 219 ALA A C   1 
ATOM   1481  O  O   . ALA A 1 218 ? 45.916  29.266  87.062  1.00 28.64  ? 219 ALA A O   1 
ATOM   1482  C  CB  . ALA A 1 218 ? 47.396  31.108  84.609  1.00 23.48  ? 219 ALA A CB  1 
ATOM   1483  N  N   . ALA A 1 219 ? 48.006  30.065  87.381  1.00 33.27  ? 220 ALA A N   1 
ATOM   1484  C  CA  . ALA A 1 219 ? 48.410  29.027  88.325  1.00 30.86  ? 220 ALA A CA  1 
ATOM   1485  C  C   . ALA A 1 219 ? 47.471  28.949  89.526  1.00 27.14  ? 220 ALA A C   1 
ATOM   1486  O  O   . ALA A 1 219 ? 46.980  27.864  89.890  1.00 27.34  ? 220 ALA A O   1 
ATOM   1487  C  CB  . ALA A 1 219 ? 49.835  29.278  88.791  1.00 28.73  ? 220 ALA A CB  1 
ATOM   1488  N  N   . ARG A 1 220 ? 47.229  30.106  90.137  1.00 24.91  ? 221 ARG A N   1 
ATOM   1489  C  CA  . ARG A 1 220 ? 46.360  30.185  91.305  1.00 29.35  ? 221 ARG A CA  1 
ATOM   1490  C  C   . ARG A 1 220 ? 44.959  29.664  91.005  1.00 26.45  ? 221 ARG A C   1 
ATOM   1491  O  O   . ARG A 1 220 ? 44.394  28.899  91.787  1.00 27.87  ? 221 ARG A O   1 
ATOM   1492  C  CB  . ARG A 1 220 ? 46.272  31.623  91.816  1.00 33.41  ? 221 ARG A CB  1 
ATOM   1493  C  CG  . ARG A 1 220 ? 45.484  31.757  93.108  1.00 36.72  ? 221 ARG A CG  1 
ATOM   1494  C  CD  . ARG A 1 220 ? 44.640  33.016  93.114  1.00 44.93  ? 221 ARG A CD  1 
ATOM   1495  N  NE  . ARG A 1 220 ? 45.452  34.227  93.087  1.00 49.09  ? 221 ARG A NE  1 
ATOM   1496  C  CZ  . ARG A 1 220 ? 45.026  35.398  92.624  1.00 54.03  ? 221 ARG A CZ  1 
ATOM   1497  N  NH1 . ARG A 1 220 ? 43.797  35.513  92.142  1.00 54.75  ? 221 ARG A NH1 1 
ATOM   1498  N  NH2 . ARG A 1 220 ? 45.831  36.451  92.638  1.00 54.05  ? 221 ARG A NH2 1 
ATOM   1499  N  N   . SER A 1 221 ? 44.402  30.080  89.871  1.00 29.94  ? 222 SER A N   1 
ATOM   1500  C  CA  A SER A 1 221 ? 43.056  29.670  89.492  0.68 31.08  ? 222 SER A CA  1 
ATOM   1501  C  CA  B SER A 1 221 ? 43.055  29.670  89.491  0.32 31.55  ? 222 SER A CA  1 
ATOM   1502  C  C   . SER A 1 221 ? 42.992  28.171  89.216  1.00 32.50  ? 222 SER A C   1 
ATOM   1503  O  O   . SER A 1 221 ? 42.004  27.511  89.546  1.00 22.99  ? 222 SER A O   1 
ATOM   1504  C  CB  A SER A 1 221 ? 42.583  30.455  88.269  0.68 28.70  ? 222 SER A CB  1 
ATOM   1505  C  CB  B SER A 1 221 ? 42.578  30.451  88.265  0.32 29.11  ? 222 SER A CB  1 
ATOM   1506  O  OG  A SER A 1 221 ? 42.562  31.845  88.542  0.68 29.94  ? 222 SER A OG  1 
ATOM   1507  O  OG  B SER A 1 221 ? 43.377  30.162  87.131  0.32 25.70  ? 222 SER A OG  1 
ATOM   1508  N  N   . PHE A 1 222 ? 44.047  27.636  88.610  1.00 29.07  ? 223 PHE A N   1 
ATOM   1509  C  CA  . PHE A 1 222 ? 44.104  26.203  88.337  1.00 28.01  ? 223 PHE A CA  1 
ATOM   1510  C  C   . PHE A 1 222 ? 44.105  25.405  89.643  1.00 29.79  ? 223 PHE A C   1 
ATOM   1511  O  O   . PHE A 1 222 ? 43.287  24.487  89.834  1.00 24.05  ? 223 PHE A O   1 
ATOM   1512  C  CB  . PHE A 1 222 ? 45.340  25.865  87.500  1.00 26.26  ? 223 PHE A CB  1 
ATOM   1513  C  CG  . PHE A 1 222 ? 45.455  24.409  87.146  1.00 31.19  ? 223 PHE A CG  1 
ATOM   1514  C  CD1 . PHE A 1 222 ? 44.708  23.873  86.109  1.00 24.07  ? 223 PHE A CD1 1 
ATOM   1515  C  CD2 . PHE A 1 222 ? 46.317  23.579  87.842  1.00 29.32  ? 223 PHE A CD2 1 
ATOM   1516  C  CE1 . PHE A 1 222 ? 44.812  22.536  85.780  1.00 24.98  ? 223 PHE A CE1 1 
ATOM   1517  C  CE2 . PHE A 1 222 ? 46.429  22.240  87.515  1.00 28.83  ? 223 PHE A CE2 1 
ATOM   1518  C  CZ  . PHE A 1 222 ? 45.675  21.718  86.484  1.00 29.73  ? 223 PHE A CZ  1 
ATOM   1519  N  N   . VAL A 1 223 ? 45.016  25.768  90.545  1.00 27.40  ? 224 VAL A N   1 
ATOM   1520  C  CA  . VAL A 1 223 ? 45.104  25.099  91.844  1.00 33.38  ? 224 VAL A CA  1 
ATOM   1521  C  C   . VAL A 1 223 ? 43.777  25.189  92.614  1.00 31.61  ? 224 VAL A C   1 
ATOM   1522  O  O   . VAL A 1 223 ? 43.280  24.186  93.156  1.00 25.19  ? 224 VAL A O   1 
ATOM   1523  C  CB  . VAL A 1 223 ? 46.253  25.693  92.688  1.00 30.19  ? 224 VAL A CB  1 
ATOM   1524  C  CG1 . VAL A 1 223 ? 46.089  25.350  94.161  1.00 33.42  ? 224 VAL A CG1 1 
ATOM   1525  C  CG2 . VAL A 1 223 ? 47.597  25.206  92.161  1.00 27.09  ? 224 VAL A CG2 1 
ATOM   1526  N  N   . GLN A 1 224 ? 43.203  26.390  92.638  1.00 29.17  ? 225 GLN A N   1 
ATOM   1527  C  CA  . GLN A 1 224 ? 41.896  26.622  93.250  1.00 34.17  ? 225 GLN A CA  1 
ATOM   1528  C  C   . GLN A 1 224 ? 40.829  25.701  92.662  1.00 29.96  ? 225 GLN A C   1 
ATOM   1529  O  O   . GLN A 1 224 ? 40.002  25.149  93.389  1.00 23.96  ? 225 GLN A O   1 
ATOM   1530  C  CB  . GLN A 1 224 ? 41.476  28.081  93.072  1.00 40.72  ? 225 GLN A CB  1 
ATOM   1531  C  CG  . GLN A 1 224 ? 41.597  28.926  94.328  1.00 52.19  ? 225 GLN A CG  1 
ATOM   1532  C  CD  . GLN A 1 224 ? 41.469  30.411  94.044  1.00 62.88  ? 225 GLN A CD  1 
ATOM   1533  O  OE1 . GLN A 1 224 ? 41.271  30.821  92.899  1.00 64.02  ? 225 GLN A OE1 1 
ATOM   1534  N  NE2 . GLN A 1 224 ? 41.577  31.225  95.087  1.00 66.38  ? 225 GLN A NE2 1 
ATOM   1535  N  N   . GLY A 1 225 ? 40.859  25.544  91.341  1.00 27.87  ? 226 GLY A N   1 
ATOM   1536  C  CA  . GLY A 1 225 ? 39.945  24.654  90.649  1.00 23.19  ? 226 GLY A CA  1 
ATOM   1537  C  C   . GLY A 1 225 ? 40.100  23.212  91.091  1.00 30.48  ? 226 GLY A C   1 
ATOM   1538  O  O   . GLY A 1 225 ? 39.106  22.517  91.332  1.00 23.43  ? 226 GLY A O   1 
ATOM   1539  N  N   . LEU A 1 226 ? 41.345  22.753  91.196  1.00 26.74  ? 227 LEU A N   1 
ATOM   1540  C  CA  . LEU A 1 226 ? 41.594  21.402  91.697  1.00 25.71  ? 227 LEU A CA  1 
ATOM   1541  C  C   . LEU A 1 226 ? 41.011  21.227  93.098  1.00 23.78  ? 227 LEU A C   1 
ATOM   1542  O  O   . LEU A 1 226 ? 40.352  20.217  93.394  1.00 24.45  ? 227 LEU A O   1 
ATOM   1543  C  CB  . LEU A 1 226 ? 43.092  21.090  91.705  1.00 26.41  ? 227 LEU A CB  1 
ATOM   1544  C  CG  . LEU A 1 226 ? 43.746  20.889  90.337  1.00 25.14  ? 227 LEU A CG  1 
ATOM   1545  C  CD1 . LEU A 1 226 ? 45.253  20.790  90.482  1.00 27.17  ? 227 LEU A CD1 1 
ATOM   1546  C  CD2 . LEU A 1 226 ? 43.185  19.650  89.655  1.00 23.13  ? 227 LEU A CD2 1 
ATOM   1547  N  N   . GLY A 1 227 ? 41.243  22.222  93.952  1.00 23.97  ? 228 GLY A N   1 
ATOM   1548  C  CA  . GLY A 1 227 ? 40.693  22.199  95.298  1.00 37.71  ? 228 GLY A CA  1 
ATOM   1549  C  C   . GLY A 1 227 ? 39.175  22.098  95.321  1.00 37.16  ? 228 GLY A C   1 
ATOM   1550  O  O   . GLY A 1 227 ? 38.599  21.295  96.067  1.00 40.19  ? 228 GLY A O   1 
ATOM   1551  N  N   . VAL A 1 228 ? 38.526  22.909  94.490  1.00 36.04  ? 229 VAL A N   1 
ATOM   1552  C  CA  . VAL A 1 228 ? 37.071  22.926  94.415  1.00 38.33  ? 229 VAL A CA  1 
ATOM   1553  C  C   . VAL A 1 228 ? 36.533  21.584  93.933  1.00 35.46  ? 229 VAL A C   1 
ATOM   1554  O  O   . VAL A 1 228 ? 35.602  21.048  94.524  1.00 32.93  ? 229 VAL A O   1 
ATOM   1555  C  CB  . VAL A 1 228 ? 36.560  24.048  93.486  1.00 33.89  ? 229 VAL A CB  1 
ATOM   1556  C  CG1 . VAL A 1 228 ? 35.102  23.806  93.098  1.00 34.65  ? 229 VAL A CG1 1 
ATOM   1557  C  CG2 . VAL A 1 228 ? 36.726  25.404  94.152  1.00 25.17  ? 229 VAL A CG2 1 
ATOM   1558  N  N   . ALA A 1 229 ? 37.121  21.039  92.871  1.00 37.59  ? 230 ALA A N   1 
ATOM   1559  C  CA  . ALA A 1 229 ? 36.705  19.730  92.371  1.00 35.03  ? 230 ALA A CA  1 
ATOM   1560  C  C   . ALA A 1 229 ? 36.831  18.670  93.465  1.00 33.05  ? 230 ALA A C   1 
ATOM   1561  O  O   . ALA A 1 229 ? 35.915  17.858  93.678  1.00 35.11  ? 230 ALA A O   1 
ATOM   1562  C  CB  . ALA A 1 229 ? 37.525  19.337  91.154  1.00 31.30  ? 230 ALA A CB  1 
ATOM   1563  N  N   . SER A 1 230 ? 37.962  18.695  94.165  1.00 32.24  ? 231 SER A N   1 
ATOM   1564  C  CA  A SER A 1 230 ? 38.207  17.747  95.247  0.60 38.47  ? 231 SER A CA  1 
ATOM   1565  C  CA  B SER A 1 230 ? 38.212  17.757  95.256  0.40 38.29  ? 231 SER A CA  1 
ATOM   1566  C  C   . SER A 1 230 ? 37.127  17.841  96.326  1.00 35.35  ? 231 SER A C   1 
ATOM   1567  O  O   . SER A 1 230 ? 36.542  16.824  96.724  1.00 34.89  ? 231 SER A O   1 
ATOM   1568  C  CB  A SER A 1 230 ? 39.590  17.984  95.857  0.60 39.63  ? 231 SER A CB  1 
ATOM   1569  C  CB  B SER A 1 230 ? 39.583  18.020  95.883  0.40 39.70  ? 231 SER A CB  1 
ATOM   1570  O  OG  A SER A 1 230 ? 40.083  16.808  96.473  0.60 38.46  ? 231 SER A OG  1 
ATOM   1571  O  OG  B SER A 1 230 ? 40.622  17.837  94.937  0.40 38.13  ? 231 SER A OG  1 
ATOM   1572  N  N   . ASP A 1 231 ? 36.858  19.059  96.791  1.00 38.31  ? 232 ASP A N   1 
ATOM   1573  C  CA  . ASP A 1 231 ? 35.849  19.270  97.827  1.00 46.12  ? 232 ASP A CA  1 
ATOM   1574  C  C   . ASP A 1 231 ? 34.454  18.851  97.366  1.00 41.80  ? 232 ASP A C   1 
ATOM   1575  O  O   . ASP A 1 231 ? 33.683  18.275  98.136  1.00 34.68  ? 232 ASP A O   1 
ATOM   1576  C  CB  . ASP A 1 231 ? 35.834  20.734  98.270  1.00 56.46  ? 232 ASP A CB  1 
ATOM   1577  C  CG  . ASP A 1 231 ? 37.003  21.081  99.168  1.00 70.07  ? 232 ASP A CG  1 
ATOM   1578  O  OD1 . ASP A 1 231 ? 37.591  20.152  99.762  1.00 74.58  ? 232 ASP A OD1 1 
ATOM   1579  O  OD2 . ASP A 1 231 ? 37.333  22.280  99.283  1.00 76.63  ? 232 ASP A OD2 1 
ATOM   1580  N  N   . VAL A 1 232 ? 34.137  19.145  96.108  1.00 38.43  ? 233 VAL A N   1 
ATOM   1581  C  CA  . VAL A 1 232 ? 32.852  18.774  95.532  1.00 38.86  ? 233 VAL A CA  1 
ATOM   1582  C  C   . VAL A 1 232 ? 32.685  17.263  95.544  1.00 39.90  ? 233 VAL A C   1 
ATOM   1583  O  O   . VAL A 1 232 ? 31.654  16.760  95.979  1.00 39.67  ? 233 VAL A O   1 
ATOM   1584  C  CB  . VAL A 1 232 ? 32.693  19.297  94.088  1.00 38.89  ? 233 VAL A CB  1 
ATOM   1585  C  CG1 . VAL A 1 232 ? 31.543  18.587  93.386  1.00 26.34  ? 233 VAL A CG1 1 
ATOM   1586  C  CG2 . VAL A 1 232 ? 32.469  20.802  94.089  1.00 32.89  ? 233 VAL A CG2 1 
ATOM   1587  N  N   . VAL A 1 233 ? 33.701  16.539  95.081  1.00 37.17  ? 234 VAL A N   1 
ATOM   1588  C  CA  . VAL A 1 233 ? 33.634  15.079  95.100  1.00 34.21  ? 234 VAL A CA  1 
ATOM   1589  C  C   . VAL A 1 233 ? 33.474  14.556  96.530  1.00 33.80  ? 234 VAL A C   1 
ATOM   1590  O  O   . VAL A 1 233 ? 32.601  13.719  96.807  1.00 33.71  ? 234 VAL A O   1 
ATOM   1591  C  CB  . VAL A 1 233 ? 34.883  14.448  94.460  1.00 34.01  ? 234 VAL A CB  1 
ATOM   1592  C  CG1 . VAL A 1 233 ? 34.866  12.933  94.634  1.00 33.32  ? 234 VAL A CG1 1 
ATOM   1593  C  CG2 . VAL A 1 233 ? 34.962  14.821  92.989  1.00 35.47  ? 234 VAL A CG2 1 
ATOM   1594  N  N   . ARG A 1 234 ? 34.308  15.067  97.434  1.00 35.40  ? 235 ARG A N   1 
ATOM   1595  C  CA  . ARG A 1 234 ? 34.262  14.664  98.839  1.00 31.73  ? 235 ARG A CA  1 
ATOM   1596  C  C   . ARG A 1 234 ? 32.881  14.870  99.467  1.00 38.29  ? 235 ARG A C   1 
ATOM   1597  O  O   . ARG A 1 234 ? 32.423  14.050  100.262 1.00 38.71  ? 235 ARG A O   1 
ATOM   1598  C  CB  . ARG A 1 234 ? 35.314  15.431  99.645  1.00 40.17  ? 235 ARG A CB  1 
ATOM   1599  C  CG  . ARG A 1 234 ? 35.257  15.176  101.145 1.00 47.71  ? 235 ARG A CG  1 
ATOM   1600  C  CD  . ARG A 1 234 ? 36.269  16.026  101.899 1.00 59.11  ? 235 ARG A CD  1 
ATOM   1601  N  NE  . ARG A 1 234 ? 36.115  17.451  101.617 1.00 63.17  ? 235 ARG A NE  1 
ATOM   1602  C  CZ  . ARG A 1 234 ? 35.246  18.247  102.231 1.00 68.76  ? 235 ARG A CZ  1 
ATOM   1603  N  NH1 . ARG A 1 234 ? 34.443  17.761  103.167 1.00 71.71  ? 235 ARG A NH1 1 
ATOM   1604  N  NH2 . ARG A 1 234 ? 35.179  19.531  101.908 1.00 70.11  ? 235 ARG A NH2 1 
ATOM   1605  N  N   . LYS A 1 235 ? 32.219  15.963  99.101  1.00 29.84  ? 236 LYS A N   1 
ATOM   1606  C  CA  . LYS A 1 235 ? 30.921  16.296  99.679  1.00 41.78  ? 236 LYS A CA  1 
ATOM   1607  C  C   . LYS A 1 235 ? 29.785  15.497  99.043  1.00 41.27  ? 236 LYS A C   1 
ATOM   1608  O  O   . LYS A 1 235 ? 28.876  15.035  99.734  1.00 42.19  ? 236 LYS A O   1 
ATOM   1609  C  CB  . LYS A 1 235 ? 30.656  17.796  99.541  1.00 41.72  ? 236 LYS A CB  1 
ATOM   1610  C  CG  . LYS A 1 235 ? 31.498  18.646  100.478 1.00 43.14  ? 236 LYS A CG  1 
ATOM   1611  C  CD  . LYS A 1 235 ? 31.440  20.116  100.109 1.00 46.30  ? 236 LYS A CD  1 
ATOM   1612  C  CE  . LYS A 1 235 ? 32.320  20.944  101.032 1.00 49.92  ? 236 LYS A CE  1 
ATOM   1613  N  NZ  . LYS A 1 235 ? 32.764  22.214  100.395 1.00 49.54  ? 236 LYS A NZ  1 
ATOM   1614  N  N   . VAL A 1 236 ? 29.846  15.338  97.724  1.00 36.22  ? 237 VAL A N   1 
ATOM   1615  C  CA  . VAL A 1 236 ? 28.844  14.581  96.982  1.00 38.58  ? 237 VAL A CA  1 
ATOM   1616  C  C   . VAL A 1 236 ? 28.859  13.113  97.395  1.00 41.83  ? 237 VAL A C   1 
ATOM   1617  O  O   . VAL A 1 236 ? 27.811  12.468  97.463  1.00 39.37  ? 237 VAL A O   1 
ATOM   1618  C  CB  . VAL A 1 236 ? 29.069  14.701  95.458  1.00 41.54  ? 237 VAL A CB  1 
ATOM   1619  C  CG1 . VAL A 1 236 ? 28.250  13.667  94.698  1.00 38.85  ? 237 VAL A CG1 1 
ATOM   1620  C  CG2 . VAL A 1 236 ? 28.727  16.106  94.988  1.00 37.84  ? 237 VAL A CG2 1 
ATOM   1621  N  N   . ALA A 1 237 ? 30.049  12.598  97.698  1.00 44.61  ? 238 ALA A N   1 
ATOM   1622  C  CA  . ALA A 1 237 ? 30.193  11.206  98.126  1.00 46.04  ? 238 ALA A CA  1 
ATOM   1623  C  C   . ALA A 1 237 ? 29.322  10.863  99.338  1.00 50.47  ? 238 ALA A C   1 
ATOM   1624  O  O   . ALA A 1 237 ? 28.981  9.699   99.554  1.00 60.19  ? 238 ALA A O   1 
ATOM   1625  C  CB  . ALA A 1 237 ? 31.650  10.904  98.435  1.00 35.19  ? 238 ALA A CB  1 
ATOM   1626  N  N   . GLN A 1 238 ? 28.957  11.875  100.118 1.00 55.27  ? 239 GLN A N   1 
ATOM   1627  C  CA  . GLN A 1 238 ? 28.194  11.659  101.343 1.00 58.25  ? 239 GLN A CA  1 
ATOM   1628  C  C   . GLN A 1 238 ? 26.682  11.660  101.120 1.00 54.35  ? 239 GLN A C   1 
ATOM   1629  O  O   . GLN A 1 238 ? 25.918  11.395  102.047 1.00 53.16  ? 239 GLN A O   1 
ATOM   1630  C  CB  . GLN A 1 238 ? 28.559  12.720  102.385 1.00 65.74  ? 239 GLN A CB  1 
ATOM   1631  C  CG  . GLN A 1 238 ? 30.013  12.677  102.840 1.00 74.89  ? 239 GLN A CG  1 
ATOM   1632  C  CD  . GLN A 1 238 ? 30.344  11.446  103.668 1.00 82.56  ? 239 GLN A CD  1 
ATOM   1633  O  OE1 . GLN A 1 238 ? 29.463  10.662  104.025 1.00 87.25  ? 239 GLN A OE1 1 
ATOM   1634  N  NE2 . GLN A 1 238 ? 31.624  11.271  103.976 1.00 84.84  ? 239 GLN A NE2 1 
ATOM   1635  N  N   . VAL A 1 239 ? 26.252  11.961  99.898  1.00 48.51  ? 240 VAL A N   1 
ATOM   1636  C  CA  . VAL A 1 239 ? 24.829  11.921  99.572  1.00 52.63  ? 240 VAL A CA  1 
ATOM   1637  C  C   . VAL A 1 239 ? 24.304  10.490  99.659  1.00 52.91  ? 240 VAL A C   1 
ATOM   1638  O  O   . VAL A 1 239 ? 24.759  9.609   98.929  1.00 45.95  ? 240 VAL A O   1 
ATOM   1639  C  CB  . VAL A 1 239 ? 24.545  12.485  98.168  1.00 46.23  ? 240 VAL A CB  1 
ATOM   1640  C  CG1 . VAL A 1 239 ? 23.066  12.355  97.836  1.00 42.85  ? 240 VAL A CG1 1 
ATOM   1641  C  CG2 . VAL A 1 239 ? 24.985  13.939  98.084  1.00 45.68  ? 240 VAL A CG2 1 
ATOM   1642  N  N   . PRO A 1 240 ? 23.341  10.256  100.564 1.00 60.93  ? 241 PRO A N   1 
ATOM   1643  C  CA  . PRO A 1 240 ? 22.813  8.915   100.835 1.00 60.38  ? 241 PRO A CA  1 
ATOM   1644  C  C   . PRO A 1 240 ? 21.894  8.390   99.737  1.00 55.80  ? 241 PRO A C   1 
ATOM   1645  O  O   . PRO A 1 240 ? 21.238  9.174   99.050  1.00 49.74  ? 241 PRO A O   1 
ATOM   1646  C  CB  . PRO A 1 240 ? 22.036  9.110   102.137 1.00 66.24  ? 241 PRO A CB  1 
ATOM   1647  C  CG  . PRO A 1 240 ? 21.573  10.521  102.070 1.00 67.43  ? 241 PRO A CG  1 
ATOM   1648  C  CD  . PRO A 1 240 ? 22.683  11.283  101.391 1.00 64.11  ? 241 PRO A CD  1 
ATOM   1649  N  N   . LEU A 1 241 ? 21.857  7.070   99.580  1.00 56.26  ? 242 LEU A N   1 
ATOM   1650  C  CA  . LEU A 1 241 ? 20.931  6.428   98.656  1.00 55.10  ? 242 LEU A CA  1 
ATOM   1651  C  C   . LEU A 1 241 ? 19.525  6.416   99.247  1.00 53.62  ? 242 LEU A C   1 
ATOM   1652  O  O   . LEU A 1 241 ? 19.353  6.236   100.452 1.00 53.78  ? 242 LEU A O   1 
ATOM   1653  C  CB  . LEU A 1 241 ? 21.387  5.003   98.338  1.00 55.52  ? 242 LEU A CB  1 
ATOM   1654  C  CG  . LEU A 1 241 ? 22.722  4.859   97.606  1.00 57.91  ? 242 LEU A CG  1 
ATOM   1655  C  CD1 . LEU A 1 241 ? 23.271  3.451   97.765  1.00 54.61  ? 242 LEU A CD1 1 
ATOM   1656  C  CD2 . LEU A 1 241 ? 22.564  5.210   96.135  1.00 57.38  ? 242 LEU A CD2 1 
ATOM   1657  N  N   . GLY A 1 242 ? 18.522  6.609   98.397  1.00 53.99  ? 243 GLY A N   1 
ATOM   1658  C  CA  . GLY A 1 242 ? 17.144  6.656   98.849  1.00 53.82  ? 243 GLY A CA  1 
ATOM   1659  C  C   . GLY A 1 242 ? 16.525  5.285   99.050  1.00 55.19  ? 243 GLY A C   1 
ATOM   1660  O  O   . GLY A 1 242 ? 17.112  4.273   98.668  1.00 55.96  ? 243 GLY A O   1 
ATOM   1661  N  N   . PRO A 1 243 ? 15.331  5.246   99.661  1.00 54.39  ? 244 PRO A N   1 
ATOM   1662  C  CA  . PRO A 1 243 ? 14.576  4.006   99.880  1.00 53.26  ? 244 PRO A CA  1 
ATOM   1663  C  C   . PRO A 1 243 ? 14.161  3.362   98.561  1.00 51.40  ? 244 PRO A C   1 
ATOM   1664  O  O   . PRO A 1 243 ? 14.241  2.139   98.409  1.00 53.48  ? 244 PRO A O   1 
ATOM   1665  C  CB  . PRO A 1 243 ? 13.348  4.473   100.671 1.00 53.95  ? 244 PRO A CB  1 
ATOM   1666  C  CG  . PRO A 1 243 ? 13.736  5.798   101.248 1.00 55.86  ? 244 PRO A CG  1 
ATOM   1667  C  CD  . PRO A 1 243 ? 14.644  6.415   100.235 1.00 53.62  ? 244 PRO A CD  1 
ATOM   1668  N  N   . GLU A 1 244 ? 13.718  4.195   97.625  1.00 47.20  ? 245 GLU A N   1 
ATOM   1669  C  CA  . GLU A 1 244 ? 13.355  3.751   96.285  1.00 50.94  ? 245 GLU A CA  1 
ATOM   1670  C  C   . GLU A 1 244 ? 14.532  3.045   95.625  1.00 47.81  ? 245 GLU A C   1 
ATOM   1671  O  O   . GLU A 1 244 ? 14.390  1.958   95.057  1.00 53.82  ? 245 GLU A O   1 
ATOM   1672  C  CB  . GLU A 1 244 ? 12.907  4.942   95.437  1.00 55.33  ? 245 GLU A CB  1 
ATOM   1673  C  CG  . GLU A 1 244 ? 11.645  5.618   95.943  1.00 67.11  ? 245 GLU A CG  1 
ATOM   1674  C  CD  . GLU A 1 244 ? 10.463  4.674   95.989  1.00 83.22  ? 245 GLU A CD  1 
ATOM   1675  O  OE1 . GLU A 1 244 ? 10.311  3.872   95.044  1.00 86.69  ? 245 GLU A OE1 1 
ATOM   1676  O  OE2 . GLU A 1 244 ? 9.691   4.727   96.970  1.00 87.20  ? 245 GLU A OE2 1 
ATOM   1677  N  N   . CYS A 1 245 ? 15.697  3.678   95.717  1.00 45.27  ? 246 CYS A N   1 
ATOM   1678  C  CA  . CYS A 1 245 ? 16.925  3.113   95.182  1.00 45.29  ? 246 CYS A CA  1 
ATOM   1679  C  C   . CYS A 1 245 ? 17.247  1.791   95.861  1.00 40.65  ? 246 CYS A C   1 
ATOM   1680  O  O   . CYS A 1 245 ? 17.661  0.842   95.207  1.00 39.25  ? 246 CYS A O   1 
ATOM   1681  C  CB  . CYS A 1 245 ? 18.090  4.091   95.350  1.00 44.59  ? 246 CYS A CB  1 
ATOM   1682  S  SG  . CYS A 1 245 ? 19.640  3.531   94.604  1.00 72.16  ? 246 CYS A SG  1 
ATOM   1683  N  N   . SER A 1 246 ? 17.049  1.735   97.175  1.00 40.55  ? 247 SER A N   1 
ATOM   1684  C  CA  . SER A 1 246 ? 17.314  0.522   97.940  1.00 54.47  ? 247 SER A CA  1 
ATOM   1685  C  C   . SER A 1 246 ? 16.454  -0.644  97.450  1.00 50.38  ? 247 SER A C   1 
ATOM   1686  O  O   . SER A 1 246 ? 16.963  -1.739  97.189  1.00 50.15  ? 247 SER A O   1 
ATOM   1687  C  CB  . SER A 1 246 ? 17.071  0.770   99.430  1.00 52.37  ? 247 SER A CB  1 
ATOM   1688  O  OG  . SER A 1 246 ? 17.578  -0.295  100.214 1.00 59.04  ? 247 SER A OG  1 
ATOM   1689  N  N   . ARG A 1 247 ? 15.152  -0.400  97.315  1.00 46.46  ? 248 ARG A N   1 
ATOM   1690  C  CA  . ARG A 1 247 ? 14.231  -1.424  96.831  1.00 52.27  ? 248 ARG A CA  1 
ATOM   1691  C  C   . ARG A 1 247 ? 14.559  -1.849  95.403  1.00 51.63  ? 248 ARG A C   1 
ATOM   1692  O  O   . ARG A 1 247 ? 14.524  -3.037  95.076  1.00 46.27  ? 248 ARG A O   1 
ATOM   1693  C  CB  . ARG A 1 247 ? 12.785  -0.931  96.898  1.00 58.61  ? 248 ARG A CB  1 
ATOM   1694  C  CG  . ARG A 1 247 ? 12.245  -0.737  98.304  1.00 67.55  ? 248 ARG A CG  1 
ATOM   1695  C  CD  . ARG A 1 247 ? 10.773  -0.341  98.282  1.00 72.52  ? 248 ARG A CD  1 
ATOM   1696  N  NE  . ARG A 1 247 ? 10.511  0.779   97.381  1.00 77.28  ? 248 ARG A NE  1 
ATOM   1697  C  CZ  . ARG A 1 247 ? 9.938   0.659   96.187  1.00 80.82  ? 248 ARG A CZ  1 
ATOM   1698  N  NH1 . ARG A 1 247 ? 9.571   -0.535  95.745  1.00 81.06  ? 248 ARG A NH1 1 
ATOM   1699  N  NH2 . ARG A 1 247 ? 9.738   1.729   95.432  1.00 80.98  ? 248 ARG A NH2 1 
ATOM   1700  N  N   . ALA A 1 248 ? 14.872  -0.873  94.554  1.00 44.20  ? 249 ALA A N   1 
ATOM   1701  C  CA  . ALA A 1 248 ? 15.188  -1.157  93.157  1.00 45.92  ? 249 ALA A CA  1 
ATOM   1702  C  C   . ALA A 1 248 ? 16.470  -1.976  93.025  1.00 43.56  ? 249 ALA A C   1 
ATOM   1703  O  O   . ALA A 1 248 ? 16.600  -2.803  92.122  1.00 42.29  ? 249 ALA A O   1 
ATOM   1704  C  CB  . ALA A 1 248 ? 15.303  0.132   92.371  1.00 39.14  ? 249 ALA A CB  1 
ATOM   1705  N  N   . VAL A 1 249 ? 17.414  -1.737  93.930  1.00 43.15  ? 250 VAL A N   1 
ATOM   1706  C  CA  . VAL A 1 249 ? 18.679  -2.460  93.935  1.00 40.18  ? 250 VAL A CA  1 
ATOM   1707  C  C   . VAL A 1 249 ? 18.471  -3.874  94.460  1.00 49.42  ? 250 VAL A C   1 
ATOM   1708  O  O   . VAL A 1 249 ? 19.049  -4.827  93.935  1.00 48.78  ? 250 VAL A O   1 
ATOM   1709  C  CB  . VAL A 1 249 ? 19.745  -1.729  94.780  1.00 48.97  ? 250 VAL A CB  1 
ATOM   1710  C  CG1 . VAL A 1 249 ? 20.919  -2.645  95.089  1.00 50.19  ? 250 VAL A CG1 1 
ATOM   1711  C  CG2 . VAL A 1 249 ? 20.222  -0.484  94.054  1.00 38.20  ? 250 VAL A CG2 1 
ATOM   1712  N  N   . MET A 1 250 ? 17.638  -4.010  95.488  1.00 50.56  ? 251 MET A N   1 
ATOM   1713  C  CA  . MET A 1 250 ? 17.269  -5.333  95.981  1.00 44.53  ? 251 MET A CA  1 
ATOM   1714  C  C   . MET A 1 250 ? 16.617  -6.147  94.868  1.00 44.68  ? 251 MET A C   1 
ATOM   1715  O  O   . MET A 1 250 ? 16.929  -7.323  94.681  1.00 45.51  ? 251 MET A O   1 
ATOM   1716  C  CB  . MET A 1 250 ? 16.325  -5.231  97.180  1.00 47.12  ? 251 MET A CB  1 
ATOM   1717  C  CG  . MET A 1 250 ? 15.674  -6.555  97.555  1.00 50.09  ? 251 MET A CG  1 
ATOM   1718  S  SD  . MET A 1 250 ? 16.883  -7.867  97.821  1.00 54.07  ? 251 MET A SD  1 
ATOM   1719  C  CE  . MET A 1 250 ? 15.824  -9.310  97.861  1.00 54.22  ? 251 MET A CE  1 
ATOM   1720  N  N   . LYS A 1 251 ? 15.718  -5.508  94.127  1.00 44.00  ? 252 LYS A N   1 
ATOM   1721  C  CA  . LYS A 1 251 ? 15.057  -6.152  93.000  1.00 50.15  ? 252 LYS A CA  1 
ATOM   1722  C  C   . LYS A 1 251 ? 16.068  -6.521  91.921  1.00 46.94  ? 252 LYS A C   1 
ATOM   1723  O  O   . LYS A 1 251 ? 15.973  -7.576  91.294  1.00 50.30  ? 252 LYS A O   1 
ATOM   1724  C  CB  . LYS A 1 251 ? 13.974  -5.239  92.423  1.00 49.03  ? 252 LYS A CB  1 
ATOM   1725  C  CG  . LYS A 1 251 ? 13.154  -5.866  91.306  1.00 54.39  ? 252 LYS A CG  1 
ATOM   1726  C  CD  . LYS A 1 251 ? 11.773  -5.234  91.217  1.00 53.13  ? 252 LYS A CD  1 
ATOM   1727  C  CE  . LYS A 1 251 ? 10.906  -5.932  90.180  1.00 57.07  ? 252 LYS A CE  1 
ATOM   1728  N  NZ  . LYS A 1 251 ? 11.373  -5.672  88.790  1.00 58.52  ? 252 LYS A NZ  1 
ATOM   1729  N  N   . LEU A 1 252 ? 17.043  -5.642  91.722  1.00 42.11  ? 253 LEU A N   1 
ATOM   1730  C  CA  . LEU A 1 252 ? 18.074  -5.835  90.712  1.00 41.40  ? 253 LEU A CA  1 
ATOM   1731  C  C   . LEU A 1 252 ? 18.977  -7.031  91.001  1.00 42.36  ? 253 LEU A C   1 
ATOM   1732  O  O   . LEU A 1 252 ? 19.278  -7.822  90.108  1.00 42.64  ? 253 LEU A O   1 
ATOM   1733  C  CB  . LEU A 1 252 ? 18.930  -4.572  90.591  1.00 39.96  ? 253 LEU A CB  1 
ATOM   1734  C  CG  . LEU A 1 252 ? 20.126  -4.659  89.641  1.00 39.27  ? 253 LEU A CG  1 
ATOM   1735  C  CD1 . LEU A 1 252 ? 19.651  -4.736  88.201  1.00 38.96  ? 253 LEU A CD1 1 
ATOM   1736  C  CD2 . LEU A 1 252 ? 21.073  -3.482  89.841  1.00 38.55  ? 253 LEU A CD2 1 
ATOM   1737  N  N   . VAL A 1 253 ? 19.403  -7.161  92.253  1.00 43.02  ? 254 VAL A N   1 
ATOM   1738  C  CA  . VAL A 1 253 ? 20.464  -8.099  92.599  1.00 56.52  ? 254 VAL A CA  1 
ATOM   1739  C  C   . VAL A 1 253 ? 19.967  -9.449  93.118  1.00 60.36  ? 254 VAL A C   1 
ATOM   1740  O  O   . VAL A 1 253 ? 20.297  -10.492 92.552  1.00 63.54  ? 254 VAL A O   1 
ATOM   1741  C  CB  . VAL A 1 253 ? 21.407  -7.492  93.658  1.00 52.14  ? 254 VAL A CB  1 
ATOM   1742  C  CG1 . VAL A 1 253 ? 22.532  -8.459  93.984  1.00 54.48  ? 254 VAL A CG1 1 
ATOM   1743  C  CG2 . VAL A 1 253 ? 21.969  -6.165  93.171  1.00 49.41  ? 254 VAL A CG2 1 
ATOM   1744  N  N   . TYR A 1 254 ? 19.179  -9.432  94.188  1.00 53.75  ? 255 TYR A N   1 
ATOM   1745  C  CA  . TYR A 1 254 ? 18.874  -10.662 94.913  1.00 53.70  ? 255 TYR A CA  1 
ATOM   1746  C  C   . TYR A 1 254 ? 17.457  -11.191 94.715  1.00 57.68  ? 255 TYR A C   1 
ATOM   1747  O  O   . TYR A 1 254 ? 17.100  -12.227 95.273  1.00 57.86  ? 255 TYR A O   1 
ATOM   1748  C  CB  . TYR A 1 254 ? 19.135  -10.453 96.405  1.00 52.89  ? 255 TYR A CB  1 
ATOM   1749  C  CG  . TYR A 1 254 ? 20.596  -10.247 96.723  1.00 53.63  ? 255 TYR A CG  1 
ATOM   1750  C  CD1 . TYR A 1 254 ? 21.558  -11.127 96.244  1.00 56.57  ? 255 TYR A CD1 1 
ATOM   1751  C  CD2 . TYR A 1 254 ? 21.017  -9.164  97.481  1.00 50.11  ? 255 TYR A CD2 1 
ATOM   1752  C  CE1 . TYR A 1 254 ? 22.898  -10.942 96.524  1.00 54.79  ? 255 TYR A CE1 1 
ATOM   1753  C  CE2 . TYR A 1 254 ? 22.355  -8.970  97.766  1.00 49.66  ? 255 TYR A CE2 1 
ATOM   1754  C  CZ  . TYR A 1 254 ? 23.291  -9.861  97.284  1.00 52.24  ? 255 TYR A CZ  1 
ATOM   1755  O  OH  . TYR A 1 254 ? 24.624  -9.670  97.565  1.00 56.54  ? 255 TYR A OH  1 
ATOM   1756  N  N   . CYS A 1 255 ? 16.648  -10.494 93.924  1.00 58.20  ? 256 CYS A N   1 
ATOM   1757  C  CA  . CYS A 1 255 ? 15.313  -10.993 93.617  1.00 49.08  ? 256 CYS A CA  1 
ATOM   1758  C  C   . CYS A 1 255 ? 15.391  -12.160 92.639  1.00 49.71  ? 256 CYS A C   1 
ATOM   1759  O  O   . CYS A 1 255 ? 14.466  -12.968 92.548  1.00 50.87  ? 256 CYS A O   1 
ATOM   1760  C  CB  . CYS A 1 255 ? 14.425  -9.883  93.056  1.00 47.88  ? 256 CYS A CB  1 
ATOM   1761  S  SG  . CYS A 1 255 ? 13.505  -8.980  94.323  1.00 76.22  ? 256 CYS A SG  1 
ATOM   1762  N  N   . ALA A 1 256 ? 16.499  -12.241 91.909  1.00 49.03  ? 257 ALA A N   1 
ATOM   1763  C  CA  . ALA A 1 256 ? 16.766  -13.393 91.059  1.00 59.92  ? 257 ALA A CA  1 
ATOM   1764  C  C   . ALA A 1 256 ? 16.911  -14.632 91.931  1.00 59.53  ? 257 ALA A C   1 
ATOM   1765  O  O   . ALA A 1 256 ? 16.380  -15.698 91.617  1.00 53.13  ? 257 ALA A O   1 
ATOM   1766  C  CB  . ALA A 1 256 ? 18.017  -13.170 90.227  1.00 48.89  ? 257 ALA A CB  1 
ATOM   1767  N  N   . HIS A 1 257 ? 17.632  -14.474 93.035  1.00 55.18  ? 258 HIS A N   1 
ATOM   1768  C  CA  . HIS A 1 257 ? 17.825  -15.549 93.997  1.00 55.52  ? 258 HIS A CA  1 
ATOM   1769  C  C   . HIS A 1 257 ? 16.490  -15.981 94.591  1.00 58.60  ? 258 HIS A C   1 
ATOM   1770  O  O   . HIS A 1 257 ? 16.180  -17.170 94.650  1.00 60.06  ? 258 HIS A O   1 
ATOM   1771  C  CB  . HIS A 1 257 ? 18.779  -15.115 95.115  1.00 57.30  ? 258 HIS A CB  1 
ATOM   1772  C  CG  . HIS A 1 257 ? 20.159  -14.772 94.643  1.00 60.78  ? 258 HIS A CG  1 
ATOM   1773  N  ND1 . HIS A 1 257 ? 20.399  -14.029 93.507  1.00 63.55  ? 258 HIS A ND1 1 
ATOM   1774  C  CD2 . HIS A 1 257 ? 21.375  -15.068 95.161  1.00 63.92  ? 258 HIS A CD2 1 
ATOM   1775  C  CE1 . HIS A 1 257 ? 21.702  -13.885 93.344  1.00 63.92  ? 258 HIS A CE1 1 
ATOM   1776  N  NE2 . HIS A 1 257 ? 22.317  -14.507 94.333  1.00 66.57  ? 258 HIS A NE2 1 
ATOM   1777  N  N   . CYS A 1 258 ? 15.700  -15.003 95.019  1.00 57.25  ? 259 CYS A N   1 
ATOM   1778  C  CA  . CYS A 1 258 ? 14.432  -15.278 95.683  1.00 62.77  ? 259 CYS A CA  1 
ATOM   1779  C  C   . CYS A 1 258 ? 13.411  -15.934 94.757  1.00 62.13  ? 259 CYS A C   1 
ATOM   1780  O  O   . CYS A 1 258 ? 12.603  -16.744 95.202  1.00 67.20  ? 259 CYS A O   1 
ATOM   1781  C  CB  . CYS A 1 258 ? 13.851  -13.988 96.267  1.00 63.46  ? 259 CYS A CB  1 
ATOM   1782  S  SG  . CYS A 1 258 ? 14.756  -13.351 97.696  1.00 61.44  ? 259 CYS A SG  1 
ATOM   1783  N  N   . LEU A 1 259 ? 13.449  -15.592 93.473  1.00 61.65  ? 260 LEU A N   1 
ATOM   1784  C  CA  . LEU A 1 259 ? 12.467  -16.119 92.529  1.00 58.21  ? 260 LEU A CA  1 
ATOM   1785  C  C   . LEU A 1 259 ? 12.948  -17.381 91.818  1.00 65.70  ? 260 LEU A C   1 
ATOM   1786  O  O   . LEU A 1 259 ? 12.403  -17.764 90.784  1.00 70.41  ? 260 LEU A O   1 
ATOM   1787  C  CB  . LEU A 1 259 ? 12.091  -15.055 91.497  1.00 56.92  ? 260 LEU A CB  1 
ATOM   1788  C  CG  . LEU A 1 259 ? 11.340  -13.833 92.032  1.00 60.66  ? 260 LEU A CG  1 
ATOM   1789  C  CD1 . LEU A 1 259 ? 10.681  -13.073 90.892  1.00 60.62  ? 260 LEU A CD1 1 
ATOM   1790  C  CD2 . LEU A 1 259 ? 10.311  -14.237 93.080  1.00 63.94  ? 260 LEU A CD2 1 
ATOM   1791  N  N   . GLY A 1 260 ? 13.971  -18.022 92.372  1.00 70.21  ? 261 GLY A N   1 
ATOM   1792  C  CA  . GLY A 1 260 ? 14.373  -19.335 91.907  1.00 73.61  ? 261 GLY A CA  1 
ATOM   1793  C  C   . GLY A 1 260 ? 15.467  -19.400 90.858  1.00 74.60  ? 261 GLY A C   1 
ATOM   1794  O  O   . GLY A 1 260 ? 15.693  -20.457 90.267  1.00 79.22  ? 261 GLY A O   1 
ATOM   1795  N  N   . VAL A 1 261 ? 16.152  -18.286 90.621  1.00 74.89  ? 262 VAL A N   1 
ATOM   1796  C  CA  . VAL A 1 261 ? 17.249  -18.270 89.657  1.00 70.67  ? 262 VAL A CA  1 
ATOM   1797  C  C   . VAL A 1 261 ? 18.477  -17.524 90.187  1.00 69.77  ? 262 VAL A C   1 
ATOM   1798  O  O   . VAL A 1 261 ? 18.834  -16.462 89.678  1.00 71.37  ? 262 VAL A O   1 
ATOM   1799  C  CB  . VAL A 1 261 ? 16.804  -17.645 88.312  1.00 67.25  ? 262 VAL A CB  1 
ATOM   1800  C  CG1 . VAL A 1 261 ? 16.038  -18.662 87.482  1.00 67.68  ? 262 VAL A CG1 1 
ATOM   1801  C  CG2 . VAL A 1 261 ? 15.953  -16.402 88.545  1.00 66.62  ? 262 VAL A CG2 1 
ATOM   1802  N  N   . PRO A 1 262 ? 19.143  -18.093 91.206  1.00 68.12  ? 263 PRO A N   1 
ATOM   1803  C  CA  . PRO A 1 262 ? 20.298  -17.432 91.825  1.00 66.43  ? 263 PRO A CA  1 
ATOM   1804  C  C   . PRO A 1 262 ? 21.502  -17.346 90.889  1.00 66.40  ? 263 PRO A C   1 
ATOM   1805  O  O   . PRO A 1 262 ? 22.364  -16.486 91.074  1.00 65.08  ? 263 PRO A O   1 
ATOM   1806  C  CB  . PRO A 1 262 ? 20.607  -18.327 93.028  1.00 69.33  ? 263 PRO A CB  1 
ATOM   1807  C  CG  . PRO A 1 262 ? 20.121  -19.672 92.621  1.00 68.36  ? 263 PRO A CG  1 
ATOM   1808  C  CD  . PRO A 1 262 ? 18.893  -19.424 91.790  1.00 69.19  ? 263 PRO A CD  1 
ATOM   1809  N  N   . GLY A 1 263 ? 21.555  -18.232 89.900  1.00 66.04  ? 264 GLY A N   1 
ATOM   1810  C  CA  . GLY A 1 263 ? 22.633  -18.225 88.929  1.00 62.54  ? 264 GLY A CA  1 
ATOM   1811  C  C   . GLY A 1 263 ? 22.454  -17.134 87.892  1.00 63.19  ? 264 GLY A C   1 
ATOM   1812  O  O   . GLY A 1 263 ? 23.396  -16.774 87.185  1.00 64.98  ? 264 GLY A O   1 
ATOM   1813  N  N   . ALA A 1 264 ? 21.238  -16.606 87.801  1.00 63.14  ? 265 ALA A N   1 
ATOM   1814  C  CA  . ALA A 1 264 ? 20.932  -15.553 86.841  1.00 62.73  ? 265 ALA A CA  1 
ATOM   1815  C  C   . ALA A 1 264 ? 21.552  -14.226 87.265  1.00 69.58  ? 265 ALA A C   1 
ATOM   1816  O  O   . ALA A 1 264 ? 21.511  -13.855 88.439  1.00 73.88  ? 265 ALA A O   1 
ATOM   1817  C  CB  . ALA A 1 264 ? 19.428  -15.406 86.673  1.00 65.44  ? 265 ALA A CB  1 
ATOM   1818  N  N   . ARG A 1 265 ? 22.122  -13.514 86.300  1.00 62.85  ? 266 ARG A N   1 
ATOM   1819  C  CA  . ARG A 1 265 ? 22.729  -12.217 86.563  1.00 62.33  ? 266 ARG A CA  1 
ATOM   1820  C  C   . ARG A 1 265 ? 21.965  -11.124 85.822  1.00 61.34  ? 266 ARG A C   1 
ATOM   1821  O  O   . ARG A 1 265 ? 21.385  -11.377 84.766  1.00 55.96  ? 266 ARG A O   1 
ATOM   1822  C  CB  . ARG A 1 265 ? 24.207  -12.228 86.159  1.00 66.30  ? 266 ARG A CB  1 
ATOM   1823  C  CG  . ARG A 1 265 ? 25.117  -12.834 87.216  1.00 73.55  ? 266 ARG A CG  1 
ATOM   1824  C  CD  . ARG A 1 265 ? 25.142  -11.964 88.464  1.00 78.47  ? 266 ARG A CD  1 
ATOM   1825  N  NE  . ARG A 1 265 ? 25.793  -12.620 89.594  1.00 87.02  ? 266 ARG A NE  1 
ATOM   1826  C  CZ  . ARG A 1 265 ? 25.176  -12.933 90.729  1.00 93.17  ? 266 ARG A CZ  1 
ATOM   1827  N  NH1 . ARG A 1 265 ? 23.890  -12.649 90.887  1.00 94.05  ? 266 ARG A NH1 1 
ATOM   1828  N  NH2 . ARG A 1 265 ? 25.844  -13.528 91.708  1.00 96.52  ? 266 ARG A NH2 1 
ATOM   1829  N  N   . PRO A 1 266 ? 21.958  -9.902  86.380  1.00 53.99  ? 267 PRO A N   1 
ATOM   1830  C  CA  . PRO A 1 266 ? 21.140  -8.813  85.835  1.00 52.09  ? 267 PRO A CA  1 
ATOM   1831  C  C   . PRO A 1 266 ? 21.548  -8.382  84.433  1.00 41.22  ? 267 PRO A C   1 
ATOM   1832  O  O   . PRO A 1 266 ? 22.733  -8.376  84.106  1.00 41.05  ? 267 PRO A O   1 
ATOM   1833  C  CB  . PRO A 1 266 ? 21.375  -7.666  86.827  1.00 40.93  ? 267 PRO A CB  1 
ATOM   1834  C  CG  . PRO A 1 266 ? 21.852  -8.321  88.074  1.00 41.87  ? 267 PRO A CG  1 
ATOM   1835  C  CD  . PRO A 1 266 ? 22.644  -9.501  87.620  1.00 62.42  ? 267 PRO A CD  1 
ATOM   1836  N  N   . CYS A 1 267 ? 20.564  -8.031  83.613  1.00 51.68  ? 268 CYS A N   1 
ATOM   1837  C  CA  A CYS A 1 267 ? 20.850  -7.489  82.295  0.68 50.32  ? 268 CYS A CA  1 
ATOM   1838  C  CA  B CYS A 1 267 ? 20.819  -7.464  82.294  0.32 49.58  ? 268 CYS A CA  1 
ATOM   1839  C  C   . CYS A 1 267 ? 21.515  -6.120  82.429  1.00 38.89  ? 268 CYS A C   1 
ATOM   1840  O  O   . CYS A 1 267 ? 21.159  -5.332  83.303  1.00 38.25  ? 268 CYS A O   1 
ATOM   1841  C  CB  A CYS A 1 267 ? 19.572  -7.396  81.456  0.68 49.17  ? 268 CYS A CB  1 
ATOM   1842  C  CB  B CYS A 1 267 ? 19.516  -7.293  81.514  0.32 47.58  ? 268 CYS A CB  1 
ATOM   1843  S  SG  A CYS A 1 267 ? 18.853  -9.003  81.014  0.68 66.39  ? 268 CYS A SG  1 
ATOM   1844  S  SG  B CYS A 1 267 ? 19.728  -6.529  79.890  0.32 53.70  ? 268 CYS A SG  1 
ATOM   1845  N  N   . PRO A 1 268 ? 22.509  -5.851  81.568  1.00 43.90  ? 269 PRO A N   1 
ATOM   1846  C  CA  . PRO A 1 268 ? 23.242  -4.579  81.570  1.00 42.61  ? 269 PRO A CA  1 
ATOM   1847  C  C   . PRO A 1 268 ? 22.342  -3.341  81.526  1.00 46.91  ? 269 PRO A C   1 
ATOM   1848  O  O   . PRO A 1 268 ? 22.524  -2.436  82.341  1.00 45.55  ? 269 PRO A O   1 
ATOM   1849  C  CB  . PRO A 1 268 ? 24.093  -4.675  80.304  1.00 46.52  ? 269 PRO A CB  1 
ATOM   1850  C  CG  . PRO A 1 268 ? 24.362  -6.134  80.167  1.00 47.87  ? 269 PRO A CG  1 
ATOM   1851  C  CD  . PRO A 1 268 ? 23.107  -6.825  80.635  1.00 44.19  ? 269 PRO A CD  1 
ATOM   1852  N  N   . ASP A 1 269 ? 21.388  -3.306  80.599  1.00 46.87  ? 270 ASP A N   1 
ATOM   1853  C  CA  . ASP A 1 269 ? 20.499  -2.153  80.460  1.00 47.04  ? 270 ASP A CA  1 
ATOM   1854  C  C   . ASP A 1 269 ? 19.570  -2.003  81.664  1.00 47.76  ? 270 ASP A C   1 
ATOM   1855  O  O   . ASP A 1 269 ? 19.218  -0.888  82.055  1.00 42.26  ? 270 ASP A O   1 
ATOM   1856  C  CB  . ASP A 1 269 ? 19.681  -2.263  79.171  1.00 47.45  ? 270 ASP A CB  1 
ATOM   1857  C  CG  . ASP A 1 269 ? 20.521  -2.039  77.926  1.00 49.29  ? 270 ASP A CG  1 
ATOM   1858  O  OD1 . ASP A 1 269 ? 21.667  -1.559  78.061  1.00 53.96  ? 270 ASP A OD1 1 
ATOM   1859  O  OD2 . ASP A 1 269 ? 20.034  -2.333  76.814  1.00 52.87  ? 270 ASP A OD2 1 
ATOM   1860  N  N   . TYR A 1 270 ? 19.175  -3.132  82.240  1.00 45.46  ? 271 TYR A N   1 
ATOM   1861  C  CA  . TYR A 1 270 ? 18.373  -3.152  83.459  1.00 50.40  ? 271 TYR A CA  1 
ATOM   1862  C  C   . TYR A 1 270 ? 19.144  -2.479  84.597  1.00 41.18  ? 271 TYR A C   1 
ATOM   1863  O  O   . TYR A 1 270 ? 18.681  -1.498  85.196  1.00 36.10  ? 271 TYR A O   1 
ATOM   1864  C  CB  . TYR A 1 270 ? 18.008  -4.598  83.817  1.00 46.03  ? 271 TYR A CB  1 
ATOM   1865  C  CG  . TYR A 1 270 ? 17.196  -4.778  85.081  1.00 45.91  ? 271 TYR A CG  1 
ATOM   1866  C  CD1 . TYR A 1 270 ? 16.352  -3.777  85.547  1.00 46.97  ? 271 TYR A CD1 1 
ATOM   1867  C  CD2 . TYR A 1 270 ? 17.273  -5.960  85.808  1.00 40.29  ? 271 TYR A CD2 1 
ATOM   1868  C  CE1 . TYR A 1 270 ? 15.614  -3.948  86.705  1.00 46.62  ? 271 TYR A CE1 1 
ATOM   1869  C  CE2 . TYR A 1 270 ? 16.540  -6.139  86.965  1.00 40.80  ? 271 TYR A CE2 1 
ATOM   1870  C  CZ  . TYR A 1 270 ? 15.712  -5.131  87.408  1.00 45.08  ? 271 TYR A CZ  1 
ATOM   1871  O  OH  . TYR A 1 270 ? 14.981  -5.308  88.561  1.00 44.12  ? 271 TYR A OH  1 
ATOM   1872  N  N   . CYS A 1 271 ? 20.328  -3.017  84.874  1.00 36.63  ? 272 CYS A N   1 
ATOM   1873  C  CA  . CYS A 1 271 ? 21.237  -2.468  85.874  1.00 40.79  ? 272 CYS A CA  1 
ATOM   1874  C  C   . CYS A 1 271 ? 21.474  -0.976  85.657  1.00 34.90  ? 272 CYS A C   1 
ATOM   1875  O  O   . CYS A 1 271 ? 21.501  -0.192  86.610  1.00 34.51  ? 272 CYS A O   1 
ATOM   1876  C  CB  . CYS A 1 271 ? 22.568  -3.226  85.839  1.00 36.40  ? 272 CYS A CB  1 
ATOM   1877  S  SG  . CYS A 1 271 ? 23.811  -2.666  87.024  1.00 59.07  ? 272 CYS A SG  1 
ATOM   1878  N  N   . ARG A 1 272 ? 21.633  -0.591  84.395  1.00 34.44  ? 273 ARG A N   1 
ATOM   1879  C  CA  . ARG A 1 272 ? 21.923  0.792   84.051  1.00 42.55  ? 273 ARG A CA  1 
ATOM   1880  C  C   . ARG A 1 272 ? 20.733  1.709   84.300  1.00 33.27  ? 273 ARG A C   1 
ATOM   1881  O  O   . ARG A 1 272 ? 20.909  2.837   84.746  1.00 34.59  ? 273 ARG A O   1 
ATOM   1882  C  CB  . ARG A 1 272 ? 22.372  0.896   82.595  1.00 48.02  ? 273 ARG A CB  1 
ATOM   1883  C  CG  . ARG A 1 272 ? 23.875  1.041   82.446  1.00 48.31  ? 273 ARG A CG  1 
ATOM   1884  C  CD  . ARG A 1 272 ? 24.358  0.505   81.115  1.00 55.67  ? 273 ARG A CD  1 
ATOM   1885  N  NE  . ARG A 1 272 ? 25.456  -0.441  81.290  1.00 64.18  ? 273 ARG A NE  1 
ATOM   1886  C  CZ  . ARG A 1 272 ? 25.949  -1.201  80.318  1.00 70.41  ? 273 ARG A CZ  1 
ATOM   1887  N  NH1 . ARG A 1 272 ? 26.950  -2.033  80.569  1.00 74.93  ? 273 ARG A NH1 1 
ATOM   1888  N  NH2 . ARG A 1 272 ? 25.442  -1.129  79.096  1.00 72.57  ? 273 ARG A NH2 1 
ATOM   1889  N  N   . ASN A 1 273 ? 19.526  1.232   84.016  1.00 33.96  ? 274 ASN A N   1 
ATOM   1890  C  CA  . ASN A 1 273 ? 18.338  2.019   84.324  1.00 34.05  ? 274 ASN A CA  1 
ATOM   1891  C  C   . ASN A 1 273 ? 18.167  2.168   85.828  1.00 34.23  ? 274 ASN A C   1 
ATOM   1892  O  O   . ASN A 1 273 ? 17.831  3.252   86.322  1.00 33.96  ? 274 ASN A O   1 
ATOM   1893  C  CB  . ASN A 1 273 ? 17.090  1.395   83.704  1.00 34.89  ? 274 ASN A CB  1 
ATOM   1894  C  CG  . ASN A 1 273 ? 16.764  1.982   82.347  1.00 35.38  ? 274 ASN A CG  1 
ATOM   1895  O  OD1 . ASN A 1 273 ? 17.530  2.779   81.807  1.00 37.34  ? 274 ASN A OD1 1 
ATOM   1896  N  ND2 . ASN A 1 273 ? 15.622  1.600   81.792  1.00 35.48  ? 274 ASN A ND2 1 
ATOM   1897  N  N   . VAL A 1 274 ? 18.420  1.083   86.555  1.00 34.84  ? 275 VAL A N   1 
ATOM   1898  C  CA  . VAL A 1 274 ? 18.346  1.127   88.012  1.00 35.21  ? 275 VAL A CA  1 
ATOM   1899  C  C   . VAL A 1 274 ? 19.316  2.157   88.588  1.00 38.73  ? 275 VAL A C   1 
ATOM   1900  O  O   . VAL A 1 274 ? 18.914  3.031   89.358  1.00 38.35  ? 275 VAL A O   1 
ATOM   1901  C  CB  . VAL A 1 274 ? 18.642  -0.245  88.642  1.00 44.33  ? 275 VAL A CB  1 
ATOM   1902  C  CG1 . VAL A 1 274 ? 18.742  -0.121  90.155  1.00 36.54  ? 275 VAL A CG1 1 
ATOM   1903  C  CG2 . VAL A 1 274 ? 17.568  -1.250  88.254  1.00 46.04  ? 275 VAL A CG2 1 
ATOM   1904  N  N   . LEU A 1 275 ? 20.586  2.066   88.206  1.00 33.80  ? 276 LEU A N   1 
ATOM   1905  C  CA  . LEU A 1 275 ? 21.593  2.972   88.753  1.00 33.07  ? 276 LEU A CA  1 
ATOM   1906  C  C   . LEU A 1 275 ? 21.399  4.411   88.278  1.00 32.27  ? 276 LEU A C   1 
ATOM   1907  O  O   . LEU A 1 275 ? 21.684  5.351   89.017  1.00 31.93  ? 276 LEU A O   1 
ATOM   1908  C  CB  . LEU A 1 275 ? 23.003  2.489   88.408  1.00 32.75  ? 276 LEU A CB  1 
ATOM   1909  C  CG  . LEU A 1 275 ? 23.422  1.182   89.087  1.00 45.03  ? 276 LEU A CG  1 
ATOM   1910  C  CD1 . LEU A 1 275 ? 24.917  0.950   88.942  1.00 33.39  ? 276 LEU A CD1 1 
ATOM   1911  C  CD2 . LEU A 1 275 ? 23.017  1.181   90.554  1.00 45.06  ? 276 LEU A CD2 1 
ATOM   1912  N  N   . LYS A 1 276 ? 20.911  4.584   87.052  1.00 36.54  ? 277 LYS A N   1 
ATOM   1913  C  CA  . LYS A 1 276 ? 20.572  5.917   86.560  1.00 33.23  ? 277 LYS A CA  1 
ATOM   1914  C  C   . LYS A 1 276 ? 19.437  6.504   87.384  1.00 32.50  ? 277 LYS A C   1 
ATOM   1915  O  O   . LYS A 1 276 ? 19.377  7.714   87.596  1.00 32.69  ? 277 LYS A O   1 
ATOM   1916  C  CB  . LYS A 1 276 ? 20.187  5.886   85.080  1.00 31.57  ? 277 LYS A CB  1 
ATOM   1917  C  CG  . LYS A 1 276 ? 21.373  5.964   84.132  1.00 32.64  ? 277 LYS A CG  1 
ATOM   1918  C  CD  . LYS A 1 276 ? 20.926  5.964   82.681  1.00 34.84  ? 277 LYS A CD  1 
ATOM   1919  C  CE  . LYS A 1 276 ? 22.115  6.061   81.741  1.00 39.25  ? 277 LYS A CE  1 
ATOM   1920  N  NZ  . LYS A 1 276 ? 21.729  6.572   80.396  1.00 42.50  ? 277 LYS A NZ  1 
ATOM   1921  N  N   . GLY A 1 277 ? 18.538  5.640   87.845  1.00 38.10  ? 278 GLY A N   1 
ATOM   1922  C  CA  . GLY A 1 277 ? 17.490  6.066   88.753  1.00 37.59  ? 278 GLY A CA  1 
ATOM   1923  C  C   . GLY A 1 277 ? 18.061  6.462   90.103  1.00 37.56  ? 278 GLY A C   1 
ATOM   1924  O  O   . GLY A 1 277 ? 17.696  7.494   90.666  1.00 39.32  ? 278 GLY A O   1 
ATOM   1925  N  N   . CYS A 1 278 ? 18.973  5.642   90.615  1.00 36.24  ? 279 CYS A N   1 
ATOM   1926  C  CA  . CYS A 1 278 ? 19.566  5.867   91.929  1.00 33.85  ? 279 CYS A CA  1 
ATOM   1927  C  C   . CYS A 1 278 ? 20.513  7.063   91.958  1.00 38.03  ? 279 CYS A C   1 
ATOM   1928  O  O   . CYS A 1 278 ? 20.592  7.776   92.957  1.00 33.14  ? 279 CYS A O   1 
ATOM   1929  C  CB  . CYS A 1 278 ? 20.321  4.618   92.391  1.00 40.57  ? 279 CYS A CB  1 
ATOM   1930  S  SG  . CYS A 1 278 ? 19.288  3.159   92.638  1.00 60.38  ? 279 CYS A SG  1 
ATOM   1931  N  N   . LEU A 1 279 ? 21.230  7.279   90.861  1.00 40.37  ? 280 LEU A N   1 
ATOM   1932  C  CA  . LEU A 1 279 ? 22.300  8.270   90.841  1.00 39.42  ? 280 LEU A CA  1 
ATOM   1933  C  C   . LEU A 1 279 ? 21.983  9.463   89.943  1.00 30.62  ? 280 LEU A C   1 
ATOM   1934  O  O   . LEU A 1 279 ? 22.874  10.026  89.309  1.00 30.74  ? 280 LEU A O   1 
ATOM   1935  C  CB  . LEU A 1 279 ? 23.606  7.613   90.394  1.00 36.08  ? 280 LEU A CB  1 
ATOM   1936  C  CG  . LEU A 1 279 ? 23.988  6.333   91.141  1.00 37.40  ? 280 LEU A CG  1 
ATOM   1937  C  CD1 . LEU A 1 279 ? 25.301  5.775   90.613  1.00 38.10  ? 280 LEU A CD1 1 
ATOM   1938  C  CD2 . LEU A 1 279 ? 24.067  6.584   92.641  1.00 31.86  ? 280 LEU A CD2 1 
ATOM   1939  N  N   . ALA A 1 280 ? 20.713  9.847   89.899  1.00 36.03  ? 281 ALA A N   1 
ATOM   1940  C  CA  . ALA A 1 280 ? 20.274  10.960  89.064  1.00 37.65  ? 281 ALA A CA  1 
ATOM   1941  C  C   . ALA A 1 280 ? 20.803  12.298  89.581  1.00 30.60  ? 281 ALA A C   1 
ATOM   1942  O  O   . ALA A 1 280 ? 21.323  13.122  88.812  1.00 30.58  ? 281 ALA A O   1 
ATOM   1943  C  CB  . ALA A 1 280 ? 18.758  10.984  88.987  1.00 38.05  ? 281 ALA A CB  1 
ATOM   1944  N  N   . ASN A 1 281 ? 20.663  12.506  90.887  1.00 31.12  ? 282 ASN A N   1 
ATOM   1945  C  CA  . ASN A 1 281 ? 21.130  13.732  91.523  1.00 36.88  ? 282 ASN A CA  1 
ATOM   1946  C  C   . ASN A 1 281 ? 22.618  13.946  91.300  1.00 40.69  ? 282 ASN A C   1 
ATOM   1947  O  O   . ASN A 1 281 ? 23.043  15.045  90.948  1.00 29.55  ? 282 ASN A O   1 
ATOM   1948  C  CB  . ASN A 1 281 ? 20.820  13.714  93.020  1.00 38.28  ? 282 ASN A CB  1 
ATOM   1949  C  CG  . ASN A 1 281 ? 19.379  14.071  93.317  1.00 32.95  ? 282 ASN A CG  1 
ATOM   1950  O  OD1 . ASN A 1 281 ? 19.005  15.243  93.312  1.00 33.22  ? 282 ASN A OD1 1 
ATOM   1951  N  ND2 . ASN A 1 281 ? 18.560  13.059  93.575  1.00 45.01  ? 282 ASN A ND2 1 
ATOM   1952  N  N   . GLN A 1 282 ? 23.403  12.890  91.498  1.00 38.64  ? 283 GLN A N   1 
ATOM   1953  C  CA  . GLN A 1 282 ? 24.834  12.944  91.229  1.00 32.07  ? 283 GLN A CA  1 
ATOM   1954  C  C   . GLN A 1 282 ? 25.084  13.275  89.762  1.00 34.00  ? 283 GLN A C   1 
ATOM   1955  O  O   . GLN A 1 282 ? 26.026  13.992  89.428  1.00 37.91  ? 283 GLN A O   1 
ATOM   1956  C  CB  . GLN A 1 282 ? 25.511  11.617  91.590  1.00 30.92  ? 283 GLN A CB  1 
ATOM   1957  C  CG  . GLN A 1 282 ? 25.562  11.311  93.079  1.00 32.62  ? 283 GLN A CG  1 
ATOM   1958  C  CD  . GLN A 1 282 ? 24.324  10.587  93.576  1.00 42.14  ? 283 GLN A CD  1 
ATOM   1959  O  OE1 . GLN A 1 282 ? 23.292  10.562  92.906  1.00 42.75  ? 283 GLN A OE1 1 
ATOM   1960  N  NE2 . GLN A 1 282 ? 24.426  9.987   94.757  1.00 31.55  ? 283 GLN A NE2 1 
ATOM   1961  N  N   . ALA A 1 283 ? 24.224  12.754  88.891  1.00 35.71  ? 284 ALA A N   1 
ATOM   1962  C  CA  . ALA A 1 283 ? 24.365  12.962  87.455  1.00 38.07  ? 284 ALA A CA  1 
ATOM   1963  C  C   . ALA A 1 283 ? 24.002  14.389  87.045  1.00 37.77  ? 284 ALA A C   1 
ATOM   1964  O  O   . ALA A 1 283 ? 24.357  14.836  85.954  1.00 27.75  ? 284 ALA A O   1 
ATOM   1965  C  CB  . ALA A 1 283 ? 23.511  11.959  86.691  1.00 28.56  ? 284 ALA A CB  1 
ATOM   1966  N  N   . ASP A 1 284 ? 23.294  15.105  87.913  1.00 28.56  ? 285 ASP A N   1 
ATOM   1967  C  CA  . ASP A 1 284 ? 22.983  16.507  87.629  1.00 37.15  ? 285 ASP A CA  1 
ATOM   1968  C  C   . ASP A 1 284 ? 24.217  17.419  87.682  1.00 37.10  ? 285 ASP A C   1 
ATOM   1969  O  O   . ASP A 1 284 ? 24.175  18.552  87.204  1.00 28.08  ? 285 ASP A O   1 
ATOM   1970  C  CB  . ASP A 1 284 ? 21.917  17.026  88.594  1.00 38.11  ? 285 ASP A CB  1 
ATOM   1971  C  CG  . ASP A 1 284 ? 20.509  16.685  88.142  1.00 50.56  ? 285 ASP A CG  1 
ATOM   1972  O  OD1 . ASP A 1 284 ? 20.321  16.385  86.944  1.00 48.41  ? 285 ASP A OD1 1 
ATOM   1973  O  OD2 . ASP A 1 284 ? 19.588  16.728  88.984  1.00 50.52  ? 285 ASP A OD2 1 
ATOM   1974  N  N   . LEU A 1 285 ? 25.312  16.924  88.252  1.00 42.56  ? 286 LEU A N   1 
ATOM   1975  C  CA  . LEU A 1 285 ? 26.552  17.698  88.344  1.00 39.55  ? 286 LEU A CA  1 
ATOM   1976  C  C   . LEU A 1 285 ? 27.288  17.779  87.007  1.00 26.40  ? 286 LEU A C   1 
ATOM   1977  O  O   . LEU A 1 285 ? 28.251  18.537  86.862  1.00 25.97  ? 286 LEU A O   1 
ATOM   1978  C  CB  . LEU A 1 285 ? 27.484  17.091  89.394  1.00 37.52  ? 286 LEU A CB  1 
ATOM   1979  C  CG  . LEU A 1 285 ? 27.036  17.077  90.855  1.00 37.82  ? 286 LEU A CG  1 
ATOM   1980  C  CD1 . LEU A 1 285 ? 27.612  15.862  91.563  1.00 39.75  ? 286 LEU A CD1 1 
ATOM   1981  C  CD2 . LEU A 1 285 ? 27.473  18.353  91.553  1.00 27.37  ? 286 LEU A CD2 1 
ATOM   1982  N  N   . ASP A 1 286 ? 26.817  16.993  86.043  1.00 30.41  ? 287 ASP A N   1 
ATOM   1983  C  CA  . ASP A 1 286 ? 27.492  16.785  84.761  1.00 34.73  ? 287 ASP A CA  1 
ATOM   1984  C  C   . ASP A 1 286 ? 27.931  18.068  84.055  1.00 33.27  ? 287 ASP A C   1 
ATOM   1985  O  O   . ASP A 1 286 ? 29.120  18.260  83.792  1.00 33.74  ? 287 ASP A O   1 
ATOM   1986  C  CB  . ASP A 1 286 ? 26.578  15.984  83.827  1.00 26.66  ? 287 ASP A CB  1 
ATOM   1987  C  CG  . ASP A 1 286 ? 27.263  15.594  82.533  1.00 26.52  ? 287 ASP A CG  1 
ATOM   1988  O  OD1 . ASP A 1 286 ? 28.375  15.032  82.597  1.00 38.69  ? 287 ASP A OD1 1 
ATOM   1989  O  OD2 . ASP A 1 286 ? 26.690  15.848  81.453  1.00 29.12  ? 287 ASP A OD2 1 
ATOM   1990  N  N   . ALA A 1 287 ? 26.970  18.936  83.758  1.00 26.56  ? 288 ALA A N   1 
ATOM   1991  C  CA  . ALA A 1 287 ? 27.219  20.139  82.964  1.00 44.89  ? 288 ALA A CA  1 
ATOM   1992  C  C   . ALA A 1 287 ? 28.277  21.059  83.578  1.00 26.23  ? 288 ALA A C   1 
ATOM   1993  O  O   . ALA A 1 287 ? 29.207  21.492  82.895  1.00 25.97  ? 288 ALA A O   1 
ATOM   1994  C  CB  . ALA A 1 287 ? 25.918  20.904  82.761  1.00 27.48  ? 288 ALA A CB  1 
ATOM   1995  N  N   . GLU A 1 288 ? 28.132  21.353  84.865  1.00 26.26  ? 289 GLU A N   1 
ATOM   1996  C  CA  . GLU A 1 288 ? 29.030  22.289  85.528  1.00 25.99  ? 289 GLU A CA  1 
ATOM   1997  C  C   . GLU A 1 288 ? 30.386  21.656  85.828  1.00 36.16  ? 289 GLU A C   1 
ATOM   1998  O  O   . GLU A 1 288 ? 31.406  22.347  85.857  1.00 24.96  ? 289 GLU A O   1 
ATOM   1999  C  CB  . GLU A 1 288 ? 28.392  22.823  86.812  1.00 26.45  ? 289 GLU A CB  1 
ATOM   2000  C  CG  . GLU A 1 288 ? 27.111  23.612  86.579  1.00 35.71  ? 289 GLU A CG  1 
ATOM   2001  C  CD  . GLU A 1 288 ? 27.227  24.607  85.435  1.00 46.70  ? 289 GLU A CD  1 
ATOM   2002  O  OE1 . GLU A 1 288 ? 28.239  25.339  85.375  1.00 46.69  ? 289 GLU A OE1 1 
ATOM   2003  O  OE2 . GLU A 1 288 ? 26.305  24.653  84.593  1.00 48.22  ? 289 GLU A OE2 1 
ATOM   2004  N  N   . TRP A 1 289 ? 30.393  20.344  86.050  1.00 36.09  ? 290 TRP A N   1 
ATOM   2005  C  CA  . TRP A 1 289 ? 31.646  19.611  86.204  1.00 24.65  ? 290 TRP A CA  1 
ATOM   2006  C  C   . TRP A 1 289 ? 32.446  19.709  84.906  1.00 31.11  ? 290 TRP A C   1 
ATOM   2007  O  O   . TRP A 1 289 ? 33.638  20.036  84.917  1.00 29.05  ? 290 TRP A O   1 
ATOM   2008  C  CB  . TRP A 1 289 ? 31.368  18.152  86.579  1.00 25.37  ? 290 TRP A CB  1 
ATOM   2009  C  CG  . TRP A 1 289 ? 32.575  17.262  86.670  1.00 24.49  ? 290 TRP A CG  1 
ATOM   2010  C  CD1 . TRP A 1 289 ? 33.065  16.448  85.691  1.00 30.99  ? 290 TRP A CD1 1 
ATOM   2011  C  CD2 . TRP A 1 289 ? 33.425  17.072  87.811  1.00 24.39  ? 290 TRP A CD2 1 
ATOM   2012  N  NE1 . TRP A 1 289 ? 34.171  15.771  86.146  1.00 33.15  ? 290 TRP A NE1 1 
ATOM   2013  C  CE2 . TRP A 1 289 ? 34.413  16.137  87.444  1.00 27.46  ? 290 TRP A CE2 1 
ATOM   2014  C  CE3 . TRP A 1 289 ? 33.448  17.606  89.104  1.00 27.54  ? 290 TRP A CE3 1 
ATOM   2015  C  CZ2 . TRP A 1 289 ? 35.415  15.725  88.322  1.00 30.97  ? 290 TRP A CZ2 1 
ATOM   2016  C  CZ3 . TRP A 1 289 ? 34.444  17.196  89.974  1.00 25.87  ? 290 TRP A CZ3 1 
ATOM   2017  C  CH2 . TRP A 1 289 ? 35.414  16.264  89.579  1.00 31.27  ? 290 TRP A CH2 1 
ATOM   2018  N  N   . ARG A 1 290 ? 31.772  19.451  83.789  1.00 24.70  ? 291 ARG A N   1 
ATOM   2019  C  CA  . ARG A 1 290 ? 32.395  19.547  82.473  1.00 24.71  ? 291 ARG A CA  1 
ATOM   2020  C  C   . ARG A 1 290 ? 32.861  20.966  82.171  1.00 35.07  ? 291 ARG A C   1 
ATOM   2021  O  O   . ARG A 1 290 ? 33.926  21.158  81.587  1.00 33.68  ? 291 ARG A O   1 
ATOM   2022  C  CB  . ARG A 1 290 ? 31.431  19.077  81.382  1.00 25.22  ? 291 ARG A CB  1 
ATOM   2023  C  CG  . ARG A 1 290 ? 31.155  17.582  81.394  1.00 30.88  ? 291 ARG A CG  1 
ATOM   2024  C  CD  . ARG A 1 290 ? 30.242  17.188  80.246  1.00 34.94  ? 291 ARG A CD  1 
ATOM   2025  N  NE  . ARG A 1 290 ? 29.832  15.790  80.323  1.00 39.96  ? 291 ARG A NE  1 
ATOM   2026  C  CZ  . ARG A 1 290 ? 30.513  14.779  79.793  1.00 38.62  ? 291 ARG A CZ  1 
ATOM   2027  N  NH1 . ARG A 1 290 ? 31.648  15.006  79.147  1.00 26.11  ? 291 ARG A NH1 1 
ATOM   2028  N  NH2 . ARG A 1 290 ? 30.060  13.538  79.912  1.00 26.48  ? 291 ARG A NH2 1 
ATOM   2029  N  N   . ASN A 1 291 ? 32.060  21.956  82.559  1.00 37.24  ? 292 ASN A N   1 
ATOM   2030  C  CA  . ASN A 1 291 ? 32.440  23.354  82.378  1.00 31.20  ? 292 ASN A CA  1 
ATOM   2031  C  C   . ASN A 1 291 ? 33.719  23.687  83.138  1.00 31.03  ? 292 ASN A C   1 
ATOM   2032  O  O   . ASN A 1 291 ? 34.671  24.255  82.576  1.00 27.21  ? 292 ASN A O   1 
ATOM   2033  C  CB  . ASN A 1 291 ? 31.312  24.285  82.831  1.00 25.66  ? 292 ASN A CB  1 
ATOM   2034  C  CG  . ASN A 1 291 ? 30.164  24.336  81.843  1.00 35.09  ? 292 ASN A CG  1 
ATOM   2035  O  OD1 . ASN A 1 291 ? 30.347  24.103  80.648  1.00 33.92  ? 292 ASN A OD1 1 
ATOM   2036  N  ND2 . ASN A 1 291 ? 28.971  24.646  82.339  1.00 26.93  ? 292 ASN A ND2 1 
ATOM   2037  N  N   . LEU A 1 292 ? 33.733  23.325  84.418  1.00 24.34  ? 293 LEU A N   1 
ATOM   2038  C  CA  . LEU A 1 292 ? 34.890  23.573  85.264  1.00 32.90  ? 293 LEU A CA  1 
ATOM   2039  C  C   . LEU A 1 292 ? 36.134  22.909  84.701  1.00 29.93  ? 293 LEU A C   1 
ATOM   2040  O  O   . LEU A 1 292 ? 37.167  23.556  84.549  1.00 23.42  ? 293 LEU A O   1 
ATOM   2041  C  CB  . LEU A 1 292 ? 34.651  23.077  86.690  1.00 33.49  ? 293 LEU A CB  1 
ATOM   2042  C  CG  . LEU A 1 292 ? 35.797  23.465  87.625  1.00 36.57  ? 293 LEU A CG  1 
ATOM   2043  C  CD1 . LEU A 1 292 ? 35.863  24.977  87.748  1.00 37.28  ? 293 LEU A CD1 1 
ATOM   2044  C  CD2 . LEU A 1 292 ? 35.660  22.818  88.993  1.00 34.45  ? 293 LEU A CD2 1 
ATOM   2045  N  N   . LEU A 1 293 ? 36.033  21.620  84.388  1.00 23.56  ? 294 LEU A N   1 
ATOM   2046  C  CA  . LEU A 1 293 ? 37.189  20.882  83.886  1.00 34.19  ? 294 LEU A CA  1 
ATOM   2047  C  C   . LEU A 1 293 ? 37.660  21.427  82.539  1.00 36.09  ? 294 LEU A C   1 
ATOM   2048  O  O   . LEU A 1 293 ? 38.856  21.419  82.246  1.00 23.49  ? 294 LEU A O   1 
ATOM   2049  C  CB  . LEU A 1 293 ? 36.875  19.390  83.777  1.00 30.00  ? 294 LEU A CB  1 
ATOM   2050  C  CG  . LEU A 1 293 ? 37.242  18.547  85.002  1.00 29.35  ? 294 LEU A CG  1 
ATOM   2051  C  CD1 . LEU A 1 293 ? 36.386  18.914  86.204  1.00 27.58  ? 294 LEU A CD1 1 
ATOM   2052  C  CD2 . LEU A 1 293 ? 37.119  17.065  84.687  1.00 32.44  ? 294 LEU A CD2 1 
ATOM   2053  N  N   . ASP A 1 294 ? 36.722  21.910  81.729  1.00 40.38  ? 295 ASP A N   1 
ATOM   2054  C  CA  . ASP A 1 294 ? 37.066  22.542  80.459  1.00 43.32  ? 295 ASP A CA  1 
ATOM   2055  C  C   . ASP A 1 294 ? 37.876  23.815  80.679  1.00 30.94  ? 295 ASP A C   1 
ATOM   2056  O  O   . ASP A 1 294 ? 38.923  24.011  80.053  1.00 26.19  ? 295 ASP A O   1 
ATOM   2057  C  CB  . ASP A 1 294 ? 35.809  22.859  79.649  1.00 49.15  ? 295 ASP A CB  1 
ATOM   2058  C  CG  . ASP A 1 294 ? 35.520  21.815  78.588  1.00 64.33  ? 295 ASP A CG  1 
ATOM   2059  O  OD1 . ASP A 1 294 ? 35.968  20.659  78.748  1.00 67.29  ? 295 ASP A OD1 1 
ATOM   2060  O  OD2 . ASP A 1 294 ? 34.845  22.152  77.592  1.00 67.03  ? 295 ASP A OD2 1 
ATOM   2061  N  N   . SER A 1 295 ? 37.396  24.676  81.573  1.00 24.12  ? 296 SER A N   1 
ATOM   2062  C  CA  . SER A 1 295 ? 38.105  25.923  81.853  1.00 28.38  ? 296 SER A CA  1 
ATOM   2063  C  C   . SER A 1 295 ? 39.455  25.651  82.521  1.00 29.17  ? 296 SER A C   1 
ATOM   2064  O  O   . SER A 1 295 ? 40.398  26.430  82.378  1.00 26.00  ? 296 SER A O   1 
ATOM   2065  C  CB  . SER A 1 295 ? 37.251  26.848  82.727  1.00 24.30  ? 296 SER A CB  1 
ATOM   2066  O  OG  . SER A 1 295 ? 37.155  26.366  84.055  1.00 26.54  ? 296 SER A OG  1 
ATOM   2067  N  N   . MET A 1 296 ? 39.545  24.534  83.236  1.00 33.48  ? 297 MET A N   1 
ATOM   2068  C  CA  . MET A 1 296 ? 40.778  24.147  83.912  1.00 35.02  ? 297 MET A CA  1 
ATOM   2069  C  C   . MET A 1 296 ? 41.804  23.611  82.921  1.00 30.55  ? 297 MET A C   1 
ATOM   2070  O  O   . MET A 1 296 ? 43.004  23.833  83.077  1.00 34.48  ? 297 MET A O   1 
ATOM   2071  C  CB  . MET A 1 296 ? 40.493  23.104  84.993  1.00 32.94  ? 297 MET A CB  1 
ATOM   2072  C  CG  . MET A 1 296 ? 40.040  23.699  86.316  1.00 26.61  ? 297 MET A CG  1 
ATOM   2073  S  SD  . MET A 1 296 ? 40.093  22.517  87.677  1.00 59.18  ? 297 MET A SD  1 
ATOM   2074  C  CE  . MET A 1 296 ? 38.934  21.285  87.103  1.00 86.21  ? 297 MET A CE  1 
ATOM   2075  N  N   . VAL A 1 297 ? 41.330  22.898  81.905  1.00 27.81  ? 298 VAL A N   1 
ATOM   2076  C  CA  . VAL A 1 297 ? 42.204  22.462  80.826  1.00 27.62  ? 298 VAL A CA  1 
ATOM   2077  C  C   . VAL A 1 297 ? 42.682  23.685  80.052  1.00 33.83  ? 298 VAL A C   1 
ATOM   2078  O  O   . VAL A 1 297 ? 43.858  23.793  79.700  1.00 30.47  ? 298 VAL A O   1 
ATOM   2079  C  CB  . VAL A 1 297 ? 41.497  21.473  79.875  1.00 30.27  ? 298 VAL A CB  1 
ATOM   2080  C  CG1 . VAL A 1 297 ? 42.274  21.320  78.576  1.00 30.33  ? 298 VAL A CG1 1 
ATOM   2081  C  CG2 . VAL A 1 297 ? 41.314  20.123  80.553  1.00 33.64  ? 298 VAL A CG2 1 
ATOM   2082  N  N   . LEU A 1 298 ? 41.766  24.619  79.815  1.00 34.22  ? 299 LEU A N   1 
ATOM   2083  C  CA  . LEU A 1 298 ? 42.086  25.828  79.062  1.00 34.54  ? 299 LEU A CA  1 
ATOM   2084  C  C   . LEU A 1 298 ? 43.094  26.736  79.762  1.00 35.00  ? 299 LEU A C   1 
ATOM   2085  O  O   . LEU A 1 298 ? 43.984  27.287  79.115  1.00 28.42  ? 299 LEU A O   1 
ATOM   2086  C  CB  . LEU A 1 298 ? 40.812  26.622  78.767  1.00 35.24  ? 299 LEU A CB  1 
ATOM   2087  C  CG  . LEU A 1 298 ? 40.070  26.231  77.489  1.00 47.21  ? 299 LEU A CG  1 
ATOM   2088  C  CD1 . LEU A 1 298 ? 38.878  27.147  77.259  1.00 46.77  ? 299 LEU A CD1 1 
ATOM   2089  C  CD2 . LEU A 1 298 ? 41.019  26.265  76.300  1.00 47.68  ? 299 LEU A CD2 1 
ATOM   2090  N  N   . ILE A 1 299 ? 42.957  26.892  81.076  1.00 26.99  ? 300 ILE A N   1 
ATOM   2091  C  CA  . ILE A 1 299 ? 43.781  27.848  81.815  1.00 30.96  ? 300 ILE A CA  1 
ATOM   2092  C  C   . ILE A 1 299 ? 45.268  27.473  81.815  1.00 37.75  ? 300 ILE A C   1 
ATOM   2093  O  O   . ILE A 1 299 ? 46.128  28.340  81.975  1.00 35.71  ? 300 ILE A O   1 
ATOM   2094  C  CB  . ILE A 1 299 ? 43.292  28.001  83.279  1.00 23.34  ? 300 ILE A CB  1 
ATOM   2095  C  CG1 . ILE A 1 299 ? 43.884  29.261  83.918  1.00 23.40  ? 300 ILE A CG1 1 
ATOM   2096  C  CG2 . ILE A 1 299 ? 43.627  26.769  84.102  1.00 24.32  ? 300 ILE A CG2 1 
ATOM   2097  C  CD1 . ILE A 1 299 ? 43.476  30.545  83.227  1.00 23.95  ? 300 ILE A CD1 1 
ATOM   2098  N  N   . THR A 1 300 ? 45.570  26.193  81.613  1.00 28.40  ? 301 THR A N   1 
ATOM   2099  C  CA  . THR A 1 300 ? 46.955  25.723  81.648  1.00 31.94  ? 301 THR A CA  1 
ATOM   2100  C  C   . THR A 1 300 ? 47.801  26.320  80.527  1.00 29.04  ? 301 THR A C   1 
ATOM   2101  O  O   . THR A 1 300 ? 49.023  26.395  80.638  1.00 25.35  ? 301 THR A O   1 
ATOM   2102  C  CB  . THR A 1 300 ? 47.036  24.184  81.560  1.00 31.73  ? 301 THR A CB  1 
ATOM   2103  O  OG1 . THR A 1 300 ? 46.512  23.742  80.302  1.00 34.13  ? 301 THR A OG1 1 
ATOM   2104  C  CG2 . THR A 1 300 ? 46.253  23.544  82.691  1.00 23.26  ? 301 THR A CG2 1 
ATOM   2105  N  N   . ASP A 1 301 ? 47.148  26.743  79.449  1.00 39.11  ? 302 ASP A N   1 
ATOM   2106  C  CA  . ASP A 1 301 ? 47.847  27.367  78.331  1.00 34.55  ? 302 ASP A CA  1 
ATOM   2107  C  C   . ASP A 1 301 ? 48.494  28.681  78.757  1.00 34.41  ? 302 ASP A C   1 
ATOM   2108  O  O   . ASP A 1 301 ? 49.539  29.072  78.233  1.00 27.32  ? 302 ASP A O   1 
ATOM   2109  C  CB  . ASP A 1 301 ? 46.887  27.613  77.163  1.00 35.15  ? 302 ASP A CB  1 
ATOM   2110  C  CG  . ASP A 1 301 ? 46.462  26.330  76.475  1.00 47.22  ? 302 ASP A CG  1 
ATOM   2111  O  OD1 . ASP A 1 301 ? 47.204  25.329  76.564  1.00 47.86  ? 302 ASP A OD1 1 
ATOM   2112  O  OD2 . ASP A 1 301 ? 45.386  26.324  75.843  1.00 50.03  ? 302 ASP A OD2 1 
ATOM   2113  N  N   . LYS A 1 302 ? 47.867  29.348  79.722  1.00 29.07  ? 303 LYS A N   1 
ATOM   2114  C  CA  . LYS A 1 302 ? 48.308  30.664  80.171  1.00 33.31  ? 303 LYS A CA  1 
ATOM   2115  C  C   . LYS A 1 302 ? 49.531  30.599  81.079  1.00 36.14  ? 303 LYS A C   1 
ATOM   2116  O  O   . LYS A 1 302 ? 50.050  31.634  81.495  1.00 34.27  ? 303 LYS A O   1 
ATOM   2117  C  CB  . LYS A 1 302 ? 47.167  31.387  80.893  1.00 26.56  ? 303 LYS A CB  1 
ATOM   2118  C  CG  . LYS A 1 302 ? 45.978  31.693  80.004  1.00 25.25  ? 303 LYS A CG  1 
ATOM   2119  C  CD  . LYS A 1 302 ? 46.424  32.370  78.718  1.00 39.98  ? 303 LYS A CD  1 
ATOM   2120  C  CE  . LYS A 1 302 ? 45.248  32.982  77.974  1.00 46.67  ? 303 LYS A CE  1 
ATOM   2121  N  NZ  . LYS A 1 302 ? 45.696  33.745  76.776  1.00 49.64  ? 303 LYS A NZ  1 
ATOM   2122  N  N   . PHE A 1 303 ? 49.991  29.389  81.383  1.00 29.17  ? 304 PHE A N   1 
ATOM   2123  C  CA  . PHE A 1 303 ? 51.185  29.221  82.207  1.00 27.49  ? 304 PHE A CA  1 
ATOM   2124  C  C   . PHE A 1 303 ? 52.416  29.730  81.462  1.00 33.13  ? 304 PHE A C   1 
ATOM   2125  O  O   . PHE A 1 303 ? 53.411  30.119  82.075  1.00 30.16  ? 304 PHE A O   1 
ATOM   2126  C  CB  . PHE A 1 303 ? 51.375  27.754  82.610  1.00 29.57  ? 304 PHE A CB  1 
ATOM   2127  C  CG  . PHE A 1 303 ? 50.320  27.235  83.556  1.00 36.34  ? 304 PHE A CG  1 
ATOM   2128  C  CD1 . PHE A 1 303 ? 49.356  28.081  84.087  1.00 34.26  ? 304 PHE A CD1 1 
ATOM   2129  C  CD2 . PHE A 1 303 ? 50.300  25.897  83.917  1.00 34.91  ? 304 PHE A CD2 1 
ATOM   2130  C  CE1 . PHE A 1 303 ? 48.391  27.600  84.953  1.00 32.40  ? 304 PHE A CE1 1 
ATOM   2131  C  CE2 . PHE A 1 303 ? 49.337  25.411  84.785  1.00 34.69  ? 304 PHE A CE2 1 
ATOM   2132  C  CZ  . PHE A 1 303 ? 48.382  26.263  85.303  1.00 32.94  ? 304 PHE A CZ  1 
ATOM   2133  N  N   . TRP A 1 304 ? 52.339  29.727  80.134  1.00 35.53  ? 305 TRP A N   1 
ATOM   2134  C  CA  . TRP A 1 304 ? 53.416  30.240  79.296  1.00 36.56  ? 305 TRP A CA  1 
ATOM   2135  C  C   . TRP A 1 304 ? 52.933  31.360  78.385  1.00 43.80  ? 305 TRP A C   1 
ATOM   2136  O  O   . TRP A 1 304 ? 51.730  31.581  78.235  1.00 43.09  ? 305 TRP A O   1 
ATOM   2137  C  CB  . TRP A 1 304 ? 54.019  29.130  78.437  1.00 29.69  ? 305 TRP A CB  1 
ATOM   2138  C  CG  . TRP A 1 304 ? 54.504  27.946  79.197  1.00 33.11  ? 305 TRP A CG  1 
ATOM   2139  C  CD1 . TRP A 1 304 ? 55.759  27.747  79.694  1.00 33.81  ? 305 TRP A CD1 1 
ATOM   2140  C  CD2 . TRP A 1 304 ? 53.748  26.779  79.533  1.00 31.86  ? 305 TRP A CD2 1 
ATOM   2141  N  NE1 . TRP A 1 304 ? 55.829  26.528  80.326  1.00 34.93  ? 305 TRP A NE1 1 
ATOM   2142  C  CE2 . TRP A 1 304 ? 54.607  25.914  80.240  1.00 35.16  ? 305 TRP A CE2 1 
ATOM   2143  C  CE3 . TRP A 1 304 ? 52.427  26.382  79.307  1.00 31.27  ? 305 TRP A CE3 1 
ATOM   2144  C  CZ2 . TRP A 1 304 ? 54.187  24.677  80.722  1.00 30.65  ? 305 TRP A CZ2 1 
ATOM   2145  C  CZ3 . TRP A 1 304 ? 52.011  25.153  79.787  1.00 32.07  ? 305 TRP A CZ3 1 
ATOM   2146  C  CH2 . TRP A 1 304 ? 52.888  24.316  80.488  1.00 31.10  ? 305 TRP A CH2 1 
ATOM   2147  N  N   . GLY A 1 305 ? 53.884  32.060  77.777  1.00 45.35  ? 306 GLY A N   1 
ATOM   2148  C  CA  . GLY A 1 305 ? 53.581  33.036  76.749  1.00 45.48  ? 306 GLY A CA  1 
ATOM   2149  C  C   . GLY A 1 305 ? 53.631  32.380  75.382  1.00 50.41  ? 306 GLY A C   1 
ATOM   2150  O  O   . GLY A 1 305 ? 53.801  31.165  75.276  1.00 48.81  ? 306 GLY A O   1 
ATOM   2151  N  N   . THR A 1 306 ? 53.474  33.181  74.334  1.00 56.37  ? 307 THR A N   1 
ATOM   2152  C  CA  . THR A 1 306 ? 53.476  32.668  72.967  1.00 67.12  ? 307 THR A CA  1 
ATOM   2153  C  C   . THR A 1 306 ? 54.840  32.779  72.281  1.00 75.81  ? 307 THR A C   1 
ATOM   2154  O  O   . THR A 1 306 ? 54.995  32.368  71.131  1.00 81.62  ? 307 THR A O   1 
ATOM   2155  C  CB  . THR A 1 306 ? 52.431  33.398  72.103  1.00 73.73  ? 307 THR A CB  1 
ATOM   2156  O  OG1 . THR A 1 306 ? 52.681  34.809  72.140  1.00 74.74  ? 307 THR A OG1 1 
ATOM   2157  C  CG2 . THR A 1 306 ? 51.026  33.125  72.622  1.00 72.04  ? 307 THR A CG2 1 
ATOM   2158  N  N   . SER A 1 307 ? 55.824  33.330  72.985  1.00 71.66  ? 308 SER A N   1 
ATOM   2159  C  CA  . SER A 1 307 ? 57.112  33.655  72.374  1.00 71.18  ? 308 SER A CA  1 
ATOM   2160  C  C   . SER A 1 307 ? 58.151  32.535  72.462  1.00 69.99  ? 308 SER A C   1 
ATOM   2161  O  O   . SER A 1 307 ? 59.295  32.713  72.041  1.00 71.74  ? 308 SER A O   1 
ATOM   2162  C  CB  . SER A 1 307 ? 57.684  34.927  73.005  1.00 71.53  ? 308 SER A CB  1 
ATOM   2163  O  OG  . SER A 1 307 ? 56.882  36.053  72.696  1.00 69.33  ? 308 SER A OG  1 
ATOM   2164  N  N   . GLY A 1 308 ? 57.762  31.390  73.011  1.00 64.66  ? 309 GLY A N   1 
ATOM   2165  C  CA  . GLY A 1 308 ? 58.678  30.270  73.136  1.00 63.90  ? 309 GLY A CA  1 
ATOM   2166  C  C   . GLY A 1 308 ? 59.665  30.474  74.268  1.00 58.89  ? 309 GLY A C   1 
ATOM   2167  O  O   . GLY A 1 308 ? 60.812  30.033  74.205  1.00 62.18  ? 309 GLY A O   1 
ATOM   2168  N  N   . VAL A 1 309 ? 59.199  31.144  75.315  1.00 58.19  ? 310 VAL A N   1 
ATOM   2169  C  CA  . VAL A 1 309 ? 60.011  31.454  76.483  1.00 53.50  ? 310 VAL A CA  1 
ATOM   2170  C  C   . VAL A 1 309 ? 59.475  30.633  77.649  1.00 55.72  ? 310 VAL A C   1 
ATOM   2171  O  O   . VAL A 1 309 ? 58.295  30.281  77.665  1.00 54.28  ? 310 VAL A O   1 
ATOM   2172  C  CB  . VAL A 1 309 ? 59.977  32.966  76.815  1.00 51.69  ? 310 VAL A CB  1 
ATOM   2173  C  CG1 . VAL A 1 309 ? 60.923  33.304  77.961  1.00 49.97  ? 310 VAL A CG1 1 
ATOM   2174  C  CG2 . VAL A 1 309 ? 60.325  33.785  75.583  1.00 50.86  ? 310 VAL A CG2 1 
ATOM   2175  N  N   . GLU A 1 310 ? 60.327  30.319  78.620  1.00 54.88  ? 311 GLU A N   1 
ATOM   2176  C  CA  . GLU A 1 310 ? 59.908  29.474  79.728  1.00 54.33  ? 311 GLU A CA  1 
ATOM   2177  C  C   . GLU A 1 310 ? 58.936  30.238  80.616  1.00 49.67  ? 311 GLU A C   1 
ATOM   2178  O  O   . GLU A 1 310 ? 58.666  31.415  80.382  1.00 48.69  ? 311 GLU A O   1 
ATOM   2179  C  CB  . GLU A 1 310 ? 61.121  29.020  80.541  1.00 60.66  ? 311 GLU A CB  1 
ATOM   2180  C  CG  . GLU A 1 310 ? 62.089  30.153  80.853  1.00 71.03  ? 311 GLU A CG  1 
ATOM   2181  C  CD  . GLU A 1 310 ? 63.060  29.815  81.967  1.00 78.21  ? 311 GLU A CD  1 
ATOM   2182  O  OE1 . GLU A 1 310 ? 62.743  28.927  82.785  1.00 80.86  ? 311 GLU A OE1 1 
ATOM   2183  O  OE2 . GLU A 1 310 ? 64.139  30.441  82.025  1.00 80.22  ? 311 GLU A OE2 1 
ATOM   2184  N  N   . SER A 1 311 ? 58.424  29.579  81.649  1.00 43.97  ? 312 SER A N   1 
ATOM   2185  C  CA  . SER A 1 311 ? 57.400  30.194  82.480  1.00 42.81  ? 312 SER A CA  1 
ATOM   2186  C  C   . SER A 1 311 ? 58.029  31.167  83.464  1.00 38.94  ? 312 SER A C   1 
ATOM   2187  O  O   . SER A 1 311 ? 59.070  30.882  84.056  1.00 34.01  ? 312 SER A O   1 
ATOM   2188  C  CB  . SER A 1 311 ? 56.589  29.133  83.223  1.00 30.23  ? 312 SER A CB  1 
ATOM   2189  O  OG  . SER A 1 311 ? 55.507  29.726  83.920  1.00 24.56  ? 312 SER A OG  1 
ATOM   2190  N  N   . VAL A 1 312 ? 57.389  32.319  83.633  1.00 25.38  ? 313 VAL A N   1 
ATOM   2191  C  CA  . VAL A 1 312 ? 57.913  33.372  84.491  1.00 28.00  ? 313 VAL A CA  1 
ATOM   2192  C  C   . VAL A 1 312 ? 57.838  32.977  85.967  1.00 28.45  ? 313 VAL A C   1 
ATOM   2193  O  O   . VAL A 1 312 ? 58.587  33.495  86.794  1.00 34.63  ? 313 VAL A O   1 
ATOM   2194  C  CB  . VAL A 1 312 ? 57.155  34.699  84.264  1.00 32.92  ? 313 VAL A CB  1 
ATOM   2195  C  CG1 . VAL A 1 312 ? 55.717  34.589  84.754  1.00 29.91  ? 313 VAL A CG1 1 
ATOM   2196  C  CG2 . VAL A 1 312 ? 57.873  35.855  84.943  1.00 26.42  ? 313 VAL A CG2 1 
ATOM   2197  N  N   . ILE A 1 313 ? 56.948  32.040  86.284  1.00 25.83  ? 314 ILE A N   1 
ATOM   2198  C  CA  . ILE A 1 313 ? 56.745  31.589  87.659  1.00 32.79  ? 314 ILE A CA  1 
ATOM   2199  C  C   . ILE A 1 313 ? 58.047  31.081  88.281  1.00 31.84  ? 314 ILE A C   1 
ATOM   2200  O  O   . ILE A 1 313 ? 58.262  31.197  89.489  1.00 31.42  ? 314 ILE A O   1 
ATOM   2201  C  CB  . ILE A 1 313 ? 55.664  30.485  87.725  1.00 38.06  ? 314 ILE A CB  1 
ATOM   2202  C  CG1 . ILE A 1 313 ? 54.332  31.021  87.194  1.00 40.22  ? 314 ILE A CG1 1 
ATOM   2203  C  CG2 . ILE A 1 313 ? 55.486  29.968  89.146  1.00 29.86  ? 314 ILE A CG2 1 
ATOM   2204  C  CD1 . ILE A 1 313 ? 53.301  29.947  86.927  1.00 42.47  ? 314 ILE A CD1 1 
ATOM   2205  N  N   . GLY A 1 314 ? 58.927  30.543  87.445  1.00 24.92  ? 315 GLY A N   1 
ATOM   2206  C  CA  . GLY A 1 314 ? 60.213  30.071  87.915  1.00 33.47  ? 315 GLY A CA  1 
ATOM   2207  C  C   . GLY A 1 314 ? 61.398  30.812  87.322  1.00 33.05  ? 315 GLY A C   1 
ATOM   2208  O  O   . GLY A 1 314 ? 62.535  30.357  87.445  1.00 34.22  ? 315 GLY A O   1 
ATOM   2209  N  N   . SER A 1 315 ? 61.147  31.956  86.689  1.00 31.25  ? 316 SER A N   1 
ATOM   2210  C  CA  . SER A 1 315 ? 62.218  32.683  86.010  1.00 38.56  ? 316 SER A CA  1 
ATOM   2211  C  C   . SER A 1 315 ? 62.141  34.206  86.168  1.00 34.52  ? 316 SER A C   1 
ATOM   2212  O  O   . SER A 1 315 ? 62.635  34.942  85.315  1.00 37.94  ? 316 SER A O   1 
ATOM   2213  C  CB  . SER A 1 315 ? 62.225  32.327  84.521  1.00 37.41  ? 316 SER A CB  1 
ATOM   2214  O  OG  . SER A 1 315 ? 61.114  32.899  83.854  1.00 43.82  ? 316 SER A OG  1 
ATOM   2215  N  N   . VAL A 1 316 ? 61.532  34.668  87.256  1.00 29.77  ? 317 VAL A N   1 
ATOM   2216  C  CA  . VAL A 1 316 ? 61.450  36.098  87.563  1.00 36.17  ? 317 VAL A CA  1 
ATOM   2217  C  C   . VAL A 1 316 ? 62.839  36.746  87.635  1.00 42.85  ? 317 VAL A C   1 
ATOM   2218  O  O   . VAL A 1 316 ? 63.067  37.862  87.131  1.00 44.43  ? 317 VAL A O   1 
ATOM   2219  C  CB  . VAL A 1 316 ? 60.710  36.332  88.901  1.00 32.38  ? 317 VAL A CB  1 
ATOM   2220  C  CG1 . VAL A 1 316 ? 60.818  37.784  89.334  1.00 30.56  ? 317 VAL A CG1 1 
ATOM   2221  C  CG2 . VAL A 1 316 ? 59.252  35.908  88.790  1.00 30.42  ? 317 VAL A CG2 1 
ATOM   2222  N  N   . HIS A 1 317 ? 63.767  36.020  88.253  1.00 38.90  ? 318 HIS A N   1 
ATOM   2223  C  CA  . HIS A 1 317 ? 65.124  36.503  88.473  1.00 27.64  ? 318 HIS A CA  1 
ATOM   2224  C  C   . HIS A 1 317 ? 65.836  36.849  87.170  1.00 41.35  ? 318 HIS A C   1 
ATOM   2225  O  O   . HIS A 1 317 ? 66.696  37.726  87.145  1.00 45.64  ? 318 HIS A O   1 
ATOM   2226  C  CB  . HIS A 1 317 ? 65.937  35.464  89.249  1.00 27.83  ? 318 HIS A CB  1 
ATOM   2227  C  CG  . HIS A 1 317 ? 66.044  34.138  88.562  1.00 37.49  ? 318 HIS A CG  1 
ATOM   2228  N  ND1 . HIS A 1 317 ? 65.059  33.177  88.640  1.00 35.26  ? 318 HIS A ND1 1 
ATOM   2229  C  CD2 . HIS A 1 317 ? 67.022  33.612  87.788  1.00 36.86  ? 318 HIS A CD2 1 
ATOM   2230  C  CE1 . HIS A 1 317 ? 65.425  32.117  87.941  1.00 36.41  ? 318 HIS A CE1 1 
ATOM   2231  N  NE2 . HIS A 1 317 ? 66.612  32.355  87.415  1.00 41.66  ? 318 HIS A NE2 1 
ATOM   2232  N  N   . THR A 1 318 ? 65.479  36.159  86.091  1.00 45.27  ? 319 THR A N   1 
ATOM   2233  C  CA  . THR A 1 318 ? 66.082  36.422  84.790  1.00 42.22  ? 319 THR A CA  1 
ATOM   2234  C  C   . THR A 1 318 ? 65.690  37.809  84.288  1.00 45.55  ? 319 THR A C   1 
ATOM   2235  O  O   . THR A 1 318 ? 66.532  38.569  83.797  1.00 46.61  ? 319 THR A O   1 
ATOM   2236  C  CB  . THR A 1 318 ? 65.668  35.365  83.749  1.00 39.85  ? 319 THR A CB  1 
ATOM   2237  O  OG1 . THR A 1 318 ? 64.278  35.514  83.435  1.00 45.94  ? 319 THR A OG1 1 
ATOM   2238  C  CG2 . THR A 1 318 ? 65.920  33.965  84.284  1.00 42.50  ? 319 THR A CG2 1 
ATOM   2239  N  N   . TRP A 1 319 ? 64.408  38.137  84.423  1.00 43.64  ? 320 TRP A N   1 
ATOM   2240  C  CA  . TRP A 1 319 ? 63.910  39.444  84.015  1.00 28.94  ? 320 TRP A CA  1 
ATOM   2241  C  C   . TRP A 1 319 ? 64.444  40.541  84.925  1.00 36.05  ? 320 TRP A C   1 
ATOM   2242  O  O   . TRP A 1 319 ? 64.770  41.636  84.458  1.00 44.60  ? 320 TRP A O   1 
ATOM   2243  C  CB  . TRP A 1 319 ? 62.381  39.466  84.002  1.00 28.40  ? 320 TRP A CB  1 
ATOM   2244  C  CG  . TRP A 1 319 ? 61.789  38.560  82.973  1.00 33.65  ? 320 TRP A CG  1 
ATOM   2245  C  CD1 . TRP A 1 319 ? 61.136  37.384  83.194  1.00 30.89  ? 320 TRP A CD1 1 
ATOM   2246  C  CD2 . TRP A 1 319 ? 61.813  38.746  81.553  1.00 37.01  ? 320 TRP A CD2 1 
ATOM   2247  N  NE1 . TRP A 1 319 ? 60.741  36.831  82.000  1.00 27.94  ? 320 TRP A NE1 1 
ATOM   2248  C  CE2 . TRP A 1 319 ? 61.146  37.647  80.977  1.00 28.81  ? 320 TRP A CE2 1 
ATOM   2249  C  CE3 . TRP A 1 319 ? 62.330  39.738  80.713  1.00 36.72  ? 320 TRP A CE3 1 
ATOM   2250  C  CZ2 . TRP A 1 319 ? 60.980  37.511  79.599  1.00 32.80  ? 320 TRP A CZ2 1 
ATOM   2251  C  CZ3 . TRP A 1 319 ? 62.166  39.602  79.345  1.00 33.42  ? 320 TRP A CZ3 1 
ATOM   2252  C  CH2 . TRP A 1 319 ? 61.496  38.497  78.802  1.00 38.51  ? 320 TRP A CH2 1 
ATOM   2253  N  N   . LEU A 1 320 ? 64.534  40.251  86.221  1.00 29.78  ? 321 LEU A N   1 
ATOM   2254  C  CA  . LEU A 1 320 ? 65.143  41.206  87.146  1.00 29.00  ? 321 LEU A CA  1 
ATOM   2255  C  C   . LEU A 1 320 ? 66.585  41.520  86.732  1.00 38.35  ? 321 LEU A C   1 
ATOM   2256  O  O   . LEU A 1 320 ? 66.983  42.688  86.630  1.00 38.89  ? 321 LEU A O   1 
ATOM   2257  C  CB  . LEU A 1 320 ? 65.106  40.672  88.580  1.00 37.87  ? 321 LEU A CB  1 
ATOM   2258  C  CG  . LEU A 1 320 ? 63.724  40.492  89.213  1.00 36.01  ? 321 LEU A CG  1 
ATOM   2259  C  CD1 . LEU A 1 320 ? 63.852  40.002  90.648  1.00 36.11  ? 321 LEU A CD1 1 
ATOM   2260  C  CD2 . LEU A 1 320 ? 62.928  41.788  89.154  1.00 28.17  ? 321 LEU A CD2 1 
ATOM   2261  N  N   . ALA A 1 321 ? 67.353  40.465  86.477  1.00 36.94  ? 322 ALA A N   1 
ATOM   2262  C  CA  . ALA A 1 321 ? 68.743  40.591  86.057  1.00 40.33  ? 322 ALA A CA  1 
ATOM   2263  C  C   . ALA A 1 321 ? 68.866  41.372  84.752  1.00 39.65  ? 322 ALA A C   1 
ATOM   2264  O  O   . ALA A 1 321 ? 69.780  42.188  84.590  1.00 38.07  ? 322 ALA A O   1 
ATOM   2265  C  CB  . ALA A 1 321 ? 69.377  39.214  85.909  1.00 30.79  ? 322 ALA A CB  1 
ATOM   2266  N  N   . GLU A 1 322 ? 67.946  41.122  83.824  1.00 31.28  ? 323 GLU A N   1 
ATOM   2267  C  CA  . GLU A 1 322 ? 67.953  41.838  82.552  1.00 44.11  ? 323 GLU A CA  1 
ATOM   2268  C  C   . GLU A 1 322 ? 67.675  43.327  82.769  1.00 37.65  ? 323 GLU A C   1 
ATOM   2269  O  O   . GLU A 1 322 ? 68.292  44.188  82.129  1.00 36.14  ? 323 GLU A O   1 
ATOM   2270  C  CB  . GLU A 1 322 ? 66.930  41.234  81.588  1.00 49.00  ? 323 GLU A CB  1 
ATOM   2271  C  CG  . GLU A 1 322 ? 66.933  41.869  80.205  1.00 59.12  ? 323 GLU A CG  1 
ATOM   2272  C  CD  . GLU A 1 322 ? 66.295  40.982  79.154  1.00 66.44  ? 323 GLU A CD  1 
ATOM   2273  O  OE1 . GLU A 1 322 ? 66.608  39.772  79.127  1.00 70.14  ? 323 GLU A OE1 1 
ATOM   2274  O  OE2 . GLU A 1 322 ? 65.484  41.493  78.353  1.00 68.22  ? 323 GLU A OE2 1 
ATOM   2275  N  N   . ALA A 1 323 ? 66.756  43.622  83.684  1.00 35.63  ? 324 ALA A N   1 
ATOM   2276  C  CA  . ALA A 1 323 ? 66.434  45.004  84.027  1.00 38.35  ? 324 ALA A CA  1 
ATOM   2277  C  C   . ALA A 1 323 ? 67.639  45.720  84.630  1.00 46.30  ? 324 ALA A C   1 
ATOM   2278  O  O   . ALA A 1 323 ? 67.931  46.869  84.281  1.00 50.88  ? 324 ALA A O   1 
ATOM   2279  C  CB  . ALA A 1 323 ? 65.263  45.051  84.987  1.00 33.31  ? 324 ALA A CB  1 
ATOM   2280  N  N   . ILE A 1 324 ? 68.338  45.037  85.532  1.00 44.57  ? 325 ILE A N   1 
ATOM   2281  C  CA  . ILE A 1 324 ? 69.507  45.625  86.179  1.00 46.98  ? 325 ILE A CA  1 
ATOM   2282  C  C   . ILE A 1 324 ? 70.644  45.857  85.179  1.00 48.70  ? 325 ILE A C   1 
ATOM   2283  O  O   . ILE A 1 324 ? 71.259  46.930  85.170  1.00 51.80  ? 325 ILE A O   1 
ATOM   2284  C  CB  . ILE A 1 324 ? 70.000  44.747  87.344  1.00 46.50  ? 325 ILE A CB  1 
ATOM   2285  C  CG1 . ILE A 1 324 ? 68.981  44.783  88.486  1.00 48.84  ? 325 ILE A CG1 1 
ATOM   2286  C  CG2 . ILE A 1 324 ? 71.353  45.225  87.845  1.00 45.43  ? 325 ILE A CG2 1 
ATOM   2287  C  CD1 . ILE A 1 324 ? 69.373  43.955  89.689  1.00 49.04  ? 325 ILE A CD1 1 
ATOM   2288  N  N   . ASN A 1 325 ? 70.912  44.860  84.338  1.00 47.29  ? 326 ASN A N   1 
ATOM   2289  C  CA  . ASN A 1 325 ? 71.879  45.019  83.252  1.00 50.28  ? 326 ASN A CA  1 
ATOM   2290  C  C   . ASN A 1 325 ? 71.547  46.233  82.387  1.00 50.95  ? 326 ASN A C   1 
ATOM   2291  O  O   . ASN A 1 325 ? 72.418  47.066  82.087  1.00 53.20  ? 326 ASN A O   1 
ATOM   2292  C  CB  . ASN A 1 325 ? 71.928  43.761  82.382  1.00 52.07  ? 326 ASN A CB  1 
ATOM   2293  C  CG  . ASN A 1 325 ? 72.947  42.749  82.870  1.00 59.46  ? 326 ASN A CG  1 
ATOM   2294  O  OD1 . ASN A 1 325 ? 74.153  42.943  82.713  1.00 62.73  ? 326 ASN A OD1 1 
ATOM   2295  N  ND2 . ASN A 1 325 ? 72.468  41.659  83.458  1.00 57.25  ? 326 ASN A ND2 1 
ATOM   2296  N  N   . ALA A 1 326 ? 70.276  46.327  82.003  1.00 49.15  ? 327 ALA A N   1 
ATOM   2297  C  CA  . ALA A 1 326 ? 69.785  47.453  81.216  1.00 51.67  ? 327 ALA A CA  1 
ATOM   2298  C  C   . ALA A 1 326 ? 70.073  48.784  81.906  1.00 53.48  ? 327 ALA A C   1 
ATOM   2299  O  O   . ALA A 1 326 ? 70.578  49.718  81.277  1.00 52.40  ? 327 ALA A O   1 
ATOM   2300  C  CB  . ALA A 1 326 ? 68.295  47.305  80.956  1.00 48.73  ? 327 ALA A CB  1 
ATOM   2301  N  N   . LEU A 1 327 ? 69.758  48.863  83.198  1.00 52.38  ? 328 LEU A N   1 
ATOM   2302  C  CA  . LEU A 1 327 ? 70.021  50.077  83.965  1.00 53.05  ? 328 LEU A CA  1 
ATOM   2303  C  C   . LEU A 1 327 ? 71.498  50.440  83.930  1.00 58.91  ? 328 LEU A C   1 
ATOM   2304  O  O   . LEU A 1 327 ? 71.858  51.594  83.682  1.00 59.04  ? 328 LEU A O   1 
ATOM   2305  C  CB  . LEU A 1 327 ? 69.570  49.924  85.417  1.00 50.89  ? 328 LEU A CB  1 
ATOM   2306  C  CG  . LEU A 1 327 ? 69.859  51.179  86.247  1.00 53.13  ? 328 LEU A CG  1 
ATOM   2307  C  CD1 . LEU A 1 327 ? 68.869  52.289  85.915  1.00 51.60  ? 328 LEU A CD1 1 
ATOM   2308  C  CD2 . LEU A 1 327 ? 69.868  50.883  87.735  1.00 49.89  ? 328 LEU A CD2 1 
ATOM   2309  N  N   . GLN A 1 328 ? 72.347  49.447  84.182  1.00 65.05  ? 329 GLN A N   1 
ATOM   2310  C  CA  . GLN A 1 328 ? 73.791  49.651  84.146  1.00 68.22  ? 329 GLN A CA  1 
ATOM   2311  C  C   . GLN A 1 328 ? 74.256  50.227  82.818  1.00 73.45  ? 329 GLN A C   1 
ATOM   2312  O  O   . GLN A 1 328 ? 74.947  51.244  82.787  1.00 74.68  ? 329 GLN A O   1 
ATOM   2313  C  CB  . GLN A 1 328 ? 74.535  48.346  84.415  1.00 72.91  ? 329 GLN A CB  1 
ATOM   2314  C  CG  . GLN A 1 328 ? 74.887  48.112  85.869  1.00 76.16  ? 329 GLN A CG  1 
ATOM   2315  C  CD  . GLN A 1 328 ? 75.463  46.732  86.096  1.00 81.76  ? 329 GLN A CD  1 
ATOM   2316  O  OE1 . GLN A 1 328 ? 75.270  45.826  85.284  1.00 83.64  ? 329 GLN A OE1 1 
ATOM   2317  N  NE2 . GLN A 1 328 ? 76.197  46.569  87.188  1.00 84.69  ? 329 GLN A NE2 1 
ATOM   2318  N  N   . ASP A 1 329 ? 73.877  49.583  81.719  1.00 76.03  ? 330 ASP A N   1 
ATOM   2319  C  CA  . ASP A 1 329 ? 74.323  50.051  80.410  1.00 81.76  ? 330 ASP A CA  1 
ATOM   2320  C  C   . ASP A 1 329 ? 73.500  51.241  79.909  1.00 78.75  ? 330 ASP A C   1 
ATOM   2321  O  O   . ASP A 1 329 ? 73.679  51.698  78.779  1.00 82.50  ? 330 ASP A O   1 
ATOM   2322  C  CB  . ASP A 1 329 ? 74.292  48.909  79.396  1.00 90.03  ? 330 ASP A CB  1 
ATOM   2323  C  CG  . ASP A 1 329 ? 75.311  47.830  79.711  1.00 96.63  ? 330 ASP A CG  1 
ATOM   2324  O  OD1 . ASP A 1 329 ? 75.880  47.864  80.823  1.00 98.35  ? 330 ASP A OD1 1 
ATOM   2325  O  OD2 . ASP A 1 329 ? 75.557  46.961  78.848  1.00 99.61  ? 330 ASP A OD2 1 
ATOM   2326  N  N   . ASN A 1 330 ? 72.609  51.742  80.760  1.00 72.15  ? 331 ASN A N   1 
ATOM   2327  C  CA  . ASN A 1 330 ? 71.954  53.024  80.519  1.00 68.87  ? 331 ASN A CA  1 
ATOM   2328  C  C   . ASN A 1 330 ? 72.262  54.036  81.622  1.00 61.51  ? 331 ASN A C   1 
ATOM   2329  O  O   . ASN A 1 330 ? 71.566  55.039  81.762  1.00 58.49  ? 331 ASN A O   1 
ATOM   2330  C  CB  . ASN A 1 330 ? 70.440  52.847  80.388  1.00 66.57  ? 331 ASN A CB  1 
ATOM   2331  C  CG  . ASN A 1 330 ? 70.008  52.535  78.968  1.00 68.30  ? 331 ASN A CG  1 
ATOM   2332  O  OD1 . ASN A 1 330 ? 70.769  51.966  78.185  1.00 70.86  ? 331 ASN A OD1 1 
ATOM   2333  N  ND2 . ASN A 1 330 ? 68.783  52.916  78.627  1.00 67.09  ? 331 ASN A ND2 1 
ATOM   2334  N  N   . ARG A 1 331 ? 73.309  53.766  82.399  1.00 59.50  ? 332 ARG A N   1 
ATOM   2335  C  CA  . ARG A 1 331 ? 73.704  54.645  83.500  1.00 63.76  ? 332 ARG A CA  1 
ATOM   2336  C  C   . ARG A 1 331 ? 74.055  56.056  83.029  1.00 66.83  ? 332 ARG A C   1 
ATOM   2337  O  O   . ARG A 1 331 ? 73.556  57.040  83.575  1.00 66.02  ? 332 ARG A O   1 
ATOM   2338  C  CB  . ARG A 1 331 ? 74.893  54.050  84.258  1.00 59.85  ? 332 ARG A CB  1 
ATOM   2339  N  N   . ASP A 1 332 ? 74.917  56.146  82.020  1.00 71.79  ? 333 ASP A N   1 
ATOM   2340  C  CA  . ASP A 1 332 ? 75.326  57.436  81.469  1.00 78.04  ? 333 ASP A CA  1 
ATOM   2341  C  C   . ASP A 1 332 ? 74.135  58.207  80.908  1.00 83.57  ? 333 ASP A C   1 
ATOM   2342  O  O   . ASP A 1 332 ? 73.912  59.367  81.258  1.00 84.97  ? 333 ASP A O   1 
ATOM   2343  C  CB  . ASP A 1 332 ? 76.377  57.247  80.372  1.00 79.47  ? 333 ASP A CB  1 
ATOM   2344  C  CG  . ASP A 1 332 ? 77.643  56.587  80.879  1.00 80.05  ? 333 ASP A CG  1 
ATOM   2345  O  OD1 . ASP A 1 332 ? 77.956  56.734  82.079  1.00 77.49  ? 333 ASP A OD1 1 
ATOM   2346  O  OD2 . ASP A 1 332 ? 78.328  55.922  80.074  1.00 82.10  ? 333 ASP A OD2 1 
ATOM   2347  N  N   . THR A 1 333 ? 73.377  57.547  80.038  1.00 81.48  ? 334 THR A N   1 
ATOM   2348  C  CA  . THR A 1 333 ? 72.244  58.168  79.360  1.00 84.98  ? 334 THR A CA  1 
ATOM   2349  C  C   . THR A 1 333 ? 71.180  58.654  80.340  1.00 85.63  ? 334 THR A C   1 
ATOM   2350  O  O   . THR A 1 333 ? 70.728  59.796  80.251  1.00 88.34  ? 334 THR A O   1 
ATOM   2351  C  CB  . THR A 1 333 ? 71.596  57.195  78.357  1.00 84.23  ? 334 THR A CB  1 
ATOM   2352  O  OG1 . THR A 1 333 ? 72.565  56.799  77.379  1.00 85.56  ? 334 THR A OG1 1 
ATOM   2353  C  CG2 . THR A 1 333 ? 70.417  57.855  77.656  1.00 83.74  ? 334 THR A CG2 1 
ATOM   2354  N  N   . LEU A 1 334 ? 70.784  57.786  81.268  1.00 84.26  ? 335 LEU A N   1 
ATOM   2355  C  CA  . LEU A 1 334 ? 69.800  58.146  82.285  1.00 82.58  ? 335 LEU A CA  1 
ATOM   2356  C  C   . LEU A 1 334 ? 70.247  59.365  83.075  1.00 89.24  ? 335 LEU A C   1 
ATOM   2357  O  O   . LEU A 1 334 ? 69.485  60.320  83.236  1.00 91.07  ? 335 LEU A O   1 
ATOM   2358  C  CB  . LEU A 1 334 ? 69.545  56.981  83.245  1.00 78.61  ? 335 LEU A CB  1 
ATOM   2359  C  CG  . LEU A 1 334 ? 68.784  57.351  84.524  1.00 75.50  ? 335 LEU A CG  1 
ATOM   2360  C  CD1 . LEU A 1 334 ? 67.395  57.899  84.213  1.00 74.08  ? 335 LEU A CD1 1 
ATOM   2361  C  CD2 . LEU A 1 334 ? 68.695  56.168  85.478  1.00 73.11  ? 335 LEU A CD2 1 
ATOM   2362  N  N   . THR A 1 335 ? 71.482  59.329  83.565  1.00 88.34  ? 336 THR A N   1 
ATOM   2363  C  CA  . THR A 1 335 ? 72.025  60.443  84.331  1.00 89.04  ? 336 THR A CA  1 
ATOM   2364  C  C   . THR A 1 335 ? 71.655  61.920  84.213  1.00 93.09  ? 336 THR A C   1 
ATOM   2365  O  O   . THR A 1 335 ? 71.755  62.691  85.167  1.00 93.53  ? 336 THR A O   1 
ATOM   2366  C  CB  . THR A 1 335 ? 73.444  60.141  84.856  1.00 89.68  ? 336 THR A CB  1 
ATOM   2367  O  OG1 . THR A 1 335 ? 73.426  58.913  85.596  1.00 87.97  ? 336 THR A OG1 1 
ATOM   2368  C  CG2 . THR A 1 335 ? 73.927  61.260  85.773  1.00 88.14  ? 336 THR A CG2 1 
ATOM   2369  N  N   . ALA A 1 336 ? 71.264  62.302  83.002  1.00 90.73  ? 337 ALA A N   1 
ATOM   2370  C  CA  . ALA A 1 336 ? 70.691  63.608  82.726  1.00 91.57  ? 337 ALA A CA  1 
ATOM   2371  C  C   . ALA A 1 336 ? 70.050  64.503  83.773  1.00 92.29  ? 337 ALA A C   1 
ATOM   2372  O  O   . ALA A 1 336 ? 68.915  64.263  84.187  1.00 91.80  ? 337 ALA A O   1 
ATOM   2373  C  CB  . ALA A 1 336 ? 69.840  63.525  81.471  1.00 88.28  ? 337 ALA A CB  1 
ATOM   2374  N  N   . LYS A 1 337 ? 70.779  65.525  84.207  1.00 96.25  ? 338 LYS A N   1 
ATOM   2375  C  CA  . LYS A 1 337 ? 70.384  66.289  85.385  1.00 97.23  ? 338 LYS A CA  1 
ATOM   2376  C  C   . LYS A 1 337 ? 69.117  67.109  85.168  1.00 100.29 ? 338 LYS A C   1 
ATOM   2377  O  O   . LYS A 1 337 ? 68.157  66.961  85.923  1.00 105.07 ? 338 LYS A O   1 
ATOM   2378  C  CB  . LYS A 1 337 ? 71.526  67.211  85.818  1.00 98.77  ? 338 LYS A CB  1 
ATOM   2379  N  N   . VAL A 1 338 ? 69.133  67.935  84.120  1.00 96.25  ? 339 VAL A N   1 
ATOM   2380  C  CA  . VAL A 1 338 ? 68.071  68.891  83.758  1.00 92.26  ? 339 VAL A CA  1 
ATOM   2381  C  C   . VAL A 1 338 ? 66.972  69.113  84.803  1.00 90.76  ? 339 VAL A C   1 
ATOM   2382  O  O   . VAL A 1 338 ? 66.027  68.328  84.911  1.00 89.19  ? 339 VAL A O   1 
ATOM   2383  C  CB  . VAL A 1 338 ? 67.389  68.471  82.439  1.00 89.00  ? 339 VAL A CB  1 
ATOM   2384  C  CG1 . VAL A 1 338 ? 66.357  69.510  82.020  1.00 89.07  ? 339 VAL A CG1 1 
ATOM   2385  C  CG2 . VAL A 1 338 ? 68.428  68.287  81.345  1.00 88.38  ? 339 VAL A CG2 1 
ATOM   2386  N  N   . PRO A 1 365 ? 65.829  35.241  80.255  1.00 97.86  ? 366 PRO A N   1 
ATOM   2387  C  CA  . PRO A 1 365 ? 64.731  34.783  79.397  1.00 96.52  ? 366 PRO A CA  1 
ATOM   2388  C  C   . PRO A 1 365 ? 65.162  33.675  78.440  1.00 94.23  ? 366 PRO A C   1 
ATOM   2389  O  O   . PRO A 1 365 ? 65.123  33.854  77.223  1.00 95.70  ? 366 PRO A O   1 
ATOM   2390  C  CB  . PRO A 1 365 ? 64.340  36.048  78.630  1.00 97.11  ? 366 PRO A CB  1 
ATOM   2391  C  CG  . PRO A 1 365 ? 64.703  37.158  79.551  1.00 96.71  ? 366 PRO A CG  1 
ATOM   2392  C  CD  . PRO A 1 365 ? 65.949  36.709  80.261  1.00 96.79  ? 366 PRO A CD  1 
ATOM   2393  N  N   . ARG A 1 366 ? 65.568  32.540  79.000  1.00 92.08  ? 367 ARG A N   1 
ATOM   2394  C  CA  . ARG A 1 366 ? 65.970  31.385  78.206  1.00 91.62  ? 367 ARG A CA  1 
ATOM   2395  C  C   . ARG A 1 366 ? 64.773  30.820  77.447  1.00 85.90  ? 367 ARG A C   1 
ATOM   2396  O  O   . ARG A 1 366 ? 63.635  30.917  77.909  1.00 85.02  ? 367 ARG A O   1 
ATOM   2397  C  CB  . ARG A 1 366 ? 66.593  30.314  79.107  1.00 95.58  ? 367 ARG A CB  1 
ATOM   2398  C  CG  . ARG A 1 366 ? 67.077  29.067  78.382  1.00 98.88  ? 367 ARG A CG  1 
ATOM   2399  C  CD  . ARG A 1 366 ? 67.737  28.092  79.343  1.00 101.89 ? 367 ARG A CD  1 
ATOM   2400  N  NE  . ARG A 1 366 ? 68.220  26.894  78.663  1.00 104.94 ? 367 ARG A NE  1 
ATOM   2401  C  CZ  . ARG A 1 366 ? 68.989  25.971  79.233  1.00 107.24 ? 367 ARG A CZ  1 
ATOM   2402  N  NH1 . ARG A 1 366 ? 69.367  26.109  80.496  1.00 107.62 ? 367 ARG A NH1 1 
ATOM   2403  N  NH2 . ARG A 1 366 ? 69.380  24.911  78.539  1.00 108.68 ? 367 ARG A NH2 1 
ATOM   2404  N  N   . GLU A 1 367 ? 65.034  30.245  76.276  1.00 81.94  ? 368 GLU A N   1 
ATOM   2405  C  CA  . GLU A 1 367 ? 63.991  29.617  75.473  1.00 78.94  ? 368 GLU A CA  1 
ATOM   2406  C  C   . GLU A 1 367 ? 63.300  28.501  76.248  1.00 75.63  ? 368 GLU A C   1 
ATOM   2407  O  O   . GLU A 1 367 ? 63.926  27.814  77.055  1.00 75.59  ? 368 GLU A O   1 
ATOM   2408  C  CB  . GLU A 1 367 ? 64.576  29.066  74.170  1.00 77.96  ? 368 GLU A CB  1 
ATOM   2409  N  N   . ARG A 1 368 ? 62.004  28.333  76.007  1.00 74.36  ? 369 ARG A N   1 
ATOM   2410  C  CA  . ARG A 1 368 ? 61.240  27.285  76.669  1.00 72.66  ? 369 ARG A CA  1 
ATOM   2411  C  C   . ARG A 1 368 ? 61.723  25.915  76.210  1.00 68.07  ? 369 ARG A C   1 
ATOM   2412  O  O   . ARG A 1 368 ? 61.754  25.635  75.011  1.00 65.64  ? 369 ARG A O   1 
ATOM   2413  C  CB  . ARG A 1 368 ? 59.743  27.442  76.388  1.00 72.83  ? 369 ARG A CB  1 
ATOM   2414  C  CG  . ARG A 1 368 ? 58.860  26.519  77.213  1.00 71.18  ? 369 ARG A CG  1 
ATOM   2415  C  CD  . ARG A 1 368 ? 57.403  26.600  76.783  1.00 73.43  ? 369 ARG A CD  1 
ATOM   2416  N  NE  . ARG A 1 368 ? 56.933  27.978  76.672  1.00 76.04  ? 369 ARG A NE  1 
ATOM   2417  C  CZ  . ARG A 1 368 ? 56.433  28.508  75.560  1.00 78.77  ? 369 ARG A CZ  1 
ATOM   2418  N  NH1 . ARG A 1 368 ? 56.334  27.772  74.461  1.00 82.08  ? 369 ARG A NH1 1 
ATOM   2419  N  NH2 . ARG A 1 368 ? 56.030  29.771  75.546  1.00 76.44  ? 369 ARG A NH2 1 
ATOM   2420  N  N   . PRO A 1 369 ? 62.114  25.059  77.168  1.00 67.44  ? 370 PRO A N   1 
ATOM   2421  C  CA  . PRO A 1 369 ? 62.570  23.699  76.860  1.00 64.29  ? 370 PRO A CA  1 
ATOM   2422  C  C   . PRO A 1 369 ? 61.500  22.910  76.115  1.00 56.90  ? 370 PRO A C   1 
ATOM   2423  O  O   . PRO A 1 369 ? 60.314  23.192  76.297  1.00 50.08  ? 370 PRO A O   1 
ATOM   2424  C  CB  . PRO A 1 369 ? 62.836  23.093  78.243  1.00 65.37  ? 370 PRO A CB  1 
ATOM   2425  C  CG  . PRO A 1 369 ? 63.055  24.263  79.138  1.00 69.17  ? 370 PRO A CG  1 
ATOM   2426  C  CD  . PRO A 1 369 ? 62.160  25.343  78.612  1.00 65.76  ? 370 PRO A CD  1 
ATOM   2427  N  N   . PRO A 1 370 ? 61.911  21.942  75.280  1.00 54.20  ? 371 PRO A N   1 
ATOM   2428  C  CA  . PRO A 1 370 ? 60.948  21.086  74.578  1.00 57.52  ? 371 PRO A CA  1 
ATOM   2429  C  C   . PRO A 1 370 ? 60.012  20.416  75.572  1.00 60.33  ? 371 PRO A C   1 
ATOM   2430  O  O   . PRO A 1 370 ? 58.809  20.313  75.333  1.00 56.19  ? 371 PRO A O   1 
ATOM   2431  C  CB  . PRO A 1 370 ? 61.836  20.060  73.863  1.00 53.41  ? 371 PRO A CB  1 
ATOM   2432  C  CG  . PRO A 1 370 ? 63.146  20.103  74.591  1.00 57.58  ? 371 PRO A CG  1 
ATOM   2433  C  CD  . PRO A 1 370 ? 63.301  21.526  75.032  1.00 52.48  ? 371 PRO A CD  1 
ATOM   2434  N  N   . SER A 1 371 ? 60.575  19.970  76.689  1.00 71.99  ? 372 SER A N   1 
ATOM   2435  C  CA  . SER A 1 371 ? 59.777  19.477  77.797  1.00 74.19  ? 372 SER A CA  1 
ATOM   2436  C  C   . SER A 1 371 ? 60.400  19.878  79.129  1.00 72.58  ? 372 SER A C   1 
ATOM   2437  O  O   . SER A 1 371 ? 61.610  19.753  79.326  1.00 87.89  ? 372 SER A O   1 
ATOM   2438  C  CB  . SER A 1 371 ? 59.625  17.959  77.719  1.00 74.08  ? 372 SER A CB  1 
ATOM   2439  O  OG  . SER A 1 371 ? 58.902  17.472  78.833  1.00 72.65  ? 372 SER A OG  1 
ATOM   2440  N  N   . GLY A 1 372 ? 59.563  20.361  80.039  1.00 56.20  ? 373 GLY A N   1 
ATOM   2441  C  CA  . GLY A 1 372 ? 59.991  20.691  81.384  1.00 47.01  ? 373 GLY A CA  1 
ATOM   2442  C  C   . GLY A 1 372 ? 59.055  20.018  82.365  1.00 43.45  ? 373 GLY A C   1 
ATOM   2443  O  O   . GLY A 1 372 ? 58.104  19.353  81.953  1.00 42.13  ? 373 GLY A O   1 
ATOM   2444  N  N   . THR A 1 373 ? 59.317  20.184  83.657  1.00 28.48  ? 374 THR A N   1 
ATOM   2445  C  CA  . THR A 1 373 ? 58.476  19.580  84.684  1.00 28.00  ? 374 THR A CA  1 
ATOM   2446  C  C   . THR A 1 373 ? 57.032  20.063  84.571  1.00 38.54  ? 374 THR A C   1 
ATOM   2447  O  O   . THR A 1 373 ? 56.095  19.260  84.583  1.00 38.77  ? 374 THR A O   1 
ATOM   2448  C  CB  . THR A 1 373 ? 59.003  19.887  86.095  1.00 27.87  ? 374 THR A CB  1 
ATOM   2449  O  OG1 . THR A 1 373 ? 60.342  19.394  86.223  1.00 39.09  ? 374 THR A OG1 1 
ATOM   2450  C  CG2 . THR A 1 373 ? 58.123  19.226  87.146  1.00 29.52  ? 374 THR A CG2 1 
ATOM   2451  N  N   . LEU A 1 374 ? 56.864  21.377  84.444  1.00 26.42  ? 375 LEU A N   1 
ATOM   2452  C  CA  . LEU A 1 374 ? 55.539  21.982  84.360  1.00 34.85  ? 375 LEU A CA  1 
ATOM   2453  C  C   . LEU A 1 374 ? 54.755  21.463  83.160  1.00 25.77  ? 375 LEU A C   1 
ATOM   2454  O  O   . LEU A 1 374 ? 53.557  21.212  83.257  1.00 40.92  ? 375 LEU A O   1 
ATOM   2455  C  CB  . LEU A 1 374 ? 55.649  23.507  84.290  1.00 35.91  ? 375 LEU A CB  1 
ATOM   2456  C  CG  . LEU A 1 374 ? 54.324  24.270  84.227  1.00 34.67  ? 375 LEU A CG  1 
ATOM   2457  C  CD1 . LEU A 1 374 ? 53.461  23.955  85.439  1.00 24.08  ? 375 LEU A CD1 1 
ATOM   2458  C  CD2 . LEU A 1 374 ? 54.567  25.769  84.110  1.00 37.28  ? 375 LEU A CD2 1 
ATOM   2459  N  N   . GLU A 1 375 ? 55.438  21.294  82.033  1.00 26.51  ? 376 GLU A N   1 
ATOM   2460  C  CA  . GLU A 1 375 ? 54.791  20.837  80.808  1.00 41.16  ? 376 GLU A CA  1 
ATOM   2461  C  C   . GLU A 1 375 ? 54.332  19.382  80.918  1.00 37.15  ? 376 GLU A C   1 
ATOM   2462  O  O   . GLU A 1 375 ? 53.229  19.035  80.488  1.00 35.48  ? 376 GLU A O   1 
ATOM   2463  C  CB  . GLU A 1 375 ? 55.736  21.009  79.617  1.00 39.64  ? 376 GLU A CB  1 
ATOM   2464  C  CG  . GLU A 1 375 ? 55.104  20.707  78.269  1.00 47.65  ? 376 GLU A CG  1 
ATOM   2465  C  CD  . GLU A 1 375 ? 55.955  21.190  77.110  1.00 53.53  ? 376 GLU A CD  1 
ATOM   2466  O  OE1 . GLU A 1 375 ? 56.770  22.114  77.316  1.00 54.56  ? 376 GLU A OE1 1 
ATOM   2467  O  OE2 . GLU A 1 375 ? 55.810  20.649  75.994  1.00 53.53  ? 376 GLU A OE2 1 
ATOM   2468  N  N   . LYS A 1 376 ? 55.177  18.535  81.497  1.00 27.72  ? 377 LYS A N   1 
ATOM   2469  C  CA  . LYS A 1 376 ? 54.821  17.137  81.712  1.00 32.19  ? 377 LYS A CA  1 
ATOM   2470  C  C   . LYS A 1 376 ? 53.642  17.034  82.671  1.00 33.62  ? 377 LYS A C   1 
ATOM   2471  O  O   . LYS A 1 376 ? 52.697  16.263  82.444  1.00 35.86  ? 377 LYS A O   1 
ATOM   2472  C  CB  . LYS A 1 376 ? 56.013  16.349  82.257  1.00 33.45  ? 377 LYS A CB  1 
ATOM   2473  C  CG  . LYS A 1 376 ? 57.193  16.259  81.307  1.00 34.57  ? 377 LYS A CG  1 
ATOM   2474  C  CD  . LYS A 1 376 ? 58.203  15.235  81.799  1.00 31.23  ? 377 LYS A CD  1 
ATOM   2475  C  CE  . LYS A 1 376 ? 59.472  15.258  80.968  1.00 34.80  ? 377 LYS A CE  1 
ATOM   2476  N  NZ  . LYS A 1 376 ? 59.172  15.138  79.514  1.00 33.16  ? 377 LYS A NZ  1 
ATOM   2477  N  N   . LEU A 1 377 ? 53.709  17.819  83.744  1.00 26.62  ? 378 LEU A N   1 
ATOM   2478  C  CA  . LEU A 1 377 ? 52.627  17.882  84.717  1.00 36.40  ? 378 LEU A CA  1 
ATOM   2479  C  C   . LEU A 1 377 ? 51.325  18.304  84.049  1.00 36.69  ? 378 LEU A C   1 
ATOM   2480  O  O   . LEU A 1 377 ? 50.264  17.762  84.349  1.00 32.65  ? 378 LEU A O   1 
ATOM   2481  C  CB  . LEU A 1 377 ? 52.972  18.850  85.848  1.00 34.84  ? 378 LEU A CB  1 
ATOM   2482  C  CG  . LEU A 1 377 ? 53.979  18.356  86.886  1.00 38.11  ? 378 LEU A CG  1 
ATOM   2483  C  CD1 . LEU A 1 377 ? 54.295  19.462  87.879  1.00 37.80  ? 378 LEU A CD1 1 
ATOM   2484  C  CD2 . LEU A 1 377 ? 53.450  17.122  87.599  1.00 33.99  ? 378 LEU A CD2 1 
ATOM   2485  N  N   . VAL A 1 378 ? 51.416  19.264  83.135  1.00 25.24  ? 379 VAL A N   1 
ATOM   2486  C  CA  . VAL A 1 378 ? 50.241  19.755  82.425  1.00 34.71  ? 379 VAL A CA  1 
ATOM   2487  C  C   . VAL A 1 378 ? 49.672  18.690  81.487  1.00 42.57  ? 379 VAL A C   1 
ATOM   2488  O  O   . VAL A 1 378 ? 48.458  18.519  81.409  1.00 40.10  ? 379 VAL A O   1 
ATOM   2489  C  CB  . VAL A 1 378 ? 50.561  21.046  81.633  1.00 30.75  ? 379 VAL A CB  1 
ATOM   2490  C  CG1 . VAL A 1 378 ? 49.542  21.281  80.529  1.00 24.96  ? 379 VAL A CG1 1 
ATOM   2491  C  CG2 . VAL A 1 378 ? 50.604  22.238  82.575  1.00 24.29  ? 379 VAL A CG2 1 
ATOM   2492  N  N   . SER A 1 379 ? 50.544  17.965  80.791  1.00 33.39  ? 380 SER A N   1 
ATOM   2493  C  CA  . SER A 1 379 ? 50.096  16.877  79.921  1.00 39.51  ? 380 SER A CA  1 
ATOM   2494  C  C   . SER A 1 379 ? 49.360  15.800  80.717  1.00 35.60  ? 380 SER A C   1 
ATOM   2495  O  O   . SER A 1 379 ? 48.233  15.410  80.376  1.00 31.98  ? 380 SER A O   1 
ATOM   2496  C  CB  . SER A 1 379 ? 51.280  16.256  79.176  1.00 44.12  ? 380 SER A CB  1 
ATOM   2497  O  OG  . SER A 1 379 ? 51.697  17.078  78.100  1.00 53.83  ? 380 SER A OG  1 
ATOM   2498  N  N   . GLU A 1 380 ? 50.004  15.327  81.781  1.00 40.58  ? 381 GLU A N   1 
ATOM   2499  C  CA  . GLU A 1 380 ? 49.408  14.313  82.645  1.00 40.98  ? 381 GLU A CA  1 
ATOM   2500  C  C   . GLU A 1 380 ? 48.070  14.783  83.218  1.00 36.01  ? 381 GLU A C   1 
ATOM   2501  O  O   . GLU A 1 380 ? 47.087  14.038  83.221  1.00 30.20  ? 381 GLU A O   1 
ATOM   2502  C  CB  . GLU A 1 380 ? 50.371  13.947  83.778  1.00 40.71  ? 381 GLU A CB  1 
ATOM   2503  C  CG  . GLU A 1 380 ? 49.733  13.183  84.930  1.00 51.58  ? 381 GLU A CG  1 
ATOM   2504  C  CD  . GLU A 1 380 ? 49.319  11.773  84.550  1.00 58.88  ? 381 GLU A CD  1 
ATOM   2505  O  OE1 . GLU A 1 380 ? 49.760  11.282  83.490  1.00 62.42  ? 381 GLU A OE1 1 
ATOM   2506  O  OE2 . GLU A 1 380 ? 48.552  11.154  85.317  1.00 63.65  ? 381 GLU A OE2 1 
ATOM   2507  N  N   . ALA A 1 381 ? 48.040  16.027  83.685  1.00 33.37  ? 382 ALA A N   1 
ATOM   2508  C  CA  . ALA A 1 381 ? 46.839  16.598  84.284  1.00 30.38  ? 382 ALA A CA  1 
ATOM   2509  C  C   . ALA A 1 381 ? 45.698  16.703  83.278  1.00 30.02  ? 382 ALA A C   1 
ATOM   2510  O  O   . ALA A 1 381 ? 44.553  16.399  83.601  1.00 30.85  ? 382 ALA A O   1 
ATOM   2511  C  CB  . ALA A 1 381 ? 47.143  17.962  84.878  1.00 24.10  ? 382 ALA A CB  1 
ATOM   2512  N  N   . LYS A 1 382 ? 46.011  17.135  82.060  1.00 36.39  ? 383 LYS A N   1 
ATOM   2513  C  CA  . LYS A 1 382 ? 45.001  17.240  81.015  1.00 24.84  ? 383 LYS A CA  1 
ATOM   2514  C  C   . LYS A 1 382 ? 44.477  15.862  80.637  1.00 40.39  ? 383 LYS A C   1 
ATOM   2515  O  O   . LYS A 1 382 ? 43.285  15.699  80.369  1.00 38.93  ? 383 LYS A O   1 
ATOM   2516  C  CB  . LYS A 1 382 ? 45.557  17.961  79.785  1.00 31.35  ? 383 LYS A CB  1 
ATOM   2517  C  CG  . LYS A 1 382 ? 45.769  19.453  80.006  1.00 41.10  ? 383 LYS A CG  1 
ATOM   2518  C  CD  . LYS A 1 382 ? 45.761  20.236  78.702  1.00 40.55  ? 383 LYS A CD  1 
ATOM   2519  C  CE  . LYS A 1 382 ? 47.027  20.010  77.899  1.00 41.77  ? 383 LYS A CE  1 
ATOM   2520  N  NZ  . LYS A 1 382 ? 47.148  21.006  76.797  1.00 38.64  ? 383 LYS A NZ  1 
ATOM   2521  N  N   . ALA A 1 383 ? 45.362  14.868  80.626  1.00 37.34  ? 384 ALA A N   1 
ATOM   2522  C  CA  . ALA A 1 383 ? 44.931  13.493  80.390  1.00 35.63  ? 384 ALA A CA  1 
ATOM   2523  C  C   . ALA A 1 383 ? 43.944  13.043  81.466  1.00 33.22  ? 384 ALA A C   1 
ATOM   2524  O  O   . ALA A 1 383 ? 42.840  12.576  81.160  1.00 33.09  ? 384 ALA A O   1 
ATOM   2525  C  CB  . ALA A 1 383 ? 46.129  12.557  80.342  1.00 27.42  ? 384 ALA A CB  1 
ATOM   2526  N  N   . GLN A 1 384 ? 44.340  13.202  82.726  1.00 25.87  ? 385 GLN A N   1 
ATOM   2527  C  CA  . GLN A 1 384 ? 43.513  12.776  83.852  1.00 25.69  ? 385 GLN A CA  1 
ATOM   2528  C  C   . GLN A 1 384 ? 42.177  13.516  83.929  1.00 33.69  ? 385 GLN A C   1 
ATOM   2529  O  O   . GLN A 1 384 ? 41.177  12.952  84.371  1.00 41.43  ? 385 GLN A O   1 
ATOM   2530  C  CB  . GLN A 1 384 ? 44.273  12.954  85.168  1.00 34.06  ? 385 GLN A CB  1 
ATOM   2531  C  CG  . GLN A 1 384 ? 45.336  11.895  85.428  1.00 46.58  ? 385 GLN A CG  1 
ATOM   2532  C  CD  . GLN A 1 384 ? 44.751  10.520  85.712  1.00 62.80  ? 385 GLN A CD  1 
ATOM   2533  O  OE1 . GLN A 1 384 ? 43.536  10.356  85.834  1.00 64.37  ? 385 GLN A OE1 1 
ATOM   2534  N  NE2 . GLN A 1 384 ? 45.621  9.522   85.821  1.00 66.56  ? 385 GLN A NE2 1 
ATOM   2535  N  N   . LEU A 1 385 ? 42.162  14.774  83.502  1.00 31.01  ? 386 LEU A N   1 
ATOM   2536  C  CA  . LEU A 1 385 ? 40.949  15.583  83.563  1.00 36.08  ? 386 LEU A CA  1 
ATOM   2537  C  C   . LEU A 1 385 ? 40.015  15.268  82.402  1.00 32.68  ? 386 LEU A C   1 
ATOM   2538  O  O   . LEU A 1 385 ? 38.797  15.239  82.573  1.00 34.67  ? 386 LEU A O   1 
ATOM   2539  C  CB  . LEU A 1 385 ? 41.292  17.073  83.579  1.00 26.31  ? 386 LEU A CB  1 
ATOM   2540  C  CG  . LEU A 1 385 ? 41.875  17.588  84.897  1.00 27.59  ? 386 LEU A CG  1 
ATOM   2541  C  CD1 . LEU A 1 385 ? 41.979  19.104  84.892  1.00 24.98  ? 386 LEU A CD1 1 
ATOM   2542  C  CD2 . LEU A 1 385 ? 41.044  17.104  86.078  1.00 30.51  ? 386 LEU A CD2 1 
ATOM   2543  N  N   . ARG A 1 386 ? 40.583  15.033  81.223  1.00 34.25  ? 387 ARG A N   1 
ATOM   2544  C  CA  . ARG A 1 386 ? 39.783  14.590  80.088  1.00 38.48  ? 387 ARG A CA  1 
ATOM   2545  C  C   . ARG A 1 386 ? 39.224  13.200  80.361  1.00 39.86  ? 387 ARG A C   1 
ATOM   2546  O  O   . ARG A 1 386 ? 38.181  12.825  79.827  1.00 34.11  ? 387 ARG A O   1 
ATOM   2547  C  CB  . ARG A 1 386 ? 40.605  14.580  78.797  1.00 39.56  ? 387 ARG A CB  1 
ATOM   2548  C  CG  . ARG A 1 386 ? 40.946  15.957  78.253  1.00 47.59  ? 387 ARG A CG  1 
ATOM   2549  C  CD  . ARG A 1 386 ? 41.677  15.852  76.922  1.00 59.60  ? 387 ARG A CD  1 
ATOM   2550  N  NE  . ARG A 1 386 ? 42.781  16.804  76.821  1.00 65.38  ? 387 ARG A NE  1 
ATOM   2551  C  CZ  . ARG A 1 386 ? 42.689  18.002  76.254  1.00 68.30  ? 387 ARG A CZ  1 
ATOM   2552  N  NH1 . ARG A 1 386 ? 41.539  18.406  75.733  1.00 71.40  ? 387 ARG A NH1 1 
ATOM   2553  N  NH2 . ARG A 1 386 ? 43.748  18.799  76.209  1.00 73.08  ? 387 ARG A NH2 1 
ATOM   2554  N  N   . ASP A 1 387 ? 39.922  12.442  81.202  1.00 40.63  ? 388 ASP A N   1 
ATOM   2555  C  CA  . ASP A 1 387 ? 39.510  11.077  81.515  1.00 35.58  ? 388 ASP A CA  1 
ATOM   2556  C  C   . ASP A 1 387 ? 38.325  11.004  82.483  1.00 34.11  ? 388 ASP A C   1 
ATOM   2557  O  O   . ASP A 1 387 ? 37.548  10.049  82.446  1.00 38.98  ? 388 ASP A O   1 
ATOM   2558  C  CB  . ASP A 1 387 ? 40.688  10.295  82.094  1.00 41.38  ? 388 ASP A CB  1 
ATOM   2559  C  CG  . ASP A 1 387 ? 40.357  8.835   82.325  1.00 51.09  ? 388 ASP A CG  1 
ATOM   2560  O  OD1 . ASP A 1 387 ? 39.865  8.182   81.381  1.00 52.35  ? 388 ASP A OD1 1 
ATOM   2561  O  OD2 . ASP A 1 387 ? 40.584  8.344   83.450  1.00 55.00  ? 388 ASP A OD2 1 
ATOM   2562  N  N   . VAL A 1 388 ? 38.184  12.007  83.345  1.00 32.02  ? 389 VAL A N   1 
ATOM   2563  C  CA  . VAL A 1 388 ? 37.152  11.968  84.379  1.00 34.37  ? 389 VAL A CA  1 
ATOM   2564  C  C   . VAL A 1 388 ? 36.066  13.032  84.200  1.00 33.06  ? 389 VAL A C   1 
ATOM   2565  O  O   . VAL A 1 388 ? 35.299  13.302  85.125  1.00 33.35  ? 389 VAL A O   1 
ATOM   2566  C  CB  . VAL A 1 388 ? 37.765  12.132  85.786  1.00 25.20  ? 389 VAL A CB  1 
ATOM   2567  C  CG1 . VAL A 1 388 ? 38.770  11.023  86.060  1.00 25.76  ? 389 VAL A CG1 1 
ATOM   2568  C  CG2 . VAL A 1 388 ? 38.414  13.505  85.933  1.00 24.64  ? 389 VAL A CG2 1 
ATOM   2569  N  N   . GLN A 1 389 ? 35.992  13.628  83.014  1.00 24.90  ? 390 GLN A N   1 
ATOM   2570  C  CA  . GLN A 1 389 ? 34.965  14.628  82.743  1.00 29.83  ? 390 GLN A CA  1 
ATOM   2571  C  C   . GLN A 1 389 ? 33.591  13.973  82.614  1.00 25.16  ? 390 GLN A C   1 
ATOM   2572  O  O   . GLN A 1 389 ? 32.564  14.635  82.762  1.00 25.09  ? 390 GLN A O   1 
ATOM   2573  C  CB  . GLN A 1 389 ? 35.293  15.418  81.474  1.00 30.95  ? 390 GLN A CB  1 
ATOM   2574  C  CG  . GLN A 1 389 ? 35.554  14.557  80.253  1.00 39.07  ? 390 GLN A CG  1 
ATOM   2575  C  CD  . GLN A 1 389 ? 35.895  15.376  79.024  1.00 44.35  ? 390 GLN A CD  1 
ATOM   2576  O  OE1 . GLN A 1 389 ? 35.731  16.595  79.012  1.00 56.29  ? 390 GLN A OE1 1 
ATOM   2577  N  NE2 . GLN A 1 389 ? 36.372  14.708  77.982  1.00 53.58  ? 390 GLN A NE2 1 
ATOM   2578  N  N   . ASP A 1 390 ? 33.584  12.670  82.344  1.00 25.52  ? 391 ASP A N   1 
ATOM   2579  C  CA  . ASP A 1 390 ? 32.344  11.925  82.145  1.00 25.95  ? 391 ASP A CA  1 
ATOM   2580  C  C   . ASP A 1 390 ? 31.874  11.227  83.414  1.00 26.09  ? 391 ASP A C   1 
ATOM   2581  O  O   . ASP A 1 390 ? 30.898  10.481  83.390  1.00 26.51  ? 391 ASP A O   1 
ATOM   2582  C  CB  . ASP A 1 390 ? 32.517  10.886  81.030  1.00 39.98  ? 391 ASP A CB  1 
ATOM   2583  C  CG  . ASP A 1 390 ? 33.649  9.894   81.310  1.00 42.32  ? 391 ASP A CG  1 
ATOM   2584  O  OD1 . ASP A 1 390 ? 34.195  9.879   82.435  1.00 38.61  ? 391 ASP A OD1 1 
ATOM   2585  O  OD2 . ASP A 1 390 ? 33.989  9.112   80.397  1.00 47.67  ? 391 ASP A OD2 1 
ATOM   2586  N  N   . PHE A 1 391 ? 32.582  11.472  84.512  1.00 25.82  ? 392 PHE A N   1 
ATOM   2587  C  CA  . PHE A 1 391 ? 32.426  10.712  85.753  1.00 37.19  ? 392 PHE A CA  1 
ATOM   2588  C  C   . PHE A 1 391 ? 30.975  10.524  86.204  1.00 33.92  ? 392 PHE A C   1 
ATOM   2589  O  O   . PHE A 1 391 ? 30.482  9.391   86.332  1.00 41.09  ? 392 PHE A O   1 
ATOM   2590  C  CB  . PHE A 1 391 ? 33.222  11.400  86.867  1.00 25.81  ? 392 PHE A CB  1 
ATOM   2591  C  CG  . PHE A 1 391 ? 33.264  10.625  88.150  1.00 33.16  ? 392 PHE A CG  1 
ATOM   2592  C  CD1 . PHE A 1 391 ? 34.019  9.467   88.247  1.00 36.22  ? 392 PHE A CD1 1 
ATOM   2593  C  CD2 . PHE A 1 391 ? 32.557  11.054  89.261  1.00 26.42  ? 392 PHE A CD2 1 
ATOM   2594  C  CE1 . PHE A 1 391 ? 34.065  8.748   89.427  1.00 27.35  ? 392 PHE A CE1 1 
ATOM   2595  C  CE2 . PHE A 1 391 ? 32.599  10.340  90.444  1.00 29.20  ? 392 PHE A CE2 1 
ATOM   2596  C  CZ  . PHE A 1 391 ? 33.355  9.185   90.527  1.00 30.07  ? 392 PHE A CZ  1 
ATOM   2597  N  N   . TRP A 1 392 ? 30.296  11.647  86.414  1.00 27.98  ? 393 TRP A N   1 
ATOM   2598  C  CA  . TRP A 1 392 ? 28.985  11.673  87.050  1.00 27.86  ? 393 TRP A CA  1 
ATOM   2599  C  C   . TRP A 1 392 ? 27.895  10.965  86.251  1.00 27.06  ? 393 TRP A C   1 
ATOM   2600  O  O   . TRP A 1 392 ? 26.866  10.585  86.806  1.00 30.56  ? 393 TRP A O   1 
ATOM   2601  C  CB  . TRP A 1 392 ? 28.581  13.123  87.318  1.00 26.40  ? 393 TRP A CB  1 
ATOM   2602  C  CG  . TRP A 1 392 ? 29.584  13.827  88.165  1.00 33.11  ? 393 TRP A CG  1 
ATOM   2603  C  CD1 . TRP A 1 392 ? 30.428  14.828  87.781  1.00 36.78  ? 393 TRP A CD1 1 
ATOM   2604  C  CD2 . TRP A 1 392 ? 29.880  13.556  89.539  1.00 35.33  ? 393 TRP A CD2 1 
ATOM   2605  N  NE1 . TRP A 1 392 ? 31.221  15.208  88.837  1.00 31.21  ? 393 TRP A NE1 1 
ATOM   2606  C  CE2 . TRP A 1 392 ? 30.905  14.441  89.928  1.00 33.97  ? 393 TRP A CE2 1 
ATOM   2607  C  CE3 . TRP A 1 392 ? 29.373  12.655  90.480  1.00 28.84  ? 393 TRP A CE3 1 
ATOM   2608  C  CZ2 . TRP A 1 392 ? 31.431  14.453  91.217  1.00 32.82  ? 393 TRP A CZ2 1 
ATOM   2609  C  CZ3 . TRP A 1 392 ? 29.896  12.667  91.758  1.00 30.21  ? 393 TRP A CZ3 1 
ATOM   2610  C  CH2 . TRP A 1 392 ? 30.915  13.560  92.116  1.00 36.17  ? 393 TRP A CH2 1 
ATOM   2611  N  N   . ILE A 1 393 ? 28.118  10.785  84.954  1.00 26.98  ? 394 ILE A N   1 
ATOM   2612  C  CA  . ILE A 1 393 ? 27.167  10.048  84.133  1.00 27.59  ? 394 ILE A CA  1 
ATOM   2613  C  C   . ILE A 1 393 ? 27.717  8.680   83.743  1.00 36.88  ? 394 ILE A C   1 
ATOM   2614  O  O   . ILE A 1 393 ? 26.976  7.815   83.280  1.00 40.04  ? 394 ILE A O   1 
ATOM   2615  C  CB  . ILE A 1 393 ? 26.795  10.816  82.857  1.00 27.45  ? 394 ILE A CB  1 
ATOM   2616  C  CG1 . ILE A 1 393 ? 27.991  10.883  81.910  1.00 27.20  ? 394 ILE A CG1 1 
ATOM   2617  C  CG2 . ILE A 1 393 ? 26.282  12.208  83.200  1.00 41.79  ? 394 ILE A CG2 1 
ATOM   2618  C  CD1 . ILE A 1 393 ? 27.618  11.275  80.514  1.00 27.46  ? 394 ILE A CD1 1 
ATOM   2619  N  N   . SER A 1 394 ? 29.019  8.487   83.927  1.00 39.50  ? 395 SER A N   1 
ATOM   2620  C  CA  . SER A 1 394 ? 29.631  7.204   83.616  1.00 40.49  ? 395 SER A CA  1 
ATOM   2621  C  C   . SER A 1 394 ? 29.520  6.263   84.808  1.00 33.32  ? 395 SER A C   1 
ATOM   2622  O  O   . SER A 1 394 ? 29.787  5.069   84.682  1.00 29.22  ? 395 SER A O   1 
ATOM   2623  C  CB  . SER A 1 394 ? 31.097  7.374   83.217  1.00 39.15  ? 395 SER A CB  1 
ATOM   2624  O  OG  . SER A 1 394 ? 31.902  7.645   84.350  1.00 42.86  ? 395 SER A OG  1 
ATOM   2625  N  N   . LEU A 1 395 ? 29.135  6.807   85.961  1.00 28.42  ? 396 LEU A N   1 
ATOM   2626  C  CA  . LEU A 1 395 ? 28.944  5.991   87.167  1.00 41.07  ? 396 LEU A CA  1 
ATOM   2627  C  C   . LEU A 1 395 ? 28.110  4.709   86.960  1.00 45.72  ? 396 LEU A C   1 
ATOM   2628  O  O   . LEU A 1 395 ? 28.570  3.622   87.321  1.00 48.45  ? 396 LEU A O   1 
ATOM   2629  C  CB  . LEU A 1 395 ? 28.312  6.832   88.283  1.00 40.90  ? 396 LEU A CB  1 
ATOM   2630  C  CG  . LEU A 1 395 ? 29.246  7.699   89.124  1.00 43.52  ? 396 LEU A CG  1 
ATOM   2631  C  CD1 . LEU A 1 395 ? 28.473  8.364   90.252  1.00 45.21  ? 396 LEU A CD1 1 
ATOM   2632  C  CD2 . LEU A 1 395 ? 30.390  6.865   89.672  1.00 46.91  ? 396 LEU A CD2 1 
ATOM   2633  N  N   . PRO A 1 396 ? 26.893  4.818   86.381  1.00 42.35  ? 397 PRO A N   1 
ATOM   2634  C  CA  . PRO A 1 396 ? 26.100  3.587   86.261  1.00 43.97  ? 397 PRO A CA  1 
ATOM   2635  C  C   . PRO A 1 396 ? 26.744  2.552   85.343  1.00 42.69  ? 397 PRO A C   1 
ATOM   2636  O  O   . PRO A 1 396 ? 26.761  1.368   85.673  1.00 45.54  ? 397 PRO A O   1 
ATOM   2637  C  CB  . PRO A 1 396 ? 24.771  4.076   85.667  1.00 41.33  ? 397 PRO A CB  1 
ATOM   2638  C  CG  . PRO A 1 396 ? 24.745  5.546   85.919  1.00 39.12  ? 397 PRO A CG  1 
ATOM   2639  C  CD  . PRO A 1 396 ? 26.169  5.975   85.827  1.00 40.41  ? 397 PRO A CD  1 
ATOM   2640  N  N   . GLY A 1 397 ? 27.268  3.006   84.209  1.00 41.34  ? 398 GLY A N   1 
ATOM   2641  C  CA  . GLY A 1 397 ? 27.901  2.123   83.247  1.00 31.34  ? 398 GLY A CA  1 
ATOM   2642  C  C   . GLY A 1 397 ? 29.077  1.358   83.822  1.00 42.66  ? 398 GLY A C   1 
ATOM   2643  O  O   . GLY A 1 397 ? 29.191  0.148   83.632  1.00 40.60  ? 398 GLY A O   1 
ATOM   2644  N  N   . THR A 1 398 ? 29.950  2.061   84.536  1.00 45.11  ? 399 THR A N   1 
ATOM   2645  C  CA  . THR A 1 398 ? 31.140  1.439   85.106  1.00 46.83  ? 399 THR A CA  1 
ATOM   2646  C  C   . THR A 1 398 ? 30.799  0.560   86.305  1.00 46.88  ? 399 THR A C   1 
ATOM   2647  O  O   . THR A 1 398 ? 31.350  -0.532  86.454  1.00 47.30  ? 399 THR A O   1 
ATOM   2648  C  CB  . THR A 1 398 ? 32.182  2.492   85.533  1.00 44.09  ? 399 THR A CB  1 
ATOM   2649  O  OG1 . THR A 1 398 ? 31.677  3.252   86.638  1.00 51.24  ? 399 THR A OG1 1 
ATOM   2650  C  CG2 . THR A 1 398 ? 32.507  3.424   84.375  1.00 42.15  ? 399 THR A CG2 1 
ATOM   2651  N  N   . LEU A 1 399 ? 29.893  1.032   87.157  1.00 42.74  ? 400 LEU A N   1 
ATOM   2652  C  CA  . LEU A 1 399 ? 29.486  0.253   88.323  1.00 46.06  ? 400 LEU A CA  1 
ATOM   2653  C  C   . LEU A 1 399 ? 28.790  -1.040  87.910  1.00 41.96  ? 400 LEU A C   1 
ATOM   2654  O  O   . LEU A 1 399 ? 28.949  -2.072  88.560  1.00 41.68  ? 400 LEU A O   1 
ATOM   2655  C  CB  . LEU A 1 399 ? 28.572  1.072   89.235  1.00 44.87  ? 400 LEU A CB  1 
ATOM   2656  C  CG  . LEU A 1 399 ? 29.277  2.058   90.166  1.00 47.06  ? 400 LEU A CG  1 
ATOM   2657  C  CD1 . LEU A 1 399 ? 28.271  2.797   91.036  1.00 43.81  ? 400 LEU A CD1 1 
ATOM   2658  C  CD2 . LEU A 1 399 ? 30.305  1.335   91.021  1.00 46.58  ? 400 LEU A CD2 1 
ATOM   2659  N  N   . CYS A 1 400 ? 28.021  -0.978  86.828  1.00 44.11  ? 401 CYS A N   1 
ATOM   2660  C  CA  . CYS A 1 400 ? 27.357  -2.162  86.297  1.00 48.14  ? 401 CYS A CA  1 
ATOM   2661  C  C   . CYS A 1 400 ? 28.354  -3.090  85.616  1.00 54.19  ? 401 CYS A C   1 
ATOM   2662  O  O   . CYS A 1 400 ? 28.323  -4.305  85.818  1.00 53.05  ? 401 CYS A O   1 
ATOM   2663  C  CB  . CYS A 1 400 ? 26.258  -1.767  85.309  1.00 50.81  ? 401 CYS A CB  1 
ATOM   2664  S  SG  . CYS A 1 400 ? 24.755  -1.135  86.078  1.00 51.31  ? 401 CYS A SG  1 
ATOM   2665  N  N   . SER A 1 401 ? 29.235  -2.508  84.809  1.00 54.97  ? 402 SER A N   1 
ATOM   2666  C  CA  . SER A 1 401 ? 30.212  -3.282  84.051  1.00 58.83  ? 402 SER A CA  1 
ATOM   2667  C  C   . SER A 1 401 ? 31.183  -4.031  84.956  1.00 67.78  ? 402 SER A C   1 
ATOM   2668  O  O   . SER A 1 401 ? 31.575  -5.160  84.657  1.00 70.15  ? 402 SER A O   1 
ATOM   2669  C  CB  . SER A 1 401 ? 30.992  -2.370  83.101  1.00 58.51  ? 402 SER A CB  1 
ATOM   2670  O  OG  . SER A 1 401 ? 32.030  -3.079  82.448  1.00 61.56  ? 402 SER A OG  1 
ATOM   2671  N  N   . GLU A 1 402 ? 31.562  -3.405  86.064  1.00 68.42  ? 403 GLU A N   1 
ATOM   2672  C  CA  . GLU A 1 402 ? 32.587  -3.970  86.935  1.00 75.24  ? 403 GLU A CA  1 
ATOM   2673  C  C   . GLU A 1 402 ? 32.054  -5.013  87.916  1.00 81.21  ? 403 GLU A C   1 
ATOM   2674  O  O   . GLU A 1 402 ? 32.673  -6.060  88.109  1.00 84.39  ? 403 GLU A O   1 
ATOM   2675  C  CB  . GLU A 1 402 ? 33.289  -2.853  87.711  1.00 74.26  ? 403 GLU A CB  1 
ATOM   2676  C  CG  . GLU A 1 402 ? 34.292  -2.063  86.885  1.00 77.43  ? 403 GLU A CG  1 
ATOM   2677  C  CD  . GLU A 1 402 ? 34.973  -0.965  87.682  1.00 81.29  ? 403 GLU A CD  1 
ATOM   2678  O  OE1 . GLU A 1 402 ? 34.477  -0.627  88.778  1.00 82.30  ? 403 GLU A OE1 1 
ATOM   2679  O  OE2 . GLU A 1 402 ? 36.006  -0.442  87.212  1.00 81.01  ? 403 GLU A OE2 1 
ATOM   2680  N  N   . LYS A 1 403 ? 30.908  -4.737  88.530  1.00 79.33  ? 404 LYS A N   1 
ATOM   2681  C  CA  . LYS A 1 403 ? 30.459  -5.546  89.659  1.00 81.26  ? 404 LYS A CA  1 
ATOM   2682  C  C   . LYS A 1 403 ? 29.203  -6.373  89.391  1.00 80.94  ? 404 LYS A C   1 
ATOM   2683  O  O   . LYS A 1 403 ? 29.257  -7.601  89.318  1.00 80.79  ? 404 LYS A O   1 
ATOM   2684  C  CB  . LYS A 1 403 ? 30.214  -4.644  90.871  1.00 81.38  ? 404 LYS A CB  1 
ATOM   2685  C  CG  . LYS A 1 403 ? 31.271  -3.568  91.067  1.00 82.91  ? 404 LYS A CG  1 
ATOM   2686  C  CD  . LYS A 1 403 ? 31.705  -3.468  92.519  1.00 86.28  ? 404 LYS A CD  1 
ATOM   2687  C  CE  . LYS A 1 403 ? 32.734  -2.364  92.708  1.00 86.30  ? 404 LYS A CE  1 
ATOM   2688  N  NZ  . LYS A 1 403 ? 33.379  -1.975  91.423  1.00 86.39  ? 404 LYS A NZ  1 
ATOM   2689  N  N   . MET A 1 404 ? 28.074  -5.688  89.252  1.00 79.67  ? 405 MET A N   1 
ATOM   2690  C  CA  . MET A 1 404 ? 26.761  -6.325  89.318  1.00 78.86  ? 405 MET A CA  1 
ATOM   2691  C  C   . MET A 1 404 ? 26.331  -7.064  88.050  1.00 74.32  ? 405 MET A C   1 
ATOM   2692  O  O   . MET A 1 404 ? 25.784  -8.164  88.126  1.00 75.88  ? 405 MET A O   1 
ATOM   2693  C  CB  . MET A 1 404 ? 25.721  -5.267  89.680  1.00 81.62  ? 405 MET A CB  1 
ATOM   2694  C  CG  . MET A 1 404 ? 26.157  -4.422  90.864  1.00 82.37  ? 405 MET A CG  1 
ATOM   2695  S  SD  . MET A 1 404 ? 25.306  -2.845  91.020  1.00 88.63  ? 405 MET A SD  1 
ATOM   2696  C  CE  . MET A 1 404 ? 26.202  -2.150  92.404  1.00 64.68  ? 405 MET A CE  1 
ATOM   2697  N  N   . ALA A 1 405 ? 26.575  -6.463  86.890  1.00 66.49  ? 406 ALA A N   1 
ATOM   2698  C  CA  . ALA A 1 405 ? 26.155  -7.064  85.628  1.00 59.68  ? 406 ALA A CA  1 
ATOM   2699  C  C   . ALA A 1 405 ? 27.249  -7.947  85.039  1.00 56.32  ? 406 ALA A C   1 
ATOM   2700  O  O   . ALA A 1 405 ? 26.963  -8.937  84.366  1.00 60.19  ? 406 ALA A O   1 
ATOM   2701  C  CB  . ALA A 1 405 ? 25.753  -5.986  84.634  1.00 57.38  ? 406 ALA A CB  1 
ATOM   2702  N  N   . ASP A 1 412 ? 24.438  -16.015 77.921  1.00 105.79 ? 413 ASP A N   1 
ATOM   2703  C  CA  . ASP A 1 412 ? 24.165  -14.584 77.997  1.00 103.14 ? 413 ASP A CA  1 
ATOM   2704  C  C   . ASP A 1 412 ? 22.666  -14.293 78.043  1.00 96.00  ? 413 ASP A C   1 
ATOM   2705  O  O   . ASP A 1 412 ? 22.201  -13.296 77.492  1.00 96.28  ? 413 ASP A O   1 
ATOM   2706  C  CB  . ASP A 1 412 ? 24.810  -13.854 76.816  1.00 107.72 ? 413 ASP A CB  1 
ATOM   2707  C  CG  . ASP A 1 412 ? 26.323  -13.785 76.930  1.00 111.30 ? 413 ASP A CG  1 
ATOM   2708  O  OD1 . ASP A 1 412 ? 26.848  -14.020 78.039  1.00 113.10 ? 413 ASP A OD1 1 
ATOM   2709  O  OD2 . ASP A 1 412 ? 26.986  -13.497 75.912  1.00 112.46 ? 413 ASP A OD2 1 
ATOM   2710  N  N   . ARG A 1 413 ? 21.917  -15.180 78.692  1.00 90.61  ? 414 ARG A N   1 
ATOM   2711  C  CA  . ARG A 1 413 ? 20.515  -14.925 79.005  1.00 80.40  ? 414 ARG A CA  1 
ATOM   2712  C  C   . ARG A 1 413 ? 20.438  -14.422 80.441  1.00 76.75  ? 414 ARG A C   1 
ATOM   2713  O  O   . ARG A 1 413 ? 20.931  -15.075 81.360  1.00 74.50  ? 414 ARG A O   1 
ATOM   2714  C  CB  . ARG A 1 413 ? 19.667  -16.183 78.814  1.00 81.32  ? 414 ARG A CB  1 
ATOM   2715  N  N   . CYS A 1 414 ? 19.813  -13.265 80.633  1.00 68.54  ? 415 CYS A N   1 
ATOM   2716  C  CA  . CYS A 1 414 ? 19.985  -12.508 81.869  1.00 60.64  ? 415 CYS A CA  1 
ATOM   2717  C  C   . CYS A 1 414 ? 18.690  -12.190 82.616  1.00 54.05  ? 415 CYS A C   1 
ATOM   2718  O  O   . CYS A 1 414 ? 17.593  -12.297 82.073  1.00 45.93  ? 415 CYS A O   1 
ATOM   2719  C  CB  . CYS A 1 414 ? 20.727  -11.207 81.562  1.00 44.28  ? 415 CYS A CB  1 
ATOM   2720  S  SG  . CYS A 1 414 ? 20.089  -10.342 80.111  1.00 94.22  ? 415 CYS A SG  1 
ATOM   2721  N  N   . TRP A 1 415 ? 18.843  -11.805 83.877  1.00 45.77  ? 416 TRP A N   1 
ATOM   2722  C  CA  . TRP A 1 415 ? 17.721  -11.468 84.746  1.00 46.41  ? 416 TRP A CA  1 
ATOM   2723  C  C   . TRP A 1 415 ? 17.218  -10.041 84.488  1.00 43.76  ? 416 TRP A C   1 
ATOM   2724  O  O   . TRP A 1 415 ? 17.957  -9.072  84.655  1.00 42.62  ? 416 TRP A O   1 
ATOM   2725  C  CB  . TRP A 1 415 ? 18.168  -11.660 86.201  1.00 46.42  ? 416 TRP A CB  1 
ATOM   2726  C  CG  . TRP A 1 415 ? 17.334  -11.029 87.274  1.00 49.90  ? 416 TRP A CG  1 
ATOM   2727  C  CD1 . TRP A 1 415 ? 17.599  -9.864  87.935  1.00 44.73  ? 416 TRP A CD1 1 
ATOM   2728  C  CD2 . TRP A 1 415 ? 16.134  -11.555 87.856  1.00 50.70  ? 416 TRP A CD2 1 
ATOM   2729  N  NE1 . TRP A 1 415 ? 16.629  -9.621  88.876  1.00 44.68  ? 416 TRP A NE1 1 
ATOM   2730  C  CE2 . TRP A 1 415 ? 15.721  -10.647 88.851  1.00 51.10  ? 416 TRP A CE2 1 
ATOM   2731  C  CE3 . TRP A 1 415 ? 15.366  -12.701 87.629  1.00 54.09  ? 416 TRP A CE3 1 
ATOM   2732  C  CZ2 . TRP A 1 415 ? 14.570  -10.845 89.612  1.00 51.35  ? 416 TRP A CZ2 1 
ATOM   2733  C  CZ3 . TRP A 1 415 ? 14.224  -12.895 88.387  1.00 56.02  ? 416 TRP A CZ3 1 
ATOM   2734  C  CH2 . TRP A 1 415 ? 13.836  -11.971 89.363  1.00 56.43  ? 416 TRP A CH2 1 
ATOM   2735  N  N   . ASN A 1 416 ? 15.957  -9.928  84.072  1.00 46.45  ? 417 ASN A N   1 
ATOM   2736  C  CA  . ASN A 1 416 ? 15.341  -8.634  83.775  1.00 42.83  ? 417 ASN A CA  1 
ATOM   2737  C  C   . ASN A 1 416 ? 14.532  -8.095  84.952  1.00 42.80  ? 417 ASN A C   1 
ATOM   2738  O  O   . ASN A 1 416 ? 13.949  -7.013  84.886  1.00 50.75  ? 417 ASN A O   1 
ATOM   2739  C  CB  . ASN A 1 416 ? 14.460  -8.735  82.524  1.00 43.12  ? 417 ASN A CB  1 
ATOM   2740  C  CG  . ASN A 1 416 ? 13.376  -9.799  82.642  1.00 44.50  ? 417 ASN A CG  1 
ATOM   2741  O  OD1 . ASN A 1 416 ? 12.874  -10.085 83.729  1.00 45.07  ? 417 ASN A OD1 1 
ATOM   2742  N  ND2 . ASN A 1 416 ? 13.007  -10.385 81.509  1.00 45.15  ? 417 ASN A ND2 1 
ATOM   2743  N  N   . GLY A 1 417 ? 14.511  -8.876  86.023  1.00 44.47  ? 418 GLY A N   1 
ATOM   2744  C  CA  . GLY A 1 417 ? 13.849  -8.527  87.266  1.00 47.71  ? 418 GLY A CA  1 
ATOM   2745  C  C   . GLY A 1 417 ? 12.511  -9.201  87.519  1.00 50.71  ? 418 GLY A C   1 
ATOM   2746  O  O   . GLY A 1 417 ? 12.104  -9.341  88.673  1.00 53.78  ? 418 GLY A O   1 
ATOM   2747  N  N   . MET A 1 418 ? 11.808  -9.603  86.466  1.00 46.89  ? 419 MET A N   1 
ATOM   2748  C  CA  . MET A 1 418 ? 10.752  -10.605 86.603  1.00 55.96  ? 419 MET A CA  1 
ATOM   2749  C  C   . MET A 1 418 ? 11.272  -12.046 86.532  1.00 60.46  ? 419 MET A C   1 
ATOM   2750  O  O   . MET A 1 418 ? 10.847  -12.906 87.303  1.00 65.77  ? 419 MET A O   1 
ATOM   2751  C  CB  . MET A 1 418 ? 9.654   -10.361 85.570  1.00 56.11  ? 419 MET A CB  1 
ATOM   2752  C  CG  . MET A 1 418 ? 8.735   -9.216  85.984  1.00 55.22  ? 419 MET A CG  1 
ATOM   2753  S  SD  . MET A 1 418 ? 8.122   -8.185  84.641  1.00 98.62  ? 419 MET A SD  1 
ATOM   2754  C  CE  . MET A 1 418 ? 8.032   -9.379  83.314  1.00 86.96  ? 419 MET A CE  1 
ATOM   2755  N  N   . ALA A 1 419 ? 12.194  -12.295 85.604  1.00 58.62  ? 420 ALA A N   1 
ATOM   2756  C  CA  . ALA A 1 419 ? 12.699  -13.644 85.352  1.00 57.02  ? 420 ALA A CA  1 
ATOM   2757  C  C   . ALA A 1 419 ? 13.996  -13.613 84.547  1.00 59.90  ? 420 ALA A C   1 
ATOM   2758  O  O   . ALA A 1 419 ? 14.505  -12.543 84.216  1.00 56.67  ? 420 ALA A O   1 
ATOM   2759  C  CB  . ALA A 1 419 ? 11.649  -14.473 84.623  1.00 55.91  ? 420 ALA A CB  1 
ATOM   2760  N  N   . ARG A 1 420 ? 14.534  -14.791 84.243  1.00 60.61  ? 421 ARG A N   1 
ATOM   2761  C  CA  . ARG A 1 420 ? 15.650  -14.896 83.308  1.00 66.81  ? 421 ARG A CA  1 
ATOM   2762  C  C   . ARG A 1 420 ? 15.115  -14.667 81.900  1.00 65.79  ? 421 ARG A C   1 
ATOM   2763  O  O   . ARG A 1 420 ? 14.007  -15.100 81.582  1.00 67.99  ? 421 ARG A O   1 
ATOM   2764  C  CB  . ARG A 1 420 ? 16.339  -16.258 83.416  1.00 51.02  ? 421 ARG A CB  1 
ATOM   2765  N  N   . GLY A 1 421 ? 15.886  -13.987 81.058  1.00 62.06  ? 422 GLY A N   1 
ATOM   2766  C  CA  . GLY A 1 421 ? 15.386  -13.606 79.749  1.00 66.98  ? 422 GLY A CA  1 
ATOM   2767  C  C   . GLY A 1 421 ? 16.065  -12.388 79.154  1.00 70.92  ? 422 GLY A C   1 
ATOM   2768  O  O   . GLY A 1 421 ? 17.223  -12.097 79.449  1.00 73.70  ? 422 GLY A O   1 
ATOM   2769  N  N   . ARG A 1 422 ? 15.349  -11.695 78.276  1.00 68.58  ? 423 ARG A N   1 
ATOM   2770  C  CA  . ARG A 1 422 ? 15.851  -10.459 77.690  1.00 68.96  ? 423 ARG A CA  1 
ATOM   2771  C  C   . ARG A 1 422 ? 15.156  -9.247  78.306  1.00 70.45  ? 423 ARG A C   1 
ATOM   2772  O  O   . ARG A 1 422 ? 13.978  -9.310  78.660  1.00 73.40  ? 423 ARG A O   1 
ATOM   2773  C  CB  . ARG A 1 422 ? 15.659  -10.467 76.172  1.00 67.61  ? 423 ARG A CB  1 
ATOM   2774  N  N   . TYR A 1 423 ? 15.895  -8.150  78.441  1.00 63.78  ? 424 TYR A N   1 
ATOM   2775  C  CA  . TYR A 1 423 ? 15.349  -6.919  79.003  1.00 60.25  ? 424 TYR A CA  1 
ATOM   2776  C  C   . TYR A 1 423 ? 15.049  -5.915  77.895  1.00 52.68  ? 424 TYR A C   1 
ATOM   2777  O  O   . TYR A 1 423 ? 15.956  -5.356  77.280  1.00 52.50  ? 424 TYR A O   1 
ATOM   2778  C  CB  . TYR A 1 423 ? 16.327  -6.333  80.023  1.00 51.99  ? 424 TYR A CB  1 
ATOM   2779  C  CG  . TYR A 1 423 ? 15.933  -5.006  80.633  1.00 50.94  ? 424 TYR A CG  1 
ATOM   2780  C  CD1 . TYR A 1 423 ? 15.088  -4.948  81.733  1.00 45.51  ? 424 TYR A CD1 1 
ATOM   2781  C  CD2 . TYR A 1 423 ? 16.438  -3.812  80.131  1.00 47.76  ? 424 TYR A CD2 1 
ATOM   2782  C  CE1 . TYR A 1 423 ? 14.738  -3.737  82.304  1.00 43.39  ? 424 TYR A CE1 1 
ATOM   2783  C  CE2 . TYR A 1 423 ? 16.093  -2.596  80.694  1.00 43.88  ? 424 TYR A CE2 1 
ATOM   2784  C  CZ  . TYR A 1 423 ? 15.244  -2.565  81.780  1.00 46.38  ? 424 TYR A CZ  1 
ATOM   2785  O  OH  . TYR A 1 423 ? 14.899  -1.358  82.345  1.00 39.12  ? 424 TYR A OH  1 
ATOM   2786  N  N   . LEU A 1 424 ? 13.761  -5.704  77.650  1.00 56.93  ? 425 LEU A N   1 
ATOM   2787  C  CA  . LEU A 1 424 ? 13.286  -4.822  76.586  1.00 56.50  ? 425 LEU A CA  1 
ATOM   2788  C  C   . LEU A 1 424 ? 13.528  -3.310  76.768  1.00 58.03  ? 425 LEU A C   1 
ATOM   2789  O  O   . LEU A 1 424 ? 14.043  -2.672  75.849  1.00 57.44  ? 425 LEU A O   1 
ATOM   2790  C  CB  . LEU A 1 424 ? 11.791  -5.068  76.357  1.00 62.36  ? 425 LEU A CB  1 
ATOM   2791  C  CG  . LEU A 1 424 ? 11.450  -6.459  75.821  1.00 66.31  ? 425 LEU A CG  1 
ATOM   2792  C  CD1 . LEU A 1 424 ? 9.948   -6.624  75.654  1.00 68.36  ? 425 LEU A CD1 1 
ATOM   2793  C  CD2 . LEU A 1 424 ? 12.175  -6.716  74.507  1.00 66.76  ? 425 LEU A CD2 1 
ATOM   2794  N  N   . PRO A 1 425 ? 13.150  -2.731  77.932  1.00 56.14  ? 426 PRO A N   1 
ATOM   2795  C  CA  . PRO A 1 425 ? 13.094  -1.263  78.042  1.00 53.94  ? 426 PRO A CA  1 
ATOM   2796  C  C   . PRO A 1 425 ? 14.368  -0.518  77.644  1.00 55.72  ? 426 PRO A C   1 
ATOM   2797  O  O   . PRO A 1 425 ? 15.478  -1.014  77.841  1.00 51.66  ? 426 PRO A O   1 
ATOM   2798  C  CB  . PRO A 1 425 ? 12.809  -1.039  79.531  1.00 54.24  ? 426 PRO A CB  1 
ATOM   2799  C  CG  . PRO A 1 425 ? 12.102  -2.262  79.961  1.00 52.37  ? 426 PRO A CG  1 
ATOM   2800  C  CD  . PRO A 1 425 ? 12.764  -3.371  79.205  1.00 53.25  ? 426 PRO A CD  1 
ATOM   2801  N  N   . GLU A 1 426 ? 14.187  0.675   77.083  1.00 58.37  ? 427 GLU A N   1 
ATOM   2802  C  CA  . GLU A 1 426 ? 15.301  1.523   76.673  1.00 58.75  ? 427 GLU A CA  1 
ATOM   2803  C  C   . GLU A 1 426 ? 16.043  2.095   77.871  1.00 46.97  ? 427 GLU A C   1 
ATOM   2804  O  O   . GLU A 1 426 ? 15.448  2.339   78.922  1.00 38.07  ? 427 GLU A O   1 
ATOM   2805  C  CB  . GLU A 1 426 ? 14.805  2.671   75.789  1.00 66.37  ? 427 GLU A CB  1 
ATOM   2806  C  CG  . GLU A 1 426 ? 14.995  2.459   74.295  1.00 72.85  ? 427 GLU A CG  1 
ATOM   2807  C  CD  . GLU A 1 426 ? 16.454  2.370   73.885  1.00 75.15  ? 427 GLU A CD  1 
ATOM   2808  O  OE1 . GLU A 1 426 ? 17.329  2.808   74.663  1.00 75.37  ? 427 GLU A OE1 1 
ATOM   2809  O  OE2 . GLU A 1 426 ? 16.726  1.861   72.778  1.00 77.11  ? 427 GLU A OE2 1 
ATOM   2810  N  N   . VAL A 1 427 ? 17.345  2.307   77.707  1.00 38.55  ? 428 VAL A N   1 
ATOM   2811  C  CA  . VAL A 1 427 ? 18.139  2.965   78.733  1.00 45.34  ? 428 VAL A CA  1 
ATOM   2812  C  C   . VAL A 1 427 ? 17.732  4.430   78.835  1.00 46.52  ? 428 VAL A C   1 
ATOM   2813  O  O   . VAL A 1 427 ? 17.633  5.127   77.826  1.00 47.23  ? 428 VAL A O   1 
ATOM   2814  C  CB  . VAL A 1 427 ? 19.650  2.864   78.445  1.00 43.67  ? 428 VAL A CB  1 
ATOM   2815  C  CG1 . VAL A 1 427 ? 20.450  3.482   79.583  1.00 39.63  ? 428 VAL A CG1 1 
ATOM   2816  C  CG2 . VAL A 1 427 ? 20.052  1.412   78.243  1.00 43.62  ? 428 VAL A CG2 1 
ATOM   2817  N  N   . MET A 1 428 ? 17.482  4.886   80.057  1.00 45.04  ? 429 MET A N   1 
ATOM   2818  C  CA  . MET A 1 428 ? 17.082  6.266   80.297  1.00 49.48  ? 429 MET A CA  1 
ATOM   2819  C  C   . MET A 1 428 ? 18.220  7.238   80.019  1.00 52.40  ? 429 MET A C   1 
ATOM   2820  O  O   . MET A 1 428 ? 19.388  6.851   79.983  1.00 44.20  ? 429 MET A O   1 
ATOM   2821  C  CB  . MET A 1 428 ? 16.595  6.441   81.737  1.00 52.80  ? 429 MET A CB  1 
ATOM   2822  C  CG  . MET A 1 428 ? 15.395  5.580   82.119  1.00 60.95  ? 429 MET A CG  1 
ATOM   2823  S  SD  . MET A 1 428 ? 13.800  6.280   81.634  1.00 51.70  ? 429 MET A SD  1 
ATOM   2824  C  CE  . MET A 1 428 ? 13.627  5.689   79.951  1.00 64.02  ? 429 MET A CE  1 
ATOM   2825  N  N   . GLY A 1 429 ? 17.867  8.500   79.803  1.00 51.41  ? 430 GLY A N   1 
ATOM   2826  C  CA  . GLY A 1 429 ? 18.855  9.556   79.716  1.00 31.56  ? 430 GLY A CA  1 
ATOM   2827  C  C   . GLY A 1 429 ? 19.414  9.857   81.095  1.00 41.98  ? 430 GLY A C   1 
ATOM   2828  O  O   . GLY A 1 429 ? 18.970  9.289   82.093  1.00 31.20  ? 430 GLY A O   1 
ATOM   2829  N  N   . ASP A 1 430 ? 20.385  10.760  81.152  1.00 42.29  ? 431 ASP A N   1 
ATOM   2830  C  CA  . ASP A 1 430 ? 21.042  11.104  82.408  1.00 42.21  ? 431 ASP A CA  1 
ATOM   2831  C  C   . ASP A 1 430 ? 20.413  12.329  83.062  1.00 36.58  ? 431 ASP A C   1 
ATOM   2832  O  O   . ASP A 1 430 ? 19.956  13.244  82.377  1.00 41.35  ? 431 ASP A O   1 
ATOM   2833  C  CB  . ASP A 1 430 ? 22.535  11.341  82.180  1.00 45.02  ? 431 ASP A CB  1 
ATOM   2834  C  CG  . ASP A 1 430 ? 23.179  10.239  81.365  1.00 53.39  ? 431 ASP A CG  1 
ATOM   2835  O  OD1 . ASP A 1 430 ? 23.268  9.099   81.869  1.00 55.86  ? 431 ASP A OD1 1 
ATOM   2836  O  OD2 . ASP A 1 430 ? 23.599  10.513  80.221  1.00 54.11  ? 431 ASP A OD2 1 
ATOM   2837  N  N   . GLY A 1 431 ? 20.378  12.333  84.391  1.00 35.14  ? 432 GLY A N   1 
ATOM   2838  C  CA  . GLY A 1 431 ? 19.876  13.475  85.135  1.00 35.32  ? 432 GLY A CA  1 
ATOM   2839  C  C   . GLY A 1 431 ? 18.532  13.230  85.790  1.00 34.12  ? 432 GLY A C   1 
ATOM   2840  O  O   . GLY A 1 431 ? 17.779  12.352  85.372  1.00 31.61  ? 432 GLY A O   1 
ATOM   2841  N  N   . LEU A 1 432 ? 18.243  14.013  86.826  1.00 36.59  ? 433 LEU A N   1 
ATOM   2842  C  CA  . LEU A 1 432 ? 17.033  13.843  87.625  1.00 42.24  ? 433 LEU A CA  1 
ATOM   2843  C  C   . LEU A 1 432 ? 15.763  13.896  86.786  1.00 36.66  ? 433 LEU A C   1 
ATOM   2844  O  O   . LEU A 1 432 ? 14.925  12.998  86.866  1.00 42.80  ? 433 LEU A O   1 
ATOM   2845  C  CB  . LEU A 1 432 ? 16.970  14.910  88.720  1.00 42.03  ? 433 LEU A CB  1 
ATOM   2846  C  CG  . LEU A 1 432 ? 15.889  14.728  89.786  1.00 38.75  ? 433 LEU A CG  1 
ATOM   2847  C  CD1 . LEU A 1 432 ? 16.127  13.447  90.564  1.00 42.45  ? 433 LEU A CD1 1 
ATOM   2848  C  CD2 . LEU A 1 432 ? 15.860  15.925  90.721  1.00 39.30  ? 433 LEU A CD2 1 
ATOM   2849  N  N   . ALA A 1 433 ? 15.634  14.945  85.979  1.00 33.34  ? 434 ALA A N   1 
ATOM   2850  C  CA  . ALA A 1 433 ? 14.440  15.160  85.167  1.00 45.11  ? 434 ALA A CA  1 
ATOM   2851  C  C   . ALA A 1 433 ? 14.152  13.978  84.245  1.00 43.08  ? 434 ALA A C   1 
ATOM   2852  O  O   . ALA A 1 433 ? 12.995  13.607  84.045  1.00 35.15  ? 434 ALA A O   1 
ATOM   2853  C  CB  . ALA A 1 433 ? 14.580  16.439  84.353  1.00 34.30  ? 434 ALA A CB  1 
ATOM   2854  N  N   . ASN A 1 434 ? 15.207  13.382  83.700  1.00 33.35  ? 435 ASN A N   1 
ATOM   2855  C  CA  . ASN A 1 434 ? 15.064  12.261  82.776  1.00 33.42  ? 435 ASN A CA  1 
ATOM   2856  C  C   . ASN A 1 434 ? 14.606  10.963  83.438  1.00 33.76  ? 435 ASN A C   1 
ATOM   2857  O  O   . ASN A 1 434 ? 14.383  9.964   82.756  1.00 33.97  ? 435 ASN A O   1 
ATOM   2858  C  CB  . ASN A 1 434 ? 16.385  12.013  82.044  1.00 43.14  ? 435 ASN A CB  1 
ATOM   2859  C  CG  . ASN A 1 434 ? 16.602  12.973  80.895  1.00 44.51  ? 435 ASN A CG  1 
ATOM   2860  O  OD1 . ASN A 1 434 ? 15.664  13.323  80.180  1.00 34.40  ? 435 ASN A OD1 1 
ATOM   2861  N  ND2 . ASN A 1 434 ? 17.845  13.405  80.711  1.00 42.93  ? 435 ASN A ND2 1 
ATOM   2862  N  N   . GLN A 1 435 ? 14.463  10.977  84.759  1.00 44.82  ? 436 GLN A N   1 
ATOM   2863  C  CA  . GLN A 1 435 ? 14.082  9.774   85.493  1.00 34.37  ? 436 GLN A CA  1 
ATOM   2864  C  C   . GLN A 1 435 ? 12.612  9.763   85.892  1.00 35.56  ? 436 GLN A C   1 
ATOM   2865  O  O   . GLN A 1 435 ? 12.182  8.899   86.656  1.00 36.12  ? 436 GLN A O   1 
ATOM   2866  C  CB  . GLN A 1 435 ? 14.947  9.616   86.745  1.00 33.98  ? 436 GLN A CB  1 
ATOM   2867  C  CG  . GLN A 1 435 ? 16.436  9.697   86.483  1.00 32.89  ? 436 GLN A CG  1 
ATOM   2868  C  CD  . GLN A 1 435 ? 16.883  8.780   85.364  1.00 40.50  ? 436 GLN A CD  1 
ATOM   2869  O  OE1 . GLN A 1 435 ? 16.472  7.621   85.291  1.00 33.06  ? 436 GLN A OE1 1 
ATOM   2870  N  NE2 . GLN A 1 435 ? 17.732  9.298   84.481  1.00 31.89  ? 436 GLN A NE2 1 
ATOM   2871  N  N   . ILE A 1 436 ? 11.844  10.720  85.379  1.00 36.08  ? 437 ILE A N   1 
ATOM   2872  C  CA  . ILE A 1 436 ? 10.428  10.817  85.715  1.00 38.49  ? 437 ILE A CA  1 
ATOM   2873  C  C   . ILE A 1 436 ? 9.677   9.561   85.255  1.00 37.92  ? 437 ILE A C   1 
ATOM   2874  O  O   . ILE A 1 436 ? 8.765   9.088   85.935  1.00 38.86  ? 437 ILE A O   1 
ATOM   2875  C  CB  . ILE A 1 436 ? 9.790   12.096  85.098  1.00 37.91  ? 437 ILE A CB  1 
ATOM   2876  C  CG1 . ILE A 1 436 ? 8.308   12.206  85.468  1.00 39.40  ? 437 ILE A CG1 1 
ATOM   2877  C  CG2 . ILE A 1 436 ? 9.986   12.144  83.586  1.00 38.40  ? 437 ILE A CG2 1 
ATOM   2878  C  CD1 . ILE A 1 436 ? 7.618   13.421  84.871  1.00 40.21  ? 437 ILE A CD1 1 
ATOM   2879  N  N   . ASN A 1 437 ? 10.073  9.028   84.103  1.00 40.55  ? 438 ASN A N   1 
ATOM   2880  C  CA  . ASN A 1 437 ? 9.466   7.824   83.537  1.00 45.62  ? 438 ASN A CA  1 
ATOM   2881  C  C   . ASN A 1 437 ? 10.203  6.511   83.817  1.00 46.49  ? 438 ASN A C   1 
ATOM   2882  O  O   . ASN A 1 437 ? 9.821   5.471   83.281  1.00 50.49  ? 438 ASN A O   1 
ATOM   2883  C  CB  . ASN A 1 437 ? 9.295   7.993   82.028  1.00 48.34  ? 438 ASN A CB  1 
ATOM   2884  C  CG  . ASN A 1 437 ? 8.163   8.937   81.679  1.00 49.82  ? 438 ASN A CG  1 
ATOM   2885  O  OD1 . ASN A 1 437 ? 7.259   9.161   82.484  1.00 45.14  ? 438 ASN A OD1 1 
ATOM   2886  N  ND2 . ASN A 1 437 ? 8.203   9.492   80.473  1.00 53.68  ? 438 ASN A ND2 1 
ATOM   2887  N  N   . ASN A 1 438 ? 11.265  6.557   84.620  1.00 42.31  ? 439 ASN A N   1 
ATOM   2888  C  CA  . ASN A 1 438 ? 12.092  5.372   84.864  1.00 45.39  ? 439 ASN A CA  1 
ATOM   2889  C  C   . ASN A 1 438 ? 11.266  4.202   85.402  1.00 44.53  ? 439 ASN A C   1 
ATOM   2890  O  O   . ASN A 1 438 ? 10.681  4.288   86.481  1.00 43.10  ? 439 ASN A O   1 
ATOM   2891  C  CB  . ASN A 1 438 ? 13.225  5.713   85.840  1.00 35.73  ? 439 ASN A CB  1 
ATOM   2892  C  CG  . ASN A 1 438 ? 14.295  4.630   85.914  1.00 40.29  ? 439 ASN A CG  1 
ATOM   2893  O  OD1 . ASN A 1 438 ? 13.997  3.436   85.954  1.00 45.89  ? 439 ASN A OD1 1 
ATOM   2894  N  ND2 . ASN A 1 438 ? 15.554  5.051   85.939  1.00 34.43  ? 439 ASN A ND2 1 
ATOM   2895  N  N   . PRO A 1 439 ? 11.225  3.097   84.640  1.00 37.68  ? 440 PRO A N   1 
ATOM   2896  C  CA  . PRO A 1 439 ? 10.397  1.926   84.957  1.00 54.43  ? 440 PRO A CA  1 
ATOM   2897  C  C   . PRO A 1 439 ? 10.861  1.173   86.201  1.00 53.96  ? 440 PRO A C   1 
ATOM   2898  O  O   . PRO A 1 439 ? 10.036  0.646   86.946  1.00 39.93  ? 440 PRO A O   1 
ATOM   2899  C  CB  . PRO A 1 439 ? 10.542  1.049   83.709  1.00 38.79  ? 440 PRO A CB  1 
ATOM   2900  C  CG  . PRO A 1 439 ? 11.865  1.430   83.137  1.00 37.72  ? 440 PRO A CG  1 
ATOM   2901  C  CD  . PRO A 1 439 ? 12.011  2.902   83.409  1.00 37.09  ? 440 PRO A CD  1 
ATOM   2902  N  N   . GLU A 1 440 ? 12.172  1.107   86.402  1.00 38.15  ? 441 GLU A N   1 
ATOM   2903  C  CA  . GLU A 1 440 ? 12.736  0.365   87.523  1.00 43.12  ? 441 GLU A CA  1 
ATOM   2904  C  C   . GLU A 1 440 ? 12.704  1.146   88.833  1.00 38.75  ? 441 GLU A C   1 
ATOM   2905  O  O   . GLU A 1 440 ? 12.405  0.591   89.889  1.00 47.60  ? 441 GLU A O   1 
ATOM   2906  C  CB  . GLU A 1 440 ? 14.167  -0.059  87.196  1.00 37.72  ? 441 GLU A CB  1 
ATOM   2907  C  CG  . GLU A 1 440 ? 14.309  -0.727  85.832  1.00 37.69  ? 441 GLU A CG  1 
ATOM   2908  C  CD  . GLU A 1 440 ? 13.248  -1.788  85.568  1.00 38.82  ? 441 GLU A CD  1 
ATOM   2909  O  OE1 . GLU A 1 440 ? 12.848  -2.500  86.514  1.00 39.68  ? 441 GLU A OE1 1 
ATOM   2910  O  OE2 . GLU A 1 440 ? 12.812  -1.910  84.404  1.00 38.93  ? 441 GLU A OE2 1 
ATOM   2911  N  N   . VAL A 1 441 ? 13.023  2.433   88.758  1.00 43.70  ? 442 VAL A N   1 
ATOM   2912  C  CA  . VAL A 1 441 ? 13.062  3.279   89.943  1.00 48.60  ? 442 VAL A CA  1 
ATOM   2913  C  C   . VAL A 1 441 ? 12.072  4.424   89.802  1.00 51.22  ? 442 VAL A C   1 
ATOM   2914  O  O   . VAL A 1 441 ? 12.039  5.096   88.772  1.00 52.22  ? 442 VAL A O   1 
ATOM   2915  C  CB  . VAL A 1 441 ? 14.469  3.864   90.183  1.00 46.09  ? 442 VAL A CB  1 
ATOM   2916  C  CG1 . VAL A 1 441 ? 14.560  4.477   91.574  1.00 47.18  ? 442 VAL A CG1 1 
ATOM   2917  C  CG2 . VAL A 1 441 ? 15.532  2.798   89.991  1.00 45.45  ? 442 VAL A CG2 1 
ATOM   2918  N  N   . GLU A 1 442 ? 11.278  4.668   90.836  1.00 53.51  ? 443 GLU A N   1 
ATOM   2919  C  CA  . GLU A 1 442 ? 10.351  5.786   90.779  1.00 58.38  ? 443 GLU A CA  1 
ATOM   2920  C  C   . GLU A 1 442 ? 10.948  6.956   91.538  1.00 55.80  ? 443 GLU A C   1 
ATOM   2921  O  O   . GLU A 1 442 ? 11.069  6.938   92.764  1.00 56.25  ? 443 GLU A O   1 
ATOM   2922  C  CB  . GLU A 1 442 ? 8.978   5.406   91.337  1.00 69.29  ? 443 GLU A CB  1 
ATOM   2923  C  CG  . GLU A 1 442 ? 7.871   5.489   90.293  1.00 76.32  ? 443 GLU A CG  1 
ATOM   2924  C  CD  . GLU A 1 442 ? 6.508   5.115   90.839  1.00 86.15  ? 443 GLU A CD  1 
ATOM   2925  O  OE1 . GLU A 1 442 ? 5.989   4.046   90.456  1.00 88.78  ? 443 GLU A OE1 1 
ATOM   2926  O  OE2 . GLU A 1 442 ? 5.953   5.893   91.643  1.00 90.42  ? 443 GLU A OE2 1 
ATOM   2927  N  N   . VAL A 1 443 ? 11.321  7.978   90.778  1.00 53.52  ? 444 VAL A N   1 
ATOM   2928  C  CA  . VAL A 1 443 ? 12.061  9.108   91.307  1.00 50.46  ? 444 VAL A CA  1 
ATOM   2929  C  C   . VAL A 1 443 ? 11.244  10.380  91.179  1.00 48.79  ? 444 VAL A C   1 
ATOM   2930  O  O   . VAL A 1 443 ? 10.759  10.707  90.096  1.00 51.49  ? 444 VAL A O   1 
ATOM   2931  C  CB  . VAL A 1 443 ? 13.401  9.292   90.570  1.00 42.51  ? 444 VAL A CB  1 
ATOM   2932  C  CG1 . VAL A 1 443 ? 14.195  10.428  91.188  1.00 35.93  ? 444 VAL A CG1 1 
ATOM   2933  C  CG2 . VAL A 1 443 ? 14.201  7.999   90.587  1.00 42.39  ? 444 VAL A CG2 1 
ATOM   2934  N  N   . ASP A 1 444 ? 11.097  11.102  92.283  1.00 52.70  ? 445 ASP A N   1 
ATOM   2935  C  CA  . ASP A 1 444 ? 10.397  12.374  92.242  1.00 55.88  ? 445 ASP A CA  1 
ATOM   2936  C  C   . ASP A 1 444 ? 11.396  13.438  91.815  1.00 46.16  ? 445 ASP A C   1 
ATOM   2937  O  O   . ASP A 1 444 ? 12.381  13.688  92.506  1.00 38.38  ? 445 ASP A O   1 
ATOM   2938  C  CB  . ASP A 1 444 ? 9.784   12.706  93.602  1.00 67.70  ? 445 ASP A CB  1 
ATOM   2939  C  CG  . ASP A 1 444 ? 9.172   14.090  93.644  1.00 76.50  ? 445 ASP A CG  1 
ATOM   2940  O  OD1 . ASP A 1 444 ? 8.519   14.481  92.654  1.00 79.86  ? 445 ASP A OD1 1 
ATOM   2941  O  OD2 . ASP A 1 444 ? 9.344   14.785  94.666  1.00 81.44  ? 445 ASP A OD2 1 
ATOM   2942  N  N   . ILE A 1 445 ? 11.131  14.062  90.673  1.00 47.20  ? 446 ILE A N   1 
ATOM   2943  C  CA  . ILE A 1 445 ? 12.096  14.962  90.058  1.00 50.95  ? 446 ILE A CA  1 
ATOM   2944  C  C   . ILE A 1 445 ? 11.990  16.373  90.620  1.00 38.07  ? 446 ILE A C   1 
ATOM   2945  O  O   . ILE A 1 445 ? 12.852  17.215  90.370  1.00 39.87  ? 446 ILE A O   1 
ATOM   2946  C  CB  . ILE A 1 445 ? 11.917  15.009  88.530  1.00 49.95  ? 446 ILE A CB  1 
ATOM   2947  C  CG1 . ILE A 1 445 ? 10.572  15.636  88.163  1.00 38.42  ? 446 ILE A CG1 1 
ATOM   2948  C  CG2 . ILE A 1 445 ? 12.017  13.611  87.948  1.00 36.64  ? 446 ILE A CG2 1 
ATOM   2949  C  CD1 . ILE A 1 445 ? 10.281  15.615  86.678  1.00 38.34  ? 446 ILE A CD1 1 
ATOM   2950  N  N   . THR A 1 446 ? 10.933  16.625  91.384  1.00 52.61  ? 447 THR A N   1 
ATOM   2951  C  CA  . THR A 1 446 ? 10.705  17.943  91.961  1.00 56.39  ? 447 THR A CA  1 
ATOM   2952  C  C   . THR A 1 446 ? 11.418  18.094  93.300  1.00 56.64  ? 447 THR A C   1 
ATOM   2953  O  O   . THR A 1 446 ? 11.338  19.143  93.940  1.00 63.38  ? 447 THR A O   1 
ATOM   2954  C  CB  . THR A 1 446 ? 9.202   18.223  92.156  1.00 42.23  ? 447 THR A CB  1 
ATOM   2955  O  OG1 . THR A 1 446 ? 8.729   17.536  93.320  1.00 43.15  ? 447 THR A OG1 1 
ATOM   2956  C  CG2 . THR A 1 446 ? 8.415   17.765  90.943  1.00 50.98  ? 447 THR A CG2 1 
ATOM   2957  N  N   . LYS A 1 447 ? 12.116  17.043  93.719  1.00 59.22  ? 448 LYS A N   1 
ATOM   2958  C  CA  . LYS A 1 447 ? 12.835  17.066  94.990  1.00 57.89  ? 448 LYS A CA  1 
ATOM   2959  C  C   . LYS A 1 447 ? 14.332  16.808  94.816  1.00 57.85  ? 448 LYS A C   1 
ATOM   2960  O  O   . LYS A 1 447 ? 14.818  15.725  95.146  1.00 62.00  ? 448 LYS A O   1 
ATOM   2961  C  CB  . LYS A 1 447 ? 12.241  16.035  95.951  1.00 55.74  ? 448 LYS A CB  1 
ATOM   2962  N  N   . PRO A 1 448 ? 15.070  17.805  94.302  1.00 51.08  ? 449 PRO A N   1 
ATOM   2963  C  CA  . PRO A 1 448 ? 16.520  17.645  94.148  1.00 47.38  ? 449 PRO A CA  1 
ATOM   2964  C  C   . PRO A 1 448 ? 17.245  17.699  95.488  1.00 48.59  ? 449 PRO A C   1 
ATOM   2965  O  O   . PRO A 1 448 ? 16.742  18.297  96.438  1.00 52.00  ? 449 PRO A O   1 
ATOM   2966  C  CB  . PRO A 1 448 ? 16.912  18.834  93.267  1.00 41.66  ? 449 PRO A CB  1 
ATOM   2967  C  CG  . PRO A 1 448 ? 15.881  19.860  93.554  1.00 50.36  ? 449 PRO A CG  1 
ATOM   2968  C  CD  . PRO A 1 448 ? 14.604  19.111  93.803  1.00 51.74  ? 449 PRO A CD  1 
ATOM   2969  N  N   . ASP A 1 449 ? 18.414  17.071  95.558  1.00 47.98  ? 450 ASP A N   1 
ATOM   2970  C  CA  . ASP A 1 449 ? 19.223  17.093  96.770  1.00 52.98  ? 450 ASP A CA  1 
ATOM   2971  C  C   . ASP A 1 449 ? 19.921  18.444  96.922  1.00 48.47  ? 450 ASP A C   1 
ATOM   2972  O  O   . ASP A 1 449 ? 20.454  18.986  95.954  1.00 49.79  ? 450 ASP A O   1 
ATOM   2973  C  CB  . ASP A 1 449 ? 20.247  15.959  96.748  1.00 54.74  ? 450 ASP A CB  1 
ATOM   2974  C  CG  . ASP A 1 449 ? 21.044  15.869  98.030  1.00 62.40  ? 450 ASP A CG  1 
ATOM   2975  O  OD1 . ASP A 1 449 ? 22.233  16.248  98.018  1.00 67.36  ? 450 ASP A OD1 1 
ATOM   2976  O  OD2 . ASP A 1 449 ? 20.483  15.421  99.052  1.00 67.08  ? 450 ASP A OD2 1 
ATOM   2977  N  N   . MET A 1 450 ? 19.914  18.982  98.138  1.00 49.47  ? 451 MET A N   1 
ATOM   2978  C  CA  . MET A 1 450 ? 20.459  20.313  98.393  1.00 52.96  ? 451 MET A CA  1 
ATOM   2979  C  C   . MET A 1 450 ? 21.981  20.363  98.281  1.00 46.90  ? 451 MET A C   1 
ATOM   2980  O  O   . MET A 1 450 ? 22.542  21.317  97.727  1.00 45.62  ? 451 MET A O   1 
ATOM   2981  C  CB  . MET A 1 450 ? 20.024  20.805  99.774  1.00 58.39  ? 451 MET A CB  1 
ATOM   2982  C  CG  . MET A 1 450 ? 18.760  21.660  99.770  1.00 66.66  ? 451 MET A CG  1 
ATOM   2983  S  SD  . MET A 1 450 ? 18.917  23.179  98.804  1.00 106.64 ? 451 MET A SD  1 
ATOM   2984  C  CE  . MET A 1 450 ? 18.115  22.716  97.269  1.00 50.27  ? 451 MET A CE  1 
ATOM   2985  N  N   . THR A 1 451 ? 22.641  19.338  98.813  1.00 43.57  ? 452 THR A N   1 
ATOM   2986  C  CA  . THR A 1 451 ? 24.097  19.249  98.767  1.00 45.19  ? 452 THR A CA  1 
ATOM   2987  C  C   . THR A 1 451 ? 24.594  19.351  97.329  1.00 37.90  ? 452 THR A C   1 
ATOM   2988  O  O   . THR A 1 451 ? 25.484  20.152  97.019  1.00 36.18  ? 452 THR A O   1 
ATOM   2989  C  CB  . THR A 1 451 ? 24.602  17.934  99.391  1.00 45.99  ? 452 THR A CB  1 
ATOM   2990  O  OG1 . THR A 1 451 ? 24.027  17.766  100.693 1.00 46.96  ? 452 THR A OG1 1 
ATOM   2991  C  CG2 . THR A 1 451 ? 26.120  17.942  99.503  1.00 42.46  ? 452 THR A CG2 1 
ATOM   2992  N  N   . ILE A 1 452 ? 23.992  18.547  96.457  1.00 36.64  ? 453 ILE A N   1 
ATOM   2993  C  CA  . ILE A 1 452 ? 24.312  18.555  95.035  1.00 38.83  ? 453 ILE A CA  1 
ATOM   2994  C  C   . ILE A 1 452 ? 24.176  19.954  94.441  1.00 36.69  ? 453 ILE A C   1 
ATOM   2995  O  O   . ILE A 1 452 ? 25.054  20.413  93.712  1.00 29.81  ? 453 ILE A O   1 
ATOM   2996  C  CB  . ILE A 1 452 ? 23.405  17.587  94.249  1.00 41.67  ? 453 ILE A CB  1 
ATOM   2997  C  CG1 . ILE A 1 452 ? 23.536  16.163  94.796  1.00 41.51  ? 453 ILE A CG1 1 
ATOM   2998  C  CG2 . ILE A 1 452 ? 23.731  17.636  92.763  1.00 35.81  ? 453 ILE A CG2 1 
ATOM   2999  C  CD1 . ILE A 1 452 ? 24.938  15.604  94.725  1.00 44.44  ? 453 ILE A CD1 1 
ATOM   3000  N  N   . ARG A 1 453 ? 23.077  20.627  94.766  1.00 38.14  ? 454 ARG A N   1 
ATOM   3001  C  CA  . ARG A 1 453 ? 22.825  21.976  94.268  1.00 45.40  ? 454 ARG A CA  1 
ATOM   3002  C  C   . ARG A 1 453 ? 23.907  22.963  94.707  1.00 46.08  ? 454 ARG A C   1 
ATOM   3003  O  O   . ARG A 1 453 ? 24.414  23.753  93.896  1.00 51.55  ? 454 ARG A O   1 
ATOM   3004  C  CB  . ARG A 1 453 ? 21.448  22.459  94.731  1.00 51.28  ? 454 ARG A CB  1 
ATOM   3005  C  CG  . ARG A 1 453 ? 20.350  22.190  93.719  1.00 60.31  ? 454 ARG A CG  1 
ATOM   3006  C  CD  . ARG A 1 453 ? 20.690  22.866  92.402  1.00 65.47  ? 454 ARG A CD  1 
ATOM   3007  N  NE  . ARG A 1 453 ? 19.979  22.289  91.267  1.00 68.55  ? 454 ARG A NE  1 
ATOM   3008  C  CZ  . ARG A 1 453 ? 20.203  22.631  90.003  1.00 74.14  ? 454 ARG A CZ  1 
ATOM   3009  N  NH1 . ARG A 1 453 ? 21.118  23.548  89.717  1.00 72.50  ? 454 ARG A NH1 1 
ATOM   3010  N  NH2 . ARG A 1 453 ? 19.515  22.059  89.024  1.00 74.22  ? 454 ARG A NH2 1 
ATOM   3011  N  N   . GLN A 1 454 ? 24.264  22.909  95.987  1.00 42.18  ? 455 GLN A N   1 
ATOM   3012  C  CA  . GLN A 1 454 ? 25.326  23.762  96.516  1.00 50.39  ? 455 GLN A CA  1 
ATOM   3013  C  C   . GLN A 1 454 ? 26.657  23.503  95.803  1.00 43.84  ? 455 GLN A C   1 
ATOM   3014  O  O   . GLN A 1 454 ? 27.376  24.444  95.432  1.00 47.55  ? 455 GLN A O   1 
ATOM   3015  C  CB  . GLN A 1 454 ? 25.477  23.550  98.024  1.00 52.72  ? 455 GLN A CB  1 
ATOM   3016  C  CG  . GLN A 1 454 ? 24.292  24.058  98.831  1.00 60.24  ? 455 GLN A CG  1 
ATOM   3017  C  CD  . GLN A 1 454 ? 24.393  23.724  100.306 1.00 70.71  ? 455 GLN A CD  1 
ATOM   3018  O  OE1 . GLN A 1 454 ? 25.294  23.000  100.730 1.00 73.66  ? 455 GLN A OE1 1 
ATOM   3019  N  NE2 . GLN A 1 454 ? 23.466  24.252  101.097 1.00 74.27  ? 455 GLN A NE2 1 
ATOM   3020  N  N   . GLN A 1 455 ? 26.975  22.226  95.601  1.00 37.04  ? 456 GLN A N   1 
ATOM   3021  C  CA  . GLN A 1 455 ? 28.195  21.857  94.887  1.00 38.34  ? 456 GLN A CA  1 
ATOM   3022  C  C   . GLN A 1 455 ? 28.187  22.397  93.459  1.00 37.83  ? 456 GLN A C   1 
ATOM   3023  O  O   . GLN A 1 455 ? 29.211  22.869  92.955  1.00 37.76  ? 456 GLN A O   1 
ATOM   3024  C  CB  . GLN A 1 455 ? 28.374  20.340  94.877  1.00 28.49  ? 456 GLN A CB  1 
ATOM   3025  C  CG  . GLN A 1 455 ? 28.518  19.732  96.261  1.00 34.19  ? 456 GLN A CG  1 
ATOM   3026  C  CD  . GLN A 1 455 ? 29.342  20.599  97.189  1.00 44.25  ? 456 GLN A CD  1 
ATOM   3027  O  OE1 . GLN A 1 455 ? 30.543  20.778  96.988  1.00 47.92  ? 456 GLN A OE1 1 
ATOM   3028  N  NE2 . GLN A 1 455 ? 28.698  21.147  98.213  1.00 49.53  ? 456 GLN A NE2 1 
ATOM   3029  N  N   . ILE A 1 456 ? 27.025  22.332  92.816  1.00 40.22  ? 457 ILE A N   1 
ATOM   3030  C  CA  . ILE A 1 456 ? 26.856  22.875  91.475  1.00 39.22  ? 457 ILE A CA  1 
ATOM   3031  C  C   . ILE A 1 456 ? 27.127  24.377  91.488  1.00 42.15  ? 457 ILE A C   1 
ATOM   3032  O  O   . ILE A 1 456 ? 27.769  24.911  90.575  1.00 44.25  ? 457 ILE A O   1 
ATOM   3033  C  CB  . ILE A 1 456 ? 25.442  22.586  90.920  1.00 37.64  ? 457 ILE A CB  1 
ATOM   3034  C  CG1 . ILE A 1 456 ? 25.293  21.095  90.615  1.00 42.86  ? 457 ILE A CG1 1 
ATOM   3035  C  CG2 . ILE A 1 456 ? 25.174  23.392  89.662  1.00 32.76  ? 457 ILE A CG2 1 
ATOM   3036  C  CD1 . ILE A 1 456 ? 23.925  20.703  90.103  1.00 43.35  ? 457 ILE A CD1 1 
ATOM   3037  N  N   . MET A 1 457 ? 26.658  25.053  92.534  1.00 37.06  ? 458 MET A N   1 
ATOM   3038  C  CA  . MET A 1 457 ? 26.959  26.474  92.687  1.00 42.82  ? 458 MET A CA  1 
ATOM   3039  C  C   . MET A 1 457 ? 28.464  26.714  92.786  1.00 40.07  ? 458 MET A C   1 
ATOM   3040  O  O   . MET A 1 457 ? 29.003  27.620  92.134  1.00 36.39  ? 458 MET A O   1 
ATOM   3041  C  CB  . MET A 1 457 ? 26.256  27.063  93.914  1.00 45.55  ? 458 MET A CB  1 
ATOM   3042  C  CG  . MET A 1 457 ? 24.744  27.196  93.782  1.00 49.00  ? 458 MET A CG  1 
ATOM   3043  S  SD  . MET A 1 457 ? 24.169  27.724  92.151  1.00 71.19  ? 458 MET A SD  1 
ATOM   3044  C  CE  . MET A 1 457 ? 25.102  29.233  91.883  1.00 64.57  ? 458 MET A CE  1 
ATOM   3045  N  N   . GLN A 1 458 ? 29.139  25.900  93.596  1.00 35.79  ? 459 GLN A N   1 
ATOM   3046  C  CA  . GLN A 1 458 ? 30.594  25.993  93.725  1.00 37.36  ? 459 GLN A CA  1 
ATOM   3047  C  C   . GLN A 1 458 ? 31.288  25.850  92.368  1.00 31.37  ? 459 GLN A C   1 
ATOM   3048  O  O   . GLN A 1 458 ? 32.173  26.647  92.018  1.00 26.55  ? 459 GLN A O   1 
ATOM   3049  C  CB  . GLN A 1 458 ? 31.116  24.932  94.696  1.00 34.00  ? 459 GLN A CB  1 
ATOM   3050  C  CG  . GLN A 1 458 ? 30.657  25.126  96.134  1.00 39.80  ? 459 GLN A CG  1 
ATOM   3051  C  CD  . GLN A 1 458 ? 31.119  26.448  96.717  1.00 48.68  ? 459 GLN A CD  1 
ATOM   3052  O  OE1 . GLN A 1 458 ? 32.307  26.645  96.974  1.00 50.89  ? 459 GLN A OE1 1 
ATOM   3053  N  NE2 . GLN A 1 458 ? 30.179  27.363  96.929  1.00 42.34  ? 459 GLN A NE2 1 
ATOM   3054  N  N   . LEU A 1 459 ? 30.874  24.840  91.606  1.00 34.31  ? 460 LEU A N   1 
ATOM   3055  C  CA  . LEU A 1 459 ? 31.408  24.626  90.264  1.00 31.76  ? 460 LEU A CA  1 
ATOM   3056  C  C   . LEU A 1 459 ? 31.198  25.856  89.385  1.00 36.30  ? 460 LEU A C   1 
ATOM   3057  O  O   . LEU A 1 459 ? 32.121  26.292  88.693  1.00 40.80  ? 460 LEU A O   1 
ATOM   3058  C  CB  . LEU A 1 459 ? 30.768  23.398  89.611  1.00 37.26  ? 460 LEU A CB  1 
ATOM   3059  C  CG  . LEU A 1 459 ? 31.010  22.037  90.268  1.00 37.85  ? 460 LEU A CG  1 
ATOM   3060  C  CD1 . LEU A 1 459 ? 30.259  20.945  89.524  1.00 42.10  ? 460 LEU A CD1 1 
ATOM   3061  C  CD2 . LEU A 1 459 ? 32.492  21.718  90.326  1.00 37.98  ? 460 LEU A CD2 1 
ATOM   3062  N  N   . LYS A 1 460 ? 29.989  26.414  89.420  1.00 32.27  ? 461 LYS A N   1 
ATOM   3063  C  CA  . LYS A 1 460 ? 29.688  27.637  88.672  1.00 30.39  ? 461 LYS A CA  1 
ATOM   3064  C  C   . LYS A 1 460 ? 30.659  28.766  89.012  1.00 27.44  ? 461 LYS A C   1 
ATOM   3065  O  O   . LYS A 1 460 ? 31.272  29.373  88.123  1.00 36.24  ? 461 LYS A O   1 
ATOM   3066  C  CB  . LYS A 1 460 ? 28.259  28.108  88.949  1.00 33.16  ? 461 LYS A CB  1 
ATOM   3067  C  CG  . LYS A 1 460 ? 27.159  27.226  88.389  1.00 40.51  ? 461 LYS A CG  1 
ATOM   3068  C  CD  . LYS A 1 460 ? 25.823  27.953  88.473  1.00 42.86  ? 461 LYS A CD  1 
ATOM   3069  C  CE  . LYS A 1 460 ? 24.650  27.019  88.251  1.00 44.70  ? 461 LYS A CE  1 
ATOM   3070  N  NZ  . LYS A 1 460 ? 23.361  27.683  88.602  1.00 49.06  ? 461 LYS A NZ  1 
ATOM   3071  N  N   . ILE A 1 461 ? 30.788  29.041  90.307  1.00 27.72  ? 462 ILE A N   1 
ATOM   3072  C  CA  . ILE A 1 461 ? 31.642  30.124  90.785  1.00 33.02  ? 462 ILE A CA  1 
ATOM   3073  C  C   . ILE A 1 461 ? 33.102  29.945  90.368  1.00 38.75  ? 462 ILE A C   1 
ATOM   3074  O  O   . ILE A 1 461 ? 33.719  30.867  89.813  1.00 33.80  ? 462 ILE A O   1 
ATOM   3075  C  CB  . ILE A 1 461 ? 31.565  30.249  92.318  1.00 36.83  ? 462 ILE A CB  1 
ATOM   3076  C  CG1 . ILE A 1 461 ? 30.155  30.672  92.739  1.00 38.85  ? 462 ILE A CG1 1 
ATOM   3077  C  CG2 . ILE A 1 461 ? 32.593  31.247  92.828  1.00 30.79  ? 462 ILE A CG2 1 
ATOM   3078  C  CD1 . ILE A 1 461 ? 29.885  30.523  94.219  1.00 38.18  ? 462 ILE A CD1 1 
ATOM   3079  N  N   . MET A 1 462 ? 33.650  28.759  90.625  1.00 34.89  ? 463 MET A N   1 
ATOM   3080  C  CA  . MET A 1 462 ? 35.039  28.489  90.269  1.00 25.38  ? 463 MET A CA  1 
ATOM   3081  C  C   . MET A 1 462 ? 35.245  28.611  88.759  1.00 28.54  ? 463 MET A C   1 
ATOM   3082  O  O   . MET A 1 462 ? 36.247  29.170  88.302  1.00 32.74  ? 463 MET A O   1 
ATOM   3083  C  CB  . MET A 1 462 ? 35.461  27.102  90.755  1.00 35.41  ? 463 MET A CB  1 
ATOM   3084  C  CG  . MET A 1 462 ? 36.953  26.822  90.631  1.00 36.67  ? 463 MET A CG  1 
ATOM   3085  S  SD  . MET A 1 462 ? 37.970  27.935  91.619  1.00 34.86  ? 463 MET A SD  1 
ATOM   3086  C  CE  . MET A 1 462 ? 38.871  28.788  90.331  1.00 24.10  ? 463 MET A CE  1 
ATOM   3087  N  N   . THR A 1 463 ? 34.285  28.101  87.991  1.00 25.26  ? 464 THR A N   1 
ATOM   3088  C  CA  . THR A 1 463 ? 34.347  28.180  86.535  1.00 25.22  ? 464 THR A CA  1 
ATOM   3089  C  C   . THR A 1 463 ? 34.409  29.626  86.068  1.00 33.05  ? 464 THR A C   1 
ATOM   3090  O  O   . THR A 1 463 ? 35.234  29.976  85.221  1.00 32.13  ? 464 THR A O   1 
ATOM   3091  C  CB  . THR A 1 463 ? 33.141  27.500  85.872  1.00 25.51  ? 464 THR A CB  1 
ATOM   3092  O  OG1 . THR A 1 463 ? 33.059  26.138  86.306  1.00 25.11  ? 464 THR A OG1 1 
ATOM   3093  C  CG2 . THR A 1 463 ? 33.276  27.539  84.355  1.00 26.98  ? 464 THR A CG2 1 
ATOM   3094  N  N   . ASN A 1 464 ? 33.533  30.463  86.622  1.00 35.12  ? 465 ASN A N   1 
ATOM   3095  C  CA  . ASN A 1 464 ? 33.556  31.889  86.314  1.00 32.42  ? 465 ASN A CA  1 
ATOM   3096  C  C   . ASN A 1 464 ? 34.912  32.504  86.643  1.00 28.77  ? 465 ASN A C   1 
ATOM   3097  O  O   . ASN A 1 464 ? 35.487  33.238  85.825  1.00 29.60  ? 465 ASN A O   1 
ATOM   3098  C  CB  . ASN A 1 464 ? 32.446  32.623  87.069  1.00 36.61  ? 465 ASN A CB  1 
ATOM   3099  C  CG  . ASN A 1 464 ? 31.061  32.254  86.570  1.00 44.95  ? 465 ASN A CG  1 
ATOM   3100  O  OD1 . ASN A 1 464 ? 30.878  31.928  85.396  1.00 47.64  ? 465 ASN A OD1 1 
ATOM   3101  N  ND2 . ASN A 1 464 ? 30.078  32.306  87.461  1.00 45.52  ? 465 ASN A ND2 1 
ATOM   3102  N  N   . ARG A 1 465 ? 35.422  32.191  87.834  1.00 28.35  ? 466 ARG A N   1 
ATOM   3103  C  CA  . ARG A 1 465 ? 36.759  32.633  88.231  1.00 33.59  ? 466 ARG A CA  1 
ATOM   3104  C  C   . ARG A 1 465 ? 37.817  32.269  87.191  1.00 36.79  ? 466 ARG A C   1 
ATOM   3105  O  O   . ARG A 1 465 ? 38.698  33.071  86.888  1.00 36.42  ? 466 ARG A O   1 
ATOM   3106  C  CB  . ARG A 1 465 ? 37.162  32.030  89.579  1.00 36.70  ? 466 ARG A CB  1 
ATOM   3107  C  CG  . ARG A 1 465 ? 36.555  32.694  90.801  1.00 38.25  ? 466 ARG A CG  1 
ATOM   3108  C  CD  . ARG A 1 465 ? 37.421  32.411  92.023  1.00 47.81  ? 466 ARG A CD  1 
ATOM   3109  N  NE  . ARG A 1 465 ? 36.812  32.864  93.270  1.00 61.20  ? 466 ARG A NE  1 
ATOM   3110  C  CZ  . ARG A 1 465 ? 36.307  32.050  94.190  1.00 70.20  ? 466 ARG A CZ  1 
ATOM   3111  N  NH1 . ARG A 1 465 ? 36.340  30.737  94.006  1.00 71.72  ? 466 ARG A NH1 1 
ATOM   3112  N  NH2 . ARG A 1 465 ? 35.772  32.546  95.297  1.00 73.16  ? 466 ARG A NH2 1 
ATOM   3113  N  N   . LEU A 1 466 ? 37.726  31.057  86.651  1.00 30.49  ? 467 LEU A N   1 
ATOM   3114  C  CA  . LEU A 1 466 ? 38.713  30.575  85.687  1.00 36.55  ? 467 LEU A CA  1 
ATOM   3115  C  C   . LEU A 1 466 ? 38.548  31.181  84.298  1.00 29.94  ? 467 LEU A C   1 
ATOM   3116  O  O   . LEU A 1 466 ? 39.520  31.313  83.555  1.00 33.13  ? 467 LEU A O   1 
ATOM   3117  C  CB  . LEU A 1 466 ? 38.656  29.051  85.591  1.00 31.66  ? 467 LEU A CB  1 
ATOM   3118  C  CG  . LEU A 1 466 ? 39.414  28.305  86.686  1.00 34.25  ? 467 LEU A CG  1 
ATOM   3119  C  CD1 . LEU A 1 466 ? 38.688  27.033  87.060  1.00 34.96  ? 467 LEU A CD1 1 
ATOM   3120  C  CD2 . LEU A 1 466 ? 40.825  27.993  86.216  1.00 23.22  ? 467 LEU A CD2 1 
ATOM   3121  N  N   . ARG A 1 467 ? 37.320  31.538  83.939  1.00 33.09  ? 468 ARG A N   1 
ATOM   3122  C  CA  . ARG A 1 467 ? 37.079  32.193  82.660  1.00 35.14  ? 468 ARG A CA  1 
ATOM   3123  C  C   . ARG A 1 467 ? 37.616  33.620  82.713  1.00 33.55  ? 468 ARG A C   1 
ATOM   3124  O  O   . ARG A 1 467 ? 38.282  34.088  81.777  1.00 34.73  ? 468 ARG A O   1 
ATOM   3125  C  CB  . ARG A 1 467 ? 35.588  32.170  82.317  1.00 42.57  ? 468 ARG A CB  1 
ATOM   3126  C  CG  . ARG A 1 467 ? 35.078  30.775  81.985  1.00 50.19  ? 468 ARG A CG  1 
ATOM   3127  C  CD  . ARG A 1 467 ? 33.578  30.742  81.735  1.00 55.68  ? 468 ARG A CD  1 
ATOM   3128  N  NE  . ARG A 1 467 ? 33.151  29.427  81.259  1.00 62.71  ? 468 ARG A NE  1 
ATOM   3129  C  CZ  . ARG A 1 467 ? 31.885  29.024  81.196  1.00 67.04  ? 468 ARG A CZ  1 
ATOM   3130  N  NH1 . ARG A 1 467 ? 30.908  29.831  81.584  1.00 70.44  ? 468 ARG A NH1 1 
ATOM   3131  N  NH2 . ARG A 1 467 ? 31.598  27.809  80.747  1.00 62.84  ? 468 ARG A NH2 1 
ATOM   3132  N  N   . SER A 1 468 ? 37.343  34.299  83.824  1.00 34.90  ? 469 SER A N   1 
ATOM   3133  C  CA  . SER A 1 468 ? 37.891  35.633  84.043  1.00 42.80  ? 469 SER A CA  1 
ATOM   3134  C  C   . SER A 1 468 ? 39.416  35.588  84.068  1.00 40.42  ? 469 SER A C   1 
ATOM   3135  O  O   . SER A 1 468 ? 40.078  36.416  83.444  1.00 41.33  ? 469 SER A O   1 
ATOM   3136  C  CB  . SER A 1 468 ? 37.357  36.231  85.345  1.00 39.35  ? 469 SER A CB  1 
ATOM   3137  O  OG  . SER A 1 468 ? 35.963  36.464  85.258  1.00 45.76  ? 469 SER A OG  1 
ATOM   3138  N  N   . ALA A 1 469 ? 39.963  34.613  84.787  1.00 34.42  ? 470 ALA A N   1 
ATOM   3139  C  CA  . ALA A 1 469 ? 41.408  34.423  84.864  1.00 33.15  ? 470 ALA A CA  1 
ATOM   3140  C  C   . ALA A 1 469 ? 41.997  34.197  83.478  1.00 34.59  ? 470 ALA A C   1 
ATOM   3141  O  O   . ALA A 1 469 ? 43.069  34.710  83.157  1.00 36.05  ? 470 ALA A O   1 
ATOM   3142  C  CB  . ALA A 1 469 ? 41.745  33.258  85.778  1.00 26.78  ? 470 ALA A CB  1 
ATOM   3143  N  N   . TYR A 1 470 ? 41.288  33.426  82.661  1.00 32.75  ? 471 TYR A N   1 
ATOM   3144  C  CA  . TYR A 1 470 ? 41.720  33.176  81.294  1.00 36.47  ? 471 TYR A CA  1 
ATOM   3145  C  C   . TYR A 1 470 ? 41.737  34.468  80.493  1.00 42.34  ? 471 TYR A C   1 
ATOM   3146  O  O   . TYR A 1 470 ? 42.653  34.704  79.706  1.00 41.04  ? 471 TYR A O   1 
ATOM   3147  C  CB  . TYR A 1 470 ? 40.815  32.152  80.611  1.00 37.40  ? 471 TYR A CB  1 
ATOM   3148  C  CG  . TYR A 1 470 ? 41.311  31.742  79.243  1.00 36.13  ? 471 TYR A CG  1 
ATOM   3149  C  CD1 . TYR A 1 470 ? 42.261  30.739  79.102  1.00 33.20  ? 471 TYR A CD1 1 
ATOM   3150  C  CD2 . TYR A 1 470 ? 40.840  32.366  78.094  1.00 34.95  ? 471 TYR A CD2 1 
ATOM   3151  C  CE1 . TYR A 1 470 ? 42.722  30.362  77.855  1.00 32.28  ? 471 TYR A CE1 1 
ATOM   3152  C  CE2 . TYR A 1 470 ? 41.296  31.996  76.843  1.00 41.10  ? 471 TYR A CE2 1 
ATOM   3153  C  CZ  . TYR A 1 470 ? 42.236  30.992  76.730  1.00 34.99  ? 471 TYR A CZ  1 
ATOM   3154  O  OH  . TYR A 1 470 ? 42.693  30.618  75.488  1.00 38.36  ? 471 TYR A OH  1 
ATOM   3155  N  N   . ASN A 1 471 ? 40.720  35.302  80.691  1.00 48.39  ? 472 ASN A N   1 
ATOM   3156  C  CA  . ASN A 1 471 ? 40.676  36.588  80.004  1.00 55.86  ? 472 ASN A CA  1 
ATOM   3157  C  C   . ASN A 1 471 ? 41.578  37.628  80.664  1.00 65.34  ? 472 ASN A C   1 
ATOM   3158  O  O   . ASN A 1 471 ? 42.294  38.364  79.983  1.00 64.07  ? 472 ASN A O   1 
ATOM   3159  C  CB  . ASN A 1 471 ? 39.240  37.107  79.938  1.00 58.21  ? 472 ASN A CB  1 
ATOM   3160  C  CG  . ASN A 1 471 ? 38.336  36.201  79.130  1.00 61.27  ? 472 ASN A CG  1 
ATOM   3161  O  OD1 . ASN A 1 471 ? 38.801  35.449  78.272  1.00 56.87  ? 472 ASN A OD1 1 
ATOM   3162  N  ND2 . ASN A 1 471 ? 37.036  36.268  79.396  1.00 59.03  ? 472 ASN A ND2 1 
ATOM   3163  N  N   . GLY A 1 472 ? 41.544  37.681  81.992  1.00 75.31  ? 473 GLY A N   1 
ATOM   3164  C  CA  . GLY A 1 472 ? 42.351  38.630  82.736  1.00 79.06  ? 473 GLY A CA  1 
ATOM   3165  C  C   . GLY A 1 472 ? 41.549  39.828  83.205  1.00 81.86  ? 473 GLY A C   1 
ATOM   3166  O  O   . GLY A 1 472 ? 40.319  39.792  83.233  1.00 83.11  ? 473 GLY A O   1 
ATOM   3167  N  N   . SER B 1 28  ? -0.022  61.663  47.729  1.00 73.44  ? 29  SER B N   1 
ATOM   3168  C  CA  . SER B 1 28  ? 0.073   61.530  46.280  1.00 74.74  ? 29  SER B CA  1 
ATOM   3169  C  C   . SER B 1 28  ? -0.113  60.078  45.847  1.00 72.13  ? 29  SER B C   1 
ATOM   3170  O  O   . SER B 1 28  ? 0.368   59.156  46.505  1.00 70.12  ? 29  SER B O   1 
ATOM   3171  C  CB  . SER B 1 28  ? 1.417   62.063  45.780  1.00 77.55  ? 29  SER B CB  1 
ATOM   3172  O  OG  . SER B 1 28  ? 1.479   62.036  44.365  1.00 80.50  ? 29  SER B OG  1 
ATOM   3173  N  N   . ARG B 1 29  ? -0.818  59.887  44.737  1.00 72.73  ? 30  ARG B N   1 
ATOM   3174  C  CA  . ARG B 1 29  ? -1.142  58.554  44.238  1.00 69.69  ? 30  ARG B CA  1 
ATOM   3175  C  C   . ARG B 1 29  ? -0.147  58.046  43.197  1.00 69.69  ? 30  ARG B C   1 
ATOM   3176  O  O   . ARG B 1 29  ? -0.343  56.978  42.616  1.00 69.78  ? 30  ARG B O   1 
ATOM   3177  C  CB  . ARG B 1 29  ? -2.556  58.542  43.657  1.00 68.13  ? 30  ARG B CB  1 
ATOM   3178  C  CG  . ARG B 1 29  ? -3.630  58.837  44.688  1.00 63.24  ? 30  ARG B CG  1 
ATOM   3179  C  CD  . ARG B 1 29  ? -4.994  58.991  44.048  1.00 64.39  ? 30  ARG B CD  1 
ATOM   3180  N  NE  . ARG B 1 29  ? -5.998  59.409  45.021  1.00 66.24  ? 30  ARG B NE  1 
ATOM   3181  C  CZ  . ARG B 1 29  ? -7.286  59.580  44.739  1.00 68.34  ? 30  ARG B CZ  1 
ATOM   3182  N  NH1 . ARG B 1 29  ? -8.129  59.959  45.689  1.00 70.65  ? 30  ARG B NH1 1 
ATOM   3183  N  NH2 . ARG B 1 29  ? -7.730  59.367  43.509  1.00 71.05  ? 30  ARG B NH2 1 
ATOM   3184  N  N   . SER B 1 30  ? 0.906   58.819  42.952  1.00 64.33  ? 31  SER B N   1 
ATOM   3185  C  CA  . SER B 1 30  ? 1.936   58.426  41.994  1.00 70.19  ? 31  SER B CA  1 
ATOM   3186  C  C   . SER B 1 30  ? 2.613   57.123  42.413  1.00 67.21  ? 31  SER B C   1 
ATOM   3187  O  O   . SER B 1 30  ? 2.721   56.822  43.602  1.00 61.30  ? 31  SER B O   1 
ATOM   3188  C  CB  . SER B 1 30  ? 2.981   59.533  41.842  1.00 71.13  ? 31  SER B CB  1 
ATOM   3189  O  OG  . SER B 1 30  ? 4.050   59.111  41.014  1.00 73.71  ? 31  SER B OG  1 
ATOM   3190  N  N   . CYS B 1 31  ? 3.062   56.352  41.428  1.00 71.79  ? 32  CYS B N   1 
ATOM   3191  C  CA  . CYS B 1 31  ? 3.671   55.053  41.687  1.00 71.28  ? 32  CYS B CA  1 
ATOM   3192  C  C   . CYS B 1 31  ? 5.165   55.058  41.375  1.00 76.34  ? 32  CYS B C   1 
ATOM   3193  O  O   . CYS B 1 31  ? 5.726   54.039  40.970  1.00 80.63  ? 32  CYS B O   1 
ATOM   3194  C  CB  . CYS B 1 31  ? 2.971   53.968  40.866  1.00 70.41  ? 32  CYS B CB  1 
ATOM   3195  S  SG  . CYS B 1 31  ? 1.247   53.686  41.323  1.00 69.86  ? 32  CYS B SG  1 
ATOM   3196  N  N   . GLY B 1 32  ? 5.801   56.209  41.571  1.00 78.65  ? 33  GLY B N   1 
ATOM   3197  C  CA  . GLY B 1 32  ? 7.209   56.378  41.259  1.00 79.07  ? 33  GLY B CA  1 
ATOM   3198  C  C   . GLY B 1 32  ? 8.140   55.449  42.016  1.00 74.10  ? 33  GLY B C   1 
ATOM   3199  O  O   . GLY B 1 32  ? 9.047   54.864  41.428  1.00 76.91  ? 33  GLY B O   1 
ATOM   3200  N  N   . GLU B 1 33  ? 7.920   55.316  43.320  1.00 73.58  ? 34  GLU B N   1 
ATOM   3201  C  CA  . GLU B 1 33  ? 8.743   54.445  44.155  1.00 75.27  ? 34  GLU B CA  1 
ATOM   3202  C  C   . GLU B 1 33  ? 8.564   52.979  43.782  1.00 74.51  ? 34  GLU B C   1 
ATOM   3203  O  O   . GLU B 1 33  ? 9.530   52.210  43.734  1.00 74.71  ? 34  GLU B O   1 
ATOM   3204  C  CB  . GLU B 1 33  ? 8.407   54.645  45.633  1.00 78.76  ? 34  GLU B CB  1 
ATOM   3205  C  CG  . GLU B 1 33  ? 9.076   55.846  46.271  1.00 83.60  ? 34  GLU B CG  1 
ATOM   3206  C  CD  . GLU B 1 33  ? 8.622   56.065  47.699  1.00 86.22  ? 34  GLU B CD  1 
ATOM   3207  O  OE1 . GLU B 1 33  ? 7.396   56.081  47.937  1.00 87.53  ? 34  GLU B OE1 1 
ATOM   3208  O  OE2 . GLU B 1 33  ? 9.492   56.212  48.584  1.00 85.80  ? 34  GLU B OE2 1 
ATOM   3209  N  N   . VAL B 1 34  ? 7.319   52.595  43.526  1.00 70.06  ? 35  VAL B N   1 
ATOM   3210  C  CA  . VAL B 1 34  ? 7.011   51.228  43.136  1.00 66.97  ? 35  VAL B CA  1 
ATOM   3211  C  C   . VAL B 1 34  ? 7.649   50.922  41.786  1.00 71.41  ? 35  VAL B C   1 
ATOM   3212  O  O   . VAL B 1 34  ? 8.086   49.802  41.541  1.00 62.91  ? 35  VAL B O   1 
ATOM   3213  C  CB  . VAL B 1 34  ? 5.493   50.990  43.077  1.00 68.32  ? 35  VAL B CB  1 
ATOM   3214  C  CG1 . VAL B 1 34  ? 5.186   49.559  42.660  1.00 63.84  ? 35  VAL B CG1 1 
ATOM   3215  C  CG2 . VAL B 1 34  ? 4.869   51.297  44.428  1.00 67.88  ? 35  VAL B CG2 1 
ATOM   3216  N  N   . ARG B 1 35  ? 7.718   51.927  40.919  1.00 71.19  ? 36  ARG B N   1 
ATOM   3217  C  CA  . ARG B 1 35  ? 8.404   51.781  39.640  1.00 77.64  ? 36  ARG B CA  1 
ATOM   3218  C  C   . ARG B 1 35  ? 9.903   51.598  39.865  1.00 79.54  ? 36  ARG B C   1 
ATOM   3219  O  O   . ARG B 1 35  ? 10.536  50.732  39.254  1.00 78.55  ? 36  ARG B O   1 
ATOM   3220  C  CB  . ARG B 1 35  ? 8.140   52.993  38.745  1.00 63.19  ? 36  ARG B CB  1 
ATOM   3221  N  N   . GLN B 1 36  ? 10.455  52.427  40.746  1.00 86.01  ? 37  GLN B N   1 
ATOM   3222  C  CA  . GLN B 1 36  ? 11.846  52.337  41.173  1.00 94.84  ? 37  GLN B CA  1 
ATOM   3223  C  C   . GLN B 1 36  ? 12.224  50.919  41.579  1.00 92.39  ? 37  GLN B C   1 
ATOM   3224  O  O   . GLN B 1 36  ? 13.152  50.317  41.028  1.00 94.58  ? 37  GLN B O   1 
ATOM   3225  C  CB  . GLN B 1 36  ? 12.081  53.294  42.342  1.00 103.00 ? 37  GLN B CB  1 
ATOM   3226  C  CG  . GLN B 1 36  ? 13.490  53.332  42.885  1.00 110.08 ? 37  GLN B CG  1 
ATOM   3227  C  CD  . GLN B 1 36  ? 13.610  54.288  44.051  1.00 115.60 ? 37  GLN B CD  1 
ATOM   3228  O  OE1 . GLN B 1 36  ? 13.340  55.482  43.918  1.00 117.58 ? 37  GLN B OE1 1 
ATOM   3229  N  NE2 . GLN B 1 36  ? 14.008  53.767  45.208  1.00 115.67 ? 37  GLN B NE2 1 
ATOM   3230  N  N   . ILE B 1 37  ? 11.472  50.391  42.538  1.00 90.70  ? 38  ILE B N   1 
ATOM   3231  C  CA  . ILE B 1 37  ? 11.752  49.088  43.128  1.00 86.97  ? 38  ILE B CA  1 
ATOM   3232  C  C   . ILE B 1 37  ? 11.466  47.924  42.173  1.00 85.75  ? 38  ILE B C   1 
ATOM   3233  O  O   . ILE B 1 37  ? 12.252  46.980  42.087  1.00 85.69  ? 38  ILE B O   1 
ATOM   3234  C  CB  . ILE B 1 37  ? 10.939  48.909  44.421  1.00 86.17  ? 38  ILE B CB  1 
ATOM   3235  C  CG1 . ILE B 1 37  ? 11.366  49.962  45.445  1.00 86.73  ? 38  ILE B CG1 1 
ATOM   3236  C  CG2 . ILE B 1 37  ? 11.128  47.517  44.989  1.00 85.22  ? 38  ILE B CG2 1 
ATOM   3237  C  CD1 . ILE B 1 37  ? 10.505  50.002  46.676  1.00 86.07  ? 38  ILE B CD1 1 
ATOM   3238  N  N   . TYR B 1 38  ? 10.345  47.996  41.460  1.00 83.50  ? 39  TYR B N   1 
ATOM   3239  C  CA  . TYR B 1 38  ? 9.971   46.964  40.492  1.00 81.71  ? 39  TYR B CA  1 
ATOM   3240  C  C   . TYR B 1 38  ? 11.002  46.877  39.375  1.00 83.77  ? 39  TYR B C   1 
ATOM   3241  O  O   . TYR B 1 38  ? 11.275  45.798  38.849  1.00 83.01  ? 39  TYR B O   1 
ATOM   3242  C  CB  . TYR B 1 38  ? 8.583   47.255  39.911  1.00 74.38  ? 39  TYR B CB  1 
ATOM   3243  C  CG  . TYR B 1 38  ? 7.915   46.091  39.208  1.00 70.73  ? 39  TYR B CG  1 
ATOM   3244  C  CD1 . TYR B 1 38  ? 7.558   44.944  39.904  1.00 63.53  ? 39  TYR B CD1 1 
ATOM   3245  C  CD2 . TYR B 1 38  ? 7.605   46.158  37.854  1.00 69.77  ? 39  TYR B CD2 1 
ATOM   3246  C  CE1 . TYR B 1 38  ? 6.934   43.885  39.267  1.00 63.41  ? 39  TYR B CE1 1 
ATOM   3247  C  CE2 . TYR B 1 38  ? 6.978   45.107  37.210  1.00 66.58  ? 39  TYR B CE2 1 
ATOM   3248  C  CZ  . TYR B 1 38  ? 6.647   43.973  37.920  1.00 64.26  ? 39  TYR B CZ  1 
ATOM   3249  O  OH  . TYR B 1 38  ? 6.026   42.924  37.282  1.00 66.01  ? 39  TYR B OH  1 
ATOM   3250  N  N   . GLY B 1 39  ? 11.576  48.024  39.021  1.00 92.01  ? 40  GLY B N   1 
ATOM   3251  C  CA  . GLY B 1 39  ? 12.595  48.080  37.990  1.00 98.60  ? 40  GLY B CA  1 
ATOM   3252  C  C   . GLY B 1 39  ? 13.951  47.617  38.487  1.00 100.01 ? 40  GLY B C   1 
ATOM   3253  O  O   . GLY B 1 39  ? 14.695  46.960  37.759  1.00 105.29 ? 40  GLY B O   1 
ATOM   3254  N  N   . ALA B 1 40  ? 14.273  47.957  39.731  1.00 98.82  ? 41  ALA B N   1 
ATOM   3255  C  CA  . ALA B 1 40  ? 15.555  47.575  40.319  1.00 94.41  ? 41  ALA B CA  1 
ATOM   3256  C  C   . ALA B 1 40  ? 15.694  46.060  40.463  1.00 87.40  ? 41  ALA B C   1 
ATOM   3257  O  O   . ALA B 1 40  ? 16.805  45.539  40.553  1.00 86.98  ? 41  ALA B O   1 
ATOM   3258  C  CB  . ALA B 1 40  ? 15.732  48.248  41.671  1.00 94.79  ? 41  ALA B CB  1 
ATOM   3259  N  N   . LYS B 1 41  ? 14.565  45.359  40.480  1.00 87.28  ? 42  LYS B N   1 
ATOM   3260  C  CA  . LYS B 1 41  ? 14.568  43.911  40.654  1.00 87.28  ? 42  LYS B CA  1 
ATOM   3261  C  C   . LYS B 1 41  ? 14.490  43.179  39.316  1.00 89.45  ? 42  LYS B C   1 
ATOM   3262  O  O   . LYS B 1 41  ? 14.331  41.958  39.273  1.00 88.67  ? 42  LYS B O   1 
ATOM   3263  C  CB  . LYS B 1 41  ? 13.416  43.486  41.566  1.00 84.21  ? 42  LYS B CB  1 
ATOM   3264  C  CG  . LYS B 1 41  ? 13.513  44.080  42.961  1.00 82.73  ? 42  LYS B CG  1 
ATOM   3265  C  CD  . LYS B 1 41  ? 12.380  43.621  43.860  1.00 78.49  ? 42  LYS B CD  1 
ATOM   3266  C  CE  . LYS B 1 41  ? 12.518  44.227  45.246  1.00 74.88  ? 42  LYS B CE  1 
ATOM   3267  N  NZ  . LYS B 1 41  ? 13.817  43.872  45.884  1.00 72.74  ? 42  LYS B NZ  1 
ATOM   3268  N  N   . GLY B 1 42  ? 14.603  43.933  38.227  1.00 96.97  ? 43  GLY B N   1 
ATOM   3269  C  CA  . GLY B 1 42  ? 14.740  43.347  36.905  1.00 99.78  ? 43  GLY B CA  1 
ATOM   3270  C  C   . GLY B 1 42  ? 13.516  43.376  36.008  1.00 98.42  ? 43  GLY B C   1 
ATOM   3271  O  O   . GLY B 1 42  ? 13.639  43.221  34.793  1.00 104.68 ? 43  GLY B O   1 
ATOM   3272  N  N   . PHE B 1 43  ? 12.337  43.571  36.589  1.00 94.03  ? 44  PHE B N   1 
ATOM   3273  C  CA  . PHE B 1 43  ? 11.116  43.626  35.793  1.00 90.12  ? 44  PHE B CA  1 
ATOM   3274  C  C   . PHE B 1 43  ? 11.033  44.945  35.027  1.00 86.13  ? 44  PHE B C   1 
ATOM   3275  O  O   . PHE B 1 43  ? 11.466  45.985  35.522  1.00 85.64  ? 44  PHE B O   1 
ATOM   3276  C  CB  . PHE B 1 43  ? 9.880   43.449  36.675  1.00 88.42  ? 44  PHE B CB  1 
ATOM   3277  C  CG  . PHE B 1 43  ? 9.903   42.201  37.512  1.00 85.91  ? 44  PHE B CG  1 
ATOM   3278  C  CD1 . PHE B 1 43  ? 9.642   40.965  36.944  1.00 86.71  ? 44  PHE B CD1 1 
ATOM   3279  C  CD2 . PHE B 1 43  ? 10.167  42.267  38.870  1.00 83.77  ? 44  PHE B CD2 1 
ATOM   3280  C  CE1 . PHE B 1 43  ? 9.661   39.816  37.712  1.00 84.99  ? 44  PHE B CE1 1 
ATOM   3281  C  CE2 . PHE B 1 43  ? 10.184  41.122  39.644  1.00 82.92  ? 44  PHE B CE2 1 
ATOM   3282  C  CZ  . PHE B 1 43  ? 9.930   39.895  39.065  1.00 82.80  ? 44  PHE B CZ  1 
ATOM   3283  N  N   . SER B 1 44  ? 10.477  44.896  33.820  1.00 84.64  ? 45  SER B N   1 
ATOM   3284  C  CA  . SER B 1 44  ? 10.369  46.084  32.978  1.00 84.48  ? 45  SER B CA  1 
ATOM   3285  C  C   . SER B 1 44  ? 9.199   46.970  33.405  1.00 83.39  ? 45  SER B C   1 
ATOM   3286  O  O   . SER B 1 44  ? 8.174   46.478  33.880  1.00 80.51  ? 45  SER B O   1 
ATOM   3287  C  CB  . SER B 1 44  ? 10.226  45.685  31.508  1.00 87.49  ? 45  SER B CB  1 
ATOM   3288  O  OG  . SER B 1 44  ? 11.301  44.856  31.101  1.00 89.03  ? 45  SER B OG  1 
ATOM   3289  N  N   . LEU B 1 45  ? 9.359   48.277  33.223  1.00 82.03  ? 46  LEU B N   1 
ATOM   3290  C  CA  . LEU B 1 45  ? 8.402   49.257  33.733  1.00 84.19  ? 46  LEU B CA  1 
ATOM   3291  C  C   . LEU B 1 45  ? 7.158   49.407  32.863  1.00 86.77  ? 46  LEU B C   1 
ATOM   3292  O  O   . LEU B 1 45  ? 6.246   50.156  33.205  1.00 89.13  ? 46  LEU B O   1 
ATOM   3293  C  CB  . LEU B 1 45  ? 9.073   50.626  33.882  1.00 81.19  ? 46  LEU B CB  1 
ATOM   3294  C  CG  . LEU B 1 45  ? 10.291  50.748  34.799  1.00 77.21  ? 46  LEU B CG  1 
ATOM   3295  C  CD1 . LEU B 1 45  ? 11.585  50.519  34.030  1.00 73.34  ? 46  LEU B CD1 1 
ATOM   3296  C  CD2 . LEU B 1 45  ? 10.304  52.107  35.483  1.00 78.25  ? 46  LEU B CD2 1 
ATOM   3297  N  N   . SER B 1 46  ? 7.115   48.701  31.741  1.00 94.04  ? 47  SER B N   1 
ATOM   3298  C  CA  . SER B 1 46  ? 5.994   48.832  30.816  1.00 99.24  ? 47  SER B CA  1 
ATOM   3299  C  C   . SER B 1 46  ? 4.678   48.374  31.443  1.00 99.33  ? 47  SER B C   1 
ATOM   3300  O  O   . SER B 1 46  ? 3.598   48.740  30.979  1.00 98.70  ? 47  SER B O   1 
ATOM   3301  C  CB  . SER B 1 46  ? 6.268   48.039  29.539  1.00 103.67 ? 47  SER B CB  1 
ATOM   3302  O  OG  . SER B 1 46  ? 6.262   46.645  29.789  1.00 103.28 ? 47  SER B OG  1 
ATOM   3303  N  N   . ASP B 1 47  ? 4.776   47.580  32.505  1.00 98.37  ? 48  ASP B N   1 
ATOM   3304  C  CA  . ASP B 1 47  ? 3.593   47.035  33.160  1.00 98.86  ? 48  ASP B CA  1 
ATOM   3305  C  C   . ASP B 1 47  ? 3.234   47.767  34.452  1.00 95.26  ? 48  ASP B C   1 
ATOM   3306  O  O   . ASP B 1 47  ? 2.152   47.557  34.999  1.00 96.74  ? 48  ASP B O   1 
ATOM   3307  C  CB  . ASP B 1 47  ? 3.790   45.544  33.449  1.00 102.83 ? 48  ASP B CB  1 
ATOM   3308  C  CG  . ASP B 1 47  ? 3.778   44.699  32.189  1.00 107.04 ? 48  ASP B CG  1 
ATOM   3309  O  OD1 . ASP B 1 47  ? 3.331   45.203  31.137  1.00 110.83 ? 48  ASP B OD1 1 
ATOM   3310  O  OD2 . ASP B 1 47  ? 4.217   43.531  32.251  1.00 105.41 ? 48  ASP B OD2 1 
ATOM   3311  N  N   . VAL B 1 48  ? 4.128   48.619  34.947  1.00 88.84  ? 49  VAL B N   1 
ATOM   3312  C  CA  . VAL B 1 48  ? 3.819   49.376  36.158  1.00 83.17  ? 49  VAL B CA  1 
ATOM   3313  C  C   . VAL B 1 48  ? 2.943   50.584  35.820  1.00 80.26  ? 49  VAL B C   1 
ATOM   3314  O  O   . VAL B 1 48  ? 3.227   51.334  34.883  1.00 80.23  ? 49  VAL B O   1 
ATOM   3315  C  CB  . VAL B 1 48  ? 5.102   49.824  36.926  1.00 102.32 ? 49  VAL B CB  1 
ATOM   3316  C  CG1 . VAL B 1 48  ? 5.904   50.853  36.149  1.00 103.75 ? 49  VAL B CG1 1 
ATOM   3317  C  CG2 . VAL B 1 48  ? 4.734   50.383  38.292  1.00 100.98 ? 49  VAL B CG2 1 
ATOM   3318  N  N   . PRO B 1 49  ? 1.836   50.742  36.558  1.00 76.43  ? 50  PRO B N   1 
ATOM   3319  C  CA  . PRO B 1 49  ? 0.923   51.875  36.387  1.00 77.14  ? 50  PRO B CA  1 
ATOM   3320  C  C   . PRO B 1 49  ? 1.552   53.212  36.766  1.00 80.08  ? 50  PRO B C   1 
ATOM   3321  O  O   . PRO B 1 49  ? 2.494   53.268  37.557  1.00 80.49  ? 50  PRO B O   1 
ATOM   3322  C  CB  . PRO B 1 49  ? -0.235  51.538  37.332  1.00 73.51  ? 50  PRO B CB  1 
ATOM   3323  C  CG  . PRO B 1 49  ? -0.195  50.057  37.458  1.00 73.00  ? 50  PRO B CG  1 
ATOM   3324  C  CD  . PRO B 1 49  ? 1.260   49.704  37.429  1.00 72.20  ? 50  PRO B CD  1 
ATOM   3325  N  N   . GLN B 1 50  ? 1.016   54.279  36.186  1.00 84.82  ? 51  GLN B N   1 
ATOM   3326  C  CA  . GLN B 1 50  ? 1.467   55.635  36.457  1.00 84.47  ? 51  GLN B CA  1 
ATOM   3327  C  C   . GLN B 1 50  ? 0.938   56.095  37.809  1.00 81.54  ? 51  GLN B C   1 
ATOM   3328  O  O   . GLN B 1 50  ? 1.657   56.706  38.601  1.00 77.93  ? 51  GLN B O   1 
ATOM   3329  C  CB  . GLN B 1 50  ? 1.002   56.589  35.350  1.00 96.93  ? 51  GLN B CB  1 
ATOM   3330  C  CG  . GLN B 1 50  ? 0.919   55.968  33.953  1.00 105.16 ? 51  GLN B CG  1 
ATOM   3331  C  CD  . GLN B 1 50  ? -0.311  55.091  33.759  1.00 110.56 ? 51  GLN B CD  1 
ATOM   3332  O  OE1 . GLN B 1 50  ? -1.182  55.021  34.627  1.00 111.26 ? 51  GLN B OE1 1 
ATOM   3333  N  NE2 . GLN B 1 50  ? -0.377  54.408  32.622  1.00 113.86 ? 51  GLN B NE2 1 
ATOM   3334  N  N   . ALA B 1 51  ? -0.330  55.787  38.061  1.00 75.59  ? 52  ALA B N   1 
ATOM   3335  C  CA  . ALA B 1 51  ? -0.987  56.134  39.314  1.00 73.76  ? 52  ALA B CA  1 
ATOM   3336  C  C   . ALA B 1 51  ? -1.772  54.937  39.838  1.00 64.22  ? 52  ALA B C   1 
ATOM   3337  O  O   . ALA B 1 51  ? -1.975  53.960  39.117  1.00 65.44  ? 52  ALA B O   1 
ATOM   3338  C  CB  . ALA B 1 51  ? -1.900  57.336  39.126  1.00 67.55  ? 52  ALA B CB  1 
ATOM   3339  N  N   . GLU B 1 52  ? -2.208  55.019  41.092  1.00 62.88  ? 53  GLU B N   1 
ATOM   3340  C  CA  . GLU B 1 52  ? -2.912  53.916  41.740  1.00 61.28  ? 53  GLU B CA  1 
ATOM   3341  C  C   . GLU B 1 52  ? -4.190  53.514  41.009  1.00 65.63  ? 53  GLU B C   1 
ATOM   3342  O  O   . GLU B 1 52  ? -4.866  54.344  40.402  1.00 74.25  ? 53  GLU B O   1 
ATOM   3343  C  CB  . GLU B 1 52  ? -3.248  54.278  43.189  1.00 60.11  ? 53  GLU B CB  1 
ATOM   3344  C  CG  . GLU B 1 52  ? -2.038  54.522  44.070  1.00 59.11  ? 53  GLU B CG  1 
ATOM   3345  C  CD  . GLU B 1 52  ? -2.419  54.809  45.509  1.00 75.62  ? 53  GLU B CD  1 
ATOM   3346  O  OE1 . GLU B 1 52  ? -3.627  54.776  45.823  1.00 77.15  ? 53  GLU B OE1 1 
ATOM   3347  O  OE2 . GLU B 1 52  ? -1.511  55.068  46.328  1.00 76.45  ? 53  GLU B OE2 1 
ATOM   3348  N  N   . ILE B 1 53  ? -4.502  52.223  41.072  1.00 66.60  ? 54  ILE B N   1 
ATOM   3349  C  CA  . ILE B 1 53  ? -5.693  51.664  40.445  1.00 62.94  ? 54  ILE B CA  1 
ATOM   3350  C  C   . ILE B 1 53  ? -6.408  50.803  41.489  1.00 61.86  ? 54  ILE B C   1 
ATOM   3351  O  O   . ILE B 1 53  ? -5.785  50.367  42.457  1.00 59.84  ? 54  ILE B O   1 
ATOM   3352  C  CB  . ILE B 1 53  ? -5.329  50.831  39.187  1.00 84.45  ? 54  ILE B CB  1 
ATOM   3353  C  CG1 . ILE B 1 53  ? -4.509  51.676  38.209  1.00 86.68  ? 54  ILE B CG1 1 
ATOM   3354  C  CG2 . ILE B 1 53  ? -6.573  50.308  38.478  1.00 86.01  ? 54  ILE B CG2 1 
ATOM   3355  C  CD1 . ILE B 1 53  ? -4.215  50.986  36.895  1.00 89.28  ? 54  ILE B CD1 1 
ATOM   3356  N  N   . SER B 1 54  ? -7.710  50.586  41.311  1.00 65.81  ? 55  SER B N   1 
ATOM   3357  C  CA  . SER B 1 54  ? -8.491  49.743  42.215  1.00 68.88  ? 55  SER B CA  1 
ATOM   3358  C  C   . SER B 1 54  ? -7.853  48.368  42.395  1.00 72.05  ? 55  SER B C   1 
ATOM   3359  O  O   . SER B 1 54  ? -7.297  47.804  41.453  1.00 70.99  ? 55  SER B O   1 
ATOM   3360  C  CB  . SER B 1 54  ? -9.922  49.587  41.696  1.00 74.64  ? 55  SER B CB  1 
ATOM   3361  O  OG  . SER B 1 54  ? -9.932  49.027  40.393  1.00 77.57  ? 55  SER B OG  1 
ATOM   3362  N  N   . GLY B 1 55  ? -7.935  47.834  43.610  1.00 70.50  ? 56  GLY B N   1 
ATOM   3363  C  CA  . GLY B 1 55  ? -7.312  46.561  43.926  1.00 71.13  ? 56  GLY B CA  1 
ATOM   3364  C  C   . GLY B 1 55  ? -8.245  45.376  43.788  1.00 72.59  ? 56  GLY B C   1 
ATOM   3365  O  O   . GLY B 1 55  ? -8.132  44.398  44.529  1.00 73.41  ? 56  GLY B O   1 
ATOM   3366  N  N   . GLU B 1 56  ? -9.163  45.465  42.832  1.00 77.10  ? 57  GLU B N   1 
ATOM   3367  C  CA  . GLU B 1 56  ? -10.130 44.404  42.571  1.00 80.38  ? 57  GLU B CA  1 
ATOM   3368  C  C   . GLU B 1 56  ? -9.466  43.112  42.097  1.00 80.68  ? 57  GLU B C   1 
ATOM   3369  O  O   . GLU B 1 56  ? -9.978  42.016  42.325  1.00 79.40  ? 57  GLU B O   1 
ATOM   3370  C  CB  . GLU B 1 56  ? -11.155 44.874  41.533  1.00 89.26  ? 57  GLU B CB  1 
ATOM   3371  C  CG  . GLU B 1 56  ? -10.550 45.649  40.362  1.00 96.83  ? 57  GLU B CG  1 
ATOM   3372  C  CD  . GLU B 1 56  ? -11.554 45.919  39.256  1.00 104.33 ? 57  GLU B CD  1 
ATOM   3373  O  OE1 . GLU B 1 56  ? -12.578 45.207  39.193  1.00 106.36 ? 57  GLU B OE1 1 
ATOM   3374  O  OE2 . GLU B 1 56  ? -11.326 46.852  38.456  1.00 104.99 ? 57  GLU B OE2 1 
ATOM   3375  N  N   . HIS B 1 57  ? -8.316  43.251  41.448  1.00 79.69  ? 58  HIS B N   1 
ATOM   3376  C  CA  . HIS B 1 57  ? -7.635  42.119  40.830  1.00 78.02  ? 58  HIS B CA  1 
ATOM   3377  C  C   . HIS B 1 57  ? -6.572  41.489  41.729  1.00 76.59  ? 58  HIS B C   1 
ATOM   3378  O  O   . HIS B 1 57  ? -5.925  40.517  41.340  1.00 77.86  ? 58  HIS B O   1 
ATOM   3379  C  CB  . HIS B 1 57  ? -6.989  42.554  39.515  1.00 78.86  ? 58  HIS B CB  1 
ATOM   3380  C  CG  . HIS B 1 57  ? -5.949  43.618  39.681  1.00 77.40  ? 58  HIS B CG  1 
ATOM   3381  N  ND1 . HIS B 1 57  ? -6.266  44.947  39.861  1.00 74.84  ? 58  HIS B ND1 1 
ATOM   3382  C  CD2 . HIS B 1 57  ? -4.598  43.546  39.711  1.00 79.53  ? 58  HIS B CD2 1 
ATOM   3383  C  CE1 . HIS B 1 57  ? -5.154  45.650  39.984  1.00 75.82  ? 58  HIS B CE1 1 
ATOM   3384  N  NE2 . HIS B 1 57  ? -4.128  44.823  39.898  1.00 78.09  ? 58  HIS B NE2 1 
ATOM   3385  N  N   . LEU B 1 58  ? -6.389  42.043  42.924  1.00 71.88  ? 59  LEU B N   1 
ATOM   3386  C  CA  . LEU B 1 58  ? -5.354  41.557  43.835  1.00 66.86  ? 59  LEU B CA  1 
ATOM   3387  C  C   . LEU B 1 58  ? -5.673  40.162  44.371  1.00 66.85  ? 59  LEU B C   1 
ATOM   3388  O  O   . LEU B 1 58  ? -6.610  39.983  45.148  1.00 68.15  ? 59  LEU B O   1 
ATOM   3389  C  CB  . LEU B 1 58  ? -5.164  42.535  44.995  1.00 62.81  ? 59  LEU B CB  1 
ATOM   3390  C  CG  . LEU B 1 58  ? -4.614  43.911  44.613  1.00 61.06  ? 59  LEU B CG  1 
ATOM   3391  C  CD1 . LEU B 1 58  ? -4.450  44.790  45.842  1.00 53.88  ? 59  LEU B CD1 1 
ATOM   3392  C  CD2 . LEU B 1 58  ? -3.294  43.772  43.868  1.00 60.16  ? 59  LEU B CD2 1 
ATOM   3393  N  N   . ARG B 1 59  ? -4.884  39.179  43.945  1.00 68.61  ? 60  ARG B N   1 
ATOM   3394  C  CA  . ARG B 1 59  ? -5.097  37.789  44.337  1.00 67.38  ? 60  ARG B CA  1 
ATOM   3395  C  C   . ARG B 1 59  ? -4.569  37.477  45.737  1.00 68.01  ? 60  ARG B C   1 
ATOM   3396  O  O   . ARG B 1 59  ? -5.088  36.594  46.419  1.00 64.98  ? 60  ARG B O   1 
ATOM   3397  C  CB  . ARG B 1 59  ? -4.444  36.850  43.319  1.00 69.04  ? 60  ARG B CB  1 
ATOM   3398  N  N   . ILE B 1 60  ? -3.536  38.201  46.158  1.00 63.85  ? 61  ILE B N   1 
ATOM   3399  C  CA  . ILE B 1 60  ? -2.887  37.938  47.440  1.00 53.81  ? 61  ILE B CA  1 
ATOM   3400  C  C   . ILE B 1 60  ? -3.020  39.119  48.397  1.00 50.62  ? 61  ILE B C   1 
ATOM   3401  O  O   . ILE B 1 60  ? -3.638  39.000  49.455  1.00 47.56  ? 61  ILE B O   1 
ATOM   3402  C  CB  . ILE B 1 60  ? -1.394  37.605  47.254  1.00 58.70  ? 61  ILE B CB  1 
ATOM   3403  C  CG1 . ILE B 1 60  ? -1.236  36.309  46.456  1.00 53.98  ? 61  ILE B CG1 1 
ATOM   3404  C  CG2 . ILE B 1 60  ? -0.702  37.477  48.603  1.00 43.30  ? 61  ILE B CG2 1 
ATOM   3405  C  CD1 . ILE B 1 60  ? -0.325  36.438  45.255  1.00 54.96  ? 61  ILE B CD1 1 
ATOM   3406  N  N   . CYS B 1 61  ? -2.419  40.248  48.028  1.00 51.61  ? 62  CYS B N   1 
ATOM   3407  C  CA  . CYS B 1 61  ? -2.482  41.463  48.835  1.00 53.08  ? 62  CYS B CA  1 
ATOM   3408  C  C   . CYS B 1 61  ? -3.927  41.885  49.088  1.00 53.87  ? 62  CYS B C   1 
ATOM   3409  O  O   . CYS B 1 61  ? -4.788  41.684  48.232  1.00 52.55  ? 62  CYS B O   1 
ATOM   3410  C  CB  . CYS B 1 61  ? -1.719  42.599  48.149  1.00 52.80  ? 62  CYS B CB  1 
ATOM   3411  S  SG  . CYS B 1 61  ? -0.035  42.176  47.649  1.00 85.78  ? 62  CYS B SG  1 
ATOM   3412  N  N   . PRO B 1 62  ? -4.196  42.459  50.274  1.00 57.21  ? 63  PRO B N   1 
ATOM   3413  C  CA  . PRO B 1 62  ? -5.536  42.955  50.607  1.00 58.03  ? 63  PRO B CA  1 
ATOM   3414  C  C   . PRO B 1 62  ? -6.045  43.935  49.559  1.00 61.20  ? 63  PRO B C   1 
ATOM   3415  O  O   . PRO B 1 62  ? -5.306  44.837  49.163  1.00 62.97  ? 63  PRO B O   1 
ATOM   3416  C  CB  . PRO B 1 62  ? -5.332  43.651  51.955  1.00 55.38  ? 63  PRO B CB  1 
ATOM   3417  C  CG  . PRO B 1 62  ? -4.138  42.986  52.544  1.00 53.05  ? 63  PRO B CG  1 
ATOM   3418  C  CD  . PRO B 1 62  ? -3.246  42.650  51.384  1.00 53.20  ? 63  PRO B CD  1 
ATOM   3419  N  N   . GLN B 1 63  ? -7.283  43.750  49.111  1.00 67.71  ? 64  GLN B N   1 
ATOM   3420  C  CA  . GLN B 1 63  ? -7.839  44.600  48.069  1.00 76.10  ? 64  GLN B CA  1 
ATOM   3421  C  C   . GLN B 1 63  ? -7.927  46.042  48.548  1.00 75.91  ? 64  GLN B C   1 
ATOM   3422  O  O   . GLN B 1 63  ? -8.501  46.337  49.597  1.00 78.77  ? 64  GLN B O   1 
ATOM   3423  C  CB  . GLN B 1 63  ? -9.213  44.095  47.630  1.00 82.35  ? 64  GLN B CB  1 
ATOM   3424  C  CG  . GLN B 1 63  ? -9.343  42.581  47.641  1.00 91.80  ? 64  GLN B CG  1 
ATOM   3425  C  CD  . GLN B 1 63  ? -10.242 42.063  46.535  1.00 99.07  ? 64  GLN B CD  1 
ATOM   3426  O  OE1 . GLN B 1 63  ? -10.195 42.545  45.403  1.00 103.33 ? 64  GLN B OE1 1 
ATOM   3427  N  NE2 . GLN B 1 63  ? -11.073 41.081  46.861  1.00 100.74 ? 64  GLN B NE2 1 
ATOM   3428  N  N   . GLY B 1 64  ? -7.345  46.932  47.758  1.00 70.18  ? 65  GLY B N   1 
ATOM   3429  C  CA  . GLY B 1 64  ? -7.264  48.340  48.084  1.00 70.17  ? 65  GLY B CA  1 
ATOM   3430  C  C   . GLY B 1 64  ? -6.484  48.989  46.965  1.00 66.43  ? 65  GLY B C   1 
ATOM   3431  O  O   . GLY B 1 64  ? -5.892  48.290  46.143  1.00 65.88  ? 65  GLY B O   1 
ATOM   3432  N  N   . TYR B 1 65  ? -6.475  50.315  46.922  1.00 62.98  ? 66  TYR B N   1 
ATOM   3433  C  CA  . TYR B 1 65  ? -5.834  51.004  45.813  1.00 61.57  ? 66  TYR B CA  1 
ATOM   3434  C  C   . TYR B 1 65  ? -4.335  50.754  45.816  1.00 58.36  ? 66  TYR B C   1 
ATOM   3435  O  O   . TYR B 1 65  ? -3.652  50.950  46.822  1.00 59.91  ? 66  TYR B O   1 
ATOM   3436  C  CB  . TYR B 1 65  ? -6.167  52.491  45.853  1.00 65.58  ? 66  TYR B CB  1 
ATOM   3437  C  CG  . TYR B 1 65  ? -7.644  52.689  45.646  1.00 70.49  ? 66  TYR B CG  1 
ATOM   3438  C  CD1 . TYR B 1 65  ? -8.179  52.720  44.367  1.00 74.67  ? 66  TYR B CD1 1 
ATOM   3439  C  CD2 . TYR B 1 65  ? -8.509  52.814  46.725  1.00 71.45  ? 66  TYR B CD2 1 
ATOM   3440  C  CE1 . TYR B 1 65  ? -9.531  52.875  44.164  1.00 77.96  ? 66  TYR B CE1 1 
ATOM   3441  C  CE2 . TYR B 1 65  ? -9.866  52.977  46.532  1.00 75.70  ? 66  TYR B CE2 1 
ATOM   3442  C  CZ  . TYR B 1 65  ? -10.371 53.005  45.249  1.00 78.83  ? 66  TYR B CZ  1 
ATOM   3443  O  OH  . TYR B 1 65  ? -11.721 53.168  45.043  1.00 82.11  ? 66  TYR B OH  1 
ATOM   3444  N  N   . THR B 1 66  ? -3.842  50.300  44.671  1.00 56.96  ? 67  THR B N   1 
ATOM   3445  C  CA  . THR B 1 66  ? -2.514  49.717  44.588  1.00 54.59  ? 67  THR B CA  1 
ATOM   3446  C  C   . THR B 1 66  ? -1.745  50.170  43.355  1.00 55.97  ? 67  THR B C   1 
ATOM   3447  O  O   . THR B 1 66  ? -2.330  50.634  42.377  1.00 57.58  ? 67  THR B O   1 
ATOM   3448  C  CB  . THR B 1 66  ? -2.596  48.176  44.580  1.00 61.02  ? 67  THR B CB  1 
ATOM   3449  O  OG1 . THR B 1 66  ? -1.276  47.620  44.621  1.00 52.60  ? 67  THR B OG1 1 
ATOM   3450  C  CG2 . THR B 1 66  ? -3.319  47.685  43.332  1.00 54.68  ? 67  THR B CG2 1 
ATOM   3451  N  N   . CYS B 1 67  ? -0.425  50.040  43.420  1.00 55.44  ? 68  CYS B N   1 
ATOM   3452  C  CA  . CYS B 1 67  ? 0.435   50.336  42.284  1.00 65.50  ? 68  CYS B CA  1 
ATOM   3453  C  C   . CYS B 1 67  ? 0.759   49.071  41.497  1.00 60.37  ? 68  CYS B C   1 
ATOM   3454  O  O   . CYS B 1 67  ? 1.503   49.116  40.519  1.00 59.47  ? 68  CYS B O   1 
ATOM   3455  C  CB  . CYS B 1 67  ? 1.727   51.009  42.749  1.00 56.56  ? 68  CYS B CB  1 
ATOM   3456  S  SG  . CYS B 1 67  ? 1.574   52.774  43.108  1.00 110.73 ? 68  CYS B SG  1 
ATOM   3457  N  N   . CYS B 1 68  ? 0.205   47.943  41.928  1.00 60.45  ? 69  CYS B N   1 
ATOM   3458  C  CA  . CYS B 1 68  ? 0.541   46.655  41.328  1.00 65.08  ? 69  CYS B CA  1 
ATOM   3459  C  C   . CYS B 1 68  ? -0.596  46.066  40.502  1.00 69.47  ? 69  CYS B C   1 
ATOM   3460  O  O   . CYS B 1 68  ? -1.703  45.869  41.004  1.00 68.88  ? 69  CYS B O   1 
ATOM   3461  C  CB  . CYS B 1 68  ? 0.944   45.653  42.414  1.00 62.23  ? 69  CYS B CB  1 
ATOM   3462  S  SG  . CYS B 1 68  ? 2.490   46.036  43.264  1.00 68.35  ? 69  CYS B SG  1 
ATOM   3463  N  N   . THR B 1 69  ? -0.316  45.780  39.234  1.00 72.75  ? 70  THR B N   1 
ATOM   3464  C  CA  . THR B 1 69  ? -1.234  44.995  38.421  1.00 73.75  ? 70  THR B CA  1 
ATOM   3465  C  C   . THR B 1 69  ? -1.098  43.534  38.836  1.00 70.87  ? 70  THR B C   1 
ATOM   3466  O  O   . THR B 1 69  ? -0.229  43.198  39.641  1.00 72.19  ? 70  THR B O   1 
ATOM   3467  C  CB  . THR B 1 69  ? -0.961  45.149  36.912  1.00 73.42  ? 70  THR B CB  1 
ATOM   3468  O  OG1 . THR B 1 69  ? 0.375   44.724  36.616  1.00 71.35  ? 70  THR B OG1 1 
ATOM   3469  C  CG2 . THR B 1 69  ? -1.131  46.599  36.485  1.00 70.35  ? 70  THR B CG2 1 
ATOM   3470  N  N   . SER B 1 70  ? -1.951  42.670  38.297  1.00 74.52  ? 71  SER B N   1 
ATOM   3471  C  CA  . SER B 1 70  ? -1.938  41.257  38.667  1.00 76.12  ? 71  SER B CA  1 
ATOM   3472  C  C   . SER B 1 70  ? -0.604  40.601  38.315  1.00 72.23  ? 71  SER B C   1 
ATOM   3473  O  O   . SER B 1 70  ? -0.059  39.811  39.095  1.00 70.06  ? 71  SER B O   1 
ATOM   3474  C  CB  . SER B 1 70  ? -3.087  40.514  37.984  1.00 79.56  ? 71  SER B CB  1 
ATOM   3475  O  OG  . SER B 1 70  ? -3.104  39.149  38.364  1.00 83.38  ? 71  SER B OG  1 
ATOM   3476  N  N   . GLU B 1 71  ? -0.085  40.944  37.139  1.00 73.20  ? 72  GLU B N   1 
ATOM   3477  C  CA  . GLU B 1 71  ? 1.210   40.447  36.687  1.00 74.57  ? 72  GLU B CA  1 
ATOM   3478  C  C   . GLU B 1 71  ? 2.311   40.840  37.665  1.00 73.35  ? 72  GLU B C   1 
ATOM   3479  O  O   . GLU B 1 71  ? 3.143   40.013  38.044  1.00 71.44  ? 72  GLU B O   1 
ATOM   3480  C  CB  . GLU B 1 71  ? 1.530   40.979  35.289  1.00 75.35  ? 72  GLU B CB  1 
ATOM   3481  N  N   . MET B 1 72  ? 2.302   42.105  38.074  1.00 69.28  ? 73  MET B N   1 
ATOM   3482  C  CA  . MET B 1 72  ? 3.265   42.611  39.045  1.00 69.57  ? 73  MET B CA  1 
ATOM   3483  C  C   . MET B 1 72  ? 3.163   41.857  40.365  1.00 65.55  ? 73  MET B C   1 
ATOM   3484  O  O   . MET B 1 72  ? 4.177   41.541  40.991  1.00 64.36  ? 73  MET B O   1 
ATOM   3485  C  CB  . MET B 1 72  ? 3.052   44.106  39.281  1.00 67.34  ? 73  MET B CB  1 
ATOM   3486  C  CG  . MET B 1 72  ? 3.200   44.959  38.037  1.00 68.08  ? 73  MET B CG  1 
ATOM   3487  S  SD  . MET B 1 72  ? 2.898   46.699  38.384  1.00 79.38  ? 73  MET B SD  1 
ATOM   3488  C  CE  . MET B 1 72  ? 4.195   47.038  39.571  1.00 56.72  ? 73  MET B CE  1 
ATOM   3489  N  N   . GLU B 1 73  ? 1.932   41.572  40.779  1.00 63.69  ? 74  GLU B N   1 
ATOM   3490  C  CA  . GLU B 1 73  ? 1.684   40.825  42.006  1.00 65.59  ? 74  GLU B CA  1 
ATOM   3491  C  C   . GLU B 1 73  ? 2.314   39.440  41.934  1.00 66.32  ? 74  GLU B C   1 
ATOM   3492  O  O   . GLU B 1 73  ? 3.105   39.063  42.799  1.00 67.67  ? 74  GLU B O   1 
ATOM   3493  C  CB  . GLU B 1 73  ? 0.183   40.702  42.270  1.00 64.65  ? 74  GLU B CB  1 
ATOM   3494  C  CG  . GLU B 1 73  ? -0.163  40.311  43.696  1.00 62.48  ? 74  GLU B CG  1 
ATOM   3495  C  CD  . GLU B 1 73  ? -1.618  39.916  43.855  1.00 63.34  ? 74  GLU B CD  1 
ATOM   3496  O  OE1 . GLU B 1 73  ? -2.268  39.608  42.834  1.00 64.13  ? 74  GLU B OE1 1 
ATOM   3497  O  OE2 . GLU B 1 73  ? -2.113  39.922  45.001  1.00 62.08  ? 74  GLU B OE2 1 
ATOM   3498  N  N   . GLU B 1 74  ? 1.950   38.691  40.896  1.00 70.13  ? 75  GLU B N   1 
ATOM   3499  C  CA  . GLU B 1 74  ? 2.517   37.366  40.644  1.00 72.63  ? 75  GLU B CA  1 
ATOM   3500  C  C   . GLU B 1 74  ? 4.048   37.383  40.665  1.00 69.00  ? 75  GLU B C   1 
ATOM   3501  O  O   . GLU B 1 74  ? 4.694   36.623  41.408  1.00 65.93  ? 75  GLU B O   1 
ATOM   3502  C  CB  . GLU B 1 74  ? 2.014   36.842  39.297  1.00 82.00  ? 75  GLU B CB  1 
ATOM   3503  C  CG  . GLU B 1 74  ? 2.824   35.702  38.707  1.00 89.93  ? 75  GLU B CG  1 
ATOM   3504  C  CD  . GLU B 1 74  ? 2.585   35.542  37.217  1.00 95.93  ? 75  GLU B CD  1 
ATOM   3505  O  OE1 . GLU B 1 74  ? 1.951   36.437  36.618  1.00 99.19  ? 75  GLU B OE1 1 
ATOM   3506  O  OE2 . GLU B 1 74  ? 3.032   34.527  36.644  1.00 97.95  ? 75  GLU B OE2 1 
ATOM   3507  N  N   . ASN B 1 75  ? 4.612   38.269  39.849  1.00 66.45  ? 76  ASN B N   1 
ATOM   3508  C  CA  . ASN B 1 75  ? 6.057   38.411  39.722  1.00 67.27  ? 76  ASN B CA  1 
ATOM   3509  C  C   . ASN B 1 75  ? 6.749   38.681  41.055  1.00 65.85  ? 76  ASN B C   1 
ATOM   3510  O  O   . ASN B 1 75  ? 7.718   38.003  41.406  1.00 68.15  ? 76  ASN B O   1 
ATOM   3511  C  CB  . ASN B 1 75  ? 6.386   39.529  38.732  1.00 71.29  ? 76  ASN B CB  1 
ATOM   3512  C  CG  . ASN B 1 75  ? 5.997   39.179  37.308  1.00 77.73  ? 76  ASN B CG  1 
ATOM   3513  O  OD1 . ASN B 1 75  ? 5.185   38.283  37.076  1.00 78.91  ? 76  ASN B OD1 1 
ATOM   3514  N  ND2 . ASN B 1 75  ? 6.575   39.889  36.346  1.00 78.01  ? 76  ASN B ND2 1 
ATOM   3515  N  N   . LEU B 1 76  ? 6.249   39.667  41.794  1.00 61.34  ? 77  LEU B N   1 
ATOM   3516  C  CA  . LEU B 1 76  ? 6.810   39.993  43.102  1.00 58.80  ? 77  LEU B CA  1 
ATOM   3517  C  C   . LEU B 1 76  ? 6.682   38.817  44.067  1.00 59.25  ? 77  LEU B C   1 
ATOM   3518  O  O   . LEU B 1 76  ? 7.569   38.579  44.887  1.00 56.98  ? 77  LEU B O   1 
ATOM   3519  C  CB  . LEU B 1 76  ? 6.130   41.230  43.692  1.00 62.23  ? 77  LEU B CB  1 
ATOM   3520  C  CG  . LEU B 1 76  ? 6.487   42.583  43.074  1.00 65.46  ? 77  LEU B CG  1 
ATOM   3521  C  CD1 . LEU B 1 76  ? 5.769   43.705  43.807  1.00 66.67  ? 77  LEU B CD1 1 
ATOM   3522  C  CD2 . LEU B 1 76  ? 7.991   42.804  43.092  1.00 65.39  ? 77  LEU B CD2 1 
ATOM   3523  N  N   . ALA B 1 77  ? 5.578   38.084  43.960  1.00 58.87  ? 78  ALA B N   1 
ATOM   3524  C  CA  . ALA B 1 77  ? 5.344   36.924  44.812  1.00 64.92  ? 78  ALA B CA  1 
ATOM   3525  C  C   . ALA B 1 77  ? 6.411   35.858  44.590  1.00 66.05  ? 78  ALA B C   1 
ATOM   3526  O  O   . ALA B 1 77  ? 7.072   35.411  45.540  1.00 63.51  ? 78  ALA B O   1 
ATOM   3527  C  CB  . ALA B 1 77  ? 3.959   36.349  44.557  1.00 44.78  ? 78  ALA B CB  1 
ATOM   3528  N  N   . ASN B 1 78  ? 6.588   35.457  43.334  1.00 69.46  ? 79  ASN B N   1 
ATOM   3529  C  CA  . ASN B 1 78  ? 7.601   34.454  43.026  1.00 76.12  ? 79  ASN B CA  1 
ATOM   3530  C  C   . ASN B 1 78  ? 9.017   34.970  43.281  1.00 70.80  ? 79  ASN B C   1 
ATOM   3531  O  O   . ASN B 1 78  ? 9.937   34.186  43.528  1.00 71.18  ? 79  ASN B O   1 
ATOM   3532  C  CB  . ASN B 1 78  ? 7.458   33.972  41.583  1.00 89.41  ? 79  ASN B CB  1 
ATOM   3533  C  CG  . ASN B 1 78  ? 6.233   33.100  41.384  1.00 99.69  ? 79  ASN B CG  1 
ATOM   3534  O  OD1 . ASN B 1 78  ? 5.720   32.506  42.334  1.00 101.88 ? 79  ASN B OD1 1 
ATOM   3535  N  ND2 . ASN B 1 78  ? 5.761   33.012  40.146  1.00 105.07 ? 79  ASN B ND2 1 
ATOM   3536  N  N   . ARG B 1 79  ? 9.187   36.288  43.238  1.00 64.54  ? 80  ARG B N   1 
ATOM   3537  C  CA  . ARG B 1 79  ? 10.467  36.891  43.592  1.00 63.59  ? 80  ARG B CA  1 
ATOM   3538  C  C   . ARG B 1 79  ? 10.763  36.697  45.077  1.00 60.41  ? 80  ARG B C   1 
ATOM   3539  O  O   . ARG B 1 79  ? 11.854  36.259  45.448  1.00 64.07  ? 80  ARG B O   1 
ATOM   3540  C  CB  . ARG B 1 79  ? 10.483  38.380  43.238  1.00 60.98  ? 80  ARG B CB  1 
ATOM   3541  C  CG  . ARG B 1 79  ? 11.688  39.141  43.781  1.00 62.83  ? 80  ARG B CG  1 
ATOM   3542  C  CD  . ARG B 1 79  ? 13.000  38.512  43.333  1.00 68.08  ? 80  ARG B CD  1 
ATOM   3543  N  NE  . ARG B 1 79  ? 13.054  38.306  41.889  1.00 74.69  ? 80  ARG B NE  1 
ATOM   3544  C  CZ  . ARG B 1 79  ? 13.765  39.055  41.053  1.00 81.67  ? 80  ARG B CZ  1 
ATOM   3545  N  NH1 . ARG B 1 79  ? 14.490  40.063  41.518  1.00 84.35  ? 80  ARG B NH1 1 
ATOM   3546  N  NH2 . ARG B 1 79  ? 13.756  38.794  39.753  1.00 84.57  ? 80  ARG B NH2 1 
ATOM   3547  N  N   . SER B 1 80  ? 9.789   37.021  45.922  1.00 56.17  ? 81  SER B N   1 
ATOM   3548  C  CA  . SER B 1 80  ? 9.942   36.861  47.365  1.00 51.21  ? 81  SER B CA  1 
ATOM   3549  C  C   . SER B 1 80  ? 10.159  35.395  47.732  1.00 46.62  ? 81  SER B C   1 
ATOM   3550  O  O   . SER B 1 80  ? 11.019  35.068  48.565  1.00 47.15  ? 81  SER B O   1 
ATOM   3551  C  CB  . SER B 1 80  ? 8.721   37.418  48.101  1.00 51.60  ? 81  SER B CB  1 
ATOM   3552  O  OG  . SER B 1 80  ? 7.532   36.765  47.691  1.00 53.20  ? 81  SER B OG  1 
ATOM   3553  N  N   . HIS B 1 81  ? 9.383   34.516  47.101  1.00 40.39  ? 82  HIS B N   1 
ATOM   3554  C  CA  . HIS B 1 81  ? 9.554   33.081  47.309  1.00 48.43  ? 82  HIS B CA  1 
ATOM   3555  C  C   . HIS B 1 81  ? 10.971  32.650  46.938  1.00 50.66  ? 82  HIS B C   1 
ATOM   3556  O  O   . HIS B 1 81  ? 11.624  31.910  47.683  1.00 47.16  ? 82  HIS B O   1 
ATOM   3557  C  CB  . HIS B 1 81  ? 8.533   32.285  46.496  1.00 49.12  ? 82  HIS B CB  1 
ATOM   3558  C  CG  . HIS B 1 81  ? 8.744   30.804  46.554  1.00 59.27  ? 82  HIS B CG  1 
ATOM   3559  N  ND1 . HIS B 1 81  ? 9.487   30.119  45.617  1.00 57.76  ? 82  HIS B ND1 1 
ATOM   3560  C  CD2 . HIS B 1 81  ? 8.316   29.877  47.444  1.00 55.53  ? 82  HIS B CD2 1 
ATOM   3561  C  CE1 . HIS B 1 81  ? 9.504   28.835  45.924  1.00 56.94  ? 82  HIS B CE1 1 
ATOM   3562  N  NE2 . HIS B 1 81  ? 8.801   28.661  47.029  1.00 55.75  ? 82  HIS B NE2 1 
ATOM   3563  N  N   . ALA B 1 82  ? 11.441  33.129  45.789  1.00 50.78  ? 83  ALA B N   1 
ATOM   3564  C  CA  . ALA B 1 82  ? 12.795  32.842  45.327  1.00 47.79  ? 83  ALA B CA  1 
ATOM   3565  C  C   . ALA B 1 82  ? 13.835  33.285  46.350  1.00 49.90  ? 83  ALA B C   1 
ATOM   3566  O  O   . ALA B 1 82  ? 14.776  32.549  46.652  1.00 54.82  ? 83  ALA B O   1 
ATOM   3567  C  CB  . ALA B 1 82  ? 13.053  33.516  43.989  1.00 49.83  ? 83  ALA B CB  1 
ATOM   3568  N  N   . GLU B 1 83  ? 13.654  34.489  46.884  1.00 48.50  ? 84  GLU B N   1 
ATOM   3569  C  CA  . GLU B 1 83  ? 14.575  35.040  47.872  1.00 45.41  ? 84  GLU B CA  1 
ATOM   3570  C  C   . GLU B 1 83  ? 14.617  34.181  49.137  1.00 44.84  ? 84  GLU B C   1 
ATOM   3571  O  O   . GLU B 1 83  ? 15.700  33.859  49.648  1.00 47.15  ? 84  GLU B O   1 
ATOM   3572  C  CB  . GLU B 1 83  ? 14.182  36.482  48.210  1.00 44.17  ? 84  GLU B CB  1 
ATOM   3573  C  CG  . GLU B 1 83  ? 14.388  37.454  47.053  1.00 48.28  ? 84  GLU B CG  1 
ATOM   3574  C  CD  . GLU B 1 83  ? 13.721  38.802  47.274  1.00 51.93  ? 84  GLU B CD  1 
ATOM   3575  O  OE1 . GLU B 1 83  ? 13.046  38.978  48.310  1.00 48.25  ? 84  GLU B OE1 1 
ATOM   3576  O  OE2 . GLU B 1 83  ? 13.872  39.686  46.404  1.00 53.73  ? 84  GLU B OE2 1 
ATOM   3577  N  N   . LEU B 1 84  ? 13.441  33.796  49.629  1.00 43.58  ? 85  LEU B N   1 
ATOM   3578  C  CA  . LEU B 1 84  ? 13.369  32.929  50.806  1.00 44.81  ? 85  LEU B CA  1 
ATOM   3579  C  C   . LEU B 1 84  ? 14.070  31.588  50.568  1.00 44.54  ? 85  LEU B C   1 
ATOM   3580  O  O   . LEU B 1 84  ? 14.875  31.132  51.397  1.00 42.40  ? 85  LEU B O   1 
ATOM   3581  C  CB  . LEU B 1 84  ? 11.913  32.693  51.210  1.00 41.35  ? 85  LEU B CB  1 
ATOM   3582  C  CG  . LEU B 1 84  ? 11.693  31.836  52.459  1.00 38.38  ? 85  LEU B CG  1 
ATOM   3583  C  CD1 . LEU B 1 84  ? 12.579  32.304  53.602  1.00 43.97  ? 85  LEU B CD1 1 
ATOM   3584  C  CD2 . LEU B 1 84  ? 10.234  31.868  52.874  1.00 39.00  ? 85  LEU B CD2 1 
ATOM   3585  N  N   . GLU B 1 85  ? 13.762  30.966  49.431  1.00 45.11  ? 86  GLU B N   1 
ATOM   3586  C  CA  . GLU B 1 85  ? 14.363  29.686  49.066  1.00 52.32  ? 86  GLU B CA  1 
ATOM   3587  C  C   . GLU B 1 85  ? 15.883  29.804  49.007  1.00 51.81  ? 86  GLU B C   1 
ATOM   3588  O  O   . GLU B 1 85  ? 16.607  28.904  49.440  1.00 48.49  ? 86  GLU B O   1 
ATOM   3589  C  CB  . GLU B 1 85  ? 13.820  29.197  47.721  1.00 58.71  ? 86  GLU B CB  1 
ATOM   3590  C  CG  . GLU B 1 85  ? 13.621  27.692  47.641  1.00 65.11  ? 86  GLU B CG  1 
ATOM   3591  C  CD  . GLU B 1 85  ? 12.275  27.256  48.185  1.00 73.84  ? 86  GLU B CD  1 
ATOM   3592  O  OE1 . GLU B 1 85  ? 11.442  28.138  48.481  1.00 75.76  ? 86  GLU B OE1 1 
ATOM   3593  O  OE2 . GLU B 1 85  ? 12.050  26.034  48.319  1.00 73.28  ? 86  GLU B OE2 1 
ATOM   3594  N  N   . THR B 1 86  ? 16.356  30.928  48.475  1.00 54.92  ? 87  THR B N   1 
ATOM   3595  C  CA  . THR B 1 86  ? 17.785  31.205  48.390  1.00 49.64  ? 87  THR B CA  1 
ATOM   3596  C  C   . THR B 1 86  ? 18.410  31.305  49.779  1.00 52.39  ? 87  THR B C   1 
ATOM   3597  O  O   . THR B 1 86  ? 19.471  30.729  50.030  1.00 55.68  ? 87  THR B O   1 
ATOM   3598  C  CB  . THR B 1 86  ? 18.056  32.503  47.603  1.00 49.13  ? 87  THR B CB  1 
ATOM   3599  O  OG1 . THR B 1 86  ? 17.824  32.270  46.209  1.00 50.76  ? 87  THR B OG1 1 
ATOM   3600  C  CG2 . THR B 1 86  ? 19.495  32.960  47.792  1.00 49.83  ? 87  THR B CG2 1 
ATOM   3601  N  N   . ALA B 1 87  ? 17.747  32.027  50.681  1.00 41.57  ? 88  ALA B N   1 
ATOM   3602  C  CA  . ALA B 1 87  ? 18.222  32.130  52.062  1.00 39.56  ? 88  ALA B CA  1 
ATOM   3603  C  C   . ALA B 1 87  ? 18.356  30.749  52.716  1.00 43.36  ? 88  ALA B C   1 
ATOM   3604  O  O   . ALA B 1 87  ? 19.430  30.384  53.241  1.00 51.27  ? 88  ALA B O   1 
ATOM   3605  C  CB  . ALA B 1 87  ? 17.289  33.010  52.873  1.00 37.31  ? 88  ALA B CB  1 
ATOM   3606  N  N   . LEU B 1 88  ? 17.262  29.988  52.671  1.00 39.24  ? 89  LEU B N   1 
ATOM   3607  C  CA  . LEU B 1 88  ? 17.240  28.631  53.216  1.00 39.52  ? 89  LEU B CA  1 
ATOM   3608  C  C   . LEU B 1 88  ? 18.384  27.786  52.661  1.00 39.02  ? 89  LEU B C   1 
ATOM   3609  O  O   . LEU B 1 88  ? 19.129  27.148  53.416  1.00 38.71  ? 89  LEU B O   1 
ATOM   3610  C  CB  . LEU B 1 88  ? 15.901  27.955  52.916  1.00 39.53  ? 89  LEU B CB  1 
ATOM   3611  C  CG  . LEU B 1 88  ? 14.684  28.477  53.679  1.00 43.95  ? 89  LEU B CG  1 
ATOM   3612  C  CD1 . LEU B 1 88  ? 13.390  28.028  53.012  1.00 35.16  ? 89  LEU B CD1 1 
ATOM   3613  C  CD2 . LEU B 1 88  ? 14.732  28.016  55.128  1.00 44.50  ? 89  LEU B CD2 1 
ATOM   3614  N  N   . ARG B 1 89  ? 18.517  27.803  51.336  1.00 36.19  ? 90  ARG B N   1 
ATOM   3615  C  CA  . ARG B 1 89  ? 19.570  27.070  50.645  1.00 45.76  ? 90  ARG B CA  1 
ATOM   3616  C  C   . ARG B 1 89  ? 20.949  27.448  51.170  1.00 39.28  ? 90  ARG B C   1 
ATOM   3617  O  O   . ARG B 1 89  ? 21.763  26.578  51.482  1.00 39.41  ? 90  ARG B O   1 
ATOM   3618  C  CB  . ARG B 1 89  ? 19.504  27.330  49.139  1.00 51.70  ? 90  ARG B CB  1 
ATOM   3619  C  CG  . ARG B 1 89  ? 20.114  26.227  48.289  1.00 64.14  ? 90  ARG B CG  1 
ATOM   3620  C  CD  . ARG B 1 89  ? 20.483  26.718  46.894  1.00 70.25  ? 90  ARG B CD  1 
ATOM   3621  N  NE  . ARG B 1 89  ? 19.439  27.536  46.281  1.00 74.73  ? 90  ARG B NE  1 
ATOM   3622  C  CZ  . ARG B 1 89  ? 19.510  28.857  46.145  1.00 77.55  ? 90  ARG B CZ  1 
ATOM   3623  N  NH1 . ARG B 1 89  ? 20.576  29.514  46.580  1.00 76.35  ? 90  ARG B NH1 1 
ATOM   3624  N  NH2 . ARG B 1 89  ? 18.514  29.521  45.573  1.00 80.87  ? 90  ARG B NH2 1 
ATOM   3625  N  N   . ASP B 1 90  ? 21.200  28.751  51.270  1.00 38.02  ? 91  ASP B N   1 
ATOM   3626  C  CA  . ASP B 1 90  ? 22.488  29.247  51.742  1.00 46.48  ? 91  ASP B CA  1 
ATOM   3627  C  C   . ASP B 1 90  ? 22.808  28.747  53.149  1.00 40.98  ? 91  ASP B C   1 
ATOM   3628  O  O   . ASP B 1 90  ? 23.884  28.179  53.382  1.00 41.62  ? 91  ASP B O   1 
ATOM   3629  C  CB  . ASP B 1 90  ? 22.518  30.777  51.710  1.00 53.53  ? 91  ASP B CB  1 
ATOM   3630  C  CG  . ASP B 1 90  ? 22.479  31.330  50.297  1.00 62.93  ? 91  ASP B CG  1 
ATOM   3631  O  OD1 . ASP B 1 90  ? 22.598  30.532  49.343  1.00 62.86  ? 91  ASP B OD1 1 
ATOM   3632  O  OD2 . ASP B 1 90  ? 22.332  32.561  50.141  1.00 69.31  ? 91  ASP B OD2 1 
ATOM   3633  N  N   . SER B 1 91  ? 21.876  28.942  54.081  1.00 33.25  ? 92  SER B N   1 
ATOM   3634  C  CA  . SER B 1 91  ? 22.121  28.514  55.461  1.00 38.75  ? 92  SER B CA  1 
ATOM   3635  C  C   . SER B 1 91  ? 22.357  27.002  55.555  1.00 36.02  ? 92  SER B C   1 
ATOM   3636  O  O   . SER B 1 91  ? 23.336  26.536  56.173  1.00 40.75  ? 92  SER B O   1 
ATOM   3637  C  CB  . SER B 1 91  ? 20.954  28.919  56.364  1.00 39.13  ? 92  SER B CB  1 
ATOM   3638  O  OG  . SER B 1 91  ? 19.803  28.138  56.092  1.00 49.06  ? 92  SER B OG  1 
ATOM   3639  N  N   . SER B 1 92  ? 21.465  26.243  54.923  1.00 37.65  ? 93  SER B N   1 
ATOM   3640  C  CA  A SER B 1 92  ? 21.551  24.788  54.958  0.65 39.21  ? 93  SER B CA  1 
ATOM   3641  C  CA  B SER B 1 92  ? 21.543  24.787  54.942  0.35 38.81  ? 93  SER B CA  1 
ATOM   3642  C  C   . SER B 1 92  ? 22.859  24.288  54.354  1.00 42.90  ? 93  SER B C   1 
ATOM   3643  O  O   . SER B 1 92  ? 23.434  23.323  54.839  1.00 53.65  ? 93  SER B O   1 
ATOM   3644  C  CB  A SER B 1 92  ? 20.363  24.159  54.228  0.65 34.69  ? 93  SER B CB  1 
ATOM   3645  C  CB  B SER B 1 92  ? 20.366  24.180  54.176  0.35 35.88  ? 93  SER B CB  1 
ATOM   3646  O  OG  A SER B 1 92  ? 20.487  24.313  52.825  0.65 33.87  ? 93  SER B OG  1 
ATOM   3647  O  OG  B SER B 1 92  ? 20.471  22.768  54.115  0.35 37.16  ? 93  SER B OG  1 
ATOM   3648  N  N   . ARG B 1 93  ? 23.332  24.949  53.302  1.00 48.27  ? 94  ARG B N   1 
ATOM   3649  C  CA  . ARG B 1 93  ? 24.575  24.530  52.661  1.00 52.27  ? 94  ARG B CA  1 
ATOM   3650  C  C   . ARG B 1 93  ? 25.804  24.964  53.458  1.00 49.49  ? 94  ARG B C   1 
ATOM   3651  O  O   . ARG B 1 93  ? 26.862  24.340  53.358  1.00 48.40  ? 94  ARG B O   1 
ATOM   3652  C  CB  . ARG B 1 93  ? 24.646  25.058  51.229  1.00 61.57  ? 94  ARG B CB  1 
ATOM   3653  C  CG  . ARG B 1 93  ? 24.257  24.009  50.196  1.00 67.57  ? 94  ARG B CG  1 
ATOM   3654  C  CD  . ARG B 1 93  ? 24.316  24.542  48.774  1.00 74.31  ? 94  ARG B CD  1 
ATOM   3655  N  NE  . ARG B 1 93  ? 25.245  25.658  48.634  1.00 78.98  ? 94  ARG B NE  1 
ATOM   3656  C  CZ  . ARG B 1 93  ? 24.883  26.887  48.280  1.00 83.19  ? 94  ARG B CZ  1 
ATOM   3657  N  NH1 . ARG B 1 93  ? 23.609  27.156  48.025  1.00 83.48  ? 94  ARG B NH1 1 
ATOM   3658  N  NH2 . ARG B 1 93  ? 25.792  27.846  48.176  1.00 82.85  ? 94  ARG B NH2 1 
ATOM   3659  N  N   . VAL B 1 94  ? 25.670  26.025  54.249  1.00 43.25  ? 95  VAL B N   1 
ATOM   3660  C  CA  . VAL B 1 94  ? 26.712  26.343  55.222  1.00 44.49  ? 95  VAL B CA  1 
ATOM   3661  C  C   . VAL B 1 94  ? 26.816  25.211  56.248  1.00 37.98  ? 95  VAL B C   1 
ATOM   3662  O  O   . VAL B 1 94  ? 27.915  24.677  56.504  1.00 39.50  ? 95  VAL B O   1 
ATOM   3663  C  CB  . VAL B 1 94  ? 26.445  27.674  55.949  1.00 39.26  ? 95  VAL B CB  1 
ATOM   3664  C  CG1 . VAL B 1 94  ? 27.349  27.806  57.168  1.00 34.97  ? 95  VAL B CG1 1 
ATOM   3665  C  CG2 . VAL B 1 94  ? 26.644  28.849  55.002  1.00 34.00  ? 95  VAL B CG2 1 
ATOM   3666  N  N   . LEU B 1 95  ? 25.668  24.845  56.822  1.00 37.14  ? 96  LEU B N   1 
ATOM   3667  C  CA  . LEU B 1 95  ? 25.609  23.747  57.793  1.00 36.70  ? 96  LEU B CA  1 
ATOM   3668  C  C   . LEU B 1 95  ? 26.254  22.495  57.213  1.00 34.27  ? 96  LEU B C   1 
ATOM   3669  O  O   . LEU B 1 95  ? 27.133  21.873  57.818  1.00 40.27  ? 96  LEU B O   1 
ATOM   3670  C  CB  . LEU B 1 95  ? 24.158  23.455  58.189  1.00 36.67  ? 96  LEU B CB  1 
ATOM   3671  C  CG  . LEU B 1 95  ? 23.891  22.330  59.191  1.00 36.23  ? 96  LEU B CG  1 
ATOM   3672  C  CD1 . LEU B 1 95  ? 24.769  22.501  60.415  1.00 33.32  ? 96  LEU B CD1 1 
ATOM   3673  C  CD2 . LEU B 1 95  ? 22.428  22.336  59.592  1.00 35.01  ? 96  LEU B CD2 1 
ATOM   3674  N  N   . GLN B 1 96  ? 25.793  22.163  56.016  1.00 36.64  ? 97  GLN B N   1 
ATOM   3675  C  CA  . GLN B 1 96  ? 26.270  21.045  55.221  1.00 42.43  ? 97  GLN B CA  1 
ATOM   3676  C  C   . GLN B 1 96  ? 27.778  21.048  55.060  1.00 37.38  ? 97  GLN B C   1 
ATOM   3677  O  O   . GLN B 1 96  ? 28.442  20.024  55.259  1.00 39.69  ? 97  GLN B O   1 
ATOM   3678  C  CB  . GLN B 1 96  ? 25.588  21.078  53.854  1.00 51.88  ? 97  GLN B CB  1 
ATOM   3679  C  CG  . GLN B 1 96  ? 25.765  19.823  53.033  1.00 64.95  ? 97  GLN B CG  1 
ATOM   3680  C  CD  . GLN B 1 96  ? 24.607  19.583  52.094  1.00 73.10  ? 97  GLN B CD  1 
ATOM   3681  O  OE1 . GLN B 1 96  ? 23.513  19.225  52.522  1.00 77.40  ? 97  GLN B OE1 1 
ATOM   3682  N  NE2 . GLN B 1 96  ? 24.822  19.853  50.811  1.00 77.90  ? 97  GLN B NE2 1 
ATOM   3683  N  N   . ALA B 1 97  ? 28.305  22.214  54.702  1.00 41.22  ? 98  ALA B N   1 
ATOM   3684  C  CA  . ALA B 1 97  ? 29.733  22.396  54.513  1.00 35.97  ? 98  ALA B CA  1 
ATOM   3685  C  C   . ALA B 1 97  ? 30.483  22.062  55.792  1.00 40.10  ? 98  ALA B C   1 
ATOM   3686  O  O   . ALA B 1 97  ? 31.451  21.286  55.780  1.00 36.37  ? 98  ALA B O   1 
ATOM   3687  C  CB  . ALA B 1 97  ? 30.027  23.818  54.077  1.00 35.49  ? 98  ALA B CB  1 
ATOM   3688  N  N   . MET B 1 98  ? 30.021  22.650  56.893  1.00 34.68  ? 99  MET B N   1 
ATOM   3689  C  CA  . MET B 1 98  ? 30.618  22.386  58.200  1.00 31.55  ? 99  MET B CA  1 
ATOM   3690  C  C   . MET B 1 98  ? 30.641  20.891  58.545  1.00 37.99  ? 99  MET B C   1 
ATOM   3691  O  O   . MET B 1 98  ? 31.692  20.337  58.904  1.00 38.55  ? 99  MET B O   1 
ATOM   3692  C  CB  . MET B 1 98  ? 29.870  23.169  59.282  1.00 31.03  ? 99  MET B CB  1 
ATOM   3693  C  CG  . MET B 1 98  ? 30.088  22.656  60.695  1.00 34.84  ? 99  MET B CG  1 
ATOM   3694  S  SD  . MET B 1 98  ? 28.776  21.526  61.198  1.00 102.65 ? 99  MET B SD  1 
ATOM   3695  C  CE  . MET B 1 98  ? 29.274  21.142  62.870  1.00 40.43  ? 99  MET B CE  1 
ATOM   3696  N  N   . LEU B 1 99  ? 29.482  20.245  58.427  1.00 35.49  ? 100 LEU B N   1 
ATOM   3697  C  CA  . LEU B 1 99  ? 29.359  18.820  58.735  1.00 35.60  ? 100 LEU B CA  1 
ATOM   3698  C  C   . LEU B 1 99  ? 30.300  17.969  57.887  1.00 34.94  ? 100 LEU B C   1 
ATOM   3699  O  O   . LEU B 1 99  ? 30.983  17.079  58.402  1.00 36.32  ? 100 LEU B O   1 
ATOM   3700  C  CB  . LEU B 1 99  ? 27.914  18.354  58.537  1.00 29.60  ? 100 LEU B CB  1 
ATOM   3701  C  CG  . LEU B 1 99  ? 26.905  18.867  59.566  1.00 37.49  ? 100 LEU B CG  1 
ATOM   3702  C  CD1 . LEU B 1 99  ? 25.475  18.645  59.093  1.00 37.84  ? 100 LEU B CD1 1 
ATOM   3703  C  CD2 . LEU B 1 99  ? 27.139  18.192  60.908  1.00 40.67  ? 100 LEU B CD2 1 
ATOM   3704  N  N   . ALA B 1 100 ? 30.333  18.250  56.588  1.00 36.76  ? 101 ALA B N   1 
ATOM   3705  C  CA  . ALA B 1 100 ? 31.225  17.543  55.676  1.00 35.43  ? 101 ALA B CA  1 
ATOM   3706  C  C   . ALA B 1 100 ? 32.685  17.717  56.090  1.00 41.93  ? 101 ALA B C   1 
ATOM   3707  O  O   . ALA B 1 100 ? 33.470  16.762  56.062  1.00 43.47  ? 101 ALA B O   1 
ATOM   3708  C  CB  . ALA B 1 100 ? 31.015  18.028  54.251  1.00 34.00  ? 101 ALA B CB  1 
ATOM   3709  N  N   . THR B 1 101 ? 33.043  18.937  56.484  1.00 36.07  ? 102 THR B N   1 
ATOM   3710  C  CA  . THR B 1 101 ? 34.403  19.219  56.933  1.00 36.23  ? 102 THR B CA  1 
ATOM   3711  C  C   . THR B 1 101 ? 34.769  18.400  58.171  1.00 37.28  ? 102 THR B C   1 
ATOM   3712  O  O   . THR B 1 101 ? 35.823  17.751  58.204  1.00 39.65  ? 102 THR B O   1 
ATOM   3713  C  CB  . THR B 1 101 ? 34.594  20.716  57.237  1.00 36.44  ? 102 THR B CB  1 
ATOM   3714  O  OG1 . THR B 1 101 ? 34.607  21.450  56.007  1.00 40.32  ? 102 THR B OG1 1 
ATOM   3715  C  CG2 . THR B 1 101 ? 35.909  20.951  57.963  1.00 35.48  ? 102 THR B CG2 1 
ATOM   3716  N  N   . GLN B 1 102 ? 33.901  18.427  59.181  1.00 32.49  ? 103 GLN B N   1 
ATOM   3717  C  CA  . GLN B 1 102 ? 34.124  17.632  60.392  1.00 32.64  ? 103 GLN B CA  1 
ATOM   3718  C  C   . GLN B 1 102 ? 34.296  16.149  60.050  1.00 39.13  ? 103 GLN B C   1 
ATOM   3719  O  O   . GLN B 1 102 ? 35.213  15.472  60.549  1.00 34.39  ? 103 GLN B O   1 
ATOM   3720  C  CB  . GLN B 1 102 ? 32.967  17.816  61.377  1.00 39.12  ? 103 GLN B CB  1 
ATOM   3721  C  CG  . GLN B 1 102 ? 32.785  19.245  61.867  1.00 37.31  ? 103 GLN B CG  1 
ATOM   3722  C  CD  . GLN B 1 102 ? 33.930  19.706  62.747  1.00 39.64  ? 103 GLN B CD  1 
ATOM   3723  O  OE1 . GLN B 1 102 ? 34.427  18.951  63.583  1.00 36.28  ? 103 GLN B OE1 1 
ATOM   3724  N  NE2 . GLN B 1 102 ? 34.357  20.950  62.560  1.00 45.50  ? 103 GLN B NE2 1 
ATOM   3725  N  N   . LEU B 1 103 ? 33.407  15.664  59.186  1.00 33.84  ? 104 LEU B N   1 
ATOM   3726  C  CA  . LEU B 1 103 ? 33.443  14.290  58.698  1.00 33.90  ? 104 LEU B CA  1 
ATOM   3727  C  C   . LEU B 1 103 ? 34.811  13.929  58.126  1.00 34.67  ? 104 LEU B C   1 
ATOM   3728  O  O   . LEU B 1 103 ? 35.464  12.978  58.588  1.00 37.37  ? 104 LEU B O   1 
ATOM   3729  C  CB  . LEU B 1 103 ? 32.356  14.088  57.640  1.00 34.90  ? 104 LEU B CB  1 
ATOM   3730  C  CG  . LEU B 1 103 ? 32.145  12.686  57.071  1.00 38.42  ? 104 LEU B CG  1 
ATOM   3731  C  CD1 . LEU B 1 103 ? 32.186  11.659  58.180  1.00 35.26  ? 104 LEU B CD1 1 
ATOM   3732  C  CD2 . LEU B 1 103 ? 30.819  12.618  56.329  1.00 35.29  ? 104 LEU B CD2 1 
ATOM   3733  N  N   . ARG B 1 104 ? 35.237  14.698  57.126  1.00 38.93  ? 105 ARG B N   1 
ATOM   3734  C  CA  . ARG B 1 104 ? 36.535  14.488  56.494  1.00 43.35  ? 105 ARG B CA  1 
ATOM   3735  C  C   . ARG B 1 104 ? 37.654  14.476  57.529  1.00 41.97  ? 105 ARG B C   1 
ATOM   3736  O  O   . ARG B 1 104 ? 38.489  13.568  57.541  1.00 43.54  ? 105 ARG B O   1 
ATOM   3737  C  CB  . ARG B 1 104 ? 36.811  15.569  55.446  1.00 45.93  ? 105 ARG B CB  1 
ATOM   3738  C  CG  . ARG B 1 104 ? 38.014  15.268  54.562  1.00 55.46  ? 105 ARG B CG  1 
ATOM   3739  C  CD  . ARG B 1 104 ? 38.616  16.532  53.969  1.00 66.61  ? 105 ARG B CD  1 
ATOM   3740  N  NE  . ARG B 1 104 ? 39.201  17.390  54.996  1.00 70.89  ? 105 ARG B NE  1 
ATOM   3741  C  CZ  . ARG B 1 104 ? 38.746  18.599  55.309  1.00 70.82  ? 105 ARG B CZ  1 
ATOM   3742  N  NH1 . ARG B 1 104 ? 37.697  19.100  54.672  1.00 73.53  ? 105 ARG B NH1 1 
ATOM   3743  N  NH2 . ARG B 1 104 ? 39.342  19.308  56.259  1.00 73.65  ? 105 ARG B NH2 1 
ATOM   3744  N  N   . SER B 1 105 ? 37.650  15.482  58.401  1.00 40.03  ? 106 SER B N   1 
ATOM   3745  C  CA  . SER B 1 105 ? 38.671  15.612  59.438  1.00 47.21  ? 106 SER B CA  1 
ATOM   3746  C  C   . SER B 1 105 ? 38.797  14.357  60.302  1.00 32.75  ? 106 SER B C   1 
ATOM   3747  O  O   . SER B 1 105 ? 39.867  13.738  60.363  1.00 33.24  ? 106 SER B O   1 
ATOM   3748  C  CB  . SER B 1 105 ? 38.372  16.822  60.328  1.00 51.24  ? 106 SER B CB  1 
ATOM   3749  O  OG  . SER B 1 105 ? 38.531  18.036  59.614  1.00 58.03  ? 106 SER B OG  1 
ATOM   3750  N  N   . PHE B 1 106 ? 37.707  13.978  60.962  1.00 31.92  ? 107 PHE B N   1 
ATOM   3751  C  CA  . PHE B 1 106 ? 37.762  12.841  61.879  1.00 31.61  ? 107 PHE B CA  1 
ATOM   3752  C  C   . PHE B 1 106 ? 38.057  11.522  61.162  1.00 32.01  ? 107 PHE B C   1 
ATOM   3753  O  O   . PHE B 1 106 ? 38.875  10.722  61.637  1.00 32.10  ? 107 PHE B O   1 
ATOM   3754  C  CB  . PHE B 1 106 ? 36.463  12.736  62.676  1.00 30.83  ? 107 PHE B CB  1 
ATOM   3755  C  CG  . PHE B 1 106 ? 36.401  13.673  63.848  1.00 35.92  ? 107 PHE B CG  1 
ATOM   3756  C  CD1 . PHE B 1 106 ? 36.889  13.285  65.086  1.00 30.78  ? 107 PHE B CD1 1 
ATOM   3757  C  CD2 . PHE B 1 106 ? 35.867  14.945  63.712  1.00 30.62  ? 107 PHE B CD2 1 
ATOM   3758  C  CE1 . PHE B 1 106 ? 36.841  14.145  66.167  1.00 41.64  ? 107 PHE B CE1 1 
ATOM   3759  C  CE2 . PHE B 1 106 ? 35.817  15.810  64.791  1.00 30.62  ? 107 PHE B CE2 1 
ATOM   3760  C  CZ  . PHE B 1 106 ? 36.302  15.410  66.019  1.00 30.73  ? 107 PHE B CZ  1 
ATOM   3761  N  N   . ASP B 1 107 ? 37.409  11.306  60.018  1.00 31.87  ? 108 ASP B N   1 
ATOM   3762  C  CA  . ASP B 1 107 ? 37.626  10.088  59.237  1.00 34.59  ? 108 ASP B CA  1 
ATOM   3763  C  C   . ASP B 1 107 ? 39.103  9.930   58.867  1.00 41.53  ? 108 ASP B C   1 
ATOM   3764  O  O   . ASP B 1 107 ? 39.750  8.899   59.170  1.00 43.70  ? 108 ASP B O   1 
ATOM   3765  C  CB  . ASP B 1 107 ? 36.758  10.113  57.976  1.00 40.79  ? 108 ASP B CB  1 
ATOM   3766  C  CG  . ASP B 1 107 ? 36.784  8.802   57.221  1.00 47.00  ? 108 ASP B CG  1 
ATOM   3767  O  OD1 . ASP B 1 107 ? 36.903  7.741   57.869  1.00 51.23  ? 108 ASP B OD1 1 
ATOM   3768  O  OD2 . ASP B 1 107 ? 36.677  8.833   55.976  1.00 50.02  ? 108 ASP B OD2 1 
ATOM   3769  N  N   . ASP B 1 108 ? 39.630  10.972  58.228  1.00 33.64  ? 109 ASP B N   1 
ATOM   3770  C  CA  . ASP B 1 108 ? 41.030  11.003  57.828  1.00 36.58  ? 109 ASP B CA  1 
ATOM   3771  C  C   . ASP B 1 108 ? 41.947  10.801  59.026  1.00 39.92  ? 109 ASP B C   1 
ATOM   3772  O  O   . ASP B 1 108 ? 42.969  10.121  58.919  1.00 38.59  ? 109 ASP B O   1 
ATOM   3773  C  CB  . ASP B 1 108 ? 41.362  12.321  57.126  1.00 40.48  ? 109 ASP B CB  1 
ATOM   3774  C  CG  . ASP B 1 108 ? 41.017  12.296  55.649  1.00 49.26  ? 109 ASP B CG  1 
ATOM   3775  O  OD1 . ASP B 1 108 ? 40.302  11.366  55.221  1.00 50.21  ? 109 ASP B OD1 1 
ATOM   3776  O  OD2 . ASP B 1 108 ? 41.457  13.210  54.918  1.00 52.06  ? 109 ASP B OD2 1 
ATOM   3777  N  N   . HIS B 1 109 ? 41.580  11.377  60.168  1.00 34.06  ? 110 HIS B N   1 
ATOM   3778  C  CA  . HIS B 1 109 ? 42.401  11.211  61.363  1.00 38.04  ? 110 HIS B CA  1 
ATOM   3779  C  C   . HIS B 1 109 ? 42.458  9.759   61.830  1.00 38.65  ? 110 HIS B C   1 
ATOM   3780  O  O   . HIS B 1 109 ? 43.538  9.229   62.074  1.00 39.35  ? 110 HIS B O   1 
ATOM   3781  C  CB  . HIS B 1 109 ? 41.902  12.085  62.510  1.00 37.42  ? 110 HIS B CB  1 
ATOM   3782  C  CG  . HIS B 1 109 ? 42.775  12.025  63.724  1.00 41.01  ? 110 HIS B CG  1 
ATOM   3783  N  ND1 . HIS B 1 109 ? 44.145  12.162  63.660  1.00 40.41  ? 110 HIS B ND1 1 
ATOM   3784  C  CD2 . HIS B 1 109 ? 42.478  11.823  65.030  1.00 40.40  ? 110 HIS B CD2 1 
ATOM   3785  C  CE1 . HIS B 1 109 ? 44.654  12.058  64.875  1.00 35.18  ? 110 HIS B CE1 1 
ATOM   3786  N  NE2 . HIS B 1 109 ? 43.663  11.852  65.725  1.00 34.41  ? 110 HIS B NE2 1 
ATOM   3787  N  N   . PHE B 1 110 ? 41.299  9.121   61.965  1.00 33.63  ? 111 PHE B N   1 
ATOM   3788  C  CA  . PHE B 1 110 ? 41.261  7.736   62.430  1.00 38.25  ? 111 PHE B CA  1 
ATOM   3789  C  C   . PHE B 1 110 ? 42.036  6.816   61.479  1.00 33.89  ? 111 PHE B C   1 
ATOM   3790  O  O   . PHE B 1 110 ? 42.859  5.974   61.919  1.00 34.31  ? 111 PHE B O   1 
ATOM   3791  C  CB  . PHE B 1 110 ? 39.811  7.273   62.587  1.00 36.25  ? 111 PHE B CB  1 
ATOM   3792  C  CG  . PHE B 1 110 ? 39.060  8.002   63.671  1.00 38.65  ? 111 PHE B CG  1 
ATOM   3793  C  CD1 . PHE B 1 110 ? 39.701  8.381   64.839  1.00 39.84  ? 111 PHE B CD1 1 
ATOM   3794  C  CD2 . PHE B 1 110 ? 37.719  8.317   63.518  1.00 31.80  ? 111 PHE B CD2 1 
ATOM   3795  C  CE1 . PHE B 1 110 ? 39.019  9.054   65.839  1.00 33.85  ? 111 PHE B CE1 1 
ATOM   3796  C  CE2 . PHE B 1 110 ? 37.030  8.992   64.515  1.00 32.17  ? 111 PHE B CE2 1 
ATOM   3797  C  CZ  . PHE B 1 110 ? 37.683  9.360   65.676  1.00 34.29  ? 111 PHE B CZ  1 
ATOM   3798  N  N   . GLN B 1 111 ? 41.802  7.001   60.177  1.00 34.14  ? 112 GLN B N   1 
ATOM   3799  C  CA  . GLN B 1 111 ? 42.563  6.250   59.178  1.00 34.98  ? 112 GLN B CA  1 
ATOM   3800  C  C   . GLN B 1 111 ? 44.072  6.460   59.343  1.00 50.58  ? 112 GLN B C   1 
ATOM   3801  O  O   . GLN B 1 111 ? 44.850  5.502   59.304  1.00 48.65  ? 112 GLN B O   1 
ATOM   3802  C  CB  . GLN B 1 111 ? 42.139  6.639   57.762  1.00 35.31  ? 112 GLN B CB  1 
ATOM   3803  C  CG  . GLN B 1 111 ? 40.721  6.239   57.404  1.00 34.76  ? 112 GLN B CG  1 
ATOM   3804  C  CD  . GLN B 1 111 ? 40.405  6.489   55.944  1.00 51.75  ? 112 GLN B CD  1 
ATOM   3805  O  OE1 . GLN B 1 111 ? 41.191  6.145   55.060  1.00 56.38  ? 112 GLN B OE1 1 
ATOM   3806  N  NE2 . GLN B 1 111 ? 39.253  7.094   55.682  1.00 57.34  ? 112 GLN B NE2 1 
ATOM   3807  N  N   . HIS B 1 112 ? 44.475  7.714   59.534  1.00 50.52  ? 113 HIS B N   1 
ATOM   3808  C  CA  . HIS B 1 112 ? 45.884  8.051   59.727  1.00 36.86  ? 113 HIS B CA  1 
ATOM   3809  C  C   . HIS B 1 112 ? 46.467  7.374   60.955  1.00 45.44  ? 113 HIS B C   1 
ATOM   3810  O  O   . HIS B 1 112 ? 47.629  6.972   60.962  1.00 37.69  ? 113 HIS B O   1 
ATOM   3811  C  CB  . HIS B 1 112 ? 46.065  9.564   59.848  1.00 37.03  ? 113 HIS B CB  1 
ATOM   3812  C  CG  . HIS B 1 112 ? 46.038  10.278  58.535  1.00 46.99  ? 113 HIS B CG  1 
ATOM   3813  N  ND1 . HIS B 1 112 ? 45.600  11.577  58.401  1.00 47.83  ? 113 HIS B ND1 1 
ATOM   3814  C  CD2 . HIS B 1 112 ? 46.400  9.872   57.296  1.00 47.76  ? 113 HIS B CD2 1 
ATOM   3815  C  CE1 . HIS B 1 112 ? 45.688  11.939  57.133  1.00 49.08  ? 113 HIS B CE1 1 
ATOM   3816  N  NE2 . HIS B 1 112 ? 46.170  10.923  56.442  1.00 51.32  ? 113 HIS B NE2 1 
ATOM   3817  N  N   . LEU B 1 113 ? 45.653  7.261   61.996  1.00 35.98  ? 114 LEU B N   1 
ATOM   3818  C  CA  . LEU B 1 113 ? 46.095  6.666   63.243  1.00 38.63  ? 114 LEU B CA  1 
ATOM   3819  C  C   . LEU B 1 113 ? 46.364  5.183   63.042  1.00 36.30  ? 114 LEU B C   1 
ATOM   3820  O  O   . LEU B 1 113 ? 47.423  4.669   63.433  1.00 45.12  ? 114 LEU B O   1 
ATOM   3821  C  CB  . LEU B 1 113 ? 45.051  6.878   64.332  1.00 35.15  ? 114 LEU B CB  1 
ATOM   3822  C  CG  . LEU B 1 113 ? 45.616  7.138   65.723  1.00 50.99  ? 114 LEU B CG  1 
ATOM   3823  C  CD1 . LEU B 1 113 ? 46.394  8.444   65.750  1.00 53.82  ? 114 LEU B CD1 1 
ATOM   3824  C  CD2 . LEU B 1 113 ? 44.486  7.164   66.713  1.00 49.23  ? 114 LEU B CD2 1 
ATOM   3825  N  N   . LEU B 1 114 ? 45.409  4.499   62.417  1.00 47.30  ? 115 LEU B N   1 
ATOM   3826  C  CA  . LEU B 1 114 ? 45.608  3.077   62.135  1.00 36.22  ? 115 LEU B CA  1 
ATOM   3827  C  C   . LEU B 1 114 ? 46.836  2.851   61.238  1.00 48.21  ? 115 LEU B C   1 
ATOM   3828  O  O   . LEU B 1 114 ? 47.711  2.017   61.535  1.00 37.91  ? 115 LEU B O   1 
ATOM   3829  C  CB  . LEU B 1 114 ? 44.357  2.484   61.486  1.00 35.75  ? 115 LEU B CB  1 
ATOM   3830  C  CG  . LEU B 1 114 ? 44.323  0.960   61.374  1.00 37.63  ? 115 LEU B CG  1 
ATOM   3831  C  CD1 . LEU B 1 114 ? 44.611  0.324   62.724  1.00 37.45  ? 115 LEU B CD1 1 
ATOM   3832  C  CD2 . LEU B 1 114 ? 42.976  0.499   60.841  1.00 35.66  ? 115 LEU B CD2 1 
ATOM   3833  N  N   . ASN B 1 115 ? 46.903  3.615   60.151  1.00 43.18  ? 116 ASN B N   1 
ATOM   3834  C  CA  . ASN B 1 115 ? 48.005  3.503   59.200  1.00 46.90  ? 116 ASN B CA  1 
ATOM   3835  C  C   . ASN B 1 115 ? 49.377  3.746   59.829  1.00 46.73  ? 116 ASN B C   1 
ATOM   3836  O  O   . ASN B 1 115 ? 50.336  3.029   59.540  1.00 41.70  ? 116 ASN B O   1 
ATOM   3837  C  CB  . ASN B 1 115 ? 47.792  4.473   58.037  1.00 48.66  ? 116 ASN B CB  1 
ATOM   3838  C  CG  . ASN B 1 115 ? 46.849  3.923   56.984  1.00 55.84  ? 116 ASN B CG  1 
ATOM   3839  O  OD1 . ASN B 1 115 ? 46.253  2.860   57.161  1.00 54.20  ? 116 ASN B OD1 1 
ATOM   3840  N  ND2 . ASN B 1 115 ? 46.711  4.647   55.880  1.00 62.89  ? 116 ASN B ND2 1 
ATOM   3841  N  N   . ASP B 1 116 ? 49.470  4.754   60.691  1.00 39.20  ? 117 ASP B N   1 
ATOM   3842  C  CA  . ASP B 1 116 ? 50.732  5.062   61.355  1.00 55.06  ? 117 ASP B CA  1 
ATOM   3843  C  C   . ASP B 1 116 ? 51.066  4.010   62.403  1.00 49.30  ? 117 ASP B C   1 
ATOM   3844  O  O   . ASP B 1 116 ? 52.242  3.754   62.681  1.00 48.82  ? 117 ASP B O   1 
ATOM   3845  C  CB  . ASP B 1 116 ? 50.690  6.452   61.986  1.00 53.52  ? 117 ASP B CB  1 
ATOM   3846  C  CG  . ASP B 1 116 ? 50.865  7.555   60.962  1.00 61.53  ? 117 ASP B CG  1 
ATOM   3847  O  OD1 . ASP B 1 116 ? 51.451  7.281   59.893  1.00 65.41  ? 117 ASP B OD1 1 
ATOM   3848  O  OD2 . ASP B 1 116 ? 50.417  8.690   61.223  1.00 60.75  ? 117 ASP B OD2 1 
ATOM   3849  N  N   . SER B 1 117 ? 50.034  3.407   62.987  1.00 44.04  ? 118 SER B N   1 
ATOM   3850  C  CA  . SER B 1 117 ? 50.244  2.234   63.825  1.00 45.60  ? 118 SER B CA  1 
ATOM   3851  C  C   . SER B 1 117 ? 50.958  1.151   63.021  1.00 46.82  ? 118 SER B C   1 
ATOM   3852  O  O   . SER B 1 117 ? 52.021  0.654   63.423  1.00 40.86  ? 118 SER B O   1 
ATOM   3853  C  CB  . SER B 1 117 ? 48.918  1.704   64.366  1.00 49.84  ? 118 SER B CB  1 
ATOM   3854  O  OG  . SER B 1 117 ? 49.050  0.355   64.780  1.00 40.00  ? 118 SER B OG  1 
ATOM   3855  N  N   . GLU B 1 118 ? 50.381  0.809   61.870  1.00 45.34  ? 119 GLU B N   1 
ATOM   3856  C  CA  . GLU B 1 118 ? 50.969  -0.218  61.009  1.00 44.37  ? 119 GLU B CA  1 
ATOM   3857  C  C   . GLU B 1 118 ? 52.395  0.125   60.568  1.00 47.93  ? 119 GLU B C   1 
ATOM   3858  O  O   . GLU B 1 118 ? 53.267  -0.747  60.536  1.00 51.12  ? 119 GLU B O   1 
ATOM   3859  C  CB  . GLU B 1 118 ? 50.098  -0.453  59.774  1.00 42.14  ? 119 GLU B CB  1 
ATOM   3860  C  CG  . GLU B 1 118 ? 50.596  -1.587  58.890  1.00 45.58  ? 119 GLU B CG  1 
ATOM   3861  C  CD  . GLU B 1 118 ? 49.721  -1.813  57.674  1.00 51.43  ? 119 GLU B CD  1 
ATOM   3862  O  OE1 . GLU B 1 118 ? 48.832  -0.978  57.416  1.00 49.10  ? 119 GLU B OE1 1 
ATOM   3863  O  OE2 . GLU B 1 118 ? 49.925  -2.827  56.973  1.00 61.71  ? 119 GLU B OE2 1 
ATOM   3864  N  N   . ARG B 1 119 ? 52.629  1.389   60.228  1.00 42.17  ? 120 ARG B N   1 
ATOM   3865  C  CA  . ARG B 1 119 ? 53.949  1.823   59.774  1.00 43.46  ? 120 ARG B CA  1 
ATOM   3866  C  C   . ARG B 1 119 ? 54.983  1.740   60.890  1.00 44.01  ? 120 ARG B C   1 
ATOM   3867  O  O   . ARG B 1 119 ? 56.128  1.345   60.655  1.00 45.20  ? 120 ARG B O   1 
ATOM   3868  C  CB  . ARG B 1 119 ? 53.891  3.247   59.218  1.00 58.42  ? 120 ARG B CB  1 
ATOM   3869  C  CG  . ARG B 1 119 ? 54.005  3.316   57.704  1.00 61.66  ? 120 ARG B CG  1 
ATOM   3870  C  CD  . ARG B 1 119 ? 53.989  4.751   57.214  1.00 63.19  ? 120 ARG B CD  1 
ATOM   3871  N  NE  . ARG B 1 119 ? 52.706  5.397   57.474  1.00 65.67  ? 120 ARG B NE  1 
ATOM   3872  C  CZ  . ARG B 1 119 ? 51.860  5.784   56.525  1.00 65.15  ? 120 ARG B CZ  1 
ATOM   3873  N  NH1 . ARG B 1 119 ? 50.714  6.363   56.853  1.00 56.32  ? 120 ARG B NH1 1 
ATOM   3874  N  NH2 . ARG B 1 119 ? 52.160  5.590   55.248  1.00 70.13  ? 120 ARG B NH2 1 
ATOM   3875  N  N   . THR B 1 120 ? 54.581  2.119   62.100  1.00 43.25  ? 121 THR B N   1 
ATOM   3876  C  CA  . THR B 1 120 ? 55.442  1.951   63.265  1.00 43.78  ? 121 THR B CA  1 
ATOM   3877  C  C   . THR B 1 120 ? 55.791  0.476   63.421  1.00 53.01  ? 121 THR B C   1 
ATOM   3878  O  O   . THR B 1 120 ? 56.959  0.115   63.615  1.00 53.92  ? 121 THR B O   1 
ATOM   3879  C  CB  . THR B 1 120 ? 54.774  2.463   64.555  1.00 42.90  ? 121 THR B CB  1 
ATOM   3880  O  OG1 . THR B 1 120 ? 54.655  3.890   64.503  1.00 42.79  ? 121 THR B OG1 1 
ATOM   3881  C  CG2 . THR B 1 120 ? 55.601  2.078   65.775  1.00 43.55  ? 121 THR B CG2 1 
ATOM   3882  N  N   . LEU B 1 121 ? 54.767  -0.370  63.315  1.00 43.35  ? 122 LEU B N   1 
ATOM   3883  C  CA  . LEU B 1 121 ? 54.953  -1.814  63.408  1.00 48.96  ? 122 LEU B CA  1 
ATOM   3884  C  C   . LEU B 1 121 ? 56.005  -2.310  62.420  1.00 47.34  ? 122 LEU B C   1 
ATOM   3885  O  O   . LEU B 1 121 ? 56.965  -2.966  62.812  1.00 45.88  ? 122 LEU B O   1 
ATOM   3886  C  CB  . LEU B 1 121 ? 53.628  -2.544  63.174  1.00 50.81  ? 122 LEU B CB  1 
ATOM   3887  C  CG  . LEU B 1 121 ? 53.662  -4.073  63.255  1.00 47.01  ? 122 LEU B CG  1 
ATOM   3888  C  CD1 . LEU B 1 121 ? 52.442  -4.575  63.997  1.00 48.89  ? 122 LEU B CD1 1 
ATOM   3889  C  CD2 . LEU B 1 121 ? 53.731  -4.703  61.871  1.00 49.29  ? 122 LEU B CD2 1 
ATOM   3890  N  N   . GLN B 1 122 ? 55.820  -1.991  61.142  1.00 45.86  ? 123 GLN B N   1 
ATOM   3891  C  CA  . GLN B 1 122 ? 56.762  -2.404  60.106  1.00 48.84  ? 123 GLN B CA  1 
ATOM   3892  C  C   . GLN B 1 122 ? 58.167  -1.872  60.373  1.00 56.61  ? 123 GLN B C   1 
ATOM   3893  O  O   . GLN B 1 122 ? 59.159  -2.563  60.138  1.00 56.69  ? 123 GLN B O   1 
ATOM   3894  C  CB  . GLN B 1 122 ? 56.292  -1.932  58.730  1.00 46.50  ? 123 GLN B CB  1 
ATOM   3895  C  CG  . GLN B 1 122 ? 54.962  -2.503  58.284  1.00 61.96  ? 123 GLN B CG  1 
ATOM   3896  C  CD  . GLN B 1 122 ? 54.526  -1.957  56.940  1.00 61.75  ? 123 GLN B CD  1 
ATOM   3897  O  OE1 . GLN B 1 122 ? 54.984  -0.898  56.511  1.00 64.99  ? 123 GLN B OE1 1 
ATOM   3898  N  NE2 . GLN B 1 122 ? 53.637  -2.677  56.268  1.00 65.41  ? 123 GLN B NE2 1 
ATOM   3899  N  N   . ALA B 1 123 ? 58.243  -0.643  60.872  1.00 51.85  ? 124 ALA B N   1 
ATOM   3900  C  CA  . ALA B 1 123 ? 59.526  0.018   61.070  1.00 58.77  ? 124 ALA B CA  1 
ATOM   3901  C  C   . ALA B 1 123 ? 60.305  -0.526  62.268  1.00 61.21  ? 124 ALA B C   1 
ATOM   3902  O  O   . ALA B 1 123 ? 61.533  -0.447  62.291  1.00 50.43  ? 124 ALA B O   1 
ATOM   3903  C  CB  . ALA B 1 123 ? 59.322  1.520   61.224  1.00 48.28  ? 124 ALA B CB  1 
ATOM   3904  N  N   . THR B 1 124 ? 59.607  -1.070  63.263  1.00 58.31  ? 125 THR B N   1 
ATOM   3905  C  CA  . THR B 1 124 ? 60.289  -1.471  64.495  1.00 58.39  ? 125 THR B CA  1 
ATOM   3906  C  C   . THR B 1 124 ? 60.235  -2.964  64.830  1.00 55.71  ? 125 THR B C   1 
ATOM   3907  O  O   . THR B 1 124 ? 60.903  -3.410  65.763  1.00 49.34  ? 125 THR B O   1 
ATOM   3908  C  CB  . THR B 1 124 ? 59.730  -0.707  65.710  1.00 47.82  ? 125 THR B CB  1 
ATOM   3909  O  OG1 . THR B 1 124 ? 58.475  -1.277  66.102  1.00 56.01  ? 125 THR B OG1 1 
ATOM   3910  C  CG2 . THR B 1 124 ? 59.552  0.771   65.384  1.00 55.75  ? 125 THR B CG2 1 
ATOM   3911  N  N   . PHE B 1 125 ? 59.451  -3.737  64.087  1.00 55.53  ? 126 PHE B N   1 
ATOM   3912  C  CA  . PHE B 1 125 ? 59.294  -5.159  64.404  1.00 58.79  ? 126 PHE B CA  1 
ATOM   3913  C  C   . PHE B 1 125 ? 60.470  -6.062  63.994  1.00 62.42  ? 126 PHE B C   1 
ATOM   3914  O  O   . PHE B 1 125 ? 60.825  -6.965  64.755  1.00 60.47  ? 126 PHE B O   1 
ATOM   3915  C  CB  . PHE B 1 125 ? 58.002  -5.705  63.788  1.00 55.12  ? 126 PHE B CB  1 
ATOM   3916  C  CG  . PHE B 1 125 ? 56.859  -5.782  64.759  1.00 56.61  ? 126 PHE B CG  1 
ATOM   3917  C  CD1 . PHE B 1 125 ? 56.823  -4.956  65.871  1.00 56.73  ? 126 PHE B CD1 1 
ATOM   3918  C  CD2 . PHE B 1 125 ? 55.833  -6.694  64.574  1.00 57.83  ? 126 PHE B CD2 1 
ATOM   3919  C  CE1 . PHE B 1 125 ? 55.777  -5.027  66.771  1.00 56.25  ? 126 PHE B CE1 1 
ATOM   3920  C  CE2 . PHE B 1 125 ? 54.786  -6.772  65.473  1.00 54.62  ? 126 PHE B CE2 1 
ATOM   3921  C  CZ  . PHE B 1 125 ? 54.757  -5.937  66.572  1.00 55.99  ? 126 PHE B CZ  1 
ATOM   3922  N  N   . PRO B 1 126 ? 61.065  -5.849  62.799  1.00 69.98  ? 127 PRO B N   1 
ATOM   3923  C  CA  . PRO B 1 126 ? 62.219  -6.691  62.458  1.00 73.15  ? 127 PRO B CA  1 
ATOM   3924  C  C   . PRO B 1 126 ? 63.342  -6.656  63.496  1.00 69.12  ? 127 PRO B C   1 
ATOM   3925  O  O   . PRO B 1 126 ? 63.930  -7.694  63.788  1.00 72.60  ? 127 PRO B O   1 
ATOM   3926  C  CB  . PRO B 1 126 ? 62.697  -6.099  61.130  1.00 75.17  ? 127 PRO B CB  1 
ATOM   3927  C  CG  . PRO B 1 126 ? 61.464  -5.568  60.511  1.00 73.48  ? 127 PRO B CG  1 
ATOM   3928  C  CD  . PRO B 1 126 ? 60.649  -5.020  61.650  1.00 71.43  ? 127 PRO B CD  1 
ATOM   3929  N  N   . GLY B 1 127 ? 63.625  -5.484  64.053  1.00 63.03  ? 128 GLY B N   1 
ATOM   3930  C  CA  . GLY B 1 127 ? 64.664  -5.365  65.061  1.00 53.88  ? 128 GLY B CA  1 
ATOM   3931  C  C   . GLY B 1 127 ? 64.271  -6.006  66.380  1.00 67.19  ? 128 GLY B C   1 
ATOM   3932  O  O   . GLY B 1 127 ? 65.122  -6.306  67.217  1.00 69.86  ? 128 GLY B O   1 
ATOM   3933  N  N   . ALA B 1 128 ? 62.972  -6.225  66.553  1.00 65.37  ? 129 ALA B N   1 
ATOM   3934  C  CA  . ALA B 1 128 ? 62.415  -6.742  67.799  1.00 64.89  ? 129 ALA B CA  1 
ATOM   3935  C  C   . ALA B 1 128 ? 62.354  -8.254  67.836  1.00 51.80  ? 129 ALA B C   1 
ATOM   3936  O  O   . ALA B 1 128 ? 62.859  -8.901  68.753  1.00 52.54  ? 129 ALA B O   1 
ATOM   3937  C  CB  . ALA B 1 128 ? 61.032  -6.197  68.001  1.00 49.91  ? 129 ALA B CB  1 
ATOM   3938  N  N   . PHE B 1 129 ? 61.690  -8.800  66.830  1.00 51.33  ? 130 PHE B N   1 
ATOM   3939  C  CA  . PHE B 1 129 ? 61.322  -10.198 66.825  1.00 65.84  ? 130 PHE B CA  1 
ATOM   3940  C  C   . PHE B 1 129 ? 62.001  -10.897 65.660  1.00 52.48  ? 130 PHE B C   1 
ATOM   3941  O  O   . PHE B 1 129 ? 61.919  -12.113 65.521  1.00 58.24  ? 130 PHE B O   1 
ATOM   3942  C  CB  . PHE B 1 129 ? 59.799  -10.333 66.750  1.00 50.09  ? 130 PHE B CB  1 
ATOM   3943  C  CG  . PHE B 1 129 ? 59.072  -9.536  67.801  1.00 49.10  ? 130 PHE B CG  1 
ATOM   3944  C  CD1 . PHE B 1 129 ? 59.182  -9.872  69.141  1.00 49.38  ? 130 PHE B CD1 1 
ATOM   3945  C  CD2 . PHE B 1 129 ? 58.291  -8.445  67.452  1.00 58.93  ? 130 PHE B CD2 1 
ATOM   3946  C  CE1 . PHE B 1 129 ? 58.521  -9.142  70.113  1.00 55.06  ? 130 PHE B CE1 1 
ATOM   3947  C  CE2 . PHE B 1 129 ? 57.627  -7.709  68.421  1.00 53.56  ? 130 PHE B CE2 1 
ATOM   3948  C  CZ  . PHE B 1 129 ? 57.743  -8.060  69.753  1.00 47.50  ? 130 PHE B CZ  1 
ATOM   3949  N  N   . GLY B 1 130 ? 62.683  -10.115 64.829  1.00 64.53  ? 131 GLY B N   1 
ATOM   3950  C  CA  . GLY B 1 130 ? 63.406  -10.666 63.701  1.00 70.47  ? 131 GLY B CA  1 
ATOM   3951  C  C   . GLY B 1 130 ? 62.507  -11.302 62.662  1.00 69.25  ? 131 GLY B C   1 
ATOM   3952  O  O   . GLY B 1 130 ? 61.542  -10.695 62.179  1.00 52.68  ? 131 GLY B O   1 
ATOM   3953  N  N   . GLU B 1 131 ? 62.831  -12.542 62.315  1.00 71.37  ? 132 GLU B N   1 
ATOM   3954  C  CA  . GLU B 1 131 ? 62.084  -13.257 61.295  1.00 77.90  ? 132 GLU B CA  1 
ATOM   3955  C  C   . GLU B 1 131 ? 60.890  -13.995 61.878  1.00 73.10  ? 132 GLU B C   1 
ATOM   3956  O  O   . GLU B 1 131 ? 60.149  -14.657 61.157  1.00 78.22  ? 132 GLU B O   1 
ATOM   3957  C  CB  . GLU B 1 131 ? 63.007  -14.201 60.521  1.00 89.37  ? 132 GLU B CB  1 
ATOM   3958  C  CG  . GLU B 1 131 ? 64.076  -13.424 59.753  1.00 99.77  ? 132 GLU B CG  1 
ATOM   3959  C  CD  . GLU B 1 131 ? 65.235  -14.267 59.269  1.00 108.89 ? 132 GLU B CD  1 
ATOM   3960  O  OE1 . GLU B 1 131 ? 66.136  -14.577 60.074  1.00 112.97 ? 132 GLU B OE1 1 
ATOM   3961  O  OE2 . GLU B 1 131 ? 65.258  -14.587 58.063  1.00 113.08 ? 132 GLU B OE2 1 
ATOM   3962  N  N   . LEU B 1 132 ? 60.693  -13.855 63.185  1.00 63.40  ? 133 LEU B N   1 
ATOM   3963  C  CA  . LEU B 1 132 ? 59.402  -14.174 63.776  1.00 51.97  ? 133 LEU B CA  1 
ATOM   3964  C  C   . LEU B 1 132 ? 58.377  -13.260 63.125  1.00 61.77  ? 133 LEU B C   1 
ATOM   3965  O  O   . LEU B 1 132 ? 57.264  -13.679 62.803  1.00 61.07  ? 133 LEU B O   1 
ATOM   3966  C  CB  . LEU B 1 132 ? 59.403  -13.985 65.296  1.00 51.61  ? 133 LEU B CB  1 
ATOM   3967  C  CG  . LEU B 1 132 ? 60.341  -14.827 66.162  1.00 62.49  ? 133 LEU B CG  1 
ATOM   3968  C  CD1 . LEU B 1 132 ? 59.899  -14.759 67.613  1.00 63.05  ? 133 LEU B CD1 1 
ATOM   3969  C  CD2 . LEU B 1 132 ? 60.383  -16.265 65.679  1.00 64.57  ? 133 LEU B CD2 1 
ATOM   3970  N  N   . TYR B 1 133 ? 58.770  -12.004 62.925  1.00 57.56  ? 134 TYR B N   1 
ATOM   3971  C  CA  . TYR B 1 133 ? 57.923  -11.048 62.228  1.00 56.25  ? 134 TYR B CA  1 
ATOM   3972  C  C   . TYR B 1 133 ? 58.118  -11.082 60.715  1.00 52.91  ? 134 TYR B C   1 
ATOM   3973  O  O   . TYR B 1 133 ? 57.144  -11.225 59.978  1.00 53.22  ? 134 TYR B O   1 
ATOM   3974  C  CB  . TYR B 1 133 ? 58.163  -9.619  62.724  1.00 60.81  ? 134 TYR B CB  1 
ATOM   3975  C  CG  . TYR B 1 133 ? 57.687  -8.579  61.729  1.00 59.31  ? 134 TYR B CG  1 
ATOM   3976  C  CD1 . TYR B 1 133 ? 56.333  -8.306  61.574  1.00 60.50  ? 134 TYR B CD1 1 
ATOM   3977  C  CD2 . TYR B 1 133 ? 58.588  -7.881  60.934  1.00 62.56  ? 134 TYR B CD2 1 
ATOM   3978  C  CE1 . TYR B 1 133 ? 55.891  -7.365  60.659  1.00 62.74  ? 134 TYR B CE1 1 
ATOM   3979  C  CE2 . TYR B 1 133 ? 58.156  -6.940  60.016  1.00 62.57  ? 134 TYR B CE2 1 
ATOM   3980  C  CZ  . TYR B 1 133 ? 56.808  -6.685  59.884  1.00 60.49  ? 134 TYR B CZ  1 
ATOM   3981  O  OH  . TYR B 1 133 ? 56.376  -5.747  58.974  1.00 56.07  ? 134 TYR B OH  1 
ATOM   3982  N  N   . THR B 1 134 ? 59.356  -10.938 60.241  1.00 51.40  ? 135 THR B N   1 
ATOM   3983  C  CA  . THR B 1 134 ? 59.549  -10.710 58.804  1.00 70.43  ? 135 THR B CA  1 
ATOM   3984  C  C   . THR B 1 134 ? 59.142  -11.911 57.944  1.00 69.02  ? 135 THR B C   1 
ATOM   3985  O  O   . THR B 1 134 ? 58.966  -11.774 56.734  1.00 72.63  ? 135 THR B O   1 
ATOM   3986  C  CB  . THR B 1 134 ? 61.007  -10.332 58.456  1.00 53.48  ? 135 THR B CB  1 
ATOM   3987  O  OG1 . THR B 1 134 ? 61.913  -11.224 59.105  1.00 54.42  ? 135 THR B OG1 1 
ATOM   3988  C  CG2 . THR B 1 134 ? 61.312  -8.913  58.907  1.00 66.27  ? 135 THR B CG2 1 
ATOM   3989  N  N   . GLN B 1 135 ? 58.982  -13.078 58.560  1.00 68.86  ? 136 GLN B N   1 
ATOM   3990  C  CA  . GLN B 1 135 ? 58.469  -14.238 57.836  1.00 68.89  ? 136 GLN B CA  1 
ATOM   3991  C  C   . GLN B 1 135 ? 56.946  -14.280 57.899  1.00 69.21  ? 136 GLN B C   1 
ATOM   3992  O  O   . GLN B 1 135 ? 56.308  -15.062 57.194  1.00 70.85  ? 136 GLN B O   1 
ATOM   3993  C  CB  . GLN B 1 135 ? 59.053  -15.538 58.394  1.00 69.22  ? 136 GLN B CB  1 
ATOM   3994  N  N   . ASN B 1 136 ? 56.369  -13.429 58.742  1.00 69.35  ? 137 ASN B N   1 
ATOM   3995  C  CA  . ASN B 1 136 ? 54.925  -13.417 58.954  1.00 66.25  ? 137 ASN B CA  1 
ATOM   3996  C  C   . ASN B 1 136 ? 54.295  -12.048 58.709  1.00 67.34  ? 137 ASN B C   1 
ATOM   3997  O  O   . ASN B 1 136 ? 53.209  -11.763 59.213  1.00 70.65  ? 137 ASN B O   1 
ATOM   3998  C  CB  . ASN B 1 136 ? 54.603  -13.881 60.375  1.00 61.88  ? 137 ASN B CB  1 
ATOM   3999  C  CG  . ASN B 1 136 ? 55.102  -15.284 60.656  1.00 58.02  ? 137 ASN B CG  1 
ATOM   4000  O  OD1 . ASN B 1 136 ? 54.896  -16.199 59.860  1.00 51.18  ? 137 ASN B OD1 1 
ATOM   4001  N  ND2 . ASN B 1 136 ? 55.777  -15.456 61.785  1.00 59.25  ? 137 ASN B ND2 1 
ATOM   4002  N  N   . ALA B 1 137 ? 54.978  -11.212 57.932  1.00 65.54  ? 138 ALA B N   1 
ATOM   4003  C  CA  . ALA B 1 137 ? 54.523  -9.849  57.666  1.00 57.87  ? 138 ALA B CA  1 
ATOM   4004  C  C   . ALA B 1 137 ? 53.140  -9.812  57.014  1.00 62.21  ? 138 ALA B C   1 
ATOM   4005  O  O   . ALA B 1 137 ? 52.317  -8.940  57.320  1.00 62.12  ? 138 ALA B O   1 
ATOM   4006  C  CB  . ALA B 1 137 ? 55.533  -9.126  56.790  1.00 55.48  ? 138 ALA B CB  1 
ATOM   4007  N  N   . ARG B 1 138 ? 52.895  -10.766 56.119  1.00 57.07  ? 139 ARG B N   1 
ATOM   4008  C  CA  . ARG B 1 138 ? 51.630  -10.845 55.396  1.00 57.35  ? 139 ARG B CA  1 
ATOM   4009  C  C   . ARG B 1 138 ? 50.445  -10.978 56.350  1.00 57.51  ? 139 ARG B C   1 
ATOM   4010  O  O   . ARG B 1 138 ? 49.388  -10.387 56.124  1.00 58.96  ? 139 ARG B O   1 
ATOM   4011  C  CB  . ARG B 1 138 ? 51.649  -12.019 54.415  1.00 53.08  ? 139 ARG B CB  1 
ATOM   4012  N  N   . ALA B 1 139 ? 50.634  -11.749 57.416  1.00 53.89  ? 140 ALA B N   1 
ATOM   4013  C  CA  . ALA B 1 139 ? 49.595  -11.942 58.424  1.00 52.20  ? 140 ALA B CA  1 
ATOM   4014  C  C   . ALA B 1 139 ? 49.189  -10.617 59.064  1.00 50.75  ? 140 ALA B C   1 
ATOM   4015  O  O   . ALA B 1 139 ? 48.009  -10.253 59.070  1.00 50.18  ? 140 ALA B O   1 
ATOM   4016  C  CB  . ALA B 1 139 ? 50.069  -12.921 59.488  1.00 53.94  ? 140 ALA B CB  1 
ATOM   4017  N  N   . PHE B 1 140 ? 50.177  -9.900  59.595  1.00 50.70  ? 141 PHE B N   1 
ATOM   4018  C  CA  . PHE B 1 140 ? 49.948  -8.606  60.231  1.00 51.55  ? 141 PHE B CA  1 
ATOM   4019  C  C   . PHE B 1 140 ? 49.309  -7.615  59.261  1.00 46.95  ? 141 PHE B C   1 
ATOM   4020  O  O   . PHE B 1 140 ? 48.357  -6.906  59.614  1.00 51.51  ? 141 PHE B O   1 
ATOM   4021  C  CB  . PHE B 1 140 ? 51.263  -8.039  60.774  1.00 51.13  ? 141 PHE B CB  1 
ATOM   4022  C  CG  . PHE B 1 140 ? 51.891  -8.881  61.851  1.00 51.14  ? 141 PHE B CG  1 
ATOM   4023  C  CD1 . PHE B 1 140 ? 51.509  -8.736  63.174  1.00 43.41  ? 141 PHE B CD1 1 
ATOM   4024  C  CD2 . PHE B 1 140 ? 52.869  -9.811  61.541  1.00 45.26  ? 141 PHE B CD2 1 
ATOM   4025  C  CE1 . PHE B 1 140 ? 52.086  -9.506  64.166  1.00 43.97  ? 141 PHE B CE1 1 
ATOM   4026  C  CE2 . PHE B 1 140 ? 53.450  -10.585 62.528  1.00 45.78  ? 141 PHE B CE2 1 
ATOM   4027  C  CZ  . PHE B 1 140 ? 53.058  -10.432 63.843  1.00 45.14  ? 141 PHE B CZ  1 
ATOM   4028  N  N   . ARG B 1 141 ? 49.834  -7.579  58.039  1.00 48.14  ? 142 ARG B N   1 
ATOM   4029  C  CA  . ARG B 1 141 ? 49.294  -6.716  56.992  1.00 51.68  ? 142 ARG B CA  1 
ATOM   4030  C  C   . ARG B 1 141 ? 47.805  -6.982  56.777  1.00 54.68  ? 142 ARG B C   1 
ATOM   4031  O  O   . ARG B 1 141 ? 46.981  -6.055  56.780  1.00 54.73  ? 142 ARG B O   1 
ATOM   4032  C  CB  . ARG B 1 141 ? 50.065  -6.921  55.686  1.00 63.09  ? 142 ARG B CB  1 
ATOM   4033  C  CG  . ARG B 1 141 ? 50.535  -5.634  55.025  1.00 70.00  ? 142 ARG B CG  1 
ATOM   4034  C  CD  . ARG B 1 141 ? 51.960  -5.768  54.506  1.00 78.77  ? 142 ARG B CD  1 
ATOM   4035  N  NE  . ARG B 1 141 ? 52.936  -5.800  55.592  1.00 84.93  ? 142 ARG B NE  1 
ATOM   4036  C  CZ  . ARG B 1 141 ? 54.254  -5.807  55.416  1.00 89.03  ? 142 ARG B CZ  1 
ATOM   4037  N  NH1 . ARG B 1 141 ? 54.762  -5.787  54.191  1.00 91.01  ? 142 ARG B NH1 1 
ATOM   4038  N  NH2 . ARG B 1 141 ? 55.065  -5.834  56.465  1.00 89.76  ? 142 ARG B NH2 1 
ATOM   4039  N  N   . ASP B 1 142 ? 47.469  -8.258  56.610  1.00 50.12  ? 143 ASP B N   1 
ATOM   4040  C  CA  . ASP B 1 142 ? 46.084  -8.673  56.424  1.00 53.81  ? 143 ASP B CA  1 
ATOM   4041  C  C   . ASP B 1 142 ? 45.216  -8.269  57.613  1.00 41.66  ? 143 ASP B C   1 
ATOM   4042  O  O   . ASP B 1 142 ? 44.077  -7.821  57.439  1.00 41.00  ? 143 ASP B O   1 
ATOM   4043  C  CB  . ASP B 1 142 ? 46.007  -10.186 56.203  1.00 60.91  ? 143 ASP B CB  1 
ATOM   4044  C  CG  . ASP B 1 142 ? 46.657  -10.619 54.901  1.00 62.57  ? 143 ASP B CG  1 
ATOM   4045  O  OD1 . ASP B 1 142 ? 46.651  -9.823  53.939  1.00 63.36  ? 143 ASP B OD1 1 
ATOM   4046  O  OD2 . ASP B 1 142 ? 47.177  -11.753 54.842  1.00 67.01  ? 143 ASP B OD2 1 
ATOM   4047  N  N   . LEU B 1 143 ? 45.759  -8.417  58.819  1.00 41.44  ? 144 LEU B N   1 
ATOM   4048  C  CA  . LEU B 1 143 ? 45.030  -8.028  60.023  1.00 40.42  ? 144 LEU B CA  1 
ATOM   4049  C  C   . LEU B 1 143 ? 44.710  -6.534  60.022  1.00 50.14  ? 144 LEU B C   1 
ATOM   4050  O  O   . LEU B 1 143 ? 43.584  -6.139  60.320  1.00 45.45  ? 144 LEU B O   1 
ATOM   4051  C  CB  . LEU B 1 143 ? 45.817  -8.390  61.285  1.00 40.56  ? 144 LEU B CB  1 
ATOM   4052  C  CG  . LEU B 1 143 ? 45.195  -7.884  62.591  1.00 48.37  ? 144 LEU B CG  1 
ATOM   4053  C  CD1 . LEU B 1 143 ? 43.761  -8.381  62.746  1.00 39.31  ? 144 LEU B CD1 1 
ATOM   4054  C  CD2 . LEU B 1 143 ? 46.035  -8.290  63.792  1.00 40.02  ? 144 LEU B CD2 1 
ATOM   4055  N  N   . TYR B 1 144 ? 45.694  -5.703  59.688  1.00 39.69  ? 145 TYR B N   1 
ATOM   4056  C  CA  . TYR B 1 144 ? 45.451  -4.264  59.620  1.00 44.91  ? 145 TYR B CA  1 
ATOM   4057  C  C   . TYR B 1 144 ? 44.432  -3.927  58.533  1.00 48.60  ? 145 TYR B C   1 
ATOM   4058  O  O   . TYR B 1 144 ? 43.606  -3.020  58.700  1.00 40.08  ? 145 TYR B O   1 
ATOM   4059  C  CB  . TYR B 1 144 ? 46.755  -3.501  59.385  1.00 45.77  ? 145 TYR B CB  1 
ATOM   4060  C  CG  . TYR B 1 144 ? 47.495  -3.169  60.662  1.00 46.14  ? 145 TYR B CG  1 
ATOM   4061  C  CD1 . TYR B 1 144 ? 48.359  -4.084  61.248  1.00 43.83  ? 145 TYR B CD1 1 
ATOM   4062  C  CD2 . TYR B 1 144 ? 47.317  -1.942  61.289  1.00 47.77  ? 145 TYR B CD2 1 
ATOM   4063  C  CE1 . TYR B 1 144 ? 49.033  -3.783  62.419  1.00 45.62  ? 145 TYR B CE1 1 
ATOM   4064  C  CE2 . TYR B 1 144 ? 47.986  -1.631  62.458  1.00 47.36  ? 145 TYR B CE2 1 
ATOM   4065  C  CZ  . TYR B 1 144 ? 48.842  -2.555  63.019  1.00 46.47  ? 145 TYR B CZ  1 
ATOM   4066  O  OH  . TYR B 1 144 ? 49.510  -2.251  64.184  1.00 49.07  ? 145 TYR B OH  1 
ATOM   4067  N  N   . SER B 1 145 ? 44.483  -4.667  57.427  1.00 51.83  ? 146 SER B N   1 
ATOM   4068  C  CA  . SER B 1 145 ? 43.497  -4.499  56.362  1.00 50.95  ? 146 SER B CA  1 
ATOM   4069  C  C   . SER B 1 145 ? 42.079  -4.764  56.870  1.00 49.39  ? 146 SER B C   1 
ATOM   4070  O  O   . SER B 1 145 ? 41.147  -3.988  56.612  1.00 54.37  ? 146 SER B O   1 
ATOM   4071  C  CB  . SER B 1 145 ? 43.812  -5.426  55.187  1.00 40.88  ? 146 SER B CB  1 
ATOM   4072  O  OG  . SER B 1 145 ? 45.147  -5.258  54.748  1.00 52.23  ? 146 SER B OG  1 
ATOM   4073  N  N   . GLU B 1 146 ? 41.922  -5.859  57.605  1.00 46.71  ? 147 GLU B N   1 
ATOM   4074  C  CA  . GLU B 1 146 ? 40.608  -6.239  58.105  1.00 53.12  ? 147 GLU B CA  1 
ATOM   4075  C  C   . GLU B 1 146 ? 40.151  -5.291  59.218  1.00 52.99  ? 147 GLU B C   1 
ATOM   4076  O  O   . GLU B 1 146 ? 38.953  -5.099  59.428  1.00 46.14  ? 147 GLU B O   1 
ATOM   4077  C  CB  . GLU B 1 146 ? 40.625  -7.694  58.582  1.00 56.67  ? 147 GLU B CB  1 
ATOM   4078  C  CG  . GLU B 1 146 ? 39.390  -8.486  58.174  1.00 68.32  ? 147 GLU B CG  1 
ATOM   4079  C  CD  . GLU B 1 146 ? 39.417  -8.933  56.721  1.00 77.16  ? 147 GLU B CD  1 
ATOM   4080  O  OE1 . GLU B 1 146 ? 40.403  -8.632  56.017  1.00 80.36  ? 147 GLU B OE1 1 
ATOM   4081  O  OE2 . GLU B 1 146 ? 38.438  -9.572  56.278  1.00 79.48  ? 147 GLU B OE2 1 
ATOM   4082  N  N   . LEU B 1 147 ? 41.108  -4.688  59.918  1.00 48.45  ? 148 LEU B N   1 
ATOM   4083  C  CA  . LEU B 1 147 ? 40.791  -3.634  60.877  1.00 47.22  ? 148 LEU B CA  1 
ATOM   4084  C  C   . LEU B 1 147 ? 40.229  -2.422  60.143  1.00 45.91  ? 148 LEU B C   1 
ATOM   4085  O  O   . LEU B 1 147 ? 39.249  -1.811  60.583  1.00 35.01  ? 148 LEU B O   1 
ATOM   4086  C  CB  . LEU B 1 147 ? 42.025  -3.236  61.689  1.00 49.51  ? 148 LEU B CB  1 
ATOM   4087  C  CG  . LEU B 1 147 ? 42.517  -4.226  62.744  1.00 46.38  ? 148 LEU B CG  1 
ATOM   4088  C  CD1 . LEU B 1 147 ? 43.631  -3.605  63.575  1.00 49.38  ? 148 LEU B CD1 1 
ATOM   4089  C  CD2 . LEU B 1 147 ? 41.366  -4.672  63.631  1.00 38.60  ? 148 LEU B CD2 1 
ATOM   4090  N  N   . ARG B 1 148 ? 40.858  -2.081  59.020  1.00 42.06  ? 149 ARG B N   1 
ATOM   4091  C  CA  . ARG B 1 148 ? 40.359  -1.003  58.173  1.00 45.17  ? 149 ARG B CA  1 
ATOM   4092  C  C   . ARG B 1 148 ? 38.943  -1.292  57.698  1.00 43.50  ? 149 ARG B C   1 
ATOM   4093  O  O   . ARG B 1 148 ? 38.086  -0.407  57.704  1.00 43.12  ? 149 ARG B O   1 
ATOM   4094  C  CB  . ARG B 1 148 ? 41.275  -0.786  56.970  1.00 46.10  ? 149 ARG B CB  1 
ATOM   4095  C  CG  . ARG B 1 148 ? 42.597  -0.137  57.311  1.00 37.07  ? 149 ARG B CG  1 
ATOM   4096  C  CD  . ARG B 1 148 ? 43.345  0.277   56.060  1.00 37.97  ? 149 ARG B CD  1 
ATOM   4097  N  NE  . ARG B 1 148 ? 44.722  0.649   56.366  1.00 38.46  ? 149 ARG B NE  1 
ATOM   4098  C  CZ  . ARG B 1 148 ? 45.723  -0.220  56.459  1.00 44.43  ? 149 ARG B CZ  1 
ATOM   4099  N  NH1 . ARG B 1 148 ? 45.500  -1.514  56.269  1.00 39.56  ? 149 ARG B NH1 1 
ATOM   4100  N  NH2 . ARG B 1 148 ? 46.945  0.204   56.743  1.00 46.88  ? 149 ARG B NH2 1 
ATOM   4101  N  N   . LEU B 1 149 ? 38.699  -2.532  57.285  1.00 46.95  ? 150 LEU B N   1 
ATOM   4102  C  CA  . LEU B 1 149 ? 37.361  -2.920  56.851  1.00 43.91  ? 150 LEU B CA  1 
ATOM   4103  C  C   . LEU B 1 149 ? 36.346  -2.815  57.988  1.00 41.39  ? 150 LEU B C   1 
ATOM   4104  O  O   . LEU B 1 149 ? 35.221  -2.360  57.782  1.00 40.91  ? 150 LEU B O   1 
ATOM   4105  C  CB  . LEU B 1 149 ? 37.369  -4.338  56.282  1.00 43.79  ? 150 LEU B CB  1 
ATOM   4106  C  CG  . LEU B 1 149 ? 37.959  -4.458  54.876  1.00 45.10  ? 150 LEU B CG  1 
ATOM   4107  C  CD1 . LEU B 1 149 ? 38.539  -5.844  54.646  1.00 39.78  ? 150 LEU B CD1 1 
ATOM   4108  C  CD2 . LEU B 1 149 ? 36.903  -4.130  53.831  1.00 38.73  ? 150 LEU B CD2 1 
ATOM   4109  N  N   . TYR B 1 150 ? 36.749  -3.231  59.185  1.00 39.57  ? 151 TYR B N   1 
ATOM   4110  C  CA  . TYR B 1 150 ? 35.885  -3.138  60.358  1.00 34.81  ? 151 TYR B CA  1 
ATOM   4111  C  C   . TYR B 1 150 ? 35.525  -1.686  60.664  1.00 47.39  ? 151 TYR B C   1 
ATOM   4112  O  O   . TYR B 1 150 ? 34.364  -1.373  60.933  1.00 48.49  ? 151 TYR B O   1 
ATOM   4113  C  CB  . TYR B 1 150 ? 36.553  -3.785  61.575  1.00 38.70  ? 151 TYR B CB  1 
ATOM   4114  C  CG  . TYR B 1 150 ? 35.699  -3.780  62.826  1.00 42.90  ? 151 TYR B CG  1 
ATOM   4115  C  CD1 . TYR B 1 150 ? 34.393  -4.255  62.805  1.00 50.52  ? 151 TYR B CD1 1 
ATOM   4116  C  CD2 . TYR B 1 150 ? 36.203  -3.305  64.031  1.00 42.34  ? 151 TYR B CD2 1 
ATOM   4117  C  CE1 . TYR B 1 150 ? 33.612  -4.253  63.949  1.00 54.26  ? 151 TYR B CE1 1 
ATOM   4118  C  CE2 . TYR B 1 150 ? 35.430  -3.301  65.179  1.00 48.51  ? 151 TYR B CE2 1 
ATOM   4119  C  CZ  . TYR B 1 150 ? 34.136  -3.775  65.132  1.00 58.74  ? 151 TYR B CZ  1 
ATOM   4120  O  OH  . TYR B 1 150 ? 33.365  -3.770  66.273  1.00 64.98  ? 151 TYR B OH  1 
ATOM   4121  N  N   . TYR B 1 151 ? 36.518  -0.800  60.619  1.00 47.03  ? 152 TYR B N   1 
ATOM   4122  C  CA  . TYR B 1 151 ? 36.264  0.622   60.831  1.00 43.65  ? 152 TYR B CA  1 
ATOM   4123  C  C   . TYR B 1 151 ? 35.355  1.186   59.747  1.00 44.30  ? 152 TYR B C   1 
ATOM   4124  O  O   . TYR B 1 151 ? 34.500  2.029   60.016  1.00 49.80  ? 152 TYR B O   1 
ATOM   4125  C  CB  . TYR B 1 151 ? 37.571  1.419   60.870  1.00 39.13  ? 152 TYR B CB  1 
ATOM   4126  C  CG  . TYR B 1 151 ? 37.363  2.912   60.714  1.00 34.86  ? 152 TYR B CG  1 
ATOM   4127  C  CD1 . TYR B 1 151 ? 36.924  3.688   61.780  1.00 36.48  ? 152 TYR B CD1 1 
ATOM   4128  C  CD2 . TYR B 1 151 ? 37.601  3.545   59.498  1.00 35.11  ? 152 TYR B CD2 1 
ATOM   4129  C  CE1 . TYR B 1 151 ? 36.728  5.049   61.641  1.00 31.73  ? 152 TYR B CE1 1 
ATOM   4130  C  CE2 . TYR B 1 151 ? 37.407  4.907   59.350  1.00 32.69  ? 152 TYR B CE2 1 
ATOM   4131  C  CZ  . TYR B 1 151 ? 36.971  5.653   60.425  1.00 32.35  ? 152 TYR B CZ  1 
ATOM   4132  O  OH  . TYR B 1 151 ? 36.776  7.008   60.283  1.00 31.78  ? 152 TYR B OH  1 
ATOM   4133  N  N   . ARG B 1 152 ? 35.543  0.710   58.520  1.00 50.61  ? 153 ARG B N   1 
ATOM   4134  C  CA  . ARG B 1 152 ? 34.790  1.204   57.373  1.00 56.30  ? 153 ARG B CA  1 
ATOM   4135  C  C   . ARG B 1 152 ? 33.300  0.883   57.450  1.00 67.16  ? 153 ARG B C   1 
ATOM   4136  O  O   . ARG B 1 152 ? 32.508  1.426   56.680  1.00 71.97  ? 153 ARG B O   1 
ATOM   4137  C  CB  . ARG B 1 152 ? 35.368  0.634   56.074  1.00 63.44  ? 153 ARG B CB  1 
ATOM   4138  C  CG  . ARG B 1 152 ? 35.999  1.672   55.157  1.00 68.91  ? 153 ARG B CG  1 
ATOM   4139  C  CD  . ARG B 1 152 ? 34.937  2.490   54.431  1.00 76.25  ? 153 ARG B CD  1 
ATOM   4140  N  NE  . ARG B 1 152 ? 35.524  3.473   53.524  1.00 81.94  ? 153 ARG B NE  1 
ATOM   4141  C  CZ  . ARG B 1 152 ? 34.923  3.942   52.435  1.00 86.50  ? 153 ARG B CZ  1 
ATOM   4142  N  NH1 . ARG B 1 152 ? 35.537  4.835   51.670  1.00 88.79  ? 153 ARG B NH1 1 
ATOM   4143  N  NH2 . ARG B 1 152 ? 33.707  3.522   52.110  1.00 87.46  ? 153 ARG B NH2 1 
ATOM   4144  N  N   . GLY B 1 153 ? 32.908  0.016   58.378  1.00 73.03  ? 154 GLY B N   1 
ATOM   4145  C  CA  . GLY B 1 153 ? 31.506  -0.338  58.488  1.00 79.87  ? 154 GLY B CA  1 
ATOM   4146  C  C   . GLY B 1 153 ? 31.120  -1.539  57.648  1.00 87.25  ? 154 GLY B C   1 
ATOM   4147  O  O   . GLY B 1 153 ? 29.962  -1.688  57.259  1.00 86.64  ? 154 GLY B O   1 
ATOM   4148  N  N   . ALA B 1 154 ? 32.088  -2.408  57.379  1.00 95.86  ? 155 ALA B N   1 
ATOM   4149  C  CA  . ALA B 1 154 ? 31.881  -3.535  56.478  1.00 104.56 ? 155 ALA B CA  1 
ATOM   4150  C  C   . ALA B 1 154 ? 31.197  -4.676  57.220  1.00 118.57 ? 155 ALA B C   1 
ATOM   4151  O  O   . ALA B 1 154 ? 30.996  -5.760  56.670  1.00 121.75 ? 155 ALA B O   1 
ATOM   4152  C  CB  . ALA B 1 154 ? 33.199  -3.996  55.881  1.00 100.82 ? 155 ALA B CB  1 
ATOM   4153  N  N   . ASN B 1 155 ? 30.871  -4.418  58.484  1.00 130.47 ? 156 ASN B N   1 
ATOM   4154  C  CA  . ASN B 1 155 ? 30.056  -5.312  59.299  1.00 131.91 ? 156 ASN B CA  1 
ATOM   4155  C  C   . ASN B 1 155 ? 30.717  -6.658  59.536  1.00 131.26 ? 156 ASN B C   1 
ATOM   4156  O  O   . ASN B 1 155 ? 30.079  -7.707  59.434  1.00 135.82 ? 156 ASN B O   1 
ATOM   4157  C  CB  . ASN B 1 155 ? 28.679  -5.512  58.661  1.00 134.05 ? 156 ASN B CB  1 
ATOM   4158  N  N   . LEU B 1 156 ? 32.005  -6.618  59.851  1.00 108.54 ? 157 LEU B N   1 
ATOM   4159  C  CA  . LEU B 1 156 ? 32.697  -7.794  60.346  1.00 93.12  ? 157 LEU B CA  1 
ATOM   4160  C  C   . LEU B 1 156 ? 32.276  -8.054  61.783  1.00 84.19  ? 157 LEU B C   1 
ATOM   4161  O  O   . LEU B 1 156 ? 31.492  -7.303  62.365  1.00 81.18  ? 157 LEU B O   1 
ATOM   4162  C  CB  . LEU B 1 156 ? 34.217  -7.615  60.290  1.00 81.92  ? 157 LEU B CB  1 
ATOM   4163  C  CG  . LEU B 1 156 ? 35.053  -7.606  59.009  1.00 70.94  ? 157 LEU B CG  1 
ATOM   4164  C  CD1 . LEU B 1 156 ? 34.540  -6.643  57.952  1.00 65.80  ? 157 LEU B CD1 1 
ATOM   4165  C  CD2 . LEU B 1 156 ? 36.471  -7.249  59.394  1.00 63.56  ? 157 LEU B CD2 1 
ATOM   4166  N  N   . HIS B 1 157 ? 32.814  -9.124  62.351  1.00 85.30  ? 158 HIS B N   1 
ATOM   4167  C  CA  . HIS B 1 157 ? 32.797  -9.322  63.789  1.00 81.44  ? 158 HIS B CA  1 
ATOM   4168  C  C   . HIS B 1 157 ? 34.249  -9.435  64.222  1.00 78.97  ? 158 HIS B C   1 
ATOM   4169  O  O   . HIS B 1 157 ? 34.929  -10.396 63.861  1.00 74.94  ? 158 HIS B O   1 
ATOM   4170  C  CB  . HIS B 1 157 ? 32.000  -10.567 64.176  1.00 81.33  ? 158 HIS B CB  1 
ATOM   4171  N  N   . LEU B 1 158 ? 34.724  -8.437  64.964  1.00 76.52  ? 159 LEU B N   1 
ATOM   4172  C  CA  . LEU B 1 158 ? 36.128  -8.357  65.360  1.00 74.28  ? 159 LEU B CA  1 
ATOM   4173  C  C   . LEU B 1 158 ? 36.582  -9.659  66.010  1.00 77.36  ? 159 LEU B C   1 
ATOM   4174  O  O   . LEU B 1 158 ? 37.684  -10.153 65.749  1.00 81.50  ? 159 LEU B O   1 
ATOM   4175  C  CB  . LEU B 1 158 ? 36.343  -7.180  66.312  1.00 70.80  ? 159 LEU B CB  1 
ATOM   4176  C  CG  . LEU B 1 158 ? 37.731  -6.546  66.274  1.00 67.61  ? 159 LEU B CG  1 
ATOM   4177  C  CD1 . LEU B 1 158 ? 38.104  -6.185  64.846  1.00 65.27  ? 159 LEU B CD1 1 
ATOM   4178  C  CD2 . LEU B 1 158 ? 37.778  -5.321  67.165  1.00 66.30  ? 159 LEU B CD2 1 
ATOM   4179  N  N   . GLU B 1 159 ? 35.697  -10.193 66.848  1.00 79.58  ? 160 GLU B N   1 
ATOM   4180  C  CA  . GLU B 1 159 ? 35.814  -11.510 67.467  1.00 74.00  ? 160 GLU B CA  1 
ATOM   4181  C  C   . GLU B 1 159 ? 36.539  -12.533 66.587  1.00 66.12  ? 160 GLU B C   1 
ATOM   4182  O  O   . GLU B 1 159 ? 37.653  -12.976 66.898  1.00 65.80  ? 160 GLU B O   1 
ATOM   4183  C  CB  . GLU B 1 159 ? 34.409  -12.026 67.799  1.00 84.11  ? 160 GLU B CB  1 
ATOM   4184  C  CG  . GLU B 1 159 ? 33.357  -10.921 67.893  1.00 90.99  ? 160 GLU B CG  1 
ATOM   4185  C  CD  . GLU B 1 159 ? 31.934  -11.455 67.869  1.00 97.24  ? 160 GLU B CD  1 
ATOM   4186  O  OE1 . GLU B 1 159 ? 31.568  -12.123 66.879  1.00 99.70  ? 160 GLU B OE1 1 
ATOM   4187  O  OE2 . GLU B 1 159 ? 31.178  -11.201 68.830  1.00 99.87  ? 160 GLU B OE2 1 
ATOM   4188  N  N   . GLU B 1 160 ? 35.897  -12.884 65.477  1.00 61.24  ? 161 GLU B N   1 
ATOM   4189  C  CA  . GLU B 1 160 ? 36.358  -13.958 64.604  1.00 69.32  ? 161 GLU B CA  1 
ATOM   4190  C  C   . GLU B 1 160 ? 37.671  -13.640 63.889  1.00 68.67  ? 161 GLU B C   1 
ATOM   4191  O  O   . GLU B 1 160 ? 38.578  -14.476 63.851  1.00 68.21  ? 161 GLU B O   1 
ATOM   4192  C  CB  . GLU B 1 160 ? 35.271  -14.284 63.580  1.00 76.86  ? 161 GLU B CB  1 
ATOM   4193  C  CG  . GLU B 1 160 ? 35.637  -15.377 62.597  1.00 84.49  ? 161 GLU B CG  1 
ATOM   4194  C  CD  . GLU B 1 160 ? 34.659  -15.459 61.444  1.00 90.78  ? 161 GLU B CD  1 
ATOM   4195  O  OE1 . GLU B 1 160 ? 33.882  -14.498 61.256  1.00 91.77  ? 161 GLU B OE1 1 
ATOM   4196  O  OE2 . GLU B 1 160 ? 34.661  -16.485 60.733  1.00 93.62  ? 161 GLU B OE2 1 
ATOM   4197  N  N   . THR B 1 161 ? 37.757  -12.442 63.317  1.00 60.45  ? 162 THR B N   1 
ATOM   4198  C  CA  . THR B 1 161 ? 38.969  -11.982 62.641  1.00 58.73  ? 162 THR B CA  1 
ATOM   4199  C  C   . THR B 1 161 ? 40.180  -12.125 63.563  1.00 55.79  ? 162 THR B C   1 
ATOM   4200  O  O   . THR B 1 161 ? 41.190  -12.764 63.211  1.00 57.54  ? 162 THR B O   1 
ATOM   4201  C  CB  . THR B 1 161 ? 38.828  -10.511 62.184  1.00 57.82  ? 162 THR B CB  1 
ATOM   4202  O  OG1 . THR B 1 161 ? 38.089  -10.458 60.957  1.00 55.37  ? 162 THR B OG1 1 
ATOM   4203  C  CG2 . THR B 1 161 ? 40.193  -9.881  61.958  1.00 57.75  ? 162 THR B CG2 1 
ATOM   4204  N  N   . LEU B 1 162 ? 40.053  -11.551 64.757  1.00 53.45  ? 163 LEU B N   1 
ATOM   4205  C  CA  . LEU B 1 162 ? 41.107  -11.632 65.759  1.00 52.47  ? 163 LEU B CA  1 
ATOM   4206  C  C   . LEU B 1 162 ? 41.433  -13.080 66.105  1.00 52.91  ? 163 LEU B C   1 
ATOM   4207  O  O   . LEU B 1 162 ? 42.601  -13.477 66.097  1.00 55.97  ? 163 LEU B O   1 
ATOM   4208  C  CB  . LEU B 1 162 ? 40.704  -10.869 67.019  1.00 53.72  ? 163 LEU B CB  1 
ATOM   4209  C  CG  . LEU B 1 162 ? 40.494  -9.365  66.845  1.00 52.28  ? 163 LEU B CG  1 
ATOM   4210  C  CD1 . LEU B 1 162 ? 39.860  -8.790  68.090  1.00 51.96  ? 163 LEU B CD1 1 
ATOM   4211  C  CD2 . LEU B 1 162 ? 41.805  -8.664  66.531  1.00 53.82  ? 163 LEU B CD2 1 
ATOM   4212  N  N   . ALA B 1 163 ? 40.396  -13.864 66.397  1.00 56.09  ? 164 ALA B N   1 
ATOM   4213  C  CA  . ALA B 1 163 ? 40.571  -15.271 66.753  1.00 54.90  ? 164 ALA B CA  1 
ATOM   4214  C  C   . ALA B 1 163 ? 41.415  -16.024 65.723  1.00 56.96  ? 164 ALA B C   1 
ATOM   4215  O  O   . ALA B 1 163 ? 42.405  -16.678 66.071  1.00 61.49  ? 164 ALA B O   1 
ATOM   4216  C  CB  . ALA B 1 163 ? 39.216  -15.943 66.917  1.00 56.13  ? 164 ALA B CB  1 
ATOM   4217  N  N   . GLU B 1 164 ? 41.029  -15.913 64.454  1.00 54.95  ? 165 GLU B N   1 
ATOM   4218  C  CA  . GLU B 1 164 ? 41.733  -16.596 63.372  1.00 59.81  ? 165 GLU B CA  1 
ATOM   4219  C  C   . GLU B 1 164 ? 43.174  -16.107 63.240  1.00 65.00  ? 165 GLU B C   1 
ATOM   4220  O  O   . GLU B 1 164 ? 44.116  -16.920 63.120  1.00 67.16  ? 165 GLU B O   1 
ATOM   4221  C  CB  . GLU B 1 164 ? 40.986  -16.406 62.051  1.00 63.88  ? 165 GLU B CB  1 
ATOM   4222  C  CG  . GLU B 1 164 ? 39.578  -16.980 62.054  1.00 75.74  ? 165 GLU B CG  1 
ATOM   4223  C  CD  . GLU B 1 164 ? 39.535  -18.419 62.535  1.00 83.88  ? 165 GLU B CD  1 
ATOM   4224  O  OE1 . GLU B 1 164 ? 40.378  -19.224 62.085  1.00 87.99  ? 165 GLU B OE1 1 
ATOM   4225  O  OE2 . GLU B 1 164 ? 38.660  -18.745 63.365  1.00 86.20  ? 165 GLU B OE2 1 
ATOM   4226  N  N   . PHE B 1 165 ? 43.339  -14.782 63.264  1.00 63.96  ? 166 PHE B N   1 
ATOM   4227  C  CA  . PHE B 1 165 ? 44.673  -14.188 63.224  1.00 62.70  ? 166 PHE B CA  1 
ATOM   4228  C  C   . PHE B 1 165 ? 45.584  -14.825 64.270  1.00 44.07  ? 166 PHE B C   1 
ATOM   4229  O  O   . PHE B 1 165 ? 46.666  -15.334 63.947  1.00 49.96  ? 166 PHE B O   1 
ATOM   4230  C  CB  . PHE B 1 165 ? 44.612  -12.674 63.447  1.00 56.33  ? 166 PHE B CB  1 
ATOM   4231  C  CG  . PHE B 1 165 ? 45.937  -12.068 63.815  1.00 42.27  ? 166 PHE B CG  1 
ATOM   4232  C  CD1 . PHE B 1 165 ? 46.899  -11.836 62.846  1.00 42.71  ? 166 PHE B CD1 1 
ATOM   4233  C  CD2 . PHE B 1 165 ? 46.228  -11.745 65.132  1.00 42.00  ? 166 PHE B CD2 1 
ATOM   4234  C  CE1 . PHE B 1 165 ? 48.124  -11.290 63.181  1.00 42.87  ? 166 PHE B CE1 1 
ATOM   4235  C  CE2 . PHE B 1 165 ? 47.451  -11.200 65.473  1.00 42.16  ? 166 PHE B CE2 1 
ATOM   4236  C  CZ  . PHE B 1 165 ? 48.400  -10.970 64.496  1.00 48.26  ? 166 PHE B CZ  1 
ATOM   4237  N  N   . TRP B 1 166 ? 45.127  -14.804 65.521  1.00 43.76  ? 167 TRP B N   1 
ATOM   4238  C  CA  . TRP B 1 166 ? 45.892  -15.367 66.627  1.00 44.41  ? 167 TRP B CA  1 
ATOM   4239  C  C   . TRP B 1 166 ? 46.155  -16.851 66.430  1.00 52.74  ? 167 TRP B C   1 
ATOM   4240  O  O   . TRP B 1 166 ? 47.220  -17.348 66.791  1.00 57.64  ? 167 TRP B O   1 
ATOM   4241  C  CB  . TRP B 1 166 ? 45.171  -15.147 67.957  1.00 44.01  ? 167 TRP B CB  1 
ATOM   4242  C  CG  . TRP B 1 166 ? 45.154  -13.724 68.405  1.00 51.91  ? 167 TRP B CG  1 
ATOM   4243  C  CD1 . TRP B 1 166 ? 44.056  -12.971 68.695  1.00 49.94  ? 167 TRP B CD1 1 
ATOM   4244  C  CD2 . TRP B 1 166 ? 46.290  -12.874 68.610  1.00 55.17  ? 167 TRP B CD2 1 
ATOM   4245  N  NE1 . TRP B 1 166 ? 44.435  -11.707 69.072  1.00 52.50  ? 167 TRP B NE1 1 
ATOM   4246  C  CE2 . TRP B 1 166 ? 45.802  -11.621 69.028  1.00 51.71  ? 167 TRP B CE2 1 
ATOM   4247  C  CE3 . TRP B 1 166 ? 47.671  -13.052 68.483  1.00 57.75  ? 167 TRP B CE3 1 
ATOM   4248  C  CZ2 . TRP B 1 166 ? 46.644  -10.552 69.318  1.00 55.67  ? 167 TRP B CZ2 1 
ATOM   4249  C  CZ3 . TRP B 1 166 ? 48.503  -11.990 68.769  1.00 54.62  ? 167 TRP B CZ3 1 
ATOM   4250  C  CH2 . TRP B 1 166 ? 47.988  -10.755 69.182  1.00 56.74  ? 167 TRP B CH2 1 
ATOM   4251  N  N   . ALA B 1 167 ? 45.183  -17.554 65.859  1.00 58.85  ? 168 ALA B N   1 
ATOM   4252  C  CA  . ALA B 1 167 ? 45.337  -18.983 65.610  1.00 62.19  ? 168 ALA B CA  1 
ATOM   4253  C  C   . ALA B 1 167 ? 46.511  -19.264 64.670  1.00 66.76  ? 168 ALA B C   1 
ATOM   4254  O  O   . ALA B 1 167 ? 47.473  -19.964 65.039  1.00 70.23  ? 168 ALA B O   1 
ATOM   4255  C  CB  . ALA B 1 167 ? 44.048  -19.562 65.041  1.00 59.72  ? 168 ALA B CB  1 
ATOM   4256  N  N   . ARG B 1 168 ? 46.450  -18.709 63.461  1.00 72.44  ? 169 ARG B N   1 
ATOM   4257  C  CA  . ARG B 1 168 ? 47.484  -19.029 62.476  1.00 80.72  ? 169 ARG B CA  1 
ATOM   4258  C  C   . ARG B 1 168 ? 48.842  -18.452 62.886  1.00 77.11  ? 169 ARG B C   1 
ATOM   4259  O  O   . ARG B 1 168 ? 49.904  -19.054 62.628  1.00 81.33  ? 169 ARG B O   1 
ATOM   4260  C  CB  . ARG B 1 168 ? 47.081  -18.531 61.089  1.00 90.27  ? 169 ARG B CB  1 
ATOM   4261  C  CG  . ARG B 1 168 ? 48.009  -19.001 59.982  1.00 100.81 ? 169 ARG B CG  1 
ATOM   4262  C  CD  . ARG B 1 168 ? 47.299  -19.022 58.640  1.00 107.24 ? 169 ARG B CD  1 
ATOM   4263  N  NE  . ARG B 1 168 ? 47.866  -18.064 57.698  1.00 113.03 ? 169 ARG B NE  1 
ATOM   4264  C  CZ  . ARG B 1 168 ? 47.396  -17.857 56.473  1.00 117.06 ? 169 ARG B CZ  1 
ATOM   4265  N  NH1 . ARG B 1 168 ? 46.348  -18.544 56.036  1.00 117.88 ? 169 ARG B NH1 1 
ATOM   4266  N  NH2 . ARG B 1 168 ? 47.974  -16.964 55.683  1.00 117.97 ? 169 ARG B NH2 1 
ATOM   4267  N  N   . LEU B 1 169 ? 48.804  -17.295 63.545  1.00 67.73  ? 170 LEU B N   1 
ATOM   4268  C  CA  . LEU B 1 169 ? 50.016  -16.722 64.117  1.00 65.41  ? 170 LEU B CA  1 
ATOM   4269  C  C   . LEU B 1 169 ? 50.654  -17.711 65.083  1.00 59.22  ? 170 LEU B C   1 
ATOM   4270  O  O   . LEU B 1 169 ? 51.861  -17.946 65.036  1.00 60.64  ? 170 LEU B O   1 
ATOM   4271  C  CB  . LEU B 1 169 ? 49.724  -15.408 64.840  1.00 59.36  ? 170 LEU B CB  1 
ATOM   4272  C  CG  . LEU B 1 169 ? 50.968  -14.729 65.420  1.00 54.00  ? 170 LEU B CG  1 
ATOM   4273  C  CD1 . LEU B 1 169 ? 51.789  -14.086 64.314  1.00 46.40  ? 170 LEU B CD1 1 
ATOM   4274  C  CD2 . LEU B 1 169 ? 50.601  -13.712 66.488  1.00 54.98  ? 170 LEU B CD2 1 
ATOM   4275  N  N   . LEU B 1 170 ? 49.831  -18.290 65.952  1.00 60.02  ? 171 LEU B N   1 
ATOM   4276  C  CA  . LEU B 1 170 ? 50.292  -19.306 66.889  1.00 61.22  ? 171 LEU B CA  1 
ATOM   4277  C  C   . LEU B 1 170 ? 50.917  -20.475 66.142  1.00 60.35  ? 171 LEU B C   1 
ATOM   4278  O  O   . LEU B 1 170 ? 51.968  -20.983 66.545  1.00 53.88  ? 171 LEU B O   1 
ATOM   4279  C  CB  . LEU B 1 170 ? 49.144  -19.799 67.772  1.00 62.30  ? 171 LEU B CB  1 
ATOM   4280  C  CG  . LEU B 1 170 ? 49.513  -20.907 68.763  1.00 65.92  ? 171 LEU B CG  1 
ATOM   4281  C  CD1 . LEU B 1 170 ? 50.485  -20.388 69.812  1.00 67.97  ? 171 LEU B CD1 1 
ATOM   4282  C  CD2 . LEU B 1 170 ? 48.272  -21.495 69.418  1.00 67.04  ? 171 LEU B CD2 1 
ATOM   4283  N  N   . GLU B 1 171 ? 50.272  -20.893 65.052  1.00 65.42  ? 172 GLU B N   1 
ATOM   4284  C  CA  . GLU B 1 171 ? 50.841  -21.935 64.196  1.00 71.90  ? 172 GLU B CA  1 
ATOM   4285  C  C   . GLU B 1 171 ? 52.274  -21.609 63.783  1.00 72.53  ? 172 GLU B C   1 
ATOM   4286  O  O   . GLU B 1 171 ? 53.231  -22.268 64.224  1.00 72.42  ? 172 GLU B O   1 
ATOM   4287  C  CB  . GLU B 1 171 ? 50.000  -22.131 62.934  1.00 79.61  ? 172 GLU B CB  1 
ATOM   4288  C  CG  . GLU B 1 171 ? 48.581  -22.599 63.164  1.00 87.82  ? 172 GLU B CG  1 
ATOM   4289  C  CD  . GLU B 1 171 ? 48.100  -23.515 62.055  1.00 95.40  ? 172 GLU B CD  1 
ATOM   4290  O  OE1 . GLU B 1 171 ? 48.853  -23.711 61.078  1.00 99.30  ? 172 GLU B OE1 1 
ATOM   4291  O  OE2 . GLU B 1 171 ? 46.964  -24.024 62.152  1.00 98.04  ? 172 GLU B OE2 1 
ATOM   4292  N  N   . ARG B 1 172 ? 52.411  -20.584 62.941  1.00 71.99  ? 173 ARG B N   1 
ATOM   4293  C  CA  . ARG B 1 172 ? 53.717  -20.250 62.366  1.00 71.97  ? 173 ARG B CA  1 
ATOM   4294  C  C   . ARG B 1 172 ? 54.778  -19.973 63.430  1.00 69.06  ? 173 ARG B C   1 
ATOM   4295  O  O   . ARG B 1 172 ? 55.899  -20.486 63.351  1.00 67.57  ? 173 ARG B O   1 
ATOM   4296  C  CB  . ARG B 1 172 ? 53.600  -19.047 61.428  1.00 76.87  ? 173 ARG B CB  1 
ATOM   4297  C  CG  . ARG B 1 172 ? 52.942  -19.363 60.094  1.00 83.47  ? 173 ARG B CG  1 
ATOM   4298  C  CD  . ARG B 1 172 ? 53.920  -19.187 58.941  1.00 89.76  ? 173 ARG B CD  1 
ATOM   4299  N  NE  . ARG B 1 172 ? 53.339  -19.586 57.662  1.00 93.99  ? 173 ARG B NE  1 
ATOM   4300  C  CZ  . ARG B 1 172 ? 53.149  -18.761 56.638  1.00 96.66  ? 173 ARG B CZ  1 
ATOM   4301  N  NH1 . ARG B 1 172 ? 53.494  -17.485 56.739  1.00 94.59  ? 173 ARG B NH1 1 
ATOM   4302  N  NH2 . ARG B 1 172 ? 52.612  -19.211 55.511  1.00 98.72  ? 173 ARG B NH2 1 
ATOM   4303  N  N   . LEU B 1 173 ? 54.417  -19.171 64.427  1.00 60.65  ? 174 LEU B N   1 
ATOM   4304  C  CA  . LEU B 1 173 ? 55.339  -18.837 65.508  1.00 59.67  ? 174 LEU B CA  1 
ATOM   4305  C  C   . LEU B 1 173 ? 55.793  -20.075 66.280  1.00 59.98  ? 174 LEU B C   1 
ATOM   4306  O  O   . LEU B 1 173 ? 56.959  -20.169 66.688  1.00 58.26  ? 174 LEU B O   1 
ATOM   4307  C  CB  . LEU B 1 173 ? 54.700  -17.831 66.466  1.00 57.21  ? 174 LEU B CB  1 
ATOM   4308  C  CG  . LEU B 1 173 ? 55.089  -16.361 66.286  1.00 58.02  ? 174 LEU B CG  1 
ATOM   4309  C  CD1 . LEU B 1 173 ? 54.898  -15.918 64.848  1.00 53.76  ? 174 LEU B CD1 1 
ATOM   4310  C  CD2 . LEU B 1 173 ? 54.302  -15.466 67.233  1.00 54.96  ? 174 LEU B CD2 1 
ATOM   4311  N  N   . PHE B 1 174 ? 54.883  -21.028 66.480  1.00 63.76  ? 175 PHE B N   1 
ATOM   4312  C  CA  . PHE B 1 174 ? 55.264  -22.242 67.189  1.00 69.63  ? 175 PHE B CA  1 
ATOM   4313  C  C   . PHE B 1 174 ? 56.181  -23.090 66.333  1.00 55.80  ? 175 PHE B C   1 
ATOM   4314  O  O   . PHE B 1 174 ? 57.117  -23.699 66.852  1.00 56.89  ? 175 PHE B O   1 
ATOM   4315  C  CB  . PHE B 1 174 ? 54.054  -23.070 67.612  1.00 54.56  ? 175 PHE B CB  1 
ATOM   4316  C  CG  . PHE B 1 174 ? 54.364  -24.063 68.697  1.00 62.98  ? 175 PHE B CG  1 
ATOM   4317  C  CD1 . PHE B 1 174 ? 54.396  -23.665 70.023  1.00 60.57  ? 175 PHE B CD1 1 
ATOM   4318  C  CD2 . PHE B 1 174 ? 54.646  -25.387 68.394  1.00 57.14  ? 175 PHE B CD2 1 
ATOM   4319  C  CE1 . PHE B 1 174 ? 54.689  -24.568 71.029  1.00 59.19  ? 175 PHE B CE1 1 
ATOM   4320  C  CE2 . PHE B 1 174 ? 54.939  -26.296 69.398  1.00 58.28  ? 175 PHE B CE2 1 
ATOM   4321  C  CZ  . PHE B 1 174 ? 54.960  -25.884 70.716  1.00 58.03  ? 175 PHE B CZ  1 
ATOM   4322  N  N   . LYS B 1 175 ? 55.919  -23.142 65.029  1.00 55.83  ? 176 LYS B N   1 
ATOM   4323  C  CA  . LYS B 1 175 ? 56.859  -23.831 64.156  1.00 57.18  ? 176 LYS B CA  1 
ATOM   4324  C  C   . LYS B 1 175 ? 58.243  -23.205 64.289  1.00 68.66  ? 176 LYS B C   1 
ATOM   4325  O  O   . LYS B 1 175 ? 59.213  -23.906 64.563  1.00 58.70  ? 176 LYS B O   1 
ATOM   4326  C  CB  . LYS B 1 175 ? 56.414  -23.803 62.693  1.00 57.21  ? 176 LYS B CB  1 
ATOM   4327  C  CG  . LYS B 1 175 ? 54.989  -24.271 62.460  1.00 71.32  ? 176 LYS B CG  1 
ATOM   4328  C  CD  . LYS B 1 175 ? 54.817  -24.857 61.062  1.00 73.59  ? 176 LYS B CD  1 
ATOM   4329  C  CE  . LYS B 1 175 ? 55.707  -24.164 60.036  1.00 74.82  ? 176 LYS B CE  1 
ATOM   4330  N  NZ  . LYS B 1 175 ? 55.474  -24.657 58.648  1.00 75.71  ? 176 LYS B NZ  1 
ATOM   4331  N  N   . GLN B 1 176 ? 58.335  -21.887 64.114  1.00 66.18  ? 177 GLN B N   1 
ATOM   4332  C  CA  . GLN B 1 176 ? 59.647  -21.232 64.073  1.00 64.40  ? 177 GLN B CA  1 
ATOM   4333  C  C   . GLN B 1 176 ? 60.397  -21.243 65.390  1.00 57.21  ? 177 GLN B C   1 
ATOM   4334  O  O   . GLN B 1 176 ? 61.631  -21.273 65.403  1.00 58.20  ? 177 GLN B O   1 
ATOM   4335  C  CB  . GLN B 1 176 ? 59.528  -19.790 63.581  1.00 64.80  ? 177 GLN B CB  1 
ATOM   4336  C  CG  . GLN B 1 176 ? 59.191  -19.657 62.103  1.00 69.61  ? 177 GLN B CG  1 
ATOM   4337  C  CD  . GLN B 1 176 ? 59.242  -18.218 61.635  1.00 74.54  ? 177 GLN B CD  1 
ATOM   4338  O  OE1 . GLN B 1 176 ? 58.748  -17.322 62.315  1.00 73.14  ? 177 GLN B OE1 1 
ATOM   4339  N  NE2 . GLN B 1 176 ? 59.874  -17.984 60.488  1.00 76.45  ? 177 GLN B NE2 1 
ATOM   4340  N  N   . LEU B 1 177 ? 59.667  -21.251 66.498  1.00 56.55  ? 178 LEU B N   1 
ATOM   4341  C  CA  . LEU B 1 177 ? 60.321  -21.280 67.802  1.00 57.01  ? 178 LEU B CA  1 
ATOM   4342  C  C   . LEU B 1 177 ? 60.809  -22.685 68.168  1.00 76.03  ? 178 LEU B C   1 
ATOM   4343  O  O   . LEU B 1 177 ? 61.441  -22.872 69.207  1.00 59.18  ? 178 LEU B O   1 
ATOM   4344  C  CB  . LEU B 1 177 ? 59.385  -20.757 68.896  1.00 55.93  ? 178 LEU B CB  1 
ATOM   4345  C  CG  . LEU B 1 177 ? 59.385  -19.243 69.145  1.00 70.84  ? 178 LEU B CG  1 
ATOM   4346  C  CD1 . LEU B 1 177 ? 58.101  -18.786 69.846  1.00 53.59  ? 178 LEU B CD1 1 
ATOM   4347  C  CD2 . LEU B 1 177 ? 60.630  -18.803 69.908  1.00 70.50  ? 178 LEU B CD2 1 
ATOM   4348  N  N   . HIS B 1 178 ? 60.504  -23.668 67.322  1.00 71.83  ? 179 HIS B N   1 
ATOM   4349  C  CA  . HIS B 1 178 ? 61.009  -25.030 67.499  1.00 75.76  ? 179 HIS B CA  1 
ATOM   4350  C  C   . HIS B 1 178 ? 61.606  -25.549 66.194  1.00 80.76  ? 179 HIS B C   1 
ATOM   4351  O  O   . HIS B 1 178 ? 60.950  -26.297 65.466  1.00 75.90  ? 179 HIS B O   1 
ATOM   4352  C  CB  . HIS B 1 178 ? 59.897  -25.968 67.978  1.00 73.50  ? 179 HIS B CB  1 
ATOM   4353  C  CG  . HIS B 1 178 ? 59.515  -25.771 69.411  1.00 73.48  ? 179 HIS B CG  1 
ATOM   4354  N  ND1 . HIS B 1 178 ? 60.415  -25.357 70.369  1.00 73.13  ? 179 HIS B ND1 1 
ATOM   4355  C  CD2 . HIS B 1 178 ? 58.329  -25.921 70.047  1.00 70.83  ? 179 HIS B CD2 1 
ATOM   4356  C  CE1 . HIS B 1 178 ? 59.802  -25.265 71.535  1.00 71.68  ? 179 HIS B CE1 1 
ATOM   4357  N  NE2 . HIS B 1 178 ? 58.535  -25.601 71.367  1.00 70.87  ? 179 HIS B NE2 1 
ATOM   4358  N  N   . PRO B 1 179 ? 62.856  -25.151 65.896  1.00 91.79  ? 180 PRO B N   1 
ATOM   4359  C  CA  . PRO B 1 179 ? 63.471  -25.445 64.595  1.00 96.49  ? 180 PRO B CA  1 
ATOM   4360  C  C   . PRO B 1 179 ? 63.588  -26.932 64.286  1.00 102.24 ? 180 PRO B C   1 
ATOM   4361  O  O   . PRO B 1 179 ? 63.189  -27.332 63.191  1.00 104.81 ? 180 PRO B O   1 
ATOM   4362  C  CB  . PRO B 1 179 ? 64.863  -24.812 64.708  1.00 98.39  ? 180 PRO B CB  1 
ATOM   4363  C  CG  . PRO B 1 179 ? 64.765  -23.843 65.835  1.00 96.28  ? 180 PRO B CG  1 
ATOM   4364  C  CD  . PRO B 1 179 ? 63.769  -24.418 66.786  1.00 93.33  ? 180 PRO B CD  1 
ATOM   4365  N  N   . GLN B 1 180 ? 64.084  -27.750 65.210  1.00 101.32 ? 181 GLN B N   1 
ATOM   4366  C  CA  . GLN B 1 180 ? 63.968  -29.171 64.952  1.00 100.70 ? 181 GLN B CA  1 
ATOM   4367  C  C   . GLN B 1 180 ? 62.843  -29.720 65.801  1.00 99.65  ? 181 GLN B C   1 
ATOM   4368  O  O   . GLN B 1 180 ? 62.983  -29.952 67.001  1.00 99.99  ? 181 GLN B O   1 
ATOM   4369  C  CB  . GLN B 1 180 ? 65.282  -29.893 65.254  1.00 101.96 ? 181 GLN B CB  1 
ATOM   4370  N  N   . LEU B 1 181 ? 61.730  -29.939 65.119  1.00 96.71  ? 182 LEU B N   1 
ATOM   4371  C  CA  . LEU B 1 181 ? 60.573  -30.675 65.580  1.00 94.42  ? 182 LEU B CA  1 
ATOM   4372  C  C   . LEU B 1 181 ? 59.862  -30.960 64.271  1.00 96.27  ? 182 LEU B C   1 
ATOM   4373  O  O   . LEU B 1 181 ? 60.120  -30.268 63.286  1.00 97.77  ? 182 LEU B O   1 
ATOM   4374  C  CB  . LEU B 1 181 ? 59.718  -29.858 66.552  1.00 86.59  ? 182 LEU B CB  1 
ATOM   4375  C  CG  . LEU B 1 181 ? 59.339  -30.452 67.914  1.00 82.80  ? 182 LEU B CG  1 
ATOM   4376  C  CD1 . LEU B 1 181 ? 60.560  -30.832 68.739  1.00 80.25  ? 182 LEU B CD1 1 
ATOM   4377  C  CD2 . LEU B 1 181 ? 58.460  -29.477 68.685  1.00 79.62  ? 182 LEU B CD2 1 
ATOM   4378  N  N   . LEU B 1 182 ? 58.973  -31.940 64.219  1.00 95.84  ? 183 LEU B N   1 
ATOM   4379  C  CA  . LEU B 1 182 ? 58.166  -32.068 63.014  1.00 92.25  ? 183 LEU B CA  1 
ATOM   4380  C  C   . LEU B 1 182 ? 56.691  -32.135 63.375  1.00 87.32  ? 183 LEU B C   1 
ATOM   4381  O  O   . LEU B 1 182 ? 56.226  -33.105 63.971  1.00 84.34  ? 183 LEU B O   1 
ATOM   4382  C  CB  . LEU B 1 182 ? 58.594  -33.290 62.196  1.00 92.79  ? 183 LEU B CB  1 
ATOM   4383  C  CG  . LEU B 1 182 ? 59.952  -33.172 61.489  1.00 92.35  ? 183 LEU B CG  1 
ATOM   4384  C  CD1 . LEU B 1 182 ? 61.113  -33.538 62.408  1.00 93.51  ? 183 LEU B CD1 1 
ATOM   4385  C  CD2 . LEU B 1 182 ? 59.987  -34.011 60.219  1.00 95.15  ? 183 LEU B CD2 1 
ATOM   4386  N  N   . LEU B 1 183 ? 55.961  -31.091 63.000  1.00 87.23  ? 184 LEU B N   1 
ATOM   4387  C  CA  . LEU B 1 183 ? 54.546  -30.993 63.326  1.00 86.83  ? 184 LEU B CA  1 
ATOM   4388  C  C   . LEU B 1 183 ? 53.696  -30.988 62.063  1.00 87.05  ? 184 LEU B C   1 
ATOM   4389  O  O   . LEU B 1 183 ? 53.688  -30.006 61.322  1.00 85.79  ? 184 LEU B O   1 
ATOM   4390  C  CB  . LEU B 1 183 ? 54.265  -29.733 64.155  1.00 86.45  ? 184 LEU B CB  1 
ATOM   4391  C  CG  . LEU B 1 183 ? 54.958  -29.551 65.512  1.00 86.67  ? 184 LEU B CG  1 
ATOM   4392  C  CD1 . LEU B 1 183 ? 56.392  -29.060 65.363  1.00 87.60  ? 184 LEU B CD1 1 
ATOM   4393  C  CD2 . LEU B 1 183 ? 54.163  -28.600 66.394  1.00 87.03  ? 184 LEU B CD2 1 
ATOM   4394  N  N   . PRO B 1 184 ? 52.968  -32.086 61.818  1.00 93.77  ? 185 PRO B N   1 
ATOM   4395  C  CA  . PRO B 1 184 ? 52.038  -32.135 60.686  1.00 96.83  ? 185 PRO B CA  1 
ATOM   4396  C  C   . PRO B 1 184 ? 50.803  -31.272 60.934  1.00 99.51  ? 185 PRO B C   1 
ATOM   4397  O  O   . PRO B 1 184 ? 50.778  -30.495 61.890  1.00 98.82  ? 185 PRO B O   1 
ATOM   4398  C  CB  . PRO B 1 184 ? 51.669  -33.619 60.597  1.00 95.41  ? 185 PRO B CB  1 
ATOM   4399  C  CG  . PRO B 1 184 ? 51.893  -34.146 61.973  1.00 95.16  ? 185 PRO B CG  1 
ATOM   4400  C  CD  . PRO B 1 184 ? 53.059  -33.378 62.520  1.00 91.78  ? 185 PRO B CD  1 
ATOM   4401  N  N   . ASP B 1 185 ? 49.793  -31.406 60.081  1.00 103.53 ? 186 ASP B N   1 
ATOM   4402  C  CA  . ASP B 1 185 ? 48.567  -30.630 60.225  1.00 103.34 ? 186 ASP B CA  1 
ATOM   4403  C  C   . ASP B 1 185 ? 47.811  -31.025 61.490  1.00 102.95 ? 186 ASP B C   1 
ATOM   4404  O  O   . ASP B 1 185 ? 47.170  -30.188 62.131  1.00 100.93 ? 186 ASP B O   1 
ATOM   4405  C  CB  . ASP B 1 185 ? 47.671  -30.810 58.998  1.00 105.28 ? 186 ASP B CB  1 
ATOM   4406  N  N   . ASP B 1 186 ? 47.896  -32.304 61.845  1.00 99.84  ? 187 ASP B N   1 
ATOM   4407  C  CA  . ASP B 1 186 ? 47.208  -32.831 63.019  1.00 96.17  ? 187 ASP B CA  1 
ATOM   4408  C  C   . ASP B 1 186 ? 47.749  -32.227 64.312  1.00 85.55  ? 187 ASP B C   1 
ATOM   4409  O  O   . ASP B 1 186 ? 46.983  -31.737 65.147  1.00 82.23  ? 187 ASP B O   1 
ATOM   4410  C  CB  . ASP B 1 186 ? 47.328  -34.356 63.066  1.00 99.86  ? 187 ASP B CB  1 
ATOM   4411  N  N   . TYR B 1 187 ? 49.069  -32.265 64.472  1.00 80.27  ? 188 TYR B N   1 
ATOM   4412  C  CA  . TYR B 1 187 ? 49.708  -31.738 65.673  1.00 81.73  ? 188 TYR B CA  1 
ATOM   4413  C  C   . TYR B 1 187 ? 49.456  -30.240 65.812  1.00 83.66  ? 188 TYR B C   1 
ATOM   4414  O  O   . TYR B 1 187 ? 49.221  -29.744 66.913  1.00 82.58  ? 188 TYR B O   1 
ATOM   4415  C  CB  . TYR B 1 187 ? 51.213  -32.021 65.657  1.00 79.79  ? 188 TYR B CB  1 
ATOM   4416  C  CG  . TYR B 1 187 ? 51.840  -32.076 67.036  1.00 78.86  ? 188 TYR B CG  1 
ATOM   4417  C  CD1 . TYR B 1 187 ? 51.933  -30.938 67.826  1.00 76.73  ? 188 TYR B CD1 1 
ATOM   4418  C  CD2 . TYR B 1 187 ? 52.341  -33.267 67.545  1.00 80.54  ? 188 TYR B CD2 1 
ATOM   4419  C  CE1 . TYR B 1 187 ? 52.502  -30.983 69.083  1.00 75.94  ? 188 TYR B CE1 1 
ATOM   4420  C  CE2 . TYR B 1 187 ? 52.914  -33.321 68.803  1.00 80.98  ? 188 TYR B CE2 1 
ATOM   4421  C  CZ  . TYR B 1 187 ? 52.990  -32.175 69.567  1.00 76.79  ? 188 TYR B CZ  1 
ATOM   4422  O  OH  . TYR B 1 187 ? 53.558  -32.220 70.820  1.00 79.47  ? 188 TYR B OH  1 
ATOM   4423  N  N   . LEU B 1 188 ? 49.505  -29.524 64.693  1.00 81.55  ? 189 LEU B N   1 
ATOM   4424  C  CA  . LEU B 1 188 ? 49.272  -28.085 64.702  1.00 80.30  ? 189 LEU B CA  1 
ATOM   4425  C  C   . LEU B 1 188 ? 47.821  -27.754 65.030  1.00 80.79  ? 189 LEU B C   1 
ATOM   4426  O  O   . LEU B 1 188 ? 47.548  -26.780 65.724  1.00 79.16  ? 189 LEU B O   1 
ATOM   4427  C  CB  . LEU B 1 188 ? 49.660  -27.465 63.359  1.00 78.57  ? 189 LEU B CB  1 
ATOM   4428  C  CG  . LEU B 1 188 ? 51.147  -27.154 63.183  1.00 78.36  ? 189 LEU B CG  1 
ATOM   4429  C  CD1 . LEU B 1 188 ? 51.408  -26.510 61.832  1.00 76.98  ? 189 LEU B CD1 1 
ATOM   4430  C  CD2 . LEU B 1 188 ? 51.639  -26.259 64.311  1.00 77.45  ? 189 LEU B CD2 1 
ATOM   4431  N  N   . ASP B 1 189 ? 46.893  -28.562 64.526  1.00 78.27  ? 190 ASP B N   1 
ATOM   4432  C  CA  . ASP B 1 189 ? 45.476  -28.374 64.832  1.00 76.41  ? 190 ASP B CA  1 
ATOM   4433  C  C   . ASP B 1 189 ? 45.221  -28.593 66.327  1.00 72.01  ? 190 ASP B C   1 
ATOM   4434  O  O   . ASP B 1 189 ? 44.565  -27.777 67.005  1.00 70.28  ? 190 ASP B O   1 
ATOM   4435  C  CB  . ASP B 1 189 ? 44.620  -29.326 63.991  1.00 78.35  ? 190 ASP B CB  1 
ATOM   4436  N  N   . CYS B 1 190 ? 45.763  -29.697 66.835  1.00 69.87  ? 191 CYS B N   1 
ATOM   4437  C  CA  . CYS B 1 190 ? 45.657  -30.021 68.252  1.00 69.45  ? 191 CYS B CA  1 
ATOM   4438  C  C   . CYS B 1 190 ? 46.213  -28.881 69.096  1.00 65.07  ? 191 CYS B C   1 
ATOM   4439  O  O   . CYS B 1 190 ? 45.580  -28.443 70.052  1.00 65.02  ? 191 CYS B O   1 
ATOM   4440  C  CB  . CYS B 1 190 ? 46.393  -31.327 68.564  1.00 70.73  ? 191 CYS B CB  1 
ATOM   4441  S  SG  . CYS B 1 190 ? 46.397  -31.777 70.316  1.00 77.75  ? 191 CYS B SG  1 
ATOM   4442  N  N   . LEU B 1 191 ? 47.393  -28.401 68.715  1.00 64.28  ? 192 LEU B N   1 
ATOM   4443  C  CA  . LEU B 1 191 ? 48.038  -27.267 69.370  1.00 61.94  ? 192 LEU B CA  1 
ATOM   4444  C  C   . LEU B 1 191 ? 47.171  -26.015 69.355  1.00 60.05  ? 192 LEU B C   1 
ATOM   4445  O  O   . LEU B 1 191 ? 47.077  -25.305 70.358  1.00 60.43  ? 192 LEU B O   1 
ATOM   4446  C  CB  . LEU B 1 191 ? 49.380  -26.968 68.699  1.00 57.27  ? 192 LEU B CB  1 
ATOM   4447  C  CG  . LEU B 1 191 ? 49.970  -25.564 68.867  1.00 65.63  ? 192 LEU B CG  1 
ATOM   4448  C  CD1 . LEU B 1 191 ? 50.397  -25.309 70.302  1.00 64.14  ? 192 LEU B CD1 1 
ATOM   4449  C  CD2 . LEU B 1 191 ? 51.136  -25.363 67.915  1.00 66.30  ? 192 LEU B CD2 1 
ATOM   4450  N  N   . GLY B 1 192 ? 46.537  -25.749 68.218  1.00 54.66  ? 193 GLY B N   1 
ATOM   4451  C  CA  . GLY B 1 192 ? 45.710  -24.572 68.078  1.00 53.15  ? 193 GLY B CA  1 
ATOM   4452  C  C   . GLY B 1 192 ? 44.556  -24.766 69.022  1.00 74.45  ? 193 GLY B C   1 
ATOM   4453  O  O   . GLY B 1 192 ? 43.903  -23.810 69.446  1.00 76.90  ? 193 GLY B O   1 
ATOM   4454  N  N   . LYS B 1 193 ? 44.291  -26.023 69.356  1.00 76.46  ? 194 LYS B N   1 
ATOM   4455  C  CA  . LYS B 1 193 ? 43.104  -26.273 70.137  1.00 76.95  ? 194 LYS B CA  1 
ATOM   4456  C  C   . LYS B 1 193 ? 43.496  -26.295 71.599  1.00 78.01  ? 194 LYS B C   1 
ATOM   4457  O  O   . LYS B 1 193 ? 42.654  -26.230 72.493  1.00 77.53  ? 194 LYS B O   1 
ATOM   4458  C  CB  . LYS B 1 193 ? 42.431  -27.560 69.715  1.00 83.16  ? 194 LYS B CB  1 
ATOM   4459  C  CG  . LYS B 1 193 ? 41.004  -27.562 70.112  1.00 86.98  ? 194 LYS B CG  1 
ATOM   4460  C  CD  . LYS B 1 193 ? 40.182  -27.672 68.878  1.00 90.88  ? 194 LYS B CD  1 
ATOM   4461  C  CE  . LYS B 1 193 ? 40.553  -28.836 68.061  1.00 95.64  ? 194 LYS B CE  1 
ATOM   4462  N  NZ  . LYS B 1 193 ? 40.422  -28.533 66.577  1.00 96.71  ? 194 LYS B NZ  1 
ATOM   4463  N  N   . GLN B 1 194 ? 44.803  -26.299 71.819  1.00 76.61  ? 195 GLN B N   1 
ATOM   4464  C  CA  . GLN B 1 194 ? 45.363  -26.163 73.146  1.00 73.39  ? 195 GLN B CA  1 
ATOM   4465  C  C   . GLN B 1 194 ? 45.477  -24.681 73.485  1.00 70.67  ? 195 GLN B C   1 
ATOM   4466  O  O   . GLN B 1 194 ? 45.792  -24.327 74.610  1.00 64.85  ? 195 GLN B O   1 
ATOM   4467  C  CB  . GLN B 1 194 ? 46.724  -26.857 73.222  1.00 74.48  ? 195 GLN B CB  1 
ATOM   4468  C  CG  . GLN B 1 194 ? 46.661  -28.350 72.928  1.00 79.17  ? 195 GLN B CG  1 
ATOM   4469  C  CD  . GLN B 1 194 ? 46.479  -29.173 74.178  1.00 82.00  ? 195 GLN B CD  1 
ATOM   4470  O  OE1 . GLN B 1 194 ? 46.564  -28.649 75.287  1.00 83.71  ? 195 GLN B OE1 1 
ATOM   4471  N  NE2 . GLN B 1 194 ? 46.247  -30.471 74.014  1.00 86.03  ? 195 GLN B NE2 1 
ATOM   4472  N  N   . ALA B 1 195 ? 45.196  -23.818 72.510  1.00 68.95  ? 196 ALA B N   1 
ATOM   4473  C  CA  . ALA B 1 195 ? 45.335  -22.373 72.708  1.00 77.33  ? 196 ALA B CA  1 
ATOM   4474  C  C   . ALA B 1 195 ? 44.511  -21.892 73.899  1.00 82.96  ? 196 ALA B C   1 
ATOM   4475  O  O   . ALA B 1 195 ? 44.998  -21.125 74.729  1.00 80.24  ? 196 ALA B O   1 
ATOM   4476  C  CB  . ALA B 1 195 ? 44.936  -21.613 71.449  1.00 71.75  ? 196 ALA B CB  1 
ATOM   4477  N  N   . GLU B 1 196 ? 43.268  -22.355 73.980  1.00 94.09  ? 197 GLU B N   1 
ATOM   4478  C  CA  . GLU B 1 196 ? 42.425  -22.100 75.143  1.00 97.10  ? 197 GLU B CA  1 
ATOM   4479  C  C   . GLU B 1 196 ? 42.995  -22.846 76.350  1.00 95.45  ? 197 GLU B C   1 
ATOM   4480  O  O   . GLU B 1 196 ? 43.661  -23.867 76.182  1.00 100.86 ? 197 GLU B O   1 
ATOM   4481  C  CB  . GLU B 1 196 ? 40.984  -22.539 74.869  1.00 106.19 ? 197 GLU B CB  1 
ATOM   4482  C  CG  . GLU B 1 196 ? 40.406  -22.025 73.555  1.00 112.72 ? 197 GLU B CG  1 
ATOM   4483  C  CD  . GLU B 1 196 ? 39.551  -20.782 73.727  1.00 117.81 ? 197 GLU B CD  1 
ATOM   4484  O  OE1 . GLU B 1 196 ? 39.481  -20.258 74.858  1.00 119.78 ? 197 GLU B OE1 1 
ATOM   4485  O  OE2 . GLU B 1 196 ? 38.945  -20.332 72.731  1.00 117.60 ? 197 GLU B OE2 1 
ATOM   4486  N  N   . ALA B 1 197 ? 42.758  -22.318 77.553  1.00 86.44  ? 198 ALA B N   1 
ATOM   4487  C  CA  . ALA B 1 197 ? 43.194  -22.937 78.816  1.00 84.98  ? 198 ALA B CA  1 
ATOM   4488  C  C   . ALA B 1 197 ? 44.719  -22.936 78.990  1.00 81.11  ? 198 ALA B C   1 
ATOM   4489  O  O   . ALA B 1 197 ? 45.239  -23.345 80.028  1.00 86.39  ? 198 ALA B O   1 
ATOM   4490  C  CB  . ALA B 1 197 ? 42.648  -24.363 78.937  1.00 86.02  ? 198 ALA B CB  1 
ATOM   4491  N  N   . LEU B 1 198 ? 45.420  -22.474 77.963  1.00 78.14  ? 199 LEU B N   1 
ATOM   4492  C  CA  . LEU B 1 198 ? 46.874  -22.344 77.960  1.00 72.22  ? 199 LEU B CA  1 
ATOM   4493  C  C   . LEU B 1 198 ? 47.246  -20.875 78.126  1.00 64.91  ? 199 LEU B C   1 
ATOM   4494  O  O   . LEU B 1 198 ? 47.987  -20.523 79.046  1.00 63.56  ? 199 LEU B O   1 
ATOM   4495  C  CB  . LEU B 1 198 ? 47.497  -22.944 76.699  1.00 72.61  ? 199 LEU B CB  1 
ATOM   4496  C  CG  . LEU B 1 198 ? 47.849  -24.431 76.865  1.00 75.80  ? 199 LEU B CG  1 
ATOM   4497  C  CD1 . LEU B 1 198 ? 48.672  -24.961 75.698  1.00 77.61  ? 199 LEU B CD1 1 
ATOM   4498  C  CD2 . LEU B 1 198 ? 48.565  -24.685 78.183  1.00 77.88  ? 199 LEU B CD2 1 
ATOM   4499  N  N   . ARG B 1 199 ? 46.752  -20.041 77.209  1.00 65.25  ? 200 ARG B N   1 
ATOM   4500  C  CA  . ARG B 1 199 ? 47.148  -18.635 77.075  1.00 61.35  ? 200 ARG B CA  1 
ATOM   4501  C  C   . ARG B 1 199 ? 48.612  -18.456 76.690  1.00 63.68  ? 200 ARG B C   1 
ATOM   4502  O  O   . ARG B 1 199 ? 49.403  -17.919 77.466  1.00 62.87  ? 200 ARG B O   1 
ATOM   4503  C  CB  . ARG B 1 199 ? 46.884  -17.872 78.380  1.00 66.55  ? 200 ARG B CB  1 
ATOM   4504  C  CG  . ARG B 1 199 ? 45.489  -17.303 78.549  1.00 73.63  ? 200 ARG B CG  1 
ATOM   4505  C  CD  . ARG B 1 199 ? 45.431  -16.465 79.820  1.00 77.74  ? 200 ARG B CD  1 
ATOM   4506  N  NE  . ARG B 1 199 ? 44.428  -15.408 79.757  1.00 78.42  ? 200 ARG B NE  1 
ATOM   4507  C  CZ  . ARG B 1 199 ? 43.926  -14.790 80.821  1.00 80.93  ? 200 ARG B CZ  1 
ATOM   4508  N  NH1 . ARG B 1 199 ? 44.335  -15.121 82.040  1.00 80.33  ? 200 ARG B NH1 1 
ATOM   4509  N  NH2 . ARG B 1 199 ? 43.016  -13.837 80.668  1.00 77.57  ? 200 ARG B NH2 1 
ATOM   4510  N  N   . PRO B 1 200 ? 48.972  -18.904 75.475  1.00 61.32  ? 201 PRO B N   1 
ATOM   4511  C  CA  . PRO B 1 200 ? 50.341  -18.758 74.974  1.00 62.60  ? 201 PRO B CA  1 
ATOM   4512  C  C   . PRO B 1 200 ? 50.733  -17.293 74.798  1.00 49.38  ? 201 PRO B C   1 
ATOM   4513  O  O   . PRO B 1 200 ? 51.889  -16.942 75.025  1.00 56.41  ? 201 PRO B O   1 
ATOM   4514  C  CB  . PRO B 1 200 ? 50.298  -19.479 73.624  1.00 50.57  ? 201 PRO B CB  1 
ATOM   4515  C  CG  . PRO B 1 200 ? 48.879  -19.373 73.190  1.00 49.78  ? 201 PRO B CG  1 
ATOM   4516  C  CD  . PRO B 1 200 ? 48.063  -19.442 74.446  1.00 49.98  ? 201 PRO B CD  1 
ATOM   4517  N  N   . PHE B 1 201 ? 49.776  -16.457 74.402  1.00 50.15  ? 202 PHE B N   1 
ATOM   4518  C  CA  . PHE B 1 201 ? 50.024  -15.032 74.197  1.00 51.05  ? 202 PHE B CA  1 
ATOM   4519  C  C   . PHE B 1 201 ? 49.705  -14.210 75.441  1.00 51.88  ? 202 PHE B C   1 
ATOM   4520  O  O   . PHE B 1 201 ? 49.798  -12.984 75.422  1.00 57.19  ? 202 PHE B O   1 
ATOM   4521  C  CB  . PHE B 1 201 ? 49.204  -14.503 73.018  1.00 49.54  ? 202 PHE B CB  1 
ATOM   4522  C  CG  . PHE B 1 201 ? 49.590  -15.094 71.694  1.00 50.68  ? 202 PHE B CG  1 
ATOM   4523  C  CD1 . PHE B 1 201 ? 50.810  -14.790 71.113  1.00 51.94  ? 202 PHE B CD1 1 
ATOM   4524  C  CD2 . PHE B 1 201 ? 48.725  -15.942 71.022  1.00 49.83  ? 202 PHE B CD2 1 
ATOM   4525  C  CE1 . PHE B 1 201 ? 51.165  -15.328 69.891  1.00 46.84  ? 202 PHE B CE1 1 
ATOM   4526  C  CE2 . PHE B 1 201 ? 49.074  -16.482 69.799  1.00 50.87  ? 202 PHE B CE2 1 
ATOM   4527  C  CZ  . PHE B 1 201 ? 50.296  -16.175 69.233  1.00 56.91  ? 202 PHE B CZ  1 
ATOM   4528  N  N   . GLY B 1 202 ? 49.326  -14.889 76.517  1.00 47.71  ? 203 GLY B N   1 
ATOM   4529  C  CA  . GLY B 1 202 ? 48.924  -14.216 77.738  1.00 47.69  ? 203 GLY B CA  1 
ATOM   4530  C  C   . GLY B 1 202 ? 47.598  -13.491 77.592  1.00 62.54  ? 203 GLY B C   1 
ATOM   4531  O  O   . GLY B 1 202 ? 46.615  -14.071 77.133  1.00 63.93  ? 203 GLY B O   1 
ATOM   4532  N  N   . GLU B 1 203 ? 47.570  -12.218 77.976  1.00 65.38  ? 204 GLU B N   1 
ATOM   4533  C  CA  . GLU B 1 203 ? 46.323  -11.460 77.997  1.00 66.99  ? 204 GLU B CA  1 
ATOM   4534  C  C   . GLU B 1 203 ? 46.222  -10.451 76.858  1.00 63.87  ? 204 GLU B C   1 
ATOM   4535  O  O   . GLU B 1 203 ? 45.269  -9.677  76.793  1.00 68.58  ? 204 GLU B O   1 
ATOM   4536  C  CB  . GLU B 1 203 ? 46.169  -10.738 79.337  1.00 70.51  ? 204 GLU B CB  1 
ATOM   4537  C  CG  . GLU B 1 203 ? 45.980  -11.670 80.522  1.00 81.91  ? 204 GLU B CG  1 
ATOM   4538  C  CD  . GLU B 1 203 ? 45.829  -10.924 81.832  1.00 90.17  ? 204 GLU B CD  1 
ATOM   4539  O  OE1 . GLU B 1 203 ? 44.884  -10.115 81.950  1.00 92.12  ? 204 GLU B OE1 1 
ATOM   4540  O  OE2 . GLU B 1 203 ? 46.652  -11.147 82.744  1.00 94.70  ? 204 GLU B OE2 1 
ATOM   4541  N  N   . ALA B 1 204 ? 47.203  -10.462 75.963  1.00 67.06  ? 205 ALA B N   1 
ATOM   4542  C  CA  . ALA B 1 204 ? 47.215  -9.533  74.835  1.00 65.85  ? 205 ALA B CA  1 
ATOM   4543  C  C   . ALA B 1 204 ? 46.005  -9.683  73.893  1.00 63.87  ? 205 ALA B C   1 
ATOM   4544  O  O   . ALA B 1 204 ? 45.376  -8.677  73.551  1.00 65.37  ? 205 ALA B O   1 
ATOM   4545  C  CB  . ALA B 1 204 ? 48.521  -9.676  74.050  1.00 68.92  ? 205 ALA B CB  1 
ATOM   4546  N  N   . PRO B 1 205 ? 45.665  -10.922 73.472  1.00 60.49  ? 206 PRO B N   1 
ATOM   4547  C  CA  . PRO B 1 205 ? 44.537  -11.034 72.536  1.00 59.18  ? 206 PRO B CA  1 
ATOM   4548  C  C   . PRO B 1 205 ? 43.196  -10.559 73.101  1.00 60.94  ? 206 PRO B C   1 
ATOM   4549  O  O   . PRO B 1 205 ? 42.450  -9.887  72.392  1.00 60.49  ? 206 PRO B O   1 
ATOM   4550  C  CB  . PRO B 1 205 ? 44.481  -12.537 72.234  1.00 58.97  ? 206 PRO B CB  1 
ATOM   4551  C  CG  . PRO B 1 205 ? 45.849  -13.031 72.516  1.00 59.89  ? 206 PRO B CG  1 
ATOM   4552  C  CD  . PRO B 1 205 ? 46.302  -12.235 73.695  1.00 63.08  ? 206 PRO B CD  1 
ATOM   4553  N  N   . ARG B 1 206 ? 42.898  -10.906 74.350  1.00 58.07  ? 207 ARG B N   1 
ATOM   4554  C  CA  . ARG B 1 206 ? 41.629  -10.529 74.969  1.00 60.73  ? 207 ARG B CA  1 
ATOM   4555  C  C   . ARG B 1 206 ? 41.511  -9.012  75.130  1.00 58.58  ? 207 ARG B C   1 
ATOM   4556  O  O   . ARG B 1 206 ? 40.514  -8.400  74.713  1.00 59.84  ? 207 ARG B O   1 
ATOM   4557  C  CB  . ARG B 1 206 ? 41.479  -11.223 76.324  1.00 64.82  ? 207 ARG B CB  1 
ATOM   4558  C  CG  . ARG B 1 206 ? 40.320  -10.722 77.164  1.00 70.25  ? 207 ARG B CG  1 
ATOM   4559  C  CD  . ARG B 1 206 ? 40.137  -11.581 78.405  1.00 73.41  ? 207 ARG B CD  1 
ATOM   4560  N  NE  . ARG B 1 206 ? 39.163  -11.009 79.329  1.00 76.25  ? 207 ARG B NE  1 
ATOM   4561  C  CZ  . ARG B 1 206 ? 39.481  -10.238 80.364  1.00 77.90  ? 207 ARG B CZ  1 
ATOM   4562  N  NH1 . ARG B 1 206 ? 40.751  -9.949  80.613  1.00 77.88  ? 207 ARG B NH1 1 
ATOM   4563  N  NH2 . ARG B 1 206 ? 38.529  -9.760  81.153  1.00 77.93  ? 207 ARG B NH2 1 
ATOM   4564  N  N   . GLU B 1 207 ? 42.537  -8.420  75.739  1.00 58.20  ? 208 GLU B N   1 
ATOM   4565  C  CA  . GLU B 1 207 ? 42.641  -6.972  75.880  1.00 57.64  ? 208 GLU B CA  1 
ATOM   4566  C  C   . GLU B 1 207 ? 42.447  -6.274  74.542  1.00 57.29  ? 208 GLU B C   1 
ATOM   4567  O  O   . GLU B 1 207 ? 41.616  -5.363  74.412  1.00 55.79  ? 208 GLU B O   1 
ATOM   4568  C  CB  . GLU B 1 207 ? 44.000  -6.585  76.466  1.00 64.42  ? 208 GLU B CB  1 
ATOM   4569  C  CG  . GLU B 1 207 ? 44.041  -6.488  77.979  1.00 75.02  ? 208 GLU B CG  1 
ATOM   4570  C  CD  . GLU B 1 207 ? 45.019  -5.431  78.457  1.00 84.28  ? 208 GLU B CD  1 
ATOM   4571  O  OE1 . GLU B 1 207 ? 45.816  -4.941  77.627  1.00 86.02  ? 208 GLU B OE1 1 
ATOM   4572  O  OE2 . GLU B 1 207 ? 44.993  -5.088  79.657  1.00 88.73  ? 208 GLU B OE2 1 
ATOM   4573  N  N   . LEU B 1 208 ? 43.219  -6.714  73.550  1.00 54.44  ? 209 LEU B N   1 
ATOM   4574  C  CA  . LEU B 1 208 ? 43.138  -6.150  72.211  1.00 51.71  ? 209 LEU B CA  1 
ATOM   4575  C  C   . LEU B 1 208 ? 41.720  -6.242  71.667  1.00 49.41  ? 209 LEU B C   1 
ATOM   4576  O  O   . LEU B 1 208 ? 41.214  -5.288  71.086  1.00 50.72  ? 209 LEU B O   1 
ATOM   4577  C  CB  . LEU B 1 208 ? 44.106  -6.856  71.261  1.00 46.76  ? 209 LEU B CB  1 
ATOM   4578  C  CG  . LEU B 1 208 ? 44.086  -6.312  69.831  1.00 38.42  ? 209 LEU B CG  1 
ATOM   4579  C  CD1 . LEU B 1 208 ? 44.529  -4.855  69.815  1.00 40.59  ? 209 LEU B CD1 1 
ATOM   4580  C  CD2 . LEU B 1 208 ? 44.951  -7.153  68.905  1.00 39.83  ? 209 LEU B CD2 1 
ATOM   4581  N  N   . ARG B 1 209 ? 41.081  -7.388  71.871  1.00 52.72  ? 210 ARG B N   1 
ATOM   4582  C  CA  . ARG B 1 209 ? 39.715  -7.596  71.407  1.00 47.89  ? 210 ARG B CA  1 
ATOM   4583  C  C   . ARG B 1 209 ? 38.763  -6.571  72.012  1.00 50.04  ? 210 ARG B C   1 
ATOM   4584  O  O   . ARG B 1 209 ? 38.139  -5.791  71.287  1.00 55.13  ? 210 ARG B O   1 
ATOM   4585  C  CB  . ARG B 1 209 ? 39.245  -9.014  71.739  1.00 51.46  ? 210 ARG B CB  1 
ATOM   4586  N  N   . LEU B 1 210 ? 38.672  -6.571  73.340  1.00 47.19  ? 211 LEU B N   1 
ATOM   4587  C  CA  . LEU B 1 210 ? 37.789  -5.648  74.054  1.00 53.20  ? 211 LEU B CA  1 
ATOM   4588  C  C   . LEU B 1 210 ? 38.014  -4.195  73.626  1.00 55.68  ? 211 LEU B C   1 
ATOM   4589  O  O   . LEU B 1 210 ? 37.095  -3.506  73.132  1.00 59.11  ? 211 LEU B O   1 
ATOM   4590  C  CB  . LEU B 1 210 ? 38.008  -5.780  75.565  1.00 57.85  ? 211 LEU B CB  1 
ATOM   4591  C  CG  . LEU B 1 210 ? 37.303  -6.910  76.324  1.00 64.88  ? 211 LEU B CG  1 
ATOM   4592  C  CD1 . LEU B 1 210 ? 37.084  -6.527  77.783  1.00 69.97  ? 211 LEU B CD1 1 
ATOM   4593  C  CD2 . LEU B 1 210 ? 35.985  -7.292  75.664  1.00 61.76  ? 211 LEU B CD2 1 
ATOM   4594  N  N   . ARG B 1 211 ? 39.254  -3.746  73.802  1.00 48.74  ? 212 ARG B N   1 
ATOM   4595  C  CA  . ARG B 1 211 ? 39.594  -2.347  73.583  1.00 46.92  ? 212 ARG B CA  1 
ATOM   4596  C  C   . ARG B 1 211 ? 39.404  -1.913  72.134  1.00 39.48  ? 212 ARG B C   1 
ATOM   4597  O  O   . ARG B 1 211 ? 38.923  -0.809  71.877  1.00 39.13  ? 212 ARG B O   1 
ATOM   4598  C  CB  . ARG B 1 211 ? 41.031  -2.082  74.032  1.00 48.85  ? 212 ARG B CB  1 
ATOM   4599  C  CG  . ARG B 1 211 ? 41.240  -2.330  75.514  1.00 53.89  ? 212 ARG B CG  1 
ATOM   4600  C  CD  . ARG B 1 211 ? 42.561  -1.768  75.998  1.00 61.66  ? 212 ARG B CD  1 
ATOM   4601  N  NE  . ARG B 1 211 ? 42.684  -1.870  77.448  1.00 69.37  ? 212 ARG B NE  1 
ATOM   4602  C  CZ  . ARG B 1 211 ? 43.521  -1.143  78.180  1.00 79.04  ? 212 ARG B CZ  1 
ATOM   4603  N  NH1 . ARG B 1 211 ? 44.312  -0.252  77.597  1.00 79.48  ? 212 ARG B NH1 1 
ATOM   4604  N  NH2 . ARG B 1 211 ? 43.565  -1.304  79.496  1.00 82.31  ? 212 ARG B NH2 1 
ATOM   4605  N  N   . ALA B 1 212 ? 39.769  -2.774  71.190  1.00 37.93  ? 213 ALA B N   1 
ATOM   4606  C  CA  . ALA B 1 212 ? 39.583  -2.446  69.781  1.00 39.05  ? 213 ALA B CA  1 
ATOM   4607  C  C   . ALA B 1 212 ? 38.103  -2.406  69.425  1.00 43.84  ? 213 ALA B C   1 
ATOM   4608  O  O   . ALA B 1 212 ? 37.685  -1.558  68.644  1.00 47.32  ? 213 ALA B O   1 
ATOM   4609  C  CB  . ALA B 1 212 ? 40.314  -3.430  68.889  1.00 39.38  ? 213 ALA B CB  1 
ATOM   4610  N  N   . THR B 1 213 ? 37.307  -3.315  69.986  1.00 44.29  ? 214 THR B N   1 
ATOM   4611  C  CA  . THR B 1 213 ? 35.865  -3.254  69.758  1.00 46.06  ? 214 THR B CA  1 
ATOM   4612  C  C   . THR B 1 213 ? 35.320  -1.908  70.222  1.00 41.52  ? 214 THR B C   1 
ATOM   4613  O  O   . THR B 1 213 ? 34.718  -1.170  69.430  1.00 44.28  ? 214 THR B O   1 
ATOM   4614  C  CB  . THR B 1 213 ? 35.096  -4.389  70.473  1.00 47.75  ? 214 THR B CB  1 
ATOM   4615  O  OG1 . THR B 1 213 ? 35.452  -4.424  71.860  1.00 51.34  ? 214 THR B OG1 1 
ATOM   4616  C  CG2 . THR B 1 213 ? 35.385  -5.735  69.826  1.00 45.95  ? 214 THR B CG2 1 
ATOM   4617  N  N   . ARG B 1 214 ? 35.557  -1.578  71.492  1.00 43.28  ? 215 ARG B N   1 
ATOM   4618  C  CA  . ARG B 1 214 ? 35.058  -0.314  72.043  1.00 46.22  ? 215 ARG B CA  1 
ATOM   4619  C  C   . ARG B 1 214 ? 35.522  0.910   71.233  1.00 39.44  ? 215 ARG B C   1 
ATOM   4620  O  O   . ARG B 1 214 ? 34.703  1.733   70.795  1.00 41.49  ? 215 ARG B O   1 
ATOM   4621  C  CB  . ARG B 1 214 ? 35.486  -0.175  73.508  1.00 47.52  ? 215 ARG B CB  1 
ATOM   4622  C  CG  . ARG B 1 214 ? 34.818  -1.187  74.436  1.00 51.96  ? 215 ARG B CG  1 
ATOM   4623  C  CD  . ARG B 1 214 ? 35.514  -1.289  75.790  1.00 62.24  ? 215 ARG B CD  1 
ATOM   4624  N  NE  . ARG B 1 214 ? 34.965  -0.368  76.782  1.00 73.73  ? 215 ARG B NE  1 
ATOM   4625  C  CZ  . ARG B 1 214 ? 35.481  0.824   77.064  1.00 78.66  ? 215 ARG B CZ  1 
ATOM   4626  N  NH1 . ARG B 1 214 ? 36.567  1.245   76.432  1.00 81.58  ? 215 ARG B NH1 1 
ATOM   4627  N  NH2 . ARG B 1 214 ? 34.914  1.594   77.984  1.00 81.81  ? 215 ARG B NH2 1 
ATOM   4628  N  N   . ALA B 1 215 ? 36.831  1.011   71.018  1.00 32.91  ? 216 ALA B N   1 
ATOM   4629  C  CA  . ALA B 1 215 ? 37.418  2.152   70.314  1.00 35.31  ? 216 ALA B CA  1 
ATOM   4630  C  C   . ALA B 1 215 ? 36.906  2.289   68.879  1.00 40.20  ? 216 ALA B C   1 
ATOM   4631  O  O   . ALA B 1 215 ? 36.382  3.343   68.491  1.00 43.15  ? 216 ALA B O   1 
ATOM   4632  C  CB  . ALA B 1 215 ? 38.935  2.041   70.318  1.00 33.87  ? 216 ALA B CB  1 
ATOM   4633  N  N   . PHE B 1 216 ? 37.065  1.224   68.096  1.00 36.04  ? 217 PHE B N   1 
ATOM   4634  C  CA  . PHE B 1 216 ? 36.652  1.243   66.697  1.00 39.02  ? 217 PHE B CA  1 
ATOM   4635  C  C   . PHE B 1 216 ? 35.159  1.525   66.559  1.00 35.74  ? 217 PHE B C   1 
ATOM   4636  O  O   . PHE B 1 216 ? 34.747  2.248   65.646  1.00 31.83  ? 217 PHE B O   1 
ATOM   4637  C  CB  . PHE B 1 216 ? 37.002  -0.078  66.001  1.00 39.75  ? 217 PHE B CB  1 
ATOM   4638  C  CG  . PHE B 1 216 ? 38.437  -0.171  65.548  1.00 47.22  ? 217 PHE B CG  1 
ATOM   4639  C  CD1 . PHE B 1 216 ? 38.838  0.398   64.350  1.00 51.91  ? 217 PHE B CD1 1 
ATOM   4640  C  CD2 . PHE B 1 216 ? 39.381  -0.841  66.311  1.00 48.46  ? 217 PHE B CD2 1 
ATOM   4641  C  CE1 . PHE B 1 216 ? 40.155  0.310   63.928  1.00 48.75  ? 217 PHE B CE1 1 
ATOM   4642  C  CE2 . PHE B 1 216 ? 40.698  -0.933  65.895  1.00 47.78  ? 217 PHE B CE2 1 
ATOM   4643  C  CZ  . PHE B 1 216 ? 41.085  -0.357  64.702  1.00 49.02  ? 217 PHE B CZ  1 
ATOM   4644  N  N   . VAL B 1 217 ? 34.347  0.973   67.460  1.00 35.28  ? 218 VAL B N   1 
ATOM   4645  C  CA  . VAL B 1 217 ? 32.910  1.208   67.359  1.00 31.50  ? 218 VAL B CA  1 
ATOM   4646  C  C   . VAL B 1 217 ? 32.591  2.658   67.730  1.00 41.01  ? 218 VAL B C   1 
ATOM   4647  O  O   . VAL B 1 217 ? 31.687  3.258   67.149  1.00 38.79  ? 218 VAL B O   1 
ATOM   4648  C  CB  . VAL B 1 217 ? 32.079  0.219   68.228  1.00 39.05  ? 218 VAL B CB  1 
ATOM   4649  C  CG1 . VAL B 1 217 ? 32.004  0.659   69.683  1.00 31.93  ? 218 VAL B CG1 1 
ATOM   4650  C  CG2 . VAL B 1 217 ? 30.680  0.074   67.658  1.00 35.18  ? 218 VAL B CG2 1 
ATOM   4651  N  N   . ALA B 1 218 ? 33.351  3.234   68.661  1.00 46.36  ? 219 ALA B N   1 
ATOM   4652  C  CA  . ALA B 1 218 ? 33.149  4.638   69.011  1.00 38.43  ? 219 ALA B CA  1 
ATOM   4653  C  C   . ALA B 1 218 ? 33.465  5.545   67.820  1.00 38.68  ? 219 ALA B C   1 
ATOM   4654  O  O   . ALA B 1 218 ? 32.642  6.387   67.422  1.00 34.38  ? 219 ALA B O   1 
ATOM   4655  C  CB  . ALA B 1 218 ? 34.000  5.018   70.212  1.00 30.87  ? 219 ALA B CB  1 
ATOM   4656  N  N   . ALA B 1 219 ? 34.654  5.360   67.252  1.00 40.75  ? 220 ALA B N   1 
ATOM   4657  C  CA  . ALA B 1 219 ? 35.092  6.153   66.102  1.00 41.68  ? 220 ALA B CA  1 
ATOM   4658  C  C   . ALA B 1 219 ? 34.111  6.042   64.933  1.00 38.96  ? 220 ALA B C   1 
ATOM   4659  O  O   . ALA B 1 219 ? 33.618  7.058   64.396  1.00 38.07  ? 220 ALA B O   1 
ATOM   4660  C  CB  . ALA B 1 219 ? 36.484  5.716   65.667  1.00 30.97  ? 220 ALA B CB  1 
ATOM   4661  N  N   . ARG B 1 220 ? 33.831  4.798   64.551  1.00 30.50  ? 221 ARG B N   1 
ATOM   4662  C  CA  . ARG B 1 220 ? 32.917  4.525   63.451  1.00 45.39  ? 221 ARG B CA  1 
ATOM   4663  C  C   . ARG B 1 220 ? 31.549  5.146   63.699  1.00 41.48  ? 221 ARG B C   1 
ATOM   4664  O  O   . ARG B 1 220 ? 30.946  5.701   62.785  1.00 34.64  ? 221 ARG B O   1 
ATOM   4665  C  CB  . ARG B 1 220 ? 32.766  3.022   63.227  1.00 38.73  ? 221 ARG B CB  1 
ATOM   4666  C  CG  . ARG B 1 220 ? 31.985  2.671   61.973  1.00 37.52  ? 221 ARG B CG  1 
ATOM   4667  C  CD  . ARG B 1 220 ? 31.878  1.169   61.797  1.00 40.73  ? 221 ARG B CD  1 
ATOM   4668  N  NE  . ARG B 1 220 ? 31.140  0.550   62.892  1.00 41.75  ? 221 ARG B NE  1 
ATOM   4669  C  CZ  . ARG B 1 220 ? 31.340  -0.692  63.318  1.00 53.82  ? 221 ARG B CZ  1 
ATOM   4670  N  NH1 . ARG B 1 220 ? 32.265  -1.450  62.744  1.00 56.55  ? 221 ARG B NH1 1 
ATOM   4671  N  NH2 . ARG B 1 220 ? 30.621  -1.175  64.321  1.00 54.69  ? 221 ARG B NH2 1 
ATOM   4672  N  N   . SER B 1 221 ? 31.066  5.056   64.934  1.00 29.92  ? 222 SER B N   1 
ATOM   4673  C  CA  . SER B 1 221 ? 29.762  5.615   65.269  1.00 36.63  ? 222 SER B CA  1 
ATOM   4674  C  C   . SER B 1 221 ? 29.750  7.134   65.141  1.00 36.30  ? 222 SER B C   1 
ATOM   4675  O  O   . SER B 1 221 ? 28.779  7.710   64.649  1.00 28.99  ? 222 SER B O   1 
ATOM   4676  C  CB  . SER B 1 221 ? 29.347  5.205   66.680  1.00 39.05  ? 222 SER B CB  1 
ATOM   4677  O  OG  . SER B 1 221 ? 29.092  3.812   66.736  1.00 48.07  ? 222 SER B OG  1 
ATOM   4678  N  N   . PHE B 1 222 ? 30.828  7.778   65.582  1.00 34.51  ? 223 PHE B N   1 
ATOM   4679  C  CA  . PHE B 1 222 ? 30.938  9.230   65.457  1.00 31.79  ? 223 PHE B CA  1 
ATOM   4680  C  C   . PHE B 1 222 ? 30.895  9.654   63.986  1.00 32.46  ? 223 PHE B C   1 
ATOM   4681  O  O   . PHE B 1 222 ? 30.068  10.500  63.579  1.00 33.49  ? 223 PHE B O   1 
ATOM   4682  C  CB  . PHE B 1 222 ? 32.225  9.722   66.123  1.00 29.17  ? 223 PHE B CB  1 
ATOM   4683  C  CG  . PHE B 1 222 ? 32.333  11.218  66.214  1.00 42.82  ? 223 PHE B CG  1 
ATOM   4684  C  CD1 . PHE B 1 222 ? 31.564  11.926  67.123  1.00 33.36  ? 223 PHE B CD1 1 
ATOM   4685  C  CD2 . PHE B 1 222 ? 33.216  11.914  65.405  1.00 38.80  ? 223 PHE B CD2 1 
ATOM   4686  C  CE1 . PHE B 1 222 ? 31.665  13.301  67.216  1.00 32.09  ? 223 PHE B CE1 1 
ATOM   4687  C  CE2 . PHE B 1 222 ? 33.322  13.291  65.493  1.00 34.63  ? 223 PHE B CE2 1 
ATOM   4688  C  CZ  . PHE B 1 222 ? 32.546  13.984  66.400  1.00 34.62  ? 223 PHE B CZ  1 
ATOM   4689  N  N   . VAL B 1 223 ? 31.775  9.049   63.188  1.00 29.35  ? 224 VAL B N   1 
ATOM   4690  C  CA  . VAL B 1 223 ? 31.825  9.350   61.753  1.00 34.54  ? 224 VAL B CA  1 
ATOM   4691  C  C   . VAL B 1 223 ? 30.467  9.118   61.067  1.00 34.46  ? 224 VAL B C   1 
ATOM   4692  O  O   . VAL B 1 223 ? 29.975  9.970   60.305  1.00 34.49  ? 224 VAL B O   1 
ATOM   4693  C  CB  . VAL B 1 223 ? 32.917  8.509   61.058  1.00 33.37  ? 224 VAL B CB  1 
ATOM   4694  C  CG1 . VAL B 1 223 ? 32.691  8.445   59.557  1.00 34.95  ? 224 VAL B CG1 1 
ATOM   4695  C  CG2 . VAL B 1 223 ? 34.297  9.074   61.377  1.00 30.37  ? 224 VAL B CG2 1 
ATOM   4696  N  N   . GLN B 1 224 ? 29.860  7.973   61.364  1.00 29.53  ? 225 GLN B N   1 
ATOM   4697  C  CA  . GLN B 1 224 ? 28.550  7.615   60.831  1.00 36.81  ? 225 GLN B CA  1 
ATOM   4698  C  C   . GLN B 1 224 ? 27.491  8.654   61.182  1.00 30.28  ? 225 GLN B C   1 
ATOM   4699  O  O   . GLN B 1 224 ? 26.701  9.054   60.328  1.00 29.27  ? 225 GLN B O   1 
ATOM   4700  C  CB  . GLN B 1 224 ? 28.117  6.244   61.354  1.00 29.80  ? 225 GLN B CB  1 
ATOM   4701  C  CG  . GLN B 1 224 ? 28.457  5.087   60.435  1.00 51.77  ? 225 GLN B CG  1 
ATOM   4702  C  CD  . GLN B 1 224 ? 28.253  3.742   61.103  1.00 54.36  ? 225 GLN B CD  1 
ATOM   4703  O  OE1 . GLN B 1 224 ? 27.469  3.617   62.044  1.00 52.43  ? 225 GLN B OE1 1 
ATOM   4704  N  NE2 . GLN B 1 224 ? 28.950  2.724   60.612  1.00 56.32  ? 225 GLN B NE2 1 
ATOM   4705  N  N   . GLY B 1 225 ? 27.477  9.075   62.443  1.00 28.83  ? 226 GLY B N   1 
ATOM   4706  C  CA  . GLY B 1 225 ? 26.566  10.111  62.894  1.00 36.65  ? 226 GLY B CA  1 
ATOM   4707  C  C   . GLY B 1 225 ? 26.737  11.386  62.090  1.00 36.89  ? 226 GLY B C   1 
ATOM   4708  O  O   . GLY B 1 225 ? 25.749  11.980  61.628  1.00 28.40  ? 226 GLY B O   1 
ATOM   4709  N  N   . LEU B 1 226 ? 27.992  11.803  61.915  1.00 28.57  ? 227 LEU B N   1 
ATOM   4710  C  CA  . LEU B 1 226 ? 28.276  12.967  61.071  1.00 32.92  ? 227 LEU B CA  1 
ATOM   4711  C  C   . LEU B 1 226 ? 27.660  12.811  59.676  1.00 34.72  ? 227 LEU B C   1 
ATOM   4712  O  O   . LEU B 1 226 ? 26.954  13.712  59.181  1.00 36.00  ? 227 LEU B O   1 
ATOM   4713  C  CB  . LEU B 1 226 ? 29.785  13.196  60.961  1.00 29.80  ? 227 LEU B CB  1 
ATOM   4714  C  CG  . LEU B 1 226 ? 30.427  13.960  62.121  1.00 32.54  ? 227 LEU B CG  1 
ATOM   4715  C  CD1 . LEU B 1 226 ? 31.943  13.959  62.017  1.00 29.33  ? 227 LEU B CD1 1 
ATOM   4716  C  CD2 . LEU B 1 226 ? 29.896  15.385  62.161  1.00 28.80  ? 227 LEU B CD2 1 
ATOM   4717  N  N   . GLY B 1 227 ? 27.914  11.660  59.056  1.00 29.35  ? 228 GLY B N   1 
ATOM   4718  C  CA  . GLY B 1 227 ? 27.367  11.374  57.739  1.00 34.48  ? 228 GLY B CA  1 
ATOM   4719  C  C   . GLY B 1 227 ? 25.849  11.455  57.670  1.00 34.85  ? 228 GLY B C   1 
ATOM   4720  O  O   . GLY B 1 227 ? 25.283  12.024  56.729  1.00 39.68  ? 228 GLY B O   1 
ATOM   4721  N  N   . VAL B 1 228 ? 25.189  10.888  58.675  1.00 30.10  ? 229 VAL B N   1 
ATOM   4722  C  CA  . VAL B 1 228 ? 23.732  10.881  58.738  1.00 33.21  ? 229 VAL B CA  1 
ATOM   4723  C  C   . VAL B 1 228 ? 23.180  12.296  58.869  1.00 34.09  ? 229 VAL B C   1 
ATOM   4724  O  O   . VAL B 1 228 ? 22.249  12.668  58.155  1.00 32.23  ? 229 VAL B O   1 
ATOM   4725  C  CB  . VAL B 1 228 ? 23.222  10.023  59.911  1.00 32.90  ? 229 VAL B CB  1 
ATOM   4726  C  CG1 . VAL B 1 228 ? 21.722  10.221  60.110  1.00 34.62  ? 229 VAL B CG1 1 
ATOM   4727  C  CG2 . VAL B 1 228 ? 23.540  8.561   59.667  1.00 35.57  ? 229 VAL B CG2 1 
ATOM   4728  N  N   . ALA B 1 229 ? 23.759  13.082  59.775  1.00 32.83  ? 230 ALA B N   1 
ATOM   4729  C  CA  . ALA B 1 229 ? 23.354  14.479  59.924  1.00 34.76  ? 230 ALA B CA  1 
ATOM   4730  C  C   . ALA B 1 229 ? 23.485  15.225  58.595  1.00 38.54  ? 230 ALA B C   1 
ATOM   4731  O  O   . ALA B 1 229 ? 22.556  15.934  58.161  1.00 39.16  ? 230 ALA B O   1 
ATOM   4732  C  CB  . ALA B 1 229 ? 24.181  15.160  61.001  1.00 33.89  ? 230 ALA B CB  1 
ATOM   4733  N  N   . SER B 1 230 ? 24.635  15.049  57.946  1.00 39.45  ? 231 SER B N   1 
ATOM   4734  C  CA  . SER B 1 230 ? 24.852  15.645  56.630  1.00 42.95  ? 231 SER B CA  1 
ATOM   4735  C  C   . SER B 1 230 ? 23.739  15.256  55.655  1.00 40.25  ? 231 SER B C   1 
ATOM   4736  O  O   . SER B 1 230 ? 23.193  16.105  54.938  1.00 44.93  ? 231 SER B O   1 
ATOM   4737  C  CB  . SER B 1 230 ? 26.211  15.227  56.068  1.00 45.70  ? 231 SER B CB  1 
ATOM   4738  O  OG  . SER B 1 230 ? 26.338  15.617  54.712  1.00 48.92  ? 231 SER B OG  1 
ATOM   4739  N  N   . ASP B 1 231 ? 23.393  13.972  55.652  1.00 30.22  ? 232 ASP B N   1 
ATOM   4740  C  CA  . ASP B 1 231 ? 22.357  13.463  54.757  1.00 33.71  ? 232 ASP B CA  1 
ATOM   4741  C  C   . ASP B 1 231 ? 20.979  14.063  55.028  1.00 35.76  ? 232 ASP B C   1 
ATOM   4742  O  O   . ASP B 1 231 ? 20.265  14.421  54.088  1.00 31.12  ? 232 ASP B O   1 
ATOM   4743  C  CB  . ASP B 1 231 ? 22.277  11.939  54.846  1.00 37.15  ? 232 ASP B CB  1 
ATOM   4744  C  CG  . ASP B 1 231 ? 23.463  11.257  54.198  1.00 52.28  ? 232 ASP B CG  1 
ATOM   4745  O  OD1 . ASP B 1 231 ? 24.140  11.901  53.369  1.00 60.99  ? 232 ASP B OD1 1 
ATOM   4746  O  OD2 . ASP B 1 231 ? 23.717  10.075  54.515  1.00 58.99  ? 232 ASP B OD2 1 
ATOM   4747  N  N   . VAL B 1 232 ? 20.598  14.168  56.300  1.00 29.96  ? 233 VAL B N   1 
ATOM   4748  C  CA  . VAL B 1 232 ? 19.276  14.697  56.617  1.00 35.41  ? 233 VAL B CA  1 
ATOM   4749  C  C   . VAL B 1 232 ? 19.226  16.178  56.256  1.00 34.83  ? 233 VAL B C   1 
ATOM   4750  O  O   . VAL B 1 232 ? 18.203  16.663  55.759  1.00 39.38  ? 233 VAL B O   1 
ATOM   4751  C  CB  . VAL B 1 232 ? 18.876  14.477  58.109  1.00 45.75  ? 233 VAL B CB  1 
ATOM   4752  C  CG1 . VAL B 1 232 ? 19.100  13.030  58.513  1.00 41.29  ? 233 VAL B CG1 1 
ATOM   4753  C  CG2 . VAL B 1 232 ? 19.619  15.413  59.049  1.00 50.96  ? 233 VAL B CG2 1 
ATOM   4754  N  N   . VAL B 1 233 ? 20.336  16.888  56.458  1.00 35.29  ? 234 VAL B N   1 
ATOM   4755  C  CA  . VAL B 1 233 ? 20.383  18.283  56.040  1.00 29.85  ? 234 VAL B CA  1 
ATOM   4756  C  C   . VAL B 1 233 ? 20.205  18.385  54.527  1.00 32.40  ? 234 VAL B C   1 
ATOM   4757  O  O   . VAL B 1 233 ? 19.416  19.200  54.041  1.00 31.73  ? 234 VAL B O   1 
ATOM   4758  C  CB  . VAL B 1 233 ? 21.697  18.967  56.453  1.00 34.75  ? 234 VAL B CB  1 
ATOM   4759  C  CG1 . VAL B 1 233 ? 21.787  20.353  55.833  1.00 32.49  ? 234 VAL B CG1 1 
ATOM   4760  C  CG2 . VAL B 1 233 ? 21.788  19.059  57.967  1.00 29.06  ? 234 VAL B CG2 1 
ATOM   4761  N  N   . ARG B 1 234 ? 20.916  17.537  53.788  1.00 36.37  ? 235 ARG B N   1 
ATOM   4762  C  CA  . ARG B 1 234 ? 20.863  17.585  52.327  1.00 41.41  ? 235 ARG B CA  1 
ATOM   4763  C  C   . ARG B 1 234 ? 19.484  17.235  51.763  1.00 43.22  ? 235 ARG B C   1 
ATOM   4764  O  O   . ARG B 1 234 ? 19.032  17.851  50.798  1.00 43.18  ? 235 ARG B O   1 
ATOM   4765  C  CB  . ARG B 1 234 ? 21.916  16.651  51.724  1.00 43.79  ? 235 ARG B CB  1 
ATOM   4766  C  CG  . ARG B 1 234 ? 21.984  16.709  50.204  1.00 51.34  ? 235 ARG B CG  1 
ATOM   4767  C  CD  . ARG B 1 234 ? 23.185  15.952  49.664  1.00 57.72  ? 235 ARG B CD  1 
ATOM   4768  N  NE  . ARG B 1 234 ? 23.195  14.559  50.100  1.00 60.01  ? 235 ARG B NE  1 
ATOM   4769  C  CZ  . ARG B 1 234 ? 22.464  13.596  49.548  1.00 62.82  ? 235 ARG B CZ  1 
ATOM   4770  N  NH1 . ARG B 1 234 ? 21.657  13.870  48.531  1.00 63.33  ? 235 ARG B NH1 1 
ATOM   4771  N  NH2 . ARG B 1 234 ? 22.540  12.356  50.012  1.00 63.04  ? 235 ARG B NH2 1 
ATOM   4772  N  N   . LYS B 1 235 ? 18.818  16.252  52.360  1.00 38.94  ? 236 LYS B N   1 
ATOM   4773  C  CA  . LYS B 1 235 ? 17.514  15.823  51.862  1.00 40.43  ? 236 LYS B CA  1 
ATOM   4774  C  C   . LYS B 1 235 ? 16.405  16.787  52.265  1.00 41.69  ? 236 LYS B C   1 
ATOM   4775  O  O   . LYS B 1 235 ? 15.499  17.059  51.477  1.00 45.92  ? 236 LYS B O   1 
ATOM   4776  C  CB  . LYS B 1 235 ? 17.186  14.410  52.350  1.00 34.80  ? 236 LYS B CB  1 
ATOM   4777  C  CG  . LYS B 1 235 ? 18.122  13.347  51.800  1.00 37.48  ? 236 LYS B CG  1 
ATOM   4778  C  CD  . LYS B 1 235 ? 17.534  11.954  51.931  1.00 37.76  ? 236 LYS B CD  1 
ATOM   4779  C  CE  . LYS B 1 235 ? 18.406  10.930  51.222  1.00 47.80  ? 236 LYS B CE  1 
ATOM   4780  N  NZ  . LYS B 1 235 ? 17.824  9.559   51.278  1.00 53.79  ? 236 LYS B NZ  1 
ATOM   4781  N  N   . VAL B 1 236 ? 16.472  17.307  53.487  1.00 39.14  ? 237 VAL B N   1 
ATOM   4782  C  CA  . VAL B 1 236 ? 15.474  18.272  53.932  1.00 38.47  ? 237 VAL B CA  1 
ATOM   4783  C  C   . VAL B 1 236 ? 15.651  19.595  53.180  1.00 39.87  ? 237 VAL B C   1 
ATOM   4784  O  O   . VAL B 1 236 ? 14.684  20.321  52.944  1.00 36.56  ? 237 VAL B O   1 
ATOM   4785  C  CB  . VAL B 1 236 ? 15.550  18.497  55.460  1.00 33.77  ? 237 VAL B CB  1 
ATOM   4786  C  CG1 . VAL B 1 236 ? 14.678  19.670  55.892  1.00 34.11  ? 237 VAL B CG1 1 
ATOM   4787  C  CG2 . VAL B 1 236 ? 15.129  17.233  56.192  1.00 33.81  ? 237 VAL B CG2 1 
ATOM   4788  N  N   . ALA B 1 237 ? 16.884  19.885  52.770  1.00 46.54  ? 238 ALA B N   1 
ATOM   4789  C  CA  . ALA B 1 237 ? 17.183  21.124  52.051  1.00 46.84  ? 238 ALA B CA  1 
ATOM   4790  C  C   . ALA B 1 237 ? 16.419  21.256  50.731  1.00 50.31  ? 238 ALA B C   1 
ATOM   4791  O  O   . ALA B 1 237 ? 16.196  22.368  50.251  1.00 54.21  ? 238 ALA B O   1 
ATOM   4792  C  CB  . ALA B 1 237 ? 18.680  21.233  51.794  1.00 47.08  ? 238 ALA B CB  1 
ATOM   4793  N  N   . GLN B 1 238 ? 16.019  20.131  50.145  1.00 51.17  ? 239 GLN B N   1 
ATOM   4794  C  CA  . GLN B 1 238 ? 15.328  20.157  48.858  1.00 55.63  ? 239 GLN B CA  1 
ATOM   4795  C  C   . GLN B 1 238 ? 13.815  20.002  48.998  1.00 50.38  ? 239 GLN B C   1 
ATOM   4796  O  O   . GLN B 1 238 ? 13.109  19.819  48.006  1.00 48.38  ? 239 GLN B O   1 
ATOM   4797  C  CB  . GLN B 1 238 ? 15.872  19.069  47.930  1.00 67.77  ? 239 GLN B CB  1 
ATOM   4798  C  CG  . GLN B 1 238 ? 16.654  19.627  46.752  1.00 78.03  ? 239 GLN B CG  1 
ATOM   4799  C  CD  . GLN B 1 238 ? 16.379  18.898  45.452  1.00 88.49  ? 239 GLN B CD  1 
ATOM   4800  O  OE1 . GLN B 1 238 ? 16.083  17.704  45.443  1.00 91.77  ? 239 GLN B OE1 1 
ATOM   4801  N  NE2 . GLN B 1 238 ? 16.469  19.622  44.341  1.00 91.72  ? 239 GLN B NE2 1 
ATOM   4802  N  N   . VAL B 1 239 ? 13.321  20.071  50.229  1.00 45.01  ? 240 VAL B N   1 
ATOM   4803  C  CA  . VAL B 1 239 ? 11.883  20.096  50.461  1.00 41.45  ? 240 VAL B CA  1 
ATOM   4804  C  C   . VAL B 1 239 ? 11.334  21.460  50.063  1.00 42.35  ? 240 VAL B C   1 
ATOM   4805  O  O   . VAL B 1 239 ? 11.751  22.483  50.607  1.00 36.67  ? 240 VAL B O   1 
ATOM   4806  C  CB  . VAL B 1 239 ? 11.528  19.801  51.929  1.00 37.57  ? 240 VAL B CB  1 
ATOM   4807  C  CG1 . VAL B 1 239 ? 10.075  20.157  52.203  1.00 38.35  ? 240 VAL B CG1 1 
ATOM   4808  C  CG2 . VAL B 1 239 ? 11.799  18.343  52.257  1.00 34.98  ? 240 VAL B CG2 1 
ATOM   4809  N  N   . PRO B 1 240 ? 10.399  21.478  49.102  1.00 50.30  ? 241 PRO B N   1 
ATOM   4810  C  CA  . PRO B 1 240 ? 9.846   22.718  48.548  1.00 48.91  ? 241 PRO B CA  1 
ATOM   4811  C  C   . PRO B 1 240 ? 8.885   23.434  49.493  1.00 44.89  ? 241 PRO B C   1 
ATOM   4812  O  O   . PRO B 1 240 ? 8.186   22.790  50.276  1.00 42.06  ? 241 PRO B O   1 
ATOM   4813  C  CB  . PRO B 1 240 ? 9.105   22.234  47.300  1.00 48.80  ? 241 PRO B CB  1 
ATOM   4814  C  CG  . PRO B 1 240 ? 8.677   20.851  47.652  1.00 49.82  ? 241 PRO B CG  1 
ATOM   4815  C  CD  . PRO B 1 240 ? 9.799   20.283  48.483  1.00 47.70  ? 241 PRO B CD  1 
ATOM   4816  N  N   . LEU B 1 241 ? 8.858   24.760  49.417  1.00 48.81  ? 242 LEU B N   1 
ATOM   4817  C  CA  . LEU B 1 241 ? 7.871   25.540  50.150  1.00 52.96  ? 242 LEU B CA  1 
ATOM   4818  C  C   . LEU B 1 241 ? 6.515   25.431  49.466  1.00 42.88  ? 242 LEU B C   1 
ATOM   4819  O  O   . LEU B 1 241 ? 6.421   25.518  48.243  1.00 43.84  ? 242 LEU B O   1 
ATOM   4820  C  CB  . LEU B 1 241 ? 8.297   27.005  50.250  1.00 58.06  ? 242 LEU B CB  1 
ATOM   4821  C  CG  . LEU B 1 241 ? 9.475   27.312  51.175  1.00 65.14  ? 242 LEU B CG  1 
ATOM   4822  C  CD1 . LEU B 1 241 ? 9.805   28.790  51.128  1.00 65.40  ? 242 LEU B CD1 1 
ATOM   4823  C  CD2 . LEU B 1 241 ? 9.165   26.877  52.598  1.00 67.81  ? 242 LEU B CD2 1 
ATOM   4824  N  N   . GLY B 1 242 ? 5.468   25.233  50.259  1.00 36.85  ? 243 GLY B N   1 
ATOM   4825  C  CA  . GLY B 1 242 ? 4.123   25.129  49.725  1.00 46.11  ? 243 GLY B CA  1 
ATOM   4826  C  C   . GLY B 1 242 ? 3.582   26.465  49.253  1.00 44.90  ? 243 GLY B C   1 
ATOM   4827  O  O   . GLY B 1 242 ? 4.096   27.516  49.638  1.00 44.55  ? 243 GLY B O   1 
ATOM   4828  N  N   . PRO B 1 243 ? 2.538   26.430  48.410  1.00 47.44  ? 244 PRO B N   1 
ATOM   4829  C  CA  . PRO B 1 243 ? 1.890   27.625  47.852  1.00 51.35  ? 244 PRO B CA  1 
ATOM   4830  C  C   . PRO B 1 243 ? 1.317   28.552  48.924  1.00 50.89  ? 244 PRO B C   1 
ATOM   4831  O  O   . PRO B 1 243 ? 1.403   29.775  48.785  1.00 51.03  ? 244 PRO B O   1 
ATOM   4832  C  CB  . PRO B 1 243 ? 0.769   27.043  46.979  1.00 51.09  ? 244 PRO B CB  1 
ATOM   4833  C  CG  . PRO B 1 243 ? 0.571   25.645  47.473  1.00 50.93  ? 244 PRO B CG  1 
ATOM   4834  C  CD  . PRO B 1 243 ? 1.921   25.189  47.915  1.00 43.44  ? 244 PRO B CD  1 
ATOM   4835  N  N   . GLU B 1 244 ? 0.735   27.971  49.970  1.00 46.84  ? 245 GLU B N   1 
ATOM   4836  C  CA  . GLU B 1 244 ? 0.224   28.741  51.099  1.00 49.44  ? 245 GLU B CA  1 
ATOM   4837  C  C   . GLU B 1 244 ? 1.326   29.618  51.680  1.00 45.67  ? 245 GLU B C   1 
ATOM   4838  O  O   . GLU B 1 244 ? 1.150   30.829  51.873  1.00 43.76  ? 245 GLU B O   1 
ATOM   4839  C  CB  . GLU B 1 244 ? -0.337  27.808  52.175  1.00 38.63  ? 245 GLU B CB  1 
ATOM   4840  N  N   . CYS B 1 245 ? 2.469   28.992  51.942  1.00 37.35  ? 246 CYS B N   1 
ATOM   4841  C  CA  . CYS B 1 245 ? 3.647   29.695  52.428  1.00 36.61  ? 246 CYS B CA  1 
ATOM   4842  C  C   . CYS B 1 245 ? 4.068   30.793  51.461  1.00 37.25  ? 246 CYS B C   1 
ATOM   4843  O  O   . CYS B 1 245 ? 4.446   31.880  51.884  1.00 37.08  ? 246 CYS B O   1 
ATOM   4844  C  CB  . CYS B 1 245 ? 4.806   28.719  52.645  1.00 43.91  ? 246 CYS B CB  1 
ATOM   4845  S  SG  . CYS B 1 245 ? 6.397   29.515  52.972  1.00 164.66 ? 246 CYS B SG  1 
ATOM   4846  N  N   . SER B 1 246 ? 3.997   30.507  50.164  1.00 40.89  ? 247 SER B N   1 
ATOM   4847  C  CA  . SER B 1 246 ? 4.378   31.478  49.143  1.00 46.04  ? 247 SER B CA  1 
ATOM   4848  C  C   . SER B 1 246 ? 3.506   32.730  49.223  1.00 48.27  ? 247 SER B C   1 
ATOM   4849  O  O   . SER B 1 246 ? 4.014   33.856  49.216  1.00 51.70  ? 247 SER B O   1 
ATOM   4850  C  CB  . SER B 1 246 ? 4.287   30.854  47.749  1.00 51.87  ? 247 SER B CB  1 
ATOM   4851  O  OG  . SER B 1 246 ? 4.788   31.737  46.760  1.00 58.90  ? 247 SER B OG  1 
ATOM   4852  N  N   . ARG B 1 247 ? 2.193   32.526  49.306  1.00 48.24  ? 248 ARG B N   1 
ATOM   4853  C  CA  . ARG B 1 247 ? 1.253   33.631  49.465  1.00 46.12  ? 248 ARG B CA  1 
ATOM   4854  C  C   . ARG B 1 247 ? 1.527   34.413  50.744  1.00 44.91  ? 248 ARG B C   1 
ATOM   4855  O  O   . ARG B 1 247 ? 1.521   35.646  50.740  1.00 40.10  ? 248 ARG B O   1 
ATOM   4856  C  CB  . ARG B 1 247 ? -0.190  33.126  49.475  1.00 51.19  ? 248 ARG B CB  1 
ATOM   4857  C  CG  . ARG B 1 247 ? -0.685  32.596  48.144  1.00 58.55  ? 248 ARG B CG  1 
ATOM   4858  C  CD  . ARG B 1 247 ? -2.194  32.413  48.170  1.00 66.50  ? 248 ARG B CD  1 
ATOM   4859  N  NE  . ARG B 1 247 ? -2.601  31.433  49.173  1.00 72.41  ? 248 ARG B NE  1 
ATOM   4860  C  CZ  . ARG B 1 247 ? -2.657  30.123  48.957  1.00 77.56  ? 248 ARG B CZ  1 
ATOM   4861  N  NH1 . ARG B 1 247 ? -3.038  29.304  49.929  1.00 78.72  ? 248 ARG B NH1 1 
ATOM   4862  N  NH2 . ARG B 1 247 ? -2.332  29.630  47.769  1.00 78.98  ? 248 ARG B NH2 1 
ATOM   4863  N  N   . ALA B 1 248 ? 1.760   33.691  51.838  1.00 40.21  ? 249 ALA B N   1 
ATOM   4864  C  CA  . ALA B 1 248 ? 2.048   34.333  53.118  1.00 39.29  ? 249 ALA B CA  1 
ATOM   4865  C  C   . ALA B 1 248 ? 3.284   35.227  53.032  1.00 43.55  ? 249 ALA B C   1 
ATOM   4866  O  O   . ALA B 1 248 ? 3.291   36.349  53.544  1.00 44.81  ? 249 ALA B O   1 
ATOM   4867  C  CB  . ALA B 1 248 ? 2.229   33.288  54.199  1.00 37.01  ? 249 ALA B CB  1 
ATOM   4868  N  N   . VAL B 1 249 ? 4.321   34.723  52.371  1.00 37.68  ? 250 VAL B N   1 
ATOM   4869  C  CA  . VAL B 1 249 ? 5.578   35.446  52.218  1.00 43.31  ? 250 VAL B CA  1 
ATOM   4870  C  C   . VAL B 1 249 ? 5.405   36.671  51.324  1.00 40.17  ? 250 VAL B C   1 
ATOM   4871  O  O   . VAL B 1 249 ? 5.946   37.742  51.614  1.00 40.66  ? 250 VAL B O   1 
ATOM   4872  C  CB  . VAL B 1 249 ? 6.679   34.532  51.642  1.00 37.38  ? 250 VAL B CB  1 
ATOM   4873  C  CG1 . VAL B 1 249 ? 7.915   35.336  51.277  1.00 37.68  ? 250 VAL B CG1 1 
ATOM   4874  C  CG2 . VAL B 1 249 ? 7.030   33.446  52.640  1.00 36.27  ? 250 VAL B CG2 1 
ATOM   4875  N  N   . MET B 1 250 ? 4.650   36.510  50.240  1.00 39.68  ? 251 MET B N   1 
ATOM   4876  C  CA  . MET B 1 250 ? 4.320   37.636  49.373  1.00 44.00  ? 251 MET B CA  1 
ATOM   4877  C  C   . MET B 1 250 ? 3.607   38.729  50.162  1.00 46.94  ? 251 MET B C   1 
ATOM   4878  O  O   . MET B 1 250 ? 3.951   39.908  50.065  1.00 41.61  ? 251 MET B O   1 
ATOM   4879  C  CB  . MET B 1 250 ? 3.449   37.182  48.200  1.00 41.91  ? 251 MET B CB  1 
ATOM   4880  C  CG  . MET B 1 250 ? 2.842   38.331  47.400  1.00 47.46  ? 251 MET B CG  1 
ATOM   4881  S  SD  . MET B 1 250 ? 4.066   39.534  46.846  1.00 53.74  ? 251 MET B SD  1 
ATOM   4882  C  CE  . MET B 1 250 ? 3.087   40.533  45.728  1.00 67.19  ? 251 MET B CE  1 
ATOM   4883  N  N   . LYS B 1 251 ? 2.620   38.323  50.954  1.00 46.58  ? 252 LYS B N   1 
ATOM   4884  C  CA  . LYS B 1 251 ? 1.863   39.253  51.784  1.00 46.26  ? 252 LYS B CA  1 
ATOM   4885  C  C   . LYS B 1 251 ? 2.757   39.880  52.849  1.00 50.31  ? 252 LYS B C   1 
ATOM   4886  O  O   . LYS B 1 251 ? 2.483   40.971  53.347  1.00 40.49  ? 252 LYS B O   1 
ATOM   4887  C  CB  . LYS B 1 251 ? 0.676   38.538  52.436  1.00 50.34  ? 252 LYS B CB  1 
ATOM   4888  C  CG  . LYS B 1 251 ? -0.521  39.433  52.704  1.00 56.35  ? 252 LYS B CG  1 
ATOM   4889  C  CD  . LYS B 1 251 ? -1.075  39.224  54.104  1.00 55.47  ? 252 LYS B CD  1 
ATOM   4890  C  CE  . LYS B 1 251 ? -2.456  39.847  54.244  1.00 49.95  ? 252 LYS B CE  1 
ATOM   4891  N  NZ  . LYS B 1 251 ? -2.955  39.781  55.644  1.00 49.57  ? 252 LYS B NZ  1 
ATOM   4892  N  N   . LEU B 1 252 ? 3.836   39.180  53.182  1.00 50.51  ? 253 LEU B N   1 
ATOM   4893  C  CA  . LEU B 1 252 ? 4.778   39.631  54.199  1.00 38.68  ? 253 LEU B CA  1 
ATOM   4894  C  C   . LEU B 1 252 ? 5.780   40.659  53.674  1.00 39.31  ? 253 LEU B C   1 
ATOM   4895  O  O   . LEU B 1 252 ? 6.191   41.561  54.403  1.00 39.39  ? 253 LEU B O   1 
ATOM   4896  C  CB  . LEU B 1 252 ? 5.534   38.427  54.776  1.00 37.58  ? 253 LEU B CB  1 
ATOM   4897  C  CG  . LEU B 1 252 ? 6.701   38.702  55.728  1.00 37.03  ? 253 LEU B CG  1 
ATOM   4898  C  CD1 . LEU B 1 252 ? 6.199   39.143  57.093  1.00 40.27  ? 253 LEU B CD1 1 
ATOM   4899  C  CD2 . LEU B 1 252 ? 7.607   37.485  55.849  1.00 44.93  ? 253 LEU B CD2 1 
ATOM   4900  N  N   . VAL B 1 253 ? 6.168   40.527  52.409  1.00 39.89  ? 254 VAL B N   1 
ATOM   4901  C  CA  . VAL B 1 253 ? 7.334   41.250  51.908  1.00 54.14  ? 254 VAL B CA  1 
ATOM   4902  C  C   . VAL B 1 253 ? 7.028   42.331  50.862  1.00 54.08  ? 254 VAL B C   1 
ATOM   4903  O  O   . VAL B 1 253 ? 7.575   43.433  50.934  1.00 61.17  ? 254 VAL B O   1 
ATOM   4904  C  CB  . VAL B 1 253 ? 8.363   40.256  51.318  1.00 40.11  ? 254 VAL B CB  1 
ATOM   4905  C  CG1 . VAL B 1 253 ? 9.566   40.990  50.746  1.00 40.88  ? 254 VAL B CG1 1 
ATOM   4906  C  CG2 . VAL B 1 253 ? 8.802   39.259  52.384  1.00 38.79  ? 254 VAL B CG2 1 
ATOM   4907  N  N   . TYR B 1 254 ? 6.159   42.035  49.898  1.00 49.16  ? 255 TYR B N   1 
ATOM   4908  C  CA  . TYR B 1 254 ? 5.962   42.952  48.774  1.00 47.67  ? 255 TYR B CA  1 
ATOM   4909  C  C   . TYR B 1 254 ? 4.554   43.536  48.658  1.00 50.91  ? 255 TYR B C   1 
ATOM   4910  O  O   . TYR B 1 254 ? 4.280   44.318  47.747  1.00 55.94  ? 255 TYR B O   1 
ATOM   4911  C  CB  . TYR B 1 254 ? 6.327   42.252  47.465  1.00 46.85  ? 255 TYR B CB  1 
ATOM   4912  C  CG  . TYR B 1 254 ? 7.813   42.052  47.286  1.00 52.02  ? 255 TYR B CG  1 
ATOM   4913  C  CD1 . TYR B 1 254 ? 8.703   43.091  47.521  1.00 51.70  ? 255 TYR B CD1 1 
ATOM   4914  C  CD2 . TYR B 1 254 ? 8.327   40.825  46.892  1.00 52.32  ? 255 TYR B CD2 1 
ATOM   4915  C  CE1 . TYR B 1 254 ? 10.063  42.915  47.364  1.00 52.58  ? 255 TYR B CE1 1 
ATOM   4916  C  CE2 . TYR B 1 254 ? 9.687   40.638  46.731  1.00 54.52  ? 255 TYR B CE2 1 
ATOM   4917  C  CZ  . TYR B 1 254 ? 10.550  41.686  46.968  1.00 55.31  ? 255 TYR B CZ  1 
ATOM   4918  O  OH  . TYR B 1 254 ? 11.905  41.504  46.810  1.00 54.35  ? 255 TYR B OH  1 
ATOM   4919  N  N   . CYS B 1 255 ? 3.665   43.167  49.572  1.00 51.45  ? 256 CYS B N   1 
ATOM   4920  C  CA  . CYS B 1 255 ? 2.324   43.741  49.571  1.00 57.56  ? 256 CYS B CA  1 
ATOM   4921  C  C   . CYS B 1 255 ? 2.349   45.184  50.062  1.00 57.78  ? 256 CYS B C   1 
ATOM   4922  O  O   . CYS B 1 255 ? 1.555   46.011  49.614  1.00 57.06  ? 256 CYS B O   1 
ATOM   4923  C  CB  . CYS B 1 255 ? 1.371   42.904  50.425  1.00 51.38  ? 256 CYS B CB  1 
ATOM   4924  S  SG  . CYS B 1 255 ? 0.543   41.587  49.505  1.00 65.30  ? 256 CYS B SG  1 
ATOM   4925  N  N   . ALA B 1 256 ? 3.266   45.477  50.980  1.00 56.00  ? 257 ALA B N   1 
ATOM   4926  C  CA  . ALA B 1 256 ? 3.454   46.837  51.474  1.00 45.22  ? 257 ALA B CA  1 
ATOM   4927  C  C   . ALA B 1 256 ? 3.794   47.775  50.322  1.00 49.76  ? 257 ALA B C   1 
ATOM   4928  O  O   . ALA B 1 256 ? 3.258   48.878  50.225  1.00 48.02  ? 257 ALA B O   1 
ATOM   4929  C  CB  . ALA B 1 256 ? 4.544   46.875  52.533  1.00 44.41  ? 257 ALA B CB  1 
ATOM   4930  N  N   . HIS B 1 257 ? 4.687   47.319  49.449  1.00 53.45  ? 258 HIS B N   1 
ATOM   4931  C  CA  . HIS B 1 257 ? 5.061   48.066  48.255  1.00 53.45  ? 258 HIS B CA  1 
ATOM   4932  C  C   . HIS B 1 257 ? 3.843   48.336  47.383  1.00 54.29  ? 258 HIS B C   1 
ATOM   4933  O  O   . HIS B 1 257 ? 3.674   49.433  46.852  1.00 50.84  ? 258 HIS B O   1 
ATOM   4934  C  CB  . HIS B 1 257 ? 6.114   47.303  47.447  1.00 57.26  ? 258 HIS B CB  1 
ATOM   4935  C  CG  . HIS B 1 257 ? 7.392   47.063  48.187  1.00 54.82  ? 258 HIS B CG  1 
ATOM   4936  N  ND1 . HIS B 1 257 ? 7.447   46.375  49.380  1.00 52.06  ? 258 HIS B ND1 1 
ATOM   4937  C  CD2 . HIS B 1 257 ? 8.667   47.414  47.897  1.00 54.65  ? 258 HIS B CD2 1 
ATOM   4938  C  CE1 . HIS B 1 257 ? 8.699   46.318  49.796  1.00 55.36  ? 258 HIS B CE1 1 
ATOM   4939  N  NE2 . HIS B 1 257 ? 9.460   46.941  48.914  1.00 56.59  ? 258 HIS B NE2 1 
ATOM   4940  N  N   . CYS B 1 258 ? 2.998   47.321  47.244  1.00 55.19  ? 259 CYS B N   1 
ATOM   4941  C  CA  . CYS B 1 258 ? 1.825   47.412  46.389  1.00 49.94  ? 259 CYS B CA  1 
ATOM   4942  C  C   . CYS B 1 258 ? 0.763   48.336  46.970  1.00 57.84  ? 259 CYS B C   1 
ATOM   4943  O  O   . CYS B 1 258 ? 0.046   49.001  46.230  1.00 61.42  ? 259 CYS B O   1 
ATOM   4944  C  CB  . CYS B 1 258 ? 1.233   46.021  46.151  1.00 49.28  ? 259 CYS B CB  1 
ATOM   4945  S  SG  . CYS B 1 258 ? 2.172   45.008  44.987  1.00 82.94  ? 259 CYS B SG  1 
ATOM   4946  N  N   . LEU B 1 259 ? 0.667   48.384  48.295  1.00 58.83  ? 260 LEU B N   1 
ATOM   4947  C  CA  . LEU B 1 259 ? -0.385  49.164  48.938  1.00 58.29  ? 260 LEU B CA  1 
ATOM   4948  C  C   . LEU B 1 259 ? 0.100   50.528  49.425  1.00 62.32  ? 260 LEU B C   1 
ATOM   4949  O  O   . LEU B 1 259 ? -0.430  51.076  50.391  1.00 63.16  ? 260 LEU B O   1 
ATOM   4950  C  CB  . LEU B 1 259 ? -0.990  48.374  50.100  1.00 62.95  ? 260 LEU B CB  1 
ATOM   4951  C  CG  . LEU B 1 259 ? -1.634  47.043  49.700  1.00 65.44  ? 260 LEU B CG  1 
ATOM   4952  C  CD1 . LEU B 1 259 ? -2.432  46.456  50.854  1.00 66.01  ? 260 LEU B CD1 1 
ATOM   4953  C  CD2 . LEU B 1 259 ? -2.511  47.211  48.465  1.00 68.50  ? 260 LEU B CD2 1 
ATOM   4954  N  N   . GLY B 1 260 ? 1.110   51.070  48.752  1.00 63.24  ? 261 GLY B N   1 
ATOM   4955  C  CA  . GLY B 1 260 ? 1.519   52.447  48.966  1.00 61.15  ? 261 GLY B CA  1 
ATOM   4956  C  C   . GLY B 1 260 ? 2.491   52.716  50.099  1.00 62.75  ? 261 GLY B C   1 
ATOM   4957  O  O   . GLY B 1 260 ? 2.672   53.867  50.496  1.00 65.62  ? 261 GLY B O   1 
ATOM   4958  N  N   . VAL B 1 261 ? 3.123   51.671  50.623  1.00 60.98  ? 262 VAL B N   1 
ATOM   4959  C  CA  . VAL B 1 261 ? 4.141   51.851  51.657  1.00 61.66  ? 262 VAL B CA  1 
ATOM   4960  C  C   . VAL B 1 261 ? 5.380   50.984  51.412  1.00 63.47  ? 262 VAL B C   1 
ATOM   4961  O  O   . VAL B 1 261 ? 5.667   50.067  52.184  1.00 64.11  ? 262 VAL B O   1 
ATOM   4962  C  CB  . VAL B 1 261 ? 3.572   51.552  53.064  1.00 61.45  ? 262 VAL B CB  1 
ATOM   4963  C  CG1 . VAL B 1 261 ? 2.767   52.738  53.573  1.00 60.01  ? 262 VAL B CG1 1 
ATOM   4964  C  CG2 . VAL B 1 261 ? 2.712   50.294  53.047  1.00 61.33  ? 262 VAL B CG2 1 
ATOM   4965  N  N   . PRO B 1 262 ? 6.131   51.286  50.340  1.00 69.28  ? 263 PRO B N   1 
ATOM   4966  C  CA  . PRO B 1 262 ? 7.310   50.493  49.969  1.00 69.06  ? 263 PRO B CA  1 
ATOM   4967  C  C   . PRO B 1 262 ? 8.416   50.546  51.019  1.00 72.06  ? 263 PRO B C   1 
ATOM   4968  O  O   . PRO B 1 262 ? 9.091   49.543  51.253  1.00 71.10  ? 263 PRO B O   1 
ATOM   4969  C  CB  . PRO B 1 262 ? 7.778   51.148  48.662  1.00 71.12  ? 263 PRO B CB  1 
ATOM   4970  C  CG  . PRO B 1 262 ? 6.603   51.933  48.169  1.00 69.55  ? 263 PRO B CG  1 
ATOM   4971  C  CD  . PRO B 1 262 ? 5.917   52.405  49.407  1.00 69.89  ? 263 PRO B CD  1 
ATOM   4972  N  N   . GLY B 1 263 ? 8.595   51.708  51.640  1.00 77.88  ? 264 GLY B N   1 
ATOM   4973  C  CA  . GLY B 1 263 ? 9.652   51.901  52.616  1.00 78.88  ? 264 GLY B CA  1 
ATOM   4974  C  C   . GLY B 1 263 ? 9.412   51.191  53.935  1.00 76.23  ? 264 GLY B C   1 
ATOM   4975  O  O   . GLY B 1 263 ? 10.312  51.097  54.770  1.00 79.16  ? 264 GLY B O   1 
ATOM   4976  N  N   . ALA B 1 264 ? 8.195   50.694  54.127  1.00 72.97  ? 265 ALA B N   1 
ATOM   4977  C  CA  . ALA B 1 264 ? 7.845   49.991  55.354  1.00 66.73  ? 265 ALA B CA  1 
ATOM   4978  C  C   . ALA B 1 264 ? 8.480   48.609  55.369  1.00 63.02  ? 265 ALA B C   1 
ATOM   4979  O  O   . ALA B 1 264 ? 8.574   47.955  54.335  1.00 60.77  ? 265 ALA B O   1 
ATOM   4980  C  CB  . ALA B 1 264 ? 6.333   49.881  55.492  1.00 67.57  ? 265 ALA B CB  1 
ATOM   4981  N  N   . ARG B 1 265 ? 8.925   48.162  56.535  1.00 58.81  ? 266 ARG B N   1 
ATOM   4982  C  CA  . ARG B 1 265 ? 9.414   46.795  56.655  1.00 53.65  ? 266 ARG B CA  1 
ATOM   4983  C  C   . ARG B 1 265 ? 8.565   46.042  57.674  1.00 51.90  ? 266 ARG B C   1 
ATOM   4984  O  O   . ARG B 1 265 ? 8.025   46.646  58.602  1.00 49.26  ? 266 ARG B O   1 
ATOM   4985  C  CB  . ARG B 1 265 ? 10.896  46.777  57.044  1.00 53.96  ? 266 ARG B CB  1 
ATOM   4986  N  N   . PRO B 1 266 ? 8.436   44.717  57.495  1.00 51.37  ? 267 PRO B N   1 
ATOM   4987  C  CA  . PRO B 1 266 ? 7.505   43.909  58.289  1.00 39.22  ? 267 PRO B CA  1 
ATOM   4988  C  C   . PRO B 1 266 ? 7.907   43.772  59.752  1.00 41.12  ? 267 PRO B C   1 
ATOM   4989  O  O   . PRO B 1 266 ? 9.094   43.737  60.077  1.00 38.51  ? 267 PRO B O   1 
ATOM   4990  C  CB  . PRO B 1 266 ? 7.548   42.546  57.593  1.00 51.58  ? 267 PRO B CB  1 
ATOM   4991  C  CG  . PRO B 1 266 ? 8.882   42.497  56.954  1.00 47.28  ? 267 PRO B CG  1 
ATOM   4992  C  CD  . PRO B 1 266 ? 9.173   43.897  56.517  1.00 39.72  ? 267 PRO B CD  1 
ATOM   4993  N  N   . CYS B 1 267 ? 6.904   43.700  60.620  1.00 38.58  ? 268 CYS B N   1 
ATOM   4994  C  CA  A CYS B 1 267 ? 7.151   43.516  62.040  0.58 38.21  ? 268 CYS B CA  1 
ATOM   4995  C  CA  B CYS B 1 267 ? 7.103   43.478  62.049  0.42 38.19  ? 268 CYS B CA  1 
ATOM   4996  C  C   . CYS B 1 267 ? 7.867   42.190  62.304  1.00 59.50  ? 268 CYS B C   1 
ATOM   4997  O  O   . CYS B 1 267 ? 7.636   41.195  61.616  1.00 36.63  ? 268 CYS B O   1 
ATOM   4998  C  CB  A CYS B 1 267 ? 5.838   43.589  62.823  0.58 38.40  ? 268 CYS B CB  1 
ATOM   4999  C  CB  B CYS B 1 267 ? 5.754   43.424  62.769  0.42 38.30  ? 268 CYS B CB  1 
ATOM   5000  S  SG  A CYS B 1 267 ? 4.988   45.187  62.684  0.58 49.04  ? 268 CYS B SG  1 
ATOM   5001  S  SG  B CYS B 1 267 ? 5.852   42.997  64.521  0.42 37.97  ? 268 CYS B SG  1 
ATOM   5002  N  N   . PRO B 1 268 ? 8.772   42.192  63.295  1.00 52.79  ? 269 PRO B N   1 
ATOM   5003  C  CA  . PRO B 1 268 ? 9.513   40.986  63.676  1.00 43.41  ? 269 PRO B CA  1 
ATOM   5004  C  C   . PRO B 1 268 ? 8.601   39.799  63.989  1.00 43.08  ? 269 PRO B C   1 
ATOM   5005  O  O   . PRO B 1 268 ? 8.875   38.694  63.527  1.00 34.79  ? 269 PRO B O   1 
ATOM   5006  C  CB  . PRO B 1 268 ? 10.275  41.431  64.924  1.00 36.36  ? 269 PRO B CB  1 
ATOM   5007  C  CG  . PRO B 1 268 ? 10.501  42.886  64.706  1.00 47.35  ? 269 PRO B CG  1 
ATOM   5008  C  CD  . PRO B 1 268 ? 9.270   43.387  64.000  1.00 44.28  ? 269 PRO B CD  1 
ATOM   5009  N  N   . ASP B 1 269 ? 7.532   40.031  64.746  1.00 39.65  ? 270 ASP B N   1 
ATOM   5010  C  CA  . ASP B 1 269 ? 6.628   38.956  65.150  1.00 35.37  ? 270 ASP B CA  1 
ATOM   5011  C  C   . ASP B 1 269 ? 5.767   38.454  63.993  1.00 44.45  ? 270 ASP B C   1 
ATOM   5012  O  O   . ASP B 1 269 ? 5.446   37.269  63.916  1.00 49.71  ? 270 ASP B O   1 
ATOM   5013  C  CB  . ASP B 1 269 ? 5.737   39.420  66.303  1.00 35.94  ? 270 ASP B CB  1 
ATOM   5014  C  CG  . ASP B 1 269 ? 6.477   39.468  67.625  1.00 45.98  ? 270 ASP B CG  1 
ATOM   5015  O  OD1 . ASP B 1 269 ? 7.724   39.401  67.610  1.00 46.26  ? 270 ASP B OD1 1 
ATOM   5016  O  OD2 . ASP B 1 269 ? 5.813   39.570  68.678  1.00 48.59  ? 270 ASP B OD2 1 
ATOM   5017  N  N   . TYR B 1 270 ? 5.389   39.366  63.104  1.00 48.33  ? 271 TYR B N   1 
ATOM   5018  C  CA  . TYR B 1 270 ? 4.668   39.016  61.885  1.00 46.00  ? 271 TYR B CA  1 
ATOM   5019  C  C   . TYR B 1 270 ? 5.526   38.068  61.047  1.00 35.39  ? 271 TYR B C   1 
ATOM   5020  O  O   . TYR B 1 270 ? 5.092   36.973  60.660  1.00 35.06  ? 271 TYR B O   1 
ATOM   5021  C  CB  . TYR B 1 270 ? 4.319   40.290  61.108  1.00 36.87  ? 271 TYR B CB  1 
ATOM   5022  C  CG  . TYR B 1 270 ? 3.589   40.089  59.798  1.00 37.21  ? 271 TYR B CG  1 
ATOM   5023  C  CD1 . TYR B 1 270 ? 2.761   38.995  59.593  1.00 36.96  ? 271 TYR B CD1 1 
ATOM   5024  C  CD2 . TYR B 1 270 ? 3.721   41.012  58.767  1.00 46.99  ? 271 TYR B CD2 1 
ATOM   5025  C  CE1 . TYR B 1 270 ? 2.095   38.819  58.394  1.00 44.77  ? 271 TYR B CE1 1 
ATOM   5026  C  CE2 . TYR B 1 270 ? 3.060   40.845  57.567  1.00 48.27  ? 271 TYR B CE2 1 
ATOM   5027  C  CZ  . TYR B 1 270 ? 2.248   39.747  57.386  1.00 38.13  ? 271 TYR B CZ  1 
ATOM   5028  O  OH  . TYR B 1 270 ? 1.588   39.579  56.191  1.00 38.73  ? 271 TYR B OH  1 
ATOM   5029  N  N   . CYS B 1 271 ? 6.755   38.506  60.792  1.00 35.36  ? 272 CYS B N   1 
ATOM   5030  C  CA  . CYS B 1 271 ? 7.756   37.710  60.093  1.00 38.58  ? 272 CYS B CA  1 
ATOM   5031  C  C   . CYS B 1 271 ? 7.938   36.338  60.734  1.00 39.60  ? 272 CYS B C   1 
ATOM   5032  O  O   . CYS B 1 271 ? 7.956   35.314  60.045  1.00 33.72  ? 272 CYS B O   1 
ATOM   5033  C  CB  . CYS B 1 271 ? 9.090   38.458  60.070  1.00 35.07  ? 272 CYS B CB  1 
ATOM   5034  S  SG  . CYS B 1 271 ? 10.437  37.581  59.250  1.00 71.30  ? 272 CYS B SG  1 
ATOM   5035  N  N   . ARG B 1 272 ? 8.075   36.332  62.056  1.00 33.82  ? 273 ARG B N   1 
ATOM   5036  C  CA  . ARG B 1 272 ? 8.273   35.103  62.809  1.00 34.25  ? 273 ARG B CA  1 
ATOM   5037  C  C   . ARG B 1 272 ? 7.098   34.151  62.646  1.00 37.96  ? 273 ARG B C   1 
ATOM   5038  O  O   . ARG B 1 272 ? 7.292   32.949  62.497  1.00 34.95  ? 273 ARG B O   1 
ATOM   5039  C  CB  . ARG B 1 272 ? 8.495   35.410  64.290  1.00 41.67  ? 273 ARG B CB  1 
ATOM   5040  C  CG  . ARG B 1 272 ? 9.892   35.907  64.620  1.00 43.37  ? 273 ARG B CG  1 
ATOM   5041  C  CD  . ARG B 1 272 ? 9.940   36.469  66.028  1.00 52.78  ? 273 ARG B CD  1 
ATOM   5042  N  NE  . ARG B 1 272 ? 9.544   35.476  67.022  1.00 56.62  ? 273 ARG B NE  1 
ATOM   5043  C  CZ  . ARG B 1 272 ? 9.349   35.744  68.309  1.00 63.16  ? 273 ARG B CZ  1 
ATOM   5044  N  NH1 . ARG B 1 272 ? 9.508   36.981  68.763  1.00 64.40  ? 273 ARG B NH1 1 
ATOM   5045  N  NH2 . ARG B 1 272 ? 8.991   34.777  69.143  1.00 64.02  ? 273 ARG B NH2 1 
ATOM   5046  N  N   . ASN B 1 273 ? 5.881   34.684  62.676  1.00 33.62  ? 274 ASN B N   1 
ATOM   5047  C  CA  . ASN B 1 273 ? 4.702   33.850  62.481  1.00 33.73  ? 274 ASN B CA  1 
ATOM   5048  C  C   . ASN B 1 273 ? 4.660   33.266  61.075  1.00 33.73  ? 274 ASN B C   1 
ATOM   5049  O  O   . ASN B 1 273 ? 4.395   32.071  60.900  1.00 34.64  ? 274 ASN B O   1 
ATOM   5050  C  CB  . ASN B 1 273 ? 3.424   34.639  62.766  1.00 42.40  ? 274 ASN B CB  1 
ATOM   5051  C  CG  . ASN B 1 273 ? 2.900   34.403  64.169  1.00 45.46  ? 274 ASN B CG  1 
ATOM   5052  O  OD1 . ASN B 1 273 ? 3.335   33.481  64.858  1.00 48.40  ? 274 ASN B OD1 1 
ATOM   5053  N  ND2 . ASN B 1 273 ? 1.956   35.233  64.598  1.00 36.01  ? 274 ASN B ND2 1 
ATOM   5054  N  N   . VAL B 1 274 ? 4.937   34.101  60.076  1.00 34.09  ? 275 VAL B N   1 
ATOM   5055  C  CA  . VAL B 1 274 ? 4.940   33.624  58.695  1.00 38.76  ? 275 VAL B CA  1 
ATOM   5056  C  C   . VAL B 1 274 ? 5.966   32.506  58.490  1.00 40.50  ? 275 VAL B C   1 
ATOM   5057  O  O   . VAL B 1 274 ? 5.649   31.459  57.920  1.00 41.67  ? 275 VAL B O   1 
ATOM   5058  C  CB  . VAL B 1 274 ? 5.226   34.762  57.696  1.00 34.87  ? 275 VAL B CB  1 
ATOM   5059  C  CG1 . VAL B 1 274 ? 5.315   34.213  56.279  1.00 35.18  ? 275 VAL B CG1 1 
ATOM   5060  C  CG2 . VAL B 1 274 ? 4.147   35.825  57.783  1.00 35.60  ? 275 VAL B CG2 1 
ATOM   5061  N  N   . LEU B 1 275 ? 7.187   32.719  58.973  1.00 33.19  ? 276 LEU B N   1 
ATOM   5062  C  CA  . LEU B 1 275 ? 8.251   31.738  58.771  1.00 34.38  ? 276 LEU B CA  1 
ATOM   5063  C  C   . LEU B 1 275 ? 8.060   30.467  59.599  1.00 32.12  ? 276 LEU B C   1 
ATOM   5064  O  O   . LEU B 1 275 ? 8.365   29.372  59.133  1.00 31.88  ? 276 LEU B O   1 
ATOM   5065  C  CB  . LEU B 1 275 ? 9.615   32.359  59.076  1.00 32.45  ? 276 LEU B CB  1 
ATOM   5066  C  CG  . LEU B 1 275 ? 10.102  33.320  57.991  1.00 45.41  ? 276 LEU B CG  1 
ATOM   5067  C  CD1 . LEU B 1 275 ? 11.541  33.736  58.237  1.00 52.47  ? 276 LEU B CD1 1 
ATOM   5068  C  CD2 . LEU B 1 275 ? 9.951   32.689  56.614  1.00 48.47  ? 276 LEU B CD2 1 
ATOM   5069  N  N   . LYS B 1 276 ? 7.555   30.608  60.821  1.00 32.04  ? 277 LYS B N   1 
ATOM   5070  C  CA  . LYS B 1 276 ? 7.252   29.443  61.646  1.00 31.73  ? 277 LYS B CA  1 
ATOM   5071  C  C   . LYS B 1 276 ? 6.064   28.692  61.060  1.00 40.30  ? 277 LYS B C   1 
ATOM   5072  O  O   . LYS B 1 276 ? 5.850   27.517  61.356  1.00 48.82  ? 277 LYS B O   1 
ATOM   5073  C  CB  . LYS B 1 276 ? 6.973   29.850  63.095  1.00 31.77  ? 277 LYS B CB  1 
ATOM   5074  C  CG  . LYS B 1 276 ? 8.218   30.276  63.856  1.00 32.50  ? 277 LYS B CG  1 
ATOM   5075  C  CD  . LYS B 1 276 ? 7.871   30.964  65.165  1.00 31.75  ? 277 LYS B CD  1 
ATOM   5076  C  CE  . LYS B 1 276 ? 7.948   30.002  66.333  1.00 39.27  ? 277 LYS B CE  1 
ATOM   5077  N  NZ  . LYS B 1 276 ? 7.836   30.715  67.637  1.00 31.97  ? 277 LYS B NZ  1 
ATOM   5078  N  N   . GLY B 1 277 ? 5.296   29.381  60.222  1.00 38.18  ? 278 GLY B N   1 
ATOM   5079  C  CA  . GLY B 1 277 ? 4.243   28.736  59.463  1.00 33.19  ? 278 GLY B CA  1 
ATOM   5080  C  C   . GLY B 1 277 ? 4.802   27.966  58.280  1.00 33.72  ? 278 GLY B C   1 
ATOM   5081  O  O   . GLY B 1 277 ? 4.393   26.835  58.015  1.00 33.33  ? 278 GLY B O   1 
ATOM   5082  N  N   . CYS B 1 278 ? 5.751   28.575  57.575  1.00 33.10  ? 279 CYS B N   1 
ATOM   5083  C  CA  . CYS B 1 278 ? 6.305   27.986  56.358  1.00 47.43  ? 279 CYS B CA  1 
ATOM   5084  C  C   . CYS B 1 278 ? 7.332   26.887  56.625  1.00 46.19  ? 279 CYS B C   1 
ATOM   5085  O  O   . CYS B 1 278 ? 7.625   26.079  55.744  1.00 46.84  ? 279 CYS B O   1 
ATOM   5086  C  CB  . CYS B 1 278 ? 6.950   29.074  55.494  1.00 47.96  ? 279 CYS B CB  1 
ATOM   5087  S  SG  . CYS B 1 278 ? 5.787   30.246  54.766  1.00 91.30  ? 279 CYS B SG  1 
ATOM   5088  N  N   . LEU B 1 279 ? 7.879   26.858  57.836  1.00 43.70  ? 280 LEU B N   1 
ATOM   5089  C  CA  . LEU B 1 279 ? 8.986   25.958  58.142  1.00 34.70  ? 280 LEU B CA  1 
ATOM   5090  C  C   . LEU B 1 279 ? 8.677   25.021  59.308  1.00 36.79  ? 280 LEU B C   1 
ATOM   5091  O  O   . LEU B 1 279 ? 9.587   24.514  59.965  1.00 34.18  ? 280 LEU B O   1 
ATOM   5092  C  CB  . LEU B 1 279 ? 10.245  26.773  58.446  1.00 38.55  ? 280 LEU B CB  1 
ATOM   5093  C  CG  . LEU B 1 279 ? 10.678  27.770  57.369  1.00 38.80  ? 280 LEU B CG  1 
ATOM   5094  C  CD1 . LEU B 1 279 ? 11.910  28.545  57.810  1.00 38.51  ? 280 LEU B CD1 1 
ATOM   5095  C  CD2 . LEU B 1 279 ? 10.932  27.060  56.048  1.00 39.89  ? 280 LEU B CD2 1 
ATOM   5096  N  N   . ALA B 1 280 ? 7.392   24.790  59.552  1.00 38.76  ? 281 ALA B N   1 
ATOM   5097  C  CA  . ALA B 1 280 ? 6.946   23.943  60.656  1.00 37.03  ? 281 ALA B CA  1 
ATOM   5098  C  C   . ALA B 1 280 ? 7.437   22.500  60.516  1.00 31.21  ? 281 ALA B C   1 
ATOM   5099  O  O   . ALA B 1 280 ? 7.913   21.887  61.486  1.00 31.51  ? 281 ALA B O   1 
ATOM   5100  C  CB  . ALA B 1 280 ? 5.435   23.977  60.748  1.00 38.85  ? 281 ALA B CB  1 
ATOM   5101  N  N   . ASN B 1 281 ? 7.312   21.965  59.305  1.00 31.57  ? 282 ASN B N   1 
ATOM   5102  C  CA  . ASN B 1 281 ? 7.796   20.624  59.005  1.00 36.29  ? 282 ASN B CA  1 
ATOM   5103  C  C   . ASN B 1 281 ? 9.275   20.492  59.333  1.00 37.70  ? 282 ASN B C   1 
ATOM   5104  O  O   . ASN B 1 281 ? 9.690   19.531  59.981  1.00 49.67  ? 282 ASN B O   1 
ATOM   5105  C  CB  . ASN B 1 281 ? 7.550   20.273  57.536  1.00 32.15  ? 282 ASN B CB  1 
ATOM   5106  C  CG  . ASN B 1 281 ? 6.095   19.963  57.246  1.00 32.99  ? 282 ASN B CG  1 
ATOM   5107  O  OD1 . ASN B 1 281 ? 5.600   18.887  57.580  1.00 40.53  ? 282 ASN B OD1 1 
ATOM   5108  N  ND2 . ASN B 1 281 ? 5.403   20.904  56.613  1.00 43.47  ? 282 ASN B ND2 1 
ATOM   5109  N  N   . GLN B 1 282 ? 10.066  21.463  58.885  1.00 30.63  ? 283 GLN B N   1 
ATOM   5110  C  CA  . GLN B 1 282 ? 11.490  21.496  59.198  1.00 36.81  ? 283 GLN B CA  1 
ATOM   5111  C  C   . GLN B 1 282 ? 11.703  21.593  60.703  1.00 32.80  ? 283 GLN B C   1 
ATOM   5112  O  O   . GLN B 1 282 ? 12.609  20.967  61.256  1.00 38.99  ? 283 GLN B O   1 
ATOM   5113  C  CB  . GLN B 1 282 ? 12.180  22.671  58.498  1.00 30.12  ? 283 GLN B CB  1 
ATOM   5114  C  CG  . GLN B 1 282 ? 12.392  22.497  56.999  1.00 30.60  ? 283 GLN B CG  1 
ATOM   5115  C  CD  . GLN B 1 282 ? 11.121  22.681  56.191  1.00 39.72  ? 283 GLN B CD  1 
ATOM   5116  O  OE1 . GLN B 1 282 ? 10.047  22.922  56.743  1.00 41.34  ? 283 GLN B OE1 1 
ATOM   5117  N  NE2 . GLN B 1 282 ? 11.240  22.575  54.873  1.00 40.25  ? 283 GLN B NE2 1 
ATOM   5118  N  N   . ALA B 1 283 ? 10.854  22.377  61.360  1.00 29.79  ? 284 ALA B N   1 
ATOM   5119  C  CA  . ALA B 1 283 ? 10.956  22.588  62.797  1.00 29.57  ? 284 ALA B CA  1 
ATOM   5120  C  C   . ALA B 1 283 ? 10.671  21.306  63.572  1.00 29.61  ? 284 ALA B C   1 
ATOM   5121  O  O   . ALA B 1 283 ? 11.084  21.170  64.724  1.00 29.44  ? 284 ALA B O   1 
ATOM   5122  C  CB  . ALA B 1 283 ? 10.011  23.695  63.239  1.00 29.88  ? 284 ALA B CB  1 
ATOM   5123  N  N   . ASP B 1 284 ? 9.966   20.367  62.945  1.00 29.94  ? 285 ASP B N   1 
ATOM   5124  C  CA  . ASP B 1 284 ? 9.703   19.079  63.590  1.00 38.85  ? 285 ASP B CA  1 
ATOM   5125  C  C   . ASP B 1 284 ? 10.957  18.206  63.780  1.00 29.72  ? 285 ASP B C   1 
ATOM   5126  O  O   . ASP B 1 284 ? 10.931  17.247  64.548  1.00 29.85  ? 285 ASP B O   1 
ATOM   5127  C  CB  . ASP B 1 284 ? 8.651   18.295  62.802  1.00 42.36  ? 285 ASP B CB  1 
ATOM   5128  C  CG  . ASP B 1 284 ? 7.233   18.684  63.176  1.00 47.94  ? 285 ASP B CG  1 
ATOM   5129  O  OD1 . ASP B 1 284 ? 7.040   19.253  64.272  1.00 45.18  ? 285 ASP B OD1 1 
ATOM   5130  O  OD2 . ASP B 1 284 ? 6.310   18.416  62.379  1.00 47.53  ? 285 ASP B OD2 1 
ATOM   5131  N  N   . LEU B 1 285 ? 12.048  18.538  63.093  1.00 29.34  ? 286 LEU B N   1 
ATOM   5132  C  CA  . LEU B 1 285 ? 13.299  17.777  63.207  1.00 29.01  ? 286 LEU B CA  1 
ATOM   5133  C  C   . LEU B 1 285 ? 14.046  18.026  64.518  1.00 28.71  ? 286 LEU B C   1 
ATOM   5134  O  O   . LEU B 1 285 ? 14.982  17.297  64.859  1.00 29.48  ? 286 LEU B O   1 
ATOM   5135  C  CB  . LEU B 1 285 ? 14.234  18.108  62.039  1.00 28.85  ? 286 LEU B CB  1 
ATOM   5136  C  CG  . LEU B 1 285 ? 13.881  17.605  60.640  1.00 33.05  ? 286 LEU B CG  1 
ATOM   5137  C  CD1 . LEU B 1 285 ? 14.603  18.427  59.590  1.00 32.43  ? 286 LEU B CD1 1 
ATOM   5138  C  CD2 . LEU B 1 285 ? 14.243  16.136  60.503  1.00 38.94  ? 286 LEU B CD2 1 
ATOM   5139  N  N   . ASP B 1 286 ? 13.616  19.056  65.243  1.00 32.07  ? 287 ASP B N   1 
ATOM   5140  C  CA  . ASP B 1 286 ? 14.339  19.589  66.399  1.00 36.94  ? 287 ASP B CA  1 
ATOM   5141  C  C   . ASP B 1 286 ? 14.775  18.544  67.430  1.00 32.39  ? 287 ASP B C   1 
ATOM   5142  O  O   . ASP B 1 286 ? 15.968  18.409  67.721  1.00 33.06  ? 287 ASP B O   1 
ATOM   5143  C  CB  . ASP B 1 286 ? 13.478  20.652  67.087  1.00 28.89  ? 287 ASP B CB  1 
ATOM   5144  C  CG  . ASP B 1 286 ? 14.205  21.353  68.219  1.00 36.60  ? 287 ASP B CG  1 
ATOM   5145  O  OD1 . ASP B 1 286 ? 15.139  22.133  67.935  1.00 31.86  ? 287 ASP B OD1 1 
ATOM   5146  O  OD2 . ASP B 1 286 ? 13.837  21.132  69.392  1.00 34.49  ? 287 ASP B OD2 1 
ATOM   5147  N  N   . ALA B 1 287 ? 13.808  17.810  67.974  1.00 30.61  ? 288 ALA B N   1 
ATOM   5148  C  CA  . ALA B 1 287 ? 14.060  16.873  69.069  1.00 29.30  ? 288 ALA B CA  1 
ATOM   5149  C  C   . ALA B 1 287 ? 15.105  15.812  68.728  1.00 39.00  ? 288 ALA B C   1 
ATOM   5150  O  O   . ALA B 1 287 ? 16.071  15.614  69.472  1.00 40.69  ? 288 ALA B O   1 
ATOM   5151  C  CB  . ALA B 1 287 ? 12.760  16.204  69.487  1.00 29.93  ? 288 ALA B CB  1 
ATOM   5152  N  N   . GLU B 1 288 ? 14.913  15.132  67.603  1.00 32.54  ? 289 GLU B N   1 
ATOM   5153  C  CA  . GLU B 1 288 ? 15.806  14.046  67.222  1.00 28.93  ? 289 GLU B CA  1 
ATOM   5154  C  C   . GLU B 1 288 ? 17.143  14.566  66.712  1.00 28.45  ? 289 GLU B C   1 
ATOM   5155  O  O   . GLU B 1 288 ? 18.170  13.903  66.865  1.00 28.35  ? 289 GLU B O   1 
ATOM   5156  C  CB  . GLU B 1 288 ? 15.146  13.150  66.174  1.00 29.59  ? 289 GLU B CB  1 
ATOM   5157  C  CG  . GLU B 1 288 ? 13.969  12.351  66.718  1.00 33.32  ? 289 GLU B CG  1 
ATOM   5158  C  CD  . GLU B 1 288 ? 14.260  11.709  68.068  1.00 39.02  ? 289 GLU B CD  1 
ATOM   5159  O  OE1 . GLU B 1 288 ? 15.378  11.183  68.262  1.00 46.42  ? 289 GLU B OE1 1 
ATOM   5160  O  OE2 . GLU B 1 288 ? 13.365  11.731  68.940  1.00 46.03  ? 289 GLU B OE2 1 
ATOM   5161  N  N   . TRP B 1 289 ? 17.126  15.748  66.104  1.00 28.24  ? 290 TRP B N   1 
ATOM   5162  C  CA  . TRP B 1 289 ? 18.367  16.428  65.749  1.00 29.21  ? 290 TRP B CA  1 
ATOM   5163  C  C   . TRP B 1 289 ? 19.210  16.615  67.008  1.00 27.90  ? 290 TRP B C   1 
ATOM   5164  O  O   . TRP B 1 289 ? 20.401  16.272  67.045  1.00 27.80  ? 290 TRP B O   1 
ATOM   5165  C  CB  . TRP B 1 289 ? 18.067  17.772  65.083  1.00 27.89  ? 290 TRP B CB  1 
ATOM   5166  C  CG  . TRP B 1 289 ? 19.269  18.595  64.760  1.00 27.75  ? 290 TRP B CG  1 
ATOM   5167  C  CD1 . TRP B 1 289 ? 19.760  19.644  65.481  1.00 27.76  ? 290 TRP B CD1 1 
ATOM   5168  C  CD2 . TRP B 1 289 ? 20.130  18.451  63.623  1.00 32.69  ? 290 TRP B CD2 1 
ATOM   5169  N  NE1 . TRP B 1 289 ? 20.875  20.160  64.866  1.00 29.80  ? 290 TRP B NE1 1 
ATOM   5170  C  CE2 . TRP B 1 289 ? 21.123  19.445  63.724  1.00 29.70  ? 290 TRP B CE2 1 
ATOM   5171  C  CE3 . TRP B 1 289 ? 20.158  17.577  62.532  1.00 33.32  ? 290 TRP B CE3 1 
ATOM   5172  C  CZ2 . TRP B 1 289 ? 22.133  19.589  62.776  1.00 35.31  ? 290 TRP B CZ2 1 
ATOM   5173  C  CZ3 . TRP B 1 289 ? 21.162  17.722  61.592  1.00 33.75  ? 290 TRP B CZ3 1 
ATOM   5174  C  CH2 . TRP B 1 289 ? 22.136  18.720  61.719  1.00 32.95  ? 290 TRP B CH2 1 
ATOM   5175  N  N   . ARG B 1 290 ? 18.566  17.134  68.049  1.00 28.09  ? 291 ARG B N   1 
ATOM   5176  C  CA  . ARG B 1 290 ? 19.227  17.370  69.325  1.00 28.24  ? 291 ARG B CA  1 
ATOM   5177  C  C   . ARG B 1 290 ? 19.711  16.075  69.965  1.00 30.54  ? 291 ARG B C   1 
ATOM   5178  O  O   . ARG B 1 290 ? 20.814  16.028  70.505  1.00 30.66  ? 291 ARG B O   1 
ATOM   5179  C  CB  . ARG B 1 290 ? 18.290  18.108  70.280  1.00 28.58  ? 291 ARG B CB  1 
ATOM   5180  C  CG  . ARG B 1 290 ? 18.171  19.586  69.975  1.00 37.79  ? 291 ARG B CG  1 
ATOM   5181  C  CD  . ARG B 1 290 ? 16.989  20.212  70.687  1.00 45.24  ? 291 ARG B CD  1 
ATOM   5182  N  NE  . ARG B 1 290 ? 16.697  21.538  70.155  1.00 47.48  ? 291 ARG B NE  1 
ATOM   5183  C  CZ  . ARG B 1 290 ? 17.201  22.664  70.648  1.00 49.83  ? 291 ARG B CZ  1 
ATOM   5184  N  NH1 . ARG B 1 290 ? 18.021  22.626  71.689  1.00 51.05  ? 291 ARG B NH1 1 
ATOM   5185  N  NH2 . ARG B 1 290 ? 16.886  23.829  70.100  1.00 51.50  ? 291 ARG B NH2 1 
ATOM   5186  N  N   . ASN B 1 291 ? 18.889  15.031  69.909  1.00 35.92  ? 292 ASN B N   1 
ATOM   5187  C  CA  . ASN B 1 291 ? 19.297  13.730  70.432  1.00 30.87  ? 292 ASN B CA  1 
ATOM   5188  C  C   . ASN B 1 291 ? 20.552  13.218  69.732  1.00 28.55  ? 292 ASN B C   1 
ATOM   5189  O  O   . ASN B 1 291 ? 21.493  12.752  70.383  1.00 28.67  ? 292 ASN B O   1 
ATOM   5190  C  CB  . ASN B 1 291 ? 18.165  12.711  70.294  1.00 40.80  ? 292 ASN B CB  1 
ATOM   5191  C  CG  . ASN B 1 291 ? 17.026  12.974  71.257  1.00 41.35  ? 292 ASN B CG  1 
ATOM   5192  O  OD1 . ASN B 1 291 ? 17.237  13.479  72.361  1.00 33.93  ? 292 ASN B OD1 1 
ATOM   5193  N  ND2 . ASN B 1 291 ? 15.809  12.627  70.848  1.00 30.02  ? 292 ASN B ND2 1 
ATOM   5194  N  N   . LEU B 1 292 ? 20.564  13.322  68.406  1.00 28.26  ? 293 LEU B N   1 
ATOM   5195  C  CA  . LEU B 1 292 ? 21.711  12.888  67.621  1.00 28.09  ? 293 LEU B CA  1 
ATOM   5196  C  C   . LEU B 1 292 ? 22.969  13.671  67.977  1.00 36.35  ? 293 LEU B C   1 
ATOM   5197  O  O   . LEU B 1 292 ? 24.008  13.078  68.269  1.00 37.10  ? 293 LEU B O   1 
ATOM   5198  C  CB  . LEU B 1 292 ? 21.435  13.025  66.124  1.00 27.97  ? 293 LEU B CB  1 
ATOM   5199  C  CG  . LEU B 1 292 ? 22.622  12.578  65.266  1.00 27.93  ? 293 LEU B CG  1 
ATOM   5200  C  CD1 . LEU B 1 292 ? 22.882  11.093  65.462  1.00 30.24  ? 293 LEU B CD1 1 
ATOM   5201  C  CD2 . LEU B 1 292 ? 22.413  12.903  63.797  1.00 27.96  ? 293 LEU B CD2 1 
ATOM   5202  N  N   . LEU B 1 293 ? 22.880  14.999  67.954  1.00 27.85  ? 294 LEU B N   1 
ATOM   5203  C  CA  . LEU B 1 293 ? 24.055  15.819  68.238  1.00 36.32  ? 294 LEU B CA  1 
ATOM   5204  C  C   . LEU B 1 293 ? 24.560  15.606  69.666  1.00 36.71  ? 294 LEU B C   1 
ATOM   5205  O  O   . LEU B 1 293 ? 25.767  15.622  69.912  1.00 28.29  ? 294 LEU B O   1 
ATOM   5206  C  CB  . LEU B 1 293 ? 23.753  17.299  67.993  1.00 27.84  ? 294 LEU B CB  1 
ATOM   5207  C  CG  . LEU B 1 293 ? 24.306  17.850  66.676  1.00 33.01  ? 294 LEU B CG  1 
ATOM   5208  C  CD1 . LEU B 1 293 ? 23.845  17.007  65.496  1.00 34.46  ? 294 LEU B CD1 1 
ATOM   5209  C  CD2 . LEU B 1 293 ? 23.901  19.299  66.484  1.00 32.60  ? 294 LEU B CD2 1 
ATOM   5210  N  N   . ASP B 1 294 ? 23.639  15.388  70.600  1.00 31.79  ? 295 ASP B N   1 
ATOM   5211  C  CA  . ASP B 1 294 ? 24.019  15.152  71.989  1.00 40.04  ? 295 ASP B CA  1 
ATOM   5212  C  C   . ASP B 1 294 ? 24.701  13.796  72.164  1.00 41.83  ? 295 ASP B C   1 
ATOM   5213  O  O   . ASP B 1 294 ? 25.670  13.677  72.914  1.00 41.35  ? 295 ASP B O   1 
ATOM   5214  C  CB  . ASP B 1 294 ? 22.798  15.251  72.907  1.00 48.03  ? 295 ASP B CB  1 
ATOM   5215  C  CG  . ASP B 1 294 ? 22.748  16.564  73.670  1.00 66.13  ? 295 ASP B CG  1 
ATOM   5216  O  OD1 . ASP B 1 294 ? 23.432  17.524  73.254  1.00 68.63  ? 295 ASP B OD1 1 
ATOM   5217  O  OD2 . ASP B 1 294 ? 22.022  16.637  74.684  1.00 68.74  ? 295 ASP B OD2 1 
ATOM   5218  N  N   . SER B 1 295 ? 24.201  12.775  71.471  1.00 34.50  ? 296 SER B N   1 
ATOM   5219  C  CA  . SER B 1 295 ? 24.819  11.453  71.540  1.00 41.34  ? 296 SER B CA  1 
ATOM   5220  C  C   . SER B 1 295 ? 26.202  11.474  70.887  1.00 28.83  ? 296 SER B C   1 
ATOM   5221  O  O   . SER B 1 295 ? 27.139  10.829  71.365  1.00 29.10  ? 296 SER B O   1 
ATOM   5222  C  CB  . SER B 1 295 ? 23.926  10.401  70.878  1.00 36.96  ? 296 SER B CB  1 
ATOM   5223  O  OG  . SER B 1 295 ? 23.756  10.664  69.497  1.00 43.33  ? 296 SER B OG  1 
ATOM   5224  N  N   . MET B 1 296 ? 26.318  12.229  69.799  1.00 35.20  ? 297 MET B N   1 
ATOM   5225  C  CA  . MET B 1 296 ? 27.590  12.417  69.107  1.00 32.03  ? 297 MET B CA  1 
ATOM   5226  C  C   . MET B 1 296 ? 28.612  13.120  69.991  1.00 35.12  ? 297 MET B C   1 
ATOM   5227  O  O   . MET B 1 296 ? 29.774  12.721  70.047  1.00 28.91  ? 297 MET B O   1 
ATOM   5228  C  CB  . MET B 1 296 ? 27.387  13.217  67.821  1.00 33.30  ? 297 MET B CB  1 
ATOM   5229  C  CG  . MET B 1 296 ? 26.729  12.436  66.704  1.00 28.04  ? 297 MET B CG  1 
ATOM   5230  S  SD  . MET B 1 296 ? 26.451  13.467  65.259  1.00 55.99  ? 297 MET B SD  1 
ATOM   5231  C  CE  . MET B 1 296 ? 28.133  13.946  64.900  1.00 57.71  ? 297 MET B CE  1 
ATOM   5232  N  N   . VAL B 1 297 ? 28.177  14.179  70.667  1.00 35.81  ? 298 VAL B N   1 
ATOM   5233  C  CA  . VAL B 1 297 ? 29.032  14.869  71.623  1.00 33.41  ? 298 VAL B CA  1 
ATOM   5234  C  C   . VAL B 1 297 ? 29.436  13.904  72.732  1.00 41.13  ? 298 VAL B C   1 
ATOM   5235  O  O   . VAL B 1 297 ? 30.578  13.907  73.198  1.00 33.31  ? 298 VAL B O   1 
ATOM   5236  C  CB  . VAL B 1 297 ? 28.329  16.107  72.224  1.00 33.00  ? 298 VAL B CB  1 
ATOM   5237  C  CG1 . VAL B 1 297 ? 29.040  16.582  73.484  1.00 29.97  ? 298 VAL B CG1 1 
ATOM   5238  C  CG2 . VAL B 1 297 ? 28.256  17.223  71.195  1.00 29.07  ? 298 VAL B CG2 1 
ATOM   5239  N  N   . LEU B 1 298 ? 28.496  13.052  73.124  1.00 29.64  ? 299 LEU B N   1 
ATOM   5240  C  CA  . LEU B 1 298 ? 28.718  12.118  74.219  1.00 34.50  ? 299 LEU B CA  1 
ATOM   5241  C  C   . LEU B 1 298 ? 29.731  11.020  73.894  1.00 36.46  ? 299 LEU B C   1 
ATOM   5242  O  O   . LEU B 1 298 ? 30.499  10.610  74.764  1.00 35.92  ? 299 LEU B O   1 
ATOM   5243  C  CB  . LEU B 1 298 ? 27.391  11.486  74.642  1.00 33.81  ? 299 LEU B CB  1 
ATOM   5244  C  CG  . LEU B 1 298 ? 26.953  11.917  76.039  1.00 46.05  ? 299 LEU B CG  1 
ATOM   5245  C  CD1 . LEU B 1 298 ? 25.564  11.405  76.371  1.00 48.61  ? 299 LEU B CD1 1 
ATOM   5246  C  CD2 . LEU B 1 298 ? 27.969  11.423  77.045  1.00 51.23  ? 299 LEU B CD2 1 
ATOM   5247  N  N   . ILE B 1 299 ? 29.738  10.543  72.652  1.00 29.83  ? 300 ILE B N   1 
ATOM   5248  C  CA  . ILE B 1 299 ? 30.639  9.452   72.284  1.00 29.97  ? 300 ILE B CA  1 
ATOM   5249  C  C   . ILE B 1 299 ? 32.109  9.896   72.275  1.00 42.32  ? 300 ILE B C   1 
ATOM   5250  O  O   . ILE B 1 299 ? 33.013  9.062   72.344  1.00 38.00  ? 300 ILE B O   1 
ATOM   5251  C  CB  . ILE B 1 299 ? 30.272  8.848   70.905  1.00 29.59  ? 300 ILE B CB  1 
ATOM   5252  C  CG1 . ILE B 1 299 ? 30.871  7.448   70.747  1.00 42.80  ? 300 ILE B CG1 1 
ATOM   5253  C  CG2 . ILE B 1 299 ? 30.727  9.746   69.774  1.00 29.26  ? 300 ILE B CG2 1 
ATOM   5254  C  CD1 . ILE B 1 299 ? 30.342  6.434   71.734  1.00 37.31  ? 300 ILE B CD1 1 
ATOM   5255  N  N   . THR B 1 300 ? 32.351  11.205  72.218  1.00 30.13  ? 301 THR B N   1 
ATOM   5256  C  CA  . THR B 1 300 ? 33.721  11.716  72.223  1.00 30.49  ? 301 THR B CA  1 
ATOM   5257  C  C   . THR B 1 300 ? 34.403  11.498  73.572  1.00 31.20  ? 301 THR B C   1 
ATOM   5258  O  O   . THR B 1 300 ? 35.619  11.643  73.687  1.00 31.66  ? 301 THR B O   1 
ATOM   5259  C  CB  . THR B 1 300 ? 33.783  13.224  71.878  1.00 36.76  ? 301 THR B CB  1 
ATOM   5260  O  OG1 . THR B 1 300 ? 33.253  13.995  72.963  1.00 30.67  ? 301 THR B OG1 1 
ATOM   5261  C  CG2 . THR B 1 300 ? 33.012  13.524  70.602  1.00 29.84  ? 301 THR B CG2 1 
ATOM   5262  N  N   . ASP B 1 301 ? 33.618  11.160  74.592  1.00 37.51  ? 302 ASP B N   1 
ATOM   5263  C  CA  . ASP B 1 301 ? 34.176  10.789  75.890  1.00 41.36  ? 302 ASP B CA  1 
ATOM   5264  C  C   . ASP B 1 301 ? 35.047  9.544   75.769  1.00 38.05  ? 302 ASP B C   1 
ATOM   5265  O  O   . ASP B 1 301 ? 36.070  9.419   76.444  1.00 33.16  ? 302 ASP B O   1 
ATOM   5266  C  CB  . ASP B 1 301 ? 33.068  10.541  76.914  1.00 43.74  ? 302 ASP B CB  1 
ATOM   5267  C  CG  . ASP B 1 301 ? 32.414  11.819  77.392  1.00 43.56  ? 302 ASP B CG  1 
ATOM   5268  O  OD1 . ASP B 1 301 ? 33.000  12.903  77.187  1.00 49.66  ? 302 ASP B OD1 1 
ATOM   5269  O  OD2 . ASP B 1 301 ? 31.316  11.736  77.984  1.00 36.02  ? 302 ASP B OD2 1 
ATOM   5270  N  N   . LYS B 1 302 ? 34.637  8.626   74.901  1.00 32.00  ? 303 LYS B N   1 
ATOM   5271  C  CA  . LYS B 1 302 ? 35.344  7.362   74.734  1.00 34.00  ? 303 LYS B CA  1 
ATOM   5272  C  C   . LYS B 1 302 ? 36.590  7.524   73.869  1.00 36.46  ? 303 LYS B C   1 
ATOM   5273  O  O   . LYS B 1 302 ? 37.279  6.548   73.575  1.00 32.51  ? 303 LYS B O   1 
ATOM   5274  C  CB  . LYS B 1 302 ? 34.416  6.307   74.127  1.00 31.94  ? 303 LYS B CB  1 
ATOM   5275  C  CG  . LYS B 1 302 ? 33.102  6.134   74.874  1.00 32.02  ? 303 LYS B CG  1 
ATOM   5276  C  CD  . LYS B 1 302 ? 33.333  5.938   76.363  1.00 48.40  ? 303 LYS B CD  1 
ATOM   5277  C  CE  . LYS B 1 302 ? 32.019  5.797   77.113  1.00 52.67  ? 303 LYS B CE  1 
ATOM   5278  N  NZ  . LYS B 1 302 ? 32.212  5.838   78.589  1.00 54.33  ? 303 LYS B NZ  1 
ATOM   5279  N  N   . PHE B 1 303 ? 36.872  8.757   73.459  1.00 32.10  ? 304 PHE B N   1 
ATOM   5280  C  CA  . PHE B 1 303 ? 38.087  9.049   72.705  1.00 32.28  ? 304 PHE B CA  1 
ATOM   5281  C  C   . PHE B 1 303 ? 39.282  9.131   73.648  1.00 33.14  ? 304 PHE B C   1 
ATOM   5282  O  O   . PHE B 1 303 ? 40.427  8.972   73.229  1.00 33.53  ? 304 PHE B O   1 
ATOM   5283  C  CB  . PHE B 1 303 ? 37.959  10.364  71.923  1.00 31.96  ? 304 PHE B CB  1 
ATOM   5284  C  CG  . PHE B 1 303 ? 36.971  10.317  70.785  1.00 42.02  ? 304 PHE B CG  1 
ATOM   5285  C  CD1 . PHE B 1 303 ? 36.290  9.152   70.471  1.00 30.95  ? 304 PHE B CD1 1 
ATOM   5286  C  CD2 . PHE B 1 303 ? 36.732  11.451  70.024  1.00 41.51  ? 304 PHE B CD2 1 
ATOM   5287  C  CE1 . PHE B 1 303 ? 35.386  9.119   69.424  1.00 39.05  ? 304 PHE B CE1 1 
ATOM   5288  C  CE2 . PHE B 1 303 ? 35.829  11.426  68.977  1.00 30.43  ? 304 PHE B CE2 1 
ATOM   5289  C  CZ  . PHE B 1 303 ? 35.157  10.259  68.676  1.00 41.76  ? 304 PHE B CZ  1 
ATOM   5290  N  N   . TRP B 1 304 ? 39.006  9.384   74.924  1.00 35.40  ? 305 TRP B N   1 
ATOM   5291  C  CA  . TRP B 1 304 ? 40.060  9.634   75.902  1.00 39.21  ? 305 TRP B CA  1 
ATOM   5292  C  C   . TRP B 1 304 ? 40.268  8.462   76.852  1.00 43.67  ? 305 TRP B C   1 
ATOM   5293  O  O   . TRP B 1 304 ? 39.398  7.605   77.000  1.00 42.17  ? 305 TRP B O   1 
ATOM   5294  C  CB  . TRP B 1 304 ? 39.744  10.890  76.719  1.00 39.29  ? 305 TRP B CB  1 
ATOM   5295  C  CG  . TRP B 1 304 ? 39.092  11.981  75.932  1.00 42.36  ? 305 TRP B CG  1 
ATOM   5296  C  CD1 . TRP B 1 304 ? 37.793  12.392  76.021  1.00 41.32  ? 305 TRP B CD1 1 
ATOM   5297  C  CD2 . TRP B 1 304 ? 39.704  12.800  74.931  1.00 43.91  ? 305 TRP B CD2 1 
ATOM   5298  N  NE1 . TRP B 1 304 ? 37.560  13.419  75.140  1.00 40.54  ? 305 TRP B NE1 1 
ATOM   5299  C  CE2 . TRP B 1 304 ? 38.718  13.688  74.458  1.00 45.92  ? 305 TRP B CE2 1 
ATOM   5300  C  CE3 . TRP B 1 304 ? 40.991  12.871  74.389  1.00 49.49  ? 305 TRP B CE3 1 
ATOM   5301  C  CZ2 . TRP B 1 304 ? 38.978  14.635  73.470  1.00 48.67  ? 305 TRP B CZ2 1 
ATOM   5302  C  CZ3 . TRP B 1 304 ? 41.247  13.810  73.408  1.00 53.49  ? 305 TRP B CZ3 1 
ATOM   5303  C  CH2 . TRP B 1 304 ? 40.246  14.680  72.959  1.00 51.97  ? 305 TRP B CH2 1 
ATOM   5304  N  N   . GLY B 1 305 ? 41.425  8.443   77.504  1.00 45.06  ? 306 GLY B N   1 
ATOM   5305  C  CA  . GLY B 1 305 ? 41.717  7.445   78.515  1.00 49.19  ? 306 GLY B CA  1 
ATOM   5306  C  C   . GLY B 1 305 ? 42.534  6.276   78.003  1.00 51.66  ? 306 GLY B C   1 
ATOM   5307  O  O   . GLY B 1 305 ? 42.880  6.214   76.823  1.00 51.57  ? 306 GLY B O   1 
ATOM   5308  N  N   . THR B 1 306 ? 42.843  5.349   78.906  1.00 56.73  ? 307 THR B N   1 
ATOM   5309  C  CA  . THR B 1 306 ? 43.633  4.167   78.575  1.00 62.17  ? 307 THR B CA  1 
ATOM   5310  C  C   . THR B 1 306 ? 42.934  3.302   77.532  1.00 63.33  ? 307 THR B C   1 
ATOM   5311  O  O   . THR B 1 306 ? 43.566  2.788   76.609  1.00 63.72  ? 307 THR B O   1 
ATOM   5312  C  CB  . THR B 1 306 ? 43.916  3.313   79.827  1.00 58.16  ? 307 THR B CB  1 
ATOM   5313  O  OG1 . THR B 1 306 ? 42.678  2.853   80.385  1.00 61.09  ? 307 THR B OG1 1 
ATOM   5314  C  CG2 . THR B 1 306 ? 44.667  4.128   80.871  1.00 54.63  ? 307 THR B CG2 1 
ATOM   5315  N  N   . SER B 1 307 ? 41.623  3.152   77.687  1.00 62.65  ? 308 SER B N   1 
ATOM   5316  C  CA  . SER B 1 307 ? 40.819  2.371   76.755  1.00 59.08  ? 308 SER B CA  1 
ATOM   5317  C  C   . SER B 1 307 ? 40.243  3.263   75.659  1.00 55.88  ? 308 SER B C   1 
ATOM   5318  O  O   . SER B 1 307 ? 39.472  2.806   74.813  1.00 46.66  ? 308 SER B O   1 
ATOM   5319  C  CB  . SER B 1 307 ? 39.695  1.644   77.495  1.00 64.45  ? 308 SER B CB  1 
ATOM   5320  O  OG  . SER B 1 307 ? 40.215  0.803   78.511  1.00 71.18  ? 308 SER B OG  1 
ATOM   5321  N  N   . GLY B 1 308 ? 40.619  4.540   75.691  1.00 47.70  ? 309 GLY B N   1 
ATOM   5322  C  CA  . GLY B 1 308 ? 40.146  5.513   74.723  1.00 34.24  ? 309 GLY B CA  1 
ATOM   5323  C  C   . GLY B 1 308 ? 40.550  5.205   73.295  1.00 33.89  ? 309 GLY B C   1 
ATOM   5324  O  O   . GLY B 1 308 ? 41.492  4.453   73.054  1.00 34.34  ? 309 GLY B O   1 
ATOM   5325  N  N   . VAL B 1 309 ? 39.837  5.808   72.348  1.00 34.18  ? 310 VAL B N   1 
ATOM   5326  C  CA  . VAL B 1 309 ? 39.995  5.503   70.927  1.00 37.84  ? 310 VAL B CA  1 
ATOM   5327  C  C   . VAL B 1 309 ? 41.410  5.726   70.393  1.00 37.60  ? 310 VAL B C   1 
ATOM   5328  O  O   . VAL B 1 309 ? 42.022  4.805   69.841  1.00 47.06  ? 310 VAL B O   1 
ATOM   5329  C  CB  . VAL B 1 309 ? 39.014  6.339   70.078  1.00 39.71  ? 310 VAL B CB  1 
ATOM   5330  C  CG1 . VAL B 1 309 ? 39.334  6.202   68.599  1.00 37.99  ? 310 VAL B CG1 1 
ATOM   5331  C  CG2 . VAL B 1 309 ? 37.584  5.914   70.358  1.00 40.18  ? 310 VAL B CG2 1 
ATOM   5332  N  N   . GLU B 1 310 ? 41.924  6.942   70.555  1.00 40.81  ? 311 GLU B N   1 
ATOM   5333  C  CA  . GLU B 1 310 ? 43.219  7.293   69.983  1.00 50.42  ? 311 GLU B CA  1 
ATOM   5334  C  C   . GLU B 1 310 ? 44.335  6.394   70.498  1.00 48.09  ? 311 GLU B C   1 
ATOM   5335  O  O   . GLU B 1 310 ? 45.163  5.909   69.719  1.00 59.25  ? 311 GLU B O   1 
ATOM   5336  C  CB  . GLU B 1 310 ? 43.560  8.757   70.261  1.00 55.65  ? 311 GLU B CB  1 
ATOM   5337  C  CG  . GLU B 1 310 ? 43.517  9.620   69.013  1.00 63.88  ? 311 GLU B CG  1 
ATOM   5338  C  CD  . GLU B 1 310 ? 44.443  10.813  69.090  1.00 67.53  ? 311 GLU B CD  1 
ATOM   5339  O  OE1 . GLU B 1 310 ? 45.023  11.051  70.170  1.00 69.96  ? 311 GLU B OE1 1 
ATOM   5340  O  OE2 . GLU B 1 310 ? 44.598  11.509  68.064  1.00 70.06  ? 311 GLU B OE2 1 
ATOM   5341  N  N   . SER B 1 311 ? 44.342  6.172   71.808  1.00 45.57  ? 312 SER B N   1 
ATOM   5342  C  CA  . SER B 1 311 ? 45.287  5.258   72.436  1.00 48.07  ? 312 SER B CA  1 
ATOM   5343  C  C   . SER B 1 311 ? 45.272  3.889   71.759  1.00 48.42  ? 312 SER B C   1 
ATOM   5344  O  O   . SER B 1 311 ? 46.280  3.449   71.217  1.00 49.53  ? 312 SER B O   1 
ATOM   5345  C  CB  . SER B 1 311 ? 44.973  5.109   73.926  1.00 49.95  ? 312 SER B CB  1 
ATOM   5346  O  OG  . SER B 1 311 ? 45.624  3.977   74.475  1.00 61.49  ? 312 SER B OG  1 
ATOM   5347  N  N   . VAL B 1 312 ? 44.112  3.240   71.773  1.00 45.99  ? 313 VAL B N   1 
ATOM   5348  C  CA  . VAL B 1 312 ? 43.958  1.881   71.254  1.00 42.00  ? 313 VAL B CA  1 
ATOM   5349  C  C   . VAL B 1 312 ? 44.292  1.757   69.764  1.00 44.26  ? 313 VAL B C   1 
ATOM   5350  O  O   . VAL B 1 312 ? 45.232  1.031   69.374  1.00 45.71  ? 313 VAL B O   1 
ATOM   5351  C  CB  . VAL B 1 312 ? 42.517  1.376   71.481  1.00 34.95  ? 313 VAL B CB  1 
ATOM   5352  C  CG1 . VAL B 1 312 ? 42.297  0.037   70.791  1.00 45.08  ? 313 VAL B CG1 1 
ATOM   5353  C  CG2 . VAL B 1 312 ? 42.213  1.285   72.969  1.00 35.27  ? 313 VAL B CG2 1 
ATOM   5354  N  N   . ILE B 1 313 ? 43.514  2.465   68.945  1.00 40.75  ? 314 ILE B N   1 
ATOM   5355  C  CA  . ILE B 1 313 ? 43.662  2.424   67.492  1.00 41.19  ? 314 ILE B CA  1 
ATOM   5356  C  C   . ILE B 1 313 ? 45.082  2.799   67.096  1.00 44.01  ? 314 ILE B C   1 
ATOM   5357  O  O   . ILE B 1 313 ? 45.646  2.236   66.156  1.00 43.33  ? 314 ILE B O   1 
ATOM   5358  C  CB  . ILE B 1 313 ? 42.660  3.370   66.787  1.00 39.39  ? 314 ILE B CB  1 
ATOM   5359  C  CG1 . ILE B 1 313 ? 41.220  2.930   67.062  1.00 37.00  ? 314 ILE B CG1 1 
ATOM   5360  C  CG2 . ILE B 1 313 ? 42.911  3.405   65.285  1.00 34.14  ? 314 ILE B CG2 1 
ATOM   5361  C  CD1 . ILE B 1 313 ? 40.192  3.614   66.183  1.00 32.77  ? 314 ILE B CD1 1 
ATOM   5362  N  N   . GLY B 1 314 ? 45.666  3.737   67.836  1.00 48.93  ? 315 GLY B N   1 
ATOM   5363  C  CA  . GLY B 1 314 ? 47.034  4.143   67.592  1.00 36.47  ? 315 GLY B CA  1 
ATOM   5364  C  C   . GLY B 1 314 ? 48.076  3.170   68.118  1.00 43.34  ? 315 GLY B C   1 
ATOM   5365  O  O   . GLY B 1 314 ? 49.245  3.261   67.742  1.00 42.04  ? 315 GLY B O   1 
ATOM   5366  N  N   . SER B 1 315 ? 47.672  2.234   68.978  1.00 49.15  ? 316 SER B N   1 
ATOM   5367  C  CA  . SER B 1 315 ? 48.650  1.361   69.632  1.00 46.61  ? 316 SER B CA  1 
ATOM   5368  C  C   . SER B 1 315 ? 48.355  -0.143  69.578  1.00 42.78  ? 316 SER B C   1 
ATOM   5369  O  O   . SER B 1 315 ? 48.830  -0.888  70.432  1.00 50.08  ? 316 SER B O   1 
ATOM   5370  C  CB  . SER B 1 315 ? 48.818  1.773   71.096  1.00 44.19  ? 316 SER B CB  1 
ATOM   5371  O  OG  . SER B 1 315 ? 49.164  3.144   71.204  1.00 43.00  ? 316 SER B OG  1 
ATOM   5372  N  N   . VAL B 1 316 ? 47.587  -0.583  68.584  1.00 37.66  ? 317 VAL B N   1 
ATOM   5373  C  CA  . VAL B 1 316 ? 47.460  -2.020  68.260  1.00 44.93  ? 317 VAL B CA  1 
ATOM   5374  C  C   . VAL B 1 316 ? 48.786  -2.828  68.288  1.00 38.99  ? 317 VAL B C   1 
ATOM   5375  O  O   . VAL B 1 316 ? 48.867  -3.954  68.847  1.00 44.68  ? 317 VAL B O   1 
ATOM   5376  C  CB  . VAL B 1 316 ? 46.838  -2.195  66.854  1.00 41.71  ? 317 VAL B CB  1 
ATOM   5377  C  CG1 . VAL B 1 316 ? 46.603  -3.666  66.544  1.00 43.92  ? 317 VAL B CG1 1 
ATOM   5378  C  CG2 . VAL B 1 316 ? 45.542  -1.403  66.738  1.00 36.62  ? 317 VAL B CG2 1 
ATOM   5379  N  N   . HIS B 1 317 ? 49.824  -2.252  67.680  1.00 39.47  ? 318 HIS B N   1 
ATOM   5380  C  CA  . HIS B 1 317 ? 51.106  -2.938  67.529  1.00 40.54  ? 318 HIS B CA  1 
ATOM   5381  C  C   . HIS B 1 317 ? 51.737  -3.258  68.880  1.00 47.45  ? 318 HIS B C   1 
ATOM   5382  O  O   . HIS B 1 317 ? 52.542  -4.183  68.996  1.00 60.09  ? 318 HIS B O   1 
ATOM   5383  C  CB  . HIS B 1 317 ? 52.078  -2.113  66.665  1.00 41.05  ? 318 HIS B CB  1 
ATOM   5384  C  CG  . HIS B 1 317 ? 52.401  -0.755  67.214  1.00 53.79  ? 318 HIS B CG  1 
ATOM   5385  N  ND1 . HIS B 1 317 ? 52.985  -0.564  68.448  1.00 55.65  ? 318 HIS B ND1 1 
ATOM   5386  C  CD2 . HIS B 1 317 ? 52.259  0.480   66.674  1.00 50.02  ? 318 HIS B CD2 1 
ATOM   5387  C  CE1 . HIS B 1 317 ? 53.164  0.728   68.655  1.00 53.90  ? 318 HIS B CE1 1 
ATOM   5388  N  NE2 . HIS B 1 317 ? 52.730  1.384   67.594  1.00 55.05  ? 318 HIS B NE2 1 
ATOM   5389  N  N   . THR B 1 318 ? 51.360  -2.493  69.899  1.00 45.75  ? 319 THR B N   1 
ATOM   5390  C  CA  . THR B 1 318 ? 51.849  -2.726  71.249  1.00 48.14  ? 319 THR B CA  1 
ATOM   5391  C  C   . THR B 1 318 ? 51.314  -4.049  71.775  1.00 45.90  ? 319 THR B C   1 
ATOM   5392  O  O   . THR B 1 318 ? 52.053  -4.842  72.358  1.00 48.89  ? 319 THR B O   1 
ATOM   5393  C  CB  . THR B 1 318 ? 51.443  -1.592  72.202  1.00 51.30  ? 319 THR B CB  1 
ATOM   5394  O  OG1 . THR B 1 318 ? 50.014  -1.494  72.250  1.00 54.18  ? 319 THR B OG1 1 
ATOM   5395  C  CG2 . THR B 1 318 ? 52.010  -0.276  71.712  1.00 52.02  ? 319 THR B CG2 1 
ATOM   5396  N  N   . TRP B 1 319 ? 50.023  -4.285  71.559  1.00 47.87  ? 320 TRP B N   1 
ATOM   5397  C  CA  . TRP B 1 319 ? 49.411  -5.543  71.961  1.00 47.01  ? 320 TRP B CA  1 
ATOM   5398  C  C   . TRP B 1 319 ? 49.952  -6.696  71.135  1.00 44.12  ? 320 TRP B C   1 
ATOM   5399  O  O   . TRP B 1 319 ? 50.187  -7.786  71.670  1.00 47.32  ? 320 TRP B O   1 
ATOM   5400  C  CB  . TRP B 1 319 ? 47.888  -5.473  71.845  1.00 48.02  ? 320 TRP B CB  1 
ATOM   5401  C  CG  . TRP B 1 319 ? 47.268  -4.721  72.972  1.00 53.92  ? 320 TRP B CG  1 
ATOM   5402  C  CD1 . TRP B 1 319 ? 47.045  -5.181  74.237  1.00 55.81  ? 320 TRP B CD1 1 
ATOM   5403  C  CD2 . TRP B 1 319 ? 46.804  -3.369  72.949  1.00 57.88  ? 320 TRP B CD2 1 
ATOM   5404  N  NE1 . TRP B 1 319 ? 46.466  -4.200  75.002  1.00 56.24  ? 320 TRP B NE1 1 
ATOM   5405  C  CE2 . TRP B 1 319 ? 46.306  -3.076  74.234  1.00 61.74  ? 320 TRP B CE2 1 
ATOM   5406  C  CE3 . TRP B 1 319 ? 46.754  -2.378  71.965  1.00 58.29  ? 320 TRP B CE3 1 
ATOM   5407  C  CZ2 . TRP B 1 319 ? 45.769  -1.833  74.561  1.00 61.09  ? 320 TRP B CZ2 1 
ATOM   5408  C  CZ3 . TRP B 1 319 ? 46.222  -1.145  72.291  1.00 58.91  ? 320 TRP B CZ3 1 
ATOM   5409  C  CH2 . TRP B 1 319 ? 45.736  -0.884  73.577  1.00 60.22  ? 320 TRP B CH2 1 
ATOM   5410  N  N   . LEU B 1 320 ? 50.160  -6.467  69.839  1.00 42.46  ? 321 LEU B N   1 
ATOM   5411  C  CA  . LEU B 1 320 ? 50.779  -7.523  69.030  1.00 47.61  ? 321 LEU B CA  1 
ATOM   5412  C  C   . LEU B 1 320 ? 52.162  -7.925  69.586  1.00 54.74  ? 321 LEU B C   1 
ATOM   5413  O  O   . LEU B 1 320 ? 52.459  -9.121  69.782  1.00 52.24  ? 321 LEU B O   1 
ATOM   5414  C  CB  . LEU B 1 320 ? 50.892  -7.083  67.568  1.00 41.84  ? 321 LEU B CB  1 
ATOM   5415  C  CG  . LEU B 1 320 ? 49.563  -6.697  66.911  1.00 48.05  ? 321 LEU B CG  1 
ATOM   5416  C  CD1 . LEU B 1 320 ? 49.738  -6.409  65.429  1.00 40.91  ? 321 LEU B CD1 1 
ATOM   5417  C  CD2 . LEU B 1 320 ? 48.521  -7.784  67.124  1.00 50.00  ? 321 LEU B CD2 1 
ATOM   5418  N  N   . ALA B 1 321 ? 52.985  -6.917  69.865  1.00 49.85  ? 322 ALA B N   1 
ATOM   5419  C  CA  . ALA B 1 321 ? 54.324  -7.127  70.412  1.00 54.19  ? 322 ALA B CA  1 
ATOM   5420  C  C   . ALA B 1 321 ? 54.288  -7.835  71.765  1.00 56.74  ? 322 ALA B C   1 
ATOM   5421  O  O   . ALA B 1 321 ? 55.091  -8.735  72.025  1.00 58.88  ? 322 ALA B O   1 
ATOM   5422  C  CB  . ALA B 1 321 ? 55.053  -5.798  70.538  1.00 44.63  ? 322 ALA B CB  1 
ATOM   5423  N  N   . GLU B 1 322 ? 53.363  -7.419  72.624  1.00 57.29  ? 323 GLU B N   1 
ATOM   5424  C  CA  . GLU B 1 322 ? 53.200  -8.044  73.932  1.00 60.82  ? 323 GLU B CA  1 
ATOM   5425  C  C   . GLU B 1 322 ? 52.809  -9.508  73.786  1.00 62.97  ? 323 GLU B C   1 
ATOM   5426  O  O   . GLU B 1 322 ? 53.246  -10.357 74.565  1.00 61.96  ? 323 GLU B O   1 
ATOM   5427  C  CB  . GLU B 1 322 ? 52.154  -7.301  74.763  1.00 67.00  ? 323 GLU B CB  1 
ATOM   5428  C  CG  . GLU B 1 322 ? 52.730  -6.219  75.660  1.00 78.38  ? 323 GLU B CG  1 
ATOM   5429  C  CD  . GLU B 1 322 ? 51.691  -5.204  76.091  1.00 84.84  ? 323 GLU B CD  1 
ATOM   5430  O  OE1 . GLU B 1 322 ? 50.953  -4.699  75.219  1.00 86.21  ? 323 GLU B OE1 1 
ATOM   5431  O  OE2 . GLU B 1 322 ? 51.609  -4.913  77.303  1.00 88.26  ? 323 GLU B OE2 1 
ATOM   5432  N  N   . ALA B 1 323 ? 51.987  -9.798  72.782  1.00 64.37  ? 324 ALA B N   1 
ATOM   5433  C  CA  . ALA B 1 323 ? 51.588  -11.173 72.510  1.00 66.84  ? 324 ALA B CA  1 
ATOM   5434  C  C   . ALA B 1 323 ? 52.785  -12.019 72.091  1.00 61.98  ? 324 ALA B C   1 
ATOM   5435  O  O   . ALA B 1 323 ? 53.020  -13.100 72.649  1.00 47.00  ? 324 ALA B O   1 
ATOM   5436  C  CB  . ALA B 1 323 ? 50.522  -11.210 71.444  1.00 44.14  ? 324 ALA B CB  1 
ATOM   5437  N  N   . ILE B 1 324 ? 53.539  -11.528 71.109  1.00 57.66  ? 325 ILE B N   1 
ATOM   5438  C  CA  . ILE B 1 324 ? 54.716  -12.263 70.643  1.00 57.24  ? 325 ILE B CA  1 
ATOM   5439  C  C   . ILE B 1 324 ? 55.714  -12.504 71.779  1.00 61.10  ? 325 ILE B C   1 
ATOM   5440  O  O   . ILE B 1 324 ? 56.191  -13.629 71.978  1.00 61.67  ? 325 ILE B O   1 
ATOM   5441  C  CB  . ILE B 1 324 ? 55.429  -11.528 69.496  1.00 51.22  ? 325 ILE B CB  1 
ATOM   5442  C  CG1 . ILE B 1 324 ? 54.464  -11.298 68.332  1.00 49.70  ? 325 ILE B CG1 1 
ATOM   5443  C  CG2 . ILE B 1 324 ? 56.640  -12.323 69.031  1.00 48.83  ? 325 ILE B CG2 1 
ATOM   5444  C  CD1 . ILE B 1 324 ? 55.089  -10.587 67.154  1.00 49.45  ? 325 ILE B CD1 1 
ATOM   5445  N  N   . ASN B 1 325 ? 56.014  -11.444 72.525  1.00 55.91  ? 326 ASN B N   1 
ATOM   5446  C  CA  . ASN B 1 325 ? 56.911  -11.539 73.671  1.00 57.05  ? 326 ASN B CA  1 
ATOM   5447  C  C   . ASN B 1 325 ? 56.410  -12.545 74.702  1.00 63.44  ? 326 ASN B C   1 
ATOM   5448  O  O   . ASN B 1 325 ? 57.197  -13.285 75.298  1.00 62.02  ? 326 ASN B O   1 
ATOM   5449  C  CB  . ASN B 1 325 ? 57.088  -10.167 74.324  1.00 57.66  ? 326 ASN B CB  1 
ATOM   5450  C  CG  . ASN B 1 325 ? 57.907  -10.229 75.599  1.00 58.83  ? 326 ASN B CG  1 
ATOM   5451  O  OD1 . ASN B 1 325 ? 57.369  -10.126 76.702  1.00 60.17  ? 326 ASN B OD1 1 
ATOM   5452  N  ND2 . ASN B 1 325 ? 59.215  -10.402 75.453  1.00 55.07  ? 326 ASN B ND2 1 
ATOM   5453  N  N   . ALA B 1 326 ? 55.096  -12.570 74.903  1.00 64.65  ? 327 ALA B N   1 
ATOM   5454  C  CA  . ALA B 1 326 ? 54.481  -13.515 75.826  1.00 66.08  ? 327 ALA B CA  1 
ATOM   5455  C  C   . ALA B 1 326 ? 54.682  -14.948 75.349  1.00 62.99  ? 327 ALA B C   1 
ATOM   5456  O  O   . ALA B 1 326 ? 54.957  -15.842 76.152  1.00 51.21  ? 327 ALA B O   1 
ATOM   5457  C  CB  . ALA B 1 326 ? 53.002  -13.216 75.989  1.00 48.27  ? 327 ALA B CB  1 
ATOM   5458  N  N   . LEU B 1 327 ? 54.543  -15.166 74.044  1.00 62.98  ? 328 LEU B N   1 
ATOM   5459  C  CA  . LEU B 1 327 ? 54.759  -16.498 73.489  1.00 54.68  ? 328 LEU B CA  1 
ATOM   5460  C  C   . LEU B 1 327 ? 56.211  -16.929 73.655  1.00 62.55  ? 328 LEU B C   1 
ATOM   5461  O  O   . LEU B 1 327 ? 56.483  -18.067 74.040  1.00 62.92  ? 328 LEU B O   1 
ATOM   5462  C  CB  . LEU B 1 327 ? 54.366  -16.554 72.013  1.00 54.72  ? 328 LEU B CB  1 
ATOM   5463  C  CG  . LEU B 1 327 ? 54.621  -17.915 71.356  1.00 57.22  ? 328 LEU B CG  1 
ATOM   5464  C  CD1 . LEU B 1 327 ? 53.989  -19.029 72.170  1.00 59.41  ? 328 LEU B CD1 1 
ATOM   5465  C  CD2 . LEU B 1 327 ? 54.093  -17.942 69.938  1.00 56.21  ? 328 LEU B CD2 1 
ATOM   5466  N  N   . GLN B 1 328 ? 57.141  -16.023 73.363  1.00 63.88  ? 329 GLN B N   1 
ATOM   5467  C  CA  . GLN B 1 328 ? 58.559  -16.337 73.522  1.00 64.29  ? 329 GLN B CA  1 
ATOM   5468  C  C   . GLN B 1 328 ? 58.902  -16.673 74.970  1.00 63.84  ? 329 GLN B C   1 
ATOM   5469  O  O   . GLN B 1 328 ? 59.599  -17.652 75.237  1.00 61.26  ? 329 GLN B O   1 
ATOM   5470  C  CB  . GLN B 1 328 ? 59.432  -15.177 73.043  1.00 69.88  ? 329 GLN B CB  1 
ATOM   5471  C  CG  . GLN B 1 328 ? 59.203  -14.768 71.603  1.00 75.29  ? 329 GLN B CG  1 
ATOM   5472  C  CD  . GLN B 1 328 ? 60.329  -13.907 71.069  1.00 80.40  ? 329 GLN B CD  1 
ATOM   5473  O  OE1 . GLN B 1 328 ? 61.284  -14.410 70.478  1.00 83.73  ? 329 GLN B OE1 1 
ATOM   5474  N  NE2 . GLN B 1 328 ? 60.229  -12.600 71.286  1.00 81.32  ? 329 GLN B NE2 1 
ATOM   5475  N  N   . ASP B 1 329 ? 58.401  -15.860 75.897  1.00 62.46  ? 330 ASP B N   1 
ATOM   5476  C  CA  . ASP B 1 329 ? 58.700  -16.018 77.319  1.00 67.44  ? 330 ASP B CA  1 
ATOM   5477  C  C   . ASP B 1 329 ? 58.340  -17.402 77.860  1.00 66.41  ? 330 ASP B C   1 
ATOM   5478  O  O   . ASP B 1 329 ? 59.128  -18.018 78.576  1.00 62.34  ? 330 ASP B O   1 
ATOM   5479  C  CB  . ASP B 1 329 ? 57.973  -14.945 78.131  1.00 73.25  ? 330 ASP B CB  1 
ATOM   5480  C  CG  . ASP B 1 329 ? 58.767  -13.656 78.236  1.00 82.71  ? 330 ASP B CG  1 
ATOM   5481  O  OD1 . ASP B 1 329 ? 59.540  -13.353 77.303  1.00 83.97  ? 330 ASP B OD1 1 
ATOM   5482  O  OD2 . ASP B 1 329 ? 58.615  -12.944 79.252  1.00 82.61  ? 330 ASP B OD2 1 
ATOM   5483  N  N   . ASN B 1 330 ? 57.152  -17.886 77.517  1.00 68.82  ? 331 ASN B N   1 
ATOM   5484  C  CA  . ASN B 1 330 ? 56.700  -19.184 78.004  1.00 79.22  ? 331 ASN B CA  1 
ATOM   5485  C  C   . ASN B 1 330 ? 56.741  -20.261 76.932  1.00 85.64  ? 331 ASN B C   1 
ATOM   5486  O  O   . ASN B 1 330 ? 55.842  -21.095 76.848  1.00 88.90  ? 331 ASN B O   1 
ATOM   5487  C  CB  . ASN B 1 330 ? 55.284  -19.078 78.569  1.00 85.15  ? 331 ASN B CB  1 
ATOM   5488  C  CG  . ASN B 1 330 ? 55.259  -19.128 80.082  1.00 91.23  ? 331 ASN B CG  1 
ATOM   5489  O  OD1 . ASN B 1 330 ? 56.182  -19.646 80.712  1.00 95.44  ? 331 ASN B OD1 1 
ATOM   5490  N  ND2 . ASN B 1 330 ? 54.199  -18.592 80.675  1.00 90.78  ? 331 ASN B ND2 1 
ATOM   5491  N  N   . ARG B 1 331 ? 57.788  -20.245 76.116  1.00 84.61  ? 332 ARG B N   1 
ATOM   5492  C  CA  . ARG B 1 331 ? 57.960  -21.259 75.085  1.00 83.35  ? 332 ARG B CA  1 
ATOM   5493  C  C   . ARG B 1 331 ? 58.141  -22.649 75.681  1.00 75.97  ? 332 ARG B C   1 
ATOM   5494  O  O   . ARG B 1 331 ? 57.608  -23.627 75.162  1.00 71.77  ? 332 ARG B O   1 
ATOM   5495  C  CB  . ARG B 1 331 ? 59.155  -20.926 74.198  1.00 84.73  ? 332 ARG B CB  1 
ATOM   5496  C  CG  . ARG B 1 331 ? 59.400  -21.950 73.107  1.00 85.83  ? 332 ARG B CG  1 
ATOM   5497  C  CD  . ARG B 1 331 ? 60.540  -21.521 72.210  1.00 87.27  ? 332 ARG B CD  1 
ATOM   5498  N  NE  . ARG B 1 331 ? 61.822  -21.478 72.906  1.00 88.57  ? 332 ARG B NE  1 
ATOM   5499  C  CZ  . ARG B 1 331 ? 62.622  -22.527 73.068  1.00 85.73  ? 332 ARG B CZ  1 
ATOM   5500  N  NH1 . ARG B 1 331 ? 62.281  -23.708 72.570  1.00 87.68  ? 332 ARG B NH1 1 
ATOM   5501  N  NH2 . ARG B 1 331 ? 63.772  -22.391 73.713  1.00 87.72  ? 332 ARG B NH2 1 
ATOM   5502  N  N   . ASP B 1 332 ? 58.896  -22.723 76.772  1.00 81.92  ? 333 ASP B N   1 
ATOM   5503  C  CA  . ASP B 1 332 ? 59.221  -23.996 77.410  1.00 86.20  ? 333 ASP B CA  1 
ATOM   5504  C  C   . ASP B 1 332 ? 57.999  -24.668 78.034  1.00 84.16  ? 333 ASP B C   1 
ATOM   5505  O  O   . ASP B 1 332 ? 57.702  -25.828 77.739  1.00 80.03  ? 333 ASP B O   1 
ATOM   5506  C  CB  . ASP B 1 332 ? 60.301  -23.788 78.474  1.00 87.34  ? 333 ASP B CB  1 
ATOM   5507  N  N   . THR B 1 333 ? 57.304  -23.938 78.904  1.00 84.09  ? 334 THR B N   1 
ATOM   5508  C  CA  . THR B 1 333 ? 56.104  -24.445 79.566  1.00 84.06  ? 334 THR B CA  1 
ATOM   5509  C  C   . THR B 1 333 ? 55.060  -24.880 78.544  1.00 72.77  ? 334 THR B C   1 
ATOM   5510  O  O   . THR B 1 333 ? 54.539  -26.005 78.594  1.00 69.82  ? 334 THR B O   1 
ATOM   5511  C  CB  . THR B 1 333 ? 55.483  -23.383 80.498  1.00 88.46  ? 334 THR B CB  1 
ATOM   5512  O  OG1 . THR B 1 333 ? 56.427  -23.021 81.513  1.00 91.33  ? 334 THR B OG1 1 
ATOM   5513  C  CG2 . THR B 1 333 ? 54.217  -23.915 81.152  1.00 90.49  ? 334 THR B CG2 1 
ATOM   5514  N  N   . LEU B 1 334 ? 54.768  -23.971 77.617  1.00 72.03  ? 335 LEU B N   1 
ATOM   5515  C  CA  . LEU B 1 334 ? 53.840  -24.236 76.528  1.00 69.25  ? 335 LEU B CA  1 
ATOM   5516  C  C   . LEU B 1 334 ? 54.239  -25.502 75.791  1.00 64.65  ? 335 LEU B C   1 
ATOM   5517  O  O   . LEU B 1 334 ? 53.403  -26.356 75.532  1.00 66.06  ? 335 LEU B O   1 
ATOM   5518  C  CB  . LEU B 1 334 ? 53.792  -23.060 75.553  1.00 67.68  ? 335 LEU B CB  1 
ATOM   5519  C  CG  . LEU B 1 334 ? 52.740  -23.165 74.449  1.00 68.76  ? 335 LEU B CG  1 
ATOM   5520  C  CD1 . LEU B 1 334 ? 51.379  -22.759 74.982  1.00 68.95  ? 335 LEU B CD1 1 
ATOM   5521  C  CD2 . LEU B 1 334 ? 53.120  -22.325 73.245  1.00 66.83  ? 335 LEU B CD2 1 
ATOM   5522  N  N   . THR B 1 335 ? 55.523  -25.618 75.467  1.00 63.42  ? 336 THR B N   1 
ATOM   5523  C  CA  . THR B 1 335 ? 56.044  -26.803 74.795  1.00 62.31  ? 336 THR B CA  1 
ATOM   5524  C  C   . THR B 1 335 ? 55.720  -28.066 75.581  1.00 64.96  ? 336 THR B C   1 
ATOM   5525  O  O   . THR B 1 335 ? 55.180  -29.024 75.032  1.00 68.76  ? 336 THR B O   1 
ATOM   5526  C  CB  . THR B 1 335 ? 57.565  -26.718 74.598  1.00 64.56  ? 336 THR B CB  1 
ATOM   5527  O  OG1 . THR B 1 335 ? 57.864  -25.676 73.663  1.00 64.06  ? 336 THR B OG1 1 
ATOM   5528  C  CG2 . THR B 1 335 ? 58.112  -28.035 74.068  1.00 67.89  ? 336 THR B CG2 1 
ATOM   5529  N  N   . ALA B 1 336 ? 56.043  -28.048 76.871  1.00 64.81  ? 337 ALA B N   1 
ATOM   5530  C  CA  . ALA B 1 336 ? 55.804  -29.191 77.745  1.00 68.58  ? 337 ALA B CA  1 
ATOM   5531  C  C   . ALA B 1 336 ? 54.339  -29.613 77.734  1.00 67.62  ? 337 ALA B C   1 
ATOM   5532  O  O   . ALA B 1 336 ? 54.020  -30.789 77.529  1.00 69.59  ? 337 ALA B O   1 
ATOM   5533  C  CB  . ALA B 1 336 ? 56.246  -28.868 79.164  1.00 65.02  ? 337 ALA B CB  1 
ATOM   5534  N  N   . LYS B 1 337 ? 53.448  -28.648 77.935  1.00 66.96  ? 338 LYS B N   1 
ATOM   5535  C  CA  . LYS B 1 337 ? 52.027  -28.965 78.055  1.00 67.99  ? 338 LYS B CA  1 
ATOM   5536  C  C   . LYS B 1 337 ? 51.423  -29.395 76.716  1.00 63.96  ? 338 LYS B C   1 
ATOM   5537  O  O   . LYS B 1 337 ? 50.508  -30.221 76.674  1.00 65.89  ? 338 LYS B O   1 
ATOM   5538  C  CB  . LYS B 1 337 ? 51.258  -27.774 78.637  1.00 72.21  ? 338 LYS B CB  1 
ATOM   5539  C  CG  . LYS B 1 337 ? 51.258  -27.718 80.169  1.00 78.02  ? 338 LYS B CG  1 
ATOM   5540  C  CD  . LYS B 1 337 ? 52.666  -27.764 80.756  1.00 81.80  ? 338 LYS B CD  1 
ATOM   5541  C  CE  . LYS B 1 337 ? 52.651  -27.857 82.272  1.00 84.95  ? 338 LYS B CE  1 
ATOM   5542  N  NZ  . LYS B 1 337 ? 53.955  -28.340 82.812  1.00 87.42  ? 338 LYS B NZ  1 
ATOM   5543  N  N   . VAL B 1 338 ? 51.950  -28.847 75.626  1.00 61.47  ? 339 VAL B N   1 
ATOM   5544  C  CA  . VAL B 1 338 ? 51.507  -29.215 74.284  1.00 61.24  ? 339 VAL B CA  1 
ATOM   5545  C  C   . VAL B 1 338 ? 51.975  -30.625 73.938  1.00 76.36  ? 339 VAL B C   1 
ATOM   5546  O  O   . VAL B 1 338 ? 51.283  -31.363 73.240  1.00 81.97  ? 339 VAL B O   1 
ATOM   5547  C  CB  . VAL B 1 338 ? 52.013  -28.206 73.224  1.00 67.10  ? 339 VAL B CB  1 
ATOM   5548  C  CG1 . VAL B 1 338 ? 51.820  -28.744 71.813  1.00 62.89  ? 339 VAL B CG1 1 
ATOM   5549  C  CG2 . VAL B 1 338 ? 51.290  -26.880 73.380  1.00 58.18  ? 339 VAL B CG2 1 
ATOM   5550  N  N   . ILE B 1 339 ? 53.147  -31.005 74.435  1.00 73.49  ? 340 ILE B N   1 
ATOM   5551  C  CA  . ILE B 1 339 ? 53.616  -32.376 74.279  1.00 70.41  ? 340 ILE B CA  1 
ATOM   5552  C  C   . ILE B 1 339 ? 52.748  -33.309 75.118  1.00 72.47  ? 340 ILE B C   1 
ATOM   5553  O  O   . ILE B 1 339 ? 52.425  -34.420 74.696  1.00 73.41  ? 340 ILE B O   1 
ATOM   5554  C  CB  . ILE B 1 339 ? 55.098  -32.531 74.683  1.00 68.86  ? 340 ILE B CB  1 
ATOM   5555  C  CG1 . ILE B 1 339 ? 55.996  -31.739 73.734  1.00 66.08  ? 340 ILE B CG1 1 
ATOM   5556  C  CG2 . ILE B 1 339 ? 55.512  -33.994 74.670  1.00 68.72  ? 340 ILE B CG2 1 
ATOM   5557  C  CD1 . ILE B 1 339 ? 57.445  -31.697 74.163  1.00 67.79  ? 340 ILE B CD1 1 
ATOM   5558  N  N   . GLN B 1 340 ? 52.357  -32.846 76.301  1.00 71.35  ? 341 GLN B N   1 
ATOM   5559  C  CA  . GLN B 1 340 ? 51.495  -33.642 77.170  1.00 71.35  ? 341 GLN B CA  1 
ATOM   5560  C  C   . GLN B 1 340 ? 50.091  -33.822 76.595  1.00 67.74  ? 341 GLN B C   1 
ATOM   5561  O  O   . GLN B 1 340 ? 49.427  -34.822 76.868  1.00 69.16  ? 341 GLN B O   1 
ATOM   5562  C  CB  . GLN B 1 340 ? 51.403  -33.010 78.560  1.00 67.97  ? 341 GLN B CB  1 
ATOM   5563  C  CG  . GLN B 1 340 ? 52.574  -33.336 79.468  1.00 69.24  ? 341 GLN B CG  1 
ATOM   5564  C  CD  . GLN B 1 340 ? 52.185  -33.336 80.933  1.00 76.51  ? 341 GLN B CD  1 
ATOM   5565  O  OE1 . GLN B 1 340 ? 51.678  -32.343 81.453  1.00 72.84  ? 341 GLN B OE1 1 
ATOM   5566  N  NE2 . GLN B 1 340 ? 52.415  -34.459 81.605  1.00 80.96  ? 341 GLN B NE2 1 
ATOM   5567  N  N   . GLY B 1 341 ? 49.641  -32.856 75.799  1.00 73.67  ? 342 GLY B N   1 
ATOM   5568  C  CA  . GLY B 1 341 ? 48.293  -32.894 75.259  1.00 72.66  ? 342 GLY B CA  1 
ATOM   5569  C  C   . GLY B 1 341 ? 48.166  -33.508 73.876  1.00 70.99  ? 342 GLY B C   1 
ATOM   5570  O  O   . GLY B 1 341 ? 47.148  -34.123 73.555  1.00 66.65  ? 342 GLY B O   1 
ATOM   5571  N  N   . CYS B 1 342 ? 49.199  -33.347 73.057  1.00 72.62  ? 343 CYS B N   1 
ATOM   5572  C  CA  . CYS B 1 342 ? 49.149  -33.773 71.662  1.00 72.79  ? 343 CYS B CA  1 
ATOM   5573  C  C   . CYS B 1 342 ? 50.168  -34.867 71.354  1.00 71.37  ? 343 CYS B C   1 
ATOM   5574  O  O   . CYS B 1 342 ? 50.270  -35.327 70.217  1.00 71.24  ? 343 CYS B O   1 
ATOM   5575  C  CB  . CYS B 1 342 ? 49.380  -32.575 70.737  1.00 76.39  ? 343 CYS B CB  1 
ATOM   5576  S  SG  . CYS B 1 342 ? 48.226  -31.203 70.987  1.00 83.36  ? 343 CYS B SG  1 
ATOM   5577  N  N   . GLY B 1 343 ? 50.923  -35.277 72.367  1.00 71.02  ? 344 GLY B N   1 
ATOM   5578  C  CA  . GLY B 1 343 ? 51.902  -36.336 72.203  1.00 70.08  ? 344 GLY B CA  1 
ATOM   5579  C  C   . GLY B 1 343 ? 53.288  -35.826 71.861  1.00 74.79  ? 344 GLY B C   1 
ATOM   5580  O  O   . GLY B 1 343 ? 53.508  -34.619 71.758  1.00 74.37  ? 344 GLY B O   1 
ATOM   5581  N  N   . ASN B 1 344 ? 54.225  -36.751 71.683  1.00 82.38  ? 345 ASN B N   1 
ATOM   5582  C  CA  . ASN B 1 344 ? 55.607  -36.396 71.380  1.00 84.13  ? 345 ASN B CA  1 
ATOM   5583  C  C   . ASN B 1 344 ? 55.873  -36.264 69.883  1.00 86.18  ? 345 ASN B C   1 
ATOM   5584  O  O   . ASN B 1 344 ? 55.697  -37.220 69.128  1.00 88.79  ? 345 ASN B O   1 
ATOM   5585  C  CB  . ASN B 1 344 ? 56.565  -37.425 71.984  1.00 89.15  ? 345 ASN B CB  1 
ATOM   5586  C  CG  . ASN B 1 344 ? 56.752  -37.240 73.477  1.00 92.34  ? 345 ASN B CG  1 
ATOM   5587  O  OD1 . ASN B 1 344 ? 56.030  -37.828 74.283  1.00 93.47  ? 345 ASN B OD1 1 
ATOM   5588  N  ND2 . ASN B 1 344 ? 57.727  -36.421 73.854  1.00 94.25  ? 345 ASN B ND2 1 
ATOM   5589  N  N   . PRO B 1 345 ? 56.293  -35.065 69.455  1.00 82.59  ? 346 PRO B N   1 
ATOM   5590  C  CA  . PRO B 1 345 ? 56.687  -34.755 68.077  1.00 85.05  ? 346 PRO B CA  1 
ATOM   5591  C  C   . PRO B 1 345 ? 58.042  -35.355 67.720  1.00 87.36  ? 346 PRO B C   1 
ATOM   5592  O  O   . PRO B 1 345 ? 58.787  -35.768 68.610  1.00 88.60  ? 346 PRO B O   1 
ATOM   5593  C  CB  . PRO B 1 345 ? 56.749  -33.228 68.069  1.00 80.01  ? 346 PRO B CB  1 
ATOM   5594  C  CG  . PRO B 1 345 ? 57.104  -32.875 69.468  1.00 79.70  ? 346 PRO B CG  1 
ATOM   5595  C  CD  . PRO B 1 345 ? 56.409  -33.888 70.334  1.00 83.14  ? 346 PRO B CD  1 
ATOM   5596  N  N   . LYS B 1 346 ? 58.354  -35.402 66.430  1.00 88.88  ? 347 LYS B N   1 
ATOM   5597  C  CA  . LYS B 1 346 ? 59.639  -35.920 65.994  1.00 87.57  ? 347 LYS B CA  1 
ATOM   5598  C  C   . LYS B 1 346 ? 60.713  -34.889 66.338  1.00 88.11  ? 347 LYS B C   1 
ATOM   5599  O  O   . LYS B 1 346 ? 60.409  -33.790 66.807  1.00 88.41  ? 347 LYS B O   1 
ATOM   5600  C  CB  . LYS B 1 346 ? 59.601  -36.214 64.486  1.00 88.02  ? 347 LYS B CB  1 
ATOM   5601  C  CG  . LYS B 1 346 ? 60.736  -37.063 63.920  1.00 89.33  ? 347 LYS B CG  1 
ATOM   5602  C  CD  . LYS B 1 346 ? 60.643  -37.131 62.400  1.00 89.61  ? 347 LYS B CD  1 
ATOM   5603  C  CE  . LYS B 1 346 ? 61.948  -37.592 61.772  1.00 91.36  ? 347 LYS B CE  1 
ATOM   5604  N  NZ  . LYS B 1 346 ? 61.929  -37.441 60.290  1.00 92.37  ? 347 LYS B NZ  1 
ATOM   5605  N  N   . VAL B 1 347 ? 61.967  -35.240 66.087  1.00 89.64  ? 348 VAL B N   1 
ATOM   5606  C  CA  . VAL B 1 347 ? 63.093  -34.362 66.360  1.00 88.80  ? 348 VAL B CA  1 
ATOM   5607  C  C   . VAL B 1 347 ? 63.937  -34.414 65.081  1.00 89.12  ? 348 VAL B C   1 
ATOM   5608  O  O   . VAL B 1 347 ? 63.504  -35.011 64.091  1.00 91.53  ? 348 VAL B O   1 
ATOM   5609  C  CB  . VAL B 1 347 ? 63.895  -34.816 67.626  1.00 75.37  ? 348 VAL B CB  1 
ATOM   5610  C  CG1 . VAL B 1 347 ? 64.868  -33.739 68.107  1.00 76.01  ? 348 VAL B CG1 1 
ATOM   5611  C  CG2 . VAL B 1 347 ? 62.952  -35.194 68.763  1.00 74.58  ? 348 VAL B CG2 1 
ATOM   5612  N  N   . ASN B 1 348 ? 65.106  -33.775 65.093  1.00 88.42  ? 349 ASN B N   1 
ATOM   5613  C  CA  . ASN B 1 348 ? 66.096  -33.852 64.013  1.00 86.89  ? 349 ASN B CA  1 
ATOM   5614  C  C   . ASN B 1 348 ? 65.631  -33.184 62.721  1.00 85.61  ? 349 ASN B C   1 
ATOM   5615  O  O   . ASN B 1 348 ? 65.059  -32.095 62.744  1.00 82.89  ? 349 ASN B O   1 
ATOM   5616  C  CB  . ASN B 1 348 ? 66.473  -35.315 63.738  1.00 86.02  ? 349 ASN B CB  1 
ATOM   5617  C  CG  . ASN B 1 348 ? 67.977  -35.521 63.630  1.00 90.06  ? 349 ASN B CG  1 
ATOM   5618  O  OD1 . ASN B 1 348 ? 68.688  -34.709 63.037  1.00 91.01  ? 349 ASN B OD1 1 
ATOM   5619  N  ND2 . ASN B 1 348 ? 68.470  -36.596 64.235  1.00 89.87  ? 349 ASN B ND2 1 
ATOM   5620  N  N   . ARG B 1 360 ? 69.762  -4.500  70.780  1.00 118.09 ? 361 ARG B N   1 
ATOM   5621  C  CA  . ARG B 1 360 ? 68.627  -4.703  69.887  1.00 116.14 ? 361 ARG B CA  1 
ATOM   5622  C  C   . ARG B 1 360 ? 67.374  -5.099  70.664  1.00 110.38 ? 361 ARG B C   1 
ATOM   5623  O  O   . ARG B 1 360 ? 67.403  -5.210  71.890  1.00 110.93 ? 361 ARG B O   1 
ATOM   5624  C  CB  . ARG B 1 360 ? 68.954  -5.767  68.837  1.00 116.83 ? 361 ARG B CB  1 
ATOM   5625  N  N   . GLY B 1 361 ? 66.279  -5.311  69.941  1.00 105.87 ? 362 GLY B N   1 
ATOM   5626  C  CA  . GLY B 1 361 ? 65.012  -5.672  70.552  1.00 100.97 ? 362 GLY B CA  1 
ATOM   5627  C  C   . GLY B 1 361 ? 64.446  -4.562  71.418  1.00 97.38  ? 362 GLY B C   1 
ATOM   5628  O  O   . GLY B 1 361 ? 63.851  -4.820  72.465  1.00 97.96  ? 362 GLY B O   1 
ATOM   5629  N  N   . LYS B 1 362 ? 64.632  -3.322  70.975  1.00 92.29  ? 363 LYS B N   1 
ATOM   5630  C  CA  . LYS B 1 362 ? 64.169  -2.155  71.718  1.00 91.24  ? 363 LYS B CA  1 
ATOM   5631  C  C   . LYS B 1 362 ? 62.843  -1.638  71.160  1.00 89.76  ? 363 LYS B C   1 
ATOM   5632  O  O   . LYS B 1 362 ? 62.773  -1.177  70.019  1.00 92.12  ? 363 LYS B O   1 
ATOM   5633  C  CB  . LYS B 1 362 ? 65.230  -1.050  71.688  1.00 90.47  ? 363 LYS B CB  1 
ATOM   5634  N  N   . LEU B 1 363 ? 61.793  -1.723  71.973  1.00 86.04  ? 364 LEU B N   1 
ATOM   5635  C  CA  . LEU B 1 363 ? 60.449  -1.316  71.563  1.00 82.02  ? 364 LEU B CA  1 
ATOM   5636  C  C   . LEU B 1 363 ? 59.906  -0.132  72.341  1.00 86.38  ? 364 LEU B C   1 
ATOM   5637  O  O   . LEU B 1 363 ? 60.012  -0.081  73.566  1.00 86.13  ? 364 LEU B O   1 
ATOM   5638  C  CB  . LEU B 1 363 ? 59.467  -2.486  71.704  1.00 78.43  ? 364 LEU B CB  1 
ATOM   5639  C  CG  . LEU B 1 363 ? 59.253  -3.432  70.521  1.00 71.07  ? 364 LEU B CG  1 
ATOM   5640  C  CD1 . LEU B 1 363 ? 60.410  -3.337  69.548  1.00 73.63  ? 364 LEU B CD1 1 
ATOM   5641  C  CD2 . LEU B 1 363 ? 58.967  -4.875  70.973  1.00 73.51  ? 364 LEU B CD2 1 
ATOM   5642  N  N   . ALA B 1 364 ? 59.306  0.811   71.623  1.00 89.79  ? 365 ALA B N   1 
ATOM   5643  C  CA  . ALA B 1 364 ? 58.541  1.862   72.269  1.00 93.03  ? 365 ALA B CA  1 
ATOM   5644  C  C   . ALA B 1 364 ? 57.354  1.215   72.967  1.00 96.22  ? 365 ALA B C   1 
ATOM   5645  O  O   . ALA B 1 364 ? 56.639  0.414   72.362  1.00 96.12  ? 365 ALA B O   1 
ATOM   5646  C  CB  . ALA B 1 364 ? 58.078  2.904   71.260  1.00 89.61  ? 365 ALA B CB  1 
ATOM   5647  N  N   . PRO B 1 365 ? 57.139  1.557   74.246  1.00 104.42 ? 366 PRO B N   1 
ATOM   5648  C  CA  . PRO B 1 365 ? 56.007  1.032   75.019  1.00 104.80 ? 366 PRO B CA  1 
ATOM   5649  C  C   . PRO B 1 365 ? 54.695  1.550   74.449  1.00 101.65 ? 366 PRO B C   1 
ATOM   5650  O  O   . PRO B 1 365 ? 54.729  2.192   73.396  1.00 101.88 ? 366 PRO B O   1 
ATOM   5651  C  CB  . PRO B 1 365 ? 56.257  1.568   76.436  1.00 108.48 ? 366 PRO B CB  1 
ATOM   5652  C  CG  . PRO B 1 365 ? 57.679  2.055   76.439  1.00 110.02 ? 366 PRO B CG  1 
ATOM   5653  C  CD  . PRO B 1 365 ? 57.969  2.476   75.039  1.00 107.52 ? 366 PRO B CD  1 
ATOM   5654  N  N   . ARG B 1 366 ? 53.569  1.272   75.104  1.00 98.24  ? 367 ARG B N   1 
ATOM   5655  C  CA  . ARG B 1 366 ? 52.285  1.718   74.580  1.00 95.66  ? 367 ARG B CA  1 
ATOM   5656  C  C   . ARG B 1 366 ? 52.382  3.200   74.296  1.00 100.09 ? 367 ARG B C   1 
ATOM   5657  O  O   . ARG B 1 366 ? 52.783  3.976   75.163  1.00 102.32 ? 367 ARG B O   1 
ATOM   5658  C  CB  . ARG B 1 366 ? 51.151  1.442   75.565  1.00 87.97  ? 367 ARG B CB  1 
ATOM   5659  C  CG  . ARG B 1 366 ? 49.834  2.102   75.179  1.00 81.25  ? 367 ARG B CG  1 
ATOM   5660  C  CD  . ARG B 1 366 ? 48.689  1.106   75.178  1.00 75.47  ? 367 ARG B CD  1 
ATOM   5661  N  NE  . ARG B 1 366 ? 48.430  0.577   76.514  1.00 74.80  ? 367 ARG B NE  1 
ATOM   5662  C  CZ  . ARG B 1 366 ? 48.832  -0.617  76.935  1.00 74.71  ? 367 ARG B CZ  1 
ATOM   5663  N  NH1 . ARG B 1 366 ? 49.520  -1.409  76.124  1.00 74.18  1 367 ARG B NH1 1 
ATOM   5664  N  NH2 . ARG B 1 366 ? 48.552  -1.017  78.168  1.00 76.04  ? 367 ARG B NH2 1 
ATOM   5665  N  N   . GLU B 1 367 ? 52.023  3.603   73.084  1.00 105.67 ? 368 GLU B N   1 
ATOM   5666  C  CA  . GLU B 1 367 ? 52.305  4.971   72.714  1.00 110.62 ? 368 GLU B CA  1 
ATOM   5667  C  C   . GLU B 1 367 ? 51.251  5.824   73.379  1.00 116.63 ? 368 GLU B C   1 
ATOM   5668  O  O   . GLU B 1 367 ? 50.063  5.721   73.079  1.00 117.58 ? 368 GLU B O   1 
ATOM   5669  C  CB  . GLU B 1 367 ? 52.292  5.151   71.193  1.00 111.67 ? 368 GLU B CB  1 
ATOM   5670  N  N   . ARG B 1 368 ? 51.708  6.686   74.277  1.00 119.30 ? 369 ARG B N   1 
ATOM   5671  C  CA  . ARG B 1 368 ? 50.820  7.591   74.983  1.00 121.31 ? 369 ARG B CA  1 
ATOM   5672  C  C   . ARG B 1 368 ? 50.563  8.724   74.018  1.00 124.23 ? 369 ARG B C   1 
ATOM   5673  O  O   . ARG B 1 368 ? 51.521  9.363   73.578  1.00 127.30 0 369 ARG B O   1 
ATOM   5674  C  CB  . ARG B 1 368 ? 51.452  8.077   76.286  1.00 121.16 ? 369 ARG B CB  1 
ATOM   5675  N  N   . PRO B 1 369 ? 49.283  8.954   73.664  1.00 124.20 ? 370 PRO B N   1 
ATOM   5676  C  CA  . PRO B 1 369 ? 49.028  9.709   72.432  1.00 121.42 ? 370 PRO B CA  1 
ATOM   5677  C  C   . PRO B 1 369 ? 49.757  11.051  72.406  1.00 118.53 ? 370 PRO B C   1 
ATOM   5678  O  O   . PRO B 1 369 ? 49.624  11.875  73.308  1.00 120.72 ? 370 PRO B O   1 
ATOM   5679  C  CB  . PRO B 1 369 ? 47.504  9.881   72.452  1.00 123.06 ? 370 PRO B CB  1 
ATOM   5680  C  CG  . PRO B 1 369 ? 47.022  8.644   73.177  1.00 122.94 ? 370 PRO B CG  1 
ATOM   5681  C  CD  . PRO B 1 369 ? 48.053  8.387   74.244  1.00 123.87 ? 370 PRO B CD  1 
ATOM   5682  N  N   . PRO B 1 370 ? 50.551  11.249  71.346  1.00 114.37 ? 371 PRO B N   1 
ATOM   5683  C  CA  . PRO B 1 370 ? 51.449  12.386  71.132  1.00 112.57 ? 371 PRO B CA  1 
ATOM   5684  C  C   . PRO B 1 370 ? 50.709  13.662  70.790  1.00 107.11 ? 371 PRO B C   1 
ATOM   5685  O  O   . PRO B 1 370 ? 51.128  14.771  71.149  1.00 109.32 ? 371 PRO B O   1 
ATOM   5686  C  CB  . PRO B 1 370 ? 52.294  11.954  69.930  1.00 113.70 ? 371 PRO B CB  1 
ATOM   5687  C  CG  . PRO B 1 370 ? 51.452  10.957  69.226  1.00 114.03 ? 371 PRO B CG  1 
ATOM   5688  C  CD  . PRO B 1 370 ? 50.609  10.281  70.245  1.00 113.62 ? 371 PRO B CD  1 
ATOM   5689  N  N   . SER B 1 371 ? 49.628  13.480  70.039  1.00 102.03 ? 372 SER B N   1 
ATOM   5690  C  CA  . SER B 1 371 ? 49.079  14.520  69.186  1.00 95.68  ? 372 SER B CA  1 
ATOM   5691  C  C   . SER B 1 371 ? 47.964  15.309  69.859  1.00 90.95  ? 372 SER B C   1 
ATOM   5692  O  O   . SER B 1 371 ? 47.001  14.739  70.371  1.00 93.27  ? 372 SER B O   1 
ATOM   5693  C  CB  . SER B 1 371 ? 48.576  13.885  67.887  1.00 95.37  ? 372 SER B CB  1 
ATOM   5694  O  OG  . SER B 1 371 ? 48.572  14.805  66.816  1.00 99.23  ? 372 SER B OG  1 
ATOM   5695  N  N   . GLY B 1 372 ? 48.098  16.630  69.838  1.00 77.51  ? 373 GLY B N   1 
ATOM   5696  C  CA  . GLY B 1 372 ? 47.031  17.508  70.276  1.00 69.06  ? 373 GLY B CA  1 
ATOM   5697  C  C   . GLY B 1 372 ? 46.016  17.668  69.160  1.00 58.22  ? 373 GLY B C   1 
ATOM   5698  O  O   . GLY B 1 372 ? 45.134  18.525  69.223  1.00 62.32  ? 373 GLY B O   1 
ATOM   5699  N  N   . THR B 1 373 ? 46.153  16.839  68.129  1.00 44.58  ? 374 THR B N   1 
ATOM   5700  C  CA  . THR B 1 373 ? 45.243  16.855  66.992  1.00 45.56  ? 374 THR B CA  1 
ATOM   5701  C  C   . THR B 1 373 ? 43.820  16.515  67.419  1.00 41.90  ? 374 THR B C   1 
ATOM   5702  O  O   . THR B 1 373 ? 42.893  17.284  67.161  1.00 35.11  ? 374 THR B O   1 
ATOM   5703  C  CB  . THR B 1 373 ? 45.696  15.871  65.893  1.00 45.01  ? 374 THR B CB  1 
ATOM   5704  O  OG1 . THR B 1 373 ? 46.919  16.337  65.312  1.00 46.84  ? 374 THR B OG1 1 
ATOM   5705  C  CG2 . THR B 1 373 ? 44.639  15.758  64.803  1.00 36.01  ? 374 THR B CG2 1 
ATOM   5706  N  N   . LEU B 1 374 ? 43.648  15.372  68.078  1.00 39.52  ? 375 LEU B N   1 
ATOM   5707  C  CA  . LEU B 1 374 ? 42.318  14.943  68.501  1.00 45.72  ? 375 LEU B CA  1 
ATOM   5708  C  C   . LEU B 1 374 ? 41.698  15.907  69.501  1.00 38.37  ? 375 LEU B C   1 
ATOM   5709  O  O   . LEU B 1 374 ? 40.494  16.125  69.481  1.00 33.42  ? 375 LEU B O   1 
ATOM   5710  C  CB  . LEU B 1 374 ? 42.352  13.543  69.114  1.00 33.98  ? 375 LEU B CB  1 
ATOM   5711  C  CG  . LEU B 1 374 ? 40.954  12.986  69.409  1.00 46.06  ? 375 LEU B CG  1 
ATOM   5712  C  CD1 . LEU B 1 374 ? 40.173  12.762  68.118  1.00 38.51  ? 375 LEU B CD1 1 
ATOM   5713  C  CD2 . LEU B 1 374 ? 41.003  11.720  70.249  1.00 43.54  ? 375 LEU B CD2 1 
ATOM   5714  N  N   . GLU B 1 375 ? 42.517  16.475  70.379  1.00 39.03  ? 376 GLU B N   1 
ATOM   5715  C  CA  . GLU B 1 375 ? 42.016  17.407  71.385  1.00 38.84  ? 376 GLU B CA  1 
ATOM   5716  C  C   . GLU B 1 375 ? 41.361  18.617  70.727  1.00 42.85  ? 376 GLU B C   1 
ATOM   5717  O  O   . GLU B 1 375 ? 40.214  18.965  71.027  1.00 46.91  ? 376 GLU B O   1 
ATOM   5718  C  CB  . GLU B 1 375 ? 43.147  17.856  72.311  1.00 39.23  ? 376 GLU B CB  1 
ATOM   5719  N  N   . LYS B 1 376 ? 42.096  19.242  69.814  1.00 38.89  ? 377 LYS B N   1 
ATOM   5720  C  CA  . LYS B 1 376 ? 41.617  20.430  69.121  1.00 46.39  ? 377 LYS B CA  1 
ATOM   5721  C  C   . LYS B 1 376 ? 40.458  20.100  68.186  1.00 35.30  ? 377 LYS B C   1 
ATOM   5722  O  O   . LYS B 1 376 ? 39.503  20.874  68.070  1.00 35.80  ? 377 LYS B O   1 
ATOM   5723  C  CB  . LYS B 1 376 ? 42.765  21.082  68.352  1.00 54.57  ? 377 LYS B CB  1 
ATOM   5724  C  CG  . LYS B 1 376 ? 43.870  21.590  69.261  1.00 56.99  ? 377 LYS B CG  1 
ATOM   5725  C  CD  . LYS B 1 376 ? 45.105  21.987  68.481  1.00 61.77  ? 377 LYS B CD  1 
ATOM   5726  C  CE  . LYS B 1 376 ? 46.308  22.125  69.398  1.00 62.10  ? 377 LYS B CE  1 
ATOM   5727  N  NZ  . LYS B 1 376 ? 46.620  20.850  70.104  1.00 63.39  ? 377 LYS B NZ  1 
ATOM   5728  N  N   . LEU B 1 377 ? 40.540  18.946  67.528  1.00 34.05  ? 378 LEU B N   1 
ATOM   5729  C  CA  . LEU B 1 377 ? 39.453  18.487  66.671  1.00 33.16  ? 378 LEU B CA  1 
ATOM   5730  C  C   . LEU B 1 377 ? 38.163  18.321  67.466  1.00 34.96  ? 378 LEU B C   1 
ATOM   5731  O  O   . LEU B 1 377 ? 37.089  18.684  66.996  1.00 31.86  ? 378 LEU B O   1 
ATOM   5732  C  CB  . LEU B 1 377 ? 39.816  17.171  65.985  1.00 45.24  ? 378 LEU B CB  1 
ATOM   5733  C  CG  . LEU B 1 377 ? 40.724  17.280  64.761  1.00 47.02  ? 378 LEU B CG  1 
ATOM   5734  C  CD1 . LEU B 1 377 ? 40.964  15.904  64.161  1.00 47.36  ? 378 LEU B CD1 1 
ATOM   5735  C  CD2 . LEU B 1 377 ? 40.120  18.225  63.731  1.00 33.66  ? 378 LEU B CD2 1 
ATOM   5736  N  N   . VAL B 1 378 ? 38.279  17.785  68.676  1.00 32.42  ? 379 VAL B N   1 
ATOM   5737  C  CA  . VAL B 1 378 ? 37.122  17.577  69.538  1.00 39.85  ? 379 VAL B CA  1 
ATOM   5738  C  C   . VAL B 1 378 ? 36.605  18.905  70.092  1.00 32.08  ? 379 VAL B C   1 
ATOM   5739  O  O   . VAL B 1 378 ? 35.399  19.086  70.233  1.00 31.56  ? 379 VAL B O   1 
ATOM   5740  C  CB  . VAL B 1 378 ? 37.449  16.605  70.699  1.00 41.03  ? 379 VAL B CB  1 
ATOM   5741  C  CG1 . VAL B 1 378 ? 36.377  16.652  71.777  1.00 31.85  ? 379 VAL B CG1 1 
ATOM   5742  C  CG2 . VAL B 1 378 ? 37.595  15.185  70.170  1.00 37.07  ? 379 VAL B CG2 1 
ATOM   5743  N  N   . SER B 1 379 ? 37.503  19.839  70.391  1.00 32.91  ? 380 SER B N   1 
ATOM   5744  C  CA  . SER B 1 379 ? 37.072  21.166  70.839  1.00 44.63  ? 380 SER B CA  1 
ATOM   5745  C  C   . SER B 1 379 ? 36.253  21.868  69.753  1.00 32.81  ? 380 SER B C   1 
ATOM   5746  O  O   . SER B 1 379 ? 35.115  22.311  69.991  1.00 36.59  ? 380 SER B O   1 
ATOM   5747  C  CB  . SER B 1 379 ? 38.276  22.024  71.229  1.00 47.13  ? 380 SER B CB  1 
ATOM   5748  O  OG  . SER B 1 379 ? 38.723  21.704  72.534  1.00 51.24  ? 380 SER B OG  1 
ATOM   5749  N  N   . GLU B 1 380 ? 36.840  21.955  68.561  1.00 32.97  ? 381 GLU B N   1 
ATOM   5750  C  CA  A GLU B 1 380 ? 36.178  22.541  67.398  0.59 32.71  ? 381 GLU B CA  1 
ATOM   5751  C  CA  B GLU B 1 380 ? 36.157  22.570  67.431  0.41 32.71  ? 381 GLU B CA  1 
ATOM   5752  C  C   . GLU B 1 380 ? 34.847  21.853  67.114  1.00 31.72  ? 381 GLU B C   1 
ATOM   5753  O  O   . GLU B 1 380 ? 33.835  22.502  66.862  1.00 31.55  ? 381 GLU B O   1 
ATOM   5754  C  CB  A GLU B 1 380 ? 37.087  22.446  66.169  0.59 33.15  ? 381 GLU B CB  1 
ATOM   5755  C  CB  B GLU B 1 380 ? 37.063  22.591  66.199  0.41 33.19  ? 381 GLU B CB  1 
ATOM   5756  C  CG  A GLU B 1 380 ? 36.451  22.927  64.872  0.59 33.00  ? 381 GLU B CG  1 
ATOM   5757  C  CG  B GLU B 1 380 ? 38.371  23.343  66.405  0.41 44.73  ? 381 GLU B CG  1 
ATOM   5758  C  CD  A GLU B 1 380 ? 36.632  24.416  64.648  0.59 45.30  ? 381 GLU B CD  1 
ATOM   5759  C  CD  B GLU B 1 380 ? 38.168  24.760  66.912  0.41 34.92  ? 381 GLU B CD  1 
ATOM   5760  O  OE1 A GLU B 1 380 ? 37.783  24.894  64.732  0.59 48.33  ? 381 GLU B OE1 1 
ATOM   5761  O  OE1 B GLU B 1 380 ? 37.189  25.415  66.495  0.41 34.60  ? 381 GLU B OE1 1 
ATOM   5762  O  OE2 A GLU B 1 380 ? 35.625  25.107  64.384  0.59 33.54  ? 381 GLU B OE2 1 
ATOM   5763  O  OE2 B GLU B 1 380 ? 38.991  25.219  67.731  0.41 35.78  ? 381 GLU B OE2 1 
ATOM   5764  N  N   . ALA B 1 381 ? 34.865  20.524  67.149  1.00 33.52  ? 382 ALA B N   1 
ATOM   5765  C  CA  . ALA B 1 381 ? 33.673  19.730  66.869  1.00 30.48  ? 382 ALA B CA  1 
ATOM   5766  C  C   . ALA B 1 381 ? 32.565  20.026  67.868  1.00 30.18  ? 382 ALA B C   1 
ATOM   5767  O  O   . ALA B 1 381 ? 31.425  20.245  67.481  1.00 29.77  ? 382 ALA B O   1 
ATOM   5768  C  CB  . ALA B 1 381 ? 34.003  18.246  66.875  1.00 30.26  ? 382 ALA B CB  1 
ATOM   5769  N  N   . LYS B 1 382 ? 32.905  20.034  69.152  1.00 30.50  ? 383 LYS B N   1 
ATOM   5770  C  CA  . LYS B 1 382 ? 31.933  20.316  70.201  1.00 30.42  ? 383 LYS B CA  1 
ATOM   5771  C  C   . LYS B 1 382 ? 31.350  21.719  70.060  1.00 38.62  ? 383 LYS B C   1 
ATOM   5772  O  O   . LYS B 1 382 ? 30.137  21.906  70.191  1.00 36.19  ? 383 LYS B O   1 
ATOM   5773  C  CB  . LYS B 1 382 ? 32.563  20.150  71.585  1.00 30.98  ? 383 LYS B CB  1 
ATOM   5774  C  CG  . LYS B 1 382 ? 32.716  18.709  72.035  1.00 41.12  ? 383 LYS B CG  1 
ATOM   5775  C  CD  . LYS B 1 382 ? 33.073  18.633  73.511  1.00 44.84  ? 383 LYS B CD  1 
ATOM   5776  C  CE  . LYS B 1 382 ? 33.171  17.191  73.983  1.00 40.01  ? 383 LYS B CE  1 
ATOM   5777  N  NZ  . LYS B 1 382 ? 33.498  17.104  75.434  1.00 32.20  ? 383 LYS B NZ  1 
ATOM   5778  N  N   . ALA B 1 383 ? 32.205  22.702  69.790  1.00 31.17  ? 384 ALA B N   1 
ATOM   5779  C  CA  . ALA B 1 383 ? 31.722  24.072  69.612  1.00 43.49  ? 384 ALA B CA  1 
ATOM   5780  C  C   . ALA B 1 383 ? 30.769  24.181  68.417  1.00 41.36  ? 384 ALA B C   1 
ATOM   5781  O  O   . ALA B 1 383 ? 29.672  24.750  68.521  1.00 45.82  ? 384 ALA B O   1 
ATOM   5782  C  CB  . ALA B 1 383 ? 32.893  25.029  69.445  1.00 32.33  ? 384 ALA B CB  1 
ATOM   5783  N  N   . GLN B 1 384 ? 31.192  23.617  67.290  1.00 39.49  ? 385 GLN B N   1 
ATOM   5784  C  CA  . GLN B 1 384 ? 30.434  23.691  66.045  1.00 40.67  ? 385 GLN B CA  1 
ATOM   5785  C  C   . GLN B 1 384 ? 29.106  22.935  66.122  1.00 42.81  ? 385 GLN B C   1 
ATOM   5786  O  O   . GLN B 1 384 ? 28.111  23.356  65.532  1.00 29.46  ? 385 GLN B O   1 
ATOM   5787  C  CB  . GLN B 1 384 ? 31.274  23.154  64.885  1.00 46.27  ? 385 GLN B CB  1 
ATOM   5788  C  CG  . GLN B 1 384 ? 32.478  24.010  64.523  1.00 57.71  ? 385 GLN B CG  1 
ATOM   5789  C  CD  . GLN B 1 384 ? 32.090  25.368  63.977  1.00 65.94  ? 385 GLN B CD  1 
ATOM   5790  O  OE1 . GLN B 1 384 ? 31.481  25.470  62.912  1.00 65.72  ? 385 GLN B OE1 1 
ATOM   5791  N  NE2 . GLN B 1 384 ? 32.444  26.422  64.704  1.00 73.85  ? 385 GLN B NE2 1 
ATOM   5792  N  N   . LEU B 1 385 ? 29.093  21.819  66.844  1.00 34.75  ? 386 LEU B N   1 
ATOM   5793  C  CA  . LEU B 1 385 ? 27.870  21.045  67.036  1.00 36.98  ? 386 LEU B CA  1 
ATOM   5794  C  C   . LEU B 1 385 ? 26.942  21.755  68.013  1.00 35.51  ? 386 LEU B C   1 
ATOM   5795  O  O   . LEU B 1 385 ? 25.719  21.701  67.878  1.00 29.66  ? 386 LEU B O   1 
ATOM   5796  C  CB  . LEU B 1 385 ? 28.179  19.634  67.544  1.00 39.59  ? 386 LEU B CB  1 
ATOM   5797  C  CG  . LEU B 1 385 ? 28.914  18.644  66.634  1.00 32.46  ? 386 LEU B CG  1 
ATOM   5798  C  CD1 . LEU B 1 385 ? 29.066  17.305  67.334  1.00 32.27  ? 386 LEU B CD1 1 
ATOM   5799  C  CD2 . LEU B 1 385 ? 28.204  18.477  65.301  1.00 40.19  ? 386 LEU B CD2 1 
ATOM   5800  N  N   . ARG B 1 386 ? 27.532  22.417  69.004  1.00 37.49  ? 387 ARG B N   1 
ATOM   5801  C  CA  . ARG B 1 386 ? 26.753  23.165  69.982  1.00 43.36  ? 387 ARG B CA  1 
ATOM   5802  C  C   . ARG B 1 386 ? 26.070  24.359  69.328  1.00 41.60  ? 387 ARG B C   1 
ATOM   5803  O  O   . ARG B 1 386 ? 24.940  24.705  69.675  1.00 36.52  ? 387 ARG B O   1 
ATOM   5804  C  CB  . ARG B 1 386 ? 27.640  23.635  71.137  1.00 41.03  ? 387 ARG B CB  1 
ATOM   5805  N  N   . ASP B 1 387 ? 26.757  24.981  68.374  1.00 41.38  ? 388 ASP B N   1 
ATOM   5806  C  CA  . ASP B 1 387 ? 26.219  26.161  67.702  1.00 44.70  ? 388 ASP B CA  1 
ATOM   5807  C  C   . ASP B 1 387 ? 24.970  25.859  66.867  1.00 39.73  ? 388 ASP B C   1 
ATOM   5808  O  O   . ASP B 1 387 ? 24.111  26.728  66.689  1.00 45.86  ? 388 ASP B O   1 
ATOM   5809  C  CB  . ASP B 1 387 ? 27.295  26.796  66.815  1.00 48.05  ? 388 ASP B CB  1 
ATOM   5810  C  CG  . ASP B 1 387 ? 26.815  28.062  66.130  1.00 55.03  ? 388 ASP B CG  1 
ATOM   5811  O  OD1 . ASP B 1 387 ? 26.526  29.053  66.835  1.00 58.88  ? 388 ASP B OD1 1 
ATOM   5812  O  OD2 . ASP B 1 387 ? 26.728  28.067  64.884  1.00 58.01  ? 388 ASP B OD2 1 
ATOM   5813  N  N   . VAL B 1 388 ? 24.861  24.628  66.371  1.00 35.30  ? 389 VAL B N   1 
ATOM   5814  C  CA  . VAL B 1 388 ? 23.811  24.283  65.413  1.00 28.76  ? 389 VAL B CA  1 
ATOM   5815  C  C   . VAL B 1 388 ? 22.746  23.324  65.950  1.00 36.28  ? 389 VAL B C   1 
ATOM   5816  O  O   . VAL B 1 388 ? 21.988  22.740  65.173  1.00 28.17  ? 389 VAL B O   1 
ATOM   5817  C  CB  . VAL B 1 388 ? 24.414  23.653  64.141  1.00 30.32  ? 389 VAL B CB  1 
ATOM   5818  C  CG1 . VAL B 1 388 ? 25.375  24.624  63.475  1.00 29.25  ? 389 VAL B CG1 1 
ATOM   5819  C  CG2 . VAL B 1 388 ? 25.113  22.341  64.475  1.00 28.50  ? 389 VAL B CG2 1 
ATOM   5820  N  N   . GLN B 1 389 ? 22.680  23.160  67.267  1.00 28.44  ? 390 GLN B N   1 
ATOM   5821  C  CA  . GLN B 1 389 ? 21.675  22.282  67.859  1.00 35.59  ? 390 GLN B CA  1 
ATOM   5822  C  C   . GLN B 1 389 ? 20.273  22.864  67.711  1.00 37.30  ? 390 GLN B C   1 
ATOM   5823  O  O   . GLN B 1 389 ? 19.283  22.132  67.692  1.00 31.93  ? 390 GLN B O   1 
ATOM   5824  C  CB  . GLN B 1 389 ? 21.976  22.030  69.338  1.00 41.07  ? 390 GLN B CB  1 
ATOM   5825  C  CG  . GLN B 1 389 ? 22.708  20.727  69.607  1.00 56.64  ? 390 GLN B CG  1 
ATOM   5826  C  CD  . GLN B 1 389 ? 22.290  20.083  70.914  1.00 66.14  ? 390 GLN B CD  1 
ATOM   5827  O  OE1 . GLN B 1 389 ? 21.751  20.745  71.801  1.00 72.13  ? 390 GLN B OE1 1 
ATOM   5828  N  NE2 . GLN B 1 389 ? 22.533  18.783  71.038  1.00 66.84  ? 390 GLN B NE2 1 
ATOM   5829  N  N   . ASP B 1 390 ? 20.202  24.186  67.602  1.00 34.43  ? 391 ASP B N   1 
ATOM   5830  C  CA  . ASP B 1 390 ? 18.933  24.901  67.539  1.00 30.53  ? 391 ASP B CA  1 
ATOM   5831  C  C   . ASP B 1 390 ? 18.526  25.227  66.107  1.00 34.21  ? 391 ASP B C   1 
ATOM   5832  O  O   . ASP B 1 390 ? 17.501  25.868  65.884  1.00 38.64  ? 391 ASP B O   1 
ATOM   5833  C  CB  . ASP B 1 390 ? 19.026  26.194  68.351  1.00 43.60  ? 391 ASP B CB  1 
ATOM   5834  C  CG  . ASP B 1 390 ? 20.224  27.040  67.954  1.00 53.38  ? 391 ASP B CG  1 
ATOM   5835  O  OD1 . ASP B 1 390 ? 20.942  26.643  67.011  1.00 61.19  ? 391 ASP B OD1 1 
ATOM   5836  O  OD2 . ASP B 1 390 ? 20.454  28.099  68.575  1.00 60.00  ? 391 ASP B OD2 1 
ATOM   5837  N  N   . PHE B 1 391 ? 19.344  24.785  65.152  1.00 28.50  ? 392 PHE B N   1 
ATOM   5838  C  CA  . PHE B 1 391 ? 19.213  25.145  63.737  1.00 34.78  ? 392 PHE B CA  1 
ATOM   5839  C  C   . PHE B 1 391 ? 17.773  25.188  63.217  1.00 36.88  ? 392 PHE B C   1 
ATOM   5840  O  O   . PHE B 1 391 ? 17.294  26.230  62.743  1.00 42.34  ? 392 PHE B O   1 
ATOM   5841  C  CB  . PHE B 1 391 ? 20.027  24.163  62.889  1.00 28.50  ? 392 PHE B CB  1 
ATOM   5842  C  CG  . PHE B 1 391 ? 20.087  24.518  61.431  1.00 28.80  ? 392 PHE B CG  1 
ATOM   5843  C  CD1 . PHE B 1 391 ? 20.949  25.504  60.980  1.00 29.20  ? 392 PHE B CD1 1 
ATOM   5844  C  CD2 . PHE B 1 391 ? 19.293  23.857  60.509  1.00 28.83  ? 392 PHE B CD2 1 
ATOM   5845  C  CE1 . PHE B 1 391 ? 21.012  25.829  59.639  1.00 29.63  ? 392 PHE B CE1 1 
ATOM   5846  C  CE2 . PHE B 1 391 ? 19.351  24.177  59.166  1.00 29.26  ? 392 PHE B CE2 1 
ATOM   5847  C  CZ  . PHE B 1 391 ? 20.211  25.164  58.731  1.00 29.67  ? 392 PHE B CZ  1 
ATOM   5848  N  N   . TRP B 1 392 ? 17.088  24.055  63.343  1.00 28.49  ? 393 TRP B N   1 
ATOM   5849  C  CA  . TRP B 1 392 ? 15.773  23.855  62.746  1.00 35.33  ? 393 TRP B CA  1 
ATOM   5850  C  C   . TRP B 1 392 ? 14.690  24.768  63.314  1.00 38.50  ? 393 TRP B C   1 
ATOM   5851  O  O   . TRP B 1 392 ? 13.711  25.071  62.632  1.00 44.50  ? 393 TRP B O   1 
ATOM   5852  C  CB  . TRP B 1 392 ? 15.354  22.392  62.903  1.00 28.52  ? 393 TRP B CB  1 
ATOM   5853  C  CG  . TRP B 1 392 ? 16.284  21.453  62.212  1.00 28.39  ? 393 TRP B CG  1 
ATOM   5854  C  CD1 . TRP B 1 392 ? 17.118  20.543  62.794  1.00 36.37  ? 393 TRP B CD1 1 
ATOM   5855  C  CD2 . TRP B 1 392 ? 16.499  21.349  60.800  1.00 34.78  ? 393 TRP B CD2 1 
ATOM   5856  N  NE1 . TRP B 1 392 ? 17.829  19.868  61.830  1.00 36.15  ? 393 TRP B NE1 1 
ATOM   5857  C  CE2 . TRP B 1 392 ? 17.468  20.347  60.597  1.00 35.69  ? 393 TRP B CE2 1 
ATOM   5858  C  CE3 . TRP B 1 392 ? 15.961  22.003  59.687  1.00 34.34  ? 393 TRP B CE3 1 
ATOM   5859  C  CZ2 . TRP B 1 392 ? 17.910  19.983  59.327  1.00 35.06  ? 393 TRP B CZ2 1 
ATOM   5860  C  CZ3 . TRP B 1 392 ? 16.401  21.641  58.428  1.00 36.74  ? 393 TRP B CZ3 1 
ATOM   5861  C  CH2 . TRP B 1 392 ? 17.365  20.640  58.258  1.00 36.35  ? 393 TRP B CH2 1 
ATOM   5862  N  N   . ILE B 1 393 ? 14.855  25.201  64.559  1.00 28.88  ? 394 ILE B N   1 
ATOM   5863  C  CA  . ILE B 1 393 ? 13.899  26.122  65.157  1.00 39.76  ? 394 ILE B CA  1 
ATOM   5864  C  C   . ILE B 1 393 ? 14.445  27.545  65.156  1.00 41.43  ? 394 ILE B C   1 
ATOM   5865  O  O   . ILE B 1 393 ? 13.706  28.502  65.383  1.00 44.35  ? 394 ILE B O   1 
ATOM   5866  C  CB  . ILE B 1 393 ? 13.537  25.723  66.598  1.00 39.53  ? 394 ILE B CB  1 
ATOM   5867  C  CG1 . ILE B 1 393 ? 14.764  25.823  67.503  1.00 29.21  ? 394 ILE B CG1 1 
ATOM   5868  C  CG2 . ILE B 1 393 ? 12.947  24.321  66.631  1.00 46.61  ? 394 ILE B CG2 1 
ATOM   5869  C  CD1 . ILE B 1 393 ? 14.442  25.696  68.971  1.00 29.51  ? 394 ILE B CD1 1 
ATOM   5870  N  N   . SER B 1 394 ? 15.743  27.679  64.899  1.00 39.24  ? 395 SER B N   1 
ATOM   5871  C  CA  . SER B 1 394 ? 16.381  28.988  64.865  1.00 34.12  ? 395 SER B CA  1 
ATOM   5872  C  C   . SER B 1 394 ? 16.240  29.630  63.493  1.00 32.47  ? 395 SER B C   1 
ATOM   5873  O  O   . SER B 1 394 ? 16.431  30.838  63.352  1.00 34.95  ? 395 SER B O   1 
ATOM   5874  C  CB  . SER B 1 394 ? 17.860  28.883  65.236  1.00 34.19  ? 395 SER B CB  1 
ATOM   5875  O  OG  . SER B 1 394 ? 18.615  28.374  64.150  1.00 35.01  ? 395 SER B OG  1 
ATOM   5876  N  N   . LEU B 1 395 ? 15.920  28.817  62.487  1.00 32.57  ? 396 LEU B N   1 
ATOM   5877  C  CA  . LEU B 1 395 ? 15.725  29.327  61.125  1.00 40.69  ? 396 LEU B CA  1 
ATOM   5878  C  C   . LEU B 1 395 ? 14.855  30.597  61.029  1.00 45.33  ? 396 LEU B C   1 
ATOM   5879  O  O   . LEU B 1 395 ? 15.278  31.569  60.410  1.00 52.45  ? 396 LEU B O   1 
ATOM   5880  C  CB  . LEU B 1 395 ? 15.135  28.233  60.223  1.00 46.93  ? 396 LEU B CB  1 
ATOM   5881  C  CG  . LEU B 1 395 ? 16.062  27.080  59.833  1.00 50.24  ? 396 LEU B CG  1 
ATOM   5882  C  CD1 . LEU B 1 395 ? 15.301  25.998  59.080  1.00 48.14  ? 396 LEU B CD1 1 
ATOM   5883  C  CD2 . LEU B 1 395 ? 17.225  27.597  59.002  1.00 50.16  ? 396 LEU B CD2 1 
ATOM   5884  N  N   . PRO B 1 396 ? 13.651  30.609  61.644  1.00 46.24  ? 397 PRO B N   1 
ATOM   5885  C  CA  . PRO B 1 396 ? 12.826  31.814  61.467  1.00 47.28  ? 397 PRO B CA  1 
ATOM   5886  C  C   . PRO B 1 396 ? 13.425  33.084  62.074  1.00 47.48  ? 397 PRO B C   1 
ATOM   5887  O  O   . PRO B 1 396 ? 13.430  34.116  61.407  1.00 47.18  ? 397 PRO B O   1 
ATOM   5888  C  CB  . PRO B 1 396 ? 11.517  31.453  62.181  1.00 44.51  ? 397 PRO B CB  1 
ATOM   5889  C  CG  . PRO B 1 396 ? 11.504  29.972  62.236  1.00 40.66  ? 397 PRO B CG  1 
ATOM   5890  C  CD  . PRO B 1 396 ? 12.933  29.580  62.416  1.00 45.64  ? 397 PRO B CD  1 
ATOM   5891  N  N   . GLY B 1 397 ? 13.906  33.011  63.312  1.00 48.41  ? 398 GLY B N   1 
ATOM   5892  C  CA  . GLY B 1 397 ? 14.502  34.164  63.965  1.00 45.67  ? 398 GLY B CA  1 
ATOM   5893  C  C   . GLY B 1 397 ? 15.687  34.688  63.178  1.00 45.87  ? 398 GLY B C   1 
ATOM   5894  O  O   . GLY B 1 397 ? 15.853  35.903  63.001  1.00 51.46  ? 398 GLY B O   1 
ATOM   5895  N  N   . THR B 1 398 ? 16.505  33.757  62.696  1.00 49.24  ? 399 THR B N   1 
ATOM   5896  C  CA  . THR B 1 398 ? 17.638  34.095  61.850  1.00 52.95  ? 399 THR B CA  1 
ATOM   5897  C  C   . THR B 1 398 ? 17.142  34.838  60.614  1.00 54.73  ? 399 THR B C   1 
ATOM   5898  O  O   . THR B 1 398 ? 17.366  36.035  60.489  1.00 57.62  ? 399 THR B O   1 
ATOM   5899  C  CB  . THR B 1 398 ? 18.437  32.839  61.438  1.00 54.32  ? 399 THR B CB  1 
ATOM   5900  O  OG1 . THR B 1 398 ? 19.122  32.315  62.582  1.00 56.80  ? 399 THR B OG1 1 
ATOM   5901  C  CG2 . THR B 1 398 ? 19.466  33.184  60.371  1.00 56.39  ? 399 THR B CG2 1 
ATOM   5902  N  N   . LEU B 1 399 ? 16.425  34.145  59.733  1.00 50.39  ? 400 LEU B N   1 
ATOM   5903  C  CA  . LEU B 1 399 ? 15.980  34.731  58.467  1.00 51.96  ? 400 LEU B CA  1 
ATOM   5904  C  C   . LEU B 1 399 ? 15.219  36.053  58.635  1.00 59.47  ? 400 LEU B C   1 
ATOM   5905  O  O   . LEU B 1 399 ? 15.241  36.904  57.745  1.00 56.79  ? 400 LEU B O   1 
ATOM   5906  C  CB  . LEU B 1 399 ? 15.109  33.732  57.703  1.00 49.28  ? 400 LEU B CB  1 
ATOM   5907  C  CG  . LEU B 1 399 ? 15.710  32.347  57.449  1.00 53.92  ? 400 LEU B CG  1 
ATOM   5908  C  CD1 . LEU B 1 399 ? 14.638  31.369  56.987  1.00 54.73  ? 400 LEU B CD1 1 
ATOM   5909  C  CD2 . LEU B 1 399 ? 16.857  32.410  56.454  1.00 52.25  ? 400 LEU B CD2 1 
ATOM   5910  N  N   . CYS B 1 400 ? 14.560  36.226  59.777  1.00 60.75  ? 401 CYS B N   1 
ATOM   5911  C  CA  . CYS B 1 400 ? 13.820  37.453  60.058  1.00 64.32  ? 401 CYS B CA  1 
ATOM   5912  C  C   . CYS B 1 400 ? 14.734  38.603  60.474  1.00 74.39  ? 401 CYS B C   1 
ATOM   5913  O  O   . CYS B 1 400 ? 14.812  39.619  59.782  1.00 80.26  ? 401 CYS B O   1 
ATOM   5914  C  CB  . CYS B 1 400 ? 12.776  37.214  61.152  1.00 64.15  ? 401 CYS B CB  1 
ATOM   5915  S  SG  . CYS B 1 400 ? 11.295  36.336  60.607  1.00 77.08  ? 401 CYS B SG  1 
ATOM   5916  N  N   . SER B 1 401 ? 15.411  38.441  61.610  1.00 78.12  ? 402 SER B N   1 
ATOM   5917  C  CA  . SER B 1 401 ? 16.234  39.509  62.180  1.00 82.19  ? 402 SER B CA  1 
ATOM   5918  C  C   . SER B 1 401 ? 17.358  39.905  61.247  1.00 87.82  ? 402 SER B C   1 
ATOM   5919  O  O   . SER B 1 401 ? 17.729  41.077  61.123  1.00 90.62  ? 402 SER B O   1 
ATOM   5920  C  CB  . SER B 1 401 ? 16.817  39.066  63.528  1.00 80.18  ? 402 SER B CB  1 
ATOM   5921  O  OG  . SER B 1 401 ? 17.955  38.232  63.349  1.00 79.46  ? 402 SER B OG  1 
ATOM   5922  N  N   . GLU B 1 402 ? 17.888  38.889  60.592  1.00 91.22  ? 403 GLU B N   1 
ATOM   5923  C  CA  . GLU B 1 402 ? 19.127  39.004  59.879  1.00 97.96  ? 403 GLU B CA  1 
ATOM   5924  C  C   . GLU B 1 402 ? 18.889  39.709  58.535  1.00 100.42 ? 403 GLU B C   1 
ATOM   5925  O  O   . GLU B 1 402 ? 19.790  40.362  58.028  1.00 104.40 ? 403 GLU B O   1 
ATOM   5926  C  CB  . GLU B 1 402 ? 19.718  37.611  59.720  1.00 100.30 ? 403 GLU B CB  1 
ATOM   5927  C  CG  . GLU B 1 402 ? 20.858  37.512  58.839  1.00 105.06 ? 403 GLU B CG  1 
ATOM   5928  C  CD  . GLU B 1 402 ? 20.388  37.096  57.477  1.00 109.18 ? 403 GLU B CD  1 
ATOM   5929  O  OE1 . GLU B 1 402 ? 19.921  35.923  57.292  1.00 110.75 ? 403 GLU B OE1 1 
ATOM   5930  O  OE2 . GLU B 1 402 ? 20.441  37.998  56.585  1.00 111.09 ? 403 GLU B OE2 1 
ATOM   5931  N  N   . LYS B 1 403 ? 17.664  39.599  58.000  1.00 100.82 ? 404 LYS B N   1 
ATOM   5932  C  CA  . LYS B 1 403 ? 17.200  40.178  56.707  1.00 98.90  ? 404 LYS B CA  1 
ATOM   5933  C  C   . LYS B 1 403 ? 16.063  41.219  56.816  1.00 95.12  ? 404 LYS B C   1 
ATOM   5934  O  O   . LYS B 1 403 ? 16.275  42.419  57.007  1.00 97.95  ? 404 LYS B O   1 
ATOM   5935  C  CB  . LYS B 1 403 ? 16.673  39.052  55.771  1.00 79.79  ? 404 LYS B CB  1 
ATOM   5936  C  CG  . LYS B 1 403 ? 17.585  38.093  54.921  1.00 104.36 ? 404 LYS B CG  1 
ATOM   5937  C  CD  . LYS B 1 403 ? 18.479  38.777  53.874  1.00 106.19 ? 404 LYS B CD  1 
ATOM   5938  C  CE  . LYS B 1 403 ? 19.727  37.948  53.610  1.00 105.86 ? 404 LYS B CE  1 
ATOM   5939  N  NZ  . LYS B 1 403 ? 19.416  36.470  53.376  1.00 104.45 ? 404 LYS B NZ  1 
ATOM   5940  N  N   . MET B 1 404 ? 14.846  40.693  56.684  1.00 91.48  ? 405 MET B N   1 
ATOM   5941  C  CA  . MET B 1 404 ? 13.629  41.430  56.332  1.00 89.04  ? 405 MET B CA  1 
ATOM   5942  C  C   . MET B 1 404 ? 13.112  42.419  57.380  1.00 92.18  ? 405 MET B C   1 
ATOM   5943  O  O   . MET B 1 404 ? 12.704  43.534  57.048  1.00 92.47  ? 405 MET B O   1 
ATOM   5944  C  CB  . MET B 1 404 ? 12.522  40.411  56.043  1.00 86.55  ? 405 MET B CB  1 
ATOM   5945  C  CG  . MET B 1 404 ? 13.075  39.051  55.662  1.00 85.32  ? 405 MET B CG  1 
ATOM   5946  S  SD  . MET B 1 404 ? 11.970  37.710  56.130  1.00 103.37 ? 405 MET B SD  1 
ATOM   5947  C  CE  . MET B 1 404 ? 12.820  36.297  55.431  1.00 63.67  ? 405 MET B CE  1 
ATOM   5948  N  N   . ALA B 1 405 ? 13.122  42.000  58.642  1.00 87.81  ? 406 ALA B N   1 
ATOM   5949  C  CA  . ALA B 1 405 ? 12.298  42.636  59.669  1.00 88.58  ? 406 ALA B CA  1 
ATOM   5950  C  C   . ALA B 1 405 ? 12.776  44.023  60.106  1.00 91.28  ? 406 ALA B C   1 
ATOM   5951  O  O   . ALA B 1 405 ? 13.784  44.534  59.619  1.00 93.11  ? 406 ALA B O   1 
ATOM   5952  C  CB  . ALA B 1 405 ? 12.205  41.719  60.882  1.00 82.00  ? 406 ALA B CB  1 
ATOM   5953  N  N   . LEU B 1 406 ? 12.024  44.619  61.030  1.00 96.91  ? 407 LEU B N   1 
ATOM   5954  C  CA  . LEU B 1 406 ? 12.346  45.923  61.606  1.00 99.72  ? 407 LEU B CA  1 
ATOM   5955  C  C   . LEU B 1 406 ? 13.244  45.788  62.833  1.00 102.84 ? 407 LEU B C   1 
ATOM   5956  O  O   . LEU B 1 406 ? 13.741  44.703  63.136  1.00 102.92 ? 407 LEU B O   1 
ATOM   5957  C  CB  . LEU B 1 406 ? 11.063  46.677  61.976  1.00 100.45 ? 407 LEU B CB  1 
ATOM   5958  C  CG  . LEU B 1 406 ? 11.018  48.182  61.685  1.00 103.74 ? 407 LEU B CG  1 
ATOM   5959  C  CD1 . LEU B 1 406 ? 10.822  48.475  60.181  1.00 104.46 ? 407 LEU B CD1 1 
ATOM   5960  C  CD2 . LEU B 1 406 ? 9.957   48.882  62.556  1.00 103.66 ? 407 LEU B CD2 1 
ATOM   5961  N  N   . ASP B 1 412 ? 9.315   52.783  64.766  1.00 136.05 ? 413 ASP B N   1 
ATOM   5962  C  CA  . ASP B 1 412 ? 8.798   51.703  65.585  1.00 136.39 ? 413 ASP B CA  1 
ATOM   5963  C  C   . ASP B 1 412 ? 7.398   51.231  65.095  1.00 114.46 ? 413 ASP B C   1 
ATOM   5964  O  O   . ASP B 1 412 ? 6.803   50.302  65.655  1.00 117.37 ? 413 ASP B O   1 
ATOM   5965  C  CB  . ASP B 1 412 ? 8.882   52.135  67.056  1.00 138.15 ? 413 ASP B CB  1 
ATOM   5966  C  CG  . ASP B 1 412 ? 7.823   53.128  67.476  1.00 141.29 ? 413 ASP B CG  1 
ATOM   5967  O  OD1 . ASP B 1 412 ? 6.673   53.079  66.976  1.00 141.99 ? 413 ASP B OD1 1 
ATOM   5968  O  OD2 . ASP B 1 412 ? 8.205   54.034  68.284  1.00 143.20 ? 413 ASP B OD2 1 
ATOM   5969  N  N   . ARG B 1 413 ? 6.923   51.787  63.983  1.00 107.84 ? 414 ARG B N   1 
ATOM   5970  C  CA  . ARG B 1 413 ? 5.705   51.256  63.389  1.00 93.60  ? 414 ARG B CA  1 
ATOM   5971  C  C   . ARG B 1 413 ? 6.104   50.562  62.106  1.00 80.90  ? 414 ARG B C   1 
ATOM   5972  O  O   . ARG B 1 413 ? 6.900   51.071  61.322  1.00 81.53  ? 414 ARG B O   1 
ATOM   5973  C  CB  . ARG B 1 413 ? 4.662   52.351  63.192  1.00 91.64  ? 414 ARG B CB  1 
ATOM   5974  C  CG  . ARG B 1 413 ? 3.977   52.721  64.505  1.00 89.15  ? 414 ARG B CG  1 
ATOM   5975  C  CD  . ARG B 1 413 ? 3.441   51.462  65.178  1.00 81.57  ? 414 ARG B CD  1 
ATOM   5976  N  NE  . ARG B 1 413 ? 2.924   51.678  66.526  1.00 81.34  ? 414 ARG B NE  1 
ATOM   5977  C  CZ  . ARG B 1 413 ? 3.604   51.429  67.640  1.00 79.99  ? 414 ARG B CZ  1 
ATOM   5978  N  NH1 . ARG B 1 413 ? 4.842   50.958  67.576  1.00 77.50  ? 414 ARG B NH1 1 
ATOM   5979  N  NH2 . ARG B 1 413 ? 3.043   51.652  68.821  1.00 80.50  ? 414 ARG B NH2 1 
ATOM   5980  N  N   . CYS B 1 414 ? 5.576   49.359  61.947  1.00 68.85  ? 415 CYS B N   1 
ATOM   5981  C  CA  . CYS B 1 414 ? 6.074   48.398  60.982  1.00 56.32  ? 415 CYS B CA  1 
ATOM   5982  C  C   . CYS B 1 414 ? 4.904   47.826  60.219  1.00 52.94  ? 415 CYS B C   1 
ATOM   5983  O  O   . CYS B 1 414 ? 3.746   48.061  60.572  1.00 50.89  ? 415 CYS B O   1 
ATOM   5984  C  CB  . CYS B 1 414 ? 6.877   47.297  61.684  1.00 50.73  ? 415 CYS B CB  1 
ATOM   5985  S  SG  . CYS B 1 414 ? 6.143   46.760  63.247  1.00 56.09  ? 415 CYS B SG  1 
ATOM   5986  N  N   . TRP B 1 415 ? 5.207   47.097  59.157  1.00 42.63  ? 416 TRP B N   1 
ATOM   5987  C  CA  . TRP B 1 415 ? 4.169   46.546  58.315  1.00 46.76  ? 416 TRP B CA  1 
ATOM   5988  C  C   . TRP B 1 415 ? 3.576   45.309  58.978  1.00 45.08  ? 416 TRP B C   1 
ATOM   5989  O  O   . TRP B 1 415 ? 4.274   44.322  59.213  1.00 46.15  ? 416 TRP B O   1 
ATOM   5990  C  CB  . TRP B 1 415 ? 4.758   46.209  56.947  1.00 42.49  ? 416 TRP B CB  1 
ATOM   5991  C  CG  . TRP B 1 415 ? 3.868   45.411  56.073  1.00 41.65  ? 416 TRP B CG  1 
ATOM   5992  C  CD1 . TRP B 1 415 ? 3.997   44.090  55.759  1.00 42.76  ? 416 TRP B CD1 1 
ATOM   5993  C  CD2 . TRP B 1 415 ? 2.708   45.878  55.382  1.00 50.59  ? 416 TRP B CD2 1 
ATOM   5994  N  NE1 . TRP B 1 415 ? 2.985   43.705  54.916  1.00 47.73  ? 416 TRP B NE1 1 
ATOM   5995  C  CE2 . TRP B 1 415 ? 2.180   44.785  54.668  1.00 49.26  ? 416 TRP B CE2 1 
ATOM   5996  C  CE3 . TRP B 1 415 ? 2.063   47.116  55.297  1.00 47.42  ? 416 TRP B CE3 1 
ATOM   5997  C  CZ2 . TRP B 1 415 ? 1.036   44.892  53.882  1.00 48.88  ? 416 TRP B CZ2 1 
ATOM   5998  C  CZ3 . TRP B 1 415 ? 0.930   47.220  54.516  1.00 46.36  ? 416 TRP B CZ3 1 
ATOM   5999  C  CH2 . TRP B 1 415 ? 0.427   46.114  53.819  1.00 46.68  ? 416 TRP B CH2 1 
ATOM   6000  N  N   . ASN B 1 416 ? 2.283   45.379  59.290  1.00 40.96  ? 417 ASN B N   1 
ATOM   6001  C  CA  . ASN B 1 416 ? 1.581   44.277  59.941  1.00 40.28  ? 417 ASN B CA  1 
ATOM   6002  C  C   . ASN B 1 416 ? 0.783   43.396  58.983  1.00 42.74  ? 417 ASN B C   1 
ATOM   6003  O  O   . ASN B 1 416 ? 0.124   42.450  59.408  1.00 39.78  ? 417 ASN B O   1 
ATOM   6004  C  CB  . ASN B 1 416 ? 0.663   44.815  61.047  1.00 47.25  ? 417 ASN B CB  1 
ATOM   6005  C  CG  . ASN B 1 416 ? -0.354  45.825  60.540  1.00 48.39  ? 417 ASN B CG  1 
ATOM   6006  O  OD1 . ASN B 1 416 ? -0.722  45.830  59.365  1.00 42.20  ? 417 ASN B OD1 1 
ATOM   6007  N  ND2 . ASN B 1 416 ? -0.817  46.687  61.437  1.00 51.79  ? 417 ASN B ND2 1 
ATOM   6008  N  N   . GLY B 1 417 ? 0.835   43.717  57.694  1.00 42.58  ? 418 GLY B N   1 
ATOM   6009  C  CA  . GLY B 1 417 ? 0.056   42.999  56.702  1.00 40.92  ? 418 GLY B CA  1 
ATOM   6010  C  C   . GLY B 1 417 ? -1.147  43.792  56.224  1.00 53.18  ? 418 GLY B C   1 
ATOM   6011  O  O   . GLY B 1 417 ? -1.714  43.500  55.171  1.00 52.99  ? 418 GLY B O   1 
ATOM   6012  N  N   . MET B 1 418 ? -1.536  44.799  57.000  1.00 55.30  ? 419 MET B N   1 
ATOM   6013  C  CA  . MET B 1 418 ? -2.607  45.711  56.609  1.00 58.64  ? 419 MET B CA  1 
ATOM   6014  C  C   . MET B 1 418 ? -2.037  47.084  56.270  1.00 61.82  ? 419 MET B C   1 
ATOM   6015  O  O   . MET B 1 418 ? -2.137  47.547  55.134  1.00 61.15  ? 419 MET B O   1 
ATOM   6016  C  CB  . MET B 1 418 ? -3.658  45.831  57.714  1.00 61.04  ? 419 MET B CB  1 
ATOM   6017  C  CG  . MET B 1 418 ? -4.593  44.638  57.818  1.00 62.87  ? 419 MET B CG  1 
ATOM   6018  S  SD  . MET B 1 418 ? -6.150  45.054  58.626  1.00 120.66 ? 419 MET B SD  1 
ATOM   6019  C  CE  . MET B 1 418 ? -7.003  43.481  58.550  1.00 57.01  ? 419 MET B CE  1 
ATOM   6020  N  N   . ALA B 1 419 ? -1.454  47.736  57.270  1.00 58.66  ? 420 ALA B N   1 
ATOM   6021  C  CA  . ALA B 1 419 ? -0.805  49.027  57.074  1.00 54.73  ? 420 ALA B CA  1 
ATOM   6022  C  C   . ALA B 1 419 ? 0.417   49.151  57.975  1.00 58.55  ? 420 ALA B C   1 
ATOM   6023  O  O   . ALA B 1 419 ? 0.758   48.216  58.703  1.00 55.62  ? 420 ALA B O   1 
ATOM   6024  C  CB  . ALA B 1 419 ? -1.780  50.158  57.345  1.00 57.81  ? 420 ALA B CB  1 
ATOM   6025  N  N   . ARG B 1 420 ? 1.083   50.301  57.916  1.00 52.38  ? 421 ARG B N   1 
ATOM   6026  C  CA  . ARG B 1 420 ? 2.159   50.592  58.853  1.00 51.75  ? 421 ARG B CA  1 
ATOM   6027  C  C   . ARG B 1 420 ? 1.555   50.717  60.241  1.00 51.15  ? 421 ARG B C   1 
ATOM   6028  O  O   . ARG B 1 420 ? 0.520   51.360  60.414  1.00 56.50  ? 421 ARG B O   1 
ATOM   6029  C  CB  . ARG B 1 420 ? 2.903   51.871  58.468  1.00 58.91  ? 421 ARG B CB  1 
ATOM   6030  C  CG  . ARG B 1 420 ? 3.515   51.842  57.080  1.00 62.64  ? 421 ARG B CG  1 
ATOM   6031  C  CD  . ARG B 1 420 ? 4.442   53.027  56.864  1.00 64.96  ? 421 ARG B CD  1 
ATOM   6032  N  NE  . ARG B 1 420 ? 5.571   53.007  57.789  1.00 66.85  ? 421 ARG B NE  1 
ATOM   6033  C  CZ  . ARG B 1 420 ? 6.813   53.345  57.458  1.00 70.57  ? 421 ARG B CZ  1 
ATOM   6034  N  NH1 . ARG B 1 420 ? 7.089   53.731  56.220  1.00 71.33  ? 421 ARG B NH1 1 
ATOM   6035  N  NH2 . ARG B 1 420 ? 7.780   53.296  58.364  1.00 70.10  ? 421 ARG B NH2 1 
ATOM   6036  N  N   . GLY B 1 421 ? 2.188   50.100  61.231  1.00 55.90  ? 422 GLY B N   1 
ATOM   6037  C  CA  . GLY B 1 421 ? 1.591   50.051  62.550  1.00 58.75  ? 422 GLY B CA  1 
ATOM   6038  C  C   . GLY B 1 421 ? 2.040   48.905  63.434  1.00 56.05  ? 422 GLY B C   1 
ATOM   6039  O  O   . GLY B 1 421 ? 3.140   48.373  63.294  1.00 49.88  ? 422 GLY B O   1 
ATOM   6040  N  N   . ARG B 1 422 ? 1.169   48.552  64.372  1.00 55.48  ? 423 ARG B N   1 
ATOM   6041  C  CA  . ARG B 1 422 ? 1.436   47.535  65.379  1.00 53.09  ? 423 ARG B CA  1 
ATOM   6042  C  C   . ARG B 1 422 ? 0.935   46.162  64.932  1.00 51.03  ? 423 ARG B C   1 
ATOM   6043  O  O   . ARG B 1 422 ? -0.104  46.059  64.279  1.00 44.24  ? 423 ARG B O   1 
ATOM   6044  C  CB  . ARG B 1 422 ? 0.774   47.942  66.698  1.00 52.57  ? 423 ARG B CB  1 
ATOM   6045  C  CG  . ARG B 1 422 ? 1.084   47.063  67.891  1.00 54.28  ? 423 ARG B CG  1 
ATOM   6046  C  CD  . ARG B 1 422 ? 0.351   47.578  69.123  1.00 54.65  ? 423 ARG B CD  1 
ATOM   6047  N  NE  . ARG B 1 422 ? -1.072  47.780  68.859  1.00 55.69  ? 423 ARG B NE  1 
ATOM   6048  C  CZ  . ARG B 1 422 ? -1.971  48.095  69.787  1.00 54.27  ? 423 ARG B CZ  1 
ATOM   6049  N  NH1 . ARG B 1 422 ? -1.598  48.252  71.050  1.00 51.24  ? 423 ARG B NH1 1 
ATOM   6050  N  NH2 . ARG B 1 422 ? -3.244  48.256  69.451  1.00 54.95  ? 423 ARG B NH2 1 
ATOM   6051  N  N   . TYR B 1 423 ? 1.677   45.111  65.270  1.00 49.60  ? 424 TYR B N   1 
ATOM   6052  C  CA  . TYR B 1 423 ? 1.230   43.753  64.973  1.00 46.32  ? 424 TYR B CA  1 
ATOM   6053  C  C   . TYR B 1 423 ? 0.672   43.103  66.233  1.00 39.64  ? 424 TYR B C   1 
ATOM   6054  O  O   . TYR B 1 423 ? 1.415   42.771  67.158  1.00 47.07  ? 424 TYR B O   1 
ATOM   6055  C  CB  . TYR B 1 423 ? 2.379   42.919  64.402  1.00 42.50  ? 424 TYR B CB  1 
ATOM   6056  C  CG  . TYR B 1 423 ? 1.994   41.511  64.000  1.00 48.29  ? 424 TYR B CG  1 
ATOM   6057  C  CD1 . TYR B 1 423 ? 1.306   41.270  62.817  1.00 47.53  ? 424 TYR B CD1 1 
ATOM   6058  C  CD2 . TYR B 1 423 ? 2.329   40.422  64.796  1.00 43.73  ? 424 TYR B CD2 1 
ATOM   6059  C  CE1 . TYR B 1 423 ? 0.955   39.986  62.443  1.00 42.63  ? 424 TYR B CE1 1 
ATOM   6060  C  CE2 . TYR B 1 423 ? 1.983   39.133  64.428  1.00 37.39  ? 424 TYR B CE2 1 
ATOM   6061  C  CZ  . TYR B 1 423 ? 1.296   38.923  63.251  1.00 40.11  ? 424 TYR B CZ  1 
ATOM   6062  O  OH  . TYR B 1 423 ? 0.947   37.646  62.880  1.00 36.62  ? 424 TYR B OH  1 
ATOM   6063  N  N   . LEU B 1 424 ? -0.646  42.934  66.257  1.00 40.08  ? 425 LEU B N   1 
ATOM   6064  C  CA  . LEU B 1 424 ? -1.349  42.360  67.405  1.00 49.48  ? 425 LEU B CA  1 
ATOM   6065  C  C   . LEU B 1 424 ? -1.122  40.861  67.680  1.00 46.99  ? 425 LEU B C   1 
ATOM   6066  O  O   . LEU B 1 424 ? -0.786  40.502  68.809  1.00 39.37  ? 425 LEU B O   1 
ATOM   6067  C  CB  . LEU B 1 424 ? -2.853  42.617  67.265  1.00 41.11  ? 425 LEU B CB  1 
ATOM   6068  C  CG  . LEU B 1 424 ? -3.293  44.082  67.277  1.00 56.67  ? 425 LEU B CG  1 
ATOM   6069  C  CD1 . LEU B 1 424 ? -4.807  44.178  67.370  1.00 58.44  ? 425 LEU B CD1 1 
ATOM   6070  C  CD2 . LEU B 1 424 ? -2.631  44.837  68.418  1.00 59.20  ? 425 LEU B CD2 1 
ATOM   6071  N  N   . PRO B 1 425 ? -1.312  39.984  66.667  1.00 38.91  ? 426 PRO B N   1 
ATOM   6072  C  CA  . PRO B 1 425 ? -1.369  38.545  66.974  1.00 47.36  ? 426 PRO B CA  1 
ATOM   6073  C  C   . PRO B 1 425 ? -0.113  37.993  67.642  1.00 45.32  ? 426 PRO B C   1 
ATOM   6074  O  O   . PRO B 1 425 ? 1.002   38.401  67.319  1.00 37.23  ? 426 PRO B O   1 
ATOM   6075  C  CB  . PRO B 1 425 ? -1.564  37.899  65.596  1.00 38.02  ? 426 PRO B CB  1 
ATOM   6076  C  CG  . PRO B 1 425 ? -2.122  38.977  64.741  1.00 48.98  ? 426 PRO B CG  1 
ATOM   6077  C  CD  . PRO B 1 425 ? -1.455  40.223  65.219  1.00 38.92  ? 426 PRO B CD  1 
ATOM   6078  N  N   . GLU B 1 426 ? -0.309  37.068  68.575  1.00 48.83  ? 427 GLU B N   1 
ATOM   6079  C  CA  . GLU B 1 426 ? 0.796   36.462  69.306  1.00 49.03  ? 427 GLU B CA  1 
ATOM   6080  C  C   . GLU B 1 426 ? 1.588   35.517  68.410  1.00 36.06  ? 427 GLU B C   1 
ATOM   6081  O  O   . GLU B 1 426 ? 1.076   35.025  67.405  1.00 35.92  ? 427 GLU B O   1 
ATOM   6082  C  CB  . GLU B 1 426 ? 0.274   35.718  70.536  1.00 55.94  ? 427 GLU B CB  1 
ATOM   6083  C  CG  . GLU B 1 426 ? 1.151   35.865  71.769  1.00 60.26  ? 427 GLU B CG  1 
ATOM   6084  C  CD  . GLU B 1 426 ? 0.405   35.565  73.053  1.00 64.76  ? 427 GLU B CD  1 
ATOM   6085  O  OE1 . GLU B 1 426 ? 0.652   34.497  73.653  1.00 65.44  ? 427 GLU B OE1 1 
ATOM   6086  O  OE2 . GLU B 1 426 ? -0.433  36.397  73.462  1.00 66.75  ? 427 GLU B OE2 1 
ATOM   6087  N  N   . VAL B 1 427 ? 2.842   35.274  68.775  1.00 40.37  ? 428 VAL B N   1 
ATOM   6088  C  CA  . VAL B 1 427 ? 3.699   34.378  68.011  1.00 41.63  ? 428 VAL B CA  1 
ATOM   6089  C  C   . VAL B 1 427 ? 3.383   32.921  68.334  1.00 34.40  ? 428 VAL B C   1 
ATOM   6090  O  O   . VAL B 1 427 ? 3.231   32.552  69.498  1.00 34.67  ? 428 VAL B O   1 
ATOM   6091  C  CB  . VAL B 1 427 ? 5.191   34.650  68.286  1.00 47.66  ? 428 VAL B CB  1 
ATOM   6092  C  CG1 . VAL B 1 427 ? 6.065   33.803  67.374  1.00 48.75  ? 428 VAL B CG1 1 
ATOM   6093  C  CG2 . VAL B 1 427 ? 5.501   36.124  68.095  1.00 47.66  ? 428 VAL B CG2 1 
ATOM   6094  N  N   . MET B 1 428 ? 3.279   32.099  67.296  1.00 36.39  ? 429 MET B N   1 
ATOM   6095  C  CA  . MET B 1 428 ? 2.986   30.681  67.462  1.00 40.06  ? 429 MET B CA  1 
ATOM   6096  C  C   . MET B 1 428 ? 4.185   29.923  68.017  1.00 40.57  ? 429 MET B C   1 
ATOM   6097  O  O   . MET B 1 428 ? 5.316   30.403  67.955  1.00 37.12  ? 429 MET B O   1 
ATOM   6098  C  CB  . MET B 1 428 ? 2.551   30.066  66.130  1.00 33.77  ? 429 MET B CB  1 
ATOM   6099  C  CG  . MET B 1 428 ? 1.307   30.696  65.516  1.00 41.29  ? 429 MET B CG  1 
ATOM   6100  S  SD  . MET B 1 428 ? -0.209  30.374  66.443  1.00 48.23  ? 429 MET B SD  1 
ATOM   6101  C  CE  . MET B 1 428 ? -0.344  31.852  67.448  1.00 53.69  ? 429 MET B CE  1 
ATOM   6102  N  N   . GLY B 1 429 ? 3.925   28.750  68.585  1.00 44.10  ? 430 GLY B N   1 
ATOM   6103  C  CA  . GLY B 1 429 ? 4.989   27.864  69.015  1.00 32.80  ? 430 GLY B CA  1 
ATOM   6104  C  C   . GLY B 1 429 ? 5.616   27.175  67.819  1.00 32.16  ? 430 GLY B C   1 
ATOM   6105  O  O   . GLY B 1 429 ? 5.105   27.268  66.703  1.00 32.22  ? 430 GLY B O   1 
ATOM   6106  N  N   . ASP B 1 430 ? 6.728   26.482  68.047  1.00 31.65  ? 431 ASP B N   1 
ATOM   6107  C  CA  . ASP B 1 430 ? 7.424   25.777  66.976  1.00 31.12  ? 431 ASP B CA  1 
ATOM   6108  C  C   . ASP B 1 430 ? 6.780   24.432  66.650  1.00 32.62  ? 431 ASP B C   1 
ATOM   6109  O  O   . ASP B 1 430 ? 6.201   23.782  67.519  1.00 31.64  ? 431 ASP B O   1 
ATOM   6110  C  CB  . ASP B 1 430 ? 8.894   25.570  67.342  1.00 37.21  ? 431 ASP B CB  1 
ATOM   6111  C  CG  . ASP B 1 430 ? 9.639   26.878  67.516  1.00 46.66  ? 431 ASP B CG  1 
ATOM   6112  O  OD1 . ASP B 1 430 ? 9.996   27.498  66.493  1.00 53.42  ? 431 ASP B OD1 1 
ATOM   6113  O  OD2 . ASP B 1 430 ? 9.871   27.284  68.674  1.00 46.17  ? 431 ASP B OD2 1 
ATOM   6114  N  N   . GLY B 1 431 ? 6.884   24.023  65.390  1.00 31.09  ? 432 GLY B N   1 
ATOM   6115  C  CA  . GLY B 1 431 ? 6.420   22.713  64.973  1.00 32.10  ? 432 GLY B CA  1 
ATOM   6116  C  C   . GLY B 1 431 ? 5.149   22.748  64.151  1.00 37.52  ? 432 GLY B C   1 
ATOM   6117  O  O   . GLY B 1 431 ? 4.464   23.768  64.096  1.00 36.30  ? 432 GLY B O   1 
ATOM   6118  N  N   . LEU B 1 432 ? 4.833   21.622  63.517  1.00 32.17  ? 433 LEU B N   1 
ATOM   6119  C  CA  . LEU B 1 432 ? 3.694   21.537  62.610  1.00 42.07  ? 433 LEU B CA  1 
ATOM   6120  C  C   . LEU B 1 432 ? 2.364   21.710  63.333  1.00 41.26  ? 433 LEU B C   1 
ATOM   6121  O  O   . LEU B 1 432 ? 1.516   22.488  62.903  1.00 43.35  ? 433 LEU B O   1 
ATOM   6122  C  CB  . LEU B 1 432 ? 3.706   20.201  61.864  1.00 33.13  ? 433 LEU B CB  1 
ATOM   6123  C  CG  . LEU B 1 432 ? 2.660   20.048  60.759  1.00 40.81  ? 433 LEU B CG  1 
ATOM   6124  C  CD1 . LEU B 1 432 ? 2.929   21.041  59.645  1.00 33.86  ? 433 LEU B CD1 1 
ATOM   6125  C  CD2 . LEU B 1 432 ? 2.645   18.626  60.218  1.00 34.38  ? 433 LEU B CD2 1 
ATOM   6126  N  N   . ALA B 1 433 ? 2.191   20.979  64.430  1.00 39.43  ? 434 ALA B N   1 
ATOM   6127  C  CA  . ALA B 1 433 ? 0.946   21.010  65.188  1.00 41.04  ? 434 ALA B CA  1 
ATOM   6128  C  C   . ALA B 1 433 ? 0.622   22.415  65.686  1.00 34.72  ? 434 ALA B C   1 
ATOM   6129  O  O   . ALA B 1 433 ? -0.537  22.825  65.693  1.00 35.48  ? 434 ALA B O   1 
ATOM   6130  C  CB  . ALA B 1 433 ? 1.017   20.040  66.357  1.00 34.91  ? 434 ALA B CB  1 
ATOM   6131  N  N   . ASN B 1 434 ? 1.652   23.153  66.086  1.00 33.99  ? 435 ASN B N   1 
ATOM   6132  C  CA  . ASN B 1 434 ? 1.465   24.487  66.647  1.00 34.10  ? 435 ASN B CA  1 
ATOM   6133  C  C   . ASN B 1 434 ? 0.962   25.529  65.646  1.00 34.27  ? 435 ASN B C   1 
ATOM   6134  O  O   . ASN B 1 434 ? 0.584   26.632  66.037  1.00 34.54  ? 435 ASN B O   1 
ATOM   6135  C  CB  . ASN B 1 434 ? 2.772   24.979  67.271  1.00 33.39  ? 435 ASN B CB  1 
ATOM   6136  C  CG  . ASN B 1 434 ? 2.940   24.521  68.705  1.00 45.63  ? 435 ASN B CG  1 
ATOM   6137  O  OD1 . ASN B 1 434 ? 1.966   24.192  69.381  1.00 34.37  ? 435 ASN B OD1 1 
ATOM   6138  N  ND2 . ASN B 1 434 ? 4.181   24.503  69.179  1.00 44.36  ? 435 ASN B ND2 1 
ATOM   6139  N  N   . GLN B 1 435 ? 0.951   25.185  64.363  1.00 34.21  ? 436 GLN B N   1 
ATOM   6140  C  CA  . GLN B 1 435 ? 0.545   26.141  63.340  1.00 34.46  ? 436 GLN B CA  1 
ATOM   6141  C  C   . GLN B 1 435 ? -0.897  25.946  62.886  1.00 41.60  ? 436 GLN B C   1 
ATOM   6142  O  O   . GLN B 1 435 ? -1.304  26.485  61.856  1.00 44.83  ? 436 GLN B O   1 
ATOM   6143  C  CB  . GLN B 1 435 ? 1.473   26.055  62.126  1.00 39.93  ? 436 GLN B CB  1 
ATOM   6144  C  CG  . GLN B 1 435 ? 2.953   25.947  62.460  1.00 40.44  ? 436 GLN B CG  1 
ATOM   6145  C  CD  . GLN B 1 435 ? 3.444   27.027  63.410  1.00 32.84  ? 436 GLN B CD  1 
ATOM   6146  O  OE1 . GLN B 1 435 ? 2.918   28.139  63.438  1.00 33.21  ? 436 GLN B OE1 1 
ATOM   6147  N  NE2 . GLN B 1 435 ? 4.465   26.699  64.193  1.00 32.30  ? 436 GLN B NE2 1 
ATOM   6148  N  N   . ILE B 1 436 ? -1.670  25.181  63.648  1.00 35.97  ? 437 ILE B N   1 
ATOM   6149  C  CA  . ILE B 1 436 ? -3.054  24.918  63.277  1.00 38.76  ? 437 ILE B CA  1 
ATOM   6150  C  C   . ILE B 1 436 ? -3.877  26.208  63.353  1.00 37.56  ? 437 ILE B C   1 
ATOM   6151  O  O   . ILE B 1 436 ? -4.733  26.461  62.502  1.00 38.25  ? 437 ILE B O   1 
ATOM   6152  C  CB  . ILE B 1 436 ? -3.680  23.811  64.168  1.00 38.43  ? 437 ILE B CB  1 
ATOM   6153  C  CG1 . ILE B 1 436 ? -5.127  23.534  63.753  1.00 38.90  ? 437 ILE B CG1 1 
ATOM   6154  C  CG2 . ILE B 1 436 ? -3.583  24.163  65.651  1.00 37.62  ? 437 ILE B CG2 1 
ATOM   6155  C  CD1 . ILE B 1 436 ? -5.683  22.250  64.324  1.00 48.83  ? 437 ILE B CD1 1 
ATOM   6156  N  N   . ASN B 1 437 ? -3.604  27.020  64.370  1.00 37.32  ? 438 ASN B N   1 
ATOM   6157  C  CA  . ASN B 1 437 ? -4.253  28.316  64.542  1.00 46.08  ? 438 ASN B CA  1 
ATOM   6158  C  C   . ASN B 1 437 ? -3.444  29.493  63.989  1.00 48.54  ? 438 ASN B C   1 
ATOM   6159  O  O   . ASN B 1 437 ? -3.818  30.648  64.192  1.00 49.31  ? 438 ASN B O   1 
ATOM   6160  C  CB  . ASN B 1 437 ? -4.579  28.551  66.017  1.00 48.74  ? 438 ASN B CB  1 
ATOM   6161  C  CG  . ASN B 1 437 ? -5.674  27.630  66.522  1.00 49.61  ? 438 ASN B CG  1 
ATOM   6162  O  OD1 . ASN B 1 437 ? -6.596  27.283  65.783  1.00 39.85  ? 438 ASN B OD1 1 
ATOM   6163  N  ND2 . ASN B 1 437 ? -5.579  27.230  67.785  1.00 51.02  ? 438 ASN B ND2 1 
ATOM   6164  N  N   . ASN B 1 438 ? -2.324  29.202  63.330  1.00 49.72  ? 439 ASN B N   1 
ATOM   6165  C  CA  . ASN B 1 438 ? -1.456  30.245  62.779  1.00 39.93  ? 439 ASN B CA  1 
ATOM   6166  C  C   . ASN B 1 438 ? -2.218  31.236  61.902  1.00 36.64  ? 439 ASN B C   1 
ATOM   6167  O  O   . ASN B 1 438 ? -2.861  30.846  60.927  1.00 37.13  ? 439 ASN B O   1 
ATOM   6168  C  CB  . ASN B 1 438 ? -0.321  29.616  61.966  1.00 35.26  ? 439 ASN B CB  1 
ATOM   6169  C  CG  . ASN B 1 438 ? 0.702   30.637  61.499  1.00 41.56  ? 439 ASN B CG  1 
ATOM   6170  O  OD1 . ASN B 1 438 ? 0.545   31.253  60.445  1.00 44.65  ? 439 ASN B OD1 1 
ATOM   6171  N  ND2 . ASN B 1 438 ? 1.768   30.802  62.270  1.00 34.25  ? 439 ASN B ND2 1 
ATOM   6172  N  N   . PRO B 1 439 ? -2.152  32.527  62.259  1.00 42.62  ? 440 PRO B N   1 
ATOM   6173  C  CA  . PRO B 1 439 ? -2.909  33.583  61.572  1.00 44.64  ? 440 PRO B CA  1 
ATOM   6174  C  C   . PRO B 1 439 ? -2.491  33.846  60.122  1.00 47.92  ? 440 PRO B C   1 
ATOM   6175  O  O   . PRO B 1 439 ? -3.364  34.045  59.278  1.00 52.08  ? 440 PRO B O   1 
ATOM   6176  C  CB  . PRO B 1 439 ? -2.639  34.821  62.435  1.00 37.57  ? 440 PRO B CB  1 
ATOM   6177  C  CG  . PRO B 1 439 ? -1.360  34.526  63.145  1.00 43.57  ? 440 PRO B CG  1 
ATOM   6178  C  CD  . PRO B 1 439 ? -1.372  33.051  63.394  1.00 36.36  ? 440 PRO B CD  1 
ATOM   6179  N  N   . GLU B 1 440 ? -1.192  33.863  59.837  1.00 39.25  ? 441 GLU B N   1 
ATOM   6180  C  CA  . GLU B 1 440 ? -0.731  34.279  58.512  1.00 41.27  ? 441 GLU B CA  1 
ATOM   6181  C  C   . GLU B 1 440 ? -0.626  33.159  57.480  1.00 36.99  ? 441 GLU B C   1 
ATOM   6182  O  O   . GLU B 1 440 ? -0.553  33.422  56.279  1.00 37.44  ? 441 GLU B O   1 
ATOM   6183  C  CB  . GLU B 1 440 ? 0.629   34.971  58.638  1.00 39.29  ? 441 GLU B CB  1 
ATOM   6184  C  CG  . GLU B 1 440 ? 0.755   35.889  59.848  1.00 36.43  ? 441 GLU B CG  1 
ATOM   6185  C  CD  . GLU B 1 440 ? -0.364  36.914  59.945  1.00 37.31  ? 441 GLU B CD  1 
ATOM   6186  O  OE1 . GLU B 1 440 ? -0.925  37.303  58.899  1.00 37.96  ? 441 GLU B OE1 1 
ATOM   6187  O  OE2 . GLU B 1 440 ? -0.686  37.328  61.078  1.00 39.04  ? 441 GLU B OE2 1 
ATOM   6188  N  N   . VAL B 1 441 ? -0.639  31.914  57.941  1.00 43.03  ? 442 VAL B N   1 
ATOM   6189  C  CA  . VAL B 1 441 ? -0.454  30.773  57.050  1.00 36.60  ? 442 VAL B CA  1 
ATOM   6190  C  C   . VAL B 1 441 ? -1.434  29.674  57.411  1.00 37.42  ? 442 VAL B C   1 
ATOM   6191  O  O   . VAL B 1 441 ? -1.509  29.269  58.571  1.00 36.59  ? 442 VAL B O   1 
ATOM   6192  C  CB  . VAL B 1 441 ? 0.979   30.186  57.126  1.00 35.70  ? 442 VAL B CB  1 
ATOM   6193  C  CG1 . VAL B 1 441 ? 1.219   29.220  55.972  1.00 36.08  ? 442 VAL B CG1 1 
ATOM   6194  C  CG2 . VAL B 1 441 ? 2.034   31.281  57.132  1.00 39.16  ? 442 VAL B CG2 1 
ATOM   6195  N  N   . GLU B 1 442 ? -2.180  29.178  56.431  1.00 41.88  ? 443 GLU B N   1 
ATOM   6196  C  CA  . GLU B 1 442 ? -3.031  28.030  56.699  1.00 49.36  ? 443 GLU B CA  1 
ATOM   6197  C  C   . GLU B 1 442 ? -2.229  26.754  56.517  1.00 45.77  ? 443 GLU B C   1 
ATOM   6198  O  O   . GLU B 1 442 ? -1.744  26.451  55.426  1.00 43.12  ? 443 GLU B O   1 
ATOM   6199  C  CB  . GLU B 1 442 ? -4.269  28.027  55.802  1.00 58.24  ? 443 GLU B CB  1 
ATOM   6200  C  CG  . GLU B 1 442 ? -5.487  28.626  56.485  1.00 71.05  ? 443 GLU B CG  1 
ATOM   6201  C  CD  . GLU B 1 442 ? -5.647  28.127  57.914  1.00 79.99  ? 443 GLU B CD  1 
ATOM   6202  O  OE1 . GLU B 1 442 ? -5.886  26.916  58.107  1.00 82.57  ? 443 GLU B OE1 1 
ATOM   6203  O  OE2 . GLU B 1 442 ? -5.525  28.947  58.849  1.00 81.42  ? 443 GLU B OE2 1 
ATOM   6204  N  N   . VAL B 1 443 ? -2.096  26.013  57.608  1.00 42.23  ? 444 VAL B N   1 
ATOM   6205  C  CA  . VAL B 1 443 ? -1.310  24.793  57.623  1.00 44.64  ? 444 VAL B CA  1 
ATOM   6206  C  C   . VAL B 1 443 ? -2.172  23.617  58.044  1.00 37.37  ? 444 VAL B C   1 
ATOM   6207  O  O   . VAL B 1 443 ? -2.794  23.644  59.106  1.00 43.39  ? 444 VAL B O   1 
ATOM   6208  C  CB  . VAL B 1 443 ? -0.110  24.905  58.582  1.00 43.04  ? 444 VAL B CB  1 
ATOM   6209  C  CG1 . VAL B 1 443 ? 0.685   23.613  58.585  1.00 41.29  ? 444 VAL B CG1 1 
ATOM   6210  C  CG2 . VAL B 1 443 ? 0.775   26.080  58.196  1.00 38.17  ? 444 VAL B CG2 1 
ATOM   6211  N  N   . ASP B 1 444 ? -2.211  22.585  57.210  1.00 51.50  ? 445 ASP B N   1 
ATOM   6212  C  CA  . ASP B 1 444 ? -2.878  21.352  57.589  1.00 38.46  ? 445 ASP B CA  1 
ATOM   6213  C  C   . ASP B 1 444 ? -1.869  20.519  58.365  1.00 37.62  ? 445 ASP B C   1 
ATOM   6214  O  O   . ASP B 1 444 ? -0.838  20.120  57.826  1.00 37.09  ? 445 ASP B O   1 
ATOM   6215  C  CB  . ASP B 1 444 ? -3.390  20.609  56.354  1.00 60.54  ? 445 ASP B CB  1 
ATOM   6216  C  CG  . ASP B 1 444 ? -4.160  19.351  56.703  1.00 64.24  ? 445 ASP B CG  1 
ATOM   6217  O  OD1 . ASP B 1 444 ? -4.543  19.187  57.881  1.00 64.09  ? 445 ASP B OD1 1 
ATOM   6218  O  OD2 . ASP B 1 444 ? -4.390  18.528  55.793  1.00 64.44  ? 445 ASP B OD2 1 
ATOM   6219  N  N   . ILE B 1 445 ? -2.169  20.256  59.631  1.00 37.59  ? 446 ILE B N   1 
ATOM   6220  C  CA  . ILE B 1 445 ? -1.197  19.630  60.516  1.00 37.58  ? 446 ILE B CA  1 
ATOM   6221  C  C   . ILE B 1 445 ? -1.271  18.110  60.438  1.00 37.32  ? 446 ILE B C   1 
ATOM   6222  O  O   . ILE B 1 445 ? -0.441  17.410  61.017  1.00 43.12  ? 446 ILE B O   1 
ATOM   6223  C  CB  . ILE B 1 445 ? -1.392  20.079  61.978  1.00 36.65  ? 446 ILE B CB  1 
ATOM   6224  C  CG1 . ILE B 1 445 ? -2.677  19.489  62.560  1.00 45.44  ? 446 ILE B CG1 1 
ATOM   6225  C  CG2 . ILE B 1 445 ? -1.416  21.595  62.066  1.00 46.60  ? 446 ILE B CG2 1 
ATOM   6226  C  CD1 . ILE B 1 445 ? -2.883  19.821  64.025  1.00 41.66  ? 446 ILE B CD1 1 
ATOM   6227  N  N   . THR B 1 446 ? -2.268  17.608  59.718  1.00 38.45  ? 447 THR B N   1 
ATOM   6228  C  CA  . THR B 1 446 ? -2.410  16.174  59.498  1.00 39.15  ? 447 THR B CA  1 
ATOM   6229  C  C   . THR B 1 446 ? -1.736  15.752  58.197  1.00 51.49  ? 447 THR B C   1 
ATOM   6230  O  O   . THR B 1 446 ? -1.850  14.604  57.783  1.00 61.73  ? 447 THR B O   1 
ATOM   6231  C  CB  . THR B 1 446 ? -3.889  15.730  59.470  1.00 40.67  ? 447 THR B CB  1 
ATOM   6232  O  OG1 . THR B 1 446 ? -4.566  16.353  58.372  1.00 41.31  ? 447 THR B OG1 1 
ATOM   6233  C  CG2 . THR B 1 446 ? -4.580  16.099  60.769  1.00 40.90  ? 447 THR B CG2 1 
ATOM   6234  N  N   . LYS B 1 447 ? -1.058  16.688  57.540  1.00 47.43  ? 448 LYS B N   1 
ATOM   6235  C  CA  . LYS B 1 447 ? -0.313  16.367  56.323  1.00 47.90  ? 448 LYS B CA  1 
ATOM   6236  C  C   . LYS B 1 447 ? 1.176   16.686  56.454  1.00 45.95  ? 448 LYS B C   1 
ATOM   6237  O  O   . LYS B 1 447 ? 1.666   17.634  55.841  1.00 47.81  ? 448 LYS B O   1 
ATOM   6238  C  CB  . LYS B 1 447 ? -0.893  17.117  55.123  1.00 48.37  ? 448 LYS B CB  1 
ATOM   6239  C  CG  . LYS B 1 447 ? -2.174  16.518  54.568  1.00 54.64  ? 448 LYS B CG  1 
ATOM   6240  C  CD  . LYS B 1 447 ? -2.596  17.222  53.288  1.00 56.98  ? 448 LYS B CD  1 
ATOM   6241  C  CE  . LYS B 1 447 ? -3.875  16.629  52.725  1.00 63.17  ? 448 LYS B CE  1 
ATOM   6242  N  NZ  . LYS B 1 447 ? -4.159  17.137  51.354  1.00 66.47  ? 448 LYS B NZ  1 
ATOM   6243  N  N   . PRO B 1 448 ? 1.905   15.883  57.246  1.00 42.93  ? 449 PRO B N   1 
ATOM   6244  C  CA  . PRO B 1 448 ? 3.340   16.118  57.436  1.00 43.87  ? 449 PRO B CA  1 
ATOM   6245  C  C   . PRO B 1 448 ? 4.159   15.749  56.202  1.00 43.31  ? 449 PRO B C   1 
ATOM   6246  O  O   . PRO B 1 448 ? 3.798   14.821  55.478  1.00 36.34  ? 449 PRO B O   1 
ATOM   6247  C  CB  . PRO B 1 448 ? 3.686   15.203  58.611  1.00 35.09  ? 449 PRO B CB  1 
ATOM   6248  C  CG  . PRO B 1 448 ? 2.727   14.070  58.477  1.00 36.21  ? 449 PRO B CG  1 
ATOM   6249  C  CD  . PRO B 1 448 ? 1.447   14.677  57.960  1.00 45.78  ? 449 PRO B CD  1 
ATOM   6250  N  N   . ASP B 1 449 ? 5.246   16.475  55.969  1.00 34.70  ? 450 ASP B N   1 
ATOM   6251  C  CA  . ASP B 1 449 ? 6.157   16.162  54.875  1.00 44.27  ? 450 ASP B CA  1 
ATOM   6252  C  C   . ASP B 1 449 ? 6.799   14.796  55.108  1.00 41.88  ? 450 ASP B C   1 
ATOM   6253  O  O   . ASP B 1 449 ? 7.365   14.544  56.171  1.00 47.15  ? 450 ASP B O   1 
ATOM   6254  C  CB  . ASP B 1 449 ? 7.224   17.252  54.743  1.00 46.09  ? 450 ASP B CB  1 
ATOM   6255  C  CG  . ASP B 1 449 ? 8.202   16.980  53.620  1.00 47.85  ? 450 ASP B CG  1 
ATOM   6256  O  OD1 . ASP B 1 449 ? 7.956   17.446  52.488  1.00 36.40  ? 450 ASP B OD1 1 
ATOM   6257  O  OD2 . ASP B 1 449 ? 9.222   16.308  53.873  1.00 54.88  ? 450 ASP B OD2 1 
ATOM   6258  N  N   . MET B 1 450 ? 6.703   13.917  54.113  1.00 35.57  ? 451 MET B N   1 
ATOM   6259  C  CA  . MET B 1 450 ? 7.159   12.534  54.253  1.00 49.51  ? 451 MET B CA  1 
ATOM   6260  C  C   . MET B 1 450 ? 8.679   12.429  54.366  1.00 45.62  ? 451 MET B C   1 
ATOM   6261  O  O   . MET B 1 450 ? 9.203   11.648  55.174  1.00 46.62  ? 451 MET B O   1 
ATOM   6262  C  CB  . MET B 1 450 ? 6.667   11.695  53.072  1.00 45.00  ? 451 MET B CB  1 
ATOM   6263  C  CG  . MET B 1 450 ? 5.157   11.510  53.031  1.00 50.01  ? 451 MET B CG  1 
ATOM   6264  N  N   . THR B 1 451 ? 9.375   13.213  53.546  1.00 38.79  ? 452 THR B N   1 
ATOM   6265  C  CA  . THR B 1 451 ? 10.834  13.256  53.557  1.00 42.97  ? 452 THR B CA  1 
ATOM   6266  C  C   . THR B 1 451 ? 11.356  13.512  54.965  1.00 33.00  ? 452 THR B C   1 
ATOM   6267  O  O   . THR B 1 451 ? 12.261  12.826  55.446  1.00 49.20  ? 452 THR B O   1 
ATOM   6268  C  CB  . THR B 1 451 ? 11.373  14.350  52.612  1.00 41.28  ? 452 THR B CB  1 
ATOM   6269  O  OG1 . THR B 1 451 ? 10.979  14.061  51.266  1.00 42.65  ? 452 THR B OG1 1 
ATOM   6270  C  CG2 . THR B 1 451 ? 12.889  14.432  52.690  1.00 33.49  ? 452 THR B CG2 1 
ATOM   6271  N  N   . ILE B 1 452 ? 10.751  14.487  55.631  1.00 35.14  ? 453 ILE B N   1 
ATOM   6272  C  CA  . ILE B 1 452 ? 11.186  14.893  56.957  1.00 35.54  ? 453 ILE B CA  1 
ATOM   6273  C  C   . ILE B 1 452 ? 10.888  13.812  57.994  1.00 36.86  ? 453 ILE B C   1 
ATOM   6274  O  O   . ILE B 1 452 ? 11.684  13.596  58.903  1.00 34.11  ? 453 ILE B O   1 
ATOM   6275  C  CB  . ILE B 1 452 ? 10.533  16.233  57.354  1.00 31.58  ? 453 ILE B CB  1 
ATOM   6276  C  CG1 . ILE B 1 452 ? 11.007  17.323  56.388  1.00 31.59  ? 453 ILE B CG1 1 
ATOM   6277  C  CG2 . ILE B 1 452 ? 10.869  16.605  58.791  1.00 33.51  ? 453 ILE B CG2 1 
ATOM   6278  C  CD1 . ILE B 1 452 ? 10.733  18.729  56.846  1.00 32.56  ? 453 ILE B CD1 1 
ATOM   6279  N  N   . ARG B 1 453 ? 9.763   13.118  57.846  1.00 32.57  ? 454 ARG B N   1 
ATOM   6280  C  CA  . ARG B 1 453 ? 9.452   11.986  58.720  1.00 40.29  ? 454 ARG B CA  1 
ATOM   6281  C  C   . ARG B 1 453 ? 10.517  10.894  58.588  1.00 32.76  ? 454 ARG B C   1 
ATOM   6282  O  O   . ARG B 1 453 ? 11.029  10.364  59.593  1.00 37.23  ? 454 ARG B O   1 
ATOM   6283  C  CB  . ARG B 1 453 ? 8.068   11.420  58.397  1.00 40.28  ? 454 ARG B CB  1 
ATOM   6284  N  N   . GLN B 1 454 ? 10.851  10.573  57.340  1.00 33.17  ? 455 GLN B N   1 
ATOM   6285  C  CA  . GLN B 1 454 ? 11.914  9.612   57.055  1.00 39.22  ? 455 GLN B CA  1 
ATOM   6286  C  C   . GLN B 1 454 ? 13.233  10.029  57.711  1.00 40.84  ? 455 GLN B C   1 
ATOM   6287  O  O   . GLN B 1 454 ? 13.898  9.220   58.372  1.00 42.01  ? 455 GLN B O   1 
ATOM   6288  C  CB  . GLN B 1 454 ? 12.100  9.453   55.544  1.00 50.61  ? 455 GLN B CB  1 
ATOM   6289  C  CG  . GLN B 1 454 ? 10.926  8.784   54.841  1.00 60.56  ? 455 GLN B CG  1 
ATOM   6290  C  CD  . GLN B 1 454 ? 11.013  8.882   53.328  1.00 66.75  ? 455 GLN B CD  1 
ATOM   6291  O  OE1 . GLN B 1 454 ? 11.760  9.698   52.787  1.00 69.96  ? 455 GLN B OE1 1 
ATOM   6292  N  NE2 . GLN B 1 454 ? 10.249  8.043   52.638  1.00 69.45  ? 455 GLN B NE2 1 
ATOM   6293  N  N   . GLN B 1 455 ? 13.598  11.297  57.539  1.00 35.12  ? 456 GLN B N   1 
ATOM   6294  C  CA  . GLN B 1 455 ? 14.835  11.810  58.122  1.00 37.86  ? 456 GLN B CA  1 
ATOM   6295  C  C   . GLN B 1 455 ? 14.819  11.737  59.649  1.00 41.25  ? 456 GLN B C   1 
ATOM   6296  O  O   . GLN B 1 455 ? 15.846  11.471  60.267  1.00 47.56  ? 456 GLN B O   1 
ATOM   6297  C  CB  . GLN B 1 455 ? 15.093  13.249  57.668  1.00 34.30  ? 456 GLN B CB  1 
ATOM   6298  C  CG  . GLN B 1 455 ? 15.237  13.404  56.161  1.00 37.37  ? 456 GLN B CG  1 
ATOM   6299  C  CD  . GLN B 1 455 ? 16.144  12.350  55.548  1.00 46.09  ? 456 GLN B CD  1 
ATOM   6300  O  OE1 . GLN B 1 455 ? 17.318  12.242  55.899  1.00 39.95  ? 456 GLN B OE1 1 
ATOM   6301  N  NE2 . GLN B 1 455 ? 15.597  11.565  54.626  1.00 43.97  ? 456 GLN B NE2 1 
ATOM   6302  N  N   . ILE B 1 456 ? 13.656  11.969  60.252  1.00 38.07  ? 457 ILE B N   1 
ATOM   6303  C  CA  . ILE B 1 456 ? 13.504  11.842  61.699  1.00 35.27  ? 457 ILE B CA  1 
ATOM   6304  C  C   . ILE B 1 456 ? 13.784  10.403  62.121  1.00 30.69  ? 457 ILE B C   1 
ATOM   6305  O  O   . ILE B 1 456 ? 14.526  10.154  63.086  1.00 36.37  ? 457 ILE B O   1 
ATOM   6306  C  CB  . ILE B 1 456 ? 12.092  12.258  62.167  1.00 33.26  ? 457 ILE B CB  1 
ATOM   6307  C  CG1 . ILE B 1 456 ? 11.881  13.759  61.970  1.00 32.20  ? 457 ILE B CG1 1 
ATOM   6308  C  CG2 . ILE B 1 456 ? 11.880  11.902  63.629  1.00 34.54  ? 457 ILE B CG2 1 
ATOM   6309  C  CD1 . ILE B 1 456 ? 10.462  14.215  62.229  1.00 32.87  ? 457 ILE B CD1 1 
ATOM   6310  N  N   . MET B 1 457 ? 13.195  9.461   61.385  1.00 31.41  ? 458 MET B N   1 
ATOM   6311  C  CA  . MET B 1 457 ? 13.459  8.042   61.624  1.00 46.41  ? 458 MET B CA  1 
ATOM   6312  C  C   . MET B 1 457 ? 14.963  7.746   61.578  1.00 43.90  ? 458 MET B C   1 
ATOM   6313  O  O   . MET B 1 457 ? 15.514  7.103   62.484  1.00 44.03  ? 458 MET B O   1 
ATOM   6314  C  CB  . MET B 1 457 ? 12.719  7.178   60.600  1.00 49.38  ? 458 MET B CB  1 
ATOM   6315  C  CG  . MET B 1 457 ? 12.817  5.682   60.857  1.00 49.50  ? 458 MET B CG  1 
ATOM   6316  S  SD  . MET B 1 457 ? 11.894  5.164   62.316  1.00 73.80  ? 458 MET B SD  1 
ATOM   6317  C  CE  . MET B 1 457 ? 10.225  5.599   61.831  1.00 62.83  ? 458 MET B CE  1 
ATOM   6318  N  N   . GLN B 1 458 ? 15.617  8.234   60.525  1.00 38.13  ? 459 GLN B N   1 
ATOM   6319  C  CA  . GLN B 1 458 ? 17.065  8.087   60.375  1.00 43.19  ? 459 GLN B CA  1 
ATOM   6320  C  C   . GLN B 1 458 ? 17.829  8.617   61.590  1.00 37.27  ? 459 GLN B C   1 
ATOM   6321  O  O   . GLN B 1 458 ? 18.711  7.938   62.133  1.00 40.13  ? 459 GLN B O   1 
ATOM   6322  C  CB  . GLN B 1 458 ? 17.542  8.804   59.111  1.00 39.98  ? 459 GLN B CB  1 
ATOM   6323  C  CG  . GLN B 1 458 ? 16.981  8.219   57.828  1.00 43.77  ? 459 GLN B CG  1 
ATOM   6324  C  CD  . GLN B 1 458 ? 17.328  6.752   57.665  1.00 51.73  ? 459 GLN B CD  1 
ATOM   6325  O  OE1 . GLN B 1 458 ? 18.501  6.378   57.646  1.00 53.28  ? 459 GLN B OE1 1 
ATOM   6326  N  NE2 . GLN B 1 458 ? 16.306  5.912   57.554  1.00 53.97  ? 459 GLN B NE2 1 
ATOM   6327  N  N   . LEU B 1 459 ? 17.481  9.833   62.005  1.00 34.49  ? 460 LEU B N   1 
ATOM   6328  C  CA  . LEU B 1 459 ? 18.073  10.458  63.183  1.00 37.94  ? 460 LEU B CA  1 
ATOM   6329  C  C   . LEU B 1 459 ? 17.954  9.557   64.404  1.00 38.97  ? 460 LEU B C   1 
ATOM   6330  O  O   . LEU B 1 459 ? 18.929  9.353   65.135  1.00 38.39  ? 460 LEU B O   1 
ATOM   6331  C  CB  . LEU B 1 459 ? 17.406  11.807  63.470  1.00 32.15  ? 460 LEU B CB  1 
ATOM   6332  C  CG  . LEU B 1 459 ? 17.609  12.942  62.464  1.00 33.93  ? 460 LEU B CG  1 
ATOM   6333  C  CD1 . LEU B 1 459 ? 16.692  14.111  62.791  1.00 28.68  ? 460 LEU B CD1 1 
ATOM   6334  C  CD2 . LEU B 1 459 ? 19.062  13.388  62.442  1.00 28.39  ? 460 LEU B CD2 1 
ATOM   6335  N  N   . LYS B 1 460 ? 16.759  9.012   64.619  1.00 38.64  ? 461 LYS B N   1 
ATOM   6336  C  CA  . LYS B 1 460 ? 16.527  8.164   65.786  1.00 39.43  ? 461 LYS B CA  1 
ATOM   6337  C  C   . LYS B 1 460 ? 17.337  6.866   65.733  1.00 38.34  ? 461 LYS B C   1 
ATOM   6338  O  O   . LYS B 1 460 ? 17.904  6.435   66.746  1.00 30.67  ? 461 LYS B O   1 
ATOM   6339  C  CB  . LYS B 1 460 ? 15.036  7.856   65.931  1.00 46.35  ? 461 LYS B CB  1 
ATOM   6340  C  CG  . LYS B 1 460 ? 14.509  8.078   67.343  1.00 55.57  ? 461 LYS B CG  1 
ATOM   6341  C  CD  . LYS B 1 460 ? 13.096  8.647   67.352  1.00 56.36  ? 461 LYS B CD  1 
ATOM   6342  C  CE  . LYS B 1 460 ? 12.222  8.037   66.273  1.00 58.20  ? 461 LYS B CE  1 
ATOM   6343  N  NZ  . LYS B 1 460 ? 10.844  8.603   66.309  1.00 57.37  ? 461 LYS B NZ  1 
ATOM   6344  N  N   . ILE B 1 461 ? 17.401  6.250   64.556  1.00 30.86  ? 462 ILE B N   1 
ATOM   6345  C  CA  . ILE B 1 461 ? 18.177  5.021   64.398  1.00 33.18  ? 462 ILE B CA  1 
ATOM   6346  C  C   . ILE B 1 461 ? 19.669  5.261   64.655  1.00 34.34  ? 462 ILE B C   1 
ATOM   6347  O  O   . ILE B 1 461 ? 20.309  4.525   65.424  1.00 35.88  ? 462 ILE B O   1 
ATOM   6348  C  CB  . ILE B 1 461 ? 17.975  4.410   62.997  1.00 40.19  ? 462 ILE B CB  1 
ATOM   6349  C  CG1 . ILE B 1 461 ? 16.626  3.692   62.930  1.00 41.78  ? 462 ILE B CG1 1 
ATOM   6350  C  CG2 . ILE B 1 461 ? 19.089  3.429   62.668  1.00 37.90  ? 462 ILE B CG2 1 
ATOM   6351  C  CD1 . ILE B 1 461 ? 15.952  3.771   61.581  1.00 44.34  ? 462 ILE B CD1 1 
ATOM   6352  N  N   . MET B 1 462 ? 20.216  6.300   64.029  1.00 33.31  ? 463 MET B N   1 
ATOM   6353  C  CA  . MET B 1 462 ? 21.623  6.641   64.225  1.00 29.64  ? 463 MET B CA  1 
ATOM   6354  C  C   . MET B 1 462 ? 21.908  6.951   65.695  1.00 29.45  ? 463 MET B C   1 
ATOM   6355  O  O   . MET B 1 462 ? 22.945  6.550   66.242  1.00 37.75  ? 463 MET B O   1 
ATOM   6356  C  CB  . MET B 1 462 ? 22.018  7.827   63.346  1.00 29.23  ? 463 MET B CB  1 
ATOM   6357  C  CG  . MET B 1 462 ? 23.509  8.125   63.345  1.00 33.02  ? 463 MET B CG  1 
ATOM   6358  S  SD  . MET B 1 462 ? 24.485  6.756   62.693  1.00 46.66  ? 463 MET B SD  1 
ATOM   6359  C  CE  . MET B 1 462 ? 25.491  6.340   64.116  1.00 29.33  ? 463 MET B CE  1 
ATOM   6360  N  N   . THR B 1 463 ? 20.976  7.655   66.331  1.00 29.38  ? 464 THR B N   1 
ATOM   6361  C  CA  . THR B 1 463 ? 21.096  7.972   67.751  1.00 37.38  ? 464 THR B CA  1 
ATOM   6362  C  C   . THR B 1 463 ? 21.175  6.694   68.581  1.00 35.63  ? 464 THR B C   1 
ATOM   6363  O  O   . THR B 1 463 ? 22.012  6.578   69.485  1.00 30.00  ? 464 THR B O   1 
ATOM   6364  C  CB  . THR B 1 463 ? 19.917  8.833   68.240  1.00 29.41  ? 464 THR B CB  1 
ATOM   6365  O  OG1 . THR B 1 463 ? 19.915  10.081  67.536  1.00 28.94  ? 464 THR B OG1 1 
ATOM   6366  C  CG2 . THR B 1 463 ? 20.034  9.107   69.732  1.00 29.59  ? 464 THR B CG2 1 
ATOM   6367  N  N   . ASN B 1 464 ? 20.309  5.734   68.261  1.00 30.47  ? 465 ASN B N   1 
ATOM   6368  C  CA  . ASN B 1 464 ? 20.346  4.432   68.920  1.00 31.16  ? 465 ASN B CA  1 
ATOM   6369  C  C   . ASN B 1 464 ? 21.699  3.747   68.752  1.00 39.32  ? 465 ASN B C   1 
ATOM   6370  O  O   . ASN B 1 464 ? 22.271  3.234   69.727  1.00 31.42  ? 465 ASN B O   1 
ATOM   6371  C  CB  . ASN B 1 464 ? 19.234  3.528   68.389  1.00 65.27  ? 465 ASN B CB  1 
ATOM   6372  C  CG  . ASN B 1 464 ? 17.879  3.877   68.967  1.00 73.05  ? 465 ASN B CG  1 
ATOM   6373  O  OD1 . ASN B 1 464 ? 17.771  4.272   70.128  1.00 71.59  ? 465 ASN B OD1 1 
ATOM   6374  N  ND2 . ASN B 1 464 ? 16.834  3.731   68.160  1.00 72.15  ? 465 ASN B ND2 1 
ATOM   6375  N  N   . ARG B 1 465 ? 22.207  3.742   67.519  1.00 33.43  ? 466 ARG B N   1 
ATOM   6376  C  CA  . ARG B 1 465 ? 23.537  3.196   67.259  1.00 39.42  ? 466 ARG B CA  1 
ATOM   6377  C  C   . ARG B 1 465 ? 24.584  3.846   68.159  1.00 39.27  ? 466 ARG B C   1 
ATOM   6378  O  O   . ARG B 1 465 ? 25.434  3.159   68.729  1.00 30.75  ? 466 ARG B O   1 
ATOM   6379  C  CB  . ARG B 1 465 ? 23.939  3.381   65.794  1.00 43.91  ? 466 ARG B CB  1 
ATOM   6380  C  CG  . ARG B 1 465 ? 23.265  2.434   64.817  1.00 50.20  ? 466 ARG B CG  1 
ATOM   6381  C  CD  . ARG B 1 465 ? 23.875  2.581   63.429  1.00 55.08  ? 466 ARG B CD  1 
ATOM   6382  N  NE  . ARG B 1 465 ? 23.173  1.793   62.421  1.00 60.76  ? 466 ARG B NE  1 
ATOM   6383  C  CZ  . ARG B 1 465 ? 22.554  2.314   61.366  1.00 65.36  ? 466 ARG B CZ  1 
ATOM   6384  N  NH1 . ARG B 1 465 ? 21.940  1.523   60.497  1.00 64.51  ? 466 ARG B NH1 1 
ATOM   6385  N  NH2 . ARG B 1 465 ? 22.550  3.628   61.179  1.00 60.54  ? 466 ARG B NH2 1 
ATOM   6386  N  N   . LEU B 1 466 ? 24.510  5.168   68.293  1.00 33.76  ? 467 LEU B N   1 
ATOM   6387  C  CA  . LEU B 1 466 ? 25.486  5.903   69.099  1.00 35.05  ? 467 LEU B CA  1 
ATOM   6388  C  C   . LEU B 1 466 ? 25.365  5.623   70.598  1.00 30.18  ? 467 LEU B C   1 
ATOM   6389  O  O   . LEU B 1 466 ? 26.368  5.630   71.315  1.00 30.32  ? 467 LEU B O   1 
ATOM   6390  C  CB  . LEU B 1 466 ? 25.361  7.403   68.837  1.00 29.23  ? 467 LEU B CB  1 
ATOM   6391  C  CG  . LEU B 1 466 ? 26.130  7.872   67.604  1.00 29.81  ? 467 LEU B CG  1 
ATOM   6392  C  CD1 . LEU B 1 466 ? 25.498  9.114   67.017  1.00 28.55  ? 467 LEU B CD1 1 
ATOM   6393  C  CD2 . LEU B 1 466 ? 27.588  8.128   67.964  1.00 28.91  ? 467 LEU B CD2 1 
ATOM   6394  N  N   . ARG B 1 467 ? 24.147  5.381   71.075  1.00 30.53  ? 468 ARG B N   1 
ATOM   6395  C  CA  . ARG B 1 467 ? 23.954  5.018   72.479  1.00 46.87  ? 468 ARG B CA  1 
ATOM   6396  C  C   . ARG B 1 467 ? 24.521  3.623   72.753  1.00 47.07  ? 468 ARG B C   1 
ATOM   6397  O  O   . ARG B 1 467 ? 25.219  3.396   73.760  1.00 48.14  ? 468 ARG B O   1 
ATOM   6398  C  CB  . ARG B 1 467 ? 22.472  5.075   72.854  1.00 52.21  ? 468 ARG B CB  1 
ATOM   6399  N  N   . SER B 1 468 ? 24.217  2.695   71.847  1.00 42.63  ? 469 SER B N   1 
ATOM   6400  C  CA  . SER B 1 468 ? 24.794  1.356   71.898  1.00 43.77  ? 469 SER B CA  1 
ATOM   6401  C  C   . SER B 1 468 ? 26.313  1.444   71.974  1.00 46.58  ? 469 SER B C   1 
ATOM   6402  O  O   . SER B 1 468 ? 26.937  0.848   72.854  1.00 39.52  ? 469 SER B O   1 
ATOM   6403  C  CB  . SER B 1 468 ? 24.376  0.533   70.677  1.00 37.61  ? 469 SER B CB  1 
ATOM   6404  O  OG  . SER B 1 468 ? 22.969  0.396   70.606  1.00 44.40  ? 469 SER B OG  1 
ATOM   6405  N  N   . ALA B 1 469 ? 26.892  2.210   71.054  1.00 42.72  ? 470 ALA B N   1 
ATOM   6406  C  CA  . ALA B 1 469 ? 28.336  2.410   71.001  1.00 41.73  ? 470 ALA B CA  1 
ATOM   6407  C  C   . ALA B 1 469 ? 28.870  3.018   72.291  1.00 38.23  ? 470 ALA B C   1 
ATOM   6408  O  O   . ALA B 1 469 ? 29.976  2.692   72.721  1.00 41.69  ? 470 ALA B O   1 
ATOM   6409  C  CB  . ALA B 1 469 ? 28.704  3.286   69.821  1.00 33.22  ? 470 ALA B CB  1 
ATOM   6410  N  N   . TYR B 1 470 ? 28.092  3.907   72.903  1.00 45.75  ? 471 TYR B N   1 
ATOM   6411  C  CA  . TYR B 1 470 ? 28.495  4.477   74.183  1.00 41.55  ? 471 TYR B CA  1 
ATOM   6412  C  C   . TYR B 1 470 ? 28.599  3.379   75.227  1.00 43.81  ? 471 TYR B C   1 
ATOM   6413  O  O   . TYR B 1 470 ? 29.591  3.294   75.950  1.00 36.36  ? 471 TYR B O   1 
ATOM   6414  C  CB  . TYR B 1 470 ? 27.520  5.554   74.658  1.00 39.32  ? 471 TYR B CB  1 
ATOM   6415  C  CG  . TYR B 1 470 ? 28.050  6.341   75.838  1.00 44.31  ? 471 TYR B CG  1 
ATOM   6416  C  CD1 . TYR B 1 470 ? 28.901  7.422   75.648  1.00 43.58  ? 471 TYR B CD1 1 
ATOM   6417  C  CD2 . TYR B 1 470 ? 27.719  5.991   77.141  1.00 45.56  ? 471 TYR B CD2 1 
ATOM   6418  C  CE1 . TYR B 1 470 ? 29.395  8.141   76.720  1.00 48.64  ? 471 TYR B CE1 1 
ATOM   6419  C  CE2 . TYR B 1 470 ? 28.211  6.704   78.222  1.00 46.73  ? 471 TYR B CE2 1 
ATOM   6420  C  CZ  . TYR B 1 470 ? 29.048  7.778   78.004  1.00 48.61  ? 471 TYR B CZ  1 
ATOM   6421  O  OH  . TYR B 1 470 ? 29.543  8.494   79.071  1.00 54.33  ? 471 TYR B OH  1 
ATOM   6422  N  N   . ASN B 1 471 ? 27.577  2.533   75.301  1.00 62.11  ? 472 ASN B N   1 
ATOM   6423  C  CA  . ASN B 1 471 ? 27.595  1.452   76.282  1.00 65.89  ? 472 ASN B CA  1 
ATOM   6424  C  C   . ASN B 1 471 ? 28.698  0.423   76.018  1.00 68.40  ? 472 ASN B C   1 
ATOM   6425  O  O   . ASN B 1 471 ? 29.185  -0.225  76.945  1.00 64.83  ? 472 ASN B O   1 
ATOM   6426  C  CB  . ASN B 1 471 ? 26.235  0.760   76.331  1.00 64.38  ? 472 ASN B CB  1 
ATOM   6427  C  CG  . ASN B 1 471 ? 25.152  1.655   76.899  1.00 65.58  ? 472 ASN B CG  1 
ATOM   6428  O  OD1 . ASN B 1 471 ? 25.410  2.476   77.779  1.00 66.39  ? 472 ASN B OD1 1 
ATOM   6429  N  ND2 . ASN B 1 471 ? 23.933  1.501   76.398  1.00 68.18  ? 472 ASN B ND2 1 
ATOM   6430  N  N   . GLY B 1 472 ? 29.094  0.285   74.757  1.00 71.75  ? 473 GLY B N   1 
ATOM   6431  C  CA  . GLY B 1 472 ? 30.138  -0.653  74.384  1.00 75.86  ? 473 GLY B CA  1 
ATOM   6432  C  C   . GLY B 1 472 ? 29.633  -1.729  73.443  1.00 80.99  ? 473 GLY B C   1 
ATOM   6433  O  O   . GLY B 1 472 ? 30.413  -2.495  72.878  1.00 82.80  ? 473 GLY B O   1 
ATOM   6434  N  N   . ASN B 1 473 ? 28.316  -1.782  73.279  1.00 81.27  ? 474 ASN B N   1 
ATOM   6435  C  CA  . ASN B 1 473 ? 27.682  -2.747  72.391  1.00 85.59  ? 474 ASN B CA  1 
ATOM   6436  C  C   . ASN B 1 473 ? 27.721  -2.275  70.940  1.00 86.42  ? 474 ASN B C   1 
ATOM   6437  O  O   . ASN B 1 473 ? 28.244  -1.201  70.643  1.00 83.79  ? 474 ASN B O   1 
ATOM   6438  C  CB  . ASN B 1 473 ? 26.231  -2.983  72.816  1.00 84.74  ? 474 ASN B CB  1 
ATOM   6439  C  CG  . ASN B 1 473 ? 26.044  -2.920  74.321  1.00 86.33  ? 474 ASN B CG  1 
ATOM   6440  O  OD1 . ASN B 1 473 ? 26.962  -3.214  75.088  1.00 86.49  ? 474 ASN B OD1 1 
ATOM   6441  N  ND2 . ASN B 1 473 ? 24.852  -2.520  74.752  1.00 86.42  ? 474 ASN B ND2 1 
ATOM   6442  N  N   . ASP B 1 474 ? 27.166  -3.085  70.041  1.00 91.87  ? 475 ASP B N   1 
ATOM   6443  C  CA  . ASP B 1 474 ? 26.929  -2.663  68.662  1.00 94.02  ? 475 ASP B CA  1 
ATOM   6444  C  C   . ASP B 1 474 ? 25.851  -3.531  68.018  1.00 92.83  ? 475 ASP B C   1 
ATOM   6445  O  O   . ASP B 1 474 ? 25.568  -3.406  66.827  1.00 91.65  ? 475 ASP B O   1 
ATOM   6446  C  CB  . ASP B 1 474 ? 28.229  -2.691  67.838  1.00 98.06  ? 475 ASP B CB  1 
ATOM   6447  C  CG  . ASP B 1 474 ? 28.777  -4.097  67.615  1.00 102.88 ? 475 ASP B CG  1 
ATOM   6448  O  OD1 . ASP B 1 474 ? 28.062  -4.963  67.065  1.00 105.93 ? 475 ASP B OD1 1 
ATOM   6449  O  OD2 . ASP B 1 474 ? 29.946  -4.334  67.983  1.00 103.38 ? 475 ASP B OD2 1 
ATOM   6450  N  N   . SER C 1 28  ? -9.315  -39.913 20.486  1.00 66.28  ? 29  SER C N   1 
ATOM   6451  C  CA  . SER C 1 28  ? -9.501  -40.357 21.862  1.00 63.93  ? 29  SER C CA  1 
ATOM   6452  C  C   . SER C 1 28  ? -9.897  -39.201 22.777  1.00 68.14  ? 29  SER C C   1 
ATOM   6453  O  O   . SER C 1 28  ? -9.465  -38.064 22.584  1.00 68.61  ? 29  SER C O   1 
ATOM   6454  C  CB  . SER C 1 28  ? -8.230  -41.025 22.387  1.00 64.79  ? 29  SER C CB  1 
ATOM   6455  O  OG  . SER C 1 28  ? -8.365  -41.366 23.756  1.00 63.86  ? 29  SER C OG  1 
ATOM   6456  N  N   . ARG C 1 29  ? -10.727 -39.505 23.769  1.00 64.02  ? 30  ARG C N   1 
ATOM   6457  C  CA  . ARG C 1 29  ? -11.224 -38.501 24.703  1.00 58.61  ? 30  ARG C CA  1 
ATOM   6458  C  C   . ARG C 1 29  ? -10.406 -38.424 25.993  1.00 55.99  ? 30  ARG C C   1 
ATOM   6459  O  O   . ARG C 1 29  ? -10.756 -37.679 26.908  1.00 55.15  ? 30  ARG C O   1 
ATOM   6460  C  CB  . ARG C 1 29  ? -12.692 -38.775 25.031  1.00 57.36  ? 30  ARG C CB  1 
ATOM   6461  C  CG  . ARG C 1 29  ? -13.614 -38.632 23.833  1.00 53.82  ? 30  ARG C CG  1 
ATOM   6462  C  CD  . ARG C 1 29  ? -15.050 -38.953 24.195  1.00 57.39  ? 30  ARG C CD  1 
ATOM   6463  N  NE  . ARG C 1 29  ? -15.923 -38.914 23.026  1.00 58.17  ? 30  ARG C NE  1 
ATOM   6464  C  CZ  . ARG C 1 29  ? -17.203 -39.271 23.040  1.00 56.61  ? 30  ARG C CZ  1 
ATOM   6465  N  NH1 . ARG C 1 29  ? -17.761 -39.695 24.165  1.00 55.54  ? 30  ARG C NH1 1 
ATOM   6466  N  NH2 . ARG C 1 29  ? -17.924 -39.204 21.929  1.00 54.64  ? 30  ARG C NH2 1 
ATOM   6467  N  N   . SER C 1 30  ? -9.331  -39.202 26.071  1.00 55.53  ? 31  SER C N   1 
ATOM   6468  C  CA  . SER C 1 30  ? -8.475  -39.201 27.255  1.00 57.56  ? 31  SER C CA  1 
ATOM   6469  C  C   . SER C 1 30  ? -7.789  -37.849 27.435  1.00 56.84  ? 31  SER C C   1 
ATOM   6470  O  O   . SER C 1 30  ? -7.608  -37.103 26.473  1.00 50.47  ? 31  SER C O   1 
ATOM   6471  C  CB  . SER C 1 30  ? -7.427  -40.311 27.166  1.00 58.95  ? 31  SER C CB  1 
ATOM   6472  O  OG  . SER C 1 30  ? -6.531  -40.081 26.092  1.00 60.54  ? 31  SER C OG  1 
ATOM   6473  N  N   . CYS C 1 31  ? -7.412  -37.538 28.671  1.00 54.75  ? 32  CYS C N   1 
ATOM   6474  C  CA  . CYS C 1 31  ? -6.791  -36.255 28.980  1.00 55.98  ? 32  CYS C CA  1 
ATOM   6475  C  C   . CYS C 1 31  ? -5.343  -36.416 29.433  1.00 59.63  ? 32  CYS C C   1 
ATOM   6476  O  O   . CYS C 1 31  ? -4.827  -35.588 30.183  1.00 55.03  ? 32  CYS C O   1 
ATOM   6477  C  CB  . CYS C 1 31  ? -7.592  -35.523 30.058  1.00 58.11  ? 32  CYS C CB  1 
ATOM   6478  S  SG  . CYS C 1 31  ? -9.228  -34.970 29.527  1.00 60.11  ? 32  CYS C SG  1 
ATOM   6479  N  N   . GLY C 1 32  ? -4.693  -37.479 28.967  1.00 59.11  ? 33  GLY C N   1 
ATOM   6480  C  CA  . GLY C 1 32  ? -3.331  -37.788 29.369  1.00 60.70  ? 33  GLY C CA  1 
ATOM   6481  C  C   . GLY C 1 32  ? -2.309  -36.742 28.965  1.00 57.08  ? 33  GLY C C   1 
ATOM   6482  O  O   . GLY C 1 32  ? -1.543  -36.257 29.802  1.00 61.60  ? 33  GLY C O   1 
ATOM   6483  N  N   . GLU C 1 33  ? -2.292  -36.401 27.679  1.00 55.80  ? 34  GLU C N   1 
ATOM   6484  C  CA  . GLU C 1 33  ? -1.375  -35.392 27.158  1.00 56.90  ? 34  GLU C CA  1 
ATOM   6485  C  C   . GLU C 1 33  ? -1.563  -34.066 27.885  1.00 54.44  ? 34  GLU C C   1 
ATOM   6486  O  O   . GLU C 1 33  ? -0.603  -33.480 28.391  1.00 56.35  ? 34  GLU C O   1 
ATOM   6487  C  CB  . GLU C 1 33  ? -1.579  -35.201 25.654  1.00 58.34  ? 34  GLU C CB  1 
ATOM   6488  N  N   . VAL C 1 34  ? -2.812  -33.611 27.939  1.00 51.72  ? 35  VAL C N   1 
ATOM   6489  C  CA  . VAL C 1 34  ? -3.164  -32.381 28.636  1.00 47.14  ? 35  VAL C CA  1 
ATOM   6490  C  C   . VAL C 1 34  ? -2.743  -32.442 30.100  1.00 47.56  ? 35  VAL C C   1 
ATOM   6491  O  O   . VAL C 1 34  ? -2.269  -31.453 30.650  1.00 59.56  ? 35  VAL C O   1 
ATOM   6492  C  CB  . VAL C 1 34  ? -4.678  -32.098 28.552  1.00 46.91  ? 35  VAL C CB  1 
ATOM   6493  C  CG1 . VAL C 1 34  ? -5.035  -30.840 29.331  1.00 46.26  ? 35  VAL C CG1 1 
ATOM   6494  C  CG2 . VAL C 1 34  ? -5.109  -31.966 27.103  1.00 46.59  ? 35  VAL C CG2 1 
ATOM   6495  N  N   . ARG C 1 35  ? -2.904  -33.605 30.725  1.00 52.41  ? 36  ARG C N   1 
ATOM   6496  C  CA  . ARG C 1 35  ? -2.497  -33.773 32.116  1.00 56.84  ? 36  ARG C CA  1 
ATOM   6497  C  C   . ARG C 1 35  ? -0.997  -33.584 32.281  1.00 61.16  ? 36  ARG C C   1 
ATOM   6498  O  O   . ARG C 1 35  ? -0.546  -32.875 33.182  1.00 64.72  ? 36  ARG C O   1 
ATOM   6499  C  CB  . ARG C 1 35  ? -2.893  -35.151 32.649  1.00 55.29  ? 36  ARG C CB  1 
ATOM   6500  C  CG  . ARG C 1 35  ? -2.353  -35.433 34.046  1.00 61.73  ? 36  ARG C CG  1 
ATOM   6501  C  CD  . ARG C 1 35  ? -2.528  -36.891 34.453  1.00 67.44  ? 36  ARG C CD  1 
ATOM   6502  N  NE  . ARG C 1 35  ? -3.860  -37.163 34.987  1.00 74.34  ? 36  ARG C NE  1 
ATOM   6503  C  CZ  . ARG C 1 35  ? -4.852  -37.701 34.287  1.00 76.99  ? 36  ARG C CZ  1 
ATOM   6504  N  NH1 . ARG C 1 35  ? -4.668  -38.034 33.017  1.00 76.38  ? 36  ARG C NH1 1 
ATOM   6505  N  NH2 . ARG C 1 35  ? -6.030  -37.912 34.859  1.00 79.41  ? 36  ARG C NH2 1 
ATOM   6506  N  N   . GLN C 1 36  ? -0.223  -34.220 31.408  1.00 60.12  ? 37  GLN C N   1 
ATOM   6507  C  CA  . GLN C 1 36  ? 1.226   -34.183 31.544  1.00 63.48  ? 37  GLN C CA  1 
ATOM   6508  C  C   . GLN C 1 36  ? 1.784   -32.801 31.223  1.00 58.52  ? 37  GLN C C   1 
ATOM   6509  O  O   . GLN C 1 36  ? 2.736   -32.353 31.858  1.00 54.41  ? 37  GLN C O   1 
ATOM   6510  C  CB  . GLN C 1 36  ? 1.878   -35.241 30.654  1.00 66.28  ? 37  GLN C CB  1 
ATOM   6511  C  CG  . GLN C 1 36  ? 3.103   -35.928 31.266  1.00 73.96  ? 37  GLN C CG  1 
ATOM   6512  C  CD  . GLN C 1 36  ? 2.860   -36.484 32.667  1.00 80.14  ? 37  GLN C CD  1 
ATOM   6513  O  OE1 . GLN C 1 36  ? 2.751   -35.740 33.644  1.00 82.02  ? 37  GLN C OE1 1 
ATOM   6514  N  NE2 . GLN C 1 36  ? 2.770   -37.806 32.764  1.00 82.16  ? 37  GLN C NE2 1 
ATOM   6515  N  N   . ILE C 1 37  ? 1.186   -32.124 30.248  1.00 59.91  ? 38  ILE C N   1 
ATOM   6516  C  CA  . ILE C 1 37  ? 1.599   -30.766 29.910  1.00 54.69  ? 38  ILE C CA  1 
ATOM   6517  C  C   . ILE C 1 37  ? 1.186   -29.789 31.014  1.00 62.40  ? 38  ILE C C   1 
ATOM   6518  O  O   . ILE C 1 37  ? 1.880   -28.806 31.284  1.00 64.70  ? 38  ILE C O   1 
ATOM   6519  C  CB  . ILE C 1 37  ? 1.006   -30.321 28.555  1.00 55.55  ? 38  ILE C CB  1 
ATOM   6520  C  CG1 . ILE C 1 37  ? 1.466   -31.267 27.443  1.00 54.34  ? 38  ILE C CG1 1 
ATOM   6521  C  CG2 . ILE C 1 37  ? 1.407   -28.890 28.224  1.00 50.43  ? 38  ILE C CG2 1 
ATOM   6522  C  CD1 . ILE C 1 37  ? 0.958   -30.892 26.068  1.00 55.25  ? 38  ILE C CD1 1 
ATOM   6523  N  N   . TYR C 1 38  ? 0.063   -30.077 31.664  1.00 58.59  ? 39  TYR C N   1 
ATOM   6524  C  CA  . TYR C 1 38  ? -0.442  -29.243 32.752  1.00 58.17  ? 39  TYR C CA  1 
ATOM   6525  C  C   . TYR C 1 38  ? 0.447   -29.360 33.983  1.00 56.86  ? 39  TYR C C   1 
ATOM   6526  O  O   . TYR C 1 38  ? 0.761   -28.362 34.632  1.00 54.67  ? 39  TYR C O   1 
ATOM   6527  C  CB  . TYR C 1 38  ? -1.880  -29.631 33.101  1.00 46.73  ? 39  TYR C CB  1 
ATOM   6528  C  CG  . TYR C 1 38  ? -2.535  -28.762 34.150  1.00 46.65  ? 39  TYR C CG  1 
ATOM   6529  C  CD1 . TYR C 1 38  ? -2.860  -27.439 33.881  1.00 55.55  ? 39  TYR C CD1 1 
ATOM   6530  C  CD2 . TYR C 1 38  ? -2.847  -29.270 35.404  1.00 47.61  ? 39  TYR C CD2 1 
ATOM   6531  C  CE1 . TYR C 1 38  ? -3.466  -26.642 34.835  1.00 45.83  ? 39  TYR C CE1 1 
ATOM   6532  C  CE2 . TYR C 1 38  ? -3.456  -28.482 36.363  1.00 47.70  ? 39  TYR C CE2 1 
ATOM   6533  C  CZ  . TYR C 1 38  ? -3.762  -27.170 36.073  1.00 46.82  ? 39  TYR C CZ  1 
ATOM   6534  O  OH  . TYR C 1 38  ? -4.364  -26.382 37.027  1.00 53.45  ? 39  TYR C OH  1 
ATOM   6535  N  N   . GLY C 1 39  ? 0.845   -30.587 34.300  1.00 48.23  ? 40  GLY C N   1 
ATOM   6536  C  CA  . GLY C 1 39  ? 1.727   -30.830 35.425  1.00 49.16  ? 40  GLY C CA  1 
ATOM   6537  C  C   . GLY C 1 39  ? 3.135   -30.343 35.147  1.00 60.20  ? 40  GLY C C   1 
ATOM   6538  O  O   . GLY C 1 39  ? 3.828   -29.879 36.052  1.00 62.84  ? 40  GLY C O   1 
ATOM   6539  N  N   . ALA C 1 40  ? 3.553   -30.445 33.888  1.00 62.97  ? 41  ALA C N   1 
ATOM   6540  C  CA  . ALA C 1 40  ? 4.885   -30.011 33.479  1.00 58.54  ? 41  ALA C CA  1 
ATOM   6541  C  C   . ALA C 1 40  ? 5.098   -28.528 33.753  1.00 62.28  ? 41  ALA C C   1 
ATOM   6542  O  O   . ALA C 1 40  ? 6.221   -28.090 34.000  1.00 65.12  ? 41  ALA C O   1 
ATOM   6543  C  CB  . ALA C 1 40  ? 5.113   -30.309 32.005  1.00 58.89  ? 41  ALA C CB  1 
ATOM   6544  N  N   . LYS C 1 41  ? 4.015   -27.758 33.710  1.00 62.39  ? 42  LYS C N   1 
ATOM   6545  C  CA  . LYS C 1 41  ? 4.096   -26.322 33.941  1.00 60.70  ? 42  LYS C CA  1 
ATOM   6546  C  C   . LYS C 1 41  ? 3.920   -25.979 35.419  1.00 58.17  ? 42  LYS C C   1 
ATOM   6547  O  O   . LYS C 1 41  ? 3.736   -24.816 35.778  1.00 56.69  ? 42  LYS C O   1 
ATOM   6548  C  CB  . LYS C 1 41  ? 3.057   -25.587 33.092  1.00 64.83  ? 42  LYS C CB  1 
ATOM   6549  C  CG  . LYS C 1 41  ? 3.304   -25.721 31.597  1.00 65.37  ? 42  LYS C CG  1 
ATOM   6550  C  CD  . LYS C 1 41  ? 2.718   -24.556 30.823  1.00 66.58  ? 42  LYS C CD  1 
ATOM   6551  C  CE  . LYS C 1 41  ? 3.328   -24.464 29.433  1.00 69.00  ? 42  LYS C CE  1 
ATOM   6552  N  NZ  . LYS C 1 41  ? 2.985   -25.636 28.584  1.00 70.18  ? 42  LYS C NZ  1 
ATOM   6553  N  N   . GLY C 1 42  ? 3.977   -26.998 36.270  1.00 58.92  ? 43  GLY C N   1 
ATOM   6554  C  CA  . GLY C 1 42  ? 4.029   -26.791 37.706  1.00 57.78  ? 43  GLY C CA  1 
ATOM   6555  C  C   . GLY C 1 42  ? 2.730   -26.975 38.467  1.00 58.50  ? 43  GLY C C   1 
ATOM   6556  O  O   . GLY C 1 42  ? 2.738   -27.055 39.695  1.00 61.79  ? 43  GLY C O   1 
ATOM   6557  N  N   . PHE C 1 43  ? 1.612   -27.047 37.752  1.00 57.17  ? 44  PHE C N   1 
ATOM   6558  C  CA  . PHE C 1 43  ? 0.313   -27.128 38.411  1.00 59.46  ? 44  PHE C CA  1 
ATOM   6559  C  C   . PHE C 1 43  ? -0.007  -28.549 38.872  1.00 61.53  ? 44  PHE C C   1 
ATOM   6560  O  O   . PHE C 1 43  ? 0.773   -29.475 38.648  1.00 65.61  ? 44  PHE C O   1 
ATOM   6561  C  CB  . PHE C 1 43  ? -0.785  -26.613 37.482  1.00 56.48  ? 44  PHE C CB  1 
ATOM   6562  C  CG  . PHE C 1 43  ? -0.536  -25.227 36.964  1.00 54.65  ? 44  PHE C CG  1 
ATOM   6563  C  CD1 . PHE C 1 43  ? -0.482  -24.148 37.831  1.00 51.85  ? 44  PHE C CD1 1 
ATOM   6564  C  CD2 . PHE C 1 43  ? -0.365  -24.999 35.608  1.00 52.60  ? 44  PHE C CD2 1 
ATOM   6565  C  CE1 . PHE C 1 43  ? -0.253  -22.868 37.358  1.00 50.02  ? 44  PHE C CE1 1 
ATOM   6566  C  CE2 . PHE C 1 43  ? -0.138  -23.722 35.127  1.00 49.09  ? 44  PHE C CE2 1 
ATOM   6567  C  CZ  . PHE C 1 43  ? -0.082  -22.655 36.004  1.00 45.59  ? 44  PHE C CZ  1 
ATOM   6568  N  N   . SER C 1 44  ? -1.164  -28.715 39.507  1.00 60.49  ? 45  SER C N   1 
ATOM   6569  C  CA  . SER C 1 44  ? -1.529  -29.985 40.132  1.00 61.42  ? 45  SER C CA  1 
ATOM   6570  C  C   . SER C 1 44  ? -2.092  -30.998 39.140  1.00 59.41  ? 45  SER C C   1 
ATOM   6571  O  O   . SER C 1 44  ? -3.040  -30.710 38.411  1.00 56.76  ? 45  SER C O   1 
ATOM   6572  C  CB  . SER C 1 44  ? -2.543  -29.747 41.254  1.00 61.20  ? 45  SER C CB  1 
ATOM   6573  O  OG  . SER C 1 44  ? -2.919  -30.968 41.868  1.00 62.56  ? 45  SER C OG  1 
ATOM   6574  N  N   . LEU C 1 45  ? -1.509  -32.193 39.131  1.00 57.31  ? 46  LEU C N   1 
ATOM   6575  C  CA  . LEU C 1 45  ? -1.961  -33.269 38.256  1.00 58.68  ? 46  LEU C CA  1 
ATOM   6576  C  C   . LEU C 1 45  ? -3.359  -33.752 38.629  1.00 52.66  ? 46  LEU C C   1 
ATOM   6577  O  O   . LEU C 1 45  ? -4.069  -34.323 37.802  1.00 52.49  ? 46  LEU C O   1 
ATOM   6578  C  CB  . LEU C 1 45  ? -0.979  -34.443 38.306  1.00 57.87  ? 46  LEU C CB  1 
ATOM   6579  C  CG  . LEU C 1 45  ? 0.407   -34.225 37.698  1.00 57.56  ? 46  LEU C CG  1 
ATOM   6580  C  CD1 . LEU C 1 45  ? 1.330   -35.383 38.045  1.00 54.34  ? 46  LEU C CD1 1 
ATOM   6581  C  CD2 . LEU C 1 45  ? 0.303   -34.057 36.192  1.00 51.82  ? 46  LEU C CD2 1 
ATOM   6582  N  N   . SER C 1 46  ? -3.748  -33.516 39.878  1.00 56.68  ? 47  SER C N   1 
ATOM   6583  C  CA  . SER C 1 46  ? -5.020  -34.007 40.396  1.00 54.10  ? 47  SER C CA  1 
ATOM   6584  C  C   . SER C 1 46  ? -6.210  -33.215 39.866  1.00 55.06  ? 47  SER C C   1 
ATOM   6585  O  O   . SER C 1 46  ? -7.351  -33.673 39.939  1.00 56.87  ? 47  SER C O   1 
ATOM   6586  C  CB  . SER C 1 46  ? -5.009  -33.976 41.923  1.00 60.55  ? 47  SER C CB  1 
ATOM   6587  O  OG  . SER C 1 46  ? -3.967  -34.792 42.423  1.00 64.40  ? 47  SER C OG  1 
ATOM   6588  N  N   . ASP C 1 47  ? -5.941  -32.027 39.336  1.00 56.25  ? 48  ASP C N   1 
ATOM   6589  C  CA  . ASP C 1 47  ? -6.984  -31.204 38.737  1.00 54.96  ? 48  ASP C CA  1 
ATOM   6590  C  C   . ASP C 1 47  ? -7.547  -31.862 37.482  1.00 54.58  ? 48  ASP C C   1 
ATOM   6591  O  O   . ASP C 1 47  ? -8.755  -31.844 37.247  1.00 56.42  ? 48  ASP C O   1 
ATOM   6592  C  CB  . ASP C 1 47  ? -6.443  -29.813 38.398  1.00 56.34  ? 48  ASP C CB  1 
ATOM   6593  C  CG  . ASP C 1 47  ? -6.254  -28.942 39.625  1.00 59.73  ? 48  ASP C CG  1 
ATOM   6594  O  OD1 . ASP C 1 47  ? -6.499  -29.427 40.750  1.00 55.22  ? 48  ASP C OD1 1 
ATOM   6595  O  OD2 . ASP C 1 47  ? -5.856  -27.768 39.463  1.00 73.85  ? 48  ASP C OD2 1 
ATOM   6596  N  N   . VAL C 1 48  ? -6.660  -32.450 36.686  1.00 50.53  ? 49  VAL C N   1 
ATOM   6597  C  CA  . VAL C 1 48  ? -7.026  -32.982 35.379  1.00 50.17  ? 49  VAL C CA  1 
ATOM   6598  C  C   . VAL C 1 48  ? -7.965  -34.182 35.466  1.00 55.63  ? 49  VAL C C   1 
ATOM   6599  O  O   . VAL C 1 48  ? -7.666  -35.164 36.145  1.00 56.22  ? 49  VAL C O   1 
ATOM   6600  C  CB  . VAL C 1 48  ? -5.778  -33.394 34.581  1.00 49.95  ? 49  VAL C CB  1 
ATOM   6601  C  CG1 . VAL C 1 48  ? -6.161  -33.756 33.153  1.00 49.56  ? 49  VAL C CG1 1 
ATOM   6602  C  CG2 . VAL C 1 48  ? -4.751  -32.274 34.594  1.00 49.15  ? 49  VAL C CG2 1 
ATOM   6603  N  N   . PRO C 1 49  ? -9.110  -34.099 34.772  1.00 54.44  ? 50  PRO C N   1 
ATOM   6604  C  CA  . PRO C 1 49  ? -10.085 -35.191 34.673  1.00 53.63  ? 50  PRO C CA  1 
ATOM   6605  C  C   . PRO C 1 49  ? -9.522  -36.398 33.929  1.00 52.13  ? 50  PRO C C   1 
ATOM   6606  O  O   . PRO C 1 49  ? -8.580  -36.252 33.150  1.00 58.42  ? 50  PRO C O   1 
ATOM   6607  C  CB  . PRO C 1 49  ? -11.241 -34.563 33.883  1.00 51.14  ? 50  PRO C CB  1 
ATOM   6608  C  CG  . PRO C 1 49  ? -11.058 -33.088 34.027  1.00 59.94  ? 50  PRO C CG  1 
ATOM   6609  C  CD  . PRO C 1 49  ? -9.582  -32.878 34.098  1.00 49.82  ? 50  PRO C CD  1 
ATOM   6610  N  N   . GLN C 1 50  ? -10.093 -37.573 34.171  1.00 54.63  ? 51  GLN C N   1 
ATOM   6611  C  CA  A GLN C 1 50  ? -9.684  -38.794 33.485  0.59 57.56  ? 51  GLN C CA  1 
ATOM   6612  C  CA  B GLN C 1 50  ? -9.650  -38.778 33.480  0.41 57.32  ? 51  GLN C CA  1 
ATOM   6613  C  C   . GLN C 1 50  ? -9.988  -38.713 31.995  1.00 57.36  ? 51  GLN C C   1 
ATOM   6614  O  O   . GLN C 1 50  ? -9.178  -39.104 31.155  1.00 59.92  ? 51  GLN C O   1 
ATOM   6615  C  CB  A GLN C 1 50  ? -10.384 -40.008 34.097  0.59 59.75  ? 51  GLN C CB  1 
ATOM   6616  C  CB  B GLN C 1 50  ? -10.267 -40.025 34.113  0.41 58.98  ? 51  GLN C CB  1 
ATOM   6617  C  CG  A GLN C 1 50  ? -9.851  -40.408 35.459  0.59 59.29  ? 51  GLN C CG  1 
ATOM   6618  C  CG  B GLN C 1 50  ? -9.619  -40.427 35.427  0.41 60.31  ? 51  GLN C CG  1 
ATOM   6619  C  CD  A GLN C 1 50  ? -8.441  -40.951 35.384  0.59 61.11  ? 51  GLN C CD  1 
ATOM   6620  C  CD  B GLN C 1 50  ? -10.496 -40.133 36.623  0.41 59.96  ? 51  GLN C CD  1 
ATOM   6621  O  OE1 A GLN C 1 50  ? -7.468  -40.205 35.492  0.59 55.86  ? 51  GLN C OE1 1 
ATOM   6622  O  OE1 B GLN C 1 50  ? -11.238 -40.997 37.084  0.41 57.67  ? 51  GLN C OE1 1 
ATOM   6623  N  NE2 A GLN C 1 50  ? -8.322  -42.258 35.190  0.59 62.13  ? 51  GLN C NE2 1 
ATOM   6624  N  NE2 B GLN C 1 50  ? -10.415 -38.910 37.134  0.41 58.78  ? 51  GLN C NE2 1 
ATOM   6625  N  N   . ALA C 1 51  ? -11.178 -38.216 31.678  1.00 52.86  ? 52  ALA C N   1 
ATOM   6626  C  CA  . ALA C 1 51  ? -11.590 -38.048 30.293  1.00 52.38  ? 52  ALA C CA  1 
ATOM   6627  C  C   . ALA C 1 51  ? -12.249 -36.688 30.114  1.00 51.47  ? 52  ALA C C   1 
ATOM   6628  O  O   . ALA C 1 51  ? -12.412 -35.940 31.077  1.00 51.26  ? 52  ALA C O   1 
ATOM   6629  C  CB  . ALA C 1 51  ? -12.533 -39.164 29.875  1.00 60.53  ? 52  ALA C CB  1 
ATOM   6630  N  N   . GLU C 1 52  ? -12.643 -36.380 28.883  1.00 51.06  ? 53  GLU C N   1 
ATOM   6631  C  CA  . GLU C 1 52  ? -13.193 -35.068 28.566  1.00 57.26  ? 53  GLU C CA  1 
ATOM   6632  C  C   . GLU C 1 52  ? -14.551 -34.848 29.226  1.00 58.81  ? 53  GLU C C   1 
ATOM   6633  O  O   . GLU C 1 52  ? -15.412 -35.727 29.210  1.00 62.79  ? 53  GLU C O   1 
ATOM   6634  C  CB  . GLU C 1 52  ? -13.303 -34.891 27.049  1.00 54.64  ? 53  GLU C CB  1 
ATOM   6635  C  CG  . GLU C 1 52  ? -11.962 -34.668 26.363  1.00 53.49  ? 53  GLU C CG  1 
ATOM   6636  C  CD  . GLU C 1 52  ? -12.061 -34.681 24.850  1.00 54.42  ? 53  GLU C CD  1 
ATOM   6637  O  OE1 . GLU C 1 52  ? -13.194 -34.664 24.324  1.00 54.35  ? 53  GLU C OE1 1 
ATOM   6638  O  OE2 . GLU C 1 52  ? -11.002 -34.706 24.185  1.00 54.76  ? 53  GLU C OE2 1 
ATOM   6639  N  N   . ILE C 1 53  ? -14.730 -33.666 29.807  1.00 56.74  ? 54  ILE C N   1 
ATOM   6640  C  CA  . ILE C 1 53  ? -15.981 -33.316 30.468  1.00 56.96  ? 54  ILE C CA  1 
ATOM   6641  C  C   . ILE C 1 53  ? -16.677 -32.190 29.711  1.00 56.48  ? 54  ILE C C   1 
ATOM   6642  O  O   . ILE C 1 53  ? -16.144 -31.679 28.729  1.00 49.50  ? 54  ILE C O   1 
ATOM   6643  C  CB  . ILE C 1 53  ? -15.743 -32.886 31.927  1.00 56.69  ? 54  ILE C CB  1 
ATOM   6644  C  CG1 . ILE C 1 53  ? -14.851 -31.644 31.973  1.00 57.70  ? 54  ILE C CG1 1 
ATOM   6645  C  CG2 . ILE C 1 53  ? -15.112 -34.020 32.719  1.00 51.51  ? 54  ILE C CG2 1 
ATOM   6646  C  CD1 . ILE C 1 53  ? -14.551 -31.153 33.373  1.00 50.04  ? 54  ILE C CD1 1 
ATOM   6647  N  N   . SER C 1 54  ? -17.857 -31.792 30.175  1.00 56.96  ? 55  SER C N   1 
ATOM   6648  C  CA  . SER C 1 54  ? -18.611 -30.734 29.510  1.00 57.12  ? 55  SER C CA  1 
ATOM   6649  C  C   . SER C 1 54  ? -18.101 -29.364 29.943  1.00 54.12  ? 55  SER C C   1 
ATOM   6650  O  O   . SER C 1 54  ? -17.773 -29.153 31.110  1.00 50.69  ? 55  SER C O   1 
ATOM   6651  C  CB  . SER C 1 54  ? -20.108 -30.870 29.798  1.00 57.71  ? 55  SER C CB  1 
ATOM   6652  O  OG  . SER C 1 54  ? -20.362 -30.937 31.189  1.00 60.90  ? 55  SER C OG  1 
ATOM   6653  N  N   . GLY C 1 55  ? -18.044 -28.435 28.993  1.00 53.58  ? 56  GLY C N   1 
ATOM   6654  C  CA  . GLY C 1 55  ? -17.374 -27.163 29.197  1.00 58.21  ? 56  GLY C CA  1 
ATOM   6655  C  C   . GLY C 1 55  ? -18.245 -25.974 29.550  1.00 57.66  ? 56  GLY C C   1 
ATOM   6656  O  O   . GLY C 1 55  ? -17.846 -24.830 29.333  1.00 56.78  ? 56  GLY C O   1 
ATOM   6657  N  N   . GLU C 1 56  ? -19.434 -26.234 30.086  1.00 58.36  ? 57  GLU C N   1 
ATOM   6658  C  CA  . GLU C 1 56  ? -20.330 -25.164 30.517  1.00 59.36  ? 57  GLU C CA  1 
ATOM   6659  C  C   . GLU C 1 56  ? -19.687 -24.296 31.599  1.00 54.56  ? 57  GLU C C   1 
ATOM   6660  O  O   . GLU C 1 56  ? -20.127 -23.176 31.857  1.00 53.97  ? 57  GLU C O   1 
ATOM   6661  C  CB  . GLU C 1 56  ? -21.650 -25.746 31.029  1.00 61.55  ? 57  GLU C CB  1 
ATOM   6662  N  N   . HIS C 1 57  ? -18.639 -24.826 32.222  1.00 50.58  ? 58  HIS C N   1 
ATOM   6663  C  CA  . HIS C 1 57  ? -17.931 -24.137 33.292  1.00 55.19  ? 58  HIS C CA  1 
ATOM   6664  C  C   . HIS C 1 57  ? -16.781 -23.274 32.776  1.00 56.41  ? 58  HIS C C   1 
ATOM   6665  O  O   . HIS C 1 57  ? -16.078 -22.643 33.565  1.00 55.89  ? 58  HIS C O   1 
ATOM   6666  C  CB  . HIS C 1 57  ? -17.381 -25.152 34.291  1.00 59.09  ? 58  HIS C CB  1 
ATOM   6667  C  CG  . HIS C 1 57  ? -16.296 -26.014 33.725  1.00 62.40  ? 58  HIS C CG  1 
ATOM   6668  N  ND1 . HIS C 1 57  ? -16.556 -27.119 32.944  1.00 62.33  ? 58  HIS C ND1 1 
ATOM   6669  C  CD2 . HIS C 1 57  ? -14.948 -25.920 33.808  1.00 62.12  ? 58  HIS C CD2 1 
ATOM   6670  C  CE1 . HIS C 1 57  ? -15.414 -27.676 32.580  1.00 64.30  ? 58  HIS C CE1 1 
ATOM   6671  N  NE2 . HIS C 1 57  ? -14.424 -26.967 33.090  1.00 63.50  ? 58  HIS C NE2 1 
ATOM   6672  N  N   . LEU C 1 58  ? -16.587 -23.241 31.460  1.00 56.91  ? 59  LEU C N   1 
ATOM   6673  C  CA  . LEU C 1 58  ? -15.439 -22.536 30.895  1.00 58.83  ? 59  LEU C CA  1 
ATOM   6674  C  C   . LEU C 1 58  ? -15.734 -21.056 30.701  1.00 65.29  ? 59  LEU C C   1 
ATOM   6675  O  O   . LEU C 1 58  ? -16.609 -20.689 29.918  1.00 66.95  ? 59  LEU C O   1 
ATOM   6676  C  CB  . LEU C 1 58  ? -15.043 -23.152 29.551  1.00 56.76  ? 59  LEU C CB  1 
ATOM   6677  C  CG  . LEU C 1 58  ? -14.358 -24.517 29.542  1.00 59.53  ? 59  LEU C CG  1 
ATOM   6678  C  CD1 . LEU C 1 58  ? -14.241 -25.026 28.114  1.00 58.49  ? 59  LEU C CD1 1 
ATOM   6679  C  CD2 . LEU C 1 58  ? -12.987 -24.425 30.191  1.00 55.20  ? 59  LEU C CD2 1 
ATOM   6680  N  N   . ARG C 1 59  ? -15.007 -20.206 31.419  1.00 61.30  ? 60  ARG C N   1 
ATOM   6681  C  CA  . ARG C 1 59  ? -15.152 -18.769 31.236  1.00 59.73  ? 60  ARG C CA  1 
ATOM   6682  C  C   . ARG C 1 59  ? -14.518 -18.259 29.941  1.00 59.78  ? 60  ARG C C   1 
ATOM   6683  O  O   . ARG C 1 59  ? -15.183 -17.631 29.118  1.00 61.73  ? 60  ARG C O   1 
ATOM   6684  C  CB  . ARG C 1 59  ? -14.546 -18.027 32.429  1.00 59.05  ? 60  ARG C CB  1 
ATOM   6685  N  N   . ILE C 1 60  ? -13.224 -18.524 29.776  1.00 55.98  ? 61  ILE C N   1 
ATOM   6686  C  CA  . ILE C 1 60  ? -12.472 -18.002 28.635  1.00 51.83  ? 61  ILE C CA  1 
ATOM   6687  C  C   . ILE C 1 60  ? -12.605 -18.779 27.322  1.00 48.42  ? 61  ILE C C   1 
ATOM   6688  O  O   . ILE C 1 60  ? -12.863 -18.192 26.271  1.00 51.44  ? 61  ILE C O   1 
ATOM   6689  C  CB  . ILE C 1 60  ? -10.979 -17.901 28.985  1.00 49.95  ? 61  ILE C CB  1 
ATOM   6690  C  CG1 . ILE C 1 60  ? -10.802 -17.059 30.250  1.00 43.76  ? 61  ILE C CG1 1 
ATOM   6691  C  CG2 . ILE C 1 60  ? -10.199 -17.304 27.825  1.00 42.09  ? 61  ILE C CG2 1 
ATOM   6692  C  CD1 . ILE C 1 60  ? -9.410  -17.097 30.826  1.00 43.58  ? 61  ILE C CD1 1 
ATOM   6693  N  N   . CYS C 1 61  ? -12.443 -20.097 27.385  1.00 47.93  ? 62  CYS C N   1 
ATOM   6694  C  CA  . CYS C 1 61  ? -12.410 -20.909 26.171  1.00 49.09  ? 62  CYS C CA  1 
ATOM   6695  C  C   . CYS C 1 61  ? -13.812 -21.112 25.623  1.00 51.46  ? 62  CYS C C   1 
ATOM   6696  O  O   . CYS C 1 61  ? -14.783 -21.063 26.381  1.00 52.76  ? 62  CYS C O   1 
ATOM   6697  C  CB  . CYS C 1 61  ? -11.749 -22.266 26.437  1.00 43.57  ? 62  CYS C CB  1 
ATOM   6698  S  SG  . CYS C 1 61  ? -10.075 -22.187 27.112  1.00 78.62  ? 62  CYS C SG  1 
ATOM   6699  N  N   . PRO C 1 62  ? -13.928 -21.321 24.300  1.00 54.29  ? 63  PRO C N   1 
ATOM   6700  C  CA  . PRO C 1 62  ? -15.236 -21.679 23.746  1.00 57.79  ? 63  PRO C CA  1 
ATOM   6701  C  C   . PRO C 1 62  ? -15.783 -22.909 24.454  1.00 58.97  ? 63  PRO C C   1 
ATOM   6702  O  O   . PRO C 1 62  ? -15.075 -23.909 24.580  1.00 61.72  ? 63  PRO C O   1 
ATOM   6703  C  CB  . PRO C 1 62  ? -14.928 -21.972 22.277  1.00 55.38  ? 63  PRO C CB  1 
ATOM   6704  C  CG  . PRO C 1 62  ? -13.732 -21.132 21.981  1.00 55.92  ? 63  PRO C CG  1 
ATOM   6705  C  CD  . PRO C 1 62  ? -12.914 -21.137 23.247  1.00 54.96  ? 63  PRO C CD  1 
ATOM   6706  N  N   . GLN C 1 63  ? -17.026 -22.832 24.914  1.00 62.97  ? 64  GLN C N   1 
ATOM   6707  C  CA  . GLN C 1 63  ? -17.589 -23.902 25.720  1.00 64.80  ? 64  GLN C CA  1 
ATOM   6708  C  C   . GLN C 1 63  ? -17.857 -25.136 24.870  1.00 66.68  ? 64  GLN C C   1 
ATOM   6709  O  O   . GLN C 1 63  ? -18.559 -25.079 23.862  1.00 70.25  ? 64  GLN C O   1 
ATOM   6710  C  CB  . GLN C 1 63  ? -18.864 -23.429 26.417  1.00 65.99  ? 64  GLN C CB  1 
ATOM   6711  C  CG  . GLN C 1 63  ? -18.635 -22.229 27.328  1.00 63.81  ? 64  GLN C CG  1 
ATOM   6712  C  CD  . GLN C 1 63  ? -19.868 -21.839 28.115  1.00 67.33  ? 64  GLN C CD  1 
ATOM   6713  O  OE1 . GLN C 1 63  ? -20.993 -22.160 27.732  1.00 70.22  ? 64  GLN C OE1 1 
ATOM   6714  N  NE2 . GLN C 1 63  ? -19.663 -21.137 29.225  1.00 67.61  ? 64  GLN C NE2 1 
ATOM   6715  N  N   . GLY C 1 64  ? -17.277 -26.251 25.297  1.00 64.51  ? 65  GLY C N   1 
ATOM   6716  C  CA  . GLY C 1 64  ? -17.381 -27.512 24.592  1.00 64.33  ? 65  GLY C CA  1 
ATOM   6717  C  C   . GLY C 1 64  ? -16.700 -28.564 25.438  1.00 59.32  ? 65  GLY C C   1 
ATOM   6718  O  O   . GLY C 1 64  ? -16.285 -28.280 26.558  1.00 57.35  ? 65  GLY C O   1 
ATOM   6719  N  N   . TYR C 1 65  ? -16.568 -29.776 24.917  1.00 61.85  ? 66  TYR C N   1 
ATOM   6720  C  CA  . TYR C 1 65  ? -15.965 -30.838 25.709  1.00 61.68  ? 66  TYR C CA  1 
ATOM   6721  C  C   . TYR C 1 65  ? -14.474 -30.588 25.890  1.00 63.47  ? 66  TYR C C   1 
ATOM   6722  O  O   . TYR C 1 65  ? -13.731 -30.426 24.922  1.00 63.21  ? 66  TYR C O   1 
ATOM   6723  C  CB  . TYR C 1 65  ? -16.238 -32.197 25.071  1.00 59.63  ? 66  TYR C CB  1 
ATOM   6724  C  CG  . TYR C 1 65  ? -17.692 -32.576 25.194  1.00 58.13  ? 66  TYR C CG  1 
ATOM   6725  C  CD1 . TYR C 1 65  ? -18.235 -32.902 26.430  1.00 58.28  ? 66  TYR C CD1 1 
ATOM   6726  C  CD2 . TYR C 1 65  ? -18.531 -32.575 24.088  1.00 57.45  ? 66  TYR C CD2 1 
ATOM   6727  C  CE1 . TYR C 1 65  ? -19.565 -33.235 26.560  1.00 59.37  ? 66  TYR C CE1 1 
ATOM   6728  C  CE2 . TYR C 1 65  ? -19.867 -32.909 24.208  1.00 58.45  ? 66  TYR C CE2 1 
ATOM   6729  C  CZ  . TYR C 1 65  ? -20.377 -33.238 25.448  1.00 59.74  ? 66  TYR C CZ  1 
ATOM   6730  O  OH  . TYR C 1 65  ? -21.703 -33.569 25.584  1.00 60.91  ? 66  TYR C OH  1 
ATOM   6731  N  N   . THR C 1 66  ? -14.053 -30.554 27.150  1.00 61.05  ? 67  THR C N   1 
ATOM   6732  C  CA  . THR C 1 66  ? -12.723 -30.083 27.503  1.00 56.37  ? 67  THR C CA  1 
ATOM   6733  C  C   . THR C 1 66  ? -12.044 -30.954 28.553  1.00 51.44  ? 67  THR C C   1 
ATOM   6734  O  O   . THR C 1 66  ? -12.705 -31.635 29.336  1.00 48.24  ? 67  THR C O   1 
ATOM   6735  C  CB  . THR C 1 66  ? -12.774 -28.634 28.030  1.00 53.74  ? 67  THR C CB  1 
ATOM   6736  O  OG1 . THR C 1 66  ? -11.459 -28.211 28.411  1.00 50.75  ? 67  THR C OG1 1 
ATOM   6737  C  CG2 . THR C 1 66  ? -13.700 -28.540 29.236  1.00 52.78  ? 67  THR C CG2 1 
ATOM   6738  N  N   . CYS C 1 67  ? -10.715 -30.924 28.557  1.00 49.09  ? 68  CYS C N   1 
ATOM   6739  C  CA  . CYS C 1 67  ? -9.931  -31.589 29.588  1.00 48.97  ? 68  CYS C CA  1 
ATOM   6740  C  C   . CYS C 1 67  ? -9.582  -30.608 30.700  1.00 51.28  ? 68  CYS C C   1 
ATOM   6741  O  O   . CYS C 1 67  ? -8.889  -30.957 31.653  1.00 52.00  ? 68  CYS C O   1 
ATOM   6742  C  CB  . CYS C 1 67  ? -8.656  -32.193 28.996  1.00 48.97  ? 68  CYS C CB  1 
ATOM   6743  S  SG  . CYS C 1 67  ? -8.921  -33.673 27.995  1.00 90.64  ? 68  CYS C SG  1 
ATOM   6744  N  N   . CYS C 1 68  ? -10.065 -29.377 30.567  1.00 50.89  ? 69  CYS C N   1 
ATOM   6745  C  CA  . CYS C 1 68  ? -9.772  -28.330 31.538  1.00 51.93  ? 69  CYS C CA  1 
ATOM   6746  C  C   . CYS C 1 68  ? -10.928 -28.093 32.502  1.00 46.90  ? 69  CYS C C   1 
ATOM   6747  O  O   . CYS C 1 68  ? -12.071 -27.906 32.085  1.00 47.05  ? 69  CYS C O   1 
ATOM   6748  C  CB  . CYS C 1 68  ? -9.426  -27.018 30.825  1.00 45.35  ? 69  CYS C CB  1 
ATOM   6749  S  SG  . CYS C 1 68  ? -7.798  -26.982 30.042  1.00 59.01  ? 69  CYS C SG  1 
ATOM   6750  N  N   . THR C 1 69  ? -10.623 -28.106 33.795  1.00 47.37  ? 70  THR C N   1 
ATOM   6751  C  CA  . THR C 1 69  ? -11.571 -27.663 34.807  1.00 47.99  ? 70  THR C CA  1 
ATOM   6752  C  C   . THR C 1 69  ? -11.398 -26.158 34.996  1.00 63.72  ? 70  THR C C   1 
ATOM   6753  O  O   . THR C 1 69  ? -10.565 -25.541 34.332  1.00 46.55  ? 70  THR C O   1 
ATOM   6754  C  CB  . THR C 1 69  ? -11.373 -28.399 36.147  1.00 50.78  ? 70  THR C CB  1 
ATOM   6755  O  OG1 . THR C 1 69  ? -10.034 -28.199 36.615  1.00 50.28  ? 70  THR C OG1 1 
ATOM   6756  C  CG2 . THR C 1 69  ? -11.629 -29.891 35.980  1.00 49.67  ? 70  THR C CG2 1 
ATOM   6757  N  N   . SER C 1 70  ? -12.183 -25.569 35.892  1.00 62.02  ? 71  SER C N   1 
ATOM   6758  C  CA  . SER C 1 70  ? -12.122 -24.128 36.126  1.00 62.71  ? 71  SER C CA  1 
ATOM   6759  C  C   . SER C 1 70  ? -10.756 -23.725 36.688  1.00 58.47  ? 71  SER C C   1 
ATOM   6760  O  O   . SER C 1 70  ? -10.150 -22.737 36.248  1.00 62.76  ? 71  SER C O   1 
ATOM   6761  C  CB  . SER C 1 70  ? -13.245 -23.696 37.072  1.00 67.10  ? 71  SER C CB  1 
ATOM   6762  O  OG  . SER C 1 70  ? -13.625 -22.351 36.835  1.00 72.52  ? 71  SER C OG  1 
ATOM   6763  N  N   . GLU C 1 71  ? -10.281 -24.505 37.657  1.00 56.81  ? 72  GLU C N   1 
ATOM   6764  C  CA  . GLU C 1 71  ? -8.943  -24.343 38.221  1.00 59.11  ? 72  GLU C CA  1 
ATOM   6765  C  C   . GLU C 1 71  ? -7.884  -24.309 37.125  1.00 55.23  ? 72  GLU C C   1 
ATOM   6766  O  O   . GLU C 1 71  ? -7.029  -23.416 37.087  1.00 54.14  ? 72  GLU C O   1 
ATOM   6767  C  CB  . GLU C 1 71  ? -8.637  -25.481 39.198  1.00 60.35  ? 72  GLU C CB  1 
ATOM   6768  C  CG  . GLU C 1 71  ? -8.906  -25.169 40.661  1.00 65.30  ? 72  GLU C CG  1 
ATOM   6769  C  CD  . GLU C 1 71  ? -8.847  -26.412 41.532  1.00 70.76  ? 72  GLU C CD  1 
ATOM   6770  O  OE1 . GLU C 1 71  ? -9.296  -27.481 41.070  1.00 74.65  ? 72  GLU C OE1 1 
ATOM   6771  O  OE2 . GLU C 1 71  ? -8.339  -26.330 42.670  1.00 75.30  ? 72  GLU C OE2 1 
ATOM   6772  N  N   . MET C 1 72  ? -7.957  -25.292 36.233  1.00 55.45  ? 73  MET C N   1 
ATOM   6773  C  CA  . MET C 1 72  ? -7.013  -25.414 35.130  1.00 53.90  ? 73  MET C CA  1 
ATOM   6774  C  C   . MET C 1 72  ? -7.065  -24.206 34.205  1.00 49.76  ? 73  MET C C   1 
ATOM   6775  O  O   . MET C 1 72  ? -6.028  -23.716 33.762  1.00 48.33  ? 73  MET C O   1 
ATOM   6776  C  CB  . MET C 1 72  ? -7.282  -26.690 34.330  1.00 55.74  ? 73  MET C CB  1 
ATOM   6777  C  CG  . MET C 1 72  ? -6.977  -27.975 35.081  1.00 57.30  ? 73  MET C CG  1 
ATOM   6778  S  SD  . MET C 1 72  ? -7.457  -29.436 34.144  1.00 52.91  ? 73  MET C SD  1 
ATOM   6779  C  CE  . MET C 1 72  ? -6.264  -29.381 32.809  1.00 49.42  ? 73  MET C CE  1 
ATOM   6780  N  N   . GLU C 1 73  ? -8.271  -23.726 33.912  1.00 52.58  ? 74  GLU C N   1 
ATOM   6781  C  CA  . GLU C 1 73  ? -8.419  -22.577 33.026  1.00 57.39  ? 74  GLU C CA  1 
ATOM   6782  C  C   . GLU C 1 73  ? -7.814  -21.327 33.654  1.00 55.16  ? 74  GLU C C   1 
ATOM   6783  O  O   . GLU C 1 73  ? -7.076  -20.591 32.991  1.00 59.14  ? 74  GLU C O   1 
ATOM   6784  C  CB  . GLU C 1 73  ? -9.888  -22.332 32.676  1.00 54.64  ? 74  GLU C CB  1 
ATOM   6785  C  CG  . GLU C 1 73  ? -10.101 -21.936 31.219  1.00 53.12  ? 74  GLU C CG  1 
ATOM   6786  C  CD  . GLU C 1 73  ? -11.430 -21.246 30.978  1.00 50.20  ? 74  GLU C CD  1 
ATOM   6787  O  OE1 . GLU C 1 73  ? -11.990 -20.677 31.937  1.00 53.69  ? 74  GLU C OE1 1 
ATOM   6788  O  OE2 . GLU C 1 73  ? -11.912 -21.266 29.825  1.00 45.57  ? 74  GLU C OE2 1 
ATOM   6789  N  N   . GLU C 1 74  ? -8.112  -21.093 34.930  1.00 64.38  ? 75  GLU C N   1 
ATOM   6790  C  CA  . GLU C 1 74  ? -7.545  -19.936 35.622  1.00 66.68  ? 75  GLU C CA  1 
ATOM   6791  C  C   . GLU C 1 74  ? -6.015  -20.004 35.673  1.00 63.06  ? 75  GLU C C   1 
ATOM   6792  O  O   . GLU C 1 74  ? -5.327  -19.021 35.365  1.00 63.57  ? 75  GLU C O   1 
ATOM   6793  C  CB  . GLU C 1 74  ? -8.120  -19.809 37.037  1.00 72.81  ? 75  GLU C CB  1 
ATOM   6794  C  CG  . GLU C 1 74  ? -9.637  -19.678 37.074  1.00 82.41  ? 75  GLU C CG  1 
ATOM   6795  C  CD  . GLU C 1 74  ? -10.164 -19.175 38.407  1.00 90.47  ? 75  GLU C CD  1 
ATOM   6796  O  OE1 . GLU C 1 74  ? -9.384  -18.573 39.176  1.00 92.73  ? 75  GLU C OE1 1 
ATOM   6797  O  OE2 . GLU C 1 74  ? -11.367 -19.374 38.680  1.00 92.28  ? 75  GLU C OE2 1 
ATOM   6798  N  N   . ASN C 1 75  ? -5.489  -21.172 36.039  1.00 57.07  ? 76  ASN C N   1 
ATOM   6799  C  CA  . ASN C 1 75  ? -4.041  -21.373 36.100  1.00 52.33  ? 76  ASN C CA  1 
ATOM   6800  C  C   . ASN C 1 75  ? -3.344  -21.160 34.756  1.00 53.99  ? 76  ASN C C   1 
ATOM   6801  O  O   . ASN C 1 75  ? -2.321  -20.476 34.680  1.00 51.90  ? 76  ASN C O   1 
ATOM   6802  C  CB  . ASN C 1 75  ? -3.718  -22.776 36.624  1.00 48.74  ? 76  ASN C CB  1 
ATOM   6803  C  CG  . ASN C 1 75  ? -3.890  -22.894 38.126  1.00 51.65  ? 76  ASN C CG  1 
ATOM   6804  O  OD1 . ASN C 1 75  ? -3.885  -21.894 38.844  1.00 55.52  ? 76  ASN C OD1 1 
ATOM   6805  N  ND2 . ASN C 1 75  ? -4.026  -24.125 38.612  1.00 48.41  ? 76  ASN C ND2 1 
ATOM   6806  N  N   . LEU C 1 76  ? -3.900  -21.747 33.699  1.00 54.21  ? 77  LEU C N   1 
ATOM   6807  C  CA  . LEU C 1 76  ? -3.324  -21.621 32.363  1.00 51.93  ? 77  LEU C CA  1 
ATOM   6808  C  C   . LEU C 1 76  ? -3.395  -20.181 31.859  1.00 53.86  ? 77  LEU C C   1 
ATOM   6809  O  O   . LEU C 1 76  ? -2.461  -19.694 31.213  1.00 54.35  ? 77  LEU C O   1 
ATOM   6810  C  CB  . LEU C 1 76  ? -4.029  -22.563 31.385  1.00 50.64  ? 77  LEU C CB  1 
ATOM   6811  C  CG  . LEU C 1 76  ? -3.707  -24.050 31.559  1.00 45.20  ? 77  LEU C CG  1 
ATOM   6812  C  CD1 . LEU C 1 76  ? -4.594  -24.911 30.672  1.00 48.53  ? 77  LEU C CD1 1 
ATOM   6813  C  CD2 . LEU C 1 76  ? -2.236  -24.314 31.270  1.00 43.03  ? 77  LEU C CD2 1 
ATOM   6814  N  N   . ALA C 1 77  ? -4.501  -19.504 32.159  1.00 51.29  ? 78  ALA C N   1 
ATOM   6815  C  CA  . ALA C 1 77  ? -4.633  -18.087 31.830  1.00 48.36  ? 78  ALA C CA  1 
ATOM   6816  C  C   . ALA C 1 77  ? -3.517  -17.287 32.495  1.00 43.96  ? 78  ALA C C   1 
ATOM   6817  O  O   . ALA C 1 77  ? -2.787  -16.537 31.830  1.00 45.92  ? 78  ALA C O   1 
ATOM   6818  C  CB  . ALA C 1 77  ? -5.993  -17.563 32.258  1.00 47.77  ? 78  ALA C CB  1 
ATOM   6819  N  N   . ASN C 1 78  ? -3.394  -17.465 33.811  1.00 45.11  ? 79  ASN C N   1 
ATOM   6820  C  CA  . ASN C 1 78  ? -2.336  -16.833 34.596  1.00 48.23  ? 79  ASN C CA  1 
ATOM   6821  C  C   . ASN C 1 78  ? -0.960  -17.062 33.970  1.00 52.01  ? 79  ASN C C   1 
ATOM   6822  O  O   . ASN C 1 78  ? -0.158  -16.129 33.813  1.00 56.02  ? 79  ASN C O   1 
ATOM   6823  C  CB  . ASN C 1 78  ? -2.360  -17.373 36.030  1.00 52.02  ? 79  ASN C CB  1 
ATOM   6824  C  CG  . ASN C 1 78  ? -2.034  -16.312 37.065  1.00 56.40  ? 79  ASN C CG  1 
ATOM   6825  O  OD1 . ASN C 1 78  ? -2.865  -15.459 37.378  1.00 63.83  ? 79  ASN C OD1 1 
ATOM   6826  N  ND2 . ASN C 1 78  ? -0.827  -16.373 37.617  1.00 54.11  ? 79  ASN C ND2 1 
ATOM   6827  N  N   . ARG C 1 79  ? -0.711  -18.313 33.592  1.00 53.07  ? 80  ARG C N   1 
ATOM   6828  C  CA  . ARG C 1 79  ? 0.553   -18.707 32.983  1.00 52.99  ? 80  ARG C CA  1 
ATOM   6829  C  C   . ARG C 1 79  ? 0.826   -17.969 31.675  1.00 49.31  ? 80  ARG C C   1 
ATOM   6830  O  O   . ARG C 1 79  ? 1.868   -17.332 31.533  1.00 54.50  ? 80  ARG C O   1 
ATOM   6831  C  CB  . ARG C 1 79  ? 0.577   -20.219 32.745  1.00 49.61  ? 80  ARG C CB  1 
ATOM   6832  C  CG  . ARG C 1 79  ? 1.892   -20.751 32.185  1.00 49.40  ? 80  ARG C CG  1 
ATOM   6833  C  CD  . ARG C 1 79  ? 3.095   -20.213 32.949  1.00 52.49  ? 80  ARG C CD  1 
ATOM   6834  N  NE  . ARG C 1 79  ? 2.944   -20.351 34.395  1.00 52.82  ? 80  ARG C NE  1 
ATOM   6835  C  CZ  . ARG C 1 79  ? 3.437   -21.359 35.107  1.00 59.04  ? 80  ARG C CZ  1 
ATOM   6836  N  NH1 . ARG C 1 79  ? 4.120   -22.325 34.507  1.00 61.23  ? 80  ARG C NH1 1 
ATOM   6837  N  NH2 . ARG C 1 79  ? 3.249   -21.400 36.419  1.00 60.42  ? 80  ARG C NH2 1 
ATOM   6838  N  N   . SER C 1 80  ? -0.104  -18.053 30.727  1.00 49.46  ? 81  SER C N   1 
ATOM   6839  C  CA  . SER C 1 80  ? 0.078   -17.406 29.427  1.00 45.56  ? 81  SER C CA  1 
ATOM   6840  C  C   . SER C 1 80  ? 0.274   -15.896 29.575  1.00 46.81  ? 81  SER C C   1 
ATOM   6841  O  O   . SER C 1 80  ? 1.126   -15.297 28.901  1.00 44.53  ? 81  SER C O   1 
ATOM   6842  C  CB  . SER C 1 80  ? -1.112  -17.700 28.507  1.00 40.96  ? 81  SER C CB  1 
ATOM   6843  O  OG  . SER C 1 80  ? -2.342  -17.379 29.133  1.00 41.27  ? 81  SER C OG  1 
ATOM   6844  N  N   . HIS C 1 81  ? -0.510  -15.293 30.466  1.00 46.85  ? 82  HIS C N   1 
ATOM   6845  C  CA  . HIS C 1 81  ? -0.365  -13.872 30.777  1.00 49.26  ? 82  HIS C CA  1 
ATOM   6846  C  C   . HIS C 1 81  ? 1.058   -13.548 31.238  1.00 50.04  ? 82  HIS C C   1 
ATOM   6847  O  O   . HIS C 1 81  ? 1.738   -12.675 30.666  1.00 47.25  ? 82  HIS C O   1 
ATOM   6848  C  CB  . HIS C 1 81  ? -1.375  -13.462 31.850  1.00 47.88  ? 82  HIS C CB  1 
ATOM   6849  C  CG  . HIS C 1 81  ? -1.273  -12.026 32.260  1.00 53.73  ? 82  HIS C CG  1 
ATOM   6850  N  ND1 . HIS C 1 81  ? -1.998  -11.024 31.650  1.00 56.72  ? 82  HIS C ND1 1 
ATOM   6851  C  CD2 . HIS C 1 81  ? -0.533  -11.423 33.221  1.00 53.15  ? 82  HIS C CD2 1 
ATOM   6852  C  CE1 . HIS C 1 81  ? -1.708  -9.867  32.217  1.00 54.98  ? 82  HIS C CE1 1 
ATOM   6853  N  NE2 . HIS C 1 81  ? -0.822  -10.081 33.173  1.00 53.11  ? 82  HIS C NE2 1 
ATOM   6854  N  N   . ALA C 1 82  ? 1.501   -14.267 32.269  1.00 50.13  ? 83  ALA C N   1 
ATOM   6855  C  CA  . ALA C 1 82  ? 2.842   -14.086 32.817  1.00 55.68  ? 83  ALA C CA  1 
ATOM   6856  C  C   . ALA C 1 82  ? 3.918   -14.234 31.742  1.00 57.17  ? 83  ALA C C   1 
ATOM   6857  O  O   . ALA C 1 82  ? 4.880   -13.462 31.700  1.00 60.91  ? 83  ALA C O   1 
ATOM   6858  C  CB  . ALA C 1 82  ? 3.086   -15.076 33.946  1.00 54.96  ? 83  ALA C CB  1 
ATOM   6859  N  N   . GLU C 1 83  ? 3.742   -15.222 30.870  1.00 58.30  ? 84  GLU C N   1 
ATOM   6860  C  CA  . GLU C 1 83  ? 4.690   -15.482 29.792  1.00 58.02  ? 84  GLU C CA  1 
ATOM   6861  C  C   . GLU C 1 83  ? 4.768   -14.308 28.818  1.00 55.77  ? 84  GLU C C   1 
ATOM   6862  O  O   . GLU C 1 83  ? 5.868   -13.855 28.457  1.00 58.32  ? 84  GLU C O   1 
ATOM   6863  C  CB  . GLU C 1 83  ? 4.310   -16.769 29.053  1.00 62.51  ? 84  GLU C CB  1 
ATOM   6864  C  CG  . GLU C 1 83  ? 4.483   -18.029 29.892  1.00 69.54  ? 84  GLU C CG  1 
ATOM   6865  C  CD  . GLU C 1 83  ? 3.970   -19.278 29.199  1.00 73.71  ? 84  GLU C CD  1 
ATOM   6866  O  OE1 . GLU C 1 83  ? 4.539   -20.365 29.438  1.00 74.86  ? 84  GLU C OE1 1 
ATOM   6867  O  OE2 . GLU C 1 83  ? 2.996   -19.176 28.424  1.00 72.80  ? 84  GLU C OE2 1 
ATOM   6868  N  N   . LEU C 1 84  ? 3.605   -13.809 28.399  1.00 50.50  ? 85  LEU C N   1 
ATOM   6869  C  CA  . LEU C 1 84  ? 3.576   -12.659 27.498  1.00 48.70  ? 85  LEU C CA  1 
ATOM   6870  C  C   . LEU C 1 84  ? 4.267   -11.453 28.134  1.00 49.80  ? 85  LEU C C   1 
ATOM   6871  O  O   . LEU C 1 84  ? 5.100   -10.794 27.493  1.00 48.87  ? 85  LEU C O   1 
ATOM   6872  C  CB  . LEU C 1 84  ? 2.142   -12.297 27.107  1.00 45.77  ? 85  LEU C CB  1 
ATOM   6873  C  CG  . LEU C 1 84  ? 2.035   -11.094 26.162  1.00 44.15  ? 85  LEU C CG  1 
ATOM   6874  C  CD1 . LEU C 1 84  ? 2.893   -11.303 24.923  1.00 39.87  ? 85  LEU C CD1 1 
ATOM   6875  C  CD2 . LEU C 1 84  ? 0.592   -10.826 25.768  1.00 42.35  ? 85  LEU C CD2 1 
ATOM   6876  N  N   . GLU C 1 85  ? 3.934   -11.175 29.395  1.00 53.36  ? 86  GLU C N   1 
ATOM   6877  C  CA  . GLU C 1 85  ? 4.569   -10.058 30.095  1.00 57.86  ? 86  GLU C CA  1 
ATOM   6878  C  C   . GLU C 1 85  ? 6.088   -10.229 30.164  1.00 57.65  ? 86  GLU C C   1 
ATOM   6879  O  O   . GLU C 1 85  ? 6.840   -9.260  30.013  1.00 60.95  ? 86  GLU C O   1 
ATOM   6880  C  CB  . GLU C 1 85  ? 3.990   -9.898  31.502  1.00 66.67  ? 86  GLU C CB  1 
ATOM   6881  C  CG  . GLU C 1 85  ? 2.655   -9.169  31.534  1.00 74.10  ? 86  GLU C CG  1 
ATOM   6882  C  CD  . GLU C 1 85  ? 2.260   -8.725  32.929  1.00 81.32  ? 86  GLU C CD  1 
ATOM   6883  O  OE1 . GLU C 1 85  ? 2.802   -9.281  33.908  1.00 83.39  ? 86  GLU C OE1 1 
ATOM   6884  O  OE2 . GLU C 1 85  ? 1.412   -7.815  33.046  1.00 82.63  ? 86  GLU C OE2 1 
ATOM   6885  N  N   . THR C 1 86  ? 6.532   -11.465 30.376  1.00 53.04  ? 87  THR C N   1 
ATOM   6886  C  CA  . THR C 1 86  ? 7.960   -11.771 30.410  1.00 50.14  ? 87  THR C CA  1 
ATOM   6887  C  C   . THR C 1 86  ? 8.636   -11.452 29.077  1.00 49.32  ? 87  THR C C   1 
ATOM   6888  O  O   . THR C 1 86  ? 9.645   -10.738 29.040  1.00 48.95  ? 87  THR C O   1 
ATOM   6889  C  CB  . THR C 1 86  ? 8.213   -13.250 30.764  1.00 44.71  ? 87  THR C CB  1 
ATOM   6890  O  OG1 . THR C 1 86  ? 7.989   -13.448 32.165  1.00 49.23  ? 87  THR C OG1 1 
ATOM   6891  C  CG2 . THR C 1 86  ? 9.645   -13.644 30.433  1.00 42.70  ? 87  THR C CG2 1 
ATOM   6892  N  N   . ALA C 1 87  ? 8.078   -11.978 27.987  1.00 50.19  ? 88  ALA C N   1 
ATOM   6893  C  CA  . ALA C 1 87  ? 8.629   -11.717 26.655  1.00 51.27  ? 88  ALA C CA  1 
ATOM   6894  C  C   . ALA C 1 87  ? 8.710   -10.214 26.375  1.00 50.46  ? 88  ALA C C   1 
ATOM   6895  O  O   . ALA C 1 87  ? 9.749   -9.693  25.918  1.00 52.71  ? 88  ALA C O   1 
ATOM   6896  C  CB  . ALA C 1 87  ? 7.793   -12.414 25.592  1.00 37.64  ? 88  ALA C CB  1 
ATOM   6897  N  N   . LEU C 1 88  ? 7.610   -9.524  26.668  1.00 47.17  ? 89  LEU C N   1 
ATOM   6898  C  CA  . LEU C 1 88  ? 7.546   -8.075  26.509  1.00 44.95  ? 89  LEU C CA  1 
ATOM   6899  C  C   . LEU C 1 88  ? 8.669   -7.367  27.261  1.00 43.95  ? 89  LEU C C   1 
ATOM   6900  O  O   . LEU C 1 88  ? 9.388   -6.537  26.688  1.00 48.19  ? 89  LEU C O   1 
ATOM   6901  C  CB  . LEU C 1 88  ? 6.190   -7.548  26.981  1.00 44.54  ? 89  LEU C CB  1 
ATOM   6902  C  CG  . LEU C 1 88  ? 5.104   -7.470  25.910  1.00 46.73  ? 89  LEU C CG  1 
ATOM   6903  C  CD1 . LEU C 1 88  ? 3.736   -7.269  26.543  1.00 46.59  ? 89  LEU C CD1 1 
ATOM   6904  C  CD2 . LEU C 1 88  ? 5.418   -6.347  24.932  1.00 45.53  ? 89  LEU C CD2 1 
ATOM   6905  N  N   . ARG C 1 89  ? 8.822   -7.701  28.540  1.00 47.97  ? 90  ARG C N   1 
ATOM   6906  C  CA  . ARG C 1 89  ? 9.857   -7.076  29.356  1.00 52.03  ? 90  ARG C CA  1 
ATOM   6907  C  C   . ARG C 1 89  ? 11.246  -7.366  28.795  1.00 54.74  ? 90  ARG C C   1 
ATOM   6908  O  O   . ARG C 1 89  ? 12.132  -6.511  28.848  1.00 57.91  ? 90  ARG C O   1 
ATOM   6909  C  CB  . ARG C 1 89  ? 9.768   -7.546  30.809  1.00 55.54  ? 90  ARG C CB  1 
ATOM   6910  C  CG  . ARG C 1 89  ? 9.779   -6.404  31.815  1.00 66.51  ? 90  ARG C CG  1 
ATOM   6911  C  CD  . ARG C 1 89  ? 9.752   -6.915  33.245  1.00 72.93  ? 90  ARG C CD  1 
ATOM   6912  N  NE  . ARG C 1 89  ? 8.813   -8.020  33.414  1.00 80.91  ? 90  ARG C NE  1 
ATOM   6913  C  CZ  . ARG C 1 89  ? 9.113   -9.166  34.016  1.00 83.46  ? 90  ARG C CZ  1 
ATOM   6914  N  NH1 . ARG C 1 89  ? 10.327  -9.358  34.514  1.00 83.98  ? 90  ARG C NH1 1 
ATOM   6915  N  NH2 . ARG C 1 89  ? 8.198   -10.120 34.125  1.00 82.87  ? 90  ARG C NH2 1 
ATOM   6916  N  N   . ASP C 1 90  ? 11.428  -8.567  28.252  1.00 54.29  ? 91  ASP C N   1 
ATOM   6917  C  CA  . ASP C 1 90  ? 12.693  -8.925  27.616  1.00 52.56  ? 91  ASP C CA  1 
ATOM   6918  C  C   . ASP C 1 90  ? 13.003  -7.995  26.444  1.00 51.05  ? 91  ASP C C   1 
ATOM   6919  O  O   . ASP C 1 90  ? 14.085  -7.387  26.389  1.00 49.83  ? 91  ASP C O   1 
ATOM   6920  C  CB  . ASP C 1 90  ? 12.669  -10.380 27.144  1.00 57.89  ? 91  ASP C CB  1 
ATOM   6921  C  CG  . ASP C 1 90  ? 12.596  -11.364 28.296  1.00 66.36  ? 91  ASP C CG  1 
ATOM   6922  O  OD1 . ASP C 1 90  ? 13.006  -10.997 29.417  1.00 66.01  ? 91  ASP C OD1 1 
ATOM   6923  O  OD2 . ASP C 1 90  ? 12.130  -12.503 28.079  1.00 65.33  ? 91  ASP C OD2 1 
ATOM   6924  N  N   . SER C 1 91  ? 12.053  -7.879  25.516  1.00 47.27  ? 92  SER C N   1 
ATOM   6925  C  CA  . SER C 1 91  ? 12.234  -6.985  24.367  1.00 50.03  ? 92  SER C CA  1 
ATOM   6926  C  C   . SER C 1 91  ? 12.543  -5.550  24.805  1.00 44.69  ? 92  SER C C   1 
ATOM   6927  O  O   . SER C 1 91  ? 13.548  -4.938  24.382  1.00 42.62  ? 92  SER C O   1 
ATOM   6928  C  CB  . SER C 1 91  ? 10.989  -6.996  23.477  1.00 50.64  ? 92  SER C CB  1 
ATOM   6929  O  OG  . SER C 1 91  ? 10.928  -8.177  22.697  1.00 56.48  ? 92  SER C OG  1 
ATOM   6930  N  N   . SER C 1 92  ? 11.674  -5.027  25.666  1.00 42.34  ? 93  SER C N   1 
ATOM   6931  C  CA  . SER C 1 92  ? 11.807  -3.660  26.151  1.00 45.33  ? 93  SER C CA  1 
ATOM   6932  C  C   . SER C 1 92  ? 13.164  -3.413  26.798  1.00 46.17  ? 93  SER C C   1 
ATOM   6933  O  O   . SER C 1 92  ? 13.768  -2.365  26.592  1.00 46.41  ? 93  SER C O   1 
ATOM   6934  C  CB  . SER C 1 92  ? 10.697  -3.332  27.147  1.00 46.65  ? 93  SER C CB  1 
ATOM   6935  O  OG  . SER C 1 92  ? 10.928  -2.068  27.741  1.00 49.67  ? 93  SER C OG  1 
ATOM   6936  N  N   . ARG C 1 93  ? 13.646  -4.382  27.571  1.00 46.04  ? 94  ARG C N   1 
ATOM   6937  C  CA  . ARG C 1 93  ? 14.917  -4.218  28.269  1.00 45.62  ? 94  ARG C CA  1 
ATOM   6938  C  C   . ARG C 1 93  ? 16.110  -4.345  27.326  1.00 43.46  ? 94  ARG C C   1 
ATOM   6939  O  O   . ARG C 1 93  ? 17.154  -3.731  27.559  1.00 45.31  ? 94  ARG C O   1 
ATOM   6940  C  CB  . ARG C 1 93  ? 15.034  -5.222  29.414  1.00 51.92  ? 94  ARG C CB  1 
ATOM   6941  C  CG  . ARG C 1 93  ? 15.083  -4.564  30.785  1.00 62.80  ? 94  ARG C CG  1 
ATOM   6942  C  CD  . ARG C 1 93  ? 14.396  -5.416  31.834  1.00 71.65  ? 94  ARG C CD  1 
ATOM   6943  N  NE  . ARG C 1 93  ? 14.674  -6.836  31.649  1.00 79.73  ? 94  ARG C NE  1 
ATOM   6944  C  CZ  . ARG C 1 93  ? 14.496  -7.759  32.588  1.00 84.00  ? 94  ARG C CZ  1 
ATOM   6945  N  NH1 . ARG C 1 93  ? 14.038  -7.412  33.783  1.00 85.79  ? 94  ARG C NH1 1 
ATOM   6946  N  NH2 . ARG C 1 93  ? 14.775  -9.030  32.332  1.00 84.98  ? 94  ARG C NH2 1 
ATOM   6947  N  N   . VAL C 1 94  ? 15.965  -5.135  26.265  1.00 40.44  ? 95  VAL C N   1 
ATOM   6948  C  CA  . VAL C 1 94  ? 16.983  -5.144  25.216  1.00 42.51  ? 95  VAL C CA  1 
ATOM   6949  C  C   . VAL C 1 94  ? 17.094  -3.750  24.595  1.00 44.96  ? 95  VAL C C   1 
ATOM   6950  O  O   . VAL C 1 94  ? 18.198  -3.177  24.482  1.00 46.66  ? 95  VAL C O   1 
ATOM   6951  C  CB  . VAL C 1 94  ? 16.672  -6.180  24.118  1.00 45.89  ? 95  VAL C CB  1 
ATOM   6952  C  CG1 . VAL C 1 94  ? 17.538  -5.935  22.890  1.00 38.41  ? 95  VAL C CG1 1 
ATOM   6953  C  CG2 . VAL C 1 94  ? 16.875  -7.592  24.646  1.00 40.86  ? 95  VAL C CG2 1 
ATOM   6954  N  N   . LEU C 1 95  ? 15.941  -3.200  24.212  1.00 47.08  ? 96  LEU C N   1 
ATOM   6955  C  CA  . LEU C 1 95  ? 15.910  -1.855  23.635  1.00 43.18  ? 96  LEU C CA  1 
ATOM   6956  C  C   . LEU C 1 95  ? 16.546  -0.825  24.577  1.00 40.16  ? 96  LEU C C   1 
ATOM   6957  O  O   . LEU C 1 95  ? 17.410  -0.035  24.167  1.00 38.78  ? 96  LEU C O   1 
ATOM   6958  C  CB  . LEU C 1 95  ? 14.472  -1.453  23.300  1.00 44.46  ? 96  LEU C CB  1 
ATOM   6959  C  CG  . LEU C 1 95  ? 14.284  -0.144  22.531  1.00 40.32  ? 96  LEU C CG  1 
ATOM   6960  C  CD1 . LEU C 1 95  ? 15.130  -0.134  21.268  1.00 39.96  ? 96  LEU C CD1 1 
ATOM   6961  C  CD2 . LEU C 1 95  ? 12.819  0.065   22.194  1.00 38.71  ? 96  LEU C CD2 1 
ATOM   6962  N  N   . GLN C 1 96  ? 16.119  -0.853  25.839  1.00 43.57  ? 97  GLN C N   1 
ATOM   6963  C  CA  . GLN C 1 96  ? 16.667  0.018   26.877  1.00 46.28  ? 97  GLN C CA  1 
ATOM   6964  C  C   . GLN C 1 96  ? 18.180  -0.101  26.965  1.00 45.27  ? 97  GLN C C   1 
ATOM   6965  O  O   . GLN C 1 96  ? 18.881  0.902   27.091  1.00 46.81  ? 97  GLN C O   1 
ATOM   6966  C  CB  . GLN C 1 96  ? 16.060  -0.311  28.243  1.00 55.65  ? 97  GLN C CB  1 
ATOM   6967  C  CG  . GLN C 1 96  ? 14.597  0.045   28.404  1.00 63.40  ? 97  GLN C CG  1 
ATOM   6968  C  CD  . GLN C 1 96  ? 14.050  -0.401  29.745  1.00 72.04  ? 97  GLN C CD  1 
ATOM   6969  O  OE1 . GLN C 1 96  ? 14.795  -0.543  30.715  1.00 76.80  ? 97  GLN C OE1 1 
ATOM   6970  N  NE2 . GLN C 1 96  ? 12.746  -0.642  29.803  1.00 75.96  ? 97  GLN C NE2 1 
ATOM   6971  N  N   . ALA C 1 97  ? 18.673  -1.335  26.911  1.00 44.73  ? 98  ALA C N   1 
ATOM   6972  C  CA  . ALA C 1 97  ? 20.108  -1.587  26.957  1.00 46.18  ? 98  ALA C CA  1 
ATOM   6973  C  C   . ALA C 1 97  ? 20.812  -0.890  25.800  1.00 47.37  ? 98  ALA C C   1 
ATOM   6974  O  O   . ALA C 1 97  ? 21.802  -0.174  26.002  1.00 44.87  ? 98  ALA C O   1 
ATOM   6975  C  CB  . ALA C 1 97  ? 20.390  -3.081  26.930  1.00 41.27  ? 98  ALA C CB  1 
ATOM   6976  N  N   . MET C 1 98  ? 20.292  -1.093  24.590  1.00 44.15  ? 99  MET C N   1 
ATOM   6977  C  CA  . MET C 1 98  ? 20.877  -0.453  23.411  1.00 45.75  ? 99  MET C CA  1 
ATOM   6978  C  C   . MET C 1 98  ? 20.927  1.072   23.564  1.00 42.96  ? 99  MET C C   1 
ATOM   6979  O  O   . MET C 1 98  ? 21.982  1.699   23.373  1.00 42.60  ? 99  MET C O   1 
ATOM   6980  C  CB  . MET C 1 98  ? 20.095  -0.836  22.152  1.00 39.21  ? 99  MET C CB  1 
ATOM   6981  C  CG  . MET C 1 98  ? 20.754  -0.412  20.846  1.00 40.53  ? 99  MET C CG  1 
ATOM   6982  S  SD  . MET C 1 98  ? 20.279  1.239   20.293  1.00 61.91  ? 99  MET C SD  1 
ATOM   6983  C  CE  . MET C 1 98  ? 18.549  0.982   19.913  1.00 44.76  ? 99  MET C CE  1 
ATOM   6984  N  N   . LEU C 1 99  ? 19.788  1.660   23.924  1.00 44.33  ? 100 LEU C N   1 
ATOM   6985  C  CA  . LEU C 1 99  ? 19.692  3.110   24.081  1.00 42.88  ? 100 LEU C CA  1 
ATOM   6986  C  C   . LEU C 1 99  ? 20.655  3.647   25.141  1.00 43.75  ? 100 LEU C C   1 
ATOM   6987  O  O   . LEU C 1 99  ? 21.277  4.697   24.953  1.00 40.24  ? 100 LEU C O   1 
ATOM   6988  C  CB  . LEU C 1 99  ? 18.257  3.510   24.427  1.00 44.17  ? 100 LEU C CB  1 
ATOM   6989  C  CG  . LEU C 1 99  ? 17.229  3.283   23.317  1.00 45.28  ? 100 LEU C CG  1 
ATOM   6990  C  CD1 . LEU C 1 99  ? 15.819  3.554   23.819  1.00 41.91  ? 100 LEU C CD1 1 
ATOM   6991  C  CD2 . LEU C 1 99  ? 17.549  4.155   22.113  1.00 41.32  ? 100 LEU C CD2 1 
ATOM   6992  N  N   . ALA C 1 100 ? 20.776  2.923   26.249  1.00 43.14  ? 101 ALA C N   1 
ATOM   6993  C  CA  . ALA C 1 100 ? 21.692  3.302   27.320  1.00 44.20  ? 101 ALA C CA  1 
ATOM   6994  C  C   . ALA C 1 100 ? 23.132  3.290   26.822  1.00 49.08  ? 101 ALA C C   1 
ATOM   6995  O  O   . ALA C 1 100 ? 23.893  4.241   27.053  1.00 49.63  ? 101 ALA C O   1 
ATOM   6996  C  CB  . ALA C 1 100 ? 21.533  2.370   28.511  1.00 42.21  ? 101 ALA C CB  1 
ATOM   6997  N  N   . THR C 1 101 ? 23.494  2.209   26.134  1.00 43.67  ? 102 THR C N   1 
ATOM   6998  C  CA  . THR C 1 101 ? 24.828  2.074   25.560  1.00 40.72  ? 102 THR C CA  1 
ATOM   6999  C  C   . THR C 1 101 ? 25.160  3.243   24.637  1.00 42.12  ? 102 THR C C   1 
ATOM   7000  O  O   . THR C 1 101 ? 26.201  3.892   24.795  1.00 41.25  ? 102 THR C O   1 
ATOM   7001  C  CB  . THR C 1 101 ? 24.975  0.756   24.779  1.00 45.94  ? 102 THR C CB  1 
ATOM   7002  O  OG1 . THR C 1 101 ? 24.942  -0.347  25.693  1.00 47.80  ? 102 THR C OG1 1 
ATOM   7003  C  CG2 . THR C 1 101 ? 26.291  0.730   24.017  1.00 47.98  ? 102 THR C CG2 1 
ATOM   7004  N  N   . GLN C 1 102 ? 24.270  3.516   23.684  1.00 43.26  ? 103 GLN C N   1 
ATOM   7005  C  CA  . GLN C 1 102 ? 24.478  4.633   22.763  1.00 42.53  ? 103 GLN C CA  1 
ATOM   7006  C  C   . GLN C 1 102 ? 24.633  5.955   23.515  1.00 44.72  ? 103 GLN C C   1 
ATOM   7007  O  O   . GLN C 1 102 ? 25.555  6.734   23.245  1.00 44.22  ? 103 GLN C O   1 
ATOM   7008  C  CB  . GLN C 1 102 ? 23.322  4.733   21.764  1.00 45.49  ? 103 GLN C CB  1 
ATOM   7009  C  CG  . GLN C 1 102 ? 23.209  3.547   20.821  1.00 49.76  ? 103 GLN C CG  1 
ATOM   7010  C  CD  . GLN C 1 102 ? 24.464  3.336   19.995  1.00 56.48  ? 103 GLN C CD  1 
ATOM   7011  O  OE1 . GLN C 1 102 ? 25.082  4.292   19.527  1.00 57.76  ? 103 GLN C OE1 1 
ATOM   7012  N  NE2 . GLN C 1 102 ? 24.846  2.078   19.813  1.00 69.75  ? 103 GLN C NE2 1 
ATOM   7013  N  N   . LEU C 1 103 ? 23.728  6.188   24.463  1.00 40.99  ? 104 LEU C N   1 
ATOM   7014  C  CA  . LEU C 1 103 ? 23.734  7.400   25.279  1.00 44.28  ? 104 LEU C CA  1 
ATOM   7015  C  C   . LEU C 1 103 ? 25.085  7.637   25.953  1.00 44.69  ? 104 LEU C C   1 
ATOM   7016  O  O   . LEU C 1 103 ? 25.728  8.681   25.751  1.00 41.29  ? 104 LEU C O   1 
ATOM   7017  C  CB  . LEU C 1 103 ? 22.631  7.317   26.337  1.00 44.15  ? 104 LEU C CB  1 
ATOM   7018  C  CG  . LEU C 1 103 ? 22.521  8.467   27.338  1.00 48.09  ? 104 LEU C CG  1 
ATOM   7019  C  CD1 . LEU C 1 103 ? 22.034  9.722   26.644  1.00 47.70  ? 104 LEU C CD1 1 
ATOM   7020  C  CD2 . LEU C 1 103 ? 21.593  8.091   28.482  1.00 49.42  ? 104 LEU C CD2 1 
ATOM   7021  N  N   . ARG C 1 104 ? 25.512  6.656   26.744  1.00 41.21  ? 105 ARG C N   1 
ATOM   7022  C  CA  . ARG C 1 104 ? 26.772  6.757   27.472  1.00 51.71  ? 105 ARG C CA  1 
ATOM   7023  C  C   . ARG C 1 104 ? 27.960  6.905   26.523  1.00 42.48  ? 105 ARG C C   1 
ATOM   7024  O  O   . ARG C 1 104 ? 28.857  7.714   26.767  1.00 43.08  ? 105 ARG C O   1 
ATOM   7025  C  CB  . ARG C 1 104 ? 26.968  5.538   28.375  1.00 42.36  ? 105 ARG C CB  1 
ATOM   7026  N  N   . SER C 1 105 ? 27.955  6.130   25.440  1.00 45.32  ? 106 SER C N   1 
ATOM   7027  C  CA  . SER C 1 105 ? 29.037  6.182   24.459  1.00 44.48  ? 106 SER C CA  1 
ATOM   7028  C  C   . SER C 1 105 ? 29.198  7.582   23.880  1.00 46.66  ? 106 SER C C   1 
ATOM   7029  O  O   . SER C 1 105 ? 30.303  8.133   23.855  1.00 51.39  ? 106 SER C O   1 
ATOM   7030  C  CB  . SER C 1 105 ? 28.791  5.178   23.329  1.00 42.62  ? 106 SER C CB  1 
ATOM   7031  O  OG  . SER C 1 105 ? 29.068  3.854   23.750  1.00 49.51  ? 106 SER C OG  1 
ATOM   7032  N  N   . PHE C 1 106 ? 28.089  8.161   23.428  1.00 42.20  ? 107 PHE C N   1 
ATOM   7033  C  CA  . PHE C 1 106 ? 28.130  9.484   22.815  1.00 42.29  ? 107 PHE C CA  1 
ATOM   7034  C  C   . PHE C 1 106 ? 28.477  10.585  23.813  1.00 46.42  ? 107 PHE C C   1 
ATOM   7035  O  O   . PHE C 1 106 ? 29.303  11.453  23.514  1.00 49.69  ? 107 PHE C O   1 
ATOM   7036  C  CB  . PHE C 1 106 ? 26.799  9.796   22.130  1.00 41.64  ? 107 PHE C CB  1 
ATOM   7037  C  CG  . PHE C 1 106 ? 26.729  9.313   20.711  1.00 41.61  ? 107 PHE C CG  1 
ATOM   7038  C  CD1 . PHE C 1 106 ? 26.218  8.061   20.413  1.00 41.28  ? 107 PHE C CD1 1 
ATOM   7039  C  CD2 . PHE C 1 106 ? 27.190  10.108  19.674  1.00 42.03  ? 107 PHE C CD2 1 
ATOM   7040  C  CE1 . PHE C 1 106 ? 26.160  7.615   19.107  1.00 41.39  ? 107 PHE C CE1 1 
ATOM   7041  C  CE2 . PHE C 1 106 ? 27.135  9.667   18.367  1.00 42.17  ? 107 PHE C CE2 1 
ATOM   7042  C  CZ  . PHE C 1 106 ? 26.619  8.419   18.083  1.00 41.86  ? 107 PHE C CZ  1 
ATOM   7043  N  N   . ASP C 1 107 ? 27.857  10.553  24.991  1.00 45.50  ? 108 ASP C N   1 
ATOM   7044  C  CA  . ASP C 1 107 ? 28.148  11.564  26.009  1.00 48.46  ? 108 ASP C CA  1 
ATOM   7045  C  C   . ASP C 1 107 ? 29.637  11.539  26.369  1.00 52.68  ? 108 ASP C C   1 
ATOM   7046  O  O   . ASP C 1 107 ? 30.334  12.574  26.326  1.00 52.09  ? 108 ASP C O   1 
ATOM   7047  C  CB  . ASP C 1 107 ? 27.290  11.336  27.255  1.00 48.65  ? 108 ASP C CB  1 
ATOM   7048  C  CG  . ASP C 1 107 ? 27.165  12.581  28.113  1.00 47.21  ? 108 ASP C CG  1 
ATOM   7049  O  OD1 . ASP C 1 107 ? 27.108  13.691  27.544  1.00 45.64  ? 108 ASP C OD1 1 
ATOM   7050  O  OD2 . ASP C 1 107 ? 27.120  12.450  29.354  1.00 50.62  ? 108 ASP C OD2 1 
ATOM   7051  N  N   . ASP C 1 108 ? 30.117  10.341  26.697  1.00 52.22  ? 109 ASP C N   1 
ATOM   7052  C  CA  . ASP C 1 108 ? 31.520  10.134  27.034  1.00 57.24  ? 109 ASP C CA  1 
ATOM   7053  C  C   . ASP C 1 108 ? 32.447  10.595  25.916  1.00 54.54  ? 109 ASP C C   1 
ATOM   7054  O  O   . ASP C 1 108 ? 33.461  11.236  26.180  1.00 52.69  ? 109 ASP C O   1 
ATOM   7055  C  CB  . ASP C 1 108 ? 31.789  8.661   27.351  1.00 58.64  ? 109 ASP C CB  1 
ATOM   7056  C  CG  . ASP C 1 108 ? 31.235  8.243   28.700  1.00 61.34  ? 109 ASP C CG  1 
ATOM   7057  O  OD1 . ASP C 1 108 ? 30.412  8.993   29.266  1.00 68.00  ? 109 ASP C OD1 1 
ATOM   7058  O  OD2 . ASP C 1 108 ? 31.619  7.161   29.193  1.00 61.23  ? 109 ASP C OD2 1 
ATOM   7059  N  N   . HIS C 1 109 ? 32.102  10.277  24.670  1.00 50.99  ? 110 HIS C N   1 
ATOM   7060  C  CA  . HIS C 1 109 ? 32.978  10.635  23.559  1.00 54.10  ? 110 HIS C CA  1 
ATOM   7061  C  C   . HIS C 1 109 ? 33.011  12.138  23.296  1.00 50.24  ? 110 HIS C C   1 
ATOM   7062  O  O   . HIS C 1 109 ? 34.050  12.675  22.923  1.00 51.47  ? 110 HIS C O   1 
ATOM   7063  C  CB  . HIS C 1 109 ? 32.577  9.914   22.274  1.00 45.07  ? 110 HIS C CB  1 
ATOM   7064  C  CG  . HIS C 1 109 ? 33.407  10.311  21.092  1.00 47.68  ? 110 HIS C CG  1 
ATOM   7065  N  ND1 . HIS C 1 109 ? 34.778  10.178  21.071  1.00 46.74  ? 110 HIS C ND1 1 
ATOM   7066  C  CD2 . HIS C 1 109 ? 33.064  10.861  19.903  1.00 50.03  ? 110 HIS C CD2 1 
ATOM   7067  C  CE1 . HIS C 1 109 ? 35.244  10.619  19.916  1.00 47.21  ? 110 HIS C CE1 1 
ATOM   7068  N  NE2 . HIS C 1 109 ? 34.224  11.037  19.188  1.00 50.72  ? 110 HIS C NE2 1 
ATOM   7069  N  N   . PHE C 1 110 ? 31.881  12.814  23.472  1.00 44.90  ? 111 PHE C N   1 
ATOM   7070  C  CA  . PHE C 1 110 ? 31.850  14.263  23.285  1.00 55.04  ? 111 PHE C CA  1 
ATOM   7071  C  C   . PHE C 1 110 ? 32.657  14.963  24.379  1.00 52.19  ? 111 PHE C C   1 
ATOM   7072  O  O   . PHE C 1 110 ? 33.532  15.810  24.093  1.00 55.04  ? 111 PHE C O   1 
ATOM   7073  C  CB  . PHE C 1 110 ? 30.407  14.772  23.264  1.00 44.38  ? 111 PHE C CB  1 
ATOM   7074  C  CG  . PHE C 1 110 ? 29.685  14.493  21.974  1.00 43.90  ? 111 PHE C CG  1 
ATOM   7075  C  CD1 . PHE C 1 110 ? 30.301  14.735  20.757  1.00 44.32  ? 111 PHE C CD1 1 
ATOM   7076  C  CD2 . PHE C 1 110 ? 28.397  13.980  21.977  1.00 48.98  ? 111 PHE C CD2 1 
ATOM   7077  C  CE1 . PHE C 1 110 ? 29.645  14.478  19.566  1.00 44.03  ? 111 PHE C CE1 1 
ATOM   7078  C  CE2 . PHE C 1 110 ? 27.736  13.717  20.789  1.00 42.82  ? 111 PHE C CE2 1 
ATOM   7079  C  CZ  . PHE C 1 110 ? 28.361  13.967  19.582  1.00 43.28  ? 111 PHE C CZ  1 
ATOM   7080  N  N   . GLN C 1 111 ? 32.374  14.595  25.629  1.00 50.60  ? 112 GLN C N   1 
ATOM   7081  C  CA  . GLN C 1 111 ? 33.116  15.151  26.757  1.00 52.53  ? 112 GLN C CA  1 
ATOM   7082  C  C   . GLN C 1 111 ? 34.619  14.906  26.598  1.00 54.56  ? 112 GLN C C   1 
ATOM   7083  O  O   . GLN C 1 111 ? 35.440  15.791  26.865  1.00 51.52  ? 112 GLN C O   1 
ATOM   7084  C  CB  . GLN C 1 111 ? 32.617  14.558  28.076  1.00 53.74  ? 112 GLN C CB  1 
ATOM   7085  C  CG  . GLN C 1 111 ? 31.280  15.120  28.538  1.00 56.50  ? 112 GLN C CG  1 
ATOM   7086  C  CD  . GLN C 1 111 ? 30.753  14.431  29.781  1.00 61.74  ? 112 GLN C CD  1 
ATOM   7087  O  OE1 . GLN C 1 111 ? 31.372  13.502  30.300  1.00 65.10  ? 112 GLN C OE1 1 
ATOM   7088  N  NE2 . GLN C 1 111 ? 29.604  14.886  30.268  1.00 64.13  ? 112 GLN C NE2 1 
ATOM   7089  N  N   . HIS C 1 112 ? 34.970  13.709  26.139  1.00 58.58  ? 113 HIS C N   1 
ATOM   7090  C  CA  . HIS C 1 112 ? 36.365  13.363  25.902  1.00 60.97  ? 113 HIS C CA  1 
ATOM   7091  C  C   . HIS C 1 112 ? 36.952  14.153  24.741  1.00 55.45  ? 113 HIS C C   1 
ATOM   7092  O  O   . HIS C 1 112 ? 38.143  14.429  24.721  1.00 50.90  ? 113 HIS C O   1 
ATOM   7093  C  CB  . HIS C 1 112 ? 36.524  11.867  25.627  1.00 69.92  ? 113 HIS C CB  1 
ATOM   7094  C  CG  . HIS C 1 112 ? 37.843  11.509  25.015  1.00 80.59  ? 113 HIS C CG  1 
ATOM   7095  N  ND1 . HIS C 1 112 ? 37.982  11.188  23.682  1.00 85.46  ? 113 HIS C ND1 1 
ATOM   7096  C  CD2 . HIS C 1 112 ? 39.085  11.445  25.549  1.00 86.54  ? 113 HIS C CD2 1 
ATOM   7097  C  CE1 . HIS C 1 112 ? 39.252  10.930  23.424  1.00 88.44  ? 113 HIS C CE1 1 
ATOM   7098  N  NE2 . HIS C 1 112 ? 39.942  11.078  24.540  1.00 89.29  ? 113 HIS C NE2 1 
ATOM   7099  N  N   . LEU C 1 113 ? 36.121  14.500  23.765  1.00 53.68  ? 114 LEU C N   1 
ATOM   7100  C  CA  . LEU C 1 113 ? 36.589  15.297  22.639  1.00 48.49  ? 114 LEU C CA  1 
ATOM   7101  C  C   . LEU C 1 113 ? 36.980  16.680  23.127  1.00 61.38  ? 114 LEU C C   1 
ATOM   7102  O  O   . LEU C 1 113 ? 38.090  17.157  22.855  1.00 49.96  ? 114 LEU C O   1 
ATOM   7103  C  CB  . LEU C 1 113 ? 35.524  15.397  21.546  1.00 47.70  ? 114 LEU C CB  1 
ATOM   7104  C  CG  . LEU C 1 113 ? 35.516  14.284  20.497  1.00 55.21  ? 114 LEU C CG  1 
ATOM   7105  C  CD1 . LEU C 1 113 ? 34.404  14.510  19.485  1.00 55.76  ? 114 LEU C CD1 1 
ATOM   7106  C  CD2 . LEU C 1 113 ? 36.868  14.192  19.805  1.00 48.68  ? 114 LEU C CD2 1 
ATOM   7107  N  N   . LEU C 1 114 ? 36.075  17.316  23.866  1.00 58.40  ? 115 LEU C N   1 
ATOM   7108  C  CA  . LEU C 1 114 ? 36.372  18.644  24.401  1.00 54.37  ? 115 LEU C CA  1 
ATOM   7109  C  C   . LEU C 1 114 ? 37.597  18.607  25.326  1.00 54.39  ? 115 LEU C C   1 
ATOM   7110  O  O   . LEU C 1 114 ? 38.509  19.441  25.213  1.00 51.04  ? 115 LEU C O   1 
ATOM   7111  C  CB  . LEU C 1 114 ? 35.160  19.208  25.143  1.00 48.58  ? 115 LEU C CB  1 
ATOM   7112  C  CG  . LEU C 1 114 ? 35.120  20.733  25.258  1.00 55.99  ? 115 LEU C CG  1 
ATOM   7113  C  CD1 . LEU C 1 114 ? 35.213  21.369  23.880  1.00 57.30  ? 115 LEU C CD1 1 
ATOM   7114  C  CD2 . LEU C 1 114 ? 33.856  21.185  25.967  1.00 48.61  ? 115 LEU C CD2 1 
ATOM   7115  N  N   . ASN C 1 115 ? 37.620  17.624  26.223  1.00 50.14  ? 116 ASN C N   1 
ATOM   7116  C  CA  . ASN C 1 115 ? 38.722  17.470  27.170  1.00 64.16  ? 116 ASN C CA  1 
ATOM   7117  C  C   . ASN C 1 115 ? 40.083  17.253  26.499  1.00 60.06  ? 116 ASN C C   1 
ATOM   7118  O  O   . ASN C 1 115 ? 41.073  17.889  26.867  1.00 59.27  ? 116 ASN C O   1 
ATOM   7119  C  CB  . ASN C 1 115 ? 38.421  16.317  28.129  1.00 64.60  ? 116 ASN C CB  1 
ATOM   7120  C  CG  . ASN C 1 115 ? 37.547  16.745  29.293  1.00 70.60  ? 116 ASN C CG  1 
ATOM   7121  O  OD1 . ASN C 1 115 ? 37.197  17.919  29.417  1.00 70.29  ? 116 ASN C OD1 1 
ATOM   7122  N  ND2 . ASN C 1 115 ? 37.189  15.796  30.153  1.00 73.63  ? 116 ASN C ND2 1 
ATOM   7123  N  N   . ASP C 1 116 ? 40.121  16.358  25.516  1.00 58.58  ? 117 ASP C N   1 
ATOM   7124  C  CA  . ASP C 1 116 ? 41.331  16.078  24.748  1.00 58.28  ? 117 ASP C CA  1 
ATOM   7125  C  C   . ASP C 1 116 ? 41.759  17.337  24.008  1.00 59.25  ? 117 ASP C C   1 
ATOM   7126  O  O   . ASP C 1 116 ? 42.949  17.621  23.899  1.00 57.74  ? 117 ASP C O   1 
ATOM   7127  C  CB  . ASP C 1 116 ? 41.095  14.921  23.765  1.00 68.02  ? 117 ASP C CB  1 
ATOM   7128  C  CG  . ASP C 1 116 ? 42.383  14.397  23.129  1.00 76.61  ? 117 ASP C CG  1 
ATOM   7129  O  OD1 . ASP C 1 116 ? 43.345  15.170  22.939  1.00 84.47  ? 117 ASP C OD1 1 
ATOM   7130  O  OD2 . ASP C 1 116 ? 42.430  13.189  22.815  1.00 79.20  ? 117 ASP C OD2 1 
ATOM   7131  N  N   . SER C 1 117 ? 40.787  18.090  23.499  1.00 56.73  ? 118 SER C N   1 
ATOM   7132  C  CA  . SER C 1 117 ? 41.094  19.365  22.861  1.00 56.43  ? 118 SER C CA  1 
ATOM   7133  C  C   . SER C 1 117 ? 41.825  20.280  23.845  1.00 58.86  ? 118 SER C C   1 
ATOM   7134  O  O   . SER C 1 117 ? 42.872  20.856  23.522  1.00 54.82  ? 118 SER C O   1 
ATOM   7135  C  CB  . SER C 1 117 ? 39.818  20.037  22.349  1.00 58.24  ? 118 SER C CB  1 
ATOM   7136  O  OG  . SER C 1 117 ? 40.113  21.251  21.679  1.00 60.20  ? 118 SER C OG  1 
ATOM   7137  N  N   . GLU C 1 118 ? 41.281  20.384  25.055  1.00 60.82  ? 119 GLU C N   1 
ATOM   7138  C  CA  . GLU C 1 118 ? 41.870  21.245  26.080  1.00 58.10  ? 119 GLU C CA  1 
ATOM   7139  C  C   . GLU C 1 118 ? 43.281  20.812  26.484  1.00 58.46  ? 119 GLU C C   1 
ATOM   7140  O  O   . GLU C 1 118 ? 44.179  21.647  26.604  1.00 62.10  ? 119 GLU C O   1 
ATOM   7141  C  CB  . GLU C 1 118 ? 40.970  21.290  27.314  1.00 61.56  ? 119 GLU C CB  1 
ATOM   7142  C  CG  . GLU C 1 118 ? 41.323  22.398  28.290  1.00 66.00  ? 119 GLU C CG  1 
ATOM   7143  C  CD  . GLU C 1 118 ? 40.247  22.611  29.334  1.00 71.31  ? 119 GLU C CD  1 
ATOM   7144  O  OE1 . GLU C 1 118 ? 39.269  21.836  29.342  1.00 70.53  ? 119 GLU C OE1 1 
ATOM   7145  O  OE2 . GLU C 1 118 ? 40.373  23.557  30.139  1.00 74.49  ? 119 GLU C OE2 1 
ATOM   7146  N  N   . ARG C 1 119 ? 43.473  19.514  26.695  1.00 61.35  ? 120 ARG C N   1 
ATOM   7147  C  CA  . ARG C 1 119 ? 44.787  18.991  27.069  1.00 66.27  ? 120 ARG C CA  1 
ATOM   7148  C  C   . ARG C 1 119 ? 45.807  19.182  25.948  1.00 67.75  ? 120 ARG C C   1 
ATOM   7149  O  O   . ARG C 1 119 ? 46.974  19.487  26.204  1.00 68.09  ? 120 ARG C O   1 
ATOM   7150  C  CB  . ARG C 1 119 ? 44.693  17.511  27.447  1.00 65.38  ? 120 ARG C CB  1 
ATOM   7151  C  CG  . ARG C 1 119 ? 44.091  17.260  28.821  1.00 69.41  ? 120 ARG C CG  1 
ATOM   7152  C  CD  . ARG C 1 119 ? 44.116  15.783  29.180  1.00 77.05  ? 120 ARG C CD  1 
ATOM   7153  N  NE  . ARG C 1 119 ? 43.162  15.008  28.392  1.00 76.71  ? 120 ARG C NE  1 
ATOM   7154  C  CZ  . ARG C 1 119 ? 41.957  14.649  28.823  1.00 79.95  ? 120 ARG C CZ  1 
ATOM   7155  N  NH1 . ARG C 1 119 ? 41.556  14.996  30.039  1.00 80.04  ? 120 ARG C NH1 1 
ATOM   7156  N  NH2 . ARG C 1 119 ? 41.152  13.943  28.040  1.00 78.86  ? 120 ARG C NH2 1 
ATOM   7157  N  N   . THR C 1 120 ? 45.358  18.997  24.710  1.00 70.48  ? 121 THR C N   1 
ATOM   7158  C  CA  . THR C 1 120 ? 46.195  19.223  23.538  1.00 71.18  ? 121 THR C CA  1 
ATOM   7159  C  C   . THR C 1 120 ? 46.647  20.676  23.498  1.00 73.39  ? 121 THR C C   1 
ATOM   7160  O  O   . THR C 1 120 ? 47.827  20.970  23.273  1.00 75.29  ? 121 THR C O   1 
ATOM   7161  C  CB  . THR C 1 120 ? 45.449  18.880  22.233  1.00 73.10  ? 121 THR C CB  1 
ATOM   7162  O  OG1 . THR C 1 120 ? 45.127  17.484  22.216  1.00 74.61  ? 121 THR C OG1 1 
ATOM   7163  C  CG2 . THR C 1 120 ? 46.306  19.210  21.022  1.00 75.70  ? 121 THR C CG2 1 
ATOM   7164  N  N   . LEU C 1 121 ? 45.699  21.582  23.728  1.00 69.84  ? 122 LEU C N   1 
ATOM   7165  C  CA  . LEU C 1 121 ? 46.010  23.005  23.786  1.00 65.72  ? 122 LEU C CA  1 
ATOM   7166  C  C   . LEU C 1 121 ? 47.045  23.296  24.870  1.00 61.31  ? 122 LEU C C   1 
ATOM   7167  O  O   . LEU C 1 121 ? 48.066  23.927  24.605  1.00 61.83  ? 122 LEU C O   1 
ATOM   7168  C  CB  . LEU C 1 121 ? 44.738  23.822  24.030  1.00 66.46  ? 122 LEU C CB  1 
ATOM   7169  C  CG  . LEU C 1 121 ? 44.899  25.333  24.215  1.00 65.12  ? 122 LEU C CG  1 
ATOM   7170  C  CD1 . LEU C 1 121 ? 43.819  26.073  23.450  1.00 64.20  ? 122 LEU C CD1 1 
ATOM   7171  C  CD2 . LEU C 1 121 ? 44.842  25.702  25.687  1.00 63.76  ? 122 LEU C CD2 1 
ATOM   7172  N  N   . GLN C 1 122 ? 46.782  22.822  26.084  1.00 59.48  ? 123 GLN C N   1 
ATOM   7173  C  CA  . GLN C 1 122 ? 47.669  23.070  27.218  1.00 63.79  ? 123 GLN C CA  1 
ATOM   7174  C  C   . GLN C 1 122 ? 49.063  22.480  27.022  1.00 66.72  ? 123 GLN C C   1 
ATOM   7175  O  O   . GLN C 1 122 ? 50.042  22.986  27.573  1.00 63.48  ? 123 GLN C O   1 
ATOM   7176  C  CB  . GLN C 1 122 ? 47.058  22.510  28.504  1.00 64.55  ? 123 GLN C CB  1 
ATOM   7177  C  CG  . GLN C 1 122 ? 45.831  23.260  28.989  1.00 67.77  ? 123 GLN C CG  1 
ATOM   7178  C  CD  . GLN C 1 122 ? 45.223  22.633  30.227  1.00 69.86  ? 123 GLN C CD  1 
ATOM   7179  O  OE1 . GLN C 1 122 ? 45.636  21.557  30.659  1.00 68.51  ? 123 GLN C OE1 1 
ATOM   7180  N  NE2 . GLN C 1 122 ? 44.238  23.308  30.809  1.00 71.19  ? 123 GLN C NE2 1 
ATOM   7181  N  N   . ALA C 1 123 ? 49.152  21.410  26.239  1.00 66.29  ? 124 ALA C N   1 
ATOM   7182  C  CA  . ALA C 1 123 ? 50.428  20.739  26.022  1.00 63.22  ? 124 ALA C CA  1 
ATOM   7183  C  C   . ALA C 1 123 ? 51.234  21.379  24.895  1.00 77.71  ? 124 ALA C C   1 
ATOM   7184  O  O   . ALA C 1 123 ? 52.460  21.455  24.970  1.00 65.59  ? 124 ALA C O   1 
ATOM   7185  C  CB  . ALA C 1 123 ? 50.203  19.264  25.732  1.00 62.78  ? 124 ALA C CB  1 
ATOM   7186  N  N   . THR C 1 124 ? 50.548  21.841  23.854  1.00 72.10  ? 125 THR C N   1 
ATOM   7187  C  CA  . THR C 1 124 ? 51.237  22.335  22.664  1.00 69.20  ? 125 THR C CA  1 
ATOM   7188  C  C   . THR C 1 124 ? 51.466  23.848  22.656  1.00 68.47  ? 125 THR C C   1 
ATOM   7189  O  O   . THR C 1 124 ? 52.477  24.322  22.136  1.00 69.18  ? 125 THR C O   1 
ATOM   7190  C  CB  . THR C 1 124 ? 50.467  21.955  21.384  1.00 66.68  ? 125 THR C CB  1 
ATOM   7191  O  OG1 . THR C 1 124 ? 49.095  22.344  21.516  1.00 62.25  ? 125 THR C OG1 1 
ATOM   7192  C  CG2 . THR C 1 124 ? 50.539  20.454  21.150  1.00 66.81  ? 125 THR C CG2 1 
ATOM   7193  N  N   . PHE C 1 125 ? 50.532  24.600  23.230  1.00 67.07  ? 126 PHE C N   1 
ATOM   7194  C  CA  . PHE C 1 125 ? 50.577  26.065  23.172  1.00 68.86  ? 126 PHE C CA  1 
ATOM   7195  C  C   . PHE C 1 125 ? 51.786  26.742  23.842  1.00 65.51  ? 126 PHE C C   1 
ATOM   7196  O  O   . PHE C 1 125 ? 52.269  27.751  23.330  1.00 66.28  ? 126 PHE C O   1 
ATOM   7197  C  CB  . PHE C 1 125 ? 49.289  26.647  23.762  1.00 62.69  ? 126 PHE C CB  1 
ATOM   7198  C  CG  . PHE C 1 125 ? 48.170  26.768  22.768  1.00 68.35  ? 126 PHE C CG  1 
ATOM   7199  C  CD1 . PHE C 1 125 ? 47.881  25.731  21.896  1.00 63.60  ? 126 PHE C CD1 1 
ATOM   7200  C  CD2 . PHE C 1 125 ? 47.408  27.923  22.703  1.00 64.67  ? 126 PHE C CD2 1 
ATOM   7201  C  CE1 . PHE C 1 125 ? 46.853  25.842  20.979  1.00 63.03  ? 126 PHE C CE1 1 
ATOM   7202  C  CE2 . PHE C 1 125 ? 46.378  28.040  21.789  1.00 63.77  ? 126 PHE C CE2 1 
ATOM   7203  C  CZ  . PHE C 1 125 ? 46.101  26.999  20.925  1.00 63.48  ? 126 PHE C CZ  1 
ATOM   7204  N  N   . PRO C 1 126 ? 52.266  26.221  24.991  1.00 71.15  ? 127 PRO C N   1 
ATOM   7205  C  CA  . PRO C 1 126 ? 53.470  26.859  25.542  1.00 75.03  ? 127 PRO C CA  1 
ATOM   7206  C  C   . PRO C 1 126 ? 54.669  26.804  24.595  1.00 81.83  ? 127 PRO C C   1 
ATOM   7207  O  O   . PRO C 1 126 ? 55.443  27.758  24.531  1.00 85.54  ? 127 PRO C O   1 
ATOM   7208  C  CB  . PRO C 1 126 ? 53.747  26.044  26.809  1.00 71.57  ? 127 PRO C CB  1 
ATOM   7209  C  CG  . PRO C 1 126 ? 52.416  25.543  27.220  1.00 66.68  ? 127 PRO C CG  1 
ATOM   7210  C  CD  . PRO C 1 126 ? 51.686  25.252  25.940  1.00 71.70  ? 127 PRO C CD  1 
ATOM   7211  N  N   . GLY C 1 127 ? 54.809  25.705  23.863  1.00 83.96  ? 128 GLY C N   1 
ATOM   7212  C  CA  . GLY C 1 127 ? 55.923  25.544  22.948  1.00 87.53  ? 128 GLY C CA  1 
ATOM   7213  C  C   . GLY C 1 127 ? 55.771  26.336  21.663  1.00 87.96  ? 128 GLY C C   1 
ATOM   7214  O  O   . GLY C 1 127 ? 56.758  26.796  21.088  1.00 91.98  ? 128 GLY C O   1 
ATOM   7215  N  N   . ALA C 1 128 ? 54.531  26.504  21.215  1.00 85.42  ? 129 ALA C N   1 
ATOM   7216  C  CA  . ALA C 1 128 ? 54.263  27.148  19.935  1.00 83.50  ? 129 ALA C CA  1 
ATOM   7217  C  C   . ALA C 1 128 ? 54.121  28.664  20.054  1.00 80.40  ? 129 ALA C C   1 
ATOM   7218  O  O   . ALA C 1 128 ? 54.399  29.393  19.103  1.00 81.65  ? 129 ALA C O   1 
ATOM   7219  C  CB  . ALA C 1 128 ? 53.010  26.555  19.305  1.00 82.95  ? 129 ALA C CB  1 
ATOM   7220  N  N   . PHE C 1 129 ? 53.692  29.136  21.221  1.00 78.50  ? 130 PHE C N   1 
ATOM   7221  C  CA  . PHE C 1 129 ? 53.399  30.555  21.399  1.00 75.68  ? 130 PHE C CA  1 
ATOM   7222  C  C   . PHE C 1 129 ? 54.137  31.177  22.581  1.00 79.73  ? 130 PHE C C   1 
ATOM   7223  O  O   . PHE C 1 129 ? 54.293  32.397  22.647  1.00 80.92  ? 130 PHE C O   1 
ATOM   7224  C  CB  . PHE C 1 129 ? 51.895  30.764  21.574  1.00 71.83  ? 130 PHE C CB  1 
ATOM   7225  C  CG  . PHE C 1 129 ? 51.068  30.134  20.494  1.00 70.45  ? 130 PHE C CG  1 
ATOM   7226  C  CD1 . PHE C 1 129 ? 50.903  30.767  19.276  1.00 69.32  ? 130 PHE C CD1 1 
ATOM   7227  C  CD2 . PHE C 1 129 ? 50.454  28.909  20.697  1.00 69.25  ? 130 PHE C CD2 1 
ATOM   7228  C  CE1 . PHE C 1 129 ? 50.142  30.192  18.282  1.00 68.77  ? 130 PHE C CE1 1 
ATOM   7229  C  CE2 . PHE C 1 129 ? 49.692  28.328  19.703  1.00 66.47  ? 130 PHE C CE2 1 
ATOM   7230  C  CZ  . PHE C 1 129 ? 49.536  28.972  18.493  1.00 67.69  ? 130 PHE C CZ  1 
ATOM   7231  N  N   . GLY C 1 130 ? 54.582  30.344  23.515  1.00 82.92  ? 131 GLY C N   1 
ATOM   7232  C  CA  . GLY C 1 130 ? 55.264  30.843  24.694  1.00 85.26  ? 131 GLY C CA  1 
ATOM   7233  C  C   . GLY C 1 130 ? 54.322  31.518  25.673  1.00 86.24  ? 131 GLY C C   1 
ATOM   7234  O  O   . GLY C 1 130 ? 53.323  30.933  26.103  1.00 86.92  ? 131 GLY C O   1 
ATOM   7235  N  N   . GLU C 1 131 ? 54.634  32.761  26.024  1.00 89.44  ? 132 GLU C N   1 
ATOM   7236  C  CA  . GLU C 1 131 ? 53.842  33.475  27.017  1.00 89.64  ? 132 GLU C CA  1 
ATOM   7237  C  C   . GLU C 1 131 ? 52.735  34.312  26.386  1.00 87.34  ? 132 GLU C C   1 
ATOM   7238  O  O   . GLU C 1 131 ? 52.089  35.111  27.063  1.00 92.34  ? 132 GLU C O   1 
ATOM   7239  C  CB  . GLU C 1 131 ? 54.740  34.352  27.889  1.00 97.73  ? 132 GLU C CB  1 
ATOM   7240  C  CG  . GLU C 1 131 ? 55.479  35.445  27.151  1.00 101.80 ? 132 GLU C CG  1 
ATOM   7241  C  CD  . GLU C 1 131 ? 56.431  36.196  28.059  1.00 107.78 ? 132 GLU C CD  1 
ATOM   7242  O  OE1 . GLU C 1 131 ? 56.273  36.094  29.294  1.00 109.20 ? 132 GLU C OE1 1 
ATOM   7243  O  OE2 . GLU C 1 131 ? 57.335  36.885  27.542  1.00 110.30 ? 132 GLU C OE2 1 
ATOM   7244  N  N   . LEU C 1 132 ? 52.512  34.122  25.089  1.00 83.37  ? 133 LEU C N   1 
ATOM   7245  C  CA  . LEU C 1 132 ? 51.304  34.637  24.460  1.00 80.62  ? 133 LEU C CA  1 
ATOM   7246  C  C   . LEU C 1 132 ? 50.155  33.719  24.853  1.00 77.91  ? 133 LEU C C   1 
ATOM   7247  O  O   . LEU C 1 132 ? 48.982  34.063  24.708  1.00 79.42  ? 133 LEU C O   1 
ATOM   7248  C  CB  . LEU C 1 132 ? 51.453  34.722  22.940  1.00 78.92  ? 133 LEU C CB  1 
ATOM   7249  C  CG  . LEU C 1 132 ? 52.315  35.879  22.426  1.00 79.26  ? 133 LEU C CG  1 
ATOM   7250  C  CD1 . LEU C 1 132 ? 52.263  35.970  20.907  1.00 77.46  ? 133 LEU C CD1 1 
ATOM   7251  C  CD2 . LEU C 1 132 ? 51.885  37.193  23.061  1.00 79.63  ? 133 LEU C CD2 1 
ATOM   7252  N  N   . TYR C 1 133 ? 50.515  32.542  25.358  1.00 73.38  ? 134 TYR C N   1 
ATOM   7253  C  CA  . TYR C 1 133 ? 49.555  31.616  25.938  1.00 72.78  ? 134 TYR C CA  1 
ATOM   7254  C  C   . TYR C 1 133 ? 49.764  31.460  27.441  1.00 74.39  ? 134 TYR C C   1 
ATOM   7255  O  O   . TYR C 1 133 ? 48.797  31.433  28.203  1.00 72.29  ? 134 TYR C O   1 
ATOM   7256  C  CB  . TYR C 1 133 ? 49.646  30.242  25.271  1.00 69.97  ? 134 TYR C CB  1 
ATOM   7257  C  CG  . TYR C 1 133 ? 49.046  29.140  26.117  1.00 69.38  ? 134 TYR C CG  1 
ATOM   7258  C  CD1 . TYR C 1 133 ? 47.671  28.972  26.195  1.00 71.22  ? 134 TYR C CD1 1 
ATOM   7259  C  CD2 . TYR C 1 133 ? 49.855  28.276  26.848  1.00 64.45  ? 134 TYR C CD2 1 
ATOM   7260  C  CE1 . TYR C 1 133 ? 47.116  27.974  26.972  1.00 61.60  ? 134 TYR C CE1 1 
ATOM   7261  C  CE2 . TYR C 1 133 ? 49.307  27.275  27.628  1.00 65.66  ? 134 TYR C CE2 1 
ATOM   7262  C  CZ  . TYR C 1 133 ? 47.938  27.128  27.684  1.00 65.03  ? 134 TYR C CZ  1 
ATOM   7263  O  OH  . TYR C 1 133 ? 47.387  26.132  28.458  1.00 66.85  ? 134 TYR C OH  1 
ATOM   7264  N  N   . THR C 1 134 ? 51.027  31.349  27.853  1.00 77.68  ? 135 THR C N   1 
ATOM   7265  C  CA  . THR C 1 134 ? 51.379  31.007  29.235  1.00 83.66  ? 135 THR C CA  1 
ATOM   7266  C  C   . THR C 1 134 ? 50.677  31.867  30.288  1.00 88.43  ? 135 THR C C   1 
ATOM   7267  O  O   . THR C 1 134 ? 50.215  31.354  31.308  1.00 88.84  ? 135 THR C O   1 
ATOM   7268  C  CB  . THR C 1 134 ? 52.902  31.110  29.463  1.00 86.80  ? 135 THR C CB  1 
ATOM   7269  O  OG1 . THR C 1 134 ? 53.589  30.305  28.497  1.00 87.79  ? 135 THR C OG1 1 
ATOM   7270  C  CG2 . THR C 1 134 ? 53.274  30.642  30.862  1.00 87.06  ? 135 THR C CG2 1 
ATOM   7271  N  N   . GLN C 1 135 ? 50.588  33.169  30.039  1.00 97.00  ? 136 GLN C N   1 
ATOM   7272  C  CA  . GLN C 1 135 ? 49.951  34.075  30.990  1.00 99.36  ? 136 GLN C CA  1 
ATOM   7273  C  C   . GLN C 1 135 ? 48.446  34.173  30.741  1.00 94.60  ? 136 GLN C C   1 
ATOM   7274  O  O   . GLN C 1 135 ? 47.678  34.518  31.639  1.00 97.18  ? 136 GLN C O   1 
ATOM   7275  C  CB  . GLN C 1 135 ? 50.598  35.462  30.921  1.00 108.79 ? 136 GLN C CB  1 
ATOM   7276  C  CG  . GLN C 1 135 ? 50.087  36.449  31.963  1.00 114.32 ? 136 GLN C CG  1 
ATOM   7277  C  CD  . GLN C 1 135 ? 50.081  35.869  33.366  1.00 117.81 ? 136 GLN C CD  1 
ATOM   7278  O  OE1 . GLN C 1 135 ? 51.102  35.385  33.855  1.00 120.20 ? 136 GLN C OE1 1 
ATOM   7279  N  NE2 . GLN C 1 135 ? 48.925  35.913  34.019  1.00 117.36 ? 136 GLN C NE2 1 
ATOM   7280  N  N   . ASN C 1 136 ? 48.029  33.850  29.522  1.00 86.48  ? 137 ASN C N   1 
ATOM   7281  C  CA  . ASN C 1 136 ? 46.625  33.958  29.141  1.00 79.91  ? 137 ASN C CA  1 
ATOM   7282  C  C   . ASN C 1 136 ? 45.896  32.617  29.172  1.00 77.68  ? 137 ASN C C   1 
ATOM   7283  O  O   . ASN C 1 136 ? 44.762  32.513  28.708  1.00 73.57  ? 137 ASN C O   1 
ATOM   7284  C  CB  . ASN C 1 136 ? 46.510  34.573  27.746  1.00 77.74  ? 137 ASN C CB  1 
ATOM   7285  C  CG  . ASN C 1 136 ? 47.319  35.845  27.602  1.00 76.51  ? 137 ASN C CG  1 
ATOM   7286  O  OD1 . ASN C 1 136 ? 47.180  36.777  28.394  1.00 77.85  ? 137 ASN C OD1 1 
ATOM   7287  N  ND2 . ASN C 1 136 ? 48.183  35.884  26.596  1.00 74.42  ? 137 ASN C ND2 1 
ATOM   7288  N  N   . ALA C 1 137 ? 46.550  31.602  29.730  1.00 77.89  ? 138 ALA C N   1 
ATOM   7289  C  CA  . ALA C 1 137 ? 46.041  30.230  29.707  1.00 77.58  ? 138 ALA C CA  1 
ATOM   7290  C  C   . ALA C 1 137 ? 44.674  30.077  30.376  1.00 81.26  ? 138 ALA C C   1 
ATOM   7291  O  O   . ALA C 1 137 ? 43.811  29.338  29.889  1.00 81.52  ? 138 ALA C O   1 
ATOM   7292  C  CB  . ALA C 1 137 ? 47.047  29.296  30.365  1.00 77.87  ? 138 ALA C CB  1 
ATOM   7293  N  N   . ARG C 1 138 ? 44.482  30.776  31.491  1.00 81.36  ? 139 ARG C N   1 
ATOM   7294  C  CA  . ARG C 1 138 ? 43.242  30.676  32.255  1.00 80.84  ? 139 ARG C CA  1 
ATOM   7295  C  C   . ARG C 1 138 ? 42.040  31.178  31.458  1.00 79.78  ? 139 ARG C C   1 
ATOM   7296  O  O   . ARG C 1 138 ? 40.912  30.743  31.689  1.00 78.56  ? 139 ARG C O   1 
ATOM   7297  C  CB  . ARG C 1 138 ? 43.361  31.451  33.568  1.00 82.30  ? 139 ARG C CB  1 
ATOM   7298  N  N   . ALA C 1 139 ? 42.282  32.094  30.526  1.00 75.63  ? 140 ALA C N   1 
ATOM   7299  C  CA  . ALA C 1 139 ? 41.229  32.565  29.634  1.00 71.62  ? 140 ALA C CA  1 
ATOM   7300  C  C   . ALA C 1 139 ? 40.704  31.402  28.799  1.00 74.05  ? 140 ALA C C   1 
ATOM   7301  O  O   . ALA C 1 139 ? 39.492  31.174  28.713  1.00 74.98  ? 140 ALA C O   1 
ATOM   7302  C  CB  . ALA C 1 139 ? 41.742  33.680  28.739  1.00 67.32  ? 140 ALA C CB  1 
ATOM   7303  N  N   . PHE C 1 140 ? 41.631  30.663  28.195  1.00 76.05  ? 141 PHE C N   1 
ATOM   7304  C  CA  . PHE C 1 140 ? 41.292  29.476  27.421  1.00 74.05  ? 141 PHE C CA  1 
ATOM   7305  C  C   . PHE C 1 140 ? 40.611  28.434  28.302  1.00 77.76  ? 141 PHE C C   1 
ATOM   7306  O  O   . PHE C 1 140 ? 39.641  27.797  27.887  1.00 78.26  ? 141 PHE C O   1 
ATOM   7307  C  CB  . PHE C 1 140 ? 42.542  28.876  26.772  1.00 72.52  ? 141 PHE C CB  1 
ATOM   7308  C  CG  . PHE C 1 140 ? 43.328  29.852  25.942  1.00 72.92  ? 141 PHE C CG  1 
ATOM   7309  C  CD1 . PHE C 1 140 ? 42.953  30.135  24.638  1.00 72.27  ? 141 PHE C CD1 1 
ATOM   7310  C  CD2 . PHE C 1 140 ? 44.449  30.477  26.461  1.00 74.35  ? 141 PHE C CD2 1 
ATOM   7311  C  CE1 . PHE C 1 140 ? 43.679  31.031  23.872  1.00 74.63  ? 141 PHE C CE1 1 
ATOM   7312  C  CE2 . PHE C 1 140 ? 45.178  31.374  25.701  1.00 74.66  ? 141 PHE C CE2 1 
ATOM   7313  C  CZ  . PHE C 1 140 ? 44.792  31.651  24.405  1.00 75.33  ? 141 PHE C CZ  1 
ATOM   7314  N  N   . ARG C 1 141 ? 41.124  28.268  29.519  1.00 78.52  ? 142 ARG C N   1 
ATOM   7315  C  CA  . ARG C 1 141 ? 40.550  27.317  30.468  1.00 80.55  ? 142 ARG C CA  1 
ATOM   7316  C  C   . ARG C 1 141 ? 39.077  27.616  30.740  1.00 86.67  ? 142 ARG C C   1 
ATOM   7317  O  O   . ARG C 1 141 ? 38.223  26.725  30.668  1.00 84.59  ? 142 ARG C O   1 
ATOM   7318  C  CB  . ARG C 1 141 ? 41.336  27.329  31.781  1.00 75.70  ? 142 ARG C CB  1 
ATOM   7319  C  CG  . ARG C 1 141 ? 40.661  26.564  32.909  1.00 73.17  ? 142 ARG C CG  1 
ATOM   7320  C  CD  . ARG C 1 141 ? 41.501  26.577  34.176  1.00 74.97  ? 142 ARG C CD  1 
ATOM   7321  N  NE  . ARG C 1 141 ? 42.823  25.994  33.964  1.00 75.79  ? 142 ARG C NE  1 
ATOM   7322  C  CZ  . ARG C 1 141 ? 43.964  26.661  34.104  1.00 79.36  ? 142 ARG C CZ  1 
ATOM   7323  N  NH1 . ARG C 1 141 ? 43.949  27.938  34.459  1.00 82.09  ? 142 ARG C NH1 1 
ATOM   7324  N  NH2 . ARG C 1 141 ? 45.122  26.050  33.891  1.00 80.32  ? 142 ARG C NH2 1 
ATOM   7325  N  N   . ASP C 1 142 ? 38.786  28.877  31.046  1.00 94.84  ? 143 ASP C N   1 
ATOM   7326  C  CA  . ASP C 1 142 ? 37.418  29.310  31.305  1.00 95.53  ? 143 ASP C CA  1 
ATOM   7327  C  C   . ASP C 1 142 ? 36.559  29.189  30.048  1.00 88.45  ? 143 ASP C C   1 
ATOM   7328  O  O   . ASP C 1 142 ? 35.360  28.900  30.129  1.00 92.79  ? 143 ASP C O   1 
ATOM   7329  C  CB  . ASP C 1 142 ? 37.406  30.747  31.830  1.00 103.99 ? 143 ASP C CB  1 
ATOM   7330  C  CG  . ASP C 1 142 ? 38.129  30.886  33.159  1.00 112.97 ? 143 ASP C CG  1 
ATOM   7331  O  OD1 . ASP C 1 142 ? 38.952  30.005  33.486  1.00 114.93 ? 143 ASP C OD1 1 
ATOM   7332  O  OD2 . ASP C 1 142 ? 37.878  31.878  33.875  1.00 115.68 ? 143 ASP C OD2 1 
ATOM   7333  N  N   . LEU C 1 143 ? 37.180  29.404  28.890  1.00 78.11  ? 144 LEU C N   1 
ATOM   7334  C  CA  . LEU C 1 143 ? 36.502  29.191  27.616  1.00 70.88  ? 144 LEU C CA  1 
ATOM   7335  C  C   . LEU C 1 143 ? 36.012  27.748  27.505  1.00 61.79  ? 144 LEU C C   1 
ATOM   7336  O  O   . LEU C 1 143 ? 34.845  27.497  27.182  1.00 55.16  ? 144 LEU C O   1 
ATOM   7337  C  CB  . LEU C 1 143 ? 37.428  29.524  26.444  1.00 67.52  ? 144 LEU C CB  1 
ATOM   7338  C  CG  . LEU C 1 143 ? 36.773  29.491  25.061  1.00 68.21  ? 144 LEU C CG  1 
ATOM   7339  C  CD1 . LEU C 1 143 ? 35.647  30.513  24.976  1.00 66.81  ? 144 LEU C CD1 1 
ATOM   7340  C  CD2 . LEU C 1 143 ? 37.797  29.715  23.955  1.00 65.31  ? 144 LEU C CD2 1 
ATOM   7341  N  N   . TYR C 1 144 ? 36.906  26.805  27.787  1.00 61.45  ? 145 TYR C N   1 
ATOM   7342  C  CA  . TYR C 1 144 ? 36.561  25.387  27.741  1.00 60.46  ? 145 TYR C CA  1 
ATOM   7343  C  C   . TYR C 1 144 ? 35.516  25.009  28.783  1.00 60.85  ? 145 TYR C C   1 
ATOM   7344  O  O   . TYR C 1 144 ? 34.626  24.205  28.510  1.00 60.80  ? 145 TYR C O   1 
ATOM   7345  C  CB  . TYR C 1 144 ? 37.807  24.523  27.929  1.00 61.28  ? 145 TYR C CB  1 
ATOM   7346  C  CG  . TYR C 1 144 ? 38.580  24.288  26.654  1.00 60.31  ? 145 TYR C CG  1 
ATOM   7347  C  CD1 . TYR C 1 144 ? 39.537  25.193  26.222  1.00 61.01  ? 145 TYR C CD1 1 
ATOM   7348  C  CD2 . TYR C 1 144 ? 38.343  23.162  25.877  1.00 58.57  ? 145 TYR C CD2 1 
ATOM   7349  C  CE1 . TYR C 1 144 ? 40.244  24.981  25.055  1.00 61.83  ? 145 TYR C CE1 1 
ATOM   7350  C  CE2 . TYR C 1 144 ? 39.043  22.941  24.708  1.00 58.88  ? 145 TYR C CE2 1 
ATOM   7351  C  CZ  . TYR C 1 144 ? 39.992  23.854  24.302  1.00 58.11  ? 145 TYR C CZ  1 
ATOM   7352  O  OH  . TYR C 1 144 ? 40.693  23.640  23.139  1.00 59.53  ? 145 TYR C OH  1 
ATOM   7353  N  N   . SER C 1 145 ? 35.629  25.583  29.978  1.00 70.77  ? 146 SER C N   1 
ATOM   7354  C  CA  . SER C 1 145 ? 34.656  25.321  31.034  1.00 75.76  ? 146 SER C CA  1 
ATOM   7355  C  C   . SER C 1 145 ? 33.256  25.770  30.615  1.00 79.73  ? 146 SER C C   1 
ATOM   7356  O  O   . SER C 1 145 ? 32.268  25.039  30.789  1.00 80.32  ? 146 SER C O   1 
ATOM   7357  C  CB  . SER C 1 145 ? 35.071  26.018  32.332  1.00 80.10  ? 146 SER C CB  1 
ATOM   7358  O  OG  . SER C 1 145 ? 36.443  25.797  32.616  1.00 82.13  ? 146 SER C OG  1 
ATOM   7359  N  N   . GLU C 1 146 ? 33.174  26.970  30.048  1.00 83.39  ? 147 GLU C N   1 
ATOM   7360  C  CA  . GLU C 1 146 ? 31.889  27.502  29.614  1.00 84.68  ? 147 GLU C CA  1 
ATOM   7361  C  C   . GLU C 1 146 ? 31.348  26.734  28.407  1.00 77.96  ? 147 GLU C C   1 
ATOM   7362  O  O   . GLU C 1 146 ? 30.135  26.585  28.257  1.00 79.41  ? 147 GLU C O   1 
ATOM   7363  C  CB  . GLU C 1 146 ? 31.999  28.994  29.295  1.00 92.81  ? 147 GLU C CB  1 
ATOM   7364  C  CG  . GLU C 1 146 ? 30.826  29.810  29.817  1.00 99.58  ? 147 GLU C CG  1 
ATOM   7365  C  CD  . GLU C 1 146 ? 30.985  30.190  31.278  1.00 105.84 ? 147 GLU C CD  1 
ATOM   7366  O  OE1 . GLU C 1 146 ? 32.006  29.805  31.887  1.00 107.26 ? 147 GLU C OE1 1 
ATOM   7367  O  OE2 . GLU C 1 146 ? 30.080  30.857  31.823  1.00 107.87 ? 147 GLU C OE2 1 
ATOM   7368  N  N   . LEU C 1 147 ? 32.243  26.242  27.554  1.00 66.76  ? 148 LEU C N   1 
ATOM   7369  C  CA  . LEU C 1 147 ? 31.829  25.347  26.474  1.00 58.95  ? 148 LEU C CA  1 
ATOM   7370  C  C   . LEU C 1 147 ? 31.215  24.076  27.051  1.00 56.63  ? 148 LEU C C   1 
ATOM   7371  O  O   . LEU C 1 147 ? 30.218  23.562  26.534  1.00 56.10  ? 148 LEU C O   1 
ATOM   7372  C  CB  . LEU C 1 147 ? 33.005  24.988  25.559  1.00 57.82  ? 148 LEU C CB  1 
ATOM   7373  C  CG  . LEU C 1 147 ? 33.414  25.973  24.462  1.00 55.57  ? 148 LEU C CG  1 
ATOM   7374  C  CD1 . LEU C 1 147 ? 34.396  25.316  23.499  1.00 52.15  ? 148 LEU C CD1 1 
ATOM   7375  C  CD2 . LEU C 1 147 ? 32.194  26.481  23.714  1.00 51.33  ? 148 LEU C CD2 1 
ATOM   7376  N  N   . ARG C 1 148 ? 31.819  23.578  28.126  1.00 55.38  ? 149 ARG C N   1 
ATOM   7377  C  CA  . ARG C 1 148 ? 31.303  22.408  28.824  1.00 58.58  ? 149 ARG C CA  1 
ATOM   7378  C  C   . ARG C 1 148 ? 29.909  22.666  29.372  1.00 58.74  ? 149 ARG C C   1 
ATOM   7379  O  O   . ARG C 1 148 ? 29.025  21.818  29.252  1.00 54.81  ? 149 ARG C O   1 
ATOM   7380  C  CB  . ARG C 1 148 ? 32.233  21.999  29.966  1.00 49.32  ? 149 ARG C CB  1 
ATOM   7381  C  CG  . ARG C 1 148 ? 33.401  21.145  29.540  1.00 49.41  ? 149 ARG C CG  1 
ATOM   7382  C  CD  . ARG C 1 148 ? 34.041  20.474  30.739  1.00 50.02  ? 149 ARG C CD  1 
ATOM   7383  N  NE  . ARG C 1 148 ? 35.435  20.134  30.480  1.00 59.58  ? 149 ARG C NE  1 
ATOM   7384  C  CZ  . ARG C 1 148 ? 36.437  21.003  30.551  1.00 61.78  ? 149 ARG C CZ  1 
ATOM   7385  N  NH1 . ARG C 1 148 ? 36.203  22.268  30.875  1.00 57.51  ? 149 ARG C NH1 1 
ATOM   7386  N  NH2 . ARG C 1 148 ? 37.675  20.606  30.299  1.00 63.36  ? 149 ARG C NH2 1 
ATOM   7387  N  N   . LEU C 1 149 ? 29.716  23.832  29.981  1.00 66.35  ? 150 LEU C N   1 
ATOM   7388  C  CA  . LEU C 1 149 ? 28.394  24.187  30.490  1.00 71.49  ? 150 LEU C CA  1 
ATOM   7389  C  C   . LEU C 1 149 ? 27.370  24.294  29.361  1.00 73.52  ? 150 LEU C C   1 
ATOM   7390  O  O   . LEU C 1 149 ? 26.232  23.844  29.502  1.00 75.34  ? 150 LEU C O   1 
ATOM   7391  C  CB  . LEU C 1 149 ? 28.453  25.495  31.278  1.00 74.92  ? 150 LEU C CB  1 
ATOM   7392  C  CG  . LEU C 1 149 ? 28.763  25.317  32.766  1.00 78.24  ? 150 LEU C CG  1 
ATOM   7393  C  CD1 . LEU C 1 149 ? 29.545  26.503  33.310  1.00 79.56  ? 150 LEU C CD1 1 
ATOM   7394  C  CD2 . LEU C 1 149 ? 27.477  25.105  33.551  1.00 78.35  ? 150 LEU C CD2 1 
ATOM   7395  N  N   . TYR C 1 150 ? 27.787  24.889  28.246  1.00 74.38  ? 151 TYR C N   1 
ATOM   7396  C  CA  . TYR C 1 150 ? 26.950  25.010  27.055  1.00 72.67  ? 151 TYR C CA  1 
ATOM   7397  C  C   . TYR C 1 150 ? 26.487  23.641  26.575  1.00 70.41  ? 151 TYR C C   1 
ATOM   7398  O  O   . TYR C 1 150 ? 25.301  23.428  26.320  1.00 71.28  ? 151 TYR C O   1 
ATOM   7399  C  CB  . TYR C 1 150 ? 27.714  25.731  25.940  1.00 76.29  ? 151 TYR C CB  1 
ATOM   7400  C  CG  . TYR C 1 150 ? 26.870  26.156  24.755  1.00 81.79  ? 151 TYR C CG  1 
ATOM   7401  C  CD1 . TYR C 1 150 ? 25.959  27.199  24.862  1.00 85.08  ? 151 TYR C CD1 1 
ATOM   7402  C  CD2 . TYR C 1 150 ? 26.998  25.524  23.523  1.00 82.95  ? 151 TYR C CD2 1 
ATOM   7403  C  CE1 . TYR C 1 150 ? 25.194  27.596  23.778  1.00 85.90  ? 151 TYR C CE1 1 
ATOM   7404  C  CE2 . TYR C 1 150 ? 26.235  25.914  22.435  1.00 84.10  ? 151 TYR C CE2 1 
ATOM   7405  C  CZ  . TYR C 1 150 ? 25.336  26.950  22.569  1.00 85.85  ? 151 TYR C CZ  1 
ATOM   7406  O  OH  . TYR C 1 150 ? 24.574  27.342  21.491  1.00 87.79  ? 151 TYR C OH  1 
ATOM   7407  N  N   . TYR C 1 151 ? 27.432  22.713  26.460  1.00 64.37  ? 152 TYR C N   1 
ATOM   7408  C  CA  . TYR C 1 151 ? 27.116  21.354  26.039  1.00 65.56  ? 152 TYR C CA  1 
ATOM   7409  C  C   . TYR C 1 151 ? 26.230  20.621  27.045  1.00 63.85  ? 152 TYR C C   1 
ATOM   7410  O  O   . TYR C 1 151 ? 25.372  19.827  26.662  1.00 64.04  ? 152 TYR C O   1 
ATOM   7411  C  CB  . TYR C 1 151 ? 28.398  20.549  25.811  1.00 60.07  ? 152 TYR C CB  1 
ATOM   7412  C  CG  . TYR C 1 151 ? 28.155  19.060  25.721  1.00 54.08  ? 152 TYR C CG  1 
ATOM   7413  C  CD1 . TYR C 1 151 ? 27.598  18.495  24.581  1.00 44.38  ? 152 TYR C CD1 1 
ATOM   7414  C  CD2 . TYR C 1 151 ? 28.469  18.219  26.782  1.00 45.03  ? 152 TYR C CD2 1 
ATOM   7415  C  CE1 . TYR C 1 151 ? 27.368  17.135  24.497  1.00 49.48  ? 152 TYR C CE1 1 
ATOM   7416  C  CE2 . TYR C 1 151 ? 28.241  16.859  26.708  1.00 44.43  ? 152 TYR C CE2 1 
ATOM   7417  C  CZ  . TYR C 1 151 ? 27.691  16.322  25.563  1.00 43.79  ? 152 TYR C CZ  1 
ATOM   7418  O  OH  . TYR C 1 151 ? 27.463  14.968  25.483  1.00 44.70  ? 152 TYR C OH  1 
ATOM   7419  N  N   . ARG C 1 152 ? 26.442  20.890  28.329  1.00 71.08  ? 153 ARG C N   1 
ATOM   7420  C  CA  . ARG C 1 152 ? 25.770  20.138  29.386  1.00 76.06  ? 153 ARG C CA  1 
ATOM   7421  C  C   . ARG C 1 152 ? 24.298  20.502  29.551  1.00 79.76  ? 153 ARG C C   1 
ATOM   7422  O  O   . ARG C 1 152 ? 23.598  19.913  30.374  1.00 79.38  ? 153 ARG C O   1 
ATOM   7423  C  CB  . ARG C 1 152 ? 26.492  20.336  30.720  1.00 81.26  ? 153 ARG C CB  1 
ATOM   7424  C  CG  . ARG C 1 152 ? 27.123  19.068  31.267  1.00 85.70  ? 153 ARG C CG  1 
ATOM   7425  C  CD  . ARG C 1 152 ? 27.589  19.255  32.700  1.00 90.60  ? 153 ARG C CD  1 
ATOM   7426  N  NE  . ARG C 1 152 ? 26.510  19.720  33.568  1.00 94.61  ? 153 ARG C NE  1 
ATOM   7427  C  CZ  . ARG C 1 152 ? 26.695  20.455  34.660  1.00 98.17  ? 153 ARG C CZ  1 
ATOM   7428  N  NH1 . ARG C 1 152 ? 27.920  20.808  35.024  1.00 99.30  ? 153 ARG C NH1 1 
ATOM   7429  N  NH2 . ARG C 1 152 ? 25.656  20.835  35.391  1.00 99.74  ? 153 ARG C NH2 1 
ATOM   7430  N  N   . GLY C 1 153 ? 23.825  21.470  28.777  1.00 81.12  ? 154 GLY C N   1 
ATOM   7431  C  CA  . GLY C 1 153 ? 22.421  21.828  28.822  1.00 85.46  ? 154 GLY C CA  1 
ATOM   7432  C  C   . GLY C 1 153 ? 22.146  23.108  29.582  1.00 89.83  ? 154 GLY C C   1 
ATOM   7433  O  O   . GLY C 1 153 ? 21.010  23.580  29.619  1.00 90.82  ? 154 GLY C O   1 
ATOM   7434  N  N   . ALA C 1 154 ? 23.182  23.682  30.184  1.00 92.20  ? 155 ALA C N   1 
ATOM   7435  C  CA  . ALA C 1 154 ? 23.033  24.996  30.783  1.00 94.29  ? 155 ALA C CA  1 
ATOM   7436  C  C   . ALA C 1 154 ? 23.427  25.985  29.706  1.00 99.13  ? 155 ALA C C   1 
ATOM   7437  O  O   . ALA C 1 154 ? 24.598  26.095  29.344  1.00 101.63 ? 155 ALA C O   1 
ATOM   7438  C  CB  . ALA C 1 154 ? 23.901  25.145  32.021  1.00 91.92  ? 155 ALA C CB  1 
ATOM   7439  N  N   . ASN C 1 155 ? 22.443  26.719  29.205  1.00 101.07 ? 156 ASN C N   1 
ATOM   7440  C  CA  . ASN C 1 155 ? 22.613  27.404  27.936  1.00 101.48 ? 156 ASN C CA  1 
ATOM   7441  C  C   . ASN C 1 155 ? 22.674  28.914  28.071  1.00 102.66 ? 156 ASN C C   1 
ATOM   7442  O  O   . ASN C 1 155 ? 21.818  29.542  28.691  1.00 100.57 ? 156 ASN C O   1 
ATOM   7443  C  CB  . ASN C 1 155 ? 21.487  27.010  26.974  1.00 103.30 ? 156 ASN C CB  1 
ATOM   7444  C  CG  . ASN C 1 155 ? 21.799  27.360  25.527  1.00 105.32 ? 156 ASN C CG  1 
ATOM   7445  O  OD1 . ASN C 1 155 ? 22.531  28.307  25.244  1.00 107.40 ? 156 ASN C OD1 1 
ATOM   7446  N  ND2 . ASN C 1 155 ? 21.247  26.584  24.603  1.00 105.35 ? 156 ASN C ND2 1 
ATOM   7447  N  N   . LEU C 1 156 ? 23.713  29.477  27.472  1.00 102.50 ? 157 LEU C N   1 
ATOM   7448  C  CA  . LEU C 1 156 ? 23.894  30.912  27.371  1.00 107.31 ? 157 LEU C CA  1 
ATOM   7449  C  C   . LEU C 1 156 ? 24.082  31.235  25.899  1.00 118.55 ? 157 LEU C C   1 
ATOM   7450  O  O   . LEU C 1 156 ? 24.417  30.352  25.109  1.00 114.65 ? 157 LEU C O   1 
ATOM   7451  C  CB  . LEU C 1 156 ? 25.104  31.364  28.193  1.00 99.25  ? 157 LEU C CB  1 
ATOM   7452  C  CG  . LEU C 1 156 ? 25.508  32.839  28.306  1.00 93.73  ? 157 LEU C CG  1 
ATOM   7453  C  CD1 . LEU C 1 156 ? 24.312  33.788  28.362  1.00 92.14  ? 157 LEU C CD1 1 
ATOM   7454  C  CD2 . LEU C 1 156 ? 26.415  33.033  29.510  1.00 91.01  ? 157 LEU C CD2 1 
ATOM   7455  N  N   . HIS C 1 157 ? 23.842  32.484  25.520  1.00 135.17 ? 158 HIS C N   1 
ATOM   7456  C  CA  . HIS C 1 157 ? 24.235  32.940  24.200  1.00 137.49 ? 158 HIS C CA  1 
ATOM   7457  C  C   . HIS C 1 157 ? 25.726  32.678  24.045  1.00 134.59 ? 158 HIS C C   1 
ATOM   7458  O  O   . HIS C 1 157 ? 26.550  33.340  24.678  1.00 138.37 ? 158 HIS C O   1 
ATOM   7459  C  CB  . HIS C 1 157 ? 23.914  34.423  24.008  1.00 141.12 ? 158 HIS C CB  1 
ATOM   7460  N  N   . LEU C 1 158 ? 26.066  31.682  23.234  1.00 116.30 ? 159 LEU C N   1 
ATOM   7461  C  CA  . LEU C 1 158 ? 27.461  31.324  23.017  1.00 105.81 ? 159 LEU C CA  1 
ATOM   7462  C  C   . LEU C 1 158 ? 28.182  32.487  22.350  1.00 103.55 ? 159 LEU C C   1 
ATOM   7463  O  O   . LEU C 1 158 ? 29.365  32.739  22.605  1.00 105.30 ? 159 LEU C O   1 
ATOM   7464  C  CB  . LEU C 1 158 ? 27.566  30.060  22.164  1.00 93.90  ? 159 LEU C CB  1 
ATOM   7465  C  CG  . LEU C 1 158 ? 28.975  29.518  21.932  1.00 81.85  ? 159 LEU C CG  1 
ATOM   7466  C  CD1 . LEU C 1 158 ? 29.506  28.876  23.203  1.00 74.13  ? 159 LEU C CD1 1 
ATOM   7467  C  CD2 . LEU C 1 158 ? 28.983  28.529  20.781  1.00 76.45  ? 159 LEU C CD2 1 
ATOM   7468  N  N   . GLU C 1 159 ? 27.442  33.197  21.503  1.00 105.03 ? 160 GLU C N   1 
ATOM   7469  C  CA  . GLU C 1 159 ? 27.942  34.382  20.820  1.00 109.12 ? 160 GLU C CA  1 
ATOM   7470  C  C   . GLU C 1 159 ? 28.467  35.418  21.806  1.00 106.87 ? 160 GLU C C   1 
ATOM   7471  O  O   . GLU C 1 159 ? 29.511  36.021  21.578  1.00 110.24 ? 160 GLU C O   1 
ATOM   7472  C  CB  . GLU C 1 159 ? 26.845  35.004  19.954  1.00 116.69 ? 160 GLU C CB  1 
ATOM   7473  C  CG  . GLU C 1 159 ? 26.728  34.408  18.562  1.00 122.81 ? 160 GLU C CG  1 
ATOM   7474  C  CD  . GLU C 1 159 ? 25.666  35.096  17.725  1.00 128.73 ? 160 GLU C CD  1 
ATOM   7475  O  OE1 . GLU C 1 159 ? 24.891  35.898  18.288  1.00 131.28 ? 160 GLU C OE1 1 
ATOM   7476  O  OE2 . GLU C 1 159 ? 25.613  34.842  16.504  1.00 130.70 ? 160 GLU C OE2 1 
ATOM   7477  N  N   . GLU C 1 160 ? 27.736  35.620  22.898  1.00 100.55 ? 161 GLU C N   1 
ATOM   7478  C  CA  . GLU C 1 160 ? 28.120  36.599  23.910  1.00 96.09  ? 161 GLU C CA  1 
ATOM   7479  C  C   . GLU C 1 160 ? 29.433  36.214  24.586  1.00 88.61  ? 161 GLU C C   1 
ATOM   7480  O  O   . GLU C 1 160 ? 30.380  37.009  24.638  1.00 89.75  ? 161 GLU C O   1 
ATOM   7481  C  CB  . GLU C 1 160 ? 27.014  36.746  24.957  1.00 96.86  ? 161 GLU C CB  1 
ATOM   7482  N  N   . THR C 1 161 ? 29.474  34.987  25.099  1.00 80.07  ? 162 THR C N   1 
ATOM   7483  C  CA  . THR C 1 161 ? 30.653  34.455  25.773  1.00 73.75  ? 162 THR C CA  1 
ATOM   7484  C  C   . THR C 1 161 ? 31.885  34.549  24.881  1.00 66.72  ? 162 THR C C   1 
ATOM   7485  O  O   . THR C 1 161 ? 32.922  35.089  25.285  1.00 59.95  ? 162 THR C O   1 
ATOM   7486  C  CB  . THR C 1 161 ? 30.443  32.985  26.189  1.00 72.18  ? 162 THR C CB  1 
ATOM   7487  O  OG1 . THR C 1 161 ? 29.119  32.815  26.711  1.00 72.07  ? 162 THR C OG1 1 
ATOM   7488  C  CG2 . THR C 1 161 ? 31.465  32.573  27.239  1.00 73.34  ? 162 THR C CG2 1 
ATOM   7489  N  N   . LEU C 1 162 ? 31.757  34.030  23.663  1.00 68.38  ? 163 LEU C N   1 
ATOM   7490  C  CA  . LEU C 1 162 ? 32.849  34.075  22.699  1.00 70.61  ? 163 LEU C CA  1 
ATOM   7491  C  C   . LEU C 1 162 ? 33.276  35.511  22.409  1.00 75.26  ? 163 LEU C C   1 
ATOM   7492  O  O   . LEU C 1 162 ? 34.466  35.805  22.357  1.00 73.38  ? 163 LEU C O   1 
ATOM   7493  C  CB  . LEU C 1 162 ? 32.449  33.368  21.403  1.00 69.21  ? 163 LEU C CB  1 
ATOM   7494  C  CG  . LEU C 1 162 ? 32.397  31.842  21.487  1.00 69.33  ? 163 LEU C CG  1 
ATOM   7495  C  CD1 . LEU C 1 162 ? 31.800  31.251  20.223  1.00 69.84  ? 163 LEU C CD1 1 
ATOM   7496  C  CD2 . LEU C 1 162 ? 33.786  31.276  21.742  1.00 68.26  ? 163 LEU C CD2 1 
ATOM   7497  N  N   . ALA C 1 163 ? 32.302  36.401  22.240  1.00 79.78  ? 164 ALA C N   1 
ATOM   7498  C  CA  . ALA C 1 163 ? 32.581  37.806  21.953  1.00 89.82  ? 164 ALA C CA  1 
ATOM   7499  C  C   . ALA C 1 163 ? 33.424  38.448  23.049  1.00 92.10  ? 164 ALA C C   1 
ATOM   7500  O  O   . ALA C 1 163 ? 34.471  39.042  22.772  1.00 95.36  ? 164 ALA C O   1 
ATOM   7501  C  CB  . ALA C 1 163 ? 31.284  38.579  21.769  1.00 89.26  ? 164 ALA C CB  1 
ATOM   7502  N  N   . GLU C 1 164 ? 32.966  38.324  24.292  1.00 96.14  ? 165 GLU C N   1 
ATOM   7503  C  CA  . GLU C 1 164 ? 33.681  38.914  25.418  1.00 98.42  ? 165 GLU C CA  1 
ATOM   7504  C  C   . GLU C 1 164 ? 35.067  38.287  25.566  1.00 96.19  ? 165 GLU C C   1 
ATOM   7505  O  O   . GLU C 1 164 ? 36.045  38.980  25.882  1.00 100.16 ? 165 GLU C O   1 
ATOM   7506  C  CB  . GLU C 1 164 ? 32.876  38.756  26.709  1.00 106.13 ? 165 GLU C CB  1 
ATOM   7507  C  CG  . GLU C 1 164 ? 33.064  39.901  27.693  1.00 114.93 ? 165 GLU C CG  1 
ATOM   7508  C  CD  . GLU C 1 164 ? 31.836  40.140  28.551  1.00 121.90 ? 165 GLU C CD  1 
ATOM   7509  O  OE1 . GLU C 1 164 ? 31.892  39.864  29.767  1.00 124.07 ? 165 GLU C OE1 1 
ATOM   7510  O  OE2 . GLU C 1 164 ? 30.812  40.604  28.006  1.00 124.15 ? 165 GLU C OE2 1 
ATOM   7511  N  N   . PHE C 1 165 ? 35.144  36.980  25.320  1.00 88.31  ? 166 PHE C N   1 
ATOM   7512  C  CA  . PHE C 1 165 ? 36.422  36.272  25.328  1.00 83.09  ? 166 PHE C CA  1 
ATOM   7513  C  C   . PHE C 1 165 ? 37.407  36.894  24.342  1.00 79.49  ? 166 PHE C C   1 
ATOM   7514  O  O   . PHE C 1 165 ? 38.532  37.236  24.710  1.00 79.90  ? 166 PHE C O   1 
ATOM   7515  C  CB  . PHE C 1 165 ? 36.221  34.790  24.998  1.00 76.52  ? 166 PHE C CB  1 
ATOM   7516  C  CG  . PHE C 1 165 ? 37.503  34.046  24.741  1.00 74.02  ? 166 PHE C CG  1 
ATOM   7517  C  CD1 . PHE C 1 165 ? 38.287  33.603  25.793  1.00 71.61  ? 166 PHE C CD1 1 
ATOM   7518  C  CD2 . PHE C 1 165 ? 37.921  33.783  23.444  1.00 71.31  ? 166 PHE C CD2 1 
ATOM   7519  C  CE1 . PHE C 1 165 ? 39.466  32.917  25.559  1.00 70.30  ? 166 PHE C CE1 1 
ATOM   7520  C  CE2 . PHE C 1 165 ? 39.099  33.100  23.204  1.00 69.86  ? 166 PHE C CE2 1 
ATOM   7521  C  CZ  . PHE C 1 165 ? 39.872  32.666  24.263  1.00 69.92  ? 166 PHE C CZ  1 
ATOM   7522  N  N   . TRP C 1 166 ? 36.975  37.042  23.093  1.00 78.45  ? 167 TRP C N   1 
ATOM   7523  C  CA  . TRP C 1 166 ? 37.827  37.593  22.045  1.00 76.45  ? 167 TRP C CA  1 
ATOM   7524  C  C   . TRP C 1 166 ? 38.205  39.042  22.325  1.00 78.31  ? 167 TRP C C   1 
ATOM   7525  O  O   . TRP C 1 166 ? 39.320  39.460  22.023  1.00 75.66  ? 167 TRP C O   1 
ATOM   7526  C  CB  . TRP C 1 166 ? 37.145  37.488  20.678  1.00 79.42  ? 167 TRP C CB  1 
ATOM   7527  C  CG  . TRP C 1 166 ? 37.059  36.085  20.155  1.00 79.53  ? 167 TRP C CG  1 
ATOM   7528  C  CD1 . TRP C 1 166 ? 35.925  35.364  19.920  1.00 79.37  ? 167 TRP C CD1 1 
ATOM   7529  C  CD2 . TRP C 1 166 ? 38.155  35.229  19.811  1.00 80.98  ? 167 TRP C CD2 1 
ATOM   7530  N  NE1 . TRP C 1 166 ? 36.245  34.115  19.450  1.00 79.12  ? 167 TRP C NE1 1 
ATOM   7531  C  CE2 . TRP C 1 166 ? 37.609  34.006  19.374  1.00 81.17  ? 167 TRP C CE2 1 
ATOM   7532  C  CE3 . TRP C 1 166 ? 39.545  35.379  19.828  1.00 83.71  ? 167 TRP C CE3 1 
ATOM   7533  C  CZ2 . TRP C 1 166 ? 38.403  32.940  18.958  1.00 82.18  ? 167 TRP C CZ2 1 
ATOM   7534  C  CZ3 . TRP C 1 166 ? 40.331  34.319  19.414  1.00 83.57  ? 167 TRP C CZ3 1 
ATOM   7535  C  CH2 . TRP C 1 166 ? 39.758  33.116  18.985  1.00 83.75  ? 167 TRP C CH2 1 
ATOM   7536  N  N   . ALA C 1 167 ? 37.280  39.805  22.899  1.00 76.18  ? 168 ALA C N   1 
ATOM   7537  C  CA  . ALA C 1 167 ? 37.557  41.198  23.242  1.00 79.17  ? 168 ALA C CA  1 
ATOM   7538  C  C   . ALA C 1 167 ? 38.648  41.300  24.309  1.00 79.11  ? 168 ALA C C   1 
ATOM   7539  O  O   . ALA C 1 167 ? 39.698  41.929  24.093  1.00 79.81  ? 168 ALA C O   1 
ATOM   7540  C  CB  . ALA C 1 167 ? 36.287  41.889  23.715  1.00 77.52  ? 168 ALA C CB  1 
ATOM   7541  N  N   . ARG C 1 168 ? 38.393  40.672  25.455  1.00 79.67  ? 169 ARG C N   1 
ATOM   7542  C  CA  . ARG C 1 168 ? 39.336  40.689  26.570  1.00 81.46  ? 169 ARG C CA  1 
ATOM   7543  C  C   . ARG C 1 168 ? 40.706  40.163  26.149  1.00 86.10  ? 169 ARG C C   1 
ATOM   7544  O  O   . ARG C 1 168 ? 41.742  40.797  26.406  1.00 90.98  ? 169 ARG C O   1 
ATOM   7545  C  CB  . ARG C 1 168 ? 38.794  39.865  27.740  1.00 77.14  ? 169 ARG C CB  1 
ATOM   7546  N  N   . LEU C 1 169 ? 40.700  39.007  25.490  1.00 83.01  ? 170 LEU C N   1 
ATOM   7547  C  CA  . LEU C 1 169 ? 41.932  38.393  25.012  1.00 80.90  ? 170 LEU C CA  1 
ATOM   7548  C  C   . LEU C 1 169 ? 42.653  39.310  24.033  1.00 82.63  ? 170 LEU C C   1 
ATOM   7549  O  O   . LEU C 1 169 ? 43.877  39.356  24.018  1.00 85.45  ? 170 LEU C O   1 
ATOM   7550  C  CB  . LEU C 1 169 ? 41.651  37.042  24.352  1.00 76.63  ? 170 LEU C CB  1 
ATOM   7551  C  CG  . LEU C 1 169 ? 42.883  36.289  23.841  1.00 73.82  ? 170 LEU C CG  1 
ATOM   7552  C  CD1 . LEU C 1 169 ? 43.778  35.874  25.000  1.00 72.25  ? 170 LEU C CD1 1 
ATOM   7553  C  CD2 . LEU C 1 169 ? 42.481  35.082  23.008  1.00 71.37  ? 170 LEU C CD2 1 
ATOM   7554  N  N   . LEU C 1 170 ? 41.895  40.042  23.221  1.00 81.29  ? 171 LEU C N   1 
ATOM   7555  C  CA  . LEU C 1 170 ? 42.499  40.977  22.277  1.00 78.75  ? 171 LEU C CA  1 
ATOM   7556  C  C   . LEU C 1 170 ? 43.202  42.108  23.010  1.00 79.48  ? 171 LEU C C   1 
ATOM   7557  O  O   . LEU C 1 170 ? 44.329  42.456  22.671  1.00 77.55  ? 171 LEU C O   1 
ATOM   7558  C  CB  . LEU C 1 170 ? 41.458  41.553  21.318  1.00 80.51  ? 171 LEU C CB  1 
ATOM   7559  C  CG  . LEU C 1 170 ? 41.984  42.601  20.334  1.00 81.74  ? 171 LEU C CG  1 
ATOM   7560  C  CD1 . LEU C 1 170 ? 43.152  42.052  19.525  1.00 82.25  ? 171 LEU C CD1 1 
ATOM   7561  C  CD2 . LEU C 1 170 ? 40.872  43.083  19.417  1.00 81.81  ? 171 LEU C CD2 1 
ATOM   7562  N  N   . GLU C 1 171 ? 42.536  42.683  24.008  1.00 82.62  ? 172 GLU C N   1 
ATOM   7563  C  CA  . GLU C 1 171 ? 43.150  43.750  24.799  1.00 86.11  ? 172 GLU C CA  1 
ATOM   7564  C  C   . GLU C 1 171 ? 44.441  43.272  25.468  1.00 87.91  ? 172 GLU C C   1 
ATOM   7565  O  O   . GLU C 1 171 ? 45.542  43.825  25.237  1.00 86.59  ? 172 GLU C O   1 
ATOM   7566  C  CB  . GLU C 1 171 ? 42.171  44.261  25.860  1.00 88.13  ? 172 GLU C CB  1 
ATOM   7567  C  CG  . GLU C 1 171 ? 40.950  44.972  25.297  1.00 89.49  ? 172 GLU C CG  1 
ATOM   7568  C  CD  . GLU C 1 171 ? 40.052  45.543  26.380  1.00 90.63  ? 172 GLU C CD  1 
ATOM   7569  O  OE1 . GLU C 1 171 ? 40.405  45.422  27.573  1.00 91.21  ? 172 GLU C OE1 1 
ATOM   7570  O  OE2 . GLU C 1 171 ? 38.995  46.114  26.040  1.00 91.54  ? 172 GLU C OE2 1 
ATOM   7571  N  N   . ARG C 1 172 ? 44.296  42.229  26.285  1.00 91.96  ? 173 ARG C N   1 
ATOM   7572  C  CA  . ARG C 1 172 ? 45.419  41.706  27.050  1.00 96.33  ? 173 ARG C CA  1 
ATOM   7573  C  C   . ARG C 1 172 ? 46.574  41.301  26.142  1.00 98.05  ? 173 ARG C C   1 
ATOM   7574  O  O   . ARG C 1 172 ? 47.700  41.714  26.374  1.00 100.14 ? 173 ARG C O   1 
ATOM   7575  C  CB  . ARG C 1 172 ? 44.985  40.525  27.921  1.00 97.23  ? 173 ARG C CB  1 
ATOM   7576  C  CG  . ARG C 1 172 ? 44.901  40.873  29.402  1.00 101.13 ? 173 ARG C CG  1 
ATOM   7577  C  CD  . ARG C 1 172 ? 44.511  39.677  30.253  1.00 103.99 ? 173 ARG C CD  1 
ATOM   7578  N  NE  . ARG C 1 172 ? 45.505  38.611  30.185  1.00 107.04 ? 173 ARG C NE  1 
ATOM   7579  C  CZ  . ARG C 1 172 ? 45.681  37.693  31.129  1.00 108.73 ? 173 ARG C CZ  1 
ATOM   7580  N  NH1 . ARG C 1 172 ? 46.610  36.759  30.983  1.00 109.83 ? 173 ARG C NH1 1 
ATOM   7581  N  NH2 . ARG C 1 172 ? 44.932  37.713  32.223  1.00 109.89 ? 173 ARG C NH2 1 
ATOM   7582  N  N   . LEU C 1 173 ? 46.294  40.521  25.100  1.00 96.40  ? 174 LEU C N   1 
ATOM   7583  C  CA  . LEU C 1 173 ? 47.332  40.114  24.151  1.00 95.04  ? 174 LEU C CA  1 
ATOM   7584  C  C   . LEU C 1 173 ? 47.992  41.299  23.470  1.00 96.60  ? 174 LEU C C   1 
ATOM   7585  O  O   . LEU C 1 173 ? 49.207  41.294  23.254  1.00 100.24 ? 174 LEU C O   1 
ATOM   7586  C  CB  . LEU C 1 173 ? 46.767  39.180  23.082  1.00 90.15  ? 174 LEU C CB  1 
ATOM   7587  C  CG  . LEU C 1 173 ? 46.822  37.686  23.386  1.00 85.26  ? 174 LEU C CG  1 
ATOM   7588  C  CD1 . LEU C 1 173 ? 46.262  36.894  22.220  1.00 83.06  ? 174 LEU C CD1 1 
ATOM   7589  C  CD2 . LEU C 1 173 ? 48.255  37.279  23.672  1.00 84.97  ? 174 LEU C CD2 1 
ATOM   7590  N  N   . PHE C 1 174 ? 47.185  42.300  23.121  1.00 97.85  ? 175 PHE C N   1 
ATOM   7591  C  CA  . PHE C 1 174 ? 47.699  43.510  22.496  1.00 96.66  ? 175 PHE C CA  1 
ATOM   7592  C  C   . PHE C 1 174 ? 48.753  44.078  23.427  1.00 97.82  ? 175 PHE C C   1 
ATOM   7593  O  O   . PHE C 1 174 ? 49.930  44.051  23.082  1.00 97.65  ? 175 PHE C O   1 
ATOM   7594  C  CB  . PHE C 1 174 ? 46.554  44.494  22.175  1.00 100.71 ? 175 PHE C CB  1 
ATOM   7595  C  CG  . PHE C 1 174 ? 46.989  45.913  21.872  1.00 106.19 ? 175 PHE C CG  1 
ATOM   7596  C  CD1 . PHE C 1 174 ? 47.331  46.271  20.578  1.00 108.43 ? 175 PHE C CD1 1 
ATOM   7597  C  CD2 . PHE C 1 174 ? 46.872  46.921  22.823  1.00 109.72 ? 175 PHE C CD2 1 
ATOM   7598  C  CE1 . PHE C 1 174 ? 47.691  47.572  20.265  1.00 111.28 ? 175 PHE C CE1 1 
ATOM   7599  C  CE2 . PHE C 1 174 ? 47.213  48.236  22.511  1.00 112.16 ? 175 PHE C CE2 1 
ATOM   7600  C  CZ  . PHE C 1 174 ? 47.620  48.558  21.227  1.00 113.12 ? 175 PHE C CZ  1 
ATOM   7601  N  N   . LYS C 1 175 ? 48.377  44.476  24.640  1.00 96.64  ? 176 LYS C N   1 
ATOM   7602  C  CA  . LYS C 1 175 ? 49.393  45.058  25.531  1.00 101.21 ? 176 LYS C CA  1 
ATOM   7603  C  C   . LYS C 1 175 ? 50.567  44.132  25.899  1.00 111.64 ? 176 LYS C C   1 
ATOM   7604  O  O   . LYS C 1 175 ? 51.686  44.608  26.089  1.00 110.61 ? 176 LYS C O   1 
ATOM   7605  C  CB  . LYS C 1 175 ? 48.755  45.576  26.818  1.00 95.72  ? 176 LYS C CB  1 
ATOM   7606  C  CG  . LYS C 1 175 ? 47.415  46.258  26.630  1.00 94.56  ? 176 LYS C CG  1 
ATOM   7607  C  CD  . LYS C 1 175 ? 46.706  46.421  27.957  1.00 93.64  ? 176 LYS C CD  1 
ATOM   7608  C  CE  . LYS C 1 175 ? 46.856  45.179  28.812  1.00 95.73  ? 176 LYS C CE  1 
ATOM   7609  N  NZ  . LYS C 1 175 ? 45.852  45.138  29.905  1.00 95.65  ? 176 LYS C NZ  1 
ATOM   7610  N  N   . GLN C 1 176 ? 50.328  42.826  25.984  1.00 125.62 ? 177 GLN C N   1 
ATOM   7611  C  CA  . GLN C 1 176 ? 51.394  41.868  26.300  1.00 130.10 ? 177 GLN C CA  1 
ATOM   7612  C  C   . GLN C 1 176 ? 52.503  41.861  25.249  1.00 127.17 ? 177 GLN C C   1 
ATOM   7613  O  O   . GLN C 1 176 ? 53.644  41.497  25.546  1.00 130.03 ? 177 GLN C O   1 
ATOM   7614  C  CB  . GLN C 1 176 ? 50.836  40.443  26.445  1.00 134.26 ? 177 GLN C CB  1 
ATOM   7615  C  CG  . GLN C 1 176 ? 49.924  40.200  27.645  1.00 140.50 ? 177 GLN C CG  1 
ATOM   7616  C  CD  . GLN C 1 176 ? 50.637  40.343  28.975  1.00 146.09 ? 177 GLN C CD  1 
ATOM   7617  O  OE1 . GLN C 1 176 ? 50.534  41.375  29.639  1.00 148.78 ? 177 GLN C OE1 1 
ATOM   7618  N  NE2 . GLN C 1 176 ? 51.360  39.303  29.374  1.00 147.31 ? 177 GLN C NE2 1 
ATOM   7619  N  N   . LEU C 1 177 ? 52.172  42.272  24.030  1.00 117.87 ? 178 LEU C N   1 
ATOM   7620  C  CA  . LEU C 1 177 ? 53.079  42.106  22.901  1.00 110.40 ? 178 LEU C CA  1 
ATOM   7621  C  C   . LEU C 1 177 ? 53.992  43.306  22.668  1.00 108.86 ? 178 LEU C C   1 
ATOM   7622  O  O   . LEU C 1 177 ? 55.010  43.190  21.984  1.00 108.20 ? 178 LEU C O   1 
ATOM   7623  C  CB  . LEU C 1 177 ? 52.271  41.809  21.627  1.00 104.91 ? 178 LEU C CB  1 
ATOM   7624  C  CG  . LEU C 1 177 ? 52.989  41.429  20.322  1.00 99.78  ? 178 LEU C CG  1 
ATOM   7625  C  CD1 . LEU C 1 177 ? 52.201  40.377  19.561  1.00 95.11  ? 178 LEU C CD1 1 
ATOM   7626  C  CD2 . LEU C 1 177 ? 53.209  42.652  19.440  1.00 98.91  ? 178 LEU C CD2 1 
ATOM   7627  N  N   . HIS C 1 178 ? 53.687  44.458  23.254  1.00 107.74 ? 179 HIS C N   1 
ATOM   7628  C  CA  . HIS C 1 178 ? 54.375  45.649  22.770  1.00 107.98 ? 179 HIS C CA  1 
ATOM   7629  C  C   . HIS C 1 178 ? 54.769  46.656  23.893  1.00 126.01 ? 179 HIS C C   1 
ATOM   7630  O  O   . HIS C 1 178 ? 54.135  46.711  24.928  1.00 123.80 ? 179 HIS C O   1 
ATOM   7631  C  CB  . HIS C 1 178 ? 53.501  46.302  21.687  1.00 108.88 ? 179 HIS C CB  1 
ATOM   7632  C  CG  . HIS C 1 178 ? 52.157  46.739  22.166  1.00 110.90 ? 179 HIS C CG  1 
ATOM   7633  N  ND1 . HIS C 1 178 ? 51.961  47.847  22.966  1.00 112.47 ? 179 HIS C ND1 1 
ATOM   7634  C  CD2 . HIS C 1 178 ? 50.926  46.280  21.862  1.00 110.19 ? 179 HIS C CD2 1 
ATOM   7635  C  CE1 . HIS C 1 178 ? 50.671  48.010  23.187  1.00 112.54 ? 179 HIS C CE1 1 
ATOM   7636  N  NE2 . HIS C 1 178 ? 50.018  47.069  22.525  1.00 111.29 ? 179 HIS C NE2 1 
ATOM   7637  N  N   . PRO C 1 179 ? 55.833  47.485  23.639  1.00 136.42 ? 180 PRO C N   1 
ATOM   7638  C  CA  . PRO C 1 179 ? 56.529  48.395  24.603  1.00 137.97 ? 180 PRO C CA  1 
ATOM   7639  C  C   . PRO C 1 179 ? 55.696  49.588  25.123  1.00 136.62 ? 180 PRO C C   1 
ATOM   7640  O  O   . PRO C 1 179 ? 55.911  50.049  26.197  1.00 139.77 ? 180 PRO C O   1 
ATOM   7641  C  CB  . PRO C 1 179 ? 57.693  48.939  23.762  1.00 142.28 ? 180 PRO C CB  1 
ATOM   7642  C  CG  . PRO C 1 179 ? 57.502  48.477  22.355  1.00 142.14 ? 180 PRO C CG  1 
ATOM   7643  C  CD  . PRO C 1 179 ? 56.230  47.787  22.231  1.00 139.87 ? 180 PRO C CD  1 
ATOM   7644  N  N   . GLN C 1 180 ? 54.805  50.085  24.285  1.00 129.57 ? 181 GLN C N   1 
ATOM   7645  C  CA  . GLN C 1 180 ? 54.280  51.426  24.456  1.00 127.36 ? 181 GLN C CA  1 
ATOM   7646  C  C   . GLN C 1 180 ? 53.137  51.543  25.475  1.00 125.19 ? 181 GLN C C   1 
ATOM   7647  O  O   . GLN C 1 180 ? 52.718  52.640  25.844  1.00 127.57 ? 181 GLN C O   1 
ATOM   7648  C  CB  . GLN C 1 180 ? 53.825  51.878  23.102  1.00 123.67 ? 181 GLN C CB  1 
ATOM   7649  C  CG  . GLN C 1 180 ? 54.805  51.358  22.048  1.00 119.94 ? 181 GLN C CG  1 
ATOM   7650  C  CD  . GLN C 1 180 ? 54.138  51.281  20.692  1.00 114.69 ? 181 GLN C CD  1 
ATOM   7651  O  OE1 . GLN C 1 180 ? 53.599  52.264  20.186  1.00 115.50 ? 181 GLN C OE1 1 
ATOM   7652  N  NE2 . GLN C 1 180 ? 54.100  50.079  20.132  1.00 110.62 ? 181 GLN C NE2 1 
ATOM   7653  N  N   . LEU C 1 181 ? 52.652  50.392  25.923  1.00 127.29 ? 182 LEU C N   1 
ATOM   7654  C  CA  . LEU C 1 181 ? 51.272  50.228  26.377  1.00 128.54 ? 182 LEU C CA  1 
ATOM   7655  C  C   . LEU C 1 181 ? 50.812  51.183  27.467  1.00 132.01 ? 182 LEU C C   1 
ATOM   7656  O  O   . LEU C 1 181 ? 51.430  51.326  28.528  1.00 135.55 ? 182 LEU C O   1 
ATOM   7657  C  CB  . LEU C 1 181 ? 51.046  48.787  26.851  1.00 129.71 ? 182 LEU C CB  1 
ATOM   7658  N  N   . LEU C 1 182 ? 49.698  51.831  27.163  1.00 128.74 ? 183 LEU C N   1 
ATOM   7659  C  CA  . LEU C 1 182 ? 48.947  52.624  28.113  1.00 128.45 ? 183 LEU C CA  1 
ATOM   7660  C  C   . LEU C 1 182 ? 47.490  52.283  27.877  1.00 125.11 ? 183 LEU C C   1 
ATOM   7661  O  O   . LEU C 1 182 ? 47.119  51.808  26.800  1.00 125.14 ? 183 LEU C O   1 
ATOM   7662  C  CB  . LEU C 1 182 ? 49.206  54.122  27.939  1.00 130.30 ? 183 LEU C CB  1 
ATOM   7663  N  N   . LEU C 1 183 ? 46.668  52.495  28.892  1.00 125.05 ? 184 LEU C N   1 
ATOM   7664  C  CA  . LEU C 1 183 ? 45.268  52.148  28.784  1.00 119.83 ? 184 LEU C CA  1 
ATOM   7665  C  C   . LEU C 1 183 ? 44.369  53.288  29.199  1.00 122.19 ? 184 LEU C C   1 
ATOM   7666  O  O   . LEU C 1 183 ? 44.714  54.074  30.084  1.00 125.06 ? 184 LEU C O   1 
ATOM   7667  C  CB  . LEU C 1 183 ? 44.947  50.915  29.626  1.00 117.78 ? 184 LEU C CB  1 
ATOM   7668  N  N   . PRO C 1 184 ? 43.207  53.374  28.536  1.00 116.19 ? 185 PRO C N   1 
ATOM   7669  C  CA  . PRO C 1 184 ? 42.042  54.190  28.863  1.00 115.23 ? 185 PRO C CA  1 
ATOM   7670  C  C   . PRO C 1 184 ? 41.871  54.386  30.370  1.00 113.28 ? 185 PRO C C   1 
ATOM   7671  O  O   . PRO C 1 184 ? 41.902  55.511  30.868  1.00 112.70 ? 185 PRO C O   1 
ATOM   7672  C  CB  . PRO C 1 184 ? 40.899  53.362  28.286  1.00 112.65 ? 185 PRO C CB  1 
ATOM   7673  C  CG  . PRO C 1 184 ? 41.498  52.745  27.045  1.00 112.68 ? 185 PRO C CG  1 
ATOM   7674  C  CD  . PRO C 1 184 ? 43.003  52.659  27.261  1.00 114.08 ? 185 PRO C CD  1 
ATOM   7675  N  N   . ALA C 1 197 ? 35.523  44.550  14.743  1.00 89.22  ? 198 ALA C N   1 
ATOM   7676  C  CA  . ALA C 1 197 ? 35.927  45.752  14.024  1.00 95.83  ? 198 ALA C CA  1 
ATOM   7677  C  C   . ALA C 1 197 ? 36.741  45.409  12.780  1.00 100.95 ? 198 ALA C C   1 
ATOM   7678  O  O   . ALA C 1 197 ? 36.193  45.274  11.685  1.00 102.87 ? 198 ALA C O   1 
ATOM   7679  C  CB  . ALA C 1 197 ? 36.722  46.674  14.939  1.00 95.47  ? 198 ALA C CB  1 
ATOM   7680  N  N   . LEU C 1 198 ? 38.051  45.270  12.958  1.00 106.75 ? 199 LEU C N   1 
ATOM   7681  C  CA  . LEU C 1 198 ? 38.965  45.009  11.850  1.00 108.47 ? 199 LEU C CA  1 
ATOM   7682  C  C   . LEU C 1 198 ? 39.193  43.509  11.644  1.00 109.18 ? 199 LEU C C   1 
ATOM   7683  O  O   . LEU C 1 198 ? 39.842  43.096  10.680  1.00 109.40 ? 199 LEU C O   1 
ATOM   7684  C  CB  . LEU C 1 198 ? 40.298  45.727  12.102  1.00 112.19 ? 199 LEU C CB  1 
ATOM   7685  C  CG  . LEU C 1 198 ? 41.417  45.686  11.056  1.00 114.62 ? 199 LEU C CG  1 
ATOM   7686  C  CD1 . LEU C 1 198 ? 40.923  46.192  9.711   1.00 116.40 ? 199 LEU C CD1 1 
ATOM   7687  C  CD2 . LEU C 1 198 ? 42.624  46.484  11.527  1.00 116.09 ? 199 LEU C CD2 1 
ATOM   7688  N  N   . ARG C 1 199 ? 38.627  42.702  12.539  1.00 103.58 ? 200 ARG C N   1 
ATOM   7689  C  CA  . ARG C 1 199 ? 38.863  41.258  12.564  1.00 99.11  ? 200 ARG C CA  1 
ATOM   7690  C  C   . ARG C 1 199 ? 40.360  40.938  12.615  1.00 94.67  ? 200 ARG C C   1 
ATOM   7691  O  O   . ARG C 1 199 ? 40.922  40.425  11.647  1.00 97.16  ? 200 ARG C O   1 
ATOM   7692  C  CB  . ARG C 1 199 ? 38.217  40.580  11.351  1.00 100.06 ? 200 ARG C CB  1 
ATOM   7693  N  N   . PRO C 1 200 ? 41.009  41.248  13.751  1.00 84.42  ? 201 PRO C N   1 
ATOM   7694  C  CA  . PRO C 1 200 ? 42.457  41.082  13.923  1.00 81.04  ? 201 PRO C CA  1 
ATOM   7695  C  C   . PRO C 1 200 ? 42.908  39.623  13.979  1.00 77.93  ? 201 PRO C C   1 
ATOM   7696  O  O   . PRO C 1 200 ? 44.046  39.323  13.617  1.00 75.07  ? 201 PRO C O   1 
ATOM   7697  C  CB  . PRO C 1 200 ? 42.727  41.778  15.258  1.00 81.94  ? 201 PRO C CB  1 
ATOM   7698  C  CG  . PRO C 1 200 ? 41.460  41.613  16.014  1.00 82.81  ? 201 PRO C CG  1 
ATOM   7699  C  CD  . PRO C 1 200 ? 40.361  41.708  14.993  1.00 82.74  ? 201 PRO C CD  1 
ATOM   7700  N  N   . PHE C 1 201 ? 42.028  38.733  14.428  1.00 75.84  ? 202 PHE C N   1 
ATOM   7701  C  CA  . PHE C 1 201 ? 42.362  37.318  14.543  1.00 78.27  ? 202 PHE C CA  1 
ATOM   7702  C  C   . PHE C 1 201 ? 42.028  36.570  13.258  1.00 84.19  ? 202 PHE C C   1 
ATOM   7703  O  O   . PHE C 1 201 ? 42.168  35.350  13.185  1.00 86.91  ? 202 PHE C O   1 
ATOM   7704  C  CB  . PHE C 1 201 ? 41.624  36.673  15.717  1.00 74.32  ? 202 PHE C CB  1 
ATOM   7705  C  CG  . PHE C 1 201 ? 41.873  37.339  17.038  1.00 74.14  ? 202 PHE C CG  1 
ATOM   7706  C  CD1 . PHE C 1 201 ? 42.951  36.967  17.824  1.00 74.83  ? 202 PHE C CD1 1 
ATOM   7707  C  CD2 . PHE C 1 201 ? 41.019  38.325  17.504  1.00 73.51  ? 202 PHE C CD2 1 
ATOM   7708  C  CE1 . PHE C 1 201 ? 43.179  37.573  19.044  1.00 74.84  ? 202 PHE C CE1 1 
ATOM   7709  C  CE2 . PHE C 1 201 ? 41.241  38.935  18.723  1.00 74.74  ? 202 PHE C CE2 1 
ATOM   7710  C  CZ  . PHE C 1 201 ? 42.323  38.558  19.495  1.00 75.75  ? 202 PHE C CZ  1 
ATOM   7711  N  N   . GLY C 1 202 ? 41.569  37.307  12.252  1.00 90.31  ? 203 GLY C N   1 
ATOM   7712  C  CA  . GLY C 1 202 ? 41.202  36.714  10.981  1.00 91.37  ? 203 GLY C CA  1 
ATOM   7713  C  C   . GLY C 1 202 ? 39.841  36.047  11.014  1.00 90.40  ? 203 GLY C C   1 
ATOM   7714  O  O   . GLY C 1 202 ? 38.923  36.517  11.687  1.00 96.89  ? 203 GLY C O   1 
ATOM   7715  N  N   . GLU C 1 203 ? 39.714  34.944  10.284  1.00 87.77  ? 204 GLU C N   1 
ATOM   7716  C  CA  . GLU C 1 203 ? 38.443  34.240  10.155  1.00 79.71  ? 204 GLU C CA  1 
ATOM   7717  C  C   . GLU C 1 203 ? 38.126  33.378  11.374  1.00 72.93  ? 204 GLU C C   1 
ATOM   7718  O  O   . GLU C 1 203 ? 36.962  33.092  11.653  1.00 70.34  ? 204 GLU C O   1 
ATOM   7719  C  CB  . GLU C 1 203 ? 38.454  33.366  8.898   1.00 82.56  ? 204 GLU C CB  1 
ATOM   7720  C  CG  . GLU C 1 203 ? 38.512  34.144  7.594   1.00 88.52  ? 204 GLU C CG  1 
ATOM   7721  C  CD  . GLU C 1 203 ? 39.474  33.529  6.594   1.00 94.26  ? 204 GLU C CD  1 
ATOM   7722  O  OE1 . GLU C 1 203 ? 40.561  33.078  7.011   1.00 95.54  ? 204 GLU C OE1 1 
ATOM   7723  O  OE2 . GLU C 1 203 ? 39.139  33.492  5.391   1.00 95.27  ? 204 GLU C OE2 1 
ATOM   7724  N  N   . ALA C 1 204 ? 39.170  32.982  12.095  1.00 70.04  ? 205 ALA C N   1 
ATOM   7725  C  CA  . ALA C 1 204 ? 39.073  32.000  13.180  1.00 66.49  ? 205 ALA C CA  1 
ATOM   7726  C  C   . ALA C 1 204 ? 37.983  32.233  14.247  1.00 63.94  ? 205 ALA C C   1 
ATOM   7727  O  O   . ALA C 1 204 ? 37.289  31.283  14.610  1.00 62.29  ? 205 ALA C O   1 
ATOM   7728  C  CB  . ALA C 1 204 ? 40.434  31.872  13.865  1.00 67.42  ? 205 ALA C CB  1 
ATOM   7729  N  N   . PRO C 1 205 ? 37.830  33.472  14.763  1.00 65.16  ? 206 PRO C N   1 
ATOM   7730  C  CA  . PRO C 1 205 ? 36.863  33.643  15.860  1.00 65.51  ? 206 PRO C CA  1 
ATOM   7731  C  C   . PRO C 1 205 ? 35.418  33.285  15.511  1.00 67.29  ? 206 PRO C C   1 
ATOM   7732  O  O   . PRO C 1 205 ? 34.835  32.388  16.123  1.00 65.01  ? 206 PRO C O   1 
ATOM   7733  C  CB  . PRO C 1 205 ? 36.962  35.139  16.181  1.00 61.67  ? 206 PRO C CB  1 
ATOM   7734  C  CG  . PRO C 1 205 ? 38.307  35.532  15.730  1.00 62.46  ? 206 PRO C CG  1 
ATOM   7735  C  CD  . PRO C 1 205 ? 38.562  34.725  14.497  1.00 61.05  ? 206 PRO C CD  1 
ATOM   7736  N  N   . ARG C 1 206 ? 34.852  33.991  14.540  1.00 68.47  ? 207 ARG C N   1 
ATOM   7737  C  CA  A ARG C 1 206 ? 33.463  33.802  14.138  0.49 72.64  ? 207 ARG C CA  1 
ATOM   7738  C  CA  B ARG C 1 206 ? 33.456  33.779  14.177  0.51 73.33  ? 207 ARG C CA  1 
ATOM   7739  C  C   . ARG C 1 206 ? 33.244  32.438  13.481  1.00 75.37  ? 207 ARG C C   1 
ATOM   7740  O  O   . ARG C 1 206 ? 32.142  31.891  13.505  1.00 75.95  ? 207 ARG C O   1 
ATOM   7741  C  CB  A ARG C 1 206 ? 33.045  34.933  13.194  0.49 72.30  ? 207 ARG C CB  1 
ATOM   7742  C  CB  B ARG C 1 206 ? 32.952  34.921  13.296  0.51 72.30  ? 207 ARG C CB  1 
ATOM   7743  C  CG  A ARG C 1 206 ? 31.648  34.821  12.611  0.49 70.38  ? 207 ARG C CG  1 
ATOM   7744  C  CG  B ARG C 1 206 ? 32.399  36.093  14.090  0.51 67.55  ? 207 ARG C CG  1 
ATOM   7745  C  CD  A ARG C 1 206 ? 31.222  36.145  12.002  0.49 72.19  ? 207 ARG C CD  1 
ATOM   7746  C  CD  B ARG C 1 206 ? 31.253  35.641  14.983  0.51 63.56  ? 207 ARG C CD  1 
ATOM   7747  N  NE  A ARG C 1 206 ? 30.248  35.978  10.929  0.49 73.19  ? 207 ARG C NE  1 
ATOM   7748  N  NE  B ARG C 1 206 ? 30.152  35.081  14.204  0.51 62.19  ? 207 ARG C NE  1 
ATOM   7749  C  CZ  A ARG C 1 206 ? 29.679  36.987  10.278  0.49 75.05  ? 207 ARG C CZ  1 
ATOM   7750  C  CZ  B ARG C 1 206 ? 29.078  34.503  14.732  0.51 59.30  ? 207 ARG C CZ  1 
ATOM   7751  N  NH1 A ARG C 1 206 ? 29.984  38.238  10.597  0.49 75.86  ? 207 ARG C NH1 1 
ATOM   7752  N  NH1 B ARG C 1 206 ? 28.955  34.402  16.048  0.51 59.45  ? 207 ARG C NH1 1 
ATOM   7753  N  NH2 A ARG C 1 206 ? 28.804  36.748  9.312   0.49 75.06  ? 207 ARG C NH2 1 
ATOM   7754  N  NH2 B ARG C 1 206 ? 28.127  34.024  13.943  0.51 59.17  ? 207 ARG C NH2 1 
ATOM   7755  N  N   . GLU C 1 207 ? 34.299  31.898  12.882  1.00 78.84  ? 208 GLU C N   1 
ATOM   7756  C  CA  . GLU C 1 207 ? 34.226  30.578  12.269  1.00 79.90  ? 208 GLU C CA  1 
ATOM   7757  C  C   . GLU C 1 207 ? 34.055  29.535  13.371  1.00 80.61  ? 208 GLU C C   1 
ATOM   7758  O  O   . GLU C 1 207 ? 33.182  28.655  13.300  1.00 80.96  ? 208 GLU C O   1 
ATOM   7759  C  CB  . GLU C 1 207 ? 35.478  30.313  11.433  1.00 86.03  ? 208 GLU C CB  1 
ATOM   7760  C  CG  . GLU C 1 207 ? 35.292  29.348  10.280  1.00 91.55  ? 208 GLU C CG  1 
ATOM   7761  C  CD  . GLU C 1 207 ? 36.388  29.490  9.241   1.00 99.26  ? 208 GLU C CD  1 
ATOM   7762  O  OE1 . GLU C 1 207 ? 37.570  29.588  9.628   1.00 102.05 ? 208 GLU C OE1 1 
ATOM   7763  O  OE2 . GLU C 1 207 ? 36.066  29.504  8.034   1.00 101.77 ? 208 GLU C OE2 1 
ATOM   7764  N  N   . LEU C 1 208 ? 34.889  29.664  14.401  1.00 75.80  ? 209 LEU C N   1 
ATOM   7765  C  CA  . LEU C 1 208 ? 34.753  28.880  15.621  1.00 73.48  ? 209 LEU C CA  1 
ATOM   7766  C  C   . LEU C 1 208 ? 33.360  29.050  16.212  1.00 71.43  ? 209 LEU C C   1 
ATOM   7767  O  O   . LEU C 1 208 ? 32.767  28.093  16.703  1.00 69.19  ? 209 LEU C O   1 
ATOM   7768  C  CB  . LEU C 1 208 ? 35.811  29.290  16.649  1.00 69.38  ? 209 LEU C CB  1 
ATOM   7769  C  CG  . LEU C 1 208 ? 35.580  28.827  18.091  1.00 67.70  ? 209 LEU C CG  1 
ATOM   7770  C  CD1 . LEU C 1 208 ? 35.790  27.326  18.222  1.00 63.37  ? 209 LEU C CD1 1 
ATOM   7771  C  CD2 . LEU C 1 208 ? 36.472  29.589  19.063  1.00 65.59  ? 209 LEU C CD2 1 
ATOM   7772  N  N   . ARG C 1 209 ? 32.842  30.274  16.152  1.00 71.48  ? 210 ARG C N   1 
ATOM   7773  C  CA  . ARG C 1 209 ? 31.514  30.572  16.678  1.00 68.51  ? 210 ARG C CA  1 
ATOM   7774  C  C   . ARG C 1 209 ? 30.430  29.781  15.950  1.00 67.64  ? 210 ARG C C   1 
ATOM   7775  O  O   . ARG C 1 209 ? 29.575  29.162  16.583  1.00 66.69  ? 210 ARG C O   1 
ATOM   7776  C  CB  . ARG C 1 209 ? 31.224  32.070  16.581  1.00 65.11  ? 210 ARG C CB  1 
ATOM   7777  N  N   . LEU C 1 210 ? 30.476  29.804  14.622  1.00 65.04  ? 211 LEU C N   1 
ATOM   7778  C  CA  . LEU C 1 210 ? 29.513  29.072  13.806  1.00 65.23  ? 211 LEU C CA  1 
ATOM   7779  C  C   . LEU C 1 210 ? 29.606  27.571  14.051  1.00 61.76  ? 211 LEU C C   1 
ATOM   7780  O  O   . LEU C 1 210 ? 28.607  26.921  14.393  1.00 65.95  ? 211 LEU C O   1 
ATOM   7781  C  CB  . LEU C 1 210 ? 29.732  29.372  12.321  1.00 67.54  ? 211 LEU C CB  1 
ATOM   7782  C  CG  . LEU C 1 210 ? 29.509  30.817  11.872  1.00 73.01  ? 211 LEU C CG  1 
ATOM   7783  C  CD1 . LEU C 1 210 ? 29.880  30.988  10.407  1.00 73.18  ? 211 LEU C CD1 1 
ATOM   7784  C  CD2 . LEU C 1 210 ? 28.067  31.232  12.112  1.00 71.06  ? 211 LEU C CD2 1 
ATOM   7785  N  N   . ARG C 1 211 ? 30.811  27.029  13.882  1.00 58.66  ? 212 ARG C N   1 
ATOM   7786  C  CA  . ARG C 1 211 ? 31.022  25.593  14.039  1.00 57.89  ? 212 ARG C CA  1 
ATOM   7787  C  C   . ARG C 1 211 ? 30.598  25.100  15.421  1.00 53.96  ? 212 ARG C C   1 
ATOM   7788  O  O   . ARG C 1 211 ? 29.963  24.053  15.542  1.00 59.29  ? 212 ARG C O   1 
ATOM   7789  C  CB  . ARG C 1 211 ? 32.486  25.235  13.779  1.00 57.47  ? 212 ARG C CB  1 
ATOM   7790  C  CG  . ARG C 1 211 ? 32.886  25.326  12.316  1.00 60.61  ? 212 ARG C CG  1 
ATOM   7791  C  CD  . ARG C 1 211 ? 34.296  24.805  12.088  1.00 64.74  ? 212 ARG C CD  1 
ATOM   7792  N  NE  . ARG C 1 211 ? 34.663  24.850  10.676  1.00 66.38  ? 212 ARG C NE  1 
ATOM   7793  C  CZ  . ARG C 1 211 ? 34.390  23.886  9.802   1.00 69.08  ? 212 ARG C CZ  1 
ATOM   7794  N  NH1 . ARG C 1 211 ? 33.747  22.795  10.194  1.00 67.80  ? 212 ARG C NH1 1 
ATOM   7795  N  NH2 . ARG C 1 211 ? 34.759  24.014  8.536   1.00 69.62  ? 212 ARG C NH2 1 
ATOM   7796  N  N   . ALA C 1 212 ? 30.940  25.859  16.457  1.00 49.62  ? 213 ALA C N   1 
ATOM   7797  C  CA  . ALA C 1 212 ? 30.567  25.495  17.820  1.00 61.34  ? 213 ALA C CA  1 
ATOM   7798  C  C   . ALA C 1 212 ? 29.057  25.563  18.010  1.00 56.26  ? 213 ALA C C   1 
ATOM   7799  O  O   . ALA C 1 212 ? 28.451  24.635  18.550  1.00 60.23  ? 213 ALA C O   1 
ATOM   7800  C  CB  . ALA C 1 212 ? 31.266  26.394  18.827  1.00 49.59  ? 213 ALA C CB  1 
ATOM   7801  N  N   . THR C 1 213 ? 28.460  26.665  17.560  1.00 58.07  ? 214 THR C N   1 
ATOM   7802  C  CA  . THR C 1 213 ? 27.019  26.869  17.671  1.00 56.19  ? 214 THR C CA  1 
ATOM   7803  C  C   . THR C 1 213 ? 26.252  25.710  17.047  1.00 58.29  ? 214 THR C C   1 
ATOM   7804  O  O   . THR C 1 213 ? 25.273  25.226  17.615  1.00 58.09  ? 214 THR C O   1 
ATOM   7805  C  CB  . THR C 1 213 ? 26.575  28.183  16.999  1.00 54.24  ? 214 THR C CB  1 
ATOM   7806  O  OG1 . THR C 1 213 ? 27.308  29.279  17.558  1.00 55.88  ? 214 THR C OG1 1 
ATOM   7807  C  CG2 . THR C 1 213 ? 25.085  28.417  17.205  1.00 56.49  ? 214 THR C CG2 1 
ATOM   7808  N  N   . ARG C 1 214 ? 26.707  25.259  15.882  1.00 58.61  ? 215 ARG C N   1 
ATOM   7809  C  CA  . ARG C 1 214 ? 26.074  24.125  15.216  1.00 57.87  ? 215 ARG C CA  1 
ATOM   7810  C  C   . ARG C 1 214 ? 26.335  22.798  15.940  1.00 52.61  ? 215 ARG C C   1 
ATOM   7811  O  O   . ARG C 1 214 ? 25.406  22.144  16.440  1.00 53.17  ? 215 ARG C O   1 
ATOM   7812  C  CB  . ARG C 1 214 ? 26.562  24.031  13.768  1.00 48.12  ? 215 ARG C CB  1 
ATOM   7813  C  CG  . ARG C 1 214 ? 26.135  22.764  13.050  1.00 51.23  ? 215 ARG C CG  1 
ATOM   7814  C  CD  . ARG C 1 214 ? 26.655  22.726  11.620  1.00 51.12  ? 215 ARG C CD  1 
ATOM   7815  N  NE  . ARG C 1 214 ? 28.061  23.113  11.521  1.00 53.78  ? 215 ARG C NE  1 
ATOM   7816  C  CZ  . ARG C 1 214 ? 29.081  22.334  11.868  1.00 51.83  ? 215 ARG C CZ  1 
ATOM   7817  N  NH1 . ARG C 1 214 ? 28.861  21.122  12.358  1.00 47.98  ? 215 ARG C NH1 1 
ATOM   7818  N  NH2 . ARG C 1 214 ? 30.326  22.774  11.736  1.00 49.58  ? 215 ARG C NH2 1 
ATOM   7819  N  N   . ALA C 1 215 ? 27.609  22.421  16.003  1.00 49.79  ? 216 ALA C N   1 
ATOM   7820  C  CA  . ALA C 1 215 ? 28.014  21.100  16.475  1.00 49.09  ? 216 ALA C CA  1 
ATOM   7821  C  C   . ALA C 1 215 ? 27.625  20.819  17.923  1.00 52.26  ? 216 ALA C C   1 
ATOM   7822  O  O   . ALA C 1 215 ? 27.233  19.700  18.253  1.00 54.80  ? 216 ALA C O   1 
ATOM   7823  C  CB  . ALA C 1 215 ? 29.516  20.927  16.300  1.00 50.82  ? 216 ALA C CB  1 
ATOM   7824  N  N   . PHE C 1 216 ? 27.736  21.823  18.787  1.00 52.79  ? 217 PHE C N   1 
ATOM   7825  C  CA  . PHE C 1 216 ? 27.467  21.602  20.205  1.00 53.85  ? 217 PHE C CA  1 
ATOM   7826  C  C   . PHE C 1 216 ? 25.977  21.415  20.485  1.00 51.15  ? 217 PHE C C   1 
ATOM   7827  O  O   . PHE C 1 216 ? 25.595  20.551  21.279  1.00 52.22  ? 217 PHE C O   1 
ATOM   7828  C  CB  . PHE C 1 216 ? 28.029  22.752  21.042  1.00 52.02  ? 217 PHE C CB  1 
ATOM   7829  C  CG  . PHE C 1 216 ? 29.494  22.612  21.347  1.00 50.46  ? 217 PHE C CG  1 
ATOM   7830  C  CD1 . PHE C 1 216 ? 29.917  21.932  22.477  1.00 47.98  ? 217 PHE C CD1 1 
ATOM   7831  C  CD2 . PHE C 1 216 ? 30.447  23.149  20.498  1.00 54.40  ? 217 PHE C CD2 1 
ATOM   7832  C  CE1 . PHE C 1 216 ? 31.262  21.797  22.760  1.00 47.10  ? 217 PHE C CE1 1 
ATOM   7833  C  CE2 . PHE C 1 216 ? 31.796  23.017  20.775  1.00 47.89  ? 217 PHE C CE2 1 
ATOM   7834  C  CZ  . PHE C 1 216 ? 32.204  22.340  21.907  1.00 49.04  ? 217 PHE C CZ  1 
ATOM   7835  N  N   . VAL C 1 217 ? 25.135  22.209  19.830  1.00 51.03  ? 218 VAL C N   1 
ATOM   7836  C  CA  . VAL C 1 217 ? 23.697  22.053  20.005  1.00 50.19  ? 218 VAL C CA  1 
ATOM   7837  C  C   . VAL C 1 217 ? 23.246  20.758  19.331  1.00 49.67  ? 218 VAL C C   1 
ATOM   7838  O  O   . VAL C 1 217 ? 22.310  20.104  19.798  1.00 46.98  ? 218 VAL C O   1 
ATOM   7839  C  CB  . VAL C 1 217 ? 22.900  23.267  19.453  1.00 63.02  ? 218 VAL C CB  1 
ATOM   7840  C  CG1 . VAL C 1 217 ? 22.817  23.242  17.934  1.00 62.34  ? 218 VAL C CG1 1 
ATOM   7841  C  CG2 . VAL C 1 217 ? 21.503  23.297  20.055  1.00 63.61  ? 218 VAL C CG2 1 
ATOM   7842  N  N   . ALA C 1 218 ? 23.933  20.370  18.257  1.00 48.52  ? 219 ALA C N   1 
ATOM   7843  C  CA  . ALA C 1 218 ? 23.635  19.103  17.596  1.00 50.54  ? 219 ALA C CA  1 
ATOM   7844  C  C   . ALA C 1 218 ? 23.911  17.929  18.535  1.00 50.42  ? 219 ALA C C   1 
ATOM   7845  O  O   . ALA C 1 218 ? 23.058  17.057  18.734  1.00 42.54  ? 219 ALA C O   1 
ATOM   7846  C  CB  . ALA C 1 218 ? 24.446  18.966  16.320  1.00 44.21  ? 219 ALA C CB  1 
ATOM   7847  N  N   . ALA C 1 219 ? 25.108  17.926  19.115  1.00 43.36  ? 220 ALA C N   1 
ATOM   7848  C  CA  . ALA C 1 219 ? 25.532  16.877  20.035  1.00 45.56  ? 220 ALA C CA  1 
ATOM   7849  C  C   . ALA C 1 219 ? 24.627  16.805  21.260  1.00 44.99  ? 220 ALA C C   1 
ATOM   7850  O  O   . ALA C 1 219 ? 24.146  15.729  21.632  1.00 42.06  ? 220 ALA C O   1 
ATOM   7851  C  CB  . ALA C 1 219 ? 26.975  17.105  20.459  1.00 43.51  ? 220 ALA C CB  1 
ATOM   7852  N  N   . ARG C 1 220 ? 24.405  17.960  21.882  1.00 49.57  ? 221 ARG C N   1 
ATOM   7853  C  CA  . ARG C 1 220 ? 23.558  18.044  23.066  1.00 48.08  ? 221 ARG C CA  1 
ATOM   7854  C  C   . ARG C 1 220 ? 22.153  17.520  22.780  1.00 44.23  ? 221 ARG C C   1 
ATOM   7855  O  O   . ARG C 1 220 ? 21.627  16.679  23.519  1.00 44.60  ? 221 ARG C O   1 
ATOM   7856  C  CB  . ARG C 1 220 ? 23.488  19.486  23.566  1.00 54.55  ? 221 ARG C CB  1 
ATOM   7857  C  CG  . ARG C 1 220 ? 22.713  19.656  24.858  1.00 58.65  ? 221 ARG C CG  1 
ATOM   7858  C  CD  . ARG C 1 220 ? 22.636  21.118  25.252  1.00 59.07  ? 221 ARG C CD  1 
ATOM   7859  N  NE  . ARG C 1 220 ? 21.798  21.882  24.334  1.00 61.12  ? 221 ARG C NE  1 
ATOM   7860  C  CZ  . ARG C 1 220 ? 21.691  23.206  24.349  1.00 67.01  ? 221 ARG C CZ  1 
ATOM   7861  N  NH1 . ARG C 1 220 ? 22.376  23.916  25.235  1.00 67.77  ? 221 ARG C NH1 1 
ATOM   7862  N  NH2 . ARG C 1 220 ? 20.903  23.819  23.478  1.00 67.58  ? 221 ARG C NH2 1 
ATOM   7863  N  N   . SER C 1 221 ? 21.558  18.018  21.699  1.00 47.56  ? 222 SER C N   1 
ATOM   7864  C  CA  . SER C 1 221 ? 20.215  17.604  21.308  1.00 49.57  ? 222 SER C CA  1 
ATOM   7865  C  C   . SER C 1 221 ? 20.158  16.104  21.033  1.00 47.23  ? 222 SER C C   1 
ATOM   7866  O  O   . SER C 1 221 ? 19.167  15.443  21.354  1.00 47.88  ? 222 SER C O   1 
ATOM   7867  C  CB  . SER C 1 221 ? 19.751  18.382  20.075  1.00 50.85  ? 222 SER C CB  1 
ATOM   7868  O  OG  . SER C 1 221 ? 19.747  19.777  20.324  1.00 52.59  ? 222 SER C OG  1 
ATOM   7869  N  N   . PHE C 1 222 ? 21.225  15.569  20.445  1.00 45.56  ? 223 PHE C N   1 
ATOM   7870  C  CA  . PHE C 1 222 ? 21.292  14.139  20.167  1.00 48.33  ? 223 PHE C CA  1 
ATOM   7871  C  C   . PHE C 1 222 ? 21.302  13.325  21.459  1.00 46.96  ? 223 PHE C C   1 
ATOM   7872  O  O   . PHE C 1 222 ? 20.519  12.381  21.620  1.00 49.20  ? 223 PHE C O   1 
ATOM   7873  C  CB  . PHE C 1 222 ? 22.529  13.811  19.327  1.00 49.18  ? 223 PHE C CB  1 
ATOM   7874  C  CG  . PHE C 1 222 ? 22.577  12.385  18.853  1.00 49.96  ? 223 PHE C CG  1 
ATOM   7875  C  CD1 . PHE C 1 222 ? 21.818  11.978  17.769  1.00 40.72  ? 223 PHE C CD1 1 
ATOM   7876  C  CD2 . PHE C 1 222 ? 23.386  11.454  19.484  1.00 49.85  ? 223 PHE C CD2 1 
ATOM   7877  C  CE1 . PHE C 1 222 ? 21.857  10.670  17.329  1.00 40.52  ? 223 PHE C CE1 1 
ATOM   7878  C  CE2 . PHE C 1 222 ? 23.432  10.143  19.044  1.00 46.43  ? 223 PHE C CE2 1 
ATOM   7879  C  CZ  . PHE C 1 222 ? 22.667  9.752   17.965  1.00 47.10  ? 223 PHE C CZ  1 
ATOM   7880  N  N   . VAL C 1 223 ? 22.188  13.700  22.379  1.00 48.66  ? 224 VAL C N   1 
ATOM   7881  C  CA  . VAL C 1 223 ? 22.309  12.998  23.656  1.00 50.55  ? 224 VAL C CA  1 
ATOM   7882  C  C   . VAL C 1 223 ? 20.998  13.040  24.444  1.00 47.46  ? 224 VAL C C   1 
ATOM   7883  O  O   . VAL C 1 223 ? 20.528  12.011  24.960  1.00 47.22  ? 224 VAL C O   1 
ATOM   7884  C  CB  . VAL C 1 223 ? 23.447  13.589  24.512  1.00 48.58  ? 224 VAL C CB  1 
ATOM   7885  C  CG1 . VAL C 1 223 ? 23.437  12.991  25.908  1.00 47.80  ? 224 VAL C CG1 1 
ATOM   7886  C  CG2 . VAL C 1 223 ? 24.792  13.351  23.836  1.00 48.03  ? 224 VAL C CG2 1 
ATOM   7887  N  N   . GLN C 1 224 ? 20.398  14.226  24.524  1.00 54.36  ? 225 GLN C N   1 
ATOM   7888  C  CA  . GLN C 1 224 ? 19.124  14.359  25.223  1.00 57.11  ? 225 GLN C CA  1 
ATOM   7889  C  C   . GLN C 1 224 ? 18.027  13.568  24.521  1.00 53.74  ? 225 GLN C C   1 
ATOM   7890  O  O   . GLN C 1 224 ? 17.109  13.067  25.168  1.00 53.34  ? 225 GLN C O   1 
ATOM   7891  C  CB  . GLN C 1 224 ? 18.708  15.825  25.350  1.00 67.66  ? 225 GLN C CB  1 
ATOM   7892  C  CG  . GLN C 1 224 ? 18.364  16.214  26.780  1.00 77.02  ? 225 GLN C CG  1 
ATOM   7893  C  CD  . GLN C 1 224 ? 17.501  17.457  26.874  1.00 84.55  ? 225 GLN C CD  1 
ATOM   7894  O  OE1 . GLN C 1 224 ? 17.889  18.533  26.421  1.00 87.80  ? 225 GLN C OE1 1 
ATOM   7895  N  NE2 . GLN C 1 224 ? 16.326  17.316  27.479  1.00 86.12  ? 225 GLN C NE2 1 
ATOM   7896  N  N   . GLY C 1 225 ? 18.132  13.451  23.201  1.00 48.35  ? 226 GLY C N   1 
ATOM   7897  C  CA  . GLY C 1 225 ? 17.206  12.636  22.433  1.00 39.67  ? 226 GLY C CA  1 
ATOM   7898  C  C   . GLY C 1 225 ? 17.294  11.177  22.837  1.00 46.75  ? 226 GLY C C   1 
ATOM   7899  O  O   . GLY C 1 225 ? 16.272  10.526  23.099  1.00 46.84  ? 226 GLY C O   1 
ATOM   7900  N  N   . LEU C 1 226 ? 18.522  10.665  22.889  1.00 48.03  ? 227 LEU C N   1 
ATOM   7901  C  CA  . LEU C 1 226 ? 18.773  9.310   23.372  1.00 44.02  ? 227 LEU C CA  1 
ATOM   7902  C  C   . LEU C 1 226 ? 18.181  9.110   24.766  1.00 48.01  ? 227 LEU C C   1 
ATOM   7903  O  O   . LEU C 1 226 ? 17.518  8.099   25.038  1.00 47.33  ? 227 LEU C O   1 
ATOM   7904  C  CB  . LEU C 1 226 ? 20.276  9.017   23.390  1.00 45.98  ? 227 LEU C CB  1 
ATOM   7905  C  CG  . LEU C 1 226 ? 20.959  8.823   22.036  1.00 39.26  ? 227 LEU C CG  1 
ATOM   7906  C  CD1 . LEU C 1 226 ? 22.468  8.877   22.185  1.00 41.89  ? 227 LEU C CD1 1 
ATOM   7907  C  CD2 . LEU C 1 226 ? 20.534  7.500   21.419  1.00 41.85  ? 227 LEU C CD2 1 
ATOM   7908  N  N   . GLY C 1 227 ? 18.415  10.087  25.640  1.00 52.41  ? 228 GLY C N   1 
ATOM   7909  C  CA  . GLY C 1 227 ? 17.865  10.045  26.986  1.00 51.77  ? 228 GLY C CA  1 
ATOM   7910  C  C   . GLY C 1 227 ? 16.348  9.941   27.017  1.00 48.60  ? 228 GLY C C   1 
ATOM   7911  O  O   . GLY C 1 227 ? 15.783  9.120   27.750  1.00 47.23  ? 228 GLY C O   1 
ATOM   7912  N  N   . VAL C 1 228 ? 15.690  10.774  26.214  1.00 46.67  ? 229 VAL C N   1 
ATOM   7913  C  CA  . VAL C 1 228 ? 14.233  10.790  26.136  1.00 46.17  ? 229 VAL C CA  1 
ATOM   7914  C  C   . VAL C 1 228 ? 13.695  9.460   25.629  1.00 48.35  ? 229 VAL C C   1 
ATOM   7915  O  O   . VAL C 1 228 ? 12.771  8.902   26.215  1.00 44.67  ? 229 VAL C O   1 
ATOM   7916  C  CB  . VAL C 1 228 ? 13.722  11.923  25.223  1.00 45.67  ? 229 VAL C CB  1 
ATOM   7917  C  CG1 . VAL C 1 228 ? 12.234  11.751  24.934  1.00 43.95  ? 229 VAL C CG1 1 
ATOM   7918  C  CG2 . VAL C 1 228 ? 13.987  13.276  25.862  1.00 40.23  ? 229 VAL C CG2 1 
ATOM   7919  N  N   . ALA C 1 229 ? 14.279  8.951   24.547  1.00 49.30  ? 230 ALA C N   1 
ATOM   7920  C  CA  . ALA C 1 229 ? 13.876  7.650   24.021  1.00 42.50  ? 230 ALA C CA  1 
ATOM   7921  C  C   . ALA C 1 229 ? 13.999  6.568   25.094  1.00 48.89  ? 230 ALA C C   1 
ATOM   7922  O  O   . ALA C 1 229 ? 13.070  5.777   25.307  1.00 53.56  ? 230 ALA C O   1 
ATOM   7923  C  CB  . ALA C 1 229 ? 14.708  7.287   22.803  1.00 39.09  ? 230 ALA C CB  1 
ATOM   7924  N  N   . SER C 1 230 ? 15.142  6.555   25.776  1.00 51.39  ? 231 SER C N   1 
ATOM   7925  C  CA  . SER C 1 230 ? 15.390  5.592   26.847  1.00 53.57  ? 231 SER C CA  1 
ATOM   7926  C  C   . SER C 1 230 ? 14.312  5.652   27.934  1.00 50.88  ? 231 SER C C   1 
ATOM   7927  O  O   . SER C 1 230 ? 13.701  4.630   28.285  1.00 51.21  ? 231 SER C O   1 
ATOM   7928  C  CB  . SER C 1 230 ? 16.772  5.834   27.459  1.00 55.55  ? 231 SER C CB  1 
ATOM   7929  O  OG  . SER C 1 230 ? 17.066  4.880   28.463  1.00 58.73  ? 231 SER C OG  1 
ATOM   7930  N  N   . ASP C 1 231 ? 14.076  6.856   28.452  1.00 56.07  ? 232 ASP C N   1 
ATOM   7931  C  CA  . ASP C 1 231 ? 13.068  7.065   29.490  1.00 60.24  ? 232 ASP C CA  1 
ATOM   7932  C  C   . ASP C 1 231 ? 11.682  6.609   29.041  1.00 55.32  ? 232 ASP C C   1 
ATOM   7933  O  O   . ASP C 1 231 ? 10.974  5.918   29.782  1.00 53.54  ? 232 ASP C O   1 
ATOM   7934  C  CB  . ASP C 1 231 ? 13.019  8.538   29.902  1.00 71.28  ? 232 ASP C CB  1 
ATOM   7935  C  CG  . ASP C 1 231 ? 14.142  8.917   30.846  1.00 82.17  ? 232 ASP C CG  1 
ATOM   7936  O  OD1 . ASP C 1 231 ? 14.649  8.023   31.556  1.00 85.46  ? 232 ASP C OD1 1 
ATOM   7937  O  OD2 . ASP C 1 231 ? 14.513  10.109  30.886  1.00 88.25  ? 232 ASP C OD2 1 
ATOM   7938  N  N   . VAL C 1 232 ? 11.306  6.999   27.825  1.00 51.08  ? 233 VAL C N   1 
ATOM   7939  C  CA  . VAL C 1 232 ? 10.015  6.627   27.260  1.00 47.26  ? 233 VAL C CA  1 
ATOM   7940  C  C   . VAL C 1 232 ? 9.857   5.117   27.213  1.00 44.71  ? 233 VAL C C   1 
ATOM   7941  O  O   . VAL C 1 232 ? 8.862   4.583   27.699  1.00 44.57  ? 233 VAL C O   1 
ATOM   7942  C  CB  . VAL C 1 232 ? 9.821   7.197   25.840  1.00 43.64  ? 233 VAL C CB  1 
ATOM   7943  C  CG1 . VAL C 1 232 ? 8.623   6.542   25.163  1.00 40.68  ? 233 VAL C CG1 1 
ATOM   7944  C  CG2 . VAL C 1 232 ? 9.638   8.705   25.894  1.00 41.84  ? 233 VAL C CG2 1 
ATOM   7945  N  N   . VAL C 1 233 ? 10.841  4.428   26.643  1.00 44.86  ? 234 VAL C N   1 
ATOM   7946  C  CA  . VAL C 1 233 ? 10.776  2.971   26.574  1.00 50.98  ? 234 VAL C CA  1 
ATOM   7947  C  C   . VAL C 1 233 ? 10.649  2.358   27.969  1.00 52.29  ? 234 VAL C C   1 
ATOM   7948  O  O   . VAL C 1 233 ? 9.832   1.454   28.188  1.00 51.32  ? 234 VAL C O   1 
ATOM   7949  C  CB  . VAL C 1 233 ? 12.007  2.376   25.865  1.00 45.89  ? 234 VAL C CB  1 
ATOM   7950  C  CG1 . VAL C 1 233 ? 11.970  0.858   25.923  1.00 37.43  ? 234 VAL C CG1 1 
ATOM   7951  C  CG2 . VAL C 1 233 ? 12.061  2.847   24.421  1.00 47.16  ? 234 VAL C CG2 1 
ATOM   7952  N  N   . ARG C 1 234 ? 11.437  2.870   28.914  1.00 55.94  ? 235 ARG C N   1 
ATOM   7953  C  CA  . ARG C 1 234 ? 11.442  2.318   30.268  1.00 56.01  ? 235 ARG C CA  1 
ATOM   7954  C  C   . ARG C 1 234 ? 10.097  2.484   30.978  1.00 52.32  ? 235 ARG C C   1 
ATOM   7955  O  O   . ARG C 1 234 ? 9.620   1.560   31.638  1.00 48.76  ? 235 ARG C O   1 
ATOM   7956  C  CB  . ARG C 1 234 ? 12.559  2.955   31.103  1.00 63.54  ? 235 ARG C CB  1 
ATOM   7957  C  CG  . ARG C 1 234 ? 12.142  3.422   32.493  1.00 72.89  ? 235 ARG C CG  1 
ATOM   7958  C  CD  . ARG C 1 234 ? 13.221  4.269   33.140  1.00 81.54  ? 235 ARG C CD  1 
ATOM   7959  N  NE  . ARG C 1 234 ? 12.733  4.911   34.354  1.00 90.06  ? 235 ARG C NE  1 
ATOM   7960  C  CZ  . ARG C 1 234 ? 12.179  6.117   34.375  1.00 97.45  ? 235 ARG C CZ  1 
ATOM   7961  N  NH1 . ARG C 1 234 ? 12.056  6.804   33.248  1.00 98.97  ? 235 ARG C NH1 1 
ATOM   7962  N  NH2 . ARG C 1 234 ? 11.753  6.641   35.517  1.00 100.05 ? 235 ARG C NH2 1 
ATOM   7963  N  N   . LYS C 1 235 ? 9.476   3.650   30.825  1.00 49.11  ? 236 LYS C N   1 
ATOM   7964  C  CA  . LYS C 1 235 ? 8.202   3.915   31.489  1.00 53.14  ? 236 LYS C CA  1 
ATOM   7965  C  C   . LYS C 1 235 ? 7.047   3.189   30.807  1.00 51.46  ? 236 LYS C C   1 
ATOM   7966  O  O   . LYS C 1 235 ? 6.146   2.679   31.474  1.00 46.64  ? 236 LYS C O   1 
ATOM   7967  C  CB  . LYS C 1 235 ? 7.918   5.419   31.540  1.00 55.51  ? 236 LYS C CB  1 
ATOM   7968  C  CG  . LYS C 1 235 ? 8.715   6.157   32.604  1.00 62.97  ? 236 LYS C CG  1 
ATOM   7969  C  CD  . LYS C 1 235 ? 8.992   7.596   32.205  1.00 65.41  ? 236 LYS C CD  1 
ATOM   7970  C  CE  . LYS C 1 235 ? 8.291   8.573   33.137  1.00 71.01  ? 236 LYS C CE  1 
ATOM   7971  N  NZ  . LYS C 1 235 ? 9.219   9.640   33.602  1.00 73.02  ? 236 LYS C NZ  1 
ATOM   7972  N  N   . VAL C 1 236 ? 7.077   3.146   29.479  1.00 53.21  ? 237 VAL C N   1 
ATOM   7973  C  CA  . VAL C 1 236 ? 6.075   2.415   28.711  1.00 51.01  ? 237 VAL C CA  1 
ATOM   7974  C  C   . VAL C 1 236 ? 6.142   0.924   29.043  1.00 56.96  ? 237 VAL C C   1 
ATOM   7975  O  O   . VAL C 1 236 ? 5.119   0.234   29.061  1.00 56.13  ? 237 VAL C O   1 
ATOM   7976  C  CB  . VAL C 1 236 ? 6.262   2.638   27.190  1.00 37.71  ? 237 VAL C CB  1 
ATOM   7977  C  CG1 . VAL C 1 236 ? 5.476   1.617   26.380  1.00 41.21  ? 237 VAL C CG1 1 
ATOM   7978  C  CG2 . VAL C 1 236 ? 5.852   4.054   26.809  1.00 42.24  ? 237 VAL C CG2 1 
ATOM   7979  N  N   . ALA C 1 237 ? 7.347   0.441   29.336  1.00 55.65  ? 238 ALA C N   1 
ATOM   7980  C  CA  . ALA C 1 237 ? 7.556   -0.960  29.702  1.00 57.80  ? 238 ALA C CA  1 
ATOM   7981  C  C   . ALA C 1 237 ? 6.681   -1.414  30.874  1.00 63.50  ? 238 ALA C C   1 
ATOM   7982  O  O   . ALA C 1 237 ? 6.264   -2.571  30.929  1.00 65.78  ? 238 ALA C O   1 
ATOM   7983  C  CB  . ALA C 1 237 ? 9.017   -1.197  30.034  1.00 57.15  ? 238 ALA C CB  1 
ATOM   7984  N  N   . GLN C 1 238 ? 6.407   -0.504  31.804  1.00 67.28  ? 239 GLN C N   1 
ATOM   7985  C  CA  . GLN C 1 238 ? 5.664   -0.850  33.014  1.00 70.19  ? 239 GLN C CA  1 
ATOM   7986  C  C   . GLN C 1 238 ? 4.152   -0.673  32.872  1.00 66.77  ? 239 GLN C C   1 
ATOM   7987  O  O   . GLN C 1 238 ? 3.433   -0.620  33.870  1.00 66.59  ? 239 GLN C O   1 
ATOM   7988  C  CB  . GLN C 1 238 ? 6.167   -0.021  34.199  1.00 78.54  ? 239 GLN C CB  1 
ATOM   7989  C  CG  . GLN C 1 238 ? 7.385   -0.609  34.896  1.00 86.88  ? 239 GLN C CG  1 
ATOM   7990  C  CD  . GLN C 1 238 ? 7.015   -1.488  36.078  1.00 95.81  ? 239 GLN C CD  1 
ATOM   7991  O  OE1 . GLN C 1 238 ? 6.160   -2.368  35.969  1.00 97.92  ? 239 GLN C OE1 1 
ATOM   7992  N  NE2 . GLN C 1 238 ? 7.660   -1.254  37.216  1.00 97.52  ? 239 GLN C NE2 1 
ATOM   7993  N  N   . VAL C 1 239 ? 3.670   -0.583  31.637  1.00 61.49  ? 240 VAL C N   1 
ATOM   7994  C  CA  . VAL C 1 239 ? 2.233   -0.537  31.390  1.00 63.90  ? 240 VAL C CA  1 
ATOM   7995  C  C   . VAL C 1 239 ? 1.671   -1.957  31.364  1.00 64.58  ? 240 VAL C C   1 
ATOM   7996  O  O   . VAL C 1 239 ? 2.123   -2.793  30.581  1.00 66.40  ? 240 VAL C O   1 
ATOM   7997  C  CB  . VAL C 1 239 ? 1.900   0.184   30.070  1.00 57.61  ? 240 VAL C CB  1 
ATOM   7998  C  CG1 . VAL C 1 239 ? 0.464   -0.097  29.653  1.00 52.52  ? 240 VAL C CG1 1 
ATOM   7999  C  CG2 . VAL C 1 239 ? 2.144   1.681   30.207  1.00 55.17  ? 240 VAL C CG2 1 
ATOM   8000  N  N   . PRO C 1 240 ? 0.685   -2.234  32.229  1.00 68.89  ? 241 PRO C N   1 
ATOM   8001  C  CA  . PRO C 1 240 ? 0.128   -3.582  32.385  1.00 66.86  ? 241 PRO C CA  1 
ATOM   8002  C  C   . PRO C 1 240 ? -0.768  -4.000  31.226  1.00 65.91  ? 241 PRO C C   1 
ATOM   8003  O  O   . PRO C 1 240 ? -1.241  -3.153  30.468  1.00 66.22  ? 241 PRO C O   1 
ATOM   8004  C  CB  . PRO C 1 240 ? -0.683  -3.469  33.676  1.00 68.41  ? 241 PRO C CB  1 
ATOM   8005  C  CG  . PRO C 1 240 ? -1.131  -2.050  33.692  1.00 70.75  ? 241 PRO C CG  1 
ATOM   8006  C  CD  . PRO C 1 240 ? 0.011   -1.258  33.105  1.00 70.18  ? 241 PRO C CD  1 
ATOM   8007  N  N   . LEU C 1 241 ? -0.993  -5.303  31.097  1.00 64.35  ? 242 LEU C N   1 
ATOM   8008  C  CA  . LEU C 1 241 ? -1.923  -5.828  30.107  1.00 62.64  ? 242 LEU C CA  1 
ATOM   8009  C  C   . LEU C 1 241 ? -3.322  -5.920  30.704  1.00 61.01  ? 242 LEU C C   1 
ATOM   8010  O  O   . LEU C 1 241 ? -3.493  -6.378  31.834  1.00 64.14  ? 242 LEU C O   1 
ATOM   8011  C  CB  . LEU C 1 241 ? -1.465  -7.198  29.608  1.00 62.67  ? 242 LEU C CB  1 
ATOM   8012  C  CG  . LEU C 1 241 ? -0.123  -7.226  28.876  1.00 60.72  ? 242 LEU C CG  1 
ATOM   8013  C  CD1 . LEU C 1 241 ? 0.321   -8.658  28.638  1.00 61.09  ? 242 LEU C CD1 1 
ATOM   8014  C  CD2 . LEU C 1 241 ? -0.217  -6.465  27.563  1.00 62.61  ? 242 LEU C CD2 1 
ATOM   8015  N  N   . GLY C 1 242 ? -4.318  -5.481  29.944  1.00 58.02  ? 243 GLY C N   1 
ATOM   8016  C  CA  . GLY C 1 242 ? -5.691  -5.475  30.416  1.00 55.30  ? 243 GLY C CA  1 
ATOM   8017  C  C   . GLY C 1 242 ? -6.287  -6.863  30.547  1.00 54.49  ? 243 GLY C C   1 
ATOM   8018  O  O   . GLY C 1 242 ? -5.758  -7.826  29.991  1.00 54.41  ? 243 GLY C O   1 
ATOM   8019  N  N   . PRO C 1 243 ? -7.400  -6.972  31.290  1.00 53.90  ? 244 PRO C N   1 
ATOM   8020  C  CA  . PRO C 1 243 ? -8.112  -8.238  31.501  1.00 57.27  ? 244 PRO C CA  1 
ATOM   8021  C  C   . PRO C 1 243 ? -8.599  -8.855  30.193  1.00 56.88  ? 244 PRO C C   1 
ATOM   8022  O  O   . PRO C 1 243 ? -8.509  -10.072 30.016  1.00 54.42  ? 244 PRO C O   1 
ATOM   8023  C  CB  . PRO C 1 243 ? -9.294  -7.833  32.391  1.00 58.74  ? 244 PRO C CB  1 
ATOM   8024  C  CG  . PRO C 1 243 ? -9.452  -6.361  32.179  1.00 56.58  ? 244 PRO C CG  1 
ATOM   8025  C  CD  . PRO C 1 243 ? -8.066  -5.846  31.964  1.00 57.07  ? 244 PRO C CD  1 
ATOM   8026  N  N   . GLU C 1 244 ? -9.109  -8.020  29.293  1.00 60.48  ? 245 GLU C N   1 
ATOM   8027  C  CA  . GLU C 1 244 ? -9.529  -8.473  27.972  1.00 64.49  ? 245 GLU C CA  1 
ATOM   8028  C  C   . GLU C 1 244 ? -8.357  -9.097  27.227  1.00 63.10  ? 245 GLU C C   1 
ATOM   8029  O  O   . GLU C 1 244 ? -8.476  -10.179 26.643  1.00 59.81  ? 245 GLU C O   1 
ATOM   8030  C  CB  . GLU C 1 244 ? -10.111 -7.310  27.163  1.00 69.01  ? 245 GLU C CB  1 
ATOM   8031  C  CG  . GLU C 1 244 ? -11.601 -7.089  27.369  1.00 76.42  ? 245 GLU C CG  1 
ATOM   8032  C  CD  . GLU C 1 244 ? -12.448 -8.174  26.729  1.00 82.47  ? 245 GLU C CD  1 
ATOM   8033  O  OE1 . GLU C 1 244 ? -11.919 -8.923  25.879  1.00 81.79  ? 245 GLU C OE1 1 
ATOM   8034  O  OE2 . GLU C 1 244 ? -13.644 -8.278  27.074  1.00 83.25  ? 245 GLU C OE2 1 
ATOM   8035  N  N   . CYS C 1 245 ? -7.223  -8.404  27.260  1.00 61.86  ? 246 CYS C N   1 
ATOM   8036  C  CA  . CYS C 1 245 ? -5.999  -8.903  26.653  1.00 62.31  ? 246 CYS C CA  1 
ATOM   8037  C  C   . CYS C 1 245 ? -5.619  -10.250 27.252  1.00 60.76  ? 246 CYS C C   1 
ATOM   8038  O  O   . CYS C 1 245 ? -5.234  -11.163 26.531  1.00 60.83  ? 246 CYS C O   1 
ATOM   8039  C  CB  . CYS C 1 245 ? -4.855  -7.902  26.835  1.00 65.50  ? 246 CYS C CB  1 
ATOM   8040  S  SG  . CYS C 1 245 ? -3.265  -8.471  26.189  1.00 128.84 ? 246 CYS C SG  1 
ATOM   8041  N  N   . SER C 1 246 ? -5.742  -10.367 28.571  1.00 57.69  ? 247 SER C N   1 
ATOM   8042  C  CA  . SER C 1 246 ? -5.440  -11.614 29.265  1.00 55.85  ? 247 SER C CA  1 
ATOM   8043  C  C   . SER C 1 246 ? -6.320  -12.759 28.763  1.00 56.30  ? 247 SER C C   1 
ATOM   8044  O  O   . SER C 1 246 ? -5.825  -13.850 28.456  1.00 55.25  ? 247 SER C O   1 
ATOM   8045  C  CB  . SER C 1 246 ? -5.613  -11.437 30.775  1.00 61.51  ? 247 SER C CB  1 
ATOM   8046  O  OG  . SER C 1 246 ? -5.315  -12.637 31.466  1.00 65.76  ? 247 SER C OG  1 
ATOM   8047  N  N   . ARG C 1 247 ? -7.623  -12.498 28.680  1.00 50.29  ? 248 ARG C N   1 
ATOM   8048  C  CA  . ARG C 1 247 ? -8.578  -13.477 28.167  1.00 46.38  ? 248 ARG C CA  1 
ATOM   8049  C  C   . ARG C 1 247 ? -8.209  -13.923 26.756  1.00 47.94  ? 248 ARG C C   1 
ATOM   8050  O  O   . ARG C 1 247 ? -8.140  -15.122 26.469  1.00 46.38  ? 248 ARG C O   1 
ATOM   8051  C  CB  . ARG C 1 247 ? -9.997  -12.903 28.172  1.00 45.44  ? 248 ARG C CB  1 
ATOM   8052  C  CG  . ARG C 1 247 ? -10.545 -12.585 29.552  1.00 47.17  ? 248 ARG C CG  1 
ATOM   8053  C  CD  . ARG C 1 247 ? -11.949 -12.004 29.464  1.00 49.75  ? 248 ARG C CD  1 
ATOM   8054  N  N   . ALA C 1 248 ? -7.969  -12.948 25.883  1.00 43.08  ? 249 ALA C N   1 
ATOM   8055  C  CA  . ALA C 1 248 ? -7.621  -13.228 24.492  1.00 41.96  ? 249 ALA C CA  1 
ATOM   8056  C  C   . ALA C 1 248 ? -6.339  -14.048 24.385  1.00 43.39  ? 249 ALA C C   1 
ATOM   8057  O  O   . ALA C 1 248 ? -6.227  -14.932 23.534  1.00 46.39  ? 249 ALA C O   1 
ATOM   8058  C  CB  . ALA C 1 248 ? -7.483  -11.932 23.715  1.00 40.05  ? 249 ALA C CB  1 
ATOM   8059  N  N   . VAL C 1 249 ? -5.376  -13.752 25.253  1.00 44.65  ? 250 VAL C N   1 
ATOM   8060  C  CA  . VAL C 1 249 ? -4.110  -14.474 25.271  1.00 44.45  ? 250 VAL C CA  1 
ATOM   8061  C  C   . VAL C 1 249 ? -4.321  -15.916 25.714  1.00 46.98  ? 250 VAL C C   1 
ATOM   8062  O  O   . VAL C 1 249 ? -3.759  -16.837 25.123  1.00 45.49  ? 250 VAL C O   1 
ATOM   8063  C  CB  . VAL C 1 249 ? -3.078  -13.792 26.194  1.00 40.00  ? 250 VAL C CB  1 
ATOM   8064  C  CG1 . VAL C 1 249 ? -1.893  -14.709 26.450  1.00 42.25  ? 250 VAL C CG1 1 
ATOM   8065  C  CG2 . VAL C 1 249 ? -2.607  -12.487 25.579  1.00 41.38  ? 250 VAL C CG2 1 
ATOM   8066  N  N   . MET C 1 250 ? -5.136  -16.113 26.747  1.00 46.17  ? 251 MET C N   1 
ATOM   8067  C  CA  . MET C 1 250 ? -5.470  -17.466 27.181  1.00 45.73  ? 251 MET C CA  1 
ATOM   8068  C  C   . MET C 1 250 ? -6.143  -18.244 26.052  1.00 45.58  ? 251 MET C C   1 
ATOM   8069  O  O   . MET C 1 250 ? -5.820  -19.408 25.808  1.00 44.63  ? 251 MET C O   1 
ATOM   8070  C  CB  . MET C 1 250 ? -6.376  -17.437 28.412  1.00 47.36  ? 251 MET C CB  1 
ATOM   8071  C  CG  . MET C 1 250 ? -6.962  -18.796 28.780  1.00 43.96  ? 251 MET C CG  1 
ATOM   8072  S  SD  . MET C 1 250 ? -5.736  -20.117 28.895  1.00 50.19  ? 251 MET C SD  1 
ATOM   8073  C  CE  . MET C 1 250 ? -6.800  -21.558 28.948  1.00 49.18  ? 251 MET C CE  1 
ATOM   8074  N  N   . LYS C 1 251 ? -7.069  -17.589 25.358  1.00 45.20  ? 252 LYS C N   1 
ATOM   8075  C  CA  . LYS C 1 251 ? -7.766  -18.211 24.236  1.00 46.21  ? 252 LYS C CA  1 
ATOM   8076  C  C   . LYS C 1 251 ? -6.787  -18.579 23.125  1.00 45.09  ? 252 LYS C C   1 
ATOM   8077  O  O   . LYS C 1 251 ? -6.936  -19.604 22.460  1.00 47.81  ? 252 LYS C O   1 
ATOM   8078  C  CB  . LYS C 1 251 ? -8.856  -17.278 23.703  1.00 47.78  ? 252 LYS C CB  1 
ATOM   8079  C  CG  . LYS C 1 251 ? -9.829  -17.929 22.731  1.00 48.76  ? 252 LYS C CG  1 
ATOM   8080  C  CD  . LYS C 1 251 ? -10.975 -16.984 22.399  1.00 54.71  ? 252 LYS C CD  1 
ATOM   8081  C  CE  . LYS C 1 251 ? -12.116 -17.705 21.698  1.00 60.21  ? 252 LYS C CE  1 
ATOM   8082  N  NZ  . LYS C 1 251 ? -11.862 -17.875 20.241  1.00 62.63  ? 252 LYS C NZ  1 
ATOM   8083  N  N   . LEU C 1 252 ? -5.776  -17.736 22.945  1.00 49.98  ? 253 LEU C N   1 
ATOM   8084  C  CA  . LEU C 1 252 ? -4.766  -17.933 21.913  1.00 48.50  ? 253 LEU C CA  1 
ATOM   8085  C  C   . LEU C 1 252 ? -3.835  -19.105 22.214  1.00 52.47  ? 253 LEU C C   1 
ATOM   8086  O  O   . LEU C 1 252 ? -3.594  -19.956 21.358  1.00 40.31  ? 253 LEU C O   1 
ATOM   8087  C  CB  . LEU C 1 252 ? -3.943  -16.652 21.746  1.00 47.66  ? 253 LEU C CB  1 
ATOM   8088  C  CG  . LEU C 1 252 ? -2.734  -16.685 20.808  1.00 46.55  ? 253 LEU C CG  1 
ATOM   8089  C  CD1 . LEU C 1 252 ? -3.170  -16.919 19.375  1.00 43.18  ? 253 LEU C CD1 1 
ATOM   8090  C  CD2 . LEU C 1 252 ? -1.930  -15.397 20.922  1.00 38.79  ? 253 LEU C CD2 1 
ATOM   8091  N  N   . VAL C 1 253 ? -3.324  -19.148 23.440  1.00 50.08  ? 254 VAL C N   1 
ATOM   8092  C  CA  . VAL C 1 253 ? -2.224  -20.042 23.782  1.00 49.87  ? 254 VAL C CA  1 
ATOM   8093  C  C   . VAL C 1 253 ? -2.656  -21.431 24.256  1.00 57.79  ? 254 VAL C C   1 
ATOM   8094  O  O   . VAL C 1 253 ? -2.258  -22.437 23.669  1.00 63.95  ? 254 VAL C O   1 
ATOM   8095  C  CB  . VAL C 1 253 ? -1.332  -19.413 24.874  1.00 41.46  ? 254 VAL C CB  1 
ATOM   8096  C  CG1 . VAL C 1 253 ? -0.170  -20.331 25.203  1.00 39.92  ? 254 VAL C CG1 1 
ATOM   8097  C  CG2 . VAL C 1 253 ? -0.821  -18.053 24.421  1.00 39.13  ? 254 VAL C CG2 1 
ATOM   8098  N  N   . TYR C 1 254 ? -3.464  -21.490 25.310  1.00 53.43  ? 255 TYR C N   1 
ATOM   8099  C  CA  . TYR C 1 254 ? -3.730  -22.763 25.977  1.00 51.50  ? 255 TYR C CA  1 
ATOM   8100  C  C   . TYR C 1 254 ? -5.144  -23.308 25.789  1.00 52.27  ? 255 TYR C C   1 
ATOM   8101  O  O   . TYR C 1 254 ? -5.447  -24.411 26.246  1.00 52.68  ? 255 TYR C O   1 
ATOM   8102  C  CB  . TYR C 1 254 ? -3.439  -22.630 27.473  1.00 47.69  ? 255 TYR C CB  1 
ATOM   8103  C  CG  . TYR C 1 254 ? -1.980  -22.397 27.783  1.00 50.70  ? 255 TYR C CG  1 
ATOM   8104  C  CD1 . TYR C 1 254 ? -0.992  -23.186 27.207  1.00 41.40  ? 255 TYR C CD1 1 
ATOM   8105  C  CD2 . TYR C 1 254 ? -1.588  -21.379 28.641  1.00 47.61  ? 255 TYR C CD2 1 
ATOM   8106  C  CE1 . TYR C 1 254 ? 0.345   -22.973 27.485  1.00 43.15  ? 255 TYR C CE1 1 
ATOM   8107  C  CE2 . TYR C 1 254 ? -0.255  -21.157 28.924  1.00 50.70  ? 255 TYR C CE2 1 
ATOM   8108  C  CZ  . TYR C 1 254 ? 0.707   -21.956 28.344  1.00 50.19  ? 255 TYR C CZ  1 
ATOM   8109  O  OH  . TYR C 1 254 ? 2.035   -21.732 28.625  1.00 51.45  ? 255 TYR C OH  1 
ATOM   8110  N  N   . CYS C 1 255 ? -6.010  -22.552 25.123  1.00 47.56  ? 256 CYS C N   1 
ATOM   8111  C  CA  . CYS C 1 255 ? -7.374  -23.019 24.894  1.00 48.21  ? 256 CYS C CA  1 
ATOM   8112  C  C   . CYS C 1 255 ? -7.419  -24.109 23.827  1.00 52.40  ? 256 CYS C C   1 
ATOM   8113  O  O   . CYS C 1 255 ? -8.437  -24.778 23.656  1.00 53.37  ? 256 CYS C O   1 
ATOM   8114  C  CB  . CYS C 1 255 ? -8.290  -21.858 24.509  1.00 46.66  ? 256 CYS C CB  1 
ATOM   8115  S  SG  . CYS C 1 255 ? -8.959  -20.965 25.934  1.00 53.43  ? 256 CYS C SG  1 
ATOM   8116  N  N   . ALA C 1 256 ? -6.312  -24.282 23.112  1.00 53.12  ? 257 ALA C N   1 
ATOM   8117  C  CA  . ALA C 1 256 ? -6.171  -25.405 22.197  1.00 42.88  ? 257 ALA C CA  1 
ATOM   8118  C  C   . ALA C 1 256 ? -6.048  -26.689 23.005  1.00 52.36  ? 257 ALA C C   1 
ATOM   8119  O  O   . ALA C 1 256 ? -6.679  -27.699 22.695  1.00 55.51  ? 257 ALA C O   1 
ATOM   8120  C  CB  . ALA C 1 256 ? -4.962  -25.220 21.295  1.00 42.70  ? 257 ALA C CB  1 
ATOM   8121  N  N   . HIS C 1 257 ? -5.232  -26.631 24.053  1.00 51.03  ? 258 HIS C N   1 
ATOM   8122  C  CA  . HIS C 1 257 ? -5.020  -27.767 24.941  1.00 51.37  ? 258 HIS C CA  1 
ATOM   8123  C  C   . HIS C 1 257 ? -6.325  -28.192 25.603  1.00 54.85  ? 258 HIS C C   1 
ATOM   8124  O  O   . HIS C 1 257 ? -6.619  -29.382 25.716  1.00 53.03  ? 258 HIS C O   1 
ATOM   8125  C  CB  . HIS C 1 257 ? -3.979  -27.429 26.013  1.00 54.24  ? 258 HIS C CB  1 
ATOM   8126  C  CG  . HIS C 1 257 ? -2.647  -27.023 25.461  1.00 61.21  ? 258 HIS C CG  1 
ATOM   8127  N  ND1 . HIS C 1 257 ? -2.481  -25.930 24.637  1.00 61.80  ? 258 HIS C ND1 1 
ATOM   8128  C  CD2 . HIS C 1 257 ? -1.416  -27.564 25.619  1.00 61.82  ? 258 HIS C CD2 1 
ATOM   8129  C  CE1 . HIS C 1 257 ? -1.206  -25.816 24.310  1.00 61.46  ? 258 HIS C CE1 1 
ATOM   8130  N  NE2 . HIS C 1 257 ? -0.538  -26.795 24.893  1.00 61.97  ? 258 HIS C NE2 1 
ATOM   8131  N  N   . CYS C 1 258 ? -7.105  -27.207 26.038  1.00 50.24  ? 259 CYS C N   1 
ATOM   8132  C  CA  . CYS C 1 258 ? -8.366  -27.473 26.716  1.00 51.01  ? 259 CYS C CA  1 
ATOM   8133  C  C   . CYS C 1 258 ? -9.375  -28.127 25.782  1.00 52.58  ? 259 CYS C C   1 
ATOM   8134  O  O   . CYS C 1 258 ? -10.074 -29.058 26.171  1.00 53.68  ? 259 CYS C O   1 
ATOM   8135  C  CB  . CYS C 1 258 ? -8.946  -26.182 27.296  1.00 51.13  ? 259 CYS C CB  1 
ATOM   8136  S  SG  . CYS C 1 258 ? -7.997  -25.494 28.673  1.00 71.03  ? 259 CYS C SG  1 
ATOM   8137  N  N   . LEU C 1 259 ? -9.442  -27.648 24.545  1.00 53.80  ? 260 LEU C N   1 
ATOM   8138  C  CA  . LEU C 1 259 ? -10.408 -28.172 23.586  1.00 49.76  ? 260 LEU C CA  1 
ATOM   8139  C  C   . LEU C 1 259 ? -9.845  -29.333 22.768  1.00 50.81  ? 260 LEU C C   1 
ATOM   8140  O  O   . LEU C 1 259 ? -10.257 -29.561 21.631  1.00 54.11  ? 260 LEU C O   1 
ATOM   8141  C  CB  . LEU C 1 259 ? -10.896 -27.056 22.660  1.00 49.91  ? 260 LEU C CB  1 
ATOM   8142  C  CG  . LEU C 1 259 ? -11.761 -26.002 23.356  1.00 51.98  ? 260 LEU C CG  1 
ATOM   8143  C  CD1 . LEU C 1 259 ? -11.954 -24.775 22.479  1.00 54.59  ? 260 LEU C CD1 1 
ATOM   8144  C  CD2 . LEU C 1 259 ? -13.104 -26.598 23.755  1.00 55.02  ? 260 LEU C CD2 1 
ATOM   8145  N  N   . GLY C 1 260 ? -8.899  -30.060 23.355  1.00 56.55  ? 261 GLY C N   1 
ATOM   8146  C  CA  . GLY C 1 260 ? -8.468  -31.340 22.820  1.00 60.82  ? 261 GLY C CA  1 
ATOM   8147  C  C   . GLY C 1 260 ? -7.468  -31.341 21.678  1.00 66.10  ? 261 GLY C C   1 
ATOM   8148  O  O   . GLY C 1 260 ? -7.361  -32.332 20.956  1.00 69.55  ? 261 GLY C O   1 
ATOM   8149  N  N   . VAL C 1 261 ? -6.732  -30.247 21.506  1.00 65.36  ? 262 VAL C N   1 
ATOM   8150  C  CA  . VAL C 1 261 ? -5.677  -30.208 20.494  1.00 60.41  ? 262 VAL C CA  1 
ATOM   8151  C  C   . VAL C 1 261 ? -4.394  -29.555 21.023  1.00 60.55  ? 262 VAL C C   1 
ATOM   8152  O  O   . VAL C 1 261 ? -3.999  -28.483 20.561  1.00 57.48  ? 262 VAL C O   1 
ATOM   8153  C  CB  . VAL C 1 261 ? -6.146  -29.468 19.218  1.00 63.04  ? 262 VAL C CB  1 
ATOM   8154  C  CG1 . VAL C 1 261 ? -6.970  -30.396 18.337  1.00 63.18  ? 262 VAL C CG1 1 
ATOM   8155  C  CG2 . VAL C 1 261 ? -6.946  -28.222 19.575  1.00 61.87  ? 262 VAL C CG2 1 
ATOM   8156  N  N   . PRO C 1 262 ? -3.728  -30.215 21.986  1.00 60.27  ? 263 PRO C N   1 
ATOM   8157  C  CA  . PRO C 1 262 ? -2.523  -29.665 22.618  1.00 59.87  ? 263 PRO C CA  1 
ATOM   8158  C  C   . PRO C 1 262 ? -1.338  -29.599 21.660  1.00 61.23  ? 263 PRO C C   1 
ATOM   8159  O  O   . PRO C 1 262 ? -0.420  -28.805 21.868  1.00 57.73  ? 263 PRO C O   1 
ATOM   8160  C  CB  . PRO C 1 262 ? -2.237  -30.651 23.761  1.00 59.33  ? 263 PRO C CB  1 
ATOM   8161  C  CG  . PRO C 1 262 ? -3.472  -31.497 23.885  1.00 61.42  ? 263 PRO C CG  1 
ATOM   8162  C  CD  . PRO C 1 262 ? -4.054  -31.547 22.517  1.00 59.94  ? 263 PRO C CD  1 
ATOM   8163  N  N   . GLY C 1 263 ? -1.363  -30.433 20.625  1.00 62.04  ? 264 GLY C N   1 
ATOM   8164  C  CA  . GLY C 1 263 ? -0.290  -30.470 19.648  1.00 64.02  ? 264 GLY C CA  1 
ATOM   8165  C  C   . GLY C 1 263 ? -0.383  -29.327 18.659  1.00 64.41  ? 264 GLY C C   1 
ATOM   8166  O  O   . GLY C 1 263 ? 0.569   -29.039 17.934  1.00 66.02  ? 264 GLY C O   1 
ATOM   8167  N  N   . ALA C 1 264 ? -1.539  -28.672 18.630  1.00 66.50  ? 265 ALA C N   1 
ATOM   8168  C  CA  . ALA C 1 264 ? -1.750  -27.538 17.742  1.00 66.10  ? 265 ALA C CA  1 
ATOM   8169  C  C   . ALA C 1 264 ? -1.142  -26.270 18.328  1.00 65.51  ? 265 ALA C C   1 
ATOM   8170  O  O   . ALA C 1 264 ? -1.234  -26.021 19.530  1.00 63.19  ? 265 ALA C O   1 
ATOM   8171  C  CB  . ALA C 1 264 ? -3.234  -27.341 17.475  1.00 67.17  ? 265 ALA C CB  1 
ATOM   8172  N  N   . ARG C 1 265 ? -0.512  -25.475 17.472  1.00 67.27  ? 266 ARG C N   1 
ATOM   8173  C  CA  . ARG C 1 265 ? 0.047   -24.198 17.888  1.00 70.20  ? 266 ARG C CA  1 
ATOM   8174  C  C   . ARG C 1 265 ? -0.518  -23.084 17.008  1.00 70.03  ? 266 ARG C C   1 
ATOM   8175  O  O   . ARG C 1 265 ? -0.723  -23.283 15.810  1.00 74.53  ? 266 ARG C O   1 
ATOM   8176  C  CB  . ARG C 1 265 ? 1.578   -24.250 17.843  1.00 76.47  ? 266 ARG C CB  1 
ATOM   8177  C  CG  . ARG C 1 265 ? 2.167   -24.895 19.093  1.00 81.88  ? 266 ARG C CG  1 
ATOM   8178  C  CD  . ARG C 1 265 ? 3.556   -25.468 18.877  1.00 87.26  ? 266 ARG C CD  1 
ATOM   8179  N  NE  . ARG C 1 265 ? 4.004   -26.211 20.054  1.00 92.01  ? 266 ARG C NE  1 
ATOM   8180  C  CZ  . ARG C 1 265 ? 4.822   -27.258 20.016  1.00 96.31  ? 266 ARG C CZ  1 
ATOM   8181  N  NH1 . ARG C 1 265 ? 5.291   -27.696 18.856  1.00 97.59  ? 266 ARG C NH1 1 
ATOM   8182  N  NH2 . ARG C 1 265 ? 5.170   -27.870 21.140  1.00 97.15  ? 266 ARG C NH2 1 
ATOM   8183  N  N   . PRO C 1 266 ? -0.772  -21.908 17.609  1.00 62.39  ? 267 PRO C N   1 
ATOM   8184  C  CA  . PRO C 1 266 ? -1.578  -20.825 17.028  1.00 58.77  ? 267 PRO C CA  1 
ATOM   8185  C  C   . PRO C 1 266 ? -1.195  -20.405 15.611  1.00 53.14  ? 267 PRO C C   1 
ATOM   8186  O  O   . PRO C 1 266 ? -0.017  -20.389 15.255  1.00 51.40  ? 267 PRO C O   1 
ATOM   8187  C  CB  . PRO C 1 266 ? -1.338  -19.664 17.996  1.00 59.56  ? 267 PRO C CB  1 
ATOM   8188  C  CG  . PRO C 1 266 ? -1.060  -20.318 19.291  1.00 61.06  ? 267 PRO C CG  1 
ATOM   8189  C  CD  . PRO C 1 266 ? -0.286  -21.557 18.956  1.00 63.42  ? 267 PRO C CD  1 
ATOM   8190  N  N   . CYS C 1 267 ? -2.208  -20.073 14.816  1.00 51.14  ? 268 CYS C N   1 
ATOM   8191  C  CA  . CYS C 1 267 ? -2.001  -19.498 13.494  1.00 51.78  ? 268 CYS C CA  1 
ATOM   8192  C  C   . CYS C 1 267 ? -1.354  -18.126 13.632  1.00 50.19  ? 268 CYS C C   1 
ATOM   8193  O  O   . CYS C 1 267 ? -1.740  -17.343 14.501  1.00 50.42  ? 268 CYS C O   1 
ATOM   8194  C  CB  . CYS C 1 267 ? -3.326  -19.389 12.735  1.00 52.85  ? 268 CYS C CB  1 
ATOM   8195  S  SG  . CYS C 1 267 ? -4.297  -20.914 12.684  1.00 98.36  ? 268 CYS C SG  1 
ATOM   8196  N  N   . PRO C 1 268 ? -0.364  -17.833 12.776  1.00 52.92  ? 269 PRO C N   1 
ATOM   8197  C  CA  . PRO C 1 268 ? 0.397   -16.577 12.819  1.00 54.52  ? 269 PRO C CA  1 
ATOM   8198  C  C   . PRO C 1 268 ? -0.486  -15.329 12.775  1.00 51.95  ? 269 PRO C C   1 
ATOM   8199  O  O   . PRO C 1 268 ? -0.241  -14.379 13.521  1.00 52.91  ? 269 PRO C O   1 
ATOM   8200  C  CB  . PRO C 1 268 ? 1.279   -16.662 11.570  1.00 57.13  ? 269 PRO C CB  1 
ATOM   8201  C  CG  . PRO C 1 268 ? 1.429   -18.124 11.321  1.00 55.35  ? 269 PRO C CG  1 
ATOM   8202  C  CD  . PRO C 1 268 ? 0.114   -18.730 11.709  1.00 52.89  ? 269 PRO C CD  1 
ATOM   8203  N  N   . ASP C 1 269 ? -1.502  -15.339 11.917  1.00 46.87  ? 270 ASP C N   1 
ATOM   8204  C  CA  . ASP C 1 269 ? -2.393  -14.192 11.777  1.00 51.99  ? 270 ASP C CA  1 
ATOM   8205  C  C   . ASP C 1 269 ? -3.287  -14.028 13.004  1.00 50.61  ? 270 ASP C C   1 
ATOM   8206  O  O   . ASP C 1 269 ? -3.594  -12.907 13.414  1.00 48.31  ? 270 ASP C O   1 
ATOM   8207  C  CB  . ASP C 1 269 ? -3.244  -14.329 10.513  1.00 54.18  ? 270 ASP C CB  1 
ATOM   8208  C  CG  . ASP C 1 269 ? -2.417  -14.245 9.244   1.00 59.34  ? 270 ASP C CG  1 
ATOM   8209  O  OD1 . ASP C 1 269 ? -1.324  -13.642 9.284   1.00 60.50  ? 270 ASP C OD1 1 
ATOM   8210  O  OD2 . ASP C 1 269 ? -2.860  -14.781 8.206   1.00 64.37  ? 270 ASP C OD2 1 
ATOM   8211  N  N   . TYR C 1 270 ? -3.702  -15.151 13.582  1.00 45.72  ? 271 TYR C N   1 
ATOM   8212  C  CA  . TYR C 1 270 ? -4.485  -15.151 14.813  1.00 45.75  ? 271 TYR C CA  1 
ATOM   8213  C  C   . TYR C 1 270 ? -3.672  -14.507 15.933  1.00 43.73  ? 271 TYR C C   1 
ATOM   8214  O  O   . TYR C 1 270 ? -4.124  -13.560 16.591  1.00 45.15  ? 271 TYR C O   1 
ATOM   8215  C  CB  . TYR C 1 270 ? -4.892  -16.584 15.181  1.00 44.95  ? 271 TYR C CB  1 
ATOM   8216  C  CG  . TYR C 1 270 ? -5.677  -16.733 16.469  1.00 45.54  ? 271 TYR C CG  1 
ATOM   8217  C  CD1 . TYR C 1 270 ? -6.416  -15.679 16.993  1.00 44.40  ? 271 TYR C CD1 1 
ATOM   8218  C  CD2 . TYR C 1 270 ? -5.678  -17.938 17.161  1.00 47.39  ? 271 TYR C CD2 1 
ATOM   8219  C  CE1 . TYR C 1 270 ? -7.128  -15.820 18.169  1.00 45.72  ? 271 TYR C CE1 1 
ATOM   8220  C  CE2 . TYR C 1 270 ? -6.387  -18.087 18.338  1.00 47.58  ? 271 TYR C CE2 1 
ATOM   8221  C  CZ  . TYR C 1 270 ? -7.110  -17.025 18.837  1.00 48.51  ? 271 TYR C CZ  1 
ATOM   8222  O  OH  . TYR C 1 270 ? -7.819  -17.168 20.007  1.00 53.00  ? 271 TYR C OH  1 
ATOM   8223  N  N   . CYS C 1 271 ? -2.467  -15.032 16.135  1.00 44.81  ? 272 CYS C N   1 
ATOM   8224  C  CA  . CYS C 1 271 ? -1.535  -14.500 17.120  1.00 44.35  ? 272 CYS C CA  1 
ATOM   8225  C  C   . CYS C 1 271 ? -1.312  -13.006 16.926  1.00 45.17  ? 272 CYS C C   1 
ATOM   8226  O  O   . CYS C 1 271 ? -1.394  -12.227 17.879  1.00 45.79  ? 272 CYS C O   1 
ATOM   8227  C  CB  . CYS C 1 271 ? -0.199  -15.243 17.043  1.00 44.43  ? 272 CYS C CB  1 
ATOM   8228  S  SG  . CYS C 1 271 ? 1.050   -14.660 18.211  1.00 56.00  ? 272 CYS C SG  1 
ATOM   8229  N  N   . ARG C 1 272 ? -1.036  -12.610 15.686  1.00 39.49  ? 273 ARG C N   1 
ATOM   8230  C  CA  . ARG C 1 272 ? -0.761  -11.211 15.381  1.00 47.94  ? 273 ARG C CA  1 
ATOM   8231  C  C   . ARG C 1 272 ? -1.968  -10.324 15.670  1.00 45.64  ? 273 ARG C C   1 
ATOM   8232  O  O   . ARG C 1 272 ? -1.813  -9.209  16.160  1.00 39.20  ? 273 ARG C O   1 
ATOM   8233  C  CB  . ARG C 1 272 ? -0.317  -11.049 13.924  1.00 47.35  ? 273 ARG C CB  1 
ATOM   8234  C  CG  . ARG C 1 272 ? 1.160   -11.356 13.703  1.00 46.87  ? 273 ARG C CG  1 
ATOM   8235  C  CD  . ARG C 1 272 ? 1.628   -10.933 12.318  1.00 53.62  ? 273 ARG C CD  1 
ATOM   8236  N  NE  . ARG C 1 272 ? 1.036   -11.739 11.255  1.00 64.81  ? 273 ARG C NE  1 
ATOM   8237  C  CZ  . ARG C 1 272 ? 1.633   -12.786 10.692  1.00 72.09  ? 273 ARG C CZ  1 
ATOM   8238  N  NH1 . ARG C 1 272 ? 2.843   -13.155 11.090  1.00 73.44  ? 273 ARG C NH1 1 
ATOM   8239  N  NH2 . ARG C 1 272 ? 1.022   -13.463 9.729   1.00 72.71  ? 273 ARG C NH2 1 
ATOM   8240  N  N   . ASN C 1 273 ? -3.168  -10.817 15.381  1.00 39.99  ? 274 ASN C N   1 
ATOM   8241  C  CA  . ASN C 1 273 ? -4.378  -10.069 15.705  1.00 40.43  ? 274 ASN C CA  1 
ATOM   8242  C  C   . ASN C 1 273 ? -4.543  -9.898  17.210  1.00 41.14  ? 274 ASN C C   1 
ATOM   8243  O  O   . ASN C 1 273 ? -4.864  -8.804  17.692  1.00 40.31  ? 274 ASN C O   1 
ATOM   8244  C  CB  . ASN C 1 273 ? -5.612  -10.753 15.115  1.00 49.87  ? 274 ASN C CB  1 
ATOM   8245  C  CG  . ASN C 1 273 ? -5.977  -10.213 13.747  1.00 57.48  ? 274 ASN C CG  1 
ATOM   8246  O  OD1 . ASN C 1 273 ? -5.827  -9.021  13.478  1.00 55.35  ? 274 ASN C OD1 1 
ATOM   8247  N  ND2 . ASN C 1 273 ? -6.463  -11.088 12.874  1.00 56.50  ? 274 ASN C ND2 1 
ATOM   8248  N  N   . VAL C 1 274 ? -4.312  -10.979 17.951  1.00 39.86  ? 275 VAL C N   1 
ATOM   8249  C  CA  . VAL C 1 274 ? -4.398  -10.927 19.407  1.00 39.18  ? 275 VAL C CA  1 
ATOM   8250  C  C   . VAL C 1 274 ? -3.418  -9.909  19.985  1.00 48.58  ? 275 VAL C C   1 
ATOM   8251  O  O   . VAL C 1 274 ? -3.797  -9.072  20.806  1.00 50.08  ? 275 VAL C O   1 
ATOM   8252  C  CB  . VAL C 1 274 ? -4.126  -12.302 20.043  1.00 39.05  ? 275 VAL C CB  1 
ATOM   8253  C  CG1 . VAL C 1 274 ? -3.960  -12.168 21.551  1.00 38.77  ? 275 VAL C CG1 1 
ATOM   8254  C  CG2 . VAL C 1 274 ? -5.248  -13.268 19.712  1.00 39.59  ? 275 VAL C CG2 1 
ATOM   8255  N  N   . LEU C 1 275 ? -2.164  -9.973  19.547  1.00 49.36  ? 276 LEU C N   1 
ATOM   8256  C  CA  . LEU C 1 275 ? -1.138  -9.077  20.072  1.00 45.53  ? 276 LEU C CA  1 
ATOM   8257  C  C   . LEU C 1 275 ? -1.366  -7.625  19.653  1.00 44.09  ? 276 LEU C C   1 
ATOM   8258  O  O   . LEU C 1 275 ? -1.093  -6.706  20.424  1.00 37.91  ? 276 LEU C O   1 
ATOM   8259  C  CB  . LEU C 1 275 ? 0.254   -9.538  19.635  1.00 37.73  ? 276 LEU C CB  1 
ATOM   8260  C  CG  . LEU C 1 275 ? 0.766   -10.813 20.309  1.00 41.17  ? 276 LEU C CG  1 
ATOM   8261  C  CD1 . LEU C 1 275 ? 2.268   -10.949 20.126  1.00 42.49  ? 276 LEU C CD1 1 
ATOM   8262  C  CD2 . LEU C 1 275 ? 0.401   -10.834 21.787  1.00 39.69  ? 276 LEU C CD2 1 
ATOM   8263  N  N   . LYS C 1 276 ? -1.864  -7.419  18.438  1.00 44.07  ? 277 LYS C N   1 
ATOM   8264  C  CA  . LYS C 1 276 ? -2.220  -6.075  17.992  1.00 38.83  ? 277 LYS C CA  1 
ATOM   8265  C  C   . LYS C 1 276 ? -3.378  -5.541  18.823  1.00 42.70  ? 277 LYS C C   1 
ATOM   8266  O  O   . LYS C 1 276 ? -3.496  -4.334  19.036  1.00 39.31  ? 277 LYS C O   1 
ATOM   8267  C  CB  . LYS C 1 276 ? -2.582  -6.060  16.505  1.00 39.42  ? 277 LYS C CB  1 
ATOM   8268  C  CG  . LYS C 1 276 ? -1.382  -6.148  15.575  1.00 39.32  ? 277 LYS C CG  1 
ATOM   8269  C  CD  . LYS C 1 276 ? -1.785  -5.910  14.130  1.00 40.09  ? 277 LYS C CD  1 
ATOM   8270  C  CE  . LYS C 1 276 ? -0.581  -5.976  13.206  1.00 43.97  ? 277 LYS C CE  1 
ATOM   8271  N  NZ  . LYS C 1 276 ? -0.943  -5.641  11.801  1.00 47.98  ? 277 LYS C NZ  1 
ATOM   8272  N  N   . GLY C 1 277 ? -4.230  -6.446  19.294  1.00 42.54  ? 278 GLY C N   1 
ATOM   8273  C  CA  . GLY C 1 277 ? -5.285  -6.073  20.217  1.00 41.24  ? 278 GLY C CA  1 
ATOM   8274  C  C   . GLY C 1 277 ? -4.727  -5.689  21.576  1.00 40.96  ? 278 GLY C C   1 
ATOM   8275  O  O   . GLY C 1 277 ? -5.165  -4.713  22.186  1.00 45.94  ? 278 GLY C O   1 
ATOM   8276  N  N   . CYS C 1 278 ? -3.748  -6.455  22.048  1.00 38.72  ? 279 CYS C N   1 
ATOM   8277  C  CA  . CYS C 1 278 ? -3.161  -6.231  23.366  1.00 44.50  ? 279 CYS C CA  1 
ATOM   8278  C  C   . CYS C 1 278 ? -2.190  -5.051  23.389  1.00 46.37  ? 279 CYS C C   1 
ATOM   8279  O  O   . CYS C 1 278 ? -2.096  -4.336  24.386  1.00 46.39  ? 279 CYS C O   1 
ATOM   8280  C  CB  . CYS C 1 278 ? -2.440  -7.493  23.846  1.00 47.43  ? 279 CYS C CB  1 
ATOM   8281  S  SG  . CYS C 1 278 ? -3.526  -8.891  24.219  1.00 63.61  ? 279 CYS C SG  1 
ATOM   8282  N  N   . LEU C 1 279 ? -1.472  -4.852  22.289  1.00 48.74  ? 280 LEU C N   1 
ATOM   8283  C  CA  . LEU C 1 279 ? -0.403  -3.858  22.246  1.00 46.49  ? 280 LEU C CA  1 
ATOM   8284  C  C   . LEU C 1 279 ? -0.785  -2.616  21.446  1.00 46.10  ? 280 LEU C C   1 
ATOM   8285  O  O   . LEU C 1 279 ? 0.073   -1.972  20.842  1.00 44.85  ? 280 LEU C O   1 
ATOM   8286  C  CB  . LEU C 1 279 ? 0.864   -4.483  21.660  1.00 46.74  ? 280 LEU C CB  1 
ATOM   8287  C  CG  . LEU C 1 279 ? 1.386   -5.710  22.408  1.00 46.11  ? 280 LEU C CG  1 
ATOM   8288  C  CD1 . LEU C 1 279 ? 2.495   -6.396  21.621  1.00 45.71  ? 280 LEU C CD1 1 
ATOM   8289  C  CD2 . LEU C 1 279 ? 1.869   -5.315  23.796  1.00 45.88  ? 280 LEU C CD2 1 
ATOM   8290  N  N   . ALA C 1 280 ? -2.071  -2.281  21.454  1.00 49.97  ? 281 ALA C N   1 
ATOM   8291  C  CA  . ALA C 1 280 ? -2.577  -1.136  20.704  1.00 49.29  ? 281 ALA C CA  1 
ATOM   8292  C  C   . ALA C 1 280 ? -2.000  0.185   21.214  1.00 51.63  ? 281 ALA C C   1 
ATOM   8293  O  O   . ALA C 1 280 ? -1.452  0.980   20.439  1.00 54.44  ? 281 ALA C O   1 
ATOM   8294  C  CB  . ALA C 1 280 ? -4.096  -1.105  20.762  1.00 53.33  ? 281 ALA C CB  1 
ATOM   8295  N  N   . ASN C 1 281 ? -2.132  0.412   22.518  1.00 51.82  ? 282 ASN C N   1 
ATOM   8296  C  CA  . ASN C 1 281 ? -1.622  1.626   23.146  1.00 49.00  ? 282 ASN C CA  1 
ATOM   8297  C  C   . ASN C 1 281 ? -0.127  1.799   22.906  1.00 50.74  ? 282 ASN C C   1 
ATOM   8298  O  O   . ASN C 1 281 ? 0.343   2.906   22.650  1.00 55.33  ? 282 ASN C O   1 
ATOM   8299  C  CB  . ASN C 1 281 ? -1.913  1.616   24.647  1.00 45.41  ? 282 ASN C CB  1 
ATOM   8300  C  CG  . ASN C 1 281 ? -3.380  1.841   24.958  1.00 42.54  ? 282 ASN C CG  1 
ATOM   8301  O  OD1 . ASN C 1 281 ? -4.015  2.736   24.399  1.00 41.19  ? 282 ASN C OD1 1 
ATOM   8302  N  ND2 . ASN C 1 281 ? -3.926  1.029   25.855  1.00 46.05  ? 282 ASN C ND2 1 
ATOM   8303  N  N   . GLN C 1 282 ? 0.613   0.697   22.986  1.00 49.62  ? 283 GLN C N   1 
ATOM   8304  C  CA  . GLN C 1 282 ? 2.036   0.709   22.676  1.00 46.48  ? 283 GLN C CA  1 
ATOM   8305  C  C   . GLN C 1 282 ? 2.259   1.090   21.218  1.00 44.38  ? 283 GLN C C   1 
ATOM   8306  O  O   . GLN C 1 282 ? 3.182   1.838   20.895  1.00 47.08  ? 283 GLN C O   1 
ATOM   8307  C  CB  . GLN C 1 282 ? 2.672   -0.654  22.962  1.00 37.35  ? 283 GLN C CB  1 
ATOM   8308  C  CG  . GLN C 1 282 ? 2.871   -0.973  24.438  1.00 44.17  ? 283 GLN C CG  1 
ATOM   8309  C  CD  . GLN C 1 282 ? 1.590   -1.384  25.139  1.00 44.29  ? 283 GLN C CD  1 
ATOM   8310  O  OE1 . GLN C 1 282 ? 0.506   -1.355  24.554  1.00 46.35  ? 283 GLN C OE1 1 
ATOM   8311  N  NE2 . GLN C 1 282 ? 1.710   -1.778  26.402  1.00 37.69  ? 283 GLN C NE2 1 
ATOM   8312  N  N   . ALA C 1 283 ? 1.402   0.573   20.343  1.00 38.17  ? 284 ALA C N   1 
ATOM   8313  C  CA  . ALA C 1 283 ? 1.511   0.832   18.912  1.00 38.44  ? 284 ALA C CA  1 
ATOM   8314  C  C   . ALA C 1 283 ? 1.205   2.290   18.583  1.00 49.73  ? 284 ALA C C   1 
ATOM   8315  O  O   . ALA C 1 283 ? 1.633   2.800   17.547  1.00 50.70  ? 284 ALA C O   1 
ATOM   8316  C  CB  . ALA C 1 283 ? 0.584   -0.092  18.135  1.00 38.71  ? 284 ALA C CB  1 
ATOM   8317  N  N   . ASP C 1 284 ? 0.470   2.959   19.467  1.00 47.32  ? 285 ASP C N   1 
ATOM   8318  C  CA  . ASP C 1 284 ? 0.151   4.375   19.276  1.00 45.33  ? 285 ASP C CA  1 
ATOM   8319  C  C   . ASP C 1 284 ? 1.379   5.290   19.383  1.00 48.17  ? 285 ASP C C   1 
ATOM   8320  O  O   . ASP C 1 284 ? 1.294   6.484   19.098  1.00 47.93  ? 285 ASP C O   1 
ATOM   8321  C  CB  . ASP C 1 284 ? -0.910  4.816   20.288  1.00 47.18  ? 285 ASP C CB  1 
ATOM   8322  C  CG  . ASP C 1 284 ? -2.323  4.703   19.742  1.00 52.56  ? 285 ASP C CG  1 
ATOM   8323  O  OD1 . ASP C 1 284 ? -2.495  4.141   18.639  1.00 50.01  ? 285 ASP C OD1 1 
ATOM   8324  O  OD2 . ASP C 1 284 ? -3.263  5.170   20.420  1.00 47.74  ? 285 ASP C OD2 1 
ATOM   8325  N  N   . LEU C 1 285 ? 2.515   4.729   19.789  1.00 43.03  ? 286 LEU C N   1 
ATOM   8326  C  CA  . LEU C 1 285 ? 3.753   5.496   19.939  1.00 47.04  ? 286 LEU C CA  1 
ATOM   8327  C  C   . LEU C 1 285 ? 4.508   5.638   18.617  1.00 38.97  ? 286 LEU C C   1 
ATOM   8328  O  O   . LEU C 1 285 ? 5.431   6.455   18.497  1.00 39.01  ? 286 LEU C O   1 
ATOM   8329  C  CB  . LEU C 1 285 ? 4.663   4.831   20.976  1.00 45.62  ? 286 LEU C CB  1 
ATOM   8330  C  CG  . LEU C 1 285 ? 4.173   4.767   22.423  1.00 50.47  ? 286 LEU C CG  1 
ATOM   8331  C  CD1 . LEU C 1 285 ? 4.902   3.670   23.182  1.00 51.02  ? 286 LEU C CD1 1 
ATOM   8332  C  CD2 . LEU C 1 285 ? 4.374   6.107   23.107  1.00 49.68  ? 286 LEU C CD2 1 
ATOM   8333  N  N   . ASP C 1 286 ? 4.093   4.842   17.634  1.00 39.05  ? 287 ASP C N   1 
ATOM   8334  C  CA  . ASP C 1 286 ? 4.822   4.663   16.378  1.00 41.62  ? 287 ASP C CA  1 
ATOM   8335  C  C   . ASP C 1 286 ? 5.206   5.963   15.678  1.00 42.74  ? 287 ASP C C   1 
ATOM   8336  O  O   . ASP C 1 286 ? 6.379   6.185   15.381  1.00 47.78  ? 287 ASP C O   1 
ATOM   8337  C  CB  . ASP C 1 286 ? 3.996   3.801   15.418  1.00 39.45  ? 287 ASP C CB  1 
ATOM   8338  C  CG  . ASP C 1 286 ? 4.767   3.418   14.169  1.00 39.63  ? 287 ASP C CG  1 
ATOM   8339  O  OD1 . ASP C 1 286 ? 5.952   3.040   14.291  1.00 51.60  ? 287 ASP C OD1 1 
ATOM   8340  O  OD2 . ASP C 1 286 ? 4.191   3.497   13.064  1.00 40.32  ? 287 ASP C OD2 1 
ATOM   8341  N  N   . ALA C 1 287 ? 4.216   6.813   15.420  1.00 40.39  ? 288 ALA C N   1 
ATOM   8342  C  CA  . ALA C 1 287 ? 4.425   8.040   14.654  1.00 53.66  ? 288 ALA C CA  1 
ATOM   8343  C  C   . ALA C 1 287 ? 5.507   8.936   15.256  1.00 40.90  ? 288 ALA C C   1 
ATOM   8344  O  O   . ALA C 1 287 ? 6.500   9.256   14.597  1.00 46.05  ? 288 ALA C O   1 
ATOM   8345  C  CB  . ALA C 1 287 ? 3.116   8.810   14.534  1.00 41.98  ? 288 ALA C CB  1 
ATOM   8346  N  N   . GLU C 1 288 ? 5.316   9.333   16.509  1.00 40.72  ? 289 GLU C N   1 
ATOM   8347  C  CA  . GLU C 1 288 ? 6.234   10.263  17.154  1.00 50.12  ? 289 GLU C CA  1 
ATOM   8348  C  C   . GLU C 1 288 ? 7.574   9.606   17.482  1.00 46.78  ? 289 GLU C C   1 
ATOM   8349  O  O   . GLU C 1 288 ? 8.600   10.285  17.557  1.00 46.21  ? 289 GLU C O   1 
ATOM   8350  C  CB  . GLU C 1 288 ? 5.599   10.845  18.419  1.00 40.85  ? 289 GLU C CB  1 
ATOM   8351  C  CG  . GLU C 1 288 ? 4.314   11.622  18.155  1.00 49.43  ? 289 GLU C CG  1 
ATOM   8352  C  CD  . GLU C 1 288 ? 4.487   12.724  17.121  1.00 55.56  ? 289 GLU C CD  1 
ATOM   8353  O  OE1 . GLU C 1 288 ? 5.564   13.358  17.088  1.00 55.26  ? 289 GLU C OE1 1 
ATOM   8354  O  OE2 . GLU C 1 288 ? 3.541   12.957  16.337  1.00 57.53  ? 289 GLU C OE2 1 
ATOM   8355  N  N   . TRP C 1 289 ? 7.562   8.288   17.672  1.00 43.37  ? 290 TRP C N   1 
ATOM   8356  C  CA  . TRP C 1 289 ? 8.805   7.534   17.838  1.00 45.87  ? 290 TRP C CA  1 
ATOM   8357  C  C   . TRP C 1 289 ? 9.663   7.648   16.577  1.00 43.25  ? 290 TRP C C   1 
ATOM   8358  O  O   . TRP C 1 289 ? 10.841  8.037   16.631  1.00 42.57  ? 290 TRP C O   1 
ATOM   8359  C  CB  . TRP C 1 289 ? 8.492   6.069   18.153  1.00 38.30  ? 290 TRP C CB  1 
ATOM   8360  C  CG  . TRP C 1 289 ? 9.684   5.179   18.312  1.00 39.55  ? 290 TRP C CG  1 
ATOM   8361  C  CD1 . TRP C 1 289 ? 10.153  4.272   17.407  1.00 37.85  ? 290 TRP C CD1 1 
ATOM   8362  C  CD2 . TRP C 1 289 ? 10.545  5.089   19.454  1.00 40.32  ? 290 TRP C CD2 1 
ATOM   8363  N  NE1 . TRP C 1 289 ? 11.258  3.629   17.910  1.00 37.57  ? 290 TRP C NE1 1 
ATOM   8364  C  CE2 . TRP C 1 289 ? 11.519  4.112   19.166  1.00 37.39  ? 290 TRP C CE2 1 
ATOM   8365  C  CE3 . TRP C 1 289 ? 10.590  5.742   20.690  1.00 37.57  ? 290 TRP C CE3 1 
ATOM   8366  C  CZ2 . TRP C 1 289 ? 12.527  3.773   20.067  1.00 40.32  ? 290 TRP C CZ2 1 
ATOM   8367  C  CZ3 . TRP C 1 289 ? 11.591  5.404   21.584  1.00 38.81  ? 290 TRP C CZ3 1 
ATOM   8368  C  CH2 . TRP C 1 289 ? 12.546  4.428   21.267  1.00 39.80  ? 290 TRP C CH2 1 
ATOM   8369  N  N   . ARG C 1 290 ? 9.050   7.320   15.442  1.00 43.10  ? 291 ARG C N   1 
ATOM   8370  C  CA  . ARG C 1 290 ? 9.696   7.435   14.140  1.00 39.84  ? 291 ARG C CA  1 
ATOM   8371  C  C   . ARG C 1 290 ? 10.167  8.861   13.882  1.00 47.81  ? 291 ARG C C   1 
ATOM   8372  O  O   . ARG C 1 290 ? 11.269  9.075   13.374  1.00 50.41  ? 291 ARG C O   1 
ATOM   8373  C  CB  . ARG C 1 290 ? 8.743   6.990   13.027  1.00 40.34  ? 291 ARG C CB  1 
ATOM   8374  C  CG  . ARG C 1 290 ? 8.409   5.510   13.045  1.00 39.96  ? 291 ARG C CG  1 
ATOM   8375  C  CD  . ARG C 1 290 ? 7.474   5.146   11.904  1.00 42.86  ? 291 ARG C CD  1 
ATOM   8376  N  NE  . ARG C 1 290 ? 7.201   3.713   11.860  1.00 44.10  ? 291 ARG C NE  1 
ATOM   8377  C  CZ  . ARG C 1 290 ? 7.912   2.838   11.156  1.00 47.51  ? 291 ARG C CZ  1 
ATOM   8378  N  NH1 . ARG C 1 290 ? 8.943   3.250   10.433  1.00 47.53  ? 291 ARG C NH1 1 
ATOM   8379  N  NH2 . ARG C 1 290 ? 7.592   1.552   11.175  1.00 46.73  ? 291 ARG C NH2 1 
ATOM   8380  N  N   . ASN C 1 291 ? 9.329   9.832   14.235  1.00 44.89  ? 292 ASN C N   1 
ATOM   8381  C  CA  . ASN C 1 291 ? 9.694   11.239  14.099  1.00 48.20  ? 292 ASN C CA  1 
ATOM   8382  C  C   . ASN C 1 291 ? 10.951  11.575  14.896  1.00 45.36  ? 292 ASN C C   1 
ATOM   8383  O  O   . ASN C 1 291 ? 11.855  12.252  14.396  1.00 41.23  ? 292 ASN C O   1 
ATOM   8384  C  CB  . ASN C 1 291 ? 8.541   12.141  14.545  1.00 50.18  ? 292 ASN C CB  1 
ATOM   8385  C  CG  . ASN C 1 291 ? 7.417   12.196  13.531  1.00 53.95  ? 292 ASN C CG  1 
ATOM   8386  O  OD1 . ASN C 1 291 ? 7.588   11.808  12.375  1.00 56.83  ? 292 ASN C OD1 1 
ATOM   8387  N  ND2 . ASN C 1 291 ? 6.258   12.689  13.957  1.00 51.87  ? 292 ASN C ND2 1 
ATOM   8388  N  N   . LEU C 1 292 ? 11.002  11.091  16.133  1.00 40.24  ? 293 LEU C N   1 
ATOM   8389  C  CA  . LEU C 1 292 ? 12.149  11.332  17.000  1.00 46.00  ? 293 LEU C CA  1 
ATOM   8390  C  C   . LEU C 1 292 ? 13.421  10.732  16.415  1.00 45.25  ? 293 LEU C C   1 
ATOM   8391  O  O   . LEU C 1 292 ? 14.429  11.429  16.242  1.00 49.29  ? 293 LEU C O   1 
ATOM   8392  C  CB  . LEU C 1 292 ? 11.904  10.757  18.396  1.00 39.42  ? 293 LEU C CB  1 
ATOM   8393  C  CG  . LEU C 1 292 ? 13.066  10.978  19.366  1.00 47.03  ? 293 LEU C CG  1 
ATOM   8394  C  CD1 . LEU C 1 292 ? 13.268  12.464  19.595  1.00 39.79  ? 293 LEU C CD1 1 
ATOM   8395  C  CD2 . LEU C 1 292 ? 12.842  10.254  20.682  1.00 38.83  ? 293 LEU C CD2 1 
ATOM   8396  N  N   . LEU C 1 293 ? 13.368  9.440   16.104  1.00 44.03  ? 294 LEU C N   1 
ATOM   8397  C  CA  . LEU C 1 293 ? 14.551  8.746   15.601  1.00 45.00  ? 294 LEU C CA  1 
ATOM   8398  C  C   . LEU C 1 293 ? 15.041  9.355   14.284  1.00 47.23  ? 294 LEU C C   1 
ATOM   8399  O  O   . LEU C 1 293 ? 16.250  9.499   14.065  1.00 46.42  ? 294 LEU C O   1 
ATOM   8400  C  CB  . LEU C 1 293 ? 14.266  7.252   15.430  1.00 45.48  ? 294 LEU C CB  1 
ATOM   8401  C  CG  . LEU C 1 293 ? 14.482  6.371   16.669  1.00 44.29  ? 294 LEU C CG  1 
ATOM   8402  C  CD1 . LEU C 1 293 ? 13.627  6.813   17.850  1.00 43.73  ? 294 LEU C CD1 1 
ATOM   8403  C  CD2 . LEU C 1 293 ? 14.226  4.908   16.343  1.00 45.40  ? 294 LEU C CD2 1 
ATOM   8404  N  N   . ASP C 1 294 ? 14.101  9.733   13.422  1.00 44.65  ? 295 ASP C N   1 
ATOM   8405  C  CA  . ASP C 1 294 ? 14.448  10.384  12.164  1.00 53.77  ? 295 ASP C CA  1 
ATOM   8406  C  C   . ASP C 1 294 ? 15.085  11.750  12.400  1.00 50.15  ? 295 ASP C C   1 
ATOM   8407  O  O   . ASP C 1 294 ? 16.022  12.131  11.698  1.00 45.30  ? 295 ASP C O   1 
ATOM   8408  C  CB  . ASP C 1 294 ? 13.218  10.526  11.269  1.00 62.62  ? 295 ASP C CB  1 
ATOM   8409  C  CG  . ASP C 1 294 ? 12.855  9.232   10.569  1.00 71.63  ? 295 ASP C CG  1 
ATOM   8410  O  OD1 . ASP C 1 294 ? 13.758  8.392   10.368  1.00 75.79  ? 295 ASP C OD1 1 
ATOM   8411  O  OD2 . ASP C 1 294 ? 11.670  9.055   10.217  1.00 74.47  ? 295 ASP C OD2 1 
ATOM   8412  N  N   . SER C 1 295 ? 14.580  12.483  13.389  1.00 47.27  ? 296 SER C N   1 
ATOM   8413  C  CA  . SER C 1 295 ? 15.153  13.782  13.728  1.00 47.85  ? 296 SER C CA  1 
ATOM   8414  C  C   . SER C 1 295 ? 16.579  13.636  14.260  1.00 45.97  ? 296 SER C C   1 
ATOM   8415  O  O   . SER C 1 295 ? 17.443  14.472  13.986  1.00 49.01  ? 296 SER C O   1 
ATOM   8416  C  CB  . SER C 1 295 ? 14.277  14.507  14.753  1.00 45.62  ? 296 SER C CB  1 
ATOM   8417  O  OG  . SER C 1 295 ? 14.286  13.835  15.999  1.00 49.06  ? 296 SER C OG  1 
ATOM   8418  N  N   . MET C 1 296 ? 16.822  12.569  15.017  1.00 43.12  ? 297 MET C N   1 
ATOM   8419  C  CA  . MET C 1 296 ? 18.154  12.309  15.560  1.00 46.10  ? 297 MET C CA  1 
ATOM   8420  C  C   . MET C 1 296 ? 19.146  11.929  14.458  1.00 46.21  ? 297 MET C C   1 
ATOM   8421  O  O   . MET C 1 296 ? 20.227  12.534  14.334  1.00 49.19  ? 297 MET C O   1 
ATOM   8422  C  CB  . MET C 1 296 ? 18.088  11.207  16.616  1.00 45.27  ? 297 MET C CB  1 
ATOM   8423  C  CG  . MET C 1 296 ? 17.238  11.566  17.823  1.00 39.80  ? 297 MET C CG  1 
ATOM   8424  S  SD  . MET C 1 296 ? 17.153  10.234  19.032  1.00 64.29  ? 297 MET C SD  1 
ATOM   8425  C  CE  . MET C 1 296 ? 18.891  9.843   19.203  1.00 52.02  ? 297 MET C CE  1 
ATOM   8426  N  N   . VAL C 1 297 ? 18.769  10.927  13.663  1.00 41.16  ? 298 VAL C N   1 
ATOM   8427  C  CA  . VAL C 1 297 ? 19.555  10.526  12.499  1.00 41.72  ? 298 VAL C CA  1 
ATOM   8428  C  C   . VAL C 1 297 ? 19.867  11.743  11.632  1.00 55.60  ? 298 VAL C C   1 
ATOM   8429  O  O   . VAL C 1 297 ? 20.978  11.896  11.123  1.00 61.21  ? 298 VAL C O   1 
ATOM   8430  C  CB  . VAL C 1 297 ? 18.818  9.462   11.655  1.00 41.77  ? 298 VAL C CB  1 
ATOM   8431  C  CG1 . VAL C 1 297 ? 19.476  9.296   10.290  1.00 42.64  ? 298 VAL C CG1 1 
ATOM   8432  C  CG2 . VAL C 1 297 ? 18.768  8.133   12.395  1.00 47.39  ? 298 VAL C CG2 1 
ATOM   8433  N  N   . LEU C 1 298 ? 18.878  12.620  11.496  1.00 52.85  ? 299 LEU C N   1 
ATOM   8434  C  CA  . LEU C 1 298 ? 19.040  13.851  10.737  1.00 51.43  ? 299 LEU C CA  1 
ATOM   8435  C  C   . LEU C 1 298 ? 20.072  14.782  11.370  1.00 52.75  ? 299 LEU C C   1 
ATOM   8436  O  O   . LEU C 1 298 ? 20.922  15.339  10.674  1.00 48.73  ? 299 LEU C O   1 
ATOM   8437  C  CB  . LEU C 1 298 ? 17.696  14.571  10.610  1.00 57.06  ? 299 LEU C CB  1 
ATOM   8438  C  CG  . LEU C 1 298 ? 17.652  15.817  9.726   1.00 63.63  ? 299 LEU C CG  1 
ATOM   8439  C  CD1 . LEU C 1 298 ? 18.022  15.470  8.292   1.00 65.85  ? 299 LEU C CD1 1 
ATOM   8440  C  CD2 . LEU C 1 298 ? 16.277  16.465  9.788   1.00 66.31  ? 299 LEU C CD2 1 
ATOM   8441  N  N   . ILE C 1 299 ? 20.005  14.950  12.688  1.00 47.51  ? 300 ILE C N   1 
ATOM   8442  C  CA  . ILE C 1 299 ? 20.874  15.915  13.353  1.00 48.06  ? 300 ILE C CA  1 
ATOM   8443  C  C   . ILE C 1 299 ? 22.296  15.391  13.562  1.00 50.28  ? 300 ILE C C   1 
ATOM   8444  O  O   . ILE C 1 299 ? 23.190  16.161  13.915  1.00 45.42  ? 300 ILE C O   1 
ATOM   8445  C  CB  . ILE C 1 299 ? 20.303  16.359  14.718  1.00 51.82  ? 300 ILE C CB  1 
ATOM   8446  C  CG1 . ILE C 1 299 ? 20.762  17.784  15.044  1.00 55.82  ? 300 ILE C CG1 1 
ATOM   8447  C  CG2 . ILE C 1 299 ? 20.700  15.385  15.817  1.00 49.23  ? 300 ILE C CG2 1 
ATOM   8448  C  CD1 . ILE C 1 299 ? 20.224  18.323  16.348  1.00 60.50  ? 300 ILE C CD1 1 
ATOM   8449  N  N   . THR C 1 300 ? 22.519  14.096  13.344  1.00 50.23  ? 301 THR C N   1 
ATOM   8450  C  CA  . THR C 1 300 ? 23.894  13.585  13.387  1.00 49.65  ? 301 THR C CA  1 
ATOM   8451  C  C   . THR C 1 300 ? 24.785  14.276  12.351  1.00 48.91  ? 301 THR C C   1 
ATOM   8452  O  O   . THR C 1 300 ? 25.992  14.410  12.549  1.00 48.50  ? 301 THR C O   1 
ATOM   8453  C  CB  . THR C 1 300 ? 23.966  12.063  13.147  1.00 42.93  ? 301 THR C CB  1 
ATOM   8454  O  OG1 . THR C 1 300 ? 23.441  11.750  11.851  1.00 55.54  ? 301 THR C OG1 1 
ATOM   8455  C  CG2 . THR C 1 300 ? 23.191  11.312  14.208  1.00 42.07  ? 301 THR C CG2 1 
ATOM   8456  N  N   . ASP C 1 301 ? 24.181  14.716  11.252  1.00 44.63  ? 302 ASP C N   1 
ATOM   8457  C  CA  . ASP C 1 301 ? 24.913  15.374  10.173  1.00 45.67  ? 302 ASP C CA  1 
ATOM   8458  C  C   . ASP C 1 301 ? 25.545  16.694  10.609  1.00 50.68  ? 302 ASP C C   1 
ATOM   8459  O  O   . ASP C 1 301 ? 26.593  17.088  10.096  1.00 50.39  ? 302 ASP C O   1 
ATOM   8460  C  CB  . ASP C 1 301 ? 23.987  15.624  8.979   1.00 53.94  ? 302 ASP C CB  1 
ATOM   8461  C  CG  . ASP C 1 301 ? 23.648  14.353  8.226   1.00 54.93  ? 302 ASP C CG  1 
ATOM   8462  O  OD1 . ASP C 1 301 ? 24.559  13.528  8.007   1.00 57.03  ? 302 ASP C OD1 1 
ATOM   8463  O  OD2 . ASP C 1 301 ? 22.469  14.180  7.852   1.00 57.65  ? 302 ASP C OD2 1 
ATOM   8464  N  N   . LYS C 1 302 ? 24.908  17.373  11.559  1.00 51.37  ? 303 LYS C N   1 
ATOM   8465  C  CA  . LYS C 1 302 ? 25.359  18.694  11.988  1.00 49.20  ? 303 LYS C CA  1 
ATOM   8466  C  C   . LYS C 1 302 ? 26.583  18.648  12.899  1.00 54.02  ? 303 LYS C C   1 
ATOM   8467  O  O   . LYS C 1 302 ? 27.045  19.684  13.373  1.00 56.33  ? 303 LYS C O   1 
ATOM   8468  C  CB  . LYS C 1 302 ? 24.222  19.437  12.692  1.00 47.71  ? 303 LYS C CB  1 
ATOM   8469  C  CG  . LYS C 1 302 ? 23.068  19.799  11.774  1.00 46.78  ? 303 LYS C CG  1 
ATOM   8470  C  CD  . LYS C 1 302 ? 23.562  20.611  10.588  1.00 49.52  ? 303 LYS C CD  1 
ATOM   8471  C  CE  . LYS C 1 302 ? 22.426  20.982  9.653   1.00 49.70  ? 303 LYS C CE  1 
ATOM   8472  N  NZ  . LYS C 1 302 ? 22.905  21.794  8.501   1.00 51.79  ? 303 LYS C NZ  1 
ATOM   8473  N  N   . PHE C 1 303 ? 27.106  17.451  13.144  1.00 53.75  ? 304 PHE C N   1 
ATOM   8474  C  CA  . PHE C 1 303 ? 28.325  17.313  13.931  1.00 53.22  ? 304 PHE C CA  1 
ATOM   8475  C  C   . PHE C 1 303 ? 29.507  17.873  13.147  1.00 46.67  ? 304 PHE C C   1 
ATOM   8476  O  O   . PHE C 1 303 ? 30.482  18.349  13.725  1.00 48.98  ? 304 PHE C O   1 
ATOM   8477  C  CB  . PHE C 1 303 ? 28.585  15.850  14.303  1.00 48.80  ? 304 PHE C CB  1 
ATOM   8478  C  CG  . PHE C 1 303 ? 27.525  15.239  15.180  1.00 46.36  ? 304 PHE C CG  1 
ATOM   8479  C  CD1 . PHE C 1 303 ? 26.581  16.030  15.819  1.00 43.90  ? 304 PHE C CD1 1 
ATOM   8480  C  CD2 . PHE C 1 303 ? 27.480  13.868  15.371  1.00 43.82  ? 304 PHE C CD2 1 
ATOM   8481  C  CE1 . PHE C 1 303 ? 25.611  15.463  16.623  1.00 43.14  ? 304 PHE C CE1 1 
ATOM   8482  C  CE2 . PHE C 1 303 ? 26.513  13.295  16.176  1.00 43.03  ? 304 PHE C CE2 1 
ATOM   8483  C  CZ  . PHE C 1 303 ? 25.577  14.094  16.803  1.00 43.82  ? 304 PHE C CZ  1 
ATOM   8484  N  N   . TRP C 1 304 ? 29.405  17.815  11.823  1.00 51.66  ? 305 TRP C N   1 
ATOM   8485  C  CA  . TRP C 1 304 ? 30.462  18.304  10.947  1.00 48.33  ? 305 TRP C CA  1 
ATOM   8486  C  C   . TRP C 1 304 ? 29.983  19.440  10.053  1.00 51.22  ? 305 TRP C C   1 
ATOM   8487  O  O   . TRP C 1 304 ? 28.788  19.730  9.981   1.00 48.64  ? 305 TRP C O   1 
ATOM   8488  C  CB  . TRP C 1 304 ? 31.003  17.170  10.076  1.00 48.76  ? 305 TRP C CB  1 
ATOM   8489  C  CG  . TRP C 1 304 ? 31.559  16.025  10.853  1.00 56.81  ? 305 TRP C CG  1 
ATOM   8490  C  CD1 . TRP C 1 304 ? 32.852  15.860  11.258  1.00 48.84  ? 305 TRP C CD1 1 
ATOM   8491  C  CD2 . TRP C 1 304 ? 30.842  14.878  11.318  1.00 47.45  ? 305 TRP C CD2 1 
ATOM   8492  N  NE1 . TRP C 1 304 ? 32.983  14.680  11.949  1.00 50.64  ? 305 TRP C NE1 1 
ATOM   8493  C  CE2 . TRP C 1 304 ? 31.763  14.058  12.000  1.00 47.49  ? 305 TRP C CE2 1 
ATOM   8494  C  CE3 . TRP C 1 304 ? 29.510  14.463  11.225  1.00 46.72  ? 305 TRP C CE3 1 
ATOM   8495  C  CZ2 . TRP C 1 304 ? 31.396  12.848  12.584  1.00 51.23  ? 305 TRP C CZ2 1 
ATOM   8496  C  CZ3 . TRP C 1 304 ? 29.146  13.262  11.808  1.00 52.29  ? 305 TRP C CZ3 1 
ATOM   8497  C  CH2 . TRP C 1 304 ? 30.085  12.469  12.479  1.00 51.86  ? 305 TRP C CH2 1 
ATOM   8498  N  N   . GLY C 1 305 ? 30.931  20.082  9.379   1.00 56.94  ? 306 GLY C N   1 
ATOM   8499  C  CA  . GLY C 1 305 ? 30.620  21.080  8.374   1.00 63.22  ? 306 GLY C CA  1 
ATOM   8500  C  C   . GLY C 1 305 ? 30.721  20.454  6.998   1.00 68.50  ? 306 GLY C C   1 
ATOM   8501  O  O   . GLY C 1 305 ? 30.932  19.247  6.877   1.00 68.05  ? 306 GLY C O   1 
ATOM   8502  N  N   . THR C 1 306 ? 30.560  21.264  5.957   1.00 78.30  ? 307 THR C N   1 
ATOM   8503  C  CA  . THR C 1 306 ? 30.624  20.753  4.593   1.00 87.85  ? 307 THR C CA  1 
ATOM   8504  C  C   . THR C 1 306 ? 32.005  20.940  3.957   1.00 95.09  ? 307 THR C C   1 
ATOM   8505  O  O   . THR C 1 306 ? 32.234  20.531  2.818   1.00 97.35  ? 307 THR C O   1 
ATOM   8506  C  CB  . THR C 1 306 ? 29.574  21.426  3.697   1.00 93.35  ? 307 THR C CB  1 
ATOM   8507  O  OG1 . THR C 1 306 ? 28.418  21.757  4.476   1.00 94.06  ? 307 THR C OG1 1 
ATOM   8508  C  CG2 . THR C 1 306 ? 29.163  20.477  2.593   1.00 95.49  ? 307 THR C CG2 1 
ATOM   8509  N  N   . SER C 1 307 ? 32.928  21.546  4.696   1.00 95.94  ? 308 SER C N   1 
ATOM   8510  C  CA  . SER C 1 307 ? 34.236  21.884  4.141   1.00 97.36  ? 308 SER C CA  1 
ATOM   8511  C  C   . SER C 1 307 ? 35.245  20.750  4.302   1.00 96.48  ? 308 SER C C   1 
ATOM   8512  O  O   . SER C 1 307 ? 36.412  20.890  3.933   1.00 98.71  ? 308 SER C O   1 
ATOM   8513  C  CB  . SER C 1 307 ? 34.775  23.160  4.790   1.00 97.63  ? 308 SER C CB  1 
ATOM   8514  O  OG  . SER C 1 307 ? 34.012  24.288  4.398   1.00 97.73  ? 308 SER C OG  1 
ATOM   8515  N  N   . GLY C 1 308 ? 34.792  19.630  4.855   1.00 91.28  ? 309 GLY C N   1 
ATOM   8516  C  CA  . GLY C 1 308 ? 35.623  18.446  4.970   1.00 88.48  ? 309 GLY C CA  1 
ATOM   8517  C  C   . GLY C 1 308 ? 36.640  18.519  6.091   1.00 84.11  ? 309 GLY C C   1 
ATOM   8518  O  O   . GLY C 1 308 ? 37.698  17.893  6.020   1.00 84.81  ? 309 GLY C O   1 
ATOM   8519  N  N   . VAL C 1 309 ? 36.322  19.287  7.127   1.00 80.38  ? 310 VAL C N   1 
ATOM   8520  C  CA  . VAL C 1 309 ? 37.200  19.403  8.283   1.00 77.83  ? 310 VAL C CA  1 
ATOM   8521  C  C   . VAL C 1 309 ? 36.744  18.419  9.362   1.00 74.56  ? 310 VAL C C   1 
ATOM   8522  O  O   . VAL C 1 309 ? 35.720  17.752  9.206   1.00 72.08  ? 310 VAL C O   1 
ATOM   8523  C  CB  . VAL C 1 309 ? 37.193  20.853  8.831   1.00 70.35  ? 310 VAL C CB  1 
ATOM   8524  C  CG1 . VAL C 1 309 ? 38.443  21.151  9.647   1.00 71.80  ? 310 VAL C CG1 1 
ATOM   8525  C  CG2 . VAL C 1 309 ? 37.085  21.840  7.683   1.00 71.79  ? 310 VAL C CG2 1 
ATOM   8526  N  N   . GLU C 1 310 ? 37.497  18.336  10.453  1.00 71.33  ? 311 GLU C N   1 
ATOM   8527  C  CA  . GLU C 1 310 ? 37.078  17.573  11.619  1.00 67.19  ? 311 GLU C CA  1 
ATOM   8528  C  C   . GLU C 1 310 ? 36.013  18.361  12.365  1.00 66.51  ? 311 GLU C C   1 
ATOM   8529  O  O   . GLU C 1 310 ? 35.902  19.574  12.187  1.00 64.64  ? 311 GLU C O   1 
ATOM   8530  C  CB  . GLU C 1 310 ? 38.267  17.270  12.532  1.00 67.91  ? 311 GLU C CB  1 
ATOM   8531  N  N   . SER C 1 311 ? 35.220  17.678  13.183  1.00 61.43  ? 312 SER C N   1 
ATOM   8532  C  CA  . SER C 1 311 ? 34.236  18.364  14.012  1.00 58.14  ? 312 SER C CA  1 
ATOM   8533  C  C   . SER C 1 311 ? 34.941  19.316  14.971  1.00 54.26  ? 312 SER C C   1 
ATOM   8534  O  O   . SER C 1 311 ? 36.060  19.052  15.411  1.00 49.86  ? 312 SER C O   1 
ATOM   8535  C  CB  . SER C 1 311 ? 33.379  17.365  14.787  1.00 47.93  ? 312 SER C CB  1 
ATOM   8536  O  OG  . SER C 1 311 ? 32.492  18.039  15.663  1.00 47.30  ? 312 SER C OG  1 
ATOM   8537  N  N   . VAL C 1 312 ? 34.282  20.424  15.289  1.00 51.18  ? 313 VAL C N   1 
ATOM   8538  C  CA  . VAL C 1 312 ? 34.882  21.465  16.114  1.00 53.66  ? 313 VAL C CA  1 
ATOM   8539  C  C   . VAL C 1 312 ? 34.942  21.049  17.584  1.00 52.30  ? 313 VAL C C   1 
ATOM   8540  O  O   . VAL C 1 312 ? 35.756  21.564  18.351  1.00 53.32  ? 313 VAL C O   1 
ATOM   8541  C  CB  . VAL C 1 312 ? 34.102  22.793  15.980  1.00 53.78  ? 313 VAL C CB  1 
ATOM   8542  C  CG1 . VAL C 1 312 ? 32.735  22.679  16.636  1.00 53.15  ? 313 VAL C CG1 1 
ATOM   8543  C  CG2 . VAL C 1 312 ? 34.894  23.953  16.572  1.00 51.49  ? 313 VAL C CG2 1 
ATOM   8544  N  N   . ILE C 1 313 ? 34.095  20.097  17.961  1.00 52.16  ? 314 ILE C N   1 
ATOM   8545  C  CA  . ILE C 1 313 ? 33.949  19.682  19.353  1.00 50.39  ? 314 ILE C CA  1 
ATOM   8546  C  C   . ILE C 1 313 ? 35.264  19.175  19.951  1.00 52.00  ? 314 ILE C C   1 
ATOM   8547  O  O   . ILE C 1 313 ? 35.495  19.288  21.157  1.00 52.44  ? 314 ILE C O   1 
ATOM   8548  C  CB  . ILE C 1 313 ? 32.863  18.594  19.483  1.00 48.22  ? 314 ILE C CB  1 
ATOM   8549  C  CG1 . ILE C 1 313 ? 31.578  19.054  18.790  1.00 47.18  ? 314 ILE C CG1 1 
ATOM   8550  C  CG2 . ILE C 1 313 ? 32.584  18.267  20.943  1.00 46.48  ? 314 ILE C CG2 1 
ATOM   8551  C  CD1 . ILE C 1 313 ? 30.543  17.965  18.631  1.00 50.26  ? 314 ILE C CD1 1 
ATOM   8552  N  N   . GLY C 1 314 ? 36.134  18.638  19.104  1.00 51.71  ? 315 GLY C N   1 
ATOM   8553  C  CA  . GLY C 1 314 ? 37.421  18.149  19.563  1.00 52.74  ? 315 GLY C CA  1 
ATOM   8554  C  C   . GLY C 1 314 ? 38.611  18.839  18.921  1.00 50.88  ? 315 GLY C C   1 
ATOM   8555  O  O   . GLY C 1 314 ? 39.737  18.351  19.020  1.00 51.68  ? 315 GLY C O   1 
ATOM   8556  N  N   . SER C 1 315 ? 38.372  19.975  18.271  1.00 51.06  ? 316 SER C N   1 
ATOM   8557  C  CA  . SER C 1 315 ? 39.438  20.666  17.547  1.00 57.48  ? 316 SER C CA  1 
ATOM   8558  C  C   . SER C 1 315 ? 39.409  22.188  17.713  1.00 60.70  ? 316 SER C C   1 
ATOM   8559  O  O   . SER C 1 315 ? 39.923  22.915  16.863  1.00 60.31  ? 316 SER C O   1 
ATOM   8560  C  CB  . SER C 1 315 ? 39.369  20.316  16.059  1.00 56.25  ? 316 SER C CB  1 
ATOM   8561  O  OG  . SER C 1 315 ? 38.105  20.650  15.513  1.00 54.83  ? 316 SER C OG  1 
ATOM   8562  N  N   . VAL C 1 316 ? 38.817  22.660  18.808  1.00 61.04  ? 317 VAL C N   1 
ATOM   8563  C  CA  . VAL C 1 316 ? 38.749  24.091  19.113  1.00 52.50  ? 317 VAL C CA  1 
ATOM   8564  C  C   . VAL C 1 316 ? 40.144  24.728  19.163  1.00 64.91  ? 317 VAL C C   1 
ATOM   8565  O  O   . VAL C 1 316 ? 40.352  25.872  18.717  1.00 69.58  ? 317 VAL C O   1 
ATOM   8566  C  CB  . VAL C 1 316 ? 38.025  24.331  20.460  1.00 51.98  ? 317 VAL C CB  1 
ATOM   8567  C  CG1 . VAL C 1 316 ? 38.160  25.778  20.906  1.00 52.67  ? 317 VAL C CG1 1 
ATOM   8568  C  CG2 . VAL C 1 316 ? 36.560  23.934  20.356  1.00 50.88  ? 317 VAL C CG2 1 
ATOM   8569  N  N   . HIS C 1 317 ? 41.097  23.965  19.691  1.00 65.82  ? 318 HIS C N   1 
ATOM   8570  C  CA  . HIS C 1 317 ? 42.471  24.427  19.848  1.00 62.69  ? 318 HIS C CA  1 
ATOM   8571  C  C   . HIS C 1 317 ? 43.094  24.849  18.519  1.00 72.35  ? 318 HIS C C   1 
ATOM   8572  O  O   . HIS C 1 317 ? 43.915  25.767  18.479  1.00 84.63  ? 318 HIS C O   1 
ATOM   8573  C  CB  . HIS C 1 317 ? 43.325  23.340  20.508  1.00 60.70  ? 318 HIS C CB  1 
ATOM   8574  C  CG  . HIS C 1 317 ? 43.256  22.011  19.822  1.00 63.20  ? 318 HIS C CG  1 
ATOM   8575  N  ND1 . HIS C 1 317 ? 42.377  21.020  20.203  1.00 65.94  ? 318 HIS C ND1 1 
ATOM   8576  C  CD2 . HIS C 1 317 ? 43.965  21.505  18.784  1.00 65.81  ? 318 HIS C CD2 1 
ATOM   8577  C  CE1 . HIS C 1 317 ? 42.543  19.964  19.428  1.00 65.43  ? 318 HIS C CE1 1 
ATOM   8578  N  NE2 . HIS C 1 317 ? 43.501  20.232  18.558  1.00 65.54  ? 318 HIS C NE2 1 
ATOM   8579  N  N   . THR C 1 318 ? 42.699  24.185  17.437  1.00 69.45  ? 319 THR C N   1 
ATOM   8580  C  CA  . THR C 1 318 ? 43.186  24.536  16.107  1.00 66.86  ? 319 THR C CA  1 
ATOM   8581  C  C   . THR C 1 318 ? 42.754  25.950  15.734  1.00 64.49  ? 319 THR C C   1 
ATOM   8582  O  O   . THR C 1 318 ? 43.563  26.764  15.276  1.00 65.64  ? 319 THR C O   1 
ATOM   8583  C  CB  . THR C 1 318 ? 42.679  23.551  15.036  1.00 67.19  ? 319 THR C CB  1 
ATOM   8584  O  OG1 . THR C 1 318 ? 41.267  23.720  14.853  1.00 66.96  ? 319 THR C OG1 1 
ATOM   8585  C  CG2 . THR C 1 318 ? 42.968  22.116  15.448  1.00 68.68  ? 319 THR C CG2 1 
ATOM   8586  N  N   . TRP C 1 319 ? 41.474  26.238  15.944  1.00 61.22  ? 320 TRP C N   1 
ATOM   8587  C  CA  . TRP C 1 319 ? 40.924  27.549  15.631  1.00 58.73  ? 320 TRP C CA  1 
ATOM   8588  C  C   . TRP C 1 319 ? 41.524  28.631  16.516  1.00 59.92  ? 320 TRP C C   1 
ATOM   8589  O  O   . TRP C 1 319 ? 41.833  29.730  16.042  1.00 64.00  ? 320 TRP C O   1 
ATOM   8590  C  CB  . TRP C 1 319 ? 39.400  27.537  15.763  1.00 55.24  ? 320 TRP C CB  1 
ATOM   8591  C  CG  . TRP C 1 319 ? 38.742  26.655  14.754  1.00 57.86  ? 320 TRP C CG  1 
ATOM   8592  C  CD1 . TRP C 1 319 ? 38.015  25.525  14.995  1.00 57.74  ? 320 TRP C CD1 1 
ATOM   8593  C  CD2 . TRP C 1 319 ? 38.789  26.806  13.332  1.00 59.05  ? 320 TRP C CD2 1 
ATOM   8594  N  NE1 . TRP C 1 319 ? 37.586  24.978  13.810  1.00 57.78  ? 320 TRP C NE1 1 
ATOM   8595  C  CE2 . TRP C 1 319 ? 38.051  25.744  12.774  1.00 59.60  ? 320 TRP C CE2 1 
ATOM   8596  C  CE3 . TRP C 1 319 ? 39.376  27.743  12.476  1.00 58.29  ? 320 TRP C CE3 1 
ATOM   8597  C  CZ2 . TRP C 1 319 ? 37.884  25.593  11.399  1.00 60.14  ? 320 TRP C CZ2 1 
ATOM   8598  C  CZ3 . TRP C 1 319 ? 39.213  27.590  11.114  1.00 58.25  ? 320 TRP C CZ3 1 
ATOM   8599  C  CH2 . TRP C 1 319 ? 38.471  26.526  10.587  1.00 59.12  ? 320 TRP C CH2 1 
ATOM   8600  N  N   . LEU C 1 320 ? 41.697  28.321  17.798  1.00 56.61  ? 321 LEU C N   1 
ATOM   8601  C  CA  . LEU C 1 320 ? 42.324  29.274  18.712  1.00 62.45  ? 321 LEU C CA  1 
ATOM   8602  C  C   . LEU C 1 320 ? 43.754  29.606  18.268  1.00 58.73  ? 321 LEU C C   1 
ATOM   8603  O  O   . LEU C 1 320 ? 44.139  30.781  18.168  1.00 69.17  ? 321 LEU C O   1 
ATOM   8604  C  CB  . LEU C 1 320 ? 42.321  28.725  20.139  1.00 60.55  ? 321 LEU C CB  1 
ATOM   8605  C  CG  . LEU C 1 320 ? 40.938  28.412  20.715  1.00 60.12  ? 321 LEU C CG  1 
ATOM   8606  C  CD1 . LEU C 1 320 ? 41.034  28.005  22.177  1.00 58.12  ? 321 LEU C CD1 1 
ATOM   8607  C  CD2 . LEU C 1 320 ? 40.001  29.600  20.545  1.00 58.77  ? 321 LEU C CD2 1 
ATOM   8608  N  N   . ALA C 1 321 ? 44.528  28.561  17.988  1.00 58.94  ? 322 ALA C N   1 
ATOM   8609  C  CA  . ALA C 1 321 ? 45.908  28.717  17.544  1.00 65.61  ? 322 ALA C CA  1 
ATOM   8610  C  C   . ALA C 1 321 ? 45.995  29.528  16.255  1.00 67.90  ? 322 ALA C C   1 
ATOM   8611  O  O   . ALA C 1 321 ? 46.851  30.409  16.124  1.00 71.06  ? 322 ALA C O   1 
ATOM   8612  C  CB  . ALA C 1 321 ? 46.558  27.356  17.355  1.00 66.71  ? 322 ALA C CB  1 
ATOM   8613  N  N   . GLU C 1 322 ? 45.109  29.234  15.306  1.00 65.71  ? 323 GLU C N   1 
ATOM   8614  C  CA  . GLU C 1 322 ? 45.095  29.968  14.044  1.00 70.30  ? 323 GLU C CA  1 
ATOM   8615  C  C   . GLU C 1 322 ? 44.732  31.432  14.277  1.00 72.25  ? 323 GLU C C   1 
ATOM   8616  O  O   . GLU C 1 322 ? 45.241  32.325  13.590  1.00 73.91  ? 323 GLU C O   1 
ATOM   8617  C  CB  . GLU C 1 322 ? 44.125  29.330  13.048  1.00 72.83  ? 323 GLU C CB  1 
ATOM   8618  C  CG  . GLU C 1 322 ? 44.154  29.980  11.671  1.00 78.35  ? 323 GLU C CG  1 
ATOM   8619  C  CD  . GLU C 1 322 ? 43.385  29.193  10.629  1.00 82.97  ? 323 GLU C CD  1 
ATOM   8620  O  OE1 . GLU C 1 322 ? 43.058  28.016  10.890  1.00 82.63  ? 323 GLU C OE1 1 
ATOM   8621  O  OE2 . GLU C 1 322 ? 43.112  29.751  9.545   1.00 86.12  ? 323 GLU C OE2 1 
ATOM   8622  N  N   . ALA C 1 323 ? 43.859  31.676  15.251  1.00 69.76  ? 324 ALA C N   1 
ATOM   8623  C  CA  . ALA C 1 323 ? 43.528  33.044  15.638  1.00 69.16  ? 324 ALA C CA  1 
ATOM   8624  C  C   . ALA C 1 323 ? 44.770  33.771  16.148  1.00 72.75  ? 324 ALA C C   1 
ATOM   8625  O  O   . ALA C 1 323 ? 45.054  34.904  15.735  1.00 75.27  ? 324 ALA C O   1 
ATOM   8626  C  CB  . ALA C 1 323 ? 42.437  33.053  16.692  1.00 67.87  ? 324 ALA C CB  1 
ATOM   8627  N  N   . ILE C 1 324 ? 45.515  33.115  17.036  1.00 73.58  ? 325 ILE C N   1 
ATOM   8628  C  CA  . ILE C 1 324 ? 46.741  33.707  17.572  1.00 73.83  ? 325 ILE C CA  1 
ATOM   8629  C  C   . ILE C 1 324 ? 47.757  34.012  16.467  1.00 77.43  ? 325 ILE C C   1 
ATOM   8630  O  O   . ILE C 1 324 ? 48.310  35.116  16.409  1.00 79.45  ? 325 ILE C O   1 
ATOM   8631  C  CB  . ILE C 1 324 ? 47.406  32.796  18.619  1.00 71.50  ? 325 ILE C CB  1 
ATOM   8632  C  CG1 . ILE C 1 324 ? 46.431  32.488  19.756  1.00 70.53  ? 325 ILE C CG1 1 
ATOM   8633  C  CG2 . ILE C 1 324 ? 48.662  33.454  19.170  1.00 70.15  ? 325 ILE C CG2 1 
ATOM   8634  C  CD1 . ILE C 1 324 ? 47.034  31.655  20.869  1.00 70.36  ? 325 ILE C CD1 1 
ATOM   8635  N  N   . ASN C 1 325 ? 47.997  33.033  15.596  1.00 80.95  ? 326 ASN C N   1 
ATOM   8636  C  CA  . ASN C 1 325 ? 48.903  33.215  14.463  1.00 80.83  ? 326 ASN C CA  1 
ATOM   8637  C  C   . ASN C 1 325 ? 48.501  34.393  13.583  1.00 79.64  ? 326 ASN C C   1 
ATOM   8638  O  O   . ASN C 1 325 ? 49.332  35.246  13.246  1.00 84.11  ? 326 ASN C O   1 
ATOM   8639  C  CB  . ASN C 1 325 ? 48.966  31.941  13.616  1.00 85.77  ? 326 ASN C CB  1 
ATOM   8640  C  CG  . ASN C 1 325 ? 49.906  30.904  14.193  1.00 89.12  ? 326 ASN C CG  1 
ATOM   8641  O  OD1 . ASN C 1 325 ? 50.179  30.898  15.390  1.00 89.78  ? 326 ASN C OD1 1 
ATOM   8642  N  ND2 . ASN C 1 325 ? 50.409  30.019  13.339  1.00 91.71  ? 326 ASN C ND2 1 
ATOM   8643  N  N   . ALA C 1 326 ? 47.221  34.432  13.220  1.00 75.13  ? 327 ALA C N   1 
ATOM   8644  C  CA  . ALA C 1 326 ? 46.683  35.520  12.412  1.00 75.09  ? 327 ALA C CA  1 
ATOM   8645  C  C   . ALA C 1 326 ? 46.939  36.864  13.083  1.00 75.66  ? 327 ALA C C   1 
ATOM   8646  O  O   . ALA C 1 326 ? 47.383  37.817  12.435  1.00 78.25  ? 327 ALA C O   1 
ATOM   8647  C  CB  . ALA C 1 326 ? 45.197  35.319  12.172  1.00 70.95  ? 327 ALA C CB  1 
ATOM   8648  N  N   . LEU C 1 327 ? 46.673  36.928  14.385  1.00 77.50  ? 328 LEU C N   1 
ATOM   8649  C  CA  . LEU C 1 327 ? 46.922  38.144  15.153  1.00 79.69  ? 328 LEU C CA  1 
ATOM   8650  C  C   . LEU C 1 327 ? 48.381  38.590  15.082  1.00 84.20  ? 328 LEU C C   1 
ATOM   8651  O  O   . LEU C 1 327 ? 48.684  39.697  14.622  1.00 81.27  ? 328 LEU C O   1 
ATOM   8652  C  CB  . LEU C 1 327 ? 46.525  37.945  16.617  1.00 81.51  ? 328 LEU C CB  1 
ATOM   8653  C  CG  . LEU C 1 327 ? 46.929  39.100  17.537  1.00 82.76  ? 328 LEU C CG  1 
ATOM   8654  C  CD1 . LEU C 1 327 ? 46.130  40.353  17.211  1.00 83.92  ? 328 LEU C CD1 1 
ATOM   8655  C  CD2 . LEU C 1 327 ? 46.781  38.726  19.005  1.00 83.35  ? 328 LEU C CD2 1 
ATOM   8656  N  N   . GLN C 1 328 ? 49.281  37.721  15.532  1.00 89.29  ? 329 GLN C N   1 
ATOM   8657  C  CA  . GLN C 1 328 ? 50.684  38.096  15.672  1.00 99.06  ? 329 GLN C CA  1 
ATOM   8658  C  C   . GLN C 1 328 ? 51.350  38.363  14.323  1.00 108.16 ? 329 GLN C C   1 
ATOM   8659  O  O   . GLN C 1 328 ? 52.327  39.112  14.250  1.00 111.07 ? 329 GLN C O   1 
ATOM   8660  C  CB  . GLN C 1 328 ? 51.458  37.014  16.433  1.00 95.73  ? 329 GLN C CB  1 
ATOM   8661  C  CG  . GLN C 1 328 ? 52.331  36.137  15.554  1.00 95.27  ? 329 GLN C CG  1 
ATOM   8662  C  CD  . GLN C 1 328 ? 53.119  35.117  16.345  1.00 94.21  ? 329 GLN C CD  1 
ATOM   8663  O  OE1 . GLN C 1 328 ? 52.733  34.736  17.449  1.00 93.66  ? 329 GLN C OE1 1 
ATOM   8664  N  NE2 . GLN C 1 328 ? 54.236  34.671  15.783  1.00 93.44  ? 329 GLN C NE2 1 
ATOM   8665  N  N   . ASP C 1 329 ? 50.817  37.766  13.257  1.00 116.72 ? 330 ASP C N   1 
ATOM   8666  C  CA  . ASP C 1 329 ? 51.421  37.917  11.940  1.00 121.01 ? 330 ASP C CA  1 
ATOM   8667  C  C   . ASP C 1 329 ? 50.869  39.242  11.395  1.00 117.82 ? 330 ASP C C   1 
ATOM   8668  O  O   . ASP C 1 329 ? 51.580  39.994  10.736  1.00 122.98 ? 330 ASP C O   1 
ATOM   8669  C  CB  . ASP C 1 329 ? 51.088  36.710  11.039  1.00 126.57 ? 330 ASP C CB  1 
ATOM   8670  C  CG  . ASP C 1 329 ? 51.618  36.841  9.599   1.00 134.26 ? 330 ASP C CG  1 
ATOM   8671  O  OD1 . ASP C 1 329 ? 52.120  37.910  9.191   1.00 136.84 ? 330 ASP C OD1 1 
ATOM   8672  O  OD2 . ASP C 1 329 ? 51.582  35.812  8.884   1.00 135.05 ? 330 ASP C OD2 1 
ATOM   8673  N  N   . ASN C 1 330 ? 49.618  39.558  11.726  1.00 109.97 ? 331 ASN C N   1 
ATOM   8674  C  CA  . ASN C 1 330 ? 49.039  40.838  11.308  1.00 107.22 ? 331 ASN C CA  1 
ATOM   8675  C  C   . ASN C 1 330 ? 49.414  42.003  12.228  1.00 103.93 ? 331 ASN C C   1 
ATOM   8676  O  O   . ASN C 1 330 ? 48.974  43.129  12.009  1.00 103.80 ? 331 ASN C O   1 
ATOM   8677  C  CB  . ASN C 1 330 ? 47.512  40.735  11.212  1.00 101.94 ? 331 ASN C CB  1 
ATOM   8678  C  CG  . ASN C 1 330 ? 47.040  40.389  9.812   1.00 99.27  ? 331 ASN C CG  1 
ATOM   8679  O  OD1 . ASN C 1 330 ? 47.803  39.861  9.003   1.00 98.79  ? 331 ASN C OD1 1 
ATOM   8680  N  ND2 . ASN C 1 330 ? 45.781  40.693  9.517   1.00 95.73  ? 331 ASN C ND2 1 
ATOM   8681  N  N   . ARG C 1 331 ? 50.247  41.724  13.229  1.00 104.49 ? 332 ARG C N   1 
ATOM   8682  C  CA  . ARG C 1 331 ? 50.605  42.686  14.280  1.00 104.49 ? 332 ARG C CA  1 
ATOM   8683  C  C   . ARG C 1 331 ? 50.943  44.113  13.824  1.00 106.94 ? 332 ARG C C   1 
ATOM   8684  O  O   . ARG C 1 331 ? 50.384  45.077  14.347  1.00 107.23 ? 332 ARG C O   1 
ATOM   8685  C  CB  . ARG C 1 331 ? 51.789  42.144  15.085  1.00 103.70 ? 332 ARG C CB  1 
ATOM   8686  N  N   . ASP C 1 332 ? 51.856  44.249  12.866  1.00 106.97 ? 333 ASP C N   1 
ATOM   8687  C  CA  . ASP C 1 332 ? 52.355  45.566  12.465  1.00 111.27 ? 333 ASP C CA  1 
ATOM   8688  C  C   . ASP C 1 332 ? 51.285  46.446  11.810  1.00 115.05 ? 333 ASP C C   1 
ATOM   8689  O  O   . ASP C 1 332 ? 51.031  47.570  12.256  1.00 117.53 ? 333 ASP C O   1 
ATOM   8690  C  CB  . ASP C 1 332 ? 53.548  45.414  11.516  1.00 107.05 ? 333 ASP C CB  1 
ATOM   8691  C  CG  . ASP C 1 332 ? 54.786  44.882  12.216  1.00 104.09 ? 333 ASP C CG  1 
ATOM   8692  O  OD1 . ASP C 1 332 ? 54.827  44.917  13.464  1.00 101.37 ? 333 ASP C OD1 1 
ATOM   8693  O  OD2 . ASP C 1 332 ? 55.720  44.432  11.519  1.00 104.01 ? 333 ASP C OD2 1 
ATOM   8694  N  N   . THR C 1 333 ? 50.662  45.940  10.752  1.00 118.20 ? 334 THR C N   1 
ATOM   8695  C  CA  . THR C 1 333 ? 49.637  46.705  10.050  1.00 120.33 ? 334 THR C CA  1 
ATOM   8696  C  C   . THR C 1 333 ? 48.387  46.856  10.913  1.00 120.42 ? 334 THR C C   1 
ATOM   8697  O  O   . THR C 1 333 ? 47.614  47.799  10.740  1.00 120.90 ? 334 THR C O   1 
ATOM   8698  C  CB  . THR C 1 333 ? 49.261  46.053  8.709   1.00 122.19 ? 334 THR C CB  1 
ATOM   8699  O  OG1 . THR C 1 333 ? 48.496  44.865  8.946   1.00 120.83 ? 334 THR C OG1 1 
ATOM   8700  C  CG2 . THR C 1 333 ? 50.512  45.708  7.917   1.00 123.40 ? 334 THR C CG2 1 
ATOM   8701  N  N   . LEU C 1 334 ? 48.193  45.922  11.839  1.00 117.96 ? 335 LEU C N   1 
ATOM   8702  C  CA  . LEU C 1 334 ? 47.120  46.034  12.821  1.00 116.81 ? 335 LEU C CA  1 
ATOM   8703  C  C   . LEU C 1 334 ? 47.357  47.233  13.727  1.00 120.96 ? 335 LEU C C   1 
ATOM   8704  O  O   . LEU C 1 334 ? 46.458  48.045  13.948  1.00 121.07 ? 335 LEU C O   1 
ATOM   8705  C  CB  . LEU C 1 334 ? 47.017  44.760  13.660  1.00 110.65 ? 335 LEU C CB  1 
ATOM   8706  C  CG  . LEU C 1 334 ? 46.491  44.903  15.090  1.00 106.76 ? 335 LEU C CG  1 
ATOM   8707  C  CD1 . LEU C 1 334 ? 44.987  45.137  15.107  1.00 105.24 ? 335 LEU C CD1 1 
ATOM   8708  C  CD2 . LEU C 1 334 ? 46.868  43.687  15.922  1.00 106.01 ? 335 LEU C CD2 1 
ATOM   8709  N  N   . THR C 1 335 ? 48.576  47.340  14.246  1.00 124.37 ? 336 THR C N   1 
ATOM   8710  C  CA  . THR C 1 335 ? 48.915  48.405  15.180  1.00 128.59 ? 336 THR C CA  1 
ATOM   8711  C  C   . THR C 1 335 ? 49.210  49.707  14.442  1.00 134.12 ? 336 THR C C   1 
ATOM   8712  O  O   . THR C 1 335 ? 49.464  50.738  15.065  1.00 137.47 ? 336 THR C O   1 
ATOM   8713  C  CB  . THR C 1 335 ? 50.124  48.023  16.062  1.00 127.73 ? 336 THR C CB  1 
ATOM   8714  O  OG1 . THR C 1 335 ? 50.170  48.876  17.213  1.00 129.83 ? 336 THR C OG1 1 
ATOM   8715  C  CG2 . THR C 1 335 ? 51.427  48.147  15.288  1.00 129.49 ? 336 THR C CG2 1 
ATOM   8716  N  N   . ALA C 1 336 ? 49.175  49.655  13.113  1.00 137.26 ? 337 ALA C N   1 
ATOM   8717  C  CA  . ALA C 1 336 ? 49.293  50.865  12.306  1.00 136.82 ? 337 ALA C CA  1 
ATOM   8718  C  C   . ALA C 1 336 ? 48.133  51.820  12.587  1.00 133.52 ? 337 ALA C C   1 
ATOM   8719  O  O   . ALA C 1 336 ? 48.293  53.039  12.524  1.00 138.37 ? 337 ALA C O   1 
ATOM   8720  C  CB  . ALA C 1 336 ? 49.348  50.517  10.826  1.00 139.68 ? 337 ALA C CB  1 
ATOM   8721  N  N   . LYS C 1 337 ? 46.968  51.259  12.903  1.00 116.49 ? 338 LYS C N   1 
ATOM   8722  C  CA  . LYS C 1 337 ? 45.782  52.055  13.209  1.00 110.63 ? 338 LYS C CA  1 
ATOM   8723  C  C   . LYS C 1 337 ? 45.950  52.840  14.510  1.00 107.99 ? 338 LYS C C   1 
ATOM   8724  O  O   . LYS C 1 337 ? 46.301  52.265  15.542  1.00 107.26 ? 338 LYS C O   1 
ATOM   8725  C  CB  . LYS C 1 337 ? 44.546  51.159  13.294  1.00 105.95 ? 338 LYS C CB  1 
ATOM   8726  N  N   . VAL C 1 338 ? 45.675  54.146  14.435  1.00 109.01 ? 339 VAL C N   1 
ATOM   8727  C  CA  . VAL C 1 338 ? 45.852  55.117  15.527  1.00 105.79 ? 339 VAL C CA  1 
ATOM   8728  C  C   . VAL C 1 338 ? 46.922  54.743  16.551  1.00 108.04 ? 339 VAL C C   1 
ATOM   8729  O  O   . VAL C 1 338 ? 48.113  54.946  16.320  1.00 109.02 ? 339 VAL C O   1 
ATOM   8730  C  CB  . VAL C 1 338 ? 44.527  55.363  16.288  1.00 102.14 ? 339 VAL C CB  1 
ATOM   8731  C  CG1 . VAL C 1 338 ? 43.377  55.555  15.311  1.00 99.47  ? 339 VAL C CG1 1 
ATOM   8732  C  CG2 . VAL C 1 338 ? 44.235  54.218  17.247  1.00 97.82  ? 339 VAL C CG2 1 
ATOM   8733  N  N   . ARG C 1 366 ? 41.774  21.084  10.707  1.00 83.80  ? 367 ARG C N   1 
ATOM   8734  C  CA  . ARG C 1 366 ? 42.676  20.036  10.246  1.00 84.49  ? 367 ARG C CA  1 
ATOM   8735  C  C   . ARG C 1 366 ? 41.944  19.030  9.363   1.00 88.11  ? 367 ARG C C   1 
ATOM   8736  O  O   . ARG C 1 366 ? 40.719  19.056  9.263   1.00 88.06  ? 367 ARG C O   1 
ATOM   8737  C  CB  . ARG C 1 366 ? 43.322  19.322  11.435  1.00 83.82  ? 367 ARG C CB  1 
ATOM   8738  N  N   . GLU C 1 367 ? 42.702  18.142  8.728   1.00 90.11  ? 368 GLU C N   1 
ATOM   8739  C  CA  . GLU C 1 367 ? 42.133  17.165  7.807   1.00 89.21  ? 368 GLU C CA  1 
ATOM   8740  C  C   . GLU C 1 367 ? 41.171  16.210  8.506   1.00 89.59  ? 368 GLU C C   1 
ATOM   8741  O  O   . GLU C 1 367 ? 41.447  15.725  9.603   1.00 88.70  ? 368 GLU C O   1 
ATOM   8742  C  CB  . GLU C 1 367 ? 43.247  16.369  7.123   1.00 90.64  ? 368 GLU C CB  1 
ATOM   8743  N  N   . ARG C 1 368 ? 40.036  15.951  7.864   1.00 91.69  ? 369 ARG C N   1 
ATOM   8744  C  CA  . ARG C 1 368 ? 39.071  14.988  8.377   1.00 92.66  ? 369 ARG C CA  1 
ATOM   8745  C  C   . ARG C 1 368 ? 39.362  13.603  7.816   1.00 94.33  ? 369 ARG C C   1 
ATOM   8746  O  O   . ARG C 1 368 ? 39.438  13.426  6.600   1.00 95.31  ? 369 ARG C O   1 
ATOM   8747  C  CB  . ARG C 1 368 ? 37.642  15.407  8.029   1.00 91.89  ? 369 ARG C CB  1 
ATOM   8748  N  N   . PRO C 1 369 ? 39.528  12.614  8.706   1.00 93.95  ? 370 PRO C N   1 
ATOM   8749  C  CA  . PRO C 1 369 ? 39.795  11.231  8.301   1.00 91.86  ? 370 PRO C CA  1 
ATOM   8750  C  C   . PRO C 1 369 ? 38.638  10.662  7.487   1.00 88.59  ? 370 PRO C C   1 
ATOM   8751  O  O   . PRO C 1 369 ? 37.534  11.203  7.565   1.00 85.66  ? 370 PRO C O   1 
ATOM   8752  C  CB  . PRO C 1 369 ? 39.942  10.490  9.639   1.00 94.46  ? 370 PRO C CB  1 
ATOM   8753  C  CG  . PRO C 1 369 ? 40.193  11.557  10.657  1.00 94.23  ? 370 PRO C CG  1 
ATOM   8754  C  CD  . PRO C 1 369 ? 39.449  12.756  10.169  1.00 92.72  ? 370 PRO C CD  1 
ATOM   8755  N  N   . PRO C 1 370 ? 38.887  9.598   6.706   1.00 84.35  ? 371 PRO C N   1 
ATOM   8756  C  CA  . PRO C 1 370 ? 37.791  8.920   6.005   1.00 82.39  ? 371 PRO C CA  1 
ATOM   8757  C  C   . PRO C 1 370 ? 36.714  8.498   6.997   1.00 76.68  ? 371 PRO C C   1 
ATOM   8758  O  O   . PRO C 1 370 ? 35.521  8.599   6.710   1.00 76.93  ? 371 PRO C O   1 
ATOM   8759  C  CB  . PRO C 1 370 ? 38.473  7.706   5.359   1.00 83.02  ? 371 PRO C CB  1 
ATOM   8760  C  CG  . PRO C 1 370 ? 39.781  7.557   6.079   1.00 85.02  ? 371 PRO C CG  1 
ATOM   8761  C  CD  . PRO C 1 370 ? 40.183  8.945   6.461   1.00 84.18  ? 371 PRO C CD  1 
ATOM   8762  N  N   . SER C 1 371 ? 37.151  8.028   8.160   1.00 76.69  ? 372 SER C N   1 
ATOM   8763  C  CA  . SER C 1 371 ? 36.265  7.840   9.299   1.00 75.46  ? 372 SER C CA  1 
ATOM   8764  C  C   . SER C 1 371 ? 37.040  8.044   10.596  1.00 75.69  ? 372 SER C C   1 
ATOM   8765  O  O   . SER C 1 371 ? 38.208  7.671   10.699  1.00 80.93  ? 372 SER C O   1 
ATOM   8766  C  CB  . SER C 1 371 ? 35.623  6.452   9.272   1.00 77.04  ? 372 SER C CB  1 
ATOM   8767  O  OG  . SER C 1 371 ? 36.575  5.443   9.555   1.00 77.85  ? 372 SER C OG  1 
ATOM   8768  N  N   . GLY C 1 372 ? 36.383  8.642   11.582  1.00 71.13  ? 373 GLY C N   1 
ATOM   8769  C  CA  . GLY C 1 372 ? 36.966  8.806   12.900  1.00 64.30  ? 373 GLY C CA  1 
ATOM   8770  C  C   . GLY C 1 372 ? 36.087  8.107   13.915  1.00 58.00  ? 373 GLY C C   1 
ATOM   8771  O  O   . GLY C 1 372 ? 35.092  7.485   13.544  1.00 56.56  ? 373 GLY C O   1 
ATOM   8772  N  N   . THR C 1 373 ? 36.452  8.203   15.190  1.00 52.20  ? 374 THR C N   1 
ATOM   8773  C  CA  . THR C 1 373 ? 35.666  7.605   16.264  1.00 48.45  ? 374 THR C CA  1 
ATOM   8774  C  C   . THR C 1 373 ? 34.209  8.063   16.204  1.00 47.23  ? 374 THR C C   1 
ATOM   8775  O  O   . THR C 1 373 ? 33.281  7.243   16.213  1.00 51.40  ? 374 THR C O   1 
ATOM   8776  C  CB  . THR C 1 373 ? 36.251  7.953   17.645  1.00 48.56  ? 374 THR C CB  1 
ATOM   8777  O  OG1 . THR C 1 373 ? 37.548  7.360   17.780  1.00 51.90  ? 374 THR C OG1 1 
ATOM   8778  C  CG2 . THR C 1 373 ? 35.348  7.436   18.753  1.00 47.61  ? 374 THR C CG2 1 
ATOM   8779  N  N   . LEU C 1 374 ? 34.023  9.378   16.123  1.00 47.05  ? 375 LEU C N   1 
ATOM   8780  C  CA  . LEU C 1 374 ? 32.693  9.969   16.079  1.00 53.31  ? 375 LEU C CA  1 
ATOM   8781  C  C   . LEU C 1 374 ? 31.899  9.474   14.875  1.00 54.55  ? 375 LEU C C   1 
ATOM   8782  O  O   . LEU C 1 374 ? 30.714  9.173   14.994  1.00 56.43  ? 375 LEU C O   1 
ATOM   8783  C  CB  . LEU C 1 374 ? 32.784  11.496  16.052  1.00 46.23  ? 375 LEU C CB  1 
ATOM   8784  C  CG  . LEU C 1 374 ? 31.446  12.237  16.065  1.00 45.68  ? 375 LEU C CG  1 
ATOM   8785  C  CD1 . LEU C 1 374 ? 30.623  11.823  17.274  1.00 44.55  ? 375 LEU C CD1 1 
ATOM   8786  C  CD2 . LEU C 1 374 ? 31.657  13.743  16.044  1.00 45.76  ? 375 LEU C CD2 1 
ATOM   8787  N  N   . GLU C 1 375 ? 32.555  9.380   13.722  1.00 46.85  ? 376 GLU C N   1 
ATOM   8788  C  CA  . GLU C 1 375 ? 31.885  8.934   12.504  1.00 53.53  ? 376 GLU C CA  1 
ATOM   8789  C  C   . GLU C 1 375 ? 31.456  7.472   12.594  1.00 50.42  ? 376 GLU C C   1 
ATOM   8790  O  O   . GLU C 1 375 ? 30.352  7.121   12.177  1.00 50.43  ? 376 GLU C O   1 
ATOM   8791  C  CB  . GLU C 1 375 ? 32.782  9.138   11.282  1.00 57.13  ? 376 GLU C CB  1 
ATOM   8792  C  CG  . GLU C 1 375 ? 32.178  8.601   9.992   1.00 62.49  ? 376 GLU C CG  1 
ATOM   8793  C  CD  . GLU C 1 375 ? 32.715  9.290   8.754   1.00 71.05  ? 376 GLU C CD  1 
ATOM   8794  O  OE1 . GLU C 1 375 ? 33.550  10.208  8.894   1.00 72.74  ? 376 GLU C OE1 1 
ATOM   8795  O  OE2 . GLU C 1 375 ? 32.300  8.912   7.638   1.00 73.45  ? 376 GLU C OE2 1 
ATOM   8796  N  N   . LYS C 1 376 ? 32.328  6.623   13.131  1.00 47.75  ? 377 LYS C N   1 
ATOM   8797  C  CA  . LYS C 1 376 ? 31.996  5.214   13.319  1.00 48.04  ? 377 LYS C CA  1 
ATOM   8798  C  C   . LYS C 1 376 ? 30.807  5.078   14.265  1.00 45.63  ? 377 LYS C C   1 
ATOM   8799  O  O   . LYS C 1 376 ? 29.849  4.340   13.987  1.00 45.78  ? 377 LYS C O   1 
ATOM   8800  C  CB  . LYS C 1 376 ? 33.202  4.440   13.856  1.00 48.59  ? 377 LYS C CB  1 
ATOM   8801  C  CG  . LYS C 1 376 ? 34.388  4.408   12.907  1.00 49.14  ? 377 LYS C CG  1 
ATOM   8802  C  CD  . LYS C 1 376 ? 35.510  3.540   13.451  1.00 55.25  ? 377 LYS C CD  1 
ATOM   8803  C  CE  . LYS C 1 376 ? 36.774  3.680   12.616  1.00 51.61  ? 377 LYS C CE  1 
ATOM   8804  N  NZ  . LYS C 1 376 ? 36.547  3.314   11.192  1.00 52.23  ? 377 LYS C NZ  1 
ATOM   8805  N  N   . LEU C 1 377 ? 30.874  5.809   15.376  1.00 49.54  ? 378 LEU C N   1 
ATOM   8806  C  CA  . LEU C 1 377 ? 29.767  5.872   16.325  1.00 47.03  ? 378 LEU C CA  1 
ATOM   8807  C  C   . LEU C 1 377 ? 28.472  6.298   15.643  1.00 45.20  ? 378 LEU C C   1 
ATOM   8808  O  O   . LEU C 1 377 ? 27.401  5.788   15.961  1.00 42.79  ? 378 LEU C O   1 
ATOM   8809  C  CB  . LEU C 1 377 ? 30.087  6.837   17.467  1.00 45.85  ? 378 LEU C CB  1 
ATOM   8810  C  CG  . LEU C 1 377 ? 31.100  6.379   18.515  1.00 47.49  ? 378 LEU C CG  1 
ATOM   8811  C  CD1 . LEU C 1 377 ? 31.205  7.418   19.618  1.00 44.29  ? 378 LEU C CD1 1 
ATOM   8812  C  CD2 . LEU C 1 377 ? 30.709  5.023   19.081  1.00 46.34  ? 378 LEU C CD2 1 
ATOM   8813  N  N   . VAL C 1 378 ? 28.581  7.234   14.705  1.00 46.58  ? 379 VAL C N   1 
ATOM   8814  C  CA  . VAL C 1 378 ? 27.418  7.758   13.996  1.00 49.13  ? 379 VAL C CA  1 
ATOM   8815  C  C   . VAL C 1 378 ? 26.828  6.728   13.033  1.00 47.38  ? 379 VAL C C   1 
ATOM   8816  O  O   . VAL C 1 378 ? 25.611  6.594   12.940  1.00 51.41  ? 379 VAL C O   1 
ATOM   8817  C  CB  . VAL C 1 378 ? 27.769  9.055   13.228  1.00 50.30  ? 379 VAL C CB  1 
ATOM   8818  C  CG1 . VAL C 1 378 ? 26.751  9.338   12.131  1.00 44.14  ? 379 VAL C CG1 1 
ATOM   8819  C  CG2 . VAL C 1 378 ? 27.855  10.229  14.192  1.00 47.14  ? 379 VAL C CG2 1 
ATOM   8820  N  N   . SER C 1 379 ? 27.685  6.000   12.323  1.00 44.45  ? 380 SER C N   1 
ATOM   8821  C  CA  . SER C 1 379 ? 27.218  4.933   11.441  1.00 44.70  ? 380 SER C CA  1 
ATOM   8822  C  C   . SER C 1 379 ? 26.488  3.866   12.251  1.00 50.75  ? 380 SER C C   1 
ATOM   8823  O  O   . SER C 1 379 ? 25.350  3.480   11.929  1.00 52.31  ? 380 SER C O   1 
ATOM   8824  C  CB  . SER C 1 379 ? 28.387  4.310   10.674  1.00 45.89  ? 380 SER C CB  1 
ATOM   8825  O  OG  . SER C 1 379 ? 28.906  5.207   9.708   1.00 50.17  ? 380 SER C OG  1 
ATOM   8826  N  N   . GLU C 1 380 ? 27.150  3.407   13.312  1.00 50.23  ? 381 GLU C N   1 
ATOM   8827  C  CA  . GLU C 1 380 ? 26.566  2.430   14.226  1.00 51.17  ? 381 GLU C CA  1 
ATOM   8828  C  C   . GLU C 1 380 ? 25.199  2.888   14.734  1.00 46.69  ? 381 GLU C C   1 
ATOM   8829  O  O   . GLU C 1 380 ? 24.213  2.152   14.650  1.00 41.99  ? 381 GLU C O   1 
ATOM   8830  C  CB  . GLU C 1 380 ? 27.509  2.180   15.406  1.00 58.46  ? 381 GLU C CB  1 
ATOM   8831  C  CG  . GLU C 1 380 ? 26.965  1.224   16.456  1.00 67.59  ? 381 GLU C CG  1 
ATOM   8832  C  CD  . GLU C 1 380 ? 26.902  -0.210  15.969  1.00 75.63  ? 381 GLU C CD  1 
ATOM   8833  O  OE1 . GLU C 1 380 ? 27.633  -0.551  15.015  1.00 79.96  ? 381 GLU C OE1 1 
ATOM   8834  O  OE2 . GLU C 1 380 ? 26.122  -0.999  16.544  1.00 77.21  ? 381 GLU C OE2 1 
ATOM   8835  N  N   . ALA C 1 381 ? 25.153  4.116   15.244  1.00 45.88  ? 382 ALA C N   1 
ATOM   8836  C  CA  . ALA C 1 381 ? 23.932  4.692   15.798  1.00 46.86  ? 382 ALA C CA  1 
ATOM   8837  C  C   . ALA C 1 381 ? 22.817  4.764   14.761  1.00 45.95  ? 382 ALA C C   1 
ATOM   8838  O  O   . ALA C 1 381 ? 21.671  4.433   15.055  1.00 49.80  ? 382 ALA C O   1 
ATOM   8839  C  CB  . ALA C 1 381 ? 24.212  6.074   16.365  1.00 41.05  ? 382 ALA C CB  1 
ATOM   8840  N  N   . LYS C 1 382 ? 23.160  5.206   13.554  1.00 41.63  ? 383 LYS C N   1 
ATOM   8841  C  CA  . LYS C 1 382 ? 22.215  5.247   12.443  1.00 41.78  ? 383 LYS C CA  1 
ATOM   8842  C  C   . LYS C 1 382 ? 21.611  3.874   12.192  1.00 46.72  ? 383 LYS C C   1 
ATOM   8843  O  O   . LYS C 1 382 ? 20.388  3.728   12.110  1.00 41.27  ? 383 LYS C O   1 
ATOM   8844  C  CB  . LYS C 1 382 ? 22.895  5.745   11.168  1.00 42.74  ? 383 LYS C CB  1 
ATOM   8845  C  CG  . LYS C 1 382 ? 23.034  7.250   11.053  1.00 45.75  ? 383 LYS C CG  1 
ATOM   8846  C  CD  . LYS C 1 382 ? 23.414  7.626   9.629   1.00 50.72  ? 383 LYS C CD  1 
ATOM   8847  C  CE  . LYS C 1 382 ? 23.749  9.099   9.503   1.00 53.39  ? 383 LYS C CE  1 
ATOM   8848  N  NZ  . LYS C 1 382 ? 24.184  9.442   8.120   1.00 58.73  ? 383 LYS C NZ  1 
ATOM   8849  N  N   . ALA C 1 383 ? 22.477  2.871   12.071  1.00 47.84  ? 384 ALA C N   1 
ATOM   8850  C  CA  . ALA C 1 383 ? 22.023  1.501   11.848  1.00 51.21  ? 384 ALA C CA  1 
ATOM   8851  C  C   . ALA C 1 383 ? 21.073  1.042   12.955  1.00 47.32  ? 384 ALA C C   1 
ATOM   8852  O  O   . ALA C 1 383 ? 20.004  0.483   12.682  1.00 47.40  ? 384 ALA C O   1 
ATOM   8853  C  CB  . ALA C 1 383 ? 23.214  0.560   11.746  1.00 47.37  ? 384 ALA C CB  1 
ATOM   8854  N  N   . GLN C 1 384 ? 21.465  1.294   14.201  1.00 50.23  ? 385 GLN C N   1 
ATOM   8855  C  CA  . GLN C 1 384 ? 20.667  0.893   15.356  1.00 50.44  ? 385 GLN C CA  1 
ATOM   8856  C  C   . GLN C 1 384 ? 19.288  1.547   15.364  1.00 47.73  ? 385 GLN C C   1 
ATOM   8857  O  O   . GLN C 1 384 ? 18.280  0.884   15.603  1.00 44.48  ? 385 GLN C O   1 
ATOM   8858  C  CB  . GLN C 1 384 ? 21.402  1.230   16.656  1.00 59.88  ? 385 GLN C CB  1 
ATOM   8859  C  CG  . GLN C 1 384 ? 22.695  0.457   16.874  1.00 66.90  ? 385 GLN C CG  1 
ATOM   8860  C  CD  . GLN C 1 384 ? 22.463  -0.992  17.259  1.00 71.88  ? 385 GLN C CD  1 
ATOM   8861  O  OE1 . GLN C 1 384 ? 21.874  -1.765  16.503  1.00 75.48  ? 385 GLN C OE1 1 
ATOM   8862  N  NE2 . GLN C 1 384 ? 22.929  -1.367  18.444  1.00 74.35  ? 385 GLN C NE2 1 
ATOM   8863  N  N   . LEU C 1 385 ? 19.252  2.849   15.099  1.00 46.17  ? 386 LEU C N   1 
ATOM   8864  C  CA  . LEU C 1 385 ? 18.007  3.606   15.138  1.00 45.69  ? 386 LEU C CA  1 
ATOM   8865  C  C   . LEU C 1 385 ? 17.087  3.234   13.982  1.00 46.20  ? 386 LEU C C   1 
ATOM   8866  O  O   . LEU C 1 385 ? 15.868  3.181   14.146  1.00 43.58  ? 386 LEU C O   1 
ATOM   8867  C  CB  . LEU C 1 385 ? 18.295  5.108   15.124  1.00 41.68  ? 386 LEU C CB  1 
ATOM   8868  C  CG  . LEU C 1 385 ? 18.999  5.634   16.376  1.00 44.90  ? 386 LEU C CG  1 
ATOM   8869  C  CD1 . LEU C 1 385 ? 19.069  7.154   16.364  1.00 46.91  ? 386 LEU C CD1 1 
ATOM   8870  C  CD2 . LEU C 1 385 ? 18.308  5.130   17.636  1.00 38.63  ? 386 LEU C CD2 1 
ATOM   8871  N  N   . ARG C 1 386 ? 17.668  2.974   12.814  1.00 47.03  ? 387 ARG C N   1 
ATOM   8872  C  CA  . ARG C 1 386 ? 16.873  2.516   11.682  1.00 50.03  ? 387 ARG C CA  1 
ATOM   8873  C  C   . ARG C 1 386 ? 16.356  1.106   11.930  1.00 55.45  ? 387 ARG C C   1 
ATOM   8874  O  O   . ARG C 1 386 ? 15.312  0.718   11.405  1.00 58.64  ? 387 ARG C O   1 
ATOM   8875  C  CB  . ARG C 1 386 ? 17.681  2.559   10.385  1.00 57.82  ? 387 ARG C CB  1 
ATOM   8876  C  CG  . ARG C 1 386 ? 17.764  3.936   9.747   1.00 67.83  ? 387 ARG C CG  1 
ATOM   8877  C  CD  . ARG C 1 386 ? 18.412  3.853   8.377   1.00 75.09  ? 387 ARG C CD  1 
ATOM   8878  N  NE  . ARG C 1 386 ? 19.661  3.100   8.420   1.00 80.56  ? 387 ARG C NE  1 
ATOM   8879  C  CZ  . ARG C 1 386 ? 20.861  3.655   8.554   1.00 82.43  ? 387 ARG C CZ  1 
ATOM   8880  N  NH1 . ARG C 1 386 ? 20.973  4.973   8.649   1.00 83.57  ? 387 ARG C NH1 1 
ATOM   8881  N  NH2 . ARG C 1 386 ? 21.947  2.895   8.587   1.00 82.80  ? 387 ARG C NH2 1 
ATOM   8882  N  N   . ASP C 1 387 ? 17.086  0.340   12.736  1.00 52.29  ? 388 ASP C N   1 
ATOM   8883  C  CA  . ASP C 1 387 ? 16.669  -1.020  13.054  1.00 55.18  ? 388 ASP C CA  1 
ATOM   8884  C  C   . ASP C 1 387 ? 15.482  -1.057  14.021  1.00 47.05  ? 388 ASP C C   1 
ATOM   8885  O  O   . ASP C 1 387 ? 14.627  -1.940  13.927  1.00 49.19  ? 388 ASP C O   1 
ATOM   8886  C  CB  . ASP C 1 387 ? 17.839  -1.812  13.641  1.00 60.80  ? 388 ASP C CB  1 
ATOM   8887  C  CG  . ASP C 1 387 ? 17.472  -3.250  13.948  1.00 67.09  ? 388 ASP C CG  1 
ATOM   8888  O  OD1 . ASP C 1 387 ? 17.201  -4.011  12.995  1.00 69.63  ? 388 ASP C OD1 1 
ATOM   8889  O  OD2 . ASP C 1 387 ? 17.453  -3.619  15.141  1.00 68.08  ? 388 ASP C OD2 1 
ATOM   8890  N  N   . VAL C 1 388 ? 15.427  -0.097  14.941  1.00 38.65  ? 389 VAL C N   1 
ATOM   8891  C  CA  . VAL C 1 388 ? 14.402  -0.101  15.986  1.00 43.17  ? 389 VAL C CA  1 
ATOM   8892  C  C   . VAL C 1 388 ? 13.306  0.945   15.780  1.00 41.88  ? 389 VAL C C   1 
ATOM   8893  O  O   . VAL C 1 388 ? 12.543  1.236   16.702  1.00 42.25  ? 389 VAL C O   1 
ATOM   8894  C  CB  . VAL C 1 388 ? 15.024  0.127   17.381  1.00 43.42  ? 389 VAL C CB  1 
ATOM   8895  C  CG1 . VAL C 1 388 ? 15.989  -0.998  17.727  1.00 37.91  ? 389 VAL C CG1 1 
ATOM   8896  C  CG2 . VAL C 1 388 ? 15.718  1.484   17.444  1.00 37.89  ? 389 VAL C CG2 1 
ATOM   8897  N  N   . GLN C 1 389 ? 13.221  1.505   14.577  1.00 38.49  ? 390 GLN C N   1 
ATOM   8898  C  CA  . GLN C 1 389 ? 12.211  2.518   14.286  1.00 42.52  ? 390 GLN C CA  1 
ATOM   8899  C  C   . GLN C 1 389 ? 10.813  1.910   14.209  1.00 43.08  ? 390 GLN C C   1 
ATOM   8900  O  O   . GLN C 1 389 ? 9.813   2.612   14.361  1.00 38.86  ? 390 GLN C O   1 
ATOM   8901  C  CB  . GLN C 1 389 ? 12.535  3.242   12.977  1.00 39.32  ? 390 GLN C CB  1 
ATOM   8902  C  CG  . GLN C 1 389 ? 12.418  2.370   11.738  1.00 39.86  ? 390 GLN C CG  1 
ATOM   8903  C  CD  . GLN C 1 389 ? 12.856  3.087   10.477  1.00 46.27  ? 390 GLN C CD  1 
ATOM   8904  O  OE1 . GLN C 1 389 ? 13.676  4.004   10.523  1.00 51.05  ? 390 GLN C OE1 1 
ATOM   8905  N  NE2 . GLN C 1 389 ? 12.306  2.675   9.340   1.00 47.10  ? 390 GLN C NE2 1 
ATOM   8906  N  N   . ASP C 1 390 ? 10.753  0.602   13.979  1.00 44.61  ? 391 ASP C N   1 
ATOM   8907  C  CA  . ASP C 1 390 ? 9.485   -0.099  13.798  1.00 45.10  ? 391 ASP C CA  1 
ATOM   8908  C  C   . ASP C 1 390 ? 9.056   -0.861  15.048  1.00 38.00  ? 391 ASP C C   1 
ATOM   8909  O  O   . ASP C 1 390 ? 8.093   -1.626  15.009  1.00 38.00  ? 391 ASP C O   1 
ATOM   8910  C  CB  . ASP C 1 390 ? 9.583   -1.068  12.615  1.00 49.91  ? 391 ASP C CB  1 
ATOM   8911  C  CG  . ASP C 1 390 ? 10.750  -2.041  12.744  1.00 57.05  ? 391 ASP C CG  1 
ATOM   8912  O  OD1 . ASP C 1 390 ? 11.371  -2.106  13.826  1.00 59.46  ? 391 ASP C OD1 1 
ATOM   8913  O  OD2 . ASP C 1 390 ? 11.047  -2.751  11.761  1.00 60.50  ? 391 ASP C OD2 1 
ATOM   8914  N  N   . PHE C 1 391 ? 9.779   -0.643  16.143  1.00 43.05  ? 392 PHE C N   1 
ATOM   8915  C  CA  . PHE C 1 391 ? 9.628   -1.415  17.378  1.00 47.31  ? 392 PHE C CA  1 
ATOM   8916  C  C   . PHE C 1 391 ? 8.177   -1.634  17.816  1.00 46.16  ? 392 PHE C C   1 
ATOM   8917  O  O   . PHE C 1 391 ? 7.705   -2.776  17.912  1.00 49.76  ? 392 PHE C O   1 
ATOM   8918  C  CB  . PHE C 1 391 ? 10.405  -0.723  18.503  1.00 41.44  ? 392 PHE C CB  1 
ATOM   8919  C  CG  . PHE C 1 391 ? 10.428  -1.491  19.793  1.00 43.77  ? 392 PHE C CG  1 
ATOM   8920  C  CD1 . PHE C 1 391 ? 11.247  -2.598  19.939  1.00 36.71  ? 392 PHE C CD1 1 
ATOM   8921  C  CD2 . PHE C 1 391 ? 9.646   -1.097  20.866  1.00 43.65  ? 392 PHE C CD2 1 
ATOM   8922  C  CE1 . PHE C 1 391 ? 11.277  -3.305  21.125  1.00 36.59  ? 392 PHE C CE1 1 
ATOM   8923  C  CE2 . PHE C 1 391 ? 9.671   -1.800  22.057  1.00 41.82  ? 392 PHE C CE2 1 
ATOM   8924  C  CZ  . PHE C 1 391 ? 10.489  -2.905  22.186  1.00 36.43  ? 392 PHE C CZ  1 
ATOM   8925  N  N   . TRP C 1 392 ? 7.474   -0.530  18.052  1.00 46.52  ? 393 TRP C N   1 
ATOM   8926  C  CA  . TRP C 1 392 ? 6.151   -0.559  18.666  1.00 48.20  ? 393 TRP C CA  1 
ATOM   8927  C  C   . TRP C 1 392 ? 5.077   -1.228  17.807  1.00 45.29  ? 393 TRP C C   1 
ATOM   8928  O  O   . TRP C 1 392 ? 4.043   -1.649  18.326  1.00 51.62  ? 393 TRP C O   1 
ATOM   8929  C  CB  . TRP C 1 392 ? 5.720   0.865   19.022  1.00 44.59  ? 393 TRP C CB  1 
ATOM   8930  C  CG  . TRP C 1 392 ? 6.710   1.557   19.907  1.00 41.38  ? 393 TRP C CG  1 
ATOM   8931  C  CD1 . TRP C 1 392 ? 7.529   2.596   19.570  1.00 42.94  ? 393 TRP C CD1 1 
ATOM   8932  C  CD2 . TRP C 1 392 ? 7.009   1.237   21.271  1.00 42.34  ? 393 TRP C CD2 1 
ATOM   8933  N  NE1 . TRP C 1 392 ? 8.309   2.952   20.645  1.00 42.10  ? 393 TRP C NE1 1 
ATOM   8934  C  CE2 . TRP C 1 392 ? 8.009   2.132   21.701  1.00 42.03  ? 393 TRP C CE2 1 
ATOM   8935  C  CE3 . TRP C 1 392 ? 6.522   0.284   22.172  1.00 41.49  ? 393 TRP C CE3 1 
ATOM   8936  C  CZ2 . TRP C 1 392 ? 8.531   2.102   22.993  1.00 39.80  ? 393 TRP C CZ2 1 
ATOM   8937  C  CZ3 . TRP C 1 392 ? 7.042   0.256   23.453  1.00 40.90  ? 393 TRP C CZ3 1 
ATOM   8938  C  CH2 . TRP C 1 392 ? 8.036   1.160   23.852  1.00 41.69  ? 393 TRP C CH2 1 
ATOM   8939  N  N   . ILE C 1 393 ? 5.315   -1.331  16.504  1.00 43.82  ? 394 ILE C N   1 
ATOM   8940  C  CA  . ILE C 1 393 ? 4.361   -2.001  15.626  1.00 43.25  ? 394 ILE C CA  1 
ATOM   8941  C  C   . ILE C 1 393 ? 4.885   -3.348  15.142  1.00 43.93  ? 394 ILE C C   1 
ATOM   8942  O  O   . ILE C 1 393 ? 4.135   -4.143  14.577  1.00 48.62  ? 394 ILE C O   1 
ATOM   8943  C  CB  . ILE C 1 393 ? 4.005   -1.142  14.398  1.00 41.26  ? 394 ILE C CB  1 
ATOM   8944  C  CG1 . ILE C 1 393 ? 5.230   -0.956  13.500  1.00 39.81  ? 394 ILE C CG1 1 
ATOM   8945  C  CG2 . ILE C 1 393 ? 3.428   0.197   14.832  1.00 41.88  ? 394 ILE C CG2 1 
ATOM   8946  C  CD1 . ILE C 1 393 ? 4.925   -0.253  12.200  1.00 44.16  ? 394 ILE C CD1 1 
ATOM   8947  N  N   . SER C 1 394 ? 6.171   -3.601  15.362  1.00 46.63  ? 395 SER C N   1 
ATOM   8948  C  CA  . SER C 1 394 ? 6.764   -4.875  14.973  1.00 51.08  ? 395 SER C CA  1 
ATOM   8949  C  C   . SER C 1 394 ? 6.736   -5.866  16.131  1.00 44.46  ? 395 SER C C   1 
ATOM   8950  O  O   . SER C 1 394 ? 6.969   -7.059  15.935  1.00 40.26  ? 395 SER C O   1 
ATOM   8951  C  CB  . SER C 1 394 ? 8.201   -4.684  14.482  1.00 54.18  ? 395 SER C CB  1 
ATOM   8952  O  OG  . SER C 1 394 ? 9.041   -4.223  15.526  1.00 56.16  ? 395 SER C OG  1 
ATOM   8953  N  N   . LEU C 1 395 ? 6.457   -5.363  17.333  1.00 43.43  ? 396 LEU C N   1 
ATOM   8954  C  CA  . LEU C 1 395 ? 6.318   -6.220  18.516  1.00 45.79  ? 396 LEU C CA  1 
ATOM   8955  C  C   . LEU C 1 395 ? 5.446   -7.475  18.302  1.00 47.89  ? 396 LEU C C   1 
ATOM   8956  O  O   . LEU C 1 395 ? 5.881   -8.583  18.642  1.00 49.06  ? 396 LEU C O   1 
ATOM   8957  C  CB  . LEU C 1 395 ? 5.764   -5.407  19.695  1.00 50.74  ? 396 LEU C CB  1 
ATOM   8958  C  CG  . LEU C 1 395 ? 6.748   -4.574  20.514  1.00 53.98  ? 396 LEU C CG  1 
ATOM   8959  C  CD1 . LEU C 1 395 ? 5.997   -3.578  21.382  1.00 51.37  ? 396 LEU C CD1 1 
ATOM   8960  C  CD2 . LEU C 1 395 ? 7.618   -5.483  21.368  1.00 50.21  ? 396 LEU C CD2 1 
ATOM   8961  N  N   . PRO C 1 396 ? 4.224   -7.320  17.741  1.00 43.30  ? 397 PRO C N   1 
ATOM   8962  C  CA  . PRO C 1 396 ? 3.400   -8.523  17.562  1.00 43.83  ? 397 PRO C CA  1 
ATOM   8963  C  C   . PRO C 1 396 ? 4.050   -9.577  16.669  1.00 46.23  ? 397 PRO C C   1 
ATOM   8964  O  O   . PRO C 1 396 ? 4.081   -10.748 17.042  1.00 43.98  ? 397 PRO C O   1 
ATOM   8965  C  CB  . PRO C 1 396 ? 2.126   -7.981  16.908  1.00 44.32  ? 397 PRO C CB  1 
ATOM   8966  C  CG  . PRO C 1 396 ? 2.062   -6.565  17.333  1.00 43.68  ? 397 PRO C CG  1 
ATOM   8967  C  CD  . PRO C 1 396 ? 3.487   -6.108  17.332  1.00 43.47  ? 397 PRO C CD  1 
ATOM   8968  N  N   . GLY C 1 397 ? 4.561   -9.161  15.514  1.00 44.57  ? 398 GLY C N   1 
ATOM   8969  C  CA  . GLY C 1 397 ? 5.212   -10.076 14.593  1.00 47.03  ? 398 GLY C CA  1 
ATOM   8970  C  C   . GLY C 1 397 ? 6.405   -10.773 15.219  1.00 50.62  ? 398 GLY C C   1 
ATOM   8971  O  O   . GLY C 1 397 ? 6.583   -11.982 15.065  1.00 51.33  ? 398 GLY C O   1 
ATOM   8972  N  N   . THR C 1 398 ? 7.219   -10.002 15.933  1.00 49.22  ? 399 THR C N   1 
ATOM   8973  C  CA  . THR C 1 398 ? 8.396   -10.529 16.614  1.00 51.98  ? 399 THR C CA  1 
ATOM   8974  C  C   . THR C 1 398 ? 8.016   -11.592 17.641  1.00 51.39  ? 399 THR C C   1 
ATOM   8975  O  O   . THR C 1 398 ? 8.450   -12.750 17.551  1.00 56.54  ? 399 THR C O   1 
ATOM   8976  C  CB  . THR C 1 398 ? 9.180   -9.403  17.318  1.00 50.48  ? 399 THR C CB  1 
ATOM   8977  O  OG1 . THR C 1 398 ? 9.704   -8.497  16.339  1.00 50.96  ? 399 THR C OG1 1 
ATOM   8978  C  CG2 . THR C 1 398 ? 10.326  -9.975  18.132  1.00 51.71  ? 399 THR C CG2 1 
ATOM   8979  N  N   . LEU C 1 399 ? 7.193   -11.190 18.607  1.00 51.04  ? 400 LEU C N   1 
ATOM   8980  C  CA  . LEU C 1 399 ? 6.786   -12.075 19.694  1.00 49.73  ? 400 LEU C CA  1 
ATOM   8981  C  C   . LEU C 1 399 ? 6.073   -13.326 19.184  1.00 57.27  ? 400 LEU C C   1 
ATOM   8982  O  O   . LEU C 1 399 ? 6.275   -14.419 19.712  1.00 57.47  ? 400 LEU C O   1 
ATOM   8983  C  CB  . LEU C 1 399 ? 5.886   -11.329 20.679  1.00 50.48  ? 400 LEU C CB  1 
ATOM   8984  C  CG  . LEU C 1 399 ? 6.536   -10.170 21.437  1.00 53.54  ? 400 LEU C CG  1 
ATOM   8985  C  CD1 . LEU C 1 399 ? 5.499   -9.408  22.248  1.00 52.32  ? 400 LEU C CD1 1 
ATOM   8986  C  CD2 . LEU C 1 399 ? 7.659   -10.676 22.329  1.00 50.38  ? 400 LEU C CD2 1 
ATOM   8987  N  N   . CYS C 1 400 ? 5.243   -13.163 18.159  1.00 55.21  ? 401 CYS C N   1 
ATOM   8988  C  CA  . CYS C 1 400 ? 4.538   -14.297 17.574  1.00 59.01  ? 401 CYS C CA  1 
ATOM   8989  C  C   . CYS C 1 400 ? 5.501   -15.257 16.888  1.00 58.67  ? 401 CYS C C   1 
ATOM   8990  O  O   . CYS C 1 400 ? 5.480   -16.459 17.147  1.00 60.83  ? 401 CYS C O   1 
ATOM   8991  C  CB  . CYS C 1 400 ? 3.483   -13.825 16.572  1.00 58.49  ? 401 CYS C CB  1 
ATOM   8992  S  SG  . CYS C 1 400 ? 2.007   -13.105 17.321  1.00 58.61  ? 401 CYS C SG  1 
ATOM   8993  N  N   . SER C 1 401 ? 6.348   -14.717 16.019  1.00 62.37  ? 402 SER C N   1 
ATOM   8994  C  CA  . SER C 1 401 ? 7.219   -15.546 15.195  1.00 68.02  ? 402 SER C CA  1 
ATOM   8995  C  C   . SER C 1 401 ? 8.312   -16.246 15.997  1.00 70.74  ? 402 SER C C   1 
ATOM   8996  O  O   . SER C 1 401 ? 8.738   -17.344 15.636  1.00 74.19  ? 402 SER C O   1 
ATOM   8997  C  CB  . SER C 1 401 ? 7.856   -14.707 14.086  1.00 68.79  ? 402 SER C CB  1 
ATOM   8998  O  OG  . SER C 1 401 ? 8.507   -15.532 13.136  1.00 72.31  ? 402 SER C OG  1 
ATOM   8999  N  N   . GLU C 1 402 ? 8.770   -15.625 17.080  1.00 73.12  ? 403 GLU C N   1 
ATOM   9000  C  CA  . GLU C 1 402 ? 9.871   -16.215 17.839  1.00 79.00  ? 403 GLU C CA  1 
ATOM   9001  C  C   . GLU C 1 402 ? 9.401   -17.140 18.964  1.00 84.83  ? 403 GLU C C   1 
ATOM   9002  O  O   . GLU C 1 402 ? 10.144  -18.019 19.398  1.00 88.00  ? 403 GLU C O   1 
ATOM   9003  C  CB  . GLU C 1 402 ? 10.772  -15.116 18.411  1.00 78.69  ? 403 GLU C CB  1 
ATOM   9004  C  CG  . GLU C 1 402 ? 10.402  -14.655 19.810  1.00 79.54  ? 403 GLU C CG  1 
ATOM   9005  C  CD  . GLU C 1 402 ? 11.015  -13.315 20.158  1.00 82.48  ? 403 GLU C CD  1 
ATOM   9006  O  OE1 . GLU C 1 402 ? 11.613  -12.684 19.261  1.00 83.01  ? 403 GLU C OE1 1 
ATOM   9007  O  OE2 . GLU C 1 402 ? 10.909  -12.898 21.331  1.00 82.33  ? 403 GLU C OE2 1 
ATOM   9008  N  N   . LYS C 1 403 ? 8.169   -16.953 19.426  1.00 86.39  ? 404 LYS C N   1 
ATOM   9009  C  CA  . LYS C 1 403 ? 7.676   -17.697 20.581  1.00 87.52  ? 404 LYS C CA  1 
ATOM   9010  C  C   . LYS C 1 403 ? 6.478   -18.588 20.276  1.00 87.88  ? 404 LYS C C   1 
ATOM   9011  O  O   . LYS C 1 403 ? 6.619   -19.793 20.058  1.00 87.64  ? 404 LYS C O   1 
ATOM   9012  C  CB  . LYS C 1 403 ? 7.301   -16.728 21.704  1.00 86.54  ? 404 LYS C CB  1 
ATOM   9013  C  CG  . LYS C 1 403 ? 8.215   -16.780 22.912  1.00 86.17  ? 404 LYS C CG  1 
ATOM   9014  C  CD  . LYS C 1 403 ? 9.675   -16.825 22.516  1.00 86.66  ? 404 LYS C CD  1 
ATOM   9015  C  CE  . LYS C 1 403 ? 10.559  -16.748 23.746  1.00 86.47  ? 404 LYS C CE  1 
ATOM   9016  N  NZ  . LYS C 1 403 ? 11.999  -16.663 23.392  1.00 86.11  ? 404 LYS C NZ  1 
ATOM   9017  N  N   . MET C 1 404 ? 5.300   -17.975 20.283  1.00 88.07  ? 405 MET C N   1 
ATOM   9018  C  CA  . MET C 1 404 ? 4.031   -18.694 20.296  1.00 89.07  ? 405 MET C CA  1 
ATOM   9019  C  C   . MET C 1 404 ? 3.668   -19.368 18.973  1.00 87.38  ? 405 MET C C   1 
ATOM   9020  O  O   . MET C 1 404 ? 3.329   -20.552 18.946  1.00 86.78  ? 405 MET C O   1 
ATOM   9021  C  CB  . MET C 1 404 ? 2.922   -17.726 20.705  1.00 89.97  ? 405 MET C CB  1 
ATOM   9022  C  CG  . MET C 1 404 ? 3.226   -16.996 22.005  1.00 90.82  ? 405 MET C CG  1 
ATOM   9023  S  SD  . MET C 1 404 ? 2.554   -15.325 22.075  1.00 84.78  ? 405 MET C SD  1 
ATOM   9024  C  CE  . MET C 1 404 ? 3.366   -14.703 23.547  1.00 48.45  ? 405 MET C CE  1 
ATOM   9025  N  N   . ALA C 1 405 ? 3.735   -18.613 17.881  1.00 83.78  ? 406 ALA C N   1 
ATOM   9026  C  CA  . ALA C 1 405 ? 3.337   -19.130 16.576  1.00 82.25  ? 406 ALA C CA  1 
ATOM   9027  C  C   . ALA C 1 405 ? 4.381   -20.088 16.014  1.00 82.38  ? 406 ALA C C   1 
ATOM   9028  O  O   . ALA C 1 405 ? 4.076   -20.918 15.157  1.00 83.26  ? 406 ALA C O   1 
ATOM   9029  C  CB  . ALA C 1 405 ? 3.090   -17.985 15.605  1.00 79.41  ? 406 ALA C CB  1 
ATOM   9030  N  N   . ARG C 1 413 ? -2.009  -27.555 9.524   1.00 87.48  ? 414 ARG C N   1 
ATOM   9031  C  CA  . ARG C 1 413 ? -3.081  -26.832 10.199  1.00 85.06  ? 414 ARG C CA  1 
ATOM   9032  C  C   . ARG C 1 413 ? -2.556  -26.091 11.427  1.00 78.32  ? 414 ARG C C   1 
ATOM   9033  O  O   . ARG C 1 413 ? -1.400  -26.257 11.816  1.00 80.39  ? 414 ARG C O   1 
ATOM   9034  C  CB  . ARG C 1 413 ? -4.206  -27.792 10.595  1.00 90.37  ? 414 ARG C CB  1 
ATOM   9035  C  CG  . ARG C 1 413 ? -4.952  -28.391 9.410   1.00 95.78  ? 414 ARG C CG  1 
ATOM   9036  C  CD  . ARG C 1 413 ? -5.584  -29.729 9.760   1.00 101.10 ? 414 ARG C CD  1 
ATOM   9037  N  NE  . ARG C 1 413 ? -6.320  -30.297 8.633   1.00 106.15 ? 414 ARG C NE  1 
ATOM   9038  C  CZ  . ARG C 1 413 ? -6.000  -31.438 8.032   1.00 111.01 ? 414 ARG C CZ  1 
ATOM   9039  N  NH1 . ARG C 1 413 ? -4.952  -32.136 8.448   1.00 112.16 ? 414 ARG C NH1 1 
ATOM   9040  N  NH2 . ARG C 1 413 ? -6.724  -31.881 7.013   1.00 112.46 ? 414 ARG C NH2 1 
ATOM   9041  N  N   . CYS C 1 414 ? -3.412  -25.270 12.028  1.00 70.06  ? 415 CYS C N   1 
ATOM   9042  C  CA  . CYS C 1 414 ? -3.029  -24.449 13.174  1.00 64.67  ? 415 CYS C CA  1 
ATOM   9043  C  C   . CYS C 1 414 ? -4.250  -24.093 14.019  1.00 59.26  ? 415 CYS C C   1 
ATOM   9044  O  O   . CYS C 1 414 ? -5.386  -24.270 13.583  1.00 59.66  ? 415 CYS C O   1 
ATOM   9045  C  CB  . CYS C 1 414 ? -2.303  -23.180 12.714  1.00 63.65  ? 415 CYS C CB  1 
ATOM   9046  S  SG  . CYS C 1 414 ? -3.204  -22.167 11.518  1.00 72.44  ? 415 CYS C SG  1 
ATOM   9047  N  N   . TRP C 1 415 ? -4.019  -23.609 15.234  1.00 56.43  ? 416 TRP C N   1 
ATOM   9048  C  CA  . TRP C 1 415 ? -5.121  -23.276 16.129  1.00 56.28  ? 416 TRP C CA  1 
ATOM   9049  C  C   . TRP C 1 415 ? -5.642  -21.870 15.839  1.00 56.93  ? 416 TRP C C   1 
ATOM   9050  O  O   . TRP C 1 415 ? -4.922  -20.883 15.995  1.00 58.28  ? 416 TRP C O   1 
ATOM   9051  C  CB  . TRP C 1 415 ? -4.658  -23.396 17.584  1.00 55.10  ? 416 TRP C CB  1 
ATOM   9052  C  CG  . TRP C 1 415 ? -5.609  -22.849 18.605  1.00 57.20  ? 416 TRP C CG  1 
ATOM   9053  C  CD1 . TRP C 1 415 ? -5.462  -21.700 19.327  1.00 58.34  ? 416 TRP C CD1 1 
ATOM   9054  C  CD2 . TRP C 1 415 ? -6.843  -23.437 19.035  1.00 60.09  ? 416 TRP C CD2 1 
ATOM   9055  N  NE1 . TRP C 1 415 ? -6.531  -21.533 20.174  1.00 56.38  ? 416 TRP C NE1 1 
ATOM   9056  C  CE2 . TRP C 1 415 ? -7.392  -22.586 20.015  1.00 58.80  ? 416 TRP C CE2 1 
ATOM   9057  C  CE3 . TRP C 1 415 ? -7.537  -24.600 18.686  1.00 60.95  ? 416 TRP C CE3 1 
ATOM   9058  C  CZ2 . TRP C 1 415 ? -8.602  -22.859 20.647  1.00 60.87  ? 416 TRP C CZ2 1 
ATOM   9059  C  CZ3 . TRP C 1 415 ? -8.739  -24.868 19.315  1.00 61.40  ? 416 TRP C CZ3 1 
ATOM   9060  C  CH2 . TRP C 1 415 ? -9.260  -24.001 20.283  1.00 61.52  ? 416 TRP C CH2 1 
ATOM   9061  N  N   . ASN C 1 416 ? -6.899  -21.793 15.410  1.00 53.64  ? 417 ASN C N   1 
ATOM   9062  C  CA  . ASN C 1 416 ? -7.524  -20.519 15.060  1.00 54.68  ? 417 ASN C CA  1 
ATOM   9063  C  C   . ASN C 1 416 ? -8.378  -19.929 16.179  1.00 50.47  ? 417 ASN C C   1 
ATOM   9064  O  O   . ASN C 1 416 ? -8.986  -18.872 16.012  1.00 55.32  ? 417 ASN C O   1 
ATOM   9065  C  CB  . ASN C 1 416 ? -8.366  -20.676 13.790  1.00 54.20  ? 417 ASN C CB  1 
ATOM   9066  C  CG  . ASN C 1 416 ? -9.345  -21.832 13.871  1.00 56.87  ? 417 ASN C CG  1 
ATOM   9067  O  OD1 . ASN C 1 416 ? -10.010 -22.033 14.887  1.00 56.71  ? 417 ASN C OD1 1 
ATOM   9068  N  ND2 . ASN C 1 416 ? -9.437  -22.602 12.792  1.00 56.96  ? 417 ASN C ND2 1 
ATOM   9069  N  N   . GLY C 1 417 ? -8.430  -20.617 17.314  1.00 42.77  ? 418 GLY C N   1 
ATOM   9070  C  CA  . GLY C 1 417 ? -9.218  -20.159 18.444  1.00 42.60  ? 418 GLY C CA  1 
ATOM   9071  C  C   . GLY C 1 417 ? -10.489 -20.963 18.638  1.00 59.49  ? 418 GLY C C   1 
ATOM   9072  O  O   . GLY C 1 417 ? -11.128 -20.889 19.687  1.00 63.07  ? 418 GLY C O   1 
ATOM   9073  N  N   . MET C 1 418 ? -10.854 -21.737 17.623  1.00 63.91  ? 419 MET C N   1 
ATOM   9074  C  CA  . MET C 1 418 ? -12.029 -22.597 17.697  1.00 66.63  ? 419 MET C CA  1 
ATOM   9075  C  C   . MET C 1 418 ? -11.627 -24.058 17.524  1.00 70.07  ? 419 MET C C   1 
ATOM   9076  O  O   . MET C 1 418 ? -11.793 -24.868 18.436  1.00 71.27  ? 419 MET C O   1 
ATOM   9077  C  CB  . MET C 1 418 ? -13.066 -22.190 16.647  1.00 66.83  ? 419 MET C CB  1 
ATOM   9078  C  CG  . MET C 1 418 ? -13.714 -20.838 16.923  1.00 67.98  ? 419 MET C CG  1 
ATOM   9079  S  SD  . MET C 1 418 ? -15.195 -20.531 15.942  1.00 116.16 ? 419 MET C SD  1 
ATOM   9080  C  CE  . MET C 1 418 ? -14.520 -20.552 14.284  1.00 60.89  ? 419 MET C CE  1 
ATOM   9081  N  N   . ALA C 1 419 ? -11.110 -24.392 16.347  1.00 71.52  ? 420 ALA C N   1 
ATOM   9082  C  CA  . ALA C 1 419 ? -10.597 -25.732 16.090  1.00 71.08  ? 420 ALA C CA  1 
ATOM   9083  C  C   . ALA C 1 419 ? -9.234  -25.665 15.408  1.00 73.97  ? 420 ALA C C   1 
ATOM   9084  O  O   . ALA C 1 419 ? -8.716  -24.580 15.146  1.00 70.64  ? 420 ALA C O   1 
ATOM   9085  C  CB  . ALA C 1 419 ? -11.578 -26.521 15.240  1.00 72.84  ? 420 ALA C CB  1 
ATOM   9086  N  N   . ARG C 1 420 ? -8.653  -26.826 15.125  1.00 69.49  ? 421 ARG C N   1 
ATOM   9087  C  CA  . ARG C 1 420 ? -7.395  -26.882 14.388  1.00 70.17  ? 421 ARG C CA  1 
ATOM   9088  C  C   . ARG C 1 420 ? -7.670  -26.794 12.890  1.00 73.93  ? 421 ARG C C   1 
ATOM   9089  O  O   . ARG C 1 420 ? -8.385  -27.627 12.332  1.00 78.85  ? 421 ARG C O   1 
ATOM   9090  C  CB  . ARG C 1 420 ? -6.628  -28.163 14.721  1.00 65.62  ? 421 ARG C CB  1 
ATOM   9091  N  N   . GLY C 1 421 ? -7.096  -25.783 12.244  1.00 77.44  ? 422 GLY C N   1 
ATOM   9092  C  CA  . GLY C 1 421 ? -7.358  -25.522 10.840  1.00 80.81  ? 422 GLY C CA  1 
ATOM   9093  C  C   . GLY C 1 421 ? -6.840  -24.162 10.414  1.00 83.16  ? 422 GLY C C   1 
ATOM   9094  O  O   . GLY C 1 421 ? -5.932  -23.617 11.035  1.00 86.62  ? 422 GLY C O   1 
ATOM   9095  N  N   . ARG C 1 422 ? -7.412  -23.604 9.353   1.00 84.91  ? 423 ARG C N   1 
ATOM   9096  C  CA  . ARG C 1 422 ? -6.937  -22.323 8.840   1.00 85.20  ? 423 ARG C CA  1 
ATOM   9097  C  C   . ARG C 1 422 ? -7.707  -21.124 9.397   1.00 80.96  ? 423 ARG C C   1 
ATOM   9098  O  O   . ARG C 1 422 ? -8.927  -21.169 9.565   1.00 80.81  ? 423 ARG C O   1 
ATOM   9099  C  CB  . ARG C 1 422 ? -6.992  -22.318 7.312   1.00 93.81  ? 423 ARG C CB  1 
ATOM   9100  C  CG  . ARG C 1 422 ? -5.839  -23.077 6.676   1.00 100.85 ? 423 ARG C CG  1 
ATOM   9101  C  CD  . ARG C 1 422 ? -5.801  -22.902 5.167   1.00 106.18 ? 423 ARG C CD  1 
ATOM   9102  N  NE  . ARG C 1 422 ? -6.107  -24.144 4.460   1.00 110.58 ? 423 ARG C NE  1 
ATOM   9103  C  CZ  . ARG C 1 422 ? -5.288  -25.190 4.378   1.00 112.24 ? 423 ARG C CZ  1 
ATOM   9104  N  NH1 . ARG C 1 422 ? -4.093  -25.156 4.953   1.00 111.77 ? 423 ARG C NH1 1 
ATOM   9105  N  NH2 . ARG C 1 422 ? -5.665  -26.273 3.712   1.00 113.42 ? 423 ARG C NH2 1 
ATOM   9106  N  N   . TYR C 1 423 ? -6.972  -20.053 9.680   1.00 72.12  ? 424 TYR C N   1 
ATOM   9107  C  CA  . TYR C 1 423 ? -7.550  -18.832 10.227  1.00 66.17  ? 424 TYR C CA  1 
ATOM   9108  C  C   . TYR C 1 423 ? -7.853  -17.845 9.101   1.00 64.52  ? 424 TYR C C   1 
ATOM   9109  O  O   . TYR C 1 423 ? -6.944  -17.278 8.495   1.00 64.56  ? 424 TYR C O   1 
ATOM   9110  C  CB  . TYR C 1 423 ? -6.580  -18.228 11.248  1.00 61.76  ? 424 TYR C CB  1 
ATOM   9111  C  CG  . TYR C 1 423 ? -7.023  -16.943 11.910  1.00 61.12  ? 424 TYR C CG  1 
ATOM   9112  C  CD1 . TYR C 1 423 ? -7.939  -16.955 12.954  1.00 59.80  ? 424 TYR C CD1 1 
ATOM   9113  C  CD2 . TYR C 1 423 ? -6.494  -15.720 11.518  1.00 61.31  ? 424 TYR C CD2 1 
ATOM   9114  C  CE1 . TYR C 1 423 ? -8.334  -15.783 13.572  1.00 57.81  ? 424 TYR C CE1 1 
ATOM   9115  C  CE2 . TYR C 1 423 ? -6.881  -14.543 12.130  1.00 58.17  ? 424 TYR C CE2 1 
ATOM   9116  C  CZ  . TYR C 1 423 ? -7.801  -14.580 13.156  1.00 59.73  ? 424 TYR C CZ  1 
ATOM   9117  O  OH  . TYR C 1 423 ? -8.191  -13.409 13.767  1.00 56.32  ? 424 TYR C OH  1 
ATOM   9118  N  N   . LEU C 1 424 ? -9.140  -17.650 8.828   1.00 66.46  ? 425 LEU C N   1 
ATOM   9119  C  CA  . LEU C 1 424 ? -9.587  -16.771 7.745   1.00 68.43  ? 425 LEU C CA  1 
ATOM   9120  C  C   . LEU C 1 424 ? -9.389  -15.248 7.932   1.00 71.24  ? 425 LEU C C   1 
ATOM   9121  O  O   . LEU C 1 424 ? -8.953  -14.583 6.991   1.00 70.80  ? 425 LEU C O   1 
ATOM   9122  C  CB  . LEU C 1 424 ? -11.064 -17.064 7.420   1.00 73.22  ? 425 LEU C CB  1 
ATOM   9123  C  CG  . LEU C 1 424 ? -12.210 -16.841 8.410   1.00 74.65  ? 425 LEU C CG  1 
ATOM   9124  C  CD1 . LEU C 1 424 ? -12.870 -15.488 8.180   1.00 75.89  ? 425 LEU C CD1 1 
ATOM   9125  C  CD2 . LEU C 1 424 ? -13.231 -17.963 8.310   1.00 76.06  ? 425 LEU C CD2 1 
ATOM   9126  N  N   . PRO C 1 425 ? -9.708  -14.687 9.124   1.00 65.27  ? 426 PRO C N   1 
ATOM   9127  C  CA  . PRO C 1 425 ? -9.819  -13.220 9.205   1.00 70.45  ? 426 PRO C CA  1 
ATOM   9128  C  C   . PRO C 1 425 ? -8.557  -12.435 8.842   1.00 75.95  ? 426 PRO C C   1 
ATOM   9129  O  O   . PRO C 1 425 ? -7.438  -12.922 9.005   1.00 73.33  ? 426 PRO C O   1 
ATOM   9130  C  CB  . PRO C 1 425 ? -10.172 -12.977 10.680  1.00 64.65  ? 426 PRO C CB  1 
ATOM   9131  C  CG  . PRO C 1 425 ? -10.710 -14.269 11.169  1.00 64.36  ? 426 PRO C CG  1 
ATOM   9132  C  CD  . PRO C 1 425 ? -9.912  -15.300 10.448  1.00 65.60  ? 426 PRO C CD  1 
ATOM   9133  N  N   . GLU C 1 426 ? -8.764  -11.215 8.352   1.00 86.14  ? 427 GLU C N   1 
ATOM   9134  C  CA  . GLU C 1 426 ? -7.675  -10.317 7.982   1.00 88.12  ? 427 GLU C CA  1 
ATOM   9135  C  C   . GLU C 1 426 ? -6.967  -9.745  9.205   1.00 78.49  ? 427 GLU C C   1 
ATOM   9136  O  O   . GLU C 1 426 ? -7.581  -9.547  10.253  1.00 80.97  ? 427 GLU C O   1 
ATOM   9137  C  CB  . GLU C 1 426 ? -8.207  -9.173  7.114   1.00 97.00  ? 427 GLU C CB  1 
ATOM   9138  C  CG  . GLU C 1 426 ? -7.877  -9.290  5.635   1.00 104.02 ? 427 GLU C CG  1 
ATOM   9139  C  CD  . GLU C 1 426 ? -6.465  -8.840  5.308   1.00 108.13 ? 427 GLU C CD  1 
ATOM   9140  O  OE1 . GLU C 1 426 ? -5.702  -8.517  6.244   1.00 108.36 ? 427 GLU C OE1 1 
ATOM   9141  O  OE2 . GLU C 1 426 ? -6.118  -8.805  4.108   1.00 110.82 ? 427 GLU C OE2 1 
ATOM   9142  N  N   . VAL C 1 427 ? -5.674  -9.476  9.061   1.00 65.96  ? 428 VAL C N   1 
ATOM   9143  C  CA  . VAL C 1 427 ? -4.899  -8.868  10.136  1.00 61.39  ? 428 VAL C CA  1 
ATOM   9144  C  C   . VAL C 1 427 ? -5.302  -7.408  10.320  1.00 55.15  ? 428 VAL C C   1 
ATOM   9145  O  O   . VAL C 1 427 ? -5.465  -6.672  9.347   1.00 57.29  ? 428 VAL C O   1 
ATOM   9146  C  CB  . VAL C 1 427 ? -3.384  -8.950  9.864   1.00 60.64  ? 428 VAL C CB  1 
ATOM   9147  C  CG1 . VAL C 1 427 ? -2.601  -8.613  11.124  1.00 57.59  ? 428 VAL C CG1 1 
ATOM   9148  C  CG2 . VAL C 1 427 ? -3.010  -10.336 9.364   1.00 60.26  ? 428 VAL C CG2 1 
ATOM   9149  N  N   . MET C 1 428 ? -5.473  -6.999  11.573  1.00 54.33  ? 429 MET C N   1 
ATOM   9150  C  CA  . MET C 1 428 ? -5.856  -5.628  11.893  1.00 52.02  ? 429 MET C CA  1 
ATOM   9151  C  C   . MET C 1 428 ? -4.739  -4.637  11.590  1.00 53.01  ? 429 MET C C   1 
ATOM   9152  O  O   . MET C 1 428 ? -3.569  -5.010  11.491  1.00 50.52  ? 429 MET C O   1 
ATOM   9153  C  CB  . MET C 1 428 ? -6.255  -5.514  13.366  1.00 59.46  ? 429 MET C CB  1 
ATOM   9154  C  CG  . MET C 1 428 ? -7.514  -6.281  13.748  1.00 63.32  ? 429 MET C CG  1 
ATOM   9155  S  SD  . MET C 1 428 ? -9.015  -5.605  13.012  1.00 60.57  ? 429 MET C SD  1 
ATOM   9156  C  CE  . MET C 1 428 ? -9.286  -6.755  11.664  1.00 88.24  ? 429 MET C CE  1 
ATOM   9157  N  N   . GLY C 1 429 ? -5.110  -3.371  11.432  1.00 54.51  ? 430 GLY C N   1 
ATOM   9158  C  CA  . GLY C 1 429 ? -4.133  -2.308  11.306  1.00 49.69  ? 430 GLY C CA  1 
ATOM   9159  C  C   . GLY C 1 429 ? -3.534  -1.991  12.662  1.00 46.03  ? 430 GLY C C   1 
ATOM   9160  O  O   . GLY C 1 429 ? -4.044  -2.432  13.692  1.00 45.30  ? 430 GLY C O   1 
ATOM   9161  N  N   . ASP C 1 430 ? -2.442  -1.235  12.665  1.00 47.24  ? 431 ASP C N   1 
ATOM   9162  C  CA  . ASP C 1 430 ? -1.778  -0.850  13.905  1.00 45.27  ? 431 ASP C CA  1 
ATOM   9163  C  C   . ASP C 1 430 ? -2.489  0.312   14.595  1.00 45.41  ? 431 ASP C C   1 
ATOM   9164  O  O   . ASP C 1 430 ? -3.169  1.107   13.948  1.00 45.73  ? 431 ASP C O   1 
ATOM   9165  C  CB  . ASP C 1 430 ? -0.319  -0.483  13.630  1.00 52.03  ? 431 ASP C CB  1 
ATOM   9166  C  CG  . ASP C 1 430 ? 0.442   -1.604  12.950  1.00 56.28  ? 431 ASP C CG  1 
ATOM   9167  O  OD1 . ASP C 1 430 ? 0.139   -2.783  13.230  1.00 58.81  ? 431 ASP C OD1 1 
ATOM   9168  O  OD2 . ASP C 1 430 ? 1.337   -1.306  12.132  1.00 57.67  ? 431 ASP C OD2 1 
ATOM   9169  N  N   . GLY C 1 431 ? -2.330  0.401   15.912  1.00 45.94  ? 432 GLY C N   1 
ATOM   9170  C  CA  . GLY C 1 431 ? -2.869  1.516   16.670  1.00 41.07  ? 432 GLY C CA  1 
ATOM   9171  C  C   . GLY C 1 431 ? -4.175  1.212   17.375  1.00 42.86  ? 432 GLY C C   1 
ATOM   9172  O  O   . GLY C 1 431 ? -4.888  0.283   17.004  1.00 41.65  ? 432 GLY C O   1 
ATOM   9173  N  N   . LEU C 1 432 ? -4.486  2.009   18.392  1.00 49.56  ? 433 LEU C N   1 
ATOM   9174  C  CA  . LEU C 1 432 ? -5.692  1.824   19.193  1.00 49.15  ? 433 LEU C CA  1 
ATOM   9175  C  C   . LEU C 1 432 ? -6.962  1.906   18.349  1.00 50.67  ? 433 LEU C C   1 
ATOM   9176  O  O   . LEU C 1 432 ? -7.820  1.029   18.429  1.00 46.95  ? 433 LEU C O   1 
ATOM   9177  C  CB  . LEU C 1 432 ? -5.746  2.863   20.317  1.00 49.33  ? 433 LEU C CB  1 
ATOM   9178  C  CG  . LEU C 1 432 ? -6.914  2.766   21.301  1.00 48.10  ? 433 LEU C CG  1 
ATOM   9179  C  CD1 . LEU C 1 432 ? -6.912  1.421   22.009  1.00 46.02  ? 433 LEU C CD1 1 
ATOM   9180  C  CD2 . LEU C 1 432 ? -6.867  3.907   22.310  1.00 46.43  ? 433 LEU C CD2 1 
ATOM   9181  N  N   . ALA C 1 433 ? -7.064  2.956   17.539  1.00 53.79  ? 434 ALA C N   1 
ATOM   9182  C  CA  . ALA C 1 433 ? -8.246  3.199   16.715  1.00 55.43  ? 434 ALA C CA  1 
ATOM   9183  C  C   . ALA C 1 433 ? -8.568  2.024   15.792  1.00 58.68  ? 434 ALA C C   1 
ATOM   9184  O  O   . ALA C 1 433 ? -9.734  1.677   15.600  1.00 61.21  ? 434 ALA C O   1 
ATOM   9185  C  CB  . ALA C 1 433 ? -8.063  4.472   15.899  1.00 45.88  ? 434 ALA C CB  1 
ATOM   9186  N  N   . ASN C 1 434 ? -7.531  1.408   15.234  1.00 53.97  ? 435 ASN C N   1 
ATOM   9187  C  CA  . ASN C 1 434 ? -7.707  0.309   14.289  1.00 54.23  ? 435 ASN C CA  1 
ATOM   9188  C  C   . ASN C 1 434 ? -8.167  -0.992  14.941  1.00 44.01  ? 435 ASN C C   1 
ATOM   9189  O  O   . ASN C 1 434 ? -8.416  -1.980  14.251  1.00 48.42  ? 435 ASN C O   1 
ATOM   9190  C  CB  . ASN C 1 434 ? -6.406  0.060   13.522  1.00 48.88  ? 435 ASN C CB  1 
ATOM   9191  C  CG  . ASN C 1 434 ? -6.179  1.072   12.417  1.00 50.70  ? 435 ASN C CG  1 
ATOM   9192  O  OD1 . ASN C 1 434 ? -7.125  1.529   11.774  1.00 51.83  ? 435 ASN C OD1 1 
ATOM   9193  N  ND2 . ASN C 1 434 ? -4.920  1.430   12.190  1.00 44.63  ? 435 ASN C ND2 1 
ATOM   9194  N  N   . GLN C 1 435 ? -8.282  -0.994  16.265  1.00 43.58  ? 436 GLN C N   1 
ATOM   9195  C  CA  . GLN C 1 435 ? -8.672  -2.199  16.989  1.00 43.24  ? 436 GLN C CA  1 
ATOM   9196  C  C   . GLN C 1 435 ? -10.130 -2.170  17.438  1.00 44.12  ? 436 GLN C C   1 
ATOM   9197  O  O   . GLN C 1 435 ? -10.551 -3.010  18.233  1.00 61.04  ? 436 GLN C O   1 
ATOM   9198  C  CB  . GLN C 1 435 ? -7.772  -2.408  18.209  1.00 47.47  ? 436 GLN C CB  1 
ATOM   9199  C  CG  . GLN C 1 435 ? -6.285  -2.362  17.912  1.00 41.41  ? 436 GLN C CG  1 
ATOM   9200  C  CD  . GLN C 1 435 ? -5.886  -3.275  16.772  1.00 46.58  ? 436 GLN C CD  1 
ATOM   9201  O  OE1 . GLN C 1 435 ? -6.276  -4.443  16.730  1.00 41.28  ? 436 GLN C OE1 1 
ATOM   9202  N  NE2 . GLN C 1 435 ? -5.104  -2.747  15.838  1.00 46.05  ? 436 GLN C NE2 1 
ATOM   9203  N  N   . ILE C 1 436 ? -10.897 -1.208  16.937  1.00 58.26  ? 437 ILE C N   1 
ATOM   9204  C  CA  . ILE C 1 436 ? -12.295 -1.076  17.335  1.00 60.32  ? 437 ILE C CA  1 
ATOM   9205  C  C   . ILE C 1 436 ? -13.100 -2.312  16.918  1.00 51.31  ? 437 ILE C C   1 
ATOM   9206  O  O   . ILE C 1 436 ? -13.958 -2.789  17.663  1.00 50.31  ? 437 ILE C O   1 
ATOM   9207  C  CB  . ILE C 1 436 ? -12.934 0.212   16.743  1.00 47.52  ? 437 ILE C CB  1 
ATOM   9208  C  CG1 . ILE C 1 436 ? -14.412 0.314   17.128  1.00 51.97  ? 437 ILE C CG1 1 
ATOM   9209  C  CG2 . ILE C 1 436 ? -12.751 0.279   15.229  1.00 47.93  ? 437 ILE C CG2 1 
ATOM   9210  C  CD1 . ILE C 1 436 ? -15.105 1.539   16.570  1.00 50.24  ? 437 ILE C CD1 1 
ATOM   9211  N  N   . ASN C 1 437 ? -12.805 -2.827  15.729  1.00 55.04  ? 438 ASN C N   1 
ATOM   9212  C  CA  . ASN C 1 437 ? -13.478 -4.007  15.195  1.00 62.09  ? 438 ASN C CA  1 
ATOM   9213  C  C   . ASN C 1 437 ? -12.727 -5.323  15.425  1.00 61.29  ? 438 ASN C C   1 
ATOM   9214  O  O   . ASN C 1 437 ? -13.151 -6.368  14.932  1.00 63.18  ? 438 ASN C O   1 
ATOM   9215  C  CB  . ASN C 1 437 ? -13.746 -3.817  13.702  1.00 66.47  ? 438 ASN C CB  1 
ATOM   9216  C  CG  . ASN C 1 437 ? -14.651 -2.630  13.423  1.00 71.38  ? 438 ASN C CG  1 
ATOM   9217  O  OD1 . ASN C 1 437 ? -15.427 -2.213  14.283  1.00 70.58  ? 438 ASN C OD1 1 
ATOM   9218  N  ND2 . ASN C 1 437 ? -14.556 -2.082  12.217  1.00 73.48  ? 438 ASN C ND2 1 
ATOM   9219  N  N   . ASN C 1 438 ? -11.613 -5.267  16.153  1.00 58.83  ? 439 ASN C N   1 
ATOM   9220  C  CA  . ASN C 1 438 ? -10.746 -6.433  16.342  1.00 54.75  ? 439 ASN C CA  1 
ATOM   9221  C  C   . ASN C 1 438 ? -11.502 -7.625  16.930  1.00 51.37  ? 439 ASN C C   1 
ATOM   9222  O  O   . ASN C 1 438 ? -12.035 -7.548  18.036  1.00 48.88  ? 439 ASN C O   1 
ATOM   9223  C  CB  . ASN C 1 438 ? -9.561  -6.063  17.244  1.00 53.14  ? 439 ASN C CB  1 
ATOM   9224  C  CG  . ASN C 1 438 ? -8.470  -7.124  17.257  1.00 55.06  ? 439 ASN C CG  1 
ATOM   9225  O  OD1 . ASN C 1 438 ? -8.737  -8.316  17.413  1.00 52.83  ? 439 ASN C OD1 1 
ATOM   9226  N  ND2 . ASN C 1 438 ? -7.226  -6.687  17.097  1.00 52.98  ? 439 ASN C ND2 1 
ATOM   9227  N  N   . PRO C 1 439 ? -11.550 -8.735  16.177  1.00 49.00  ? 440 PRO C N   1 
ATOM   9228  C  CA  . PRO C 1 439 ? -12.337 -9.921  16.534  1.00 53.18  ? 440 PRO C CA  1 
ATOM   9229  C  C   . PRO C 1 439 ? -11.826 -10.683 17.757  1.00 56.15  ? 440 PRO C C   1 
ATOM   9230  O  O   . PRO C 1 439 ? -12.636 -11.181 18.539  1.00 60.12  ? 440 PRO C O   1 
ATOM   9231  C  CB  . PRO C 1 439 ? -12.230 -10.795 15.281  1.00 44.52  ? 440 PRO C CB  1 
ATOM   9232  C  CG  . PRO C 1 439 ? -10.946 -10.391 14.652  1.00 45.93  ? 440 PRO C CG  1 
ATOM   9233  C  CD  . PRO C 1 439 ? -10.813 -8.920  14.914  1.00 43.95  ? 440 PRO C CD  1 
ATOM   9234  N  N   . GLU C 1 440 ? -10.509 -10.780 17.913  1.00 52.23  ? 441 GLU C N   1 
ATOM   9235  C  CA  . GLU C 1 440 ? -9.941  -11.605 18.975  1.00 47.85  ? 441 GLU C CA  1 
ATOM   9236  C  C   . GLU C 1 440 ? -9.822  -10.874 20.306  1.00 48.17  ? 441 GLU C C   1 
ATOM   9237  O  O   . GLU C 1 440 ? -9.669  -11.500 21.353  1.00 51.82  ? 441 GLU C O   1 
ATOM   9238  C  CB  . GLU C 1 440 ? -8.563  -12.122 18.555  1.00 47.70  ? 441 GLU C CB  1 
ATOM   9239  C  CG  . GLU C 1 440 ? -8.479  -12.566 17.103  1.00 48.71  ? 441 GLU C CG  1 
ATOM   9240  C  CD  . GLU C 1 440 ? -9.435  -13.697 16.769  1.00 50.04  ? 441 GLU C CD  1 
ATOM   9241  O  OE1 . GLU C 1 440 ? -9.854  -14.428 17.692  1.00 49.60  ? 441 GLU C OE1 1 
ATOM   9242  O  OE2 . GLU C 1 440 ? -9.771  -13.852 15.577  1.00 52.75  ? 441 GLU C OE2 1 
ATOM   9243  N  N   . VAL C 1 441 ? -9.899  -9.548  20.264  1.00 50.21  ? 442 VAL C N   1 
ATOM   9244  C  CA  . VAL C 1 441 ? -9.759  -8.735  21.469  1.00 54.93  ? 442 VAL C CA  1 
ATOM   9245  C  C   . VAL C 1 441 ? -10.761 -7.593  21.456  1.00 58.18  ? 442 VAL C C   1 
ATOM   9246  O  O   . VAL C 1 441 ? -10.881 -6.879  20.461  1.00 60.54  ? 442 VAL C O   1 
ATOM   9247  C  CB  . VAL C 1 441 ? -8.338  -8.129  21.617  1.00 45.39  ? 442 VAL C CB  1 
ATOM   9248  C  CG1 . VAL C 1 441 ? -8.158  -7.543  23.010  1.00 40.69  ? 442 VAL C CG1 1 
ATOM   9249  C  CG2 . VAL C 1 441 ? -7.256  -9.163  21.338  1.00 40.15  ? 442 VAL C CG2 1 
ATOM   9250  N  N   . GLU C 1 442 ? -11.469 -7.405  22.563  1.00 64.67  ? 443 GLU C N   1 
ATOM   9251  C  CA  . GLU C 1 442 ? -12.369 -6.270  22.671  1.00 70.33  ? 443 GLU C CA  1 
ATOM   9252  C  C   . GLU C 1 442 ? -11.631 -5.113  23.322  1.00 68.91  ? 443 GLU C C   1 
ATOM   9253  O  O   . GLU C 1 442 ? -11.290 -5.160  24.504  1.00 66.65  ? 443 GLU C O   1 
ATOM   9254  C  CB  . GLU C 1 442 ? -13.621 -6.631  23.474  1.00 78.39  ? 443 GLU C CB  1 
ATOM   9255  C  CG  . GLU C 1 442 ? -14.872 -6.823  22.627  1.00 86.83  ? 443 GLU C CG  1 
ATOM   9256  C  CD  . GLU C 1 442 ? -15.514 -5.507  22.225  1.00 94.15  ? 443 GLU C CD  1 
ATOM   9257  O  OE1 . GLU C 1 442 ? -15.728 -4.654  23.112  1.00 97.91  ? 443 GLU C OE1 1 
ATOM   9258  O  OE2 . GLU C 1 442 ? -15.804 -5.325  21.022  1.00 96.56  ? 443 GLU C OE2 1 
ATOM   9259  N  N   . VAL C 1 443 ? -11.384 -4.073  22.534  1.00 67.09  ? 444 VAL C N   1 
ATOM   9260  C  CA  . VAL C 1 443 ? -10.697 -2.892  23.025  1.00 67.53  ? 444 VAL C CA  1 
ATOM   9261  C  C   . VAL C 1 443 ? -11.527 -1.667  22.664  1.00 65.76  ? 444 VAL C C   1 
ATOM   9262  O  O   . VAL C 1 443 ? -12.101 -1.587  21.575  1.00 68.79  ? 444 VAL C O   1 
ATOM   9263  C  CB  . VAL C 1 443 ? -9.249  -2.779  22.452  1.00 53.26  ? 444 VAL C CB  1 
ATOM   9264  C  CG1 . VAL C 1 443 ? -8.882  -4.024  21.653  1.00 52.88  ? 444 VAL C CG1 1 
ATOM   9265  C  CG2 . VAL C 1 443 ? -9.069  -1.523  21.608  1.00 53.79  ? 444 VAL C CG2 1 
ATOM   9266  N  N   . ASP C 1 444 ? -11.625 -0.733  23.602  1.00 65.38  ? 445 ASP C N   1 
ATOM   9267  C  CA  . ASP C 1 444 ? -12.336 0.508   23.350  1.00 67.17  ? 445 ASP C CA  1 
ATOM   9268  C  C   . ASP C 1 444 ? -11.332 1.601   23.022  1.00 64.33  ? 445 ASP C C   1 
ATOM   9269  O  O   . ASP C 1 444 ? -10.367 1.817   23.756  1.00 63.34  ? 445 ASP C O   1 
ATOM   9270  C  CB  . ASP C 1 444 ? -13.198 0.902   24.547  1.00 71.62  ? 445 ASP C CB  1 
ATOM   9271  C  CG  . ASP C 1 444 ? -13.938 2.204   24.325  1.00 78.07  ? 445 ASP C CG  1 
ATOM   9272  O  OD1 . ASP C 1 444 ? -14.870 2.226   23.493  1.00 80.72  ? 445 ASP C OD1 1 
ATOM   9273  O  OD2 . ASP C 1 444 ? -13.589 3.204   24.985  1.00 78.92  ? 445 ASP C OD2 1 
ATOM   9274  N  N   . ILE C 1 445 ? -11.569 2.285   21.910  1.00 62.51  ? 446 ILE C N   1 
ATOM   9275  C  CA  . ILE C 1 445 ? -10.618 3.251   21.382  1.00 58.77  ? 446 ILE C CA  1 
ATOM   9276  C  C   . ILE C 1 445 ? -10.741 4.609   22.070  1.00 59.15  ? 446 ILE C C   1 
ATOM   9277  O  O   . ILE C 1 445 ? -9.948  5.515   21.814  1.00 62.06  ? 446 ILE C O   1 
ATOM   9278  C  CB  . ILE C 1 445 ? -10.807 3.418   19.866  1.00 54.95  ? 446 ILE C CB  1 
ATOM   9279  C  CG1 . ILE C 1 445 ? -12.191 3.987   19.558  1.00 52.43  ? 446 ILE C CG1 1 
ATOM   9280  C  CG2 . ILE C 1 445 ? -10.663 2.077   19.176  1.00 59.33  ? 446 ILE C CG2 1 
ATOM   9281  C  CD1 . ILE C 1 445 ? -12.512 4.029   18.079  1.00 48.72  ? 446 ILE C CD1 1 
ATOM   9282  N  N   . THR C 1 446 ? -11.732 4.741   22.947  1.00 58.93  ? 447 THR C N   1 
ATOM   9283  C  CA  . THR C 1 446 ? -11.977 6.003   23.640  1.00 63.64  ? 447 THR C CA  1 
ATOM   9284  C  C   . THR C 1 446 ? -11.257 6.077   24.988  1.00 66.39  ? 447 THR C C   1 
ATOM   9285  O  O   . THR C 1 446 ? -11.388 7.062   25.715  1.00 71.92  ? 447 THR C O   1 
ATOM   9286  C  CB  . THR C 1 446 ? -13.486 6.236   23.860  1.00 57.09  ? 447 THR C CB  1 
ATOM   9287  O  OG1 . THR C 1 446 ? -13.949 5.420   24.942  1.00 50.45  ? 447 THR C OG1 1 
ATOM   9288  C  CG2 . THR C 1 446 ? -14.267 5.898   22.602  1.00 50.99  ? 447 THR C CG2 1 
ATOM   9289  N  N   . LYS C 1 447 ? -10.499 5.033   25.315  1.00 69.65  ? 448 LYS C N   1 
ATOM   9290  C  CA  . LYS C 1 447 ? -9.642  5.027   26.501  1.00 72.58  ? 448 LYS C CA  1 
ATOM   9291  C  C   . LYS C 1 447 ? -8.212  4.740   26.039  1.00 73.60  ? 448 LYS C C   1 
ATOM   9292  O  O   . LYS C 1 447 ? -7.814  3.580   25.913  1.00 73.77  ? 448 LYS C O   1 
ATOM   9293  C  CB  . LYS C 1 447 ? -10.138 3.986   27.529  1.00 73.62  ? 448 LYS C CB  1 
ATOM   9294  C  CG  . LYS C 1 447 ? -9.181  3.502   28.671  1.00 96.90  ? 448 LYS C CG  1 
ATOM   9295  C  CD  . LYS C 1 447 ? -8.069  4.462   29.114  1.00 96.53  ? 448 LYS C CD  1 
ATOM   9296  C  CE  . LYS C 1 447 ? -7.271  3.874   30.281  1.00 95.04  ? 448 LYS C CE  1 
ATOM   9297  N  NZ  . LYS C 1 447 ? -6.608  2.590   29.906  1.00 93.15  ? 448 LYS C NZ  1 
ATOM   9298  N  N   . PRO C 1 448 ? -7.457  5.803   25.722  1.00 71.59  ? 449 PRO C N   1 
ATOM   9299  C  CA  . PRO C 1 448 ? -6.000  5.728   25.593  1.00 71.36  ? 449 PRO C CA  1 
ATOM   9300  C  C   . PRO C 1 448 ? -5.336  5.652   26.964  1.00 69.64  ? 449 PRO C C   1 
ATOM   9301  O  O   . PRO C 1 448 ? -5.780  6.346   27.879  1.00 71.99  ? 449 PRO C O   1 
ATOM   9302  C  CB  . PRO C 1 448 ? -5.633  7.039   24.886  1.00 69.23  ? 449 PRO C CB  1 
ATOM   9303  C  CG  . PRO C 1 448 ? -6.927  7.598   24.369  1.00 70.88  ? 449 PRO C CG  1 
ATOM   9304  C  CD  . PRO C 1 448 ? -7.967  7.126   25.330  1.00 71.78  ? 449 PRO C CD  1 
ATOM   9305  N  N   . ASP C 1 449 ? -4.283  4.851   27.102  1.00 66.20  ? 450 ASP C N   1 
ATOM   9306  C  CA  . ASP C 1 449 ? -3.514  4.823   28.343  1.00 64.34  ? 450 ASP C CA  1 
ATOM   9307  C  C   . ASP C 1 449 ? -2.829  6.175   28.526  1.00 51.25  ? 450 ASP C C   1 
ATOM   9308  O  O   . ASP C 1 449 ? -2.272  6.722   27.576  1.00 51.34  ? 450 ASP C O   1 
ATOM   9309  C  CB  . ASP C 1 449 ? -2.490  3.685   28.322  1.00 67.71  ? 450 ASP C CB  1 
ATOM   9310  C  CG  . ASP C 1 449 ? -1.677  3.605   29.599  1.00 71.95  ? 450 ASP C CG  1 
ATOM   9311  O  OD1 . ASP C 1 449 ? -0.735  4.409   29.757  1.00 76.87  ? 450 ASP C OD1 1 
ATOM   9312  O  OD2 . ASP C 1 449 ? -1.975  2.734   30.444  1.00 72.42  ? 450 ASP C OD2 1 
ATOM   9313  N  N   . MET C 1 450 ? -2.875  6.716   29.740  1.00 50.56  ? 451 MET C N   1 
ATOM   9314  C  CA  . MET C 1 450 ? -2.373  8.068   29.984  1.00 55.30  ? 451 MET C CA  1 
ATOM   9315  C  C   . MET C 1 450 ? -0.847  8.147   30.002  1.00 52.38  ? 451 MET C C   1 
ATOM   9316  O  O   . MET C 1 450 ? -0.266  9.126   29.524  1.00 53.14  ? 451 MET C O   1 
ATOM   9317  C  CB  . MET C 1 450 ? -2.940  8.614   31.296  1.00 56.48  ? 451 MET C CB  1 
ATOM   9318  C  CG  . MET C 1 450 ? -4.330  9.225   31.162  1.00 62.78  ? 451 MET C CG  1 
ATOM   9319  S  SD  . MET C 1 450 ? -4.404  10.553  29.938  1.00 116.23 ? 451 MET C SD  1 
ATOM   9320  C  CE  . MET C 1 450 ? -5.254  9.742   28.585  1.00 58.58  ? 451 MET C CE  1 
ATOM   9321  N  N   . THR C 1 451 ? -0.203  7.124   30.557  1.00 48.16  ? 452 THR C N   1 
ATOM   9322  C  CA  . THR C 1 451 ? 1.255   7.057   30.573  1.00 50.29  ? 452 THR C CA  1 
ATOM   9323  C  C   . THR C 1 451 ? 1.792   7.136   29.146  1.00 52.00  ? 452 THR C C   1 
ATOM   9324  O  O   . THR C 1 451 ? 2.684   7.941   28.839  1.00 58.67  ? 452 THR C O   1 
ATOM   9325  C  CB  . THR C 1 451 ? 1.753   5.764   31.245  1.00 49.50  ? 452 THR C CB  1 
ATOM   9326  O  OG1 . THR C 1 451 ? 1.243   5.691   32.582  1.00 48.67  ? 452 THR C OG1 1 
ATOM   9327  C  CG2 . THR C 1 451 ? 3.273   5.730   31.282  1.00 48.49  ? 452 THR C CG2 1 
ATOM   9328  N  N   . ILE C 1 452 ? 1.218   6.305   28.281  1.00 52.06  ? 453 ILE C N   1 
ATOM   9329  C  CA  . ILE C 1 452 ? 1.527   6.312   26.857  1.00 52.07  ? 453 ILE C CA  1 
ATOM   9330  C  C   . ILE C 1 452 ? 1.365   7.708   26.263  1.00 54.56  ? 453 ILE C C   1 
ATOM   9331  O  O   . ILE C 1 452 ? 2.231   8.179   25.528  1.00 54.99  ? 453 ILE C O   1 
ATOM   9332  C  CB  . ILE C 1 452 ? 0.627   5.328   26.083  1.00 48.40  ? 453 ILE C CB  1 
ATOM   9333  C  CG1 . ILE C 1 452 ? 0.872   3.893   26.554  1.00 44.12  ? 453 ILE C CG1 1 
ATOM   9334  C  CG2 . ILE C 1 452 ? 0.862   5.450   24.586  1.00 47.36  ? 453 ILE C CG2 1 
ATOM   9335  C  CD1 . ILE C 1 452 ? 2.179   3.302   26.071  1.00 42.59  ? 453 ILE C CD1 1 
ATOM   9336  N  N   . ARG C 1 453 ? 0.257   8.364   26.597  1.00 57.71  ? 454 ARG C N   1 
ATOM   9337  C  CA  . ARG C 1 453 ? -0.017  9.719   26.119  1.00 63.51  ? 454 ARG C CA  1 
ATOM   9338  C  C   . ARG C 1 453 ? 1.092   10.694  26.495  1.00 62.30  ? 454 ARG C C   1 
ATOM   9339  O  O   . ARG C 1 453 ? 1.603   11.441  25.645  1.00 65.06  ? 454 ARG C O   1 
ATOM   9340  C  CB  . ARG C 1 453 ? -1.354  10.218  26.671  1.00 66.01  ? 454 ARG C CB  1 
ATOM   9341  C  CG  . ARG C 1 453 ? -2.558  9.611   25.983  1.00 70.18  ? 454 ARG C CG  1 
ATOM   9342  C  CD  . ARG C 1 453 ? -2.470  9.853   24.489  1.00 76.75  ? 454 ARG C CD  1 
ATOM   9343  N  NE  . ARG C 1 453 ? -3.465  9.094   23.742  1.00 81.69  ? 454 ARG C NE  1 
ATOM   9344  C  CZ  . ARG C 1 453 ? -3.461  8.961   22.421  1.00 88.07  ? 454 ARG C CZ  1 
ATOM   9345  N  NH1 . ARG C 1 453 ? -2.509  9.537   21.700  1.00 89.41  ? 454 ARG C NH1 1 
ATOM   9346  N  NH2 . ARG C 1 453 ? -4.406  8.251   21.820  1.00 89.58  ? 454 ARG C NH2 1 
ATOM   9347  N  N   . GLN C 1 454 ? 1.467   10.681  27.770  1.00 62.25  ? 455 GLN C N   1 
ATOM   9348  C  CA  . GLN C 1 454 ? 2.514   11.573  28.243  1.00 65.08  ? 455 GLN C CA  1 
ATOM   9349  C  C   . GLN C 1 454 ? 3.831   11.284  27.532  1.00 56.86  ? 455 GLN C C   1 
ATOM   9350  O  O   . GLN C 1 454 ? 4.552   12.209  27.147  1.00 55.05  ? 455 GLN C O   1 
ATOM   9351  C  CB  . GLN C 1 454 ? 2.691   11.456  29.757  1.00 70.98  ? 455 GLN C CB  1 
ATOM   9352  C  CG  . GLN C 1 454 ? 3.544   12.569  30.342  1.00 77.13  ? 455 GLN C CG  1 
ATOM   9353  C  CD  . GLN C 1 454 ? 3.156   13.937  29.807  1.00 83.13  ? 455 GLN C CD  1 
ATOM   9354  O  OE1 . GLN C 1 454 ? 3.991   14.666  29.269  1.00 82.55  ? 455 GLN C OE1 1 
ATOM   9355  N  NE2 . GLN C 1 454 ? 1.884   14.296  29.959  1.00 84.43  ? 455 GLN C NE2 1 
ATOM   9356  N  N   . GLN C 1 455 ? 4.137   10.003  27.342  1.00 53.76  ? 456 GLN C N   1 
ATOM   9357  C  CA  . GLN C 1 455 ? 5.361   9.640   26.632  1.00 51.86  ? 456 GLN C CA  1 
ATOM   9358  C  C   . GLN C 1 455 ? 5.343   10.152  25.189  1.00 52.62  ? 456 GLN C C   1 
ATOM   9359  O  O   . GLN C 1 455 ? 6.368   10.609  24.673  1.00 51.32  ? 456 GLN C O   1 
ATOM   9360  C  CB  . GLN C 1 455 ? 5.573   8.127   26.664  1.00 51.99  ? 456 GLN C CB  1 
ATOM   9361  C  CG  . GLN C 1 455 ? 5.728   7.575   28.071  1.00 51.23  ? 456 GLN C CG  1 
ATOM   9362  C  CD  . GLN C 1 455 ? 6.505   8.514   28.976  1.00 51.54  ? 456 GLN C CD  1 
ATOM   9363  O  OE1 . GLN C 1 455 ? 7.699   8.739   28.781  1.00 45.27  ? 456 GLN C OE1 1 
ATOM   9364  N  NE2 . GLN C 1 455 ? 5.825   9.074   29.970  1.00 59.17  ? 456 GLN C NE2 1 
ATOM   9365  N  N   . ILE C 1 456 ? 4.177   10.087  24.550  1.00 50.00  ? 457 ILE C N   1 
ATOM   9366  C  CA  . ILE C 1 456 ? 3.999   10.649  23.213  1.00 50.75  ? 457 ILE C CA  1 
ATOM   9367  C  C   . ILE C 1 456 ? 4.308   12.141  23.228  1.00 49.46  ? 457 ILE C C   1 
ATOM   9368  O  O   . ILE C 1 456 ? 5.033   12.650  22.360  1.00 53.66  ? 457 ILE C O   1 
ATOM   9369  C  CB  . ILE C 1 456 ? 2.564   10.430  22.680  1.00 52.35  ? 457 ILE C CB  1 
ATOM   9370  C  CG1 . ILE C 1 456 ? 2.289   8.941   22.469  1.00 52.65  ? 457 ILE C CG1 1 
ATOM   9371  C  CG2 . ILE C 1 456 ? 2.353   11.188  21.379  1.00 48.49  ? 457 ILE C CG2 1 
ATOM   9372  C  CD1 . ILE C 1 456 ? 0.910   8.644   21.919  1.00 54.85  ? 457 ILE C CD1 1 
ATOM   9373  N  N   . MET C 1 457 ? 3.761   12.834  24.224  1.00 50.93  ? 458 MET C N   1 
ATOM   9374  C  CA  . MET C 1 457 ? 4.037   14.258  24.398  1.00 50.12  ? 458 MET C CA  1 
ATOM   9375  C  C   . MET C 1 457 ? 5.543   14.521  24.480  1.00 47.18  ? 458 MET C C   1 
ATOM   9376  O  O   . MET C 1 457 ? 6.068   15.400  23.788  1.00 47.45  ? 458 MET C O   1 
ATOM   9377  C  CB  . MET C 1 457 ? 3.338   14.793  25.649  1.00 48.87  ? 458 MET C CB  1 
ATOM   9378  N  N   . GLN C 1 458 ? 6.230   13.744  25.315  1.00 47.73  ? 459 GLN C N   1 
ATOM   9379  C  CA  . GLN C 1 458 ? 7.679   13.873  25.471  1.00 48.16  ? 459 GLN C CA  1 
ATOM   9380  C  C   . GLN C 1 458 ? 8.411   13.691  24.142  1.00 47.22  ? 459 GLN C C   1 
ATOM   9381  O  O   . GLN C 1 458 ? 9.286   14.493  23.782  1.00 54.44  ? 459 GLN C O   1 
ATOM   9382  C  CB  . GLN C 1 458 ? 8.200   12.859  26.493  1.00 49.31  ? 459 GLN C CB  1 
ATOM   9383  C  CG  . GLN C 1 458 ? 7.543   12.945  27.866  1.00 54.42  ? 459 GLN C CG  1 
ATOM   9384  C  CD  . GLN C 1 458 ? 7.999   14.147  28.674  1.00 58.81  ? 459 GLN C CD  1 
ATOM   9385  O  OE1 . GLN C 1 458 ? 7.873   15.292  28.239  1.00 60.43  ? 459 GLN C OE1 1 
ATOM   9386  N  NE2 . GLN C 1 458 ? 8.530   13.889  29.863  1.00 62.19  ? 459 GLN C NE2 1 
ATOM   9387  N  N   . LEU C 1 459 ? 8.044   12.634  23.420  1.00 49.68  ? 460 LEU C N   1 
ATOM   9388  C  CA  . LEU C 1 459 ? 8.606   12.366  22.100  1.00 44.81  ? 460 LEU C CA  1 
ATOM   9389  C  C   . LEU C 1 459 ? 8.450   13.573  21.184  1.00 45.24  ? 460 LEU C C   1 
ATOM   9390  O  O   . LEU C 1 459 ? 9.401   13.982  20.511  1.00 46.20  ? 460 LEU C O   1 
ATOM   9391  C  CB  . LEU C 1 459 ? 7.940   11.144  21.463  1.00 41.69  ? 460 LEU C CB  1 
ATOM   9392  C  CG  . LEU C 1 459 ? 8.165   9.787   22.129  1.00 39.22  ? 460 LEU C CG  1 
ATOM   9393  C  CD1 . LEU C 1 459 ? 7.387   8.701   21.403  1.00 40.33  ? 460 LEU C CD1 1 
ATOM   9394  C  CD2 . LEU C 1 459 ? 9.643   9.451   22.173  1.00 38.80  ? 460 LEU C CD2 1 
ATOM   9395  N  N   . LYS C 1 460 ? 7.249   14.147  21.172  1.00 41.71  ? 461 LYS C N   1 
ATOM   9396  C  CA  . LYS C 1 460 ? 6.967   15.293  20.312  1.00 53.65  ? 461 LYS C CA  1 
ATOM   9397  C  C   . LYS C 1 460 ? 7.806   16.516  20.692  1.00 48.70  ? 461 LYS C C   1 
ATOM   9398  O  O   . LYS C 1 460 ? 8.358   17.197  19.818  1.00 44.13  ? 461 LYS C O   1 
ATOM   9399  C  CB  . LYS C 1 460 ? 5.477   15.636  20.356  1.00 54.58  ? 461 LYS C CB  1 
ATOM   9400  C  CG  . LYS C 1 460 ? 5.040   16.621  19.286  1.00 60.42  ? 461 LYS C CG  1 
ATOM   9401  C  CD  . LYS C 1 460 ? 3.548   16.512  19.016  1.00 69.79  ? 461 LYS C CD  1 
ATOM   9402  C  CE  . LYS C 1 460 ? 2.732   16.763  20.271  1.00 74.10  ? 461 LYS C CE  1 
ATOM   9403  N  NZ  . LYS C 1 460 ? 1.276   16.568  20.027  1.00 79.44  ? 461 LYS C NZ  1 
ATOM   9404  N  N   . ILE C 1 461 ? 7.907   16.788  21.992  1.00 52.55  ? 462 ILE C N   1 
ATOM   9405  C  CA  . ILE C 1 461 ? 8.723   17.903  22.474  1.00 53.08  ? 462 ILE C CA  1 
ATOM   9406  C  C   . ILE C 1 461 ? 10.184  17.750  22.050  1.00 53.10  ? 462 ILE C C   1 
ATOM   9407  O  O   . ILE C 1 461 ? 10.778  18.669  21.462  1.00 48.94  ? 462 ILE C O   1 
ATOM   9408  C  CB  . ILE C 1 461 ? 8.660   18.032  24.009  1.00 55.21  ? 462 ILE C CB  1 
ATOM   9409  C  CG1 . ILE C 1 461 ? 7.224   18.289  24.469  1.00 55.93  ? 462 ILE C CG1 1 
ATOM   9410  C  CG2 . ILE C 1 461 ? 9.579   19.144  24.491  1.00 54.67  ? 462 ILE C CG2 1 
ATOM   9411  C  CD1 . ILE C 1 461 ? 7.048   18.235  25.972  1.00 56.19  ? 462 ILE C CD1 1 
ATOM   9412  N  N   . MET C 1 462 ? 10.754  16.583  22.345  1.00 50.37  ? 463 MET C N   1 
ATOM   9413  C  CA  . MET C 1 462 ? 12.144  16.312  21.992  1.00 47.42  ? 463 MET C CA  1 
ATOM   9414  C  C   . MET C 1 462 ? 12.358  16.439  20.485  1.00 47.48  ? 463 MET C C   1 
ATOM   9415  O  O   . MET C 1 462 ? 13.376  16.974  20.033  1.00 47.14  ? 463 MET C O   1 
ATOM   9416  C  CB  . MET C 1 462 ? 12.560  14.920  22.473  1.00 43.22  ? 463 MET C CB  1 
ATOM   9417  C  CG  . MET C 1 462 ? 14.058  14.651  22.396  1.00 46.26  ? 463 MET C CG  1 
ATOM   9418  S  SD  . MET C 1 462 ? 15.037  15.753  23.441  1.00 49.95  ? 463 MET C SD  1 
ATOM   9419  C  CE  . MET C 1 462 ? 15.788  16.823  22.217  1.00 41.54  ? 463 MET C CE  1 
ATOM   9420  N  N   . THR C 1 463 ? 11.387  15.959  19.713  1.00 41.78  ? 464 THR C N   1 
ATOM   9421  C  CA  . THR C 1 463 ? 11.451  16.058  18.258  1.00 42.05  ? 464 THR C CA  1 
ATOM   9422  C  C   . THR C 1 463 ? 11.484  17.514  17.800  1.00 44.57  ? 464 THR C C   1 
ATOM   9423  O  O   . THR C 1 463 ? 12.272  17.876  16.922  1.00 43.26  ? 464 THR C O   1 
ATOM   9424  C  CB  . THR C 1 463 ? 10.262  15.344  17.591  1.00 42.06  ? 464 THR C CB  1 
ATOM   9425  O  OG1 . THR C 1 463 ? 10.260  13.964  17.971  1.00 42.69  ? 464 THR C OG1 1 
ATOM   9426  C  CG2 . THR C 1 463 ? 10.361  15.444  16.076  1.00 42.50  ? 464 THR C CG2 1 
ATOM   9427  N  N   . ASN C 1 464 ? 10.631  18.347  18.392  1.00 47.70  ? 465 ASN C N   1 
ATOM   9428  C  CA  . ASN C 1 464 ? 10.648  19.777  18.088  1.00 52.26  ? 465 ASN C CA  1 
ATOM   9429  C  C   . ASN C 1 464 ? 12.007  20.395  18.396  1.00 51.89  ? 465 ASN C C   1 
ATOM   9430  O  O   . ASN C 1 464 ? 12.564  21.144  17.578  1.00 48.10  ? 465 ASN C O   1 
ATOM   9431  C  CB  . ASN C 1 464 ? 9.554   20.514  18.862  1.00 58.32  ? 465 ASN C CB  1 
ATOM   9432  C  CG  . ASN C 1 464 ? 8.172   20.276  18.288  1.00 66.73  ? 465 ASN C CG  1 
ATOM   9433  O  OD1 . ASN C 1 464 ? 8.029   19.785  17.168  1.00 72.18  ? 465 ASN C OD1 1 
ATOM   9434  N  ND2 . ASN C 1 464 ? 7.145   20.633  19.050  1.00 68.00  ? 465 ASN C ND2 1 
ATOM   9435  N  N   . ARG C 1 465 ? 12.537  20.072  19.575  1.00 50.67  ? 466 ARG C N   1 
ATOM   9436  C  CA  . ARG C 1 465 ? 13.864  20.547  19.962  1.00 54.70  ? 466 ARG C CA  1 
ATOM   9437  C  C   . ARG C 1 465 ? 14.916  20.171  18.921  1.00 53.46  ? 466 ARG C C   1 
ATOM   9438  O  O   . ARG C 1 465 ? 15.737  21.000  18.529  1.00 53.66  ? 466 ARG C O   1 
ATOM   9439  C  CB  . ARG C 1 465 ? 14.270  19.986  21.326  1.00 57.93  ? 466 ARG C CB  1 
ATOM   9440  C  CG  . ARG C 1 465 ? 13.417  20.459  22.490  1.00 65.30  ? 466 ARG C CG  1 
ATOM   9441  C  CD  . ARG C 1 465 ? 14.115  20.182  23.814  1.00 71.74  ? 466 ARG C CD  1 
ATOM   9442  N  NE  . ARG C 1 465 ? 13.218  20.336  24.956  1.00 78.66  ? 466 ARG C NE  1 
ATOM   9443  C  CZ  . ARG C 1 465 ? 13.595  20.203  26.223  1.00 83.35  ? 466 ARG C CZ  1 
ATOM   9444  N  NH1 . ARG C 1 465 ? 14.856  19.917  26.516  1.00 84.87  ? 466 ARG C NH1 1 
ATOM   9445  N  NH2 . ARG C 1 465 ? 12.711  20.359  27.200  1.00 85.27  ? 466 ARG C NH2 1 
ATOM   9446  N  N   . LEU C 1 466 ? 14.876  18.921  18.471  1.00 51.44  ? 467 LEU C N   1 
ATOM   9447  C  CA  . LEU C 1 466 ? 15.854  18.421  17.507  1.00 47.03  ? 467 LEU C CA  1 
ATOM   9448  C  C   . LEU C 1 466 ? 15.709  19.055  16.125  1.00 47.12  ? 467 LEU C C   1 
ATOM   9449  O  O   . LEU C 1 466 ? 16.703  19.273  15.431  1.00 47.61  ? 467 LEU C O   1 
ATOM   9450  C  CB  . LEU C 1 466 ? 15.746  16.901  17.396  1.00 47.47  ? 467 LEU C CB  1 
ATOM   9451  C  CG  . LEU C 1 466 ? 16.473  16.140  18.503  1.00 46.86  ? 467 LEU C CG  1 
ATOM   9452  C  CD1 . LEU C 1 466 ? 15.835  14.788  18.732  1.00 43.36  ? 467 LEU C CD1 1 
ATOM   9453  C  CD2 . LEU C 1 466 ? 17.938  15.980  18.142  1.00 41.51  ? 467 LEU C CD2 1 
ATOM   9454  N  N   . ARG C 1 467 ? 14.476  19.346  15.726  1.00 51.27  ? 468 ARG C N   1 
ATOM   9455  C  CA  . ARG C 1 467 ? 14.232  19.978  14.433  1.00 53.33  ? 468 ARG C CA  1 
ATOM   9456  C  C   . ARG C 1 467 ? 14.714  21.427  14.440  1.00 55.77  ? 468 ARG C C   1 
ATOM   9457  O  O   . ARG C 1 467 ? 15.412  21.870  13.515  1.00 56.23  ? 468 ARG C O   1 
ATOM   9458  C  CB  . ARG C 1 467 ? 12.747  19.903  14.072  1.00 58.15  ? 468 ARG C CB  1 
ATOM   9459  C  CG  . ARG C 1 467 ? 12.280  18.500  13.703  1.00 60.48  ? 468 ARG C CG  1 
ATOM   9460  C  CD  . ARG C 1 467 ? 10.773  18.437  13.506  1.00 66.73  ? 468 ARG C CD  1 
ATOM   9461  N  NE  . ARG C 1 467 ? 10.347  17.140  12.987  1.00 71.09  ? 468 ARG C NE  1 
ATOM   9462  C  CZ  . ARG C 1 467 ? 9.078   16.758  12.876  1.00 69.46  ? 468 ARG C CZ  1 
ATOM   9463  N  NH1 . ARG C 1 467 ? 8.102   17.574  13.250  1.00 74.90  ? 468 ARG C NH1 1 
ATOM   9464  N  NH2 . ARG C 1 467 ? 8.784   15.558  12.392  1.00 63.92  ? 468 ARG C NH2 1 
ATOM   9465  N  N   . SER C 1 468 ? 14.351  22.158  15.491  1.00 58.76  ? 469 SER C N   1 
ATOM   9466  C  CA  . SER C 1 468 ? 14.816  23.534  15.642  1.00 63.06  ? 469 SER C CA  1 
ATOM   9467  C  C   . SER C 1 468 ? 16.340  23.588  15.702  1.00 66.06  ? 469 SER C C   1 
ATOM   9468  O  O   . SER C 1 468 ? 16.966  24.415  15.037  1.00 69.76  ? 469 SER C O   1 
ATOM   9469  C  CB  . SER C 1 468 ? 14.217  24.175  16.893  1.00 66.18  ? 469 SER C CB  1 
ATOM   9470  O  OG  . SER C 1 468 ? 12.942  24.727  16.619  1.00 72.04  ? 469 SER C OG  1 
ATOM   9471  N  N   . ALA C 1 469 ? 16.927  22.697  16.497  1.00 59.77  ? 470 ALA C N   1 
ATOM   9472  C  CA  . ALA C 1 469 ? 18.377  22.611  16.619  1.00 54.87  ? 470 ALA C CA  1 
ATOM   9473  C  C   . ALA C 1 469 ? 19.020  22.344  15.264  1.00 51.15  ? 470 ALA C C   1 
ATOM   9474  O  O   . ALA C 1 469 ? 20.018  22.970  14.909  1.00 53.85  ? 470 ALA C O   1 
ATOM   9475  C  CB  . ALA C 1 469 ? 18.766  21.528  17.612  1.00 52.97  ? 470 ALA C CB  1 
ATOM   9476  N  N   . TYR C 1 470 ? 18.437  21.414  14.511  1.00 51.75  ? 471 TYR C N   1 
ATOM   9477  C  CA  . TYR C 1 470 ? 18.925  21.094  13.175  1.00 52.99  ? 471 TYR C CA  1 
ATOM   9478  C  C   . TYR C 1 470 ? 18.902  22.323  12.278  1.00 58.52  ? 471 TYR C C   1 
ATOM   9479  O  O   . TYR C 1 470 ? 19.860  22.587  11.551  1.00 60.92  ? 471 TYR C O   1 
ATOM   9480  C  CB  . TYR C 1 470 ? 18.094  19.973  12.545  1.00 53.48  ? 471 TYR C CB  1 
ATOM   9481  C  CG  . TYR C 1 470 ? 18.495  19.643  11.123  1.00 52.83  ? 471 TYR C CG  1 
ATOM   9482  C  CD1 . TYR C 1 470 ? 19.550  18.780  10.860  1.00 54.66  ? 471 TYR C CD1 1 
ATOM   9483  C  CD2 . TYR C 1 470 ? 17.817  20.195  10.043  1.00 55.32  ? 471 TYR C CD2 1 
ATOM   9484  C  CE1 . TYR C 1 470 ? 19.920  18.478  9.562   1.00 56.18  ? 471 TYR C CE1 1 
ATOM   9485  C  CE2 . TYR C 1 470 ? 18.180  19.900  8.743   1.00 55.82  ? 471 TYR C CE2 1 
ATOM   9486  C  CZ  . TYR C 1 470 ? 19.231  19.040  8.508   1.00 55.08  ? 471 TYR C CZ  1 
ATOM   9487  O  OH  . TYR C 1 470 ? 19.593  18.742  7.215   1.00 55.23  ? 471 TYR C OH  1 
ATOM   9488  N  N   . ASN C 1 471 ? 17.808  23.076  12.330  1.00 68.14  ? 472 ASN C N   1 
ATOM   9489  C  CA  . ASN C 1 471 ? 17.695  24.275  11.505  1.00 76.72  ? 472 ASN C CA  1 
ATOM   9490  C  C   . ASN C 1 471 ? 18.573  25.426  11.985  1.00 83.66  ? 472 ASN C C   1 
ATOM   9491  O  O   . ASN C 1 471 ? 19.055  26.226  11.183  1.00 84.94  ? 472 ASN C O   1 
ATOM   9492  C  CB  . ASN C 1 471 ? 16.241  24.740  11.441  1.00 76.59  ? 472 ASN C CB  1 
ATOM   9493  C  CG  . ASN C 1 471 ? 15.426  23.955  10.438  1.00 78.06  ? 472 ASN C CG  1 
ATOM   9494  O  OD1 . ASN C 1 471 ? 15.917  23.599  9.367   1.00 79.01  ? 472 ASN C OD1 1 
ATOM   9495  N  ND2 . ASN C 1 471 ? 14.172  23.681  10.778  1.00 76.34  ? 472 ASN C ND2 1 
ATOM   9496  N  N   . GLY C 1 472 ? 18.785  25.503  13.293  1.00 90.41  ? 473 GLY C N   1 
ATOM   9497  C  CA  . GLY C 1 472 ? 19.461  26.643  13.882  1.00 98.78  ? 473 GLY C CA  1 
ATOM   9498  C  C   . GLY C 1 472 ? 18.422  27.569  14.479  1.00 107.28 ? 473 GLY C C   1 
ATOM   9499  O  O   . GLY C 1 472 ? 17.417  27.878  13.841  1.00 109.68 ? 473 GLY C O   1 
ATOM   9500  N  N   . ASN C 1 473 ? 18.657  28.013  15.706  1.00 110.99 ? 474 ASN C N   1 
ATOM   9501  C  CA  . ASN C 1 473 ? 17.645  28.765  16.433  1.00 113.44 ? 474 ASN C CA  1 
ATOM   9502  C  C   . ASN C 1 473 ? 18.240  29.785  17.397  1.00 113.79 ? 474 ASN C C   1 
ATOM   9503  O  O   . ASN C 1 473 ? 18.690  30.852  16.980  1.00 114.04 ? 474 ASN C O   1 
ATOM   9504  C  CB  . ASN C 1 473 ? 16.741  27.794  17.187  1.00 114.30 ? 474 ASN C CB  1 
ATOM   9505  C  CG  . ASN C 1 473 ? 17.484  27.035  18.264  1.00 115.48 ? 474 ASN C CG  1 
ATOM   9506  O  OD1 . ASN C 1 473 ? 18.121  26.016  17.993  1.00 114.48 ? 474 ASN C OD1 1 
ATOM   9507  N  ND2 . ASN C 1 473 ? 17.406  27.525  19.494  1.00 115.99 ? 474 ASN C ND2 1 
ATOM   9508  N  N   . SER D 1 28  ? -22.072 48.877  -21.435 1.00 78.74  ? 29  SER D N   1 
ATOM   9509  C  CA  . SER D 1 28  ? -23.012 49.446  -22.392 1.00 77.93  ? 29  SER D CA  1 
ATOM   9510  C  C   . SER D 1 28  ? -23.235 48.514  -23.583 1.00 77.93  ? 29  SER D C   1 
ATOM   9511  O  O   . SER D 1 28  ? -23.171 48.940  -24.736 1.00 86.38  ? 29  SER D O   1 
ATOM   9512  C  CB  . SER D 1 28  ? -22.521 50.813  -22.874 1.00 81.31  ? 29  SER D CB  1 
ATOM   9513  O  OG  . SER D 1 28  ? -21.221 50.723  -23.429 1.00 81.98  ? 29  SER D OG  1 
ATOM   9514  N  N   . ARG D 1 29  ? -23.475 47.240  -23.284 1.00 67.45  ? 30  ARG D N   1 
ATOM   9515  C  CA  . ARG D 1 29  ? -23.921 46.249  -24.266 1.00 66.41  ? 30  ARG D CA  1 
ATOM   9516  C  C   . ARG D 1 29  ? -22.977 46.033  -25.449 1.00 64.19  ? 30  ARG D C   1 
ATOM   9517  O  O   . ARG D 1 29  ? -23.415 45.614  -26.520 1.00 63.12  ? 30  ARG D O   1 
ATOM   9518  C  CB  . ARG D 1 29  ? -25.301 46.629  -24.810 1.00 59.59  ? 30  ARG D CB  1 
ATOM   9519  C  CG  . ARG D 1 29  ? -26.382 46.778  -23.758 1.00 59.75  ? 30  ARG D CG  1 
ATOM   9520  C  CD  . ARG D 1 29  ? -27.739 46.931  -24.420 1.00 59.55  ? 30  ARG D CD  1 
ATOM   9521  N  NE  . ARG D 1 29  ? -28.765 47.393  -23.491 1.00 60.67  ? 30  ARG D NE  1 
ATOM   9522  C  CZ  . ARG D 1 29  ? -30.036 47.587  -23.827 1.00 61.68  ? 30  ARG D CZ  1 
ATOM   9523  N  NH1 . ARG D 1 29  ? -30.436 47.354  -25.070 1.00 60.64  ? 30  ARG D NH1 1 
ATOM   9524  N  NH2 . ARG D 1 29  ? -30.908 48.011  -22.922 1.00 63.41  ? 30  ARG D NH2 1 
ATOM   9525  N  N   . SER D 1 30  ? -21.691 46.307  -25.266 1.00 70.53  ? 31  SER D N   1 
ATOM   9526  C  CA  . SER D 1 30  ? -20.722 46.047  -26.324 1.00 72.17  ? 31  SER D CA  1 
ATOM   9527  C  C   . SER D 1 30  ? -20.179 44.627  -26.201 1.00 66.97  ? 31  SER D C   1 
ATOM   9528  O  O   . SER D 1 30  ? -19.913 44.153  -25.097 1.00 64.83  ? 31  SER D O   1 
ATOM   9529  C  CB  . SER D 1 30  ? -19.579 47.063  -26.279 1.00 76.76  ? 31  SER D CB  1 
ATOM   9530  O  OG  . SER D 1 30  ? -18.710 46.900  -27.387 1.00 79.92  ? 31  SER D OG  1 
ATOM   9531  N  N   . CYS D 1 31  ? -20.027 43.947  -27.333 1.00 68.19  ? 32  CYS D N   1 
ATOM   9532  C  CA  A CYS D 1 31  ? -19.510 42.583  -27.330 0.64 70.73  ? 32  CYS D CA  1 
ATOM   9533  C  CA  B CYS D 1 31  ? -19.513 42.582  -27.349 0.36 70.72  ? 32  CYS D CA  1 
ATOM   9534  C  C   . CYS D 1 31  ? -18.057 42.535  -27.792 1.00 73.15  ? 32  CYS D C   1 
ATOM   9535  O  O   . CYS D 1 31  ? -17.552 41.478  -28.170 1.00 73.54  ? 32  CYS D O   1 
ATOM   9536  C  CB  A CYS D 1 31  ? -20.372 41.678  -28.213 0.64 69.08  ? 32  CYS D CB  1 
ATOM   9537  C  CB  B CYS D 1 31  ? -20.357 41.700  -28.271 0.36 69.41  ? 32  CYS D CB  1 
ATOM   9538  S  SG  A CYS D 1 31  ? -21.907 41.123  -27.434 0.64 67.34  ? 32  CYS D SG  1 
ATOM   9539  S  SG  B CYS D 1 31  ? -22.013 41.354  -27.659 0.36 67.58  ? 32  CYS D SG  1 
ATOM   9540  N  N   . GLY D 1 32  ? -17.389 43.683  -27.751 1.00 74.66  ? 33  GLY D N   1 
ATOM   9541  C  CA  . GLY D 1 32  ? -16.002 43.777  -28.170 1.00 74.95  ? 33  GLY D CA  1 
ATOM   9542  C  C   . GLY D 1 32  ? -15.065 42.917  -27.344 1.00 72.94  ? 33  GLY D C   1 
ATOM   9543  O  O   . GLY D 1 32  ? -14.261 42.158  -27.890 1.00 72.22  ? 33  GLY D O   1 
ATOM   9544  N  N   . GLU D 1 33  ? -15.173 43.037  -26.024 1.00 73.08  ? 34  GLU D N   1 
ATOM   9545  C  CA  . GLU D 1 33  ? -14.318 42.294  -25.105 1.00 73.14  ? 34  GLU D CA  1 
ATOM   9546  C  C   . GLU D 1 33  ? -14.492 40.790  -25.286 1.00 73.18  ? 34  GLU D C   1 
ATOM   9547  O  O   . GLU D 1 33  ? -13.512 40.055  -25.425 1.00 74.06  ? 34  GLU D O   1 
ATOM   9548  C  CB  . GLU D 1 33  ? -14.619 42.692  -23.658 1.00 75.86  ? 34  GLU D CB  1 
ATOM   9549  C  CG  . GLU D 1 33  ? -13.695 42.061  -22.631 1.00 78.93  ? 34  GLU D CG  1 
ATOM   9550  C  CD  . GLU D 1 33  ? -13.866 42.661  -21.249 1.00 84.67  ? 34  GLU D CD  1 
ATOM   9551  O  OE1 . GLU D 1 33  ? -14.592 43.670  -21.124 1.00 86.47  ? 34  GLU D OE1 1 
ATOM   9552  O  OE2 . GLU D 1 33  ? -13.276 42.124  -20.288 1.00 85.32  ? 34  GLU D OE2 1 
ATOM   9553  N  N   . VAL D 1 34  ? -15.744 40.342  -25.292 1.00 70.97  ? 35  VAL D N   1 
ATOM   9554  C  CA  . VAL D 1 34  ? -16.057 38.935  -25.509 1.00 69.14  ? 35  VAL D CA  1 
ATOM   9555  C  C   . VAL D 1 34  ? -15.549 38.476  -26.871 1.00 75.04  ? 35  VAL D C   1 
ATOM   9556  O  O   . VAL D 1 34  ? -15.039 37.368  -27.005 1.00 75.82  ? 35  VAL D O   1 
ATOM   9557  C  CB  . VAL D 1 34  ? -17.574 38.670  -25.401 1.00 66.85  ? 35  VAL D CB  1 
ATOM   9558  C  CG1 . VAL D 1 34  ? -17.932 37.303  -25.974 1.00 61.69  ? 35  VAL D CG1 1 
ATOM   9559  C  CG2 . VAL D 1 34  ? -18.026 38.787  -23.956 1.00 64.07  ? 35  VAL D CG2 1 
ATOM   9560  N  N   . ARG D 1 35  ? -15.676 39.338  -27.876 1.00 71.31  ? 36  ARG D N   1 
ATOM   9561  C  CA  . ARG D 1 35  ? -15.161 39.033  -29.207 1.00 74.81  ? 36  ARG D CA  1 
ATOM   9562  C  C   . ARG D 1 35  ? -13.654 38.795  -29.156 1.00 77.73  ? 36  ARG D C   1 
ATOM   9563  O  O   . ARG D 1 35  ? -13.135 37.891  -29.817 1.00 78.84  ? 36  ARG D O   1 
ATOM   9564  C  CB  . ARG D 1 35  ? -15.485 40.161  -30.188 1.00 69.96  ? 36  ARG D CB  1 
ATOM   9565  N  N   . GLN D 1 36  ? -12.958 39.601  -28.359 1.00 82.69  ? 37  GLN D N   1 
ATOM   9566  C  CA  . GLN D 1 36  ? -11.513 39.456  -28.214 1.00 83.64  ? 37  GLN D CA  1 
ATOM   9567  C  C   . GLN D 1 36  ? -11.160 38.165  -27.489 1.00 83.84  ? 37  GLN D C   1 
ATOM   9568  O  O   . GLN D 1 36  ? -10.372 37.383  -28.004 1.00 85.42  ? 37  GLN D O   1 
ATOM   9569  C  CB  . GLN D 1 36  ? -10.911 40.664  -27.484 1.00 84.96  ? 37  GLN D CB  1 
ATOM   9570  C  CG  . GLN D 1 36  ? -9.462  40.526  -26.939 1.00 107.60 ? 37  GLN D CG  1 
ATOM   9571  C  CD  . GLN D 1 36  ? -8.503  39.657  -27.763 1.00 109.03 ? 37  GLN D CD  1 
ATOM   9572  O  OE1 . GLN D 1 36  ? -8.600  39.566  -28.988 1.00 110.05 ? 37  GLN D OE1 1 
ATOM   9573  N  NE2 . GLN D 1 36  ? -7.565  39.016  -27.073 1.00 109.32 ? 37  GLN D NE2 1 
ATOM   9574  N  N   . ILE D 1 37  ? -11.723 37.939  -26.304 1.00 78.87  ? 38  ILE D N   1 
ATOM   9575  C  CA  . ILE D 1 37  ? -11.440 36.702  -25.573 1.00 74.07  ? 38  ILE D CA  1 
ATOM   9576  C  C   . ILE D 1 37  ? -11.719 35.487  -26.459 1.00 73.64  ? 38  ILE D C   1 
ATOM   9577  O  O   . ILE D 1 37  ? -10.959 34.520  -26.466 1.00 75.88  ? 38  ILE D O   1 
ATOM   9578  C  CB  . ILE D 1 37  ? -12.259 36.606  -24.263 1.00 68.52  ? 38  ILE D CB  1 
ATOM   9579  C  CG1 . ILE D 1 37  ? -11.571 37.398  -23.149 1.00 62.89  ? 38  ILE D CG1 1 
ATOM   9580  C  CG2 . ILE D 1 37  ? -12.417 35.158  -23.821 1.00 64.08  ? 38  ILE D CG2 1 
ATOM   9581  C  CD1 . ILE D 1 37  ? -12.221 38.721  -22.836 1.00 61.66  ? 38  ILE D CD1 1 
ATOM   9582  N  N   . TYR D 1 38  ? -12.788 35.573  -27.242 1.00 71.63  ? 39  TYR D N   1 
ATOM   9583  C  CA  . TYR D 1 38  ? -13.170 34.516  -28.170 1.00 69.01  ? 39  TYR D CA  1 
ATOM   9584  C  C   . TYR D 1 38  ? -12.117 34.308  -29.258 1.00 71.17  ? 39  TYR D C   1 
ATOM   9585  O  O   . TYR D 1 38  ? -11.757 33.174  -29.571 1.00 68.68  ? 39  TYR D O   1 
ATOM   9586  C  CB  . TYR D 1 38  ? -14.526 34.845  -28.801 1.00 62.30  ? 39  TYR D CB  1 
ATOM   9587  C  CG  . TYR D 1 38  ? -15.203 33.685  -29.491 1.00 56.03  ? 39  TYR D CG  1 
ATOM   9588  C  CD1 . TYR D 1 38  ? -15.607 32.566  -28.775 1.00 55.07  ? 39  TYR D CD1 1 
ATOM   9589  C  CD2 . TYR D 1 38  ? -15.464 33.720  -30.852 1.00 54.54  ? 39  TYR D CD2 1 
ATOM   9590  C  CE1 . TYR D 1 38  ? -16.237 31.506  -29.402 1.00 56.09  ? 39  TYR D CE1 1 
ATOM   9591  C  CE2 . TYR D 1 38  ? -16.097 32.668  -31.486 1.00 53.72  ? 39  TYR D CE2 1 
ATOM   9592  C  CZ  . TYR D 1 38  ? -16.477 31.564  -30.759 1.00 55.57  ? 39  TYR D CZ  1 
ATOM   9593  O  OH  . TYR D 1 38  ? -17.104 30.516  -31.393 1.00 59.75  ? 39  TYR D OH  1 
ATOM   9594  N  N   . GLY D 1 39  ? -11.622 35.404  -29.826 1.00 76.56  ? 40  GLY D N   1 
ATOM   9595  C  CA  . GLY D 1 39  ? -10.641 35.323  -30.896 1.00 82.07  ? 40  GLY D CA  1 
ATOM   9596  C  C   . GLY D 1 39  ? -9.251  34.911  -30.442 1.00 86.06  ? 40  GLY D C   1 
ATOM   9597  O  O   . GLY D 1 39  ? -8.475  34.352  -31.216 1.00 87.21  ? 40  GLY D O   1 
ATOM   9598  N  N   . ALA D 1 40  ? -8.939  35.186  -29.180 1.00 86.65  ? 41  ALA D N   1 
ATOM   9599  C  CA  . ALA D 1 40  ? -7.617  34.923  -28.624 1.00 86.47  ? 41  ALA D CA  1 
ATOM   9600  C  C   . ALA D 1 40  ? -7.440  33.447  -28.295 1.00 85.13  ? 41  ALA D C   1 
ATOM   9601  O  O   . ALA D 1 40  ? -6.315  32.963  -28.164 1.00 88.00  ? 41  ALA D O   1 
ATOM   9602  C  CB  . ALA D 1 40  ? -7.388  35.772  -27.386 1.00 84.88  ? 41  ALA D CB  1 
ATOM   9603  N  N   . LYS D 1 41  ? -8.557  32.741  -28.155 1.00 81.60  ? 42  LYS D N   1 
ATOM   9604  C  CA  . LYS D 1 41  ? -8.531  31.303  -27.912 1.00 78.71  ? 42  LYS D CA  1 
ATOM   9605  C  C   . LYS D 1 41  ? -8.584  30.544  -29.238 1.00 80.99  ? 42  LYS D C   1 
ATOM   9606  O  O   . LYS D 1 41  ? -8.729  29.321  -29.264 1.00 79.24  ? 42  LYS D O   1 
ATOM   9607  C  CB  . LYS D 1 41  ? -9.686  30.887  -26.992 1.00 76.09  ? 42  LYS D CB  1 
ATOM   9608  C  CG  . LYS D 1 41  ? -9.790  31.741  -25.733 1.00 76.92  ? 42  LYS D CG  1 
ATOM   9609  C  CD  . LYS D 1 41  ? -10.444 31.020  -24.567 1.00 75.42  ? 42  LYS D CD  1 
ATOM   9610  C  CE  . LYS D 1 41  ? -9.439  30.841  -23.438 1.00 77.14  ? 42  LYS D CE  1 
ATOM   9611  N  NZ  . LYS D 1 41  ? -9.512  31.945  -22.438 1.00 78.34  ? 42  LYS D NZ  1 
ATOM   9612  N  N   . GLY D 1 42  ? -8.461  31.286  -30.335 1.00 81.62  ? 43  GLY D N   1 
ATOM   9613  C  CA  . GLY D 1 42  ? -8.333  30.698  -31.656 1.00 83.80  ? 43  GLY D CA  1 
ATOM   9614  C  C   . GLY D 1 42  ? -9.596  30.718  -32.497 1.00 86.41  ? 43  GLY D C   1 
ATOM   9615  O  O   . GLY D 1 42  ? -9.561  30.396  -33.685 1.00 89.72  ? 43  GLY D O   1 
ATOM   9616  N  N   . PHE D 1 43  ? -10.713 31.094  -31.885 1.00 84.14  ? 44  PHE D N   1 
ATOM   9617  C  CA  . PHE D 1 43  ? -12.009 31.036  -32.555 1.00 83.32  ? 44  PHE D CA  1 
ATOM   9618  C  C   . PHE D 1 43  ? -12.266 32.190  -33.523 1.00 84.13  ? 44  PHE D C   1 
ATOM   9619  O  O   . PHE D 1 43  ? -11.692 33.272  -33.397 1.00 83.74  ? 44  PHE D O   1 
ATOM   9620  C  CB  . PHE D 1 43  ? -13.131 30.980  -31.521 1.00 79.07  ? 44  PHE D CB  1 
ATOM   9621  C  CG  . PHE D 1 43  ? -13.177 29.695  -30.753 1.00 77.81  ? 44  PHE D CG  1 
ATOM   9622  C  CD1 . PHE D 1 43  ? -13.505 28.510  -31.388 1.00 78.06  ? 44  PHE D CD1 1 
ATOM   9623  C  CD2 . PHE D 1 43  ? -12.903 29.670  -29.395 1.00 75.48  ? 44  PHE D CD2 1 
ATOM   9624  C  CE1 . PHE D 1 43  ? -13.546 27.321  -30.690 1.00 76.40  ? 44  PHE D CE1 1 
ATOM   9625  C  CE2 . PHE D 1 43  ? -12.948 28.483  -28.688 1.00 75.32  ? 44  PHE D CE2 1 
ATOM   9626  C  CZ  . PHE D 1 43  ? -13.272 27.307  -29.337 1.00 75.24  ? 44  PHE D CZ  1 
ATOM   9627  N  N   . SER D 1 44  ? -13.136 31.929  -34.494 1.00 89.02  ? 45  SER D N   1 
ATOM   9628  C  CA  . SER D 1 44  ? -13.536 32.912  -35.494 1.00 94.50  ? 45  SER D CA  1 
ATOM   9629  C  C   . SER D 1 44  ? -14.262 34.109  -34.888 1.00 94.44  ? 45  SER D C   1 
ATOM   9630  O  O   . SER D 1 44  ? -15.032 33.966  -33.945 1.00 91.50  ? 45  SER D O   1 
ATOM   9631  C  CB  . SER D 1 44  ? -14.436 32.250  -36.541 1.00 101.42 ? 45  SER D CB  1 
ATOM   9632  O  OG  . SER D 1 44  ? -15.802 32.365  -36.179 1.00 103.17 ? 45  SER D OG  1 
ATOM   9633  N  N   . LEU D 1 45  ? -14.022 35.291  -35.445 1.00 93.63  ? 46  LEU D N   1 
ATOM   9634  C  CA  . LEU D 1 45  ? -14.751 36.485  -35.034 1.00 94.79  ? 46  LEU D CA  1 
ATOM   9635  C  C   . LEU D 1 45  ? -15.970 36.672  -35.928 1.00 97.56  ? 46  LEU D C   1 
ATOM   9636  O  O   . LEU D 1 45  ? -16.688 37.665  -35.823 1.00 97.52  ? 46  LEU D O   1 
ATOM   9637  C  CB  . LEU D 1 45  ? -13.861 37.730  -35.082 1.00 91.60  ? 46  LEU D CB  1 
ATOM   9638  C  CG  . LEU D 1 45  ? -12.564 37.731  -34.270 1.00 87.26  ? 46  LEU D CG  1 
ATOM   9639  C  CD1 . LEU D 1 45  ? -11.410 37.118  -35.053 1.00 87.35  ? 46  LEU D CD1 1 
ATOM   9640  C  CD2 . LEU D 1 45  ? -12.220 39.143  -33.819 1.00 86.52  ? 46  LEU D CD2 1 
ATOM   9641  N  N   . SER D 1 46  ? -16.185 35.711  -36.820 1.00 104.44 ? 47  SER D N   1 
ATOM   9642  C  CA  . SER D 1 46  ? -17.278 35.776  -37.783 1.00 107.89 ? 47  SER D CA  1 
ATOM   9643  C  C   . SER D 1 46  ? -18.654 35.719  -37.125 1.00 108.64 ? 47  SER D C   1 
ATOM   9644  O  O   . SER D 1 46  ? -19.530 36.530  -37.429 1.00 109.67 ? 47  SER D O   1 
ATOM   9645  C  CB  . SER D 1 46  ? -17.149 34.638  -38.799 1.00 111.86 ? 47  SER D CB  1 
ATOM   9646  O  OG  . SER D 1 46  ? -18.304 34.548  -39.615 1.00 113.04 ? 47  SER D OG  1 
ATOM   9647  N  N   . ASP D 1 47  ? -18.841 34.759  -36.227 1.00 106.07 ? 48  ASP D N   1 
ATOM   9648  C  CA  . ASP D 1 47  ? -20.162 34.486  -35.674 1.00 102.41 ? 48  ASP D CA  1 
ATOM   9649  C  C   . ASP D 1 47  ? -20.447 35.197  -34.351 1.00 96.00  ? 48  ASP D C   1 
ATOM   9650  O  O   . ASP D 1 47  ? -21.508 35.001  -33.759 1.00 94.75  ? 48  ASP D O   1 
ATOM   9651  C  CB  . ASP D 1 47  ? -20.347 32.978  -35.503 1.00 104.35 ? 48  ASP D CB  1 
ATOM   9652  C  CG  . ASP D 1 47  ? -19.707 32.185  -36.627 1.00 106.36 ? 48  ASP D CG  1 
ATOM   9653  O  OD1 . ASP D 1 47  ? -19.869 32.584  -37.800 1.00 108.10 ? 48  ASP D OD1 1 
ATOM   9654  O  OD2 . ASP D 1 47  ? -19.048 31.163  -36.341 1.00 104.12 ? 48  ASP D OD2 1 
ATOM   9655  N  N   . VAL D 1 48  ? -19.510 36.017  -33.884 1.00 89.68  ? 49  VAL D N   1 
ATOM   9656  C  CA  . VAL D 1 48  ? -19.758 36.817  -32.688 1.00 85.04  ? 49  VAL D CA  1 
ATOM   9657  C  C   . VAL D 1 48  ? -20.437 38.136  -33.072 1.00 82.83  ? 49  VAL D C   1 
ATOM   9658  O  O   . VAL D 1 48  ? -19.981 38.839  -33.975 1.00 83.51  ? 49  VAL D O   1 
ATOM   9659  C  CB  . VAL D 1 48  ? -18.452 37.085  -31.891 1.00 67.32  ? 49  VAL D CB  1 
ATOM   9660  C  CG1 . VAL D 1 48  ? -17.376 37.679  -32.777 1.00 69.23  ? 49  VAL D CG1 1 
ATOM   9661  C  CG2 . VAL D 1 48  ? -18.723 37.986  -30.693 1.00 66.73  ? 49  VAL D CG2 1 
ATOM   9662  N  N   . PRO D 1 49  ? -21.554 38.459  -32.400 1.00 75.98  ? 50  PRO D N   1 
ATOM   9663  C  CA  . PRO D 1 49  ? -22.335 39.669  -32.687 1.00 76.62  ? 50  PRO D CA  1 
ATOM   9664  C  C   . PRO D 1 49  ? -21.646 40.951  -32.224 1.00 76.12  ? 50  PRO D C   1 
ATOM   9665  O  O   . PRO D 1 49  ? -20.719 40.892  -31.416 1.00 75.50  ? 50  PRO D O   1 
ATOM   9666  C  CB  . PRO D 1 49  ? -23.630 39.438  -31.903 1.00 73.76  ? 50  PRO D CB  1 
ATOM   9667  C  CG  . PRO D 1 49  ? -23.227 38.548  -30.780 1.00 71.63  ? 50  PRO D CG  1 
ATOM   9668  C  CD  . PRO D 1 49  ? -22.189 37.632  -31.358 1.00 72.98  ? 50  PRO D CD  1 
ATOM   9669  N  N   . GLN D 1 50  ? -22.095 42.093  -32.739 1.00 73.89  ? 51  GLN D N   1 
ATOM   9670  C  CA  . GLN D 1 50  ? -21.537 43.381  -32.339 1.00 72.02  ? 51  GLN D CA  1 
ATOM   9671  C  C   . GLN D 1 50  ? -21.982 43.763  -30.933 1.00 69.79  ? 51  GLN D C   1 
ATOM   9672  O  O   . GLN D 1 50  ? -21.179 44.219  -30.118 1.00 72.85  ? 51  GLN D O   1 
ATOM   9673  C  CB  . GLN D 1 50  ? -21.943 44.486  -33.316 1.00 74.55  ? 51  GLN D CB  1 
ATOM   9674  C  CG  . GLN D 1 50  ? -22.475 44.009  -34.653 1.00 75.67  ? 51  GLN D CG  1 
ATOM   9675  C  CD  . GLN D 1 50  ? -22.861 45.167  -35.554 1.00 83.07  ? 51  GLN D CD  1 
ATOM   9676  O  OE1 . GLN D 1 50  ? -22.073 46.089  -35.767 1.00 85.39  ? 51  GLN D OE1 1 
ATOM   9677  N  NE2 . GLN D 1 50  ? -24.078 45.132  -36.080 1.00 82.01  ? 51  GLN D NE2 1 
ATOM   9678  N  N   . ALA D 1 51  ? -23.271 43.582  -30.659 1.00 70.23  ? 52  ALA D N   1 
ATOM   9679  C  CA  . ALA D 1 51  ? -23.844 43.949  -29.370 1.00 69.93  ? 52  ALA D CA  1 
ATOM   9680  C  C   . ALA D 1 51  ? -24.690 42.813  -28.804 1.00 65.90  ? 52  ALA D C   1 
ATOM   9681  O  O   . ALA D 1 51  ? -25.023 41.865  -29.517 1.00 67.13  ? 52  ALA D O   1 
ATOM   9682  C  CB  . ALA D 1 51  ? -24.674 45.216  -29.501 1.00 67.12  ? 52  ALA D CB  1 
ATOM   9683  N  N   . GLU D 1 52  ? -25.019 42.912  -27.519 1.00 62.71  ? 53  GLU D N   1 
ATOM   9684  C  CA  . GLU D 1 52  ? -25.765 41.870  -26.816 1.00 58.56  ? 53  GLU D CA  1 
ATOM   9685  C  C   . GLU D 1 52  ? -27.088 41.533  -27.497 1.00 58.97  ? 53  GLU D C   1 
ATOM   9686  O  O   . GLU D 1 52  ? -27.815 42.422  -27.943 1.00 64.93  ? 53  GLU D O   1 
ATOM   9687  C  CB  . GLU D 1 52  ? -26.029 42.288  -25.368 1.00 55.88  ? 53  GLU D CB  1 
ATOM   9688  C  CG  . GLU D 1 52  ? -24.776 42.513  -24.541 1.00 57.09  ? 53  GLU D CG  1 
ATOM   9689  C  CD  . GLU D 1 52  ? -25.090 42.852  -23.097 1.00 61.02  ? 53  GLU D CD  1 
ATOM   9690  O  OE1 . GLU D 1 52  ? -26.273 43.110  -22.791 1.00 60.69  ? 53  GLU D OE1 1 
ATOM   9691  O  OE2 . GLU D 1 52  ? -24.155 42.861  -22.268 1.00 62.37  ? 53  GLU D OE2 1 
ATOM   9692  N  N   . ILE D 1 53  ? -27.388 40.241  -27.574 1.00 51.84  ? 54  ILE D N   1 
ATOM   9693  C  CA  . ILE D 1 53  ? -28.625 39.766  -28.181 1.00 56.71  ? 54  ILE D CA  1 
ATOM   9694  C  C   . ILE D 1 53  ? -29.437 38.948  -27.183 1.00 58.46  ? 54  ILE D C   1 
ATOM   9695  O  O   . ILE D 1 53  ? -29.016 38.754  -26.045 1.00 61.60  ? 54  ILE D O   1 
ATOM   9696  C  CB  . ILE D 1 53  ? -28.345 38.910  -29.427 1.00 58.47  ? 54  ILE D CB  1 
ATOM   9697  C  CG1 . ILE D 1 53  ? -27.465 37.713  -29.057 1.00 60.41  ? 54  ILE D CG1 1 
ATOM   9698  C  CG2 . ILE D 1 53  ? -27.683 39.749  -30.509 1.00 51.44  ? 54  ILE D CG2 1 
ATOM   9699  C  CD1 . ILE D 1 53  ? -27.000 36.903  -30.247 1.00 61.27  ? 54  ILE D CD1 1 
ATOM   9700  N  N   . SER D 1 54  ? -30.598 38.464  -27.616 1.00 61.70  ? 55  SER D N   1 
ATOM   9701  C  CA  . SER D 1 54  ? -31.460 37.657  -26.757 1.00 61.54  ? 55  SER D CA  1 
ATOM   9702  C  C   . SER D 1 54  ? -30.802 36.319  -26.437 1.00 64.91  ? 55  SER D C   1 
ATOM   9703  O  O   . SER D 1 54  ? -30.199 35.692  -27.307 1.00 64.14  ? 55  SER D O   1 
ATOM   9704  C  CB  . SER D 1 54  ? -32.822 37.434  -27.417 1.00 66.37  ? 55  SER D CB  1 
ATOM   9705  O  OG  . SER D 1 54  ? -33.637 36.586  -26.627 1.00 67.23  ? 55  SER D OG  1 
ATOM   9706  N  N   . GLY D 1 55  ? -30.924 35.887  -25.186 1.00 63.97  ? 56  GLY D N   1 
ATOM   9707  C  CA  . GLY D 1 55  ? -30.241 34.695  -24.716 1.00 66.59  ? 56  GLY D CA  1 
ATOM   9708  C  C   . GLY D 1 55  ? -31.097 33.448  -24.613 1.00 67.42  ? 56  GLY D C   1 
ATOM   9709  O  O   . GLY D 1 55  ? -30.759 32.519  -23.878 1.00 67.78  ? 56  GLY D O   1 
ATOM   9710  N  N   . GLU D 1 56  ? -32.206 33.422  -25.344 1.00 71.41  ? 57  GLU D N   1 
ATOM   9711  C  CA  . GLU D 1 56  ? -33.111 32.276  -25.319 1.00 71.51  ? 57  GLU D CA  1 
ATOM   9712  C  C   . GLU D 1 56  ? -32.503 31.051  -26.001 1.00 69.03  ? 57  GLU D C   1 
ATOM   9713  O  O   . GLU D 1 56  ? -33.040 29.947  -25.908 1.00 69.94  ? 57  GLU D O   1 
ATOM   9714  C  CB  . GLU D 1 56  ? -34.440 32.637  -25.986 1.00 74.56  ? 57  GLU D CB  1 
ATOM   9715  N  N   . HIS D 1 57  ? -31.381 31.254  -26.683 1.00 65.94  ? 58  HIS D N   1 
ATOM   9716  C  CA  . HIS D 1 57  ? -30.735 30.196  -27.452 1.00 65.56  ? 58  HIS D CA  1 
ATOM   9717  C  C   . HIS D 1 57  ? -29.647 29.462  -26.667 1.00 66.62  ? 58  HIS D C   1 
ATOM   9718  O  O   . HIS D 1 57  ? -28.968 28.591  -27.210 1.00 66.92  ? 58  HIS D O   1 
ATOM   9719  C  CB  . HIS D 1 57  ? -30.135 30.773  -28.735 1.00 67.55  ? 58  HIS D CB  1 
ATOM   9720  C  CG  . HIS D 1 57  ? -29.029 31.753  -28.493 1.00 71.50  ? 58  HIS D CG  1 
ATOM   9721  N  ND1 . HIS D 1 57  ? -29.233 32.966  -27.872 1.00 72.30  ? 58  HIS D ND1 1 
ATOM   9722  C  CD2 . HIS D 1 57  ? -27.708 31.695  -28.781 1.00 72.35  ? 58  HIS D CD2 1 
ATOM   9723  C  CE1 . HIS D 1 57  ? -28.085 33.615  -27.792 1.00 72.66  ? 58  HIS D CE1 1 
ATOM   9724  N  NE2 . HIS D 1 57  ? -27.144 32.865  -28.336 1.00 72.92  ? 58  HIS D NE2 1 
ATOM   9725  N  N   . LEU D 1 58  ? -29.481 29.808  -25.394 1.00 64.14  ? 59  LEU D N   1 
ATOM   9726  C  CA  . LEU D 1 58  ? -28.385 29.256  -24.602 1.00 59.80  ? 59  LEU D CA  1 
ATOM   9727  C  C   . LEU D 1 58  ? -28.770 27.942  -23.930 1.00 58.86  ? 59  LEU D C   1 
ATOM   9728  O  O   . LEU D 1 58  ? -29.660 27.900  -23.080 1.00 61.33  ? 59  LEU D O   1 
ATOM   9729  C  CB  . LEU D 1 58  ? -27.934 30.266  -23.545 1.00 58.62  ? 59  LEU D CB  1 
ATOM   9730  C  CG  . LEU D 1 58  ? -27.374 31.596  -24.052 1.00 56.21  ? 59  LEU D CG  1 
ATOM   9731  C  CD1 . LEU D 1 58  ? -27.267 32.597  -22.914 1.00 54.64  ? 59  LEU D CD1 1 
ATOM   9732  C  CD2 . LEU D 1 58  ? -26.020 31.388  -24.712 1.00 55.50  ? 59  LEU D CD2 1 
ATOM   9733  N  N   . ARG D 1 59  ? -28.083 26.872  -24.318 1.00 63.23  ? 60  ARG D N   1 
ATOM   9734  C  CA  . ARG D 1 59  ? -28.346 25.539  -23.785 1.00 61.65  ? 60  ARG D CA  1 
ATOM   9735  C  C   . ARG D 1 59  ? -27.706 25.312  -22.418 1.00 60.00  ? 60  ARG D C   1 
ATOM   9736  O  O   . ARG D 1 59  ? -28.230 24.561  -21.595 1.00 57.90  ? 60  ARG D O   1 
ATOM   9737  C  CB  . ARG D 1 59  ? -27.854 24.474  -24.768 1.00 63.72  ? 60  ARG D CB  1 
ATOM   9738  N  N   . ILE D 1 60  ? -26.572 25.963  -22.180 1.00 55.41  ? 61  ILE D N   1 
ATOM   9739  C  CA  . ILE D 1 60  ? -25.788 25.719  -20.975 1.00 52.97  ? 61  ILE D CA  1 
ATOM   9740  C  C   . ILE D 1 60  ? -25.834 26.907  -20.014 1.00 54.29  ? 61  ILE D C   1 
ATOM   9741  O  O   . ILE D 1 60  ? -26.329 26.786  -18.894 1.00 53.05  ? 61  ILE D O   1 
ATOM   9742  C  CB  . ILE D 1 60  ? -24.323 25.395  -21.322 1.00 48.74  ? 61  ILE D CB  1 
ATOM   9743  C  CG1 . ILE D 1 60  ? -24.261 24.184  -22.257 1.00 48.16  ? 61  ILE D CG1 1 
ATOM   9744  C  CG2 . ILE D 1 60  ? -23.523 25.134  -20.056 1.00 45.58  ? 61  ILE D CG2 1 
ATOM   9745  C  CD1 . ILE D 1 60  ? -22.858 23.691  -22.542 1.00 45.69  ? 61  ILE D CD1 1 
ATOM   9746  N  N   . CYS D 1 61  ? -25.299 28.044  -20.450 1.00 54.07  ? 62  CYS D N   1 
ATOM   9747  C  CA  . CYS D 1 61  ? -25.329 29.268  -19.654 1.00 52.99  ? 62  CYS D CA  1 
ATOM   9748  C  C   . CYS D 1 61  ? -26.759 29.661  -19.295 1.00 53.34  ? 62  CYS D C   1 
ATOM   9749  O  O   . CYS D 1 61  ? -27.689 29.383  -20.053 1.00 51.32  ? 62  CYS D O   1 
ATOM   9750  C  CB  . CYS D 1 61  ? -24.655 30.418  -20.408 1.00 52.78  ? 62  CYS D CB  1 
ATOM   9751  S  SG  . CYS D 1 61  ? -22.947 30.112  -20.898 1.00 75.42  ? 62  CYS D SG  1 
ATOM   9752  N  N   . PRO D 1 62  ? -26.939 30.299  -18.127 1.00 57.04  ? 63  PRO D N   1 
ATOM   9753  C  CA  . PRO D 1 62  ? -28.246 30.843  -17.744 1.00 59.68  ? 63  PRO D CA  1 
ATOM   9754  C  C   . PRO D 1 62  ? -28.772 31.821  -18.790 1.00 65.36  ? 63  PRO D C   1 
ATOM   9755  O  O   . PRO D 1 62  ? -28.005 32.631  -19.312 1.00 68.68  ? 63  PRO D O   1 
ATOM   9756  C  CB  . PRO D 1 62  ? -27.955 31.554  -16.421 1.00 57.59  ? 63  PRO D CB  1 
ATOM   9757  C  CG  . PRO D 1 62  ? -26.779 30.828  -15.864 1.00 56.08  ? 63  PRO D CG  1 
ATOM   9758  C  CD  . PRO D 1 62  ? -25.943 30.446  -17.052 1.00 54.05  ? 63  PRO D CD  1 
ATOM   9759  N  N   . GLN D 1 63  ? -30.061 31.736  -19.100 1.00 70.01  ? 64  GLN D N   1 
ATOM   9760  C  CA  . GLN D 1 63  ? -30.639 32.568  -20.147 1.00 71.45  ? 64  GLN D CA  1 
ATOM   9761  C  C   . GLN D 1 63  ? -30.720 34.032  -19.734 1.00 69.28  ? 64  GLN D C   1 
ATOM   9762  O  O   . GLN D 1 63  ? -31.089 34.361  -18.606 1.00 71.11  ? 64  GLN D O   1 
ATOM   9763  C  CB  . GLN D 1 63  ? -32.025 32.054  -20.539 1.00 78.65  ? 64  GLN D CB  1 
ATOM   9764  C  CG  . GLN D 1 63  ? -31.993 30.759  -21.333 1.00 84.64  ? 64  GLN D CG  1 
ATOM   9765  C  CD  . GLN D 1 63  ? -33.376 30.278  -21.721 1.00 90.91  ? 64  GLN D CD  1 
ATOM   9766  O  OE1 . GLN D 1 63  ? -34.384 30.801  -21.247 1.00 93.87  ? 64  GLN D OE1 1 
ATOM   9767  N  NE2 . GLN D 1 63  ? -33.431 29.279  -22.595 1.00 92.76  ? 64  GLN D NE2 1 
ATOM   9768  N  N   . GLY D 1 64  ? -30.365 34.901  -20.671 1.00 64.38  ? 65  GLY D N   1 
ATOM   9769  C  CA  . GLY D 1 64  ? -30.334 36.333  -20.451 1.00 61.05  ? 65  GLY D CA  1 
ATOM   9770  C  C   . GLY D 1 64  ? -29.571 36.934  -21.610 1.00 58.92  ? 65  GLY D C   1 
ATOM   9771  O  O   . GLY D 1 64  ? -28.923 36.203  -22.358 1.00 61.38  ? 65  GLY D O   1 
ATOM   9772  N  N   . TYR D 1 65  ? -29.632 38.252  -21.763 1.00 59.72  ? 66  TYR D N   1 
ATOM   9773  C  CA  . TYR D 1 65  ? -28.993 38.901  -22.902 1.00 58.58  ? 66  TYR D CA  1 
ATOM   9774  C  C   . TYR D 1 65  ? -27.490 38.637  -22.901 1.00 61.07  ? 66  TYR D C   1 
ATOM   9775  O  O   . TYR D 1 65  ? -26.805 38.868  -21.905 1.00 60.04  ? 66  TYR D O   1 
ATOM   9776  C  CB  . TYR D 1 65  ? -29.296 40.397  -22.901 1.00 59.12  ? 66  TYR D CB  1 
ATOM   9777  C  CG  . TYR D 1 65  ? -30.746 40.684  -23.218 1.00 59.08  ? 66  TYR D CG  1 
ATOM   9778  C  CD1 . TYR D 1 65  ? -31.200 40.688  -24.531 1.00 59.63  ? 66  TYR D CD1 1 
ATOM   9779  C  CD2 . TYR D 1 65  ? -31.665 40.925  -22.206 1.00 56.60  ? 66  TYR D CD2 1 
ATOM   9780  C  CE1 . TYR D 1 65  ? -32.526 40.937  -24.828 1.00 61.43  ? 66  TYR D CE1 1 
ATOM   9781  C  CE2 . TYR D 1 65  ? -32.995 41.177  -22.493 1.00 59.56  ? 66  TYR D CE2 1 
ATOM   9782  C  CZ  . TYR D 1 65  ? -33.419 41.181  -23.806 1.00 59.78  ? 66  TYR D CZ  1 
ATOM   9783  O  OH  . TYR D 1 65  ? -34.740 41.431  -24.100 1.00 61.99  ? 66  TYR D OH  1 
ATOM   9784  N  N   . THR D 1 66  ? -26.992 38.142  -24.030 1.00 58.39  ? 67  THR D N   1 
ATOM   9785  C  CA  . THR D 1 66  ? -25.663 37.547  -24.075 1.00 56.72  ? 67  THR D CA  1 
ATOM   9786  C  C   . THR D 1 66  ? -24.833 37.946  -25.288 1.00 54.39  ? 67  THR D C   1 
ATOM   9787  O  O   . THR D 1 66  ? -25.362 38.367  -26.316 1.00 54.31  ? 67  THR D O   1 
ATOM   9788  C  CB  . THR D 1 66  ? -25.756 36.010  -24.060 1.00 52.49  ? 67  THR D CB  1 
ATOM   9789  O  OG1 . THR D 1 66  ? -24.437 35.450  -24.113 1.00 52.21  ? 67  THR D OG1 1 
ATOM   9790  C  CG2 . THR D 1 66  ? -26.557 35.516  -25.254 1.00 46.15  ? 67  THR D CG2 1 
ATOM   9791  N  N   . CYS D 1 67  ? -23.519 37.815  -25.143 1.00 59.10  ? 68  CYS D N   1 
ATOM   9792  C  CA  A CYS D 1 67  ? -22.616 38.060  -26.262 0.49 59.90  ? 68  CYS D CA  1 
ATOM   9793  C  CA  B CYS D 1 67  ? -22.570 38.051  -26.222 0.51 59.96  ? 68  CYS D CA  1 
ATOM   9794  C  C   . CYS D 1 67  ? -22.267 36.758  -26.974 1.00 60.24  ? 68  CYS D C   1 
ATOM   9795  O  O   . CYS D 1 67  ? -21.584 36.766  -27.998 1.00 58.94  ? 68  CYS D O   1 
ATOM   9796  C  CB  A CYS D 1 67  ? -21.343 38.764  -25.788 0.49 59.61  ? 68  CYS D CB  1 
ATOM   9797  C  CB  B CYS D 1 67  ? -21.275 38.642  -25.664 0.51 59.58  ? 68  CYS D CB  1 
ATOM   9798  S  SG  A CYS D 1 67  ? -21.534 40.543  -25.523 0.49 69.27  ? 68  CYS D SG  1 
ATOM   9799  S  SG  B CYS D 1 67  ? -21.514 39.891  -24.377 0.51 69.67  ? 68  CYS D SG  1 
ATOM   9800  N  N   . CYS D 1 68  ? -22.765 35.646  -26.444 1.00 61.35  ? 69  CYS D N   1 
ATOM   9801  C  CA  . CYS D 1 68  ? -22.466 34.333  -27.004 1.00 66.17  ? 69  CYS D CA  1 
ATOM   9802  C  C   . CYS D 1 68  ? -23.621 33.753  -27.810 1.00 69.10  ? 69  CYS D C   1 
ATOM   9803  O  O   . CYS D 1 68  ? -24.733 33.604  -27.304 1.00 64.15  ? 69  CYS D O   1 
ATOM   9804  C  CB  . CYS D 1 68  ? -22.085 33.357  -25.887 1.00 66.63  ? 69  CYS D CB  1 
ATOM   9805  S  SG  . CYS D 1 68  ? -20.690 33.881  -24.863 1.00 71.68  ? 69  CYS D SG  1 
ATOM   9806  N  N   . THR D 1 69  ? -23.348 33.422  -29.068 1.00 73.18  ? 70  THR D N   1 
ATOM   9807  C  CA  . THR D 1 69  ? -24.299 32.676  -29.880 1.00 78.27  ? 70  THR D CA  1 
ATOM   9808  C  C   . THR D 1 69  ? -24.206 31.199  -29.510 1.00 84.20  ? 70  THR D C   1 
ATOM   9809  O  O   . THR D 1 69  ? -23.422 30.824  -28.639 1.00 86.05  ? 70  THR D O   1 
ATOM   9810  C  CB  . THR D 1 69  ? -24.044 32.861  -31.388 1.00 74.28  ? 70  THR D CB  1 
ATOM   9811  O  OG1 . THR D 1 69  ? -22.741 32.368  -31.721 1.00 71.90  ? 70  THR D OG1 1 
ATOM   9812  C  CG2 . THR D 1 69  ? -24.139 34.331  -31.769 1.00 74.50  ? 70  THR D CG2 1 
ATOM   9813  N  N   . SER D 1 70  ? -25.007 30.364  -30.164 1.00 92.57  ? 71  SER D N   1 
ATOM   9814  C  CA  . SER D 1 70  ? -25.005 28.931  -29.884 1.00 95.57  ? 71  SER D CA  1 
ATOM   9815  C  C   . SER D 1 70  ? -23.650 28.306  -30.209 1.00 96.20  ? 71  SER D C   1 
ATOM   9816  O  O   . SER D 1 70  ? -23.069 27.583  -29.389 1.00 98.91  ? 71  SER D O   1 
ATOM   9817  C  CB  . SER D 1 70  ? -26.112 28.231  -30.674 1.00 100.46 ? 71  SER D CB  1 
ATOM   9818  O  OG  . SER D 1 70  ? -26.082 26.831  -30.459 1.00 102.25 ? 71  SER D OG  1 
ATOM   9819  N  N   . GLU D 1 71  ? -23.156 28.597  -31.410 1.00 94.31  ? 72  GLU D N   1 
ATOM   9820  C  CA  . GLU D 1 71  ? -21.855 28.115  -31.856 1.00 92.01  ? 72  GLU D CA  1 
ATOM   9821  C  C   . GLU D 1 71  ? -20.761 28.538  -30.883 1.00 85.93  ? 72  GLU D C   1 
ATOM   9822  O  O   . GLU D 1 71  ? -19.927 27.724  -30.484 1.00 87.88  ? 72  GLU D O   1 
ATOM   9823  C  CB  . GLU D 1 71  ? -21.542 28.635  -33.262 1.00 93.04  ? 72  GLU D CB  1 
ATOM   9824  N  N   . MET D 1 72  ? -20.781 29.812  -30.501 1.00 78.96  ? 73  MET D N   1 
ATOM   9825  C  CA  . MET D 1 72  ? -19.841 30.343  -29.520 1.00 73.11  ? 73  MET D CA  1 
ATOM   9826  C  C   . MET D 1 72  ? -19.908 29.570  -28.208 1.00 69.12  ? 73  MET D C   1 
ATOM   9827  O  O   . MET D 1 72  ? -18.879 29.213  -27.632 1.00 72.00  ? 73  MET D O   1 
ATOM   9828  C  CB  . MET D 1 72  ? -20.117 31.823  -29.254 1.00 71.00  ? 73  MET D CB  1 
ATOM   9829  C  CG  . MET D 1 72  ? -19.802 32.746  -30.415 1.00 70.11  ? 73  MET D CG  1 
ATOM   9830  S  SD  . MET D 1 72  ? -20.067 34.472  -29.972 1.00 77.18  ? 73  MET D SD  1 
ATOM   9831  C  CE  . MET D 1 72  ? -19.054 34.605  -28.502 1.00 58.43  ? 73  MET D CE  1 
ATOM   9832  N  N   . GLU D 1 73  ? -21.128 29.314  -27.745 1.00 65.47  ? 74  GLU D N   1 
ATOM   9833  C  CA  . GLU D 1 73  ? -21.340 28.631  -26.475 1.00 63.16  ? 74  GLU D CA  1 
ATOM   9834  C  C   . GLU D 1 73  ? -20.771 27.216  -26.497 1.00 60.10  ? 74  GLU D C   1 
ATOM   9835  O  O   . GLU D 1 73  ? -20.014 26.833  -25.603 1.00 57.45  ? 74  GLU D O   1 
ATOM   9836  C  CB  . GLU D 1 73  ? -22.830 28.587  -26.128 1.00 60.21  ? 74  GLU D CB  1 
ATOM   9837  C  CG  . GLU D 1 73  ? -23.115 28.107  -24.712 1.00 60.88  ? 74  GLU D CG  1 
ATOM   9838  C  CD  . GLU D 1 73  ? -24.587 27.834  -24.469 1.00 60.31  ? 74  GLU D CD  1 
ATOM   9839  O  OE1 . GLU D 1 73  ? -25.271 27.375  -25.408 1.00 62.64  ? 74  GLU D OE1 1 
ATOM   9840  O  OE2 . GLU D 1 73  ? -25.060 28.080  -23.339 1.00 58.20  ? 74  GLU D OE2 1 
ATOM   9841  N  N   . GLU D 1 74  ? -21.132 26.444  -27.518 1.00 62.10  ? 75  GLU D N   1 
ATOM   9842  C  CA  . GLU D 1 74  ? -20.647 25.070  -27.628 1.00 63.93  ? 75  GLU D CA  1 
ATOM   9843  C  C   . GLU D 1 74  ? -19.128 25.027  -27.792 1.00 66.39  ? 75  GLU D C   1 
ATOM   9844  O  O   . GLU D 1 74  ? -18.447 24.197  -27.177 1.00 69.51  ? 75  GLU D O   1 
ATOM   9845  C  CB  . GLU D 1 74  ? -21.328 24.352  -28.794 1.00 65.38  ? 75  GLU D CB  1 
ATOM   9846  C  CG  . GLU D 1 74  ? -22.717 23.826  -28.467 1.00 64.69  ? 75  GLU D CG  1 
ATOM   9847  N  N   . ASN D 1 75  ? -18.604 25.927  -28.620 1.00 62.31  ? 76  ASN D N   1 
ATOM   9848  C  CA  . ASN D 1 75  ? -17.163 26.043  -28.821 1.00 64.99  ? 76  ASN D CA  1 
ATOM   9849  C  C   . ASN D 1 75  ? -16.423 26.297  -27.511 1.00 61.40  ? 76  ASN D C   1 
ATOM   9850  O  O   . ASN D 1 75  ? -15.441 25.619  -27.197 1.00 65.14  ? 76  ASN D O   1 
ATOM   9851  C  CB  . ASN D 1 75  ? -16.853 27.161  -29.818 1.00 67.08  ? 76  ASN D CB  1 
ATOM   9852  C  CG  . ASN D 1 75  ? -17.173 26.773  -31.250 1.00 72.94  ? 76  ASN D CG  1 
ATOM   9853  O  OD1 . ASN D 1 75  ? -17.982 25.879  -31.498 1.00 75.50  ? 76  ASN D OD1 1 
ATOM   9854  N  ND2 . ASN D 1 75  ? -16.539 27.449  -32.201 1.00 74.12  ? 76  ASN D ND2 1 
ATOM   9855  N  N   . LEU D 1 76  ? -16.906 27.273  -26.748 1.00 60.02  ? 77  LEU D N   1 
ATOM   9856  C  CA  . LEU D 1 76  ? -16.318 27.599  -25.453 1.00 56.20  ? 77  LEU D CA  1 
ATOM   9857  C  C   . LEU D 1 76  ? -16.461 26.446  -24.464 1.00 56.51  ? 77  LEU D C   1 
ATOM   9858  O  O   . LEU D 1 76  ? -15.606 26.252  -23.599 1.00 56.29  ? 77  LEU D O   1 
ATOM   9859  C  CB  . LEU D 1 76  ? -16.957 28.865  -24.878 1.00 55.04  ? 77  LEU D CB  1 
ATOM   9860  C  CG  . LEU D 1 76  ? -16.508 30.195  -25.486 1.00 56.77  ? 77  LEU D CG  1 
ATOM   9861  C  CD1 . LEU D 1 76  ? -17.420 31.326  -25.036 1.00 57.90  ? 77  LEU D CD1 1 
ATOM   9862  C  CD2 . LEU D 1 76  ? -15.063 30.490  -25.114 1.00 54.37  ? 77  LEU D CD2 1 
ATOM   9863  N  N   . ALA D 1 77  ? -17.544 25.684  -24.592 1.00 53.84  ? 78  ALA D N   1 
ATOM   9864  C  CA  . ALA D 1 77  ? -17.765 24.524  -23.735 1.00 58.58  ? 78  ALA D CA  1 
ATOM   9865  C  C   . ALA D 1 77  ? -16.706 23.455  -23.991 1.00 60.08  ? 78  ALA D C   1 
ATOM   9866  O  O   . ALA D 1 77  ? -16.041 22.983  -23.058 1.00 61.13  ? 78  ALA D O   1 
ATOM   9867  C  CB  . ALA D 1 77  ? -19.159 23.958  -23.955 1.00 54.03  ? 78  ALA D CB  1 
ATOM   9868  N  N   . ASN D 1 78  ? -16.548 23.081  -25.259 1.00 64.72  ? 79  ASN D N   1 
ATOM   9869  C  CA  . ASN D 1 78  ? -15.516 22.123  -25.642 1.00 67.47  ? 79  ASN D CA  1 
ATOM   9870  C  C   . ASN D 1 78  ? -14.127 22.629  -25.266 1.00 66.26  ? 79  ASN D C   1 
ATOM   9871  O  O   . ASN D 1 78  ? -13.246 21.846  -24.900 1.00 67.79  ? 79  ASN D O   1 
ATOM   9872  C  CB  . ASN D 1 78  ? -15.581 21.824  -27.141 1.00 76.26  ? 79  ASN D CB  1 
ATOM   9873  C  CG  . ASN D 1 78  ? -16.794 20.994  -27.519 1.00 82.96  ? 79  ASN D CG  1 
ATOM   9874  O  OD1 . ASN D 1 78  ? -17.360 20.287  -26.685 1.00 85.75  ? 79  ASN D OD1 1 
ATOM   9875  N  ND2 . ASN D 1 78  ? -17.195 21.073  -28.783 1.00 85.60  ? 79  ASN D ND2 1 
ATOM   9876  N  N   . ARG D 1 79  ? -13.942 23.944  -25.347 1.00 59.56  ? 80  ARG D N   1 
ATOM   9877  C  CA  . ARG D 1 79  ? -12.680 24.562  -24.956 1.00 57.65  ? 80  ARG D CA  1 
ATOM   9878  C  C   . ARG D 1 79  ? -12.390 24.353  -23.471 1.00 58.05  ? 80  ARG D C   1 
ATOM   9879  O  O   . ARG D 1 79  ? -11.330 23.839  -23.113 1.00 60.87  ? 80  ARG D O   1 
ATOM   9880  C  CB  . ARG D 1 79  ? -12.690 26.056  -25.294 1.00 54.35  ? 80  ARG D CB  1 
ATOM   9881  C  CG  . ARG D 1 79  ? -11.539 26.870  -24.697 1.00 54.82  ? 80  ARG D CG  1 
ATOM   9882  C  CD  . ARG D 1 79  ? -10.164 26.254  -24.958 1.00 58.54  ? 80  ARG D CD  1 
ATOM   9883  N  NE  . ARG D 1 79  ? -10.017 25.733  -26.315 1.00 63.23  ? 80  ARG D NE  1 
ATOM   9884  C  CZ  . ARG D 1 79  ? -9.459  26.400  -27.318 1.00 65.90  ? 80  ARG D CZ  1 
ATOM   9885  N  NH1 . ARG D 1 79  ? -8.989  27.625  -27.124 1.00 67.63  ? 80  ARG D NH1 1 
ATOM   9886  N  NH2 . ARG D 1 79  ? -9.370  25.841  -28.517 1.00 66.65  ? 80  ARG D NH2 1 
ATOM   9887  N  N   . SER D 1 80  ? -13.325 24.754  -22.614 1.00 53.85  ? 81  SER D N   1 
ATOM   9888  C  CA  . SER D 1 80  ? -13.154 24.601  -21.172 1.00 50.32  ? 81  SER D CA  1 
ATOM   9889  C  C   . SER D 1 80  ? -12.940 23.135  -20.802 1.00 48.18  ? 81  SER D C   1 
ATOM   9890  O  O   . SER D 1 80  ? -12.089 22.809  -19.961 1.00 55.12  ? 81  SER D O   1 
ATOM   9891  C  CB  . SER D 1 80  ? -14.362 25.166  -20.423 1.00 45.74  ? 81  SER D CB  1 
ATOM   9892  O  OG  . SER D 1 80  ? -15.548 24.469  -20.760 1.00 46.43  ? 81  SER D OG  1 
ATOM   9893  N  N   . HIS D 1 81  ? -13.709 22.259  -21.444 1.00 48.21  ? 82  HIS D N   1 
ATOM   9894  C  CA  . HIS D 1 81  ? -13.557 20.820  -21.251 1.00 51.31  ? 82  HIS D CA  1 
ATOM   9895  C  C   . HIS D 1 81  ? -12.128 20.373  -21.566 1.00 51.95  ? 82  HIS D C   1 
ATOM   9896  O  O   . HIS D 1 81  ? -11.499 19.655  -20.780 1.00 51.40  ? 82  HIS D O   1 
ATOM   9897  C  CB  . HIS D 1 81  ? -14.556 20.059  -22.125 1.00 61.13  ? 82  HIS D CB  1 
ATOM   9898  C  CG  . HIS D 1 81  ? -14.519 18.575  -21.935 1.00 69.84  ? 82  HIS D CG  1 
ATOM   9899  N  ND1 . HIS D 1 81  ? -13.578 17.769  -22.539 1.00 72.90  ? 82  HIS D ND1 1 
ATOM   9900  C  CD2 . HIS D 1 81  ? -15.311 17.750  -21.211 1.00 71.70  ? 82  HIS D CD2 1 
ATOM   9901  C  CE1 . HIS D 1 81  ? -13.791 16.512  -22.194 1.00 75.61  ? 82  HIS D CE1 1 
ATOM   9902  N  NE2 . HIS D 1 81  ? -14.837 16.473  -21.388 1.00 74.86  ? 82  HIS D NE2 1 
ATOM   9903  N  N   . ALA D 1 82  ? -11.621 20.815  -22.714 1.00 48.27  ? 83  ALA D N   1 
ATOM   9904  C  CA  . ALA D 1 82  ? -10.271 20.469  -23.147 1.00 48.28  ? 83  ALA D CA  1 
ATOM   9905  C  C   . ALA D 1 82  ? -9.212  20.996  -22.182 1.00 50.45  ? 83  ALA D C   1 
ATOM   9906  O  O   . ALA D 1 82  ? -8.210  20.327  -21.924 1.00 49.60  ? 83  ALA D O   1 
ATOM   9907  C  CB  . ALA D 1 82  ? -10.015 21.001  -24.548 1.00 44.85  ? 83  ALA D CB  1 
ATOM   9908  N  N   . GLU D 1 83  ? -9.435  22.196  -21.657 1.00 46.32  ? 84  GLU D N   1 
ATOM   9909  C  CA  . GLU D 1 83  ? -8.507  22.805  -20.709 1.00 49.29  ? 84  GLU D CA  1 
ATOM   9910  C  C   . GLU D 1 83  ? -8.449  21.988  -19.418 1.00 44.47  ? 84  GLU D C   1 
ATOM   9911  O  O   . GLU D 1 83  ? -7.360  21.684  -18.899 1.00 42.96  ? 84  GLU D O   1 
ATOM   9912  C  CB  . GLU D 1 83  ? -8.917  24.252  -20.420 1.00 51.89  ? 84  GLU D CB  1 
ATOM   9913  C  CG  . GLU D 1 83  ? -8.801  25.176  -21.629 1.00 58.54  ? 84  GLU D CG  1 
ATOM   9914  C  CD  . GLU D 1 83  ? -9.375  26.559  -21.378 1.00 64.64  ? 84  GLU D CD  1 
ATOM   9915  O  OE1 . GLU D 1 83  ? -10.245 26.694  -20.493 1.00 66.42  ? 84  GLU D OE1 1 
ATOM   9916  O  OE2 . GLU D 1 83  ? -8.962  27.513  -22.073 1.00 65.59  ? 84  GLU D OE2 1 
ATOM   9917  N  N   . LEU D 1 84  ? -9.626  21.621  -18.914 1.00 43.65  ? 85  LEU D N   1 
ATOM   9918  C  CA  . LEU D 1 84  ? -9.713  20.789  -17.717 1.00 46.99  ? 85  LEU D CA  1 
ATOM   9919  C  C   . LEU D 1 84  ? -9.006  19.448  -17.925 1.00 46.49  ? 85  LEU D C   1 
ATOM   9920  O  O   . LEU D 1 84  ? -8.186  19.031  -17.095 1.00 46.13  ? 85  LEU D O   1 
ATOM   9921  C  CB  . LEU D 1 84  ? -11.173 20.562  -17.324 1.00 42.41  ? 85  LEU D CB  1 
ATOM   9922  C  CG  . LEU D 1 84  ? -11.385 19.795  -16.017 1.00 47.91  ? 85  LEU D CG  1 
ATOM   9923  C  CD1 . LEU D 1 84  ? -10.628 20.463  -14.880 1.00 46.19  ? 85  LEU D CD1 1 
ATOM   9924  C  CD2 . LEU D 1 84  ? -12.862 19.691  -15.685 1.00 47.85  ? 85  LEU D CD2 1 
ATOM   9925  N  N   . GLU D 1 85  ? -9.325  18.786  -19.036 1.00 45.64  ? 86  GLU D N   1 
ATOM   9926  C  CA  . GLU D 1 85  ? -8.675  17.527  -19.397 1.00 52.20  ? 86  GLU D CA  1 
ATOM   9927  C  C   . GLU D 1 85  ? -7.156  17.674  -19.399 1.00 51.34  ? 86  GLU D C   1 
ATOM   9928  O  O   . GLU D 1 85  ? -6.436  16.843  -18.837 1.00 54.81  ? 86  GLU D O   1 
ATOM   9929  C  CB  . GLU D 1 85  ? -9.151  17.045  -20.772 1.00 57.78  ? 86  GLU D CB  1 
ATOM   9930  C  CG  . GLU D 1 85  ? -10.581 16.525  -20.814 1.00 64.22  ? 86  GLU D CG  1 
ATOM   9931  C  CD  . GLU D 1 85  ? -10.713 15.092  -20.324 1.00 69.80  ? 86  GLU D CD  1 
ATOM   9932  O  OE1 . GLU D 1 85  ? -11.759 14.466  -20.599 1.00 72.35  ? 86  GLU D OE1 1 
ATOM   9933  O  OE2 . GLU D 1 85  ? -9.777  14.587  -19.669 1.00 72.61  ? 86  GLU D OE2 1 
ATOM   9934  N  N   . THR D 1 86  ? -6.685  18.747  -20.029 1.00 55.09  ? 87  THR D N   1 
ATOM   9935  C  CA  . THR D 1 86  ? -5.261  19.049  -20.117 1.00 54.82  ? 87  THR D CA  1 
ATOM   9936  C  C   . THR D 1 86  ? -4.620  19.147  -18.733 1.00 56.48  ? 87  THR D C   1 
ATOM   9937  O  O   . THR D 1 86  ? -3.599  18.497  -18.465 1.00 57.02  ? 87  THR D O   1 
ATOM   9938  C  CB  . THR D 1 86  ? -5.024  20.364  -20.890 1.00 55.75  ? 87  THR D CB  1 
ATOM   9939  O  OG1 . THR D 1 86  ? -5.253  20.143  -22.287 1.00 56.11  ? 87  THR D OG1 1 
ATOM   9940  C  CG2 . THR D 1 86  ? -3.598  20.857  -20.697 1.00 56.90  ? 87  THR D CG2 1 
ATOM   9941  N  N   . ALA D 1 87  ? -5.224  19.949  -17.857 1.00 54.17  ? 88  ALA D N   1 
ATOM   9942  C  CA  . ALA D 1 87  ? -4.726  20.081  -16.487 1.00 54.30  ? 88  ALA D CA  1 
ATOM   9943  C  C   . ALA D 1 87  ? -4.641  18.718  -15.790 1.00 58.41  ? 88  ALA D C   1 
ATOM   9944  O  O   . ALA D 1 87  ? -3.585  18.339  -15.240 1.00 60.21  ? 88  ALA D O   1 
ATOM   9945  C  CB  . ALA D 1 87  ? -5.611  21.027  -15.693 1.00 49.81  ? 88  ALA D CB  1 
ATOM   9946  N  N   . LEU D 1 88  ? -5.757  17.989  -15.833 1.00 58.42  ? 89  LEU D N   1 
ATOM   9947  C  CA  . LEU D 1 88  ? -5.835  16.640  -15.272 1.00 60.20  ? 89  LEU D CA  1 
ATOM   9948  C  C   . LEU D 1 88  ? -4.666  15.767  -15.708 1.00 60.76  ? 89  LEU D C   1 
ATOM   9949  O  O   . LEU D 1 88  ? -3.902  15.261  -14.877 1.00 60.67  ? 89  LEU D O   1 
ATOM   9950  C  CB  . LEU D 1 88  ? -7.145  15.960  -15.681 1.00 59.40  ? 89  LEU D CB  1 
ATOM   9951  C  CG  . LEU D 1 88  ? -8.311  15.951  -14.693 1.00 60.25  ? 89  LEU D CG  1 
ATOM   9952  C  CD1 . LEU D 1 88  ? -8.792  17.356  -14.420 1.00 62.14  ? 89  LEU D CD1 1 
ATOM   9953  C  CD2 . LEU D 1 88  ? -9.448  15.089  -15.219 1.00 63.11  ? 89  LEU D CD2 1 
ATOM   9954  N  N   . ARG D 1 89  ? -4.529  15.602  -17.020 1.00 63.07  ? 90  ARG D N   1 
ATOM   9955  C  CA  . ARG D 1 89  ? -3.510  14.719  -17.570 1.00 66.58  ? 90  ARG D CA  1 
ATOM   9956  C  C   . ARG D 1 89  ? -2.099  15.212  -17.253 1.00 66.77  ? 90  ARG D C   1 
ATOM   9957  O  O   . ARG D 1 89  ? -1.178  14.408  -17.134 1.00 70.59  ? 90  ARG D O   1 
ATOM   9958  C  CB  . ARG D 1 89  ? -3.696  14.566  -19.083 1.00 73.59  ? 90  ARG D CB  1 
ATOM   9959  C  CG  . ARG D 1 89  ? -2.719  15.360  -19.928 1.00 81.34  ? 90  ARG D CG  1 
ATOM   9960  C  CD  . ARG D 1 89  ? -3.248  15.558  -21.335 1.00 89.44  ? 90  ARG D CD  1 
ATOM   9961  N  NE  . ARG D 1 89  ? -2.804  16.826  -21.903 1.00 93.83  ? 90  ARG D NE  1 
ATOM   9962  C  CZ  . ARG D 1 89  ? -3.170  17.277  -23.097 1.00 99.45  ? 90  ARG D CZ  1 
ATOM   9963  N  NH1 . ARG D 1 89  ? -3.993  16.565  -23.854 1.00 101.68 ? 90  ARG D NH1 1 
ATOM   9964  N  NH2 . ARG D 1 89  ? -2.716  18.444  -23.534 1.00 101.77 ? 90  ARG D NH2 1 
ATOM   9965  N  N   . ASP D 1 90  ? -1.925  16.523  -17.102 1.00 63.02  ? 91  ASP D N   1 
ATOM   9966  C  CA  . ASP D 1 90  ? -0.606  17.047  -16.754 1.00 62.97  ? 91  ASP D CA  1 
ATOM   9967  C  C   . ASP D 1 90  ? -0.227  16.678  -15.318 1.00 57.80  ? 91  ASP D C   1 
ATOM   9968  O  O   . ASP D 1 90  ? 0.892   16.199  -15.063 1.00 57.51  ? 91  ASP D O   1 
ATOM   9969  C  CB  . ASP D 1 90  ? -0.552  18.561  -16.959 1.00 66.44  ? 91  ASP D CB  1 
ATOM   9970  C  CG  . ASP D 1 90  ? -0.427  18.943  -18.425 1.00 74.18  ? 91  ASP D CG  1 
ATOM   9971  O  OD1 . ASP D 1 90  ? -0.497  18.038  -19.284 1.00 74.48  ? 91  ASP D OD1 1 
ATOM   9972  O  OD2 . ASP D 1 90  ? -0.249  20.144  -18.719 1.00 76.50  ? 91  ASP D OD2 1 
ATOM   9973  N  N   . SER D 1 91  ? -1.155  16.882  -14.384 1.00 55.75  ? 92  SER D N   1 
ATOM   9974  C  CA  . SER D 1 91  ? -0.920  16.448  -13.003 1.00 55.36  ? 92  SER D CA  1 
ATOM   9975  C  C   . SER D 1 91  ? -0.630  14.944  -12.950 1.00 53.28  ? 92  SER D C   1 
ATOM   9976  O  O   . SER D 1 91  ? 0.355   14.485  -12.333 1.00 53.89  ? 92  SER D O   1 
ATOM   9977  C  CB  . SER D 1 91  ? -2.123  16.785  -12.119 1.00 54.37  ? 92  SER D CB  1 
ATOM   9978  O  OG  . SER D 1 91  ? -2.358  18.182  -12.087 1.00 57.32  ? 92  SER D OG  1 
ATOM   9979  N  N   . SER D 1 92  ? -1.495  14.189  -13.624 1.00 53.27  ? 93  SER D N   1 
ATOM   9980  C  CA  . SER D 1 92  ? -1.371  12.739  -13.706 1.00 57.19  ? 93  SER D CA  1 
ATOM   9981  C  C   . SER D 1 92  ? -0.007  12.309  -14.238 1.00 57.54  ? 93  SER D C   1 
ATOM   9982  O  O   . SER D 1 92  ? 0.563   11.324  -13.770 1.00 61.86  ? 93  SER D O   1 
ATOM   9983  C  CB  . SER D 1 92  ? -2.477  12.163  -14.590 1.00 52.77  ? 93  SER D CB  1 
ATOM   9984  O  OG  . SER D 1 92  ? -2.340  10.759  -14.720 1.00 58.39  ? 93  SER D OG  1 
ATOM   9985  N  N   . ARG D 1 93  ? 0.515   13.049  -15.211 1.00 56.06  ? 94  ARG D N   1 
ATOM   9986  C  CA  . ARG D 1 93  ? 1.808   12.719  -15.799 1.00 57.02  ? 94  ARG D CA  1 
ATOM   9987  C  C   . ARG D 1 93  ? 2.965   13.112  -14.887 1.00 56.50  ? 94  ARG D C   1 
ATOM   9988  O  O   . ARG D 1 93  ? 4.012   12.461  -14.901 1.00 54.64  ? 94  ARG D O   1 
ATOM   9989  C  CB  . ARG D 1 93  ? 1.968   13.380  -17.170 1.00 65.36  ? 94  ARG D CB  1 
ATOM   9990  C  CG  . ARG D 1 93  ? 1.162   12.701  -18.270 1.00 70.68  ? 94  ARG D CG  1 
ATOM   9991  C  CD  . ARG D 1 93  ? 1.395   13.338  -19.633 1.00 76.72  ? 94  ARG D CD  1 
ATOM   9992  N  NE  . ARG D 1 93  ? 1.154   14.778  -19.626 1.00 78.31  ? 94  ARG D NE  1 
ATOM   9993  C  CZ  . ARG D 1 93  ? 2.115   15.695  -19.682 1.00 79.20  ? 94  ARG D CZ  1 
ATOM   9994  N  NH1 . ARG D 1 93  ? 1.806   16.984  -19.671 1.00 77.50  ? 94  ARG D NH1 1 
ATOM   9995  N  NH2 . ARG D 1 93  ? 3.385   15.322  -19.750 1.00 80.01  ? 94  ARG D NH2 1 
ATOM   9996  N  N   . VAL D 1 94  ? 2.789   14.170  -14.099 1.00 47.58  ? 95  VAL D N   1 
ATOM   9997  C  CA  . VAL D 1 94  ? 3.785   14.492  -13.078 1.00 46.68  ? 95  VAL D CA  1 
ATOM   9998  C  C   . VAL D 1 94  ? 3.900   13.336  -12.082 1.00 49.15  ? 95  VAL D C   1 
ATOM   9999  O  O   . VAL D 1 94  ? 4.998   12.790  -11.850 1.00 50.38  ? 95  VAL D O   1 
ATOM   10000 C  CB  . VAL D 1 94  ? 3.440   15.788  -12.322 1.00 42.68  ? 95  VAL D CB  1 
ATOM   10001 C  CG1 . VAL D 1 94  ? 4.345   15.956  -11.108 1.00 40.18  ? 95  VAL D CG1 1 
ATOM   10002 C  CG2 . VAL D 1 94  ? 3.555   16.988  -13.248 1.00 47.81  ? 95  VAL D CG2 1 
ATOM   10003 N  N   . LEU D 1 95  ? 2.756   12.958  -11.511 1.00 47.24  ? 96  LEU D N   1 
ATOM   10004 C  CA  . LEU D 1 95  ? 2.702   11.830  -10.578 1.00 44.01  ? 96  LEU D CA  1 
ATOM   10005 C  C   . LEU D 1 95  ? 3.323   10.566  -11.182 1.00 38.96  ? 96  LEU D C   1 
ATOM   10006 O  O   . LEU D 1 95  ? 4.174   9.902   -10.565 1.00 43.52  ? 96  LEU D O   1 
ATOM   10007 C  CB  . LEU D 1 95  ? 1.253   11.562  -10.166 1.00 44.55  ? 96  LEU D CB  1 
ATOM   10008 C  CG  . LEU D 1 95  ? 0.973   10.375  -9.246  1.00 41.27  ? 96  LEU D CG  1 
ATOM   10009 C  CD1 . LEU D 1 95  ? 1.836   10.443  -8.000  1.00 42.23  ? 96  LEU D CD1 1 
ATOM   10010 C  CD2 . LEU D 1 95  ? -0.495  10.347  -8.873  1.00 35.65  ? 96  LEU D CD2 1 
ATOM   10011 N  N   . GLN D 1 96  ? 2.889   10.260  -12.402 1.00 40.93  ? 97  GLN D N   1 
ATOM   10012 C  CA  . GLN D 1 96  ? 3.374   9.116   -13.166 1.00 46.54  ? 97  GLN D CA  1 
ATOM   10013 C  C   . GLN D 1 96  ? 4.896   9.117   -13.289 1.00 47.57  ? 97  GLN D C   1 
ATOM   10014 O  O   . GLN D 1 96  ? 5.551   8.096   -13.065 1.00 51.92  ? 97  GLN D O   1 
ATOM   10015 C  CB  . GLN D 1 96  ? 2.738   9.121   -14.557 1.00 53.28  ? 97  GLN D CB  1 
ATOM   10016 C  CG  . GLN D 1 96  ? 2.158   7.794   -15.002 1.00 59.52  ? 97  GLN D CG  1 
ATOM   10017 C  CD  . GLN D 1 96  ? 1.339   7.926   -16.272 1.00 67.99  ? 97  GLN D CD  1 
ATOM   10018 O  OE1 . GLN D 1 96  ? 0.489   8.811   -16.387 1.00 65.67  ? 97  GLN D OE1 1 
ATOM   10019 N  NE2 . GLN D 1 96  ? 1.595   7.050   -17.236 1.00 70.20  ? 97  GLN D NE2 1 
ATOM   10020 N  N   . ALA D 1 97  ? 5.448   10.273  -13.648 1.00 49.61  ? 98  ALA D N   1 
ATOM   10021 C  CA  . ALA D 1 97  ? 6.889   10.427  -13.792 1.00 44.76  ? 98  ALA D CA  1 
ATOM   10022 C  C   . ALA D 1 97  ? 7.596   10.167  -12.469 1.00 49.78  ? 98  ALA D C   1 
ATOM   10023 O  O   . ALA D 1 97  ? 8.625   9.485   -12.432 1.00 44.70  ? 98  ALA D O   1 
ATOM   10024 C  CB  . ALA D 1 97  ? 7.227   11.815  -14.309 1.00 43.38  ? 98  ALA D CB  1 
ATOM   10025 N  N   . MET D 1 98  ? 7.045   10.712  -11.386 1.00 47.87  ? 99  MET D N   1 
ATOM   10026 C  CA  . MET D 1 98  ? 7.608   10.462  -10.060 1.00 45.95  ? 99  MET D CA  1 
ATOM   10027 C  C   . MET D 1 98  ? 7.686   8.961   -9.763  1.00 45.39  ? 99  MET D C   1 
ATOM   10028 O  O   . MET D 1 98  ? 8.770   8.415   -9.472  1.00 45.50  ? 99  MET D O   1 
ATOM   10029 C  CB  . MET D 1 98  ? 6.780   11.174  -8.986  1.00 44.68  ? 99  MET D CB  1 
ATOM   10030 C  CG  . MET D 1 98  ? 7.370   11.102  -7.584  1.00 49.77  ? 99  MET D CG  1 
ATOM   10031 S  SD  . MET D 1 98  ? 6.872   9.636   -6.657  1.00 46.75  ? 99  MET D SD  1 
ATOM   10032 C  CE  . MET D 1 98  ? 5.134   9.979   -6.387  1.00 36.49  ? 99  MET D CE  1 
ATOM   10033 N  N   . LEU D 1 99  ? 6.534   8.298   -9.849  1.00 44.06  ? 100 LEU D N   1 
ATOM   10034 C  CA  . LEU D 1 99  ? 6.455   6.865   -9.565  1.00 37.50  ? 100 LEU D CA  1 
ATOM   10035 C  C   . LEU D 1 99  ? 7.406   6.045   -10.444 1.00 46.54  ? 100 LEU D C   1 
ATOM   10036 O  O   . LEU D 1 99  ? 8.029   5.080   -9.979  1.00 46.55  ? 100 LEU D O   1 
ATOM   10037 C  CB  . LEU D 1 99  ? 5.018   6.373   -9.739  1.00 37.12  ? 100 LEU D CB  1 
ATOM   10038 C  CG  . LEU D 1 99  ? 4.005   6.957   -8.753  1.00 36.53  ? 100 LEU D CG  1 
ATOM   10039 C  CD1 . LEU D 1 99  ? 2.589   6.598   -9.163  1.00 41.43  ? 100 LEU D CD1 1 
ATOM   10040 C  CD2 . LEU D 1 99  ? 4.297   6.467   -7.343  1.00 36.25  ? 100 LEU D CD2 1 
ATOM   10041 N  N   . ALA D 1 100 ? 7.523   6.446   -11.708 1.00 44.52  ? 101 ALA D N   1 
ATOM   10042 C  CA  . ALA D 1 100 ? 8.416   5.778   -12.650 1.00 44.98  ? 101 ALA D CA  1 
ATOM   10043 C  C   . ALA D 1 100 ? 9.876   5.913   -12.221 1.00 47.40  ? 101 ALA D C   1 
ATOM   10044 O  O   . ALA D 1 100 ? 10.617  4.921   -12.176 1.00 49.38  ? 101 ALA D O   1 
ATOM   10045 C  CB  . ALA D 1 100 ? 8.220   6.341   -14.050 1.00 40.25  ? 101 ALA D CB  1 
ATOM   10046 N  N   . THR D 1 101 ? 10.278  7.144   -11.910 1.00 47.71  ? 102 THR D N   1 
ATOM   10047 C  CA  . THR D 1 101 ? 11.624  7.424   -11.415 1.00 46.85  ? 102 THR D CA  1 
ATOM   10048 C  C   . THR D 1 101 ? 11.956  6.559   -10.197 1.00 48.52  ? 102 THR D C   1 
ATOM   10049 O  O   . THR D 1 101 ? 12.997  5.881   -10.168 1.00 40.53  ? 102 THR D O   1 
ATOM   10050 C  CB  . THR D 1 101 ? 11.795  8.910   -11.032 1.00 46.52  ? 102 THR D CB  1 
ATOM   10051 O  OG1 . THR D 1 101 ? 11.906  9.709   -12.216 1.00 52.94  ? 102 THR D OG1 1 
ATOM   10052 C  CG2 . THR D 1 101 ? 13.054  9.097   -10.204 1.00 47.53  ? 102 THR D CG2 1 
ATOM   10053 N  N   . GLN D 1 102 ? 11.066  6.576   -9.201  1.00 48.28  ? 103 GLN D N   1 
ATOM   10054 C  CA  . GLN D 1 102 ? 11.268  5.771   -7.988  1.00 51.05  ? 103 GLN D CA  1 
ATOM   10055 C  C   . GLN D 1 102 ? 11.424  4.286   -8.326  1.00 50.55  ? 103 GLN D C   1 
ATOM   10056 O  O   . GLN D 1 102 ? 12.323  3.601   -7.807  1.00 49.63  ? 103 GLN D O   1 
ATOM   10057 C  CB  . GLN D 1 102 ? 10.106  5.969   -7.002  1.00 54.30  ? 103 GLN D CB  1 
ATOM   10058 C  CG  . GLN D 1 102 ? 10.549  6.461   -5.628  1.00 61.56  ? 103 GLN D CG  1 
ATOM   10059 C  CD  . GLN D 1 102 ? 11.093  7.870   -5.696  1.00 64.16  ? 103 GLN D CD  1 
ATOM   10060 O  OE1 . GLN D 1 102 ? 10.908  8.560   -6.696  1.00 73.74  ? 103 GLN D OE1 1 
ATOM   10061 N  NE2 . GLN D 1 102 ? 11.760  8.310   -4.633  1.00 67.06  ? 103 GLN D NE2 1 
ATOM   10062 N  N   . LEU D 1 103 ? 10.551  3.805   -9.210  1.00 44.04  ? 104 LEU D N   1 
ATOM   10063 C  CA  . LEU D 1 103 ? 10.569  2.410   -9.654  1.00 44.30  ? 104 LEU D CA  1 
ATOM   10064 C  C   . LEU D 1 103 ? 11.915  2.003   -10.250 1.00 42.32  ? 104 LEU D C   1 
ATOM   10065 O  O   . LEU D 1 103 ? 12.542  1.030   -9.799  1.00 42.71  ? 104 LEU D O   1 
ATOM   10066 C  CB  . LEU D 1 103 ? 9.456   2.170   -10.682 1.00 46.25  ? 104 LEU D CB  1 
ATOM   10067 C  CG  . LEU D 1 103 ? 9.183   0.720   -11.108 1.00 44.62  ? 104 LEU D CG  1 
ATOM   10068 C  CD1 . LEU D 1 103 ? 9.111   -0.185  -9.903  1.00 46.64  ? 104 LEU D CD1 1 
ATOM   10069 C  CD2 . LEU D 1 103 ? 7.906   0.592   -11.940 1.00 41.83  ? 104 LEU D CD2 1 
ATOM   10070 N  N   . ARG D 1 104 ? 12.344  2.746   -11.270 1.00 42.81  ? 105 ARG D N   1 
ATOM   10071 C  CA  . ARG D 1 104 ? 13.638  2.508   -11.903 1.00 44.81  ? 105 ARG D CA  1 
ATOM   10072 C  C   . ARG D 1 104 ? 14.753  2.509   -10.868 1.00 41.58  ? 105 ARG D C   1 
ATOM   10073 O  O   . ARG D 1 104 ? 15.593  1.599   -10.842 1.00 51.25  ? 105 ARG D O   1 
ATOM   10074 C  CB  . ARG D 1 104 ? 13.929  3.563   -12.975 1.00 50.31  ? 105 ARG D CB  1 
ATOM   10075 C  CG  . ARG D 1 104 ? 13.062  3.471   -14.221 1.00 60.41  ? 105 ARG D CG  1 
ATOM   10076 C  CD  . ARG D 1 104 ? 13.624  4.343   -15.341 1.00 66.93  ? 105 ARG D CD  1 
ATOM   10077 N  NE  . ARG D 1 104 ? 13.630  5.761   -14.987 1.00 71.21  ? 105 ARG D NE  1 
ATOM   10078 C  CZ  . ARG D 1 104 ? 12.598  6.579   -15.165 1.00 76.08  ? 105 ARG D CZ  1 
ATOM   10079 N  NH1 . ARG D 1 104 ? 12.690  7.854   -14.814 1.00 78.18  ? 105 ARG D NH1 1 
ATOM   10080 N  NH2 . ARG D 1 104 ? 11.472  6.122   -15.695 1.00 77.28  ? 105 ARG D NH2 1 
ATOM   10081 N  N   . SER D 1 105 ? 14.742  3.529   -10.013 1.00 49.40  ? 106 SER D N   1 
ATOM   10082 C  CA  . SER D 1 105 ? 15.751  3.669   -8.966  1.00 48.28  ? 106 SER D CA  1 
ATOM   10083 C  C   . SER D 1 105 ? 15.877  2.410   -8.110  1.00 45.08  ? 106 SER D C   1 
ATOM   10084 O  O   . SER D 1 105 ? 16.960  1.810   -8.026  1.00 41.52  ? 106 SER D O   1 
ATOM   10085 C  CB  . SER D 1 105 ? 15.431  4.874   -8.077  1.00 40.96  ? 106 SER D CB  1 
ATOM   10086 O  OG  . SER D 1 105 ? 15.217  6.039   -8.856  1.00 49.56  ? 106 SER D OG  1 
ATOM   10087 N  N   . PHE D 1 106 ? 14.775  1.996   -7.489  1.00 42.10  ? 107 PHE D N   1 
ATOM   10088 C  CA  . PHE D 1 106 ? 14.841  0.849   -6.583  1.00 39.86  ? 107 PHE D CA  1 
ATOM   10089 C  C   . PHE D 1 106 ? 15.148  -0.464  -7.304  1.00 40.27  ? 107 PHE D C   1 
ATOM   10090 O  O   . PHE D 1 106 ? 15.946  -1.276  -6.813  1.00 40.52  ? 107 PHE D O   1 
ATOM   10091 C  CB  . PHE D 1 106 ? 13.544  0.727   -5.788  1.00 39.05  ? 107 PHE D CB  1 
ATOM   10092 C  CG  . PHE D 1 106 ? 13.463  1.681   -4.635  1.00 38.76  ? 107 PHE D CG  1 
ATOM   10093 C  CD1 . PHE D 1 106 ? 12.943  2.953   -4.805  1.00 38.60  ? 107 PHE D CD1 1 
ATOM   10094 C  CD2 . PHE D 1 106 ? 13.923  1.312   -3.382  1.00 38.74  ? 107 PHE D CD2 1 
ATOM   10095 C  CE1 . PHE D 1 106 ? 12.875  3.837   -3.745  1.00 38.46  ? 107 PHE D CE1 1 
ATOM   10096 C  CE2 . PHE D 1 106 ? 13.857  2.190   -2.318  1.00 38.64  ? 107 PHE D CE2 1 
ATOM   10097 C  CZ  . PHE D 1 106 ? 13.332  3.455   -2.499  1.00 38.51  ? 107 PHE D CZ  1 
ATOM   10098 N  N   . ASP D 1 107 ? 14.529  -0.667  -8.465  1.00 40.44  ? 108 ASP D N   1 
ATOM   10099 C  CA  . ASP D 1 107 ? 14.782  -1.870  -9.256  1.00 43.93  ? 108 ASP D CA  1 
ATOM   10100 C  C   . ASP D 1 107 ? 16.277  -2.016  -9.556  1.00 44.09  ? 108 ASP D C   1 
ATOM   10101 O  O   . ASP D 1 107 ? 16.914  -3.044  -9.234  1.00 42.13  ? 108 ASP D O   1 
ATOM   10102 C  CB  . ASP D 1 107 ? 13.980  -1.826  -10.559 1.00 47.26  ? 108 ASP D CB  1 
ATOM   10103 C  CG  . ASP D 1 107 ? 13.872  -3.182  -11.226 1.00 50.47  ? 108 ASP D CG  1 
ATOM   10104 O  OD1 . ASP D 1 107 ? 13.820  -4.201  -10.504 1.00 51.12  ? 108 ASP D OD1 1 
ATOM   10105 O  OD2 . ASP D 1 107 ? 13.838  -3.229  -12.474 1.00 52.06  ? 108 ASP D OD2 1 
ATOM   10106 N  N   . ASP D 1 108 ? 16.829  -0.963  -10.154 1.00 48.35  ? 109 ASP D N   1 
ATOM   10107 C  CA  . ASP D 1 108 ? 18.244  -0.925  -10.496 1.00 51.89  ? 109 ASP D CA  1 
ATOM   10108 C  C   . ASP D 1 108 ? 19.126  -1.107  -9.265  1.00 43.26  ? 109 ASP D C   1 
ATOM   10109 O  O   . ASP D 1 108 ? 20.157  -1.775  -9.335  1.00 43.93  ? 109 ASP D O   1 
ATOM   10110 C  CB  . ASP D 1 108 ? 18.590  0.388   -11.199 1.00 53.51  ? 109 ASP D CB  1 
ATOM   10111 C  CG  . ASP D 1 108 ? 18.087  0.433   -12.629 1.00 59.35  ? 109 ASP D CG  1 
ATOM   10112 O  OD1 . ASP D 1 108 ? 17.350  -0.491  -13.034 1.00 60.85  ? 109 ASP D OD1 1 
ATOM   10113 O  OD2 . ASP D 1 108 ? 18.427  1.395   -13.350 1.00 62.19  ? 109 ASP D OD2 1 
ATOM   10114 N  N   . HIS D 1 109 ? 18.722  -0.522  -8.139  1.00 42.51  ? 110 HIS D N   1 
ATOM   10115 C  CA  . HIS D 1 109 ? 19.512  -0.663  -6.918  1.00 42.51  ? 110 HIS D CA  1 
ATOM   10116 C  C   . HIS D 1 109 ? 19.568  -2.109  -6.427  1.00 50.25  ? 110 HIS D C   1 
ATOM   10117 O  O   . HIS D 1 109 ? 20.637  -2.605  -6.076  1.00 52.28  ? 110 HIS D O   1 
ATOM   10118 C  CB  . HIS D 1 109 ? 18.971  0.226   -5.800  1.00 41.85  ? 110 HIS D CB  1 
ATOM   10119 C  CG  . HIS D 1 109 ? 19.720  0.082   -4.511  1.00 50.43  ? 110 HIS D CG  1 
ATOM   10120 N  ND1 . HIS D 1 109 ? 21.057  0.397   -4.390  1.00 42.82  ? 110 HIS D ND1 1 
ATOM   10121 C  CD2 . HIS D 1 109 ? 19.327  -0.361  -3.294  1.00 50.80  ? 110 HIS D CD2 1 
ATOM   10122 C  CE1 . HIS D 1 109 ? 21.452  0.164   -3.151  1.00 51.87  ? 110 HIS D CE1 1 
ATOM   10123 N  NE2 . HIS D 1 109 ? 20.421  -0.297  -2.465  1.00 52.27  ? 110 HIS D NE2 1 
ATOM   10124 N  N   . PHE D 1 110 ? 18.420  -2.781  -6.393  1.00 41.70  ? 111 PHE D N   1 
ATOM   10125 C  CA  . PHE D 1 110 ? 18.379  -4.168  -5.926  1.00 41.63  ? 111 PHE D CA  1 
ATOM   10126 C  C   . PHE D 1 110 ? 19.175  -5.090  -6.858  1.00 42.47  ? 111 PHE D C   1 
ATOM   10127 O  O   . PHE D 1 110 ? 20.000  -5.922  -6.399  1.00 54.09  ? 111 PHE D O   1 
ATOM   10128 C  CB  . PHE D 1 110 ? 16.929  -4.636  -5.800  1.00 40.96  ? 111 PHE D CB  1 
ATOM   10129 C  CG  . PHE D 1 110 ? 16.146  -3.892  -4.753  1.00 40.22  ? 111 PHE D CG  1 
ATOM   10130 C  CD1 . PHE D 1 110 ? 16.757  -3.481  -3.578  1.00 44.32  ? 111 PHE D CD1 1 
ATOM   10131 C  CD2 . PHE D 1 110 ? 14.809  -3.588  -4.947  1.00 44.23  ? 111 PHE D CD2 1 
ATOM   10132 C  CE1 . PHE D 1 110 ? 16.046  -2.792  -2.612  1.00 39.65  ? 111 PHE D CE1 1 
ATOM   10133 C  CE2 . PHE D 1 110 ? 14.092  -2.895  -3.985  1.00 44.17  ? 111 PHE D CE2 1 
ATOM   10134 C  CZ  . PHE D 1 110 ? 14.713  -2.499  -2.816  1.00 45.38  ? 111 PHE D CZ  1 
ATOM   10135 N  N   . GLN D 1 111 ? 18.942  -4.928  -8.162  1.00 42.88  ? 112 GLN D N   1 
ATOM   10136 C  CA  . GLN D 1 111 ? 19.730  -5.663  -9.151  1.00 47.49  ? 112 GLN D CA  1 
ATOM   10137 C  C   . GLN D 1 111 ? 21.226  -5.449  -8.919  1.00 47.95  ? 112 GLN D C   1 
ATOM   10138 O  O   . GLN D 1 111 ? 22.022  -6.393  -8.973  1.00 52.97  ? 112 GLN D O   1 
ATOM   10139 C  CB  . GLN D 1 111 ? 19.359  -5.241  -10.573 1.00 47.72  ? 112 GLN D CB  1 
ATOM   10140 C  CG  . GLN D 1 111 ? 18.001  -5.729  -11.045 1.00 50.41  ? 112 GLN D CG  1 
ATOM   10141 C  CD  . GLN D 1 111 ? 17.668  -5.241  -12.441 1.00 55.52  ? 112 GLN D CD  1 
ATOM   10142 O  OE1 . GLN D 1 111 ? 18.453  -5.412  -13.374 1.00 55.77  ? 112 GLN D OE1 1 
ATOM   10143 N  NE2 . GLN D 1 111 ? 16.498  -4.631  -12.593 1.00 55.72  ? 112 GLN D NE2 1 
ATOM   10144 N  N   . HIS D 1 112 ? 21.595  -4.202  -8.641  1.00 45.83  ? 113 HIS D N   1 
ATOM   10145 C  CA  . HIS D 1 112 ? 22.987  -3.844  -8.400  1.00 46.39  ? 113 HIS D CA  1 
ATOM   10146 C  C   . HIS D 1 112 ? 23.530  -4.477  -7.125  1.00 47.01  ? 113 HIS D C   1 
ATOM   10147 O  O   . HIS D 1 112 ? 24.716  -4.774  -7.039  1.00 47.64  ? 113 HIS D O   1 
ATOM   10148 C  CB  . HIS D 1 112 ? 23.146  -2.325  -8.334  1.00 48.37  ? 113 HIS D CB  1 
ATOM   10149 C  CG  . HIS D 1 112 ? 23.214  -1.670  -9.677  1.00 54.96  ? 113 HIS D CG  1 
ATOM   10150 N  ND1 . HIS D 1 112 ? 23.341  -0.307  -9.836  1.00 60.86  ? 113 HIS D ND1 1 
ATOM   10151 C  CD2 . HIS D 1 112 ? 23.175  -2.192  -10.926 1.00 61.09  ? 113 HIS D CD2 1 
ATOM   10152 C  CE1 . HIS D 1 112 ? 23.376  -0.018  -11.125 1.00 61.73  ? 113 HIS D CE1 1 
ATOM   10153 N  NE2 . HIS D 1 112 ? 23.277  -1.144  -11.808 1.00 61.70  ? 113 HIS D NE2 1 
ATOM   10154 N  N   . LEU D 1 113 ? 22.667  -4.670  -6.133  1.00 44.17  ? 114 LEU D N   1 
ATOM   10155 C  CA  . LEU D 1 113 ? 23.069  -5.363  -4.915  1.00 50.62  ? 114 LEU D CA  1 
ATOM   10156 C  C   . LEU D 1 113 ? 23.421  -6.806  -5.232  1.00 50.42  ? 114 LEU D C   1 
ATOM   10157 O  O   . LEU D 1 113 ? 24.519  -7.287  -4.894  1.00 51.82  ? 114 LEU D O   1 
ATOM   10158 C  CB  . LEU D 1 113 ? 21.962  -5.314  -3.865  1.00 48.49  ? 114 LEU D CB  1 
ATOM   10159 C  CG  . LEU D 1 113 ? 21.796  -4.012  -3.087  1.00 50.29  ? 114 LEU D CG  1 
ATOM   10160 C  CD1 . LEU D 1 113 ? 20.620  -4.132  -2.140  1.00 52.66  ? 114 LEU D CD1 1 
ATOM   10161 C  CD2 . LEU D 1 113 ? 23.070  -3.687  -2.326  1.00 50.89  ? 114 LEU D CD2 1 
ATOM   10162 N  N   . LEU D 1 114 ? 22.489  -7.494  -5.890  1.00 48.40  ? 115 LEU D N   1 
ATOM   10163 C  CA  . LEU D 1 114 ? 22.733  -8.892  -6.245  1.00 49.13  ? 115 LEU D CA  1 
ATOM   10164 C  C   . LEU D 1 114 ? 24.015  -9.025  -7.073  1.00 46.82  ? 115 LEU D C   1 
ATOM   10165 O  O   . LEU D 1 114 ? 24.843  -9.925  -6.850  1.00 49.02  ? 115 LEU D O   1 
ATOM   10166 C  CB  . LEU D 1 114 ? 21.543  -9.469  -7.011  1.00 44.50  ? 115 LEU D CB  1 
ATOM   10167 C  CG  . LEU D 1 114 ? 21.574  -10.981 -7.231  1.00 45.00  ? 115 LEU D CG  1 
ATOM   10168 C  CD1 . LEU D 1 114 ? 21.821  -11.694 -5.913  1.00 44.74  ? 115 LEU D CD1 1 
ATOM   10169 C  CD2 . LEU D 1 114 ? 20.273  -11.451 -7.851  1.00 50.66  ? 115 LEU D CD2 1 
ATOM   10170 N  N   . ASN D 1 115 ? 24.182  -8.099  -8.011  1.00 50.90  ? 116 ASN D N   1 
ATOM   10171 C  CA  . ASN D 1 115 ? 25.342  -8.085  -8.892  1.00 53.27  ? 116 ASN D CA  1 
ATOM   10172 C  C   . ASN D 1 115 ? 26.662  -7.796  -8.178  1.00 51.75  ? 116 ASN D C   1 
ATOM   10173 O  O   . ASN D 1 115 ? 27.706  -8.336  -8.548  1.00 55.77  ? 116 ASN D O   1 
ATOM   10174 C  CB  . ASN D 1 115 ? 25.114  -7.072  -10.011 1.00 61.39  ? 116 ASN D CB  1 
ATOM   10175 C  CG  . ASN D 1 115 ? 24.244  -7.629  -11.110 1.00 66.31  ? 116 ASN D CG  1 
ATOM   10176 O  OD1 . ASN D 1 115 ? 23.747  -8.751  -11.006 1.00 65.18  ? 116 ASN D OD1 1 
ATOM   10177 N  ND2 . ASN D 1 115 ? 24.047  -6.859  -12.169 1.00 75.01  ? 116 ASN D ND2 1 
ATOM   10178 N  N   . ASP D 1 116 ? 26.612  -6.947  -7.156  1.00 50.51  ? 117 ASP D N   1 
ATOM   10179 C  CA  . ASP D 1 116 ? 27.788  -6.673  -6.340  1.00 50.34  ? 117 ASP D CA  1 
ATOM   10180 C  C   . ASP D 1 116 ? 28.159  -7.914  -5.544  1.00 51.17  ? 117 ASP D C   1 
ATOM   10181 O  O   . ASP D 1 116 ? 29.343  -8.231  -5.385  1.00 53.57  ? 117 ASP D O   1 
ATOM   10182 C  CB  . ASP D 1 116 ? 27.543  -5.491  -5.399  1.00 56.55  ? 117 ASP D CB  1 
ATOM   10183 C  CG  . ASP D 1 116 ? 27.485  -4.164  -6.131  1.00 58.97  ? 117 ASP D CG  1 
ATOM   10184 O  OD1 . ASP D 1 116 ? 28.103  -4.051  -7.211  1.00 62.80  ? 117 ASP D OD1 1 
ATOM   10185 O  OD2 . ASP D 1 116 ? 26.820  -3.235  -5.626  1.00 58.16  ? 117 ASP D OD2 1 
ATOM   10186 N  N   . SER D 1 117 ? 27.142  -8.615  -5.046  1.00 51.24  ? 118 SER D N   1 
ATOM   10187 C  CA  . SER D 1 117 ? 27.377  -9.880  -4.354  1.00 46.98  ? 118 SER D CA  1 
ATOM   10188 C  C   . SER D 1 117 ? 28.079  -10.879 -5.274  1.00 50.75  ? 118 SER D C   1 
ATOM   10189 O  O   . SER D 1 117 ? 29.117  -11.451 -4.913  1.00 48.61  ? 118 SER D O   1 
ATOM   10190 C  CB  . SER D 1 117 ? 26.063  -10.471 -3.840  1.00 48.10  ? 118 SER D CB  1 
ATOM   10191 O  OG  . SER D 1 117 ? 26.303  -11.610 -3.033  1.00 48.23  ? 118 SER D OG  1 
ATOM   10192 N  N   . GLU D 1 118 ? 27.519  -11.074 -6.466  1.00 52.39  ? 119 GLU D N   1 
ATOM   10193 C  CA  . GLU D 1 118 ? 28.108  -12.006 -7.427  1.00 53.02  ? 119 GLU D CA  1 
ATOM   10194 C  C   . GLU D 1 118 ? 29.536  -11.614 -7.813  1.00 59.27  ? 119 GLU D C   1 
ATOM   10195 O  O   . GLU D 1 118 ? 30.416  -12.473 -7.923  1.00 60.30  ? 119 GLU D O   1 
ATOM   10196 C  CB  . GLU D 1 118 ? 27.242  -12.102 -8.683  1.00 49.32  ? 119 GLU D CB  1 
ATOM   10197 C  CG  . GLU D 1 118 ? 27.662  -13.213 -9.633  1.00 50.45  ? 119 GLU D CG  1 
ATOM   10198 C  CD  . GLU D 1 118 ? 26.788  -13.286 -10.869 1.00 57.40  ? 119 GLU D CD  1 
ATOM   10199 O  OE1 . GLU D 1 118 ? 26.017  -12.334 -11.107 1.00 62.64  ? 119 GLU D OE1 1 
ATOM   10200 O  OE2 . GLU D 1 118 ? 26.872  -14.293 -11.603 1.00 57.36  ? 119 GLU D OE2 1 
ATOM   10201 N  N   . ARG D 1 119 ? 29.762  -10.319 -8.014  1.00 59.93  ? 120 ARG D N   1 
ATOM   10202 C  CA  . ARG D 1 119 ? 31.088  -9.819  -8.373  1.00 57.71  ? 120 ARG D CA  1 
ATOM   10203 C  C   . ARG D 1 119 ? 32.107  -10.082 -7.267  1.00 51.99  ? 120 ARG D C   1 
ATOM   10204 O  O   . ARG D 1 119 ? 33.217  -10.552 -7.534  1.00 53.13  ? 120 ARG D O   1 
ATOM   10205 C  CB  . ARG D 1 119 ? 31.031  -8.322  -8.686  1.00 58.57  ? 120 ARG D CB  1 
ATOM   10206 C  CG  . ARG D 1 119 ? 31.261  -7.985  -10.151 1.00 60.34  ? 120 ARG D CG  1 
ATOM   10207 C  CD  . ARG D 1 119 ? 30.171  -8.571  -11.034 1.00 59.55  ? 120 ARG D CD  1 
ATOM   10208 N  N   . THR D 1 120 ? 31.727  -9.779  -6.029  1.00 53.21  ? 121 THR D N   1 
ATOM   10209 C  CA  . THR D 1 120 ? 32.593  -10.038 -4.883  1.00 51.25  ? 121 THR D CA  1 
ATOM   10210 C  C   . THR D 1 120 ? 32.907  -11.529 -4.778  1.00 56.86  ? 121 THR D C   1 
ATOM   10211 O  O   . THR D 1 120 ? 34.044  -11.914 -4.485  1.00 60.15  ? 121 THR D O   1 
ATOM   10212 C  CB  . THR D 1 120 ? 31.958  -9.551  -3.568  1.00 55.74  ? 121 THR D CB  1 
ATOM   10213 O  OG1 . THR D 1 120 ? 31.691  -8.146  -3.657  1.00 56.12  ? 121 THR D OG1 1 
ATOM   10214 C  CG2 . THR D 1 120 ? 32.893  -9.808  -2.394  1.00 55.79  ? 121 THR D CG2 1 
ATOM   10215 N  N   . LEU D 1 121 ? 31.897  -12.361 -5.028  1.00 53.24  ? 122 LEU D N   1 
ATOM   10216 C  CA  . LEU D 1 121 ? 32.097  -13.808 -5.072  1.00 55.14  ? 122 LEU D CA  1 
ATOM   10217 C  C   . LEU D 1 121 ? 33.179  -14.166 -6.087  1.00 55.65  ? 122 LEU D C   1 
ATOM   10218 O  O   . LEU D 1 121 ? 34.163  -14.833 -5.756  1.00 53.38  ? 122 LEU D O   1 
ATOM   10219 C  CB  . LEU D 1 121 ? 30.787  -14.527 -5.414  1.00 53.58  ? 122 LEU D CB  1 
ATOM   10220 C  CG  . LEU D 1 121 ? 30.798  -16.058 -5.487  1.00 53.99  ? 122 LEU D CG  1 
ATOM   10221 C  CD1 . LEU D 1 121 ? 29.487  -16.617 -4.968  1.00 54.36  ? 122 LEU D CD1 1 
ATOM   10222 C  CD2 . LEU D 1 121 ? 31.042  -16.546 -6.909  1.00 53.01  ? 122 LEU D CD2 1 
ATOM   10223 N  N   . GLN D 1 122 ? 32.981  -13.710 -7.321  1.00 56.49  ? 123 GLN D N   1 
ATOM   10224 C  CA  . GLN D 1 122 ? 33.929  -13.935 -8.409  1.00 58.84  ? 123 GLN D CA  1 
ATOM   10225 C  C   . GLN D 1 122 ? 35.342  -13.489 -8.050  1.00 61.39  ? 123 GLN D C   1 
ATOM   10226 O  O   . GLN D 1 122 ? 36.323  -14.103 -8.469  1.00 56.81  ? 123 GLN D O   1 
ATOM   10227 C  CB  . GLN D 1 122 ? 33.471  -13.197 -9.668  1.00 62.80  ? 123 GLN D CB  1 
ATOM   10228 C  CG  . GLN D 1 122 ? 32.652  -14.029 -10.636 1.00 63.75  ? 123 GLN D CG  1 
ATOM   10229 C  CD  . GLN D 1 122 ? 32.092  -13.195 -11.772 1.00 67.30  ? 123 GLN D CD  1 
ATOM   10230 O  OE1 . GLN D 1 122 ? 31.859  -11.996 -11.619 1.00 70.34  ? 123 GLN D OE1 1 
ATOM   10231 N  NE2 . GLN D 1 122 ? 31.887  -13.823 -12.924 1.00 69.10  ? 123 GLN D NE2 1 
ATOM   10232 N  N   . ALA D 1 123 ? 35.437  -12.417 -7.271  1.00 69.11  ? 124 ALA D N   1 
ATOM   10233 C  CA  . ALA D 1 123 ? 36.728  -11.821 -6.949  1.00 70.85  ? 124 ALA D CA  1 
ATOM   10234 C  C   . ALA D 1 123 ? 37.458  -12.540 -5.816  1.00 69.07  ? 124 ALA D C   1 
ATOM   10235 O  O   . ALA D 1 123 ? 38.685  -12.650 -5.840  1.00 67.11  ? 124 ALA D O   1 
ATOM   10236 C  CB  . ALA D 1 123 ? 36.547  -10.350 -6.600  1.00 70.05  ? 124 ALA D CB  1 
ATOM   10237 N  N   . THR D 1 124 ? 36.714  -13.028 -4.827  1.00 66.78  ? 125 THR D N   1 
ATOM   10238 C  CA  . THR D 1 124 ? 37.343  -13.571 -3.624  1.00 69.91  ? 125 THR D CA  1 
ATOM   10239 C  C   . THR D 1 124 ? 37.396  -15.099 -3.563  1.00 70.73  ? 125 THR D C   1 
ATOM   10240 O  O   . THR D 1 124 ? 38.281  -15.663 -2.918  1.00 73.02  ? 125 THR D O   1 
ATOM   10241 C  CB  . THR D 1 124 ? 36.627  -13.070 -2.354  1.00 65.08  ? 125 THR D CB  1 
ATOM   10242 O  OG1 . THR D 1 124 ? 35.226  -13.350 -2.450  1.00 64.89  ? 125 THR D OG1 1 
ATOM   10243 C  CG2 . THR D 1 124 ? 36.830  -11.573 -2.185  1.00 66.13  ? 125 THR D CG2 1 
ATOM   10244 N  N   . PHE D 1 125 ? 36.459  -15.770 -4.226  1.00 72.68  ? 126 PHE D N   1 
ATOM   10245 C  CA  . PHE D 1 125 ? 36.364  -17.228 -4.116  1.00 72.79  ? 126 PHE D CA  1 
ATOM   10246 C  C   . PHE D 1 125 ? 37.536  -18.029 -4.715  1.00 73.41  ? 126 PHE D C   1 
ATOM   10247 O  O   . PHE D 1 125 ? 37.937  -19.037 -4.131  1.00 74.23  ? 126 PHE D O   1 
ATOM   10248 C  CB  . PHE D 1 125 ? 35.049  -17.717 -4.733  1.00 74.28  ? 126 PHE D CB  1 
ATOM   10249 C  CG  . PHE D 1 125 ? 33.884  -17.677 -3.784  1.00 76.24  ? 126 PHE D CG  1 
ATOM   10250 C  CD1 . PHE D 1 125 ? 33.836  -16.740 -2.764  1.00 76.83  ? 126 PHE D CD1 1 
ATOM   10251 C  CD2 . PHE D 1 125 ? 32.847  -18.588 -3.899  1.00 77.81  ? 126 PHE D CD2 1 
ATOM   10252 C  CE1 . PHE D 1 125 ? 32.768  -16.702 -1.886  1.00 77.46  ? 126 PHE D CE1 1 
ATOM   10253 C  CE2 . PHE D 1 125 ? 31.778  -18.557 -3.022  1.00 77.93  ? 126 PHE D CE2 1 
ATOM   10254 C  CZ  . PHE D 1 125 ? 31.739  -17.612 -2.016  1.00 78.35  ? 126 PHE D CZ  1 
ATOM   10255 N  N   . PRO D 1 126 ? 38.082  -17.609 -5.877  1.00 69.21  ? 127 PRO D N   1 
ATOM   10256 C  CA  . PRO D 1 126 ? 39.231  -18.373 -6.386  1.00 74.56  ? 127 PRO D CA  1 
ATOM   10257 C  C   . PRO D 1 126 ? 40.439  -18.360 -5.451  1.00 70.05  ? 127 PRO D C   1 
ATOM   10258 O  O   . PRO D 1 126 ? 41.240  -19.291 -5.473  1.00 72.22  ? 127 PRO D O   1 
ATOM   10259 C  CB  . PRO D 1 126 ? 39.570  -17.663 -7.699  1.00 72.46  ? 127 PRO D CB  1 
ATOM   10260 C  CG  . PRO D 1 126 ? 38.295  -17.059 -8.134  1.00 58.84  ? 127 PRO D CG  1 
ATOM   10261 C  CD  . PRO D 1 126 ? 37.609  -16.627 -6.871  1.00 66.57  ? 127 PRO D CD  1 
ATOM   10262 N  N   . GLY D 1 127 ? 40.570  -17.313 -4.646  1.00 71.78  ? 128 GLY D N   1 
ATOM   10263 C  CA  . GLY D 1 127 ? 41.676  -17.223 -3.712  1.00 73.84  ? 128 GLY D CA  1 
ATOM   10264 C  C   . GLY D 1 127 ? 41.411  -18.000 -2.439  1.00 73.06  ? 128 GLY D C   1 
ATOM   10265 O  O   . GLY D 1 127 ? 42.312  -18.625 -1.880  1.00 77.57  ? 128 GLY D O   1 
ATOM   10266 N  N   . ALA D 1 128 ? 40.162  -17.970 -1.987  1.00 74.08  ? 129 ALA D N   1 
ATOM   10267 C  CA  . ALA D 1 128 ? 39.797  -18.554 -0.702  1.00 71.73  ? 129 ALA D CA  1 
ATOM   10268 C  C   . ALA D 1 128 ? 39.564  -20.057 -0.777  1.00 69.60  ? 129 ALA D C   1 
ATOM   10269 O  O   . ALA D 1 128 ? 39.992  -20.804 0.103   1.00 69.05  ? 129 ALA D O   1 
ATOM   10270 C  CB  . ALA D 1 128 ? 38.563  -17.865 -0.155  1.00 70.09  ? 129 ALA D CB  1 
ATOM   10271 N  N   . PHE D 1 129 ? 38.878  -20.498 -1.824  1.00 68.71  ? 130 PHE D N   1 
ATOM   10272 C  CA  . PHE D 1 129 ? 38.502  -21.899 -1.938  1.00 72.98  ? 130 PHE D CA  1 
ATOM   10273 C  C   . PHE D 1 129 ? 39.230  -22.576 -3.086  1.00 76.76  ? 130 PHE D C   1 
ATOM   10274 O  O   . PHE D 1 129 ? 39.181  -23.795 -3.230  1.00 73.11  ? 130 PHE D O   1 
ATOM   10275 C  CB  . PHE D 1 129 ? 36.990  -22.020 -2.109  1.00 66.61  ? 130 PHE D CB  1 
ATOM   10276 C  CG  . PHE D 1 129 ? 36.216  -21.351 -1.017  1.00 61.76  ? 130 PHE D CG  1 
ATOM   10277 C  CD1 . PHE D 1 129 ? 36.146  -21.921 0.242   1.00 61.43  ? 130 PHE D CD1 1 
ATOM   10278 C  CD2 . PHE D 1 129 ? 35.581  -20.141 -1.238  1.00 62.17  ? 130 PHE D CD2 1 
ATOM   10279 C  CE1 . PHE D 1 129 ? 35.446  -21.307 1.258   1.00 60.81  ? 130 PHE D CE1 1 
ATOM   10280 C  CE2 . PHE D 1 129 ? 34.878  -19.521 -0.225  1.00 59.25  ? 130 PHE D CE2 1 
ATOM   10281 C  CZ  . PHE D 1 129 ? 34.812  -20.106 1.025   1.00 58.75  ? 130 PHE D CZ  1 
ATOM   10282 N  N   . GLY D 1 130 ? 39.917  -21.777 -3.894  1.00 84.51  ? 131 GLY D N   1 
ATOM   10283 C  CA  . GLY D 1 130 ? 40.699  -22.305 -4.992  1.00 90.76  ? 131 GLY D CA  1 
ATOM   10284 C  C   . GLY D 1 130 ? 39.857  -23.051 -6.005  1.00 93.05  ? 131 GLY D C   1 
ATOM   10285 O  O   . GLY D 1 130 ? 38.762  -22.611 -6.367  1.00 91.67  ? 131 GLY D O   1 
ATOM   10286 N  N   . GLU D 1 131 ? 40.364  -24.200 -6.440  1.00 96.45  ? 132 GLU D N   1 
ATOM   10287 C  CA  . GLU D 1 131 ? 39.739  -24.957 -7.514  1.00 97.48  ? 132 GLU D CA  1 
ATOM   10288 C  C   . GLU D 1 131 ? 38.372  -25.475 -7.072  1.00 90.71  ? 132 GLU D C   1 
ATOM   10289 O  O   . GLU D 1 131 ? 37.470  -25.644 -7.897  1.00 92.35  ? 132 GLU D O   1 
ATOM   10290 C  CB  . GLU D 1 131 ? 40.653  -26.104 -7.961  1.00 103.80 ? 132 GLU D CB  1 
ATOM   10291 C  CG  . GLU D 1 131 ? 40.014  -27.128 -8.889  1.00 108.58 ? 132 GLU D CG  1 
ATOM   10292 C  CD  . GLU D 1 131 ? 40.528  -26.986 -10.314 1.00 114.32 ? 132 GLU D CD  1 
ATOM   10293 O  OE1 . GLU D 1 131 ? 41.622  -26.406 -10.491 1.00 116.15 ? 132 GLU D OE1 1 
ATOM   10294 O  OE2 . GLU D 1 131 ? 39.848  -27.444 -11.256 1.00 115.79 ? 132 GLU D OE2 1 
ATOM   10295 N  N   . LEU D 1 132 ? 38.218  -25.682 -5.764  1.00 84.91  ? 133 LEU D N   1 
ATOM   10296 C  CA  . LEU D 1 132 ? 36.930  -26.049 -5.175  1.00 79.02  ? 133 LEU D CA  1 
ATOM   10297 C  C   . LEU D 1 132 ? 35.833  -25.128 -5.682  1.00 77.27  ? 133 LEU D C   1 
ATOM   10298 O  O   . LEU D 1 132 ? 34.701  -25.556 -5.911  1.00 78.81  ? 133 LEU D O   1 
ATOM   10299 C  CB  . LEU D 1 132 ? 36.983  -25.993 -3.645  1.00 74.78  ? 133 LEU D CB  1 
ATOM   10300 C  CG  . LEU D 1 132 ? 37.925  -26.941 -2.903  1.00 75.34  ? 133 LEU D CG  1 
ATOM   10301 C  CD1 . LEU D 1 132 ? 37.745  -26.785 -1.402  1.00 72.30  ? 133 LEU D CD1 1 
ATOM   10302 C  CD2 . LEU D 1 132 ? 37.681  -28.380 -3.324  1.00 76.94  ? 133 LEU D CD2 1 
ATOM   10303 N  N   . TYR D 1 133 ? 36.180  -23.859 -5.866  1.00 76.08  ? 134 TYR D N   1 
ATOM   10304 C  CA  . TYR D 1 133 ? 35.259  -22.907 -6.464  1.00 74.13  ? 134 TYR D CA  1 
ATOM   10305 C  C   . TYR D 1 133 ? 35.331  -22.913 -7.988  1.00 75.65  ? 134 TYR D C   1 
ATOM   10306 O  O   . TYR D 1 133 ? 34.299  -22.880 -8.659  1.00 75.24  ? 134 TYR D O   1 
ATOM   10307 C  CB  . TYR D 1 133 ? 35.530  -21.492 -5.956  1.00 76.03  ? 134 TYR D CB  1 
ATOM   10308 C  CG  . TYR D 1 133 ? 34.941  -20.438 -6.865  1.00 79.26  ? 134 TYR D CG  1 
ATOM   10309 C  CD1 . TYR D 1 133 ? 33.568  -20.251 -6.942  1.00 78.85  ? 134 TYR D CD1 1 
ATOM   10310 C  CD2 . TYR D 1 133 ? 35.757  -19.646 -7.663  1.00 80.11  ? 134 TYR D CD2 1 
ATOM   10311 C  CE1 . TYR D 1 133 ? 33.023  -19.299 -7.780  1.00 78.78  ? 134 TYR D CE1 1 
ATOM   10312 C  CE2 . TYR D 1 133 ? 35.220  -18.691 -8.504  1.00 80.33  ? 134 TYR D CE2 1 
ATOM   10313 C  CZ  . TYR D 1 133 ? 33.853  -18.521 -8.558  1.00 80.22  ? 134 TYR D CZ  1 
ATOM   10314 O  OH  . TYR D 1 133 ? 33.314  -17.569 -9.393  1.00 80.14  ? 134 TYR D OH  1 
ATOM   10315 N  N   . THR D 1 134 ? 36.545  -22.953 -8.533  1.00 75.59  ? 135 THR D N   1 
ATOM   10316 C  CA  . THR D 1 134 ? 36.729  -22.708 -9.963  1.00 79.08  ? 135 THR D CA  1 
ATOM   10317 C  C   . THR D 1 134 ? 36.140  -23.836 -10.803 1.00 84.82  ? 135 THR D C   1 
ATOM   10318 O  O   . THR D 1 134 ? 35.778  -23.634 -11.961 1.00 86.44  ? 135 THR D O   1 
ATOM   10319 C  CB  . THR D 1 134 ? 38.216  -22.528 -10.332 1.00 73.56  ? 135 THR D CB  1 
ATOM   10320 O  OG1 . THR D 1 134 ? 38.894  -23.785 -10.241 1.00 72.39  ? 135 THR D OG1 1 
ATOM   10321 C  CG2 . THR D 1 134 ? 38.880  -21.520 -9.404  1.00 61.37  ? 135 THR D CG2 1 
ATOM   10322 N  N   . GLN D 1 135 ? 36.049  -25.024 -10.213 1.00 91.84  ? 136 GLN D N   1 
ATOM   10323 C  CA  . GLN D 1 135 ? 35.421  -26.161 -10.874 1.00 96.86  ? 136 GLN D CA  1 
ATOM   10324 C  C   . GLN D 1 135 ? 33.915  -25.988 -10.986 1.00 96.66  ? 136 GLN D C   1 
ATOM   10325 O  O   . GLN D 1 135 ? 33.289  -26.519 -11.904 1.00 100.79 ? 136 GLN D O   1 
ATOM   10326 C  CB  . GLN D 1 135 ? 35.729  -27.462 -10.127 1.00 102.17 ? 136 GLN D CB  1 
ATOM   10327 C  CG  . GLN D 1 135 ? 36.950  -28.204 -10.635 1.00 107.30 ? 136 GLN D CG  1 
ATOM   10328 C  CD  . GLN D 1 135 ? 36.593  -29.271 -11.652 1.00 111.62 ? 136 GLN D CD  1 
ATOM   10329 O  OE1 . GLN D 1 135 ? 37.127  -29.295 -12.762 1.00 113.86 ? 136 GLN D OE1 1 
ATOM   10330 N  NE2 . GLN D 1 135 ? 35.684  -30.164 -11.275 1.00 111.76 ? 136 GLN D NE2 1 
ATOM   10331 N  N   . ASN D 1 136 ? 33.339  -25.242 -10.049 1.00 92.40  ? 137 ASN D N   1 
ATOM   10332 C  CA  . ASN D 1 136 ? 31.893  -25.195 -9.898  1.00 87.49  ? 137 ASN D CA  1 
ATOM   10333 C  C   . ASN D 1 136 ? 31.318  -23.785 -10.000 1.00 85.42  ? 137 ASN D C   1 
ATOM   10334 O  O   . ASN D 1 136 ? 30.187  -23.544 -9.580  1.00 84.63  ? 137 ASN D O   1 
ATOM   10335 C  CB  . ASN D 1 136 ? 31.504  -25.812 -8.554  1.00 84.67  ? 137 ASN D CB  1 
ATOM   10336 C  CG  . ASN D 1 136 ? 32.190  -27.143 -8.304  1.00 81.95  ? 137 ASN D CG  1 
ATOM   10337 O  OD1 . ASN D 1 136 ? 32.839  -27.333 -7.276  1.00 81.06  ? 137 ASN D OD1 1 
ATOM   10338 N  ND2 . ASN D 1 136 ? 32.047  -28.071 -9.244  1.00 82.35  ? 137 ASN D ND2 1 
ATOM   10339 N  N   . ALA D 1 137 ? 32.100  -22.863 -10.558 1.00 82.48  ? 138 ALA D N   1 
ATOM   10340 C  CA  . ALA D 1 137 ? 31.693  -21.463 -10.681 1.00 80.93  ? 138 ALA D CA  1 
ATOM   10341 C  C   . ALA D 1 137 ? 30.385  -21.318 -11.452 1.00 80.10  ? 138 ALA D C   1 
ATOM   10342 O  O   . ALA D 1 137 ? 29.557  -20.455 -11.145 1.00 79.18  ? 138 ALA D O   1 
ATOM   10343 C  CB  . ALA D 1 137 ? 32.790  -20.655 -11.353 1.00 78.09  ? 138 ALA D CB  1 
ATOM   10344 N  N   . ARG D 1 138 ? 30.203  -22.173 -12.452 1.00 82.99  ? 139 ARG D N   1 
ATOM   10345 C  CA  . ARG D 1 138 ? 28.989  -22.154 -13.250 1.00 83.08  ? 139 ARG D CA  1 
ATOM   10346 C  C   . ARG D 1 138 ? 27.756  -22.459 -12.401 1.00 77.99  ? 139 ARG D C   1 
ATOM   10347 O  O   . ARG D 1 138 ? 26.679  -21.930 -12.665 1.00 81.44  ? 139 ARG D O   1 
ATOM   10348 C  CB  . ARG D 1 138 ? 29.087  -23.148 -14.404 1.00 92.46  ? 139 ARG D CB  1 
ATOM   10349 C  CG  . ARG D 1 138 ? 28.109  -22.864 -15.528 1.00 100.41 ? 139 ARG D CG  1 
ATOM   10350 C  CD  . ARG D 1 138 ? 28.750  -23.112 -16.881 1.00 107.34 ? 139 ARG D CD  1 
ATOM   10351 N  NE  . ARG D 1 138 ? 27.959  -22.555 -17.974 1.00 111.55 ? 139 ARG D NE  1 
ATOM   10352 C  CZ  . ARG D 1 138 ? 26.901  -23.153 -18.514 1.00 114.48 ? 139 ARG D CZ  1 
ATOM   10353 N  NH1 . ARG D 1 138 ? 26.497  -24.335 -18.065 1.00 114.38 ? 139 ARG D NH1 1 
ATOM   10354 N  NH2 . ARG D 1 138 ? 26.245  -22.568 -19.506 1.00 115.99 ? 139 ARG D NH2 1 
ATOM   10355 N  N   . ALA D 1 139 ? 27.911  -23.313 -11.391 1.00 68.60  ? 140 ALA D N   1 
ATOM   10356 C  CA  . ALA D 1 139 ? 26.808  -23.620 -10.484 1.00 64.94  ? 140 ALA D CA  1 
ATOM   10357 C  C   . ALA D 1 139 ? 26.377  -22.371 -9.722  1.00 60.82  ? 140 ALA D C   1 
ATOM   10358 O  O   . ALA D 1 139 ? 25.181  -22.088 -9.591  1.00 58.63  ? 140 ALA D O   1 
ATOM   10359 C  CB  . ALA D 1 139 ? 27.200  -24.726 -9.515  1.00 63.90  ? 140 ALA D CB  1 
ATOM   10360 N  N   . PHE D 1 140 ? 27.363  -21.633 -9.220  1.00 53.36  ? 141 PHE D N   1 
ATOM   10361 C  CA  . PHE D 1 140 ? 27.117  -20.379 -8.519  1.00 61.79  ? 141 PHE D CA  1 
ATOM   10362 C  C   . PHE D 1 140 ? 26.436  -19.369 -9.440  1.00 55.85  ? 141 PHE D C   1 
ATOM   10363 O  O   . PHE D 1 140 ? 25.481  -18.691 -9.042  1.00 58.07  ? 141 PHE D O   1 
ATOM   10364 C  CB  . PHE D 1 140 ? 28.427  -19.803 -7.976  1.00 61.59  ? 141 PHE D CB  1 
ATOM   10365 C  CG  . PHE D 1 140 ? 29.064  -20.645 -6.903  1.00 52.27  ? 141 PHE D CG  1 
ATOM   10366 C  CD1 . PHE D 1 140 ? 29.955  -21.653 -7.230  1.00 53.44  ? 141 PHE D CD1 1 
ATOM   10367 C  CD2 . PHE D 1 140 ? 28.774  -20.424 -5.567  1.00 51.29  ? 141 PHE D CD2 1 
ATOM   10368 C  CE1 . PHE D 1 140 ? 30.542  -22.428 -6.246  1.00 58.23  ? 141 PHE D CE1 1 
ATOM   10369 C  CE2 . PHE D 1 140 ? 29.358  -21.193 -4.578  1.00 53.27  ? 141 PHE D CE2 1 
ATOM   10370 C  CZ  . PHE D 1 140 ? 30.243  -22.197 -4.918  1.00 56.12  ? 141 PHE D CZ  1 
ATOM   10371 N  N   . ARG D 1 141 ? 26.930  -19.278 -10.673 1.00 60.05  ? 142 ARG D N   1 
ATOM   10372 C  CA  . ARG D 1 141 ? 26.340  -18.384 -11.665 1.00 67.22  ? 142 ARG D CA  1 
ATOM   10373 C  C   . ARG D 1 141 ? 24.871  -18.720 -11.902 1.00 72.28  ? 142 ARG D C   1 
ATOM   10374 O  O   . ARG D 1 141 ? 24.012  -17.834 -11.898 1.00 75.81  ? 142 ARG D O   1 
ATOM   10375 C  CB  . ARG D 1 141 ? 27.115  -18.450 -12.982 1.00 74.50  ? 142 ARG D CB  1 
ATOM   10376 C  CG  . ARG D 1 141 ? 26.337  -17.933 -14.183 1.00 81.21  ? 142 ARG D CG  1 
ATOM   10377 C  CD  . ARG D 1 141 ? 27.270  -17.385 -15.248 1.00 88.41  ? 142 ARG D CD  1 
ATOM   10378 N  NE  . ARG D 1 141 ? 28.227  -16.435 -14.688 1.00 94.09  ? 142 ARG D NE  1 
ATOM   10379 C  CZ  . ARG D 1 141 ? 28.176  -15.121 -14.882 1.00 98.32  ? 142 ARG D CZ  1 
ATOM   10380 N  NH1 . ARG D 1 141 ? 27.209  -14.594 -15.621 1.00 99.07  ? 142 ARG D NH1 1 
ATOM   10381 N  NH2 . ARG D 1 141 ? 29.089  -14.331 -14.333 1.00 99.38  ? 142 ARG D NH2 1 
ATOM   10382 N  N   . ASP D 1 142 ? 24.590  -20.003 -12.103 1.00 71.77  ? 143 ASP D N   1 
ATOM   10383 C  CA  . ASP D 1 142 ? 23.220  -20.471 -12.272 1.00 68.17  ? 143 ASP D CA  1 
ATOM   10384 C  C   . ASP D 1 142 ? 22.370  -20.098 -11.065 1.00 59.84  ? 143 ASP D C   1 
ATOM   10385 O  O   . ASP D 1 142 ? 21.222  -19.671 -11.215 1.00 58.24  ? 143 ASP D O   1 
ATOM   10386 C  CB  . ASP D 1 142 ? 23.192  -21.984 -12.501 1.00 76.27  ? 143 ASP D CB  1 
ATOM   10387 C  CG  . ASP D 1 142 ? 23.645  -22.370 -13.896 1.00 82.10  ? 143 ASP D CG  1 
ATOM   10388 O  OD1 . ASP D 1 142 ? 24.549  -21.700 -14.437 1.00 83.86  ? 143 ASP D OD1 1 
ATOM   10389 O  OD2 . ASP D 1 142 ? 23.097  -23.345 -14.453 1.00 85.11  ? 143 ASP D OD2 1 
ATOM   10390 N  N   . LEU D 1 143 ? 22.942  -20.245 -9.872  1.00 58.25  ? 144 LEU D N   1 
ATOM   10391 C  CA  . LEU D 1 143 ? 22.246  -19.859 -8.648  1.00 59.74  ? 144 LEU D CA  1 
ATOM   10392 C  C   . LEU D 1 143 ? 21.857  -18.387 -8.678  1.00 56.33  ? 144 LEU D C   1 
ATOM   10393 O  O   . LEU D 1 143 ? 20.720  -18.033 -8.362  1.00 60.85  ? 144 LEU D O   1 
ATOM   10394 C  CB  . LEU D 1 143 ? 23.105  -20.137 -7.414  1.00 49.60  ? 144 LEU D CB  1 
ATOM   10395 C  CG  . LEU D 1 143 ? 22.527  -19.557 -6.120  1.00 48.41  ? 144 LEU D CG  1 
ATOM   10396 C  CD1 . LEU D 1 143 ? 21.217  -20.241 -5.763  1.00 48.23  ? 144 LEU D CD1 1 
ATOM   10397 C  CD2 . LEU D 1 143 ? 23.521  -19.656 -4.975  1.00 50.75  ? 144 LEU D CD2 1 
ATOM   10398 N  N   . TYR D 1 144 ? 22.801  -17.533 -9.062  1.00 56.74  ? 145 TYR D N   1 
ATOM   10399 C  CA  . TYR D 1 144 ? 22.537  -16.098 -9.106  1.00 53.71  ? 145 TYR D CA  1 
ATOM   10400 C  C   . TYR D 1 144 ? 21.506  -15.734 -10.173 1.00 52.59  ? 145 TYR D C   1 
ATOM   10401 O  O   . TYR D 1 144 ? 20.701  -14.821 -9.977  1.00 54.30  ? 145 TYR D O   1 
ATOM   10402 C  CB  . TYR D 1 144 ? 23.836  -15.324 -9.334  1.00 55.37  ? 145 TYR D CB  1 
ATOM   10403 C  CG  . TYR D 1 144 ? 24.553  -14.988 -8.047  1.00 54.71  ? 145 TYR D CG  1 
ATOM   10404 C  CD1 . TYR D 1 144 ? 24.221  -13.850 -7.325  1.00 53.12  ? 145 TYR D CD1 1 
ATOM   10405 C  CD2 . TYR D 1 144 ? 25.551  -15.813 -7.546  1.00 55.86  ? 145 TYR D CD2 1 
ATOM   10406 C  CE1 . TYR D 1 144 ? 24.866  -13.537 -6.145  1.00 53.35  ? 145 TYR D CE1 1 
ATOM   10407 C  CE2 . TYR D 1 144 ? 26.203  -15.508 -6.364  1.00 55.73  ? 145 TYR D CE2 1 
ATOM   10408 C  CZ  . TYR D 1 144 ? 25.856  -14.368 -5.669  1.00 54.18  ? 145 TYR D CZ  1 
ATOM   10409 O  OH  . TYR D 1 144 ? 26.499  -14.057 -4.494  1.00 55.45  ? 145 TYR D OH  1 
ATOM   10410 N  N   . SER D 1 145 ? 21.527  -16.449 -11.294 1.00 56.35  ? 146 SER D N   1 
ATOM   10411 C  CA  . SER D 1 145 ? 20.519  -16.251 -12.332 1.00 57.94  ? 146 SER D CA  1 
ATOM   10412 C  C   . SER D 1 145 ? 19.137  -16.605 -11.793 1.00 59.02  ? 146 SER D C   1 
ATOM   10413 O  O   . SER D 1 145 ? 18.152  -15.896 -12.035 1.00 58.65  ? 146 SER D O   1 
ATOM   10414 C  CB  . SER D 1 145 ? 20.841  -17.093 -13.568 1.00 59.02  ? 146 SER D CB  1 
ATOM   10415 O  OG  . SER D 1 145 ? 22.064  -16.688 -14.157 1.00 60.51  ? 146 SER D OG  1 
ATOM   10416 N  N   . GLU D 1 146 ? 19.077  -17.705 -11.050 1.00 61.24  ? 147 GLU D N   1 
ATOM   10417 C  CA  . GLU D 1 146 ? 17.835  -18.141 -10.427 1.00 63.23  ? 147 GLU D CA  1 
ATOM   10418 C  C   . GLU D 1 146 ? 17.338  -17.120 -9.410  1.00 60.01  ? 147 GLU D C   1 
ATOM   10419 O  O   . GLU D 1 146 ? 16.137  -16.878 -9.300  1.00 58.47  ? 147 GLU D O   1 
ATOM   10420 C  CB  . GLU D 1 146 ? 18.025  -19.504 -9.764  1.00 71.62  ? 147 GLU D CB  1 
ATOM   10421 C  CG  . GLU D 1 146 ? 18.227  -20.641 -10.752 1.00 78.71  ? 147 GLU D CG  1 
ATOM   10422 C  CD  . GLU D 1 146 ? 17.027  -20.846 -11.654 1.00 84.43  ? 147 GLU D CD  1 
ATOM   10423 O  OE1 . GLU D 1 146 ? 15.885  -20.695 -11.170 1.00 86.10  ? 147 GLU D OE1 1 
ATOM   10424 O  OE2 . GLU D 1 146 ? 17.225  -21.159 -12.847 1.00 88.04  ? 147 GLU D OE2 1 
ATOM   10425 N  N   . LEU D 1 147 ? 18.265  -16.519 -8.670  1.00 58.72  ? 148 LEU D N   1 
ATOM   10426 C  CA  . LEU D 1 147 ? 17.915  -15.467 -7.724  1.00 52.22  ? 148 LEU D CA  1 
ATOM   10427 C  C   . LEU D 1 147 ? 17.343  -14.258 -8.458  1.00 47.73  ? 148 LEU D C   1 
ATOM   10428 O  O   . LEU D 1 147 ? 16.351  -13.665 -8.021  1.00 47.08  ? 148 LEU D O   1 
ATOM   10429 C  CB  . LEU D 1 147 ? 19.132  -15.060 -6.891  1.00 54.29  ? 148 LEU D CB  1 
ATOM   10430 C  CG  . LEU D 1 147 ? 19.566  -16.065 -5.823  1.00 51.10  ? 148 LEU D CG  1 
ATOM   10431 C  CD1 . LEU D 1 147 ? 20.765  -15.545 -5.046  1.00 52.93  ? 148 LEU D CD1 1 
ATOM   10432 C  CD2 . LEU D 1 147 ? 18.410  -16.373 -4.884  1.00 46.35  ? 148 LEU D CD2 1 
ATOM   10433 N  N   . ARG D 1 148 ? 17.972  -13.903 -9.577  1.00 48.68  ? 149 ARG D N   1 
ATOM   10434 C  CA  . ARG D 1 148 ? 17.483  -12.814 -10.419 1.00 49.55  ? 149 ARG D CA  1 
ATOM   10435 C  C   . ARG D 1 148 ? 16.060  -13.077 -10.884 1.00 55.93  ? 149 ARG D C   1 
ATOM   10436 O  O   . ARG D 1 148 ? 15.209  -12.188 -10.842 1.00 56.40  ? 149 ARG D O   1 
ATOM   10437 C  CB  . ARG D 1 148 ? 18.385  -12.610 -11.636 1.00 50.92  ? 149 ARG D CB  1 
ATOM   10438 C  CG  . ARG D 1 148 ? 19.716  -11.965 -11.329 1.00 50.29  ? 149 ARG D CG  1 
ATOM   10439 C  CD  . ARG D 1 148 ? 20.466  -11.642 -12.605 1.00 50.19  ? 149 ARG D CD  1 
ATOM   10440 N  NE  . ARG D 1 148 ? 21.838  -11.233 -12.332 1.00 51.72  ? 149 ARG D NE  1 
ATOM   10441 C  CZ  . ARG D 1 148 ? 22.879  -12.058 -12.357 1.00 54.09  ? 149 ARG D CZ  1 
ATOM   10442 N  NH1 . ARG D 1 148 ? 22.702  -13.340 -12.645 1.00 53.62  ? 149 ARG D NH1 1 
ATOM   10443 N  NH2 . ARG D 1 148 ? 24.095  -11.601 -12.096 1.00 52.68  ? 149 ARG D NH2 1 
ATOM   10444 N  N   . LEU D 1 149 ? 15.808  -14.302 -11.332 1.00 60.45  ? 150 LEU D N   1 
ATOM   10445 C  CA  . LEU D 1 149 ? 14.474  -14.665 -11.789 1.00 57.98  ? 150 LEU D CA  1 
ATOM   10446 C  C   . LEU D 1 149 ? 13.467  -14.614 -10.644 1.00 57.94  ? 150 LEU D C   1 
ATOM   10447 O  O   . LEU D 1 149 ? 12.343  -14.151 -10.825 1.00 61.26  ? 150 LEU D O   1 
ATOM   10448 C  CB  . LEU D 1 149 ? 14.484  -16.052 -12.433 1.00 65.36  ? 150 LEU D CB  1 
ATOM   10449 C  CG  . LEU D 1 149 ? 15.214  -16.105 -13.776 1.00 69.79  ? 150 LEU D CG  1 
ATOM   10450 C  CD1 . LEU D 1 149 ? 15.129  -17.493 -14.390 1.00 71.45  ? 150 LEU D CD1 1 
ATOM   10451 C  CD2 . LEU D 1 149 ? 14.654  -15.055 -14.726 1.00 69.59  ? 150 LEU D CD2 1 
ATOM   10452 N  N   . TYR D 1 150 ? 13.877  -15.070 -9.464  1.00 56.57  ? 151 TYR D N   1 
ATOM   10453 C  CA  . TYR D 1 150 ? 12.996  -15.043 -8.301  1.00 55.33  ? 151 TYR D CA  1 
ATOM   10454 C  C   . TYR D 1 150 ? 12.617  -13.614 -7.930  1.00 61.13  ? 151 TYR D C   1 
ATOM   10455 O  O   . TYR D 1 150 ? 11.460  -13.333 -7.617  1.00 59.70  ? 151 TYR D O   1 
ATOM   10456 C  CB  . TYR D 1 150 ? 13.645  -15.735 -7.101  1.00 56.47  ? 151 TYR D CB  1 
ATOM   10457 C  CG  . TYR D 1 150 ? 12.767  -15.735 -5.869  1.00 58.08  ? 151 TYR D CG  1 
ATOM   10458 C  CD1 . TYR D 1 150 ? 11.537  -16.380 -5.872  1.00 62.55  ? 151 TYR D CD1 1 
ATOM   10459 C  CD2 . TYR D 1 150 ? 13.163  -15.084 -4.708  1.00 53.47  ? 151 TYR D CD2 1 
ATOM   10460 C  CE1 . TYR D 1 150 ? 10.726  -16.382 -4.752  1.00 63.18  ? 151 TYR D CE1 1 
ATOM   10461 C  CE2 . TYR D 1 150 ? 12.359  -15.080 -3.582  1.00 56.33  ? 151 TYR D CE2 1 
ATOM   10462 C  CZ  . TYR D 1 150 ? 11.142  -15.731 -3.610  1.00 63.33  ? 151 TYR D CZ  1 
ATOM   10463 O  OH  . TYR D 1 150 ? 10.336  -15.731 -2.494  1.00 66.14  ? 151 TYR D OH  1 
ATOM   10464 N  N   . TYR D 1 151 ? 13.596  -12.714 -7.967  1.00 59.58  ? 152 TYR D N   1 
ATOM   10465 C  CA  . TYR D 1 151 ? 13.335  -11.307 -7.681  1.00 57.04  ? 152 TYR D CA  1 
ATOM   10466 C  C   . TYR D 1 151 ? 12.400  -10.684 -8.714  1.00 57.44  ? 152 TYR D C   1 
ATOM   10467 O  O   . TYR D 1 151 ? 11.603  -9.803  -8.390  1.00 56.87  ? 152 TYR D O   1 
ATOM   10468 C  CB  . TYR D 1 151 ? 14.643  -10.512 -7.624  1.00 55.64  ? 152 TYR D CB  1 
ATOM   10469 C  CG  . TYR D 1 151 ? 14.448  -9.015  -7.737  1.00 56.04  ? 152 TYR D CG  1 
ATOM   10470 C  CD1 . TYR D 1 151 ? 14.031  -8.264  -6.646  1.00 41.07  ? 152 TYR D CD1 1 
ATOM   10471 C  CD2 . TYR D 1 151 ? 14.677  -8.353  -8.938  1.00 42.27  ? 152 TYR D CD2 1 
ATOM   10472 C  CE1 . TYR D 1 151 ? 13.848  -6.898  -6.746  1.00 40.64  ? 152 TYR D CE1 1 
ATOM   10473 C  CE2 . TYR D 1 151 ? 14.497  -6.988  -9.048  1.00 41.83  ? 152 TYR D CE2 1 
ATOM   10474 C  CZ  . TYR D 1 151 ? 14.083  -6.265  -7.950  1.00 49.22  ? 152 TYR D CZ  1 
ATOM   10475 O  OH  . TYR D 1 151 ? 13.902  -4.905  -8.056  1.00 40.65  ? 152 TYR D OH  1 
ATOM   10476 N  N   . ARG D 1 152 ? 12.496  -11.152 -9.954  1.00 62.31  ? 153 ARG D N   1 
ATOM   10477 C  CA  . ARG D 1 152 ? 11.773  -10.531 -11.061 1.00 71.13  ? 153 ARG D CA  1 
ATOM   10478 C  C   . ARG D 1 152 ? 10.275  -10.833 -11.061 1.00 77.47  ? 153 ARG D C   1 
ATOM   10479 O  O   . ARG D 1 152 ? 9.537   -10.315 -11.898 1.00 78.24  ? 153 ARG D O   1 
ATOM   10480 C  CB  . ARG D 1 152 ? 12.384  -10.964 -12.396 1.00 75.81  ? 153 ARG D CB  1 
ATOM   10481 C  CG  . ARG D 1 152 ? 12.964  -9.808  -13.195 1.00 82.29  ? 153 ARG D CG  1 
ATOM   10482 C  CD  . ARG D 1 152 ? 13.494  -10.257 -14.544 1.00 88.59  ? 153 ARG D CD  1 
ATOM   10483 N  NE  . ARG D 1 152 ? 13.709  -9.122  -15.438 1.00 94.37  ? 153 ARG D NE  1 
ATOM   10484 C  CZ  . ARG D 1 152 ? 14.883  -8.528  -15.625 1.00 99.03  ? 153 ARG D CZ  1 
ATOM   10485 N  NH1 . ARG D 1 152 ? 15.958  -8.961  -14.980 1.00 100.09 ? 153 ARG D NH1 1 
ATOM   10486 N  NH2 . ARG D 1 152 ? 14.983  -7.500  -16.456 1.00 99.65  ? 153 ARG D NH2 1 
ATOM   10487 N  N   . GLY D 1 153 ? 9.826   -11.663 -10.127 1.00 79.40  ? 154 GLY D N   1 
ATOM   10488 C  CA  . GLY D 1 153 ? 8.414   -11.985 -10.028 1.00 82.78  ? 154 GLY D CA  1 
ATOM   10489 C  C   . GLY D 1 153 ? 8.060   -13.254 -10.774 1.00 87.36  ? 154 GLY D C   1 
ATOM   10490 O  O   . GLY D 1 153 ? 6.890   -13.547 -11.015 1.00 85.83  ? 154 GLY D O   1 
ATOM   10491 N  N   . ALA D 1 154 ? 9.087   -14.014 -11.133 1.00 94.72  ? 155 ALA D N   1 
ATOM   10492 C  CA  . ALA D 1 154 ? 8.911   -15.306 -11.780 1.00 105.54 ? 155 ALA D CA  1 
ATOM   10493 C  C   . ALA D 1 154 ? 8.285   -16.290 -10.798 1.00 119.03 ? 155 ALA D C   1 
ATOM   10494 O  O   . ALA D 1 154 ? 8.285   -16.062 -9.589  1.00 120.37 ? 155 ALA D O   1 
ATOM   10495 C  CB  . ALA D 1 154 ? 10.227  -15.832 -12.312 1.00 102.09 ? 155 ALA D CB  1 
ATOM   10496 N  N   . ASN D 1 155 ? 7.767   -17.392 -11.327 1.00 133.28 ? 156 ASN D N   1 
ATOM   10497 C  CA  . ASN D 1 155 ? 6.869   -18.279 -10.596 1.00 134.64 ? 156 ASN D CA  1 
ATOM   10498 C  C   . ASN D 1 155 ? 7.643   -19.210 -9.674  1.00 133.23 ? 156 ASN D C   1 
ATOM   10499 O  O   . ASN D 1 155 ? 7.070   -20.103 -9.048  1.00 135.76 ? 156 ASN D O   1 
ATOM   10500 C  CB  . ASN D 1 155 ? 6.015   -19.094 -11.569 1.00 137.87 ? 156 ASN D CB  1 
ATOM   10501 N  N   . LEU D 1 156 ? 8.954   -18.991 -9.614  1.00 122.36 ? 157 LEU D N   1 
ATOM   10502 C  CA  . LEU D 1 156 ? 9.875   -19.824 -8.852  1.00 112.55 ? 157 LEU D CA  1 
ATOM   10503 C  C   . LEU D 1 156 ? 9.470   -20.102 -7.416  1.00 104.10 ? 157 LEU D C   1 
ATOM   10504 O  O   . LEU D 1 156 ? 9.093   -19.200 -6.665  1.00 103.24 ? 157 LEU D O   1 
ATOM   10505 C  CB  . LEU D 1 156 ? 11.261  -19.173 -8.808  1.00 107.08 ? 157 LEU D CB  1 
ATOM   10506 C  CG  . LEU D 1 156 ? 12.294  -19.389 -9.910  1.00 102.27 ? 157 LEU D CG  1 
ATOM   10507 C  CD1 . LEU D 1 156 ? 11.844  -18.785 -11.223 1.00 98.49  ? 157 LEU D CD1 1 
ATOM   10508 C  CD2 . LEU D 1 156 ? 13.625  -18.802 -9.471  1.00 98.10  ? 157 LEU D CD2 1 
ATOM   10509 N  N   . HIS D 1 157 ? 9.546   -21.376 -7.055  1.00 101.21 ? 158 HIS D N   1 
ATOM   10510 C  CA  . HIS D 1 157 ? 9.671   -21.758 -5.664  1.00 94.04  ? 158 HIS D CA  1 
ATOM   10511 C  C   . HIS D 1 157 ? 11.160  -21.727 -5.330  1.00 90.00  ? 158 HIS D C   1 
ATOM   10512 O  O   . HIS D 1 157 ? 11.922  -22.592 -5.766  1.00 88.95  ? 158 HIS D O   1 
ATOM   10513 C  CB  . HIS D 1 157 ? 9.071   -23.140 -5.407  1.00 93.59  ? 158 HIS D CB  1 
ATOM   10514 N  N   . LEU D 1 158 ? 11.562  -20.709 -4.573  1.00 86.47  ? 159 LEU D N   1 
ATOM   10515 C  CA  . LEU D 1 158 ? 12.955  -20.500 -4.177  1.00 85.45  ? 159 LEU D CA  1 
ATOM   10516 C  C   . LEU D 1 158 ? 13.514  -21.707 -3.428  1.00 90.18  ? 159 LEU D C   1 
ATOM   10517 O  O   . LEU D 1 158 ? 14.626  -22.173 -3.705  1.00 95.01  ? 159 LEU D O   1 
ATOM   10518 C  CB  . LEU D 1 158 ? 13.061  -19.244 -3.307  1.00 76.62  ? 159 LEU D CB  1 
ATOM   10519 C  CG  . LEU D 1 158 ? 14.427  -18.846 -2.751  1.00 68.07  ? 159 LEU D CG  1 
ATOM   10520 C  CD1 . LEU D 1 158 ? 15.386  -18.551 -3.887  1.00 64.38  ? 159 LEU D CD1 1 
ATOM   10521 C  CD2 . LEU D 1 158 ? 14.292  -17.642 -1.839  1.00 65.58  ? 159 LEU D CD2 1 
ATOM   10522 N  N   . GLU D 1 159 ? 12.718  -22.183 -2.473  1.00 93.19  ? 160 GLU D N   1 
ATOM   10523 C  CA  . GLU D 1 159 ? 12.977  -23.393 -1.699  1.00 91.58  ? 160 GLU D CA  1 
ATOM   10524 C  C   . GLU D 1 159 ? 13.627  -24.515 -2.526  1.00 94.51  ? 160 GLU D C   1 
ATOM   10525 O  O   . GLU D 1 159 ? 14.712  -25.006 -2.191  1.00 95.74  ? 160 GLU D O   1 
ATOM   10526 C  CB  . GLU D 1 159 ? 11.667  -23.914 -1.070  1.00 92.93  ? 160 GLU D CB  1 
ATOM   10527 C  CG  . GLU D 1 159 ? 10.678  -22.883 -0.442  1.00 130.00 ? 160 GLU D CG  1 
ATOM   10528 C  CD  . GLU D 1 159 ? 10.027  -21.902 -1.424  1.00 129.68 ? 160 GLU D CD  1 
ATOM   10529 O  OE1 . GLU D 1 159 ? 10.474  -21.806 -2.580  1.00 129.88 ? 160 GLU D OE1 1 
ATOM   10530 O  OE2 . GLU D 1 159 ? 9.056   -21.220 -1.030  1.00 129.18 ? 160 GLU D OE2 1 
ATOM   10531 N  N   . GLU D 1 160 ? 12.953  -24.908 -3.604  1.00 93.60  ? 161 GLU D N   1 
ATOM   10532 C  CA  . GLU D 1 160 ? 13.407  -25.989 -4.480  1.00 94.18  ? 161 GLU D CA  1 
ATOM   10533 C  C   . GLU D 1 160 ? 14.781  -25.717 -5.091  1.00 89.73  ? 161 GLU D C   1 
ATOM   10534 O  O   . GLU D 1 160 ? 15.682  -26.566 -5.044  1.00 92.87  ? 161 GLU D O   1 
ATOM   10535 C  CB  . GLU D 1 160 ? 12.384  -26.210 -5.596  1.00 99.06  ? 161 GLU D CB  1 
ATOM   10536 C  CG  . GLU D 1 160 ? 11.707  -27.567 -5.569  1.00 104.99 ? 161 GLU D CG  1 
ATOM   10537 C  CD  . GLU D 1 160 ? 11.091  -27.928 -6.904  1.00 110.04 ? 161 GLU D CD  1 
ATOM   10538 O  OE1 . GLU D 1 160 ? 10.207  -27.180 -7.375  1.00 111.73 ? 161 GLU D OE1 1 
ATOM   10539 O  OE2 . GLU D 1 160 ? 11.497  -28.955 -7.486  1.00 111.51 ? 161 GLU D OE2 1 
ATOM   10540 N  N   . THR D 1 161 ? 14.922  -24.528 -5.669  1.00 81.03  ? 162 THR D N   1 
ATOM   10541 C  CA  . THR D 1 161 ? 16.158  -24.111 -6.318  1.00 74.12  ? 162 THR D CA  1 
ATOM   10542 C  C   . THR D 1 161 ? 17.327  -24.191 -5.343  1.00 65.11  ? 162 THR D C   1 
ATOM   10543 O  O   . THR D 1 161 ? 18.384  -24.762 -5.654  1.00 62.70  ? 162 THR D O   1 
ATOM   10544 C  CB  . THR D 1 161 ? 16.044  -22.677 -6.866  1.00 77.83  ? 162 THR D CB  1 
ATOM   10545 O  OG1 . THR D 1 161 ? 14.729  -22.462 -7.396  1.00 79.31  ? 162 THR D OG1 1 
ATOM   10546 C  CG2 . THR D 1 161 ? 17.068  -22.445 -7.952  1.00 79.24  ? 162 THR D CG2 1 
ATOM   10547 N  N   . LEU D 1 162 ? 17.118  -23.623 -4.159  1.00 59.43  ? 163 LEU D N   1 
ATOM   10548 C  CA  . LEU D 1 162 ? 18.104  -23.679 -3.088  1.00 58.17  ? 163 LEU D CA  1 
ATOM   10549 C  C   . LEU D 1 162 ? 18.484  -25.117 -2.760  1.00 64.54  ? 163 LEU D C   1 
ATOM   10550 O  O   . LEU D 1 162 ? 19.665  -25.483 -2.784  1.00 62.13  ? 163 LEU D O   1 
ATOM   10551 C  CB  . LEU D 1 162 ? 17.566  -22.987 -1.835  1.00 55.43  ? 163 LEU D CB  1 
ATOM   10552 C  CG  . LEU D 1 162 ? 17.378  -21.473 -1.927  1.00 51.23  ? 163 LEU D CG  1 
ATOM   10553 C  CD1 . LEU D 1 162 ? 16.885  -20.919 -0.604  1.00 46.24  ? 163 LEU D CD1 1 
ATOM   10554 C  CD2 . LEU D 1 162 ? 18.680  -20.806 -2.337  1.00 46.76  ? 163 LEU D CD2 1 
ATOM   10555 N  N   . ALA D 1 163 ? 17.469  -25.925 -2.468  1.00 68.40  ? 164 ALA D N   1 
ATOM   10556 C  CA  . ALA D 1 163 ? 17.676  -27.312 -2.069  1.00 71.15  ? 164 ALA D CA  1 
ATOM   10557 C  C   . ALA D 1 163 ? 18.516  -28.084 -3.087  1.00 76.80  ? 164 ALA D C   1 
ATOM   10558 O  O   . ALA D 1 163 ? 19.524  -28.711 -2.725  1.00 78.96  ? 164 ALA D O   1 
ATOM   10559 C  CB  . ALA D 1 163 ? 16.332  -28.002 -1.854  1.00 75.51  ? 164 ALA D CB  1 
ATOM   10560 N  N   . GLU D 1 164 ? 18.124  -28.021 -4.360  1.00 78.67  ? 165 GLU D N   1 
ATOM   10561 C  CA  . GLU D 1 164 ? 18.830  -28.792 -5.383  1.00 85.89  ? 165 GLU D CA  1 
ATOM   10562 C  C   . GLU D 1 164 ? 20.235  -28.238 -5.617  1.00 83.92  ? 165 GLU D C   1 
ATOM   10563 O  O   . GLU D 1 164 ? 21.189  -29.003 -5.843  1.00 88.64  ? 165 GLU D O   1 
ATOM   10564 C  CB  . GLU D 1 164 ? 18.048  -28.824 -6.700  1.00 94.84  ? 165 GLU D CB  1 
ATOM   10565 C  CG  . GLU D 1 164 ? 18.837  -29.423 -7.873  1.00 103.17 ? 165 GLU D CG  1 
ATOM   10566 C  CD  . GLU D 1 164 ? 18.058  -30.505 -8.599  1.00 110.55 ? 165 GLU D CD  1 
ATOM   10567 O  OE1 . GLU D 1 164 ? 17.203  -31.145 -7.950  1.00 112.80 ? 165 GLU D OE1 1 
ATOM   10568 O  OE2 . GLU D 1 164 ? 18.310  -30.736 -9.802  1.00 113.43 ? 165 GLU D OE2 1 
ATOM   10569 N  N   . PHE D 1 165 ? 20.367  -26.915 -5.535  1.00 78.91  ? 166 PHE D N   1 
ATOM   10570 C  CA  . PHE D 1 165 ? 21.685  -26.287 -5.638  1.00 70.32  ? 166 PHE D CA  1 
ATOM   10571 C  C   . PHE D 1 165 ? 22.631  -26.850 -4.591  1.00 61.43  ? 166 PHE D C   1 
ATOM   10572 O  O   . PHE D 1 165 ? 23.742  -27.281 -4.914  1.00 58.76  ? 166 PHE D O   1 
ATOM   10573 C  CB  . PHE D 1 165 ? 21.605  -24.764 -5.482  1.00 59.80  ? 166 PHE D CB  1 
ATOM   10574 C  CG  . PHE D 1 165 ? 22.943  -24.114 -5.223  1.00 56.56  ? 166 PHE D CG  1 
ATOM   10575 C  CD1 . PHE D 1 165 ? 23.845  -23.913 -6.256  1.00 55.35  ? 166 PHE D CD1 1 
ATOM   10576 C  CD2 . PHE D 1 165 ? 23.304  -23.720 -3.942  1.00 53.90  ? 166 PHE D CD2 1 
ATOM   10577 C  CE1 . PHE D 1 165 ? 25.081  -23.322 -6.018  1.00 56.12  ? 166 PHE D CE1 1 
ATOM   10578 C  CE2 . PHE D 1 165 ? 24.536  -23.130 -3.697  1.00 55.89  ? 166 PHE D CE2 1 
ATOM   10579 C  CZ  . PHE D 1 165 ? 25.425  -22.930 -4.737  1.00 56.68  ? 166 PHE D CZ  1 
ATOM   10580 N  N   . TRP D 1 166 ? 22.188  -26.839 -3.336  1.00 64.69  ? 167 TRP D N   1 
ATOM   10581 C  CA  . TRP D 1 166 ? 22.996  -27.382 -2.248  1.00 63.66  ? 167 TRP D CA  1 
ATOM   10582 C  C   . TRP D 1 166 ? 23.308  -28.856 -2.477  1.00 71.97  ? 167 TRP D C   1 
ATOM   10583 O  O   . TRP D 1 166 ? 24.434  -29.304 -2.229  1.00 73.96  ? 167 TRP D O   1 
ATOM   10584 C  CB  . TRP D 1 166 ? 22.297  -27.207 -0.899  1.00 66.50  ? 167 TRP D CB  1 
ATOM   10585 C  CG  . TRP D 1 166 ? 22.293  -25.800 -0.378  1.00 67.33  ? 167 TRP D CG  1 
ATOM   10586 C  CD1 . TRP D 1 166 ? 21.206  -25.084 0.028   1.00 67.66  ? 167 TRP D CD1 1 
ATOM   10587 C  CD2 . TRP D 1 166 ? 23.428  -24.940 -0.200  1.00 69.90  ? 167 TRP D CD2 1 
ATOM   10588 N  NE1 . TRP D 1 166 ? 21.590  -23.834 0.448   1.00 69.78  ? 167 TRP D NE1 1 
ATOM   10589 C  CE2 . TRP D 1 166 ? 22.949  -23.720 0.318   1.00 67.88  ? 167 TRP D CE2 1 
ATOM   10590 C  CE3 . TRP D 1 166 ? 24.802  -25.082 -0.427  1.00 70.90  ? 167 TRP D CE3 1 
ATOM   10591 C  CZ2 . TRP D 1 166 ? 23.792  -22.650 0.610   1.00 68.04  ? 167 TRP D CZ2 1 
ATOM   10592 C  CZ3 . TRP D 1 166 ? 25.635  -24.018 -0.136  1.00 69.48  ? 167 TRP D CZ3 1 
ATOM   10593 C  CH2 . TRP D 1 166 ? 25.127  -22.818 0.375   1.00 70.56  ? 167 TRP D CH2 1 
ATOM   10594 N  N   . ALA D 1 167 ? 22.309  -29.600 -2.952  1.00 73.65  ? 168 ALA D N   1 
ATOM   10595 C  CA  . ALA D 1 167 ? 22.496  -31.017 -3.263  1.00 76.97  ? 168 ALA D CA  1 
ATOM   10596 C  C   . ALA D 1 167 ? 23.684  -31.220 -4.202  1.00 79.33  ? 168 ALA D C   1 
ATOM   10597 O  O   . ALA D 1 167 ? 24.624  -31.970 -3.883  1.00 81.49  ? 168 ALA D O   1 
ATOM   10598 C  CB  . ALA D 1 167 ? 21.231  -31.601 -3.873  1.00 75.72  ? 168 ALA D CB  1 
ATOM   10599 N  N   . ARG D 1 168 ? 23.650  -30.531 -5.344  1.00 82.74  ? 169 ARG D N   1 
ATOM   10600 C  CA  . ARG D 1 168 ? 24.748  -30.609 -6.308  1.00 85.78  ? 169 ARG D CA  1 
ATOM   10601 C  C   . ARG D 1 168 ? 26.054  -30.197 -5.633  1.00 88.19  ? 169 ARG D C   1 
ATOM   10602 O  O   . ARG D 1 168 ? 27.026  -30.949 -5.680  1.00 91.98  ? 169 ARG D O   1 
ATOM   10603 C  CB  . ARG D 1 168 ? 24.438  -29.753 -7.560  1.00 88.18  ? 169 ARG D CB  1 
ATOM   10604 C  CG  . ARG D 1 168 ? 25.536  -28.840 -8.205  1.00 124.64 ? 169 ARG D CG  1 
ATOM   10605 C  CD  . ARG D 1 168 ? 26.919  -29.472 -8.429  1.00 126.20 ? 169 ARG D CD  1 
ATOM   10606 N  NE  . ARG D 1 168 ? 26.906  -30.644 -9.303  1.00 128.71 ? 169 ARG D NE  1 
ATOM   10607 C  CZ  . ARG D 1 168 ? 27.977  -31.390 -9.564  1.00 130.98 ? 169 ARG D CZ  1 
ATOM   10608 N  NH1 . ARG D 1 168 ? 29.150  -31.073 -9.036  1.00 130.36 ? 169 ARG D NH1 1 
ATOM   10609 N  NH2 . ARG D 1 168 ? 27.881  -32.447 -10.358 1.00 133.10 ? 169 ARG D NH2 1 
ATOM   10610 N  N   . LEU D 1 169 ? 26.079  -29.024 -5.003  1.00 85.28  ? 170 LEU D N   1 
ATOM   10611 C  CA  . LEU D 1 169 ? 27.322  -28.506 -4.432  1.00 85.63  ? 170 LEU D CA  1 
ATOM   10612 C  C   . LEU D 1 169 ? 27.994  -29.540 -3.528  1.00 85.32  ? 170 LEU D C   1 
ATOM   10613 O  O   . LEU D 1 169 ? 29.212  -29.775 -3.615  1.00 86.62  ? 170 LEU D O   1 
ATOM   10614 C  CB  . LEU D 1 169 ? 27.062  -27.217 -3.655  1.00 83.92  ? 170 LEU D CB  1 
ATOM   10615 C  CG  . LEU D 1 169 ? 28.322  -26.422 -3.310  1.00 83.62  ? 170 LEU D CG  1 
ATOM   10616 C  CD1 . LEU D 1 169 ? 29.039  -25.976 -4.577  1.00 83.25  ? 170 LEU D CD1 1 
ATOM   10617 C  CD2 . LEU D 1 169 ? 27.983  -25.230 -2.438  1.00 82.68  ? 170 LEU D CD2 1 
ATOM   10618 N  N   . LEU D 1 170 ? 27.183  -30.177 -2.687  1.00 80.75  ? 171 LEU D N   1 
ATOM   10619 C  CA  . LEU D 1 170 ? 27.663  -31.263 -1.844  1.00 77.50  ? 171 LEU D CA  1 
ATOM   10620 C  C   . LEU D 1 170 ? 28.209  -32.402 -2.698  1.00 76.66  ? 171 LEU D C   1 
ATOM   10621 O  O   . LEU D 1 170 ? 29.311  -32.913 -2.439  1.00 75.80  ? 171 LEU D O   1 
ATOM   10622 C  CB  . LEU D 1 170 ? 26.547  -31.773 -0.931  1.00 72.50  ? 171 LEU D CB  1 
ATOM   10623 C  CG  . LEU D 1 170 ? 26.946  -32.877 0.051   1.00 71.60  ? 171 LEU D CG  1 
ATOM   10624 C  CD1 . LEU D 1 170 ? 28.133  -32.443 0.899   1.00 69.15  ? 171 LEU D CD1 1 
ATOM   10625 C  CD2 . LEU D 1 170 ? 25.767  -33.262 0.931   1.00 68.96  ? 171 LEU D CD2 1 
ATOM   10626 N  N   . GLU D 1 171 ? 27.446  -32.784 -3.723  1.00 79.67  ? 172 GLU D N   1 
ATOM   10627 C  CA  . GLU D 1 171 ? 27.868  -33.862 -4.619  1.00 84.80  ? 172 GLU D CA  1 
ATOM   10628 C  C   . GLU D 1 171 ? 29.254  -33.613 -5.231  1.00 84.57  ? 172 GLU D C   1 
ATOM   10629 O  O   . GLU D 1 171 ? 30.043  -34.541 -5.352  1.00 85.28  ? 172 GLU D O   1 
ATOM   10630 C  CB  . GLU D 1 171 ? 26.826  -34.081 -5.723  1.00 92.52  ? 172 GLU D CB  1 
ATOM   10631 C  CG  . GLU D 1 171 ? 25.503  -34.650 -5.214  1.00 99.17  ? 172 GLU D CG  1 
ATOM   10632 C  CD  . GLU D 1 171 ? 24.445  -34.753 -6.296  1.00 105.77 ? 172 GLU D CD  1 
ATOM   10633 O  OE1 . GLU D 1 171 ? 24.632  -34.145 -7.370  1.00 108.20 ? 172 GLU D OE1 1 
ATOM   10634 O  OE2 . GLU D 1 171 ? 23.421  -35.435 -6.070  1.00 108.52 ? 172 GLU D OE2 1 
ATOM   10635 N  N   . ARG D 1 172 ? 29.548  -32.366 -5.594  1.00 82.98  ? 173 ARG D N   1 
ATOM   10636 C  CA  . ARG D 1 172 ? 30.873  -31.981 -6.086  1.00 79.86  ? 173 ARG D CA  1 
ATOM   10637 C  C   . ARG D 1 172 ? 31.932  -32.072 -5.012  1.00 78.29  ? 173 ARG D C   1 
ATOM   10638 O  O   . ARG D 1 172 ? 32.889  -32.868 -5.078  1.00 78.59  ? 173 ARG D O   1 
ATOM   10639 C  CB  . ARG D 1 172 ? 30.856  -30.542 -6.605  1.00 81.15  ? 173 ARG D CB  1 
ATOM   10640 N  N   . LEU D 1 173 ? 31.738  -31.212 -4.020  1.00 77.95  ? 174 LEU D N   1 
ATOM   10641 C  CA  . LEU D 1 173 ? 32.767  -30.913 -3.050  1.00 78.84  ? 174 LEU D CA  1 
ATOM   10642 C  C   . LEU D 1 173 ? 33.125  -32.159 -2.259  1.00 79.81  ? 174 LEU D C   1 
ATOM   10643 O  O   . LEU D 1 173 ? 34.209  -32.242 -1.686  1.00 82.91  ? 174 LEU D O   1 
ATOM   10644 C  CB  . LEU D 1 173 ? 32.309  -29.778 -2.135  1.00 75.45  ? 174 LEU D CB  1 
ATOM   10645 C  CG  . LEU D 1 173 ? 32.553  -28.333 -2.597  1.00 73.74  ? 174 LEU D CG  1 
ATOM   10646 C  CD1 . LEU D 1 173 ? 32.070  -28.077 -4.023  1.00 72.34  ? 174 LEU D CD1 1 
ATOM   10647 C  CD2 . LEU D 1 173 ? 31.893  -27.352 -1.636  1.00 70.29  ? 174 LEU D CD2 1 
ATOM   10648 N  N   . PHE D 1 174 ? 32.230  -33.144 -2.252  1.00 80.04  ? 175 PHE D N   1 
ATOM   10649 C  CA  . PHE D 1 174 ? 32.578  -34.416 -1.636  1.00 79.06  ? 175 PHE D CA  1 
ATOM   10650 C  C   . PHE D 1 174 ? 33.589  -35.189 -2.485  1.00 79.41  ? 175 PHE D C   1 
ATOM   10651 O  O   . PHE D 1 174 ? 34.544  -35.747 -1.946  1.00 81.25  ? 175 PHE D O   1 
ATOM   10652 C  CB  . PHE D 1 174 ? 31.343  -35.275 -1.386  1.00 77.09  ? 175 PHE D CB  1 
ATOM   10653 C  CG  . PHE D 1 174 ? 31.565  -36.344 -0.358  1.00 76.34  ? 175 PHE D CG  1 
ATOM   10654 C  CD1 . PHE D 1 174 ? 31.461  -36.052 0.992   1.00 74.25  ? 175 PHE D CD1 1 
ATOM   10655 C  CD2 . PHE D 1 174 ? 31.909  -37.630 -0.735  1.00 77.37  ? 175 PHE D CD2 1 
ATOM   10656 C  CE1 . PHE D 1 174 ? 31.677  -37.027 1.945   1.00 73.19  ? 175 PHE D CE1 1 
ATOM   10657 C  CE2 . PHE D 1 174 ? 32.125  -38.611 0.214   1.00 76.46  ? 175 PHE D CE2 1 
ATOM   10658 C  CZ  . PHE D 1 174 ? 32.008  -38.308 1.555   1.00 76.14  ? 175 PHE D CZ  1 
ATOM   10659 N  N   . LYS D 1 175 ? 33.383  -35.232 -3.802  1.00 78.10  ? 176 LYS D N   1 
ATOM   10660 C  CA  . LYS D 1 175 ? 34.367  -35.853 -4.690  1.00 78.08  ? 176 LYS D CA  1 
ATOM   10661 C  C   . LYS D 1 175 ? 35.696  -35.131 -4.572  1.00 77.15  ? 176 LYS D C   1 
ATOM   10662 O  O   . LYS D 1 175 ? 36.749  -35.757 -4.439  1.00 76.25  ? 176 LYS D O   1 
ATOM   10663 C  CB  . LYS D 1 175 ? 33.927  -35.830 -6.158  1.00 75.91  ? 176 LYS D CB  1 
ATOM   10664 C  CG  . LYS D 1 175 ? 32.449  -35.958 -6.425  1.00 76.74  ? 176 LYS D CG  1 
ATOM   10665 C  CD  . LYS D 1 175 ? 32.191  -35.905 -7.927  1.00 79.25  ? 176 LYS D CD  1 
ATOM   10666 C  CE  . LYS D 1 175 ? 30.711  -35.789 -8.252  1.00 79.66  ? 176 LYS D CE  1 
ATOM   10667 N  NZ  . LYS D 1 175 ? 30.483  -35.003 -9.499  1.00 81.08  ? 176 LYS D NZ  1 
ATOM   10668 N  N   . GLN D 1 176 ? 35.638  -33.804 -4.625  1.00 81.32  ? 177 GLN D N   1 
ATOM   10669 C  CA  . GLN D 1 176 ? 36.855  -33.001 -4.645  1.00 83.33  ? 177 GLN D CA  1 
ATOM   10670 C  C   . GLN D 1 176 ? 37.633  -33.083 -3.333  1.00 87.68  ? 177 GLN D C   1 
ATOM   10671 O  O   . GLN D 1 176 ? 38.864  -33.109 -3.339  1.00 87.89  ? 177 GLN D O   1 
ATOM   10672 C  CB  . GLN D 1 176 ? 36.519  -31.549 -4.976  1.00 80.50  ? 177 GLN D CB  1 
ATOM   10673 C  CG  . GLN D 1 176 ? 36.347  -31.307 -6.465  1.00 81.38  ? 177 GLN D CG  1 
ATOM   10674 C  CD  . GLN D 1 176 ? 35.781  -29.941 -6.772  1.00 80.03  ? 177 GLN D CD  1 
ATOM   10675 O  OE1 . GLN D 1 176 ? 36.321  -28.926 -6.341  1.00 79.62  ? 177 GLN D OE1 1 
ATOM   10676 N  NE2 . GLN D 1 176 ? 34.688  -29.907 -7.525  1.00 79.03  ? 177 GLN D NE2 1 
ATOM   10677 N  N   . LEU D 1 177 ? 36.923  -33.136 -2.211  1.00 86.32  ? 178 LEU D N   1 
ATOM   10678 C  CA  . LEU D 1 177 ? 37.585  -33.265 -0.916  1.00 85.82  ? 178 LEU D CA  1 
ATOM   10679 C  C   . LEU D 1 177 ? 38.138  -34.672 -0.703  1.00 86.28  ? 178 LEU D C   1 
ATOM   10680 O  O   . LEU D 1 177 ? 38.992  -34.883 0.157   1.00 87.95  ? 178 LEU D O   1 
ATOM   10681 C  CB  . LEU D 1 177 ? 36.628  -32.904 0.223   1.00 81.60  ? 178 LEU D CB  1 
ATOM   10682 C  CG  . LEU D 1 177 ? 36.396  -31.412 0.476   1.00 79.49  ? 178 LEU D CG  1 
ATOM   10683 C  CD1 . LEU D 1 177 ? 35.241  -31.202 1.445   1.00 77.22  ? 178 LEU D CD1 1 
ATOM   10684 C  CD2 . LEU D 1 177 ? 37.663  -30.756 1.002   1.00 78.26  ? 178 LEU D CD2 1 
ATOM   10685 N  N   . HIS D 1 178 ? 37.647  -35.632 -1.482  1.00 89.48  ? 179 HIS D N   1 
ATOM   10686 C  CA  . HIS D 1 178 ? 38.070  -37.024 -1.342  1.00 94.15  ? 179 HIS D CA  1 
ATOM   10687 C  C   . HIS D 1 178 ? 38.400  -37.653 -2.693  1.00 96.11  ? 179 HIS D C   1 
ATOM   10688 O  O   . HIS D 1 178 ? 37.572  -38.356 -3.272  1.00 96.09  ? 179 HIS D O   1 
ATOM   10689 C  CB  . HIS D 1 178 ? 36.985  -37.841 -0.638  1.00 99.82  ? 179 HIS D CB  1 
ATOM   10690 C  CG  . HIS D 1 178 ? 36.656  -37.349 0.737   1.00 103.65 ? 179 HIS D CG  1 
ATOM   10691 N  ND1 . HIS D 1 178 ? 37.543  -36.620 1.499   1.00 105.71 ? 179 HIS D ND1 1 
ATOM   10692 C  CD2 . HIS D 1 178 ? 35.531  -37.468 1.480   1.00 104.80 ? 179 HIS D CD2 1 
ATOM   10693 C  CE1 . HIS D 1 178 ? 36.981  -36.317 2.656   1.00 105.49 ? 179 HIS D CE1 1 
ATOM   10694 N  NE2 . HIS D 1 178 ? 35.760  -36.819 2.669   1.00 105.47 ? 179 HIS D NE2 1 
ATOM   10695 N  N   . PRO D 1 179 ? 39.616  -37.395 -3.199  1.00 96.72  ? 180 PRO D N   1 
ATOM   10696 C  CA  . PRO D 1 179 ? 40.081  -37.908 -4.493  1.00 100.00 ? 180 PRO D CA  1 
ATOM   10697 C  C   . PRO D 1 179 ? 40.113  -39.434 -4.558  1.00 105.35 ? 180 PRO D C   1 
ATOM   10698 O  O   . PRO D 1 179 ? 39.705  -40.014 -5.565  1.00 105.79 ? 180 PRO D O   1 
ATOM   10699 C  CB  . PRO D 1 179 ? 41.500  -37.337 -4.610  1.00 99.04  ? 180 PRO D CB  1 
ATOM   10700 C  CG  . PRO D 1 179 ? 41.528  -36.175 -3.676  1.00 96.88  ? 180 PRO D CG  1 
ATOM   10701 C  CD  . PRO D 1 179 ? 40.636  -36.561 -2.542  1.00 95.67  ? 180 PRO D CD  1 
ATOM   10702 N  N   . GLN D 1 180 ? 40.596  -40.064 -3.492  1.00 106.68 ? 181 GLN D N   1 
ATOM   10703 C  CA  . GLN D 1 180 ? 40.767  -41.514 -3.456  1.00 110.63 ? 181 GLN D CA  1 
ATOM   10704 C  C   . GLN D 1 180 ? 39.446  -42.257 -3.629  1.00 114.68 ? 181 GLN D C   1 
ATOM   10705 O  O   . GLN D 1 180 ? 39.362  -43.222 -4.389  1.00 119.02 ? 181 GLN D O   1 
ATOM   10706 C  CB  . GLN D 1 180 ? 41.431  -41.937 -2.145  1.00 109.16 ? 181 GLN D CB  1 
ATOM   10707 N  N   . LEU D 1 181 ? 38.419  -41.804 -2.920  1.00 118.62 ? 182 LEU D N   1 
ATOM   10708 C  CA  . LEU D 1 181 ? 37.117  -42.456 -2.960  1.00 118.83 ? 182 LEU D CA  1 
ATOM   10709 C  C   . LEU D 1 181 ? 36.455  -42.310 -4.330  1.00 117.32 ? 182 LEU D C   1 
ATOM   10710 O  O   . LEU D 1 181 ? 36.316  -41.203 -4.850  1.00 120.15 ? 182 LEU D O   1 
ATOM   10711 C  CB  . LEU D 1 181 ? 36.209  -41.888 -1.868  1.00 118.66 ? 182 LEU D CB  1 
ATOM   10712 N  N   . LEU D 1 182 ? 36.052  -43.439 -4.908  1.00 112.36 ? 183 LEU D N   1 
ATOM   10713 C  CA  . LEU D 1 182 ? 35.391  -43.449 -6.210  1.00 108.40 ? 183 LEU D CA  1 
ATOM   10714 C  C   . LEU D 1 182 ? 33.891  -43.659 -6.043  1.00 103.86 ? 183 LEU D C   1 
ATOM   10715 O  O   . LEU D 1 182 ? 33.445  -44.736 -5.646  1.00 105.51 ? 183 LEU D O   1 
ATOM   10716 C  CB  . LEU D 1 182 ? 35.984  -44.537 -7.107  1.00 109.92 ? 183 LEU D CB  1 
ATOM   10717 N  N   . LEU D 1 183 ? 33.116  -42.626 -6.359  1.00 103.41 ? 184 LEU D N   1 
ATOM   10718 C  CA  . LEU D 1 183 ? 31.690  -42.619 -6.053  1.00 103.44 ? 184 LEU D CA  1 
ATOM   10719 C  C   . LEU D 1 183 ? 30.800  -42.680 -7.288  1.00 106.14 ? 184 LEU D C   1 
ATOM   10720 O  O   . LEU D 1 183 ? 30.796  -41.757 -8.102  1.00 106.82 ? 184 LEU D O   1 
ATOM   10721 C  CB  . LEU D 1 183 ? 31.328  -41.369 -5.243  1.00 102.60 ? 184 LEU D CB  1 
ATOM   10722 C  CG  . LEU D 1 183 ? 31.598  -41.327 -3.736  1.00 101.03 ? 184 LEU D CG  1 
ATOM   10723 C  CD1 . LEU D 1 183 ? 33.071  -41.483 -3.412  1.00 100.22 ? 184 LEU D CD1 1 
ATOM   10724 C  CD2 . LEU D 1 183 ? 31.063  -40.032 -3.149  1.00 99.98  ? 184 LEU D CD2 1 
ATOM   10725 N  N   . PRO D 1 184 ? 30.036  -43.774 -7.430  1.00 106.77 ? 185 PRO D N   1 
ATOM   10726 C  CA  . PRO D 1 184 ? 28.956  -43.810 -8.419  1.00 108.75 ? 185 PRO D CA  1 
ATOM   10727 C  C   . PRO D 1 184 ? 27.774  -42.974 -7.936  1.00 108.80 ? 185 PRO D C   1 
ATOM   10728 O  O   . PRO D 1 184 ? 27.801  -42.502 -6.800  1.00 108.87 ? 185 PRO D O   1 
ATOM   10729 C  CB  . PRO D 1 184 ? 28.595  -45.295 -8.497  1.00 110.00 ? 185 PRO D CB  1 
ATOM   10730 C  CG  . PRO D 1 184 ? 28.994  -45.844 -7.170  1.00 109.23 ? 185 PRO D CG  1 
ATOM   10731 C  CD  . PRO D 1 184 ? 30.206  -45.066 -6.743  1.00 108.14 ? 185 PRO D CD  1 
ATOM   10732 N  N   . ASP D 1 185 ? 26.759  -42.796 -8.776  1.00 109.97 ? 186 ASP D N   1 
ATOM   10733 C  CA  . ASP D 1 185 ? 25.590  -42.007 -8.399  1.00 108.30 ? 186 ASP D CA  1 
ATOM   10734 C  C   . ASP D 1 185 ? 24.861  -42.613 -7.198  1.00 108.46 ? 186 ASP D C   1 
ATOM   10735 O  O   . ASP D 1 185 ? 24.238  -41.892 -6.405  1.00 107.49 ? 186 ASP D O   1 
ATOM   10736 C  CB  . ASP D 1 185 ? 24.630  -41.875 -9.584  1.00 110.98 ? 186 ASP D CB  1 
ATOM   10737 N  N   . ASP D 1 186 ? 24.956  -43.937 -7.070  1.00 106.28 ? 187 ASP D N   1 
ATOM   10738 C  CA  . ASP D 1 186 ? 24.297  -44.665 -5.987  1.00 104.58 ? 187 ASP D CA  1 
ATOM   10739 C  C   . ASP D 1 186 ? 24.726  -44.125 -4.627  1.00 99.88  ? 187 ASP D C   1 
ATOM   10740 O  O   . ASP D 1 186 ? 23.917  -44.007 -3.706  1.00 98.01  ? 187 ASP D O   1 
ATOM   10741 C  CB  . ASP D 1 186 ? 24.550  -46.192 -6.128  1.00 107.53 ? 187 ASP D CB  1 
ATOM   10742 C  CG  . ASP D 1 186 ? 25.923  -46.668 -5.598  1.00 108.90 ? 187 ASP D CG  1 
ATOM   10743 O  OD1 . ASP D 1 186 ? 26.667  -45.939 -4.914  1.00 108.49 ? 187 ASP D OD1 1 
ATOM   10744 O  OD2 . ASP D 1 186 ? 26.265  -47.834 -5.887  1.00 110.54 ? 187 ASP D OD2 1 
ATOM   10745 N  N   . TYR D 1 187 ? 26.003  -43.774 -4.532  1.00 99.35  ? 188 TYR D N   1 
ATOM   10746 C  CA  . TYR D 1 187 ? 26.594  -43.284 -3.297  1.00 98.40  ? 188 TYR D CA  1 
ATOM   10747 C  C   . TYR D 1 187 ? 26.301  -41.804 -3.117  1.00 99.70  ? 188 TYR D C   1 
ATOM   10748 O  O   . TYR D 1 187 ? 26.038  -41.337 -2.006  1.00 99.13  ? 188 TYR D O   1 
ATOM   10749 C  CB  . TYR D 1 187 ? 28.101  -43.526 -3.311  1.00 92.29  ? 188 TYR D CB  1 
ATOM   10750 C  CG  . TYR D 1 187 ? 28.702  -43.748 -1.948  1.00 87.50  ? 188 TYR D CG  1 
ATOM   10751 C  CD1 . TYR D 1 187 ? 29.291  -42.706 -1.248  1.00 85.80  ? 188 TYR D CD1 1 
ATOM   10752 C  CD2 . TYR D 1 187 ? 28.693  -45.007 -1.366  1.00 85.65  ? 188 TYR D CD2 1 
ATOM   10753 C  CE1 . TYR D 1 187 ? 29.846  -42.910 -0.000  1.00 83.34  ? 188 TYR D CE1 1 
ATOM   10754 C  CE2 . TYR D 1 187 ? 29.243  -45.222 -0.120  1.00 83.37  ? 188 TYR D CE2 1 
ATOM   10755 C  CZ  . TYR D 1 187 ? 29.819  -44.170 0.558   1.00 82.34  ? 188 TYR D CZ  1 
ATOM   10756 O  OH  . TYR D 1 187 ? 30.371  -44.378 1.800   1.00 82.79  ? 188 TYR D OH  1 
ATOM   10757 N  N   . LEU D 1 188 ? 26.360  -41.074 -4.227  1.00 103.59 ? 189 LEU D N   1 
ATOM   10758 C  CA  . LEU D 1 188 ? 26.102  -39.642 -4.234  1.00 104.55 ? 189 LEU D CA  1 
ATOM   10759 C  C   . LEU D 1 188 ? 24.723  -39.336 -3.679  1.00 107.74 ? 189 LEU D C   1 
ATOM   10760 O  O   . LEU D 1 188 ? 24.570  -38.482 -2.800  1.00 107.67 ? 189 LEU D O   1 
ATOM   10761 C  CB  . LEU D 1 188 ? 26.228  -39.080 -5.650  1.00 105.06 ? 189 LEU D CB  1 
ATOM   10762 C  CG  . LEU D 1 188 ? 27.561  -39.311 -6.360  1.00 106.83 ? 189 LEU D CG  1 
ATOM   10763 C  CD1 . LEU D 1 188 ? 27.504  -38.769 -7.778  1.00 107.98 ? 189 LEU D CD1 1 
ATOM   10764 C  CD2 . LEU D 1 188 ? 28.692  -38.669 -5.579  1.00 105.36 ? 189 LEU D CD2 1 
ATOM   10765 N  N   . ASP D 1 189 ? 23.717  -40.043 -4.184  1.00 109.97 ? 190 ASP D N   1 
ATOM   10766 C  CA  . ASP D 1 189 ? 22.350  -39.776 -3.753  1.00 108.60 ? 190 ASP D CA  1 
ATOM   10767 C  C   . ASP D 1 189 ? 22.116  -40.151 -2.288  1.00 101.43 ? 190 ASP D C   1 
ATOM   10768 O  O   . ASP D 1 189 ? 21.516  -39.378 -1.549  1.00 99.17  ? 190 ASP D O   1 
ATOM   10769 C  CB  . ASP D 1 189 ? 21.355  -40.491 -4.664  1.00 115.35 ? 190 ASP D CB  1 
ATOM   10770 C  CG  . ASP D 1 189 ? 21.425  -39.992 -6.095  1.00 119.93 ? 190 ASP D CG  1 
ATOM   10771 O  OD1 . ASP D 1 189 ? 22.388  -39.264 -6.417  1.00 121.94 ? 190 ASP D OD1 1 
ATOM   10772 O  OD2 . ASP D 1 189 ? 20.510  -40.299 -6.888  1.00 121.24 ? 190 ASP D OD2 1 
ATOM   10773 N  N   . CYS D 1 190 ? 22.612  -41.313 -1.867  1.00 96.96  ? 191 CYS D N   1 
ATOM   10774 C  CA  . CYS D 1 190 ? 22.544  -41.726 -0.461  1.00 92.64  ? 191 CYS D CA  1 
ATOM   10775 C  C   . CYS D 1 190 ? 23.164  -40.672 0.460   1.00 85.53  ? 191 CYS D C   1 
ATOM   10776 O  O   . CYS D 1 190 ? 22.599  -40.312 1.506   1.00 84.84  ? 191 CYS D O   1 
ATOM   10777 C  CB  . CYS D 1 190 ? 23.249  -43.070 -0.271  1.00 93.90  ? 191 CYS D CB  1 
ATOM   10778 S  SG  . CYS D 1 190 ? 23.485  -43.559 1.451   1.00 97.04  ? 191 CYS D SG  1 
ATOM   10779 N  N   . LEU D 1 191 ? 24.337  -40.194 0.054   1.00 84.41  ? 192 LEU D N   1 
ATOM   10780 C  CA  . LEU D 1 191 ? 24.999  -39.065 0.697   1.00 80.60  ? 192 LEU D CA  1 
ATOM   10781 C  C   . LEU D 1 191 ? 24.045  -37.877 0.795   1.00 72.96  ? 192 LEU D C   1 
ATOM   10782 O  O   . LEU D 1 191 ? 23.931  -37.233 1.845   1.00 69.44  ? 192 LEU D O   1 
ATOM   10783 C  CB  . LEU D 1 191 ? 26.260  -38.689 -0.088  1.00 82.04  ? 192 LEU D CB  1 
ATOM   10784 C  CG  . LEU D 1 191 ? 26.927  -37.327 0.117   1.00 81.79  ? 192 LEU D CG  1 
ATOM   10785 C  CD1 . LEU D 1 191 ? 27.395  -37.150 1.549   1.00 82.60  ? 192 LEU D CD1 1 
ATOM   10786 C  CD2 . LEU D 1 191 ? 28.088  -37.159 -0.856  1.00 81.81  ? 192 LEU D CD2 1 
ATOM   10787 N  N   . GLY D 1 192 ? 23.345  -37.612 -0.305  1.00 72.02  ? 193 GLY D N   1 
ATOM   10788 C  CA  . GLY D 1 192 ? 22.386  -36.525 -0.368  1.00 71.65  ? 193 GLY D CA  1 
ATOM   10789 C  C   . GLY D 1 192 ? 21.201  -36.677 0.570   1.00 73.35  ? 193 GLY D C   1 
ATOM   10790 O  O   . GLY D 1 192 ? 20.634  -35.678 1.015   1.00 75.98  ? 193 GLY D O   1 
ATOM   10791 N  N   . LYS D 1 193 ? 20.814  -37.917 0.864   1.00 76.15  ? 194 LYS D N   1 
ATOM   10792 C  CA  . LYS D 1 193 ? 19.716  -38.166 1.798   1.00 78.51  ? 194 LYS D CA  1 
ATOM   10793 C  C   . LYS D 1 193 ? 20.207  -38.179 3.242   1.00 73.02  ? 194 LYS D C   1 
ATOM   10794 O  O   . LYS D 1 193 ? 19.421  -38.012 4.175   1.00 73.98  ? 194 LYS D O   1 
ATOM   10795 C  CB  . LYS D 1 193 ? 19.002  -39.483 1.477   1.00 79.79  ? 194 LYS D CB  1 
ATOM   10796 C  CG  . LYS D 1 193 ? 19.035  -39.863 0.012   1.00 79.77  ? 194 LYS D CG  1 
ATOM   10797 C  CD  . LYS D 1 193 ? 17.684  -40.343 -0.484  1.00 80.00  ? 194 LYS D CD  1 
ATOM   10798 C  CE  . LYS D 1 193 ? 17.841  -41.383 -1.578  1.00 79.00  ? 194 LYS D CE  1 
ATOM   10799 N  NZ  . LYS D 1 193 ? 18.257  -42.697 -1.018  1.00 76.18  ? 194 LYS D NZ  1 
ATOM   10800 N  N   . GLN D 1 194 ? 21.508  -38.376 3.422   1.00 77.01  ? 195 GLN D N   1 
ATOM   10801 C  CA  . GLN D 1 194 ? 22.111  -38.248 4.748   1.00 79.74  ? 195 GLN D CA  1 
ATOM   10802 C  C   . GLN D 1 194 ? 22.273  -36.768 5.119   1.00 78.12  ? 195 GLN D C   1 
ATOM   10803 O  O   . GLN D 1 194 ? 22.150  -36.373 6.300   1.00 79.32  ? 195 GLN D O   1 
ATOM   10804 C  CB  . GLN D 1 194 ? 23.465  -38.957 4.786   1.00 84.17  ? 195 GLN D CB  1 
ATOM   10805 C  CG  . GLN D 1 194 ? 23.685  -39.791 6.031   1.00 90.20  ? 195 GLN D CG  1 
ATOM   10806 C  CD  . GLN D 1 194 ? 24.798  -40.803 5.865   1.00 96.26  ? 195 GLN D CD  1 
ATOM   10807 O  OE1 . GLN D 1 194 ? 25.850  -40.684 6.487   1.00 99.35  ? 195 GLN D OE1 1 
ATOM   10808 N  NE2 . GLN D 1 194 ? 24.575  -41.801 5.016   1.00 97.18  ? 195 GLN D NE2 1 
ATOM   10809 N  N   . ALA D 1 195 ? 22.549  -35.968 4.087   1.00 75.62  ? 196 ALA D N   1 
ATOM   10810 C  CA  . ALA D 1 195 ? 22.740  -34.520 4.203   1.00 76.79  ? 196 ALA D CA  1 
ATOM   10811 C  C   . ALA D 1 195 ? 21.764  -33.862 5.174   1.00 76.34  ? 196 ALA D C   1 
ATOM   10812 O  O   . ALA D 1 195 ? 22.179  -33.155 6.092   1.00 74.18  ? 196 ALA D O   1 
ATOM   10813 C  CB  . ALA D 1 195 ? 22.623  -33.871 2.831   1.00 76.45  ? 196 ALA D CB  1 
ATOM   10814 N  N   . GLU D 1 196 ? 20.472  -34.096 4.967   1.00 79.90  ? 197 GLU D N   1 
ATOM   10815 C  CA  . GLU D 1 196 ? 19.459  -33.636 5.908   1.00 86.18  ? 197 GLU D CA  1 
ATOM   10816 C  C   . GLU D 1 196 ? 19.714  -34.275 7.267   1.00 95.83  ? 197 GLU D C   1 
ATOM   10817 O  O   . GLU D 1 196 ? 19.775  -35.499 7.382   1.00 97.89  ? 197 GLU D O   1 
ATOM   10818 C  CB  . GLU D 1 196 ? 18.052  -33.970 5.411   1.00 84.57  ? 197 GLU D CB  1 
ATOM   10819 N  N   . ALA D 1 197 ? 19.882  -33.423 8.275   1.00 105.89 ? 198 ALA D N   1 
ATOM   10820 C  CA  . ALA D 1 197 ? 20.234  -33.810 9.642   1.00 106.93 ? 198 ALA D CA  1 
ATOM   10821 C  C   . ALA D 1 197 ? 21.676  -34.314 9.781   1.00 107.70 ? 198 ALA D C   1 
ATOM   10822 O  O   . ALA D 1 197 ? 22.155  -34.458 10.907  1.00 113.15 ? 198 ALA D O   1 
ATOM   10823 C  CB  . ALA D 1 197 ? 19.253  -34.850 10.190  1.00 110.94 ? 198 ALA D CB  1 
ATOM   10824 N  N   . LEU D 1 198 ? 22.385  -34.580 8.681   1.00 97.94  ? 199 LEU D N   1 
ATOM   10825 C  CA  . LEU D 1 198 ? 23.839  -34.627 8.837   1.00 85.77  ? 199 LEU D CA  1 
ATOM   10826 C  C   . LEU D 1 198 ? 24.374  -33.196 8.876   1.00 74.56  ? 199 LEU D C   1 
ATOM   10827 O  O   . LEU D 1 198 ? 25.352  -32.908 9.568   1.00 72.56  ? 199 LEU D O   1 
ATOM   10828 C  CB  . LEU D 1 198 ? 24.518  -35.421 7.725   1.00 78.22  ? 199 LEU D CB  1 
ATOM   10829 C  CG  . LEU D 1 198 ? 25.568  -36.410 8.233   1.00 74.48  ? 199 LEU D CG  1 
ATOM   10830 C  CD1 . LEU D 1 198 ? 24.955  -37.333 9.273   1.00 73.25  ? 199 LEU D CD1 1 
ATOM   10831 C  CD2 . LEU D 1 198 ? 26.151  -37.213 7.085   1.00 73.67  ? 199 LEU D CD2 1 
ATOM   10832 N  N   . ARG D 1 199 ? 23.708  -32.308 8.138   1.00 72.81  ? 200 ARG D N   1 
ATOM   10833 C  CA  . ARG D 1 199 ? 24.080  -30.893 8.044   1.00 73.22  ? 200 ARG D CA  1 
ATOM   10834 C  C   . ARG D 1 199 ? 25.541  -30.667 7.652   1.00 65.30  ? 200 ARG D C   1 
ATOM   10835 O  O   . ARG D 1 199 ? 26.322  -30.154 8.453   1.00 64.71  ? 200 ARG D O   1 
ATOM   10836 C  CB  . ARG D 1 199 ? 23.803  -30.176 9.369   1.00 75.97  ? 200 ARG D CB  1 
ATOM   10837 C  CG  . ARG D 1 199 ? 22.429  -29.537 9.474   1.00 80.72  ? 200 ARG D CG  1 
ATOM   10838 C  CD  . ARG D 1 199 ? 21.476  -30.393 10.290  1.00 85.53  ? 200 ARG D CD  1 
ATOM   10839 N  NE  . ARG D 1 199 ? 20.494  -29.579 11.001  1.00 88.02  ? 200 ARG D NE  1 
ATOM   10840 C  CZ  . ARG D 1 199 ? 19.569  -30.068 11.820  1.00 89.86  ? 200 ARG D CZ  1 
ATOM   10841 N  NH1 . ARG D 1 199 ? 19.496  -31.374 12.035  1.00 90.45  ? 200 ARG D NH1 1 
ATOM   10842 N  NH2 . ARG D 1 199 ? 18.718  -29.251 12.426  1.00 89.96  ? 200 ARG D NH2 1 
ATOM   10843 N  N   . PRO D 1 200 ? 25.914  -31.042 6.417   1.00 63.79  ? 201 PRO D N   1 
ATOM   10844 C  CA  . PRO D 1 200 ? 27.299  -30.865 5.963   1.00 60.06  ? 201 PRO D CA  1 
ATOM   10845 C  C   . PRO D 1 200 ? 27.721  -29.398 5.915   1.00 59.89  ? 201 PRO D C   1 
ATOM   10846 O  O   . PRO D 1 200 ? 28.834  -29.063 6.322   1.00 58.46  ? 201 PRO D O   1 
ATOM   10847 C  CB  . PRO D 1 200 ? 27.292  -31.471 4.554   1.00 60.47  ? 201 PRO D CB  1 
ATOM   10848 C  CG  . PRO D 1 200 ? 26.076  -32.340 4.508   1.00 61.52  ? 201 PRO D CG  1 
ATOM   10849 C  CD  . PRO D 1 200 ? 25.073  -31.655 5.375   1.00 60.80  ? 201 PRO D CD  1 
ATOM   10850 N  N   . PHE D 1 201 ? 26.833  -28.538 5.427   1.00 56.33  ? 202 PHE D N   1 
ATOM   10851 C  CA  . PHE D 1 201 ? 27.134  -27.118 5.291   1.00 59.51  ? 202 PHE D CA  1 
ATOM   10852 C  C   . PHE D 1 201 ? 26.750  -26.343 6.546   1.00 64.79  ? 202 PHE D C   1 
ATOM   10853 O  O   . PHE D 1 201 ? 26.890  -25.121 6.601   1.00 60.88  ? 202 PHE D O   1 
ATOM   10854 C  CB  . PHE D 1 201 ? 26.414  -26.532 4.077   1.00 59.35  ? 202 PHE D CB  1 
ATOM   10855 C  CG  . PHE D 1 201 ? 26.750  -27.217 2.785   1.00 51.61  ? 202 PHE D CG  1 
ATOM   10856 C  CD1 . PHE D 1 201 ? 27.996  -27.056 2.203   1.00 51.96  ? 202 PHE D CD1 1 
ATOM   10857 C  CD2 . PHE D 1 201 ? 25.817  -28.017 2.149   1.00 56.98  ? 202 PHE D CD2 1 
ATOM   10858 C  CE1 . PHE D 1 201 ? 28.307  -27.685 1.012   1.00 55.89  ? 202 PHE D CE1 1 
ATOM   10859 C  CE2 . PHE D 1 201 ? 26.121  -28.648 0.958   1.00 57.66  ? 202 PHE D CE2 1 
ATOM   10860 C  CZ  . PHE D 1 201 ? 27.368  -28.481 0.389   1.00 55.74  ? 202 PHE D CZ  1 
ATOM   10861 N  N   . GLY D 1 202 ? 26.267  -27.062 7.552   1.00 65.82  ? 203 GLY D N   1 
ATOM   10862 C  CA  . GLY D 1 202 ? 25.884  -26.452 8.811   1.00 69.63  ? 203 GLY D CA  1 
ATOM   10863 C  C   . GLY D 1 202 ? 24.650  -25.573 8.732   1.00 69.70  ? 203 GLY D C   1 
ATOM   10864 O  O   . GLY D 1 202 ? 23.608  -25.990 8.226   1.00 68.12  ? 203 GLY D O   1 
ATOM   10865 N  N   . GLU D 1 203 ? 24.775  -24.348 9.232   1.00 75.70  ? 204 GLU D N   1 
ATOM   10866 C  CA  . GLU D 1 203 ? 23.630  -23.460 9.405   1.00 80.18  ? 204 GLU D CA  1 
ATOM   10867 C  C   . GLU D 1 203 ? 23.401  -22.524 8.221   1.00 80.24  ? 204 GLU D C   1 
ATOM   10868 O  O   . GLU D 1 203 ? 22.327  -21.938 8.089   1.00 82.59  ? 204 GLU D O   1 
ATOM   10869 C  CB  . GLU D 1 203 ? 23.806  -22.634 10.679  1.00 86.94  ? 204 GLU D CB  1 
ATOM   10870 C  CG  . GLU D 1 203 ? 22.612  -22.664 11.613  1.00 94.21  ? 204 GLU D CG  1 
ATOM   10871 C  CD  . GLU D 1 203 ? 22.890  -21.961 12.926  1.00 99.51  ? 204 GLU D CD  1 
ATOM   10872 O  OE1 . GLU D 1 203 ? 23.581  -20.921 12.909  1.00 101.90 ? 204 GLU D OE1 1 
ATOM   10873 O  OE2 . GLU D 1 203 ? 22.421  -22.450 13.975  1.00 101.76 ? 204 GLU D OE2 1 
ATOM   10874 N  N   . ALA D 1 204 ? 24.413  -22.385 7.371   1.00 77.16  ? 205 ALA D N   1 
ATOM   10875 C  CA  . ALA D 1 204 ? 24.353  -21.459 6.241   1.00 71.76  ? 205 ALA D CA  1 
ATOM   10876 C  C   . ALA D 1 204 ? 23.149  -21.662 5.301   1.00 68.92  ? 205 ALA D C   1 
ATOM   10877 O  O   . ALA D 1 204 ? 22.479  -20.685 4.964   1.00 72.43  ? 205 ALA D O   1 
ATOM   10878 C  CB  . ALA D 1 204 ? 25.659  -21.525 5.445   1.00 69.61  ? 205 ALA D CB  1 
ATOM   10879 N  N   . PRO D 1 205 ? 22.862  -22.914 4.876   1.00 69.49  ? 206 PRO D N   1 
ATOM   10880 C  CA  . PRO D 1 205 ? 21.745  -23.077 3.933   1.00 65.58  ? 206 PRO D CA  1 
ATOM   10881 C  C   . PRO D 1 205 ? 20.392  -22.603 4.467   1.00 64.09  ? 206 PRO D C   1 
ATOM   10882 O  O   . PRO D 1 205 ? 19.640  -21.965 3.730   1.00 63.36  ? 206 PRO D O   1 
ATOM   10883 C  CB  . PRO D 1 205 ? 21.714  -24.590 3.688   1.00 67.96  ? 206 PRO D CB  1 
ATOM   10884 C  CG  . PRO D 1 205 ? 23.092  -25.044 3.970   1.00 68.05  ? 206 PRO D CG  1 
ATOM   10885 C  CD  . PRO D 1 205 ? 23.548  -24.199 5.116   1.00 68.18  ? 206 PRO D CD  1 
ATOM   10886 N  N   . ARG D 1 206 ? 20.091  -22.910 5.725   1.00 66.78  ? 207 ARG D N   1 
ATOM   10887 C  CA  . ARG D 1 206 ? 18.798  -22.562 6.307   1.00 70.76  ? 207 ARG D CA  1 
ATOM   10888 C  C   . ARG D 1 206 ? 18.656  -21.053 6.499   1.00 68.16  ? 207 ARG D C   1 
ATOM   10889 O  O   . ARG D 1 206 ? 17.659  -20.453 6.078   1.00 70.41  ? 207 ARG D O   1 
ATOM   10890 C  CB  . ARG D 1 206 ? 18.603  -23.284 7.643   1.00 75.98  ? 207 ARG D CB  1 
ATOM   10891 C  CG  . ARG D 1 206 ? 17.681  -22.559 8.612   1.00 80.00  ? 207 ARG D CG  1 
ATOM   10892 C  CD  . ARG D 1 206 ? 17.743  -23.167 10.001  1.00 84.72  ? 207 ARG D CD  1 
ATOM   10893 N  NE  . ARG D 1 206 ? 16.451  -23.111 10.678  1.00 87.18  ? 207 ARG D NE  1 
ATOM   10894 C  CZ  . ARG D 1 206 ? 16.299  -22.831 11.969  1.00 90.08  ? 207 ARG D CZ  1 
ATOM   10895 N  NH1 . ARG D 1 206 ? 17.360  -22.582 12.724  1.00 90.52  ? 207 ARG D NH1 1 
ATOM   10896 N  NH2 . ARG D 1 206 ? 15.086  -22.801 12.505  1.00 90.38  ? 207 ARG D NH2 1 
ATOM   10897 N  N   . GLU D 1 207 ? 19.656  -20.450 7.136   1.00 69.01  ? 208 GLU D N   1 
ATOM   10898 C  CA  . GLU D 1 207 ? 19.671  -19.010 7.368   1.00 69.93  ? 208 GLU D CA  1 
ATOM   10899 C  C   . GLU D 1 207 ? 19.565  -18.262 6.045   1.00 66.06  ? 208 GLU D C   1 
ATOM   10900 O  O   . GLU D 1 207 ? 18.793  -17.302 5.917   1.00 66.37  ? 208 GLU D O   1 
ATOM   10901 C  CB  . GLU D 1 207 ? 20.943  -18.593 8.114   1.00 72.90  ? 208 GLU D CB  1 
ATOM   10902 C  CG  . GLU D 1 207 ? 21.065  -19.151 9.530   1.00 79.50  ? 208 GLU D CG  1 
ATOM   10903 C  CD  . GLU D 1 207 ? 20.170  -18.441 10.534  1.00 84.41  ? 208 GLU D CD  1 
ATOM   10904 O  OE1 . GLU D 1 207 ? 19.448  -17.500 10.141  1.00 84.04  ? 208 GLU D OE1 1 
ATOM   10905 O  OE2 . GLU D 1 207 ? 20.193  -18.824 11.723  1.00 84.76  ? 208 GLU D OE2 1 
ATOM   10906 N  N   . LEU D 1 208 ? 20.333  -18.719 5.059   1.00 60.74  ? 209 LEU D N   1 
ATOM   10907 C  CA  . LEU D 1 208 ? 20.282  -18.130 3.730   1.00 60.48  ? 209 LEU D CA  1 
ATOM   10908 C  C   . LEU D 1 208 ? 18.891  -18.277 3.131   1.00 61.58  ? 209 LEU D C   1 
ATOM   10909 O  O   . LEU D 1 208 ? 18.387  -17.353 2.511   1.00 63.33  ? 209 LEU D O   1 
ATOM   10910 C  CB  . LEU D 1 208 ? 21.319  -18.765 2.802   1.00 54.63  ? 209 LEU D CB  1 
ATOM   10911 C  CG  . LEU D 1 208 ? 21.279  -18.253 1.360   1.00 54.16  ? 209 LEU D CG  1 
ATOM   10912 C  CD1 . LEU D 1 208 ? 21.588  -16.763 1.315   1.00 49.47  ? 209 LEU D CD1 1 
ATOM   10913 C  CD2 . LEU D 1 208 ? 22.236  -19.031 0.474   1.00 45.95  ? 209 LEU D CD2 1 
ATOM   10914 N  N   . ARG D 1 209 ? 18.272  -19.437 3.324   1.00 62.36  ? 210 ARG D N   1 
ATOM   10915 C  CA  . ARG D 1 209 ? 16.932  -19.679 2.798   1.00 59.90  ? 210 ARG D CA  1 
ATOM   10916 C  C   . ARG D 1 209 ? 15.933  -18.673 3.363   1.00 63.31  ? 210 ARG D C   1 
ATOM   10917 O  O   . ARG D 1 209 ? 15.287  -17.931 2.613   1.00 65.91  ? 210 ARG D O   1 
ATOM   10918 C  CB  . ARG D 1 209 ? 16.480  -21.107 3.112   1.00 60.90  ? 210 ARG D CB  1 
ATOM   10919 N  N   . LEU D 1 210 ? 15.830  -18.646 4.689   1.00 62.82  ? 211 LEU D N   1 
ATOM   10920 C  CA  . LEU D 1 210 ? 14.930  -17.726 5.382   1.00 65.22  ? 211 LEU D CA  1 
ATOM   10921 C  C   . LEU D 1 210 ? 15.165  -16.270 4.976   1.00 61.94  ? 211 LEU D C   1 
ATOM   10922 O  O   . LEU D 1 210 ? 14.259  -15.590 4.461   1.00 63.88  ? 211 LEU D O   1 
ATOM   10923 C  CB  . LEU D 1 210 ? 15.097  -17.869 6.897   1.00 68.17  ? 211 LEU D CB  1 
ATOM   10924 C  CG  . LEU D 1 210 ? 14.663  -19.192 7.532   1.00 70.82  ? 211 LEU D CG  1 
ATOM   10925 C  CD1 . LEU D 1 210 ? 15.012  -19.215 9.014   1.00 73.25  ? 211 LEU D CD1 1 
ATOM   10926 C  CD2 . LEU D 1 210 ? 13.175  -19.423 7.330   1.00 71.11  ? 211 LEU D CD2 1 
ATOM   10927 N  N   . ARG D 1 211 ? 16.389  -15.801 5.199   1.00 59.27  ? 212 ARG D N   1 
ATOM   10928 C  CA  . ARG D 1 211 ? 16.712  -14.397 4.976   1.00 56.99  ? 212 ARG D CA  1 
ATOM   10929 C  C   . ARG D 1 211 ? 16.558  -13.977 3.514   1.00 52.34  ? 212 ARG D C   1 
ATOM   10930 O  O   . ARG D 1 211 ? 16.107  -12.864 3.232   1.00 53.89  ? 212 ARG D O   1 
ATOM   10931 C  CB  . ARG D 1 211 ? 18.127  -14.098 5.472   1.00 62.57  ? 212 ARG D CB  1 
ATOM   10932 C  CG  . ARG D 1 211 ? 18.168  -13.734 6.948   1.00 70.11  ? 212 ARG D CG  1 
ATOM   10933 C  CD  . ARG D 1 211 ? 19.536  -13.952 7.568   1.00 77.85  ? 212 ARG D CD  1 
ATOM   10934 N  NE  . ARG D 1 211 ? 19.666  -13.216 8.823   1.00 84.85  ? 212 ARG D NE  1 
ATOM   10935 C  CZ  . ARG D 1 211 ? 20.733  -13.265 9.615   1.00 90.47  ? 212 ARG D CZ  1 
ATOM   10936 N  NH1 . ARG D 1 211 ? 21.769  -14.025 9.289   1.00 92.30  ? 212 ARG D NH1 1 
ATOM   10937 N  NH2 . ARG D 1 211 ? 20.759  -12.559 10.737  1.00 91.94  ? 212 ARG D NH2 1 
ATOM   10938 N  N   . ALA D 1 212 ? 16.913  -14.863 2.587   1.00 51.65  ? 213 ALA D N   1 
ATOM   10939 C  CA  . ALA D 1 212 ? 16.735  -14.566 1.169   1.00 54.27  ? 213 ALA D CA  1 
ATOM   10940 C  C   . ALA D 1 212 ? 15.257  -14.485 0.826   1.00 54.54  ? 213 ALA D C   1 
ATOM   10941 O  O   . ALA D 1 212 ? 14.843  -13.575 0.108   1.00 58.04  ? 213 ALA D O   1 
ATOM   10942 C  CB  . ALA D 1 212 ? 17.419  -15.600 0.298   1.00 43.16  ? 213 ALA D CB  1 
ATOM   10943 N  N   . THR D 1 213 ? 14.466  -15.432 1.331   1.00 57.04  ? 214 THR D N   1 
ATOM   10944 C  CA  . THR D 1 213 ? 13.022  -15.378 1.114   1.00 56.64  ? 214 THR D CA  1 
ATOM   10945 C  C   . THR D 1 213 ? 12.478  -14.029 1.563   1.00 51.00  ? 214 THR D C   1 
ATOM   10946 O  O   . THR D 1 213 ? 11.886  -13.295 0.765   1.00 56.90  ? 214 THR D O   1 
ATOM   10947 C  CB  . THR D 1 213 ? 12.262  -16.496 1.864   1.00 60.01  ? 214 THR D CB  1 
ATOM   10948 O  OG1 . THR D 1 213 ? 12.729  -16.580 3.215   1.00 65.99  ? 214 THR D OG1 1 
ATOM   10949 C  CG2 . THR D 1 213 ? 12.455  -17.837 1.181   1.00 56.76  ? 214 THR D CG2 1 
ATOM   10950 N  N   . ARG D 1 214 ? 12.715  -13.691 2.828   1.00 49.60  ? 215 ARG D N   1 
ATOM   10951 C  CA  . ARG D 1 214 ? 12.172  -12.454 3.392   1.00 54.30  ? 215 ARG D CA  1 
ATOM   10952 C  C   . ARG D 1 214 ? 12.640  -11.198 2.645   1.00 52.60  ? 215 ARG D C   1 
ATOM   10953 O  O   . ARG D 1 214 ? 11.819  -10.379 2.216   1.00 48.34  ? 215 ARG D O   1 
ATOM   10954 C  CB  . ARG D 1 214 ? 12.537  -12.344 4.874   1.00 61.62  ? 215 ARG D CB  1 
ATOM   10955 C  CG  . ARG D 1 214 ? 11.632  -11.410 5.664   1.00 67.91  ? 215 ARG D CG  1 
ATOM   10956 C  CD  . ARG D 1 214 ? 12.423  -10.553 6.638   1.00 69.13  ? 215 ARG D CD  1 
ATOM   10957 N  N   . ALA D 1 215 ? 13.953  -11.054 2.482   1.00 50.77  ? 216 ALA D N   1 
ATOM   10958 C  CA  . ALA D 1 215 ? 14.521  -9.868  1.840   1.00 48.20  ? 216 ALA D CA  1 
ATOM   10959 C  C   . ALA D 1 215 ? 14.067  -9.714  0.386   1.00 44.07  ? 216 ALA D C   1 
ATOM   10960 O  O   . ALA D 1 215 ? 13.553  -8.656  -0.009  1.00 47.35  ? 216 ALA D O   1 
ATOM   10961 C  CB  . ALA D 1 215 ? 16.039  -9.910  1.912   1.00 40.66  ? 216 ALA D CB  1 
ATOM   10962 N  N   . PHE D 1 216 ? 14.259  -10.769 -0.404  1.00 45.43  ? 217 PHE D N   1 
ATOM   10963 C  CA  . PHE D 1 216 ? 13.869  -10.751 -1.811  1.00 45.47  ? 217 PHE D CA  1 
ATOM   10964 C  C   . PHE D 1 216 ? 12.381  -10.461 -1.971  1.00 47.90  ? 217 PHE D C   1 
ATOM   10965 O  O   . PHE D 1 216 ? 11.991  -9.656  -2.822  1.00 48.27  ? 217 PHE D O   1 
ATOM   10966 C  CB  . PHE D 1 216 ? 14.215  -12.078 -2.493  1.00 49.01  ? 217 PHE D CB  1 
ATOM   10967 C  CG  . PHE D 1 216 ? 15.618  -12.141 -3.029  1.00 51.82  ? 217 PHE D CG  1 
ATOM   10968 C  CD1 . PHE D 1 216 ? 15.893  -11.751 -4.329  1.00 50.30  ? 217 PHE D CD1 1 
ATOM   10969 C  CD2 . PHE D 1 216 ? 16.662  -12.594 -2.237  1.00 53.04  ? 217 PHE D CD2 1 
ATOM   10970 C  CE1 . PHE D 1 216 ? 17.181  -11.808 -4.830  1.00 49.61  ? 217 PHE D CE1 1 
ATOM   10971 C  CE2 . PHE D 1 216 ? 17.953  -12.654 -2.733  1.00 53.08  ? 217 PHE D CE2 1 
ATOM   10972 C  CZ  . PHE D 1 216 ? 18.212  -12.260 -4.031  1.00 51.43  ? 217 PHE D CZ  1 
ATOM   10973 N  N   . VAL D 1 217 ? 11.555  -11.108 -1.152  1.00 48.47  ? 218 VAL D N   1 
ATOM   10974 C  CA  . VAL D 1 217 ? 10.113  -10.891 -1.224  1.00 46.79  ? 218 VAL D CA  1 
ATOM   10975 C  C   . VAL D 1 217 ? 9.775   -9.443  -0.865  1.00 49.93  ? 218 VAL D C   1 
ATOM   10976 O  O   . VAL D 1 217 ? 8.881   -8.846  -1.465  1.00 49.20  ? 218 VAL D O   1 
ATOM   10977 C  CB  . VAL D 1 217 ? 9.339   -11.878 -0.307  1.00 53.12  ? 218 VAL D CB  1 
ATOM   10978 C  CG1 . VAL D 1 217 ? 8.333   -11.155 0.585   1.00 52.17  ? 218 VAL D CG1 1 
ATOM   10979 C  CG2 . VAL D 1 217 ? 8.656   -12.954 -1.141  1.00 55.07  ? 218 VAL D CG2 1 
ATOM   10980 N  N   . ALA D 1 218 ? 10.507  -8.873  0.090   1.00 47.22  ? 219 ALA D N   1 
ATOM   10981 C  CA  . ALA D 1 218 ? 10.281  -7.484  0.484   1.00 47.05  ? 219 ALA D CA  1 
ATOM   10982 C  C   . ALA D 1 218 ? 10.589  -6.523  -0.666  1.00 47.74  ? 219 ALA D C   1 
ATOM   10983 O  O   . ALA D 1 218 ? 9.749   -5.690  -1.045  1.00 38.27  ? 219 ALA D O   1 
ATOM   10984 C  CB  . ALA D 1 218 ? 11.119  -7.137  1.705   1.00 38.92  ? 219 ALA D CB  1 
ATOM   10985 N  N   . ALA D 1 219 ? 11.792  -6.649  -1.221  1.00 38.88  ? 220 ALA D N   1 
ATOM   10986 C  CA  . ALA D 1 219 ? 12.211  -5.801  -2.337  1.00 46.48  ? 220 ALA D CA  1 
ATOM   10987 C  C   . ALA D 1 219 ? 11.250  -5.916  -3.522  1.00 45.08  ? 220 ALA D C   1 
ATOM   10988 O  O   . ALA D 1 219 ? 10.771  -4.903  -4.065  1.00 38.58  ? 220 ALA D O   1 
ATOM   10989 C  CB  . ALA D 1 219 ? 13.624  -6.162  -2.766  1.00 39.35  ? 220 ALA D CB  1 
ATOM   10990 N  N   . ARG D 1 220 ? 10.966  -7.158  -3.908  1.00 39.25  ? 221 ARG D N   1 
ATOM   10991 C  CA  . ARG D 1 220 ? 10.078  -7.428  -5.030  1.00 45.92  ? 221 ARG D CA  1 
ATOM   10992 C  C   . ARG D 1 220 ? 8.693   -6.840  -4.792  1.00 42.69  ? 221 ARG D C   1 
ATOM   10993 O  O   . ARG D 1 220 ? 8.089   -6.282  -5.703  1.00 38.97  ? 221 ARG D O   1 
ATOM   10994 C  CB  . ARG D 1 220 ? 9.967   -8.932  -5.287  1.00 40.11  ? 221 ARG D CB  1 
ATOM   10995 C  CG  . ARG D 1 220 ? 9.060   -9.283  -6.454  1.00 48.92  ? 221 ARG D CG  1 
ATOM   10996 C  CD  . ARG D 1 220 ? 8.979   -10.781 -6.672  1.00 50.33  ? 221 ARG D CD  1 
ATOM   10997 N  NE  . ARG D 1 220 ? 8.301   -11.465 -5.575  1.00 54.44  ? 221 ARG D NE  1 
ATOM   10998 C  CZ  . ARG D 1 220 ? 8.377   -12.773 -5.353  1.00 56.61  ? 221 ARG D CZ  1 
ATOM   10999 N  NH1 . ARG D 1 220 ? 9.103   -13.541 -6.153  1.00 58.17  ? 221 ARG D NH1 1 
ATOM   11000 N  NH2 . ARG D 1 220 ? 7.727   -13.314 -4.332  1.00 55.57  ? 221 ARG D NH2 1 
ATOM   11001 N  N   . SER D 1 221 ? 8.199   -6.960  -3.565  1.00 38.78  ? 222 SER D N   1 
ATOM   11002 C  CA  . SER D 1 221 ? 6.892   -6.412  -3.225  1.00 41.78  ? 222 SER D CA  1 
ATOM   11003 C  C   . SER D 1 221 ? 6.882   -4.890  -3.318  1.00 42.19  ? 222 SER D C   1 
ATOM   11004 O  O   . SER D 1 221 ? 5.907   -4.303  -3.787  1.00 40.26  ? 222 SER D O   1 
ATOM   11005 C  CB  . SER D 1 221 ? 6.469   -6.857  -1.826  1.00 42.61  ? 222 SER D CB  1 
ATOM   11006 O  OG  . SER D 1 221 ? 6.199   -8.247  -1.803  1.00 49.37  ? 222 SER D OG  1 
ATOM   11007 N  N   . PHE D 1 222 ? 7.962   -4.251  -2.876  1.00 42.35  ? 223 PHE D N   1 
ATOM   11008 C  CA  . PHE D 1 222 ? 8.054   -2.794  -2.974  1.00 37.41  ? 223 PHE D CA  1 
ATOM   11009 C  C   . PHE D 1 222 ? 8.033   -2.339  -4.438  1.00 37.51  ? 223 PHE D C   1 
ATOM   11010 O  O   . PHE D 1 222 ? 7.203   -1.497  -4.840  1.00 37.25  ? 223 PHE D O   1 
ATOM   11011 C  CB  . PHE D 1 222 ? 9.318   -2.290  -2.274  1.00 37.46  ? 223 PHE D CB  1 
ATOM   11012 C  CG  . PHE D 1 222 ? 9.432   -0.793  -2.227  1.00 39.01  ? 223 PHE D CG  1 
ATOM   11013 C  CD1 . PHE D 1 222 ? 8.654   -0.053  -1.351  1.00 36.96  ? 223 PHE D CD1 1 
ATOM   11014 C  CD2 . PHE D 1 222 ? 10.327  -0.125  -3.048  1.00 39.52  ? 223 PHE D CD2 1 
ATOM   11015 C  CE1 . PHE D 1 222 ? 8.758   1.325   -1.302  1.00 40.37  ? 223 PHE D CE1 1 
ATOM   11016 C  CE2 . PHE D 1 222 ? 10.436  1.254   -3.002  1.00 41.80  ? 223 PHE D CE2 1 
ATOM   11017 C  CZ  . PHE D 1 222 ? 9.651   1.979   -2.128  1.00 37.08  ? 223 PHE D CZ  1 
ATOM   11018 N  N   . VAL D 1 223 ? 8.940   -2.910  -5.229  1.00 37.96  ? 224 VAL D N   1 
ATOM   11019 C  CA  . VAL D 1 223 ? 9.020   -2.598  -6.657  1.00 38.27  ? 224 VAL D CA  1 
ATOM   11020 C  C   . VAL D 1 223 ? 7.670   -2.807  -7.360  1.00 43.18  ? 224 VAL D C   1 
ATOM   11021 O  O   . VAL D 1 223 ? 7.169   -1.919  -8.073  1.00 46.75  ? 224 VAL D O   1 
ATOM   11022 C  CB  . VAL D 1 223 ? 10.111  -3.455  -7.342  1.00 45.83  ? 224 VAL D CB  1 
ATOM   11023 C  CG1 . VAL D 1 223 ? 9.943   -3.457  -8.852  1.00 46.89  ? 224 VAL D CG1 1 
ATOM   11024 C  CG2 . VAL D 1 223 ? 11.498  -2.961  -6.947  1.00 39.06  ? 224 VAL D CG2 1 
ATOM   11025 N  N   . GLN D 1 224 ? 7.079   -3.977  -7.132  1.00 40.44  ? 225 GLN D N   1 
ATOM   11026 C  CA  . GLN D 1 224 ? 5.764   -4.306  -7.671  1.00 44.37  ? 225 GLN D CA  1 
ATOM   11027 C  C   . GLN D 1 224 ? 4.723   -3.267  -7.280  1.00 43.98  ? 225 GLN D C   1 
ATOM   11028 O  O   . GLN D 1 224 ? 3.926   -2.850  -8.112  1.00 38.14  ? 225 GLN D O   1 
ATOM   11029 C  CB  . GLN D 1 224 ? 5.310   -5.687  -7.195  1.00 44.65  ? 225 GLN D CB  1 
ATOM   11030 C  CG  . GLN D 1 224 ? 5.940   -6.851  -7.936  1.00 55.77  ? 225 GLN D CG  1 
ATOM   11031 C  CD  . GLN D 1 224 ? 5.391   -8.187  -7.477  1.00 65.66  ? 225 GLN D CD  1 
ATOM   11032 O  OE1 . GLN D 1 224 ? 4.420   -8.246  -6.722  1.00 67.99  ? 225 GLN D OE1 1 
ATOM   11033 N  NE2 . GLN D 1 224 ? 6.011   -9.270  -7.932  1.00 69.42  ? 225 GLN D NE2 1 
ATOM   11034 N  N   . GLY D 1 225 ? 4.735   -2.860  -6.014  1.00 46.72  ? 226 GLY D N   1 
ATOM   11035 C  CA  . GLY D 1 225 ? 3.803   -1.861  -5.521  1.00 37.14  ? 226 GLY D CA  1 
ATOM   11036 C  C   . GLY D 1 225 ? 3.917   -0.555  -6.282  1.00 39.33  ? 226 GLY D C   1 
ATOM   11037 O  O   . GLY D 1 225 ? 2.906   0.013   -6.730  1.00 36.82  ? 226 GLY D O   1 
ATOM   11038 N  N   . LEU D 1 226 ? 5.152   -0.078  -6.432  1.00 36.98  ? 227 LEU D N   1 
ATOM   11039 C  CA  . LEU D 1 226 ? 5.393   1.117   -7.238  1.00 36.97  ? 227 LEU D CA  1 
ATOM   11040 C  C   . LEU D 1 226 ? 4.812   0.953   -8.642  1.00 40.28  ? 227 LEU D C   1 
ATOM   11041 O  O   . LEU D 1 226 ? 4.110   1.844   -9.151  1.00 37.22  ? 227 LEU D O   1 
ATOM   11042 C  CB  . LEU D 1 226 ? 6.890   1.426   -7.318  1.00 38.40  ? 227 LEU D CB  1 
ATOM   11043 C  CG  . LEU D 1 226 ? 7.493   2.144   -6.111  1.00 37.20  ? 227 LEU D CG  1 
ATOM   11044 C  CD1 . LEU D 1 226 ? 9.008   2.182   -6.213  1.00 37.43  ? 227 LEU D CD1 1 
ATOM   11045 C  CD2 . LEU D 1 226 ? 6.924   3.552   -5.994  1.00 36.72  ? 227 LEU D CD2 1 
ATOM   11046 N  N   . GLY D 1 227 ? 5.094   -0.196  -9.255  1.00 40.46  ? 228 GLY D N   1 
ATOM   11047 C  CA  . GLY D 1 227 ? 4.563   -0.496  -10.576 1.00 39.70  ? 228 GLY D CA  1 
ATOM   11048 C  C   . GLY D 1 227 ? 3.047   -0.398  -10.654 1.00 45.06  ? 228 GLY D C   1 
ATOM   11049 O  O   . GLY D 1 227 ? 2.496   0.201   -11.582 1.00 47.69  ? 228 GLY D O   1 
ATOM   11050 N  N   . VAL D 1 228 ? 2.375   -0.980  -9.665  1.00 45.65  ? 229 VAL D N   1 
ATOM   11051 C  CA  . VAL D 1 228 ? 0.918   -0.997  -9.611  1.00 45.26  ? 229 VAL D CA  1 
ATOM   11052 C  C   . VAL D 1 228 ? 0.348   0.407   -9.458  1.00 47.17  ? 229 VAL D C   1 
ATOM   11053 O  O   . VAL D 1 228 ? -0.598  0.771   -10.156 1.00 45.57  ? 229 VAL D O   1 
ATOM   11054 C  CB  . VAL D 1 228 ? 0.406   -1.883  -8.458  1.00 42.59  ? 229 VAL D CB  1 
ATOM   11055 C  CG1 . VAL D 1 228 ? -1.104  -1.747  -8.303  1.00 44.16  ? 229 VAL D CG1 1 
ATOM   11056 C  CG2 . VAL D 1 228 ? 0.791   -3.333  -8.697  1.00 39.81  ? 229 VAL D CG2 1 
ATOM   11057 N  N   . ALA D 1 229 ? 0.921   1.193   -8.548  1.00 39.84  ? 230 ALA D N   1 
ATOM   11058 C  CA  . ALA D 1 229 ? 0.488   2.581   -8.386  1.00 40.84  ? 230 ALA D CA  1 
ATOM   11059 C  C   . ALA D 1 229 ? 0.621   3.346   -9.705  1.00 43.33  ? 230 ALA D C   1 
ATOM   11060 O  O   . ALA D 1 229 ? -0.322  4.023   -10.158 1.00 49.21  ? 230 ALA D O   1 
ATOM   11061 C  CB  . ALA D 1 229 ? 1.286   3.264   -7.290  1.00 36.12  ? 230 ALA D CB  1 
ATOM   11062 N  N   . SER D 1 230 ? 1.793   3.222   -10.325 1.00 41.70  ? 231 SER D N   1 
ATOM   11063 C  CA  . SER D 1 230 ? 2.037   3.850   -11.620 1.00 43.90  ? 231 SER D CA  1 
ATOM   11064 C  C   . SER D 1 230 ? 0.975   3.452   -12.646 1.00 43.67  ? 231 SER D C   1 
ATOM   11065 O  O   . SER D 1 230 ? 0.462   4.295   -13.390 1.00 44.74  ? 231 SER D O   1 
ATOM   11066 C  CB  . SER D 1 230 ? 3.428   3.484   -12.138 1.00 43.67  ? 231 SER D CB  1 
ATOM   11067 O  OG  . SER D 1 230 ? 3.709   4.147   -13.357 1.00 49.10  ? 231 SER D OG  1 
ATOM   11068 N  N   . ASP D 1 231 ? 0.636   2.166   -12.665 1.00 50.79  ? 232 ASP D N   1 
ATOM   11069 C  CA  . ASP D 1 231 ? -0.330  1.649   -13.629 1.00 56.15  ? 232 ASP D CA  1 
ATOM   11070 C  C   . ASP D 1 231 ? -1.757  2.135   -13.377 1.00 51.20  ? 232 ASP D C   1 
ATOM   11071 O  O   . ASP D 1 231 ? -2.488  2.419   -14.327 1.00 46.32  ? 232 ASP D O   1 
ATOM   11072 C  CB  . ASP D 1 231 ? -0.302  0.121   -13.642 1.00 67.57  ? 232 ASP D CB  1 
ATOM   11073 C  CG  . ASP D 1 231 ? 0.612   -0.432  -14.717 1.00 79.26  ? 232 ASP D CG  1 
ATOM   11074 O  OD1 . ASP D 1 231 ? 0.799   0.252   -15.746 1.00 82.48  ? 232 ASP D OD1 1 
ATOM   11075 O  OD2 . ASP D 1 231 ? 1.142   -1.548  -14.535 1.00 82.13  ? 232 ASP D OD2 1 
ATOM   11076 N  N   . VAL D 1 232 ? -2.162  2.229   -12.114 1.00 51.32  ? 233 VAL D N   1 
ATOM   11077 C  CA  . VAL D 1 232 ? -3.514  2.696   -11.826 1.00 47.91  ? 233 VAL D CA  1 
ATOM   11078 C  C   . VAL D 1 232 ? -3.610  4.189   -12.128 1.00 48.25  ? 233 VAL D C   1 
ATOM   11079 O  O   . VAL D 1 232 ? -4.651  4.659   -12.592 1.00 45.10  ? 233 VAL D O   1 
ATOM   11080 C  CB  . VAL D 1 232 ? -3.958  2.406   -10.362 1.00 52.05  ? 233 VAL D CB  1 
ATOM   11081 C  CG1 . VAL D 1 232 ? -3.802  0.926   -10.039 1.00 51.92  ? 233 VAL D CG1 1 
ATOM   11082 C  CG2 . VAL D 1 232 ? -3.200  3.259   -9.357  1.00 53.04  ? 233 VAL D CG2 1 
ATOM   11083 N  N   . VAL D 1 233 ? -2.526  4.931   -11.903 1.00 47.51  ? 234 VAL D N   1 
ATOM   11084 C  CA  . VAL D 1 233 ? -2.528  6.342   -12.286 1.00 46.06  ? 234 VAL D CA  1 
ATOM   11085 C  C   . VAL D 1 233 ? -2.658  6.471   -13.802 1.00 47.49  ? 234 VAL D C   1 
ATOM   11086 O  O   . VAL D 1 233 ? -3.501  7.224   -14.308 1.00 48.37  ? 234 VAL D O   1 
ATOM   11087 C  CB  . VAL D 1 233 ? -1.259  7.071   -11.815 1.00 36.71  ? 234 VAL D CB  1 
ATOM   11088 C  CG1 . VAL D 1 233 ? -1.211  8.476   -12.398 1.00 36.79  ? 234 VAL D CG1 1 
ATOM   11089 C  CG2 . VAL D 1 233 ? -1.216  7.121   -10.300 1.00 36.16  ? 234 VAL D CG2 1 
ATOM   11090 N  N   . ARG D 1 234 ? -1.828  5.716   -14.517 1.00 38.19  ? 235 ARG D N   1 
ATOM   11091 C  CA  . ARG D 1 234 ? -1.848  5.710   -15.977 1.00 48.58  ? 235 ARG D CA  1 
ATOM   11092 C  C   . ARG D 1 234 ? -3.226  5.368   -16.547 1.00 47.77  ? 235 ARG D C   1 
ATOM   11093 O  O   . ARG D 1 234 ? -3.696  6.016   -17.482 1.00 46.22  ? 235 ARG D O   1 
ATOM   11094 C  CB  . ARG D 1 234 ? -0.803  4.725   -16.509 1.00 53.69  ? 235 ARG D CB  1 
ATOM   11095 C  CG  . ARG D 1 234 ? -1.044  4.257   -17.934 1.00 62.00  ? 235 ARG D CG  1 
ATOM   11096 C  CD  . ARG D 1 234 ? -0.017  3.215   -18.347 1.00 70.93  ? 235 ARG D CD  1 
ATOM   11097 N  NE  . ARG D 1 234 ? -0.542  2.298   -19.355 1.00 79.00  ? 235 ARG D NE  1 
ATOM   11098 C  CZ  . ARG D 1 234 ? -1.129  1.140   -19.072 1.00 84.43  ? 235 ARG D CZ  1 
ATOM   11099 N  NH1 . ARG D 1 234 ? -1.267  0.757   -17.810 1.00 86.12  ? 235 ARG D NH1 1 
ATOM   11100 N  NH2 . ARG D 1 234 ? -1.579  0.364   -20.049 1.00 87.40  ? 235 ARG D NH2 1 
ATOM   11101 N  N   . LYS D 1 235 ? -3.877  4.359   -15.975 1.00 45.07  ? 236 LYS D N   1 
ATOM   11102 C  CA  . LYS D 1 235 ? -5.160  3.897   -16.496 1.00 45.84  ? 236 LYS D CA  1 
ATOM   11103 C  C   . LYS D 1 235 ? -6.322  4.810   -16.104 1.00 45.29  ? 236 LYS D C   1 
ATOM   11104 O  O   . LYS D 1 235 ? -7.267  4.978   -16.876 1.00 42.48  ? 236 LYS D O   1 
ATOM   11105 C  CB  . LYS D 1 235 ? -5.442  2.466   -16.033 1.00 45.57  ? 236 LYS D CB  1 
ATOM   11106 C  CG  . LYS D 1 235 ? -5.062  1.415   -17.065 1.00 47.84  ? 236 LYS D CG  1 
ATOM   11107 C  CD  . LYS D 1 235 ? -5.307  0.005   -16.558 1.00 53.86  ? 236 LYS D CD  1 
ATOM   11108 C  CE  . LYS D 1 235 ? -4.908  -1.023  -17.606 1.00 61.30  ? 236 LYS D CE  1 
ATOM   11109 N  NZ  . LYS D 1 235 ? -4.942  -2.415  -17.077 1.00 62.77  ? 236 LYS D NZ  1 
ATOM   11110 N  N   . VAL D 1 236 ? -6.259  5.395   -14.911 1.00 48.18  ? 237 VAL D N   1 
ATOM   11111 C  CA  . VAL D 1 236 ? -7.292  6.340   -14.495 1.00 46.65  ? 237 VAL D CA  1 
ATOM   11112 C  C   . VAL D 1 236 ? -7.172  7.627   -15.313 1.00 46.89  ? 237 VAL D C   1 
ATOM   11113 O  O   . VAL D 1 236 ? -8.169  8.288   -15.598 1.00 50.90  ? 237 VAL D O   1 
ATOM   11114 C  CB  . VAL D 1 236 ? -7.210  6.646   -12.980 1.00 43.49  ? 237 VAL D CB  1 
ATOM   11115 C  CG1 . VAL D 1 236 ? -8.070  7.846   -12.609 1.00 38.49  ? 237 VAL D CG1 1 
ATOM   11116 C  CG2 . VAL D 1 236 ? -7.643  5.428   -12.178 1.00 45.54  ? 237 VAL D CG2 1 
ATOM   11117 N  N   . ALA D 1 237 ? -5.950  7.958   -15.722 1.00 54.42  ? 238 ALA D N   1 
ATOM   11118 C  CA  . ALA D 1 237 ? -5.716  9.144   -16.546 1.00 52.44  ? 238 ALA D CA  1 
ATOM   11119 C  C   . ALA D 1 237 ? -6.520  9.132   -17.849 1.00 57.13  ? 238 ALA D C   1 
ATOM   11120 O  O   . ALA D 1 237 ? -6.790  10.187  -18.426 1.00 57.83  ? 238 ALA D O   1 
ATOM   11121 C  CB  . ALA D 1 237 ? -4.233  9.281   -16.854 1.00 50.98  ? 238 ALA D CB  1 
ATOM   11122 N  N   . GLN D 1 238 ? -6.908  7.944   -18.305 1.00 62.83  ? 239 GLN D N   1 
ATOM   11123 C  CA  . GLN D 1 238 ? -7.573  7.805   -19.597 1.00 70.25  ? 239 GLN D CA  1 
ATOM   11124 C  C   . GLN D 1 238 ? -9.087  7.994   -19.506 1.00 66.53  ? 239 GLN D C   1 
ATOM   11125 O  O   . GLN D 1 238 ? -9.733  8.293   -20.511 1.00 67.64  ? 239 GLN D O   1 
ATOM   11126 C  CB  . GLN D 1 238 ? -7.248  6.438   -20.214 1.00 78.71  ? 239 GLN D CB  1 
ATOM   11127 C  CG  . GLN D 1 238 ? -7.467  6.353   -21.726 1.00 88.62  ? 239 GLN D CG  1 
ATOM   11128 C  CD  . GLN D 1 238 ? -8.757  5.650   -22.112 1.00 97.44  ? 239 GLN D CD  1 
ATOM   11129 O  OE1 . GLN D 1 238 ? -9.735  5.659   -21.365 1.00 99.33  ? 239 GLN D OE1 1 
ATOM   11130 N  NE2 . GLN D 1 238 ? -8.766  5.042   -23.294 1.00 100.39 ? 239 GLN D NE2 1 
ATOM   11131 N  N   . VAL D 1 239 ? -9.656  7.831   -18.313 1.00 63.60  ? 240 VAL D N   1 
ATOM   11132 C  CA  . VAL D 1 239 ? -11.106 7.938   -18.164 1.00 65.38  ? 240 VAL D CA  1 
ATOM   11133 C  C   . VAL D 1 239 ? -11.573 9.362   -18.498 1.00 63.09  ? 240 VAL D C   1 
ATOM   11134 O  O   . VAL D 1 239 ? -10.970 10.348  -18.069 1.00 64.85  ? 240 VAL D O   1 
ATOM   11135 C  CB  . VAL D 1 239 ? -11.579 7.512   -16.742 1.00 59.48  ? 240 VAL D CB  1 
ATOM   11136 C  CG1 . VAL D 1 239 ? -10.924 6.198   -16.344 1.00 56.86  ? 240 VAL D CG1 1 
ATOM   11137 C  CG2 . VAL D 1 239 ? -11.290 8.581   -15.697 1.00 57.55  ? 240 VAL D CG2 1 
ATOM   11138 N  N   . PRO D 1 240 ? -12.622 9.464   -19.327 1.00 59.39  ? 241 PRO D N   1 
ATOM   11139 C  CA  . PRO D 1 240 ? -13.142 10.736  -19.841 1.00 60.27  ? 241 PRO D CA  1 
ATOM   11140 C  C   . PRO D 1 240 ? -14.001 11.511  -18.844 1.00 55.76  ? 241 PRO D C   1 
ATOM   11141 O  O   . PRO D 1 240 ? -14.549 10.928  -17.908 1.00 55.81  ? 241 PRO D O   1 
ATOM   11142 C  CB  . PRO D 1 240 ? -13.983 10.300  -21.040 1.00 58.54  ? 241 PRO D CB  1 
ATOM   11143 C  CG  . PRO D 1 240 ? -14.477 8.952   -20.657 1.00 60.16  ? 241 PRO D CG  1 
ATOM   11144 C  CD  . PRO D 1 240 ? -13.359 8.311   -19.876 1.00 60.37  ? 241 PRO D CD  1 
ATOM   11145 N  N   . LEU D 1 241 ? -14.110 12.819  -19.055 1.00 56.37  ? 242 LEU D N   1 
ATOM   11146 C  CA  . LEU D 1 241 ? -15.051 13.644  -18.309 1.00 59.09  ? 242 LEU D CA  1 
ATOM   11147 C  C   . LEU D 1 241 ? -16.443 13.506  -18.913 1.00 60.88  ? 242 LEU D C   1 
ATOM   11148 O  O   . LEU D 1 241 ? -16.601 13.524  -20.134 1.00 64.20  ? 242 LEU D O   1 
ATOM   11149 C  CB  . LEU D 1 241 ? -14.619 15.112  -18.313 1.00 59.39  ? 242 LEU D CB  1 
ATOM   11150 C  CG  . LEU D 1 241 ? -13.338 15.488  -17.569 1.00 57.16  ? 242 LEU D CG  1 
ATOM   11151 C  CD1 . LEU D 1 241 ? -12.876 16.869  -17.994 1.00 58.97  ? 242 LEU D CD1 1 
ATOM   11152 C  CD2 . LEU D 1 241 ? -13.559 15.441  -16.067 1.00 56.71  ? 242 LEU D CD2 1 
ATOM   11153 N  N   . GLY D 1 242 ? -17.450 13.366  -18.059 1.00 58.19  ? 243 GLY D N   1 
ATOM   11154 C  CA  . GLY D 1 242 ? -18.817 13.212  -18.522 1.00 58.75  ? 243 GLY D CA  1 
ATOM   11155 C  C   . GLY D 1 242 ? -19.396 14.496  -19.086 1.00 54.99  ? 243 GLY D C   1 
ATOM   11156 O  O   . GLY D 1 242 ? -18.864 15.579  -18.843 1.00 56.51  ? 243 GLY D O   1 
ATOM   11157 N  N   . PRO D 1 243 ? -20.490 14.379  -19.855 1.00 53.49  ? 244 PRO D N   1 
ATOM   11158 C  CA  . PRO D 1 243 ? -21.198 15.527  -20.434 1.00 50.47  ? 244 PRO D CA  1 
ATOM   11159 C  C   . PRO D 1 243 ? -21.693 16.509  -19.373 1.00 50.82  ? 244 PRO D C   1 
ATOM   11160 O  O   . PRO D 1 243 ? -21.468 17.712  -19.510 1.00 53.16  ? 244 PRO D O   1 
ATOM   11161 C  CB  . PRO D 1 243 ? -22.376 14.877  -21.166 1.00 49.63  ? 244 PRO D CB  1 
ATOM   11162 C  CG  . PRO D 1 243 ? -21.907 13.501  -21.477 1.00 51.64  ? 244 PRO D CG  1 
ATOM   11163 C  CD  . PRO D 1 243 ? -21.061 13.099  -20.306 1.00 50.97  ? 244 PRO D CD  1 
ATOM   11164 N  N   . GLU D 1 244 ? -22.357 15.995  -18.340 1.00 49.70  ? 245 GLU D N   1 
ATOM   11165 C  CA  . GLU D 1 244 ? -22.836 16.814  -17.228 1.00 48.43  ? 245 GLU D CA  1 
ATOM   11166 C  C   . GLU D 1 244 ? -21.704 17.640  -16.631 1.00 50.31  ? 245 GLU D C   1 
ATOM   11167 O  O   . GLU D 1 244 ? -21.850 18.843  -16.381 1.00 50.63  ? 245 GLU D O   1 
ATOM   11168 C  CB  . GLU D 1 244 ? -23.463 15.932  -16.147 1.00 50.69  ? 245 GLU D CB  1 
ATOM   11169 C  CG  . GLU D 1 244 ? -24.765 15.270  -16.558 1.00 60.81  ? 245 GLU D CG  1 
ATOM   11170 C  CD  . GLU D 1 244 ? -25.904 16.260  -16.676 1.00 69.47  ? 245 GLU D CD  1 
ATOM   11171 O  OE1 . GLU D 1 244 ? -25.838 17.325  -16.027 1.00 70.01  ? 245 GLU D OE1 1 
ATOM   11172 O  OE2 . GLU D 1 244 ? -26.865 15.977  -17.422 1.00 72.88  ? 245 GLU D OE2 1 
ATOM   11173 N  N   . CYS D 1 245 ? -20.574 16.974  -16.411 1.00 48.14  ? 246 CYS D N   1 
ATOM   11174 C  CA  . CYS D 1 245 ? -19.372 17.623  -15.910 1.00 48.94  ? 246 CYS D CA  1 
ATOM   11175 C  C   . CYS D 1 245 ? -18.942 18.748  -16.841 1.00 45.47  ? 246 CYS D C   1 
ATOM   11176 O  O   . CYS D 1 245 ? -18.643 19.851  -16.392 1.00 41.23  ? 246 CYS D O   1 
ATOM   11177 C  CB  . CYS D 1 245 ? -18.240 16.607  -15.750 1.00 48.82  ? 246 CYS D CB  1 
ATOM   11178 S  SG  . CYS D 1 245 ? -16.641 17.334  -15.322 1.00 120.30 ? 246 CYS D SG  1 
ATOM   11179 N  N   . SER D 1 246 ? -18.924 18.463  -18.140 1.00 47.57  ? 247 SER D N   1 
ATOM   11180 C  CA  . SER D 1 246 ? -18.528 19.449  -19.138 1.00 50.59  ? 247 SER D CA  1 
ATOM   11181 C  C   . SER D 1 246 ? -19.434 20.676  -19.106 1.00 52.73  ? 247 SER D C   1 
ATOM   11182 O  O   . SER D 1 246 ? -18.969 21.804  -19.269 1.00 58.44  ? 247 SER D O   1 
ATOM   11183 C  CB  . SER D 1 246 ? -18.540 18.828  -20.536 1.00 52.81  ? 247 SER D CB  1 
ATOM   11184 O  OG  . SER D 1 246 ? -18.104 19.760  -21.510 1.00 55.76  ? 247 SER D OG  1 
ATOM   11185 N  N   . ARG D 1 247 ? -20.726 20.449  -18.888 1.00 49.62  ? 248 ARG D N   1 
ATOM   11186 C  CA  . ARG D 1 247 ? -21.691 21.541  -18.836 1.00 49.89  ? 248 ARG D CA  1 
ATOM   11187 C  C   . ARG D 1 247 ? -21.496 22.382  -17.577 1.00 46.98  ? 248 ARG D C   1 
ATOM   11188 O  O   . ARG D 1 247 ? -21.511 23.615  -17.637 1.00 39.44  ? 248 ARG D O   1 
ATOM   11189 C  CB  . ARG D 1 247 ? -23.121 21.001  -18.900 1.00 51.95  ? 248 ARG D CB  1 
ATOM   11190 C  CG  . ARG D 1 247 ? -23.393 20.143  -20.125 1.00 56.89  ? 248 ARG D CG  1 
ATOM   11191 C  CD  . ARG D 1 247 ? -24.843 20.226  -20.566 1.00 62.70  ? 248 ARG D CD  1 
ATOM   11192 N  NE  . ARG D 1 247 ? -25.777 19.989  -19.470 1.00 69.07  ? 248 ARG D NE  1 
ATOM   11193 C  CZ  . ARG D 1 247 ? -26.231 18.790  -19.118 1.00 74.84  ? 248 ARG D CZ  1 
ATOM   11194 N  NH1 . ARG D 1 247 ? -25.832 17.707  -19.771 1.00 75.72  ? 248 ARG D NH1 1 
ATOM   11195 N  NH2 . ARG D 1 247 ? -27.085 18.676  -18.110 1.00 76.15  ? 248 ARG D NH2 1 
ATOM   11196 N  N   . ALA D 1 248 ? -21.310 21.712  -16.443 1.00 42.19  ? 249 ALA D N   1 
ATOM   11197 C  CA  . ALA D 1 248 ? -21.052 22.408  -15.185 1.00 43.31  ? 249 ALA D CA  1 
ATOM   11198 C  C   . ALA D 1 248 ? -19.777 23.244  -15.277 1.00 44.19  ? 249 ALA D C   1 
ATOM   11199 O  O   . ALA D 1 248 ? -19.702 24.349  -14.736 1.00 49.10  ? 249 ALA D O   1 
ATOM   11200 C  CB  . ALA D 1 248 ? -20.954 21.415  -14.038 1.00 38.12  ? 249 ALA D CB  1 
ATOM   11201 N  N   . VAL D 1 249 ? -18.783 22.708  -15.978 1.00 39.66  ? 250 VAL D N   1 
ATOM   11202 C  CA  . VAL D 1 249 ? -17.504 23.380  -16.160 1.00 38.60  ? 250 VAL D CA  1 
ATOM   11203 C  C   . VAL D 1 249 ? -17.648 24.589  -17.079 1.00 44.28  ? 250 VAL D C   1 
ATOM   11204 O  O   . VAL D 1 249 ? -17.084 25.649  -16.811 1.00 47.14  ? 250 VAL D O   1 
ATOM   11205 C  CB  . VAL D 1 249 ? -16.443 22.414  -16.730 1.00 43.12  ? 250 VAL D CB  1 
ATOM   11206 C  CG1 . VAL D 1 249 ? -15.240 23.178  -17.265 1.00 44.67  ? 250 VAL D CG1 1 
ATOM   11207 C  CG2 . VAL D 1 249 ? -16.016 21.419  -15.665 1.00 41.28  ? 250 VAL D CG2 1 
ATOM   11208 N  N   . MET D 1 250 ? -18.407 24.427  -18.158 1.00 42.81  ? 251 MET D N   1 
ATOM   11209 C  CA  . MET D 1 250 ? -18.691 25.539  -19.058 1.00 41.68  ? 251 MET D CA  1 
ATOM   11210 C  C   . MET D 1 250 ? -19.401 26.660  -18.307 1.00 44.98  ? 251 MET D C   1 
ATOM   11211 O  O   . MET D 1 250 ? -19.078 27.837  -18.475 1.00 46.80  ? 251 MET D O   1 
ATOM   11212 C  CB  . MET D 1 250 ? -19.538 25.078  -20.245 1.00 40.40  ? 251 MET D CB  1 
ATOM   11213 C  CG  . MET D 1 250 ? -20.150 26.218  -21.050 1.00 41.01  ? 251 MET D CG  1 
ATOM   11214 S  SD  . MET D 1 250 ? -18.924 27.380  -21.683 1.00 49.44  ? 251 MET D SD  1 
ATOM   11215 C  CE  . MET D 1 250 ? -19.978 28.577  -22.497 1.00 71.88  ? 251 MET D CE  1 
ATOM   11216 N  N   . LYS D 1 251 ? -20.361 26.285  -17.468 1.00 44.41  ? 252 LYS D N   1 
ATOM   11217 C  CA  . LYS D 1 251 ? -21.094 27.260  -16.667 1.00 46.18  ? 252 LYS D CA  1 
ATOM   11218 C  C   . LYS D 1 251 ? -20.180 27.903  -15.628 1.00 45.22  ? 252 LYS D C   1 
ATOM   11219 O  O   . LYS D 1 251 ? -20.390 29.044  -15.217 1.00 44.51  ? 252 LYS D O   1 
ATOM   11220 C  CB  . LYS D 1 251 ? -22.296 26.599  -15.989 1.00 48.72  ? 252 LYS D CB  1 
ATOM   11221 C  CG  . LYS D 1 251 ? -23.183 27.553  -15.208 1.00 52.79  ? 252 LYS D CG  1 
ATOM   11222 C  CD  . LYS D 1 251 ? -24.372 26.823  -14.611 1.00 57.96  ? 252 LYS D CD  1 
ATOM   11223 C  CE  . LYS D 1 251 ? -25.201 27.736  -13.724 1.00 61.71  ? 252 LYS D CE  1 
ATOM   11224 N  NZ  . LYS D 1 251 ? -26.095 26.956  -12.823 1.00 65.08  ? 252 LYS D NZ  1 
ATOM   11225 N  N   . LEU D 1 252 ? -19.155 27.165  -15.218 1.00 47.98  ? 253 LEU D N   1 
ATOM   11226 C  CA  . LEU D 1 252 ? -18.207 27.649  -14.221 1.00 43.73  ? 253 LEU D CA  1 
ATOM   11227 C  C   . LEU D 1 252 ? -17.210 28.652  -14.797 1.00 38.54  ? 253 LEU D C   1 
ATOM   11228 O  O   . LEU D 1 252 ? -16.837 29.619  -14.134 1.00 38.65  ? 253 LEU D O   1 
ATOM   11229 C  CB  . LEU D 1 252 ? -17.449 26.470  -13.605 1.00 41.52  ? 253 LEU D CB  1 
ATOM   11230 C  CG  . LEU D 1 252 ? -16.303 26.789  -12.643 1.00 41.27  ? 253 LEU D CG  1 
ATOM   11231 C  CD1 . LEU D 1 252 ? -16.839 27.356  -11.343 1.00 37.50  ? 253 LEU D CD1 1 
ATOM   11232 C  CD2 . LEU D 1 252 ? -15.459 25.550  -12.383 1.00 40.48  ? 253 LEU D CD2 1 
ATOM   11233 N  N   . VAL D 1 253 ? -16.789 28.424  -16.037 1.00 43.76  ? 254 VAL D N   1 
ATOM   11234 C  CA  . VAL D 1 253 ? -15.651 29.150  -16.590 1.00 48.39  ? 254 VAL D CA  1 
ATOM   11235 C  C   . VAL D 1 253 ? -16.024 30.262  -17.575 1.00 54.23  ? 254 VAL D C   1 
ATOM   11236 O  O   . VAL D 1 253 ? -15.636 31.414  -17.381 1.00 60.57  ? 254 VAL D O   1 
ATOM   11237 C  CB  . VAL D 1 253 ? -14.677 28.177  -17.289 1.00 48.78  ? 254 VAL D CB  1 
ATOM   11238 C  CG1 . VAL D 1 253 ? -13.512 28.935  -17.901 1.00 49.07  ? 254 VAL D CG1 1 
ATOM   11239 C  CG2 . VAL D 1 253 ? -14.177 27.133  -16.302 1.00 38.72  ? 254 VAL D CG2 1 
ATOM   11240 N  N   . TYR D 1 254 ? -16.769 29.929  -18.625 1.00 49.89  ? 255 TYR D N   1 
ATOM   11241 C  CA  . TYR D 1 254 ? -16.996 30.887  -19.707 1.00 47.05  ? 255 TYR D CA  1 
ATOM   11242 C  C   . TYR D 1 254 ? -18.435 31.384  -19.840 1.00 47.60  ? 255 TYR D C   1 
ATOM   11243 O  O   . TYR D 1 254 ? -18.799 31.947  -20.871 1.00 48.59  ? 255 TYR D O   1 
ATOM   11244 C  CB  . TYR D 1 254 ? -16.556 30.284  -21.044 1.00 50.20  ? 255 TYR D CB  1 
ATOM   11245 C  CG  . TYR D 1 254 ? -15.081 29.958  -21.122 1.00 56.93  ? 255 TYR D CG  1 
ATOM   11246 C  CD1 . TYR D 1 254 ? -14.125 30.962  -21.032 1.00 54.16  ? 255 TYR D CD1 1 
ATOM   11247 C  CD2 . TYR D 1 254 ? -14.645 28.652  -21.306 1.00 53.58  ? 255 TYR D CD2 1 
ATOM   11248 C  CE1 . TYR D 1 254 ? -12.777 30.673  -21.106 1.00 55.86  ? 255 TYR D CE1 1 
ATOM   11249 C  CE2 . TYR D 1 254 ? -13.297 28.354  -21.384 1.00 57.78  ? 255 TYR D CE2 1 
ATOM   11250 C  CZ  . TYR D 1 254 ? -12.369 29.368  -21.283 1.00 58.91  ? 255 TYR D CZ  1 
ATOM   11251 O  OH  . TYR D 1 254 ? -11.026 29.082  -21.359 1.00 56.80  ? 255 TYR D OH  1 
ATOM   11252 N  N   . CYS D 1 255 ? -19.253 31.188  -18.812 1.00 40.72  ? 256 CYS D N   1 
ATOM   11253 C  CA  . CYS D 1 255 ? -20.606 31.729  -18.846 1.00 48.41  ? 256 CYS D CA  1 
ATOM   11254 C  C   . CYS D 1 255 ? -20.637 33.141  -18.273 1.00 53.47  ? 256 CYS D C   1 
ATOM   11255 O  O   . CYS D 1 255 ? -21.548 33.916  -18.563 1.00 49.31  ? 256 CYS D O   1 
ATOM   11256 C  CB  . CYS D 1 255 ? -21.581 30.821  -18.098 1.00 42.45  ? 256 CYS D CB  1 
ATOM   11257 S  SG  . CYS D 1 255 ? -22.220 29.469  -19.115 1.00 51.42  ? 256 CYS D SG  1 
ATOM   11258 N  N   . ALA D 1 256 ? -19.636 33.472  -17.464 1.00 53.76  ? 257 ALA D N   1 
ATOM   11259 C  CA  . ALA D 1 256 ? -19.475 34.835  -16.979 1.00 41.30  ? 257 ALA D CA  1 
ATOM   11260 C  C   . ALA D 1 256 ? -19.200 35.752  -18.163 1.00 57.78  ? 257 ALA D C   1 
ATOM   11261 O  O   . ALA D 1 256 ? -19.743 36.853  -18.252 1.00 60.34  ? 257 ALA D O   1 
ATOM   11262 C  CB  . ALA D 1 256 ? -18.353 34.919  -15.961 1.00 41.10  ? 257 ALA D CB  1 
ATOM   11263 N  N   . HIS D 1 257 ? -18.358 35.276  -19.075 1.00 42.38  ? 258 HIS D N   1 
ATOM   11264 C  CA  . HIS D 1 257 ? -18.068 35.993  -20.309 1.00 43.31  ? 258 HIS D CA  1 
ATOM   11265 C  C   . HIS D 1 257 ? -19.337 36.158  -21.134 1.00 55.60  ? 258 HIS D C   1 
ATOM   11266 O  O   . HIS D 1 257 ? -19.647 37.250  -21.606 1.00 61.44  ? 258 HIS D O   1 
ATOM   11267 C  CB  . HIS D 1 257 ? -17.007 35.256  -21.130 1.00 43.57  ? 258 HIS D CB  1 
ATOM   11268 C  CG  . HIS D 1 257 ? -15.716 35.043  -20.403 1.00 55.85  ? 258 HIS D CG  1 
ATOM   11269 N  ND1 . HIS D 1 257 ? -15.591 34.162  -19.350 1.00 42.41  ? 258 HIS D ND1 1 
ATOM   11270 C  CD2 . HIS D 1 257 ? -14.490 35.589  -20.583 1.00 54.19  ? 258 HIS D CD2 1 
ATOM   11271 C  CE1 . HIS D 1 257 ? -14.346 34.180  -18.909 1.00 52.68  ? 258 HIS D CE1 1 
ATOM   11272 N  NE2 . HIS D 1 257 ? -13.657 35.038  -19.641 1.00 51.26  ? 258 HIS D NE2 1 
ATOM   11273 N  N   . CYS D 1 258 ? -20.069 35.060  -21.293 1.00 57.76  ? 259 CYS D N   1 
ATOM   11274 C  CA  . CYS D 1 258 ? -21.285 35.051  -22.095 1.00 55.34  ? 259 CYS D CA  1 
ATOM   11275 C  C   . CYS D 1 258 ? -22.369 35.948  -21.508 1.00 57.23  ? 259 CYS D C   1 
ATOM   11276 O  O   . CYS D 1 258 ? -23.243 36.423  -22.228 1.00 57.53  ? 259 CYS D O   1 
ATOM   11277 C  CB  . CYS D 1 258 ? -21.815 33.622  -22.240 1.00 55.75  ? 259 CYS D CB  1 
ATOM   11278 S  SG  . CYS D 1 258 ? -20.826 32.565  -23.322 1.00 96.12  ? 259 CYS D SG  1 
ATOM   11279 N  N   . LEU D 1 259 ? -22.309 36.188  -20.202 1.00 56.24  ? 260 LEU D N   1 
ATOM   11280 C  CA  . LEU D 1 259 ? -23.341 36.977  -19.541 1.00 57.50  ? 260 LEU D CA  1 
ATOM   11281 C  C   . LEU D 1 259 ? -22.836 38.340  -19.068 1.00 61.88  ? 260 LEU D C   1 
ATOM   11282 O  O   . LEU D 1 259 ? -23.215 38.815  -17.998 1.00 61.15  ? 260 LEU D O   1 
ATOM   11283 C  CB  . LEU D 1 259 ? -23.927 36.195  -18.365 1.00 54.31  ? 260 LEU D CB  1 
ATOM   11284 C  CG  . LEU D 1 259 ? -24.791 35.002  -18.782 1.00 50.35  ? 260 LEU D CG  1 
ATOM   11285 C  CD1 . LEU D 1 259 ? -25.021 34.053  -17.616 1.00 50.69  ? 260 LEU D CD1 1 
ATOM   11286 C  CD2 . LEU D 1 259 ? -26.114 35.481  -19.360 1.00 49.56  ? 260 LEU D CD2 1 
ATOM   11287 N  N   . GLY D 1 260 ? -21.980 38.962  -19.874 1.00 63.74  ? 261 GLY D N   1 
ATOM   11288 C  CA  . GLY D 1 260 ? -21.600 40.349  -19.669 1.00 64.11  ? 261 GLY D CA  1 
ATOM   11289 C  C   . GLY D 1 260 ? -20.552 40.653  -18.613 1.00 62.45  ? 261 GLY D C   1 
ATOM   11290 O  O   . GLY D 1 260 ? -20.202 41.815  -18.413 1.00 65.91  ? 261 GLY D O   1 
ATOM   11291 N  N   . VAL D 1 261 ? -20.046 39.630  -17.933 1.00 64.85  ? 262 VAL D N   1 
ATOM   11292 C  CA  . VAL D 1 261 ? -19.031 39.850  -16.904 1.00 66.06  ? 262 VAL D CA  1 
ATOM   11293 C  C   . VAL D 1 261 ? -17.800 38.950  -17.066 1.00 66.34  ? 262 VAL D C   1 
ATOM   11294 O  O   . VAL D 1 261 ? -17.532 38.098  -16.219 1.00 66.39  ? 262 VAL D O   1 
ATOM   11295 C  CB  . VAL D 1 261 ? -19.624 39.647  -15.492 1.00 65.60  ? 262 VAL D CB  1 
ATOM   11296 C  CG1 . VAL D 1 261 ? -20.376 40.891  -15.050 1.00 66.06  ? 262 VAL D CG1 1 
ATOM   11297 C  CG2 . VAL D 1 261 ? -20.541 38.430  -15.464 1.00 66.16  ? 262 VAL D CG2 1 
ATOM   11298 N  N   . PRO D 1 262 ? -17.032 39.155  -18.150 1.00 66.13  ? 263 PRO D N   1 
ATOM   11299 C  CA  . PRO D 1 262 ? -15.853 38.325  -18.428 1.00 66.46  ? 263 PRO D CA  1 
ATOM   11300 C  C   . PRO D 1 262 ? -14.731 38.515  -17.409 1.00 70.14  ? 263 PRO D C   1 
ATOM   11301 O  O   . PRO D 1 262 ? -13.978 37.577  -17.146 1.00 69.58  ? 263 PRO D O   1 
ATOM   11302 C  CB  . PRO D 1 262 ? -15.412 38.801  -19.814 1.00 66.25  ? 263 PRO D CB  1 
ATOM   11303 C  CG  . PRO D 1 262 ? -15.893 40.199  -19.896 1.00 66.77  ? 263 PRO D CG  1 
ATOM   11304 C  CD  . PRO D 1 262 ? -17.189 40.233  -19.143 1.00 66.88  ? 263 PRO D CD  1 
ATOM   11305 N  N   . GLY D 1 263 ? -14.625 39.716  -16.848 1.00 71.87  ? 264 GLY D N   1 
ATOM   11306 C  CA  . GLY D 1 263 ? -13.579 40.020  -15.888 1.00 73.69  ? 264 GLY D CA  1 
ATOM   11307 C  C   . GLY D 1 263 ? -13.750 39.277  -14.578 1.00 72.42  ? 264 GLY D C   1 
ATOM   11308 O  O   . GLY D 1 263 ? -12.797 39.114  -13.816 1.00 72.08  ? 264 GLY D O   1 
ATOM   11309 N  N   . ALA D 1 264 ? -14.972 38.825  -14.317 1.00 74.33  ? 265 ALA D N   1 
ATOM   11310 C  CA  . ALA D 1 264 ? -15.269 38.079  -13.101 1.00 72.32  ? 265 ALA D CA  1 
ATOM   11311 C  C   . ALA D 1 264 ? -14.639 36.691  -13.144 1.00 69.97  ? 265 ALA D C   1 
ATOM   11312 O  O   . ALA D 1 264 ? -14.572 36.061  -14.199 1.00 71.75  ? 265 ALA D O   1 
ATOM   11313 C  CB  . ALA D 1 264 ? -16.771 37.972  -12.899 1.00 75.55  ? 265 ALA D CB  1 
ATOM   11314 N  N   . ARG D 1 265 ? -14.176 36.225  -11.990 1.00 62.62  ? 266 ARG D N   1 
ATOM   11315 C  CA  . ARG D 1 265 ? -13.597 34.893  -11.876 1.00 60.01  ? 266 ARG D CA  1 
ATOM   11316 C  C   . ARG D 1 265 ? -14.429 34.050  -10.912 1.00 55.61  ? 266 ARG D C   1 
ATOM   11317 O  O   . ARG D 1 265 ? -15.033 34.584  -9.982  1.00 59.30  ? 266 ARG D O   1 
ATOM   11318 C  CB  . ARG D 1 265 ? -12.139 34.978  -11.416 1.00 59.94  ? 266 ARG D CB  1 
ATOM   11319 C  CG  . ARG D 1 265 ? -11.183 35.458  -12.499 1.00 62.06  ? 266 ARG D CG  1 
ATOM   11320 C  CD  . ARG D 1 265 ? -9.734  35.208  -12.114 1.00 62.03  ? 266 ARG D CD  1 
ATOM   11321 N  N   . PRO D 1 266 ? -14.467 32.727  -11.134 1.00 53.41  ? 267 PRO D N   1 
ATOM   11322 C  CA  . PRO D 1 266 ? -15.377 31.866  -10.372 1.00 54.65  ? 267 PRO D CA  1 
ATOM   11323 C  C   . PRO D 1 266 ? -15.020 31.746  -8.895  1.00 56.13  ? 267 PRO D C   1 
ATOM   11324 O  O   . PRO D 1 266 ? -13.846 31.802  -8.527  1.00 53.86  ? 267 PRO D O   1 
ATOM   11325 C  CB  . PRO D 1 266 ? -15.234 30.513  -11.071 1.00 49.70  ? 267 PRO D CB  1 
ATOM   11326 C  CG  . PRO D 1 266 ? -13.865 30.535  -11.633 1.00 48.01  ? 267 PRO D CG  1 
ATOM   11327 C  CD  . PRO D 1 266 ? -13.639 31.950  -12.074 1.00 52.33  ? 267 PRO D CD  1 
ATOM   11328 N  N   . CYS D 1 267 ? -16.044 31.580  -8.064  1.00 61.87  ? 268 CYS D N   1 
ATOM   11329 C  CA  A CYS D 1 267 ? -15.845 31.439  -6.630  0.57 61.04  ? 268 CYS D CA  1 
ATOM   11330 C  CA  B CYS D 1 267 ? -15.867 31.416  -6.625  0.43 61.07  ? 268 CYS D CA  1 
ATOM   11331 C  C   . CYS D 1 267 ? -15.090 30.152  -6.301  1.00 59.10  ? 268 CYS D C   1 
ATOM   11332 O  O   . CYS D 1 267 ? -15.281 29.126  -6.955  1.00 59.67  ? 268 CYS D O   1 
ATOM   11333 C  CB  A CYS D 1 267 ? -17.190 31.473  -5.901  0.57 62.40  ? 268 CYS D CB  1 
ATOM   11334 C  CB  B CYS D 1 267 ? -17.223 31.369  -5.919  0.43 61.98  ? 268 CYS D CB  1 
ATOM   11335 S  SG  A CYS D 1 267 ? -18.177 32.955  -6.241  0.57 47.11  ? 268 CYS D SG  1 
ATOM   11336 S  SG  B CYS D 1 267 ? -17.116 31.393  -4.114  0.43 78.71  ? 268 CYS D SG  1 
ATOM   11337 N  N   . PRO D 1 268 ? -14.211 30.216  -5.289  1.00 55.96  ? 269 PRO D N   1 
ATOM   11338 C  CA  . PRO D 1 268 ? -13.470 29.043  -4.818  1.00 56.69  ? 269 PRO D CA  1 
ATOM   11339 C  C   . PRO D 1 268 ? -14.378 27.851  -4.515  1.00 52.73  ? 269 PRO D C   1 
ATOM   11340 O  O   . PRO D 1 268 ? -14.135 26.767  -5.038  1.00 49.54  ? 269 PRO D O   1 
ATOM   11341 C  CB  . PRO D 1 268 ? -12.795 29.555  -3.547  1.00 56.24  ? 269 PRO D CB  1 
ATOM   11342 C  CG  . PRO D 1 268 ? -12.551 30.995  -3.832  1.00 57.81  ? 269 PRO D CG  1 
ATOM   11343 C  CD  . PRO D 1 268 ? -13.723 31.458  -4.660  1.00 57.19  ? 269 PRO D CD  1 
ATOM   11344 N  N   . ASP D 1 269 ? -15.413 28.056  -3.703  1.00 50.34  ? 270 ASP D N   1 
ATOM   11345 C  CA  . ASP D 1 269 ? -16.314 26.971  -3.314  1.00 50.67  ? 270 ASP D CA  1 
ATOM   11346 C  C   . ASP D 1 269 ? -17.136 26.447  -4.493  1.00 48.52  ? 270 ASP D C   1 
ATOM   11347 O  O   . ASP D 1 269 ? -17.427 25.252  -4.576  1.00 48.19  ? 270 ASP D O   1 
ATOM   11348 C  CB  . ASP D 1 269 ? -17.246 27.433  -2.191  1.00 50.87  ? 270 ASP D CB  1 
ATOM   11349 C  CG  . ASP D 1 269 ? -16.521 27.616  -0.871  1.00 52.49  ? 270 ASP D CG  1 
ATOM   11350 O  OD1 . ASP D 1 269 ? -15.423 27.041  -0.709  1.00 55.49  ? 270 ASP D OD1 1 
ATOM   11351 O  OD2 . ASP D 1 269 ? -17.048 28.332  0.006   1.00 53.93  ? 270 ASP D OD2 1 
ATOM   11352 N  N   . TYR D 1 270 ? -17.514 27.350  -5.393  1.00 49.11  ? 271 TYR D N   1 
ATOM   11353 C  CA  . TYR D 1 270 ? -18.205 26.988  -6.628  1.00 47.23  ? 271 TYR D CA  1 
ATOM   11354 C  C   . TYR D 1 270 ? -17.334 26.023  -7.429  1.00 41.95  ? 271 TYR D C   1 
ATOM   11355 O  O   . TYR D 1 270 ? -17.765 24.924  -7.805  1.00 41.48  ? 271 TYR D O   1 
ATOM   11356 C  CB  . TYR D 1 270 ? -18.523 28.251  -7.438  1.00 37.84  ? 271 TYR D CB  1 
ATOM   11357 C  CG  . TYR D 1 270 ? -19.315 28.044  -8.715  1.00 50.55  ? 271 TYR D CG  1 
ATOM   11358 C  CD1 . TYR D 1 270 ? -20.000 26.861  -8.960  1.00 37.65  ? 271 TYR D CD1 1 
ATOM   11359 C  CD2 . TYR D 1 270 ? -19.380 29.046  -9.675  1.00 38.07  ? 271 TYR D CD2 1 
ATOM   11360 C  CE1 . TYR D 1 270 ? -20.717 26.680  -10.128 1.00 37.77  ? 271 TYR D CE1 1 
ATOM   11361 C  CE2 . TYR D 1 270 ? -20.095 28.874  -10.845 1.00 38.15  ? 271 TYR D CE2 1 
ATOM   11362 C  CZ  . TYR D 1 270 ? -20.763 27.690  -11.066 1.00 40.71  ? 271 TYR D CZ  1 
ATOM   11363 O  OH  . TYR D 1 270 ? -21.479 27.515  -12.228 1.00 42.33  ? 271 TYR D OH  1 
ATOM   11364 N  N   . CYS D 1 271 ? -16.099 26.449  -7.671  1.00 41.97  ? 272 CYS D N   1 
ATOM   11365 C  CA  . CYS D 1 271 ? -15.101 25.635  -8.350  1.00 41.32  ? 272 CYS D CA  1 
ATOM   11366 C  C   . CYS D 1 271 ? -14.938 24.275  -7.676  1.00 41.86  ? 272 CYS D C   1 
ATOM   11367 O  O   . CYS D 1 271 ? -14.883 23.239  -8.346  1.00 41.98  ? 272 CYS D O   1 
ATOM   11368 C  CB  . CYS D 1 271 ? -13.760 26.372  -8.382  1.00 36.98  ? 272 CYS D CB  1 
ATOM   11369 S  SG  . CYS D 1 271 ? -12.473 25.564  -9.357  1.00 62.80  ? 272 CYS D SG  1 
ATOM   11370 N  N   . ARG D 1 272 ? -14.867 24.289  -6.349  1.00 45.00  ? 273 ARG D N   1 
ATOM   11371 C  CA  . ARG D 1 272 ? -14.680 23.065  -5.581  1.00 48.05  ? 273 ARG D CA  1 
ATOM   11372 C  C   . ARG D 1 272 ? -15.843 22.100  -5.769  1.00 49.11  ? 273 ARG D C   1 
ATOM   11373 O  O   . ARG D 1 272 ? -15.630 20.905  -5.945  1.00 53.09  ? 273 ARG D O   1 
ATOM   11374 C  CB  . ARG D 1 272 ? -14.493 23.379  -4.094  1.00 52.41  ? 273 ARG D CB  1 
ATOM   11375 C  CG  . ARG D 1 272 ? -13.188 24.091  -3.781  1.00 59.36  ? 273 ARG D CG  1 
ATOM   11376 C  CD  . ARG D 1 272 ? -12.500 23.506  -2.559  1.00 66.65  ? 273 ARG D CD  1 
ATOM   11377 N  NE  . ARG D 1 272 ? -13.178 23.856  -1.315  1.00 74.85  ? 273 ARG D NE  1 
ATOM   11378 C  CZ  . ARG D 1 272 ? -13.409 23.000  -0.325  1.00 81.60  ? 273 ARG D CZ  1 
ATOM   11379 N  NH1 . ARG D 1 272 ? -14.030 23.405  0.774   1.00 84.45  ? 273 ARG D NH1 1 
ATOM   11380 N  NH2 . ARG D 1 272 ? -13.016 21.738  -0.432  1.00 83.13  ? 273 ARG D NH2 1 
ATOM   11381 N  N   . ASN D 1 273 ? -17.070 22.611  -5.736  1.00 45.81  ? 274 ASN D N   1 
ATOM   11382 C  CA  . ASN D 1 273 ? -18.230 21.752  -5.948  1.00 50.06  ? 274 ASN D CA  1 
ATOM   11383 C  C   . ASN D 1 273 ? -18.290 21.214  -7.373  1.00 36.66  ? 274 ASN D C   1 
ATOM   11384 O  O   . ASN D 1 273 ? -18.642 20.050  -7.589  1.00 38.03  ? 274 ASN D O   1 
ATOM   11385 C  CB  . ASN D 1 273 ? -19.523 22.493  -5.606  1.00 43.80  ? 274 ASN D CB  1 
ATOM   11386 C  CG  . ASN D 1 273 ? -19.922 22.320  -4.154  1.00 48.00  ? 274 ASN D CG  1 
ATOM   11387 O  OD1 . ASN D 1 273 ? -19.589 21.314  -3.527  1.00 48.44  ? 274 ASN D OD1 1 
ATOM   11388 N  ND2 . ASN D 1 273 ? -20.640 23.296  -3.613  1.00 49.22  ? 274 ASN D ND2 1 
ATOM   11389 N  N   . VAL D 1 274 ? -17.933 22.051  -8.343  1.00 36.60  ? 275 VAL D N   1 
ATOM   11390 C  CA  . VAL D 1 274 ? -17.893 21.604  -9.733  1.00 45.24  ? 275 VAL D CA  1 
ATOM   11391 C  C   . VAL D 1 274 ? -16.894 20.462  -9.923  1.00 42.70  ? 275 VAL D C   1 
ATOM   11392 O  O   . VAL D 1 274 ? -17.242 19.399  -10.445 1.00 42.94  ? 275 VAL D O   1 
ATOM   11393 C  CB  . VAL D 1 274 ? -17.534 22.756  -10.694 1.00 43.66  ? 275 VAL D CB  1 
ATOM   11394 C  CG1 . VAL D 1 274 ? -17.292 22.222  -12.099 1.00 42.24  ? 275 VAL D CG1 1 
ATOM   11395 C  CG2 . VAL D 1 274 ? -18.637 23.802  -10.704 1.00 42.91  ? 275 VAL D CG2 1 
ATOM   11396 N  N   . LEU D 1 275 ? -15.656 20.674  -9.484  1.00 43.02  ? 276 LEU D N   1 
ATOM   11397 C  CA  . LEU D 1 275 ? -14.610 19.673  -9.682  1.00 40.92  ? 276 LEU D CA  1 
ATOM   11398 C  C   . LEU D 1 275 ? -14.826 18.419  -8.833  1.00 41.72  ? 276 LEU D C   1 
ATOM   11399 O  O   . LEU D 1 275 ? -14.452 17.321  -9.245  1.00 36.62  ? 276 LEU D O   1 
ATOM   11400 C  CB  . LEU D 1 275 ? -13.234 20.273  -9.391  1.00 44.26  ? 276 LEU D CB  1 
ATOM   11401 C  CG  . LEU D 1 275 ? -12.800 21.385  -10.349 1.00 48.08  ? 276 LEU D CG  1 
ATOM   11402 C  CD1 . LEU D 1 275 ? -11.323 21.700  -10.177 1.00 51.35  ? 276 LEU D CD1 1 
ATOM   11403 C  CD2 . LEU D 1 275 ? -13.108 21.008  -11.792 1.00 48.37  ? 276 LEU D CD2 1 
ATOM   11404 N  N   . LYS D 1 276 ? -15.421 18.580  -7.655  1.00 41.10  ? 277 LYS D N   1 
ATOM   11405 C  CA  . LYS D 1 276 ? -15.785 17.431  -6.830  1.00 37.74  ? 277 LYS D CA  1 
ATOM   11406 C  C   . LYS D 1 276 ? -16.879 16.630  -7.517  1.00 41.99  ? 277 LYS D C   1 
ATOM   11407 O  O   . LYS D 1 276 ? -16.915 15.402  -7.426  1.00 41.55  ? 277 LYS D O   1 
ATOM   11408 C  CB  . LYS D 1 276 ? -16.251 17.863  -5.438  1.00 36.23  ? 277 LYS D CB  1 
ATOM   11409 C  CG  . LYS D 1 276 ? -15.128 18.115  -4.444  1.00 36.07  ? 277 LYS D CG  1 
ATOM   11410 C  CD  . LYS D 1 276 ? -15.674 18.230  -3.029  1.00 37.04  ? 277 LYS D CD  1 
ATOM   11411 C  CE  . LYS D 1 276 ? -14.567 18.491  -2.022  1.00 42.09  ? 277 LYS D CE  1 
ATOM   11412 N  NZ  . LYS D 1 276 ? -15.083 18.518  -0.625  1.00 49.40  ? 277 LYS D NZ  1 
ATOM   11413 N  N   . GLY D 1 277 ? -17.775 17.335  -8.200  1.00 38.91  ? 278 GLY D N   1 
ATOM   11414 C  CA  . GLY D 1 277 ? -18.807 16.681  -8.980  1.00 39.97  ? 278 GLY D CA  1 
ATOM   11415 C  C   . GLY D 1 277 ? -18.217 15.942  -10.166 1.00 43.63  ? 278 GLY D C   1 
ATOM   11416 O  O   . GLY D 1 277 ? -18.698 14.875  -10.546 1.00 52.56  ? 278 GLY D O   1 
ATOM   11417 N  N   . CYS D 1 278 ? -17.160 16.507  -10.744 1.00 41.28  ? 279 CYS D N   1 
ATOM   11418 C  CA  . CYS D 1 278 ? -16.545 15.940  -11.941 1.00 45.47  ? 279 CYS D CA  1 
ATOM   11419 C  C   . CYS D 1 278 ? -15.548 14.821  -11.643 1.00 47.24  ? 279 CYS D C   1 
ATOM   11420 O  O   . CYS D 1 278 ? -15.368 13.915  -12.457 1.00 48.65  ? 279 CYS D O   1 
ATOM   11421 C  CB  . CYS D 1 278 ? -15.840 17.039  -12.741 1.00 48.43  ? 279 CYS D CB  1 
ATOM   11422 S  SG  . CYS D 1 278 ? -16.947 18.231  -13.525 1.00 53.81  ? 279 CYS D SG  1 
ATOM   11423 N  N   . LEU D 1 279 ? -14.901 14.886  -10.484 1.00 46.12  ? 280 LEU D N   1 
ATOM   11424 C  CA  . LEU D 1 279 ? -13.810 13.966  -10.171 1.00 39.35  ? 280 LEU D CA  1 
ATOM   11425 C  C   . LEU D 1 279 ? -14.120 13.068  -8.975  1.00 38.70  ? 280 LEU D C   1 
ATOM   11426 O  O   . LEU D 1 279 ? -13.214 12.654  -8.252  1.00 40.41  ? 280 LEU D O   1 
ATOM   11427 C  CB  . LEU D 1 279 ? -12.525 14.753  -9.907  1.00 42.47  ? 280 LEU D CB  1 
ATOM   11428 C  CG  . LEU D 1 279 ? -12.075 15.704  -11.019 1.00 44.68  ? 280 LEU D CG  1 
ATOM   11429 C  CD1 . LEU D 1 279 ? -10.840 16.483  -10.596 1.00 44.42  ? 280 LEU D CD1 1 
ATOM   11430 C  CD2 . LEU D 1 279 ? -11.815 14.942  -12.310 1.00 36.18  ? 280 LEU D CD2 1 
ATOM   11431 N  N   . ALA D 1 280 ? -15.398 12.765  -8.776  1.00 38.31  ? 281 ALA D N   1 
ATOM   11432 C  CA  . ALA D 1 280 ? -15.835 11.969  -7.632  1.00 38.22  ? 281 ALA D CA  1 
ATOM   11433 C  C   . ALA D 1 280 ? -15.358 10.517  -7.723  1.00 39.83  ? 281 ALA D C   1 
ATOM   11434 O  O   . ALA D 1 280 ? -14.880 9.938   -6.735  1.00 43.85  ? 281 ALA D O   1 
ATOM   11435 C  CB  . ALA D 1 280 ? -17.341 12.021  -7.516  1.00 37.33  ? 281 ALA D CB  1 
ATOM   11436 N  N   . ASN D 1 281 ? -15.499 9.934   -8.910  1.00 37.32  ? 282 ASN D N   1 
ATOM   11437 C  CA  . ASN D 1 281 ? -14.997 8.590   -9.165  1.00 40.43  ? 282 ASN D CA  1 
ATOM   11438 C  C   . ASN D 1 281 ? -13.513 8.497   -8.845  1.00 43.62  ? 282 ASN D C   1 
ATOM   11439 O  O   . ASN D 1 281 ? -13.075 7.571   -8.163  1.00 47.68  ? 282 ASN D O   1 
ATOM   11440 C  CB  . ASN D 1 281 ? -15.249 8.184   -10.619 1.00 38.20  ? 282 ASN D CB  1 
ATOM   11441 C  CG  . ASN D 1 281 ? -16.706 7.869   -10.892 1.00 41.56  ? 282 ASN D CG  1 
ATOM   11442 O  OD1 . ASN D 1 281 ? -17.207 6.813   -10.505 1.00 40.97  ? 282 ASN D OD1 1 
ATOM   11443 N  ND2 . ASN D 1 281 ? -17.393 8.782   -11.568 1.00 45.56  ? 282 ASN D ND2 1 
ATOM   11444 N  N   . GLN D 1 282 ? -12.746 9.467   -9.334  1.00 43.55  ? 283 GLN D N   1 
ATOM   11445 C  CA  . GLN D 1 282 ? -11.321 9.548   -9.034  1.00 38.46  ? 283 GLN D CA  1 
ATOM   11446 C  C   . GLN D 1 282 ? -11.097 9.686   -7.535  1.00 37.66  ? 283 GLN D C   1 
ATOM   11447 O  O   . GLN D 1 282 ? -10.130 9.154   -6.992  1.00 39.77  ? 283 GLN D O   1 
ATOM   11448 C  CB  . GLN D 1 282 ? -10.673 10.725  -9.770  1.00 37.63  ? 283 GLN D CB  1 
ATOM   11449 C  CG  . GLN D 1 282 ? -10.599 10.573  -11.284 1.00 40.57  ? 283 GLN D CG  1 
ATOM   11450 C  CD  . GLN D 1 282 ? -11.918 10.863  -11.979 1.00 45.26  ? 283 GLN D CD  1 
ATOM   11451 O  OE1 . GLN D 1 282 ? -12.957 11.015  -11.336 1.00 45.23  ? 283 GLN D OE1 1 
ATOM   11452 N  NE2 . GLN D 1 282 ? -11.878 10.945  -13.304 1.00 45.31  ? 283 GLN D NE2 1 
ATOM   11453 N  N   . ALA D 1 283 ? -12.002 10.398  -6.871  1.00 35.92  ? 284 ALA D N   1 
ATOM   11454 C  CA  . ALA D 1 283 ? -11.907 10.600  -5.431  1.00 45.00  ? 284 ALA D CA  1 
ATOM   11455 C  C   . ALA D 1 283 ? -12.170 9.303   -4.670  1.00 42.22  ? 284 ALA D C   1 
ATOM   11456 O  O   . ALA D 1 283 ? -11.755 9.157   -3.520  1.00 38.92  ? 284 ALA D O   1 
ATOM   11457 C  CB  . ALA D 1 283 ? -12.874 11.685  -4.983  1.00 35.91  ? 284 ALA D CB  1 
ATOM   11458 N  N   . ASP D 1 284 ? -12.857 8.361   -5.309  1.00 36.63  ? 285 ASP D N   1 
ATOM   11459 C  CA  . ASP D 1 284 ? -13.124 7.072   -4.670  1.00 44.26  ? 285 ASP D CA  1 
ATOM   11460 C  C   . ASP D 1 284 ? -11.867 6.208   -4.502  1.00 43.25  ? 285 ASP D C   1 
ATOM   11461 O  O   . ASP D 1 284 ? -11.877 5.230   -3.754  1.00 37.34  ? 285 ASP D O   1 
ATOM   11462 C  CB  . ASP D 1 284 ? -14.180 6.297   -5.460  1.00 43.65  ? 285 ASP D CB  1 
ATOM   11463 C  CG  . ASP D 1 284 ? -15.592 6.656   -5.048  1.00 48.86  ? 285 ASP D CG  1 
ATOM   11464 O  OD1 . ASP D 1 284 ? -15.769 7.190   -3.931  1.00 49.68  ? 285 ASP D OD1 1 
ATOM   11465 O  OD2 . ASP D 1 284 ? -16.525 6.403   -5.838  1.00 49.23  ? 285 ASP D OD2 1 
ATOM   11466 N  N   . LEU D 1 285 ? -10.789 6.571   -5.192  1.00 43.48  ? 286 LEU D N   1 
ATOM   11467 C  CA  . LEU D 1 285 ? -9.529  5.830   -5.109  1.00 41.97  ? 286 LEU D CA  1 
ATOM   11468 C  C   . LEU D 1 285 ? -8.791  6.070   -3.793  1.00 42.53  ? 286 LEU D C   1 
ATOM   11469 O  O   . LEU D 1 285 ? -7.890  5.309   -3.428  1.00 40.04  ? 286 LEU D O   1 
ATOM   11470 C  CB  . LEU D 1 285 ? -8.615  6.206   -6.277  1.00 40.26  ? 286 LEU D CB  1 
ATOM   11471 C  CG  . LEU D 1 285 ? -9.049  5.794   -7.683  1.00 40.77  ? 286 LEU D CG  1 
ATOM   11472 C  CD1 . LEU D 1 285 ? -8.400  6.692   -8.724  1.00 36.23  ? 286 LEU D CD1 1 
ATOM   11473 C  CD2 . LEU D 1 285 ? -8.692  4.339   -7.936  1.00 36.89  ? 286 LEU D CD2 1 
ATOM   11474 N  N   . ASP D 1 286 ? -9.194  7.131   -3.097  1.00 35.98  ? 287 ASP D N   1 
ATOM   11475 C  CA  . ASP D 1 286 ? -8.528  7.634   -1.893  1.00 42.62  ? 287 ASP D CA  1 
ATOM   11476 C  C   . ASP D 1 286 ? -8.095  6.555   -0.895  1.00 41.44  ? 287 ASP D C   1 
ATOM   11477 O  O   . ASP D 1 286 ? -6.902  6.404   -0.610  1.00 45.95  ? 287 ASP D O   1 
ATOM   11478 C  CB  . ASP D 1 286 ? -9.454  8.635   -1.191  1.00 47.80  ? 287 ASP D CB  1 
ATOM   11479 C  CG  . ASP D 1 286 ? -8.749  9.432   -0.111  1.00 48.44  ? 287 ASP D CG  1 
ATOM   11480 O  OD1 . ASP D 1 286 ? -7.658  9.976   -0.385  1.00 49.77  ? 287 ASP D OD1 1 
ATOM   11481 O  OD2 . ASP D 1 286 ? -9.292  9.523   1.012   1.00 48.45  ? 287 ASP D OD2 1 
ATOM   11482 N  N   . ALA D 1 287 ? -9.068  5.808   -0.380  1.00 40.99  ? 288 ALA D N   1 
ATOM   11483 C  CA  . ALA D 1 287 ? -8.833  4.831   0.683   1.00 39.40  ? 288 ALA D CA  1 
ATOM   11484 C  C   . ALA D 1 287 ? -7.779  3.784   0.324   1.00 37.48  ? 288 ALA D C   1 
ATOM   11485 O  O   . ALA D 1 287 ? -6.804  3.594   1.055   1.00 42.05  ? 288 ALA D O   1 
ATOM   11486 C  CB  . ALA D 1 287 ? -10.140 4.144   1.051   1.00 38.57  ? 288 ALA D CB  1 
ATOM   11487 N  N   . GLU D 1 288 ? -7.977  3.109   -0.803  1.00 37.07  ? 289 GLU D N   1 
ATOM   11488 C  CA  . GLU D 1 288 ? -7.089  2.025   -1.205  1.00 37.12  ? 289 GLU D CA  1 
ATOM   11489 C  C   . GLU D 1 288 ? -5.735  2.544   -1.679  1.00 36.54  ? 289 GLU D C   1 
ATOM   11490 O  O   . GLU D 1 288 ? -4.717  1.864   -1.534  1.00 41.15  ? 289 GLU D O   1 
ATOM   11491 C  CB  . GLU D 1 288 ? -7.746  1.178   -2.296  1.00 37.53  ? 289 GLU D CB  1 
ATOM   11492 C  CG  . GLU D 1 288 ? -8.991  0.434   -1.830  1.00 40.27  ? 289 GLU D CG  1 
ATOM   11493 C  CD  . GLU D 1 288 ? -8.767  -0.355  -0.549  1.00 52.78  ? 289 GLU D CD  1 
ATOM   11494 O  OE1 . GLU D 1 288 ? -7.684  -0.961  -0.395  1.00 57.36  ? 289 GLU D OE1 1 
ATOM   11495 O  OE2 . GLU D 1 288 ? -9.677  -0.370  0.307   1.00 58.80  ? 289 GLU D OE2 1 
ATOM   11496 N  N   . TRP D 1 289 ? -5.731  3.745   -2.250  1.00 45.38  ? 290 TRP D N   1 
ATOM   11497 C  CA  . TRP D 1 289 ? -4.489  4.420   -2.614  1.00 44.50  ? 290 TRP D CA  1 
ATOM   11498 C  C   . TRP D 1 289 ? -3.641  4.620   -1.359  1.00 35.67  ? 290 TRP D C   1 
ATOM   11499 O  O   . TRP D 1 289 ? -2.450  4.274   -1.321  1.00 35.62  ? 290 TRP D O   1 
ATOM   11500 C  CB  . TRP D 1 289 ? -4.799  5.757   -3.296  1.00 35.44  ? 290 TRP D CB  1 
ATOM   11501 C  CG  . TRP D 1 289 ? -3.615  6.587   -3.684  1.00 35.18  ? 290 TRP D CG  1 
ATOM   11502 C  CD1 . TRP D 1 289 ? -3.143  7.693   -3.036  1.00 35.05  ? 290 TRP D CD1 1 
ATOM   11503 C  CD2 . TRP D 1 289 ? -2.770  6.402   -4.826  1.00 35.19  ? 290 TRP D CD2 1 
ATOM   11504 N  NE1 . TRP D 1 289 ? -2.051  8.199   -3.697  1.00 34.98  ? 290 TRP D NE1 1 
ATOM   11505 C  CE2 . TRP D 1 289 ? -1.801  7.425   -4.800  1.00 35.06  ? 290 TRP D CE2 1 
ATOM   11506 C  CE3 . TRP D 1 289 ? -2.734  5.466   -5.865  1.00 35.42  ? 290 TRP D CE3 1 
ATOM   11507 C  CZ2 . TRP D 1 289 ? -0.809  7.538   -5.770  1.00 35.17  ? 290 TRP D CZ2 1 
ATOM   11508 C  CZ3 . TRP D 1 289 ? -1.748  5.581   -6.827  1.00 35.51  ? 290 TRP D CZ3 1 
ATOM   11509 C  CH2 . TRP D 1 289 ? -0.798  6.609   -6.772  1.00 39.34  ? 290 TRP D CH2 1 
ATOM   11510 N  N   . ARG D 1 290 ? -4.283  5.153   -0.323  1.00 35.81  ? 291 ARG D N   1 
ATOM   11511 C  CA  . ARG D 1 290 ? -3.624  5.373   0.958   1.00 43.78  ? 291 ARG D CA  1 
ATOM   11512 C  C   . ARG D 1 290 ? -3.159  4.067   1.593   1.00 43.81  ? 291 ARG D C   1 
ATOM   11513 O  O   . ARG D 1 290 ? -2.069  4.007   2.157   1.00 50.19  ? 291 ARG D O   1 
ATOM   11514 C  CB  . ARG D 1 290 ? -4.556  6.115   1.915   1.00 36.22  ? 291 ARG D CB  1 
ATOM   11515 C  CG  . ARG D 1 290 ? -4.757  7.573   1.556   1.00 35.97  ? 291 ARG D CG  1 
ATOM   11516 C  CD  . ARG D 1 290 ? -5.830  8.212   2.413   1.00 44.75  ? 291 ARG D CD  1 
ATOM   11517 N  NE  . ARG D 1 290 ? -6.192  9.532   1.912   1.00 52.11  ? 291 ARG D NE  1 
ATOM   11518 C  CZ  . ARG D 1 290 ? -5.626  10.663  2.318   1.00 52.38  ? 291 ARG D CZ  1 
ATOM   11519 N  NH1 . ARG D 1 290 ? -4.669  10.635  3.236   1.00 51.90  ? 291 ARG D NH1 1 
ATOM   11520 N  NH2 . ARG D 1 290 ? -6.014  11.822  1.807   1.00 54.44  ? 291 ARG D NH2 1 
ATOM   11521 N  N   . ASN D 1 291 ? -3.983  3.026   1.504   1.00 43.14  ? 292 ASN D N   1 
ATOM   11522 C  CA  . ASN D 1 291 ? -3.605  1.721   2.042   1.00 41.35  ? 292 ASN D CA  1 
ATOM   11523 C  C   . ASN D 1 291 ? -2.366  1.159   1.347   1.00 40.38  ? 292 ASN D C   1 
ATOM   11524 O  O   . ASN D 1 291 ? -1.454  0.639   1.999   1.00 39.77  ? 292 ASN D O   1 
ATOM   11525 C  CB  . ASN D 1 291 ? -4.766  0.733   1.925   1.00 37.53  ? 292 ASN D CB  1 
ATOM   11526 C  CG  . ASN D 1 291 ? -5.897  1.048   2.884   1.00 45.04  ? 292 ASN D CG  1 
ATOM   11527 O  OD1 . ASN D 1 291 ? -5.671  1.573   3.975   1.00 45.74  ? 292 ASN D OD1 1 
ATOM   11528 N  ND2 . ASN D 1 291 ? -7.122  0.723   2.485   1.00 38.41  ? 292 ASN D ND2 1 
ATOM   11529 N  N   . LEU D 1 292 ? -2.339  1.273   0.022   1.00 39.84  ? 293 LEU D N   1 
ATOM   11530 C  CA  . LEU D 1 292 ? -1.189  0.841   -0.763  1.00 40.58  ? 293 LEU D CA  1 
ATOM   11531 C  C   . LEU D 1 292 ? 0.074   1.596   -0.364  1.00 41.58  ? 293 LEU D C   1 
ATOM   11532 O  O   . LEU D 1 292 ? 1.080   0.987   0.027   1.00 41.86  ? 293 LEU D O   1 
ATOM   11533 C  CB  . LEU D 1 292 ? -1.452  1.034   -2.257  1.00 40.68  ? 293 LEU D CB  1 
ATOM   11534 C  CG  . LEU D 1 292 ? -0.251  0.730   -3.156  1.00 38.81  ? 293 LEU D CG  1 
ATOM   11535 C  CD1 . LEU D 1 292 ? 0.081   -0.750  -3.113  1.00 36.61  ? 293 LEU D CD1 1 
ATOM   11536 C  CD2 . LEU D 1 292 ? -0.493  1.189   -4.585  1.00 36.16  ? 293 LEU D CD2 1 
ATOM   11537 N  N   . LEU D 1 293 ? 0.015   2.923   -0.463  1.00 44.06  ? 294 LEU D N   1 
ATOM   11538 C  CA  . LEU D 1 293 ? 1.181   3.752   -0.162  1.00 42.56  ? 294 LEU D CA  1 
ATOM   11539 C  C   . LEU D 1 293 ? 1.697   3.504   1.254   1.00 39.87  ? 294 LEU D C   1 
ATOM   11540 O  O   . LEU D 1 293 ? 2.907   3.362   1.472   1.00 36.10  ? 294 LEU D O   1 
ATOM   11541 C  CB  . LEU D 1 293 ? 0.851   5.233   -0.356  1.00 35.53  ? 294 LEU D CB  1 
ATOM   11542 C  CG  . LEU D 1 293 ? 1.210   5.823   -1.723  1.00 38.96  ? 294 LEU D CG  1 
ATOM   11543 C  CD1 . LEU D 1 293 ? 0.426   5.147   -2.838  1.00 40.76  ? 294 LEU D CD1 1 
ATOM   11544 C  CD2 . LEU D 1 293 ? 0.976   7.326   -1.738  1.00 36.80  ? 294 LEU D CD2 1 
ATOM   11545 N  N   . ASP D 1 294 ? 0.774   3.435   2.208   1.00 37.28  ? 295 ASP D N   1 
ATOM   11546 C  CA  . ASP D 1 294 ? 1.127   3.135   3.590   1.00 48.15  ? 295 ASP D CA  1 
ATOM   11547 C  C   . ASP D 1 294 ? 1.801   1.774   3.703   1.00 43.25  ? 295 ASP D C   1 
ATOM   11548 O  O   . ASP D 1 294 ? 2.765   1.617   4.449   1.00 40.49  ? 295 ASP D O   1 
ATOM   11549 C  CB  . ASP D 1 294 ? -0.107  3.181   4.493   1.00 54.22  ? 295 ASP D CB  1 
ATOM   11550 C  CG  . ASP D 1 294 ? -0.408  4.579   4.996   1.00 63.33  ? 295 ASP D CG  1 
ATOM   11551 O  OD1 . ASP D 1 294 ? 0.527   5.404   5.057   1.00 66.60  ? 295 ASP D OD1 1 
ATOM   11552 O  OD2 . ASP D 1 294 ? -1.579  4.850   5.336   1.00 67.46  ? 295 ASP D OD2 1 
ATOM   11553 N  N   . SER D 1 295 ? 1.296   0.794   2.957   1.00 45.80  ? 296 SER D N   1 
ATOM   11554 C  CA  . SER D 1 295 ? 1.874   -0.546  2.992   1.00 37.08  ? 296 SER D CA  1 
ATOM   11555 C  C   . SER D 1 295 ? 3.289   -0.564  2.413   1.00 36.90  ? 296 SER D C   1 
ATOM   11556 O  O   . SER D 1 295 ? 4.132   -1.345  2.853   1.00 37.16  ? 296 SER D O   1 
ATOM   11557 C  CB  . SER D 1 295 ? 0.984   -1.539  2.242   1.00 44.31  ? 296 SER D CB  1 
ATOM   11558 O  OG  . SER D 1 295 ? 0.802   -1.145  0.895   1.00 50.24  ? 296 SER D OG  1 
ATOM   11559 N  N   . MET D 1 296 ? 3.550   0.295   1.431   1.00 36.54  ? 297 MET D N   1 
ATOM   11560 C  CA  . MET D 1 296 ? 4.893   0.402   0.858   1.00 40.50  ? 297 MET D CA  1 
ATOM   11561 C  C   . MET D 1 296 ? 5.865   1.071   1.836   1.00 43.70  ? 297 MET D C   1 
ATOM   11562 O  O   . MET D 1 296 ? 6.952   0.539   2.136   1.00 36.90  ? 297 MET D O   1 
ATOM   11563 C  CB  . MET D 1 296 ? 4.851   1.178   -0.460  1.00 36.24  ? 297 MET D CB  1 
ATOM   11564 C  CG  . MET D 1 296 ? 4.067   0.478   -1.557  1.00 36.24  ? 297 MET D CG  1 
ATOM   11565 S  SD  . MET D 1 296 ? 4.240   1.243   -3.181  1.00 58.57  ? 297 MET D SD  1 
ATOM   11566 C  CE  . MET D 1 296 ? 3.118   2.628   -3.034  1.00 50.13  ? 297 MET D CE  1 
ATOM   11567 N  N   . VAL D 1 297 ? 5.461   2.236   2.337   1.00 36.60  ? 298 VAL D N   1 
ATOM   11568 C  CA  . VAL D 1 297 ? 6.241   2.949   3.344   1.00 46.86  ? 298 VAL D CA  1 
ATOM   11569 C  C   . VAL D 1 297 ? 6.537   2.026   4.525   1.00 49.49  ? 298 VAL D C   1 
ATOM   11570 O  O   . VAL D 1 297 ? 7.600   2.104   5.147   1.00 46.93  ? 298 VAL D O   1 
ATOM   11571 C  CB  . VAL D 1 297 ? 5.507   4.216   3.831   1.00 41.80  ? 298 VAL D CB  1 
ATOM   11572 C  CG1 . VAL D 1 297 ? 6.273   4.888   4.960   1.00 39.97  ? 298 VAL D CG1 1 
ATOM   11573 C  CG2 . VAL D 1 297 ? 5.304   5.182   2.675   1.00 36.59  ? 298 VAL D CG2 1 
ATOM   11574 N  N   . LEU D 1 298 ? 5.599   1.127   4.806   1.00 50.28  ? 299 LEU D N   1 
ATOM   11575 C  CA  . LEU D 1 298 ? 5.778   0.144   5.863   1.00 50.45  ? 299 LEU D CA  1 
ATOM   11576 C  C   . LEU D 1 298 ? 6.768   -0.948  5.464   1.00 48.53  ? 299 LEU D C   1 
ATOM   11577 O  O   . LEU D 1 298 ? 7.600   -1.351  6.274   1.00 44.51  ? 299 LEU D O   1 
ATOM   11578 C  CB  . LEU D 1 298 ? 4.438   -0.482  6.245   1.00 58.14  ? 299 LEU D CB  1 
ATOM   11579 C  CG  . LEU D 1 298 ? 4.237   -0.681  7.748   1.00 66.26  ? 299 LEU D CG  1 
ATOM   11580 C  CD1 . LEU D 1 298 ? 4.258   0.662   8.459   1.00 66.24  ? 299 LEU D CD1 1 
ATOM   11581 C  CD2 . LEU D 1 298 ? 2.942   -1.424  8.030   1.00 73.35  ? 299 LEU D CD2 1 
ATOM   11582 N  N   . ILE D 1 299 ? 6.687   -1.428  4.223   1.00 41.47  ? 300 ILE D N   1 
ATOM   11583 C  CA  . ILE D 1 299 ? 7.578   -2.502  3.783   1.00 42.34  ? 300 ILE D CA  1 
ATOM   11584 C  C   . ILE D 1 299 ? 9.016   -2.005  3.696   1.00 42.56  ? 300 ILE D C   1 
ATOM   11585 O  O   . ILE D 1 299 ? 9.953   -2.805  3.706   1.00 43.37  ? 300 ILE D O   1 
ATOM   11586 C  CB  . ILE D 1 299 ? 7.161   -3.105  2.416   1.00 37.57  ? 300 ILE D CB  1 
ATOM   11587 C  CG1 . ILE D 1 299 ? 7.704   -4.527  2.270   1.00 42.37  ? 300 ILE D CG1 1 
ATOM   11588 C  CG2 . ILE D 1 299 ? 7.681   -2.275  1.263   1.00 37.28  ? 300 ILE D CG2 1 
ATOM   11589 C  CD1 . ILE D 1 299 ? 7.089   -5.519  3.214   1.00 42.09  ? 300 ILE D CD1 1 
ATOM   11590 N  N   . THR D 1 300 ? 9.199   -0.688  3.625   1.00 37.69  ? 301 THR D N   1 
ATOM   11591 C  CA  . THR D 1 300 ? 10.558  -0.144  3.679   1.00 42.83  ? 301 THR D CA  1 
ATOM   11592 C  C   . THR D 1 300 ? 11.249  -0.419  5.023   1.00 40.92  ? 301 THR D C   1 
ATOM   11593 O  O   . THR D 1 300 ? 12.473  -0.330  5.123   1.00 41.00  ? 301 THR D O   1 
ATOM   11594 C  CB  . THR D 1 300 ? 10.583  1.374   3.419   1.00 41.59  ? 301 THR D CB  1 
ATOM   11595 O  OG1 . THR D 1 300 ? 9.773   2.045   4.392   1.00 51.54  ? 301 THR D OG1 1 
ATOM   11596 C  CG2 . THR D 1 300 ? 10.070  1.684   2.022   1.00 44.95  ? 301 THR D CG2 1 
ATOM   11597 N  N   . ASP D 1 301 ? 10.468  -0.755  6.049   1.00 43.06  ? 302 ASP D N   1 
ATOM   11598 C  CA  . ASP D 1 301 ? 11.018  -1.065  7.370   1.00 43.39  ? 302 ASP D CA  1 
ATOM   11599 C  C   . ASP D 1 301 ? 11.924  -2.290  7.339   1.00 43.95  ? 302 ASP D C   1 
ATOM   11600 O  O   . ASP D 1 301 ? 12.851  -2.406  8.141   1.00 41.34  ? 302 ASP D O   1 
ATOM   11601 C  CB  . ASP D 1 301 ? 9.897   -1.293  8.389   1.00 51.85  ? 302 ASP D CB  1 
ATOM   11602 C  CG  . ASP D 1 301 ? 9.293   -0.000  8.897   1.00 62.70  ? 302 ASP D CG  1 
ATOM   11603 O  OD1 . ASP D 1 301 ? 10.023  1.011   8.979   1.00 63.43  ? 302 ASP D OD1 1 
ATOM   11604 O  OD2 . ASP D 1 301 ? 8.086   0.004   9.220   1.00 63.37  ? 302 ASP D OD2 1 
ATOM   11605 N  N   . LYS D 1 302 ? 11.650  -3.204  6.414   1.00 44.70  ? 303 LYS D N   1 
ATOM   11606 C  CA  . LYS D 1 302 ? 12.384  -4.462  6.343   1.00 44.64  ? 303 LYS D CA  1 
ATOM   11607 C  C   . LYS D 1 302 ? 13.594  -4.370  5.418   1.00 43.95  ? 303 LYS D C   1 
ATOM   11608 O  O   . LYS D 1 302 ? 14.125  -5.388  4.975   1.00 45.45  ? 303 LYS D O   1 
ATOM   11609 C  CB  . LYS D 1 302 ? 11.458  -5.591  5.886   1.00 39.36  ? 303 LYS D CB  1 
ATOM   11610 C  CG  . LYS D 1 302 ? 10.249  -5.797  6.786   1.00 43.36  ? 303 LYS D CG  1 
ATOM   11611 C  CD  . LYS D 1 302 ? 10.645  -5.759  8.256   1.00 49.51  ? 303 LYS D CD  1 
ATOM   11612 C  CE  . LYS D 1 302 ? 9.497   -6.184  9.154   1.00 51.54  ? 303 LYS D CE  1 
ATOM   11613 N  NZ  . LYS D 1 302 ? 9.142   -7.614  8.947   1.00 55.06  ? 303 LYS D NZ  1 
ATOM   11614 N  N   . PHE D 1 303 ? 14.027  -3.148  5.132   1.00 45.78  ? 304 PHE D N   1 
ATOM   11615 C  CA  . PHE D 1 303 ? 15.222  -2.934  4.323   1.00 41.55  ? 304 PHE D CA  1 
ATOM   11616 C  C   . PHE D 1 303 ? 16.459  -2.918  5.214   1.00 40.80  ? 304 PHE D C   1 
ATOM   11617 O  O   . PHE D 1 303 ? 17.566  -3.210  4.764   1.00 40.79  ? 304 PHE D O   1 
ATOM   11618 C  CB  . PHE D 1 303 ? 15.129  -1.623  3.534   1.00 44.16  ? 304 PHE D CB  1 
ATOM   11619 C  CG  . PHE D 1 303 ? 14.152  -1.660  2.388   1.00 46.41  ? 304 PHE D CG  1 
ATOM   11620 C  CD1 . PHE D 1 303 ? 13.394  -2.790  2.130   1.00 48.87  ? 304 PHE D CD1 1 
ATOM   11621 C  CD2 . PHE D 1 303 ? 14.000  -0.557  1.563   1.00 51.37  ? 304 PHE D CD2 1 
ATOM   11622 C  CE1 . PHE D 1 303 ? 12.499  -2.819  1.076   1.00 48.44  ? 304 PHE D CE1 1 
ATOM   11623 C  CE2 . PHE D 1 303 ? 13.107  -0.579  0.506   1.00 51.11  ? 304 PHE D CE2 1 
ATOM   11624 C  CZ  . PHE D 1 303 ? 12.356  -1.712  0.263   1.00 50.08  ? 304 PHE D CZ  1 
ATOM   11625 N  N   . TRP D 1 304 ? 16.257  -2.578  6.483   1.00 42.48  ? 305 TRP D N   1 
ATOM   11626 C  CA  . TRP D 1 304 ? 17.358  -2.414  7.425   1.00 46.81  ? 305 TRP D CA  1 
ATOM   11627 C  C   . TRP D 1 304 ? 17.547  -3.643  8.308   1.00 53.17  ? 305 TRP D C   1 
ATOM   11628 O  O   . TRP D 1 304 ? 16.707  -4.542  8.328   1.00 49.46  ? 305 TRP D O   1 
ATOM   11629 C  CB  . TRP D 1 304 ? 17.122  -1.183  8.301   1.00 49.19  ? 305 TRP D CB  1 
ATOM   11630 C  CG  . TRP D 1 304 ? 16.340  -0.112  7.614   1.00 55.54  ? 305 TRP D CG  1 
ATOM   11631 C  CD1 . TRP D 1 304 ? 15.040  0.231   7.848   1.00 56.29  ? 305 TRP D CD1 1 
ATOM   11632 C  CD2 . TRP D 1 304 ? 16.800  0.748   6.567   1.00 58.62  ? 305 TRP D CD2 1 
ATOM   11633 N  NE1 . TRP D 1 304 ? 14.665  1.257   7.016   1.00 58.74  ? 305 TRP D NE1 1 
ATOM   11634 C  CE2 . TRP D 1 304 ? 15.728  1.593   6.219   1.00 61.70  ? 305 TRP D CE2 1 
ATOM   11635 C  CE3 . TRP D 1 304 ? 18.016  0.888   5.891   1.00 64.07  ? 305 TRP D CE3 1 
ATOM   11636 C  CZ2 . TRP D 1 304 ? 15.835  2.564   5.227   1.00 65.48  ? 305 TRP D CZ2 1 
ATOM   11637 C  CZ3 . TRP D 1 304 ? 18.120  1.853   4.906   1.00 67.21  ? 305 TRP D CZ3 1 
ATOM   11638 C  CH2 . TRP D 1 304 ? 17.036  2.678   4.583   1.00 64.94  ? 305 TRP D CH2 1 
ATOM   11639 N  N   . GLY D 1 305 ? 18.653  -3.666  9.043   1.00 54.18  ? 306 GLY D N   1 
ATOM   11640 C  CA  . GLY D 1 305 ? 18.952  -4.765  9.941   1.00 60.41  ? 306 GLY D CA  1 
ATOM   11641 C  C   . GLY D 1 305 ? 19.814  -5.825  9.288   1.00 62.72  ? 306 GLY D C   1 
ATOM   11642 O  O   . GLY D 1 305 ? 20.072  -5.774  8.085   1.00 64.40  ? 306 GLY D O   1 
ATOM   11643 N  N   . THR D 1 306 ? 20.264  -6.788  10.087  1.00 69.12  ? 307 THR D N   1 
ATOM   11644 C  CA  . THR D 1 306 ? 21.080  -7.887  9.586   1.00 70.81  ? 307 THR D CA  1 
ATOM   11645 C  C   . THR D 1 306 ? 20.262  -8.786  8.666   1.00 69.08  ? 307 THR D C   1 
ATOM   11646 O  O   . THR D 1 306 ? 20.804  -9.443  7.776   1.00 68.35  ? 307 THR D O   1 
ATOM   11647 C  CB  . THR D 1 306 ? 21.658  -8.730  10.737  1.00 75.65  ? 307 THR D CB  1 
ATOM   11648 O  OG1 . THR D 1 306 ? 20.594  -9.411  11.414  1.00 76.39  ? 307 THR D OG1 1 
ATOM   11649 C  CG2 . THR D 1 306 ? 22.402  -7.844  11.725  1.00 77.40  ? 307 THR D CG2 1 
ATOM   11650 N  N   . SER D 1 307 ? 18.953  -8.808  8.891   1.00 64.83  ? 308 SER D N   1 
ATOM   11651 C  CA  . SER D 1 307 ? 18.036  -9.585  8.068   1.00 61.21  ? 308 SER D CA  1 
ATOM   11652 C  C   . SER D 1 307 ? 17.462  -8.730  6.943   1.00 52.38  ? 308 SER D C   1 
ATOM   11653 O  O   . SER D 1 307 ? 16.636  -9.193  6.156   1.00 51.46  ? 308 SER D O   1 
ATOM   11654 C  CB  . SER D 1 307 ? 16.906  -10.159 8.926   1.00 63.51  ? 308 SER D CB  1 
ATOM   11655 O  OG  . SER D 1 307 ? 16.210  -11.185 8.241   1.00 63.71  ? 308 SER D OG  1 
ATOM   11656 N  N   . GLY D 1 308 ? 17.912  -7.481  6.875   1.00 52.91  ? 309 GLY D N   1 
ATOM   11657 C  CA  . GLY D 1 308 ? 17.393  -6.520  5.918   1.00 50.26  ? 309 GLY D CA  1 
ATOM   11658 C  C   . GLY D 1 308 ? 17.678  -6.844  4.465   1.00 48.41  ? 309 GLY D C   1 
ATOM   11659 O  O   . GLY D 1 308 ? 18.481  -7.722  4.156   1.00 48.94  ? 309 GLY D O   1 
ATOM   11660 N  N   . VAL D 1 309 ? 17.012  -6.119  3.572   1.00 53.56  ? 310 VAL D N   1 
ATOM   11661 C  CA  . VAL D 1 309 ? 17.145  -6.334  2.135   1.00 53.90  ? 310 VAL D CA  1 
ATOM   11662 C  C   . VAL D 1 309 ? 18.569  -6.082  1.647   1.00 51.00  ? 310 VAL D C   1 
ATOM   11663 O  O   . VAL D 1 309 ? 19.182  -6.953  1.027   1.00 53.87  ? 310 VAL D O   1 
ATOM   11664 C  CB  . VAL D 1 309 ? 16.168  -5.434  1.348   1.00 48.19  ? 310 VAL D CB  1 
ATOM   11665 C  CG1 . VAL D 1 309 ? 16.563  -5.354  -0.118  1.00 43.62  ? 310 VAL D CG1 1 
ATOM   11666 C  CG2 . VAL D 1 309 ? 14.745  -5.949  1.496   1.00 49.66  ? 310 VAL D CG2 1 
ATOM   11667 N  N   . GLU D 1 310 ? 19.094  -4.894  1.935   1.00 52.29  ? 311 GLU D N   1 
ATOM   11668 C  CA  . GLU D 1 310 ? 20.434  -4.525  1.491   1.00 57.20  ? 311 GLU D CA  1 
ATOM   11669 C  C   . GLU D 1 310 ? 21.489  -5.447  2.089   1.00 54.41  ? 311 GLU D C   1 
ATOM   11670 O  O   . GLU D 1 310 ? 22.456  -5.816  1.422   1.00 57.99  ? 311 GLU D O   1 
ATOM   11671 C  CB  . GLU D 1 310 ? 20.745  -3.072  1.858   1.00 63.27  ? 311 GLU D CB  1 
ATOM   11672 C  CG  . GLU D 1 310 ? 21.556  -2.327  0.806   1.00 72.62  ? 311 GLU D CG  1 
ATOM   11673 C  CD  . GLU D 1 310 ? 22.050  -0.977  1.288   1.00 81.11  ? 311 GLU D CD  1 
ATOM   11674 O  OE1 . GLU D 1 310 ? 21.933  -0.695  2.499   1.00 83.14  ? 311 GLU D OE1 1 
ATOM   11675 O  OE2 . GLU D 1 310 ? 22.550  -0.194  0.452   1.00 83.23  ? 311 GLU D OE2 1 
ATOM   11676 N  N   . SER D 1 311 ? 21.290  -5.822  3.347   1.00 50.96  ? 312 SER D N   1 
ATOM   11677 C  CA  . SER D 1 311 ? 22.247  -6.661  4.056   1.00 52.30  ? 312 SER D CA  1 
ATOM   11678 C  C   . SER D 1 311 ? 22.283  -8.086  3.513   1.00 51.08  ? 312 SER D C   1 
ATOM   11679 O  O   . SER D 1 311 ? 23.346  -8.695  3.436   1.00 52.82  ? 312 SER D O   1 
ATOM   11680 C  CB  . SER D 1 311 ? 21.927  -6.685  5.552   1.00 52.84  ? 312 SER D CB  1 
ATOM   11681 O  OG  . SER D 1 311 ? 22.971  -7.296  6.286   1.00 56.50  ? 312 SER D OG  1 
ATOM   11682 N  N   . VAL D 1 312 ? 21.123  -8.616  3.134   1.00 51.14  ? 313 VAL D N   1 
ATOM   11683 C  CA  . VAL D 1 312 ? 21.035  -10.002 2.682   1.00 51.49  ? 313 VAL D CA  1 
ATOM   11684 C  C   . VAL D 1 312 ? 21.325  -10.163 1.191   1.00 49.26  ? 313 VAL D C   1 
ATOM   11685 O  O   . VAL D 1 312 ? 22.152  -10.991 0.803   1.00 47.75  ? 313 VAL D O   1 
ATOM   11686 C  CB  . VAL D 1 312 ? 19.644  -10.603 2.982   1.00 48.34  ? 313 VAL D CB  1 
ATOM   11687 C  CG1 . VAL D 1 312 ? 19.482  -11.950 2.291   1.00 44.62  ? 313 VAL D CG1 1 
ATOM   11688 C  CG2 . VAL D 1 312 ? 19.442  -10.745 4.483   1.00 50.91  ? 313 VAL D CG2 1 
ATOM   11689 N  N   . ILE D 1 313 ? 20.648  -9.374  0.361   1.00 43.78  ? 314 ILE D N   1 
ATOM   11690 C  CA  . ILE D 1 313 ? 20.752  -9.515  -1.091  1.00 42.36  ? 314 ILE D CA  1 
ATOM   11691 C  C   . ILE D 1 313 ? 22.186  -9.319  -1.591  1.00 51.74  ? 314 ILE D C   1 
ATOM   11692 O  O   . ILE D 1 313 ? 22.625  -9.994  -2.524  1.00 51.90  ? 314 ILE D O   1 
ATOM   11693 C  CB  . ILE D 1 313 ? 19.811  -8.523  -1.815  1.00 47.24  ? 314 ILE D CB  1 
ATOM   11694 C  CG1 . ILE D 1 313 ? 18.353  -8.816  -1.450  1.00 47.57  ? 314 ILE D CG1 1 
ATOM   11695 C  CG2 . ILE D 1 313 ? 19.993  -8.599  -3.325  1.00 42.29  ? 314 ILE D CG2 1 
ATOM   11696 C  CD1 . ILE D 1 313 ? 17.344  -8.106  -2.328  1.00 40.90  ? 314 ILE D CD1 1 
ATOM   11697 N  N   . GLY D 1 314 ? 22.922  -8.414  -0.955  1.00 53.56  ? 315 GLY D N   1 
ATOM   11698 C  CA  . GLY D 1 314 ? 24.290  -8.142  -1.358  1.00 48.39  ? 315 GLY D CA  1 
ATOM   11699 C  C   . GLY D 1 314 ? 25.334  -8.928  -0.584  1.00 50.86  ? 315 GLY D C   1 
ATOM   11700 O  O   . GLY D 1 314 ? 26.502  -8.542  -0.555  1.00 49.43  ? 315 GLY D O   1 
ATOM   11701 N  N   . SER D 1 315 ? 24.924  -10.034 0.034   1.00 54.17  ? 316 SER D N   1 
ATOM   11702 C  CA  . SER D 1 315 ? 25.836  -10.820 0.864   1.00 51.21  ? 316 SER D CA  1 
ATOM   11703 C  C   . SER D 1 315 ? 25.633  -12.330 0.744   1.00 56.43  ? 316 SER D C   1 
ATOM   11704 O  O   . SER D 1 315 ? 26.137  -13.088 1.572   1.00 55.69  ? 316 SER D O   1 
ATOM   11705 C  CB  . SER D 1 315 ? 25.693  -10.417 2.332   1.00 44.70  ? 316 SER D CB  1 
ATOM   11706 O  OG  . SER D 1 315 ? 25.889  -9.025  2.508   1.00 44.69  ? 316 SER D OG  1 
ATOM   11707 N  N   . VAL D 1 316 ? 24.896  -12.758 -0.277  1.00 54.68  ? 317 VAL D N   1 
ATOM   11708 C  CA  . VAL D 1 316 ? 24.633  -14.178 -0.518  1.00 54.46  ? 317 VAL D CA  1 
ATOM   11709 C  C   . VAL D 1 316 ? 25.923  -15.003 -0.534  1.00 55.01  ? 317 VAL D C   1 
ATOM   11710 O  O   . VAL D 1 316 ? 25.994  -16.116 0.016   1.00 57.55  ? 317 VAL D O   1 
ATOM   11711 C  CB  . VAL D 1 316 ? 23.895  -14.378 -1.856  1.00 54.38  ? 317 VAL D CB  1 
ATOM   11712 C  CG1 . VAL D 1 316 ? 23.427  -15.816 -1.998  1.00 54.24  ? 317 VAL D CG1 1 
ATOM   11713 C  CG2 . VAL D 1 316 ? 22.719  -13.417 -1.960  1.00 52.49  ? 317 VAL D CG2 1 
ATOM   11714 N  N   . HIS D 1 317 ? 26.946  -14.428 -1.157  1.00 54.41  ? 318 HIS D N   1 
ATOM   11715 C  CA  . HIS D 1 317 ? 28.247  -15.067 -1.290  1.00 56.76  ? 318 HIS D CA  1 
ATOM   11716 C  C   . HIS D 1 317 ? 28.877  -15.382 0.064   1.00 59.24  ? 318 HIS D C   1 
ATOM   11717 O  O   . HIS D 1 317 ? 29.641  -16.335 0.186   1.00 68.26  ? 318 HIS D O   1 
ATOM   11718 C  CB  . HIS D 1 317 ? 29.187  -14.179 -2.108  1.00 58.73  ? 318 HIS D CB  1 
ATOM   11719 C  CG  . HIS D 1 317 ? 29.477  -12.858 -1.467  1.00 58.15  ? 318 HIS D CG  1 
ATOM   11720 N  ND1 . HIS D 1 317 ? 28.810  -11.702 -1.810  1.00 60.65  ? 318 HIS D ND1 1 
ATOM   11721 C  CD2 . HIS D 1 317 ? 30.365  -12.508 -0.507  1.00 59.96  ? 318 HIS D CD2 1 
ATOM   11722 C  CE1 . HIS D 1 317 ? 29.272  -10.698 -1.087  1.00 60.21  ? 318 HIS D CE1 1 
ATOM   11723 N  NE2 . HIS D 1 317 ? 30.216  -11.160 -0.288  1.00 60.49  ? 318 HIS D NE2 1 
ATOM   11724 N  N   . THR D 1 318 ? 28.561  -14.579 1.075   1.00 59.23  ? 319 THR D N   1 
ATOM   11725 C  CA  . THR D 1 318 ? 29.097  -14.808 2.413   1.00 58.78  ? 319 THR D CA  1 
ATOM   11726 C  C   . THR D 1 318 ? 28.510  -16.076 3.018   1.00 54.23  ? 319 THR D C   1 
ATOM   11727 O  O   . THR D 1 318 ? 29.218  -16.852 3.658   1.00 58.84  ? 319 THR D O   1 
ATOM   11728 C  CB  . THR D 1 318 ? 28.822  -13.621 3.355   1.00 54.86  ? 319 THR D CB  1 
ATOM   11729 O  OG1 . THR D 1 318 ? 27.417  -13.345 3.386   1.00 56.47  ? 319 THR D OG1 1 
ATOM   11730 C  CG2 . THR D 1 318 ? 29.567  -12.383 2.884   1.00 54.71  ? 319 THR D CG2 1 
ATOM   11731 N  N   . TRP D 1 319 ? 27.213  -16.285 2.812   1.00 54.50  ? 320 TRP D N   1 
ATOM   11732 C  CA  . TRP D 1 319 ? 26.564  -17.505 3.275   1.00 56.91  ? 320 TRP D CA  1 
ATOM   11733 C  C   . TRP D 1 319 ? 27.058  -18.708 2.485   1.00 56.81  ? 320 TRP D C   1 
ATOM   11734 O  O   . TRP D 1 319 ? 27.289  -19.778 3.055   1.00 61.20  ? 320 TRP D O   1 
ATOM   11735 C  CB  . TRP D 1 319 ? 25.042  -17.392 3.170   1.00 61.99  ? 320 TRP D CB  1 
ATOM   11736 C  CG  . TRP D 1 319 ? 24.424  -16.630 4.299   1.00 68.68  ? 320 TRP D CG  1 
ATOM   11737 C  CD1 . TRP D 1 319 ? 24.290  -17.046 5.592   1.00 69.82  ? 320 TRP D CD1 1 
ATOM   11738 C  CD2 . TRP D 1 319 ? 23.849  -15.320 4.238   1.00 74.40  ? 320 TRP D CD2 1 
ATOM   11739 N  NE1 . TRP D 1 319 ? 23.671  -16.075 6.341   1.00 72.39  ? 320 TRP D NE1 1 
ATOM   11740 C  CE2 . TRP D 1 319 ? 23.389  -15.005 5.533   1.00 76.39  ? 320 TRP D CE2 1 
ATOM   11741 C  CE3 . TRP D 1 319 ? 23.679  -14.382 3.215   1.00 78.02  ? 320 TRP D CE3 1 
ATOM   11742 C  CZ2 . TRP D 1 319 ? 22.771  -13.793 5.831   1.00 78.79  ? 320 TRP D CZ2 1 
ATOM   11743 C  CZ3 . TRP D 1 319 ? 23.065  -13.179 3.513   1.00 80.98  ? 320 TRP D CZ3 1 
ATOM   11744 C  CH2 . TRP D 1 319 ? 22.619  -12.895 4.810   1.00 80.54  ? 320 TRP D CH2 1 
ATOM   11745 N  N   . LEU D 1 320 ? 27.218  -18.532 1.175   1.00 52.45  ? 321 LEU D N   1 
ATOM   11746 C  CA  . LEU D 1 320 ? 27.770  -19.597 0.338   1.00 57.75  ? 321 LEU D CA  1 
ATOM   11747 C  C   . LEU D 1 320 ? 29.145  -20.044 0.851   1.00 56.64  ? 321 LEU D C   1 
ATOM   11748 O  O   . LEU D 1 320 ? 29.402  -21.240 1.060   1.00 55.52  ? 321 LEU D O   1 
ATOM   11749 C  CB  . LEU D 1 320 ? 27.874  -19.132 -1.117  1.00 52.91  ? 321 LEU D CB  1 
ATOM   11750 C  CG  . LEU D 1 320 ? 26.555  -18.755 -1.797  1.00 52.50  ? 321 LEU D CG  1 
ATOM   11751 C  CD1 . LEU D 1 320 ? 26.790  -18.295 -3.227  1.00 54.54  ? 321 LEU D CD1 1 
ATOM   11752 C  CD2 . LEU D 1 320 ? 25.582  -19.920 -1.763  1.00 49.23  ? 321 LEU D CD2 1 
ATOM   11753 N  N   . ALA D 1 321 ? 30.014  -19.062 1.068   1.00 54.27  ? 322 ALA D N   1 
ATOM   11754 C  CA  . ALA D 1 321 ? 31.367  -19.294 1.554   1.00 56.70  ? 322 ALA D CA  1 
ATOM   11755 C  C   . ALA D 1 321 ? 31.365  -19.922 2.942   1.00 59.39  ? 322 ALA D C   1 
ATOM   11756 O  O   . ALA D 1 321 ? 32.190  -20.782 3.244   1.00 58.65  ? 322 ALA D O   1 
ATOM   11757 C  CB  . ALA D 1 321 ? 32.148  -17.989 1.569   1.00 55.26  ? 322 ALA D CB  1 
ATOM   11758 N  N   . GLU D 1 322 ? 30.436  -19.480 3.784   1.00 62.20  ? 323 GLU D N   1 
ATOM   11759 C  CA  . GLU D 1 322 ? 30.303  -20.019 5.131   1.00 63.89  ? 323 GLU D CA  1 
ATOM   11760 C  C   . GLU D 1 322 ? 29.915  -21.493 5.066   1.00 69.63  ? 323 GLU D C   1 
ATOM   11761 O  O   . GLU D 1 322 ? 30.371  -22.306 5.873   1.00 68.46  ? 323 GLU D O   1 
ATOM   11762 C  CB  . GLU D 1 322 ? 29.268  -19.222 5.926   1.00 66.05  ? 323 GLU D CB  1 
ATOM   11763 C  CG  . GLU D 1 322 ? 29.438  -19.292 7.434   1.00 72.02  ? 323 GLU D CG  1 
ATOM   11764 C  CD  . GLU D 1 322 ? 28.659  -18.206 8.155   1.00 80.18  ? 323 GLU D CD  1 
ATOM   11765 O  OE1 . GLU D 1 322 ? 27.989  -17.402 7.473   1.00 81.34  ? 323 GLU D OE1 1 
ATOM   11766 O  OE2 . GLU D 1 322 ? 28.719  -18.154 9.401   1.00 83.32  ? 323 GLU D OE2 1 
ATOM   11767 N  N   . ALA D 1 323 ? 29.077  -21.827 4.089   1.00 68.75  ? 324 ALA D N   1 
ATOM   11768 C  CA  . ALA D 1 323 ? 28.666  -23.208 3.869   1.00 65.54  ? 324 ALA D CA  1 
ATOM   11769 C  C   . ALA D 1 323 ? 29.839  -24.069 3.407   1.00 62.57  ? 324 ALA D C   1 
ATOM   11770 O  O   . ALA D 1 323 ? 30.099  -25.137 3.975   1.00 58.55  ? 324 ALA D O   1 
ATOM   11771 C  CB  . ALA D 1 323 ? 27.539  -23.267 2.855   1.00 66.43  ? 324 ALA D CB  1 
ATOM   11772 N  N   . ILE D 1 324 ? 30.541  -23.603 2.375   1.00 61.01  ? 325 ILE D N   1 
ATOM   11773 C  CA  . ILE D 1 324 ? 31.701  -24.328 1.856   1.00 61.41  ? 325 ILE D CA  1 
ATOM   11774 C  C   . ILE D 1 324 ? 32.740  -24.564 2.955   1.00 61.45  ? 325 ILE D C   1 
ATOM   11775 O  O   . ILE D 1 324 ? 33.277  -25.669 3.100   1.00 61.64  ? 325 ILE D O   1 
ATOM   11776 C  CB  . ILE D 1 324 ? 32.363  -23.576 0.685   1.00 61.36  ? 325 ILE D CB  1 
ATOM   11777 C  CG1 . ILE D 1 324 ? 31.355  -23.352 -0.444  1.00 64.28  ? 325 ILE D CG1 1 
ATOM   11778 C  CG2 . ILE D 1 324 ? 33.569  -24.344 0.171   1.00 62.12  ? 325 ILE D CG2 1 
ATOM   11779 C  CD1 . ILE D 1 324 ? 31.894  -22.519 -1.588  1.00 64.67  ? 325 ILE D CD1 1 
ATOM   11780 N  N   . ASN D 1 325 ? 33.005  -23.518 3.731   1.00 64.85  ? 326 ASN D N   1 
ATOM   11781 C  CA  . ASN D 1 325 ? 33.906  -23.609 4.872   1.00 67.54  ? 326 ASN D CA  1 
ATOM   11782 C  C   . ASN D 1 325 ? 33.433  -24.642 5.886   1.00 67.63  ? 326 ASN D C   1 
ATOM   11783 O  O   . ASN D 1 325 ? 34.217  -25.469 6.352   1.00 70.82  ? 326 ASN D O   1 
ATOM   11784 C  CB  . ASN D 1 325 ? 34.044  -22.248 5.554   1.00 66.27  ? 326 ASN D CB  1 
ATOM   11785 C  CG  . ASN D 1 325 ? 34.876  -22.314 6.818   1.00 67.41  ? 326 ASN D CG  1 
ATOM   11786 O  OD1 . ASN D 1 325 ? 35.931  -22.948 6.849   1.00 70.60  ? 326 ASN D OD1 1 
ATOM   11787 N  ND2 . ASN D 1 325 ? 34.399  -21.666 7.875   1.00 67.75  ? 326 ASN D ND2 1 
ATOM   11788 N  N   . ALA D 1 326 ? 32.147  -24.581 6.223   1.00 71.17  ? 327 ALA D N   1 
ATOM   11789 C  CA  . ALA D 1 326 ? 31.549  -25.520 7.166   1.00 71.68  ? 327 ALA D CA  1 
ATOM   11790 C  C   . ALA D 1 326 ? 31.752  -26.959 6.706   1.00 73.69  ? 327 ALA D C   1 
ATOM   11791 O  O   . ALA D 1 326 ? 32.033  -27.844 7.513   1.00 73.56  ? 327 ALA D O   1 
ATOM   11792 C  CB  . ALA D 1 326 ? 30.069  -25.226 7.342   1.00 72.97  ? 327 ALA D CB  1 
ATOM   11793 N  N   . LEU D 1 327 ? 31.615  -27.182 5.402   1.00 72.97  ? 328 LEU D N   1 
ATOM   11794 C  CA  . LEU D 1 327 ? 31.839  -28.507 4.837   1.00 72.25  ? 328 LEU D CA  1 
ATOM   11795 C  C   . LEU D 1 327 ? 33.301  -28.927 4.945   1.00 74.12  ? 328 LEU D C   1 
ATOM   11796 O  O   . LEU D 1 327 ? 33.602  -30.036 5.386   1.00 72.63  ? 328 LEU D O   1 
ATOM   11797 C  CB  . LEU D 1 327 ? 31.400  -28.552 3.377   1.00 69.61  ? 328 LEU D CB  1 
ATOM   11798 C  CG  . LEU D 1 327 ? 31.805  -29.844 2.668   1.00 67.62  ? 328 LEU D CG  1 
ATOM   11799 C  CD1 . LEU D 1 327 ? 31.027  -31.012 3.232   1.00 63.79  ? 328 LEU D CD1 1 
ATOM   11800 C  CD2 . LEU D 1 327 ? 31.570  -29.724 1.189   1.00 66.57  ? 328 LEU D CD2 1 
ATOM   11801 N  N   . GLN D 1 328 ? 34.201  -28.039 4.529   1.00 77.51  ? 329 GLN D N   1 
ATOM   11802 C  CA  . GLN D 1 328 ? 35.636  -28.305 4.605   1.00 78.03  ? 329 GLN D CA  1 
ATOM   11803 C  C   . GLN D 1 328 ? 36.068  -28.669 6.024   1.00 78.23  ? 329 GLN D C   1 
ATOM   11804 O  O   . GLN D 1 328 ? 36.891  -29.561 6.227   1.00 77.41  ? 329 GLN D O   1 
ATOM   11805 C  CB  . GLN D 1 328 ? 36.433  -27.089 4.129   1.00 83.41  ? 329 GLN D CB  1 
ATOM   11806 C  CG  . GLN D 1 328 ? 36.611  -26.983 2.624   1.00 87.76  ? 329 GLN D CG  1 
ATOM   11807 C  CD  . GLN D 1 328 ? 37.668  -25.963 2.245   1.00 91.90  ? 329 GLN D CD  1 
ATOM   11808 O  OE1 . GLN D 1 328 ? 38.803  -26.027 2.718   1.00 94.42  ? 329 GLN D OE1 1 
ATOM   11809 N  NE2 . GLN D 1 328 ? 37.297  -25.008 1.399   1.00 91.74  ? 329 GLN D NE2 1 
ATOM   11810 N  N   . ASP D 1 329 ? 35.496  -27.976 7.002   1.00 79.00  ? 330 ASP D N   1 
ATOM   11811 C  CA  . ASP D 1 329 ? 35.923  -28.106 8.391   1.00 83.41  ? 330 ASP D CA  1 
ATOM   11812 C  C   . ASP D 1 329 ? 35.300  -29.302 9.112   1.00 84.00  ? 330 ASP D C   1 
ATOM   11813 O  O   . ASP D 1 329 ? 35.708  -29.644 10.224  1.00 84.48  ? 330 ASP D O   1 
ATOM   11814 C  CB  . ASP D 1 329 ? 35.604  -26.812 9.139   1.00 86.94  ? 330 ASP D CB  1 
ATOM   11815 C  CG  . ASP D 1 329 ? 36.580  -25.699 8.808   1.00 92.23  ? 330 ASP D CG  1 
ATOM   11816 O  OD1 . ASP D 1 329 ? 37.230  -25.768 7.742   1.00 93.77  ? 330 ASP D OD1 1 
ATOM   11817 O  OD2 . ASP D 1 329 ? 36.668  -24.737 9.597   1.00 92.56  ? 330 ASP D OD2 1 
ATOM   11818 N  N   . ASN D 1 330 ? 34.311  -29.927 8.480   1.00 88.00  ? 331 ASN D N   1 
ATOM   11819 C  CA  . ASN D 1 330 ? 33.648  -31.103 9.040   1.00 90.61  ? 331 ASN D CA  1 
ATOM   11820 C  C   . ASN D 1 330 ? 33.889  -32.327 8.169   1.00 91.61  ? 331 ASN D C   1 
ATOM   11821 O  O   . ASN D 1 330 ? 33.391  -33.415 8.455   1.00 90.63  ? 331 ASN D O   1 
ATOM   11822 C  CB  . ASN D 1 330 ? 32.144  -30.863 9.180   1.00 95.73  ? 331 ASN D CB  1 
ATOM   11823 C  CG  . ASN D 1 330 ? 31.800  -29.945 10.336  1.00 99.67  ? 331 ASN D CG  1 
ATOM   11824 O  OD1 . ASN D 1 330 ? 32.299  -30.116 11.447  1.00 103.53 ? 331 ASN D OD1 1 
ATOM   11825 N  ND2 . ASN D 1 330 ? 30.932  -28.971 10.083  1.00 98.36  ? 331 ASN D ND2 1 
ATOM   11826 N  N   . ARG D 1 331 ? 34.683  -32.119 7.124   1.00 92.19  ? 332 ARG D N   1 
ATOM   11827 C  CA  . ARG D 1 331 ? 34.915  -33.078 6.044   1.00 94.88  ? 332 ARG D CA  1 
ATOM   11828 C  C   . ARG D 1 331 ? 35.016  -34.552 6.442   1.00 98.13  ? 332 ARG D C   1 
ATOM   11829 O  O   . ARG D 1 331 ? 34.309  -35.393 5.889   1.00 100.49 ? 332 ARG D O   1 
ATOM   11830 C  CB  . ARG D 1 331 ? 36.192  -32.686 5.294   1.00 95.01  ? 332 ARG D CB  1 
ATOM   11831 N  N   . ASP D 1 332 ? 35.887  -34.867 7.395   1.00 98.88  ? 333 ASP D N   1 
ATOM   11832 C  CA  . ASP D 1 332 ? 36.230  -36.265 7.651   1.00 101.01 ? 333 ASP D CA  1 
ATOM   11833 C  C   . ASP D 1 332 ? 35.372  -36.951 8.719   1.00 98.20  ? 333 ASP D C   1 
ATOM   11834 O  O   . ASP D 1 332 ? 35.176  -38.167 8.667   1.00 101.50 ? 333 ASP D O   1 
ATOM   11835 C  CB  . ASP D 1 332 ? 37.711  -36.374 8.010   1.00 103.07 ? 333 ASP D CB  1 
ATOM   11836 C  CG  . ASP D 1 332 ? 38.606  -36.278 6.787   1.00 106.03 ? 333 ASP D CG  1 
ATOM   11837 O  OD1 . ASP D 1 332 ? 38.115  -35.831 5.728   1.00 106.66 ? 333 ASP D OD1 1 
ATOM   11838 O  OD2 . ASP D 1 332 ? 39.792  -36.655 6.879   1.00 108.31 ? 333 ASP D OD2 1 
ATOM   11839 N  N   . THR D 1 333 ? 34.865  -36.189 9.682   1.00 94.14  ? 334 THR D N   1 
ATOM   11840 C  CA  . THR D 1 333 ? 33.842  -36.716 10.579  1.00 90.39  ? 334 THR D CA  1 
ATOM   11841 C  C   . THR D 1 333 ? 32.621  -37.045 9.731   1.00 86.00  ? 334 THR D C   1 
ATOM   11842 O  O   . THR D 1 333 ? 32.054  -38.150 9.796   1.00 84.43  ? 334 THR D O   1 
ATOM   11843 C  CB  . THR D 1 333 ? 33.462  -35.712 11.683  1.00 93.18  ? 334 THR D CB  1 
ATOM   11844 O  OG1 . THR D 1 333 ? 34.591  -35.477 12.533  1.00 95.62  ? 334 THR D OG1 1 
ATOM   11845 C  CG2 . THR D 1 333 ? 32.306  -36.246 12.517  1.00 94.08  ? 334 THR D CG2 1 
ATOM   11846 N  N   . LEU D 1 334 ? 32.246  -36.061 8.920   1.00 77.88  ? 335 LEU D N   1 
ATOM   11847 C  CA  . LEU D 1 334 ? 31.178  -36.201 7.946   1.00 77.74  ? 335 LEU D CA  1 
ATOM   11848 C  C   . LEU D 1 334 ? 31.360  -37.440 7.087   1.00 77.54  ? 335 LEU D C   1 
ATOM   11849 O  O   . LEU D 1 334 ? 30.442  -38.233 6.961   1.00 80.92  ? 335 LEU D O   1 
ATOM   11850 C  CB  . LEU D 1 334 ? 31.103  -34.968 7.048   1.00 73.15  ? 335 LEU D CB  1 
ATOM   11851 C  CG  . LEU D 1 334 ? 30.331  -35.177 5.745   1.00 74.74  ? 335 LEU D CG  1 
ATOM   11852 C  CD1 . LEU D 1 334 ? 28.835  -35.014 5.962   1.00 72.20  ? 335 LEU D CD1 1 
ATOM   11853 C  CD2 . LEU D 1 334 ? 30.833  -34.244 4.661   1.00 74.57  ? 335 LEU D CD2 1 
ATOM   11854 N  N   . THR D 1 335 ? 32.544  -37.610 6.502   1.00 80.22  ? 336 THR D N   1 
ATOM   11855 C  CA  . THR D 1 335 ? 32.767  -38.728 5.589   1.00 81.05  ? 336 THR D CA  1 
ATOM   11856 C  C   . THR D 1 335 ? 32.809  -40.053 6.343   1.00 80.64  ? 336 THR D C   1 
ATOM   11857 O  O   . THR D 1 335 ? 32.502  -41.101 5.775   1.00 83.17  ? 336 THR D O   1 
ATOM   11858 C  CB  . THR D 1 335 ? 34.067  -38.563 4.766   1.00 90.29  ? 336 THR D CB  1 
ATOM   11859 O  OG1 . THR D 1 335 ? 34.004  -39.393 3.601   1.00 96.39  ? 336 THR D OG1 1 
ATOM   11860 C  CG2 . THR D 1 335 ? 35.294  -38.948 5.574   1.00 92.88  ? 336 THR D CG2 1 
ATOM   11861 N  N   . ALA D 1 336 ? 33.179  -40.007 7.619   1.00 75.87  ? 337 ALA D N   1 
ATOM   11862 C  CA  . ALA D 1 336 ? 33.145  -41.203 8.447   1.00 74.09  ? 337 ALA D CA  1 
ATOM   11863 C  C   . ALA D 1 336 ? 31.698  -41.646 8.615   1.00 70.40  ? 337 ALA D C   1 
ATOM   11864 O  O   . ALA D 1 336 ? 31.365  -42.822 8.424   1.00 74.42  ? 337 ALA D O   1 
ATOM   11865 C  CB  . ALA D 1 336 ? 33.794  -40.948 9.798   1.00 64.11  ? 337 ALA D CB  1 
ATOM   11866 N  N   . LYS D 1 337 ? 30.836  -40.690 8.953   1.00 68.85  ? 338 LYS D N   1 
ATOM   11867 C  CA  . LYS D 1 337 ? 29.413  -40.980 9.110   1.00 66.33  ? 338 LYS D CA  1 
ATOM   11868 C  C   . LYS D 1 337 ? 28.756  -41.399 7.790   1.00 68.07  ? 338 LYS D C   1 
ATOM   11869 O  O   . LYS D 1 337 ? 27.856  -42.238 7.776   1.00 69.22  ? 338 LYS D O   1 
ATOM   11870 C  CB  . LYS D 1 337 ? 28.686  -39.767 9.691   1.00 65.47  ? 338 LYS D CB  1 
ATOM   11871 N  N   . VAL D 1 338 ? 29.213  -40.812 6.688   1.00 67.72  ? 339 VAL D N   1 
ATOM   11872 C  CA  . VAL D 1 338 ? 28.677  -41.108 5.364   1.00 70.46  ? 339 VAL D CA  1 
ATOM   11873 C  C   . VAL D 1 338 ? 29.111  -42.506 4.944   1.00 70.72  ? 339 VAL D C   1 
ATOM   11874 O  O   . VAL D 1 338 ? 28.400  -43.197 4.218   1.00 76.18  ? 339 VAL D O   1 
ATOM   11875 C  CB  . VAL D 1 338 ? 29.127  -40.054 4.319   1.00 64.81  ? 339 VAL D CB  1 
ATOM   11876 C  CG1 . VAL D 1 338 ? 28.781  -40.493 2.902   1.00 63.55  ? 339 VAL D CG1 1 
ATOM   11877 C  CG2 . VAL D 1 338 ? 28.481  -38.712 4.619   1.00 66.66  ? 339 VAL D CG2 1 
ATOM   11878 N  N   . ILE D 1 339 ? 30.273  -42.930 5.426   1.00 65.87  ? 340 ILE D N   1 
ATOM   11879 C  CA  . ILE D 1 339 ? 30.709  -44.304 5.220   1.00 70.97  ? 340 ILE D CA  1 
ATOM   11880 C  C   . ILE D 1 339 ? 29.850  -45.250 6.056   1.00 72.95  ? 340 ILE D C   1 
ATOM   11881 O  O   . ILE D 1 339 ? 29.367  -46.264 5.553   1.00 76.59  ? 340 ILE D O   1 
ATOM   11882 C  CB  . ILE D 1 339 ? 32.197  -44.491 5.572   1.00 67.76  ? 340 ILE D CB  1 
ATOM   11883 C  CG1 . ILE D 1 339 ? 33.076  -43.934 4.451   1.00 67.44  ? 340 ILE D CG1 1 
ATOM   11884 C  CG2 . ILE D 1 339 ? 32.516  -45.962 5.786   1.00 69.45  ? 340 ILE D CG2 1 
ATOM   11885 C  CD1 . ILE D 1 339 ? 34.558  -44.117 4.687   1.00 73.76  ? 340 ILE D CD1 1 
ATOM   11886 N  N   . GLN D 1 340 ? 29.644  -44.908 7.325   1.00 73.12  ? 341 GLN D N   1 
ATOM   11887 C  CA  . GLN D 1 340 ? 28.826  -45.741 8.207   1.00 68.98  ? 341 GLN D CA  1 
ATOM   11888 C  C   . GLN D 1 340 ? 27.372  -45.847 7.748   1.00 69.26  ? 341 GLN D C   1 
ATOM   11889 O  O   . GLN D 1 340 ? 26.678  -46.803 8.087   1.00 70.58  ? 341 GLN D O   1 
ATOM   11890 C  CB  . GLN D 1 340 ? 28.860  -45.207 9.640   1.00 75.94  ? 341 GLN D CB  1 
ATOM   11891 C  CG  . GLN D 1 340 ? 30.193  -45.365 10.342  1.00 77.23  ? 341 GLN D CG  1 
ATOM   11892 C  CD  . GLN D 1 340 ? 30.101  -45.045 11.821  1.00 80.73  ? 341 GLN D CD  1 
ATOM   11893 O  OE1 . GLN D 1 340 ? 30.800  -44.166 12.325  1.00 81.69  ? 341 GLN D OE1 1 
ATOM   11894 N  NE2 . GLN D 1 340 ? 29.230  -45.760 12.526  1.00 81.60  ? 341 GLN D NE2 1 
ATOM   11895 N  N   . GLY D 1 341 ? 26.912  -44.864 6.984   1.00 68.10  ? 342 GLY D N   1 
ATOM   11896 C  CA  . GLY D 1 341 ? 25.528  -44.834 6.550   1.00 71.69  ? 342 GLY D CA  1 
ATOM   11897 C  C   . GLY D 1 341 ? 25.306  -45.377 5.152   1.00 71.98  ? 342 GLY D C   1 
ATOM   11898 O  O   . GLY D 1 341 ? 24.278  -45.991 4.872   1.00 71.23  ? 342 GLY D O   1 
ATOM   11899 N  N   . CYS D 1 342 ? 26.275  -45.156 4.272   1.00 73.33  ? 343 CYS D N   1 
ATOM   11900 C  CA  . CYS D 1 342 ? 26.127  -45.523 2.868   1.00 76.14  ? 343 CYS D CA  1 
ATOM   11901 C  C   . CYS D 1 342 ? 27.008  -46.709 2.481   1.00 82.40  ? 343 CYS D C   1 
ATOM   11902 O  O   . CYS D 1 342 ? 26.799  -47.333 1.441   1.00 83.47  ? 343 CYS D O   1 
ATOM   11903 C  CB  . CYS D 1 342 ? 26.442  -44.321 1.975   1.00 73.25  ? 343 CYS D CB  1 
ATOM   11904 S  SG  . CYS D 1 342 ? 25.288  -42.938 2.152   1.00 93.50  ? 343 CYS D SG  1 
ATOM   11905 N  N   . GLY D 1 343 ? 27.990  -47.020 3.320   1.00 85.84  ? 344 GLY D N   1 
ATOM   11906 C  CA  . GLY D 1 343 ? 28.872  -48.144 3.064   1.00 90.52  ? 344 GLY D CA  1 
ATOM   11907 C  C   . GLY D 1 343 ? 30.274  -47.720 2.672   1.00 90.79  ? 344 GLY D C   1 
ATOM   11908 O  O   . GLY D 1 343 ? 30.577  -46.529 2.599   1.00 92.51  ? 344 GLY D O   1 
ATOM   11909 N  N   . ASN D 1 344 ? 31.132  -48.702 2.417   1.00 94.76  ? 345 ASN D N   1 
ATOM   11910 C  CA  . ASN D 1 344 ? 32.519  -48.437 2.056   1.00 95.17  ? 345 ASN D CA  1 
ATOM   11911 C  C   . ASN D 1 344 ? 32.720  -48.419 0.544   1.00 97.06  ? 345 ASN D C   1 
ATOM   11912 O  O   . ASN D 1 344 ? 32.394  -49.389 -0.140  1.00 100.55 ? 345 ASN D O   1 
ATOM   11913 C  CB  . ASN D 1 344 ? 33.442  -49.482 2.686   1.00 101.73 ? 345 ASN D CB  1 
ATOM   11914 C  CG  . ASN D 1 344 ? 33.061  -49.809 4.117   1.00 105.16 ? 345 ASN D CG  1 
ATOM   11915 O  OD1 . ASN D 1 344 ? 33.412  -49.084 5.047   1.00 105.92 ? 345 ASN D OD1 1 
ATOM   11916 N  ND2 . ASN D 1 344 ? 32.341  -50.911 4.300   1.00 105.31 ? 345 ASN D ND2 1 
ATOM   11917 N  N   . PRO D 1 345 ? 33.254  -47.307 0.016   1.00 92.67  ? 346 PRO D N   1 
ATOM   11918 C  CA  . PRO D 1 345 ? 33.538  -47.186 -1.417  1.00 97.55  ? 346 PRO D CA  1 
ATOM   11919 C  C   . PRO D 1 345 ? 34.936  -47.690 -1.773  1.00 104.97 ? 346 PRO D C   1 
ATOM   11920 O  O   . PRO D 1 345 ? 35.681  -48.106 -0.886  1.00 104.15 ? 346 PRO D O   1 
ATOM   11921 C  CB  . PRO D 1 345 ? 33.420  -45.675 -1.675  1.00 90.93  ? 346 PRO D CB  1 
ATOM   11922 C  CG  . PRO D 1 345 ? 33.197  -45.025 -0.305  1.00 88.56  ? 346 PRO D CG  1 
ATOM   11923 C  CD  . PRO D 1 345 ? 33.535  -46.052 0.726   1.00 90.64  ? 346 PRO D CD  1 
ATOM   11924 N  N   . LYS D 1 346 ? 35.283  -47.645 -3.057  1.00 118.54 ? 347 LYS D N   1 
ATOM   11925 C  CA  . LYS D 1 346 ? 36.598  -48.085 -3.515  1.00 123.81 ? 347 LYS D CA  1 
ATOM   11926 C  C   . LYS D 1 346 ? 37.654  -47.021 -3.228  1.00 123.42 ? 347 LYS D C   1 
ATOM   11927 O  O   . LYS D 1 346 ? 37.356  -45.827 -3.230  1.00 125.90 ? 347 LYS D O   1 
ATOM   11928 C  CB  . LYS D 1 346 ? 36.566  -48.413 -5.009  1.00 125.95 ? 347 LYS D CB  1 
ATOM   11929 N  N   . VAL D 1 347 ? 38.887  -47.456 -2.986  1.00 123.12 ? 348 VAL D N   1 
ATOM   11930 C  CA  . VAL D 1 347 ? 39.956  -46.540 -2.593  1.00 118.97 ? 348 VAL D CA  1 
ATOM   11931 C  C   . VAL D 1 347 ? 41.082  -46.468 -3.627  1.00 117.13 ? 348 VAL D C   1 
ATOM   11932 O  O   . VAL D 1 347 ? 41.427  -47.472 -4.252  1.00 118.65 ? 348 VAL D O   1 
ATOM   11933 C  CB  . VAL D 1 347 ? 40.553  -46.942 -1.226  1.00 119.73 ? 348 VAL D CB  1 
ATOM   11934 C  CG1 . VAL D 1 347 ? 41.475  -45.852 -0.700  1.00 119.04 ? 348 VAL D CG1 1 
ATOM   11935 C  CG2 . VAL D 1 347 ? 39.443  -47.214 -0.225  1.00 118.58 ? 348 VAL D CG2 1 
ATOM   11936 N  N   . ASN D 1 348 ? 41.638  -45.267 -3.793  1.00 110.81 ? 349 ASN D N   1 
ATOM   11937 C  CA  . ASN D 1 348 ? 42.758  -44.999 -4.697  1.00 107.15 ? 349 ASN D CA  1 
ATOM   11938 C  C   . ASN D 1 348 ? 42.428  -45.359 -6.143  1.00 107.58 ? 349 ASN D C   1 
ATOM   11939 O  O   . ASN D 1 348 ? 42.857  -44.676 -7.074  1.00 107.36 ? 349 ASN D O   1 
ATOM   11940 C  CB  . ASN D 1 348 ? 44.015  -45.749 -4.235  1.00 103.58 ? 349 ASN D CB  1 
ATOM   11941 C  CG  . ASN D 1 348 ? 45.232  -45.454 -5.101  1.00 100.17 ? 349 ASN D CG  1 
ATOM   11942 O  OD1 . ASN D 1 348 ? 45.253  -44.486 -5.861  1.00 100.10 ? 349 ASN D OD1 1 
ATOM   11943 N  ND2 . ASN D 1 348 ? 46.255  -46.293 -4.986  1.00 98.31  ? 349 ASN D ND2 1 
ATOM   11944 N  N   . ARG D 1 360 ? 46.484  -17.115 1.538   1.00 104.63 ? 361 ARG D N   1 
ATOM   11945 C  CA  . ARG D 1 360 ? 45.251  -17.609 0.937   1.00 103.46 ? 361 ARG D CA  1 
ATOM   11946 C  C   . ARG D 1 360 ? 44.053  -17.367 1.850   1.00 101.60 ? 361 ARG D C   1 
ATOM   11947 O  O   . ARG D 1 360 ? 44.209  -17.146 3.051   1.00 101.55 ? 361 ARG D O   1 
ATOM   11948 C  CB  . ARG D 1 360 ? 45.371  -19.101 0.617   1.00 103.10 ? 361 ARG D CB  1 
ATOM   11949 N  N   . GLY D 1 361 ? 42.859  -17.410 1.269   1.00 100.10 ? 362 GLY D N   1 
ATOM   11950 C  CA  . GLY D 1 361 ? 41.628  -17.311 2.031   1.00 99.44  ? 362 GLY D CA  1 
ATOM   11951 C  C   . GLY D 1 361 ? 41.339  -15.982 2.700   1.00 98.97  ? 362 GLY D C   1 
ATOM   11952 O  O   . GLY D 1 361 ? 41.094  -15.933 3.906   1.00 100.77 ? 362 GLY D O   1 
ATOM   11953 N  N   . LYS D 1 362 ? 41.361  -14.901 1.927   1.00 97.00  ? 363 LYS D N   1 
ATOM   11954 C  CA  . LYS D 1 362 ? 40.910  -13.612 2.436   1.00 96.36  ? 363 LYS D CA  1 
ATOM   11955 C  C   . LYS D 1 362 ? 39.480  -13.359 1.973   1.00 92.32  ? 363 LYS D C   1 
ATOM   11956 O  O   . LYS D 1 362 ? 39.229  -13.146 0.787   1.00 92.22  ? 363 LYS D O   1 
ATOM   11957 C  CB  . LYS D 1 362 ? 41.834  -12.484 1.973   1.00 95.49  ? 363 LYS D CB  1 
ATOM   11958 N  N   . LEU D 1 363 ? 38.547  -13.375 2.919   1.00 89.77  ? 364 LEU D N   1 
ATOM   11959 C  CA  . LEU D 1 363 ? 37.131  -13.227 2.603   1.00 87.90  ? 364 LEU D CA  1 
ATOM   11960 C  C   . LEU D 1 363 ? 36.505  -12.088 3.390   1.00 87.08  ? 364 LEU D C   1 
ATOM   11961 O  O   . LEU D 1 363 ? 36.595  -12.045 4.617   1.00 87.01  ? 364 LEU D O   1 
ATOM   11962 C  CB  . LEU D 1 363 ? 36.376  -14.527 2.888   1.00 85.17  ? 364 LEU D CB  1 
ATOM   11963 C  CG  . LEU D 1 363 ? 36.603  -15.696 1.930   1.00 82.80  ? 364 LEU D CG  1 
ATOM   11964 C  CD1 . LEU D 1 363 ? 36.082  -16.991 2.533   1.00 80.51  ? 364 LEU D CD1 1 
ATOM   11965 C  CD2 . LEU D 1 363 ? 35.936  -15.422 0.590   1.00 80.99  ? 364 LEU D CD2 1 
ATOM   11966 N  N   . ALA D 1 364 ? 35.868  -11.168 2.676   1.00 94.53  ? 365 ALA D N   1 
ATOM   11967 C  CA  . ALA D 1 364 ? 35.188  -10.056 3.317   1.00 103.97 ? 365 ALA D CA  1 
ATOM   11968 C  C   . ALA D 1 364 ? 33.981  -10.551 4.101   1.00 113.27 ? 365 ALA D C   1 
ATOM   11969 O  O   . ALA D 1 364 ? 33.156  -11.298 3.573   1.00 115.46 ? 365 ALA D O   1 
ATOM   11970 C  CB  . ALA D 1 364 ? 34.763  -9.023  2.284   1.00 104.36 ? 365 ALA D CB  1 
ATOM   11971 N  N   . PRO D 1 365 ? 33.881  -10.148 5.375   1.00 120.08 ? 366 PRO D N   1 
ATOM   11972 C  CA  . PRO D 1 365 ? 32.652  -10.399 6.129   1.00 117.40 ? 366 PRO D CA  1 
ATOM   11973 C  C   . PRO D 1 365 ? 31.525  -9.581  5.521   1.00 111.17 ? 366 PRO D C   1 
ATOM   11974 O  O   . PRO D 1 365 ? 31.808  -8.635  4.784   1.00 112.32 ? 366 PRO D O   1 
ATOM   11975 C  CB  . PRO D 1 365 ? 32.988  -9.915  7.546   1.00 120.88 ? 366 PRO D CB  1 
ATOM   11976 C  CG  . PRO D 1 365 ? 34.483  -9.809  7.586   1.00 123.27 ? 366 PRO D CG  1 
ATOM   11977 C  CD  . PRO D 1 365 ? 34.902  -9.471  6.191   1.00 122.31 ? 366 PRO D CD  1 
ATOM   11978 N  N   . ARG D 1 366 ? 30.275  -9.911  5.815   1.00 104.44 ? 367 ARG D N   1 
ATOM   11979 C  CA  . ARG D 1 366 ? 29.203  -9.071  5.318   1.00 99.37  ? 367 ARG D CA  1 
ATOM   11980 C  C   . ARG D 1 366 ? 29.035  -7.916  6.296   1.00 98.80  ? 367 ARG D C   1 
ATOM   11981 O  O   . ARG D 1 366 ? 28.706  -8.111  7.465   1.00 99.28  ? 367 ARG D O   1 
ATOM   11982 C  CB  . ARG D 1 366 ? 27.901  -9.858  5.153   1.00 96.59  ? 367 ARG D CB  1 
ATOM   11983 C  CG  . ARG D 1 366 ? 27.555  -10.767 6.317   1.00 92.93  ? 367 ARG D CG  1 
ATOM   11984 C  CD  . ARG D 1 366 ? 26.107  -11.222 6.245   1.00 87.93  ? 367 ARG D CD  1 
ATOM   11985 N  NE  . ARG D 1 366 ? 25.497  -11.275 7.569   1.00 86.58  ? 367 ARG D NE  1 
ATOM   11986 C  CZ  . ARG D 1 366 ? 25.412  -12.376 8.308   1.00 85.37  ? 367 ARG D CZ  1 
ATOM   11987 N  NH1 . ARG D 1 366 ? 25.897  -13.522 7.851   1.00 85.99  1 367 ARG D NH1 1 
ATOM   11988 N  NH2 . ARG D 1 366 ? 24.842  -12.331 9.504   1.00 85.75  ? 367 ARG D NH2 1 
ATOM   11989 N  N   . GLU D 1 367 ? 29.275  -6.708  5.801   1.00 96.06  ? 368 GLU D N   1 
ATOM   11990 C  CA  . GLU D 1 367 ? 29.250  -5.516  6.634   1.00 92.81  ? 368 GLU D CA  1 
ATOM   11991 C  C   . GLU D 1 367 ? 28.432  -4.451  5.932   1.00 93.58  ? 368 GLU D C   1 
ATOM   11992 O  O   . GLU D 1 367 ? 28.546  -4.272  4.719   1.00 89.27  ? 368 GLU D O   1 
ATOM   11993 C  CB  . GLU D 1 367 ? 30.670  -5.020  6.919   1.00 92.52  ? 368 GLU D CB  1 
ATOM   11994 N  N   . ARG D 1 368 ? 27.603  -3.740  6.684   1.00 97.07  ? 369 ARG D N   1 
ATOM   11995 C  CA  . ARG D 1 368 ? 26.658  -2.847  6.045   1.00 102.56 ? 369 ARG D CA  1 
ATOM   11996 C  C   . ARG D 1 368 ? 26.319  -1.611  6.883   1.00 108.72 ? 369 ARG D C   1 
ATOM   11997 C  CB  . ARG D 1 368 ? 25.383  -3.649  5.738   1.00 100.98 ? 369 ARG D CB  1 
ATOM   11998 N  N   . PRO D 1 369 ? 25.552  -0.655  6.311   1.00 118.22 ? 370 PRO D N   1 
ATOM   11999 C  CA  . PRO D 1 369 ? 25.406  -0.479  4.859   1.00 121.72 ? 370 PRO D CA  1 
ATOM   12000 C  C   . PRO D 1 369 ? 26.713  0.007   4.230   1.00 123.39 ? 370 PRO D C   1 
ATOM   12001 O  O   . PRO D 1 369 ? 27.327  0.935   4.754   1.00 125.88 ? 370 PRO D O   1 
ATOM   12002 C  CB  . PRO D 1 369 ? 24.292  0.568   4.742   1.00 123.64 ? 370 PRO D CB  1 
ATOM   12003 C  CG  . PRO D 1 369 ? 24.214  1.252   6.084   1.00 124.24 ? 370 PRO D CG  1 
ATOM   12004 C  CD  . PRO D 1 369 ? 25.070  0.510   7.068   1.00 122.18 ? 370 PRO D CD  1 
ATOM   12005 N  N   . PRO D 1 370 ? 27.153  -0.647  3.140   1.00 117.35 ? 371 PRO D N   1 
ATOM   12006 C  CA  . PRO D 1 370 ? 28.310  -0.161  2.385   1.00 119.29 ? 371 PRO D CA  1 
ATOM   12007 C  C   . PRO D 1 370 ? 27.936  1.124   1.665   1.00 118.17 ? 371 PRO D C   1 
ATOM   12008 O  O   . PRO D 1 370 ? 28.779  1.982   1.393   1.00 121.84 ? 371 PRO D O   1 
ATOM   12009 C  CB  . PRO D 1 370 ? 28.595  -1.296  1.399   1.00 118.31 ? 371 PRO D CB  1 
ATOM   12010 C  CG  . PRO D 1 370 ? 27.274  -1.962  1.211   1.00 117.55 ? 371 PRO D CG  1 
ATOM   12011 C  CD  . PRO D 1 370 ? 26.584  -1.872  2.549   1.00 116.66 ? 371 PRO D CD  1 
ATOM   12012 N  N   . SER D 1 371 ? 26.644  1.245   1.383   1.00 116.69 ? 372 SER D N   1 
ATOM   12013 C  CA  . SER D 1 371 ? 26.096  2.382   0.667   1.00 113.83 ? 372 SER D CA  1 
ATOM   12014 C  C   . SER D 1 371 ? 25.278  3.283   1.582   1.00 108.14 ? 372 SER D C   1 
ATOM   12015 O  O   . SER D 1 371 ? 24.628  2.816   2.517   1.00 110.37 ? 372 SER D O   1 
ATOM   12016 C  CB  . SER D 1 371 ? 25.222  1.899   -0.492  1.00 115.41 ? 372 SER D CB  1 
ATOM   12017 O  OG  . SER D 1 371 ? 25.994  1.663   -1.654  1.00 117.67 ? 372 SER D OG  1 
ATOM   12018 N  N   . GLY D 1 372 ? 25.323  4.582   1.311   1.00 91.63  ? 373 GLY D N   1 
ATOM   12019 C  CA  . GLY D 1 372 ? 24.378  5.509   1.901   1.00 80.00  ? 373 GLY D CA  1 
ATOM   12020 C  C   . GLY D 1 372 ? 23.209  5.614   0.942   1.00 70.15  ? 373 GLY D C   1 
ATOM   12021 O  O   . GLY D 1 372 ? 22.213  6.283   1.213   1.00 68.01  ? 373 GLY D O   1 
ATOM   12022 N  N   . THR D 1 373 ? 23.348  4.922   -0.187  1.00 59.70  ? 374 THR D N   1 
ATOM   12023 C  CA  . THR D 1 373 ? 22.385  4.954   -1.283  1.00 56.23  ? 374 THR D CA  1 
ATOM   12024 C  C   . THR D 1 373 ? 20.962  4.591   -0.861  1.00 43.13  ? 374 THR D C   1 
ATOM   12025 O  O   . THR D 1 373 ? 20.018  5.337   -1.133  1.00 49.77  ? 374 THR D O   1 
ATOM   12026 C  CB  . THR D 1 373 ? 22.817  3.996   -2.413  1.00 51.02  ? 374 THR D CB  1 
ATOM   12027 O  OG1 . THR D 1 373 ? 24.062  4.437   -2.965  1.00 45.73  ? 374 THR D OG1 1 
ATOM   12028 C  CG2 . THR D 1 373 ? 21.769  3.952   -3.513  1.00 48.16  ? 374 THR D CG2 1 
ATOM   12029 N  N   . LEU D 1 374 ? 20.815  3.446   -0.201  1.00 47.97  ? 375 LEU D N   1 
ATOM   12030 C  CA  . LEU D 1 374 ? 19.495  2.949   0.170   1.00 50.00  ? 375 LEU D CA  1 
ATOM   12031 C  C   . LEU D 1 374 ? 18.773  3.908   1.107   1.00 50.67  ? 375 LEU D C   1 
ATOM   12032 O  O   . LEU D 1 374 ? 17.569  4.109   0.980   1.00 40.81  ? 375 LEU D O   1 
ATOM   12033 C  CB  . LEU D 1 374 ? 19.595  1.569   0.821   1.00 51.09  ? 375 LEU D CB  1 
ATOM   12034 C  CG  . LEU D 1 374 ? 18.241  0.927   1.143   1.00 47.90  ? 375 LEU D CG  1 
ATOM   12035 C  CD1 . LEU D 1 374 ? 17.451  0.655   -0.130  1.00 45.66  ? 375 LEU D CD1 1 
ATOM   12036 C  CD2 . LEU D 1 374 ? 18.413  -0.344  1.956   1.00 45.29  ? 375 LEU D CD2 1 
ATOM   12037 N  N   . GLU D 1 375 ? 19.506  4.502   2.044   1.00 50.80  ? 376 GLU D N   1 
ATOM   12038 C  CA  . GLU D 1 375 ? 18.904  5.451   2.974   1.00 55.16  ? 376 GLU D CA  1 
ATOM   12039 C  C   . GLU D 1 375 ? 18.389  6.680   2.230   1.00 52.57  ? 376 GLU D C   1 
ATOM   12040 O  O   . GLU D 1 375 ? 17.310  7.192   2.535   1.00 53.30  ? 376 GLU D O   1 
ATOM   12041 C  CB  . GLU D 1 375 ? 19.903  5.861   4.060   1.00 67.55  ? 376 GLU D CB  1 
ATOM   12042 C  CG  . GLU D 1 375 ? 19.677  7.262   4.615   1.00 78.56  ? 376 GLU D CG  1 
ATOM   12043 C  CD  . GLU D 1 375 ? 19.969  7.361   6.100   1.00 89.05  ? 376 GLU D CD  1 
ATOM   12044 O  OE1 . GLU D 1 375 ? 20.590  6.428   6.651   1.00 91.36  ? 376 GLU D OE1 1 
ATOM   12045 O  OE2 . GLU D 1 375 ? 19.573  8.373   6.717   1.00 92.10  ? 376 GLU D OE2 1 
ATOM   12046 N  N   . LYS D 1 376 ? 19.157  7.140   1.247   1.00 47.13  ? 377 LYS D N   1 
ATOM   12047 C  CA  . LYS D 1 376 ? 18.754  8.278   0.427   1.00 51.87  ? 377 LYS D CA  1 
ATOM   12048 C  C   . LYS D 1 376 ? 17.492  7.959   -0.368  1.00 47.27  ? 377 LYS D C   1 
ATOM   12049 O  O   . LYS D 1 376 ? 16.521  8.726   -0.354  1.00 52.89  ? 377 LYS D O   1 
ATOM   12050 C  CB  . LYS D 1 376 ? 19.883  8.685   -0.525  1.00 55.61  ? 377 LYS D CB  1 
ATOM   12051 C  CG  . LYS D 1 376 ? 21.182  9.070   0.166   1.00 53.65  ? 377 LYS D CG  1 
ATOM   12052 C  CD  . LYS D 1 376 ? 20.933  9.991   1.348   1.00 56.06  ? 377 LYS D CD  1 
ATOM   12053 C  CE  . LYS D 1 376 ? 22.199  10.733  1.743   1.00 62.25  ? 377 LYS D CE  1 
ATOM   12054 N  NZ  . LYS D 1 376 ? 22.539  11.799  0.760   1.00 63.80  ? 377 LYS D NZ  1 
ATOM   12055 N  N   . LEU D 1 377 ? 17.516  6.820   -1.056  1.00 48.29  ? 378 LEU D N   1 
ATOM   12056 C  CA  . LEU D 1 377 ? 16.377  6.370   -1.852  1.00 47.89  ? 378 LEU D CA  1 
ATOM   12057 C  C   . LEU D 1 377 ? 15.113  6.240   -1.010  1.00 45.73  ? 378 LEU D C   1 
ATOM   12058 O  O   . LEU D 1 377 ? 14.049  6.704   -1.407  1.00 46.30  ? 378 LEU D O   1 
ATOM   12059 C  CB  . LEU D 1 377 ? 16.685  5.032   -2.525  1.00 40.55  ? 378 LEU D CB  1 
ATOM   12060 C  CG  . LEU D 1 377 ? 17.766  5.024   -3.605  1.00 47.72  ? 378 LEU D CG  1 
ATOM   12061 C  CD1 . LEU D 1 377 ? 17.971  3.611   -4.129  1.00 46.47  ? 378 LEU D CD1 1 
ATOM   12062 C  CD2 . LEU D 1 377 ? 17.400  5.973   -4.736  1.00 41.49  ? 378 LEU D CD2 1 
ATOM   12063 N  N   . VAL D 1 378 ? 15.242  5.608   0.152   1.00 39.78  ? 379 VAL D N   1 
ATOM   12064 C  CA  . VAL D 1 378 ? 14.118  5.410   1.060   1.00 39.23  ? 379 VAL D CA  1 
ATOM   12065 C  C   . VAL D 1 378 ? 13.601  6.742   1.597   1.00 46.59  ? 379 VAL D C   1 
ATOM   12066 O  O   . VAL D 1 378 ? 12.394  6.939   1.721   1.00 47.10  ? 379 VAL D O   1 
ATOM   12067 C  CB  . VAL D 1 378 ? 14.507  4.488   2.240   1.00 39.61  ? 379 VAL D CB  1 
ATOM   12068 C  CG1 . VAL D 1 378 ? 13.469  4.552   3.351   1.00 39.16  ? 379 VAL D CG1 1 
ATOM   12069 C  CG2 . VAL D 1 378 ? 14.681  3.058   1.757   1.00 40.90  ? 379 VAL D CG2 1 
ATOM   12070 N  N   . SER D 1 379 ? 14.517  7.656   1.903   1.00 44.01  ? 380 SER D N   1 
ATOM   12071 C  CA  . SER D 1 379 ? 14.145  8.980   2.394   1.00 40.41  ? 380 SER D CA  1 
ATOM   12072 C  C   . SER D 1 379 ? 13.314  9.733   1.357   1.00 48.41  ? 380 SER D C   1 
ATOM   12073 O  O   . SER D 1 379 ? 12.163  10.133  1.619   1.00 49.93  ? 380 SER D O   1 
ATOM   12074 C  CB  . SER D 1 379 ? 15.397  9.784   2.756   1.00 52.07  ? 380 SER D CB  1 
ATOM   12075 O  OG  . SER D 1 379 ? 15.066  11.106  3.146   1.00 56.73  ? 380 SER D OG  1 
ATOM   12076 N  N   . GLU D 1 380 ? 13.903  9.914   0.177   1.00 46.96  ? 381 GLU D N   1 
ATOM   12077 C  CA  A GLU D 1 380 ? 13.225  10.603  -0.913  0.44 48.85  ? 381 GLU D CA  1 
ATOM   12078 C  CA  B GLU D 1 380 ? 13.229  10.598  -0.920  0.56 48.97  ? 381 GLU D CA  1 
ATOM   12079 C  C   . GLU D 1 380 ? 11.886  9.943   -1.232  1.00 47.16  ? 381 GLU D C   1 
ATOM   12080 O  O   . GLU D 1 380 ? 10.881  10.627  -1.405  1.00 49.24  ? 381 GLU D O   1 
ATOM   12081 C  CB  A GLU D 1 380 ? 14.112  10.639  -2.160  0.44 49.98  ? 381 GLU D CB  1 
ATOM   12082 C  CB  B GLU D 1 380 ? 14.114  10.611  -2.169  0.56 49.97  ? 381 GLU D CB  1 
ATOM   12083 C  CG  A GLU D 1 380 ? 14.726  12.003  -2.447  0.44 50.54  ? 381 GLU D CG  1 
ATOM   12084 C  CG  B GLU D 1 380 ? 13.456  11.212  -3.406  0.56 52.95  ? 381 GLU D CG  1 
ATOM   12085 C  CD  A GLU D 1 380 ? 15.524  12.548  -1.277  0.44 51.32  ? 381 GLU D CD  1 
ATOM   12086 C  CD  B GLU D 1 380 ? 13.280  12.719  -3.316  0.56 57.97  ? 381 GLU D CD  1 
ATOM   12087 O  OE1 A GLU D 1 380 ? 16.508  11.895  -0.868  0.44 52.25  ? 381 GLU D OE1 1 
ATOM   12088 O  OE1 B GLU D 1 380 ? 13.845  13.338  -2.390  0.56 60.56  ? 381 GLU D OE1 1 
ATOM   12089 O  OE2 A GLU D 1 380 ? 15.165  13.629  -0.764  0.44 49.43  ? 381 GLU D OE2 1 
ATOM   12090 O  OE2 B GLU D 1 380 ? 12.573  13.285  -4.176  0.56 59.46  ? 381 GLU D OE2 1 
ATOM   12091 N  N   . ALA D 1 381 ? 11.878  8.613   -1.289  1.00 41.59  ? 382 ALA D N   1 
ATOM   12092 C  CA  . ALA D 1 381 ? 10.664  7.855   -1.586  1.00 42.09  ? 382 ALA D CA  1 
ATOM   12093 C  C   . ALA D 1 381 ? 9.574   8.118   -0.558  1.00 42.48  ? 382 ALA D C   1 
ATOM   12094 O  O   . ALA D 1 381 ? 8.418   8.325   -0.914  1.00 38.51  ? 382 ALA D O   1 
ATOM   12095 C  CB  . ALA D 1 381 ? 10.966  6.368   -1.654  1.00 39.35  ? 382 ALA D CB  1 
ATOM   12096 N  N   . LYS D 1 382 ? 9.947   8.100   0.717   1.00 41.48  ? 383 LYS D N   1 
ATOM   12097 C  CA  . LYS D 1 382 ? 9.010   8.398   1.789   1.00 42.24  ? 383 LYS D CA  1 
ATOM   12098 C  C   . LYS D 1 382 ? 8.429   9.794   1.610   1.00 46.41  ? 383 LYS D C   1 
ATOM   12099 O  O   . LYS D 1 382 ? 7.214   9.987   1.721   1.00 49.00  ? 383 LYS D O   1 
ATOM   12100 C  CB  . LYS D 1 382 ? 9.690   8.275   3.153   1.00 41.41  ? 383 LYS D CB  1 
ATOM   12101 C  CG  . LYS D 1 382 ? 9.762   6.854   3.683   1.00 38.20  ? 383 LYS D CG  1 
ATOM   12102 C  CD  . LYS D 1 382 ? 10.210  6.839   5.133   1.00 43.27  ? 383 LYS D CD  1 
ATOM   12103 C  CE  . LYS D 1 382 ? 10.187  5.434   5.706   1.00 53.03  ? 383 LYS D CE  1 
ATOM   12104 N  NZ  . LYS D 1 382 ? 10.518  5.436   7.157   1.00 58.90  ? 383 LYS D NZ  1 
ATOM   12105 N  N   . ALA D 1 383 ? 9.297   10.760  1.315   1.00 42.22  ? 384 ALA D N   1 
ATOM   12106 C  CA  . ALA D 1 383 ? 8.843   12.133  1.084   1.00 43.64  ? 384 ALA D CA  1 
ATOM   12107 C  C   . ALA D 1 383 ? 7.814   12.210  -0.049  1.00 41.57  ? 384 ALA D C   1 
ATOM   12108 O  O   . ALA D 1 383 ? 6.712   12.747  0.129   1.00 42.20  ? 384 ALA D O   1 
ATOM   12109 C  CB  . ALA D 1 383 ? 10.028  13.037  0.782   1.00 39.37  ? 384 ALA D CB  1 
ATOM   12110 N  N   . GLN D 1 384 ? 8.180   11.664  -1.206  1.00 40.64  ? 385 GLN D N   1 
ATOM   12111 C  CA  . GLN D 1 384 ? 7.313   11.662  -2.382  1.00 41.62  ? 385 GLN D CA  1 
ATOM   12112 C  C   . GLN D 1 384 ? 5.967   11.003  -2.100  1.00 41.56  ? 385 GLN D C   1 
ATOM   12113 O  O   . GLN D 1 384 ? 4.915   11.571  -2.390  1.00 42.74  ? 385 GLN D O   1 
ATOM   12114 C  CB  . GLN D 1 384 ? 7.995   10.944  -3.550  1.00 45.24  ? 385 GLN D CB  1 
ATOM   12115 C  CG  . GLN D 1 384 ? 9.376   11.469  -3.905  1.00 49.63  ? 385 GLN D CG  1 
ATOM   12116 C  CD  . GLN D 1 384 ? 9.352   12.485  -5.027  1.00 57.40  ? 385 GLN D CD  1 
ATOM   12117 O  OE1 . GLN D 1 384 ? 8.396   13.247  -5.171  1.00 55.38  ? 385 GLN D OE1 1 
ATOM   12118 N  NE2 . GLN D 1 384 ? 10.409  12.500  -5.832  1.00 58.85  ? 385 GLN D NE2 1 
ATOM   12119 N  N   . LEU D 1 385 ? 6.012   9.800   -1.536  1.00 44.89  ? 386 LEU D N   1 
ATOM   12120 C  CA  . LEU D 1 385 ? 4.807   9.029   -1.256  1.00 45.58  ? 386 LEU D CA  1 
ATOM   12121 C  C   . LEU D 1 385 ? 3.894   9.750   -0.275  1.00 47.66  ? 386 LEU D C   1 
ATOM   12122 O  O   . LEU D 1 385 ? 2.679   9.794   -0.470  1.00 51.00  ? 386 LEU D O   1 
ATOM   12123 C  CB  . LEU D 1 385 ? 5.169   7.644   -0.715  1.00 43.70  ? 386 LEU D CB  1 
ATOM   12124 C  CG  . LEU D 1 385 ? 5.846   6.691   -1.702  1.00 42.09  ? 386 LEU D CG  1 
ATOM   12125 C  CD1 . LEU D 1 385 ? 5.973   5.299   -1.105  1.00 45.01  ? 386 LEU D CD1 1 
ATOM   12126 C  CD2 . LEU D 1 385 ? 5.086   6.648   -3.018  1.00 43.91  ? 386 LEU D CD2 1 
ATOM   12127 N  N   . ARG D 1 386 ? 4.474   10.319  0.777   1.00 47.79  ? 387 ARG D N   1 
ATOM   12128 C  CA  . ARG D 1 386 ? 3.675   11.060  1.745   1.00 50.98  ? 387 ARG D CA  1 
ATOM   12129 C  C   . ARG D 1 386 ? 3.094   12.324  1.114   1.00 56.57  ? 387 ARG D C   1 
ATOM   12130 O  O   . ARG D 1 386 ? 2.029   12.792  1.516   1.00 52.75  ? 387 ARG D O   1 
ATOM   12131 C  CB  . ARG D 1 386 ? 4.502   11.412  2.982   1.00 56.40  ? 387 ARG D CB  1 
ATOM   12132 C  CG  . ARG D 1 386 ? 4.793   10.225  3.888   1.00 67.00  ? 387 ARG D CG  1 
ATOM   12133 C  CD  . ARG D 1 386 ? 3.525   9.439   4.197   1.00 72.12  ? 387 ARG D CD  1 
ATOM   12134 N  NE  . ARG D 1 386 ? 3.727   8.466   5.267   1.00 78.83  ? 387 ARG D NE  1 
ATOM   12135 C  CZ  . ARG D 1 386 ? 3.178   7.255   5.291   1.00 81.01  ? 387 ARG D CZ  1 
ATOM   12136 N  NH1 . ARG D 1 386 ? 2.394   6.858   4.297   1.00 82.96  ? 387 ARG D NH1 1 
ATOM   12137 N  NH2 . ARG D 1 386 ? 3.417   6.437   6.307   1.00 79.54  ? 387 ARG D NH2 1 
ATOM   12138 N  N   . ASP D 1 387 ? 3.789   12.868  0.119   1.00 55.27  ? 388 ASP D N   1 
ATOM   12139 C  CA  . ASP D 1 387 ? 3.298   14.054  -0.577  1.00 54.96  ? 388 ASP D CA  1 
ATOM   12140 C  C   . ASP D 1 387 ? 2.090   13.753  -1.471  1.00 54.23  ? 388 ASP D C   1 
ATOM   12141 O  O   . ASP D 1 387 ? 1.206   14.598  -1.635  1.00 57.78  ? 388 ASP D O   1 
ATOM   12142 C  CB  . ASP D 1 387 ? 4.418   14.682  -1.411  1.00 57.83  ? 388 ASP D CB  1 
ATOM   12143 C  CG  . ASP D 1 387 ? 3.944   15.873  -2.222  1.00 64.49  ? 388 ASP D CG  1 
ATOM   12144 O  OD1 . ASP D 1 387 ? 3.560   16.895  -1.615  1.00 68.01  ? 388 ASP D OD1 1 
ATOM   12145 O  OD2 . ASP D 1 387 ? 3.960   15.788  -3.468  1.00 68.15  ? 388 ASP D OD2 1 
ATOM   12146 N  N   . VAL D 1 388 ? 2.049   12.550  -2.038  1.00 55.06  ? 389 VAL D N   1 
ATOM   12147 C  CA  . VAL D 1 388 ? 0.994   12.183  -2.982  1.00 46.98  ? 389 VAL D CA  1 
ATOM   12148 C  C   . VAL D 1 388 ? -0.079  11.298  -2.354  1.00 43.37  ? 389 VAL D C   1 
ATOM   12149 O  O   . VAL D 1 388 ? -0.884  10.690  -3.060  1.00 44.10  ? 389 VAL D O   1 
ATOM   12150 C  CB  . VAL D 1 388 ? 1.570   11.450  -4.209  1.00 41.99  ? 389 VAL D CB  1 
ATOM   12151 C  CG1 . VAL D 1 388 ? 2.504   12.367  -4.983  1.00 39.20  ? 389 VAL D CG1 1 
ATOM   12152 C  CG2 . VAL D 1 388 ? 2.285   10.177  -3.782  1.00 35.53  ? 389 VAL D CG2 1 
ATOM   12153 N  N   . GLN D 1 389 ? -0.087  11.229  -1.027  1.00 35.43  ? 390 GLN D N   1 
ATOM   12154 C  CA  . GLN D 1 389 ? -1.068  10.429  -0.304  1.00 35.38  ? 390 GLN D CA  1 
ATOM   12155 C  C   . GLN D 1 389 ? -2.479  10.986  -0.502  1.00 43.09  ? 390 GLN D C   1 
ATOM   12156 O  O   . GLN D 1 389 ? -3.457  10.240  -0.539  1.00 42.16  ? 390 GLN D O   1 
ATOM   12157 C  CB  . GLN D 1 389 ? -0.718  10.385  1.186   1.00 35.74  ? 390 GLN D CB  1 
ATOM   12158 C  CG  . GLN D 1 389 ? -1.434  9.300   1.976   1.00 59.83  ? 390 GLN D CG  1 
ATOM   12159 C  CD  . GLN D 1 389 ? -0.550  8.097   2.247   1.00 63.07  ? 390 GLN D CD  1 
ATOM   12160 O  OE1 . GLN D 1 389 ? 0.507   7.937   1.635   1.00 59.17  ? 390 GLN D OE1 1 
ATOM   12161 N  NE2 . GLN D 1 389 ? -0.976  7.246   3.174   1.00 58.00  ? 390 GLN D NE2 1 
ATOM   12162 N  N   . ASP D 1 390 ? -2.565  12.306  -0.636  1.00 46.61  ? 391 ASP D N   1 
ATOM   12163 C  CA  . ASP D 1 390 ? -3.839  13.012  -0.734  1.00 42.98  ? 391 ASP D CA  1 
ATOM   12164 C  C   . ASP D 1 390 ? -4.286  13.245  -2.176  1.00 40.99  ? 391 ASP D C   1 
ATOM   12165 O  O   . ASP D 1 390 ? -5.305  13.892  -2.414  1.00 37.29  ? 391 ASP D O   1 
ATOM   12166 C  CB  . ASP D 1 390 ? -3.744  14.359  -0.008  1.00 51.67  ? 391 ASP D CB  1 
ATOM   12167 C  CG  . ASP D 1 390 ? -2.573  15.208  -0.494  1.00 64.03  ? 391 ASP D CG  1 
ATOM   12168 O  OD1 . ASP D 1 390 ? -2.023  14.918  -1.577  1.00 69.50  ? 391 ASP D OD1 1 
ATOM   12169 O  OD2 . ASP D 1 390 ? -2.198  16.170  0.208   1.00 69.71  ? 391 ASP D OD2 1 
ATOM   12170 N  N   . PHE D 1 391 ? -3.512  12.720  -3.124  1.00 41.29  ? 392 PHE D N   1 
ATOM   12171 C  CA  . PHE D 1 391 ? -3.624  13.096  -4.535  1.00 34.93  ? 392 PHE D CA  1 
ATOM   12172 C  C   . PHE D 1 391 ? -5.037  13.072  -5.117  1.00 39.67  ? 392 PHE D C   1 
ATOM   12173 O  O   . PHE D 1 391 ? -5.424  13.986  -5.843  1.00 40.60  ? 392 PHE D O   1 
ATOM   12174 C  CB  . PHE D 1 391 ? -2.734  12.189  -5.388  1.00 34.95  ? 392 PHE D CB  1 
ATOM   12175 C  CG  . PHE D 1 391 ? -2.805  12.486  -6.859  1.00 35.07  ? 392 PHE D CG  1 
ATOM   12176 C  CD1 . PHE D 1 391 ? -2.119  13.564  -7.394  1.00 36.22  ? 392 PHE D CD1 1 
ATOM   12177 C  CD2 . PHE D 1 391 ? -3.564  11.694  -7.706  1.00 35.09  ? 392 PHE D CD2 1 
ATOM   12178 C  CE1 . PHE D 1 391 ? -2.185  13.846  -8.747  1.00 35.54  ? 392 PHE D CE1 1 
ATOM   12179 C  CE2 . PHE D 1 391 ? -3.635  11.971  -9.060  1.00 35.33  ? 392 PHE D CE2 1 
ATOM   12180 C  CZ  . PHE D 1 391 ? -2.944  13.048  -9.581  1.00 38.16  ? 392 PHE D CZ  1 
ATOM   12181 N  N   . TRP D 1 392 ? -5.806  12.035  -4.804  1.00 39.02  ? 393 TRP D N   1 
ATOM   12182 C  CA  . TRP D 1 392 ? -7.090  11.840  -5.466  1.00 42.23  ? 393 TRP D CA  1 
ATOM   12183 C  C   . TRP D 1 392 ? -8.192  12.770  -4.952  1.00 46.69  ? 393 TRP D C   1 
ATOM   12184 O  O   . TRP D 1 392 ? -9.094  13.135  -5.705  1.00 46.51  ? 393 TRP D O   1 
ATOM   12185 C  CB  . TRP D 1 392 ? -7.528  10.380  -5.336  1.00 41.65  ? 393 TRP D CB  1 
ATOM   12186 C  CG  . TRP D 1 392 ? -6.607  9.435   -6.051  1.00 43.54  ? 393 TRP D CG  1 
ATOM   12187 C  CD1 . TRP D 1 392 ? -5.812  8.480   -5.490  1.00 41.36  ? 393 TRP D CD1 1 
ATOM   12188 C  CD2 . TRP D 1 392 ? -6.369  9.376   -7.464  1.00 41.49  ? 393 TRP D CD2 1 
ATOM   12189 N  NE1 . TRP D 1 392 ? -5.101  7.822   -6.465  1.00 43.39  ? 393 TRP D NE1 1 
ATOM   12190 C  CE2 . TRP D 1 392 ? -5.425  8.354   -7.686  1.00 38.79  ? 393 TRP D CE2 1 
ATOM   12191 C  CE3 . TRP D 1 392 ? -6.865  10.086  -8.563  1.00 38.53  ? 393 TRP D CE3 1 
ATOM   12192 C  CZ2 . TRP D 1 392 ? -4.968  8.022   -8.960  1.00 37.65  ? 393 TRP D CZ2 1 
ATOM   12193 C  CZ3 . TRP D 1 392 ? -6.411  9.755   -9.827  1.00 38.37  ? 393 TRP D CZ3 1 
ATOM   12194 C  CH2 . TRP D 1 392 ? -5.472  8.732   -10.015 1.00 35.76  ? 393 TRP D CH2 1 
ATOM   12195 N  N   . ILE D 1 393 ? -8.127  13.152  -3.680  1.00 43.21  ? 394 ILE D N   1 
ATOM   12196 C  CA  . ILE D 1 393 ? -9.125  14.062  -3.121  1.00 42.95  ? 394 ILE D CA  1 
ATOM   12197 C  C   . ILE D 1 393 ? -8.679  15.521  -3.141  1.00 43.73  ? 394 ILE D C   1 
ATOM   12198 O  O   . ILE D 1 393 ? -9.439  16.409  -2.755  1.00 46.32  ? 394 ILE D O   1 
ATOM   12199 C  CB  . ILE D 1 393 ? -9.479  13.694  -1.668  1.00 43.25  ? 394 ILE D CB  1 
ATOM   12200 C  CG1 . ILE D 1 393 ? -8.238  13.788  -0.778  1.00 40.33  ? 394 ILE D CG1 1 
ATOM   12201 C  CG2 . ILE D 1 393 ? -10.102 12.307  -1.603  1.00 38.43  ? 394 ILE D CG2 1 
ATOM   12202 C  CD1 . ILE D 1 393 ? -8.536  13.650  0.697   1.00 37.68  ? 394 ILE D CD1 1 
ATOM   12203 N  N   . SER D 1 394 ? -7.455  15.772  -3.593  1.00 43.25  ? 395 SER D N   1 
ATOM   12204 C  CA  . SER D 1 394 ? -6.908  17.124  -3.561  1.00 43.58  ? 395 SER D CA  1 
ATOM   12205 C  C   . SER D 1 394 ? -6.898  17.769  -4.942  1.00 44.45  ? 395 SER D C   1 
ATOM   12206 O  O   . SER D 1 394 ? -6.492  18.922  -5.092  1.00 49.39  ? 395 SER D O   1 
ATOM   12207 C  CB  . SER D 1 394 ? -5.492  17.115  -2.980  1.00 44.06  ? 395 SER D CB  1 
ATOM   12208 O  OG  . SER D 1 394 ? -4.596  16.426  -3.833  1.00 45.07  ? 395 SER D OG  1 
ATOM   12209 N  N   . LEU D 1 395 ? -7.344  17.021  -5.946  1.00 42.54  ? 396 LEU D N   1 
ATOM   12210 C  CA  . LEU D 1 395 ? -7.439  17.540  -7.308  1.00 45.63  ? 396 LEU D CA  1 
ATOM   12211 C  C   . LEU D 1 395 ? -8.313  18.800  -7.419  1.00 47.95  ? 396 LEU D C   1 
ATOM   12212 O  O   . LEU D 1 395 ? -7.907  19.761  -8.073  1.00 48.49  ? 396 LEU D O   1 
ATOM   12213 C  CB  . LEU D 1 395 ? -7.961  16.458  -8.259  1.00 51.74  ? 396 LEU D CB  1 
ATOM   12214 C  CG  . LEU D 1 395 ? -7.120  15.189  -8.399  1.00 53.52  ? 396 LEU D CG  1 
ATOM   12215 C  CD1 . LEU D 1 395 ? -7.841  14.166  -9.263  1.00 52.54  ? 396 LEU D CD1 1 
ATOM   12216 C  CD2 . LEU D 1 395 ? -5.752  15.515  -8.977  1.00 51.53  ? 396 LEU D CD2 1 
ATOM   12217 N  N   . PRO D 1 396 ? -9.510  18.809  -6.791  1.00 46.47  ? 397 PRO D N   1 
ATOM   12218 C  CA  . PRO D 1 396 ? -10.300 20.042  -6.891  1.00 49.50  ? 397 PRO D CA  1 
ATOM   12219 C  C   . PRO D 1 396 ? -9.588  21.276  -6.340  1.00 51.82  ? 397 PRO D C   1 
ATOM   12220 O  O   . PRO D 1 396 ? -9.546  22.283  -7.034  1.00 54.56  ? 397 PRO D O   1 
ATOM   12221 C  CB  . PRO D 1 396 ? -11.546 19.725  -6.061  1.00 47.46  ? 397 PRO D CB  1 
ATOM   12222 C  CG  . PRO D 1 396 ? -11.685 18.258  -6.160  1.00 35.37  ? 397 PRO D CG  1 
ATOM   12223 C  CD  . PRO D 1 396 ? -10.280 17.735  -6.134  1.00 48.63  ? 397 PRO D CD  1 
ATOM   12224 N  N   . GLY D 1 397 ? -9.039  21.199  -5.132  1.00 53.88  ? 398 GLY D N   1 
ATOM   12225 C  CA  . GLY D 1 397 ? -8.338  22.331  -4.550  1.00 54.02  ? 398 GLY D CA  1 
ATOM   12226 C  C   . GLY D 1 397 ? -7.165  22.772  -5.407  1.00 56.82  ? 398 GLY D C   1 
ATOM   12227 O  O   . GLY D 1 397 ? -6.990  23.965  -5.691  1.00 56.66  ? 398 GLY D O   1 
ATOM   12228 N  N   . THR D 1 398 ? -6.372  21.792  -5.831  1.00 56.66  ? 399 THR D N   1 
ATOM   12229 C  CA  . THR D 1 398 ? -5.204  22.037  -6.665  1.00 60.46  ? 399 THR D CA  1 
ATOM   12230 C  C   . THR D 1 398 ? -5.569  22.776  -7.947  1.00 60.92  ? 399 THR D C   1 
ATOM   12231 O  O   . THR D 1 398 ? -5.066  23.868  -8.199  1.00 66.25  ? 399 THR D O   1 
ATOM   12232 C  CB  . THR D 1 398 ? -4.488  20.722  -7.036  1.00 61.44  ? 399 THR D CB  1 
ATOM   12233 O  OG1 . THR D 1 398 ? -4.026  20.071  -5.846  1.00 64.11  ? 399 THR D OG1 1 
ATOM   12234 C  CG2 . THR D 1 398 ? -3.303  21.000  -7.947  1.00 60.10  ? 399 THR D CG2 1 
ATOM   12235 N  N   . LEU D 1 399 ? -6.454  22.186  -8.746  1.00 58.60  ? 400 LEU D N   1 
ATOM   12236 C  CA  . LEU D 1 399 ? -6.822  22.768  -10.034 1.00 58.33  ? 400 LEU D CA  1 
ATOM   12237 C  C   . LEU D 1 399 ? -7.582  24.083  -9.888  1.00 56.81  ? 400 LEU D C   1 
ATOM   12238 O  O   . LEU D 1 399 ? -7.498  24.952  -10.755 1.00 53.78  ? 400 LEU D O   1 
ATOM   12239 C  CB  . LEU D 1 399 ? -7.659  21.782  -10.847 1.00 61.16  ? 400 LEU D CB  1 
ATOM   12240 C  CG  . LEU D 1 399 ? -7.102  20.367  -11.001 1.00 66.05  ? 400 LEU D CG  1 
ATOM   12241 C  CD1 . LEU D 1 399 ? -8.110  19.494  -11.718 1.00 65.93  ? 400 LEU D CD1 1 
ATOM   12242 C  CD2 . LEU D 1 399 ? -5.768  20.371  -11.733 1.00 66.60  ? 400 LEU D CD2 1 
ATOM   12243 N  N   . CYS D 1 400 ? -8.329  24.226  -8.799  1.00 56.14  ? 401 CYS D N   1 
ATOM   12244 C  CA  . CYS D 1 400 ? -9.074  25.457  -8.561  1.00 62.00  ? 401 CYS D CA  1 
ATOM   12245 C  C   . CYS D 1 400 ? -8.137  26.612  -8.244  1.00 67.39  ? 401 CYS D C   1 
ATOM   12246 O  O   . CYS D 1 400 ? -8.204  27.662  -8.885  1.00 68.26  ? 401 CYS D O   1 
ATOM   12247 C  CB  . CYS D 1 400 ? -10.085 25.280  -7.426  1.00 62.09  ? 401 CYS D CB  1 
ATOM   12248 S  SG  . CYS D 1 400 ? -11.604 24.430  -7.912  1.00 70.33  ? 401 CYS D SG  1 
ATOM   12249 N  N   . SER D 1 401 ? -7.261  26.419  -7.262  1.00 67.81  ? 402 SER D N   1 
ATOM   12250 C  CA  . SER D 1 401 ? -6.350  27.488  -6.866  1.00 73.19  ? 402 SER D CA  1 
ATOM   12251 C  C   . SER D 1 401 ? -5.320  27.770  -7.959  1.00 78.78  ? 402 SER D C   1 
ATOM   12252 O  O   . SER D 1 401 ? -4.932  28.918  -8.170  1.00 82.14  ? 402 SER D O   1 
ATOM   12253 C  CB  . SER D 1 401 ? -5.647  27.146  -5.550  1.00 69.33  ? 402 SER D CB  1 
ATOM   12254 O  OG  . SER D 1 401 ? -4.395  26.525  -5.781  1.00 69.87  ? 402 SER D OG  1 
ATOM   12255 N  N   . GLU D 1 402 ? -4.888  26.725  -8.660  1.00 82.07  ? 403 GLU D N   1 
ATOM   12256 C  CA  . GLU D 1 402 ? -3.901  26.889  -9.725  1.00 87.43  ? 403 GLU D CA  1 
ATOM   12257 C  C   . GLU D 1 402 ? -4.457  27.746  -10.858 1.00 91.18  ? 403 GLU D C   1 
ATOM   12258 O  O   . GLU D 1 402 ? -3.743  28.571  -11.428 1.00 94.58  ? 403 GLU D O   1 
ATOM   12259 C  CB  . GLU D 1 402 ? -3.420  25.515  -10.242 1.00 88.82  ? 403 GLU D CB  1 
ATOM   12260 C  CG  . GLU D 1 402 ? -2.953  25.463  -11.705 1.00 92.11  ? 403 GLU D CG  1 
ATOM   12261 C  CD  . GLU D 1 402 ? -4.096  25.320  -12.708 1.00 94.32  ? 403 GLU D CD  1 
ATOM   12262 O  OE1 . GLU D 1 402 ? -5.169  24.799  -12.331 1.00 94.92  ? 403 GLU D OE1 1 
ATOM   12263 O  OE2 . GLU D 1 402 ? -3.928  25.757  -13.866 1.00 95.41  ? 403 GLU D OE2 1 
ATOM   12264 N  N   . LYS D 1 403 ? -5.736  27.571  -11.164 1.00 92.25  ? 404 LYS D N   1 
ATOM   12265 C  CA  . LYS D 1 403 ? -6.338  28.252  -12.301 1.00 92.03  ? 404 LYS D CA  1 
ATOM   12266 C  C   . LYS D 1 403 ? -7.437  29.227  -11.905 1.00 94.38  ? 404 LYS D C   1 
ATOM   12267 O  O   . LYS D 1 403 ? -7.212  30.426  -11.724 1.00 95.74  ? 404 LYS D O   1 
ATOM   12268 C  CB  . LYS D 1 403 ? -6.918  27.218  -13.269 1.00 89.90  ? 404 LYS D CB  1 
ATOM   12269 C  CG  . LYS D 1 403 ? -6.895  27.591  -14.748 1.00 88.49  ? 404 LYS D CG  1 
ATOM   12270 C  CD  . LYS D 1 403 ? -6.973  26.322  -15.595 1.00 84.34  ? 404 LYS D CD  1 
ATOM   12271 C  CE  . LYS D 1 403 ? -6.799  26.613  -17.073 1.00 84.43  ? 404 LYS D CE  1 
ATOM   12272 N  NZ  . LYS D 1 403 ? -6.247  27.976  -17.296 1.00 83.44  ? 404 LYS D NZ  1 
ATOM   12273 N  N   . MET D 1 404 ? -8.631  28.668  -11.758 1.00 93.69  ? 405 MET D N   1 
ATOM   12274 C  CA  . MET D 1 404 ? -9.875  29.421  -11.785 1.00 92.73  ? 405 MET D CA  1 
ATOM   12275 C  C   . MET D 1 404 ? -10.147 30.271  -10.545 1.00 92.99  ? 405 MET D C   1 
ATOM   12276 O  O   . MET D 1 404 ? -10.524 31.437  -10.667 1.00 94.37  ? 405 MET D O   1 
ATOM   12277 C  CB  . MET D 1 404 ? -11.028 28.443  -12.016 1.00 89.48  ? 405 MET D CB  1 
ATOM   12278 C  CG  . MET D 1 404 ? -10.572 27.120  -12.621 1.00 87.69  ? 405 MET D CG  1 
ATOM   12279 S  SD  . MET D 1 404 ? -11.872 25.880  -12.735 1.00 137.41 ? 405 MET D SD  1 
ATOM   12280 C  CE  . MET D 1 404 ? -10.964 24.505  -13.434 1.00 39.04  ? 405 MET D CE  1 
ATOM   12281 N  N   . ALA D 1 405 ? -9.955  29.691  -9.364  1.00 89.75  ? 406 ALA D N   1 
ATOM   12282 C  CA  . ALA D 1 405 ? -10.283 30.367  -8.108  1.00 88.44  ? 406 ALA D CA  1 
ATOM   12283 C  C   . ALA D 1 405 ? -9.578  31.713  -7.973  1.00 85.93  ? 406 ALA D C   1 
ATOM   12284 O  O   . ALA D 1 405 ? -10.174 32.761  -8.224  1.00 83.57  ? 406 ALA D O   1 
ATOM   12285 C  CB  . ALA D 1 405 ? -9.938  29.474  -6.924  1.00 87.70  ? 406 ALA D CB  1 
ATOM   12286 N  N   . ASP D 1 412 ? -14.823 40.507  -2.017  1.00 103.74 ? 413 ASP D N   1 
ATOM   12287 C  CA  . ASP D 1 412 ? -15.498 39.218  -2.110  1.00 101.61 ? 413 ASP D CA  1 
ATOM   12288 C  C   . ASP D 1 412 ? -16.593 39.238  -3.173  1.00 97.03  ? 413 ASP D C   1 
ATOM   12289 O  O   . ASP D 1 412 ? -17.685 38.708  -2.963  1.00 99.75  ? 413 ASP D O   1 
ATOM   12290 C  CB  . ASP D 1 412 ? -16.087 38.822  -0.755  1.00 102.70 ? 413 ASP D CB  1 
ATOM   12291 N  N   . ARG D 1 413 ? -16.297 39.860  -4.310  1.00 89.97  ? 414 ARG D N   1 
ATOM   12292 C  CA  . ARG D 1 413 ? -17.205 39.836  -5.448  1.00 80.98  ? 414 ARG D CA  1 
ATOM   12293 C  C   . ARG D 1 413 ? -16.693 38.838  -6.479  1.00 73.42  ? 414 ARG D C   1 
ATOM   12294 O  O   . ARG D 1 413 ? -15.679 39.073  -7.137  1.00 74.20  ? 414 ARG D O   1 
ATOM   12295 C  CB  . ARG D 1 413 ? -17.345 41.229  -6.067  1.00 83.18  ? 414 ARG D CB  1 
ATOM   12296 N  N   . CYS D 1 414 ? -17.414 37.731  -6.628  1.00 65.51  ? 415 CYS D N   1 
ATOM   12297 C  CA  . CYS D 1 414 ? -16.974 36.629  -7.475  1.00 59.44  ? 415 CYS D CA  1 
ATOM   12298 C  C   . CYS D 1 414 ? -18.131 36.047  -8.279  1.00 55.28  ? 415 CYS D C   1 
ATOM   12299 O  O   . CYS D 1 414 ? -19.295 36.342  -8.012  1.00 60.99  ? 415 CYS D O   1 
ATOM   12300 C  CB  . CYS D 1 414 ? -16.322 35.534  -6.629  1.00 56.76  ? 415 CYS D CB  1 
ATOM   12301 S  SG  . CYS D 1 414 ? -17.454 34.702  -5.494  1.00 80.90  ? 415 CYS D SG  1 
ATOM   12302 N  N   . TRP D 1 415 ? -17.804 35.215  -9.262  1.00 53.32  ? 416 TRP D N   1 
ATOM   12303 C  CA  . TRP D 1 415 ? -18.814 34.631  -10.136 1.00 50.86  ? 416 TRP D CA  1 
ATOM   12304 C  C   . TRP D 1 415 ? -19.419 33.366  -9.529  1.00 52.53  ? 416 TRP D C   1 
ATOM   12305 O  O   . TRP D 1 415 ? -18.724 32.370  -9.326  1.00 50.92  ? 416 TRP D O   1 
ATOM   12306 C  CB  . TRP D 1 415 ? -18.195 34.322  -11.500 1.00 53.95  ? 416 TRP D CB  1 
ATOM   12307 C  CG  . TRP D 1 415 ? -19.066 33.514  -12.397 1.00 55.89  ? 416 TRP D CG  1 
ATOM   12308 C  CD1 . TRP D 1 415 ? -18.948 32.183  -12.673 1.00 56.74  ? 416 TRP D CD1 1 
ATOM   12309 C  CD2 . TRP D 1 415 ? -20.193 33.981  -13.145 1.00 58.72  ? 416 TRP D CD2 1 
ATOM   12310 N  NE1 . TRP D 1 415 ? -19.932 31.792  -13.547 1.00 56.36  ? 416 TRP D NE1 1 
ATOM   12311 C  CE2 . TRP D 1 415 ? -20.710 32.878  -13.853 1.00 59.06  ? 416 TRP D CE2 1 
ATOM   12312 C  CE3 . TRP D 1 415 ? -20.815 35.225  -13.285 1.00 56.79  ? 416 TRP D CE3 1 
ATOM   12313 C  CZ2 . TRP D 1 415 ? -21.821 32.981  -14.687 1.00 60.47  ? 416 TRP D CZ2 1 
ATOM   12314 C  CZ3 . TRP D 1 415 ? -21.915 35.325  -14.115 1.00 58.85  ? 416 TRP D CZ3 1 
ATOM   12315 C  CH2 . TRP D 1 415 ? -22.408 34.210  -14.804 1.00 59.57  ? 416 TRP D CH2 1 
ATOM   12316 N  N   . ASN D 1 416 ? -20.720 33.411  -9.248  1.00 49.79  ? 417 ASN D N   1 
ATOM   12317 C  CA  . ASN D 1 416 ? -21.416 32.281  -8.632  1.00 49.12  ? 417 ASN D CA  1 
ATOM   12318 C  C   . ASN D 1 416 ? -22.155 31.383  -9.625  1.00 47.71  ? 417 ASN D C   1 
ATOM   12319 O  O   . ASN D 1 416 ? -22.760 30.385  -9.235  1.00 46.92  ? 417 ASN D O   1 
ATOM   12320 C  CB  . ASN D 1 416 ? -22.392 32.785  -7.557  1.00 49.46  ? 417 ASN D CB  1 
ATOM   12321 C  CG  . ASN D 1 416 ? -23.465 33.716  -8.111  1.00 50.08  ? 417 ASN D CG  1 
ATOM   12322 O  OD1 . ASN D 1 416 ? -23.973 33.525  -9.216  1.00 40.18  ? 417 ASN D OD1 1 
ATOM   12323 N  ND2 . ASN D 1 416 ? -23.817 34.731  -7.330  1.00 51.34  ? 417 ASN D ND2 1 
ATOM   12324 N  N   . GLY D 1 417 ? -22.104 31.739  -10.905 1.00 47.30  ? 418 GLY D N   1 
ATOM   12325 C  CA  . GLY D 1 417 ? -22.836 31.014  -11.928 1.00 45.23  ? 418 GLY D CA  1 
ATOM   12326 C  C   . GLY D 1 417 ? -24.033 31.792  -12.443 1.00 52.00  ? 418 GLY D C   1 
ATOM   12327 O  O   . GLY D 1 417 ? -24.610 31.454  -13.477 1.00 52.68  ? 418 GLY D O   1 
ATOM   12328 N  N   . MET D 1 418 ? -24.406 32.839  -11.712 1.00 52.58  ? 419 MET D N   1 
ATOM   12329 C  CA  . MET D 1 418 ? -25.457 33.757  -12.140 1.00 51.86  ? 419 MET D CA  1 
ATOM   12330 C  C   . MET D 1 418 ? -24.872 35.141  -12.413 1.00 57.99  ? 419 MET D C   1 
ATOM   12331 O  O   . MET D 1 418 ? -24.921 35.633  -13.540 1.00 61.49  ? 419 MET D O   1 
ATOM   12332 C  CB  . MET D 1 418 ? -26.574 33.841  -11.096 1.00 49.21  ? 419 MET D CB  1 
ATOM   12333 C  CG  . MET D 1 418 ? -27.649 32.775  -11.257 1.00 48.92  ? 419 MET D CG  1 
ATOM   12334 S  SD  . MET D 1 418 ? -28.810 32.675  -9.878  1.00 118.56 ? 419 MET D SD  1 
ATOM   12335 C  CE  . MET D 1 418 ? -27.950 33.604  -8.612  1.00 53.71  ? 419 MET D CE  1 
ATOM   12336 N  N   . ALA D 1 419 ? -24.338 35.773  -11.373 1.00 56.45  ? 420 ALA D N   1 
ATOM   12337 C  CA  . ALA D 1 419 ? -23.685 37.070  -11.518 1.00 54.63  ? 420 ALA D CA  1 
ATOM   12338 C  C   . ALA D 1 419 ? -22.433 37.166  -10.651 1.00 58.80  ? 420 ALA D C   1 
ATOM   12339 O  O   . ALA D 1 419 ? -22.042 36.196  -10.000 1.00 55.75  ? 420 ALA D O   1 
ATOM   12340 C  CB  . ALA D 1 419 ? -24.652 38.188  -11.170 1.00 57.71  ? 420 ALA D CB  1 
ATOM   12341 N  N   . ARG D 1 420 ? -21.799 38.336  -10.659 1.00 56.51  ? 421 ARG D N   1 
ATOM   12342 C  CA  . ARG D 1 420 ? -20.700 38.614  -9.743  1.00 55.91  ? 421 ARG D CA  1 
ATOM   12343 C  C   . ARG D 1 420 ? -21.297 38.803  -8.352  1.00 54.18  ? 421 ARG D C   1 
ATOM   12344 O  O   . ARG D 1 420 ? -22.242 39.573  -8.185  1.00 54.42  ? 421 ARG D O   1 
ATOM   12345 C  CB  . ARG D 1 420 ? -19.910 39.850  -10.185 1.00 59.89  ? 421 ARG D CB  1 
ATOM   12346 C  CG  . ARG D 1 420 ? -18.399 39.710  -10.035 1.00 65.44  ? 421 ARG D CG  1 
ATOM   12347 C  CD  . ARG D 1 420 ? -17.656 40.934  -10.560 1.00 70.94  ? 421 ARG D CD  1 
ATOM   12348 N  NE  . ARG D 1 420 ? -17.720 41.046  -12.015 1.00 77.75  ? 421 ARG D NE  1 
ATOM   12349 C  CZ  . ARG D 1 420 ? -17.001 41.903  -12.733 1.00 84.18  ? 421 ARG D CZ  1 
ATOM   12350 N  NH1 . ARG D 1 420 ? -16.153 42.727  -12.132 1.00 87.49  ? 421 ARG D NH1 1 
ATOM   12351 N  NH2 . ARG D 1 420 ? -17.125 41.936  -14.053 1.00 84.33  ? 421 ARG D NH2 1 
ATOM   12352 N  N   . GLY D 1 421 ? -20.766 38.098  -7.357  1.00 51.68  ? 422 GLY D N   1 
ATOM   12353 C  CA  . GLY D 1 421 ? -21.448 38.020  -6.078  1.00 56.95  ? 422 GLY D CA  1 
ATOM   12354 C  C   . GLY D 1 421 ? -20.948 36.972  -5.101  1.00 56.25  ? 422 GLY D C   1 
ATOM   12355 O  O   . GLY D 1 421 ? -19.775 36.611  -5.095  1.00 58.09  ? 422 GLY D O   1 
ATOM   12356 N  N   . ARG D 1 422 ? -21.856 36.534  -4.234  1.00 58.17  ? 423 ARG D N   1 
ATOM   12357 C  CA  . ARG D 1 422 ? -21.599 35.505  -3.227  1.00 57.54  ? 423 ARG D CA  1 
ATOM   12358 C  C   . ARG D 1 422 ? -21.983 34.109  -3.722  1.00 57.36  ? 423 ARG D C   1 
ATOM   12359 O  O   . ARG D 1 422 ? -22.941 33.961  -4.480  1.00 57.10  ? 423 ARG D O   1 
ATOM   12360 C  CB  . ARG D 1 422 ? -22.384 35.816  -1.952  1.00 61.06  ? 423 ARG D CB  1 
ATOM   12361 C  CG  . ARG D 1 422 ? -21.568 35.841  -0.676  1.00 65.86  ? 423 ARG D CG  1 
ATOM   12362 C  CD  . ARG D 1 422 ? -22.488 35.893  0.535   1.00 71.21  ? 423 ARG D CD  1 
ATOM   12363 N  NE  . ARG D 1 422 ? -23.730 36.604  0.243   1.00 73.98  ? 423 ARG D NE  1 
ATOM   12364 C  CZ  . ARG D 1 422 ? -24.878 36.395  0.879   1.00 75.92  ? 423 ARG D CZ  1 
ATOM   12365 N  NH1 . ARG D 1 422 ? -24.949 35.498  1.851   1.00 76.59  ? 423 ARG D NH1 1 
ATOM   12366 N  NH2 . ARG D 1 422 ? -25.958 37.085  0.545   1.00 77.60  ? 423 ARG D NH2 1 
ATOM   12367 N  N   . TYR D 1 423 ? -21.230 33.089  -3.317  1.00 57.20  ? 424 TYR D N   1 
ATOM   12368 C  CA  . TYR D 1 423 ? -21.654 31.710  -3.557  1.00 53.87  ? 424 TYR D CA  1 
ATOM   12369 C  C   . TYR D 1 423 ? -22.217 31.103  -2.274  1.00 53.37  ? 424 TYR D C   1 
ATOM   12370 O  O   . TYR D 1 423 ? -21.480 30.816  -1.330  1.00 55.16  ? 424 TYR D O   1 
ATOM   12371 C  CB  . TYR D 1 423 ? -20.491 30.866  -4.081  1.00 53.92  ? 424 TYR D CB  1 
ATOM   12372 C  CG  . TYR D 1 423 ? -20.861 29.448  -4.469  1.00 56.12  ? 424 TYR D CG  1 
ATOM   12373 C  CD1 . TYR D 1 423 ? -21.464 29.176  -5.690  1.00 56.26  ? 424 TYR D CD1 1 
ATOM   12374 C  CD2 . TYR D 1 423 ? -20.591 28.380  -3.620  1.00 54.25  ? 424 TYR D CD2 1 
ATOM   12375 C  CE1 . TYR D 1 423 ? -21.798 27.882  -6.053  1.00 54.71  ? 424 TYR D CE1 1 
ATOM   12376 C  CE2 . TYR D 1 423 ? -20.921 27.083  -3.974  1.00 53.78  ? 424 TYR D CE2 1 
ATOM   12377 C  CZ  . TYR D 1 423 ? -21.524 26.840  -5.191  1.00 54.34  ? 424 TYR D CZ  1 
ATOM   12378 O  OH  . TYR D 1 423 ? -21.853 25.552  -5.549  1.00 50.36  ? 424 TYR D OH  1 
ATOM   12379 N  N   . LEU D 1 424 ? -23.532 30.912  -2.257  1.00 58.07  ? 425 LEU D N   1 
ATOM   12380 C  CA  . LEU D 1 424 ? -24.243 30.402  -1.084  1.00 57.23  ? 425 LEU D CA  1 
ATOM   12381 C  C   . LEU D 1 424 ? -23.994 28.931  -0.705  1.00 56.22  ? 425 LEU D C   1 
ATOM   12382 O  O   . LEU D 1 424 ? -23.688 28.653  0.455   1.00 59.16  ? 425 LEU D O   1 
ATOM   12383 C  CB  . LEU D 1 424 ? -25.748 30.624  -1.263  1.00 63.85  ? 425 LEU D CB  1 
ATOM   12384 C  CG  . LEU D 1 424 ? -26.212 32.076  -1.152  1.00 68.78  ? 425 LEU D CG  1 
ATOM   12385 C  CD1 . LEU D 1 424 ? -27.720 32.166  -1.304  1.00 72.37  ? 425 LEU D CD1 1 
ATOM   12386 C  CD2 . LEU D 1 424 ? -25.764 32.676  0.172   1.00 71.42  ? 425 LEU D CD2 1 
ATOM   12387 N  N   . PRO D 1 425 ? -24.138 27.986  -1.661  1.00 50.97  ? 426 PRO D N   1 
ATOM   12388 C  CA  . PRO D 1 425 ? -24.146 26.573  -1.255  1.00 52.53  ? 426 PRO D CA  1 
ATOM   12389 C  C   . PRO D 1 425 ? -22.864 26.106  -0.572  1.00 55.80  ? 426 PRO D C   1 
ATOM   12390 O  O   . PRO D 1 425 ? -21.786 26.638  -0.838  1.00 58.83  ? 426 PRO D O   1 
ATOM   12391 C  CB  . PRO D 1 425 ? -24.336 25.825  -2.582  1.00 45.32  ? 426 PRO D CB  1 
ATOM   12392 C  CG  . PRO D 1 425 ? -24.915 26.825  -3.512  1.00 43.86  ? 426 PRO D CG  1 
ATOM   12393 C  CD  . PRO D 1 425 ? -24.286 28.120  -3.122  1.00 46.80  ? 426 PRO D CD  1 
ATOM   12394 N  N   . GLU D 1 426 ? -22.994 25.120  0.309   1.00 58.87  ? 427 GLU D N   1 
ATOM   12395 C  CA  . GLU D 1 426 ? -21.837 24.524  0.960   1.00 58.79  ? 427 GLU D CA  1 
ATOM   12396 C  C   . GLU D 1 426 ? -21.120 23.588  -0.001  1.00 54.64  ? 427 GLU D C   1 
ATOM   12397 O  O   . GLU D 1 426 ? -21.731 23.038  -0.917  1.00 51.75  ? 427 GLU D O   1 
ATOM   12398 C  CB  . GLU D 1 426 ? -22.248 23.762  2.222   1.00 67.75  ? 427 GLU D CB  1 
ATOM   12399 C  CG  . GLU D 1 426 ? -22.780 24.635  3.345   1.00 77.55  ? 427 GLU D CG  1 
ATOM   12400 C  CD  . GLU D 1 426 ? -22.838 23.900  4.670   1.00 87.38  ? 427 GLU D CD  1 
ATOM   12401 O  OE1 . GLU D 1 426 ? -21.776 23.441  5.142   1.00 89.95  ? 427 GLU D OE1 1 
ATOM   12402 O  OE2 . GLU D 1 426 ? -23.944 23.778  5.238   1.00 90.30  ? 427 GLU D OE2 1 
ATOM   12403 N  N   . VAL D 1 427 ? -19.820 23.415  0.210   1.00 52.69  ? 428 VAL D N   1 
ATOM   12404 C  CA  . VAL D 1 427 ? -19.040 22.469  -0.572  1.00 48.77  ? 428 VAL D CA  1 
ATOM   12405 C  C   . VAL D 1 427 ? -19.531 21.059  -0.248  1.00 51.16  ? 428 VAL D C   1 
ATOM   12406 O  O   . VAL D 1 427 ? -20.078 20.823  0.828   1.00 51.93  ? 428 VAL D O   1 
ATOM   12407 C  CB  . VAL D 1 427 ? -17.530 22.607  -0.278  1.00 51.94  ? 428 VAL D CB  1 
ATOM   12408 C  CG1 . VAL D 1 427 ? -16.702 21.771  -1.246  1.00 50.28  ? 428 VAL D CG1 1 
ATOM   12409 C  CG2 . VAL D 1 427 ? -17.113 24.068  -0.347  1.00 53.49  ? 428 VAL D CG2 1 
ATOM   12410 N  N   . MET D 1 428 ? -19.372 20.130  -1.183  1.00 49.02  ? 429 MET D N   1 
ATOM   12411 C  CA  . MET D 1 428 ? -19.777 18.754  -0.939  1.00 47.67  ? 429 MET D CA  1 
ATOM   12412 C  C   . MET D 1 428 ? -18.658 17.969  -0.269  1.00 49.44  ? 429 MET D C   1 
ATOM   12413 O  O   . MET D 1 428 ? -17.567 18.491  -0.040  1.00 47.65  ? 429 MET D O   1 
ATOM   12414 C  CB  . MET D 1 428 ? -20.183 18.071  -2.247  1.00 49.51  ? 429 MET D CB  1 
ATOM   12415 C  CG  . MET D 1 428 ? -21.428 18.652  -2.900  1.00 50.70  ? 429 MET D CG  1 
ATOM   12416 S  SD  . MET D 1 428 ? -22.934 18.330  -1.962  1.00 62.61  ? 429 MET D SD  1 
ATOM   12417 C  CE  . MET D 1 428 ? -23.181 19.905  -1.146  1.00 47.33  ? 429 MET D CE  1 
ATOM   12418 N  N   . GLY D 1 429 ? -18.935 16.709  0.038   1.00 47.48  ? 430 GLY D N   1 
ATOM   12419 C  CA  . GLY D 1 429 ? -17.917 15.815  0.546   1.00 38.37  ? 430 GLY D CA  1 
ATOM   12420 C  C   . GLY D 1 429 ? -17.243 15.151  -0.633  1.00 43.36  ? 430 GLY D C   1 
ATOM   12421 O  O   . GLY D 1 429 ? -17.746 15.215  -1.755  1.00 37.59  ? 430 GLY D O   1 
ATOM   12422 N  N   . ASP D 1 430 ? -16.097 14.527  -0.393  1.00 37.45  ? 431 ASP D N   1 
ATOM   12423 C  CA  . ASP D 1 430 ? -15.393 13.821  -1.454  1.00 51.93  ? 431 ASP D CA  1 
ATOM   12424 C  C   . ASP D 1 430 ? -16.036 12.462  -1.708  1.00 37.33  ? 431 ASP D C   1 
ATOM   12425 O  O   . ASP D 1 430 ? -16.660 11.885  -0.819  1.00 40.02  ? 431 ASP D O   1 
ATOM   12426 C  CB  . ASP D 1 430 ? -13.914 13.659  -1.103  1.00 48.64  ? 431 ASP D CB  1 
ATOM   12427 C  CG  . ASP D 1 430 ? -13.243 14.981  -0.787  1.00 54.25  ? 431 ASP D CG  1 
ATOM   12428 O  OD1 . ASP D 1 430 ? -12.853 15.694  -1.736  1.00 56.85  ? 431 ASP D OD1 1 
ATOM   12429 O  OD2 . ASP D 1 430 ? -13.107 15.309  0.411   1.00 55.65  ? 431 ASP D OD2 1 
ATOM   12430 N  N   . GLY D 1 431 ? -15.889 11.958  -2.928  1.00 37.10  ? 432 GLY D N   1 
ATOM   12431 C  CA  . GLY D 1 431 ? -16.417 10.651  -3.269  1.00 42.23  ? 432 GLY D CA  1 
ATOM   12432 C  C   . GLY D 1 431 ? -17.693 10.721  -4.080  1.00 43.55  ? 432 GLY D C   1 
ATOM   12433 O  O   . GLY D 1 431 ? -18.408 11.721  -4.042  1.00 50.81  ? 432 GLY D O   1 
ATOM   12434 N  N   . LEU D 1 432 ? -17.979 9.646   -4.808  1.00 46.24  ? 433 LEU D N   1 
ATOM   12435 C  CA  . LEU D 1 432 ? -19.141 9.584   -5.688  1.00 45.42  ? 433 LEU D CA  1 
ATOM   12436 C  C   . LEU D 1 432 ? -20.454 9.767   -4.936  1.00 47.76  ? 433 LEU D C   1 
ATOM   12437 O  O   . LEU D 1 432 ? -21.279 10.599  -5.311  1.00 52.83  ? 433 LEU D O   1 
ATOM   12438 C  CB  . LEU D 1 432 ? -19.164 8.254   -6.442  1.00 39.45  ? 433 LEU D CB  1 
ATOM   12439 C  CG  . LEU D 1 432 ? -20.216 8.125   -7.544  1.00 40.12  ? 433 LEU D CG  1 
ATOM   12440 C  CD1 . LEU D 1 432 ? -19.894 9.065   -8.693  1.00 39.61  ? 433 LEU D CD1 1 
ATOM   12441 C  CD2 . LEU D 1 432 ? -20.313 6.689   -8.033  1.00 40.89  ? 433 LEU D CD2 1 
ATOM   12442 N  N   . ALA D 1 433 ? -20.634 8.988   -3.874  1.00 40.19  ? 434 ALA D N   1 
ATOM   12443 C  CA  . ALA D 1 433 ? -21.882 8.971   -3.117  1.00 46.22  ? 434 ALA D CA  1 
ATOM   12444 C  C   . ALA D 1 433 ? -22.261 10.347  -2.576  1.00 49.69  ? 434 ALA D C   1 
ATOM   12445 O  O   . ALA D 1 433 ? -23.442 10.689  -2.502  1.00 43.59  ? 434 ALA D O   1 
ATOM   12446 C  CB  . ALA D 1 433 ? -21.786 7.969   -1.977  1.00 41.73  ? 434 ALA D CB  1 
ATOM   12447 N  N   . ASN D 1 434 ? -21.258 11.137  -2.206  1.00 44.56  ? 435 ASN D N   1 
ATOM   12448 C  CA  . ASN D 1 434 ? -21.501 12.458  -1.639  1.00 44.34  ? 435 ASN D CA  1 
ATOM   12449 C  C   . ASN D 1 434 ? -21.933 13.497  -2.673  1.00 39.69  ? 435 ASN D C   1 
ATOM   12450 O  O   . ASN D 1 434 ? -22.249 14.633  -2.319  1.00 39.68  ? 435 ASN D O   1 
ATOM   12451 C  CB  . ASN D 1 434 ? -20.251 12.956  -0.911  1.00 44.89  ? 435 ASN D CB  1 
ATOM   12452 C  CG  . ASN D 1 434 ? -20.104 12.352  0.470   1.00 47.24  ? 435 ASN D CG  1 
ATOM   12453 O  OD1 . ASN D 1 434 ? -21.093 12.041  1.133   1.00 46.31  ? 435 ASN D OD1 1 
ATOM   12454 N  ND2 . ASN D 1 434 ? -18.863 12.186  0.913   1.00 48.62  ? 435 ASN D ND2 1 
ATOM   12455 N  N   . GLN D 1 435 ? -21.953 13.110  -3.945  1.00 39.53  ? 436 GLN D N   1 
ATOM   12456 C  CA  . GLN D 1 435 ? -22.289 14.044  -5.015  1.00 39.29  ? 436 GLN D CA  1 
ATOM   12457 C  C   . GLN D 1 435 ? -23.723 13.883  -5.505  1.00 52.88  ? 436 GLN D C   1 
ATOM   12458 O  O   . GLN D 1 435 ? -24.098 14.444  -6.535  1.00 52.31  ? 436 GLN D O   1 
ATOM   12459 C  CB  . GLN D 1 435 ? -21.328 13.873  -6.193  1.00 38.70  ? 436 GLN D CB  1 
ATOM   12460 C  CG  . GLN D 1 435 ? -19.860 13.932  -5.811  1.00 40.13  ? 436 GLN D CG  1 
ATOM   12461 C  CD  . GLN D 1 435 ? -19.506 15.173  -5.020  1.00 40.59  ? 436 GLN D CD  1 
ATOM   12462 O  OE1 . GLN D 1 435 ? -20.002 16.265  -5.296  1.00 44.48  ? 436 GLN D OE1 1 
ATOM   12463 N  NE2 . GLN D 1 435 ? -18.645 15.010  -4.022  1.00 37.48  ? 436 GLN D NE2 1 
ATOM   12464 N  N   . ILE D 1 436 ? -24.522 13.119  -4.768  1.00 40.95  ? 437 ILE D N   1 
ATOM   12465 C  CA  . ILE D 1 436 ? -25.909 12.880  -5.152  1.00 44.53  ? 437 ILE D CA  1 
ATOM   12466 C  C   . ILE D 1 436 ? -26.708 14.188  -5.128  1.00 42.94  ? 437 ILE D C   1 
ATOM   12467 O  O   . ILE D 1 436 ? -27.490 14.469  -6.041  1.00 46.70  ? 437 ILE D O   1 
ATOM   12468 C  CB  . ILE D 1 436 ? -26.568 11.815  -4.230  1.00 42.98  ? 437 ILE D CB  1 
ATOM   12469 C  CG1 . ILE D 1 436 ? -28.047 11.631  -4.572  1.00 44.52  ? 437 ILE D CG1 1 
ATOM   12470 C  CG2 . ILE D 1 436 ? -26.387 12.163  -2.754  1.00 43.04  ? 437 ILE D CG2 1 
ATOM   12471 C  CD1 . ILE D 1 436 ? -28.736 10.587  -3.721  1.00 46.06  ? 437 ILE D CD1 1 
ATOM   12472 N  N   . ASN D 1 437 ? -26.489 14.984  -4.086  1.00 44.69  ? 438 ASN D N   1 
ATOM   12473 C  CA  . ASN D 1 437 ? -27.156 16.270  -3.911  1.00 46.59  ? 438 ASN D CA  1 
ATOM   12474 C  C   . ASN D 1 437 ? -26.355 17.471  -4.416  1.00 47.48  ? 438 ASN D C   1 
ATOM   12475 O  O   . ASN D 1 437 ? -26.748 18.615  -4.182  1.00 48.59  ? 438 ASN D O   1 
ATOM   12476 C  CB  . ASN D 1 437 ? -27.527 16.473  -2.443  1.00 51.43  ? 438 ASN D CB  1 
ATOM   12477 C  CG  . ASN D 1 437 ? -28.803 15.748  -2.067  1.00 54.27  ? 438 ASN D CG  1 
ATOM   12478 O  OD1 . ASN D 1 437 ? -29.684 15.550  -2.905  1.00 56.13  ? 438 ASN D OD1 1 
ATOM   12479 N  ND2 . ASN D 1 437 ? -28.909 15.344  -0.807  1.00 56.36  ? 438 ASN D ND2 1 
ATOM   12480 N  N   . ASN D 1 438 ? -25.220 17.215  -5.065  1.00 46.43  ? 439 ASN D N   1 
ATOM   12481 C  CA  . ASN D 1 438 ? -24.377 18.287  -5.591  1.00 49.01  ? 439 ASN D CA  1 
ATOM   12482 C  C   . ASN D 1 438 ? -25.182 19.254  -6.458  1.00 48.64  ? 439 ASN D C   1 
ATOM   12483 O  O   . ASN D 1 438 ? -25.780 18.853  -7.456  1.00 51.26  ? 439 ASN D O   1 
ATOM   12484 C  CB  . ASN D 1 438 ? -23.219 17.695  -6.402  1.00 38.81  ? 439 ASN D CB  1 
ATOM   12485 C  CG  . ASN D 1 438 ? -22.203 18.741  -6.833  1.00 46.68  ? 439 ASN D CG  1 
ATOM   12486 O  OD1 . ASN D 1 438 ? -22.468 19.559  -7.715  1.00 40.66  ? 439 ASN D OD1 1 
ATOM   12487 N  ND2 . ASN D 1 438 ? -21.023 18.702  -6.225  1.00 42.28  ? 439 ASN D ND2 1 
ATOM   12488 N  N   . PRO D 1 439 ? -25.195 20.539  -6.071  1.00 48.88  ? 440 PRO D N   1 
ATOM   12489 C  CA  . PRO D 1 439 ? -26.018 21.564  -6.725  1.00 43.66  ? 440 PRO D CA  1 
ATOM   12490 C  C   . PRO D 1 439 ? -25.574 21.893  -8.148  1.00 45.81  ? 440 PRO D C   1 
ATOM   12491 O  O   . PRO D 1 439 ? -26.415 22.171  -9.003  1.00 47.47  ? 440 PRO D O   1 
ATOM   12492 C  CB  . PRO D 1 439 ? -25.848 22.782  -5.810  1.00 43.14  ? 440 PRO D CB  1 
ATOM   12493 C  CG  . PRO D 1 439 ? -24.534 22.572  -5.143  1.00 44.57  ? 440 PRO D CG  1 
ATOM   12494 C  CD  . PRO D 1 439 ? -24.410 21.089  -4.951  1.00 45.06  ? 440 PRO D CD  1 
ATOM   12495 N  N   . GLU D 1 440 ? -24.267 21.885  -8.385  1.00 41.79  ? 441 GLU D N   1 
ATOM   12496 C  CA  . GLU D 1 440 ? -23.723 22.242  -9.691  1.00 45.13  ? 441 GLU D CA  1 
ATOM   12497 C  C   . GLU D 1 440 ? -23.757 21.112  -10.717 1.00 43.86  ? 441 GLU D C   1 
ATOM   12498 O  O   . GLU D 1 440 ? -24.078 21.335  -11.884 1.00 52.54  ? 441 GLU D O   1 
ATOM   12499 C  CB  . GLU D 1 440 ? -22.291 22.752  -9.529  1.00 44.88  ? 441 GLU D CB  1 
ATOM   12500 C  CG  . GLU D 1 440 ? -22.172 23.882  -8.520  1.00 42.26  ? 441 GLU D CG  1 
ATOM   12501 C  CD  . GLU D 1 440 ? -23.235 24.952  -8.716  1.00 42.06  ? 441 GLU D CD  1 
ATOM   12502 O  OE1 . GLU D 1 440 ? -23.501 25.333  -9.877  1.00 42.29  ? 441 GLU D OE1 1 
ATOM   12503 O  OE2 . GLU D 1 440 ? -23.811 25.408  -7.706  1.00 38.58  ? 441 GLU D OE2 1 
ATOM   12504 N  N   . VAL D 1 441 ? -23.421 19.902  -10.284 1.00 45.27  ? 442 VAL D N   1 
ATOM   12505 C  CA  . VAL D 1 441 ? -23.289 18.781  -11.209 1.00 44.00  ? 442 VAL D CA  1 
ATOM   12506 C  C   . VAL D 1 441 ? -24.282 17.668  -10.901 1.00 44.51  ? 442 VAL D C   1 
ATOM   12507 O  O   . VAL D 1 441 ? -24.424 17.254  -9.749  1.00 43.84  ? 442 VAL D O   1 
ATOM   12508 C  CB  . VAL D 1 441 ? -21.866 18.187  -11.177 1.00 42.63  ? 442 VAL D CB  1 
ATOM   12509 C  CG1 . VAL D 1 441 ? -21.594 17.400  -12.449 1.00 44.76  ? 442 VAL D CG1 1 
ATOM   12510 C  CG2 . VAL D 1 441 ? -20.832 19.287  -11.000 1.00 41.07  ? 442 VAL D CG2 1 
ATOM   12511 N  N   . GLU D 1 442 ? -24.966 17.181  -11.931 1.00 44.25  ? 443 GLU D N   1 
ATOM   12512 C  CA  . GLU D 1 442 ? -25.848 16.038  -11.754 1.00 51.19  ? 443 GLU D CA  1 
ATOM   12513 C  C   . GLU D 1 442 ? -25.049 14.754  -11.896 1.00 52.39  ? 443 GLU D C   1 
ATOM   12514 O  O   . GLU D 1 442 ? -24.466 14.478  -12.945 1.00 50.81  ? 443 GLU D O   1 
ATOM   12515 C  CB  . GLU D 1 442 ? -27.005 16.062  -12.755 1.00 57.61  ? 443 GLU D CB  1 
ATOM   12516 C  CG  . GLU D 1 442 ? -28.110 17.055  -12.416 1.00 66.08  ? 443 GLU D CG  1 
ATOM   12517 C  CD  . GLU D 1 442 ? -28.658 16.901  -11.001 1.00 73.53  ? 443 GLU D CD  1 
ATOM   12518 O  OE1 . GLU D 1 442 ? -28.608 15.785  -10.433 1.00 75.48  ? 443 GLU D OE1 1 
ATOM   12519 O  OE2 . GLU D 1 442 ? -29.149 17.909  -10.453 1.00 78.32  ? 443 GLU D OE2 1 
ATOM   12520 N  N   . VAL D 1 443 ? -25.029 13.975  -10.823 1.00 50.89  ? 444 VAL D N   1 
ATOM   12521 C  CA  . VAL D 1 443 ? -24.234 12.760  -10.771 1.00 51.09  ? 444 VAL D CA  1 
ATOM   12522 C  C   . VAL D 1 443 ? -25.102 11.577  -10.371 1.00 52.88  ? 444 VAL D C   1 
ATOM   12523 O  O   . VAL D 1 443 ? -25.853 11.650  -9.397  1.00 56.07  ? 444 VAL D O   1 
ATOM   12524 C  CB  . VAL D 1 443 ? -23.063 12.896  -9.771  1.00 50.48  ? 444 VAL D CB  1 
ATOM   12525 C  CG1 . VAL D 1 443 ? -22.237 11.621  -9.737  1.00 48.66  ? 444 VAL D CG1 1 
ATOM   12526 C  CG2 . VAL D 1 443 ? -22.192 14.093  -10.124 1.00 49.25  ? 444 VAL D CG2 1 
ATOM   12527 N  N   . ASP D 1 444 ? -25.001 10.487  -11.121 1.00 55.52  ? 445 ASP D N   1 
ATOM   12528 C  CA  . ASP D 1 444 ? -25.679 9.260   -10.737 1.00 59.26  ? 445 ASP D CA  1 
ATOM   12529 C  C   . ASP D 1 444 ? -24.699 8.437   -9.916  1.00 52.40  ? 445 ASP D C   1 
ATOM   12530 O  O   . ASP D 1 444 ? -23.703 7.939   -10.436 1.00 45.76  ? 445 ASP D O   1 
ATOM   12531 C  CB  . ASP D 1 444 ? -26.159 8.486   -11.966 1.00 65.52  ? 445 ASP D CB  1 
ATOM   12532 C  CG  . ASP D 1 444 ? -26.943 7.239   -11.603 1.00 73.40  ? 445 ASP D CG  1 
ATOM   12533 O  OD1 . ASP D 1 444 ? -27.556 7.214   -10.515 1.00 75.34  ? 445 ASP D OD1 1 
ATOM   12534 O  OD2 . ASP D 1 444 ? -26.950 6.285   -12.410 1.00 76.32  ? 445 ASP D OD2 1 
ATOM   12535 N  N   . ILE D 1 445 ? -24.990 8.296   -8.628  1.00 53.54  ? 446 ILE D N   1 
ATOM   12536 C  CA  . ILE D 1 445 ? -24.054 7.670   -7.705  1.00 55.37  ? 446 ILE D CA  1 
ATOM   12537 C  C   . ILE D 1 445 ? -24.130 6.154   -7.797  1.00 47.94  ? 446 ILE D C   1 
ATOM   12538 O  O   . ILE D 1 445 ? -23.301 5.444   -7.228  1.00 52.24  ? 446 ILE D O   1 
ATOM   12539 C  CB  . ILE D 1 445 ? -24.317 8.111   -6.254  1.00 49.71  ? 446 ILE D CB  1 
ATOM   12540 C  CG1 . ILE D 1 445 ? -25.665 7.576   -5.768  1.00 48.03  ? 446 ILE D CG1 1 
ATOM   12541 C  CG2 . ILE D 1 445 ? -24.272 9.627   -6.145  1.00 42.04  ? 446 ILE D CG2 1 
ATOM   12542 C  CD1 . ILE D 1 445 ? -25.922 7.823   -4.296  1.00 44.41  ? 446 ILE D CD1 1 
ATOM   12543 N  N   . THR D 1 446 ? -25.131 5.666   -8.521  1.00 47.95  ? 447 THR D N   1 
ATOM   12544 C  CA  . THR D 1 446 ? -25.302 4.235   -8.727  1.00 51.21  ? 447 THR D CA  1 
ATOM   12545 C  C   . THR D 1 446 ? -24.630 3.789   -10.019 1.00 54.91  ? 447 THR D C   1 
ATOM   12546 O  O   . THR D 1 446 ? -24.717 2.623   -10.402 1.00 55.18  ? 447 THR D O   1 
ATOM   12547 C  CB  . THR D 1 446 ? -26.787 3.842   -8.767  1.00 49.07  ? 447 THR D CB  1 
ATOM   12548 O  OG1 . THR D 1 446 ? -27.452 4.581   -9.800  1.00 48.94  ? 447 THR D OG1 1 
ATOM   12549 C  CG2 . THR D 1 446 ? -27.447 4.140   -7.434  1.00 52.55  ? 447 THR D CG2 1 
ATOM   12550 N  N   . LYS D 1 447 ? -23.961 4.723   -10.689 1.00 50.58  ? 448 LYS D N   1 
ATOM   12551 C  CA  . LYS D 1 447 ? -23.267 4.415   -11.935 1.00 53.42  ? 448 LYS D CA  1 
ATOM   12552 C  C   . LYS D 1 447 ? -21.773 4.728   -11.852 1.00 49.68  ? 448 LYS D C   1 
ATOM   12553 O  O   . LYS D 1 447 ? -21.300 5.678   -12.476 1.00 54.41  ? 448 LYS D O   1 
ATOM   12554 C  CB  . LYS D 1 447 ? -23.895 5.188   -13.096 1.00 45.15  ? 448 LYS D CB  1 
ATOM   12555 N  N   . PRO D 1 448 ? -21.023 3.925   -11.080 1.00 47.51  ? 449 PRO D N   1 
ATOM   12556 C  CA  . PRO D 1 448 ? -19.580 4.150   -10.947 1.00 46.18  ? 449 PRO D CA  1 
ATOM   12557 C  C   . PRO D 1 448 ? -18.814 3.757   -12.204 1.00 46.41  ? 449 PRO D C   1 
ATOM   12558 O  O   . PRO D 1 448 ? -19.160 2.769   -12.850 1.00 48.33  ? 449 PRO D O   1 
ATOM   12559 C  CB  . PRO D 1 448 ? -19.197 3.248   -9.773  1.00 45.94  ? 449 PRO D CB  1 
ATOM   12560 C  CG  . PRO D 1 448 ? -20.176 2.129   -9.843  1.00 46.76  ? 449 PRO D CG  1 
ATOM   12561 C  CD  . PRO D 1 448 ? -21.465 2.739   -10.324 1.00 45.29  ? 449 PRO D CD  1 
ATOM   12562 N  N   . ASP D 1 449 ? -17.789 4.531   -12.545 1.00 46.95  ? 450 ASP D N   1 
ATOM   12563 C  CA  . ASP D 1 449 ? -16.909 4.185   -13.653 1.00 50.33  ? 450 ASP D CA  1 
ATOM   12564 C  C   . ASP D 1 449 ? -16.149 2.909   -13.303 1.00 50.35  ? 450 ASP D C   1 
ATOM   12565 O  O   . ASP D 1 449 ? -15.403 2.872   -12.324 1.00 50.01  ? 450 ASP D O   1 
ATOM   12566 C  CB  . ASP D 1 449 ? -15.945 5.334   -13.954 1.00 56.42  ? 450 ASP D CB  1 
ATOM   12567 C  CG  . ASP D 1 449 ? -14.924 4.976   -15.014 1.00 60.31  ? 450 ASP D CG  1 
ATOM   12568 O  OD1 . ASP D 1 449 ? -15.247 5.086   -16.216 1.00 62.07  ? 450 ASP D OD1 1 
ATOM   12569 O  OD2 . ASP D 1 449 ? -13.797 4.590   -14.644 1.00 62.26  ? 450 ASP D OD2 1 
ATOM   12570 N  N   . MET D 1 450 ? -16.347 1.864   -14.100 1.00 50.04  ? 451 MET D N   1 
ATOM   12571 C  CA  . MET D 1 450 ? -15.841 0.538   -13.756 1.00 53.91  ? 451 MET D CA  1 
ATOM   12572 C  C   . MET D 1 450 ? -14.327 0.401   -13.900 1.00 50.65  ? 451 MET D C   1 
ATOM   12573 O  O   . MET D 1 450 ? -13.723 -0.485  -13.292 1.00 49.50  ? 451 MET D O   1 
ATOM   12574 C  CB  . MET D 1 450 ? -16.542 -0.526  -14.602 1.00 55.55  ? 451 MET D CB  1 
ATOM   12575 C  CG  . MET D 1 450 ? -17.743 -1.143  -13.903 1.00 58.28  ? 451 MET D CG  1 
ATOM   12576 S  SD  . MET D 1 450 ? -17.247 -2.022  -12.407 1.00 122.19 ? 451 MET D SD  1 
ATOM   12577 C  CE  . MET D 1 450 ? -18.728 -1.881  -11.410 1.00 67.98  ? 451 MET D CE  1 
ATOM   12578 N  N   . THR D 1 451 ? -13.717 1.269   -14.701 1.00 51.37  ? 452 THR D N   1 
ATOM   12579 C  CA  . THR D 1 451 ? -12.262 1.308   -14.806 1.00 51.75  ? 452 THR D CA  1 
ATOM   12580 C  C   . THR D 1 451 ? -11.656 1.580   -13.433 1.00 53.25  ? 452 THR D C   1 
ATOM   12581 O  O   . THR D 1 451 ? -10.762 0.862   -12.969 1.00 51.53  ? 452 THR D O   1 
ATOM   12582 C  CB  . THR D 1 451 ? -11.789 2.387   -15.799 1.00 54.72  ? 452 THR D CB  1 
ATOM   12583 O  OG1 . THR D 1 451 ? -12.278 2.083   -17.111 1.00 56.94  ? 452 THR D OG1 1 
ATOM   12584 C  CG2 . THR D 1 451 ? -10.270 2.457   -15.831 1.00 56.03  ? 452 THR D CG2 1 
ATOM   12585 N  N   . ILE D 1 452 ? -12.173 2.616   -12.781 1.00 46.47  ? 453 ILE D N   1 
ATOM   12586 C  CA  . ILE D 1 452 ? -11.706 3.013   -11.462 1.00 48.48  ? 453 ILE D CA  1 
ATOM   12587 C  C   . ILE D 1 452 ? -11.994 1.922   -10.432 1.00 46.30  ? 453 ILE D C   1 
ATOM   12588 O  O   . ILE D 1 452 ? -11.194 1.697   -9.525  1.00 42.39  ? 453 ILE D O   1 
ATOM   12589 C  CB  . ILE D 1 452 ? -12.346 4.350   -11.034 1.00 38.74  ? 453 ILE D CB  1 
ATOM   12590 C  CG1 . ILE D 1 452 ? -11.867 5.461   -11.974 1.00 45.07  ? 453 ILE D CG1 1 
ATOM   12591 C  CG2 . ILE D 1 452 ? -12.014 4.683   -9.586  1.00 38.09  ? 453 ILE D CG2 1 
ATOM   12592 C  CD1 . ILE D 1 452 ? -12.006 6.854   -11.422 1.00 46.25  ? 453 ILE D CD1 1 
ATOM   12593 N  N   . ARG D 1 453 ? -13.119 1.231   -10.587 1.00 40.50  ? 454 ARG D N   1 
ATOM   12594 C  CA  . ARG D 1 453 ? -13.436 0.093   -9.727  1.00 41.08  ? 454 ARG D CA  1 
ATOM   12595 C  C   . ARG D 1 453 ? -12.358 -0.986  -9.848  1.00 57.47  ? 454 ARG D C   1 
ATOM   12596 O  O   . ARG D 1 453 ? -11.835 -1.486  -8.841  1.00 64.68  ? 454 ARG D O   1 
ATOM   12597 C  CB  . ARG D 1 453 ? -14.808 -0.485  -10.080 1.00 42.25  ? 454 ARG D CB  1 
ATOM   12598 N  N   . GLN D 1 454 ? -12.025 -1.329  -11.089 1.00 52.92  ? 455 GLN D N   1 
ATOM   12599 C  CA  . GLN D 1 454 ? -10.990 -2.317  -11.367 1.00 59.44  ? 455 GLN D CA  1 
ATOM   12600 C  C   . GLN D 1 454 ? -9.647  -1.904  -10.770 1.00 52.43  ? 455 GLN D C   1 
ATOM   12601 O  O   . GLN D 1 454 ? -8.943  -2.724  -10.172 1.00 55.26  ? 455 GLN D O   1 
ATOM   12602 C  CB  . GLN D 1 454 ? -10.848 -2.533  -12.875 1.00 64.97  ? 455 GLN D CB  1 
ATOM   12603 C  CG  . GLN D 1 454 ? -11.981 -3.333  -13.497 1.00 73.53  ? 455 GLN D CG  1 
ATOM   12604 C  CD  . GLN D 1 454 ? -11.873 -3.423  -15.007 1.00 80.54  ? 455 GLN D CD  1 
ATOM   12605 O  OE1 . GLN D 1 454 ? -10.995 -2.812  -15.616 1.00 83.44  ? 455 GLN D OE1 1 
ATOM   12606 N  NE2 . GLN D 1 454 ? -12.765 -4.194  -15.619 1.00 83.57  ? 455 GLN D NE2 1 
ATOM   12607 N  N   . GLN D 1 455 ? -9.299  -0.630  -10.925 1.00 47.07  ? 456 GLN D N   1 
ATOM   12608 C  CA  . GLN D 1 455 ? -8.039  -0.130  -10.384 1.00 47.26  ? 456 GLN D CA  1 
ATOM   12609 C  C   . GLN D 1 455 ? -8.030  -0.188  -8.856  1.00 42.34  ? 456 GLN D C   1 
ATOM   12610 O  O   . GLN D 1 455 ? -6.993  -0.450  -8.243  1.00 46.92  ? 456 GLN D O   1 
ATOM   12611 C  CB  . GLN D 1 455 ? -7.775  1.296   -10.869 1.00 44.42  ? 456 GLN D CB  1 
ATOM   12612 C  CG  . GLN D 1 455 ? -7.655  1.407   -12.381 1.00 46.16  ? 456 GLN D CG  1 
ATOM   12613 C  CD  . GLN D 1 455 ? -6.788  0.312   -12.979 1.00 47.64  ? 456 GLN D CD  1 
ATOM   12614 O  OE1 . GLN D 1 455 ? -5.607  0.193   -12.656 1.00 48.20  ? 456 GLN D OE1 1 
ATOM   12615 N  NE2 . GLN D 1 455 ? -7.375  -0.497  -13.852 1.00 50.05  ? 456 GLN D NE2 1 
ATOM   12616 N  N   . ILE D 1 456 ? -9.189  0.048   -8.249  1.00 38.97  ? 457 ILE D N   1 
ATOM   12617 C  CA  . ILE D 1 456 ? -9.346  -0.094  -6.805  1.00 40.37  ? 457 ILE D CA  1 
ATOM   12618 C  C   . ILE D 1 456 ? -9.083  -1.539  -6.396  1.00 39.45  ? 457 ILE D C   1 
ATOM   12619 O  O   . ILE D 1 456 ? -8.376  -1.803  -5.414  1.00 41.22  ? 457 ILE D O   1 
ATOM   12620 C  CB  . ILE D 1 456 ? -10.755 0.334   -6.338  1.00 39.11  ? 457 ILE D CB  1 
ATOM   12621 C  CG1 . ILE D 1 456 ? -10.904 1.855   -6.422  1.00 46.26  ? 457 ILE D CG1 1 
ATOM   12622 C  CG2 . ILE D 1 456 ? -11.021 -0.134  -4.916  1.00 39.36  ? 457 ILE D CG2 1 
ATOM   12623 C  CD1 . ILE D 1 456 ? -12.328 2.343   -6.254  1.00 44.18  ? 457 ILE D CD1 1 
ATOM   12624 N  N   . MET D 1 457 ? -9.645  -2.471  -7.163  1.00 40.34  ? 458 MET D N   1 
ATOM   12625 C  CA  . MET D 1 457 ? -9.396  -3.892  -6.932  1.00 45.64  ? 458 MET D CA  1 
ATOM   12626 C  C   . MET D 1 457 ? -7.897  -4.192  -6.985  1.00 43.70  ? 458 MET D C   1 
ATOM   12627 O  O   . MET D 1 457 ? -7.359  -4.877  -6.108  1.00 41.13  ? 458 MET D O   1 
ATOM   12628 C  CB  . MET D 1 457 ? -10.145 -4.745  -7.957  1.00 47.23  ? 458 MET D CB  1 
ATOM   12629 C  CG  . MET D 1 457 ? -10.059 -6.243  -7.706  1.00 46.61  ? 458 MET D CG  1 
ATOM   12630 S  SD  . MET D 1 457 ? -10.753 -6.715  -6.111  1.00 66.41  ? 458 MET D SD  1 
ATOM   12631 C  CE  . MET D 1 457 ? -12.450 -7.061  -6.571  1.00 62.24  ? 458 MET D CE  1 
ATOM   12632 N  N   . GLN D 1 458 ? -7.229  -3.664  -8.008  1.00 46.10  ? 459 GLN D N   1 
ATOM   12633 C  CA  . GLN D 1 458 ? -5.781  -3.816  -8.147  1.00 46.96  ? 459 GLN D CA  1 
ATOM   12634 C  C   . GLN D 1 458 ? -5.038  -3.302  -6.916  1.00 44.40  ? 459 GLN D C   1 
ATOM   12635 O  O   . GLN D 1 458 ? -4.115  -3.956  -6.410  1.00 44.83  ? 459 GLN D O   1 
ATOM   12636 C  CB  . GLN D 1 458 ? -5.286  -3.088  -9.398  1.00 44.39  ? 459 GLN D CB  1 
ATOM   12637 C  CG  . GLN D 1 458 ? -5.703  -3.751  -10.695 1.00 50.79  ? 459 GLN D CG  1 
ATOM   12638 C  CD  . GLN D 1 458 ? -5.218  -5.183  -10.790 1.00 59.41  ? 459 GLN D CD  1 
ATOM   12639 O  OE1 . GLN D 1 458 ? -4.015  -5.443  -10.805 1.00 67.25  ? 459 GLN D OE1 1 
ATOM   12640 N  NE2 . GLN D 1 458 ? -6.154  -6.123  -10.844 1.00 59.90  ? 459 GLN D NE2 1 
ATOM   12641 N  N   . LEU D 1 459 ? -5.452  -2.131  -6.438  1.00 45.38  ? 460 LEU D N   1 
ATOM   12642 C  CA  . LEU D 1 459 ? -4.880  -1.549  -5.230  1.00 46.60  ? 460 LEU D CA  1 
ATOM   12643 C  C   . LEU D 1 459 ? -5.025  -2.496  -4.045  1.00 46.81  ? 460 LEU D C   1 
ATOM   12644 O  O   . LEU D 1 459 ? -4.062  -2.736  -3.315  1.00 49.42  ? 460 LEU D O   1 
ATOM   12645 C  CB  . LEU D 1 459 ? -5.542  -0.207  -4.908  1.00 45.98  ? 460 LEU D CB  1 
ATOM   12646 C  CG  . LEU D 1 459 ? -5.301  0.938   -5.891  1.00 48.14  ? 460 LEU D CG  1 
ATOM   12647 C  CD1 . LEU D 1 459 ? -6.014  2.201   -5.428  1.00 49.56  ? 460 LEU D CD1 1 
ATOM   12648 C  CD2 . LEU D 1 459 ? -3.814  1.190   -6.065  1.00 46.00  ? 460 LEU D CD2 1 
ATOM   12649 N  N   . LYS D 1 460 ? -6.229  -3.034  -3.861  1.00 49.61  ? 461 LYS D N   1 
ATOM   12650 C  CA  . LYS D 1 460 ? -6.486  -3.963  -2.762  1.00 49.56  ? 461 LYS D CA  1 
ATOM   12651 C  C   . LYS D 1 460 ? -5.598  -5.203  -2.844  1.00 47.33  ? 461 LYS D C   1 
ATOM   12652 O  O   . LYS D 1 460 ? -4.999  -5.619  -1.847  1.00 43.25  ? 461 LYS D O   1 
ATOM   12653 C  CB  . LYS D 1 460 ? -7.957  -4.384  -2.745  1.00 55.23  ? 461 LYS D CB  1 
ATOM   12654 C  CG  . LYS D 1 460 ? -8.920  -3.268  -2.394  1.00 60.79  ? 461 LYS D CG  1 
ATOM   12655 C  CD  . LYS D 1 460 ? -10.331 -3.798  -2.203  1.00 69.63  ? 461 LYS D CD  1 
ATOM   12656 C  CE  . LYS D 1 460 ? -11.125 -2.919  -1.251  1.00 73.98  ? 461 LYS D CE  1 
ATOM   12657 N  NZ  . LYS D 1 460 ? -12.462 -3.498  -0.945  1.00 78.30  ? 461 LYS D NZ  1 
ATOM   12658 N  N   . ILE D 1 461 ? -5.519  -5.788  -4.036  1.00 47.15  ? 462 ILE D N   1 
ATOM   12659 C  CA  . ILE D 1 461 ? -4.690  -6.968  -4.259  1.00 40.76  ? 462 ILE D CA  1 
ATOM   12660 C  C   . ILE D 1 461 ? -3.224  -6.701  -3.914  1.00 48.61  ? 462 ILE D C   1 
ATOM   12661 O  O   . ILE D 1 461 ? -2.612  -7.432  -3.120  1.00 46.99  ? 462 ILE D O   1 
ATOM   12662 C  CB  . ILE D 1 461 ? -4.785  -7.448  -5.719  1.00 44.29  ? 462 ILE D CB  1 
ATOM   12663 C  CG1 . ILE D 1 461 ? -6.229  -7.818  -6.064  1.00 50.05  ? 462 ILE D CG1 1 
ATOM   12664 C  CG2 . ILE D 1 461 ? -3.859  -8.633  -5.953  1.00 43.44  ? 462 ILE D CG2 1 
ATOM   12665 C  CD1 . ILE D 1 461 ? -6.471  -8.018  -7.544  1.00 53.53  ? 462 ILE D CD1 1 
ATOM   12666 N  N   . MET D 1 462 ? -2.669  -5.645  -4.506  1.00 42.75  ? 463 MET D N   1 
ATOM   12667 C  CA  . MET D 1 462 ? -1.271  -5.301  -4.271  1.00 40.36  ? 463 MET D CA  1 
ATOM   12668 C  C   . MET D 1 462 ? -1.008  -5.034  -2.790  1.00 42.45  ? 463 MET D C   1 
ATOM   12669 O  O   . MET D 1 462 ? 0.021   -5.448  -2.246  1.00 38.47  ? 463 MET D O   1 
ATOM   12670 C  CB  . MET D 1 462 ? -0.865  -4.084  -5.103  1.00 42.29  ? 463 MET D CB  1 
ATOM   12671 C  CG  . MET D 1 462 ? 0.619   -3.778  -5.034  1.00 37.88  ? 463 MET D CG  1 
ATOM   12672 S  SD  . MET D 1 462 ? 1.608   -5.146  -5.664  1.00 49.35  ? 463 MET D SD  1 
ATOM   12673 C  CE  . MET D 1 462 ? 2.869   -5.266  -4.400  1.00 38.83  ? 463 MET D CE  1 
ATOM   12674 N  N   . THR D 1 463 ? -1.947  -4.349  -2.142  1.00 41.56  ? 464 THR D N   1 
ATOM   12675 C  CA  . THR D 1 463 ? -1.831  -4.056  -0.718  1.00 42.93  ? 464 THR D CA  1 
ATOM   12676 C  C   . THR D 1 463 ? -1.811  -5.350  0.092   1.00 46.11  ? 464 THR D C   1 
ATOM   12677 O  O   . THR D 1 463 ? -1.078  -5.463  1.076   1.00 42.94  ? 464 THR D O   1 
ATOM   12678 C  CB  . THR D 1 463 ? -2.981  -3.156  -0.226  1.00 44.22  ? 464 THR D CB  1 
ATOM   12679 O  OG1 . THR D 1 463 ? -3.009  -1.950  -0.999  1.00 44.81  ? 464 THR D OG1 1 
ATOM   12680 C  CG2 . THR D 1 463 ? -2.795  -2.800  1.242   1.00 38.19  ? 464 THR D CG2 1 
ATOM   12681 N  N   . ASN D 1 464 ? -2.611  -6.326  -0.328  1.00 44.85  ? 465 ASN D N   1 
ATOM   12682 C  CA  . ASN D 1 464 ? -2.586  -7.636  0.313   1.00 50.12  ? 465 ASN D CA  1 
ATOM   12683 C  C   . ASN D 1 464 ? -1.225  -8.306  0.147   1.00 47.45  ? 465 ASN D C   1 
ATOM   12684 O  O   . ASN D 1 464 ? -0.680  -8.872  1.103   1.00 40.63  ? 465 ASN D O   1 
ATOM   12685 C  CB  . ASN D 1 464 ? -3.688  -8.538  -0.245  1.00 58.91  ? 465 ASN D CB  1 
ATOM   12686 C  CG  . ASN D 1 464 ? -5.072  -8.113  0.203   1.00 69.25  ? 465 ASN D CG  1 
ATOM   12687 O  OD1 . ASN D 1 464 ? -5.227  -7.443  1.225   1.00 70.98  ? 465 ASN D OD1 1 
ATOM   12688 N  ND2 . ASN D 1 464 ? -6.088  -8.507  -0.556  1.00 69.91  ? 465 ASN D ND2 1 
ATOM   12689 N  N   . ARG D 1 465 ? -0.677  -8.231  -1.065  1.00 43.05  ? 466 ARG D N   1 
ATOM   12690 C  CA  . ARG D 1 465 ? 0.647   -8.793  -1.328  1.00 43.13  ? 466 ARG D CA  1 
ATOM   12691 C  C   . ARG D 1 465 ? 1.710   -8.174  -0.421  1.00 48.61  ? 466 ARG D C   1 
ATOM   12692 O  O   . ARG D 1 465 ? 2.525   -8.885  0.170   1.00 50.47  ? 466 ARG D O   1 
ATOM   12693 C  CB  . ARG D 1 465 ? 1.038   -8.598  -2.793  1.00 46.60  ? 466 ARG D CB  1 
ATOM   12694 C  CG  . ARG D 1 465 ? 0.113   -9.286  -3.779  1.00 56.65  ? 466 ARG D CG  1 
ATOM   12695 C  CD  . ARG D 1 465 ? 0.823   -9.579  -5.090  1.00 61.05  ? 466 ARG D CD  1 
ATOM   12696 N  NE  . ARG D 1 465 ? -0.110  -9.991  -6.135  1.00 69.41  ? 466 ARG D NE  1 
ATOM   12697 C  CZ  . ARG D 1 465 ? -0.610  -11.218 -6.251  1.00 74.61  ? 466 ARG D CZ  1 
ATOM   12698 N  NH1 . ARG D 1 465 ? -0.270  -12.162 -5.384  1.00 77.06  ? 466 ARG D NH1 1 
ATOM   12699 N  NH2 . ARG D 1 465 ? -1.454  -11.500 -7.235  1.00 76.23  ? 466 ARG D NH2 1 
ATOM   12700 N  N   . LEU D 1 466 ? 1.691   -6.849  -0.310  1.00 53.20  ? 467 LEU D N   1 
ATOM   12701 C  CA  . LEU D 1 466 ? 2.652   -6.139  0.531   1.00 54.90  ? 467 LEU D CA  1 
ATOM   12702 C  C   . LEU D 1 466 ? 2.486   -6.469  2.011   1.00 52.99  ? 467 LEU D C   1 
ATOM   12703 O  O   . LEU D 1 466 ? 3.470   -6.675  2.726   1.00 56.80  ? 467 LEU D O   1 
ATOM   12704 C  CB  . LEU D 1 466 ? 2.526   -4.631  0.322   1.00 37.83  ? 467 LEU D CB  1 
ATOM   12705 C  CG  . LEU D 1 466 ? 3.156   -4.083  -0.956  1.00 38.13  ? 467 LEU D CG  1 
ATOM   12706 C  CD1 . LEU D 1 466 ? 2.527   -2.757  -1.328  1.00 37.08  ? 467 LEU D CD1 1 
ATOM   12707 C  CD2 . LEU D 1 466 ? 4.653   -3.923  -0.768  1.00 42.76  ? 467 LEU D CD2 1 
ATOM   12708 N  N   . ARG D 1 467 ? 1.238   -6.519  2.467   1.00 55.28  ? 468 ARG D N   1 
ATOM   12709 C  CA  . ARG D 1 467 ? 0.957   -6.783  3.873   1.00 58.80  ? 468 ARG D CA  1 
ATOM   12710 C  C   . ARG D 1 467 ? 1.338   -8.211  4.249   1.00 60.20  ? 468 ARG D C   1 
ATOM   12711 O  O   . ARG D 1 467 ? 1.731   -8.474  5.386   1.00 57.04  ? 468 ARG D O   1 
ATOM   12712 C  CB  . ARG D 1 467 ? -0.517  -6.515  4.186   1.00 63.13  ? 468 ARG D CB  1 
ATOM   12713 C  CG  . ARG D 1 467 ? -0.816  -5.048  4.460   1.00 69.99  ? 468 ARG D CG  1 
ATOM   12714 C  CD  . ARG D 1 467 ? -2.272  -4.816  4.829   1.00 75.32  ? 468 ARG D CD  1 
ATOM   12715 N  NE  . ARG D 1 467 ? -2.428  -4.502  6.247   1.00 81.48  ? 468 ARG D NE  1 
ATOM   12716 C  CZ  . ARG D 1 467 ? -3.437  -3.799  6.752   1.00 85.84  ? 468 ARG D CZ  1 
ATOM   12717 N  NH1 . ARG D 1 467 ? -4.382  -3.322  5.953   1.00 85.55  ? 468 ARG D NH1 1 
ATOM   12718 N  NH2 . ARG D 1 467 ? -3.496  -3.564  8.056   1.00 87.61  ? 468 ARG D NH2 1 
ATOM   12719 N  N   . SER D 1 468 ? 1.229   -9.132  3.296   1.00 61.34  ? 469 SER D N   1 
ATOM   12720 C  CA  . SER D 1 468 ? 1.723   -10.486 3.516   1.00 62.23  ? 469 SER D CA  1 
ATOM   12721 C  C   . SER D 1 468 ? 3.249   -10.501 3.481   1.00 60.75  ? 469 SER D C   1 
ATOM   12722 O  O   . SER D 1 468 ? 3.888   -11.285 4.183   1.00 64.27  ? 469 SER D O   1 
ATOM   12723 C  CB  . SER D 1 468 ? 1.158   -11.453 2.476   1.00 64.87  ? 469 SER D CB  1 
ATOM   12724 O  OG  . SER D 1 468 ? -0.133  -11.905 2.848   1.00 69.44  ? 469 SER D OG  1 
ATOM   12725 N  N   . ALA D 1 469 ? 3.825   -9.624  2.664   1.00 56.35  ? 470 ALA D N   1 
ATOM   12726 C  CA  . ALA D 1 469 ? 5.275   -9.537  2.529   1.00 52.37  ? 470 ALA D CA  1 
ATOM   12727 C  C   . ALA D 1 469 ? 5.933   -8.970  3.784   1.00 52.28  ? 470 ALA D C   1 
ATOM   12728 O  O   . ALA D 1 469 ? 7.100   -9.251  4.058   1.00 52.74  ? 470 ALA D O   1 
ATOM   12729 C  CB  . ALA D 1 469 ? 5.642   -8.695  1.320   1.00 50.37  ? 470 ALA D CB  1 
ATOM   12730 N  N   . TYR D 1 470 ? 5.187   -8.169  4.539   1.00 48.61  ? 471 TYR D N   1 
ATOM   12731 C  CA  . TYR D 1 470 ? 5.717   -7.570  5.761   1.00 52.12  ? 471 TYR D CA  1 
ATOM   12732 C  C   . TYR D 1 470 ? 6.035   -8.633  6.806   1.00 57.54  ? 471 TYR D C   1 
ATOM   12733 O  O   . TYR D 1 470 ? 7.036   -8.539  7.516   1.00 57.70  ? 471 TYR D O   1 
ATOM   12734 C  CB  . TYR D 1 470 ? 4.731   -6.549  6.333   1.00 51.29  ? 471 TYR D CB  1 
ATOM   12735 C  CG  . TYR D 1 470 ? 5.319   -5.671  7.417   1.00 48.83  ? 471 TYR D CG  1 
ATOM   12736 C  CD1 . TYR D 1 470 ? 6.165   -4.616  7.100   1.00 48.93  ? 471 TYR D CD1 1 
ATOM   12737 C  CD2 . TYR D 1 470 ? 5.024   -5.893  8.756   1.00 50.09  ? 471 TYR D CD2 1 
ATOM   12738 C  CE1 . TYR D 1 470 ? 6.704   -3.810  8.085   1.00 50.52  ? 471 TYR D CE1 1 
ATOM   12739 C  CE2 . TYR D 1 470 ? 5.560   -5.091  9.750   1.00 49.19  ? 471 TYR D CE2 1 
ATOM   12740 C  CZ  . TYR D 1 470 ? 6.399   -4.051  9.407   1.00 53.44  ? 471 TYR D CZ  1 
ATOM   12741 O  OH  . TYR D 1 470 ? 6.935   -3.248  10.389  1.00 53.77  ? 471 TYR D OH  1 
ATOM   12742 N  N   . ASN D 1 471 ? 5.181   -9.647  6.890   1.00 67.82  ? 472 ASN D N   1 
ATOM   12743 C  CA  . ASN D 1 471 ? 5.365   -10.729 7.849   1.00 75.79  ? 472 ASN D CA  1 
ATOM   12744 C  C   . ASN D 1 471 ? 6.412   -11.733 7.378   1.00 86.14  ? 472 ASN D C   1 
ATOM   12745 O  O   . ASN D 1 471 ? 6.883   -12.564 8.155   1.00 87.46  ? 472 ASN D O   1 
ATOM   12746 C  CB  . ASN D 1 471 ? 4.037   -11.442 8.104   1.00 75.39  ? 472 ASN D CB  1 
ATOM   12747 C  CG  . ASN D 1 471 ? 2.918   -10.482 8.457   1.00 70.42  ? 472 ASN D CG  1 
ATOM   12748 O  OD1 . ASN D 1 471 ? 3.131   -9.492  9.156   1.00 74.07  ? 472 ASN D OD1 1 
ATOM   12749 N  ND2 . ASN D 1 471 ? 1.717   -10.770 7.969   1.00 66.96  ? 472 ASN D ND2 1 
ATOM   12750 N  N   . GLY D 1 472 ? 6.769   -11.652 6.100   1.00 98.03  ? 473 GLY D N   1 
ATOM   12751 C  CA  . GLY D 1 472 ? 7.741   -12.560 5.520   1.00 103.06 ? 473 GLY D CA  1 
ATOM   12752 C  C   . GLY D 1 472 ? 7.097   -13.840 5.026   1.00 102.33 ? 473 GLY D C   1 
ATOM   12753 O  O   . GLY D 1 472 ? 7.419   -14.931 5.497   1.00 105.79 ? 473 GLY D O   1 
ATOM   12754 N  N   . ASN D 1 473 ? 6.180   -13.705 4.073   1.00 93.91  ? 474 ASN D N   1 
ATOM   12755 C  CA  . ASN D 1 473 ? 5.475   -14.855 3.522   1.00 90.04  ? 474 ASN D CA  1 
ATOM   12756 C  C   . ASN D 1 473 ? 5.485   -14.851 1.998   1.00 85.13  ? 474 ASN D C   1 
ATOM   12757 O  O   . ASN D 1 473 ? 5.211   -13.828 1.369   1.00 79.73  ? 474 ASN D O   1 
ATOM   12758 C  CB  . ASN D 1 473 ? 4.033   -14.890 4.033   1.00 88.81  ? 474 ASN D CB  1 
ATOM   12759 C  CG  . ASN D 1 473 ? 3.935   -14.614 5.520   1.00 87.81  ? 474 ASN D CG  1 
ATOM   12760 O  OD1 . ASN D 1 473 ? 3.235   -13.696 5.947   1.00 85.86  ? 474 ASN D OD1 1 
ATOM   12761 N  ND2 . ASN D 1 473 ? 4.643   -15.407 6.317   1.00 87.47  ? 474 ASN D ND2 1 
HETATM 12762 C  C1  . NAG E 2 .   ? 58.773  28.095  99.749  1.00 56.86  ? 601 NAG A C1  1 
HETATM 12763 C  C2  . NAG E 2 .   ? 58.396  26.761  100.416 1.00 65.63  ? 601 NAG A C2  1 
HETATM 12764 C  C3  . NAG E 2 .   ? 57.487  26.997  101.625 1.00 74.14  ? 601 NAG A C3  1 
HETATM 12765 C  C4  . NAG E 2 .   ? 58.095  28.023  102.569 1.00 77.45  ? 601 NAG A C4  1 
HETATM 12766 C  C5  . NAG E 2 .   ? 58.394  29.302  101.800 1.00 70.72  ? 601 NAG A C5  1 
HETATM 12767 C  C6  . NAG E 2 .   ? 59.055  30.364  102.648 1.00 71.89  ? 601 NAG A C6  1 
HETATM 12768 C  C7  . NAG E 2 .   ? 58.325  24.766  98.980  1.00 62.62  ? 601 NAG A C7  1 
HETATM 12769 C  C8  . NAG E 2 .   ? 59.715  24.477  99.463  1.00 68.20  ? 601 NAG A C8  1 
HETATM 12770 N  N2  . NAG E 2 .   ? 57.750  25.871  99.467  1.00 63.15  ? 601 NAG A N2  1 
HETATM 12771 O  O3  . NAG E 2 .   ? 57.293  25.765  102.311 1.00 78.76  ? 601 NAG A O3  1 
HETATM 12772 O  O4  . NAG E 2 .   ? 57.193  28.307  103.632 1.00 81.59  ? 601 NAG A O4  1 
HETATM 12773 O  O5  . NAG E 2 .   ? 59.301  29.001  100.731 1.00 63.14  ? 601 NAG A O5  1 
HETATM 12774 O  O6  . NAG E 2 .   ? 59.994  29.798  103.552 1.00 72.44  ? 601 NAG A O6  1 
HETATM 12775 O  O7  . NAG E 2 .   ? 57.749  24.034  98.181  1.00 66.60  ? 601 NAG A O7  1 
HETATM 12776 CA CA  . CA  F 3 .   ? 35.946  8.539   81.591  1.00 47.23  ? 602 CA  A CA  1 
HETATM 12777 CA CA  . CA  G 3 .   ? 7.645   7.812   87.604  1.00 90.30  ? 603 CA  A CA  1 
HETATM 12778 C  C1  . NAG H 2 .   ? 45.850  4.238   54.796  1.00 69.06  ? 601 NAG B C1  1 
HETATM 12779 C  C2  . NAG H 2 .   ? 45.434  5.448   53.955  1.00 69.48  ? 601 NAG B C2  1 
HETATM 12780 C  C3  . NAG H 2 .   ? 44.586  4.998   52.765  1.00 73.81  ? 601 NAG B C3  1 
HETATM 12781 C  C4  . NAG H 2 .   ? 45.301  3.912   51.975  1.00 71.36  ? 601 NAG B C4  1 
HETATM 12782 C  C5  . NAG H 2 .   ? 45.681  2.765   52.905  1.00 75.85  ? 601 NAG B C5  1 
HETATM 12783 C  C6  . NAG H 2 .   ? 46.466  1.674   52.214  1.00 80.94  ? 601 NAG B C6  1 
HETATM 12784 C  C7  . NAG H 2 .   ? 45.064  7.709   54.840  1.00 74.48  ? 601 NAG B C7  1 
HETATM 12785 C  C8  . NAG H 2 .   ? 46.272  8.118   54.050  1.00 76.05  ? 601 NAG B C8  1 
HETATM 12786 N  N2  . NAG H 2 .   ? 44.715  6.419   54.754  1.00 71.26  ? 601 NAG B N2  1 
HETATM 12787 O  O3  . NAG H 2 .   ? 44.323  6.119   51.926  1.00 72.54  ? 601 NAG B O3  1 
HETATM 12788 O  O4  . NAG H 2 .   ? 44.458  3.424   50.938  1.00 65.79  ? 601 NAG B O4  1 
HETATM 12789 O  O5  . NAG H 2 .   ? 46.506  3.263   53.969  1.00 71.84  ? 601 NAG B O5  1 
HETATM 12790 O  O6  . NAG H 2 .   ? 47.866  1.857   52.372  1.00 84.65  ? 601 NAG B O6  1 
HETATM 12791 O  O7  . NAG H 2 .   ? 44.433  8.507   55.524  1.00 74.86  ? 601 NAG B O7  1 
HETATM 12792 CA CA  . CA  I 3 .   ? -5.662  27.208  60.441  1.00 87.84  ? 602 CA  B CA  1 
HETATM 12793 CA CA  . CA  J 3 .   ? 22.545  28.304  67.491  0.46 43.07  ? 603 CA  B CA  1 
HETATM 12794 C  C1  . NAG K 2 .   ? 36.369  16.127  31.290  1.00 79.84  ? 601 NAG C C1  1 
HETATM 12795 C  C2  . NAG K 2 .   ? 35.814  14.880  31.992  1.00 82.81  ? 601 NAG C C2  1 
HETATM 12796 C  C3  . NAG K 2 .   ? 35.058  15.264  33.262  1.00 85.60  ? 601 NAG C C3  1 
HETATM 12797 C  C4  . NAG K 2 .   ? 35.934  16.134  34.157  1.00 87.52  ? 601 NAG C C4  1 
HETATM 12798 C  C5  . NAG K 2 .   ? 36.434  17.339  33.371  1.00 86.62  ? 601 NAG C C5  1 
HETATM 12799 C  C6  . NAG K 2 .   ? 37.375  18.214  34.166  1.00 88.45  ? 601 NAG C C6  1 
HETATM 12800 C  C7  . NAG K 2 .   ? 34.989  12.804  30.952  1.00 82.61  ? 601 NAG C C7  1 
HETATM 12801 C  C8  . NAG K 2 .   ? 36.019  12.086  31.771  1.00 84.27  ? 601 NAG C C8  1 
HETATM 12802 N  N2  . NAG K 2 .   ? 34.936  14.130  31.091  1.00 82.24  ? 601 NAG C N2  1 
HETATM 12803 O  O3  . NAG K 2 .   ? 34.665  14.089  33.959  1.00 85.34  ? 601 NAG C O3  1 
HETATM 12804 O  O4  . NAG K 2 .   ? 35.190  16.578  35.286  1.00 89.74  ? 601 NAG C O4  1 
HETATM 12805 O  O5  . NAG K 2 .   ? 37.159  16.882  32.223  1.00 84.41  ? 601 NAG C O5  1 
HETATM 12806 O  O6  . NAG K 2 .   ? 37.110  18.131  35.560  1.00 90.00  ? 601 NAG C O6  1 
HETATM 12807 O  O7  . NAG K 2 .   ? 34.235  12.205  30.187  1.00 83.91  ? 601 NAG C O7  1 
HETATM 12808 CA CA  . CA  L 3 .   ? -7.840  -28.636 42.526  1.00 71.81  ? 602 CA  C CA  1 
HETATM 12809 CA CA  . CA  M 3 .   ? -15.330 -4.210  18.995  1.00 99.23  ? 603 CA  C CA  1 
HETATM 12810 CA CA  . CA  N 3 .   ? 13.099  -3.329  12.780  1.00 60.96  ? 604 CA  C CA  1 
HETATM 12811 C  C1  . NAG O 2 .   ? 23.244  -7.396  -13.231 1.00 83.04  ? 601 NAG D C1  1 
HETATM 12812 C  C2  . NAG O 2 .   ? 22.840  -6.351  -14.270 1.00 86.33  ? 601 NAG D C2  1 
HETATM 12813 C  C3  . NAG O 2 .   ? 22.136  -7.026  -15.445 1.00 90.66  ? 601 NAG D C3  1 
HETATM 12814 C  C4  . NAG O 2 .   ? 23.006  -8.136  -16.017 1.00 94.10  ? 601 NAG D C4  1 
HETATM 12815 C  C5  . NAG O 2 .   ? 23.385  -9.119  -14.914 1.00 92.93  ? 601 NAG D C5  1 
HETATM 12816 C  C6  . NAG O 2 .   ? 24.351  -10.186 -15.375 1.00 93.35  ? 601 NAG D C6  1 
HETATM 12817 C  C7  . NAG O 2 .   ? 22.201  -4.014  -13.857 1.00 81.50  ? 601 NAG D C7  1 
HETATM 12818 C  C8  . NAG O 2 .   ? 23.383  -3.638  -14.702 1.00 82.64  ? 601 NAG D C8  1 
HETATM 12819 N  N2  . NAG O 2 .   ? 21.995  -5.326  -13.687 1.00 84.42  ? 601 NAG D N2  1 
HETATM 12820 O  O3  . NAG O 2 .   ? 21.853  -6.059  -16.450 1.00 93.62  ? 601 NAG D O3  1 
HETATM 12821 O  O4  . NAG O 2 .   ? 22.309  -8.828  -17.047 1.00 96.10  ? 601 NAG D O4  1 
HETATM 12822 O  O5  . NAG O 2 .   ? 24.038  -8.415  -13.847 1.00 89.53  ? 601 NAG D O5  1 
HETATM 12823 O  O6  . NAG O 2 .   ? 23.994  -10.704 -16.648 1.00 95.27  ? 601 NAG D O6  1 
HETATM 12824 O  O7  . NAG O 2 .   ? 21.468  -3.170  -13.352 1.00 80.20  ? 601 NAG D O7  1 
HETATM 12825 CA CA  . CA  P 3 .   ? -28.222 15.308  -8.150  1.00 93.11  ? 602 CA  D CA  1 
HETATM 12826 CA CA  . CA  Q 3 .   ? -0.240  16.388  -1.097  1.00 82.01  ? 603 CA  D CA  1 
HETATM 12827 O  O   . HOH R 4 .   ? 40.220  15.507  98.270  1.00 63.13  ? 701 HOH A O   1 
HETATM 12828 O  O   . HOH R 4 .   ? 23.843  -1.354  77.431  1.00 42.73  ? 702 HOH A O   1 
HETATM 12829 O  O   . HOH R 4 .   ? 57.216  21.670  74.384  1.00 28.60  ? 703 HOH A O   1 
HETATM 12830 O  O   . HOH R 4 .   ? 35.448  18.915  80.181  1.00 31.47  ? 704 HOH A O   1 
HETATM 12831 O  O   . HOH R 4 .   ? 58.763  23.328  78.021  1.00 48.70  ? 705 HOH A O   1 
HETATM 12832 O  O   . HOH R 4 .   ? 24.178  8.264   83.848  1.00 37.11  ? 706 HOH A O   1 
HETATM 12833 O  O   . HOH R 4 .   ? 5.619   -23.903 97.088  1.00 64.04  ? 707 HOH A O   1 
HETATM 12834 O  O   . HOH R 4 .   ? 70.996  37.946  99.459  1.00 40.49  ? 708 HOH A O   1 
HETATM 12835 O  O   . HOH R 4 .   ? 18.982  -2.991  98.824  1.00 47.03  ? 709 HOH A O   1 
HETATM 12836 O  O   . HOH R 4 .   ? 33.480  17.340  78.673  1.00 20.19  ? 710 HOH A O   1 
HETATM 12837 O  O   . HOH R 4 .   ? 55.387  48.129  83.203  1.00 53.09  ? 711 HOH A O   1 
HETATM 12838 O  O   . HOH R 4 .   ? 61.106  17.812  87.875  1.00 51.13  ? 712 HOH A O   1 
HETATM 12839 O  O   . HOH R 4 .   ? 7.987   17.286  95.613  1.00 40.50  ? 713 HOH A O   1 
HETATM 12840 O  O   . HOH R 4 .   ? 43.179  24.345  95.586  1.00 43.15  ? 714 HOH A O   1 
HETATM 12841 O  O   . HOH R 4 .   ? 37.478  24.587  98.485  1.00 42.36  ? 715 HOH A O   1 
HETATM 12842 O  O   . HOH R 4 .   ? 22.265  14.977  100.721 1.00 54.19  ? 716 HOH A O   1 
HETATM 12843 O  O   . HOH R 4 .   ? 51.033  36.487  71.305  1.00 40.03  ? 717 HOH A O   1 
HETATM 12844 O  O   . HOH R 4 .   ? 30.881  24.877  86.189  1.00 29.81  ? 718 HOH A O   1 
HETATM 12845 O  O   . HOH R 4 .   ? 32.136  7.039   86.812  1.00 29.58  ? 719 HOH A O   1 
HETATM 12846 O  O   . HOH R 4 .   ? 67.202  39.293  98.001  1.00 39.72  ? 720 HOH A O   1 
HETATM 12847 O  O   . HOH R 4 .   ? 50.152  16.269  86.416  1.00 25.05  ? 721 HOH A O   1 
HETATM 12848 O  O   . HOH R 4 .   ? 19.083  4.714   75.757  1.00 47.06  ? 722 HOH A O   1 
HETATM 12849 O  O   . HOH R 4 .   ? 57.520  35.024  101.596 1.00 28.16  ? 723 HOH A O   1 
HETATM 12850 O  O   . HOH R 4 .   ? 17.420  -23.796 105.663 1.00 50.28  ? 724 HOH A O   1 
HETATM 12851 O  O   . HOH R 4 .   ? 37.700  17.449  80.438  1.00 39.54  ? 725 HOH A O   1 
HETATM 12852 O  O   . HOH R 4 .   ? 36.435  6.336   90.275  1.00 25.96  ? 726 HOH A O   1 
HETATM 12853 O  O   . HOH R 4 .   ? 22.277  5.467   102.096 1.00 60.67  ? 727 HOH A O   1 
HETATM 12854 O  O   . HOH R 4 .   ? 51.692  45.611  98.295  1.00 45.70  ? 728 HOH A O   1 
HETATM 12855 O  O   . HOH R 4 .   ? 25.049  9.119   87.999  1.00 20.55  ? 729 HOH A O   1 
HETATM 12856 O  O   . HOH R 4 .   ? 48.055  23.286  77.970  1.00 33.26  ? 730 HOH A O   1 
HETATM 12857 O  O   . HOH R 4 .   ? 35.537  8.181   83.920  1.00 56.47  ? 731 HOH A O   1 
HETATM 12858 O  O   . HOH R 4 .   ? 62.911  28.389  89.153  1.00 33.29  ? 732 HOH A O   1 
HETATM 12859 O  O   . HOH R 4 .   ? 27.310  14.465  79.297  1.00 27.28  ? 733 HOH A O   1 
HETATM 12860 O  O   . HOH R 4 .   ? 56.374  31.885  79.141  1.00 35.56  ? 734 HOH A O   1 
HETATM 12861 O  O   . HOH R 4 .   ? 60.034  34.179  81.784  1.00 27.37  ? 735 HOH A O   1 
HETATM 12862 O  O   . HOH R 4 .   ? 9.650   0.666   89.582  1.00 55.94  ? 736 HOH A O   1 
HETATM 12863 O  O   . HOH R 4 .   ? 56.370  46.828  95.952  1.00 25.60  ? 737 HOH A O   1 
HETATM 12864 O  O   . HOH R 4 .   ? 25.736  20.668  86.725  1.00 27.31  ? 738 HOH A O   1 
HETATM 12865 O  O   . HOH R 4 .   ? 58.827  21.006  91.964  1.00 48.72  ? 739 HOH A O   1 
HETATM 12866 O  O   . HOH R 4 .   ? 60.868  35.973  100.023 1.00 25.06  ? 740 HOH A O   1 
HETATM 12867 O  O   . HOH R 4 .   ? 36.392  10.206  79.939  1.00 38.19  ? 741 HOH A O   1 
HETATM 12868 O  O   . HOH R 4 .   ? 30.049  13.925  84.380  1.00 26.97  ? 742 HOH A O   1 
HETATM 12869 O  O   . HOH R 4 .   ? 55.583  20.557  73.320  1.00 41.89  ? 743 HOH A O   1 
HETATM 12870 O  O   . HOH R 4 .   ? 32.612  24.208  79.205  1.00 47.41  ? 744 HOH A O   1 
HETATM 12871 O  O   . HOH R 4 .   ? 21.014  14.957  80.590  1.00 41.01  ? 745 HOH A O   1 
HETATM 12872 O  O   . HOH R 4 .   ? 39.807  29.221  81.865  1.00 40.58  ? 746 HOH A O   1 
HETATM 12873 O  O   . HOH R 4 .   ? 65.573  36.955  98.426  1.00 42.62  ? 747 HOH A O   1 
HETATM 12874 O  O   . HOH R 4 .   ? 19.916  -20.038 88.695  1.00 32.87  ? 748 HOH A O   1 
HETATM 12875 O  O   . HOH R 4 .   ? 20.429  10.498  92.937  1.00 31.18  ? 749 HOH A O   1 
HETATM 12876 O  O   . HOH R 4 .   ? 15.739  13.172  95.474  1.00 61.47  ? 750 HOH A O   1 
HETATM 12877 O  O   . HOH R 4 .   ? 59.780  28.447  85.087  1.00 35.30  ? 751 HOH A O   1 
HETATM 12878 O  O   . HOH R 4 .   ? 12.491  -2.157  89.910  1.00 42.45  ? 752 HOH A O   1 
HETATM 12879 O  O   . HOH R 4 .   ? 77.446  34.962  93.033  1.00 33.70  ? 753 HOH A O   1 
HETATM 12880 O  O   . HOH R 4 .   ? 34.129  25.776  80.334  1.00 42.52  ? 754 HOH A O   1 
HETATM 12881 O  O   . HOH R 4 .   ? 20.773  9.579   86.103  1.00 29.92  ? 755 HOH A O   1 
HETATM 12882 O  O   . HOH R 4 .   ? 58.592  26.370  80.426  1.00 21.13  ? 756 HOH A O   1 
HETATM 12883 O  O   . HOH R 4 .   ? 44.401  23.503  76.994  1.00 30.65  ? 757 HOH A O   1 
HETATM 12884 O  O   . HOH R 4 .   ? 59.459  48.415  79.831  1.00 56.96  ? 758 HOH A O   1 
HETATM 12885 O  O   . HOH R 4 .   ? 68.475  38.160  100.548 1.00 47.42  ? 759 HOH A O   1 
HETATM 12886 O  O   . HOH R 4 .   ? 32.732  22.463  97.490  1.00 36.44  ? 760 HOH A O   1 
HETATM 12887 O  O   . HOH R 4 .   ? 14.610  -2.978  90.142  1.00 35.33  ? 761 HOH A O   1 
HETATM 12888 O  O   . HOH R 4 .   ? 30.129  23.443  77.918  1.00 41.03  ? 762 HOH A O   1 
HETATM 12889 O  O   . HOH R 4 .   ? 8.337   -0.925  88.574  1.00 46.87  ? 763 HOH A O   1 
HETATM 12890 O  O   . HOH R 4 .   ? 17.246  18.264  88.564  1.00 50.58  ? 764 HOH A O   1 
HETATM 12891 O  O   . HOH R 4 .   ? 42.153  33.077  91.065  1.00 48.12  ? 765 HOH A O   1 
HETATM 12892 O  O   . HOH R 4 .   ? 8.401   9.291   89.321  1.00 60.83  ? 766 HOH A O   1 
HETATM 12893 O  O   . HOH R 4 .   ? 58.874  23.441  85.496  1.00 25.36  ? 767 HOH A O   1 
HETATM 12894 O  O   . HOH R 4 .   ? 29.050  21.611  80.024  1.00 40.74  ? 768 HOH A O   1 
HETATM 12895 O  O   . HOH R 4 .   ? 56.715  33.208  75.986  1.00 22.13  ? 769 HOH A O   1 
HETATM 12896 O  O   . HOH R 4 .   ? 9.978   7.468   88.002  1.00 64.59  ? 770 HOH A O   1 
HETATM 12897 O  O   . HOH R 4 .   ? 17.593  15.034  83.351  1.00 47.87  ? 771 HOH A O   1 
HETATM 12898 O  O   . HOH R 4 .   ? 55.338  33.459  81.240  1.00 19.47  ? 772 HOH A O   1 
HETATM 12899 O  O   . HOH R 4 .   ? 4.445   -12.306 89.697  1.00 49.75  ? 773 HOH A O   1 
HETATM 12900 O  O   . HOH R 4 .   ? 52.164  15.298  94.963  1.00 45.67  ? 774 HOH A O   1 
HETATM 12901 O  O   . HOH R 4 .   ? 61.761  50.567  82.126  1.00 56.15  ? 775 HOH A O   1 
HETATM 12902 O  O   . HOH R 4 .   ? 77.246  34.395  89.860  1.00 49.79  ? 776 HOH A O   1 
HETATM 12903 O  O   . HOH R 4 .   ? 21.196  24.693  99.211  1.00 55.18  ? 777 HOH A O   1 
HETATM 12904 O  O   . HOH R 4 .   ? 35.754  19.185  76.136  1.00 42.84  ? 778 HOH A O   1 
HETATM 12905 O  O   . HOH R 4 .   ? 8.614   -1.847  86.003  1.00 52.93  ? 779 HOH A O   1 
HETATM 12906 O  O   . HOH R 4 .   ? 5.824   8.334   86.147  1.00 58.38  ? 780 HOH A O   1 
HETATM 12907 O  O   . HOH R 4 .   ? 24.001  18.278  84.126  1.00 17.10  ? 781 HOH A O   1 
HETATM 12908 O  O   . HOH R 4 .   ? 54.263  54.048  92.928  1.00 45.89  ? 782 HOH A O   1 
HETATM 12909 O  O   . HOH R 4 .   ? 57.774  23.168  81.252  1.00 23.34  ? 783 HOH A O   1 
HETATM 12910 O  O   . HOH R 4 .   ? 38.714  16.929  99.975  1.00 55.18  ? 784 HOH A O   1 
HETATM 12911 O  O   . HOH R 4 .   ? 67.174  40.365  102.398 1.00 37.90  ? 785 HOH A O   1 
HETATM 12912 O  O   . HOH R 4 .   ? 38.926  18.493  77.645  1.00 55.47  ? 786 HOH A O   1 
HETATM 12913 O  O   . HOH R 4 .   ? 34.831  6.685   82.611  1.00 60.40  ? 787 HOH A O   1 
HETATM 12914 O  O   . HOH R 4 .   ? 39.593  25.060  96.768  1.00 38.99  ? 788 HOH A O   1 
HETATM 12915 O  O   . HOH R 4 .   ? 58.130  56.752  98.181  1.00 48.66  ? 789 HOH A O   1 
HETATM 12916 O  O   . HOH R 4 .   ? 20.842  -5.460  77.873  1.00 35.17  ? 790 HOH A O   1 
HETATM 12917 O  O   . HOH R 4 .   ? 23.396  14.785  82.670  1.00 28.18  ? 791 HOH A O   1 
HETATM 12918 O  O   . HOH R 4 .   ? 61.265  22.683  85.770  1.00 41.19  ? 792 HOH A O   1 
HETATM 12919 O  O   . HOH R 4 .   ? 58.543  26.261  82.588  1.00 11.53  ? 793 HOH A O   1 
HETATM 12920 O  O   . HOH R 4 .   ? 23.250  8.459   85.973  1.00 43.48  ? 794 HOH A O   1 
HETATM 12921 O  O   . HOH R 4 .   ? 57.585  21.802  72.168  1.00 28.94  ? 795 HOH A O   1 
HETATM 12922 O  O   . HOH R 4 .   ? 23.919  22.462  86.416  1.00 42.06  ? 796 HOH A O   1 
HETATM 12923 O  O   . HOH R 4 .   ? 35.931  27.537  79.645  1.00 49.06  ? 797 HOH A O   1 
HETATM 12924 O  O   . HOH R 4 .   ? 28.301  15.404  76.944  1.00 37.32  ? 798 HOH A O   1 
HETATM 12925 O  O   . HOH R 4 .   ? 35.146  5.908   87.034  1.00 58.47  ? 799 HOH A O   1 
HETATM 12926 O  O   . HOH R 4 .   ? 55.744  47.637  85.985  1.00 42.95  ? 800 HOH A O   1 
HETATM 12927 O  O   . HOH R 4 .   ? 63.503  25.992  87.602  1.00 44.62  ? 801 HOH A O   1 
HETATM 12928 O  O   . HOH R 4 .   ? 58.229  26.081  84.762  1.00 20.61  ? 802 HOH A O   1 
HETATM 12929 O  O   . HOH S 4 .   ? 49.442  -0.025  66.867  1.00 75.37  ? 701 HOH B O   1 
HETATM 12930 O  O   . HOH S 4 .   ? 21.927  27.619  65.285  1.00 51.99  ? 702 HOH B O   1 
HETATM 12931 O  O   . HOH S 4 .   ? 10.215  21.513  66.801  1.00 33.82  ? 703 HOH B O   1 
HETATM 12932 O  O   . HOH S 4 .   ? -4.958  15.702  56.220  1.00 67.02  ? 704 HOH B O   1 
HETATM 12933 O  O   . HOH S 4 .   ? 45.556  13.565  68.637  1.00 62.11  ? 705 HOH B O   1 
HETATM 12934 O  O   . HOH S 4 .   ? 14.805  41.868  45.106  1.00 59.99  ? 706 HOH B O   1 
HETATM 12935 O  O   . HOH S 4 .   ? -7.025  27.063  62.402  1.00 45.50  ? 707 HOH B O   1 
HETATM 12936 O  O   . HOH S 4 .   ? 6.819   44.495  33.744  1.00 47.66  ? 708 HOH B O   1 
HETATM 12937 O  O   . HOH S 4 .   ? 48.482  7.305   56.673  1.00 37.35  ? 709 HOH B O   1 
HETATM 12938 O  O   . HOH S 4 .   ? 37.178  3.534   74.192  1.00 35.41  ? 710 HOH B O   1 
HETATM 12939 O  O   . HOH S 4 .   ? 5.060   19.564  65.751  1.00 37.30  ? 711 HOH B O   1 
HETATM 12940 O  O   . HOH S 4 .   ? 2.844   39.921  68.028  1.00 53.99  ? 712 HOH B O   1 
HETATM 12941 O  O   . HOH S 4 .   ? 17.110  7.015   69.050  1.00 47.90  ? 713 HOH B O   1 
HETATM 12942 O  O   . HOH S 4 .   ? 61.526  -10.455 71.652  1.00 49.51  ? 714 HOH B O   1 
HETATM 12943 O  O   . HOH S 4 .   ? 51.780  -17.104 77.921  1.00 60.31  ? 715 HOH B O   1 
HETATM 12944 O  O   . HOH S 4 .   ? -3.275  27.355  60.483  1.00 34.07  ? 716 HOH B O   1 
HETATM 12945 O  O   . HOH S 4 .   ? -1.237  35.660  55.250  1.00 43.18  ? 717 HOH B O   1 
HETATM 12946 O  O   . HOH S 4 .   ? 17.667  11.302  67.078  1.00 24.08  ? 718 HOH B O   1 
HETATM 12947 O  O   . HOH S 4 .   ? 42.125  -10.926 69.965  1.00 54.16  ? 719 HOH B O   1 
HETATM 12948 O  O   . HOH S 4 .   ? 6.168   54.288  53.854  1.00 42.50  ? 720 HOH B O   1 
HETATM 12949 O  O   . HOH S 4 .   ? -1.707  27.594  66.827  1.00 35.55  ? 721 HOH B O   1 
HETATM 12950 O  O   . HOH S 4 .   ? 43.190  7.741   73.550  1.00 51.69  ? 722 HOH B O   1 
HETATM 12951 O  O   . HOH S 4 .   ? 37.055  19.402  64.469  1.00 21.56  ? 723 HOH B O   1 
HETATM 12952 O  O   . HOH S 4 .   ? 30.998  14.441  75.750  1.00 33.00  ? 724 HOH B O   1 
HETATM 12953 O  O   . HOH S 4 .   ? 11.547  26.489  62.072  1.00 31.38  ? 725 HOH B O   1 
HETATM 12954 O  O   . HOH S 4 .   ? 1.504   36.940  55.441  1.00 27.65  ? 726 HOH B O   1 
HETATM 12955 O  O   . HOH S 4 .   ? 8.784   16.066  65.638  1.00 59.44  ? 727 HOH B O   1 
HETATM 12956 O  O   . HOH S 4 .   ? 12.381  25.424  60.327  1.00 55.86  ? 728 HOH B O   1 
HETATM 12957 O  O   . HOH S 4 .   ? 47.549  -3.074  55.501  1.00 41.73  ? 729 HOH B O   1 
HETATM 12958 O  O   . HOH S 4 .   ? 16.349  9.248   69.861  1.00 31.78  ? 730 HOH B O   1 
HETATM 12959 O  O   . HOH S 4 .   ? 24.000  29.472  65.998  1.00 43.72  ? 731 HOH B O   1 
HETATM 12960 O  O   . HOH S 4 .   ? 16.874  22.054  65.866  1.00 35.52  ? 732 HOH B O   1 
HETATM 12961 O  O   . HOH S 4 .   ? 3.729   40.693  69.995  1.00 47.29  ? 733 HOH B O   1 
HETATM 12962 O  O   . HOH S 4 .   ? -2.120  43.151  63.970  1.00 46.18  ? 734 HOH B O   1 
HETATM 12963 O  O   . HOH S 4 .   ? -0.170  22.463  55.401  1.00 39.47  ? 735 HOH B O   1 
HETATM 12964 O  O   . HOH S 4 .   ? 30.296  25.985  56.899  1.00 52.51  ? 736 HOH B O   1 
HETATM 12965 O  O   . HOH S 4 .   ? 4.565   21.577  67.317  1.00 27.67  ? 737 HOH B O   1 
HETATM 12966 O  O   . HOH S 4 .   ? 6.099   24.970  52.931  1.00 55.11  ? 738 HOH B O   1 
HETATM 12967 O  O   . HOH S 4 .   ? 23.317  27.833  58.612  1.00 39.94  ? 739 HOH B O   1 
HETATM 12968 O  O   . HOH S 4 .   ? 35.032  14.533  75.320  1.00 28.71  ? 740 HOH B O   1 
HETATM 12969 O  O   . HOH S 4 .   ? 22.980  26.732  69.238  1.00 31.56  ? 741 HOH B O   1 
HETATM 12970 O  O   . HOH S 4 .   ? 25.301  14.900  51.911  1.00 43.27  ? 742 HOH B O   1 
HETATM 12971 O  O   . HOH S 4 .   ? 20.673  32.522  54.593  1.00 47.74  ? 743 HOH B O   1 
HETATM 12972 O  O   . HOH S 4 .   ? 7.056   23.192  56.377  1.00 29.57  ? 744 HOH B O   1 
HETATM 12973 O  O   . HOH S 4 .   ? -3.924  31.428  58.287  1.00 44.14  ? 745 HOH B O   1 
HETATM 12974 O  O   . HOH S 4 .   ? 7.607   26.009  63.467  1.00 26.46  ? 746 HOH B O   1 
HETATM 12975 O  O   . HOH S 4 .   ? 1.280   27.691  68.881  1.00 35.52  ? 747 HOH B O   1 
HETATM 12976 O  O   . HOH S 4 .   ? 40.100  5.003   79.701  1.00 46.15  ? 748 HOH B O   1 
HETATM 12977 O  O   . HOH S 4 .   ? 7.625   22.928  53.108  1.00 56.62  ? 749 HOH B O   1 
HETATM 12978 O  O   . HOH S 4 .   ? 12.535  15.209  65.826  1.00 30.15  ? 750 HOH B O   1 
HETATM 12979 O  O   . HOH S 4 .   ? 26.774  0.711   67.960  1.00 38.10  ? 751 HOH B O   1 
HETATM 12980 O  O   . HOH S 4 .   ? 45.262  12.829  61.054  1.00 33.99  ? 752 HOH B O   1 
HETATM 12981 O  O   . HOH S 4 .   ? 6.554   17.045  59.647  1.00 52.46  ? 753 HOH B O   1 
HETATM 12982 O  O   . HOH S 4 .   ? 22.559  19.401  75.531  1.00 52.10  ? 754 HOH B O   1 
HETATM 12983 O  O   . HOH S 4 .   ? 38.647  -1.689  78.267  1.00 36.97  ? 755 HOH B O   1 
HETATM 12984 O  O   . HOH S 4 .   ? 28.510  25.506  63.153  1.00 37.62  ? 756 HOH B O   1 
HETATM 12985 O  O   . HOH S 4 .   ? 25.807  15.904  74.893  1.00 37.51  ? 757 HOH B O   1 
HETATM 12986 O  O   . HOH S 4 .   ? 59.374  0.943   68.639  1.00 63.99  ? 758 HOH B O   1 
HETATM 12987 O  O   . HOH S 4 .   ? 43.325  3.306   57.659  1.00 31.90  ? 759 HOH B O   1 
HETATM 12988 O  O   . HOH S 4 .   ? 4.428   42.587  67.645  1.00 49.53  ? 760 HOH B O   1 
HETATM 12989 O  O   . HOH S 4 .   ? 19.553  14.811  74.477  1.00 42.59  ? 761 HOH B O   1 
HETATM 12990 O  O   . HOH S 4 .   ? 10.786  18.255  67.517  1.00 16.07  ? 762 HOH B O   1 
HETATM 12991 O  O   . HOH S 4 .   ? 3.143   26.029  52.672  1.00 56.76  ? 763 HOH B O   1 
HETATM 12992 O  O   . HOH S 4 .   ? 58.838  -3.939  57.341  1.00 35.47  ? 764 HOH B O   1 
HETATM 12993 O  O   . HOH S 4 .   ? 6.578   20.114  50.605  1.00 67.21  ? 765 HOH B O   1 
HETATM 12994 O  O   . HOH S 4 .   ? 10.816  22.042  69.341  1.00 27.92  ? 766 HOH B O   1 
HETATM 12995 O  O   . HOH S 4 .   ? 26.169  8.277   73.026  1.00 38.61  ? 767 HOH B O   1 
HETATM 12996 O  O   . HOH S 4 .   ? 21.765  18.203  77.420  1.00 56.91  ? 768 HOH B O   1 
HETATM 12997 O  O   . HOH S 4 .   ? 4.580   22.265  53.879  1.00 54.91  ? 769 HOH B O   1 
HETATM 12998 O  O   . HOH S 4 .   ? -5.123  21.249  60.345  1.00 40.60  ? 770 HOH B O   1 
HETATM 12999 O  O   . HOH S 4 .   ? 42.610  -10.838 55.154  1.00 50.19  ? 771 HOH B O   1 
HETATM 13000 O  O   . HOH S 4 .   ? -2.154  30.138  53.336  1.00 36.01  ? 772 HOH B O   1 
HETATM 13001 O  O   . HOH S 4 .   ? -3.709  32.922  55.603  1.00 55.28  ? 773 HOH B O   1 
HETATM 13002 O  O   . HOH S 4 .   ? 7.798   20.250  67.299  1.00 43.98  ? 774 HOH B O   1 
HETATM 13003 O  O   . HOH S 4 .   ? 4.880   22.110  51.076  1.00 51.02  ? 775 HOH B O   1 
HETATM 13004 O  O   . HOH S 4 .   ? 21.623  29.993  66.072  1.00 52.44  ? 776 HOH B O   1 
HETATM 13005 O  O   . HOH S 4 .   ? 9.688   27.277  63.136  1.00 28.77  ? 777 HOH B O   1 
HETATM 13006 O  O   . HOH S 4 .   ? 62.745  -8.606  72.161  1.00 48.74  ? 778 HOH B O   1 
HETATM 13007 O  O   . HOH S 4 .   ? 40.623  -13.065 72.768  1.00 40.50  ? 779 HOH B O   1 
HETATM 13008 O  O   . HOH S 4 .   ? 40.859  -12.953 69.915  1.00 35.92  ? 780 HOH B O   1 
HETATM 13009 O  O   . HOH S 4 .   ? 6.587   42.925  66.877  1.00 28.31  ? 781 HOH B O   1 
HETATM 13010 O  O   . HOH S 4 .   ? 49.632  8.507   65.062  1.00 37.80  ? 782 HOH B O   1 
HETATM 13011 O  O   . HOH S 4 .   ? 24.788  26.987  60.178  1.00 49.91  ? 783 HOH B O   1 
HETATM 13012 O  O   . HOH S 4 .   ? 10.365  13.808  66.705  1.00 33.15  ? 784 HOH B O   1 
HETATM 13013 O  O   . HOH S 4 .   ? 9.012   16.290  68.634  1.00 38.39  ? 785 HOH B O   1 
HETATM 13014 O  O   . HOH S 4 .   ? 8.358   20.902  70.434  1.00 52.71  ? 786 HOH B O   1 
HETATM 13015 O  O   . HOH T 4 .   ? 33.644  9.539   5.810   1.00 55.83  ? 701 HOH C O   1 
HETATM 13016 O  O   . HOH T 4 .   ? 7.739   13.203  17.791  1.00 48.36  ? 702 HOH C O   1 
HETATM 13017 O  O   . HOH T 4 .   ? -6.297  -30.434 42.850  1.00 54.83  ? 703 HOH C O   1 
HETATM 13018 O  O   . HOH T 4 .   ? -13.765 -13.082 19.310  1.00 60.64  ? 704 HOH C O   1 
HETATM 13019 O  O   . HOH T 4 .   ? 4.728   2.695   10.930  1.00 46.35  ? 705 HOH C O   1 
HETATM 13020 O  O   . HOH T 4 .   ? -5.586  -36.115 37.556  1.00 50.39  ? 706 HOH C O   1 
HETATM 13021 O  O   . HOH T 4 .   ? -9.699  -28.571 38.949  1.00 38.30  ? 707 HOH C O   1 
HETATM 13022 O  O   . HOH T 4 .   ? 14.015  -5.504  22.077  1.00 39.47  ? 708 HOH C O   1 
HETATM 13023 O  O   . HOH T 4 .   ? 14.947  5.377   12.101  1.00 56.66  ? 709 HOH C O   1 
HETATM 13024 O  O   . HOH T 4 .   ? 6.586   10.332  10.627  1.00 50.95  ? 710 HOH C O   1 
HETATM 13025 O  O   . HOH T 4 .   ? 0.835   -26.678 21.460  1.00 50.91  ? 711 HOH C O   1 
HETATM 13026 O  O   . HOH T 4 .   ? 21.817  11.821  8.474   1.00 41.22  ? 712 HOH C O   1 
HETATM 13027 O  O   . HOH T 4 .   ? -1.423  4.392   16.341  1.00 41.61  ? 713 HOH C O   1 
HETATM 13028 O  O   . HOH T 4 .   ? -7.898  1.013   25.885  1.00 56.80  ? 714 HOH C O   1 
HETATM 13029 O  O   . HOH T 4 .   ? 12.120  2.639   6.769   1.00 52.39  ? 715 HOH C O   1 
HETATM 13030 O  O   . HOH T 4 .   ? -1.327  -6.895  33.169  1.00 61.10  ? 716 HOH C O   1 
HETATM 13031 O  O   . HOH T 4 .   ? 13.276  -1.345  11.458  1.00 55.71  ? 717 HOH C O   1 
HETATM 13032 O  O   . HOH T 4 .   ? 32.230  17.939  3.417   1.00 45.80  ? 718 HOH C O   1 
HETATM 13033 O  O   . HOH T 4 .   ? 37.259  22.342  13.637  1.00 57.36  ? 719 HOH C O   1 
HETATM 13034 O  O   . HOH T 4 .   ? -13.021 -4.385  19.590  1.00 56.69  ? 720 HOH C O   1 
HETATM 13035 O  O   . HOH T 4 .   ? -8.319  -35.828 38.664  1.00 100.00 ? 721 HOH C O   1 
HETATM 13036 O  O   . HOH T 4 .   ? 32.426  21.372  12.667  1.00 34.34  ? 722 HOH C O   1 
HETATM 13037 O  O   . HOH T 4 .   ? -7.135  -38.196 37.335  1.00 54.74  ? 723 HOH C O   1 
HETATM 13038 O  O   . HOH T 4 .   ? -14.372 -2.495  20.358  1.00 71.50  ? 724 HOH C O   1 
HETATM 13039 O  O   . HOH T 4 .   ? 35.155  9.498   4.125   1.00 52.61  ? 725 HOH C O   1 
HETATM 13040 O  O   . HOH T 4 .   ? 2.833   8.582   18.166  1.00 41.56  ? 726 HOH C O   1 
HETATM 13041 O  O   . HOH T 4 .   ? 27.490  3.990   18.192  1.00 46.16  ? 727 HOH C O   1 
HETATM 13042 O  O   . HOH T 4 .   ? 25.484  11.753  9.965   1.00 54.08  ? 728 HOH C O   1 
HETATM 13043 O  O   . HOH T 4 .   ? 20.110  -0.893  10.266  1.00 41.00  ? 729 HOH C O   1 
HETATM 13044 O  O   . HOH T 4 .   ? 10.958  13.768  12.219  1.00 47.20  ? 730 HOH C O   1 
HETATM 13045 O  O   . HOH T 4 .   ? -2.480  -1.537  24.894  1.00 43.25  ? 731 HOH C O   1 
HETATM 13046 O  O   . HOH T 4 .   ? 36.801  16.493  16.485  1.00 54.62  ? 732 HOH C O   1 
HETATM 13047 O  O   . HOH T 4 .   ? 33.508  19.490  10.594  1.00 39.16  ? 733 HOH C O   1 
HETATM 13048 O  O   . HOH T 4 .   ? 33.851  21.298  7.702   1.00 34.10  ? 734 HOH C O   1 
HETATM 13049 O  O   . HOH T 4 .   ? 29.886  5.893   31.187  1.00 56.94  ? 735 HOH C O   1 
HETATM 13050 O  O   . HOH T 4 .   ? 12.804  17.424  27.313  1.00 54.30  ? 736 HOH C O   1 
HETATM 13051 O  O   . HOH T 4 .   ? 35.939  11.648  16.854  1.00 40.85  ? 737 HOH C O   1 
HETATM 13052 O  O   . HOH T 4 .   ? -19.017 -20.434 32.060  1.00 66.58  ? 738 HOH C O   1 
HETATM 13053 O  O   . HOH T 4 .   ? -5.135  3.152   15.019  1.00 32.90  ? 739 HOH C O   1 
HETATM 13054 O  O   . HOH T 4 .   ? -2.785  5.446   23.815  1.00 49.83  ? 740 HOH C O   1 
HETATM 13055 O  O   . HOH T 4 .   ? -9.728  -37.542 39.757  1.00 56.78  ? 741 HOH C O   1 
HETATM 13056 O  O   . HOH T 4 .   ? 35.903  14.703  13.420  1.00 27.36  ? 742 HOH C O   1 
HETATM 13057 O  O   . HOH T 4 .   ? 42.702  12.976  9.042   1.00 46.09  ? 743 HOH C O   1 
HETATM 13058 O  O   . HOH T 4 .   ? -1.145  7.908   17.791  1.00 52.80  ? 744 HOH C O   1 
HETATM 13059 O  O   . HOH T 4 .   ? 11.612  -6.091  15.575  1.00 52.95  ? 745 HOH C O   1 
HETATM 13060 O  O   . HOH T 4 .   ? 13.061  15.691  11.749  1.00 38.67  ? 746 HOH C O   1 
HETATM 13061 O  O   . HOH T 4 .   ? 40.396  18.291  31.917  1.00 60.00  ? 747 HOH C O   1 
HETATM 13062 O  O   . HOH T 4 .   ? 28.498  2.159   19.850  1.00 51.46  ? 748 HOH C O   1 
HETATM 13063 O  O   . HOH T 4 .   ? 21.410  -3.681  13.425  1.00 42.58  ? 749 HOH C O   1 
HETATM 13064 O  O   . HOH T 4 .   ? 31.656  18.703  25.325  1.00 51.90  ? 750 HOH C O   1 
HETATM 13065 O  O   . HOH T 4 .   ? 29.174  17.373  36.484  1.00 56.46  ? 751 HOH C O   1 
HETATM 13066 O  O   . HOH T 4 .   ? 0.760   10.234  17.372  1.00 43.90  ? 752 HOH C O   1 
HETATM 13067 O  O   . HOH T 4 .   ? 35.160  14.602  15.861  1.00 40.10  ? 753 HOH C O   1 
HETATM 13068 O  O   . HOH U 4 .   ? -4.003  16.617  -6.029  1.00 48.53  ? 701 HOH D O   1 
HETATM 13069 O  O   . HOH U 4 .   ? -6.054  10.281  -2.032  1.00 37.62  ? 702 HOH D O   1 
HETATM 13070 O  O   . HOH U 4 .   ? -16.238 41.945  -16.303 1.00 49.59  ? 703 HOH D O   1 
HETATM 13071 O  O   . HOH U 4 .   ? 19.861  -4.365  4.727   1.00 67.49  ? 704 HOH D O   1 
HETATM 13072 O  O   . HOH U 4 .   ? 25.191  -14.861 -13.331 1.00 62.45  ? 705 HOH D O   1 
HETATM 13073 O  O   . HOH U 4 .   ? -21.841 25.122  -12.871 1.00 63.81  ? 706 HOH D O   1 
HETATM 13074 O  O   . HOH U 4 .   ? -10.385 3.445   -2.697  1.00 36.76  ? 707 HOH D O   1 
HETATM 13075 O  O   . HOH U 4 .   ? -24.728 15.073  -1.822  1.00 36.19  ? 708 HOH D O   1 
HETATM 13076 O  O   . HOH U 4 .   ? -27.903 23.324  -10.751 1.00 66.91  ? 709 HOH D O   1 
HETATM 13077 O  O   . HOH U 4 .   ? -5.314  -0.876  -1.485  1.00 47.41  ? 710 HOH D O   1 
HETATM 13078 O  O   . HOH U 4 .   ? -13.854 37.449  -9.724  1.00 49.09  ? 711 HOH D O   1 
HETATM 13079 O  O   . HOH U 4 .   ? -25.839 15.488  -8.176  1.00 56.65  ? 712 HOH D O   1 
HETATM 13080 O  O   . HOH U 4 .   ? -10.877 7.686   2.000   1.00 43.14  ? 713 HOH D O   1 
HETATM 13081 O  O   . HOH U 4 .   ? -15.793 11.501  -11.477 1.00 48.10  ? 714 HOH D O   1 
HETATM 13082 O  O   . HOH U 4 .   ? 3.061   3.398   6.408   1.00 62.94  ? 715 HOH D O   1 
HETATM 13083 O  O   . HOH U 4 .   ? -11.047 14.400  -7.041  1.00 46.48  ? 716 HOH D O   1 
HETATM 13084 O  O   . HOH U 4 .   ? -6.149  -3.526  -14.883 1.00 50.44  ? 717 HOH D O   1 
HETATM 13085 O  O   . HOH U 4 .   ? -24.209 23.787  -13.124 1.00 36.70  ? 718 HOH D O   1 
HETATM 13086 O  O   . HOH U 4 .   ? -26.937 19.512  -10.105 1.00 48.41  ? 719 HOH D O   1 
HETATM 13087 O  O   . HOH U 4 .   ? -18.661 30.274  1.125   1.00 55.10  ? 720 HOH D O   1 
HETATM 13088 O  O   . HOH U 4 .   ? -21.305 30.196  1.372   1.00 50.65  ? 721 HOH D O   1 
HETATM 13089 O  O   . HOH U 4 .   ? 25.407  -0.885  -6.438  1.00 49.60  ? 722 HOH D O   1 
HETATM 13090 O  O   . HOH U 4 .   ? -26.938 43.366  -31.036 1.00 57.10  ? 723 HOH D O   1 
HETATM 13091 O  O   . HOH U 4 .   ? 3.153   -15.482 8.798   1.00 60.38  ? 724 HOH D O   1 
HETATM 13092 O  O   . HOH U 4 .   ? -18.424 7.648   -2.566  1.00 44.70  ? 725 HOH D O   1 
HETATM 13093 O  O   . HOH U 4 .   ? 25.431  -4.301  -12.214 1.00 53.97  ? 726 HOH D O   1 
HETATM 13094 O  O   . HOH U 4 .   ? -19.985 28.219  0.830   1.00 58.53  ? 727 HOH D O   1 
HETATM 13095 O  O   . HOH U 4 .   ? -11.341 17.210  1.787   1.00 62.06  ? 728 HOH D O   1 
HETATM 13096 O  O   . HOH U 4 .   ? 12.856  15.439  -0.563  1.00 46.42  ? 729 HOH D O   1 
HETATM 13097 O  O   . HOH U 4 .   ? 20.795  -14.153 -15.031 1.00 52.79  ? 730 HOH D O   1 
HETATM 13098 O  O   . HOH U 4 .   ? -18.479 33.185  -2.128  1.00 41.70  ? 731 HOH D O   1 
HETATM 13099 O  O   . HOH U 4 .   ? -12.086 10.627  1.191   1.00 49.76  ? 732 HOH D O   1 
HETATM 13100 O  O   . HOH U 4 .   ? 26.864  -3.350  -2.549  1.00 40.86  ? 733 HOH D O   1 
HETATM 13101 O  O   . HOH U 4 .   ? -12.084 6.441   -0.821  1.00 36.08  ? 734 HOH D O   1 
HETATM 13102 O  O   . HOH U 4 .   ? -28.424 9.030   -8.131  1.00 46.20  ? 735 HOH D O   1 
HETATM 13103 O  O   . HOH U 4 .   ? 17.596  -2.948  -15.157 1.00 58.94  ? 736 HOH D O   1 
HETATM 13104 O  O   . HOH U 4 .   ? -22.207 2.465   -7.054  1.00 58.07  ? 737 HOH D O   1 
HETATM 13105 O  O   . HOH U 4 .   ? -1.089  17.679  -2.922  1.00 72.39  ? 738 HOH D O   1 
HETATM 13106 O  O   . HOH U 4 .   ? 22.504  1.387   -7.092  1.00 36.94  ? 739 HOH D O   1 
HETATM 13107 O  O   . HOH U 4 .   ? -25.943 47.167  -37.777 1.00 38.52  ? 740 HOH D O   1 
HETATM 13108 O  O   . HOH U 4 .   ? -16.727 31.127  -1.616  1.00 53.33  ? 741 HOH D O   1 
HETATM 13109 O  O   . HOH U 4 .   ? 10.490  12.340  -10.730 1.00 54.15  ? 742 HOH D O   1 
HETATM 13110 O  O   . HOH U 4 .   ? -6.480  20.162  -1.799  1.00 54.51  ? 743 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N  N   . PRO A 24  ? 1.1419 0.9448 1.7818 -0.1931 -0.1164 0.1520  25  PRO A N   
2     C  CA  . PRO A 24  ? 1.1798 0.9755 1.8225 -0.2049 -0.1201 0.1549  25  PRO A CA  
3     C  C   . PRO A 24  ? 1.1955 0.9946 1.8397 -0.2020 -0.1111 0.1349  25  PRO A C   
4     O  O   . PRO A 24  ? 1.2162 1.0269 1.8481 -0.2142 -0.1049 0.1353  25  PRO A O   
5     C  CB  . PRO A 24  ? 1.1524 0.9613 1.7735 -0.2247 -0.1183 0.1727  25  PRO A CB  
6     C  CG  . PRO A 24  ? 1.1698 0.9882 1.7798 -0.2233 -0.1175 0.1821  25  PRO A CG  
7     C  CD  . PRO A 24  ? 1.1168 0.9360 1.7350 -0.2038 -0.1123 0.1658  25  PRO A CD  
8     N  N   . ALA A 25  ? 1.2418 1.0321 1.9019 -0.1867 -0.1106 0.1175  26  ALA A N   
9     C  CA  . ALA A 25  ? 1.2664 1.0564 1.9303 -0.1845 -0.1049 0.0988  26  ALA A CA  
10    C  C   . ALA A 25  ? 1.3247 1.0934 2.0118 -0.1798 -0.1139 0.0929  26  ALA A C   
11    O  O   . ALA A 25  ? 1.3608 1.1165 2.0612 -0.1789 -0.1247 0.1048  26  ALA A O   
12    C  CB  . ALA A 25  ? 1.2334 1.0351 1.8928 -0.1720 -0.0942 0.0806  26  ALA A CB  
13    N  N   . SER A 26  ? 1.3098 1.0755 2.0024 -0.1774 -0.1098 0.0748  27  SER A N   
14    C  CA  . SER A 26  ? 1.3219 1.0684 2.0368 -0.1739 -0.1168 0.0662  27  SER A CA  
15    C  C   . SER A 26  ? 1.3415 1.0750 2.0636 -0.1865 -0.1282 0.0839  27  SER A C   
16    O  O   . SER A 26  ? 1.3879 1.1057 2.1303 -0.1826 -0.1388 0.0899  27  SER A O   
17    C  CB  . SER A 26  ? 1.2799 1.0183 2.0143 -0.1579 -0.1195 0.0579  27  SER A CB  
18    O  OG  . SER A 26  ? 1.2725 1.0062 2.0134 -0.1573 -0.1289 0.0769  27  SER A OG  
19    N  N   . LYS A 27  ? 1.3421 1.0834 2.0483 -0.2018 -0.1260 0.0923  28  LYS A N   
20    C  CA  . LYS A 27  ? 1.3499 1.0807 2.0599 -0.2163 -0.1352 0.1077  28  LYS A CA  
21    C  C   . LYS A 27  ? 1.3228 1.0481 2.0342 -0.2217 -0.1459 0.1320  28  LYS A C   
22    O  O   . LYS A 27  ? 1.3815 1.0909 2.1067 -0.2279 -0.1577 0.1430  28  LYS A O   
23    C  CB  . LYS A 27  ? 1.3757 1.0868 2.1084 -0.2134 -0.1413 0.0962  28  LYS A CB  
24    N  N   . SER A 28  ? 1.2141 0.9525 1.9115 -0.2199 -0.1426 0.1405  29  SER A N   
25    C  CA  . SER A 28  ? 1.1248 0.8623 1.8167 -0.2293 -0.1517 0.1652  29  SER A CA  
26    C  C   . SER A 28  ? 1.0222 0.7824 1.6869 -0.2374 -0.1420 0.1729  29  SER A C   
27    O  O   . SER A 28  ? 1.0165 0.7889 1.6739 -0.2275 -0.1324 0.1617  29  SER A O   
28    C  CB  . SER A 28  ? 1.1176 0.8428 1.8293 -0.2164 -0.1626 0.1698  29  SER A CB  
29    O  OG  . SER A 28  ? 1.1133 0.8383 1.8189 -0.2264 -0.1729 0.1947  29  SER A OG  
30    N  N   . ARG A 29  ? 0.9861 0.7528 1.6360 -0.2561 -0.1440 0.1910  30  ARG A N   
31    C  CA  . ARG A 29  ? 0.8615 0.6511 1.4862 -0.2656 -0.1342 0.1982  30  ARG A CA  
32    C  C   . ARG A 29  ? 0.8338 0.6236 1.4519 -0.2691 -0.1423 0.2180  30  ARG A C   
33    O  O   . ARG A 29  ? 0.8401 0.6487 1.4369 -0.2788 -0.1348 0.2252  30  ARG A O   
34    C  CB  . ARG A 29  ? 0.9139 0.7165 1.5240 -0.2855 -0.1278 0.2028  30  ARG A CB  
35    C  CG  . ARG A 29  ? 0.9085 0.7066 1.5285 -0.2841 -0.1245 0.1869  30  ARG A CG  
36    C  CD  . ARG A 29  ? 0.9088 0.7240 1.5156 -0.3022 -0.1160 0.1879  30  ARG A CD  
37    N  NE  . ARG A 29  ? 0.8923 0.7088 1.5067 -0.2976 -0.1103 0.1688  30  ARG A NE  
38    C  CZ  . ARG A 29  ? 0.8877 0.7167 1.4966 -0.3109 -0.1040 0.1657  30  ARG A CZ  
39    N  NH1 . ARG A 29  ? 0.7956 0.6371 1.3922 -0.3299 -0.1015 0.1797  30  ARG A NH1 
40    N  NH2 . ARG A 29  ? 0.8289 0.6584 1.4453 -0.3060 -0.1004 0.1485  30  ARG A NH2 
41    N  N   . SER A 30  ? 0.8560 0.6260 1.4932 -0.2621 -0.1577 0.2266  31  SER A N   
42    C  CA  . SER A 30  ? 0.8773 0.6465 1.5108 -0.2652 -0.1681 0.2464  31  SER A CA  
43    C  C   . SER A 30  ? 0.8336 0.6167 1.4567 -0.2551 -0.1594 0.2401  31  SER A C   
44    O  O   . SER A 30  ? 0.7591 0.5407 1.3934 -0.2372 -0.1537 0.2216  31  SER A O   
45    C  CB  . SER A 30  ? 0.9484 0.6944 1.6106 -0.2567 -0.1869 0.2538  31  SER A CB  
46    O  OG  . SER A 30  ? 0.9602 0.7002 1.6423 -0.2349 -0.1855 0.2363  31  SER A OG  
47    N  N   . CYS A 31  ? 0.8278 0.6252 1.4289 -0.2676 -0.1580 0.2552  32  CYS A N   
48    C  CA  . CYS A 31  ? 0.7992 0.6117 1.3876 -0.2608 -0.1487 0.2502  32  CYS A CA  
49    C  C   . CYS A 31  ? 0.7954 0.5983 1.3957 -0.2505 -0.1617 0.2594  32  CYS A C   
50    O  O   . CYS A 31  ? 0.8011 0.6160 1.3877 -0.2504 -0.1580 0.2633  32  CYS A O   
51    C  CB  . CYS A 31  ? 0.8026 0.6381 1.3611 -0.2802 -0.1390 0.2597  32  CYS A CB  
52    S  SG  . CYS A 31  ? 0.7481 0.6030 1.2935 -0.2905 -0.1198 0.2447  32  CYS A SG  
53    N  N   . GLY A 32  ? 0.8956 0.6779 1.5230 -0.2419 -0.1766 0.2621  33  GLY A N   
54    C  CA  . GLY A 32  ? 0.9462 0.7192 1.5900 -0.2333 -0.1915 0.2724  33  GLY A CA  
55    C  C   . GLY A 32  ? 0.9303 0.7110 1.5754 -0.2174 -0.1847 0.2609  33  GLY A C   
56    O  O   . GLY A 32  ? 0.9691 0.7554 1.6066 -0.2199 -0.1906 0.2742  33  GLY A O   
57    N  N   . GLU A 33  ? 0.9353 0.7167 1.5895 -0.2017 -0.1727 0.2366  34  GLU A N   
58    C  CA  . GLU A 33  ? 0.8864 0.6743 1.5440 -0.1856 -0.1659 0.2239  34  GLU A CA  
59    C  C   . GLU A 33  ? 0.8367 0.6445 1.4644 -0.1928 -0.1537 0.2265  34  GLU A C   
60    O  O   . GLU A 33  ? 0.7954 0.6088 1.4204 -0.1875 -0.1547 0.2298  34  GLU A O   
61    C  CB  . GLU A 33  ? 0.9514 0.7362 1.6240 -0.1692 -0.1557 0.1972  34  GLU A CB  
62    C  CG  . GLU A 33  ? 1.0602 0.8272 1.7608 -0.1641 -0.1649 0.1916  34  GLU A CG  
63    C  CD  . GLU A 33  ? 1.1095 0.8735 1.8299 -0.1454 -0.1579 0.1661  34  GLU A CD  
64    O  OE1 . GLU A 33  ? 1.0892 0.8652 1.7973 -0.1387 -0.1437 0.1510  34  GLU A OE1 
65    O  OE2 . GLU A 33  ? 1.1520 0.9025 1.9009 -0.1381 -0.1664 0.1607  34  GLU A OE2 
66    N  N   . VAL A 34  ? 0.7918 0.6114 1.3988 -0.2053 -0.1422 0.2241  35  VAL A N   
67    C  CA  . VAL A 34  ? 0.7519 0.5927 1.3318 -0.2146 -0.1299 0.2260  35  VAL A CA  
68    C  C   . VAL A 34  ? 0.7788 0.6234 1.3445 -0.2291 -0.1396 0.2498  35  VAL A C   
69    O  O   . VAL A 34  ? 0.7506 0.6082 1.3017 -0.2306 -0.1346 0.2524  35  VAL A O   
70    C  CB  . VAL A 34  ? 0.7110 0.5653 1.2751 -0.2269 -0.1167 0.2193  35  VAL A CB  
71    C  CG1 . VAL A 34  ? 0.6499 0.5283 1.1879 -0.2394 -0.1046 0.2226  35  VAL A CG1 
72    C  CG2 . VAL A 34  ? 0.6347 0.4883 1.2102 -0.2127 -0.1070 0.1958  35  VAL A CG2 
73    N  N   . ARG A 35  ? 0.8156 0.6489 1.3859 -0.2403 -0.1542 0.2673  36  ARG A N   
74    C  CA  . ARG A 35  ? 0.8860 0.7217 1.4437 -0.2553 -0.1665 0.2919  36  ARG A CA  
75    C  C   . ARG A 35  ? 0.9590 0.7894 1.5290 -0.2431 -0.1772 0.2972  36  ARG A C   
76    O  O   . ARG A 35  ? 0.9696 0.8124 1.5212 -0.2503 -0.1767 0.3068  36  ARG A O   
77    C  CB  . ARG A 35  ? 0.7869 0.6092 1.3521 -0.2676 -0.1823 0.3094  36  ARG A CB  
78    N  N   . GLN A 36  ? 1.0179 0.8314 1.6197 -0.2252 -0.1863 0.2897  37  GLN A N   
79    C  CA  . GLN A 36  ? 1.0745 0.8832 1.6939 -0.2125 -0.1972 0.2931  37  GLN A CA  
80    C  C   . GLN A 36  ? 0.9939 0.8162 1.6024 -0.2027 -0.1829 0.2798  37  GLN A C   
81    O  O   . GLN A 36  ? 1.0275 0.8551 1.6314 -0.2033 -0.1888 0.2899  37  GLN A O   
82    C  CB  . GLN A 36  ? 1.1485 0.9394 1.8070 -0.1949 -0.2065 0.2829  37  GLN A CB  
83    C  CG  . GLN A 36  ? 1.1850 0.9764 1.8632 -0.1747 -0.2051 0.2694  37  GLN A CG  
84    C  CD  . GLN A 36  ? 1.2456 1.0222 1.9641 -0.1594 -0.2144 0.2592  37  GLN A CD  
85    O  OE1 . GLN A 36  ? 1.2941 1.0584 2.0280 -0.1641 -0.2250 0.2655  37  GLN A OE1 
86    N  NE2 . GLN A 36  ? 1.2344 1.0132 1.9710 -0.1415 -0.2097 0.2426  37  GLN A NE2 
87    N  N   . ILE A 37  ? 0.9434 0.7716 1.5481 -0.1944 -0.1651 0.2578  38  ILE A N   
88    C  CA  . ILE A 37  ? 0.8756 0.7166 1.4715 -0.1847 -0.1512 0.2440  38  ILE A CA  
89    C  C   . ILE A 37  ? 0.8642 0.7238 1.4278 -0.2012 -0.1439 0.2545  38  ILE A C   
90    O  O   . ILE A 37  ? 0.8515 0.7189 1.4085 -0.1983 -0.1427 0.2565  38  ILE A O   
91    C  CB  . ILE A 37  ? 0.8092 0.6532 1.4085 -0.1734 -0.1349 0.2189  38  ILE A CB  
92    C  CG1 . ILE A 37  ? 0.8010 0.6294 1.4316 -0.1558 -0.1401 0.2052  38  ILE A CG1 
93    C  CG2 . ILE A 37  ? 0.8126 0.6720 1.3992 -0.1667 -0.1203 0.2068  38  ILE A CG2 
94    C  CD1 . ILE A 37  ? 0.7711 0.6019 1.4044 -0.1462 -0.1260 0.1813  38  ILE A CD1 
95    N  N   . TYR A 38  ? 0.8589 0.7267 1.4031 -0.2193 -0.1387 0.2604  39  TYR A N   
96    C  CA  . TYR A 38  ? 0.8872 0.7757 1.4007 -0.2375 -0.1301 0.2686  39  TYR A CA  
97    C  C   . TYR A 38  ? 0.9781 0.8666 1.4823 -0.2489 -0.1451 0.2921  39  TYR A C   
98    O  O   . TYR A 38  ? 1.0009 0.9060 1.4831 -0.2584 -0.1392 0.2966  39  TYR A O   
99    C  CB  . TYR A 38  ? 0.8202 0.7179 1.3188 -0.2548 -0.1218 0.2690  39  TYR A CB  
100   C  CG  . TYR A 38  ? 0.7890 0.7112 1.2572 -0.2752 -0.1107 0.2746  39  TYR A CG  
101   C  CD1 . TYR A 38  ? 0.7349 0.6776 1.1922 -0.2733 -0.0916 0.2580  39  TYR A CD1 
102   C  CD2 . TYR A 38  ? 0.7810 0.7071 1.2323 -0.2968 -0.1191 0.2954  39  TYR A CD2 
103   C  CE1 . TYR A 38  ? 0.7422 0.7096 1.1742 -0.2918 -0.0799 0.2603  39  TYR A CE1 
104   C  CE2 . TYR A 38  ? 0.7977 0.7484 1.2210 -0.3161 -0.1075 0.2983  39  TYR A CE2 
105   C  CZ  . TYR A 38  ? 0.7938 0.7654 1.2084 -0.3133 -0.0873 0.2798  39  TYR A CZ  
106   O  OH  . TYR A 38  ? 0.8345 0.8324 1.2238 -0.3322 -0.0745 0.2802  39  TYR A OH  
107   N  N   . GLY A 39  ? 1.0811 0.9517 1.6032 -0.2481 -0.1651 0.3067  40  GLY A N   
108   C  CA  . GLY A 39  ? 1.1390 1.0085 1.6556 -0.2589 -0.1831 0.3308  40  GLY A CA  
109   C  C   . GLY A 39  ? 1.1648 1.0315 1.6951 -0.2443 -0.1902 0.3306  40  GLY A C   
110   O  O   . GLY A 39  ? 1.2130 1.0891 1.7271 -0.2541 -0.1960 0.3447  40  GLY A O   
111   N  N   . ALA A 40  ? 1.1295 0.9844 1.6893 -0.2215 -0.1895 0.3139  41  ALA A N   
112   C  CA  . ALA A 40  ? 1.0776 0.9305 1.6543 -0.2058 -0.1948 0.3105  41  ALA A CA  
113   C  C   . ALA A 40  ? 1.0259 0.8955 1.5816 -0.2041 -0.1775 0.2997  41  ALA A C   
114   O  O   . ALA A 40  ? 1.0504 0.9215 1.6142 -0.1936 -0.1798 0.2974  41  ALA A O   
115   C  CB  . ALA A 40  ? 1.0582 0.8969 1.6718 -0.1832 -0.1962 0.2927  41  ALA A CB  
116   N  N   . LYS A 41  ? 0.9849 0.8680 1.5152 -0.2146 -0.1602 0.2924  42  LYS A N   
117   C  CA  . LYS A 41  ? 0.8925 0.7937 1.4034 -0.2147 -0.1428 0.2812  42  LYS A CA  
118   C  C   . LYS A 41  ? 0.9168 0.8353 1.3956 -0.2374 -0.1422 0.2972  42  LYS A C   
119   O  O   . LYS A 41  ? 0.9378 0.8751 1.3969 -0.2425 -0.1259 0.2881  42  LYS A O   
120   C  CB  . LYS A 41  ? 0.8674 0.7759 1.3747 -0.2107 -0.1231 0.2599  42  LYS A CB  
121   C  CG  . LYS A 41  ? 0.8169 0.7140 1.3504 -0.1871 -0.1194 0.2397  42  LYS A CG  
122   C  CD  . LYS A 41  ? 0.8066 0.7120 1.3357 -0.1846 -0.1020 0.2205  42  LYS A CD  
123   C  CE  . LYS A 41  ? 0.7855 0.6858 1.3336 -0.1623 -0.0954 0.1993  42  LYS A CE  
124   N  NZ  . LYS A 41  ? 0.7825 0.6914 1.3273 -0.1543 -0.0902 0.1947  42  LYS A NZ  
125   N  N   . GLY A 42  ? 0.9488 0.8623 1.4231 -0.2515 -0.1601 0.3203  43  GLY A N   
126   C  CA  . GLY A 42  ? 0.9395 0.8695 1.3831 -0.2737 -0.1624 0.3371  43  GLY A CA  
127   C  C   . GLY A 42  ? 0.9332 0.8799 1.3485 -0.2955 -0.1499 0.3379  43  GLY A C   
128   O  O   . GLY A 42  ? 0.9355 0.9031 1.3223 -0.3121 -0.1419 0.3413  43  GLY A O   
129   N  N   . PHE A 43  ? 0.9397 0.8787 1.3638 -0.2959 -0.1479 0.3338  44  PHE A N   
130   C  CA  . PHE A 43  ? 0.9643 0.9190 1.3654 -0.3166 -0.1366 0.3343  44  PHE A CA  
131   C  C   . PHE A 43  ? 0.9927 0.9347 1.3969 -0.3286 -0.1538 0.3536  44  PHE A C   
132   O  O   . PHE A 43  ? 1.0167 0.9363 1.4467 -0.3171 -0.1714 0.3610  44  PHE A O   
133   C  CB  . PHE A 43  ? 0.9103 0.8722 1.3169 -0.3084 -0.1152 0.3094  44  PHE A CB  
134   C  CG  . PHE A 43  ? 0.8570 0.8322 1.2624 -0.2967 -0.0986 0.2899  44  PHE A CG  
135   C  CD1 . PHE A 43  ? 0.8698 0.8698 1.2503 -0.3098 -0.0861 0.2878  44  PHE A CD1 
136   C  CD2 . PHE A 43  ? 0.8174 0.7813 1.2465 -0.2730 -0.0951 0.2730  44  PHE A CD2 
137   C  CE1 . PHE A 43  ? 0.8586 0.8710 1.2399 -0.2990 -0.0712 0.2696  44  PHE A CE1 
138   C  CE2 . PHE A 43  ? 0.8286 0.8048 1.2571 -0.2626 -0.0807 0.2559  44  PHE A CE2 
139   C  CZ  . PHE A 43  ? 0.8106 0.8107 1.2160 -0.2754 -0.0690 0.2544  44  PHE A CZ  
140   N  N   . SER A 44  ? 1.0657 1.0232 1.4451 -0.3519 -0.1483 0.3610  45  SER A N   
141   C  CA  . SER A 44  ? 1.1009 1.0488 1.4794 -0.3666 -0.1645 0.3811  45  SER A CA  
142   C  C   . SER A 44  ? 1.0736 1.0018 1.4792 -0.3547 -0.1670 0.3737  45  SER A C   
143   O  O   . SER A 44  ? 1.0704 1.0039 1.4796 -0.3488 -0.1491 0.3535  45  SER A O   
144   C  CB  . SER A 44  ? 1.1629 1.1346 1.5083 -0.3941 -0.1545 0.3868  45  SER A CB  
145   O  OG  . SER A 44  ? 1.2025 1.1904 1.5215 -0.4091 -0.1582 0.3992  45  SER A OG  
146   N  N   . LEU A 45  ? 1.0437 0.9501 1.4695 -0.3514 -0.1899 0.3898  46  LEU A N   
147   C  CA  . LEU A 45  ? 1.0342 0.9214 1.4854 -0.3423 -0.1943 0.3845  46  LEU A CA  
148   C  C   . LEU A 45  ? 1.0318 0.9273 1.4666 -0.3629 -0.1882 0.3889  46  LEU A C   
149   O  O   . LEU A 45  ? 1.0499 0.9364 1.4991 -0.3579 -0.1837 0.3787  46  LEU A O   
150   C  CB  . LEU A 45  ? 1.0018 0.8653 1.4815 -0.3343 -0.2209 0.4004  46  LEU A CB  
151   C  CG  . LEU A 45  ? 0.9634 0.8133 1.4738 -0.3082 -0.2270 0.3903  46  LEU A CG  
152   C  CD1 . LEU A 45  ? 0.9247 0.7860 1.4231 -0.3075 -0.2283 0.3953  46  LEU A CD1 
153   C  CD2 . LEU A 45  ? 0.8780 0.7051 1.4230 -0.3006 -0.2507 0.4014  46  LEU A CD2 
154   N  N   . SER A 46  ? 1.0808 0.9946 1.4850 -0.3868 -0.1878 0.4036  47  SER A N   
155   C  CA  . SER A 46  ? 1.1082 1.0333 1.4943 -0.4088 -0.1816 0.4088  47  SER A CA  
156   C  C   . SER A 46  ? 1.0603 1.0027 1.4408 -0.4074 -0.1541 0.3835  47  SER A C   
157   O  O   . SER A 46  ? 1.0669 1.0132 1.4453 -0.4179 -0.1477 0.3811  47  SER A O   
158   C  CB  . SER A 46  ? 1.1444 1.0882 1.4975 -0.4350 -0.1870 0.4289  47  SER A CB  
159   O  OG  . SER A 46  ? 1.1355 1.1016 1.4679 -0.4365 -0.1713 0.4187  47  SER A OG  
160   N  N   . ASP A 47  ? 1.0455 0.9987 1.4251 -0.3944 -0.1386 0.3647  48  ASP A N   
161   C  CA  . ASP A 47  ? 1.0093 0.9810 1.3863 -0.3921 -0.1134 0.3401  48  ASP A CA  
162   C  C   . ASP A 47  ? 0.9924 0.9483 1.3958 -0.3755 -0.1109 0.3249  48  ASP A C   
163   O  O   . ASP A 47  ? 0.9773 0.9467 1.3813 -0.3759 -0.0932 0.3070  48  ASP A O   
164   C  CB  . ASP A 47  ? 1.0521 1.0397 1.4226 -0.3826 -0.0991 0.3250  48  ASP A CB  
165   C  CG  . ASP A 47  ? 1.1016 1.1099 1.4430 -0.4008 -0.0973 0.3359  48  ASP A CG  
166   O  OD1 . ASP A 47  ? 1.1070 1.1313 1.4284 -0.4232 -0.0936 0.3437  48  ASP A OD1 
167   O  OD2 . ASP A 47  ? 1.1257 1.1355 1.4639 -0.3930 -0.0991 0.3356  48  ASP A OD2 
168   N  N   . VAL A 48  ? 0.9257 0.8540 1.3521 -0.3612 -0.1288 0.3312  49  VAL A N   
169   C  CA  . VAL A 48  ? 0.7984 0.7109 1.2498 -0.3449 -0.1276 0.3161  49  VAL A CA  
170   C  C   . VAL A 48  ? 0.9524 0.8572 1.4079 -0.3570 -0.1330 0.3233  49  VAL A C   
171   O  O   . VAL A 48  ? 0.8599 0.7511 1.3179 -0.3657 -0.1513 0.3440  49  VAL A O   
172   C  CB  . VAL A 48  ? 0.7903 0.6781 1.2681 -0.3225 -0.1426 0.3157  49  VAL A CB  
173   C  CG1 . VAL A 48  ? 0.7758 0.6489 1.2778 -0.3073 -0.1406 0.2989  49  VAL A CG1 
174   C  CG2 . VAL A 48  ? 0.7791 0.6741 1.2548 -0.3095 -0.1369 0.3075  49  VAL A CG2 
175   N  N   . PRO A 49  ? 0.9000 0.8139 1.3572 -0.3580 -0.1177 0.3066  50  PRO A N   
176   C  CA  . PRO A 49  ? 0.8849 0.7912 1.3481 -0.3682 -0.1216 0.3108  50  PRO A CA  
177   C  C   . PRO A 49  ? 0.8872 0.7626 1.3768 -0.3552 -0.1402 0.3155  50  PRO A C   
178   O  O   . PRO A 49  ? 0.8337 0.6965 1.3420 -0.3337 -0.1422 0.3033  50  PRO A O   
179   C  CB  . PRO A 49  ? 0.8773 0.7994 1.3420 -0.3657 -0.1014 0.2875  50  PRO A CB  
180   C  CG  . PRO A 49  ? 0.8469 0.7762 1.3145 -0.3478 -0.0915 0.2703  50  PRO A CG  
181   C  CD  . PRO A 49  ? 0.8443 0.7774 1.2986 -0.3503 -0.0967 0.2831  50  PRO A CD  
182   N  N   . GLN A 50  ? 0.9346 0.7994 1.4262 -0.3688 -0.1532 0.3325  51  GLN A N   
183   C  CA  . GLN A 50  ? 0.9725 0.8088 1.4903 -0.3597 -0.1721 0.3391  51  GLN A CA  
184   C  C   . GLN A 50  ? 0.8770 0.7024 1.4168 -0.3421 -0.1657 0.3162  51  GLN A C   
185   O  O   . GLN A 50  ? 0.8715 0.6777 1.4356 -0.3238 -0.1753 0.3107  51  GLN A O   
186   C  CB  . GLN A 50  ? 1.0547 0.8852 1.5687 -0.3805 -0.1843 0.3598  51  GLN A CB  
187   C  CG  . GLN A 50  ? 1.0761 0.9265 1.5707 -0.4005 -0.1691 0.3569  51  GLN A CG  
188   C  CD  . GLN A 50  ? 1.0775 0.9577 1.5418 -0.4153 -0.1547 0.3588  51  GLN A CD  
189   O  OE1 . GLN A 50  ? 1.0934 0.9779 1.5434 -0.4235 -0.1633 0.3758  51  GLN A OE1 
190   N  NE2 . GLN A 50  ? 1.0387 0.9407 1.4946 -0.4187 -0.1329 0.3404  51  GLN A NE2 
191   N  N   . ALA A 51  ? 0.8642 0.7036 1.3961 -0.3481 -0.1495 0.3022  52  ALA A N   
192   C  CA  . ALA A 51  ? 0.8414 0.6740 1.3904 -0.3332 -0.1426 0.2799  52  ALA A CA  
193   C  C   . ALA A 51  ? 0.8063 0.6632 1.3429 -0.3311 -0.1216 0.2607  52  ALA A C   
194   O  O   . ALA A 51  ? 0.8004 0.6792 1.3169 -0.3413 -0.1117 0.2639  52  ALA A O   
195   C  CB  . ALA A 51  ? 0.8656 0.6869 1.4245 -0.3421 -0.1478 0.2820  52  ALA A CB  
196   N  N   . GLU A 52  ? 0.7845 0.6383 1.3342 -0.3183 -0.1153 0.2406  53  GLU A N   
197   C  CA  . GLU A 52  ? 0.8189 0.6946 1.3614 -0.3140 -0.0977 0.2217  53  GLU A CA  
198   C  C   . GLU A 52  ? 0.8166 0.7159 1.3440 -0.3343 -0.0857 0.2225  53  GLU A C   
199   O  O   . GLU A 52  ? 0.8663 0.7616 1.3972 -0.3453 -0.0882 0.2257  53  GLU A O   
200   C  CB  . GLU A 52  ? 0.8063 0.6719 1.3665 -0.2973 -0.0964 0.2020  53  GLU A CB  
201   C  CG  . GLU A 52  ? 0.6955 0.5805 1.2522 -0.2884 -0.0817 0.1826  53  GLU A CG  
202   C  CD  . GLU A 52  ? 0.7343 0.6065 1.3081 -0.2698 -0.0833 0.1650  53  GLU A CD  
203   O  OE1 . GLU A 52  ? 0.6911 0.5722 1.2671 -0.2698 -0.0764 0.1515  53  GLU A OE1 
204   O  OE2 . GLU A 52  ? 0.6788 0.5332 1.2642 -0.2557 -0.0916 0.1644  53  GLU A OE2 
205   N  N   . ILE A 53  ? 0.7398 0.6647 1.2520 -0.3391 -0.0721 0.2185  54  ILE A N   
206   C  CA  . ILE A 53  ? 0.7461 0.6971 1.2456 -0.3587 -0.0591 0.2179  54  ILE A CA  
207   C  C   . ILE A 53  ? 0.7535 0.7279 1.2554 -0.3533 -0.0426 0.1961  54  ILE A C   
208   O  O   . ILE A 53  ? 0.7353 0.7050 1.2469 -0.3348 -0.0422 0.1828  54  ILE A O   
209   C  CB  . ILE A 53  ? 0.7599 0.7262 1.2394 -0.3733 -0.0557 0.2316  54  ILE A CB  
210   C  CG1 . ILE A 53  ? 0.8426 0.8213 1.3163 -0.3620 -0.0475 0.2229  54  ILE A CG1 
211   C  CG2 . ILE A 53  ? 0.7951 0.7398 1.2716 -0.3798 -0.0742 0.2555  54  ILE A CG2 
212   C  CD1 . ILE A 53  ? 0.8250 0.8238 1.2782 -0.3770 -0.0408 0.2323  54  ILE A CD1 
213   N  N   . SER A 54  ? 0.7437 0.7445 1.2381 -0.3696 -0.0293 0.1925  55  SER A N   
214   C  CA  . SER A 54  ? 0.7081 0.7344 1.2072 -0.3662 -0.0142 0.1724  55  SER A CA  
215   C  C   . SER A 54  ? 0.7082 0.7521 1.2007 -0.3585 -0.0044 0.1646  55  SER A C   
216   O  O   . SER A 54  ? 0.7236 0.7715 1.2031 -0.3652 -0.0032 0.1746  55  SER A O   
217   C  CB  . SER A 54  ? 0.7244 0.7742 1.2217 -0.3862 -0.0028 0.1701  55  SER A CB  
218   O  OG  . SER A 54  ? 0.7378 0.8070 1.2457 -0.3815 0.0072  0.1509  55  SER A OG  
219   N  N   . GLY A 55  ? 0.7187 0.7734 1.2201 -0.3448 0.0019  0.1472  56  GLY A N   
220   C  CA  . GLY A 55  ? 0.7194 0.7864 1.2177 -0.3335 0.0087  0.1391  56  GLY A CA  
221   C  C   . GLY A 55  ? 0.7325 0.8359 1.2283 -0.3408 0.0263  0.1262  56  GLY A C   
222   O  O   . GLY A 55  ? 0.7470 0.8619 1.2454 -0.3282 0.0314  0.1154  56  GLY A O   
223   N  N   . GLU A 56  ? 0.7728 0.8948 1.2659 -0.3603 0.0356  0.1264  57  GLU A N   
224   C  CA  . GLU A 56  ? 0.7723 0.9309 1.2671 -0.3681 0.0539  0.1116  57  GLU A CA  
225   C  C   . GLU A 56  ? 0.6840 0.8559 1.1707 -0.3645 0.0625  0.1076  57  GLU A C   
226   O  O   . GLU A 56  ? 0.6365 0.8331 1.1278 -0.3593 0.0725  0.0920  57  GLU A O   
227   C  CB  . GLU A 56  ? 0.8377 1.0113 1.3329 -0.3901 0.0638  0.1144  57  GLU A CB  
228   C  CG  . GLU A 56  ? 0.9185 1.0862 1.3995 -0.4028 0.0627  0.1323  57  GLU A CG  
229   C  CD  . GLU A 56  ? 0.9839 1.1821 1.4681 -0.4182 0.0800  0.1290  57  GLU A CD  
230   O  OE1 . GLU A 56  ? 1.0134 1.2240 1.5090 -0.4287 0.0860  0.1263  57  GLU A OE1 
231   O  OE2 . GLU A 56  ? 0.9769 1.1874 1.4540 -0.4187 0.0870  0.1299  57  GLU A OE2 
232   N  N   . HIS A 57  ? 0.7332 0.8891 1.2071 -0.3672 0.0565  0.1229  58  HIS A N   
233   C  CA  . HIS A 57  ? 0.7787 0.9487 1.2433 -0.3691 0.0657  0.1217  58  HIS A CA  
234   C  C   . HIS A 57  ? 0.7472 0.9144 1.2121 -0.3501 0.0634  0.1141  58  HIS A C   
235   O  O   . HIS A 57  ? 0.6984 0.8823 1.1583 -0.3503 0.0737  0.1077  58  HIS A O   
236   C  CB  . HIS A 57  ? 0.8129 0.9674 1.2609 -0.3801 0.0566  0.1443  58  HIS A CB  
237   C  CG  . HIS A 57  ? 0.8710 0.9899 1.3164 -0.3702 0.0356  0.1596  58  HIS A CG  
238   N  ND1 . HIS A 57  ? 0.9041 1.0023 1.3574 -0.3693 0.0239  0.1658  58  HIS A ND1 
239   C  CD2 . HIS A 57  ? 0.8997 1.0003 1.3391 -0.3596 0.0247  0.1687  58  HIS A CD2 
240   C  CE1 . HIS A 57  ? 0.9233 0.9920 1.3773 -0.3580 0.0071  0.1772  58  HIS A CE1 
241   N  NE2 . HIS A 57  ? 0.9010 0.9707 1.3471 -0.3518 0.0072  0.1794  58  HIS A NE2 
242   N  N   . LEU A 58  ? 0.7930 0.9387 1.2661 -0.3328 0.0503  0.1147  59  LEU A N   
243   C  CA  . LEU A 58  ? 0.8383 0.9758 1.3144 -0.3124 0.0459  0.1106  59  LEU A CA  
244   C  C   . LEU A 58  ? 0.8403 1.0073 1.3214 -0.3063 0.0585  0.0933  59  LEU A C   
245   O  O   . LEU A 58  ? 0.8823 1.0648 1.3749 -0.3037 0.0621  0.0828  59  LEU A O   
246   C  CB  . LEU A 58  ? 0.7849 0.8953 1.2742 -0.2944 0.0323  0.1111  59  LEU A CB  
247   C  CG  . LEU A 58  ? 0.7608 0.8425 1.2502 -0.2986 0.0185  0.1256  59  LEU A CG  
248   C  CD1 . LEU A 58  ? 0.7416 0.8028 1.2466 -0.2814 0.0089  0.1200  59  LEU A CD1 
249   C  CD2 . LEU A 58  ? 0.7602 0.8242 1.2390 -0.3001 0.0098  0.1416  59  LEU A CD2 
250   N  N   . ARG A 59  ? 0.8567 1.0318 1.3299 -0.3036 0.0637  0.0917  60  ARG A N   
251   C  CA  . ARG A 59  ? 0.8353 1.0360 1.3139 -0.2946 0.0729  0.0771  60  ARG A CA  
252   C  C   . ARG A 59  ? 0.7555 0.9404 1.2481 -0.2675 0.0657  0.0714  60  ARG A C   
253   O  O   . ARG A 59  ? 0.7448 0.9441 1.2502 -0.2554 0.0701  0.0588  60  ARG A O   
254   C  CB  . ARG A 59  ? 0.9777 1.1950 1.4416 -0.3045 0.0828  0.0763  60  ARG A CB  
255   C  CG  . ARG A 59  ? 1.0865 1.3215 1.5417 -0.3303 0.0970  0.0746  60  ARG A CG  
256   C  CD  . ARG A 59  ? 1.1379 1.4092 1.5941 -0.3351 0.1041  0.0637  60  ARG A CD  
257   N  NE  . ARG A 59  ? 1.1507 1.4523 1.6172 -0.3220 0.1007  0.0692  60  ARG A NE  
258   C  CZ  . ARG A 59  ? 1.1362 1.4656 1.6326 -0.3145 0.1067  0.0656  60  ARG A CZ  
259   N  NH1 . ARG A 59  ? 1.1491 1.4882 1.6573 -0.3210 0.1069  0.0668  60  ARG A NH1 
260   N  NH2 . ARG A 59  ? 1.1309 1.4716 1.6367 -0.2988 0.1163  0.0514  60  ARG A NH2 
261   N  N   . ILE A 60  ? 0.6466 0.8016 1.1378 -0.2578 0.0548  0.0803  61  ILE A N   
262   C  CA  . ILE A 60  ? 0.5350 0.6746 1.0371 -0.2339 0.0496  0.0739  61  ILE A CA  
263   C  C   . ILE A 60  ? 0.4905 0.6062 1.0041 -0.2240 0.0389  0.0745  61  ILE A C   
264   O  O   . ILE A 60  ? 0.4899 0.6085 1.0159 -0.2123 0.0396  0.0635  61  ILE A O   
265   C  CB  . ILE A 60  ? 0.5200 0.6457 1.0141 -0.2278 0.0458  0.0808  61  ILE A CB  
266   C  CG1 . ILE A 60  ? 0.4903 0.6400 0.9719 -0.2384 0.0567  0.0793  61  ILE A CG1 
267   C  CG2 . ILE A 60  ? 0.4554 0.5670 0.9607 -0.2041 0.0421  0.0726  61  ILE A CG2 
268   C  CD1 . ILE A 60  ? 0.4262 0.5634 0.8954 -0.2414 0.0519  0.0912  61  ILE A CD1 
269   N  N   . CYS A 61  ? 0.4975 0.5896 1.0070 -0.2285 0.0287  0.0872  62  CYS A N   
270   C  CA  . CYS A 61  ? 0.5172 0.5862 1.0373 -0.2205 0.0184  0.0873  62  CYS A CA  
271   C  C   . CYS A 61  ? 0.5302 0.6104 1.0575 -0.2267 0.0209  0.0811  62  CYS A C   
272   O  O   . CYS A 61  ? 0.4545 0.5538 0.9763 -0.2434 0.0274  0.0831  62  CYS A O   
273   C  CB  . CYS A 61  ? 0.4647 0.5093 0.9801 -0.2270 0.0071  0.1027  62  CYS A CB  
274   S  SG  . CYS A 61  ? 0.9361 0.9656 1.4457 -0.2190 0.0012  0.1117  62  CYS A SG  
275   N  N   . PRO A 62  ? 0.5117 0.5812 1.0513 -0.2142 0.0161  0.0728  63  PRO A N   
276   C  CA  . PRO A 62  ? 0.5444 0.6229 1.0921 -0.2192 0.0169  0.0670  63  PRO A CA  
277   C  C   . PRO A 62  ? 0.6031 0.6784 1.1458 -0.2380 0.0140  0.0775  63  PRO A C   
278   O  O   . PRO A 62  ? 0.6383 0.6906 1.1774 -0.2405 0.0053  0.0878  63  PRO A O   
279   C  CB  . PRO A 62  ? 0.4731 0.5323 1.0312 -0.2041 0.0092  0.0597  63  PRO A CB  
280   C  CG  . PRO A 62  ? 0.4113 0.4625 0.9685 -0.1887 0.0092  0.0564  63  PRO A CG  
281   C  CD  . PRO A 62  ? 0.4203 0.4698 0.9663 -0.1957 0.0101  0.0678  63  PRO A CD  
282   N  N   . GLN A 63  ? 0.6836 0.7818 1.2269 -0.2511 0.0209  0.0750  64  GLN A N   
283   C  CA  . GLN A 63  ? 0.7667 0.8649 1.3034 -0.2713 0.0201  0.0848  64  GLN A CA  
284   C  C   . GLN A 63  ? 0.7870 0.8624 1.3311 -0.2707 0.0095  0.0874  64  GLN A C   
285   O  O   . GLN A 63  ? 0.8301 0.9073 1.3855 -0.2641 0.0080  0.0780  64  GLN A O   
286   C  CB  . GLN A 63  ? 0.8442 0.9757 1.3808 -0.2858 0.0317  0.0794  64  GLN A CB  
287   C  CG  . GLN A 63  ? 0.9087 1.0606 1.4326 -0.2963 0.0423  0.0811  64  GLN A CG  
288   C  CD  . GLN A 63  ? 0.9347 1.1240 1.4631 -0.3029 0.0548  0.0700  64  GLN A CD  
289   O  OE1 . GLN A 63  ? 0.9762 1.1765 1.5180 -0.3004 0.0549  0.0626  64  GLN A OE1 
290   N  NE2 . GLN A 63  ? 0.9269 1.1368 1.4450 -0.3113 0.0649  0.0688  64  GLN A NE2 
291   N  N   . GLY A 64  ? 0.7577 0.8116 1.2957 -0.2780 0.0016  0.1004  65  GLY A N   
292   C  CA  . GLY A 64  ? 0.7324 0.7614 1.2774 -0.2771 -0.0094 0.1038  65  GLY A CA  
293   C  C   . GLY A 64  ? 0.7314 0.7413 1.2685 -0.2857 -0.0171 0.1205  65  GLY A C   
294   O  O   . GLY A 64  ? 0.7044 0.7213 1.2302 -0.2915 -0.0137 0.1284  65  GLY A O   
295   N  N   . TYR A 65  ? 0.6967 0.6826 1.2402 -0.2865 -0.0280 0.1259  66  TYR A N   
296   C  CA  . TYR A 65  ? 0.7253 0.6930 1.2639 -0.2949 -0.0372 0.1433  66  TYR A CA  
297   C  C   . TYR A 65  ? 0.6178 0.5718 1.1550 -0.2825 -0.0430 0.1486  66  TYR A C   
298   O  O   . TYR A 65  ? 0.6023 0.5434 1.1497 -0.2645 -0.0469 0.1397  66  TYR A O   
299   C  CB  . TYR A 65  ? 0.6461 0.5910 1.1953 -0.2969 -0.0481 0.1463  66  TYR A CB  
300   C  CG  . TYR A 65  ? 0.6597 0.6178 1.2077 -0.3140 -0.0434 0.1460  66  TYR A CG  
301   C  CD1 . TYR A 65  ? 0.6814 0.6507 1.2182 -0.3340 -0.0399 0.1587  66  TYR A CD1 
302   C  CD2 . TYR A 65  ? 0.6749 0.6360 1.2330 -0.3107 -0.0418 0.1328  66  TYR A CD2 
303   C  CE1 . TYR A 65  ? 0.6941 0.6769 1.2310 -0.3499 -0.0345 0.1575  66  TYR A CE1 
304   C  CE2 . TYR A 65  ? 0.7015 0.6760 1.2598 -0.3265 -0.0375 0.1323  66  TYR A CE2 
305   C  CZ  . TYR A 65  ? 0.6845 0.6699 1.2327 -0.3459 -0.0334 0.1443  66  TYR A CZ  
306   O  OH  . TYR A 65  ? 0.8696 0.8694 1.4192 -0.3619 -0.0282 0.1429  66  TYR A OH  
307   N  N   . THR A 66  ? 0.6315 0.5895 1.1561 -0.2930 -0.0434 0.1628  67  THR A N   
308   C  CA  . THR A 66  ? 0.6986 0.6506 1.2195 -0.2833 -0.0468 0.1679  67  THR A CA  
309   C  C   . THR A 66  ? 0.7253 0.6631 1.2402 -0.2926 -0.0585 0.1889  67  THR A C   
310   O  O   . THR A 66  ? 0.6806 0.6206 1.1882 -0.3105 -0.0606 0.2008  67  THR A O   
311   C  CB  . THR A 66  ? 0.7169 0.6961 1.2260 -0.2849 -0.0328 0.1614  67  THR A CB  
312   O  OG1 . THR A 66  ? 0.7757 0.7489 1.2801 -0.2776 -0.0367 0.1680  67  THR A OG1 
313   C  CG2 . THR A 66  ? 0.6174 0.6196 1.1125 -0.3074 -0.0234 0.1670  67  THR A CG2 
314   N  N   . CYS A 67  ? 0.7241 0.6479 1.2429 -0.2802 -0.0667 0.1935  68  CYS A N   
315   C  CA  . CYS A 67  ? 0.6766 0.5893 1.1903 -0.2875 -0.0791 0.2142  68  CYS A CA  
316   C  C   . CYS A 67  ? 0.6774 0.6091 1.1718 -0.2954 -0.0723 0.2205  68  CYS A C   
317   O  O   . CYS A 67  ? 0.7073 0.6329 1.1947 -0.3017 -0.0824 0.2379  68  CYS A O   
318   C  CB  . CYS A 67  ? 0.6782 0.5649 1.2106 -0.2698 -0.0935 0.2159  68  CYS A CB  
319   S  SG  . CYS A 67  ? 1.2621 1.1237 1.8171 -0.2654 -0.1052 0.2140  68  CYS A SG  
320   N  N   . CYS A 68  ? 0.6743 0.6296 1.1613 -0.2948 -0.0558 0.2060  69  CYS A N   
321   C  CA  . CYS A 68  ? 0.6701 0.6452 1.1403 -0.3009 -0.0473 0.2081  69  CYS A CA  
322   C  C   . CYS A 68  ? 0.7575 0.7588 1.2110 -0.3231 -0.0347 0.2095  69  CYS A C   
323   O  O   . CYS A 68  ? 0.7612 0.7753 1.2184 -0.3279 -0.0248 0.1984  69  CYS A O   
324   C  CB  . CYS A 68  ? 0.6063 0.5910 1.0817 -0.2838 -0.0373 0.1900  69  CYS A CB  
325   S  SG  . CYS A 68  ? 0.8816 0.8412 1.3729 -0.2591 -0.0493 0.1885  69  CYS A SG  
326   N  N   . THR A 69  ? 0.7961 0.8066 1.2319 -0.3365 -0.0350 0.2227  70  THR A N   
327   C  CA  . THR A 69  ? 0.8462 0.8852 1.2657 -0.3567 -0.0205 0.2215  70  THR A CA  
328   C  C   . THR A 69  ? 0.8223 0.8852 1.2365 -0.3523 -0.0045 0.2065  70  THR A C   
329   O  O   . THR A 69  ? 0.8379 0.8938 1.2599 -0.3343 -0.0060 0.1988  70  THR A O   
330   C  CB  . THR A 69  ? 0.8152 0.8530 1.2163 -0.3765 -0.0300 0.2448  70  THR A CB  
331   O  OG1 . THR A 69  ? 0.7208 0.7527 1.1130 -0.3723 -0.0385 0.2551  70  THR A OG1 
332   C  CG2 . THR A 69  ? 0.8054 0.8187 1.2139 -0.3804 -0.0473 0.2605  70  THR A CG2 
333   N  N   . SER A 70  ? 0.8683 0.9597 1.2709 -0.3683 0.0109  0.2016  71  SER A N   
334   C  CA  . SER A 70  ? 0.8940 1.0103 1.2934 -0.3653 0.0273  0.1860  71  SER A CA  
335   C  C   . SER A 70  ? 0.8341 0.9431 1.2222 -0.3604 0.0198  0.1954  71  SER A C   
336   O  O   . SER A 70  ? 0.8143 0.9255 1.2086 -0.3453 0.0242  0.1836  71  SER A O   
337   C  CB  . SER A 70  ? 1.0192 1.1669 1.4104 -0.3841 0.0442  0.1808  71  SER A CB  
338   O  OG  . SER A 70  ? 1.0717 1.2440 1.4660 -0.3792 0.0612  0.1628  71  SER A OG  
339   N  N   . GLU A 71  ? 0.8101 0.9107 1.1816 -0.3735 0.0074  0.2173  72  GLU A N   
340   C  CA  . GLU A 71  ? 0.8489 0.9416 1.2091 -0.3707 -0.0027 0.2293  72  GLU A CA  
341   C  C   . GLU A 71  ? 0.8251 0.8913 1.2031 -0.3475 -0.0152 0.2287  72  GLU A C   
342   O  O   . GLU A 71  ? 0.8177 0.8841 1.1955 -0.3367 -0.0147 0.2249  72  GLU A O   
343   C  CB  . GLU A 71  ? 0.8577 0.9433 1.1989 -0.3891 -0.0180 0.2553  72  GLU A CB  
344   C  CG  . GLU A 71  ? 0.9017 1.0154 1.2208 -0.4132 -0.0065 0.2573  72  GLU A CG  
345   C  CD  . GLU A 71  ? 0.9744 1.0797 1.2763 -0.4327 -0.0235 0.2836  72  GLU A CD  
346   O  OE1 . GLU A 71  ? 0.9960 1.0774 1.2985 -0.4286 -0.0448 0.3024  72  GLU A OE1 
347   O  OE2 . GLU A 71  ? 0.9877 1.1109 1.2769 -0.4520 -0.0160 0.2855  72  GLU A OE2 
348   N  N   . MET A 72  ? 0.8152 0.8593 1.2092 -0.3397 -0.0259 0.2317  73  MET A N   
349   C  CA  . MET A 72  ? 0.7508 0.7701 1.1645 -0.3169 -0.0370 0.2290  73  MET A CA  
350   C  C   . MET A 72  ? 0.6547 0.6834 1.0792 -0.2998 -0.0239 0.2064  73  MET A C   
351   O  O   . MET A 72  ? 0.6312 0.6519 1.0620 -0.2842 -0.0275 0.2034  73  MET A O   
352   C  CB  . MET A 72  ? 0.7661 0.7629 1.1956 -0.3130 -0.0486 0.2334  73  MET A CB  
353   C  CG  . MET A 72  ? 0.8354 0.8169 1.2599 -0.3256 -0.0662 0.2573  73  MET A CG  
354   S  SD  . MET A 72  ? 0.7232 0.6779 1.1700 -0.3192 -0.0793 0.2599  73  MET A SD  
355   C  CE  . MET A 72  ? 0.6709 0.6055 1.1428 -0.2892 -0.0848 0.2467  73  MET A CE  
356   N  N   . GLU A 73  ? 0.5841 0.6305 1.0115 -0.3027 -0.0095 0.1908  74  GLU A N   
357   C  CA  . GLU A 73  ? 0.6255 0.6826 1.0639 -0.2872 0.0017  0.1699  74  GLU A CA  
358   C  C   . GLU A 73  ? 0.6066 0.6807 1.0361 -0.2854 0.0109  0.1642  74  GLU A C   
359   O  O   . GLU A 73  ? 0.6714 0.7404 1.1098 -0.2674 0.0105  0.1560  74  GLU A O   
360   C  CB  . GLU A 73  ? 0.5421 0.6188 0.9848 -0.2936 0.0146  0.1559  74  GLU A CB  
361   C  CG  . GLU A 73  ? 0.5107 0.5887 0.9703 -0.2745 0.0185  0.1380  74  GLU A CG  
362   C  CD  . GLU A 73  ? 0.5026 0.6064 0.9659 -0.2813 0.0319  0.1237  74  GLU A CD  
363   O  OE1 . GLU A 73  ? 0.6275 0.7541 1.0804 -0.2992 0.0431  0.1228  74  GLU A OE1 
364   O  OE2 . GLU A 73  ? 0.4854 0.5872 0.9630 -0.2686 0.0314  0.1129  74  GLU A OE2 
365   N  N   . GLU A 74  ? 0.6163 0.7107 1.0284 -0.3042 0.0194  0.1681  75  GLU A N   
366   C  CA  . GLU A 74  ? 0.6314 0.7436 1.0338 -0.3050 0.0289  0.1626  75  GLU A CA  
367   C  C   . GLU A 74  ? 0.6209 0.7139 1.0208 -0.2953 0.0151  0.1747  75  GLU A C   
368   O  O   . GLU A 74  ? 0.6146 0.7106 1.0194 -0.2819 0.0189  0.1653  75  GLU A O   
369   C  CB  . GLU A 74  ? 0.7213 0.8571 1.1054 -0.3279 0.0393  0.1661  75  GLU A CB  
370   C  CG  . GLU A 74  ? 0.7819 0.9433 1.1728 -0.3356 0.0577  0.1489  75  GLU A CG  
371   C  CD  . GLU A 74  ? 0.8916 1.0757 1.2671 -0.3566 0.0674  0.1532  75  GLU A CD  
372   O  OE1 . GLU A 74  ? 0.9485 1.1258 1.3032 -0.3684 0.0567  0.1728  75  GLU A OE1 
373   O  OE2 . GLU A 74  ? 0.8845 1.0940 1.2696 -0.3606 0.0845  0.1378  75  GLU A OE2 
374   N  N   . ASN A 75  ? 0.6266 0.7004 1.0207 -0.3019 -0.0015 0.1957  76  ASN A N   
375   C  CA  . ASN A 75  ? 0.6313 0.6863 1.0259 -0.2933 -0.0168 0.2088  76  ASN A CA  
376   C  C   . ASN A 75  ? 0.6474 0.6846 1.0645 -0.2678 -0.0213 0.1989  76  ASN A C   
377   O  O   . ASN A 75  ? 0.6224 0.6580 1.0417 -0.2570 -0.0222 0.1965  76  ASN A O   
378   C  CB  . ASN A 75  ? 0.6638 0.6998 1.0540 -0.3031 -0.0359 0.2325  76  ASN A CB  
379   C  CG  . ASN A 75  ? 0.7199 0.7720 1.0839 -0.3274 -0.0357 0.2468  76  ASN A CG  
380   O  OD1 . ASN A 75  ? 0.7809 0.8532 1.1295 -0.3341 -0.0256 0.2424  76  ASN A OD1 
381   N  ND2 . ASN A 75  ? 0.7313 0.7746 1.0897 -0.3410 -0.0473 0.2640  76  ASN A ND2 
382   N  N   . LEU A 76  ? 0.6398 0.6642 1.0731 -0.2586 -0.0238 0.1927  77  LEU A N   
383   C  CA  . LEU A 76  ? 0.6191 0.6273 1.0734 -0.2350 -0.0272 0.1817  77  LEU A CA  
384   C  C   . LEU A 76  ? 0.5664 0.5916 1.0235 -0.2241 -0.0124 0.1624  77  LEU A C   
385   O  O   . LEU A 76  ? 0.5486 0.5650 1.0167 -0.2062 -0.0142 0.1555  77  LEU A O   
386   C  CB  . LEU A 76  ? 0.5706 0.5642 1.0395 -0.2300 -0.0320 0.1781  77  LEU A CB  
387   C  CG  . LEU A 76  ? 0.5886 0.5597 1.0624 -0.2346 -0.0493 0.1955  77  LEU A CG  
388   C  CD1 . LEU A 76  ? 0.5495 0.5095 1.0366 -0.2315 -0.0516 0.1896  77  LEU A CD1 
389   C  CD2 . LEU A 76  ? 0.5456 0.4975 1.0316 -0.2203 -0.0626 0.2017  77  LEU A CD2 
390   N  N   . ALA A 77  ? 0.5774 0.6277 1.0259 -0.2347 0.0022  0.1530  78  ALA A N   
391   C  CA  . ALA A 77  ? 0.5456 0.6147 0.9971 -0.2254 0.0159  0.1351  78  ALA A CA  
392   C  C   . ALA A 77  ? 0.5941 0.6682 1.0378 -0.2232 0.0173  0.1372  78  ALA A C   
393   O  O   . ALA A 77  ? 0.5520 0.6217 1.0055 -0.2054 0.0183  0.1281  78  ALA A O   
394   C  CB  . ALA A 77  ? 0.5734 0.6705 1.0186 -0.2390 0.0307  0.1252  78  ALA A CB  
395   N  N   . ASN A 78  ? 0.6035 0.6871 1.0290 -0.2417 0.0173  0.1491  79  ASN A N   
396   C  CA  . ASN A 78  ? 0.5919 0.6797 1.0075 -0.2427 0.0166  0.1539  79  ASN A CA  
397   C  C   . ASN A 78  ? 0.6319 0.6945 1.0598 -0.2250 0.0025  0.1604  79  ASN A C   
398   O  O   . ASN A 78  ? 0.6084 0.6731 1.0398 -0.2137 0.0053  0.1538  79  ASN A O   
399   C  CB  . ASN A 78  ? 0.6722 0.7680 1.0654 -0.2660 0.0139  0.1701  79  ASN A CB  
400   C  CG  . ASN A 78  ? 0.6825 0.8103 1.0610 -0.2806 0.0321  0.1593  79  ASN A CG  
401   O  OD1 . ASN A 78  ? 0.6941 0.8390 1.0738 -0.2881 0.0449  0.1479  79  ASN A OD1 
402   N  ND2 . ASN A 78  ? 0.6803 0.8168 1.0463 -0.2845 0.0336  0.1619  79  ASN A ND2 
403   N  N   . ARG A 79  ? 0.6234 0.6625 1.0596 -0.2224 -0.0123 0.1721  80  ARG A N   
404   C  CA  . ARG A 79  ? 0.6494 0.6646 1.1010 -0.2058 -0.0260 0.1772  80  ARG A CA  
405   C  C   . ARG A 79  ? 0.5830 0.5940 1.0520 -0.1835 -0.0198 0.1585  80  ARG A C   
406   O  O   . ARG A 79  ? 0.5547 0.5631 1.0285 -0.1723 -0.0205 0.1555  80  ARG A O   
407   C  CB  . ARG A 79  ? 0.7369 0.7296 1.1980 -0.2064 -0.0414 0.1895  80  ARG A CB  
408   C  CG  . ARG A 79  ? 0.7894 0.7591 1.2698 -0.1895 -0.0554 0.1933  80  ARG A CG  
409   C  CD  . ARG A 79  ? 0.8571 0.8289 1.3302 -0.1921 -0.0620 0.2048  80  ARG A CD  
410   N  NE  . ARG A 79  ? 0.9498 0.9274 1.4033 -0.2139 -0.0694 0.2248  80  ARG A NE  
411   C  CZ  . ARG A 79  ? 1.0421 1.0041 1.5004 -0.2189 -0.0874 0.2431  80  ARG A CZ  
412   N  NH1 . ARG A 79  ? 1.0440 0.9846 1.5282 -0.2029 -0.0988 0.2422  80  ARG A NH1 
413   N  NH2 . ARG A 79  ? 1.0823 1.0514 1.5203 -0.2399 -0.0939 0.2615  80  ARG A NH2 
414   N  N   . SER A 80  ? 0.5625 0.5735 1.0403 -0.1777 -0.0141 0.1462  81  SER A N   
415   C  CA  . SER A 80  ? 0.5162 0.5233 1.0088 -0.1577 -0.0088 0.1287  81  SER A CA  
416   C  C   . SER A 80  ? 0.4553 0.4807 0.9431 -0.1527 0.0034  0.1173  81  SER A C   
417   O  O   . SER A 80  ? 0.4283 0.4476 0.9252 -0.1367 0.0041  0.1089  81  SER A O   
418   C  CB  . SER A 80  ? 0.4349 0.4425 0.9344 -0.1559 -0.0048 0.1187  81  SER A CB  
419   O  OG  . SER A 80  ? 0.4129 0.4420 0.9010 -0.1709 0.0048  0.1173  81  SER A OG  
420   N  N   . HIS A 81  ? 0.4660 0.5146 0.9398 -0.1668 0.0136  0.1162  82  HIS A N   
421   C  CA  . HIS A 81  ? 0.4035 0.4713 0.8727 -0.1634 0.0256  0.1049  82  HIS A CA  
422   C  C   . HIS A 81  ? 0.4368 0.4995 0.9028 -0.1599 0.0209  0.1115  82  HIS A C   
423   O  O   . HIS A 81  ? 0.3948 0.4567 0.8678 -0.1450 0.0245  0.1013  82  HIS A O   
424   C  CB  . HIS A 81  ? 0.4247 0.5194 0.8799 -0.1817 0.0370  0.1026  82  HIS A CB  
425   C  CG  . HIS A 81  ? 0.5465 0.6622 0.9972 -0.1795 0.0494  0.0905  82  HIS A CG  
426   N  ND1 . HIS A 81  ? 0.5610 0.6852 0.9988 -0.1889 0.0506  0.0967  82  HIS A ND1 
427   C  CD2 . HIS A 81  ? 0.5692 0.6984 1.0265 -0.1688 0.0603  0.0725  82  HIS A CD2 
428   C  CE1 . HIS A 81  ? 0.5754 0.7179 1.0127 -0.1841 0.0627  0.0818  82  HIS A CE1 
429   N  NE2 . HIS A 81  ? 0.5740 0.7192 1.0233 -0.1713 0.0683  0.0672  82  HIS A NE2 
430   N  N   . ALA A 82  ? 0.4252 0.4843 0.8803 -0.1742 0.0121  0.1292  83  ALA A N   
431   C  CA  . ALA A 82  ? 0.4631 0.5172 0.9149 -0.1728 0.0052  0.1382  83  ALA A CA  
432   C  C   . ALA A 82  ? 0.4952 0.5272 0.9663 -0.1518 -0.0033 0.1355  83  ALA A C   
433   O  O   . ALA A 82  ? 0.4944 0.5265 0.9685 -0.1429 -0.0026 0.1321  83  ALA A O   
434   C  CB  . ALA A 82  ? 0.4883 0.5388 0.9261 -0.1912 -0.0064 0.1598  83  ALA A CB  
435   N  N   . GLU A 83  ? 0.4590 0.4732 0.9432 -0.1446 -0.0105 0.1356  84  GLU A N   
436   C  CA  . GLU A 83  ? 0.4281 0.4227 0.9317 -0.1256 -0.0174 0.1305  84  GLU A CA  
437   C  C   . GLU A 83  ? 0.4520 0.4523 0.9622 -0.1100 -0.0060 0.1109  84  GLU A C   
438   O  O   . GLU A 83  ? 0.5138 0.5082 1.0322 -0.0979 -0.0074 0.1067  84  GLU A O   
439   C  CB  . GLU A 83  ? 0.4369 0.4145 0.9524 -0.1229 -0.0258 0.1323  84  GLU A CB  
440   C  CG  . GLU A 83  ? 0.4876 0.4540 1.0018 -0.1340 -0.0409 0.1524  84  GLU A CG  
441   C  CD  . GLU A 83  ? 0.5843 0.5384 1.1067 -0.1356 -0.0470 0.1542  84  GLU A CD  
442   O  OE1 . GLU A 83  ? 0.5722 0.5303 1.0962 -0.1330 -0.0382 0.1414  84  GLU A OE1 
443   O  OE2 . GLU A 83  ? 0.5662 0.5069 1.0942 -0.1397 -0.0612 0.1685  84  GLU A OE2 
444   N  N   . LEU A 84  ? 0.3692 0.3815 0.8762 -0.1107 0.0047  0.0993  85  LEU A N   
445   C  CA  . LEU A 84  ? 0.3739 0.3929 0.8852 -0.0972 0.0148  0.0819  85  LEU A CA  
446   C  C   . LEU A 84  ? 0.3826 0.4140 0.8866 -0.0964 0.0208  0.0798  85  LEU A C   
447   O  O   . LEU A 84  ? 0.3466 0.3745 0.8570 -0.0829 0.0230  0.0708  85  LEU A O   
448   C  CB  . LEU A 84  ? 0.3657 0.3978 0.8745 -0.0998 0.0238  0.0718  85  LEU A CB  
449   C  CG  . LEU A 84  ? 0.3923 0.4322 0.9041 -0.0869 0.0330  0.0551  85  LEU A CG  
450   C  CD1 . LEU A 84  ? 0.4088 0.4320 0.9324 -0.0715 0.0288  0.0483  85  LEU A CD1 
451   C  CD2 . LEU A 84  ? 0.4153 0.4677 0.9264 -0.0897 0.0397  0.0468  85  LEU A CD2 
452   N  N   . GLU A 85  ? 0.4409 0.4874 0.9308 -0.1118 0.0236  0.0877  86  GLU A N   
453   C  CA  . GLU A 85  ? 0.3727 0.4320 0.8545 -0.1133 0.0289  0.0863  86  GLU A CA  
454   C  C   . GLU A 85  ? 0.4870 0.5317 0.9757 -0.1054 0.0195  0.0932  86  GLU A C   
455   O  O   . GLU A 85  ? 0.5521 0.5995 1.0436 -0.0951 0.0239  0.0845  86  GLU A O   
456   C  CB  . GLU A 85  ? 0.4194 0.4966 0.8838 -0.1344 0.0319  0.0954  86  GLU A CB  
457   C  CG  . GLU A 85  ? 0.5247 0.6247 0.9822 -0.1409 0.0462  0.0828  86  GLU A CG  
458   C  CD  . GLU A 85  ? 0.6785 0.7998 1.1182 -0.1624 0.0517  0.0886  86  GLU A CD  
459   O  OE1 . GLU A 85  ? 0.7236 0.8399 1.1539 -0.1744 0.0424  0.1056  86  GLU A OE1 
460   O  OE2 . GLU A 85  ? 0.7047 0.8479 1.1397 -0.1675 0.0650  0.0757  86  GLU A OE2 
461   N  N   . THR A 86  ? 0.4629 0.4924 0.9553 -0.1100 0.0060  0.1085  87  THR A N   
462   C  CA  . THR A 86  ? 0.4591 0.4743 0.9610 -0.1026 -0.0049 0.1160  87  THR A CA  
463   C  C   . THR A 86  ? 0.3901 0.3944 0.9090 -0.0823 -0.0028 0.1014  87  THR A C   
464   O  O   . THR A 86  ? 0.4486 0.4528 0.9719 -0.0743 -0.0022 0.0979  87  THR A O   
465   C  CB  . THR A 86  ? 0.4690 0.4682 0.9754 -0.1089 -0.0211 0.1337  87  THR A CB  
466   O  OG1 . THR A 86  ? 0.5353 0.5449 1.0230 -0.1293 -0.0246 0.1495  87  THR A OG1 
467   C  CG2 . THR A 86  ? 0.4091 0.3931 0.9318 -0.0975 -0.0326 0.1382  87  THR A CG2 
468   N  N   . ALA A 87  ? 0.2939 0.2901 0.8213 -0.0753 -0.0015 0.0928  88  ALA A N   
469   C  CA  . ALA A 87  ? 0.3721 0.3600 0.9129 -0.0583 0.0013  0.0779  88  ALA A CA  
470   C  C   . ALA A 87  ? 0.3902 0.3907 0.9256 -0.0520 0.0129  0.0652  88  ALA A C   
471   O  O   . ALA A 87  ? 0.3759 0.3729 0.9179 -0.0420 0.0134  0.0597  88  ALA A O   
472   C  CB  . ALA A 87  ? 0.2787 0.2602 0.8252 -0.0552 0.0021  0.0703  88  ALA A CB  
473   N  N   . LEU A 88  ? 0.3855 0.4013 0.9095 -0.0580 0.0221  0.0605  89  LEU A N   
474   C  CA  . LEU A 88  ? 0.3769 0.4053 0.8952 -0.0518 0.0326  0.0480  89  LEU A CA  
475   C  C   . LEU A 88  ? 0.3333 0.3671 0.8477 -0.0514 0.0332  0.0506  89  LEU A C   
476   O  O   . LEU A 88  ? 0.2372 0.2691 0.7555 -0.0403 0.0359  0.0420  89  LEU A O   
477   C  CB  . LEU A 88  ? 0.4125 0.4580 0.9199 -0.0597 0.0410  0.0438  89  LEU A CB  
478   C  CG  . LEU A 88  ? 0.4961 0.5525 0.9988 -0.0517 0.0507  0.0294  89  LEU A CG  
479   C  CD1 . LEU A 88  ? 0.4986 0.5454 1.0090 -0.0396 0.0506  0.0194  89  LEU A CD1 
480   C  CD2 . LEU A 88  ? 0.4922 0.5673 0.9853 -0.0609 0.0587  0.0260  89  LEU A CD2 
481   N  N   . ARG A 89  ? 0.4186 0.4597 0.9246 -0.0646 0.0302  0.0629  90  ARG A N   
482   C  CA  . ARG A 89  ? 0.5088 0.5572 1.0096 -0.0663 0.0307  0.0658  90  ARG A CA  
483   C  C   . ARG A 89  ? 0.5456 0.5787 1.0599 -0.0578 0.0212  0.0709  90  ARG A C   
484   O  O   . ARG A 89  ? 0.5787 0.6154 1.0894 -0.0529 0.0221  0.0684  90  ARG A O   
485   C  CB  . ARG A 89  ? 0.6226 0.6838 1.1093 -0.0851 0.0294  0.0785  90  ARG A CB  
486   C  CG  . ARG A 89  ? 0.7354 0.8117 1.2098 -0.0880 0.0352  0.0752  90  ARG A CG  
487   C  CD  . ARG A 89  ? 0.8355 0.9226 1.2928 -0.1077 0.0315  0.0893  90  ARG A CD  
488   N  NE  . ARG A 89  ? 0.9235 1.0122 1.3781 -0.1222 0.0292  0.0989  90  ARG A NE  
489   C  CZ  . ARG A 89  ? 0.9890 1.0974 1.4307 -0.1372 0.0388  0.0960  90  ARG A CZ  
490   N  NH1 . ARG A 89  ? 1.0132 1.1408 1.4449 -0.1388 0.0516  0.0827  90  ARG A NH1 
491   N  NH2 . ARG A 89  ? 1.0006 1.1090 1.4369 -0.1497 0.0358  0.1048  90  ARG A NH2 
492   N  N   . ASP A 90  ? 0.5410 0.5569 1.0678 -0.0545 0.0118  0.0762  91  ASP A N   
493   C  CA  . ASP A 90  ? 0.5058 0.5070 1.0489 -0.0441 0.0036  0.0773  91  ASP A CA  
494   C  C   . ASP A 90  ? 0.4874 0.4875 1.0376 -0.0295 0.0118  0.0598  91  ASP A C   
495   O  O   . ASP A 90  ? 0.4929 0.4934 1.0453 -0.0223 0.0117  0.0567  91  ASP A O   
496   C  CB  . ASP A 90  ? 0.5949 0.5794 1.1503 -0.0426 -0.0076 0.0840  91  ASP A CB  
497   C  CG  . ASP A 90  ? 0.6451 0.6261 1.1987 -0.0543 -0.0209 0.1045  91  ASP A CG  
498   O  OD1 . ASP A 90  ? 0.6681 0.6614 1.2062 -0.0673 -0.0201 0.1139  91  ASP A OD1 
499   O  OD2 . ASP A 90  ? 0.6952 0.6627 1.2626 -0.0509 -0.0324 0.1107  91  ASP A OD2 
500   N  N   . SER A 91  ? 0.4041 0.4035 0.9539 -0.0250 0.0180  0.0486  92  SER A N   
501   C  CA  . SER A 91  ? 0.4325 0.4318 0.9858 -0.0135 0.0253  0.0330  92  SER A CA  
502   C  C   . SER A 91  ? 0.2358 0.2490 0.7776 -0.0117 0.0329  0.0282  92  SER A C   
503   O  O   . SER A 91  ? 0.1880 0.1999 0.7320 -0.0030 0.0345  0.0217  92  SER A O   
504   C  CB  . SER A 91  ? 0.3926 0.3916 0.9437 -0.0120 0.0299  0.0241  92  SER A CB  
505   O  OG  . SER A 91  ? 0.4607 0.4560 1.0179 -0.0021 0.0333  0.0112  92  SER A OG  
506   N  N   . SER A 92  ? 0.2320 0.2583 0.7595 -0.0199 0.0375  0.0305  93  SER A N   
507   C  CA  . SER A 92  ? 0.3490 0.3879 0.8629 -0.0191 0.0442  0.0256  93  SER A CA  
508   C  C   . SER A 92  ? 0.3673 0.4069 0.8835 -0.0189 0.0401  0.0315  93  SER A C   
509   O  O   . SER A 92  ? 0.2535 0.2959 0.7647 -0.0120 0.0440  0.0243  93  SER A O   
510   C  CB  . SER A 92  ? 0.3287 0.3824 0.8295 -0.0302 0.0494  0.0273  93  SER A CB  
511   O  OG  . SER A 92  ? 0.4179 0.4833 0.9070 -0.0301 0.0558  0.0216  93  SER A OG  
512   N  N   . ARG A 93  ? 0.4154 0.4496 0.9339 -0.0258 0.0305  0.0453  94  ARG A N   
513   C  CA  . ARG A 93  ? 0.4209 0.4541 0.9393 -0.0259 0.0238  0.0529  94  ARG A CA  
514   C  C   . ARG A 93  ? 0.3920 0.4153 0.9250 -0.0120 0.0221  0.0457  94  ARG A C   
515   O  O   . ARG A 93  ? 0.3797 0.4072 0.9107 -0.0081 0.0228  0.0436  94  ARG A O   
516   C  CB  . ARG A 93  ? 0.4641 0.4918 0.9849 -0.0366 0.0115  0.0710  94  ARG A CB  
517   C  CG  . ARG A 93  ? 0.5805 0.6227 1.0819 -0.0519 0.0111  0.0808  94  ARG A CG  
518   C  CD  . ARG A 93  ? 0.7064 0.7438 1.2075 -0.0659 -0.0009 0.0999  94  ARG A CD  
519   N  NE  . ARG A 93  ? 0.7951 0.8488 1.2739 -0.0833 0.0002  0.1083  94  ARG A NE  
520   C  CZ  . ARG A 93  ? 0.9147 0.9694 1.3859 -0.1002 -0.0083 0.1254  94  ARG A CZ  
521   N  NH1 . ARG A 93  ? 0.9149 0.9535 1.4010 -0.1009 -0.0193 0.1364  94  ARG A NH1 
522   N  NH2 . ARG A 93  ? 0.9443 1.0162 1.3928 -0.1174 -0.0058 0.1311  94  ARG A NH2 
523   N  N   . VAL A 94  ? 0.3198 0.3307 0.8676 -0.0055 0.0205  0.0410  95  VAL A N   
524   C  CA  . VAL A 94  ? 0.2953 0.2986 0.8558 0.0063  0.0212  0.0310  95  VAL A CA  
525   C  C   . VAL A 94  ? 0.3613 0.3685 0.8946 0.0081  0.0307  0.0181  95  VAL A C   
526   O  O   . VAL A 94  ? 0.3670 0.3744 0.8910 0.0101  0.0308  0.0149  95  VAL A O   
527   C  CB  . VAL A 94  ? 0.2631 0.2586 0.8253 0.0059  0.0198  0.0242  95  VAL A CB  
528   C  CG1 . VAL A 94  ? 0.1986 0.1933 0.7473 0.0084  0.0230  0.0105  95  VAL A CG1 
529   C  CG2 . VAL A 94  ? 0.2281 0.2167 0.8085 0.0041  0.0082  0.0359  95  VAL A CG2 
530   N  N   . LEU A 95  ? 0.3389 0.3485 0.8597 0.0071  0.0375  0.0117  96  LEU A N   
531   C  CA  . LEU A 95  ? 0.2979 0.3088 0.7937 0.0084  0.0439  0.0015  96  LEU A CA  
532   C  C   . LEU A 95  ? 0.2620 0.2813 0.7500 0.0089  0.0459  0.0032  96  LEU A C   
533   O  O   . LEU A 95  ? 0.3185 0.3358 0.7927 0.0109  0.0471  -0.0022 96  LEU A O   
534   C  CB  . LEU A 95  ? 0.3224 0.3355 0.8099 0.0070  0.0486  -0.0032 96  LEU A CB  
535   C  CG  . LEU A 95  ? 0.2656 0.2797 0.7311 0.0079  0.0529  -0.0115 96  LEU A CG  
536   C  CD1 . LEU A 95  ? 0.2823 0.2908 0.7388 0.0090  0.0516  -0.0173 96  LEU A CD1 
537   C  CD2 . LEU A 95  ? 0.2362 0.2526 0.6985 0.0065  0.0556  -0.0147 96  LEU A CD2 
538   N  N   . GLN A 96  ? 0.3179 0.3503 0.8143 0.0045  0.0461  0.0109  97  GLN A N   
539   C  CA  . GLN A 96  ? 0.3217 0.3668 0.8115 0.0013  0.0484  0.0125  97  GLN A CA  
540   C  C   . GLN A 96  ? 0.3364 0.3790 0.8332 0.0044  0.0428  0.0166  97  GLN A C   
541   O  O   . GLN A 96  ? 0.3977 0.4428 0.8830 0.0063  0.0454  0.0120  97  GLN A O   
542   C  CB  . GLN A 96  ? 0.3993 0.4598 0.8921 -0.0116 0.0485  0.0215  97  GLN A CB  
543   C  CG  . GLN A 96  ? 0.5189 0.5940 0.9970 -0.0176 0.0552  0.0174  97  GLN A CG  
544   C  CD  . GLN A 96  ? 0.6142 0.7019 1.0853 -0.0331 0.0562  0.0246  97  GLN A CD  
545   O  OE1 . GLN A 96  ? 0.6140 0.7002 1.0871 -0.0379 0.0554  0.0283  97  GLN A OE1 
546   N  NE2 . GLN A 96  ? 0.6730 0.7725 1.1315 -0.0418 0.0577  0.0262  97  GLN A NE2 
547   N  N   . ALA A 97  ? 0.3334 0.3704 0.8503 0.0049  0.0344  0.0252  98  ALA A N   
548   C  CA  . ALA A 97  ? 0.3003 0.3327 0.8260 0.0087  0.0275  0.0289  98  ALA A CA  
549   C  C   . ALA A 97  ? 0.2918 0.3135 0.7979 0.0136  0.0318  0.0158  98  ALA A C   
550   O  O   . ALA A 97  ? 0.2447 0.2693 0.7447 0.0150  0.0319  0.0141  98  ALA A O   
551   C  CB  . ALA A 97  ? 0.2640 0.2883 0.8144 0.0090  0.0166  0.0390  98  ALA A CB  
552   N  N   . MET A 98  ? 0.2136 0.2274 0.7107 0.0139  0.0350  0.0073  99  MET A N   
553   C  CA  . MET A 98  ? 0.2918 0.3025 0.7716 0.0152  0.0385  -0.0036 99  MET A CA  
554   C  C   . MET A 98  ? 0.2846 0.2999 0.7453 0.0156  0.0437  -0.0078 99  MET A C   
555   O  O   . MET A 98  ? 0.2815 0.2979 0.7360 0.0169  0.0438  -0.0105 99  MET A O   
556   C  CB  . MET A 98  ? 0.2339 0.2404 0.7085 0.0142  0.0409  -0.0106 99  MET A CB  
557   C  CG  . MET A 98  ? 0.2728 0.2782 0.7357 0.0150  0.0435  -0.0202 99  MET A CG  
558   S  SD  . MET A 98  ? 0.4647 0.4729 0.9038 0.0147  0.0490  -0.0256 99  MET A SD  
559   C  CE  . MET A 98  ? 0.3636 0.3707 0.8002 0.0128  0.0508  -0.0264 99  MET A CE  
560   N  N   . LEU A 99  ? 0.2702 0.2887 0.7233 0.0143  0.0477  -0.0087 100 LEU A N   
561   C  CA  . LEU A 99  ? 0.3110 0.3336 0.7479 0.0144  0.0521  -0.0133 100 LEU A CA  
562   C  C   . LEU A 99  ? 0.3295 0.3593 0.7696 0.0148  0.0515  -0.0100 100 LEU A C   
563   O  O   . LEU A 99  ? 0.2678 0.2983 0.6967 0.0156  0.0531  -0.0143 100 LEU A O   
564   C  CB  . LEU A 99  ? 0.2600 0.2865 0.6928 0.0127  0.0560  -0.0149 100 LEU A CB  
565   C  CG  . LEU A 99  ? 0.2988 0.3197 0.7275 0.0120  0.0565  -0.0185 100 LEU A CG  
566   C  CD1 . LEU A 99  ? 0.2401 0.2662 0.6684 0.0104  0.0599  -0.0197 100 LEU A CD1 
567   C  CD2 . LEU A 99  ? 0.1619 0.1790 0.5772 0.0126  0.0566  -0.0242 100 LEU A CD2 
568   N  N   . ALA A 100 ? 0.3379 0.3749 0.7953 0.0135  0.0484  -0.0015 101 ALA A N   
569   C  CA  . ALA A 100 ? 0.2173 0.2655 0.6811 0.0120  0.0468  0.0032  101 ALA A CA  
570   C  C   . ALA A 100 ? 0.3176 0.3599 0.7827 0.0155  0.0425  0.0029  101 ALA A C   
571   O  O   . ALA A 100 ? 0.3063 0.3533 0.7643 0.0157  0.0441  0.0000  101 ALA A O   
572   C  CB  . ALA A 100 ? 0.2008 0.2618 0.6846 0.0055  0.0419  0.0157  101 ALA A CB  
573   N  N   . THR A 101 ? 0.2825 0.3155 0.7570 0.0173  0.0376  0.0047  102 THR A N   
574   C  CA  . THR A 101 ? 0.3042 0.3334 0.7806 0.0195  0.0343  0.0027  102 THR A CA  
575   C  C   . THR A 101 ? 0.2468 0.2739 0.7021 0.0202  0.0403  -0.0079 102 THR A C   
576   O  O   . THR A 101 ? 0.2011 0.2309 0.6539 0.0212  0.0401  -0.0097 102 THR A O   
577   C  CB  . THR A 101 ? 0.2522 0.2737 0.7428 0.0203  0.0290  0.0038  102 THR A CB  
578   O  OG1 . THR A 101 ? 0.3804 0.3965 0.8610 0.0196  0.0336  -0.0039 102 THR A OG1 
579   C  CG2 . THR A 101 ? 0.2385 0.2609 0.7530 0.0192  0.0205  0.0170  102 THR A CG2 
580   N  N   . GLN A 102 ? 0.2557 0.2789 0.6977 0.0193  0.0447  -0.0138 103 GLN A N   
581   C  CA  . GLN A 102 ? 0.2154 0.2378 0.6399 0.0191  0.0490  -0.0213 103 GLN A CA  
582   C  C   . GLN A 102 ? 0.3544 0.3821 0.7708 0.0189  0.0511  -0.0216 103 GLN A C   
583   O  O   . GLN A 102 ? 0.2992 0.3278 0.7098 0.0194  0.0519  -0.0246 103 GLN A O   
584   C  CB  . GLN A 102 ? 0.2196 0.2387 0.6347 0.0177  0.0518  -0.0251 103 GLN A CB  
585   C  CG  . GLN A 102 ? 0.2516 0.2666 0.6726 0.0176  0.0509  -0.0279 103 GLN A CG  
586   C  CD  . GLN A 102 ? 0.3083 0.3233 0.7286 0.0183  0.0518  -0.0336 103 GLN A CD  
587   O  OE1 . GLN A 102 ? 0.2992 0.3163 0.7103 0.0184  0.0539  -0.0362 103 GLN A OE1 
588   N  NE2 . GLN A 102 ? 0.3127 0.3257 0.7446 0.0187  0.0504  -0.0362 103 GLN A NE2 
589   N  N   . LEU A 103 ? 0.2836 0.3156 0.7013 0.0178  0.0525  -0.0190 104 LEU A N   
590   C  CA  . LEU A 103 ? 0.3262 0.3648 0.7380 0.0169  0.0554  -0.0210 104 LEU A CA  
591   C  C   . LEU A 103 ? 0.2806 0.3252 0.6995 0.0176  0.0530  -0.0185 104 LEU A C   
592   O  O   . LEU A 103 ? 0.3327 0.3781 0.7437 0.0177  0.0547  -0.0225 104 LEU A O   
593   C  CB  . LEU A 103 ? 0.3104 0.3567 0.7265 0.0147  0.0580  -0.0195 104 LEU A CB  
594   C  CG  . LEU A 103 ? 0.2646 0.3197 0.6753 0.0125  0.0625  -0.0241 104 LEU A CG  
595   C  CD1 . LEU A 103 ? 0.3023 0.3496 0.6989 0.0136  0.0641  -0.0308 104 LEU A CD1 
596   C  CD2 . LEU A 103 ? 0.2456 0.3103 0.6597 0.0085  0.0665  -0.0249 104 LEU A CD2 
597   N  N   . ARG A 104 ? 0.2664 0.3155 0.7025 0.0176  0.0483  -0.0109 105 ARG A N   
598   C  CA  . ARG A 104 ? 0.2689 0.3250 0.7158 0.0179  0.0440  -0.0067 105 ARG A CA  
599   C  C   . ARG A 104 ? 0.2548 0.3040 0.6958 0.0205  0.0436  -0.0117 105 ARG A C   
600   O  O   . ARG A 104 ? 0.1631 0.2170 0.6013 0.0204  0.0443  -0.0138 105 ARG A O   
601   C  CB  . ARG A 104 ? 0.1667 0.2272 0.6364 0.0171  0.0359  0.0046  105 ARG A CB  
602   N  N   . SER A 105 ? 0.1669 0.2072 0.6070 0.0218  0.0430  -0.0141 106 SER A N   
603   C  CA  . SER A 105 ? 0.3261 0.3633 0.7627 0.0229  0.0438  -0.0197 106 SER A CA  
604   C  C   . SER A 105 ? 0.2823 0.3202 0.7022 0.0219  0.0488  -0.0258 106 SER A C   
605   O  O   . SER A 105 ? 0.2745 0.3157 0.6950 0.0224  0.0489  -0.0276 106 SER A O   
606   C  CB  . SER A 105 ? 0.2443 0.2749 0.6822 0.0231  0.0441  -0.0233 106 SER A CB  
607   O  OG  . SER A 105 ? 0.3424 0.3715 0.7992 0.0241  0.0385  -0.0181 106 SER A OG  
608   N  N   . PHE A 106 ? 0.2009 0.2358 0.6081 0.0205  0.0524  -0.0285 107 PHE A N   
609   C  CA  . PHE A 106 ? 0.2597 0.2942 0.6543 0.0194  0.0559  -0.0330 107 PHE A CA  
610   C  C   . PHE A 106 ? 0.1988 0.2386 0.5923 0.0188  0.0566  -0.0329 107 PHE A C   
611   O  O   . PHE A 106 ? 0.2191 0.2602 0.6095 0.0185  0.0578  -0.0356 107 PHE A O   
612   C  CB  . PHE A 106 ? 0.1584 0.1886 0.5438 0.0180  0.0580  -0.0349 107 PHE A CB  
613   C  CG  . PHE A 106 ? 0.2315 0.2581 0.6156 0.0178  0.0588  -0.0377 107 PHE A CG  
614   C  CD1 . PHE A 106 ? 0.1619 0.1861 0.5520 0.0182  0.0575  -0.0369 107 PHE A CD1 
615   C  CD2 . PHE A 106 ? 0.1599 0.1862 0.5390 0.0169  0.0612  -0.0415 107 PHE A CD2 
616   C  CE1 . PHE A 106 ? 0.1639 0.1861 0.5544 0.0177  0.0590  -0.0411 107 PHE A CE1 
617   C  CE2 . PHE A 106 ? 0.1620 0.1868 0.5421 0.0163  0.0630  -0.0452 107 PHE A CE2 
618   C  CZ  . PHE A 106 ? 0.1641 0.1871 0.5495 0.0168  0.0620  -0.0455 107 PHE A CZ  
619   N  N   . ASP A 107 ? 0.2152 0.2595 0.6128 0.0182  0.0565  -0.0303 108 ASP A N   
620   C  CA  . ASP A 107 ? 0.2410 0.2930 0.6395 0.0169  0.0580  -0.0316 108 ASP A CA  
621   C  C   . ASP A 107 ? 0.3308 0.3885 0.7378 0.0176  0.0552  -0.0297 108 ASP A C   
622   O  O   . ASP A 107 ? 0.3389 0.3982 0.7422 0.0169  0.0567  -0.0332 108 ASP A O   
623   C  CB  . ASP A 107 ? 0.1793 0.2395 0.5842 0.0150  0.0590  -0.0295 108 ASP A CB  
624   C  CG  . ASP A 107 ? 0.2926 0.3628 0.6971 0.0118  0.0625  -0.0337 108 ASP A CG  
625   O  OD1 . ASP A 107 ? 0.3254 0.3907 0.7210 0.0118  0.0651  -0.0396 108 ASP A OD1 
626   O  OD2 . ASP A 107 ? 0.3152 0.3995 0.7297 0.0080  0.0623  -0.0308 108 ASP A OD2 
627   N  N   . ASP A 108 ? 0.2664 0.3267 0.6867 0.0188  0.0505  -0.0239 109 ASP A N   
628   C  CA  . ASP A 108 ? 0.3116 0.3777 0.7439 0.0197  0.0462  -0.0209 109 ASP A CA  
629   C  C   . ASP A 108 ? 0.2551 0.3163 0.6815 0.0210  0.0478  -0.0263 109 ASP A C   
630   O  O   . ASP A 108 ? 0.2820 0.3491 0.7126 0.0207  0.0469  -0.0269 109 ASP A O   
631   C  CB  . ASP A 108 ? 0.3226 0.3897 0.7730 0.0210  0.0392  -0.0131 109 ASP A CB  
632   C  CG  . ASP A 108 ? 0.3527 0.4316 0.8158 0.0177  0.0352  -0.0046 109 ASP A CG  
633   O  OD1 . ASP A 108 ? 0.4181 0.5045 0.8737 0.0138  0.0401  -0.0070 109 ASP A OD1 
634   O  OD2 . ASP A 108 ? 0.4049 0.4871 0.8866 0.0175  0.0268  0.0049  109 ASP A OD2 
635   N  N   . HIS A 109 ? 0.1624 0.2151 0.5805 0.0215  0.0503  -0.0300 110 HIS A N   
636   C  CA  . HIS A 109 ? 0.2315 0.2826 0.6465 0.0217  0.0524  -0.0351 110 HIS A CA  
637   C  C   . HIS A 109 ? 0.3020 0.3536 0.7060 0.0197  0.0564  -0.0389 110 HIS A C   
638   O  O   . HIS A 109 ? 0.2314 0.2859 0.6371 0.0194  0.0576  -0.0416 110 HIS A O   
639   C  CB  . HIS A 109 ? 0.1658 0.2109 0.5783 0.0219  0.0542  -0.0383 110 HIS A CB  
640   C  CG  . HIS A 109 ? 0.2976 0.3438 0.7098 0.0215  0.0574  -0.0443 110 HIS A CG  
641   N  ND1 . HIS A 109 ? 0.2302 0.2812 0.6542 0.0227  0.0561  -0.0459 110 HIS A ND1 
642   C  CD2 . HIS A 109 ? 0.2922 0.3367 0.6961 0.0197  0.0620  -0.0492 110 HIS A CD2 
643   C  CE1 . HIS A 109 ? 0.3083 0.3607 0.7304 0.0216  0.0607  -0.0524 110 HIS A CE1 
644   N  NE2 . HIS A 109 ? 0.3465 0.3952 0.7566 0.0197  0.0644  -0.0542 110 HIS A NE2 
645   N  N   . PHE A 110 ? 0.2372 0.2858 0.6319 0.0183  0.0584  -0.0393 111 PHE A N   
646   C  CA  . PHE A 110 ? 0.2634 0.3117 0.6515 0.0164  0.0613  -0.0425 111 PHE A CA  
647   C  C   . PHE A 110 ? 0.3242 0.3800 0.7180 0.0158  0.0606  -0.0426 111 PHE A C   
648   O  O   . PHE A 110 ? 0.2965 0.3543 0.6909 0.0148  0.0619  -0.0451 111 PHE A O   
649   C  CB  . PHE A 110 ? 0.1563 0.2001 0.5372 0.0152  0.0628  -0.0431 111 PHE A CB  
650   C  CG  . PHE A 110 ? 0.2095 0.2471 0.5854 0.0150  0.0635  -0.0435 111 PHE A CG  
651   C  CD1 . PHE A 110 ? 0.2616 0.2981 0.6372 0.0145  0.0651  -0.0455 111 PHE A CD1 
652   C  CD2 . PHE A 110 ? 0.1758 0.2103 0.5492 0.0151  0.0631  -0.0423 111 PHE A CD2 
653   C  CE1 . PHE A 110 ? 0.1578 0.1906 0.5312 0.0139  0.0662  -0.0463 111 PHE A CE1 
654   C  CE2 . PHE A 110 ? 0.1558 0.1860 0.5263 0.0147  0.0635  -0.0426 111 PHE A CE2 
655   C  CZ  . PHE A 110 ? 0.1569 0.1864 0.5277 0.0141  0.0651  -0.0446 111 PHE A CZ  
656   N  N   . GLN A 111 ? 0.1570 0.2186 0.5568 0.0158  0.0587  -0.0398 112 GLN A N   
657   C  CA  . GLN A 111 ? 0.2914 0.3636 0.6991 0.0143  0.0578  -0.0397 112 GLN A CA  
658   C  C   . GLN A 111 ? 0.3498 0.4265 0.7664 0.0154  0.0547  -0.0381 112 GLN A C   
659   O  O   . GLN A 111 ? 0.3207 0.4032 0.7398 0.0136  0.0552  -0.0403 112 GLN A O   
660   C  CB  . GLN A 111 ? 0.2731 0.3548 0.6891 0.0127  0.0559  -0.0358 112 GLN A CB  
661   C  CG  . GLN A 111 ? 0.3216 0.4033 0.7307 0.0103  0.0605  -0.0399 112 GLN A CG  
662   C  CD  . GLN A 111 ? 0.4662 0.5615 0.8843 0.0063  0.0599  -0.0366 112 GLN A CD  
663   O  OE1 . GLN A 111 ? 0.4706 0.5644 0.8868 0.0059  0.0616  -0.0359 112 GLN A OE1 
664   N  NE2 . GLN A 111 ? 0.4722 0.5828 0.9007 0.0015  0.0572  -0.0339 112 GLN A NE2 
665   N  N   . HIS A 112 ? 0.2668 0.3407 0.6893 0.0180  0.0518  -0.0353 113 HIS A N   
666   C  CA  A HIS A 112 ? 0.2768 0.3547 0.7099 0.0193  0.0490  -0.0349 113 HIS A CA  
667   C  CA  B HIS A 112 ? 0.2828 0.3605 0.7159 0.0193  0.0490  -0.0349 113 HIS A CA  
668   C  C   . HIS A 112 ? 0.2863 0.3616 0.7125 0.0185  0.0535  -0.0409 113 HIS A C   
669   O  O   . HIS A 112 ? 0.2586 0.3403 0.6919 0.0181  0.0528  -0.0420 113 HIS A O   
670   C  CB  A HIS A 112 ? 0.1662 0.2410 0.6096 0.0221  0.0452  -0.0320 113 HIS A CB  
671   C  CB  B HIS A 112 ? 0.1661 0.2402 0.6087 0.0221  0.0455  -0.0322 113 HIS A CB  
672   C  CG  A HIS A 112 ? 0.2035 0.2808 0.6577 0.0236  0.0439  -0.0343 113 HIS A CG  
673   C  CG  B HIS A 112 ? 0.2126 0.2923 0.6713 0.0229  0.0382  -0.0241 113 HIS A CG  
674   N  ND1 A HIS A 112 ? 0.2567 0.3295 0.7072 0.0240  0.0483  -0.0407 113 HIS A ND1 
675   N  ND1 B HIS A 112 ? 0.1699 0.2447 0.6344 0.0242  0.0352  -0.0198 113 HIS A ND1 
676   C  CD2 A HIS A 112 ? 0.2505 0.3361 0.7207 0.0243  0.0388  -0.0315 113 HIS A CD2 
677   C  CD2 B HIS A 112 ? 0.2188 0.3101 0.6911 0.0215  0.0323  -0.0183 113 HIS A CD2 
678   C  CE1 A HIS A 112 ? 0.2805 0.3584 0.7443 0.0252  0.0469  -0.0428 113 HIS A CE1 
679   C  CE1 B HIS A 112 ? 0.1719 0.2544 0.6535 0.0237  0.0272  -0.0108 113 HIS A CE1 
680   N  NE2 A HIS A 112 ? 0.2736 0.3586 0.7495 0.0257  0.0407  -0.0371 113 HIS A NE2 
681   N  NE2 B HIS A 112 ? 0.2108 0.3042 0.6973 0.0217  0.0250  -0.0094 113 HIS A NE2 
682   N  N   . LEU A 113 ? 0.2567 0.3241 0.6711 0.0178  0.0577  -0.0441 114 LEU A N   
683   C  CA  . LEU A 113 ? 0.2496 0.3161 0.6597 0.0162  0.0620  -0.0489 114 LEU A CA  
684   C  C   . LEU A 113 ? 0.3017 0.3717 0.7106 0.0138  0.0632  -0.0500 114 LEU A C   
685   O  O   . LEU A 113 ? 0.3007 0.3759 0.7144 0.0126  0.0644  -0.0523 114 LEU A O   
686   C  CB  . LEU A 113 ? 0.2484 0.3073 0.6487 0.0152  0.0654  -0.0508 114 LEU A CB  
687   C  CG  . LEU A 113 ? 0.2789 0.3358 0.6813 0.0164  0.0661  -0.0525 114 LEU A CG  
688   C  CD1 . LEU A 113 ? 0.3026 0.3537 0.6964 0.0150  0.0690  -0.0538 114 LEU A CD1 
689   C  CD2 . LEU A 113 ? 0.1694 0.2320 0.5802 0.0163  0.0685  -0.0573 114 LEU A CD2 
690   N  N   . LEU A 114 ? 0.2197 0.2878 0.6239 0.0128  0.0631  -0.0492 115 LEU A N   
691   C  CA  . LEU A 114 ? 0.3072 0.3785 0.7121 0.0101  0.0645  -0.0517 115 LEU A CA  
692   C  C   . LEU A 114 ? 0.3043 0.3869 0.7195 0.0095  0.0619  -0.0509 115 LEU A C   
693   O  O   . LEU A 114 ? 0.2461 0.3326 0.6647 0.0075  0.0630  -0.0533 115 LEU A O   
694   C  CB  . LEU A 114 ? 0.2602 0.3287 0.6609 0.0091  0.0653  -0.0527 115 LEU A CB  
695   C  CG  . LEU A 114 ? 0.3388 0.4076 0.7408 0.0060  0.0677  -0.0574 115 LEU A CG  
696   C  CD1 . LEU A 114 ? 0.3365 0.3988 0.7375 0.0050  0.0699  -0.0588 115 LEU A CD1 
697   C  CD2 . LEU A 114 ? 0.3733 0.4395 0.7729 0.0052  0.0693  -0.0602 115 LEU A CD2 
698   N  N   . ASN A 115 ? 0.2337 0.3225 0.6558 0.0106  0.0578  -0.0469 116 ASN A N   
699   C  CA  . ASN A 115 ? 0.2883 0.3901 0.7232 0.0093  0.0535  -0.0444 116 ASN A CA  
700   C  C   . ASN A 115 ? 0.3193 0.4239 0.7619 0.0106  0.0522  -0.0447 116 ASN A C   
701   O  O   . ASN A 115 ? 0.2420 0.3558 0.6919 0.0083  0.0508  -0.0454 116 ASN A O   
702   C  CB  . ASN A 115 ? 0.2879 0.3961 0.7321 0.0099  0.0480  -0.0379 116 ASN A CB  
703   C  CG  . ASN A 115 ? 0.3768 0.4894 0.8174 0.0062  0.0496  -0.0383 116 ASN A CG  
704   O  OD1 . ASN A 115 ? 0.3374 0.4448 0.7677 0.0047  0.0552  -0.0444 116 ASN A OD1 
705   N  ND2 . ASN A 115 ? 0.4355 0.5584 0.8864 0.0038  0.0444  -0.0318 116 ASN A ND2 
706   N  N   . ASP A 116 ? 0.2874 0.3852 0.7291 0.0137  0.0531  -0.0452 117 ASP A N   
707   C  CA  . ASP A 116 ? 0.2336 0.3346 0.6837 0.0149  0.0532  -0.0474 117 ASP A CA  
708   C  C   . ASP A 116 ? 0.2953 0.3968 0.7397 0.0119  0.0588  -0.0527 117 ASP A C   
709   O  O   . ASP A 116 ? 0.2681 0.3772 0.7212 0.0110  0.0588  -0.0546 117 ASP A O   
710   C  CB  . ASP A 116 ? 0.3264 0.4209 0.7775 0.0178  0.0540  -0.0485 117 ASP A CB  
711   C  CG  . ASP A 116 ? 0.4945 0.5946 0.9619 0.0199  0.0518  -0.0500 117 ASP A CG  
712   O  OD1 . ASP A 116 ? 0.5185 0.6221 1.0005 0.0222  0.0448  -0.0449 117 ASP A OD1 
713   O  OD2 . ASP A 116 ? 0.5581 0.6599 1.0258 0.0190  0.0568  -0.0563 117 ASP A OD2 
714   N  N   . SER A 117 ? 0.2836 0.3771 0.7153 0.0101  0.0630  -0.0546 118 SER A N   
715   C  CA  . SER A 117 ? 0.2559 0.3497 0.6844 0.0066  0.0676  -0.0583 118 SER A CA  
716   C  C   . SER A 117 ? 0.2297 0.3314 0.6640 0.0038  0.0659  -0.0584 118 SER A C   
717   O  O   . SER A 117 ? 0.1681 0.2762 0.6078 0.0014  0.0675  -0.0607 118 SER A O   
718   C  CB  . SER A 117 ? 0.2612 0.3450 0.6792 0.0052  0.0708  -0.0590 118 SER A CB  
719   O  OG  . SER A 117 ? 0.3112 0.3952 0.7293 0.0017  0.0751  -0.0617 118 SER A OG  
720   N  N   . GLU A 118 ? 0.2494 0.3523 0.6834 0.0035  0.0630  -0.0565 119 GLU A N   
721   C  CA  . GLU A 118 ? 0.2349 0.3470 0.6749 -0.0003 0.0614  -0.0576 119 GLU A CA  
722   C  C   . GLU A 118 ? 0.2388 0.3636 0.6918 -0.0006 0.0570  -0.0554 119 GLU A C   
723   O  O   . GLU A 118 ? 0.2583 0.3902 0.7162 -0.0043 0.0573  -0.0576 119 GLU A O   
724   C  CB  . GLU A 118 ? 0.2133 0.3274 0.6519 -0.0017 0.0598  -0.0570 119 GLU A CB  
725   C  CG  . GLU A 118 ? 0.2036 0.3264 0.6463 -0.0077 0.0600  -0.0608 119 GLU A CG  
726   C  CD  . GLU A 118 ? 0.3541 0.4821 0.7960 -0.0110 0.0597  -0.0622 119 GLU A CD  
727   O  OE1 . GLU A 118 ? 0.3880 0.5131 0.8268 -0.0082 0.0591  -0.0592 119 GLU A OE1 
728   O  OE2 . GLU A 118 ? 0.3666 0.5023 0.8111 -0.0174 0.0605  -0.0672 119 GLU A OE2 
729   N  N   . ARG A 119 ? 0.2663 0.3937 0.7264 0.0032  0.0525  -0.0511 120 ARG A N   
730   C  CA  . ARG A 119 ? 0.2596 0.3985 0.7356 0.0036  0.0469  -0.0484 120 ARG A CA  
731   C  C   . ARG A 119 ? 0.2358 0.3759 0.7152 0.0039  0.0508  -0.0529 120 ARG A C   
732   O  O   . ARG A 119 ? 0.2244 0.3752 0.7143 0.0017  0.0485  -0.0532 120 ARG A O   
733   C  CB  . ARG A 119 ? 0.2736 0.4128 0.7595 0.0079  0.0407  -0.0426 120 ARG A CB  
734   C  CG  . ARG A 119 ? 0.4046 0.5508 0.8951 0.0055  0.0342  -0.0361 120 ARG A CG  
735   C  CD  . ARG A 119 ? 0.4735 0.6207 0.9780 0.0091  0.0262  -0.0285 120 ARG A CD  
736   N  NE  . ARG A 119 ? 0.5519 0.6952 1.0514 0.0089  0.0251  -0.0244 120 ARG A NE  
737   C  CZ  . ARG A 119 ? 0.5926 0.7230 1.0850 0.0132  0.0285  -0.0255 120 ARG A CZ  
738   N  NH1 . ARG A 119 ? 0.6090 0.7300 1.0982 0.0171  0.0330  -0.0308 120 ARG A NH1 
739   N  NH2 . ARG A 119 ? 0.5984 0.7271 1.0876 0.0124  0.0275  -0.0215 120 ARG A NH2 
740   N  N   . THR A 120 ? 0.2269 0.3577 0.6981 0.0057  0.0565  -0.0565 121 THR A N   
741   C  CA  . THR A 120 ? 0.2741 0.4076 0.7478 0.0045  0.0617  -0.0617 121 THR A CA  
742   C  C   . THR A 120 ? 0.3416 0.4794 0.8125 -0.0011 0.0649  -0.0641 121 THR A C   
743   O  O   . THR A 120 ? 0.4117 0.5589 0.8912 -0.0033 0.0660  -0.0665 121 THR A O   
744   C  CB  . THR A 120 ? 0.2343 0.3589 0.6987 0.0055  0.0676  -0.0652 121 THR A CB  
745   O  OG1 . THR A 120 ? 0.3271 0.4468 0.7941 0.0100  0.0645  -0.0633 121 THR A OG1 
746   C  CG2 . THR A 120 ? 0.1817 0.3128 0.6512 0.0033  0.0735  -0.0714 121 THR A CG2 
747   N  N   . LEU A 121 ? 0.3186 0.4493 0.7789 -0.0035 0.0664  -0.0636 122 LEU A N   
748   C  CA  . LEU A 121 ? 0.3165 0.4495 0.7758 -0.0091 0.0688  -0.0658 122 LEU A CA  
749   C  C   . LEU A 121 ? 0.2939 0.4394 0.7637 -0.0118 0.0640  -0.0649 122 LEU A C   
750   O  O   . LEU A 121 ? 0.2602 0.4133 0.7357 -0.0157 0.0654  -0.0670 122 LEU A O   
751   C  CB  . LEU A 121 ? 0.3401 0.4627 0.7900 -0.0106 0.0702  -0.0661 122 LEU A CB  
752   C  CG  . LEU A 121 ? 0.3170 0.4396 0.7680 -0.0166 0.0721  -0.0688 122 LEU A CG  
753   C  CD1 . LEU A 121 ? 0.3727 0.4826 0.8175 -0.0174 0.0758  -0.0697 122 LEU A CD1 
754   C  CD2 . LEU A 121 ? 0.2921 0.4204 0.7468 -0.0191 0.0683  -0.0697 122 LEU A CD2 
755   N  N   . GLN A 122 ? 0.2567 0.4057 0.7296 -0.0107 0.0582  -0.0616 123 GLN A N   
756   C  CA  . GLN A 122 ? 0.2323 0.3951 0.7158 -0.0147 0.0524  -0.0600 123 GLN A CA  
757   C  C   . GLN A 122 ? 0.3274 0.5009 0.8250 -0.0135 0.0494  -0.0588 123 GLN A C   
758   O  O   . GLN A 122 ? 0.3795 0.5644 0.8854 -0.0181 0.0464  -0.0590 123 GLN A O   
759   C  CB  . GLN A 122 ? 0.2144 0.3816 0.7003 -0.0148 0.0461  -0.0555 123 GLN A CB  
760   C  CG  . GLN A 122 ? 0.3870 0.5481 0.8621 -0.0179 0.0492  -0.0584 123 GLN A CG  
761   C  CD  . GLN A 122 ? 0.4697 0.6387 0.9477 -0.0200 0.0436  -0.0544 123 GLN A CD  
762   O  OE1 . GLN A 122 ? 0.5147 0.6840 0.9867 -0.0249 0.0457  -0.0580 123 GLN A OE1 
763   N  NE2 . GLN A 122 ? 0.5142 0.6901 1.0030 -0.0172 0.0364  -0.0471 123 GLN A NE2 
764   N  N   . ALA A 123 ? 0.3468 0.5170 0.8480 -0.0077 0.0501  -0.0585 124 ALA A N   
765   C  CA  . ALA A 123 ? 0.4096 0.5895 0.9271 -0.0057 0.0475  -0.0586 124 ALA A CA  
766   C  C   . ALA A 123 ? 0.1862 0.3691 0.7038 -0.0084 0.0549  -0.0649 124 ALA A C   
767   O  O   . ALA A 123 ? 0.1900 0.3848 0.7210 -0.0100 0.0531  -0.0660 124 ALA A O   
768   C  CB  . ALA A 123 ? 0.1844 0.3596 0.7086 0.0011  0.0452  -0.0569 124 ALA A CB  
769   N  N   . THR A 124 ? 0.3038 0.4773 0.8077 -0.0096 0.0628  -0.0686 125 THR A N   
770   C  CA  . THR A 124 ? 0.1896 0.3674 0.6939 -0.0132 0.0703  -0.0742 125 THR A CA  
771   C  C   . THR A 124 ? 0.3211 0.5007 0.8195 -0.0209 0.0735  -0.0752 125 THR A C   
772   O  O   . THR A 124 ? 0.1949 0.3837 0.6988 -0.0256 0.0771  -0.0783 125 THR A O   
773   C  CB  . THR A 124 ? 0.1904 0.3598 0.6857 -0.0117 0.0770  -0.0776 125 THR A CB  
774   O  OG1 . THR A 124 ? 0.1862 0.3433 0.6664 -0.0126 0.0782  -0.0753 125 THR A OG1 
775   C  CG2 . THR A 124 ? 0.2976 0.4652 0.8004 -0.0049 0.0744  -0.0780 125 THR A CG2 
776   N  N   . PHE A 125 ? 0.3174 0.4881 0.8060 -0.0227 0.0722  -0.0729 126 PHE A N   
777   C  CA  . PHE A 125 ? 0.2436 0.4130 0.7277 -0.0302 0.0750  -0.0740 126 PHE A CA  
778   C  C   . PHE A 125 ? 0.2853 0.4670 0.7788 -0.0359 0.0723  -0.0747 126 PHE A C   
779   O  O   . PHE A 125 ? 0.2762 0.4603 0.7693 -0.0426 0.0763  -0.0765 126 PHE A O   
780   C  CB  . PHE A 125 ? 0.2029 0.3603 0.6783 -0.0302 0.0735  -0.0728 126 PHE A CB  
781   C  CG  . PHE A 125 ? 0.3067 0.4513 0.7725 -0.0295 0.0783  -0.0728 126 PHE A CG  
782   C  CD1 . PHE A 125 ? 0.3251 0.4677 0.7876 -0.0256 0.0812  -0.0728 126 PHE A CD1 
783   C  CD2 . PHE A 125 ? 0.2963 0.4314 0.7582 -0.0333 0.0794  -0.0732 126 PHE A CD2 
784   C  CE1 . PHE A 125 ? 0.3441 0.4766 0.7986 -0.0260 0.0849  -0.0723 126 PHE A CE1 
785   C  CE2 . PHE A 125 ? 0.3375 0.4617 0.7934 -0.0329 0.0826  -0.0721 126 PHE A CE2 
786   C  CZ  . PHE A 125 ? 0.3178 0.4415 0.7696 -0.0295 0.0853  -0.0713 126 PHE A CZ  
787   N  N   . PRO A 126 ? 0.3158 0.5060 0.8182 -0.0343 0.0651  -0.0725 127 PRO A N   
788   C  CA  . PRO A 126 ? 0.3368 0.5395 0.8483 -0.0407 0.0622  -0.0731 127 PRO A CA  
789   C  C   . PRO A 126 ? 0.3487 0.5616 0.8686 -0.0427 0.0662  -0.0756 127 PRO A C   
790   O  O   . PRO A 126 ? 0.4111 0.6306 0.9336 -0.0501 0.0673  -0.0770 127 PRO A O   
791   C  CB  . PRO A 126 ? 0.2862 0.4982 0.8076 -0.0384 0.0529  -0.0692 127 PRO A CB  
792   C  CG  . PRO A 126 ? 0.3080 0.5136 0.8285 -0.0299 0.0517  -0.0666 127 PRO A CG  
793   C  CD  . PRO A 126 ? 0.2962 0.4861 0.8011 -0.0287 0.0587  -0.0688 127 PRO A CD  
794   N  N   . GLY A 127 ? 0.4246 0.6391 0.9490 -0.0369 0.0687  -0.0769 128 GLY A N   
795   C  CA  . GLY A 127 ? 0.4431 0.6684 0.9763 -0.0390 0.0739  -0.0811 128 GLY A CA  
796   C  C   . GLY A 127 ? 0.4741 0.6960 0.9963 -0.0459 0.0829  -0.0840 128 GLY A C   
797   O  O   . GLY A 127 ? 0.5301 0.7621 1.0566 -0.0529 0.0866  -0.0863 128 GLY A O   
798   N  N   . ALA A 128 ? 0.4486 0.6570 0.9573 -0.0448 0.0860  -0.0831 129 ALA A N   
799   C  CA  . ALA A 128 ? 0.4769 0.6821 0.9758 -0.0518 0.0938  -0.0845 129 ALA A CA  
800   C  C   . ALA A 128 ? 0.4462 0.6472 0.9398 -0.0607 0.0935  -0.0818 129 ALA A C   
801   O  O   . ALA A 128 ? 0.4804 0.6842 0.9704 -0.0698 0.0988  -0.0819 129 ALA A O   
802   C  CB  . ALA A 128 ? 0.3943 0.5872 0.8827 -0.0475 0.0963  -0.0839 129 ALA A CB  
803   N  N   . PHE A 129 ? 0.3988 0.5932 0.8922 -0.0593 0.0872  -0.0796 130 PHE A N   
804   C  CA  . PHE A 129 ? 0.4263 0.6130 0.9154 -0.0670 0.0865  -0.0781 130 PHE A CA  
805   C  C   . PHE A 129 ? 0.4471 0.6392 0.9429 -0.0701 0.0807  -0.0787 130 PHE A C   
806   O  O   . PHE A 129 ? 0.4698 0.6583 0.9646 -0.0782 0.0804  -0.0787 130 PHE A O   
807   C  CB  . PHE A 129 ? 0.3429 0.5125 0.8236 -0.0637 0.0858  -0.0764 130 PHE A CB  
808   C  CG  . PHE A 129 ? 0.3322 0.4965 0.8062 -0.0610 0.0904  -0.0754 130 PHE A CG  
809   C  CD1 . PHE A 129 ? 0.3036 0.4705 0.7741 -0.0691 0.0960  -0.0743 130 PHE A CD1 
810   C  CD2 . PHE A 129 ? 0.2714 0.4291 0.7420 -0.0518 0.0891  -0.0752 130 PHE A CD2 
811   C  CE1 . PHE A 129 ? 0.3329 0.4967 0.7969 -0.0682 0.1003  -0.0736 130 PHE A CE1 
812   C  CE2 . PHE A 129 ? 0.2370 0.3903 0.7015 -0.0500 0.0932  -0.0746 130 PHE A CE2 
813   C  CZ  . PHE A 129 ? 0.2679 0.4249 0.7294 -0.0583 0.0989  -0.0741 130 PHE A CZ  
814   N  N   . GLY A 130 ? 0.4629 0.6633 0.9658 -0.0645 0.0756  -0.0789 131 GLY A N   
815   C  CA  . GLY A 130 ? 0.4378 0.6464 0.9476 -0.0685 0.0695  -0.0792 131 GLY A CA  
816   C  C   . GLY A 130 ? 0.4521 0.6508 0.9564 -0.0717 0.0665  -0.0805 131 GLY A C   
817   O  O   . GLY A 130 ? 0.4077 0.5978 0.9068 -0.0665 0.0654  -0.0804 131 GLY A O   
818   N  N   . GLU A 131 ? 0.3798 0.5798 0.8857 -0.0808 0.0654  -0.0824 132 GLU A N   
819   C  CA  . GLU A 131 ? 0.3959 0.5874 0.8983 -0.0852 0.0629  -0.0860 132 GLU A CA  
820   C  C   . GLU A 131 ? 0.3246 0.4971 0.8196 -0.0833 0.0668  -0.0872 132 GLU A C   
821   O  O   . GLU A 131 ? 0.3437 0.5080 0.8364 -0.0835 0.0655  -0.0913 132 GLU A O   
822   C  CB  . GLU A 131 ? 0.3657 0.5611 0.8716 -0.0959 0.0613  -0.0884 132 GLU A CB  
823   N  N   . LEU A 132 ? 0.2241 0.3909 0.7163 -0.0822 0.0715  -0.0839 133 LEU A N   
824   C  CA  . LEU A 132 ? 0.2900 0.4398 0.7769 -0.0801 0.0742  -0.0832 133 LEU A CA  
825   C  C   . LEU A 132 ? 0.3684 0.5136 0.8523 -0.0711 0.0733  -0.0843 133 LEU A C   
826   O  O   . LEU A 132 ? 0.4114 0.5442 0.8942 -0.0701 0.0733  -0.0871 133 LEU A O   
827   C  CB  . LEU A 132 ? 0.2254 0.3740 0.7091 -0.0814 0.0788  -0.0785 133 LEU A CB  
828   C  CG  . LEU A 132 ? 0.3317 0.4783 0.8156 -0.0925 0.0802  -0.0759 133 LEU A CG  
829   C  CD1 . LEU A 132 ? 0.3788 0.5220 0.8570 -0.0949 0.0844  -0.0708 133 LEU A CD1 
830   C  CD2 . LEU A 132 ? 0.3628 0.4948 0.8487 -0.0976 0.0767  -0.0776 133 LEU A CD2 
831   N  N   . TYR A 133 ? 0.3111 0.4661 0.7948 -0.0647 0.0724  -0.0823 134 TYR A N   
832   C  CA  . TYR A 133 ? 0.3126 0.4643 0.7928 -0.0570 0.0709  -0.0822 134 TYR A CA  
833   C  C   . TYR A 133 ? 0.3180 0.4771 0.8006 -0.0588 0.0661  -0.0850 134 TYR A C   
834   O  O   . TYR A 133 ? 0.3026 0.4552 0.7820 -0.0580 0.0659  -0.0883 134 TYR A O   
835   C  CB  . TYR A 133 ? 0.3121 0.4692 0.7915 -0.0498 0.0713  -0.0784 134 TYR A CB  
836   C  CG  . TYR A 133 ? 0.3506 0.5085 0.8286 -0.0435 0.0676  -0.0772 134 TYR A CG  
837   C  CD1 . TYR A 133 ? 0.3553 0.5013 0.8265 -0.0397 0.0689  -0.0777 134 TYR A CD1 
838   C  CD2 . TYR A 133 ? 0.3092 0.4804 0.7940 -0.0422 0.0621  -0.0749 134 TYR A CD2 
839   C  CE1 . TYR A 133 ? 0.3020 0.4498 0.7715 -0.0354 0.0656  -0.0763 134 TYR A CE1 
840   C  CE2 . TYR A 133 ? 0.3285 0.5013 0.8130 -0.0381 0.0579  -0.0724 134 TYR A CE2 
841   C  CZ  . TYR A 133 ? 0.2988 0.4601 0.7748 -0.0350 0.0601  -0.0732 134 TYR A CZ  
842   O  OH  . TYR A 133 ? 0.3318 0.4957 0.8073 -0.0320 0.0563  -0.0704 134 TYR A OH  
843   N  N   . THR A 134 ? 0.2034 0.3774 0.6922 -0.0622 0.0620  -0.0839 135 THR A N   
844   C  CA  . THR A 134 ? 0.4210 0.6059 0.9125 -0.0650 0.0560  -0.0847 135 THR A CA  
845   C  C   . THR A 134 ? 0.3904 0.5709 0.8787 -0.0725 0.0561  -0.0922 135 THR A C   
846   O  O   . THR A 134 ? 0.4497 0.6362 0.9363 -0.0751 0.0530  -0.0943 135 THR A O   
847   C  CB  . THR A 134 ? 0.3964 0.5987 0.8976 -0.0687 0.0505  -0.0818 135 THR A CB  
848   O  OG1 . THR A 134 ? 0.4106 0.6132 0.9136 -0.0759 0.0524  -0.0847 135 THR A OG1 
849   C  CG2 . THR A 134 ? 0.2018 0.4097 0.7091 -0.0608 0.0501  -0.0764 135 THR A CG2 
850   N  N   . GLN A 135 ? 0.4116 0.5820 0.8995 -0.0769 0.0597  -0.0965 136 GLN A N   
851   C  CA  . GLN A 135 ? 0.4557 0.6196 0.9422 -0.0837 0.0605  -0.1055 136 GLN A CA  
852   C  C   . GLN A 135 ? 0.4301 0.5771 0.9139 -0.0790 0.0651  -0.1094 136 GLN A C   
853   O  O   . GLN A 135 ? 0.3961 0.5346 0.8811 -0.0832 0.0669  -0.1182 136 GLN A O   
854   C  CB  . GLN A 135 ? 0.5779 0.7395 1.0680 -0.0918 0.0605  -0.1083 136 GLN A CB  
855   C  CG  . GLN A 135 ? 0.7100 0.8890 1.2038 -0.0980 0.0554  -0.1061 136 GLN A CG  
856   C  CD  . GLN A 135 ? 0.8132 1.0042 1.3054 -0.1042 0.0504  -0.1106 136 GLN A CD  
857   O  OE1 . GLN A 135 ? 0.8378 1.0417 1.3309 -0.1018 0.0460  -0.1055 136 GLN A OE1 
858   N  NE2 . GLN A 135 ? 0.8476 1.0345 1.3374 -0.1130 0.0508  -0.1204 136 GLN A NE2 
859   N  N   . ASN A 136 ? 0.4148 0.5571 0.8960 -0.0702 0.0669  -0.1034 137 ASN A N   
860   C  CA  . ASN A 136 ? 0.4000 0.5278 0.8798 -0.0649 0.0705  -0.1058 137 ASN A CA  
861   C  C   . ASN A 136 ? 0.3129 0.4435 0.7874 -0.0572 0.0703  -0.1016 137 ASN A C   
862   O  O   . ASN A 136 ? 0.2682 0.3876 0.7407 -0.0513 0.0729  -0.1008 137 ASN A O   
863   C  CB  . ASN A 136 ? 0.4162 0.5307 0.8985 -0.0635 0.0728  -0.1018 137 ASN A CB  
864   C  CG  . ASN A 136 ? 0.4108 0.5204 0.8986 -0.0717 0.0722  -0.1047 137 ASN A CG  
865   O  OD1 . ASN A 136 ? 0.4126 0.5176 0.9042 -0.0760 0.0720  -0.1133 137 ASN A OD1 
866   N  ND2 . ASN A 136 ? 0.3890 0.4999 0.8770 -0.0746 0.0722  -0.0982 137 ASN A ND2 
867   N  N   . ALA A 137 ? 0.3181 0.4636 0.7914 -0.0576 0.0664  -0.0983 138 ALA A N   
868   C  CA  . ALA A 137 ? 0.2940 0.4428 0.7635 -0.0510 0.0649  -0.0929 138 ALA A CA  
869   C  C   . ALA A 137 ? 0.2960 0.4396 0.7613 -0.0499 0.0673  -0.0979 138 ALA A C   
870   O  O   . ALA A 137 ? 0.2537 0.3913 0.7148 -0.0429 0.0683  -0.0941 138 ALA A O   
871   C  CB  . ALA A 137 ? 0.2715 0.4382 0.7448 -0.0534 0.0585  -0.0881 138 ALA A CB  
872   N  N   . ARG A 138 ? 0.2324 0.3784 0.6986 -0.0575 0.0686  -0.1073 139 ARG A N   
873   C  CA  . ARG A 138 ? 0.2978 0.4411 0.7607 -0.0579 0.0721  -0.1145 139 ARG A CA  
874   C  C   . ARG A 138 ? 0.3211 0.4461 0.7857 -0.0506 0.0767  -0.1164 139 ARG A C   
875   O  O   . ARG A 138 ? 0.3345 0.4559 0.7962 -0.0469 0.0791  -0.1184 139 ARG A O   
876   C  CB  . ARG A 138 ? 0.3008 0.4508 0.7643 -0.0689 0.0738  -0.1271 139 ARG A CB  
877   C  CG  . ARG A 138 ? 0.3791 0.5311 0.8383 -0.0712 0.0782  -0.1359 139 ARG A CG  
878   C  CD  . ARG A 138 ? 0.4282 0.5823 0.8880 -0.0815 0.0824  -0.1525 139 ARG A CD  
879   N  NE  . ARG A 138 ? 0.4927 0.6451 0.9509 -0.0816 0.0890  -0.1629 139 ARG A NE  
880   C  CZ  . ARG A 138 ? 0.5051 0.6606 0.9631 -0.0904 0.0946  -0.1801 139 ARG A CZ  
881   N  NH1 . ARG A 138 ? 0.5311 0.6904 0.9889 -0.1000 0.0938  -0.1884 139 ARG A NH1 
882   N  NH2 . ARG A 138 ? 0.5122 0.6672 0.9697 -0.0897 0.1013  -0.1898 139 ARG A NH2 
883   N  N   . ALA A 139 ? 0.3286 0.4428 0.7985 -0.0495 0.0772  -0.1152 140 ALA A N   
884   C  CA  . ALA A 139 ? 0.3428 0.4404 0.8168 -0.0438 0.0796  -0.1148 140 ALA A CA  
885   C  C   . ALA A 139 ? 0.3477 0.4423 0.8143 -0.0358 0.0789  -0.1054 140 ALA A C   
886   O  O   . ALA A 139 ? 0.4026 0.4886 0.8682 -0.0312 0.0804  -0.1063 140 ALA A O   
887   C  CB  . ALA A 139 ? 0.2264 0.3155 0.7080 -0.0463 0.0791  -0.1130 140 ALA A CB  
888   N  N   . PHE A 140 ? 0.3672 0.4688 0.8290 -0.0346 0.0764  -0.0972 141 PHE A N   
889   C  CA  . PHE A 140 ? 0.3721 0.4710 0.8268 -0.0279 0.0756  -0.0894 141 PHE A CA  
890   C  C   . PHE A 140 ? 0.3556 0.4590 0.8045 -0.0250 0.0746  -0.0890 141 PHE A C   
891   O  O   . PHE A 140 ? 0.3778 0.4732 0.8213 -0.0199 0.0752  -0.0864 141 PHE A O   
892   C  CB  . PHE A 140 ? 0.3271 0.4340 0.7810 -0.0278 0.0738  -0.0833 141 PHE A CB  
893   C  CG  . PHE A 140 ? 0.2888 0.3931 0.7473 -0.0318 0.0755  -0.0829 141 PHE A CG  
894   C  CD1 . PHE A 140 ? 0.2232 0.3175 0.6811 -0.0306 0.0778  -0.0799 141 PHE A CD1 
895   C  CD2 . PHE A 140 ? 0.3394 0.4524 0.8030 -0.0379 0.0744  -0.0847 141 PHE A CD2 
896   C  CE1 . PHE A 140 ? 0.2405 0.3341 0.7028 -0.0361 0.0791  -0.0784 141 PHE A CE1 
897   C  CE2 . PHE A 140 ? 0.3384 0.4496 0.8057 -0.0427 0.0759  -0.0837 141 PHE A CE2 
898   C  CZ  . PHE A 140 ? 0.1933 0.2950 0.6598 -0.0422 0.0784  -0.0802 141 PHE A CZ  
899   N  N   . ARG A 141 ? 0.2894 0.4066 0.7397 -0.0295 0.0726  -0.0911 142 ARG A N   
900   C  CA  . ARG A 141 ? 0.3286 0.4534 0.7754 -0.0293 0.0715  -0.0903 142 ARG A CA  
901   C  C   . ARG A 141 ? 0.3257 0.4422 0.7701 -0.0286 0.0760  -0.0974 142 ARG A C   
902   O  O   . ARG A 141 ? 0.3210 0.4352 0.7602 -0.0247 0.0762  -0.0946 142 ARG A O   
903   C  CB  . ARG A 141 ? 0.4009 0.5440 0.8514 -0.0378 0.0683  -0.0919 142 ARG A CB  
904   C  CG  . ARG A 141 ? 0.4495 0.6037 0.8976 -0.0413 0.0669  -0.0911 142 ARG A CG  
905   C  CD  . ARG A 141 ? 0.5717 0.7456 1.0243 -0.0508 0.0606  -0.0884 142 ARG A CD  
906   N  NE  . ARG A 141 ? 0.6721 0.8504 1.1316 -0.0462 0.0535  -0.0772 142 ARG A NE  
907   C  CZ  . ARG A 141 ? 0.7401 0.9337 1.2071 -0.0525 0.0459  -0.0725 142 ARG A CZ  
908   N  NH1 . ARG A 141 ? 0.7813 0.9877 1.2473 -0.0653 0.0440  -0.0778 142 ARG A NH1 
909   N  NH2 . ARG A 141 ? 0.7555 0.9517 1.2312 -0.0466 0.0398  -0.0633 142 ARG A NH2 
910   N  N   . ASP A 142 ? 0.3720 0.4839 0.8218 -0.0324 0.0795  -0.1071 143 ASP A N   
911   C  CA  . ASP A 142 ? 0.3871 0.4903 0.8389 -0.0314 0.0840  -0.1158 143 ASP A CA  
912   C  C   . ASP A 142 ? 0.3194 0.4066 0.7695 -0.0235 0.0835  -0.1100 143 ASP A C   
913   O  O   . ASP A 142 ? 0.2662 0.3490 0.7131 -0.0208 0.0851  -0.1116 143 ASP A O   
914   C  CB  . ASP A 142 ? 0.4795 0.5792 0.9420 -0.0366 0.0872  -0.1277 143 ASP A CB  
915   C  CG  . ASP A 142 ? 0.5785 0.6938 1.0404 -0.0466 0.0892  -0.1378 143 ASP A CG  
916   O  OD1 . ASP A 142 ? 0.6093 0.7369 1.0637 -0.0499 0.0898  -0.1383 143 ASP A OD1 
917   O  OD2 . ASP A 142 ? 0.6334 0.7491 1.1018 -0.0525 0.0898  -0.1452 143 ASP A OD2 
918   N  N   . LEU A 143 ? 0.2386 0.3182 0.6904 -0.0212 0.0814  -0.1033 144 LEU A N   
919   C  CA  . LEU A 143 ? 0.2729 0.3397 0.7226 -0.0160 0.0805  -0.0970 144 LEU A CA  
920   C  C   . LEU A 143 ? 0.3752 0.4437 0.8128 -0.0120 0.0789  -0.0904 144 LEU A C   
921   O  O   . LEU A 143 ? 0.3644 0.4248 0.7988 -0.0091 0.0789  -0.0893 144 LEU A O   
922   C  CB  . LEU A 143 ? 0.1802 0.2435 0.6333 -0.0165 0.0793  -0.0909 144 LEU A CB  
923   C  CG  . LEU A 143 ? 0.2867 0.3396 0.7385 -0.0132 0.0785  -0.0843 144 LEU A CG  
924   C  CD1 . LEU A 143 ? 0.3025 0.3442 0.7631 -0.0120 0.0785  -0.0879 144 LEU A CD1 
925   C  CD2 . LEU A 143 ? 0.2807 0.3337 0.7374 -0.0158 0.0786  -0.0796 144 LEU A CD2 
926   N  N   . TYR A 144 ? 0.3250 0.4045 0.7579 -0.0121 0.0769  -0.0859 145 TYR A N   
927   C  CA  . TYR A 144 ? 0.3042 0.3856 0.7290 -0.0084 0.0749  -0.0797 145 TYR A CA  
928   C  C   . TYR A 144 ? 0.2694 0.3543 0.6921 -0.0090 0.0763  -0.0833 145 TYR A C   
929   O  O   . TYR A 144 ? 0.2351 0.3151 0.6519 -0.0057 0.0757  -0.0798 145 TYR A O   
930   C  CB  . TYR A 144 ? 0.2203 0.3132 0.6463 -0.0085 0.0716  -0.0745 145 TYR A CB  
931   C  CG  . TYR A 144 ? 0.2312 0.3203 0.6563 -0.0063 0.0709  -0.0699 145 TYR A CG  
932   C  CD1 . TYR A 144 ? 0.2634 0.3558 0.6940 -0.0093 0.0716  -0.0713 145 TYR A CD1 
933   C  CD2 . TYR A 144 ? 0.1638 0.2472 0.5831 -0.0022 0.0701  -0.0653 145 TYR A CD2 
934   C  CE1 . TYR A 144 ? 0.2578 0.3492 0.6882 -0.0084 0.0722  -0.0685 145 TYR A CE1 
935   C  CE2 . TYR A 144 ? 0.1640 0.2462 0.5832 -0.0014 0.0708  -0.0633 145 TYR A CE2 
936   C  CZ  . TYR A 144 ? 0.2542 0.3410 0.6790 -0.0046 0.0722  -0.0651 145 TYR A CZ  
937   O  OH  . TYR A 144 ? 0.3025 0.3905 0.7280 -0.0048 0.0741  -0.0643 145 TYR A OH  
938   N  N   . SER A 145 ? 0.2330 0.3278 0.6606 -0.0143 0.0785  -0.0909 146 SER A N   
939   C  CA  . SER A 145 ? 0.3048 0.4056 0.7310 -0.0169 0.0816  -0.0965 146 SER A CA  
940   C  C   . SER A 145 ? 0.3356 0.4224 0.7613 -0.0138 0.0844  -0.1012 146 SER A C   
941   O  O   . SER A 145 ? 0.2431 0.3299 0.6643 -0.0126 0.0855  -0.1009 146 SER A O   
942   C  CB  . SER A 145 ? 0.2652 0.3805 0.6963 -0.0258 0.0846  -0.1063 146 SER A CB  
943   O  OG  . SER A 145 ? 0.3138 0.4454 0.7455 -0.0308 0.0805  -0.1004 146 SER A OG  
944   N  N   . GLU A 146 ? 0.3648 0.4402 0.7970 -0.0131 0.0848  -0.1048 147 GLU A N   
945   C  CA  . GLU A 146 ? 0.3760 0.4381 0.8122 -0.0110 0.0855  -0.1078 147 GLU A CA  
946   C  C   . GLU A 146 ? 0.3069 0.3608 0.7350 -0.0065 0.0819  -0.0973 147 GLU A C   
947   O  O   . GLU A 146 ? 0.2168 0.2667 0.6435 -0.0053 0.0822  -0.0981 147 GLU A O   
948   C  CB  . GLU A 146 ? 0.4782 0.5310 0.9278 -0.0121 0.0852  -0.1116 147 GLU A CB  
949   C  CG  . GLU A 146 ? 0.6291 0.6864 1.0901 -0.0168 0.0896  -0.1258 147 GLU A CG  
950   C  CD  . GLU A 146 ? 0.7044 0.7564 1.1740 -0.0174 0.0922  -0.1357 147 GLU A CD  
951   O  OE1 . GLU A 146 ? 0.7722 0.8122 1.2538 -0.0160 0.0893  -0.1341 147 GLU A OE1 
952   O  OE2 . GLU A 146 ? 0.7560 0.8178 1.2217 -0.0202 0.0969  -0.1447 147 GLU A OE2 
953   N  N   . LEU A 147 ? 0.2284 0.2812 0.6518 -0.0046 0.0790  -0.0885 148 LEU A N   
954   C  CA  . LEU A 147 ? 0.2027 0.2501 0.6181 -0.0014 0.0764  -0.0799 148 LEU A CA  
955   C  C   . LEU A 147 ? 0.2603 0.3130 0.6677 0.0001  0.0763  -0.0780 148 LEU A C   
956   O  O   . LEU A 147 ? 0.3104 0.3577 0.7134 0.0019  0.0753  -0.0749 148 LEU A O   
957   C  CB  . LEU A 147 ? 0.2681 0.3167 0.6810 -0.0006 0.0747  -0.0736 148 LEU A CB  
958   C  CG  . LEU A 147 ? 0.2477 0.2906 0.6681 -0.0020 0.0749  -0.0727 148 LEU A CG  
959   C  CD1 . LEU A 147 ? 0.2569 0.3050 0.6744 -0.0019 0.0748  -0.0683 148 LEU A CD1 
960   C  CD2 . LEU A 147 ? 0.2402 0.2735 0.6637 -0.0012 0.0739  -0.0699 148 LEU A CD2 
961   N  N   . ARG A 148 ? 0.3415 0.4061 0.7492 -0.0014 0.0772  -0.0796 149 ARG A N   
962   C  CA  . ARG A 148 ? 0.3784 0.4509 0.7825 -0.0010 0.0771  -0.0770 149 ARG A CA  
963   C  C   . ARG A 148 ? 0.3588 0.4312 0.7630 -0.0023 0.0806  -0.0833 149 ARG A C   
964   O  O   . ARG A 148 ? 0.3419 0.4118 0.7418 -0.0004 0.0800  -0.0798 149 ARG A O   
965   C  CB  . ARG A 148 ? 0.3339 0.4226 0.7428 -0.0044 0.0767  -0.0767 149 ARG A CB  
966   C  CG  . ARG A 148 ? 0.3508 0.4490 0.7602 -0.0044 0.0742  -0.0699 149 ARG A CG  
967   C  CD  . ARG A 148 ? 0.2887 0.4020 0.7059 -0.0082 0.0707  -0.0661 149 ARG A CD  
968   N  NE  . ARG A 148 ? 0.3453 0.4530 0.7639 -0.0041 0.0669  -0.0613 149 ARG A NE  
969   C  CZ  . ARG A 148 ? 0.3321 0.4463 0.7561 -0.0067 0.0655  -0.0624 149 ARG A CZ  
970   N  NH1 . ARG A 148 ? 0.3181 0.4442 0.7460 -0.0139 0.0671  -0.0679 149 ARG A NH1 
971   N  NH2 . ARG A 148 ? 0.2869 0.3967 0.7121 -0.0032 0.0630  -0.0588 149 ARG A NH2 
972   N  N   . LEU A 149 ? 0.3805 0.4557 0.7907 -0.0060 0.0846  -0.0937 150 LEU A N   
973   C  CA  . LEU A 149 ? 0.3962 0.4712 0.8087 -0.0077 0.0888  -0.1024 150 LEU A CA  
974   C  C   . LEU A 149 ? 0.3621 0.4225 0.7741 -0.0039 0.0861  -0.0990 150 LEU A C   
975   O  O   . LEU A 149 ? 0.2672 0.3278 0.6779 -0.0037 0.0875  -0.1004 150 LEU A O   
976   C  CB  . LEU A 149 ? 0.3829 0.4611 0.8042 -0.0123 0.0935  -0.1158 150 LEU A CB  
977   C  CG  . LEU A 149 ? 0.4571 0.5547 0.8786 -0.0198 0.0988  -0.1241 150 LEU A CG  
978   C  CD1 . LEU A 149 ? 0.4215 0.5203 0.8520 -0.0244 0.1028  -0.1376 150 LEU A CD1 
979   C  CD2 . LEU A 149 ? 0.4163 0.5238 0.8342 -0.0235 0.1037  -0.1288 150 LEU A CD2 
980   N  N   . TYR A 150 ? 0.3366 0.3867 0.7509 -0.0022 0.0824  -0.0942 151 TYR A N   
981   C  CA  . TYR A 150 ? 0.3443 0.3836 0.7602 -0.0002 0.0790  -0.0896 151 TYR A CA  
982   C  C   . TYR A 150 ? 0.3822 0.4209 0.7877 0.0024  0.0768  -0.0812 151 TYR A C   
983   O  O   . TYR A 150 ? 0.4041 0.4388 0.8103 0.0032  0.0756  -0.0800 151 TYR A O   
984   C  CB  . TYR A 150 ? 0.4046 0.4367 0.8265 -0.0002 0.0761  -0.0856 151 TYR A CB  
985   C  CG  . TYR A 150 ? 0.4546 0.4785 0.8824 0.0006  0.0726  -0.0807 151 TYR A CG  
986   C  CD1 . TYR A 150 ? 0.4884 0.5093 0.9291 -0.0003 0.0720  -0.0857 151 TYR A CD1 
987   C  CD2 . TYR A 150 ? 0.5262 0.5470 0.9490 0.0020  0.0698  -0.0718 151 TYR A CD2 
988   C  CE1 . TYR A 150 ? 0.5415 0.5570 0.9907 0.0004  0.0678  -0.0803 151 TYR A CE1 
989   C  CE2 . TYR A 150 ? 0.5999 0.6152 1.0301 0.0024  0.0666  -0.0673 151 TYR A CE2 
990   C  CZ  . TYR A 150 ? 0.6377 0.6505 1.0815 0.0017  0.0650  -0.0708 151 TYR A CZ  
991   O  OH  . TYR A 150 ? 0.6774 0.6863 1.1315 0.0021  0.0605  -0.0654 151 TYR A OH  
992   N  N   . TYR A 151 ? 0.3506 0.3936 0.7487 0.0035  0.0759  -0.0756 152 TYR A N   
993   C  CA  . TYR A 151 ? 0.4345 0.4772 0.8250 0.0058  0.0738  -0.0687 152 TYR A CA  
994   C  C   . TYR A 151 ? 0.4090 0.4577 0.7987 0.0054  0.0762  -0.0711 152 TYR A C   
995   O  O   . TYR A 151 ? 0.4269 0.4725 0.8137 0.0066  0.0751  -0.0681 152 TYR A O   
996   C  CB  . TYR A 151 ? 0.3430 0.3893 0.7299 0.0070  0.0721  -0.0632 152 TYR A CB  
997   C  CG  . TYR A 151 ? 0.2825 0.3298 0.6650 0.0089  0.0704  -0.0576 152 TYR A CG  
998   C  CD1 . TYR A 151 ? 0.2289 0.2692 0.6071 0.0103  0.0685  -0.0537 152 TYR A CD1 
999   C  CD2 . TYR A 151 ? 0.2262 0.2827 0.6114 0.0088  0.0707  -0.0565 152 TYR A CD2 
1000  C  CE1 . TYR A 151 ? 0.1784 0.2190 0.5544 0.0118  0.0670  -0.0496 152 TYR A CE1 
1001  C  CE2 . TYR A 151 ? 0.2092 0.2659 0.5940 0.0105  0.0687  -0.0510 152 TYR A CE2 
1002  C  CZ  . TYR A 151 ? 0.2505 0.2983 0.6302 0.0122  0.0670  -0.0481 152 TYR A CZ  
1003  O  OH  . TYR A 151 ? 0.1764 0.2238 0.5571 0.0136  0.0651  -0.0437 152 TYR A OH  
1004  N  N   . ARG A 152 ? 0.4828 0.5421 0.8761 0.0028  0.0799  -0.0770 153 ARG A N   
1005  C  CA  . ARG A 152 ? 0.4723 0.5415 0.8662 0.0008  0.0834  -0.0796 153 ARG A CA  
1006  C  C   . ARG A 152 ? 0.5381 0.6040 0.9345 0.0000  0.0863  -0.0866 153 ARG A C   
1007  O  O   . ARG A 152 ? 0.5726 0.6462 0.9693 -0.0019 0.0896  -0.0890 153 ARG A O   
1008  C  CB  . ARG A 152 ? 0.5419 0.6276 0.9399 -0.0044 0.0873  -0.0845 153 ARG A CB  
1009  C  CG  . ARG A 152 ? 0.5782 0.6712 0.9773 -0.0044 0.0834  -0.0759 153 ARG A CG  
1010  C  CD  . ARG A 152 ? 0.6520 0.7660 1.0561 -0.0128 0.0862  -0.0782 153 ARG A CD  
1011  N  NE  . ARG A 152 ? 0.7309 0.8524 1.1401 -0.0137 0.0805  -0.0690 153 ARG A NE  
1012  C  CZ  . ARG A 152 ? 0.7920 0.9223 1.2051 -0.0182 0.0795  -0.0706 153 ARG A CZ  
1013  N  NH1 . ARG A 152 ? 0.7984 0.9308 1.2103 -0.0222 0.0845  -0.0819 153 ARG A NH1 
1014  N  NH2 . ARG A 152 ? 0.8010 0.9379 1.2210 -0.0187 0.0728  -0.0613 153 ARG A NH2 
1015  N  N   . GLY A 153 ? 0.5138 0.5697 0.9144 0.0008  0.0848  -0.0896 154 GLY A N   
1016  C  CA  . GLY A 153 ? 0.5389 0.5910 0.9456 0.0004  0.0858  -0.0950 154 GLY A CA  
1017  C  C   . GLY A 153 ? 0.6207 0.6754 1.0383 -0.0028 0.0902  -0.1079 154 GLY A C   
1018  O  O   . GLY A 153 ? 0.5746 0.6258 1.0014 -0.0031 0.0904  -0.1131 154 GLY A O   
1019  N  N   . ALA A 154 ? 0.6282 0.6898 1.0465 -0.0056 0.0936  -0.1138 155 ALA A N   
1020  C  CA  . ALA A 154 ? 0.7518 0.8158 1.1812 -0.0094 0.0981  -0.1278 155 ALA A CA  
1021  C  C   . ALA A 154 ? 0.9309 0.9818 1.3725 -0.0076 0.0932  -0.1267 155 ALA A C   
1022  O  O   . ALA A 154 ? 0.8626 0.9055 1.3020 -0.0048 0.0874  -0.1161 155 ALA A O   
1023  C  CB  . ALA A 154 ? 0.6559 0.7291 1.0838 -0.0130 0.1014  -0.1326 155 ALA A CB  
1024  N  N   . ASN A 155 ? 1.1989 1.2496 1.6555 -0.0098 0.0956  -0.1380 156 ASN A N   
1025  C  CA  . ASN A 155 ? 1.2305 1.2712 1.7023 -0.0081 0.0897  -0.1345 156 ASN A CA  
1026  C  C   . ASN A 155 ? 1.2155 1.2522 1.6992 -0.0095 0.0880  -0.1368 156 ASN A C   
1027  O  O   . ASN A 155 ? 1.2433 1.2839 1.7388 -0.0131 0.0924  -0.1499 156 ASN A O   
1028  C  CB  . ASN A 155 ? 1.2651 1.3078 1.7521 -0.0094 0.0917  -0.1442 156 ASN A CB  
1029  N  N   . LEU A 156 ? 0.9957 1.0254 1.4768 -0.0071 0.0820  -0.1241 157 LEU A N   
1030  C  CA  . LEU A 156 ? 0.8904 0.9161 1.3809 -0.0080 0.0797  -0.1225 157 LEU A CA  
1031  C  C   . LEU A 156 ? 0.8355 0.8543 1.3267 -0.0054 0.0727  -0.1082 157 LEU A C   
1032  O  O   . LEU A 156 ? 0.8269 0.8449 1.3078 -0.0032 0.0709  -0.1013 157 LEU A O   
1033  C  CB  . LEU A 156 ? 0.8225 0.8521 1.3003 -0.0091 0.0830  -0.1235 157 LEU A CB  
1034  C  CG  . LEU A 156 ? 0.7493 0.7894 1.2198 -0.0119 0.0903  -0.1351 157 LEU A CG  
1035  C  CD1 . LEU A 156 ? 0.7285 0.7742 1.1823 -0.0108 0.0905  -0.1279 157 LEU A CD1 
1036  C  CD2 . LEU A 156 ? 0.7549 0.7975 1.2410 -0.0163 0.0942  -0.1495 157 LEU A CD2 
1037  N  N   . HIS A 157 ? 0.8577 0.8725 1.3623 -0.0059 0.0690  -0.1042 158 HIS A N   
1038  C  CA  . HIS A 157 ? 0.9178 0.9281 1.4187 -0.0042 0.0642  -0.0909 158 HIS A CA  
1039  C  C   . HIS A 157 ? 0.8451 0.8539 1.3506 -0.0057 0.0642  -0.0887 158 HIS A C   
1040  O  O   . HIS A 157 ? 0.8190 0.8290 1.3368 -0.0079 0.0659  -0.0964 158 HIS A O   
1041  C  CB  . HIS A 157 ? 1.0401 1.0475 1.5573 -0.0029 0.0575  -0.0847 158 HIS A CB  
1042  C  CG  . HIS A 157 ? 1.1318 1.1357 1.6504 -0.0019 0.0525  -0.0721 158 HIS A CG  
1043  N  ND1 . HIS A 157 ? 1.1834 1.1857 1.7132 -0.0029 0.0504  -0.0676 158 HIS A ND1 
1044  C  CD2 . HIS A 157 ? 1.1585 1.1609 1.6682 -0.0004 0.0501  -0.0636 158 HIS A CD2 
1045  C  CE1 . HIS A 157 ? 1.1949 1.1950 1.7240 -0.0020 0.0469  -0.0569 158 HIS A CE1 
1046  N  NE2 . HIS A 157 ? 1.1943 1.1945 1.7113 -0.0006 0.0467  -0.0547 158 HIS A NE2 
1047  N  N   . LEU A 158 ? 0.7932 0.7999 1.2894 -0.0047 0.0630  -0.0792 159 LEU A N   
1048  C  CA  . LEU A 158 ? 0.7777 0.7835 1.2754 -0.0059 0.0642  -0.0767 159 LEU A CA  
1049  C  C   . LEU A 158 ? 0.7473 0.7507 1.2708 -0.0077 0.0605  -0.0741 159 LEU A C   
1050  O  O   . LEU A 158 ? 0.7614 0.7648 1.2886 -0.0090 0.0624  -0.0755 159 LEU A O   
1051  C  CB  . LEU A 158 ? 0.7840 0.7898 1.2669 -0.0042 0.0646  -0.0681 159 LEU A CB  
1052  C  CG  . LEU A 158 ? 0.7802 0.7907 1.2407 -0.0021 0.0668  -0.0689 159 LEU A CG  
1053  C  CD1 . LEU A 158 ? 0.7988 0.8103 1.2480 -0.0006 0.0666  -0.0614 159 LEU A CD1 
1054  C  CD2 . LEU A 158 ? 0.7693 0.7857 1.2205 -0.0026 0.0705  -0.0754 159 LEU A CD2 
1055  N  N   . GLU A 159 ? 0.6473 0.6502 1.1874 -0.0062 0.0542  -0.0691 160 GLU A N   
1056  C  CA  . GLU A 159 ? 0.6258 0.6262 1.1862 -0.0045 0.0480  -0.0633 160 GLU A CA  
1057  C  C   . GLU A 159 ? 0.5747 0.5760 1.1464 -0.0054 0.0496  -0.0723 160 GLU A C   
1058  O  O   . GLU A 159 ? 0.5750 0.5716 1.1471 -0.0059 0.0493  -0.0702 160 GLU A O   
1059  C  CB  . GLU A 159 ? 0.5951 0.5907 1.1674 -0.0019 0.0385  -0.0565 160 GLU A CB  
1060  N  N   . GLU A 160 ? 0.5699 0.5747 1.1475 -0.0063 0.0515  -0.0831 161 GLU A N   
1061  C  CA  . GLU A 160 ? 0.5633 0.5702 1.1537 -0.0074 0.0538  -0.0943 161 GLU A CA  
1062  C  C   . GLU A 160 ? 0.5535 0.5647 1.1318 -0.0108 0.0620  -0.1019 161 GLU A C   
1063  O  O   . GLU A 160 ? 0.6182 0.6296 1.2050 -0.0111 0.0630  -0.1059 161 GLU A O   
1064  C  CB  . GLU A 160 ? 0.6631 0.6732 1.2624 -0.0079 0.0549  -0.1052 161 GLU A CB  
1065  C  CG  . GLU A 160 ? 0.7956 0.8027 1.4025 -0.0051 0.0479  -0.0985 161 GLU A CG  
1066  C  CD  . GLU A 160 ? 0.9278 0.9350 1.5131 -0.0051 0.0498  -0.0935 161 GLU A CD  
1067  O  OE1 . GLU A 160 ? 0.9541 0.9608 1.5197 -0.0060 0.0532  -0.0890 161 GLU A OE1 
1068  O  OE2 . GLU A 160 ? 0.9710 0.9784 1.5595 -0.0040 0.0479  -0.0946 161 GLU A OE2 
1069  N  N   . THR A 161 ? 0.5068 0.5181 1.0612 -0.0124 0.0665  -0.1033 162 THR A N   
1070  C  CA  . THR A 161 ? 0.4253 0.4377 0.9641 -0.0147 0.0725  -0.1100 162 THR A CA  
1071  C  C   . THR A 161 ? 0.3676 0.3773 0.9034 -0.0141 0.0722  -0.1034 162 THR A C   
1072  O  O   . THR A 161 ? 0.3380 0.3490 0.8753 -0.0154 0.0754  -0.1101 162 THR A O   
1073  C  CB  . THR A 161 ? 0.3952 0.4097 0.9083 -0.0129 0.0752  -0.1092 162 THR A CB  
1074  O  OG1 . THR A 161 ? 0.4152 0.4331 0.9288 -0.0133 0.0772  -0.1178 162 THR A OG1 
1075  C  CG2 . THR A 161 ? 0.4581 0.4793 0.9552 -0.0130 0.0792  -0.1118 162 THR A CG2 
1076  N  N   . LEU A 162 ? 0.2249 0.2310 0.7575 -0.0121 0.0691  -0.0912 163 LEU A N   
1077  C  CA  . LEU A 162 ? 0.3288 0.3336 0.8622 -0.0111 0.0696  -0.0845 163 LEU A CA  
1078  C  C   . LEU A 162 ? 0.2877 0.2891 0.8336 -0.0146 0.0645  -0.0814 163 LEU A C   
1079  O  O   . LEU A 162 ? 0.3349 0.3370 0.8732 -0.0209 0.0645  -0.0796 163 LEU A O   
1080  C  CB  . LEU A 162 ? 0.3235 0.3285 0.8482 -0.0108 0.0672  -0.0725 163 LEU A CB  
1081  C  CG  . LEU A 162 ? 0.2879 0.2979 0.7892 -0.0092 0.0699  -0.0713 163 LEU A CG  
1082  C  CD1 . LEU A 162 ? 0.1841 0.1926 0.6840 -0.0081 0.0676  -0.0617 163 LEU A CD1 
1083  C  CD2 . LEU A 162 ? 0.2918 0.3127 0.7763 -0.0108 0.0736  -0.0721 163 LEU A CD2 
1084  N  N   . ALA A 163 ? 0.3279 0.3239 0.8882 -0.0121 0.0584  -0.0796 164 ALA A N   
1085  C  CA  . ALA A 163 ? 0.2815 0.2672 0.8494 -0.0155 0.0512  -0.0762 164 ALA A CA  
1086  C  C   . ALA A 163 ? 0.3683 0.3573 0.9402 -0.0178 0.0559  -0.0887 164 ALA A C   
1087  O  O   . ALA A 163 ? 0.4577 0.4417 1.0247 -0.0240 0.0538  -0.0856 164 ALA A O   
1088  C  CB  . ALA A 163 ? 0.3514 0.3324 0.9362 -0.0116 0.0435  -0.0739 164 ALA A CB  
1089  N  N   . GLU A 164 ? 0.3111 0.3102 0.8908 -0.0147 0.0623  -0.1027 165 GLU A N   
1090  C  CA  . GLU A 164 ? 0.3599 0.3636 0.9417 -0.0176 0.0678  -0.1167 165 GLU A CA  
1091  C  C   . GLU A 164 ? 0.4467 0.4529 1.0105 -0.0230 0.0711  -0.1154 165 GLU A C   
1092  O  O   . GLU A 164 ? 0.4570 0.4616 1.0192 -0.0288 0.0702  -0.1174 165 GLU A O   
1093  C  CB  . GLU A 164 ? 0.4210 0.4379 1.0094 -0.0167 0.0749  -0.1311 165 GLU A CB  
1094  C  CG  . GLU A 164 ? 0.4469 0.4696 1.0345 -0.0206 0.0817  -0.1473 165 GLU A CG  
1095  C  CD  . GLU A 164 ? 0.5708 0.5887 1.1736 -0.0221 0.0794  -0.1548 165 GLU A CD  
1096  O  OE1 . GLU A 164 ? 0.5863 0.5974 1.2033 -0.0191 0.0726  -0.1488 165 GLU A OE1 
1097  O  OE2 . GLU A 164 ? 0.5624 0.5829 1.1629 -0.0267 0.0837  -0.1667 165 GLU A OE2 
1098  N  N   . PHE A 165 ? 0.4007 0.4127 0.9509 -0.0218 0.0740  -0.1112 166 PHE A N   
1099  C  CA  . PHE A 165 ? 0.3974 0.4187 0.9294 -0.0267 0.0758  -0.1073 166 PHE A CA  
1100  C  C   . PHE A 165 ? 0.3080 0.3263 0.8372 -0.0331 0.0719  -0.0979 166 PHE A C   
1101  O  O   . PHE A 165 ? 0.2822 0.3069 0.8062 -0.0387 0.0729  -0.1003 166 PHE A O   
1102  C  CB  . PHE A 165 ? 0.2610 0.2877 0.7776 -0.0230 0.0771  -0.1003 166 PHE A CB  
1103  C  CG  . PHE A 165 ? 0.2434 0.2802 0.7446 -0.0261 0.0774  -0.0931 166 PHE A CG  
1104  C  CD1 . PHE A 165 ? 0.1965 0.2452 0.6882 -0.0282 0.0792  -0.0973 166 PHE A CD1 
1105  C  CD2 . PHE A 165 ? 0.2090 0.2446 0.7064 -0.0275 0.0758  -0.0824 166 PHE A CD2 
1106  C  CE1 . PHE A 165 ? 0.2566 0.3149 0.7380 -0.0302 0.0790  -0.0912 166 PHE A CE1 
1107  C  CE2 . PHE A 165 ? 0.2172 0.2632 0.7028 -0.0304 0.0771  -0.0780 166 PHE A CE2 
1108  C  CZ  . PHE A 165 ? 0.2865 0.3433 0.7652 -0.0309 0.0785  -0.0825 166 PHE A CZ  
1109  N  N   . TRP A 166 ? 0.3625 0.3714 0.8940 -0.0333 0.0669  -0.0868 167 TRP A N   
1110  C  CA  . TRP A 166 ? 0.3245 0.3298 0.8502 -0.0412 0.0629  -0.0764 167 TRP A CA  
1111  C  C   . TRP A 166 ? 0.4064 0.4028 0.9411 -0.0454 0.0588  -0.0793 167 TRP A C   
1112  O  O   . TRP A 166 ? 0.4058 0.4040 0.9346 -0.0533 0.0580  -0.0760 167 TRP A O   
1113  C  CB  . TRP A 166 ? 0.3389 0.3364 0.8620 -0.0421 0.0577  -0.0632 167 TRP A CB  
1114  C  CG  . TRP A 166 ? 0.3899 0.3974 0.9016 -0.0404 0.0619  -0.0593 167 TRP A CG  
1115  C  CD1 . TRP A 166 ? 0.3653 0.3710 0.8780 -0.0344 0.0616  -0.0571 167 TRP A CD1 
1116  C  CD2 . TRP A 166 ? 0.4022 0.4238 0.9004 -0.0441 0.0670  -0.0578 167 TRP A CD2 
1117  N  NE1 . TRP A 166 ? 0.3188 0.3358 0.8187 -0.0344 0.0663  -0.0546 167 TRP A NE1 
1118  C  CE2 . TRP A 166 ? 0.2842 0.3113 0.7755 -0.0397 0.0697  -0.0553 167 TRP A CE2 
1119  C  CE3 . TRP A 166 ? 0.3088 0.3396 0.8012 -0.0503 0.0694  -0.0589 167 TRP A CE3 
1120  C  CZ2 . TRP A 166 ? 0.2751 0.3156 0.7539 -0.0406 0.0746  -0.0546 167 TRP A CZ2 
1121  C  CZ3 . TRP A 166 ? 0.3257 0.3709 0.8070 -0.0511 0.0742  -0.0578 167 TRP A CZ3 
1122  C  CH2 . TRP A 166 ? 0.3008 0.3503 0.7755 -0.0459 0.0768  -0.0561 167 TRP A CH2 
1123  N  N   . ALA A 167 ? 0.3902 0.3781 0.9400 -0.0402 0.0563  -0.0859 168 ALA A N   
1124  C  CA  . ALA A 167 ? 0.3531 0.3330 0.9133 -0.0431 0.0528  -0.0908 168 ALA A CA  
1125  C  C   . ALA A 167 ? 0.3495 0.3392 0.9050 -0.0479 0.0586  -0.1017 168 ALA A C   
1126  O  O   . ALA A 167 ? 0.4094 0.3977 0.9606 -0.0557 0.0564  -0.0982 168 ALA A O   
1127  C  CB  . ALA A 167 ? 0.3567 0.3315 0.9361 -0.0356 0.0511  -0.0990 168 ALA A CB  
1128  N  N   . ARG A 168 ? 0.3764 0.3766 0.9315 -0.0443 0.0654  -0.1141 169 ARG A N   
1129  C  CA  . ARG A 168 ? 0.4058 0.4165 0.9553 -0.0496 0.0699  -0.1248 169 ARG A CA  
1130  C  C   . ARG A 168 ? 0.4827 0.5035 1.0176 -0.0559 0.0700  -0.1163 169 ARG A C   
1131  O  O   . ARG A 168 ? 0.4766 0.5016 1.0089 -0.0628 0.0697  -0.1193 169 ARG A O   
1132  C  CB  . ARG A 168 ? 0.3764 0.3976 0.9247 -0.0464 0.0764  -0.1374 169 ARG A CB  
1133  C  CG  . ARG A 168 ? 0.4731 0.4890 1.0372 -0.0401 0.0782  -0.1475 169 ARG A CG  
1134  C  CD  . ARG A 168 ? 0.5021 0.5132 1.0796 -0.0425 0.0780  -0.1591 169 ARG A CD  
1135  N  NE  . ARG A 168 ? 0.5133 0.5102 1.1011 -0.0418 0.0700  -0.1491 169 ARG A NE  
1136  C  CZ  . ARG A 168 ? 0.5042 0.4932 1.1068 -0.0355 0.0652  -0.1444 169 ARG A CZ  
1137  N  NH1 . ARG A 168 ? 0.4665 0.4621 1.0766 -0.0293 0.0685  -0.1495 169 ARG A NH1 
1138  N  NH2 . ARG A 168 ? 0.4594 0.4351 1.0696 -0.0366 0.0563  -0.1340 169 ARG A NH2 
1139  N  N   . LEU A 169 ? 0.4216 0.4472 0.9476 -0.0534 0.0704  -0.1062 170 LEU A N   
1140  C  CA  . LEU A 169 ? 0.4261 0.4636 0.9400 -0.0580 0.0711  -0.0988 170 LEU A CA  
1141  C  C   . LEU A 169 ? 0.4451 0.4765 0.9591 -0.0661 0.0674  -0.0912 170 LEU A C   
1142  O  O   . LEU A 169 ? 0.3925 0.4335 0.9014 -0.0723 0.0681  -0.0907 170 LEU A O   
1143  C  CB  . LEU A 169 ? 0.3789 0.4222 0.8843 -0.0532 0.0728  -0.0908 170 LEU A CB  
1144  C  CG  . LEU A 169 ? 0.3422 0.4000 0.8367 -0.0563 0.0745  -0.0855 170 LEU A CG  
1145  C  CD1 . LEU A 169 ? 0.2891 0.3603 0.7802 -0.0565 0.0757  -0.0925 170 LEU A CD1 
1146  C  CD2 . LEU A 169 ? 0.3790 0.4405 0.8657 -0.0514 0.0763  -0.0788 170 LEU A CD2 
1147  N  N   . LEU A 170 ? 0.4890 0.5048 1.0088 -0.0665 0.0626  -0.0844 171 LEU A N   
1148  C  CA  . LEU A 170 ? 0.4204 0.4286 0.9392 -0.0756 0.0577  -0.0757 171 LEU A CA  
1149  C  C   . LEU A 170 ? 0.4769 0.4821 1.0022 -0.0801 0.0564  -0.0840 171 LEU A C   
1150  O  O   . LEU A 170 ? 0.4341 0.4431 0.9547 -0.0889 0.0556  -0.0806 171 LEU A O   
1151  C  CB  . LEU A 170 ? 0.3932 0.3843 0.9166 -0.0754 0.0506  -0.0656 171 LEU A CB  
1152  C  CG  . LEU A 170 ? 0.3966 0.3770 0.9188 -0.0859 0.0436  -0.0553 171 LEU A CG  
1153  C  CD1 . LEU A 170 ? 0.4097 0.4026 0.9174 -0.0963 0.0466  -0.0475 171 LEU A CD1 
1154  C  CD2 . LEU A 170 ? 0.4120 0.3754 0.9389 -0.0852 0.0346  -0.0442 171 LEU A CD2 
1155  N  N   . GLU A 171 ? 0.5250 0.5246 1.0612 -0.0745 0.0568  -0.0959 172 GLU A N   
1156  C  CA  . GLU A 171 ? 0.5032 0.5014 1.0456 -0.0786 0.0568  -0.1066 172 GLU A CA  
1157  C  C   . GLU A 171 ? 0.5415 0.5570 1.0740 -0.0846 0.0607  -0.1107 172 GLU A C   
1158  O  O   . GLU A 171 ? 0.5958 0.6121 1.1264 -0.0930 0.0586  -0.1085 172 GLU A O   
1159  C  CB  . GLU A 171 ? 0.5232 0.5181 1.0776 -0.0718 0.0593  -0.1216 172 GLU A CB  
1160  C  CG  . GLU A 171 ? 0.5546 0.5344 1.1232 -0.0649 0.0546  -0.1190 172 GLU A CG  
1161  C  CD  . GLU A 171 ? 0.6084 0.5891 1.1907 -0.0586 0.0587  -0.1358 172 GLU A CD  
1162  O  OE1 . GLU A 171 ? 0.6357 0.6293 1.2125 -0.0591 0.0660  -0.1481 172 GLU A OE1 
1163  O  OE2 . GLU A 171 ? 0.6417 0.6118 1.2407 -0.0539 0.0544  -0.1366 172 GLU A OE2 
1164  N  N   . ARG A 172 ? 0.5022 0.5319 1.0288 -0.0806 0.0656  -0.1158 173 ARG A N   
1165  C  CA  . ARG A 172 ? 0.4887 0.5365 1.0069 -0.0852 0.0678  -0.1189 173 ARG A CA  
1166  C  C   . ARG A 172 ? 0.4673 0.5232 0.9787 -0.0907 0.0666  -0.1076 173 ARG A C   
1167  O  O   . ARG A 172 ? 0.4398 0.5035 0.9497 -0.0980 0.0657  -0.1091 173 ARG A O   
1168  C  CB  . ARG A 172 ? 0.5268 0.5876 1.0391 -0.0795 0.0713  -0.1226 173 ARG A CB  
1169  C  CG  . ARG A 172 ? 0.5854 0.6442 1.1023 -0.0772 0.0739  -0.1364 173 ARG A CG  
1170  C  CD  . ARG A 172 ? 0.6345 0.7068 1.1436 -0.0730 0.0766  -0.1376 173 ARG A CD  
1171  N  NE  . ARG A 172 ? 0.6942 0.7845 1.1940 -0.0775 0.0752  -0.1348 173 ARG A NE  
1172  C  CZ  . ARG A 172 ? 0.7278 0.8289 1.2247 -0.0847 0.0748  -0.1434 173 ARG A CZ  
1173  N  NH1 . ARG A 172 ? 0.7643 0.8600 1.2653 -0.0885 0.0772  -0.1573 173 ARG A NH1 
1174  N  NH2 . ARG A 172 ? 0.7046 0.8224 1.1950 -0.0884 0.0718  -0.1385 173 ARG A NH2 
1175  N  N   . LEU A 173 ? 0.4465 0.5016 0.9539 -0.0878 0.0670  -0.0972 174 LEU A N   
1176  C  CA  . LEU A 173 ? 0.4742 0.5387 0.9749 -0.0934 0.0675  -0.0879 174 LEU A CA  
1177  C  C   . LEU A 173 ? 0.5143 0.5708 1.0170 -0.1037 0.0641  -0.0836 174 LEU A C   
1178  O  O   . LEU A 173 ? 0.5300 0.5979 1.0293 -0.1109 0.0647  -0.0814 174 LEU A O   
1179  C  CB  . LEU A 173 ? 0.4354 0.4996 0.9309 -0.0895 0.0692  -0.0791 174 LEU A CB  
1180  C  CG  . LEU A 173 ? 0.3750 0.4513 0.8659 -0.0807 0.0728  -0.0810 174 LEU A CG  
1181  C  CD1 . LEU A 173 ? 0.2950 0.3688 0.7811 -0.0775 0.0743  -0.0734 174 LEU A CD1 
1182  C  CD2 . LEU A 173 ? 0.3773 0.4725 0.8646 -0.0822 0.0743  -0.0822 174 LEU A CD2 
1183  N  N   . PHE A 174 ? 0.5559 0.5930 1.0648 -0.1044 0.0598  -0.0823 175 PHE A N   
1184  C  CA  . PHE A 174 ? 0.5805 0.6075 1.0911 -0.1145 0.0550  -0.0771 175 PHE A CA  
1185  C  C   . PHE A 174 ? 0.5538 0.5845 1.0685 -0.1190 0.0548  -0.0868 175 PHE A C   
1186  O  O   . PHE A 174 ? 0.5703 0.6039 1.0828 -0.1289 0.0531  -0.0831 175 PHE A O   
1187  C  CB  . PHE A 174 ? 0.6104 0.6146 1.1282 -0.1131 0.0487  -0.0724 175 PHE A CB  
1188  C  CG  . PHE A 174 ? 0.6334 0.6262 1.1510 -0.1243 0.0424  -0.0632 175 PHE A CG  
1189  C  CD1 . PHE A 174 ? 0.6341 0.6289 1.1414 -0.1335 0.0410  -0.0491 175 PHE A CD1 
1190  C  CD2 . PHE A 174 ? 0.6099 0.5906 1.1372 -0.1267 0.0380  -0.0690 175 PHE A CD2 
1191  C  CE1 . PHE A 174 ? 0.6670 0.6514 1.1724 -0.1457 0.0348  -0.0397 175 PHE A CE1 
1192  C  CE2 . PHE A 174 ? 0.6128 0.5822 1.1399 -0.1376 0.0315  -0.0597 175 PHE A CE2 
1193  C  CZ  . PHE A 174 ? 0.6154 0.5864 1.1310 -0.1474 0.0296  -0.0444 175 PHE A CZ  
1194  N  N   . LYS A 175 ? 0.6006 0.6320 1.1205 -0.1131 0.0565  -0.0997 176 LYS A N   
1195  C  CA  . LYS A 175 ? 0.6206 0.6581 1.1425 -0.1183 0.0566  -0.1103 176 LYS A CA  
1196  C  C   . LYS A 175 ? 0.6956 0.7544 1.2099 -0.1234 0.0585  -0.1079 176 LYS A C   
1197  O  O   . LYS A 175 ? 0.6852 0.7482 1.1998 -0.1320 0.0567  -0.1091 176 LYS A O   
1198  C  CB  . LYS A 175 ? 0.5859 0.6243 1.1118 -0.1124 0.0593  -0.1250 176 LYS A CB  
1199  C  CG  . LYS A 175 ? 0.6223 0.6414 1.1598 -0.1081 0.0578  -0.1317 176 LYS A CG  
1200  C  CD  . LYS A 175 ? 0.6472 0.6713 1.1876 -0.1048 0.0622  -0.1488 176 LYS A CD  
1201  C  CE  . LYS A 175 ? 0.6777 0.7155 1.2123 -0.1135 0.0633  -0.1580 176 LYS A CE  
1202  N  NZ  . LYS A 175 ? 0.6966 0.7402 1.2315 -0.1130 0.0678  -0.1753 176 LYS A NZ  
1203  N  N   . GLN A 176 ? 0.7805 0.8530 1.2893 -0.1177 0.0617  -0.1045 177 GLN A N   
1204  C  CA  . GLN A 176 ? 0.8019 0.8958 1.3063 -0.1202 0.0628  -0.1026 177 GLN A CA  
1205  C  C   . GLN A 176 ? 0.7818 0.8803 1.2840 -0.1276 0.0629  -0.0930 177 GLN A C   
1206  O  O   . GLN A 176 ? 0.8283 0.9414 1.3306 -0.1334 0.0626  -0.0929 177 GLN A O   
1207  C  CB  . GLN A 176 ? 0.8694 0.9750 1.3699 -0.1110 0.0655  -0.1015 177 GLN A CB  
1208  C  CG  . GLN A 176 ? 0.9497 1.0772 1.4487 -0.1119 0.0650  -0.1011 177 GLN A CG  
1209  C  CD  . GLN A 176 ? 0.9891 1.1261 1.4851 -0.1024 0.0664  -0.0987 177 GLN A CD  
1210  O  OE1 . GLN A 176 ? 0.9892 1.1177 1.4828 -0.0957 0.0687  -0.0961 177 GLN A OE1 
1211  N  NE2 . GLN A 176 ? 1.0061 1.1606 1.5030 -0.1021 0.0640  -0.0989 177 GLN A NE2 
1212  N  N   . LEU A 177 ? 0.7249 0.8120 1.2252 -0.1285 0.0631  -0.0846 178 LEU A N   
1213  C  CA  . LEU A 177 ? 0.7110 0.8019 1.2076 -0.1383 0.0634  -0.0755 178 LEU A CA  
1214  C  C   . LEU A 177 ? 0.7374 0.8221 1.2371 -0.1492 0.0594  -0.0761 178 LEU A C   
1215  O  O   . LEU A 177 ? 0.7429 0.8386 1.2406 -0.1584 0.0601  -0.0720 178 LEU A O   
1216  C  CB  . LEU A 177 ? 0.7152 0.7942 1.2073 -0.1392 0.0631  -0.0658 178 LEU A CB  
1217  C  CG  . LEU A 177 ? 0.7130 0.8057 1.1981 -0.1371 0.0684  -0.0607 178 LEU A CG  
1218  C  CD1 . LEU A 177 ? 0.7267 0.8256 1.2127 -0.1236 0.0713  -0.0664 178 LEU A CD1 
1219  C  CD2 . LEU A 177 ? 0.7385 0.8199 1.2174 -0.1433 0.0671  -0.0499 178 LEU A CD2 
1220  N  N   . HIS A 178 ? 0.7026 0.7700 1.2080 -0.1481 0.0555  -0.0818 179 HIS A N   
1221  C  CA  . HIS A 178 ? 0.6901 0.7482 1.1992 -0.1579 0.0512  -0.0829 179 HIS A CA  
1222  C  C   . HIS A 178 ? 0.6696 0.7288 1.1842 -0.1565 0.0504  -0.0966 179 HIS A C   
1223  O  O   . HIS A 178 ? 0.6280 0.6707 1.1488 -0.1535 0.0482  -0.1036 179 HIS A O   
1224  C  CB  . HIS A 178 ? 0.7062 0.7396 1.2181 -0.1603 0.0458  -0.0762 179 HIS A CB  
1225  C  CG  . HIS A 178 ? 0.7249 0.7563 1.2293 -0.1643 0.0455  -0.0620 179 HIS A CG  
1226  N  ND1 . HIS A 178 ? 0.7207 0.7712 1.2168 -0.1703 0.0500  -0.0559 179 HIS A ND1 
1227  C  CD2 . HIS A 178 ? 0.7465 0.7602 1.2504 -0.1638 0.0411  -0.0530 179 HIS A CD2 
1228  C  CE1 . HIS A 178 ? 0.7285 0.7735 1.2176 -0.1747 0.0492  -0.0444 179 HIS A CE1 
1229  N  NE2 . HIS A 178 ? 0.7399 0.7622 1.2330 -0.1710 0.0431  -0.0416 179 HIS A NE2 
1230  N  N   . PRO A 179 ? 0.6730 0.7525 1.1858 -0.1591 0.0520  -0.1009 180 PRO A N   
1231  C  CA  . PRO A 179 ? 0.7658 0.8484 1.2816 -0.1613 0.0506  -0.1133 180 PRO A CA  
1232  C  C   . PRO A 179 ? 0.8987 0.9693 1.4186 -0.1714 0.0466  -0.1151 180 PRO A C   
1233  O  O   . PRO A 179 ? 0.9258 0.9902 1.4493 -0.1729 0.0453  -0.1268 180 PRO A O   
1234  C  CB  . PRO A 179 ? 0.7080 0.8165 1.2208 -0.1627 0.0516  -0.1132 180 PRO A CB  
1235  C  CG  . PRO A 179 ? 0.6707 0.7885 1.1804 -0.1572 0.0549  -0.1034 180 PRO A CG  
1236  C  CD  . PRO A 179 ? 0.6780 0.7794 1.1866 -0.1600 0.0549  -0.0948 180 PRO A CD  
1237  N  N   . GLN A 180 ? 0.9945 1.0621 1.5131 -0.1792 0.0449  -0.1040 181 GLN A N   
1238  C  CA  . GLN A 180 ? 1.0541 1.1104 1.5761 -0.1901 0.0405  -0.1032 181 GLN A CA  
1239  C  C   . GLN A 180 ? 1.0885 1.1188 1.6178 -0.1872 0.0369  -0.1084 181 GLN A C   
1240  O  O   . GLN A 180 ? 1.1395 1.1624 1.6741 -0.1917 0.0344  -0.1174 181 GLN A O   
1241  C  CB  . GLN A 180 ? 1.0907 1.1482 1.6084 -0.1996 0.0395  -0.0886 181 GLN A CB  
1242  N  N   . LEU A 181 ? 1.0503 1.0674 1.5808 -0.1796 0.0366  -0.1031 182 LEU A N   
1243  C  CA  . LEU A 181 ? 1.0284 1.0214 1.5688 -0.1751 0.0326  -0.1071 182 LEU A CA  
1244  C  C   . LEU A 181 ? 0.9856 0.9788 1.5311 -0.1633 0.0365  -0.1213 182 LEU A C   
1245  O  O   . LEU A 181 ? 1.0064 1.0079 1.5477 -0.1552 0.0404  -0.1201 182 LEU A O   
1246  C  CB  . LEU A 181 ? 1.0213 0.9987 1.5615 -0.1748 0.0282  -0.0918 182 LEU A CB  
1247  N  N   . LEU A 182 ? 1.0074 0.9923 1.5619 -0.1630 0.0360  -0.1355 183 LEU A N   
1248  C  CA  . LEU A 182 ? 0.9945 0.9787 1.5549 -0.1532 0.0403  -0.1503 183 LEU A CA  
1249  C  C   . LEU A 182 ? 0.9899 0.9546 1.5619 -0.1442 0.0373  -0.1461 183 LEU A C   
1250  O  O   . LEU A 182 ? 0.9952 0.9421 1.5769 -0.1467 0.0310  -0.1412 183 LEU A O   
1251  C  CB  . LEU A 182 ? 1.0194 1.0042 1.5848 -0.1574 0.0419  -0.1686 183 LEU A CB  
1252  C  CG  . LEU A 182 ? 1.0223 1.0244 1.5815 -0.1552 0.0486  -0.1840 183 LEU A CG  
1253  C  CD1 . LEU A 182 ? 0.9908 1.0140 1.5360 -0.1562 0.0503  -0.1756 183 LEU A CD1 
1254  C  CD2 . LEU A 182 ? 1.0261 1.0320 1.5859 -0.1637 0.0496  -0.2002 183 LEU A CD2 
1255  N  N   . LEU A 183 ? 0.9727 0.9413 1.5443 -0.1341 0.0410  -0.1473 184 LEU A N   
1256  C  CA  . LEU A 183 ? 0.9616 0.9148 1.5431 -0.1256 0.0372  -0.1399 184 LEU A CA  
1257  C  C   . LEU A 183 ? 0.9591 0.9101 1.5533 -0.1149 0.0412  -0.1548 184 LEU A C   
1258  O  O   . LEU A 183 ? 0.9470 0.9076 1.5368 -0.1080 0.0462  -0.1573 184 LEU A O   
1259  C  CB  . LEU A 183 ? 0.9001 0.8590 1.4701 -0.1236 0.0371  -0.1240 184 LEU A CB  
1260  N  N   . PRO A 184 ? 1.0238 0.9631 1.6351 -0.1137 0.0393  -0.1653 185 PRO A N   
1261  C  CA  . PRO A 184 ? 1.0548 0.9918 1.6832 -0.1037 0.0428  -0.1794 185 PRO A CA  
1262  C  C   . PRO A 184 ? 1.1069 1.0325 1.7465 -0.0946 0.0368  -0.1669 185 PRO A C   
1263  O  O   . PRO A 184 ? 1.1333 1.0494 1.7679 -0.0977 0.0289  -0.1477 185 PRO A O   
1264  C  CB  . PRO A 184 ? 1.0317 0.9599 1.6761 -0.1072 0.0414  -0.1922 185 PRO A CB  
1265  C  CG  . PRO A 184 ? 1.0318 0.9483 1.6721 -0.1163 0.0327  -0.1770 185 PRO A CG  
1266  C  CD  . PRO A 184 ? 0.9981 0.9271 1.6147 -0.1227 0.0341  -0.1651 185 PRO A CD  
1267  N  N   . ASP A 185 ? 1.1378 1.0662 1.7917 -0.0848 0.0407  -0.1775 186 ASP A N   
1268  C  CA  . ASP A 185 ? 1.1544 1.0743 1.8213 -0.0758 0.0347  -0.1668 186 ASP A CA  
1269  C  C   . ASP A 185 ? 1.1703 1.0703 1.8506 -0.0777 0.0220  -0.1530 186 ASP A C   
1270  O  O   . ASP A 185 ? 1.1582 1.0502 1.8294 -0.0803 0.0141  -0.1327 186 ASP A O   
1271  C  CB  . ASP A 185 ? 1.1771 1.1041 1.8635 -0.0664 0.0407  -0.1839 186 ASP A CB  
1272  C  CG  . ASP A 185 ? 1.1885 1.1343 1.8636 -0.0678 0.0536  -0.2024 186 ASP A CG  
1273  O  OD1 . ASP A 185 ? 1.1857 1.1406 1.8378 -0.0713 0.0570  -0.1973 186 ASP A OD1 
1274  O  OD2 . ASP A 185 ? 1.1966 1.1488 1.8862 -0.0663 0.0602  -0.2222 186 ASP A OD2 
1275  N  N   . GLY A 192 ? 0.9137 0.8225 1.5724 -0.0605 0.0174  -0.1156 193 GLY A N   
1276  C  CA  . GLY A 192 ? 0.9367 0.8327 1.6036 -0.0584 0.0055  -0.0985 193 GLY A CA  
1277  C  C   . GLY A 192 ? 0.9337 0.8217 1.5802 -0.0687 -0.0015 -0.0775 193 GLY A C   
1278  O  O   . GLY A 192 ? 0.9472 0.8216 1.5974 -0.0758 -0.0108 -0.0678 193 GLY A O   
1279  N  N   . LYS A 193 ? 0.9816 0.8792 1.6063 -0.0708 0.0035  -0.0711 194 LYS A N   
1280  C  CA  . LYS A 193 ? 1.0429 0.9365 1.6479 -0.0820 -0.0016 -0.0521 194 LYS A CA  
1281  C  C   . LYS A 193 ? 1.1195 1.0101 1.7211 -0.0788 -0.0072 -0.0385 194 LYS A C   
1282  O  O   . LYS A 193 ? 1.0269 0.9288 1.6205 -0.0736 -0.0003 -0.0413 194 LYS A O   
1283  C  CB  . LYS A 193 ? 1.0283 0.9374 1.6119 -0.0888 0.0084  -0.0547 194 LYS A CB  
1284  C  CG  . LYS A 193 ? 0.9620 0.8825 1.5471 -0.0880 0.0180  -0.0734 194 LYS A CG  
1285  C  CD  . LYS A 193 ? 0.9822 0.8940 1.5859 -0.0867 0.0158  -0.0852 194 LYS A CD  
1286  C  CE  . LYS A 193 ? 0.9709 0.8963 1.5761 -0.0837 0.0264  -0.1059 194 LYS A CE  
1287  N  NZ  . LYS A 193 ? 0.9855 0.9042 1.6090 -0.0828 0.0256  -0.1198 194 LYS A NZ  
1288  N  N   . GLN A 194 ? 1.2039 1.0794 1.8115 -0.0826 -0.0203 -0.0235 195 GLN A N   
1289  C  CA  . GLN A 194 ? 1.2732 1.1452 1.8776 -0.0811 -0.0274 -0.0095 195 GLN A CA  
1290  C  C   . GLN A 194 ? 1.3128 1.1839 1.8909 -0.0959 -0.0304 0.0090  195 GLN A C   
1291  O  O   . GLN A 194 ? 1.3408 1.2083 1.9120 -0.0985 -0.0374 0.0231  195 GLN A O   
1292  C  CB  . GLN A 194 ? 1.3007 1.1589 1.9302 -0.0756 -0.0409 -0.0043 195 GLN A CB  
1293  C  CG  . GLN A 194 ? 1.3278 1.1851 1.9596 -0.0708 -0.0480 0.0063  195 GLN A CG  
1294  C  CD  . GLN A 194 ? 1.3313 1.2034 1.9643 -0.0593 -0.0373 -0.0065 195 GLN A CD  
1295  O  OE1 . GLN A 194 ? 1.3338 1.2168 1.9702 -0.0533 -0.0251 -0.0247 195 GLN A OE1 
1296  N  NE2 . GLN A 194 ? 1.3378 1.2103 1.9666 -0.0574 -0.0421 0.0037  195 GLN A NE2 
1297  N  N   . ALA A 195 ? 1.3603 1.2364 1.9242 -0.1067 -0.0250 0.0087  196 ALA A N   
1298  C  CA  . ALA A 195 ? 1.3613 1.2420 1.9001 -0.1223 -0.0248 0.0233  196 ALA A CA  
1299  C  C   . ALA A 195 ? 1.3189 1.2132 1.8439 -0.1200 -0.0174 0.0240  196 ALA A C   
1300  O  O   . ALA A 195 ? 1.3921 1.2903 1.8981 -0.1319 -0.0182 0.0369  196 ALA A O   
1301  C  CB  . ALA A 195 ? 1.4080 1.2971 1.9371 -0.1324 -0.0176 0.0186  196 ALA A CB  
1302  N  N   . GLU A 196 ? 1.1623 1.0644 1.6970 -0.1054 -0.0101 0.0098  197 GLU A N   
1303  C  CA  . GLU A 196 ? 1.1004 1.0133 1.6259 -0.1009 -0.0041 0.0097  197 GLU A CA  
1304  C  C   . GLU A 196 ? 1.1306 1.0327 1.6556 -0.1021 -0.0153 0.0247  197 GLU A C   
1305  O  O   . GLU A 196 ? 1.1204 1.0073 1.6585 -0.1014 -0.0274 0.0315  197 GLU A O   
1306  C  CB  . GLU A 196 ? 1.0314 0.9529 1.5690 -0.0854 0.0047  -0.0082 197 GLU A CB  
1307  N  N   . ALA A 197 ? 1.2347 1.1455 1.7456 -0.1040 -0.0115 0.0294  198 ALA A N   
1308  C  CA  . ALA A 197 ? 1.2562 1.1603 1.7571 -0.1120 -0.0212 0.0468  198 ALA A CA  
1309  C  C   . ALA A 197 ? 1.2419 1.1426 1.7255 -0.1317 -0.0264 0.0616  198 ALA A C   
1310  O  O   . ALA A 197 ? 1.2866 1.1769 1.7639 -0.1408 -0.0384 0.0782  198 ALA A O   
1311  C  CB  . ALA A 197 ? 1.2803 1.1696 1.8009 -0.1024 -0.0344 0.0513  198 ALA A CB  
1312  N  N   . LEU A 198 ? 1.1147 1.0253 1.5907 -0.1388 -0.0173 0.0555  199 LEU A N   
1313  C  CA  . LEU A 198 ? 1.0218 0.9413 1.4751 -0.1584 -0.0142 0.0652  199 LEU A CA  
1314  C  C   . LEU A 198 ? 0.9035 0.8448 1.3473 -0.1565 0.0003  0.0560  199 LEU A C   
1315  O  O   . LEU A 198 ? 0.9253 0.8813 1.3516 -0.1706 0.0073  0.0594  199 LEU A O   
1316  C  CB  . LEU A 198 ? 0.9928 0.9124 1.4454 -0.1676 -0.0128 0.0637  199 LEU A CB  
1317  C  CG  . LEU A 198 ? 0.9442 0.8787 1.4016 -0.1628 -0.0002 0.0471  199 LEU A CG  
1318  C  CD1 . LEU A 198 ? 0.9086 0.8667 1.3489 -0.1735 0.0123  0.0451  199 LEU A CD1 
1319  C  CD2 . LEU A 198 ? 0.9497 0.8740 1.4150 -0.1670 -0.0051 0.0464  199 LEU A CD2 
1320  N  N   . ARG A 199 ? 0.8261 0.7702 1.2830 -0.1387 0.0050  0.0437  200 ARG A N   
1321  C  CA  . ARG A 199 ? 0.7071 0.6703 1.1598 -0.1326 0.0180  0.0331  200 ARG A CA  
1322  C  C   . ARG A 199 ? 0.6610 0.6431 1.1079 -0.1375 0.0299  0.0242  200 ARG A C   
1323  O  O   . ARG A 199 ? 0.6456 0.6432 1.0784 -0.1482 0.0370  0.0264  200 ARG A O   
1324  C  CB  . ARG A 199 ? 0.7732 0.7411 1.2115 -0.1400 0.0179  0.0423  200 ARG A CB  
1325  C  CG  . ARG A 199 ? 0.8312 0.7872 1.2783 -0.1289 0.0100  0.0452  200 ARG A CG  
1326  C  CD  . ARG A 199 ? 0.9145 0.8659 1.3470 -0.1416 0.0018  0.0615  200 ARG A CD  
1327  N  NE  . ARG A 199 ? 0.9861 0.9307 1.4267 -0.1305 -0.0037 0.0626  200 ARG A NE  
1328  C  CZ  . ARG A 199 ? 1.0654 1.0100 1.4939 -0.1384 -0.0085 0.0734  200 ARG A CZ  
1329  N  NH1 . ARG A 199 ? 1.1058 1.0574 1.5124 -0.1583 -0.0079 0.0837  200 ARG A NH1 
1330  N  NH2 . ARG A 199 ? 1.0915 1.0303 1.5293 -0.1273 -0.0136 0.0735  200 ARG A NH2 
1331  N  N   . PRO A 200 ? 0.5665 0.5486 1.0253 -0.1299 0.0322  0.0135  201 PRO A N   
1332  C  CA  . PRO A 200 ? 0.5591 0.5590 1.0146 -0.1333 0.0420  0.0049  201 PRO A CA  
1333  C  C   . PRO A 200 ? 0.5296 0.5499 0.9818 -0.1260 0.0535  -0.0046 201 PRO A C   
1334  O  O   . PRO A 200 ? 0.5593 0.5976 1.0048 -0.1318 0.0613  -0.0081 201 PRO A O   
1335  C  CB  . PRO A 200 ? 0.5318 0.5243 1.0021 -0.1248 0.0400  -0.0047 201 PRO A CB  
1336  C  CG  . PRO A 200 ? 0.5018 0.4798 0.9844 -0.1119 0.0344  -0.0071 201 PRO A CG  
1337  C  CD  . PRO A 200 ? 0.5342 0.5009 1.0107 -0.1176 0.0261  0.0076  201 PRO A CD  
1338  N  N   . PHE A 201 ? 0.4983 0.5161 0.9560 -0.1131 0.0541  -0.0090 202 PHE A N   
1339  C  CA  . PHE A 201 ? 0.4504 0.4853 0.9054 -0.1052 0.0636  -0.0175 202 PHE A CA  
1340  C  C   . PHE A 201 ? 0.5542 0.5954 0.9975 -0.1113 0.0663  -0.0112 202 PHE A C   
1341  O  O   . PHE A 201 ? 0.5658 0.6199 1.0066 -0.1048 0.0737  -0.0178 202 PHE A O   
1342  C  CB  . PHE A 201 ? 0.4554 0.4858 0.9213 -0.0891 0.0637  -0.0261 202 PHE A CB  
1343  C  CG  . PHE A 201 ? 0.3507 0.3804 0.8263 -0.0835 0.0639  -0.0356 202 PHE A CG  
1344  C  CD1 . PHE A 201 ? 0.3577 0.4030 0.8310 -0.0839 0.0698  -0.0425 202 PHE A CD1 
1345  C  CD2 . PHE A 201 ? 0.3266 0.3411 0.8141 -0.0779 0.0582  -0.0383 202 PHE A CD2 
1346  C  CE1 . PHE A 201 ? 0.4115 0.4569 0.8923 -0.0804 0.0695  -0.0509 202 PHE A CE1 
1347  C  CE2 . PHE A 201 ? 0.3717 0.3869 0.8673 -0.0744 0.0593  -0.0485 202 PHE A CE2 
1348  C  CZ  . PHE A 201 ? 0.3898 0.4203 0.8811 -0.0763 0.0647  -0.0544 202 PHE A CZ  
1349  N  N   . GLY A 202 ? 0.5303 0.5620 0.9658 -0.1245 0.0596  0.0017  203 GLY A N   
1350  C  CA  . GLY A 202 ? 0.6044 0.6418 1.0271 -0.1334 0.0614  0.0083  203 GLY A CA  
1351  C  C   . GLY A 202 ? 0.6156 0.6427 1.0421 -0.1243 0.0567  0.0107  203 GLY A C   
1352  O  O   . GLY A 202 ? 0.6717 0.6818 1.1093 -0.1159 0.0478  0.0129  203 GLY A O   
1353  N  N   . GLU A 203 ? 0.5955 0.6339 1.0137 -0.1258 0.0629  0.0092  204 GLU A N   
1354  C  CA  . GLU A 203 ? 0.5893 0.6198 1.0098 -0.1188 0.0587  0.0119  204 GLU A CA  
1355  C  C   . GLU A 203 ? 0.4730 0.5090 0.9039 -0.1002 0.0649  -0.0013 204 GLU A C   
1356  O  O   . GLU A 203 ? 0.4749 0.5044 0.9104 -0.0921 0.0618  -0.0008 204 GLU A O   
1357  C  CB  . GLU A 203 ? 0.7118 0.7510 1.1169 -0.1321 0.0617  0.0176  204 GLU A CB  
1358  C  CG  . GLU A 203 ? 0.8692 0.9168 1.2592 -0.1531 0.0639  0.0244  204 GLU A CG  
1359  C  CD  . GLU A 203 ? 0.9895 1.0471 1.3581 -0.1664 0.0673  0.0281  204 GLU A CD  
1360  O  OE1 . GLU A 203 ? 1.0397 1.0847 1.3986 -0.1745 0.0558  0.0421  204 GLU A OE1 
1361  O  OE2 . GLU A 203 ? 1.0252 1.1037 1.3872 -0.1688 0.0810  0.0164  204 GLU A OE2 
1362  N  N   . ALA A 204 ? 0.3594 0.4075 0.7934 -0.0943 0.0728  -0.0121 205 ALA A N   
1363  C  CA  . ALA A 204 ? 0.3954 0.4500 0.8358 -0.0785 0.0781  -0.0234 205 ALA A CA  
1364  C  C   . ALA A 204 ? 0.3537 0.3947 0.8067 -0.0664 0.0723  -0.0251 205 ALA A C   
1365  O  O   . ALA A 204 ? 0.4596 0.5023 0.9146 -0.0564 0.0743  -0.0296 205 ALA A O   
1366  C  CB  . ALA A 204 ? 0.3395 0.4070 0.7803 -0.0757 0.0844  -0.0321 205 ALA A CB  
1367  N  N   . PRO A 205 ? 0.3281 0.3560 0.7896 -0.0672 0.0654  -0.0225 206 PRO A N   
1368  C  CA  . PRO A 205 ? 0.3632 0.3801 0.8379 -0.0560 0.0612  -0.0263 206 PRO A CA  
1369  C  C   . PRO A 205 ? 0.3561 0.3644 0.8325 -0.0534 0.0560  -0.0202 206 PRO A C   
1370  O  O   . PRO A 205 ? 0.3497 0.3572 0.8339 -0.0428 0.0570  -0.0261 206 PRO A O   
1371  C  CB  . PRO A 205 ? 0.3482 0.3523 0.8313 -0.0591 0.0543  -0.0242 206 PRO A CB  
1372  C  CG  . PRO A 205 ? 0.3814 0.3942 0.8568 -0.0685 0.0578  -0.0240 206 PRO A CG  
1373  C  CD  . PRO A 205 ? 0.3739 0.3982 0.8351 -0.0766 0.0623  -0.0189 206 PRO A CD  
1374  N  N   . ARG A 206 ? 0.3222 0.3249 0.7908 -0.0641 0.0501  -0.0082 207 ARG A N   
1375  C  CA  . ARG A 206 ? 0.3889 0.3835 0.8579 -0.0633 0.0435  -0.0008 207 ARG A CA  
1376  C  C   . ARG A 206 ? 0.3157 0.3227 0.7783 -0.0599 0.0513  -0.0055 207 ARG A C   
1377  O  O   . ARG A 206 ? 0.2260 0.2300 0.6956 -0.0508 0.0500  -0.0078 207 ARG A O   
1378  C  CB  . ARG A 206 ? 0.3362 0.3221 0.7956 -0.0782 0.0339  0.0148  207 ARG A CB  
1379  C  CG  . ARG A 206 ? 0.4555 0.4342 0.9129 -0.0795 0.0257  0.0243  207 ARG A CG  
1380  C  CD  . ARG A 206 ? 0.5668 0.5364 1.0131 -0.0958 0.0142  0.0415  207 ARG A CD  
1381  N  NE  . ARG A 206 ? 0.6833 0.6486 1.1247 -0.0994 0.0063  0.0514  207 ARG A NE  
1382  C  CZ  . ARG A 206 ? 0.8191 0.7912 1.2410 -0.1152 0.0063  0.0600  207 ARG A CZ  
1383  N  NH1 . ARG A 206 ? 0.8620 0.8467 1.2662 -0.1278 0.0148  0.0588  207 ARG A NH1 
1384  N  NH2 . ARG A 206 ? 0.8632 0.8313 1.2793 -0.1178 -0.0019 0.0686  207 ARG A NH2 
1385  N  N   . GLU A 207 ? 0.2785 0.3003 0.7285 -0.0670 0.0597  -0.0077 208 GLU A N   
1386  C  CA  . GLU A 207 ? 0.3281 0.3626 0.7700 -0.0625 0.0677  -0.0140 208 GLU A CA  
1387  C  C   . GLU A 207 ? 0.3575 0.3947 0.8102 -0.0470 0.0715  -0.0243 208 GLU A C   
1388  O  O   . GLU A 207 ? 0.3080 0.3450 0.7615 -0.0401 0.0718  -0.0259 208 GLU A O   
1389  C  CB  . GLU A 207 ? 0.4044 0.4558 0.8363 -0.0708 0.0773  -0.0185 208 GLU A CB  
1390  C  CG  . GLU A 207 ? 0.4923 0.5453 0.9074 -0.0880 0.0758  -0.0096 208 GLU A CG  
1391  C  CD  . GLU A 207 ? 0.6311 0.6836 1.0340 -0.0906 0.0741  -0.0061 208 GLU A CD  
1392  O  OE1 . GLU A 207 ? 0.6933 0.7412 1.0825 -0.1047 0.0679  0.0049  208 GLU A OE1 
1393  O  OE2 . GLU A 207 ? 0.6532 0.7099 1.0599 -0.0794 0.0785  -0.0140 208 GLU A OE2 
1394  N  N   . LEU A 208 ? 0.3618 0.4007 0.8187 -0.0420 0.0736  -0.0305 209 LEU A N   
1395  C  CA  . LEU A 208 ? 0.4049 0.4444 0.8652 -0.0291 0.0758  -0.0391 209 LEU A CA  
1396  C  C   . LEU A 208 ? 0.2985 0.3269 0.7702 -0.0226 0.0705  -0.0384 209 LEU A C   
1397  O  O   . LEU A 208 ? 0.1776 0.2054 0.6454 -0.0143 0.0718  -0.0426 209 LEU A O   
1398  C  CB  . LEU A 208 ? 0.3530 0.3947 0.8149 -0.0280 0.0772  -0.0446 209 LEU A CB  
1399  C  CG  . LEU A 208 ? 0.3183 0.3593 0.7766 -0.0184 0.0782  -0.0522 209 LEU A CG  
1400  C  CD1 . LEU A 208 ? 0.2650 0.3115 0.7085 -0.0143 0.0808  -0.0539 209 LEU A CD1 
1401  C  CD2 . LEU A 208 ? 0.1806 0.2247 0.6406 -0.0198 0.0788  -0.0570 209 LEU A CD2 
1402  N  N   . ARG A 209 ? 0.3333 0.3505 0.8161 -0.0269 0.0636  -0.0330 210 ARG A N   
1403  C  CA  . ARG A 209 ? 0.2871 0.2936 0.7840 -0.0206 0.0580  -0.0332 210 ARG A CA  
1404  C  C   . ARG A 209 ? 0.3104 0.3172 0.8051 -0.0184 0.0567  -0.0294 210 ARG A C   
1405  O  O   . ARG A 209 ? 0.2666 0.2751 0.7643 -0.0093 0.0590  -0.0354 210 ARG A O   
1406  C  CB  . ARG A 209 ? 0.3605 0.3525 0.8657 -0.0249 0.0482  -0.0261 210 ARG A CB  
1407  C  CG  . ARG A 209 ? 0.3666 0.3506 0.8887 -0.0161 0.0425  -0.0286 210 ARG A CG  
1408  C  CD  . ARG A 209 ? 0.4718 0.4435 1.0021 -0.0191 0.0309  -0.0204 210 ARG A CD  
1409  N  NE  . ARG A 209 ? 0.5228 0.4867 1.0473 -0.0251 0.0212  -0.0060 210 ARG A NE  
1410  C  CZ  . ARG A 209 ? 0.5725 0.5309 1.0849 -0.0375 0.0154  0.0063  210 ARG A CZ  
1411  N  NH1 . ARG A 209 ? 0.5676 0.5278 1.0735 -0.0444 0.0189  0.0054  210 ARG A NH1 
1412  N  NH2 . ARG A 209 ? 0.5954 0.5477 1.1015 -0.0444 0.0060  0.0197  210 ARG A NH2 
1413  N  N   . LEU A 210 ? 0.2493 0.2538 0.7332 -0.0271 0.0525  -0.0194 211 LEU A N   
1414  C  CA  . LEU A 210 ? 0.2775 0.2815 0.7549 -0.0263 0.0499  -0.0150 211 LEU A CA  
1415  C  C   . LEU A 210 ? 0.2888 0.3053 0.7600 -0.0195 0.0591  -0.0234 211 LEU A C   
1416  O  O   . LEU A 210 ? 0.3511 0.3668 0.8280 -0.0115 0.0589  -0.0262 211 LEU A O   
1417  C  CB  . LEU A 210 ? 0.2666 0.2693 0.7284 -0.0398 0.0452  -0.0037 211 LEU A CB  
1418  C  CG  . LEU A 210 ? 0.3820 0.3701 0.8492 -0.0482 0.0328  0.0088  211 LEU A CG  
1419  C  CD1 . LEU A 210 ? 0.4233 0.4138 0.8702 -0.0647 0.0302  0.0195  211 LEU A CD1 
1420  C  CD2 . LEU A 210 ? 0.3511 0.3273 0.8330 -0.0426 0.0223  0.0139  211 LEU A CD2 
1421  N  N   . ARG A 211 ? 0.2162 0.2442 0.6779 -0.0229 0.0669  -0.0273 212 ARG A N   
1422  C  CA  . ARG A 211 ? 0.2731 0.3098 0.7253 -0.0166 0.0737  -0.0344 212 ARG A CA  
1423  C  C   . ARG A 211 ? 0.3566 0.3859 0.8029 -0.0060 0.0731  -0.0405 212 ARG A C   
1424  O  O   . ARG A 211 ? 0.3553 0.3820 0.7924 -0.0021 0.0725  -0.0417 212 ARG A O   
1425  C  CB  . ARG A 211 ? 0.1905 0.2375 0.6321 -0.0210 0.0804  -0.0384 212 ARG A CB  
1426  C  CG  . ARG A 211 ? 0.1856 0.2401 0.6226 -0.0344 0.0827  -0.0341 212 ARG A CG  
1427  C  CD  . ARG A 211 ? 0.2377 0.3042 0.6659 -0.0381 0.0904  -0.0403 212 ARG A CD  
1428  N  NE  . ARG A 211 ? 0.2795 0.3541 0.7000 -0.0528 0.0940  -0.0378 212 ARG A NE  
1429  C  CZ  . ARG A 211 ? 0.3807 0.4621 0.7934 -0.0551 0.0986  -0.0419 212 ARG A CZ  
1430  N  NH1 . ARG A 211 ? 0.4030 0.4903 0.8004 -0.0696 0.1012  -0.0402 212 ARG A NH1 
1431  N  NH2 . ARG A 211 ? 0.4099 0.4904 0.8251 -0.0433 0.0998  -0.0478 212 ARG A NH2 
1432  N  N   . ALA A 212 ? 0.2455 0.2715 0.6939 -0.0049 0.0725  -0.0435 213 ALA A N   
1433  C  CA  . ALA A 212 ? 0.2806 0.3021 0.7188 -0.0011 0.0713  -0.0482 213 ALA A CA  
1434  C  C   . ALA A 212 ? 0.2900 0.3044 0.7321 0.0006  0.0672  -0.0473 213 ALA A C   
1435  O  O   . ALA A 212 ? 0.3268 0.3414 0.7564 0.0023  0.0667  -0.0489 213 ALA A O   
1436  C  CB  . ALA A 212 ? 0.1700 0.1919 0.6118 -0.0022 0.0719  -0.0524 213 ALA A CB  
1437  N  N   . THR A 213 ? 0.2879 0.2971 0.7494 -0.0003 0.0635  -0.0442 214 THR A N   
1438  C  CA  . THR A 213 ? 0.3150 0.3192 0.7835 0.0006  0.0586  -0.0432 214 THR A CA  
1439  C  C   . THR A 213 ? 0.3582 0.3637 0.8171 0.0022  0.0579  -0.0403 214 THR A C   
1440  O  O   . THR A 213 ? 0.2601 0.2657 0.7106 0.0034  0.0571  -0.0427 214 THR A O   
1441  C  CB  . THR A 213 ? 0.3287 0.3281 0.8241 -0.0007 0.0524  -0.0378 214 THR A CB  
1442  O  OG1 . THR A 213 ? 0.4616 0.4601 0.9682 -0.0024 0.0526  -0.0415 214 THR A OG1 
1443  C  CG2 . THR A 213 ? 0.3930 0.3911 0.8951 0.0005  0.0463  -0.0364 214 THR A CG2 
1444  N  N   . ARG A 214 ? 0.2281 0.2364 0.6895 0.0019  0.0590  -0.0357 215 ARG A N   
1445  C  CA  . ARG A 214 ? 0.3197 0.3298 0.7733 0.0031  0.0589  -0.0339 215 ARG A CA  
1446  C  C   . ARG A 214 ? 0.3251 0.3381 0.7559 0.0045  0.0628  -0.0388 215 ARG A C   
1447  O  O   . ARG A 214 ? 0.2845 0.2962 0.7075 0.0058  0.0611  -0.0396 215 ARG A O   
1448  C  CB  . ARG A 214 ? 0.2792 0.2979 0.7419 -0.0008 0.0604  -0.0289 215 ARG A CB  
1449  C  CG  . ARG A 214 ? 0.2502 0.2738 0.7023 -0.0006 0.0631  -0.0301 215 ARG A CG  
1450  C  CD  . ARG A 214 ? 0.1877 0.2172 0.6324 -0.0115 0.0634  -0.0255 215 ARG A CD  
1451  N  NE  . ARG A 214 ? 0.2102 0.2447 0.6488 -0.0180 0.0677  -0.0265 215 ARG A NE  
1452  C  CZ  . ARG A 214 ? 0.2973 0.3422 0.7352 -0.0160 0.0767  -0.0347 215 ARG A CZ  
1453  N  NH1 . ARG A 214 ? 0.3705 0.4204 0.8045 -0.0227 0.0801  -0.0353 215 ARG A NH1 
1454  N  NH2 . ARG A 214 ? 0.2369 0.2796 0.6649 -0.0075 0.0790  -0.0409 215 ARG A NH2 
1455  N  N   . ALA A 215 ? 0.2323 0.2500 0.6550 0.0038  0.0672  -0.0415 216 ALA A N   
1456  C  CA  . ALA A 215 ? 0.2818 0.3028 0.6883 0.0051  0.0693  -0.0444 216 ALA A CA  
1457  C  C   . ALA A 215 ? 0.3025 0.3223 0.7003 0.0065  0.0675  -0.0461 216 ALA A C   
1458  O  O   . ALA A 215 ? 0.1927 0.2135 0.5817 0.0079  0.0670  -0.0461 216 ALA A O   
1459  C  CB  . ALA A 215 ? 0.2025 0.2297 0.6064 0.0039  0.0734  -0.0468 216 ALA A CB  
1460  N  N   . PHE A 216 ? 0.1961 0.2148 0.5982 0.0059  0.0670  -0.0481 217 PHE A N   
1461  C  CA  . PHE A 216 ? 0.2376 0.2580 0.6333 0.0066  0.0668  -0.0510 217 PHE A CA  
1462  C  C   . PHE A 216 ? 0.2733 0.2916 0.6691 0.0072  0.0650  -0.0512 217 PHE A C   
1463  O  O   . PHE A 216 ? 0.3601 0.3808 0.7484 0.0082  0.0655  -0.0520 217 PHE A O   
1464  C  CB  . PHE A 216 ? 0.2446 0.2658 0.6463 0.0053  0.0678  -0.0550 217 PHE A CB  
1465  C  CG  . PHE A 216 ? 0.2658 0.2921 0.6641 0.0051  0.0695  -0.0558 217 PHE A CG  
1466  C  CD1 . PHE A 216 ? 0.3235 0.3554 0.7151 0.0062  0.0698  -0.0568 217 PHE A CD1 
1467  C  CD2 . PHE A 216 ? 0.2004 0.2272 0.6047 0.0037  0.0708  -0.0551 217 PHE A CD2 
1468  C  CE1 . PHE A 216 ? 0.3061 0.3438 0.6975 0.0061  0.0705  -0.0571 217 PHE A CE1 
1469  C  CE2 . PHE A 216 ? 0.1630 0.1958 0.5653 0.0034  0.0723  -0.0562 217 PHE A CE2 
1470  C  CZ  . PHE A 216 ? 0.3183 0.3564 0.7143 0.0047  0.0717  -0.0571 217 PHE A CZ  
1471  N  N   . VAL A 217 ? 0.2538 0.2680 0.6604 0.0066  0.0629  -0.0502 218 VAL A N   
1472  C  CA  . VAL A 217 ? 0.3253 0.3384 0.7340 0.0072  0.0610  -0.0506 218 VAL A CA  
1473  C  C   . VAL A 217 ? 0.2501 0.2636 0.6512 0.0083  0.0603  -0.0468 218 VAL A C   
1474  O  O   . VAL A 217 ? 0.1613 0.1757 0.5585 0.0091  0.0601  -0.0476 218 VAL A O   
1475  C  CB  . VAL A 217 ? 0.3531 0.3625 0.7794 0.0064  0.0575  -0.0500 218 VAL A CB  
1476  C  CG1 . VAL A 217 ? 0.3628 0.3697 0.7978 0.0063  0.0545  -0.0435 218 VAL A CG1 
1477  C  CG2 . VAL A 217 ? 0.3378 0.3476 0.7676 0.0070  0.0561  -0.0525 218 VAL A CG2 
1478  N  N   . ALA A 218 ? 0.1974 0.2107 0.5979 0.0083  0.0607  -0.0438 219 ALA A N   
1479  C  CA  . ALA A 218 ? 0.2591 0.2734 0.6535 0.0091  0.0609  -0.0419 219 ALA A CA  
1480  C  C   . ALA A 218 ? 0.2136 0.2306 0.5962 0.0101  0.0623  -0.0434 219 ALA A C   
1481  O  O   . ALA A 218 ? 0.2306 0.2476 0.6100 0.0108  0.0615  -0.0429 219 ALA A O   
1482  C  CB  . ALA A 218 ? 0.1597 0.1752 0.5571 0.0085  0.0627  -0.0408 219 ALA A CB  
1483  N  N   . ALA A 219 ? 0.2886 0.3081 0.6673 0.0102  0.0640  -0.0447 220 ALA A N   
1484  C  CA  . ALA A 219 ? 0.2592 0.2819 0.6315 0.0113  0.0645  -0.0450 220 ALA A CA  
1485  C  C   . ALA A 219 ? 0.2119 0.2357 0.5837 0.0116  0.0643  -0.0460 220 ALA A C   
1486  O  O   . ALA A 219 ? 0.2148 0.2397 0.5844 0.0124  0.0640  -0.0447 220 ALA A O   
1487  C  CB  . ALA A 219 ? 0.2311 0.2571 0.6033 0.0113  0.0657  -0.0462 220 ALA A CB  
1488  N  N   . ARG A 220 ? 0.1823 0.2062 0.5582 0.0107  0.0650  -0.0490 221 ARG A N   
1489  C  CA  . ARG A 220 ? 0.2370 0.2635 0.6146 0.0104  0.0663  -0.0523 221 ARG A CA  
1490  C  C   . ARG A 220 ? 0.2006 0.2254 0.5789 0.0107  0.0654  -0.0514 221 ARG A C   
1491  O  O   . ARG A 220 ? 0.2178 0.2460 0.5951 0.0110  0.0668  -0.0521 221 ARG A O   
1492  C  CB  . ARG A 220 ? 0.2860 0.3126 0.6707 0.0090  0.0676  -0.0577 221 ARG A CB  
1493  C  CG  . ARG A 220 ? 0.3254 0.3567 0.7132 0.0082  0.0707  -0.0638 221 ARG A CG  
1494  C  CD  . ARG A 220 ? 0.4267 0.4556 0.8249 0.0070  0.0710  -0.0694 221 ARG A CD  
1495  N  NE  . ARG A 220 ? 0.4778 0.5049 0.8823 0.0059  0.0710  -0.0723 221 ARG A NE  
1496  C  CZ  . ARG A 220 ? 0.5377 0.5605 0.9547 0.0051  0.0693  -0.0745 221 ARG A CZ  
1497  N  NH1 . ARG A 220 ? 0.5451 0.5655 0.9696 0.0055  0.0670  -0.0739 221 ARG A NH1 
1498  N  NH2 . ARG A 220 ? 0.5360 0.5573 0.9603 0.0038  0.0693  -0.0769 221 ARG A NH2 
1499  N  N   . SER A 221 ? 0.2450 0.2655 0.6272 0.0106  0.0631  -0.0497 222 SER A N   
1500  C  CA  A SER A 221 ? 0.2589 0.2782 0.6440 0.0108  0.0617  -0.0488 222 SER A CA  
1501  C  CA  B SER A 221 ? 0.2647 0.2841 0.6499 0.0108  0.0617  -0.0488 222 SER A CA  
1502  C  C   . SER A 221 ? 0.2787 0.2985 0.6576 0.0116  0.0615  -0.0455 222 SER A C   
1503  O  O   . SER A 221 ? 0.1576 0.1785 0.5373 0.0117  0.0617  -0.0457 222 SER A O   
1504  C  CB  A SER A 221 ? 0.2269 0.2425 0.6211 0.0105  0.0585  -0.0467 222 SER A CB  
1505  C  CB  B SER A 221 ? 0.2321 0.2477 0.6263 0.0105  0.0584  -0.0467 222 SER A CB  
1506  O  OG  A SER A 221 ? 0.2397 0.2543 0.6436 0.0097  0.0580  -0.0497 222 SER A OG  
1507  O  OG  B SER A 221 ? 0.1901 0.2042 0.5823 0.0106  0.0577  -0.0431 222 SER A OG  
1508  N  N   . PHE A 222 ? 0.2369 0.2562 0.6114 0.0119  0.0613  -0.0433 223 PHE A N   
1509  C  CA  . PHE A 222 ? 0.2246 0.2440 0.5958 0.0126  0.0611  -0.0412 223 PHE A CA  
1510  C  C   . PHE A 222 ? 0.2463 0.2689 0.6166 0.0131  0.0622  -0.0411 223 PHE A C   
1511  O  O   . PHE A 222 ? 0.1730 0.1959 0.5450 0.0132  0.0621  -0.0399 223 PHE A O   
1512  C  CB  . PHE A 222 ? 0.2031 0.2223 0.5725 0.0128  0.0615  -0.0408 223 PHE A CB  
1513  C  CG  . PHE A 222 ? 0.2657 0.2848 0.6346 0.0134  0.0614  -0.0402 223 PHE A CG  
1514  C  CD1 . PHE A 222 ? 0.1753 0.1927 0.5466 0.0131  0.0610  -0.0403 223 PHE A CD1 
1515  C  CD2 . PHE A 222 ? 0.2413 0.2622 0.6106 0.0143  0.0614  -0.0396 223 PHE A CD2 
1516  C  CE1 . PHE A 222 ? 0.1864 0.2035 0.5592 0.0134  0.0611  -0.0410 223 PHE A CE1 
1517  C  CE2 . PHE A 222 ? 0.2342 0.2545 0.6066 0.0149  0.0609  -0.0394 223 PHE A CE2 
1518  C  CZ  . PHE A 222 ? 0.2458 0.2640 0.6196 0.0143  0.0610  -0.0406 223 PHE A CZ  
1519  N  N   . VAL A 223 ? 0.2151 0.2409 0.5851 0.0133  0.0634  -0.0420 224 VAL A N   
1520  C  CA  . VAL A 223 ? 0.2882 0.3190 0.6611 0.0136  0.0646  -0.0414 224 VAL A CA  
1521  C  C   . VAL A 223 ? 0.2636 0.2975 0.6397 0.0126  0.0668  -0.0437 224 VAL A C   
1522  O  O   . VAL A 223 ? 0.1800 0.2170 0.5600 0.0126  0.0674  -0.0418 224 VAL A O   
1523  C  CB  . VAL A 223 ? 0.2458 0.2814 0.6200 0.0135  0.0656  -0.0427 224 VAL A CB  
1524  C  CG1 . VAL A 223 ? 0.2817 0.3261 0.6620 0.0127  0.0677  -0.0430 224 VAL A CG1 
1525  C  CG2 . VAL A 223 ? 0.2069 0.2415 0.5810 0.0146  0.0636  -0.0401 224 VAL A CG2 
1526  N  N   . GLN A 224 ? 0.2327 0.2662 0.6094 0.0118  0.0680  -0.0482 225 GLN A N   
1527  C  CA  . GLN A 224 ? 0.2934 0.3301 0.6746 0.0107  0.0706  -0.0524 225 GLN A CA  
1528  C  C   . GLN A 224 ? 0.2406 0.2749 0.6230 0.0111  0.0692  -0.0496 225 GLN A C   
1529  O  O   . GLN A 224 ? 0.1615 0.2009 0.5479 0.0103  0.0718  -0.0510 225 GLN A O   
1530  C  CB  . GLN A 224 ? 0.3759 0.4105 0.7609 0.0100  0.0709  -0.0576 225 GLN A CB  
1531  C  CG  . GLN A 224 ? 0.5175 0.5588 0.9065 0.0084  0.0754  -0.0652 225 GLN A CG  
1532  C  CD  . GLN A 224 ? 0.6522 0.6897 1.0475 0.0078  0.0748  -0.0701 225 GLN A CD  
1533  O  OE1 . GLN A 224 ? 0.6680 0.6987 1.0658 0.0086  0.0706  -0.0667 225 GLN A OE1 
1534  N  NE2 . GLN A 224 ? 0.6930 0.7360 1.0932 0.0060  0.0791  -0.0785 225 GLN A NE2 
1535  N  N   . GLY A 225 ? 0.2170 0.2450 0.5971 0.0118  0.0656  -0.0462 226 GLY A N   
1536  C  CA  . GLY A 225 ? 0.1578 0.1835 0.5397 0.0119  0.0639  -0.0438 226 GLY A CA  
1537  C  C   . GLY A 225 ? 0.2494 0.2768 0.6319 0.0121  0.0645  -0.0407 226 GLY A C   
1538  O  O   . GLY A 225 ? 0.1581 0.1871 0.5452 0.0116  0.0653  -0.0404 226 GLY A O   
1539  N  N   . LEU A 226 ? 0.2028 0.2300 0.5833 0.0128  0.0639  -0.0383 227 LEU A N   
1540  C  CA  . LEU A 226 ? 0.1875 0.2162 0.5732 0.0131  0.0636  -0.0346 227 LEU A CA  
1541  C  C   . LEU A 226 ? 0.1581 0.1949 0.5505 0.0119  0.0667  -0.0348 227 LEU A C   
1542  O  O   . LEU A 226 ? 0.1634 0.2024 0.5631 0.0112  0.0670  -0.0320 227 LEU A O   
1543  C  CB  . LEU A 226 ? 0.1964 0.2247 0.5823 0.0142  0.0619  -0.0325 227 LEU A CB  
1544  C  CG  . LEU A 226 ? 0.1834 0.2065 0.5654 0.0147  0.0600  -0.0330 227 LEU A CG  
1545  C  CD1 . LEU A 226 ? 0.2082 0.2324 0.5915 0.0158  0.0591  -0.0323 227 LEU A CD1 
1546  C  CD2 . LEU A 226 ? 0.1575 0.1774 0.5440 0.0146  0.0587  -0.0319 227 LEU A CD2 
1547  N  N   . GLY A 227 ? 0.1587 0.2018 0.5501 0.0110  0.0696  -0.0385 228 GLY A N   
1548  C  CA  . GLY A 227 ? 0.3267 0.3820 0.7242 0.0081  0.0742  -0.0405 228 GLY A CA  
1549  C  C   . GLY A 227 ? 0.3181 0.3757 0.7181 0.0066  0.0769  -0.0435 228 GLY A C   
1550  O  O   . GLY A 227 ? 0.3511 0.4180 0.7579 0.0034  0.0794  -0.0416 228 GLY A O   
1551  N  N   . VAL A 228 ? 0.3076 0.3579 0.7038 0.0080  0.0758  -0.0476 229 VAL A N   
1552  C  CA  . VAL A 228 ? 0.3346 0.3866 0.7351 0.0070  0.0775  -0.0510 229 VAL A CA  
1553  C  C   . VAL A 228 ? 0.2979 0.3474 0.7019 0.0072  0.0754  -0.0455 229 VAL A C   
1554  O  O   . VAL A 228 ? 0.2612 0.3184 0.6714 0.0048  0.0786  -0.0463 229 VAL A O   
1555  C  CB  . VAL A 228 ? 0.2809 0.3258 0.6808 0.0084  0.0749  -0.0544 229 VAL A CB  
1556  C  CG1 . VAL A 228 ? 0.2883 0.3333 0.6948 0.0081  0.0745  -0.0558 229 VAL A CG1 
1557  C  CG2 . VAL A 228 ? 0.1688 0.2174 0.5700 0.0076  0.0778  -0.0616 229 VAL A CG2 
1558  N  N   . ALA A 229 ? 0.3291 0.3692 0.7301 0.0092  0.0706  -0.0406 230 ALA A N   
1559  C  CA  . ALA A 229 ? 0.2961 0.3329 0.7019 0.0092  0.0685  -0.0362 230 ALA A CA  
1560  C  C   . ALA A 229 ? 0.2657 0.3100 0.6802 0.0074  0.0705  -0.0320 230 ALA A C   
1561  O  O   . ALA A 229 ? 0.2880 0.3360 0.7101 0.0055  0.0715  -0.0302 230 ALA A O   
1562  C  CB  . ALA A 229 ? 0.2532 0.2811 0.6549 0.0106  0.0642  -0.0335 230 ALA A CB  
1563  N  N   . SER A 230 ? 0.2538 0.3021 0.6689 0.0072  0.0706  -0.0296 231 SER A N   
1564  C  CA  A SER A 230 ? 0.3256 0.3841 0.7520 0.0038  0.0711  -0.0232 231 SER A CA  
1565  C  CA  B SER A 230 ? 0.3234 0.3819 0.7497 0.0037  0.0711  -0.0233 231 SER A CA  
1566  C  C   . SER A 230 ? 0.2799 0.3541 0.7091 -0.0031 0.0768  -0.0252 231 SER A C   
1567  O  O   . SER A 230 ? 0.2693 0.3497 0.7067 -0.0083 0.0767  -0.0195 231 SER A O   
1568  C  CB  A SER A 230 ? 0.3385 0.4011 0.7660 0.0036  0.0697  -0.0204 231 SER A CB  
1569  C  CB  B SER A 230 ? 0.3394 0.4023 0.7667 0.0035  0.0699  -0.0206 231 SER A CB  
1570  O  OG  A SER A 230 ? 0.3171 0.3853 0.7587 0.0005  0.0659  -0.0105 231 SER A OG  
1571  O  OG  B SER A 230 ? 0.3246 0.3749 0.7495 0.0085  0.0651  -0.0192 231 SER A OG  
1572  N  N   . ASP A 231 ? 0.3176 0.3983 0.7399 -0.0045 0.0817  -0.0335 232 ASP A N   
1573  C  CA  . ASP A 231 ? 0.4108 0.5078 0.8339 -0.0124 0.0886  -0.0381 232 ASP A CA  
1574  C  C   . ASP A 231 ? 0.3555 0.4508 0.7817 -0.0123 0.0894  -0.0399 232 ASP A C   
1575  O  O   . ASP A 231 ? 0.2599 0.3684 0.6894 -0.0207 0.0932  -0.0386 232 ASP A O   
1576  C  CB  . ASP A 231 ? 0.5422 0.6439 0.9591 -0.0127 0.0936  -0.0490 232 ASP A CB  
1577  C  CG  . ASP A 231 ? 0.7122 0.8232 1.1270 -0.0171 0.0950  -0.0482 232 ASP A CG  
1578  O  OD1 . ASP A 231 ? 0.7653 0.8843 1.1842 -0.0235 0.0931  -0.0386 232 ASP A OD1 
1579  O  OD2 . ASP A 231 ? 0.7970 0.9072 1.2074 -0.0152 0.0973  -0.0562 232 ASP A OD2 
1580  N  N   . VAL A 232 ? 0.3186 0.3986 0.7431 -0.0048 0.0855  -0.0421 233 VAL A N   
1581  C  CA  . VAL A 232 ? 0.3233 0.4010 0.7521 -0.0044 0.0850  -0.0434 233 VAL A CA  
1582  C  C   . VAL A 232 ? 0.3337 0.4127 0.7698 -0.0074 0.0830  -0.0349 233 VAL A C   
1583  O  O   . VAL A 232 ? 0.3259 0.4144 0.7668 -0.0129 0.0860  -0.0348 233 VAL A O   
1584  C  CB  . VAL A 232 ? 0.3300 0.3921 0.7557 0.0016  0.0796  -0.0449 233 VAL A CB  
1585  C  CG1 . VAL A 232 ? 0.1697 0.2292 0.6018 0.0016  0.0777  -0.0437 233 VAL A CG1 
1586  C  CG2 . VAL A 232 ? 0.2548 0.3169 0.6778 0.0028  0.0809  -0.0527 233 VAL A CG2 
1587  N  N   . VAL A 233 ? 0.3015 0.3711 0.7396 -0.0045 0.0779  -0.0278 234 VAL A N   
1588  C  CA  . VAL A 233 ? 0.2607 0.3299 0.7092 -0.0075 0.0748  -0.0191 234 VAL A CA  
1589  C  C   . VAL A 233 ? 0.2486 0.3347 0.7008 -0.0189 0.0775  -0.0131 234 VAL A C   
1590  O  O   . VAL A 233 ? 0.2442 0.3356 0.7011 -0.0259 0.0778  -0.0089 234 VAL A O   
1591  C  CB  . VAL A 233 ? 0.2610 0.3176 0.7135 -0.0025 0.0687  -0.0137 234 VAL A CB  
1592  C  CG1 . VAL A 233 ? 0.2475 0.3036 0.7149 -0.0062 0.0644  -0.0042 234 VAL A CG1 
1593  C  CG2 . VAL A 233 ? 0.2871 0.3286 0.7320 0.0036  0.0661  -0.0190 234 VAL A CG2 
1594  N  N   . ARG A 234 ? 0.2673 0.3621 0.7156 -0.0229 0.0792  -0.0122 235 ARG A N   
1595  C  CA  . ARG A 234 ? 0.2156 0.3269 0.6631 -0.0378 0.0812  -0.0055 235 ARG A CA  
1596  C  C   . ARG A 234 ? 0.2957 0.4214 0.7378 -0.0469 0.0889  -0.0116 235 ARG A C   
1597  O  O   . ARG A 234 ? 0.2981 0.4333 0.7395 -0.0605 0.0892  -0.0039 235 ARG A O   
1598  C  CB  . ARG A 234 ? 0.3216 0.4410 0.7638 -0.0412 0.0827  -0.0061 235 ARG A CB  
1599  C  CG  . ARG A 234 ? 0.4128 0.5505 0.8496 -0.0599 0.0852  0.0003  235 ARG A CG  
1600  C  CD  . ARG A 234 ? 0.5561 0.7024 0.9873 -0.0638 0.0870  -0.0018 235 ARG A CD  
1601  N  NE  . ARG A 234 ? 0.6092 0.7564 1.0344 -0.0549 0.0943  -0.0184 235 ARG A NE  
1602  C  CZ  . ARG A 234 ? 0.6782 0.8385 1.0957 -0.0607 0.1037  -0.0304 235 ARG A CZ  
1603  N  NH1 . ARG A 234 ? 0.7121 0.8878 1.1246 -0.0763 0.1084  -0.0287 235 ARG A NH1 
1604  N  NH2 . ARG A 234 ? 0.6975 0.8543 1.1121 -0.0516 0.1078  -0.0439 235 ARG A NH2 
1605  N  N   . LYS A 235 ? 0.1899 0.3159 0.6281 -0.0400 0.0943  -0.0249 236 LYS A N   
1606  C  CA  . LYS A 235 ? 0.3372 0.4774 0.7728 -0.0472 0.1020  -0.0330 236 LYS A CA  
1607  C  C   . LYS A 235 ? 0.3300 0.4662 0.7720 -0.0463 0.1002  -0.0311 236 LYS A C   
1608  O  O   . LYS A 235 ? 0.3374 0.4871 0.7786 -0.0575 0.1044  -0.0305 236 LYS A O   
1609  C  CB  . LYS A 235 ? 0.3375 0.4777 0.7700 -0.0400 0.1067  -0.0475 236 LYS A CB  
1610  C  CG  . LYS A 235 ? 0.3546 0.5043 0.7802 -0.0446 0.1111  -0.0520 236 LYS A CG  
1611  C  CD  . LYS A 235 ? 0.3971 0.5401 0.8218 -0.0354 0.1130  -0.0648 236 LYS A CD  
1612  C  CE  . LYS A 235 ? 0.4421 0.5941 0.8605 -0.0401 0.1173  -0.0699 236 LYS A CE  
1613  N  NZ  . LYS A 235 ? 0.4418 0.5802 0.8603 -0.0295 0.1150  -0.0773 236 LYS A NZ  
1614  N  N   . VAL A 236 ? 0.2701 0.3884 0.7175 -0.0343 0.0940  -0.0302 237 VAL A N   
1615  C  CA  . VAL A 236 ? 0.2996 0.4127 0.7538 -0.0330 0.0915  -0.0285 237 VAL A CA  
1616  C  C   . VAL A 236 ? 0.3386 0.4539 0.7968 -0.0427 0.0882  -0.0162 237 VAL A C   
1617  O  O   . VAL A 236 ? 0.3047 0.4251 0.7660 -0.0488 0.0891  -0.0148 237 VAL A O   
1618  C  CB  . VAL A 236 ? 0.3427 0.4361 0.7995 -0.0204 0.0851  -0.0296 237 VAL A CB  
1619  C  CG1 . VAL A 236 ? 0.3078 0.3956 0.7727 -0.0204 0.0814  -0.0259 237 VAL A CG1 
1620  C  CG2 . VAL A 236 ? 0.2983 0.3883 0.7512 -0.0140 0.0864  -0.0398 237 VAL A CG2 
1621  N  N   . ALA A 237 ? 0.3751 0.4860 0.8338 -0.0448 0.0836  -0.0067 238 ALA A N   
1622  C  CA  . ALA A 237 ? 0.3924 0.5015 0.8554 -0.0549 0.0778  0.0074  238 ALA A CA  
1623  C  C   . ALA A 237 ? 0.4450 0.5715 0.9010 -0.0726 0.0823  0.0111  238 ALA A C   
1624  O  O   . ALA A 237 ? 0.5683 0.6922 1.0262 -0.0818 0.0775  0.0221  238 ALA A O   
1625  C  CB  . ALA A 237 ? 0.2564 0.3592 0.7215 -0.0553 0.0713  0.0172  238 ALA A CB  
1626  N  N   . GLN A 238 ? 0.5030 0.6466 0.9503 -0.0778 0.0916  0.0015  239 GLN A N   
1627  C  CA  . GLN A 238 ? 0.5372 0.7004 0.9756 -0.0966 0.0977  0.0032  239 GLN A CA  
1628  C  C   . GLN A 238 ? 0.4844 0.6555 0.9253 -0.0975 0.1032  -0.0052 239 GLN A C   
1629  O  O   . GLN A 238 ? 0.4659 0.6540 0.9000 -0.1134 0.1087  -0.0044 239 GLN A O   
1630  C  CB  . GLN A 238 ? 0.6301 0.8101 1.0578 -0.1037 0.1057  -0.0045 239 GLN A CB  
1631  C  CG  . GLN A 238 ? 0.7483 0.9244 1.1728 -0.1069 0.1003  0.0053  239 GLN A CG  
1632  C  CD  . GLN A 238 ? 0.8466 1.0236 1.2667 -0.1250 0.0929  0.0251  239 GLN A CD  
1633  O  OE1 . GLN A 238 ? 0.9053 1.0879 1.3220 -0.1374 0.0932  0.0310  239 GLN A OE1 
1634  N  NE2 . GLN A 238 ? 0.8803 1.0490 1.2942 -0.1254 0.0835  0.0362  239 GLN A NE2 
1635  N  N   . VAL A 239 ? 0.4111 0.5705 0.8613 -0.0816 0.1015  -0.0128 240 VAL A N   
1636  C  CA  . VAL A 239 ? 0.4598 0.6250 0.9151 -0.0815 0.1049  -0.0196 240 VAL A CA  
1637  C  C   . VAL A 239 ? 0.4629 0.6272 0.9201 -0.0924 0.1007  -0.0078 240 VAL A C   
1638  O  O   . VAL A 239 ? 0.3787 0.5256 0.8416 -0.0877 0.0918  0.0015  240 VAL A O   
1639  C  CB  . VAL A 239 ? 0.3805 0.5311 0.8450 -0.0637 0.1016  -0.0275 240 VAL A CB  
1640  C  CG1 . VAL A 239 ? 0.3333 0.4898 0.8049 -0.0645 0.1037  -0.0329 240 VAL A CG1 
1641  C  CG2 . VAL A 239 ? 0.3749 0.5242 0.8366 -0.0542 0.1047  -0.0383 240 VAL A CG2 
1642  N  N   . PRO A 240 ? 0.5600 0.7429 1.0121 -0.1076 0.1069  -0.0084 241 PRO A N   
1643  C  CA  . PRO A 240 ? 0.5532 0.7368 1.0043 -0.1215 0.1031  0.0039  241 PRO A CA  
1644  C  C   . PRO A 240 ? 0.4944 0.6685 0.9572 -0.1135 0.0993  0.0021  241 PRO A C   
1645  O  O   . PRO A 240 ? 0.4147 0.5901 0.8851 -0.1019 0.1025  -0.0103 241 PRO A O   
1646  C  CB  . PRO A 240 ? 0.6221 0.8318 1.0628 -0.1401 0.1129  0.0008  241 PRO A CB  
1647  C  CG  . PRO A 240 ? 0.6325 0.8527 1.0766 -0.1298 0.1219  -0.0178 241 PRO A CG  
1648  C  CD  . PRO A 240 ? 0.5948 0.7992 1.0419 -0.1129 0.1181  -0.0214 241 PRO A CD  
1649  N  N   . LEU A 241 ? 0.5032 0.6667 0.9675 -0.1202 0.0916  0.0151  242 LEU A N   
1650  C  CA  . LEU A 241 ? 0.4877 0.6440 0.9620 -0.1160 0.0880  0.0143  242 LEU A CA  
1651  C  C   . LEU A 241 ? 0.4623 0.6396 0.9352 -0.1282 0.0956  0.0095  242 LEU A C   
1652  O  O   . LEU A 241 ? 0.4625 0.6561 0.9247 -0.1458 0.1004  0.0140  242 LEU A O   
1653  C  CB  . LEU A 241 ? 0.4988 0.6355 0.9754 -0.1192 0.0768  0.0292  242 LEU A CB  
1654  C  CG  . LEU A 241 ? 0.5345 0.6494 1.0162 -0.1061 0.0684  0.0333  242 LEU A CG  
1655  C  CD1 . LEU A 241 ? 0.4981 0.5965 0.9802 -0.1130 0.0574  0.0495  242 LEU A CD1 
1656  C  CD2 . LEU A 241 ? 0.5278 0.6318 1.0206 -0.0887 0.0670  0.0231  242 LEU A CD2 
1657  N  N   . GLY A 242 ? 0.4632 0.6411 0.9471 -0.1198 0.0964  0.0007  243 GLY A N   
1658  C  CA  . GLY A 242 ? 0.4535 0.6517 0.9395 -0.1293 0.1034  -0.0050 243 GLY A CA  
1659  C  C   . GLY A 242 ? 0.4714 0.6697 0.9559 -0.1441 0.0996  0.0061  243 GLY A C   
1660  O  O   . GLY A 242 ? 0.4877 0.6668 0.9716 -0.1446 0.0902  0.0178  243 GLY A O   
1661  N  N   . PRO A 243 ? 0.4541 0.6737 0.9386 -0.1562 0.1065  0.0025  244 PRO A N   
1662  C  CA  . PRO A 243 ? 0.4395 0.6617 0.9225 -0.1718 0.1036  0.0123  244 PRO A CA  
1663  C  C   . PRO A 243 ? 0.4176 0.6218 0.9134 -0.1614 0.0953  0.0129  244 PRO A C   
1664  O  O   . PRO A 243 ? 0.4492 0.6399 0.9430 -0.1686 0.0876  0.0246  244 PRO A O   
1665  C  CB  . PRO A 243 ? 0.4382 0.6897 0.9220 -0.1824 0.1146  0.0040  244 PRO A CB  
1666  C  CG  . PRO A 243 ? 0.4594 0.7230 0.9401 -0.1769 0.1232  -0.0069 244 PRO A CG  
1667  C  CD  . PRO A 243 ? 0.4360 0.6786 0.9226 -0.1559 0.1178  -0.0116 244 PRO A CD  
1668  N  N   . GLU A 244 ? 0.3602 0.5639 0.8690 -0.1450 0.0965  0.0005  245 GLU A N   
1669  C  CA  . GLU A 244 ? 0.4089 0.5968 0.9297 -0.1345 0.0886  -0.0002 245 GLU A CA  
1670  C  C   . GLU A 244 ? 0.3789 0.5404 0.8973 -0.1281 0.0787  0.0089  245 GLU A C   
1671  O  O   . GLU A 244 ? 0.4585 0.6064 0.9802 -0.1302 0.0711  0.0156  245 GLU A O   
1672  C  CB  . GLU A 244 ? 0.4596 0.6500 0.9927 -0.1183 0.0904  -0.0137 245 GLU A CB  
1673  C  CG  . GLU A 244 ? 0.5983 0.8128 1.1387 -0.1223 0.0989  -0.0238 245 GLU A CG  
1674  C  CD  . GLU A 244 ? 0.7975 1.0213 1.3432 -0.1342 0.0985  -0.0204 245 GLU A CD  
1675  O  OE1 . GLU A 244 ? 0.8446 1.0538 1.3955 -0.1316 0.0901  -0.0155 245 GLU A OE1 
1676  O  OE2 . GLU A 244 ? 0.8408 1.0869 1.3853 -0.1466 0.1067  -0.0229 245 GLU A OE2 
1677  N  N   . CYS A 245 ? 0.3506 0.5052 0.8641 -0.1201 0.0788  0.0083  246 CYS A N   
1678  C  CA  . CYS A 245 ? 0.3590 0.4903 0.8715 -0.1134 0.0702  0.0160  246 CYS A CA  
1679  C  C   . CYS A 245 ? 0.3052 0.4285 0.8108 -0.1274 0.0646  0.0308  246 CYS A C   
1680  O  O   . CYS A 245 ? 0.2928 0.3960 0.8026 -0.1242 0.0555  0.0372  246 CYS A O   
1681  C  CB  . CYS A 245 ? 0.3524 0.4814 0.8603 -0.1044 0.0724  0.0128  246 CYS A CB  
1682  S  SG  . CYS A 245 ? 0.7101 0.8121 1.2197 -0.0942 0.0624  0.0200  246 CYS A SG  
1683  N  N   . SER A 246 ? 0.3023 0.4413 0.7970 -0.1437 0.0696  0.0361  247 SER A N   
1684  C  CA  . SER A 246 ? 0.4839 0.6157 0.9699 -0.1596 0.0634  0.0521  247 SER A CA  
1685  C  C   . SER A 246 ? 0.4330 0.5566 0.9245 -0.1649 0.0576  0.0566  247 SER A C   
1686  O  O   . SER A 246 ? 0.4369 0.5390 0.9295 -0.1653 0.0471  0.0673  247 SER A O   
1687  C  CB  . SER A 246 ? 0.4547 0.6090 0.9262 -0.1790 0.0713  0.0556  247 SER A CB  
1688  O  OG  . SER A 246 ? 0.5461 0.6905 1.0065 -0.1941 0.0637  0.0729  247 SER A OG  
1689  N  N   . ARG A 247 ? 0.3762 0.5167 0.8723 -0.1684 0.0641  0.0481  248 ARG A N   
1690  C  CA  . ARG A 247 ? 0.4497 0.5848 0.9515 -0.1739 0.0595  0.0510  248 ARG A CA  
1691  C  C   . ARG A 247 ? 0.4455 0.5571 0.9590 -0.1580 0.0505  0.0488  248 ARG A C   
1692  O  O   . ARG A 247 ? 0.3823 0.4777 0.8979 -0.1616 0.0421  0.0565  248 ARG A O   
1693  C  CB  . ARG A 247 ? 0.5200 0.6797 1.0271 -0.1789 0.0683  0.0409  248 ARG A CB  
1694  C  CG  . ARG A 247 ? 0.6284 0.8140 1.1243 -0.1984 0.0776  0.0425  248 ARG A CG  
1695  C  CD  . ARG A 247 ? 0.6803 0.8900 1.1850 -0.2020 0.0854  0.0322  248 ARG A CD  
1696  N  NE  . ARG A 247 ? 0.7350 0.9475 1.2539 -0.1822 0.0881  0.0176  248 ARG A NE  
1697  C  CZ  . ARG A 247 ? 0.7780 0.9820 1.3108 -0.1714 0.0831  0.0127  248 ARG A CZ  
1698  N  NH1 . ARG A 247 ? 0.7843 0.9767 1.3189 -0.1776 0.0759  0.0201  248 ARG A NH1 
1699  N  NH2 . ARG A 247 ? 0.7754 0.9817 1.3196 -0.1550 0.0847  0.0008  248 ARG A NH2 
1700  N  N   . ALA A 248 ? 0.3495 0.4598 0.8702 -0.1412 0.0524  0.0379  249 ALA A N   
1701  C  CA  . ALA A 248 ? 0.3744 0.4655 0.9047 -0.1274 0.0451  0.0340  249 ALA A CA  
1702  C  C   . ALA A 248 ? 0.3528 0.4204 0.8817 -0.1241 0.0364  0.0426  249 ALA A C   
1703  O  O   . ALA A 248 ? 0.3402 0.3907 0.8758 -0.1196 0.0290  0.0427  249 ALA A O   
1704  C  CB  . ALA A 248 ? 0.2853 0.3808 0.8212 -0.1123 0.0489  0.0217  249 ALA A CB  
1705  N  N   . VAL A 249 ? 0.3503 0.4179 0.8713 -0.1265 0.0371  0.0491  250 VAL A N   
1706  C  CA  . VAL A 249 ? 0.3196 0.3663 0.8407 -0.1232 0.0283  0.0579  250 VAL A CA  
1707  C  C   . VAL A 249 ? 0.4409 0.4774 0.9596 -0.1362 0.0202  0.0714  250 VAL A C   
1708  O  O   . VAL A 249 ? 0.4374 0.4530 0.9629 -0.1314 0.0108  0.0753  250 VAL A O   
1709  C  CB  . VAL A 249 ? 0.4321 0.4829 0.9457 -0.1224 0.0307  0.0616  250 VAL A CB  
1710  C  CG1 . VAL A 249 ? 0.4540 0.4853 0.9678 -0.1230 0.0200  0.0742  250 VAL A CG1 
1711  C  CG2 . VAL A 249 ? 0.2932 0.3471 0.8110 -0.1069 0.0360  0.0489  250 VAL A CG2 
1712  N  N   . MET A 250 ? 0.4533 0.5050 0.9626 -0.1530 0.0241  0.0776  251 MET A N   
1713  C  CA  . MET A 250 ? 0.3810 0.4241 0.8867 -0.1671 0.0168  0.0905  251 MET A CA  
1714  C  C   . MET A 250 ? 0.3832 0.4144 0.9002 -0.1625 0.0120  0.0858  251 MET A C   
1715  O  O   . MET A 250 ? 0.3989 0.4104 0.9199 -0.1635 0.0018  0.0936  251 MET A O   
1716  C  CB  . MET A 250 ? 0.4107 0.4760 0.9036 -0.1872 0.0241  0.0951  251 MET A CB  
1717  C  CG  . MET A 250 ? 0.4518 0.5102 0.9413 -0.2026 0.0178  0.1066  251 MET A CG  
1718  S  SD  . MET A 250 ? 0.5123 0.5406 1.0014 -0.2029 0.0009  0.1249  251 MET A SD  
1719  C  CE  . MET A 250 ? 0.5166 0.5370 1.0064 -0.2171 -0.0053 0.1332  251 MET A CE  
1720  N  N   . LYS A 251 ? 0.3685 0.4121 0.8912 -0.1575 0.0188  0.0727  252 LYS A N   
1721  C  CA  . LYS A 251 ? 0.4460 0.4807 0.9788 -0.1534 0.0148  0.0669  252 LYS A CA  
1722  C  C   . LYS A 251 ? 0.4099 0.4221 0.9516 -0.1386 0.0074  0.0629  252 LYS A C   
1723  O  O   . LYS A 251 ? 0.4555 0.4522 1.0036 -0.1383 0.0003  0.0634  252 LYS A O   
1724  C  CB  . LYS A 251 ? 0.4239 0.4775 0.9616 -0.1500 0.0228  0.0541  252 LYS A CB  
1725  C  CG  . LYS A 251 ? 0.4907 0.5381 1.0377 -0.1483 0.0186  0.0484  252 LYS A CG  
1726  C  CD  . LYS A 251 ? 0.4660 0.5361 1.0167 -0.1523 0.0255  0.0410  252 LYS A CD  
1727  C  CE  . LYS A 251 ? 0.5149 0.5794 1.0741 -0.1528 0.0204  0.0369  252 LYS A CE  
1728  N  NZ  . LYS A 251 ? 0.5350 0.5877 1.1009 -0.1383 0.0164  0.0277  252 LYS A NZ  
1729  N  N   . LEU A 252 ? 0.3488 0.3603 0.8908 -0.1268 0.0099  0.0579  253 LEU A N   
1730  C  CA  . LEU A 252 ? 0.3431 0.3368 0.8931 -0.1129 0.0049  0.0519  253 LEU A CA  
1731  C  C   . LEU A 252 ? 0.3608 0.3344 0.9142 -0.1138 -0.0050 0.0617  253 LEU A C   
1732  O  O   . LEU A 252 ? 0.3663 0.3246 0.9291 -0.1076 -0.0107 0.0569  253 LEU A O   
1733  C  CB  . LEU A 252 ? 0.3235 0.3228 0.8721 -0.1018 0.0103  0.0455  253 LEU A CB  
1734  C  CG  . LEU A 252 ? 0.3174 0.3012 0.8733 -0.0883 0.0066  0.0387  253 LEU A CG  
1735  C  CD1 . LEU A 252 ? 0.3125 0.2931 0.8746 -0.0824 0.0067  0.0261  253 LEU A CD1 
1736  C  CD2 . LEU A 252 ? 0.3075 0.2968 0.8603 -0.0800 0.0115  0.0358  253 LEU A CD2 
1737  N  N   . VAL A 253 ? 0.3712 0.3459 0.9174 -0.1220 -0.0073 0.0751  254 VAL A N   
1738  C  CA  . VAL A 253 ? 0.5467 0.5032 1.0977 -0.1208 -0.0179 0.0853  254 VAL A CA  
1739  C  C   . VAL A 253 ? 0.5984 0.5454 1.1495 -0.1333 -0.0266 0.0979  254 VAL A C   
1740  O  O   . VAL A 253 ? 0.6407 0.5702 1.2035 -0.1286 -0.0349 0.0975  254 VAL A O   
1741  C  CB  . VAL A 253 ? 0.4922 0.4534 1.0356 -0.1222 -0.0179 0.0944  254 VAL A CB  
1742  C  CG1 . VAL A 253 ? 0.5254 0.4682 1.0764 -0.1200 -0.0305 0.1054  254 VAL A CG1 
1743  C  CG2 . VAL A 253 ? 0.4547 0.4242 0.9985 -0.1098 -0.0097 0.0823  254 VAL A CG2 
1744  N  N   . TYR A 254 ? 0.5148 0.4742 1.0531 -0.1497 -0.0241 0.1081  255 TYR A N   
1745  C  CA  . TYR A 254 ? 0.5181 0.4687 1.0538 -0.1636 -0.0332 0.1233  255 TYR A CA  
1746  C  C   . TYR A 254 ? 0.5672 0.5230 1.1015 -0.1743 -0.0306 0.1216  255 TYR A C   
1747  O  O   . TYR A 254 ? 0.5726 0.5213 1.1045 -0.1867 -0.0377 0.1337  255 TYR A O   
1748  C  CB  . TYR A 254 ? 0.5099 0.4695 1.0302 -0.1775 -0.0340 0.1389  255 TYR A CB  
1749  C  CG  . TYR A 254 ? 0.5213 0.4722 1.0442 -0.1690 -0.0404 0.1448  255 TYR A CG  
1750  C  CD1 . TYR A 254 ? 0.5605 0.4896 1.0994 -0.1581 -0.0526 0.1474  255 TYR A CD1 
1751  C  CD2 . TYR A 254 ? 0.4758 0.4416 0.9867 -0.1718 -0.0341 0.1464  255 TYR A CD2 
1752  C  CE1 . TYR A 254 ? 0.5384 0.4611 1.0822 -0.1500 -0.0588 0.1522  255 TYR A CE1 
1753  C  CE2 . TYR A 254 ? 0.4716 0.4299 0.9853 -0.1643 -0.0404 0.1520  255 TYR A CE2 
1754  C  CZ  . TYR A 254 ? 0.5058 0.4427 1.0364 -0.1533 -0.0530 0.1551  255 TYR A CZ  
1755  O  OH  . TYR A 254 ? 0.5605 0.4914 1.0963 -0.1457 -0.0596 0.1602  255 TYR A OH  
1756  N  N   . CYS A 255 ? 0.5688 0.5372 1.1052 -0.1699 -0.0214 0.1070  256 CYS A N   
1757  C  CA  . CYS A 255 ? 0.4513 0.4248 0.9887 -0.1789 -0.0195 0.1042  256 CYS A CA  
1758  C  C   . CYS A 255 ? 0.4621 0.4139 1.0126 -0.1730 -0.0287 0.1014  256 CYS A C   
1759  O  O   . CYS A 255 ? 0.4771 0.4269 1.0289 -0.1825 -0.0310 0.1035  256 CYS A O   
1760  C  CB  . CYS A 255 ? 0.4291 0.4234 0.9669 -0.1754 -0.0083 0.0899  256 CYS A CB  
1761  S  SG  . CYS A 255 ? 0.7821 0.8076 1.3065 -0.1913 0.0037  0.0924  256 CYS A SG  
1762  N  N   . ALA A 256 ? 0.4553 0.3920 1.0158 -0.1577 -0.0332 0.0955  257 ALA A N   
1763  C  CA  . ALA A 256 ? 0.5955 0.5117 1.1695 -0.1520 -0.0417 0.0918  257 ALA A CA  
1764  C  C   . ALA A 256 ? 0.5945 0.4973 1.1700 -0.1623 -0.0525 0.1085  257 ALA A C   
1765  O  O   . ALA A 256 ? 0.5148 0.4070 1.0969 -0.1672 -0.0581 0.1095  257 ALA A O   
1766  C  CB  . ALA A 256 ? 0.4556 0.3618 1.0402 -0.1345 -0.0430 0.0814  257 ALA A CB  
1767  N  N   . HIS A 257 ? 0.5414 0.4448 1.1103 -0.1660 -0.0559 0.1220  258 HIS A N   
1768  C  CA  . HIS A 257 ? 0.5496 0.4417 1.1182 -0.1769 -0.0674 0.1405  258 HIS A CA  
1769  C  C   . HIS A 257 ? 0.5895 0.4899 1.1471 -0.1960 -0.0655 0.1486  258 HIS A C   
1770  O  O   . HIS A 257 ? 0.6104 0.4977 1.1740 -0.2028 -0.0743 0.1562  258 HIS A O   
1771  C  CB  . HIS A 257 ? 0.5739 0.4690 1.1344 -0.1790 -0.0707 0.1538  258 HIS A CB  
1772  C  CG  . HIS A 257 ? 0.6165 0.5036 1.1891 -0.1612 -0.0735 0.1473  258 HIS A CG  
1773  N  ND1 . HIS A 257 ? 0.6484 0.5385 1.2276 -0.1461 -0.0653 0.1283  258 HIS A ND1 
1774  C  CD2 . HIS A 257 ? 0.6572 0.5346 1.2369 -0.1568 -0.0838 0.1575  258 HIS A CD2 
1775  C  CE1 . HIS A 257 ? 0.6520 0.5351 1.2415 -0.1333 -0.0693 0.1262  258 HIS A CE1 
1776  N  NE2 . HIS A 257 ? 0.6876 0.5631 1.2786 -0.1391 -0.0807 0.1435  258 HIS A NE2 
1777  N  N   . CYS A 258 ? 0.5697 0.4928 1.1126 -0.2046 -0.0537 0.1461  259 CYS A N   
1778  C  CA  . CYS A 258 ? 0.6391 0.5750 1.1710 -0.2239 -0.0496 0.1525  259 CYS A CA  
1779  C  C   . CYS A 258 ? 0.6293 0.5611 1.1703 -0.2249 -0.0495 0.1439  259 CYS A C   
1780  O  O   . CYS A 258 ? 0.6947 0.6261 1.2323 -0.2398 -0.0520 0.1523  259 CYS A O   
1781  C  CB  . CYS A 258 ? 0.6431 0.6074 1.1607 -0.2312 -0.0353 0.1478  259 CYS A CB  
1782  S  SG  . CYS A 258 ? 0.6200 0.5932 1.1214 -0.2384 -0.0345 0.1608  259 CYS A SG  
1783  N  N   . LEU A 259 ? 0.6205 0.5496 1.1725 -0.2099 -0.0467 0.1273  260 LEU A N   
1784  C  CA  . LEU A 259 ? 0.5750 0.5021 1.1348 -0.2109 -0.0463 0.1180  260 LEU A CA  
1785  C  C   . LEU A 259 ? 0.6736 0.5747 1.2480 -0.2045 -0.0576 0.1173  260 LEU A C   
1786  O  O   . LEU A 259 ? 0.7320 0.6286 1.3147 -0.2015 -0.0576 0.1062  260 LEU A O   
1787  C  CB  . LEU A 259 ? 0.5532 0.4938 1.1159 -0.2003 -0.0371 0.1001  260 LEU A CB  
1788  C  CG  . LEU A 259 ? 0.5943 0.5632 1.1471 -0.2065 -0.0253 0.0975  260 LEU A CG  
1789  C  CD1 . LEU A 259 ? 0.5878 0.5683 1.1470 -0.1978 -0.0193 0.0811  260 LEU A CD1 
1790  C  CD2 . LEU A 259 ? 0.6348 0.6163 1.1785 -0.2271 -0.0227 0.1077  260 LEU A CD2 
1791  N  N   . GLY A 260 ? 0.7346 0.6196 1.3132 -0.2027 -0.0674 0.1288  261 GLY A N   
1792  C  CA  . GLY A 260 ? 0.7801 0.6418 1.3748 -0.1988 -0.0788 0.1299  261 GLY A CA  
1793  C  C   . GLY A 260 ? 0.7917 0.6402 1.4027 -0.1797 -0.0814 0.1164  261 GLY A C   
1794  O  O   . GLY A 260 ? 0.8506 0.6819 1.4774 -0.1758 -0.0889 0.1126  261 GLY A O   
1795  N  N   . VAL A 261 ? 0.7934 0.6507 1.4014 -0.1683 -0.0749 0.1084  262 VAL A N   
1796  C  CA  . VAL A 261 ? 0.7384 0.5859 1.3610 -0.1510 -0.0759 0.0947  262 VAL A CA  
1797  C  C   . VAL A 261 ? 0.7263 0.5768 1.3478 -0.1424 -0.0759 0.0988  262 VAL A C   
1798  O  O   . VAL A 261 ? 0.7446 0.6046 1.3626 -0.1328 -0.0676 0.0874  262 VAL A O   
1799  C  CB  . VAL A 261 ? 0.6927 0.5476 1.3150 -0.1436 -0.0666 0.0741  262 VAL A CB  
1800  C  CG1 . VAL A 261 ? 0.6985 0.5441 1.3290 -0.1477 -0.0694 0.0666  262 VAL A CG1 
1801  C  CG2 . VAL A 261 ? 0.6828 0.5595 1.2889 -0.1488 -0.0564 0.0734  262 VAL A CG2 
1802  N  N   . PRO A 262 ? 0.7070 0.5492 1.3320 -0.1461 -0.0860 0.1155  263 PRO A N   
1803  C  CA  . PRO A 262 ? 0.6850 0.5303 1.3086 -0.1396 -0.0873 0.1214  263 PRO A CA  
1804  C  C   . PRO A 262 ? 0.6810 0.5199 1.3222 -0.1215 -0.0873 0.1066  263 PRO A C   
1805  O  O   . PRO A 262 ? 0.6628 0.5082 1.3017 -0.1139 -0.0843 0.1053  263 PRO A O   
1806  C  CB  . PRO A 262 ? 0.7241 0.5602 1.3498 -0.1496 -0.1008 0.1434  263 PRO A CB  
1807  C  CG  . PRO A 262 ? 0.7121 0.5335 1.3516 -0.1532 -0.1086 0.1435  263 PRO A CG  
1808  C  CD  . PRO A 262 ? 0.7228 0.5515 1.3545 -0.1565 -0.0979 0.1300  263 PRO A CD  
1809  N  N   . GLY A 263 ? 0.6745 0.5018 1.3329 -0.1155 -0.0900 0.0948  264 GLY A N   
1810  C  CA  . GLY A 263 ? 0.6257 0.4492 1.3013 -0.0999 -0.0884 0.0782  264 GLY A CA  
1811  C  C   . GLY A 263 ? 0.6332 0.4684 1.2995 -0.0929 -0.0751 0.0595  264 GLY A C   
1812  O  O   . GLY A 263 ? 0.6524 0.4892 1.3272 -0.0810 -0.0711 0.0461  264 GLY A O   
1813  N  N   . ALA A 264 ? 0.6350 0.4795 1.2846 -0.1009 -0.0683 0.0587  265 ALA A N   
1814  C  CA  . ALA A 264 ? 0.6288 0.4851 1.2696 -0.0957 -0.0570 0.0427  265 ALA A CA  
1815  C  C   . ALA A 264 ? 0.7147 0.5832 1.3460 -0.0903 -0.0511 0.0442  265 ALA A C   
1816  O  O   . ALA A 264 ? 0.7704 0.6443 1.3925 -0.0965 -0.0525 0.0592  265 ALA A O   
1817  C  CB  . ALA A 264 ? 0.6644 0.5284 1.2934 -0.1063 -0.0529 0.0423  265 ALA A CB  
1818  N  N   . ARG A 265 ? 0.6274 0.5007 1.2600 -0.0797 -0.0442 0.0284  266 ARG A N   
1819  C  CA  . ARG A 265 ? 0.6198 0.5043 1.2442 -0.0738 -0.0381 0.0280  266 ARG A CA  
1820  C  C   . ARG A 265 ? 0.6068 0.5044 1.2196 -0.0735 -0.0285 0.0173  266 ARG A C   
1821  O  O   . ARG A 265 ? 0.5387 0.4350 1.1526 -0.0740 -0.0267 0.0057  266 ARG A O   
1822  C  CB  . ARG A 265 ? 0.6674 0.5477 1.3040 -0.0618 -0.0386 0.0199  266 ARG A CB  
1823  C  CG  . ARG A 265 ? 0.7583 0.6312 1.4051 -0.0614 -0.0481 0.0341  266 ARG A CG  
1824  C  CD  . ARG A 265 ? 0.8223 0.7035 1.4555 -0.0660 -0.0477 0.0493  266 ARG A CD  
1825  N  NE  . ARG A 265 ? 0.9308 0.8047 1.5708 -0.0694 -0.0587 0.0663  266 ARG A NE  
1826  C  CZ  . ARG A 265 ? 1.0121 0.8851 1.6429 -0.0821 -0.0645 0.0844  266 ARG A CZ  
1827  N  NH1 . ARG A 265 ? 1.0258 0.9062 1.6415 -0.0924 -0.0590 0.0866  266 ARG A NH1 
1828  N  NH2 . ARG A 265 ? 1.0547 0.9209 1.6917 -0.0855 -0.0758 0.1004  266 ARG A NH2 
1829  N  N   . PRO A 266 ? 0.5131 0.4233 1.1151 -0.0731 -0.0230 0.0214  267 PRO A N   
1830  C  CA  . PRO A 266 ? 0.4875 0.4115 1.0802 -0.0736 -0.0152 0.0137  267 PRO A CA  
1831  C  C   . PRO A 266 ? 0.3491 0.2734 0.9436 -0.0650 -0.0110 -0.0035 267 PRO A C   
1832  O  O   . PRO A 266 ? 0.3468 0.2663 0.9467 -0.0567 -0.0107 -0.0094 267 PRO A O   
1833  C  CB  . PRO A 266 ? 0.3450 0.2808 0.9291 -0.0735 -0.0108 0.0215  267 PRO A CB  
1834  C  CG  . PRO A 266 ? 0.3588 0.2882 0.9440 -0.0785 -0.0171 0.0369  267 PRO A CG  
1835  C  CD  . PRO A 266 ? 0.6201 0.5329 1.2187 -0.0736 -0.0246 0.0345  267 PRO A CD  
1836  N  N   . CYS A 267 ? 0.4809 0.4120 1.0708 -0.0681 -0.0081 -0.0112 268 CYS A N   
1837  C  CA  A CYS A 267 ? 0.4636 0.3967 1.0518 -0.0626 -0.0043 -0.0263 268 CYS A CA  
1838  C  CA  B CYS A 267 ? 0.4540 0.3876 1.0420 -0.0627 -0.0042 -0.0263 268 CYS A CA  
1839  C  C   . CYS A 267 ? 0.3175 0.2601 0.9002 -0.0557 0.0011  -0.0273 268 CYS A C   
1840  O  O   . CYS A 267 ? 0.3076 0.2600 0.8857 -0.0572 0.0034  -0.0187 268 CYS A O   
1841  C  CB  A CYS A 267 ? 0.4483 0.3874 1.0325 -0.0691 -0.0042 -0.0321 268 CYS A CB  
1842  C  CB  B CYS A 267 ? 0.4279 0.3684 1.0116 -0.0692 -0.0039 -0.0315 268 CYS A CB  
1843  S  SG  A CYS A 267 ? 0.6683 0.5954 1.2588 -0.0771 -0.0102 -0.0345 268 CYS A SG  
1844  S  SG  B CYS A 267 ? 0.5060 0.4502 1.0842 -0.0659 -0.0007 -0.0482 268 CYS A SG  
1845  N  N   . PRO A 268 ? 0.3815 0.3217 0.9648 -0.0489 0.0037  -0.0386 269 PRO A N   
1846  C  CA  . PRO A 268 ? 0.3643 0.3123 0.9425 -0.0424 0.0088  -0.0406 269 PRO A CA  
1847  C  C   . PRO A 268 ? 0.4170 0.3780 0.9875 -0.0446 0.0116  -0.0390 269 PRO A C   
1848  O  O   . PRO A 268 ? 0.3981 0.3667 0.9660 -0.0420 0.0144  -0.0325 269 PRO A O   
1849  C  CB  . PRO A 268 ? 0.4150 0.3588 0.9937 -0.0385 0.0111  -0.0557 269 PRO A CB  
1850  C  CG  . PRO A 268 ? 0.4326 0.3648 1.0214 -0.0395 0.0072  -0.0587 269 PRO A CG  
1851  C  CD  . PRO A 268 ? 0.3865 0.3161 0.9763 -0.0472 0.0024  -0.0501 269 PRO A CD  
1852  N  N   . ASP A 269 ? 0.4163 0.3805 0.9840 -0.0495 0.0104  -0.0450 270 ASP A N   
1853  C  CA  . ASP A 269 ? 0.4153 0.3931 0.9787 -0.0512 0.0116  -0.0436 270 ASP A CA  
1854  C  C   . ASP A 269 ? 0.4209 0.4076 0.9860 -0.0548 0.0119  -0.0324 270 ASP A C   
1855  O  O   . ASP A 269 ? 0.3480 0.3467 0.9112 -0.0531 0.0148  -0.0296 270 ASP A O   
1856  C  CB  . ASP A 269 ? 0.4207 0.4002 0.9818 -0.0568 0.0084  -0.0516 270 ASP A CB  
1857  C  CG  . ASP A 269 ? 0.4473 0.4223 1.0031 -0.0552 0.0093  -0.0636 270 ASP A CG  
1858  O  OD1 . ASP A 269 ? 0.5075 0.4807 1.0618 -0.0487 0.0132  -0.0655 270 ASP A OD1 
1859  O  OD2 . ASP A 269 ? 0.4941 0.4683 1.0465 -0.0615 0.0064  -0.0713 270 ASP A OD2 
1860  N  N   . TYR A 270 ? 0.3927 0.3735 0.9610 -0.0603 0.0092  -0.0267 271 TYR A N   
1861  C  CA  . TYR A 270 ? 0.4525 0.4416 1.0209 -0.0661 0.0101  -0.0161 271 TYR A CA  
1862  C  C   . TYR A 270 ? 0.3354 0.3284 0.9009 -0.0625 0.0141  -0.0095 271 TYR A C   
1863  O  O   . TYR A 270 ? 0.2674 0.2743 0.8299 -0.0629 0.0184  -0.0071 271 TYR A O   
1864  C  CB  . TYR A 270 ? 0.3992 0.3787 0.9710 -0.0736 0.0054  -0.0106 271 TYR A CB  
1865  C  CG  . TYR A 270 ? 0.3955 0.3832 0.9657 -0.0823 0.0062  0.0007  271 TYR A CG  
1866  C  CD1 . TYR A 270 ? 0.4036 0.4097 0.9714 -0.0847 0.0112  0.0019  271 TYR A CD1 
1867  C  CD2 . TYR A 270 ? 0.3271 0.3050 0.8987 -0.0890 0.0019  0.0097  271 TYR A CD2 
1868  C  CE1 . TYR A 270 ? 0.3966 0.4125 0.9622 -0.0942 0.0133  0.0106  271 TYR A CE1 
1869  C  CE2 . TYR A 270 ? 0.3320 0.3183 0.9000 -0.0993 0.0029  0.0202  271 TYR A CE2 
1870  C  CZ  . TYR A 270 ? 0.3806 0.3869 0.9452 -0.1023 0.0093  0.0200  271 TYR A CZ  
1871  O  OH  . TYR A 270 ? 0.3663 0.3835 0.9266 -0.1141 0.0116  0.0288  271 TYR A OH  
1872  N  N   . CYS A 271 ? 0.2814 0.2624 0.8482 -0.0590 0.0123  -0.0073 272 CYS A N   
1873  C  CA  . CYS A 271 ? 0.3342 0.3171 0.8983 -0.0557 0.0149  -0.0011 272 CYS A CA  
1874  C  C   . CYS A 271 ? 0.2574 0.2509 0.8176 -0.0493 0.0206  -0.0066 272 CYS A C   
1875  O  O   . CYS A 271 ? 0.2507 0.2538 0.8066 -0.0499 0.0246  -0.0017 272 CYS A O   
1876  C  CB  . CYS A 271 ? 0.2818 0.2502 0.8509 -0.0508 0.0110  -0.0006 272 CYS A CB  
1877  S  SG  . CYS A 271 ? 0.5694 0.5388 1.1363 -0.0472 0.0122  0.0077  272 CYS A SG  
1878  N  N   . ARG A 272 ? 0.2519 0.2439 0.8129 -0.0442 0.0208  -0.0168 273 ARG A N   
1879  C  CA  . ARG A 272 ? 0.3531 0.3531 0.9106 -0.0382 0.0248  -0.0216 273 ARG A CA  
1880  C  C   . ARG A 272 ? 0.2312 0.2459 0.7869 -0.0405 0.0270  -0.0205 273 ARG A C   
1881  O  O   . ARG A 272 ? 0.2464 0.2691 0.7987 -0.0367 0.0310  -0.0202 273 ARG A O   
1882  C  CB  . ARG A 272 ? 0.4241 0.4189 0.9814 -0.0347 0.0236  -0.0322 273 ARG A CB  
1883  C  CG  . ARG A 272 ? 0.4302 0.4184 0.9871 -0.0281 0.0256  -0.0359 273 ARG A CG  
1884  C  CD  . ARG A 272 ? 0.5260 0.5066 1.0828 -0.0277 0.0243  -0.0469 273 ARG A CD  
1885  N  NE  . ARG A 272 ? 0.6351 0.6063 1.1970 -0.0246 0.0238  -0.0484 273 ARG A NE  
1886  C  CZ  . ARG A 272 ? 0.7158 0.6800 1.2795 -0.0245 0.0234  -0.0587 273 ARG A CZ  
1887  N  NH1 . ARG A 272 ? 0.7726 0.7305 1.3437 -0.0211 0.0226  -0.0597 273 ARG A NH1 
1888  N  NH2 . ARG A 272 ? 0.7448 0.7092 1.3035 -0.0287 0.0235  -0.0683 273 ARG A NH2 
1889  N  N   . ASN A 273 ? 0.2378 0.2563 0.7963 -0.0465 0.0244  -0.0204 274 ASN A N   
1890  C  CA  . ASN A 273 ? 0.2336 0.2672 0.7929 -0.0486 0.0264  -0.0196 274 ASN A CA  
1891  C  C   . ASN A 273 ? 0.2340 0.2762 0.7905 -0.0522 0.0315  -0.0131 274 ASN A C   
1892  O  O   . ASN A 273 ? 0.2270 0.2814 0.7819 -0.0501 0.0360  -0.0144 274 ASN A O   
1893  C  CB  . ASN A 273 ? 0.2416 0.2781 0.8058 -0.0549 0.0222  -0.0208 274 ASN A CB  
1894  C  CG  . ASN A 273 ? 0.2465 0.2850 0.8127 -0.0525 0.0181  -0.0273 274 ASN A CG  
1895  O  OD1 . ASN A 273 ? 0.2731 0.3095 0.8363 -0.0465 0.0183  -0.0308 274 ASN A OD1 
1896  N  ND2 . ASN A 273 ? 0.2449 0.2878 0.8156 -0.0581 0.0138  -0.0282 274 ASN A ND2 
1897  N  N   . VAL A 274 ? 0.2442 0.2799 0.7996 -0.0583 0.0303  -0.0062 275 VAL A N   
1898  C  CA  . VAL A 274 ? 0.2476 0.2919 0.7982 -0.0646 0.0346  0.0010  275 VAL A CA  
1899  C  C   . VAL A 274 ? 0.2930 0.3405 0.8381 -0.0587 0.0391  0.0006  275 VAL A C   
1900  O  O   . VAL A 274 ? 0.2846 0.3466 0.8259 -0.0603 0.0450  -0.0005 275 VAL A O   
1901  C  CB  . VAL A 274 ? 0.3669 0.4008 0.9167 -0.0726 0.0303  0.0105  275 VAL A CB  
1902  C  CG1 . VAL A 274 ? 0.2676 0.3108 0.8100 -0.0808 0.0341  0.0191  275 VAL A CG1 
1903  C  CG2 . VAL A 274 ? 0.3877 0.4197 0.9417 -0.0800 0.0263  0.0115  275 VAL A CG2 
1904  N  N   . LEU A 275 ? 0.2347 0.2695 0.7799 -0.0521 0.0367  0.0002  276 LEU A N   
1905  C  CA  . LEU A 275 ? 0.2264 0.2634 0.7666 -0.0470 0.0405  0.0002  276 LEU A CA  
1906  C  C   . LEU A 275 ? 0.2143 0.2594 0.7523 -0.0397 0.0444  -0.0080 276 LEU A C   
1907  O  O   . LEU A 275 ? 0.2094 0.2622 0.7415 -0.0381 0.0492  -0.0086 276 LEU A O   
1908  C  CB  . LEU A 275 ? 0.2267 0.2484 0.7695 -0.0416 0.0367  0.0013  276 LEU A CB  
1909  C  CG  . LEU A 275 ? 0.3847 0.3966 0.9296 -0.0477 0.0313  0.0111  276 LEU A CG  
1910  C  CD1 . LEU A 275 ? 0.2401 0.2397 0.7888 -0.0409 0.0282  0.0116  276 LEU A CD1 
1911  C  CD2 . LEU A 275 ? 0.3840 0.4065 0.9217 -0.0582 0.0335  0.0208  276 LEU A CD2 
1912  N  N   . LYS A 276 ? 0.2676 0.3106 0.8100 -0.0360 0.0417  -0.0141 277 LYS A N   
1913  C  CA  . LYS A 276 ? 0.2241 0.2735 0.7651 -0.0303 0.0432  -0.0201 277 LYS A CA  
1914  C  C   . LYS A 276 ? 0.2097 0.2742 0.7507 -0.0338 0.0474  -0.0206 277 LYS A C   
1915  O  O   . LYS A 276 ? 0.2111 0.2816 0.7493 -0.0296 0.0504  -0.0245 277 LYS A O   
1916  C  CB  . LYS A 276 ? 0.2028 0.2481 0.7488 -0.0283 0.0377  -0.0247 277 LYS A CB  
1917  C  CG  . LYS A 276 ? 0.2204 0.2551 0.7646 -0.0233 0.0356  -0.0282 277 LYS A CG  
1918  C  CD  . LYS A 276 ? 0.2475 0.2812 0.7952 -0.0240 0.0302  -0.0328 277 LYS A CD  
1919  C  CE  . LYS A 276 ? 0.3069 0.3326 0.8518 -0.0210 0.0293  -0.0376 277 LYS A CE  
1920  N  NZ  . LYS A 276 ? 0.3471 0.3757 0.8922 -0.0226 0.0243  -0.0414 277 LYS A NZ  
1921  N  N   . GLY A 277 ? 0.2776 0.3480 0.8221 -0.0421 0.0475  -0.0173 278 GLY A N   
1922  C  CA  . GLY A 277 ? 0.2655 0.3523 0.8107 -0.0473 0.0529  -0.0186 278 GLY A CA  
1923  C  C   . GLY A 277 ? 0.2653 0.3595 0.8022 -0.0503 0.0595  -0.0168 278 GLY A C   
1924  O  O   . GLY A 277 ? 0.2842 0.3903 0.8197 -0.0492 0.0651  -0.0222 278 GLY A O   
1925  N  N   . CYS A 278 ? 0.2528 0.3396 0.7847 -0.0544 0.0583  -0.0094 279 CYS A N   
1926  C  CA  . CYS A 278 ? 0.2230 0.3170 0.7463 -0.0597 0.0634  -0.0057 279 CYS A CA  
1927  C  C   . CYS A 278 ? 0.2779 0.3707 0.7963 -0.0507 0.0660  -0.0105 279 CYS A C   
1928  O  O   . CYS A 278 ? 0.2142 0.3188 0.7263 -0.0538 0.0722  -0.0126 279 CYS A O   
1929  C  CB  . CYS A 278 ? 0.3122 0.3963 0.8331 -0.0669 0.0588  0.0055  279 CYS A CB  
1930  S  SG  . CYS A 278 ? 0.5621 0.6466 1.0855 -0.0804 0.0553  0.0134  279 CYS A SG  
1931  N  N   . LEU A 279 ? 0.3115 0.3904 0.8320 -0.0406 0.0616  -0.0128 280 LEU A N   
1932  C  CA  . LEU A 279 ? 0.3029 0.3776 0.8174 -0.0329 0.0630  -0.0158 280 LEU A CA  
1933  C  C   . LEU A 279 ? 0.1919 0.2651 0.7066 -0.0246 0.0624  -0.0239 280 LEU A C   
1934  O  O   . LEU A 279 ? 0.1979 0.2614 0.7087 -0.0178 0.0603  -0.0257 280 LEU A O   
1935  C  CB  . LEU A 279 ? 0.2652 0.3250 0.7806 -0.0294 0.0583  -0.0114 280 LEU A CB  
1936  C  CG  . LEU A 279 ? 0.2822 0.3391 0.7996 -0.0375 0.0557  -0.0015 280 LEU A CG  
1937  C  CD1 . LEU A 279 ? 0.2947 0.3361 0.8167 -0.0321 0.0506  0.0011  280 LEU A CD1 
1938  C  CD2 . LEU A 279 ? 0.2104 0.2800 0.7200 -0.0460 0.0603  0.0032  280 LEU A CD2 
1939  N  N   . ALA A 280 ? 0.2556 0.3382 0.7753 -0.0262 0.0638  -0.0281 281 ALA A N   
1940  C  CA  . ALA A 280 ? 0.2757 0.3566 0.7982 -0.0197 0.0614  -0.0341 281 ALA A CA  
1941  C  C   . ALA A 280 ? 0.1882 0.2707 0.7036 -0.0157 0.0650  -0.0385 281 ALA A C   
1942  O  O   . ALA A 280 ? 0.1921 0.2654 0.7045 -0.0099 0.0614  -0.0401 281 ALA A O   
1943  C  CB  . ALA A 280 ? 0.2738 0.3653 0.8066 -0.0226 0.0614  -0.0371 281 ALA A CB  
1944  N  N   . ASN A 281 ? 0.1916 0.2866 0.7041 -0.0203 0.0722  -0.0406 282 ASN A N   
1945  C  CA  . ASN A 281 ? 0.2656 0.3636 0.7720 -0.0178 0.0764  -0.0459 282 ASN A CA  
1946  C  C   . ASN A 281 ? 0.3212 0.4071 0.8176 -0.0135 0.0741  -0.0428 282 ASN A C   
1947  O  O   . ASN A 281 ? 0.1834 0.2633 0.6760 -0.0084 0.0726  -0.0463 282 ASN A O   
1948  C  CB  . ASN A 281 ? 0.2781 0.3938 0.7824 -0.0259 0.0851  -0.0487 282 ASN A CB  
1949  C  CG  . ASN A 281 ? 0.2028 0.3323 0.7170 -0.0289 0.0891  -0.0559 282 ASN A CG  
1950  O  OD1 . ASN A 281 ? 0.2040 0.3354 0.7230 -0.0246 0.0905  -0.0641 282 ASN A OD1 
1951  N  ND2 . ASN A 281 ? 0.3509 0.4897 0.8695 -0.0366 0.0905  -0.0529 282 ASN A ND2 
1952  N  N   . GLN A 282 ? 0.2975 0.3798 0.7909 -0.0161 0.0734  -0.0359 283 GLN A N   
1953  C  CA  . GLN A 282 ? 0.2204 0.2913 0.7067 -0.0119 0.0709  -0.0329 283 GLN A CA  
1954  C  C   . GLN A 282 ? 0.2496 0.3068 0.7355 -0.0058 0.0648  -0.0341 283 GLN A C   
1955  O  O   . GLN A 282 ? 0.3041 0.3541 0.7821 -0.0022 0.0634  -0.0350 283 GLN A O   
1956  C  CB  . GLN A 282 ? 0.2059 0.2745 0.6945 -0.0159 0.0697  -0.0248 283 GLN A CB  
1957  C  CG  . GLN A 282 ? 0.2237 0.3058 0.7099 -0.0248 0.0745  -0.0209 283 GLN A CG  
1958  C  CD  . GLN A 282 ? 0.3390 0.4324 0.8298 -0.0342 0.0766  -0.0190 283 GLN A CD  
1959  O  OE1 . GLN A 282 ? 0.3447 0.4382 0.8413 -0.0326 0.0756  -0.0227 283 GLN A OE1 
1960  N  NE2 . GLN A 282 ? 0.2027 0.3058 0.6902 -0.0454 0.0790  -0.0125 283 GLN A NE2 
1961  N  N   . ALA A 283 ? 0.2691 0.3246 0.7632 -0.0062 0.0610  -0.0339 284 ALA A N   
1962  C  CA  . ALA A 283 ? 0.3020 0.3477 0.7968 -0.0028 0.0551  -0.0346 284 ALA A CA  
1963  C  C   . ALA A 283 ? 0.2982 0.3448 0.7919 -0.0002 0.0532  -0.0382 284 ALA A C   
1964  O  O   . ALA A 283 ? 0.1739 0.2142 0.6663 0.0017  0.0483  -0.0379 284 ALA A O   
1965  C  CB  . ALA A 283 ? 0.1780 0.2237 0.6835 -0.0049 0.0514  -0.0334 284 ALA A CB  
1966  N  N   . ASP A 284 ? 0.1778 0.2333 0.6739 -0.0008 0.0570  -0.0418 285 ASP A N   
1967  C  CA  . ASP A 284 ? 0.2857 0.3414 0.7842 0.0018  0.0549  -0.0453 285 ASP A CA  
1968  C  C   . ASP A 284 ? 0.2909 0.3405 0.7781 0.0039  0.0550  -0.0455 285 ASP A C   
1969  O  O   . ASP A 284 ? 0.1767 0.2241 0.6662 0.0058  0.0517  -0.0468 285 ASP A O   
1970  C  CB  . ASP A 284 ? 0.2914 0.3588 0.7979 0.0004  0.0597  -0.0511 285 ASP A CB  
1971  C  CG  . ASP A 284 ? 0.4423 0.5153 0.9634 -0.0007 0.0570  -0.0519 285 ASP A CG  
1972  O  OD1 . ASP A 284 ? 0.4155 0.4827 0.9413 0.0004  0.0499  -0.0481 285 ASP A OD1 
1973  O  OD2 . ASP A 284 ? 0.4354 0.5202 0.9638 -0.0031 0.0622  -0.0567 285 ASP A OD2 
1974  N  N   . LEU A 285 ? 0.3643 0.4117 0.8412 0.0033  0.0584  -0.0436 286 LEU A N   
1975  C  CA  . LEU A 285 ? 0.3314 0.3740 0.7973 0.0049  0.0586  -0.0435 286 LEU A CA  
1976  C  C   . LEU A 285 ? 0.1691 0.2029 0.6311 0.0062  0.0530  -0.0404 286 LEU A C   
1977  O  O   . LEU A 285 ? 0.1674 0.1980 0.6214 0.0073  0.0524  -0.0403 286 LEU A O   
1978  C  CB  . LEU A 285 ? 0.3075 0.3519 0.7662 0.0037  0.0634  -0.0419 286 LEU A CB  
1979  C  CG  . LEU A 285 ? 0.3064 0.3631 0.7675 0.0009  0.0701  -0.0448 286 LEU A CG  
1980  C  CD1 . LEU A 285 ? 0.3300 0.3898 0.7907 -0.0020 0.0724  -0.0395 286 LEU A CD1 
1981  C  CD2 . LEU A 285 ? 0.1747 0.2349 0.6305 0.0016  0.0733  -0.0498 286 LEU A CD2 
1982  N  N   . ASP A 286 ? 0.2183 0.2500 0.6870 0.0056  0.0492  -0.0386 287 ASP A N   
1983  C  CA  . ASP A 286 ? 0.2755 0.3016 0.7424 0.0059  0.0451  -0.0369 287 ASP A CA  
1984  C  C   . ASP A 286 ? 0.2583 0.2830 0.7229 0.0073  0.0417  -0.0366 287 ASP A C   
1985  O  O   . ASP A 286 ? 0.2681 0.2898 0.7239 0.0076  0.0424  -0.0361 287 ASP A O   
1986  C  CB  . ASP A 286 ? 0.1692 0.1959 0.6478 0.0049  0.0412  -0.0364 287 ASP A CB  
1987  C  CG  . ASP A 286 ? 0.1686 0.1917 0.6475 0.0046  0.0381  -0.0365 287 ASP A CG  
1988  O  OD1 . ASP A 286 ? 0.3263 0.3457 0.7981 0.0044  0.0410  -0.0374 287 ASP A OD1 
1989  O  OD2 . ASP A 286 ? 0.1976 0.2229 0.6859 0.0045  0.0327  -0.0361 287 ASP A OD2 
1990  N  N   . ALA A 287 ? 0.1691 0.1964 0.6437 0.0079  0.0378  -0.0366 288 ALA A N   
1991  C  CA  . ALA A 287 ? 0.4005 0.4265 0.8786 0.0090  0.0328  -0.0349 288 ALA A CA  
1992  C  C   . ALA A 287 ? 0.1683 0.1926 0.6358 0.0098  0.0360  -0.0358 288 ALA A C   
1993  O  O   . ALA A 287 ? 0.1671 0.1890 0.6308 0.0101  0.0342  -0.0340 288 ALA A O   
1994  C  CB  . ALA A 287 ? 0.1737 0.2026 0.6679 0.0097  0.0276  -0.0345 288 ALA A CB  
1995  N  N   . GLU A 288 ? 0.1690 0.1956 0.6332 0.0099  0.0409  -0.0392 289 GLU A N   
1996  C  CA  . GLU A 288 ? 0.1684 0.1943 0.6247 0.0104  0.0436  -0.0408 289 GLU A CA  
1997  C  C   . GLU A 288 ? 0.3029 0.3267 0.7444 0.0101  0.0472  -0.0398 289 GLU A C   
1998  O  O   . GLU A 288 ? 0.1639 0.1860 0.5985 0.0105  0.0476  -0.0396 289 GLU A O   
1999  C  CB  . GLU A 288 ? 0.1714 0.2021 0.6317 0.0105  0.0480  -0.0463 289 GLU A CB  
2000  C  CG  . GLU A 288 ? 0.2821 0.3151 0.7597 0.0111  0.0445  -0.0486 289 GLU A CG  
2001  C  CD  . GLU A 288 ? 0.4197 0.4486 0.9060 0.0120  0.0368  -0.0448 289 GLU A CD  
2002  O  OE1 . GLU A 288 ? 0.4225 0.4486 0.9029 0.0122  0.0366  -0.0439 289 GLU A OE1 
2003  O  OE2 . GLU A 288 ? 0.4341 0.4631 0.9347 0.0123  0.0305  -0.0422 289 GLU A OE2 
2004  N  N   . TRP A 289 ? 0.3028 0.3266 0.7416 0.0092  0.0494  -0.0390 290 TRP A N   
2005  C  CA  . TRP A 289 ? 0.1621 0.1834 0.5910 0.0090  0.0516  -0.0376 290 TRP A CA  
2006  C  C   . TRP A 289 ? 0.2459 0.2639 0.6724 0.0093  0.0487  -0.0364 290 TRP A C   
2007  O  O   . TRP A 289 ? 0.2229 0.2395 0.6413 0.0097  0.0498  -0.0363 290 TRP A O   
2008  C  CB  . TRP A 289 ? 0.1701 0.1915 0.6022 0.0080  0.0534  -0.0366 290 TRP A CB  
2009  C  CG  . TRP A 289 ? 0.1617 0.1800 0.5887 0.0079  0.0545  -0.0350 290 TRP A CG  
2010  C  CD1 . TRP A 289 ? 0.2448 0.2595 0.6731 0.0075  0.0528  -0.0350 290 TRP A CD1 
2011  C  CD2 . TRP A 289 ? 0.1615 0.1808 0.5844 0.0081  0.0573  -0.0337 290 TRP A CD2 
2012  N  NE1 . TRP A 289 ? 0.2736 0.2865 0.6994 0.0077  0.0542  -0.0339 290 TRP A NE1 
2013  C  CE2 . TRP A 289 ? 0.2017 0.2172 0.6246 0.0081  0.0564  -0.0322 290 TRP A CE2 
2014  C  CE3 . TRP A 289 ? 0.2003 0.2245 0.6217 0.0081  0.0606  -0.0342 290 TRP A CE3 
2015  C  CZ2 . TRP A 289 ? 0.2462 0.2617 0.6688 0.0086  0.0575  -0.0298 290 TRP A CZ2 
2016  C  CZ3 . TRP A 289 ? 0.1791 0.2045 0.5994 0.0083  0.0623  -0.0319 290 TRP A CZ3 
2017  C  CH2 . TRP A 289 ? 0.2487 0.2692 0.6703 0.0087  0.0601  -0.0290 290 TRP A CH2 
2018  N  N   . ARG A 290 ? 0.1619 0.1796 0.5971 0.0090  0.0451  -0.0359 291 ARG A N   
2019  C  CA  . ARG A 290 ? 0.1620 0.1785 0.5985 0.0091  0.0429  -0.0358 291 ARG A CA  
2020  C  C   . ARG A 290 ? 0.2932 0.3097 0.7295 0.0100  0.0410  -0.0345 291 ARG A C   
2021  O  O   . ARG A 290 ? 0.2772 0.2929 0.7097 0.0101  0.0420  -0.0349 291 ARG A O   
2022  C  CB  . ARG A 290 ? 0.1637 0.1814 0.6133 0.0085  0.0388  -0.0356 291 ARG A CB  
2023  C  CG  . ARG A 290 ? 0.2348 0.2519 0.6868 0.0073  0.0406  -0.0376 291 ARG A CG  
2024  C  CD  . ARG A 290 ? 0.2806 0.3001 0.7468 0.0065  0.0362  -0.0381 291 ARG A CD  
2025  N  NE  . ARG A 290 ? 0.3430 0.3617 0.8137 0.0052  0.0376  -0.0404 291 ARG A NE  
2026  C  CZ  . ARG A 290 ? 0.3261 0.3432 0.7981 0.0042  0.0402  -0.0448 291 ARG A CZ  
2027  N  NH1 . ARG A 290 ? 0.1692 0.1861 0.6369 0.0046  0.0424  -0.0482 291 ARG A NH1 
2028  N  NH2 . ARG A 290 ? 0.1705 0.1861 0.6495 0.0029  0.0409  -0.0468 291 ARG A NH2 
2029  N  N   . ASN A 291 ? 0.3184 0.3359 0.7608 0.0104  0.0385  -0.0335 292 ASN A N   
2030  C  CA  . ASN A 291 ? 0.2411 0.2580 0.6865 0.0111  0.0361  -0.0320 292 ASN A CA  
2031  C  C   . ASN A 291 ? 0.2437 0.2596 0.6758 0.0113  0.0408  -0.0336 292 ASN A C   
2032  O  O   . ASN A 291 ? 0.1962 0.2110 0.6268 0.0114  0.0404  -0.0325 292 ASN A O   
2033  C  CB  . ASN A 291 ? 0.1668 0.1848 0.6234 0.0115  0.0330  -0.0323 292 ASN A CB  
2034  C  CG  . ASN A 291 ? 0.2802 0.2990 0.7539 0.0116  0.0257  -0.0290 292 ASN A CG  
2035  O  OD1 . ASN A 291 ? 0.2636 0.2823 0.7430 0.0113  0.0213  -0.0254 292 ASN A OD1 
2036  N  ND2 . ASN A 291 ? 0.1730 0.1934 0.6570 0.0119  0.0241  -0.0306 292 ASN A ND2 
2037  N  N   . LEU A 292 ? 0.1612 0.1781 0.5856 0.0112  0.0450  -0.0360 293 LEU A N   
2038  C  CA  . LEU A 292 ? 0.2732 0.2899 0.6867 0.0113  0.0488  -0.0373 293 LEU A CA  
2039  C  C   . LEU A 292 ? 0.2387 0.2539 0.6446 0.0113  0.0500  -0.0364 293 LEU A C   
2040  O  O   . LEU A 292 ? 0.1578 0.1723 0.5596 0.0115  0.0506  -0.0364 293 LEU A O   
2041  C  CB  . LEU A 292 ? 0.2812 0.3004 0.6910 0.0111  0.0528  -0.0394 293 LEU A CB  
2042  C  CG  . LEU A 292 ? 0.3226 0.3426 0.7241 0.0113  0.0559  -0.0406 293 LEU A CG  
2043  C  CD1 . LEU A 292 ? 0.3305 0.3506 0.7352 0.0115  0.0552  -0.0428 293 LEU A CD1 
2044  C  CD2 . LEU A 292 ? 0.2949 0.3186 0.6952 0.0109  0.0599  -0.0420 293 LEU A CD2 
2045  N  N   . LEU A 293 ? 0.1582 0.1729 0.5640 0.0109  0.0506  -0.0364 294 LEU A N   
2046  C  CA  . LEU A 293 ? 0.2947 0.3083 0.6959 0.0108  0.0523  -0.0374 294 LEU A CA  
2047  C  C   . LEU A 293 ? 0.3176 0.3312 0.7224 0.0108  0.0515  -0.0382 294 LEU A C   
2048  O  O   . LEU A 293 ? 0.1594 0.1730 0.5601 0.0109  0.0539  -0.0400 294 LEU A O   
2049  C  CB  . LEU A 293 ? 0.2409 0.2537 0.6451 0.0102  0.0528  -0.0382 294 LEU A CB  
2050  C  CG  . LEU A 293 ? 0.2336 0.2462 0.6352 0.0103  0.0546  -0.0371 294 LEU A CG  
2051  C  CD1 . LEU A 293 ? 0.2102 0.2248 0.6128 0.0102  0.0552  -0.0356 294 LEU A CD1 
2052  C  CD2 . LEU A 293 ? 0.2712 0.2820 0.6792 0.0097  0.0545  -0.0379 294 LEU A CD2 
2053  N  N   . ASP A 294 ? 0.3683 0.3825 0.7834 0.0107  0.0480  -0.0369 295 ASP A N   
2054  C  CA  . ASP A 294 ? 0.4024 0.4179 0.8259 0.0105  0.0467  -0.0366 295 ASP A CA  
2055  C  C   . ASP A 294 ? 0.2465 0.2614 0.6679 0.0109  0.0468  -0.0350 295 ASP A C   
2056  O  O   . ASP A 294 ? 0.1857 0.2020 0.6073 0.0105  0.0495  -0.0365 295 ASP A O   
2057  C  CB  . ASP A 294 ? 0.4705 0.4875 0.9097 0.0104  0.0407  -0.0334 295 ASP A CB  
2058  C  CG  . ASP A 294 ? 0.6587 0.6792 1.1063 0.0093  0.0408  -0.0360 295 ASP A CG  
2059  O  OD1 . ASP A 294 ? 0.6991 0.7186 1.1392 0.0089  0.0457  -0.0410 295 ASP A OD1 
2060  O  OD2 . ASP A 294 ? 0.6857 0.7116 1.1497 0.0080  0.0350  -0.0328 295 ASP A OD2 
2061  N  N   . SER A 295 ? 0.1606 0.1744 0.5816 0.0113  0.0447  -0.0330 296 SER A N   
2062  C  CA  . SER A 295 ? 0.2148 0.2278 0.6357 0.0114  0.0447  -0.0321 296 SER A CA  
2063  C  C   . SER A 295 ? 0.2294 0.2425 0.6367 0.0114  0.0498  -0.0348 296 SER A C   
2064  O  O   . SER A 295 ? 0.1892 0.2022 0.5966 0.0112  0.0508  -0.0347 296 SER A O   
2065  C  CB  . SER A 295 ? 0.1617 0.1741 0.5873 0.0117  0.0421  -0.0317 296 SER A CB  
2066  O  OG  . SER A 295 ? 0.1933 0.2066 0.6086 0.0118  0.0459  -0.0349 296 SER A OG  
2067  N  N   . MET A 296 ? 0.2868 0.3003 0.6850 0.0115  0.0523  -0.0365 297 MET A N   
2068  C  CA  . MET A 296 ? 0.3094 0.3233 0.6979 0.0117  0.0555  -0.0381 297 MET A CA  
2069  C  C   . MET A 296 ? 0.2526 0.2672 0.6409 0.0115  0.0579  -0.0404 297 MET A C   
2070  O  O   . MET A 296 ? 0.3035 0.3189 0.6878 0.0115  0.0601  -0.0417 297 MET A O   
2071  C  CB  . MET A 296 ? 0.2844 0.2987 0.6684 0.0120  0.0563  -0.0381 297 MET A CB  
2072  C  CG  . MET A 296 ? 0.2043 0.2198 0.5871 0.0121  0.0566  -0.0380 297 MET A CG  
2073  S  SD  . MET A 296 ? 0.6168 0.6341 0.9975 0.0124  0.0585  -0.0375 297 MET A SD  
2074  C  CE  . MET A 296 ? 0.9577 0.9738 1.3441 0.0119  0.0573  -0.0366 297 MET A CE  
2075  N  N   . VAL A 297 ? 0.2158 0.2307 0.6100 0.0110  0.0580  -0.0419 298 VAL A N   
2076  C  CA  . VAL A 297 ? 0.2117 0.2289 0.6089 0.0102  0.0617  -0.0466 298 VAL A CA  
2077  C  C   . VAL A 297 ? 0.2874 0.3071 0.6909 0.0094  0.0628  -0.0462 298 VAL A C   
2078  O  O   . VAL A 297 ? 0.2442 0.2669 0.6467 0.0085  0.0671  -0.0499 298 VAL A O   
2079  C  CB  . VAL A 297 ? 0.2424 0.2607 0.6471 0.0094  0.0623  -0.0500 298 VAL A CB  
2080  C  CG1 . VAL A 297 ? 0.2390 0.2628 0.6504 0.0075  0.0678  -0.0570 298 VAL A CG1 
2081  C  CG2 . VAL A 297 ? 0.2871 0.3030 0.6880 0.0098  0.0621  -0.0510 298 VAL A CG2 
2082  N  N   . LEU A 298 ? 0.2895 0.3087 0.7019 0.0095  0.0584  -0.0415 299 LEU A N   
2083  C  CA  . LEU A 298 ? 0.2886 0.3113 0.7127 0.0083  0.0576  -0.0389 299 LEU A CA  
2084  C  C   . LEU A 298 ? 0.2970 0.3178 0.7152 0.0086  0.0591  -0.0383 299 LEU A C   
2085  O  O   . LEU A 298 ? 0.2099 0.2359 0.6342 0.0066  0.0621  -0.0389 299 LEU A O   
2086  C  CB  . LEU A 298 ? 0.2929 0.3147 0.7316 0.0087  0.0499  -0.0322 299 LEU A CB  
2087  C  CG  . LEU A 298 ? 0.4391 0.4670 0.8876 0.0044  0.0461  -0.0299 299 LEU A CG  
2088  C  CD1 . LEU A 298 ? 0.4317 0.4554 0.8897 0.0034  0.0348  -0.0208 299 LEU A CD1 
2089  C  CD2 . LEU A 298 ? 0.4508 0.4806 0.8804 -0.0063 0.0476  -0.0302 299 LEU A CD2 
2090  N  N   . ILE A 299 ? 0.2003 0.2167 0.6085 0.0100  0.0574  -0.0374 300 ILE A N   
2091  C  CA  . ILE A 299 ? 0.2520 0.2675 0.6569 0.0099  0.0581  -0.0371 300 ILE A CA  
2092  C  C   . ILE A 299 ? 0.3394 0.3577 0.7372 0.0094  0.0632  -0.0409 300 ILE A C   
2093  O  O   . ILE A 299 ? 0.3129 0.3318 0.7119 0.0088  0.0644  -0.0409 300 ILE A O   
2094  C  CB  . ILE A 299 ? 0.1586 0.1721 0.5561 0.0107  0.0564  -0.0371 300 ILE A CB  
2095  C  CG1 . ILE A 299 ? 0.1590 0.1718 0.5582 0.0103  0.0564  -0.0372 300 ILE A CG1 
2096  C  CG2 . ILE A 299 ? 0.1745 0.1892 0.5603 0.0113  0.0586  -0.0391 300 ILE A CG2 
2097  C  CD1 . ILE A 299 ? 0.1614 0.1721 0.5765 0.0097  0.0528  -0.0342 300 ILE A CD1 
2098  N  N   . THR A 300 ? 0.2222 0.2422 0.6146 0.0095  0.0658  -0.0444 301 THR A N   
2099  C  CA  . THR A 300 ? 0.2677 0.2906 0.6554 0.0092  0.0699  -0.0485 301 THR A CA  
2100  C  C   . THR A 300 ? 0.2266 0.2552 0.6216 0.0068  0.0747  -0.0516 301 THR A C   
2101  O  O   . THR A 300 ? 0.1796 0.2114 0.5722 0.0061  0.0780  -0.0547 301 THR A O   
2102  C  CB  . THR A 300 ? 0.2658 0.2893 0.6507 0.0097  0.0712  -0.0523 301 THR A CB  
2103  O  OG1 . THR A 300 ? 0.2930 0.3188 0.6849 0.0082  0.0736  -0.0558 301 THR A OG1 
2104  C  CG2 . THR A 300 ? 0.1613 0.1812 0.5412 0.0112  0.0671  -0.0487 301 THR A CG2 
2105  N  N   . ASP A 301 ? 0.3491 0.3816 0.7553 0.0045  0.0752  -0.0504 302 ASP A N   
2106  C  CA  . ASP A 301 ? 0.2845 0.3283 0.7000 -0.0016 0.0803  -0.0519 302 ASP A CA  
2107  C  C   . ASP A 301 ? 0.2820 0.3252 0.7000 -0.0024 0.0791  -0.0479 302 ASP A C   
2108  O  O   . ASP A 301 ? 0.1890 0.2409 0.6081 -0.0085 0.0842  -0.0500 302 ASP A O   
2109  C  CB  . ASP A 301 ? 0.2903 0.3369 0.7084 -0.0093 0.0764  -0.0470 302 ASP A CB  
2110  C  CG  . ASP A 301 ? 0.4440 0.4930 0.8570 -0.0116 0.0788  -0.0528 302 ASP A CG  
2111  O  OD1 . ASP A 301 ? 0.4491 0.5039 0.8654 -0.0092 0.0870  -0.0628 302 ASP A OD1 
2112  O  OD2 . ASP A 301 ? 0.4828 0.5280 0.8902 -0.0159 0.0721  -0.0476 302 ASP A OD2 
2113  N  N   . LYS A 302 ? 0.2178 0.2511 0.6357 0.0023  0.0728  -0.0429 303 LYS A N   
2114  C  CA  . LYS A 302 ? 0.2703 0.3018 0.6935 0.0019  0.0710  -0.0395 303 LYS A CA  
2115  C  C   . LYS A 302 ? 0.3103 0.3409 0.7220 0.0031  0.0740  -0.0436 303 LYS A C   
2116  O  O   . LYS A 302 ? 0.2857 0.3154 0.7012 0.0024  0.0734  -0.0422 303 LYS A O   
2117  C  CB  . LYS A 302 ? 0.1863 0.2085 0.6142 0.0050  0.0638  -0.0350 303 LYS A CB  
2118  C  CG  . LYS A 302 ? 0.1639 0.1870 0.6086 0.0040  0.0583  -0.0291 303 LYS A CG  
2119  C  CD  . LYS A 302 ? 0.3505 0.3761 0.7925 -0.0065 0.0553  -0.0226 303 LYS A CD  
2120  C  CE  . LYS A 302 ? 0.4373 0.4548 0.8812 -0.0108 0.0434  -0.0125 303 LYS A CE  
2121  N  NZ  . LYS A 302 ? 0.4802 0.4953 0.9105 -0.0243 0.0375  -0.0034 303 LYS A NZ  
2122  N  N   . PHE A 303 ? 0.2256 0.2570 0.6259 0.0045  0.0762  -0.0481 304 PHE A N   
2123  C  CA  . PHE A 303 ? 0.2063 0.2389 0.5992 0.0052  0.0776  -0.0507 304 PHE A CA  
2124  C  C   . PHE A 303 ? 0.2733 0.3141 0.6713 0.0017  0.0831  -0.0538 304 PHE A C   
2125  O  O   . PHE A 303 ? 0.2358 0.2780 0.6320 0.0017  0.0836  -0.0548 304 PHE A O   
2126  C  CB  . PHE A 303 ? 0.2353 0.2679 0.6204 0.0072  0.0774  -0.0534 304 PHE A CB  
2127  C  CG  . PHE A 303 ? 0.3245 0.3519 0.7043 0.0094  0.0726  -0.0500 304 PHE A CG  
2128  C  CD1 . PHE A 303 ? 0.2992 0.3228 0.6796 0.0096  0.0694  -0.0463 304 PHE A CD1 
2129  C  CD2 . PHE A 303 ? 0.3076 0.3350 0.6840 0.0108  0.0717  -0.0509 304 PHE A CD2 
2130  C  CE1 . PHE A 303 ? 0.2779 0.2991 0.6539 0.0108  0.0664  -0.0445 304 PHE A CE1 
2131  C  CE2 . PHE A 303 ? 0.3069 0.3312 0.6798 0.0121  0.0682  -0.0476 304 PHE A CE2 
2132  C  CZ  . PHE A 303 ? 0.2860 0.3078 0.6580 0.0119  0.0661  -0.0448 304 PHE A CZ  
2133  N  N   . TRP A 304 ? 0.2989 0.3474 0.7035 -0.0031 0.0875  -0.0554 305 TRP A N   
2134  C  CA  . TRP A 304 ? 0.3070 0.3671 0.7151 -0.0107 0.0938  -0.0580 305 TRP A CA  
2135  C  C   . TRP A 304 ? 0.3941 0.4590 0.8111 -0.0208 0.0927  -0.0509 305 TRP A C   
2136  O  O   . TRP A 304 ? 0.3864 0.4447 0.8062 -0.0206 0.0864  -0.0445 305 TRP A O   
2137  C  CB  . TRP A 304 ? 0.2182 0.2873 0.6225 -0.0143 0.1009  -0.0669 305 TRP A CB  
2138  C  CG  . TRP A 304 ? 0.2652 0.3291 0.6637 -0.0071 0.0998  -0.0721 305 TRP A CG  
2139  C  CD1 . TRP A 304 ? 0.2737 0.3400 0.6708 -0.0057 0.1009  -0.0758 305 TRP A CD1 
2140  C  CD2 . TRP A 304 ? 0.2528 0.3094 0.6483 -0.0023 0.0962  -0.0726 305 TRP A CD2 
2141  N  NE1 . TRP A 304 ? 0.2902 0.3515 0.6854 -0.0007 0.0976  -0.0777 305 TRP A NE1 
2142  C  CE2 . TRP A 304 ? 0.2957 0.3510 0.6892 0.0010  0.0949  -0.0757 305 TRP A CE2 
2143  C  CE3 . TRP A 304 ? 0.2467 0.2987 0.6426 -0.0012 0.0936  -0.0702 305 TRP A CE3 
2144  C  CZ2 . TRP A 304 ? 0.2409 0.2907 0.6331 0.0046  0.0911  -0.0756 305 TRP A CZ2 
2145  C  CZ3 . TRP A 304 ? 0.2600 0.3060 0.6524 0.0026  0.0903  -0.0710 305 TRP A CZ3 
2146  C  CH2 . TRP A 304 ? 0.2485 0.2937 0.6393 0.0051  0.0891  -0.0734 305 TRP A CH2 
2147  N  N   . GLY A 305 ? 0.4122 0.4844 0.8265 -0.0313 0.0961  -0.0502 306 GLY A N   
2148  C  CA  . GLY A 305 ? 0.4203 0.4874 0.8205 -0.0441 0.0898  -0.0405 306 GLY A CA  
2149  C  C   . GLY A 305 ? 0.4856 0.5601 0.8696 -0.0558 0.0938  -0.0434 306 GLY A C   
2150  O  O   . GLY A 305 ? 0.4620 0.5443 0.8483 -0.0524 0.1015  -0.0541 306 GLY A O   
2151  N  N   . THR A 306 ? 0.5674 0.6392 0.9353 -0.0705 0.0882  -0.0340 307 THR A N   
2152  C  CA  . THR A 306 ? 0.7073 0.7869 1.0560 -0.0850 0.0914  -0.0361 307 THR A CA  
2153  C  C   . THR A 306 ? 0.8160 0.9102 1.1544 -0.0984 0.1016  -0.0427 307 THR A C   
2154  O  O   . THR A 306 ? 0.8922 0.9958 1.2135 -0.1126 0.1065  -0.0469 307 THR A O   
2155  C  CB  . THR A 306 ? 0.7991 0.8687 1.1334 -0.0962 0.0779  -0.0206 307 THR A CB  
2156  O  OG1 . THR A 306 ? 0.8147 0.8769 1.1483 -0.1025 0.0699  -0.0081 307 THR A OG1 
2157  C  CG2 . THR A 306 ? 0.7780 0.8360 1.1233 -0.0840 0.0691  -0.0162 307 THR A CG2 
2158  N  N   . SER A 307 ? 0.7588 0.8561 1.1079 -0.0948 0.1052  -0.0446 308 SER A N   
2159  C  CA  . SER A 307 ? 0.7509 0.8619 1.0918 -0.1085 0.1139  -0.0492 308 SER A CA  
2160  C  C   . SER A 307 ? 0.7265 0.8550 1.0780 -0.1045 0.1292  -0.0682 308 SER A C   
2161  O  O   . SER A 307 ? 0.7448 0.8873 1.0937 -0.1146 0.1382  -0.0747 308 SER A O   
2162  C  CB  . SER A 307 ? 0.7549 0.8606 1.1021 -0.1086 0.1093  -0.0408 308 SER A CB  
2163  O  OG  . SER A 307 ? 0.7351 0.8259 1.0732 -0.1158 0.0953  -0.0235 308 SER A OG  
2164  N  N   . GLY A 308 ? 0.6545 0.7823 1.0199 -0.0901 0.1318  -0.0771 309 GLY A N   
2165  C  CA  . GLY A 308 ? 0.6374 0.7774 1.0131 -0.0836 0.1429  -0.0940 309 GLY A CA  
2166  C  C   . GLY A 308 ? 0.5721 0.7089 0.9563 -0.0707 0.1409  -0.0951 309 GLY A C   
2167  O  O   . GLY A 308 ? 0.6109 0.7560 0.9957 -0.0697 0.1469  -0.1054 309 GLY A O   
2168  N  N   . VAL A 309 ? 0.5652 0.6896 0.9561 -0.0617 0.1318  -0.0846 310 VAL A N   
2169  C  CA  . VAL A 309 ? 0.5054 0.6254 0.9020 -0.0514 0.1284  -0.0840 310 VAL A CA  
2170  C  C   . VAL A 309 ? 0.5364 0.6432 0.9375 -0.0350 0.1216  -0.0839 310 VAL A C   
2171  O  O   . VAL A 309 ? 0.5207 0.6199 0.9218 -0.0314 0.1180  -0.0806 310 VAL A O   
2172  C  CB  . VAL A 309 ? 0.4833 0.5992 0.8816 -0.0566 0.1232  -0.0727 310 VAL A CB  
2173  C  CG1 . VAL A 309 ? 0.4606 0.5743 0.8636 -0.0482 0.1208  -0.0735 310 VAL A CG1 
2174  C  CG2 . VAL A 309 ? 0.4726 0.5980 0.8620 -0.0767 0.1275  -0.0693 310 VAL A CG2 
2175  N  N   . GLU A 310 ? 0.5259 0.6298 0.9294 -0.0269 0.1190  -0.0864 311 GLU A N   
2176  C  CA  . GLU A 310 ? 0.5229 0.6147 0.9266 -0.0157 0.1117  -0.0847 311 GLU A CA  
2177  C  C   . GLU A 310 ? 0.4682 0.5487 0.8705 -0.0117 0.1043  -0.0751 311 GLU A C   
2178  O  O   . GLU A 310 ? 0.4548 0.5361 0.8593 -0.0164 0.1045  -0.0702 311 GLU A O   
2179  C  CB  . GLU A 310 ? 0.6014 0.6948 1.0088 -0.0113 0.1098  -0.0878 311 GLU A CB  
2180  C  CG  . GLU A 310 ? 0.7299 0.8292 1.1396 -0.0146 0.1106  -0.0861 311 GLU A CG  
2181  C  CD  . GLU A 310 ? 0.8192 0.9184 1.2339 -0.0093 0.1062  -0.0863 311 GLU A CD  
2182  O  OE1 . GLU A 310 ? 0.8550 0.9471 1.2702 -0.0031 0.1003  -0.0841 311 GLU A OE1 
2183  O  OE2 . GLU A 310 ? 0.8406 0.9480 1.2594 -0.0124 0.1084  -0.0880 311 GLU A OE2 
2184  N  N   . SER A 311 ? 0.4002 0.4709 0.7997 -0.0046 0.0978  -0.0723 312 SER A N   
2185  C  CA  . SER A 311 ? 0.3896 0.4504 0.7867 -0.0017 0.0918  -0.0652 312 SER A CA  
2186  C  C   . SER A 311 ? 0.3402 0.4005 0.7388 -0.0014 0.0894  -0.0628 312 SER A C   
2187  O  O   . SER A 311 ? 0.2761 0.3405 0.6754 -0.0002 0.0889  -0.0648 312 SER A O   
2188  C  CB  . SER A 311 ? 0.2345 0.2878 0.6264 0.0032  0.0867  -0.0632 312 SER A CB  
2189  O  OG  . SER A 311 ? 0.1661 0.2117 0.5554 0.0046  0.0822  -0.0578 312 SER A OG  
2190  N  N   . VAL A 312 ? 0.1691 0.2248 0.5705 -0.0025 0.0876  -0.0587 313 VAL A N   
2191  C  CA  . VAL A 312 ? 0.2014 0.2566 0.6061 -0.0031 0.0859  -0.0575 313 VAL A CA  
2192  C  C   . VAL A 312 ? 0.2099 0.2614 0.6096 0.0011  0.0812  -0.0570 313 VAL A C   
2193  O  O   . VAL A 312 ? 0.2866 0.3408 0.6885 0.0007  0.0804  -0.0578 313 VAL A O   
2194  C  CB  . VAL A 312 ? 0.2625 0.3128 0.6754 -0.0055 0.0847  -0.0538 313 VAL A CB  
2195  C  CG1 . VAL A 312 ? 0.2281 0.2687 0.6397 -0.0017 0.0802  -0.0514 313 VAL A CG1 
2196  C  CG2 . VAL A 312 ? 0.1780 0.2292 0.5968 -0.0074 0.0841  -0.0540 313 VAL A CG2 
2197  N  N   . ILE A 313 ? 0.1803 0.2273 0.5740 0.0040  0.0785  -0.0556 314 ILE A N   
2198  C  CA  . ILE A 313 ? 0.2700 0.3159 0.6598 0.0065  0.0747  -0.0544 314 ILE A CA  
2199  C  C   . ILE A 313 ? 0.2547 0.3078 0.6471 0.0074  0.0741  -0.0556 314 ILE A C   
2200  O  O   . ILE A 313 ? 0.2482 0.3038 0.6420 0.0081  0.0717  -0.0548 314 ILE A O   
2201  C  CB  . ILE A 313 ? 0.3399 0.3820 0.7243 0.0086  0.0726  -0.0525 314 ILE A CB  
2202  C  CG1 . ILE A 313 ? 0.3695 0.4053 0.7533 0.0079  0.0724  -0.0512 314 ILE A CG1 
2203  C  CG2 . ILE A 313 ? 0.2362 0.2796 0.6189 0.0105  0.0695  -0.0510 314 ILE A CG2 
2204  C  CD1 . ILE A 313 ? 0.4004 0.4333 0.7798 0.0093  0.0711  -0.0497 314 ILE A CD1 
2205  N  N   . GLY A 314 ? 0.1645 0.2224 0.5599 0.0070  0.0766  -0.0580 315 GLY A N   
2206  C  CA  . GLY A 314 ? 0.2684 0.3337 0.6697 0.0080  0.0758  -0.0594 315 GLY A CA  
2207  C  C   . GLY A 314 ? 0.2589 0.3314 0.6656 0.0050  0.0797  -0.0629 315 GLY A C   
2208  O  O   . GLY A 314 ? 0.2689 0.3487 0.6825 0.0056  0.0797  -0.0651 315 GLY A O   
2209  N  N   . SER A 315 ? 0.2367 0.3079 0.6426 0.0014  0.0829  -0.0632 316 SER A N   
2210  C  CA  . SER A 315 ? 0.3249 0.4042 0.7360 -0.0029 0.0874  -0.0662 316 SER A CA  
2211  C  C   . SER A 315 ? 0.2733 0.3512 0.6872 -0.0067 0.0878  -0.0643 316 SER A C   
2212  O  O   . SER A 315 ? 0.3136 0.3970 0.7310 -0.0122 0.0920  -0.0652 316 SER A O   
2213  C  CB  . SER A 315 ? 0.3089 0.3925 0.7199 -0.0061 0.0934  -0.0697 316 SER A CB  
2214  O  OG  . SER A 315 ? 0.3926 0.4709 0.8015 -0.0085 0.0945  -0.0669 316 SER A OG  
2215  N  N   . VAL A 316 ? 0.2155 0.2871 0.6286 -0.0046 0.0837  -0.0621 317 VAL A N   
2216  C  CA  . VAL A 316 ? 0.2955 0.3647 0.7140 -0.0077 0.0835  -0.0617 317 VAL A CA  
2217  C  C   . VAL A 316 ? 0.3751 0.4535 0.7993 -0.0119 0.0853  -0.0635 317 VAL A C   
2218  O  O   . VAL A 316 ? 0.3930 0.4723 0.8227 -0.0174 0.0873  -0.0629 317 VAL A O   
2219  C  CB  . VAL A 316 ? 0.2498 0.3132 0.6672 -0.0051 0.0797  -0.0617 317 VAL A CB  
2220  C  CG1 . VAL A 316 ? 0.2244 0.2863 0.6502 -0.0084 0.0798  -0.0635 317 VAL A CG1 
2221  C  CG2 . VAL A 316 ? 0.2295 0.2841 0.6421 -0.0023 0.0781  -0.0600 317 VAL A CG2 
2222  N  N   . HIS A 317 ? 0.3227 0.4084 0.7470 -0.0099 0.0840  -0.0650 318 HIS A N   
2223  C  CA  . HIS A 317 ? 0.1746 0.2703 0.6051 -0.0134 0.0848  -0.0669 318 HIS A CA  
2224  C  C   . HIS A 317 ? 0.3453 0.4479 0.7779 -0.0192 0.0904  -0.0683 318 HIS A C   
2225  O  O   . HIS A 317 ? 0.3960 0.5048 0.8332 -0.0246 0.0918  -0.0689 318 HIS A O   
2226  C  CB  . HIS A 317 ? 0.1737 0.2768 0.6071 -0.0096 0.0817  -0.0674 318 HIS A CB  
2227  C  CG  . HIS A 317 ? 0.2957 0.4003 0.7283 -0.0064 0.0828  -0.0685 318 HIS A CG  
2228  N  ND1 . HIS A 317 ? 0.2717 0.3689 0.6990 -0.0021 0.0807  -0.0667 318 HIS A ND1 
2229  C  CD2 . HIS A 317 ? 0.2833 0.3963 0.7209 -0.0074 0.0862  -0.0721 318 HIS A CD2 
2230  C  CE1 . HIS A 317 ? 0.2845 0.3847 0.7141 -0.0004 0.0824  -0.0692 318 HIS A CE1 
2231  N  NE2 . HIS A 317 ? 0.3456 0.4555 0.7819 -0.0034 0.0860  -0.0731 318 HIS A NE2 
2232  N  N   . THR A 318 ? 0.3962 0.4987 0.8250 -0.0192 0.0938  -0.0690 319 THR A N   
2233  C  CA  . THR A 318 ? 0.3544 0.4659 0.7840 -0.0266 0.1002  -0.0710 319 THR A CA  
2234  C  C   . THR A 318 ? 0.3973 0.5058 0.8277 -0.0348 0.1011  -0.0667 319 THR A C   
2235  O  O   . THR A 318 ? 0.4075 0.5239 0.8396 -0.0436 0.1041  -0.0664 319 THR A O   
2236  C  CB  . THR A 318 ? 0.3253 0.4382 0.7507 -0.0260 0.1041  -0.0738 319 THR A CB  
2237  O  OG1 . THR A 318 ? 0.4069 0.5100 0.8284 -0.0255 0.1027  -0.0697 319 THR A OG1 
2238  C  CG2 . THR A 318 ? 0.3585 0.4713 0.7850 -0.0181 0.1016  -0.0771 319 THR A CG2 
2239  N  N   . TRP A 319 ? 0.3771 0.4739 0.8072 -0.0326 0.0978  -0.0627 320 TRP A N   
2240  C  CA  . TRP A 319 ? 0.1915 0.2826 0.6255 -0.0400 0.0964  -0.0572 320 TRP A CA  
2241  C  C   . TRP A 319 ? 0.2802 0.3694 0.7203 -0.0418 0.0935  -0.0571 320 TRP A C   
2242  O  O   . TRP A 319 ? 0.3878 0.4764 0.8303 -0.0514 0.0931  -0.0533 320 TRP A O   
2243  C  CB  . TRP A 319 ? 0.1882 0.2672 0.6239 -0.0360 0.0927  -0.0535 320 TRP A CB  
2244  C  CG  . TRP A 319 ? 0.2557 0.3367 0.6861 -0.0365 0.0953  -0.0528 320 TRP A CG  
2245  C  CD1 . TRP A 319 ? 0.2231 0.3012 0.6494 -0.0279 0.0950  -0.0555 320 TRP A CD1 
2246  C  CD2 . TRP A 319 ? 0.2977 0.3840 0.7246 -0.0481 0.0984  -0.0491 320 TRP A CD2 
2247  N  NE1 . TRP A 319 ? 0.1855 0.2675 0.6084 -0.0322 0.0982  -0.0548 320 TRP A NE1 
2248  C  CE2 . TRP A 319 ? 0.1948 0.2824 0.6174 -0.0452 0.1006  -0.0510 320 TRP A CE2 
2249  C  CE3 . TRP A 319 ? 0.2937 0.3829 0.7185 -0.0625 0.0988  -0.0437 320 TRP A CE3 
2250  C  CZ2 . TRP A 319 ? 0.2454 0.3388 0.6621 -0.0565 0.1040  -0.0487 320 TRP A CZ2 
2251  C  CZ3 . TRP A 319 ? 0.2532 0.3470 0.6696 -0.0746 0.1015  -0.0401 320 TRP A CZ3 
2252  C  CH2 . TRP A 319 ? 0.3180 0.4145 0.7306 -0.0718 0.1044  -0.0431 320 TRP A CH2 
2253  N  N   . LEU A 320 ? 0.2008 0.2885 0.6421 -0.0342 0.0909  -0.0608 321 LEU A N   
2254  C  CA  . LEU A 320 ? 0.1889 0.2770 0.6359 -0.0365 0.0887  -0.0623 321 LEU A CA  
2255  C  C   . LEU A 320 ? 0.3032 0.4032 0.7507 -0.0440 0.0915  -0.0629 321 LEU A C   
2256  O  O   . LEU A 320 ? 0.3091 0.4081 0.7605 -0.0520 0.0908  -0.0610 321 LEU A O   
2257  C  CB  . LEU A 320 ? 0.3015 0.3896 0.7477 -0.0293 0.0858  -0.0661 321 LEU A CB  
2258  C  CG  . LEU A 320 ? 0.2819 0.3593 0.7269 -0.0234 0.0832  -0.0666 321 LEU A CG  
2259  C  CD1 . LEU A 320 ? 0.2828 0.3637 0.7255 -0.0197 0.0806  -0.0697 321 LEU A CD1 
2260  C  CD2 . LEU A 320 ? 0.1829 0.2504 0.6370 -0.0262 0.0821  -0.0663 321 LEU A CD2 
2261  N  N   . ALA A 321 ? 0.2828 0.3934 0.7271 -0.0419 0.0944  -0.0657 322 ALA A N   
2262  C  CA  . ALA A 321 ? 0.3208 0.4447 0.7668 -0.0483 0.0979  -0.0676 322 ALA A CA  
2263  C  C   . ALA A 321 ? 0.3124 0.4386 0.7556 -0.0603 0.1018  -0.0641 322 ALA A C   
2264  O  O   . ALA A 321 ? 0.2897 0.4222 0.7345 -0.0690 0.1029  -0.0634 322 ALA A O   
2265  C  CB  . ALA A 321 ? 0.1969 0.3304 0.6426 -0.0430 0.1001  -0.0719 322 ALA A CB  
2266  N  N   . GLU A 322 ? 0.2097 0.3312 0.6477 -0.0620 0.1034  -0.0613 323 GLU A N   
2267  C  CA  . GLU A 322 ? 0.3733 0.4964 0.8062 -0.0760 0.1059  -0.0560 323 GLU A CA  
2268  C  C   . GLU A 322 ? 0.2945 0.4057 0.7304 -0.0831 0.1000  -0.0488 323 GLU A C   
2269  O  O   . GLU A 322 ? 0.2756 0.3894 0.7081 -0.0963 0.1004  -0.0443 323 GLU A O   
2270  C  CB  . GLU A 322 ? 0.4384 0.5583 0.8652 -0.0770 0.1075  -0.0537 323 GLU A CB  
2271  C  CG  . GLU A 322 ? 0.5687 0.6909 0.9868 -0.0942 0.1094  -0.0469 323 GLU A CG  
2272  C  CD  . GLU A 322 ? 0.6627 0.7886 1.0730 -0.0970 0.1135  -0.0476 323 GLU A CD  
2273  O  OE1 . GLU A 322 ? 0.7063 0.8420 1.1165 -0.0896 0.1192  -0.0568 323 GLU A OE1 
2274  O  OE2 . GLU A 322 ? 0.6900 0.8078 1.0942 -0.1071 0.1100  -0.0385 323 GLU A OE2 
2275  N  N   . ALA A 323 ? 0.2712 0.3689 0.7135 -0.0747 0.0943  -0.0482 324 ALA A N   
2276  C  CA  . ALA A 323 ? 0.3083 0.3925 0.7563 -0.0793 0.0880  -0.0434 324 ALA A CA  
2277  C  C   . ALA A 323 ? 0.4060 0.4959 0.8571 -0.0838 0.0880  -0.0461 324 ALA A C   
2278  O  O   . ALA A 323 ? 0.4661 0.5501 0.9170 -0.0944 0.0848  -0.0406 324 ALA A O   
2279  C  CB  . ALA A 323 ? 0.2462 0.3175 0.7020 -0.0684 0.0834  -0.0455 324 ALA A CB  
2280  N  N   . ILE A 324 ? 0.3799 0.4803 0.8332 -0.0762 0.0905  -0.0536 325 ILE A N   
2281  C  CA  . ILE A 324 ? 0.4069 0.5143 0.8640 -0.0802 0.0902  -0.0565 325 ILE A CA  
2282  C  C   . ILE A 324 ? 0.4263 0.5456 0.8787 -0.0921 0.0942  -0.0541 325 ILE A C   
2283  O  O   . ILE A 324 ? 0.4653 0.5836 0.9190 -0.1016 0.0924  -0.0515 325 ILE A O   
2284  C  CB  . ILE A 324 ? 0.3968 0.5131 0.8568 -0.0703 0.0904  -0.0634 325 ILE A CB  
2285  C  CG1 . ILE A 324 ? 0.4289 0.5344 0.8925 -0.0621 0.0863  -0.0660 325 ILE A CG1 
2286  C  CG2 . ILE A 324 ? 0.3784 0.5053 0.8425 -0.0756 0.0901  -0.0658 325 ILE A CG2 
2287  C  CD1 . ILE A 324 ? 0.4285 0.5420 0.8929 -0.0549 0.0849  -0.0708 325 ILE A CD1 
2288  N  N   . ASN A 325 ? 0.4063 0.5372 0.8534 -0.0921 0.1000  -0.0556 326 ASN A N   
2289  C  CA  . ASN A 325 ? 0.4417 0.5856 0.8833 -0.1048 0.1053  -0.0544 326 ASN A CA  
2290  C  C   . ASN A 325 ? 0.4555 0.5897 0.8907 -0.1199 0.1024  -0.0445 326 ASN A C   
2291  O  O   . ASN A 325 ? 0.4830 0.6219 0.9162 -0.1320 0.1026  -0.0415 326 ASN A O   
2292  C  CB  . ASN A 325 ? 0.4622 0.6175 0.8987 -0.1028 0.1122  -0.0586 326 ASN A CB  
2293  C  CG  . ASN A 325 ? 0.5488 0.7185 0.9918 -0.0943 0.1155  -0.0675 326 ASN A CG  
2294  O  OD1 . ASN A 325 ? 0.5848 0.7678 1.0307 -0.1004 0.1187  -0.0702 326 ASN A OD1 
2295  N  ND2 . ASN A 325 ? 0.5209 0.6873 0.9669 -0.0807 0.1140  -0.0714 326 ASN A ND2 
2296  N  N   . ALA A 326 ? 0.4385 0.5583 0.8706 -0.1193 0.0986  -0.0386 327 ALA A N   
2297  C  CA  . ALA A 326 ? 0.4769 0.5831 0.9031 -0.1329 0.0928  -0.0270 327 ALA A CA  
2298  C  C   . ALA A 326 ? 0.5015 0.5963 0.9340 -0.1364 0.0859  -0.0239 327 ALA A C   
2299  O  O   . ALA A 326 ? 0.4904 0.5832 0.9172 -0.1515 0.0834  -0.0162 327 ALA A O   
2300  C  CB  . ALA A 326 ? 0.4451 0.5357 0.8708 -0.1283 0.0876  -0.0216 327 ALA A CB  
2301  N  N   . LEU A 327 ? 0.4864 0.5740 0.9299 -0.1235 0.0829  -0.0301 328 LEU A N   
2302  C  CA  . LEU A 327 ? 0.4959 0.5732 0.9465 -0.1259 0.0771  -0.0298 328 LEU A CA  
2303  C  C   . LEU A 327 ? 0.5661 0.6574 1.0147 -0.1356 0.0804  -0.0312 328 LEU A C   
2304  O  O   . LEU A 327 ? 0.5707 0.6545 1.0181 -0.1472 0.0758  -0.0250 328 LEU A O   
2305  C  CB  . LEU A 327 ? 0.4665 0.5390 0.9279 -0.1115 0.0756  -0.0389 328 LEU A CB  
2306  C  CG  . LEU A 327 ? 0.4956 0.5584 0.9646 -0.1144 0.0704  -0.0409 328 LEU A CG  
2307  C  CD1 . LEU A 327 ? 0.4828 0.5226 0.9551 -0.1174 0.0619  -0.0336 328 LEU A CD1 
2308  C  CD2 . LEU A 327 ? 0.4507 0.5172 0.9276 -0.1038 0.0715  -0.0521 328 LEU A CD2 
2309  N  N   . GLN A 328 ? 0.6371 0.7482 1.0862 -0.1308 0.0875  -0.0390 329 GLN A N   
2310  C  CA  . GLN A 328 ? 0.6719 0.7991 1.1212 -0.1388 0.0910  -0.0412 329 GLN A CA  
2311  C  C   . GLN A 328 ? 0.7402 0.8711 1.1793 -0.1568 0.0926  -0.0327 329 GLN A C   
2312  O  O   . GLN A 328 ? 0.7563 0.8861 1.1952 -0.1680 0.0899  -0.0288 329 GLN A O   
2313  C  CB  . GLN A 328 ? 0.7235 0.8708 1.1757 -0.1300 0.0976  -0.0500 329 GLN A CB  
2314  C  CG  . GLN A 328 ? 0.7606 0.9107 1.2225 -0.1192 0.0951  -0.0572 329 GLN A CG  
2315  C  CD  . GLN A 328 ? 0.8251 0.9913 1.2903 -0.1096 0.0991  -0.0638 329 GLN A CD  
2316  O  OE1 . GLN A 328 ? 0.8484 1.0201 1.3093 -0.1073 0.1039  -0.0646 329 GLN A OE1 
2317  N  NE2 . GLN A 328 ? 0.8570 1.0307 1.3302 -0.1048 0.0966  -0.0683 329 GLN A NE2 
2318  N  N   . ASP A 329 ? 0.7744 0.9102 1.2043 -0.1608 0.0968  -0.0297 330 ASP A N   
2319  C  CA  . ASP A 329 ? 0.8490 0.9907 1.2667 -0.1802 0.0987  -0.0213 330 ASP A CA  
2320  C  C   . ASP A 329 ? 0.8205 0.9397 1.2318 -0.1918 0.0889  -0.0075 330 ASP A C   
2321  O  O   . ASP A 329 ? 0.8717 0.9924 1.2705 -0.2100 0.0883  0.0025  330 ASP A O   
2322  C  CB  . ASP A 329 ? 0.9515 1.1085 1.3606 -0.1818 0.1074  -0.0242 330 ASP A CB  
2323  C  CG  . ASP A 329 ? 1.0255 1.2047 1.4415 -0.1726 0.1164  -0.0373 330 ASP A CG  
2324  O  OD1 . ASP A 329 ? 1.0426 1.2239 1.4702 -0.1632 0.1147  -0.0432 330 ASP A OD1 
2325  O  OD2 . ASP A 329 ? 1.0602 1.2541 1.4704 -0.1751 0.1245  -0.0418 330 ASP A OD2 
2326  N  N   . ASN A 330 ? 0.7410 0.8392 1.1611 -0.1814 0.0806  -0.0067 331 ASN A N   
2327  C  CA  . ASN A 330 ? 0.7080 0.7822 1.1265 -0.1897 0.0692  0.0053  331 ASN A CA  
2328  C  C   . ASN A 330 ? 0.6146 0.6779 1.0445 -0.1859 0.0636  0.0020  331 ASN A C   
2329  O  O   . ASN A 330 ? 0.5826 0.6233 1.0164 -0.1864 0.0536  0.0082  331 ASN A O   
2330  C  CB  . ASN A 330 ? 0.6844 0.7406 1.1042 -0.1812 0.0629  0.0098  331 ASN A CB  
2331  C  CG  . ASN A 330 ? 0.7110 0.7685 1.1157 -0.1938 0.0627  0.0204  331 ASN A CG  
2332  O  OD1 . ASN A 330 ? 0.7403 0.8180 1.1342 -0.2046 0.0715  0.0195  331 ASN A OD1 
2333  N  ND2 . ASN A 330 ? 0.7027 0.7395 1.1067 -0.1928 0.0525  0.0302  331 ASN A ND2 
2334  N  N   . ARG A 331 ? 0.5818 0.6613 1.0177 -0.1820 0.0697  -0.0082 332 ARG A N   
2335  C  CA  . ARG A 331 ? 0.6348 0.7070 1.0809 -0.1794 0.0654  -0.0130 332 ARG A CA  
2336  C  C   . ARG A 331 ? 0.6791 0.7386 1.1214 -0.1956 0.0582  -0.0029 332 ARG A C   
2337  O  O   . ARG A 331 ? 0.6732 0.7123 1.1229 -0.1932 0.0499  -0.0018 332 ARG A O   
2338  C  CB  . ARG A 331 ? 0.5761 0.6705 1.0273 -0.1750 0.0727  -0.0239 332 ARG A CB  
2339  N  N   . ASP A 332 ? 0.7415 0.8137 1.1725 -0.2124 0.0615  0.0040  333 ASP A N   
2340  C  CA  . ASP A 332 ? 0.8263 0.8878 1.2511 -0.2305 0.0548  0.0148  333 ASP A CA  
2341  C  C   . ASP A 332 ? 0.9069 0.9407 1.3276 -0.2339 0.0438  0.0269  333 ASP A C   
2342  O  O   . ASP A 332 ? 0.9297 0.9426 1.3563 -0.2351 0.0346  0.0305  333 ASP A O   
2343  C  CB  . ASP A 332 ? 0.8418 0.9247 1.2531 -0.2494 0.0614  0.0203  333 ASP A CB  
2344  C  CG  . ASP A 332 ? 0.8376 0.9481 1.2557 -0.2455 0.0710  0.0091  333 ASP A CG  
2345  O  OD1 . ASP A 332 ? 0.8013 0.9110 1.2319 -0.2347 0.0702  -0.0001 333 ASP A OD1 
2346  O  OD2 . ASP A 332 ? 0.8583 0.9914 1.2699 -0.2530 0.0791  0.0095  333 ASP A OD2 
2347  N  N   . THR A 333 ? 0.8835 0.9172 1.2951 -0.2348 0.0444  0.0329  334 THR A N   
2348  C  CA  . THR A 333 ? 0.9376 0.9468 1.3444 -0.2383 0.0333  0.0460  334 THR A CA  
2349  C  C   . THR A 333 ? 0.9476 0.9341 1.3719 -0.2201 0.0242  0.0424  334 THR A C   
2350  O  O   . THR A 333 ? 0.9881 0.9522 1.4164 -0.2229 0.0128  0.0507  334 THR A O   
2351  C  CB  . THR A 333 ? 0.9299 0.9460 1.3245 -0.2409 0.0364  0.0512  334 THR A CB  
2352  O  OG1 . THR A 333 ? 0.9448 0.9832 1.3230 -0.2596 0.0458  0.0535  334 THR A OG1 
2353  C  CG2 . THR A 333 ? 0.9336 0.9243 1.3238 -0.2439 0.0232  0.0660  334 THR A CG2 
2354  N  N   . LEU A 334 ? 0.9242 0.9175 1.3597 -0.2017 0.0296  0.0295  335 LEU A N   
2355  C  CA  . LEU A 334 ? 0.9030 0.8790 1.3555 -0.1848 0.0236  0.0230  335 LEU A CA  
2356  C  C   . LEU A 334 ? 0.9876 0.9526 1.4506 -0.1860 0.0187  0.0192  335 LEU A C   
2357  O  O   . LEU A 334 ? 1.0145 0.9579 1.4877 -0.1823 0.0086  0.0225  335 LEU A O   
2358  C  CB  . LEU A 334 ? 0.8458 0.8349 1.3062 -0.1676 0.0324  0.0082  335 LEU A CB  
2359  C  CG  . LEU A 334 ? 0.8046 0.7814 1.2826 -0.1520 0.0292  -0.0026 335 LEU A CG  
2360  C  CD1 . LEU A 334 ? 0.7916 0.7463 1.2770 -0.1465 0.0188  0.0044  335 LEU A CD1 
2361  C  CD2 . LEU A 334 ? 0.7678 0.7597 1.2502 -0.1383 0.0385  -0.0166 335 LEU A CD2 
2362  N  N   . THR A 335 ? 0.9713 0.9520 1.4333 -0.1908 0.0256  0.0119  336 THR A N   
2363  C  CA  . THR A 335 ? 0.9799 0.9524 1.4510 -0.1933 0.0218  0.0075  336 THR A CA  
2364  C  C   . THR A 335 ? 1.0374 0.9844 1.5151 -0.1983 0.0098  0.0149  336 THR A C   
2365  O  O   . THR A 335 ? 1.0415 0.9802 1.5320 -0.1939 0.0073  0.0063  336 THR A O   
2366  C  CB  . THR A 335 ? 0.9813 0.9761 1.4503 -0.1981 0.0304  -0.0009 336 THR A CB  
2367  O  OG1 . THR A 335 ? 0.9526 0.9646 1.4252 -0.1847 0.0390  -0.0130 336 THR A OG1 
2368  C  CG2 . THR A 335 ? 0.9613 0.9472 1.4404 -0.1998 0.0264  -0.0071 336 THR A CG2 
2369  N  N   . ALA A 336 ? 1.0145 0.9499 1.4828 -0.2084 0.0024  0.0310  337 ALA A N   
2370  C  CA  . ALA A 336 ? 1.0313 0.9410 1.5069 -0.2114 -0.0107 0.0404  337 ALA A CA  
2371  C  C   . ALA A 336 ? 1.0387 0.9308 1.5371 -0.1984 -0.0173 0.0314  337 ALA A C   
2372  O  O   . ALA A 336 ? 1.0305 0.9159 1.5417 -0.1830 -0.0194 0.0259  337 ALA A O   
2373  C  CB  . ALA A 336 ? 0.9960 0.8960 1.4623 -0.2162 -0.0184 0.0569  337 ALA A CB  
2374  N  N   . LYS A 337 ? 1.0891 0.9750 1.5932 -0.2050 -0.0197 0.0287  338 LYS A N   
2375  C  CA  . LYS A 337 ? 1.0980 0.9723 1.6240 -0.1934 -0.0226 0.0154  338 LYS A CA  
2376  C  C   . LYS A 337 ? 1.1388 0.9900 1.6820 -0.1856 -0.0350 0.0211  338 LYS A C   
2377  O  O   . LYS A 337 ? 1.1946 1.0429 1.7547 -0.1694 -0.0344 0.0096  338 LYS A O   
2378  C  CB  . LYS A 337 ? 1.1174 0.9908 1.6447 -0.2042 -0.0226 0.0119  338 LYS A CB  
2379  N  N   . VAL A 338 ? 1.0939 0.9305 1.6328 -0.1975 -0.0459 0.0389  339 VAL A N   
2380  C  CA  . VAL A 338 ? 1.0448 0.8590 1.6017 -0.1926 -0.0605 0.0478  339 VAL A CA  
2381  C  C   . VAL A 338 ? 1.0185 0.8262 1.6039 -0.1727 -0.0618 0.0322  339 VAL A C   
2382  O  O   . VAL A 338 ? 0.9954 0.8082 1.5854 -0.1602 -0.0596 0.0281  339 VAL A O   
2383  C  CB  . VAL A 338 ? 1.0085 0.8196 1.5536 -0.1968 -0.0678 0.0667  339 VAL A CB  
2384  C  CG1 . VAL A 338 ? 1.0098 0.7990 1.5753 -0.1926 -0.0849 0.0778  339 VAL A CG1 
2385  C  CG2 . VAL A 338 ? 1.0074 0.8265 1.5240 -0.2181 -0.0656 0.0814  339 VAL A CG2 
2386  N  N   . PRO A 365 ? 1.0560 1.1898 1.4727 -0.0481 0.1217  -0.0799 366 PRO A N   
2387  C  CA  . PRO A 365 ? 1.0417 1.1726 1.4530 -0.0504 0.1236  -0.0793 366 PRO A CA  
2388  C  C   . PRO A 365 ? 1.0099 1.1516 1.4187 -0.0531 0.1313  -0.0892 366 PRO A C   
2389  O  O   . PRO A 365 ? 1.0280 1.1786 1.4297 -0.0658 0.1378  -0.0907 366 PRO A O   
2390  C  CB  . PRO A 365 ? 1.0506 1.1816 1.4575 -0.0645 0.1237  -0.0709 366 PRO A CB  
2391  C  CG  . PRO A 365 ? 1.0456 1.1712 1.4579 -0.0634 0.1185  -0.0655 366 PRO A CG  
2392  C  CD  . PRO A 365 ? 1.0427 1.1757 1.4594 -0.0570 0.1201  -0.0728 366 PRO A CD  
2393  N  N   . ARG A 366 ? 0.9814 1.1218 1.3956 -0.0426 0.1301  -0.0958 367 ARG A N   
2394  C  CA  . ARG A 366 ? 0.9724 1.1208 1.3878 -0.0435 0.1366  -0.1069 367 ARG A CA  
2395  C  C   . ARG A 366 ? 0.9033 1.0480 1.3126 -0.0453 0.1385  -0.1078 367 ARG A C   
2396  O  O   . ARG A 366 ? 0.8967 1.0295 1.3041 -0.0402 0.1323  -0.1001 367 ARG A O   
2397  C  CB  . ARG A 366 ? 1.0204 1.1651 1.4459 -0.0322 0.1322  -0.1112 367 ARG A CB  
2398  C  CG  . ARG A 366 ? 1.0580 1.2095 1.4895 -0.0322 0.1380  -0.1236 367 ARG A CG  
2399  C  CD  . ARG A 366 ? 1.0929 1.2405 1.5378 -0.0223 0.1320  -0.1255 367 ARG A CD  
2400  N  NE  . ARG A 366 ? 1.1265 1.2798 1.5811 -0.0223 0.1372  -0.1380 367 ARG A NE  
2401  C  CZ  . ARG A 366 ? 1.1503 1.3034 1.6211 -0.0159 0.1336  -0.1418 367 ARG A CZ  
2402  N  NH1 . ARG A 366 ? 1.1544 1.3030 1.6316 -0.0097 0.1248  -0.1334 367 ARG A NH1 
2403  N  NH2 . ARG A 366 ? 1.1631 1.3211 1.6450 -0.0166 0.1388  -0.1543 367 ARG A NH2 
2404  N  N   . GLU A 367 ? 0.8505 1.0063 1.2568 -0.0532 0.1475  -0.1178 368 GLU A N   
2405  C  CA  . GLU A 367 ? 0.8148 0.9692 1.2153 -0.0563 0.1503  -0.1206 368 GLU A CA  
2406  C  C   . GLU A 367 ? 0.7754 0.9160 1.1821 -0.0422 0.1434  -0.1206 368 GLU A C   
2407  O  O   . GLU A 367 ? 0.7735 0.9098 1.1889 -0.0330 0.1393  -0.1232 368 GLU A O   
2408  C  CB  . GLU A 367 ? 0.7987 0.9684 1.1949 -0.0675 0.1618  -0.1344 368 GLU A CB  
2409  N  N   . ARG A 368 ? 0.7631 0.8970 1.1653 -0.0421 0.1414  -0.1165 369 ARG A N   
2410  C  CA  . ARG A 368 ? 0.7447 0.8655 1.1506 -0.0308 0.1348  -0.1156 369 ARG A CA  
2411  C  C   . ARG A 368 ? 0.6835 0.8078 1.0951 -0.0296 0.1393  -0.1287 369 ARG A C   
2412  O  O   . ARG A 368 ? 0.6502 0.7851 1.0588 -0.0387 0.1484  -0.1387 369 ARG A O   
2413  C  CB  . ARG A 368 ? 0.7504 0.8651 1.1515 -0.0320 0.1324  -0.1090 369 ARG A CB  
2414  C  CG  . ARG A 368 ? 0.7338 0.8340 1.1368 -0.0210 0.1244  -0.1057 369 ARG A CG  
2415  C  CD  . ARG A 368 ? 0.7644 0.8608 1.1647 -0.0228 0.1231  -0.1009 369 ARG A CD  
2416  N  NE  . ARG A 368 ? 0.7974 0.8951 1.1966 -0.0284 0.1214  -0.0912 369 ARG A NE  
2417  C  CZ  . ARG A 368 ? 0.8301 0.9361 1.2269 -0.0412 0.1252  -0.0892 369 ARG A CZ  
2418  N  NH1 . ARG A 368 ? 0.8702 0.9853 1.2631 -0.0497 0.1323  -0.0978 369 ARG A NH1 
2419  N  NH2 . ARG A 368 ? 0.8008 0.9049 1.1985 -0.0476 0.1208  -0.0779 369 ARG A NH2 
2420  N  N   . PRO A 369 ? 0.6752 0.7915 1.0956 -0.0199 0.1327  -0.1285 370 PRO A N   
2421  C  CA  . PRO A 369 ? 0.6313 0.7493 1.0620 -0.0182 0.1351  -0.1400 370 PRO A CA  
2422  C  C   . PRO A 369 ? 0.5396 0.6548 0.9675 -0.0201 0.1378  -0.1449 370 PRO A C   
2423  O  O   . PRO A 369 ? 0.4583 0.5659 0.8785 -0.0187 0.1336  -0.1361 370 PRO A O   
2424  C  CB  . PRO A 369 ? 0.6453 0.7533 1.0852 -0.0083 0.1246  -0.1328 370 PRO A CB  
2425  C  CG  . PRO A 369 ? 0.6957 0.8020 1.1303 -0.0067 0.1197  -0.1220 370 PRO A CG  
2426  C  CD  . PRO A 369 ? 0.6568 0.7632 1.0787 -0.0119 0.1224  -0.1173 370 PRO A CD  
2427  N  N   . PRO A 370 ? 0.5007 0.6226 0.9361 -0.0236 0.1448  -0.1597 371 PRO A N   
2428  C  CA  . PRO A 370 ? 0.5439 0.6635 0.9780 -0.0258 0.1476  -0.1662 371 PRO A CA  
2429  C  C   . PRO A 370 ? 0.5837 0.6876 1.0208 -0.0163 0.1364  -0.1555 371 PRO A C   
2430  O  O   . PRO A 370 ? 0.5351 0.6341 0.9657 -0.0169 0.1353  -0.1523 371 PRO A O   
2431  C  CB  . PRO A 370 ? 0.4849 0.6128 0.9317 -0.0293 0.1551  -0.1843 371 PRO A CB  
2432  C  CG  . PRO A 370 ? 0.5330 0.6625 0.9922 -0.0246 0.1520  -0.1836 371 PRO A CG  
2433  C  CD  . PRO A 370 ? 0.4716 0.6029 0.9193 -0.0253 0.1500  -0.1718 371 PRO A CD  
2434  N  N   . SER A 371 ? 0.7303 0.8276 1.1773 -0.0088 0.1282  -0.1498 372 SER A N   
2435  C  CA  . SER A 371 ? 0.7624 0.8468 1.2097 -0.0016 0.1174  -0.1377 372 SER A CA  
2436  C  C   . SER A 371 ? 0.7425 0.8234 1.1918 0.0036  0.1095  -0.1269 372 SER A C   
2437  O  O   . SER A 371 ? 0.9308 1.0172 1.3913 0.0045  0.1102  -0.1312 372 SER A O   
2438  C  CB  . SER A 371 ? 0.7578 0.8384 1.2187 0.0005  0.1159  -0.1441 372 SER A CB  
2439  O  OG  . SER A 371 ? 0.7432 0.8130 1.2043 0.0061  0.1058  -0.1318 372 SER A OG  
2440  N  N   . GLY A 372 ? 0.5411 0.6138 0.9803 0.0066  0.1023  -0.1138 373 GLY A N   
2441  C  CA  . GLY A 372 ? 0.4255 0.4953 0.8656 0.0106  0.0948  -0.1040 373 GLY A CA  
2442  C  C   . GLY A 372 ? 0.3838 0.4444 0.8227 0.0143  0.0867  -0.0948 373 GLY A C   
2443  O  O   . GLY A 372 ? 0.3690 0.4254 0.8064 0.0139  0.0869  -0.0959 373 GLY A O   
2444  N  N   . THR A 373 ? 0.1945 0.2530 0.6346 0.0173  0.0801  -0.0862 374 THR A N   
2445  C  CA  . THR A 373 ? 0.1908 0.2426 0.6305 0.0198  0.0731  -0.0775 374 THR A CA  
2446  C  C   . THR A 373 ? 0.3312 0.3777 0.7555 0.0184  0.0732  -0.0729 374 THR A C   
2447  O  O   . THR A 373 ? 0.3355 0.3774 0.7601 0.0189  0.0712  -0.0712 374 THR A O   
2448  C  CB  . THR A 373 ? 0.1878 0.2404 0.6310 0.0221  0.0671  -0.0695 374 THR A CB  
2449  O  OG1 . THR A 373 ? 0.3224 0.3800 0.7829 0.0238  0.0661  -0.0732 374 THR A OG1 
2450  C  CG2 . THR A 373 ? 0.2100 0.2573 0.6544 0.0238  0.0608  -0.0611 374 THR A CG2 
2451  N  N   . LEU A 374 ? 0.1810 0.2286 0.5941 0.0166  0.0753  -0.0712 375 LEU A N   
2452  C  CA  . LEU A 374 ? 0.2933 0.3363 0.6947 0.0154  0.0750  -0.0670 375 LEU A CA  
2453  C  C   . LEU A 374 ? 0.1789 0.2206 0.5799 0.0137  0.0786  -0.0719 375 LEU A C   
2454  O  O   . LEU A 374 ? 0.3737 0.4107 0.7705 0.0139  0.0764  -0.0683 375 LEU A O   
2455  C  CB  . LEU A 374 ? 0.3084 0.3531 0.7029 0.0135  0.0770  -0.0655 375 LEU A CB  
2456  C  CG  . LEU A 374 ? 0.2970 0.3370 0.6833 0.0125  0.0762  -0.0612 375 LEU A CG  
2457  C  CD1 . LEU A 374 ? 0.1656 0.2011 0.5484 0.0143  0.0709  -0.0550 375 LEU A CD1 
2458  C  CD2 . LEU A 374 ? 0.3303 0.3717 0.7144 0.0106  0.0780  -0.0603 375 LEU A CD2 
2459  N  N   . GLU A 375 ? 0.1846 0.2317 0.5910 0.0116  0.0847  -0.0811 376 GLU A N   
2460  C  CA  . GLU A 375 ? 0.3695 0.4174 0.7769 0.0090  0.0895  -0.0879 376 GLU A CA  
2461  C  C   . GLU A 375 ? 0.3177 0.3617 0.7320 0.0107  0.0869  -0.0895 376 GLU A C   
2462  O  O   . GLU A 375 ? 0.2984 0.3393 0.7104 0.0099  0.0870  -0.0895 376 GLU A O   
2463  C  CB  . GLU A 375 ? 0.3455 0.4027 0.7577 0.0050  0.0983  -0.0993 376 GLU A CB  
2464  C  CG  . GLU A 375 ? 0.4456 0.5066 0.8583 0.0005  0.1052  -0.1080 376 GLU A CG  
2465  C  CD  . GLU A 375 ? 0.5155 0.5889 0.9295 -0.0060 0.1154  -0.1189 376 GLU A CD  
2466  O  OE1 . GLU A 375 ? 0.5276 0.6056 0.9398 -0.0071 0.1165  -0.1168 376 GLU A OE1 
2467  O  OE2 . GLU A 375 ? 0.5125 0.5924 0.9289 -0.0113 0.1229  -0.1302 376 GLU A OE2 
2468  N  N   . LYS A 376 ? 0.1947 0.2389 0.6195 0.0131  0.0843  -0.0906 377 LYS A N   
2469  C  CA  . LYS A 376 ? 0.2493 0.2896 0.6842 0.0147  0.0811  -0.0912 377 LYS A CA  
2470  C  C   . LYS A 376 ? 0.2717 0.3056 0.7001 0.0163  0.0747  -0.0803 377 LYS A C   
2471  O  O   . LYS A 376 ? 0.3006 0.3309 0.7308 0.0160  0.0739  -0.0805 377 LYS A O   
2472  C  CB  . LYS A 376 ? 0.2591 0.3013 0.7105 0.0172  0.0785  -0.0932 377 LYS A CB  
2473  C  CG  . LYS A 376 ? 0.2675 0.3171 0.7290 0.0154  0.0853  -0.1059 377 LYS A CG  
2474  C  CD  . LYS A 376 ? 0.2179 0.2683 0.7006 0.0182  0.0819  -0.1085 377 LYS A CD  
2475  C  CE  . LYS A 376 ? 0.2564 0.3154 0.7503 0.0165  0.0888  -0.1216 377 LYS A CE  
2476  N  NZ  . LYS A 376 ? 0.2350 0.2984 0.7265 0.0116  0.0982  -0.1349 377 LYS A NZ  
2477  N  N   . LEU A 377 ? 0.1855 0.2186 0.6071 0.0176  0.0709  -0.0717 378 LEU A N   
2478  C  CA  . LEU A 377 ? 0.3130 0.3417 0.7282 0.0184  0.0662  -0.0626 378 LEU A CA  
2479  C  C   . LEU A 377 ? 0.3208 0.3472 0.7261 0.0165  0.0682  -0.0625 378 LEU A C   
2480  O  O   . LEU A 377 ? 0.2709 0.2939 0.6759 0.0166  0.0657  -0.0589 378 LEU A O   
2481  C  CB  . LEU A 377 ? 0.2946 0.3246 0.7044 0.0192  0.0637  -0.0561 378 LEU A CB  
2482  C  CG  . LEU A 377 ? 0.3315 0.3635 0.7531 0.0214  0.0596  -0.0531 378 LEU A CG  
2483  C  CD1 . LEU A 377 ? 0.3285 0.3631 0.7445 0.0216  0.0582  -0.0483 378 LEU A CD1 
2484  C  CD2 . LEU A 377 ? 0.2768 0.3056 0.7090 0.0227  0.0548  -0.0483 378 LEU A CD2 
2485  N  N   . VAL A 378 ? 0.1769 0.2057 0.5764 0.0146  0.0725  -0.0664 379 VAL A N   
2486  C  CA  . VAL A 378 ? 0.2992 0.3265 0.6929 0.0130  0.0740  -0.0661 379 VAL A CA  
2487  C  C   . VAL A 378 ? 0.3970 0.4237 0.7969 0.0119  0.0762  -0.0721 379 VAL A C   
2488  O  O   . VAL A 378 ? 0.3672 0.3910 0.7654 0.0116  0.0745  -0.0694 379 VAL A O   
2489  C  CB  . VAL A 378 ? 0.2490 0.2798 0.6395 0.0109  0.0782  -0.0685 379 VAL A CB  
2490  C  CG1 . VAL A 378 ? 0.1752 0.2065 0.5666 0.0088  0.0808  -0.0707 379 VAL A CG1 
2491  C  CG2 . VAL A 378 ? 0.1697 0.1994 0.5540 0.0117  0.0752  -0.0616 379 VAL A CG2 
2492  N  N   . SER A 379 ? 0.2768 0.3068 0.6851 0.0111  0.0802  -0.0811 380 SER A N   
2493  C  CA  . SER A 379 ? 0.3518 0.3817 0.7679 0.0096  0.0829  -0.0889 380 SER A CA  
2494  C  C   . SER A 379 ? 0.3025 0.3270 0.7232 0.0116  0.0771  -0.0835 380 SER A C   
2495  O  O   . SER A 379 ? 0.2573 0.2794 0.6782 0.0107  0.0767  -0.0835 380 SER A O   
2496  C  CB  . SER A 379 ? 0.4048 0.4400 0.8313 0.0082  0.0886  -0.1011 380 SER A CB  
2497  O  OG  . SER A 379 ? 0.5266 0.5689 0.9500 0.0043  0.0963  -0.1091 380 SER A OG  
2498  N  N   . GLU A 380 ? 0.3642 0.3873 0.7902 0.0140  0.0728  -0.0789 381 GLU A N   
2499  C  CA  . GLU A 380 ? 0.3684 0.3872 0.8014 0.0155  0.0674  -0.0731 381 GLU A CA  
2500  C  C   . GLU A 380 ? 0.3099 0.3258 0.7327 0.0152  0.0646  -0.0646 381 GLU A C   
2501  O  O   . GLU A 380 ? 0.2358 0.2490 0.6626 0.0148  0.0630  -0.0634 381 GLU A O   
2502  C  CB  . GLU A 380 ? 0.3620 0.3808 0.8039 0.0179  0.0630  -0.0683 381 GLU A CB  
2503  C  CG  . GLU A 380 ? 0.4988 0.5138 0.9474 0.0190  0.0569  -0.0595 381 GLU A CG  
2504  C  CD  . GLU A 380 ? 0.5871 0.5994 1.0506 0.0188  0.0557  -0.0630 381 GLU A CD  
2505  O  OE1 . GLU A 380 ? 0.6290 0.6426 1.0999 0.0181  0.0594  -0.0733 381 GLU A OE1 
2506  O  OE2 . GLU A 380 ? 0.6468 0.6559 1.1157 0.0189  0.0513  -0.0559 381 GLU A OE2 
2507  N  N   . ALA A 381 ? 0.2798 0.2968 0.6912 0.0153  0.0643  -0.0597 382 ALA A N   
2508  C  CA  . ALA A 381 ? 0.2452 0.2605 0.6486 0.0150  0.0623  -0.0530 382 ALA A CA  
2509  C  C   . ALA A 381 ? 0.2416 0.2560 0.6429 0.0134  0.0640  -0.0556 382 ALA A C   
2510  O  O   . ALA A 381 ? 0.2527 0.2651 0.6544 0.0131  0.0619  -0.0521 382 ALA A O   
2511  C  CB  . ALA A 381 ? 0.1683 0.1852 0.5623 0.0153  0.0622  -0.0494 382 ALA A CB  
2512  N  N   . LYS A 382 ? 0.3217 0.3383 0.7225 0.0122  0.0680  -0.0621 383 LYS A N   
2513  C  CA  . LYS A 382 ? 0.1749 0.1917 0.5771 0.0106  0.0697  -0.0651 383 LYS A CA  
2514  C  C   . LYS A 382 ? 0.3695 0.3846 0.7806 0.0100  0.0698  -0.0693 383 LYS A C   
2515  O  O   . LYS A 382 ? 0.3508 0.3647 0.7637 0.0093  0.0685  -0.0681 383 LYS A O   
2516  C  CB  . LYS A 382 ? 0.2557 0.2768 0.6588 0.0088  0.0751  -0.0720 383 LYS A CB  
2517  C  CG  . LYS A 382 ? 0.3808 0.4032 0.7778 0.0090  0.0746  -0.0670 383 LYS A CG  
2518  C  CD  . LYS A 382 ? 0.3704 0.3982 0.7721 0.0064  0.0794  -0.0716 383 LYS A CD  
2519  C  CE  . LYS A 382 ? 0.3827 0.4170 0.7874 0.0038  0.0868  -0.0818 383 LYS A CE  
2520  N  NZ  . LYS A 382 ? 0.3383 0.3824 0.7475 -0.0009 0.0924  -0.0848 383 LYS A NZ  
2521  N  N   . ALA A 383 ? 0.3282 0.3435 0.7470 0.0103  0.0709  -0.0744 384 ALA A N   
2522  C  CA  . ALA A 383 ? 0.3036 0.3169 0.7334 0.0098  0.0704  -0.0784 384 ALA A CA  
2523  C  C   . ALA A 383 ? 0.2740 0.2836 0.7047 0.0108  0.0649  -0.0691 384 ALA A C   
2524  O  O   . ALA A 383 ? 0.2716 0.2797 0.7060 0.0097  0.0643  -0.0694 384 ALA A O   
2525  C  CB  . ALA A 383 ? 0.1955 0.2096 0.6366 0.0103  0.0716  -0.0849 384 ALA A CB  
2526  N  N   . GLN A 384 ? 0.1819 0.1907 0.6104 0.0124  0.0616  -0.0613 385 GLN A N   
2527  C  CA  . GLN A 384 ? 0.1794 0.1859 0.6108 0.0127  0.0575  -0.0532 385 GLN A CA  
2528  C  C   . GLN A 384 ? 0.2834 0.2900 0.7068 0.0117  0.0574  -0.0494 385 GLN A C   
2529  O  O   . GLN A 384 ? 0.3801 0.3853 0.8089 0.0111  0.0555  -0.0459 385 GLN A O   
2530  C  CB  . GLN A 384 ? 0.2851 0.2920 0.7171 0.0143  0.0548  -0.0466 385 GLN A CB  
2531  C  CG  . GLN A 384 ? 0.4389 0.4451 0.8857 0.0155  0.0525  -0.0476 385 GLN A CG  
2532  C  CD  . GLN A 384 ? 0.6401 0.6432 1.1029 0.0152  0.0491  -0.0453 385 GLN A CD  
2533  O  OE1 . GLN A 384 ? 0.6606 0.6625 1.1227 0.0139  0.0487  -0.0423 385 GLN A OE1 
2534  N  NE2 . GLN A 384 ? 0.6825 0.6846 1.1618 0.0164  0.0463  -0.0466 385 GLN A NE2 
2535  N  N   . LEU A 385 ? 0.2522 0.2607 0.6652 0.0116  0.0591  -0.0502 386 LEU A N   
2536  C  CA  . LEU A 385 ? 0.3180 0.3269 0.7261 0.0110  0.0583  -0.0469 386 LEU A CA  
2537  C  C   . LEU A 385 ? 0.2731 0.2818 0.6867 0.0097  0.0588  -0.0509 386 LEU A C   
2538  O  O   . LEU A 385 ? 0.2976 0.3059 0.7137 0.0091  0.0570  -0.0481 386 LEU A O   
2539  C  CB  . LEU A 385 ? 0.1967 0.2074 0.5955 0.0114  0.0590  -0.0457 386 LEU A CB  
2540  C  CG  . LEU A 385 ? 0.2144 0.2258 0.6081 0.0124  0.0583  -0.0416 386 LEU A CG  
2541  C  CD1 . LEU A 385 ? 0.1832 0.1961 0.5697 0.0125  0.0587  -0.0409 386 LEU A CD1 
2542  C  CD2 . LEU A 385 ? 0.2502 0.2614 0.6475 0.0123  0.0569  -0.0372 386 LEU A CD2 
2543  N  N   . ARG A 386 ? 0.2916 0.3011 0.7086 0.0091  0.0616  -0.0582 387 ARG A N   
2544  C  CA  . ARG A 386 ? 0.3422 0.3523 0.7674 0.0076  0.0627  -0.0637 387 ARG A CA  
2545  C  C   . ARG A 386 ? 0.3576 0.3651 0.7918 0.0071  0.0612  -0.0644 387 ARG A C   
2546  O  O   . ARG A 386 ? 0.2825 0.2899 0.7237 0.0059  0.0605  -0.0662 387 ARG A O   
2547  C  CB  . ARG A 386 ? 0.3538 0.3668 0.7825 0.0063  0.0681  -0.0741 387 ARG A CB  
2548  C  CG  . ARG A 386 ? 0.4557 0.4725 0.8800 0.0061  0.0701  -0.0740 387 ARG A CG  
2549  C  CD  . ARG A 386 ? 0.6039 0.6266 1.0341 0.0034  0.0774  -0.0862 387 ARG A CD  
2550  N  NE  . ARG A 386 ? 0.6775 0.7041 1.1025 0.0030  0.0807  -0.0868 387 ARG A NE  
2551  C  CZ  . ARG A 386 ? 0.7117 0.7449 1.1384 0.0012  0.0820  -0.0849 387 ARG A CZ  
2552  N  NH1 . ARG A 386 ? 0.7466 0.7847 1.1814 -0.0008 0.0791  -0.0811 387 ARG A NH1 
2553  N  NH2 . ARG A 386 ? 0.7723 0.8094 1.1950 0.0002  0.0853  -0.0854 387 ARG A NH2 
2554  N  N   . ASP A 387 ? 0.3671 0.3729 0.8037 0.0079  0.0603  -0.0625 388 ASP A N   
2555  C  CA  . ASP A 387 ? 0.3000 0.3033 0.7487 0.0075  0.0583  -0.0623 388 ASP A CA  
2556  C  C   . ASP A 387 ? 0.2811 0.2834 0.7314 0.0071  0.0552  -0.0540 388 ASP A C   
2557  O  O   . ASP A 387 ? 0.3396 0.3404 0.8008 0.0060  0.0538  -0.0542 388 ASP A O   
2558  C  CB  . ASP A 387 ? 0.3716 0.3737 0.8270 0.0087  0.0574  -0.0624 388 ASP A CB  
2559  C  CG  . ASP A 387 ? 0.4900 0.4895 0.9617 0.0083  0.0548  -0.0624 388 ASP A CG  
2560  O  OD1 . ASP A 387 ? 0.5036 0.5027 0.9827 0.0070  0.0563  -0.0698 388 ASP A OD1 
2561  O  OD2 . ASP A 387 ? 0.5377 0.5357 1.0164 0.0093  0.0511  -0.0551 388 ASP A OD2 
2562  N  N   . VAL A 388 ? 0.2574 0.2609 0.6982 0.0078  0.0545  -0.0476 389 VAL A N   
2563  C  CA  . VAL A 388 ? 0.2863 0.2897 0.7298 0.0073  0.0530  -0.0410 389 VAL A CA  
2564  C  C   . VAL A 388 ? 0.2711 0.2766 0.7085 0.0069  0.0531  -0.0402 389 VAL A C   
2565  O  O   . VAL A 388 ? 0.2742 0.2810 0.7121 0.0067  0.0530  -0.0360 389 VAL A O   
2566  C  CB  . VAL A 388 ? 0.1705 0.1744 0.6125 0.0082  0.0525  -0.0350 389 VAL A CB  
2567  C  CG1 . VAL A 388 ? 0.1747 0.1766 0.6274 0.0089  0.0507  -0.0344 389 VAL A CG1 
2568  C  CG2 . VAL A 388 ? 0.1674 0.1734 0.5955 0.0094  0.0539  -0.0352 389 VAL A CG2 
2569  N  N   . GLN A 389 ? 0.1683 0.1749 0.6028 0.0069  0.0534  -0.0443 390 GLN A N   
2570  C  CA  . GLN A 389 ? 0.2305 0.2392 0.6636 0.0068  0.0520  -0.0430 390 GLN A CA  
2571  C  C   . GLN A 389 ? 0.1677 0.1766 0.6117 0.0056  0.0503  -0.0426 390 GLN A C   
2572  O  O   . GLN A 389 ? 0.1657 0.1766 0.6112 0.0056  0.0486  -0.0404 390 GLN A O   
2573  C  CB  . GLN A 389 ? 0.2446 0.2547 0.6765 0.0071  0.0520  -0.0465 390 GLN A CB  
2574  C  CG  . GLN A 389 ? 0.3449 0.3548 0.7848 0.0062  0.0536  -0.0535 390 GLN A CG  
2575  C  CD  . GLN A 389 ? 0.4101 0.4232 0.8518 0.0061  0.0547  -0.0575 390 GLN A CD  
2576  O  OE1 . GLN A 389 ? 0.5614 0.5764 1.0008 0.0069  0.0526  -0.0532 390 GLN A OE1 
2577  N  NE2 . GLN A 389 ? 0.5244 0.5389 0.9726 0.0048  0.0584  -0.0664 390 GLN A NE2 
2578  N  N   . ASP A 390 ? 0.1700 0.1767 0.6230 0.0045  0.0505  -0.0451 391 ASP A N   
2579  C  CA  . ASP A 390 ? 0.1714 0.1781 0.6366 0.0031  0.0488  -0.0454 391 ASP A CA  
2580  C  C   . ASP A 390 ? 0.1716 0.1771 0.6425 0.0024  0.0490  -0.0405 391 ASP A C   
2581  O  O   . ASP A 390 ? 0.1733 0.1784 0.6557 0.0010  0.0479  -0.0402 391 ASP A O   
2582  C  CB  . ASP A 390 ? 0.3462 0.3514 0.8215 0.0019  0.0491  -0.0524 391 ASP A CB  
2583  C  CG  . ASP A 390 ? 0.3761 0.3785 0.8533 0.0020  0.0507  -0.0546 391 ASP A CG  
2584  O  OD1 . ASP A 390 ? 0.3307 0.3322 0.8041 0.0028  0.0507  -0.0491 391 ASP A OD1 
2585  O  OD2 . ASP A 390 ? 0.4418 0.4433 0.9261 0.0014  0.0520  -0.0625 391 ASP A OD2 
2586  N  N   . PHE A 391 ? 0.1703 0.1758 0.6349 0.0033  0.0505  -0.0367 392 PHE A N   
2587  C  CA  . PHE A 391 ? 0.3118 0.3166 0.7847 0.0027  0.0509  -0.0315 392 PHE A CA  
2588  C  C   . PHE A 391 ? 0.2668 0.2743 0.7478 0.0017  0.0512  -0.0294 392 PHE A C   
2589  O  O   . PHE A 391 ? 0.3535 0.3591 0.8485 0.0003  0.0502  -0.0276 392 PHE A O   
2590  C  CB  . PHE A 391 ? 0.1699 0.1766 0.6343 0.0041  0.0526  -0.0281 392 PHE A CB  
2591  C  CG  . PHE A 391 ? 0.2590 0.2664 0.7346 0.0036  0.0528  -0.0218 392 PHE A CG  
2592  C  CD1 . PHE A 391 ? 0.2950 0.2982 0.7832 0.0033  0.0501  -0.0189 392 PHE A CD1 
2593  C  CD2 . PHE A 391 ? 0.1711 0.1859 0.6467 0.0031  0.0555  -0.0188 392 PHE A CD2 
2594  C  CE1 . PHE A 391 ? 0.1774 0.1816 0.6802 0.0028  0.0487  -0.0108 392 PHE A CE1 
2595  C  CE2 . PHE A 391 ? 0.2008 0.2209 0.6877 0.0012  0.0555  -0.0117 392 PHE A CE2 
2596  C  CZ  . PHE A 391 ? 0.2089 0.2233 0.7104 0.0012  0.0514  -0.0065 392 PHE A CZ  
2597  N  N   . TRP A 392 ? 0.1925 0.2051 0.6657 0.0023  0.0524  -0.0300 393 TRP A N   
2598  C  CA  . TRP A 392 ? 0.1869 0.2062 0.6657 0.0012  0.0537  -0.0288 393 TRP A CA  
2599  C  C   . TRP A 392 ? 0.1731 0.1923 0.6627 -0.0002 0.0512  -0.0300 393 TRP A C   
2600  O  O   . TRP A 392 ? 0.2131 0.2387 0.7094 -0.0024 0.0521  -0.0283 393 TRP A O   
2601  C  CB  . TRP A 392 ? 0.1695 0.1943 0.6395 0.0022  0.0552  -0.0311 393 TRP A CB  
2602  C  CG  . TRP A 392 ? 0.2573 0.2831 0.7176 0.0032  0.0578  -0.0306 393 TRP A CG  
2603  C  CD1 . TRP A 392 ? 0.3082 0.3313 0.7581 0.0049  0.0570  -0.0323 393 TRP A CD1 
2604  C  CD2 . TRP A 392 ? 0.2829 0.3148 0.7445 0.0019  0.0615  -0.0279 393 TRP A CD2 
2605  N  NE1 . TRP A 392 ? 0.2386 0.2643 0.6828 0.0053  0.0599  -0.0314 393 TRP A NE1 
2606  C  CE2 . TRP A 392 ? 0.2691 0.3007 0.7208 0.0035  0.0627  -0.0287 393 TRP A CE2 
2607  C  CE3 . TRP A 392 ? 0.1953 0.2348 0.6659 -0.0016 0.0636  -0.0240 393 TRP A CE3 
2608  C  CZ2 . TRP A 392 ? 0.2523 0.2910 0.7038 0.0021  0.0660  -0.0265 393 TRP A CZ2 
2609  C  CZ3 . TRP A 392 ? 0.2102 0.2580 0.6798 -0.0045 0.0668  -0.0208 393 TRP A CZ3 
2610  C  CH2 . TRP A 392 ? 0.2887 0.3363 0.7495 -0.0022 0.0680  -0.0223 393 TRP A CH2 
2611  N  N   . ILE A 393 ? 0.1732 0.1875 0.6645 0.0001  0.0482  -0.0333 394 ILE A N   
2612  C  CA  . ILE A 393 ? 0.1768 0.1916 0.6799 -0.0014 0.0454  -0.0351 394 ILE A CA  
2613  C  C   . ILE A 393 ? 0.2931 0.3013 0.8067 -0.0024 0.0447  -0.0367 394 ILE A C   
2614  O  O   . ILE A 393 ? 0.3293 0.3380 0.8540 -0.0041 0.0426  -0.0380 394 ILE A O   
2615  C  CB  . ILE A 393 ? 0.1746 0.1914 0.6768 -0.0010 0.0419  -0.0384 394 ILE A CB  
2616  C  CG1 . ILE A 393 ? 0.1741 0.1869 0.6724 -0.0003 0.0419  -0.0424 394 ILE A CG1 
2617  C  CG2 . ILE A 393 ? 0.3567 0.3786 0.8526 0.0004  0.0415  -0.0369 394 ILE A CG2 
2618  C  CD1 . ILE A 393 ? 0.1745 0.1911 0.6778 -0.0008 0.0381  -0.0456 394 ILE A CD1 
2619  N  N   . SER A 394 ? 0.3290 0.3322 0.8396 -0.0019 0.0460  -0.0370 395 SER A N   
2620  C  CA  . SER A 394 ? 0.3387 0.3377 0.8619 -0.0034 0.0450  -0.0392 395 SER A CA  
2621  C  C   . SER A 394 ? 0.2453 0.2428 0.7780 -0.0028 0.0441  -0.0320 395 SER A C   
2622  O  O   . SER A 394 ? 0.1882 0.1874 0.7348 -0.0024 0.0419  -0.0321 395 SER A O   
2623  C  CB  . SER A 394 ? 0.3244 0.3239 0.8392 -0.0023 0.0460  -0.0429 395 SER A CB  
2624  O  OG  . SER A 394 ? 0.3737 0.3726 0.8823 -0.0011 0.0468  -0.0370 395 SER A OG  
2625  N  N   . LEU A 395 ? 0.1833 0.1842 0.7123 -0.0025 0.0459  -0.0258 396 LEU A N   
2626  C  CA  . LEU A 395 ? 0.3399 0.3444 0.8762 -0.0054 0.0447  -0.0170 396 LEU A CA  
2627  C  C   . LEU A 395 ? 0.3968 0.3991 0.9414 -0.0102 0.0408  -0.0148 396 LEU A C   
2628  O  O   . LEU A 395 ? 0.4313 0.4269 0.9825 -0.0119 0.0367  -0.0098 396 LEU A O   
2629  C  CB  . LEU A 395 ? 0.3376 0.3536 0.8628 -0.0087 0.0481  -0.0128 396 LEU A CB  
2630  C  CG  . LEU A 395 ? 0.3726 0.3918 0.8890 -0.0068 0.0508  -0.0109 396 LEU A CG  
2631  C  CD1 . LEU A 395 ? 0.3923 0.4252 0.9003 -0.0117 0.0550  -0.0087 396 LEU A CD1 
2632  C  CD2 . LEU A 395 ? 0.4142 0.4281 0.9401 -0.0072 0.0475  -0.0043 396 LEU A CD2 
2633  N  N   . PRO A 396 ? 0.3534 0.3598 0.8960 -0.0127 0.0409  -0.0181 397 PRO A N   
2634  C  CA  . PRO A 396 ? 0.3733 0.3761 0.9211 -0.0184 0.0369  -0.0157 397 PRO A CA  
2635  C  C   . PRO A 396 ? 0.3585 0.3503 0.9133 -0.0162 0.0332  -0.0206 397 PRO A C   
2636  O  O   . PRO A 396 ? 0.3954 0.3801 0.9548 -0.0193 0.0289  -0.0160 397 PRO A O   
2637  C  CB  . PRO A 396 ? 0.3381 0.3487 0.8834 -0.0205 0.0376  -0.0196 397 PRO A CB  
2638  C  CG  . PRO A 396 ? 0.3098 0.3290 0.8475 -0.0169 0.0418  -0.0213 397 PRO A CG  
2639  C  CD  . PRO A 396 ? 0.3289 0.3421 0.8644 -0.0111 0.0431  -0.0233 397 PRO A CD  
2640  N  N   . GLY A 397 ? 0.3416 0.3329 0.8961 -0.0116 0.0348  -0.0302 398 GLY A N   
2641  C  CA  . GLY A 397 ? 0.2162 0.2006 0.7740 -0.0104 0.0328  -0.0378 398 GLY A CA  
2642  C  C   . GLY A 397 ? 0.3592 0.3388 0.9228 -0.0079 0.0308  -0.0347 398 GLY A C   
2643  O  O   . GLY A 397 ? 0.3335 0.3057 0.9034 -0.0091 0.0269  -0.0358 398 GLY A O   
2644  N  N   . THR A 398 ? 0.3892 0.3731 0.9516 -0.0049 0.0326  -0.0306 399 THR A N   
2645  C  CA  . THR A 398 ? 0.4104 0.3907 0.9783 -0.0031 0.0294  -0.0268 399 THR A CA  
2646  C  C   . THR A 398 ? 0.4111 0.3850 0.9850 -0.0064 0.0235  -0.0139 399 THR A C   
2647  O  O   . THR A 398 ? 0.4159 0.3829 0.9986 -0.0062 0.0177  -0.0113 399 THR A O   
2648  C  CB  . THR A 398 ? 0.3754 0.3619 0.9379 -0.0007 0.0325  -0.0256 399 THR A CB  
2649  O  OG1 . THR A 398 ? 0.4652 0.4555 1.0261 -0.0015 0.0341  -0.0168 399 THR A OG1 
2650  C  CG2 . THR A 398 ? 0.3532 0.3440 0.9043 -0.0002 0.0375  -0.0365 399 THR A CG2 
2651  N  N   . LEU A 399 ? 0.3596 0.3363 0.9278 -0.0109 0.0246  -0.0058 400 LEU A N   
2652  C  CA  . LEU A 399 ? 0.4028 0.3754 0.9717 -0.0181 0.0192  0.0076  400 LEU A CA  
2653  C  C   . LEU A 399 ? 0.3518 0.3165 0.9259 -0.0219 0.0140  0.0078  400 LEU A C   
2654  O  O   . LEU A 399 ? 0.3491 0.3062 0.9284 -0.0257 0.0067  0.0173  400 LEU A O   
2655  C  CB  . LEU A 399 ? 0.3880 0.3708 0.9463 -0.0251 0.0234  0.0138  400 LEU A CB  
2656  C  CG  . LEU A 399 ? 0.4152 0.4051 0.9678 -0.0249 0.0265  0.0183  400 LEU A CG  
2657  C  CD1 . LEU A 399 ? 0.3730 0.3776 0.9141 -0.0329 0.0319  0.0217  400 LEU A CD1 
2658  C  CD2 . LEU A 399 ? 0.4100 0.3924 0.9674 -0.0266 0.0190  0.0293  400 LEU A CD2 
2659  N  N   . CYS A 400 ? 0.3790 0.3453 0.9517 -0.0215 0.0171  -0.0022 401 CYS A N   
2660  C  CA  . CYS A 400 ? 0.4309 0.3898 1.0085 -0.0251 0.0127  -0.0041 401 CYS A CA  
2661  C  C   . CYS A 400 ? 0.5068 0.4574 1.0949 -0.0201 0.0092  -0.0110 401 CYS A C   
2662  O  O   . CYS A 400 ? 0.4926 0.4342 1.0890 -0.0226 0.0027  -0.0067 401 CYS A O   
2663  C  CB  . CYS A 400 ? 0.4646 0.4285 1.0374 -0.0270 0.0165  -0.0129 401 CYS A CB  
2664  S  SG  . CYS A 400 ? 0.4698 0.4450 1.0346 -0.0351 0.0190  -0.0054 401 CYS A SG  
2665  N  N   . SER A 401 ? 0.5154 0.4700 1.1033 -0.0138 0.0137  -0.0219 402 SER A N   
2666  C  CA  . SER A 401 ? 0.5625 0.5127 1.1600 -0.0101 0.0124  -0.0314 402 SER A CA  
2667  C  C   . SER A 401 ? 0.6736 0.6188 1.2831 -0.0084 0.0057  -0.0227 402 SER A C   
2668  O  O   . SER A 401 ? 0.7015 0.6397 1.3239 -0.0077 0.0012  -0.0262 402 SER A O   
2669  C  CB  . SER A 401 ? 0.5580 0.5155 1.1497 -0.0060 0.0194  -0.0440 402 SER A CB  
2670  O  OG  . SER A 401 ? 0.5944 0.5492 1.1954 -0.0035 0.0193  -0.0537 402 SER A OG  
2671  N  N   . GLU A 402 ? 0.6816 0.6302 1.2878 -0.0081 0.0045  -0.0114 403 GLU A N   
2672  C  CA  . GLU A 402 ? 0.7657 0.7102 1.3829 -0.0068 -0.0030 -0.0023 403 GLU A CA  
2673  C  C   . GLU A 402 ? 0.8426 0.7777 1.4655 -0.0128 -0.0127 0.0129  403 GLU A C   
2674  O  O   . GLU A 402 ? 0.8802 0.8081 1.5182 -0.0120 -0.0210 0.0165  403 GLU A O   
2675  C  CB  . GLU A 402 ? 0.7531 0.7047 1.3637 -0.0050 -0.0008 0.0037  403 GLU A CB  
2676  C  CG  . GLU A 402 ? 0.7916 0.7509 1.3995 0.0002  0.0060  -0.0093 403 GLU A CG  
2677  C  CD  . GLU A 402 ? 0.8406 0.8063 1.4418 0.0014  0.0078  -0.0033 403 GLU A CD  
2678  O  OE1 . GLU A 402 ? 0.8549 0.8202 1.4519 -0.0017 0.0059  0.0092  403 GLU A OE1 
2679  O  OE2 . GLU A 402 ? 0.8363 0.8066 1.4351 0.0042  0.0114  -0.0112 403 GLU A OE2 
2680  N  N   . LYS A 403 ? 0.8226 0.7581 1.4336 -0.0199 -0.0120 0.0219  404 LYS A N   
2681  C  CA  . LYS A 403 ? 0.8491 0.7777 1.4605 -0.0286 -0.0210 0.0391  404 LYS A CA  
2682  C  C   . LYS A 403 ? 0.8472 0.7707 1.4574 -0.0355 -0.0227 0.0397  404 LYS A C   
2683  O  O   . LYS A 403 ? 0.8447 0.7582 1.4667 -0.0368 -0.0307 0.0424  404 LYS A O   
2684  C  CB  . LYS A 403 ? 0.8532 0.7888 1.4501 -0.0356 -0.0192 0.0516  404 LYS A CB  
2685  C  CG  . LYS A 403 ? 0.8709 0.8132 1.4661 -0.0293 -0.0153 0.0493  404 LYS A CG  
2686  C  CD  . LYS A 403 ? 0.9151 0.8578 1.5055 -0.0366 -0.0216 0.0668  404 LYS A CD  
2687  C  CE  . LYS A 403 ? 0.9136 0.8630 1.5023 -0.0307 -0.0175 0.0641  404 LYS A CE  
2688  N  NZ  . LYS A 403 ? 0.9114 0.8631 1.5080 -0.0183 -0.0112 0.0461  404 LYS A NZ  
2689  N  N   . MET A 404 ? 0.8329 0.7639 1.4301 -0.0402 -0.0155 0.0371  405 MET A N   
2690  C  CA  . MET A 404 ? 0.8247 0.7538 1.4180 -0.0497 -0.0171 0.0412  405 MET A CA  
2691  C  C   . MET A 404 ? 0.7667 0.6896 1.3676 -0.0469 -0.0171 0.0286  405 MET A C   
2692  O  O   . MET A 404 ? 0.7876 0.7023 1.3933 -0.0527 -0.0231 0.0333  405 MET A O   
2693  C  CB  . MET A 404 ? 0.8599 0.8028 1.4384 -0.0561 -0.0091 0.0423  405 MET A CB  
2694  C  CG  . MET A 404 ? 0.8695 0.8208 1.4392 -0.0595 -0.0072 0.0520  405 MET A CG  
2695  S  SD  . MET A 404 ? 0.9466 0.9180 1.5030 -0.0621 0.0050  0.0463  405 MET A SD  
2696  C  CE  . MET A 404 ? 0.6436 0.6218 1.1922 -0.0657 0.0054  0.0572  405 MET A CE  
2697  N  N   . ALA A 405 ? 0.6660 0.5930 1.2672 -0.0392 -0.0104 0.0128  406 ALA A N   
2698  C  CA  . ALA A 405 ? 0.5796 0.5024 1.1855 -0.0382 -0.0095 -0.0002 406 ALA A CA  
2699  C  C   . ALA A 405 ? 0.5349 0.4493 1.1557 -0.0319 -0.0129 -0.0083 406 ALA A C   
2700  O  O   . ALA A 405 ? 0.5838 0.4907 1.2126 -0.0333 -0.0154 -0.0150 406 ALA A O   
2701  C  CB  . ALA A 405 ? 0.5504 0.4825 1.1472 -0.0358 -0.0012 -0.0126 406 ALA A CB  
2702  N  N   . ASP A 412 ? 1.1618 1.0126 1.8453 -0.0532 -0.0210 -0.0975 413 ASP A N   
2703  C  CA  . ASP A 412 ? 1.1309 0.9942 1.7939 -0.0534 -0.0160 -0.0935 413 ASP A CA  
2704  C  C   . ASP A 412 ? 1.0446 0.9107 1.6923 -0.0626 -0.0175 -0.0865 413 ASP A C   
2705  O  O   . ASP A 412 ? 1.0501 0.9259 1.6823 -0.0650 -0.0128 -0.0910 413 ASP A O   
2706  C  CB  . ASP A 412 ? 1.1885 1.0597 1.8447 -0.0503 -0.0068 -0.1122 413 ASP A CB  
2707  C  CG  . ASP A 412 ? 1.2287 1.1023 1.8978 -0.0410 -0.0041 -0.1170 413 ASP A CG  
2708  O  OD1 . ASP A 412 ? 1.2487 1.1197 1.9291 -0.0366 -0.0098 -0.1031 413 ASP A OD1 
2709  O  OD2 . ASP A 412 ? 1.2422 1.1207 1.9100 -0.0393 0.0036  -0.1345 413 ASP A OD2 
2710  N  N   . ARG A 413 ? 0.9771 0.8352 1.6303 -0.0685 -0.0246 -0.0753 414 ARG A N   
2711  C  CA  . ARG A 413 ? 0.8504 0.7131 1.4914 -0.0777 -0.0265 -0.0655 414 ARG A CA  
2712  C  C   . ARG A 413 ? 0.8037 0.6713 1.4410 -0.0778 -0.0291 -0.0455 414 ARG A C   
2713  O  O   . ARG A 413 ? 0.7746 0.6344 1.4219 -0.0766 -0.0348 -0.0344 414 ARG A O   
2714  C  CB  . ARG A 413 ? 0.8634 0.7155 1.5110 -0.0860 -0.0320 -0.0659 414 ARG A CB  
2715  N  N   . CYS A 414 ? 0.6999 0.5810 1.3233 -0.0800 -0.0252 -0.0410 415 CYS A N   
2716  C  CA  . CYS A 414 ? 0.5990 0.4875 1.2174 -0.0788 -0.0248 -0.0261 415 CYS A CA  
2717  C  C   . CYS A 414 ? 0.5154 0.4132 1.1250 -0.0884 -0.0252 -0.0140 415 CYS A C   
2718  O  O   . CYS A 414 ? 0.4123 0.3141 1.0186 -0.0952 -0.0250 -0.0178 415 CYS A O   
2719  C  CB  . CYS A 414 ? 0.3907 0.2891 1.0027 -0.0706 -0.0182 -0.0324 415 CYS A CB  
2720  S  SG  . CYS A 414 ? 1.0234 0.9316 1.6251 -0.0719 -0.0125 -0.0480 415 CYS A SG  
2721  N  N   . TRP A 415 ? 0.4101 0.3126 1.0163 -0.0898 -0.0256 0.0003  416 TRP A N   
2722  C  CA  . TRP A 415 ? 0.4172 0.3310 1.0151 -0.0997 -0.0245 0.0117  416 TRP A CA  
2723  C  C   . TRP A 415 ? 0.3804 0.3123 0.9700 -0.0979 -0.0171 0.0067  416 TRP A C   
2724  O  O   . TRP A 415 ? 0.3651 0.3027 0.9516 -0.0907 -0.0130 0.0056  416 TRP A O   
2725  C  CB  . TRP A 415 ? 0.4185 0.3303 1.0150 -0.1034 -0.0278 0.0283  416 TRP A CB  
2726  C  CG  . TRP A 415 ? 0.4609 0.3881 1.0468 -0.1131 -0.0242 0.0392  416 TRP A CG  
2727  C  CD1 . TRP A 415 ? 0.3936 0.3340 0.9718 -0.1113 -0.0184 0.0424  416 TRP A CD1 
2728  C  CD2 . TRP A 415 ? 0.4706 0.4029 1.0527 -0.1271 -0.0255 0.0478  416 TRP A CD2 
2729  N  NE1 . TRP A 415 ? 0.3910 0.3455 0.9611 -0.1233 -0.0152 0.0511  416 TRP A NE1 
2730  C  CE2 . TRP A 415 ? 0.4731 0.4233 1.0452 -0.1334 -0.0194 0.0547  416 TRP A CE2 
2731  C  CE3 . TRP A 415 ? 0.5149 0.4390 1.1012 -0.1354 -0.0306 0.0495  416 TRP A CE3 
2732  C  CZ2 . TRP A 415 ? 0.4743 0.4361 1.0405 -0.1481 -0.0176 0.0626  416 TRP A CZ2 
2733  C  CZ3 . TRP A 415 ? 0.5380 0.4723 1.1182 -0.1498 -0.0296 0.0585  416 TRP A CZ3 
2734  C  CH2 . TRP A 415 ? 0.5401 0.4937 1.1102 -0.1562 -0.0228 0.0646  416 TRP A CH2 
2735  N  N   . ASN A 416 ? 0.4121 0.3533 0.9995 -0.1046 -0.0159 0.0038  417 ASN A N   
2736  C  CA  . ASN A 416 ? 0.3619 0.3209 0.9444 -0.1032 -0.0103 -0.0008 417 ASN A CA  
2737  C  C   . ASN A 416 ? 0.3574 0.3327 0.9360 -0.1103 -0.0066 0.0093  417 ASN A C   
2738  O  O   . ASN A 416 ? 0.4533 0.4451 1.0301 -0.1091 -0.0019 0.0063  417 ASN A O   
2739  C  CB  . ASN A 416 ? 0.3642 0.3259 0.9482 -0.1058 -0.0118 -0.0110 417 ASN A CB  
2740  C  CG  . ASN A 416 ? 0.3815 0.3410 0.9684 -0.1169 -0.0159 -0.0069 417 ASN A CG  
2741  O  OD1 . ASN A 416 ? 0.3875 0.3513 0.9737 -0.1245 -0.0158 0.0041  417 ASN A OD1 
2742  N  ND2 . ASN A 416 ? 0.3910 0.3442 0.9802 -0.1192 -0.0193 -0.0162 417 ASN A ND2 
2743  N  N   . GLY A 417 ? 0.3806 0.3512 0.9580 -0.1182 -0.0091 0.0210  418 GLY A N   
2744  C  CA  . GLY A 417 ? 0.4183 0.4042 0.9901 -0.1276 -0.0051 0.0308  418 GLY A CA  
2745  C  C   . GLY A 417 ? 0.4540 0.4465 1.0263 -0.1410 -0.0061 0.0350  418 GLY A C   
2746  O  O   . GLY A 417 ? 0.4919 0.4928 1.0588 -0.1520 -0.0042 0.0450  418 GLY A O   
2747  N  N   . MET A 418 ? 0.4045 0.3945 0.9824 -0.1414 -0.0089 0.0273  419 MET A N   
2748  C  CA  . MET A 418 ? 0.5190 0.5086 1.0986 -0.1540 -0.0121 0.0317  419 MET A CA  
2749  C  C   . MET A 418 ? 0.5829 0.5489 1.1654 -0.1566 -0.0203 0.0362  419 MET A C   
2750  O  O   . MET A 418 ? 0.6517 0.6145 1.2328 -0.1683 -0.0232 0.0465  419 MET A O   
2751  C  CB  . MET A 418 ? 0.5159 0.5155 1.1005 -0.1547 -0.0118 0.0220  419 MET A CB  
2752  C  CG  . MET A 418 ? 0.4959 0.5216 1.0807 -0.1569 -0.0048 0.0211  419 MET A CG  
2753  S  SD  . MET A 418 ? 1.0393 1.0772 1.6306 -0.1486 -0.0045 0.0083  419 MET A SD  
2754  C  CE  . MET A 418 ? 0.8970 0.9162 1.4911 -0.1507 -0.0132 0.0023  419 MET A CE  
2755  N  N   . ALA A 419 ? 0.5632 0.5135 1.1505 -0.1460 -0.0237 0.0279  420 ALA A N   
2756  C  CA  . ALA A 419 ? 0.5482 0.4764 1.1418 -0.1464 -0.0312 0.0287  420 ALA A CA  
2757  C  C   . ALA A 419 ? 0.5873 0.5027 1.1859 -0.1329 -0.0323 0.0187  420 ALA A C   
2758  O  O   . ALA A 419 ? 0.5447 0.4680 1.1404 -0.1241 -0.0273 0.0122  420 ALA A O   
2759  C  CB  . ALA A 419 ? 0.5338 0.4590 1.1314 -0.1542 -0.0344 0.0238  420 ALA A CB  
2760  N  N   . ARG A 420 ? 0.5997 0.4963 1.2071 -0.1316 -0.0385 0.0170  421 ARG A N   
2761  C  CA  . ARG A 420 ? 0.6793 0.5654 1.2936 -0.1200 -0.0386 0.0040  421 ARG A CA  
2762  C  C   . ARG A 420 ? 0.6657 0.5558 1.2782 -0.1195 -0.0356 -0.0122 421 ARG A C   
2763  O  O   . ARG A 420 ? 0.6931 0.5852 1.3049 -0.1285 -0.0373 -0.0132 421 ARG A O   
2764  C  CB  . ARG A 420 ? 0.4817 0.3481 1.1089 -0.1189 -0.0460 0.0060  421 ARG A CB  
2765  N  N   . GLY A 421 ? 0.6183 0.5102 1.2295 -0.1102 -0.0314 -0.0247 422 GLY A N   
2766  C  CA  . GLY A 421 ? 0.6803 0.5780 1.2868 -0.1114 -0.0289 -0.0389 422 GLY A CA  
2767  C  C   . GLY A 421 ? 0.7294 0.6357 1.3297 -0.1033 -0.0234 -0.0476 422 GLY A C   
2768  O  O   . GLY A 421 ? 0.7649 0.6681 1.3672 -0.0947 -0.0212 -0.0475 422 GLY A O   
2769  N  N   . ARG A 422 ? 0.6986 0.6155 1.2916 -0.1066 -0.0219 -0.0548 423 ARG A N   
2770  C  CA  . ARG A 422 ? 0.7027 0.6287 1.2887 -0.1007 -0.0176 -0.0616 423 ARG A CA  
2771  C  C   . ARG A 422 ? 0.7172 0.6605 1.2991 -0.1010 -0.0159 -0.0520 423 ARG A C   
2772  O  O   . ARG A 422 ? 0.7515 0.7030 1.3344 -0.1080 -0.0179 -0.0453 423 ARG A O   
2773  C  CB  . ARG A 422 ? 0.6875 0.6135 1.2680 -0.1049 -0.0180 -0.0769 423 ARG A CB  
2774  N  N   . TYR A 423 ? 0.6318 0.5812 1.2102 -0.0933 -0.0118 -0.0520 424 TYR A N   
2775  C  CA  . TYR A 423 ? 0.5825 0.5483 1.1585 -0.0922 -0.0095 -0.0446 424 TYR A CA  
2776  C  C   . TYR A 423 ? 0.4848 0.4607 1.0559 -0.0921 -0.0100 -0.0522 424 TYR A C   
2777  O  O   . TYR A 423 ? 0.4848 0.4586 1.0513 -0.0871 -0.0080 -0.0592 424 TYR A O   
2778  C  CB  . TYR A 423 ? 0.4778 0.4442 1.0536 -0.0843 -0.0053 -0.0381 424 TYR A CB  
2779  C  CG  . TYR A 423 ? 0.4596 0.4424 1.0333 -0.0821 -0.0017 -0.0323 424 TYR A CG  
2780  C  CD1 . TYR A 423 ? 0.3871 0.3797 0.9626 -0.0869 -0.0005 -0.0226 424 TYR A CD1 
2781  C  CD2 . TYR A 423 ? 0.4186 0.4075 0.9888 -0.0757 0.0008  -0.0372 424 TYR A CD2 
2782  C  CE1 . TYR A 423 ? 0.3551 0.3636 0.9299 -0.0846 0.0038  -0.0193 424 TYR A CE1 
2783  C  CE2 . TYR A 423 ? 0.3646 0.3680 0.9346 -0.0729 0.0039  -0.0327 424 TYR A CE2 
2784  C  CZ  . TYR A 423 ? 0.3922 0.4054 0.9648 -0.0769 0.0057  -0.0245 424 TYR A CZ  
2785  O  OH  . TYR A 423 ? 0.2950 0.3231 0.8681 -0.0740 0.0097  -0.0221 424 TYR A OH  
2786  N  N   . LEU A 424 ? 0.5345 0.5216 1.1069 -0.0986 -0.0132 -0.0502 425 LEU A N   
2787  C  CA  . LEU A 424 ? 0.5266 0.5242 1.0958 -0.1005 -0.0164 -0.0552 425 LEU A CA  
2788  C  C   . LEU A 424 ? 0.5423 0.5517 1.1108 -0.0935 -0.0142 -0.0521 425 LEU A C   
2789  O  O   . LEU A 424 ? 0.5367 0.5464 1.0994 -0.0922 -0.0155 -0.0581 425 LEU A O   
2790  C  CB  . LEU A 424 ? 0.5962 0.6034 1.1698 -0.1092 -0.0216 -0.0527 425 LEU A CB  
2791  C  CG  . LEU A 424 ? 0.6500 0.6462 1.2231 -0.1177 -0.0252 -0.0578 425 LEU A CG  
2792  C  CD1 . LEU A 424 ? 0.6707 0.6781 1.2487 -0.1264 -0.0303 -0.0546 425 LEU A CD1 
2793  C  CD2 . LEU A 424 ? 0.6619 0.6481 1.2266 -0.1198 -0.0268 -0.0707 425 LEU A CD2 
2794  N  N   . PRO A 425 ? 0.5132 0.5328 1.0871 -0.0899 -0.0107 -0.0434 426 PRO A N   
2795  C  CA  . PRO A 425 ? 0.4805 0.5130 1.0559 -0.0839 -0.0095 -0.0412 426 PRO A CA  
2796  C  C   . PRO A 425 ? 0.5069 0.5344 1.0758 -0.0771 -0.0074 -0.0451 426 PRO A C   
2797  O  O   . PRO A 425 ? 0.4609 0.4763 1.0257 -0.0741 -0.0038 -0.0476 426 PRO A O   
2798  C  CB  . PRO A 425 ? 0.4803 0.5204 1.0603 -0.0815 -0.0037 -0.0335 426 PRO A CB  
2799  C  CG  . PRO A 425 ? 0.4566 0.4940 1.0393 -0.0896 -0.0046 -0.0305 426 PRO A CG  
2800  C  CD  . PRO A 425 ? 0.4751 0.4950 1.0533 -0.0921 -0.0077 -0.0358 426 PRO A CD  
2801  N  N   . GLU A 426 ? 0.5372 0.5742 1.1064 -0.0749 -0.0103 -0.0453 427 GLU A N   
2802  C  CA  . GLU A 426 ? 0.5450 0.5792 1.1080 -0.0695 -0.0088 -0.0482 427 GLU A CA  
2803  C  C   . GLU A 426 ? 0.3954 0.4299 0.9593 -0.0608 -0.0013 -0.0442 427 GLU A C   
2804  O  O   . GLU A 426 ? 0.2782 0.3204 0.8477 -0.0588 0.0017  -0.0387 427 GLU A O   
2805  C  CB  . GLU A 426 ? 0.6377 0.6824 1.2016 -0.0706 -0.0156 -0.0473 427 GLU A CB  
2806  C  CG  . GLU A 426 ? 0.7240 0.7648 1.2791 -0.0789 -0.0222 -0.0537 427 GLU A CG  
2807  C  CD  . GLU A 426 ? 0.7604 0.7903 1.3047 -0.0777 -0.0175 -0.0611 427 GLU A CD  
2808  O  OE1 . GLU A 426 ? 0.7637 0.7913 1.3086 -0.0691 -0.0108 -0.0595 427 GLU A OE1 
2809  O  OE2 . GLU A 426 ? 0.7901 0.8145 1.3251 -0.0859 -0.0201 -0.0694 427 GLU A OE2 
2810  N  N   . VAL A 427 ? 0.2934 0.3201 0.8511 -0.0564 0.0019  -0.0478 428 VAL A N   
2811  C  CA  . VAL A 427 ? 0.3793 0.4066 0.9368 -0.0485 0.0082  -0.0443 428 VAL A CA  
2812  C  C   . VAL A 427 ? 0.3894 0.4286 0.9494 -0.0442 0.0075  -0.0411 428 VAL A C   
2813  O  O   . VAL A 427 ? 0.3977 0.4403 0.9566 -0.0453 0.0023  -0.0428 428 VAL A O   
2814  C  CB  . VAL A 427 ? 0.3637 0.3804 0.9152 -0.0449 0.0115  -0.0495 428 VAL A CB  
2815  C  CG1 . VAL A 427 ? 0.3122 0.3298 0.8637 -0.0375 0.0174  -0.0452 428 VAL A CG1 
2816  C  CG2 . VAL A 427 ? 0.3676 0.3715 0.9184 -0.0482 0.0116  -0.0541 428 VAL A CG2 
2817  N  N   . MET A 428 ? 0.3677 0.4129 0.9306 -0.0403 0.0123  -0.0366 429 MET A N   
2818  C  CA  . MET A 428 ? 0.4198 0.4747 0.9856 -0.0354 0.0124  -0.0348 429 MET A CA  
2819  C  C   . MET A 428 ? 0.4599 0.5111 1.0199 -0.0295 0.0136  -0.0362 429 MET A C   
2820  O  O   . MET A 428 ? 0.3609 0.4035 0.9149 -0.0283 0.0166  -0.0383 429 MET A O   
2821  C  CB  . MET A 428 ? 0.4589 0.5207 1.0267 -0.0342 0.0188  -0.0320 429 MET A CB  
2822  C  CG  . MET A 428 ? 0.5579 0.6259 1.1318 -0.0410 0.0185  -0.0303 429 MET A CG  
2823  S  SD  . MET A 428 ? 0.4322 0.5138 1.0184 -0.0421 0.0131  -0.0309 429 MET A SD  
2824  C  CE  . MET A 428 ? 0.5896 0.6660 1.1769 -0.0471 0.0024  -0.0319 429 MET A CE  
2825  N  N   . GLY A 429 ? 0.4443 0.5018 1.0072 -0.0259 0.0107  -0.0350 430 GLY A N   
2826  C  CA  . GLY A 429 ? 0.1958 0.2503 0.7532 -0.0204 0.0120  -0.0353 430 GLY A CA  
2827  C  C   . GLY A 429 ? 0.3303 0.3828 0.8817 -0.0158 0.0206  -0.0349 430 GLY A C   
2828  O  O   . GLY A 429 ? 0.1927 0.2478 0.7451 -0.0176 0.0251  -0.0340 430 GLY A O   
2829  N  N   . ASP A 430 ? 0.3380 0.3865 0.8823 -0.0112 0.0225  -0.0353 431 ASP A N   
2830  C  CA  . ASP A 430 ? 0.3406 0.3868 0.8764 -0.0081 0.0299  -0.0352 431 ASP A CA  
2831  C  C   . ASP A 430 ? 0.2671 0.3190 0.8037 -0.0058 0.0311  -0.0356 431 ASP A C   
2832  O  O   . ASP A 430 ? 0.3250 0.3788 0.8673 -0.0043 0.0257  -0.0353 431 ASP A O   
2833  C  CB  . ASP A 430 ? 0.3821 0.4201 0.9083 -0.0054 0.0316  -0.0361 431 ASP A CB  
2834  C  CG  . ASP A 430 ? 0.4891 0.5220 1.0175 -0.0076 0.0305  -0.0383 431 ASP A CG  
2835  O  OD1 . ASP A 430 ? 0.5204 0.5505 1.0514 -0.0096 0.0329  -0.0380 431 ASP A OD1 
2836  O  OD2 . ASP A 430 ? 0.4983 0.5307 1.0269 -0.0081 0.0270  -0.0406 431 ASP A OD2 
2837  N  N   . GLY A 431 ? 0.2490 0.3045 0.7816 -0.0063 0.0380  -0.0363 432 GLY A N   
2838  C  CA  . GLY A 431 ? 0.2488 0.3106 0.7825 -0.0047 0.0409  -0.0390 432 GLY A CA  
2839  C  C   . GLY A 431 ? 0.2264 0.2999 0.7701 -0.0078 0.0436  -0.0410 432 GLY A C   
2840  O  O   . GLY A 431 ? 0.1910 0.2676 0.7424 -0.0111 0.0407  -0.0394 432 GLY A O   
2841  N  N   . LEU A 432 ? 0.2551 0.3362 0.7990 -0.0076 0.0494  -0.0454 433 LEU A N   
2842  C  CA  . LEU A 432 ? 0.3190 0.4140 0.8721 -0.0114 0.0540  -0.0489 433 LEU A CA  
2843  C  C   . LEU A 432 ? 0.2417 0.3406 0.8108 -0.0112 0.0478  -0.0494 433 LEU A C   
2844  O  O   . LEU A 432 ? 0.3148 0.4211 0.8903 -0.0159 0.0483  -0.0485 433 LEU A O   
2845  C  CB  . LEU A 432 ? 0.3138 0.4167 0.8664 -0.0107 0.0611  -0.0557 433 LEU A CB  
2846  C  CG  . LEU A 432 ? 0.2640 0.3842 0.8243 -0.0162 0.0686  -0.0611 433 LEU A CG  
2847  C  CD1 . LEU A 432 ? 0.3116 0.4381 0.8634 -0.0239 0.0737  -0.0568 433 LEU A CD1 
2848  C  CD2 . LEU A 432 ? 0.2680 0.3956 0.8296 -0.0151 0.0752  -0.0699 433 LEU A CD2 
2849  N  N   . ALA A 433 ? 0.1988 0.2930 0.7750 -0.0065 0.0413  -0.0500 434 ALA A N   
2850  C  CA  . ALA A 433 ? 0.3406 0.4389 0.9345 -0.0061 0.0339  -0.0497 434 ALA A CA  
2851  C  C   . ALA A 433 ? 0.3146 0.4117 0.9104 -0.0095 0.0278  -0.0444 434 ALA A C   
2852  O  O   . ALA A 433 ? 0.2073 0.3125 0.8158 -0.0121 0.0251  -0.0446 434 ALA A O   
2853  C  CB  . ALA A 433 ? 0.2037 0.2951 0.8044 -0.0012 0.0261  -0.0486 434 ALA A CB  
2854  N  N   . ASN A 434 ? 0.1986 0.2862 0.7824 -0.0098 0.0258  -0.0405 435 ASN A N   
2855  C  CA  . ASN A 434 ? 0.1996 0.2853 0.7848 -0.0137 0.0201  -0.0369 435 ASN A CA  
2856  C  C   . ASN A 434 ? 0.2023 0.2932 0.7871 -0.0196 0.0250  -0.0369 435 ASN A C   
2857  O  O   . ASN A 434 ? 0.2049 0.2943 0.7915 -0.0239 0.0205  -0.0347 435 ASN A O   
2858  C  CB  . ASN A 434 ? 0.3301 0.4049 0.9042 -0.0127 0.0177  -0.0347 435 ASN A CB  
2859  C  CG  . ASN A 434 ? 0.3472 0.4191 0.9248 -0.0101 0.0090  -0.0326 435 ASN A CG  
2860  O  OD1 . ASN A 434 ? 0.2134 0.2904 0.8034 -0.0110 0.0008  -0.0306 435 ASN A OD1 
2861  N  ND2 . ASN A 434 ? 0.3332 0.3976 0.9004 -0.0075 0.0102  -0.0324 435 ASN A ND2 
2862  N  N   . GLN A 435 ? 0.3410 0.4388 0.9233 -0.0210 0.0339  -0.0393 436 GLN A N   
2863  C  CA  . GLN A 435 ? 0.2071 0.3107 0.7883 -0.0282 0.0386  -0.0379 436 GLN A CA  
2864  C  C   . GLN A 435 ? 0.2130 0.3314 0.8068 -0.0323 0.0403  -0.0406 436 GLN A C   
2865  O  O   . GLN A 435 ? 0.2177 0.3438 0.8108 -0.0396 0.0451  -0.0396 436 GLN A O   
2866  C  CB  . GLN A 435 ? 0.2059 0.3098 0.7753 -0.0299 0.0471  -0.0375 436 GLN A CB  
2867  C  CG  . GLN A 435 ? 0.2003 0.2908 0.7586 -0.0255 0.0461  -0.0354 436 GLN A CG  
2868  C  CD  . GLN A 435 ? 0.3004 0.3797 0.8587 -0.0260 0.0396  -0.0323 436 GLN A CD  
2869  O  OE1 . GLN A 435 ? 0.2052 0.2845 0.7666 -0.0318 0.0381  -0.0298 436 GLN A OE1 
2870  N  NE2 . GLN A 435 ? 0.1956 0.2658 0.7502 -0.0208 0.0357  -0.0330 436 GLN A NE2 
2871  N  N   . ILE A 436 ? 0.2139 0.3365 0.8203 -0.0281 0.0360  -0.0436 437 ILE A N   
2872  C  CA  . ILE A 436 ? 0.2346 0.3718 0.8561 -0.0311 0.0375  -0.0472 437 ILE A CA  
2873  C  C   . ILE A 436 ? 0.2247 0.3652 0.8508 -0.0382 0.0334  -0.0436 437 ILE A C   
2874  O  O   . ILE A 436 ? 0.2303 0.3837 0.8625 -0.0445 0.0382  -0.0454 437 ILE A O   
2875  C  CB  . ILE A 436 ? 0.2215 0.3602 0.8588 -0.0247 0.0313  -0.0502 437 ILE A CB  
2876  C  CG1 . ILE A 436 ? 0.2287 0.3833 0.8848 -0.0273 0.0332  -0.0549 437 ILE A CG1 
2877  C  CG2 . ILE A 436 ? 0.2302 0.3589 0.8701 -0.0222 0.0186  -0.0444 437 ILE A CG2 
2878  C  CD1 . ILE A 436 ? 0.2321 0.3877 0.9078 -0.0212 0.0260  -0.0573 437 ILE A CD1 
2879  N  N   . ASN A 437 ? 0.2627 0.3924 0.8856 -0.0382 0.0248  -0.0390 438 ASN A N   
2880  C  CA  . ASN A 437 ? 0.3257 0.4561 0.9516 -0.0454 0.0198  -0.0360 438 ASN A CA  
2881  C  C   . ASN A 437 ? 0.3438 0.4657 0.9568 -0.0513 0.0226  -0.0326 438 ASN A C   
2882  O  O   . ASN A 437 ? 0.3950 0.5144 1.0091 -0.0575 0.0179  -0.0305 438 ASN A O   
2883  C  CB  . ASN A 437 ? 0.3599 0.4853 0.9915 -0.0439 0.0077  -0.0338 438 ASN A CB  
2884  C  CG  . ASN A 437 ? 0.3693 0.5047 1.0189 -0.0410 0.0022  -0.0351 438 ASN A CG  
2885  O  OD1 . ASN A 437 ? 0.3026 0.4500 0.9626 -0.0418 0.0076  -0.0386 438 ASN A OD1 
2886  N  ND2 . ASN A 437 ? 0.4181 0.5493 1.0723 -0.0385 -0.0089 -0.0322 438 ASN A ND2 
2887  N  N   . ASN A 438 ? 0.2966 0.4131 0.8980 -0.0496 0.0292  -0.0321 439 ASN A N   
2888  C  CA  . ASN A 438 ? 0.3425 0.4487 0.9335 -0.0542 0.0304  -0.0280 439 ASN A CA  
2889  C  C   . ASN A 438 ? 0.3289 0.4408 0.9222 -0.0647 0.0319  -0.0251 439 ASN A C   
2890  O  O   . ASN A 438 ? 0.3060 0.4310 0.9006 -0.0695 0.0386  -0.0253 439 ASN A O   
2891  C  CB  . ASN A 438 ? 0.2247 0.3276 0.8052 -0.0515 0.0373  -0.0272 439 ASN A CB  
2892  C  CG  . ASN A 438 ? 0.2899 0.3791 0.8619 -0.0541 0.0365  -0.0226 439 ASN A CG  
2893  O  OD1 . ASN A 438 ? 0.3618 0.4476 0.9344 -0.0616 0.0344  -0.0189 439 ASN A OD1 
2894  N  ND2 . ASN A 438 ? 0.2209 0.3015 0.7858 -0.0481 0.0377  -0.0226 439 ASN A ND2 
2895  N  N   . PRO A 439 ? 0.2454 0.3478 0.8385 -0.0692 0.0257  -0.0228 440 PRO A N   
2896  C  CA  . PRO A 439 ? 0.4557 0.5612 1.0512 -0.0798 0.0252  -0.0196 440 PRO A CA  
2897  C  C   . PRO A 439 ? 0.4532 0.5567 1.0404 -0.0867 0.0306  -0.0139 440 PRO A C   
2898  O  O   . PRO A 439 ? 0.2717 0.3851 0.8605 -0.0964 0.0335  -0.0111 440 PRO A O   
2899  C  CB  . PRO A 439 ? 0.2623 0.3540 0.8575 -0.0813 0.0167  -0.0199 440 PRO A CB  
2900  C  CG  . PRO A 439 ? 0.2552 0.3341 0.8438 -0.0734 0.0153  -0.0219 440 PRO A CG  
2901  C  CD  . PRO A 439 ? 0.2438 0.3316 0.8337 -0.0654 0.0189  -0.0241 440 PRO A CD  
2902  N  N   . GLU A 440 ? 0.2599 0.3509 0.8386 -0.0828 0.0313  -0.0116 441 GLU A N   
2903  C  CA  . GLU A 440 ? 0.3268 0.4138 0.8978 -0.0897 0.0342  -0.0043 441 GLU A CA  
2904  C  C   . GLU A 440 ? 0.2677 0.3703 0.8343 -0.0922 0.0428  -0.0036 441 GLU A C   
2905  O  O   . GLU A 440 ? 0.3789 0.4886 0.9411 -0.1035 0.0461  0.0021  441 GLU A O   
2906  C  CB  . GLU A 440 ? 0.2667 0.3342 0.8325 -0.0844 0.0306  -0.0021 441 GLU A CB  
2907  C  CG  . GLU A 440 ? 0.2698 0.3229 0.8393 -0.0816 0.0233  -0.0058 441 GLU A CG  
2908  C  CD  . GLU A 440 ? 0.2828 0.3355 0.8566 -0.0908 0.0192  -0.0042 441 GLU A CD  
2909  O  OE1 . GLU A 440 ? 0.2934 0.3488 0.8655 -0.1003 0.0204  0.0028  441 GLU A OE1 
2910  O  OE2 . GLU A 440 ? 0.2837 0.3339 0.8617 -0.0897 0.0145  -0.0096 441 GLU A OE2 
2911  N  N   . VAL A 441 ? 0.3287 0.4364 0.8955 -0.0828 0.0462  -0.0096 442 VAL A N   
2912  C  CA  . VAL A 441 ? 0.3874 0.5096 0.9496 -0.0844 0.0547  -0.0112 442 VAL A CA  
2913  C  C   . VAL A 441 ? 0.4124 0.5500 0.9837 -0.0799 0.0582  -0.0200 442 VAL A C   
2914  O  O   . VAL A 441 ? 0.4247 0.5571 1.0022 -0.0701 0.0538  -0.0246 442 VAL A O   
2915  C  CB  . VAL A 441 ? 0.3612 0.4749 0.9151 -0.0773 0.0562  -0.0107 442 VAL A CB  
2916  C  CG1 . VAL A 441 ? 0.3723 0.5012 0.9192 -0.0825 0.0649  -0.0112 442 VAL A CG1 
2917  C  CG2 . VAL A 441 ? 0.3608 0.4559 0.9101 -0.0783 0.0505  -0.0030 442 VAL A CG2 
2918  N  N   . GLU A 442 ? 0.4347 0.5914 1.0071 -0.0875 0.0658  -0.0225 443 GLU A N   
2919  C  CA  . GLU A 442 ? 0.4879 0.6588 1.0714 -0.0826 0.0692  -0.0319 443 GLU A CA  
2920  C  C   . GLU A 442 ? 0.4552 0.6316 1.0334 -0.0778 0.0762  -0.0374 443 GLU A C   
2921  O  O   . GLU A 442 ? 0.4595 0.6478 1.0298 -0.0863 0.0841  -0.0372 443 GLU A O   
2922  C  CB  . GLU A 442 ? 0.6171 0.8072 1.2084 -0.0933 0.0736  -0.0337 443 GLU A CB  
2923  C  CG  . GLU A 442 ? 0.7000 0.8922 1.3077 -0.0893 0.0676  -0.0372 443 GLU A CG  
2924  C  CD  . GLU A 442 ? 0.8147 1.0269 1.4317 -0.0998 0.0721  -0.0393 443 GLU A CD  
2925  O  OE1 . GLU A 442 ? 0.8481 1.0581 1.4671 -0.1071 0.0674  -0.0342 443 GLU A OE1 
2926  O  OE2 . GLU A 442 ? 0.8609 1.0910 1.4837 -0.1010 0.0805  -0.0468 443 GLU A OE2 
2927  N  N   . VAL A 443 ? 0.4280 0.5957 1.0100 -0.0652 0.0726  -0.0419 444 VAL A N   
2928  C  CA  . VAL A 443 ? 0.3910 0.5590 0.9672 -0.0594 0.0775  -0.0468 444 VAL A CA  
2929  C  C   . VAL A 443 ? 0.3627 0.5388 0.9522 -0.0529 0.0790  -0.0567 444 VAL A C   
2930  O  O   . VAL A 443 ? 0.3951 0.5652 0.9960 -0.0463 0.0715  -0.0575 444 VAL A O   
2931  C  CB  . VAL A 443 ? 0.2998 0.4479 0.8676 -0.0507 0.0716  -0.0431 444 VAL A CB  
2932  C  CG1 . VAL A 443 ? 0.2187 0.3672 0.7794 -0.0457 0.0766  -0.0478 444 VAL A CG1 
2933  C  CG2 . VAL A 443 ? 0.3047 0.4426 0.8633 -0.0561 0.0690  -0.0338 444 VAL A CG2 
2934  N  N   . ASP A 444 ? 0.4079 0.5977 0.9968 -0.0553 0.0882  -0.0640 445 ASP A N   
2935  C  CA  . ASP A 444 ? 0.4414 0.6373 1.0447 -0.0488 0.0898  -0.0744 445 ASP A CA  
2936  C  C   . ASP A 444 ? 0.3247 0.5054 0.9236 -0.0385 0.0861  -0.0757 445 ASP A C   
2937  O  O   . ASP A 444 ? 0.2314 0.4103 0.8167 -0.0391 0.0908  -0.0761 445 ASP A O   
2938  C  CB  . ASP A 444 ? 0.5829 0.8004 1.1889 -0.0565 0.1018  -0.0834 445 ASP A CB  
2939  C  CG  . ASP A 444 ? 0.6873 0.9094 1.3100 -0.0494 0.1040  -0.0957 445 ASP A CG  
2940  O  OD1 . ASP A 444 ? 0.7262 0.9423 1.3656 -0.0423 0.0962  -0.0966 445 ASP A OD1 
2941  O  OD2 . ASP A 444 ? 0.7476 0.9792 1.3677 -0.0515 0.1131  -0.1044 445 ASP A OD2 
2942  N  N   . ILE A 445 ? 0.3376 0.5078 0.9478 -0.0302 0.0772  -0.0758 446 ILE A N   
2943  C  CA  . ILE A 445 ? 0.3921 0.5462 0.9974 -0.0218 0.0717  -0.0746 446 ILE A CA  
2944  C  C   . ILE A 445 ? 0.2253 0.3831 0.8381 -0.0180 0.0760  -0.0844 446 ILE A C   
2945  O  O   . ILE A 445 ? 0.2539 0.3999 0.8611 -0.0127 0.0731  -0.0843 446 ILE A O   
2946  C  CB  . ILE A 445 ? 0.3809 0.5227 0.9943 -0.0166 0.0592  -0.0688 446 ILE A CB  
2947  C  CG1 . ILE A 445 ? 0.2246 0.3738 0.8614 -0.0146 0.0555  -0.0735 446 ILE A CG1 
2948  C  CG2 . ILE A 445 ? 0.2156 0.3537 0.8229 -0.0208 0.0552  -0.0607 446 ILE A CG2 
2949  C  CD1 . ILE A 445 ? 0.2234 0.3636 0.8696 -0.0114 0.0424  -0.0667 446 ILE A CD1 
2950  N  N   . THR A 446 ? 0.3995 0.5737 1.0257 -0.0214 0.0829  -0.0935 447 THR A N   
2951  C  CA  . THR A 446 ? 0.4423 0.6209 1.0794 -0.0184 0.0876  -0.1049 447 THR A CA  
2952  C  C   . THR A 446 ? 0.4477 0.6345 1.0700 -0.0233 0.0990  -0.1106 447 THR A C   
2953  O  O   . THR A 446 ? 0.5292 0.7206 1.1585 -0.0221 0.1044  -0.1215 447 THR A O   
2954  C  CB  . THR A 446 ? 0.2497 0.4431 0.9116 -0.0197 0.0903  -0.1140 447 THR A CB  
2955  O  OG1 . THR A 446 ? 0.2560 0.4693 0.9141 -0.0292 0.1020  -0.1191 447 THR A OG1 
2956  C  CG2 . THR A 446 ? 0.3574 0.5466 1.0328 -0.0173 0.0795  -0.1069 447 THR A CG2 
2957  N  N   . LYS A 447 ? 0.4862 0.6749 1.0891 -0.0294 0.1021  -0.1033 448 LYS A N   
2958  C  CA  . LYS A 447 ? 0.4714 0.6692 1.0591 -0.0357 0.1120  -0.1066 448 LYS A CA  
2959  C  C   . LYS A 447 ? 0.4822 0.6657 1.0503 -0.0338 0.1083  -0.0974 448 LYS A C   
2960  O  O   . LYS A 447 ? 0.5382 0.7241 1.0934 -0.0405 0.1096  -0.0892 448 LYS A O   
2961  C  CB  . LYS A 447 ? 0.4387 0.6566 1.0224 -0.0485 0.1205  -0.1062 448 LYS A CB  
2962  N  N   . PRO A 448 ? 0.4017 0.5704 0.9686 -0.0253 0.1034  -0.0985 449 PRO A N   
2963  C  CA  . PRO A 448 ? 0.3650 0.5209 0.9144 -0.0232 0.1004  -0.0908 449 PRO A CA  
2964  C  C   . PRO A 448 ? 0.3811 0.5477 0.9175 -0.0297 0.1097  -0.0939 449 PRO A C   
2965  O  O   . PRO A 448 ? 0.4179 0.5989 0.9588 -0.0339 0.1182  -0.1046 449 PRO A O   
2966  C  CB  . PRO A 448 ? 0.2962 0.4362 0.8503 -0.0140 0.0931  -0.0922 449 PRO A CB  
2967  C  CG  . PRO A 448 ? 0.3978 0.5457 0.9700 -0.0129 0.0960  -0.1037 449 PRO A CG  
2968  C  CD  . PRO A 448 ? 0.4066 0.5695 0.9898 -0.0180 0.0997  -0.1060 449 PRO A CD  
2969  N  N   . ASP A 449 ? 0.3806 0.5406 0.9018 -0.0312 0.1081  -0.0849 450 ASP A N   
2970  C  CA  . ASP A 449 ? 0.4449 0.6147 0.9535 -0.0381 0.1154  -0.0859 450 ASP A CA  
2971  C  C   . ASP A 449 ? 0.3905 0.5544 0.8968 -0.0322 0.1163  -0.0933 450 ASP A C   
2972  O  O   . ASP A 449 ? 0.4128 0.5593 0.9197 -0.0232 0.1087  -0.0909 450 ASP A O   
2973  C  CB  . ASP A 449 ? 0.4731 0.6369 0.9697 -0.0416 0.1119  -0.0729 450 ASP A CB  
2974  C  CG  . ASP A 449 ? 0.5703 0.7460 1.0546 -0.0512 0.1185  -0.0716 450 ASP A CG  
2975  O  OD1 . ASP A 449 ? 0.6386 0.8056 1.1154 -0.0471 0.1164  -0.0694 450 ASP A OD1 
2976  O  OD2 . ASP A 449 ? 0.6243 0.8186 1.1059 -0.0639 0.1256  -0.0724 450 ASP A OD2 
2977  N  N   . MET A 450 ? 0.3991 0.5781 0.9024 -0.0388 0.1257  -0.1024 451 MET A N   
2978  C  CA  . MET A 450 ? 0.4448 0.6196 0.9479 -0.0344 0.1275  -0.1115 451 MET A CA  
2979  C  C   . MET A 450 ? 0.3764 0.5399 0.8656 -0.0316 0.1236  -0.1040 451 MET A C   
2980  O  O   . MET A 450 ? 0.3644 0.5142 0.8547 -0.0238 0.1189  -0.1060 451 MET A O   
2981  C  CB  . MET A 450 ? 0.5066 0.7018 1.0102 -0.0436 0.1396  -0.1246 451 MET A CB  
2982  C  CG  . MET A 450 ? 0.6032 0.8034 1.1262 -0.0414 0.1429  -0.1387 451 MET A CG  
2983  S  SD  . MET A 450 ? 1.1115 1.2913 1.6491 -0.0285 0.1347  -0.1443 451 MET A SD  
2984  C  CE  . MET A 450 ? 0.3976 0.5644 0.9480 -0.0210 0.1231  -0.1347 451 MET A CE  
2985  N  N   . THR A 451 ? 0.3360 0.5058 0.8134 -0.0389 0.1252  -0.0950 452 THR A N   
2986  C  CA  . THR A 451 ? 0.3633 0.5241 0.8296 -0.0370 0.1216  -0.0873 452 THR A CA  
2987  C  C   . THR A 451 ? 0.2780 0.4160 0.7460 -0.0252 0.1111  -0.0811 452 THR A C   
2988  O  O   . THR A 451 ? 0.2612 0.3885 0.7250 -0.0195 0.1080  -0.0819 452 THR A O   
2989  C  CB  . THR A 451 ? 0.3735 0.5428 0.8312 -0.0474 0.1224  -0.0758 452 THR A CB  
2990  O  OG1 . THR A 451 ? 0.3796 0.5714 0.8333 -0.0616 0.1318  -0.0801 452 THR A OG1 
2991  C  CG2 . THR A 451 ? 0.3341 0.4963 0.7829 -0.0461 0.1193  -0.0691 452 THR A CG2 
2992  N  N   . ILE A 452 ? 0.2623 0.3939 0.7360 -0.0231 0.1059  -0.0752 453 ILE A N   
2993  C  CA  . ILE A 452 ? 0.2961 0.4082 0.7709 -0.0144 0.0964  -0.0697 453 ILE A CA  
2994  C  C   . ILE A 452 ? 0.2704 0.3739 0.7498 -0.0082 0.0933  -0.0761 453 ILE A C   
2995  O  O   . ILE A 452 ? 0.1895 0.2797 0.6634 -0.0035 0.0876  -0.0726 453 ILE A O   
2996  C  CB  . ILE A 452 ? 0.3303 0.4399 0.8129 -0.0145 0.0923  -0.0649 453 ILE A CB  
2997  C  CG1 . ILE A 452 ? 0.3268 0.4437 0.8068 -0.0218 0.0943  -0.0572 453 ILE A CG1 
2998  C  CG2 . ILE A 452 ? 0.2620 0.3536 0.7450 -0.0074 0.0830  -0.0601 453 ILE A CG2 
2999  C  CD1 . ILE A 452 ? 0.3696 0.4773 0.8417 -0.0209 0.0910  -0.0488 453 ILE A CD1 
3000  N  N   . ARG A 453 ? 0.2822 0.3942 0.7728 -0.0091 0.0968  -0.0853 454 ARG A N   
3001  C  CA  . ARG A 453 ? 0.3734 0.4782 0.8732 -0.0044 0.0934  -0.0913 454 ARG A CA  
3002  C  C   . ARG A 453 ? 0.3857 0.4870 0.8780 -0.0034 0.0949  -0.0947 454 ARG A C   
3003  O  O   . ARG A 453 ? 0.4591 0.5478 0.9517 0.0008  0.0883  -0.0923 454 ARG A O   
3004  C  CB  . ARG A 453 ? 0.4385 0.5550 0.9550 -0.0062 0.0981  -0.1020 454 ARG A CB  
3005  C  CG  . ARG A 453 ? 0.5494 0.6623 1.0797 -0.0037 0.0918  -0.0992 454 ARG A CG  
3006  C  CD  . ARG A 453 ? 0.6192 0.7156 1.1529 0.0020  0.0811  -0.0934 454 ARG A CD  
3007  N  NE  . ARG A 453 ? 0.6570 0.7488 1.1987 0.0036  0.0736  -0.0868 454 ARG A NE  
3008  C  CZ  . ARG A 453 ? 0.7310 0.8108 1.2753 0.0068  0.0638  -0.0801 454 ARG A CZ  
3009  N  NH1 . ARG A 453 ? 0.7147 0.7860 1.2542 0.0087  0.0606  -0.0786 454 ARG A NH1 
3010  N  NH2 . ARG A 453 ? 0.7301 0.8078 1.2822 0.0074  0.0573  -0.0746 454 ARG A NH2 
3011  N  N   . GLN A 454 ? 0.3343 0.4481 0.8201 -0.0085 0.1035  -0.0999 455 GLN A N   
3012  C  CA  . GLN A 454 ? 0.4412 0.5535 0.9198 -0.0084 0.1057  -0.1035 455 GLN A CA  
3013  C  C   . GLN A 454 ? 0.3669 0.4654 0.8332 -0.0047 0.0989  -0.0927 455 GLN A C   
3014  O  O   . GLN A 454 ? 0.4177 0.5068 0.8820 -0.0015 0.0952  -0.0931 455 GLN A O   
3015  C  CB  . GLN A 454 ? 0.4666 0.5974 0.9392 -0.0166 0.1163  -0.1099 455 GLN A CB  
3016  C  CG  . GLN A 454 ? 0.5531 0.6987 1.0372 -0.0213 0.1247  -0.1238 455 GLN A CG  
3017  C  CD  . GLN A 454 ? 0.6815 0.8481 1.1570 -0.0325 0.1358  -0.1295 455 GLN A CD  
3018  O  OE1 . GLN A 454 ? 0.7219 0.8929 1.1839 -0.0374 0.1365  -0.1211 455 GLN A OE1 
3019  N  NE2 . GLN A 454 ? 0.7192 0.8996 1.2033 -0.0378 0.1444  -0.1438 455 GLN A NE2 
3020  N  N   . GLN A 455 ? 0.2834 0.3812 0.7429 -0.0058 0.0971  -0.0832 456 GLN A N   
3021  C  CA  . GLN A 455 ? 0.3072 0.3924 0.7571 -0.0025 0.0910  -0.0738 456 GLN A CA  
3022  C  C   . GLN A 455 ? 0.3052 0.3754 0.7570 0.0026  0.0826  -0.0706 456 GLN A C   
3023  O  O   . GLN A 455 ? 0.3095 0.3708 0.7543 0.0048  0.0788  -0.0674 456 GLN A O   
3024  C  CB  . GLN A 455 ? 0.1828 0.2695 0.6300 -0.0047 0.0904  -0.0651 456 GLN A CB  
3025  C  CG  . GLN A 455 ? 0.2502 0.3536 0.6954 -0.0123 0.0976  -0.0650 456 GLN A CG  
3026  C  CD  . GLN A 455 ? 0.3773 0.4873 0.8166 -0.0145 0.1022  -0.0701 456 GLN A CD  
3027  O  OE1 . GLN A 455 ? 0.4284 0.5306 0.8618 -0.0115 0.0989  -0.0662 456 GLN A OE1 
3028  N  NE2 . GLN A 455 ? 0.4384 0.5637 0.8798 -0.0205 0.1101  -0.0797 456 GLN A NE2 
3029  N  N   . ILE A 456 ? 0.3321 0.4016 0.7943 0.0034  0.0799  -0.0713 457 ILE A N   
3030  C  CA  . ILE A 456 ? 0.3214 0.3803 0.7883 0.0064  0.0718  -0.0681 457 ILE A CA  
3031  C  C   . ILE A 456 ? 0.3581 0.4143 0.8290 0.0077  0.0707  -0.0728 457 ILE A C   
3032  O  O   . ILE A 456 ? 0.3883 0.4361 0.8568 0.0093  0.0648  -0.0681 457 ILE A O   
3033  C  CB  . ILE A 456 ? 0.2961 0.3572 0.7769 0.0066  0.0693  -0.0687 457 ILE A CB  
3034  C  CG1 . ILE A 456 ? 0.3633 0.4244 0.8407 0.0054  0.0686  -0.0626 457 ILE A CG1 
3035  C  CG2 . ILE A 456 ? 0.2340 0.2872 0.7236 0.0089  0.0610  -0.0660 457 ILE A CG2 
3036  C  CD1 . ILE A 456 ? 0.3640 0.4282 0.8549 0.0051  0.0662  -0.0629 457 ILE A CD1 
3037  N  N   . MET A 457 ? 0.2885 0.3532 0.7666 0.0064  0.0768  -0.0824 458 MET A N   
3038  C  CA  . MET A 457 ? 0.3602 0.4226 0.8442 0.0071  0.0764  -0.0880 458 MET A CA  
3039  C  C   . MET A 457 ? 0.3319 0.3894 0.8014 0.0073  0.0761  -0.0845 458 MET A C   
3040  O  O   . MET A 457 ? 0.2871 0.3373 0.7584 0.0088  0.0711  -0.0824 458 MET A O   
3041  C  CB  . MET A 457 ? 0.3875 0.4612 0.8819 0.0048  0.0845  -0.1011 458 MET A CB  
3042  C  CG  . MET A 457 ? 0.4232 0.5016 0.9368 0.0050  0.0844  -0.1067 458 MET A CG  
3043  S  SD  . MET A 457 ? 0.7030 0.7700 1.2321 0.0088  0.0722  -0.0996 458 MET A SD  
3044  C  CE  . MET A 457 ? 0.6205 0.6793 1.1534 0.0100  0.0680  -0.1001 458 MET A CE  
3045  N  N   . GLN A 458 ? 0.2800 0.3427 0.7371 0.0056  0.0812  -0.0836 459 GLN A N   
3046  C  CA  . GLN A 458 ? 0.3054 0.3643 0.7498 0.0058  0.0808  -0.0799 459 GLN A CA  
3047  C  C   . GLN A 458 ? 0.2354 0.2827 0.6737 0.0082  0.0730  -0.0703 459 GLN A C   
3048  O  O   . GLN A 458 ? 0.1772 0.2194 0.6122 0.0090  0.0704  -0.0690 459 GLN A O   
3049  C  CB  . GLN A 458 ? 0.2631 0.3302 0.6985 0.0033  0.0863  -0.0783 459 GLN A CB  
3050  C  CG  . GLN A 458 ? 0.3302 0.4127 0.7694 -0.0012 0.0954  -0.0881 459 GLN A CG  
3051  C  CD  . GLN A 458 ? 0.4416 0.5258 0.8824 -0.0019 0.0984  -0.0969 459 GLN A CD  
3052  O  OE1 . GLN A 458 ? 0.4726 0.5555 0.9054 -0.0020 0.0984  -0.0950 459 GLN A OE1 
3053  N  NE2 . GLN A 458 ? 0.3562 0.4433 0.8094 -0.0025 0.1009  -0.1072 459 GLN A NE2 
3054  N  N   . LEU A 459 ? 0.2738 0.3184 0.7116 0.0087  0.0698  -0.0644 460 LEU A N   
3055  C  CA  . LEU A 459 ? 0.2456 0.2818 0.6792 0.0099  0.0634  -0.0570 460 LEU A CA  
3056  C  C   . LEU A 459 ? 0.3016 0.3337 0.7439 0.0108  0.0582  -0.0570 460 LEU A C   
3057  O  O   . LEU A 459 ? 0.3617 0.3892 0.7994 0.0113  0.0551  -0.0532 460 LEU A O   
3058  C  CB  . LEU A 459 ? 0.3151 0.3502 0.7504 0.0097  0.0613  -0.0527 460 LEU A CB  
3059  C  CG  . LEU A 459 ? 0.3234 0.3614 0.7535 0.0087  0.0649  -0.0507 460 LEU A CG  
3060  C  CD1 . LEU A 459 ? 0.3761 0.4124 0.8112 0.0083  0.0623  -0.0473 460 LEU A CD1 
3061  C  CD2 . LEU A 459 ? 0.3297 0.3642 0.7490 0.0090  0.0649  -0.0470 460 LEU A CD2 
3062  N  N   . LYS A 460 ? 0.2448 0.2794 0.7018 0.0110  0.0574  -0.0611 461 LYS A N   
3063  C  CA  . LYS A 460 ? 0.2176 0.2489 0.6883 0.0119  0.0517  -0.0609 461 LYS A CA  
3064  C  C   . LYS A 460 ? 0.1813 0.2108 0.6503 0.0118  0.0525  -0.0632 461 LYS A C   
3065  O  O   . LYS A 460 ? 0.2940 0.3187 0.7644 0.0122  0.0474  -0.0583 461 LYS A O   
3066  C  CB  . LYS A 460 ? 0.2450 0.2802 0.7348 0.0121  0.0515  -0.0669 461 LYS A CB  
3067  C  CG  . LYS A 460 ? 0.3355 0.3720 0.8319 0.0123  0.0489  -0.0643 461 LYS A CG  
3068  C  CD  . LYS A 460 ? 0.3566 0.3963 0.8757 0.0129  0.0471  -0.0699 461 LYS A CD  
3069  C  CE  . LYS A 460 ? 0.3764 0.4199 0.9023 0.0129  0.0465  -0.0693 461 LYS A CE  
3070  N  NZ  . LYS A 460 ? 0.4223 0.4708 0.9710 0.0134  0.0467  -0.0770 461 LYS A NZ  
3071  N  N   . ILE A 461 ? 0.1840 0.2182 0.6511 0.0110  0.0592  -0.0710 462 ILE A N   
3072  C  CA  . ILE A 461 ? 0.2513 0.2847 0.7184 0.0106  0.0607  -0.0748 462 ILE A CA  
3073  C  C   . ILE A 461 ? 0.3304 0.3595 0.7823 0.0107  0.0593  -0.0682 462 ILE A C   
3074  O  O   . ILE A 461 ? 0.2679 0.2930 0.7235 0.0109  0.0557  -0.0661 462 ILE A O   
3075  C  CB  . ILE A 461 ? 0.2972 0.3383 0.7638 0.0090  0.0692  -0.0853 462 ILE A CB  
3076  C  CG1 . ILE A 461 ? 0.3150 0.3613 0.8000 0.0085  0.0714  -0.0942 462 ILE A CG1 
3077  C  CG2 . ILE A 461 ? 0.2215 0.2619 0.6865 0.0082  0.0710  -0.0893 462 ILE A CG2 
3078  C  CD1 . ILE A 461 ? 0.3031 0.3602 0.7874 0.0060  0.0811  -0.1054 462 ILE A CD1 
3079  N  N   . MET A 462 ? 0.2861 0.3165 0.7231 0.0105  0.0619  -0.0650 463 MET A N   
3080  C  CA  . MET A 462 ? 0.1710 0.1982 0.5951 0.0107  0.0610  -0.0597 463 MET A CA  
3081  C  C   . MET A 462 ? 0.2122 0.2339 0.6381 0.0114  0.0549  -0.0529 463 MET A C   
3082  O  O   . MET A 462 ? 0.2672 0.2862 0.6904 0.0114  0.0534  -0.0506 463 MET A O   
3083  C  CB  . MET A 462 ? 0.3012 0.3307 0.7137 0.0106  0.0640  -0.0573 463 MET A CB  
3084  C  CG  . MET A 462 ? 0.3215 0.3488 0.7230 0.0108  0.0638  -0.0534 463 MET A CG  
3085  S  SD  . MET A 462 ? 0.2983 0.3280 0.6982 0.0103  0.0669  -0.0583 463 MET A SD  
3086  C  CE  . MET A 462 ? 0.1643 0.1876 0.5638 0.0108  0.0623  -0.0541 463 MET A CE  
3087  N  N   . THR A 463 ? 0.1689 0.1900 0.6010 0.0117  0.0516  -0.0502 464 THR A N   
3088  C  CA  . THR A 463 ? 0.1679 0.1855 0.6048 0.0120  0.0459  -0.0443 464 THR A CA  
3089  C  C   . THR A 463 ? 0.2635 0.2789 0.7135 0.0121  0.0416  -0.0436 464 THR A C   
3090  O  O   . THR A 463 ? 0.2526 0.2655 0.7027 0.0120  0.0389  -0.0393 464 THR A O   
3091  C  CB  . THR A 463 ? 0.1688 0.1868 0.6138 0.0122  0.0426  -0.0422 464 THR A CB  
3092  O  OG1 . THR A 463 ? 0.1663 0.1861 0.6015 0.0118  0.0463  -0.0427 464 THR A OG1 
3093  C  CG2 . THR A 463 ? 0.1861 0.2015 0.6374 0.0123  0.0366  -0.0361 464 THR A CG2 
3094  N  N   . ASN A 464 ? 0.2848 0.3014 0.7484 0.0122  0.0410  -0.0482 465 ASN A N   
3095  C  CA  . ASN A 464 ? 0.2459 0.2603 0.7257 0.0121  0.0364  -0.0480 465 ASN A CA  
3096  C  C   . ASN A 464 ? 0.2026 0.2157 0.6747 0.0116  0.0391  -0.0489 465 ASN A C   
3097  O  O   . ASN A 464 ? 0.2117 0.2219 0.6910 0.0114  0.0345  -0.0441 465 ASN A O   
3098  C  CB  . ASN A 464 ? 0.2926 0.3092 0.7892 0.0123  0.0369  -0.0554 465 ASN A CB  
3099  C  CG  . ASN A 464 ? 0.3936 0.4111 0.9032 0.0129  0.0326  -0.0540 465 ASN A CG  
3100  O  OD1 . ASN A 464 ? 0.4272 0.4425 0.9405 0.0131  0.0261  -0.0461 465 ASN A OD1 
3101  N  ND2 . ASN A 464 ? 0.3967 0.4181 0.9148 0.0130  0.0363  -0.0622 465 ASN A ND2 
3102  N  N   . ARG A 465 ? 0.2008 0.2166 0.6599 0.0112  0.0461  -0.0545 466 ARG A N   
3103  C  CA  . ARG A 465 ? 0.2702 0.2853 0.7210 0.0106  0.0488  -0.0555 466 ARG A CA  
3104  C  C   . ARG A 465 ? 0.3143 0.3268 0.7567 0.0107  0.0468  -0.0482 466 ARG A C   
3105  O  O   . ARG A 465 ? 0.3093 0.3198 0.7548 0.0103  0.0457  -0.0468 466 ARG A O   
3106  C  CB  . ARG A 465 ? 0.3126 0.3318 0.7500 0.0102  0.0558  -0.0610 466 ARG A CB  
3107  C  CG  . ARG A 465 ? 0.3279 0.3510 0.7742 0.0094  0.0599  -0.0708 466 ARG A CG  
3108  C  CD  . ARG A 465 ? 0.4516 0.4790 0.8862 0.0085  0.0661  -0.0753 466 ARG A CD  
3109  N  NE  . ARG A 465 ? 0.6165 0.6500 1.0589 0.0070  0.0717  -0.0863 466 ARG A NE  
3110  C  CZ  . ARG A 465 ? 0.7295 0.7700 1.1677 0.0061  0.0771  -0.0906 466 ARG A CZ  
3111  N  NH1 . ARG A 465 ? 0.7522 0.7935 1.1795 0.0069  0.0768  -0.0839 466 ARG A NH1 
3112  N  NH2 . ARG A 465 ? 0.7619 0.8097 1.2083 0.0039  0.0833  -0.1022 466 ARG A NH2 
3113  N  N   . LEU A 466 ? 0.2374 0.2501 0.6709 0.0112  0.0468  -0.0445 467 LEU A N   
3114  C  CA  . LEU A 466 ? 0.3169 0.3282 0.7435 0.0112  0.0462  -0.0397 467 LEU A CA  
3115  C  C   . LEU A 466 ? 0.2293 0.2382 0.6703 0.0111  0.0404  -0.0342 467 LEU A C   
3116  O  O   . LEU A 466 ? 0.2700 0.2779 0.7108 0.0107  0.0404  -0.0313 467 LEU A O   
3117  C  CB  . LEU A 466 ? 0.2585 0.2710 0.6736 0.0115  0.0483  -0.0388 467 LEU A CB  
3118  C  CG  . LEU A 466 ? 0.2952 0.3098 0.6964 0.0115  0.0531  -0.0413 467 LEU A CG  
3119  C  CD1 . LEU A 466 ? 0.3049 0.3210 0.7022 0.0117  0.0543  -0.0415 467 LEU A CD1 
3120  C  CD2 . LEU A 466 ? 0.1582 0.1722 0.5518 0.0115  0.0545  -0.0398 467 LEU A CD2 
3121  N  N   . ARG A 467 ? 0.2644 0.2728 0.7203 0.0113  0.0351  -0.0326 468 ARG A N   
3122  C  CA  . ARG A 467 ? 0.2851 0.2913 0.7589 0.0111  0.0271  -0.0257 468 ARG A CA  
3123  C  C   . ARG A 467 ? 0.2617 0.2658 0.7474 0.0105  0.0243  -0.0245 468 ARG A C   
3124  O  O   . ARG A 467 ? 0.2745 0.2767 0.7684 0.0099  0.0203  -0.0182 468 ARG A O   
3125  C  CB  . ARG A 467 ? 0.3742 0.3806 0.8626 0.0115  0.0207  -0.0236 468 ARG A CB  
3126  C  CG  . ARG A 467 ? 0.4728 0.4811 0.9530 0.0118  0.0222  -0.0233 468 ARG A CG  
3127  C  CD  . ARG A 467 ? 0.5373 0.5460 1.0323 0.0121  0.0160  -0.0218 468 ARG A CD  
3128  N  NE  . ARG A 467 ? 0.6276 0.6381 1.1171 0.0122  0.0166  -0.0208 468 ARG A NE  
3129  C  CZ  . ARG A 467 ? 0.6792 0.6909 1.1771 0.0124  0.0134  -0.0208 468 ARG A CZ  
3130  N  NH1 . ARG A 467 ? 0.7174 0.7290 1.2301 0.0126  0.0095  -0.0221 468 ARG A NH1 
3131  N  NH2 . ARG A 467 ? 0.6269 0.6403 1.1202 0.0122  0.0141  -0.0202 468 ARG A NH2 
3132  N  N   . SER A 468 ? 0.2778 0.2824 0.7659 0.0105  0.0264  -0.0308 469 SER A N   
3133  C  CA  . SER A 468 ? 0.3745 0.3775 0.8741 0.0098  0.0246  -0.0315 469 SER A CA  
3134  C  C   . SER A 468 ? 0.3487 0.3514 0.8357 0.0092  0.0296  -0.0312 469 SER A C   
3135  O  O   . SER A 468 ? 0.3573 0.3579 0.8552 0.0084  0.0258  -0.0265 469 SER A O   
3136  C  CB  . SER A 468 ? 0.3287 0.3334 0.8329 0.0098  0.0280  -0.0408 469 SER A CB  
3137  O  OG  . SER A 468 ? 0.4042 0.4092 0.9252 0.0104  0.0231  -0.0416 469 SER A OG  
3138  N  N   . ALA A 469 ? 0.2791 0.2839 0.7449 0.0094  0.0371  -0.0357 470 ALA A N   
3139  C  CA  . ALA A 469 ? 0.2670 0.2721 0.7206 0.0089  0.0418  -0.0361 470 ALA A CA  
3140  C  C   . ALA A 469 ? 0.2843 0.2884 0.7418 0.0087  0.0399  -0.0296 470 ALA A C   
3141  O  O   . ALA A 469 ? 0.3019 0.3053 0.7624 0.0079  0.0411  -0.0281 470 ALA A O   
3142  C  CB  . ALA A 469 ? 0.1922 0.2001 0.6252 0.0094  0.0479  -0.0403 470 ALA A CB  
3143  N  N   . TYR A 470 ? 0.2602 0.2648 0.7195 0.0092  0.0374  -0.0261 471 TYR A N   
3144  C  CA  . TYR A 470 ? 0.3048 0.3097 0.7714 0.0089  0.0358  -0.0205 471 TYR A CA  
3145  C  C   . TYR A 470 ? 0.3725 0.3740 0.8621 0.0081  0.0277  -0.0126 471 TYR A C   
3146  O  O   . TYR A 470 ? 0.3535 0.3559 0.8498 0.0069  0.0280  -0.0085 471 TYR A O   
3147  C  CB  . TYR A 470 ? 0.3158 0.3223 0.7829 0.0096  0.0337  -0.0187 471 TYR A CB  
3148  C  CG  . TYR A 470 ? 0.2951 0.3065 0.7711 0.0085  0.0337  -0.0147 471 TYR A CG  
3149  C  CD1 . TYR A 470 ? 0.2602 0.2781 0.7230 0.0074  0.0427  -0.0204 471 TYR A CD1 
3150  C  CD2 . TYR A 470 ? 0.2800 0.2881 0.7598 0.0020  0.0228  -0.0044 471 TYR A CD2 
3151  C  CE1 . TYR A 470 ? 0.2522 0.2733 0.7011 -0.0017 0.0425  -0.0182 471 TYR A CE1 
3152  C  CE2 . TYR A 470 ? 0.3646 0.3741 0.8229 -0.0091 0.0213  -0.0001 471 TYR A CE2 
3153  C  CZ  . TYR A 470 ? 0.2901 0.3067 0.7328 -0.0109 0.0321  -0.0082 471 TYR A CZ  
3154  O  OH  . TYR A 470 ? 0.3386 0.3583 0.7605 -0.0229 0.0323  -0.0065 471 TYR A OH  
3155  N  N   . ASN A 471 ? 0.4457 0.4446 0.9485 0.0081  0.0198  -0.0101 472 ASN A N   
3156  C  CA  . ASN A 471 ? 0.5349 0.5286 1.0587 0.0070  0.0090  -0.0008 472 ASN A CA  
3157  C  C   . ASN A 471 ? 0.6546 0.6475 1.1805 0.0063  0.0116  -0.0040 472 ASN A C   
3158  O  O   . ASN A 471 ? 0.6390 0.6247 1.1707 0.0041  0.0067  0.0038  472 ASN A O   
3159  C  CB  . ASN A 471 ? 0.5598 0.5527 1.0992 0.0072  -0.0014 0.0026  472 ASN A CB  
3160  C  CG  . ASN A 471 ? 0.5982 0.5910 1.1389 0.0073  -0.0064 0.0078  472 ASN A CG  
3161  O  OD1 . ASN A 471 ? 0.5458 0.5351 1.0800 0.0063  -0.0058 0.0123  472 ASN A OD1 
3162  N  ND2 . ASN A 471 ? 0.5662 0.5607 1.1159 0.0079  -0.0111 0.0064  472 ASN A ND2 
3163  N  N   . GLY A 472 ? 0.7827 0.7790 1.2997 0.0068  0.0187  -0.0145 473 GLY A N   
3164  C  CA  . GLY A 472 ? 0.8294 0.8255 1.3489 0.0061  0.0215  -0.0189 473 GLY A CA  
3165  C  C   . GLY A 472 ? 0.8590 0.8542 1.3971 0.0062  0.0154  -0.0208 473 GLY A C   
3166  O  O   . GLY A 472 ? 0.8720 0.8677 1.4181 0.0070  0.0111  -0.0213 473 GLY A O   
3167  N  N   . SER B 28  ? 0.7959 0.6121 1.3822 0.2099  0.0229  0.1777  29  SER B N   
3168  C  CA  . SER B 28  ? 0.8209 0.6312 1.3878 0.2209  0.0256  0.1958  29  SER B CA  
3169  C  C   . SER B 28  ? 0.7914 0.6130 1.3360 0.2245  0.0228  0.1931  29  SER B C   
3170  O  O   . SER B 28  ? 0.7621 0.5932 1.3089 0.2144  0.0248  0.1834  29  SER B O   
3171  C  CB  . SER B 28  ? 0.8570 0.6569 1.4327 0.2160  0.0379  0.2126  29  SER B CB  
3172  O  OG  . SER B 28  ? 0.9031 0.6966 1.4588 0.2282  0.0414  0.2315  29  SER B OG  
3173  N  N   . ARG B 29  ? 0.8064 0.6269 1.3300 0.2396  0.0174  0.2013  30  ARG B N   
3174  C  CA  . ARG B 29  ? 0.7715 0.6025 1.2740 0.2454  0.0123  0.1981  30  ARG B CA  
3175  C  C   . ARG B 29  ? 0.7784 0.6051 1.2645 0.2486  0.0206  0.2137  30  ARG B C   
3176  O  O   . ARG B 29  ? 0.7837 0.6172 1.2503 0.2555  0.0163  0.2128  30  ARG B O   
3177  C  CB  . ARG B 29  ? 0.7551 0.5894 1.2441 0.2612  -0.0006 0.1957  30  ARG B CB  
3178  C  CG  . ARG B 29  ? 0.6855 0.5277 1.1897 0.2586  -0.0084 0.1793  30  ARG B CG  
3179  C  CD  . ARG B 29  ? 0.7025 0.5475 1.1963 0.2749  -0.0206 0.1787  30  ARG B CD  
3180  N  NE  . ARG B 29  ? 0.7181 0.5703 1.2283 0.2727  -0.0261 0.1647  30  ARG B NE  
3181  C  CZ  . ARG B 29  ? 0.7439 0.6016 1.2511 0.2849  -0.0367 0.1610  30  ARG B CZ  
3182  N  NH1 . ARG B 29  ? 0.7652 0.6302 1.2889 0.2820  -0.0399 0.1486  30  ARG B NH1 
3183  N  NH2 . ARG B 29  ? 0.7853 0.6415 1.2729 0.3004  -0.0442 0.1696  30  ARG B NH2 
3184  N  N   . SER B 30  ? 0.7112 0.5269 1.2060 0.2443  0.0325  0.2281  31  SER B N   
3185  C  CA  . SER B 30  ? 0.7913 0.6032 1.2725 0.2469  0.0431  0.2446  31  SER B CA  
3186  C  C   . SER B 30  ? 0.7507 0.5734 1.2294 0.2376  0.0464  0.2359  31  SER B C   
3187  O  O   . SER B 30  ? 0.6679 0.4981 1.1631 0.2244  0.0450  0.2202  31  SER B O   
3188  C  CB  . SER B 30  ? 0.8014 0.6018 1.2994 0.2414  0.0567  0.2604  31  SER B CB  
3189  O  OG  . SER B 30  ? 0.8382 0.6371 1.3255 0.2428  0.0691  0.2762  31  SER B OG  
3190  N  N   . CYS B 31  ? 0.8157 0.6392 1.2728 0.2453  0.0506  0.2463  32  CYS B N   
3191  C  CA  . CYS B 31  ? 0.8077 0.6408 1.2598 0.2385  0.0533  0.2390  32  CYS B CA  
3192  C  C   . CYS B 31  ? 0.8717 0.7010 1.3278 0.2323  0.0700  0.2532  32  CYS B C   
3193  O  O   . CYS B 31  ? 0.9291 0.7633 1.3712 0.2339  0.0743  0.2555  32  CYS B O   
3194  C  CB  . CYS B 31  ? 0.8039 0.6431 1.2282 0.2526  0.0436  0.2368  32  CYS B CB  
3195  S  SG  . CYS B 31  ? 0.7941 0.6427 1.2177 0.2583  0.0237  0.2174  32  CYS B SG  
3196  N  N   . GLY B 32  ? 0.8966 0.7180 1.3736 0.2256  0.0793  0.2625  33  GLY B N   
3197  C  CA  . GLY B 32  ? 0.8999 0.7185 1.3858 0.2199  0.0960  0.2773  33  GLY B CA  
3198  C  C   . GLY B 32  ? 0.8304 0.6583 1.3268 0.2062  0.1008  0.2675  33  GLY B C   
3199  O  O   . GLY B 32  ? 0.8682 0.6980 1.3561 0.2074  0.1116  0.2777  33  GLY B O   
3200  N  N   . GLU B 33  ? 0.8159 0.6499 1.3300 0.1937  0.0931  0.2480  34  GLU B N   
3201  C  CA  . GLU B 33  ? 0.8308 0.6739 1.3554 0.1804  0.0960  0.2372  34  GLU B CA  
3202  C  C   . GLU B 33  ? 0.8268 0.6775 1.3268 0.1858  0.0927  0.2324  34  GLU B C   
3203  O  O   . GLU B 33  ? 0.8282 0.6832 1.3273 0.1810  0.1006  0.2344  34  GLU B O   
3204  C  CB  . GLU B 33  ? 0.8664 0.7143 1.4118 0.1681  0.0874  0.2173  34  GLU B CB  
3205  C  CG  . GLU B 33  ? 0.9191 0.7621 1.4951 0.1582  0.0923  0.2189  34  GLU B CG  
3206  C  CD  . GLU B 33  ? 0.9454 0.7926 1.5379 0.1488  0.0826  0.1989  34  GLU B CD  
3207  O  OE1 . GLU B 33  ? 0.9648 0.8130 1.5481 0.1544  0.0723  0.1896  34  GLU B OE1 
3208  O  OE2 . GLU B 33  ? 0.9317 0.7819 1.5463 0.1367  0.0852  0.1924  34  GLU B OE2 
3209  N  N   . VAL B 34  ? 0.7759 0.6285 1.2574 0.1961  0.0804  0.2255  35  VAL B N   
3210  C  CA  . VAL B 34  ? 0.7416 0.6017 1.2011 0.2026  0.0749  0.2198  35  VAL B CA  
3211  C  C   . VAL B 34  ? 0.8065 0.6622 1.2445 0.2145  0.0843  0.2380  35  VAL B C   
3212  O  O   . VAL B 34  ? 0.7011 0.5622 1.1268 0.2158  0.0864  0.2364  35  VAL B O   
3213  C  CB  . VAL B 34  ? 0.7614 0.6254 1.2091 0.2122  0.0590  0.2092  35  VAL B CB  
3214  C  CG1 . VAL B 34  ? 0.7085 0.5809 1.1364 0.2191  0.0523  0.2026  35  VAL B CG1 
3215  C  CG2 . VAL B 34  ? 0.7473 0.6165 1.2155 0.2011  0.0517  0.1921  35  VAL B CG2 
3216  N  N   . ARG B 35  ? 0.8085 0.6545 1.2417 0.2237  0.0906  0.2558  36  ARG B N   
3217  C  CA  . ARG B 35  ? 0.8986 0.7403 1.3112 0.2354  0.1023  0.2756  36  ARG B CA  
3218  C  C   . ARG B 35  ? 0.9170 0.7607 1.3444 0.2241  0.1187  0.2822  36  ARG B C   
3219  O  O   . ARG B 35  ? 0.9090 0.7557 1.3200 0.2294  0.1261  0.2884  36  ARG B O   
3220  C  CB  . ARG B 35  ? 0.7212 0.5522 1.1274 0.2470  0.1063  0.2939  36  ARG B CB  
3221  N  N   . GLN B 36  ? 0.9886 0.8313 1.4480 0.2092  0.1238  0.2803  37  GLN B N   
3222  C  CA  . GLN B 36  ? 1.0921 0.9384 1.5730 0.1962  0.1370  0.2834  37  GLN B CA  
3223  C  C   . GLN B 36  ? 1.0601 0.9158 1.5345 0.1910  0.1352  0.2712  37  GLN B C   
3224  O  O   . GLN B 36  ? 1.0895 0.9475 1.5566 0.1933  0.1468  0.2806  37  GLN B O   
3225  C  CB  . GLN B 36  ? 1.1835 1.0295 1.7005 0.1806  0.1357  0.2752  37  GLN B CB  
3226  C  CG  . GLN B 36  ? 1.2623 1.1132 1.8070 0.1668  0.1471  0.2767  37  GLN B CG  
3227  C  CD  . GLN B 36  ? 1.3209 1.1717 1.8998 0.1534  0.1427  0.2666  37  GLN B CD  
3228  O  OE1 . GLN B 36  ? 1.3444 1.1877 1.9352 0.1554  0.1431  0.2735  37  GLN B OE1 
3229  N  NE2 . GLN B 36  ? 1.3140 1.1728 1.9082 0.1403  0.1381  0.2499  37  GLN B NE2 
3230  N  N   . ILE B 37  ? 1.0360 0.8973 1.5130 0.1846  0.1210  0.2506  38  ILE B N   
3231  C  CA  . ILE B 37  ? 0.9865 0.8569 1.4612 0.1776  0.1178  0.2367  38  ILE B CA  
3232  C  C   . ILE B 37  ? 0.9808 0.8533 1.4241 0.1914  0.1155  0.2388  38  ILE B C   
3233  O  O   . ILE B 37  ? 0.9802 0.8570 1.4187 0.1895  0.1215  0.2386  38  ILE B O   
3234  C  CB  . ILE B 37  ? 0.9707 0.8469 1.4567 0.1678  0.1038  0.2150  38  ILE B CB  
3235  C  CG1 . ILE B 37  ? 0.9679 0.8429 1.4846 0.1543  0.1059  0.2114  38  ILE B CG1 
3236  C  CG2 . ILE B 37  ? 0.9568 0.8424 1.4386 0.1615  0.1000  0.2013  38  ILE B CG2 
3237  C  CD1 . ILE B 37  ? 0.9549 0.8344 1.4810 0.1469  0.0933  0.1921  38  ILE B CD1 
3238  N  N   . TYR B 38  ? 0.9603 0.8297 1.3827 0.2060  0.1061  0.2403  39  TYR B N   
3239  C  CA  . TYR B 38  ? 0.9472 0.8186 1.3390 0.2216  0.1015  0.2415  39  TYR B CA  
3240  C  C   . TYR B 38  ? 0.9799 0.8473 1.3557 0.2312  0.1175  0.2613  39  TYR B C   
3241  O  O   . TYR B 38  ? 0.9757 0.8466 1.3319 0.2390  0.1187  0.2610  39  TYR B O   
3242  C  CB  . TYR B 38  ? 0.8606 0.7297 1.2357 0.2363  0.0877  0.2403  39  TYR B CB  
3243  C  CG  . TYR B 38  ? 0.8216 0.6957 1.1702 0.2509  0.0766  0.2341  39  TYR B CG  
3244  C  CD1 . TYR B 38  ? 0.7255 0.6096 1.0789 0.2446  0.0664  0.2150  39  TYR B CD1 
3245  C  CD2 . TYR B 38  ? 0.8208 0.6903 1.1399 0.2716  0.0755  0.2470  39  TYR B CD2 
3246  C  CE1 . TYR B 38  ? 0.7291 0.6184 1.0618 0.2579  0.0550  0.2083  39  TYR B CE1 
3247  C  CE2 . TYR B 38  ? 0.7865 0.6613 1.0818 0.2860  0.0635  0.2398  39  TYR B CE2 
3248  C  CZ  . TYR B 38  ? 0.7510 0.6357 1.0548 0.2789  0.0530  0.2202  39  TYR B CZ  
3249  O  OH  . TYR B 38  ? 0.7780 0.6686 1.0614 0.2932  0.0400  0.2122  39  TYR B OH  
3250  N  N   . GLY B 39  ? 1.0836 0.9440 1.4683 0.2311  0.1304  0.2787  40  GLY B N   
3251  C  CA  . GLY B 39  ? 1.1723 1.0296 1.5445 0.2398  0.1484  0.2996  40  GLY B CA  
3252  C  C   . GLY B 39  ? 1.1820 1.0448 1.5731 0.2267  0.1615  0.2997  40  GLY B C   
3253  O  O   . GLY B 39  ? 1.2538 1.1181 1.6285 0.2347  0.1727  0.3094  40  GLY B O   
3254  N  N   . ALA B 40  ? 1.1547 1.0206 1.5794 0.2076  0.1597  0.2886  41  ALA B N   
3255  C  CA  . ALA B 40  ? 1.0895 0.9615 1.5360 0.1941  0.1703  0.2871  41  ALA B CA  
3256  C  C   . ALA B 40  ? 1.0034 0.8820 1.4354 0.1944  0.1660  0.2753  41  ALA B C   
3257  O  O   . ALA B 40  ? 0.9938 0.8768 1.4341 0.1889  0.1767  0.2779  41  ALA B O   
3258  C  CB  . ALA B 40  ? 1.0814 0.9559 1.5644 0.1751  0.1658  0.2752  41  ALA B CB  
3259  N  N   . LYS B 41  ? 1.0081 0.8879 1.4204 0.2010  0.1501  0.2620  42  LYS B N   
3260  C  CA  . LYS B 41  ? 1.0098 0.8961 1.4102 0.2013  0.1439  0.2490  42  LYS B CA  
3261  C  C   . LYS B 41  ? 1.0498 0.9343 1.4146 0.2219  0.1466  0.2582  42  LYS B C   
3262  O  O   . LYS B 41  ? 1.0429 0.9323 1.3940 0.2260  0.1397  0.2473  42  LYS B O   
3263  C  CB  . LYS B 41  ? 0.9681 0.8591 1.3723 0.1953  0.1249  0.2274  42  LYS B CB  
3264  C  CG  . LYS B 41  ? 0.9381 0.8317 1.3734 0.1762  0.1221  0.2168  42  LYS B CG  
3265  C  CD  . LYS B 41  ? 0.8818 0.7812 1.3194 0.1712  0.1053  0.1967  42  LYS B CD  
3266  C  CE  . LYS B 41  ? 0.8260 0.7280 1.2911 0.1541  0.1035  0.1868  42  LYS B CE  
3267  N  NZ  . LYS B 41  ? 0.7922 0.6981 1.2736 0.1413  0.1121  0.1853  42  LYS B NZ  
3268  N  N   . GLY B 42  ? 1.1522 1.0302 1.5018 0.2355  0.1566  0.2780  43  GLY B N   
3269  C  CA  . GLY B 42  ? 1.2005 1.0768 1.5140 0.2565  0.1625  0.2896  43  GLY B CA  
3270  C  C   . GLY B 42  ? 1.1950 1.0680 1.4767 0.2763  0.1498  0.2903  43  GLY B C   
3271  O  O   . GLY B 42  ? 1.2860 1.1563 1.5351 0.2960  0.1562  0.3037  43  GLY B O   
3272  N  N   . PHE B 43  ? 1.1361 1.0100 1.4264 0.2722  0.1317  0.2760  44  PHE B N   
3273  C  CA  . PHE B 43  ? 1.0961 0.9680 1.3598 0.2905  0.1176  0.2753  44  PHE B CA  
3274  C  C   . PHE B 43  ? 1.0513 0.9145 1.3068 0.2997  0.1256  0.2955  44  PHE B C   
3275  O  O   . PHE B 43  ? 1.0376 0.8970 1.3192 0.2870  0.1350  0.3030  44  PHE B O   
3276  C  CB  . PHE B 43  ? 1.0679 0.9448 1.3469 0.2830  0.0966  0.2540  44  PHE B CB  
3277  C  CG  . PHE B 43  ? 1.0294 0.9153 1.3196 0.2726  0.0889  0.2342  44  PHE B CG  
3278  C  CD1 . PHE B 43  ? 1.0453 0.9362 1.3130 0.2854  0.0804  0.2263  44  PHE B CD1 
3279  C  CD2 . PHE B 43  ? 0.9903 0.8800 1.3126 0.2506  0.0895  0.2230  44  PHE B CD2 
3280  C  CE1 . PHE B 43  ? 1.0167 0.9158 1.2967 0.2754  0.0736  0.2084  44  PHE B CE1 
3281  C  CE2 . PHE B 43  ? 0.9737 0.8718 1.3053 0.2410  0.0829  0.2057  44  PHE B CE2 
3282  C  CZ  . PHE B 43  ? 0.9772 0.8798 1.2890 0.2529  0.0752  0.1987  44  PHE B CZ  
3283  N  N   . SER B 44  ? 1.0454 0.9058 1.2647 0.3222  0.1212  0.3036  45  SER B N   
3284  C  CA  . SER B 44  ? 1.0503 0.9025 1.2572 0.3331  0.1288  0.3238  45  SER B CA  
3285  C  C   . SER B 44  ? 1.0325 0.8817 1.2542 0.3296  0.1138  0.3173  45  SER B C   
3286  O  O   . SER B 44  ? 0.9931 0.8474 1.2186 0.3285  0.0941  0.2982  45  SER B O   
3287  C  CB  . SER B 44  ? 1.1051 0.9558 1.2635 0.3599  0.1294  0.3347  45  SER B CB  
3288  O  OG  . SER B 44  ? 1.1287 0.9823 1.2716 0.3647  0.1438  0.3404  45  SER B OG  
3289  N  N   . LEU B 45  ? 1.0147 0.8561 1.2461 0.3282  0.1236  0.3333  46  LEU B N   
3290  C  CA  . LEU B 45  ? 1.0370 0.8746 1.2872 0.3229  0.1120  0.3280  46  LEU B CA  
3291  C  C   . LEU B 45  ? 1.0799 0.9152 1.3018 0.3429  0.0963  0.3287  46  LEU B C   
3292  O  O   . LEU B 45  ? 1.1064 0.9389 1.3412 0.3409  0.0850  0.3237  46  LEU B O   
3293  C  CB  . LEU B 45  ? 0.9937 0.8236 1.2675 0.3137  0.1281  0.3445  46  LEU B CB  
3294  C  CG  . LEU B 45  ? 0.9311 0.7633 1.2394 0.2928  0.1428  0.3441  46  LEU B CG  
3295  C  CD1 . LEU B 45  ? 0.8855 0.7182 1.1830 0.2978  0.1645  0.3629  46  LEU B CD1 
3296  C  CD2 . LEU B 45  ? 0.9347 0.7615 1.2770 0.2798  0.1454  0.3467  46  LEU B CD2 
3297  N  N   . SER B 46  ? 1.1844 1.0213 1.3672 0.3628  0.0950  0.3343  47  SER B N   
3298  C  CA  . SER B 46  ? 1.2608 1.0962 1.4138 0.3835  0.0796  0.3354  47  SER B CA  
3299  C  C   . SER B 46  ? 1.2557 1.0981 1.4202 0.3811  0.0540  0.3114  47  SER B C   
3300  O  O   . SER B 46  ? 1.2519 1.0933 1.4050 0.3933  0.0389  0.3099  47  SER B O   
3301  C  CB  . SER B 46  ? 1.3320 1.1691 1.4380 0.4058  0.0824  0.3431  47  SER B CB  
3302  O  OG  . SER B 46  ? 1.3260 1.1722 1.4259 0.4056  0.0730  0.3250  47  SER B OG  
3303  N  N   . ASP B 47  ? 1.2329 1.0831 1.4215 0.3653  0.0497  0.2932  48  ASP B N   
3304  C  CA  . ASP B 47  ? 1.2315 1.0905 1.4342 0.3621  0.0275  0.2703  48  ASP B CA  
3305  C  C   . ASP B 47  ? 1.1728 1.0317 1.4149 0.3427  0.0254  0.2609  48  ASP B C   
3306  O  O   . ASP B 47  ? 1.1848 1.0506 1.4402 0.3406  0.0083  0.2439  48  ASP B O   
3307  C  CB  . ASP B 47  ? 1.2791 1.1483 1.4798 0.3594  0.0222  0.2544  48  ASP B CB  
3308  C  CG  . ASP B 47  ? 1.3456 1.2169 1.5045 0.3817  0.0172  0.2572  48  ASP B CG  
3309  O  OD1 . ASP B 47  ? 1.4046 1.2712 1.5354 0.4001  0.0130  0.2677  48  ASP B OD1 
3310  O  OD2 . ASP B 47  ? 1.3252 1.2025 1.4776 0.3814  0.0172  0.2481  48  ASP B OD2 
3311  N  N   . VAL B 48  ? 1.0875 0.9395 1.3485 0.3291  0.0426  0.2713  49  VAL B N   
3312  C  CA  . VAL B 48  ? 1.0045 0.8561 1.2995 0.3121  0.0407  0.2620  49  VAL B CA  
3313  C  C   . VAL B 48  ? 0.9702 0.8144 1.2650 0.3205  0.0341  0.2687  49  VAL B C   
3314  O  O   . VAL B 48  ? 0.9781 0.8130 1.2573 0.3312  0.0424  0.2883  49  VAL B O   
3315  C  CB  . VAL B 48  ? 1.2401 1.0882 1.5592 0.2933  0.0595  0.2678  49  VAL B CB  
3316  C  CG1 . VAL B 48  ? 1.2637 1.1010 1.5772 0.2981  0.0763  0.2920  49  VAL B CG1 
3317  C  CG2 . VAL B 48  ? 1.2117 1.0618 1.5634 0.2761  0.0551  0.2537  49  VAL B CG2 
3318  N  N   . PRO B 49  ? 0.9146 0.7636 1.2258 0.3166  0.0193  0.2526  50  PRO B N   
3319  C  CA  . PRO B 49  ? 0.9246 0.7673 1.2390 0.3235  0.0117  0.2562  50  PRO B CA  
3320  C  C   . PRO B 49  ? 0.9592 0.7911 1.2925 0.3135  0.0259  0.2681  50  PRO B C   
3321  O  O   . PRO B 49  ? 0.9578 0.7897 1.3107 0.2971  0.0382  0.2670  50  PRO B O   
3322  C  CB  . PRO B 49  ? 0.8692 0.7227 1.2011 0.3182  -0.0045 0.2336  50  PRO B CB  
3323  C  CG  . PRO B 49  ? 0.8606 0.7261 1.1870 0.3169  -0.0102 0.2206  50  PRO B CG  
3324  C  CD  . PRO B 49  ? 0.8527 0.7148 1.1758 0.3088  0.0074  0.2300  50  PRO B CD  
3325  N  N   . GLN B 50  ? 1.0239 0.8467 1.3521 0.3239  0.0232  0.2790  51  GLN B N   
3326  C  CA  . GLN B 50  ? 1.0168 0.8287 1.3639 0.3165  0.0346  0.2904  51  GLN B CA  
3327  C  C   . GLN B 50  ? 0.9687 0.7836 1.3460 0.3026  0.0286  0.2731  51  GLN B C   
3328  O  O   . GLN B 50  ? 0.9160 0.7275 1.3175 0.2877  0.0391  0.2735  51  GLN B O   
3329  C  CB  . GLN B 50  ? 1.1839 0.9849 1.5141 0.3335  0.0329  0.3079  51  GLN B CB  
3330  C  CG  . GLN B 50  ? 1.3006 1.1021 1.5928 0.3534  0.0303  0.3194  51  GLN B CG  
3331  C  CD  . GLN B 50  ? 1.3705 1.1819 1.6483 0.3647  0.0080  0.3031  51  GLN B CD  
3332  O  OE1 . GLN B 50  ? 1.3709 1.1887 1.6677 0.3586  -0.0049 0.2844  51  GLN B OE1 
3333  N  NE2 . GLN B 50  ? 1.4226 1.2364 1.6673 0.3817  0.0039  0.3098  51  GLN B NE2 
3334  N  N   . ALA B 51  ? 0.8914 0.7136 1.2672 0.3082  0.0116  0.2576  52  ALA B N   
3335  C  CA  . ALA B 51  ? 0.8581 0.6854 1.2589 0.2973  0.0056  0.2405  52  ALA B CA  
3336  C  C   . ALA B 51  ? 0.7321 0.5755 1.1324 0.2961  -0.0068 0.2203  52  ALA B C   
3337  O  O   . ALA B 51  ? 0.7522 0.6013 1.1329 0.3061  -0.0138 0.2194  52  ALA B O   
3338  C  CB  . ALA B 51  ? 0.7808 0.6004 1.1855 0.3062  -0.0013 0.2442  52  ALA B CB  
3339  N  N   . GLU B 52  ? 0.7053 0.5562 1.1277 0.2841  -0.0093 0.2043  53  GLU B N   
3340  C  CA  . GLU B 52  ? 0.6782 0.5456 1.1044 0.2804  -0.0184 0.1856  53  GLU B CA  
3341  C  C   . GLU B 52  ? 0.7354 0.6100 1.1480 0.2972  -0.0346 0.1811  53  GLU B C   
3342  O  O   . GLU B 52  ? 0.8487 0.7168 1.2555 0.3098  -0.0410 0.1877  53  GLU B O   
3343  C  CB  . GLU B 52  ? 0.6529 0.5265 1.1045 0.2663  -0.0174 0.1714  53  GLU B CB  
3344  C  CG  . GLU B 52  ? 0.6365 0.5058 1.1036 0.2491  -0.0042 0.1717  53  GLU B CG  
3345  C  CD  . GLU B 52  ? 0.8359 0.7119 1.3253 0.2369  -0.0048 0.1567  53  GLU B CD  
3346  O  OE1 . GLU B 52  ? 0.8512 0.7359 1.3442 0.2413  -0.0140 0.1466  53  GLU B OE1 
3347  O  OE2 . GLU B 52  ? 0.8429 0.7158 1.3462 0.2236  0.0039  0.1549  53  GLU B OE2 
3348  N  N   . ILE B 53  ? 0.7445 0.6329 1.1531 0.2972  -0.0416 0.1697  54  ILE B N   
3349  C  CA  . ILE B 53  ? 0.6982 0.5965 1.0969 0.3120  -0.0581 0.1631  54  ILE B CA  
3350  C  C   . ILE B 53  ? 0.6721 0.5894 1.0891 0.3015  -0.0627 0.1443  54  ILE B C   
3351  O  O   . ILE B 53  ? 0.6409 0.5623 1.0706 0.2849  -0.0538 0.1379  54  ILE B O   
3352  C  CB  . ILE B 53  ? 0.9798 0.8762 1.3526 0.3256  -0.0634 0.1702  54  ILE B CB  
3353  C  CG1 . ILE B 53  ? 1.0200 0.8982 1.3754 0.3338  -0.0553 0.1913  54  ILE B CG1 
3354  C  CG2 . ILE B 53  ? 0.9995 0.9061 1.3624 0.3427  -0.0827 0.1629  54  ILE B CG2 
3355  C  CD1 . ILE B 53  ? 1.0630 0.9390 1.3903 0.3490  -0.0602 0.2002  54  ILE B CD1 
3356  N  N   . SER B 54  ? 0.7172 0.6466 1.1368 0.3107  -0.0760 0.1362  55  SER B N   
3357  C  CA  . SER B 54  ? 0.7431 0.6921 1.1819 0.3006  -0.0802 0.1199  55  SER B CA  
3358  C  C   . SER B 54  ? 0.7811 0.7376 1.2187 0.2919  -0.0781 0.1138  55  SER B C   
3359  O  O   . SER B 54  ? 0.7758 0.7276 1.1940 0.3009  -0.0805 0.1197  55  SER B O   
3360  C  CB  . SER B 54  ? 0.8112 0.7731 1.2516 0.3136  -0.0954 0.1147  55  SER B CB  
3361  O  OG  . SER B 54  ? 0.8561 0.8172 1.2740 0.3305  -0.1053 0.1201  55  SER B OG  
3362  N  N   . GLY B 55  ? 0.7512 0.7187 1.2088 0.2749  -0.0737 0.1020  56  GLY B N   
3363  C  CA  . GLY B 55  ? 0.7567 0.7307 1.2153 0.2647  -0.0709 0.0957  56  GLY B CA  
3364  C  C   . GLY B 55  ? 0.7670 0.7586 1.2325 0.2661  -0.0831 0.0844  56  GLY B C   
3365  O  O   . GLY B 55  ? 0.7703 0.7715 1.2475 0.2530  -0.0810 0.0750  56  GLY B O   
3366  N  N   . GLU B 56  ? 0.8249 0.8206 1.2838 0.2818  -0.0961 0.0856  57  GLU B N   
3367  C  CA  . GLU B 56  ? 0.8579 0.8706 1.3255 0.2837  -0.1099 0.0749  57  GLU B CA  
3368  C  C   . GLU B 56  ? 0.8644 0.8788 1.3221 0.2835  -0.1129 0.0720  57  GLU B C   
3369  O  O   . GLU B 56  ? 0.8392 0.8672 1.3104 0.2765  -0.1206 0.0601  57  GLU B O   
3370  C  CB  . GLU B 56  ? 0.9717 0.9872 1.4325 0.3020  -0.1237 0.0782  57  GLU B CB  
3371  C  CG  . GLU B 56  ? 1.0830 1.0815 1.5146 0.3207  -0.1232 0.0941  57  GLU B CG  
3372  C  CD  . GLU B 56  ? 1.1794 1.1825 1.6022 0.3398  -0.1382 0.0977  57  GLU B CD  
3373  O  OE1 . GLU B 56  ? 1.1947 1.2144 1.6322 0.3384  -0.1515 0.0863  57  GLU B OE1 
3374  O  OE2 . GLU B 56  ? 1.1992 1.1888 1.6012 0.3558  -0.1371 0.1118  57  GLU B OE2 
3375  N  N   . HIS B 57  ? 0.8644 0.8641 1.2992 0.2909  -0.1067 0.0829  58  HIS B N   
3376  C  CA  . HIS B 57  ? 0.8478 0.8473 1.2695 0.2943  -0.1098 0.0817  58  HIS B CA  
3377  C  C   . HIS B 57  ? 0.8279 0.8256 1.2564 0.2769  -0.0969 0.0785  58  HIS B C   
3378  O  O   . HIS B 57  ? 0.8473 0.8445 1.2667 0.2780  -0.0980 0.0768  58  HIS B O   
3379  C  CB  . HIS B 57  ? 0.8736 0.8584 1.2643 0.3146  -0.1104 0.0964  58  HIS B CB  
3380  C  CG  . HIS B 57  ? 0.8641 0.8311 1.2458 0.3124  -0.0948 0.1098  58  HIS B CG  
3381  N  ND1 . HIS B 57  ? 0.8330 0.7926 1.2181 0.3137  -0.0913 0.1165  58  HIS B ND1 
3382  C  CD2 . HIS B 57  ? 0.8978 0.8534 1.2706 0.3069  -0.0818 0.1175  58  HIS B CD2 
3383  C  CE1 . HIS B 57  ? 0.8523 0.7966 1.2319 0.3083  -0.0771 0.1278  58  HIS B CE1 
3384  N  NE2 . HIS B 57  ? 0.8840 0.8264 1.2565 0.3038  -0.0706 0.1290  58  HIS B NE2 
3385  N  N   . LEU B 58  ? 0.7634 0.7602 1.2074 0.2615  -0.0852 0.0775  59  LEU B N   
3386  C  CA  . LEU B 58  ? 0.6985 0.6933 1.1485 0.2450  -0.0727 0.0753  59  LEU B CA  
3387  C  C   . LEU B 58  ? 0.6888 0.6978 1.1532 0.2343  -0.0776 0.0619  59  LEU B C   
3388  O  O   . LEU B 58  ? 0.6947 0.7157 1.1789 0.2257  -0.0811 0.0526  59  LEU B O   
3389  C  CB  . LEU B 58  ? 0.6442 0.6352 1.1071 0.2323  -0.0609 0.0767  59  LEU B CB  
3390  C  CG  . LEU B 58  ? 0.6311 0.6060 1.0831 0.2389  -0.0537 0.0901  59  LEU B CG  
3391  C  CD1 . LEU B 58  ? 0.5359 0.5082 1.0033 0.2256  -0.0439 0.0888  59  LEU B CD1 
3392  C  CD2 . LEU B 58  ? 0.6300 0.5924 1.0634 0.2432  -0.0465 0.1011  59  LEU B CD2 
3393  N  N   . ARG B 59  ? 0.7151 0.7222 1.1695 0.2350  -0.0776 0.0612  60  ARG B N   
3394  C  CA  . ARG B 59  ? 0.6916 0.7103 1.1585 0.2255  -0.0830 0.0489  60  ARG B CA  
3395  C  C   . ARG B 59  ? 0.6938 0.7149 1.1753 0.2057  -0.0706 0.0450  60  ARG B C   
3396  O  O   . ARG B 59  ? 0.6461 0.6784 1.1446 0.1952  -0.0737 0.0348  60  ARG B O   
3397  C  CB  . ARG B 59  ? 0.7194 0.7344 1.1694 0.2350  -0.0885 0.0490  60  ARG B CB  
3398  N  N   . ILE B 60  ? 0.6469 0.6572 1.1220 0.2009  -0.0568 0.0533  61  ILE B N   
3399  C  CA  . ILE B 60  ? 0.5159 0.5272 1.0015 0.1836  -0.0455 0.0502  61  ILE B CA  
3400  C  C   . ILE B 60  ? 0.4734 0.4822 0.9678 0.1769  -0.0377 0.0524  61  ILE B C   
3401  O  O   . ILE B 60  ? 0.4264 0.4440 0.9366 0.1673  -0.0369 0.0451  61  ILE B O   
3402  C  CB  . ILE B 60  ? 0.5852 0.5869 1.0582 0.1812  -0.0361 0.0562  61  ILE B CB  
3403  C  CG1 . ILE B 60  ? 0.5269 0.5316 0.9925 0.1868  -0.0436 0.0521  61  ILE B CG1 
3404  C  CG2 . ILE B 60  ? 0.3866 0.3889 0.8698 0.1641  -0.0250 0.0535  61  ILE B CG2 
3405  C  CD1 . ILE B 60  ? 0.5504 0.5437 0.9941 0.2003  -0.0415 0.0621  61  ILE B CD1 
3406  N  N   . CYS B 61  ? 0.4934 0.4898 0.9776 0.1823  -0.0318 0.0625  62  CYS B N   
3407  C  CA  . CYS B 61  ? 0.5108 0.5030 1.0031 0.1773  -0.0255 0.0645  62  CYS B CA  
3408  C  C   . CYS B 61  ? 0.5140 0.5150 1.0179 0.1807  -0.0331 0.0589  62  CYS B C   
3409  O  O   . CYS B 61  ? 0.4965 0.5024 0.9977 0.1915  -0.0436 0.0581  62  CYS B O   
3410  C  CB  . CYS B 61  ? 0.5162 0.4932 0.9968 0.1845  -0.0198 0.0772  62  CYS B CB  
3411  S  SG  . CYS B 61  ? 0.9418 0.9085 1.4089 0.1827  -0.0102 0.0861  62  CYS B SG  
3412  N  N   . PRO B 62  ? 0.5512 0.5546 1.0681 0.1720  -0.0281 0.0547  63  PRO B N   
3413  C  CA  . PRO B 62  ? 0.5548 0.5664 1.0838 0.1751  -0.0336 0.0498  63  PRO B CA  
3414  C  C   . PRO B 62  ? 0.5993 0.6048 1.1210 0.1896  -0.0398 0.0568  63  PRO B C   
3415  O  O   . PRO B 62  ? 0.6296 0.6214 1.1417 0.1936  -0.0350 0.0659  63  PRO B O   
3416  C  CB  . PRO B 62  ? 0.5185 0.5283 1.0572 0.1655  -0.0249 0.0468  63  PRO B CB  
3417  C  CG  . PRO B 62  ? 0.4910 0.4980 1.0268 0.1547  -0.0171 0.0461  63  PRO B CG  
3418  C  CD  . PRO B 62  ? 0.5004 0.4994 1.0214 0.1597  -0.0174 0.0538  63  PRO B CD  
3419  N  N   . GLN B 63  ? 0.6767 0.6921 1.2038 0.1973  -0.0503 0.0529  64  GLN B N   
3420  C  CA  . GLN B 63  ? 0.7873 0.7978 1.3065 0.2125  -0.0576 0.0594  64  GLN B CA  
3421  C  C   . GLN B 63  ? 0.7862 0.7884 1.3095 0.2131  -0.0522 0.0632  64  GLN B C   
3422  O  O   . GLN B 63  ? 0.8151 0.8239 1.3538 0.2063  -0.0497 0.0565  64  GLN B O   
3423  C  CB  . GLN B 63  ? 0.8589 0.8836 1.3864 0.2194  -0.0708 0.0530  64  GLN B CB  
3424  C  CG  . GLN B 63  ? 0.9728 1.0093 1.5061 0.2135  -0.0759 0.0448  64  GLN B CG  
3425  C  CD  . GLN B 63  ? 1.0626 1.1071 1.5946 0.2253  -0.0916 0.0421  64  GLN B CD  
3426  O  OE1 . GLN B 63  ? 1.1246 1.1616 1.6400 0.2403  -0.0977 0.0495  64  GLN B OE1 
3427  N  NE2 . GLN B 63  ? 1.0728 1.1323 1.6225 0.2189  -0.0984 0.0318  64  GLN B NE2 
3428  N  N   . GLY B 64  ? 0.7231 0.7105 1.2328 0.2219  -0.0504 0.0744  65  GLY B N   
3429  C  CA  . GLY B 64  ? 0.7254 0.7021 1.2386 0.2227  -0.0452 0.0793  65  GLY B CA  
3430  C  C   . GLY B 64  ? 0.6894 0.6496 1.1852 0.2327  -0.0434 0.0934  65  GLY B C   
3431  O  O   . GLY B 64  ? 0.6880 0.6457 1.1693 0.2370  -0.0442 0.0984  65  GLY B O   
3432  N  N   . TYR B 65  ? 0.6489 0.5978 1.1462 0.2366  -0.0407 0.1002  66  TYR B N   
3433  C  CA  . TYR B 65  ? 0.6417 0.5745 1.1232 0.2468  -0.0388 0.1152  66  TYR B CA  
3434  C  C   . TYR B 65  ? 0.6059 0.5298 1.0819 0.2383  -0.0278 0.1219  66  TYR B C   
3435  O  O   . TYR B 65  ? 0.6219 0.5442 1.1102 0.2246  -0.0193 0.1184  66  TYR B O   
3436  C  CB  . TYR B 65  ? 0.6939 0.6164 1.1814 0.2515  -0.0380 0.1208  66  TYR B CB  
3437  C  CG  . TYR B 65  ? 0.7521 0.6835 1.2428 0.2623  -0.0493 0.1157  66  TYR B CG  
3438  C  CD1 . TYR B 65  ? 0.8110 0.7403 1.2859 0.2796  -0.0588 0.1230  66  TYR B CD1 
3439  C  CD2 . TYR B 65  ? 0.7542 0.6968 1.2637 0.2558  -0.0508 0.1036  66  TYR B CD2 
3440  C  CE1 . TYR B 65  ? 0.8480 0.7868 1.3271 0.2896  -0.0697 0.1182  66  TYR B CE1 
3441  C  CE2 . TYR B 65  ? 0.8032 0.7554 1.3178 0.2652  -0.0606 0.0992  66  TYR B CE2 
3442  C  CZ  . TYR B 65  ? 0.8481 0.7987 1.3483 0.2818  -0.0702 0.1064  66  TYR B CZ  
3443  O  OH  . TYR B 65  ? 0.8841 0.8452 1.3907 0.2913  -0.0804 0.1021  66  TYR B OH  
3444  N  N   . THR B 66  ? 0.5961 0.5149 1.0533 0.2476  -0.0286 0.1314  67  THR B N   
3445  C  CA  . THR B 66  ? 0.5696 0.4839 1.0207 0.2404  -0.0191 0.1365  67  THR B CA  
3446  C  C   . THR B 66  ? 0.5978 0.4979 1.0310 0.2510  -0.0142 0.1544  67  THR B C   
3447  O  O   . THR B 66  ? 0.6241 0.5190 1.0445 0.2665  -0.0209 0.1623  67  THR B O   
3448  C  CB  . THR B 66  ? 0.6484 0.5755 1.0947 0.2387  -0.0240 0.1271  67  THR B CB  
3449  O  OG1 . THR B 66  ? 0.5444 0.4676 0.9865 0.2308  -0.0139 0.1312  67  THR B OG1 
3450  C  CG2 . THR B 66  ? 0.5729 0.5029 1.0017 0.2568  -0.0362 0.1294  67  THR B CG2 
3451  N  N   . CYS B 67  ? 0.5932 0.4873 1.0260 0.2426  -0.0020 0.1614  68  CYS B N   
3452  C  CA  . CYS B 67  ? 0.7300 0.6122 1.1464 0.2512  0.0056  0.1797  68  CYS B CA  
3453  C  C   . CYS B 67  ? 0.6701 0.5567 1.0669 0.2586  0.0038  0.1809  68  CYS B C   
3454  O  O   . CYS B 67  ? 0.6670 0.5456 1.0471 0.2667  0.0109  0.1960  68  CYS B O   
3455  C  CB  . CYS B 67  ? 0.6152 0.4890 1.0448 0.2383  0.0212  0.1880  68  CYS B CB  
3456  S  SG  . CYS B 67  ? 1.2991 1.1618 1.7463 0.2357  0.0246  0.1944  68  CYS B SG  
3457  N  N   . CYS B 68  ? 0.6659 0.5657 1.0653 0.2559  -0.0052 0.1653  69  CYS B N   
3458  C  CA  . CYS B 68  ? 0.7281 0.6328 1.1121 0.2614  -0.0076 0.1639  69  CYS B CA  
3459  C  C   . CYS B 68  ? 0.7859 0.6974 1.1562 0.2783  -0.0245 0.1585  69  CYS B C   
3460  O  O   . CYS B 68  ? 0.7710 0.6931 1.1529 0.2771  -0.0356 0.1453  69  CYS B O   
3461  C  CB  . CYS B 68  ? 0.6838 0.5985 1.0821 0.2449  -0.0046 0.1503  69  CYS B CB  
3462  S  SG  . CYS B 68  ? 0.7590 0.6672 1.1708 0.2265  0.0138  0.1558  69  CYS B SG  
3463  N  N   . THR B 69  ? 0.8375 0.7437 1.1831 0.2943  -0.0264 0.1690  70  THR B N   
3464  C  CA  . THR B 69  ? 0.8522 0.7660 1.1839 0.3108  -0.0439 0.1623  70  THR B CA  
3465  C  C   . THR B 69  ? 0.8099 0.7356 1.1475 0.3041  -0.0475 0.1481  70  THR B C   
3466  O  O   . THR B 69  ? 0.8227 0.7490 1.1714 0.2880  -0.0355 0.1458  70  THR B O   
3467  C  CB  . THR B 69  ? 0.8615 0.7663 1.1618 0.3312  -0.0449 0.1782  70  THR B CB  
3468  O  OG1 . THR B 69  ? 0.8414 0.7410 1.1284 0.3290  -0.0295 0.1881  70  THR B OG1 
3469  C  CG2 . THR B 69  ? 0.8283 0.7213 1.1234 0.3375  -0.0412 0.1931  70  THR B CG2 
3470  N  N   . SER B 70  ? 0.8548 0.7901 1.1864 0.3162  -0.0646 0.1384  71  SER B N   
3471  C  CA  . SER B 70  ? 0.8685 0.8157 1.2082 0.3099  -0.0695 0.1241  71  SER B CA  
3472  C  C   . SER B 70  ? 0.8259 0.7671 1.1514 0.3097  -0.0583 0.1310  71  SER B C   
3473  O  O   . SER B 70  ? 0.7924 0.7386 1.1308 0.2949  -0.0522 0.1230  71  SER B O   
3474  C  CB  . SER B 70  ? 0.9096 0.8681 1.2452 0.3248  -0.0908 0.1137  71  SER B CB  
3475  O  OG  . SER B 70  ? 0.9503 0.9204 1.2974 0.3160  -0.0960 0.0992  71  SER B OG  
3476  N  N   . GLU B 71  ? 0.8511 0.7820 1.1482 0.3260  -0.0543 0.1465  72  GLU B N   
3477  C  CA  . GLU B 71  ? 0.8768 0.8019 1.1547 0.3279  -0.0403 0.1557  72  GLU B CA  
3478  C  C   . GLU B 71  ? 0.8572 0.7774 1.1524 0.3071  -0.0206 0.1607  72  GLU B C   
3479  O  O   . GLU B 71  ? 0.8309 0.7535 1.1299 0.2982  -0.0130 0.1568  72  GLU B O   
3480  C  CB  . GLU B 71  ? 0.9025 0.8175 1.1429 0.3483  -0.0362 0.1736  72  GLU B CB  
3481  N  N   . MET B 72  ? 0.8042 0.7177 1.1103 0.2997  -0.0134 0.1685  73  MET B N   
3482  C  CA  . MET B 72  ? 0.8031 0.7126 1.1276 0.2803  0.0031  0.1721  73  MET B CA  
3483  C  C   . MET B 72  ? 0.7406 0.6606 1.0894 0.2619  0.0005  0.1542  73  MET B C   
3484  O  O   . MET B 72  ? 0.7228 0.6426 1.0801 0.2484  0.0120  0.1538  73  MET B O   
3485  C  CB  . MET B 72  ? 0.7743 0.6759 1.1084 0.2769  0.0076  0.1807  73  MET B CB  
3486  C  CG  . MET B 72  ? 0.7949 0.6854 1.1063 0.2934  0.0121  0.2003  73  MET B CG  
3487  S  SD  . MET B 72  ? 0.9360 0.8172 1.2627 0.2885  0.0162  0.2090  73  MET B SD  
3488  C  CE  . MET B 72  ? 0.6410 0.5200 0.9940 0.2649  0.0342  0.2098  73  MET B CE  
3489  N  N   . GLU B 73  ? 0.7102 0.6400 1.0698 0.2614  -0.0142 0.1399  74  GLU B N   
3490  C  CA  . GLU B 73  ? 0.7234 0.6646 1.1043 0.2447  -0.0167 0.1236  74  GLU B CA  
3491  C  C   . GLU B 73  ? 0.7324 0.6783 1.1092 0.2426  -0.0161 0.1177  74  GLU B C   
3492  O  O   . GLU B 73  ? 0.7454 0.6927 1.1329 0.2271  -0.0069 0.1142  74  GLU B O   
3493  C  CB  . GLU B 73  ? 0.7042 0.6565 1.0959 0.2468  -0.0320 0.1111  74  GLU B CB  
3494  C  CG  . GLU B 73  ? 0.6652 0.6284 1.0805 0.2279  -0.0314 0.0974  74  GLU B CG  
3495  C  CD  . GLU B 73  ? 0.6679 0.6444 1.0943 0.2298  -0.0458 0.0852  74  GLU B CD  
3496  O  OE1 . GLU B 73  ? 0.6805 0.6596 1.0966 0.2452  -0.0584 0.0845  74  GLU B OE1 
3497  O  OE2 . GLU B 73  ? 0.6428 0.6275 1.0884 0.2163  -0.0447 0.0766  74  GLU B OE2 
3498  N  N   . GLU B 74  ? 0.7850 0.7332 1.1463 0.2589  -0.0269 0.1161  75  GLU B N   
3499  C  CA  . GLU B 74  ? 0.8176 0.7692 1.1730 0.2603  -0.0278 0.1106  75  GLU B CA  
3500  C  C   . GLU B 74  ? 0.7769 0.7201 1.1248 0.2547  -0.0094 0.1214  75  GLU B C   
3501  O  O   . GLU B 74  ? 0.7332 0.6801 1.0918 0.2410  -0.0038 0.1145  75  GLU B O   
3502  C  CB  . GLU B 74  ? 0.9429 0.8953 1.2776 0.2834  -0.0414 0.1110  75  GLU B CB  
3503  C  CG  . GLU B 74  ? 1.0498 1.0017 1.3653 0.2886  -0.0396 0.1087  75  GLU B CG  
3504  C  CD  . GLU B 74  ? 1.1403 1.0890 1.4157 0.3107  -0.0492 0.1107  75  GLU B CD  
3505  O  OE1 . GLU B 74  ? 1.1861 1.1314 1.4513 0.3241  -0.0544 0.1190  75  GLU B OE1 
3506  O  OE2 . GLU B 74  ? 1.1729 1.1223 1.4263 0.3156  -0.0519 0.1038  75  GLU B OE2 
3507  N  N   . ASN B 75  ? 0.7541 0.6866 1.0840 0.2650  0.0003  0.1389  76  ASN B N   
3508  C  CA  . ASN B 75  ? 0.7695 0.6943 1.0922 0.2611  0.0189  0.1515  76  ASN B CA  
3509  C  C   . ASN B 75  ? 0.7430 0.6686 1.0906 0.2379  0.0293  0.1483  76  ASN B C   
3510  O  O   . ASN B 75  ? 0.7704 0.6973 1.1217 0.2294  0.0377  0.1466  76  ASN B O   
3511  C  CB  . ASN B 75  ? 0.8305 0.7444 1.1337 0.2740  0.0281  0.1718  76  ASN B CB  
3512  C  CG  . ASN B 75  ? 0.9237 0.8360 1.1936 0.2989  0.0206  0.1772  76  ASN B CG  
3513  O  OD1 . ASN B 75  ? 0.9380 0.8578 1.2026 0.3076  0.0044  0.1641  76  ASN B OD1 
3514  N  ND2 . ASN B 75  ? 0.9382 0.8412 1.1847 0.3110  0.0323  0.1965  76  ASN B ND2 
3515  N  N   . LEU B 76  ? 0.6806 0.6057 1.0444 0.2288  0.0283  0.1469  77  LEU B N   
3516  C  CA  . LEU B 76  ? 0.6405 0.5669 1.0268 0.2083  0.0363  0.1427  77  LEU B CA  
3517  C  C   . LEU B 76  ? 0.6388 0.5757 1.0368 0.1962  0.0308  0.1260  77  LEU B C   
3518  O  O   . LEU B 76  ? 0.6060 0.5440 1.0148 0.1822  0.0390  0.1237  77  LEU B O   
3519  C  CB  . LEU B 76  ? 0.6801 0.6047 1.0798 0.2033  0.0341  0.1426  77  LEU B CB  
3520  C  CG  . LEU B 76  ? 0.7262 0.6393 1.1217 0.2094  0.0426  0.1596  77  LEU B CG  
3521  C  CD1 . LEU B 76  ? 0.7365 0.6486 1.1479 0.2033  0.0391  0.1563  77  LEU B CD1 
3522  C  CD2 . LEU B 76  ? 0.7259 0.6333 1.1252 0.2020  0.0591  0.1707  77  LEU B CD2 
3523  N  N   . ALA B 77  ? 0.6316 0.5767 1.0286 0.2017  0.0168  0.1148  78  ALA B N   
3524  C  CA  . ALA B 77  ? 0.7008 0.6563 1.1094 0.1907  0.0114  0.0997  78  ALA B CA  
3525  C  C   . ALA B 77  ? 0.7176 0.6725 1.1195 0.1895  0.0171  0.0996  78  ALA B C   
3526  O  O   . ALA B 77  ? 0.6810 0.6386 1.0937 0.1748  0.0230  0.0947  78  ALA B O   
3527  C  CB  . ALA B 77  ? 0.4423 0.4068 0.8525 0.1980  -0.0049 0.0890  78  ALA B CB  
3528  N  N   . ASN B 78  ? 0.7684 0.7195 1.1513 0.2062  0.0153  0.1052  79  ASN B N   
3529  C  CA  . ASN B 78  ? 0.8557 0.8059 1.2306 0.2073  0.0212  0.1055  79  ASN B CA  
3530  C  C   . ASN B 78  ? 0.7902 0.7337 1.1661 0.1990  0.0389  0.1169  79  ASN B C   
3531  O  O   . ASN B 78  ? 0.7942 0.7387 1.1716 0.1928  0.0452  0.1147  79  ASN B O   
3532  C  CB  . ASN B 78  ? 1.0327 0.9802 1.3843 0.2296  0.0156  0.1094  79  ASN B CB  
3533  C  CG  . ASN B 78  ? 1.1588 1.1149 1.5141 0.2362  -0.0039 0.0946  79  ASN B CG  
3534  O  OD1 . ASN B 78  ? 1.1772 1.1419 1.5520 0.2222  -0.0109 0.0807  79  ASN B OD1 
3535  N  ND2 . ASN B 78  ? 1.2365 1.1911 1.5646 0.2542  -0.0134 0.0951  79  ASN B ND2 
3536  N  N   . ARG B 79  ? 0.7127 0.6496 1.0901 0.1985  0.0464  0.1287  80  ARG B N   
3537  C  CA  . ARG B 79  ? 0.6998 0.6316 1.0848 0.1886  0.0621  0.1387  80  ARG B CA  
3538  C  C   . ARG B 79  ? 0.6503 0.5878 1.0573 0.1681  0.0628  0.1279  80  ARG B C   
3539  O  O   . ARG B 79  ? 0.6946 0.6326 1.1070 0.1597  0.0712  0.1284  80  ARG B O   
3540  C  CB  . ARG B 79  ? 0.6694 0.5931 1.0545 0.1923  0.0686  0.1530  80  ARG B CB  
3541  C  CG  . ARG B 79  ? 0.6888 0.6087 1.0897 0.1796  0.0832  0.1617  80  ARG B CG  
3542  C  CD  . ARG B 79  ? 0.7576 0.6765 1.1526 0.1807  0.0956  0.1693  80  ARG B CD  
3543  N  NE  . ARG B 79  ? 0.8516 0.7660 1.2204 0.2006  0.0994  0.1811  80  ARG B NE  
3544  C  CZ  . ARG B 79  ? 0.9448 0.8524 1.3058 0.2083  0.1134  0.2001  80  ARG B CZ  
3545  N  NH1 . ARG B 79  ? 0.9729 0.8776 1.3543 0.1969  0.1242  0.2088  80  ARG B NH1 
3546  N  NH2 . ARG B 79  ? 0.9922 0.8964 1.3248 0.2281  0.1166  0.2105  80  ARG B NH2 
3547  N  N   . SER B 80  ? 0.5911 0.5331 1.0099 0.1611  0.0542  0.1185  81  SER B N   
3548  C  CA  . SER B 80  ? 0.5204 0.4681 0.9571 0.1436  0.0542  0.1083  81  SER B CA  
3549  C  C   . SER B 80  ? 0.4601 0.4146 0.8967 0.1384  0.0512  0.0981  81  SER B C   
3550  O  O   . SER B 80  ? 0.4632 0.4195 0.9087 0.1263  0.0567  0.0953  81  SER B O   
3551  C  CB  . SER B 80  ? 0.5207 0.4726 0.9671 0.1400  0.0456  0.1006  81  SER B CB  
3552  O  OG  . SER B 80  ? 0.5411 0.4988 0.9815 0.1482  0.0339  0.0934  81  SER B OG  
3553  N  N   . HIS B 81  ? 0.3831 0.3414 0.8103 0.1479  0.0417  0.0923  82  HIS B N   
3554  C  CA  . HIS B 81  ? 0.4830 0.4470 0.9103 0.1443  0.0381  0.0828  82  HIS B CA  
3555  C  C   . HIS B 81  ? 0.5149 0.4744 0.9356 0.1446  0.0487  0.0891  82  HIS B C   
3556  O  O   . HIS B 81  ? 0.4671 0.4298 0.8949 0.1337  0.0515  0.0837  82  HIS B O   
3557  C  CB  . HIS B 81  ? 0.4929 0.4609 0.9125 0.1565  0.0254  0.0760  82  HIS B CB  
3558  C  CG  . HIS B 81  ? 0.6197 0.5923 1.0398 0.1542  0.0213  0.0666  82  HIS B CG  
3559  N  ND1 . HIS B 81  ? 0.6064 0.5750 1.0130 0.1645  0.0239  0.0692  82  HIS B ND1 
3560  C  CD2 . HIS B 81  ? 0.5656 0.5461 0.9984 0.1431  0.0154  0.0549  82  HIS B CD2 
3561  C  CE1 . HIS B 81  ? 0.5928 0.5663 1.0045 0.1594  0.0187  0.0584  82  HIS B CE1 
3562  N  NE2 . HIS B 81  ? 0.5699 0.5506 0.9978 0.1460  0.0136  0.0502  82  HIS B NE2 
3563  N  N   . ALA B 82  ? 0.5233 0.4757 0.9302 0.1577  0.0551  0.1014  83  ALA B N   
3564  C  CA  . ALA B 82  ? 0.4891 0.4373 0.8894 0.1597  0.0672  0.1097  83  ALA B CA  
3565  C  C   . ALA B 82  ? 0.5102 0.4584 0.9272 0.1432  0.0772  0.1122  83  ALA B C   
3566  O  O   . ALA B 82  ? 0.5709 0.5208 0.9911 0.1369  0.0823  0.1101  83  ALA B O   
3567  C  CB  . ALA B 82  ? 0.5233 0.4638 0.9062 0.1766  0.0745  0.1253  83  ALA B CB  
3568  N  N   . GLU B 83  ? 0.4894 0.4357 0.9177 0.1368  0.0789  0.1159  84  GLU B N   
3569  C  CA  . GLU B 83  ? 0.4442 0.3907 0.8904 0.1221  0.0864  0.1174  84  GLU B CA  
3570  C  C   . GLU B 83  ? 0.4313 0.3850 0.8875 0.1087  0.0811  0.1037  84  GLU B C   
3571  O  O   . GLU B 83  ? 0.4574 0.4124 0.9218 0.1001  0.0871  0.1035  84  GLU B O   
3572  C  CB  . GLU B 83  ? 0.4261 0.3694 0.8827 0.1193  0.0867  0.1216  84  GLU B CB  
3573  C  CG  . GLU B 83  ? 0.4832 0.4185 0.9326 0.1307  0.0946  0.1379  84  GLU B CG  
3574  C  CD  . GLU B 83  ? 0.5278 0.4596 0.9855 0.1300  0.0922  0.1408  84  GLU B CD  
3575  O  OE1 . GLU B 83  ? 0.4765 0.4124 0.9445 0.1217  0.0843  0.1296  84  GLU B OE1 
3576  O  OE2 . GLU B 83  ? 0.5544 0.4793 1.0079 0.1385  0.0989  0.1547  84  GLU B OE2 
3577  N  N   . LEU B 84  ? 0.4136 0.3724 0.8698 0.1073  0.0702  0.0930  85  LEU B N   
3578  C  CA  . LEU B 84  ? 0.4242 0.3898 0.8885 0.0958  0.0657  0.0813  85  LEU B CA  
3579  C  C   . LEU B 84  ? 0.4221 0.3894 0.8807 0.0958  0.0671  0.0785  85  LEU B C   
3580  O  O   . LEU B 84  ? 0.3918 0.3614 0.8579 0.0856  0.0701  0.0753  85  LEU B O   
3581  C  CB  . LEU B 84  ? 0.3781 0.3493 0.8435 0.0960  0.0549  0.0721  85  LEU B CB  
3582  C  CG  . LEU B 84  ? 0.3354 0.3136 0.8092 0.0848  0.0510  0.0616  85  LEU B CG  
3583  C  CD1 . LEU B 84  ? 0.4029 0.3807 0.8872 0.0735  0.0567  0.0616  85  LEU B CD1 
3584  C  CD2 . LEU B 84  ? 0.3400 0.3239 0.8181 0.0850  0.0425  0.0548  85  LEU B CD2 
3585  N  N   . GLU B 85  ? 0.4343 0.4003 0.8794 0.1081  0.0642  0.0793  86  GLU B N   
3586  C  CA  . GLU B 85  ? 0.5274 0.4944 0.9660 0.1104  0.0649  0.0761  86  GLU B CA  
3587  C  C   . GLU B 85  ? 0.5215 0.4853 0.9619 0.1073  0.0771  0.0841  86  GLU B C   
3588  O  O   . GLU B 85  ? 0.4776 0.4437 0.9211 0.1010  0.0788  0.0797  86  GLU B O   
3589  C  CB  . GLU B 85  ? 0.6142 0.5793 1.0371 0.1273  0.0598  0.0763  86  GLU B CB  
3590  C  CG  . GLU B 85  ? 0.6947 0.6637 1.1154 0.1286  0.0522  0.0652  86  GLU B CG  
3591  C  CD  . GLU B 85  ? 0.8003 0.7759 1.2295 0.1243  0.0392  0.0541  86  GLU B CD  
3592  O  OE1 . GLU B 85  ? 0.8224 0.7995 1.2566 0.1229  0.0361  0.0551  86  GLU B OE1 
3593  O  OE2 . GLU B 85  ? 0.7910 0.7703 1.2232 0.1223  0.0324  0.0445  86  GLU B OE2 
3594  N  N   . THR B 86  ? 0.5628 0.5213 1.0028 0.1117  0.0859  0.0963  87  THR B N   
3595  C  CA  . THR B 86  ? 0.4947 0.4508 0.9405 0.1085  0.0986  0.1055  87  THR B CA  
3596  C  C   . THR B 86  ? 0.5220 0.4819 0.9866 0.0918  0.0992  0.1004  87  THR B C   
3597  O  O   . THR B 86  ? 0.5614 0.5229 1.0311 0.0866  0.1043  0.1003  87  THR B O   
3598  C  CB  . THR B 86  ? 0.4905 0.4405 0.9356 0.1156  0.1080  0.1207  87  THR B CB  
3599  O  OG1 . THR B 86  ? 0.5193 0.4654 0.9439 0.1333  0.1102  0.1277  87  THR B OG1 
3600  C  CG2 . THR B 86  ? 0.4948 0.4441 0.9545 0.1086  0.1210  0.1298  87  THR B CG2 
3601  N  N   . ALA B 87  ? 0.3812 0.3427 0.8555 0.0844  0.0936  0.0959  88  ALA B N   
3602  C  CA  . ALA B 87  ? 0.3491 0.3146 0.8395 0.0705  0.0926  0.0898  88  ALA B CA  
3603  C  C   . ALA B 87  ? 0.3963 0.3665 0.8847 0.0649  0.0879  0.0800  88  ALA B C   
3604  O  O   . ALA B 87  ? 0.4932 0.4652 0.9897 0.0579  0.0916  0.0794  88  ALA B O   
3605  C  CB  . ALA B 87  ? 0.3179 0.2845 0.8154 0.0663  0.0863  0.0851  88  ALA B CB  
3606  N  N   . LEU B 88  ? 0.3463 0.3189 0.8256 0.0681  0.0796  0.0727  89  LEU B N   
3607  C  CA  . LEU B 88  ? 0.3489 0.3257 0.8269 0.0634  0.0749  0.0640  89  LEU B CA  
3608  C  C   . LEU B 88  ? 0.3443 0.3199 0.8182 0.0656  0.0805  0.0666  89  LEU B C   
3609  O  O   . LEU B 88  ? 0.3377 0.3156 0.8176 0.0576  0.0813  0.0631  89  LEU B O   
3610  C  CB  . LEU B 88  ? 0.3506 0.3299 0.8214 0.0687  0.0658  0.0575  89  LEU B CB  
3611  C  CG  . LEU B 88  ? 0.4036 0.3863 0.8802 0.0652  0.0595  0.0530  89  LEU B CG  
3612  C  CD1 . LEU B 88  ? 0.2933 0.2783 0.7645 0.0731  0.0513  0.0489  89  LEU B CD1 
3613  C  CD2 . LEU B 88  ? 0.4062 0.3931 0.8917 0.0539  0.0578  0.0466  89  LEU B CD2 
3614  N  N   . ARG B 89  ? 0.3135 0.2851 0.7765 0.0774  0.0846  0.0729  90  ARG B N   
3615  C  CA  . ARG B 89  ? 0.4370 0.4072 0.8945 0.0821  0.0912  0.0761  90  ARG B CA  
3616  C  C   . ARG B 89  ? 0.3506 0.3209 0.8210 0.0737  0.1002  0.0815  90  ARG B C   
3617  O  O   . ARG B 89  ? 0.3507 0.3229 0.8238 0.0694  0.1017  0.0785  90  ARG B O   
3618  C  CB  . ARG B 89  ? 0.5186 0.4840 0.9617 0.0982  0.0960  0.0843  90  ARG B CB  
3619  C  CG  . ARG B 89  ? 0.6803 0.6448 1.1119 0.1074  0.0992  0.0837  90  ARG B CG  
3620  C  CD  . ARG B 89  ? 0.7636 0.7233 1.1820 0.1233  0.1091  0.0958  90  ARG B CD  
3621  N  NE  . ARG B 89  ? 0.8243 0.7810 1.2342 0.1329  0.1054  0.0999  90  ARG B NE  
3622  C  CZ  . ARG B 89  ? 0.8597 0.8133 1.2738 0.1330  0.1122  0.1114  90  ARG B CZ  
3623  N  NH1 . ARG B 89  ? 0.8396 0.7930 1.2685 0.1239  0.1229  0.1196  90  ARG B NH1 
3624  N  NH2 . ARG B 89  ? 0.9056 0.8564 1.3107 0.1425  0.1078  0.1147  90  ARG B NH2 
3625  N  N   . ASP B 90  ? 0.3319 0.3006 0.8122 0.0713  0.1055  0.0892  91  ASP B N   
3626  C  CA  . ASP B 90  ? 0.4331 0.4026 0.9302 0.0634  0.1134  0.0944  91  ASP B CA  
3627  C  C   . ASP B 90  ? 0.3582 0.3324 0.8663 0.0509  0.1075  0.0848  91  ASP B C   
3628  O  O   . ASP B 90  ? 0.3637 0.3396 0.8782 0.0468  0.1111  0.0847  91  ASP B O   
3629  C  CB  . ASP B 90  ? 0.5191 0.4866 1.0283 0.0623  0.1181  0.1027  91  ASP B CB  
3630  C  CG  . ASP B 90  ? 0.6431 0.6053 1.1427 0.0751  0.1268  0.1155  91  ASP B CG  
3631  O  OD1 . ASP B 90  ? 0.6480 0.6085 1.1319 0.0852  0.1302  0.1182  91  ASP B OD1 
3632  O  OD2 . ASP B 90  ? 0.7222 0.6819 1.2296 0.0758  0.1302  0.1231  91  ASP B OD2 
3633  N  N   . SER B 91  ? 0.2591 0.2354 0.7688 0.0458  0.0987  0.0770  92  SER B N   
3634  C  CA  . SER B 91  ? 0.3246 0.3050 0.8428 0.0357  0.0933  0.0686  92  SER B CA  
3635  C  C   . SER B 91  ? 0.2921 0.2740 0.8027 0.0350  0.0909  0.0634  92  SER B C   
3636  O  O   . SER B 91  ? 0.3487 0.3325 0.8670 0.0292  0.0919  0.0617  92  SER B O   
3637  C  CB  . SER B 91  ? 0.3287 0.3108 0.8472 0.0326  0.0853  0.0619  92  SER B CB  
3638  O  OG  . SER B 91  ? 0.4586 0.4411 0.9642 0.0369  0.0798  0.0576  92  SER B OG  
3639  N  N   . SER B 92  ? 0.3175 0.2987 0.8144 0.0414  0.0871  0.0607  93  SER B N   
3640  C  CA  A SER B 92  ? 0.3387 0.3214 0.8296 0.0414  0.0839  0.0551  93  SER B CA  
3641  C  CA  B SER B 92  ? 0.3338 0.3164 0.8245 0.0415  0.0839  0.0551  93  SER B CA  
3642  C  C   . SER B 92  ? 0.3860 0.3672 0.8767 0.0438  0.0911  0.0592  93  SER B C   
3643  O  O   . SER B 92  ? 0.5210 0.5038 1.0136 0.0396  0.0898  0.0552  93  SER B O   
3644  C  CB  A SER B 92  ? 0.2855 0.2678 0.7648 0.0491  0.0782  0.0512  93  SER B CB  
3645  C  CB  B SER B 92  ? 0.3006 0.2828 0.7796 0.0495  0.0783  0.0515  93  SER B CB  
3646  O  OG  A SER B 92  ? 0.2796 0.2583 0.7491 0.0606  0.0825  0.0566  93  SER B OG  
3647  O  OG  B SER B 92  ? 0.3180 0.3011 0.7931 0.0499  0.0751  0.0458  93  SER B OG  
3648  N  N   . ARG B 93  ? 0.4558 0.4340 0.9444 0.0510  0.0994  0.0679  94  ARG B N   
3649  C  CA  . ARG B 93  ? 0.5066 0.4838 0.9955 0.0545  0.1080  0.0730  94  ARG B CA  
3650  C  C   . ARG B 93  ? 0.4647 0.4437 0.9718 0.0449  0.1126  0.0760  94  ARG B C   
3651  O  O   . ARG B 93  ? 0.4496 0.4292 0.9602 0.0443  0.1172  0.0772  94  ARG B O   
3652  C  CB  . ARG B 93  ? 0.6286 0.6022 1.1085 0.0671  0.1167  0.0827  94  ARG B CB  
3653  C  CG  . ARG B 93  ? 0.7113 0.6834 1.1727 0.0796  0.1149  0.0793  94  ARG B CG  
3654  C  CD  . ARG B 93  ? 0.8018 0.7702 1.2515 0.0946  0.1239  0.0895  94  ARG B CD  
3655  N  NE  . ARG B 93  ? 0.8573 0.8248 1.3188 0.0927  0.1365  0.1027  94  ARG B NE  
3656  C  CZ  . ARG B 93  ? 0.9109 0.8757 1.3741 0.0958  0.1405  0.1118  94  ARG B CZ  
3657  N  NH1 . ARG B 93  ? 0.9189 0.8818 1.3711 0.1015  0.1326  0.1089  94  ARG B NH1 
3658  N  NH2 . ARG B 93  ? 0.9021 0.8663 1.3796 0.0933  0.1524  0.1240  94  ARG B NH2 
3659  N  N   . VAL B 94  ? 0.3811 0.3614 0.9010 0.0379  0.1108  0.0765  95  VAL B N   
3660  C  CA  . VAL B 94  ? 0.3894 0.3724 0.9285 0.0284  0.1116  0.0759  95  VAL B CA  
3661  C  C   . VAL B 94  ? 0.3068 0.2921 0.8442 0.0225  0.1039  0.0665  95  VAL B C   
3662  O  O   . VAL B 94  ? 0.3232 0.3094 0.8681 0.0193  0.1060  0.0664  95  VAL B O   
3663  C  CB  . VAL B 94  ? 0.3179 0.3027 0.8712 0.0231  0.1092  0.0759  95  VAL B CB  
3664  C  CG1 . VAL B 94  ? 0.2558 0.2448 0.8280 0.0139  0.1061  0.0713  95  VAL B CG1 
3665  C  CG2 . VAL B 94  ? 0.2496 0.2323 0.8102 0.0277  0.1184  0.0869  95  VAL B CG2 
3666  N  N   . LEU B 95  ? 0.2989 0.2851 0.8272 0.0215  0.0955  0.0593  96  LEU B N   
3667  C  CA  . LEU B 95  ? 0.2934 0.2815 0.8195 0.0169  0.0887  0.0516  96  LEU B CA  
3668  C  C   . LEU B 95  ? 0.2649 0.2522 0.7850 0.0199  0.0911  0.0515  96  LEU B C   
3669  O  O   . LEU B 95  ? 0.3386 0.3268 0.8646 0.0156  0.0904  0.0495  96  LEU B O   
3670  C  CB  . LEU B 95  ? 0.2958 0.2847 0.8128 0.0174  0.0815  0.0461  96  LEU B CB  
3671  C  CG  . LEU B 95  ? 0.2903 0.2810 0.8054 0.0133  0.0754  0.0396  96  LEU B CG  
3672  C  CD1 . LEU B 95  ? 0.2495 0.2415 0.7750 0.0071  0.0740  0.0378  96  LEU B CD1 
3673  C  CD2 . LEU B 95  ? 0.2761 0.2677 0.7865 0.0136  0.0701  0.0360  96  LEU B CD2 
3674  N  N   . GLN B 96  ? 0.2997 0.2849 0.8078 0.0283  0.0934  0.0534  97  GLN B N   
3675  C  CA  . GLN B 96  ? 0.3760 0.3601 0.8763 0.0340  0.0958  0.0528  97  GLN B CA  
3676  C  C   . GLN B 96  ? 0.3091 0.2930 0.8181 0.0331  0.1036  0.0578  97  GLN B C   
3677  O  O   . GLN B 96  ? 0.3381 0.3225 0.8474 0.0319  0.1029  0.0547  97  GLN B O   
3678  C  CB  . GLN B 96  ? 0.5009 0.4825 0.9877 0.0456  0.0979  0.0549  97  GLN B CB  
3679  C  CG  . GLN B 96  ? 0.6704 0.6507 1.1466 0.0536  0.0978  0.0514  97  GLN B CG  
3680  C  CD  . GLN B 96  ? 0.7788 0.7572 1.2416 0.0639  0.0934  0.0481  97  GLN B CD  
3681  O  OE1 . GLN B 96  ? 0.8331 0.8124 1.2954 0.0612  0.0842  0.0416  97  GLN B OE1 
3682  N  NE2 . GLN B 96  ? 0.8439 0.8195 1.2966 0.0764  0.1001  0.0533  97  GLN B NE2 
3683  N  N   . ALA B 97  ? 0.3551 0.3382 0.8727 0.0336  0.1113  0.0660  98  ALA B N   
3684  C  CA  . ALA B 97  ? 0.2845 0.2675 0.8145 0.0324  0.1199  0.0723  98  ALA B CA  
3685  C  C   . ALA B 97  ? 0.3319 0.3167 0.8752 0.0225  0.1146  0.0673  98  ALA B C   
3686  O  O   . ALA B 97  ? 0.2836 0.2683 0.8299 0.0222  0.1168  0.0670  98  ALA B O   
3687  C  CB  . ALA B 97  ? 0.2750 0.2570 0.8166 0.0331  0.1283  0.0823  98  ALA B CB  
3688  N  N   . MET B 98  ? 0.2602 0.2467 0.8108 0.0154  0.1076  0.0631  99  MET B N   
3689  C  CA  . MET B 98  ? 0.2181 0.2063 0.7743 0.0094  0.1001  0.0567  99  MET B CA  
3690  C  C   . MET B 98  ? 0.3019 0.2903 0.8515 0.0085  0.0959  0.0514  99  MET B C   
3691  O  O   . MET B 98  ? 0.3080 0.2965 0.8603 0.0077  0.0950  0.0499  99  MET B O   
3692  C  CB  . MET B 98  ? 0.2118 0.2019 0.7652 0.0071  0.0914  0.0510  99  MET B CB  
3693  C  CG  . MET B 98  ? 0.2609 0.2524 0.8103 0.0045  0.0819  0.0429  99  MET B CG  
3694  S  SD  . MET B 98  ? 1.1237 1.1158 1.6606 0.0040  0.0762  0.0377  99  MET B SD  
3695  C  CE  . MET B 98  ? 0.3354 0.3290 0.8716 0.0020  0.0676  0.0310  99  MET B CE  
3696  N  N   . LEU B 99  ? 0.2742 0.2629 0.8113 0.0107  0.0921  0.0477  100 LEU B N   
3697  C  CA  . LEU B 99  ? 0.2778 0.2670 0.8078 0.0109  0.0873  0.0425  100 LEU B CA  
3698  C  C   . LEU B 99  ? 0.2705 0.2585 0.7985 0.0153  0.0924  0.0442  100 LEU B C   
3699  O  O   . LEU B 99  ? 0.2867 0.2752 0.8181 0.0130  0.0902  0.0415  100 LEU B O   
3700  C  CB  . LEU B 99  ? 0.2058 0.1951 0.7238 0.0137  0.0827  0.0388  100 LEU B CB  
3701  C  CG  . LEU B 99  ? 0.3048 0.2956 0.8240 0.0095  0.0769  0.0361  100 LEU B CG  
3702  C  CD1 . LEU B 99  ? 0.3124 0.3030 0.8223 0.0131  0.0739  0.0341  100 LEU B CD1 
3703  C  CD2 . LEU B 99  ? 0.3431 0.3354 0.8668 0.0044  0.0718  0.0324  100 LEU B CD2 
3704  N  N   . ALA B 100 ? 0.2960 0.2825 0.8181 0.0228  0.0996  0.0487  101 ALA B N   
3705  C  CA  . ALA B 100 ? 0.2805 0.2661 0.7996 0.0291  0.1059  0.0507  101 ALA B CA  
3706  C  C   . ALA B 100 ? 0.3576 0.3435 0.8920 0.0245  0.1102  0.0543  101 ALA B C   
3707  O  O   . ALA B 100 ? 0.3767 0.3630 0.9120 0.0256  0.1107  0.0524  101 ALA B O   
3708  C  CB  . ALA B 100 ? 0.2659 0.2499 0.7758 0.0394  0.1140  0.0563  101 ALA B CB  
3709  N  N   . THR B 101 ? 0.2789 0.2645 0.8270 0.0195  0.1125  0.0589  102 THR B N   
3710  C  CA  . THR B 101 ? 0.2753 0.2601 0.8414 0.0146  0.1152  0.0619  102 THR B CA  
3711  C  C   . THR B 101 ? 0.2874 0.2734 0.8557 0.0095  0.1056  0.0542  102 THR B C   
3712  O  O   . THR B 101 ? 0.3155 0.3010 0.8900 0.0096  0.1071  0.0543  102 THR B O   
3713  C  CB  . THR B 101 ? 0.2745 0.2591 0.8509 0.0120  0.1157  0.0654  102 THR B CB  
3714  O  OG1 . THR B 101 ? 0.3225 0.3050 0.9045 0.0160  0.1283  0.0761  102 THR B OG1 
3715  C  CG2 . THR B 101 ? 0.2590 0.2440 0.8452 0.0100  0.1123  0.0637  102 THR B CG2 
3716  N  N   . GLN B 102 ? 0.2290 0.2169 0.7887 0.0072  0.0956  0.0477  103 GLN B N   
3717  C  CA  . GLN B 102 ? 0.2314 0.2209 0.7880 0.0050  0.0864  0.0411  103 GLN B CA  
3718  C  C   . GLN B 102 ? 0.3138 0.3030 0.8700 0.0057  0.0877  0.0400  103 GLN B C   
3719  O  O   . GLN B 102 ? 0.2521 0.2418 0.8127 0.0051  0.0852  0.0381  103 GLN B O   
3720  C  CB  . GLN B 102 ? 0.3158 0.3070 0.8634 0.0036  0.0781  0.0362  103 GLN B CB  
3721  C  CG  . GLN B 102 ? 0.2920 0.2837 0.8419 0.0027  0.0758  0.0359  103 GLN B CG  
3722  C  CD  . GLN B 102 ? 0.3180 0.3104 0.8777 0.0014  0.0716  0.0336  103 GLN B CD  
3723  O  OE1 . GLN B 102 ? 0.2748 0.2679 0.8356 0.0007  0.0664  0.0299  103 GLN B OE1 
3724  N  NE2 . GLN B 102 ? 0.3892 0.3813 0.9582 0.0012  0.0736  0.0358  103 GLN B NE2 
3725  N  N   . LEU B 103 ? 0.2500 0.2389 0.7968 0.0093  0.0902  0.0401  104 LEU B N   
3726  C  CA  . LEU B 103 ? 0.2535 0.2424 0.7922 0.0139  0.0898  0.0371  104 LEU B CA  
3727  C  C   . LEU B 103 ? 0.2616 0.2500 0.8059 0.0170  0.0960  0.0397  104 LEU B C   
3728  O  O   . LEU B 103 ? 0.2942 0.2833 0.8424 0.0159  0.0931  0.0369  104 LEU B O   
3729  C  CB  . LEU B 103 ? 0.2712 0.2590 0.7958 0.0205  0.0909  0.0360  104 LEU B CB  
3730  C  CG  . LEU B 103 ? 0.3192 0.3057 0.8350 0.0261  0.0888  0.0311  104 LEU B CG  
3731  C  CD1 . LEU B 103 ? 0.2771 0.2646 0.7979 0.0208  0.0816  0.0271  104 LEU B CD1 
3732  C  CD2 . LEU B 103 ? 0.2840 0.2688 0.7881 0.0315  0.0864  0.0283  104 LEU B CD2 
3733  N  N   . ARG B 104 ? 0.3152 0.3029 0.8609 0.0213  0.1052  0.0456  105 ARG B N   
3734  C  CA  . ARG B 104 ? 0.3689 0.3568 0.9212 0.0251  0.1132  0.0495  105 ARG B CA  
3735  C  C   . ARG B 104 ? 0.3459 0.3338 0.9151 0.0182  0.1101  0.0492  105 ARG B C   
3736  O  O   . ARG B 104 ? 0.3645 0.3533 0.9367 0.0199  0.1103  0.0476  105 ARG B O   
3737  C  CB  . ARG B 104 ? 0.4012 0.3884 0.9557 0.0299  0.1246  0.0582  105 ARG B CB  
3738  C  CG  . ARG B 104 ? 0.5202 0.5085 1.0787 0.0364  0.1351  0.0632  105 ARG B CG  
3739  C  CD  . ARG B 104 ? 0.6577 0.6451 1.2279 0.0376  0.1465  0.0742  105 ARG B CD  
3740  N  NE  . ARG B 104 ? 0.7058 0.6904 1.2973 0.0273  0.1430  0.0761  105 ARG B NE  
3741  C  CZ  . ARG B 104 ? 0.7033 0.6852 1.3022 0.0226  0.1420  0.0792  105 ARG B CZ  
3742  N  NH1 . ARG B 104 ? 0.7415 0.7240 1.3283 0.0268  0.1448  0.0818  105 ARG B NH1 
3743  N  NH2 . ARG B 104 ? 0.7346 0.7147 1.3489 0.0161  0.1363  0.0780  105 ARG B NH2 
3744  N  N   . SER B 105 ? 0.3181 0.3047 0.8983 0.0113  0.1064  0.0501  106 SER B N   
3745  C  CA  . SER B 105 ? 0.4050 0.3918 0.9970 0.0074  0.1007  0.0479  106 SER B CA  
3746  C  C   . SER B 105 ? 0.2219 0.2104 0.8118 0.0060  0.0926  0.0417  106 SER B C   
3747  O  O   . SER B 105 ? 0.2250 0.2134 0.8247 0.0062  0.0936  0.0418  106 SER B O   
3748  C  CB  . SER B 105 ? 0.4562 0.4442 1.0465 0.0055  0.0935  0.0455  106 SER B CB  
3749  O  OG  . SER B 105 ? 0.5407 0.5271 1.1371 0.0067  0.1007  0.0517  106 SER B OG  
3750  N  N   . PHE B 106 ? 0.2149 0.2047 0.7933 0.0049  0.0852  0.0372  107 PHE B N   
3751  C  CA  . PHE B 106 ? 0.2108 0.2022 0.7879 0.0038  0.0777  0.0326  107 PHE B CA  
3752  C  C   . PHE B 106 ? 0.2162 0.2075 0.7926 0.0068  0.0812  0.0323  107 PHE B C   
3753  O  O   . PHE B 106 ? 0.2151 0.2071 0.7976 0.0068  0.0783  0.0307  107 PHE B O   
3754  C  CB  . PHE B 106 ? 0.2045 0.1971 0.7698 0.0029  0.0707  0.0293  107 PHE B CB  
3755  C  CG  . PHE B 106 ? 0.2688 0.2625 0.8334 0.0016  0.0641  0.0272  107 PHE B CG  
3756  C  CD1 . PHE B 106 ? 0.2017 0.1967 0.7710 0.0009  0.0568  0.0243  107 PHE B CD1 
3757  C  CD2 . PHE B 106 ? 0.2027 0.1962 0.7643 0.0014  0.0651  0.0280  107 PHE B CD2 
3758  C  CE1 . PHE B 106 ? 0.3380 0.3339 0.9100 0.0002  0.0507  0.0216  107 PHE B CE1 
3759  C  CE2 . PHE B 106 ? 0.2017 0.1961 0.7654 0.0004  0.0589  0.0252  107 PHE B CE2 
3760  C  CZ  . PHE B 106 ? 0.2010 0.1965 0.7703 -0.0001 0.0517  0.0217  107 PHE B CZ  
3761  N  N   . ASP B 107 ? 0.2185 0.2092 0.7833 0.0118  0.0862  0.0329  108 ASP B N   
3762  C  CA  . ASP B 107 ? 0.2552 0.2457 0.8135 0.0179  0.0884  0.0307  108 ASP B CA  
3763  C  C   . ASP B 107 ? 0.3395 0.3308 0.9077 0.0204  0.0941  0.0331  108 ASP B C   
3764  O  O   . ASP B 107 ? 0.3655 0.3574 0.9373 0.0213  0.0913  0.0305  108 ASP B O   
3765  C  CB  . ASP B 107 ? 0.3388 0.3279 0.8833 0.0247  0.0928  0.0304  108 ASP B CB  
3766  C  CG  . ASP B 107 ? 0.4206 0.4082 0.9569 0.0320  0.0929  0.0260  108 ASP B CG  
3767  O  OD1 . ASP B 107 ? 0.4734 0.4607 1.0124 0.0301  0.0868  0.0223  108 ASP B OD1 
3768  O  OD2 . ASP B 107 ? 0.4624 0.4488 0.9892 0.0406  0.0989  0.0261  108 ASP B OD2 
3769  N  N   . ASP B 108 ? 0.2378 0.2289 0.8116 0.0216  0.1023  0.0387  109 ASP B N   
3770  C  CA  . ASP B 108 ? 0.2706 0.2628 0.8564 0.0239  0.1093  0.0424  109 ASP B CA  
3771  C  C   . ASP B 108 ? 0.3076 0.3002 0.9089 0.0181  0.1025  0.0406  109 ASP B C   
3772  O  O   . ASP B 108 ? 0.2879 0.2820 0.8964 0.0205  0.1043  0.0403  109 ASP B O   
3773  C  CB  . ASP B 108 ? 0.3180 0.3094 0.9108 0.0249  0.1191  0.0502  109 ASP B CB  
3774  C  CG  . ASP B 108 ? 0.4334 0.4258 1.0125 0.0347  0.1293  0.0535  109 ASP B CG  
3775  O  OD1 . ASP B 108 ? 0.4508 0.4433 1.0137 0.0404  0.1268  0.0481  109 ASP B OD1 
3776  O  OD2 . ASP B 108 ? 0.4669 0.4594 1.0519 0.0375  0.1397  0.0616  109 ASP B OD2 
3777  N  N   . HIS B 109 ? 0.2322 0.2236 0.8383 0.0113  0.0944  0.0388  110 HIS B N   
3778  C  CA  . HIS B 109 ? 0.2780 0.2697 0.8976 0.0073  0.0867  0.0362  110 HIS B CA  
3779  C  C   . HIS B 109 ? 0.2867 0.2805 0.9014 0.0091  0.0808  0.0319  110 HIS B C   
3780  O  O   . HIS B 109 ? 0.2916 0.2867 0.9168 0.0099  0.0796  0.0312  110 HIS B O   
3781  C  CB  . HIS B 109 ? 0.2707 0.2625 0.8886 0.0036  0.0778  0.0335  110 HIS B CB  
3782  C  CG  . HIS B 109 ? 0.3122 0.3056 0.9405 0.0024  0.0688  0.0299  110 HIS B CG  
3783  N  ND1 . HIS B 109 ? 0.2988 0.2920 0.9447 0.0025  0.0705  0.0311  110 HIS B ND1 
3784  C  CD2 . HIS B 109 ? 0.3048 0.2998 0.9304 0.0014  0.0583  0.0253  110 HIS B CD2 
3785  C  CE1 . HIS B 109 ? 0.2294 0.2241 0.8832 0.0015  0.0603  0.0267  110 HIS B CE1 
3786  N  NE2 . HIS B 109 ? 0.2233 0.2191 0.8651 0.0009  0.0531  0.0233  110 HIS B NE2 
3787  N  N   . PHE B 110 ? 0.2278 0.2218 0.8283 0.0097  0.0771  0.0292  111 PHE B N   
3788  C  CA  . PHE B 110 ? 0.2872 0.2820 0.8842 0.0113  0.0715  0.0259  111 PHE B CA  
3789  C  C   . PHE B 110 ? 0.2319 0.2268 0.8291 0.0171  0.0769  0.0256  111 PHE B C   
3790  O  O   . PHE B 110 ? 0.2344 0.2303 0.8388 0.0181  0.0736  0.0241  111 PHE B O   
3791  C  CB  . PHE B 110 ? 0.2666 0.2606 0.8503 0.0111  0.0678  0.0240  111 PHE B CB  
3792  C  CG  . PHE B 110 ? 0.2969 0.2917 0.8801 0.0066  0.0622  0.0241  111 PHE B CG  
3793  C  CD1 . PHE B 110 ? 0.3084 0.3042 0.9012 0.0042  0.0565  0.0237  111 PHE B CD1 
3794  C  CD2 . PHE B 110 ? 0.2136 0.2079 0.7868 0.0059  0.0623  0.0240  111 PHE B CD2 
3795  C  CE1 . PHE B 110 ? 0.2330 0.2294 0.8238 0.0020  0.0513  0.0230  111 PHE B CE1 
3796  C  CE2 . PHE B 110 ? 0.2182 0.2134 0.7907 0.0027  0.0577  0.0240  111 PHE B CE2 
3797  C  CZ  . PHE B 110 ? 0.2428 0.2390 0.8213 0.0019  0.0521  0.0232  111 PHE B CZ  
3798  N  N   . GLN B 111 ? 0.2379 0.2320 0.8273 0.0218  0.0852  0.0268  112 GLN B N   
3799  C  CA  . GLN B 111 ? 0.2486 0.2433 0.8373 0.0291  0.0915  0.0263  112 GLN B CA  
3800  C  C   . GLN B 111 ? 0.4396 0.4368 1.0453 0.0287  0.0947  0.0291  112 GLN B C   
3801  O  O   . GLN B 111 ? 0.4134 0.4118 1.0234 0.0321  0.0943  0.0271  112 GLN B O   
3802  C  CB  . GLN B 111 ? 0.2568 0.2508 0.8341 0.0359  0.1006  0.0279  112 GLN B CB  
3803  C  CG  . GLN B 111 ? 0.2562 0.2472 0.8172 0.0384  0.0970  0.0238  112 GLN B CG  
3804  C  CD  . GLN B 111 ? 0.4759 0.4660 1.0244 0.0478  0.1054  0.0243  112 GLN B CD  
3805  O  OE1 . GLN B 111 ? 0.5345 0.5258 1.0818 0.0560  0.1126  0.0245  112 GLN B OE1 
3806  N  NE2 . GLN B 111 ? 0.5503 0.5388 1.0893 0.0477  0.1046  0.0244  112 GLN B NE2 
3807  N  N   . HIS B 112 ? 0.4351 0.4326 1.0517 0.0245  0.0974  0.0335  113 HIS B N   
3808  C  CA  . HIS B 112 ? 0.2550 0.2543 0.8911 0.0234  0.0999  0.0363  113 HIS B CA  
3809  C  C   . HIS B 112 ? 0.3602 0.3604 1.0060 0.0203  0.0895  0.0323  113 HIS B C   
3810  O  O   . HIS B 112 ? 0.2570 0.2595 0.9155 0.0222  0.0907  0.0326  113 HIS B O   
3811  C  CB  . HIS B 112 ? 0.2540 0.2514 0.9017 0.0187  0.1026  0.0410  113 HIS B CB  
3812  C  CG  . HIS B 112 ? 0.3810 0.3784 1.0261 0.0231  0.1155  0.0475  113 HIS B CG  
3813  N  ND1 . HIS B 112 ? 0.3919 0.3862 1.0393 0.0201  0.1186  0.0520  113 HIS B ND1 
3814  C  CD2 . HIS B 112 ? 0.3916 0.3917 1.0314 0.0313  0.1265  0.0505  113 HIS B CD2 
3815  C  CE1 . HIS B 112 ? 0.4086 0.4040 1.0524 0.0262  0.1312  0.0584  113 HIS B CE1 
3816  N  NE2 . HIS B 112 ? 0.4373 0.4366 1.0759 0.0334  0.1364  0.0575  113 HIS B NE2 
3817  N  N   . LEU B 113 ? 0.2428 0.2418 0.8827 0.0163  0.0797  0.0291  114 LEU B N   
3818  C  CA  . LEU B 113 ? 0.2734 0.2736 0.9207 0.0146  0.0695  0.0259  114 LEU B CA  
3819  C  C   . LEU B 113 ? 0.2449 0.2460 0.8882 0.0194  0.0688  0.0238  114 LEU B C   
3820  O  O   . LEU B 113 ? 0.3521 0.3551 1.0072 0.0208  0.0659  0.0230  114 LEU B O   
3821  C  CB  . LEU B 113 ? 0.2323 0.2315 0.8718 0.0110  0.0606  0.0239  114 LEU B CB  
3822  C  CG  . LEU B 113 ? 0.4287 0.4291 1.0797 0.0089  0.0505  0.0217  114 LEU B CG  
3823  C  CD1 . LEU B 113 ? 0.4592 0.4590 1.1265 0.0060  0.0515  0.0224  114 LEU B CD1 
3824  C  CD2 . LEU B 113 ? 0.4101 0.4103 1.0502 0.0077  0.0432  0.0202  114 LEU B CD2 
3825  N  N   . LEU B 114 ? 0.3901 0.3894 1.0178 0.0224  0.0709  0.0226  115 LEU B N   
3826  C  CA  . LEU B 114 ? 0.2512 0.2499 0.8753 0.0275  0.0701  0.0199  115 LEU B CA  
3827  C  C   . LEU B 114 ? 0.3996 0.4004 1.0319 0.0329  0.0778  0.0206  115 LEU B C   
3828  O  O   . LEU B 114 ? 0.2659 0.2680 0.9065 0.0352  0.0751  0.0191  115 LEU B O   
3829  C  CB  . LEU B 114 ? 0.2518 0.2471 0.8593 0.0302  0.0708  0.0176  115 LEU B CB  
3830  C  CG  . LEU B 114 ? 0.2779 0.2704 0.8817 0.0348  0.0675  0.0139  115 LEU B CG  
3831  C  CD1 . LEU B 114 ? 0.2728 0.2656 0.8844 0.0320  0.0585  0.0143  115 LEU B CD1 
3832  C  CD2 . LEU B 114 ? 0.2590 0.2472 0.8487 0.0365  0.0665  0.0110  115 LEU B CD2 
3833  N  N   . ASN B 115 ? 0.3363 0.3379 0.9664 0.0354  0.0878  0.0233  116 ASN B N   
3834  C  CA  . ASN B 115 ? 0.3800 0.3847 1.0172 0.0416  0.0973  0.0251  116 ASN B CA  
3835  C  C   . ASN B 115 ? 0.3694 0.3776 1.0284 0.0389  0.0961  0.0271  116 ASN B C   
3836  O  O   . ASN B 115 ? 0.3023 0.3132 0.9688 0.0438  0.0988  0.0264  116 ASN B O   
3837  C  CB  . ASN B 115 ? 0.4039 0.4093 1.0357 0.0448  0.1088  0.0295  116 ASN B CB  
3838  C  CG  . ASN B 115 ? 0.5026 0.5056 1.1136 0.0526  0.1124  0.0263  116 ASN B CG  
3839  O  OD1 . ASN B 115 ? 0.4860 0.4858 1.0874 0.0543  0.1055  0.0205  116 ASN B OD1 
3840  N  ND2 . ASN B 115 ? 0.5936 0.5978 1.1980 0.0578  0.1230  0.0301  116 ASN B ND2 
3841  N  N   . ASP B 116 ? 0.2706 0.2785 0.9405 0.0317  0.0915  0.0290  117 ASP B N   
3842  C  CA  . ASP B 116 ? 0.4632 0.4736 1.1554 0.0291  0.0884  0.0299  117 ASP B CA  
3843  C  C   . ASP B 116 ? 0.3887 0.3999 1.0844 0.0293  0.0773  0.0255  117 ASP B C   
3844  O  O   . ASP B 116 ? 0.3760 0.3904 1.0885 0.0305  0.0757  0.0251  117 ASP B O   
3845  C  CB  . ASP B 116 ? 0.4408 0.4492 1.1434 0.0224  0.0852  0.0318  117 ASP B CB  
3846  C  CG  . ASP B 116 ? 0.5407 0.5485 1.2486 0.0227  0.0973  0.0380  117 ASP B CG  
3847  O  OD1 . ASP B 116 ? 0.5883 0.5991 1.2980 0.0285  0.1083  0.0414  117 ASP B OD1 
3848  O  OD2 . ASP B 116 ? 0.5313 0.5356 1.2415 0.0180  0.0961  0.0396  117 ASP B OD2 
3849  N  N   . SER B 117 ? 0.3279 0.3365 1.0088 0.0284  0.0699  0.0226  118 SER B N   
3850  C  CA  . SER B 117 ? 0.3475 0.3562 1.0290 0.0302  0.0608  0.0196  118 SER B CA  
3851  C  C   . SER B 117 ? 0.3620 0.3719 1.0452 0.0369  0.0661  0.0186  118 SER B C   
3852  O  O   . SER B 117 ? 0.2810 0.2936 0.9778 0.0389  0.0628  0.0178  118 SER B O   
3853  C  CB  . SER B 117 ? 0.4079 0.4130 1.0727 0.0292  0.0546  0.0182  118 SER B CB  
3854  O  OG  . SER B 117 ? 0.2842 0.2881 0.9475 0.0327  0.0491  0.0164  118 SER B OG  
3855  N  N   . GLU B 118 ? 0.3484 0.3564 1.0180 0.0413  0.0739  0.0181  119 GLU B N   
3856  C  CA  . GLU B 118 ? 0.3361 0.3449 1.0050 0.0493  0.0791  0.0161  119 GLU B CA  
3857  C  C   . GLU B 118 ? 0.3734 0.3879 1.0599 0.0520  0.0864  0.0186  119 GLU B C   
3858  O  O   . GLU B 118 ? 0.4104 0.4270 1.1048 0.0568  0.0860  0.0168  119 GLU B O   
3859  C  CB  . GLU B 118 ? 0.3150 0.3207 0.9656 0.0548  0.0862  0.0143  119 GLU B CB  
3860  C  CG  . GLU B 118 ? 0.3598 0.3650 1.0070 0.0647  0.0905  0.0106  119 GLU B CG  
3861  C  CD  . GLU B 118 ? 0.4415 0.4430 1.0696 0.0718  0.0961  0.0074  119 GLU B CD  
3862  O  OE1 . GLU B 118 ? 0.4155 0.4159 1.0343 0.0691  0.0982  0.0091  119 GLU B OE1 
3863  O  OE2 . GLU B 118 ? 0.5744 0.5738 1.1966 0.0808  0.0978  0.0025  119 GLU B OE2 
3864  N  N   . ARG B 119 ? 0.2972 0.3142 0.9910 0.0491  0.0933  0.0231  120 ARG B N   
3865  C  CA  . ARG B 119 ? 0.3053 0.3278 1.0183 0.0512  0.1014  0.0267  120 ARG B CA  
3866  C  C   . ARG B 119 ? 0.3042 0.3293 1.0387 0.0476  0.0925  0.0258  120 ARG B C   
3867  O  O   . ARG B 119 ? 0.3128 0.3426 1.0621 0.0517  0.0960  0.0262  120 ARG B O   
3868  C  CB  . ARG B 119 ? 0.4931 0.5162 1.2104 0.0484  0.1105  0.0328  120 ARG B CB  
3869  C  CG  . ARG B 119 ? 0.5356 0.5615 1.2457 0.0568  0.1259  0.0365  120 ARG B CG  
3870  C  CD  . ARG B 119 ? 0.5528 0.5790 1.2691 0.0540  0.1351  0.0440  120 ARG B CD  
3871  N  NE  . ARG B 119 ? 0.5908 0.6116 1.2929 0.0489  0.1307  0.0436  120 ARG B NE  
3872  C  CZ  . ARG B 119 ? 0.5903 0.6098 1.2755 0.0528  0.1387  0.0462  120 ARG B CZ  
3873  N  NH1 . ARG B 119 ? 0.4836 0.4985 1.1578 0.0477  0.1337  0.0455  120 ARG B NH1 
3874  N  NH2 . ARG B 119 ? 0.6541 0.6773 1.3330 0.0627  0.1517  0.0492  120 ARG B NH2 
3875  N  N   . THR B 120 ? 0.2949 0.3173 1.0310 0.0409  0.0809  0.0242  121 THR B N   
3876  C  CA  . THR B 120 ? 0.2951 0.3196 1.0486 0.0389  0.0701  0.0220  121 THR B CA  
3877  C  C   . THR B 120 ? 0.4125 0.4379 1.1636 0.0447  0.0660  0.0189  121 THR B C   
3878  O  O   . THR B 120 ? 0.4168 0.4464 1.1854 0.0472  0.0645  0.0183  121 THR B O   
3879  C  CB  . THR B 120 ? 0.2860 0.3076 1.0365 0.0331  0.0576  0.0199  121 THR B CB  
3880  O  OG1 . THR B 120 ? 0.2827 0.3031 1.0400 0.0279  0.0602  0.0221  121 THR B OG1 
3881  C  CG2 . THR B 120 ? 0.2886 0.3126 1.0535 0.0334  0.0451  0.0167  121 THR B CG2 
3882  N  N   . LEU B 121 ? 0.2984 0.3195 1.0290 0.0469  0.0643  0.0169  122 LEU B N   
3883  C  CA  . LEU B 121 ? 0.3712 0.3910 1.0981 0.0525  0.0605  0.0141  122 LEU B CA  
3884  C  C   . LEU B 121 ? 0.3463 0.3701 1.0822 0.0596  0.0696  0.0139  122 LEU B C   
3885  O  O   . LEU B 121 ? 0.3225 0.3491 1.0715 0.0626  0.0656  0.0126  122 LEU B O   
3886  C  CB  . LEU B 121 ? 0.4043 0.4175 1.1089 0.0539  0.0595  0.0122  122 LEU B CB  
3887  C  CG  . LEU B 121 ? 0.3588 0.3684 1.0590 0.0596  0.0551  0.0093  122 LEU B CG  
3888  C  CD1 . LEU B 121 ? 0.3892 0.3924 1.0759 0.0569  0.0469  0.0090  122 LEU B CD1 
3889  C  CD2 . LEU B 121 ? 0.3905 0.3989 1.0835 0.0673  0.0645  0.0066  122 LEU B CD2 
3890  N  N   . GLN B 122 ? 0.3297 0.3544 1.0583 0.0631  0.0820  0.0152  123 GLN B N   
3891  C  CA  . GLN B 122 ? 0.3638 0.3932 1.0989 0.0713  0.0923  0.0153  123 GLN B CA  
3892  C  C   . GLN B 122 ? 0.4507 0.4875 1.2127 0.0699  0.0942  0.0184  123 GLN B C   
3893  O  O   . GLN B 122 ? 0.4466 0.4877 1.2197 0.0759  0.0966  0.0174  123 GLN B O   
3894  C  CB  . GLN B 122 ? 0.3384 0.3682 1.0603 0.0760  0.1057  0.0172  123 GLN B CB  
3895  C  CG  . GLN B 122 ? 0.5451 0.5677 1.2415 0.0791  0.1042  0.0130  123 GLN B CG  
3896  C  CD  . GLN B 122 ? 0.5465 0.5700 1.2296 0.0850  0.1168  0.0146  123 GLN B CD  
3897  O  OE1 . GLN B 122 ? 0.5830 0.6117 1.2748 0.0840  0.1261  0.0206  123 GLN B OE1 
3898  N  NE2 . GLN B 122 ? 0.6017 0.6197 1.2640 0.0917  0.1167  0.0093  123 GLN B NE2 
3899  N  N   . ALA B 123 ? 0.3864 0.4241 1.1596 0.0621  0.0926  0.0218  124 ALA B N   
3900  C  CA  . ALA B 123 ? 0.4627 0.5065 1.2637 0.0601  0.0944  0.0248  124 ALA B CA  
3901  C  C   . ALA B 123 ? 0.4877 0.5333 1.3047 0.0590  0.0811  0.0213  124 ALA B C   
3902  O  O   . ALA B 123 ? 0.3413 0.3928 1.1818 0.0603  0.0826  0.0223  124 ALA B O   
3903  C  CB  . ALA B 123 ? 0.3278 0.3702 1.1364 0.0526  0.0959  0.0288  124 ALA B CB  
3904  N  N   . THR B 124 ? 0.4566 0.4974 1.2617 0.0571  0.0683  0.0175  125 THR B N   
3905  C  CA  . THR B 124 ? 0.4524 0.4947 1.2713 0.0566  0.0547  0.0147  125 THR B CA  
3906  C  C   . THR B 124 ? 0.4222 0.4624 1.2320 0.0625  0.0483  0.0117  125 THR B C   
3907  O  O   . THR B 124 ? 0.3370 0.3790 1.1585 0.0638  0.0378  0.0098  125 THR B O   
3908  C  CB  . THR B 124 ? 0.3200 0.3594 1.1375 0.0501  0.0425  0.0134  125 THR B CB  
3909  O  OG1 . THR B 124 ? 0.4339 0.4673 1.2270 0.0501  0.0373  0.0123  125 THR B OG1 
3910  C  CG2 . THR B 124 ? 0.4186 0.4575 1.2420 0.0441  0.0482  0.0160  125 THR B CG2 
3911  N  N   . PHE B 125 ? 0.4281 0.4639 1.2179 0.0664  0.0539  0.0110  126 PHE B N   
3912  C  CA  . PHE B 125 ? 0.4737 0.5053 1.2548 0.0717  0.0475  0.0083  126 PHE B CA  
3913  C  C   . PHE B 125 ? 0.5139 0.5496 1.3083 0.0794  0.0504  0.0068  126 PHE B C   
3914  O  O   . PHE B 125 ? 0.4883 0.5226 1.2868 0.0823  0.0410  0.0053  126 PHE B O   
3915  C  CB  . PHE B 125 ? 0.4379 0.4621 1.1945 0.0733  0.0510  0.0072  126 PHE B CB  
3916  C  CG  . PHE B 125 ? 0.4633 0.4812 1.2063 0.0686  0.0412  0.0076  126 PHE B CG  
3917  C  CD1 . PHE B 125 ? 0.4625 0.4821 1.2111 0.0629  0.0330  0.0092  126 PHE B CD1 
3918  C  CD2 . PHE B 125 ? 0.4873 0.4975 1.2126 0.0707  0.0399  0.0062  126 PHE B CD2 
3919  C  CE1 . PHE B 125 ? 0.4623 0.4769 1.1979 0.0600  0.0248  0.0101  126 PHE B CE1 
3920  C  CE2 . PHE B 125 ? 0.4519 0.4570 1.1664 0.0667  0.0320  0.0077  126 PHE B CE2 
3921  C  CZ  . PHE B 125 ? 0.4670 0.4746 1.1859 0.0617  0.0249  0.0100  126 PHE B CZ  
3922  N  N   . PRO B 126 ? 0.6058 0.6467 1.4063 0.0835  0.0636  0.0076  127 PRO B N   
3923  C  CA  . PRO B 126 ? 0.6398 0.6854 1.4540 0.0914  0.0663  0.0060  127 PRO B CA  
3924  C  C   . PRO B 126 ? 0.5788 0.6299 1.4175 0.0898  0.0568  0.0062  127 PRO B C   
3925  O  O   . PRO B 126 ? 0.6210 0.6722 1.4655 0.0955  0.0517  0.0040  127 PRO B O   
3926  C  CB  . PRO B 126 ? 0.6616 0.7138 1.4809 0.0951  0.0827  0.0084  127 PRO B CB  
3927  C  CG  . PRO B 126 ? 0.6492 0.6963 1.4465 0.0929  0.0884  0.0093  127 PRO B CG  
3928  C  CD  . PRO B 126 ? 0.6264 0.6685 1.4189 0.0832  0.0769  0.0099  127 PRO B CD  
3929  N  N   . GLY B 127 ? 0.4958 0.5505 1.3487 0.0827  0.0538  0.0083  128 GLY B N   
3930  C  CA  . GLY B 127 ? 0.3703 0.4300 1.2468 0.0815  0.0433  0.0075  128 GLY B CA  
3931  C  C   . GLY B 127 ? 0.5433 0.5979 1.4117 0.0815  0.0269  0.0051  128 GLY B C   
3932  O  O   . GLY B 127 ? 0.5707 0.6286 1.4549 0.0836  0.0168  0.0036  128 GLY B O   
3933  N  N   . ALA B 128 ? 0.5313 0.5778 1.3749 0.0797  0.0246  0.0053  129 ALA B N   
3934  C  CA  . ALA B 128 ? 0.5304 0.5714 1.3635 0.0799  0.0104  0.0047  129 ALA B CA  
3935  C  C   . ALA B 128 ? 0.3693 0.4052 1.1938 0.0869  0.0077  0.0041  129 ALA B C   
3936  O  O   . ALA B 128 ? 0.3765 0.4122 1.2073 0.0908  -0.0031 0.0038  129 ALA B O   
3937  C  CB  . ALA B 128 ? 0.3495 0.3847 1.1621 0.0745  0.0098  0.0060  129 ALA B CB  
3938  N  N   . PHE B 129 ? 0.3699 0.4009 1.1794 0.0889  0.0169  0.0037  130 PHE B N   
3939  C  CA  . PHE B 129 ? 0.5601 0.5833 1.3583 0.0946  0.0141  0.0028  130 PHE B CA  
3940  C  C   . PHE B 129 ? 0.3885 0.4136 1.1920 0.1018  0.0237  0.0000  130 PHE B C   
3941  O  O   . PHE B 129 ? 0.4654 0.4842 1.2631 0.1077  0.0219  -0.0017 130 PHE B O   
3942  C  CB  . PHE B 129 ? 0.3714 0.3855 1.1463 0.0914  0.0145  0.0037  130 PHE B CB  
3943  C  CG  . PHE B 129 ? 0.3612 0.3744 1.1298 0.0850  0.0070  0.0065  130 PHE B CG  
3944  C  CD1 . PHE B 129 ? 0.3648 0.3763 1.1351 0.0865  -0.0055 0.0087  130 PHE B CD1 
3945  C  CD2 . PHE B 129 ? 0.4882 0.5022 1.2486 0.0788  0.0123  0.0071  130 PHE B CD2 
3946  C  CE1 . PHE B 129 ? 0.4394 0.4502 1.2025 0.0824  -0.0123 0.0109  130 PHE B CE1 
3947  C  CE2 . PHE B 129 ? 0.4224 0.4356 1.1770 0.0738  0.0054  0.0092  130 PHE B CE2 
3948  C  CZ  . PHE B 129 ? 0.3458 0.3576 1.1014 0.0759  -0.0069 0.0109  130 PHE B CZ  
3949  N  N   . GLY B 130 ? 0.5345 0.5679 1.3494 0.1017  0.0339  -0.0001 131 GLY B N   
3950  C  CA  . GLY B 130 ? 0.6068 0.6437 1.4272 0.1098  0.0442  -0.0024 131 GLY B CA  
3951  C  C   . GLY B 130 ? 0.6010 0.6303 1.3998 0.1146  0.0513  -0.0053 131 GLY B C   
3952  O  O   . GLY B 130 ? 0.3971 0.4236 1.1808 0.1110  0.0562  -0.0049 131 GLY B O   
3953  N  N   . GLU B 131 ? 0.6295 0.6550 1.4272 0.1233  0.0511  -0.0090 132 GLU B N   
3954  C  CA  . GLU B 131 ? 0.7212 0.7388 1.4999 0.1296  0.0565  -0.0135 132 GLU B CA  
3955  C  C   . GLU B 131 ? 0.6699 0.6746 1.4329 0.1266  0.0467  -0.0144 132 GLU B C   
3956  O  O   . GLU B 131 ? 0.7427 0.7388 1.4903 0.1310  0.0487  -0.0188 132 GLU B O   
3957  C  CB  . GLU B 131 ? 0.8638 0.8831 1.6487 0.1416  0.0618  -0.0179 132 GLU B CB  
3958  C  CG  . GLU B 131 ? 0.9863 1.0191 1.7855 0.1453  0.0743  -0.0164 132 GLU B CG  
3959  C  CD  . GLU B 131 ? 1.0961 1.1336 1.9076 0.1566  0.0785  -0.0195 132 GLU B CD  
3960  O  OE1 . GLU B 131 ? 1.1400 1.1816 1.9708 0.1561  0.0717  -0.0181 132 GLU B OE1 
3961  O  OE2 . GLU B 131 ? 1.1524 1.1902 1.9541 0.1668  0.0888  -0.0236 132 GLU B OE2 
3962  N  N   . LEU B 132 ? 0.5462 0.5496 1.3133 0.1196  0.0361  -0.0102 133 LEU B N   
3963  C  CA  . LEU B 132 ? 0.4098 0.4029 1.1618 0.1148  0.0288  -0.0089 133 LEU B CA  
3964  C  C   . LEU B 132 ? 0.5388 0.5316 1.2765 0.1099  0.0354  -0.0091 133 LEU B C   
3965  O  O   . LEU B 132 ? 0.5380 0.5219 1.2605 0.1094  0.0348  -0.0111 133 LEU B O   
3966  C  CB  . LEU B 132 ? 0.4032 0.3967 1.1610 0.1093  0.0175  -0.0035 133 LEU B CB  
3967  C  CG  . LEU B 132 ? 0.5366 0.5300 1.3076 0.1140  0.0088  -0.0022 133 LEU B CG  
3968  C  CD1 . LEU B 132 ? 0.5457 0.5360 1.3139 0.1101  -0.0025 0.0032  133 LEU B CD1 
3969  C  CD2 . LEU B 132 ? 0.5668 0.5515 1.3352 0.1217  0.0087  -0.0055 133 LEU B CD2 
3970  N  N   . TYR B 133 ? 0.4802 0.4825 1.2243 0.1063  0.0415  -0.0070 134 TYR B N   
3971  C  CA  . TYR B 133 ? 0.4676 0.4704 1.1993 0.1025  0.0489  -0.0068 134 TYR B CA  
3972  C  C   . TYR B 133 ? 0.4266 0.4312 1.1525 0.1105  0.0611  -0.0107 134 TYR B C   
3973  O  O   . TYR B 133 ? 0.4384 0.4368 1.1470 0.1125  0.0641  -0.0138 134 TYR B O   
3974  C  CB  . TYR B 133 ? 0.5195 0.5304 1.2604 0.0947  0.0497  -0.0023 134 TYR B CB  
3975  C  CG  . TYR B 133 ? 0.5025 0.5160 1.2350 0.0931  0.0605  -0.0016 134 TYR B CG  
3976  C  CD1 . TYR B 133 ? 0.5256 0.5331 1.2401 0.0893  0.0603  -0.0019 134 TYR B CD1 
3977  C  CD2 . TYR B 133 ? 0.5373 0.5593 1.2805 0.0958  0.0713  -0.0003 134 TYR B CD2 
3978  C  CE1 . TYR B 133 ? 0.5560 0.5656 1.2623 0.0886  0.0698  -0.0011 134 TYR B CE1 
3979  C  CE2 . TYR B 133 ? 0.5393 0.5634 1.2745 0.0952  0.0817  0.0014  134 TYR B CE2 
3980  C  CZ  . TYR B 133 ? 0.5215 0.5392 1.2375 0.0918  0.0806  0.0008  134 TYR B CZ  
3981  O  OH  . TYR B 133 ? 0.4678 0.4874 1.1753 0.0920  0.0906  0.0027  134 TYR B OH  
3982  N  N   . THR B 134 ? 0.3998 0.4131 1.1399 0.1159  0.0682  -0.0105 135 THR B N   
3983  C  CA  . THR B 134 ? 0.6417 0.6587 1.3754 0.1241  0.0817  -0.0128 135 THR B CA  
3984  C  C   . THR B 134 ? 0.6320 0.6405 1.3501 0.1348  0.0827  -0.0202 135 THR B C   
3985  O  O   . THR B 134 ? 0.6815 0.6907 1.3876 0.1428  0.0925  -0.0233 135 THR B O   
3986  C  CB  . THR B 134 ? 0.4163 0.4455 1.1703 0.1284  0.0904  -0.0103 135 THR B CB  
3987  O  OG1 . THR B 134 ? 0.4229 0.4529 1.1920 0.1313  0.0834  -0.0116 135 THR B OG1 
3988  C  CG2 . THR B 134 ? 0.5710 0.6081 1.3389 0.1189  0.0925  -0.0037 135 THR B CG2 
3989  N  N   . GLN B 135 ? 0.6328 0.6327 1.3508 0.1356  0.0724  -0.0231 136 GLN B N   
3990  C  CA  . GLN B 135 ? 0.6414 0.6307 1.3452 0.1446  0.0712  -0.0307 136 GLN B CA  
3991  C  C   . GLN B 135 ? 0.6547 0.6335 1.3413 0.1392  0.0657  -0.0324 136 GLN B C   
3992  O  O   . GLN B 135 ? 0.6833 0.6523 1.3565 0.1458  0.0646  -0.0394 136 GLN B O   
3993  C  CB  . GLN B 135 ? 0.6441 0.6282 1.3577 0.1486  0.0632  -0.0330 136 GLN B CB  
3994  N  N   . ASN B 136 ? 0.6556 0.6363 1.3432 0.1276  0.0619  -0.0263 137 ASN B N   
3995  C  CA  . ASN B 136 ? 0.6236 0.5957 1.2977 0.1214  0.0564  -0.0267 137 ASN B CA  
3996  C  C   . ASN B 136 ? 0.6383 0.6155 1.3048 0.1155  0.0620  -0.0235 137 ASN B C   
3997  O  O   . ASN B 136 ? 0.6839 0.6570 1.3436 0.1077  0.0569  -0.0215 137 ASN B O   
3998  C  CB  . ASN B 136 ? 0.5675 0.5352 1.2483 0.1134  0.0449  -0.0222 137 ASN B CB  
3999  C  CG  . ASN B 136 ? 0.5186 0.4797 1.2064 0.1190  0.0388  -0.0247 137 ASN B CG  
4000  O  OD1 . ASN B 136 ? 0.4368 0.3899 1.1180 0.1265  0.0391  -0.0315 137 ASN B OD1 
4001  N  ND2 . ASN B 136 ? 0.5287 0.4927 1.2298 0.1162  0.0327  -0.0196 137 ASN B ND2 
4002  N  N   . ALA B 137 ? 0.6118 0.5979 1.2803 0.1195  0.0728  -0.0225 138 ALA B N   
4003  C  CA  . ALA B 137 ? 0.5147 0.5060 1.1781 0.1143  0.0790  -0.0185 138 ALA B CA  
4004  C  C   . ALA B 137 ? 0.5790 0.5626 1.2221 0.1152  0.0789  -0.0224 138 ALA B C   
4005  O  O   . ALA B 137 ? 0.5794 0.5634 1.2177 0.1072  0.0780  -0.0188 138 ALA B O   
4006  C  CB  . ALA B 137 ? 0.4790 0.4806 1.1485 0.1204  0.0919  -0.0165 138 ALA B CB  
4007  N  N   . ARG B 138 ? 0.5201 0.4965 1.1519 0.1256  0.0793  -0.0302 139 ARG B N   
4008  C  CA  . ARG B 138 ? 0.5326 0.5009 1.1457 0.1283  0.0782  -0.0357 139 ARG B CA  
4009  C  C   . ARG B 138 ? 0.5372 0.4986 1.1492 0.1171  0.0675  -0.0340 139 ARG B C   
4010  O  O   . ARG B 138 ? 0.5598 0.5192 1.1613 0.1136  0.0674  -0.0341 139 ARG B O   
4011  C  CB  . ARG B 138 ? 0.4846 0.4446 1.0877 0.1419  0.0778  -0.0458 139 ARG B CB  
4012  N  N   . ALA B 139 ? 0.4886 0.4470 1.1119 0.1120  0.0590  -0.0320 140 ALA B N   
4013  C  CA  . ALA B 139 ? 0.4688 0.4219 1.0928 0.1020  0.0497  -0.0289 140 ALA B CA  
4014  C  C   . ALA B 139 ? 0.4478 0.4080 1.0724 0.0923  0.0511  -0.0218 140 ALA B C   
4015  O  O   . ALA B 139 ? 0.4443 0.4016 1.0605 0.0875  0.0492  -0.0216 140 ALA B O   
4016  C  CB  . ALA B 139 ? 0.4875 0.4378 1.1242 0.0999  0.0419  -0.0263 140 ALA B CB  
4017  N  N   . PHE B 140 ? 0.4405 0.4097 1.0760 0.0895  0.0541  -0.0164 141 PHE B N   
4018  C  CA  . PHE B 140 ? 0.4485 0.4241 1.0862 0.0809  0.0550  -0.0102 141 PHE B CA  
4019  C  C   . PHE B 140 ? 0.3935 0.3707 1.0195 0.0815  0.0626  -0.0110 141 PHE B C   
4020  O  O   . PHE B 140 ? 0.4531 0.4301 1.0737 0.0747  0.0608  -0.0084 141 PHE B O   
4021  C  CB  . PHE B 140 ? 0.4350 0.4194 1.0882 0.0795  0.0568  -0.0059 141 PHE B CB  
4022  C  CG  . PHE B 140 ? 0.4317 0.4151 1.0964 0.0790  0.0485  -0.0045 141 PHE B CG  
4023  C  CD1 . PHE B 140 ? 0.3330 0.3159 1.0005 0.0723  0.0402  -0.0001 141 PHE B CD1 
4024  C  CD2 . PHE B 140 ? 0.3549 0.3380 1.0270 0.0865  0.0491  -0.0074 141 PHE B CD2 
4025  C  CE1 . PHE B 140 ? 0.3374 0.3192 1.0141 0.0733  0.0324  0.0018  141 PHE B CE1 
4026  C  CE2 . PHE B 140 ? 0.3583 0.3402 1.0408 0.0867  0.0412  -0.0057 141 PHE B CE2 
4027  C  CZ  . PHE B 140 ? 0.3498 0.3310 1.0343 0.0802  0.0327  -0.0009 141 PHE B CZ  
4028  N  N   . ARG B 141 ? 0.4095 0.3884 1.0311 0.0905  0.0712  -0.0144 142 ARG B N   
4029  C  CA  . ARG B 141 ? 0.4582 0.4383 1.0672 0.0937  0.0792  -0.0151 142 ARG B CA  
4030  C  C   . ARG B 141 ? 0.5037 0.4755 1.0983 0.0926  0.0739  -0.0193 142 ARG B C   
4031  O  O   . ARG B 141 ? 0.5061 0.4789 1.0945 0.0876  0.0749  -0.0167 142 ARG B O   
4032  C  CB  . ARG B 141 ? 0.6034 0.5858 1.2080 0.1067  0.0890  -0.0188 142 ARG B CB  
4033  C  CG  . ARG B 141 ? 0.6877 0.6790 1.2931 0.1084  0.1011  -0.0135 142 ARG B CG  
4034  C  CD  . ARG B 141 ? 0.7929 0.7915 1.4084 0.1166  0.1101  -0.0125 142 ARG B CD  
4035  N  NE  . ARG B 141 ? 0.8623 0.8656 1.4990 0.1094  0.1061  -0.0082 142 ARG B NE  
4036  C  CZ  . ARG B 141 ? 0.9069 0.9178 1.5581 0.1136  0.1125  -0.0059 142 ARG B CZ  
4037  N  NH1 . ARG B 141 ? 0.9320 0.9475 1.5785 0.1252  0.1244  -0.0069 142 ARG B NH1 
4038  N  NH2 . ARG B 141 ? 0.9085 0.9230 1.5792 0.1069  0.1071  -0.0028 142 ARG B NH2 
4039  N  N   . ASP B 142 ? 0.4501 0.4133 1.0410 0.0972  0.0677  -0.0258 143 ASP B N   
4040  C  CA  . ASP B 142 ? 0.5032 0.4577 1.0838 0.0960  0.0612  -0.0305 143 ASP B CA  
4041  C  C   . ASP B 142 ? 0.3474 0.3026 0.9328 0.0835  0.0550  -0.0245 143 ASP B C   
4042  O  O   . ASP B 142 ? 0.3424 0.2956 0.9198 0.0803  0.0537  -0.0251 143 ASP B O   
4043  C  CB  . ASP B 142 ? 0.5964 0.5411 1.1769 0.1019  0.0546  -0.0380 143 ASP B CB  
4044  C  CG  . ASP B 142 ? 0.6209 0.5635 1.1929 0.1164  0.0603  -0.0458 143 ASP B CG  
4045  O  OD1 . ASP B 142 ? 0.6334 0.5797 1.1942 0.1231  0.0685  -0.0471 143 ASP B OD1 
4046  O  OD2 . ASP B 142 ? 0.6775 0.6150 1.2537 0.1220  0.0570  -0.0505 143 ASP B OD2 
4047  N  N   . LEU B 143 ? 0.3393 0.2978 0.9373 0.0773  0.0513  -0.0188 144 LEU B N   
4048  C  CA  . LEU B 143 ? 0.3246 0.2847 0.9264 0.0671  0.0460  -0.0128 144 LEU B CA  
4049  C  C   . LEU B 143 ? 0.4469 0.4133 1.0448 0.0624  0.0509  -0.0088 144 LEU B C   
4050  O  O   . LEU B 143 ? 0.3894 0.3549 0.9825 0.0570  0.0483  -0.0073 144 LEU B O   
4051  C  CB  . LEU B 143 ? 0.3212 0.2839 0.9358 0.0639  0.0414  -0.0076 144 LEU B CB  
4052  C  CG  . LEU B 143 ? 0.4185 0.3838 1.0357 0.0555  0.0367  -0.0010 144 LEU B CG  
4053  C  CD1 . LEU B 143 ? 0.3073 0.2667 0.9195 0.0524  0.0323  -0.0011 144 LEU B CD1 
4054  C  CD2 . LEU B 143 ? 0.3086 0.2756 0.9365 0.0547  0.0317  0.0035  144 LEU B CD2 
4055  N  N   . TYR B 144 ? 0.3113 0.2842 0.9124 0.0642  0.0580  -0.0069 145 TYR B N   
4056  C  CA  . TYR B 144 ? 0.3766 0.3547 0.9752 0.0600  0.0629  -0.0029 145 TYR B CA  
4057  C  C   . TYR B 144 ? 0.4293 0.4041 1.0133 0.0633  0.0666  -0.0063 145 TYR B C   
4058  O  O   . TYR B 144 ? 0.3223 0.2985 0.9019 0.0582  0.0668  -0.0037 145 TYR B O   
4059  C  CB  . TYR B 144 ? 0.3821 0.3672 0.9896 0.0616  0.0703  0.0001  145 TYR B CB  
4060  C  CG  . TYR B 144 ? 0.3804 0.3700 1.0026 0.0552  0.0658  0.0046  145 TYR B CG  
4061  C  CD1 . TYR B 144 ? 0.3478 0.3375 0.9801 0.0571  0.0611  0.0040  145 TYR B CD1 
4062  C  CD2 . TYR B 144 ? 0.3988 0.3919 1.0245 0.0482  0.0654  0.0088  145 TYR B CD2 
4063  C  CE1 . TYR B 144 ? 0.3650 0.3585 1.0100 0.0526  0.0559  0.0074  145 TYR B CE1 
4064  C  CE2 . TYR B 144 ? 0.3882 0.3846 1.0266 0.0437  0.0599  0.0115  145 TYR B CE2 
4065  C  CZ  . TYR B 144 ? 0.3737 0.3705 1.0215 0.0462  0.0550  0.0107  145 TYR B CZ  
4066  O  OH  . TYR B 144 ? 0.4016 0.4015 1.0614 0.0431  0.0484  0.0127  145 TYR B OH  
4067  N  N   . SER B 145 ? 0.4743 0.4446 1.0504 0.0729  0.0688  -0.0126 146 SER B N   
4068  C  CA  . SER B 145 ? 0.4696 0.4356 1.0307 0.0782  0.0706  -0.0173 146 SER B CA  
4069  C  C   . SER B 145 ? 0.4525 0.4134 1.0108 0.0718  0.0620  -0.0187 146 SER B C   
4070  O  O   . SER B 145 ? 0.5179 0.4790 1.0688 0.0698  0.0628  -0.0182 146 SER B O   
4071  C  CB  . SER B 145 ? 0.3465 0.3074 0.8995 0.0912  0.0726  -0.0255 146 SER B CB  
4072  O  OG  . SER B 145 ? 0.4868 0.4537 1.0438 0.0977  0.0813  -0.0237 146 SER B OG  
4073  N  N   . GLU B 146 ? 0.4176 0.3743 0.9831 0.0687  0.0541  -0.0199 147 GLU B N   
4074  C  CA  . GLU B 146 ? 0.5000 0.4523 1.0659 0.0628  0.0464  -0.0204 147 GLU B CA  
4075  C  C   . GLU B 146 ? 0.4948 0.4535 1.0652 0.0529  0.0459  -0.0125 147 GLU B C   
4076  O  O   . GLU B 146 ? 0.4091 0.3667 0.9774 0.0485  0.0427  -0.0120 147 GLU B O   
4077  C  CB  . GLU B 146 ? 0.5442 0.4905 1.1185 0.0627  0.0391  -0.0226 147 GLU B CB  
4078  C  CG  . GLU B 146 ? 0.6951 0.6332 1.2674 0.0632  0.0323  -0.0287 147 GLU B CG  
4079  C  CD  . GLU B 146 ? 0.8129 0.7439 1.3747 0.0742  0.0326  -0.0394 147 GLU B CD  
4080  O  OE1 . GLU B 146 ? 0.8549 0.7881 1.4102 0.0822  0.0395  -0.0412 147 GLU B OE1 
4081  O  OE2 . GLU B 146 ? 0.8453 0.7688 1.4059 0.0754  0.0260  -0.0461 147 GLU B OE2 
4082  N  N   . LEU B 147 ? 0.4330 0.3980 1.0099 0.0500  0.0488  -0.0069 148 LEU B N   
4083  C  CA  . LEU B 147 ? 0.4146 0.3853 0.9941 0.0423  0.0487  -0.0006 148 LEU B CA  
4084  C  C   . LEU B 147 ? 0.4003 0.3730 0.9710 0.0422  0.0539  -0.0006 148 LEU B C   
4085  O  O   . LEU B 147 ? 0.2625 0.2365 0.8310 0.0370  0.0522  0.0017  148 LEU B O   
4086  C  CB  . LEU B 147 ? 0.4387 0.4148 1.0277 0.0404  0.0496  0.0039  148 LEU B CB  
4087  C  CG  . LEU B 147 ? 0.3964 0.3715 0.9945 0.0398  0.0433  0.0058  148 LEU B CG  
4088  C  CD1 . LEU B 147 ? 0.4295 0.4101 1.0366 0.0380  0.0431  0.0096  148 LEU B CD1 
4089  C  CD2 . LEU B 147 ? 0.2988 0.2715 0.8964 0.0357  0.0374  0.0085  148 LEU B CD2 
4090  N  N   . ARG B 148 ? 0.3531 0.3261 0.9188 0.0487  0.0608  -0.0029 149 ARG B N   
4091  C  CA  . ARG B 148 ? 0.3953 0.3693 0.9516 0.0505  0.0665  -0.0026 149 ARG B CA  
4092  C  C   . ARG B 148 ? 0.3791 0.3479 0.9259 0.0518  0.0624  -0.0071 149 ARG B C   
4093  O  O   . ARG B 148 ? 0.3752 0.3454 0.9177 0.0485  0.0629  -0.0052 149 ARG B O   
4094  C  CB  . ARG B 148 ? 0.4081 0.3833 0.9602 0.0597  0.0755  -0.0038 149 ARG B CB  
4095  C  CG  . ARG B 148 ? 0.2878 0.2694 0.8513 0.0578  0.0812  0.0018  149 ARG B CG  
4096  C  CD  . ARG B 148 ? 0.2997 0.2838 0.8593 0.0669  0.0921  0.0024  149 ARG B CD  
4097  N  NE  . ARG B 148 ? 0.2990 0.2890 0.8732 0.0653  0.0971  0.0073  149 ARG B NE  
4098  C  CZ  . ARG B 148 ? 0.3716 0.3626 0.9538 0.0688  0.0967  0.0056  149 ARG B CZ  
4099  N  NH1 . ARG B 148 ? 0.3137 0.2995 0.8899 0.0740  0.0917  -0.0010 149 ARG B NH1 
4100  N  NH2 . ARG B 148 ? 0.3958 0.3923 0.9930 0.0670  0.1009  0.0101  149 ARG B NH2 
4101  N  N   . LEU B 149 ? 0.4255 0.3880 0.9704 0.0566  0.0577  -0.0136 150 LEU B N   
4102  C  CA  . LEU B 149 ? 0.3909 0.3476 0.9298 0.0575  0.0520  -0.0190 150 LEU B CA  
4103  C  C   . LEU B 149 ? 0.3559 0.3145 0.9021 0.0474  0.0464  -0.0147 150 LEU B C   
4104  O  O   . LEU B 149 ? 0.3514 0.3095 0.8935 0.0457  0.0447  -0.0156 150 LEU B O   
4105  C  CB  . LEU B 149 ? 0.3924 0.3410 0.9306 0.0642  0.0468  -0.0273 150 LEU B CB  
4106  C  CG  . LEU B 149 ? 0.4140 0.3593 0.9403 0.0774  0.0517  -0.0340 150 LEU B CG  
4107  C  CD1 . LEU B 149 ? 0.3476 0.2867 0.8769 0.0833  0.0480  -0.0405 150 LEU B CD1 
4108  C  CD2 . LEU B 149 ? 0.3390 0.2800 0.8524 0.0836  0.0503  -0.0403 150 LEU B CD2 
4109  N  N   . TYR B 150 ? 0.3285 0.2898 0.8854 0.0417  0.0439  -0.0099 151 TYR B N   
4110  C  CA  . TYR B 150 ? 0.2649 0.2292 0.8286 0.0338  0.0400  -0.0047 151 TYR B CA  
4111  C  C   . TYR B 150 ? 0.4235 0.3936 0.9835 0.0296  0.0437  -0.0002 151 TYR B C   
4112  O  O   . TYR B 150 ? 0.4370 0.4083 0.9969 0.0260  0.0416  0.0010  151 TYR B O   
4113  C  CB  . TYR B 150 ? 0.3102 0.2762 0.8840 0.0309  0.0374  0.0002  151 TYR B CB  
4114  C  CG  . TYR B 150 ? 0.3604 0.3295 0.9403 0.0249  0.0342  0.0064  151 TYR B CG  
4115  C  CD1 . TYR B 150 ? 0.4566 0.4236 1.0395 0.0230  0.0308  0.0057  151 TYR B CD1 
4116  C  CD2 . TYR B 150 ? 0.3506 0.3245 0.9338 0.0222  0.0346  0.0128  151 TYR B CD2 
4117  C  CE1 . TYR B 150 ? 0.5006 0.4711 1.0898 0.0186  0.0293  0.0124  151 TYR B CE1 
4118  C  CE2 . TYR B 150 ? 0.4267 0.4028 1.0136 0.0187  0.0324  0.0187  151 TYR B CE2 
4119  C  CZ  . TYR B 150 ? 0.5557 0.5305 1.1457 0.0170  0.0306  0.0191  151 TYR B CZ  
4120  O  OH  . TYR B 150 ? 0.6324 0.6097 1.2267 0.0145  0.0298  0.0261  151 TYR B OH  
4121  N  N   . TYR B 151 ? 0.4181 0.3920 0.9767 0.0302  0.0490  0.0023  152 TYR B N   
4122  C  CA  . TYR B 151 ? 0.3748 0.3532 0.9306 0.0266  0.0524  0.0061  152 TYR B CA  
4123  C  C   . TYR B 151 ? 0.3870 0.3633 0.9329 0.0295  0.0546  0.0031  152 TYR B C   
4124  O  O   . TYR B 151 ? 0.4565 0.4350 1.0005 0.0257  0.0545  0.0053  152 TYR B O   
4125  C  CB  . TYR B 151 ? 0.3154 0.2972 0.8742 0.0269  0.0576  0.0089  152 TYR B CB  
4126  C  CG  . TYR B 151 ? 0.2614 0.2460 0.8172 0.0246  0.0620  0.0119  152 TYR B CG  
4127  C  CD1 . TYR B 151 ? 0.2798 0.2675 0.8387 0.0185  0.0594  0.0152  152 TYR B CD1 
4128  C  CD2 . TYR B 151 ? 0.2668 0.2508 0.8164 0.0295  0.0689  0.0114  152 TYR B CD2 
4129  C  CE1 . TYR B 151 ? 0.2198 0.2092 0.7766 0.0165  0.0628  0.0175  152 TYR B CE1 
4130  C  CE2 . TYR B 151 ? 0.2361 0.2221 0.7841 0.0275  0.0731  0.0149  152 TYR B CE2 
4131  C  CZ  . TYR B 151 ? 0.2296 0.2179 0.7817 0.0205  0.0697  0.0176  152 TYR B CZ  
4132  O  OH  . TYR B 151 ? 0.2222 0.2117 0.7736 0.0185  0.0733  0.0207  152 TYR B OH  
4133  N  N   . ARG B 152 ? 0.4707 0.4424 1.0098 0.0372  0.0564  -0.0022 153 ARG B N   
4134  C  CA  . ARG B 152 ? 0.5473 0.5164 1.0754 0.0426  0.0583  -0.0056 153 ARG B CA  
4135  C  C   . ARG B 152 ? 0.6859 0.6523 1.2138 0.0401  0.0513  -0.0088 153 ARG B C   
4136  O  O   . ARG B 152 ? 0.7500 0.7148 1.2698 0.0435  0.0516  -0.0112 153 ARG B O   
4137  C  CB  . ARG B 152 ? 0.6420 0.6065 1.1619 0.0538  0.0612  -0.0115 153 ARG B CB  
4138  C  CG  . ARG B 152 ? 0.7130 0.6802 1.2250 0.0604  0.0709  -0.0089 153 ARG B CG  
4139  C  CD  . ARG B 152 ? 0.8099 0.7759 1.3113 0.0637  0.0716  -0.0098 153 ARG B CD  
4140  N  NE  . ARG B 152 ? 0.8834 0.8523 1.3776 0.0711  0.0819  -0.0060 153 ARG B NE  
4141  C  CZ  . ARG B 152 ? 0.9462 0.9130 1.4274 0.0802  0.0846  -0.0080 153 ARG B CZ  
4142  N  NH1 . ARG B 152 ? 0.9758 0.9461 1.4519 0.0871  0.0954  -0.0026 153 ARG B NH1 
4143  N  NH2 . ARG B 152 ? 0.9622 0.9238 1.4369 0.0828  0.0765  -0.0150 153 ARG B NH2 
4144  N  N   . GLY B 153 ? 0.7568 0.7232 1.2947 0.0346  0.0454  -0.0082 154 GLY B N   
4145  C  CA  . GLY B 153 ? 0.8428 0.8075 1.3843 0.0317  0.0392  -0.0104 154 GLY B CA  
4146  C  C   . GLY B 153 ? 0.9387 0.8957 1.4805 0.0370  0.0331  -0.0190 154 GLY B C   
4147  O  O   . GLY B 153 ? 0.9314 0.8858 1.4745 0.0371  0.0279  -0.0232 154 GLY B O   
4148  N  N   . ALA B 154 ? 1.0490 1.0022 1.5909 0.0415  0.0331  -0.0221 155 ALA B N   
4149  C  CA  . ALA B 154 ? 1.1625 1.1071 1.7032 0.0481  0.0272  -0.0317 155 ALA B CA  
4150  C  C   . ALA B 154 ? 1.3352 1.2780 1.8917 0.0421  0.0194  -0.0317 155 ALA B C   
4151  O  O   . ALA B 154 ? 1.3768 1.3123 1.9367 0.0458  0.0129  -0.0396 155 ALA B O   
4152  C  CB  . ALA B 154 ? 1.1182 1.0597 1.6528 0.0563  0.0308  -0.0351 155 ALA B CB  
4153  N  N   . ASN B 155 ? 1.4804 1.4301 2.0468 0.0334  0.0204  -0.0227 156 ASN B N   
4154  C  CA  . ASN B 155 ? 1.4929 1.4433 2.0757 0.0277  0.0149  -0.0200 156 ASN B CA  
4155  C  C   . ASN B 155 ? 1.4835 1.4292 2.0747 0.0290  0.0118  -0.0210 156 ASN B C   
4156  O  O   . ASN B 155 ? 1.5389 1.4800 2.1415 0.0284  0.0051  -0.0245 156 ASN B O   
4157  C  CB  . ASN B 155 ? 1.5193 1.4668 2.1072 0.0275  0.0083  -0.0262 156 ASN B CB  
4158  N  N   . LEU B 156 ? 1.1968 1.1436 1.7836 0.0309  0.0162  -0.0179 157 LEU B N   
4159  C  CA  . LEU B 156 ? 0.9996 0.9431 1.5952 0.0314  0.0139  -0.0166 157 LEU B CA  
4160  C  C   . LEU B 156 ? 0.8807 0.8292 1.4889 0.0250  0.0134  -0.0063 157 LEU B C   
4161  O  O   . LEU B 156 ? 0.8401 0.7948 1.4495 0.0207  0.0154  -0.0008 157 LEU B O   
4162  C  CB  . LEU B 156 ? 0.8600 0.8041 1.4485 0.0356  0.0187  -0.0160 157 LEU B CB  
4163  C  CG  . LEU B 156 ? 0.7263 0.6657 1.3035 0.0443  0.0210  -0.0244 157 LEU B CG  
4164  C  CD1 . LEU B 156 ? 0.6655 0.6048 1.2299 0.0481  0.0235  -0.0293 157 LEU B CD1 
4165  C  CD2 . LEU B 156 ? 0.6318 0.5756 1.2076 0.0457  0.0268  -0.0199 157 LEU B CD2 
4166  N  N   . HIS B 157 ? 0.8929 0.8383 1.5098 0.0254  0.0113  -0.0035 158 HIS B N   
4167  C  CA  . HIS B 157 ? 0.8399 0.7893 1.4651 0.0218  0.0125  0.0076  158 HIS B CA  
4168  C  C   . HIS B 157 ? 0.8100 0.7590 1.4316 0.0247  0.0143  0.0100  158 HIS B C   
4169  O  O   . HIS B 157 ? 0.7598 0.7029 1.3846 0.0282  0.0117  0.0060  158 HIS B O   
4170  C  CB  . HIS B 157 ? 0.8344 0.7801 1.4757 0.0199  0.0079  0.0104  158 HIS B CB  
4171  N  N   . LEU B 158 ? 0.7788 0.7341 1.3945 0.0235  0.0182  0.0157  159 LEU B N   
4172  C  CA  . LEU B 158 ? 0.7510 0.7071 1.3642 0.0262  0.0194  0.0173  159 LEU B CA  
4173  C  C   . LEU B 158 ? 0.7887 0.7397 1.4109 0.0280  0.0159  0.0211  159 LEU B C   
4174  O  O   . LEU B 158 ? 0.8420 0.7901 1.4648 0.0318  0.0150  0.0180  159 LEU B O   
4175  C  CB  . LEU B 158 ? 0.7061 0.6691 1.3147 0.0241  0.0222  0.0236  159 LEU B CB  
4176  C  CG  . LEU B 158 ? 0.6662 0.6318 1.2709 0.0264  0.0240  0.0220  159 LEU B CG  
4177  C  CD1 . LEU B 158 ? 0.6385 0.6037 1.2378 0.0287  0.0272  0.0139  159 LEU B CD1 
4178  C  CD2 . LEU B 158 ? 0.6488 0.6203 1.2499 0.0242  0.0254  0.0268  159 LEU B CD2 
4179  N  N   . GLU B 159 ? 0.8147 0.7646 1.4444 0.0255  0.0143  0.0283  160 GLU B N   
4180  C  CA  . GLU B 159 ? 0.7426 0.6865 1.3825 0.0267  0.0112  0.0334  160 GLU B CA  
4181  C  C   . GLU B 159 ? 0.6439 0.5809 1.2875 0.0304  0.0079  0.0255  160 GLU B C   
4182  O  O   . GLU B 159 ? 0.6404 0.5750 1.2847 0.0339  0.0069  0.0266  160 GLU B O   
4183  C  CB  . GLU B 159 ? 0.8677 0.8105 1.5177 0.0233  0.0105  0.0385  160 GLU B CB  
4184  C  CG  . GLU B 159 ? 0.9538 0.9036 1.5998 0.0198  0.0138  0.0403  160 GLU B CG  
4185  C  CD  . GLU B 159 ? 1.0289 0.9783 1.6875 0.0167  0.0128  0.0427  160 GLU B CD  
4186  O  OE1 . GLU B 159 ? 1.0590 1.0044 1.7248 0.0165  0.0087  0.0346  160 GLU B OE1 
4187  O  OE2 . GLU B 159 ? 1.0599 1.0129 1.7218 0.0149  0.0161  0.0525  160 GLU B OE2 
4188  N  N   . GLU B 160 ? 0.5825 0.5159 1.2284 0.0303  0.0058  0.0169  161 GLU B N   
4189  C  CA  . GLU B 160 ? 0.6862 0.6114 1.3362 0.0344  0.0018  0.0085  161 GLU B CA  
4190  C  C   . GLU B 160 ? 0.6813 0.6064 1.3215 0.0399  0.0040  0.0016  161 GLU B C   
4191  O  O   . GLU B 160 ? 0.6759 0.5962 1.3197 0.0441  0.0022  -0.0001 161 GLU B O   
4192  C  CB  . GLU B 160 ? 0.7818 0.7029 1.4355 0.0336  -0.0020 0.0000  161 GLU B CB  
4193  C  CG  . GLU B 160 ? 0.8807 0.7919 1.5377 0.0387  -0.0071 -0.0105 161 GLU B CG  
4194  C  CD  . GLU B 160 ? 0.9618 0.8689 1.6188 0.0394  -0.0115 -0.0212 161 GLU B CD  
4195  O  OE1 . GLU B 160 ? 0.9744 0.8868 1.6258 0.0367  -0.0097 -0.0213 161 GLU B OE1 
4196  O  OE2 . GLU B 160 ? 0.9988 0.8969 1.6615 0.0431  -0.0176 -0.0300 161 GLU B OE2 
4197  N  N   . THR B 161 ? 0.5792 0.5097 1.2080 0.0403  0.0083  -0.0018 162 THR B N   
4198  C  CA  . THR B 161 ? 0.5597 0.4917 1.1801 0.0456  0.0121  -0.0068 162 THR B CA  
4199  C  C   . THR B 161 ? 0.5201 0.4548 1.1449 0.0467  0.0127  -0.0007 162 THR B C   
4200  O  O   . THR B 161 ? 0.5427 0.4742 1.1695 0.0521  0.0123  -0.0044 162 THR B O   
4201  C  CB  . THR B 161 ? 0.5496 0.4883 1.1589 0.0446  0.0176  -0.0077 162 THR B CB  
4202  O  OG1 . THR B 161 ? 0.5222 0.4568 1.1248 0.0472  0.0171  -0.0162 162 THR B OG1 
4203  C  CG2 . THR B 161 ? 0.5487 0.4919 1.1537 0.0484  0.0228  -0.0082 162 THR B CG2 
4204  N  N   . LEU B 162 ? 0.4882 0.4284 1.1144 0.0423  0.0132  0.0084  163 LEU B N   
4205  C  CA  . LEU B 162 ? 0.4738 0.4162 1.1038 0.0437  0.0124  0.0143  163 LEU B CA  
4206  C  C   . LEU B 162 ? 0.4788 0.4137 1.1178 0.0467  0.0078  0.0159  163 LEU B C   
4207  O  O   . LEU B 162 ? 0.5169 0.4509 1.1588 0.0511  0.0071  0.0145  163 LEU B O   
4208  C  CB  . LEU B 162 ? 0.4883 0.4358 1.1170 0.0398  0.0124  0.0233  163 LEU B CB  
4209  C  CG  . LEU B 162 ? 0.4702 0.4252 1.0912 0.0369  0.0165  0.0224  163 LEU B CG  
4210  C  CD1 . LEU B 162 ? 0.4656 0.4236 1.0850 0.0338  0.0158  0.0307  163 LEU B CD1 
4211  C  CD2 . LEU B 162 ? 0.4886 0.4481 1.1084 0.0393  0.0189  0.0192  163 LEU B CD2 
4212  N  N   . ALA B 163 ? 0.5188 0.4485 1.1636 0.0442  0.0049  0.0191  164 ALA B N   
4213  C  CA  . ALA B 163 ? 0.5032 0.4248 1.1580 0.0464  0.0006  0.0216  164 ALA B CA  
4214  C  C   . ALA B 163 ? 0.5305 0.4467 1.1870 0.0520  -0.0009 0.0119  164 ALA B C   
4215  O  O   . ALA B 163 ? 0.5872 0.5006 1.2484 0.0561  -0.0027 0.0134  164 ALA B O   
4216  C  CB  . ALA B 163 ? 0.5176 0.4347 1.1804 0.0425  -0.0016 0.0249  164 ALA B CB  
4217  N  N   . GLU B 164 ? 0.5072 0.4215 1.1592 0.0532  -0.0001 0.0018  165 GLU B N   
4218  C  CA  . GLU B 164 ? 0.5710 0.4793 1.2224 0.0601  -0.0011 -0.0084 165 GLU B CA  
4219  C  C   . GLU B 164 ? 0.6364 0.5500 1.2835 0.0651  0.0030  -0.0096 165 GLU B C   
4220  O  O   . GLU B 164 ? 0.6634 0.5730 1.3152 0.0707  0.0016  -0.0122 165 GLU B O   
4221  C  CB  . GLU B 164 ? 0.6259 0.5312 1.2702 0.0617  -0.0011 -0.0190 165 GLU B CB  
4222  C  CG  . GLU B 164 ? 0.7752 0.6753 1.4271 0.0571  -0.0064 -0.0195 165 GLU B CG  
4223  C  CD  . GLU B 164 ? 0.8761 0.7679 1.5429 0.0571  -0.0122 -0.0172 165 GLU B CD  
4224  O  OE1 . GLU B 164 ? 0.9298 0.8152 1.5983 0.0633  -0.0142 -0.0231 165 GLU B OE1 
4225  O  OE2 . GLU B 164 ? 0.9021 0.7937 1.5793 0.0512  -0.0143 -0.0090 165 GLU B OE2 
4226  N  N   . PHE B 165 ? 0.6226 0.5453 1.2622 0.0631  0.0082  -0.0077 166 PHE B N   
4227  C  CA  . PHE B 165 ? 0.6048 0.5341 1.2433 0.0667  0.0124  -0.0077 166 PHE B CA  
4228  C  C   . PHE B 165 ? 0.3658 0.2948 1.0139 0.0680  0.0088  -0.0018 166 PHE B C   
4229  O  O   . PHE B 165 ? 0.4393 0.3675 1.0916 0.0741  0.0092  -0.0052 166 PHE B O   
4230  C  CB  . PHE B 165 ? 0.5229 0.4618 1.1556 0.0624  0.0171  -0.0040 166 PHE B CB  
4231  C  CG  . PHE B 165 ? 0.3410 0.2874 0.9777 0.0640  0.0197  -0.0015 166 PHE B CG  
4232  C  CD1 . PHE B 165 ? 0.3458 0.2952 0.9819 0.0698  0.0252  -0.0068 166 PHE B CD1 
4233  C  CD2 . PHE B 165 ? 0.3345 0.2850 0.9763 0.0607  0.0165  0.0062  166 PHE B CD2 
4234  C  CE1 . PHE B 165 ? 0.3429 0.2998 0.9860 0.0708  0.0275  -0.0043 166 PHE B CE1 
4235  C  CE2 . PHE B 165 ? 0.3323 0.2896 0.9799 0.0623  0.0175  0.0076  166 PHE B CE2 
4236  C  CZ  . PHE B 165 ? 0.4078 0.3686 1.0574 0.0667  0.0230  0.0025  166 PHE B CZ  
4237  N  N   . TRP B 166 ? 0.3606 0.2903 1.0118 0.0633  0.0055  0.0072  167 TRP B N   
4238  C  CA  . TRP B 166 ? 0.3667 0.2953 1.0252 0.0654  0.0014  0.0139  167 TRP B CA  
4239  C  C   . TRP B 166 ? 0.4728 0.3920 1.1390 0.0699  -0.0024 0.0117  167 TRP B C   
4240  O  O   . TRP B 166 ? 0.5331 0.4517 1.2052 0.0745  -0.0046 0.0129  167 TRP B O   
4241  C  CB  . TRP B 166 ? 0.3617 0.2909 1.0197 0.0611  -0.0012 0.0243  167 TRP B CB  
4242  C  CG  . TRP B 166 ? 0.4609 0.3990 1.1126 0.0580  0.0012  0.0269  167 TRP B CG  
4243  C  CD1 . TRP B 166 ? 0.4371 0.3777 1.0828 0.0529  0.0029  0.0303  167 TRP B CD1 
4244  C  CD2 . TRP B 166 ? 0.4994 0.4451 1.1518 0.0597  0.0018  0.0261  167 TRP B CD2 
4245  N  NE1 . TRP B 166 ? 0.4682 0.4167 1.1098 0.0517  0.0043  0.0313  167 TRP B NE1 
4246  C  CE2 . TRP B 166 ? 0.4555 0.4073 1.1018 0.0555  0.0034  0.0287  167 TRP B CE2 
4247  C  CE3 . TRP B 166 ? 0.5291 0.4772 1.1881 0.0645  0.0010  0.0233  167 TRP B CE3 
4248  C  CZ2 . TRP B 166 ? 0.5028 0.4623 1.1501 0.0557  0.0036  0.0281  167 TRP B CZ2 
4249  C  CZ3 . TRP B 166 ? 0.4859 0.4425 1.1468 0.0644  0.0016  0.0232  167 TRP B CZ3 
4250  C  CH2 . TRP B 166 ? 0.5129 0.4748 1.1682 0.0599  0.0025  0.0254  167 TRP B CH2 
4251  N  N   . ALA B 167 ? 0.5525 0.4641 1.2195 0.0686  -0.0039 0.0081  168 ALA B N   
4252  C  CA  . ALA B 167 ? 0.5955 0.4969 1.2707 0.0726  -0.0081 0.0051  168 ALA B CA  
4253  C  C   . ALA B 167 ? 0.6536 0.5545 1.3287 0.0804  -0.0065 -0.0041 168 ALA B C   
4254  O  O   . ALA B 167 ? 0.6960 0.5945 1.3781 0.0851  -0.0088 -0.0026 168 ALA B O   
4255  C  CB  . ALA B 167 ? 0.5659 0.4600 1.2433 0.0697  -0.0105 0.0011  168 ALA B CB  
4256  N  N   . ARG B 168 ? 0.7276 0.6306 1.3942 0.0827  -0.0023 -0.0132 169 ARG B N   
4257  C  CA  . ARG B 168 ? 0.8331 0.7351 1.4986 0.0916  0.0003  -0.0220 169 ARG B CA  
4258  C  C   . ARG B 168 ? 0.7832 0.6946 1.4518 0.0942  0.0039  -0.0184 169 ARG B C   
4259  O  O   . ARG B 168 ? 0.8353 0.7457 1.5092 0.1014  0.0041  -0.0217 169 ARG B O   
4260  C  CB  . ARG B 168 ? 0.9581 0.8598 1.6118 0.0951  0.0047  -0.0319 169 ARG B CB  
4261  C  CG  . ARG B 168 ? 1.0935 0.9925 1.7443 0.1063  0.0076  -0.0416 169 ARG B CG  
4262  C  CD  . ARG B 168 ? 1.1809 1.0739 1.8197 0.1116  0.0086  -0.0525 169 ARG B CD  
4263  N  NE  . ARG B 168 ? 1.2556 1.1561 1.8830 0.1184  0.0177  -0.0563 169 ARG B NE  
4264  C  CZ  . ARG B 168 ? 1.3123 1.2094 1.9259 0.1252  0.0203  -0.0654 169 ARG B CZ  
4265  N  NH1 . ARG B 168 ? 1.3274 1.2135 1.9379 0.1256  0.0133  -0.0727 169 ARG B NH1 
4266  N  NH2 . ARG B 168 ? 1.3247 1.2295 1.9283 0.1321  0.0298  -0.0669 169 ARG B NH2 
4267  N  N   . LEU B 169 ? 0.6621 0.5828 1.3286 0.0885  0.0062  -0.0118 170 LEU B N   
4268  C  CA  . LEU B 169 ? 0.6277 0.5575 1.2999 0.0897  0.0078  -0.0078 170 LEU B CA  
4269  C  C   . LEU B 169 ? 0.5473 0.4731 1.2298 0.0922  0.0014  -0.0030 170 LEU B C   
4270  O  O   . LEU B 169 ? 0.5619 0.4907 1.2516 0.0978  0.0018  -0.0045 170 LEU B O   
4271  C  CB  . LEU B 169 ? 0.5493 0.4876 1.2185 0.0828  0.0090  -0.0015 170 LEU B CB  
4272  C  CG  . LEU B 169 ? 0.4758 0.4235 1.1525 0.0837  0.0096  0.0017  170 LEU B CG  
4273  C  CD1 . LEU B 169 ? 0.3770 0.3316 1.0545 0.0874  0.0175  -0.0040 170 LEU B CD1 
4274  C  CD2 . LEU B 169 ? 0.4869 0.4401 1.1618 0.0774  0.0073  0.0085  170 LEU B CD2 
4275  N  N   . LEU B 170 ? 0.5592 0.4784 1.2428 0.0885  -0.0041 0.0033  171 LEU B N   
4276  C  CA  . LEU B 170 ? 0.5735 0.4870 1.2656 0.0914  -0.0102 0.0090  171 LEU B CA  
4277  C  C   . LEU B 170 ? 0.5627 0.4692 1.2610 0.0986  -0.0112 0.0021  171 LEU B C   
4278  O  O   . LEU B 170 ? 0.4781 0.3846 1.1843 0.1038  -0.0138 0.0036  171 LEU B O   
4279  C  CB  . LEU B 170 ? 0.5897 0.4960 1.2814 0.0868  -0.0143 0.0173  171 LEU B CB  
4280  C  CG  . LEU B 170 ? 0.6354 0.5343 1.3351 0.0904  -0.0202 0.0249  171 LEU B CG  
4281  C  CD1 . LEU B 170 ? 0.6588 0.5644 1.3592 0.0931  -0.0227 0.0312  171 LEU B CD1 
4282  C  CD2 . LEU B 170 ? 0.6520 0.5427 1.3524 0.0861  -0.0225 0.0331  171 LEU B CD2 
4283  N  N   . GLU B 171 ? 0.6303 0.5304 1.3249 0.0995  -0.0097 -0.0060 172 GLU B N   
4284  C  CA  . GLU B 171 ? 0.7133 0.6063 1.4121 0.1075  -0.0104 -0.0145 172 GLU B CA  
4285  C  C   . GLU B 171 ? 0.7179 0.6189 1.4190 0.1146  -0.0060 -0.0184 172 GLU B C   
4286  O  O   . GLU B 171 ? 0.7136 0.6137 1.4242 0.1194  -0.0088 -0.0165 172 GLU B O   
4287  C  CB  . GLU B 171 ? 0.8156 0.7022 1.5071 0.1088  -0.0089 -0.0247 172 GLU B CB  
4288  C  CG  . GLU B 171 ? 0.9220 0.8002 1.6146 0.1024  -0.0138 -0.0227 172 GLU B CG  
4289  C  CD  . GLU B 171 ? 1.0217 0.8888 1.7141 0.1068  -0.0166 -0.0341 172 GLU B CD  
4290  O  OE1 . GLU B 171 ? 1.0729 0.9388 1.7613 0.1158  -0.0141 -0.0437 172 GLU B OE1 
4291  O  OE2 . GLU B 171 ? 1.0562 0.9161 1.7530 0.1019  -0.0214 -0.0336 172 GLU B OE2 
4292  N  N   . ARG B 172 ? 0.7109 0.6200 1.4043 0.1154  0.0013  -0.0231 173 ARG B N   
4293  C  CA  . ARG B 172 ? 0.7068 0.6242 1.4034 0.1226  0.0072  -0.0269 173 ARG B CA  
4294  C  C   . ARG B 172 ? 0.6633 0.5891 1.3715 0.1218  0.0051  -0.0196 173 ARG B C   
4295  O  O   . ARG B 172 ? 0.6408 0.5683 1.3583 0.1287  0.0052  -0.0214 173 ARG B O   
4296  C  CB  . ARG B 172 ? 0.7694 0.6950 1.4562 0.1227  0.0160  -0.0305 173 ARG B CB  
4297  C  CG  . ARG B 172 ? 0.8596 0.7778 1.5342 0.1284  0.0190  -0.0403 173 ARG B CG  
4298  C  CD  . ARG B 172 ? 0.9384 0.8620 1.6101 0.1394  0.0278  -0.0470 173 ARG B CD  
4299  N  NE  . ARG B 172 ? 0.9992 0.9146 1.6574 0.1475  0.0298  -0.0573 173 ARG B NE  
4300  C  CZ  . ARG B 172 ? 1.0360 0.9557 1.6811 0.1520  0.0379  -0.0612 173 ARG B CZ  
4301  N  NH1 . ARG B 172 ? 1.0053 0.9377 1.6511 0.1482  0.0452  -0.0550 173 ARG B NH1 
4302  N  NH2 . ARG B 172 ? 1.0693 0.9804 1.7010 0.1609  0.0384  -0.0714 173 ARG B NH2 
4303  N  N   . LEU B 173 ? 0.5553 0.4861 1.2631 0.1139  0.0028  -0.0117 174 LEU B N   
4304  C  CA  . LEU B 173 ? 0.5371 0.4752 1.2548 0.1134  -0.0008 -0.0053 174 LEU B CA  
4305  C  C   . LEU B 173 ? 0.5407 0.4715 1.2669 0.1178  -0.0085 -0.0021 174 LEU B C   
4306  O  O   . LEU B 173 ? 0.5135 0.4496 1.2504 0.1222  -0.0106 -0.0009 174 LEU B O   
4307  C  CB  . LEU B 173 ? 0.5060 0.4485 1.2192 0.1053  -0.0031 0.0018  174 LEU B CB  
4308  C  CG  . LEU B 173 ? 0.5120 0.4668 1.2256 0.1019  0.0022  0.0014  174 LEU B CG  
4309  C  CD1 . LEU B 173 ? 0.4595 0.4164 1.1667 0.1030  0.0117  -0.0053 174 LEU B CD1 
4310  C  CD2 . LEU B 173 ? 0.4745 0.4316 1.1822 0.0945  -0.0009 0.0076  174 LEU B CD2 
4311  N  N   . PHE B 174 ? 0.5937 0.5125 1.3165 0.1168  -0.0127 -0.0004 175 PHE B N   
4312  C  CA  . PHE B 174 ? 0.6680 0.5786 1.3990 0.1212  -0.0196 0.0035  175 PHE B CA  
4313  C  C   . PHE B 174 ? 0.4913 0.3993 1.2295 0.1298  -0.0181 -0.0043 175 PHE B C   
4314  O  O   . PHE B 174 ? 0.5020 0.4095 1.2501 0.1352  -0.0222 -0.0021 175 PHE B O   
4315  C  CB  . PHE B 174 ? 0.4824 0.3804 1.2103 0.1176  -0.0239 0.0082  175 PHE B CB  
4316  C  CG  . PHE B 174 ? 0.5890 0.4796 1.3242 0.1209  -0.0310 0.0164  175 PHE B CG  
4317  C  CD1 . PHE B 174 ? 0.5581 0.4516 1.2917 0.1195  -0.0351 0.0269  175 PHE B CD1 
4318  C  CD2 . PHE B 174 ? 0.5159 0.3961 1.2589 0.1265  -0.0339 0.0135  175 PHE B CD2 
4319  C  CE1 . PHE B 174 ? 0.5415 0.4275 1.2800 0.1239  -0.0415 0.0353  175 PHE B CE1 
4320  C  CE2 . PHE B 174 ? 0.5306 0.4034 1.2803 0.1300  -0.0402 0.0219  175 PHE B CE2 
4321  C  CZ  . PHE B 174 ? 0.5274 0.4031 1.2743 0.1289  -0.0438 0.0332  175 PHE B CZ  
4322  N  N   . LYS B 175 ? 0.4942 0.4002 1.2270 0.1322  -0.0125 -0.0137 176 LYS B N   
4323  C  CA  . LYS B 175 ? 0.5099 0.4145 1.2480 0.1420  -0.0100 -0.0218 176 LYS B CA  
4324  C  C   . LYS B 175 ? 0.6479 0.5660 1.3951 0.1458  -0.0067 -0.0209 176 LYS B C   
4325  O  O   . LYS B 175 ? 0.5181 0.4359 1.2764 0.1522  -0.0097 -0.0207 176 LYS B O   
4326  C  CB  . LYS B 175 ? 0.5147 0.4164 1.2427 0.1458  -0.0038 -0.0324 176 LYS B CB  
4327  C  CG  . LYS B 175 ? 0.7000 0.5896 1.4201 0.1415  -0.0073 -0.0347 176 LYS B CG  
4328  C  CD  . LYS B 175 ? 0.7336 0.6155 1.4470 0.1497  -0.0048 -0.0472 176 LYS B CD  
4329  C  CE  . LYS B 175 ? 0.7476 0.6395 1.4556 0.1580  0.0048  -0.0535 176 LYS B CE  
4330  N  NZ  . LYS B 175 ? 0.7649 0.6491 1.4625 0.1678  0.0076  -0.0661 176 LYS B NZ  
4331  N  N   . GLN B 176 ? 0.6135 0.5435 1.3576 0.1418  -0.0008 -0.0201 177 GLN B N   
4332  C  CA  . GLN B 176 ? 0.5828 0.5263 1.3379 0.1451  0.0033  -0.0200 177 GLN B CA  
4333  C  C   . GLN B 176 ? 0.4860 0.4338 1.2537 0.1440  -0.0044 -0.0129 177 GLN B C   
4334  O  O   . GLN B 176 ? 0.4916 0.4472 1.2727 0.1494  -0.0037 -0.0138 177 GLN B O   
4335  C  CB  . GLN B 176 ? 0.5857 0.5402 1.3361 0.1404  0.0115  -0.0202 177 GLN B CB  
4336  C  CG  . GLN B 176 ? 0.6506 0.6041 1.3900 0.1451  0.0210  -0.0278 177 GLN B CG  
4337  C  CD  . GLN B 176 ? 0.7102 0.6752 1.4468 0.1414  0.0298  -0.0267 177 GLN B CD  
4338  O  OE1 . GLN B 176 ? 0.6918 0.6602 1.4268 0.1323  0.0277  -0.0213 177 GLN B OE1 
4339  N  NE2 . GLN B 176 ? 0.7323 0.7035 1.4689 0.1492  0.0400  -0.0314 177 GLN B NE2 
4340  N  N   . LEU B 177 ? 0.4808 0.4236 1.2441 0.1382  -0.0119 -0.0058 178 LEU B N   
4341  C  CA  . LEU B 177 ? 0.4826 0.4285 1.2550 0.1388  -0.0203 0.0010  178 LEU B CA  
4342  C  C   . LEU B 177 ? 0.7240 0.6610 1.5037 0.1462  -0.0266 0.0021  178 LEU B C   
4343  O  O   . LEU B 177 ? 0.5076 0.4462 1.2949 0.1489  -0.0342 0.0075  178 LEU B O   
4344  C  CB  . LEU B 177 ? 0.4726 0.4164 1.2359 0.1318  -0.0257 0.0088  178 LEU B CB  
4345  C  CG  . LEU B 177 ? 0.6581 0.6134 1.4200 0.1257  -0.0238 0.0100  178 LEU B CG  
4346  C  CD1 . LEU B 177 ? 0.4456 0.3967 1.1940 0.1190  -0.0263 0.0158  178 LEU B CD1 
4347  C  CD2 . LEU B 177 ? 0.6459 0.6112 1.4215 0.1287  -0.0292 0.0117  178 LEU B CD2 
4348  N  N   . HIS B 178 ? 0.6750 0.6021 1.4522 0.1500  -0.0241 -0.0032 179 HIS B N   
4349  C  CA  . HIS B 178 ? 0.7251 0.6431 1.5104 0.1576  -0.0293 -0.0033 179 HIS B CA  
4350  C  C   . HIS B 178 ? 0.7871 0.7048 1.5764 0.1654  -0.0229 -0.0135 179 HIS B C   
4351  O  O   . HIS B 178 ? 0.7314 0.6381 1.5145 0.1673  -0.0217 -0.0188 179 HIS B O   
4352  C  CB  . HIS B 178 ? 0.7039 0.6062 1.4828 0.1551  -0.0348 0.0014  179 HIS B CB  
4353  C  CG  . HIS B 178 ? 0.7050 0.6059 1.4811 0.1511  -0.0417 0.0129  179 HIS B CG  
4354  N  ND1 . HIS B 178 ? 0.6957 0.6049 1.4779 0.1538  -0.0466 0.0181  179 HIS B ND1 
4355  C  CD2 . HIS B 178 ? 0.6771 0.5695 1.4446 0.1456  -0.0444 0.0203  179 HIS B CD2 
4356  C  CE1 . HIS B 178 ? 0.6810 0.5861 1.4563 0.1511  -0.0523 0.0280  179 HIS B CE1 
4357  N  NE2 . HIS B 178 ? 0.6770 0.5721 1.4436 0.1460  -0.0504 0.0300  179 HIS B NE2 
4358  N  N   . PRO B 179 ? 0.9191 0.8491 1.7193 0.1706  -0.0190 -0.0164 180 PRO B N   
4359  C  CA  . PRO B 179 ? 0.9770 0.9092 1.7798 0.1792  -0.0109 -0.0258 180 PRO B CA  
4360  C  C   . PRO B 179 ? 1.0534 0.9724 1.8588 0.1876  -0.0142 -0.0303 180 PRO B C   
4361  O  O   . PRO B 179 ? 1.0909 1.0034 1.8881 0.1920  -0.0094 -0.0385 180 PRO B O   
4362  C  CB  . PRO B 179 ? 0.9905 0.9388 1.8090 0.1825  -0.0080 -0.0250 180 PRO B CB  
4363  C  CG  . PRO B 179 ? 0.9607 0.9162 1.7813 0.1738  -0.0131 -0.0171 180 PRO B CG  
4364  C  CD  . PRO B 179 ? 0.9307 0.8732 1.7423 0.1694  -0.0223 -0.0111 180 PRO B CD  
4365  N  N   . GLN B 180 ? 1.0399 0.9542 1.8557 0.1905  -0.0227 -0.0254 181 GLN B N   
4366  C  CA  . GLN B 180 ? 1.0365 0.9358 1.8539 0.1970  -0.0264 -0.0291 181 GLN B CA  
4367  C  C   . GLN B 180 ? 1.0297 0.9151 1.8414 0.1903  -0.0344 -0.0220 181 GLN B C   
4368  O  O   . GLN B 180 ? 1.0329 0.9163 1.8498 0.1889  -0.0419 -0.0126 181 GLN B O   
4369  C  CB  . GLN B 180 ? 1.0464 0.9479 1.8799 0.2064  -0.0297 -0.0290 181 GLN B CB  
4370  N  N   . LEU B 181 ? 0.9992 0.8750 1.8004 0.1872  -0.0325 -0.0267 182 LEU B N   
4371  C  CA  . LEU B 181 ? 0.9763 0.8370 1.7742 0.1819  -0.0387 -0.0223 182 LEU B CA  
4372  C  C   . LEU B 181 ? 1.0050 0.8581 1.7948 0.1834  -0.0348 -0.0337 182 LEU B C   
4373  O  O   . LEU B 181 ? 1.0233 0.8849 1.8066 0.1865  -0.0271 -0.0416 182 LEU B O   
4374  C  CB  . LEU B 181 ? 0.8785 0.7423 1.6694 0.1713  -0.0406 -0.0119 182 LEU B CB  
4375  C  CG  . LEU B 181 ? 0.8322 0.6874 1.6265 0.1685  -0.0486 0.0007  182 LEU B CG  
4376  C  CD1 . LEU B 181 ? 0.7954 0.6534 1.6002 0.1757  -0.0536 0.0060  182 LEU B CD1 
4377  C  CD2 . LEU B 181 ? 0.7936 0.6534 1.5783 0.1592  -0.0486 0.0094  182 LEU B CD2 
4378  N  N   . LEU B 182 ? 1.0045 0.8420 1.7950 0.1818  -0.0398 -0.0348 183 LEU B N   
4379  C  CA  . LEU B 182 ? 0.9642 0.7949 1.7460 0.1824  -0.0373 -0.0461 183 LEU B CA  
4380  C  C   . LEU B 182 ? 0.9056 0.7280 1.6842 0.1720  -0.0414 -0.0415 183 LEU B C   
4381  O  O   . LEU B 182 ? 0.8689 0.6793 1.6565 0.1696  -0.0480 -0.0364 183 LEU B O   
4382  C  CB  . LEU B 182 ? 0.9730 0.7923 1.7603 0.1932  -0.0393 -0.0569 183 LEU B CB  
4383  C  CG  . LEU B 182 ? 0.9642 0.7924 1.7525 0.2053  -0.0330 -0.0643 183 LEU B CG  
4384  C  CD1 . LEU B 182 ? 0.9727 0.8050 1.7752 0.2090  -0.0359 -0.0567 183 LEU B CD1 
4385  C  CD2 . LEU B 182 ? 1.0042 0.8219 1.7892 0.2161  -0.0321 -0.0790 183 LEU B CD2 
4386  N  N   . LEU B 183 ? 0.9061 0.7353 1.6729 0.1660  -0.0369 -0.0430 184 LEU B N   
4387  C  CA  . LEU B 183 ? 0.9037 0.7276 1.6679 0.1558  -0.0399 -0.0385 184 LEU B CA  
4388  C  C   . LEU B 183 ? 0.9111 0.7297 1.6668 0.1564  -0.0387 -0.0510 184 LEU B C   
4389  O  O   . LEU B 183 ? 0.8964 0.7236 1.6397 0.1575  -0.0324 -0.0566 184 LEU B O   
4390  C  CB  . LEU B 183 ? 0.8970 0.7331 1.6548 0.1472  -0.0369 -0.0280 184 LEU B CB  
4391  C  CG  . LEU B 183 ? 0.8958 0.7377 1.6594 0.1462  -0.0389 -0.0151 184 LEU B CG  
4392  C  CD1 . LEU B 183 ? 0.9033 0.7568 1.6685 0.1532  -0.0353 -0.0178 184 LEU B CD1 
4393  C  CD2 . LEU B 183 ? 0.9005 0.7486 1.6576 0.1367  -0.0383 -0.0048 184 LEU B CD2 
4394  N  N   . PRO B 184 ? 0.9987 0.8027 1.7616 0.1561  -0.0452 -0.0555 185 PRO B N   
4395  C  CA  . PRO B 184 ? 1.0419 0.8396 1.7977 0.1565  -0.0461 -0.0677 185 PRO B CA  
4396  C  C   . PRO B 184 ? 1.0761 0.8786 1.8262 0.1454  -0.0454 -0.0626 185 PRO B C   
4397  O  O   . PRO B 184 ? 1.0646 0.8765 1.8135 0.1385  -0.0426 -0.0503 185 PRO B O   
4398  C  CB  . PRO B 184 ? 1.0246 0.8057 1.7948 0.1582  -0.0548 -0.0721 185 PRO B CB  
4399  C  CG  . PRO B 184 ? 1.0174 0.7965 1.8017 0.1536  -0.0580 -0.0571 185 PRO B CG  
4400  C  CD  . PRO B 184 ? 0.9720 0.7641 1.7509 0.1566  -0.0522 -0.0501 185 PRO B CD  
4401  N  N   . ASP B 185 ? 1.1303 0.9263 1.8770 0.1442  -0.0483 -0.0723 186 ASP B N   
4402  C  CA  . ASP B 185 ? 1.1280 0.9282 1.8702 0.1342  -0.0480 -0.0684 186 ASP B CA  
4403  C  C   . ASP B 185 ? 1.1190 0.9166 1.8760 0.1238  -0.0521 -0.0542 186 ASP B C   
4404  O  O   . ASP B 185 ? 1.0919 0.8974 1.8456 0.1154  -0.0494 -0.0447 186 ASP B O   
4405  C  CB  . ASP B 185 ? 1.1567 0.9495 1.8937 0.1365  -0.0517 -0.0831 186 ASP B CB  
4406  N  N   . ASP B 186 ? 1.0781 0.8644 1.8511 0.1251  -0.0582 -0.0524 187 ASP B N   
4407  C  CA  . ASP B 186 ? 1.0278 0.8102 1.8161 0.1167  -0.0616 -0.0382 187 ASP B CA  
4408  C  C   . ASP B 186 ? 0.8914 0.6829 1.6764 0.1141  -0.0570 -0.0220 187 ASP B C   
4409  O  O   . ASP B 186 ? 0.8477 0.6439 1.6330 0.1061  -0.0553 -0.0104 187 ASP B O   
4410  C  CB  . ASP B 186 ? 1.0733 0.8411 1.8800 0.1200  -0.0686 -0.0398 187 ASP B CB  
4411  N  N   . TYR B 187 ? 0.8245 0.6186 1.6066 0.1216  -0.0553 -0.0218 188 TYR B N   
4412  C  CA  . TYR B 187 ? 0.8413 0.6435 1.6207 0.1207  -0.0525 -0.0080 188 TYR B CA  
4413  C  C   . TYR B 187 ? 0.8658 0.6819 1.6309 0.1157  -0.0468 -0.0051 188 TYR B C   
4414  O  O   . TYR B 187 ? 0.8511 0.6722 1.6145 0.1109  -0.0456 0.0078  188 TYR B O   
4415  C  CB  . TYR B 187 ? 0.8160 0.6195 1.5963 0.1303  -0.0524 -0.0106 188 TYR B CB  
4416  C  CG  . TYR B 187 ? 0.8023 0.6080 1.5861 0.1310  -0.0535 0.0041  188 TYR B CG  
4417  C  CD1 . TYR B 187 ? 0.7745 0.5920 1.5491 0.1274  -0.0503 0.0129  188 TYR B CD1 
4418  C  CD2 . TYR B 187 ? 0.8230 0.6183 1.6189 0.1359  -0.0583 0.0088  188 TYR B CD2 
4419  C  CE1 . TYR B 187 ? 0.7634 0.5822 1.5397 0.1294  -0.0523 0.0256  188 TYR B CE1 
4420  C  CE2 . TYR B 187 ? 0.8275 0.6241 1.6251 0.1377  -0.0599 0.0222  188 TYR B CE2 
4421  C  CZ  . TYR B 187 ? 0.7740 0.5824 1.5612 0.1348  -0.0572 0.0304  188 TYR B CZ  
4422  O  OH  . TYR B 187 ? 0.8078 0.6169 1.5950 0.1380  -0.0597 0.0431  188 TYR B OH  
4423  N  N   . LEU B 188 ? 0.8407 0.6625 1.5953 0.1176  -0.0431 -0.0170 189 LEU B N   
4424  C  CA  . LEU B 188 ? 0.8249 0.6595 1.5667 0.1131  -0.0374 -0.0152 189 LEU B CA  
4425  C  C   . LEU B 188 ? 0.8313 0.6657 1.5726 0.1036  -0.0379 -0.0097 189 LEU B C   
4426  O  O   . LEU B 188 ? 0.8098 0.6531 1.5448 0.0983  -0.0347 -0.0013 189 LEU B O   
4427  C  CB  . LEU B 188 ? 0.8050 0.6446 1.5356 0.1185  -0.0328 -0.0288 189 LEU B CB  
4428  C  CG  . LEU B 188 ? 0.8007 0.6478 1.5290 0.1266  -0.0286 -0.0313 189 LEU B CG  
4429  C  CD1 . LEU B 188 ? 0.7855 0.6374 1.5020 0.1324  -0.0225 -0.0433 189 LEU B CD1 
4430  C  CD2 . LEU B 188 ? 0.7854 0.6440 1.5133 0.1226  -0.0265 -0.0196 189 LEU B CD2 
4431  N  N   . ASP B 189 ? 0.8001 0.6246 1.5492 0.1016  -0.0422 -0.0149 190 ASP B N   
4432  C  CA  . ASP B 189 ? 0.7754 0.5998 1.5279 0.0927  -0.0431 -0.0095 190 ASP B CA  
4433  C  C   . ASP B 189 ? 0.7172 0.5413 1.4774 0.0880  -0.0432 0.0081  190 ASP B C   
4434  O  O   . ASP B 189 ? 0.6946 0.5260 1.4499 0.0820  -0.0399 0.0172  190 ASP B O   
4435  C  CB  . ASP B 189 ? 0.8001 0.6135 1.5633 0.0922  -0.0490 -0.0192 190 ASP B CB  
4436  N  N   . CYS B 190 ? 0.6893 0.5047 1.4607 0.0918  -0.0468 0.0129  191 CYS B N   
4437  C  CA  . CYS B 190 ? 0.6827 0.4960 1.4601 0.0896  -0.0469 0.0301  191 CYS B CA  
4438  C  C   . CYS B 190 ? 0.6281 0.4525 1.3916 0.0901  -0.0426 0.0384  191 CYS B C   
4439  O  O   . CYS B 190 ? 0.6274 0.4550 1.3882 0.0857  -0.0404 0.0507  191 CYS B O   
4440  C  CB  . CYS B 190 ? 0.6985 0.5007 1.4881 0.0955  -0.0513 0.0328  191 CYS B CB  
4441  S  SG  . CYS B 190 ? 0.7872 0.5851 1.5818 0.0953  -0.0512 0.0549  191 CYS B SG  
4442  N  N   . LEU B 191 ? 0.6188 0.4492 1.3744 0.0958  -0.0416 0.0313  192 LEU B N   
4443  C  CA  . LEU B 191 ? 0.5891 0.4309 1.3334 0.0967  -0.0386 0.0366  192 LEU B CA  
4444  C  C   . LEU B 191 ? 0.5656 0.4166 1.2996 0.0899  -0.0343 0.0376  192 LEU B C   
4445  O  O   . LEU B 191 ? 0.5706 0.4273 1.2982 0.0882  -0.0329 0.0477  192 LEU B O   
4446  C  CB  . LEU B 191 ? 0.5291 0.3767 1.2700 0.1035  -0.0377 0.0266  192 LEU B CB  
4447  C  CG  . LEU B 191 ? 0.6338 0.4954 1.3643 0.1033  -0.0339 0.0266  192 LEU B CG  
4448  C  CD1 . LEU B 191 ? 0.6145 0.4790 1.3436 0.1045  -0.0363 0.0394  192 LEU B CD1 
4449  C  CD2 . LEU B 191 ? 0.6406 0.5075 1.3709 0.1095  -0.0317 0.0154  192 LEU B CD2 
4450  N  N   . GLY B 192 ? 0.4976 0.3497 1.2295 0.0870  -0.0326 0.0268  193 GLY B N   
4451  C  CA  . GLY B 192 ? 0.4788 0.3394 1.2014 0.0810  -0.0286 0.0266  193 GLY B CA  
4452  C  C   . GLY B 192 ? 0.7479 0.6057 1.4752 0.0752  -0.0289 0.0389  193 GLY B C   
4453  O  O   . GLY B 192 ? 0.7790 0.6439 1.4990 0.0705  -0.0256 0.0441  193 GLY B O   
4454  N  N   . LYS B 193 ? 0.7725 0.6197 1.5127 0.0757  -0.0325 0.0439  194 LYS B N   
4455  C  CA  . LYS B 193 ? 0.7774 0.6219 1.5244 0.0701  -0.0316 0.0557  194 LYS B CA  
4456  C  C   . LYS B 193 ? 0.7922 0.6360 1.5359 0.0728  -0.0308 0.0716  194 LYS B C   
4457  O  O   . LYS B 193 ? 0.7860 0.6294 1.5306 0.0696  -0.0283 0.0844  194 LYS B O   
4458  C  CB  . LYS B 193 ? 0.8538 0.6875 1.6184 0.0684  -0.0355 0.0535  194 LYS B CB  
4459  C  CG  . LYS B 193 ? 0.8993 0.7335 1.6720 0.0613  -0.0336 0.0618  194 LYS B CG  
4460  C  CD  . LYS B 193 ? 0.9465 0.7800 1.7264 0.0578  -0.0362 0.0485  194 LYS B CD  
4461  C  CE  . LYS B 193 ? 1.0064 0.8294 1.7980 0.0614  -0.0424 0.0379  194 LYS B CE  
4462  N  NZ  . LYS B 193 ? 1.0214 0.8453 1.8079 0.0625  -0.0452 0.0193  194 LYS B NZ  
4463  N  N   . GLN B 194 ? 0.7759 0.6203 1.5148 0.0794  -0.0328 0.0706  195 GLN B N   
4464  C  CA  . GLN B 194 ? 0.7370 0.5816 1.4697 0.0839  -0.0332 0.0837  195 GLN B CA  
4465  C  C   . GLN B 194 ? 0.7036 0.5601 1.4213 0.0830  -0.0305 0.0842  195 GLN B C   
4466  O  O   . GLN B 194 ? 0.6321 0.4899 1.3419 0.0867  -0.0311 0.0945  195 GLN B O   
4467  C  CB  . GLN B 194 ? 0.7511 0.5913 1.4873 0.0919  -0.0377 0.0817  195 GLN B CB  
4468  C  CG  . GLN B 194 ? 0.8097 0.6372 1.5613 0.0934  -0.0409 0.0812  195 GLN B CG  
4469  C  CD  . GLN B 194 ? 0.8471 0.6653 1.6034 0.0958  -0.0421 0.0982  195 GLN B CD  
4470  O  OE1 . GLN B 194 ? 0.8713 0.6923 1.6170 0.0983  -0.0411 0.1101  195 GLN B OE1 
4471  N  NE2 . GLN B 194 ? 0.8969 0.7034 1.6685 0.0960  -0.0445 0.0997  195 GLN B NE2 
4472  N  N   . ALA B 195 ? 0.6807 0.5450 1.3941 0.0787  -0.0277 0.0730  196 ALA B N   
4473  C  CA  . ALA B 195 ? 0.7872 0.6628 1.4880 0.0775  -0.0251 0.0721  196 ALA B CA  
4474  C  C   . ALA B 195 ? 0.8605 0.7370 1.5545 0.0757  -0.0232 0.0856  196 ALA B C   
4475  O  O   . ALA B 195 ? 0.8277 0.7091 1.5119 0.0791  -0.0240 0.0905  196 ALA B O   
4476  C  CB  . ALA B 195 ? 0.7153 0.5975 1.4132 0.0728  -0.0218 0.0596  196 ALA B CB  
4477  N  N   . GLU B 196 ? 1.0011 0.8730 1.7009 0.0709  -0.0208 0.0915  197 GLU B N   
4478  C  CA  . GLU B 196 ? 1.0410 0.9123 1.7359 0.0701  -0.0179 0.1062  197 GLU B CA  
4479  C  C   . GLU B 196 ? 1.0231 0.8865 1.7169 0.0774  -0.0206 0.1195  197 GLU B C   
4480  O  O   . GLU B 196 ? 1.0912 0.9476 1.7935 0.0809  -0.0242 0.1182  197 GLU B O   
4481  C  CB  . GLU B 196 ? 1.1536 1.0222 1.8589 0.0632  -0.0144 0.1093  197 GLU B CB  
4482  C  CG  . GLU B 196 ? 1.2335 1.1082 1.9413 0.0570  -0.0133 0.0952  197 GLU B CG  
4483  C  CD  . GLU B 196 ? 1.2980 1.1816 1.9967 0.0528  -0.0087 0.0970  197 GLU B CD  
4484  O  OE1 . GLU B 196 ? 1.3253 1.2106 2.0149 0.0551  -0.0064 0.1083  197 GLU B OE1 
4485  O  OE2 . GLU B 196 ? 1.2932 1.1815 1.9934 0.0481  -0.0077 0.0870  197 GLU B OE2 
4486  N  N   . ALA B 197 ? 0.9126 0.7770 1.5949 0.0808  -0.0190 0.1322  198 ALA B N   
4487  C  CA  . ALA B 197 ? 0.8982 0.7548 1.5758 0.0893  -0.0213 0.1469  198 ALA B CA  
4488  C  C   . ALA B 197 ? 0.8505 0.7078 1.5236 0.0976  -0.0284 0.1421  198 ALA B C   
4489  O  O   . ALA B 197 ? 0.9212 0.7728 1.5883 0.1063  -0.0318 0.1530  198 ALA B O   
4490  C  CB  . ALA B 197 ? 0.9103 0.7557 1.6023 0.0880  -0.0198 0.1562  198 ALA B CB  
4491  N  N   . LEU B 198 ? 0.8095 0.6739 1.4856 0.0954  -0.0303 0.1262  199 LEU B N   
4492  C  CA  . LEU B 198 ? 0.7337 0.6016 1.4086 0.1021  -0.0362 0.1196  199 LEU B CA  
4493  C  C   . LEU B 198 ? 0.6409 0.5204 1.3049 0.1028  -0.0372 0.1144  199 LEU B C   
4494  O  O   . LEU B 198 ? 0.6256 0.5073 1.2820 0.1108  -0.0426 0.1186  199 LEU B O   
4495  C  CB  . LEU B 198 ? 0.7345 0.6020 1.4222 0.1001  -0.0371 0.1063  199 LEU B CB  
4496  C  CG  . LEU B 198 ? 0.7756 0.6312 1.4734 0.1046  -0.0402 0.1112  199 LEU B CG  
4497  C  CD1 . LEU B 198 ? 0.7948 0.6504 1.5036 0.1051  -0.0418 0.0975  199 LEU B CD1 
4498  C  CD2 . LEU B 198 ? 0.8054 0.6572 1.4967 0.1145  -0.0453 0.1231  199 LEU B CD2 
4499  N  N   . ARG B 199 ? 0.6426 0.5297 1.3069 0.0950  -0.0327 0.1048  200 ARG B N   
4500  C  CA  . ARG B 199 ? 0.5915 0.4902 1.2492 0.0941  -0.0331 0.0972  200 ARG B CA  
4501  C  C   . ARG B 199 ? 0.6172 0.5219 1.2804 0.0979  -0.0374 0.0877  200 ARG B C   
4502  O  O   . ARG B 199 ? 0.6068 0.5160 1.2658 0.1040  -0.0428 0.0891  200 ARG B O   
4503  C  CB  . ARG B 199 ? 0.6613 0.5616 1.3056 0.0988  -0.0352 0.1069  200 ARG B CB  
4504  C  CG  . ARG B 199 ? 0.7532 0.6540 1.3904 0.0934  -0.0293 0.1121  200 ARG B CG  
4505  C  CD  . ARG B 199 ? 0.8092 0.7124 1.4320 0.1003  -0.0323 0.1201  200 ARG B CD  
4506  N  NE  . ARG B 199 ? 0.8183 0.7268 1.4345 0.0950  -0.0273 0.1195  200 ARG B NE  
4507  C  CZ  . ARG B 199 ? 0.8544 0.7631 1.4574 0.1002  -0.0276 0.1283  200 ARG B CZ  
4508  N  NH1 . ARG B 199 ? 0.8513 0.7555 1.4452 0.1116  -0.0329 0.1387  200 ARG B NH1 
4509  N  NH2 . ARG B 199 ? 0.8118 0.7254 1.4102 0.0952  -0.0227 0.1268  200 ARG B NH2 
4510  N  N   . PRO B 200 ? 0.5840 0.4890 1.2570 0.0951  -0.0351 0.0779  201 PRO B N   
4511  C  CA  . PRO B 200 ? 0.5957 0.5069 1.2758 0.0985  -0.0374 0.0689  201 PRO B CA  
4512  C  C   . PRO B 200 ? 0.4252 0.3487 1.1024 0.0961  -0.0364 0.0626  201 PRO B C   
4513  O  O   . PRO B 200 ? 0.5104 0.4403 1.1924 0.1004  -0.0405 0.0595  201 PRO B O   
4514  C  CB  . PRO B 200 ? 0.4417 0.3496 1.1300 0.0957  -0.0333 0.0602  201 PRO B CB  
4515  C  CG  . PRO B 200 ? 0.4340 0.3392 1.1180 0.0885  -0.0284 0.0607  201 PRO B CG  
4516  C  CD  . PRO B 200 ? 0.4404 0.3408 1.1180 0.0888  -0.0300 0.0737  201 PRO B CD  
4517  N  N   . PHE B 201 ? 0.4359 0.3628 1.1069 0.0893  -0.0312 0.0607  202 PHE B N   
4518  C  CA  . PHE B 201 ? 0.4444 0.3821 1.1132 0.0863  -0.0296 0.0552  202 PHE B CA  
4519  C  C   . PHE B 201 ? 0.4573 0.3973 1.1167 0.0881  -0.0337 0.0618  202 PHE B C   
4520  O  O   . PHE B 201 ? 0.5225 0.4706 1.1798 0.0856  -0.0333 0.0578  202 PHE B O   
4521  C  CB  . PHE B 201 ? 0.4253 0.3655 1.0917 0.0787  -0.0219 0.0489  202 PHE B CB  
4522  C  CG  . PHE B 201 ? 0.4377 0.3768 1.1110 0.0785  -0.0179 0.0407  202 PHE B CG  
4523  C  CD1 . PHE B 201 ? 0.4491 0.3947 1.1298 0.0809  -0.0169 0.0341  202 PHE B CD1 
4524  C  CD2 . PHE B 201 ? 0.4297 0.3612 1.1026 0.0765  -0.0153 0.0395  202 PHE B CD2 
4525  C  CE1 . PHE B 201 ? 0.3833 0.3276 1.0687 0.0824  -0.0126 0.0268  202 PHE B CE1 
4526  C  CE2 . PHE B 201 ? 0.4418 0.3715 1.1194 0.0779  -0.0124 0.0310  202 PHE B CE2 
4527  C  CZ  . PHE B 201 ? 0.5145 0.4505 1.1972 0.0814  -0.0107 0.0248  202 PHE B CZ  
4528  N  N   . GLY B 202 ? 0.4089 0.3412 1.0626 0.0932  -0.0376 0.0721  203 GLY B N   
4529  C  CA  . GLY B 202 ? 0.4123 0.3453 1.0545 0.0970  -0.0413 0.0794  203 GLY B CA  
4530  C  C   . GLY B 202 ? 0.6027 0.5365 1.2369 0.0905  -0.0352 0.0809  203 GLY B C   
4531  O  O   . GLY B 202 ? 0.6219 0.5503 1.2567 0.0856  -0.0294 0.0837  203 GLY B O   
4532  N  N   . GLU B 203 ? 0.6384 0.5793 1.2665 0.0906  -0.0368 0.0786  204 GLU B N   
4533  C  CA  . GLU B 203 ? 0.6613 0.6032 1.2810 0.0857  -0.0317 0.0807  204 GLU B CA  
4534  C  C   . GLU B 203 ? 0.6178 0.5676 1.2414 0.0772  -0.0266 0.0702  204 GLU B C   
4535  O  O   . GLU B 203 ? 0.6788 0.6306 1.2962 0.0730  -0.0226 0.0705  204 GLU B O   
4536  C  CB  . GLU B 203 ? 0.7094 0.6525 1.3171 0.0931  -0.0371 0.0866  204 GLU B CB  
4537  C  CG  . GLU B 203 ? 0.8593 0.7937 1.4591 0.1025  -0.0404 0.0999  204 GLU B CG  
4538  C  CD  . GLU B 203 ? 0.9682 0.9041 1.5537 0.1121  -0.0461 0.1056  204 GLU B CD  
4539  O  OE1 . GLU B 203 ? 0.9947 0.9327 1.5729 0.1096  -0.0420 0.1068  204 GLU B OE1 
4540  O  OE2 . GLU B 203 ? 1.0272 0.9625 1.6084 0.1230  -0.0552 0.1087  204 GLU B OE2 
4541  N  N   . ALA B 204 ? 0.6534 0.6074 1.2871 0.0753  -0.0263 0.0616  205 ALA B N   
4542  C  CA  . ALA B 204 ? 0.6347 0.5956 1.2718 0.0683  -0.0208 0.0528  205 ALA B CA  
4543  C  C   . ALA B 204 ? 0.6114 0.5698 1.2455 0.0617  -0.0130 0.0520  205 ALA B C   
4544  O  O   . ALA B 204 ? 0.6305 0.5930 1.2601 0.0569  -0.0092 0.0495  205 ALA B O   
4545  C  CB  . ALA B 204 ? 0.6682 0.6333 1.3172 0.0689  -0.0208 0.0456  205 ALA B CB  
4546  N  N   . PRO B 205 ? 0.5699 0.5214 1.2069 0.0616  -0.0113 0.0536  206 PRO B N   
4547  C  CA  . PRO B 205 ? 0.5544 0.5042 1.1899 0.0558  -0.0054 0.0513  206 PRO B CA  
4548  C  C   . PRO B 205 ? 0.5794 0.5287 1.2074 0.0528  -0.0034 0.0573  206 PRO B C   
4549  O  O   . PRO B 205 ? 0.5734 0.5261 1.1987 0.0477  0.0010  0.0534  206 PRO B O   
4550  C  CB  . PRO B 205 ? 0.5524 0.4940 1.1942 0.0576  -0.0062 0.0524  206 PRO B CB  
4551  C  CG  . PRO B 205 ? 0.5623 0.5034 1.2098 0.0634  -0.0106 0.0517  206 PRO B CG  
4552  C  CD  . PRO B 205 ? 0.6028 0.5480 1.2460 0.0667  -0.0150 0.0563  206 PRO B CD  
4553  N  N   . ARG B 206 ? 0.5457 0.4907 1.1702 0.0566  -0.0063 0.0672  207 ARG B N   
4554  C  CA  . ARG B 206 ? 0.5818 0.5260 1.1997 0.0549  -0.0036 0.0744  207 ARG B CA  
4555  C  C   . ARG B 206 ? 0.5546 0.5060 1.1651 0.0535  -0.0029 0.0712  207 ARG B C   
4556  O  O   . ARG B 206 ? 0.5706 0.5246 1.1785 0.0484  0.0017  0.0698  207 ARG B O   
4557  C  CB  . ARG B 206 ? 0.6371 0.5744 1.2514 0.0612  -0.0062 0.0871  207 ARG B CB  
4558  C  CG  . ARG B 206 ? 0.7087 0.6456 1.3149 0.0616  -0.0031 0.0961  207 ARG B CG  
4559  C  CD  . ARG B 206 ? 0.7525 0.6815 1.3551 0.0687  -0.0042 0.1104  207 ARG B CD  
4560  N  NE  . ARG B 206 ? 0.7916 0.7207 1.3847 0.0713  -0.0008 0.1201  207 ARG B NE  
4561  C  CZ  . ARG B 206 ? 0.8161 0.7470 1.3967 0.0797  -0.0047 0.1235  207 ARG B CZ  
4562  N  NH1 . ARG B 206 ? 0.8159 0.7492 1.3940 0.0857  -0.0129 0.1176  207 ARG B NH1 
4563  N  NH2 . ARG B 206 ? 0.8195 0.7503 1.3910 0.0829  -0.0007 0.1326  207 ARG B NH2 
4564  N  N   . GLU B 207 ? 0.5494 0.5041 1.1578 0.0584  -0.0082 0.0695  208 GLU B N   
4565  C  CA  . GLU B 207 ? 0.5415 0.5031 1.1454 0.0576  -0.0091 0.0649  208 GLU B CA  
4566  C  C   . GLU B 207 ? 0.5343 0.5010 1.1414 0.0498  -0.0034 0.0563  208 GLU B C   
4567  O  O   . GLU B 207 ? 0.5161 0.4855 1.1181 0.0462  -0.0001 0.0554  208 GLU B O   
4568  C  CB  . GLU B 207 ? 0.6254 0.5905 1.2316 0.0634  -0.0167 0.0617  208 GLU B CB  
4569  C  CG  . GLU B 207 ? 0.7632 0.7264 1.3609 0.0727  -0.0237 0.0686  208 GLU B CG  
4570  C  CD  . GLU B 207 ? 0.8777 0.8478 1.4770 0.0766  -0.0315 0.0620  208 GLU B CD  
4571  O  OE1 . GLU B 207 ? 0.8944 0.8701 1.5040 0.0717  -0.0310 0.0534  208 GLU B OE1 
4572  O  OE2 . GLU B 207 ? 0.9368 0.9068 1.5276 0.0850  -0.0381 0.0656  208 GLU B OE2 
4573  N  N   . LEU B 208 ? 0.4954 0.4629 1.1103 0.0483  -0.0022 0.0504  209 LEU B N   
4574  C  CA  . LEU B 208 ? 0.4588 0.4302 1.0755 0.0428  0.0035  0.0431  209 LEU B CA  
4575  C  C   . LEU B 208 ? 0.4318 0.4013 1.0441 0.0384  0.0084  0.0440  209 LEU B C   
4576  O  O   . LEU B 208 ? 0.4483 0.4217 1.0571 0.0345  0.0122  0.0406  209 LEU B O   
4577  C  CB  . LEU B 208 ? 0.3938 0.3647 1.0183 0.0439  0.0046  0.0379  209 LEU B CB  
4578  C  CG  . LEU B 208 ? 0.2870 0.2611 0.9117 0.0404  0.0111  0.0311  209 LEU B CG  
4579  C  CD1 . LEU B 208 ? 0.3121 0.2928 0.9373 0.0382  0.0125  0.0288  209 LEU B CD1 
4580  C  CD2 . LEU B 208 ? 0.3034 0.2758 0.9343 0.0433  0.0127  0.0266  209 LEU B CD2 
4581  N  N   . ARG B 209 ? 0.4753 0.4389 1.0890 0.0392  0.0080  0.0487  210 ARG B N   
4582  C  CA  . ARG B 209 ? 0.4149 0.3770 1.0276 0.0352  0.0117  0.0496  210 ARG B CA  
4583  C  C   . ARG B 209 ? 0.4434 0.4086 1.0494 0.0331  0.0135  0.0534  210 ARG B C   
4584  O  O   . ARG B 209 ? 0.5074 0.4764 1.1108 0.0292  0.0170  0.0491  210 ARG B O   
4585  C  CB  . ARG B 209 ? 0.4606 0.4156 1.0789 0.0365  0.0103  0.0554  210 ARG B CB  
4586  N  N   . LEU B 210 ? 0.4091 0.3723 1.0117 0.0369  0.0112  0.0616  211 LEU B N   
4587  C  CA  . LEU B 210 ? 0.4868 0.4521 1.0823 0.0366  0.0129  0.0659  211 LEU B CA  
4588  C  C   . LEU B 210 ? 0.5175 0.4891 1.1089 0.0342  0.0136  0.0585  211 LEU B C   
4589  O  O   . LEU B 210 ? 0.5608 0.5353 1.1499 0.0299  0.0176  0.0565  211 LEU B O   
4590  C  CB  . LEU B 210 ? 0.5487 0.5105 1.1388 0.0439  0.0093  0.0749  211 LEU B CB  
4591  C  CG  . LEU B 210 ? 0.6395 0.5947 1.2309 0.0467  0.0109  0.0867  211 LEU B CG  
4592  C  CD1 . LEU B 210 ? 0.7080 0.6614 1.2892 0.0545  0.0096  0.0964  211 LEU B CD1 
4593  C  CD2 . LEU B 210 ? 0.5978 0.5530 1.1956 0.0402  0.0168  0.0882  211 LEU B CD2 
4594  N  N   . ARG B 211 ? 0.4286 0.4025 1.0206 0.0368  0.0095  0.0545  212 ARG B N   
4595  C  CA  . ARG B 211 ? 0.4044 0.3838 0.9946 0.0349  0.0094  0.0486  212 ARG B CA  
4596  C  C   . ARG B 211 ? 0.3085 0.2908 0.9008 0.0289  0.0150  0.0423  212 ARG B C   
4597  O  O   . ARG B 211 ? 0.3043 0.2896 0.8930 0.0259  0.0174  0.0399  212 ARG B O   
4598  C  CB  . ARG B 211 ? 0.4268 0.4082 1.0213 0.0389  0.0034  0.0455  212 ARG B CB  
4599  C  CG  . ARG B 211 ? 0.4928 0.4718 1.0830 0.0469  -0.0035 0.0511  212 ARG B CG  
4600  C  CD  . ARG B 211 ? 0.5883 0.5712 1.1834 0.0509  -0.0110 0.0463  212 ARG B CD  
4601  N  NE  . ARG B 211 ? 0.6887 0.6698 1.2773 0.0604  -0.0188 0.0510  212 ARG B NE  
4602  C  CZ  . ARG B 211 ? 0.8093 0.7943 1.3996 0.0657  -0.0274 0.0466  212 ARG B CZ  
4603  N  NH1 . ARG B 211 ? 0.8096 0.8002 1.4101 0.0611  -0.0286 0.0381  212 ARG B NH1 
4604  N  NH2 . ARG B 211 ? 0.8539 0.8374 1.4362 0.0762  -0.0351 0.0511  212 ARG B NH2 
4605  N  N   . ALA B 212 ? 0.2877 0.2685 0.8849 0.0281  0.0168  0.0396  213 ALA B N   
4606  C  CA  . ALA B 212 ? 0.3014 0.2840 0.8985 0.0246  0.0220  0.0339  213 ALA B CA  
4607  C  C   . ALA B 212 ? 0.3637 0.3457 0.9564 0.0216  0.0250  0.0349  213 ALA B C   
4608  O  O   . ALA B 212 ? 0.4081 0.3926 0.9973 0.0189  0.0286  0.0315  213 ALA B O   
4609  C  CB  . ALA B 212 ? 0.3046 0.2848 0.9067 0.0264  0.0228  0.0304  213 ALA B CB  
4610  N  N   . THR B 213 ? 0.3700 0.3487 0.9640 0.0222  0.0237  0.0399  214 THR B N   
4611  C  CA  . THR B 213 ? 0.3927 0.3718 0.9855 0.0193  0.0262  0.0413  214 THR B CA  
4612  C  C   . THR B 213 ? 0.3359 0.3189 0.9226 0.0177  0.0279  0.0425  214 THR B C   
4613  O  O   . THR B 213 ? 0.3710 0.3566 0.9549 0.0148  0.0308  0.0388  214 THR B O   
4614  C  CB  . THR B 213 ? 0.4137 0.3890 1.0116 0.0201  0.0252  0.0484  214 THR B CB  
4615  O  OG1 . THR B 213 ? 0.4605 0.4339 1.0563 0.0237  0.0231  0.0558  214 THR B OG1 
4616  C  CG2 . THR B 213 ? 0.3901 0.3608 0.9951 0.0210  0.0234  0.0459  214 THR B CG2 
4617  N  N   . ARG B 214 ? 0.3594 0.3419 0.9433 0.0205  0.0256  0.0474  215 ARG B N   
4618  C  CA  . ARG B 214 ? 0.3978 0.3830 0.9756 0.0202  0.0263  0.0482  215 ARG B CA  
4619  C  C   . ARG B 214 ? 0.3113 0.3001 0.8871 0.0173  0.0275  0.0411  215 ARG B C   
4620  O  O   . ARG B 214 ? 0.3377 0.3286 0.9103 0.0144  0.0306  0.0395  215 ARG B O   
4621  C  CB  . ARG B 214 ? 0.4160 0.3994 0.9901 0.0260  0.0222  0.0530  215 ARG B CB  
4622  C  CG  . ARG B 214 ? 0.4738 0.4528 1.0478 0.0296  0.0226  0.0627  215 ARG B CG  
4623  C  CD  . ARG B 214 ? 0.6064 0.5829 1.1757 0.0378  0.0175  0.0677  215 ARG B CD  
4624  N  NE  . ARG B 214 ? 0.7543 0.7319 1.3152 0.0426  0.0172  0.0707  215 ARG B NE  
4625  C  CZ  . ARG B 214 ? 0.8170 0.7981 1.3736 0.0450  0.0130  0.0644  215 ARG B CZ  
4626  N  NH1 . ARG B 214 ? 0.8515 0.8353 1.4129 0.0421  0.0096  0.0559  215 ARG B NH1 
4627  N  NH2 . ARG B 214 ? 0.8592 0.8414 1.4079 0.0507  0.0125  0.0666  215 ARG B NH2 
4628  N  N   . ALA B 215 ? 0.2272 0.2167 0.8064 0.0183  0.0255  0.0376  216 ALA B N   
4629  C  CA  . ALA B 215 ? 0.2565 0.2488 0.8364 0.0159  0.0272  0.0325  216 ALA B CA  
4630  C  C   . ALA B 215 ? 0.3187 0.3116 0.8970 0.0127  0.0329  0.0295  216 ALA B C   
4631  O  O   . ALA B 215 ? 0.3568 0.3512 0.9314 0.0103  0.0356  0.0282  216 ALA B O   
4632  C  CB  . ALA B 215 ? 0.2356 0.2286 0.8227 0.0177  0.0246  0.0301  216 ALA B CB  
4633  N  N   . PHE B 216 ? 0.2661 0.2570 0.8465 0.0136  0.0341  0.0282  217 PHE B N   
4634  C  CA  . PHE B 216 ? 0.3050 0.2952 0.8824 0.0129  0.0385  0.0245  217 PHE B CA  
4635  C  C   . PHE B 216 ? 0.2648 0.2555 0.8377 0.0108  0.0395  0.0252  217 PHE B C   
4636  O  O   . PHE B 216 ? 0.2167 0.2078 0.7849 0.0099  0.0428  0.0227  217 PHE B O   
4637  C  CB  . PHE B 216 ? 0.3145 0.3013 0.8946 0.0157  0.0382  0.0222  217 PHE B CB  
4638  C  CG  . PHE B 216 ? 0.4080 0.3946 0.9917 0.0183  0.0397  0.0199  217 PHE B CG  
4639  C  CD1 . PHE B 216 ? 0.4682 0.4550 1.0491 0.0196  0.0451  0.0168  217 PHE B CD1 
4640  C  CD2 . PHE B 216 ? 0.4215 0.4078 1.0119 0.0201  0.0360  0.0215  217 PHE B CD2 
4641  C  CE1 . PHE B 216 ? 0.4264 0.4136 1.0122 0.0225  0.0476  0.0156  217 PHE B CE1 
4642  C  CE2 . PHE B 216 ? 0.4110 0.3978 1.0066 0.0226  0.0375  0.0195  217 PHE B CE2 
4643  C  CZ  . PHE B 216 ? 0.4270 0.4145 1.0209 0.0236  0.0437  0.0166  217 PHE B CZ  
4644  N  N   . VAL B 217 ? 0.2584 0.2489 0.8331 0.0104  0.0371  0.0292  218 VAL B N   
4645  C  CA  . VAL B 217 ? 0.2107 0.2023 0.7838 0.0085  0.0383  0.0301  218 VAL B CA  
4646  C  C   . VAL B 217 ? 0.3320 0.3263 0.9000 0.0068  0.0399  0.0309  218 VAL B C   
4647  O  O   . VAL B 217 ? 0.3044 0.2999 0.8694 0.0051  0.0419  0.0294  218 VAL B O   
4648  C  CB  . VAL B 217 ? 0.3048 0.2955 0.8836 0.0088  0.0366  0.0356  218 VAL B CB  
4649  C  CG1 . VAL B 217 ? 0.2149 0.2062 0.7919 0.0099  0.0361  0.0418  218 VAL B CG1 
4650  C  CG2 . VAL B 217 ? 0.2543 0.2463 0.8361 0.0070  0.0375  0.0347  218 VAL B CG2 
4651  N  N   . ALA B 218 ? 0.3998 0.3945 0.9670 0.0077  0.0382  0.0324  219 ALA B N   
4652  C  CA  . ALA B 218 ? 0.3004 0.2965 0.8632 0.0066  0.0387  0.0319  219 ALA B CA  
4653  C  C   . ALA B 218 ? 0.3039 0.3007 0.8650 0.0046  0.0420  0.0279  219 ALA B C   
4654  O  O   . ALA B 218 ? 0.2506 0.2480 0.8077 0.0030  0.0442  0.0273  219 ALA B O   
4655  C  CB  . ALA B 218 ? 0.2046 0.2004 0.7680 0.0092  0.0346  0.0328  219 ALA B CB  
4656  N  N   . ALA B 219 ? 0.3292 0.3254 0.8937 0.0054  0.0427  0.0260  220 ALA B N   
4657  C  CA  . ALA B 219 ? 0.3413 0.3372 0.9050 0.0047  0.0471  0.0238  220 ALA B CA  
4658  C  C   . ALA B 219 ? 0.3094 0.3042 0.8668 0.0052  0.0506  0.0225  220 ALA B C   
4659  O  O   . ALA B 219 ? 0.2994 0.2943 0.8526 0.0043  0.0534  0.0223  220 ALA B O   
4660  C  CB  . ALA B 219 ? 0.2040 0.1993 0.7735 0.0064  0.0483  0.0228  220 ALA B CB  
4661  N  N   . ARG B 220 ? 0.2027 0.1960 0.7602 0.0071  0.0495  0.0212  221 ARG B N   
4662  C  CA  . ARG B 220 ? 0.3937 0.3849 0.9461 0.0087  0.0507  0.0184  221 ARG B CA  
4663  C  C   . ARG B 220 ? 0.3445 0.3373 0.8945 0.0063  0.0500  0.0195  221 ARG B C   
4664  O  O   . ARG B 220 ? 0.2601 0.2517 0.8044 0.0074  0.0519  0.0177  221 ARG B O   
4665  C  CB  . ARG B 220 ? 0.3092 0.2977 0.8647 0.0108  0.0477  0.0162  221 ARG B CB  
4666  C  CG  . ARG B 220 ? 0.2968 0.2815 0.8474 0.0139  0.0475  0.0114  221 ARG B CG  
4667  C  CD  . ARG B 220 ? 0.3371 0.3180 0.8925 0.0159  0.0433  0.0083  221 ARG B CD  
4668  N  NE  . ARG B 220 ? 0.3462 0.3293 0.9107 0.0122  0.0397  0.0120  221 ARG B NE  
4669  C  CZ  . ARG B 220 ? 0.4972 0.4784 1.0694 0.0126  0.0365  0.0127  221 ARG B CZ  
4670  N  NH1 . ARG B 220 ? 0.5335 0.5102 1.1051 0.0162  0.0359  0.0090  221 ARG B NH1 
4671  N  NH2 . ARG B 220 ? 0.5046 0.4880 1.0854 0.0100  0.0345  0.0177  221 ARG B NH2 
4672  N  N   . SER B 221 ? 0.1959 0.1910 0.7497 0.0040  0.0475  0.0227  222 SER B N   
4673  C  CA  . SER B 221 ? 0.2808 0.2777 0.8335 0.0022  0.0475  0.0242  222 SER B CA  
4674  C  C   . SER B 221 ? 0.2794 0.2761 0.8238 0.0020  0.0495  0.0239  222 SER B C   
4675  O  O   . SER B 221 ? 0.1883 0.1848 0.7282 0.0019  0.0504  0.0231  222 SER B O   
4676  C  CB  . SER B 221 ? 0.3102 0.3082 0.8652 0.0022  0.0454  0.0286  222 SER B CB  
4677  O  OG  . SER B 221 ? 0.4213 0.4195 0.9857 0.0023  0.0438  0.0299  222 SER B OG  
4678  N  N   . PHE B 222 ? 0.2569 0.2536 0.8009 0.0019  0.0498  0.0244  223 PHE B N   
4679  C  CA  . PHE B 222 ? 0.2243 0.2207 0.7629 0.0018  0.0514  0.0240  223 PHE B CA  
4680  C  C   . PHE B 222 ? 0.2335 0.2288 0.7712 0.0021  0.0559  0.0231  223 PHE B C   
4681  O  O   . PHE B 222 ? 0.2482 0.2432 0.7811 0.0022  0.0573  0.0232  223 PHE B O   
4682  C  CB  . PHE B 222 ? 0.1896 0.1863 0.7326 0.0016  0.0500  0.0241  223 PHE B CB  
4683  C  CG  . PHE B 222 ? 0.3633 0.3598 0.9038 0.0013  0.0504  0.0234  223 PHE B CG  
4684  C  CD1 . PHE B 222 ? 0.2443 0.2412 0.7821 0.0012  0.0478  0.0232  223 PHE B CD1 
4685  C  CD2 . PHE B 222 ? 0.3117 0.3075 0.8552 0.0013  0.0539  0.0235  223 PHE B CD2 
4686  C  CE1 . PHE B 222 ? 0.2283 0.2250 0.7661 0.0009  0.0476  0.0219  223 PHE B CE1 
4687  C  CE2 . PHE B 222 ? 0.2588 0.2545 0.8023 0.0010  0.0541  0.0233  223 PHE B CE2 
4688  C  CZ  . PHE B 222 ? 0.2596 0.2558 0.8002 0.0007  0.0504  0.0219  223 PHE B CZ  
4689  N  N   . VAL B 223 ? 0.1931 0.1874 0.7346 0.0036  0.0584  0.0224  224 VAL B N   
4690  C  CA  . VAL B 223 ? 0.2615 0.2536 0.7975 0.0073  0.0632  0.0217  224 VAL B CA  
4691  C  C   . VAL B 223 ? 0.2632 0.2540 0.7923 0.0095  0.0619  0.0195  224 VAL B C   
4692  O  O   . VAL B 223 ? 0.2657 0.2555 0.7891 0.0117  0.0645  0.0199  224 VAL B O   
4693  C  CB  . VAL B 223 ? 0.2468 0.2372 0.7838 0.0112  0.0656  0.0205  224 VAL B CB  
4694  C  CG1 . VAL B 223 ? 0.2707 0.2582 0.7990 0.0177  0.0696  0.0189  224 VAL B CG1 
4695  C  CG2 . VAL B 223 ? 0.2059 0.1973 0.7508 0.0097  0.0684  0.0231  224 VAL B CG2 
4696  N  N   . GLN B 224 ? 0.2000 0.1907 0.7314 0.0091  0.0574  0.0174  225 GLN B N   
4697  C  CA  . GLN B 224 ? 0.2935 0.2828 0.8224 0.0106  0.0546  0.0146  225 GLN B CA  
4698  C  C   . GLN B 224 ? 0.2105 0.2018 0.7383 0.0080  0.0544  0.0164  225 GLN B C   
4699  O  O   . GLN B 224 ? 0.1998 0.1896 0.7225 0.0108  0.0542  0.0146  225 GLN B O   
4700  C  CB  . GLN B 224 ? 0.2020 0.1916 0.7386 0.0091  0.0498  0.0132  225 GLN B CB  
4701  C  CG  . GLN B 224 ? 0.4821 0.4671 1.0178 0.0137  0.0479  0.0083  225 GLN B CG  
4702  C  CD  . GLN B 224 ? 0.5114 0.4966 1.0574 0.0116  0.0435  0.0081  225 GLN B CD  
4703  O  OE1 . GLN B 224 ? 0.4831 0.4721 1.0370 0.0077  0.0418  0.0114  225 GLN B OE1 
4704  N  NE2 . GLN B 224 ? 0.5375 0.5186 1.0839 0.0150  0.0421  0.0046  225 GLN B NE2 
4705  N  N   . GLY B 225 ? 0.1897 0.1841 0.7218 0.0037  0.0540  0.0196  226 GLY B N   
4706  C  CA  . GLY B 225 ? 0.2892 0.2846 0.8189 0.0021  0.0540  0.0211  226 GLY B CA  
4707  C  C   . GLY B 225 ? 0.2944 0.2886 0.8188 0.0036  0.0574  0.0214  226 GLY B C   
4708  O  O   . GLY B 225 ? 0.1881 0.1819 0.7090 0.0047  0.0573  0.0210  226 GLY B O   
4709  N  N   . LEU B 226 ? 0.1891 0.1827 0.7138 0.0041  0.0606  0.0227  227 LEU B N   
4710  C  CA  . LEU B 226 ? 0.2457 0.2381 0.7671 0.0062  0.0651  0.0244  227 LEU B CA  
4711  C  C   . LEU B 226 ? 0.2719 0.2621 0.7853 0.0121  0.0665  0.0231  227 LEU B C   
4712  O  O   . LEU B 226 ? 0.2895 0.2794 0.7988 0.0141  0.0676  0.0242  227 LEU B O   
4713  C  CB  . LEU B 226 ? 0.2047 0.1967 0.7308 0.0062  0.0690  0.0265  227 LEU B CB  
4714  C  CG  . LEU B 226 ? 0.2377 0.2308 0.7680 0.0030  0.0670  0.0272  227 LEU B CG  
4715  C  CD1 . LEU B 226 ? 0.1949 0.1876 0.7321 0.0032  0.0696  0.0286  227 LEU B CD1 
4716  C  CD2 . LEU B 226 ? 0.1913 0.1843 0.7188 0.0029  0.0675  0.0283  227 LEU B CD2 
4717  N  N   . GLY B 227 ? 0.2051 0.1936 0.7164 0.0159  0.0658  0.0203  228 GLY B N   
4718  C  CA  . GLY B 227 ? 0.2738 0.2593 0.7768 0.0233  0.0656  0.0173  228 GLY B CA  
4719  C  C   . GLY B 227 ? 0.2790 0.2646 0.7807 0.0234  0.0605  0.0148  228 GLY B C   
4720  O  O   . GLY B 227 ? 0.3430 0.3270 0.8376 0.0292  0.0611  0.0143  228 GLY B O   
4721  N  N   . VAL B 228 ? 0.2155 0.2031 0.7249 0.0176  0.0558  0.0137  229 VAL B N   
4722  C  CA  . VAL B 228 ? 0.2537 0.2422 0.7658 0.0167  0.0511  0.0117  229 VAL B CA  
4723  C  C   . VAL B 228 ? 0.2654 0.2554 0.7746 0.0159  0.0531  0.0148  229 VAL B C   
4724  O  O   . VAL B 228 ? 0.2431 0.2324 0.7490 0.0197  0.0509  0.0131  229 VAL B O   
4725  C  CB  . VAL B 228 ? 0.2451 0.2362 0.7686 0.0105  0.0476  0.0120  229 VAL B CB  
4726  C  CG1 . VAL B 228 ? 0.2646 0.2574 0.7936 0.0088  0.0442  0.0115  229 VAL B CG1 
4727  C  CG2 . VAL B 228 ? 0.2780 0.2673 0.8063 0.0117  0.0444  0.0085  229 VAL B CG2 
4728  N  N   . ALA B 229 ? 0.2483 0.2400 0.7591 0.0116  0.0564  0.0187  230 ALA B N   
4729  C  CA  . ALA B 229 ? 0.2732 0.2657 0.7819 0.0110  0.0582  0.0213  230 ALA B CA  
4730  C  C   . ALA B 229 ? 0.3243 0.3147 0.8254 0.0175  0.0614  0.0224  230 ALA B C   
4731  O  O   . ALA B 229 ? 0.3332 0.3236 0.8312 0.0202  0.0604  0.0226  230 ALA B O   
4732  C  CB  . ALA B 229 ? 0.2607 0.2541 0.7730 0.0066  0.0604  0.0239  230 ALA B CB  
4733  N  N   . SER B 230 ? 0.3372 0.3259 0.8357 0.0208  0.0657  0.0238  231 SER B N   
4734  C  CA  . SER B 230 ? 0.3848 0.3713 0.8757 0.0287  0.0704  0.0261  231 SER B CA  
4735  C  C   . SER B 230 ? 0.3538 0.3384 0.8373 0.0361  0.0660  0.0220  231 SER B C   
4736  O  O   . SER B 230 ? 0.4152 0.3990 0.8931 0.0416  0.0671  0.0240  231 SER B O   
4737  C  CB  . SER B 230 ? 0.4205 0.4055 0.9102 0.0322  0.0760  0.0278  231 SER B CB  
4738  O  OG  . SER B 230 ? 0.4650 0.4476 0.9459 0.0422  0.0813  0.0303  231 SER B OG  
4739  N  N   . ASP B 231 ? 0.2265 0.2104 0.7114 0.0364  0.0603  0.0162  232 ASP B N   
4740  C  CA  . ASP B 231 ? 0.2728 0.2546 0.7534 0.0434  0.0540  0.0104  232 ASP B CA  
4741  C  C   . ASP B 231 ? 0.2968 0.2809 0.7811 0.0413  0.0493  0.0099  232 ASP B C   
4742  O  O   . ASP B 231 ? 0.2405 0.2232 0.7187 0.0491  0.0466  0.0081  232 ASP B O   
4743  C  CB  . ASP B 231 ? 0.3152 0.2954 0.8009 0.0425  0.0480  0.0038  232 ASP B CB  
4744  C  CG  . ASP B 231 ? 0.5101 0.4868 0.9896 0.0483  0.0514  0.0023  232 ASP B CG  
4745  O  OD1 . ASP B 231 ? 0.6240 0.5994 1.0940 0.0559  0.0581  0.0056  232 ASP B OD1 
4746  O  OD2 . ASP B 231 ? 0.5935 0.5691 1.0787 0.0458  0.0480  -0.0016 232 ASP B OD2 
4747  N  N   . VAL B 232 ? 0.2190 0.2066 0.7128 0.0318  0.0483  0.0115  233 VAL B N   
4748  C  CA  . VAL B 232 ? 0.2855 0.2757 0.7840 0.0298  0.0445  0.0111  233 VAL B CA  
4749  C  C   . VAL B 232 ? 0.2805 0.2707 0.7721 0.0332  0.0484  0.0155  233 VAL B C   
4750  O  O   . VAL B 232 ? 0.3384 0.3292 0.8286 0.0373  0.0450  0.0143  233 VAL B O   
4751  C  CB  . VAL B 232 ? 0.4118 0.4053 0.9212 0.0204  0.0439  0.0124  233 VAL B CB  
4752  C  CG1 . VAL B 232 ? 0.3527 0.3459 0.8701 0.0171  0.0414  0.0100  233 VAL B CG1 
4753  C  CG2 . VAL B 232 ? 0.4781 0.4722 0.9859 0.0160  0.0495  0.0174  233 VAL B CG2 
4754  N  N   . VAL B 233 ? 0.2875 0.2770 0.7763 0.0317  0.0553  0.0205  234 VAL B N   
4755  C  CA  . VAL B 233 ? 0.2203 0.2091 0.7048 0.0350  0.0596  0.0254  234 VAL B CA  
4756  C  C   . VAL B 233 ? 0.2569 0.2427 0.7314 0.0466  0.0599  0.0256  234 VAL B C   
4757  O  O   . VAL B 233 ? 0.2496 0.2352 0.7207 0.0514  0.0587  0.0271  234 VAL B O   
4758  C  CB  . VAL B 233 ? 0.2817 0.2700 0.7688 0.0313  0.0666  0.0307  234 VAL B CB  
4759  C  CG1 . VAL B 233 ? 0.2543 0.2412 0.7391 0.0355  0.0716  0.0365  234 VAL B CG1 
4760  C  CG2 . VAL B 233 ? 0.2059 0.1966 0.7015 0.0220  0.0651  0.0298  234 VAL B CG2 
4761  N  N   . ARG B 234 ? 0.3098 0.2931 0.7789 0.0522  0.0614  0.0239  235 ARG B N   
4762  C  CA  . ARG B 234 ? 0.3788 0.3586 0.8361 0.0657  0.0624  0.0240  235 ARG B CA  
4763  C  C   . ARG B 234 ? 0.4027 0.3821 0.8575 0.0720  0.0525  0.0173  235 ARG B C   
4764  O  O   . ARG B 234 ? 0.4056 0.3832 0.8519 0.0825  0.0522  0.0189  235 ARG B O   
4765  C  CB  . ARG B 234 ? 0.4115 0.3887 0.8635 0.0713  0.0659  0.0224  235 ARG B CB  
4766  C  CG  . ARG B 234 ? 0.5132 0.4865 0.9509 0.0876  0.0684  0.0228  235 ARG B CG  
4767  C  CD  . ARG B 234 ? 0.5965 0.5677 1.0288 0.0935  0.0745  0.0225  235 ARG B CD  
4768  N  NE  . ARG B 234 ? 0.6241 0.5948 1.0612 0.0891  0.0672  0.0134  235 ARG B NE  
4769  C  CZ  . ARG B 234 ? 0.6619 0.6296 1.0954 0.0958  0.0576  0.0034  235 ARG B CZ  
4770  N  NH1 . ARG B 234 ? 0.6723 0.6377 1.0964 0.1083  0.0533  0.0004  235 ARG B NH1 
4771  N  NH2 . ARG B 234 ? 0.6626 0.6295 1.1031 0.0905  0.0516  -0.0038 235 ARG B NH2 
4772  N  N   . LYS B 235 ? 0.3448 0.3262 0.8087 0.0659  0.0445  0.0103  236 LYS B N   
4773  C  CA  . LYS B 235 ? 0.3628 0.3445 0.8289 0.0708  0.0339  0.0030  236 LYS B CA  
4774  C  C   . LYS B 235 ? 0.3757 0.3613 0.8472 0.0676  0.0313  0.0052  236 LYS B C   
4775  O  O   . LYS B 235 ? 0.4303 0.4157 0.8988 0.0759  0.0251  0.0023  236 LYS B O   
4776  C  CB  . LYS B 235 ? 0.2874 0.2697 0.7650 0.0647  0.0264  -0.0046 236 LYS B CB  
4777  C  CG  . LYS B 235 ? 0.3247 0.3024 0.7969 0.0697  0.0268  -0.0089 236 LYS B CG  
4778  C  CD  . LYS B 235 ? 0.3247 0.3014 0.8086 0.0668  0.0166  -0.0181 236 LYS B CD  
4779  C  CE  . LYS B 235 ? 0.4561 0.4271 0.9328 0.0738  0.0159  -0.0238 236 LYS B CE  
4780  N  NZ  . LYS B 235 ? 0.5284 0.4974 1.0179 0.0713  0.0049  -0.0335 236 LYS B NZ  
4781  N  N   . VAL B 236 ? 0.3397 0.3286 0.8189 0.0566  0.0356  0.0097  237 VAL B N   
4782  C  CA  . VAL B 236 ? 0.3285 0.3209 0.8123 0.0540  0.0341  0.0117  237 VAL B CA  
4783  C  C   . VAL B 236 ? 0.3504 0.3404 0.8239 0.0617  0.0387  0.0176  237 VAL B C   
4784  O  O   . VAL B 236 ? 0.3080 0.2995 0.7818 0.0651  0.0352  0.0180  237 VAL B O   
4785  C  CB  . VAL B 236 ? 0.2649 0.2604 0.7579 0.0420  0.0377  0.0144  237 VAL B CB  
4786  C  CG1 . VAL B 236 ? 0.2675 0.2655 0.7631 0.0406  0.0377  0.0168  237 VAL B CG1 
4787  C  CG2 . VAL B 236 ? 0.2608 0.2584 0.7653 0.0355  0.0333  0.0100  237 VAL B CG2 
4788  N  N   . ALA B 237 ? 0.4388 0.4251 0.9043 0.0648  0.0466  0.0228  238 ALA B N   
4789  C  CA  . ALA B 237 ? 0.4462 0.4297 0.9038 0.0721  0.0528  0.0304  238 ALA B CA  
4790  C  C   . ALA B 237 ? 0.4942 0.4755 0.9419 0.0864  0.0480  0.0294  238 ALA B C   
4791  O  O   . ALA B 237 ? 0.5458 0.5253 0.9886 0.0923  0.0508  0.0356  238 ALA B O   
4792  C  CB  . ALA B 237 ? 0.4516 0.4321 0.9052 0.0730  0.0628  0.0365  238 ALA B CB  
4793  N  N   . GLN B 238 ? 0.5060 0.4869 0.9512 0.0925  0.0402  0.0212  239 GLN B N   
4794  C  CA  . GLN B 238 ? 0.5666 0.5452 1.0020 0.1080  0.0337  0.0185  239 GLN B CA  
4795  C  C   . GLN B 238 ? 0.4957 0.4785 0.9401 0.1070  0.0210  0.0111  239 GLN B C   
4796  O  O   . GLN B 238 ? 0.4725 0.4542 0.9114 0.1194  0.0119  0.0059  239 GLN B O   
4797  C  CB  . GLN B 238 ? 0.7248 0.6993 1.1509 0.1186  0.0319  0.0129  239 GLN B CB  
4798  C  CG  . GLN B 238 ? 0.8622 0.8316 1.2712 0.1342  0.0410  0.0208  239 GLN B CG  
4799  C  CD  . GLN B 238 ? 1.0002 0.9659 1.3961 0.1523  0.0334  0.0130  239 GLN B CD  
4800  O  OE1 . GLN B 238 ? 1.0409 1.0066 1.4393 0.1513  0.0229  0.0006  239 GLN B OE1 
4801  N  NE2 . GLN B 238 ? 1.0503 1.0130 1.4218 0.1662  0.0374  0.0199  239 GLN B NE2 
4802  N  N   . VAL B 239 ? 0.4212 0.4092 0.8798 0.0931  0.0201  0.0104  240 VAL B N   
4803  C  CA  . VAL B 239 ? 0.3707 0.3639 0.8402 0.0911  0.0102  0.0053  240 VAL B CA  
4804  C  C   . VAL B 239 ? 0.3840 0.3772 0.8480 0.0977  0.0109  0.0110  240 VAL B C   
4805  O  O   . VAL B 239 ? 0.3127 0.3051 0.7755 0.0929  0.0196  0.0187  240 VAL B O   
4806  C  CB  . VAL B 239 ? 0.3144 0.3130 0.8003 0.0756  0.0111  0.0043  240 VAL B CB  
4807  C  CG1 . VAL B 239 ? 0.3184 0.3230 0.8158 0.0740  0.0040  0.0017  240 VAL B CG1 
4808  C  CG2 . VAL B 239 ? 0.2788 0.2774 0.7727 0.0701  0.0081  -0.0017 240 VAL B CG2 
4809  N  N   . PRO B 240 ? 0.4854 0.4792 0.9466 0.1091  0.0006  0.0066  241 PRO B N   
4810  C  CA  . PRO B 240 ? 0.4702 0.4634 0.9247 0.1180  0.0000  0.0121  241 PRO B CA  
4811  C  C   . PRO B 240 ? 0.4130 0.4122 0.8805 0.1087  -0.0011 0.0129  241 PRO B C   
4812  O  O   . PRO B 240 ? 0.3699 0.3753 0.8528 0.0992  -0.0060 0.0067  241 PRO B O   
4813  C  CB  . PRO B 240 ? 0.4708 0.4635 0.9197 0.1331  -0.0136 0.0046  241 PRO B CB  
4814  C  CG  . PRO B 240 ? 0.4778 0.4746 0.9407 0.1261  -0.0231 -0.0072 241 PRO B CG  
4815  C  CD  . PRO B 240 ? 0.4507 0.4457 0.9159 0.1147  -0.0125 -0.0048 241 PRO B CD  
4816  N  N   . LEU B 241 ? 0.4651 0.4622 0.9270 0.1118  0.0041  0.0209  242 LEU B N   
4817  C  CA  . LEU B 241 ? 0.5125 0.5147 0.9849 0.1060  0.0023  0.0212  242 LEU B CA  
4818  C  C   . LEU B 241 ? 0.3820 0.3889 0.8585 0.1145  -0.0109 0.0152  242 LEU B C   
4819  O  O   . LEU B 241 ? 0.3991 0.4026 0.8640 0.1289  -0.0167 0.0155  242 LEU B O   
4820  C  CB  . LEU B 241 ? 0.5808 0.5783 1.0470 0.1070  0.0112  0.0310  242 LEU B CB  
4821  C  CG  . LEU B 241 ? 0.6710 0.6655 1.1385 0.0962  0.0228  0.0358  242 LEU B CG  
4822  C  CD1 . LEU B 241 ? 0.6772 0.6665 1.1411 0.0981  0.0297  0.0446  242 LEU B CD1 
4823  C  CD2 . LEU B 241 ? 0.6984 0.6988 1.1794 0.0827  0.0227  0.0304  242 LEU B CD2 
4824  N  N   . GLY B 242 ? 0.2975 0.3123 0.7906 0.1062  -0.0159 0.0100  243 GLY B N   
4825  C  CA  . GLY B 242 ? 0.4101 0.4309 0.9111 0.1125  -0.0289 0.0038  243 GLY B CA  
4826  C  C   . GLY B 242 ? 0.3973 0.4171 0.8916 0.1214  -0.0300 0.0092  243 GLY B C   
4827  O  O   . GLY B 242 ? 0.3964 0.4117 0.8846 0.1195  -0.0199 0.0174  243 GLY B O   
4828  N  N   . PRO B 243 ? 0.4276 0.4511 0.9237 0.1314  -0.0432 0.0042  244 PRO B N   
4829  C  CA  . PRO B 243 ? 0.4794 0.5023 0.9693 0.1417  -0.0465 0.0088  244 PRO B CA  
4830  C  C   . PRO B 243 ? 0.4685 0.4955 0.9698 0.1325  -0.0404 0.0120  244 PRO B C   
4831  O  O   . PRO B 243 ? 0.4744 0.4968 0.9676 0.1375  -0.0356 0.0196  244 PRO B O   
4832  C  CB  . PRO B 243 ? 0.4725 0.5013 0.9676 0.1509  -0.0645 -0.0006 244 PRO B CB  
4833  C  CG  . PRO B 243 ? 0.4629 0.4975 0.9748 0.1404  -0.0695 -0.0106 244 PRO B CG  
4834  C  CD  . PRO B 243 ? 0.3724 0.4007 0.8773 0.1337  -0.0573 -0.0070 244 PRO B CD  
4835  N  N   . GLU B 244 ? 0.4081 0.4433 0.9282 0.1200  -0.0404 0.0064  245 GLU B N   
4836  C  CA  . GLU B 244 ? 0.4365 0.4755 0.9667 0.1117  -0.0339 0.0085  245 GLU B CA  
4837  C  C   . GLU B 244 ? 0.3948 0.4258 0.9146 0.1078  -0.0207 0.0164  245 GLU B C   
4838  O  O   . GLU B 244 ? 0.3721 0.4008 0.8896 0.1099  -0.0171 0.0209  245 GLU B O   
4839  C  CB  . GLU B 244 ? 0.2902 0.3374 0.8400 0.0993  -0.0336 0.0028  245 GLU B CB  
4840  N  N   . CYS B 245 ? 0.2926 0.3193 0.8072 0.1022  -0.0142 0.0174  246 CYS B N   
4841  C  CA  . CYS B 245 ? 0.2886 0.3077 0.7947 0.0982  -0.0027 0.0241  246 CYS B CA  
4842  C  C   . CYS B 245 ? 0.3041 0.3149 0.7965 0.1089  -0.0008 0.0319  246 CYS B C   
4843  O  O   . CYS B 245 ? 0.3039 0.3102 0.7949 0.1067  0.0061  0.0372  246 CYS B O   
4844  C  CB  . CYS B 245 ? 0.3833 0.3994 0.8858 0.0922  0.0022  0.0236  246 CYS B CB  
4845  S  SG  . CYS B 245 ? 1.9190 1.9258 2.4117 0.0886  0.0148  0.0318  246 CYS B SG  
4846  N  N   . SER B 246 ? 0.3541 0.3627 0.8368 0.1211  -0.0073 0.0326  247 SER B N   
4847  C  CA  . SER B 246 ? 0.4271 0.4270 0.8952 0.1333  -0.0051 0.0417  247 SER B CA  
4848  C  C   . SER B 246 ? 0.4541 0.4544 0.9256 0.1367  -0.0070 0.0446  247 SER B C   
4849  O  O   . SER B 246 ? 0.5017 0.4945 0.9683 0.1379  0.0004  0.0530  247 SER B O   
4850  C  CB  . SER B 246 ? 0.5055 0.5038 0.9616 0.1481  -0.0135 0.0409  247 SER B CB  
4851  O  OG  . SER B 246 ? 0.6031 0.5919 1.0429 0.1610  -0.0094 0.0519  247 SER B OG  
4852  N  N   . ARG B 247 ? 0.4474 0.4564 0.9289 0.1379  -0.0169 0.0376  248 ARG B N   
4853  C  CA  . ARG B 247 ? 0.4182 0.4290 0.9049 0.1407  -0.0193 0.0391  248 ARG B CA  
4854  C  C   . ARG B 247 ? 0.4007 0.4103 0.8953 0.1293  -0.0096 0.0406  248 ARG B C   
4855  O  O   . ARG B 247 ? 0.3424 0.3464 0.8348 0.1324  -0.0063 0.0462  248 ARG B O   
4856  C  CB  . ARG B 247 ? 0.4744 0.4966 0.9741 0.1418  -0.0311 0.0304  248 ARG B CB  
4857  C  CG  . ARG B 247 ? 0.5693 0.5931 1.0622 0.1554  -0.0442 0.0277  248 ARG B CG  
4858  C  CD  . ARG B 247 ? 0.6611 0.6963 1.1695 0.1565  -0.0562 0.0198  248 ARG B CD  
4859  N  NE  . ARG B 247 ? 0.7263 0.7710 1.2541 0.1427  -0.0561 0.0117  248 ARG B NE  
4860  C  CZ  . ARG B 247 ? 0.7880 0.8369 1.3220 0.1402  -0.0632 0.0043  248 ARG B CZ  
4861  N  NH1 . ARG B 247 ? 0.7940 0.8504 1.3466 0.1274  -0.0617 -0.0013 248 ARG B NH1 
4862  N  NH2 . ARG B 247 ? 0.8116 0.8564 1.3329 0.1513  -0.0718 0.0026  248 ARG B NH2 
4863  N  N   . ALA B 248 ? 0.3366 0.3509 0.8402 0.1169  -0.0056 0.0353  249 ALA B N   
4864  C  CA  . ALA B 248 ? 0.3232 0.3365 0.8332 0.1073  0.0025  0.0354  249 ALA B CA  
4865  C  C   . ALA B 248 ? 0.3835 0.3859 0.8852 0.1071  0.0108  0.0431  249 ALA B C   
4866  O  O   . ALA B 248 ? 0.3996 0.3984 0.9045 0.1056  0.0144  0.0452  249 ALA B O   
4867  C  CB  . ALA B 248 ? 0.2898 0.3087 0.8075 0.0960  0.0052  0.0297  249 ALA B CB  
4868  N  N   . VAL B 249 ? 0.3140 0.3112 0.8063 0.1087  0.0138  0.0472  250 VAL B N   
4869  C  CA  . VAL B 249 ? 0.3905 0.3780 0.8770 0.1079  0.0225  0.0553  250 VAL B CA  
4870  C  C   . VAL B 249 ? 0.3552 0.3353 0.8360 0.1183  0.0226  0.0638  250 VAL B C   
4871  O  O   . VAL B 249 ? 0.3624 0.3361 0.8464 0.1156  0.0287  0.0691  250 VAL B O   
4872  C  CB  . VAL B 249 ? 0.3193 0.3038 0.7973 0.1084  0.0261  0.0580  250 VAL B CB  
4873  C  CG1 . VAL B 249 ? 0.3277 0.3026 0.8012 0.1092  0.0355  0.0681  250 VAL B CG1 
4874  C  CG2 . VAL B 249 ? 0.3012 0.2913 0.7856 0.0971  0.0273  0.0508  250 VAL B CG2 
4875  N  N   . MET B 250 ? 0.3513 0.3323 0.8243 0.1304  0.0153  0.0651  251 MET B N   
4876  C  CA  . MET B 250 ? 0.4104 0.3846 0.8768 0.1418  0.0142  0.0735  251 MET B CA  
4877  C  C   . MET B 250 ? 0.4436 0.4186 0.9211 0.1381  0.0136  0.0716  251 MET B C   
4878  O  O   . MET B 250 ? 0.3788 0.3455 0.8565 0.1397  0.0184  0.0791  251 MET B O   
4879  C  CB  . MET B 250 ? 0.3862 0.3631 0.8431 0.1562  0.0037  0.0729  251 MET B CB  
4880  C  CG  . MET B 250 ? 0.4606 0.4318 0.9111 0.1688  0.0003  0.0806  251 MET B CG  
4881  S  SD  . MET B 250 ? 0.5481 0.5041 0.9894 0.1724  0.0129  0.0971  251 MET B SD  
4882  C  CE  . MET B 250 ? 0.7237 0.6745 1.1547 0.1902  0.0055  0.1050  251 MET B CE  
4883  N  N   . LYS B 251 ? 0.4322 0.4174 0.9200 0.1332  0.0080  0.0616  252 LYS B N   
4884  C  CA  . LYS B 251 ? 0.4239 0.4112 0.9224 0.1304  0.0074  0.0585  252 LYS B CA  
4885  C  C   . LYS B 251 ? 0.4748 0.4572 0.9796 0.1202  0.0160  0.0588  252 LYS B C   
4886  O  O   . LYS B 251 ? 0.3492 0.3288 0.8606 0.1198  0.0170  0.0588  252 LYS B O   
4887  C  CB  . LYS B 251 ? 0.4679 0.4680 0.9767 0.1271  0.0010  0.0484  252 LYS B CB  
4888  C  CG  . LYS B 251 ? 0.5402 0.5438 1.0570 0.1310  -0.0030 0.0462  252 LYS B CG  
4889  C  CD  . LYS B 251 ? 0.5219 0.5341 1.0517 0.1219  -0.0012 0.0379  252 LYS B CD  
4890  C  CE  . LYS B 251 ? 0.4469 0.4654 0.9856 0.1271  -0.0063 0.0348  252 LYS B CE  
4891  N  NZ  . LYS B 251 ? 0.4357 0.4617 0.9858 0.1198  -0.0028 0.0280  252 LYS B NZ  
4892  N  N   . LEU B 252 ? 0.4781 0.4596 0.9815 0.1126  0.0213  0.0584  253 LEU B N   
4893  C  CA  . LEU B 252 ? 0.3272 0.3051 0.8373 0.1030  0.0281  0.0577  253 LEU B CA  
4894  C  C   . LEU B 252 ? 0.3392 0.3060 0.8483 0.1047  0.0342  0.0674  253 LEU B C   
4895  O  O   . LEU B 252 ? 0.3385 0.3014 0.8567 0.0997  0.0374  0.0669  253 LEU B O   
4896  C  CB  . LEU B 252 ? 0.3121 0.2940 0.8219 0.0944  0.0309  0.0534  253 LEU B CB  
4897  C  CG  . LEU B 252 ? 0.3042 0.2827 0.8199 0.0851  0.0371  0.0526  253 LEU B CG  
4898  C  CD1 . LEU B 252 ? 0.3412 0.3231 0.8657 0.0805  0.0359  0.0447  253 LEU B CD1 
4899  C  CD2 . LEU B 252 ? 0.4048 0.3854 0.9172 0.0794  0.0398  0.0515  253 LEU B CD2 
4900  N  N   . VAL B 253 ? 0.3516 0.3135 0.8504 0.1123  0.0357  0.0764  254 VAL B N   
4901  C  CA  . VAL B 253 ? 0.5354 0.4876 1.0341 0.1126  0.0438  0.0871  254 VAL B CA  
4902  C  C   . VAL B 253 ? 0.5390 0.4829 1.0330 0.1235  0.0442  0.0979  254 VAL B C   
4903  O  O   . VAL B 253 ? 0.6284 0.5651 1.1306 0.1216  0.0495  0.1044  254 VAL B O   
4904  C  CB  . VAL B 253 ? 0.3606 0.3123 0.8512 0.1124  0.0487  0.0914  254 VAL B CB  
4905  C  CG1 . VAL B 253 ? 0.3727 0.3155 0.8648 0.1130  0.0585  0.1040  254 VAL B CG1 
4906  C  CG2 . VAL B 253 ? 0.3397 0.2983 0.8357 0.1011  0.0490  0.0818  254 VAL B CG2 
4907  N  N   . TYR B 254 ? 0.4804 0.4254 0.9622 0.1353  0.0380  0.0999  255 TYR B N   
4908  C  CA  . TYR B 254 ? 0.4671 0.4034 0.9408 0.1475  0.0385  0.1119  255 TYR B CA  
4909  C  C   . TYR B 254 ? 0.5075 0.4455 0.9814 0.1553  0.0294  0.1088  255 TYR B C   
4910  O  O   . TYR B 254 ? 0.5760 0.5068 1.0426 0.1663  0.0286  0.1185  255 TYR B O   
4911  C  CB  . TYR B 254 ? 0.4635 0.3972 0.9192 0.1587  0.0398  0.1202  255 TYR B CB  
4912  C  CG  . TYR B 254 ? 0.5309 0.4599 0.9859 0.1540  0.0515  0.1283  255 TYR B CG  
4913  C  CD1 . TYR B 254 ? 0.5253 0.4474 0.9916 0.1479  0.0612  0.1368  255 TYR B CD1 
4914  C  CD2 . TYR B 254 ? 0.5369 0.4691 0.9818 0.1558  0.0527  0.1272  255 TYR B CD2 
4915  C  CE1 . TYR B 254 ? 0.5366 0.4560 1.0053 0.1433  0.0722  0.1445  255 TYR B CE1 
4916  C  CE2 . TYR B 254 ? 0.5659 0.4946 1.0110 0.1518  0.0640  0.1347  255 TYR B CE2 
4917  C  CZ  . TYR B 254 ? 0.5737 0.4965 1.0313 0.1455  0.0740  0.1436  255 TYR B CZ  
4918  O  OH  . TYR B 254 ? 0.5610 0.4820 1.0219 0.1413  0.0855  0.1513  255 TYR B OH  
4919  N  N   . CYS B 255 ? 0.5082 0.4560 0.9906 0.1501  0.0229  0.0961  256 CYS B N   
4920  C  CA  . CYS B 255 ? 0.5835 0.5344 1.0690 0.1566  0.0148  0.0926  256 CYS B CA  
4921  C  C   . CYS B 255 ? 0.5853 0.5289 1.0810 0.1543  0.0183  0.0955  256 CYS B C   
4922  O  O   . CYS B 255 ? 0.5777 0.5181 1.0724 0.1632  0.0139  0.0989  256 CYS B O   
4923  C  CB  . CYS B 255 ? 0.4981 0.4625 0.9915 0.1513  0.0083  0.0790  256 CYS B CB  
4924  S  SG  . CYS B 255 ? 0.6743 0.6481 1.1588 0.1604  -0.0021 0.0750  256 CYS B SG  
4925  N  N   . ALA B 256 ? 0.5603 0.5013 1.0663 0.1428  0.0253  0.0938  257 ALA B N   
4926  C  CA  . ALA B 256 ? 0.4223 0.3557 0.9401 0.1401  0.0284  0.0959  257 ALA B CA  
4927  C  C   . ALA B 256 ? 0.4855 0.4070 0.9983 0.1488  0.0319  0.1108  257 ALA B C   
4928  O  O   . ALA B 256 ? 0.4637 0.3796 0.9812 0.1537  0.0299  0.1137  257 ALA B O   
4929  C  CB  . ALA B 256 ? 0.4084 0.3412 0.9378 0.1272  0.0345  0.0917  257 ALA B CB  
4930  N  N   . HIS B 257 ? 0.5368 0.4543 1.0397 0.1512  0.0375  0.1207  258 HIS B N   
4931  C  CA  . HIS B 257 ? 0.5430 0.4496 1.0384 0.1606  0.0423  0.1369  258 HIS B CA  
4932  C  C   . HIS B 257 ? 0.5581 0.4634 1.0413 0.1754  0.0339  0.1401  258 HIS B C   
4933  O  O   . HIS B 257 ? 0.5174 0.4137 1.0007 0.1823  0.0350  0.1498  258 HIS B O   
4934  C  CB  . HIS B 257 ? 0.5956 0.5004 1.0797 0.1624  0.0498  0.1462  258 HIS B CB  
4935  C  CG  . HIS B 257 ? 0.5600 0.4661 1.0567 0.1488  0.0584  0.1445  258 HIS B CG  
4936  N  ND1 . HIS B 257 ? 0.5193 0.4341 1.0247 0.1374  0.0555  0.1302  258 HIS B ND1 
4937  C  CD2 . HIS B 257 ? 0.5577 0.4581 1.0606 0.1451  0.0696  0.1557  258 HIS B CD2 
4938  C  CE1 . HIS B 257 ? 0.5579 0.4719 1.0735 0.1278  0.0635  0.1319  258 HIS B CE1 
4939  N  NE2 . HIS B 257 ? 0.5761 0.4821 1.0918 0.1318  0.0722  0.1471  258 HIS B NE2 
4940  N  N   . CYS B 258 ? 0.5694 0.4843 1.0435 0.1803  0.0251  0.1316  259 CYS B N   
4941  C  CA  . CYS B 258 ? 0.5063 0.4221 0.9691 0.1951  0.0152  0.1331  259 CYS B CA  
4942  C  C   . CYS B 258 ? 0.6020 0.5191 1.0765 0.1956  0.0094  0.1273  259 CYS B C   
4943  O  O   . CYS B 258 ? 0.6509 0.5636 1.1191 0.2078  0.0041  0.1332  259 CYS B O   
4944  C  CB  . CYS B 258 ? 0.4970 0.4244 0.9511 0.1992  0.0065  0.1241  259 CYS B CB  
4945  S  SG  . CYS B 258 ? 0.9311 0.8554 1.3648 0.2069  0.0100  0.1328  259 CYS B SG  
4946  N  N   . LEU B 259 ? 0.6072 0.5302 1.0979 0.1832  0.0104  0.1159  260 LEU B N   
4947  C  CA  . LEU B 259 ? 0.5957 0.5215 1.0977 0.1839  0.0052  0.1090  260 LEU B CA  
4948  C  C   . LEU B 259 ? 0.6462 0.5612 1.1604 0.1794  0.0111  0.1130  260 LEU B C   
4949  O  O   . LEU B 259 ? 0.6517 0.5694 1.1788 0.1753  0.0092  0.1043  260 LEU B O   
4950  C  CB  . LEU B 259 ? 0.6468 0.5866 1.1583 0.1753  0.0018  0.0936  260 LEU B CB  
4951  C  CG  . LEU B 259 ? 0.6768 0.6286 1.1809 0.1790  -0.0052 0.0882  260 LEU B CG  
4952  C  CD1 . LEU B 259 ? 0.6754 0.6411 1.1918 0.1713  -0.0081 0.0745  260 LEU B CD1 
4953  C  CD2 . LEU B 259 ? 0.7193 0.6705 1.2130 0.1949  -0.0140 0.0936  260 LEU B CD2 
4954  N  N   . GLY B 260 ? 0.6628 0.5660 1.1740 0.1805  0.0184  0.1263  261 GLY B N   
4955  C  CA  . GLY B 260 ? 0.6358 0.5279 1.1597 0.1782  0.0232  0.1322  261 GLY B CA  
4956  C  C   . GLY B 260 ? 0.6506 0.5418 1.1920 0.1638  0.0294  0.1267  261 GLY B C   
4957  O  O   . GLY B 260 ? 0.6847 0.5683 1.2403 0.1613  0.0312  0.1278  261 GLY B O   
4958  N  N   . VAL B 261 ? 0.6258 0.5244 1.1667 0.1549  0.0320  0.1203  262 VAL B N   
4959  C  CA  . VAL B 261 ? 0.6294 0.5275 1.1859 0.1421  0.0371  0.1151  262 VAL B CA  
4960  C  C   . VAL B 261 ? 0.6530 0.5525 1.2060 0.1360  0.0442  0.1198  262 VAL B C   
4961  O  O   . VAL B 261 ? 0.6581 0.5658 1.2118 0.1281  0.0438  0.1102  262 VAL B O   
4962  C  CB  . VAL B 261 ? 0.6211 0.5285 1.1850 0.1357  0.0320  0.0980  262 VAL B CB  
4963  C  CG1 . VAL B 261 ? 0.6008 0.5044 1.1750 0.1390  0.0277  0.0933  262 VAL B CG1 
4964  C  CG2 . VAL B 261 ? 0.6199 0.5392 1.1713 0.1383  0.0269  0.0910  262 VAL B CG2 
4965  N  N   . PRO B 262 ? 0.7305 0.6221 1.2798 0.1400  0.0513  0.1354  263 PRO B N   
4966  C  CA  . PRO B 262 ? 0.7285 0.6214 1.2740 0.1358  0.0592  0.1415  263 PRO B CA  
4967  C  C   . PRO B 262 ? 0.7594 0.6545 1.3240 0.1221  0.0635  0.1355  263 PRO B C   
4968  O  O   . PRO B 262 ? 0.7462 0.6473 1.3082 0.1163  0.0662  0.1322  263 PRO B O   
4969  C  CB  . PRO B 262 ? 0.7596 0.6424 1.3001 0.1442  0.0668  0.1608  263 PRO B CB  
4970  C  CG  . PRO B 262 ? 0.7436 0.6211 1.2778 0.1553  0.0604  0.1639  263 PRO B CG  
4971  C  CD  . PRO B 262 ? 0.7421 0.6229 1.2906 0.1493  0.0531  0.1489  263 PRO B CD  
4972  N  N   . GLY B 263 ? 0.8283 0.7186 1.4123 0.1176  0.0635  0.1337  264 GLY B N   
4973  C  CA  . GLY B 263 ? 0.8335 0.7257 1.4378 0.1059  0.0661  0.1277  264 GLY B CA  
4974  C  C   . GLY B 263 ? 0.7969 0.6979 1.4017 0.0990  0.0596  0.1100  264 GLY B C   
4975  O  O   . GLY B 263 ? 0.8285 0.7324 1.4467 0.0900  0.0606  0.1038  264 GLY B O   
4976  N  N   . ALA B 264 ? 0.7586 0.6644 1.3497 0.1038  0.0528  0.1022  265 ALA B N   
4977  C  CA  . ALA B 264 ? 0.6769 0.5914 1.2672 0.0986  0.0476  0.0867  265 ALA B CA  
4978  C  C   . ALA B 264 ? 0.6303 0.5520 1.2122 0.0937  0.0503  0.0854  265 ALA B C   
4979  O  O   . ALA B 264 ? 0.6059 0.5278 1.1753 0.0979  0.0534  0.0939  265 ALA B O   
4980  C  CB  . ALA B 264 ? 0.6892 0.6080 1.2700 0.1054  0.0407  0.0801  265 ALA B CB  
4981  N  N   . ARG B 265 ? 0.5732 0.5002 1.1611 0.0856  0.0489  0.0746  266 ARG B N   
4982  C  CA  . ARG B 265 ? 0.5083 0.4423 1.0878 0.0811  0.0506  0.0722  266 ARG B CA  
4983  C  C   . ARG B 265 ? 0.4854 0.4277 1.0587 0.0799  0.0451  0.0594  266 ARG B C   
4984  O  O   . ARG B 265 ? 0.4499 0.3925 1.0293 0.0801  0.0411  0.0508  266 ARG B O   
4985  C  CB  . ARG B 265 ? 0.5081 0.4417 1.1003 0.0728  0.0551  0.0728  266 ARG B CB  
4986  N  N   . PRO B 266 ? 0.4804 0.4294 1.0420 0.0793  0.0452  0.0583  267 PRO B N   
4987  C  CA  . PRO B 266 ? 0.3256 0.2832 0.8814 0.0790  0.0409  0.0483  267 PRO B CA  
4988  C  C   . PRO B 266 ? 0.3466 0.3072 0.9085 0.0725  0.0401  0.0380  267 PRO B C   
4989  O  O   . PRO B 266 ? 0.3123 0.2707 0.8801 0.0667  0.0425  0.0380  267 PRO B O   
4990  C  CB  . PRO B 266 ? 0.4843 0.4468 1.0288 0.0792  0.0419  0.0514  267 PRO B CB  
4991  C  CG  . PRO B 266 ? 0.4312 0.3886 0.9765 0.0765  0.0475  0.0596  267 PRO B CG  
4992  C  CD  . PRO B 266 ? 0.3355 0.2843 0.8894 0.0792  0.0498  0.0667  267 PRO B CD  
4993  N  N   . CYS B 267 ? 0.3132 0.2789 0.8737 0.0745  0.0366  0.0295  268 CYS B N   
4994  C  CA  A CYS B 267 ? 0.3067 0.2753 0.8699 0.0709  0.0357  0.0196  268 CYS B CA  
4995  C  CA  B CYS B 267 ? 0.3064 0.2754 0.8693 0.0710  0.0357  0.0195  268 CYS B CA  
4996  C  C   . CYS B 267 ? 0.5766 0.5498 1.1345 0.0651  0.0378  0.0188  268 CYS B C   
4997  O  O   . CYS B 267 ? 0.2881 0.2653 0.8385 0.0649  0.0389  0.0229  268 CYS B O   
4998  C  CB  A CYS B 267 ? 0.3078 0.2822 0.8690 0.0758  0.0331  0.0121  268 CYS B CB  
4999  C  CB  B CYS B 267 ? 0.3066 0.2821 0.8667 0.0758  0.0332  0.0124  268 CYS B CB  
5000  S  SG  A CYS B 267 ? 0.4421 0.4110 1.0104 0.0831  0.0302  0.0115  268 CYS B SG  
5001  S  SG  B CYS B 267 ? 0.3010 0.2814 0.8600 0.0744  0.0331  0.0009  268 CYS B SG  
5002  N  N   . PRO B 268 ? 0.4905 0.4627 1.0528 0.0608  0.0377  0.0131  269 PRO B N   
5003  C  CA  . PRO B 268 ? 0.3718 0.3479 0.9297 0.0556  0.0394  0.0118  269 PRO B CA  
5004  C  C   . PRO B 268 ? 0.3681 0.3522 0.9165 0.0567  0.0396  0.0094  269 PRO B C   
5005  O  O   . PRO B 268 ? 0.2639 0.2508 0.8072 0.0537  0.0414  0.0130  269 PRO B O   
5006  C  CB  . PRO B 268 ? 0.2810 0.2550 0.8454 0.0538  0.0372  0.0035  269 PRO B CB  
5007  C  CG  . PRO B 268 ? 0.4187 0.3856 0.9948 0.0552  0.0354  0.0041  269 PRO B CG  
5008  C  CD  . PRO B 268 ? 0.3810 0.3475 0.9541 0.0609  0.0354  0.0079  269 PRO B CD  
5009  N  N   . ASP B 269 ? 0.3237 0.3117 0.8711 0.0613  0.0381  0.0036  270 ASP B N   
5010  C  CA  . ASP B 269 ? 0.2685 0.2652 0.8102 0.0624  0.0392  0.0018  270 ASP B CA  
5011  C  C   . ASP B 269 ? 0.3829 0.3833 0.9227 0.0638  0.0387  0.0076  270 ASP B C   
5012  O  O   . ASP B 269 ? 0.4485 0.4548 0.9853 0.0619  0.0395  0.0085  270 ASP B O   
5013  C  CB  . ASP B 269 ? 0.2741 0.2750 0.8164 0.0681  0.0388  -0.0055 270 ASP B CB  
5014  C  CG  . ASP B 269 ? 0.4020 0.4020 0.9432 0.0684  0.0389  -0.0127 270 ASP B CG  
5015  O  OD1 . ASP B 269 ? 0.4068 0.4016 0.9493 0.0636  0.0382  -0.0124 270 ASP B OD1 
5016  O  OD2 . ASP B 269 ? 0.4340 0.4390 0.9732 0.0741  0.0397  -0.0188 270 ASP B OD2 
5017  N  N   . TYR B 270 ? 0.4324 0.4291 0.9748 0.0676  0.0369  0.0112  271 TYR B N   
5018  C  CA  . TYR B 270 ? 0.4028 0.4019 0.9430 0.0704  0.0351  0.0166  271 TYR B CA  
5019  C  C   . TYR B 270 ? 0.2706 0.2682 0.8058 0.0668  0.0363  0.0217  271 TYR B C   
5020  O  O   . TYR B 270 ? 0.2655 0.2686 0.7980 0.0665  0.0352  0.0222  271 TYR B O   
5021  C  CB  . TYR B 270 ? 0.2881 0.2816 0.8311 0.0761  0.0331  0.0203  271 TYR B CB  
5022  C  CG  . TYR B 270 ? 0.2929 0.2880 0.8328 0.0814  0.0302  0.0257  271 TYR B CG  
5023  C  CD1 . TYR B 270 ? 0.2872 0.2912 0.8260 0.0820  0.0278  0.0242  271 TYR B CD1 
5024  C  CD2 . TYR B 270 ? 0.4196 0.4074 0.9587 0.0864  0.0294  0.0325  271 TYR B CD2 
5025  C  CE1 . TYR B 270 ? 0.3862 0.3920 0.9228 0.0878  0.0235  0.0279  271 TYR B CE1 
5026  C  CE2 . TYR B 270 ? 0.4368 0.4258 0.9715 0.0931  0.0259  0.0372  271 TYR B CE2 
5027  C  CZ  . TYR B 270 ? 0.3058 0.3040 0.8391 0.0940  0.0223  0.0343  271 TYR B CZ  
5028  O  OH  . TYR B 270 ? 0.3140 0.3138 0.8436 0.1017  0.0172  0.0378  271 TYR B OH  
5029  N  N   . CYS B 271 ? 0.2725 0.2628 0.8081 0.0642  0.0387  0.0252  272 CYS B N   
5030  C  CA  . CYS B 271 ? 0.3153 0.3038 0.8467 0.0611  0.0410  0.0301  272 CYS B CA  
5031  C  C   . CYS B 271 ? 0.3273 0.3213 0.8559 0.0561  0.0416  0.0262  272 CYS B C   
5032  O  O   . CYS B 271 ? 0.2536 0.2499 0.7775 0.0559  0.0413  0.0285  272 CYS B O   
5033  C  CB  . CYS B 271 ? 0.2716 0.2529 0.8078 0.0580  0.0443  0.0334  272 CYS B CB  
5034  S  SG  . CYS B 271 ? 0.7325 0.7118 1.2649 0.0546  0.0487  0.0399  272 CYS B SG  
5035  N  N   . ARG B 272 ? 0.2526 0.2484 0.7838 0.0530  0.0422  0.0202  273 ARG B N   
5036  C  CA  . ARG B 272 ? 0.2575 0.2577 0.7861 0.0489  0.0433  0.0170  273 ARG B CA  
5037  C  C   . ARG B 272 ? 0.3025 0.3099 0.8300 0.0504  0.0418  0.0165  273 ARG B C   
5038  O  O   . ARG B 272 ? 0.2643 0.2740 0.7897 0.0473  0.0422  0.0173  273 ARG B O   
5039  C  CB  . ARG B 272 ? 0.3507 0.3514 0.8812 0.0481  0.0438  0.0106  273 ARG B CB  
5040  C  CG  . ARG B 272 ? 0.3731 0.3680 0.9067 0.0449  0.0443  0.0097  273 ARG B CG  
5041  C  CD  . ARG B 272 ? 0.4916 0.4866 1.0273 0.0469  0.0430  0.0019  273 ARG B CD  
5042  N  NE  . ARG B 272 ? 0.5399 0.5411 1.0703 0.0477  0.0442  -0.0016 273 ARG B NE  
5043  C  CZ  . ARG B 272 ? 0.6224 0.6258 1.1517 0.0520  0.0438  -0.0084 273 ARG B CZ  
5044  N  NH1 . ARG B 272 ? 0.6381 0.6374 1.1714 0.0555  0.0411  -0.0137 273 ARG B NH1 
5045  N  NH2 . ARG B 272 ? 0.6328 0.6425 1.1572 0.0536  0.0463  -0.0098 273 ARG B NH2 
5046  N  N   . ASN B 273 ? 0.2453 0.2563 0.7758 0.0550  0.0399  0.0150  274 ASN B N   
5047  C  CA  . ASN B 273 ? 0.2432 0.2621 0.7764 0.0563  0.0381  0.0145  274 ASN B CA  
5048  C  C   . ASN B 273 ? 0.2438 0.2624 0.7753 0.0574  0.0347  0.0183  274 ASN B C   
5049  O  O   . ASN B 273 ? 0.2534 0.2763 0.7864 0.0553  0.0334  0.0178  274 ASN B O   
5050  C  CB  . ASN B 273 ? 0.3497 0.3732 0.8881 0.0614  0.0367  0.0122  274 ASN B CB  
5051  C  CG  . ASN B 273 ? 0.3854 0.4153 0.9266 0.0614  0.0400  0.0080  274 ASN B CG  
5052  O  OD1 . ASN B 273 ? 0.4226 0.4542 0.9620 0.0576  0.0429  0.0074  274 ASN B OD1 
5053  N  ND2 . ASN B 273 ? 0.2631 0.2967 0.8083 0.0665  0.0400  0.0054  274 ASN B ND2 
5054  N  N   . VAL B 274 ? 0.2512 0.2643 0.7796 0.0615  0.0334  0.0221  275 VAL B N   
5055  C  CA  . VAL B 274 ? 0.3120 0.3243 0.8365 0.0652  0.0301  0.0257  275 VAL B CA  
5056  C  C   . VAL B 274 ? 0.3361 0.3468 0.8561 0.0609  0.0320  0.0266  275 VAL B C   
5057  O  O   . VAL B 274 ? 0.3497 0.3640 0.8696 0.0617  0.0285  0.0256  275 VAL B O   
5058  C  CB  . VAL B 274 ? 0.2666 0.2718 0.7867 0.0715  0.0299  0.0313  275 VAL B CB  
5059  C  CG1 . VAL B 274 ? 0.2731 0.2771 0.7863 0.0774  0.0268  0.0352  275 VAL B CG1 
5060  C  CG2 . VAL B 274 ? 0.2738 0.2804 0.7985 0.0765  0.0272  0.0304  275 VAL B CG2 
5061  N  N   . LEU B 275 ? 0.2458 0.2515 0.7637 0.0564  0.0368  0.0280  276 LEU B N   
5062  C  CA  . LEU B 275 ? 0.2628 0.2668 0.7768 0.0527  0.0390  0.0292  276 LEU B CA  
5063  C  C   . LEU B 275 ? 0.2315 0.2405 0.7482 0.0474  0.0386  0.0249  276 LEU B C   
5064  O  O   . LEU B 275 ? 0.2290 0.2387 0.7438 0.0463  0.0377  0.0250  276 LEU B O   
5065  C  CB  . LEU B 275 ? 0.2406 0.2384 0.7541 0.0493  0.0439  0.0318  276 LEU B CB  
5066  C  CG  . LEU B 275 ? 0.4075 0.3992 0.9186 0.0542  0.0459  0.0386  276 LEU B CG  
5067  C  CD1 . LEU B 275 ? 0.4974 0.4845 1.0118 0.0498  0.0511  0.0415  276 LEU B CD1 
5068  C  CD2 . LEU B 275 ? 0.4489 0.4403 0.9524 0.0607  0.0443  0.0423  276 LEU B CD2 
5069  N  N   . LYS B 276 ? 0.2281 0.2402 0.7492 0.0449  0.0396  0.0214  277 LYS B N   
5070  C  CA  . LYS B 276 ? 0.2216 0.2383 0.7458 0.0410  0.0402  0.0188  277 LYS B CA  
5071  C  C   . LYS B 276 ? 0.3262 0.3488 0.8561 0.0428  0.0359  0.0179  277 LYS B C   
5072  O  O   . LYS B 276 ? 0.4316 0.4574 0.9659 0.0395  0.0356  0.0168  277 LYS B O   
5073  C  CB  . LYS B 276 ? 0.2207 0.2396 0.7470 0.0402  0.0431  0.0160  277 LYS B CB  
5074  C  CG  . LYS B 276 ? 0.2327 0.2467 0.7553 0.0379  0.0460  0.0152  277 LYS B CG  
5075  C  CD  . LYS B 276 ? 0.2222 0.2383 0.7459 0.0402  0.0476  0.0113  277 LYS B CD  
5076  C  CE  . LYS B 276 ? 0.3166 0.3363 0.8393 0.0388  0.0504  0.0099  277 LYS B CE  
5077  N  NZ  . LYS B 276 ? 0.2237 0.2456 0.7456 0.0429  0.0522  0.0056  277 LYS B NZ  
5078  N  N   . GLY B 277 ? 0.2984 0.3225 0.8297 0.0483  0.0320  0.0183  278 GLY B N   
5079  C  CA  . GLY B 277 ? 0.2313 0.2609 0.7690 0.0510  0.0260  0.0167  278 GLY B CA  
5080  C  C   . GLY B 277 ? 0.2403 0.2674 0.7737 0.0530  0.0223  0.0173  278 GLY B C   
5081  O  O   . GLY B 277 ? 0.2318 0.2627 0.7717 0.0518  0.0181  0.0146  278 GLY B O   
5082  N  N   . CYS B 278 ? 0.2379 0.2585 0.7612 0.0564  0.0240  0.0208  279 CYS B N   
5083  C  CA  . CYS B 278 ? 0.4227 0.4404 0.9392 0.0609  0.0213  0.0218  279 CYS B CA  
5084  C  C   . CYS B 278 ? 0.4081 0.4239 0.9229 0.0553  0.0243  0.0212  279 CYS B C   
5085  O  O   . CYS B 278 ? 0.4178 0.4326 0.9292 0.0588  0.0211  0.0201  279 CYS B O   
5086  C  CB  . CYS B 278 ? 0.4350 0.4458 0.9412 0.0677  0.0237  0.0276  279 CYS B CB  
5087  S  SG  . CYS B 278 ? 0.9838 0.9954 1.4899 0.0773  0.0185  0.0293  279 CYS B SG  
5088  N  N   . LEU B 279 ? 0.3763 0.3913 0.8929 0.0478  0.0298  0.0214  280 LEU B N   
5089  C  CA  . LEU B 279 ? 0.2639 0.2763 0.7782 0.0428  0.0331  0.0215  280 LEU B CA  
5090  C  C   . LEU B 279 ? 0.2868 0.3025 0.8087 0.0361  0.0338  0.0189  280 LEU B C   
5091  O  O   . LEU B 279 ? 0.2551 0.2683 0.7753 0.0314  0.0375  0.0195  280 LEU B O   
5092  C  CB  . LEU B 279 ? 0.3164 0.3235 0.8250 0.0410  0.0393  0.0252  280 LEU B CB  
5093  C  CG  . LEU B 279 ? 0.3232 0.3257 0.8253 0.0474  0.0407  0.0299  280 LEU B CG  
5094  C  CD1 . LEU B 279 ? 0.3213 0.3192 0.8229 0.0439  0.0468  0.0334  280 LEU B CD1 
5095  C  CD2 . LEU B 279 ? 0.3398 0.3407 0.8353 0.0537  0.0387  0.0310  280 LEU B CD2 
5096  N  N   . ALA B 280 ? 0.3069 0.3280 0.8378 0.0363  0.0305  0.0167  281 ALA B N   
5097  C  CA  . ALA B 280 ? 0.2812 0.3052 0.8203 0.0311  0.0323  0.0158  281 ALA B CA  
5098  C  C   . ALA B 280 ? 0.2070 0.2295 0.7493 0.0276  0.0311  0.0149  281 ALA B C   
5099  O  O   . ALA B 280 ? 0.2112 0.2319 0.7540 0.0231  0.0353  0.0163  281 ALA B O   
5100  C  CB  . ALA B 280 ? 0.2985 0.3290 0.8486 0.0325  0.0291  0.0142  281 ALA B CB  
5101  N  N   . ASN B 281 ? 0.2107 0.2338 0.7549 0.0307  0.0250  0.0124  282 ASN B N   
5102  C  CA  . ASN B 281 ? 0.2698 0.2912 0.8176 0.0284  0.0227  0.0105  282 ASN B CA  
5103  C  C   . ASN B 281 ? 0.2928 0.3089 0.8307 0.0259  0.0284  0.0129  282 ASN B C   
5104  O  O   . ASN B 281 ? 0.4437 0.4582 0.9854 0.0211  0.0304  0.0133  282 ASN B O   
5105  C  CB  . ASN B 281 ? 0.2170 0.2392 0.7653 0.0348  0.0144  0.0062  282 ASN B CB  
5106  C  CG  . ASN B 281 ? 0.2208 0.2487 0.7839 0.0361  0.0065  0.0021  282 ASN B CG  
5107  O  OD1 . ASN B 281 ? 0.3109 0.3405 0.8886 0.0315  0.0037  -0.0002 282 ASN B OD1 
5108  N  ND2 . ASN B 281 ? 0.3535 0.3841 0.9142 0.0424  0.0026  0.0015  282 ASN B ND2 
5109  N  N   . GLN B 282 ? 0.2080 0.2213 0.7344 0.0293  0.0311  0.0151  283 GLN B N   
5110  C  CA  . GLN B 282 ? 0.2903 0.2992 0.8091 0.0268  0.0366  0.0176  283 GLN B CA  
5111  C  C   . GLN B 282 ? 0.2390 0.2475 0.7598 0.0211  0.0410  0.0190  283 GLN B C   
5112  O  O   . GLN B 282 ? 0.3185 0.3247 0.8382 0.0176  0.0435  0.0197  283 GLN B O   
5113  C  CB  . GLN B 282 ? 0.2097 0.2157 0.7191 0.0313  0.0393  0.0207  283 GLN B CB  
5114  C  CG  . GLN B 282 ? 0.2187 0.2227 0.7215 0.0390  0.0368  0.0207  283 GLN B CG  
5115  C  CD  . GLN B 282 ? 0.3326 0.3394 0.8373 0.0456  0.0301  0.0183  283 GLN B CD  
5116  O  OE1 . GLN B 282 ? 0.3491 0.3600 0.8617 0.0435  0.0276  0.0168  283 GLN B OE1 
5117  N  NE2 . GLN B 282 ? 0.3426 0.3470 0.8398 0.0546  0.0272  0.0179  283 GLN B NE2 
5118  N  N   . ALA B 283 ? 0.1993 0.2101 0.7224 0.0215  0.0416  0.0191  284 ALA B N   
5119  C  CA  . ALA B 283 ? 0.1967 0.2072 0.7198 0.0189  0.0455  0.0199  284 ALA B CA  
5120  C  C   . ALA B 283 ? 0.1948 0.2062 0.7239 0.0159  0.0463  0.0204  284 ALA B C   
5121  O  O   . ALA B 283 ? 0.1936 0.2042 0.7209 0.0146  0.0499  0.0216  284 ALA B O   
5122  C  CB  . ALA B 283 ? 0.1992 0.2128 0.7235 0.0216  0.0459  0.0194  284 ALA B CB  
5123  N  N   . ASP B 284 ? 0.1958 0.2088 0.7330 0.0154  0.0427  0.0194  285 ASP B N   
5124  C  CA  . ASP B 284 ? 0.3059 0.3186 0.8515 0.0125  0.0436  0.0208  285 ASP B CA  
5125  C  C   . ASP B 284 ? 0.1929 0.2009 0.7353 0.0098  0.0450  0.0218  285 ASP B C   
5126  O  O   . ASP B 284 ? 0.1932 0.1999 0.7410 0.0079  0.0470  0.0242  285 ASP B O   
5127  C  CB  . ASP B 284 ? 0.3453 0.3605 0.9038 0.0124  0.0380  0.0186  285 ASP B CB  
5128  C  CG  . ASP B 284 ? 0.4113 0.4319 0.9782 0.0137  0.0381  0.0192  285 ASP B CG  
5129  O  OD1 . ASP B 284 ? 0.3768 0.3994 0.9404 0.0144  0.0437  0.0221  285 ASP B OD1 
5130  O  OD2 . ASP B 284 ? 0.4015 0.4253 0.9791 0.0145  0.0321  0.0164  285 ASP B OD2 
5131  N  N   . LEU B 285 ? 0.1915 0.1974 0.7259 0.0102  0.0445  0.0206  286 LEU B N   
5132  C  CA  . LEU B 285 ? 0.1893 0.1919 0.7211 0.0079  0.0459  0.0212  286 LEU B CA  
5133  C  C   . LEU B 285 ? 0.1876 0.1886 0.7146 0.0068  0.0501  0.0236  286 LEU B C   
5134  O  O   . LEU B 285 ? 0.1983 0.1970 0.7248 0.0049  0.0512  0.0245  286 LEU B O   
5135  C  CB  . LEU B 285 ? 0.1897 0.1917 0.7148 0.0099  0.0450  0.0198  286 LEU B CB  
5136  C  CG  . LEU B 285 ? 0.2418 0.2450 0.7690 0.0133  0.0402  0.0167  286 LEU B CG  
5137  C  CD1 . LEU B 285 ? 0.2378 0.2398 0.7548 0.0182  0.0412  0.0171  286 LEU B CD1 
5138  C  CD2 . LEU B 285 ? 0.3148 0.3169 0.8480 0.0113  0.0381  0.0149  286 LEU B CD2 
5139  N  N   . ASP B 286 ? 0.2305 0.2333 0.7546 0.0086  0.0520  0.0239  287 ASP B N   
5140  C  CA  . ASP B 286 ? 0.2939 0.2966 0.8132 0.0093  0.0547  0.0242  287 ASP B CA  
5141  C  C   . ASP B 286 ? 0.2359 0.2381 0.7567 0.0087  0.0567  0.0266  287 ASP B C   
5142  O  O   . ASP B 286 ? 0.2459 0.2464 0.7639 0.0079  0.0567  0.0263  287 ASP B O   
5143  C  CB  . ASP B 286 ? 0.1910 0.1974 0.7093 0.0126  0.0560  0.0234  287 ASP B CB  
5144  C  CG  . ASP B 286 ? 0.2898 0.2971 0.8037 0.0148  0.0574  0.0218  287 ASP B CG  
5145  O  OD1 . ASP B 286 ? 0.2315 0.2362 0.7429 0.0142  0.0559  0.0196  287 ASP B OD1 
5146  O  OD2 . ASP B 286 ? 0.2616 0.2730 0.7759 0.0177  0.0600  0.0228  287 ASP B OD2 
5147  N  N   . ALA B 287 ? 0.2106 0.2151 0.7374 0.0094  0.0585  0.0296  288 ALA B N   
5148  C  CA  . ALA B 287 ? 0.1928 0.1983 0.7222 0.0101  0.0616  0.0337  288 ALA B CA  
5149  C  C   . ALA B 287 ? 0.3168 0.3174 0.8477 0.0071  0.0600  0.0344  288 ALA B C   
5150  O  O   . ALA B 287 ? 0.3391 0.3400 0.8670 0.0079  0.0610  0.0353  288 ALA B O   
5151  C  CB  . ALA B 287 ? 0.1966 0.2055 0.7351 0.0110  0.0646  0.0382  288 ALA B CB  
5152  N  N   . GLU B 288 ? 0.2343 0.2314 0.7705 0.0042  0.0571  0.0332  289 GLU B N   
5153  C  CA  . GLU B 288 ? 0.1894 0.1852 0.7246 0.0030  0.0551  0.0328  289 GLU B CA  
5154  C  C   . GLU B 288 ? 0.1862 0.1819 0.7128 0.0025  0.0538  0.0296  289 GLU B C   
5155  O  O   . GLU B 288 ? 0.1858 0.1815 0.7101 0.0023  0.0534  0.0299  289 GLU B O   
5156  C  CB  . GLU B 288 ? 0.1956 0.1915 0.7373 0.0022  0.0512  0.0309  289 GLU B CB  
5157  C  CG  . GLU B 288 ? 0.2390 0.2349 0.7922 0.0026  0.0523  0.0348  289 GLU B CG  
5158  C  CD  . GLU B 288 ? 0.3105 0.3063 0.8659 0.0037  0.0571  0.0414  289 GLU B CD  
5159  O  OE1 . GLU B 288 ? 0.4059 0.4013 0.9565 0.0034  0.0568  0.0417  289 GLU B OE1 
5160  O  OE2 . GLU B 288 ? 0.3963 0.3927 0.9601 0.0049  0.0617  0.0470  289 GLU B OE2 
5161  N  N   . TRP B 289 ? 0.1845 0.1803 0.7083 0.0025  0.0534  0.0272  290 TRP B N   
5162  C  CA  . TRP B 289 ? 0.1987 0.1943 0.7167 0.0024  0.0535  0.0255  290 TRP B CA  
5163  C  C   . TRP B 289 ? 0.1825 0.1780 0.6995 0.0026  0.0546  0.0263  290 TRP B C   
5164  O  O   . TRP B 289 ? 0.1820 0.1775 0.6968 0.0023  0.0540  0.0258  290 TRP B O   
5165  C  CB  . TRP B 289 ? 0.1824 0.1784 0.6990 0.0031  0.0536  0.0242  290 TRP B CB  
5166  C  CG  . TRP B 289 ? 0.1818 0.1773 0.6954 0.0031  0.0546  0.0237  290 TRP B CG  
5167  C  CD1 . TRP B 289 ? 0.1821 0.1776 0.6950 0.0033  0.0550  0.0229  290 TRP B CD1 
5168  C  CD2 . TRP B 289 ? 0.2446 0.2399 0.7574 0.0033  0.0555  0.0241  290 TRP B CD2 
5169  N  NE1 . TRP B 289 ? 0.2078 0.2028 0.7218 0.0026  0.0561  0.0233  290 TRP B NE1 
5170  C  CE2 . TRP B 289 ? 0.2069 0.2018 0.7200 0.0029  0.0572  0.0246  290 TRP B CE2 
5171  C  CE3 . TRP B 289 ? 0.2527 0.2482 0.7651 0.0046  0.0551  0.0237  290 TRP B CE3 
5172  C  CZ2 . TRP B 289 ? 0.2779 0.2723 0.7914 0.0036  0.0598  0.0262  290 TRP B CZ2 
5173  C  CZ3 . TRP B 289 ? 0.2593 0.2541 0.7691 0.0066  0.0574  0.0246  290 TRP B CZ3 
5174  C  CH2 . TRP B 289 ? 0.2491 0.2433 0.7596 0.0059  0.0604  0.0265  290 TRP B CH2 
5175  N  N   . ARG B 290 ? 0.1844 0.1813 0.7016 0.0047  0.0558  0.0269  291 ARG B N   
5176  C  CA  . ARG B 290 ? 0.1863 0.1850 0.7016 0.0073  0.0559  0.0265  291 ARG B CA  
5177  C  C   . ARG B 290 ? 0.2144 0.2133 0.7326 0.0074  0.0565  0.0297  291 ARG B C   
5178  O  O   . ARG B 290 ? 0.2161 0.2154 0.7334 0.0084  0.0549  0.0286  291 ARG B O   
5179  C  CB  . ARG B 290 ? 0.1899 0.1926 0.7034 0.0118  0.0574  0.0261  291 ARG B CB  
5180  C  CG  . ARG B 290 ? 0.3073 0.3101 0.8183 0.0126  0.0560  0.0220  291 ARG B CG  
5181  C  CD  . ARG B 290 ? 0.4006 0.4079 0.9105 0.0171  0.0579  0.0216  291 ARG B CD  
5182  N  NE  . ARG B 290 ? 0.4295 0.4360 0.9384 0.0173  0.0565  0.0182  291 ARG B NE  
5183  C  CZ  . ARG B 290 ? 0.4595 0.4662 0.9675 0.0199  0.0543  0.0136  291 ARG B CZ  
5184  N  NH1 . ARG B 290 ? 0.4749 0.4828 0.9821 0.0231  0.0527  0.0110  291 ARG B NH1 
5185  N  NH2 . ARG B 290 ? 0.4808 0.4864 0.9897 0.0198  0.0533  0.0114  291 ARG B NH2 
5186  N  N   . ASN B 291 ? 0.2810 0.2794 0.8043 0.0065  0.0583  0.0337  292 ASN B N   
5187  C  CA  . ASN B 291 ? 0.2155 0.2136 0.7438 0.0064  0.0592  0.0379  292 ASN B CA  
5188  C  C   . ASN B 291 ? 0.1869 0.1832 0.7146 0.0036  0.0564  0.0356  292 ASN B C   
5189  O  O   . ASN B 291 ? 0.1877 0.1847 0.7171 0.0044  0.0560  0.0369  292 ASN B O   
5190  C  CB  . ASN B 291 ? 0.3388 0.3355 0.8761 0.0051  0.0614  0.0426  292 ASN B CB  
5191  C  CG  . ASN B 291 ? 0.3436 0.3450 0.8824 0.0091  0.0657  0.0469  292 ASN B CG  
5192  O  OD1 . ASN B 291 ? 0.2494 0.2563 0.7834 0.0140  0.0679  0.0479  292 ASN B OD1 
5193  N  ND2 . ASN B 291 ? 0.1981 0.1983 0.7444 0.0079  0.0668  0.0490  292 ASN B ND2 
5194  N  N   . LEU B 292 ? 0.1852 0.1812 0.7075 0.0026  0.0543  0.0320  293 LEU B N   
5195  C  CA  . LEU B 292 ? 0.1839 0.1801 0.7033 0.0020  0.0525  0.0297  293 LEU B CA  
5196  C  C   . LEU B 292 ? 0.2890 0.2852 0.8067 0.0021  0.0521  0.0281  293 LEU B C   
5197  O  O   . LEU B 292 ? 0.2978 0.2942 0.8175 0.0020  0.0512  0.0283  293 LEU B O   
5198  C  CB  . LEU B 292 ? 0.1831 0.1791 0.7005 0.0015  0.0517  0.0268  293 LEU B CB  
5199  C  CG  . LEU B 292 ? 0.1826 0.1788 0.6998 0.0014  0.0514  0.0250  293 LEU B CG  
5200  C  CD1 . LEU B 292 ? 0.2100 0.2068 0.7321 0.0012  0.0501  0.0258  293 LEU B CD1 
5201  C  CD2 . LEU B 292 ? 0.1826 0.1785 0.7011 0.0016  0.0518  0.0229  293 LEU B CD2 
5202  N  N   . LEU B 293 ? 0.1820 0.1779 0.6981 0.0021  0.0524  0.0262  294 LEU B N   
5203  C  CA  . LEU B 293 ? 0.2888 0.2848 0.8063 0.0020  0.0512  0.0241  294 LEU B CA  
5204  C  C   . LEU B 293 ? 0.2919 0.2887 0.8143 0.0034  0.0494  0.0242  294 LEU B C   
5205  O  O   . LEU B 293 ? 0.1842 0.1813 0.7096 0.0035  0.0470  0.0225  294 LEU B O   
5206  C  CB  . LEU B 293 ? 0.1816 0.1774 0.6988 0.0019  0.0515  0.0221  294 LEU B CB  
5207  C  CG  . LEU B 293 ? 0.2481 0.2436 0.7625 0.0015  0.0528  0.0219  294 LEU B CG  
5208  C  CD1 . LEU B 293 ? 0.2676 0.2628 0.7788 0.0017  0.0544  0.0234  294 LEU B CD1 
5209  C  CD2 . LEU B 293 ? 0.2424 0.2377 0.7584 0.0016  0.0533  0.0210  294 LEU B CD2 
5210  N  N   . ASP B 294 ? 0.2298 0.2279 0.7501 0.0067  0.0501  0.0261  295 ASP B N   
5211  C  CA  . ASP B 294 ? 0.3338 0.3341 0.8534 0.0119  0.0483  0.0265  295 ASP B CA  
5212  C  C   . ASP B 294 ? 0.3556 0.3554 0.8785 0.0117  0.0479  0.0299  295 ASP B C   
5213  O  O   . ASP B 294 ? 0.3491 0.3497 0.8723 0.0150  0.0445  0.0287  295 ASP B O   
5214  C  CB  . ASP B 294 ? 0.4349 0.4382 0.9517 0.0170  0.0510  0.0291  295 ASP B CB  
5215  C  CG  . ASP B 294 ? 0.6645 0.6705 1.1774 0.0223  0.0488  0.0239  295 ASP B CG  
5216  O  OD1 . ASP B 294 ? 0.6965 0.7006 1.2104 0.0202  0.0453  0.0186  295 ASP B OD1 
5217  O  OD2 . ASP B 294 ? 0.6973 0.7074 1.2073 0.0289  0.0509  0.0254  295 ASP B OD2 
5218  N  N   . SER B 295 ? 0.2619 0.2605 0.7884 0.0081  0.0506  0.0336  296 SER B N   
5219  C  CA  . SER B 295 ? 0.3470 0.3454 0.8783 0.0076  0.0502  0.0367  296 SER B CA  
5220  C  C   . SER B 295 ? 0.1884 0.1862 0.7208 0.0053  0.0475  0.0329  296 SER B C   
5221  O  O   . SER B 295 ? 0.1910 0.1891 0.7256 0.0070  0.0452  0.0336  296 SER B O   
5222  C  CB  . SER B 295 ? 0.2895 0.2874 0.8273 0.0042  0.0528  0.0402  296 SER B CB  
5223  O  OG  . SER B 295 ? 0.3728 0.3702 0.9033 0.0028  0.0517  0.0356  296 SER B OG  
5224  N  N   . MET B 296 ? 0.2699 0.2672 0.8004 0.0026  0.0480  0.0294  297 MET B N   
5225  C  CA  . MET B 296 ? 0.2301 0.2273 0.7597 0.0020  0.0468  0.0266  297 MET B CA  
5226  C  C   . MET B 296 ? 0.2671 0.2647 0.8027 0.0026  0.0435  0.0244  297 MET B C   
5227  O  O   . MET B 296 ? 0.1868 0.1846 0.7269 0.0026  0.0416  0.0237  297 MET B O   
5228  C  CB  . MET B 296 ? 0.2485 0.2452 0.7715 0.0015  0.0488  0.0247  297 MET B CB  
5229  C  CG  . MET B 296 ? 0.1831 0.1795 0.7029 0.0014  0.0506  0.0252  297 MET B CG  
5230  S  SD  . MET B 296 ? 0.5385 0.5343 1.0547 0.0014  0.0534  0.0240  297 MET B SD  
5231  C  CE  . MET B 296 ? 0.5593 0.5547 1.0786 0.0014  0.0551  0.0238  297 MET B CE  
5232  N  N   . VAL B 297 ? 0.2766 0.2745 0.8097 0.0047  0.0420  0.0224  298 VAL B N   
5233  C  CA  . VAL B 297 ? 0.2450 0.2437 0.7809 0.0079  0.0368  0.0185  298 VAL B CA  
5234  C  C   . VAL B 297 ? 0.3426 0.3423 0.8777 0.0129  0.0334  0.0199  298 VAL B C   
5235  O  O   . VAL B 297 ? 0.2418 0.2419 0.7817 0.0147  0.0285  0.0172  298 VAL B O   
5236  C  CB  . VAL B 297 ? 0.2405 0.2400 0.7735 0.0108  0.0353  0.0152  298 VAL B CB  
5237  C  CG1 . VAL B 297 ? 0.2009 0.2019 0.7360 0.0166  0.0283  0.0102  298 VAL B CG1 
5238  C  CG2 . VAL B 297 ? 0.1899 0.1884 0.7262 0.0063  0.0375  0.0136  298 VAL B CG2 
5239  N  N   . LEU B 298 ? 0.1987 0.1985 0.7292 0.0152  0.0363  0.0248  299 LEU B N   
5240  C  CA  . LEU B 298 ? 0.2603 0.2608 0.7897 0.0211  0.0342  0.0282  299 LEU B CA  
5241  C  C   . LEU B 298 ? 0.2839 0.2832 0.8183 0.0192  0.0329  0.0299  299 LEU B C   
5242  O  O   . LEU B 298 ? 0.2768 0.2763 0.8116 0.0244  0.0284  0.0302  299 LEU B O   
5243  C  CB  . LEU B 298 ? 0.2524 0.2536 0.7788 0.0236  0.0393  0.0349  299 LEU B CB  
5244  C  CG  . LEU B 298 ? 0.4083 0.4124 0.9290 0.0332  0.0384  0.0358  299 LEU B CG  
5245  C  CD1 . LEU B 298 ? 0.4403 0.4462 0.9604 0.0352  0.0455  0.0436  299 LEU B CD1 
5246  C  CD2 . LEU B 298 ? 0.4742 0.4785 0.9939 0.0406  0.0329  0.0362  299 LEU B CD2 
5247  N  N   . ILE B 299 ? 0.1991 0.1974 0.7369 0.0129  0.0364  0.0306  300 ILE B N   
5248  C  CA  . ILE B 299 ? 0.1994 0.1972 0.7422 0.0116  0.0356  0.0318  300 ILE B CA  
5249  C  C   . ILE B 299 ? 0.3540 0.3522 0.9015 0.0117  0.0314  0.0273  300 ILE B C   
5250  O  O   . ILE B 299 ? 0.2980 0.2960 0.8497 0.0127  0.0293  0.0280  300 ILE B O   
5251  C  CB  . ILE B 299 ? 0.1937 0.1915 0.7390 0.0065  0.0400  0.0323  300 ILE B CB  
5252  C  CG1 . ILE B 299 ? 0.3595 0.3570 0.9096 0.0069  0.0394  0.0343  300 ILE B CG1 
5253  C  CG2 . ILE B 299 ? 0.1892 0.1873 0.7352 0.0031  0.0416  0.0283  300 ILE B CG2 
5254  C  CD1 . ILE B 299 ? 0.2901 0.2866 0.8411 0.0101  0.0390  0.0402  300 ILE B CD1 
5255  N  N   . THR B 300 ? 0.1991 0.1979 0.7479 0.0108  0.0299  0.0229  301 THR B N   
5256  C  CA  . THR B 300 ? 0.2006 0.2000 0.7580 0.0103  0.0258  0.0188  301 THR B CA  
5257  C  C   . THR B 300 ? 0.2088 0.2091 0.7675 0.0168  0.0179  0.0171  301 THR B C   
5258  O  O   . THR B 300 ? 0.2113 0.2124 0.7791 0.0169  0.0133  0.0138  301 THR B O   
5259  C  CB  . THR B 300 ? 0.2784 0.2780 0.8401 0.0076  0.0258  0.0148  301 THR B CB  
5260  O  OG1 . THR B 300 ? 0.2023 0.2027 0.7602 0.0121  0.0212  0.0118  301 THR B OG1 
5261  C  CG2 . THR B 300 ? 0.1922 0.1908 0.7508 0.0029  0.0331  0.0171  301 THR B CG2 
5262  N  N   . ASP B 301 ? 0.2915 0.2919 0.8418 0.0229  0.0165  0.0196  302 ASP B N   
5263  C  CA  . ASP B 301 ? 0.3405 0.3415 0.8895 0.0314  0.0092  0.0191  302 ASP B CA  
5264  C  C   . ASP B 301 ? 0.2975 0.2975 0.8507 0.0313  0.0081  0.0223  302 ASP B C   
5265  O  O   . ASP B 301 ? 0.2339 0.2347 0.7912 0.0360  0.0007  0.0197  302 ASP B O   
5266  C  CB  . ASP B 301 ? 0.3741 0.3752 0.9125 0.0391  0.0102  0.0237  302 ASP B CB  
5267  C  CG  . ASP B 301 ? 0.3727 0.3756 0.9068 0.0425  0.0088  0.0190  302 ASP B CG  
5268  O  OD1 . ASP B 301 ? 0.4477 0.4514 0.9879 0.0402  0.0044  0.0113  302 ASP B OD1 
5269  O  OD2 . ASP B 301 ? 0.2796 0.2833 0.8056 0.0478  0.0124  0.0232  302 ASP B OD2 
5270  N  N   . LYS B 302 ? 0.2215 0.2199 0.7745 0.0264  0.0148  0.0271  303 LYS B N   
5271  C  CA  . LYS B 302 ? 0.2459 0.2430 0.8029 0.0265  0.0144  0.0301  303 LYS B CA  
5272  C  C   . LYS B 302 ? 0.2733 0.2715 0.8403 0.0221  0.0137  0.0257  303 LYS B C   
5273  O  O   . LYS B 302 ? 0.2222 0.2197 0.7936 0.0219  0.0137  0.0271  303 LYS B O   
5274  C  CB  . LYS B 302 ? 0.2211 0.2163 0.7761 0.0235  0.0210  0.0359  303 LYS B CB  
5275  C  CG  . LYS B 302 ? 0.2247 0.2190 0.7731 0.0269  0.0236  0.0417  303 LYS B CG  
5276  C  CD  . LYS B 302 ? 0.4339 0.4274 0.9776 0.0366  0.0186  0.0452  303 LYS B CD  
5277  C  CE  . LYS B 302 ? 0.4902 0.4832 1.0279 0.0411  0.0230  0.0526  303 LYS B CE  
5278  N  NZ  . LYS B 302 ? 0.5133 0.5067 1.0442 0.0530  0.0184  0.0559  303 LYS B NZ  
5279  N  N   . PHE B 303 ? 0.2161 0.2158 0.7876 0.0187  0.0136  0.0208  304 PHE B N   
5280  C  CA  . PHE B 303 ? 0.2143 0.2148 0.7975 0.0149  0.0139  0.0177  304 PHE B CA  
5281  C  C   . PHE B 303 ? 0.2218 0.2238 0.8136 0.0192  0.0047  0.0141  304 PHE B C   
5282  O  O   . PHE B 303 ? 0.2227 0.2254 0.8258 0.0175  0.0041  0.0127  304 PHE B O   
5283  C  CB  . PHE B 303 ? 0.2088 0.2095 0.7959 0.0099  0.0177  0.0152  304 PHE B CB  
5284  C  CG  . PHE B 303 ? 0.3389 0.3385 0.9191 0.0061  0.0262  0.0182  304 PHE B CG  
5285  C  CD1 . PHE B 303 ? 0.2013 0.2003 0.7744 0.0066  0.0295  0.0217  304 PHE B CD1 
5286  C  CD2 . PHE B 303 ? 0.3320 0.3311 0.9139 0.0024  0.0303  0.0174  304 PHE B CD2 
5287  C  CE1 . PHE B 303 ? 0.3058 0.3042 0.8735 0.0039  0.0357  0.0232  304 PHE B CE1 
5288  C  CE2 . PHE B 303 ? 0.1953 0.1935 0.7675 0.0010  0.0370  0.0196  304 PHE B CE2 
5289  C  CZ  . PHE B 303 ? 0.3406 0.3387 0.9072 0.0014  0.0393  0.0221  304 PHE B CZ  
5290  N  N   . TRP B 304 ? 0.2520 0.2547 0.8384 0.0258  -0.0025 0.0126  305 TRP B N   
5291  C  CA  . TRP B 304 ? 0.2971 0.3017 0.8911 0.0313  -0.0133 0.0075  305 TRP B CA  
5292  C  C   . TRP B 304 ? 0.3557 0.3598 0.9436 0.0396  -0.0186 0.0110  305 TRP B C   
5293  O  O   . TRP B 304 ? 0.3413 0.3430 0.9181 0.0419  -0.0141 0.0177  305 TRP B O   
5294  C  CB  . TRP B 304 ? 0.2979 0.3039 0.8909 0.0351  -0.0199 0.0015  305 TRP B CB  
5295  C  CG  . TRP B 304 ? 0.3365 0.3419 0.9308 0.0283  -0.0137 0.0001  305 TRP B CG  
5296  C  CD1 . TRP B 304 ? 0.3276 0.3323 0.9102 0.0291  -0.0097 0.0016  305 TRP B CD1 
5297  C  CD2 . TRP B 304 ? 0.3514 0.3566 0.9602 0.0203  -0.0103 -0.0023 305 TRP B CD2 
5298  N  NE1 . TRP B 304 ? 0.3161 0.3202 0.9042 0.0221  -0.0049 -0.0001 305 TRP B NE1 
5299  C  CE2 . TRP B 304 ? 0.3789 0.3830 0.9829 0.0168  -0.0049 -0.0020 305 TRP B CE2 
5300  C  CE3 . TRP B 304 ? 0.4164 0.4218 1.0423 0.0162  -0.0108 -0.0038 305 TRP B CE3 
5301  C  CZ2 . TRP B 304 ? 0.4103 0.4132 1.0255 0.0097  -0.0001 -0.0026 305 TRP B CZ2 
5302  C  CZ3 . TRP B 304 ? 0.4636 0.4674 1.1012 0.0091  -0.0052 -0.0040 305 TRP B CZ3 
5303  C  CH2 . TRP B 304 ? 0.4468 0.4492 1.0787 0.0061  0.0001  -0.0031 305 TRP B CH2 
5304  N  N   . GLY B 305 ? 0.3699 0.3759 0.9664 0.0442  -0.0283 0.0068  306 GLY B N   
5305  C  CA  . GLY B 305 ? 0.4244 0.4298 1.0149 0.0537  -0.0350 0.0099  306 GLY B CA  
5306  C  C   . GLY B 305 ? 0.4538 0.4582 1.0510 0.0516  -0.0330 0.0134  306 GLY B C   
5307  O  O   . GLY B 305 ? 0.4496 0.4541 1.0557 0.0432  -0.0260 0.0132  306 GLY B O   
5308  N  N   . THR B 306 ? 0.5200 0.5233 1.1122 0.0605  -0.0393 0.0169  307 THR B N   
5309  C  CA  . THR B 306 ? 0.5874 0.5894 1.1856 0.0601  -0.0386 0.0202  307 THR B CA  
5310  C  C   . THR B 306 ? 0.6043 0.6027 1.1992 0.0534  -0.0267 0.0264  307 THR B C   
5311  O  O   . THR B 306 ? 0.6062 0.6047 1.2101 0.0483  -0.0227 0.0259  307 THR B O   
5312  C  CB  . THR B 306 ? 0.5395 0.5399 1.1303 0.0721  -0.0475 0.0244  307 THR B CB  
5313  O  OG1 . THR B 306 ? 0.5835 0.5796 1.1582 0.0772  -0.0435 0.0329  307 THR B OG1 
5314  C  CG2 . THR B 306 ? 0.4924 0.4971 1.0864 0.0802  -0.0615 0.0168  307 THR B CG2 
5315  N  N   . SER B 307 ? 0.6008 0.5962 1.1835 0.0539  -0.0214 0.0319  308 SER B N   
5316  C  CA  . SER B 307 ? 0.5574 0.5496 1.1379 0.0478  -0.0114 0.0369  308 SER B CA  
5317  C  C   . SER B 307 ? 0.5157 0.5098 1.0976 0.0391  -0.0042 0.0332  308 SER B C   
5318  O  O   . SER B 307 ? 0.4002 0.3927 0.9801 0.0342  0.0033  0.0358  308 SER B O   
5319  C  CB  . SER B 307 ? 0.6304 0.6182 1.2000 0.0527  -0.0093 0.0459  308 SER B CB  
5320  O  OG  . SER B 307 ? 0.7174 0.7026 1.2845 0.0617  -0.0156 0.0509  308 SER B OG  
5321  N  N   . GLY B 308 ? 0.4097 0.4072 0.9957 0.0378  -0.0072 0.0270  309 GLY B N   
5322  C  CA  . GLY B 308 ? 0.2382 0.2371 0.8255 0.0305  -0.0009 0.0241  309 GLY B CA  
5323  C  C   . GLY B 308 ? 0.2315 0.2304 0.8256 0.0240  0.0062  0.0235  309 GLY B C   
5324  O  O   . GLY B 308 ? 0.2348 0.2338 0.8360 0.0248  0.0053  0.0234  309 GLY B O   
5325  N  N   . VAL B 309 ? 0.2360 0.2350 0.8275 0.0187  0.0131  0.0231  310 VAL B N   
5326  C  CA  . VAL B 309 ? 0.2815 0.2803 0.8759 0.0145  0.0206  0.0231  310 VAL B CA  
5327  C  C   . VAL B 309 ? 0.2739 0.2739 0.8808 0.0135  0.0210  0.0205  310 VAL B C   
5328  O  O   . VAL B 309 ? 0.3926 0.3922 1.0032 0.0144  0.0232  0.0210  310 VAL B O   
5329  C  CB  . VAL B 309 ? 0.3072 0.3058 0.8960 0.0104  0.0269  0.0229  310 VAL B CB  
5330  C  CG1 . VAL B 309 ? 0.2847 0.2829 0.8758 0.0081  0.0341  0.0225  310 VAL B CG1 
5331  C  CG2 . VAL B 309 ? 0.3168 0.3143 0.8954 0.0110  0.0279  0.0258  310 VAL B CG2 
5332  N  N   . GLU B 310 ? 0.3115 0.3128 0.9262 0.0118  0.0191  0.0177  311 GLU B N   
5333  C  CA  . GLU B 310 ? 0.4280 0.4301 1.0574 0.0101  0.0208  0.0161  311 GLU B CA  
5334  C  C   . GLU B 310 ? 0.3954 0.3988 1.0332 0.0137  0.0153  0.0153  311 GLU B C   
5335  O  O   . GLU B 310 ? 0.5340 0.5377 1.1795 0.0136  0.0197  0.0159  311 GLU B O   
5336  C  CB  . GLU B 310 ? 0.4909 0.4934 1.1303 0.0077  0.0181  0.0131  311 GLU B CB  
5337  C  CG  . GLU B 310 ? 0.5946 0.5950 1.2375 0.0033  0.0276  0.0150  311 GLU B CG  
5338  C  CD  . GLU B 310 ? 0.6351 0.6346 1.2962 0.0009  0.0258  0.0128  311 GLU B CD  
5339  O  OE1 . GLU B 310 ? 0.6621 0.6633 1.3329 0.0024  0.0157  0.0084  311 GLU B OE1 
5340  O  OE2 . GLU B 310 ? 0.6678 0.6660 1.3284 0.0003  0.0338  0.0154  311 GLU B OE2 
5341  N  N   . SER B 311 ? 0.3637 0.3680 0.9997 0.0180  0.0057  0.0141  312 SER B N   
5342  C  CA  . SER B 311 ? 0.3930 0.3983 1.0351 0.0227  -0.0008 0.0138  312 SER B CA  
5343  C  C   . SER B 311 ? 0.3993 0.4028 1.0375 0.0236  0.0045  0.0172  312 SER B C   
5344  O  O   . SER B 311 ? 0.4097 0.4141 1.0580 0.0238  0.0064  0.0166  312 SER B O   
5345  C  CB  . SER B 311 ? 0.4192 0.4246 1.0540 0.0292  -0.0111 0.0136  312 SER B CB  
5346  O  OG  . SER B 311 ? 0.5650 0.5701 1.2013 0.0348  -0.0164 0.0152  312 SER B OG  
5347  N  N   . VAL B 312 ? 0.3740 0.3748 0.9986 0.0243  0.0070  0.0206  313 VAL B N   
5348  C  CA  . VAL B 312 ? 0.3254 0.3236 0.9467 0.0255  0.0105  0.0232  313 VAL B CA  
5349  C  C   . VAL B 312 ? 0.3526 0.3511 0.9778 0.0228  0.0190  0.0217  313 VAL B C   
5350  O  O   . VAL B 312 ? 0.3685 0.3671 1.0010 0.0249  0.0197  0.0209  313 VAL B O   
5351  C  CB  . VAL B 312 ? 0.2414 0.2364 0.8500 0.0257  0.0120  0.0271  313 VAL B CB  
5352  C  CG1 . VAL B 312 ? 0.3712 0.3631 0.9786 0.0262  0.0155  0.0287  313 VAL B CG1 
5353  C  CG2 . VAL B 312 ? 0.2477 0.2415 0.8511 0.0307  0.0047  0.0302  313 VAL B CG2 
5354  N  N   . ILE B 313 ? 0.3103 0.3085 0.9296 0.0192  0.0254  0.0214  314 ILE B N   
5355  C  CA  . ILE B 313 ? 0.3159 0.3137 0.9354 0.0184  0.0339  0.0204  314 ILE B CA  
5356  C  C   . ILE B 313 ? 0.3464 0.3464 0.9792 0.0189  0.0362  0.0193  314 ILE B C   
5357  O  O   . ILE B 313 ? 0.3370 0.3369 0.9725 0.0213  0.0416  0.0188  314 ILE B O   
5358  C  CB  . ILE B 313 ? 0.2959 0.2934 0.9074 0.0152  0.0395  0.0207  314 ILE B CB  
5359  C  CG1 . ILE B 313 ? 0.2700 0.2657 0.8702 0.0148  0.0380  0.0218  314 ILE B CG1 
5360  C  CG2 . ILE B 313 ? 0.2300 0.2267 0.8404 0.0165  0.0483  0.0200  314 ILE B CG2 
5361  C  CD1 . ILE B 313 ? 0.2194 0.2145 0.8113 0.0127  0.0435  0.0215  314 ILE B CD1 
5362  N  N   . GLY B 314 ? 0.4048 0.4069 1.0472 0.0172  0.0317  0.0186  315 GLY B N   
5363  C  CA  . GLY B 314 ? 0.2409 0.2451 0.8996 0.0172  0.0330  0.0178  315 GLY B CA  
5364  C  C   . GLY B 314 ? 0.3243 0.3302 0.9923 0.0210  0.0274  0.0168  315 GLY B C   
5365  O  O   . GLY B 314 ? 0.3023 0.3102 0.9847 0.0217  0.0297  0.0163  315 GLY B O   
5366  N  N   . SER B 315 ? 0.4007 0.4054 1.0613 0.0239  0.0205  0.0171  316 SER B N   
5367  C  CA  . SER B 315 ? 0.3653 0.3711 1.0344 0.0282  0.0139  0.0164  316 SER B CA  
5368  C  C   . SER B 315 ? 0.3204 0.3231 0.9819 0.0321  0.0136  0.0181  316 SER B C   
5369  O  O   . SER B 315 ? 0.4120 0.4143 1.0766 0.0363  0.0063  0.0187  316 SER B O   
5370  C  CB  . SER B 315 ? 0.3333 0.3405 1.0052 0.0301  0.0023  0.0152  316 SER B CB  
5371  O  OG  . SER B 315 ? 0.3141 0.3238 0.9958 0.0268  0.0010  0.0125  316 SER B OG  
5372  N  N   . VAL B 316 ? 0.2596 0.2595 0.9117 0.0313  0.0210  0.0187  317 VAL B N   
5373  C  CA  . VAL B 316 ? 0.3542 0.3503 1.0025 0.0349  0.0216  0.0190  317 VAL B CA  
5374  C  C   . VAL B 316 ? 0.2748 0.2720 0.9348 0.0394  0.0194  0.0179  317 VAL B C   
5375  O  O   . VAL B 316 ? 0.3481 0.3421 1.0076 0.0431  0.0142  0.0192  317 VAL B O   
5376  C  CB  . VAL B 316 ? 0.3167 0.3107 0.9573 0.0345  0.0304  0.0173  317 VAL B CB  
5377  C  CG1 . VAL B 316 ? 0.3476 0.3366 0.9846 0.0383  0.0296  0.0165  317 VAL B CG1 
5378  C  CG2 . VAL B 316 ? 0.2561 0.2494 0.8860 0.0304  0.0326  0.0182  317 VAL B CG2 
5379  N  N   . HIS B 317 ? 0.2757 0.2771 0.9470 0.0392  0.0238  0.0161  318 HIS B N   
5380  C  CA  . HIS B 317 ? 0.2843 0.2877 0.9683 0.0436  0.0233  0.0148  318 HIS B CA  
5381  C  C   . HIS B 317 ? 0.3689 0.3734 1.0606 0.0460  0.0122  0.0155  318 HIS B C   
5382  O  O   . HIS B 317 ? 0.5266 0.5311 1.2256 0.0505  0.0095  0.0150  318 HIS B O   
5383  C  CB  . HIS B 317 ? 0.2849 0.2933 0.9815 0.0428  0.0310  0.0139  318 HIS B CB  
5384  C  CG  . HIS B 317 ? 0.4418 0.4537 1.1482 0.0383  0.0283  0.0142  318 HIS B CG  
5385  N  ND1 . HIS B 317 ? 0.4612 0.4753 1.1778 0.0385  0.0176  0.0133  318 HIS B ND1 
5386  C  CD2 . HIS B 317 ? 0.3929 0.4059 1.1015 0.0342  0.0346  0.0151  318 HIS B CD2 
5387  C  CE1 . HIS B 317 ? 0.4355 0.4518 1.1605 0.0344  0.0168  0.0126  318 HIS B CE1 
5388  N  NE2 . HIS B 317 ? 0.4518 0.4671 1.1726 0.0313  0.0273  0.0142  318 HIS B NE2 
5389  N  N   . THR B 318 ? 0.3479 0.3532 1.0373 0.0439  0.0055  0.0163  319 THR B N   
5390  C  CA  . THR B 318 ? 0.3764 0.3825 1.0702 0.0478  -0.0061 0.0168  319 THR B CA  
5391  C  C   . THR B 318 ? 0.3535 0.3538 1.0368 0.0524  -0.0099 0.0203  319 THR B C   
5392  O  O   . THR B 318 ? 0.3896 0.3894 1.0786 0.0577  -0.0162 0.0211  319 THR B O   
5393  C  CB  . THR B 318 ? 0.4169 0.4246 1.1079 0.0462  -0.0126 0.0162  319 THR B CB  
5394  O  OG1 . THR B 318 ? 0.4602 0.4640 1.1342 0.0441  -0.0098 0.0189  319 THR B OG1 
5395  C  CG2 . THR B 318 ? 0.4201 0.4324 1.1240 0.0413  -0.0093 0.0129  319 THR B CG2 
5396  N  N   . TRP B 319 ? 0.3846 0.3802 1.0539 0.0503  -0.0060 0.0228  320 TRP B N   
5397  C  CA  . TRP B 319 ? 0.3788 0.3677 1.0398 0.0538  -0.0083 0.0270  320 TRP B CA  
5398  C  C   . TRP B 319 ? 0.3412 0.3275 1.0078 0.0562  -0.0050 0.0255  320 TRP B C   
5399  O  O   . TRP B 319 ? 0.3828 0.3648 1.0503 0.0609  -0.0098 0.0283  320 TRP B O   
5400  C  CB  . TRP B 319 ? 0.3973 0.3822 1.0450 0.0503  -0.0044 0.0298  320 TRP B CB  
5401  C  CG  . TRP B 319 ? 0.4743 0.4598 1.1147 0.0506  -0.0092 0.0329  320 TRP B CG  
5402  C  CD1 . TRP B 319 ? 0.5013 0.4832 1.1359 0.0561  -0.0161 0.0385  320 TRP B CD1 
5403  C  CD2 . TRP B 319 ? 0.5243 0.5136 1.1614 0.0465  -0.0075 0.0309  320 TRP B CD2 
5404  N  NE1 . TRP B 319 ? 0.5087 0.4922 1.1360 0.0564  -0.0188 0.0396  320 TRP B NE1 
5405  C  CE2 . TRP B 319 ? 0.5761 0.5643 1.2054 0.0502  -0.0138 0.0345  320 TRP B CE2 
5406  C  CE3 . TRP B 319 ? 0.5274 0.5203 1.1669 0.0409  -0.0010 0.0268  320 TRP B CE3 
5407  C  CZ2 . TRP B 319 ? 0.5686 0.5595 1.1932 0.0482  -0.0144 0.0331  320 TRP B CZ2 
5408  C  CZ3 . TRP B 319 ? 0.5358 0.5310 1.1713 0.0382  -0.0015 0.0260  320 TRP B CZ3 
5409  C  CH2 . TRP B 319 ? 0.5551 0.5495 1.1836 0.0417  -0.0083 0.0286  320 TRP B CH2 
5410  N  N   . LEU B 320 ? 0.3185 0.3069 0.9881 0.0539  0.0032  0.0213  321 LEU B N   
5411  C  CA  . LEU B 320 ? 0.3826 0.3688 1.0574 0.0578  0.0063  0.0189  321 LEU B CA  
5412  C  C   . LEU B 320 ? 0.4675 0.4566 1.1558 0.0626  0.0006  0.0187  321 LEU B C   
5413  O  O   . LEU B 320 ? 0.4367 0.4213 1.1270 0.0674  -0.0027 0.0196  321 LEU B O   
5414  C  CB  . LEU B 320 ? 0.3086 0.2974 0.9837 0.0566  0.0163  0.0146  321 LEU B CB  
5415  C  CG  . LEU B 320 ? 0.3927 0.3787 1.0545 0.0528  0.0214  0.0141  321 LEU B CG  
5416  C  CD1 . LEU B 320 ? 0.3022 0.2896 0.9625 0.0543  0.0310  0.0101  321 LEU B CD1 
5417  C  CD2 . LEU B 320 ? 0.4226 0.4009 1.0762 0.0535  0.0182  0.0155  321 LEU B CD2 
5418  N  N   . ALA B 321 ? 0.3998 0.3961 1.0982 0.0614  -0.0009 0.0174  322 ALA B N   
5419  C  CA  . ALA B 321 ? 0.4484 0.4488 1.1617 0.0656  -0.0070 0.0166  322 ALA B CA  
5420  C  C   . ALA B 321 ? 0.4831 0.4797 1.1931 0.0705  -0.0182 0.0202  322 ALA B C   
5421  O  O   . ALA B 321 ? 0.5080 0.5037 1.2254 0.0760  -0.0225 0.0205  322 ALA B O   
5422  C  CB  . ALA B 321 ? 0.3205 0.3287 1.0463 0.0625  -0.0077 0.0144  322 ALA B CB  
5423  N  N   . GLU B 322 ? 0.4947 0.4890 1.1931 0.0693  -0.0225 0.0235  323 GLU B N   
5424  C  CA  . GLU B 322 ? 0.5429 0.5328 1.2350 0.0752  -0.0322 0.0284  323 GLU B CA  
5425  C  C   . GLU B 322 ? 0.5748 0.5560 1.2616 0.0783  -0.0307 0.0324  323 GLU B C   
5426  O  O   . GLU B 322 ? 0.5628 0.5405 1.2508 0.0848  -0.0377 0.0360  323 GLU B O   
5427  C  CB  . GLU B 322 ? 0.6261 0.6147 1.3049 0.0741  -0.0351 0.0316  323 GLU B CB  
5428  C  CG  . GLU B 322 ? 0.7666 0.7615 1.4500 0.0761  -0.0437 0.0290  323 GLU B CG  
5429  C  CD  . GLU B 322 ? 0.8523 0.8473 1.5242 0.0735  -0.0438 0.0297  323 GLU B CD  
5430  O  OE1 . GLU B 322 ? 0.8707 0.8658 1.5392 0.0664  -0.0348 0.0286  323 GLU B OE1 
5431  O  OE2 . GLU B 322 ? 0.8976 0.8927 1.5631 0.0796  -0.0531 0.0314  323 GLU B OE2 
5432  N  N   . ALA B 323 ? 0.5956 0.5731 1.2770 0.0739  -0.0222 0.0315  324 ALA B N   
5433  C  CA  . ALA B 323 ? 0.6306 0.5996 1.3094 0.0761  -0.0209 0.0340  324 ALA B CA  
5434  C  C   . ALA B 323 ? 0.5651 0.5342 1.2557 0.0810  -0.0217 0.0308  324 ALA B C   
5435  O  O   . ALA B 323 ? 0.3768 0.3399 1.0689 0.0862  -0.0268 0.0345  324 ALA B O   
5436  C  CB  . ALA B 323 ? 0.3463 0.3122 1.0184 0.0709  -0.0128 0.0317  324 ALA B CB  
5437  N  N   . ILE B 324 ? 0.5052 0.4810 1.2044 0.0797  -0.0162 0.0245  325 ILE B N   
5438  C  CA  . ILE B 324 ? 0.4955 0.4724 1.2068 0.0848  -0.0159 0.0212  325 ILE B CA  
5439  C  C   . ILE B 324 ? 0.5407 0.5198 1.2610 0.0903  -0.0257 0.0238  325 ILE B C   
5440  O  O   . ILE B 324 ? 0.5481 0.5226 1.2727 0.0960  -0.0293 0.0251  325 ILE B O   
5441  C  CB  . ILE B 324 ? 0.4138 0.3987 1.1336 0.0833  -0.0076 0.0154  325 ILE B CB  
5442  C  CG1 . ILE B 324 ? 0.3989 0.3813 1.1081 0.0796  0.0016  0.0127  325 ILE B CG1 
5443  C  CG2 . ILE B 324 ? 0.3787 0.3651 1.1114 0.0895  -0.0067 0.0123  325 ILE B CG2 
5444  C  CD1 . ILE B 324 ? 0.3915 0.3807 1.1066 0.0795  0.0110  0.0084  325 ILE B CD1 
5445  N  N   . ASN B 325 ? 0.4718 0.4576 1.1949 0.0890  -0.0305 0.0242  326 ASN B N   
5446  C  CA  . ASN B 325 ? 0.4828 0.4713 1.2134 0.0950  -0.0414 0.0259  326 ASN B CA  
5447  C  C   . ASN B 325 ? 0.5704 0.5496 1.2903 0.1008  -0.0486 0.0330  326 ASN B C   
5448  O  O   . ASN B 325 ? 0.5509 0.5288 1.2768 0.1079  -0.0557 0.0349  326 ASN B O   
5449  C  CB  . ASN B 325 ? 0.4872 0.4833 1.2205 0.0927  -0.0464 0.0243  326 ASN B CB  
5450  C  CG  . ASN B 325 ? 0.4992 0.4979 1.2380 0.1000  -0.0597 0.0254  326 ASN B CG  
5451  O  OD1 . ASN B 325 ? 0.5213 0.5168 1.2480 0.1037  -0.0674 0.0296  326 ASN B OD1 
5452  N  ND2 . ASN B 325 ? 0.4437 0.4482 1.2006 0.1030  -0.0624 0.0217  326 ASN B ND2 
5453  N  N   . ALA B 326 ? 0.5931 0.5657 1.2978 0.0980  -0.0463 0.0377  327 ALA B N   
5454  C  CA  . ALA B 326 ? 0.6179 0.5807 1.3123 0.1030  -0.0511 0.0462  327 ALA B CA  
5455  C  C   . ALA B 326 ? 0.5797 0.5347 1.2788 0.1059  -0.0493 0.0473  327 ALA B C   
5456  O  O   . ALA B 326 ? 0.4328 0.3817 1.1312 0.1129  -0.0557 0.0532  327 ALA B O   
5457  C  CB  . ALA B 326 ? 0.3988 0.3568 1.0785 0.0985  -0.0472 0.0510  327 ALA B CB  
5458  N  N   . LEU B 327 ? 0.5783 0.5331 1.2815 0.1013  -0.0409 0.0415  328 LEU B N   
5459  C  CA  . LEU B 327 ? 0.4739 0.4212 1.1824 0.1044  -0.0395 0.0407  328 LEU B CA  
5460  C  C   . LEU B 327 ? 0.5681 0.5190 1.2897 0.1113  -0.0444 0.0385  328 LEU B C   
5461  O  O   . LEU B 327 ? 0.5743 0.5178 1.2984 0.1172  -0.0487 0.0422  328 LEU B O   
5462  C  CB  . LEU B 327 ? 0.4743 0.4213 1.1834 0.0998  -0.0302 0.0335  328 LEU B CB  
5463  C  CG  . LEU B 327 ? 0.5067 0.4458 1.2214 0.1039  -0.0293 0.0308  328 LEU B CG  
5464  C  CD1 . LEU B 327 ? 0.5397 0.4668 1.2509 0.1061  -0.0343 0.0389  328 LEU B CD1 
5465  C  CD2 . LEU B 327 ? 0.4953 0.4331 1.2074 0.1008  -0.0212 0.0233  328 LEU B CD2 
5466  N  N   . GLN B 328 ? 0.5779 0.5402 1.3091 0.1107  -0.0436 0.0328  329 GLN B N   
5467  C  CA  . GLN B 328 ? 0.5764 0.5437 1.3225 0.1169  -0.0483 0.0304  329 GLN B CA  
5468  C  C   . GLN B 328 ? 0.5720 0.5370 1.3168 0.1239  -0.0601 0.0369  329 GLN B C   
5469  O  O   . GLN B 328 ? 0.5383 0.4998 1.2897 0.1309  -0.0648 0.0385  329 GLN B O   
5470  C  CB  . GLN B 328 ? 0.6387 0.6190 1.3972 0.1141  -0.0454 0.0242  329 GLN B CB  
5471  C  CG  . GLN B 328 ? 0.7062 0.6893 1.4653 0.1089  -0.0332 0.0186  329 GLN B CG  
5472  C  CD  . GLN B 328 ? 0.7614 0.7565 1.5370 0.1080  -0.0294 0.0137  329 GLN B CD  
5473  O  OE1 . GLN B 328 ? 0.7984 0.7966 1.5865 0.1125  -0.0264 0.0105  329 GLN B OE1 
5474  N  NE2 . GLN B 328 ? 0.7704 0.7723 1.5471 0.1025  -0.0293 0.0133  329 GLN B NE2 
5475  N  N   . ASP B 329 ? 0.5572 0.5238 1.2923 0.1231  -0.0651 0.0407  330 ASP B N   
5476  C  CA  . ASP B 329 ? 0.6222 0.5873 1.3531 0.1313  -0.0769 0.0468  330 ASP B CA  
5477  C  C   . ASP B 329 ? 0.6160 0.5682 1.3392 0.1378  -0.0797 0.0555  330 ASP B C   
5478  O  O   . ASP B 329 ? 0.5636 0.5144 1.2907 0.1466  -0.0880 0.0586  330 ASP B O   
5479  C  CB  . ASP B 329 ? 0.6993 0.6667 1.4174 0.1299  -0.0804 0.0494  330 ASP B CB  
5480  C  CG  . ASP B 329 ? 0.8113 0.7915 1.5399 0.1283  -0.0847 0.0421  330 ASP B CG  
5481  O  OD1 . ASP B 329 ? 0.8194 0.8069 1.5642 0.1240  -0.0798 0.0349  330 ASP B OD1 
5482  O  OD2 . ASP B 329 ? 0.8117 0.7943 1.5326 0.1317  -0.0929 0.0437  330 ASP B OD2 
5483  N  N   . ASN B 330 ? 0.6529 0.5956 1.3662 0.1334  -0.0729 0.0597  331 ASN B N   
5484  C  CA  . ASN B 330 ? 0.7911 0.7204 1.4985 0.1382  -0.0746 0.0689  331 ASN B CA  
5485  C  C   . ASN B 330 ? 0.8715 0.7945 1.5880 0.1361  -0.0687 0.0652  331 ASN B C   
5486  O  O   . ASN B 330 ? 0.9181 0.8299 1.6298 0.1345  -0.0656 0.0705  331 ASN B O   
5487  C  CB  . ASN B 330 ? 0.8740 0.7959 1.5652 0.1357  -0.0722 0.0779  331 ASN B CB  
5488  C  CG  . ASN B 330 ? 0.9562 0.8745 1.6356 0.1453  -0.0808 0.0887  331 ASN B CG  
5489  O  OD1 . ASN B 330 ? 1.0088 0.9261 1.6913 0.1546  -0.0888 0.0913  331 ASN B OD1 
5490  N  ND2 . ASN B 330 ? 0.9562 0.8722 1.6210 0.1441  -0.0793 0.0954  331 ASN B ND2 
5491  N  N   . ARG B 331 ? 0.8514 0.7815 1.5817 0.1366  -0.0672 0.0561  332 ARG B N   
5492  C  CA  . ARG B 331 ? 0.8346 0.7591 1.5732 0.1367  -0.0624 0.0514  332 ARG B CA  
5493  C  C   . ARG B 331 ? 0.7444 0.6571 1.4849 0.1441  -0.0679 0.0584  332 ARG B C   
5494  O  O   . ARG B 331 ? 0.6943 0.5967 1.4358 0.1430  -0.0646 0.0587  332 ARG B O   
5495  C  CB  . ARG B 331 ? 0.8437 0.7789 1.5966 0.1377  -0.0596 0.0414  332 ARG B CB  
5496  C  CG  . ARG B 331 ? 0.8570 0.7867 1.6173 0.1396  -0.0547 0.0356  332 ARG B CG  
5497  C  CD  . ARG B 331 ? 0.8671 0.8082 1.6405 0.1412  -0.0503 0.0266  332 ARG B CD  
5498  N  NE  . ARG B 331 ? 0.8770 0.8254 1.6628 0.1475  -0.0574 0.0274  332 ARG B NE  
5499  C  CZ  . ARG B 331 ? 0.8392 0.7837 1.6344 0.1554  -0.0618 0.0279  332 ARG B CZ  
5500  N  NH1 . ARG B 331 ? 0.8682 0.8011 1.6621 0.1578  -0.0596 0.0274  332 ARG B NH1 
5501  N  NH2 . ARG B 331 ? 0.8578 0.8102 1.6649 0.1609  -0.0687 0.0284  332 ARG B NH2 
5502  N  N   . ASP B 332 ? 0.8189 0.7331 1.5604 0.1520  -0.0767 0.0638  333 ASP B N   
5503  C  CA  . ASP B 332 ? 0.8760 0.7796 1.6195 0.1605  -0.0826 0.0711  333 ASP B CA  
5504  C  C   . ASP B 332 ? 0.8589 0.7483 1.5903 0.1600  -0.0821 0.0829  333 ASP B C   
5505  O  O   . ASP B 332 ? 0.8092 0.6869 1.5447 0.1604  -0.0803 0.0854  333 ASP B O   
5506  C  CB  . ASP B 332 ? 0.8877 0.7974 1.6335 0.1700  -0.0930 0.0742  333 ASP B CB  
5507  N  N   . THR B 333 ? 0.8625 0.7528 1.5799 0.1593  -0.0836 0.0902  334 THR B N   
5508  C  CA  . THR B 333 ? 0.8700 0.7480 1.5758 0.1589  -0.0820 0.1029  334 THR B CA  
5509  C  C   . THR B 333 ? 0.7279 0.5995 1.4374 0.1491  -0.0731 0.0999  334 THR B C   
5510  O  O   . THR B 333 ? 0.6939 0.5528 1.4061 0.1493  -0.0719 0.1066  334 THR B O   
5511  C  CB  . THR B 333 ? 0.9297 0.8119 1.6194 0.1593  -0.0835 0.1094  334 THR B CB  
5512  O  OG1 . THR B 333 ? 0.9657 0.8533 1.6510 0.1699  -0.0934 0.1118  334 THR B OG1 
5513  C  CG2 . THR B 333 ? 0.9634 0.8332 1.6418 0.1590  -0.0802 0.1235  334 THR B CG2 
5514  N  N   . LEU B 334 ? 0.7153 0.5959 1.4255 0.1408  -0.0674 0.0898  335 LEU B N   
5515  C  CA  . LEU B 334 ? 0.6804 0.5571 1.3939 0.1322  -0.0600 0.0846  335 LEU B CA  
5516  C  C   . LEU B 334 ? 0.6206 0.4892 1.3465 0.1343  -0.0600 0.0800  335 LEU B C   
5517  O  O   . LEU B 334 ? 0.6411 0.4992 1.3699 0.1313  -0.0578 0.0827  335 LEU B O   
5518  C  CB  . LEU B 334 ? 0.6567 0.5454 1.3695 0.1253  -0.0547 0.0731  335 LEU B CB  
5519  C  CG  . LEU B 334 ? 0.6712 0.5568 1.3845 0.1172  -0.0477 0.0674  335 LEU B CG  
5520  C  CD1 . LEU B 334 ? 0.6777 0.5609 1.3812 0.1116  -0.0452 0.0756  335 LEU B CD1 
5521  C  CD2 . LEU B 334 ? 0.6427 0.5387 1.3580 0.1137  -0.0428 0.0545  335 LEU B CD2 
5522  N  N   . THR B 335 ? 0.6005 0.4743 1.3350 0.1399  -0.0627 0.0729  336 THR B N   
5523  C  CA  . THR B 335 ? 0.5850 0.4515 1.3312 0.1436  -0.0632 0.0679  336 THR B CA  
5524  C  C   . THR B 335 ? 0.6229 0.4744 1.3709 0.1477  -0.0672 0.0793  336 THR B C   
5525  O  O   . THR B 335 ? 0.6723 0.5134 1.4268 0.1456  -0.0654 0.0780  336 THR B O   
5526  C  CB  . THR B 335 ? 0.6075 0.4825 1.3630 0.1505  -0.0661 0.0611  336 THR B CB  
5527  O  OG1 . THR B 335 ? 0.5966 0.4844 1.3531 0.1465  -0.0607 0.0503  336 THR B OG1 
5528  C  CG2 . THR B 335 ? 0.6487 0.5149 1.4159 0.1560  -0.0673 0.0574  336 THR B CG2 
5529  N  N   . ALA B 336 ? 0.6233 0.4737 1.3655 0.1541  -0.0729 0.0906  337 ALA B N   
5530  C  CA  . ALA B 336 ? 0.6757 0.5119 1.4181 0.1593  -0.0765 0.1037  337 ALA B CA  
5531  C  C   . ALA B 336 ? 0.6677 0.4937 1.4080 0.1520  -0.0716 0.1108  337 ALA B C   
5532  O  O   . ALA B 336 ? 0.6935 0.5072 1.4432 0.1518  -0.0713 0.1135  337 ALA B O   
5533  C  CB  . ALA B 336 ? 0.6337 0.4714 1.3654 0.1680  -0.0831 0.1152  337 ALA B CB  
5534  N  N   . LYS B 337 ? 0.6611 0.4925 1.3907 0.1459  -0.0677 0.1135  338 LYS B N   
5535  C  CA  . LYS B 337 ? 0.6772 0.5004 1.4055 0.1392  -0.0629 0.1217  338 LYS B CA  
5536  C  C   . LYS B 337 ? 0.6231 0.4438 1.3632 0.1310  -0.0587 0.1106  338 LYS B C   
5537  O  O   . LYS B 337 ? 0.6485 0.4590 1.3959 0.1271  -0.0568 0.1160  338 LYS B O   
5538  C  CB  . LYS B 337 ? 0.7331 0.5636 1.4469 0.1356  -0.0599 0.1273  338 LYS B CB  
5539  C  CG  . LYS B 337 ? 0.8123 0.6390 1.5130 0.1439  -0.0632 0.1440  338 LYS B CG  
5540  C  CD  . LYS B 337 ? 0.8603 0.6894 1.5585 0.1553  -0.0715 0.1439  338 LYS B CD  
5541  C  CE  . LYS B 337 ? 0.9069 0.7304 1.5904 0.1656  -0.0757 0.1609  338 LYS B CE  
5542  N  NZ  . LYS B 337 ? 0.9383 0.7606 1.6228 0.1777  -0.0846 0.1623  338 LYS B NZ  
5543  N  N   . VAL B 338 ? 0.5878 0.4176 1.3301 0.1292  -0.0576 0.0951  339 VAL B N   
5544  C  CA  . VAL B 338 ? 0.5827 0.4103 1.3337 0.1238  -0.0546 0.0829  339 VAL B CA  
5545  C  C   . VAL B 338 ? 0.7736 0.5896 1.5381 0.1286  -0.0581 0.0803  339 VAL B C   
5546  O  O   . VAL B 338 ? 0.8443 0.6523 1.6178 0.1249  -0.0574 0.0759  339 VAL B O   
5547  C  CB  . VAL B 338 ? 0.6540 0.4943 1.4013 0.1223  -0.0517 0.0680  339 VAL B CB  
5548  C  CG1 . VAL B 338 ? 0.5995 0.4359 1.3543 0.1205  -0.0498 0.0547  339 VAL B CG1 
5549  C  CG2 . VAL B 338 ? 0.5416 0.3916 1.2774 0.1159  -0.0477 0.0695  339 VAL B CG2 
5550  N  N   . ILE B 339 ? 0.7368 0.5519 1.5036 0.1372  -0.0625 0.0828  340 ILE B N   
5551  C  CA  . ILE B 339 ? 0.6974 0.5007 1.4771 0.1427  -0.0662 0.0823  340 ILE B CA  
5552  C  C   . ILE B 339 ? 0.7266 0.5161 1.5107 0.1414  -0.0673 0.0971  340 ILE B C   
5553  O  O   . ILE B 339 ? 0.7380 0.5159 1.5352 0.1406  -0.0684 0.0955  340 ILE B O   
5554  C  CB  . ILE B 339 ? 0.6762 0.4825 1.4578 0.1528  -0.0709 0.0823  340 ILE B CB  
5555  C  CG1 . ILE B 339 ? 0.6366 0.4563 1.4180 0.1541  -0.0689 0.0674  340 ILE B CG1 
5556  C  CG2 . ILE B 339 ? 0.6745 0.4672 1.4692 0.1589  -0.0750 0.0838  340 ILE B CG2 
5557  C  CD1 . ILE B 339 ? 0.6550 0.4810 1.4396 0.1633  -0.0732 0.0673  340 ILE B CD1 
5558  N  N   . GLN B 340 ? 0.7156 0.5061 1.4891 0.1415  -0.0667 0.1117  341 GLN B N   
5559  C  CA  . GLN B 340 ? 0.7187 0.4969 1.4953 0.1406  -0.0661 0.1280  341 GLN B CA  
5560  C  C   . GLN B 340 ? 0.6716 0.4463 1.4561 0.1302  -0.0615 0.1268  341 GLN B C   
5561  O  O   . GLN B 340 ? 0.6896 0.4526 1.4856 0.1284  -0.0612 0.1358  341 GLN B O   
5562  C  CB  . GLN B 340 ? 0.6804 0.4612 1.4409 0.1446  -0.0660 0.1439  341 GLN B CB  
5563  C  CG  . GLN B 340 ? 0.6991 0.4771 1.4548 0.1567  -0.0723 0.1512  341 GLN B CG  
5564  C  CD  . GLN B 340 ? 0.7973 0.5698 1.5398 0.1621  -0.0725 0.1715  341 GLN B CD  
5565  O  OE1 . GLN B 340 ? 0.7533 0.5328 1.4813 0.1607  -0.0700 0.1764  341 GLN B OE1 
5566  N  NE2 . GLN B 340 ? 0.8567 0.6161 1.6034 0.1692  -0.0753 0.1837  341 GLN B NE2 
5567  N  N   . GLY B 341 ? 0.7448 0.5300 1.5244 0.1235  -0.0581 0.1157  342 GLY B N   
5568  C  CA  . GLY B 341 ? 0.7301 0.5140 1.5166 0.1140  -0.0544 0.1139  342 GLY B CA  
5569  C  C   . GLY B 341 ? 0.7057 0.4858 1.5056 0.1112  -0.0561 0.0977  342 GLY B C   
5570  O  O   . GLY B 341 ? 0.6488 0.4223 1.4614 0.1054  -0.0558 0.0981  342 GLY B O   
5571  N  N   . CYS B 342 ? 0.7258 0.5101 1.5234 0.1159  -0.0582 0.0836  343 CYS B N   
5572  C  CA  . CYS B 342 ? 0.7261 0.5075 1.5321 0.1151  -0.0596 0.0667  343 CYS B CA  
5573  C  C   . CYS B 342 ? 0.7078 0.4802 1.5239 0.1232  -0.0643 0.0612  343 CYS B C   
5574  O  O   . CYS B 342 ? 0.7052 0.4739 1.5277 0.1247  -0.0661 0.0467  343 CYS B O   
5575  C  CB  . CYS B 342 ? 0.7716 0.5659 1.5651 0.1140  -0.0564 0.0532  343 CYS B CB  
5576  S  SG  . CYS B 342 ? 0.8602 0.6656 1.6416 0.1049  -0.0510 0.0578  343 CYS B SG  
5577  N  N   . GLY B 343 ? 0.7042 0.4731 1.5210 0.1293  -0.0665 0.0725  344 GLY B N   
5578  C  CA  . GLY B 343 ? 0.6919 0.4520 1.5189 0.1375  -0.0710 0.0689  344 GLY B CA  
5579  C  C   . GLY B 343 ? 0.7506 0.5203 1.5708 0.1451  -0.0713 0.0599  344 GLY B C   
5580  O  O   . GLY B 343 ? 0.7448 0.5281 1.5528 0.1437  -0.0680 0.0566  344 GLY B O   
5581  N  N   . ASN B 344 ? 0.8459 0.6087 1.6755 0.1532  -0.0752 0.0561  345 ASN B N   
5582  C  CA  . ASN B 344 ? 0.8661 0.6379 1.6927 0.1613  -0.0754 0.0481  345 ASN B CA  
5583  C  C   . ASN B 344 ? 0.8906 0.6662 1.7177 0.1630  -0.0728 0.0294  345 ASN B C   
5584  O  O   . ASN B 344 ? 0.9242 0.6889 1.7606 0.1649  -0.0748 0.0210  345 ASN B O   
5585  C  CB  . ASN B 344 ? 0.9291 0.6926 1.7654 0.1705  -0.0806 0.0539  345 ASN B CB  
5586  C  CG  . ASN B 344 ? 0.9712 0.7354 1.8018 0.1727  -0.0830 0.0714  345 ASN B CG  
5587  O  OD1 . ASN B 344 ? 0.9883 0.7418 1.8212 0.1707  -0.0844 0.0849  345 ASN B OD1 
5588  N  ND2 . ASN B 344 ? 0.9936 0.7705 1.8170 0.1776  -0.0837 0.0715  345 ASN B ND2 
5589  N  N   . PRO B 345 ? 0.8436 0.6342 1.6602 0.1627  -0.0682 0.0229  346 PRO B N   
5590  C  CA  . PRO B 345 ? 0.8738 0.6700 1.6877 0.1660  -0.0642 0.0064  346 PRO B CA  
5591  C  C   . PRO B 345 ? 0.9004 0.6965 1.7223 0.1770  -0.0653 -0.0002 346 PRO B C   
5592  O  O   . PRO B 345 ? 0.9144 0.7093 1.7428 0.1817  -0.0692 0.0082  346 PRO B O   
5593  C  CB  . PRO B 345 ? 0.8085 0.6213 1.6100 0.1619  -0.0587 0.0064  346 PRO B CB  
5594  C  CG  . PRO B 345 ? 0.8033 0.6209 1.6041 0.1614  -0.0614 0.0205  346 PRO B CG  
5595  C  CD  . PRO B 345 ? 0.8497 0.6529 1.6562 0.1597  -0.0664 0.0319  346 PRO B CD  
5596  N  N   . LYS B 346 ? 0.9198 0.7169 1.7403 0.1821  -0.0618 -0.0150 347 LYS B N   
5597  C  CA  . LYS B 346 ? 0.9004 0.6986 1.7282 0.1934  -0.0617 -0.0220 347 LYS B CA  
5598  C  C   . LYS B 346 ? 0.9020 0.7179 1.7278 0.1958  -0.0579 -0.0191 347 LYS B C   
5599  O  O   . LYS B 346 ? 0.9049 0.7311 1.7230 0.1888  -0.0557 -0.0131 347 LYS B O   
5600  C  CB  . LYS B 346 ? 0.9085 0.7027 1.7331 0.1992  -0.0582 -0.0387 347 LYS B CB  
5601  C  CG  . LYS B 346 ? 0.9234 0.7142 1.7565 0.2121  -0.0585 -0.0472 347 LYS B CG  
5602  C  CD  . LYS B 346 ? 0.9303 0.7187 1.7556 0.2188  -0.0539 -0.0639 347 LYS B CD  
5603  C  CE  . LYS B 346 ? 0.9500 0.7408 1.7805 0.2329  -0.0509 -0.0724 347 LYS B CE  
5604  N  NZ  . LYS B 346 ? 0.9666 0.7577 1.7855 0.2411  -0.0445 -0.0879 347 LYS B NZ  
5605  N  N   . VAL B 347 ? 0.9174 0.7371 1.7515 0.2059  -0.0574 -0.0237 348 VAL B N   
5606  C  CA  . VAL B 347 ? 0.9001 0.7370 1.7367 0.2089  -0.0544 -0.0217 348 VAL B CA  
5607  C  C   . VAL B 347 ? 0.9017 0.7441 1.7405 0.2185  -0.0477 -0.0350 348 VAL B C   
5608  O  O   . VAL B 347 ? 0.9368 0.7694 1.7717 0.2221  -0.0459 -0.0448 348 VAL B O   
5609  C  CB  . VAL B 347 ? 0.7265 0.5633 1.5740 0.2126  -0.0618 -0.0111 348 VAL B CB  
5610  C  CG1 . VAL B 347 ? 0.7275 0.5828 1.5779 0.2133  -0.0605 -0.0078 348 VAL B CG1 
5611  C  CG2 . VAL B 347 ? 0.7212 0.5466 1.5658 0.2061  -0.0685 0.0016  348 VAL B CG2 
5612  N  N   . ASN B 348 ? 0.8854 0.7437 1.7305 0.2231  -0.0439 -0.0352 349 ASN B N   
5613  C  CA  . ASN B 348 ? 0.8621 0.7274 1.7117 0.2340  -0.0368 -0.0458 349 ASN B CA  
5614  C  C   . ASN B 348 ? 0.8491 0.7184 1.6852 0.2343  -0.0271 -0.0553 349 ASN B C   
5615  O  O   . ASN B 348 ? 0.8153 0.6921 1.6421 0.2259  -0.0235 -0.0526 349 ASN B O   
5616  C  CB  . ASN B 348 ? 0.8530 0.7044 1.7109 0.2441  -0.0408 -0.0511 349 ASN B CB  
5617  C  CG  . ASN B 348 ? 0.8961 0.7574 1.7683 0.2553  -0.0387 -0.0535 349 ASN B CG  
5618  O  OD1 . ASN B 348 ? 0.9025 0.7797 1.7759 0.2589  -0.0302 -0.0574 349 ASN B OD1 
5619  N  ND2 . ASN B 348 ? 0.8926 0.7451 1.7769 0.2608  -0.0463 -0.0503 349 ASN B ND2 
5620  N  N   . ARG B 360 ? 1.1349 1.2198 2.1321 0.0824  -0.0298 -0.0073 361 ARG B N   
5621  C  CA  . ARG B 360 ? 1.1212 1.1999 2.0916 0.0810  -0.0166 -0.0035 361 ARG B CA  
5622  C  C   . ARG B 360 ? 1.0612 1.1315 2.0014 0.0815  -0.0254 -0.0037 361 ARG B C   
5623  O  O   . ARG B 360 ? 1.0688 1.1382 2.0077 0.0838  -0.0412 -0.0062 361 ARG B O   
5624  C  CB  . ARG B 360 ? 1.1301 1.2104 2.0985 0.0871  -0.0041 -0.0014 361 ARG B CB  
5625  N  N   . GLY B 361 ? 1.0141 1.0783 1.9303 0.0802  -0.0152 -0.0010 362 GLY B N   
5626  C  CA  . GLY B 361 ? 0.9641 1.0200 1.8524 0.0803  -0.0214 -0.0002 362 GLY B CA  
5627  C  C   . GLY B 361 ? 0.9203 0.9750 1.8046 0.0751  -0.0301 -0.0015 362 GLY B C   
5628  O  O   . GLY B 361 ? 0.9338 0.9845 1.8035 0.0774  -0.0416 -0.0018 362 GLY B O   
5629  N  N   . LYS B 362 ? 0.8505 0.9082 1.7478 0.0687  -0.0244 -0.0020 363 LYS B N   
5630  C  CA  . LYS B 362 ? 0.8380 0.8944 1.7343 0.0638  -0.0324 -0.0042 363 LYS B CA  
5631  C  C   . LYS B 362 ? 0.8284 0.8791 1.7028 0.0587  -0.0232 -0.0014 363 LYS B C   
5632  O  O   . LYS B 362 ? 0.8575 0.9083 1.7343 0.0551  -0.0091 0.0012  363 LYS B O   
5633  C  CB  . LYS B 362 ? 0.8161 0.8781 1.7433 0.0599  -0.0335 -0.0068 363 LYS B CB  
5634  N  N   . LEU B 363 ? 0.7901 0.8360 1.6431 0.0593  -0.0311 -0.0017 364 LEU B N   
5635  C  CA  . LEU B 363 ? 0.7482 0.7887 1.5795 0.0550  -0.0238 0.0008  364 LEU B CA  
5636  C  C   . LEU B 363 ? 0.8046 0.8441 1.6333 0.0512  -0.0315 -0.0017 364 LEU B C   
5637  O  O   . LEU B 363 ? 0.8011 0.8414 1.6300 0.0547  -0.0459 -0.0049 364 LEU B O   
5638  C  CB  . LEU B 363 ? 0.7129 0.7478 1.5193 0.0589  -0.0240 0.0035  364 LEU B CB  
5639  C  CG  . LEU B 363 ? 0.6232 0.6555 1.4215 0.0605  -0.0116 0.0061  364 LEU B CG  
5640  C  CD1 . LEU B 363 ? 0.6471 0.6849 1.4657 0.0609  -0.0026 0.0056  364 LEU B CD1 
5641  C  CD2 . LEU B 363 ? 0.6599 0.6874 1.4457 0.0667  -0.0168 0.0075  364 LEU B CD2 
5642  N  N   . ALA B 364 ? 0.8496 0.8871 1.6750 0.0450  -0.0221 -0.0003 365 ALA B N   
5643  C  CA  . ALA B 364 ? 0.8936 0.9289 1.7121 0.0417  -0.0280 -0.0024 365 ALA B CA  
5644  C  C   . ALA B 364 ? 0.9442 0.9757 1.7361 0.0451  -0.0332 -0.0010 365 ALA B C   
5645  O  O   . ALA B 364 ? 0.9495 0.9776 1.7250 0.0457  -0.0250 0.0030  365 ALA B O   
5646  C  CB  . ALA B 364 ? 0.8511 0.8839 1.6699 0.0349  -0.0156 -0.0001 365 ALA B CB  
5647  N  N   . PRO B 365 ? 1.0493 1.0811 1.8370 0.0482  -0.0469 -0.0043 366 PRO B N   
5648  C  CA  . PRO B 365 ? 1.0637 1.0917 1.8266 0.0526  -0.0517 -0.0019 366 PRO B CA  
5649  C  C   . PRO B 365 ? 1.0305 1.0547 1.7772 0.0473  -0.0422 0.0007  366 PRO B C   
5650  O  O   . PRO B 365 ? 1.0309 1.0552 1.7848 0.0409  -0.0317 0.0010  366 PRO B O   
5651  C  CB  . PRO B 365 ? 1.1086 1.1390 1.8741 0.0579  -0.0684 -0.0070 366 PRO B CB  
5652  C  CG  . PRO B 365 ? 1.1171 1.1526 1.9107 0.0568  -0.0740 -0.0125 366 PRO B CG  
5653  C  CD  . PRO B 365 ? 1.0809 1.1164 1.8879 0.0485  -0.0590 -0.0107 366 PRO B CD  
5654  N  N   . ARG B 366 ? 0.9955 1.0162 1.7212 0.0504  -0.0452 0.0032  367 ARG B N   
5655  C  CA  . ARG B 366 ? 0.9688 0.9862 1.6797 0.0456  -0.0364 0.0057  367 ARG B CA  
5656  C  C   . ARG B 366 ? 1.0207 1.0400 1.7422 0.0396  -0.0350 0.0017  367 ARG B C   
5657  O  O   . ARG B 366 ? 1.0454 1.0671 1.7753 0.0413  -0.0456 -0.0033 367 ARG B O   
5658  C  CB  . ARG B 366 ? 0.8793 0.8934 1.5696 0.0505  -0.0417 0.0085  367 ARG B CB  
5659  C  CG  . ARG B 366 ? 0.7994 0.8110 1.4766 0.0457  -0.0344 0.0101  367 ARG B CG  
5660  C  CD  . ARG B 366 ? 0.7341 0.7406 1.3930 0.0475  -0.0298 0.0164  367 ARG B CD  
5661  N  NE  . ARG B 366 ? 0.7296 0.7340 1.3783 0.0562  -0.0391 0.0194  367 ARG B NE  
5662  C  CZ  . ARG B 366 ? 0.7297 0.7316 1.3771 0.0622  -0.0428 0.0231  367 ARG B CZ  
5663  N  NH1 . ARG B 366 ? 0.7200 0.7218 1.3767 0.0602  -0.0384 0.0232  367 ARG B NH1 
5664  N  NH2 . ARG B 366 ? 0.7511 0.7504 1.3876 0.0712  -0.0508 0.0271  367 ARG B NH2 
5665  N  N   . GLU B 367 ? 1.0920 1.1097 1.8132 0.0332  -0.0224 0.0038  368 GLU B N   
5666  C  CA  . GLU B 367 ? 1.1500 1.1684 1.8847 0.0278  -0.0201 0.0011  368 GLU B CA  
5667  C  C   . GLU B 367 ? 1.2304 1.2474 1.9534 0.0271  -0.0246 -0.0007 368 GLU B C   
5668  O  O   . GLU B 367 ? 1.2493 1.2637 1.9545 0.0258  -0.0185 0.0026  368 GLU B O   
5669  C  CB  . GLU B 367 ? 1.1630 1.1797 1.9001 0.0228  -0.0048 0.0049  368 GLU B CB  
5670  N  N   . ARG B 368 ? 1.2600 1.2788 1.9942 0.0283  -0.0358 -0.0066 369 ARG B N   
5671  C  CA  . ARG B 368 ? 1.2887 1.3067 2.0138 0.0288  -0.0414 -0.0097 369 ARG B CA  
5672  C  C   . ARG B 368 ? 1.3243 1.3396 2.0563 0.0209  -0.0319 -0.0091 369 ARG B C   
5673  O  O   . ARG B 368 ? 1.3561 1.3711 2.1098 0.0172  -0.0305 -0.0109 369 ARG B O   
5674  C  CB  . ARG B 368 ? 1.2825 1.3034 2.0175 0.0342  -0.0582 -0.0176 369 ARG B CB  
5675  N  N   . PRO B 369 ? 1.3305 1.3434 2.0450 0.0188  -0.0249 -0.0060 370 PRO B N   
5676  C  CA  . PRO B 369 ? 1.2953 1.3049 2.0133 0.0121  -0.0126 -0.0028 370 PRO B CA  
5677  C  C   . PRO B 369 ? 1.2518 1.2597 1.9922 0.0083  -0.0152 -0.0068 370 PRO B C   
5678  O  O   . PRO B 369 ? 1.2780 1.2862 2.0226 0.0092  -0.0254 -0.0129 370 PRO B O   
5679  C  CB  . PRO B 369 ? 1.3237 1.3318 2.0201 0.0117  -0.0092 -0.0008 370 PRO B CB  
5680  C  CG  . PRO B 369 ? 1.3271 1.3367 2.0072 0.0177  -0.0137 0.0007  370 PRO B CG  
5681  C  CD  . PRO B 369 ? 1.3344 1.3469 2.0253 0.0231  -0.0263 -0.0038 370 PRO B CD  
5682  N  N   . PRO B 370 ? 1.1949 1.2003 1.9504 0.0048  -0.0057 -0.0031 371 PRO B N   
5683  C  CA  . PRO B 370 ? 1.1646 1.1666 1.9460 0.0015  -0.0058 -0.0048 371 PRO B CA  
5684  C  C   . PRO B 370 ? 1.0985 1.0978 1.8735 -0.0005 -0.0016 -0.0040 371 PRO B C   
5685  O  O   . PRO B 370 ? 1.1218 1.1204 1.9112 -0.0008 -0.0073 -0.0082 371 PRO B O   
5686  C  CB  . PRO B 370 ? 1.1758 1.1769 1.9672 0.0008  0.0067  0.0018  371 PRO B CB  
5687  C  CG  . PRO B 370 ? 1.1877 1.1902 1.9546 0.0022  0.0160  0.0070  371 PRO B CG  
5688  C  CD  . PRO B 370 ? 1.1878 1.1934 1.9358 0.0051  0.0064  0.0035  371 PRO B CD  
5689  N  N   . SER B 371 ? 1.0420 1.0410 1.7938 -0.0007 0.0085  0.0015  372 SER B N   
5690  C  CA  . SER B 371 ? 0.9650 0.9626 1.7080 -0.0013 0.0176  0.0055  372 SER B CA  
5691  C  C   . SER B 371 ? 0.9090 0.9065 1.6400 -0.0016 0.0116  0.0015  372 SER B C   
5692  O  O   . SER B 371 ? 0.9431 0.9416 1.6590 -0.0012 0.0083  0.0002  372 SER B O   
5693  C  CB  . SER B 371 ? 0.9667 0.9636 1.6934 -0.0008 0.0317  0.0133  372 SER B CB  
5694  O  OG  . SER B 371 ? 1.0161 1.0111 1.7431 -0.0008 0.0421  0.0188  372 SER B OG  
5695  N  N   . GLY B 372 ? 0.7362 0.7327 1.4762 -0.0021 0.0106  0.0000  373 GLY B N   
5696  C  CA  . GLY B 372 ? 0.6326 0.6290 1.3623 -0.0024 0.0068  -0.0032 373 GLY B CA  
5697  C  C   . GLY B 372 ? 0.5025 0.4980 1.2116 -0.0026 0.0193  0.0041  373 GLY B C   
5698  O  O   . GLY B 372 ? 0.5573 0.5525 1.2582 -0.0030 0.0191  0.0032  373 GLY B O   
5699  N  N   . THR B 373 ? 0.3323 0.3273 1.0343 -0.0022 0.0298  0.0108  374 THR B N   
5700  C  CA  . THR B 373 ? 0.3512 0.3451 1.0350 -0.0018 0.0410  0.0172  374 THR B CA  
5701  C  C   . THR B 373 ? 0.3113 0.3064 0.9744 -0.0018 0.0382  0.0152  374 THR B C   
5702  O  O   . THR B 373 ? 0.2288 0.2234 0.8818 -0.0020 0.0406  0.0162  374 THR B O   
5703  C  CB  . THR B 373 ? 0.3447 0.3380 1.0274 -0.0007 0.0514  0.0233  374 THR B CB  
5704  O  OG1 . THR B 373 ? 0.3616 0.3536 1.0645 -0.0003 0.0568  0.0270  374 THR B OG1 
5705  C  CG2 . THR B 373 ? 0.2372 0.2295 0.9013 0.0001  0.0612  0.0284  374 THR B CG2 
5706  N  N   . LEU B 374 ? 0.2822 0.2787 0.9407 -0.0015 0.0332  0.0128  375 LEU B N   
5707  C  CA  . LEU B 374 ? 0.3662 0.3635 1.0076 -0.0012 0.0312  0.0119  375 LEU B CA  
5708  C  C   . LEU B 374 ? 0.2725 0.2705 0.9148 -0.0015 0.0233  0.0069  375 LEU B C   
5709  O  O   . LEU B 374 ? 0.2144 0.2124 0.8431 -0.0014 0.0250  0.0075  375 LEU B O   
5710  C  CB  . LEU B 374 ? 0.2174 0.2158 0.8581 -0.0006 0.0270  0.0111  375 LEU B CB  
5711  C  CG  . LEU B 374 ? 0.3756 0.3744 1.0001 -0.0001 0.0270  0.0119  375 LEU B CG  
5712  C  CD1 . LEU B 374 ? 0.2854 0.2832 0.8947 0.0000  0.0369  0.0164  375 LEU B CD1 
5713  C  CD2 . LEU B 374 ? 0.3431 0.3431 0.9683 0.0016  0.0215  0.0115  375 LEU B CD2 
5714  N  N   . GLU B 375 ? 0.2748 0.2732 0.9349 -0.0016 0.0143  0.0013  376 GLU B N   
5715  C  CA  . GLU B 375 ? 0.2706 0.2697 0.9353 -0.0014 0.0054  -0.0051 376 GLU B CA  
5716  C  C   . GLU B 375 ? 0.3238 0.3221 0.9822 -0.0023 0.0111  -0.0033 376 GLU B C   
5717  O  O   . GLU B 375 ? 0.3783 0.3771 1.0269 -0.0020 0.0103  -0.0045 376 GLU B O   
5718  C  CB  . GLU B 375 ? 0.2678 0.2670 0.9556 -0.0011 -0.0063 -0.0127 376 GLU B CB  
5719  N  N   . LYS B 376 ? 0.2717 0.2686 0.9375 -0.0030 0.0171  0.0003  377 LYS B N   
5720  C  CA  . LYS B 376 ? 0.3678 0.3636 1.0312 -0.0036 0.0227  0.0031  377 LYS B CA  
5721  C  C   . LYS B 376 ? 0.2346 0.2301 0.8764 -0.0033 0.0322  0.0092  377 LYS B C   
5722  O  O   . LYS B 376 ? 0.2432 0.2390 0.8781 -0.0035 0.0335  0.0094  377 LYS B O   
5723  C  CB  . LYS B 376 ? 0.4668 0.4604 1.1463 -0.0040 0.0277  0.0069  377 LYS B CB  
5724  C  CG  . LYS B 376 ? 0.4893 0.4829 1.1930 -0.0042 0.0174  0.0001  377 LYS B CG  
5725  C  CD  . LYS B 376 ? 0.5447 0.5356 1.2666 -0.0040 0.0233  0.0049  377 LYS B CD  
5726  C  CE  . LYS B 376 ? 0.5407 0.5316 1.2873 -0.0040 0.0123  -0.0022 377 LYS B CE  
5727  N  NZ  . LYS B 376 ? 0.5569 0.5500 1.3018 -0.0036 0.0058  -0.0061 377 LYS B NZ  
5728  N  N   . LEU B 377 ? 0.2219 0.2170 0.8548 -0.0027 0.0382  0.0136  378 LEU B N   
5729  C  CA  . LEU B 377 ? 0.2170 0.2117 0.8314 -0.0021 0.0457  0.0181  378 LEU B CA  
5730  C  C   . LEU B 377 ? 0.2432 0.2394 0.8458 -0.0020 0.0408  0.0148  378 LEU B C   
5731  O  O   . LEU B 377 ? 0.2078 0.2037 0.7992 -0.0018 0.0446  0.0167  378 LEU B O   
5732  C  CB  . LEU B 377 ? 0.3715 0.3658 0.9818 -0.0012 0.0511  0.0216  378 LEU B CB  
5733  C  CG  . LEU B 377 ? 0.3919 0.3844 1.0104 -0.0005 0.0605  0.0273  378 LEU B CG  
5734  C  CD1 . LEU B 377 ? 0.3973 0.3897 1.0125 0.0006  0.0652  0.0296  378 LEU B CD1 
5735  C  CD2 . LEU B 377 ? 0.2247 0.2157 0.8386 0.0002  0.0684  0.0324  378 LEU B CD2 
5736  N  N   . VAL B 378 ? 0.2092 0.2066 0.8162 -0.0018 0.0326  0.0101  379 VAL B N   
5737  C  CA  . VAL B 378 ? 0.3056 0.3038 0.9048 -0.0013 0.0285  0.0076  379 VAL B CA  
5738  C  C   . VAL B 378 ? 0.2055 0.2040 0.8093 -0.0015 0.0243  0.0035  379 VAL B C   
5739  O  O   . VAL B 378 ? 0.2020 0.2006 0.7966 -0.0012 0.0254  0.0036  379 VAL B O   
5740  C  CB  . VAL B 378 ? 0.3179 0.3169 0.9241 -0.0006 0.0211  0.0047  379 VAL B CB  
5741  C  CG1 . VAL B 378 ? 0.2029 0.2027 0.8046 0.0014  0.0163  0.0020  379 VAL B CG1 
5742  C  CG2 . VAL B 378 ? 0.2700 0.2689 0.8695 -0.0003 0.0256  0.0092  379 VAL B CG2 
5743  N  N   . SER B 379 ? 0.2107 0.2095 0.8304 -0.0020 0.0195  -0.0004 380 SER B N   
5744  C  CA  . SER B 379 ? 0.3566 0.3559 0.9831 -0.0022 0.0153  -0.0051 380 SER B CA  
5745  C  C   . SER B 379 ? 0.2107 0.2094 0.8265 -0.0027 0.0239  0.0002  380 SER B C   
5746  O  O   . SER B 379 ? 0.2606 0.2596 0.8701 -0.0023 0.0236  -0.0011 380 SER B O   
5747  C  CB  . SER B 379 ? 0.3812 0.3806 1.0289 -0.0026 0.0084  -0.0102 380 SER B CB  
5748  O  OG  . SER B 379 ? 0.4289 0.4290 1.0889 -0.0014 -0.0035 -0.0184 380 SER B OG  
5749  N  N   . GLU B 380 ? 0.2133 0.2108 0.8288 -0.0033 0.0317  0.0063  381 GLU B N   
5750  C  CA  A GLU B 380 ? 0.2129 0.2097 0.8203 -0.0032 0.0402  0.0122  381 GLU B CA  
5751  C  CA  B GLU B 380 ? 0.2128 0.2097 0.8204 -0.0033 0.0400  0.0120  381 GLU B CA  
5752  C  C   . GLU B 380 ? 0.2066 0.2033 0.7952 -0.0024 0.0436  0.0143  381 GLU B C   
5753  O  O   . GLU B 380 ? 0.2063 0.2031 0.7893 -0.0022 0.0455  0.0152  381 GLU B O   
5754  C  CB  A GLU B 380 ? 0.2177 0.2128 0.8289 -0.0031 0.0487  0.0190  381 GLU B CB  
5755  C  CB  B GLU B 380 ? 0.2180 0.2131 0.8301 -0.0032 0.0484  0.0188  381 GLU B CB  
5756  C  CG  A GLU B 380 ? 0.2185 0.2126 0.8229 -0.0023 0.0582  0.0260  381 GLU B CG  
5757  C  CG  B GLU B 380 ? 0.3572 0.3518 0.9905 -0.0040 0.0458  0.0176  381 GLU B CG  
5758  C  CD  A GLU B 380 ? 0.3696 0.3640 0.9875 -0.0029 0.0595  0.0277  381 GLU B CD  
5759  C  CD  B GLU B 380 ? 0.2285 0.2245 0.8739 -0.0049 0.0408  0.0138  381 GLU B CD  
5760  O  OE1 A GLU B 380 ? 0.4027 0.3962 1.0375 -0.0036 0.0587  0.0279  381 GLU B OE1 
5761  O  OE1 B GLU B 380 ? 0.2262 0.2232 0.8653 -0.0047 0.0443  0.0160  381 GLU B OE1 
5762  O  OE2 A GLU B 380 ? 0.2220 0.2174 0.8350 -0.0026 0.0612  0.0289  381 GLU B OE2 
5763  O  OE2 B GLU B 380 ? 0.2333 0.2297 0.8964 -0.0057 0.0329  0.0080  381 GLU B OE2 
5764  N  N   . ALA B 381 ? 0.2321 0.2286 0.8128 -0.0019 0.0441  0.0151  382 ALA B N   
5765  C  CA  . ALA B 381 ? 0.1988 0.1951 0.7643 -0.0012 0.0469  0.0170  382 ALA B CA  
5766  C  C   . ALA B 381 ? 0.1957 0.1928 0.7583 -0.0011 0.0422  0.0133  382 ALA B C   
5767  O  O   . ALA B 381 ? 0.1935 0.1902 0.7473 -0.0008 0.0451  0.0149  382 ALA B O   
5768  C  CB  . ALA B 381 ? 0.1974 0.1936 0.7589 -0.0009 0.0472  0.0180  382 ALA B CB  
5769  N  N   . LYS B 382 ? 0.1964 0.1943 0.7683 -0.0011 0.0349  0.0083  383 LYS B N   
5770  C  CA  . LYS B 382 ? 0.1947 0.1931 0.7678 -0.0004 0.0307  0.0045  383 LYS B CA  
5771  C  C   . LYS B 382 ? 0.2977 0.2961 0.8735 -0.0007 0.0308  0.0027  383 LYS B C   
5772  O  O   . LYS B 382 ? 0.2691 0.2673 0.8389 -0.0002 0.0323  0.0028  383 LYS B O   
5773  C  CB  . LYS B 382 ? 0.1978 0.1971 0.7823 0.0012  0.0219  -0.0014 383 LYS B CB  
5774  C  CG  . LYS B 382 ? 0.3290 0.3287 0.9049 0.0043  0.0210  0.0006  383 LYS B CG  
5775  C  CD  . LYS B 382 ? 0.3758 0.3768 0.9513 0.0112  0.0115  -0.0052 383 LYS B CD  
5776  C  CE  . LYS B 382 ? 0.3171 0.3188 0.8844 0.0151  0.0112  -0.0018 383 LYS B CE  
5777  N  NZ  . LYS B 382 ? 0.2184 0.2215 0.7837 0.0239  0.0019  -0.0068 383 LYS B NZ  
5778  N  N   . ALA B 383 ? 0.1998 0.1984 0.7861 -0.0014 0.0295  0.0013  384 ALA B N   
5779  C  CA  . ALA B 383 ? 0.3541 0.3529 0.9453 -0.0016 0.0297  0.0000  384 ALA B CA  
5780  C  C   . ALA B 383 ? 0.3319 0.3299 0.9099 -0.0015 0.0379  0.0065  384 ALA B C   
5781  O  O   . ALA B 383 ? 0.3892 0.3872 0.9645 -0.0012 0.0381  0.0056  384 ALA B O   
5782  C  CB  . ALA B 383 ? 0.2073 0.2067 0.8146 -0.0025 0.0275  -0.0014 384 ALA B CB  
5783  N  N   . GLN B 384 ? 0.3106 0.3079 0.8821 -0.0016 0.0442  0.0125  385 GLN B N   
5784  C  CA  . GLN B 384 ? 0.3289 0.3254 0.8910 -0.0010 0.0515  0.0184  385 GLN B CA  
5785  C  C   . GLN B 384 ? 0.3605 0.3566 0.9095 -0.0003 0.0519  0.0184  385 GLN B C   
5786  O  O   . GLN B 384 ? 0.1931 0.1888 0.7376 0.0002  0.0548  0.0206  385 GLN B O   
5787  C  CB  . GLN B 384 ? 0.4004 0.3960 0.9617 -0.0006 0.0579  0.0241  385 GLN B CB  
5788  C  CG  . GLN B 384 ? 0.5405 0.5362 1.1162 -0.0010 0.0601  0.0263  385 GLN B CG  
5789  C  CD  . GLN B 384 ? 0.6424 0.6384 1.2247 -0.0007 0.0633  0.0294  385 GLN B CD  
5790  O  OE1 . GLN B 384 ? 0.6418 0.6368 1.2187 0.0006  0.0701  0.0352  385 GLN B OE1 
5791  N  NE2 . GLN B 384 ? 0.7375 0.7349 1.3336 -0.0017 0.0583  0.0255  385 GLN B NE2 
5792  N  N   . LEU B 385 ? 0.2597 0.2560 0.8047 -0.0003 0.0490  0.0164  386 LEU B N   
5793  C  CA  . LEU B 385 ? 0.2911 0.2872 0.8268 0.0002  0.0493  0.0168  386 LEU B CA  
5794  C  C   . LEU B 385 ? 0.2713 0.2677 0.8104 0.0004  0.0463  0.0134  386 LEU B C   
5795  O  O   . LEU B 385 ? 0.1991 0.1952 0.7327 0.0009  0.0481  0.0146  386 LEU B O   
5796  C  CB  . LEU B 385 ? 0.3249 0.3212 0.8583 0.0004  0.0478  0.0168  386 LEU B CB  
5797  C  CG  . LEU B 385 ? 0.2358 0.2317 0.7660 0.0004  0.0508  0.0196  386 LEU B CG  
5798  C  CD1 . LEU B 385 ? 0.2334 0.2296 0.7631 0.0005  0.0485  0.0193  386 LEU B CD1 
5799  C  CD2 . LEU B 385 ? 0.3361 0.3312 0.8597 0.0009  0.0557  0.0228  386 LEU B CD2 
5800  N  N   . ARG B 386 ? 0.2923 0.2893 0.8429 0.0003  0.0414  0.0086  387 ARG B N   
5801  C  CA  . ARG B 386 ? 0.3661 0.3634 0.9178 0.0028  0.0378  0.0039  387 ARG B CA  
5802  C  C   . ARG B 386 ? 0.3431 0.3401 0.8974 0.0018  0.0401  0.0046  387 ARG B C   
5803  O  O   . ARG B 386 ? 0.2814 0.2782 0.8281 0.0050  0.0399  0.0032  387 ARG B O   
5804  C  CB  . ARG B 386 ? 0.3335 0.3315 0.8938 0.0054  0.0302  -0.0031 387 ARG B CB  
5805  N  N   . ASP B 387 ? 0.3386 0.3356 0.8982 0.0000  0.0425  0.0073  388 ASP B N   
5806  C  CA  . ASP B 387 ? 0.3798 0.3766 0.9422 0.0001  0.0448  0.0090  388 ASP B CA  
5807  C  C   . ASP B 387 ? 0.3207 0.3167 0.8719 0.0007  0.0496  0.0135  388 ASP B C   
5808  O  O   . ASP B 387 ? 0.3975 0.3934 0.9514 0.0011  0.0504  0.0136  388 ASP B O   
5809  C  CB  . ASP B 387 ? 0.4199 0.4168 0.9891 -0.0004 0.0475  0.0125  388 ASP B CB  
5810  C  CG  . ASP B 387 ? 0.5062 0.5031 1.0814 -0.0001 0.0503  0.0153  388 ASP B CG  
5811  O  OD1 . ASP B 387 ? 0.5514 0.5487 1.1370 -0.0003 0.0460  0.0104  388 ASP B OD1 
5812  O  OD2 . ASP B 387 ? 0.5456 0.5418 1.1169 0.0006  0.0568  0.0223  388 ASP B OD2 
5813  N  N   . VAL B 388 ? 0.2683 0.2639 0.8091 0.0010  0.0522  0.0167  389 VAL B N   
5814  C  CA  . VAL B 388 ? 0.1882 0.1832 0.7213 0.0017  0.0558  0.0205  389 VAL B CA  
5815  C  C   . VAL B 388 ? 0.2854 0.2805 0.8125 0.0019  0.0547  0.0194  389 VAL B C   
5816  O  O   . VAL B 388 ? 0.1845 0.1793 0.7067 0.0024  0.0565  0.0219  389 VAL B O   
5817  C  CB  . VAL B 388 ? 0.2093 0.2038 0.7389 0.0021  0.0601  0.0252  389 VAL B CB  
5818  C  CG1 . VAL B 388 ? 0.1931 0.1875 0.7306 0.0023  0.0634  0.0284  389 VAL B CG1 
5819  C  CG2 . VAL B 388 ? 0.1876 0.1822 0.7130 0.0017  0.0589  0.0242  389 VAL B CG2 
5820  N  N   . GLN B 389 ? 0.1859 0.1815 0.7130 0.0029  0.0514  0.0157  390 GLN B N   
5821  C  CA  . GLN B 389 ? 0.2788 0.2751 0.7986 0.0050  0.0513  0.0158  390 GLN B CA  
5822  C  C   . GLN B 389 ? 0.3013 0.2982 0.8176 0.0072  0.0521  0.0159  390 GLN B C   
5823  O  O   . GLN B 389 ? 0.2342 0.2320 0.7471 0.0080  0.0532  0.0176  390 GLN B O   
5824  C  CB  . GLN B 389 ? 0.3478 0.3455 0.8671 0.0080  0.0484  0.0127  390 GLN B CB  
5825  C  CG  . GLN B 389 ? 0.5451 0.5427 1.0641 0.0072  0.0482  0.0144  390 GLN B CG  
5826  C  CD  . GLN B 389 ? 0.6659 0.6660 1.1812 0.0119  0.0475  0.0143  390 GLN B CD  
5827  O  OE1 . GLN B 389 ? 0.7416 0.7440 1.2548 0.0168  0.0466  0.0115  390 GLN B OE1 
5828  N  NE2 . GLN B 389 ? 0.6747 0.6748 1.1899 0.0113  0.0485  0.0177  390 GLN B NE2 
5829  N  N   . ASP B 390 ? 0.2640 0.2607 0.7835 0.0080  0.0514  0.0140  391 ASP B N   
5830  C  CA  . ASP B 390 ? 0.2151 0.2126 0.7322 0.0106  0.0517  0.0135  391 ASP B CA  
5831  C  C   . ASP B 390 ? 0.2620 0.2586 0.7792 0.0098  0.0535  0.0171  391 ASP B C   
5832  O  O   . ASP B 390 ? 0.3183 0.3156 0.8344 0.0121  0.0534  0.0170  391 ASP B O   
5833  C  CB  . ASP B 390 ? 0.3794 0.3771 0.9001 0.0133  0.0491  0.0086  391 ASP B CB  
5834  C  CG  . ASP B 390 ? 0.5007 0.4966 1.0308 0.0106  0.0480  0.0081  391 ASP B CG  
5835  O  OD1 . ASP B 390 ? 0.5990 0.5943 1.1318 0.0072  0.0504  0.0124  391 ASP B OD1 
5836  O  OD2 . ASP B 390 ? 0.5828 0.5782 1.1188 0.0123  0.0449  0.0034  391 ASP B OD2 
5837  N  N   . PHE B 391 ? 0.1897 0.1853 0.7081 0.0077  0.0553  0.0202  392 PHE B N   
5838  C  CA  . PHE B 391 ? 0.2695 0.2644 0.7874 0.0088  0.0575  0.0241  392 PHE B CA  
5839  C  C   . PHE B 391 ? 0.2973 0.2931 0.8108 0.0119  0.0566  0.0244  392 PHE B C   
5840  O  O   . PHE B 391 ? 0.3664 0.3618 0.8807 0.0144  0.0568  0.0256  392 PHE B O   
5841  C  CB  . PHE B 391 ? 0.1906 0.1851 0.7071 0.0080  0.0597  0.0268  392 PHE B CB  
5842  C  CG  . PHE B 391 ? 0.1954 0.1889 0.7100 0.0113  0.0628  0.0311  392 PHE B CG  
5843  C  CD1 . PHE B 391 ? 0.1988 0.1912 0.7194 0.0115  0.0665  0.0348  392 PHE B CD1 
5844  C  CD2 . PHE B 391 ? 0.1980 0.1916 0.7060 0.0150  0.0620  0.0316  392 PHE B CD2 
5845  C  CE1 . PHE B 391 ? 0.2058 0.1965 0.7236 0.0161  0.0706  0.0401  392 PHE B CE1 
5846  C  CE2 . PHE B 391 ? 0.2052 0.1973 0.7094 0.0203  0.0646  0.0355  392 PHE B CE2 
5847  C  CZ  . PHE B 391 ? 0.2097 0.1999 0.7177 0.0212  0.0696  0.0404  392 PHE B CZ  
5848  N  N   . TRP B 392 ? 0.1916 0.1888 0.7023 0.0118  0.0552  0.0235  393 TRP B N   
5849  C  CA  . TRP B 392 ? 0.2780 0.2769 0.7874 0.0145  0.0535  0.0235  393 TRP B CA  
5850  C  C   . TRP B 392 ? 0.3172 0.3178 0.8279 0.0164  0.0525  0.0220  393 TRP B C   
5851  O  O   . TRP B 392 ? 0.3926 0.3948 0.9035 0.0194  0.0509  0.0224  393 TRP B O   
5852  C  CB  . TRP B 392 ? 0.1910 0.1912 0.7016 0.0130  0.0520  0.0227  393 TRP B CB  
5853  C  CG  . TRP B 392 ? 0.1902 0.1890 0.6997 0.0121  0.0524  0.0234  393 TRP B CG  
5854  C  CD1 . TRP B 392 ? 0.2912 0.2890 0.8017 0.0091  0.0532  0.0233  393 TRP B CD1 
5855  C  CD2 . TRP B 392 ? 0.2722 0.2705 0.7786 0.0157  0.0522  0.0242  393 TRP B CD2 
5856  N  NE1 . TRP B 392 ? 0.2891 0.2863 0.7982 0.0099  0.0535  0.0237  393 TRP B NE1 
5857  C  CE2 . TRP B 392 ? 0.2843 0.2816 0.7902 0.0144  0.0531  0.0242  393 TRP B CE2 
5858  C  CE3 . TRP B 392 ? 0.2677 0.2662 0.7711 0.0210  0.0512  0.0251  393 TRP B CE3 
5859  C  CZ2 . TRP B 392 ? 0.2781 0.2742 0.7798 0.0188  0.0535  0.0245  393 TRP B CZ2 
5860  C  CZ3 . TRP B 392 ? 0.3002 0.2971 0.7986 0.0259  0.0515  0.0259  393 TRP B CZ3 
5861  C  CH2 . TRP B 392 ? 0.2961 0.2917 0.7934 0.0250  0.0528  0.0254  393 TRP B CH2 
5862  N  N   . ILE B 393 ? 0.1949 0.1957 0.7066 0.0158  0.0530  0.0199  394 ILE B N   
5863  C  CA  . ILE B 393 ? 0.3317 0.3345 0.8444 0.0187  0.0525  0.0178  394 ILE B CA  
5864  C  C   . ILE B 393 ? 0.3530 0.3534 0.8677 0.0196  0.0523  0.0168  394 ILE B C   
5865  O  O   . ILE B 393 ? 0.3893 0.3905 0.9052 0.0226  0.0515  0.0151  394 ILE B O   
5866  C  CB  . ILE B 393 ? 0.3279 0.3336 0.8403 0.0198  0.0533  0.0156  394 ILE B CB  
5867  C  CG1 . ILE B 393 ? 0.1981 0.2021 0.7098 0.0191  0.0532  0.0134  394 ILE B CG1 
5868  C  CG2 . ILE B 393 ? 0.4165 0.4244 0.9299 0.0185  0.0541  0.0178  394 ILE B CG2 
5869  C  CD1 . ILE B 393 ? 0.2011 0.2088 0.7113 0.0229  0.0541  0.0108  394 ILE B CD1 
5870  N  N   . SER B 394 ? 0.3254 0.3231 0.8422 0.0171  0.0530  0.0179  395 SER B N   
5871  C  CA  . SER B 394 ? 0.2594 0.2549 0.7821 0.0172  0.0529  0.0175  395 SER B CA  
5872  C  C   . SER B 394 ? 0.2388 0.2326 0.7624 0.0189  0.0547  0.0226  395 SER B C   
5873  O  O   . SER B 394 ? 0.2688 0.2608 0.7985 0.0198  0.0549  0.0233  395 SER B O   
5874  C  CB  . SER B 394 ? 0.2590 0.2533 0.7869 0.0139  0.0531  0.0168  395 SER B CB  
5875  O  OG  . SER B 394 ? 0.2694 0.2631 0.7979 0.0120  0.0561  0.0219  395 SER B OG  
5876  N  N   . LEU B 395 ? 0.2416 0.2360 0.7599 0.0201  0.0556  0.0260  396 LEU B N   
5877  C  CA  . LEU B 395 ? 0.3454 0.3382 0.8622 0.0240  0.0572  0.0310  396 LEU B CA  
5878  C  C   . LEU B 395 ? 0.4039 0.3958 0.9228 0.0276  0.0559  0.0313  396 LEU B C   
5879  O  O   . LEU B 395 ? 0.4938 0.4826 1.0163 0.0293  0.0582  0.0356  396 LEU B O   
5880  C  CB  . LEU B 395 ? 0.4264 0.4207 0.9362 0.0268  0.0560  0.0320  396 LEU B CB  
5881  C  CG  . LEU B 395 ? 0.4693 0.4632 0.9764 0.0252  0.0578  0.0331  396 LEU B CG  
5882  C  CD1 . LEU B 395 ? 0.4438 0.4395 0.9459 0.0286  0.0548  0.0319  396 LEU B CD1 
5883  C  CD2 . LEU B 395 ? 0.4690 0.4597 0.9770 0.0267  0.0628  0.0387  396 LEU B CD2 
5884  N  N   . PRO B 396 ? 0.4149 0.4095 0.9326 0.0290  0.0528  0.0272  397 PRO B N   
5885  C  CA  . PRO B 396 ? 0.4276 0.4214 0.9475 0.0330  0.0516  0.0275  397 PRO B CA  
5886  C  C   . PRO B 396 ? 0.4286 0.4192 0.9560 0.0319  0.0521  0.0263  397 PRO B C   
5887  O  O   . PRO B 396 ? 0.4249 0.4122 0.9556 0.0346  0.0530  0.0301  397 PRO B O   
5888  C  CB  . PRO B 396 ? 0.3913 0.3898 0.9101 0.0343  0.0489  0.0230  397 PRO B CB  
5889  C  CG  . PRO B 396 ? 0.3425 0.3440 0.8584 0.0318  0.0487  0.0224  397 PRO B CG  
5890  C  CD  . PRO B 396 ? 0.4065 0.4053 0.9222 0.0277  0.0510  0.0233  397 PRO B CD  
5891  N  N   . GLY B 397 ? 0.4393 0.4306 0.9696 0.0289  0.0512  0.0209  398 GLY B N   
5892  C  CA  . GLY B 397 ? 0.4026 0.3912 0.9417 0.0283  0.0501  0.0179  398 GLY B CA  
5893  C  C   . GLY B 397 ? 0.4033 0.3887 0.9507 0.0260  0.0529  0.0234  398 GLY B C   
5894  O  O   . GLY B 397 ? 0.4721 0.4546 1.0287 0.0269  0.0529  0.0247  398 GLY B O   
5895  N  N   . THR B 398 ? 0.4463 0.4327 0.9919 0.0232  0.0557  0.0271  399 THR B N   
5896  C  CA  . THR B 398 ? 0.4911 0.4759 1.0449 0.0217  0.0601  0.0337  399 THR B CA  
5897  C  C   . THR B 398 ? 0.5152 0.4968 1.0676 0.0265  0.0631  0.0413  399 THR B C   
5898  O  O   . THR B 398 ? 0.5492 0.5281 1.1122 0.0271  0.0641  0.0437  399 THR B O   
5899  C  CB  . THR B 398 ? 0.5094 0.4958 1.0588 0.0195  0.0631  0.0365  399 THR B CB  
5900  O  OG1 . THR B 398 ? 0.5389 0.5274 1.0920 0.0152  0.0604  0.0305  399 THR B OG1 
5901  C  CG2 . THR B 398 ? 0.5336 0.5186 1.0904 0.0197  0.0694  0.0450  399 THR B CG2 
5902  N  N   . LEU B 399 ? 0.4643 0.4460 1.0044 0.0306  0.0638  0.0445  400 LEU B N   
5903  C  CA  . LEU B 399 ? 0.4866 0.4648 1.0228 0.0371  0.0663  0.0521  400 LEU B CA  
5904  C  C   . LEU B 399 ? 0.5808 0.5565 1.1222 0.0397  0.0640  0.0517  400 LEU B C   
5905  O  O   . LEU B 399 ? 0.5476 0.5190 1.0911 0.0440  0.0671  0.0593  400 LEU B O   
5906  C  CB  . LEU B 399 ? 0.4569 0.4365 0.9791 0.0422  0.0644  0.0525  400 LEU B CB  
5907  C  CG  . LEU B 399 ? 0.5170 0.4986 1.0331 0.0408  0.0658  0.0522  400 LEU B CG  
5908  C  CD1 . LEU B 399 ? 0.5298 0.5141 1.0356 0.0452  0.0613  0.0493  400 LEU B CD1 
5909  C  CD2 . LEU B 399 ? 0.4969 0.4751 1.0133 0.0430  0.0728  0.0606  400 LEU B CD2 
5910  N  N   . CYS B 400 ? 0.5957 0.5736 1.1389 0.0379  0.0591  0.0433  401 CYS B N   
5911  C  CA  . CYS B 400 ? 0.6400 0.6156 1.1883 0.0407  0.0565  0.0415  401 CYS B CA  
5912  C  C   . CYS B 400 ? 0.7635 0.7357 1.3272 0.0378  0.0574  0.0416  401 CYS B C   
5913  O  O   . CYS B 400 ? 0.8372 0.8049 1.4074 0.0404  0.0596  0.0480  401 CYS B O   
5914  C  CB  . CYS B 400 ? 0.6378 0.6172 1.1824 0.0411  0.0516  0.0325  401 CYS B CB  
5915  S  SG  . CYS B 400 ? 0.8039 0.7879 1.3368 0.0459  0.0493  0.0325  401 CYS B SG  
5916  N  N   . SER B 401 ? 0.8078 0.7821 1.3782 0.0329  0.0551  0.0344  402 SER B N   
5917  C  CA  . SER B 401 ? 0.8545 0.8265 1.4419 0.0303  0.0538  0.0318  402 SER B CA  
5918  C  C   . SER B 401 ? 0.9221 0.8927 1.5220 0.0284  0.0596  0.0414  402 SER B C   
5919  O  O   . SER B 401 ? 0.9534 0.9210 1.5689 0.0283  0.0602  0.0439  402 SER B O   
5920  C  CB  . SER B 401 ? 0.8271 0.8019 1.4177 0.0266  0.0495  0.0220  402 SER B CB  
5921  O  OG  . SER B 401 ? 0.8160 0.7937 1.4095 0.0222  0.0524  0.0248  402 SER B OG  
5922  N  N   . GLU B 402 ? 0.9666 0.9395 1.5600 0.0273  0.0644  0.0468  403 GLU B N   
5923  C  CA  . GLU B 402 ? 1.0477 1.0211 1.6532 0.0252  0.0710  0.0552  403 GLU B CA  
5924  C  C   . GLU B 402 ? 1.0807 1.0492 1.6856 0.0306  0.0773  0.0672  403 GLU B C   
5925  O  O   . GLU B 402 ? 1.1261 1.0939 1.7466 0.0299  0.0832  0.0751  403 GLU B O   
5926  C  CB  . GLU B 402 ? 1.0789 1.0559 1.6760 0.0231  0.0736  0.0559  403 GLU B CB  
5927  C  CG  . GLU B 402 ? 1.1361 1.1139 1.7418 0.0226  0.0818  0.0654  403 GLU B CG  
5928  C  CD  . GLU B 402 ? 1.1950 1.1691 1.7842 0.0292  0.0875  0.0747  403 GLU B CD  
5929  O  OE1 . GLU B 402 ? 1.2206 1.1954 1.7921 0.0311  0.0859  0.0723  403 GLU B OE1 
5930  O  OE2 . GLU B 402 ? 1.2187 1.1890 1.8131 0.0333  0.0932  0.0845  403 GLU B OE2 
5931  N  N   . LYS B 403 ? 1.0923 1.0579 1.6803 0.0366  0.0758  0.0687  404 LYS B N   
5932  C  CA  . LYS B 403 ? 1.0718 1.0319 1.6541 0.0440  0.0803  0.0797  404 LYS B CA  
5933  C  C   . LYS B 403 ? 1.0254 0.9815 1.6074 0.0481  0.0756  0.0780  404 LYS B C   
5934  O  O   . LYS B 403 ? 1.0571 1.0100 1.6545 0.0471  0.0758  0.0795  404 LYS B O   
5935  C  CB  . LYS B 403 ? 0.8368 0.7970 1.3977 0.0501  0.0815  0.0832  404 LYS B CB  
5936  C  CG  . LYS B 403 ? 1.1500 1.1107 1.7046 0.0515  0.0886  0.0902  404 LYS B CG  
5937  C  CD  . LYS B 403 ? 1.1720 1.1285 1.7341 0.0551  0.0989  0.1044  404 LYS B CD  
5938  C  CE  . LYS B 403 ? 1.1660 1.1253 1.7310 0.0527  0.1061  0.1082  404 LYS B CE  
5939  N  NZ  . LYS B 403 ? 1.1541 1.1152 1.6993 0.0555  0.1033  0.1035  404 LYS B NZ  
5940  N  N   . MET B 404 ? 0.9843 0.9414 1.5500 0.0529  0.0711  0.0745  405 MET B N   
5941  C  CA  . MET B 404 ? 0.9563 0.9099 1.5169 0.0596  0.0676  0.0757  405 MET B CA  
5942  C  C   . MET B 404 ? 0.9929 0.9457 1.5640 0.0577  0.0623  0.0676  405 MET B C   
5943  O  O   . MET B 404 ? 0.9965 0.9441 1.5727 0.0618  0.0620  0.0715  405 MET B O   
5944  C  CB  . MET B 404 ? 0.9292 0.8867 1.4726 0.0645  0.0633  0.0722  405 MET B CB  
5945  C  CG  . MET B 404 ? 0.9155 0.8764 1.4499 0.0634  0.0657  0.0731  405 MET B CG  
5946  S  SD  . MET B 404 ? 1.1452 1.1138 1.6686 0.0635  0.0586  0.0631  405 MET B SD  
5947  C  CE  . MET B 404 ? 0.6449 0.6149 1.1593 0.0634  0.0621  0.0661  405 MET B CE  
5948  N  N   . ALA B 405 ? 0.9352 0.8927 1.5086 0.0525  0.0581  0.0564  406 ALA B N   
5949  C  CA  . ALA B 405 ? 0.9437 0.9014 1.5205 0.0532  0.0523  0.0470  406 ALA B CA  
5950  C  C   . ALA B 405 ? 0.9738 0.9262 1.5681 0.0518  0.0513  0.0457  406 ALA B C   
5951  O  O   . ALA B 405 ? 0.9940 0.9432 1.6004 0.0495  0.0554  0.0527  406 ALA B O   
5952  C  CB  . ALA B 405 ? 0.8598 0.8236 1.4323 0.0496  0.0490  0.0363  406 ALA B CB  
5953  N  N   . LEU B 406 ? 1.0446 0.9965 1.6410 0.0538  0.0458  0.0365  407 LEU B N   
5954  C  CA  . LEU B 406 ? 1.0764 1.0231 1.6893 0.0532  0.0430  0.0325  407 LEU B CA  
5955  C  C   . LEU B 406 ? 1.1123 1.0611 1.7341 0.0480  0.0395  0.0225  407 LEU B C   
5956  O  O   . LEU B 406 ? 1.1136 1.0674 1.7293 0.0444  0.0405  0.0205  407 LEU B O   
5957  C  CB  . LEU B 406 ? 1.0874 1.0318 1.6975 0.0594  0.0385  0.0270  407 LEU B CB  
5958  C  CG  . LEU B 406 ? 1.1270 1.0634 1.7513 0.0620  0.0374  0.0301  407 LEU B CG  
5959  C  CD1 . LEU B 406 ? 1.1383 1.0706 1.7601 0.0657  0.0424  0.0446  407 LEU B CD1 
5960  C  CD2 . LEU B 406 ? 1.1266 1.0616 1.7504 0.0673  0.0316  0.0198  407 LEU B CD2 
5961  N  N   . ASP B 412 ? 1.5308 1.4464 2.1920 0.0771  0.0147  -0.0058 413 ASP B N   
5962  C  CA  . ASP B 412 ? 1.5380 1.4620 2.1821 0.0790  0.0141  -0.0141 413 ASP B CA  
5963  C  C   . ASP B 412 ? 1.2638 1.1930 1.8920 0.0849  0.0167  -0.0102 413 ASP B C   
5964  O  O   . ASP B 412 ? 1.3024 1.2398 1.9174 0.0869  0.0174  -0.0152 413 ASP B O   
5965  C  CB  . ASP B 412 ? 1.5597 1.4822 2.2072 0.0821  0.0075  -0.0302 413 ASP B CB  
5966  C  CG  . ASP B 412 ? 1.6006 1.5192 2.2487 0.0906  0.0038  -0.0371 413 ASP B CG  
5967  O  OD1 . ASP B 412 ? 1.6115 1.5327 2.2507 0.0957  0.0065  -0.0325 413 ASP B OD1 
5968  O  OD2 . ASP B 412 ? 1.6229 1.5354 2.2826 0.0924  -0.0024 -0.0474 413 ASP B OD2 
5969  N  N   . ARG B 413 ? 1.1806 1.1057 1.8110 0.0875  0.0186  -0.0001 414 ARG B N   
5970  C  CA  . ARG B 413 ? 1.0027 0.9336 1.6198 0.0927  0.0203  0.0043  414 ARG B CA  
5971  C  C   . ARG B 413 ? 0.8434 0.7752 1.4552 0.0896  0.0249  0.0174  414 ARG B C   
5972  O  O   . ARG B 413 ? 0.8508 0.7759 1.4709 0.0872  0.0273  0.0265  414 ARG B O   
5973  C  CB  . ARG B 413 ? 0.9782 0.9047 1.5990 0.1005  0.0176  0.0041  414 ARG B CB  
5974  C  CG  . ARG B 413 ? 0.9459 0.8746 1.5667 0.1057  0.0138  -0.0099 414 ARG B CG  
5975  C  CD  . ARG B 413 ? 0.8504 0.7912 1.4578 0.1064  0.0154  -0.0155 414 ARG B CD  
5976  N  NE  . ARG B 413 ? 0.8470 0.7910 1.4526 0.1120  0.0132  -0.0286 414 ARG B NE  
5977  C  CZ  . ARG B 413 ? 0.8301 0.7747 1.4344 0.1106  0.0120  -0.0380 414 ARG B CZ  
5978  N  NH1 . ARG B 413 ? 0.7986 0.7411 1.4051 0.1027  0.0124  -0.0358 414 ARG B NH1 
5979  N  NH2 . ARG B 413 ? 0.8368 0.7844 1.4375 0.1180  0.0105  -0.0495 414 ARG B NH2 
5980  N  N   . CYS B 414 ? 0.6922 0.6329 1.2907 0.0900  0.0262  0.0179  415 CYS B N   
5981  C  CA  . CYS B 414 ? 0.5352 0.4783 1.1264 0.0867  0.0301  0.0272  415 CYS B CA  
5982  C  C   . CYS B 414 ? 0.4943 0.4429 1.0744 0.0925  0.0293  0.0311  415 CYS B C   
5983  O  O   . CYS B 414 ? 0.4674 0.4198 1.0465 0.0979  0.0263  0.0259  415 CYS B O   
5984  C  CB  . CYS B 414 ? 0.4637 0.4123 1.0516 0.0799  0.0316  0.0224  415 CYS B CB  
5985  S  SG  . CYS B 414 ? 0.5306 0.4874 1.1133 0.0812  0.0287  0.0082  415 CYS B SG  
5986  N  N   . TRP B 415 ? 0.3659 0.3152 0.9385 0.0922  0.0318  0.0399  416 TRP B N   
5987  C  CA  . TRP B 415 ? 0.4198 0.3741 0.9827 0.0984  0.0298  0.0434  416 TRP B CA  
5988  C  C   . TRP B 415 ? 0.3964 0.3622 0.9541 0.0963  0.0283  0.0356  416 TRP B C   
5989  O  O   . TRP B 415 ? 0.4101 0.3790 0.9643 0.0904  0.0306  0.0345  416 TRP B O   
5990  C  CB  . TRP B 415 ? 0.3694 0.3198 0.9253 0.1003  0.0326  0.0551  416 TRP B CB  
5991  C  CG  . TRP B 415 ? 0.3605 0.3165 0.9054 0.1068  0.0294  0.0576  416 TRP B CG  
5992  C  CD1 . TRP B 415 ? 0.3753 0.3375 0.9120 0.1052  0.0294  0.0573  416 TRP B CD1 
5993  C  CD2 . TRP B 415 ? 0.4746 0.4309 1.0168 0.1164  0.0246  0.0601  416 TRP B CD2 
5994  N  NE1 . TRP B 415 ? 0.4392 0.4056 0.9689 0.1133  0.0243  0.0589  416 TRP B NE1 
5995  C  CE2 . TRP B 415 ? 0.4586 0.4218 0.9913 0.1204  0.0212  0.0607  416 TRP B CE2 
5996  C  CE3 . TRP B 415 ? 0.4344 0.3855 0.9818 0.1224  0.0223  0.0615  416 TRP B CE3 
5997  C  CZ2 . TRP B 415 ? 0.4542 0.4201 0.9829 0.1304  0.0150  0.0624  416 TRP B CZ2 
5998  C  CZ3 . TRP B 415 ? 0.4218 0.3754 0.9644 0.1322  0.0168  0.0639  416 TRP B CZ3 
5999  C  CH2 . TRP B 415 ? 0.4263 0.3876 0.9598 0.1362  0.0130  0.0642  416 TRP B CH2 
6000  N  N   . ASN B 416 ? 0.3419 0.3141 0.9003 0.1011  0.0249  0.0306  417 ASN B N   
6001  C  CA  . ASN B 416 ? 0.3301 0.3139 0.8862 0.0995  0.0242  0.0240  417 ASN B CA  
6002  C  C   . ASN B 416 ? 0.3606 0.3515 0.9120 0.1030  0.0211  0.0274  417 ASN B C   
6003  O  O   . ASN B 416 ? 0.3195 0.3205 0.8716 0.1015  0.0203  0.0228  417 ASN B O   
6004  C  CB  . ASN B 416 ? 0.4150 0.4034 0.9768 0.1025  0.0231  0.0157  417 ASN B CB  
6005  C  CG  . ASN B 416 ? 0.4286 0.4156 0.9944 0.1107  0.0197  0.0173  417 ASN B CG  
6006  O  OD1 . ASN B 416 ? 0.3514 0.3375 0.9146 0.1151  0.0170  0.0240  417 ASN B OD1 
6007  N  ND2 . ASN B 416 ? 0.4700 0.4565 1.0415 0.1139  0.0193  0.0109  417 ASN B ND2 
6008  N  N   . GLY B 417 ? 0.3617 0.3472 0.9090 0.1083  0.0192  0.0354  418 GLY B N   
6009  C  CA  . GLY B 417 ? 0.3402 0.3316 0.8830 0.1138  0.0145  0.0379  418 GLY B CA  
6010  C  C   . GLY B 417 ? 0.4940 0.4867 1.0398 0.1230  0.0093  0.0387  418 GLY B C   
6011  O  O   . GLY B 417 ? 0.4922 0.4873 1.0337 0.1300  0.0040  0.0422  418 GLY B O   
6012  N  N   . MET B 418 ? 0.5190 0.5101 1.0721 0.1238  0.0100  0.0351  419 MET B N   
6013  C  CA  . MET B 418 ? 0.5601 0.5512 1.1169 0.1328  0.0055  0.0360  419 MET B CA  
6014  C  C   . MET B 418 ? 0.6049 0.5821 1.1619 0.1360  0.0070  0.0422  419 MET B C   
6015  O  O   . MET B 418 ? 0.6001 0.5711 1.1521 0.1436  0.0045  0.0503  419 MET B O   
6016  C  CB  . MET B 418 ? 0.5842 0.5848 1.1504 0.1328  0.0049  0.0272  419 MET B CB  
6017  C  CG  . MET B 418 ? 0.6012 0.6166 1.1709 0.1320  0.0023  0.0229  419 MET B CG  
6018  S  SD  . MET B 418 ? 1.3252 1.3519 1.9072 0.1367  0.0009  0.0160  419 MET B SD  
6019  C  CE  . MET B 418 ? 0.5116 0.5547 1.0997 0.1338  -0.0017 0.0132  419 MET B CE  
6020  N  N   . ALA B 419 ? 0.5645 0.5367 1.1275 0.1309  0.0109  0.0381  420 ALA B N   
6021  C  CA  . ALA B 419 ? 0.5180 0.4767 1.0846 0.1323  0.0126  0.0433  420 ALA B CA  
6022  C  C   . ALA B 419 ? 0.5665 0.5203 1.1379 0.1233  0.0172  0.0398  420 ALA B C   
6023  O  O   . ALA B 419 ? 0.5277 0.4882 1.0974 0.1169  0.0190  0.0340  420 ALA B O   
6024  C  CB  . ALA B 419 ? 0.5552 0.5123 1.1291 0.1391  0.0094  0.0402  420 ALA B CB  
6025  N  N   . ARG B 420 ? 0.4898 0.4322 1.0683 0.1231  0.0187  0.0435  421 ARG B N   
6026  C  CA  . ARG B 420 ? 0.4805 0.4185 1.0670 0.1154  0.0213  0.0386  421 ARG B CA  
6027  C  C   . ARG B 420 ? 0.4698 0.4133 1.0603 0.1156  0.0190  0.0254  421 ARG B C   
6028  O  O   . ARG B 420 ? 0.5364 0.4809 1.1296 0.1223  0.0161  0.0220  421 ARG B O   
6029  C  CB  . ARG B 420 ? 0.5721 0.4971 1.1690 0.1154  0.0227  0.0453  421 ARG B CB  
6030  C  CG  . ARG B 420 ? 0.6228 0.5418 1.2155 0.1167  0.0265  0.0599  421 ARG B CG  
6031  C  CD  . ARG B 420 ? 0.6516 0.5587 1.2580 0.1147  0.0295  0.0668  421 ARG B CD  
6032  N  NE  . ARG B 420 ? 0.6717 0.5787 1.2895 0.1053  0.0312  0.0606  421 ARG B NE  
6033  C  CZ  . ARG B 420 ? 0.7172 0.6184 1.3457 0.1001  0.0359  0.0681  421 ARG B CZ  
6034  N  NH1 . ARG B 420 ? 0.7292 0.6238 1.3573 0.1036  0.0407  0.0831  421 ARG B NH1 
6035  N  NH2 . ARG B 420 ? 0.7070 0.6095 1.3471 0.0920  0.0360  0.0609  421 ARG B NH2 
6036  N  N   . GLY B 421 ? 0.5288 0.4761 1.1190 0.1093  0.0205  0.0180  422 GLY B N   
6037  C  CA  . GLY B 421 ? 0.5626 0.5161 1.1533 0.1111  0.0191  0.0060  422 GLY B CA  
6038  C  C   . GLY B 421 ? 0.5278 0.4888 1.1130 0.1058  0.0212  0.0000  422 GLY B C   
6039  O  O   . GLY B 421 ? 0.4507 0.4097 1.0348 0.0991  0.0231  0.0029  422 GLY B O   
6040  N  N   . ARG B 422 ? 0.5187 0.4886 1.1008 0.1095  0.0212  -0.0080 423 ARG B N   
6041  C  CA  . ARG B 422 ? 0.4878 0.4651 1.0643 0.1064  0.0235  -0.0141 423 ARG B CA  
6042  C  C   . ARG B 422 ? 0.4603 0.4481 1.0304 0.1041  0.0258  -0.0097 423 ARG B C   
6043  O  O   . ARG B 422 ? 0.3724 0.3655 0.9431 0.1078  0.0248  -0.0062 423 ARG B O   
6044  C  CB  . ARG B 422 ? 0.4797 0.4611 1.0565 0.1131  0.0233  -0.0249 423 ARG B CB  
6045  C  CG  . ARG B 422 ? 0.5013 0.4894 1.0716 0.1122  0.0259  -0.0316 423 ARG B CG  
6046  C  CD  . ARG B 422 ? 0.5049 0.4971 1.0742 0.1215  0.0263  -0.0416 423 ARG B CD  
6047  N  NE  . ARG B 422 ? 0.5148 0.5146 1.0865 0.1279  0.0274  -0.0402 423 ARG B NE  
6048  C  CZ  . ARG B 422 ? 0.4948 0.5014 1.0659 0.1370  0.0292  -0.0472 423 ARG B CZ  
6049  N  NH1 . ARG B 422 ? 0.4581 0.4644 1.0244 0.1418  0.0301  -0.0565 423 ARG B NH1 
6050  N  NH2 . ARG B 422 ? 0.4995 0.5137 1.0748 0.1422  0.0301  -0.0451 423 ARG B NH2 
6051  N  N   . TYR B 423 ? 0.4429 0.4336 1.0081 0.0981  0.0281  -0.0100 424 TYR B N   
6052  C  CA  . TYR B 423 ? 0.3997 0.4001 0.9603 0.0956  0.0300  -0.0067 424 TYR B CA  
6053  C  C   . TYR B 423 ? 0.3124 0.3229 0.8710 0.0976  0.0330  -0.0133 424 TYR B C   
6054  O  O   . TYR B 423 ? 0.4078 0.4178 0.9628 0.0955  0.0348  -0.0176 424 TYR B O   
6055  C  CB  . TYR B 423 ? 0.3536 0.3508 0.9103 0.0881  0.0312  -0.0015 424 TYR B CB  
6056  C  CG  . TYR B 423 ? 0.4255 0.4311 0.9782 0.0854  0.0323  0.0017  424 TYR B CG  
6057  C  CD1 . TYR B 423 ? 0.4149 0.4231 0.9679 0.0875  0.0299  0.0072  424 TYR B CD1 
6058  C  CD2 . TYR B 423 ? 0.3671 0.3780 0.9165 0.0813  0.0351  -0.0010 424 TYR B CD2 
6059  C  CE1 . TYR B 423 ? 0.3509 0.3665 0.9022 0.0851  0.0297  0.0090  424 TYR B CE1 
6060  C  CE2 . TYR B 423 ? 0.2851 0.3030 0.8328 0.0784  0.0358  0.0019  424 TYR B CE2 
6061  C  CZ  . TYR B 423 ? 0.3182 0.3384 0.8676 0.0801  0.0328  0.0064  424 TYR B CZ  
6062  O  OH  . TYR B 423 ? 0.2717 0.2986 0.8213 0.0775  0.0323  0.0081  424 TYR B OH  
6063  N  N   . LEU B 424 ? 0.3138 0.3338 0.8752 0.1022  0.0335  -0.0137 425 LEU B N   
6064  C  CA  . LEU B 424 ? 0.4292 0.4606 0.9902 0.1054  0.0377  -0.0184 425 LEU B CA  
6065  C  C   . LEU B 424 ? 0.3963 0.4349 0.9541 0.0999  0.0414  -0.0161 425 LEU B C   
6066  O  O   . LEU B 424 ? 0.3002 0.3418 0.8538 0.1009  0.0451  -0.0201 425 LEU B O   
6067  C  CB  . LEU B 424 ? 0.3178 0.3584 0.8856 0.1117  0.0377  -0.0184 425 LEU B CB  
6068  C  CG  . LEU B 424 ? 0.5153 0.5508 1.0869 0.1191  0.0349  -0.0218 425 LEU B CG  
6069  C  CD1 . LEU B 424 ? 0.5315 0.5787 1.1103 0.1256  0.0359  -0.0226 425 LEU B CD1 
6070  C  CD2 . LEU B 424 ? 0.5508 0.5802 1.1185 0.1227  0.0359  -0.0295 425 LEU B CD2 
6071  N  N   . PRO B 425 ? 0.2926 0.3337 0.8522 0.0950  0.0399  -0.0101 426 PRO B N   
6072  C  CA  . PRO B 425 ? 0.3970 0.4461 0.9563 0.0904  0.0434  -0.0082 426 PRO B CA  
6073  C  C   . PRO B 425 ? 0.3751 0.4199 0.9270 0.0861  0.0460  -0.0093 426 PRO B C   
6074  O  O   . PRO B 425 ? 0.2774 0.3119 0.8252 0.0832  0.0437  -0.0091 426 PRO B O   
6075  C  CB  . PRO B 425 ? 0.2777 0.3268 0.8400 0.0864  0.0393  -0.0026 426 PRO B CB  
6076  C  CG  . PRO B 425 ? 0.4165 0.4625 0.9821 0.0914  0.0346  -0.0018 426 PRO B CG  
6077  C  CD  . PRO B 425 ? 0.2933 0.3301 0.8552 0.0942  0.0350  -0.0049 426 PRO B CD  
6078  N  N   . GLU B 426 ? 0.4171 0.4701 0.9682 0.0859  0.0510  -0.0098 427 GLU B N   
6079  C  CA  . GLU B 426 ? 0.4228 0.4731 0.9670 0.0830  0.0535  -0.0109 427 GLU B CA  
6080  C  C   . GLU B 426 ? 0.2606 0.3061 0.8033 0.0746  0.0515  -0.0059 427 GLU B C   
6081  O  O   . GLU B 426 ? 0.2568 0.3040 0.8039 0.0717  0.0493  -0.0018 427 GLU B O   
6082  C  CB  . GLU B 426 ? 0.5067 0.5683 1.0507 0.0866  0.0602  -0.0116 427 GLU B CB  
6083  C  CG  . GLU B 426 ? 0.5647 0.6245 1.1002 0.0906  0.0626  -0.0166 427 GLU B CG  
6084  C  CD  . GLU B 426 ? 0.6178 0.6900 1.1526 0.0987  0.0700  -0.0180 427 GLU B CD  
6085  O  OE1 . GLU B 426 ? 0.6255 0.7030 1.1580 0.0975  0.0749  -0.0150 427 GLU B OE1 
6086  O  OE2 . GLU B 426 ? 0.6408 0.7179 1.1774 0.1068  0.0715  -0.0217 427 GLU B OE2 
6087  N  N   . VAL B 427 ? 0.3193 0.3588 0.8559 0.0714  0.0518  -0.0069 428 VAL B N   
6088  C  CA  . VAL B 427 ? 0.3374 0.3723 0.8720 0.0641  0.0505  -0.0026 428 VAL B CA  
6089  C  C   . VAL B 427 ? 0.2431 0.2852 0.7789 0.0612  0.0540  0.0004  428 VAL B C   
6090  O  O   . VAL B 427 ? 0.2449 0.2930 0.7795 0.0640  0.0585  -0.0010 428 VAL B O   
6091  C  CB  . VAL B 427 ? 0.4183 0.4447 0.9480 0.0615  0.0495  -0.0046 428 VAL B CB  
6092  C  CG1 . VAL B 427 ? 0.4340 0.4561 0.9622 0.0546  0.0485  0.0002  428 VAL B CG1 
6093  C  CG2 . VAL B 427 ? 0.4201 0.4393 0.9515 0.0642  0.0463  -0.0075 428 VAL B CG2 
6094  N  N   . MET B 428 ? 0.2674 0.3091 0.8060 0.0564  0.0518  0.0045  429 MET B N   
6095  C  CA  . MET B 428 ? 0.3110 0.3580 0.8531 0.0529  0.0542  0.0076  429 MET B CA  
6096  C  C   . MET B 428 ? 0.3206 0.3639 0.8567 0.0494  0.0564  0.0082  429 MET B C   
6097  O  O   . MET B 428 ? 0.2814 0.3173 0.8115 0.0483  0.0549  0.0066  429 MET B O   
6098  C  CB  . MET B 428 ? 0.2294 0.2764 0.7772 0.0498  0.0496  0.0102  429 MET B CB  
6099  C  CG  . MET B 428 ? 0.3207 0.3724 0.8759 0.0538  0.0463  0.0097  429 MET B CG  
6100  S  SD  . MET B 428 ? 0.4003 0.4650 0.9670 0.0565  0.0507  0.0098  429 MET B SD  
6101  C  CE  . MET B 428 ? 0.4708 0.5367 1.0325 0.0638  0.0542  0.0060  429 MET B CE  
6102  N  N   . GLY B 429 ? 0.3627 0.4112 0.9018 0.0477  0.0601  0.0109  430 GLY B N   
6103  C  CA  . GLY B 429 ? 0.2221 0.2674 0.7566 0.0443  0.0619  0.0123  430 GLY B CA  
6104  C  C   . GLY B 429 ? 0.2163 0.2549 0.7508 0.0384  0.0577  0.0143  430 GLY B C   
6105  O  O   . GLY B 429 ? 0.2159 0.2539 0.7544 0.0376  0.0537  0.0146  430 GLY B O   
6106  N  N   . ASP B 430 ? 0.2128 0.2470 0.7428 0.0353  0.0584  0.0152  431 ASP B N   
6107  C  CA  . ASP B 430 ? 0.2081 0.2366 0.7376 0.0305  0.0551  0.0167  431 ASP B CA  
6108  C  C   . ASP B 430 ? 0.2237 0.2548 0.7610 0.0277  0.0547  0.0194  431 ASP B C   
6109  O  O   . ASP B 430 ? 0.2079 0.2440 0.7503 0.0280  0.0586  0.0216  431 ASP B O   
6110  C  CB  . ASP B 430 ? 0.2892 0.3123 0.8122 0.0283  0.0559  0.0164  431 ASP B CB  
6111  C  CG  . ASP B 430 ? 0.4117 0.4312 0.9300 0.0302  0.0550  0.0133  431 ASP B CG  
6112  O  OD1 . ASP B 430 ? 0.4989 0.5142 1.0167 0.0293  0.0525  0.0135  431 ASP B OD1 
6113  O  OD2 . ASP B 430 ? 0.4057 0.4268 0.9218 0.0333  0.0567  0.0106  431 ASP B OD2 
6114  N  N   . GLY B 431 ? 0.2046 0.2326 0.7440 0.0256  0.0501  0.0192  432 GLY B N   
6115  C  CA  . GLY B 431 ? 0.2141 0.2432 0.7624 0.0229  0.0480  0.0203  432 GLY B CA  
6116  C  C   . GLY B 431 ? 0.2778 0.3117 0.8362 0.0244  0.0433  0.0189  432 GLY B C   
6117  O  O   . GLY B 431 ? 0.2611 0.2985 0.8198 0.0278  0.0427  0.0179  432 GLY B O   
6118  N  N   . LEU B 432 ? 0.2067 0.2408 0.7747 0.0221  0.0391  0.0183  433 LEU B N   
6119  C  CA  . LEU B 432 ? 0.3267 0.3655 0.9063 0.0237  0.0325  0.0157  433 LEU B CA  
6120  C  C   . LEU B 432 ? 0.3103 0.3564 0.9011 0.0245  0.0350  0.0172  433 LEU B C   
6121  O  O   . LEU B 432 ? 0.3340 0.3848 0.9284 0.0278  0.0317  0.0153  433 LEU B O   
6122  C  CB  . LEU B 432 ? 0.2106 0.2479 0.8001 0.0212  0.0267  0.0135  433 LEU B CB  
6123  C  CG  . LEU B 432 ? 0.3022 0.3441 0.9044 0.0236  0.0172  0.0090  433 LEU B CG  
6124  C  CD1 . LEU B 432 ? 0.2178 0.2596 0.8090 0.0296  0.0123  0.0064  433 LEU B CD1 
6125  C  CD2 . LEU B 432 ? 0.2170 0.2572 0.8319 0.0209  0.0110  0.0058  433 LEU B CD2 
6126  N  N   . ALA B 433 ? 0.2848 0.3323 0.8810 0.0220  0.0411  0.0211  434 ALA B N   
6127  C  CA  . ALA B 433 ? 0.2985 0.3542 0.9065 0.0230  0.0451  0.0237  434 ALA B CA  
6128  C  C   . ALA B 433 ? 0.2193 0.2797 0.8200 0.0277  0.0487  0.0233  434 ALA B C   
6129  O  O   . ALA B 433 ? 0.2233 0.2910 0.8337 0.0299  0.0484  0.0230  434 ALA B O   
6130  C  CB  . ALA B 433 ? 0.2191 0.2757 0.8316 0.0208  0.0528  0.0296  434 ALA B CB  
6131  N  N   . ASN B 434 ? 0.2169 0.2730 0.8017 0.0293  0.0517  0.0227  435 ASN B N   
6132  C  CA  . ASN B 434 ? 0.2194 0.2787 0.7973 0.0342  0.0548  0.0214  435 ASN B CA  
6133  C  C   . ASN B 434 ? 0.2213 0.2809 0.7997 0.0373  0.0487  0.0179  435 ASN B C   
6134  O  O   . ASN B 434 ? 0.2247 0.2873 0.8005 0.0417  0.0506  0.0166  435 ASN B O   
6135  C  CB  . ASN B 434 ? 0.2174 0.2710 0.7803 0.0351  0.0579  0.0206  435 ASN B CB  
6136  C  CG  . ASN B 434 ? 0.3716 0.4293 0.9329 0.0362  0.0657  0.0236  435 ASN B CG  
6137  O  OD1 . ASN B 434 ? 0.2232 0.2894 0.7933 0.0379  0.0706  0.0267  435 ASN B OD1 
6138  N  ND2 . ASN B 434 ? 0.3606 0.4132 0.9116 0.0359  0.0671  0.0231  435 ASN B ND2 
6139  N  N   . GLN B 435 ? 0.2203 0.2772 0.8022 0.0359  0.0413  0.0164  436 GLN B N   
6140  C  CA  . GLN B 435 ? 0.2235 0.2808 0.8049 0.0400  0.0352  0.0138  436 GLN B CA  
6141  C  C   . GLN B 435 ? 0.3059 0.3713 0.9033 0.0415  0.0305  0.0126  436 GLN B C   
6142  O  O   . GLN B 435 ? 0.3461 0.4123 0.9449 0.0453  0.0235  0.0104  436 GLN B O   
6143  C  CB  . GLN B 435 ? 0.2977 0.3481 0.8713 0.0401  0.0297  0.0128  436 GLN B CB  
6144  C  CG  . GLN B 435 ? 0.3109 0.3536 0.8720 0.0373  0.0339  0.0143  436 GLN B CG  
6145  C  CD  . GLN B 435 ? 0.2182 0.2587 0.7709 0.0387  0.0394  0.0147  436 GLN B CD  
6146  O  OE1 . GLN B 435 ? 0.2224 0.2645 0.7749 0.0428  0.0391  0.0138  436 GLN B OE1 
6147  N  NE2 . GLN B 435 ? 0.2148 0.2513 0.7610 0.0358  0.0438  0.0155  436 GLN B NE2 
6148  N  N   . ILE B 436 ? 0.2284 0.2999 0.8384 0.0390  0.0342  0.0144  437 ILE B N   
6149  C  CA  . ILE B 436 ? 0.2549 0.3346 0.8833 0.0396  0.0297  0.0133  437 ILE B CA  
6150  C  C   . ILE B 436 ? 0.2375 0.3229 0.8666 0.0454  0.0299  0.0122  437 ILE B C   
6151  O  O   . ILE B 436 ? 0.2417 0.3313 0.8804 0.0481  0.0224  0.0096  437 ILE B O   
6152  C  CB  . ILE B 436 ? 0.2439 0.3288 0.8873 0.0356  0.0353  0.0171  437 ILE B CB  
6153  C  CG1 . ILE B 436 ? 0.2398 0.3332 0.9053 0.0358  0.0303  0.0159  437 ILE B CG1 
6154  C  CG2 . ILE B 436 ? 0.2347 0.3230 0.8717 0.0371  0.0470  0.0214  437 ILE B CG2 
6155  C  CD1 . ILE B 436 ? 0.3584 0.4551 1.0420 0.0310  0.0339  0.0198  437 ILE B CD1 
6156  N  N   . ASN B 437 ? 0.2377 0.3233 0.8570 0.0478  0.0378  0.0137  438 ASN B N   
6157  C  CA  . ASN B 437 ? 0.3474 0.4372 0.9661 0.0538  0.0385  0.0122  438 ASN B CA  
6158  C  C   . ASN B 437 ? 0.3864 0.4679 0.9900 0.0574  0.0354  0.0102  438 ASN B C   
6159  O  O   . ASN B 437 ? 0.3963 0.4792 0.9979 0.0627  0.0362  0.0089  438 ASN B O   
6160  C  CB  . ASN B 437 ? 0.3788 0.4752 0.9978 0.0560  0.0488  0.0141  438 ASN B CB  
6161  C  CG  . ASN B 437 ? 0.3803 0.4871 1.0175 0.0541  0.0527  0.0174  438 ASN B CG  
6162  O  OD1 . ASN B 437 ? 0.2500 0.3613 0.9028 0.0530  0.0468  0.0167  438 ASN B OD1 
6163  N  ND2 . ASN B 437 ? 0.3971 0.5082 1.0331 0.0542  0.0627  0.0212  438 ASN B ND2 
6164  N  N   . ASN B 438 ? 0.4076 0.4803 1.0014 0.0549  0.0324  0.0103  439 ASN B N   
6165  C  CA  . ASN B 438 ? 0.2907 0.3549 0.8714 0.0578  0.0304  0.0099  439 ASN B CA  
6166  C  C   . ASN B 438 ? 0.2477 0.3134 0.8312 0.0641  0.0245  0.0089  439 ASN B C   
6167  O  O   . ASN B 438 ? 0.2503 0.3194 0.8412 0.0656  0.0174  0.0082  439 ASN B O   
6168  C  CB  . ASN B 438 ? 0.2367 0.2934 0.8097 0.0548  0.0276  0.0109  439 ASN B CB  
6169  C  CG  . ASN B 438 ? 0.3237 0.3714 0.8839 0.0573  0.0275  0.0120  439 ASN B CG  
6170  O  OD1 . ASN B 438 ? 0.3642 0.4099 0.9225 0.0621  0.0226  0.0127  439 ASN B OD1 
6171  N  ND2 . ASN B 438 ? 0.2355 0.2778 0.7879 0.0544  0.0329  0.0125  439 ASN B ND2 
6172  N  N   . PRO B 439 ? 0.3262 0.3890 0.9042 0.0683  0.0268  0.0085  440 PRO B N   
6173  C  CA  . PRO B 439 ? 0.3504 0.4143 0.9312 0.0749  0.0220  0.0081  440 PRO B CA  
6174  C  C   . PRO B 439 ? 0.3963 0.4537 0.9707 0.0783  0.0152  0.0102  440 PRO B C   
6175  O  O   . PRO B 439 ? 0.4459 0.5072 1.0259 0.0835  0.0086  0.0099  440 PRO B O   
6176  C  CB  . PRO B 439 ? 0.2641 0.3241 0.8394 0.0778  0.0268  0.0070  440 PRO B CB  
6177  C  CG  . PRO B 439 ? 0.3452 0.3989 0.9115 0.0729  0.0320  0.0071  440 PRO B CG  
6178  C  CD  . PRO B 439 ? 0.2510 0.3096 0.8210 0.0674  0.0336  0.0079  440 PRO B CD  
6179  N  N   . GLU B 440 ? 0.2933 0.3415 0.8565 0.0764  0.0170  0.0125  441 GLU B N   
6180  C  CA  . GLU B 440 ? 0.3237 0.3652 0.8790 0.0814  0.0125  0.0159  441 GLU B CA  
6181  C  C   . GLU B 440 ? 0.2694 0.3123 0.8238 0.0819  0.0069  0.0161  441 GLU B C   
6182  O  O   . GLU B 440 ? 0.2783 0.3178 0.8266 0.0889  0.0018  0.0185  441 GLU B O   
6183  C  CB  . GLU B 440 ? 0.3057 0.3365 0.8507 0.0799  0.0177  0.0191  441 GLU B CB  
6184  C  CG  . GLU B 440 ? 0.2697 0.2985 0.8161 0.0782  0.0228  0.0171  441 GLU B CG  
6185  C  CD  . GLU B 440 ? 0.2778 0.3097 0.8301 0.0843  0.0206  0.0157  441 GLU B CD  
6186  O  OE1 . GLU B 440 ? 0.2860 0.3177 0.8386 0.0905  0.0154  0.0181  441 GLU B OE1 
6187  O  OE2 . GLU B 440 ? 0.2976 0.3321 0.8536 0.0838  0.0240  0.0120  441 GLU B OE2 
6188  N  N   . VAL B 441 ? 0.3424 0.3900 0.9026 0.0756  0.0077  0.0135  442 VAL B N   
6189  C  CA  . VAL B 441 ? 0.2607 0.3090 0.8210 0.0757  0.0021  0.0124  442 VAL B CA  
6190  C  C   . VAL B 441 ? 0.2627 0.3204 0.8388 0.0715  -0.0011 0.0083  442 VAL B C   
6191  O  O   . VAL B 441 ? 0.2494 0.3097 0.8313 0.0650  0.0051  0.0081  442 VAL B O   
6192  C  CB  . VAL B 441 ? 0.2548 0.2961 0.8054 0.0710  0.0070  0.0143  442 VAL B CB  
6193  C  CG1 . VAL B 441 ? 0.2607 0.3014 0.8088 0.0741  0.0004  0.0130  442 VAL B CG1 
6194  C  CG2 . VAL B 441 ? 0.3057 0.3380 0.8443 0.0725  0.0126  0.0188  442 VAL B CG2 
6195  N  N   . GLU B 442 ? 0.3152 0.3775 0.8987 0.0757  -0.0110 0.0053  443 GLU B N   
6196  C  CA  . GLU B 442 ? 0.4013 0.4716 1.0025 0.0709  -0.0147 0.0013  443 GLU B CA  
6197  C  C   . GLU B 442 ? 0.3574 0.4242 0.9576 0.0662  -0.0155 -0.0001 443 GLU B C   
6198  O  O   . GLU B 442 ? 0.3274 0.3907 0.9202 0.0711  -0.0221 -0.0017 443 GLU B O   
6199  C  CB  . GLU B 442 ? 0.5074 0.5849 1.1206 0.0769  -0.0264 -0.0028 443 GLU B CB  
6200  C  CG  . GLU B 442 ? 0.6625 0.7480 1.2890 0.0768  -0.0246 -0.0028 443 GLU B CG  
6201  C  CD  . GLU B 442 ? 0.7716 0.8604 1.4074 0.0681  -0.0144 -0.0012 443 GLU B CD  
6202  O  OE1 . GLU B 442 ? 0.7989 0.8907 1.4477 0.0623  -0.0156 -0.0028 443 GLU B OE1 
6203  O  OE2 . GLU B 442 ? 0.7919 0.8799 1.4218 0.0679  -0.0054 0.0017  443 GLU B OE2 
6204  N  N   . VAL B 443 ? 0.3100 0.3777 0.9169 0.0578  -0.0085 0.0008  444 VAL B N   
6205  C  CA  . VAL B 443 ? 0.3417 0.4057 0.9486 0.0526  -0.0080 0.0001  444 VAL B CA  
6206  C  C   . VAL B 443 ? 0.2409 0.3103 0.8686 0.0469  -0.0101 -0.0021 444 VAL B C   
6207  O  O   . VAL B 443 ? 0.3130 0.3864 0.9494 0.0432  -0.0035 0.0006  444 VAL B O   
6208  C  CB  . VAL B 443 ? 0.3279 0.3853 0.9220 0.0480  0.0030  0.0044  444 VAL B CB  
6209  C  CG1 . VAL B 443 ? 0.3068 0.3604 0.9016 0.0430  0.0033  0.0038  444 VAL B CG1 
6210  C  CG2 . VAL B 443 ? 0.2743 0.3255 0.8506 0.0528  0.0054  0.0069  444 VAL B CG2 
6211  N  N   . ASP B 444 ? 0.4173 0.4864 1.0531 0.0468  -0.0193 -0.0069 445 ASP B N   
6212  C  CA  . ASP B 444 ? 0.2441 0.3161 0.9012 0.0405  -0.0213 -0.0087 445 ASP B CA  
6213  C  C   . ASP B 444 ? 0.2371 0.3027 0.8895 0.0341  -0.0130 -0.0051 445 ASP B C   
6214  O  O   . ASP B 444 ? 0.2357 0.2956 0.8780 0.0347  -0.0150 -0.0068 445 ASP B O   
6215  C  CB  . ASP B 444 ? 0.5188 0.5929 1.1886 0.0436  -0.0366 -0.0169 445 ASP B CB  
6216  C  CG  . ASP B 444 ? 0.5565 0.6325 1.2518 0.0368  -0.0396 -0.0191 445 ASP B CG  
6217  O  OD1 . ASP B 444 ? 0.5513 0.6287 1.2552 0.0312  -0.0293 -0.0131 445 ASP B OD1 
6218  O  OD2 . ASP B 444 ? 0.5554 0.6311 1.2621 0.0381  -0.0524 -0.0269 445 ASP B OD2 
6219  N  N   . ILE B 445 ? 0.2342 0.3009 0.8934 0.0289  -0.0034 0.0001  446 ILE B N   
6220  C  CA  . ILE B 445 ? 0.2385 0.2990 0.8905 0.0243  0.0054  0.0047  446 ILE B CA  
6221  C  C   . ILE B 445 ? 0.2308 0.2883 0.8989 0.0196  0.0019  0.0034  446 ILE B C   
6222  O  O   . ILE B 445 ? 0.3077 0.3594 0.9713 0.0162  0.0075  0.0068  446 ILE B O   
6223  C  CB  . ILE B 445 ? 0.2269 0.2898 0.8757 0.0231  0.0177  0.0114  446 ILE B CB  
6224  C  CG1 . ILE B 445 ? 0.3289 0.3984 0.9994 0.0209  0.0196  0.0140  446 ILE B CG1 
6225  C  CG2 . ILE B 445 ? 0.3566 0.4220 0.9922 0.0280  0.0202  0.0116  446 ILE B CG2 
6226  C  CD1 . ILE B 445 ? 0.2807 0.3543 0.9481 0.0212  0.0322  0.0211  446 ILE B CD1 
6227  N  N   . THR B 446 ? 0.2372 0.2986 0.9251 0.0198  -0.0082 -0.0018 447 THR B N   
6228  C  CA  . THR B 446 ? 0.2412 0.2990 0.9475 0.0158  -0.0139 -0.0045 447 THR B CA  
6229  C  C   . THR B 446 ? 0.4000 0.4541 1.1024 0.0184  -0.0258 -0.0132 447 THR B C   
6230  O  O   . THR B 446 ? 0.5254 0.5763 1.2436 0.0162  -0.0336 -0.0182 447 THR B O   
6231  C  CB  . THR B 446 ? 0.2494 0.3128 0.9830 0.0144  -0.0192 -0.0062 447 THR B CB  
6232  O  OG1 . THR B 446 ? 0.2543 0.3235 0.9918 0.0193  -0.0313 -0.0140 447 THR B OG1 
6233  C  CG2 . THR B 446 ? 0.2492 0.3178 0.9871 0.0129  -0.0065 0.0029  447 THR B CG2 
6234  N  N   . LYS B 447 ? 0.3553 0.4098 1.0371 0.0241  -0.0273 -0.0151 448 LYS B N   
6235  C  CA  . LYS B 447 ? 0.3650 0.4164 1.0387 0.0290  -0.0371 -0.0223 448 LYS B CA  
6236  C  C   . LYS B 447 ? 0.3501 0.3959 1.0001 0.0300  -0.0287 -0.0182 448 LYS B C   
6237  O  O   . LYS B 447 ? 0.3799 0.4254 1.0113 0.0369  -0.0288 -0.0180 448 LYS B O   
6238  C  CB  . LYS B 447 ? 0.3704 0.4268 1.0406 0.0382  -0.0487 -0.0286 448 LYS B CB  
6239  C  CG  . LYS B 447 ? 0.4402 0.5012 1.1347 0.0387  -0.0626 -0.0366 448 LYS B CG  
6240  C  CD  . LYS B 447 ? 0.4712 0.5358 1.1580 0.0499  -0.0757 -0.0434 448 LYS B CD  
6241  C  CE  . LYS B 447 ? 0.5397 0.6090 1.2514 0.0505  -0.0912 -0.0527 448 LYS B CE  
6242  N  NZ  . LYS B 447 ? 0.5842 0.6555 1.2856 0.0634  -0.1067 -0.0609 448 LYS B NZ  
6243  N  N   . PRO B 448 ? 0.3133 0.3538 0.9641 0.0237  -0.0214 -0.0144 449 PRO B N   
6244  C  CA  . PRO B 448 ? 0.3339 0.3691 0.9640 0.0240  -0.0136 -0.0106 449 PRO B CA  
6245  C  C   . PRO B 448 ? 0.3307 0.3630 0.9518 0.0299  -0.0210 -0.0168 449 PRO B C   
6246  O  O   . PRO B 448 ? 0.2382 0.2705 0.8720 0.0314  -0.0318 -0.0244 449 PRO B O   
6247  C  CB  . PRO B 448 ? 0.2219 0.2525 0.8589 0.0164  -0.0057 -0.0055 449 PRO B CB  
6248  C  CG  . PRO B 448 ? 0.2277 0.2586 0.8895 0.0135  -0.0131 -0.0093 449 PRO B CG  
6249  C  CD  . PRO B 448 ? 0.3434 0.3815 1.0147 0.0168  -0.0203 -0.0131 449 PRO B CD  
6250  N  N   . ASP B 449 ? 0.2300 0.2591 0.8291 0.0341  -0.0154 -0.0138 450 ASP B N   
6251  C  CA  . ASP B 449 ? 0.3571 0.3817 0.9433 0.0412  -0.0197 -0.0180 450 ASP B CA  
6252  C  C   . ASP B 449 ? 0.3256 0.3463 0.9193 0.0362  -0.0199 -0.0203 450 ASP B C   
6253  O  O   . ASP B 449 ? 0.3927 0.4116 0.9873 0.0287  -0.0108 -0.0146 450 ASP B O   
6254  C  CB  . ASP B 449 ? 0.3892 0.4100 0.9520 0.0456  -0.0110 -0.0120 450 ASP B CB  
6255  C  CG  . ASP B 449 ? 0.4186 0.4336 0.9660 0.0543  -0.0131 -0.0148 450 ASP B CG  
6256  O  OD1 . ASP B 449 ? 0.2770 0.2910 0.8149 0.0654  -0.0192 -0.0175 450 ASP B OD1 
6257  O  OD2 . ASP B 449 ? 0.5101 0.5212 1.0539 0.0511  -0.0085 -0.0140 450 ASP B OD2 
6258  N  N   . MET B 450 ? 0.2447 0.2636 0.8433 0.0414  -0.0310 -0.0292 451 MET B N   
6259  C  CA  . MET B 450 ? 0.4190 0.4341 1.0282 0.0370  -0.0333 -0.0329 451 MET B CA  
6260  C  C   . MET B 450 ? 0.3776 0.3871 0.9685 0.0375  -0.0244 -0.0290 451 MET B C   
6261  O  O   . MET B 450 ? 0.3885 0.3962 0.9868 0.0299  -0.0195 -0.0261 451 MET B O   
6262  C  CB  . MET B 450 ? 0.3596 0.3731 0.9772 0.0439  -0.0492 -0.0453 451 MET B CB  
6263  C  CG  . MET B 450 ? 0.4129 0.4319 1.0551 0.0415  -0.0598 -0.0504 451 MET B CG  
6264  N  N   . THR B 451 ? 0.2998 0.3064 0.8677 0.0469  -0.0224 -0.0285 452 THR B N   
6265  C  CA  . THR B 451 ? 0.3603 0.3617 0.9106 0.0483  -0.0134 -0.0243 452 THR B CA  
6266  C  C   . THR B 451 ? 0.2326 0.2358 0.7853 0.0376  -0.0020 -0.0154 452 THR B C   
6267  O  O   . THR B 451 ? 0.4387 0.4394 0.9912 0.0333  0.0024  -0.0138 452 THR B O   
6268  C  CB  . THR B 451 ? 0.3475 0.3460 0.8750 0.0594  -0.0101 -0.0219 452 THR B CB  
6269  O  OG1 . THR B 451 ? 0.3677 0.3633 0.8896 0.0718  -0.0210 -0.0305 452 THR B OG1 
6270  C  CG2 . THR B 451 ? 0.2553 0.2492 0.7680 0.0598  0.0002  -0.0166 452 THR B CG2 
6271  N  N   . ILE B 452 ? 0.2577 0.2649 0.8123 0.0342  0.0019  -0.0104 453 ILE B N   
6272  C  CA  . ILE B 452 ? 0.2629 0.2706 0.8167 0.0263  0.0117  -0.0029 453 ILE B CA  
6273  C  C   . ILE B 452 ? 0.2739 0.2819 0.8446 0.0180  0.0122  -0.0020 453 ILE B C   
6274  O  O   . ILE B 452 ? 0.2407 0.2465 0.8088 0.0132  0.0189  0.0026  453 ILE B O   
6275  C  CB  . ILE B 452 ? 0.2128 0.2236 0.7635 0.0265  0.0148  0.0010  453 ILE B CB  
6276  C  CG1 . ILE B 452 ? 0.2191 0.2282 0.7531 0.0347  0.0158  0.0020  453 ILE B CG1 
6277  C  CG2 . ILE B 452 ? 0.2378 0.2480 0.7876 0.0197  0.0232  0.0070  453 ILE B CG2 
6278  C  CD1 . ILE B 452 ? 0.2325 0.2431 0.7617 0.0345  0.0204  0.0067  453 ILE B CD1 
6279  N  N   . ARG B 453 ? 0.2130 0.2228 0.8017 0.0166  0.0050  -0.0060 454 ARG B N   
6280  C  CA  . ARG B 453 ? 0.3054 0.3133 0.9123 0.0095  0.0057  -0.0042 454 ARG B CA  
6281  C  C   . ARG B 453 ? 0.2109 0.2155 0.8183 0.0082  0.0054  -0.0059 454 ARG B C   
6282  O  O   . ARG B 453 ? 0.2674 0.2691 0.8779 0.0029  0.0115  -0.0004 454 ARG B O   
6283  C  CB  . ARG B 453 ? 0.2974 0.3070 0.9260 0.0088  -0.0030 -0.0089 454 ARG B CB  
6284  N  N   . GLN B 454 ? 0.2180 0.2219 0.8204 0.0146  -0.0020 -0.0136 455 GLN B N   
6285  C  CA  . GLN B 454 ? 0.2970 0.2971 0.8961 0.0154  -0.0027 -0.0164 455 GLN B CA  
6286  C  C   . GLN B 454 ? 0.3232 0.3222 0.9062 0.0137  0.0079  -0.0094 455 GLN B C   
6287  O  O   . GLN B 454 ? 0.3367 0.3349 0.9248 0.0092  0.0111  -0.0068 455 GLN B O   
6288  C  CB  . GLN B 454 ? 0.4460 0.4425 1.0345 0.0257  -0.0113 -0.0258 455 GLN B CB  
6289  C  CG  . GLN B 454 ? 0.5659 0.5627 1.1722 0.0280  -0.0248 -0.0354 455 GLN B CG  
6290  C  CD  . GLN B 454 ? 0.6510 0.6433 1.2419 0.0410  -0.0340 -0.0451 455 GLN B CD  
6291  O  OE1 . GLN B 454 ? 0.7004 0.6903 1.2674 0.0488  -0.0286 -0.0428 455 GLN B OE1 
6292  N  NE2 . GLN B 454 ? 0.6809 0.6716 1.2861 0.0439  -0.0480 -0.0562 455 GLN B NE2 
6293  N  N   . GLN B 455 ? 0.2566 0.2558 0.8221 0.0174  0.0128  -0.0063 456 GLN B N   
6294  C  CA  . GLN B 455 ? 0.2960 0.2941 0.8484 0.0158  0.0217  -0.0005 456 GLN B CA  
6295  C  C   . GLN B 455 ? 0.3360 0.3354 0.8960 0.0079  0.0272  0.0058  456 GLN B C   
6296  O  O   . GLN B 455 ? 0.4175 0.4159 0.9739 0.0054  0.0318  0.0089  456 GLN B O   
6297  C  CB  . GLN B 455 ? 0.2562 0.2543 0.7928 0.0207  0.0254  0.0018  456 GLN B CB  
6298  C  CG  . GLN B 455 ? 0.2997 0.2950 0.8252 0.0308  0.0216  -0.0027 456 GLN B CG  
6299  C  CD  . GLN B 455 ? 0.4130 0.4038 0.9345 0.0344  0.0203  -0.0067 456 GLN B CD  
6300  O  OE1 . GLN B 455 ? 0.3375 0.3269 0.8537 0.0323  0.0265  -0.0033 456 GLN B OE1 
6301  N  NE2 . GLN B 455 ? 0.3859 0.3743 0.9106 0.0402  0.0114  -0.0147 456 GLN B NE2 
6302  N  N   . ILE B 456 ? 0.2922 0.2927 0.8616 0.0051  0.0269  0.0078  457 ILE B N   
6303  C  CA  . ILE B 456 ? 0.2563 0.2547 0.8291 0.0007  0.0322  0.0141  457 ILE B CA  
6304  C  C   . ILE B 456 ? 0.1969 0.1950 0.7741 -0.0001 0.0313  0.0149  457 ILE B C   
6305  O  O   . ILE B 456 ? 0.2719 0.2694 0.8405 -0.0001 0.0358  0.0194  457 ILE B O   
6306  C  CB  . ILE B 456 ? 0.2285 0.2270 0.8080 0.0007  0.0322  0.0160  457 ILE B CB  
6307  C  CG1 . ILE B 456 ? 0.2177 0.2190 0.7866 0.0034  0.0337  0.0159  457 ILE B CG1 
6308  C  CG2 . ILE B 456 ? 0.2458 0.2432 0.8232 0.0009  0.0376  0.0226  457 ILE B CG2 
6309  C  CD1 . ILE B 456 ? 0.2230 0.2268 0.7991 0.0043  0.0328  0.0166  457 ILE B CD1 
6310  N  N   . MET B 457 ? 0.2007 0.1994 0.7932 -0.0005 0.0245  0.0101  458 MET B N   
6311  C  CA  . MET B 457 ? 0.3882 0.3871 0.9881 -0.0012 0.0227  0.0101  458 MET B CA  
6312  C  C   . MET B 457 ? 0.3591 0.3586 0.9504 -0.0009 0.0252  0.0100  458 MET B C   
6313  O  O   . MET B 457 ? 0.3616 0.3615 0.9498 -0.0013 0.0286  0.0147  458 MET B O   
6314  C  CB  . MET B 457 ? 0.4190 0.4187 1.0387 -0.0013 0.0130  0.0025  458 MET B CB  
6315  C  CG  . MET B 457 ? 0.4161 0.4171 1.0478 -0.0020 0.0104  0.0025  458 MET B CG  
6316  S  SD  . MET B 457 ? 0.7246 0.7201 1.3594 -0.0027 0.0158  0.0127  458 MET B SD  
6317  C  CE  . MET B 457 ? 0.5813 0.5748 1.2310 -0.0002 0.0103  0.0094  458 MET B CE  
6318  N  N   . GLN B 458 ? 0.2867 0.2859 0.8763 0.0000  0.0238  0.0051  459 GLN B N   
6319  C  CA  . GLN B 458 ? 0.3549 0.3529 0.9334 0.0017  0.0267  0.0051  459 GLN B CA  
6320  C  C   . GLN B 458 ? 0.2837 0.2821 0.8501 0.0003  0.0340  0.0121  459 GLN B C   
6321  O  O   . GLN B 458 ? 0.3207 0.3193 0.8847 0.0002  0.0357  0.0141  459 GLN B O   
6322  C  CB  . GLN B 458 ? 0.3214 0.3156 0.8820 0.0089  0.0256  0.0004  459 GLN B CB  
6323  C  CG  . GLN B 458 ? 0.3698 0.3607 0.9327 0.0146  0.0170  -0.0082 459 GLN B CG  
6324  C  CD  . GLN B 458 ? 0.4684 0.4567 1.0404 0.0144  0.0124  -0.0126 459 GLN B CD  
6325  O  OE1 . GLN B 458 ? 0.4916 0.4774 1.0553 0.0158  0.0157  -0.0121 459 GLN B OE1 
6326  N  NE2 . GLN B 458 ? 0.4902 0.4793 1.0811 0.0125  0.0046  -0.0171 459 GLN B NE2 
6327  N  N   . LEU B 459 ? 0.2516 0.2497 0.8092 0.0004  0.0371  0.0150  460 LEU B N   
6328  C  CA  . LEU B 459 ? 0.2996 0.2971 0.8448 0.0005  0.0421  0.0200  460 LEU B CA  
6329  C  C   . LEU B 459 ? 0.3120 0.3096 0.8592 0.0001  0.0433  0.0244  460 LEU B C   
6330  O  O   . LEU B 459 ? 0.3061 0.3038 0.8486 0.0003  0.0455  0.0270  460 LEU B O   
6331  C  CB  . LEU B 459 ? 0.2281 0.2251 0.7682 0.0008  0.0441  0.0215  460 LEU B CB  
6332  C  CG  . LEU B 459 ? 0.2514 0.2484 0.7892 0.0014  0.0445  0.0193  460 LEU B CG  
6333  C  CD1 . LEU B 459 ? 0.1855 0.1824 0.7219 0.0017  0.0456  0.0206  460 LEU B CD1 
6334  C  CD2 . LEU B 459 ? 0.1841 0.1806 0.7141 0.0018  0.0478  0.0201  460 LEU B CD2 
6335  N  N   . LYS B 460 ? 0.3047 0.3021 0.8612 -0.0003 0.0419  0.0258  461 LYS B N   
6336  C  CA  . LYS B 460 ? 0.3134 0.3101 0.8747 -0.0002 0.0443  0.0319  461 LYS B CA  
6337  C  C   . LYS B 460 ? 0.2963 0.2961 0.8642 -0.0006 0.0427  0.0317  461 LYS B C   
6338  O  O   . LYS B 460 ? 0.1990 0.1997 0.7666 -0.0001 0.0459  0.0370  461 LYS B O   
6339  C  CB  . LYS B 460 ? 0.3981 0.3925 0.9706 0.0004  0.0436  0.0341  461 LYS B CB  
6340  C  CG  . LYS B 460 ? 0.5146 0.5082 1.0888 0.0028  0.0500  0.0424  461 LYS B CG  
6341  C  CD  . LYS B 460 ? 0.5215 0.5160 1.1039 0.0034  0.0509  0.0435  461 LYS B CD  
6342  C  CE  . LYS B 460 ? 0.5406 0.5349 1.1361 0.0028  0.0444  0.0385  461 LYS B CE  
6343  N  NZ  . LYS B 460 ? 0.5262 0.5218 1.1318 0.0030  0.0451  0.0397  461 LYS B NZ  
6344  N  N   . ILE B 461 ? 0.1984 0.1996 0.7744 -0.0008 0.0376  0.0255  462 ILE B N   
6345  C  CA  . ILE B 461 ? 0.2247 0.2272 0.8086 -0.0003 0.0355  0.0243  462 ILE B CA  
6346  C  C   . ILE B 461 ? 0.2436 0.2449 0.8163 0.0001  0.0384  0.0251  462 ILE B C   
6347  O  O   . ILE B 461 ? 0.2620 0.2640 0.8372 0.0006  0.0399  0.0291  462 ILE B O   
6348  C  CB  . ILE B 461 ? 0.3097 0.3115 0.9058 -0.0005 0.0287  0.0160  462 ILE B CB  
6349  C  CG1 . ILE B 461 ? 0.3236 0.3270 0.9369 -0.0006 0.0243  0.0154  462 ILE B CG1 
6350  C  CG2 . ILE B 461 ? 0.2793 0.2803 0.8804 -0.0002 0.0270  0.0134  462 ILE B CG2 
6351  C  CD1 . ILE B 461 ? 0.3530 0.3553 0.9764 -0.0009 0.0166  0.0063  462 ILE B CD1 
6352  N  N   . MET B 462 ? 0.2345 0.2343 0.7970 0.0001  0.0393  0.0219  463 MET B N   
6353  C  CA  . MET B 462 ? 0.1911 0.1902 0.7449 0.0005  0.0420  0.0226  463 MET B CA  
6354  C  C   . MET B 462 ? 0.1906 0.1899 0.7383 0.0007  0.0451  0.0285  463 MET B C   
6355  O  O   . MET B 462 ? 0.2957 0.2951 0.8434 0.0011  0.0459  0.0303  463 MET B O   
6356  C  CB  . MET B 462 ? 0.1888 0.1867 0.7353 0.0008  0.0434  0.0195  463 MET B CB  
6357  C  CG  . MET B 462 ? 0.2388 0.2360 0.7798 0.0012  0.0461  0.0198  463 MET B CG  
6358  S  SD  . MET B 462 ? 0.4088 0.4054 0.9589 0.0017  0.0448  0.0169  463 MET B SD  
6359  C  CE  . MET B 462 ? 0.1896 0.1871 0.7377 0.0014  0.0457  0.0216  463 MET B CE  
6360  N  N   . THR B 463 ? 0.1908 0.1899 0.7358 0.0007  0.0468  0.0314  464 THR B N   
6361  C  CA  . THR B 463 ? 0.2929 0.2916 0.8358 0.0014  0.0500  0.0370  464 THR B CA  
6362  C  C   . THR B 463 ? 0.2670 0.2670 0.8197 0.0019  0.0510  0.0425  464 THR B C   
6363  O  O   . THR B 463 ? 0.1955 0.1955 0.7489 0.0027  0.0525  0.0461  464 THR B O   
6364  C  CB  . THR B 463 ? 0.1927 0.1902 0.7344 0.0017  0.0524  0.0393  464 THR B CB  
6365  O  OG1 . THR B 463 ? 0.1896 0.1864 0.7234 0.0016  0.0516  0.0348  464 THR B OG1 
6366  C  CG2 . THR B 463 ? 0.1944 0.1918 0.7380 0.0032  0.0564  0.0454  464 THR B CG2 
6367  N  N   . ASN B 464 ? 0.1977 0.1993 0.7608 0.0016  0.0498  0.0434  465 ASN B N   
6368  C  CA  . ASN B 464 ? 0.2015 0.2051 0.7772 0.0026  0.0507  0.0491  465 ASN B CA  
6369  C  C   . ASN B 464 ? 0.3048 0.3078 0.8813 0.0027  0.0486  0.0473  465 ASN B C   
6370  O  O   . ASN B 464 ? 0.2032 0.2064 0.7844 0.0035  0.0507  0.0534  465 ASN B O   
6371  C  CB  . ASN B 464 ? 0.6282 0.6338 1.2180 0.0031  0.0483  0.0486  465 ASN B CB  
6372  C  CG  . ASN B 464 ? 0.7245 0.7317 1.3193 0.0047  0.0518  0.0537  465 ASN B CG  
6373  O  OD1 . ASN B 464 ? 0.7065 0.7141 1.2996 0.0053  0.0576  0.0613  465 ASN B OD1 
6374  N  ND2 . ASN B 464 ? 0.7107 0.7174 1.3133 0.0057  0.0482  0.0498  465 ASN B ND2 
6375  N  N   . ARG B 465 ? 0.2315 0.2337 0.8051 0.0019  0.0450  0.0396  466 ARG B N   
6376  C  CA  . ARG B 465 ? 0.3073 0.3086 0.8818 0.0019  0.0435  0.0374  466 ARG B CA  
6377  C  C   . ARG B 465 ? 0.3081 0.3088 0.8750 0.0023  0.0458  0.0403  466 ARG B C   
6378  O  O   . ARG B 465 ? 0.1983 0.1991 0.7709 0.0028  0.0456  0.0433  466 ARG B O   
6379  C  CB  . ARG B 465 ? 0.3654 0.3655 0.9376 0.0013  0.0411  0.0293  466 ARG B CB  
6380  C  CG  . ARG B 465 ? 0.4407 0.4407 1.0259 0.0010  0.0370  0.0246  466 ARG B CG  
6381  C  CD  . ARG B 465 ? 0.5029 0.5013 1.0886 0.0010  0.0353  0.0170  466 ARG B CD  
6382  N  NE  . ARG B 465 ? 0.5735 0.5686 1.1667 0.0022  0.0296  0.0106  466 ARG B NE  
6383  C  CZ  . ARG B 465 ? 0.6344 0.6264 1.2225 0.0038  0.0269  0.0047  466 ARG B CZ  
6384  N  NH1 . ARG B 465 ? 0.6228 0.6105 1.2179 0.0056  0.0200  -0.0023 466 ARG B NH1 
6385  N  NH2 . ARG B 465 ? 0.5772 0.5695 1.1534 0.0042  0.0303  0.0055  466 ARG B NH2 
6386  N  N   . LEU B 466 ? 0.2420 0.2422 0.7986 0.0022  0.0472  0.0393  467 LEU B N   
6387  C  CA  . LEU B 466 ? 0.2600 0.2596 0.8123 0.0027  0.0480  0.0406  467 LEU B CA  
6388  C  C   . LEU B 466 ? 0.1957 0.1957 0.7554 0.0039  0.0500  0.0483  467 LEU B C   
6389  O  O   . LEU B 466 ? 0.1973 0.1967 0.7579 0.0053  0.0489  0.0497  467 LEU B O   
6390  C  CB  . LEU B 466 ? 0.1897 0.1886 0.7322 0.0024  0.0486  0.0372  467 LEU B CB  
6391  C  CG  . LEU B 466 ? 0.1990 0.1973 0.7362 0.0018  0.0478  0.0316  467 LEU B CG  
6392  C  CD1 . LEU B 466 ? 0.1858 0.1835 0.7157 0.0015  0.0489  0.0292  467 LEU B CD1 
6393  C  CD2 . LEU B 466 ? 0.1875 0.1855 0.7255 0.0020  0.0471  0.0310  467 LEU B CD2 
6394  N  N   . ARG B 467 ? 0.1984 0.1990 0.7625 0.0044  0.0528  0.0536  468 ARG B N   
6395  C  CA  . ARG B 467 ? 0.4022 0.4034 0.9753 0.0065  0.0567  0.0633  468 ARG B CA  
6396  C  C   . ARG B 467 ? 0.4023 0.4032 0.9830 0.0078  0.0557  0.0678  468 ARG B C   
6397  O  O   . ARG B 467 ? 0.4187 0.4164 0.9941 0.0126  0.0552  0.0725  468 ARG B O   
6398  C  CB  . ARG B 467 ? 0.4681 0.4700 1.0454 0.0070  0.0614  0.0691  468 ARG B CB  
6399  N  N   . SER B 468 ? 0.3429 0.3455 0.9313 0.0057  0.0540  0.0653  469 SER B N   
6400  C  CA  . SER B 468 ? 0.3534 0.3564 0.9533 0.0060  0.0526  0.0681  469 SER B CA  
6401  C  C   . SER B 468 ? 0.3940 0.3927 0.9830 0.0076  0.0489  0.0645  469 SER B C   
6402  O  O   . SER B 468 ? 0.3063 0.3012 0.8939 0.0110  0.0484  0.0702  469 SER B O   
6403  C  CB  . SER B 468 ? 0.2737 0.2769 0.8786 0.0048  0.0490  0.0621  469 SER B CB  
6404  O  OG  . SER B 468 ? 0.3574 0.3617 0.9678 0.0049  0.0505  0.0644  469 SER B OG  
6405  N  N   . ALA B 469 ? 0.3472 0.3466 0.9292 0.0058  0.0467  0.0558  470 ALA B N   
6406  C  CA  . ALA B 469 ? 0.3379 0.3348 0.9127 0.0072  0.0437  0.0519  470 ALA B CA  
6407  C  C   . ALA B 469 ? 0.2970 0.2915 0.8640 0.0113  0.0428  0.0554  470 ALA B C   
6408  O  O   . ALA B 469 ? 0.3422 0.3345 0.9074 0.0142  0.0396  0.0555  470 ALA B O   
6409  C  CB  . ALA B 469 ? 0.2314 0.2297 0.8012 0.0048  0.0432  0.0437  470 ALA B CB  
6410  N  N   . TYR B 470 ? 0.3936 0.3887 0.9561 0.0126  0.0450  0.0576  471 TYR B N   
6411  C  CA  . TYR B 470 ? 0.3436 0.3371 0.8980 0.0190  0.0433  0.0602  471 TYR B CA  
6412  C  C   . TYR B 470 ? 0.3725 0.3633 0.9289 0.0244  0.0435  0.0693  471 TYR B C   
6413  O  O   . TYR B 470 ? 0.2802 0.2693 0.8319 0.0300  0.0392  0.0697  471 TYR B O   
6414  C  CB  . TYR B 470 ? 0.3166 0.3118 0.8657 0.0210  0.0460  0.0609  471 TYR B CB  
6415  C  CG  . TYR B 470 ? 0.3826 0.3782 0.9227 0.0292  0.0426  0.0601  471 TYR B CG  
6416  C  CD1 . TYR B 470 ? 0.3744 0.3711 0.9104 0.0290  0.0376  0.0512  471 TYR B CD1 
6417  C  CD2 . TYR B 470 ? 0.3995 0.3952 0.9363 0.0379  0.0442  0.0683  471 TYR B CD2 
6418  C  CE1 . TYR B 470 ? 0.4399 0.4381 0.9700 0.0371  0.0328  0.0487  471 TYR B CE1 
6419  C  CE2 . TYR B 470 ? 0.4166 0.4141 0.9447 0.0475  0.0398  0.0664  471 TYR B CE2 
6420  C  CZ  . TYR B 470 ? 0.4410 0.4398 0.9663 0.0469  0.0332  0.0556  471 TYR B CZ  
6421  O  OH  . TYR B 470 ? 0.5149 0.5159 1.0337 0.0568  0.0271  0.0518  471 TYR B OH  
6422  N  N   . ASN B 471 ? 0.6017 0.5923 1.1661 0.0231  0.0484  0.0771  472 ASN B N   
6423  C  CA  . ASN B 471 ? 0.6497 0.6370 1.2167 0.0282  0.0499  0.0880  472 ASN B CA  
6424  C  C   . ASN B 471 ? 0.6815 0.6656 1.2517 0.0277  0.0454  0.0867  472 ASN B C   
6425  O  O   . ASN B 471 ? 0.6383 0.6187 1.2061 0.0338  0.0443  0.0941  472 ASN B O   
6426  C  CB  . ASN B 471 ? 0.6262 0.6147 1.2051 0.0257  0.0569  0.0971  472 ASN B CB  
6427  C  CG  . ASN B 471 ? 0.6415 0.6328 1.2175 0.0285  0.0625  0.1014  472 ASN B CG  
6428  O  OD1 . ASN B 471 ? 0.6559 0.6474 1.2193 0.0362  0.0620  0.1021  472 ASN B OD1 
6429  N  ND2 . ASN B 471 ? 0.6690 0.6638 1.2576 0.0232  0.0674  0.1036  472 ASN B ND2 
6430  N  N   . GLY B 472 ? 0.7218 0.7077 1.2968 0.0216  0.0430  0.0777  473 GLY B N   
6431  C  CA  . GLY B 472 ? 0.7734 0.7569 1.3519 0.0215  0.0391  0.0754  473 GLY B CA  
6432  C  C   . GLY B 472 ? 0.8342 0.8184 1.4247 0.0170  0.0401  0.0743  473 GLY B C   
6433  O  O   . GLY B 472 ? 0.8566 0.8389 1.4505 0.0166  0.0370  0.0705  473 GLY B O   
6434  N  N   . ASN B 473 ? 0.8343 0.8214 1.4321 0.0145  0.0439  0.0772  474 ASN B N   
6435  C  CA  . ASN B 473 ? 0.8841 0.8728 1.4951 0.0113  0.0434  0.0750  474 ASN B CA  
6436  C  C   . ASN B 473 ? 0.8940 0.8859 1.5036 0.0083  0.0410  0.0630  474 ASN B C   
6437  O  O   . ASN B 473 ? 0.8637 0.8568 1.4630 0.0079  0.0407  0.0577  474 ASN B O   
6438  C  CB  . ASN B 473 ? 0.8687 0.8603 1.4907 0.0106  0.0481  0.0829  474 ASN B CB  
6439  C  CG  . ASN B 473 ? 0.8910 0.8797 1.5094 0.0146  0.0530  0.0961  474 ASN B CG  
6440  O  OD1 . ASN B 473 ? 0.8974 0.8807 1.5083 0.0186  0.0517  0.1007  474 ASN B OD1 
6441  N  ND2 . ASN B 473 ? 0.8894 0.8817 1.5126 0.0146  0.0588  0.1025  474 ASN B ND2 
6442  N  N   . ASP B 474 ? 0.9594 0.9517 1.5795 0.0067  0.0389  0.0591  475 ASP B N   
6443  C  CA  . ASP B 474 ? 0.9867 0.9807 1.6050 0.0050  0.0367  0.0488  475 ASP B CA  
6444  C  C   . ASP B 474 ? 0.9668 0.9610 1.5995 0.0041  0.0341  0.0467  475 ASP B C   
6445  O  O   . ASP B 474 ? 0.9521 0.9457 1.5843 0.0034  0.0309  0.0380  475 ASP B O   
6446  C  CB  . ASP B 474 ? 1.0420 1.0322 1.6517 0.0060  0.0342  0.0412  475 ASP B CB  
6447  C  CG  . ASP B 474 ? 1.1025 1.0873 1.7192 0.0073  0.0307  0.0401  475 ASP B CG  
6448  O  OD1 . ASP B 474 ? 1.1383 1.1212 1.7654 0.0067  0.0278  0.0376  475 ASP B OD1 
6449  O  OD2 . ASP B 474 ? 1.1112 1.0932 1.7237 0.0092  0.0303  0.0412  475 ASP B OD2 
6450  N  N   . SER C 28  ? 0.7875 0.6809 1.0498 -0.1550 0.0017  0.0724  29  SER C N   
6451  C  CA  . SER C 28  ? 0.7565 0.6469 1.0257 -0.1550 -0.0019 0.0853  29  SER C CA  
6452  C  C   . SER C 28  ? 0.8037 0.7151 1.0700 -0.1524 -0.0030 0.0956  29  SER C C   
6453  O  O   . SER C 28  ? 0.8064 0.7306 1.0699 -0.1455 -0.0009 0.0938  29  SER C O   
6454  C  CB  . SER C 28  ? 0.7696 0.6421 1.0502 -0.1469 -0.0016 0.0868  29  SER C CB  
6455  O  OG  . SER C 28  ? 0.7572 0.6272 1.0421 -0.1478 -0.0063 0.1008  29  SER C OG  
6456  N  N   . ARG C 29  ? 0.7504 0.6647 1.0175 -0.1587 -0.0057 0.1060  30  ARG C N   
6457  C  CA  . ARG C 29  ? 0.6765 0.6096 0.9409 -0.1581 -0.0052 0.1149  30  ARG C CA  
6458  C  C   . ARG C 29  ? 0.6444 0.5731 0.9098 -0.1527 -0.0062 0.1243  30  ARG C C   
6459  O  O   . ARG C 29  ? 0.6307 0.5725 0.8922 -0.1534 -0.0049 0.1316  30  ARG C O   
6460  C  CB  . ARG C 29  ? 0.6580 0.5992 0.9222 -0.1695 -0.0060 0.1202  30  ARG C CB  
6461  C  CG  . ARG C 29  ? 0.6104 0.5606 0.8741 -0.1757 -0.0065 0.1129  30  ARG C CG  
6462  C  CD  . ARG C 29  ? 0.6516 0.6104 0.9185 -0.1871 -0.0076 0.1187  30  ARG C CD  
6463  N  NE  . ARG C 29  ? 0.6587 0.6253 0.9264 -0.1941 -0.0100 0.1127  30  ARG C NE  
6464  C  CZ  . ARG C 29  ? 0.6349 0.6089 0.9074 -0.2050 -0.0120 0.1161  30  ARG C CZ  
6465  N  NH1 . ARG C 29  ? 0.6197 0.5943 0.8964 -0.2101 -0.0105 0.1248  30  ARG C NH1 
6466  N  NH2 . ARG C 29  ? 0.6074 0.5885 0.8803 -0.2117 -0.0157 0.1110  30  ARG C NH2 
6467  N  N   . SER C 30  ? 0.6429 0.5531 0.9140 -0.1481 -0.0084 0.1242  31  SER C N   
6468  C  CA  . SER C 30  ? 0.6698 0.5746 0.9426 -0.1436 -0.0115 0.1342  31  SER C CA  
6469  C  C   . SER C 30  ? 0.6571 0.5762 0.9266 -0.1349 -0.0094 0.1337  31  SER C C   
6470  O  O   . SER C 30  ? 0.5737 0.5014 0.8426 -0.1298 -0.0057 0.1242  31  SER C O   
6471  C  CB  . SER C 30  ? 0.6910 0.5733 0.9755 -0.1395 -0.0150 0.1339  31  SER C CB  
6472  O  OG  . SER C 30  ? 0.7099 0.5896 1.0007 -0.1309 -0.0115 0.1220  31  SER C OG  
6473  N  N   . CYS C 31  ? 0.6312 0.5519 0.8971 -0.1342 -0.0119 0.1441  32  CYS C N   
6474  C  CA  . CYS C 31  ? 0.6439 0.5775 0.9056 -0.1271 -0.0101 0.1443  32  CYS C CA  
6475  C  C   . CYS C 31  ? 0.6913 0.6146 0.9596 -0.1197 -0.0150 0.1487  32  CYS C C   
6476  O  O   . CYS C 31  ? 0.6324 0.5630 0.8955 -0.1169 -0.0161 0.1538  32  CYS C O   
6477  C  CB  . CYS C 31  ? 0.6702 0.6173 0.9205 -0.1334 -0.0080 0.1517  32  CYS C CB  
6478  S  SG  . CYS C 31  ? 0.6904 0.6553 0.9382 -0.1399 -0.0013 0.1464  32  CYS C SG  
6479  N  N   . GLY C 32  ? 0.6862 0.5924 0.9672 -0.1168 -0.0180 0.1466  33  GLY C N   
6480  C  CA  . GLY C 32  ? 0.7060 0.6015 0.9988 -0.1098 -0.0235 0.1515  33  GLY C CA  
6481  C  C   . GLY C 32  ? 0.6559 0.5607 0.9523 -0.0995 -0.0209 0.1455  33  GLY C C   
6482  O  O   . GLY C 32  ? 0.7122 0.6199 1.0086 -0.0965 -0.0253 0.1533  33  GLY C O   
6483  N  N   . GLU C 33  ? 0.6375 0.5468 0.9360 -0.0953 -0.0139 0.1319  34  GLU C N   
6484  C  CA  . GLU C 33  ? 0.6473 0.5658 0.9487 -0.0863 -0.0103 0.1251  34  GLU C CA  
6485  C  C   . GLU C 33  ? 0.6150 0.5503 0.9032 -0.0865 -0.0102 0.1303  34  GLU C C   
6486  O  O   . GLU C 33  ? 0.6371 0.5757 0.9282 -0.0811 -0.0127 0.1342  34  GLU C O   
6487  C  CB  . GLU C 33  ? 0.6650 0.5862 0.9653 -0.0850 -0.0025 0.1102  34  GLU C CB  
6488  N  N   . VAL C 34  ? 0.5812 0.5272 0.8566 -0.0931 -0.0072 0.1303  35  VAL C N   
6489  C  CA  . VAL C 34  ? 0.5219 0.4833 0.7857 -0.0943 -0.0055 0.1341  35  VAL C CA  
6490  C  C   . VAL C 34  ? 0.5298 0.4877 0.7894 -0.0970 -0.0113 0.1464  35  VAL C C   
6491  O  O   . VAL C 34  ? 0.6809 0.6471 0.9349 -0.0945 -0.0112 0.1486  35  VAL C O   
6492  C  CB  . VAL C 34  ? 0.5184 0.4903 0.7736 -0.1019 -0.0014 0.1330  35  VAL C CB  
6493  C  CG1 . VAL C 34  ? 0.5083 0.4951 0.7541 -0.1029 0.0018  0.1362  35  VAL C CG1 
6494  C  CG2 . VAL C 34  ? 0.5121 0.4882 0.7699 -0.1006 0.0025  0.1221  35  VAL C CG2 
6495  N  N   . ARG C 35  ? 0.5950 0.5398 0.8563 -0.1029 -0.0168 0.1546  36  ARG C N   
6496  C  CA  . ARG C 35  ? 0.6548 0.5945 0.9103 -0.1073 -0.0240 0.1677  36  ARG C CA  
6497  C  C   . ARG C 35  ? 0.7075 0.6434 0.9729 -0.0992 -0.0298 0.1705  36  ARG C C   
6498  O  O   . ARG C 35  ? 0.7538 0.6948 1.0105 -0.1004 -0.0329 0.1770  36  ARG C O   
6499  C  CB  . ARG C 35  ? 0.6397 0.5642 0.8969 -0.1153 -0.0299 0.1768  36  ARG C CB  
6500  C  CG  . ARG C 35  ? 0.7257 0.6427 0.9770 -0.1208 -0.0393 0.1920  36  ARG C CG  
6501  C  CD  . ARG C 35  ? 0.8021 0.7013 1.0588 -0.1274 -0.0468 0.2017  36  ARG C CD  
6502  N  NE  . ARG C 35  ? 0.8942 0.7949 1.1357 -0.1399 -0.0436 0.2057  36  ARG C NE  
6503  C  CZ  . ARG C 35  ? 0.9270 0.8267 1.1715 -0.1429 -0.0383 0.1992  36  ARG C CZ  
6504  N  NH1 . ARG C 35  ? 0.9154 0.8115 1.1751 -0.1351 -0.0357 0.1882  36  ARG C NH1 
6505  N  NH2 . ARG C 35  ? 0.9609 0.8633 1.1929 -0.1547 -0.0354 0.2036  36  ARG C NH2 
6506  N  N   . GLN C 36  ? 0.6911 0.6179 0.9753 -0.0915 -0.0308 0.1652  37  GLN C N   
6507  C  CA  . GLN C 36  ? 0.7302 0.6529 1.0290 -0.0835 -0.0365 0.1682  37  GLN C CA  
6508  C  C   . GLN C 36  ? 0.6635 0.6009 0.9591 -0.0770 -0.0318 0.1616  37  GLN C C   
6509  O  O   . GLN C 36  ? 0.6098 0.5492 0.9081 -0.0743 -0.0374 0.1678  37  GLN C O   
6510  C  CB  . GLN C 36  ? 0.7623 0.6713 1.0848 -0.0770 -0.0367 0.1627  37  GLN C CB  
6511  C  CG  . GLN C 36  ? 0.8567 0.7541 1.1993 -0.0730 -0.0471 0.1731  37  GLN C CG  
6512  C  CD  . GLN C 36  ? 0.9401 0.8300 1.2748 -0.0823 -0.0586 0.1908  37  GLN C CD  
6513  O  OE1 . GLN C 36  ? 0.9672 0.8653 1.2838 -0.0879 -0.0623 0.1991  37  GLN C OE1 
6514  N  NE2 . GLN C 36  ? 0.9671 0.8401 1.3144 -0.0848 -0.0639 0.1966  37  GLN C NE2 
6515  N  N   . ILE C 37  ? 0.6797 0.6270 0.9694 -0.0752 -0.0223 0.1497  38  ILE C N   
6516  C  CA  . ILE C 37  ? 0.6104 0.5716 0.8961 -0.0698 -0.0176 0.1436  38  ILE C CA  
6517  C  C   . ILE C 37  ? 0.7106 0.6818 0.9785 -0.0752 -0.0183 0.1502  38  ILE C C   
6518  O  O   . ILE C 37  ? 0.7380 0.7167 1.0036 -0.0718 -0.0186 0.1504  38  ILE C O   
6519  C  CB  . ILE C 37  ? 0.6195 0.5879 0.9031 -0.0676 -0.0083 0.1304  38  ILE C CB  
6520  C  CG1 . ILE C 37  ? 0.6028 0.5603 0.9015 -0.0635 -0.0062 0.1222  38  ILE C CG1 
6521  C  CG2 . ILE C 37  ? 0.5516 0.5337 0.8308 -0.0626 -0.0039 0.1252  38  ILE C CG2 
6522  C  CD1 . ILE C 37  ? 0.6139 0.5771 0.9082 -0.0631 0.0019  0.1096  38  ILE C CD1 
6523  N  N   . TYR C 38  ? 0.6666 0.6374 0.9222 -0.0844 -0.0180 0.1551  39  TYR C N   
6524  C  CA  . TYR C 38  ? 0.6644 0.6435 0.9023 -0.0913 -0.0168 0.1603  39  TYR C CA  
6525  C  C   . TYR C 38  ? 0.6513 0.6243 0.8850 -0.0945 -0.0260 0.1719  39  TYR C C   
6526  O  O   . TYR C 38  ? 0.6247 0.6048 0.8477 -0.0959 -0.0257 0.1735  39  TYR C O   
6527  C  CB  . TYR C 38  ? 0.5226 0.5025 0.7505 -0.1010 -0.0131 0.1622  39  TYR C CB  
6528  C  CG  . TYR C 38  ? 0.5244 0.5134 0.7349 -0.1087 -0.0087 0.1652  39  TYR C CG  
6529  C  CD1 . TYR C 38  ? 0.6336 0.6366 0.8404 -0.1058 -0.0004 0.1575  39  TYR C CD1 
6530  C  CD2 . TYR C 38  ? 0.5430 0.5256 0.7405 -0.1197 -0.0121 0.1754  39  TYR C CD2 
6531  C  CE1 . TYR C 38  ? 0.5128 0.5232 0.7054 -0.1129 0.0053  0.1587  39  TYR C CE1 
6532  C  CE2 . TYR C 38  ? 0.5473 0.5375 0.7276 -0.1280 -0.0062 0.1766  39  TYR C CE2 
6533  C  CZ  . TYR C 38  ? 0.5320 0.5360 0.7108 -0.1242 0.0031  0.1676  39  TYR C CZ  
6534  O  OH  . TYR C 38  ? 0.6189 0.6297 0.7823 -0.1324 0.0106  0.1675  39  TYR C OH  
6535  N  N   . GLY C 39  ? 0.5438 0.5029 0.7859 -0.0964 -0.0349 0.1805  40  GLY C N   
6536  C  CA  . GLY C 39  ? 0.5585 0.5106 0.7987 -0.1001 -0.0462 0.1936  40  GLY C CA  
6537  C  C   . GLY C 39  ? 0.6927 0.6472 0.9473 -0.0905 -0.0504 0.1923  40  GLY C C   
6538  O  O   . GLY C 39  ? 0.7280 0.6839 0.9759 -0.0935 -0.0575 0.2004  40  GLY C O   
6539  N  N   . ALA C 40  ? 0.7213 0.6763 0.9949 -0.0799 -0.0458 0.1820  41  ALA C N   
6540  C  CA  . ALA C 40  ? 0.6587 0.6167 0.9488 -0.0703 -0.0479 0.1793  41  ALA C CA  
6541  C  C   . ALA C 40  ? 0.7060 0.6777 0.9827 -0.0701 -0.0446 0.1765  41  ALA C C   
6542  O  O   . ALA C 40  ? 0.7385 0.7127 1.0231 -0.0663 -0.0499 0.1796  41  ALA C O   
6543  C  CB  . ALA C 40  ? 0.6572 0.6141 0.9660 -0.0608 -0.0403 0.1665  41  ALA C CB  
6544  N  N   . LYS C 41  ? 0.7107 0.6910 0.9689 -0.0743 -0.0357 0.1706  42  LYS C N   
6545  C  CA  . LYS C 41  ? 0.6895 0.6818 0.9353 -0.0743 -0.0312 0.1668  42  LYS C CA  
6546  C  C   . LYS C 41  ? 0.6642 0.6563 0.8895 -0.0851 -0.0358 0.1764  42  LYS C C   
6547  O  O   . LYS C 41  ? 0.6473 0.6480 0.8586 -0.0876 -0.0306 0.1730  42  LYS C O   
6548  C  CB  . LYS C 41  ? 0.7405 0.7425 0.9803 -0.0727 -0.0191 0.1554  42  LYS C CB  
6549  C  CG  . LYS C 41  ? 0.7416 0.7447 0.9973 -0.0635 -0.0143 0.1453  42  LYS C CG  
6550  C  CD  . LYS C 41  ? 0.7549 0.7700 1.0049 -0.0610 -0.0049 0.1356  42  LYS C CD  
6551  C  CE  . LYS C 41  ? 0.7808 0.7973 1.0438 -0.0527 -0.0012 0.1265  42  LYS C CE  
6552  N  NZ  . LYS C 41  ? 0.7956 0.8039 1.0669 -0.0524 -0.0002 0.1227  42  LYS C NZ  
6553  N  N   . GLY C 42  ? 0.6782 0.6595 0.9011 -0.0922 -0.0453 0.1882  43  GLY C N   
6554  C  CA  . GLY C 42  ? 0.6712 0.6503 0.8737 -0.1040 -0.0519 0.1989  43  GLY C CA  
6555  C  C   . GLY C 42  ? 0.6882 0.6658 0.8686 -0.1165 -0.0470 0.2015  43  GLY C C   
6556  O  O   . GLY C 42  ? 0.7377 0.7106 0.8995 -0.1284 -0.0530 0.2115  43  GLY C O   
6557  N  N   . PHE C 43  ? 0.6695 0.6511 0.8517 -0.1148 -0.0363 0.1927  44  PHE C N   
6558  C  CA  . PHE C 43  ? 0.7044 0.6868 0.8682 -0.1263 -0.0296 0.1937  44  PHE C CA  
6559  C  C   . PHE C 43  ? 0.7351 0.7047 0.8982 -0.1341 -0.0371 0.2045  44  PHE C C   
6560  O  O   . PHE C 43  ? 0.7849 0.7445 0.9634 -0.1298 -0.0476 0.2111  44  PHE C O   
6561  C  CB  . PHE C 43  ? 0.6615 0.6544 0.8299 -0.1218 -0.0161 0.1811  44  PHE C CB  
6562  C  CG  . PHE C 43  ? 0.6337 0.6385 0.8043 -0.1142 -0.0089 0.1710  44  PHE C CG  
6563  C  CD1 . PHE C 43  ? 0.6019 0.6120 0.7562 -0.1196 -0.0049 0.1703  44  PHE C CD1 
6564  C  CD2 . PHE C 43  ? 0.6003 0.6102 0.7882 -0.1025 -0.0059 0.1623  44  PHE C CD2 
6565  C  CE1 . PHE C 43  ? 0.5744 0.5943 0.7317 -0.1126 0.0015  0.1613  44  PHE C CE1 
6566  C  CE2 . PHE C 43  ? 0.5518 0.5719 0.7415 -0.0961 0.0001  0.1541  44  PHE C CE2 
6567  C  CZ  . PHE C 43  ? 0.5106 0.5357 0.6860 -0.1007 0.0037  0.1538  44  PHE C CZ  
6568  N  N   . SER C 44  ? 0.7273 0.6971 0.8740 -0.1456 -0.0311 0.2062  45  SER C N   
6569  C  CA  . SER C 44  ? 0.7448 0.7023 0.8865 -0.1557 -0.0380 0.2178  45  SER C CA  
6570  C  C   . SER C 44  ? 0.7148 0.6678 0.8748 -0.1506 -0.0367 0.2146  45  SER C C   
6571  O  O   . SER C 44  ? 0.6770 0.6387 0.8410 -0.1480 -0.0258 0.2042  45  SER C O   
6572  C  CB  . SER C 44  ? 0.7501 0.7097 0.8655 -0.1717 -0.0309 0.2206  45  SER C CB  
6573  O  OG  . SER C 44  ? 0.7736 0.7210 0.8826 -0.1827 -0.0375 0.2324  45  SER C OG  
6574  N  N   . LEU C 45  ? 0.6889 0.6277 0.8607 -0.1498 -0.0484 0.2239  46  LEU C N   
6575  C  CA  . LEU C 45  ? 0.7032 0.6346 0.8918 -0.1461 -0.0481 0.2212  46  LEU C CA  
6576  C  C   . LEU C 45  ? 0.6311 0.5620 0.8075 -0.1581 -0.0421 0.2229  46  LEU C C   
6577  O  O   . LEU C 45  ? 0.6258 0.5556 0.8128 -0.1560 -0.0377 0.2170  46  LEU C O   
6578  C  CB  . LEU C 45  ? 0.6929 0.6077 0.8982 -0.1433 -0.0620 0.2317  46  LEU C CB  
6579  C  CG  . LEU C 45  ? 0.6822 0.5966 0.9084 -0.1298 -0.0673 0.2289  46  LEU C CG  
6580  C  CD1 . LEU C 45  ? 0.6413 0.5390 0.8843 -0.1291 -0.0821 0.2422  46  LEU C CD1 
6581  C  CD2 . LEU C 45  ? 0.6020 0.5219 0.8449 -0.1178 -0.0577 0.2127  46  LEU C CD2 
6582  N  N   . SER C 46  ? 0.6896 0.6212 0.8429 -0.1715 -0.0417 0.2308  47  SER C N   
6583  C  CA  . SER C 46  ? 0.6614 0.5921 0.8021 -0.1847 -0.0359 0.2339  47  SER C CA  
6584  C  C   . SER C 46  ? 0.6682 0.6153 0.8087 -0.1838 -0.0200 0.2204  47  SER C C   
6585  O  O   . SER C 46  ? 0.6914 0.6398 0.8294 -0.1920 -0.0140 0.2202  47  SER C O   
6586  C  CB  . SER C 46  ? 0.7536 0.6795 0.8677 -0.2007 -0.0397 0.2463  47  SER C CB  
6587  O  OG  . SER C 46  ? 0.8068 0.7172 0.9229 -0.2026 -0.0564 0.2610  47  SER C OG  
6588  N  N   . ASP C 47  ? 0.6777 0.6373 0.8223 -0.1742 -0.0138 0.2099  48  ASP C N   
6589  C  CA  . ASP C 47  ? 0.6547 0.6302 0.8034 -0.1716 -0.0001 0.1976  48  ASP C CA  
6590  C  C   . ASP C 47  ? 0.6433 0.6191 0.8112 -0.1656 0.0007  0.1918  48  ASP C C   
6591  O  O   . ASP C 47  ? 0.6630 0.6471 0.8336 -0.1699 0.0090  0.1873  48  ASP C O   
6592  C  CB  . ASP C 47  ? 0.6676 0.6547 0.8181 -0.1620 0.0046  0.1888  48  ASP C CB  
6593  C  CG  . ASP C 47  ? 0.7167 0.7068 0.8462 -0.1701 0.0081  0.1913  48  ASP C CG  
6594  O  OD1 . ASP C 47  ? 0.6677 0.6508 0.7795 -0.1838 0.0066  0.2002  48  ASP C OD1 
6595  O  OD2 . ASP C 47  ? 0.8926 0.8914 1.0221 -0.1636 0.0125  0.1843  48  ASP C OD2 
6596  N  N   . VAL C 48  ? 0.5905 0.5570 0.7723 -0.1563 -0.0078 0.1915  49  VAL C N   
6597  C  CA  . VAL C 48  ? 0.5806 0.5464 0.7790 -0.1502 -0.0069 0.1840  49  VAL C CA  
6598  C  C   . VAL C 48  ? 0.6521 0.6099 0.8515 -0.1597 -0.0078 0.1885  49  VAL C C   
6599  O  O   . VAL C 48  ? 0.6656 0.6089 0.8617 -0.1658 -0.0155 0.1989  49  VAL C O   
6600  C  CB  . VAL C 48  ? 0.5765 0.5324 0.7890 -0.1392 -0.0145 0.1821  49  VAL C CB  
6601  C  CG1 . VAL C 48  ? 0.5669 0.5232 0.7932 -0.1338 -0.0116 0.1719  49  VAL C CG1 
6602  C  CG2 . VAL C 48  ? 0.5644 0.5272 0.7760 -0.1307 -0.0145 0.1792  49  VAL C CG2 
6603  N  N   . PRO C 49  ? 0.6319 0.5995 0.8371 -0.1613 -0.0007 0.1812  50  PRO C N   
6604  C  CA  . PRO C 49  ? 0.6225 0.5842 0.8309 -0.1701 -0.0010 0.1838  50  PRO C CA  
6605  C  C   . PRO C 49  ? 0.6054 0.5499 0.8252 -0.1664 -0.0091 0.1839  50  PRO C C   
6606  O  O   . PRO C 49  ? 0.6834 0.6245 0.9118 -0.1557 -0.0119 0.1782  50  PRO C O   
6607  C  CB  . PRO C 49  ? 0.5829 0.5619 0.7985 -0.1699 0.0076  0.1745  50  PRO C CB  
6608  C  CG  . PRO C 49  ? 0.6904 0.6845 0.9026 -0.1641 0.0139  0.1697  50  PRO C CG  
6609  C  CD  . PRO C 49  ? 0.5659 0.5517 0.7754 -0.1557 0.0077  0.1710  50  PRO C CD  
6610  N  N   . GLN C 50  ? 0.6407 0.5739 0.8611 -0.1755 -0.0121 0.1898  51  GLN C N   
6611  C  CA  A GLN C 50  ? 0.6798 0.5951 0.9121 -0.1731 -0.0188 0.1893  51  GLN C CA  
6612  C  CA  B GLN C 50  ? 0.6768 0.5921 0.9092 -0.1728 -0.0189 0.1892  51  GLN C CA  
6613  C  C   . GLN C 50  ? 0.6721 0.5923 0.9151 -0.1673 -0.0151 0.1758  51  GLN C C   
6614  O  O   . GLN C 50  ? 0.7046 0.6145 0.9576 -0.1595 -0.0179 0.1699  51  GLN C O   
6615  C  CB  A GLN C 50  ? 0.7124 0.6155 0.9423 -0.1857 -0.0221 0.1986  51  GLN C CB  
6616  C  CB  B GLN C 50  ? 0.7029 0.6049 0.9330 -0.1850 -0.0227 0.1990  51  GLN C CB  
6617  C  CG  A GLN C 50  ? 0.7137 0.6055 0.9336 -0.1920 -0.0291 0.2137  51  GLN C CG  
6618  C  CG  B GLN C 50  ? 0.7267 0.6167 0.9480 -0.1902 -0.0304 0.2139  51  GLN C CG  
6619  C  CD  A GLN C 50  ? 0.7388 0.6138 0.9693 -0.1835 -0.0391 0.2179  51  GLN C CD  
6620  C  CD  B GLN C 50  ? 0.7256 0.6237 0.9287 -0.2037 -0.0260 0.2219  51  GLN C CD  
6621  O  OE1 A GLN C 50  ? 0.6710 0.5501 0.9015 -0.1752 -0.0410 0.2174  51  GLN C OE1 
6622  O  OE1 B GLN C 50  ? 0.7004 0.5911 0.8996 -0.2155 -0.0269 0.2290  51  GLN C OE1 
6623  N  NE2 A GLN C 50  ? 0.7544 0.6102 0.9960 -0.1855 -0.0456 0.2221  51  GLN C NE2 
6624  N  NE2 B GLN C 50  ? 0.7095 0.6224 0.9013 -0.2027 -0.0204 0.2203  51  GLN C NE2 
6625  N  N   . ALA C 51  ? 0.6104 0.5462 0.8517 -0.1720 -0.0086 0.1710  52  ALA C N   
6626  C  CA  . ALA C 51  ? 0.5996 0.5418 0.8487 -0.1687 -0.0061 0.1595  52  ALA C CA  
6627  C  C   . ALA C 51  ? 0.5808 0.5462 0.8285 -0.1670 0.0005  0.1550  52  ALA C C   
6628  O  O   . ALA C 51  ? 0.5771 0.5524 0.8183 -0.1686 0.0044  0.1598  52  ALA C O   
6629  C  CB  . ALA C 51  ? 0.7039 0.6387 0.9574 -0.1781 -0.0074 0.1589  52  ALA C CB  
6630  N  N   . GLU C 52  ? 0.5710 0.5443 0.8247 -0.1646 0.0017  0.1460  53  GLU C N   
6631  C  CA  . GLU C 52  ? 0.6419 0.6363 0.8975 -0.1619 0.0067  0.1420  53  GLU C CA  
6632  C  C   . GLU C 52  ? 0.6560 0.6645 0.9140 -0.1709 0.0115  0.1465  53  GLU C C   
6633  O  O   . GLU C 52  ? 0.7064 0.7118 0.9677 -0.1802 0.0104  0.1487  53  GLU C O   
6634  C  CB  . GLU C 52  ? 0.6058 0.6039 0.8665 -0.1589 0.0050  0.1327  53  GLU C CB  
6635  C  CG  . GLU C 52  ? 0.5947 0.5845 0.8532 -0.1489 0.0034  0.1264  53  GLU C CG  
6636  C  CD  . GLU C 52  ? 0.6058 0.5961 0.8658 -0.1486 0.0019  0.1170  53  GLU C CD  
6637  O  OE1 . GLU C 52  ? 0.6008 0.6005 0.8636 -0.1557 0.0011  0.1160  53  GLU C OE1 
6638  O  OE2 . GLU C 52  ? 0.6136 0.5950 0.8718 -0.1422 0.0016  0.1107  53  GLU C OE2 
6639  N  N   . ILE C 53  ? 0.6249 0.6486 0.8824 -0.1684 0.0176  0.1472  54  ILE C N   
6640  C  CA  . ILE C 53  ? 0.6211 0.6596 0.8834 -0.1762 0.0245  0.1502  54  ILE C CA  
6641  C  C   . ILE C 53  ? 0.6041 0.6628 0.8793 -0.1723 0.0278  0.1449  54  ILE C C   
6642  O  O   . ILE C 53  ? 0.5145 0.5747 0.7918 -0.1643 0.0243  0.1397  54  ILE C O   
6643  C  CB  . ILE C 53  ? 0.6211 0.6603 0.8727 -0.1786 0.0306  0.1555  54  ILE C CB  
6644  C  CG1 . ILE C 53  ? 0.6332 0.6777 0.8812 -0.1682 0.0327  0.1520  54  ILE C CG1 
6645  C  CG2 . ILE C 53  ? 0.5662 0.5854 0.8054 -0.1839 0.0255  0.1630  54  ILE C CG2 
6646  C  CD1 . ILE C 53  ? 0.5405 0.5850 0.7756 -0.1714 0.0385  0.1562  54  ILE C CD1 
6647  N  N   . SER C 54  ? 0.6016 0.6759 0.8867 -0.1783 0.0348  0.1465  55  SER C N   
6648  C  CA  . SER C 54  ? 0.5914 0.6856 0.8932 -0.1748 0.0374  0.1429  55  SER C CA  
6649  C  C   . SER C 54  ? 0.5510 0.6534 0.8519 -0.1664 0.0438  0.1406  55  SER C C   
6650  O  O   . SER C 54  ? 0.5119 0.6113 0.8027 -0.1677 0.0504  0.1425  55  SER C O   
6651  C  CB  . SER C 54  ? 0.5888 0.6974 0.9065 -0.1843 0.0427  0.1454  55  SER C CB  
6652  O  OG  . SER C 54  ? 0.6312 0.7398 0.9430 -0.1907 0.0522  0.1488  55  SER C OG  
6653  N  N   . GLY C 55  ? 0.5377 0.6500 0.8483 -0.1587 0.0415  0.1368  56  GLY C N   
6654  C  CA  . GLY C 55  ? 0.5952 0.7124 0.9043 -0.1496 0.0457  0.1340  56  GLY C CA  
6655  C  C   . GLY C 55  ? 0.5761 0.7123 0.9026 -0.1484 0.0549  0.1330  56  GLY C C   
6656  O  O   . GLY C 55  ? 0.5616 0.7037 0.8920 -0.1403 0.0567  0.1302  56  GLY C O   
6657  N  N   . GLU C 56  ? 0.5777 0.7233 0.9164 -0.1566 0.0613  0.1350  57  GLU C N   
6658  C  CA  . GLU C 56  ? 0.5776 0.7413 0.9365 -0.1560 0.0721  0.1334  57  GLU C CA  
6659  C  C   . GLU C 56  ? 0.5212 0.6826 0.8690 -0.1527 0.0826  0.1304  57  GLU C C   
6660  O  O   . GLU C 56  ? 0.5044 0.6786 0.8677 -0.1494 0.0919  0.1271  57  GLU C O   
6661  C  CB  . GLU C 56  ? 0.5976 0.7704 0.9704 -0.1667 0.0786  0.1358  57  GLU C CB  
6662  N  N   . HIS C 57  ? 0.4851 0.6297 0.8068 -0.1541 0.0807  0.1315  58  HIS C N   
6663  C  CA  . HIS C 57  ? 0.5501 0.6902 0.8566 -0.1530 0.0888  0.1294  58  HIS C CA  
6664  C  C   . HIS C 57  ? 0.5685 0.7050 0.8696 -0.1417 0.0839  0.1265  58  HIS C C   
6665  O  O   . HIS C 57  ? 0.5677 0.7000 0.8558 -0.1403 0.0892  0.1245  58  HIS C O   
6666  C  CB  . HIS C 57  ? 0.6133 0.7373 0.8947 -0.1615 0.0878  0.1338  58  HIS C CB  
6667  C  CG  . HIS C 57  ? 0.6649 0.7729 0.9331 -0.1580 0.0741  0.1371  58  HIS C CG  
6668  N  ND1 . HIS C 57  ? 0.6642 0.7670 0.9369 -0.1602 0.0652  0.1398  58  HIS C ND1 
6669  C  CD2 . HIS C 57  ? 0.6706 0.7666 0.9232 -0.1524 0.0682  0.1376  58  HIS C CD2 
6670  C  CE1 . HIS C 57  ? 0.6981 0.7860 0.9592 -0.1559 0.0555  0.1412  58  HIS C CE1 
6671  N  NE2 . HIS C 57  ? 0.6929 0.7771 0.9428 -0.1509 0.0569  0.1403  58  HIS C NE2 
6672  N  N   . LEU C 58  ? 0.5715 0.7095 0.8815 -0.1348 0.0740  0.1262  59  LEU C N   
6673  C  CA  . LEU C 58  ? 0.5993 0.7329 0.9029 -0.1250 0.0689  0.1238  59  LEU C CA  
6674  C  C   . LEU C 58  ? 0.6713 0.8184 0.9912 -0.1184 0.0749  0.1201  59  LEU C C   
6675  O  O   . LEU C 58  ? 0.6809 0.8405 1.0223 -0.1168 0.0736  0.1203  59  LEU C O   
6676  C  CB  . LEU C 58  ? 0.5751 0.7032 0.8786 -0.1217 0.0565  0.1244  59  LEU C CB  
6677  C  CG  . LEU C 58  ? 0.6210 0.7323 0.9086 -0.1251 0.0493  0.1267  59  LEU C CG  
6678  C  CD1 . LEU C 58  ? 0.6078 0.7159 0.8986 -0.1231 0.0397  0.1254  59  LEU C CD1 
6679  C  CD2 . LEU C 58  ? 0.5760 0.6752 0.8463 -0.1213 0.0487  0.1268  59  LEU C CD2 
6680  N  N   . ARG C 59  ? 0.6248 0.7691 0.9352 -0.1150 0.0810  0.1172  60  ARG C N   
6681  C  CA  . ARG C 59  ? 0.5964 0.7512 0.9218 -0.1082 0.0866  0.1133  60  ARG C CA  
6682  C  C   . ARG C 59  ? 0.5956 0.7507 0.9252 -0.0992 0.0767  0.1134  60  ARG C C   
6683  O  O   . ARG C 59  ? 0.6096 0.7759 0.9600 -0.0957 0.0749  0.1139  60  ARG C O   
6684  C  CB  . ARG C 59  ? 0.5938 0.7441 0.9057 -0.1086 0.0964  0.1095  60  ARG C CB  
6685  N  N   . ILE C 60  ? 0.5579 0.7006 0.8683 -0.0961 0.0702  0.1133  61  ILE C N   
6686  C  CA  . ILE C 60  ? 0.5054 0.6473 0.8166 -0.0884 0.0625  0.1126  61  ILE C CA  
6687  C  C   . ILE C 60  ? 0.4618 0.6025 0.7753 -0.0890 0.0519  0.1147  61  ILE C C   
6688  O  O   . ILE C 60  ? 0.4940 0.6419 0.8186 -0.0858 0.0473  0.1151  61  ILE C O   
6689  C  CB  . ILE C 60  ? 0.4919 0.6220 0.7838 -0.0847 0.0608  0.1111  61  ILE C CB  
6690  C  CG1 . ILE C 60  ? 0.4150 0.5456 0.7021 -0.0853 0.0707  0.1086  61  ILE C CG1 
6691  C  CG2 . ILE C 60  ? 0.3922 0.5220 0.6851 -0.0774 0.0544  0.1098  61  ILE C CG2 
6692  C  CD1 . ILE C 60  ? 0.4232 0.5422 0.6905 -0.0842 0.0685  0.1083  61  ILE C CD1 
6693  N  N   . CYS C 61  ? 0.4626 0.5935 0.7651 -0.0940 0.0478  0.1160  62  CYS C N   
6694  C  CA  . CYS C 61  ? 0.4792 0.6059 0.7802 -0.0954 0.0386  0.1163  62  CYS C CA  
6695  C  C   . CYS C 61  ? 0.5001 0.6378 0.8173 -0.1007 0.0364  0.1188  62  CYS C C   
6696  O  O   . CYS C 61  ? 0.5102 0.6560 0.8385 -0.1046 0.0426  0.1205  62  CYS C O   
6697  C  CB  . CYS C 61  ? 0.4194 0.5307 0.7055 -0.0987 0.0354  0.1166  62  CYS C CB  
6698  S  SG  . CYS C 61  ? 0.8729 0.9713 1.1429 -0.0932 0.0360  0.1153  62  CYS C SG  
6699  N  N   . PRO C 62  ? 0.5352 0.6735 0.8540 -0.1017 0.0279  0.1188  63  PRO C N   
6700  C  CA  . PRO C 62  ? 0.5716 0.7194 0.9047 -0.1084 0.0237  0.1219  63  PRO C CA  
6701  C  C   . PRO C 62  ? 0.5889 0.7319 0.9199 -0.1160 0.0258  0.1231  63  PRO C C   
6702  O  O   . PRO C 62  ? 0.6340 0.7622 0.9491 -0.1178 0.0241  0.1215  63  PRO C O   
6703  C  CB  . PRO C 62  ? 0.5452 0.6885 0.8707 -0.1100 0.0136  0.1208  63  PRO C CB  
6704  C  CG  . PRO C 62  ? 0.5565 0.6955 0.8725 -0.1022 0.0140  0.1180  63  PRO C CG  
6705  C  CD  . PRO C 62  ? 0.5496 0.6811 0.8576 -0.0977 0.0220  0.1161  63  PRO C CD  
6706  N  N   . GLN C 63  ? 0.6295 0.7848 0.9781 -0.1205 0.0297  0.1261  64  GLN C N   
6707  C  CA  . GLN C 63  ? 0.6544 0.8061 1.0015 -0.1284 0.0332  0.1277  64  GLN C CA  
6708  C  C   . GLN C 63  ? 0.6821 0.8268 1.0245 -0.1356 0.0241  0.1284  64  GLN C C   
6709  O  O   . GLN C 63  ? 0.7209 0.8740 1.0742 -0.1388 0.0170  0.1298  64  GLN C O   
6710  C  CB  . GLN C 63  ? 0.6567 0.8248 1.0259 -0.1317 0.0413  0.1300  64  GLN C CB  
6711  C  CG  . GLN C 63  ? 0.6257 0.7995 0.9992 -0.1255 0.0522  0.1278  64  GLN C CG  
6712  C  CD  . GLN C 63  ? 0.6579 0.8466 1.0536 -0.1293 0.0629  0.1285  64  GLN C CD  
6713  O  OE1 . GLN C 63  ? 0.6845 0.8841 1.0996 -0.1345 0.0606  0.1315  64  GLN C OE1 
6714  N  NE2 . GLN C 63  ? 0.6621 0.8515 1.0554 -0.1274 0.0753  0.1253  64  GLN C NE2 
6715  N  N   . GLY C 64  ? 0.6655 0.7940 0.9916 -0.1388 0.0239  0.1276  65  GLY C N   
6716  C  CA  . GLY C 64  ? 0.6688 0.7868 0.9885 -0.1456 0.0166  0.1270  65  GLY C CA  
6717  C  C   . GLY C 64  ? 0.6161 0.7166 0.9212 -0.1476 0.0187  0.1273  65  GLY C C   
6718  O  O   . GLY C 64  ? 0.5933 0.6920 0.8936 -0.1449 0.0250  0.1289  65  GLY C O   
6719  N  N   . TYR C 65  ? 0.6550 0.7419 0.9530 -0.1527 0.0130  0.1259  66  TYR C N   
6720  C  CA  . TYR C 65  ? 0.6623 0.7318 0.9495 -0.1548 0.0139  0.1275  66  TYR C CA  
6721  C  C   . TYR C 65  ? 0.6924 0.7507 0.9685 -0.1457 0.0143  0.1253  66  TYR C C   
6722  O  O   . TYR C 65  ? 0.6918 0.7455 0.9642 -0.1406 0.0110  0.1200  66  TYR C O   
6723  C  CB  . TYR C 65  ? 0.6413 0.6983 0.9262 -0.1627 0.0082  0.1261  66  TYR C CB  
6724  C  CG  . TYR C 65  ? 0.6153 0.6823 0.9112 -0.1730 0.0081  0.1298  66  TYR C CG  
6725  C  CD1 . TYR C 65  ? 0.6159 0.6845 0.9141 -0.1784 0.0135  0.1356  66  TYR C CD1 
6726  C  CD2 . TYR C 65  ? 0.6010 0.6768 0.9050 -0.1781 0.0027  0.1279  66  TYR C CD2 
6727  C  CE1 . TYR C 65  ? 0.6223 0.7012 0.9324 -0.1881 0.0144  0.1389  66  TYR C CE1 
6728  C  CE2 . TYR C 65  ? 0.6059 0.6922 0.9227 -0.1877 0.0023  0.1318  66  TYR C CE2 
6729  C  CZ  . TYR C 65  ? 0.6204 0.7085 0.9411 -0.1923 0.0087  0.1370  66  TYR C CZ  
6730  O  OH  . TYR C 65  ? 0.6267 0.7261 0.9616 -0.2021 0.0092  0.1407  66  TYR C OH  
6731  N  N   . THR C 66  ? 0.6648 0.7193 0.9355 -0.1447 0.0182  0.1295  67  THR C N   
6732  C  CA  . THR C 66  ? 0.6104 0.6583 0.8730 -0.1363 0.0187  0.1288  67  THR C CA  
6733  C  C   . THR C 66  ? 0.5560 0.5884 0.8100 -0.1384 0.0174  0.1341  67  THR C C   
6734  O  O   . THR C 66  ? 0.5168 0.5465 0.7694 -0.1468 0.0184  0.1396  67  THR C O   
6735  C  CB  . THR C 66  ? 0.5715 0.6342 0.8361 -0.1316 0.0248  0.1289  67  THR C CB  
6736  O  OG1 . THR C 66  ? 0.5387 0.5946 0.7948 -0.1243 0.0246  0.1285  67  THR C OG1 
6737  C  CG2 . THR C 66  ? 0.5565 0.6265 0.8224 -0.1387 0.0314  0.1337  67  THR C CG2 
6738  N  N   . CYS C 67  ? 0.5312 0.5537 0.7804 -0.1312 0.0147  0.1332  68  CYS C N   
6739  C  CA  . CYS C 67  ? 0.5364 0.5451 0.7790 -0.1323 0.0119  0.1397  68  CYS C CA  
6740  C  C   . CYS C 67  ? 0.5659 0.5814 0.8009 -0.1310 0.0154  0.1436  68  CYS C C   
6741  O  O   . CYS C 67  ? 0.5808 0.5866 0.8084 -0.1326 0.0123  0.1501  68  CYS C O   
6742  C  CB  . CYS C 67  ? 0.5406 0.5344 0.7857 -0.1256 0.0065  0.1371  68  CYS C CB  
6743  S  SG  . CYS C 67  ? 1.0711 1.0502 1.3226 -0.1295 0.0028  0.1331  68  CYS C SG  
6744  N  N   . CYS C 68  ? 0.5550 0.5866 0.7922 -0.1286 0.0214  0.1397  69  CYS C N   
6745  C  CA  . CYS C 68  ? 0.5684 0.6065 0.7983 -0.1275 0.0261  0.1413  69  CYS C CA  
6746  C  C   . CYS C 68  ? 0.5026 0.5495 0.7298 -0.1366 0.0339  0.1440  69  CYS C C   
6747  O  O   . CYS C 68  ? 0.4974 0.5556 0.7348 -0.1392 0.0383  0.1414  69  CYS C O   
6748  C  CB  . CYS C 68  ? 0.4797 0.5287 0.7147 -0.1183 0.0288  0.1347  69  CYS C CB  
6749  S  SG  . CYS C 68  ? 0.6558 0.6956 0.8908 -0.1079 0.0224  0.1315  69  CYS C SG  
6750  N  N   . THR C 69  ? 0.5148 0.5566 0.7285 -0.1423 0.0355  0.1495  70  THR C N   
6751  C  CA  . THR C 69  ? 0.5214 0.5720 0.7301 -0.1511 0.0453  0.1505  70  THR C CA  
6752  C  C   . THR C 69  ? 0.7169 0.7786 0.9255 -0.1459 0.0529  0.1448  70  THR C C   
6753  O  O   . THR C 69  ? 0.4981 0.5605 0.7102 -0.1359 0.0493  0.1412  70  THR C O   
6754  C  CB  . THR C 69  ? 0.5667 0.6056 0.7573 -0.1622 0.0439  0.1591  70  THR C CB  
6755  O  OG1 . THR C 69  ? 0.5672 0.5969 0.7461 -0.1589 0.0376  0.1624  70  THR C OG1 
6756  C  CG2 . THR C 69  ? 0.5558 0.5830 0.7482 -0.1678 0.0368  0.1652  70  THR C CG2 
6757  N  N   . SER C 70  ? 0.6938 0.7638 0.8989 -0.1529 0.0640  0.1435  71  SER C N   
6758  C  CA  . SER C 70  ? 0.6988 0.7787 0.9053 -0.1487 0.0727  0.1372  71  SER C CA  
6759  C  C   . SER C 70  ? 0.6538 0.7247 0.8432 -0.1464 0.0684  0.1386  71  SER C C   
6760  O  O   . SER C 70  ? 0.7054 0.7803 0.8990 -0.1374 0.0684  0.1339  71  SER C O   
6761  C  CB  . SER C 70  ? 0.7514 0.8404 0.9575 -0.1583 0.0872  0.1347  71  SER C CB  
6762  O  OG  . SER C 70  ? 0.8110 0.9134 1.0310 -0.1522 0.0967  0.1269  71  SER C OG  
6763  N  N   . GLU C 71  ? 0.6431 0.7016 0.8138 -0.1552 0.0638  0.1460  72  GLU C N   
6764  C  CA  . GLU C 71  ? 0.6808 0.7295 0.8358 -0.1545 0.0566  0.1498  72  GLU C CA  
6765  C  C   . GLU C 71  ? 0.6289 0.6748 0.7948 -0.1413 0.0467  0.1486  72  GLU C C   
6766  O  O   . GLU C 71  ? 0.6152 0.6627 0.7790 -0.1352 0.0459  0.1457  72  GLU C O   
6767  C  CB  . GLU C 71  ? 0.7071 0.7417 0.8444 -0.1658 0.0492  0.1606  72  GLU C CB  
6768  C  CG  . GLU C 71  ? 0.7779 0.8110 0.8921 -0.1801 0.0568  0.1628  72  GLU C CG  
6769  C  CD  . GLU C 71  ? 0.8571 0.8768 0.9549 -0.1930 0.0492  0.1748  72  GLU C CD  
6770  O  OE1 . GLU C 71  ? 0.9042 0.9200 1.0120 -0.1934 0.0448  0.1789  72  GLU C OE1 
6771  O  OE2 . GLU C 71  ? 0.9247 0.9371 0.9992 -0.2034 0.0470  0.1806  72  GLU C OE2 
6772  N  N   . MET C 72  ? 0.6292 0.6708 0.8066 -0.1377 0.0398  0.1504  73  MET C N   
6773  C  CA  . MET C 72  ? 0.6073 0.6454 0.7954 -0.1264 0.0318  0.1484  73  MET C CA  
6774  C  C   . MET C 72  ? 0.5472 0.5975 0.7461 -0.1170 0.0369  0.1396  73  MET C C   
6775  O  O   . MET C 72  ? 0.5288 0.5780 0.7296 -0.1089 0.0331  0.1375  73  MET C O   
6776  C  CB  . MET C 72  ? 0.6296 0.6607 0.8274 -0.1260 0.0260  0.1501  73  MET C CB  
6777  C  CG  . MET C 72  ? 0.6569 0.6731 0.8471 -0.1334 0.0184  0.1597  73  MET C CG  
6778  S  SD  . MET C 72  ? 0.6001 0.6076 0.8027 -0.1339 0.0135  0.1602  73  MET C SD  
6779  C  CE  . MET C 72  ? 0.5528 0.5566 0.7683 -0.1202 0.0082  0.1537  73  MET C CE  
6780  N  N   . GLU C 73  ? 0.5761 0.6381 0.7835 -0.1182 0.0450  0.1352  74  GLU C N   
6781  C  CA  . GLU C 73  ? 0.6292 0.7028 0.8485 -0.1100 0.0489  0.1284  74  GLU C CA  
6782  C  C   . GLU C 73  ? 0.6023 0.6789 0.8146 -0.1076 0.0536  0.1257  74  GLU C C   
6783  O  O   . GLU C 73  ? 0.6506 0.7293 0.8671 -0.0991 0.0515  0.1224  74  GLU C O   
6784  C  CB  . GLU C 73  ? 0.5857 0.6717 0.8185 -0.1125 0.0558  0.1257  74  GLU C CB  
6785  C  CG  . GLU C 73  ? 0.5588 0.6524 0.8070 -0.1049 0.0529  0.1218  74  GLU C CG  
6786  C  CD  . GLU C 73  ? 0.5113 0.6200 0.7761 -0.1059 0.0598  0.1195  74  GLU C CD  
6787  O  OE1 . GLU C 73  ? 0.5532 0.6678 0.8189 -0.1097 0.0694  0.1185  74  GLU C OE1 
6788  O  OE2 . GLU C 73  ? 0.4465 0.5611 0.7240 -0.1033 0.0557  0.1187  74  GLU C OE2 
6789  N  N   . GLU C 74  ? 0.7231 0.7994 0.9236 -0.1159 0.0603  0.1270  75  GLU C N   
6790  C  CA  . GLU C 74  ? 0.7548 0.8325 0.9463 -0.1154 0.0653  0.1238  75  GLU C CA  
6791  C  C   . GLU C 74  ? 0.7151 0.7835 0.8973 -0.1115 0.0554  0.1270  75  GLU C C   
6792  O  O   . GLU C 74  ? 0.7198 0.7912 0.9043 -0.1047 0.0556  0.1230  75  GLU C O   
6793  C  CB  . GLU C 74  ? 0.8375 0.9147 1.0144 -0.1274 0.0746  0.1242  75  GLU C CB  
6794  C  CG  . GLU C 74  ? 0.9516 1.0393 1.1405 -0.1316 0.0863  0.1204  75  GLU C CG  
6795  C  CD  . GLU C 74  ? 1.0575 1.1465 1.2335 -0.1425 0.0995  0.1174  75  GLU C CD  
6796  O  OE1 . GLU C 74  ? 1.0936 1.1773 1.2525 -0.1454 0.1008  0.1161  75  GLU C OE1 
6797  O  OE2 . GLU C 74  ? 1.0758 1.1714 1.2589 -0.1489 0.1090  0.1158  75  GLU C OE2 
6798  N  N   . ASN C 75  ? 0.6456 0.7030 0.8196 -0.1157 0.0464  0.1345  76  ASN C N   
6799  C  CA  . ASN C 75  ? 0.5901 0.6388 0.7593 -0.1121 0.0360  0.1387  76  ASN C CA  
6800  C  C   . ASN C 75  ? 0.6052 0.6562 0.7899 -0.0997 0.0318  0.1346  76  ASN C C   
6801  O  O   . ASN C 75  ? 0.5788 0.6299 0.7631 -0.0945 0.0293  0.1332  76  ASN C O   
6802  C  CB  . ASN C 75  ? 0.5509 0.5872 0.7138 -0.1183 0.0264  0.1484  76  ASN C CB  
6803  C  CG  . ASN C 75  ? 0.5965 0.6278 0.7382 -0.1318 0.0275  0.1545  76  ASN C CG  
6804  O  OD1 . ASN C 75  ? 0.6482 0.6835 0.7780 -0.1360 0.0340  0.1513  76  ASN C OD1 
6805  N  ND2 . ASN C 75  ? 0.5605 0.5821 0.6967 -0.1394 0.0211  0.1634  76  ASN C ND2 
6806  N  N   . LEU C 76  ? 0.6034 0.6559 0.8006 -0.0960 0.0313  0.1325  77  LEU C N   
6807  C  CA  . LEU C 76  ? 0.5699 0.6239 0.7794 -0.0861 0.0283  0.1280  77  LEU C CA  
6808  C  C   . LEU C 76  ? 0.5892 0.6540 0.8031 -0.0805 0.0343  0.1215  77  LEU C C   
6809  O  O   . LEU C 76  ? 0.5940 0.6592 0.8118 -0.0734 0.0319  0.1189  77  LEU C O   
6810  C  CB  . LEU C 76  ? 0.5509 0.6036 0.7697 -0.0859 0.0270  0.1267  77  LEU C CB  
6811  C  CG  . LEU C 76  ? 0.4864 0.5261 0.7049 -0.0890 0.0198  0.1321  77  LEU C CG  
6812  C  CD1 . LEU C 76  ? 0.5264 0.5650 0.7524 -0.0907 0.0199  0.1300  77  LEU C CD1 
6813  C  CD2 . LEU C 76  ? 0.4601 0.4918 0.6829 -0.0824 0.0132  0.1327  77  LEU C CD2 
6814  N  N   . ALA C 77  ? 0.5536 0.6271 0.7683 -0.0838 0.0424  0.1192  78  ALA C N   
6815  C  CA  . ALA C 77  ? 0.5113 0.5943 0.7317 -0.0790 0.0484  0.1139  78  ALA C CA  
6816  C  C   . ALA C 77  ? 0.4596 0.5398 0.6708 -0.0776 0.0481  0.1134  78  ALA C C   
6817  O  O   . ALA C 77  ? 0.4822 0.5646 0.6979 -0.0707 0.0467  0.1105  78  ALA C O   
6818  C  CB  . ALA C 77  ? 0.4993 0.5912 0.7245 -0.0834 0.0579  0.1118  78  ALA C CB  
6819  N  N   . ASN C 78  ? 0.4807 0.5557 0.6777 -0.0854 0.0491  0.1166  79  ASN C N   
6820  C  CA  . ASN C 78  ? 0.5253 0.5966 0.7108 -0.0866 0.0474  0.1172  79  ASN C CA  
6821  C  C   . ASN C 78  ? 0.5732 0.6400 0.7628 -0.0796 0.0378  0.1192  79  ASN C C   
6822  O  O   . ASN C 78  ? 0.6231 0.6921 0.8135 -0.0751 0.0377  0.1164  79  ASN C O   
6823  C  CB  . ASN C 78  ? 0.5817 0.6457 0.7489 -0.0981 0.0467  0.1226  79  ASN C CB  
6824  C  CG  . ASN C 78  ? 0.6421 0.7060 0.7948 -0.1036 0.0518  0.1200  79  ASN C CG  
6825  O  OD1 . ASN C 78  ? 0.7346 0.8042 0.8866 -0.1063 0.0634  0.1137  79  ASN C OD1 
6826  N  ND2 . ASN C 78  ? 0.6190 0.6761 0.7609 -0.1058 0.0431  0.1247  79  ASN C ND2 
6827  N  N   . ARG C 79  ? 0.5872 0.6479 0.7813 -0.0787 0.0305  0.1235  80  ARG C N   
6828  C  CA  . ARG C 79  ? 0.5853 0.6414 0.7868 -0.0722 0.0224  0.1250  80  ARG C CA  
6829  C  C   . ARG C 79  ? 0.5328 0.5953 0.7456 -0.0632 0.0251  0.1183  80  ARG C C   
6830  O  O   . ARG C 79  ? 0.5975 0.6610 0.8123 -0.0588 0.0232  0.1170  80  ARG C O   
6831  C  CB  . ARG C 79  ? 0.5435 0.5912 0.7504 -0.0730 0.0161  0.1296  80  ARG C CB  
6832  C  CG  . ARG C 79  ? 0.5391 0.5811 0.7569 -0.0664 0.0087  0.1308  80  ARG C CG  
6833  C  CD  . ARG C 79  ? 0.5797 0.6207 0.7939 -0.0664 0.0036  0.1346  80  ARG C CD  
6834  N  NE  . ARG C 79  ? 0.5904 0.6272 0.7892 -0.0762 0.0001  0.1421  80  ARG C NE  
6835  C  CZ  . ARG C 79  ? 0.6727 0.7003 0.8704 -0.0807 -0.0095 0.1516  80  ARG C CZ  
6836  N  NH1 . ARG C 79  ? 0.6969 0.7185 0.9111 -0.0749 -0.0159 0.1540  80  ARG C NH1 
6837  N  NH2 . ARG C 79  ? 0.6973 0.7211 0.8774 -0.0914 -0.0124 0.1586  80  ARG C NH2 
6838  N  N   . SER C 80  ? 0.5307 0.5977 0.7506 -0.0613 0.0289  0.1145  81  SER C N   
6839  C  CA  . SER C 80  ? 0.4767 0.5492 0.7052 -0.0545 0.0306  0.1091  81  SER C CA  
6840  C  C   . SER C 80  ? 0.4906 0.5699 0.7178 -0.0521 0.0350  0.1062  81  SER C C   
6841  O  O   . SER C 80  ? 0.4601 0.5410 0.6911 -0.0468 0.0342  0.1037  81  SER C O   
6842  C  CB  . SER C 80  ? 0.4151 0.4918 0.6495 -0.0552 0.0329  0.1069  81  SER C CB  
6843  O  OG  . SER C 80  ? 0.4176 0.4997 0.6508 -0.0599 0.0379  0.1077  81  SER C OG  
6844  N  N   . HIS C 81  ? 0.4917 0.5745 0.7139 -0.0566 0.0405  0.1062  82  HIS C N   
6845  C  CA  . HIS C 81  ? 0.5210 0.6085 0.7419 -0.0552 0.0456  0.1030  82  HIS C CA  
6846  C  C   . HIS C 81  ? 0.5345 0.6176 0.7491 -0.0542 0.0414  0.1040  82  HIS C C   
6847  O  O   . HIS C 81  ? 0.4968 0.5827 0.7157 -0.0491 0.0416  0.1012  82  HIS C O   
6848  C  CB  . HIS C 81  ? 0.5046 0.5944 0.7203 -0.0616 0.0533  0.1021  82  HIS C CB  
6849  C  CG  . HIS C 81  ? 0.5780 0.6710 0.7926 -0.0610 0.0598  0.0977  82  HIS C CG  
6850  N  ND1 . HIS C 81  ? 0.6091 0.7096 0.8363 -0.0569 0.0659  0.0939  82  HIS C ND1 
6851  C  CD2 . HIS C 81  ? 0.5758 0.6649 0.7786 -0.0644 0.0609  0.0968  82  HIS C CD2 
6852  C  CE1 . HIS C 81  ? 0.5880 0.6886 0.8123 -0.0572 0.0713  0.0901  82  HIS C CE1 
6853  N  NE2 . HIS C 81  ? 0.5720 0.6657 0.7804 -0.0621 0.0686  0.0914  82  HIS C NE2 
6854  N  N   . ALA C 82  ? 0.5412 0.6176 0.7460 -0.0597 0.0370  0.1087  83  ALA C N   
6855  C  CA  . ALA C 82  ? 0.6144 0.6869 0.8142 -0.0600 0.0311  0.1113  83  ALA C CA  
6856  C  C   . ALA C 82  ? 0.6292 0.7020 0.8410 -0.0520 0.0262  0.1106  83  ALA C C   
6857  O  O   . ALA C 82  ? 0.6756 0.7500 0.8888 -0.0494 0.0249  0.1094  83  ALA C O   
6858  C  CB  . ALA C 82  ? 0.6113 0.6761 0.8007 -0.0676 0.0246  0.1185  83  ALA C CB  
6859  N  N   . GLU C 83  ? 0.6411 0.7122 0.8617 -0.0489 0.0242  0.1108  84  GLU C N   
6860  C  CA  . GLU C 83  ? 0.6339 0.7046 0.8660 -0.0422 0.0215  0.1087  84  GLU C CA  
6861  C  C   . GLU C 83  ? 0.6018 0.6795 0.8377 -0.0374 0.0266  0.1030  84  GLU C C   
6862  O  O   . GLU C 83  ? 0.6320 0.7109 0.8729 -0.0336 0.0255  0.1015  84  GLU C O   
6863  C  CB  . GLU C 83  ? 0.6900 0.7565 0.9288 -0.0412 0.0202  0.1085  84  GLU C CB  
6864  C  CG  . GLU C 83  ? 0.7820 0.8399 1.0203 -0.0450 0.0137  0.1151  84  GLU C CG  
6865  C  CD  . GLU C 83  ? 0.8346 0.8871 1.0790 -0.0448 0.0133  0.1143  84  GLU C CD  
6866  O  OE1 . GLU C 83  ? 0.8496 0.8940 1.1005 -0.0447 0.0076  0.1183  84  GLU C OE1 
6867  O  OE2 . GLU C 83  ? 0.8221 0.8783 1.0657 -0.0450 0.0181  0.1099  84  GLU C OE2 
6868  N  N   . LEU C 84  ? 0.5338 0.6163 0.7686 -0.0380 0.0319  0.1003  85  LEU C N   
6869  C  CA  . LEU C 84  ? 0.5078 0.5964 0.7463 -0.0343 0.0357  0.0964  85  LEU C CA  
6870  C  C   . LEU C 84  ? 0.5221 0.6125 0.7576 -0.0339 0.0370  0.0958  85  LEU C C   
6871  O  O   . LEU C 84  ? 0.5084 0.6008 0.7477 -0.0303 0.0370  0.0938  85  LEU C O   
6872  C  CB  . LEU C 84  ? 0.4683 0.5620 0.7087 -0.0356 0.0398  0.0954  85  LEU C CB  
6873  C  CG  . LEU C 84  ? 0.4441 0.5438 0.6894 -0.0323 0.0423  0.0931  85  LEU C CG  
6874  C  CD1 . LEU C 84  ? 0.3897 0.4884 0.6369 -0.0294 0.0399  0.0912  85  LEU C CD1 
6875  C  CD2 . LEU C 84  ? 0.4177 0.5229 0.6685 -0.0336 0.0446  0.0936  85  LEU C CD2 
6876  N  N   . GLU C 85  ? 0.5702 0.6593 0.7978 -0.0386 0.0385  0.0972  86  GLU C N   
6877  C  CA  . GLU C 85  ? 0.6287 0.7182 0.8514 -0.0397 0.0399  0.0960  86  GLU C CA  
6878  C  C   . GLU C 85  ? 0.6265 0.7135 0.8504 -0.0382 0.0335  0.0980  86  GLU C C   
6879  O  O   . GLU C 85  ? 0.6670 0.7562 0.8926 -0.0363 0.0341  0.0961  86  GLU C O   
6880  C  CB  . GLU C 85  ? 0.7451 0.8320 0.9562 -0.0470 0.0430  0.0966  86  GLU C CB  
6881  C  CG  . GLU C 85  ? 0.8371 0.9281 1.0503 -0.0479 0.0520  0.0927  86  GLU C CG  
6882  C  CD  . GLU C 85  ? 0.9335 1.0218 1.1346 -0.0556 0.0577  0.0909  86  GLU C CD  
6883  O  OE1 . GLU C 85  ? 0.9659 1.0487 1.1539 -0.0620 0.0534  0.0942  86  GLU C OE1 
6884  O  OE2 . GLU C 85  ? 0.9477 1.0390 1.1527 -0.0559 0.0666  0.0862  86  GLU C OE2 
6885  N  N   . THR C 86  ? 0.5690 0.6518 0.7943 -0.0391 0.0273  0.1022  87  THR C N   
6886  C  CA  . THR C 86  ? 0.5308 0.6120 0.7624 -0.0371 0.0207  0.1048  87  THR C CA  
6887  C  C   . THR C 86  ? 0.5151 0.6002 0.7587 -0.0304 0.0227  0.1007  87  THR C C   
6888  O  O   . THR C 86  ? 0.5084 0.5960 0.7556 -0.0288 0.0217  0.1000  87  THR C O   
6889  C  CB  . THR C 86  ? 0.4627 0.5380 0.6980 -0.0384 0.0136  0.1105  87  THR C CB  
6890  O  OG1 . THR C 86  ? 0.5257 0.5968 0.7481 -0.0463 0.0096  0.1159  87  THR C OG1 
6891  C  CG2 . THR C 86  ? 0.4326 0.5075 0.6821 -0.0341 0.0078  0.1123  87  THR C CG2 
6892  N  N   . ALA C 87  ? 0.5244 0.6099 0.7728 -0.0274 0.0258  0.0979  88  ALA C N   
6893  C  CA  . ALA C 87  ? 0.5342 0.6228 0.7909 -0.0228 0.0287  0.0934  88  ALA C CA  
6894  C  C   . ALA C 87  ? 0.5232 0.6169 0.7772 -0.0221 0.0326  0.0910  88  ALA C C   
6895  O  O   . ALA C 87  ? 0.5491 0.6452 0.8085 -0.0198 0.0331  0.0893  88  ALA C O   
6896  C  CB  . ALA C 87  ? 0.3616 0.4493 0.6192 -0.0222 0.0315  0.0906  88  ALA C CB  
6897  N  N   . LEU C 88  ? 0.4833 0.5785 0.7304 -0.0242 0.0356  0.0909  89  LEU C N   
6898  C  CA  . LEU C 88  ? 0.4544 0.5532 0.7004 -0.0236 0.0393  0.0890  89  LEU C CA  
6899  C  C   . LEU C 88  ? 0.4422 0.5407 0.6871 -0.0244 0.0376  0.0894  89  LEU C C   
6900  O  O   . LEU C 88  ? 0.4938 0.5949 0.7425 -0.0225 0.0388  0.0877  89  LEU C O   
6901  C  CB  . LEU C 88  ? 0.4501 0.5500 0.6923 -0.0258 0.0431  0.0889  89  LEU C CB  
6902  C  CG  . LEU C 88  ? 0.4753 0.5785 0.7219 -0.0245 0.0453  0.0885  89  LEU C CG  
6903  C  CD1 . LEU C 88  ? 0.4730 0.5776 0.7198 -0.0267 0.0488  0.0889  89  LEU C CD1 
6904  C  CD2 . LEU C 88  ? 0.4576 0.5639 0.7082 -0.0220 0.0467  0.0875  89  LEU C CD2 
6905  N  N   . ARG C 89  ? 0.4961 0.5914 0.7350 -0.0284 0.0343  0.0919  90  ARG C N   
6906  C  CA  . ARG C 89  ? 0.5487 0.6434 0.7849 -0.0308 0.0313  0.0929  90  ARG C CA  
6907  C  C   . ARG C 89  ? 0.5785 0.6753 0.8259 -0.0275 0.0271  0.0938  90  ARG C C   
6908  O  O   . ARG C 89  ? 0.6173 0.7162 0.8669 -0.0276 0.0265  0.0931  90  ARG C O   
6909  C  CB  . ARG C 89  ? 0.5983 0.6884 0.8238 -0.0374 0.0271  0.0966  90  ARG C CB  
6910  C  CG  . ARG C 89  ? 0.7415 0.8300 0.9556 -0.0432 0.0293  0.0947  90  ARG C CG  
6911  C  CD  . ARG C 89  ? 0.8291 0.9125 1.0292 -0.0518 0.0248  0.0986  90  ARG C CD  
6912  N  NE  . ARG C 89  ? 0.9320 1.0131 1.1292 -0.0532 0.0249  0.1011  90  ARG C NE  
6913  C  CZ  . ARG C 89  ? 0.9665 1.0439 1.1608 -0.0569 0.0169  0.1077  90  ARG C CZ  
6914  N  NH1 . ARG C 89  ? 0.9733 1.0493 1.1685 -0.0593 0.0074  0.1129  90  ARG C NH1 
6915  N  NH2 . ARG C 89  ? 0.9607 1.0355 1.1524 -0.0585 0.0177  0.1097  90  ARG C NH2 
6916  N  N   . ASP C 90  ? 0.5704 0.6664 0.8261 -0.0246 0.0249  0.0950  91  ASP C N   
6917  C  CA  . ASP C 90  ? 0.5430 0.6412 0.8128 -0.0209 0.0229  0.0947  91  ASP C CA  
6918  C  C   . ASP C 90  ? 0.5211 0.6239 0.7947 -0.0181 0.0290  0.0898  91  ASP C C   
6919  O  O   . ASP C 90  ? 0.5023 0.6084 0.7825 -0.0175 0.0283  0.0895  91  ASP C O   
6920  C  CB  . ASP C 90  ? 0.6084 0.7038 0.8872 -0.0183 0.0216  0.0951  91  ASP C CB  
6921  C  CG  . ASP C 90  ? 0.7178 0.8081 0.9953 -0.0213 0.0141  0.1014  91  ASP C CG  
6922  O  OD1 . ASP C 90  ? 0.7152 0.8051 0.9877 -0.0254 0.0084  0.1059  91  ASP C OD1 
6923  O  OD2 . ASP C 90  ? 0.7052 0.7913 0.9857 -0.0205 0.0135  0.1020  91  ASP C OD2 
6924  N  N   . SER C 91  ? 0.4745 0.5776 0.7438 -0.0171 0.0342  0.0869  92  SER C N   
6925  C  CA  . SER C 91  ? 0.5080 0.6146 0.7783 -0.0158 0.0393  0.0835  92  SER C CA  
6926  C  C   . SER C 91  ? 0.4408 0.5493 0.7080 -0.0172 0.0398  0.0839  92  SER C C   
6927  O  O   . SER C 91  ? 0.4117 0.5231 0.6844 -0.0166 0.0410  0.0827  92  SER C O   
6928  C  CB  . SER C 91  ? 0.5180 0.6241 0.7822 -0.0162 0.0426  0.0822  92  SER C CB  
6929  O  OG  . SER C 91  ? 0.5915 0.6959 0.8585 -0.0156 0.0435  0.0801  92  SER C OG  
6930  N  N   . SER C 92  ? 0.4144 0.5208 0.6735 -0.0195 0.0397  0.0851  93  SER C N   
6931  C  CA  . SER C 92  ? 0.4534 0.5599 0.7091 -0.0213 0.0411  0.0845  93  SER C CA  
6932  C  C   . SER C 92  ? 0.4628 0.5701 0.7214 -0.0229 0.0373  0.0853  93  SER C C   
6933  O  O   . SER C 92  ? 0.4647 0.5736 0.7252 -0.0234 0.0388  0.0841  93  SER C O   
6934  C  CB  . SER C 92  ? 0.4740 0.5773 0.7213 -0.0241 0.0428  0.0844  93  SER C CB  
6935  O  OG  . SER C 92  ? 0.5138 0.6156 0.7577 -0.0265 0.0447  0.0827  93  SER C OG  
6936  N  N   . ARG C 93  ? 0.4610 0.5673 0.7211 -0.0242 0.0316  0.0881  94  ARG C N   
6937  C  CA  . ARG C 93  ? 0.4538 0.5614 0.7182 -0.0266 0.0260  0.0903  94  ARG C CA  
6938  C  C   . ARG C 93  ? 0.4195 0.5324 0.6995 -0.0229 0.0262  0.0896  94  ARG C C   
6939  O  O   . ARG C 93  ? 0.4401 0.5560 0.7256 -0.0244 0.0238  0.0902  94  ARG C O   
6940  C  CB  . ARG C 93  ? 0.5354 0.6400 0.7972 -0.0299 0.0182  0.0952  94  ARG C CB  
6941  C  CG  . ARG C 93  ? 0.6788 0.7801 0.9272 -0.0374 0.0145  0.0969  94  ARG C CG  
6942  C  CD  . ARG C 93  ? 0.7965 0.8926 1.0334 -0.0423 0.0106  0.1006  94  ARG C CD  
6943  N  NE  . ARG C 93  ? 0.8952 0.9914 1.1429 -0.0394 0.0048  0.1054  94  ARG C NE  
6944  C  CZ  . ARG C 93  ? 0.9528 1.0446 1.1943 -0.0441 -0.0021 0.1113  94  ARG C CZ  
6945  N  NH1 . ARG C 93  ? 0.9833 1.0706 1.2057 -0.0528 -0.0035 0.1126  94  ARG C NH1 
6946  N  NH2 . ARG C 93  ? 0.9611 1.0523 1.2154 -0.0407 -0.0071 0.1156  94  ARG C NH2 
6947  N  N   . VAL C 94  ? 0.3784 0.4924 0.6655 -0.0188 0.0297  0.0877  95  VAL C N   
6948  C  CA  . VAL C 94  ? 0.3986 0.5174 0.6992 -0.0160 0.0331  0.0851  95  VAL C CA  
6949  C  C   . VAL C 94  ? 0.4303 0.5514 0.7267 -0.0172 0.0381  0.0826  95  VAL C C   
6950  O  O   . VAL C 94  ? 0.4476 0.5730 0.7525 -0.0178 0.0382  0.0823  95  VAL C O   
6951  C  CB  . VAL C 94  ? 0.4401 0.5582 0.7454 -0.0129 0.0377  0.0818  95  VAL C CB  
6952  C  CG1 . VAL C 94  ? 0.3408 0.4634 0.6554 -0.0117 0.0444  0.0774  95  VAL C CG1 
6953  C  CG2 . VAL C 94  ? 0.3740 0.4897 0.6888 -0.0112 0.0328  0.0842  95  VAL C CG2 
6954  N  N   . LEU C 95  ? 0.4619 0.5803 0.7467 -0.0177 0.0417  0.0816  96  LEU C N   
6955  C  CA  . LEU C 95  ? 0.4134 0.5327 0.6944 -0.0190 0.0456  0.0805  96  LEU C CA  
6956  C  C   . LEU C 95  ? 0.3754 0.4946 0.6561 -0.0218 0.0430  0.0815  96  LEU C C   
6957  O  O   . LEU C 95  ? 0.3552 0.4773 0.6408 -0.0228 0.0447  0.0808  96  LEU C O   
6958  C  CB  . LEU C 95  ? 0.4339 0.5499 0.7053 -0.0191 0.0480  0.0808  96  LEU C CB  
6959  C  CG  . LEU C 95  ? 0.3823 0.4984 0.6515 -0.0202 0.0514  0.0810  96  LEU C CG  
6960  C  CD1 . LEU C 95  ? 0.3753 0.4948 0.6481 -0.0207 0.0545  0.0798  96  LEU C CD1 
6961  C  CD2 . LEU C 95  ? 0.3644 0.4780 0.6283 -0.0198 0.0523  0.0825  96  LEU C CD2 
6962  N  N   . GLN C 96  ? 0.4220 0.5376 0.6959 -0.0240 0.0393  0.0828  97  GLN C N   
6963  C  CA  . GLN C 96  ? 0.4579 0.5720 0.7284 -0.0283 0.0363  0.0831  97  GLN C CA  
6964  C  C   . GLN C 96  ? 0.4396 0.5588 0.7215 -0.0292 0.0319  0.0846  97  GLN C C   
6965  O  O   . GLN C 96  ? 0.4583 0.5787 0.7417 -0.0320 0.0318  0.0841  97  GLN C O   
6966  C  CB  . GLN C 96  ? 0.5818 0.6910 0.8415 -0.0320 0.0328  0.0842  97  GLN C CB  
6967  C  CG  . GLN C 96  ? 0.6849 0.7893 0.9347 -0.0322 0.0381  0.0820  97  GLN C CG  
6968  C  CD  . GLN C 96  ? 0.7996 0.8995 1.0380 -0.0370 0.0357  0.0826  97  GLN C CD  
6969  O  OE1 . GLN C 96  ? 0.8617 0.9605 1.0956 -0.0422 0.0298  0.0846  97  GLN C OE1 
6970  N  NE2 . GLN C 96  ? 0.8517 0.9491 1.0851 -0.0363 0.0401  0.0814  97  GLN C NE2 
6971  N  N   . ALA C 97  ? 0.4284 0.5507 0.7204 -0.0269 0.0283  0.0867  98  ALA C N   
6972  C  CA  . ALA C 97  ? 0.4393 0.5677 0.7476 -0.0269 0.0240  0.0886  98  ALA C CA  
6973  C  C   . ALA C 97  ? 0.4496 0.5832 0.7671 -0.0255 0.0305  0.0855  98  ALA C C   
6974  O  O   . ALA C 97  ? 0.4143 0.5518 0.7386 -0.0283 0.0285  0.0861  98  ALA C O   
6975  C  CB  . ALA C 97  ? 0.3723 0.5025 0.6934 -0.0235 0.0204  0.0909  98  ALA C CB  
6976  N  N   . MET C 98  ? 0.4092 0.5427 0.7257 -0.0224 0.0380  0.0823  99  MET C N   
6977  C  CA  . MET C 98  ? 0.4263 0.5639 0.7481 -0.0225 0.0449  0.0795  99  MET C CA  
6978  C  C   . MET C 98  ? 0.3939 0.5300 0.7082 -0.0263 0.0455  0.0799  99  MET C C   
6979  O  O   . MET C 98  ? 0.3849 0.5256 0.7080 -0.0284 0.0464  0.0796  99  MET C O   
6980  C  CB  . MET C 98  ? 0.3460 0.4819 0.6618 -0.0207 0.0519  0.0766  99  MET C CB  
6981  C  CG  . MET C 98  ? 0.3600 0.4999 0.6800 -0.0221 0.0596  0.0735  99  MET C CG  
6982  S  SD  . MET C 98  ? 0.6363 0.7732 0.9428 -0.0261 0.0623  0.0750  99  MET C SD  
6983  C  CE  . MET C 98  ? 0.4264 0.5568 0.7173 -0.0251 0.0622  0.0761  99  MET C CE  
6984  N  N   . LEU C 99  ? 0.4183 0.5478 0.7182 -0.0272 0.0454  0.0803  100 LEU C N   
6985  C  CA  . LEU C 99  ? 0.4031 0.5292 0.6968 -0.0305 0.0466  0.0801  100 LEU C CA  
6986  C  C   . LEU C 99  ? 0.4128 0.5399 0.7097 -0.0346 0.0415  0.0808  100 LEU C C   
6987  O  O   . LEU C 99  ? 0.3673 0.4950 0.6665 -0.0375 0.0430  0.0804  100 LEU C O   
6988  C  CB  . LEU C 99  ? 0.4260 0.5448 0.7075 -0.0302 0.0477  0.0800  100 LEU C CB  
6989  C  CG  . LEU C 99  ? 0.4415 0.5593 0.7197 -0.0273 0.0517  0.0804  100 LEU C CG  
6990  C  CD1 . LEU C 99  ? 0.4032 0.5153 0.6739 -0.0266 0.0521  0.0806  100 LEU C CD1 
6991  C  CD2 . LEU C 99  ? 0.3904 0.5094 0.6702 -0.0286 0.0555  0.0811  100 LEU C CD2 
6992  N  N   . ALA C 100 ? 0.4053 0.5321 0.7017 -0.0357 0.0350  0.0824  101 ALA C N   
6993  C  CA  . ALA C 100 ? 0.4179 0.5457 0.7159 -0.0411 0.0283  0.0839  101 ALA C CA  
6994  C  C   . ALA C 100 ? 0.4705 0.6073 0.7869 -0.0412 0.0270  0.0851  101 ALA C C   
6995  O  O   . ALA C 100 ? 0.4762 0.6144 0.7951 -0.0457 0.0256  0.0850  101 ALA C O   
6996  C  CB  . ALA C 100 ? 0.3947 0.5207 0.6882 -0.0431 0.0204  0.0868  101 ALA C CB  
6997  N  N   . THR C 101 ? 0.3954 0.5383 0.7257 -0.0364 0.0283  0.0856  102 THR C N   
6998  C  CA  . THR C 101 ? 0.3478 0.5002 0.6992 -0.0357 0.0292  0.0858  102 THR C CA  
6999  C  C   . THR C 101 ? 0.3650 0.5190 0.7163 -0.0377 0.0367  0.0831  102 THR C C   
7000  O  O   . THR C 101 ? 0.3491 0.5081 0.7102 -0.0414 0.0348  0.0839  102 THR C O   
7001  C  CB  . THR C 101 ? 0.4076 0.5645 0.7734 -0.0299 0.0329  0.0846  102 THR C CB  
7002  O  OG1 . THR C 101 ? 0.4297 0.5860 0.8006 -0.0285 0.0244  0.0885  102 THR C OG1 
7003  C  CG2 . THR C 101 ? 0.4225 0.5894 0.8112 -0.0293 0.0373  0.0830  102 THR C CG2 
7004  N  N   . GLN C 102 ? 0.3847 0.5343 0.7248 -0.0360 0.0443  0.0807  103 GLN C N   
7005  C  CA  . GLN C 102 ? 0.3762 0.5258 0.7139 -0.0387 0.0509  0.0794  103 GLN C CA  
7006  C  C   . GLN C 102 ? 0.4073 0.5527 0.7390 -0.0437 0.0474  0.0804  103 GLN C C   
7007  O  O   . GLN C 102 ? 0.3973 0.5464 0.7363 -0.0474 0.0489  0.0805  103 GLN C O   
7008  C  CB  . GLN C 102 ? 0.4200 0.5641 0.7444 -0.0370 0.0570  0.0784  103 GLN C CB  
7009  C  CG  . GLN C 102 ? 0.4718 0.6191 0.7999 -0.0338 0.0619  0.0762  103 GLN C CG  
7010  C  CD  . GLN C 102 ? 0.5490 0.7048 0.8923 -0.0350 0.0679  0.0737  103 GLN C CD  
7011  O  OE1 . GLN C 102 ? 0.5639 0.7219 0.9087 -0.0391 0.0714  0.0738  103 GLN C OE1 
7012  N  NE2 . GLN C 102 ? 0.7113 0.8717 1.0671 -0.0317 0.0699  0.0711  103 GLN C NE2 
7013  N  N   . LEU C 103 ? 0.3673 0.5046 0.6856 -0.0444 0.0436  0.0807  104 LEU C N   
7014  C  CA  . LEU C 103 ? 0.4136 0.5447 0.7242 -0.0497 0.0412  0.0802  104 LEU C CA  
7015  C  C   . LEU C 103 ? 0.4136 0.5503 0.7342 -0.0548 0.0353  0.0813  104 LEU C C   
7016  O  O   . LEU C 103 ? 0.3694 0.5064 0.6931 -0.0590 0.0367  0.0809  104 LEU C O   
7017  C  CB  . LEU C 103 ? 0.4197 0.5421 0.7158 -0.0501 0.0387  0.0791  104 LEU C CB  
7018  C  CG  . LEU C 103 ? 0.4756 0.5897 0.7617 -0.0562 0.0374  0.0769  104 LEU C CG  
7019  C  CD1 . LEU C 103 ? 0.4737 0.5814 0.7574 -0.0561 0.0441  0.0753  104 LEU C CD1 
7020  C  CD2 . LEU C 103 ? 0.4992 0.6066 0.7718 -0.0577 0.0354  0.0752  104 LEU C CD2 
7021  N  N   . ARG C 104 ? 0.3660 0.5072 0.6925 -0.0549 0.0278  0.0835  105 ARG C N   
7022  C  CA  . ARG C 104 ? 0.4932 0.6407 0.8308 -0.0602 0.0198  0.0860  105 ARG C CA  
7023  C  C   . ARG C 104 ? 0.3658 0.5239 0.7243 -0.0597 0.0233  0.0864  105 ARG C C   
7024  O  O   . ARG C 104 ? 0.3703 0.5315 0.7351 -0.0654 0.0206  0.0871  105 ARG C O   
7025  C  CB  . ARG C 104 ? 0.3721 0.5229 0.7146 -0.0599 0.0102  0.0900  105 ARG C CB  
7026  N  N   . SER C 105 ? 0.3966 0.5601 0.7654 -0.0536 0.0300  0.0854  106 SER C N   
7027  C  CA  . SER C 105 ? 0.3759 0.5497 0.7644 -0.0533 0.0358  0.0845  106 SER C CA  
7028  C  C   . SER C 105 ? 0.4065 0.5777 0.7888 -0.0581 0.0415  0.0831  106 SER C C   
7029  O  O   . SER C 105 ? 0.4596 0.6377 0.8553 -0.0625 0.0409  0.0838  106 SER C O   
7030  C  CB  . SER C 105 ? 0.3491 0.5262 0.7441 -0.0471 0.0443  0.0819  106 SER C CB  
7031  O  OG  . SER C 105 ? 0.4297 0.6118 0.8396 -0.0429 0.0395  0.0834  106 SER C OG  
7032  N  N   . PHE C 106 ? 0.3596 0.5208 0.7229 -0.0574 0.0466  0.0817  107 PHE C N   
7033  C  CA  . PHE C 106 ? 0.3642 0.5213 0.7214 -0.0618 0.0517  0.0814  107 PHE C CA  
7034  C  C   . PHE C 106 ? 0.4192 0.5716 0.7729 -0.0681 0.0458  0.0819  107 PHE C C   
7035  O  O   . PHE C 106 ? 0.4575 0.6125 0.8179 -0.0732 0.0476  0.0823  107 PHE C O   
7036  C  CB  . PHE C 106 ? 0.3649 0.5121 0.7050 -0.0593 0.0568  0.0812  107 PHE C CB  
7037  C  CG  . PHE C 106 ? 0.3627 0.5140 0.7043 -0.0574 0.0648  0.0807  107 PHE C CG  
7038  C  CD1 . PHE C 106 ? 0.3580 0.5112 0.6991 -0.0522 0.0663  0.0794  107 PHE C CD1 
7039  C  CD2 . PHE C 106 ? 0.3676 0.5200 0.7096 -0.0619 0.0711  0.0814  107 PHE C CD2 
7040  C  CE1 . PHE C 106 ? 0.3589 0.5148 0.6989 -0.0519 0.0741  0.0780  107 PHE C CE1 
7041  C  CE2 . PHE C 106 ? 0.3689 0.5244 0.7090 -0.0620 0.0789  0.0807  107 PHE C CE2 
7042  C  CZ  . PHE C 106 ? 0.3650 0.5220 0.7035 -0.0572 0.0806  0.0785  107 PHE C CZ  
7043  N  N   . ASP C 107 ? 0.4138 0.5588 0.7562 -0.0688 0.0395  0.0815  108 ASP C N   
7044  C  CA  . ASP C 107 ? 0.4552 0.5943 0.7916 -0.0761 0.0344  0.0808  108 ASP C CA  
7045  C  C   . ASP C 107 ? 0.4995 0.6494 0.8527 -0.0813 0.0282  0.0829  108 ASP C C   
7046  O  O   . ASP C 107 ? 0.4908 0.6407 0.8476 -0.0875 0.0285  0.0826  108 ASP C O   
7047  C  CB  . ASP C 107 ? 0.4658 0.5961 0.7864 -0.0771 0.0293  0.0793  108 ASP C CB  
7048  C  CG  . ASP C 107 ? 0.4555 0.5747 0.7636 -0.0847 0.0281  0.0761  108 ASP C CG  
7049  O  OD1 . ASP C 107 ? 0.4377 0.5514 0.7452 -0.0862 0.0337  0.0748  108 ASP C OD1 
7050  O  OD2 . ASP C 107 ? 0.5032 0.6186 0.8015 -0.0899 0.0217  0.0750  108 ASP C OD2 
7051  N  N   . ASP C 108 ? 0.4864 0.6458 0.8520 -0.0788 0.0224  0.0854  109 ASP C N   
7052  C  CA  . ASP C 108 ? 0.5388 0.7104 0.9255 -0.0827 0.0154  0.0885  109 ASP C CA  
7053  C  C   . ASP C 108 ? 0.4957 0.6765 0.9002 -0.0833 0.0229  0.0881  109 ASP C C   
7054  O  O   . ASP C 108 ? 0.4667 0.6530 0.8822 -0.0899 0.0191  0.0894  109 ASP C O   
7055  C  CB  . ASP C 108 ? 0.5488 0.7291 0.9501 -0.0780 0.0091  0.0920  109 ASP C CB  
7056  C  CG  . ASP C 108 ? 0.5905 0.7638 0.9765 -0.0808 -0.0015 0.0943  109 ASP C CG  
7057  O  OD1 . ASP C 108 ? 0.6869 0.8477 1.0489 -0.0849 -0.0011 0.0914  109 ASP C OD1 
7058  O  OD2 . ASP C 108 ? 0.5827 0.7625 0.9812 -0.0792 -0.0100 0.0989  109 ASP C OD2 
7059  N  N   . HIS C 109 ? 0.4496 0.6319 0.8560 -0.0776 0.0337  0.0861  110 HIS C N   
7060  C  CA  . HIS C 109 ? 0.4809 0.6720 0.9027 -0.0792 0.0422  0.0853  110 HIS C CA  
7061  C  C   . HIS C 109 ? 0.4379 0.6219 0.8492 -0.0859 0.0455  0.0849  110 HIS C C   
7062  O  O   . HIS C 109 ? 0.4462 0.6379 0.8717 -0.0909 0.0479  0.0854  110 HIS C O   
7063  C  CB  . HIS C 109 ? 0.3655 0.5588 0.7882 -0.0732 0.0534  0.0828  110 HIS C CB  
7064  C  CG  . HIS C 109 ? 0.3919 0.5931 0.8265 -0.0764 0.0638  0.0813  110 HIS C CG  
7065  N  ND1 . HIS C 109 ? 0.3664 0.5816 0.8280 -0.0789 0.0642  0.0815  110 HIS C ND1 
7066  C  CD2 . HIS C 109 ? 0.4270 0.6239 0.8500 -0.0784 0.0741  0.0800  110 HIS C CD2 
7067  C  CE1 . HIS C 109 ? 0.3695 0.5889 0.8352 -0.0824 0.0757  0.0795  110 HIS C CE1 
7068  N  NE2 . HIS C 109 ? 0.4260 0.6340 0.8671 -0.0826 0.0815  0.0788  110 HIS C NE2 
7069  N  N   . PHE C 110 ? 0.3827 0.5521 0.7712 -0.0861 0.0459  0.0840  111 PHE C N   
7070  C  CA  . PHE C 110 ? 0.5170 0.6776 0.8966 -0.0922 0.0485  0.0840  111 PHE C CA  
7071  C  C   . PHE C 110 ? 0.4796 0.6402 0.8633 -0.1001 0.0402  0.0842  111 PHE C C   
7072  O  O   . PHE C 110 ? 0.5117 0.6756 0.9040 -0.1065 0.0417  0.0849  111 PHE C O   
7073  C  CB  . PHE C 110 ? 0.3944 0.5393 0.7526 -0.0897 0.0508  0.0830  111 PHE C CB  
7074  C  CG  . PHE C 110 ? 0.3905 0.5341 0.7435 -0.0849 0.0588  0.0840  111 PHE C CG  
7075  C  CD1 . PHE C 110 ? 0.3916 0.5411 0.7513 -0.0875 0.0659  0.0855  111 PHE C CD1 
7076  C  CD2 . PHE C 110 ? 0.4611 0.5979 0.8020 -0.0788 0.0592  0.0836  111 PHE C CD2 
7077  C  CE1 . PHE C 110 ? 0.3911 0.5389 0.7430 -0.0850 0.0727  0.0867  111 PHE C CE1 
7078  C  CE2 . PHE C 110 ? 0.3853 0.5210 0.7206 -0.0756 0.0652  0.0851  111 PHE C CE2 
7079  C  CZ  . PHE C 110 ? 0.3879 0.5288 0.7277 -0.0791 0.0717  0.0867  111 PHE C CZ  
7080  N  N   . GLN C 111 ? 0.4630 0.6201 0.8396 -0.1007 0.0313  0.0836  112 GLN C N   
7081  C  CA  . GLN C 111 ? 0.4871 0.6439 0.8648 -0.1097 0.0220  0.0839  112 GLN C CA  
7082  C  C   . GLN C 111 ? 0.4984 0.6722 0.9023 -0.1131 0.0183  0.0872  112 GLN C C   
7083  O  O   . GLN C 111 ? 0.4577 0.6328 0.8670 -0.1216 0.0152  0.0876  112 GLN C O   
7084  C  CB  . GLN C 111 ? 0.5082 0.6600 0.8735 -0.1106 0.0128  0.0835  112 GLN C CB  
7085  C  CG  . GLN C 111 ? 0.5576 0.6917 0.8976 -0.1106 0.0161  0.0791  112 GLN C CG  
7086  C  CD  . GLN C 111 ? 0.6299 0.7595 0.9562 -0.1121 0.0086  0.0784  112 GLN C CD  
7087  O  OE1 . GLN C 111 ? 0.6663 0.8057 1.0015 -0.1131 -0.0005 0.0825  112 GLN C OE1 
7088  N  NE2 . GLN C 111 ? 0.6721 0.7869 0.9778 -0.1127 0.0126  0.0736  112 GLN C NE2 
7089  N  N   . HIS C 112 ? 0.5391 0.7258 0.9609 -0.1066 0.0193  0.0891  113 HIS C N   
7090  C  CA  . HIS C 112 ? 0.5536 0.7578 1.0054 -0.1084 0.0174  0.0919  113 HIS C CA  
7091  C  C   . HIS C 112 ? 0.4791 0.6877 0.9402 -0.1111 0.0283  0.0906  113 HIS C C   
7092  O  O   . HIS C 112 ? 0.4104 0.6307 0.8928 -0.1165 0.0264  0.0924  113 HIS C O   
7093  C  CB  . HIS C 112 ? 0.6568 0.8724 1.1274 -0.0999 0.0177  0.0934  113 HIS C CB  
7094  C  CG  . HIS C 112 ? 0.7744 1.0082 1.2794 -0.0998 0.0210  0.0946  113 HIS C CG  
7095  N  ND1 . HIS C 112 ? 0.8304 1.0704 1.3462 -0.0951 0.0353  0.0913  113 HIS C ND1 
7096  C  CD2 . HIS C 112 ? 0.8364 1.0836 1.3681 -0.1044 0.0122  0.0986  113 HIS C CD2 
7097  C  CE1 . HIS C 112 ? 0.8516 1.1082 1.4004 -0.0964 0.0366  0.0923  113 HIS C CE1 
7098  N  NE2 . HIS C 112 ? 0.8568 1.1186 1.4174 -0.1016 0.0222  0.0972  113 HIS C NE2 
7099  N  N   . LEU C 113 ? 0.4647 0.6646 0.9104 -0.1080 0.0392  0.0882  114 LEU C N   
7100  C  CA  . LEU C 113 ? 0.3967 0.5988 0.8470 -0.1120 0.0495  0.0878  114 LEU C CA  
7101  C  C   . LEU C 113 ? 0.5637 0.7593 1.0090 -0.1216 0.0453  0.0885  114 LEU C C   
7102  O  O   . LEU C 113 ? 0.4103 0.6153 0.8727 -0.1279 0.0468  0.0897  114 LEU C O   
7103  C  CB  . LEU C 113 ? 0.3960 0.5885 0.8280 -0.1079 0.0598  0.0865  114 LEU C CB  
7104  C  CG  . LEU C 113 ? 0.4854 0.6868 0.9256 -0.1018 0.0691  0.0849  114 LEU C CG  
7105  C  CD1 . LEU C 113 ? 0.5033 0.6936 0.9216 -0.0999 0.0771  0.0846  114 LEU C CD1 
7106  C  CD2 . LEU C 113 ? 0.3890 0.6063 0.8544 -0.1057 0.0762  0.0842  114 LEU C CD2 
7107  N  N   . LEU C 114 ? 0.5390 0.7181 0.9618 -0.1230 0.0407  0.0874  115 LEU C N   
7108  C  CA  . LEU C 114 ? 0.4929 0.6632 0.9095 -0.1325 0.0371  0.0870  115 LEU C CA  
7109  C  C   . LEU C 114 ? 0.4839 0.6653 0.9172 -0.1399 0.0266  0.0885  115 LEU C C   
7110  O  O   . LEU C 114 ? 0.4369 0.6220 0.8803 -0.1482 0.0265  0.0894  115 LEU C O   
7111  C  CB  . LEU C 114 ? 0.4346 0.5852 0.8260 -0.1324 0.0347  0.0841  115 LEU C CB  
7112  C  CG  . LEU C 114 ? 0.5363 0.6727 0.9183 -0.1404 0.0362  0.0826  115 LEU C CG  
7113  C  CD1 . LEU C 114 ? 0.5518 0.6877 0.9378 -0.1406 0.0459  0.0852  115 LEU C CD1 
7114  C  CD2 . LEU C 114 ? 0.4565 0.5737 0.8167 -0.1391 0.0358  0.0785  115 LEU C CD2 
7115  N  N   . ASN C 115 ? 0.4272 0.6140 0.8638 -0.1375 0.0173  0.0895  116 ASN C N   
7116  C  CA  . ASN C 115 ? 0.5959 0.7935 1.0484 -0.1447 0.0048  0.0925  116 ASN C CA  
7117  C  C   . ASN C 115 ? 0.5261 0.7439 1.0122 -0.1460 0.0068  0.0956  116 ASN C C   
7118  O  O   . ASN C 115 ? 0.5099 0.7338 1.0084 -0.1554 0.0008  0.0975  116 ASN C O   
7119  C  CB  . ASN C 115 ? 0.6014 0.8013 1.0518 -0.1411 -0.0057 0.0945  116 ASN C CB  
7120  C  CG  . ASN C 115 ? 0.6934 0.8757 1.1136 -0.1462 -0.0122 0.0918  116 ASN C CG  
7121  O  OD1 . ASN C 115 ? 0.6997 0.8681 1.1027 -0.1521 -0.0088 0.0877  116 ASN C OD1 
7122  N  ND2 . ASN C 115 ? 0.7339 0.9161 1.1478 -0.1445 -0.0210 0.0937  116 ASN C ND2 
7123  N  N   . ASP C 116 ? 0.4988 0.7268 1.0000 -0.1372 0.0158  0.0956  117 ASP C N   
7124  C  CA  . ASP C 116 ? 0.4776 0.7249 1.0121 -0.1375 0.0214  0.0971  117 ASP C CA  
7125  C  C   . ASP C 116 ? 0.4909 0.7362 1.0242 -0.1452 0.0300  0.0959  117 ASP C C   
7126  O  O   . ASP C 116 ? 0.4590 0.7179 1.0171 -0.1514 0.0294  0.0977  117 ASP C O   
7127  C  CB  . ASP C 116 ? 0.5948 0.8496 1.1401 -0.1269 0.0323  0.0952  117 ASP C CB  
7128  C  CG  . ASP C 116 ? 0.6835 0.9596 1.2678 -0.1265 0.0381  0.0957  117 ASP C CG  
7129  O  OD1 . ASP C 116 ? 0.7753 1.0595 1.3748 -0.1344 0.0397  0.0966  117 ASP C OD1 
7130  O  OD2 . ASP C 116 ? 0.7077 0.9925 1.3089 -0.1182 0.0417  0.0947  117 ASP C OD2 
7131  N  N   . SER C 117 ? 0.4737 0.7021 0.9798 -0.1450 0.0375  0.0935  118 SER C N   
7132  C  CA  . SER C 117 ? 0.4728 0.6963 0.9749 -0.1531 0.0444  0.0934  118 SER C CA  
7133  C  C   . SER C 117 ? 0.5027 0.7251 1.0086 -0.1640 0.0336  0.0947  118 SER C C   
7134  O  O   . SER C 117 ? 0.4426 0.6743 0.9662 -0.1717 0.0357  0.0962  118 SER C O   
7135  C  CB  . SER C 117 ? 0.5125 0.7158 0.9847 -0.1510 0.0510  0.0920  118 SER C CB  
7136  O  OG  . SER C 117 ? 0.5401 0.7380 1.0093 -0.1589 0.0572  0.0931  118 SER C OG  
7137  N  N   . GLU C 118 ? 0.5370 0.7480 1.0259 -0.1655 0.0225  0.0939  119 GLU C N   
7138  C  CA  . GLU C 118 ? 0.5042 0.7116 0.9916 -0.1772 0.0116  0.0942  119 GLU C CA  
7139  C  C   . GLU C 118 ? 0.4912 0.7199 1.0102 -0.1825 0.0024  0.0984  119 GLU C C   
7140  O  O   . GLU C 118 ? 0.5324 0.7651 1.0619 -0.1929 -0.0005 0.0996  119 GLU C O   
7141  C  CB  . GLU C 118 ? 0.5622 0.7534 1.0234 -0.1784 0.0025  0.0916  119 GLU C CB  
7142  C  CG  . GLU C 118 ? 0.6252 0.8064 1.0761 -0.1918 -0.0060 0.0898  119 GLU C CG  
7143  C  CD  . GLU C 118 ? 0.7094 0.8707 1.1296 -0.1934 -0.0103 0.0850  119 GLU C CD  
7144  O  OE1 . GLU C 118 ? 0.7045 0.8616 1.1136 -0.1838 -0.0077 0.0839  119 GLU C OE1 
7145  O  OE2 . GLU C 118 ? 0.7578 0.9074 1.1650 -0.2047 -0.0154 0.0817  119 GLU C OE2 
7146  N  N   . ARG C 119 ? 0.5177 0.7599 1.0534 -0.1754 -0.0025 0.1010  120 ARG C N   
7147  C  CA  . ARG C 119 ? 0.5612 0.8249 1.1319 -0.1791 -0.0120 0.1061  120 ARG C CA  
7148  C  C   . ARG C 119 ? 0.5644 0.8446 1.1653 -0.1802 -0.0008 0.1065  120 ARG C C   
7149  O  O   . ARG C 119 ? 0.5557 0.8495 1.1818 -0.1885 -0.0071 0.1099  120 ARG C O   
7150  C  CB  . ARG C 119 ? 0.5422 0.8156 1.1262 -0.1700 -0.0188 0.1092  120 ARG C CB  
7151  C  CG  . ARG C 119 ? 0.6046 0.8668 1.1658 -0.1729 -0.0343 0.1110  120 ARG C CG  
7152  C  CD  . ARG C 119 ? 0.6923 0.9651 1.2701 -0.1648 -0.0422 0.1157  120 ARG C CD  
7153  N  NE  . ARG C 119 ? 0.6922 0.9603 1.2621 -0.1517 -0.0297 0.1121  120 ARG C NE  
7154  C  CZ  . ARG C 119 ? 0.7479 1.0011 1.2888 -0.1473 -0.0309 0.1102  120 ARG C CZ  
7155  N  NH1 . ARG C 119 ? 0.7612 1.0024 1.2774 -0.1551 -0.0430 0.1110  120 ARG C NH1 
7156  N  NH2 . ARG C 119 ? 0.7366 0.9869 1.2727 -0.1360 -0.0197 0.1072  120 ARG C NH2 
7157  N  N   . THR C 120 ? 0.6004 0.8792 1.1982 -0.1728 0.0159  0.1032  121 THR C N   
7158  C  CA  . THR C 120 ? 0.5972 0.8893 1.2180 -0.1747 0.0296  0.1025  121 THR C CA  
7159  C  C   . THR C 120 ? 0.6292 0.9155 1.2439 -0.1872 0.0300  0.1029  121 THR C C   
7160  O  O   . THR C 120 ? 0.6388 0.9406 1.2814 -0.1942 0.0313  0.1047  121 THR C O   
7161  C  CB  . THR C 120 ? 0.6271 0.9143 1.2359 -0.1667 0.0472  0.0986  121 THR C CB  
7162  O  OG1 . THR C 120 ? 0.6411 0.9347 1.2589 -0.1556 0.0477  0.0977  121 THR C OG1 
7163  C  CG2 . THR C 120 ? 0.6496 0.9489 1.2777 -0.1712 0.0624  0.0974  121 THR C CG2 
7164  N  N   . LEU C 121 ? 0.6034 0.8670 1.1832 -0.1901 0.0291  0.1011  122 LEU C N   
7165  C  CA  . LEU C 121 ? 0.5572 0.8115 1.1285 -0.2019 0.0286  0.1012  122 LEU C CA  
7166  C  C   . LEU C 121 ? 0.4926 0.7560 1.0810 -0.2123 0.0137  0.1039  122 LEU C C   
7167  O  O   . LEU C 121 ? 0.4894 0.7627 1.0971 -0.2214 0.0151  0.1056  122 LEU C O   
7168  C  CB  . LEU C 121 ? 0.5882 0.8155 1.1216 -0.2020 0.0288  0.0985  122 LEU C CB  
7169  C  CG  . LEU C 121 ? 0.5797 0.7929 1.1016 -0.2140 0.0276  0.0979  122 LEU C CG  
7170  C  CD1 . LEU C 121 ? 0.5833 0.7759 1.0802 -0.2113 0.0379  0.0966  122 LEU C CD1 
7171  C  CD2 . LEU C 121 ? 0.5697 0.7731 1.0797 -0.2210 0.0129  0.0961  122 LEU C CD2 
7172  N  N   . GLN C 122 ? 0.4729 0.7333 1.0538 -0.2119 -0.0010 0.1046  123 GLN C N   
7173  C  CA  . GLN C 122 ? 0.5213 0.7885 1.1138 -0.2231 -0.0176 0.1078  123 GLN C CA  
7174  C  C   . GLN C 122 ? 0.5340 0.8294 1.1718 -0.2246 -0.0209 0.1130  123 GLN C C   
7175  O  O   . GLN C 122 ? 0.4847 0.7887 1.1386 -0.2362 -0.0313 0.1163  123 GLN C O   
7176  C  CB  . GLN C 122 ? 0.5400 0.7988 1.1137 -0.2224 -0.0323 0.1082  123 GLN C CB  
7177  C  CG  . GLN C 122 ? 0.6041 0.8353 1.1354 -0.2244 -0.0312 0.1023  123 GLN C CG  
7178  C  CD  . GLN C 122 ? 0.6396 0.8632 1.1516 -0.2243 -0.0440 0.1022  123 GLN C CD  
7179  O  OE1 . GLN C 122 ? 0.6117 0.8502 1.1411 -0.2215 -0.0541 0.1075  123 GLN C OE1 
7180  N  NE2 . GLN C 122 ? 0.6760 0.8761 1.1529 -0.2278 -0.0433 0.0963  123 GLN C NE2 
7181  N  N   . ALA C 123 ? 0.5164 0.8262 1.1761 -0.2132 -0.0118 0.1136  124 ALA C N   
7182  C  CA  . ALA C 123 ? 0.4527 0.7897 1.1598 -0.2129 -0.0133 0.1178  124 ALA C CA  
7183  C  C   . ALA C 123 ? 0.6258 0.9735 1.3533 -0.2176 0.0020  0.1163  124 ALA C C   
7184  O  O   . ALA C 123 ? 0.4537 0.8211 1.2174 -0.2242 -0.0020 0.1199  124 ALA C O   
7185  C  CB  . ALA C 123 ? 0.4380 0.7853 1.1620 -0.1988 -0.0097 0.1182  124 ALA C CB  
7186  N  N   . THR C 124 ? 0.5665 0.9015 1.2714 -0.2150 0.0190  0.1116  125 THR C N   
7187  C  CA  . THR C 124 ? 0.5211 0.8657 1.2427 -0.2195 0.0355  0.1102  125 THR C CA  
7188  C  C   . THR C 124 ? 0.5203 0.8540 1.2275 -0.2331 0.0353  0.1107  125 THR C C   
7189  O  O   . THR C 124 ? 0.5167 0.8638 1.2479 -0.2412 0.0418  0.1118  125 THR C O   
7190  C  CB  . THR C 124 ? 0.4962 0.8348 1.2028 -0.2107 0.0549  0.1057  125 THR C CB  
7191  O  OG1 . THR C 124 ? 0.4632 0.7761 1.1260 -0.2076 0.0536  0.1040  125 THR C OG1 
7192  C  CG2 . THR C 124 ? 0.4849 0.8385 1.2150 -0.1986 0.0590  0.1043  125 THR C CG2 
7193  N  N   . PHE C 125 ? 0.5233 0.8325 1.1927 -0.2357 0.0287  0.1095  126 PHE C N   
7194  C  CA  . PHE C 125 ? 0.5565 0.8509 1.2089 -0.2477 0.0298  0.1093  126 PHE C CA  
7195  C  C   . PHE C 125 ? 0.5034 0.8082 1.1775 -0.2618 0.0188  0.1122  126 PHE C C   
7196  O  O   . PHE C 125 ? 0.5130 0.8159 1.1895 -0.2716 0.0253  0.1127  126 PHE C O   
7197  C  CB  . PHE C 125 ? 0.5020 0.7675 1.1126 -0.2467 0.0247  0.1066  126 PHE C CB  
7198  C  CG  . PHE C 125 ? 0.5871 0.8369 1.1728 -0.2390 0.0386  0.1046  126 PHE C CG  
7199  C  CD1 . PHE C 125 ? 0.5219 0.7810 1.1136 -0.2280 0.0492  0.1041  126 PHE C CD1 
7200  C  CD2 . PHE C 125 ? 0.5582 0.7835 1.1154 -0.2433 0.0408  0.1034  126 PHE C CD2 
7201  C  CE1 . PHE C 125 ? 0.5273 0.7723 1.0953 -0.2223 0.0605  0.1031  126 PHE C CE1 
7202  C  CE2 . PHE C 125 ? 0.5585 0.7698 1.0948 -0.2366 0.0518  0.1031  126 PHE C CE2 
7203  C  CZ  . PHE C 125 ? 0.5500 0.7714 1.0907 -0.2266 0.0611  0.1033  126 PHE C CZ  
7204  N  N   . PRO C 126 ? 0.5665 0.8816 1.2554 -0.2637 0.0015  0.1149  127 PRO C N   
7205  C  CA  . PRO C 126 ? 0.6042 0.9309 1.3159 -0.2781 -0.0091 0.1183  127 PRO C CA  
7206  C  C   . PRO C 126 ? 0.6682 1.0198 1.4212 -0.2810 0.0017  0.1206  127 PRO C C   
7207  O  O   . PRO C 126 ? 0.7108 1.0655 1.4738 -0.2938 0.0013  0.1220  127 PRO C O   
7208  C  CB  . PRO C 126 ? 0.5532 0.8896 1.2764 -0.2781 -0.0295 0.1222  127 PRO C CB  
7209  C  CG  . PRO C 126 ? 0.5092 0.8267 1.1977 -0.2683 -0.0314 0.1191  127 PRO C CG  
7210  C  CD  . PRO C 126 ? 0.5770 0.8899 1.2574 -0.2560 -0.0111 0.1154  127 PRO C CD  
7211  N  N   . GLY C 127 ? 0.6815 1.0501 1.4583 -0.2696 0.0122  0.1204  128 GLY C N   
7212  C  CA  . GLY C 127 ? 0.7049 1.0979 1.5228 -0.2717 0.0248  0.1212  128 GLY C CA  
7213  C  C   . GLY C 127 ? 0.7179 1.1028 1.5215 -0.2755 0.0454  0.1180  128 GLY C C   
7214  O  O   . GLY C 127 ? 0.7560 1.1549 1.5839 -0.2841 0.0537  0.1188  128 GLY C O   
7215  N  N   . ALA C 128 ? 0.7069 1.0687 1.4701 -0.2696 0.0532  0.1149  129 ALA C N   
7216  C  CA  . ALA C 128 ? 0.6909 1.0438 1.4378 -0.2726 0.0720  0.1131  129 ALA C CA  
7217  C  C   . ALA C 128 ? 0.6666 0.9994 1.3890 -0.2852 0.0690  0.1147  129 ALA C C   
7218  O  O   . ALA C 128 ? 0.6836 1.0147 1.4042 -0.2930 0.0819  0.1155  129 ALA C O   
7219  C  CB  . ALA C 128 ? 0.6983 1.0372 1.4162 -0.2604 0.0815  0.1100  129 ALA C CB  
7220  N  N   . PHE C 129 ? 0.6542 0.9710 1.3576 -0.2879 0.0524  0.1150  130 PHE C N   
7221  C  CA  . PHE C 129 ? 0.6346 0.9284 1.3124 -0.2986 0.0497  0.1153  130 PHE C CA  
7222  C  C   . PHE C 129 ? 0.6822 0.9775 1.3696 -0.3109 0.0329  0.1164  130 PHE C C   
7223  O  O   . PHE C 129 ? 0.7054 0.9872 1.3822 -0.3228 0.0319  0.1167  130 PHE C O   
7224  C  CB  . PHE C 129 ? 0.6093 0.8744 1.2456 -0.2912 0.0488  0.1127  130 PHE C CB  
7225  C  CG  . PHE C 129 ? 0.5968 0.8591 1.2209 -0.2796 0.0629  0.1121  130 PHE C CG  
7226  C  CD1 . PHE C 129 ? 0.5885 0.8432 1.2021 -0.2833 0.0771  0.1140  130 PHE C CD1 
7227  C  CD2 . PHE C 129 ? 0.5809 0.8475 1.2027 -0.2661 0.0612  0.1101  130 PHE C CD2 
7228  C  CE1 . PHE C 129 ? 0.5870 0.8388 1.1873 -0.2743 0.0890  0.1137  130 PHE C CE1 
7229  C  CE2 . PHE C 129 ? 0.5507 0.8143 1.1604 -0.2565 0.0737  0.1092  130 PHE C CE2 
7230  C  CZ  . PHE C 129 ? 0.5725 0.8287 1.1708 -0.2609 0.0875  0.1110  130 PHE C CZ  
7231  N  N   . GLY C 130 ? 0.7110 1.0219 1.4177 -0.3087 0.0191  0.1174  131 GLY C N   
7232  C  CA  . GLY C 130 ? 0.7376 1.0504 1.4517 -0.3213 0.0012  0.1191  131 GLY C CA  
7233  C  C   . GLY C 130 ? 0.7731 1.0566 1.4469 -0.3249 -0.0091 0.1153  131 GLY C C   
7234  O  O   . GLY C 130 ? 0.7930 1.0650 1.4444 -0.3150 -0.0122 0.1127  131 GLY C O   
7235  N  N   . GLU C 131 ? 0.8210 1.0918 1.4857 -0.3396 -0.0135 0.1144  132 GLU C N   
7236  C  CA  . GLU C 131 ? 0.8448 1.0875 1.4734 -0.3450 -0.0225 0.1095  132 GLU C CA  
7237  C  C   . GLU C 131 ? 0.8356 1.0498 1.4329 -0.3413 -0.0094 0.1055  132 GLU C C   
7238  O  O   . GLU C 131 ? 0.9168 1.1054 1.4863 -0.3466 -0.0135 0.1004  132 GLU C O   
7239  C  CB  . GLU C 131 ? 0.9456 1.1878 1.5798 -0.3638 -0.0360 0.1097  132 GLU C CB  
7240  C  CG  . GLU C 131 ? 0.9927 1.2355 1.6396 -0.3752 -0.0279 0.1114  132 GLU C CG  
7241  C  CD  . GLU C 131 ? 1.0651 1.3099 1.7202 -0.3943 -0.0426 0.1119  132 GLU C CD  
7242  O  OE1 . GLU C 131 ? 1.0906 1.3281 1.7306 -0.3997 -0.0583 0.1093  132 GLU C OE1 
7243  O  OE2 . GLU C 131 ? 1.0872 1.3408 1.7628 -0.4048 -0.0386 0.1149  132 GLU C OE2 
7244  N  N   . LEU C 132 ? 0.7822 1.0006 1.3848 -0.3328 0.0063  0.1079  133 LEU C N   
7245  C  CA  . LEU C 132 ? 0.7653 0.9585 1.3392 -0.3262 0.0173  0.1058  133 LEU C CA  
7246  C  C   . LEU C 132 ? 0.7398 0.9258 1.2948 -0.3119 0.0154  0.1026  133 LEU C C   
7247  O  O   . LEU C 132 ? 0.7752 0.9382 1.3041 -0.3058 0.0205  0.0999  133 LEU C O   
7248  C  CB  . LEU C 132 ? 0.7385 0.9385 1.3217 -0.3237 0.0337  0.1102  133 LEU C CB  
7249  C  CG  . LEU C 132 ? 0.7395 0.9389 1.3331 -0.3385 0.0382  0.1134  133 LEU C CG  
7250  C  CD1 . LEU C 132 ? 0.7151 0.9173 1.3105 -0.3365 0.0550  0.1178  133 LEU C CD1 
7251  C  CD2 . LEU C 132 ? 0.7614 0.9316 1.3324 -0.3478 0.0325  0.1104  133 LEU C CD2 
7252  N  N   . TYR C 133 ? 0.6705 0.8766 1.2411 -0.3067 0.0076  0.1035  134 TYR C N   
7253  C  CA  . TYR C 133 ? 0.6699 0.8709 1.2244 -0.2950 0.0031  0.1007  134 TYR C CA  
7254  C  C   . TYR C 133 ? 0.6923 0.8924 1.2417 -0.3020 -0.0145 0.0987  134 TYR C C   
7255  O  O   . TYR C 133 ? 0.6809 0.8628 1.2031 -0.2993 -0.0186 0.0940  134 TYR C O   
7256  C  CB  . TYR C 133 ? 0.6206 0.8435 1.1944 -0.2821 0.0087  0.1037  134 TYR C CB  
7257  C  CG  . TYR C 133 ? 0.6154 0.8395 1.1813 -0.2729 -0.0004 0.1023  134 TYR C CG  
7258  C  CD1 . TYR C 133 ? 0.6549 0.8596 1.1914 -0.2634 0.0030  0.0986  134 TYR C CD1 
7259  C  CD2 . TYR C 133 ? 0.5383 0.7830 1.1274 -0.2742 -0.0130 0.1055  134 TYR C CD2 
7260  C  CE1 . TYR C 133 ? 0.5355 0.7409 1.0640 -0.2559 -0.0049 0.0975  134 TYR C CE1 
7261  C  CE2 . TYR C 133 ? 0.5563 0.8012 1.1373 -0.2668 -0.0220 0.1052  134 TYR C CE2 
7262  C  CZ  . TYR C 133 ? 0.5653 0.7904 1.1151 -0.2578 -0.0175 0.1010  134 TYR C CZ  
7263  O  OH  . TYR C 133 ? 0.5914 0.8164 1.1324 -0.2512 -0.0259 0.1009  134 TYR C OH  
7264  N  N   . THR C 134 ? 0.7184 0.9388 1.2944 -0.3118 -0.0247 0.1026  135 THR C N   
7265  C  CA  . THR C 134 ? 0.7930 1.0176 1.3682 -0.3193 -0.0435 0.1029  135 THR C CA  
7266  C  C   . THR C 134 ? 0.8751 1.0714 1.4135 -0.3285 -0.0501 0.0959  135 THR C C   
7267  O  O   . THR C 134 ? 0.8879 1.0785 1.4090 -0.3284 -0.0605 0.0938  135 THR C O   
7268  C  CB  . THR C 134 ? 0.8133 1.0614 1.4231 -0.3318 -0.0539 0.1086  135 THR C CB  
7269  O  OG1 . THR C 134 ? 0.8044 1.0795 1.4517 -0.3234 -0.0462 0.1140  135 THR C OG1 
7270  C  CG2 . THR C 134 ? 0.8147 1.0688 1.4245 -0.3399 -0.0753 0.1109  135 THR C CG2 
7271  N  N   . GLN C 135 ? 0.9939 1.1716 1.5201 -0.3369 -0.0435 0.0921  136 GLN C N   
7272  C  CA  . GLN C 135 ? 1.0443 1.1936 1.5374 -0.3463 -0.0475 0.0839  136 GLN C CA  
7273  C  C   . GLN C 135 ? 1.0013 1.1265 1.4665 -0.3342 -0.0357 0.0779  136 GLN C C   
7274  O  O   . GLN C 135 ? 1.0506 1.1540 1.4877 -0.3378 -0.0382 0.0702  136 GLN C O   
7275  C  CB  . GLN C 135 ? 1.1664 1.3058 1.6615 -0.3619 -0.0467 0.0823  136 GLN C CB  
7276  C  CG  . GLN C 135 ? 1.2568 1.3668 1.7201 -0.3740 -0.0508 0.0727  136 GLN C CG  
7277  C  CD  . GLN C 135 ? 1.3058 1.4165 1.7540 -0.3810 -0.0666 0.0698  136 GLN C CD  
7278  O  OE1 . GLN C 135 ? 1.3230 1.4551 1.7890 -0.3893 -0.0811 0.0757  136 GLN C OE1 
7279  N  NE2 . GLN C 135 ? 1.3186 1.4061 1.7344 -0.3781 -0.0639 0.0611  136 GLN C NE2 
7280  N  N   . ASN C 136 ? 0.8942 1.0240 1.3677 -0.3205 -0.0226 0.0814  137 ASN C N   
7281  C  CA  . ASN C 136 ? 0.8254 0.9343 1.2766 -0.3088 -0.0116 0.0774  137 ASN C CA  
7282  C  C   . ASN C 136 ? 0.7956 0.9128 1.2430 -0.2939 -0.0115 0.0782  137 ASN C C   
7283  O  O   . ASN C 136 ? 0.7524 0.8570 1.1859 -0.2825 -0.0023 0.0764  137 ASN C O   
7284  C  CB  . ASN C 136 ? 0.7967 0.9017 1.2552 -0.3047 0.0022  0.0812  137 ASN C CB  
7285  C  CG  . ASN C 136 ? 0.7809 0.8797 1.2463 -0.3195 0.0025  0.0818  137 ASN C CG  
7286  O  OD1 . ASN C 136 ? 0.8098 0.8883 1.2600 -0.3297 -0.0014 0.0757  137 ASN C OD1 
7287  N  ND2 . ASN C 136 ? 0.7411 0.8571 1.2295 -0.3215 0.0078  0.0887  137 ASN C ND2 
7288  N  N   . ALA C 137 ? 0.7869 0.9250 1.2477 -0.2944 -0.0225 0.0815  138 ALA C N   
7289  C  CA  . ALA C 137 ? 0.7788 0.9279 1.2411 -0.2807 -0.0231 0.0836  138 ALA C CA  
7290  C  C   . ALA C 137 ? 0.8427 0.9709 1.2739 -0.2750 -0.0223 0.0771  138 ALA C C   
7291  O  O   . ALA C 137 ? 0.8475 0.9757 1.2743 -0.2611 -0.0154 0.0775  138 ALA C O   
7292  C  CB  . ALA C 137 ? 0.7675 0.9405 1.2508 -0.2846 -0.0376 0.0888  138 ALA C CB  
7293  N  N   . ARG C 138 ? 0.8570 0.9675 1.2667 -0.2864 -0.0287 0.0706  139 ARG C N   
7294  C  CA  . ARG C 138 ? 0.8669 0.9575 1.2471 -0.2831 -0.0274 0.0631  139 ARG C CA  
7295  C  C   . ARG C 138 ? 0.8633 0.9353 1.2327 -0.2724 -0.0120 0.0595  139 ARG C C   
7296  O  O   . ARG C 138 ? 0.8565 0.9186 1.2097 -0.2636 -0.0080 0.0556  139 ARG C O   
7297  C  CB  . ARG C 138 ? 0.8980 0.9722 1.2570 -0.3000 -0.0356 0.0556  139 ARG C CB  
7298  N  N   . ALA C 139 ? 0.8089 0.8765 1.1882 -0.2736 -0.0040 0.0614  140 ALA C N   
7299  C  CA  . ALA C 139 ? 0.7654 0.8173 1.1385 -0.2636 0.0090  0.0606  140 ALA C CA  
7300  C  C   . ALA C 139 ? 0.7895 0.8549 1.1692 -0.2478 0.0138  0.0660  140 ALA C C   
7301  O  O   . ALA C 139 ? 0.8094 0.8633 1.1761 -0.2378 0.0196  0.0634  140 ALA C O   
7302  C  CB  . ALA C 139 ? 0.7088 0.7559 1.0930 -0.2692 0.0150  0.0639  140 ALA C CB  
7303  N  N   . PHE C 140 ? 0.7996 0.8895 1.2006 -0.2461 0.0118  0.0730  141 PHE C N   
7304  C  CA  . PHE C 140 ? 0.7668 0.8711 1.1756 -0.2325 0.0162  0.0774  141 PHE C CA  
7305  C  C   . PHE C 140 ? 0.8175 0.9224 1.2147 -0.2260 0.0104  0.0745  141 PHE C C   
7306  O  O   . PHE C 140 ? 0.8269 0.9295 1.2172 -0.2141 0.0161  0.0746  141 PHE C O   
7307  C  CB  . PHE C 140 ? 0.7295 0.8602 1.1659 -0.2335 0.0153  0.0839  141 PHE C CB  
7308  C  CG  . PHE C 140 ? 0.7298 0.8622 1.1786 -0.2415 0.0209  0.0870  141 PHE C CG  
7309  C  CD1 . PHE C 140 ? 0.7228 0.8516 1.1714 -0.2366 0.0329  0.0903  141 PHE C CD1 
7310  C  CD2 . PHE C 140 ? 0.7424 0.8801 1.2026 -0.2551 0.0138  0.0873  141 PHE C CD2 
7311  C  CE1 . PHE C 140 ? 0.7491 0.8789 1.2077 -0.2452 0.0382  0.0938  141 PHE C CE1 
7312  C  CE2 . PHE C 140 ? 0.7419 0.8812 1.2137 -0.2632 0.0193  0.0903  141 PHE C CE2 
7313  C  CZ  . PHE C 140 ? 0.7521 0.8873 1.2229 -0.2582 0.0318  0.0936  141 PHE C CZ  
7314  N  N   . ARG C 141 ? 0.8272 0.9350 1.2213 -0.2349 -0.0014 0.0724  142 ARG C N   
7315  C  CA  . ARG C 141 ? 0.8573 0.9650 1.2384 -0.2313 -0.0082 0.0702  142 ARG C CA  
7316  C  C   . ARG C 141 ? 0.9510 1.0356 1.3065 -0.2259 -0.0010 0.0632  142 ARG C C   
7317  O  O   . ARG C 141 ? 0.9264 1.0120 1.2758 -0.2151 0.0015  0.0633  142 ARG C O   
7318  C  CB  . ARG C 141 ? 0.7959 0.9068 1.1737 -0.2452 -0.0229 0.0693  142 ARG C CB  
7319  C  CG  . ARG C 141 ? 0.7723 0.8779 1.1298 -0.2449 -0.0301 0.0664  142 ARG C CG  
7320  C  CD  . ARG C 141 ? 0.7955 0.9048 1.1484 -0.2607 -0.0462 0.0669  142 ARG C CD  
7321  N  NE  . ARG C 141 ? 0.7871 0.9220 1.1706 -0.2629 -0.0565 0.0764  142 ARG C NE  
7322  C  CZ  . ARG C 141 ? 0.8254 0.9672 1.2225 -0.2756 -0.0636 0.0786  142 ARG C CZ  
7323  N  NH1 . ARG C 141 ? 0.8715 0.9953 1.2522 -0.2876 -0.0616 0.0718  142 ARG C NH1 
7324  N  NH2 . ARG C 141 ? 0.8188 0.9854 1.2477 -0.2763 -0.0723 0.0875  142 ARG C NH2 
7325  N  N   . ASP C 142 ? 1.0657 1.1296 1.4081 -0.2337 0.0028  0.0569  143 ASP C N   
7326  C  CA  . ASP C 142 ? 1.0887 1.1299 1.4109 -0.2292 0.0109  0.0494  143 ASP C CA  
7327  C  C   . ASP C 142 ? 0.9975 1.0372 1.3258 -0.2148 0.0218  0.0532  143 ASP C C   
7328  O  O   . ASP C 142 ? 1.0595 1.0895 1.3766 -0.2062 0.0270  0.0500  143 ASP C O   
7329  C  CB  . ASP C 142 ? 1.2069 1.2261 1.5182 -0.2410 0.0134  0.0417  143 ASP C CB  
7330  C  CG  . ASP C 142 ? 1.3247 1.3428 1.6248 -0.2569 0.0025  0.0368  143 ASP C CG  
7331  O  OD1 . ASP C 142 ? 1.3405 1.3783 1.6482 -0.2600 -0.0087 0.0424  143 ASP C OD1 
7332  O  OD2 . ASP C 142 ? 1.3713 1.3684 1.6557 -0.2669 0.0049  0.0275  143 ASP C OD2 
7333  N  N   . LEU C 143 ? 0.8576 0.9070 1.2031 -0.2133 0.0250  0.0602  144 LEU C N   
7334  C  CA  . LEU C 143 ? 0.7640 0.8145 1.1147 -0.2015 0.0338  0.0654  144 LEU C CA  
7335  C  C   . LEU C 143 ? 0.6446 0.7080 0.9950 -0.1902 0.0330  0.0675  144 LEU C C   
7336  O  O   . LEU C 143 ? 0.5658 0.6214 0.9084 -0.1805 0.0385  0.0669  144 LEU C O   
7337  C  CB  . LEU C 143 ? 0.7120 0.7736 1.0799 -0.2042 0.0368  0.0727  144 LEU C CB  
7338  C  CG  . LEU C 143 ? 0.7204 0.7808 1.0905 -0.1951 0.0457  0.0785  144 LEU C CG  
7339  C  CD1 . LEU C 143 ? 0.7146 0.7503 1.0735 -0.1932 0.0507  0.0766  144 LEU C CD1 
7340  C  CD2 . LEU C 143 ? 0.6744 0.7475 1.0597 -0.1998 0.0491  0.0853  144 LEU C CD2 
7341  N  N   . TYR C 144 ? 0.6303 0.7134 0.9912 -0.1917 0.0258  0.0701  145 TYR C N   
7342  C  CA  . TYR C 144 ? 0.6129 0.7085 0.9757 -0.1817 0.0242  0.0721  145 TYR C CA  
7343  C  C   . TYR C 144 ? 0.6282 0.7123 0.9715 -0.1790 0.0217  0.0666  145 TYR C C   
7344  O  O   . TYR C 144 ? 0.6289 0.7137 0.9677 -0.1686 0.0251  0.0672  145 TYR C O   
7345  C  CB  . TYR C 144 ? 0.6095 0.7277 0.9910 -0.1846 0.0160  0.0763  145 TYR C CB  
7346  C  CG  . TYR C 144 ? 0.5845 0.7191 0.9879 -0.1818 0.0219  0.0818  145 TYR C CG  
7347  C  CD1 . TYR C 144 ? 0.5883 0.7262 1.0037 -0.1906 0.0235  0.0837  145 TYR C CD1 
7348  C  CD2 . TYR C 144 ? 0.5559 0.7022 0.9673 -0.1711 0.0266  0.0845  145 TYR C CD2 
7349  C  CE1 . TYR C 144 ? 0.5873 0.7403 1.0218 -0.1891 0.0304  0.0880  145 TYR C CE1 
7350  C  CE2 . TYR C 144 ? 0.5489 0.7096 0.9788 -0.1696 0.0337  0.0881  145 TYR C CE2 
7351  C  CZ  . TYR C 144 ? 0.5342 0.6983 0.9754 -0.1788 0.0359  0.0898  145 TYR C CZ  
7352  O  OH  . TYR C 144 ? 0.5416 0.7200 1.0004 -0.1784 0.0444  0.0928  145 TYR C OH  
7353  N  N   . SER C 145 ? 0.7616 0.8351 1.0924 -0.1894 0.0162  0.0610  146 SER C N   
7354  C  CA  . SER C 145 ? 0.8358 0.8969 1.1457 -0.1891 0.0151  0.0546  146 SER C CA  
7355  C  C   . SER C 145 ? 0.8949 0.9391 1.1955 -0.1807 0.0264  0.0506  146 SER C C   
7356  O  O   . SER C 145 ? 0.9058 0.9480 1.1980 -0.1727 0.0288  0.0491  146 SER C O   
7357  C  CB  . SER C 145 ? 0.8989 0.9497 1.1949 -0.2042 0.0085  0.0482  146 SER C CB  
7358  O  OG  . SER C 145 ? 0.9153 0.9818 1.2233 -0.2132 -0.0028 0.0531  146 SER C OG  
7359  N  N   . GLU C 146 ? 0.9441 0.9762 1.2480 -0.1825 0.0329  0.0497  147 GLU C N   
7360  C  CA  . GLU C 146 ? 0.9674 0.9832 1.2667 -0.1748 0.0427  0.0472  147 GLU C CA  
7361  C  C   . GLU C 146 ? 0.8761 0.9018 1.1841 -0.1619 0.0465  0.0546  147 GLU C C   
7362  O  O   . GLU C 146 ? 0.8988 0.9164 1.2019 -0.1535 0.0518  0.0533  147 GLU C O   
7363  C  CB  . GLU C 146 ? 1.0744 1.0744 1.3774 -0.1806 0.0475  0.0456  147 GLU C CB  
7364  C  CG  . GLU C 146 ? 1.1713 1.1477 1.4647 -0.1796 0.0550  0.0370  147 GLU C CG  
7365  C  CD  . GLU C 146 ? 1.2596 1.2246 1.5373 -0.1914 0.0531  0.0259  147 GLU C CD  
7366  O  OE1 . GLU C 146 ? 1.2752 1.2512 1.5490 -0.2006 0.0441  0.0261  147 GLU C OE1 
7367  O  OE2 . GLU C 146 ? 1.2945 1.2397 1.5643 -0.1919 0.0606  0.0168  147 GLU C OE2 
7368  N  N   . LEU C 147 ? 0.7240 0.7674 1.0451 -0.1609 0.0442  0.0621  148 LEU C N   
7369  C  CA  . LEU C 147 ? 0.6196 0.6736 0.9466 -0.1502 0.0475  0.0682  148 LEU C CA  
7370  C  C   . LEU C 147 ? 0.5905 0.6504 0.9107 -0.1434 0.0448  0.0662  148 LEU C C   
7371  O  O   . LEU C 147 ? 0.5851 0.6438 0.9026 -0.1341 0.0489  0.0678  148 LEU C O   
7372  C  CB  . LEU C 147 ? 0.5940 0.6664 0.9363 -0.1518 0.0468  0.0746  148 LEU C CB  
7373  C  CG  . LEU C 147 ? 0.5641 0.6336 0.9137 -0.1557 0.0518  0.0794  148 LEU C CG  
7374  C  CD1 . LEU C 147 ? 0.5094 0.5989 0.8731 -0.1558 0.0534  0.0848  148 LEU C CD1 
7375  C  CD2 . LEU C 147 ? 0.5174 0.5725 0.8604 -0.1497 0.0579  0.0818  148 LEU C CD2 
7376  N  N   . ARG C 148 ? 0.5735 0.6396 0.8909 -0.1490 0.0372  0.0636  149 ARG C N   
7377  C  CA  . ARG C 148 ? 0.6152 0.6857 0.9249 -0.1445 0.0335  0.0621  149 ARG C CA  
7378  C  C   . ARG C 148 ? 0.6282 0.6816 0.9219 -0.1414 0.0386  0.0560  149 ARG C C   
7379  O  O   . ARG C 148 ? 0.5791 0.6343 0.8692 -0.1328 0.0406  0.0566  149 ARG C O   
7380  C  CB  . ARG C 148 ? 0.4960 0.5739 0.8042 -0.1534 0.0228  0.0613  149 ARG C CB  
7381  C  CG  . ARG C 148 ? 0.4834 0.5827 0.8112 -0.1527 0.0168  0.0681  149 ARG C CG  
7382  C  CD  . ARG C 148 ? 0.4892 0.5959 0.8155 -0.1595 0.0044  0.0690  149 ARG C CD  
7383  N  NE  . ARG C 148 ? 0.5964 0.7217 0.9458 -0.1627 -0.0023 0.0750  149 ARG C NE  
7384  C  CZ  . ARG C 148 ? 0.6207 0.7482 0.9784 -0.1725 -0.0055 0.0755  149 ARG C CZ  
7385  N  NH1 . ARG C 148 ? 0.5769 0.6879 0.9204 -0.1803 -0.0026 0.0701  149 ARG C NH1 
7386  N  NH2 . ARG C 148 ? 0.6263 0.7725 1.0084 -0.1746 -0.0112 0.0811  149 ARG C NH2 
7387  N  N   . LEU C 149 ? 0.7330 0.7699 1.0183 -0.1486 0.0412  0.0496  150 LEU C N   
7388  C  CA  . LEU C 149 ? 0.8077 0.8277 1.0810 -0.1459 0.0481  0.0425  150 LEU C CA  
7389  C  C   . LEU C 149 ? 0.8320 0.8484 1.1132 -0.1344 0.0557  0.0463  150 LEU C C   
7390  O  O   . LEU C 149 ? 0.8578 0.8703 1.1343 -0.1274 0.0596  0.0441  150 LEU C O   
7391  C  CB  . LEU C 149 ? 0.8599 0.8618 1.1251 -0.1562 0.0509  0.0340  150 LEU C CB  
7392  C  CG  . LEU C 149 ? 0.9089 0.9073 1.1565 -0.1676 0.0456  0.0268  150 LEU C CG  
7393  C  CD1 . LEU C 149 ? 0.9305 0.9184 1.1740 -0.1812 0.0442  0.0214  150 LEU C CD1 
7394  C  CD2 . LEU C 149 ? 0.9193 0.9058 1.1519 -0.1654 0.0523  0.0186  150 LEU C CD2 
7395  N  N   . TYR C 150 ? 0.8383 0.8564 1.1315 -0.1334 0.0572  0.0524  151 TYR C N   
7396  C  CA  . TYR C 150 ? 0.8148 0.8307 1.1154 -0.1243 0.0623  0.0582  151 TYR C CA  
7397  C  C   . TYR C 150 ? 0.7819 0.8109 1.0825 -0.1153 0.0613  0.0624  151 TYR C C   
7398  O  O   . TYR C 150 ? 0.7947 0.8190 1.0944 -0.1076 0.0649  0.0629  151 TYR C O   
7399  C  CB  . TYR C 150 ? 0.8565 0.8746 1.1675 -0.1273 0.0627  0.0652  151 TYR C CB  
7400  C  CG  . TYR C 150 ? 0.9263 0.9381 1.2431 -0.1209 0.0669  0.0720  151 TYR C CG  
7401  C  CD1 . TYR C 150 ? 0.9735 0.9668 1.2925 -0.1196 0.0710  0.0701  151 TYR C CD1 
7402  C  CD2 . TYR C 150 ? 0.9356 0.9598 1.2563 -0.1169 0.0666  0.0805  151 TYR C CD2 
7403  C  CE1 . TYR C 150 ? 0.9833 0.9712 1.3094 -0.1142 0.0729  0.0780  151 TYR C CE1 
7404  C  CE2 . TYR C 150 ? 0.9511 0.9694 1.2751 -0.1128 0.0689  0.0878  151 TYR C CE2 
7405  C  CZ  . TYR C 150 ? 0.9781 0.9785 1.3054 -0.1114 0.0712  0.0874  151 TYR C CZ  
7406  O  OH  . TYR C 150 ? 1.0029 0.9977 1.3352 -0.1076 0.0716  0.0963  151 TYR C OH  
7407  N  N   . TYR C 151 ? 0.6989 0.7445 1.0024 -0.1164 0.0563  0.0654  152 TYR C N   
7408  C  CA  . TYR C 151 ? 0.7095 0.7676 1.0139 -0.1085 0.0554  0.0687  152 TYR C CA  
7409  C  C   . TYR C 151 ? 0.6924 0.7472 0.9864 -0.1053 0.0544  0.0638  152 TYR C C   
7410  O  O   . TYR C 151 ? 0.6941 0.7519 0.9871 -0.0974 0.0562  0.0657  152 TYR C O   
7411  C  CB  . TYR C 151 ? 0.6312 0.7070 0.9443 -0.1108 0.0508  0.0720  152 TYR C CB  
7412  C  CG  . TYR C 151 ? 0.5512 0.6386 0.8651 -0.1037 0.0490  0.0736  152 TYR C CG  
7413  C  CD1 . TYR C 151 ? 0.4261 0.5178 0.7423 -0.0964 0.0534  0.0774  152 TYR C CD1 
7414  C  CD2 . TYR C 151 ? 0.4354 0.5285 0.7470 -0.1053 0.0425  0.0716  152 TYR C CD2 
7415  C  CE1 . TYR C 151 ? 0.4874 0.5883 0.8044 -0.0903 0.0522  0.0781  152 TYR C CE1 
7416  C  CE2 . TYR C 151 ? 0.4241 0.5266 0.7376 -0.0989 0.0406  0.0733  152 TYR C CE2 
7417  C  CZ  . TYR C 151 ? 0.4137 0.5198 0.7302 -0.0912 0.0460  0.0761  152 TYR C CZ  
7418  O  OH  . TYR C 151 ? 0.4218 0.5361 0.7404 -0.0852 0.0446  0.0772  152 TYR C OH  
7419  N  N   . ARG C 152 ? 0.7890 0.8377 1.0743 -0.1125 0.0517  0.0576  153 ARG C N   
7420  C  CA  . ARG C 152 ? 0.8567 0.9032 1.1299 -0.1119 0.0503  0.0531  153 ARG C CA  
7421  C  C   . ARG C 152 ? 0.9101 0.9430 1.1776 -0.1071 0.0582  0.0484  153 ARG C C   
7422  O  O   . ARG C 152 ? 0.9094 0.9398 1.1667 -0.1065 0.0589  0.0442  153 ARG C O   
7423  C  CB  . ARG C 152 ? 0.9269 0.9706 1.1898 -0.1233 0.0446  0.0480  153 ARG C CB  
7424  C  CG  . ARG C 152 ? 0.9792 1.0364 1.2404 -0.1250 0.0352  0.0514  153 ARG C CG  
7425  C  CD  . ARG C 152 ? 1.0479 1.1000 1.2946 -0.1376 0.0287  0.0468  153 ARG C CD  
7426  N  NE  . ARG C 152 ? 1.1102 1.1456 1.3388 -0.1408 0.0353  0.0378  153 ARG C NE  
7427  C  CZ  . ARG C 152 ? 1.1643 1.1881 1.3776 -0.1532 0.0347  0.0305  153 ARG C CZ  
7428  N  NH1 . ARG C 152 ? 1.1773 1.2048 1.3911 -0.1637 0.0262  0.0319  153 ARG C NH1 
7429  N  NH2 . ARG C 152 ? 1.1944 1.2031 1.3922 -0.1558 0.0431  0.0212  153 ARG C NH2 
7430  N  N   . GLY C 153 ? 0.9275 0.9518 1.2029 -0.1040 0.0639  0.0495  154 GLY C N   
7431  C  CA  . GLY C 153 ? 0.9863 0.9989 1.2620 -0.0984 0.0712  0.0461  154 GLY C CA  
7432  C  C   . GLY C 153 ? 1.0484 1.0431 1.3217 -0.1041 0.0771  0.0376  154 GLY C C   
7433  O  O   . GLY C 153 ? 1.0631 1.0469 1.3409 -0.0996 0.0843  0.0341  154 GLY C O   
7434  N  N   . ALA C 154 ? 1.0813 1.0729 1.3490 -0.1144 0.0742  0.0338  155 ALA C N   
7435  C  CA  . ALA C 154 ? 1.1143 1.0877 1.3805 -0.1208 0.0803  0.0254  155 ALA C CA  
7436  C  C   . ALA C 154 ? 1.1720 1.1418 1.4527 -0.1198 0.0806  0.0317  155 ALA C C   
7437  O  O   . ALA C 154 ? 1.2004 1.1779 1.4832 -0.1250 0.0748  0.0364  155 ALA C O   
7438  C  CB  . ALA C 154 ? 1.0906 1.0609 1.3412 -0.1340 0.0767  0.0178  155 ALA C CB  
7439  N  N   . ASN C 155 ? 1.1966 1.1549 1.4886 -0.1136 0.0871  0.0322  156 ASN C N   
7440  C  CA  . ASN C 155 ? 1.1973 1.1546 1.5038 -0.1107 0.0861  0.0419  156 ASN C CA  
7441  C  C   . ASN C 155 ? 1.2161 1.1546 1.5298 -0.1158 0.0906  0.0379  156 ASN C C   
7442  O  O   . ASN C 155 ? 1.1938 1.1168 1.5107 -0.1149 0.0981  0.0296  156 ASN C O   
7443  C  CB  . ASN C 155 ? 1.2160 1.1764 1.5327 -0.0993 0.0872  0.0497  156 ASN C CB  
7444  C  CG  . ASN C 155 ? 1.2369 1.2010 1.5637 -0.0976 0.0835  0.0624  156 ASN C CG  
7445  O  OD1 . ASN C 155 ? 1.2641 1.2220 1.5948 -0.1037 0.0828  0.0645  156 ASN C OD1 
7446  N  ND2 . ASN C 155 ? 1.2330 1.2071 1.5627 -0.0903 0.0811  0.0709  156 ASN C ND2 
7447  N  N   . LEU C 156 ? 1.2124 1.1526 1.5297 -0.1215 0.0865  0.0437  157 LEU C N   
7448  C  CA  . LEU C 156 ? 1.2760 1.1993 1.6019 -0.1265 0.0896  0.0426  157 LEU C CA  
7449  C  C   . LEU C 156 ? 1.4132 1.3402 1.7510 -0.1236 0.0861  0.0567  157 LEU C C   
7450  O  O   . LEU C 156 ? 1.3588 1.3028 1.6945 -0.1209 0.0815  0.0652  157 LEU C O   
7451  C  CB  . LEU C 156 ? 1.1780 1.0987 1.4943 -0.1394 0.0875  0.0355  157 LEU C CB  
7452  C  CG  . LEU C 156 ? 1.1122 1.0147 1.4344 -0.1476 0.0903  0.0320  157 LEU C CG  
7453  C  CD1 . LEU C 156 ? 1.0952 0.9763 1.4294 -0.1423 0.0990  0.0277  157 LEU C CD1 
7454  C  CD2 . LEU C 156 ? 1.0834 0.9830 1.3914 -0.1606 0.0888  0.0213  157 LEU C CD2 
7455  N  N   . HIS C 157 ? 1.6252 1.5357 1.9750 -0.1246 0.0887  0.0592  158 HIS C N   
7456  C  CA  . HIS C 157 ? 1.6512 1.5636 2.0093 -0.1255 0.0848  0.0728  158 HIS C CA  
7457  C  C   . HIS C 157 ? 1.6126 1.5387 1.9625 -0.1346 0.0804  0.0748  158 HIS C C   
7458  O  O   . HIS C 157 ? 1.6634 1.5832 2.0109 -0.1439 0.0807  0.0686  158 HIS C O   
7459  C  CB  . HIS C 157 ? 1.6996 1.5902 2.0720 -0.1273 0.0876  0.0745  158 HIS C CB  
7460  N  N   . LEU C 158 ? 1.3758 1.3208 1.7221 -0.1322 0.0767  0.0827  159 LEU C N   
7461  C  CA  . LEU C 158 ? 1.2393 1.1995 1.5815 -0.1397 0.0734  0.0847  159 LEU C CA  
7462  C  C   . LEU C 158 ? 1.2109 1.1637 1.5598 -0.1480 0.0732  0.0910  159 LEU C C   
7463  O  O   . LEU C 158 ? 1.2317 1.1893 1.5800 -0.1572 0.0718  0.0888  159 LEU C O   
7464  C  CB  . LEU C 158 ? 1.0827 1.0629 1.4220 -0.1349 0.0715  0.0915  159 LEU C CB  
7465  C  CG  . LEU C 158 ? 0.9243 0.9226 1.2630 -0.1413 0.0694  0.0929  159 LEU C CG  
7466  C  CD1 . LEU C 158 ? 0.8254 0.8313 1.1599 -0.1434 0.0668  0.0834  159 LEU C CD1 
7467  C  CD2 . LEU C 158 ? 0.8510 0.8649 1.1888 -0.1371 0.0698  0.1005  159 LEU C CD2 
7468  N  N   . GLU C 159 ? 1.2313 1.1721 1.5872 -0.1450 0.0740  0.0995  160 GLU C N   
7469  C  CA  . GLU C 159 ? 1.2844 1.2149 1.6468 -0.1526 0.0736  0.1070  160 GLU C CA  
7470  C  C   . GLU C 159 ? 1.2598 1.1759 1.6249 -0.1606 0.0753  0.0978  160 GLU C C   
7471  O  O   . GLU C 159 ? 1.3020 1.2183 1.6685 -0.1705 0.0743  0.1002  160 GLU C O   
7472  C  CB  . GLU C 159 ? 1.3819 1.2988 1.7529 -0.1473 0.0730  0.1174  160 GLU C CB  
7473  C  CG  . GLU C 159 ? 1.4567 1.3856 1.8239 -0.1458 0.0699  0.1310  160 GLU C CG  
7474  C  CD  . GLU C 159 ? 1.5334 1.4482 1.9094 -0.1421 0.0671  0.1431  160 GLU C CD  
7475  O  OE1 . GLU C 159 ? 1.5677 1.4645 1.9559 -0.1381 0.0682  0.1399  160 GLU C OE1 
7476  O  OE2 . GLU C 159 ? 1.5578 1.4792 1.9291 -0.1438 0.0638  0.1558  160 GLU C OE2 
7477  N  N   . GLU C 160 ? 1.1840 1.0873 1.5493 -0.1572 0.0784  0.0867  161 GLU C N   
7478  C  CA  . GLU C 160 ? 1.1326 1.0199 1.4983 -0.1654 0.0810  0.0760  161 GLU C CA  
7479  C  C   . GLU C 160 ? 1.0368 0.9371 1.3927 -0.1753 0.0779  0.0697  161 GLU C C   
7480  O  O   . GLU C 160 ? 1.0522 0.9480 1.4100 -0.1859 0.0768  0.0694  161 GLU C O   
7481  C  CB  . GLU C 160 ? 1.1473 1.0195 1.5133 -0.1599 0.0866  0.0639  161 GLU C CB  
7482  N  N   . THR C 161 ? 0.9264 0.8429 1.2730 -0.1720 0.0760  0.0654  162 THR C N   
7483  C  CA  . THR C 161 ? 0.8439 0.7749 1.1832 -0.1804 0.0714  0.0608  162 THR C CA  
7484  C  C   . THR C 161 ? 0.7481 0.6926 1.0942 -0.1870 0.0681  0.0700  162 THR C C   
7485  O  O   . THR C 161 ? 0.6621 0.6065 1.0091 -0.1982 0.0657  0.0672  162 THR C O   
7486  C  CB  . THR C 161 ? 0.8210 0.7691 1.1523 -0.1740 0.0689  0.0585  162 THR C CB  
7487  O  OG1 . THR C 161 ? 0.8249 0.7620 1.1516 -0.1660 0.0733  0.0524  162 THR C OG1 
7488  C  CG2 . THR C 161 ? 0.8350 0.7928 1.1589 -0.1833 0.0633  0.0519  162 THR C CG2 
7489  N  N   . LEU C 162 ? 0.7639 0.7197 1.1144 -0.1809 0.0685  0.0806  163 LEU C N   
7490  C  CA  . LEU C 162 ? 0.7857 0.7547 1.1424 -0.1871 0.0675  0.0892  163 LEU C CA  
7491  C  C   . LEU C 162 ? 0.8479 0.8015 1.2103 -0.1966 0.0686  0.0923  163 LEU C C   
7492  O  O   . LEU C 162 ? 0.8201 0.7812 1.1868 -0.2067 0.0670  0.0932  163 LEU C O   
7493  C  CB  . LEU C 162 ? 0.7641 0.7440 1.1214 -0.1798 0.0692  0.0994  163 LEU C CB  
7494  C  CG  . LEU C 162 ? 0.7603 0.7598 1.1140 -0.1725 0.0682  0.0976  163 LEU C CG  
7495  C  CD1 . LEU C 162 ? 0.7653 0.7711 1.1173 -0.1657 0.0705  0.1065  163 LEU C CD1 
7496  C  CD2 . LEU C 162 ? 0.7386 0.7576 1.0973 -0.1791 0.0658  0.0955  163 LEU C CD2 
7497  N  N   . ALA C 163 ? 0.9116 0.8436 1.2761 -0.1933 0.0711  0.0939  164 ALA C N   
7498  C  CA  . ALA C 163 ? 1.0423 0.9567 1.4135 -0.2016 0.0720  0.0974  164 ALA C CA  
7499  C  C   . ALA C 163 ? 1.0738 0.9816 1.4441 -0.2127 0.0710  0.0870  164 ALA C C   
7500  O  O   . ALA C 163 ? 1.1130 1.0228 1.4876 -0.2234 0.0698  0.0903  164 ALA C O   
7501  C  CB  . ALA C 163 ? 1.0412 0.9326 1.4178 -0.1948 0.0744  0.0997  164 ALA C CB  
7502  N  N   . GLU C 164 ? 1.1297 1.0296 1.4934 -0.2111 0.0717  0.0744  165 GLU C N   
7503  C  CA  . GLU C 164 ? 1.1626 1.0547 1.5222 -0.2228 0.0704  0.0635  165 GLU C CA  
7504  C  C   . GLU C 164 ? 1.1269 1.0422 1.4855 -0.2312 0.0644  0.0645  165 GLU C C   
7505  O  O   . GLU C 164 ? 1.1774 1.0903 1.5381 -0.2438 0.0620  0.0623  165 GLU C O   
7506  C  CB  . GLU C 164 ? 1.2676 1.1481 1.6169 -0.2202 0.0729  0.0495  165 GLU C CB  
7507  C  CG  . GLU C 164 ? 1.3876 1.2459 1.7333 -0.2314 0.0752  0.0377  165 GLU C CG  
7508  C  CD  . GLU C 164 ? 1.4843 1.3224 1.8248 -0.2263 0.0824  0.0255  165 GLU C CD  
7509  O  OE1 . GLU C 164 ? 1.5174 1.3535 1.8433 -0.2322 0.0825  0.0130  165 GLU C OE1 
7510  O  OE2 . GLU C 164 ? 1.5139 1.3381 1.8652 -0.2170 0.0881  0.0288  165 GLU C OE2 
7511  N  N   . PHE C 165 ? 1.0201 0.9578 1.3774 -0.2243 0.0621  0.0681  166 PHE C N   
7512  C  CA  . PHE C 165 ? 0.9445 0.9065 1.3060 -0.2304 0.0568  0.0705  166 PHE C CA  
7513  C  C   . PHE C 165 ? 0.8931 0.8608 1.2663 -0.2384 0.0575  0.0793  166 PHE C C   
7514  O  O   . PHE C 165 ? 0.8946 0.8683 1.2729 -0.2500 0.0538  0.0777  166 PHE C O   
7515  C  CB  . PHE C 165 ? 0.8543 0.8375 1.2157 -0.2199 0.0558  0.0740  166 PHE C CB  
7516  C  CG  . PHE C 165 ? 0.8106 0.8196 1.1822 -0.2243 0.0518  0.0781  166 PHE C CG  
7517  C  CD1 . PHE C 165 ? 0.7764 0.7961 1.1484 -0.2307 0.0444  0.0729  166 PHE C CD1 
7518  C  CD2 . PHE C 165 ? 0.7685 0.7911 1.1498 -0.2225 0.0556  0.0874  166 PHE C CD2 
7519  C  CE1 . PHE C 165 ? 0.7469 0.7911 1.1331 -0.2341 0.0406  0.0772  166 PHE C CE1 
7520  C  CE2 . PHE C 165 ? 0.7379 0.7846 1.1319 -0.2262 0.0537  0.0902  166 PHE C CE2 
7521  C  CZ  . PHE C 165 ? 0.7335 0.7913 1.1319 -0.2314 0.0461  0.0853  166 PHE C CZ  
7522  N  N   . TRP C 166 ? 0.8794 0.8453 1.2562 -0.2331 0.0622  0.0889  167 TRP C N   
7523  C  CA  . TRP C 166 ? 0.8493 0.8204 1.2350 -0.2410 0.0640  0.0982  167 TRP C CA  
7524  C  C   . TRP C 166 ? 0.8784 0.8300 1.2669 -0.2525 0.0637  0.0966  167 TRP C C   
7525  O  O   . TRP C 166 ? 0.8397 0.7988 1.2361 -0.2635 0.0631  0.1001  167 TRP C O   
7526  C  CB  . TRP C 166 ? 0.8875 0.8577 1.2725 -0.2341 0.0684  0.1091  167 TRP C CB  
7527  C  CG  . TRP C 166 ? 0.8821 0.8741 1.2655 -0.2257 0.0697  0.1117  167 TRP C CG  
7528  C  CD1 . TRP C 166 ? 0.8828 0.8738 1.2593 -0.2136 0.0706  0.1128  167 TRP C CD1 
7529  C  CD2 . TRP C 166 ? 0.8896 0.9072 1.2803 -0.2288 0.0705  0.1131  167 TRP C CD2 
7530  N  NE1 . TRP C 166 ? 0.8719 0.8853 1.2492 -0.2094 0.0720  0.1145  167 TRP C NE1 
7531  C  CE2 . TRP C 166 ? 0.8891 0.9190 1.2759 -0.2183 0.0723  0.1144  167 TRP C CE2 
7532  C  CE3 . TRP C 166 ? 0.9157 0.9473 1.3178 -0.2396 0.0701  0.1131  167 TRP C CE3 
7533  C  CZ2 . TRP C 166 ? 0.8913 0.9457 1.2855 -0.2179 0.0746  0.1151  167 TRP C CZ2 
7534  C  CZ3 . TRP C 166 ? 0.9023 0.9595 1.3136 -0.2389 0.0722  0.1143  167 TRP C CZ3 
7535  C  CH2 . TRP C 166 ? 0.9023 0.9701 1.3097 -0.2279 0.0748  0.1149  167 TRP C CH2 
7536  N  N   . ALA C 167 ? 0.8615 0.7880 1.2451 -0.2503 0.0649  0.0910  168 ALA C N   
7537  C  CA  . ALA C 167 ? 0.9056 0.8106 1.2920 -0.2610 0.0652  0.0880  168 ALA C CA  
7538  C  C   . ALA C 167 ? 0.9032 0.8141 1.2885 -0.2734 0.0605  0.0789  168 ALA C C   
7539  O  O   . ALA C 167 ? 0.9088 0.8224 1.3013 -0.2855 0.0590  0.0820  168 ALA C O   
7540  C  CB  . ALA C 167 ? 0.8949 0.7721 1.2782 -0.2550 0.0686  0.0820  168 ALA C CB  
7541  N  N   . ARG C 168 ? 0.9127 0.8258 1.2886 -0.2711 0.0578  0.0683  169 ARG C N   
7542  C  CA  . ARG C 168 ? 0.9348 0.8531 1.3071 -0.2834 0.0516  0.0599  169 ARG C CA  
7543  C  C   . ARG C 168 ? 0.9805 0.9265 1.3645 -0.2900 0.0465  0.0670  169 ARG C C   
7544  O  O   . ARG C 168 ? 1.0400 0.9873 1.4297 -0.3038 0.0428  0.0662  169 ARG C O   
7545  C  CB  . ARG C 168 ? 0.8842 0.8039 1.2427 -0.2793 0.0488  0.0497  169 ARG C CB  
7546  N  N   . LEU C 169 ? 0.9324 0.9005 1.3213 -0.2803 0.0470  0.0737  170 LEU C N   
7547  C  CA  . LEU C 169 ? 0.8915 0.8873 1.2949 -0.2847 0.0441  0.0801  170 LEU C CA  
7548  C  C   . LEU C 169 ? 0.9100 0.9048 1.3246 -0.2935 0.0480  0.0879  170 LEU C C   
7549  O  O   . LEU C 169 ? 0.9362 0.9468 1.3636 -0.3037 0.0450  0.0899  170 LEU C O   
7550  C  CB  . LEU C 169 ? 0.8295 0.8457 1.2363 -0.2718 0.0463  0.0852  170 LEU C CB  
7551  C  CG  . LEU C 169 ? 0.7781 0.8238 1.2028 -0.2748 0.0452  0.0907  170 LEU C CG  
7552  C  CD1 . LEU C 169 ? 0.7515 0.8108 1.1827 -0.2821 0.0350  0.0858  170 LEU C CD1 
7553  C  CD2 . LEU C 169 ? 0.7410 0.8025 1.1682 -0.2620 0.0500  0.0952  170 LEU C CD2 
7554  N  N   . LEU C 170 ? 0.9004 0.8769 1.3113 -0.2901 0.0543  0.0928  171 LEU C N   
7555  C  CA  . LEU C 170 ? 0.8667 0.8395 1.2859 -0.2994 0.0579  0.1011  171 LEU C CA  
7556  C  C   . LEU C 170 ? 0.8794 0.8393 1.3013 -0.3142 0.0543  0.0960  171 LEU C C   
7557  O  O   . LEU C 170 ? 0.8475 0.8181 1.2808 -0.3256 0.0537  0.1002  171 LEU C O   
7558  C  CB  . LEU C 170 ? 0.8971 0.8507 1.3111 -0.2931 0.0636  0.1086  171 LEU C CB  
7559  C  CG  . LEU C 170 ? 0.9130 0.8593 1.3333 -0.3035 0.0668  0.1185  171 LEU C CG  
7560  C  CD1 . LEU C 170 ? 0.9070 0.8808 1.3372 -0.3097 0.0693  0.1250  171 LEU C CD1 
7561  C  CD2 . LEU C 170 ? 0.9221 0.8494 1.3370 -0.2969 0.0703  0.1274  171 LEU C CD2 
7562  N  N   . GLU C 171 ? 0.9303 0.8669 1.3418 -0.3146 0.0525  0.0864  172 GLU C N   
7563  C  CA  . GLU C 171 ? 0.9794 0.9015 1.3910 -0.3295 0.0491  0.0797  172 GLU C CA  
7564  C  C   . GLU C 171 ? 0.9923 0.9373 1.4104 -0.3402 0.0412  0.0768  172 GLU C C   
7565  O  O   . GLU C 171 ? 0.9696 0.9213 1.3992 -0.3531 0.0394  0.0805  172 GLU C O   
7566  C  CB  . GLU C 171 ? 1.0188 0.9134 1.4164 -0.3278 0.0497  0.0675  172 GLU C CB  
7567  C  CG  . GLU C 171 ? 1.0451 0.9139 1.4414 -0.3191 0.0569  0.0700  172 GLU C CG  
7568  C  CD  . GLU C 171 ? 1.0722 0.9134 1.4581 -0.3184 0.0594  0.0563  172 GLU C CD  
7569  O  OE1 . GLU C 171 ? 1.0827 0.9239 1.4589 -0.3263 0.0555  0.0445  172 GLU C OE1 
7570  O  OE2 . GLU C 171 ? 1.0902 0.9098 1.4781 -0.3105 0.0653  0.0573  172 GLU C OE2 
7571  N  N   . ARG C 172 ? 1.0417 0.9990 1.4535 -0.3349 0.0361  0.0711  173 ARG C N   
7572  C  CA  . ARG C 172 ? 1.0878 1.0661 1.5061 -0.3444 0.0264  0.0688  173 ARG C CA  
7573  C  C   . ARG C 172 ? 1.0927 1.0994 1.5333 -0.3474 0.0264  0.0790  173 ARG C C   
7574  O  O   . ARG C 172 ? 1.1125 1.1278 1.5647 -0.3612 0.0212  0.0797  173 ARG C O   
7575  C  CB  . ARG C 172 ? 1.0993 1.0872 1.5078 -0.3366 0.0209  0.0634  173 ARG C CB  
7576  C  CG  . ARG C 172 ? 1.1594 1.1321 1.5509 -0.3468 0.0138  0.0516  173 ARG C CG  
7577  C  CD  . ARG C 172 ? 1.1959 1.1786 1.5766 -0.3405 0.0077  0.0476  173 ARG C CD  
7578  N  NE  . ARG C 172 ? 1.2182 1.2332 1.6157 -0.3408 -0.0009 0.0550  173 ARG C NE  
7579  C  CZ  . ARG C 172 ? 1.2372 1.2644 1.6297 -0.3421 -0.0112 0.0530  173 ARG C CZ  
7580  N  NH1 . ARG C 172 ? 1.2345 1.2910 1.6474 -0.3416 -0.0189 0.0607  173 ARG C NH1 
7581  N  NH2 . ARG C 172 ? 1.2660 1.2756 1.6338 -0.3445 -0.0137 0.0434  173 ARG C NH2 
7582  N  N   . LEU C 173 ? 1.0650 1.0857 1.5119 -0.3352 0.0329  0.0863  174 LEU C N   
7583  C  CA  . LEU C 173 ? 1.0320 1.0791 1.5000 -0.3377 0.0358  0.0949  174 LEU C CA  
7584  C  C   . LEU C 173 ? 1.0513 1.0915 1.5276 -0.3503 0.0400  0.1000  174 LEU C C   
7585  O  O   . LEU C 173 ? 1.0845 1.1445 1.5798 -0.3600 0.0388  0.1036  174 LEU C O   
7586  C  CB  . LEU C 173 ? 0.9660 1.0243 1.4349 -0.3234 0.0439  0.1008  174 LEU C CB  
7587  C  CG  . LEU C 173 ? 0.8944 0.9759 1.3693 -0.3135 0.0405  0.0994  174 LEU C CG  
7588  C  CD1 . LEU C 173 ? 0.8638 0.9537 1.3384 -0.3010 0.0500  0.1047  174 LEU C CD1 
7589  C  CD2 . LEU C 173 ? 0.8737 0.9820 1.3726 -0.3222 0.0346  0.1006  174 LEU C CD2 
7590  N  N   . PHE C 174 ? 1.0806 1.0930 1.5442 -0.3501 0.0450  0.1009  175 PHE C N   
7591  C  CA  . PHE C 174 ? 1.0673 1.0689 1.5366 -0.3623 0.0487  0.1063  175 PHE C CA  
7592  C  C   . PHE C 174 ? 1.0787 1.0823 1.5559 -0.3782 0.0407  0.1010  175 PHE C C   
7593  O  O   . PHE C 174 ? 1.0636 1.0877 1.5589 -0.3877 0.0403  0.1056  175 PHE C O   
7594  C  CB  . PHE C 174 ? 1.1342 1.1026 1.5895 -0.3588 0.0533  0.1075  175 PHE C CB  
7595  C  CG  . PHE C 174 ? 1.2085 1.1585 1.6676 -0.3727 0.0548  0.1111  175 PHE C CG  
7596  C  CD1 . PHE C 174 ? 1.2334 1.1873 1.6993 -0.3770 0.0611  0.1230  175 PHE C CD1 
7597  C  CD2 . PHE C 174 ? 1.2634 1.1886 1.7167 -0.3809 0.0509  0.1026  175 PHE C CD2 
7598  C  CE1 . PHE C 174 ? 1.2743 1.2103 1.7435 -0.3899 0.0623  0.1274  175 PHE C CE1 
7599  C  CE2 . PHE C 174 ? 1.2994 1.2057 1.7567 -0.3933 0.0526  0.1061  175 PHE C CE2 
7600  C  CZ  . PHE C 174 ? 1.3069 1.2188 1.7726 -0.3975 0.0579  0.1191  175 PHE C CZ  
7601  N  N   . LYS C 175 ? 1.0742 1.0592 1.5386 -0.3816 0.0343  0.0908  176 LYS C N   
7602  C  CA  . LYS C 175 ? 1.1299 1.1157 1.5997 -0.3987 0.0259  0.0858  176 LYS C CA  
7603  C  C   . LYS C 175 ? 1.2449 1.2647 1.7322 -0.4036 0.0175  0.0874  176 LYS C C   
7604  O  O   . LYS C 175 ? 1.2243 1.2529 1.7254 -0.4186 0.0124  0.0886  176 LYS C O   
7605  C  CB  . LYS C 175 ? 1.0759 1.0353 1.5256 -0.4025 0.0210  0.0733  176 LYS C CB  
7606  C  CG  . LYS C 175 ? 1.0771 1.0040 1.5116 -0.3941 0.0292  0.0700  176 LYS C CG  
7607  C  CD  . LYS C 175 ? 1.0790 0.9848 1.4939 -0.3952 0.0261  0.0559  176 LYS C CD  
7608  C  CE  . LYS C 175 ? 1.1003 1.0271 1.5098 -0.3922 0.0179  0.0517  176 LYS C CE  
7609  N  NZ  . LYS C 175 ? 1.1136 1.0199 1.5007 -0.3893 0.0180  0.0389  176 LYS C NZ  
7610  N  N   . GLN C 176 ? 1.4150 1.4540 1.9040 -0.3912 0.0158  0.0879  177 GLN C N   
7611  C  CA  . GLN C 176 ? 1.4540 1.5258 1.9635 -0.3941 0.0075  0.0903  177 GLN C CA  
7612  C  C   . GLN C 176 ? 1.3997 1.4953 1.9369 -0.3992 0.0130  0.0993  177 GLN C C   
7613  O  O   . GLN C 176 ? 1.4202 1.5403 1.9800 -0.4071 0.0058  0.1014  177 GLN C O   
7614  C  CB  . GLN C 176 ? 1.5026 1.5888 2.0099 -0.3782 0.0062  0.0900  177 GLN C CB  
7615  C  CG  . GLN C 176 ? 1.5954 1.6650 2.0781 -0.3745 -0.0008 0.0812  177 GLN C CG  
7616  C  CD  . GLN C 176 ? 1.6660 1.7378 2.1471 -0.3892 -0.0154 0.0762  177 GLN C CD  
7617  O  OE1 . GLN C 176 ? 1.7129 1.7616 2.1786 -0.4010 -0.0180 0.0693  177 GLN C OE1 
7618  N  NE2 . GLN C 176 ? 1.6669 1.7660 2.1641 -0.3892 -0.0255 0.0798  177 GLN C NE2 
7619  N  N   . LEU C 177 ? 1.2847 1.3730 1.8207 -0.3955 0.0256  0.1048  178 LEU C N   
7620  C  CA  . LEU C 177 ? 1.1748 1.2861 1.7341 -0.3988 0.0338  0.1130  178 LEU C CA  
7621  C  C   . LEU C 177 ? 1.1531 1.2603 1.7229 -0.4166 0.0346  0.1160  178 LEU C C   
7622  O  O   . LEU C 177 ? 1.1291 1.2592 1.7226 -0.4230 0.0395  0.1217  178 LEU C O   
7623  C  CB  . LEU C 177 ? 1.1094 1.2170 1.6599 -0.3867 0.0471  0.1183  178 LEU C CB  
7624  C  CG  . LEU C 177 ? 1.0303 1.1612 1.5997 -0.3879 0.0587  0.1258  178 LEU C CG  
7625  C  CD1 . LEU C 177 ? 0.9714 1.1088 1.5334 -0.3721 0.0670  0.1275  178 LEU C CD1 
7626  C  CD2 . LEU C 177 ? 1.0249 1.1418 1.5915 -0.3997 0.0664  0.1321  178 LEU C CD2 
7627  N  N   . HIS C 178 ? 1.1536 1.2324 1.7078 -0.4254 0.0303  0.1119  179 HIS C N   
7628  C  CA  . HIS C 178 ? 1.1566 1.2278 1.7185 -0.4409 0.0337  0.1162  179 HIS C CA  
7629  C  C   . HIS C 178 ? 1.3920 1.4462 1.9495 -0.4568 0.0231  0.1095  179 HIS C C   
7630  O  O   . HIS C 178 ? 1.3757 1.4127 1.9153 -0.4549 0.0160  0.1008  179 HIS C O   
7631  C  CB  . HIS C 178 ? 1.1805 1.2288 1.7277 -0.4362 0.0451  0.1218  179 HIS C CB  
7632  C  CG  . HIS C 178 ? 1.2256 1.2407 1.7475 -0.4282 0.0438  0.1163  179 HIS C CG  
7633  N  ND1 . HIS C 178 ? 1.2583 1.2453 1.7697 -0.4375 0.0388  0.1098  179 HIS C ND1 
7634  C  CD2 . HIS C 178 ? 1.2252 1.2298 1.7318 -0.4122 0.0481  0.1165  179 HIS C CD2 
7635  C  CE1 . HIS C 178 ? 1.2740 1.2355 1.7664 -0.4268 0.0406  0.1056  179 HIS C CE1 
7636  N  NE2 . HIS C 178 ? 1.2557 1.2278 1.7451 -0.4114 0.0457  0.1100  179 HIS C NE2 
7637  N  N   . PRO C 179 ? 1.5170 1.5758 2.0906 -0.4737 0.0231  0.1134  180 PRO C N   
7638  C  CA  . PRO C 179 ? 1.5392 1.5885 2.1145 -0.4922 0.0127  0.1081  180 PRO C CA  
7639  C  C   . PRO C 179 ? 1.5446 1.5520 2.0945 -0.4969 0.0122  0.1009  180 PRO C C   
7640  O  O   . PRO C 179 ? 1.5905 1.5868 2.1334 -0.5080 0.0028  0.0928  180 PRO C O   
7641  C  CB  . PRO C 179 ? 1.5838 1.6471 2.1750 -0.5013 0.0192  0.1134  180 PRO C CB  
7642  C  CG  . PRO C 179 ? 1.5762 1.6513 2.1730 -0.4911 0.0331  0.1222  180 PRO C CG  
7643  C  CD  . PRO C 179 ? 1.5540 1.6205 2.1399 -0.4765 0.0355  0.1236  180 PRO C CD  
7644  N  N   . GLN C 180 ? 1.4664 1.4518 2.0049 -0.4891 0.0227  0.1046  181 GLN C N   
7645  C  CA  . GLN C 180 ? 1.4558 1.4034 1.9801 -0.4963 0.0245  0.1009  181 GLN C CA  
7646  C  C   . GLN C 180 ? 1.4455 1.3652 1.9461 -0.4893 0.0217  0.0887  181 GLN C C   
7647  O  O   . GLN C 180 ? 1.4901 1.3772 1.9799 -0.4958 0.0227  0.0827  181 GLN C O   
7648  C  CB  . GLN C 180 ? 1.4125 1.3494 1.9370 -0.4912 0.0359  0.1118  181 GLN C CB  
7649  C  CG  . GLN C 180 ? 1.3478 1.3177 1.8915 -0.4935 0.0411  0.1224  181 GLN C CG  
7650  C  CD  . GLN C 180 ? 1.2843 1.2501 1.8233 -0.4838 0.0522  0.1332  181 GLN C CD  
7651  O  OE1 . GLN C 180 ? 1.3073 1.2455 1.8356 -0.4854 0.0565  0.1373  181 GLN C OE1 
7652  N  NE2 . GLN C 180 ? 1.2221 1.2140 1.7670 -0.4729 0.0565  0.1372  181 GLN C NE2 
7653  N  N   . LEU C 181 ? 1.4699 1.4028 1.9638 -0.4762 0.0189  0.0847  182 LEU C N   
7654  C  CA  . LEU C 181 ? 1.5002 1.4108 1.9731 -0.4627 0.0215  0.0769  182 LEU C CA  
7655  C  C   . LEU C 181 ? 1.5611 1.4378 2.0167 -0.4712 0.0192  0.0635  182 LEU C C   
7656  O  O   . LEU C 181 ? 1.6070 1.4846 2.0584 -0.4849 0.0103  0.0550  182 LEU C O   
7657  C  CB  . LEU C 181 ? 1.5085 1.4420 1.9779 -0.4507 0.0168  0.0743  182 LEU C CB  
7658  N  N   . LEU C 182 ? 1.5327 1.3795 1.9792 -0.4631 0.0275  0.0620  183 LEU C N   
7659  C  CA  . LEU C 182 ? 1.5461 1.3582 1.9762 -0.4664 0.0289  0.0479  183 LEU C CA  
7660  C  C   . LEU C 182 ? 1.5113 1.3097 1.9328 -0.4467 0.0366  0.0468  183 LEU C C   
7661  O  O   . LEU C 182 ? 1.5054 1.3149 1.9344 -0.4336 0.0410  0.0587  183 LEU C O   
7662  C  CB  . LEU C 182 ? 1.5773 1.3616 2.0119 -0.4801 0.0319  0.0474  183 LEU C CB  
7663  N  N   . LEU C 183 ? 1.5236 1.2987 1.9291 -0.4453 0.0384  0.0321  184 LEU C N   
7664  C  CA  . LEU C 183 ? 1.4638 1.2267 1.8626 -0.4269 0.0457  0.0298  184 LEU C CA  
7665  C  C   . LEU C 183 ? 1.5088 1.2315 1.9025 -0.4277 0.0535  0.0190  184 LEU C C   
7666  O  O   . LEU C 183 ? 1.5539 1.2579 1.9402 -0.4428 0.0526  0.0067  184 LEU C O   
7667  C  CB  . LEU C 183 ? 1.4370 1.2162 1.8219 -0.4199 0.0419  0.0222  184 LEU C CB  
7668  N  N   . PRO C 184 ? 1.4355 1.1446 1.8345 -0.4116 0.0611  0.0238  185 PRO C N   
7669  C  CA  . PRO C 184 ? 1.4356 1.1090 1.8337 -0.4059 0.0700  0.0142  185 PRO C CA  
7670  C  C   . PRO C 184 ? 1.4224 1.0788 1.8029 -0.4148 0.0719  -0.0077 185 PRO C C   
7671  O  O   . PRO C 184 ? 1.4249 1.0525 1.8048 -0.4260 0.0760  -0.0181 185 PRO C O   
7672  C  CB  . PRO C 184 ? 1.3995 1.0804 1.8003 -0.3847 0.0739  0.0209  185 PRO C CB  
7673  C  CG  . PRO C 184 ? 1.3872 1.0970 1.7972 -0.3810 0.0690  0.0404  185 PRO C CG  
7674  C  CD  . PRO C 184 ? 1.3985 1.1286 1.8076 -0.3978 0.0614  0.0412  185 PRO C CD  
7675  N  N   . ALA C 197 ? 1.0445 0.9010 1.4446 -0.2669 0.0698  0.1862  198 ALA C N   
7676  C  CA  . ALA C 197 ? 1.1320 0.9734 1.5358 -0.2792 0.0686  0.1983  198 ALA C CA  
7677  C  C   . ALA C 197 ? 1.1941 1.0533 1.5883 -0.2897 0.0709  0.2099  198 ALA C C   
7678  O  O   . ALA C 197 ? 1.2213 1.0796 1.6075 -0.2895 0.0691  0.2236  198 ALA C O   
7679  C  CB  . ALA C 197 ? 1.1281 0.9586 1.5408 -0.2881 0.0695  0.1889  198 ALA C CB  
7680  N  N   . LEU C 198 ? 1.2618 1.1374 1.6570 -0.2997 0.0752  0.2041  199 LEU C N   
7681  C  CA  . LEU C 198 ? 1.2800 1.1730 1.6683 -0.3114 0.0797  0.2129  199 LEU C CA  
7682  C  C   . LEU C 198 ? 1.2817 1.2033 1.6632 -0.3057 0.0845  0.2074  199 LEU C C   
7683  O  O   . LEU C 198 ? 1.2814 1.2192 1.6562 -0.3139 0.0901  0.2132  199 LEU C O   
7684  C  CB  . LEU C 198 ? 1.3235 1.2190 1.7203 -0.3260 0.0824  0.2101  199 LEU C CB  
7685  C  CG  . LEU C 198 ? 1.3499 1.2619 1.7431 -0.3409 0.0887  0.2181  199 LEU C CG  
7686  C  CD1 . LEU C 198 ? 1.3807 1.2801 1.7619 -0.3475 0.0879  0.2364  199 LEU C CD1 
7687  C  CD2 . LEU C 198 ? 1.3646 1.2767 1.7697 -0.3543 0.0901  0.2141  199 LEU C CD2 
7688  N  N   . ARG C 199 ? 1.2086 1.1354 1.5916 -0.2920 0.0828  0.1961  200 ARG C N   
7689  C  CA  . ARG C 199 ? 1.1444 1.0973 1.5240 -0.2856 0.0867  0.1890  200 ARG C CA  
7690  C  C   . ARG C 199 ? 1.0780 1.0535 1.4655 -0.2954 0.0924  0.1837  200 ARG C C   
7691  O  O   . ARG C 199 ? 1.1053 1.0974 1.4888 -0.3014 0.0989  0.1884  200 ARG C O   
7692  C  CB  . ARG C 199 ? 1.1591 1.1177 1.5250 -0.2827 0.0886  0.1988  200 ARG C CB  
7693  N  N   . PRO C 200 ? 0.9441 0.9202 1.3433 -0.2978 0.0899  0.1738  201 PRO C N   
7694  C  CA  . PRO C 200 ? 0.8904 0.8871 1.3015 -0.3078 0.0935  0.1692  201 PRO C CA  
7695  C  C   . PRO C 200 ? 0.8399 0.8652 1.2557 -0.3017 0.0973  0.1626  201 PRO C C   
7696  O  O   . PRO C 200 ? 0.7934 0.8392 1.2196 -0.3098 0.1031  0.1623  201 PRO C O   
7697  C  CB  . PRO C 200 ? 0.9026 0.8883 1.3223 -0.3103 0.0873  0.1603  201 PRO C CB  
7698  C  CG  . PRO C 200 ? 0.9212 0.8914 1.3337 -0.2969 0.0824  0.1547  201 PRO C CG  
7699  C  CD  . PRO C 200 ? 0.9281 0.8859 1.3298 -0.2912 0.0836  0.1655  201 PRO C CD  
7700  N  N   . PHE C 201 ? 0.8149 0.8416 1.2251 -0.2877 0.0946  0.1574  202 PHE C N   
7701  C  CA  . PHE C 201 ? 0.8355 0.8874 1.2510 -0.2808 0.0974  0.1511  202 PHE C CA  
7702  C  C   . PHE C 201 ? 0.9108 0.9715 1.3164 -0.2783 0.1049  0.1572  202 PHE C C   
7703  O  O   . PHE C 201 ? 0.9378 1.0176 1.3467 -0.2718 0.1086  0.1524  202 PHE C O   
7704  C  CB  . PHE C 201 ? 0.7869 0.8363 1.2007 -0.2679 0.0907  0.1422  202 PHE C CB  
7705  C  CG  . PHE C 201 ? 0.7859 0.8255 1.2055 -0.2711 0.0834  0.1350  202 PHE C CG  
7706  C  CD1 . PHE C 201 ? 0.7842 0.8411 1.2177 -0.2756 0.0806  0.1284  202 PHE C CD1 
7707  C  CD2 . PHE C 201 ? 0.7895 0.8022 1.2012 -0.2702 0.0794  0.1345  202 PHE C CD2 
7708  C  CE1 . PHE C 201 ? 0.7868 0.8342 1.2227 -0.2803 0.0732  0.1218  202 PHE C CE1 
7709  C  CE2 . PHE C 201 ? 0.8076 0.8100 1.2223 -0.2744 0.0739  0.1265  202 PHE C CE2 
7710  C  CZ  . PHE C 201 ? 0.8112 0.8308 1.2362 -0.2801 0.0705  0.1201  202 PHE C CZ  
7711  N  N   . GLY C 202 ? 0.9974 1.0434 1.3905 -0.2840 0.1068  0.1679  203 GLY C N   
7712  C  CA  . GLY C 202 ? 1.0135 1.0651 1.3930 -0.2842 0.1132  0.1746  203 GLY C CA  
7713  C  C   . GLY C 202 ? 1.0076 1.0521 1.3749 -0.2705 0.1090  0.1747  203 GLY C C   
7714  O  O   . GLY C 202 ? 1.0964 1.1228 1.4620 -0.2632 0.1010  0.1746  203 GLY C O   
7715  N  N   . GLU C 203 ? 0.9721 1.0309 1.3318 -0.2674 0.1150  0.1742  204 GLU C N   
7716  C  CA  . GLU C 203 ? 0.8760 0.9296 1.2232 -0.2557 0.1115  0.1751  204 GLU C CA  
7717  C  C   . GLU C 203 ? 0.7850 0.8450 1.1409 -0.2418 0.1073  0.1638  204 GLU C C   
7718  O  O   . GLU C 203 ? 0.7577 0.8084 1.1064 -0.2313 0.1020  0.1637  204 GLU C O   
7719  C  CB  . GLU C 203 ? 0.9124 0.9782 1.2464 -0.2591 0.1200  0.1782  204 GLU C CB  
7720  C  CG  . GLU C 203 ? 0.9958 1.0529 1.3148 -0.2735 0.1232  0.1910  204 GLU C CG  
7721  C  CD  . GLU C 203 ? 1.0635 1.1394 1.3784 -0.2841 0.1368  0.1894  204 GLU C CD  
7722  O  OE1 . GLU C 203 ? 1.0677 1.1619 1.4004 -0.2848 0.1438  0.1797  204 GLU C OE1 
7723  O  OE2 . GLU C 203 ? 1.0844 1.1567 1.3787 -0.2923 0.1405  0.1978  204 GLU C OE2 
7724  N  N   . ALA C 204 ? 0.7377 0.8139 1.1096 -0.2425 0.1094  0.1549  205 ALA C N   
7725  C  CA  . ALA C 204 ? 0.6867 0.7727 1.0670 -0.2312 0.1058  0.1447  205 ALA C CA  
7726  C  C   . ALA C 204 ? 0.6614 0.7306 1.0373 -0.2214 0.0966  0.1417  205 ALA C C   
7727  O  O   . ALA C 204 ? 0.6405 0.7133 1.0129 -0.2106 0.0947  0.1374  205 ALA C O   
7728  C  CB  . ALA C 204 ? 0.6862 0.7890 1.0866 -0.2361 0.1066  0.1381  205 ALA C CB  
7729  N  N   . PRO C 205 ? 0.6828 0.7334 1.0594 -0.2255 0.0917  0.1432  206 PRO C N   
7730  C  CA  . PRO C 205 ? 0.6932 0.7288 1.0672 -0.2168 0.0850  0.1380  206 PRO C CA  
7731  C  C   . PRO C 205 ? 0.7225 0.7485 1.0855 -0.2063 0.0836  0.1415  206 PRO C C   
7732  O  O   . PRO C 205 ? 0.6928 0.7233 1.0539 -0.1963 0.0818  0.1353  206 PRO C O   
7733  C  CB  . PRO C 205 ? 0.6502 0.6658 1.0270 -0.2247 0.0823  0.1400  206 PRO C CB  
7734  C  CG  . PRO C 205 ? 0.6542 0.6802 1.0389 -0.2374 0.0858  0.1426  206 PRO C CG  
7735  C  CD  . PRO C 205 ? 0.6319 0.6745 1.0130 -0.2384 0.0925  0.1481  206 PRO C CD  
7736  N  N   . ARG C 206 ? 0.7442 0.7570 1.1004 -0.2093 0.0839  0.1520  207 ARG C N   
7737  C  CA  A ARG C 206 ? 0.8032 0.8059 1.1510 -0.2007 0.0812  0.1574  207 ARG C CA  
7738  C  CA  B ARG C 206 ? 0.8118 0.8147 1.1597 -0.2004 0.0811  0.1570  207 ARG C CA  
7739  C  C   . ARG C 206 ? 0.8348 0.8542 1.1745 -0.1956 0.0842  0.1576  207 ARG C C   
7740  O  O   . ARG C 206 ? 0.8451 0.8614 1.1795 -0.1861 0.0816  0.1579  207 ARG C O   
7741  C  CB  A ARG C 206 ? 0.8059 0.7912 1.1501 -0.2071 0.0792  0.1706  207 ARG C CB  
7742  C  CB  B ARG C 206 ? 0.8059 0.7904 1.1506 -0.2059 0.0788  0.1700  207 ARG C CB  
7743  C  CG  A ARG C 206 ? 0.7871 0.7624 1.1245 -0.1998 0.0751  0.1790  207 ARG C CG  
7744  C  CG  B ARG C 206 ? 0.7506 0.7123 1.1037 -0.2041 0.0745  0.1689  207 ARG C CG  
7745  C  CD  A ARG C 206 ? 0.8165 0.7710 1.1555 -0.2057 0.0708  0.1920  207 ARG C CD  
7746  C  CD  B ARG C 206 ? 0.7013 0.6574 1.0564 -0.1907 0.0720  0.1615  207 ARG C CD  
7747  N  NE  A ARG C 206 ? 0.8336 0.7839 1.1635 -0.2043 0.0667  0.2048  207 ARG C NE  
7748  N  NE  B ARG C 206 ? 0.6860 0.6423 1.0347 -0.1837 0.0698  0.1694  207 ARG C NE  
7749  C  CZ  A ARG C 206 ? 0.8626 0.7951 1.1939 -0.2084 0.0608  0.2188  207 ARG C CZ  
7750  C  CZ  B ARG C 206 ? 0.6496 0.6043 0.9993 -0.1720 0.0681  0.1649  207 ARG C CZ  
7751  N  NH1 A ARG C 206 ? 0.8746 0.7911 1.2167 -0.2135 0.0595  0.2210  207 ARG C NH1 
7752  N  NH1 B ARG C 206 ? 0.6506 0.6027 1.0056 -0.1665 0.0690  0.1522  207 ARG C NH1 
7753  N  NH2 A ARG C 206 ? 0.8664 0.7968 1.1889 -0.2078 0.0557  0.2311  207 ARG C NH2 
7754  N  NH2 B ARG C 206 ? 0.6494 0.6049 0.9938 -0.1670 0.0654  0.1731  207 ARG C NH2 
7755  N  N   . GLU C 207 ? 0.8730 0.9101 1.2127 -0.2023 0.0904  0.1570  208 GLU C N   
7756  C  CA  . GLU C 207 ? 0.8832 0.9363 1.2163 -0.1985 0.0949  0.1554  208 GLU C CA  
7757  C  C   . GLU C 207 ? 0.8871 0.9494 1.2265 -0.1873 0.0930  0.1446  208 GLU C C   
7758  O  O   . GLU C 207 ? 0.8931 0.9572 1.2258 -0.1785 0.0919  0.1435  208 GLU C O   
7759  C  CB  . GLU C 207 ? 0.9548 1.0242 1.2896 -0.2090 0.1038  0.1558  208 GLU C CB  
7760  C  CG  . GLU C 207 ? 1.0255 1.1050 1.3479 -0.2099 0.1103  0.1580  208 GLU C CG  
7761  C  CD  . GLU C 207 ? 1.1204 1.2099 1.4412 -0.2235 0.1203  0.1607  208 GLU C CD  
7762  O  OE1 . GLU C 207 ? 1.1467 1.2475 1.4833 -0.2281 0.1245  0.1554  208 GLU C OE1 
7763  O  OE2 . GLU C 207 ? 1.1591 1.2453 1.4626 -0.2306 0.1238  0.1684  208 GLU C OE2 
7764  N  N   . LEU C 208 ? 0.8202 0.8877 1.1722 -0.1885 0.0916  0.1372  209 LEU C N   
7765  C  CA  . LEU C 208 ? 0.7871 0.8603 1.1446 -0.1798 0.0878  0.1279  209 LEU C CA  
7766  C  C   . LEU C 208 ? 0.7691 0.8259 1.1191 -0.1709 0.0825  0.1272  209 LEU C C   
7767  O  O   . LEU C 208 ? 0.7399 0.8011 1.0877 -0.1619 0.0809  0.1225  209 LEU C O   
7768  C  CB  . LEU C 208 ? 0.7295 0.8069 1.0997 -0.1853 0.0851  0.1221  209 LEU C CB  
7769  C  CG  . LEU C 208 ? 0.7075 0.7848 1.0800 -0.1789 0.0788  0.1136  209 LEU C CG  
7770  C  CD1 . LEU C 208 ? 0.6448 0.7410 1.0220 -0.1721 0.0794  0.1097  209 LEU C CD1 
7771  C  CD2 . LEU C 208 ? 0.6787 0.7540 1.0596 -0.1871 0.0746  0.1095  209 LEU C CD2 
7772  N  N   . ARG C 209 ? 0.7768 0.8144 1.1246 -0.1737 0.0803  0.1320  210 ARG C N   
7773  C  CA  . ARG C 209 ? 0.7458 0.7668 1.0905 -0.1656 0.0765  0.1313  210 ARG C CA  
7774  C  C   . ARG C 209 ? 0.7369 0.7597 1.0735 -0.1577 0.0764  0.1361  210 ARG C C   
7775  O  O   . ARG C 209 ? 0.7255 0.7474 1.0608 -0.1485 0.0746  0.1312  210 ARG C O   
7776  C  CB  . ARG C 209 ? 0.7087 0.7088 1.0562 -0.1705 0.0749  0.1366  210 ARG C CB  
7777  N  N   . LEU C 210 ? 0.7052 0.7306 1.0356 -0.1626 0.0784  0.1456  211 LEU C N   
7778  C  CA  . LEU C 210 ? 0.7100 0.7375 1.0310 -0.1574 0.0777  0.1511  211 LEU C CA  
7779  C  C   . LEU C 210 ? 0.6611 0.7056 0.9799 -0.1509 0.0802  0.1433  211 LEU C C   
7780  O  O   . LEU C 210 ? 0.7154 0.7586 1.0318 -0.1417 0.0777  0.1411  211 LEU C O   
7781  C  CB  . LEU C 210 ? 0.7423 0.7699 1.0539 -0.1669 0.0796  0.1625  211 LEU C CB  
7782  C  CG  . LEU C 210 ? 0.8173 0.8269 1.1300 -0.1737 0.0758  0.1733  211 LEU C CG  
7783  C  CD1 . LEU C 210 ? 0.8226 0.8346 1.1232 -0.1852 0.0781  0.1845  211 LEU C CD1 
7784  C  CD2 . LEU C 210 ? 0.7968 0.7903 1.1130 -0.1653 0.0690  0.1780  211 LEU C CD2 
7785  N  N   . ARG C 211 ? 0.6156 0.6758 0.9373 -0.1559 0.0854  0.1393  212 ARG C N   
7786  C  CA  . ARG C 211 ? 0.6001 0.6767 0.9227 -0.1503 0.0882  0.1323  212 ARG C CA  
7787  C  C   . ARG C 211 ? 0.5487 0.6249 0.8765 -0.1409 0.0836  0.1242  212 ARG C C   
7788  O  O   . ARG C 211 ? 0.6158 0.6969 0.9401 -0.1332 0.0831  0.1214  212 ARG C O   
7789  C  CB  . ARG C 211 ? 0.5865 0.6798 0.9175 -0.1571 0.0947  0.1288  212 ARG C CB  
7790  C  CG  . ARG C 211 ? 0.6275 0.7248 0.9505 -0.1664 0.1018  0.1350  212 ARG C CG  
7791  C  CD  . ARG C 211 ? 0.6698 0.7855 1.0043 -0.1719 0.1101  0.1297  212 ARG C CD  
7792  N  NE  . ARG C 211 ? 0.6925 0.8120 1.0175 -0.1819 0.1189  0.1344  212 ARG C NE  
7793  C  CZ  . ARG C 211 ? 0.7281 0.8540 1.0427 -0.1816 0.1251  0.1333  212 ARG C CZ  
7794  N  NH1 . ARG C 211 ? 0.7108 0.8402 1.0250 -0.1709 0.1230  0.1281  212 ARG C NH1 
7795  N  NH2 . ARG C 211 ? 0.7379 0.8660 1.0413 -0.1928 0.1337  0.1372  212 ARG C NH2 
7796  N  N   . ALA C 212 ? 0.4936 0.5633 0.8284 -0.1428 0.0805  0.1204  213 ALA C N   
7797  C  CA  . ALA C 212 ? 0.6420 0.7096 0.9789 -0.1363 0.0763  0.1127  213 ALA C CA  
7798  C  C   . ALA C 212 ? 0.5843 0.6387 0.9145 -0.1284 0.0740  0.1136  213 ALA C C   
7799  O  O   . ALA C 212 ? 0.6342 0.6923 0.9618 -0.1209 0.0727  0.1093  213 ALA C O   
7800  C  CB  . ALA C 212 ? 0.4930 0.5549 0.8362 -0.1423 0.0737  0.1083  213 ALA C CB  
7801  N  N   . THR C 213 ? 0.6127 0.6518 0.9418 -0.1303 0.0734  0.1198  214 THR C N   
7802  C  CA  . THR C 213 ? 0.5938 0.6201 0.9211 -0.1231 0.0713  0.1217  214 THR C CA  
7803  C  C   . THR C 213 ? 0.6198 0.6544 0.9407 -0.1165 0.0711  0.1244  214 THR C C   
7804  O  O   . THR C 213 ? 0.6182 0.6503 0.9387 -0.1086 0.0698  0.1210  214 THR C O   
7805  C  CB  . THR C 213 ? 0.5734 0.5836 0.9036 -0.1266 0.0701  0.1308  214 THR C CB  
7806  O  OG1 . THR C 213 ? 0.5952 0.5965 0.9314 -0.1334 0.0706  0.1279  214 THR C OG1 
7807  C  CG2 . THR C 213 ? 0.6051 0.6025 0.9387 -0.1184 0.0678  0.1325  214 THR C CG2 
7808  N  N   . ARG C 214 ? 0.6222 0.6667 0.9378 -0.1206 0.0732  0.1300  215 ARG C N   
7809  C  CA  . ARG C 214 ? 0.6129 0.6653 0.9208 -0.1159 0.0735  0.1320  215 ARG C CA  
7810  C  C   . ARG C 214 ? 0.5416 0.6070 0.8504 -0.1103 0.0749  0.1228  215 ARG C C   
7811  O  O   . ARG C 214 ? 0.5495 0.6140 0.8568 -0.1025 0.0728  0.1199  215 ARG C O   
7812  C  CB  . ARG C 214 ? 0.4901 0.5485 0.7898 -0.1239 0.0766  0.1392  215 ARG C CB  
7813  C  CG  . ARG C 214 ? 0.5295 0.5973 0.8197 -0.1211 0.0782  0.1394  215 ARG C CG  
7814  C  CD  . ARG C 214 ? 0.5302 0.6028 0.8096 -0.1311 0.0826  0.1454  215 ARG C CD  
7815  N  NE  . ARG C 214 ? 0.5599 0.6389 0.8445 -0.1392 0.0884  0.1431  215 ARG C NE  
7816  C  CZ  . ARG C 214 ? 0.5280 0.6212 0.8203 -0.1388 0.0941  0.1343  215 ARG C CZ  
7817  N  NH1 . ARG C 214 ? 0.4755 0.5770 0.7705 -0.1305 0.0945  0.1272  215 ARG C NH1 
7818  N  NH2 . ARG C 214 ? 0.4951 0.5943 0.7944 -0.1466 0.0991  0.1331  215 ARG C NH2 
7819  N  N   . ALA C 215 ? 0.5003 0.5779 0.8135 -0.1146 0.0782  0.1186  216 ALA C N   
7820  C  CA  . ALA C 215 ? 0.4858 0.5771 0.8022 -0.1102 0.0793  0.1117  216 ALA C CA  
7821  C  C   . ALA C 215 ? 0.5259 0.6145 0.8452 -0.1041 0.0748  0.1053  216 ALA C C   
7822  O  O   . ALA C 215 ? 0.5566 0.6511 0.8745 -0.0978 0.0739  0.1020  216 ALA C O   
7823  C  CB  . ALA C 215 ? 0.5003 0.6048 0.8258 -0.1163 0.0833  0.1093  216 ALA C CB  
7824  N  N   . PHE C 216 ? 0.5348 0.6138 0.8571 -0.1068 0.0723  0.1033  217 PHE C N   
7825  C  CA  . PHE C 216 ? 0.5493 0.6252 0.8716 -0.1034 0.0687  0.0965  217 PHE C CA  
7826  C  C   . PHE C 216 ? 0.5202 0.5868 0.8364 -0.0960 0.0680  0.0959  217 PHE C C   
7827  O  O   . PHE C 216 ? 0.5336 0.6033 0.8472 -0.0913 0.0664  0.0913  217 PHE C O   
7828  C  CB  . PHE C 216 ? 0.5279 0.5952 0.8533 -0.1100 0.0671  0.0934  217 PHE C CB  
7829  C  CG  . PHE C 216 ? 0.5016 0.5808 0.8348 -0.1165 0.0656  0.0914  217 PHE C CG  
7830  C  CD1 . PHE C 216 ? 0.4675 0.5534 0.8022 -0.1165 0.0610  0.0862  217 PHE C CD1 
7831  C  CD2 . PHE C 216 ? 0.5477 0.6317 0.8873 -0.1232 0.0683  0.0955  217 PHE C CD2 
7832  C  CE1 . PHE C 216 ? 0.4490 0.5467 0.7940 -0.1225 0.0583  0.0855  217 PHE C CE1 
7833  C  CE2 . PHE C 216 ? 0.4577 0.5539 0.8078 -0.1291 0.0670  0.0939  217 PHE C CE2 
7834  C  CZ  . PHE C 216 ? 0.4687 0.5721 0.8226 -0.1285 0.0615  0.0891  217 PHE C CZ  
7835  N  N   . VAL C 217 ? 0.5227 0.5782 0.8379 -0.0951 0.0689  0.1013  218 VAL C N   
7836  C  CA  . VAL C 217 ? 0.5153 0.5632 0.8284 -0.0879 0.0684  0.1015  218 VAL C CA  
7837  C  C   . VAL C 217 ? 0.5067 0.5652 0.8152 -0.0829 0.0682  0.1039  218 VAL C C   
7838  O  O   . VAL C 217 ? 0.4736 0.5315 0.7801 -0.0767 0.0674  0.1014  218 VAL C O   
7839  C  CB  . VAL C 217 ? 0.6812 0.7146 0.9985 -0.0881 0.0683  0.1079  218 VAL C CB  
7840  C  CG1 . VAL C 217 ? 0.6724 0.7091 0.9871 -0.0901 0.0673  0.1184  218 VAL C CG1 
7841  C  CG2 . VAL C 217 ? 0.6907 0.7152 1.0112 -0.0808 0.0684  0.1055  218 VAL C CG2 
7842  N  N   . ALA C 218 ? 0.4898 0.5576 0.7962 -0.0864 0.0696  0.1081  219 ALA C N   
7843  C  CA  . ALA C 218 ? 0.5139 0.5914 0.8151 -0.0830 0.0703  0.1091  219 ALA C CA  
7844  C  C   . ALA C 218 ? 0.5088 0.5952 0.8115 -0.0788 0.0699  0.1017  219 ALA C C   
7845  O  O   . ALA C 218 ? 0.4098 0.4974 0.7092 -0.0729 0.0688  0.1003  219 ALA C O   
7846  C  CB  . ALA C 218 ? 0.4322 0.5173 0.7303 -0.0891 0.0738  0.1132  219 ALA C CB  
7847  N  N   . ALA C 219 ? 0.4154 0.5080 0.7240 -0.0823 0.0700  0.0977  220 ALA C N   
7848  C  CA  . ALA C 219 ? 0.4393 0.5406 0.7513 -0.0796 0.0680  0.0922  220 ALA C CA  
7849  C  C   . ALA C 219 ? 0.4361 0.5296 0.7436 -0.0757 0.0646  0.0884  220 ALA C C   
7850  O  O   . ALA C 219 ? 0.3986 0.4959 0.7037 -0.0707 0.0633  0.0865  220 ALA C O   
7851  C  CB  . ALA C 219 ? 0.4079 0.5163 0.7291 -0.0853 0.0671  0.0901  220 ALA C CB  
7852  N  N   . ARG C 220 ? 0.4983 0.5803 0.8048 -0.0784 0.0641  0.0870  221 ARG C N   
7853  C  CA  . ARG C 220 ? 0.4840 0.5572 0.7856 -0.0763 0.0630  0.0821  221 ARG C CA  
7854  C  C   . ARG C 220 ? 0.4372 0.5076 0.7356 -0.0691 0.0643  0.0835  221 ARG C C   
7855  O  O   . ARG C 220 ? 0.4428 0.5148 0.7370 -0.0658 0.0633  0.0801  221 ARG C O   
7856  C  CB  . ARG C 220 ? 0.5703 0.6299 0.8724 -0.0807 0.0643  0.0798  221 ARG C CB  
7857  C  CG  . ARG C 220 ? 0.6274 0.6771 0.9239 -0.0802 0.0651  0.0728  221 ARG C CG  
7858  C  CD  . ARG C 220 ? 0.6370 0.6719 0.9353 -0.0848 0.0680  0.0696  221 ARG C CD  
7859  N  NE  . ARG C 220 ? 0.6634 0.6899 0.9690 -0.0809 0.0709  0.0748  221 ARG C NE  
7860  C  CZ  . ARG C 220 ? 0.7406 0.7537 1.0518 -0.0838 0.0735  0.0742  221 ARG C CZ  
7861  N  NH1 . ARG C 220 ? 0.7534 0.7596 1.0620 -0.0910 0.0742  0.0676  221 ARG C NH1 
7862  N  NH2 . ARG C 220 ? 0.7473 0.7534 1.0671 -0.0799 0.0747  0.0807  221 ARG C NH2 
7863  N  N   . SER C 221 ? 0.4801 0.5465 0.7805 -0.0676 0.0659  0.0894  222 SER C N   
7864  C  CA  . SER C 221 ? 0.5067 0.5709 0.8059 -0.0615 0.0661  0.0921  222 SER C CA  
7865  C  C   . SER C 221 ? 0.4747 0.5502 0.7698 -0.0580 0.0651  0.0920  222 SER C C   
7866  O  O   . SER C 221 ? 0.4837 0.5588 0.7768 -0.0532 0.0648  0.0908  222 SER C O   
7867  C  CB  . SER C 221 ? 0.5235 0.5827 0.8258 -0.0620 0.0660  0.1004  222 SER C CB  
7868  O  OG  . SER C 221 ? 0.5475 0.5950 0.8558 -0.0647 0.0668  0.1009  222 SER C OG  
7869  N  N   . PHE C 222 ? 0.4503 0.5356 0.7454 -0.0607 0.0653  0.0929  223 PHE C N   
7870  C  CA  . PHE C 222 ? 0.4826 0.5779 0.7757 -0.0577 0.0653  0.0920  223 PHE C CA  
7871  C  C   . PHE C 222 ? 0.4646 0.5622 0.7575 -0.0552 0.0629  0.0867  223 PHE C C   
7872  O  O   . PHE C 222 ? 0.4936 0.5926 0.7833 -0.0508 0.0621  0.0859  223 PHE C O   
7873  C  CB  . PHE C 222 ? 0.4891 0.5940 0.7853 -0.0616 0.0676  0.0928  223 PHE C CB  
7874  C  CG  . PHE C 222 ? 0.4963 0.6102 0.7919 -0.0587 0.0691  0.0914  223 PHE C CG  
7875  C  CD1 . PHE C 222 ? 0.3817 0.4952 0.6703 -0.0578 0.0708  0.0944  223 PHE C CD1 
7876  C  CD2 . PHE C 222 ? 0.4897 0.6119 0.7925 -0.0573 0.0682  0.0873  223 PHE C CD2 
7877  C  CE1 . PHE C 222 ? 0.3772 0.4976 0.6646 -0.0558 0.0729  0.0920  223 PHE C CE1 
7878  C  CE2 . PHE C 222 ? 0.4435 0.5728 0.7479 -0.0543 0.0701  0.0856  223 PHE C CE2 
7879  C  CZ  . PHE C 222 ? 0.4551 0.5831 0.7513 -0.0536 0.0731  0.0873  223 PHE C CZ  
7880  N  N   . VAL C 223 ? 0.4852 0.5830 0.7807 -0.0590 0.0611  0.0836  224 VAL C N   
7881  C  CA  . VAL C 223 ? 0.5092 0.6087 0.8028 -0.0588 0.0574  0.0796  224 VAL C CA  
7882  C  C   . VAL C 223 ? 0.4755 0.5662 0.7616 -0.0562 0.0579  0.0771  224 VAL C C   
7883  O  O   . VAL C 223 ? 0.4730 0.5660 0.7553 -0.0534 0.0562  0.0759  224 VAL C O   
7884  C  CB  . VAL C 223 ? 0.4831 0.5831 0.7795 -0.0653 0.0542  0.0775  224 VAL C CB  
7885  C  CG1 . VAL C 223 ? 0.4752 0.5748 0.7662 -0.0668 0.0493  0.0743  224 VAL C CG1 
7886  C  CG2 . VAL C 223 ? 0.4687 0.5800 0.7761 -0.0675 0.0539  0.0796  224 VAL C CG2 
7887  N  N   . GLN C 224 ? 0.5667 0.6469 0.8519 -0.0572 0.0608  0.0763  225 GLN C N   
7888  C  CA  . GLN C 224 ? 0.6057 0.6774 0.8868 -0.0547 0.0632  0.0731  225 GLN C CA  
7889  C  C   . GLN C 224 ? 0.5617 0.6364 0.8437 -0.0483 0.0640  0.0764  225 GLN C C   
7890  O  O   . GLN C 224 ? 0.5585 0.6312 0.8372 -0.0458 0.0650  0.0737  225 GLN C O   
7891  C  CB  . GLN C 224 ? 0.7422 0.8018 1.0266 -0.0565 0.0670  0.0713  225 GLN C CB  
7892  C  CG  . GLN C 224 ? 0.8659 0.9164 1.1441 -0.0599 0.0697  0.0633  225 GLN C CG  
7893  C  CD  . GLN C 224 ? 0.9636 1.0010 1.2479 -0.0591 0.0757  0.0606  225 GLN C CD  
7894  O  OE1 . GLN C 224 ? 1.0045 1.0363 1.2951 -0.0612 0.0764  0.0623  225 GLN C OE1 
7895  N  NE2 . GLN C 224 ? 0.9853 1.0177 1.2693 -0.0563 0.0804  0.0562  225 GLN C NE2 
7896  N  N   . GLY C 225 ? 0.4907 0.5701 0.7763 -0.0467 0.0635  0.0820  226 GLY C N   
7897  C  CA  . GLY C 225 ? 0.3798 0.4627 0.6648 -0.0421 0.0633  0.0855  226 GLY C CA  
7898  C  C   . GLY C 225 ? 0.4684 0.5585 0.7494 -0.0401 0.0616  0.0833  226 GLY C C   
7899  O  O   . GLY C 225 ? 0.4704 0.5600 0.7494 -0.0367 0.0616  0.0827  226 GLY C O   
7900  N  N   . LEU C 226 ? 0.4821 0.5791 0.7639 -0.0424 0.0599  0.0823  227 LEU C N   
7901  C  CA  . LEU C 226 ? 0.4295 0.5328 0.7103 -0.0408 0.0574  0.0806  227 LEU C CA  
7902  C  C   . LEU C 226 ? 0.4835 0.5821 0.7586 -0.0410 0.0559  0.0774  227 LEU C C   
7903  O  O   . LEU C 226 ? 0.4755 0.5754 0.7475 -0.0383 0.0550  0.0772  227 LEU C O   
7904  C  CB  . LEU C 226 ? 0.4497 0.5605 0.7367 -0.0435 0.0555  0.0802  227 LEU C CB  
7905  C  CG  . LEU C 226 ? 0.3605 0.4781 0.6532 -0.0437 0.0585  0.0821  227 LEU C CG  
7906  C  CD1 . LEU C 226 ? 0.3882 0.5128 0.6907 -0.0470 0.0576  0.0813  227 LEU C CD1 
7907  C  CD2 . LEU C 226 ? 0.3921 0.5139 0.6842 -0.0398 0.0596  0.0821  227 LEU C CD2 
7908  N  N   . GLY C 227 ? 0.5421 0.6345 0.8147 -0.0452 0.0561  0.0745  228 GLY C N   
7909  C  CA  . GLY C 227 ? 0.5387 0.6252 0.8032 -0.0475 0.0561  0.0704  228 GLY C CA  
7910  C  C   . GLY C 227 ? 0.5007 0.5826 0.7633 -0.0436 0.0603  0.0694  228 GLY C C   
7911  O  O   . GLY C 227 ? 0.4854 0.5673 0.7418 -0.0435 0.0598  0.0678  228 GLY C O   
7912  N  N   . VAL C 228 ? 0.4753 0.5535 0.7443 -0.0408 0.0640  0.0709  229 VAL C N   
7913  C  CA  . VAL C 228 ? 0.4692 0.5440 0.7412 -0.0367 0.0677  0.0709  229 VAL C CA  
7914  C  C   . VAL C 228 ? 0.4946 0.5765 0.7659 -0.0328 0.0654  0.0741  229 VAL C C   
7915  O  O   . VAL C 228 ? 0.4491 0.5301 0.7180 -0.0315 0.0670  0.0722  229 VAL C O   
7916  C  CB  . VAL C 228 ? 0.4609 0.5312 0.7432 -0.0345 0.0699  0.0742  229 VAL C CB  
7917  C  CG1 . VAL C 228 ? 0.4370 0.5066 0.7263 -0.0296 0.0719  0.0762  229 VAL C CG1 
7918  C  CG2 . VAL C 228 ? 0.3944 0.4552 0.6788 -0.0380 0.0736  0.0699  229 VAL C CG2 
7919  N  N   . ALA C 229 ? 0.5040 0.5924 0.7769 -0.0316 0.0623  0.0784  230 ALA C N   
7920  C  CA  . ALA C 229 ? 0.4163 0.5106 0.6878 -0.0287 0.0604  0.0806  230 ALA C CA  
7921  C  C   . ALA C 229 ? 0.4986 0.5945 0.7643 -0.0294 0.0585  0.0778  230 ALA C C   
7922  O  O   . ALA C 229 ? 0.5584 0.6547 0.8221 -0.0275 0.0588  0.0778  230 ALA C O   
7923  C  CB  . ALA C 229 ? 0.3707 0.4709 0.6434 -0.0289 0.0588  0.0837  230 ALA C CB  
7924  N  N   . SER C 230 ? 0.5307 0.6276 0.7943 -0.0329 0.0561  0.0761  231 SER C N   
7925  C  CA  . SER C 230 ? 0.5599 0.6577 0.8179 -0.0349 0.0525  0.0750  231 SER C CA  
7926  C  C   . SER C 230 ? 0.5304 0.6223 0.7805 -0.0367 0.0551  0.0720  231 SER C C   
7927  O  O   . SER C 230 ? 0.5355 0.6283 0.7818 -0.0359 0.0542  0.0725  231 SER C O   
7928  C  CB  . SER C 230 ? 0.5843 0.6837 0.8425 -0.0395 0.0483  0.0746  231 SER C CB  
7929  O  OG  . SER C 230 ? 0.6259 0.7264 0.8793 -0.0422 0.0430  0.0754  231 SER C OG  
7930  N  N   . ASP C 231 ? 0.5990 0.6842 0.8470 -0.0395 0.0593  0.0682  232 ASP C N   
7931  C  CA  . ASP C 231 ? 0.6563 0.7350 0.8974 -0.0421 0.0643  0.0636  232 ASP C CA  
7932  C  C   . ASP C 231 ? 0.5919 0.6719 0.8383 -0.0370 0.0680  0.0646  232 ASP C C   
7933  O  O   . ASP C 231 ? 0.5717 0.6508 0.8119 -0.0385 0.0696  0.0630  232 ASP C O   
7934  C  CB  . ASP C 231 ? 0.7988 0.8693 1.0403 -0.0452 0.0700  0.0585  232 ASP C CB  
7935  C  CG  . ASP C 231 ? 0.9412 1.0085 1.1726 -0.0532 0.0670  0.0556  232 ASP C CG  
7936  O  OD1 . ASP C 231 ? 0.9851 1.0550 1.2071 -0.0573 0.0613  0.0569  232 ASP C OD1 
7937  O  OD2 . ASP C 231 ? 1.0192 1.0811 1.2526 -0.0557 0.0696  0.0526  232 ASP C OD2 
7938  N  N   . VAL C 232 ? 0.5338 0.6159 0.7913 -0.0319 0.0687  0.0680  233 VAL C N   
7939  C  CA  . VAL C 232 ? 0.4823 0.5665 0.7468 -0.0274 0.0707  0.0702  233 VAL C CA  
7940  C  C   . VAL C 232 ? 0.4498 0.5394 0.7094 -0.0266 0.0669  0.0724  233 VAL C C   
7941  O  O   . VAL C 232 ? 0.4485 0.5379 0.7071 -0.0264 0.0693  0.0713  233 VAL C O   
7942  C  CB  . VAL C 232 ? 0.4322 0.5184 0.7075 -0.0235 0.0693  0.0754  233 VAL C CB  
7943  C  CG1 . VAL C 232 ? 0.3914 0.4817 0.6728 -0.0200 0.0685  0.0792  233 VAL C CG1 
7944  C  CG2 . VAL C 232 ? 0.4087 0.4884 0.6924 -0.0236 0.0734  0.0740  233 VAL C CG2 
7945  N  N   . VAL C 233 ? 0.4509 0.5449 0.7086 -0.0262 0.0616  0.0753  234 VAL C N   
7946  C  CA  . VAL C 233 ? 0.5282 0.6261 0.7828 -0.0253 0.0581  0.0771  234 VAL C CA  
7947  C  C   . VAL C 233 ? 0.5486 0.6439 0.7944 -0.0291 0.0577  0.0750  234 VAL C C   
7948  O  O   . VAL C 233 ? 0.5368 0.6327 0.7805 -0.0287 0.0578  0.0757  234 VAL C O   
7949  C  CB  . VAL C 233 ? 0.4617 0.5640 0.7180 -0.0246 0.0539  0.0791  234 VAL C CB  
7950  C  CG1 . VAL C 233 ? 0.3542 0.4589 0.6090 -0.0237 0.0507  0.0803  234 VAL C CG1 
7951  C  CG2 . VAL C 233 ? 0.4751 0.5798 0.7369 -0.0225 0.0549  0.0812  234 VAL C CG2 
7952  N  N   . ARG C 234 ? 0.5980 0.6900 0.8375 -0.0338 0.0569  0.0727  235 ARG C N   
7953  C  CA  . ARG C 234 ? 0.6038 0.6927 0.8317 -0.0395 0.0553  0.0716  235 ARG C CA  
7954  C  C   . ARG C 234 ? 0.5601 0.6448 0.7830 -0.0416 0.0624  0.0678  235 ARG C C   
7955  O  O   . ARG C 234 ? 0.5177 0.6018 0.7332 -0.0444 0.0617  0.0685  235 ARG C O   
7956  C  CB  . ARG C 234 ? 0.7024 0.7884 0.9234 -0.0457 0.0524  0.0701  235 ARG C CB  
7957  C  CG  . ARG C 234 ? 0.8280 0.9066 1.0347 -0.0537 0.0563  0.0652  235 ARG C CG  
7958  C  CD  . ARG C 234 ? 0.9409 1.0161 1.1410 -0.0603 0.0536  0.0632  235 ARG C CD  
7959  N  NE  . ARG C 234 ? 1.0566 1.1233 1.2419 -0.0688 0.0596  0.0566  235 ARG C NE  
7960  C  CZ  . ARG C 234 ? 1.1514 1.2124 1.3389 -0.0689 0.0692  0.0498  235 ARG C CZ  
7961  N  NH1 . ARG C 234 ? 1.1645 1.2275 1.3682 -0.0611 0.0721  0.0503  235 ARG C NH1 
7962  N  NH2 . ARG C 234 ? 1.1919 1.2444 1.3653 -0.0773 0.0761  0.0425  235 ARG C NH2 
7963  N  N   . LYS C 235 ? 0.5185 0.6002 0.7471 -0.0403 0.0696  0.0639  236 LYS C N   
7964  C  CA  . LYS C 235 ? 0.5710 0.6492 0.7990 -0.0420 0.0782  0.0593  236 LYS C CA  
7965  C  C   . LYS C 235 ? 0.5448 0.6280 0.7823 -0.0368 0.0792  0.0623  236 LYS C C   
7966  O  O   . LYS C 235 ? 0.4853 0.5678 0.7192 -0.0393 0.0835  0.0604  236 LYS C O   
7967  C  CB  . LYS C 235 ? 0.6004 0.6733 0.8355 -0.0417 0.0860  0.0539  236 LYS C CB  
7968  C  CG  . LYS C 235 ? 0.7016 0.7673 0.9239 -0.0496 0.0878  0.0483  236 LYS C CG  
7969  C  CD  . LYS C 235 ? 0.7308 0.7921 0.9626 -0.0479 0.0914  0.0455  236 LYS C CD  
7970  C  CE  . LYS C 235 ? 0.8051 0.8573 1.0356 -0.0522 0.1031  0.0360  236 LYS C CE  
7971  N  NZ  . LYS C 235 ? 0.8353 0.8800 1.0592 -0.0579 0.1040  0.0312  236 LYS C NZ  
7972  N  N   . VAL C 236 ? 0.5617 0.6496 0.8104 -0.0307 0.0754  0.0670  237 VAL C N   
7973  C  CA  . VAL C 236 ? 0.5294 0.6224 0.7863 -0.0267 0.0746  0.0706  237 VAL C CA  
7974  C  C   . VAL C 236 ? 0.6072 0.7020 0.8550 -0.0287 0.0703  0.0726  237 VAL C C   
7975  O  O   . VAL C 236 ? 0.5952 0.6922 0.8455 -0.0283 0.0718  0.0735  237 VAL C O   
7976  C  CB  . VAL C 236 ? 0.3565 0.4534 0.6230 -0.0219 0.0702  0.0755  237 VAL C CB  
7977  C  CG1 . VAL C 236 ? 0.3978 0.4998 0.6682 -0.0196 0.0670  0.0796  237 VAL C CG1 
7978  C  CG2 . VAL C 236 ? 0.4104 0.5054 0.6890 -0.0197 0.0739  0.0753  237 VAL C CG2 
7979  N  N   . ALA C 237 ? 0.5939 0.6878 0.8329 -0.0310 0.0648  0.0737  238 ALA C N   
7980  C  CA  . ALA C 237 ? 0.6232 0.7177 0.8552 -0.0329 0.0597  0.0764  238 ALA C CA  
7981  C  C   . ALA C 237 ? 0.6992 0.7908 0.9226 -0.0381 0.0633  0.0748  238 ALA C C   
7982  O  O   . ALA C 237 ? 0.7285 0.8210 0.9498 -0.0386 0.0608  0.0776  238 ALA C O   
7983  C  CB  . ALA C 237 ? 0.6170 0.7106 0.8439 -0.0351 0.0532  0.0781  238 ALA C CB  
7984  N  N   . GLN C 238 ? 0.7504 0.8378 0.9681 -0.0426 0.0698  0.0699  239 GLN C N   
7985  C  CA  . GLN C 238 ? 0.7922 0.8761 0.9987 -0.0494 0.0747  0.0673  239 GLN C CA  
7986  C  C   . GLN C 238 ? 0.7448 0.8309 0.9614 -0.0474 0.0837  0.0645  239 GLN C C   
7987  O  O   . GLN C 238 ? 0.7457 0.8289 0.9555 -0.0533 0.0914  0.0601  239 GLN C O   
7988  C  CB  . GLN C 238 ? 0.9047 0.9821 1.0974 -0.0574 0.0782  0.0623  239 GLN C CB  
7989  C  CG  . GLN C 238 ? 1.0162 1.0909 1.1940 -0.0637 0.0685  0.0662  239 GLN C CG  
7990  C  CD  . GLN C 238 ? 1.1363 1.2072 1.2969 -0.0729 0.0680  0.0675  239 GLN C CD  
7991  O  OE1 . GLN C 238 ? 1.1616 1.2345 1.3245 -0.0718 0.0692  0.0697  239 GLN C OE1 
7992  N  NE2 . GLN C 238 ? 1.1660 1.2311 1.3082 -0.0832 0.0656  0.0666  239 GLN C NE2 
7993  N  N   . VAL C 239 ? 0.6706 0.7621 0.9038 -0.0398 0.0828  0.0670  240 VAL C N   
7994  C  CA  . VAL C 239 ? 0.6953 0.7906 0.9418 -0.0375 0.0891  0.0661  240 VAL C CA  
7995  C  C   . VAL C 239 ? 0.7040 0.8023 0.9476 -0.0388 0.0858  0.0699  240 VAL C C   
7996  O  O   . VAL C 239 ? 0.7264 0.8268 0.9698 -0.0362 0.0775  0.0748  240 VAL C O   
7997  C  CB  . VAL C 239 ? 0.6079 0.7077 0.8734 -0.0301 0.0879  0.0686  240 VAL C CB  
7998  C  CG1 . VAL C 239 ? 0.5363 0.6419 0.8172 -0.0278 0.0907  0.0704  240 VAL C CG1 
7999  C  CG2 . VAL C 239 ? 0.5762 0.6723 0.8478 -0.0291 0.0932  0.0644  240 VAL C CG2 
8000  N  N   . PRO C 240 ? 0.7593 0.8574 1.0010 -0.0435 0.0931  0.0671  241 PRO C N   
8001  C  CA  . PRO C 240 ? 0.7343 0.8341 0.9717 -0.0463 0.0906  0.0706  241 PRO C CA  
8002  C  C   . PRO C 240 ? 0.7143 0.8212 0.9687 -0.0408 0.0881  0.0744  241 PRO C C   
8003  O  O   . PRO C 240 ? 0.7113 0.8224 0.9823 -0.0357 0.0900  0.0742  241 PRO C O   
8004  C  CB  . PRO C 240 ? 0.7570 0.8545 0.9878 -0.0538 0.1015  0.0653  241 PRO C CB  
8005  C  CG  . PRO C 240 ? 0.7820 0.8801 1.0261 -0.0513 0.1113  0.0590  241 PRO C CG  
8006  C  CD  . PRO C 240 ? 0.7755 0.8712 1.0197 -0.0468 0.1055  0.0598  241 PRO C CD  
8007  N  N   . LEU C 241 ? 0.6956 0.8034 0.9459 -0.0425 0.0832  0.0783  242 LEU C N   
8008  C  CA  . LEU C 241 ? 0.6673 0.7814 0.9313 -0.0394 0.0806  0.0817  242 LEU C CA  
8009  C  C   . LEU C 241 ? 0.6425 0.7606 0.9150 -0.0427 0.0890  0.0799  242 LEU C C   
8010  O  O   . LEU C 241 ? 0.6872 0.8019 0.9481 -0.0493 0.0938  0.0779  242 LEU C O   
8011  C  CB  . LEU C 241 ? 0.6708 0.7830 0.9272 -0.0398 0.0716  0.0861  242 LEU C CB  
8012  C  CG  . LEU C 241 ? 0.6487 0.7581 0.9004 -0.0362 0.0642  0.0875  242 LEU C CG  
8013  C  CD1 . LEU C 241 ? 0.6567 0.7627 0.9019 -0.0374 0.0574  0.0905  242 LEU C CD1 
8014  C  CD2 . LEU C 241 ? 0.6672 0.7812 0.9306 -0.0311 0.0625  0.0883  242 LEU C CD2 
8015  N  N   . GLY C 242 ? 0.5954 0.7209 0.8884 -0.0389 0.0905  0.0810  243 GLY C N   
8016  C  CA  . GLY C 242 ? 0.5544 0.6855 0.8612 -0.0413 0.0990  0.0792  243 GLY C CA  
8017  C  C   . GLY C 242 ? 0.5451 0.6778 0.8474 -0.0460 0.0966  0.0822  243 GLY C C   
8018  O  O   . GLY C 242 ? 0.5482 0.6783 0.8408 -0.0460 0.0871  0.0863  243 GLY C O   
8019  N  N   . PRO C 243 ? 0.5337 0.6704 0.8440 -0.0502 0.1061  0.0797  244 PRO C N   
8020  C  CA  . PRO C 243 ? 0.5766 0.7152 0.8843 -0.0557 0.1052  0.0824  244 PRO C CA  
8021  C  C   . PRO C 243 ? 0.5654 0.7101 0.8858 -0.0525 0.0953  0.0885  244 PRO C C   
8022  O  O   . PRO C 243 ? 0.5384 0.6804 0.8488 -0.0557 0.0888  0.0919  244 PRO C O   
8023  C  CB  . PRO C 243 ? 0.5891 0.7331 0.9096 -0.0597 0.1196  0.0775  244 PRO C CB  
8024  C  CG  . PRO C 243 ? 0.5542 0.7018 0.8938 -0.0536 0.1257  0.0735  244 PRO C CG  
8025  C  CD  . PRO C 243 ? 0.5683 0.7079 0.8924 -0.0503 0.1195  0.0733  244 PRO C CD  
8026  N  N   . GLU C 244 ? 0.6012 0.7535 0.9434 -0.0469 0.0937  0.0900  245 GLU C N   
8027  C  CA  . GLU C 244 ? 0.6466 0.8045 0.9993 -0.0450 0.0831  0.0962  245 GLU C CA  
8028  C  C   . GLU C 244 ? 0.6379 0.7883 0.9712 -0.0442 0.0725  0.0984  245 GLU C C   
8029  O  O   . GLU C 244 ? 0.5982 0.7478 0.9264 -0.0468 0.0655  0.1014  245 GLU C O   
8030  C  CB  . GLU C 244 ? 0.6927 0.8588 1.0706 -0.0397 0.0818  0.0986  245 GLU C CB  
8031  C  CG  . GLU C 244 ? 0.7734 0.9506 1.1794 -0.0404 0.0879  0.0994  245 GLU C CG  
8032  C  CD  . GLU C 244 ? 0.8458 1.0294 1.2581 -0.0444 0.0803  0.1049  245 GLU C CD  
8033  O  OE1 . GLU C 244 ? 0.8437 1.0232 1.2408 -0.0457 0.0692  0.1085  245 GLU C OE1 
8034  O  OE2 . GLU C 244 ? 0.8459 1.0385 1.2788 -0.0466 0.0859  0.1052  245 GLU C OE2 
8035  N  N   . CYS C 245 ? 0.6274 0.7720 0.9509 -0.0408 0.0723  0.0963  246 CYS C N   
8036  C  CA  . CYS C 245 ? 0.6409 0.7786 0.9479 -0.0398 0.0644  0.0972  246 CYS C CA  
8037  C  C   . CYS C 245 ? 0.6289 0.7597 0.9199 -0.0442 0.0629  0.0970  246 CYS C C   
8038  O  O   . CYS C 245 ? 0.6331 0.7605 0.9176 -0.0447 0.0559  0.0988  246 CYS C O   
8039  C  CB  . CYS C 245 ? 0.6850 0.8182 0.9854 -0.0362 0.0659  0.0946  246 CYS C CB  
8040  S  SG  . CYS C 245 ? 1.4955 1.6211 1.7788 -0.0348 0.0580  0.0950  246 CYS C SG  
8041  N  N   . SER C 246 ? 0.5930 0.7213 0.8776 -0.0481 0.0697  0.0949  247 SER C N   
8042  C  CA  . SER C 246 ? 0.5769 0.6982 0.8468 -0.0532 0.0678  0.0961  247 SER C CA  
8043  C  C   . SER C 246 ? 0.5802 0.7037 0.8552 -0.0563 0.0642  0.0992  247 SER C C   
8044  O  O   . SER C 246 ? 0.5718 0.6889 0.8384 -0.0575 0.0577  0.1011  247 SER C O   
8045  C  CB  . SER C 246 ? 0.6523 0.7711 0.9137 -0.0589 0.0763  0.0938  247 SER C CB  
8046  O  OG  . SER C 246 ? 0.7135 0.8250 0.9601 -0.0648 0.0732  0.0966  247 SER C OG  
8047  N  N   . ARG C 247 ? 0.4959 0.6283 0.7865 -0.0576 0.0685  0.0994  248 ARG C N   
8048  C  CA  . ARG C 247 ? 0.4429 0.5789 0.7406 -0.0611 0.0649  0.1025  248 ARG C CA  
8049  C  C   . ARG C 247 ? 0.4634 0.5978 0.7603 -0.0588 0.0548  0.1044  248 ARG C C   
8050  O  O   . ARG C 247 ? 0.4478 0.5769 0.7376 -0.0621 0.0498  0.1057  248 ARG C O   
8051  C  CB  . ARG C 247 ? 0.4197 0.5676 0.7392 -0.0619 0.0706  0.1027  248 ARG C CB  
8052  C  CG  . ARG C 247 ? 0.4404 0.5902 0.7618 -0.0658 0.0829  0.0994  248 ARG C CG  
8053  C  CD  . ARG C 247 ? 0.4598 0.6225 0.8081 -0.0657 0.0893  0.0993  248 ARG C CD  
8054  N  N   . ALA C 248 ? 0.3983 0.5366 0.7019 -0.0539 0.0522  0.1044  249 ALA C N   
8055  C  CA  . ALA C 248 ? 0.3855 0.5224 0.6863 -0.0530 0.0436  0.1058  249 ALA C CA  
8056  C  C   . ALA C 248 ? 0.4130 0.5388 0.6966 -0.0527 0.0405  0.1036  249 ALA C C   
8057  O  O   . ALA C 248 ? 0.4540 0.5759 0.7327 -0.0550 0.0352  0.1035  249 ALA C O   
8058  C  CB  . ALA C 248 ? 0.3568 0.4990 0.6659 -0.0486 0.0419  0.1068  249 ALA C CB  
8059  N  N   . VAL C 249 ? 0.4334 0.5540 0.7090 -0.0503 0.0440  0.1017  250 VAL C N   
8060  C  CA  . VAL C 249 ? 0.4382 0.5489 0.7017 -0.0494 0.0411  0.1003  250 VAL C CA  
8061  C  C   . VAL C 249 ? 0.4741 0.5783 0.7327 -0.0539 0.0393  0.1016  250 VAL C C   
8062  O  O   . VAL C 249 ? 0.4589 0.5561 0.7133 -0.0541 0.0352  0.1006  250 VAL C O   
8063  C  CB  . VAL C 249 ? 0.3849 0.4925 0.6424 -0.0466 0.0441  0.0991  250 VAL C CB  
8064  C  CG1 . VAL C 249 ? 0.4195 0.5176 0.6682 -0.0464 0.0405  0.0991  250 VAL C CG1 
8065  C  CG2 . VAL C 249 ? 0.3999 0.5115 0.6610 -0.0419 0.0448  0.0976  250 VAL C CG2 
8066  N  N   . MET C 250 ? 0.4628 0.5688 0.7225 -0.0581 0.0431  0.1034  251 MET C N   
8067  C  CA  . MET C 250 ? 0.4607 0.5606 0.7162 -0.0634 0.0413  0.1056  251 MET C CA  
8068  C  C   . MET C 250 ? 0.4569 0.5576 0.7175 -0.0657 0.0370  0.1056  251 MET C C   
8069  O  O   . MET C 250 ? 0.4493 0.5412 0.7053 -0.0676 0.0331  0.1056  251 MET C O   
8070  C  CB  . MET C 250 ? 0.4802 0.5834 0.7360 -0.0688 0.0473  0.1075  251 MET C CB  
8071  C  CG  . MET C 250 ? 0.4397 0.5379 0.6926 -0.0755 0.0456  0.1105  251 MET C CG  
8072  S  SD  . MET C 250 ? 0.5274 0.6102 0.7695 -0.0758 0.0381  0.1128  251 MET C SD  
8073  C  CE  . MET C 250 ? 0.5153 0.5943 0.7590 -0.0837 0.0364  0.1160  251 MET C CE  
8074  N  N   . LYS C 251 ? 0.4453 0.5561 0.7161 -0.0657 0.0373  0.1057  252 LYS C N   
8075  C  CA  . LYS C 251 ? 0.4562 0.5687 0.7310 -0.0692 0.0322  0.1061  252 LYS C CA  
8076  C  C   . LYS C 251 ? 0.4472 0.5521 0.7137 -0.0675 0.0275  0.1029  252 LYS C C   
8077  O  O   . LYS C 251 ? 0.4847 0.5840 0.7478 -0.0717 0.0239  0.1016  252 LYS C O   
8078  C  CB  . LYS C 251 ? 0.4669 0.5926 0.7561 -0.0694 0.0319  0.1082  252 LYS C CB  
8079  C  CG  . LYS C 251 ? 0.4763 0.6056 0.7709 -0.0752 0.0259  0.1101  252 LYS C CG  
8080  C  CD  . LYS C 251 ? 0.5407 0.6843 0.8537 -0.0754 0.0250  0.1139  252 LYS C CD  
8081  C  CE  . LYS C 251 ? 0.6061 0.7548 0.9267 -0.0827 0.0187  0.1170  252 LYS C CE  
8082  N  NZ  . LYS C 251 ? 0.6406 0.7864 0.9528 -0.0856 0.0098  0.1169  252 LYS C NZ  
8083  N  N   . LEU C 252 ? 0.5104 0.6147 0.7737 -0.0621 0.0286  0.1010  253 LEU C N   
8084  C  CA  . LEU C 252 ? 0.4963 0.5942 0.7523 -0.0604 0.0262  0.0971  253 LEU C CA  
8085  C  C   . LEU C 252 ? 0.5527 0.6383 0.8028 -0.0601 0.0262  0.0945  253 LEU C C   
8086  O  O   . LEU C 252 ? 0.4022 0.4808 0.6486 -0.0624 0.0244  0.0908  253 LEU C O   
8087  C  CB  . LEU C 252 ? 0.4846 0.5860 0.7402 -0.0549 0.0279  0.0962  253 LEU C CB  
8088  C  CG  . LEU C 252 ? 0.4749 0.5705 0.7234 -0.0530 0.0274  0.0917  253 LEU C CG  
8089  C  CD1 . LEU C 252 ? 0.4334 0.5294 0.6777 -0.0580 0.0240  0.0901  253 LEU C CD1 
8090  C  CD2 . LEU C 252 ? 0.3751 0.4744 0.6243 -0.0477 0.0297  0.0917  253 LEU C CD2 
8091  N  N   . VAL C 253 ? 0.5235 0.6060 0.7733 -0.0578 0.0280  0.0965  254 VAL C N   
8092  C  CA  . VAL C 253 ? 0.5254 0.5968 0.7727 -0.0560 0.0270  0.0955  254 VAL C CA  
8093  C  C   . VAL C 253 ? 0.6284 0.6917 0.8757 -0.0607 0.0249  0.0977  254 VAL C C   
8094  O  O   . VAL C 253 ? 0.7093 0.7634 0.9572 -0.0613 0.0233  0.0946  254 VAL C O   
8095  C  CB  . VAL C 253 ? 0.4192 0.4906 0.6655 -0.0522 0.0280  0.0979  254 VAL C CB  
8096  C  CG1 . VAL C 253 ? 0.4029 0.4637 0.6502 -0.0503 0.0253  0.0982  254 VAL C CG1 
8097  C  CG2 . VAL C 253 ? 0.3872 0.4656 0.6339 -0.0477 0.0301  0.0956  254 VAL C CG2 
8098  N  N   . TYR C 254 ? 0.5725 0.6384 0.8193 -0.0644 0.0255  0.1026  255 TYR C N   
8099  C  CA  . TYR C 254 ? 0.5513 0.6084 0.7970 -0.0691 0.0233  0.1061  255 TYR C CA  
8100  C  C   . TYR C 254 ? 0.5593 0.6194 0.8071 -0.0758 0.0234  0.1072  255 TYR C C   
8101  O  O   . TYR C 254 ? 0.5674 0.6198 0.8144 -0.0806 0.0216  0.1101  255 TYR C O   
8102  C  CB  . TYR C 254 ? 0.5051 0.5605 0.7463 -0.0704 0.0236  0.1117  255 TYR C CB  
8103  C  CG  . TYR C 254 ? 0.5452 0.5956 0.7854 -0.0651 0.0213  0.1121  255 TYR C CG  
8104  C  CD1 . TYR C 254 ? 0.4288 0.4700 0.6743 -0.0615 0.0179  0.1102  255 TYR C CD1 
8105  C  CD2 . TYR C 254 ? 0.5061 0.5613 0.7415 -0.0641 0.0230  0.1140  255 TYR C CD2 
8106  C  CE1 . TYR C 254 ? 0.4510 0.4890 0.6993 -0.0566 0.0156  0.1111  255 TYR C CE1 
8107  C  CE2 . TYR C 254 ? 0.5465 0.5980 0.7820 -0.0599 0.0200  0.1150  255 TYR C CE2 
8108  C  CZ  . TYR C 254 ? 0.5402 0.5837 0.7832 -0.0560 0.0160  0.1139  255 TYR C CZ  
8109  O  OH  . TYR C 254 ? 0.5557 0.5969 0.8023 -0.0518 0.0128  0.1153  255 TYR C OH  
8110  N  N   . CYS C 255 ? 0.4947 0.5659 0.7464 -0.0766 0.0249  0.1056  256 CYS C N   
8111  C  CA  . CYS C 255 ? 0.4999 0.5757 0.7561 -0.0832 0.0243  0.1071  256 CYS C CA  
8112  C  C   . CYS C 255 ? 0.5562 0.6238 0.8109 -0.0866 0.0201  0.1038  256 CYS C C   
8113  O  O   . CYS C 255 ? 0.5673 0.6357 0.8248 -0.0932 0.0185  0.1050  256 CYS C O   
8114  C  CB  . CYS C 255 ? 0.4726 0.5635 0.7369 -0.0829 0.0260  0.1075  256 CYS C CB  
8115  S  SG  . CYS C 255 ? 0.5532 0.6539 0.8230 -0.0832 0.0333  0.1109  256 CYS C SG  
8116  N  N   . ALA C 256 ? 0.5694 0.6289 0.8201 -0.0827 0.0191  0.0990  257 ALA C N   
8117  C  CA  . ALA C 256 ? 0.4442 0.4928 0.6923 -0.0862 0.0169  0.0942  257 ALA C CA  
8118  C  C   . ALA C 256 ? 0.5680 0.6041 0.8172 -0.0886 0.0159  0.0967  257 ALA C C   
8119  O  O   . ALA C 256 ? 0.6099 0.6398 0.8593 -0.0949 0.0140  0.0958  257 ALA C O   
8120  C  CB  . ALA C 256 ? 0.4448 0.4879 0.6895 -0.0815 0.0182  0.0875  257 ALA C CB  
8121  N  N   . HIS C 257 ? 0.5522 0.5845 0.8021 -0.0842 0.0164  0.1005  258 HIS C N   
8122  C  CA  . HIS C 257 ? 0.5601 0.5803 0.8112 -0.0864 0.0141  0.1050  258 HIS C CA  
8123  C  C   . HIS C 257 ? 0.6036 0.6268 0.8538 -0.0945 0.0137  0.1105  258 HIS C C   
8124  O  O   . HIS C 257 ? 0.5835 0.5963 0.8348 -0.0996 0.0114  0.1121  258 HIS C O   
8125  C  CB  . HIS C 257 ? 0.5974 0.6153 0.8482 -0.0815 0.0133  0.1098  258 HIS C CB  
8126  C  CG  . HIS C 257 ? 0.6853 0.7011 0.9395 -0.0736 0.0138  0.1050  258 HIS C CG  
8127  N  ND1 . HIS C 257 ? 0.6900 0.7153 0.9427 -0.0699 0.0170  0.0997  258 HIS C ND1 
8128  C  CD2 . HIS C 257 ? 0.6943 0.6998 0.9549 -0.0690 0.0117  0.1053  258 HIS C CD2 
8129  C  CE1 . HIS C 257 ? 0.6858 0.7070 0.9425 -0.0637 0.0175  0.0962  258 HIS C CE1 
8130  N  NE2 . HIS C 257 ? 0.6940 0.7037 0.9569 -0.0628 0.0144  0.0993  258 HIS C NE2 
8131  N  N   . CYS C 258 ? 0.5407 0.5778 0.7902 -0.0958 0.0166  0.1130  259 CYS C N   
8132  C  CA  . CYS C 258 ? 0.5485 0.5907 0.7990 -0.1035 0.0181  0.1178  259 CYS C CA  
8133  C  C   . CYS C 258 ? 0.5666 0.6098 0.8215 -0.1095 0.0161  0.1153  259 CYS C C   
8134  O  O   . CYS C 258 ? 0.5818 0.6205 0.8374 -0.1167 0.0152  0.1186  259 CYS C O   
8135  C  CB  . CYS C 258 ? 0.5443 0.6019 0.7964 -0.1029 0.0233  0.1193  259 CYS C CB  
8136  S  SG  . CYS C 258 ? 0.7996 0.8556 1.0435 -0.0997 0.0260  0.1228  259 CYS C SG  
8137  N  N   . LEU C 259 ? 0.5796 0.6283 0.8363 -0.1075 0.0150  0.1099  260 LEU C N   
8138  C  CA  . LEU C 259 ? 0.5269 0.5774 0.7864 -0.1144 0.0121  0.1078  260 LEU C CA  
8139  C  C   . LEU C 259 ? 0.5473 0.5814 0.8020 -0.1164 0.0092  0.1023  260 LEU C C   
8140  O  O   . LEU C 259 ? 0.5896 0.6238 0.8427 -0.1210 0.0067  0.0977  260 LEU C O   
8141  C  CB  . LEU C 259 ? 0.5227 0.5877 0.7859 -0.1134 0.0112  0.1060  260 LEU C CB  
8142  C  CG  . LEU C 259 ? 0.5402 0.6220 0.8130 -0.1127 0.0145  0.1110  260 LEU C CG  
8143  C  CD1 . LEU C 259 ? 0.5672 0.6616 0.8453 -0.1095 0.0129  0.1101  260 LEU C CD1 
8144  C  CD2 . LEU C 259 ? 0.5741 0.6613 0.8552 -0.1212 0.0144  0.1150  260 LEU C CD2 
8145  N  N   . GLY C 260 ? 0.6252 0.6451 0.8782 -0.1134 0.0096  0.1027  261 GLY C N   
8146  C  CA  . GLY C 260 ? 0.6853 0.6879 0.9376 -0.1158 0.0079  0.0980  261 GLY C CA  
8147  C  C   . GLY C 260 ? 0.7554 0.7507 1.0052 -0.1116 0.0093  0.0886  261 GLY C C   
8148  O  O   . GLY C 260 ? 0.8039 0.7862 1.0527 -0.1154 0.0092  0.0823  261 GLY C O   
8149  N  N   . VAL C 261 ? 0.7440 0.7468 0.9924 -0.1044 0.0114  0.0869  262 VAL C N   
8150  C  CA  . VAL C 261 ? 0.6843 0.6805 0.9304 -0.1004 0.0141  0.0778  262 VAL C CA  
8151  C  C   . VAL C 261 ? 0.6846 0.6815 0.9346 -0.0905 0.0164  0.0789  262 VAL C C   
8152  O  O   . VAL C 261 ? 0.6438 0.6496 0.8907 -0.0867 0.0183  0.0765  262 VAL C O   
8153  C  CB  . VAL C 261 ? 0.7173 0.7227 0.9553 -0.1043 0.0141  0.0727  262 VAL C CB  
8154  C  CG1 . VAL C 261 ? 0.7229 0.7218 0.9558 -0.1147 0.0121  0.0679  262 VAL C CG1 
8155  C  CG2 . VAL C 261 ? 0.6959 0.7199 0.9350 -0.1037 0.0122  0.0797  262 VAL C CG2 
8156  N  N   . PRO C 262 ? 0.6819 0.6691 0.9390 -0.0871 0.0153  0.0832  263 PRO C N   
8157  C  CA  . PRO C 262 ? 0.6749 0.6630 0.9370 -0.0786 0.0158  0.0858  263 PRO C CA  
8158  C  C   . PRO C 262 ? 0.6924 0.6755 0.9585 -0.0731 0.0200  0.0765  263 PRO C C   
8159  O  O   . PRO C 262 ? 0.6455 0.6337 0.9145 -0.0665 0.0211  0.0771  263 PRO C O   
8160  C  CB  . PRO C 262 ? 0.6694 0.6462 0.9387 -0.0786 0.0117  0.0934  263 PRO C CB  
8161  C  CG  . PRO C 262 ? 0.6982 0.6712 0.9644 -0.0874 0.0098  0.0960  263 PRO C CG  
8162  C  CD  . PRO C 262 ? 0.6806 0.6549 0.9421 -0.0916 0.0125  0.0866  263 PRO C CD  
8163  N  N   . GLY C 263 ? 0.7060 0.6790 0.9720 -0.0767 0.0229  0.0675  264 GLY C N   
8164  C  CA  . GLY C 263 ? 0.7319 0.6992 1.0013 -0.0730 0.0289  0.0570  264 GLY C CA  
8165  C  C   . GLY C 263 ? 0.7370 0.7157 0.9945 -0.0743 0.0321  0.0517  264 GLY C C   
8166  O  O   . GLY C 263 ? 0.7576 0.7350 1.0161 -0.0711 0.0378  0.0439  264 GLY C O   
8167  N  N   . ALA C 264 ? 0.7630 0.7532 1.0104 -0.0794 0.0284  0.0564  265 ALA C N   
8168  C  CA  . ALA C 264 ? 0.7576 0.7592 0.9946 -0.0813 0.0295  0.0538  265 ALA C CA  
8169  C  C   . ALA C 264 ? 0.7455 0.7582 0.9855 -0.0735 0.0297  0.0589  265 ALA C C   
8170  O  O   . ALA C 264 ? 0.7128 0.7297 0.9585 -0.0698 0.0269  0.0671  265 ALA C O   
8171  C  CB  . ALA C 264 ? 0.7711 0.7809 1.0003 -0.0895 0.0246  0.0577  265 ALA C CB  
8172  N  N   . ARG C 265 ? 0.7681 0.7848 1.0030 -0.0721 0.0333  0.0537  266 ARG C N   
8173  C  CA  . ARG C 265 ? 0.8012 0.8282 1.0381 -0.0656 0.0336  0.0578  266 ARG C CA  
8174  C  C   . ARG C 265 ? 0.7989 0.8366 1.0254 -0.0695 0.0326  0.0580  266 ARG C C   
8175  O  O   . ARG C 265 ? 0.8601 0.8950 1.0767 -0.0762 0.0337  0.0520  266 ARG C O   
8176  C  CB  . ARG C 265 ? 0.8798 0.9014 1.1244 -0.0590 0.0388  0.0526  266 ARG C CB  
8177  C  CG  . ARG C 265 ? 0.9456 0.9614 1.2039 -0.0533 0.0367  0.0576  266 ARG C CG  
8178  C  CD  . ARG C 265 ? 1.0126 1.0194 1.2834 -0.0481 0.0415  0.0513  266 ARG C CD  
8179  N  NE  . ARG C 265 ? 1.0702 1.0705 1.3552 -0.0438 0.0373  0.0577  266 ARG C NE  
8180  C  CZ  . ARG C 265 ? 1.1235 1.1120 1.4238 -0.0408 0.0394  0.0540  266 ARG C CZ  
8181  N  NH1 . ARG C 265 ? 1.1411 1.1229 1.4440 -0.0416 0.0474  0.0421  266 ARG C NH1 
8182  N  NH2 . ARG C 265 ? 1.1317 1.1148 1.4449 -0.0376 0.0335  0.0622  266 ARG C NH2 
8183  N  N   . PRO C 266 ? 0.6976 0.7469 0.9262 -0.0660 0.0303  0.0651  267 PRO C N   
8184  C  CA  . PRO C 266 ? 0.6499 0.7103 0.8730 -0.0693 0.0273  0.0685  267 PRO C CA  
8185  C  C   . PRO C 266 ? 0.5823 0.6424 0.7944 -0.0735 0.0288  0.0631  267 PRO C C   
8186  O  O   . PRO C 266 ? 0.5624 0.6176 0.7729 -0.0708 0.0342  0.0570  267 PRO C O   
8187  C  CB  . PRO C 266 ? 0.6547 0.7238 0.8845 -0.0623 0.0275  0.0744  267 PRO C CB  
8188  C  CG  . PRO C 266 ? 0.6730 0.7372 0.9098 -0.0585 0.0281  0.0767  267 PRO C CG  
8189  C  CD  . PRO C 266 ? 0.7070 0.7586 0.9441 -0.0589 0.0302  0.0705  267 PRO C CD  
8190  N  N   . CYS C 267 ? 0.5574 0.6231 0.7625 -0.0809 0.0239  0.0657  268 CYS C N   
8191  C  CA  . CYS C 267 ? 0.5695 0.6363 0.7618 -0.0867 0.0236  0.0629  268 CYS C CA  
8192  C  C   . CYS C 267 ? 0.5460 0.6202 0.7409 -0.0806 0.0249  0.0663  268 CYS C C   
8193  O  O   . CYS C 267 ? 0.5426 0.6251 0.7481 -0.0750 0.0224  0.0736  268 CYS C O   
8194  C  CB  . CYS C 267 ? 0.5832 0.6555 0.7692 -0.0965 0.0154  0.0677  268 CYS C CB  
8195  S  SG  . CYS C 267 ? 1.1626 1.2278 1.3470 -0.1045 0.0125  0.0652  268 CYS C SG  
8196  N  N   . PRO C 268 ? 0.5848 0.6556 0.7702 -0.0821 0.0296  0.0605  269 PRO C N   
8197  C  CA  . PRO C 268 ? 0.6026 0.6791 0.7897 -0.0770 0.0315  0.0629  269 PRO C CA  
8198  C  C   . PRO C 268 ? 0.5657 0.6530 0.7551 -0.0778 0.0242  0.0729  269 PRO C C   
8199  O  O   . PRO C 268 ? 0.5728 0.6658 0.7719 -0.0704 0.0247  0.0774  269 PRO C O   
8200  C  CB  . PRO C 268 ? 0.6426 0.7130 0.8150 -0.0831 0.0372  0.0546  269 PRO C CB  
8201  C  CG  . PRO C 268 ? 0.6248 0.6842 0.7939 -0.0867 0.0418  0.0453  269 PRO C CG  
8202  C  CD  . PRO C 268 ? 0.5924 0.6527 0.7645 -0.0896 0.0345  0.0502  269 PRO C CD  
8203  N  N   . ASP C 269 ? 0.5031 0.5929 0.6849 -0.0868 0.0173  0.0765  270 ASP C N   
8204  C  CA  . ASP C 269 ? 0.5626 0.6627 0.7499 -0.0879 0.0093  0.0870  270 ASP C CA  
8205  C  C   . ASP C 269 ? 0.5363 0.6437 0.7430 -0.0813 0.0069  0.0932  270 ASP C C   
8206  O  O   . ASP C 269 ? 0.5007 0.6159 0.7189 -0.0767 0.0049  0.1000  270 ASP C O   
8207  C  CB  . ASP C 269 ? 0.5944 0.6953 0.7690 -0.1005 0.0010  0.0901  270 ASP C CB  
8208  C  CG  . ASP C 269 ? 0.6690 0.7635 0.8219 -0.1088 0.0035  0.0847  270 ASP C CG  
8209  O  OD1 . ASP C 269 ? 0.6847 0.7779 0.8361 -0.1040 0.0100  0.0818  270 ASP C OD1 
8210  O  OD2 . ASP C 269 ? 0.7394 0.8302 0.8761 -0.1211 -0.0007 0.0832  270 ASP C OD2 
8211  N  N   . TYR C 270 ? 0.4744 0.5783 0.6845 -0.0815 0.0080  0.0906  271 TYR C N   
8212  C  CA  . TYR C 270 ? 0.4673 0.5770 0.6939 -0.0765 0.0078  0.0951  271 TYR C CA  
8213  C  C   . TYR C 270 ? 0.4391 0.5493 0.6732 -0.0667 0.0140  0.0946  271 TYR C C   
8214  O  O   . TYR C 270 ? 0.4505 0.5683 0.6966 -0.0624 0.0138  0.0998  271 TYR C O   
8215  C  CB  . TYR C 270 ? 0.4594 0.5632 0.6855 -0.0795 0.0085  0.0917  271 TYR C CB  
8216  C  CG  . TYR C 270 ? 0.4603 0.5689 0.7009 -0.0759 0.0093  0.0958  271 TYR C CG  
8217  C  CD1 . TYR C 270 ? 0.4375 0.5571 0.6923 -0.0727 0.0081  0.1024  271 TYR C CD1 
8218  C  CD2 . TYR C 270 ? 0.4862 0.5877 0.7267 -0.0763 0.0119  0.0928  271 TYR C CD2 
8219  C  CE1 . TYR C 270 ? 0.4488 0.5726 0.7159 -0.0704 0.0108  0.1049  271 TYR C CE1 
8220  C  CE2 . TYR C 270 ? 0.4836 0.5891 0.7350 -0.0745 0.0132  0.0966  271 TYR C CE2 
8221  C  CZ  . TYR C 270 ? 0.4875 0.6043 0.7515 -0.0719 0.0133  0.1021  271 TYR C CZ  
8222  O  OH  . TYR C 270 ? 0.5397 0.6604 0.8137 -0.0711 0.0164  0.1047  271 TYR C OH  
8223  N  N   . CYS C 271 ? 0.4577 0.5594 0.6854 -0.0637 0.0195  0.0880  272 CYS C N   
8224  C  CA  . CYS C 271 ? 0.4503 0.5517 0.6831 -0.0557 0.0243  0.0873  272 CYS C CA  
8225  C  C   . CYS C 271 ? 0.4576 0.5654 0.6930 -0.0529 0.0241  0.0908  272 CYS C C   
8226  O  O   . CYS C 271 ? 0.4612 0.5733 0.7055 -0.0478 0.0257  0.0937  272 CYS C O   
8227  C  CB  . CYS C 271 ? 0.4563 0.5484 0.6836 -0.0538 0.0290  0.0802  272 CYS C CB  
8228  S  SG  . CYS C 271 ? 0.6007 0.6925 0.8345 -0.0452 0.0332  0.0801  272 CYS C SG  
8229  N  N   . ARG C 272 ? 0.3888 0.4964 0.6153 -0.0570 0.0223  0.0902  273 ARG C N   
8230  C  CA  . ARG C 272 ? 0.4937 0.6061 0.7218 -0.0552 0.0215  0.0940  273 ARG C CA  
8231  C  C   . ARG C 272 ? 0.4573 0.5784 0.6984 -0.0543 0.0167  0.1021  273 ARG C C   
8232  O  O   . ARG C 272 ? 0.3717 0.4964 0.6213 -0.0493 0.0182  0.1049  273 ARG C O   
8233  C  CB  . ARG C 272 ? 0.4918 0.6018 0.7056 -0.0620 0.0200  0.0926  273 ARG C CB  
8234  C  CG  . ARG C 272 ? 0.4906 0.5940 0.6962 -0.0607 0.0273  0.0845  273 ARG C CG  
8235  C  CD  . ARG C 272 ? 0.5815 0.6833 0.7724 -0.0679 0.0273  0.0832  273 ARG C CD  
8236  N  NE  . ARG C 272 ? 0.7289 0.8272 0.9063 -0.0782 0.0242  0.0812  273 ARG C NE  
8237  C  CZ  . ARG C 272 ? 0.8276 0.9177 0.9939 -0.0827 0.0301  0.0717  273 ARG C CZ  
8238  N  NH1 . ARG C 272 ? 0.8448 0.9304 1.0152 -0.0770 0.0390  0.0640  273 ARG C NH1 
8239  N  NH2 . ARG C 272 ? 0.8413 0.9277 0.9937 -0.0933 0.0271  0.0697  273 ARG C NH2 
8240  N  N   . ASN C 273 ? 0.3835 0.5080 0.6281 -0.0592 0.0114  0.1057  274 ASN C N   
8241  C  CA  . ASN C 273 ? 0.3802 0.5139 0.6421 -0.0580 0.0074  0.1133  274 ASN C CA  
8242  C  C   . ASN C 273 ? 0.3841 0.5199 0.6590 -0.0511 0.0138  0.1121  274 ASN C C   
8243  O  O   . ASN C 273 ? 0.3673 0.5083 0.6559 -0.0468 0.0152  0.1156  274 ASN C O   
8244  C  CB  . ASN C 273 ? 0.4977 0.6352 0.7620 -0.0653 0.0001  0.1172  274 ASN C CB  
8245  C  CG  . ASN C 273 ? 0.5946 0.7352 0.8543 -0.0725 -0.0092 0.1236  274 ASN C CG  
8246  O  OD1 . ASN C 273 ? 0.5648 0.7086 0.8298 -0.0704 -0.0114 0.1287  274 ASN C OD1 
8247  N  ND2 . ASN C 273 ? 0.5862 0.7252 0.8355 -0.0818 -0.0153 0.1238  274 ASN C ND2 
8248  N  N   . VAL C 274 ? 0.3712 0.5018 0.6413 -0.0506 0.0179  0.1072  275 VAL C N   
8249  C  CA  . VAL C 274 ? 0.3599 0.4911 0.6378 -0.0461 0.0240  0.1060  275 VAL C CA  
8250  C  C   . VAL C 274 ? 0.4795 0.6092 0.7571 -0.0404 0.0288  0.1042  275 VAL C C   
8251  O  O   . VAL C 274 ? 0.4936 0.6273 0.7818 -0.0373 0.0325  0.1054  275 VAL C O   
8252  C  CB  . VAL C 274 ? 0.3631 0.4873 0.6333 -0.0475 0.0263  0.1020  275 VAL C CB  
8253  C  CG1 . VAL C 274 ? 0.3588 0.4822 0.6322 -0.0441 0.0323  0.1010  275 VAL C CG1 
8254  C  CG2 . VAL C 274 ? 0.3684 0.4945 0.6412 -0.0533 0.0224  0.1038  275 VAL C CG2 
8255  N  N   . LEU C 275 ? 0.4951 0.6190 0.7613 -0.0396 0.0292  0.1009  276 LEU C N   
8256  C  CA  . LEU C 275 ? 0.4474 0.5697 0.7129 -0.0349 0.0331  0.0991  276 LEU C CA  
8257  C  C   . LEU C 275 ? 0.4248 0.5521 0.6981 -0.0333 0.0321  0.1029  276 LEU C C   
8258  O  O   . LEU C 275 ? 0.3448 0.4725 0.6233 -0.0295 0.0360  0.1024  276 LEU C O   
8259  C  CB  . LEU C 275 ? 0.3543 0.4703 0.6088 -0.0346 0.0339  0.0947  276 LEU C CB  
8260  C  CG  . LEU C 275 ? 0.4013 0.5112 0.6517 -0.0344 0.0354  0.0912  276 LEU C CG  
8261  C  CD1 . LEU C 275 ? 0.4212 0.5263 0.6670 -0.0322 0.0373  0.0872  276 LEU C CD1 
8262  C  CD2 . LEU C 275 ? 0.3810 0.4913 0.6358 -0.0329 0.0376  0.0926  276 LEU C CD2 
8263  N  N   . LYS C 276 ? 0.4236 0.5538 0.6972 -0.0368 0.0264  0.1070  277 LYS C N   
8264  C  CA  . LYS C 276 ? 0.3525 0.4872 0.6358 -0.0358 0.0238  0.1125  277 LYS C CA  
8265  C  C   . LYS C 276 ? 0.3930 0.5338 0.6958 -0.0329 0.0255  0.1154  277 LYS C C   
8266  O  O   . LYS C 276 ? 0.3453 0.4882 0.6600 -0.0295 0.0271  0.1178  277 LYS C O   
8267  C  CB  . LYS C 276 ? 0.3609 0.4975 0.6394 -0.0419 0.0156  0.1177  277 LYS C CB  
8268  C  CG  . LYS C 276 ? 0.3676 0.4986 0.6279 -0.0451 0.0156  0.1147  277 LYS C CG  
8269  C  CD  . LYS C 276 ? 0.3790 0.5115 0.6326 -0.0528 0.0073  0.1208  277 LYS C CD  
8270  C  CE  . LYS C 276 ? 0.4366 0.5633 0.6708 -0.0572 0.0093  0.1168  277 LYS C CE  
8271  N  NZ  . LYS C 276 ? 0.4904 0.6179 0.7147 -0.0665 0.0011  0.1233  277 LYS C NZ  
8272  N  N   . GLY C 277 ? 0.3888 0.5318 0.6957 -0.0346 0.0261  0.1149  278 GLY C N   
8273  C  CA  . GLY C 277 ? 0.3643 0.5130 0.6898 -0.0323 0.0303  0.1159  278 GLY C CA  
8274  C  C   . GLY C 277 ? 0.3623 0.5073 0.6866 -0.0285 0.0397  0.1102  278 GLY C C   
8275  O  O   . GLY C 277 ? 0.4196 0.5674 0.7585 -0.0255 0.0449  0.1100  278 GLY C O   
8276  N  N   . CYS C 278 ? 0.3418 0.4801 0.6492 -0.0291 0.0418  0.1055  279 CYS C N   
8277  C  CA  . CYS C 278 ? 0.4180 0.5521 0.7207 -0.0274 0.0491  0.1008  279 CYS C CA  
8278  C  C   . CYS C 278 ? 0.4432 0.5745 0.7443 -0.0242 0.0510  0.0993  279 CYS C C   
8279  O  O   . CYS C 278 ? 0.4430 0.5728 0.7466 -0.0229 0.0574  0.0962  279 CYS C O   
8280  C  CB  . CYS C 278 ? 0.4623 0.5902 0.7495 -0.0296 0.0488  0.0980  279 CYS C CB  
8281  S  SG  . CYS C 278 ? 0.6665 0.7957 0.9547 -0.0341 0.0484  0.0990  279 CYS C SG  
8282  N  N   . LEU C 279 ? 0.4753 0.6055 0.7711 -0.0238 0.0458  0.1011  280 LEU C N   
8283  C  CA  . LEU C 279 ? 0.4489 0.5760 0.7414 -0.0214 0.0472  0.0998  280 LEU C CA  
8284  C  C   . LEU C 279 ? 0.4390 0.5692 0.7432 -0.0200 0.0449  0.1044  280 LEU C C   
8285  O  O   . LEU C 279 ? 0.4255 0.5534 0.7250 -0.0196 0.0431  0.1053  280 LEU C O   
8286  C  CB  . LEU C 279 ? 0.4582 0.5813 0.7365 -0.0224 0.0444  0.0981  280 LEU C CB  
8287  C  CG  . LEU C 279 ? 0.4546 0.5737 0.7239 -0.0234 0.0455  0.0946  280 LEU C CG  
8288  C  CD1 . LEU C 279 ? 0.4534 0.5693 0.7139 -0.0240 0.0431  0.0928  280 LEU C CD1 
8289  C  CD2 . LEU C 279 ? 0.4532 0.5696 0.7207 -0.0224 0.0499  0.0919  280 LEU C CD2 
8290  N  N   . ALA C 280 ? 0.4809 0.6162 0.8015 -0.0195 0.0447  0.1078  281 ALA C N   
8291  C  CA  . ALA C 280 ? 0.4662 0.6047 0.8020 -0.0181 0.0411  0.1139  281 ALA C CA  
8292  C  C   . ALA C 280 ? 0.4954 0.6300 0.8365 -0.0146 0.0463  0.1117  281 ALA C C   
8293  O  O   . ALA C 280 ? 0.5317 0.6645 0.8720 -0.0144 0.0425  0.1153  281 ALA C O   
8294  C  CB  . ALA C 280 ? 0.5079 0.6535 0.8649 -0.0177 0.0403  0.1179  281 ALA C CB  
8295  N  N   . ASN C 281 ? 0.4969 0.6297 0.8422 -0.0128 0.0552  0.1056  282 ASN C N   
8296  C  CA  . ASN C 281 ? 0.4614 0.5894 0.8108 -0.0104 0.0613  0.1019  282 ASN C CA  
8297  C  C   . ASN C 281 ? 0.4911 0.6138 0.8232 -0.0113 0.0593  0.1004  282 ASN C C   
8298  O  O   . ASN C 281 ? 0.5488 0.6685 0.8851 -0.0099 0.0594  0.1015  282 ASN C O   
8299  C  CB  . ASN C 281 ? 0.4164 0.5423 0.7668 -0.0108 0.0719  0.0941  282 ASN C CB  
8300  C  CG  . ASN C 281 ? 0.3706 0.5018 0.7440 -0.0093 0.0769  0.0944  282 ASN C CG  
8301  O  OD1 . ASN C 281 ? 0.3454 0.4794 0.7405 -0.0062 0.0754  0.0989  282 ASN C OD1 
8302  N  ND2 . ASN C 281 ? 0.4156 0.5484 0.7858 -0.0119 0.0827  0.0901  282 ASN C ND2 
8303  N  N   . GLN C 282 ? 0.4831 0.6046 0.7976 -0.0136 0.0576  0.0981  283 GLN C N   
8304  C  CA  . GLN C 282 ? 0.4490 0.5670 0.7498 -0.0144 0.0555  0.0969  283 GLN C CA  
8305  C  C   . GLN C 282 ? 0.4219 0.5412 0.7231 -0.0150 0.0494  0.1026  283 GLN C C   
8306  O  O   . GLN C 282 ? 0.4581 0.5748 0.7560 -0.0151 0.0492  0.1029  283 GLN C O   
8307  C  CB  . GLN C 282 ? 0.3385 0.4556 0.6251 -0.0163 0.0544  0.0940  283 GLN C CB  
8308  C  CG  . GLN C 282 ? 0.4278 0.5418 0.7088 -0.0173 0.0592  0.0891  283 GLN C CG  
8309  C  CD  . GLN C 282 ? 0.4267 0.5426 0.7134 -0.0182 0.0627  0.0884  283 GLN C CD  
8310  O  OE1 . GLN C 282 ? 0.4475 0.5679 0.7456 -0.0173 0.0617  0.0916  283 GLN C OE1 
8311  N  NE2 . GLN C 282 ? 0.3467 0.4597 0.6256 -0.0209 0.0667  0.0846  283 GLN C NE2 
8312  N  N   . ALA C 283 ? 0.3409 0.4643 0.6452 -0.0166 0.0442  0.1076  284 ALA C N   
8313  C  CA  . ALA C 283 ? 0.3448 0.4693 0.6463 -0.0194 0.0375  0.1137  284 ALA C CA  
8314  C  C   . ALA C 283 ? 0.4834 0.6075 0.7985 -0.0179 0.0357  0.1194  284 ALA C C   
8315  O  O   . ALA C 283 ? 0.4977 0.6206 0.8081 -0.0207 0.0310  0.1244  284 ALA C O   
8316  C  CB  . ALA C 283 ? 0.3472 0.4758 0.6478 -0.0228 0.0316  0.1177  284 ALA C CB  
8317  N  N   . ASP C 284 ? 0.4471 0.5714 0.7793 -0.0141 0.0400  0.1185  285 ASP C N   
8318  C  CA  . ASP C 284 ? 0.4167 0.5396 0.7660 -0.0118 0.0393  0.1233  285 ASP C CA  
8319  C  C   . ASP C 284 ? 0.4570 0.5737 0.7996 -0.0116 0.0422  0.1209  285 ASP C C   
8320  O  O   . ASP C 284 ? 0.4509 0.5648 0.8056 -0.0104 0.0409  0.1254  285 ASP C O   
8321  C  CB  . ASP C 284 ? 0.4325 0.5567 0.8035 -0.0076 0.0456  0.1208  285 ASP C CB  
8322  C  CG  . ASP C 284 ? 0.4917 0.6228 0.8824 -0.0072 0.0400  0.1285  285 ASP C CG  
8323  O  OD1 . ASP C 284 ? 0.4606 0.5953 0.8445 -0.0111 0.0304  0.1355  285 ASP C OD1 
8324  O  OD2 . ASP C 284 ? 0.4225 0.5556 0.8359 -0.0036 0.0453  0.1272  285 ASP C OD2 
8325  N  N   . LEU C 285 ? 0.3985 0.5129 0.7234 -0.0129 0.0455  0.1143  286 LEU C N   
8326  C  CA  . LEU C 285 ? 0.4532 0.5626 0.7715 -0.0133 0.0481  0.1116  286 LEU C CA  
8327  C  C   . LEU C 285 ? 0.3542 0.4636 0.6627 -0.0172 0.0426  0.1169  286 LEU C C   
8328  O  O   . LEU C 285 ? 0.3569 0.4627 0.6627 -0.0182 0.0438  0.1167  286 LEU C O   
8329  C  CB  . LEU C 285 ? 0.4398 0.5476 0.7457 -0.0136 0.0532  0.1031  286 LEU C CB  
8330  C  CG  . LEU C 285 ? 0.5005 0.6067 0.8105 -0.0120 0.0597  0.0969  286 LEU C CG  
8331  C  CD1 . LEU C 285 ? 0.5123 0.6184 0.8077 -0.0138 0.0609  0.0916  286 LEU C CD1 
8332  C  CD2 . LEU C 285 ? 0.4899 0.5903 0.8074 -0.0111 0.0650  0.0936  286 LEU C CD2 
8333  N  N   . ASP C 286 ? 0.3561 0.4692 0.6585 -0.0203 0.0370  0.1213  287 ASP C N   
8334  C  CA  . ASP C 286 ? 0.3933 0.5065 0.6814 -0.0258 0.0332  0.1245  287 ASP C CA  
8335  C  C   . ASP C 286 ? 0.4079 0.5178 0.6982 -0.0282 0.0305  0.1309  287 ASP C C   
8336  O  O   . ASP C 286 ? 0.4758 0.5837 0.7558 -0.0309 0.0329  0.1287  287 ASP C O   
8337  C  CB  . ASP C 286 ? 0.3664 0.4832 0.6492 -0.0300 0.0269  0.1291  287 ASP C CB  
8338  C  CG  . ASP C 286 ? 0.3752 0.4914 0.6393 -0.0372 0.0249  0.1301  287 ASP C CG  
8339  O  OD1 . ASP C 286 ? 0.5306 0.6455 0.7847 -0.0377 0.0306  0.1232  287 ASP C OD1 
8340  O  OD2 . ASP C 286 ? 0.3850 0.5020 0.6448 -0.0431 0.0177  0.1378  287 ASP C OD2 
8341  N  N   . ALA C 287 ? 0.3733 0.4828 0.6787 -0.0273 0.0254  0.1391  288 ALA C N   
8342  C  CA  . ALA C 287 ? 0.5414 0.6471 0.8503 -0.0301 0.0210  0.1475  288 ALA C CA  
8343  C  C   . ALA C 287 ? 0.3813 0.4818 0.6908 -0.0283 0.0273  0.1427  288 ALA C C   
8344  O  O   . ALA C 287 ? 0.4513 0.5497 0.7489 -0.0331 0.0271  0.1441  288 ALA C O   
8345  C  CB  . ALA C 287 ? 0.3859 0.4918 0.7174 -0.0277 0.0148  0.1568  288 ALA C CB  
8346  N  N   . GLU C 288 ? 0.3754 0.4736 0.6980 -0.0223 0.0333  0.1367  289 GLU C N   
8347  C  CA  . GLU C 288 ? 0.4959 0.5883 0.8201 -0.0213 0.0388  0.1321  289 GLU C CA  
8348  C  C   . GLU C 288 ? 0.4589 0.5526 0.7660 -0.0233 0.0434  0.1240  289 GLU C C   
8349  O  O   . GLU C 288 ? 0.4539 0.5442 0.7577 -0.0252 0.0457  0.1223  289 GLU C O   
8350  C  CB  . GLU C 288 ? 0.3740 0.4628 0.7154 -0.0157 0.0447  0.1268  289 GLU C CB  
8351  C  CG  . GLU C 288 ? 0.4754 0.5629 0.8400 -0.0127 0.0412  0.1345  289 GLU C CG  
8352  C  CD  . GLU C 288 ? 0.5525 0.6357 0.9228 -0.0154 0.0345  0.1452  289 GLU C CD  
8353  O  OE1 . GLU C 288 ? 0.5531 0.6312 0.9155 -0.0179 0.0366  0.1436  289 GLU C OE1 
8354  O  OE2 . GLU C 288 ? 0.5726 0.6575 0.9557 -0.0156 0.0265  0.1559  289 GLU C OE2 
8355  N  N   . TRP C 289 ? 0.4171 0.5157 0.7152 -0.0231 0.0443  0.1194  290 TRP C N   
8356  C  CA  . TRP C 289 ? 0.4525 0.5531 0.7374 -0.0249 0.0475  0.1131  290 TRP C CA  
8357  C  C   . TRP C 289 ? 0.4224 0.5238 0.6971 -0.0305 0.0457  0.1167  290 TRP C C   
8358  O  O   . TRP C 289 ? 0.4152 0.5158 0.6865 -0.0323 0.0488  0.1140  290 TRP C O   
8359  C  CB  . TRP C 289 ? 0.3571 0.4618 0.6364 -0.0237 0.0479  0.1089  290 TRP C CB  
8360  C  CG  . TRP C 289 ? 0.3753 0.4822 0.6451 -0.0248 0.0505  0.1031  290 TRP C CG  
8361  C  CD1 . TRP C 289 ? 0.3559 0.4658 0.6166 -0.0278 0.0502  0.1025  290 TRP C CD1 
8362  C  CD2 . TRP C 289 ? 0.3851 0.4915 0.6552 -0.0233 0.0537  0.0971  290 TRP C CD2 
8363  N  NE1 . TRP C 289 ? 0.3524 0.4639 0.6110 -0.0271 0.0534  0.0966  290 TRP C NE1 
8364  C  CE2 . TRP C 289 ? 0.3489 0.4586 0.6130 -0.0246 0.0545  0.0940  290 TRP C CE2 
8365  C  CE3 . TRP C 289 ? 0.3500 0.4529 0.6246 -0.0218 0.0560  0.0940  290 TRP C CE3 
8366  C  CZ2 . TRP C 289 ? 0.3855 0.4961 0.6504 -0.0239 0.0559  0.0895  290 TRP C CZ2 
8367  C  CZ3 . TRP C 289 ? 0.3667 0.4699 0.6381 -0.0223 0.0572  0.0892  290 TRP C CZ3 
8368  C  CH2 . TRP C 289 ? 0.3789 0.4865 0.6467 -0.0232 0.0564  0.0878  290 TRP C CH2 
8369  N  N   . ARG C 290 ? 0.4216 0.5247 0.6911 -0.0341 0.0410  0.1228  291 ARG C N   
8370  C  CA  . ARG C 290 ? 0.3844 0.4877 0.6416 -0.0413 0.0396  0.1266  291 ARG C CA  
8371  C  C   . ARG C 290 ? 0.4855 0.5843 0.7467 -0.0436 0.0389  0.1318  291 ARG C C   
8372  O  O   . ARG C 290 ? 0.5214 0.6201 0.7739 -0.0483 0.0418  0.1308  291 ARG C O   
8373  C  CB  . ARG C 290 ? 0.3926 0.4973 0.6430 -0.0461 0.0331  0.1336  291 ARG C CB  
8374  C  CG  . ARG C 290 ? 0.3888 0.4972 0.6323 -0.0458 0.0340  0.1282  291 ARG C CG  
8375  C  CD  . ARG C 290 ? 0.4279 0.5372 0.6634 -0.0521 0.0268  0.1354  291 ARG C CD  
8376  N  NE  . ARG C 290 ? 0.4453 0.5572 0.6731 -0.0528 0.0280  0.1296  291 ARG C NE  
8377  C  CZ  . ARG C 290 ? 0.4938 0.6057 0.7057 -0.0584 0.0321  0.1240  291 ARG C CZ  
8378  N  NH1 . ARG C 290 ? 0.4980 0.6085 0.6994 -0.0642 0.0358  0.1233  291 ARG C NH1 
8379  N  NH2 . ARG C 290 ? 0.4852 0.5982 0.6922 -0.0586 0.0332  0.1187  291 ARG C NH2 
8380  N  N   . ASN C 291 ? 0.4450 0.5400 0.7207 -0.0403 0.0355  0.1372  292 ASN C N   
8381  C  CA  . ASN C 291 ? 0.4868 0.5759 0.7689 -0.0418 0.0346  0.1423  292 ASN C CA  
8382  C  C   . ASN C 291 ? 0.4515 0.5390 0.7329 -0.0408 0.0416  0.1342  292 ASN C C   
8383  O  O   . ASN C 291 ? 0.4015 0.4869 0.6783 -0.0456 0.0424  0.1364  292 ASN C O   
8384  C  CB  . ASN C 291 ? 0.5066 0.5912 0.8090 -0.0368 0.0313  0.1476  292 ASN C CB  
8385  C  CG  . ASN C 291 ? 0.5525 0.6382 0.8590 -0.0394 0.0219  0.1594  292 ASN C CG  
8386  O  OD1 . ASN C 291 ? 0.5935 0.6813 0.8845 -0.0468 0.0172  0.1649  292 ASN C OD1 
8387  N  ND2 . ASN C 291 ? 0.5197 0.6037 0.8475 -0.0340 0.0191  0.1633  292 ASN C ND2 
8388  N  N   . LEU C 292 ? 0.3849 0.4738 0.6704 -0.0356 0.0460  0.1254  293 LEU C N   
8389  C  CA  . LEU C 292 ? 0.4583 0.5462 0.7432 -0.0353 0.0512  0.1180  293 LEU C CA  
8390  C  C   . LEU C 292 ? 0.4509 0.5439 0.7244 -0.0398 0.0534  0.1155  293 LEU C C   
8391  O  O   . LEU C 292 ? 0.5027 0.5946 0.7755 -0.0434 0.0553  0.1155  293 LEU C O   
8392  C  CB  . LEU C 292 ? 0.3737 0.4622 0.6619 -0.0304 0.0543  0.1100  293 LEU C CB  
8393  C  CG  . LEU C 292 ? 0.4708 0.5585 0.7576 -0.0313 0.0580  0.1031  293 LEU C CG  
8394  C  CD1 . LEU C 292 ? 0.3794 0.4594 0.6732 -0.0327 0.0592  0.1042  293 LEU C CD1 
8395  C  CD2 . LEU C 292 ? 0.3669 0.4554 0.6530 -0.0285 0.0600  0.0962  293 LEU C CD2 
8396  N  N   . LEU C 293 ? 0.4360 0.5347 0.7022 -0.0397 0.0537  0.1130  294 LEU C N   
8397  C  CA  . LEU C 293 ? 0.4491 0.5529 0.7077 -0.0433 0.0574  0.1090  294 LEU C CA  
8398  C  C   . LEU C 293 ? 0.4801 0.5833 0.7312 -0.0507 0.0578  0.1142  294 LEU C C   
8399  O  O   . LEU C 293 ? 0.4694 0.5751 0.7191 -0.0543 0.0623  0.1114  294 LEU C O   
8400  C  CB  . LEU C 293 ? 0.4555 0.5638 0.7087 -0.0420 0.0581  0.1053  294 LEU C CB  
8401  C  CG  . LEU C 293 ? 0.4379 0.5486 0.6964 -0.0367 0.0594  0.0986  294 LEU C CG  
8402  C  CD1 . LEU C 293 ? 0.4299 0.5368 0.6950 -0.0323 0.0573  0.0987  294 LEU C CD1 
8403  C  CD2 . LEU C 293 ? 0.4524 0.5664 0.7060 -0.0361 0.0600  0.0956  294 LEU C CD2 
8404  N  N   . ASP C 294 ? 0.4498 0.5498 0.6967 -0.0538 0.0529  0.1224  295 ASP C N   
8405  C  CA  . ASP C 294 ? 0.5692 0.6673 0.8066 -0.0623 0.0520  0.1291  295 ASP C CA  
8406  C  C   . ASP C 294 ? 0.5224 0.6161 0.7668 -0.0637 0.0526  0.1320  295 ASP C C   
8407  O  O   . ASP C 294 ? 0.4632 0.5573 0.7006 -0.0706 0.0557  0.1331  295 ASP C O   
8408  C  CB  . ASP C 294 ? 0.6838 0.7791 0.9162 -0.0658 0.0442  0.1390  295 ASP C CB  
8409  C  CG  . ASP C 294 ? 0.8010 0.9003 1.0202 -0.0692 0.0442  0.1368  295 ASP C CG  
8410  O  OD1 . ASP C 294 ? 0.8552 0.9584 1.0663 -0.0715 0.0514  0.1287  295 ASP C OD1 
8411  O  OD2 . ASP C 294 ? 0.8375 0.9359 1.0559 -0.0697 0.0370  0.1431  295 ASP C OD2 
8412  N  N   . SER C 295 ? 0.4831 0.5720 0.7410 -0.0577 0.0504  0.1326  296 SER C N   
8413  C  CA  . SER C 295 ? 0.4898 0.5731 0.7552 -0.0587 0.0512  0.1342  296 SER C CA  
8414  C  C   . SER C 295 ? 0.4647 0.5522 0.7298 -0.0598 0.0575  0.1259  296 SER C C   
8415  O  O   . SER C 295 ? 0.5039 0.5894 0.7690 -0.0648 0.0592  0.1277  296 SER C O   
8416  C  CB  . SER C 295 ? 0.4587 0.5354 0.7392 -0.0521 0.0492  0.1344  296 SER C CB  
8417  O  OG  . SER C 295 ? 0.5002 0.5796 0.7843 -0.0463 0.0527  0.1248  296 SER C OG  
8418  N  N   . MET C 296 ? 0.4264 0.5197 0.6922 -0.0555 0.0602  0.1177  297 MET C N   
8419  C  CA  . MET C 296 ? 0.4616 0.5601 0.7299 -0.0562 0.0647  0.1107  297 MET C CA  
8420  C  C   . MET C 296 ? 0.4632 0.5678 0.7247 -0.0626 0.0692  0.1103  297 MET C C   
8421  O  O   . MET C 296 ? 0.4995 0.6056 0.7637 -0.0670 0.0723  0.1098  297 MET C O   
8422  C  CB  . MET C 296 ? 0.4486 0.5513 0.7200 -0.0504 0.0650  0.1036  297 MET C CB  
8423  C  CG  . MET C 296 ? 0.3795 0.4764 0.6563 -0.0454 0.0625  0.1023  297 MET C CG  
8424  S  SD  . MET C 296 ? 0.6879 0.7893 0.9654 -0.0405 0.0623  0.0953  297 MET C SD  
8425  C  CE  . MET C 296 ? 0.5289 0.6378 0.8097 -0.0434 0.0643  0.0912  297 MET C CE  
8426  N  N   . VAL C 297 ? 0.4010 0.5090 0.6538 -0.0637 0.0702  0.1101  298 VAL C N   
8427  C  CA  . VAL C 297 ? 0.4095 0.5222 0.6537 -0.0708 0.0760  0.1089  298 VAL C CA  
8428  C  C   . VAL C 297 ? 0.5886 0.6971 0.8269 -0.0791 0.0761  0.1160  298 VAL C C   
8429  O  O   . VAL C 297 ? 0.6587 0.7712 0.8957 -0.0852 0.0824  0.1139  298 VAL C O   
8430  C  CB  . VAL C 297 ? 0.4137 0.5275 0.6460 -0.0725 0.0762  0.1086  298 VAL C CB  
8431  C  CG1 . VAL C 297 ? 0.4283 0.5443 0.6476 -0.0825 0.0827  0.1081  298 VAL C CG1 
8432  C  CG2 . VAL C 297 ? 0.4814 0.5996 0.7197 -0.0655 0.0777  0.1008  298 VAL C CG2 
8433  N  N   . LEU C 298 ? 0.5569 0.6576 0.7937 -0.0794 0.0691  0.1247  299 LEU C N   
8434  C  CA  . LEU C 298 ? 0.5423 0.6373 0.7747 -0.0871 0.0672  0.1334  299 LEU C CA  
8435  C  C   . LEU C 298 ? 0.5559 0.6499 0.7986 -0.0875 0.0701  0.1314  299 LEU C C   
8436  O  O   . LEU C 298 ? 0.5064 0.6008 0.7445 -0.0957 0.0737  0.1338  299 LEU C O   
8437  C  CB  . LEU C 298 ? 0.6158 0.7023 0.8498 -0.0856 0.0580  0.1437  299 LEU C CB  
8438  C  CG  . LEU C 298 ? 0.7030 0.7820 0.9326 -0.0939 0.0537  0.1554  299 LEU C CG  
8439  C  CD1 . LEU C 298 ? 0.7372 0.8187 0.9463 -0.1058 0.0558  0.1590  299 LEU C CD1 
8440  C  CD2 . LEU C 298 ? 0.7368 0.8080 0.9747 -0.0902 0.0438  0.1653  299 LEU C CD2 
8441  N  N   . ILE C 299 ? 0.4857 0.5783 0.7413 -0.0798 0.0687  0.1268  300 ILE C N   
8442  C  CA  . ILE C 299 ? 0.4903 0.5806 0.7552 -0.0809 0.0701  0.1252  300 ILE C CA  
8443  C  C   . ILE C 299 ? 0.5139 0.6141 0.7825 -0.0830 0.0764  0.1176  300 ILE C C   
8444  O  O   . ILE C 299 ? 0.4501 0.5500 0.7255 -0.0861 0.0779  0.1167  300 ILE C O   
8445  C  CB  . ILE C 299 ? 0.5364 0.6206 0.8121 -0.0737 0.0667  0.1224  300 ILE C CB  
8446  C  CG1 . ILE C 299 ? 0.5874 0.6636 0.8698 -0.0770 0.0663  0.1246  300 ILE C CG1 
8447  C  CG2 . ILE C 299 ? 0.4999 0.5910 0.7798 -0.0685 0.0685  0.1130  300 ILE C CG2 
8448  C  CD1 . ILE C 299 ? 0.6463 0.7146 0.9378 -0.0715 0.0645  0.1207  300 ILE C CD1 
8449  N  N   . THR C 300 ? 0.5111 0.6200 0.7773 -0.0815 0.0802  0.1122  301 THR C N   
8450  C  CA  . THR C 300 ? 0.4980 0.6171 0.7715 -0.0836 0.0867  0.1057  301 THR C CA  
8451  C  C   . THR C 300 ? 0.4893 0.6100 0.7590 -0.0935 0.0923  0.1086  301 THR C C   
8452  O  O   . THR C 300 ? 0.4785 0.6059 0.7585 -0.0962 0.0968  0.1049  301 THR C O   
8453  C  CB  . THR C 300 ? 0.4104 0.5376 0.6833 -0.0807 0.0909  0.0995  301 THR C CB  
8454  O  OG1 . THR C 300 ? 0.5757 0.7013 0.8333 -0.0858 0.0936  0.1023  301 THR C OG1 
8455  C  CG2 . THR C 300 ? 0.3984 0.5246 0.6752 -0.0717 0.0856  0.0968  301 THR C CG2 
8456  N  N   . ASP C 301 ? 0.4420 0.5566 0.6973 -0.0996 0.0916  0.1158  302 ASP C N   
8457  C  CA  . ASP C 301 ? 0.4575 0.5723 0.7053 -0.1108 0.0968  0.1196  302 ASP C CA  
8458  C  C   . ASP C 301 ? 0.5193 0.6302 0.7761 -0.1137 0.0952  0.1230  302 ASP C C   
8459  O  O   . ASP C 301 ? 0.5141 0.6290 0.7716 -0.1218 0.1015  0.1228  302 ASP C O   
8460  C  CB  . ASP C 301 ? 0.5711 0.6786 0.7998 -0.1176 0.0936  0.1287  302 ASP C CB  
8461  C  CG  . ASP C 301 ? 0.5864 0.6984 0.8025 -0.1191 0.0977  0.1247  302 ASP C CG  
8462  O  OD1 . ASP C 301 ? 0.6092 0.7302 0.8276 -0.1209 0.1076  0.1158  302 ASP C OD1 
8463  O  OD2 . ASP C 301 ? 0.6263 0.7327 0.8315 -0.1188 0.0910  0.1304  302 ASP C OD2 
8464  N  N   . LYS C 302 ? 0.5285 0.6311 0.7921 -0.1077 0.0876  0.1255  303 LYS C N   
8465  C  CA  . LYS C 302 ? 0.5007 0.5969 0.7718 -0.1108 0.0856  0.1286  303 LYS C CA  
8466  C  C   . LYS C 302 ? 0.5545 0.6585 0.8397 -0.1101 0.0888  0.1209  303 LYS C C   
8467  O  O   . LYS C 302 ? 0.5830 0.6822 0.8750 -0.1130 0.0872  0.1221  303 LYS C O   
8468  C  CB  . LYS C 302 ? 0.4848 0.5684 0.7594 -0.1049 0.0777  0.1326  303 LYS C CB  
8469  C  CG  . LYS C 302 ? 0.4792 0.5541 0.7443 -0.1068 0.0726  0.1430  303 LYS C CG  
8470  C  CD  . LYS C 302 ? 0.5178 0.5894 0.7743 -0.1183 0.0738  0.1517  303 LYS C CD  
8471  C  CE  . LYS C 302 ? 0.5261 0.5890 0.7731 -0.1214 0.0667  0.1640  303 LYS C CE  
8472  N  NZ  . LYS C 302 ? 0.5576 0.6163 0.7940 -0.1341 0.0670  0.1738  303 LYS C NZ  
8473  N  N   . PHE C 303 ? 0.5452 0.6611 0.8359 -0.1067 0.0927  0.1133  304 PHE C N   
8474  C  CA  . PHE C 303 ? 0.5303 0.6554 0.8365 -0.1066 0.0946  0.1072  304 PHE C CA  
8475  C  C   . PHE C 303 ? 0.4443 0.5750 0.7540 -0.1165 0.1015  0.1084  304 PHE C C   
8476  O  O   . PHE C 303 ? 0.4679 0.6028 0.7904 -0.1191 0.1015  0.1065  304 PHE C O   
8477  C  CB  . PHE C 303 ? 0.4679 0.6044 0.7818 -0.1004 0.0966  0.1000  304 PHE C CB  
8478  C  CG  . PHE C 303 ? 0.4394 0.5715 0.7507 -0.0915 0.0902  0.0985  304 PHE C CG  
8479  C  CD1 . PHE C 303 ? 0.4139 0.5339 0.7201 -0.0890 0.0838  0.1015  304 PHE C CD1 
8480  C  CD2 . PHE C 303 ? 0.4035 0.5431 0.7186 -0.0858 0.0912  0.0936  304 PHE C CD2 
8481  C  CE1 . PHE C 303 ? 0.4063 0.5227 0.7102 -0.0815 0.0792  0.0996  304 PHE C CE1 
8482  C  CE2 . PHE C 303 ? 0.3957 0.5313 0.7078 -0.0784 0.0855  0.0925  304 PHE C CE2 
8483  C  CZ  . PHE C 303 ? 0.4116 0.5359 0.7176 -0.0765 0.0798  0.0953  304 PHE C CZ  
8484  N  N   . TRP C 304 ? 0.5117 0.6423 0.8089 -0.1229 0.1073  0.1119  305 TRP C N   
8485  C  CA  . TRP C 304 ? 0.4676 0.6033 0.7653 -0.1337 0.1154  0.1131  305 TRP C CA  
8486  C  C   . TRP C 304 ? 0.5137 0.6372 0.7953 -0.1423 0.1135  0.1233  305 TRP C C   
8487  O  O   . TRP C 304 ? 0.4884 0.6005 0.7593 -0.1395 0.1062  0.1295  305 TRP C O   
8488  C  CB  . TRP C 304 ? 0.4695 0.6170 0.7663 -0.1364 0.1264  0.1071  305 TRP C CB  
8489  C  CG  . TRP C 304 ? 0.5610 0.7206 0.8767 -0.1283 0.1284  0.0980  305 TRP C CG  
8490  C  CD1 . TRP C 304 ? 0.4486 0.6207 0.7864 -0.1290 0.1330  0.0928  305 TRP C CD1 
8491  C  CD2 . TRP C 304 ? 0.4422 0.6026 0.7582 -0.1185 0.1251  0.0940  305 TRP C CD2 
8492  N  NE1 . TRP C 304 ? 0.4637 0.6441 0.8162 -0.1201 0.1320  0.0864  305 TRP C NE1 
8493  C  CE2 . TRP C 304 ? 0.4309 0.6039 0.7695 -0.1137 0.1275  0.0869  305 TRP C CE2 
8494  C  CE3 . TRP C 304 ? 0.4409 0.5928 0.7414 -0.1137 0.1200  0.0962  305 TRP C CE3 
8495  C  CZ2 . TRP C 304 ? 0.4751 0.6513 0.8200 -0.1044 0.1248  0.0823  305 TRP C CZ2 
8496  C  CZ3 . TRP C 304 ? 0.5082 0.6639 0.8146 -0.1046 0.1181  0.0909  305 TRP C CZ3 
8497  C  CH2 . TRP C 304 ? 0.4919 0.6591 0.8196 -0.1001 0.1205  0.0842  305 TRP C CH2 
8498  N  N   . GLY C 305 ? 0.5852 0.7114 0.8668 -0.1531 0.1200  0.1254  306 GLY C N   
8499  C  CA  . GLY C 305 ? 0.6737 0.7894 0.9390 -0.1635 0.1190  0.1359  306 GLY C CA  
8500  C  C   . GLY C 305 ? 0.7448 0.8651 0.9927 -0.1726 0.1281  0.1361  306 GLY C C   
8501  O  O   . GLY C 305 ? 0.7351 0.8658 0.9848 -0.1695 0.1352  0.1273  306 GLY C O   
8502  N  N   . THR C 306 ? 0.8776 0.9895 1.1081 -0.1846 0.1279  0.1461  307 THR C N   
8503  C  CA  . THR C 306 ? 1.0047 1.1194 1.2139 -0.1960 0.1366  0.1468  307 THR C CA  
8504  C  C   . THR C 306 ? 1.0927 1.2166 1.3036 -0.2084 0.1505  0.1429  307 THR C C   
8505  O  O   . THR C 306 ? 1.1262 1.2532 1.3194 -0.2198 0.1606  0.1416  307 THR C O   
8506  C  CB  . THR C 306 ? 1.0871 1.1873 1.2725 -0.2040 0.1277  0.1612  307 THR C CB  
8507  O  OG1 . THR C 306 ? 1.0973 1.1874 1.2891 -0.1926 0.1135  0.1670  307 THR C OG1 
8508  C  CG2 . THR C 306 ? 1.1215 1.2237 1.2832 -0.2111 0.1328  0.1599  307 THR C CG2 
8509  N  N   . SER C 307 ? 1.0949 1.2234 1.3271 -0.2070 0.1516  0.1406  308 SER C N   
8510  C  CA  . SER C 307 ? 1.1085 1.2457 1.3452 -0.2192 0.1641  0.1382  308 SER C CA  
8511  C  C   . SER C 307 ? 1.0848 1.2406 1.3403 -0.2159 0.1776  0.1238  308 SER C C   
8512  O  O   . SER C 307 ? 1.1066 1.2724 1.3716 -0.2247 0.1896  0.1197  308 SER C O   
8513  C  CB  . SER C 307 ? 1.1084 1.2413 1.3596 -0.2210 0.1585  0.1435  308 SER C CB  
8514  O  OG  . SER C 307 ? 1.1211 1.2366 1.3557 -0.2270 0.1487  0.1574  308 SER C OG  
8515  N  N   . GLY C 308 ? 1.0151 1.1753 1.2778 -0.2033 0.1756  0.1164  309 GLY C N   
8516  C  CA  . GLY C 308 ? 0.9678 1.1443 1.2495 -0.1992 0.1876  0.1033  309 GLY C CA  
8517  C  C   . GLY C 308 ? 0.8974 1.0855 1.2129 -0.1924 0.1865  0.0984  309 GLY C C   
8518  O  O   . GLY C 308 ? 0.8942 1.0975 1.2305 -0.1932 0.1983  0.0895  309 GLY C O   
8519  N  N   . VAL C 309 ? 0.8504 1.0312 1.1723 -0.1864 0.1724  0.1041  310 VAL C N   
8520  C  CA  . VAL C 309 ? 0.8053 0.9955 1.1565 -0.1809 0.1687  0.1005  310 VAL C CA  
8521  C  C   . VAL C 309 ? 0.7591 0.9521 1.1219 -0.1663 0.1607  0.0955  310 VAL C C   
8522  O  O   . VAL C 309 ? 0.7346 0.9213 1.0826 -0.1605 0.1582  0.0952  310 VAL C O   
8523  C  CB  . VAL C 309 ? 0.7143 0.8939 1.0647 -0.1846 0.1587  0.1087  310 VAL C CB  
8524  C  CG1 . VAL C 309 ? 0.7193 0.9106 1.0980 -0.1855 0.1585  0.1054  310 VAL C CG1 
8525  C  CG2 . VAL C 309 ? 0.7429 0.9128 1.0721 -0.1981 0.1628  0.1171  310 VAL C CG2 
8526  N  N   . GLU C 310 ? 0.7065 0.9086 1.0951 -0.1613 0.1561  0.0923  311 GLU C N   
8527  C  CA  . GLU C 310 ? 0.6505 0.8536 1.0488 -0.1489 0.1461  0.0894  311 GLU C CA  
8528  C  C   . GLU C 310 ? 0.6526 0.8391 1.0353 -0.1454 0.1328  0.0954  311 GLU C C   
8529  O  O   . GLU C 310 ? 0.6355 0.8120 1.0085 -0.1522 0.1304  0.1013  311 GLU C O   
8530  C  CB  . GLU C 310 ? 0.6438 0.8621 1.0744 -0.1465 0.1442  0.0854  311 GLU C CB  
8531  N  N   . SER C 311 ? 0.5900 0.7731 0.9711 -0.1352 0.1248  0.0937  312 SER C N   
8532  C  CA  . SER C 311 ? 0.5572 0.7254 0.9266 -0.1315 0.1134  0.0977  312 SER C CA  
8533  C  C   . SER C 311 ? 0.5044 0.6718 0.8855 -0.1352 0.1071  0.0985  312 SER C C   
8534  O  O   . SER C 311 ? 0.4375 0.6179 0.8391 -0.1367 0.1076  0.0953  312 SER C O   
8535  C  CB  . SER C 311 ? 0.4290 0.5956 0.7964 -0.1207 0.1071  0.0947  312 SER C CB  
8536  O  OG  . SER C 311 ? 0.4286 0.5816 0.7868 -0.1177 0.0977  0.0973  312 SER C OG  
8537  N  N   . VAL C 312 ? 0.4745 0.6263 0.8438 -0.1370 0.1011  0.1027  313 VAL C N   
8538  C  CA  . VAL C 312 ? 0.5046 0.6527 0.8817 -0.1421 0.0958  0.1032  313 VAL C CA  
8539  C  C   . VAL C 312 ? 0.4839 0.6342 0.8692 -0.1369 0.0870  0.0987  313 VAL C C   
8540  O  O   . VAL C 312 ? 0.4923 0.6452 0.8883 -0.1419 0.0826  0.0976  313 VAL C O   
8541  C  CB  . VAL C 312 ? 0.5173 0.6462 0.8801 -0.1456 0.0930  0.1086  313 VAL C CB  
8542  C  CG1 . VAL C 312 ? 0.5172 0.6333 0.8690 -0.1370 0.0868  0.1081  313 VAL C CG1 
8543  C  CG2 . VAL C 312 ? 0.4868 0.6118 0.8578 -0.1534 0.0899  0.1090  313 VAL C CG2 
8544  N  N   . ILE C 313 ? 0.4843 0.6336 0.8638 -0.1280 0.0842  0.0965  314 ILE C N   
8545  C  CA  . ILE C 313 ? 0.4610 0.6100 0.8434 -0.1237 0.0754  0.0930  314 ILE C CA  
8546  C  C   . ILE C 313 ? 0.4691 0.6341 0.8725 -0.1262 0.0722  0.0910  314 ILE C C   
8547  O  O   . ILE C 313 ? 0.4741 0.6381 0.8804 -0.1277 0.0634  0.0896  314 ILE C O   
8548  C  CB  . ILE C 313 ? 0.4372 0.5843 0.8106 -0.1141 0.0742  0.0915  314 ILE C CB  
8549  C  CG1 . ILE C 313 ? 0.4346 0.5677 0.7904 -0.1118 0.0770  0.0945  314 ILE C CG1 
8550  C  CG2 . ILE C 313 ? 0.4165 0.5607 0.7887 -0.1111 0.0652  0.0886  314 ILE C CG2 
8551  C  CD1 . ILE C 313 ? 0.4763 0.6091 0.8241 -0.1034 0.0773  0.0937  314 ILE C CD1 
8552  N  N   . GLY C 314 ? 0.4554 0.6352 0.8741 -0.1273 0.0794  0.0909  315 GLY C N   
8553  C  CA  . GLY C 314 ? 0.4544 0.6511 0.8984 -0.1293 0.0768  0.0897  315 GLY C CA  
8554  C  C   . GLY C 314 ? 0.4227 0.6285 0.8819 -0.1382 0.0830  0.0909  315 GLY C C   
8555  O  O   . GLY C 314 ? 0.4187 0.6414 0.9034 -0.1397 0.0835  0.0900  315 GLY C O   
8556  N  N   . SER C 315 ? 0.4332 0.6282 0.8785 -0.1445 0.0876  0.0933  316 SER C N   
8557  C  CA  . SER C 315 ? 0.5081 0.7107 0.9652 -0.1540 0.0948  0.0948  316 SER C CA  
8558  C  C   . SER C 315 ? 0.5570 0.7457 1.0037 -0.1626 0.0916  0.0981  316 SER C C   
8559  O  O   . SER C 315 ? 0.5513 0.7408 0.9993 -0.1708 0.0988  0.1006  316 SER C O   
8560  C  CB  . SER C 315 ? 0.4927 0.6993 0.9452 -0.1548 0.1086  0.0947  316 SER C CB  
8561  O  OG  . SER C 315 ? 0.4893 0.6791 0.9148 -0.1531 0.1096  0.0976  316 SER C OG  
8562  N  N   . VAL C 316 ? 0.5690 0.7447 1.0055 -0.1613 0.0814  0.0976  317 VAL C N   
8563  C  CA  . VAL C 316 ? 0.4689 0.6295 0.8966 -0.1690 0.0781  0.0995  317 VAL C CA  
8564  C  C   . VAL C 316 ? 0.6165 0.7871 1.0626 -0.1797 0.0782  0.1003  317 VAL C C   
8565  O  O   . VAL C 316 ? 0.6798 0.8420 1.1220 -0.1880 0.0811  0.1033  317 VAL C O   
8566  C  CB  . VAL C 316 ? 0.4706 0.6175 0.8871 -0.1663 0.0679  0.0965  317 VAL C CB  
8567  C  CG1 . VAL C 316 ? 0.4858 0.6181 0.8973 -0.1754 0.0647  0.0967  317 VAL C CG1 
8568  C  CG2 . VAL C 316 ? 0.4666 0.6016 0.8651 -0.1568 0.0687  0.0961  317 VAL C CG2 
8569  N  N   . HIS C 317 ? 0.6148 0.8037 1.0825 -0.1795 0.0745  0.0984  318 HIS C N   
8570  C  CA  . HIS C 317 ? 0.5637 0.7651 1.0532 -0.1893 0.0732  0.0992  318 HIS C CA  
8571  C  C   . HIS C 317 ? 0.6814 0.8894 1.1781 -0.1958 0.0860  0.1017  318 HIS C C   
8572  O  O   . HIS C 317 ? 0.8335 1.0431 1.3389 -0.2062 0.0862  0.1035  318 HIS C O   
8573  C  CB  . HIS C 317 ? 0.5230 0.7450 1.0383 -0.1865 0.0672  0.0979  318 HIS C CB  
8574  C  CG  . HIS C 317 ? 0.5469 0.7819 1.0724 -0.1772 0.0750  0.0965  318 HIS C CG  
8575  N  ND1 . HIS C 317 ? 0.5859 0.8175 1.1021 -0.1667 0.0713  0.0948  318 HIS C ND1 
8576  C  CD2 . HIS C 317 ? 0.5684 0.8193 1.1128 -0.1774 0.0871  0.0957  318 HIS C CD2 
8577  C  CE1 . HIS C 317 ? 0.5710 0.8151 1.1000 -0.1607 0.0802  0.0932  318 HIS C CE1 
8578  N  NE2 . HIS C 317 ? 0.5628 0.8187 1.1089 -0.1670 0.0904  0.0932  318 HIS C NE2 
8579  N  N   . THR C 318 ? 0.6453 0.8565 1.1368 -0.1908 0.0966  0.1016  319 THR C N   
8580  C  CA  . THR C 318 ? 0.6103 0.8264 1.1036 -0.1981 0.1099  0.1036  319 THR C CA  
8581  C  C   . THR C 318 ? 0.5934 0.7902 1.0667 -0.2062 0.1101  0.1087  319 THR C C   
8582  O  O   . THR C 318 ? 0.6046 0.8042 1.0851 -0.2170 0.1148  0.1113  319 THR C O   
8583  C  CB  . THR C 318 ? 0.6157 0.8359 1.1014 -0.1922 0.1210  0.1021  319 THR C CB  
8584  O  OG1 . THR C 318 ? 0.6288 0.8297 1.0856 -0.1872 0.1184  0.1044  319 THR C OG1 
8585  C  CG2 . THR C 318 ? 0.6225 0.8590 1.1279 -0.1829 0.1204  0.0970  319 THR C CG2 
8586  N  N   . TRP C 319 ? 0.5662 0.7433 1.0163 -0.2008 0.1048  0.1102  320 TRP C N   
8587  C  CA  . TRP C 319 ? 0.5473 0.7040 0.9801 -0.2069 0.1040  0.1155  320 TRP C CA  
8588  C  C   . TRP C 319 ? 0.5619 0.7126 1.0022 -0.2148 0.0968  0.1153  320 TRP C C   
8589  O  O   . TRP C 319 ? 0.6170 0.7596 1.0550 -0.2246 0.0994  0.1198  320 TRP C O   
8590  C  CB  . TRP C 319 ? 0.5164 0.6548 0.9278 -0.1981 0.0995  0.1168  320 TRP C CB  
8591  C  CG  . TRP C 319 ? 0.5520 0.6936 0.9527 -0.1925 0.1062  0.1182  320 TRP C CG  
8592  C  CD1 . TRP C 319 ? 0.5509 0.6956 0.9475 -0.1816 0.1046  0.1147  320 TRP C CD1 
8593  C  CD2 . TRP C 319 ? 0.5699 0.7120 0.9616 -0.1991 0.1157  0.1234  320 TRP C CD2 
8594  N  NE1 . TRP C 319 ? 0.5543 0.7010 0.9400 -0.1808 0.1124  0.1170  320 TRP C NE1 
8595  C  CE2 . TRP C 319 ? 0.5793 0.7245 0.9609 -0.1918 0.1192  0.1224  320 TRP C CE2 
8596  C  CE3 . TRP C 319 ? 0.5618 0.7015 0.9516 -0.2114 0.1214  0.1292  320 TRP C CE3 
8597  C  CZ2 . TRP C 319 ? 0.5905 0.7361 0.9586 -0.1971 0.1281  0.1264  320 TRP C CZ2 
8598  C  CZ3 . TRP C 319 ? 0.5655 0.7059 0.9417 -0.2168 0.1303  0.1337  320 TRP C CZ3 
8599  C  CH2 . TRP C 319 ? 0.5794 0.7226 0.9442 -0.2099 0.1335  0.1321  320 TRP C CH2 
8600  N  N   . LEU C 320 ? 0.5162 0.6702 0.9646 -0.2116 0.0875  0.1104  321 LEU C N   
8601  C  CA  . LEU C 320 ? 0.5897 0.7387 1.0446 -0.2204 0.0801  0.1092  321 LEU C CA  
8602  C  C   . LEU C 320 ? 0.5303 0.6951 1.0060 -0.2315 0.0845  0.1112  321 LEU C C   
8603  O  O   . LEU C 320 ? 0.6657 0.8217 1.1409 -0.2419 0.0846  0.1138  321 LEU C O   
8604  C  CB  . LEU C 320 ? 0.5634 0.7153 1.0220 -0.2164 0.0690  0.1039  321 LEU C CB  
8605  C  CG  . LEU C 320 ? 0.5697 0.7062 1.0083 -0.2065 0.0650  0.1010  321 LEU C CG  
8606  C  CD1 . LEU C 320 ? 0.5435 0.6817 0.9833 -0.2058 0.0539  0.0961  321 LEU C CD1 
8607  C  CD2 . LEU C 320 ? 0.5671 0.6783 0.9875 -0.2081 0.0665  0.1025  321 LEU C CD2 
8608  N  N   . ALA C 321 ? 0.5186 0.7068 1.0142 -0.2292 0.0887  0.1098  322 ALA C N   
8609  C  CA  . ALA C 321 ? 0.5888 0.7954 1.1087 -0.2388 0.0944  0.1110  322 ALA C CA  
8610  C  C   . ALA C 321 ? 0.6225 0.8233 1.1340 -0.2473 0.1060  0.1157  322 ALA C C   
8611  O  O   . ALA C 321 ? 0.6585 0.8614 1.1799 -0.2590 0.1075  0.1181  322 ALA C O   
8612  C  CB  . ALA C 321 ? 0.5863 0.8181 1.1303 -0.2329 0.0990  0.1082  322 ALA C CB  
8613  N  N   . GLU C 322 ? 0.6037 0.7969 1.0962 -0.2423 0.1137  0.1177  323 GLU C N   
8614  C  CA  . GLU C 322 ? 0.6681 0.8543 1.1487 -0.2513 0.1237  0.1234  323 GLU C CA  
8615  C  C   . GLU C 322 ? 0.7050 0.8682 1.1720 -0.2584 0.1174  0.1285  323 GLU C C   
8616  O  O   . GLU C 322 ? 0.7271 0.8872 1.1937 -0.2703 0.1227  0.1336  323 GLU C O   
8617  C  CB  . GLU C 322 ? 0.7084 0.8897 1.1689 -0.2452 0.1309  0.1250  323 GLU C CB  
8618  C  CG  . GLU C 322 ? 0.7850 0.9604 1.2313 -0.2561 0.1412  0.1318  323 GLU C CG  
8619  C  CD  . GLU C 322 ? 0.8500 1.0247 1.2778 -0.2521 0.1490  0.1328  323 GLU C CD  
8620  O  OE1 . GLU C 322 ? 0.8417 1.0249 1.2729 -0.2411 0.1490  0.1269  323 GLU C OE1 
8621  O  OE2 . GLU C 322 ? 0.8992 1.0644 1.3084 -0.2608 0.1547  0.1398  323 GLU C OE2 
8622  N  N   . ALA C 323 ? 0.6824 0.8292 1.1389 -0.2517 0.1066  0.1267  324 ALA C N   
8623  C  CA  . ALA C 323 ? 0.6856 0.8097 1.1326 -0.2577 0.1006  0.1297  324 ALA C CA  
8624  C  C   . ALA C 323 ? 0.7230 0.8534 1.1876 -0.2696 0.0980  0.1286  324 ALA C C   
8625  O  O   . ALA C 323 ? 0.7592 0.8790 1.2216 -0.2804 0.0999  0.1336  324 ALA C O   
8626  C  CB  . ALA C 323 ? 0.6786 0.7862 1.1141 -0.2482 0.0912  0.1257  324 ALA C CB  
8627  N  N   . ILE C 324 ? 0.7217 0.8694 1.2044 -0.2683 0.0930  0.1228  325 ILE C N   
8628  C  CA  . ILE C 324 ? 0.7158 0.8720 1.2174 -0.2800 0.0891  0.1219  325 ILE C CA  
8629  C  C   . ILE C 324 ? 0.7525 0.9220 1.2676 -0.2908 0.1000  0.1265  325 ILE C C   
8630  O  O   . ILE C 324 ? 0.7792 0.9421 1.2974 -0.3030 0.0998  0.1295  325 ILE C O   
8631  C  CB  . ILE C 324 ? 0.6732 0.8489 1.1945 -0.2768 0.0810  0.1166  325 ILE C CB  
8632  C  CG1 . ILE C 324 ? 0.6705 0.8330 1.1764 -0.2679 0.0705  0.1119  325 ILE C CG1 
8633  C  CG2 . ILE C 324 ? 0.6465 0.8310 1.1878 -0.2900 0.0756  0.1165  325 ILE C CG2 
8634  C  CD1 . ILE C 324 ? 0.6574 0.8365 1.1795 -0.2662 0.0602  0.1081  325 ILE C CD1 
8635  N  N   . ASN C 325 ? 0.7883 0.9761 1.3112 -0.2869 0.1104  0.1265  326 ASN C N   
8636  C  CA  . ASN C 325 ? 0.7786 0.9797 1.3127 -0.2973 0.1234  0.1299  326 ASN C CA  
8637  C  C   . ASN C 325 ? 0.7775 0.9581 1.2905 -0.3066 0.1281  0.1374  326 ASN C C   
8638  O  O   . ASN C 325 ? 0.8308 1.0131 1.3521 -0.3200 0.1319  0.1409  326 ASN C O   
8639  C  CB  . ASN C 325 ? 0.8331 1.0526 1.3731 -0.2907 0.1354  0.1274  326 ASN C CB  
8640  C  CG  . ASN C 325 ? 0.8558 1.1019 1.4286 -0.2864 0.1345  0.1215  326 ASN C CG  
8641  O  OD1 . ASN C 325 ? 0.8589 1.1078 1.4443 -0.2847 0.1215  0.1195  326 ASN C OD1 
8642  N  ND2 . ASN C 325 ? 0.8772 1.1428 1.4644 -0.2854 0.1483  0.1189  326 ASN C ND2 
8643  N  N   . ALA C 326 ? 0.7353 0.8968 1.2223 -0.2997 0.1272  0.1405  327 ALA C N   
8644  C  CA  . ALA C 326 ? 0.7489 0.8888 1.2154 -0.3073 0.1294  0.1493  327 ALA C CA  
8645  C  C   . ALA C 326 ? 0.7606 0.8844 1.2298 -0.3160 0.1214  0.1513  327 ALA C C   
8646  O  O   . ALA C 326 ? 0.7960 0.9135 1.2638 -0.3289 0.1255  0.1579  327 ALA C O   
8647  C  CB  . ALA C 326 ? 0.7106 0.8325 1.1528 -0.2968 0.1262  0.1522  327 ALA C CB  
8648  N  N   . LEU C 327 ? 0.7852 0.9020 1.2576 -0.3100 0.1102  0.1453  328 LEU C N   
8649  C  CA  . LEU C 327 ? 0.8173 0.9183 1.2923 -0.3184 0.1026  0.1451  328 LEU C CA  
8650  C  C   . LEU C 327 ? 0.8625 0.9787 1.3581 -0.3329 0.1054  0.1457  328 LEU C C   
8651  O  O   . LEU C 327 ? 0.8298 0.9346 1.3233 -0.3450 0.1077  0.1516  328 LEU C O   
8652  C  CB  . LEU C 327 ? 0.8423 0.9372 1.3173 -0.3108 0.0913  0.1366  328 LEU C CB  
8653  C  CG  . LEU C 327 ? 0.8618 0.9425 1.3403 -0.3209 0.0836  0.1340  328 LEU C CG  
8654  C  CD1 . LEU C 327 ? 0.8918 0.9420 1.3549 -0.3241 0.0838  0.1390  328 LEU C CD1 
8655  C  CD2 . LEU C 327 ? 0.8692 0.9493 1.3483 -0.3160 0.0732  0.1246  328 LEU C CD2 
8656  N  N   . GLN C 328 ? 0.9110 1.0532 1.4283 -0.3319 0.1051  0.1402  329 GLN C N   
8657  C  CA  . GLN C 328 ? 1.0213 1.1798 1.5627 -0.3450 0.1058  0.1401  329 GLN C CA  
8658  C  C   . GLN C 328 ? 1.1316 1.2996 1.6782 -0.3557 0.1198  0.1464  329 GLN C C   
8659  O  O   . GLN C 328 ? 1.1622 1.3350 1.7229 -0.3695 0.1213  0.1486  329 GLN C O   
8660  C  CB  . GLN C 328 ? 0.9618 1.1472 1.5285 -0.3405 0.1014  0.1338  329 GLN C CB  
8661  C  CG  . GLN C 328 ? 0.9388 1.1532 1.5278 -0.3413 0.1139  0.1342  329 GLN C CG  
8662  C  CD  . GLN C 328 ? 0.9067 1.1473 1.5255 -0.3367 0.1082  0.1291  329 GLN C CD  
8663  O  OE1 . GLN C 328 ? 0.9018 1.1388 1.5180 -0.3292 0.0954  0.1256  329 GLN C OE1 
8664  N  NE2 . GLN C 328 ? 0.8784 1.1455 1.5265 -0.3416 0.1179  0.1291  329 GLN C NE2 
8665  N  N   . ASP C 329 ? 1.2436 1.4136 1.7775 -0.3505 0.1301  0.1491  330 ASP C N   
8666  C  CA  . ASP C 329 ? 1.2943 1.4737 1.8299 -0.3615 0.1447  0.1544  330 ASP C CA  
8667  C  C   . ASP C 329 ? 1.2708 1.4223 1.7835 -0.3706 0.1437  0.1638  330 ASP C C   
8668  O  O   . ASP C 329 ? 1.3348 1.4871 1.8509 -0.3855 0.1505  0.1693  330 ASP C O   
8669  C  CB  . ASP C 329 ? 1.3624 1.5548 1.8919 -0.3536 0.1562  0.1528  330 ASP C CB  
8670  C  CG  . ASP C 329 ? 1.4584 1.6587 1.9842 -0.3663 0.1731  0.1576  330 ASP C CG  
8671  O  OD1 . ASP C 329 ? 1.4937 1.6873 2.0184 -0.3811 0.1759  0.1639  330 ASP C OD1 
8672  O  OD2 . ASP C 329 ? 1.4641 1.6784 1.9889 -0.3621 0.1845  0.1543  330 ASP C OD2 
8673  N  N   . ASN C 330 ? 1.1869 1.3133 1.6783 -0.3621 0.1348  0.1657  331 ASN C N   
8674  C  CA  . ASN C 330 ? 1.1675 1.2656 1.6407 -0.3695 0.1321  0.1751  331 ASN C CA  
8675  C  C   . ASN C 330 ? 1.1278 1.2117 1.6096 -0.3772 0.1230  0.1741  331 ASN C C   
8676  O  O   . ASN C 330 ? 1.1382 1.1972 1.6085 -0.3833 0.1200  0.1813  331 ASN C O   
8677  C  CB  . ASN C 330 ? 1.1155 1.1924 1.5656 -0.3572 0.1268  0.1782  331 ASN C CB  
8678  C  CG  . ASN C 330 ? 1.0876 1.1647 1.5195 -0.3587 0.1356  0.1865  331 ASN C CG  
8679  O  OD1 . ASN C 330 ? 1.0735 1.1706 1.5096 -0.3657 0.1472  0.1866  331 ASN C OD1 
8680  N  ND2 . ASN C 330 ? 1.0569 1.1116 1.4688 -0.3529 0.1302  0.1935  331 ASN C ND2 
8681  N  N   . ARG C 331 ? 1.1227 1.2224 1.6253 -0.3778 0.1186  0.1656  332 ARG C N   
8682  C  CA  . ARG C 331 ? 1.1242 1.2116 1.6343 -0.3849 0.1088  0.1623  332 ARG C CA  
8683  C  C   . ARG C 331 ? 1.1620 1.2316 1.6695 -0.4007 0.1101  0.1702  332 ARG C C   
8684  O  O   . ARG C 331 ? 1.1777 1.2204 1.6762 -0.4019 0.1028  0.1705  332 ARG C O   
8685  C  CB  . ARG C 331 ? 1.0967 1.2106 1.6329 -0.3881 0.1057  0.1549  332 ARG C CB  
8686  N  N   . ASP C 332 ? 1.1547 1.2389 1.6709 -0.4130 0.1201  0.1760  333 ASP C N   
8687  C  CA  . ASP C 332 ? 1.2136 1.2839 1.7302 -0.4299 0.1215  0.1836  333 ASP C CA  
8688  C  C   . ASP C 332 ? 1.2800 1.3184 1.7729 -0.4304 0.1204  0.1938  333 ASP C C   
8689  O  O   . ASP C 332 ? 1.3210 1.3339 1.8107 -0.4352 0.1133  0.1957  333 ASP C O   
8690  C  CB  . ASP C 332 ? 1.1493 1.2433 1.6748 -0.4410 0.1339  0.1854  333 ASP C CB  
8691  C  CG  . ASP C 332 ? 1.0932 1.2159 1.6457 -0.4429 0.1332  0.1759  333 ASP C CG  
8692  O  OD1 . ASP C 332 ? 1.0557 1.1767 1.6192 -0.4401 0.1215  0.1698  333 ASP C OD1 
8693  O  OD2 . ASP C 332 ? 1.0807 1.2276 1.6435 -0.4479 0.1443  0.1744  333 ASP C OD2 
8694  N  N   . THR C 333 ? 1.3249 1.3641 1.8019 -0.4258 0.1271  0.2006  334 THR C N   
8695  C  CA  . THR C 333 ? 1.3686 1.3792 1.8244 -0.4265 0.1248  0.2123  334 THR C CA  
8696  C  C   . THR C 333 ? 1.3799 1.3672 1.8281 -0.4118 0.1139  0.2085  334 THR C C   
8697  O  O   . THR C 333 ? 1.3987 1.3576 1.8373 -0.4127 0.1089  0.2165  334 THR C O   
8698  C  CB  . THR C 333 ? 1.3951 1.4134 1.8341 -0.4263 0.1338  0.2206  334 THR C CB  
8699  O  OG1 . THR C 333 ? 1.3769 1.4038 1.8104 -0.4091 0.1327  0.2139  334 THR C OG1 
8700  C  CG2 . THR C 333 ? 1.3999 1.4439 1.8447 -0.4382 0.1472  0.2195  334 THR C CG2 
8701  N  N   . LEU C 334 ? 1.3430 1.3422 1.7967 -0.3985 0.1106  0.1966  335 LEU C N   
8702  C  CA  . LEU C 334 ? 1.3368 1.3161 1.7853 -0.3856 0.1014  0.1905  335 LEU C CA  
8703  C  C   . LEU C 334 ? 1.3938 1.3527 1.8495 -0.3932 0.0948  0.1868  335 LEU C C   
8704  O  O   . LEU C 334 ? 1.4071 1.3372 1.8560 -0.3900 0.0900  0.1890  335 LEU C O   
8705  C  CB  . LEU C 334 ? 1.2510 1.2494 1.7040 -0.3722 0.0995  0.1785  335 LEU C CB  
8706  C  CG  . LEU C 334 ? 1.2060 1.1907 1.6598 -0.3642 0.0904  0.1676  335 LEU C CG  
8707  C  CD1 . LEU C 334 ? 1.1999 1.1591 1.6394 -0.3526 0.0871  0.1698  335 LEU C CD1 
8708  C  CD2 . LEU C 334 ? 1.1856 1.1946 1.6476 -0.3567 0.0883  0.1568  335 LEU C CD2 
8709  N  N   . THR C 335 ? 1.4270 1.4008 1.8978 -0.4036 0.0948  0.1811  336 THR C N   
8710  C  CA  . THR C 335 ? 1.4840 1.4405 1.9615 -0.4124 0.0884  0.1759  336 THR C CA  
8711  C  C   . THR C 335 ? 1.5602 1.4983 2.0375 -0.4272 0.0906  0.1869  336 THR C C   
8712  O  O   . THR C 335 ? 1.6071 1.5271 2.0892 -0.4361 0.0861  0.1840  336 THR C O   
8713  C  CB  . THR C 335 ? 1.4596 1.4396 1.9541 -0.4189 0.0857  0.1662  336 THR C CB  
8714  O  OG1 . THR C 335 ? 1.4921 1.4528 1.9880 -0.4245 0.0778  0.1582  336 THR C OG1 
8715  C  CG2 . THR C 335 ? 1.4701 1.4711 1.9789 -0.4338 0.0924  0.1725  336 THR C CG2 
8716  N  N   . ALA C 336 ? 1.6009 1.5431 2.0714 -0.4308 0.0974  0.1995  337 ALA C N   
8717  C  CA  . ALA C 336 ? 1.6045 1.5268 2.0674 -0.4424 0.0990  0.2103  337 ALA C CA  
8718  C  C   . ALA C 336 ? 1.5773 1.4624 2.0333 -0.4372 0.0919  0.2137  337 ALA C C   
8719  O  O   . ALA C 336 ? 1.6469 1.5101 2.1005 -0.4455 0.0900  0.2166  337 ALA C O   
8720  C  CB  . ALA C 336 ? 1.6414 1.5744 2.0913 -0.4453 0.1075  0.2215  337 ALA C CB  
8721  N  N   . LYS C 337 ? 1.3652 1.2434 1.8173 -0.4221 0.0886  0.2117  338 LYS C N   
8722  C  CA  . LYS C 337 ? 1.3035 1.1478 1.7521 -0.4147 0.0828  0.2135  338 LYS C CA  
8723  C  C   . LYS C 337 ? 1.2729 1.0996 1.7307 -0.4176 0.0785  0.2008  338 LYS C C   
8724  O  O   . LYS C 337 ? 1.2580 1.0982 1.7192 -0.4144 0.0772  0.1864  338 LYS C O   
8725  C  CB  . LYS C 337 ? 1.2469 1.0917 1.6870 -0.3957 0.0812  0.2110  338 LYS C CB  
8726  N  N   . VAL C 338 ? 1.2956 1.0916 1.7545 -0.4233 0.0760  0.2058  339 VAL C N   
8727  C  CA  . VAL C 338 ? 1.2600 1.0342 1.7255 -0.4287 0.0730  0.1944  339 VAL C CA  
8728  C  C   . VAL C 338 ? 1.2795 1.0730 1.7527 -0.4368 0.0723  0.1806  339 VAL C C   
8729  O  O   . VAL C 338 ? 1.2863 1.0946 1.7613 -0.4494 0.0738  0.1815  339 VAL C O   
8730  C  CB  . VAL C 338 ? 1.2219 0.9688 1.6902 -0.4159 0.0703  0.1876  339 VAL C CB  
8731  C  CG1 . VAL C 338 ? 1.1947 0.9261 1.6585 -0.4059 0.0694  0.2020  339 VAL C CG1 
8732  C  CG2 . VAL C 338 ? 1.1632 0.9272 1.6265 -0.4034 0.0701  0.1722  339 VAL C CG2 
8733  N  N   . ARG C 366 ? 0.8334 1.0651 1.2856 -0.1918 0.1672  0.0952  367 ARG C N   
8734  C  CA  . ARG C 366 ? 0.8280 1.0792 1.3030 -0.1914 0.1805  0.0873  367 ARG C CA  
8735  C  C   . ARG C 366 ? 0.8803 1.1292 1.3382 -0.1880 0.1897  0.0831  367 ARG C C   
8736  O  O   . ARG C 366 ? 0.8939 1.1273 1.3245 -0.1845 0.1832  0.0868  367 ARG C O   
8737  C  CB  . ARG C 366 ? 0.8036 1.0689 1.3121 -0.1824 0.1730  0.0833  367 ARG C CB  
8738  N  N   . GLU C 367 ? 0.8948 1.1589 1.3700 -0.1893 0.2050  0.0751  368 GLU C N   
8739  C  CA  . GLU C 367 ? 0.8894 1.1516 1.3486 -0.1881 0.2160  0.0694  368 GLU C CA  
8740  C  C   . GLU C 367 ? 0.8972 1.1540 1.3529 -0.1740 0.2056  0.0678  368 GLU C C   
8741  O  O   . GLU C 367 ? 0.8751 1.1393 1.3557 -0.1642 0.1967  0.0663  368 GLU C O   
8742  C  CB  . GLU C 367 ? 0.8931 1.1736 1.3773 -0.1917 0.2356  0.0592  368 GLU C CB  
8743  N  N   . ARG C 368 ? 0.9384 1.1824 1.3628 -0.1739 0.2061  0.0689  369 ARG C N   
8744  C  CA  . ARG C 368 ? 0.9542 1.1930 1.3733 -0.1617 0.1982  0.0670  369 ARG C CA  
8745  C  C   . ARG C 368 ? 0.9683 1.2169 1.3987 -0.1588 0.2121  0.0563  369 ARG C C   
8746  O  O   . ARG C 368 ? 0.9856 1.2341 1.4015 -0.1679 0.2271  0.0520  369 ARG C O   
8747  C  CB  . ARG C 368 ? 0.9631 1.1832 1.3451 -0.1627 0.1903  0.0741  369 ARG C CB  
8748  N  N   . PRO C 369 ? 0.9525 1.2089 1.4084 -0.1467 0.2073  0.0519  370 PRO C N   
8749  C  CA  . PRO C 369 ? 0.9181 1.1829 1.3893 -0.1423 0.2197  0.0415  370 PRO C CA  
8750  C  C   . PRO C 369 ? 0.8918 1.1442 1.3299 -0.1431 0.2237  0.0391  370 PRO C C   
8751  O  O   . PRO C 369 ? 0.8691 1.1075 1.2780 -0.1434 0.2123  0.0469  370 PRO C O   
8752  C  CB  . PRO C 369 ? 0.9391 1.2104 1.4397 -0.1287 0.2073  0.0415  370 PRO C CB  
8753  C  CG  . PRO C 369 ? 0.9341 1.2052 1.4409 -0.1290 0.1922  0.0502  370 PRO C CG  
8754  C  CD  . PRO C 369 ? 0.9319 1.1884 1.4028 -0.1374 0.1894  0.0569  370 PRO C CD  
8755  N  N   . PRO C 370 ? 0.8346 1.0921 1.2781 -0.1441 0.2398  0.0283  371 PRO C N   
8756  C  CA  . PRO C 370 ? 0.8238 1.0697 1.2370 -0.1448 0.2428  0.0253  371 PRO C CA  
8757  C  C   . PRO C 370 ? 0.7558 0.9936 1.1642 -0.1323 0.2248  0.0304  371 PRO C C   
8758  O  O   . PRO C 370 ? 0.7739 0.9986 1.1505 -0.1336 0.2182  0.0348  371 PRO C O   
8759  C  CB  . PRO C 370 ? 0.8223 1.0775 1.2544 -0.1450 0.2625  0.0110  371 PRO C CB  
8760  C  CG  . PRO C 370 ? 0.8262 1.0984 1.3060 -0.1391 0.2650  0.0080  371 PRO C CG  
8761  C  CD  . PRO C 370 ? 0.8149 1.0890 1.2947 -0.1444 0.2563  0.0179  371 PRO C CD  
8762  N  N   . SER C 371 ? 0.7426 0.9884 1.1830 -0.1210 0.2167  0.0301  372 SER C N   
8763  C  CA  . SER C 371 ? 0.7303 0.9692 1.1677 -0.1103 0.1983  0.0363  372 SER C CA  
8764  C  C   . SER C 371 ? 0.7196 0.9677 1.1886 -0.1038 0.1874  0.0400  372 SER C C   
8765  O  O   . SER C 371 ? 0.7701 1.0322 1.2726 -0.1028 0.1942  0.0354  372 SER C O   
8766  C  CB  . SER C 371 ? 0.7516 0.9872 1.1883 -0.1026 0.1998  0.0302  372 SER C CB  
8767  O  OG  . SER C 371 ? 0.7453 0.9933 1.2193 -0.0964 0.2066  0.0227  372 SER C OG  
8768  N  N   . GLY C 372 ? 0.6679 0.9082 1.1266 -0.1001 0.1705  0.0483  373 GLY C N   
8769  C  CA  . GLY C 372 ? 0.5710 0.8180 1.0541 -0.0950 0.1580  0.0523  373 GLY C CA  
8770  C  C   . GLY C 372 ? 0.4946 0.7351 0.9739 -0.0853 0.1446  0.0548  373 GLY C C   
8771  O  O   . GLY C 372 ? 0.4855 0.7176 0.9461 -0.0822 0.1461  0.0529  373 GLY C O   
8772  N  N   . THR C 373 ? 0.4144 0.6587 0.9103 -0.0815 0.1314  0.0591  374 THR C N   
8773  C  CA  . THR C 373 ? 0.3706 0.6087 0.8618 -0.0738 0.1181  0.0621  374 THR C CA  
8774  C  C   . THR C 373 ? 0.3724 0.5944 0.8278 -0.0738 0.1139  0.0649  374 THR C C   
8775  O  O   . THR C 373 ? 0.4309 0.6467 0.8753 -0.0684 0.1125  0.0637  374 THR C O   
8776  C  CB  . THR C 373 ? 0.3650 0.6076 0.8723 -0.0734 0.1036  0.0676  374 THR C CB  
8777  O  OG1 . THR C 373 ? 0.3895 0.6481 0.9345 -0.0721 0.1054  0.0661  374 THR C OG1 
8778  C  CG2 . THR C 373 ? 0.3593 0.5937 0.8560 -0.0674 0.0902  0.0710  374 THR C CG2 
8779  N  N   . LEU C 374 ? 0.3777 0.5931 0.8170 -0.0801 0.1120  0.0688  375 LEU C N   
8780  C  CA  . LEU C 374 ? 0.4717 0.6723 0.8815 -0.0803 0.1077  0.0722  375 LEU C CA  
8781  C  C   . LEU C 374 ? 0.4949 0.6906 0.8871 -0.0806 0.1165  0.0699  375 LEU C C   
8782  O  O   . LEU C 374 ? 0.5274 0.7140 0.9029 -0.0766 0.1120  0.0712  375 LEU C O   
8783  C  CB  . LEU C 374 ? 0.3873 0.5819 0.7873 -0.0876 0.1058  0.0766  375 LEU C CB  
8784  C  CG  . LEU C 374 ? 0.3941 0.5732 0.7684 -0.0876 0.1008  0.0808  375 LEU C CG  
8785  C  CD1 . LEU C 374 ? 0.3829 0.5562 0.7535 -0.0805 0.0906  0.0812  375 LEU C CD1 
8786  C  CD2 . LEU C 374 ? 0.3989 0.5718 0.7678 -0.0947 0.0993  0.0850  375 LEU C CD2 
8787  N  N   . GLU C 375 ? 0.3943 0.5960 0.7898 -0.0862 0.1292  0.0661  376 GLU C N   
8788  C  CA  . GLU C 375 ? 0.4869 0.6837 0.8632 -0.0889 0.1380  0.0635  376 GLU C CA  
8789  C  C   . GLU C 375 ? 0.4458 0.6436 0.8263 -0.0814 0.1391  0.0583  376 GLU C C   
8790  O  O   . GLU C 375 ? 0.4557 0.6450 0.8156 -0.0807 0.1383  0.0587  376 GLU C O   
8791  C  CB  . GLU C 375 ? 0.5298 0.7330 0.9081 -0.0982 0.1528  0.0596  376 GLU C CB  
8792  C  CG  . GLU C 375 ? 0.6065 0.8048 0.9631 -0.1031 0.1627  0.0559  376 GLU C CG  
8793  C  CD  . GLU C 375 ? 0.7183 0.9177 1.0637 -0.1159 0.1747  0.0554  376 GLU C CD  
8794  O  OE1 . GLU C 375 ? 0.7348 0.9388 1.0904 -0.1205 0.1755  0.0582  376 GLU C OE1 
8795  O  OE2 . GLU C 375 ? 0.7569 0.9520 1.0819 -0.1224 0.1833  0.0524  376 GLU C OE2 
8796  N  N   . LYS C 376 ? 0.3992 0.6073 0.8077 -0.0762 0.1404  0.0539  377 LYS C N   
8797  C  CA  . LYS C 376 ? 0.4002 0.6088 0.8164 -0.0687 0.1407  0.0494  377 LYS C CA  
8798  C  C   . LYS C 376 ? 0.3774 0.5766 0.7799 -0.0626 0.1269  0.0546  377 LYS C C   
8799  O  O   . LYS C 376 ? 0.3859 0.5786 0.7747 -0.0598 0.1272  0.0530  377 LYS C O   
8800  C  CB  . LYS C 376 ? 0.3906 0.6119 0.8437 -0.0639 0.1423  0.0458  377 LYS C CB  
8801  C  CG  . LYS C 376 ? 0.3879 0.6199 0.8592 -0.0692 0.1582  0.0390  377 LYS C CG  
8802  C  CD  . LYS C 376 ? 0.4472 0.6921 0.9599 -0.0632 0.1593  0.0358  377 LYS C CD  
8803  C  CE  . LYS C 376 ? 0.3896 0.6467 0.9246 -0.0688 0.1753  0.0293  377 LYS C CE  
8804  N  NZ  . LYS C 376 ? 0.4042 0.6576 0.9229 -0.0746 0.1936  0.0201  377 LYS C NZ  
8805  N  N   . LEU C 377 ? 0.4260 0.6244 0.8318 -0.0614 0.1155  0.0604  378 LEU C N   
8806  C  CA  . LEU C 377 ? 0.4020 0.5912 0.7938 -0.0571 0.1036  0.0650  378 LEU C CA  
8807  C  C   . LEU C 377 ? 0.3919 0.5700 0.7555 -0.0593 0.1045  0.0669  378 LEU C C   
8808  O  O   . LEU C 377 ? 0.3671 0.5387 0.7199 -0.0549 0.0996  0.0679  378 LEU C O   
8809  C  CB  . LEU C 377 ? 0.3860 0.5747 0.7816 -0.0584 0.0935  0.0698  378 LEU C CB  
8810  C  CG  . LEU C 377 ? 0.3951 0.5931 0.8161 -0.0560 0.0868  0.0704  378 LEU C CG  
8811  C  CD1 . LEU C 377 ? 0.3570 0.5517 0.7743 -0.0593 0.0764  0.0750  378 LEU C CD1 
8812  C  CD2 . LEU C 377 ? 0.3784 0.5765 0.8057 -0.0489 0.0820  0.0698  378 LEU C CD2 
8813  N  N   . VAL C 378 ? 0.4135 0.5898 0.7665 -0.0665 0.1103  0.0683  379 VAL C N   
8814  C  CA  . VAL C 378 ? 0.4575 0.6236 0.7856 -0.0696 0.1098  0.0720  379 VAL C CA  
8815  C  C   . VAL C 378 ? 0.4394 0.6040 0.7567 -0.0699 0.1160  0.0682  379 VAL C C   
8816  O  O   . VAL C 378 ? 0.4983 0.6552 0.7998 -0.0684 0.1113  0.0710  379 VAL C O   
8817  C  CB  . VAL C 378 ? 0.4758 0.6398 0.7957 -0.0785 0.1135  0.0758  379 VAL C CB  
8818  C  CG1 . VAL C 378 ? 0.4085 0.5640 0.7045 -0.0835 0.1148  0.0796  379 VAL C CG1 
8819  C  CG2 . VAL C 378 ? 0.4357 0.5960 0.7593 -0.0783 0.1053  0.0806  379 VAL C CG2 
8820  N  N   . SER C 379 ? 0.3968 0.5687 0.7233 -0.0722 0.1269  0.0614  380 SER C N   
8821  C  CA  . SER C 379 ? 0.4038 0.5739 0.7206 -0.0732 0.1339  0.0561  380 SER C CA  
8822  C  C   . SER C 379 ? 0.4799 0.6475 0.8009 -0.0642 0.1271  0.0550  380 SER C C   
8823  O  O   . SER C 379 ? 0.5078 0.6683 0.8114 -0.0641 0.1245  0.0560  380 SER C O   
8824  C  CB  . SER C 379 ? 0.4115 0.5900 0.7420 -0.0769 0.1485  0.0471  380 SER C CB  
8825  O  OG  . SER C 379 ? 0.4686 0.6482 0.7896 -0.0873 0.1567  0.0477  380 SER C OG  
8826  N  N   . GLU C 380 ? 0.4636 0.6372 0.8079 -0.0574 0.1233  0.0538  381 GLU C N   
8827  C  CA  . GLU C 380 ? 0.4744 0.6458 0.8241 -0.0494 0.1158  0.0539  381 GLU C CA  
8828  C  C   . GLU C 380 ? 0.4271 0.5895 0.7576 -0.0479 0.1056  0.0602  381 GLU C C   
8829  O  O   . GLU C 380 ? 0.3726 0.5298 0.6931 -0.0455 0.1038  0.0597  381 GLU C O   
8830  C  CB  . GLU C 380 ? 0.5555 0.7342 0.9314 -0.0442 0.1102  0.0547  381 GLU C CB  
8831  C  CG  . GLU C 380 ? 0.6703 0.8464 1.0513 -0.0370 0.1011  0.0563  381 GLU C CG  
8832  C  CD  . GLU C 380 ? 0.7695 0.9457 1.1582 -0.0336 0.1073  0.0503  381 GLU C CD  
8833  O  OE1 . GLU C 380 ? 0.8197 1.0006 1.2179 -0.0360 0.1192  0.0436  381 GLU C OE1 
8834  O  OE2 . GLU C 380 ? 0.7925 0.9637 1.1776 -0.0291 0.1010  0.0517  381 GLU C OE2 
8835  N  N   . ALA C 381 ? 0.4188 0.5791 0.7454 -0.0496 0.0998  0.0657  382 ALA C N   
8836  C  CA  . ALA C 381 ? 0.4387 0.5907 0.7511 -0.0480 0.0914  0.0711  382 ALA C CA  
8837  C  C   . ALA C 381 ? 0.4359 0.5815 0.7285 -0.0512 0.0931  0.0730  382 ALA C C   
8838  O  O   . ALA C 381 ? 0.4890 0.6294 0.7736 -0.0480 0.0881  0.0749  382 ALA C O   
8839  C  CB  . ALA C 381 ? 0.3655 0.5157 0.6785 -0.0504 0.0872  0.0753  382 ALA C CB  
8840  N  N   . LYS C 382 ? 0.3836 0.5297 0.6685 -0.0583 0.1000  0.0728  383 LYS C N   
8841  C  CA  . LYS C 382 ? 0.3940 0.5345 0.6591 -0.0634 0.1010  0.0753  383 LYS C CA  
8842  C  C   . LYS C 382 ? 0.4582 0.5980 0.7191 -0.0610 0.1025  0.0708  383 LYS C C   
8843  O  O   . LYS C 382 ? 0.3948 0.5292 0.6442 -0.0603 0.0969  0.0744  383 LYS C O   
8844  C  CB  . LYS C 382 ? 0.4084 0.5504 0.6652 -0.0732 0.1094  0.0748  383 LYS C CB  
8845  C  CG  . LYS C 382 ? 0.4488 0.5879 0.7016 -0.0780 0.1065  0.0820  383 LYS C CG  
8846  C  CD  . LYS C 382 ? 0.5167 0.6554 0.7551 -0.0895 0.1141  0.0828  383 LYS C CD  
8847  C  CE  . LYS C 382 ? 0.5519 0.6879 0.7886 -0.0950 0.1119  0.0900  383 LYS C CE  
8848  N  NZ  . LYS C 382 ? 0.6249 0.7605 0.8463 -0.1075 0.1197  0.0912  383 LYS C NZ  
8849  N  N   . ALA C 383 ? 0.4667 0.6120 0.7389 -0.0598 0.1101  0.0629  384 ALA C N   
8850  C  CA  . ALA C 383 ? 0.5106 0.6544 0.7810 -0.0576 0.1126  0.0575  384 ALA C CA  
8851  C  C   . ALA C 383 ? 0.4615 0.6021 0.7345 -0.0498 0.1027  0.0607  384 ALA C C   
8852  O  O   . ALA C 383 ? 0.4679 0.6038 0.7292 -0.0500 0.1001  0.0612  384 ALA C O   
8853  C  CB  . ALA C 383 ? 0.4537 0.6038 0.7424 -0.0560 0.1223  0.0486  384 ALA C CB  
8854  N  N   . GLN C 384 ? 0.4927 0.6358 0.7801 -0.0441 0.0971  0.0628  385 GLN C N   
8855  C  CA  . GLN C 384 ? 0.4956 0.6359 0.7851 -0.0379 0.0885  0.0655  385 GLN C CA  
8856  C  C   . GLN C 384 ? 0.4684 0.6024 0.7425 -0.0388 0.0826  0.0713  385 GLN C C   
8857  O  O   . GLN C 384 ? 0.4300 0.5608 0.6993 -0.0362 0.0790  0.0720  385 GLN C O   
8858  C  CB  . GLN C 384 ? 0.6091 0.7527 0.9134 -0.0342 0.0834  0.0672  385 GLN C CB  
8859  C  CG  . GLN C 384 ? 0.6887 0.8393 1.0137 -0.0320 0.0866  0.0630  385 GLN C CG  
8860  C  CD  . GLN C 384 ? 0.7496 0.8994 1.0821 -0.0271 0.0851  0.0606  385 GLN C CD  
8861  O  OE1 . GLN C 384 ? 0.7988 0.9453 1.1238 -0.0275 0.0894  0.0572  385 GLN C OE1 
8862  N  NE2 . GLN C 384 ? 0.7752 0.9274 1.1222 -0.0232 0.0782  0.0628  385 GLN C NE2 
8863  N  N   . LEU C 385 ? 0.4511 0.5836 0.7196 -0.0424 0.0816  0.0758  386 LEU C N   
8864  C  CA  . LEU C 385 ? 0.4501 0.5769 0.7091 -0.0427 0.0759  0.0819  386 LEU C CA  
8865  C  C   . LEU C 385 ? 0.4620 0.5862 0.7072 -0.0468 0.0761  0.0836  386 LEU C C   
8866  O  O   . LEU C 385 ? 0.4313 0.5522 0.6723 -0.0451 0.0708  0.0873  386 LEU C O   
8867  C  CB  . LEU C 385 ? 0.3998 0.5249 0.6590 -0.0456 0.0748  0.0864  386 LEU C CB  
8868  C  CG  . LEU C 385 ? 0.4364 0.5626 0.7070 -0.0426 0.0729  0.0854  386 LEU C CG  
8869  C  CD1 . LEU C 385 ? 0.4635 0.5856 0.7333 -0.0457 0.0716  0.0898  386 LEU C CD1 
8870  C  CD2 . LEU C 385 ? 0.3567 0.4809 0.6302 -0.0370 0.0681  0.0846  386 LEU C CD2 
8871  N  N   . ARG C 386 ? 0.4744 0.6002 0.7125 -0.0530 0.0825  0.0808  387 ARG C N   
8872  C  CA  . ARG C 386 ? 0.5185 0.6414 0.7409 -0.0588 0.0827  0.0817  387 ARG C CA  
8873  C  C   . ARG C 386 ? 0.5870 0.7096 0.8103 -0.0551 0.0827  0.0768  387 ARG C C   
8874  O  O   . ARG C 386 ? 0.6321 0.7517 0.8443 -0.0579 0.0793  0.0790  387 ARG C O   
8875  C  CB  . ARG C 386 ? 0.6203 0.7442 0.8323 -0.0681 0.0911  0.0786  387 ARG C CB  
8876  C  CG  . ARG C 386 ? 0.7506 0.8725 0.9540 -0.0751 0.0894  0.0861  387 ARG C CG  
8877  C  CD  . ARG C 386 ? 0.8474 0.9696 1.0362 -0.0864 0.0980  0.0829  387 ARG C CD  
8878  N  NE  . ARG C 386 ? 0.9113 1.0389 1.1106 -0.0852 0.1095  0.0721  387 ARG C NE  
8879  C  CZ  . ARG C 386 ? 0.9298 1.0621 1.1400 -0.0858 0.1155  0.0700  387 ARG C CZ  
8880  N  NH1 . ARG C 386 ? 0.9449 1.0760 1.1545 -0.0880 0.1112  0.0777  387 ARG C NH1 
8881  N  NH2 . ARG C 386 ? 0.9281 1.0661 1.1516 -0.0843 0.1257  0.0603  387 ARG C NH2 
8882  N  N   . ASP C 387 ? 0.5413 0.6669 0.7787 -0.0492 0.0857  0.0709  388 ASP C N   
8883  C  CA  . ASP C 387 ? 0.5773 0.7017 0.8175 -0.0454 0.0854  0.0666  388 ASP C CA  
8884  C  C   . ASP C 387 ? 0.4748 0.5970 0.7160 -0.0403 0.0767  0.0716  388 ASP C C   
8885  O  O   . ASP C 387 ? 0.5043 0.6240 0.7408 -0.0400 0.0748  0.0709  388 ASP C O   
8886  C  CB  . ASP C 387 ? 0.6414 0.7696 0.8992 -0.0407 0.0901  0.0602  388 ASP C CB  
8887  C  CG  . ASP C 387 ? 0.7203 0.8463 0.9825 -0.0369 0.0898  0.0562  388 ASP C CG  
8888  O  OD1 . ASP C 387 ? 0.7564 0.8795 1.0097 -0.0411 0.0948  0.0514  388 ASP C OD1 
8889  O  OD2 . ASP C 387 ? 0.7289 0.8554 1.0023 -0.0307 0.0846  0.0579  388 ASP C OD2 
8890  N  N   . VAL C 388 ? 0.3663 0.4889 0.6134 -0.0371 0.0722  0.0762  389 VAL C N   
8891  C  CA  . VAL C 388 ? 0.4234 0.5439 0.6728 -0.0325 0.0660  0.0796  389 VAL C CA  
8892  C  C   . VAL C 388 ? 0.4097 0.5278 0.6538 -0.0341 0.0616  0.0862  389 VAL C C   
8893  O  O   . VAL C 388 ? 0.4134 0.5301 0.6618 -0.0305 0.0579  0.0886  389 VAL C O   
8894  C  CB  . VAL C 388 ? 0.4227 0.5444 0.6829 -0.0281 0.0643  0.0790  389 VAL C CB  
8895  C  CG1 . VAL C 388 ? 0.3489 0.4732 0.6183 -0.0258 0.0664  0.0742  389 VAL C CG1 
8896  C  CG2 . VAL C 388 ? 0.3515 0.4739 0.6141 -0.0298 0.0649  0.0809  389 VAL C CG2 
8897  N  N   . GLN C 389 ? 0.3699 0.4872 0.6053 -0.0399 0.0620  0.0893  390 GLN C N   
8898  C  CA  . GLN C 389 ? 0.4224 0.5374 0.6557 -0.0415 0.0567  0.0971  390 GLN C CA  
8899  C  C   . GLN C 389 ? 0.4304 0.5448 0.6617 -0.0410 0.0518  0.0999  390 GLN C C   
8900  O  O   . GLN C 389 ? 0.3757 0.4890 0.6117 -0.0398 0.0468  0.1061  390 GLN C O   
8901  C  CB  . GLN C 389 ? 0.3855 0.4996 0.6090 -0.0492 0.0572  0.1012  390 GLN C CB  
8902  C  CG  . GLN C 389 ? 0.3972 0.5112 0.6061 -0.0564 0.0588  0.0995  390 GLN C CG  
8903  C  CD  . GLN C 389 ? 0.4830 0.5957 0.6793 -0.0659 0.0600  0.1032  390 GLN C CD  
8904  O  OE1 . GLN C 389 ? 0.5423 0.6553 0.7420 -0.0667 0.0625  0.1044  390 GLN C OE1 
8905  N  NE2 . GLN C 389 ? 0.4993 0.6104 0.6798 -0.0742 0.0581  0.1053  390 GLN C NE2 
8906  N  N   . ASP C 390 ? 0.4513 0.5663 0.6775 -0.0418 0.0535  0.0952  391 ASP C N   
8907  C  CA  . ASP C 390 ? 0.4585 0.5732 0.6819 -0.0425 0.0490  0.0974  391 ASP C CA  
8908  C  C   . ASP C 390 ? 0.3655 0.4806 0.5976 -0.0361 0.0488  0.0944  391 ASP C C   
8909  O  O   . ASP C 390 ? 0.3660 0.4812 0.5968 -0.0366 0.0460  0.0951  391 ASP C O   
8910  C  CB  . ASP C 390 ? 0.5243 0.6380 0.7340 -0.0494 0.0510  0.0940  391 ASP C CB  
8911  C  CG  . ASP C 390 ? 0.6146 0.7282 0.8250 -0.0481 0.0588  0.0845  391 ASP C CG  
8912  O  OD1 . ASP C 390 ? 0.6407 0.7556 0.8628 -0.0416 0.0607  0.0818  391 ASP C OD1 
8913  O  OD2 . ASP C 390 ? 0.6622 0.7742 0.8622 -0.0540 0.0630  0.0798  391 ASP C OD2 
8914  N  N   . PHE C 391 ? 0.4268 0.5421 0.6668 -0.0313 0.0513  0.0916  392 PHE C N   
8915  C  CA  . PHE C 391 ? 0.4789 0.5940 0.7246 -0.0267 0.0514  0.0887  392 PHE C CA  
8916  C  C   . PHE C 391 ? 0.4635 0.5786 0.7117 -0.0255 0.0479  0.0917  392 PHE C C   
8917  O  O   . PHE C 391 ? 0.5098 0.6246 0.7563 -0.0256 0.0472  0.0900  392 PHE C O   
8918  C  CB  . PHE C 391 ? 0.4024 0.5174 0.6546 -0.0236 0.0527  0.0875  392 PHE C CB  
8919  C  CG  . PHE C 391 ? 0.4310 0.5453 0.6866 -0.0207 0.0521  0.0852  392 PHE C CG  
8920  C  CD1 . PHE C 391 ? 0.3411 0.4556 0.5982 -0.0199 0.0528  0.0818  392 PHE C CD1 
8921  C  CD2 . PHE C 391 ? 0.4292 0.5421 0.6871 -0.0192 0.0512  0.0864  392 PHE C CD2 
8922  C  CE1 . PHE C 391 ? 0.3391 0.4524 0.5988 -0.0181 0.0508  0.0812  392 PHE C CE1 
8923  C  CE2 . PHE C 391 ? 0.4065 0.5181 0.6645 -0.0182 0.0505  0.0849  392 PHE C CE2 
8924  C  CZ  . PHE C 391 ? 0.3380 0.4498 0.5965 -0.0179 0.0494  0.0830  392 PHE C CZ  
8925  N  N   . TRP C 392 ? 0.4662 0.5815 0.7199 -0.0245 0.0463  0.0960  393 TRP C N   
8926  C  CA  . TRP C 392 ? 0.4850 0.6011 0.7455 -0.0227 0.0446  0.0983  393 TRP C CA  
8927  C  C   . TRP C 392 ? 0.4481 0.5661 0.7067 -0.0256 0.0405  0.1017  393 TRP C C   
8928  O  O   . TRP C 392 ? 0.5258 0.6454 0.7901 -0.0244 0.0395  0.1025  393 TRP C O   
8929  C  CB  . TRP C 392 ? 0.4361 0.5516 0.7063 -0.0208 0.0449  0.1016  393 TRP C CB  
8930  C  CG  . TRP C 392 ? 0.3961 0.5090 0.6671 -0.0191 0.0487  0.0979  393 TRP C CG  
8931  C  CD1 . TRP C 392 ? 0.4164 0.5276 0.6875 -0.0200 0.0494  0.0989  393 TRP C CD1 
8932  C  CD2 . TRP C 392 ? 0.4090 0.5203 0.6793 -0.0176 0.0518  0.0931  393 TRP C CD2 
8933  N  NE1 . TRP C 392 ? 0.4063 0.5153 0.6778 -0.0188 0.0526  0.0946  393 TRP C NE1 
8934  C  CE2 . TRP C 392 ? 0.4059 0.5149 0.6762 -0.0177 0.0538  0.0912  393 TRP C CE2 
8935  C  CE3 . TRP C 392 ? 0.3986 0.5100 0.6676 -0.0172 0.0526  0.0908  393 TRP C CE3 
8936  C  CZ2 . TRP C 392 ? 0.3792 0.4859 0.6471 -0.0179 0.0559  0.0870  393 TRP C CZ2 
8937  C  CZ3 . TRP C 392 ? 0.3931 0.5020 0.6590 -0.0174 0.0548  0.0871  393 TRP C CZ3 
8938  C  CH2 . TRP C 392 ? 0.4042 0.5108 0.6692 -0.0180 0.0561  0.0853  393 TRP C CH2 
8939  N  N   . ILE C 393 ? 0.4323 0.5503 0.6823 -0.0303 0.0382  0.1035  394 ILE C N   
8940  C  CA  . ILE C 393 ? 0.4261 0.5455 0.6717 -0.0348 0.0335  0.1065  394 ILE C CA  
8941  C  C   . ILE C 393 ? 0.4393 0.5566 0.6732 -0.0381 0.0356  0.1005  394 ILE C C   
8942  O  O   . ILE C 393 ? 0.5004 0.6178 0.7293 -0.0421 0.0325  0.1013  394 ILE C O   
8943  C  CB  . ILE C 393 ? 0.4017 0.5219 0.6442 -0.0401 0.0279  0.1141  394 ILE C CB  
8944  C  CG1 . ILE C 393 ? 0.3886 0.5062 0.6176 -0.0448 0.0306  0.1118  394 ILE C CG1 
8945  C  CG2 . ILE C 393 ? 0.4040 0.5255 0.6618 -0.0364 0.0256  0.1204  394 ILE C CG2 
8946  C  CD1 . ILE C 393 ? 0.4464 0.5639 0.6678 -0.0524 0.0246  0.1197  394 ILE C CD1 
8947  N  N   . SER C 394 ? 0.4752 0.5904 0.7062 -0.0365 0.0411  0.0946  395 SER C N   
8948  C  CA  . SER C 394 ? 0.5348 0.6474 0.7588 -0.0386 0.0446  0.0879  395 SER C CA  
8949  C  C   . SER C 394 ? 0.4491 0.5604 0.6799 -0.0338 0.0457  0.0846  395 SER C C   
8950  O  O   . SER C 394 ? 0.3978 0.5061 0.6258 -0.0349 0.0477  0.0798  395 SER C O   
8951  C  CB  . SER C 394 ? 0.5756 0.6872 0.7959 -0.0398 0.0503  0.0833  395 SER C CB  
8952  O  OG  . SER C 394 ? 0.5971 0.7098 0.8271 -0.0340 0.0525  0.0822  395 SER C OG  
8953  N  N   . LEU C 395 ? 0.4327 0.5454 0.6720 -0.0292 0.0447  0.0870  396 LEU C N   
8954  C  CA  . LEU C 395 ? 0.4616 0.5729 0.7054 -0.0261 0.0449  0.0854  396 LEU C CA  
8955  C  C   . LEU C 395 ? 0.4896 0.5992 0.7308 -0.0284 0.0431  0.0847  396 LEU C C   
8956  O  O   . LEU C 395 ? 0.5054 0.6115 0.7470 -0.0276 0.0442  0.0813  396 LEU C O   
8957  C  CB  . LEU C 395 ? 0.5216 0.6345 0.7717 -0.0233 0.0444  0.0883  396 LEU C CB  
8958  C  CG  . LEU C 395 ? 0.5619 0.6744 0.8146 -0.0208 0.0465  0.0873  396 LEU C CG  
8959  C  CD1 . LEU C 395 ? 0.5270 0.6403 0.7845 -0.0196 0.0473  0.0894  396 LEU C CD1 
8960  C  CD2 . LEU C 395 ? 0.5149 0.6249 0.7678 -0.0195 0.0467  0.0846  396 LEU C CD2 
8961  N  N   . PRO C 396 ? 0.4311 0.5430 0.6712 -0.0315 0.0397  0.0885  397 PRO C N   
8962  C  CA  . PRO C 396 ? 0.4391 0.5495 0.6769 -0.0345 0.0376  0.0878  397 PRO C CA  
8963  C  C   . PRO C 396 ? 0.4739 0.5793 0.7034 -0.0379 0.0396  0.0821  397 PRO C C   
8964  O  O   . PRO C 396 ? 0.4465 0.5478 0.6769 -0.0375 0.0405  0.0790  397 PRO C O   
8965  C  CB  . PRO C 396 ? 0.4434 0.5583 0.6824 -0.0380 0.0327  0.0936  397 PRO C CB  
8966  C  CG  . PRO C 396 ? 0.4313 0.5500 0.6785 -0.0346 0.0329  0.0976  397 PRO C CG  
8967  C  CD  . PRO C 396 ? 0.4308 0.5469 0.6740 -0.0325 0.0367  0.0942  397 PRO C CD  
8968  N  N   . GLY C 397 ? 0.4556 0.5607 0.6771 -0.0417 0.0408  0.0807  398 GLY C N   
8969  C  CA  . GLY C 397 ? 0.4913 0.5913 0.7043 -0.0459 0.0448  0.0737  398 GLY C CA  
8970  C  C   . GLY C 397 ? 0.5355 0.6318 0.7559 -0.0409 0.0502  0.0677  398 GLY C C   
8971  O  O   . GLY C 397 ? 0.5464 0.6373 0.7668 -0.0419 0.0528  0.0623  398 GLY C O   
8972  N  N   . THR C 398 ? 0.5144 0.6135 0.7423 -0.0357 0.0515  0.0691  399 THR C N   
8973  C  CA  . THR C 398 ? 0.5467 0.6437 0.7845 -0.0309 0.0549  0.0653  399 THR C CA  
8974  C  C   . THR C 398 ? 0.5382 0.6318 0.7825 -0.0281 0.0521  0.0663  399 THR C C   
8975  O  O   . THR C 398 ? 0.6037 0.6921 0.8524 -0.0277 0.0543  0.0618  399 THR C O   
8976  C  CB  . THR C 398 ? 0.5242 0.6255 0.7683 -0.0269 0.0549  0.0681  399 THR C CB  
8977  O  OG1 . THR C 398 ? 0.5312 0.6349 0.7702 -0.0297 0.0581  0.0670  399 THR C OG1 
8978  C  CG2 . THR C 398 ? 0.5362 0.6362 0.7923 -0.0223 0.0561  0.0659  399 THR C CG2 
8979  N  N   . LEU C 399 ? 0.5327 0.6287 0.7778 -0.0268 0.0477  0.0721  400 LEU C N   
8980  C  CA  . LEU C 399 ? 0.5157 0.6087 0.7650 -0.0253 0.0448  0.0742  400 LEU C CA  
8981  C  C   . LEU C 399 ? 0.6138 0.7019 0.8602 -0.0286 0.0444  0.0719  400 LEU C C   
8982  O  O   . LEU C 399 ? 0.6165 0.6992 0.8680 -0.0275 0.0436  0.0712  400 LEU C O   
8983  C  CB  . LEU C 399 ? 0.5242 0.6210 0.7729 -0.0250 0.0421  0.0797  400 LEU C CB  
8984  C  CG  . LEU C 399 ? 0.5612 0.6610 0.8122 -0.0223 0.0425  0.0815  400 LEU C CG  
8985  C  CD1 . LEU C 399 ? 0.5449 0.6477 0.7951 -0.0229 0.0419  0.0851  400 LEU C CD1 
8986  C  CD2 . LEU C 399 ? 0.5204 0.6173 0.7766 -0.0200 0.0414  0.0814  400 LEU C CD2 
8987  N  N   . CYS C 400 ? 0.5899 0.6795 0.8284 -0.0333 0.0441  0.0714  401 CYS C N   
8988  C  CA  . CYS C 400 ? 0.6411 0.7259 0.8752 -0.0379 0.0434  0.0688  401 CYS C CA  
8989  C  C   . CYS C 400 ? 0.6390 0.7166 0.8736 -0.0386 0.0484  0.0609  401 CYS C C   
8990  O  O   . CYS C 400 ? 0.6671 0.7380 0.9059 -0.0385 0.0486  0.0585  401 CYS C O   
8991  C  CB  . CYS C 400 ? 0.6363 0.7249 0.8614 -0.0439 0.0407  0.0708  401 CYS C CB  
8992  S  SG  . CYS C 400 ? 0.6335 0.7298 0.8634 -0.0437 0.0352  0.0794  401 CYS C SG  
8993  N  N   . SER C 401 ? 0.6866 0.7652 0.9178 -0.0395 0.0531  0.0566  402 SER C N   
8994  C  CA  . SER C 401 ? 0.7603 0.8324 0.9918 -0.0413 0.0600  0.0474  402 SER C CA  
8995  C  C   . SER C 401 ? 0.7903 0.8587 1.0388 -0.0345 0.0626  0.0451  402 SER C C   
8996  O  O   . SER C 401 ? 0.8346 0.8956 1.0887 -0.0349 0.0673  0.0381  402 SER C O   
8997  C  CB  . SER C 401 ? 0.7720 0.8468 0.9951 -0.0450 0.0653  0.0435  402 SER C CB  
8998  O  OG  . SER C 401 ? 0.8195 0.8876 1.0402 -0.0488 0.0737  0.0332  402 SER C OG  
8999  N  N   . GLU C 402 ? 0.8157 0.8889 1.0734 -0.0288 0.0592  0.0510  403 GLU C N   
9000  C  CA  . GLU C 402 ? 0.8854 0.9560 1.1604 -0.0230 0.0597  0.0505  403 GLU C CA  
9001  C  C   . GLU C 402 ? 0.9587 1.0246 1.2400 -0.0211 0.0535  0.0558  403 GLU C C   
9002  O  O   . GLU C 402 ? 0.9956 1.0564 1.2917 -0.0176 0.0532  0.0552  403 GLU C O   
9003  C  CB  . GLU C 402 ? 0.8769 0.9546 1.1582 -0.0190 0.0587  0.0541  403 GLU C CB  
9004  C  CG  . GLU C 402 ? 0.8866 0.9672 1.1683 -0.0169 0.0510  0.0630  403 GLU C CG  
9005  C  CD  . GLU C 402 ? 0.9214 1.0090 1.2036 -0.0153 0.0505  0.0658  403 GLU C CD  
9006  O  OE1 . GLU C 402 ? 0.9273 1.0181 1.2087 -0.0159 0.0557  0.0617  403 GLU C OE1 
9007  O  OE2 . GLU C 402 ? 0.9188 1.0082 1.2011 -0.0142 0.0452  0.0718  403 GLU C OE2 
9008  N  N   . LYS C 403 ? 0.9813 1.0487 1.2525 -0.0238 0.0485  0.0613  404 LYS C N   
9009  C  CA  . LYS C 403 ? 0.9956 1.0592 1.2705 -0.0233 0.0428  0.0672  404 LYS C CA  
9010  C  C   . LYS C 403 ? 1.0041 1.0626 1.2723 -0.0279 0.0418  0.0664  404 LYS C C   
9011  O  O   . LYS C 403 ? 1.0020 1.0520 1.2760 -0.0284 0.0428  0.0630  404 LYS C O   
9012  C  CB  . LYS C 403 ? 0.9826 1.0523 1.2531 -0.0228 0.0383  0.0747  404 LYS C CB  
9013  C  CG  . LYS C 403 ? 0.9753 1.0442 1.2547 -0.0197 0.0341  0.0796  404 LYS C CG  
9014  C  CD  . LYS C 403 ? 0.9771 1.0460 1.2697 -0.0156 0.0365  0.0760  404 LYS C CD  
9015  C  CE  . LYS C 403 ? 0.9714 1.0409 1.2731 -0.0133 0.0304  0.0825  404 LYS C CE  
9016  N  NZ  . LYS C 403 ? 0.9609 1.0323 1.2786 -0.0091 0.0324  0.0796  404 LYS C NZ  
9017  N  N   . MET C 404 ? 1.0082 1.0721 1.2662 -0.0314 0.0398  0.0697  405 MET C N   
9018  C  CA  . MET C 404 ? 1.0233 1.0846 1.2764 -0.0361 0.0374  0.0713  405 MET C CA  
9019  C  C   . MET C 404 ? 1.0053 1.0619 1.2528 -0.0410 0.0400  0.0646  405 MET C C   
9020  O  O   . MET C 404 ? 0.9998 1.0487 1.2489 -0.0436 0.0394  0.0628  405 MET C O   
9021  C  CB  . MET C 404 ? 1.0336 1.1036 1.2813 -0.0379 0.0351  0.0768  405 MET C CB  
9022  C  CG  . MET C 404 ? 1.0422 1.1160 1.2927 -0.0345 0.0338  0.0821  405 MET C CG  
9023  S  SD  . MET C 404 ? 0.9631 1.0476 1.2104 -0.0344 0.0347  0.0849  405 MET C SD  
9024  C  CE  . MET C 404 ? 0.5022 0.5873 0.7513 -0.0312 0.0345  0.0882  405 MET C CE  
9025  N  N   . ALA C 405 ? 0.9609 1.0217 1.2008 -0.0433 0.0426  0.0610  406 ALA C N   
9026  C  CA  . ALA C 405 ? 0.9460 1.0026 1.1764 -0.0503 0.0446  0.0548  406 ALA C CA  
9027  C  C   . ALA C 405 ? 0.9497 0.9963 1.1839 -0.0499 0.0512  0.0453  406 ALA C C   
9028  O  O   . ALA C 405 ? 0.9654 1.0049 1.1931 -0.0560 0.0537  0.0388  406 ALA C O   
9029  C  CB  . ALA C 405 ? 0.9113 0.9751 1.1308 -0.0542 0.0445  0.0552  406 ALA C CB  
9030  N  N   . ARG C 413 ? 1.0663 1.0481 1.2093 -0.1350 0.0458  0.0013  414 ARG C N   
9031  C  CA  . ARG C 413 ? 1.0289 1.0258 1.1774 -0.1332 0.0344  0.0160  414 ARG C CA  
9032  C  C   . ARG C 413 ? 0.9344 0.9403 1.1010 -0.1187 0.0346  0.0243  414 ARG C C   
9033  O  O   . ARG C 413 ? 0.9595 0.9597 1.1353 -0.1102 0.0420  0.0197  414 ARG C O   
9034  C  CB  . ARG C 413 ? 1.0958 1.0893 1.2485 -0.1384 0.0283  0.0193  414 ARG C CB  
9035  C  CG  . ARG C 413 ? 1.1728 1.1598 1.3065 -0.1546 0.0254  0.0131  414 ARG C CG  
9036  C  CD  . ARG C 413 ? 1.2419 1.2184 1.3810 -0.1589 0.0240  0.0110  414 ARG C CD  
9037  N  NE  . ARG C 413 ? 1.3145 1.2844 1.4344 -0.1755 0.0207  0.0049  414 ARG C NE  
9038  C  CZ  . ARG C 413 ? 1.3850 1.3366 1.4962 -0.1830 0.0278  -0.0087 414 ARG C CZ  
9039  N  NH1 . ARG C 413 ? 1.4002 1.3384 1.5230 -0.1743 0.0386  -0.0172 414 ARG C NH1 
9040  N  NH2 . ARG C 413 ? 1.4118 1.3579 1.5033 -0.1996 0.0239  -0.0138 414 ARG C NH2 
9041  N  N   . CYS C 414 ? 0.8233 0.8432 0.9953 -0.1165 0.0264  0.0364  415 CYS C N   
9042  C  CA  . CYS C 414 ? 0.7473 0.7762 0.9336 -0.1045 0.0264  0.0441  415 CYS C CA  
9043  C  C   . CYS C 414 ? 0.6721 0.7123 0.8672 -0.1039 0.0189  0.0554  415 CYS C C   
9044  O  O   . CYS C 414 ? 0.6772 0.7211 0.8685 -0.1125 0.0128  0.0583  415 CYS C O   
9045  C  CB  . CYS C 414 ? 0.7337 0.7698 0.9151 -0.1014 0.0286  0.0443  415 CYS C CB  
9046  S  SG  . CYS C 414 ? 0.8465 0.8929 1.0130 -0.1117 0.0210  0.0490  415 CYS C SG  
9047  N  N   . TRP C 415 ? 0.6302 0.6760 0.8377 -0.0946 0.0196  0.0616  416 TRP C N   
9048  C  CA  . TRP C 415 ? 0.6218 0.6779 0.8386 -0.0939 0.0150  0.0710  416 TRP C CA  
9049  C  C   . TRP C 415 ? 0.6248 0.6953 0.8429 -0.0936 0.0113  0.0770  416 TRP C C   
9050  O  O   . TRP C 415 ? 0.6401 0.7147 0.8594 -0.0872 0.0138  0.0779  416 TRP C O   
9051  C  CB  . TRP C 415 ? 0.6041 0.6586 0.8310 -0.0858 0.0179  0.0744  416 TRP C CB  
9052  C  CG  . TRP C 415 ? 0.6240 0.6895 0.8598 -0.0846 0.0158  0.0829  416 TRP C CG  
9053  C  CD1 . TRP C 415 ? 0.6336 0.7082 0.8747 -0.0785 0.0173  0.0873  416 TRP C CD1 
9054  C  CD2 . TRP C 415 ? 0.6580 0.7262 0.8988 -0.0902 0.0130  0.0871  416 TRP C CD2 
9055  N  NE1 . TRP C 415 ? 0.6035 0.6861 0.8527 -0.0799 0.0167  0.0932  416 TRP C NE1 
9056  C  CE2 . TRP C 415 ? 0.6351 0.7145 0.8847 -0.0870 0.0140  0.0936  416 TRP C CE2 
9057  C  CE3 . TRP C 415 ? 0.6717 0.7337 0.9106 -0.0980 0.0103  0.0857  416 TRP C CE3 
9058  C  CZ2 . TRP C 415 ? 0.6566 0.7421 0.9141 -0.0913 0.0131  0.0985  416 TRP C CZ2 
9059  C  CZ3 . TRP C 415 ? 0.6728 0.7409 0.9194 -0.1023 0.0083  0.0914  416 TRP C CZ3 
9060  C  CH2 . TRP C 415 ? 0.6671 0.7472 0.9232 -0.0989 0.0100  0.0977  416 TRP C CH2 
9061  N  N   . ASN C 416 ? 0.5802 0.6583 0.7997 -0.1008 0.0049  0.0816  417 ASN C N   
9062  C  CA  . ASN C 416 ? 0.5873 0.6790 0.8114 -0.1012 0.0000  0.0886  417 ASN C CA  
9063  C  C   . ASN C 416 ? 0.5241 0.6275 0.7662 -0.0966 -0.0004 0.0964  417 ASN C C   
9064  O  O   . ASN C 416 ? 0.5786 0.6937 0.8297 -0.0959 -0.0041 0.1026  417 ASN C O   
9065  C  CB  . ASN C 416 ? 0.5830 0.6771 0.7993 -0.1127 -0.0081 0.0898  417 ASN C CB  
9066  C  CG  . ASN C 416 ? 0.6168 0.7085 0.8354 -0.1203 -0.0115 0.0900  417 ASN C CG  
9067  O  OD1 . ASN C 416 ? 0.6085 0.7051 0.8413 -0.1175 -0.0109 0.0943  417 ASN C OD1 
9068  N  ND2 . ASN C 416 ? 0.6257 0.7093 0.8293 -0.1308 -0.0147 0.0848  417 ASN C ND2 
9069  N  N   . GLY C 417 ? 0.4259 0.5257 0.6736 -0.0938 0.0037  0.0961  418 GLY C N   
9070  C  CA  . GLY C 417 ? 0.4155 0.5251 0.6783 -0.0908 0.0054  0.1020  418 GLY C CA  
9071  C  C   . GLY C 417 ? 0.6256 0.7386 0.8960 -0.0978 0.0026  0.1051  418 GLY C C   
9072  O  O   . GLY C 417 ? 0.6651 0.7842 0.9471 -0.0966 0.0059  0.1086  418 GLY C O   
9073  N  N   . MET C 418 ? 0.6853 0.7942 0.9486 -0.1061 -0.0031 0.1033  419 MET C N   
9074  C  CA  . MET C 418 ? 0.7169 0.8282 0.9867 -0.1140 -0.0066 0.1058  419 MET C CA  
9075  C  C   . MET C 418 ? 0.7700 0.8652 1.0273 -0.1190 -0.0060 0.0997  419 MET C C   
9076  O  O   . MET C 418 ? 0.7856 0.8758 1.0464 -0.1193 -0.0029 0.1001  419 MET C O   
9077  C  CB  . MET C 418 ? 0.7139 0.8362 0.9892 -0.1214 -0.0157 0.1105  419 MET C CB  
9078  C  CG  . MET C 418 ? 0.7164 0.8555 1.0111 -0.1168 -0.0168 0.1180  419 MET C CG  
9079  S  SD  . MET C 418 ? 1.3168 1.4708 1.6260 -0.1261 -0.0292 0.1264  419 MET C SD  
9080  C  CE  . MET C 418 ? 0.6279 0.7733 0.9124 -0.1333 -0.0375 0.1235  419 MET C CE  
9081  N  N   . ALA C 419 ? 0.7960 0.8826 1.0389 -0.1234 -0.0085 0.0938  420 ALA C N   
9082  C  CA  . ALA C 419 ? 0.7998 0.8693 1.0316 -0.1275 -0.0065 0.0862  420 ALA C CA  
9083  C  C   . ALA C 419 ? 0.8443 0.9032 1.0630 -0.1243 -0.0023 0.0779  420 ALA C C   
9084  O  O   . ALA C 419 ? 0.8006 0.8657 1.0176 -0.1195 -0.0015 0.0787  420 ALA C O   
9085  C  CB  . ALA C 419 ? 0.8241 0.8920 1.0514 -0.1402 -0.0130 0.0853  420 ALA C CB  
9086  N  N   . ARG C 420 ? 0.7955 0.8382 1.0064 -0.1271 0.0010  0.0697  421 ARG C N   
9087  C  CA  . ARG C 420 ? 0.8113 0.8435 1.0114 -0.1252 0.0064  0.0603  421 ARG C CA  
9088  C  C   . ARG C 420 ? 0.8646 0.8960 1.0485 -0.1362 0.0032  0.0554  421 ARG C C   
9089  O  O   . ARG C 420 ? 0.9309 0.9569 1.1083 -0.1469 -0.0004 0.0527  421 ARG C O   
9090  C  CB  . ARG C 420 ? 0.7590 0.7735 0.9608 -0.1232 0.0122  0.0531  421 ARG C CB  
9091  N  N   . GLY C 421 ? 0.9099 0.9462 1.0862 -0.1347 0.0041  0.0545  422 GLY C N   
9092  C  CA  . GLY C 421 ? 0.9583 0.9951 1.1170 -0.1462 0.0000  0.0517  422 GLY C CA  
9093  C  C   . GLY C 421 ? 0.9866 1.0322 1.1408 -0.1429 -0.0002 0.0547  422 GLY C C   
9094  O  O   . GLY C 421 ? 1.0275 1.0744 1.1892 -0.1317 0.0057  0.0547  422 GLY C O   
9095  N  N   . ARG C 422 ? 1.0110 1.0625 1.1529 -0.1532 -0.0079 0.0581  423 ARG C N   
9096  C  CA  . ARG C 422 ? 1.0142 1.0728 1.1502 -0.1517 -0.0089 0.0616  423 ARG C CA  
9097  C  C   . ARG C 422 ? 0.9490 1.0248 1.1023 -0.1459 -0.0169 0.0755  423 ARG C C   
9098  O  O   . ARG C 422 ? 0.9409 1.0252 1.1044 -0.1497 -0.0255 0.0835  423 ARG C O   
9099  C  CB  . ARG C 422 ? 1.1332 1.1872 1.2438 -0.1672 -0.0126 0.0577  423 ARG C CB  
9100  C  CG  . ARG C 422 ? 1.2338 1.2714 1.3267 -0.1710 -0.0007 0.0421  423 ARG C CG  
9101  C  CD  . ARG C 422 ? 1.3122 1.3454 1.3766 -0.1873 -0.0031 0.0380  423 ARG C CD  
9102  N  NE  . ARG C 422 ? 1.3779 1.3980 1.4255 -0.2011 -0.0017 0.0278  423 ARG C NE  
9103  C  CZ  . ARG C 422 ? 1.4060 1.4100 1.4486 -0.2010 0.0114  0.0124  423 ARG C CZ  
9104  N  NH1 . ARG C 422 ? 1.3975 1.3976 1.4518 -0.1878 0.0236  0.0063  423 ARG C NH1 
9105  N  NH2 . ARG C 422 ? 1.4303 1.4220 1.4574 -0.2146 0.0121  0.0032  423 ARG C NH2 
9106  N  N   . TYR C 423 ? 0.8338 0.9145 0.9919 -0.1368 -0.0134 0.0780  424 TYR C N   
9107  C  CA  . TYR C 423 ? 0.7478 0.8431 0.9234 -0.1302 -0.0189 0.0897  424 TYR C CA  
9108  C  C   . TYR C 423 ? 0.7277 0.8294 0.8945 -0.1382 -0.0279 0.0967  424 TYR C C   
9109  O  O   . TYR C 423 ? 0.7337 0.8319 0.8873 -0.1388 -0.0248 0.0939  424 TYR C O   
9110  C  CB  . TYR C 423 ? 0.6883 0.7841 0.8742 -0.1163 -0.0102 0.0885  424 TYR C CB  
9111  C  CG  . TYR C 423 ? 0.6697 0.7786 0.8739 -0.1086 -0.0132 0.0984  424 TYR C CG  
9112  C  CD1 . TYR C 423 ? 0.6438 0.7606 0.8677 -0.1041 -0.0143 0.1038  424 TYR C CD1 
9113  C  CD2 . TYR C 423 ? 0.6715 0.7842 0.8737 -0.1061 -0.0138 0.1016  424 TYR C CD2 
9114  C  CE1 . TYR C 423 ? 0.6090 0.7367 0.8507 -0.0972 -0.0152 0.1113  424 TYR C CE1 
9115  C  CE2 . TYR C 423 ? 0.6223 0.7455 0.8425 -0.0989 -0.0158 0.1099  424 TYR C CE2 
9116  C  CZ  . TYR C 423 ? 0.6329 0.7635 0.8733 -0.0944 -0.0160 0.1142  424 TYR C CZ  
9117  O  OH  . TYR C 423 ? 0.5800 0.7203 0.8395 -0.0875 -0.0163 0.1209  424 TYR C OH  
9118  N  N   . LEU C 424 ? 0.7462 0.8577 0.9213 -0.1447 -0.0396 0.1064  425 LEU C N   
9119  C  CA  . LEU C 424 ? 0.7711 0.8891 0.9396 -0.1537 -0.0512 0.1155  425 LEU C CA  
9120  C  C   . LEU C 424 ? 0.7994 0.9265 0.9809 -0.1455 -0.0532 0.1245  425 LEU C C   
9121  O  O   . LEU C 424 ? 0.7994 0.9249 0.9656 -0.1515 -0.0569 0.1270  425 LEU C O   
9122  C  CB  . LEU C 424 ? 0.8261 0.9526 1.0034 -0.1634 -0.0646 0.1244  425 LEU C CB  
9123  C  CG  . LEU C 424 ? 0.8287 0.9689 1.0387 -0.1564 -0.0684 0.1334  425 LEU C CG  
9124  C  CD1 . LEU C 424 ? 0.8334 0.9877 1.0622 -0.1550 -0.0791 0.1477  425 LEU C CD1 
9125  C  CD2 . LEU C 424 ? 0.8457 0.9865 1.0575 -0.1659 -0.0742 0.1334  425 LEU C CD2 
9126  N  N   . PRO C 425 ? 0.7119 0.8478 0.9204 -0.1328 -0.0503 0.1291  426 PRO C N   
9127  C  CA  . PRO C 425 ? 0.7691 0.9144 0.9932 -0.1269 -0.0543 0.1391  426 PRO C CA  
9128  C  C   . PRO C 425 ? 0.8454 0.9849 1.0553 -0.1241 -0.0492 0.1362  426 PRO C C   
9129  O  O   . PRO C 425 ? 0.8204 0.9500 1.0159 -0.1213 -0.0385 0.1253  426 PRO C O   
9130  C  CB  . PRO C 425 ? 0.6842 0.8364 0.9359 -0.1139 -0.0476 0.1399  426 PRO C CB  
9131  C  CG  . PRO C 425 ? 0.6806 0.8308 0.9339 -0.1163 -0.0453 0.1351  426 PRO C CG  
9132  C  CD  . PRO C 425 ? 0.7104 0.8470 0.9352 -0.1239 -0.0424 0.1252  426 PRO C CD  
9133  N  N   . GLU C 426 ? 0.9703 1.1161 1.1864 -0.1250 -0.0572 0.1466  427 GLU C N   
9134  C  CA  . GLU C 426 ? 1.0006 1.1422 1.2054 -0.1230 -0.0536 0.1460  427 GLU C CA  
9135  C  C   . GLU C 426 ? 0.8735 1.0154 1.0934 -0.1080 -0.0422 0.1419  427 GLU C C   
9136  O  O   . GLU C 426 ? 0.8947 1.0433 1.1387 -0.0993 -0.0404 0.1443  427 GLU C O   
9137  C  CB  . GLU C 426 ? 1.1095 1.2576 1.3183 -0.1291 -0.0671 0.1602  427 GLU C CB  
9138  C  CG  . GLU C 426 ? 1.2111 1.3526 1.3884 -0.1450 -0.0739 0.1612  427 GLU C CG  
9139  C  CD  . GLU C 426 ? 1.2725 1.4057 1.4301 -0.1444 -0.0646 0.1547  427 GLU C CD  
9140  O  OE1 . GLU C 426 ? 1.2722 1.4044 1.4405 -0.1314 -0.0533 0.1489  427 GLU C OE1 
9141  O  OE2 . GLU C 426 ? 1.3175 1.4451 1.4481 -0.1578 -0.0686 0.1554  427 GLU C OE2 
9142  N  N   . VAL C 427 ? 0.7221 0.8569 0.9273 -0.1059 -0.0343 0.1354  428 VAL C N   
9143  C  CA  . VAL C 427 ? 0.6603 0.7949 0.8772 -0.0932 -0.0246 0.1319  428 VAL C CA  
9144  C  C   . VAL C 427 ? 0.5723 0.7144 0.8085 -0.0881 -0.0295 0.1425  428 VAL C C   
9145  O  O   . VAL C 427 ? 0.6005 0.7442 0.8322 -0.0947 -0.0383 0.1509  428 VAL C O   
9146  C  CB  . VAL C 427 ? 0.6602 0.7859 0.8581 -0.0929 -0.0154 0.1227  428 VAL C CB  
9147  C  CG1 . VAL C 427 ? 0.6176 0.7428 0.8276 -0.0804 -0.0056 0.1180  428 VAL C CG1 
9148  C  CG2 . VAL C 427 ? 0.6646 0.7819 0.8431 -0.0999 -0.0112 0.1126  428 VAL C CG2 
9149  N  N   . MET C 428 ? 0.5536 0.6996 0.8111 -0.0772 -0.0239 0.1420  429 MET C N   
9150  C  CA  . MET C 428 ? 0.5151 0.6672 0.7943 -0.0713 -0.0264 0.1502  429 MET C CA  
9151  C  C   . MET C 428 ? 0.5321 0.6795 0.8027 -0.0696 -0.0237 0.1502  429 MET C C   
9152  O  O   . MET C 428 ? 0.5091 0.6495 0.7608 -0.0702 -0.0168 0.1419  429 MET C O   
9153  C  CB  . MET C 428 ? 0.6005 0.7565 0.9020 -0.0612 -0.0185 0.1472  429 MET C CB  
9154  C  CG  . MET C 428 ? 0.6427 0.8051 0.9581 -0.0626 -0.0209 0.1489  429 MET C CG  
9155  S  SD  . MET C 428 ? 0.5961 0.7698 0.9357 -0.0668 -0.0349 0.1634  429 MET C SD  
9156  C  CE  . MET C 428 ? 0.9551 1.1267 1.2710 -0.0810 -0.0460 0.1654  429 MET C CE  
9157  N  N   . GLY C 429 ? 0.5444 0.6959 0.8309 -0.0676 -0.0292 0.1597  430 GLY C N   
9158  C  CA  . GLY C 429 ? 0.4861 0.6334 0.7686 -0.0650 -0.0263 0.1603  430 GLY C CA  
9159  C  C   . GLY C 429 ? 0.4369 0.5825 0.7294 -0.0542 -0.0143 0.1523  430 GLY C C   
9160  O  O   . GLY C 429 ? 0.4227 0.5710 0.7276 -0.0489 -0.0093 0.1482  430 GLY C O   
9161  N  N   . ASP C 430 ? 0.4562 0.5970 0.7419 -0.0520 -0.0098 0.1502  431 ASP C N   
9162  C  CA  . ASP C 430 ? 0.4295 0.5680 0.7223 -0.0432 0.0005  0.1429  431 ASP C CA  
9163  C  C   . ASP C 430 ? 0.4215 0.5632 0.7406 -0.0367 0.0009  0.1478  431 ASP C C   
9164  O  O   . ASP C 430 ? 0.4204 0.5649 0.7523 -0.0384 -0.0073 0.1579  431 ASP C O   
9165  C  CB  . ASP C 430 ? 0.5225 0.6551 0.7993 -0.0440 0.0051  0.1388  431 ASP C CB  
9166  C  CG  . ASP C 430 ? 0.5852 0.7143 0.8387 -0.0501 0.0067  0.1327  431 ASP C CG  
9167  O  OD1 . ASP C 430 ? 0.6183 0.7477 0.8686 -0.0505 0.0083  0.1278  431 ASP C OD1 
9168  O  OD2 . ASP C 430 ? 0.6087 0.7345 0.8479 -0.0548 0.0072  0.1324  431 ASP C OD2 
9169  N  N   . GLY C 431 ? 0.4258 0.5666 0.7533 -0.0299 0.0104  0.1405  432 GLY C N   
9170  C  CA  . GLY C 431 ? 0.3556 0.4978 0.7070 -0.0238 0.0138  0.1422  432 GLY C CA  
9171  C  C   . GLY C 431 ? 0.3694 0.5177 0.7413 -0.0212 0.0158  0.1423  432 GLY C C   
9172  O  O   . GLY C 431 ? 0.3529 0.5059 0.7238 -0.0248 0.0109  0.1447  432 GLY C O   
9173  N  N   . LEU C 432 ? 0.4480 0.5962 0.8388 -0.0154 0.0237  0.1391  433 LEU C N   
9174  C  CA  . LEU C 432 ? 0.4336 0.5877 0.8460 -0.0128 0.0285  0.1377  433 LEU C CA  
9175  C  C   . LEU C 432 ? 0.4428 0.6054 0.8771 -0.0143 0.0185  0.1485  433 LEU C C   
9176  O  O   . LEU C 432 ? 0.3918 0.5606 0.8314 -0.0164 0.0171  0.1491  433 LEU C O   
9177  C  CB  . LEU C 432 ? 0.4313 0.5825 0.8604 -0.0071 0.0398  0.1318  433 LEU C CB  
9178  C  CG  . LEU C 432 ? 0.4065 0.5631 0.8581 -0.0047 0.0484  0.1279  433 LEU C CG  
9179  C  CD1 . LEU C 432 ? 0.3857 0.5431 0.8199 -0.0079 0.0532  0.1212  433 LEU C CD1 
9180  C  CD2 . LEU C 432 ? 0.3819 0.5339 0.8483 -0.0001 0.0606  0.1211  433 LEU C CD2 
9181  N  N   . ALA C 433 ? 0.4780 0.6406 0.9251 -0.0138 0.0107  0.1578  434 ALA C N   
9182  C  CA  . ALA C 433 ? 0.4881 0.6588 0.9593 -0.0155 -0.0008 0.1702  434 ALA C CA  
9183  C  C   . ALA C 433 ? 0.5331 0.7081 0.9882 -0.0236 -0.0117 0.1752  434 ALA C C   
9184  O  O   . ALA C 433 ? 0.5560 0.7398 1.0299 -0.0252 -0.0176 0.1811  434 ALA C O   
9185  C  CB  . ALA C 433 ? 0.3645 0.5324 0.8462 -0.0151 -0.0092 0.1806  434 ALA C CB  
9186  N  N   . ASN C 434 ? 0.4868 0.6557 0.9081 -0.0290 -0.0136 0.1721  435 ASN C N   
9187  C  CA  . ASN C 434 ? 0.4957 0.6666 0.8982 -0.0378 -0.0229 0.1753  435 ASN C CA  
9188  C  C   . ASN C 434 ? 0.3664 0.5402 0.7655 -0.0384 -0.0177 0.1680  435 ASN C C   
9189  O  O   . ASN C 434 ? 0.4265 0.6016 0.8118 -0.0458 -0.0246 0.1696  435 ASN C O   
9190  C  CB  . ASN C 434 ? 0.4420 0.6046 0.8105 -0.0434 -0.0241 0.1724  435 ASN C CB  
9191  C  CG  . ASN C 434 ? 0.4663 0.6270 0.8330 -0.0477 -0.0340 0.1832  435 ASN C CG  
9192  O  OD1 . ASN C 434 ? 0.4732 0.6392 0.8569 -0.0507 -0.0457 0.1954  435 ASN C OD1 
9193  N  ND2 . ASN C 434 ? 0.3986 0.5517 0.7455 -0.0485 -0.0300 0.1793  435 ASN C ND2 
9194  N  N   . GLN C 435 ? 0.3570 0.5313 0.7676 -0.0317 -0.0056 0.1600  436 GLN C N   
9195  C  CA  . GLN C 435 ? 0.3533 0.5296 0.7600 -0.0326 0.0000  0.1533  436 GLN C CA  
9196  C  C   . GLN C 435 ? 0.3506 0.5371 0.7885 -0.0310 0.0004  0.1569  436 GLN C C   
9197  O  O   . GLN C 435 ? 0.5640 0.7526 1.0028 -0.0312 0.0071  0.1512  436 GLN C O   
9198  C  CB  . GLN C 435 ? 0.4134 0.5828 0.8074 -0.0284 0.0133  0.1417  436 GLN C CB  
9199  C  CG  . GLN C 435 ? 0.3483 0.5087 0.7165 -0.0289 0.0142  0.1376  436 GLN C CG  
9200  C  CD  . GLN C 435 ? 0.4220 0.5798 0.7680 -0.0360 0.0063  0.1391  436 GLN C CD  
9201  O  OE1 . GLN C 435 ? 0.3567 0.5155 0.6961 -0.0398 0.0049  0.1373  436 GLN C OE1 
9202  N  NE2 . GLN C 435 ? 0.4206 0.5747 0.7545 -0.0384 0.0018  0.1419  436 GLN C NE2 
9203  N  N   . ILE C 436 ? 0.5186 0.7115 0.9834 -0.0295 -0.0066 0.1667  437 ILE C N   
9204  C  CA  . ILE C 436 ? 0.5293 0.7332 1.0295 -0.0274 -0.0059 0.1705  437 ILE C CA  
9205  C  C   . ILE C 436 ? 0.4138 0.6244 0.9114 -0.0345 -0.0134 0.1737  437 ILE C C   
9206  O  O   . ILE C 436 ? 0.3933 0.6107 0.9077 -0.0337 -0.0071 0.1707  437 ILE C O   
9207  C  CB  . ILE C 436 ? 0.3543 0.5638 0.8872 -0.0245 -0.0143 0.1823  437 ILE C CB  
9208  C  CG1 . ILE C 436 ? 0.3927 0.6149 0.9671 -0.0220 -0.0134 0.1865  437 ILE C CG1 
9209  C  CG2 . ILE C 436 ? 0.3643 0.5730 0.8839 -0.0318 -0.0323 0.1944  437 ILE C CG2 
9210  C  CD1 . ILE C 436 ? 0.3562 0.5845 0.9683 -0.0186 -0.0224 0.1990  437 ILE C CD1 
9211  N  N   . ASN C 437 ? 0.4692 0.6774 0.9445 -0.0424 -0.0261 0.1792  438 ASN C N   
9212  C  CA  . ASN C 437 ? 0.5591 0.7720 1.0279 -0.0508 -0.0344 0.1820  438 ASN C CA  
9213  C  C   . ASN C 437 ? 0.5632 0.7674 0.9982 -0.0546 -0.0287 0.1715  438 ASN C C   
9214  O  O   . ASN C 437 ? 0.5899 0.7955 1.0153 -0.0623 -0.0352 0.1726  438 ASN C O   
9215  C  CB  . ASN C 437 ? 0.6151 0.8304 1.0802 -0.0592 -0.0527 0.1946  438 ASN C CB  
9216  C  CG  . ASN C 437 ? 0.6614 0.8863 1.1645 -0.0562 -0.0612 0.2075  438 ASN C CG  
9217  O  OD1 . ASN C 437 ? 0.6373 0.8699 1.1747 -0.0490 -0.0541 0.2070  438 ASN C OD1 
9218  N  ND2 . ASN C 437 ? 0.6901 0.9142 1.1878 -0.0622 -0.0762 0.2191  438 ASN C ND2 
9219  N  N   . ASN C 438 ? 0.5407 0.7357 0.9589 -0.0496 -0.0173 0.1618  439 ASN C N   
9220  C  CA  . ASN C 438 ? 0.5021 0.6880 0.8903 -0.0524 -0.0124 0.1526  439 ASN C CA  
9221  C  C   . ASN C 438 ? 0.4572 0.6461 0.8485 -0.0553 -0.0095 0.1494  439 ASN C C   
9222  O  O   . ASN C 438 ? 0.4187 0.6118 0.8269 -0.0511 -0.0007 0.1466  439 ASN C O   
9223  C  CB  . ASN C 438 ? 0.4881 0.6657 0.8652 -0.0457 -0.0007 0.1440  439 ASN C CB  
9224  C  CG  . ASN C 438 ? 0.5255 0.6931 0.8733 -0.0482 0.0024  0.1362  439 ASN C CG  
9225  O  OD1 . ASN C 438 ? 0.5002 0.6665 0.8407 -0.0520 0.0027  0.1332  439 ASN C OD1 
9226  N  ND2 . ASN C 438 ? 0.5066 0.6671 0.8394 -0.0460 0.0048  0.1328  439 ASN C ND2 
9227  N  N   . PRO C 439 ? 0.4339 0.6200 0.8078 -0.0634 -0.0164 0.1494  440 PRO C N   
9228  C  CA  . PRO C 439 ? 0.4851 0.6738 0.8615 -0.0678 -0.0158 0.1477  440 PRO C CA  
9229  C  C   . PRO C 439 ? 0.5284 0.7101 0.8950 -0.0646 -0.0038 0.1384  440 PRO C C   
9230  O  O   . PRO C 439 ? 0.5730 0.7595 0.9519 -0.0652 0.0005  0.1376  440 PRO C O   
9231  C  CB  . PRO C 439 ? 0.3842 0.5682 0.7393 -0.0777 -0.0261 0.1488  440 PRO C CB  
9232  C  CG  . PRO C 439 ? 0.4124 0.5872 0.7454 -0.0772 -0.0261 0.1460  440 PRO C CG  
9233  C  CD  . PRO C 439 ? 0.3804 0.5597 0.7297 -0.0697 -0.0243 0.1503  440 PRO C CD  
9234  N  N   . GLU C 440 ? 0.4894 0.6604 0.8348 -0.0619 0.0010  0.1320  441 GLU C N   
9235  C  CA  . GLU C 440 ? 0.4401 0.6036 0.7743 -0.0601 0.0098  0.1246  441 GLU C CA  
9236  C  C   . GLU C 440 ? 0.4404 0.6053 0.7845 -0.0536 0.0202  0.1220  441 GLU C C   
9237  O  O   . GLU C 440 ? 0.4898 0.6506 0.8285 -0.0534 0.0271  0.1178  441 GLU C O   
9238  C  CB  . GLU C 440 ? 0.4504 0.6020 0.7600 -0.0605 0.0100  0.1192  441 GLU C CB  
9239  C  CG  . GLU C 440 ? 0.4683 0.6172 0.7652 -0.0675 0.0013  0.1203  441 GLU C CG  
9240  C  CD  . GLU C 440 ? 0.4847 0.6348 0.7818 -0.0752 -0.0037 0.1215  441 GLU C CD  
9241  O  OE1 . GLU C 440 ? 0.4776 0.6274 0.7798 -0.0749 0.0006  0.1197  441 GLU C OE1 
9242  O  OE2 . GLU C 440 ? 0.5208 0.6718 0.8118 -0.0825 -0.0123 0.1244  441 GLU C OE2 
9243  N  N   . VAL C 441 ? 0.4599 0.6299 0.8179 -0.0490 0.0211  0.1247  442 VAL C N   
9244  C  CA  . VAL C 441 ? 0.5168 0.6871 0.8834 -0.0434 0.0316  0.1211  442 VAL C CA  
9245  C  C   . VAL C 441 ? 0.5449 0.7254 0.9404 -0.0404 0.0324  0.1257  442 VAL C C   
9246  O  O   . VAL C 441 ? 0.5708 0.7548 0.9748 -0.0398 0.0244  0.1318  442 VAL C O   
9247  C  CB  . VAL C 441 ? 0.4039 0.5657 0.7551 -0.0393 0.0345  0.1171  442 VAL C CB  
9248  C  CG1 . VAL C 441 ? 0.3437 0.5039 0.6985 -0.0357 0.0458  0.1121  442 VAL C CG1 
9249  C  CG2 . VAL C 441 ? 0.3488 0.5012 0.6755 -0.0416 0.0320  0.1137  442 VAL C CG2 
9250  N  N   . GLU C 442 ? 0.6204 0.8054 1.0316 -0.0390 0.0424  0.1228  443 GLU C N   
9251  C  CA  . GLU C 442 ? 0.6785 0.8727 1.1209 -0.0352 0.0456  0.1257  443 GLU C CA  
9252  C  C   . GLU C 442 ? 0.6624 0.8512 1.1046 -0.0296 0.0543  0.1206  443 GLU C C   
9253  O  O   . GLU C 442 ? 0.6385 0.8223 1.0717 -0.0294 0.0656  0.1130  443 GLU C O   
9254  C  CB  . GLU C 442 ? 0.7709 0.9737 1.2340 -0.0372 0.0533  0.1244  443 GLU C CB  
9255  C  CG  . GLU C 442 ? 0.8654 1.0804 1.3534 -0.0398 0.0439  0.1330  443 GLU C CG  
9256  C  CD  . GLU C 442 ? 0.9439 1.1676 1.4658 -0.0347 0.0418  0.1388  443 GLU C CD  
9257  O  OE1 . GLU C 442 ? 0.9849 1.2101 1.5250 -0.0298 0.0544  0.1339  443 GLU C OE1 
9258  O  OE2 . GLU C 442 ? 0.9700 1.1985 1.5005 -0.0360 0.0276  0.1484  443 GLU C OE2 
9259  N  N   . VAL C 443 ? 0.6363 0.8254 1.0873 -0.0259 0.0484  0.1254  444 VAL C N   
9260  C  CA  . VAL C 443 ? 0.6433 0.8268 1.0956 -0.0208 0.0556  0.1212  444 VAL C CA  
9261  C  C   . VAL C 443 ? 0.6070 0.7977 1.0940 -0.0164 0.0545  0.1268  444 VAL C C   
9262  O  O   . VAL C 443 ? 0.6385 0.8358 1.1393 -0.0173 0.0425  0.1366  444 VAL C O   
9263  C  CB  . VAL C 443 ? 0.4747 0.6488 0.9003 -0.0206 0.0500  0.1209  444 VAL C CB  
9264  C  CG1 . VAL C 443 ? 0.4778 0.6499 0.8814 -0.0258 0.0406  0.1233  444 VAL C CG1 
9265  C  CG2 . VAL C 443 ? 0.4773 0.6516 0.9150 -0.0172 0.0440  0.1270  444 VAL C CG2 
9266  N  N   . ASP C 444 ? 0.5977 0.7870 1.0996 -0.0121 0.0671  0.1206  445 ASP C N   
9267  C  CA  . ASP C 444 ? 0.6067 0.8011 1.1444 -0.0069 0.0675  0.1250  445 ASP C CA  
9268  C  C   . ASP C 444 ? 0.5759 0.7616 1.1069 -0.0034 0.0655  0.1256  445 ASP C C   
9269  O  O   . ASP C 444 ? 0.5732 0.7496 1.0839 -0.0031 0.0739  0.1170  445 ASP C O   
9270  C  CB  . ASP C 444 ? 0.6533 0.8516 1.2164 -0.0047 0.0842  0.1171  445 ASP C CB  
9271  C  CG  . ASP C 444 ? 0.7194 0.9226 1.3244 0.0015  0.0858  0.1210  445 ASP C CG  
9272  O  OD1 . ASP C 444 ? 0.7402 0.9538 1.3728 0.0023  0.0754  0.1317  445 ASP C OD1 
9273  O  OD2 . ASP C 444 ? 0.7304 0.9268 1.3415 0.0053  0.0971  0.1137  445 ASP C OD2 
9274  N  N   . ILE C 445 ? 0.5460 0.7350 1.0942 -0.0015 0.0535  0.1366  446 ILE C N   
9275  C  CA  . ILE C 445 ? 0.5039 0.6848 1.0443 0.0006  0.0489  0.1394  446 ILE C CA  
9276  C  C   . ILE C 445 ? 0.5015 0.6788 1.0671 0.0068  0.0599  0.1349  446 ILE C C   
9277  O  O   . ILE C 445 ? 0.5426 0.7121 1.1035 0.0088  0.0583  0.1359  446 ILE C O   
9278  C  CB  . ILE C 445 ? 0.4524 0.6372 0.9980 -0.0017 0.0306  0.1540  446 ILE C CB  
9279  C  CG1 . ILE C 445 ? 0.4025 0.5977 0.9920 0.0012  0.0258  0.1634  446 ILE C CG1 
9280  C  CG2 . ILE C 445 ? 0.5162 0.7031 1.0351 -0.0088 0.0211  0.1568  446 ILE C CG2 
9281  C  CD1 . ILE C 445 ? 0.3524 0.5524 0.9464 -0.0031 0.0058  0.1794  446 ILE C CD1 
9282  N  N   . THR C 446 ? 0.4880 0.6706 1.0806 0.0094  0.0718  0.1294  447 THR C N   
9283  C  CA  . THR C 446 ? 0.5396 0.7186 1.1598 0.0150  0.0842  0.1236  447 THR C CA  
9284  C  C   . THR C 446 ? 0.5850 0.7541 1.1834 0.0138  0.1016  0.1077  447 THR C C   
9285  O  O   . THR C 446 ? 0.6506 0.8150 1.2671 0.0171  0.1146  0.1000  447 THR C O   
9286  C  CB  . THR C 446 ? 0.4375 0.6277 1.1040 0.0185  0.0896  0.1254  447 THR C CB  
9287  O  OG1 . THR C 446 ? 0.3539 0.5475 1.0154 0.0154  0.1036  0.1146  447 THR C OG1 
9288  C  CG2 . THR C 446 ? 0.3503 0.5518 1.0353 0.0176  0.0709  0.1416  447 THR C CG2 
9289  N  N   . LYS C 447 ? 0.6402 0.8059 1.2002 0.0083  0.1014  0.1032  448 LYS C N   
9290  C  CA  . LYS C 447 ? 0.6894 0.8452 1.2230 0.0055  0.1141  0.0903  448 LYS C CA  
9291  C  C   . LYS C 447 ? 0.7166 0.8651 1.2147 0.0031  0.1044  0.0924  448 LYS C C   
9292  O  O   . LYS C 447 ? 0.7267 0.8762 1.1999 -0.0010 0.0986  0.0936  448 LYS C O   
9293  C  CB  . LYS C 447 ? 0.7049 0.8639 1.2286 0.0004  0.1243  0.0826  448 LYS C CB  
9294  C  CG  . LYS C 447 ? 1.0153 1.1648 1.5017 -0.0057 0.1327  0.0721  448 LYS C CG  
9295  C  CD  . LYS C 447 ? 1.0193 1.1571 1.4914 -0.0055 0.1373  0.0657  448 LYS C CD  
9296  C  CE  . LYS C 447 ? 1.0147 1.1447 1.4517 -0.0129 0.1441  0.0568  448 LYS C CE  
9297  N  NZ  . LYS C 447 ? 0.9994 1.1304 1.4096 -0.0161 0.1320  0.0626  448 LYS C NZ  
9298  N  N   . PRO C 448 ? 0.6935 0.8348 1.1917 0.0057  0.1024  0.0934  449 PRO C N   
9299  C  CA  . PRO C 448 ? 0.7039 0.8372 1.1701 0.0033  0.0978  0.0922  449 PRO C CA  
9300  C  C   . PRO C 448 ? 0.6918 0.8173 1.1368 -0.0004 0.1099  0.0798  449 PRO C C   
9301  O  O   . PRO C 448 ? 0.7183 0.8406 1.1763 0.0000  0.1230  0.0715  449 PRO C O   
9302  C  CB  . PRO C 448 ? 0.6740 0.8028 1.1537 0.0071  0.0933  0.0973  449 PRO C CB  
9303  C  CG  . PRO C 448 ? 0.6798 0.8155 1.1980 0.0115  0.0911  0.1045  449 PRO C CG  
9304  C  CD  . PRO C 448 ? 0.6848 0.8259 1.2166 0.0113  0.1029  0.0973  449 PRO C CD  
9305  N  N   . ASP C 449 ? 0.6597 0.7819 1.0736 -0.0045 0.1057  0.0785  450 ASP C N   
9306  C  CA  . ASP C 449 ? 0.6461 0.7605 1.0380 -0.0091 0.1144  0.0686  450 ASP C CA  
9307  C  C   . ASP C 449 ? 0.4823 0.5882 0.8766 -0.0078 0.1185  0.0645  450 ASP C C   
9308  O  O   . ASP C 449 ? 0.4828 0.5877 0.8803 -0.0049 0.1102  0.0708  450 ASP C O   
9309  C  CB  . ASP C 449 ? 0.6991 0.8123 1.0614 -0.0131 0.1066  0.0702  450 ASP C CB  
9310  C  CG  . ASP C 449 ? 0.7630 0.8685 1.1024 -0.0189 0.1131  0.0619  450 ASP C CG  
9311  O  OD1 . ASP C 449 ? 0.8298 0.9289 1.1620 -0.0194 0.1135  0.0592  450 ASP C OD1 
9312  O  OD2 . ASP C 449 ? 0.7726 0.8785 1.1006 -0.0237 0.1171  0.0587  450 ASP C OD2 
9313  N  N   . MET C 450 ? 0.4765 0.5759 0.8685 -0.0110 0.1316  0.0539  451 MET C N   
9314  C  CA  . MET C 450 ? 0.5378 0.6283 0.9350 -0.0102 0.1372  0.0487  451 MET C CA  
9315  C  C   . MET C 450 ? 0.5117 0.5958 0.8828 -0.0136 0.1308  0.0486  451 MET C C   
9316  O  O   . MET C 450 ? 0.5209 0.6004 0.8976 -0.0113 0.1282  0.0502  451 MET C O   
9317  C  CB  . MET C 450 ? 0.5531 0.6378 0.9552 -0.0137 0.1547  0.0358  451 MET C CB  
9318  C  CG  . MET C 450 ? 0.6190 0.7076 1.0588 -0.0082 0.1633  0.0348  451 MET C CG  
9319  S  SD  . MET C 450 ? 1.2855 1.3729 1.7577 0.0008  0.1563  0.0433  451 MET C SD  
9320  C  CE  . MET C 450 ? 0.5445 0.6463 1.0350 0.0059  0.1415  0.0589  451 MET C CE  
9321  N  N   . THR C 451 ? 0.4671 0.5512 0.8115 -0.0192 0.1281  0.0471  452 THR C N   
9322  C  CA  . THR C 451 ? 0.5029 0.5828 0.8250 -0.0225 0.1211  0.0479  452 THR C CA  
9323  C  C   . THR C 451 ? 0.5213 0.6051 0.8493 -0.0174 0.1093  0.0576  452 THR C C   
9324  O  O   . THR C 451 ? 0.6079 0.6873 0.9339 -0.0172 0.1067  0.0581  452 THR C O   
9325  C  CB  . THR C 451 ? 0.5009 0.5819 0.7981 -0.0285 0.1176  0.0475  452 THR C CB  
9326  O  OG1 . THR C 451 ? 0.4946 0.5714 0.7833 -0.0350 0.1286  0.0389  452 THR C OG1 
9327  C  CG2 . THR C 451 ? 0.4953 0.5730 0.7740 -0.0316 0.1100  0.0487  452 THR C CG2 
9328  N  N   . ILE C 452 ? 0.5173 0.6092 0.8517 -0.0143 0.1026  0.0649  453 ILE C N   
9329  C  CA  . ILE C 452 ? 0.5145 0.6103 0.8537 -0.0108 0.0922  0.0741  453 ILE C CA  
9330  C  C   . ILE C 452 ? 0.5408 0.6335 0.8989 -0.0073 0.0926  0.0768  453 ILE C C   
9331  O  O   . ILE C 452 ? 0.5482 0.6389 0.9023 -0.0071 0.0868  0.0809  453 ILE C O   
9332  C  CB  . ILE C 452 ? 0.4631 0.5672 0.8089 -0.0091 0.0865  0.0806  453 ILE C CB  
9333  C  CG1 . ILE C 452 ? 0.4142 0.5204 0.7416 -0.0126 0.0849  0.0789  453 ILE C CG1 
9334  C  CG2 . ILE C 452 ? 0.4475 0.5547 0.7971 -0.0071 0.0763  0.0898  453 ILE C CG2 
9335  C  CD1 . ILE C 452 ? 0.4010 0.5064 0.7107 -0.0140 0.0775  0.0811  453 ILE C CD1 
9336  N  N   . ARG C 453 ? 0.5735 0.6656 0.9534 -0.0046 0.0999  0.0746  454 ARG C N   
9337  C  CA  . ARG C 453 ? 0.6408 0.7292 1.0432 -0.0008 0.1007  0.0774  454 ARG C CA  
9338  C  C   . ARG C 453 ? 0.6317 0.7104 1.0251 -0.0029 0.1038  0.0724  454 ARG C C   
9339  O  O   . ARG C 453 ? 0.6660 0.7421 1.0640 -0.0015 0.0977  0.0786  454 ARG C O   
9340  C  CB  . ARG C 453 ? 0.6633 0.7521 1.0927 0.0023  0.1106  0.0734  454 ARG C CB  
9341  C  CG  . ARG C 453 ? 0.7065 0.8056 1.1546 0.0054  0.1053  0.0815  454 ARG C CG  
9342  C  CD  . ARG C 453 ? 0.7861 0.8885 1.2418 0.0076  0.0912  0.0949  454 ARG C CD  
9343  N  NE  . ARG C 453 ? 0.8414 0.9540 1.3086 0.0086  0.0834  0.1036  454 ARG C NE  
9344  C  CZ  . ARG C 453 ? 0.9207 1.0374 1.3881 0.0081  0.0698  0.1156  454 ARG C CZ  
9345  N  NH1 . ARG C 453 ? 0.9429 1.0544 1.3999 0.0068  0.0633  0.1203  454 ARG C NH1 
9346  N  NH2 . ARG C 453 ? 0.9336 1.0594 1.4107 0.0078  0.0627  0.1228  454 ARG C NH2 
9347  N  N   . GLN C 454 ? 0.6375 0.7106 1.0169 -0.0072 0.1129  0.0616  455 GLN C N   
9348  C  CA  . GLN C 454 ? 0.6799 0.7436 1.0494 -0.0105 0.1159  0.0559  455 GLN C CA  
9349  C  C   . GLN C 454 ? 0.5810 0.6463 0.9331 -0.0123 0.1052  0.0619  455 GLN C C   
9350  O  O   . GLN C 454 ? 0.5592 0.6194 0.9132 -0.0125 0.1031  0.0635  455 GLN C O   
9351  C  CB  . GLN C 454 ? 0.7620 0.8198 1.1152 -0.0170 0.1263  0.0436  455 GLN C CB  
9352  C  CG  . GLN C 454 ? 0.8458 0.8925 1.1924 -0.0211 0.1312  0.0364  455 GLN C CG  
9353  C  CD  . GLN C 454 ? 0.9150 0.9558 1.2878 -0.0161 0.1345  0.0375  455 GLN C CD  
9354  O  OE1 . GLN C 454 ? 0.9091 0.9457 1.2816 -0.0160 0.1293  0.0410  455 GLN C OE1 
9355  N  NE2 . GLN C 454 ? 0.9234 0.9639 1.3207 -0.0119 0.1431  0.0347  455 GLN C NE2 
9356  N  N   . GLN C 455 ? 0.5445 0.6168 0.8815 -0.0137 0.0989  0.0651  456 GLN C N   
9357  C  CA  . GLN C 455 ? 0.5241 0.5989 0.8474 -0.0151 0.0899  0.0701  456 GLN C CA  
9358  C  C   . GLN C 455 ? 0.5292 0.6061 0.8640 -0.0119 0.0831  0.0794  456 GLN C C   
9359  O  O   . GLN C 455 ? 0.5152 0.5902 0.8445 -0.0135 0.0794  0.0819  456 GLN C O   
9360  C  CB  . GLN C 455 ? 0.5284 0.6098 0.8371 -0.0166 0.0853  0.0714  456 GLN C CB  
9361  C  CG  . GLN C 455 ? 0.5244 0.6032 0.8189 -0.0213 0.0900  0.0640  456 GLN C CG  
9362  C  CD  . GLN C 455 ? 0.5334 0.6041 0.8206 -0.0259 0.0945  0.0573  456 GLN C CD  
9363  O  OE1 . GLN C 455 ? 0.4569 0.5266 0.7367 -0.0279 0.0898  0.0585  456 GLN C OE1 
9364  N  NE2 . GLN C 455 ? 0.6313 0.6960 0.9208 -0.0283 0.1043  0.0495  456 GLN C NE2 
9365  N  N   . ILE C 456 ? 0.4895 0.5703 0.8402 -0.0082 0.0812  0.0851  457 ILE C N   
9366  C  CA  . ILE C 456 ? 0.4946 0.5768 0.8567 -0.0063 0.0739  0.0952  457 ILE C CA  
9367  C  C   . ILE C 456 ? 0.4774 0.5511 0.8506 -0.0058 0.0765  0.0951  457 ILE C C   
9368  O  O   . ILE C 456 ? 0.5322 0.6042 0.9022 -0.0074 0.0708  0.1011  457 ILE C O   
9369  C  CB  . ILE C 456 ? 0.5069 0.5946 0.8876 -0.0030 0.0710  0.1016  457 ILE C CB  
9370  C  CG1 . ILE C 456 ? 0.5118 0.6075 0.8809 -0.0042 0.0672  0.1028  457 ILE C CG1 
9371  C  CG2 . ILE C 456 ? 0.4539 0.5415 0.8472 -0.0022 0.0625  0.1132  457 ILE C CG2 
9372  C  CD1 . ILE C 456 ? 0.5318 0.6339 0.9183 -0.0020 0.0632  0.1095  457 ILE C CD1 
9373  N  N   . MET C 457 ? 0.4938 0.5616 0.8796 -0.0042 0.0858  0.0878  458 MET C N   
9374  C  CA  . MET C 457 ? 0.4831 0.5410 0.8802 -0.0039 0.0898  0.0857  458 MET C CA  
9375  C  C   . MET C 457 ? 0.4539 0.5075 0.8313 -0.0088 0.0883  0.0832  458 MET C C   
9376  O  O   . MET C 457 ? 0.4573 0.5066 0.8391 -0.0094 0.0845  0.0886  458 MET C O   
9377  C  CB  . MET C 457 ? 0.4655 0.5168 0.8747 -0.0029 0.1027  0.0747  458 MET C CB  
9378  N  N   . GLN C 458 ? 0.4672 0.5223 0.8241 -0.0126 0.0907  0.0759  459 GLN C N   
9379  C  CA  . GLN C 458 ? 0.4791 0.5319 0.8190 -0.0175 0.0887  0.0736  459 GLN C CA  
9380  C  C   . GLN C 458 ? 0.4669 0.5250 0.8024 -0.0179 0.0796  0.0832  459 GLN C C   
9381  O  O   . GLN C 458 ? 0.5601 0.6142 0.8944 -0.0203 0.0780  0.0850  459 GLN C O   
9382  C  CB  . GLN C 458 ? 0.4992 0.5548 0.8196 -0.0215 0.0902  0.0667  459 GLN C CB  
9383  C  CG  . GLN C 458 ? 0.5661 0.6162 0.8853 -0.0235 0.0998  0.0567  459 GLN C CG  
9384  C  CD  . GLN C 458 ? 0.6257 0.6647 0.9441 -0.0277 0.1066  0.0486  459 GLN C CD  
9385  O  OE1 . GLN C 458 ? 0.6433 0.6760 0.9767 -0.0256 0.1084  0.0499  459 GLN C OE1 
9386  N  NE2 . GLN C 458 ? 0.6758 0.7114 0.9759 -0.0346 0.1098  0.0405  459 GLN C NE2 
9387  N  N   . LEU C 459 ? 0.4962 0.5629 0.8286 -0.0163 0.0743  0.0887  460 LEU C N   
9388  C  CA  . LEU C 459 ? 0.4347 0.5062 0.7615 -0.0176 0.0670  0.0970  460 LEU C CA  
9389  C  C   . LEU C 459 ? 0.4377 0.5045 0.7767 -0.0175 0.0639  0.1048  460 LEU C C   
9390  O  O   . LEU C 459 ? 0.4522 0.5181 0.7850 -0.0210 0.0611  0.1084  460 LEU C O   
9391  C  CB  . LEU C 459 ? 0.3936 0.4732 0.7173 -0.0163 0.0627  0.1012  460 LEU C CB  
9392  C  CG  . LEU C 459 ? 0.3648 0.4494 0.6761 -0.0167 0.0639  0.0955  460 LEU C CG  
9393  C  CD1 . LEU C 459 ? 0.3769 0.4681 0.6872 -0.0156 0.0597  0.1000  460 LEU C CD1 
9394  C  CD2 . LEU C 459 ? 0.3633 0.4494 0.6614 -0.0200 0.0631  0.0929  460 LEU C CD2 
9395  N  N   . LYS C 460 ? 0.3878 0.4516 0.7455 -0.0138 0.0646  0.1079  461 LYS C N   
9396  C  CA  . LYS C 460 ? 0.5358 0.5945 0.9082 -0.0134 0.0603  0.1171  461 LYS C CA  
9397  C  C   . LYS C 460 ? 0.4756 0.5246 0.8501 -0.0155 0.0642  0.1137  461 LYS C C   
9398  O  O   . LYS C 460 ? 0.4189 0.4650 0.7930 -0.0185 0.0594  0.1212  461 LYS C O   
9399  C  CB  . LYS C 460 ? 0.5396 0.5975 0.9366 -0.0082 0.0605  0.1207  461 LYS C CB  
9400  C  CG  . LYS C 460 ? 0.6091 0.6634 1.0233 -0.0079 0.0528  0.1336  461 LYS C CG  
9401  C  CD  . LYS C 460 ? 0.7187 0.7771 1.1558 -0.0034 0.0492  0.1403  461 LYS C CD  
9402  C  CE  . LYS C 460 ? 0.7677 0.8232 1.2245 0.0022  0.0601  0.1301  461 LYS C CE  
9403  N  NZ  . LYS C 460 ? 0.8251 0.8865 1.3068 0.0067  0.0570  0.1364  461 LYS C NZ  
9404  N  N   . ILE C 461 ? 0.5259 0.5694 0.9013 -0.0149 0.0729  0.1024  462 ILE C N   
9405  C  CA  . ILE C 461 ? 0.5358 0.5694 0.9116 -0.0178 0.0770  0.0976  462 ILE C CA  
9406  C  C   . ILE C 461 ? 0.5413 0.5777 0.8987 -0.0234 0.0731  0.0990  462 ILE C C   
9407  O  O   . ILE C 461 ? 0.4894 0.5206 0.8495 -0.0262 0.0707  0.1040  462 ILE C O   
9408  C  CB  . ILE C 461 ? 0.5654 0.5931 0.9393 -0.0185 0.0872  0.0838  462 ILE C CB  
9409  C  CG1 . ILE C 461 ? 0.5686 0.5931 0.9633 -0.0132 0.0936  0.0808  462 ILE C CG1 
9410  C  CG2 . ILE C 461 ? 0.5627 0.5799 0.9345 -0.0229 0.0910  0.0783  462 ILE C CG2 
9411  C  CD1 . ILE C 461 ? 0.5753 0.5948 0.9649 -0.0152 0.1049  0.0664  462 ILE C CD1 
9412  N  N   . MET C 462 ? 0.5095 0.5541 0.8502 -0.0252 0.0726  0.0950  463 MET C N   
9413  C  CA  . MET C 462 ? 0.4755 0.5244 0.8019 -0.0300 0.0698  0.0956  463 MET C CA  
9414  C  C   . MET C 462 ? 0.4752 0.5273 0.8014 -0.0317 0.0637  0.1065  463 MET C C   
9415  O  O   . MET C 462 ? 0.4727 0.5236 0.7948 -0.0362 0.0627  0.1087  463 MET C O   
9416  C  CB  . MET C 462 ? 0.4239 0.4817 0.7367 -0.0305 0.0695  0.0909  463 MET C CB  
9417  C  CG  . MET C 462 ? 0.4644 0.5267 0.7667 -0.0352 0.0678  0.0896  463 MET C CG  
9418  S  SD  . MET C 462 ? 0.5141 0.5684 0.8155 -0.0403 0.0709  0.0828  463 MET C SD  
9419  C  CE  . MET C 462 ? 0.4067 0.4587 0.7129 -0.0437 0.0687  0.0903  463 MET C CE  
9420  N  N   . THR C 463 ? 0.4004 0.4565 0.7304 -0.0290 0.0598  0.1133  464 THR C N   
9421  C  CA  . THR C 463 ? 0.4041 0.4624 0.7313 -0.0322 0.0535  0.1241  464 THR C CA  
9422  C  C   . THR C 463 ? 0.4355 0.4845 0.7733 -0.0342 0.0515  0.1311  464 THR C C   
9423  O  O   . THR C 463 ? 0.4214 0.4702 0.7519 -0.0398 0.0488  0.1368  464 THR C O   
9424  C  CB  . THR C 463 ? 0.4016 0.4649 0.7315 -0.0299 0.0485  0.1305  464 THR C CB  
9425  O  OG1 . THR C 463 ? 0.4104 0.4815 0.7301 -0.0285 0.0503  0.1243  464 THR C OG1 
9426  C  CG2 . THR C 463 ? 0.4088 0.4738 0.7321 -0.0353 0.0415  0.1419  464 THR C CG2 
9427  N  N   . ASN C 464 ? 0.4717 0.5128 0.8278 -0.0298 0.0535  0.1304  465 ASN C N   
9428  C  CA  . ASN C 464 ? 0.5286 0.5591 0.8980 -0.0311 0.0520  0.1364  465 ASN C CA  
9429  C  C   . ASN C 464 ? 0.5282 0.5542 0.8891 -0.0362 0.0556  0.1315  465 ASN C C   
9430  O  O   . ASN C 464 ? 0.4819 0.5039 0.8419 -0.0411 0.0520  0.1393  465 ASN C O   
9431  C  CB  . ASN C 464 ? 0.6002 0.6224 0.9932 -0.0249 0.0560  0.1336  465 ASN C CB  
9432  C  CG  . ASN C 464 ? 0.7003 0.7260 1.1090 -0.0205 0.0503  0.1425  465 ASN C CG  
9433  O  OD1 . ASN C 464 ? 0.7697 0.8018 1.1711 -0.0232 0.0418  0.1530  465 ASN C OD1 
9434  N  ND2 . ASN C 464 ? 0.7107 0.7320 1.1412 -0.0143 0.0554  0.1382  465 ASN C ND2 
9435  N  N   . ARG C 465 ? 0.5148 0.5414 0.8691 -0.0360 0.0621  0.1191  466 ARG C N   
9436  C  CA  . ARG C 465 ? 0.5694 0.5932 0.9156 -0.0415 0.0648  0.1139  466 ARG C CA  
9437  C  C   . ARG C 465 ? 0.5555 0.5872 0.8887 -0.0471 0.0610  0.1198  466 ARG C C   
9438  O  O   . ARG C 465 ? 0.5596 0.5871 0.8922 -0.0524 0.0605  0.1230  466 ARG C O   
9439  C  CB  . ARG C 465 ? 0.6124 0.6382 0.9505 -0.0416 0.0702  0.1011  466 ARG C CB  
9440  C  CG  . ARG C 465 ? 0.7055 0.7221 1.0533 -0.0383 0.0765  0.0928  466 ARG C CG  
9441  C  CD  . ARG C 465 ? 0.7913 0.8075 1.1270 -0.0421 0.0810  0.0809  466 ARG C CD  
9442  N  NE  . ARG C 465 ? 0.8798 0.8888 1.2202 -0.0400 0.0883  0.0716  466 ARG C NE  
9443  C  CZ  . ARG C 465 ? 0.9439 0.9500 1.2731 -0.0445 0.0929  0.0608  466 ARG C CZ  
9444  N  NH1 . ARG C 465 ? 0.9665 0.9768 1.2812 -0.0506 0.0895  0.0589  466 ARG C NH1 
9445  N  NH2 . ARG C 465 ? 0.9693 0.9685 1.3019 -0.0435 0.1008  0.0520  466 ARG C NH2 
9446  N  N   . LEU C 466 ? 0.5296 0.5723 0.8527 -0.0464 0.0591  0.1208  467 LEU C N   
9447  C  CA  . LEU C 466 ? 0.4751 0.5258 0.7859 -0.0519 0.0575  0.1243  467 LEU C CA  
9448  C  C   . LEU C 466 ? 0.4775 0.5252 0.7877 -0.0565 0.0529  0.1365  467 LEU C C   
9449  O  O   . LEU C 466 ? 0.4856 0.5354 0.7881 -0.0632 0.0534  0.1393  467 LEU C O   
9450  C  CB  . LEU C 466 ? 0.4802 0.5418 0.7817 -0.0498 0.0575  0.1214  467 LEU C CB  
9451  C  CG  . LEU C 466 ? 0.4719 0.5389 0.7697 -0.0486 0.0610  0.1111  467 LEU C CG  
9452  C  CD1 . LEU C 466 ? 0.4267 0.5003 0.7205 -0.0442 0.0606  0.1082  467 LEU C CD1 
9453  C  CD2 . LEU C 466 ? 0.4039 0.4772 0.6960 -0.0540 0.0626  0.1098  467 LEU C CD2 
9454  N  N   . ARG C 467 ? 0.5287 0.5719 0.8475 -0.0535 0.0482  0.1442  468 ARG C N   
9455  C  CA  . ARG C 467 ? 0.5562 0.5957 0.8745 -0.0587 0.0418  0.1576  468 ARG C CA  
9456  C  C   . ARG C 467 ? 0.5879 0.6165 0.9147 -0.0621 0.0418  0.1615  468 ARG C C   
9457  O  O   . ARG C 467 ? 0.5969 0.6244 0.9153 -0.0701 0.0398  0.1687  468 ARG C O   
9458  C  CB  . ARG C 467 ? 0.6142 0.6523 0.9428 -0.0546 0.0353  0.1658  468 ARG C CB  
9459  C  CG  . ARG C 467 ? 0.6440 0.6925 0.9614 -0.0538 0.0336  0.1649  468 ARG C CG  
9460  C  CD  . ARG C 467 ? 0.7190 0.7669 1.0497 -0.0494 0.0269  0.1724  468 ARG C CD  
9461  N  NE  . ARG C 467 ? 0.7753 0.8323 1.0935 -0.0505 0.0242  0.1728  468 ARG C NE  
9462  C  CZ  . ARG C 467 ? 0.7507 0.8102 1.0783 -0.0469 0.0189  0.1775  468 ARG C CZ  
9463  N  NH1 . ARG C 467 ? 0.8134 0.8674 1.1650 -0.0414 0.0161  0.1822  468 ARG C NH1 
9464  N  NH2 . ARG C 467 ? 0.6823 0.7497 0.9967 -0.0490 0.0166  0.1772  468 ARG C NH2 
9465  N  N   . SER C 468 ? 0.6232 0.6432 0.9661 -0.0568 0.0448  0.1561  469 SER C N   
9466  C  CA  . SER C 468 ? 0.6785 0.6867 1.0306 -0.0598 0.0458  0.1579  469 SER C CA  
9467  C  C   . SER C 468 ? 0.7198 0.7312 1.0589 -0.0667 0.0498  0.1528  469 SER C C   
9468  O  O   . SER C 468 ? 0.7688 0.7753 1.1065 -0.0735 0.0480  0.1597  469 SER C O   
9469  C  CB  . SER C 468 ? 0.7154 0.7138 1.0854 -0.0532 0.0507  0.1495  469 SER C CB  
9470  O  OG  . SER C 468 ? 0.7853 0.7767 1.1752 -0.0483 0.0466  0.1577  469 SER C OG  
9471  N  N   . ALA C 469 ? 0.6401 0.6600 0.9709 -0.0654 0.0547  0.1413  470 ALA C N   
9472  C  CA  . ALA C 469 ? 0.5793 0.6045 0.9009 -0.0715 0.0581  0.1362  470 ALA C CA  
9473  C  C   . ALA C 469 ? 0.5337 0.5659 0.8438 -0.0786 0.0564  0.1442  470 ALA C C   
9474  O  O   . ALA C 469 ? 0.5691 0.6002 0.8769 -0.0858 0.0578  0.1462  470 ALA C O   
9475  C  CB  . ALA C 469 ? 0.5540 0.5884 0.8702 -0.0685 0.0617  0.1247  470 ALA C CB  
9476  N  N   . TYR C 470 ? 0.5415 0.5807 0.8439 -0.0775 0.0539  0.1483  471 TYR C N   
9477  C  CA  . TYR C 470 ? 0.5598 0.6049 0.8486 -0.0854 0.0532  0.1552  471 TYR C CA  
9478  C  C   . TYR C 470 ? 0.6329 0.6683 0.9224 -0.0926 0.0490  0.1675  471 TYR C C   
9479  O  O   . TYR C 470 ? 0.6656 0.7030 0.9462 -0.1016 0.0512  0.1705  471 TYR C O   
9480  C  CB  . TYR C 470 ? 0.5668 0.6184 0.8469 -0.0836 0.0506  0.1577  471 TYR C CB  
9481  C  CG  . TYR C 470 ? 0.5626 0.6188 0.8259 -0.0932 0.0504  0.1642  471 TYR C CG  
9482  C  CD1 . TYR C 470 ? 0.5857 0.6522 0.8388 -0.0972 0.0575  0.1569  471 TYR C CD1 
9483  C  CD2 . TYR C 470 ? 0.5979 0.6479 0.8560 -0.0991 0.0432  0.1777  471 TYR C CD2 
9484  C  CE1 . TYR C 470 ? 0.6093 0.6793 0.8459 -0.1071 0.0594  0.1612  471 TYR C CE1 
9485  C  CE2 . TYR C 470 ? 0.6095 0.6628 0.8486 -0.1099 0.0434  0.1833  471 TYR C CE2 
9486  C  CZ  . TYR C 470 ? 0.6007 0.6639 0.8284 -0.1141 0.0524  0.1743  471 TYR C CZ  
9487  O  OH  . TYR C 470 ? 0.6083 0.6742 0.8160 -0.1258 0.0546  0.1784  471 TYR C OH  
9488  N  N   . ASN C 471 ? 0.7541 0.7791 1.0557 -0.0888 0.0430  0.1749  472 ASN C N   
9489  C  CA  . ASN C 471 ? 0.8653 0.8797 1.1700 -0.0952 0.0374  0.1883  472 ASN C CA  
9490  C  C   . ASN C 471 ? 0.9534 0.9593 1.2659 -0.0984 0.0407  0.1861  472 ASN C C   
9491  O  O   . ASN C 471 ? 0.9728 0.9732 1.2813 -0.1072 0.0385  0.1955  472 ASN C O   
9492  C  CB  . ASN C 471 ? 0.8613 0.8671 1.1815 -0.0894 0.0294  0.1975  472 ASN C CB  
9493  C  CG  . ASN C 471 ? 0.8813 0.8931 1.1915 -0.0914 0.0224  0.2066  472 ASN C CG  
9494  O  OD1 . ASN C 471 ? 0.8983 0.9149 1.1888 -0.1011 0.0212  0.2122  472 ASN C OD1 
9495  N  ND2 . ASN C 471 ? 0.8552 0.8667 1.1787 -0.0831 0.0183  0.2078  472 ASN C ND2 
9496  N  N   . GLY C 472 ? 1.0362 1.0406 1.3583 -0.0923 0.0460  0.1738  473 GLY C N   
9497  C  CA  . GLY C 472 ? 1.1426 1.1371 1.4735 -0.0951 0.0487  0.1707  473 GLY C CA  
9498  C  C   . GLY C 472 ? 1.2486 1.2284 1.5992 -0.0885 0.0467  0.1720  473 GLY C C   
9499  O  O   . GLY C 472 ? 1.2780 1.2522 1.6369 -0.0865 0.0403  0.1833  473 GLY C O   
9500  N  N   . ASN C 473 ? 1.2949 1.2683 1.6540 -0.0857 0.0521  0.1605  474 ASN C N   
9501  C  CA  . ASN C 473 ? 1.3238 1.2836 1.7026 -0.0789 0.0530  0.1581  474 ASN C CA  
9502  C  C   . ASN C 473 ? 1.3300 1.2776 1.7161 -0.0814 0.0585  0.1490  474 ASN C C   
9503  O  O   . ASN C 473 ? 1.3348 1.2722 1.7261 -0.0871 0.0568  0.1554  474 ASN C O   
9504  C  CB  . ASN C 473 ? 1.3320 1.2982 1.7127 -0.0700 0.0557  0.1497  474 ASN C CB  
9505  C  CG  . ASN C 473 ? 1.3483 1.3225 1.7171 -0.0703 0.0619  0.1349  474 ASN C CG  
9506  O  OD1 . ASN C 473 ? 1.3360 1.3240 1.6897 -0.0726 0.0613  0.1338  474 ASN C OD1 
9507  N  ND2 . ASN C 473 ? 1.3554 1.3206 1.7310 -0.0687 0.0678  0.1234  474 ASN C ND2 
9508  N  N   . SER D 28  ? 0.9457 0.9703 1.0758 0.1995  0.1283  0.2411  29  SER D N   
9509  C  CA  . SER D 28  ? 0.9396 0.9671 1.0544 0.2108  0.1320  0.2484  29  SER D CA  
9510  C  C   . SER D 28  ? 0.9405 0.9847 1.0358 0.2159  0.1403  0.2531  29  SER D C   
9511  O  O   . SER D 28  ? 1.0491 1.0935 1.1392 0.2238  0.1488  0.2671  29  SER D O   
9512  C  CB  . SER D 28  ? 0.9821 0.9936 1.1138 0.2138  0.1359  0.2641  29  SER D CB  
9513  O  OG  . SER D 28  ? 0.9855 0.9949 1.1345 0.2090  0.1452  0.2781  29  SER D OG  
9514  N  N   . ARG D 29  ? 0.8068 0.8644 0.8917 0.2122  0.1375  0.2414  30  ARG D N   
9515  C  CA  . ARG D 29  ? 0.7952 0.8685 0.8595 0.2179  0.1411  0.2410  30  ARG D CA  
9516  C  C   . ARG D 29  ? 0.7670 0.8422 0.8297 0.2213  0.1526  0.2549  30  ARG D C   
9517  O  O   . ARG D 29  ? 0.7570 0.8416 0.7997 0.2309  0.1561  0.2577  30  ARG D O   
9518  C  CB  . ARG D 29  ? 0.7130 0.7918 0.7591 0.2291  0.1381  0.2398  30  ARG D CB  
9519  C  CG  . ARG D 29  ? 0.7148 0.7952 0.7602 0.2283  0.1279  0.2270  30  ARG D CG  
9520  C  CD  . ARG D 29  ? 0.7152 0.8046 0.7430 0.2395  0.1251  0.2259  30  ARG D CD  
9521  N  NE  . ARG D 29  ? 0.7289 0.8183 0.7578 0.2410  0.1173  0.2174  30  ARG D NE  
9522  C  CZ  . ARG D 29  ? 0.7430 0.8405 0.7602 0.2500  0.1135  0.2153  30  ARG D CZ  
9523  N  NH1 . ARG D 29  ? 0.7319 0.8373 0.7348 0.2582  0.1155  0.2200  30  ARG D NH1 
9524  N  NH2 . ARG D 29  ? 0.7639 0.8620 0.7834 0.2519  0.1074  0.2083  30  ARG D NH2 
9525  N  N   . SER D 30  ? 0.8433 0.9097 0.9268 0.2144  0.1583  0.2638  31  SER D N   
9526  C  CA  . SER D 30  ? 0.8629 0.9326 0.9467 0.2181  0.1707  0.2783  31  SER D CA  
9527  C  C   . SER D 30  ? 0.7949 0.8747 0.8749 0.2123  0.1710  0.2702  31  SER D C   
9528  O  O   . SER D 30  ? 0.7643 0.8429 0.8561 0.2011  0.1641  0.2590  31  SER D O   
9529  C  CB  . SER D 30  ? 0.9160 0.9725 1.0280 0.2140  0.1776  0.2944  31  SER D CB  
9530  O  OG  . SER D 30  ? 0.9544 1.0156 1.0665 0.2198  0.1916  0.3114  31  SER D OG  
9531  N  N   . CYS D 31  ? 0.8130 0.9025 0.8755 0.2211  0.1785  0.2755  32  CYS D N   
9532  C  CA  A CYS D 31  ? 0.8437 0.9423 0.9013 0.2172  0.1788  0.2681  32  CYS D CA  
9533  C  CA  B CYS D 31  ? 0.8437 0.9424 0.9009 0.2174  0.1789  0.2682  32  CYS D CA  
9534  C  C   . CYS D 31  ? 0.8704 0.9678 0.9413 0.2165  0.1915  0.2829  32  CYS D C   
9535  O  O   . CYS D 31  ? 0.8753 0.9808 0.9380 0.2179  0.1949  0.2808  32  CYS D O   
9536  C  CB  A CYS D 31  ? 0.8288 0.9393 0.8565 0.2282  0.1759  0.2605  32  CYS D CB  
9537  C  CB  B CYS D 31  ? 0.8332 0.9436 0.8604 0.2288  0.1764  0.2613  32  CYS D CB  
9538  S  SG  A CYS D 31  ? 0.8079 0.9246 0.8263 0.2246  0.1594  0.2396  32  CYS D SG  
9539  S  SG  B CYS D 31  ? 0.8119 0.9280 0.8276 0.2276  0.1605  0.2422  32  CYS D SG  
9540  N  N   . GLY D 32  ? 0.8854 0.9727 0.9787 0.2146  0.1981  0.2983  33  GLY D N   
9541  C  CA  . GLY D 32  ? 0.8831 0.9698 0.9949 0.2138  0.2109  0.3153  33  GLY D CA  
9542  C  C   . GLY D 32  ? 0.8515 0.9397 0.9802 0.2010  0.2084  0.3077  33  GLY D C   
9543  O  O   . GLY D 32  ? 0.8406 0.9365 0.9668 0.2036  0.2172  0.3134  33  GLY D O   
9544  N  N   . GLU D 33  ? 0.8505 0.9312 0.9949 0.1882  0.1964  0.2949  34  GLU D N   
9545  C  CA  . GLU D 33  ? 0.8456 0.9265 1.0069 0.1758  0.1924  0.2868  34  GLU D CA  
9546  C  C   . GLU D 33  ? 0.8491 0.9426 0.9886 0.1771  0.1912  0.2750  34  GLU D C   
9547  O  O   . GLU D 33  ? 0.8565 0.9548 1.0026 0.1745  0.1971  0.2781  34  GLU D O   
9548  C  CB  . GLU D 33  ? 0.8787 0.9495 1.0541 0.1651  0.1783  0.2733  34  GLU D CB  
9549  C  CG  . GLU D 33  ? 0.9119 0.9811 1.1061 0.1528  0.1732  0.2655  34  GLU D CG  
9550  C  CD  . GLU D 33  ? 0.9837 1.0407 1.1926 0.1449  0.1597  0.2544  34  GLU D CD  
9551  O  OE1 . GLU D 33  ? 1.0097 1.0584 1.2174 0.1487  0.1551  0.2545  34  GLU D OE1 
9552  O  OE2 . GLU D 33  ? 0.9886 1.0441 1.2091 0.1360  0.1533  0.2454  34  GLU D OE2 
9553  N  N   . VAL D 34  ? 0.8275 0.9262 0.9428 0.1814  0.1833  0.2618  35  VAL D N   
9554  C  CA  . VAL D 34  ? 0.8073 0.9171 0.9028 0.1832  0.1802  0.2500  35  VAL D CA  
9555  C  C   . VAL D 34  ? 0.8845 1.0014 0.9651 0.1951  0.1916  0.2603  35  VAL D C   
9556  O  O   . VAL D 34  ? 0.8939 1.0172 0.9697 0.1944  0.1928  0.2556  35  VAL D O   
9557  C  CB  . VAL D 34  ? 0.7834 0.8978 0.8588 0.1869  0.1695  0.2363  35  VAL D CB  
9558  C  CG1 . VAL D 34  ? 0.7212 0.8466 0.7761 0.1918  0.1667  0.2269  35  VAL D CG1 
9559  C  CG2 . VAL D 34  ? 0.7454 0.8558 0.8331 0.1759  0.1587  0.2244  35  VAL D CG2 
9560  N  N   . ARG D 35  ? 0.8403 0.9560 0.9132 0.2071  0.2002  0.2747  36  ARG D N   
9561  C  CA  . ARG D 35  ? 0.8877 1.0099 0.9447 0.2213  0.2126  0.2868  36  ARG D CA  
9562  C  C   . ARG D 35  ? 0.9175 1.0405 0.9955 0.2164  0.2233  0.2979  36  ARG D C   
9563  O  O   . ARG D 35  ? 0.9332 1.0639 0.9984 0.2238  0.2295  0.2990  36  ARG D O   
9564  C  CB  . ARG D 35  ? 0.8299 0.9498 0.8783 0.2350  0.2212  0.3032  36  ARG D CB  
9565  N  N   . GLN D 36  ? 0.9721 1.0869 1.0830 0.2045  0.2246  0.3054  37  GLN D N   
9566  C  CA  . GLN D 36  ? 0.9752 1.0907 1.1119 0.1984  0.2336  0.3164  37  GLN D CA  
9567  C  C   . GLN D 36  ? 0.9761 1.0959 1.1134 0.1890  0.2264  0.3005  37  GLN D C   
9568  O  O   . GLN D 36  ? 0.9948 1.1220 1.1287 0.1934  0.2347  0.3049  37  GLN D O   
9569  C  CB  . GLN D 36  ? 0.9830 1.0873 1.1577 0.1875  0.2335  0.3268  37  GLN D CB  
9570  C  CG  . GLN D 36  ? 1.2585 1.3618 1.4681 0.1764  0.2375  0.3340  37  GLN D CG  
9571  C  CD  . GLN D 36  ? 1.2740 1.3892 1.4794 0.1836  0.2514  0.3440  37  GLN D CD  
9572  O  OE1 . GLN D 36  ? 1.2916 1.4144 1.4754 0.1995  0.2634  0.3552  37  GLN D OE1 
9573  N  NE2 . GLN D 36  ? 1.2705 1.3871 1.4958 0.1729  0.2494  0.3398  37  GLN D NE2 
9574  N  N   . ILE D 37  ? 0.9134 1.0288 1.0547 0.1773  0.2118  0.2828  38  ILE D N   
9575  C  CA  . ILE D 37  ? 0.8510 0.9704 0.9929 0.1685  0.2048  0.2681  38  ILE D CA  
9576  C  C   . ILE D 37  ? 0.8519 0.9815 0.9647 0.1790  0.2067  0.2620  38  ILE D C   
9577  O  O   . ILE D 37  ? 0.8780 1.0125 0.9924 0.1773  0.2093  0.2597  38  ILE D O   
9578  C  CB  . ILE D 37  ? 0.7815 0.8963 0.9257 0.1578  0.1892  0.2502  38  ILE D CB  
9579  C  CG1 . ILE D 37  ? 0.7032 0.8076 0.8788 0.1459  0.1854  0.2523  38  ILE D CG1 
9580  C  CG2 . ILE D 37  ? 0.7265 0.8481 0.8602 0.1535  0.1821  0.2344  38  ILE D CG2 
9581  C  CD1 . ILE D 37  ? 0.6889 0.7834 0.8706 0.1462  0.1807  0.2545  38  ILE D CD1 
9582  N  N   . TYR D 38  ? 0.8342 0.9663 0.9209 0.1907  0.2049  0.2596  39  TYR D N   
9583  C  CA  . TYR D 38  ? 0.8082 0.9484 0.8657 0.2029  0.2043  0.2527  39  TYR D CA  
9584  C  C   . TYR D 38  ? 0.8359 0.9809 0.8874 0.2150  0.2194  0.2673  39  TYR D C   
9585  O  O   . TYR D 38  ? 0.8064 0.9569 0.8463 0.2191  0.2195  0.2609  39  TYR D O   
9586  C  CB  . TYR D 38  ? 0.7310 0.8720 0.7642 0.2137  0.1986  0.2484  39  TYR D CB  
9587  C  CG  . TYR D 38  ? 0.6587 0.8064 0.6637 0.2239  0.1912  0.2353  39  TYR D CG  
9588  C  CD1 . TYR D 38  ? 0.6455 0.7956 0.6514 0.2148  0.1785  0.2175  39  TYR D CD1 
9589  C  CD2 . TYR D 38  ? 0.6478 0.7988 0.6257 0.2433  0.1960  0.2407  39  TYR D CD2 
9590  C  CE1 . TYR D 38  ? 0.6642 0.8192 0.6478 0.2236  0.1698  0.2050  39  TYR D CE1 
9591  C  CE2 . TYR D 38  ? 0.6444 0.7999 0.5967 0.2534  0.1867  0.2271  39  TYR D CE2 
9592  C  CZ  . TYR D 38  ? 0.6658 0.8230 0.6225 0.2430  0.1731  0.2091  39  TYR D CZ  
9593  O  OH  . TYR D 38  ? 0.7250 0.8856 0.6597 0.2527  0.1622  0.1952  39  TYR D OH  
9594  N  N   . GLY D 39  ? 0.9018 1.0451 0.9622 0.2214  0.2325  0.2875  40  GLY D N   
9595  C  CA  . GLY D 39  ? 0.9712 1.1204 1.0268 0.2349  0.2492  0.3048  40  GLY D CA  
9596  C  C   . GLY D 39  ? 1.0123 1.1638 1.0939 0.2260  0.2563  0.3110  40  GLY D C   
9597  O  O   . GLY D 39  ? 1.0272 1.1859 1.1004 0.2370  0.2676  0.3192  40  GLY D O   
9598  N  N   . ALA D 40  ? 1.0115 1.1568 1.1239 0.2070  0.2493  0.3066  41  ALA D N   
9599  C  CA  . ALA D 40  ? 0.9991 1.1454 1.1409 0.1968  0.2543  0.3125  41  ALA D CA  
9600  C  C   . ALA D 40  ? 0.9841 1.1351 1.1152 0.1936  0.2476  0.2959  41  ALA D C   
9601  O  O   . ALA D 40  ? 1.0138 1.1687 1.1609 0.1903  0.2540  0.3010  41  ALA D O   
9602  C  CB  . ALA D 40  ? 0.9704 1.1070 1.1475 0.1792  0.2470  0.3124  41  ALA D CB  
9603  N  N   . LYS D 41  ? 0.9478 1.0987 1.0540 0.1944  0.2346  0.2766  42  LYS D N   
9604  C  CA  . LYS D 41  ? 0.9137 1.0685 1.0086 0.1923  0.2271  0.2604  42  LYS D CA  
9605  C  C   . LYS D 41  ? 0.9509 1.1124 1.0140 0.2117  0.2328  0.2607  42  LYS D C   
9606  O  O   . LYS D 41  ? 0.9328 1.0968 0.9812 0.2134  0.2253  0.2463  42  LYS D O   
9607  C  CB  . LYS D 41  ? 0.8834 1.0348 0.9728 0.1824  0.2094  0.2401  42  LYS D CB  
9608  C  CG  . LYS D 41  ? 0.8879 1.0320 1.0028 0.1669  0.2032  0.2391  42  LYS D CG  
9609  C  CD  . LYS D 41  ? 0.8688 1.0117 0.9851 0.1553  0.1884  0.2205  42  LYS D CD  
9610  C  CE  . LYS D 41  ? 0.8826 1.0227 1.0256 0.1415  0.1869  0.2195  42  LYS D CE  
9611  N  NZ  . LYS D 41  ? 0.8939 1.0256 1.0572 0.1322  0.1822  0.2210  42  LYS D NZ  
9612  N  N   . GLY D 42  ? 0.9615 1.1255 1.0142 0.2271  0.2457  0.2774  43  GLY D N   
9613  C  CA  . GLY D 42  ? 0.9972 1.1675 1.0192 0.2487  0.2534  0.2808  43  GLY D CA  
9614  C  C   . GLY D 42  ? 1.0421 1.2120 1.0293 0.2638  0.2464  0.2729  43  GLY D C   
9615  O  O   . GLY D 42  ? 1.0922 1.2664 1.0505 0.2848  0.2526  0.2765  43  GLY D O   
9616  N  N   . PHE D 43  ? 1.0143 1.1791 1.0034 0.2542  0.2331  0.2622  44  PHE D N   
9617  C  CA  . PHE D 43  ? 1.0141 1.1785 0.9731 0.2664  0.2233  0.2522  44  PHE D CA  
9618  C  C   . PHE D 43  ? 1.0286 1.1932 0.9748 0.2819  0.2338  0.2689  44  PHE D C   
9619  O  O   . PHE D 43  ? 1.0171 1.1802 0.9844 0.2782  0.2461  0.2875  44  PHE D O   
9620  C  CB  . PHE D 43  ? 0.9587 1.1192 0.9264 0.2509  0.2058  0.2354  44  PHE D CB  
9621  C  CG  . PHE D 43  ? 0.9407 1.1019 0.9138 0.2396  0.1934  0.2173  44  PHE D CG  
9622  C  CD1 . PHE D 43  ? 0.9508 1.1146 0.9006 0.2501  0.1849  0.2039  44  PHE D CD1 
9623  C  CD2 . PHE D 43  ? 0.9026 1.0613 0.9041 0.2193  0.1895  0.2135  44  PHE D CD2 
9624  C  CE1 . PHE D 43  ? 0.9273 1.0913 0.8843 0.2396  0.1735  0.1882  44  PHE D CE1 
9625  C  CE2 . PHE D 43  ? 0.8984 1.0582 0.9051 0.2096  0.1789  0.1982  44  PHE D CE2 
9626  C  CZ  . PHE D 43  ? 0.9036 1.0660 0.8892 0.2192  0.1712  0.1861  44  PHE D CZ  
9627  N  N   . SER D 44  ? 1.1013 1.2675 1.0135 0.2998  0.2280  0.2620  45  SER D N   
9628  C  CA  . SER D 44  ? 1.1766 1.3432 1.0706 0.3173  0.2361  0.2758  45  SER D CA  
9629  C  C   . SER D 44  ? 1.1720 1.3333 1.0831 0.3061  0.2328  0.2798  45  SER D C   
9630  O  O   . SER D 44  ? 1.1322 1.2904 1.0541 0.2909  0.2181  0.2645  45  SER D O   
9631  C  CB  . SER D 44  ? 1.2774 1.4458 1.1305 0.3380  0.2258  0.2627  45  SER D CB  
9632  O  OG  . SER D 44  ? 1.3015 1.4669 1.1515 0.3319  0.2084  0.2478  45  SER D OG  
9633  N  N   . LEU D 45  ? 1.1612 1.3218 1.0747 0.3148  0.2469  0.3010  46  LEU D N   
9634  C  CA  . LEU D 45  ? 1.1736 1.3284 1.0997 0.3077  0.2439  0.3055  46  LEU D CA  
9635  C  C   . LEU D 45  ? 1.2194 1.3751 1.1124 0.3251  0.2371  0.3005  46  LEU D C   
9636  O  O   . LEU D 45  ? 1.2189 1.3705 1.1157 0.3239  0.2350  0.3047  46  LEU D O   
9637  C  CB  . LEU D 45  ? 1.1256 1.2777 1.0771 0.3061  0.2615  0.3316  46  LEU D CB  
9638  C  CG  . LEU D 45  ? 1.0586 1.2096 1.0472 0.2899  0.2691  0.3399  46  LEU D CG  
9639  C  CD1 . LEU D 45  ? 1.0590 1.2183 1.0417 0.3020  0.2844  0.3521  46  LEU D CD1 
9640  C  CD2 . LEU D 45  ? 1.0403 1.1842 1.0628 0.2804  0.2761  0.3576  46  LEU D CD2 
9641  N  N   . SER D 46  ? 1.3159 1.4764 1.1761 0.3421  0.2329  0.2911  47  SER D N   
9642  C  CA  . SER D 46  ? 1.3706 1.5323 1.1966 0.3614  0.2252  0.2853  47  SER D CA  
9643  C  C   . SER D 46  ? 1.3800 1.5391 1.2086 0.3505  0.2048  0.2661  47  SER D C   
9644  O  O   . SER D 46  ? 1.3964 1.5540 1.2166 0.3571  0.2019  0.2690  47  SER D O   
9645  C  CB  . SER D 46  ? 1.4310 1.5971 1.2222 0.3819  0.2223  0.2765  47  SER D CB  
9646  O  OG  . SER D 46  ? 1.4566 1.6229 1.2154 0.3993  0.2098  0.2659  47  SER D OG  
9647  N  N   . ASP D 47  ? 1.3431 1.5026 1.1845 0.3346  0.1914  0.2475  48  ASP D N   
9648  C  CA  . ASP D 47  ? 1.2961 1.4556 1.1393 0.3262  0.1719  0.2288  48  ASP D CA  
9649  C  C   . ASP D 47  ? 1.2055 1.3617 1.0805 0.3047  0.1698  0.2293  48  ASP D C   
9650  O  O   . ASP D 47  ? 1.1875 1.3448 1.0678 0.2967  0.1553  0.2156  48  ASP D O   
9651  C  CB  . ASP D 47  ? 1.3213 1.4837 1.1598 0.3230  0.1571  0.2082  48  ASP D CB  
9652  C  CG  . ASP D 47  ? 1.3554 1.5195 1.1663 0.3425  0.1609  0.2078  48  ASP D CG  
9653  O  OD1 . ASP D 47  ? 1.3866 1.5513 1.1693 0.3647  0.1654  0.2150  48  ASP D OD1 
9654  O  OD2 . ASP D 47  ? 1.3250 1.4898 1.1413 0.3369  0.1593  0.2003  48  ASP D OD2 
9655  N  N   . VAL D 48  ? 1.1196 1.2716 1.0163 0.2962  0.1838  0.2451  49  VAL D N   
9656  C  CA  . VAL D 48  ? 1.0533 1.2004 0.9774 0.2787  0.1814  0.2458  49  VAL D CA  
9657  C  C   . VAL D 48  ? 1.0281 1.1716 0.9476 0.2866  0.1842  0.2563  49  VAL D C   
9658  O  O   . VAL D 48  ? 1.0400 1.1821 0.9509 0.2997  0.1971  0.2735  49  VAL D O   
9659  C  CB  . VAL D 48  ? 0.8206 0.9633 0.7739 0.2646  0.1918  0.2559  49  VAL D CB  
9660  C  CG1 . VAL D 48  ? 0.8453 0.9873 0.7979 0.2756  0.2101  0.2777  49  VAL D CG1 
9661  C  CG2 . VAL D 48  ? 0.8068 0.9427 0.7858 0.2493  0.1879  0.2557  49  VAL D CG2 
9662  N  N   . PRO D 49  ? 0.9398 1.0823 0.8649 0.2796  0.1725  0.2464  50  PRO D N   
9663  C  CA  . PRO D 49  ? 0.9505 1.0895 0.8712 0.2868  0.1731  0.2541  50  PRO D CA  
9664  C  C   . PRO D 49  ? 0.9394 1.0692 0.8835 0.2800  0.1841  0.2706  50  PRO D C   
9665  O  O   . PRO D 49  ? 0.9251 1.0511 0.8926 0.2665  0.1879  0.2727  50  PRO D O   
9666  C  CB  . PRO D 49  ? 0.9121 1.0541 0.8364 0.2790  0.1569  0.2371  50  PRO D CB  
9667  C  CG  . PRO D 49  ? 0.8784 1.0218 0.8213 0.2621  0.1519  0.2261  50  PRO D CG  
9668  C  CD  . PRO D 49  ? 0.8973 1.0431 0.8327 0.2659  0.1581  0.2277  50  PRO D CD  
9669  N  N   . GLN D 50  ? 0.9144 1.0400 0.8532 0.2895  0.1883  0.2820  51  GLN D N   
9670  C  CA  . GLN D 50  ? 0.8861 1.0015 0.8488 0.2836  0.1970  0.2976  51  GLN D CA  
9671  C  C   . GLN D 50  ? 0.8527 0.9619 0.8372 0.2676  0.1866  0.2869  51  GLN D C   
9672  O  O   . GLN D 50  ? 0.8853 0.9864 0.8962 0.2556  0.1895  0.2917  51  GLN D O   
9673  C  CB  . GLN D 50  ? 0.9232 1.0356 0.8736 0.2993  0.2040  0.3132  51  GLN D CB  
9674  C  CG  . GLN D 50  ? 0.9466 1.0674 0.8612 0.3198  0.2046  0.3131  51  GLN D CG  
9675  C  CD  . GLN D 50  ? 1.0452 1.1627 0.9483 0.3356  0.2120  0.3297  51  GLN D CD  
9676  O  OE1 . GLN D 50  ? 1.0717 1.1830 0.9898 0.3371  0.2259  0.3506  51  GLN D OE1 
9677  N  NE2 . GLN D 50  ? 1.0387 1.1603 0.9171 0.3475  0.2024  0.3210  51  GLN D NE2 
9678  N  N   . ALA D 51  ? 0.8607 0.9739 0.8340 0.2685  0.1741  0.2726  52  ALA D N   
9679  C  CA  . ALA D 51  ? 0.8529 0.9617 0.8426 0.2566  0.1645  0.2625  52  ALA D CA  
9680  C  C   . ALA D 51  ? 0.8006 0.9195 0.7840 0.2515  0.1519  0.2431  52  ALA D C   
9681  O  O   . ALA D 51  ? 0.8188 0.9471 0.7846 0.2583  0.1485  0.2369  52  ALA D O   
9682  C  CB  . ALA D 51  ? 0.8199 0.9226 0.8077 0.2636  0.1633  0.2683  52  ALA D CB  
9683  N  N   . GLU D 52  ? 0.7556 0.8723 0.7546 0.2403  0.1446  0.2339  53  GLU D N   
9684  C  CA  . GLU D 52  ? 0.7000 0.8266 0.6984 0.2341  0.1339  0.2177  53  GLU D CA  
9685  C  C   . GLU D 52  ? 0.7076 0.8447 0.6885 0.2441  0.1261  0.2113  53  GLU D C   
9686  O  O   . GLU D 52  ? 0.7862 0.9215 0.7593 0.2533  0.1256  0.2160  53  GLU D O   
9687  C  CB  . GLU D 52  ? 0.6618 0.7842 0.6772 0.2243  0.1287  0.2115  53  GLU D CB  
9688  C  CG  . GLU D 52  ? 0.6742 0.7862 0.7085 0.2138  0.1330  0.2146  53  GLU D CG  
9689  C  CD  . GLU D 52  ? 0.7213 0.8290 0.7683 0.2065  0.1263  0.2065  53  GLU D CD  
9690  O  OE1 . GLU D 52  ? 0.7175 0.8296 0.7590 0.2108  0.1203  0.2010  53  GLU D OE1 
9691  O  OE2 . GLU D 52  ? 0.7358 0.8360 0.7978 0.1977  0.1268  0.2057  53  GLU D OE2 
9692  N  N   . ILE D 53  ? 0.6154 0.7629 0.5915 0.2423  0.1191  0.2005  54  ILE D N   
9693  C  CA  . ILE D 53  ? 0.6779 0.8358 0.6412 0.2508  0.1091  0.1927  54  ILE D CA  
9694  C  C   . ILE D 53  ? 0.6923 0.8600 0.6688 0.2414  0.0987  0.1801  54  ILE D C   
9695  O  O   . ILE D 53  ? 0.7273 0.8935 0.7198 0.2296  0.1000  0.1777  54  ILE D O   
9696  C  CB  . ILE D 53  ? 0.7050 0.8668 0.6497 0.2604  0.1083  0.1913  54  ILE D CB  
9697  C  CG1 . ILE D 53  ? 0.7266 0.8901 0.6786 0.2509  0.1085  0.1854  54  ILE D CG1 
9698  C  CG2 . ILE D 53  ? 0.6237 0.7779 0.5530 0.2729  0.1196  0.2057  54  ILE D CG2 
9699  C  CD1 . ILE D 53  ? 0.7434 0.9086 0.6761 0.2614  0.1087  0.1843  54  ILE D CD1 
9700  N  N   . SER D 54  ? 0.7318 0.9099 0.7028 0.2472  0.0881  0.1728  55  SER D N   
9701  C  CA  . SER D 54  ? 0.7208 0.9102 0.7071 0.2393  0.0784  0.1628  55  SER D CA  
9702  C  C   . SER D 54  ? 0.7599 0.9524 0.7542 0.2299  0.0763  0.1562  55  SER D C   
9703  O  O   . SER D 54  ? 0.7546 0.9452 0.7374 0.2340  0.0762  0.1548  55  SER D O   
9704  C  CB  . SER D 54  ? 0.7801 0.9801 0.7616 0.2481  0.0667  0.1573  55  SER D CB  
9705  O  OG  . SER D 54  ? 0.7806 0.9929 0.7810 0.2401  0.0577  0.1494  55  SER D OG  
9706  N  N   . GLY D 55  ? 0.7401 0.9373 0.7533 0.2184  0.0749  0.1524  56  GLY D N   
9707  C  CA  . GLY D 55  ? 0.7694 0.9686 0.7922 0.2085  0.0739  0.1473  56  GLY D CA  
9708  C  C   . GLY D 55  ? 0.7718 0.9839 0.8061 0.2052  0.0621  0.1383  56  GLY D C   
9709  O  O   . GLY D 55  ? 0.7707 0.9860 0.8186 0.1953  0.0610  0.1347  56  GLY D O   
9710  N  N   . GLU D 56  ? 0.8211 1.0404 0.8517 0.2134  0.0527  0.1351  57  GLU D N   
9711  C  CA  . GLU D 56  ? 0.8133 1.0450 0.8588 0.2105  0.0395  0.1270  57  GLU D CA  
9712  C  C   . GLU D 56  ? 0.7841 1.0135 0.8251 0.2102  0.0332  0.1196  57  GLU D C   
9713  O  O   . GLU D 56  ? 0.7877 1.0254 0.8444 0.2058  0.0218  0.1124  57  GLU D O   
9714  C  CB  . GLU D 56  ? 0.8499 1.0893 0.8936 0.2202  0.0297  0.1253  57  GLU D CB  
9715  N  N   . HIS D 57  ? 0.7553 0.9737 0.7763 0.2152  0.0406  0.1220  58  HIS D N   
9716  C  CA  . HIS D 57  ? 0.7548 0.9697 0.7665 0.2181  0.0357  0.1152  58  HIS D CA  
9717  C  C   . HIS D 57  ? 0.7656 0.9775 0.7880 0.2062  0.0418  0.1150  58  HIS D C   
9718  O  O   . HIS D 57  ? 0.7732 0.9814 0.7882 0.2081  0.0392  0.1098  58  HIS D O   
9719  C  CB  . HIS D 57  ? 0.7927 0.9988 0.7750 0.2329  0.0410  0.1189  58  HIS D CB  
9720  C  CG  . HIS D 57  ? 0.8479 1.0451 0.8239 0.2316  0.0584  0.1308  58  HIS D CG  
9721  N  ND1 . HIS D 57  ? 0.8567 1.0520 0.8385 0.2289  0.0662  0.1393  58  HIS D ND1 
9722  C  CD2 . HIS D 57  ? 0.8643 1.0538 0.8309 0.2327  0.0689  0.1358  58  HIS D CD2 
9723  C  CE1 . HIS D 57  ? 0.8656 1.0518 0.8434 0.2278  0.0796  0.1487  58  HIS D CE1 
9724  N  NE2 . HIS D 57  ? 0.8726 1.0559 0.8421 0.2298  0.0821  0.1474  58  HIS D NE2 
9725  N  N   . LEU D 58  ? 0.7284 0.9415 0.7670 0.1951  0.0494  0.1200  59  LEU D N   
9726  C  CA  . LEU D 58  ? 0.6718 0.8811 0.7191 0.1845  0.0560  0.1207  59  LEU D CA  
9727  C  C   . LEU D 58  ? 0.6501 0.8679 0.7186 0.1750  0.0470  0.1138  59  LEU D C   
9728  O  O   . LEU D 58  ? 0.6722 0.8992 0.7588 0.1695  0.0438  0.1145  59  LEU D O   
9729  C  CB  . LEU D 58  ? 0.6563 0.8614 0.7095 0.1786  0.0674  0.1288  59  LEU D CB  
9730  C  CG  . LEU D 58  ? 0.6343 0.8293 0.6721 0.1858  0.0773  0.1373  59  LEU D CG  
9731  C  CD1 . LEU D 58  ? 0.6125 0.8038 0.6596 0.1804  0.0841  0.1429  59  LEU D CD1 
9732  C  CD2 . LEU D 58  ? 0.6317 0.8184 0.6587 0.1879  0.0845  0.1401  59  LEU D CD2 
9733  N  N   . ARG D 59  ? 0.7071 0.9219 0.7736 0.1737  0.0435  0.1081  60  ARG D N   
9734  C  CA  . ARG D 59  ? 0.6780 0.8993 0.7653 0.1649  0.0344  0.1018  60  ARG D CA  
9735  C  C   . ARG D 59  ? 0.6517 0.8735 0.7546 0.1524  0.0427  0.1060  60  ARG D C   
9736  O  O   . ARG D 59  ? 0.6149 0.8452 0.7398 0.1443  0.0379  0.1050  60  ARG D O   
9737  C  CB  . ARG D 59  ? 0.7090 0.9253 0.7868 0.1697  0.0263  0.0930  60  ARG D CB  
9738  N  N   . ILE D 60  ? 0.5998 0.8129 0.6925 0.1515  0.0549  0.1114  61  ILE D N   
9739  C  CA  . ILE D 60  ? 0.5654 0.7772 0.6701 0.1411  0.0618  0.1142  61  ILE D CA  
9740  C  C   . ILE D 60  ? 0.5817 0.7924 0.6885 0.1392  0.0702  0.1212  61  ILE D C   
9741  O  O   . ILE D 60  ? 0.5590 0.7765 0.6803 0.1338  0.0699  0.1225  61  ILE D O   
9742  C  CB  . ILE D 60  ? 0.5179 0.7204 0.6135 0.1404  0.0678  0.1140  61  ILE D CB  
9743  C  CG1 . ILE D 60  ? 0.5119 0.7145 0.6035 0.1438  0.0588  0.1058  61  ILE D CG1 
9744  C  CG2 . ILE D 60  ? 0.4741 0.6752 0.5825 0.1299  0.0737  0.1163  61  ILE D CG2 
9745  C  CD1 . ILE D 60  ? 0.4856 0.6807 0.5698 0.1436  0.0645  0.1054  61  ILE D CD1 
9746  N  N   . CYS D 61  ? 0.5867 0.7885 0.6793 0.1447  0.0774  0.1259  62  CYS D N   
9747  C  CA  . CYS D 61  ? 0.5739 0.7721 0.6674 0.1445  0.0837  0.1316  62  CYS D CA  
9748  C  C   . CYS D 61  ? 0.5735 0.7808 0.6722 0.1474  0.0792  0.1318  62  CYS D C   
9749  O  O   . CYS D 61  ? 0.5462 0.7604 0.6435 0.1523  0.0721  0.1292  62  CYS D O   
9750  C  CB  . CYS D 61  ? 0.5795 0.7668 0.6590 0.1509  0.0907  0.1374  62  CYS D CB  
9751  S  SG  . CYS D 61  ? 0.8708 1.0488 0.9460 0.1489  0.0981  0.1400  62  CYS D SG  
9752  N  N   . PRO D 62  ? 0.6183 0.8259 0.7232 0.1454  0.0827  0.1346  63  PRO D N   
9753  C  CA  . PRO D 62  ? 0.6476 0.8637 0.7563 0.1500  0.0803  0.1362  63  PRO D CA  
9754  C  C   . PRO D 62  ? 0.7248 0.9378 0.8207 0.1593  0.0795  0.1381  63  PRO D C   
9755  O  O   . PRO D 62  ? 0.7747 0.9758 0.8588 0.1624  0.0844  0.1411  63  PRO D O   
9756  C  CB  . PRO D 62  ? 0.6218 0.8335 0.7329 0.1487  0.0856  0.1386  63  PRO D CB  
9757  C  CG  . PRO D 62  ? 0.6027 0.8096 0.7185 0.1407  0.0880  0.1370  63  PRO D CG  
9758  C  CD  . PRO D 62  ? 0.5814 0.7820 0.6904 0.1396  0.0882  0.1358  63  PRO D CD  
9759  N  N   . GLN D 63  ? 0.7788 1.0028 0.8784 0.1638  0.0733  0.1373  64  GLN D N   
9760  C  CA  . GLN D 63  ? 0.8018 1.0239 0.8889 0.1734  0.0713  0.1387  64  GLN D CA  
9761  C  C   . GLN D 63  ? 0.7790 0.9939 0.8595 0.1784  0.0773  0.1438  64  GLN D C   
9762  O  O   . GLN D 63  ? 0.7985 1.0166 0.8867 0.1772  0.0792  0.1450  64  GLN D O   
9763  C  CB  . GLN D 63  ? 0.8854 1.1219 0.9811 0.1767  0.0616  0.1359  64  GLN D CB  
9764  C  CG  . GLN D 63  ? 0.9587 1.1992 1.0580 0.1747  0.0528  0.1297  64  GLN D CG  
9765  C  CD  . GLN D 63  ? 1.0295 1.2835 1.1410 0.1778  0.0411  0.1266  64  GLN D CD  
9766  O  OE1 . GLN D 63  ? 1.0609 1.3240 1.1816 0.1801  0.0408  0.1301  64  GLN D OE1 
9767  N  NE2 . GLN D 63  ? 1.0522 1.3076 1.1647 0.1785  0.0307  0.1197  64  GLN D NE2 
9768  N  N   . GLY D 64  ? 0.7252 0.9300 0.7909 0.1850  0.0802  0.1471  65  GLY D N   
9769  C  CA  . GLY D 64  ? 0.6883 0.8835 0.7479 0.1901  0.0852  0.1522  65  GLY D CA  
9770  C  C   . GLY D 64  ? 0.6697 0.8535 0.7156 0.1953  0.0896  0.1572  65  GLY D C   
9771  O  O   . GLY D 64  ? 0.7027 0.8858 0.7437 0.1944  0.0901  0.1564  65  GLY D O   
9772  N  N   . TYR D 65  ? 0.6848 0.8596 0.7247 0.2015  0.0933  0.1631  66  TYR D N   
9773  C  CA  . TYR D 65  ? 0.6776 0.8426 0.7056 0.2079  0.0986  0.1704  66  TYR D CA  
9774  C  C   . TYR D 65  ? 0.7110 0.8672 0.7423 0.2015  0.1053  0.1736  66  TYR D C   
9775  O  O   . TYR D 65  ? 0.6964 0.8457 0.7390 0.1940  0.1077  0.1737  66  TYR D O   
9776  C  CB  . TYR D 65  ? 0.6884 0.8443 0.7134 0.2146  0.1014  0.1769  66  TYR D CB  
9777  C  CG  . TYR D 65  ? 0.6869 0.8519 0.7060 0.2232  0.0955  0.1751  66  TYR D CG  
9778  C  CD1 . TYR D 65  ? 0.6973 0.8658 0.7025 0.2329  0.0937  0.1774  66  TYR D CD1 
9779  C  CD2 . TYR D 65  ? 0.6509 0.8216 0.6780 0.2226  0.0916  0.1712  66  TYR D CD2 
9780  C  CE1 . TYR D 65  ? 0.7186 0.8957 0.7198 0.2408  0.0873  0.1755  66  TYR D CE1 
9781  C  CE2 . TYR D 65  ? 0.6863 0.8666 0.7103 0.2306  0.0864  0.1703  66  TYR D CE2 
9782  C  CZ  . TYR D 65  ? 0.6921 0.8754 0.7039 0.2391  0.0838  0.1722  66  TYR D CZ  
9783  O  OH  . TYR D 65  ? 0.7175 0.9105 0.7275 0.2471  0.0777  0.1710  66  TYR D OH  
9784  N  N   . THR D 66  ? 0.6803 0.8371 0.7014 0.2056  0.1078  0.1761  67  THR D N   
9785  C  CA  . THR D 66  ? 0.6593 0.8119 0.6841 0.1997  0.1134  0.1779  67  THR D CA  
9786  C  C   . THR D 66  ? 0.6354 0.7818 0.6494 0.2077  0.1221  0.1883  67  THR D C   
9787  O  O   . THR D 66  ? 0.6390 0.7866 0.6381 0.2194  0.1226  0.1925  67  THR D O   
9788  C  CB  . THR D 66  ? 0.6021 0.7648 0.6274 0.1954  0.1073  0.1683  67  THR D CB  
9789  O  OG1 . THR D 66  ? 0.5989 0.7574 0.6273 0.1904  0.1131  0.1702  67  THR D OG1 
9790  C  CG2 . THR D 66  ? 0.5245 0.6946 0.5343 0.2058  0.1013  0.1649  67  THR D CG2 
9791  N  N   . CYS D 67  ? 0.6941 0.8348 0.7164 0.2021  0.1294  0.1933  68  CYS D N   
9792  C  CA  A CYS D 67  ? 0.7083 0.8451 0.7226 0.2098  0.1395  0.2049  68  CYS D CA  
9793  C  CA  B CYS D 67  ? 0.7088 0.8454 0.7239 0.2093  0.1396  0.2049  68  CYS D CA  
9794  C  C   . CYS D 67  ? 0.7141 0.8579 0.7167 0.2132  0.1390  0.2001  68  CYS D C   
9795  O  O   . CYS D 67  ? 0.7015 0.8445 0.6934 0.2222  0.1474  0.2089  68  CYS D O   
9796  C  CB  A CYS D 67  ? 0.7019 0.8283 0.7347 0.2028  0.1483  0.2152  68  CYS D CB  
9797  C  CB  B CYS D 67  ? 0.7009 0.8277 0.7353 0.2012  0.1478  0.2140  68  CYS D CB  
9798  S  SG  A CYS D 67  ? 0.8248 0.9392 0.8678 0.2045  0.1509  0.2255  68  CYS D SG  
9799  S  SG  B CYS D 67  ? 0.8259 0.9422 0.8791 0.1937  0.1441  0.2140  68  CYS D SG  
9800  N  N   . CYS D 68  ? 0.7250 0.8761 0.7298 0.2070  0.1293  0.1868  69  CYS D N   
9801  C  CA  . CYS D 68  ? 0.7872 0.9438 0.7830 0.2094  0.1265  0.1802  69  CYS D CA  
9802  C  C   . CYS D 68  ? 0.8275 0.9915 0.8065 0.2194  0.1159  0.1714  69  CYS D C   
9803  O  O   . CYS D 68  ? 0.7612 0.9305 0.7459 0.2159  0.1059  0.1634  69  CYS D O   
9804  C  CB  . CYS D 68  ? 0.7868 0.9457 0.7992 0.1953  0.1224  0.1717  69  CYS D CB  
9805  S  SG  . CYS D 68  ? 0.8466 0.9969 0.8800 0.1834  0.1319  0.1795  69  CYS D SG  
9806  N  N   . THR D 69  ? 0.8858 1.0501 0.8444 0.2327  0.1178  0.1730  70  THR D N   
9807  C  CA  . THR D 69  ? 0.9538 1.1240 0.8961 0.2430  0.1054  0.1623  70  THR D CA  
9808  C  C   . THR D 69  ? 1.0250 1.1992 0.9748 0.2354  0.0960  0.1494  70  THR D C   
9809  O  O   . THR D 69  ? 1.0436 1.2165 1.0095 0.2229  0.1003  0.1497  70  THR D O   
9810  C  CB  . THR D 69  ? 0.9132 1.0815 0.8275 0.2628  0.1100  0.1680  70  THR D CB  
9811  O  OG1 . THR D 69  ? 0.8854 1.0513 0.7951 0.2651  0.1196  0.1726  70  THR D OG1 
9812  C  CG2 . THR D 69  ? 0.9194 1.0837 0.8277 0.2705  0.1199  0.1824  70  THR D CG2 
9813  N  N   . SER D 70  ? 1.1331 1.3118 1.0725 0.2431  0.0822  0.1379  71  SER D N   
9814  C  CA  . SER D 70  ? 1.1672 1.3489 1.1152 0.2367  0.0715  0.1252  71  SER D CA  
9815  C  C   . SER D 70  ? 1.1792 1.3564 1.1196 0.2388  0.0793  0.1268  71  SER D C   
9816  O  O   . SER D 70  ? 1.2080 1.3853 1.1648 0.2263  0.0799  0.1238  71  SER D O   
9817  C  CB  . SER D 70  ? 1.2310 1.4168 1.1693 0.2466  0.0536  0.1126  71  SER D CB  
9818  O  OG  . SER D 70  ? 1.2497 1.4372 1.1980 0.2407  0.0422  0.1005  71  SER D OG  
9819  N  N   . GLU D 71  ? 1.1648 1.3386 1.0799 0.2558  0.0859  0.1323  72  GLU D N   
9820  C  CA  . GLU D 71  ? 1.1400 1.3106 1.0454 0.2612  0.0954  0.1359  72  GLU D CA  
9821  C  C   . GLU D 71  ? 1.0567 1.2251 0.9830 0.2467  0.1098  0.1469  72  GLU D C   
9822  O  O   . GLU D 71  ? 1.0787 1.2466 1.0137 0.2397  0.1116  0.1441  72  GLU D O   
9823  C  CB  . GLU D 71  ? 1.1639 1.3324 1.0389 0.2835  0.1034  0.1442  72  GLU D CB  
9824  N  N   . MET D 72  ? 0.9662 1.1328 0.9011 0.2427  0.1189  0.1587  73  MET D N   
9825  C  CA  . MET D 72  ? 0.8859 1.0493 0.8428 0.2289  0.1301  0.1683  73  MET D CA  
9826  C  C   . MET D 72  ? 0.8273 0.9925 0.8064 0.2112  0.1224  0.1584  73  MET D C   
9827  O  O   . MET D 72  ? 0.8601 1.0235 0.8520 0.2025  0.1281  0.1605  73  MET D O   
9828  C  CB  . MET D 72  ? 0.8579 1.0180 0.8218 0.2274  0.1366  0.1796  73  MET D CB  
9829  C  CG  . MET D 72  ? 0.8531 1.0106 0.8001 0.2433  0.1480  0.1940  73  MET D CG  
9830  S  SD  . MET D 72  ? 0.9402 1.0921 0.9004 0.2396  0.1546  0.2071  73  MET D SD  
9831  C  CE  . MET D 72  ? 0.6934 0.8404 0.6862 0.2193  0.1589  0.2095  73  MET D CE  
9832  N  N   . GLU D 73  ? 0.7780 0.9473 0.7623 0.2067  0.1097  0.1486  74  GLU D N   
9833  C  CA  . GLU D 73  ? 0.7407 0.9129 0.7461 0.1913  0.1030  0.1408  74  GLU D CA  
9834  C  C   . GLU D 73  ? 0.7009 0.8743 0.7081 0.1884  0.0986  0.1326  74  GLU D C   
9835  O  O   . GLU D 73  ? 0.6627 0.8350 0.6850 0.1772  0.1021  0.1330  74  GLU D O   
9836  C  CB  . GLU D 73  ? 0.6994 0.8778 0.7104 0.1893  0.0909  0.1335  74  GLU D CB  
9837  C  CG  . GLU D 73  ? 0.6989 0.8814 0.7328 0.1744  0.0865  0.1291  74  GLU D CG  
9838  C  CD  . GLU D 73  ? 0.6864 0.8774 0.7279 0.1734  0.0745  0.1225  74  GLU D CD  
9839  O  OE1 . GLU D 73  ? 0.7179 0.9120 0.7500 0.1820  0.0649  0.1163  74  GLU D OE1 
9840  O  OE2 . GLU D 73  ? 0.6531 0.8480 0.7104 0.1650  0.0743  0.1237  74  GLU D OE2 
9841  N  N   . GLU D 74  ? 0.7312 0.9060 0.7223 0.1995  0.0902  0.1247  75  GLU D N   
9842  C  CA  . GLU D 74  ? 0.7543 0.9290 0.7458 0.1984  0.0844  0.1157  75  GLU D CA  
9843  C  C   . GLU D 74  ? 0.7880 0.9586 0.7758 0.1998  0.0978  0.1232  75  GLU D C   
9844  O  O   . GLU D 74  ? 0.8236 0.9938 0.8236 0.1908  0.0978  0.1199  75  GLU D O   
9845  C  CB  . GLU D 74  ? 0.7786 0.9539 0.7514 0.2126  0.0713  0.1049  75  GLU D CB  
9846  C  CG  . GLU D 74  ? 0.7639 0.9444 0.7495 0.2076  0.0541  0.0942  75  GLU D CG  
9847  N  N   . ASN D 75  ? 0.7424 0.9104 0.7148 0.2114  0.1096  0.1343  76  ASN D N   
9848  C  CA  . ASN D 75  ? 0.7774 0.9429 0.7491 0.2136  0.1242  0.1445  76  ASN D CA  
9849  C  C   . ASN D 75  ? 0.7235 0.8877 0.7218 0.1960  0.1306  0.1499  76  ASN D C   
9850  O  O   . ASN D 75  ? 0.7683 0.9320 0.7747 0.1910  0.1342  0.1496  76  ASN D O   
9851  C  CB  . ASN D 75  ? 0.8097 0.9738 0.7652 0.2281  0.1369  0.1588  76  ASN D CB  
9852  C  CG  . ASN D 75  ? 0.8940 1.0589 0.8184 0.2494  0.1333  0.1548  76  ASN D CG  
9853  O  OD1 . ASN D 75  ? 0.9292 1.0949 0.8446 0.2530  0.1178  0.1396  76  ASN D OD1 
9854  N  ND2 . ASN D 75  ? 0.9144 1.0789 0.8229 0.2644  0.1473  0.1686  76  ASN D ND2 
9855  N  N   . LEU D 76  ? 0.7020 0.8653 0.7131 0.1877  0.1312  0.1542  77  LEU D N   
9856  C  CA  . LEU D 76  ? 0.6465 0.8074 0.6814 0.1725  0.1349  0.1578  77  LEU D CA  
9857  C  C   . LEU D 76  ? 0.6453 0.8088 0.6929 0.1607  0.1256  0.1464  77  LEU D C   
9858  O  O   . LEU D 76  ? 0.6378 0.7997 0.7012 0.1507  0.1289  0.1478  77  LEU D O   
9859  C  CB  . LEU D 76  ? 0.6300 0.7886 0.6728 0.1685  0.1353  0.1627  77  LEU D CB  
9860  C  CG  . LEU D 76  ? 0.6544 0.8083 0.6944 0.1757  0.1467  0.1773  77  LEU D CG  
9861  C  CD1 . LEU D 76  ? 0.6681 0.8195 0.7121 0.1739  0.1438  0.1792  77  LEU D CD1 
9862  C  CD2 . LEU D 76  ? 0.6196 0.7695 0.6767 0.1695  0.1571  0.1872  77  LEU D CD2 
9863  N  N   . ALA D 77  ? 0.6118 0.7796 0.6542 0.1623  0.1135  0.1355  78  ALA D N   
9864  C  CA  . ALA D 77  ? 0.6664 0.8374 0.7222 0.1520  0.1044  0.1259  78  ALA D CA  
9865  C  C   . ALA D 77  ? 0.6863 0.8557 0.7409 0.1524  0.1061  0.1230  78  ALA D C   
9866  O  O   . ALA D 77  ? 0.6946 0.8636 0.7644 0.1419  0.1076  0.1225  78  ALA D O   
9867  C  CB  . ALA D 77  ? 0.6078 0.7838 0.6612 0.1544  0.0908  0.1163  78  ALA D CB  
9868  N  N   . ASN D 78  ? 0.7518 0.9203 0.7870 0.1659  0.1057  0.1209  79  ASN D N   
9869  C  CA  . ASN D 78  ? 0.7886 0.9554 0.8195 0.1692  0.1081  0.1184  79  ASN D CA  
9870  C  C   . ASN D 78  ? 0.7708 0.9356 0.8110 0.1648  0.1227  0.1299  79  ASN D C   
9871  O  O   . ASN D 78  ? 0.7877 0.9520 0.8361 0.1598  0.1244  0.1282  79  ASN D O   
9872  C  CB  . ASN D 78  ? 0.9091 1.0748 0.9134 0.1880  0.1063  0.1152  79  ASN D CB  
9873  C  CG  . ASN D 78  ? 0.9959 1.1624 0.9937 0.1922  0.0885  0.1008  79  ASN D CG  
9874  O  OD1 . ASN D 78  ? 1.0247 1.1931 1.0404 0.1804  0.0780  0.0930  79  ASN D OD1 
9875  N  ND2 . ASN D 78  ? 1.0380 1.2033 1.0112 0.2097  0.0846  0.0977  79  ASN D ND2 
9876  N  N   . ARG D 79  ? 0.6861 0.8497 0.7272 0.1664  0.1325  0.1418  80  ARG D N   
9877  C  CA  . ARG D 79  ? 0.6580 0.8194 0.7129 0.1614  0.1452  0.1536  80  ARG D CA  
9878  C  C   . ARG D 79  ? 0.6555 0.8160 0.7340 0.1446  0.1419  0.1506  80  ARG D C   
9879  O  O   . ARG D 79  ? 0.6880 0.8481 0.7769 0.1397  0.1458  0.1519  80  ARG D O   
9880  C  CB  . ARG D 79  ? 0.6170 0.7764 0.6715 0.1658  0.1543  0.1668  80  ARG D CB  
9881  C  CG  . ARG D 79  ? 0.6169 0.7732 0.6929 0.1580  0.1648  0.1791  80  ARG D CG  
9882  C  CD  . ARG D 79  ? 0.6616 0.8196 0.7430 0.1595  0.1734  0.1842  80  ARG D CD  
9883  N  NE  . ARG D 79  ? 0.7276 0.8889 0.7857 0.1761  0.1783  0.1857  80  ARG D NE  
9884  C  CZ  . ARG D 79  ? 0.7635 0.9263 0.8142 0.1887  0.1916  0.2003  80  ARG D CZ  
9885  N  NH1 . ARG D 79  ? 0.7802 0.9411 0.8485 0.1850  0.2010  0.2152  80  ARG D NH1 
9886  N  NH2 . ARG D 79  ? 0.7801 0.9461 0.8062 0.2059  0.1952  0.2002  80  ARG D NH2 
9887  N  N   . SER D 80  ? 0.6000 0.7604 0.6858 0.1370  0.1349  0.1469  81  SER D N   
9888  C  CA  . SER D 80  ? 0.5491 0.7087 0.6541 0.1234  0.1314  0.1439  81  SER D CA  
9889  C  C   . SER D 80  ? 0.5198 0.6820 0.6288 0.1185  0.1255  0.1351  81  SER D C   
9890  O  O   . SER D 80  ? 0.6035 0.7644 0.7263 0.1103  0.1271  0.1355  81  SER D O   
9891  C  CB  . SER D 80  ? 0.4897 0.6502 0.5978 0.1194  0.1247  0.1409  81  SER D CB  
9892  O  OG  . SER D 80  ? 0.4996 0.6653 0.5992 0.1227  0.1157  0.1327  81  SER D OG  
9893  N  N   . HIS D 81  ? 0.5229 0.6882 0.6207 0.1240  0.1177  0.1269  82  HIS D N   
9894  C  CA  . HIS D 81  ? 0.5603 0.7272 0.6621 0.1206  0.1110  0.1183  82  HIS D CA  
9895  C  C   . HIS D 81  ? 0.5692 0.7337 0.6708 0.1226  0.1187  0.1214  82  HIS D C   
9896  O  O   . HIS D 81  ? 0.5580 0.7224 0.6724 0.1144  0.1178  0.1191  82  HIS D O   
9897  C  CB  . HIS D 81  ? 0.6882 0.8570 0.7776 0.1285  0.1005  0.1092  82  HIS D CB  
9898  C  CG  . HIS D 81  ? 0.7962 0.9655 0.8920 0.1250  0.0916  0.0998  82  HIS D CG  
9899  N  ND1 . HIS D 81  ? 0.8383 1.0046 0.9270 0.1305  0.0933  0.0970  82  HIS D ND1 
9900  C  CD2 . HIS D 81  ? 0.8140 0.9864 0.9238 0.1169  0.0811  0.0933  82  HIS D CD2 
9901  C  CE1 . HIS D 81  ? 0.8696 1.0360 0.9674 0.1256  0.0833  0.0883  82  HIS D CE1 
9902  N  NE2 . HIS D 81  ? 0.8541 1.0244 0.9659 0.1170  0.0759  0.0864  82  HIS D NE2 
9903  N  N   . ALA D 82  ? 0.5277 0.6911 0.6151 0.1344  0.1268  0.1274  83  ALA D N   
9904  C  CA  . ALA D 82  ? 0.5283 0.6911 0.6150 0.1387  0.1358  0.1322  83  ALA D CA  
9905  C  C   . ALA D 82  ? 0.5490 0.7107 0.6570 0.1280  0.1436  0.1407  83  ALA D C   
9906  O  O   . ALA D 82  ? 0.5354 0.6974 0.6519 0.1249  0.1464  0.1408  83  ALA D O   
9907  C  CB  . ALA D 82  ? 0.4913 0.6544 0.5585 0.1550  0.1447  0.1397  83  ALA D CB  
9908  N  N   . GLU D 83  ? 0.4943 0.6544 0.6113 0.1230  0.1460  0.1471  84  GLU D N   
9909  C  CA  . GLU D 83  ? 0.5257 0.6833 0.6640 0.1133  0.1508  0.1539  84  GLU D CA  
9910  C  C   . GLU D 83  ? 0.4603 0.6178 0.6114 0.1016  0.1428  0.1455  84  GLU D C   
9911  O  O   . GLU D 83  ? 0.4369 0.5937 0.6018 0.0962  0.1455  0.1476  84  GLU D O   
9912  C  CB  . GLU D 83  ? 0.5579 0.7121 0.7018 0.1115  0.1524  0.1605  84  GLU D CB  
9913  C  CG  . GLU D 83  ? 0.6451 0.7991 0.7799 0.1226  0.1621  0.1719  84  GLU D CG  
9914  C  CD  . GLU D 83  ? 0.7223 0.8722 0.8616 0.1213  0.1620  0.1772  84  GLU D CD  
9915  O  OE1 . GLU D 83  ? 0.7447 0.8930 0.8859 0.1150  0.1530  0.1696  84  GLU D OE1 
9916  O  OE2 . GLU D 83  ? 0.7342 0.8825 0.8754 0.1272  0.1714  0.1898  84  GLU D OE2 
9917  N  N   . LEU D 84  ? 0.4508 0.6097 0.5981 0.0985  0.1331  0.1370  85  LEU D N   
9918  C  CA  . LEU D 84  ? 0.4892 0.6490 0.6472 0.0890  0.1260  0.1302  85  LEU D CA  
9919  C  C   . LEU D 84  ? 0.4822 0.6432 0.6410 0.0890  0.1253  0.1259  85  LEU D C   
9920  O  O   . LEU D 84  ? 0.4736 0.6339 0.6452 0.0821  0.1256  0.1257  85  LEU D O   
9921  C  CB  . LEU D 84  ? 0.4313 0.5943 0.5858 0.0875  0.1171  0.1237  85  LEU D CB  
9922  C  CG  . LEU D 84  ? 0.4963 0.6615 0.6625 0.0787  0.1110  0.1190  85  LEU D CG  
9923  C  CD1 . LEU D 84  ? 0.4719 0.6336 0.6496 0.0727  0.1136  0.1227  85  LEU D CD1 
9924  C  CD2 . LEU D 84  ? 0.4943 0.6644 0.6595 0.0782  0.1039  0.1155  85  LEU D CD2 
9925  N  N   . GLU D 85  ? 0.4757 0.6381 0.6203 0.0976  0.1236  0.1219  86  GLU D N   
9926  C  CA  . GLU D 85  ? 0.5593 0.7218 0.7020 0.0999  0.1225  0.1171  86  GLU D CA  
9927  C  C   . GLU D 85  ? 0.5462 0.7078 0.6968 0.0998  0.1326  0.1245  86  GLU D C   
9928  O  O   . GLU D 85  ? 0.5868 0.7483 0.7472 0.0946  0.1315  0.1220  86  GLU D O   
9929  C  CB  . GLU D 85  ? 0.6367 0.7992 0.7595 0.1128  0.1195  0.1120  86  GLU D CB  
9930  C  CG  . GLU D 85  ? 0.7193 0.8827 0.8380 0.1127  0.1067  0.1026  86  GLU D CG  
9931  C  CD  . GLU D 85  ? 0.7870 0.9500 0.9151 0.1070  0.0968  0.0935  86  GLU D CD  
9932  O  OE1 . GLU D 85  ? 0.8198 0.9833 0.9460 0.1087  0.0854  0.0855  86  GLU D OE1 
9933  O  OE2 . GLU D 85  ? 0.8191 0.9815 0.9581 0.1008  0.0998  0.0947  86  GLU D OE2 
9934  N  N   . THR D 86  ? 0.5945 0.7561 0.7425 0.1056  0.1424  0.1345  87  THR D N   
9935  C  CA  . THR D 86  ? 0.5873 0.7493 0.7464 0.1059  0.1531  0.1442  87  THR D CA  
9936  C  C   . THR D 86  ? 0.6012 0.7617 0.7831 0.0928  0.1511  0.1450  87  THR D C   
9937  O  O   . THR D 86  ? 0.6044 0.7658 0.7963 0.0902  0.1532  0.1454  87  THR D O   
9938  C  CB  . THR D 86  ? 0.5995 0.7619 0.7568 0.1130  0.1637  0.1570  87  THR D CB  
9939  O  OG1 . THR D 86  ? 0.6108 0.7753 0.7456 0.1281  0.1680  0.1579  87  THR D OG1 
9940  C  CG2 . THR D 86  ? 0.6070 0.7702 0.7849 0.1100  0.1738  0.1689  87  THR D CG2 
9941  N  N   . ALA D 87  ? 0.5705 0.7284 0.7593 0.0858  0.1464  0.1446  88  ALA D N   
9942  C  CA  . ALA D 87  ? 0.5667 0.7222 0.7740 0.0752  0.1426  0.1437  88  ALA D CA  
9943  C  C   . ALA D 87  ? 0.6176 0.7745 0.8271 0.0703  0.1361  0.1352  88  ALA D C   
9944  O  O   . ALA D 87  ? 0.6361 0.7927 0.8590 0.0658  0.1370  0.1362  88  ALA D O   
9945  C  CB  . ALA D 87  ? 0.5105 0.6628 0.7193 0.0712  0.1371  0.1424  88  ALA D CB  
9946  N  N   . LEU D 88  ? 0.6209 0.7795 0.8191 0.0712  0.1293  0.1275  89  LEU D N   
9947  C  CA  . LEU D 88  ? 0.6422 0.8021 0.8430 0.0671  0.1229  0.1201  89  LEU D CA  
9948  C  C   . LEU D 88  ? 0.6483 0.8085 0.8520 0.0693  0.1267  0.1203  89  LEU D C   
9949  O  O   . LEU D 88  ? 0.6432 0.8030 0.8591 0.0634  0.1257  0.1197  89  LEU D O   
9950  C  CB  . LEU D 88  ? 0.6350 0.7970 0.8250 0.0700  0.1158  0.1133  89  LEU D CB  
9951  C  CG  . LEU D 88  ? 0.6437 0.8078 0.8377 0.0644  0.1086  0.1104  89  LEU D CG  
9952  C  CD1 . LEU D 88  ? 0.6685 0.8319 0.8608 0.0647  0.1107  0.1148  89  LEU D CD1 
9953  C  CD2 . LEU D 88  ? 0.6810 0.8477 0.8693 0.0670  0.1011  0.1042  89  LEU D CD2 
9954  N  N   . ARG D 89  ? 0.6814 0.8424 0.8727 0.0790  0.1313  0.1212  90  ARG D N   
9955  C  CA  . ARG D 89  ? 0.7259 0.8875 0.9165 0.0838  0.1352  0.1208  90  ARG D CA  
9956  C  C   . ARG D 89  ? 0.7226 0.8852 0.9292 0.0810  0.1438  0.1298  90  ARG D C   
9957  O  O   . ARG D 89  ? 0.7684 0.9318 0.9817 0.0805  0.1453  0.1291  90  ARG D O   
9958  C  CB  . ARG D 89  ? 0.8211 0.9832 0.9917 0.0978  0.1386  0.1202  90  ARG D CB  
9959  C  CG  . ARG D 89  ? 0.9190 1.0836 1.0881 0.1062  0.1521  0.1318  90  ARG D CG  
9960  C  CD  . ARG D 89  ? 1.0292 1.1943 1.1749 0.1212  0.1551  0.1323  90  ARG D CD  
9961  N  NE  . ARG D 89  ? 1.0835 1.2513 1.2303 0.1267  0.1675  0.1462  90  ARG D NE  
9962  C  CZ  . ARG D 89  ? 1.1609 1.3297 1.2881 0.1405  0.1727  0.1501  90  ARG D CZ  
9963  N  NH1 . ARG D 89  ? 1.1974 1.3645 1.3016 0.1506  0.1651  0.1396  90  ARG D NH1 
9964  N  NH2 . ARG D 89  ? 1.1879 1.3594 1.3195 0.1448  0.1849  0.1647  90  ARG D NH2 
9965  N  N   . ASP D 90  ? 0.6725 0.8348 0.8873 0.0790  0.1487  0.1383  91  ASP D N   
9966  C  CA  . ASP D 90  ? 0.6648 0.8278 0.8998 0.0754  0.1553  0.1471  91  ASP D CA  
9967  C  C   . ASP D 90  ? 0.5947 0.7557 0.8457 0.0645  0.1477  0.1425  91  ASP D C   
9968  O  O   . ASP D 90  ? 0.5862 0.7487 0.8503 0.0625  0.1499  0.1444  91  ASP D O   
9969  C  CB  . ASP D 90  ? 0.7067 0.8686 0.9492 0.0759  0.1609  0.1573  91  ASP D CB  
9970  C  CG  . ASP D 90  ? 0.8072 0.9726 1.0386 0.0880  0.1721  0.1663  91  ASP D CG  
9971  O  OD1 . ASP D 90  ? 0.8159 0.9839 1.0302 0.0972  0.1742  0.1627  91  ASP D OD1 
9972  O  OD2 . ASP D 90  ? 0.8339 0.9991 1.0735 0.0894  0.1786  0.1770  91  ASP D OD2 
9973  N  N   . SER D 91  ? 0.5703 0.7284 0.8195 0.0587  0.1391  0.1367  92  SER D N   
9974  C  CA  . SER D 91  ? 0.5624 0.7187 0.8224 0.0507  0.1316  0.1319  92  SER D CA  
9975  C  C   . SER D 91  ? 0.5359 0.6943 0.7941 0.0505  0.1295  0.1264  92  SER D C   
9976  O  O   . SER D 91  ? 0.5394 0.6978 0.8103 0.0468  0.1288  0.1266  92  SER D O   
9977  C  CB  . SER D 91  ? 0.5524 0.7068 0.8065 0.0474  0.1238  0.1270  92  SER D CB  
9978  O  OG  . SER D 91  ? 0.5901 0.7414 0.8463 0.0478  0.1248  0.1312  92  SER D OG  
9979  N  N   . SER D 92  ? 0.5405 0.6999 0.7836 0.0548  0.1276  0.1214  93  SER D N   
9980  C  CA  . SER D 92  ? 0.5907 0.7507 0.8315 0.0556  0.1243  0.1154  93  SER D CA  
9981  C  C   . SER D 92  ? 0.5929 0.7542 0.8392 0.0593  0.1310  0.1187  93  SER D C   
9982  O  O   . SER D 92  ? 0.6455 0.8066 0.8985 0.0568  0.1284  0.1156  93  SER D O   
9983  C  CB  . SER D 92  ? 0.5401 0.7000 0.7648 0.0614  0.1205  0.1096  93  SER D CB  
9984  O  OG  . SER D 92  ? 0.6119 0.7709 0.8359 0.0625  0.1160  0.1033  93  SER D OG  
9985  N  N   . ARG D 93  ? 0.5743 0.7374 0.8185 0.0661  0.1402  0.1259  94  ARG D N   
9986  C  CA  . ARG D 93  ? 0.5834 0.7496 0.8335 0.0713  0.1485  0.1311  94  ARG D CA  
9987  C  C   . ARG D 93  ? 0.5685 0.7359 0.8425 0.0638  0.1503  0.1370  94  ARG D C   
9988  O  O   . ARG D 93  ? 0.5411 0.7109 0.8241 0.0649  0.1535  0.1385  94  ARG D O   
9989  C  CB  . ARG D 93  ? 0.6913 0.8605 0.9315 0.0827  0.1592  0.1390  94  ARG D CB  
9990  C  CG  . ARG D 93  ? 0.7674 0.9356 0.9825 0.0938  0.1574  0.1321  94  ARG D CG  
9991  C  CD  . ARG D 93  ? 0.8468 1.0185 1.0496 0.1075  0.1689  0.1407  94  ARG D CD  
9992  N  NE  . ARG D 93  ? 0.8647 1.0372 1.0734 0.1051  0.1738  0.1502  94  ARG D NE  
9993  C  CZ  . ARG D 93  ? 0.8690 1.0453 1.0950 0.1046  0.1844  0.1638  94  ARG D CZ  
9994  N  NH1 . ARG D 93  ? 0.8458 1.0213 1.0777 0.1023  0.1873  0.1716  94  ARG D NH1 
9995  N  NH2 . ARG D 93  ? 0.8733 1.0540 1.1127 0.1064  0.1917  0.1700  94  ARG D NH2 
9996  N  N   . VAL D 94  ? 0.4527 0.6179 0.7372 0.0569  0.1474  0.1397  95  VAL D N   
9997  C  CA  . VAL D 94  ? 0.4338 0.5985 0.7413 0.0495  0.1451  0.1426  95  VAL D CA  
9998  C  C   . VAL D 94  ? 0.4650 0.6283 0.7742 0.0446  0.1370  0.1345  95  VAL D C   
9999  O  O   . VAL D 94  ? 0.4756 0.6409 0.7978 0.0435  0.1383  0.1359  95  VAL D O   
10000 C  CB  . VAL D 94  ? 0.3817 0.5421 0.6977 0.0440  0.1404  0.1443  95  VAL D CB  
10001 C  CG1 . VAL D 94  ? 0.3437 0.5019 0.6811 0.0369  0.1340  0.1438  95  VAL D CG1 
10002 C  CG2 . VAL D 94  ? 0.4450 0.6064 0.7651 0.0480  0.1489  0.1545  95  VAL D CG2 
10003 N  N   . LEU D 95  ? 0.4458 0.6064 0.7427 0.0422  0.1292  0.1269  96  LEU D N   
10004 C  CA  . LEU D 95  ? 0.4049 0.5646 0.7026 0.0383  0.1221  0.1204  96  LEU D CA  
10005 C  C   . LEU D 95  ? 0.3408 0.5023 0.6373 0.0420  0.1248  0.1187  96  LEU D C   
10006 O  O   . LEU D 95  ? 0.3948 0.5566 0.7020 0.0393  0.1230  0.1179  96  LEU D O   
10007 C  CB  . LEU D 95  ? 0.4165 0.5749 0.7014 0.0369  0.1156  0.1149  96  LEU D CB  
10008 C  CG  . LEU D 95  ? 0.3748 0.5328 0.6603 0.0335  0.1089  0.1100  96  LEU D CG  
10009 C  CD1 . LEU D 95  ? 0.3832 0.5402 0.6812 0.0294  0.1056  0.1108  96  LEU D CD1 
10010 C  CD2 . LEU D 95  ? 0.3066 0.4649 0.5830 0.0326  0.1042  0.1075  96  LEU D CD2 
10011 N  N   . GLN D 96  ? 0.3702 0.5325 0.6527 0.0492  0.1287  0.1176  97  GLN D N   
10012 C  CA  . GLN D 96  ? 0.4426 0.6056 0.7200 0.0555  0.1309  0.1148  97  GLN D CA  
10013 C  C   . GLN D 96  ? 0.4498 0.6163 0.7414 0.0573  0.1383  0.1211  97  GLN D C   
10014 O  O   . GLN D 96  ? 0.5032 0.6698 0.7997 0.0575  0.1368  0.1184  97  GLN D O   
10015 C  CB  . GLN D 96  ? 0.5343 0.6972 0.7929 0.0655  0.1342  0.1133  97  GLN D CB  
10016 C  CG  . GLN D 96  ? 0.6185 0.7779 0.8648 0.0700  0.1275  0.1037  97  GLN D CG  
10017 C  CD  . GLN D 96  ? 0.7330 0.8912 0.9593 0.0802  0.1277  0.1006  97  GLN D CD  
10018 O  OE1 . GLN D 96  ? 0.7053 0.8639 0.9261 0.0794  0.1274  0.1023  97  GLN D OE1 
10019 N  NE2 . GLN D 96  ? 0.7654 0.9218 0.9799 0.0909  0.1277  0.0957  97  GLN D NE2 
10020 N  N   . ALA D 97  ? 0.4716 0.6415 0.7718 0.0587  0.1462  0.1303  98  ALA D N   
10021 C  CA  . ALA D 97  ? 0.4025 0.5774 0.7208 0.0602  0.1540  0.1387  98  ALA D CA  
10022 C  C   . ALA D 97  ? 0.4599 0.6340 0.7975 0.0511  0.1472  0.1370  98  ALA D C   
10023 O  O   . ALA D 97  ? 0.3911 0.5682 0.7392 0.0525  0.1496  0.1385  98  ALA D O   
10024 C  CB  . ALA D 97  ? 0.3805 0.5589 0.7087 0.0619  0.1627  0.1502  98  ALA D CB  
10025 N  N   . MET D 98  ? 0.4360 0.6059 0.7771 0.0432  0.1386  0.1339  99  MET D N   
10026 C  CA  . MET D 98  ? 0.4074 0.5756 0.7631 0.0362  0.1306  0.1312  99  MET D CA  
10027 C  C   . MET D 98  ? 0.4024 0.5699 0.7524 0.0367  0.1269  0.1248  99  MET D C   
10028 O  O   . MET D 98  ? 0.3985 0.5683 0.7619 0.0362  0.1272  0.1260  99  MET D O   
10029 C  CB  . MET D 98  ? 0.3937 0.5569 0.7470 0.0306  0.1216  0.1274  99  MET D CB  
10030 C  CG  . MET D 98  ? 0.4545 0.6155 0.8210 0.0254  0.1126  0.1246  99  MET D CG  
10031 S  SD  . MET D 98  ? 0.4207 0.5799 0.7758 0.0243  0.1054  0.1169  99  MET D SD  
10032 C  CE  . MET D 98  ? 0.2981 0.4546 0.6336 0.0242  0.1018  0.1133  99  MET D CE  
10033 N  N   . LEU D 99  ? 0.3924 0.5570 0.7245 0.0377  0.1231  0.1184  100 LEU D N   
10034 C  CA  . LEU D 99  ? 0.3113 0.4741 0.6393 0.0378  0.1185  0.1125  100 LEU D CA  
10035 C  C   . LEU D 99  ? 0.4245 0.5896 0.7542 0.0443  0.1244  0.1132  100 LEU D C   
10036 O  O   . LEU D 99  ? 0.4225 0.5871 0.7589 0.0434  0.1217  0.1110  100 LEU D O   
10037 C  CB  . LEU D 99  ? 0.3129 0.4726 0.6249 0.0383  0.1138  0.1068  100 LEU D CB  
10038 C  CG  . LEU D 99  ? 0.3066 0.4650 0.6164 0.0329  0.1080  0.1062  100 LEU D CG  
10039 C  CD1 . LEU D 99  ? 0.3735 0.5306 0.6703 0.0340  0.1049  0.1024  100 LEU D CD1 
10040 C  CD2 . LEU D 99  ? 0.3004 0.4580 0.6188 0.0281  0.1020  0.1055  100 LEU D CD2 
10041 N  N   . ALA D 100 ? 0.4002 0.5680 0.7232 0.0519  0.1329  0.1167  101 ALA D N   
10042 C  CA  . ALA D 100 ? 0.4053 0.5762 0.7273 0.0609  0.1401  0.1183  101 ALA D CA  
10043 C  C   . ALA D 100 ? 0.4267 0.6029 0.7712 0.0589  0.1444  0.1252  101 ALA D C   
10044 O  O   . ALA D 100 ? 0.4501 0.6271 0.7989 0.0615  0.1445  0.1233  101 ALA D O   
10045 C  CB  . ALA D 100 ? 0.3489 0.5225 0.6577 0.0711  0.1493  0.1223  101 ALA D CB  
10046 N  N   . THR D 101 ? 0.4243 0.6039 0.7846 0.0544  0.1472  0.1330  102 THR D N   
10047 C  CA  . THR D 101 ? 0.4030 0.5876 0.7895 0.0512  0.1494  0.1398  102 THR D CA  
10048 C  C   . THR D 101 ? 0.4227 0.6043 0.8166 0.0452  0.1395  0.1335  102 THR D C   
10049 O  O   . THR D 101 ? 0.3165 0.5017 0.7219 0.0473  0.1417  0.1351  102 THR D O   
10050 C  CB  . THR D 101 ? 0.3926 0.5783 0.7967 0.0453  0.1493  0.1470  102 THR D CB  
10051 O  OG1 . THR D 101 ? 0.4720 0.6628 0.8766 0.0517  0.1612  0.1567  102 THR D OG1 
10052 C  CG2 . THR D 101 ? 0.3946 0.5834 0.8280 0.0399  0.1462  0.1511  102 THR D CG2 
10053 N  N   . GLN D 102 ? 0.4240 0.5995 0.8109 0.0388  0.1293  0.1270  103 GLN D N   
10054 C  CA  . GLN D 102 ? 0.4586 0.6311 0.8500 0.0342  0.1201  0.1217  103 GLN D CA  
10055 C  C   . GLN D 102 ? 0.4550 0.6267 0.8390 0.0386  0.1207  0.1176  103 GLN D C   
10056 O  O   . GLN D 102 ? 0.4392 0.6121 0.8346 0.0380  0.1186  0.1173  103 GLN D O   
10057 C  CB  . GLN D 102 ? 0.5052 0.6721 0.8859 0.0292  0.1110  0.1166  103 GLN D CB  
10058 C  CG  . GLN D 102 ? 0.5933 0.7588 0.9867 0.0242  0.1025  0.1162  103 GLN D CG  
10059 C  CD  . GLN D 102 ? 0.6206 0.7876 1.0295 0.0225  0.1035  0.1212  103 GLN D CD  
10060 O  OE1 . GLN D 102 ? 0.7417 0.9107 1.1495 0.0245  0.1111  0.1258  103 GLN D OE1 
10061 N  NE2 . GLN D 102 ? 0.6528 0.8182 1.0768 0.0193  0.0952  0.1205  103 GLN D NE2 
10062 N  N   . LEU D 103 ? 0.3795 0.5487 0.7450 0.0435  0.1228  0.1138  104 LEU D N   
10063 C  CA  . LEU D 103 ? 0.3865 0.5529 0.7437 0.0487  0.1219  0.1085  104 LEU D CA  
10064 C  C   . LEU D 103 ? 0.3567 0.5281 0.7231 0.0554  0.1293  0.1121  104 LEU D C   
10065 O  O   . LEU D 103 ? 0.3597 0.5302 0.7328 0.0555  0.1262  0.1098  104 LEU D O   
10066 C  CB  . LEU D 103 ? 0.4193 0.5819 0.7560 0.0543  0.1221  0.1036  104 LEU D CB  
10067 C  CG  . LEU D 103 ? 0.4038 0.5607 0.7308 0.0595  0.1175  0.0957  104 LEU D CG  
10068 C  CD1 . LEU D 103 ? 0.4279 0.5809 0.7634 0.0524  0.1088  0.0928  104 LEU D CD1 
10069 C  CD2 . LEU D 103 ? 0.3761 0.5282 0.6850 0.0636  0.1142  0.0897  104 LEU D CD2 
10070 N  N   . ARG D 104 ? 0.3608 0.5381 0.7278 0.0619  0.1397  0.1186  105 ARG D N   
10071 C  CA  . ARG D 104 ? 0.3803 0.5646 0.7575 0.0697  0.1491  0.1246  105 ARG D CA  
10072 C  C   . ARG D 104 ? 0.3296 0.5179 0.7323 0.0631  0.1465  0.1285  105 ARG D C   
10073 O  O   . ARG D 104 ? 0.4494 0.6395 0.8584 0.0668  0.1474  0.1278  105 ARG D O   
10074 C  CB  . ARG D 104 ? 0.4471 0.6389 0.8256 0.0765  0.1617  0.1346  105 ARG D CB  
10075 C  CG  . ARG D 104 ? 0.5847 0.7739 0.9365 0.0872  0.1658  0.1314  105 ARG D CG  
10076 C  CD  . ARG D 104 ? 0.6636 0.8620 1.0175 0.0971  0.1808  0.1435  105 ARG D CD  
10077 N  NE  . ARG D 104 ? 0.7110 0.9131 1.0817 0.0889  0.1833  0.1528  105 ARG D NE  
10078 C  CZ  . ARG D 104 ? 0.7776 0.9762 1.1369 0.0867  0.1817  0.1522  105 ARG D CZ  
10079 N  NH1 . ARG D 104 ? 0.7975 0.9986 1.1741 0.0795  0.1833  0.1606  105 ARG D NH1 
10080 N  NH2 . ARG D 104 ? 0.8041 0.9961 1.1360 0.0919  0.1775  0.1430  105 ARG D NH2 
10081 N  N   . SER D 105 ? 0.4238 0.6127 0.8404 0.0540  0.1423  0.1318  106 SER D N   
10082 C  CA  . SER D 105 ? 0.4005 0.5922 0.8418 0.0478  0.1374  0.1345  106 SER D CA  
10083 C  C   . SER D 105 ? 0.3622 0.5494 0.8013 0.0461  0.1289  0.1272  106 SER D C   
10084 O  O   . SER D 105 ? 0.3112 0.5026 0.7639 0.0485  0.1305  0.1292  106 SER D O   
10085 C  CB  . SER D 105 ? 0.3054 0.4949 0.7561 0.0391  0.1303  0.1354  106 SER D CB  
10086 O  OG  . SER D 105 ? 0.4127 0.6051 0.8654 0.0404  0.1376  0.1423  106 SER D OG  
10087 N  N   . PHE D 106 ? 0.3325 0.5118 0.7554 0.0423  0.1204  0.1197  107 PHE D N   
10088 C  CA  . PHE D 106 ? 0.3058 0.4808 0.7280 0.0405  0.1124  0.1145  107 PHE D CA  
10089 C  C   . PHE D 106 ? 0.3134 0.4874 0.7294 0.0476  0.1158  0.1116  107 PHE D C   
10090 O  O   . PHE D 106 ? 0.3132 0.4876 0.7388 0.0482  0.1132  0.1109  107 PHE D O   
10091 C  CB  . PHE D 106 ? 0.3025 0.4706 0.7106 0.0357  0.1041  0.1094  107 PHE D CB  
10092 C  CG  . PHE D 106 ? 0.2967 0.4645 0.7114 0.0298  0.0975  0.1106  107 PHE D CG  
10093 C  CD1 . PHE D 106 ? 0.2953 0.4635 0.7079 0.0279  0.0987  0.1125  107 PHE D CD1 
10094 C  CD2 . PHE D 106 ? 0.2944 0.4610 0.7166 0.0276  0.0896  0.1093  107 PHE D CD2 
10095 C  CE1 . PHE D 106 ? 0.2924 0.4590 0.7100 0.0239  0.0914  0.1122  107 PHE D CE1 
10096 C  CE2 . PHE D 106 ? 0.2923 0.4576 0.7181 0.0244  0.0822  0.1091  107 PHE D CE2 
10097 C  CZ  . PHE D 106 ? 0.2915 0.4566 0.7151 0.0226  0.0828  0.1101  107 PHE D CZ  
10098 N  N   . ASP D 107 ? 0.3216 0.4937 0.7213 0.0540  0.1207  0.1093  108 ASP D N   
10099 C  CA  . ASP D 107 ? 0.3693 0.5389 0.7608 0.0629  0.1229  0.1051  108 ASP D CA  
10100 C  C   . ASP D 107 ? 0.3636 0.5412 0.7705 0.0687  0.1305  0.1107  108 ASP D C   
10101 O  O   . ASP D 107 ? 0.3373 0.5135 0.7498 0.0707  0.1277  0.1083  108 ASP D O   
10102 C  CB  . ASP D 107 ? 0.4191 0.5861 0.7903 0.0709  0.1270  0.1018  108 ASP D CB  
10103 C  CG  . ASP D 107 ? 0.4662 0.6265 0.8248 0.0798  0.1243  0.0938  108 ASP D CG  
10104 O  OD1 . ASP D 107 ? 0.4752 0.6294 0.8376 0.0762  0.1161  0.0891  108 ASP D OD1 
10105 O  OD2 . ASP D 107 ? 0.4910 0.6515 0.8355 0.0913  0.1301  0.0922  108 ASP D OD2 
10106 N  N   . ASP D 108 ? 0.4116 0.5981 0.8272 0.0714  0.1402  0.1192  109 ASP D N   
10107 C  CA  . ASP D 108 ? 0.4470 0.6435 0.8811 0.0770  0.1492  0.1272  109 ASP D CA  
10108 C  C   . ASP D 108 ? 0.3292 0.5279 0.7865 0.0696  0.1425  0.1286  109 ASP D C   
10109 O  O   . ASP D 108 ? 0.3325 0.5359 0.8009 0.0745  0.1456  0.1307  109 ASP D O   
10110 C  CB  . ASP D 108 ? 0.4609 0.6670 0.9052 0.0792  0.1604  0.1384  109 ASP D CB  
10111 C  CG  . ASP D 108 ? 0.5422 0.7488 0.9641 0.0914  0.1700  0.1390  109 ASP D CG  
10112 O  OD1 . ASP D 108 ? 0.5720 0.7701 0.9700 0.0971  0.1658  0.1289  109 ASP D OD1 
10113 O  OD2 . ASP D 108 ? 0.5729 0.7882 1.0019 0.0958  0.1813  0.1498  109 ASP D OD2 
10114 N  N   . HIS D 109 ? 0.3188 0.5142 0.7822 0.0588  0.1331  0.1272  110 HIS D N   
10115 C  CA  . HIS D 109 ? 0.3118 0.5084 0.7949 0.0529  0.1250  0.1275  110 HIS D CA  
10116 C  C   . HIS D 109 ? 0.4142 0.6049 0.8902 0.0547  0.1189  0.1209  110 HIS D C   
10117 O  O   . HIS D 109 ? 0.4332 0.6280 0.9251 0.0562  0.1182  0.1228  110 HIS D O   
10118 C  CB  . HIS D 109 ? 0.3038 0.4964 0.7899 0.0435  0.1150  0.1259  110 HIS D CB  
10119 C  CG  . HIS D 109 ? 0.4068 0.5995 0.9097 0.0391  0.1050  0.1249  110 HIS D CG  
10120 N  ND1 . HIS D 109 ? 0.2984 0.4993 0.8292 0.0391  0.1059  0.1308  110 HIS D ND1 
10121 C  CD2 . HIS D 109 ? 0.4161 0.6021 0.9120 0.0356  0.0938  0.1192  110 HIS D CD2 
10122 C  CE1 . HIS D 109 ? 0.4110 0.6095 0.9503 0.0358  0.0944  0.1274  110 HIS D CE1 
10123 N  NE2 . HIS D 109 ? 0.4264 0.6159 0.9436 0.0341  0.0874  0.1206  110 HIS D NE2 
10124 N  N   . PHE D 110 ? 0.3163 0.4976 0.7707 0.0543  0.1143  0.1138  111 PHE D N   
10125 C  CA  . PHE D 110 ? 0.3192 0.4940 0.7685 0.0556  0.1081  0.1083  111 PHE D CA  
10126 C  C   . PHE D 110 ? 0.3291 0.5058 0.7788 0.0656  0.1146  0.1077  111 PHE D C   
10127 O  O   . PHE D 110 ? 0.4728 0.6498 0.9325 0.0673  0.1120  0.1074  111 PHE D O   
10128 C  CB  . PHE D 110 ? 0.3205 0.4854 0.7504 0.0531  0.1022  0.1022  111 PHE D CB  
10129 C  CG  . PHE D 110 ? 0.3122 0.4755 0.7406 0.0448  0.0958  0.1030  111 PHE D CG  
10130 C  CD1 . PHE D 110 ? 0.3588 0.5249 0.8002 0.0405  0.0906  0.1056  111 PHE D CD1 
10131 C  CD2 . PHE D 110 ? 0.3693 0.5283 0.7829 0.0424  0.0945  0.1007  111 PHE D CD2 
10132 C  CE1 . PHE D 110 ? 0.3017 0.4657 0.7389 0.0352  0.0844  0.1056  111 PHE D CE1 
10133 C  CE2 . PHE D 110 ? 0.3697 0.5277 0.7809 0.0364  0.0893  0.1018  111 PHE D CE2 
10134 C  CZ  . PHE D 110 ? 0.3807 0.5411 0.8026 0.0333  0.0844  0.1041  111 PHE D CZ  
10135 N  N   . GLN D 111 ? 0.3378 0.5158 0.7757 0.0735  0.1229  0.1077  112 GLN D N   
10136 C  CA  . GLN D 111 ? 0.3959 0.5767 0.8319 0.0858  0.1304  0.1076  112 GLN D CA  
10137 C  C   . GLN D 111 ? 0.3895 0.5819 0.8505 0.0872  0.1361  0.1159  112 GLN D C   
10138 O  O   . GLN D 111 ? 0.4512 0.6444 0.9171 0.0935  0.1370  0.1149  112 GLN D O   
10139 C  CB  . GLN D 111 ? 0.4035 0.5862 0.8233 0.0957  0.1399  0.1083  112 GLN D CB  
10140 C  CG  . GLN D 111 ? 0.4499 0.6207 0.8448 0.0977  0.1336  0.0984  112 GLN D CG  
10141 C  CD  . GLN D 111 ? 0.5197 0.6927 0.8973 0.1089  0.1424  0.0989  112 GLN D CD  
10142 O  OE1 . GLN D 111 ? 0.5219 0.7006 0.8964 0.1222  0.1521  0.1019  112 GLN D OE1 
10143 N  NE2 . GLN D 111 ? 0.5277 0.6965 0.8930 0.1047  0.1393  0.0965  112 GLN D NE2 
10144 N  N   . HIS D 112 ? 0.3540 0.5551 0.8324 0.0813  0.1393  0.1241  113 HIS D N   
10145 C  CA  . HIS D 112 ? 0.3475 0.5604 0.8547 0.0813  0.1437  0.1331  113 HIS D CA  
10146 C  C   . HIS D 112 ? 0.3517 0.5622 0.8724 0.0755  0.1328  0.1301  113 HIS D C   
10147 O  O   . HIS D 112 ? 0.3504 0.5688 0.8908 0.0789  0.1354  0.1346  113 HIS D O   
10148 C  CB  . HIS D 112 ? 0.3640 0.5848 0.8892 0.0751  0.1469  0.1420  113 HIS D CB  
10149 C  CG  . HIS D 112 ? 0.4457 0.6744 0.9684 0.0835  0.1616  0.1502  113 HIS D CG  
10150 N  ND1 . HIS D 112 ? 0.5124 0.7483 1.0517 0.0793  0.1666  0.1599  113 HIS D ND1 
10151 C  CD2 . HIS D 112 ? 0.5286 0.7590 1.0336 0.0970  0.1724  0.1506  113 HIS D CD2 
10152 C  CE1 . HIS D 112 ? 0.5236 0.7661 1.0559 0.0897  0.1809  0.1672  113 HIS D CE1 
10153 N  NE2 . HIS D 112 ? 0.5317 0.7711 1.0417 0.1013  0.1846  0.1613  113 HIS D NE2 
10154 N  N   . LEU D 113 ? 0.3225 0.5230 0.8328 0.0677  0.1210  0.1232  114 LEU D N   
10155 C  CA  . LEU D 113 ? 0.4026 0.5998 0.9211 0.0639  0.1106  0.1203  114 LEU D CA  
10156 C  C   . LEU D 113 ? 0.4032 0.5969 0.9156 0.0717  0.1117  0.1165  114 LEU D C   
10157 O  O   . LEU D 113 ? 0.4137 0.6124 0.9427 0.0742  0.1111  0.1188  114 LEU D O   
10158 C  CB  . LEU D 113 ? 0.3832 0.5707 0.8885 0.0561  0.0996  0.1150  114 LEU D CB  
10159 C  CG  . LEU D 113 ? 0.4026 0.5921 0.9162 0.0485  0.0941  0.1172  114 LEU D CG  
10160 C  CD1 . LEU D 113 ? 0.4415 0.6216 0.9377 0.0438  0.0850  0.1122  114 LEU D CD1 
10161 C  CD2 . LEU D 113 ? 0.3990 0.5954 0.9391 0.0469  0.0891  0.1207  114 LEU D CD2 
10162 N  N   . LEU D 114 ? 0.3882 0.5729 0.8779 0.0758  0.1124  0.1104  115 LEU D N   
10163 C  CA  . LEU D 114 ? 0.4016 0.5806 0.8844 0.0839  0.1120  0.1055  115 LEU D CA  
10164 C  C   . LEU D 114 ? 0.3651 0.5545 0.8594 0.0945  0.1224  0.1103  115 LEU D C   
10165 O  O   . LEU D 114 ? 0.3900 0.5799 0.8927 0.0991  0.1212  0.1097  115 LEU D O   
10166 C  CB  . LEU D 114 ? 0.3549 0.5227 0.8134 0.0878  0.1106  0.0978  115 LEU D CB  
10167 C  CG  . LEU D 114 ? 0.3669 0.5249 0.8179 0.0949  0.1062  0.0907  115 LEU D CG  
10168 C  CD1 . LEU D 114 ? 0.3613 0.5153 0.8233 0.0885  0.0971  0.0909  115 LEU D CD1 
10169 C  CD2 . LEU D 114 ? 0.4496 0.5953 0.8799 0.0968  0.1015  0.0825  115 LEU D CD2 
10170 N  N   . ASN D 115 ? 0.4133 0.6117 0.9089 0.0988  0.1333  0.1161  116 ASN D N   
10171 C  CA  . ASN D 115 ? 0.4355 0.6460 0.9424 0.1101  0.1459  0.1233  116 ASN D CA  
10172 C  C   . ASN D 115 ? 0.4014 0.6239 0.9408 0.1066  0.1464  0.1317  116 ASN D C   
10173 O  O   . ASN D 115 ? 0.4463 0.6764 0.9965 0.1158  0.1530  0.1355  116 ASN D O   
10174 C  CB  . ASN D 115 ? 0.5380 0.7557 1.0389 0.1154  0.1580  0.1295  116 ASN D CB  
10175 C  CG  . ASN D 115 ? 0.6139 0.8225 1.0832 0.1264  0.1604  0.1216  116 ASN D CG  
10176 O  OD1 . ASN D 115 ? 0.6089 0.8049 1.0626 0.1286  0.1517  0.1109  116 ASN D OD1 
10177 N  ND2 . ASN D 115 ? 0.7250 0.9396 1.1855 0.1338  0.1713  0.1268  116 ASN D ND2 
10178 N  N   . ASP D 116 ? 0.3802 0.6041 0.9350 0.0940  0.1388  0.1342  117 ASP D N   
10179 C  CA  . ASP D 116 ? 0.3643 0.5977 0.9508 0.0897  0.1355  0.1403  117 ASP D CA  
10180 C  C   . ASP D 116 ? 0.3767 0.6043 0.9632 0.0907  0.1266  0.1344  117 ASP D C   
10181 O  O   . ASP D 116 ? 0.3970 0.6333 1.0051 0.0943  0.1281  0.1389  117 ASP D O   
10182 C  CB  . ASP D 116 ? 0.4384 0.6721 1.0381 0.0772  0.1267  0.1420  117 ASP D CB  
10183 C  CG  . ASP D 116 ? 0.4632 0.7051 1.0724 0.0761  0.1357  0.1504  117 ASP D CG  
10184 O  OD1 . ASP D 116 ? 0.5053 0.7579 1.1229 0.0848  0.1499  0.1590  117 ASP D OD1 
10185 O  OD2 . ASP D 116 ? 0.4547 0.6923 1.0628 0.0673  0.1291  0.1491  117 ASP D OD2 
10186 N  N   . SER D 117 ? 0.3900 0.6032 0.9537 0.0875  0.1175  0.1252  118 SER D N   
10187 C  CA  . SER D 117 ? 0.3392 0.5453 0.9007 0.0892  0.1096  0.1201  118 SER D CA  
10188 C  C   . SER D 117 ? 0.3866 0.5949 0.9468 0.1019  0.1176  0.1197  118 SER D C   
10189 O  O   . SER D 117 ? 0.3525 0.5656 0.9287 0.1054  0.1165  0.1218  118 SER D O   
10190 C  CB  . SER D 117 ? 0.3662 0.5569 0.9044 0.0846  0.1005  0.1122  118 SER D CB  
10191 O  OG  . SER D 117 ? 0.3697 0.5538 0.9088 0.0852  0.0925  0.1091  118 SER D OG  
10192 N  N   . GLU D 118 ? 0.4153 0.6199 0.9555 0.1100  0.1252  0.1168  119 GLU D N   
10193 C  CA  . GLU D 118 ? 0.4249 0.6303 0.9593 0.1247  0.1327  0.1152  119 GLU D CA  
10194 C  C   . GLU D 118 ? 0.4898 0.7133 1.0490 0.1317  0.1440  0.1259  119 GLU D C   
10195 O  O   . GLU D 118 ? 0.4996 0.7260 1.0657 0.1406  0.1462  0.1261  119 GLU D O   
10196 C  CB  . GLU D 118 ? 0.3891 0.5880 0.8966 0.1337  0.1383  0.1099  119 GLU D CB  
10197 C  CG  . GLU D 118 ? 0.4087 0.6042 0.9038 0.1507  0.1429  0.1050  119 GLU D CG  
10198 C  CD  . GLU D 118 ? 0.5088 0.6967 0.9754 0.1611  0.1465  0.0984  119 GLU D CD  
10199 O  OE1 . GLU D 118 ? 0.5772 0.7662 1.0366 0.1557  0.1484  0.1001  119 GLU D OE1 
10200 O  OE2 . GLU D 118 ? 0.5160 0.6964 0.9670 0.1754  0.1465  0.0908  119 GLU D OE2 
10201 N  N   . ARG D 119 ? 0.4889 0.7247 1.0633 0.1277  0.1512  0.1354  120 ARG D N   
10202 C  CA  . ARG D 119 ? 0.4449 0.6996 1.0484 0.1332  0.1625  0.1480  120 ARG D CA  
10203 C  C   . ARG D 119 ? 0.3610 0.6212 0.9932 0.1276  0.1545  0.1505  120 ARG D C   
10204 O  O   . ARG D 119 ? 0.3666 0.6371 1.0152 0.1366  0.1611  0.1560  120 ARG D O   
10205 C  CB  . ARG D 119 ? 0.4475 0.7128 1.0651 0.1278  0.1698  0.1583  120 ARG D CB  
10206 C  CG  . ARG D 119 ? 0.4680 0.7441 1.0807 0.1419  0.1883  0.1671  120 ARG D CG  
10207 C  CD  . ARG D 119 ? 0.4762 0.7390 1.0476 0.1513  0.1899  0.1568  120 ARG D CD  
10208 N  N   . THR D 120 ? 0.3770 0.6304 1.0142 0.1141  0.1402  0.1465  121 THR D N   
10209 C  CA  . THR D 120 ? 0.3433 0.5999 1.0042 0.1092  0.1300  0.1473  121 THR D CA  
10210 C  C   . THR D 120 ? 0.4197 0.6698 1.0710 0.1173  0.1274  0.1413  121 THR D C   
10211 O  O   . THR D 120 ? 0.4510 0.7097 1.1246 0.1210  0.1272  0.1454  121 THR D O   
10212 C  CB  . THR D 120 ? 0.4035 0.6514 1.0632 0.0959  0.1142  0.1422  121 THR D CB  
10213 O  OG1 . THR D 120 ? 0.4033 0.6563 1.0728 0.0887  0.1157  0.1471  121 THR D OG1 
10214 C  CG2 . THR D 120 ? 0.3953 0.6464 1.0780 0.0928  0.1029  0.1426  121 THR D CG2 
10215 N  N   . LEU D 121 ? 0.3895 0.6241 1.0093 0.1202  0.1249  0.1319  122 LEU D N   
10216 C  CA  . LEU D 121 ? 0.4198 0.6461 1.0292 0.1288  0.1225  0.1258  122 LEU D CA  
10217 C  C   . LEU D 121 ? 0.4192 0.6573 1.0381 0.1436  0.1357  0.1310  122 LEU D C   
10218 O  O   . LEU D 121 ? 0.3838 0.6265 1.0181 0.1483  0.1345  0.1328  122 LEU D O   
10219 C  CB  . LEU D 121 ? 0.4170 0.6251 0.9938 0.1302  0.1186  0.1155  122 LEU D CB  
10220 C  CG  . LEU D 121 ? 0.4303 0.6260 0.9949 0.1386  0.1140  0.1078  122 LEU D CG  
10221 C  CD1 . LEU D 121 ? 0.4476 0.6250 0.9929 0.1314  0.1026  0.0996  122 LEU D CD1 
10222 C  CD2 . LEU D 121 ? 0.4220 0.6184 0.9739 0.1550  0.1246  0.1054  122 LEU D CD2 
10223 N  N   . GLN D 122 ? 0.4316 0.6747 1.0402 0.1518  0.1485  0.1340  123 GLN D N   
10224 C  CA  . GLN D 122 ? 0.4551 0.7109 1.0696 0.1683  0.1635  0.1405  123 GLN D CA  
10225 C  C   . GLN D 122 ? 0.4677 0.7433 1.1216 0.1676  0.1685  0.1532  123 GLN D C   
10226 O  O   . GLN D 122 ? 0.4034 0.6879 1.0671 0.1802  0.1762  0.1572  123 GLN D O   
10227 C  CB  . GLN D 122 ? 0.5086 0.7692 1.1083 0.1759  0.1768  0.1445  123 GLN D CB  
10228 C  CG  . GLN D 122 ? 0.5381 0.7842 1.0999 0.1890  0.1780  0.1333  123 GLN D CG  
10229 C  CD  . GLN D 122 ? 0.5872 0.8373 1.1328 0.1957  0.1894  0.1368  123 GLN D CD  
10230 O  OE1 . GLN D 122 ? 0.6194 0.8769 1.1764 0.1853  0.1921  0.1445  123 GLN D OE1 
10231 N  NE2 . GLN D 122 ? 0.6209 0.8657 1.1390 0.2141  0.1956  0.1310  123 GLN D NE2 
10232 N  N   . ALA D 123 ? 0.5553 0.8376 1.2329 0.1533  0.1632  0.1591  124 ALA D N   
10233 C  CA  . ALA D 123 ? 0.5599 0.8583 1.2736 0.1498  0.1652  0.1706  124 ALA D CA  
10234 C  C   . ALA D 123 ? 0.5319 0.8293 1.2631 0.1464  0.1528  0.1675  124 ALA D C   
10235 O  O   . ALA D 123 ? 0.4986 0.8046 1.2467 0.1489  0.1553  0.1738  124 ALA D O   
10236 C  CB  . ALA D 123 ? 0.5444 0.8456 1.2718 0.1353  0.1616  0.1763  124 ALA D CB  
10237 N  N   . THR D 124 ? 0.5116 0.7949 1.2308 0.1395  0.1382  0.1572  125 THR D N   
10238 C  CA  . THR D 124 ? 0.5465 0.8284 1.2815 0.1354  0.1249  0.1547  125 THR D CA  
10239 C  C   . THR D 124 ? 0.5664 0.8375 1.2837 0.1443  0.1220  0.1471  125 THR D C   
10240 O  O   . THR D 124 ? 0.5882 0.8631 1.3230 0.1462  0.1163  0.1481  125 THR D O   
10241 C  CB  . THR D 124 ? 0.4901 0.7617 1.2210 0.1211  0.1083  0.1490  125 THR D CB  
10242 O  OG1 . THR D 124 ? 0.5055 0.7599 1.2003 0.1186  0.1058  0.1404  125 THR D OG1 
10243 C  CG2 . THR D 124 ? 0.4913 0.7738 1.2473 0.1121  0.1075  0.1562  125 THR D CG2 
10244 N  N   . PHE D 125 ? 0.6069 0.8639 1.2909 0.1499  0.1249  0.1393  126 PHE D N   
10245 C  CA  . PHE D 125 ? 0.6185 0.8618 1.2854 0.1572  0.1198  0.1310  126 PHE D CA  
10246 C  C   . PHE D 125 ? 0.6197 0.8720 1.2977 0.1725  0.1284  0.1341  126 PHE D C   
10247 O  O   . PHE D 125 ? 0.6313 0.8776 1.3115 0.1753  0.1210  0.1304  126 PHE D O   
10248 C  CB  . PHE D 125 ? 0.6551 0.8806 1.2866 0.1596  0.1194  0.1214  126 PHE D CB  
10249 C  CG  . PHE D 125 ? 0.6895 0.9002 1.3073 0.1464  0.1063  0.1156  126 PHE D CG  
10250 C  CD1 . PHE D 125 ? 0.6907 0.9063 1.3221 0.1337  0.0994  0.1196  126 PHE D CD1 
10251 C  CD2 . PHE D 125 ? 0.7241 0.9159 1.3165 0.1475  0.1005  0.1064  126 PHE D CD2 
10252 C  CE1 . PHE D 125 ? 0.7075 0.9106 1.3250 0.1236  0.0886  0.1152  126 PHE D CE1 
10253 C  CE2 . PHE D 125 ? 0.7329 0.9129 1.3151 0.1360  0.0899  0.1032  126 PHE D CE2 
10254 C  CZ  . PHE D 125 ? 0.7324 0.9186 1.3259 0.1247  0.0848  0.1079  126 PHE D CZ  
10255 N  N   . PRO D 126 ? 0.5595 0.8263 1.2438 0.1833  0.1445  0.1415  127 PRO D N   
10256 C  CA  . PRO D 126 ? 0.6203 0.8968 1.3158 0.1990  0.1530  0.1453  127 PRO D CA  
10257 C  C   . PRO D 126 ? 0.5478 0.8363 1.2775 0.1943  0.1476  0.1520  127 PRO D C   
10258 O  O   . PRO D 126 ? 0.5741 0.8634 1.3066 0.2037  0.1481  0.1512  127 PRO D O   
10259 C  CB  . PRO D 126 ? 0.5888 0.8800 1.2842 0.2092  0.1714  0.1543  127 PRO D CB  
10260 C  CG  . PRO D 126 ? 0.4267 0.7092 1.0996 0.2051  0.1724  0.1502  127 PRO D CG  
10261 C  CD  . PRO D 126 ? 0.5266 0.7997 1.2031 0.1850  0.1563  0.1460  127 PRO D CD  
10262 N  N   . GLY D 127 ? 0.5614 0.8557 1.3102 0.1787  0.1405  0.1569  128 GLY D N   
10263 C  CA  . GLY D 127 ? 0.5764 0.8780 1.3513 0.1720  0.1318  0.1610  128 GLY D CA  
10264 C  C   . GLY D 127 ? 0.5695 0.8604 1.3459 0.1683  0.1155  0.1534  128 GLY D C   
10265 O  O   . GLY D 127 ? 0.6217 0.9149 1.4106 0.1707  0.1097  0.1538  128 GLY D O   
10266 N  N   . ALA D 128 ? 0.5943 0.8704 1.3501 0.1611  0.1073  0.1460  129 ALA D N   
10267 C  CA  . ALA D 128 ? 0.5721 0.8342 1.3192 0.1543  0.0907  0.1392  129 ALA D CA  
10268 C  C   . ALA D 128 ? 0.5575 0.8043 1.2829 0.1629  0.0887  0.1320  129 ALA D C   
10269 O  O   . ALA D 128 ? 0.5499 0.7926 1.2810 0.1636  0.0791  0.1305  129 ALA D O   
10270 C  CB  . ALA D 128 ? 0.5609 0.8120 1.2903 0.1420  0.0828  0.1349  129 ALA D CB  
10271 N  N   . PHE D 129 ? 0.5574 0.7951 1.2582 0.1699  0.0968  0.1272  130 PHE D N   
10272 C  CA  . PHE D 129 ? 0.6243 0.8445 1.3040 0.1774  0.0931  0.1191  130 PHE D CA  
10273 C  C   . PHE D 129 ? 0.6708 0.8959 1.3499 0.1945  0.1045  0.1190  130 PHE D C   
10274 O  O   . PHE D 129 ? 0.6333 0.8452 1.2995 0.2032  0.1013  0.1123  130 PHE D O   
10275 C  CB  . PHE D 129 ? 0.5597 0.7613 1.2097 0.1720  0.0892  0.1115  130 PHE D CB  
10276 C  CG  . PHE D 129 ? 0.5003 0.6977 1.1486 0.1568  0.0792  0.1121  130 PHE D CG  
10277 C  CD1 . PHE D 129 ? 0.4983 0.6875 1.1481 0.1518  0.0669  0.1115  130 PHE D CD1 
10278 C  CD2 . PHE D 129 ? 0.5051 0.7071 1.1499 0.1489  0.0825  0.1139  130 PHE D CD2 
10279 C  CE1 . PHE D 129 ? 0.4929 0.6788 1.1389 0.1403  0.0584  0.1125  130 PHE D CE1 
10280 C  CE2 . PHE D 129 ? 0.4704 0.6684 1.1124 0.1365  0.0733  0.1142  130 PHE D CE2 
10281 C  CZ  . PHE D 129 ? 0.4667 0.6568 1.1086 0.1328  0.0614  0.1134  130 PHE D CZ  
10282 N  N   . GLY D 130 ? 0.7577 1.0018 1.4516 0.2002  0.1180  0.1269  131 GLY D N   
10283 C  CA  . GLY D 130 ? 0.8340 1.0861 1.5284 0.2186  0.1309  0.1288  131 GLY D CA  
10284 C  C   . GLY D 130 ? 0.8804 1.1153 1.5396 0.2299  0.1337  0.1184  131 GLY D C   
10285 O  O   . GLY D 130 ? 0.8727 1.0987 1.5116 0.2248  0.1332  0.1139  131 GLY D O   
10286 N  N   . GLU D 131 ? 0.9275 1.1572 1.5800 0.2456  0.1352  0.1137  132 GLU D N   
10287 C  CA  . GLU D 131 ? 0.9564 1.1704 1.5770 0.2601  0.1373  0.1029  132 GLU D CA  
10288 C  C   . GLU D 131 ? 0.8867 1.0748 1.4851 0.2497  0.1220  0.0911  132 GLU D C   
10289 O  O   . GLU D 131 ? 0.9206 1.0955 1.4930 0.2553  0.1216  0.0823  132 GLU D O   
10290 C  CB  . GLU D 131 ? 1.0369 1.2501 1.6570 0.2797  0.1406  0.1000  132 GLU D CB  
10291 C  CG  . GLU D 131 ? 1.1156 1.3075 1.7023 0.2954  0.1376  0.0856  132 GLU D CG  
10292 C  CD  . GLU D 131 ? 1.1884 1.3918 1.7633 0.3183  0.1544  0.0874  132 GLU D CD  
10293 O  OE1 . GLU D 131 ? 1.1957 1.4242 1.7931 0.3241  0.1687  0.1010  132 GLU D OE1 
10294 O  OE2 . GLU D 131 ? 1.2225 1.4105 1.7664 0.3314  0.1532  0.0758  132 GLU D OE2 
10295 N  N   . LEU D 132 ? 0.8114 0.9934 1.4213 0.2351  0.1095  0.0919  133 LEU D N   
10296 C  CA  . LEU D 132 ? 0.7491 0.9097 1.3436 0.2232  0.0960  0.0844  133 LEU D CA  
10297 C  C   . LEU D 132 ? 0.7328 0.8915 1.3117 0.2163  0.0986  0.0827  133 LEU D C   
10298 O  O   . LEU D 132 ? 0.7650 0.9053 1.3240 0.2145  0.0913  0.0739  133 LEU D O   
10299 C  CB  . LEU D 132 ? 0.6898 0.8506 1.3008 0.2081  0.0855  0.0896  133 LEU D CB  
10300 C  CG  . LEU D 132 ? 0.6921 0.8524 1.3181 0.2125  0.0799  0.0913  133 LEU D CG  
10301 C  CD1 . LEU D 132 ? 0.6506 0.8094 1.2872 0.1980  0.0689  0.0959  133 LEU D CD1 
10302 C  CD2 . LEU D 132 ? 0.7241 0.8641 1.3352 0.2236  0.0745  0.0817  133 LEU D CD2 
10303 N  N   . TYR D 133 ? 0.7075 0.8855 1.2977 0.2126  0.1086  0.0916  134 TYR D N   
10304 C  CA  . TYR D 133 ? 0.6873 0.8658 1.2635 0.2080  0.1131  0.0910  134 TYR D CA  
10305 C  C   . TYR D 133 ? 0.7114 0.8924 1.2705 0.2257  0.1250  0.0881  134 TYR D C   
10306 O  O   . TYR D 133 ? 0.7180 0.8873 1.2535 0.2275  0.1235  0.0805  134 TYR D O   
10307 C  CB  . TYR D 133 ? 0.6987 0.8953 1.2950 0.1956  0.1176  0.1020  134 TYR D CB  
10308 C  CG  . TYR D 133 ? 0.7413 0.9435 1.3267 0.1957  0.1269  0.1039  134 TYR D CG  
10309 C  CD1 . TYR D 133 ? 0.7479 0.9360 1.3119 0.1882  0.1210  0.0971  134 TYR D CD1 
10310 C  CD2 . TYR D 133 ? 0.7413 0.9634 1.3391 0.2039  0.1422  0.1135  134 TYR D CD2 
10311 C  CE1 . TYR D 133 ? 0.7491 0.9420 1.3023 0.1889  0.1293  0.0988  134 TYR D CE1 
10312 C  CE2 . TYR D 133 ? 0.7458 0.9730 1.3333 0.2047  0.1513  0.1163  134 TYR D CE2 
10313 C  CZ  . TYR D 133 ? 0.7572 0.9693 1.3214 0.1973  0.1445  0.1083  134 TYR D CZ  
10314 O  OH  . TYR D 133 ? 0.7582 0.9752 1.3116 0.1986  0.1532  0.1111  134 TYR D OH  
10315 N  N   . THR D 134 ? 0.7014 0.8982 1.2723 0.2398  0.1369  0.0944  135 THR D N   
10316 C  CA  . THR D 134 ? 0.7480 0.9524 1.3044 0.2579  0.1515  0.0952  135 THR D CA  
10317 C  C   . THR D 134 ? 0.8383 1.0217 1.3629 0.2736  0.1462  0.0802  135 THR D C   
10318 O  O   . THR D 134 ? 0.8666 1.0490 1.3688 0.2868  0.1536  0.0765  135 THR D O   
10319 C  CB  . THR D 134 ? 0.6628 0.8907 1.2415 0.2709  0.1666  0.1075  135 THR D CB  
10320 O  OG1 . THR D 134 ? 0.6498 0.8716 1.2291 0.2828  0.1629  0.1023  135 THR D OG1 
10321 C  CG2 . THR D 134 ? 0.4897 0.7370 1.1051 0.2550  0.1685  0.1214  135 THR D CG2 
10322 N  N   . GLN D 135 ? 0.9334 1.0996 1.4564 0.2726  0.1327  0.0713  136 GLN D N   
10323 C  CA  . GLN D 135 ? 1.0137 1.1566 1.5100 0.2854  0.1237  0.0557  136 GLN D CA  
10324 C  C   . GLN D 135 ? 1.0232 1.1488 1.5004 0.2756  0.1136  0.0467  136 GLN D C   
10325 O  O   . GLN D 135 ? 1.0892 1.1991 1.5412 0.2882  0.1090  0.0343  136 GLN D O   
10326 C  CB  . GLN D 135 ? 1.0831 1.2118 1.5873 0.2855  0.1113  0.0501  136 GLN D CB  
10327 C  CG  . GLN D 135 ? 1.1452 1.2799 1.6519 0.3066  0.1185  0.0500  136 GLN D CG  
10328 C  CD  . GLN D 135 ? 1.2162 1.3302 1.6946 0.3269  0.1126  0.0339  136 GLN D CD  
10329 O  OE1 . GLN D 135 ? 1.2469 1.3680 1.7112 0.3491  0.1238  0.0325  136 GLN D OE1 
10330 N  NE2 . GLN D 135 ? 1.2292 1.3172 1.6999 0.3202  0.0945  0.0221  136 GLN D NE2 
10331 N  N   . ASN D 136 ? 0.9644 1.0929 1.4536 0.2539  0.1094  0.0528  137 ASN D N   
10332 C  CA  . ASN D 136 ? 0.9123 1.0240 1.3881 0.2421  0.0980  0.0455  137 ASN D CA  
10333 C  C   . ASN D 136 ? 0.8828 1.0059 1.3571 0.2316  0.1049  0.0521  137 ASN D C   
10334 O  O   . ASN D 136 ? 0.8774 0.9910 1.3471 0.2178  0.0963  0.0495  137 ASN D O   
10335 C  CB  . ASN D 136 ? 0.8759 0.9759 1.3653 0.2260  0.0840  0.0456  137 ASN D CB  
10336 C  CG  . ASN D 136 ? 0.8427 0.9330 1.3380 0.2350  0.0777  0.0414  137 ASN D CG  
10337 O  OD1 . ASN D 136 ? 0.8230 0.9190 1.3378 0.2281  0.0759  0.0486  137 ASN D OD1 
10338 N  ND2 . ASN D 136 ? 0.8586 0.9336 1.3366 0.2513  0.0734  0.0291  137 ASN D ND2 
10339 N  N   . ALA D 137 ? 0.8367 0.9806 1.3164 0.2384  0.1207  0.0615  138 ALA D N   
10340 C  CA  . ALA D 137 ? 0.8125 0.9687 1.2936 0.2292  0.1283  0.0693  138 ALA D CA  
10341 C  C   . ALA D 137 ? 0.8154 0.9583 1.2696 0.2309  0.1242  0.0598  138 ALA D C   
10342 O  O   . ALA D 137 ? 0.8036 0.9473 1.2575 0.2169  0.1224  0.0624  138 ALA D O   
10343 C  CB  . ALA D 137 ? 0.7652 0.9449 1.2570 0.2399  0.1467  0.0813  138 ALA D CB  
10344 N  N   . ARG D 138 ? 0.8639 0.9941 1.2954 0.2488  0.1219  0.0483  139 ARG D N   
10345 C  CA  . ARG D 138 ? 0.8783 0.9945 1.2839 0.2527  0.1159  0.0374  139 ARG D CA  
10346 C  C   . ARG D 138 ? 0.8190 0.9179 1.2265 0.2341  0.0989  0.0312  139 ARG D C   
10347 O  O   . ARG D 138 ? 0.8682 0.9621 1.2642 0.2282  0.0955  0.0280  139 ARG D O   
10348 C  CB  . ARG D 138 ? 1.0095 1.1130 1.3907 0.2770  0.1134  0.0243  139 ARG D CB  
10349 C  CG  . ARG D 138 ? 1.1226 1.2176 1.4749 0.2869  0.1117  0.0148  139 ARG D CG  
10350 C  CD  . ARG D 138 ? 1.2170 1.3152 1.5461 0.3162  0.1216  0.0106  139 ARG D CD  
10351 N  NE  . ARG D 138 ? 1.2804 1.3759 1.5819 0.3268  0.1236  0.0050  139 ARG D NE  
10352 C  CZ  . ARG D 138 ? 1.3327 1.4058 1.6113 0.3329  0.1075  -0.0124 139 ARG D CZ  
10353 N  NH1 . ARG D 138 ? 1.3374 1.3888 1.6198 0.3287  0.0884  -0.0253 139 ARG D NH1 
10354 N  NH2 . ARG D 138 ? 1.3604 1.4329 1.6139 0.3434  0.1100  -0.0166 139 ARG D NH2 
10355 N  N   . ALA D 139 ? 0.6977 0.7883 1.1206 0.2257  0.0890  0.0305  140 ALA D N   
10356 C  CA  . ALA D 139 ? 0.6542 0.7306 1.0825 0.2084  0.0746  0.0278  140 ALA D CA  
10357 C  C   . ALA D 139 ? 0.5948 0.6833 1.0329 0.1902  0.0786  0.0384  140 ALA D C   
10358 O  O   . ALA D 139 ? 0.5715 0.6524 1.0038 0.1801  0.0719  0.0358  140 ALA D O   
10359 C  CB  . ALA D 139 ? 0.6387 0.7063 1.0828 0.2042  0.0655  0.0279  140 ALA D CB  
10360 N  N   . PHE D 140 ? 0.4885 0.5959 0.9429 0.1865  0.0888  0.0500  141 PHE D N   
10361 C  CA  . PHE D 140 ? 0.5879 0.7074 1.0524 0.1712  0.0925  0.0597  141 PHE D CA  
10362 C  C   . PHE D 140 ? 0.5164 0.6400 0.9657 0.1728  0.0991  0.0591  141 PHE D C   
10363 O  O   . PHE D 140 ? 0.5456 0.6677 0.9931 0.1602  0.0956  0.0605  141 PHE D O   
10364 C  CB  . PHE D 140 ? 0.5717 0.7103 1.0581 0.1696  0.1012  0.0710  141 PHE D CB  
10365 C  CG  . PHE D 140 ? 0.4493 0.5851 0.9517 0.1661  0.0940  0.0727  141 PHE D CG  
10366 C  CD1 . PHE D 140 ? 0.4639 0.5978 0.9686 0.1794  0.0950  0.0698  141 PHE D CD1 
10367 C  CD2 . PHE D 140 ? 0.4332 0.5685 0.9470 0.1510  0.0864  0.0773  141 PHE D CD2 
10368 C  CE1 . PHE D 140 ? 0.5207 0.6519 1.0400 0.1766  0.0883  0.0716  141 PHE D CE1 
10369 C  CE2 . PHE D 140 ? 0.4547 0.5877 0.9816 0.1491  0.0799  0.0793  141 PHE D CE2 
10370 C  CZ  . PHE D 140 ? 0.4903 0.6212 1.0206 0.1614  0.0808  0.0766  141 PHE D CZ  
10371 N  N   . ARG D 141 ? 0.5716 0.7007 1.0093 0.1897  0.1091  0.0576  142 ARG D N   
10372 C  CA  . ARG D 141 ? 0.6666 0.7996 1.0876 0.1943  0.1162  0.0573  142 ARG D CA  
10373 C  C   . ARG D 141 ? 0.7430 0.8576 1.1455 0.1909  0.1038  0.0459  142 ARG D C   
10374 O  O   . ARG D 141 ? 0.7888 0.9050 1.1866 0.1818  0.1040  0.0478  142 ARG D O   
10375 C  CB  . ARG D 141 ? 0.7606 0.9009 1.1690 0.2167  0.1286  0.0571  142 ARG D CB  
10376 C  CG  . ARG D 141 ? 0.8550 0.9929 1.2379 0.2266  0.1326  0.0525  142 ARG D CG  
10377 C  CD  . ARG D 141 ? 0.9422 1.0971 1.3200 0.2451  0.1511  0.0608  142 ARG D CD  
10378 N  NE  . ARG D 141 ? 0.9974 1.1738 1.4037 0.2364  0.1634  0.0779  142 ARG D NE  
10379 C  CZ  . ARG D 141 ? 1.0442 1.2347 1.4570 0.2314  0.1740  0.0891  142 ARG D CZ  
10380 N  NH1 . ARG D 141 ? 1.0626 1.2483 1.4533 0.2344  0.1748  0.0855  142 ARG D NH1 
10381 N  NH2 . ARG D 141 ? 1.0416 1.2503 1.4842 0.2234  0.1830  0.1040  142 ARG D NH2 
10382 N  N   . ASP D 142 ? 0.7453 0.8422 1.1393 0.1980  0.0924  0.0341  143 ASP D N   
10383 C  CA  . ASP D 142 ? 0.7101 0.7884 1.0918 0.1943  0.0782  0.0231  143 ASP D CA  
10384 C  C   . ASP D 142 ? 0.6002 0.6773 0.9961 0.1724  0.0715  0.0287  143 ASP D C   
10385 O  O   . ASP D 142 ? 0.5842 0.6564 0.9723 0.1659  0.0668  0.0260  143 ASP D O   
10386 C  CB  . ASP D 142 ? 0.8206 0.8795 1.1978 0.2041  0.0655  0.0106  143 ASP D CB  
10387 C  CG  . ASP D 142 ? 0.9029 0.9585 1.2580 0.2286  0.0690  0.0010  143 ASP D CG  
10388 O  OD1 . ASP D 142 ? 0.9210 0.9934 1.2717 0.2393  0.0850  0.0083  143 ASP D OD1 
10389 O  OD2 . ASP D 142 ? 0.9518 0.9878 1.2943 0.2380  0.0555  -0.0134 143 ASP D OD2 
10390 N  N   . LEU D 143 ? 0.5717 0.6539 0.9875 0.1623  0.0713  0.0368  144 LEU D N   
10391 C  CA  . LEU D 143 ? 0.5864 0.6692 1.0144 0.1438  0.0662  0.0434  144 LEU D CA  
10392 C  C   . LEU D 143 ? 0.5401 0.6353 0.9651 0.1364  0.0740  0.0499  144 LEU D C   
10393 O  O   . LEU D 143 ? 0.5996 0.6905 1.0219 0.1262  0.0688  0.0498  144 LEU D O   
10394 C  CB  . LEU D 143 ? 0.4496 0.5381 0.8971 0.1373  0.0661  0.0515  144 LEU D CB  
10395 C  CG  . LEU D 143 ? 0.4299 0.5219 0.8874 0.1207  0.0629  0.0597  144 LEU D CG  
10396 C  CD1 . LEU D 143 ? 0.4333 0.5100 0.8891 0.1135  0.0514  0.0563  144 LEU D CD1 
10397 C  CD2 . LEU D 143 ? 0.4514 0.5512 0.9259 0.1168  0.0635  0.0676  144 LEU D CD2 
10398 N  N   . TYR D 144 ? 0.5393 0.6502 0.9666 0.1417  0.0866  0.0561  145 TYR D N   
10399 C  CA  . TYR D 144 ? 0.4970 0.6198 0.9240 0.1351  0.0942  0.0630  145 TYR D CA  
10400 C  C   . TYR D 144 ? 0.4914 0.6088 0.8978 0.1398  0.0944  0.0568  145 TYR D C   
10401 O  O   . TYR D 144 ? 0.5131 0.6330 0.9172 0.1303  0.0945  0.0597  145 TYR D O   
10402 C  CB  . TYR D 144 ? 0.5082 0.6490 0.9466 0.1403  0.1075  0.0723  145 TYR D CB  
10403 C  CG  . TYR D 144 ? 0.4891 0.6388 0.9507 0.1294  0.1066  0.0808  145 TYR D CG  
10404 C  CD1 . TYR D 144 ? 0.4642 0.6205 0.9336 0.1168  0.1063  0.0870  145 TYR D CD1 
10405 C  CD2 . TYR D 144 ? 0.4990 0.6497 0.9737 0.1327  0.1048  0.0819  145 TYR D CD2 
10406 C  CE1 . TYR D 144 ? 0.4582 0.6215 0.9472 0.1083  0.1035  0.0933  145 TYR D CE1 
10407 C  CE2 . TYR D 144 ? 0.4880 0.6465 0.9831 0.1238  0.1024  0.0889  145 TYR D CE2 
10408 C  CZ  . TYR D 144 ? 0.4642 0.6286 0.9659 0.1119  0.1013  0.0942  145 TYR D CZ  
10409 O  OH  . TYR D 144 ? 0.4718 0.6428 0.9923 0.1046  0.0971  0.0997  145 TYR D OH  
10410 N  N   . SER D 145 ? 0.5470 0.6565 0.9374 0.1553  0.0938  0.0477  146 SER D N   
10411 C  CA  . SER D 145 ? 0.5768 0.6790 0.9458 0.1617  0.0915  0.0398  146 SER D CA  
10412 C  C   . SER D 145 ? 0.5950 0.6834 0.9640 0.1494  0.0771  0.0342  146 SER D C   
10413 O  O   . SER D 145 ? 0.5931 0.6813 0.9540 0.1445  0.0760  0.0335  146 SER D O   
10414 C  CB  . SER D 145 ? 0.5992 0.6935 0.9498 0.1828  0.0910  0.0295  146 SER D CB  
10415 O  OG  . SER D 145 ? 0.6134 0.7225 0.9633 0.1958  0.1065  0.0365  146 SER D OG  
10416 N  N   . GLU D 146 ? 0.6230 0.7008 1.0032 0.1445  0.0666  0.0312  147 GLU D N   
10417 C  CA  . GLU D 146 ? 0.6504 0.7162 1.0360 0.1326  0.0536  0.0285  147 GLU D CA  
10418 C  C   . GLU D 146 ? 0.6032 0.6787 0.9983 0.1164  0.0568  0.0391  147 GLU D C   
10419 O  O   . GLU D 146 ? 0.5857 0.6569 0.9789 0.1086  0.0511  0.0381  147 GLU D O   
10420 C  CB  . GLU D 146 ? 0.7562 0.8102 1.1550 0.1311  0.0436  0.0261  147 GLU D CB  
10421 C  CG  . GLU D 146 ? 0.8539 0.8937 1.2430 0.1468  0.0362  0.0131  147 GLU D CG  
10422 C  CD  . GLU D 146 ? 0.9353 0.9616 1.3113 0.1509  0.0254  0.0015  147 GLU D CD  
10423 O  OE1 . GLU D 146 ? 0.9551 0.9776 1.3388 0.1380  0.0183  0.0035  147 GLU D OE1 
10424 O  OE2 . GLU D 146 ? 0.9891 1.0089 1.3471 0.1680  0.0238  -0.0096 147 GLU D OE2 
10425 N  N   . LEU D 147 ? 0.5789 0.6676 0.9847 0.1120  0.0653  0.0488  148 LEU D N   
10426 C  CA  . LEU D 147 ? 0.4911 0.5891 0.9041 0.0989  0.0680  0.0579  148 LEU D CA  
10427 C  C   . LEU D 147 ? 0.4362 0.5402 0.8372 0.0990  0.0740  0.0582  148 LEU D C   
10428 O  O   . LEU D 147 ? 0.4281 0.5323 0.8283 0.0895  0.0714  0.0606  148 LEU D O   
10429 C  CB  . LEU D 147 ? 0.5085 0.6186 0.9356 0.0962  0.0742  0.0665  148 LEU D CB  
10430 C  CG  . LEU D 147 ? 0.4653 0.5708 0.9055 0.0931  0.0678  0.0686  148 LEU D CG  
10431 C  CD1 . LEU D 147 ? 0.4797 0.5977 0.9335 0.0912  0.0729  0.0764  148 LEU D CD1 
10432 C  CD2 . LEU D 147 ? 0.4069 0.5046 0.8498 0.0827  0.0591  0.0706  148 LEU D CD2 
10433 N  N   . ARG D 148 ? 0.4495 0.5590 0.8410 0.1108  0.0827  0.0565  149 ARG D N   
10434 C  CA  . ARG D 148 ? 0.4630 0.5779 0.8418 0.1134  0.0891  0.0571  149 ARG D CA  
10435 C  C   . ARG D 148 ? 0.5521 0.6552 0.9177 0.1126  0.0798  0.0487  149 ARG D C   
10436 O  O   . ARG D 148 ? 0.5585 0.6643 0.9201 0.1059  0.0803  0.0510  149 ARG D O   
10437 C  CB  . ARG D 148 ? 0.4812 0.6029 0.8506 0.1293  0.1001  0.0571  149 ARG D CB  
10438 C  CG  . ARG D 148 ? 0.4627 0.6000 0.8480 0.1294  0.1117  0.0681  149 ARG D CG  
10439 C  CD  . ARG D 148 ? 0.4615 0.6075 0.8378 0.1458  0.1247  0.0705  149 ARG D CD  
10440 N  NE  . ARG D 148 ? 0.4693 0.6303 0.8656 0.1469  0.1352  0.0816  149 ARG D NE  
10441 C  CZ  . ARG D 148 ? 0.4962 0.6592 0.8998 0.1553  0.1374  0.0816  149 ARG D CZ  
10442 N  NH1 . ARG D 148 ? 0.4988 0.6486 0.8900 0.1638  0.1295  0.0707  149 ARG D NH1 
10443 N  NH2 . ARG D 148 ? 0.4662 0.6442 0.8911 0.1554  0.1468  0.0926  149 ARG D NH2 
10444 N  N   . LEU D 149 ? 0.6157 0.7052 0.9759 0.1198  0.0703  0.0386  150 LEU D N   
10445 C  CA  . LEU D 149 ? 0.5916 0.6687 0.9428 0.1194  0.0590  0.0297  150 LEU D CA  
10446 C  C   . LEU D 149 ? 0.5871 0.6622 0.9522 0.1027  0.0519  0.0346  150 LEU D C   
10447 O  O   . LEU D 149 ? 0.6313 0.7047 0.9916 0.0981  0.0482  0.0332  150 LEU D O   
10448 C  CB  . LEU D 149 ? 0.6920 0.7536 1.0380 0.1307  0.0482  0.0173  150 LEU D CB  
10449 C  CG  . LEU D 149 ? 0.7545 0.8165 1.0805 0.1509  0.0542  0.0105  150 LEU D CG  
10450 C  CD1 . LEU D 149 ? 0.7836 0.8279 1.1030 0.1630  0.0410  -0.0037 150 LEU D CD1 
10451 C  CD2 . LEU D 149 ? 0.7566 0.8238 1.0639 0.1567  0.0597  0.0096  150 LEU D CD2 
10452 N  N   . TYR D 150 ? 0.5638 0.6399 0.9456 0.0946  0.0506  0.0409  151 TYR D N   
10453 C  CA  . TYR D 150 ? 0.5441 0.6196 0.9384 0.0806  0.0455  0.0475  151 TYR D CA  
10454 C  C   . TYR D 150 ? 0.6147 0.7019 1.0060 0.0732  0.0528  0.0549  151 TYR D C   
10455 O  O   . TYR D 150 ? 0.5966 0.6827 0.9891 0.0656  0.0488  0.0568  151 TYR D O   
10456 C  CB  . TYR D 150 ? 0.5532 0.6288 0.9634 0.0757  0.0441  0.0539  151 TYR D CB  
10457 C  CG  . TYR D 150 ? 0.5697 0.6457 0.9915 0.0636  0.0402  0.0623  151 TYR D CG  
10458 C  CD1 . TYR D 150 ? 0.6275 0.6939 1.0553 0.0593  0.0307  0.0606  151 TYR D CD1 
10459 C  CD2 . TYR D 150 ? 0.5060 0.5923 0.9332 0.0574  0.0456  0.0721  151 TYR D CD2 
10460 C  CE1 . TYR D 150 ? 0.6309 0.6994 1.0702 0.0494  0.0288  0.0703  151 TYR D CE1 
10461 C  CE2 . TYR D 150 ? 0.5393 0.6266 0.9743 0.0487  0.0430  0.0803  151 TYR D CE2 
10462 C  CZ  . TYR D 150 ? 0.6286 0.7078 1.0698 0.0449  0.0356  0.0803  151 TYR D CZ  
10463 O  OH  . TYR D 150 ? 0.6604 0.7422 1.1103 0.0375  0.0346  0.0904  151 TYR D OH  
10464 N  N   . TYR D 151 ? 0.5920 0.6906 0.9812 0.0755  0.0632  0.0595  152 TYR D N   
10465 C  CA  . TYR D 151 ? 0.5571 0.6659 0.9441 0.0695  0.0696  0.0659  152 TYR D CA  
10466 C  C   . TYR D 151 ? 0.5674 0.6750 0.9399 0.0723  0.0702  0.0615  152 TYR D C   
10467 O  O   . TYR D 151 ? 0.5595 0.6708 0.9304 0.0653  0.0709  0.0651  152 TYR D O   
10468 C  CB  . TYR D 151 ? 0.5341 0.6545 0.9255 0.0720  0.0795  0.0715  152 TYR D CB  
10469 C  CG  . TYR D 151 ? 0.5373 0.6667 0.9253 0.0687  0.0863  0.0764  152 TYR D CG  
10470 C  CD1 . TYR D 151 ? 0.3446 0.4778 0.7383 0.0587  0.0846  0.0820  152 TYR D CD1 
10471 C  CD2 . TYR D 151 ? 0.3645 0.4985 0.7430 0.0767  0.0944  0.0758  152 TYR D CD2 
10472 C  CE1 . TYR D 151 ? 0.3375 0.4777 0.7288 0.0559  0.0897  0.0858  152 TYR D CE1 
10473 C  CE2 . TYR D 151 ? 0.3569 0.4986 0.7341 0.0736  0.1005  0.0810  152 TYR D CE2 
10474 C  CZ  . TYR D 151 ? 0.4473 0.5914 0.8314 0.0627  0.0976  0.0856  152 TYR D CZ  
10475 O  OH  . TYR D 151 ? 0.3368 0.4874 0.7202 0.0599  0.1027  0.0902  152 TYR D OH  
10476 N  N   . ARG D 152 ? 0.6349 0.7369 0.9958 0.0838  0.0695  0.0532  153 ARG D N   
10477 C  CA  . ARG D 152 ? 0.7522 0.8536 1.0968 0.0895  0.0708  0.0487  153 ARG D CA  
10478 C  C   . ARG D 152 ? 0.8360 0.9286 1.1791 0.0842  0.0595  0.0437  153 ARG D C   
10479 O  O   . ARG D 152 ? 0.8503 0.9420 1.1805 0.0880  0.0589  0.0396  153 ARG D O   
10480 C  CB  . ARG D 152 ? 0.8175 0.9156 1.1474 0.1063  0.0733  0.0411  153 ARG D CB  
10481 C  CG  . ARG D 152 ? 0.8992 1.0087 1.2186 0.1142  0.0870  0.0462  153 ARG D CG  
10482 C  CD  . ARG D 152 ? 0.9857 1.0925 1.2877 0.1334  0.0903  0.0395  153 ARG D CD  
10483 N  NE  . ARG D 152 ? 1.0598 1.1767 1.3493 0.1419  0.1029  0.0449  153 ARG D NE  
10484 C  CZ  . ARG D 152 ? 1.1128 1.2425 1.4075 0.1473  0.1173  0.0548  153 ARG D CZ  
10485 N  NH1 . ARG D 152 ? 1.1193 1.2532 1.4306 0.1451  0.1202  0.0593  153 ARG D NH1 
10486 N  NH2 . ARG D 152 ? 1.1210 1.2596 1.4057 0.1550  0.1289  0.0610  153 ARG D NH2 
10487 N  N   . GLY D 153 ? 0.8575 0.9442 1.2152 0.0757  0.0510  0.0448  154 GLY D N   
10488 C  CA  . GLY D 153 ? 0.9011 0.9809 1.2633 0.0696  0.0406  0.0423  154 GLY D CA  
10489 C  C   . GLY D 153 ? 0.9639 1.0290 1.3262 0.0764  0.0279  0.0309  154 GLY D C   
10490 O  O   . GLY D 153 ? 0.9457 1.0038 1.3116 0.0738  0.0176  0.0266  154 GLY D O   
10491 N  N   . ALA D 154 ? 1.0596 1.1199 1.4193 0.0857  0.0279  0.0259  155 ALA D N   
10492 C  CA  . ALA D 154 ? 1.2016 1.2463 1.5620 0.0935  0.0147  0.0141  155 ALA D CA  
10493 C  C   . ALA D 154 ? 1.3670 1.4040 1.7515 0.0824  0.0041  0.0175  155 ALA D C   
10494 O  O   . ALA D 154 ? 1.3770 1.4217 1.7750 0.0712  0.0091  0.0296  155 ALA D O   
10495 C  CB  . ALA D 154 ? 1.1616 1.2041 1.5133 0.1068  0.0186  0.0090  155 ALA D CB  
10496 N  N   . ASN D 155 ? 1.5508 1.5723 1.9408 0.0866  -0.0110 0.0071  156 ASN D N   
10497 C  CA  . ASN D 155 ? 1.5623 1.5756 1.9780 0.0760  -0.0229 0.0105  156 ASN D CA  
10498 C  C   . ASN D 155 ? 1.5399 1.5503 1.9719 0.0730  -0.0227 0.0166  156 ASN D C   
10499 O  O   . ASN D 155 ? 1.5667 1.5695 2.0221 0.0655  -0.0319 0.0206  156 ASN D O   
10500 C  CB  . ASN D 155 ? 1.6078 1.6044 2.0261 0.0818  -0.0413 -0.0039 156 ASN D CB  
10501 N  N   . LEU D 156 ? 1.4038 1.4206 1.8247 0.0792  -0.0118 0.0179  157 LEU D N   
10502 C  CA  . LEU D 156 ? 1.2763 1.2909 1.7091 0.0787  -0.0108 0.0226  157 LEU D CA  
10503 C  C   . LEU D 156 ? 1.1607 1.1785 1.6162 0.0653  -0.0108 0.0368  157 LEU D C   
10504 O  O   . LEU D 156 ? 1.1453 1.1754 1.6020 0.0568  -0.0030 0.0476  157 LEU D O   
10505 C  CB  . LEU D 156 ? 1.2074 1.2339 1.6272 0.0846  0.0035  0.0257  157 LEU D CB  
10506 C  CG  . LEU D 156 ? 1.1531 1.1767 1.5560 0.1008  0.0060  0.0152  157 LEU D CG  
10507 C  CD1 . LEU D 156 ? 1.1126 1.1352 1.4945 0.1103  0.0058  0.0056  157 LEU D CD1 
10508 C  CD2 . LEU D 156 ? 1.0962 1.1340 1.4970 0.1024  0.0204  0.0234  157 LEU D CD2 
10509 N  N   . HIS D 157 ? 1.1220 1.1283 1.5951 0.0646  -0.0198 0.0369  158 HIS D N   
10510 C  CA  . HIS D 157 ? 1.0238 1.0341 1.5153 0.0560  -0.0168 0.0515  158 HIS D CA  
10511 C  C   . HIS D 157 ? 0.9733 0.9894 1.4567 0.0617  -0.0079 0.0530  158 HIS D C   
10512 O  O   . HIS D 157 ? 0.9632 0.9700 1.4466 0.0700  -0.0123 0.0453  158 HIS D O   
10513 C  CB  . HIS D 157 ? 1.0146 1.0101 1.5314 0.0525  -0.0301 0.0526  158 HIS D CB  
10514 N  N   . LEU D 158 ? 0.9256 0.9571 1.4029 0.0578  0.0039  0.0625  159 LEU D N   
10515 C  CA  . LEU D 158 ? 0.9117 0.9511 1.3838 0.0621  0.0123  0.0651  159 LEU D CA  
10516 C  C   . LEU D 158 ? 0.9689 1.0014 1.4561 0.0626  0.0080  0.0694  159 LEU D C   
10517 O  O   . LEU D 158 ? 1.0317 1.0618 1.5163 0.0706  0.0088  0.0645  159 LEU D O   
10518 C  CB  . LEU D 158 ? 0.7961 0.8514 1.2635 0.0562  0.0223  0.0752  159 LEU D CB  
10519 C  CG  . LEU D 158 ? 0.6855 0.7506 1.1505 0.0591  0.0299  0.0790  159 LEU D CG  
10520 C  CD1 . LEU D 158 ? 0.6415 0.7089 1.0957 0.0685  0.0345  0.0700  159 LEU D CD1 
10521 C  CD2 . LEU D 158 ? 0.6507 0.7287 1.1125 0.0529  0.0363  0.0879  159 LEU D CD2 
10522 N  N   . GLU D 159 ? 1.0025 1.0326 1.5057 0.0545  0.0042  0.0798  160 GLU D N   
10523 C  CA  . GLU D 159 ? 0.9789 1.0012 1.4994 0.0539  -0.0007 0.0862  160 GLU D CA  
10524 C  C   . GLU D 159 ? 1.0199 1.0278 1.5430 0.0626  -0.0086 0.0745  160 GLU D C   
10525 O  O   . GLU D 159 ? 1.0352 1.0428 1.5598 0.0676  -0.0069 0.0753  160 GLU D O   
10526 C  CB  . GLU D 159 ? 0.9909 1.0087 1.5311 0.0453  -0.0063 0.0966  160 GLU D CB  
10527 C  CG  . GLU D 159 ? 1.4569 1.4871 1.9952 0.0375  0.0000  0.1072  160 GLU D CG  
10528 C  CD  . GLU D 159 ? 1.4564 1.4897 1.9812 0.0369  0.0005  0.0982  160 GLU D CD  
10529 O  OE1 . GLU D 159 ? 1.4646 1.4931 1.9771 0.0435  -0.0017 0.0842  160 GLU D OE1 
10530 O  OE2 . GLU D 159 ? 1.4471 1.4881 1.9731 0.0308  0.0036  0.1059  160 GLU D OE2 
10531 N  N   . GLU D 160 ? 1.0126 1.0083 1.5357 0.0654  -0.0181 0.0630  161 GLU D N   
10532 C  CA  . GLU D 160 ? 1.0249 1.0045 1.5490 0.0752  -0.0280 0.0499  161 GLU D CA  
10533 C  C   . GLU D 160 ? 0.9732 0.9577 1.4784 0.0872  -0.0207 0.0417  161 GLU D C   
10534 O  O   . GLU D 160 ? 1.0139 0.9920 1.5228 0.0941  -0.0228 0.0391  161 GLU D O   
10535 C  CB  . GLU D 160 ? 1.0913 1.0581 1.6146 0.0772  -0.0400 0.0374  161 GLU D CB  
10536 C  CG  . GLU D 160 ? 1.1644 1.1123 1.7124 0.0749  -0.0562 0.0355  161 GLU D CG  
10537 C  CD  . GLU D 160 ? 1.2351 1.1673 1.7785 0.0821  -0.0709 0.0176  161 GLU D CD  
10538 O  OE1 . GLU D 160 ? 1.2574 1.1935 1.7942 0.0792  -0.0717 0.0148  161 GLU D OE1 
10539 O  OE2 . GLU D 160 ? 1.2587 1.1741 1.8040 0.0917  -0.0821 0.0057  161 GLU D OE2 
10540 N  N   . THR D 161 ? 0.8654 0.8616 1.3516 0.0899  -0.0118 0.0386  162 THR D N   
10541 C  CA  . THR D 161 ? 0.7809 0.7845 1.2507 0.1014  -0.0030 0.0329  162 THR D CA  
10542 C  C   . THR D 161 ? 0.6614 0.6740 1.1386 0.1006  0.0043  0.0423  162 THR D C   
10543 O  O   . THR D 161 ? 0.6321 0.6424 1.1077 0.1108  0.0052  0.0376  162 THR D O   
10544 C  CB  . THR D 161 ? 0.8291 0.8463 1.2818 0.1018  0.0070  0.0327  162 THR D CB  
10545 O  OG1 . THR D 161 ? 0.8511 0.8622 1.3003 0.0983  0.0002  0.0279  162 THR D OG1 
10546 C  CG2 . THR D 161 ? 0.8512 0.8723 1.2872 0.1167  0.0138  0.0246  162 THR D CG2 
10547 N  N   . LEU D 162 ? 0.5834 0.6063 1.0684 0.0896  0.0090  0.0551  163 LEU D N   
10548 C  CA  . LEU D 162 ? 0.5621 0.5933 1.0549 0.0883  0.0140  0.0644  163 LEU D CA  
10549 C  C   . LEU D 162 ? 0.6427 0.6612 1.1484 0.0918  0.0063  0.0641  163 LEU D C   
10550 O  O   . LEU D 162 ? 0.6114 0.6316 1.1175 0.0995  0.0088  0.0623  163 LEU D O   
10551 C  CB  . LEU D 162 ? 0.5225 0.5633 1.0203 0.0772  0.0173  0.0773  163 LEU D CB  
10552 C  CG  . LEU D 162 ? 0.4685 0.5231 0.9549 0.0736  0.0253  0.0790  163 LEU D CG  
10553 C  CD1 . LEU D 162 ? 0.4013 0.4638 0.8917 0.0648  0.0272  0.0911  163 LEU D CD1 
10554 C  CD2 . LEU D 162 ? 0.4105 0.4759 0.8904 0.0803  0.0334  0.0762  163 LEU D CD2 
10555 N  N   . ALA D 163 ? 0.6915 0.6976 1.2098 0.0862  -0.0030 0.0665  164 ALA D N   
10556 C  CA  . ALA D 163 ? 0.7254 0.7183 1.2595 0.0881  -0.0112 0.0680  164 ALA D CA  
10557 C  C   . ALA D 163 ? 0.8023 0.7846 1.3311 0.1012  -0.0156 0.0543  164 ALA D C   
10558 O  O   . ALA D 163 ? 0.8284 0.8097 1.3621 0.1066  -0.0149 0.0558  164 ALA D O   
10559 C  CB  . ALA D 163 ? 0.7792 0.7597 1.3301 0.0803  -0.0212 0.0719  164 ALA D CB  
10560 N  N   . GLU D 164 ? 0.8323 0.8072 1.3496 0.1076  -0.0200 0.0408  165 GLU D N   
10561 C  CA  . GLU D 164 ? 0.9302 0.8937 1.4398 0.1225  -0.0251 0.0268  165 GLU D CA  
10562 C  C   . GLU D 164 ? 0.9046 0.8825 1.4013 0.1321  -0.0125 0.0263  165 GLU D C   
10563 O  O   . GLU D 164 ? 0.9660 0.9389 1.4630 0.1429  -0.0136 0.0215  165 GLU D O   
10564 C  CB  . GLU D 164 ? 1.0514 1.0033 1.5490 0.1291  -0.0336 0.0118  165 GLU D CB  
10565 C  CG  . GLU D 164 ? 1.1650 1.1072 1.6478 0.1481  -0.0371 -0.0039 165 GLU D CG  
10566 C  CD  . GLU D 164 ? 1.2652 1.1829 1.7520 0.1537  -0.0560 -0.0180 165 GLU D CD  
10567 O  OE1 . GLU D 164 ? 1.2897 1.1967 1.7993 0.1422  -0.0668 -0.0130 165 GLU D OE1 
10568 O  OE2 . GLU D 164 ? 1.3108 1.2198 1.7791 0.1702  -0.0606 -0.0337 165 GLU D OE2 
10569 N  N   . PHE D 165 ? 0.8381 0.8342 1.3259 0.1282  -0.0007 0.0320  166 PHE D N   
10570 C  CA  . PHE D 165 ? 0.7261 0.7382 1.2075 0.1353  0.0117  0.0345  166 PHE D CA  
10571 C  C   . PHE D 165 ? 0.6076 0.6228 1.1035 0.1341  0.0126  0.0425  166 PHE D C   
10572 O  O   . PHE D 165 ? 0.5735 0.5901 1.0688 0.1453  0.0154  0.0392  166 PHE D O   
10573 C  CB  . PHE D 165 ? 0.5888 0.6192 1.0642 0.1283  0.0227  0.0415  166 PHE D CB  
10574 C  CG  . PHE D 165 ? 0.5411 0.5890 1.0190 0.1317  0.0341  0.0478  166 PHE D CG  
10575 C  CD1 . PHE D 165 ? 0.5265 0.5809 0.9955 0.1452  0.0420  0.0429  166 PHE D CD1 
10576 C  CD2 . PHE D 165 ? 0.4999 0.5580 0.9900 0.1223  0.0365  0.0590  166 PHE D CD2 
10577 C  CE1 . PHE D 165 ? 0.5282 0.5997 1.0044 0.1478  0.0523  0.0500  166 PHE D CE1 
10578 C  CE2 . PHE D 165 ? 0.5180 0.5917 1.0138 0.1251  0.0449  0.0643  166 PHE D CE2 
10579 C  CZ  . PHE D 165 ? 0.5273 0.6081 1.0180 0.1371  0.0529  0.0603  166 PHE D CZ  
10580 N  N   . TRP D 166 ? 0.6444 0.6612 1.1526 0.1218  0.0104  0.0535  167 TRP D N   
10581 C  CA  . TRP D 166 ? 0.6261 0.6454 1.1473 0.1208  0.0103  0.0618  167 TRP D CA  
10582 C  C   . TRP D 166 ? 0.7346 0.7370 1.2629 0.1290  0.0016  0.0560  167 TRP D C   
10583 O  O   . TRP D 166 ? 0.7572 0.7625 1.2903 0.1358  0.0036  0.0571  167 TRP D O   
10584 C  CB  . TRP D 166 ? 0.6581 0.6800 1.1886 0.1082  0.0087  0.0746  167 TRP D CB  
10585 C  CG  . TRP D 166 ? 0.6647 0.7041 1.1896 0.1016  0.0169  0.0815  167 TRP D CG  
10586 C  CD1 . TRP D 166 ? 0.6686 0.7112 1.1908 0.0921  0.0174  0.0869  167 TRP D CD1 
10587 C  CD2 . TRP D 166 ? 0.6924 0.7478 1.2155 0.1043  0.0247  0.0836  167 TRP D CD2 
10588 N  NE1 . TRP D 166 ? 0.6920 0.7504 1.2090 0.0893  0.0246  0.0912  167 TRP D NE1 
10589 C  CE2 . TRP D 166 ? 0.6647 0.7310 1.1835 0.0961  0.0286  0.0894  167 TRP D CE2 
10590 C  CE3 . TRP D 166 ? 0.7018 0.7636 1.2283 0.1130  0.0284  0.0815  167 TRP D CE3 
10591 C  CZ2 . TRP D 166 ? 0.6614 0.7434 1.1804 0.0960  0.0347  0.0924  167 TRP D CZ2 
10592 C  CZ3 . TRP D 166 ? 0.6775 0.7564 1.2061 0.1124  0.0353  0.0856  167 TRP D CZ3 
10593 C  CH2 . TRP D 166 ? 0.6891 0.7773 1.2144 0.1037  0.0377  0.0906  167 TRP D CH2 
10594 N  N   . ALA D 167 ? 0.7611 0.7459 1.2915 0.1284  -0.0088 0.0495  168 ALA D N   
10595 C  CA  . ALA D 167 ? 0.8069 0.7728 1.3449 0.1364  -0.0194 0.0422  168 ALA D CA  
10596 C  C   . ALA D 167 ? 0.8404 0.8072 1.3667 0.1529  -0.0158 0.0316  168 ALA D C   
10597 O  O   . ALA D 167 ? 0.8661 0.8307 1.3996 0.1594  -0.0164 0.0326  168 ALA D O   
10598 C  CB  . ALA D 167 ? 0.7962 0.7433 1.3376 0.1344  -0.0322 0.0342  168 ALA D CB  
10599 N  N   . ARG D 168 ? 0.8881 0.8594 1.3964 0.1605  -0.0112 0.0224  169 ARG D N   
10600 C  CA  . ARG D 168 ? 0.9296 0.9044 1.4251 0.1779  -0.0054 0.0137  169 ARG D CA  
10601 C  C   . ARG D 168 ? 0.9516 0.9454 1.4539 0.1786  0.0063  0.0240  169 ARG D C   
10602 O  O   . ARG D 168 ? 0.9992 0.9906 1.5052 0.1891  0.0062  0.0219  169 ARG D O   
10603 C  CB  . ARG D 168 ? 0.9654 0.9451 1.4397 0.1856  -0.0001 0.0053  169 ARG D CB  
10604 C  CG  . ARG D 168 ? 1.4246 1.4244 1.8867 0.1968  0.0161  0.0069  169 ARG D CG  
10605 C  CD  . ARG D 168 ? 1.4430 1.4458 1.9063 0.2121  0.0208  0.0053  169 ARG D CD  
10606 N  NE  . ARG D 168 ? 1.4848 1.4676 1.9379 0.2285  0.0106  -0.0095 169 ARG D NE  
10607 C  CZ  . ARG D 168 ? 1.5143 1.4955 1.9669 0.2437  0.0122  -0.0131 169 ARG D CZ  
10608 N  NH1 . ARG D 168 ? 1.4966 1.4964 1.9601 0.2441  0.0240  -0.0022 169 ARG D NH1 
10609 N  NH2 . ARG D 168 ? 1.5514 1.5125 1.9934 0.2592  0.0013  -0.0279 169 ARG D NH2 
10610 N  N   . LEU D 169 ? 0.9078 0.9197 1.4129 0.1679  0.0154  0.0347  170 LEU D N   
10611 C  CA  . LEU D 169 ? 0.9033 0.9339 1.4163 0.1686  0.0254  0.0436  170 LEU D CA  
10612 C  C   . LEU D 169 ? 0.8962 0.9216 1.4240 0.1695  0.0201  0.0478  170 LEU D C   
10613 O  O   . LEU D 169 ? 0.9087 0.9414 1.4408 0.1793  0.0248  0.0482  170 LEU D O   
10614 C  CB  . LEU D 169 ? 0.8751 0.9217 1.3917 0.1550  0.0313  0.0541  170 LEU D CB  
10615 C  CG  . LEU D 169 ? 0.8616 0.9290 1.3864 0.1565  0.0414  0.0616  170 LEU D CG  
10616 C  CD1 . LEU D 169 ? 0.8564 0.9334 1.3734 0.1694  0.0517  0.0572  170 LEU D CD1 
10617 C  CD2 . LEU D 169 ? 0.8443 0.9239 1.3733 0.1430  0.0440  0.0706  170 LEU D CD2 
10618 N  N   . LEU D 170 ? 0.8397 0.8525 1.3760 0.1600  0.0105  0.0517  171 LEU D N   
10619 C  CA  . LEU D 170 ? 0.7966 0.8016 1.3465 0.1610  0.0044  0.0561  171 LEU D CA  
10620 C  C   . LEU D 170 ? 0.7912 0.7824 1.3392 0.1761  -0.0005 0.0450  171 LEU D C   
10621 O  O   . LEU D 170 ? 0.7770 0.7714 1.3318 0.1838  0.0011  0.0467  171 LEU D O   
10622 C  CB  . LEU D 170 ? 0.7340 0.7270 1.2936 0.1492  -0.0044 0.0631  171 LEU D CB  
10623 C  CG  . LEU D 170 ? 0.7202 0.7053 1.2950 0.1495  -0.0103 0.0702  171 LEU D CG  
10624 C  CD1 . LEU D 170 ? 0.6821 0.6845 1.2609 0.1508  -0.0034 0.0785  171 LEU D CD1 
10625 C  CD2 . LEU D 170 ? 0.6865 0.6620 1.2716 0.1380  -0.0168 0.0798  171 LEU D CD2 
10626 N  N   . GLU D 171 ? 0.8377 0.8135 1.3760 0.1811  -0.0071 0.0332  172 GLU D N   
10627 C  CA  . GLU D 171 ? 0.9094 0.8697 1.4429 0.1973  -0.0135 0.0204  172 GLU D CA  
10628 C  C   . GLU D 171 ? 0.9044 0.8788 1.4299 0.2128  -0.0024 0.0177  172 GLU D C   
10629 O  O   . GLU D 171 ? 0.9147 0.8821 1.4434 0.2245  -0.0052 0.0136  172 GLU D O   
10630 C  CB  . GLU D 171 ? 1.0169 0.9603 1.5380 0.2017  -0.0226 0.0066  172 GLU D CB  
10631 C  CG  . GLU D 171 ? 1.1026 1.0285 1.6370 0.1886  -0.0362 0.0083  172 GLU D CG  
10632 C  CD  . GLU D 171 ? 1.1947 1.1052 1.7187 0.1921  -0.0463 -0.0056 172 GLU D CD  
10633 O  OE1 . GLU D 171 ? 1.2306 1.1469 1.7336 0.2032  -0.0408 -0.0150 172 GLU D OE1 
10634 O  OE2 . GLU D 171 ? 1.2308 1.1238 1.7687 0.1842  -0.0599 -0.0065 172 GLU D OE2 
10635 N  N   . ARG D 172 ? 0.8804 0.8749 1.3975 0.2128  0.0104  0.0210  173 ARG D N   
10636 C  CA  . ARG D 172 ? 0.8361 0.8481 1.3503 0.2260  0.0231  0.0223  173 ARG D CA  
10637 C  C   . ARG D 172 ? 0.8059 0.8300 1.3388 0.2225  0.0267  0.0334  173 ARG D C   
10638 O  O   . ARG D 172 ? 0.8086 0.8311 1.3465 0.2344  0.0266  0.0315  173 ARG D O   
10639 C  CB  . ARG D 172 ? 0.8488 0.8801 1.3544 0.2242  0.0359  0.0261  173 ARG D CB  
10640 N  N   . LEU D 173 ? 0.7943 0.8308 1.3369 0.2068  0.0293  0.0445  174 LEU D N   
10641 C  CA  . LEU D 173 ? 0.7946 0.8474 1.3536 0.2033  0.0338  0.0552  174 LEU D CA  
10642 C  C   . LEU D 173 ? 0.8072 0.8482 1.3772 0.2051  0.0249  0.0566  174 LEU D C   
10643 O  O   . LEU D 173 ? 0.8385 0.8904 1.4212 0.2080  0.0276  0.0627  174 LEU D O   
10644 C  CB  . LEU D 173 ? 0.7461 0.8106 1.3102 0.1869  0.0355  0.0648  174 LEU D CB  
10645 C  CG  . LEU D 173 ? 0.7184 0.8029 1.2806 0.1851  0.0469  0.0681  174 LEU D CG  
10646 C  CD1 . LEU D 173 ? 0.7076 0.7888 1.2523 0.1932  0.0520  0.0596  174 LEU D CD1 
10647 C  CD2 . LEU D 173 ? 0.6716 0.7624 1.2369 0.1689  0.0453  0.0756  174 LEU D CD2 
10648 N  N   . PHE D 174 ? 0.8185 0.8371 1.3855 0.2037  0.0138  0.0513  175 PHE D N   
10649 C  CA  . PHE D 174 ? 0.8068 0.8123 1.3847 0.2071  0.0054  0.0523  175 PHE D CA  
10650 C  C   . PHE D 174 ? 0.8132 0.8153 1.3886 0.2258  0.0067  0.0437  175 PHE D C   
10651 O  O   . PHE D 174 ? 0.8318 0.8369 1.4184 0.2309  0.0065  0.0478  175 PHE D O   
10652 C  CB  . PHE D 174 ? 0.7891 0.7712 1.3687 0.2002  -0.0072 0.0504  175 PHE D CB  
10653 C  CG  . PHE D 174 ? 0.7778 0.7499 1.3727 0.1986  -0.0148 0.0573  175 PHE D CG  
10654 C  CD1 . PHE D 174 ? 0.7456 0.7257 1.3501 0.1871  -0.0143 0.0713  175 PHE D CD1 
10655 C  CD2 . PHE D 174 ? 0.7956 0.7501 1.3941 0.2099  -0.0226 0.0499  175 PHE D CD2 
10656 C  CE1 . PHE D 174 ? 0.7307 0.7021 1.3481 0.1869  -0.0206 0.0789  175 PHE D CE1 
10657 C  CE2 . PHE D 174 ? 0.7823 0.7274 1.3956 0.2087  -0.0293 0.0572  175 PHE D CE2 
10658 C  CZ  . PHE D 174 ? 0.7720 0.7261 1.3948 0.1972  -0.0278 0.0723  175 PHE D CZ  
10659 N  N   . LYS D 175 ? 0.8040 0.7997 1.3636 0.2373  0.0080  0.0317  176 LYS D N   
10660 C  CA  . LYS D 175 ? 0.8062 0.8006 1.3600 0.2577  0.0110  0.0234  176 LYS D CA  
10661 C  C   . LYS D 175 ? 0.7828 0.8039 1.3448 0.2626  0.0251  0.0322  176 LYS D C   
10662 O  O   . LYS D 175 ? 0.7675 0.7917 1.3381 0.2730  0.0264  0.0333  176 LYS D O   
10663 C  CB  . LYS D 175 ? 0.7888 0.7747 1.3206 0.2712  0.0113  0.0095  176 LYS D CB  
10664 C  CG  . LYS D 175 ? 0.8087 0.7751 1.3318 0.2632  -0.0001 0.0018  176 LYS D CG  
10665 C  CD  . LYS D 175 ? 0.8507 0.8104 1.3500 0.2799  0.0003  -0.0129 176 LYS D CD  
10666 C  CE  . LYS D 175 ? 0.8639 0.8080 1.3550 0.2712  -0.0102 -0.0201 176 LYS D CE  
10667 N  NZ  . LYS D 175 ? 0.8877 0.8379 1.3551 0.2821  -0.0032 -0.0279 176 LYS D NZ  
10668 N  N   . GLN D 176 ? 0.8295 0.8699 1.3906 0.2550  0.0351  0.0387  177 GLN D N   
10669 C  CA  . GLN D 176 ? 0.8426 0.9093 1.4144 0.2595  0.0486  0.0473  177 GLN D CA  
10670 C  C   . GLN D 176 ? 0.8871 0.9634 1.4812 0.2517  0.0464  0.0579  177 GLN D C   
10671 O  O   . GLN D 176 ? 0.8805 0.9716 1.4871 0.2607  0.0530  0.0623  177 GLN D O   
10672 C  CB  . GLN D 176 ? 0.8025 0.8857 1.3704 0.2519  0.0584  0.0520  177 GLN D CB  
10673 C  CG  . GLN D 176 ? 0.8203 0.9036 1.3681 0.2664  0.0663  0.0442  177 GLN D CG  
10674 C  CD  . GLN D 176 ? 0.8009 0.8965 1.3433 0.2576  0.0741  0.0485  177 GLN D CD  
10675 O  OE1 . GLN D 176 ? 0.7837 0.9001 1.3416 0.2499  0.0824  0.0596  177 GLN D OE1 
10676 N  NE2 . GLN D 176 ? 0.7998 0.8819 1.3213 0.2589  0.0706  0.0393  177 GLN D NE2 
10677 N  N   . LEU D 177 ? 0.8707 0.9391 1.4699 0.2362  0.0371  0.0623  178 LEU D N   
10678 C  CA  . LEU D 177 ? 0.8559 0.9316 1.4731 0.2301  0.0335  0.0717  178 LEU D CA  
10679 C  C   . LEU D 177 ? 0.8644 0.9270 1.4870 0.2402  0.0267  0.0691  178 LEU D C   
10680 O  O   . LEU D 177 ? 0.8778 0.9483 1.5155 0.2404  0.0251  0.0760  178 LEU D O   
10681 C  CB  . LEU D 177 ? 0.8037 0.8749 1.4217 0.2128  0.0263  0.0780  178 LEU D CB  
10682 C  CG  . LEU D 177 ? 0.7709 0.8593 1.3899 0.2016  0.0319  0.0837  178 LEU D CG  
10683 C  CD1 . LEU D 177 ? 0.7464 0.8266 1.3610 0.1871  0.0247  0.0881  178 LEU D CD1 
10684 C  CD2 . LEU D 177 ? 0.7420 0.8524 1.3790 0.2025  0.0363  0.0912  178 LEU D CD2 
10685 N  N   . HIS D 178 ? 0.9158 0.9577 1.5265 0.2490  0.0216  0.0586  179 HIS D N   
10686 C  CA  . HIS D 178 ? 0.9786 1.0048 1.5939 0.2590  0.0138  0.0549  179 HIS D CA  
10687 C  C   . HIS D 178 ? 1.0103 1.0280 1.6133 0.2786  0.0158  0.0424  179 HIS D C   
10688 O  O   . HIS D 178 ? 1.0215 1.0167 1.6128 0.2823  0.0072  0.0318  179 HIS D O   
10689 C  CB  . HIS D 178 ? 1.0578 1.0607 1.6742 0.2490  0.0005  0.0553  179 HIS D CB  
10690 C  CG  . HIS D 178 ? 1.1007 1.1108 1.7267 0.2328  -0.0015 0.0682  179 HIS D CG  
10691 N  ND1 . HIS D 178 ? 1.1161 1.1479 1.7524 0.2298  0.0041  0.0775  179 HIS D ND1 
10692 C  CD2 . HIS D 178 ? 1.1188 1.1176 1.7455 0.2198  -0.0086 0.0734  179 HIS D CD2 
10693 C  CE1 . HIS D 178 ? 1.1119 1.1444 1.7517 0.2168  -0.0001 0.0867  179 HIS D CE1 
10694 N  NE2 . HIS D 178 ? 1.1200 1.1335 1.7540 0.2107  -0.0067 0.0853  179 HIS D NE2 
10695 N  N   . PRO D 179 ? 1.0108 1.0468 1.6172 0.2920  0.0269  0.0436  180 PRO D N   
10696 C  CA  . PRO D 179 ? 1.0582 1.0900 1.6514 0.3139  0.0312  0.0329  180 PRO D CA  
10697 C  C   . PRO D 179 ? 1.1351 1.1417 1.7259 0.3251  0.0191  0.0235  180 PRO D C   
10698 O  O   . PRO D 179 ? 1.1525 1.1415 1.7257 0.3382  0.0145  0.0099  180 PRO D O   
10699 C  CB  . PRO D 179 ? 1.0323 1.0925 1.6383 0.3230  0.0458  0.0415  180 PRO D CB  
10700 C  CG  . PRO D 179 ? 0.9930 1.0729 1.6149 0.3043  0.0496  0.0544  180 PRO D CG  
10701 C  CD  . PRO D 179 ? 0.9824 1.0454 1.6071 0.2876  0.0358  0.0560  180 PRO D CD  
10702 N  N   . GLN D 180 ? 1.1469 1.1513 1.7552 0.3206  0.0132  0.0304  181 GLN D N   
10703 C  CA  . GLN D 180 ? 1.2040 1.1858 1.8138 0.3313  0.0021  0.0233  181 GLN D CA  
10704 C  C   . GLN D 180 ? 1.2684 1.2195 1.8695 0.3265  -0.0129 0.0136  181 GLN D C   
10705 O  O   . GLN D 180 ? 1.3334 1.2636 1.9251 0.3412  -0.0210 0.0004  181 GLN D O   
10706 C  CB  . GLN D 180 ? 1.1767 1.1630 1.8077 0.3249  -0.0014 0.0347  181 GLN D CB  
10707 N  N   . LEU D 181 ? 1.3178 1.2661 1.9232 0.3065  -0.0172 0.0202  182 LEU D N   
10708 C  CA  . LEU D 181 ? 1.3304 1.2515 1.9333 0.2994  -0.0315 0.0138  182 LEU D CA  
10709 C  C   . LEU D 181 ? 1.3215 1.2323 1.9037 0.3084  -0.0334 -0.0017 182 LEU D C   
10710 O  O   . LEU D 181 ? 1.3558 1.2828 1.9264 0.3069  -0.0233 -0.0015 182 LEU D O   
10711 C  CB  . LEU D 181 ? 1.3237 1.2484 1.9364 0.2767  -0.0332 0.0265  182 LEU D CB  
10712 N  N   . LEU D 182 ? 1.2694 1.1525 1.8473 0.3185  -0.0474 -0.0152 183 LEU D N   
10713 C  CA  . LEU D 182 ? 1.2307 1.1001 1.7879 0.3293  -0.0527 -0.0321 183 LEU D CA  
10714 C  C   . LEU D 182 ? 1.1783 1.0269 1.7409 0.3141  -0.0673 -0.0348 183 LEU D C   
10715 O  O   . LEU D 182 ? 1.2022 1.0273 1.7795 0.3107  -0.0825 -0.0366 183 LEU D O   
10716 C  CB  . LEU D 182 ? 1.2593 1.1110 1.8061 0.3541  -0.0600 -0.0480 183 LEU D CB  
10717 N  N   . LEU D 183 ? 1.1729 1.0307 1.7257 0.3051  -0.0625 -0.0343 184 LEU D N   
10718 C  CA  . LEU D 183 ? 1.1751 1.0190 1.7362 0.2878  -0.0737 -0.0331 184 LEU D CA  
10719 C  C   . LEU D 183 ? 1.2207 1.0474 1.7648 0.2960  -0.0840 -0.0511 184 LEU D C   
10720 O  O   . LEU D 183 ? 1.2319 1.0717 1.7552 0.3022  -0.0747 -0.0560 184 LEU D O   
10721 C  CB  . LEU D 183 ? 1.1550 1.0221 1.7211 0.2681  -0.0619 -0.0169 184 LEU D CB  
10722 C  CG  . LEU D 183 ? 1.1246 1.0026 1.7114 0.2532  -0.0578 0.0021  184 LEU D CG  
10723 C  CD1 . LEU D 183 ? 1.1087 1.0004 1.6986 0.2634  -0.0491 0.0069  184 LEU D CD1 
10724 C  CD2 . LEU D 183 ? 1.1048 1.0026 1.6914 0.2362  -0.0483 0.0142  184 LEU D CD2 
10725 N  N   . PRO D 184 ? 1.2353 1.0323 1.7893 0.2963  -0.1041 -0.0607 185 PRO D N   
10726 C  CA  . PRO D 184 ? 1.2700 1.0491 1.8129 0.2998  -0.1174 -0.0767 185 PRO D CA  
10727 C  C   . PRO D 184 ? 1.2651 1.0519 1.8170 0.2774  -0.1161 -0.0664 185 PRO D C   
10728 O  O   . PRO D 184 ? 1.2556 1.0587 1.8224 0.2605  -0.1062 -0.0474 185 PRO D O   
10729 C  CB  . PRO D 184 ? 1.2919 1.0372 1.8503 0.3049  -0.1403 -0.0876 185 PRO D CB  
10730 C  CG  . PRO D 184 ? 1.2725 1.0197 1.8581 0.2930  -0.1383 -0.0701 185 PRO D CG  
10731 C  CD  . PRO D 184 ? 1.2515 1.0292 1.8282 0.2954  -0.1163 -0.0581 185 PRO D CD  
10732 N  N   . ASP D 185 ? 1.2871 1.0621 1.8294 0.2784  -0.1263 -0.0789 186 ASP D N   
10733 C  CA  . ASP D 185 ? 1.2608 1.0426 1.8113 0.2583  -0.1255 -0.0700 186 ASP D CA  
10734 C  C   . ASP D 185 ? 1.2544 1.0268 1.8396 0.2383  -0.1342 -0.0555 186 ASP D C   
10735 O  O   . ASP D 185 ? 1.2340 1.0204 1.8296 0.2199  -0.1268 -0.0398 186 ASP D O   
10736 C  CB  . ASP D 185 ? 1.3045 1.0722 1.8399 0.2651  -0.1380 -0.0879 186 ASP D CB  
10737 N  N   . ASP D 186 ? 1.2290 0.9777 1.8316 0.2431  -0.1494 -0.0601 187 ASP D N   
10738 C  CA  . ASP D 186 ? 1.1993 0.9369 1.8373 0.2263  -0.1583 -0.0457 187 ASP D CA  
10739 C  C   . ASP D 186 ? 1.1286 0.8903 1.7760 0.2128  -0.1406 -0.0216 187 ASP D C   
10740 O  O   . ASP D 186 ? 1.0969 0.8619 1.7653 0.1952  -0.1401 -0.0051 187 ASP D O   
10741 C  CB  . ASP D 186 ? 1.2410 0.9495 1.8951 0.2365  -0.1766 -0.0551 187 ASP D CB  
10742 C  CG  . ASP D 186 ? 1.2566 0.9710 1.9099 0.2457  -0.1679 -0.0492 187 ASP D CG  
10743 O  OD1 . ASP D 186 ? 1.2451 0.9854 1.8917 0.2419  -0.1489 -0.0351 187 ASP D OD1 
10744 O  OD2 . ASP D 186 ? 1.2827 0.9740 1.9433 0.2576  -0.1819 -0.0596 187 ASP D OD2 
10745 N  N   . TYR D 187 ? 1.1215 0.9003 1.7529 0.2223  -0.1264 -0.0198 188 TYR D N   
10746 C  CA  . TYR D 187 ? 1.0998 0.9010 1.7378 0.2129  -0.1111 0.0005  188 TYR D CA  
10747 C  C   . TYR D 187 ? 1.1121 0.9385 1.7374 0.2027  -0.0965 0.0084  188 TYR D C   
10748 O  O   . TYR D 187 ? 1.0970 0.9366 1.7329 0.1885  -0.0892 0.0261  188 TYR D O   
10749 C  CB  . TYR D 187 ? 1.0229 0.8319 1.6517 0.2277  -0.1034 -0.0017 188 TYR D CB  
10750 C  CG  . TYR D 187 ? 0.9536 0.7724 1.5986 0.2206  -0.0971 0.0170  188 TYR D CG  
10751 C  CD1 . TYR D 187 ? 0.9249 0.7713 1.5638 0.2151  -0.0810 0.0295  188 TYR D CD1 
10752 C  CD2 . TYR D 187 ? 0.9292 0.7289 1.5960 0.2204  -0.1080 0.0218  188 TYR D CD2 
10753 C  CE1 . TYR D 187 ? 0.8867 0.7414 1.5385 0.2103  -0.0766 0.0455  188 TYR D CE1 
10754 C  CE2 . TYR D 187 ? 0.8930 0.7017 1.5730 0.2154  -0.1022 0.0392  188 TYR D CE2 
10755 C  CZ  . TYR D 187 ? 0.8737 0.7098 1.5450 0.2109  -0.0868 0.0505  188 TYR D CZ  
10756 O  OH  . TYR D 187 ? 0.8729 0.7174 1.5554 0.2074  -0.0823 0.0668  188 TYR D OH  
10757 N  N   . LEU D 188 ? 1.1672 0.9998 1.7690 0.2114  -0.0924 -0.0049 189 LEU D N   
10758 C  CA  . LEU D 188 ? 1.1763 1.0314 1.7648 0.2035  -0.0792 0.0006  189 LEU D CA  
10759 C  C   . LEU D 188 ? 1.2129 1.0661 1.8147 0.1853  -0.0834 0.0099  189 LEU D C   
10760 O  O   . LEU D 188 ? 1.2050 1.0765 1.8094 0.1729  -0.0728 0.0248  189 LEU D O   
10761 C  CB  . LEU D 188 ? 1.1907 1.0482 1.7529 0.2174  -0.0765 -0.0160 189 LEU D CB  
10762 C  CG  . LEU D 188 ? 1.2171 1.0783 1.7638 0.2381  -0.0707 -0.0253 189 LEU D CG  
10763 C  CD1 . LEU D 188 ? 1.2402 1.1027 1.7600 0.2527  -0.0682 -0.0405 189 LEU D CD1 
10764 C  CD2 . LEU D 188 ? 1.1890 1.0758 1.7384 0.2358  -0.0540 -0.0111 189 LEU D CD2 
10765 N  N   . ASP D 189 ? 1.2455 1.0762 1.8568 0.1842  -0.0995 0.0011  190 ASP D N   
10766 C  CA  . ASP D 189 ? 1.2237 1.0527 1.8500 0.1675  -0.1038 0.0099  190 ASP D CA  
10767 C  C   . ASP D 189 ? 1.1234 0.9550 1.7754 0.1539  -0.1019 0.0315  190 ASP D C   
10768 O  O   . ASP D 189 ? 1.0887 0.9348 1.7445 0.1410  -0.0938 0.0457  190 ASP D O   
10769 C  CB  . ASP D 189 ? 1.3151 1.1188 1.9490 0.1701  -0.1233 -0.0050 190 ASP D CB  
10770 C  CG  . ASP D 189 ? 1.3832 1.1854 1.9882 0.1840  -0.1249 -0.0255 190 ASP D CG  
10771 O  OD1 . ASP D 189 ? 1.4108 1.2303 1.9919 0.1935  -0.1106 -0.0279 190 ASP D OD1 
10772 O  OD2 . ASP D 189 ? 1.4050 1.1897 2.0120 0.1858  -0.1404 -0.0386 190 ASP D OD2 
10773 N  N   . CYS D 190 ? 1.0658 0.8840 1.7341 0.1581  -0.1088 0.0342  191 CYS D N   
10774 C  CA  . CYS D 190 ? 1.0026 0.8238 1.6934 0.1480  -0.1057 0.0558  191 CYS D CA  
10775 C  C   . CYS D 190 ? 0.9075 0.7562 1.5859 0.1439  -0.0877 0.0697  191 CYS D C   
10776 O  O   . CYS D 190 ? 0.8922 0.7510 1.5802 0.1323  -0.0819 0.0876  191 CYS D O   
10777 C  CB  . CYS D 190 ? 1.0196 0.8235 1.7248 0.1565  -0.1144 0.0547  191 CYS D CB  
10778 S  SG  . CYS D 190 ? 1.0498 0.8600 1.7773 0.1484  -0.1082 0.0814  191 CYS D SG  
10779 N  N   . LEU D 191 ? 0.8964 0.7568 1.5539 0.1546  -0.0795 0.0613  192 LEU D N   
10780 C  CA  . LEU D 191 ? 0.8438 0.7303 1.4884 0.1522  -0.0641 0.0705  192 LEU D CA  
10781 C  C   . LEU D 191 ? 0.7451 0.6444 1.3827 0.1408  -0.0580 0.0755  192 LEU D C   
10782 O  O   . LEU D 191 ? 0.6951 0.6095 1.3339 0.1325  -0.0499 0.0904  192 LEU D O   
10783 C  CB  . LEU D 191 ? 0.8653 0.7612 1.4909 0.1659  -0.0576 0.0582  192 LEU D CB  
10784 C  CG  . LEU D 191 ? 0.8581 0.7804 1.4691 0.1648  -0.0429 0.0625  192 LEU D CG  
10785 C  CD1 . LEU D 191 ? 0.8612 0.7966 1.4808 0.1588  -0.0372 0.0792  192 LEU D CD1 
10786 C  CD2 . LEU D 191 ? 0.8609 0.7897 1.4579 0.1798  -0.0376 0.0502  192 LEU D CD2 
10787 N  N   . GLY D 192 ? 0.7381 0.6307 1.3676 0.1415  -0.0627 0.0626  193 GLY D N   
10788 C  CA  . GLY D 192 ? 0.7323 0.6352 1.3550 0.1317  -0.0581 0.0655  193 GLY D CA  
10789 C  C   . GLY D 192 ? 0.7481 0.6486 1.3903 0.1178  -0.0608 0.0812  193 GLY D C   
10790 O  O   . GLY D 192 ? 0.7783 0.6933 1.4153 0.1092  -0.0530 0.0898  193 GLY D O   
10791 N  N   . LYS D 193 ? 0.7819 0.6643 1.4473 0.1163  -0.0716 0.0856  194 LYS D N   
10792 C  CA  . LYS D 193 ? 0.8049 0.6855 1.4928 0.1041  -0.0732 0.1035  194 LYS D CA  
10793 C  C   . LYS D 193 ? 0.7296 0.6224 1.4224 0.1019  -0.0639 0.1233  194 LYS D C   
10794 O  O   . LYS D 193 ? 0.7359 0.6352 1.4399 0.0931  -0.0598 0.1410  194 LYS D O   
10795 C  CB  . LYS D 193 ? 0.8203 0.6759 1.5356 0.1027  -0.0895 0.1012  194 LYS D CB  
10796 C  CG  . LYS D 193 ? 0.8281 0.6663 1.5363 0.1117  -0.1024 0.0771  194 LYS D CG  
10797 C  CD  . LYS D 193 ? 0.8296 0.6505 1.5597 0.1049  -0.1173 0.0736  194 LYS D CD  
10798 C  CE  . LYS D 193 ? 0.8241 0.6191 1.5586 0.1156  -0.1356 0.0529  194 LYS D CE  
10799 N  NZ  . LYS D 193 ? 0.7856 0.5647 1.5441 0.1179  -0.1433 0.0595  194 LYS D NZ  
10800 N  N   . GLN D 194 ? 0.7820 0.6783 1.4658 0.1110  -0.0605 0.1205  195 GLN D N   
10801 C  CA  . GLN D 194 ? 0.8122 0.7218 1.4958 0.1109  -0.0519 0.1371  195 GLN D CA  
10802 C  C   . GLN D 194 ? 0.7908 0.7238 1.4536 0.1082  -0.0399 0.1401  195 GLN D C   
10803 O  O   . GLN D 194 ? 0.8022 0.7472 1.4645 0.1046  -0.0333 0.1561  195 GLN D O   
10804 C  CB  . GLN D 194 ? 0.8699 0.7755 1.5525 0.1219  -0.0535 0.1324  195 GLN D CB  
10805 C  CG  . GLN D 194 ? 0.9420 0.8448 1.6404 0.1222  -0.0536 0.1502  195 GLN D CG  
10806 C  CD  . GLN D 194 ? 1.0207 0.9128 1.7239 0.1328  -0.0590 0.1439  195 GLN D CD  
10807 O  OE1 . GLN D 194 ? 1.0587 0.9616 1.7547 0.1388  -0.0536 0.1480  195 GLN D OE1 
10808 N  NE2 . GLN D 194 ? 1.0355 0.9057 1.7510 0.1360  -0.0705 0.1332  195 GLN D NE2 
10809 N  N   . ALA D 195 ? 0.7630 0.7015 1.4086 0.1110  -0.0377 0.1245  196 ALA D N   
10810 C  CA  . ALA D 195 ? 0.7773 0.7362 1.4042 0.1087  -0.0277 0.1244  196 ALA D CA  
10811 C  C   . ALA D 195 ? 0.7680 0.7365 1.3959 0.0992  -0.0229 0.1396  196 ALA D C   
10812 O  O   . ALA D 195 ? 0.7385 0.7221 1.3579 0.0992  -0.0160 0.1481  196 ALA D O   
10813 C  CB  . ALA D 195 ? 0.7774 0.7367 1.3907 0.1107  -0.0274 0.1078  196 ALA D CB  
10814 N  N   . GLU D 196 ? 0.8124 0.7723 1.4512 0.0920  -0.0271 0.1427  197 GLU D N   
10815 C  CA  . GLU D 196 ? 0.8879 0.8561 1.5306 0.0840  -0.0223 0.1591  197 GLU D CA  
10816 C  C   . GLU D 196 ? 1.0063 0.9760 1.6589 0.0859  -0.0202 0.1772  197 GLU D C   
10817 O  O   . GLU D 196 ? 1.0308 0.9867 1.7018 0.0877  -0.0264 0.1815  197 GLU D O   
10818 C  CB  . GLU D 196 ? 0.8658 0.8232 1.5242 0.0763  -0.0283 0.1601  197 GLU D CB  
10819 N  N   . ALA D 197 ? 1.1326 1.1187 1.7721 0.0864  -0.0120 0.1873  198 ALA D N   
10820 C  CA  . ALA D 197 ? 1.1434 1.1341 1.7854 0.0908  -0.0088 0.2042  198 ALA D CA  
10821 C  C   . ALA D 197 ? 1.1545 1.1436 1.7940 0.0996  -0.0112 0.1990  198 ALA D C   
10822 O  O   . ALA D 197 ? 1.2223 1.2174 1.8593 0.1048  -0.0087 0.2108  198 ALA D O   
10823 C  CB  . ALA D 197 ? 1.1895 1.1705 1.8552 0.0873  -0.0106 0.2218  198 ALA D CB  
10824 N  N   . LEU D 198 ? 1.0333 1.0151 1.6728 0.1026  -0.0159 0.1819  199 LEU D N   
10825 C  CA  . LEU D 198 ? 0.8798 0.8666 1.5124 0.1112  -0.0156 0.1764  199 LEU D CA  
10826 C  C   . LEU D 198 ? 0.7380 0.7431 1.3517 0.1117  -0.0098 0.1705  199 LEU D C   
10827 O  O   . LEU D 198 ? 0.7114 0.7265 1.3191 0.1172  -0.0084 0.1727  199 LEU D O   
10828 C  CB  . LEU D 198 ? 0.7864 0.7605 1.4251 0.1165  -0.0215 0.1616  199 LEU D CB  
10829 C  CG  . LEU D 198 ? 0.7380 0.7071 1.3847 0.1249  -0.0246 0.1650  199 LEU D CG  
10830 C  CD1 . LEU D 198 ? 0.7202 0.6810 1.3822 0.1231  -0.0267 0.1833  199 LEU D CD1 
10831 C  CD2 . LEU D 198 ? 0.7306 0.6861 1.3825 0.1313  -0.0307 0.1499  199 LEU D CD2 
10832 N  N   . ARG D 199 ? 0.7172 0.7261 1.3230 0.1059  -0.0074 0.1632  200 ARG D N   
10833 C  CA  . ARG D 199 ? 0.7223 0.7473 1.3125 0.1052  -0.0022 0.1574  200 ARG D CA  
10834 C  C   . ARG D 199 ? 0.6207 0.6526 1.2079 0.1122  -0.0017 0.1475  200 ARG D C   
10835 O  O   . ARG D 199 ? 0.6107 0.6541 1.1939 0.1153  -0.0005 0.1511  200 ARG D O   
10836 C  CB  . ARG D 199 ? 0.7560 0.7926 1.3379 0.1040  0.0011  0.1701  200 ARG D CB  
10837 C  CG  . ARG D 199 ? 0.8170 0.8559 1.3942 0.0967  0.0043  0.1758  200 ARG D CG  
10838 C  CD  . ARG D 199 ? 0.8766 0.9087 1.4644 0.0951  0.0040  0.1923  200 ARG D CD  
10839 N  NE  . ARG D 199 ? 0.9080 0.9492 1.4870 0.0920  0.0090  0.2027  200 ARG D NE  
10840 C  CZ  . ARG D 199 ? 0.9293 0.9689 1.5159 0.0913  0.0113  0.2198  200 ARG D CZ  
10841 N  NH1 . ARG D 199 ? 0.9345 0.9630 1.5393 0.0925  0.0086  0.2290  200 ARG D NH1 
10842 N  NH2 . ARG D 199 ? 0.9308 0.9800 1.5075 0.0899  0.0167  0.2286  200 ARG D NH2 
10843 N  N   . PRO D 200 ? 0.6029 0.6280 1.1926 0.1155  -0.0028 0.1351  201 PRO D N   
10844 C  CA  . PRO D 200 ? 0.5534 0.5862 1.1424 0.1231  -0.0009 0.1269  201 PRO D CA  
10845 C  C   . PRO D 200 ? 0.5481 0.5988 1.1287 0.1213  0.0048  0.1244  201 PRO D C   
10846 O  O   . PRO D 200 ? 0.5254 0.5871 1.1088 0.1255  0.0057  0.1250  201 PRO D O   
10847 C  CB  . PRO D 200 ? 0.5622 0.5834 1.1520 0.1276  -0.0025 0.1144  201 PRO D CB  
10848 C  CG  . PRO D 200 ? 0.5793 0.5831 1.1752 0.1231  -0.0086 0.1168  201 PRO D CG  
10849 C  CD  . PRO D 200 ? 0.5689 0.5789 1.1622 0.1137  -0.0064 0.1280  201 PRO D CD  
10850 N  N   . PHE D 201 ? 0.5051 0.5582 1.0772 0.1149  0.0079  0.1217  202 PHE D N   
10851 C  CA  . PHE D 201 ? 0.5423 0.6110 1.1079 0.1126  0.0131  0.1193  202 PHE D CA  
10852 C  C   . PHE D 201 ? 0.6081 0.6847 1.1689 0.1076  0.0123  0.1284  202 PHE D C   
10853 O  O   . PHE D 201 ? 0.5564 0.6447 1.1123 0.1050  0.0150  0.1270  202 PHE D O   
10854 C  CB  . PHE D 201 ? 0.5434 0.6108 1.1010 0.1095  0.0169  0.1115  202 PHE D CB  
10855 C  CG  . PHE D 201 ? 0.4477 0.5072 1.0060 0.1167  0.0174  0.1014  202 PHE D CG  
10856 C  CD1 . PHE D 201 ? 0.4483 0.5164 1.0094 0.1247  0.0218  0.0966  202 PHE D CD1 
10857 C  CD2 . PHE D 201 ? 0.5216 0.5651 1.0783 0.1164  0.0129  0.0968  202 PHE D CD2 
10858 C  CE1 . PHE D 201 ? 0.5012 0.5622 1.0601 0.1338  0.0227  0.0874  202 PHE D CE1 
10859 C  CE2 . PHE D 201 ? 0.5338 0.5686 1.0885 0.1251  0.0119  0.0861  202 PHE D CE2 
10860 C  CZ  . PHE D 201 ? 0.5066 0.5504 1.0607 0.1345  0.0173  0.0814  202 PHE D CZ  
10861 N  N   . GLY D 202 ? 0.6228 0.6929 1.1851 0.1073  0.0087  0.1380  203 GLY D N   
10862 C  CA  . GLY D 202 ? 0.6712 0.7480 1.2264 0.1055  0.0080  0.1473  203 GLY D CA  
10863 C  C   . GLY D 202 ? 0.6746 0.7535 1.2201 0.0985  0.0111  0.1488  203 GLY D C   
10864 O  O   . GLY D 202 ? 0.6570 0.7272 1.2040 0.0941  0.0120  0.1496  203 GLY D O   
10865 N  N   . GLU D 203 ? 0.7497 0.8400 1.2865 0.0977  0.0118  0.1488  204 GLU D N   
10866 C  CA  . GLU D 203 ? 0.8091 0.9024 1.3352 0.0923  0.0143  0.1516  204 GLU D CA  
10867 C  C   . GLU D 203 ? 0.8096 0.9063 1.3328 0.0871  0.0181  0.1420  204 GLU D C   
10868 O  O   . GLU D 203 ? 0.8417 0.9387 1.3575 0.0820  0.0206  0.1432  204 GLU D O   
10869 C  CB  . GLU D 203 ? 0.8950 0.9973 1.4111 0.0957  0.0118  0.1567  204 GLU D CB  
10870 C  CG  . GLU D 203 ? 0.9907 1.0916 1.4971 0.0959  0.0132  0.1682  204 GLU D CG  
10871 C  CD  . GLU D 203 ? 1.0595 1.1681 1.5532 0.1027  0.0096  0.1725  204 GLU D CD  
10872 O  OE1 . GLU D 203 ? 1.0885 1.2043 1.5789 0.1034  0.0062  0.1641  204 GLU D OE1 
10873 O  OE2 . GLU D 203 ? 1.0906 1.1979 1.5781 0.1082  0.0098  0.1843  204 GLU D OE2 
10874 N  N   . ALA D 204 ? 0.7674 0.8674 1.2968 0.0891  0.0191  0.1334  205 ALA D N   
10875 C  CA  . ALA D 204 ? 0.6984 0.8031 1.2252 0.0860  0.0237  0.1255  205 ALA D CA  
10876 C  C   . ALA D 204 ? 0.6668 0.7631 1.1887 0.0817  0.0263  0.1227  205 ALA D C   
10877 O  O   . ALA D 204 ? 0.7125 0.8128 1.2268 0.0771  0.0292  0.1210  205 ALA D O   
10878 C  CB  . ALA D 204 ? 0.6665 0.7758 1.2027 0.0909  0.0257  0.1190  205 ALA D CB  
10879 N  N   . PRO D 205 ? 0.6763 0.7606 1.2034 0.0833  0.0241  0.1217  206 PRO D N   
10880 C  CA  . PRO D 205 ? 0.6306 0.7065 1.1545 0.0797  0.0245  0.1175  206 PRO D CA  
10881 C  C   . PRO D 205 ? 0.6134 0.6896 1.1322 0.0727  0.0247  0.1244  206 PRO D C   
10882 O  O   . PRO D 205 ? 0.6060 0.6828 1.1187 0.0690  0.0268  0.1201  206 PRO D O   
10883 C  CB  . PRO D 205 ? 0.6624 0.7240 1.1958 0.0830  0.0194  0.1166  206 PRO D CB  
10884 C  CG  . PRO D 205 ? 0.6608 0.7250 1.1999 0.0899  0.0189  0.1161  206 PRO D CG  
10885 C  CD  . PRO D 205 ? 0.6590 0.7359 1.1957 0.0888  0.0204  0.1231  206 PRO D CD  
10886 N  N   . ARG D 206 ? 0.6465 0.7231 1.1676 0.0720  0.0231  0.1355  207 ARG D N   
10887 C  CA  . ARG D 206 ? 0.6978 0.7756 1.2152 0.0669  0.0243  0.1440  207 ARG D CA  
10888 C  C   . ARG D 206 ? 0.6653 0.7546 1.1698 0.0649  0.0279  0.1428  207 ARG D C   
10889 O  O   . ARG D 206 ? 0.6952 0.7853 1.1946 0.0601  0.0300  0.1419  207 ARG D O   
10890 C  CB  . ARG D 206 ? 0.7627 0.8392 1.2849 0.0691  0.0230  0.1579  207 ARG D CB  
10891 C  CG  . ARG D 206 ? 0.8142 0.8981 1.3276 0.0676  0.0261  0.1683  207 ARG D CG  
10892 C  CD  . ARG D 206 ? 0.8732 0.9581 1.3878 0.0731  0.0259  0.1825  207 ARG D CD  
10893 N  NE  . ARG D 206 ? 0.9039 0.9911 1.4175 0.0716  0.0297  0.1960  207 ARG D NE  
10894 C  CZ  . ARG D 206 ? 0.9416 1.0360 1.4451 0.0778  0.0322  0.2076  207 ARG D CZ  
10895 N  NH1 . ARG D 206 ? 0.9490 1.0479 1.4424 0.0856  0.0296  0.2062  207 ARG D NH1 
10896 N  NH2 . ARG D 206 ? 0.9444 1.0418 1.4479 0.0773  0.0370  0.2209  207 ARG D NH2 
10897 N  N   . GLU D 207 ? 0.6748 0.7723 1.1751 0.0688  0.0275  0.1424  208 GLU D N   
10898 C  CA  . GLU D 207 ? 0.6865 0.7939 1.1765 0.0676  0.0291  0.1403  208 GLU D CA  
10899 C  C   . GLU D 207 ? 0.6375 0.7466 1.1259 0.0638  0.0326  0.1309  208 GLU D C   
10900 O  O   . GLU D 207 ? 0.6431 0.7557 1.1232 0.0601  0.0348  0.1305  208 GLU D O   
10901 C  CB  . GLU D 207 ? 0.7217 0.8362 1.2121 0.0728  0.0258  0.1393  208 GLU D CB  
10902 C  CG  . GLU D 207 ? 0.8061 0.9202 1.2942 0.0785  0.0220  0.1486  208 GLU D CG  
10903 C  CD  . GLU D 207 ? 0.8717 0.9896 1.3459 0.0797  0.0221  0.1555  208 GLU D CD  
10904 O  OE1 . GLU D 207 ? 0.8683 0.9890 1.3356 0.0753  0.0248  0.1528  208 GLU D OE1 
10905 O  OE2 . GLU D 207 ? 0.8777 0.9960 1.3468 0.0861  0.0197  0.1640  208 GLU D OE2 
10906 N  N   . LEU D 208 ? 0.5688 0.6752 1.0640 0.0660  0.0333  0.1239  209 LEU D N   
10907 C  CA  . LEU D 208 ? 0.5659 0.6737 1.0584 0.0647  0.0374  0.1157  209 LEU D CA  
10908 C  C   . LEU D 208 ? 0.5839 0.6847 1.0713 0.0605  0.0379  0.1149  209 LEU D C   
10909 O  O   . LEU D 208 ? 0.6072 0.7116 1.0875 0.0577  0.0410  0.1116  209 LEU D O   
10910 C  CB  . LEU D 208 ? 0.4901 0.5960 0.9896 0.0704  0.0387  0.1093  209 LEU D CB  
10911 C  CG  . LEU D 208 ? 0.4853 0.5925 0.9799 0.0717  0.0438  0.1017  209 LEU D CG  
10912 C  CD1 . LEU D 208 ? 0.4225 0.5418 0.9152 0.0694  0.0484  0.1022  209 LEU D CD1 
10913 C  CD2 . LEU D 208 ? 0.3806 0.4852 0.8801 0.0798  0.0454  0.0960  209 LEU D CD2 
10914 N  N   . ARG D 209 ? 0.5951 0.6862 1.0881 0.0599  0.0341  0.1183  210 ARG D N   
10915 C  CA  . ARG D 209 ? 0.5664 0.6504 1.0590 0.0556  0.0328  0.1179  210 ARG D CA  
10916 C  C   . ARG D 209 ? 0.6098 0.7006 1.0950 0.0505  0.0353  0.1239  210 ARG D C   
10917 O  O   . ARG D 209 ? 0.6445 0.7369 1.1230 0.0477  0.0373  0.1194  210 ARG D O   
10918 C  CB  . ARG D 209 ? 0.5787 0.6514 1.0836 0.0553  0.0274  0.1229  210 ARG D CB  
10919 N  N   . LEU D 210 ? 0.6022 0.6972 1.0874 0.0506  0.0353  0.1342  211 LEU D N   
10920 C  CA  . LEU D 210 ? 0.6332 0.7350 1.1099 0.0479  0.0379  0.1407  211 LEU D CA  
10921 C  C   . LEU D 210 ? 0.5927 0.7023 1.0583 0.0471  0.0407  0.1339  211 LEU D C   
10922 O  O   . LEU D 210 ? 0.6186 0.7296 1.0788 0.0433  0.0428  0.1322  211 LEU D O   
10923 C  CB  . LEU D 210 ? 0.6698 0.7756 1.1447 0.0518  0.0375  0.1517  211 LEU D CB  
10924 C  CG  . LEU D 210 ? 0.7017 0.8014 1.1878 0.0528  0.0361  0.1628  211 LEU D CG  
10925 C  CD1 . LEU D 210 ? 0.7327 0.8376 1.2131 0.0593  0.0364  0.1731  211 LEU D CD1 
10926 C  CD2 . LEU D 210 ? 0.7040 0.8013 1.1966 0.0476  0.0376  0.1693  211 LEU D CD2 
10927 N  N   . ARG D 211 ? 0.5576 0.6723 1.0221 0.0505  0.0403  0.1305  212 ARG D N   
10928 C  CA  . ARG D 211 ? 0.5285 0.6508 0.9863 0.0497  0.0422  0.1256  212 ARG D CA  
10929 C  C   . ARG D 211 ? 0.4700 0.5916 0.9269 0.0473  0.0459  0.1179  212 ARG D C   
10930 O  O   . ARG D 211 ? 0.4906 0.6165 0.9405 0.0448  0.0483  0.1162  212 ARG D O   
10931 C  CB  . ARG D 211 ? 0.5959 0.7233 1.0581 0.0537  0.0397  0.1239  212 ARG D CB  
10932 C  CG  . ARG D 211 ? 0.6923 0.8232 1.1484 0.0570  0.0354  0.1295  212 ARG D CG  
10933 C  CD  . ARG D 211 ? 0.7870 0.9205 1.2504 0.0620  0.0306  0.1287  212 ARG D CD  
10934 N  NE  . ARG D 211 ? 0.8771 1.0145 1.3323 0.0662  0.0250  0.1308  212 ARG D NE  
10935 C  CZ  . ARG D 211 ? 0.9461 1.0860 1.4054 0.0716  0.0185  0.1302  212 ARG D CZ  
10936 N  NH1 . ARG D 211 ? 0.9649 1.1044 1.4376 0.0729  0.0178  0.1285  212 ARG D NH1 
10937 N  NH2 . ARG D 211 ? 0.9672 1.1095 1.4167 0.0767  0.0121  0.1308  212 ARG D NH2 
10938 N  N   . ALA D 212 ? 0.4613 0.5772 0.9239 0.0493  0.0462  0.1132  213 ALA D N   
10939 C  CA  . ALA D 212 ? 0.4961 0.6108 0.9551 0.0495  0.0496  0.1059  213 ALA D CA  
10940 C  C   . ALA D 212 ? 0.5029 0.6134 0.9560 0.0453  0.0490  0.1060  213 ALA D C   
10941 O  O   . ALA D 212 ? 0.5487 0.6622 0.9942 0.0440  0.0522  0.1026  213 ALA D O   
10942 C  CB  . ALA D 212 ? 0.3557 0.4644 0.8199 0.0549  0.0491  0.1002  213 ALA D CB  
10943 N  N   . THR D 213 ? 0.5351 0.6390 0.9932 0.0433  0.0449  0.1108  214 THR D N   
10944 C  CA  . THR D 213 ? 0.5315 0.6325 0.9880 0.0388  0.0438  0.1125  214 THR D CA  
10945 C  C   . THR D 213 ? 0.4604 0.5701 0.9074 0.0358  0.0475  0.1160  214 THR D C   
10946 O  O   . THR D 213 ? 0.5368 0.6479 0.9771 0.0341  0.0494  0.1117  214 THR D O   
10947 C  CB  . THR D 213 ? 0.5724 0.6674 1.0402 0.0365  0.0396  0.1209  214 THR D CB  
10948 O  OG1 . THR D 213 ? 0.6462 0.7458 1.1154 0.0381  0.0406  0.1300  214 THR D OG1 
10949 C  CG2 . THR D 213 ? 0.5316 0.6149 1.0100 0.0386  0.0341  0.1159  214 THR D CG2 
10950 N  N   . ARG D 214 ? 0.4412 0.5566 0.8867 0.0365  0.0480  0.1232  215 ARG D N   
10951 C  CA  . ARG D 214 ? 0.5016 0.6243 0.9372 0.0351  0.0503  0.1264  215 ARG D CA  
10952 C  C   . ARG D 214 ? 0.4808 0.6080 0.9097 0.0348  0.0531  0.1191  215 ARG D C   
10953 O  O   . ARG D 214 ? 0.4286 0.5577 0.8505 0.0323  0.0552  0.1178  215 ARG D O   
10954 C  CB  . ARG D 214 ? 0.5938 0.7207 1.0267 0.0386  0.0491  0.1337  215 ARG D CB  
10955 C  CG  . ARG D 214 ? 0.6753 0.8077 1.0975 0.0389  0.0506  0.1392  215 ARG D CG  
10956 C  CD  . ARG D 214 ? 0.6919 0.8291 1.1058 0.0438  0.0482  0.1387  215 ARG D CD  
10957 N  N   . ALA D 215 ? 0.4557 0.5850 0.8883 0.0376  0.0532  0.1151  216 ALA D N   
10958 C  CA  . ALA D 215 ? 0.4221 0.5567 0.8526 0.0376  0.0563  0.1104  216 ALA D CA  
10959 C  C   . ALA D 215 ? 0.3717 0.5043 0.7985 0.0369  0.0603  0.1052  216 ALA D C   
10960 O  O   . ALA D 215 ? 0.4143 0.5501 0.8345 0.0350  0.0630  0.1042  216 ALA D O   
10961 C  CB  . ALA D 215 ? 0.3224 0.4603 0.7623 0.0408  0.0559  0.1088  216 ALA D CB  
10962 N  N   . PHE D 216 ? 0.3897 0.5166 0.8199 0.0396  0.0601  0.1015  217 PHE D N   
10963 C  CA  . PHE D 216 ? 0.3931 0.5171 0.8175 0.0416  0.0627  0.0955  217 PHE D CA  
10964 C  C   . PHE D 216 ? 0.4270 0.5486 0.8443 0.0376  0.0612  0.0958  217 PHE D C   
10965 O  O   . PHE D 216 ? 0.4337 0.5573 0.8431 0.0379  0.0645  0.0927  217 PHE D O   
10966 C  CB  . PHE D 216 ? 0.4394 0.5554 0.8673 0.0466  0.0603  0.0906  217 PHE D CB  
10967 C  CG  . PHE D 216 ? 0.4726 0.5922 0.9040 0.0531  0.0645  0.0880  217 PHE D CG  
10968 C  CD1 . PHE D 216 ? 0.4550 0.5765 0.8796 0.0591  0.0700  0.0833  217 PHE D CD1 
10969 C  CD2 . PHE D 216 ? 0.4839 0.6057 0.9255 0.0543  0.0633  0.0911  217 PHE D CD2 
10970 C  CE1 . PHE D 216 ? 0.4432 0.5695 0.8723 0.0661  0.0754  0.0828  217 PHE D CE1 
10971 C  CE2 . PHE D 216 ? 0.4812 0.6074 0.9284 0.0605  0.0676  0.0896  217 PHE D CE2 
10972 C  CZ  . PHE D 216 ? 0.4611 0.5902 0.9027 0.0665  0.0742  0.0860  217 PHE D CZ  
10973 N  N   . VAL D 217 ? 0.4341 0.5522 0.8554 0.0341  0.0568  0.1006  218 VAL D N   
10974 C  CA  . VAL D 217 ? 0.4142 0.5312 0.8323 0.0302  0.0554  0.1023  218 VAL D CA  
10975 C  C   . VAL D 217 ? 0.4542 0.5792 0.8637 0.0280  0.0593  0.1051  218 VAL D C   
10976 O  O   . VAL D 217 ? 0.4469 0.5725 0.8502 0.0264  0.0604  0.1033  218 VAL D O   
10977 C  CB  . VAL D 217 ? 0.4923 0.6058 0.9202 0.0272  0.0512  0.1098  218 VAL D CB  
10978 C  CG1 . VAL D 217 ? 0.4792 0.5990 0.9040 0.0239  0.0530  0.1180  218 VAL D CG1 
10979 C  CG2 . VAL D 217 ? 0.5176 0.6216 0.9533 0.0267  0.0454  0.1057  218 VAL D CG2 
10980 N  N   . ALA D 218 ? 0.4182 0.5485 0.8274 0.0286  0.0605  0.1087  219 ALA D N   
10981 C  CA  . ALA D 218 ? 0.4166 0.5530 0.8182 0.0274  0.0627  0.1102  219 ALA D CA  
10982 C  C   . ALA D 218 ? 0.4259 0.5644 0.8234 0.0280  0.0667  0.1048  219 ALA D C   
10983 O  O   . ALA D 218 ? 0.3080 0.4480 0.6980 0.0263  0.0685  0.1043  219 ALA D O   
10984 C  CB  . ALA D 218 ? 0.3119 0.4519 0.7148 0.0293  0.0608  0.1134  219 ALA D CB  
10985 N  N   . ALA D 219 ? 0.3117 0.4510 0.7145 0.0309  0.0687  0.1018  220 ALA D N   
10986 C  CA  . ALA D 219 ? 0.4077 0.5501 0.8084 0.0328  0.0742  0.0988  220 ALA D CA  
10987 C  C   . ALA D 219 ? 0.3941 0.5330 0.7856 0.0340  0.0758  0.0949  220 ALA D C   
10988 O  O   . ALA D 219 ? 0.3132 0.4547 0.6978 0.0335  0.0791  0.0946  220 ALA D O   
10989 C  CB  . ALA D 219 ? 0.3137 0.4581 0.7234 0.0371  0.0769  0.0976  220 ALA D CB  
10990 N  N   . ARG D 220 ? 0.3224 0.4547 0.7143 0.0359  0.0725  0.0916  221 ARG D N   
10991 C  CA  . ARG D 220 ? 0.4112 0.5385 0.7952 0.0382  0.0713  0.0863  221 ARG D CA  
10992 C  C   . ARG D 220 ? 0.3716 0.4996 0.7507 0.0332  0.0695  0.0883  221 ARG D C   
10993 O  O   . ARG D 220 ? 0.3275 0.4555 0.6978 0.0349  0.0710  0.0851  221 ARG D O   
10994 C  CB  . ARG D 220 ? 0.3392 0.4574 0.7275 0.0407  0.0652  0.0819  221 ARG D CB  
10995 C  CG  . ARG D 220 ? 0.4555 0.5669 0.8362 0.0441  0.0612  0.0746  221 ARG D CG  
10996 C  CD  . ARG D 220 ? 0.4747 0.5755 0.8620 0.0467  0.0530  0.0695  221 ARG D CD  
10997 N  NE  . ARG D 220 ? 0.5232 0.6214 0.9240 0.0393  0.0472  0.0754  221 ARG D NE  
10998 C  CZ  . ARG D 220 ? 0.5496 0.6395 0.9617 0.0396  0.0404  0.0744  221 ARG D CZ  
10999 N  NH1 . ARG D 220 ? 0.5726 0.6552 0.9825 0.0473  0.0378  0.0663  221 ARG D NH1 
11000 N  NH2 . ARG D 220 ? 0.5323 0.6211 0.9580 0.0331  0.0367  0.0823  221 ARG D NH2 
11001 N  N   . SER D 221 ? 0.3200 0.4491 0.7044 0.0283  0.0667  0.0942  222 SER D N   
11002 C  CA  . SER D 221 ? 0.3584 0.4896 0.7394 0.0243  0.0658  0.0976  222 SER D CA  
11003 C  C   . SER D 221 ? 0.3646 0.5017 0.7368 0.0241  0.0706  0.0982  222 SER D C   
11004 O  O   . SER D 221 ? 0.3420 0.4800 0.7078 0.0231  0.0711  0.0975  222 SER D O   
11005 C  CB  . SER D 221 ? 0.3661 0.4987 0.7540 0.0212  0.0634  0.1055  222 SER D CB  
11006 O  OG  . SER D 221 ? 0.4503 0.5769 0.8487 0.0205  0.0586  0.1063  222 SER D OG  
11007 N  N   . PHE D 222 ? 0.3649 0.5058 0.7386 0.0249  0.0733  0.0996  223 PHE D N   
11008 C  CA  . PHE D 222 ? 0.3025 0.4479 0.6711 0.0246  0.0769  0.1003  223 PHE D CA  
11009 C  C   . PHE D 222 ? 0.3056 0.4510 0.6684 0.0275  0.0815  0.0965  223 PHE D C   
11010 O  O   . PHE D 222 ? 0.3046 0.4512 0.6597 0.0268  0.0830  0.0965  223 PHE D O   
11011 C  CB  . PHE D 222 ? 0.2997 0.4483 0.6754 0.0251  0.0771  0.1020  223 PHE D CB  
11012 C  CG  . PHE D 222 ? 0.3186 0.4707 0.6928 0.0243  0.0789  0.1030  223 PHE D CG  
11013 C  CD1 . PHE D 222 ? 0.2945 0.4471 0.6625 0.0228  0.0760  0.1047  223 PHE D CD1 
11014 C  CD2 . PHE D 222 ? 0.3223 0.4771 0.7023 0.0257  0.0836  0.1028  223 PHE D CD2 
11015 C  CE1 . PHE D 222 ? 0.3375 0.4918 0.7048 0.0224  0.0763  0.1048  223 PHE D CE1 
11016 C  CE2 . PHE D 222 ? 0.3496 0.5069 0.7315 0.0245  0.0846  0.1044  223 PHE D CE2 
11017 C  CZ  . PHE D 222 ? 0.2924 0.4486 0.6678 0.0226  0.0803  0.1046  223 PHE D CZ  
11018 N  N   . VAL D 223 ? 0.3108 0.4551 0.6763 0.0319  0.0839  0.0938  224 VAL D N   
11019 C  CA  . VAL D 223 ? 0.3171 0.4617 0.6751 0.0374  0.0891  0.0908  224 VAL D CA  
11020 C  C   . VAL D 223 ? 0.3844 0.5247 0.7316 0.0383  0.0859  0.0867  224 VAL D C   
11021 O  O   . VAL D 223 ? 0.4319 0.5741 0.7702 0.0400  0.0892  0.0864  224 VAL D O   
11022 C  CB  . VAL D 223 ? 0.4122 0.5557 0.7733 0.0441  0.0916  0.0883  224 VAL D CB  
11023 C  CG1 . VAL D 223 ? 0.4302 0.5723 0.7791 0.0526  0.0956  0.0841  224 VAL D CG1 
11024 C  CG2 . VAL D 223 ? 0.3203 0.4703 0.6936 0.0442  0.0964  0.0932  224 VAL D CG2 
11025 N  N   . GLN D 224 ? 0.3507 0.4853 0.7006 0.0370  0.0790  0.0838  225 GLN D N   
11026 C  CA  . GLN D 224 ? 0.4038 0.5339 0.7483 0.0369  0.0736  0.0799  225 GLN D CA  
11027 C  C   . GLN D 224 ? 0.3986 0.5330 0.7396 0.0321  0.0743  0.0838  225 GLN D C   
11028 O  O   . GLN D 224 ? 0.3277 0.4614 0.6602 0.0342  0.0738  0.0808  225 GLN D O   
11029 C  CB  . GLN D 224 ? 0.4060 0.5299 0.7606 0.0342  0.0653  0.0787  225 GLN D CB  
11030 C  CG  . GLN D 224 ? 0.5491 0.6655 0.9044 0.0406  0.0617  0.0717  225 GLN D CG  
11031 C  CD  . GLN D 224 ? 0.6725 0.7816 1.0406 0.0373  0.0524  0.0710  225 GLN D CD  
11032 O  OE1 . GLN D 224 ? 0.6987 0.8091 1.0754 0.0306  0.0492  0.0764  225 GLN D OE1 
11033 N  NE2 . GLN D 224 ? 0.7219 0.8234 1.0925 0.0426  0.0483  0.0650  225 GLN D NE2 
11034 N  N   . GLY D 225 ? 0.4300 0.5685 0.7767 0.0270  0.0750  0.0901  226 GLY D N   
11035 C  CA  . GLY D 225 ? 0.3086 0.4513 0.6514 0.0236  0.0759  0.0940  226 GLY D CA  
11036 C  C   . GLY D 225 ? 0.3385 0.4839 0.6719 0.0260  0.0812  0.0931  226 GLY D C   
11037 O  O   . GLY D 225 ? 0.3088 0.4550 0.6353 0.0260  0.0810  0.0925  226 GLY D O   
11038 N  N   . LEU D 226 ? 0.3075 0.4548 0.6427 0.0282  0.0860  0.0938  227 LEU D N   
11039 C  CA  . LEU D 226 ? 0.3085 0.4585 0.6378 0.0310  0.0920  0.0946  227 LEU D CA  
11040 C  C   . LEU D 226 ? 0.3547 0.5025 0.6730 0.0365  0.0931  0.0902  227 LEU D C   
11041 O  O   . LEU D 226 ? 0.3183 0.4675 0.6284 0.0375  0.0950  0.0907  227 LEU D O   
11042 C  CB  . LEU D 226 ? 0.3229 0.4757 0.6605 0.0330  0.0971  0.0971  227 LEU D CB  
11043 C  CG  . LEU D 226 ? 0.3035 0.4589 0.6512 0.0286  0.0958  0.1010  227 LEU D CG  
11044 C  CD1 . LEU D 226 ? 0.3012 0.4595 0.6616 0.0303  0.0994  0.1034  227 LEU D CD1 
11045 C  CD2 . LEU D 226 ? 0.2982 0.4549 0.6420 0.0267  0.0967  0.1033  227 LEU D CD2 
11046 N  N   . GLY D 227 ? 0.3586 0.5024 0.6761 0.0410  0.0910  0.0854  228 GLY D N   
11047 C  CA  . GLY D 227 ? 0.3544 0.4946 0.6596 0.0483  0.0898  0.0794  228 GLY D CA  
11048 C  C   . GLY D 227 ? 0.4245 0.5628 0.7249 0.0456  0.0835  0.0770  228 GLY D C   
11049 O  O   . GLY D 227 ? 0.4616 0.6001 0.7504 0.0504  0.0848  0.0750  228 GLY D O   
11050 N  N   . VAL D 228 ? 0.4289 0.5661 0.7394 0.0386  0.0772  0.0783  229 VAL D N   
11051 C  CA  . VAL D 228 ? 0.4239 0.5607 0.7349 0.0353  0.0711  0.0776  229 VAL D CA  
11052 C  C   . VAL D 228 ? 0.4484 0.5908 0.7530 0.0335  0.0757  0.0820  229 VAL D C   
11053 O  O   . VAL D 228 ? 0.4306 0.5729 0.7281 0.0356  0.0735  0.0795  229 VAL D O   
11054 C  CB  . VAL D 228 ? 0.3853 0.5217 0.7114 0.0284  0.0654  0.0812  229 VAL D CB  
11055 C  CG1 . VAL D 228 ? 0.4032 0.5417 0.7330 0.0248  0.0608  0.0832  229 VAL D CG1 
11056 C  CG2 . VAL D 228 ? 0.3499 0.4791 0.6836 0.0302  0.0592  0.0763  229 VAL D CG2 
11057 N  N   . ALA D 229 ? 0.3533 0.4999 0.6607 0.0302  0.0809  0.0879  230 ALA D N   
11058 C  CA  . ALA D 229 ? 0.3664 0.5171 0.6680 0.0292  0.0847  0.0915  230 ALA D CA  
11059 C  C   . ALA D 229 ? 0.4019 0.5524 0.6922 0.0353  0.0894  0.0894  230 ALA D C   
11060 O  O   . ALA D 229 ? 0.4785 0.6301 0.7611 0.0364  0.0891  0.0892  230 ALA D O   
11061 C  CB  . ALA D 229 ? 0.3041 0.4574 0.6108 0.0263  0.0879  0.0964  230 ALA D CB  
11062 N  N   . SER D 230 ? 0.3817 0.5315 0.6711 0.0400  0.0941  0.0888  231 SER D N   
11063 C  CA  . SER D 230 ? 0.4130 0.5635 0.6914 0.0478  0.1001  0.0885  231 SER D CA  
11064 C  C   . SER D 230 ? 0.4153 0.5625 0.6813 0.0533  0.0951  0.0821  231 SER D C   
11065 O  O   . SER D 230 ? 0.4321 0.5805 0.6873 0.0576  0.0978  0.0827  231 SER D O   
11066 C  CB  . SER D 230 ? 0.4092 0.5602 0.6897 0.0535  0.1060  0.0893  231 SER D CB  
11067 O  OG  . SER D 230 ? 0.4808 0.6338 0.7508 0.0624  0.1138  0.0914  231 SER D OG  
11068 N  N   . ASP D 231 ? 0.5063 0.6487 0.7749 0.0535  0.0868  0.0758  232 ASP D N   
11069 C  CA  . ASP D 231 ? 0.5787 0.7166 0.8381 0.0591  0.0791  0.0681  232 ASP D CA  
11070 C  C   . ASP D 231 ? 0.5151 0.6549 0.7755 0.0542  0.0742  0.0688  232 ASP D C   
11071 O  O   . ASP D 231 ? 0.4575 0.5960 0.7065 0.0601  0.0713  0.0646  232 ASP D O   
11072 C  CB  . ASP D 231 ? 0.7234 0.8545 0.9893 0.0598  0.0698  0.0611  232 ASP D CB  
11073 C  CG  . ASP D 231 ? 0.8767 1.0035 1.1313 0.0717  0.0714  0.0551  232 ASP D CG  
11074 O  OD1 . ASP D 231 ? 0.9224 1.0507 1.1608 0.0814  0.0773  0.0547  232 ASP D OD1 
11075 O  OD2 . ASP D 231 ? 0.9123 1.0343 1.1738 0.0723  0.0672  0.0514  232 ASP D OD2 
11076 N  N   . VAL D 232 ? 0.5111 0.6543 0.7844 0.0447  0.0732  0.0742  233 VAL D N   
11077 C  CA  . VAL D 232 ? 0.4663 0.6127 0.7416 0.0408  0.0696  0.0762  233 VAL D CA  
11078 C  C   . VAL D 232 ? 0.4731 0.6233 0.7370 0.0431  0.0768  0.0798  233 VAL D C   
11079 O  O   . VAL D 232 ? 0.4347 0.5861 0.6929 0.0448  0.0742  0.0786  233 VAL D O   
11080 C  CB  . VAL D 232 ? 0.5122 0.6623 0.8031 0.0320  0.0679  0.0824  233 VAL D CB  
11081 C  CG1 . VAL D 232 ? 0.5075 0.6536 0.8118 0.0295  0.0614  0.0805  233 VAL D CG1 
11082 C  CG2 . VAL D 232 ? 0.5234 0.6773 0.8144 0.0291  0.0756  0.0891  233 VAL D CG2 
11083 N  N   . VAL D 233 ? 0.4638 0.6155 0.7259 0.0435  0.0854  0.0842  234 VAL D N   
11084 C  CA  . VAL D 233 ? 0.4474 0.6017 0.7008 0.0461  0.0920  0.0881  234 VAL D CA  
11085 C  C   . VAL D 233 ? 0.4711 0.6235 0.7096 0.0559  0.0933  0.0843  234 VAL D C   
11086 O  O   . VAL D 233 ? 0.4849 0.6384 0.7146 0.0586  0.0932  0.0845  234 VAL D O   
11087 C  CB  . VAL D 233 ? 0.3268 0.4826 0.5854 0.0446  0.0998  0.0939  234 VAL D CB  
11088 C  CG1 . VAL D 233 ? 0.3296 0.4869 0.5813 0.0481  0.1065  0.0983  234 VAL D CG1 
11089 C  CG2 . VAL D 233 ? 0.3156 0.4727 0.5854 0.0369  0.0975  0.0969  234 VAL D CG2 
11090 N  N   . ARG D 234 ? 0.3556 0.5052 0.5901 0.0623  0.0944  0.0808  235 ARG D N   
11091 C  CA  . ARG D 234 ? 0.4936 0.6411 0.7111 0.0745  0.0956  0.0768  235 ARG D CA  
11092 C  C   . ARG D 234 ? 0.4869 0.6314 0.6966 0.0775  0.0850  0.0692  235 ARG D C   
11093 O  O   . ARG D 234 ? 0.4721 0.6169 0.6672 0.0854  0.0863  0.0684  235 ARG D O   
11094 C  CB  . ARG D 234 ? 0.5602 0.7047 0.7749 0.0818  0.0967  0.0730  235 ARG D CB  
11095 C  CG  . ARG D 234 ? 0.6734 0.8135 0.8688 0.0962  0.0932  0.0651  235 ARG D CG  
11096 C  CD  . ARG D 234 ? 0.7885 0.9252 0.9812 0.1041  0.0938  0.0608  235 ARG D CD  
11097 N  NE  . ARG D 234 ? 0.8983 1.0273 1.0762 0.1155  0.0832  0.0486  235 ARG D NE  
11098 C  CZ  . ARG D 234 ? 0.9667 1.0886 1.1527 0.1117  0.0689  0.0393  235 ARG D CZ  
11099 N  NH1 . ARG D 234 ? 0.9805 1.1032 1.1883 0.0971  0.0655  0.0422  235 ARG D NH1 
11100 N  NH2 . ARG D 234 ? 1.0114 1.1251 1.1842 0.1232  0.0577  0.0272  235 ARG D NH2 
11101 N  N   . LYS D 235 ? 0.4497 0.5916 0.6710 0.0713  0.0744  0.0642  236 LYS D N   
11102 C  CA  . LYS D 235 ? 0.4612 0.6001 0.6804 0.0734  0.0624  0.0568  236 LYS D CA  
11103 C  C   . LYS D 235 ? 0.4514 0.5956 0.6738 0.0680  0.0617  0.0611  236 LYS D C   
11104 O  O   . LYS D 235 ? 0.4188 0.5621 0.6332 0.0731  0.0554  0.0565  236 LYS D O   
11105 C  CB  . LYS D 235 ? 0.4539 0.5883 0.6891 0.0684  0.0509  0.0513  236 LYS D CB  
11106 C  CG  . LYS D 235 ? 0.4886 0.6143 0.7149 0.0789  0.0433  0.0405  236 LYS D CG  
11107 C  CD  . LYS D 235 ? 0.5604 0.6805 0.8056 0.0731  0.0314  0.0357  236 LYS D CD  
11108 C  CE  . LYS D 235 ? 0.6614 0.7712 0.8966 0.0849  0.0226  0.0234  236 LYS D CE  
11109 N  NZ  . LYS D 235 ? 0.6754 0.7787 0.9308 0.0792  0.0116  0.0193  236 LYS D NZ  
11110 N  N   . VAL D 236 ? 0.4828 0.6322 0.7158 0.0588  0.0676  0.0695  237 VAL D N   
11111 C  CA  . VAL D 236 ? 0.4611 0.6157 0.6957 0.0549  0.0682  0.0741  237 VAL D CA  
11112 C  C   . VAL D 236 ? 0.4695 0.6250 0.6873 0.0620  0.0755  0.0763  237 VAL D C   
11113 O  O   . VAL D 236 ? 0.5211 0.6790 0.7340 0.0634  0.0735  0.0766  237 VAL D O   
11114 C  CB  . VAL D 236 ? 0.4152 0.5745 0.6628 0.0456  0.0723  0.0820  237 VAL D CB  
11115 C  CG1 . VAL D 236 ? 0.3509 0.5153 0.5961 0.0441  0.0750  0.0870  237 VAL D CG1 
11116 C  CG2 . VAL D 236 ? 0.4351 0.5950 0.7001 0.0393  0.0651  0.0818  237 VAL D CG2 
11117 N  N   . ALA D 237 ? 0.5677 0.7218 0.7780 0.0667  0.0841  0.0786  238 ALA D N   
11118 C  CA  . ALA D 237 ? 0.5470 0.7021 0.7435 0.0740  0.0924  0.0827  238 ALA D CA  
11119 C  C   . ALA D 237 ? 0.6125 0.7658 0.7923 0.0845  0.0876  0.0769  238 ALA D C   
11120 O  O   . ALA D 237 ? 0.6244 0.7794 0.7933 0.0898  0.0925  0.0807  238 ALA D O   
11121 C  CB  . ALA D 237 ? 0.5291 0.6839 0.7238 0.0782  0.1024  0.0871  238 ALA D CB  
11122 N  N   . GLN D 238 ? 0.6866 0.8359 0.8649 0.0881  0.0769  0.0674  239 GLN D N   
11123 C  CA  . GLN D 238 ? 0.7874 0.9335 0.9485 0.1001  0.0701  0.0598  239 GLN D CA  
11124 C  C   . GLN D 238 ? 0.7382 0.8861 0.9037 0.0966  0.0602  0.0570  239 GLN D C   
11125 O  O   . GLN D 238 ? 0.7576 0.9043 0.9081 0.1063  0.0558  0.0526  239 GLN D O   
11126 C  CB  . GLN D 238 ? 0.8981 1.0375 1.0550 0.1073  0.0612  0.0493  239 GLN D CB  
11127 C  CG  . GLN D 238 ? 1.0333 1.1680 1.1657 0.1248  0.0565  0.0412  239 GLN D CG  
11128 C  CD  . GLN D 238 ? 1.1460 1.2761 1.2801 0.1266  0.0380  0.0294  239 GLN D CD  
11129 O  OE1 . GLN D 238 ? 1.1628 1.2959 1.3152 0.1151  0.0313  0.0305  239 GLN D OE1 
11130 N  NE2 . GLN D 238 ? 1.1920 1.3149 1.3075 0.1421  0.0292  0.0182  239 GLN D NE2 
11131 N  N   . VAL D 239 ? 0.6930 0.8445 0.8788 0.0839  0.0570  0.0601  240 VAL D N   
11132 C  CA  . VAL D 239 ? 0.7118 0.8667 0.9056 0.0804  0.0480  0.0587  240 VAL D CA  
11133 C  C   . VAL D 239 ? 0.6856 0.8443 0.8670 0.0843  0.0544  0.0638  240 VAL D C   
11134 O  O   . VAL D 239 ? 0.7081 0.8691 0.8866 0.0822  0.0661  0.0720  240 VAL D O   
11135 C  CB  . VAL D 239 ? 0.6272 0.7869 0.8457 0.0672  0.0458  0.0637  240 VAL D CB  
11136 C  CG1 . VAL D 239 ? 0.5914 0.7470 0.8220 0.0633  0.0418  0.0607  240 VAL D CG1 
11137 C  CG2 . VAL D 239 ? 0.6002 0.7653 0.8210 0.0612  0.0575  0.0740  240 VAL D CG2 
11138 N  N   . PRO D 240 ? 0.6413 0.7999 0.8155 0.0907  0.0456  0.0584  241 PRO D N   
11139 C  CA  . PRO D 240 ? 0.6560 0.8174 0.8165 0.0964  0.0501  0.0621  241 PRO D CA  
11140 C  C   . PRO D 240 ? 0.5922 0.7607 0.7656 0.0874  0.0523  0.0693  241 PRO D C   
11141 O  O   . PRO D 240 ? 0.5850 0.7573 0.7784 0.0782  0.0473  0.0702  241 PRO D O   
11142 C  CB  . PRO D 240 ? 0.6387 0.7969 0.7887 0.1068  0.0370  0.0518  241 PRO D CB  
11143 C  CG  . PRO D 240 ? 0.6530 0.8096 0.8232 0.1004  0.0231  0.0448  241 PRO D CG  
11144 C  CD  . PRO D 240 ? 0.6531 0.8079 0.8328 0.0935  0.0293  0.0476  241 PRO D CD  
11145 N  N   . LEU D 241 ? 0.6032 0.7734 0.7652 0.0910  0.0601  0.0750  242 LEU D N   
11146 C  CA  . LEU D 241 ? 0.6328 0.8092 0.8030 0.0857  0.0612  0.0805  242 LEU D CA  
11147 C  C   . LEU D 241 ? 0.6543 0.8337 0.8252 0.0895  0.0498  0.0755  242 LEU D C   
11148 O  O   . LEU D 241 ? 0.7027 0.8786 0.8579 0.0998  0.0452  0.0697  242 LEU D O   
11149 C  CB  . LEU D 241 ? 0.6406 0.8164 0.7996 0.0883  0.0729  0.0882  242 LEU D CB  
11150 C  CG  . LEU D 241 ? 0.6119 0.7853 0.7745 0.0835  0.0833  0.0943  242 LEU D CG  
11151 C  CD1 . LEU D 241 ? 0.6393 0.8105 0.7909 0.0885  0.0929  0.1010  242 LEU D CD1 
11152 C  CD2 . LEU D 241 ? 0.5996 0.7767 0.7786 0.0735  0.0832  0.0975  242 LEU D CD2 
11153 N  N   . GLY D 242 ? 0.6116 0.7980 0.8011 0.0821  0.0453  0.0780  243 GLY D N   
11154 C  CA  . GLY D 242 ? 0.6152 0.8060 0.8110 0.0845  0.0339  0.0742  243 GLY D CA  
11155 C  C   . GLY D 242 ? 0.5720 0.7645 0.7527 0.0916  0.0370  0.0765  243 GLY D C   
11156 O  O   . GLY D 242 ? 0.5953 0.7868 0.7652 0.0925  0.0486  0.0829  243 GLY D O   
11157 N  N   . PRO D 243 ? 0.5522 0.7470 0.7333 0.0969  0.0255  0.0711  244 PRO D N   
11158 C  CA  . PRO D 243 ? 0.5176 0.7146 0.6855 0.1042  0.0267  0.0729  244 PRO D CA  
11159 C  C   . PRO D 243 ? 0.5167 0.7212 0.6932 0.0985  0.0352  0.0827  244 PRO D C   
11160 O  O   . PRO D 243 ? 0.5520 0.7546 0.7132 0.1029  0.0441  0.0875  244 PRO D O   
11161 C  CB  . PRO D 243 ? 0.5035 0.7029 0.6793 0.1082  0.0096  0.0646  244 PRO D CB  
11162 C  CG  . PRO D 243 ? 0.5290 0.7224 0.7105 0.1077  -0.0001 0.0558  244 PRO D CG  
11163 C  CD  . PRO D 243 ? 0.5162 0.7101 0.7105 0.0970  0.0093  0.0620  244 PRO D CD  
11164 N  N   . GLU D 244 ? 0.4917 0.7044 0.6923 0.0898  0.0323  0.0862  245 GLU D N   
11165 C  CA  . GLU D 244 ? 0.4704 0.6907 0.6788 0.0859  0.0403  0.0954  245 GLU D CA  
11166 C  C   . GLU D 244 ? 0.5005 0.7150 0.6961 0.0850  0.0535  0.1002  245 GLU D C   
11167 O  O   . GLU D 244 ? 0.5073 0.7221 0.6943 0.0877  0.0602  0.1049  245 GLU D O   
11168 C  CB  . GLU D 244 ? 0.4866 0.7165 0.7229 0.0775  0.0372  0.0997  245 GLU D CB  
11169 C  CG  . GLU D 244 ? 0.6055 0.8433 0.8617 0.0772  0.0241  0.0974  245 GLU D CG  
11170 C  CD  . GLU D 244 ? 0.7128 0.9584 0.9683 0.0819  0.0240  0.1010  245 GLU D CD  
11171 O  OE1 . GLU D 244 ? 0.7221 0.9697 0.9682 0.0833  0.0350  0.1076  245 GLU D OE1 
11172 O  OE2 . GLU D 244 ? 0.7516 1.0011 1.0162 0.0846  0.0120  0.0967  245 GLU D OE2 
11173 N  N   . CYS D 245 ? 0.4748 0.6837 0.6707 0.0812  0.0561  0.0987  246 CYS D N   
11174 C  CA  . CYS D 245 ? 0.4900 0.6928 0.6768 0.0800  0.0668  0.1025  246 CYS D CA  
11175 C  C   . CYS D 245 ? 0.4549 0.6512 0.6217 0.0876  0.0720  0.1031  246 CYS D C   
11176 O  O   . CYS D 245 ? 0.4035 0.5975 0.5655 0.0880  0.0795  0.1082  246 CYS D O   
11177 C  CB  . CYS D 245 ? 0.4887 0.6868 0.6795 0.0758  0.0673  0.0999  246 CYS D CB  
11178 S  SG  . CYS D 245 ? 1.3996 1.5898 1.5816 0.0747  0.0788  0.1038  246 CYS D SG  
11179 N  N   . SER D 246 ? 0.4863 0.6794 0.6418 0.0946  0.0677  0.0979  247 SER D N   
11180 C  CA  . SER D 246 ? 0.5328 0.7205 0.6689 0.1036  0.0734  0.0999  247 SER D CA  
11181 C  C   . SER D 246 ? 0.5603 0.7508 0.6923 0.1068  0.0750  0.1042  247 SER D C   
11182 O  O   . SER D 246 ? 0.6373 0.8234 0.7599 0.1102  0.0832  0.1098  247 SER D O   
11183 C  CB  . SER D 246 ? 0.5663 0.7512 0.6890 0.1130  0.0670  0.0930  247 SER D CB  
11184 O  OG  . SER D 246 ? 0.6118 0.7923 0.7147 0.1231  0.0742  0.0967  247 SER D OG  
11185 N  N   . ARG D 247 ? 0.5153 0.7134 0.6566 0.1057  0.0670  0.1022  248 ARG D N   
11186 C  CA  . ARG D 247 ? 0.5184 0.7202 0.6569 0.1093  0.0677  0.1059  248 ARG D CA  
11187 C  C   . ARG D 247 ? 0.4796 0.6815 0.6238 0.1044  0.0757  0.1124  248 ARG D C   
11188 O  O   . ARG D 247 ? 0.3884 0.5867 0.5236 0.1085  0.0809  0.1166  248 ARG D O   
11189 C  CB  . ARG D 247 ? 0.5374 0.7486 0.6878 0.1093  0.0568  0.1026  248 ARG D CB  
11190 C  CG  . ARG D 247 ? 0.6019 0.8119 0.7477 0.1150  0.0457  0.0942  248 ARG D CG  
11191 C  CD  . ARG D 247 ? 0.6712 0.8886 0.8225 0.1191  0.0353  0.0918  248 ARG D CD  
11192 N  NE  . ARG D 247 ? 0.7399 0.9683 0.9159 0.1114  0.0332  0.0960  248 ARG D NE  
11193 C  CZ  . ARG D 247 ? 0.8034 1.0379 1.0025 0.1050  0.0244  0.0936  248 ARG D CZ  
11194 N  NH1 . ARG D 247 ? 0.8160 1.0450 1.0159 0.1052  0.0155  0.0855  248 ARG D NH1 
11195 N  NH2 . ARG D 247 ? 0.8085 1.0544 1.0304 0.0992  0.0247  0.1001  248 ARG D NH2 
11196 N  N   . ALA D 248 ? 0.4131 0.6183 0.5715 0.0967  0.0759  0.1131  249 ALA D N   
11197 C  CA  . ALA D 248 ? 0.4264 0.6308 0.5883 0.0936  0.0822  0.1179  249 ALA D CA  
11198 C  C   . ALA D 248 ? 0.4445 0.6379 0.5967 0.0945  0.0894  0.1199  249 ALA D C   
11199 O  O   . ALA D 248 ? 0.5090 0.6985 0.6583 0.0960  0.0933  0.1232  249 ALA D O   
11200 C  CB  . ALA D 248 ? 0.3540 0.5636 0.5309 0.0867  0.0813  0.1183  249 ALA D CB  
11201 N  N   . VAL D 249 ? 0.3901 0.5783 0.5386 0.0940  0.0907  0.1181  250 VAL D N   
11202 C  CA  . VAL D 249 ? 0.3813 0.5605 0.5248 0.0945  0.0979  0.1214  250 VAL D CA  
11203 C  C   . VAL D 249 ? 0.4585 0.6335 0.5902 0.1021  0.1016  0.1255  250 VAL D C   
11204 O  O   . VAL D 249 ? 0.4968 0.6653 0.6290 0.1022  0.1068  0.1304  250 VAL D O   
11205 C  CB  . VAL D 249 ? 0.4395 0.6161 0.5826 0.0934  0.0991  0.1193  250 VAL D CB  
11206 C  CG1 . VAL D 249 ? 0.4634 0.6325 0.6015 0.0961  0.1074  0.1247  250 VAL D CG1 
11207 C  CG2 . VAL D 249 ? 0.4113 0.5898 0.5671 0.0853  0.0971  0.1169  250 VAL D CG2 
11208 N  N   . MET D 250 ? 0.4421 0.6204 0.5642 0.1087  0.0981  0.1235  251 MET D N   
11209 C  CA  . MET D 250 ? 0.4329 0.6081 0.5427 0.1172  0.1013  0.1278  251 MET D CA  
11210 C  C   . MET D 250 ? 0.4737 0.6488 0.5866 0.1168  0.1017  0.1308  251 MET D C   
11211 O  O   . MET D 250 ? 0.5002 0.6687 0.6092 0.1200  0.1070  0.1366  251 MET D O   
11212 C  CB  . MET D 250 ? 0.4190 0.5985 0.5174 0.1253  0.0952  0.1235  251 MET D CB  
11213 C  CG  . MET D 250 ? 0.4314 0.6096 0.5172 0.1346  0.0969  0.1277  251 MET D CG  
11214 S  SD  . MET D 250 ? 0.5441 0.7130 0.6213 0.1400  0.1097  0.1383  251 MET D SD  
11215 C  CE  . MET D 250 ? 0.8329 1.0017 0.8966 0.1508  0.1095  0.1425  251 MET D CE  
11216 N  N   . LYS D 251 ? 0.4613 0.6438 0.5822 0.1135  0.0961  0.1275  252 LYS D N   
11217 C  CA  . LYS D 251 ? 0.4828 0.6661 0.6057 0.1146  0.0963  0.1299  252 LYS D CA  
11218 C  C   . LYS D 251 ? 0.4717 0.6470 0.5996 0.1107  0.1005  0.1322  252 LYS D C   
11219 O  O   . LYS D 251 ? 0.4649 0.6355 0.5909 0.1137  0.1018  0.1346  252 LYS D O   
11220 C  CB  . LYS D 251 ? 0.5081 0.7031 0.6400 0.1128  0.0905  0.1273  252 LYS D CB  
11221 C  CG  . LYS D 251 ? 0.5585 0.7563 0.6911 0.1161  0.0910  0.1299  252 LYS D CG  
11222 C  CD  . LYS D 251 ? 0.6156 0.8272 0.7595 0.1150  0.0866  0.1294  252 LYS D CD  
11223 C  CE  . LYS D 251 ? 0.6618 0.8772 0.8059 0.1197  0.0883  0.1326  252 LYS D CE  
11224 N  NZ  . LYS D 251 ? 0.6951 0.9246 0.8532 0.1182  0.0868  0.1346  252 LYS D NZ  
11225 N  N   . LEU D 252 ? 0.5051 0.6782 0.6395 0.1047  0.1017  0.1308  253 LEU D N   
11226 C  CA  . LEU D 252 ? 0.4519 0.6172 0.5924 0.1009  0.1039  0.1318  253 LEU D CA  
11227 C  C   . LEU D 252 ? 0.3902 0.5445 0.5298 0.1024  0.1087  0.1367  253 LEU D C   
11228 O  O   . LEU D 252 ? 0.3928 0.5390 0.5367 0.1022  0.1087  0.1382  253 LEU D O   
11229 C  CB  . LEU D 252 ? 0.4205 0.5877 0.5693 0.0942  0.1031  0.1290  253 LEU D CB  
11230 C  CG  . LEU D 252 ? 0.4178 0.5768 0.5736 0.0902  0.1041  0.1291  253 LEU D CG  
11231 C  CD1 . LEU D 252 ? 0.3702 0.5286 0.5261 0.0922  0.1009  0.1274  253 LEU D CD1 
11232 C  CD2 . LEU D 252 ? 0.4048 0.5658 0.5676 0.0842  0.1040  0.1269  253 LEU D CD2 
11233 N  N   . VAL D 253 ? 0.4579 0.6121 0.5928 0.1047  0.1126  0.1397  254 VAL D N   
11234 C  CA  . VAL D 253 ? 0.5183 0.6640 0.6562 0.1056  0.1190  0.1466  254 VAL D CA  
11235 C  C   . VAL D 253 ? 0.5960 0.7384 0.7259 0.1133  0.1228  0.1532  254 VAL D C   
11236 O  O   . VAL D 253 ? 0.6770 0.8110 0.8135 0.1136  0.1250  0.1586  254 VAL D O   
11237 C  CB  . VAL D 253 ? 0.5224 0.6700 0.6608 0.1045  0.1230  0.1476  254 VAL D CB  
11238 C  CG1 . VAL D 253 ? 0.5265 0.6675 0.6706 0.1061  0.1312  0.1572  254 VAL D CG1 
11239 C  CG2 . VAL D 253 ? 0.3912 0.5410 0.5391 0.0966  0.1196  0.1420  254 VAL D CG2 
11240 N  N   . TYR D 254 ? 0.5435 0.6919 0.6600 0.1201  0.1227  0.1528  255 TYR D N   
11241 C  CA  . TYR D 254 ? 0.5118 0.6573 0.6187 0.1289  0.1273  0.1601  255 TYR D CA  
11242 C  C   . TYR D 254 ? 0.5207 0.6696 0.6183 0.1344  0.1225  0.1578  255 TYR D C   
11243 O  O   . TYR D 254 ? 0.5371 0.6856 0.6236 0.1431  0.1252  0.1627  255 TYR D O   
11244 C  CB  . TYR D 254 ? 0.5543 0.7029 0.6500 0.1358  0.1322  0.1631  255 TYR D CB  
11245 C  CG  . TYR D 254 ? 0.6376 0.7833 0.7422 0.1325  0.1393  0.1681  255 TYR D CG  
11246 C  CD1 . TYR D 254 ? 0.6007 0.7392 0.7180 0.1309  0.1467  0.1786  255 TYR D CD1 
11247 C  CD2 . TYR D 254 ? 0.5945 0.7447 0.6966 0.1314  0.1383  0.1628  255 TYR D CD2 
11248 C  CE1 . TYR D 254 ? 0.6189 0.7561 0.7474 0.1280  0.1533  0.1842  255 TYR D CE1 
11249 C  CE2 . TYR D 254 ? 0.6454 0.7940 0.7561 0.1291  0.1452  0.1678  255 TYR D CE2 
11250 C  CZ  . TYR D 254 ? 0.6571 0.7998 0.7814 0.1274  0.1530  0.1788  255 TYR D CZ  
11251 O  OH  . TYR D 254 ? 0.6268 0.7689 0.7626 0.1250  0.1600  0.1848  255 TYR D OH  
11252 N  N   . CYS D 255 ? 0.4307 0.5837 0.5329 0.1304  0.1158  0.1513  256 CYS D N   
11253 C  CA  . CYS D 255 ? 0.5288 0.6857 0.6247 0.1358  0.1117  0.1500  256 CYS D CA  
11254 C  C   . CYS D 255 ? 0.5947 0.7429 0.6940 0.1371  0.1132  0.1541  256 CYS D C   
11255 O  O   . CYS D 255 ? 0.5440 0.6926 0.6368 0.1435  0.1120  0.1557  256 CYS D O   
11256 C  CB  . CYS D 255 ? 0.4485 0.6159 0.5486 0.1325  0.1046  0.1427  256 CYS D CB  
11257 S  SG  . CYS D 255 ? 0.5604 0.7382 0.6550 0.1350  0.0989  0.1373  256 CYS D SG  
11258 N  N   . ALA D 256 ? 0.5976 0.7373 0.7078 0.1315  0.1148  0.1552  257 ALA D N   
11259 C  CA  . ALA D 256 ? 0.4418 0.5704 0.5572 0.1329  0.1149  0.1586  257 ALA D CA  
11260 C  C   . ALA D 256 ? 0.6535 0.7760 0.7658 0.1386  0.1209  0.1684  257 ALA D C   
11261 O  O   . ALA D 256 ? 0.6886 0.8056 0.7985 0.1439  0.1203  0.1715  257 ALA D O   
11262 C  CB  . ALA D 256 ? 0.4374 0.5575 0.5667 0.1260  0.1137  0.1572  257 ALA D CB  
11263 N  N   . HIS D 257 ? 0.4582 0.5818 0.5702 0.1386  0.1271  0.1738  258 HIS D N   
11264 C  CA  . HIS D 257 ? 0.4727 0.5928 0.5802 0.1457  0.1347  0.1849  258 HIS D CA  
11265 C  C   . HIS D 257 ? 0.6323 0.7583 0.7220 0.1553  0.1332  0.1845  258 HIS D C   
11266 O  O   . HIS D 257 ? 0.7091 0.8299 0.7957 0.1617  0.1357  0.1916  258 HIS D O   
11267 C  CB  . HIS D 257 ? 0.4750 0.5979 0.5824 0.1459  0.1422  0.1903  258 HIS D CB  
11268 C  CG  . HIS D 257 ? 0.6258 0.7440 0.7521 0.1367  0.1438  0.1913  258 HIS D CG  
11269 N  ND1 . HIS D 257 ? 0.4528 0.5736 0.5848 0.1285  0.1376  0.1812  258 HIS D ND1 
11270 C  CD2 . HIS D 257 ? 0.6017 0.7133 0.7440 0.1346  0.1508  0.2020  258 HIS D CD2 
11271 C  CE1 . HIS D 257 ? 0.5790 0.6946 0.7281 0.1220  0.1399  0.1845  258 HIS D CE1 
11272 N  NE2 . HIS D 257 ? 0.5601 0.6702 0.7171 0.1252  0.1477  0.1971  258 HIS D NE2 
11273 N  N   . CYS D 258 ? 0.6594 0.7960 0.7391 0.1563  0.1282  0.1761  259 CYS D N   
11274 C  CA  . CYS D 258 ? 0.6316 0.7750 0.6959 0.1653  0.1248  0.1742  259 CYS D CA  
11275 C  C   . CYS D 258 ? 0.6557 0.7982 0.7207 0.1672  0.1202  0.1726  259 CYS D C   
11276 O  O   . CYS D 258 ? 0.6624 0.8072 0.7164 0.1759  0.1190  0.1745  259 CYS D O   
11277 C  CB  . CYS D 258 ? 0.6350 0.7893 0.6939 0.1644  0.1181  0.1645  259 CYS D CB  
11278 S  SG  . CYS D 258 ? 1.1487 1.3046 1.1989 0.1677  0.1222  0.1653  259 CYS D SG  
11279 N  N   . LEU D 259 ? 0.6403 0.7794 0.7173 0.1603  0.1174  0.1690  260 LEU D N   
11280 C  CA  . LEU D 259 ? 0.6563 0.7951 0.7332 0.1633  0.1129  0.1667  260 LEU D CA  
11281 C  C   . LEU D 259 ? 0.7143 0.8386 0.7985 0.1636  0.1149  0.1718  260 LEU D C   
11282 O  O   . LEU D 259 ? 0.7046 0.8257 0.7931 0.1630  0.1105  0.1674  260 LEU D O   
11283 C  CB  . LEU D 259 ? 0.6113 0.7586 0.6937 0.1583  0.1071  0.1581  260 LEU D CB  
11284 C  CG  . LEU D 259 ? 0.5575 0.7196 0.6361 0.1589  0.1029  0.1532  260 LEU D CG  
11285 C  CD1 . LEU D 259 ? 0.5558 0.7261 0.6442 0.1522  0.0992  0.1472  260 LEU D CD1 
11286 C  CD2 . LEU D 259 ? 0.5480 0.7162 0.6187 0.1675  0.0997  0.1538  260 LEU D CD2 
11287 N  N   . GLY D 260 ? 0.7399 0.8556 0.8262 0.1653  0.1213  0.1813  261 GLY D N   
11288 C  CA  . GLY D 260 ? 0.7465 0.8479 0.8417 0.1667  0.1225  0.1878  261 GLY D CA  
11289 C  C   . GLY D 260 ? 0.7232 0.8134 0.8363 0.1588  0.1204  0.1863  261 GLY D C   
11290 O  O   . GLY D 260 ? 0.7679 0.8447 0.8914 0.1596  0.1196  0.1910  261 GLY D O   
11291 N  N   . VAL D 261 ? 0.7505 0.8453 0.8683 0.1514  0.1184  0.1796  262 VAL D N   
11292 C  CA  . VAL D 261 ? 0.7637 0.8480 0.8981 0.1445  0.1149  0.1771  262 VAL D CA  
11293 C  C   . VAL D 261 ? 0.7634 0.8500 0.9072 0.1370  0.1192  0.1794  262 VAL D C   
11294 O  O   . VAL D 261 ? 0.7619 0.8522 0.9084 0.1314  0.1154  0.1715  262 VAL D O   
11295 C  CB  . VAL D 261 ? 0.7586 0.8439 0.8902 0.1439  0.1063  0.1652  262 VAL D CB  
11296 C  CG1 . VAL D 261 ? 0.7683 0.8447 0.8972 0.1509  0.1012  0.1636  262 VAL D CG1 
11297 C  CG2 . VAL D 261 ? 0.7641 0.8664 0.8834 0.1444  0.1062  0.1595  262 VAL D CG2 
11298 N  N   . PRO D 262 ? 0.7595 0.8445 0.9087 0.1378  0.1276  0.1910  263 PRO D N   
11299 C  CA  . PRO D 262 ? 0.7596 0.8479 0.9175 0.1323  0.1330  0.1946  263 PRO D CA  
11300 C  C   . PRO D 262 ? 0.8020 0.8807 0.9821 0.1238  0.1288  0.1929  263 PRO D C   
11301 O  O   . PRO D 262 ? 0.7917 0.8748 0.9774 0.1180  0.1295  0.1902  263 PRO D O   
11302 C  CB  . PRO D 262 ? 0.7570 0.8450 0.9153 0.1381  0.1438  0.2096  263 PRO D CB  
11303 C  CG  . PRO D 262 ? 0.7658 0.8440 0.9273 0.1428  0.1426  0.2152  263 PRO D CG  
11304 C  CD  . PRO D 262 ? 0.7711 0.8508 0.9194 0.1449  0.1332  0.2027  263 PRO D CD  
11305 N  N   . GLY D 263 ? 0.8241 0.8894 1.0172 0.1236  0.1234  0.1938  264 GLY D N   
11306 C  CA  . GLY D 263 ? 0.8433 0.8976 1.0589 0.1165  0.1170  0.1914  264 GLY D CA  
11307 C  C   . GLY D 263 ? 0.8284 0.8847 1.0386 0.1133  0.1077  0.1766  264 GLY D C   
11308 O  O   . GLY D 263 ? 0.8208 0.8715 1.0466 0.1073  0.1026  0.1731  264 GLY D O   
11309 N  N   . ALA D 264 ? 0.8569 0.9216 1.0458 0.1178  0.1056  0.1686  265 ALA D N   
11310 C  CA  . ALA D 264 ? 0.8323 0.9010 1.0144 0.1164  0.0985  0.1564  265 ALA D CA  
11311 C  C   . ALA D 264 ? 0.7987 0.8776 0.9821 0.1101  0.1021  0.1553  265 ALA D C   
11312 O  O   . ALA D 264 ? 0.8197 0.9074 0.9989 0.1096  0.1101  0.1611  265 ALA D O   
11313 C  CB  . ALA D 264 ? 0.8770 0.9541 1.0394 0.1233  0.0968  0.1510  265 ALA D CB  
11314 N  N   . ARG D 265 ? 0.7048 0.7817 0.8930 0.1064  0.0957  0.1474  266 ARG D N   
11315 C  CA  . ARG D 265 ? 0.6682 0.7540 0.8579 0.1006  0.0981  0.1455  266 ARG D CA  
11316 C  C   . ARG D 265 ? 0.6140 0.7084 0.7907 0.1023  0.0940  0.1365  266 ARG D C   
11317 O  O   . ARG D 265 ? 0.6639 0.7543 0.8348 0.1074  0.0876  0.1307  266 ARG D O   
11318 C  CB  . ARG D 265 ? 0.6635 0.7404 0.8736 0.0943  0.0950  0.1460  266 ARG D CB  
11319 C  CG  . ARG D 265 ? 0.6862 0.7591 0.9127 0.0915  0.1022  0.1579  266 ARG D CG  
11320 C  CD  . ARG D 265 ? 0.6800 0.7486 0.9284 0.0843  0.1004  0.1591  266 ARG D CD  
11321 N  N   . PRO D 266 ? 0.5833 0.6897 0.7562 0.0989  0.0977  0.1358  267 PRO D N   
11322 C  CA  . PRO D 266 ? 0.5989 0.7156 0.7618 0.1006  0.0954  0.1300  267 PRO D CA  
11323 C  C   . PRO D 266 ? 0.6184 0.7311 0.7833 0.1007  0.0888  0.1235  267 PRO D C   
11324 O  O   . PRO D 266 ? 0.5887 0.6932 0.7645 0.0966  0.0860  0.1222  267 PRO D O   
11325 C  CB  . PRO D 266 ? 0.5327 0.6603 0.6955 0.0959  0.1001  0.1315  267 PRO D CB  
11326 C  CG  . PRO D 266 ? 0.5096 0.6309 0.6835 0.0911  0.1034  0.1356  267 PRO D CG  
11327 C  CD  . PRO D 266 ? 0.5663 0.6770 0.7449 0.0940  0.1042  0.1408  267 PRO D CD  
11328 N  N   . CYS D 267 ? 0.6923 0.8115 0.8471 0.1063  0.0866  0.1198  268 CYS D N   
11329 C  CA  A CYS D 267 ? 0.6834 0.8000 0.8358 0.1094  0.0809  0.1139  268 CYS D CA  
11330 C  CA  B CYS D 267 ? 0.6837 0.8006 0.8359 0.1094  0.0810  0.1139  268 CYS D CA  
11331 C  C   . CYS D 267 ? 0.6550 0.7770 0.8133 0.1028  0.0819  0.1131  268 CYS D C   
11332 O  O   . CYS D 267 ? 0.6581 0.7909 0.8183 0.0980  0.0870  0.1164  268 CYS D O   
11333 C  CB  A CYS D 267 ? 0.7021 0.8272 0.8417 0.1185  0.0806  0.1125  268 CYS D CB  
11334 C  CB  B CYS D 267 ? 0.6963 0.8226 0.8359 0.1181  0.0810  0.1127  268 CYS D CB  
11335 S  SG  A CYS D 267 ? 0.5130 0.6325 0.6445 0.1274  0.0793  0.1130  268 CYS D SG  
11336 S  SG  B CYS D 267 ? 0.9121 1.0351 1.0436 0.1268  0.0745  0.1060  268 CYS D SG  
11337 N  N   . PRO D 268 ? 0.6169 0.7308 0.7786 0.1032  0.0758  0.1082  269 PRO D N   
11338 C  CA  . PRO D 268 ? 0.6230 0.7413 0.7898 0.0981  0.0759  0.1071  269 PRO D CA  
11339 C  C   . PRO D 268 ? 0.5698 0.7037 0.7300 0.0991  0.0804  0.1092  269 PRO D C   
11340 O  O   . PRO D 268 ? 0.5249 0.6662 0.6913 0.0922  0.0844  0.1119  269 PRO D O   
11341 C  CB  . PRO D 268 ? 0.6213 0.7282 0.7873 0.1029  0.0666  0.1002  269 PRO D CB  
11342 C  CG  . PRO D 268 ? 0.6445 0.7371 0.8151 0.1051  0.0615  0.0987  269 PRO D CG  
11343 C  CD  . PRO D 268 ? 0.6373 0.7352 0.8005 0.1080  0.0672  0.1032  269 PRO D CD  
11344 N  N   . ASP D 269 ? 0.5415 0.6806 0.6907 0.1081  0.0797  0.1085  270 ASP D N   
11345 C  CA  . ASP D 269 ? 0.5412 0.6961 0.6878 0.1097  0.0843  0.1124  270 ASP D CA  
11346 C  C   . ASP D 269 ? 0.5087 0.6746 0.6604 0.1048  0.0896  0.1176  270 ASP D C   
11347 O  O   . ASP D 269 ? 0.4987 0.6758 0.6566 0.1006  0.0926  0.1209  270 ASP D O   
11348 C  CB  . ASP D 269 ? 0.5467 0.7054 0.6807 0.1223  0.0834  0.1120  270 ASP D CB  
11349 C  CG  . ASP D 269 ? 0.5724 0.7227 0.6991 0.1293  0.0774  0.1063  270 ASP D CG  
11350 O  OD1 . ASP D 269 ? 0.6097 0.7554 0.7431 0.1231  0.0750  0.1042  270 ASP D OD1 
11351 O  OD2 . ASP D 269 ? 0.5960 0.7440 0.7093 0.1419  0.0746  0.1037  270 ASP D OD2 
11352 N  N   . TYR D 270 ? 0.5182 0.6802 0.6676 0.1058  0.0900  0.1181  271 TYR D N   
11353 C  CA  . TYR D 270 ? 0.4905 0.6607 0.6432 0.1023  0.0934  0.1218  271 TYR D CA  
11354 C  C   . TYR D 270 ? 0.4210 0.5911 0.5819 0.0933  0.0947  0.1220  271 TYR D C   
11355 O  O   . TYR D 270 ? 0.4100 0.5902 0.5760 0.0898  0.0959  0.1236  271 TYR D O   
11356 C  CB  . TYR D 270 ? 0.3756 0.5389 0.5231 0.1060  0.0932  0.1221  271 TYR D CB  
11357 C  CG  . TYR D 270 ? 0.5340 0.7049 0.6818 0.1049  0.0956  0.1252  271 TYR D CG  
11358 C  CD1 . TYR D 270 ? 0.3645 0.5487 0.5175 0.1021  0.0963  0.1269  271 TYR D CD1 
11359 C  CD2 . TYR D 270 ? 0.3796 0.5437 0.5230 0.1073  0.0963  0.1265  271 TYR D CD2 
11360 C  CE1 . TYR D 270 ? 0.3640 0.5540 0.5172 0.1021  0.0963  0.1283  271 TYR D CE1 
11361 C  CE2 . TYR D 270 ? 0.3791 0.5497 0.5207 0.1079  0.0976  0.1288  271 TYR D CE2 
11362 C  CZ  . TYR D 270 ? 0.4059 0.5891 0.5519 0.1055  0.0969  0.1289  271 TYR D CZ  
11363 O  OH  . TYR D 270 ? 0.4252 0.6140 0.5692 0.1070  0.0960  0.1297  271 TYR D OH  
11364 N  N   . CYS D 271 ? 0.4242 0.5827 0.5878 0.0901  0.0940  0.1203  272 CYS D N   
11365 C  CA  . CYS D 271 ? 0.4138 0.5713 0.5847 0.0830  0.0958  0.1207  272 CYS D CA  
11366 C  C   . CYS D 271 ? 0.4166 0.5813 0.5925 0.0793  0.0953  0.1198  272 CYS D C   
11367 O  O   . CYS D 271 ? 0.4150 0.5851 0.5952 0.0749  0.0967  0.1204  272 CYS D O   
11368 C  CB  . CYS D 271 ? 0.3614 0.5061 0.5377 0.0809  0.0950  0.1202  272 CYS D CB  
11369 S  SG  . CYS D 271 ? 0.6856 0.8293 0.8710 0.0739  0.0990  0.1224  272 CYS D SG  
11370 N  N   . ARG D 272 ? 0.4570 0.6211 0.6316 0.0820  0.0929  0.1182  273 ARG D N   
11371 C  CA  . ARG D 272 ? 0.4921 0.6626 0.6712 0.0795  0.0928  0.1185  273 ARG D CA  
11372 C  C   . ARG D 272 ? 0.4997 0.6839 0.6823 0.0789  0.0949  0.1223  273 ARG D C   
11373 O  O   . ARG D 272 ? 0.5458 0.7348 0.7365 0.0735  0.0953  0.1231  273 ARG D O   
11374 C  CB  . ARG D 272 ? 0.5500 0.7175 0.7239 0.0854  0.0898  0.1165  273 ARG D CB  
11375 C  CG  . ARG D 272 ? 0.6423 0.7958 0.8174 0.0848  0.0852  0.1118  273 ARG D CG  
11376 C  CD  . ARG D 272 ? 0.7349 0.8873 0.9101 0.0862  0.0819  0.1094  273 ARG D CD  
11377 N  NE  . ARG D 272 ? 0.8422 0.9964 1.0054 0.0970  0.0797  0.1084  273 ARG D NE  
11378 C  CZ  . ARG D 272 ? 0.9262 1.0884 1.0859 0.1010  0.0810  0.1107  273 ARG D CZ  
11379 N  NH1 . ARG D 272 ? 0.9660 1.1301 1.1127 0.1131  0.0798  0.1105  273 ARG D NH1 
11380 N  NH2 . ARG D 272 ? 0.9404 1.1086 1.1093 0.0940  0.0837  0.1137  273 ARG D NH2 
11381 N  N   . ASN D 273 ? 0.4572 0.6478 0.6356 0.0845  0.0957  0.1247  274 ASN D N   
11382 C  CA  . ASN D 273 ? 0.5039 0.7083 0.6899 0.0837  0.0968  0.1290  274 ASN D CA  
11383 C  C   . ASN D 273 ? 0.3321 0.5372 0.5235 0.0781  0.0955  0.1277  274 ASN D C   
11384 O  O   . ASN D 273 ? 0.3432 0.5561 0.5455 0.0740  0.0942  0.1292  274 ASN D O   
11385 C  CB  . ASN D 273 ? 0.4238 0.6353 0.6052 0.0916  0.0981  0.1324  274 ASN D CB  
11386 C  CG  . ASN D 273 ? 0.4750 0.6938 0.6551 0.0981  0.1004  0.1366  274 ASN D CG  
11387 O  OD1 . ASN D 273 ? 0.4768 0.7000 0.6638 0.0955  0.1015  0.1392  274 ASN D OD1 
11388 N  ND2 . ASN D 273 ? 0.4930 0.7134 0.6636 0.1078  0.1016  0.1378  274 ASN D ND2 
11389 N  N   . VAL D 274 ? 0.3366 0.5334 0.5207 0.0788  0.0954  0.1251  275 VAL D N   
11390 C  CA  . VAL D 274 ? 0.4457 0.6422 0.6309 0.0761  0.0942  0.1234  275 VAL D CA  
11391 C  C   . VAL D 274 ? 0.4123 0.6065 0.6037 0.0702  0.0936  0.1212  275 VAL D C   
11392 O  O   . VAL D 274 ? 0.4113 0.6107 0.6093 0.0677  0.0907  0.1201  275 VAL D O   
11393 C  CB  . VAL D 274 ? 0.4320 0.6197 0.6073 0.0793  0.0959  0.1226  275 VAL D CB  
11394 C  CG1 . VAL D 274 ? 0.4150 0.6017 0.5882 0.0785  0.0953  0.1209  275 VAL D CG1 
11395 C  CG2 . VAL D 274 ? 0.4238 0.6138 0.5930 0.0854  0.0958  0.1245  275 VAL D CG2 
11396 N  N   . LEU D 275 ? 0.4193 0.6054 0.6097 0.0683  0.0955  0.1203  276 LEU D N   
11397 C  CA  . LEU D 275 ? 0.3917 0.5753 0.5877 0.0634  0.0955  0.1184  276 LEU D CA  
11398 C  C   . LEU D 275 ? 0.3963 0.5868 0.6021 0.0599  0.0936  0.1192  276 LEU D C   
11399 O  O   . LEU D 275 ? 0.3294 0.5206 0.5413 0.0561  0.0920  0.1174  276 LEU D O   
11400 C  CB  . LEU D 275 ? 0.4374 0.6114 0.6328 0.0622  0.0977  0.1181  276 LEU D CB  
11401 C  CG  . LEU D 275 ? 0.4900 0.6569 0.6801 0.0648  0.1006  0.1193  276 LEU D CG  
11402 C  CD1 . LEU D 275 ? 0.5321 0.6909 0.7280 0.0623  0.1025  0.1200  276 LEU D CD1 
11403 C  CD2 . LEU D 275 ? 0.4945 0.6639 0.6797 0.0668  0.1018  0.1191  276 LEU D CD2 
11404 N  N   . LYS D 276 ? 0.3862 0.5819 0.5934 0.0620  0.0939  0.1222  277 LYS D N   
11405 C  CA  . LYS D 276 ? 0.3374 0.5414 0.5551 0.0598  0.0932  0.1254  277 LYS D CA  
11406 C  C   . LYS D 276 ? 0.3849 0.5977 0.6128 0.0580  0.0904  0.1270  277 LYS D C   
11407 O  O   . LYS D 276 ? 0.3738 0.5907 0.6143 0.0538  0.0883  0.1282  277 LYS D O   
11408 C  CB  . LYS D 276 ? 0.3177 0.5263 0.5325 0.0652  0.0954  0.1297  277 LYS D CB  
11409 C  CG  . LYS D 276 ? 0.3201 0.5212 0.5293 0.0667  0.0956  0.1278  277 LYS D CG  
11410 C  CD  . LYS D 276 ? 0.3316 0.5389 0.5370 0.0739  0.0973  0.1323  277 LYS D CD  
11411 C  CE  . LYS D 276 ? 0.4007 0.5996 0.5988 0.0769  0.0956  0.1291  277 LYS D CE  
11412 N  NZ  . LYS D 276 ? 0.4935 0.6986 0.6849 0.0864  0.0973  0.1334  277 LYS D NZ  
11413 N  N   . GLY D 277 ? 0.3465 0.5617 0.5702 0.0614  0.0895  0.1268  278 GLY D N   
11414 C  CA  . GLY D 277 ? 0.3542 0.5767 0.5880 0.0602  0.0849  0.1270  278 GLY D CA  
11415 C  C   . GLY D 277 ? 0.4025 0.6187 0.6365 0.0572  0.0803  0.1206  278 GLY D C   
11416 O  O   . GLY D 277 ? 0.5099 0.7303 0.7568 0.0544  0.0744  0.1195  278 GLY D O   
11417 N  N   . CYS D 278 ? 0.3805 0.5868 0.6011 0.0586  0.0829  0.1168  279 CYS D N   
11418 C  CA  . CYS D 278 ? 0.4369 0.6373 0.6536 0.0586  0.0800  0.1112  279 CYS D CA  
11419 C  C   . CYS D 278 ? 0.4579 0.6552 0.6818 0.0539  0.0795  0.1094  279 CYS D C   
11420 O  O   . CYS D 278 ? 0.4759 0.6709 0.7017 0.0538  0.0747  0.1046  279 CYS D O   
11421 C  CB  . CYS D 278 ? 0.4822 0.6748 0.6830 0.0632  0.0845  0.1101  279 CYS D CB  
11422 S  SG  . CYS D 278 ? 0.5533 0.7477 0.7437 0.0700  0.0840  0.1110  279 CYS D SG  
11423 N  N   . LEU D 279 ? 0.4430 0.6396 0.6699 0.0511  0.0836  0.1127  280 LEU D N   
11424 C  CA  . LEU D 279 ? 0.3566 0.5495 0.5889 0.0472  0.0839  0.1113  280 LEU D CA  
11425 C  C   . LEU D 279 ? 0.3417 0.5408 0.5879 0.0434  0.0827  0.1155  280 LEU D C   
11426 O  O   . LEU D 279 ? 0.3633 0.5599 0.6123 0.0410  0.0845  0.1163  280 LEU D O   
11427 C  CB  . LEU D 279 ? 0.4011 0.5869 0.6258 0.0478  0.0892  0.1115  280 LEU D CB  
11428 C  CG  . LEU D 279 ? 0.4347 0.6147 0.6480 0.0518  0.0923  0.1102  280 LEU D CG  
11429 C  CD1 . LEU D 279 ? 0.4339 0.6077 0.6461 0.0512  0.0969  0.1120  280 LEU D CD1 
11430 C  CD2 . LEU D 279 ? 0.3289 0.5069 0.5390 0.0538  0.0905  0.1060  280 LEU D CD2 
11431 N  N   . ALA D 280 ? 0.3306 0.5383 0.5868 0.0432  0.0799  0.1190  281 ALA D N   
11432 C  CA  . ALA D 280 ? 0.3217 0.5374 0.5930 0.0406  0.0803  0.1258  281 ALA D CA  
11433 C  C   . ALA D 280 ? 0.3383 0.5521 0.6230 0.0355  0.0761  0.1243  281 ALA D C   
11434 O  O   . ALA D 280 ? 0.3867 0.6016 0.6778 0.0335  0.0786  0.1286  281 ALA D O   
11435 C  CB  . ALA D 280 ? 0.3033 0.5299 0.5852 0.0419  0.0788  0.1313  281 ALA D CB  
11436 N  N   . ASN D 281 ? 0.3066 0.5168 0.5947 0.0345  0.0693  0.1179  282 ASN D N   
11437 C  CA  . ASN D 281 ? 0.3436 0.5496 0.6428 0.0307  0.0639  0.1145  282 ASN D CA  
11438 C  C   . ASN D 281 ? 0.3894 0.5882 0.6798 0.0302  0.0685  0.1125  282 ASN D C   
11439 O  O   . ASN D 281 ? 0.4372 0.6360 0.7384 0.0267  0.0682  0.1151  282 ASN D O   
11440 C  CB  . ASN D 281 ? 0.3176 0.5185 0.6153 0.0326  0.0550  0.1054  282 ASN D CB  
11441 C  CG  . ASN D 281 ? 0.3523 0.5602 0.6664 0.0318  0.0470  0.1068  282 ASN D CG  
11442 O  OD1 . ASN D 281 ? 0.3358 0.5477 0.6732 0.0271  0.0416  0.1103  282 ASN D OD1 
11443 N  ND2 . ASN D 281 ? 0.4057 0.6154 0.7099 0.0362  0.0460  0.1047  282 ASN D ND2 
11444 N  N   . GLN D 282 ? 0.3963 0.5894 0.6690 0.0337  0.0727  0.1088  283 GLN D N   
11445 C  CA  . GLN D 282 ? 0.3359 0.5230 0.6024 0.0333  0.0772  0.1078  283 GLN D CA  
11446 C  C   . GLN D 282 ? 0.3234 0.5138 0.5938 0.0316  0.0811  0.1140  283 GLN D C   
11447 O  O   . GLN D 282 ? 0.3500 0.5375 0.6234 0.0297  0.0822  0.1142  283 GLN D O   
11448 C  CB  . GLN D 282 ? 0.3323 0.5143 0.5831 0.0374  0.0817  0.1052  283 GLN D CB  
11449 C  CG  . GLN D 282 ? 0.3737 0.5515 0.6164 0.0415  0.0793  0.0992  283 GLN D CG  
11450 C  CD  . GLN D 282 ? 0.4329 0.6140 0.6729 0.0445  0.0748  0.0978  283 GLN D CD  
11451 O  OE1 . GLN D 282 ? 0.4279 0.6155 0.6754 0.0425  0.0732  0.1016  283 GLN D OE1 
11452 N  NE2 . GLN D 282 ? 0.4384 0.6158 0.6673 0.0504  0.0729  0.0926  283 GLN D NE2 
11453 N  N   . ALA D 283 ? 0.2996 0.4962 0.5689 0.0336  0.0831  0.1190  284 ALA D N   
11454 C  CA  . ALA D 283 ? 0.4134 0.6134 0.6829 0.0348  0.0866  0.1248  284 ALA D CA  
11455 C  C   . ALA D 283 ? 0.3712 0.5768 0.6562 0.0321  0.0856  0.1306  284 ALA D C   
11456 O  O   . ALA D 283 ? 0.3290 0.5360 0.6138 0.0336  0.0882  0.1349  284 ALA D O   
11457 C  CB  . ALA D 283 ? 0.2988 0.5041 0.5616 0.0396  0.0890  0.1286  284 ALA D CB  
11458 N  N   . ASP D 284 ? 0.2948 0.5032 0.5938 0.0287  0.0811  0.1308  285 ASP D N   
11459 C  CA  . ASP D 284 ? 0.3834 0.5968 0.7014 0.0254  0.0796  0.1373  285 ASP D CA  
11460 C  C   . ASP D 284 ? 0.3724 0.5786 0.6922 0.0227  0.0787  0.1344  285 ASP D C   
11461 O  O   . ASP D 284 ? 0.2919 0.5014 0.6254 0.0207  0.0787  0.1408  285 ASP D O   
11462 C  CB  . ASP D 284 ? 0.3685 0.5855 0.7046 0.0220  0.0728  0.1374  285 ASP D CB  
11463 C  CG  . ASP D 284 ? 0.4273 0.6562 0.7729 0.0237  0.0746  0.1463  285 ASP D CG  
11464 O  OD1 . ASP D 284 ? 0.4371 0.6727 0.7778 0.0277  0.0820  0.1544  285 ASP D OD1 
11465 O  OD2 . ASP D 284 ? 0.4270 0.6587 0.7849 0.0219  0.0684  0.1449  285 ASP D OD2 
11466 N  N   . LEU D 285 ? 0.3825 0.5798 0.6898 0.0232  0.0784  0.1259  286 LEU D N   
11467 C  CA  . LEU D 285 ? 0.3651 0.5560 0.6737 0.0213  0.0778  0.1228  286 LEU D CA  
11468 C  C   . LEU D 285 ? 0.3734 0.5649 0.6777 0.0230  0.0821  0.1272  286 LEU D C   
11469 O  O   . LEU D 285 ? 0.3414 0.5297 0.6501 0.0215  0.0816  0.1270  286 LEU D O   
11470 C  CB  . LEU D 285 ? 0.3499 0.5327 0.6473 0.0225  0.0773  0.1139  286 LEU D CB  
11471 C  CG  . LEU D 285 ? 0.3571 0.5368 0.6551 0.0231  0.0719  0.1074  286 LEU D CG  
11472 C  CD1 . LEU D 285 ? 0.3067 0.4814 0.5886 0.0273  0.0747  0.1018  286 LEU D CD1 
11473 C  CD2 . LEU D 285 ? 0.3055 0.4810 0.6150 0.0208  0.0663  0.1043  286 LEU D CD2 
11474 N  N   . ASP D 286 ? 0.2923 0.4876 0.5874 0.0270  0.0856  0.1306  287 ASP D N   
11475 C  CA  . ASP D 286 ? 0.3793 0.5740 0.6660 0.0310  0.0881  0.1327  287 ASP D CA  
11476 C  C   . ASP D 286 ? 0.3612 0.5575 0.6558 0.0308  0.0883  0.1379  287 ASP D C   
11477 O  O   . ASP D 286 ? 0.4210 0.6118 0.7131 0.0307  0.0873  0.1346  287 ASP D O   
11478 C  CB  . ASP D 286 ? 0.4459 0.6463 0.7239 0.0370  0.0908  0.1371  287 ASP D CB  
11479 C  CG  . ASP D 286 ? 0.4594 0.6565 0.7245 0.0431  0.0913  0.1361  287 ASP D CG  
11480 O  OD1 . ASP D 286 ? 0.4807 0.6694 0.7407 0.0421  0.0891  0.1292  287 ASP D OD1 
11481 O  OD2 . ASP D 286 ? 0.4590 0.6620 0.7198 0.0497  0.0935  0.1425  287 ASP D OD2 
11482 N  N   . ALA D 287 ? 0.3489 0.5536 0.6548 0.0310  0.0897  0.1469  288 ALA D N   
11483 C  CA  . ALA D 287 ? 0.3251 0.5329 0.6388 0.0322  0.0913  0.1547  288 ALA D CA  
11484 C  C   . ALA D 287 ? 0.3004 0.5012 0.6224 0.0271  0.0878  0.1505  288 ALA D C   
11485 O  O   . ALA D 287 ? 0.3608 0.5585 0.6784 0.0293  0.0881  0.1504  288 ALA D O   
11486 C  CB  . ALA D 287 ? 0.3057 0.5244 0.6356 0.0322  0.0938  0.1668  288 ALA D CB  
11487 N  N   . GLU D 288 ? 0.2924 0.4903 0.6259 0.0213  0.0839  0.1465  289 GLU D N   
11488 C  CA  . GLU D 288 ? 0.2924 0.4835 0.6345 0.0174  0.0802  0.1424  289 GLU D CA  
11489 C  C   . GLU D 288 ? 0.2919 0.4749 0.6213 0.0180  0.0798  0.1328  289 GLU D C   
11490 O  O   . GLU D 288 ? 0.3508 0.5293 0.6833 0.0171  0.0787  0.1309  289 GLU D O   
11491 C  CB  . GLU D 288 ? 0.2933 0.4826 0.6502 0.0127  0.0746  0.1397  289 GLU D CB  
11492 C  CG  . GLU D 288 ? 0.3185 0.5158 0.6958 0.0107  0.0739  0.1505  289 GLU D CG  
11493 C  CD  . GLU D 288 ? 0.4724 0.6736 0.8594 0.0115  0.0774  0.1616  289 GLU D CD  
11494 O  OE1 . GLU D 288 ? 0.5328 0.7276 0.9190 0.0110  0.0762  0.1585  289 GLU D OE1 
11495 O  OE2 . GLU D 288 ? 0.5425 0.7539 0.9377 0.0137  0.0819  0.1741  289 GLU D OE2 
11496 N  N   . TRP D 289 ? 0.4086 0.5902 0.7256 0.0197  0.0810  0.1277  290 TRP D N   
11497 C  CA  . TRP D 289 ? 0.4026 0.5781 0.7102 0.0206  0.0818  0.1211  290 TRP D CA  
11498 C  C   . TRP D 289 ? 0.2919 0.4671 0.5963 0.0232  0.0825  0.1233  290 TRP D C   
11499 O  O   . TRP D 289 ? 0.2919 0.4628 0.5986 0.0225  0.0816  0.1204  290 TRP D O   
11500 C  CB  . TRP D 289 ? 0.2916 0.4666 0.5884 0.0224  0.0834  0.1177  290 TRP D CB  
11501 C  CG  . TRP D 289 ? 0.2920 0.4619 0.5828 0.0233  0.0849  0.1131  290 TRP D CG  
11502 C  CD1 . TRP D 289 ? 0.2928 0.4612 0.5776 0.0256  0.0855  0.1131  290 TRP D CD1 
11503 C  CD2 . TRP D 289 ? 0.2933 0.4589 0.5848 0.0227  0.0857  0.1084  290 TRP D CD2 
11504 N  NE1 . TRP D 289 ? 0.2932 0.4572 0.5787 0.0252  0.0867  0.1097  290 TRP D NE1 
11505 C  CE2 . TRP D 289 ? 0.2935 0.4565 0.5823 0.0239  0.0879  0.1075  290 TRP D CE2 
11506 C  CE3 . TRP D 289 ? 0.2959 0.4595 0.5904 0.0223  0.0845  0.1050  290 TRP D CE3 
11507 C  CZ2 . TRP D 289 ? 0.2953 0.4555 0.5856 0.0245  0.0907  0.1053  290 TRP D CZ2 
11508 C  CZ3 . TRP D 289 ? 0.2991 0.4592 0.5910 0.0244  0.0871  0.1015  290 TRP D CZ3 
11509 C  CH2 . TRP D 289 ? 0.3484 0.5077 0.6388 0.0253  0.0911  0.1026  290 TRP D CH2 
11510 N  N   . ARG D 290 ? 0.2940 0.4738 0.5926 0.0273  0.0839  0.1285  291 ARG D N   
11511 C  CA  . ARG D 290 ? 0.3970 0.5764 0.6899 0.0320  0.0833  0.1303  291 ARG D CA  
11512 C  C   . ARG D 290 ? 0.3943 0.5743 0.6959 0.0314  0.0827  0.1345  291 ARG D C   
11513 O  O   . ARG D 290 ? 0.4770 0.6534 0.7767 0.0333  0.0806  0.1323  291 ARG D O   
11514 C  CB  . ARG D 290 ? 0.3028 0.4876 0.5856 0.0389  0.0850  0.1353  291 ARG D CB  
11515 C  CG  . ARG D 290 ? 0.3041 0.4863 0.5762 0.0410  0.0845  0.1303  291 ARG D CG  
11516 C  CD  . ARG D 290 ? 0.4167 0.6048 0.6788 0.0487  0.0865  0.1354  291 ARG D CD  
11517 N  NE  . ARG D 290 ? 0.5136 0.6991 0.7672 0.0502  0.0860  0.1308  291 ARG D NE  
11518 C  CZ  . ARG D 290 ? 0.5227 0.7017 0.7659 0.0549  0.0823  0.1252  291 ARG D CZ  
11519 N  NH1 . ARG D 290 ? 0.5192 0.6939 0.7589 0.0589  0.0781  0.1227  291 ARG D NH1 
11520 N  NH2 . ARG D 290 ? 0.5515 0.7280 0.7889 0.0558  0.0819  0.1218  291 ARG D NH2 
11521 N  N   . ASN D 291 ? 0.3806 0.5650 0.6936 0.0289  0.0839  0.1409  292 ASN D N   
11522 C  CA  . ASN D 291 ? 0.3543 0.5389 0.6781 0.0280  0.0834  0.1459  292 ASN D CA  
11523 C  C   . ASN D 291 ? 0.3429 0.5198 0.6715 0.0240  0.0803  0.1384  292 ASN D C   
11524 O  O   . ASN D 291 ? 0.3354 0.5103 0.6655 0.0255  0.0792  0.1391  292 ASN D O   
11525 C  CB  . ASN D 291 ? 0.2987 0.4888 0.6385 0.0250  0.0844  0.1544  292 ASN D CB  
11526 C  CG  . ASN D 291 ? 0.3911 0.5911 0.7292 0.0304  0.0891  0.1656  292 ASN D CG  
11527 O  OD1 . ASN D 291 ? 0.4035 0.6059 0.7285 0.0381  0.0916  0.1689  292 ASN D OD1 
11528 N  ND2 . ASN D 291 ? 0.3006 0.5064 0.6523 0.0274  0.0900  0.1715  292 ASN D ND2 
11529 N  N   . LEU D 292 ? 0.3367 0.5099 0.6670 0.0201  0.0790  0.1313  293 LEU D N   
11530 C  CA  . LEU D 292 ? 0.3474 0.5141 0.6805 0.0181  0.0772  0.1242  293 LEU D CA  
11531 C  C   . LEU D 292 ? 0.3630 0.5275 0.6894 0.0204  0.0776  0.1208  293 LEU D C   
11532 O  O   . LEU D 292 ? 0.3658 0.5279 0.6967 0.0207  0.0762  0.1204  293 LEU D O   
11533 C  CB  . LEU D 292 ? 0.3500 0.5139 0.6818 0.0163  0.0766  0.1176  293 LEU D CB  
11534 C  CG  . LEU D 292 ? 0.3280 0.4863 0.6601 0.0166  0.0762  0.1108  293 LEU D CG  
11535 C  CD1 . LEU D 292 ? 0.2977 0.4526 0.6408 0.0153  0.0729  0.1107  293 LEU D CD1 
11536 C  CD2 . LEU D 292 ? 0.2974 0.4537 0.6231 0.0177  0.0768  0.1049  293 LEU D CD2 
11537 N  N   . LEU D 293 ? 0.3974 0.5622 0.7146 0.0221  0.0787  0.1185  294 LEU D N   
11538 C  CA  . LEU D 293 ? 0.3802 0.5423 0.6947 0.0237  0.0776  0.1151  294 LEU D CA  
11539 C  C   . LEU D 293 ? 0.3462 0.5086 0.6600 0.0273  0.0746  0.1177  294 LEU D C   
11540 O  O   . LEU D 293 ? 0.2977 0.4575 0.6164 0.0275  0.0722  0.1151  294 LEU D O   
11541 C  CB  . LEU D 293 ? 0.2939 0.4558 0.6002 0.0252  0.0782  0.1132  294 LEU D CB  
11542 C  CG  . LEU D 293 ? 0.3377 0.4974 0.6453 0.0231  0.0809  0.1094  294 LEU D CG  
11543 C  CD1 . LEU D 293 ? 0.3602 0.5209 0.6678 0.0215  0.0831  0.1090  294 LEU D CD1 
11544 C  CD2 . LEU D 293 ? 0.3128 0.4715 0.6141 0.0247  0.0810  0.1085  294 LEU D CD2 
11545 N  N   . ASP D 294 ? 0.3141 0.4804 0.6220 0.0311  0.0749  0.1233  295 ASP D N   
11546 C  CA  . ASP D 294 ? 0.4527 0.6199 0.7569 0.0367  0.0725  0.1267  295 ASP D CA  
11547 C  C   . ASP D 294 ? 0.3875 0.5537 0.7022 0.0347  0.0720  0.1289  295 ASP D C   
11548 O  O   . ASP D 294 ? 0.3533 0.5175 0.6676 0.0379  0.0685  0.1278  295 ASP D O   
11549 C  CB  . ASP D 294 ? 0.5302 0.7035 0.8263 0.0426  0.0751  0.1346  295 ASP D CB  
11550 C  CG  . ASP D 294 ? 0.6507 0.8236 0.9321 0.0490  0.0733  0.1318  295 ASP D CG  
11551 O  OD1 . ASP D 294 ? 0.6951 0.8622 0.9733 0.0502  0.0682  0.1243  295 ASP D OD1 
11552 O  OD2 . ASP D 294 ? 0.7034 0.8818 0.9780 0.0532  0.0768  0.1373  295 ASP D OD2 
11553 N  N   . SER D 295 ? 0.4162 0.5832 0.7407 0.0298  0.0743  0.1314  296 SER D N   
11554 C  CA  . SER D 295 ? 0.3028 0.4678 0.6383 0.0278  0.0734  0.1332  296 SER D CA  
11555 C  C   . SER D 295 ? 0.3008 0.4608 0.6403 0.0260  0.0712  0.1256  296 SER D C   
11556 O  O   . SER D 295 ? 0.3028 0.4611 0.6479 0.0269  0.0694  0.1263  296 SER D O   
11557 C  CB  . SER D 295 ? 0.3905 0.5558 0.7372 0.0232  0.0744  0.1361  296 SER D CB  
11558 O  OG  . SER D 295 ? 0.4666 0.6294 0.8130 0.0197  0.0743  0.1291  296 SER D OG  
11559 N  N   . MET D 296 ? 0.2975 0.4559 0.6349 0.0240  0.0721  0.1195  297 MET D N   
11560 C  CA  . MET D 296 ? 0.3468 0.5023 0.6896 0.0231  0.0716  0.1141  297 MET D CA  
11561 C  C   . MET D 296 ? 0.3876 0.5429 0.7298 0.0262  0.0678  0.1131  297 MET D C   
11562 O  O   . MET D 296 ? 0.2994 0.4536 0.6490 0.0268  0.0655  0.1122  297 MET D O   
11563 C  CB  . MET D 296 ? 0.2936 0.4485 0.6349 0.0214  0.0748  0.1100  297 MET D CB  
11564 C  CG  . MET D 296 ? 0.2938 0.4478 0.6354 0.0197  0.0766  0.1088  297 MET D CG  
11565 S  SD  . MET D 296 ? 0.5782 0.7313 0.9159 0.0203  0.0808  0.1041  297 MET D SD  
11566 C  CE  . MET D 296 ? 0.4737 0.6293 0.8017 0.0201  0.0817  0.1057  297 MET D CE  
11567 N  N   . VAL D 297 ? 0.3003 0.4562 0.6340 0.0286  0.0662  0.1126  298 VAL D N   
11568 C  CA  . VAL D 297 ? 0.4313 0.5856 0.7634 0.0327  0.0601  0.1103  298 VAL D CA  
11569 C  C   . VAL D 297 ? 0.4650 0.6197 0.7957 0.0372  0.0567  0.1134  298 VAL D C   
11570 O  O   . VAL D 297 ? 0.4319 0.5847 0.7664 0.0398  0.0509  0.1107  298 VAL D O   
11571 C  CB  . VAL D 297 ? 0.3714 0.5253 0.6917 0.0365  0.0578  0.1093  298 VAL D CB  
11572 C  CG1 . VAL D 297 ? 0.3502 0.5009 0.6677 0.0423  0.0490  0.1055  298 VAL D CG1 
11573 C  CG2 . VAL D 297 ? 0.3049 0.4580 0.6274 0.0323  0.0610  0.1067  298 VAL D CG2 
11574 N  N   . LEU D 298 ? 0.4753 0.6328 0.8023 0.0381  0.0602  0.1197  299 LEU D N   
11575 C  CA  . LEU D 298 ? 0.4774 0.6358 0.8037 0.0426  0.0586  0.1249  299 LEU D CA  
11576 C  C   . LEU D 298 ? 0.4494 0.6057 0.7890 0.0391  0.0583  0.1240  299 LEU D C   
11577 O  O   . LEU D 298 ? 0.3983 0.5537 0.7392 0.0430  0.0542  0.1244  299 LEU D O   
11578 C  CB  . LEU D 298 ? 0.5746 0.7374 0.8970 0.0444  0.0635  0.1342  299 LEU D CB  
11579 C  CG  . LEU D 298 ? 0.6800 0.8457 0.9919 0.0542  0.0624  0.1411  299 LEU D CG  
11580 C  CD1 . LEU D 298 ? 0.6853 0.8503 0.9812 0.0621  0.0580  0.1365  299 LEU D CD1 
11581 C  CD2 . LEU D 298 ? 0.7672 0.9389 1.0807 0.0554  0.0689  0.1530  299 LEU D CD2 
11582 N  N   . ILE D 299 ? 0.3573 0.5126 0.7058 0.0329  0.0619  0.1224  300 ILE D N   
11583 C  CA  . ILE D 299 ? 0.3654 0.5182 0.7253 0.0307  0.0617  0.1212  300 ILE D CA  
11584 C  C   . ILE D 299 ? 0.3665 0.5184 0.7322 0.0312  0.0587  0.1157  300 ILE D C   
11585 O  O   . ILE D 299 ? 0.3742 0.5250 0.7488 0.0315  0.0575  0.1152  300 ILE D O   
11586 C  CB  . ILE D 299 ? 0.3035 0.4544 0.6694 0.0260  0.0653  0.1193  300 ILE D CB  
11587 C  CG1 . ILE D 299 ? 0.3621 0.5097 0.7380 0.0256  0.0643  0.1199  300 ILE D CG1 
11588 C  CG2 . ILE D 299 ? 0.2998 0.4503 0.6663 0.0242  0.0674  0.1130  300 ILE D CG2 
11589 C  CD1 . ILE D 299 ? 0.3576 0.5054 0.7363 0.0267  0.0633  0.1279  300 ILE D CD1 
11590 N  N   . THR D 300 ? 0.3055 0.4580 0.6685 0.0314  0.0573  0.1122  301 THR D N   
11591 C  CA  . THR D 300 ? 0.3675 0.5197 0.7403 0.0318  0.0533  0.1082  301 THR D CA  
11592 C  C   . THR D 300 ? 0.3435 0.4950 0.7162 0.0370  0.0458  0.1084  301 THR D C   
11593 O  O   . THR D 300 ? 0.3406 0.4921 0.7250 0.0373  0.0415  0.1057  301 THR D O   
11594 C  CB  . THR D 300 ? 0.3518 0.5040 0.7245 0.0309  0.0519  0.1051  301 THR D CB  
11595 O  OG1 . THR D 300 ? 0.4828 0.6339 0.8416 0.0350  0.0477  0.1051  301 THR D OG1 
11596 C  CG2 . THR D 300 ? 0.3939 0.5471 0.7670 0.0268  0.0595  0.1051  301 THR D CG2 
11597 N  N   . ASP D 301 ? 0.3749 0.5264 0.7349 0.0418  0.0443  0.1123  302 ASP D N   
11598 C  CA  . ASP D 301 ? 0.3806 0.5315 0.7367 0.0489  0.0373  0.1131  302 ASP D CA  
11599 C  C   . ASP D 301 ? 0.3839 0.5346 0.7515 0.0482  0.0372  0.1147  302 ASP D C   
11600 O  O   . ASP D 301 ? 0.3501 0.5001 0.7203 0.0528  0.0303  0.1130  302 ASP D O   
11601 C  CB  . ASP D 301 ? 0.4928 0.6451 0.8321 0.0558  0.0384  0.1195  302 ASP D CB  
11602 C  CG  . ASP D 301 ? 0.6351 0.7870 0.9601 0.0609  0.0351  0.1168  302 ASP D CG  
11603 O  OD1 . ASP D 301 ? 0.6445 0.7935 0.9718 0.0618  0.0276  0.1092  302 ASP D OD1 
11604 O  OD2 . ASP D 301 ? 0.6467 0.8014 0.9596 0.0643  0.0397  0.1226  302 ASP D OD2 
11605 N  N   . LYS D 302 ? 0.3911 0.5418 0.7654 0.0430  0.0440  0.1172  303 LYS D N   
11606 C  CA  . LYS D 302 ? 0.3874 0.5370 0.7718 0.0428  0.0442  0.1187  303 LYS D CA  
11607 C  C   . LYS D 302 ? 0.3736 0.5235 0.7727 0.0396  0.0445  0.1135  303 LYS D C   
11608 O  O   . LYS D 302 ? 0.3900 0.5390 0.7979 0.0389  0.0465  0.1139  303 LYS D O   
11609 C  CB  . LYS D 302 ? 0.3207 0.4688 0.7059 0.0401  0.0497  0.1238  303 LYS D CB  
11610 C  CG  . LYS D 302 ? 0.3743 0.5238 0.7493 0.0434  0.0510  0.1318  303 LYS D CG  
11611 C  CD  . LYS D 302 ? 0.4545 0.6052 0.8214 0.0518  0.0461  0.1352  303 LYS D CD  
11612 C  CE  . LYS D 302 ? 0.4823 0.6357 0.8403 0.0567  0.0494  0.1458  303 LYS D CE  
11613 N  NZ  . LYS D 302 ? 0.5234 0.6755 0.8931 0.0537  0.0532  0.1535  303 LYS D NZ  
11614 N  N   . PHE D 303 ? 0.3950 0.5466 0.7977 0.0383  0.0429  0.1094  304 PHE D N   
11615 C  CA  . PHE D 303 ? 0.3351 0.4890 0.7545 0.0361  0.0440  0.1066  304 PHE D CA  
11616 C  C   . PHE D 303 ? 0.3218 0.4767 0.7516 0.0394  0.0357  0.1051  304 PHE D C   
11617 O  O   . PHE D 303 ? 0.3154 0.4730 0.7614 0.0388  0.0364  0.1046  304 PHE D O   
11618 C  CB  . PHE D 303 ? 0.3666 0.5223 0.7891 0.0329  0.0467  0.1046  304 PHE D CB  
11619 C  CG  . PHE D 303 ? 0.3977 0.5531 0.8126 0.0301  0.0552  0.1054  304 PHE D CG  
11620 C  CD1 . PHE D 303 ? 0.4322 0.5851 0.8396 0.0301  0.0585  0.1069  304 PHE D CD1 
11621 C  CD2 . PHE D 303 ? 0.4595 0.6165 0.8760 0.0278  0.0590  0.1047  304 PHE D CD2 
11622 C  CE1 . PHE D 303 ? 0.4291 0.5811 0.8302 0.0282  0.0643  0.1064  304 PHE D CE1 
11623 C  CE2 . PHE D 303 ? 0.4591 0.6157 0.8673 0.0264  0.0660  0.1050  304 PHE D CE2 
11624 C  CZ  . PHE D 303 ? 0.4496 0.6035 0.8497 0.0267  0.0680  0.1052  304 PHE D CZ  
11625 N  N   . TRP D 304 ? 0.3470 0.5001 0.7671 0.0441  0.0275  0.1044  305 TRP D N   
11626 C  CA  . TRP D 304 ? 0.3991 0.5523 0.8273 0.0484  0.0169  0.1016  305 TRP D CA  
11627 C  C   . TRP D 304 ? 0.4817 0.6338 0.9045 0.0539  0.0143  0.1046  305 TRP D C   
11628 O  O   . TRP D 304 ? 0.4387 0.5895 0.8510 0.0544  0.0202  0.1096  305 TRP D O   
11629 C  CB  . TRP D 304 ? 0.4329 0.5837 0.8526 0.0524  0.0073  0.0974  305 TRP D CB  
11630 C  CG  . TRP D 304 ? 0.5147 0.6650 0.9306 0.0482  0.0114  0.0964  305 TRP D CG  
11631 C  CD1 . TRP D 304 ? 0.5314 0.6799 0.9275 0.0502  0.0140  0.0975  305 TRP D CD1 
11632 C  CD2 . TRP D 304 ? 0.5473 0.6997 0.9805 0.0420  0.0143  0.0950  305 TRP D CD2 
11633 N  NE1 . TRP D 304 ? 0.5614 0.7099 0.9605 0.0453  0.0174  0.0960  305 TRP D NE1 
11634 C  CE2 . TRP D 304 ? 0.5906 0.7414 1.0122 0.0403  0.0178  0.0948  305 TRP D CE2 
11635 C  CE3 . TRP D 304 ? 0.6066 0.7628 1.0649 0.0382  0.0149  0.0952  305 TRP D CE3 
11636 C  CZ2 . TRP D 304 ? 0.6342 0.7864 1.0675 0.0351  0.0217  0.0947  305 TRP D CZ2 
11637 C  CZ3 . TRP D 304 ? 0.6414 0.7999 1.1124 0.0332  0.0196  0.0961  305 TRP D CZ3 
11638 C  CH2 . TRP D 304 ? 0.6177 0.7738 1.0757 0.0317  0.0228  0.0958  305 TRP D CH2 
11639 N  N   . GLY D 305 ? 0.4915 0.6439 0.9231 0.0581  0.0048  0.1020  306 GLY D N   
11640 C  CA  . GLY D 305 ? 0.5723 0.7237 0.9992 0.0644  0.0014  0.1049  306 GLY D CA  
11641 C  C   . GLY D 305 ? 0.5955 0.7488 1.0390 0.0615  0.0058  0.1067  306 GLY D C   
11642 O  O   . GLY D 305 ? 0.6116 0.7674 1.0680 0.0554  0.0128  0.1061  306 GLY D O   
11643 N  N   . THR D 306 ? 0.6773 0.8296 1.1195 0.0672  0.0018  0.1092  307 THR D N   
11644 C  CA  . THR D 306 ? 0.6934 0.8468 1.1502 0.0660  0.0052  0.1109  307 THR D CA  
11645 C  C   . THR D 306 ? 0.6734 0.8244 1.1268 0.0617  0.0164  0.1149  307 THR D C   
11646 O  O   . THR D 306 ? 0.6599 0.8115 1.1256 0.0593  0.0212  0.1145  307 THR D O   
11647 C  CB  . THR D 306 ? 0.7560 0.9081 1.2104 0.0739  -0.0021 0.1131  307 THR D CB  
11648 O  OG1 . THR D 306 ? 0.7728 0.9214 1.2084 0.0780  0.0008  0.1198  307 THR D OG1 
11649 C  CG2 . THR D 306 ? 0.7773 0.9306 1.2330 0.0797  -0.0157 0.1078  307 THR D CG2 
11650 N  N   . SER D 307 ? 0.6258 0.7741 1.0632 0.0615  0.0197  0.1186  308 SER D N   
11651 C  CA  . SER D 307 ? 0.5817 0.7269 1.0171 0.0573  0.0282  0.1220  308 SER D CA  
11652 C  C   . SER D 307 ? 0.4697 0.6161 0.9045 0.0513  0.0337  0.1184  308 SER D C   
11653 O  O   . SER D 307 ? 0.4596 0.6033 0.8922 0.0479  0.0396  0.1196  308 SER D O   
11654 C  CB  . SER D 307 ? 0.6159 0.7587 1.0384 0.0603  0.0293  0.1299  308 SER D CB  
11655 O  OG  . SER D 307 ? 0.6185 0.7574 1.0449 0.0565  0.0351  0.1336  308 SER D OG  
11656 N  N   . GLY D 308 ? 0.4742 0.6242 0.9119 0.0505  0.0310  0.1141  309 GLY D N   
11657 C  CA  . GLY D 308 ? 0.4407 0.5920 0.8771 0.0457  0.0358  0.1115  309 GLY D CA  
11658 C  C   . GLY D 308 ? 0.4138 0.5659 0.8595 0.0424  0.0434  0.1099  309 GLY D C   
11659 O  O   . GLY D 308 ? 0.4173 0.5695 0.8727 0.0440  0.0445  0.1098  309 GLY D O   
11660 N  N   . VAL D 309 ? 0.4804 0.6332 0.9217 0.0391  0.0486  0.1086  310 VAL D N   
11661 C  CA  . VAL D 309 ? 0.4829 0.6363 0.9286 0.0380  0.0562  0.1069  310 VAL D CA  
11662 C  C   . VAL D 309 ? 0.4386 0.5977 0.9013 0.0395  0.0581  0.1063  310 VAL D C   
11663 O  O   . VAL D 309 ? 0.4728 0.6321 0.9418 0.0423  0.0616  0.1060  310 VAL D O   
11664 C  CB  . VAL D 309 ? 0.4136 0.5672 0.8503 0.0351  0.0609  0.1060  310 VAL D CB  
11665 C  CG1 . VAL D 309 ? 0.3533 0.5093 0.7947 0.0362  0.0686  0.1045  310 VAL D CG1 
11666 C  CG2 . VAL D 309 ? 0.4383 0.5870 0.8615 0.0338  0.0607  0.1071  310 VAL D CG2 
11667 N  N   . GLU D 310 ? 0.4504 0.6141 0.9222 0.0381  0.0553  0.1066  311 GLU D N   
11668 C  CA  . GLU D 310 ? 0.5033 0.6740 0.9962 0.0389  0.0572  0.1078  311 GLU D CA  
11669 C  C   . GLU D 310 ? 0.4637 0.6356 0.9679 0.0421  0.0528  0.1081  311 GLU D C   
11670 O  O   . GLU D 310 ? 0.5026 0.6795 1.0212 0.0445  0.0577  0.1097  311 GLU D O   
11671 C  CB  . GLU D 310 ? 0.5754 0.7495 1.0791 0.0361  0.0525  0.1081  311 GLU D CB  
11672 C  CG  . GLU D 310 ? 0.6846 0.8665 1.2082 0.0352  0.0598  0.1118  311 GLU D CG  
11673 C  CD  . GLU D 310 ? 0.7854 0.9700 1.3265 0.0321  0.0527  0.1125  311 GLU D CD  
11674 O  OE1 . GLU D 310 ? 0.8137 0.9938 1.3513 0.0319  0.0405  0.1085  311 GLU D OE1 
11675 O  OE2 . GLU D 310 ? 0.8042 0.9952 1.3629 0.0306  0.0590  0.1172  311 GLU D OE2 
11676 N  N   . SER D 311 ? 0.4238 0.5914 0.9209 0.0433  0.0439  0.1071  312 SER D N   
11677 C  CA  . SER D 311 ? 0.4374 0.6057 0.9439 0.0469  0.0383  0.1074  312 SER D CA  
11678 C  C   . SER D 311 ? 0.4239 0.5893 0.9278 0.0495  0.0439  0.1082  312 SER D C   
11679 O  O   . SER D 311 ? 0.4403 0.6088 0.9578 0.0526  0.0438  0.1088  312 SER D O   
11680 C  CB  . SER D 311 ? 0.4493 0.6135 0.9451 0.0493  0.0277  0.1068  312 SER D CB  
11681 O  OG  . SER D 311 ? 0.4916 0.6572 0.9979 0.0533  0.0210  0.1068  312 SER D OG  
11682 N  N   . VAL D 312 ? 0.4319 0.5913 0.9198 0.0486  0.0479  0.1081  313 VAL D N   
11683 C  CA  . VAL D 312 ? 0.4389 0.5931 0.9243 0.0512  0.0508  0.1079  313 VAL D CA  
11684 C  C   . VAL D 312 ? 0.4090 0.5649 0.8979 0.0533  0.0594  0.1057  313 VAL D C   
11685 O  O   . VAL D 312 ? 0.3870 0.5433 0.8838 0.0579  0.0613  0.1051  313 VAL D O   
11686 C  CB  . VAL D 312 ? 0.4068 0.5530 0.8770 0.0495  0.0498  0.1091  313 VAL D CB  
11687 C  CG1 . VAL D 312 ? 0.3620 0.5014 0.8320 0.0517  0.0520  0.1078  313 VAL D CG1 
11688 C  CG2 . VAL D 312 ? 0.4413 0.5862 0.9070 0.0505  0.0427  0.1129  313 VAL D CG2 
11689 N  N   . ILE D 313 ? 0.3416 0.4984 0.8233 0.0512  0.0646  0.1047  314 ILE D N   
11690 C  CA  . ILE D 313 ? 0.3240 0.4817 0.8040 0.0551  0.0729  0.1027  314 ILE D CA  
11691 C  C   . ILE D 313 ? 0.4339 0.6009 0.9309 0.0597  0.0782  0.1049  314 ILE D C   
11692 O  O   . ILE D 313 ? 0.4359 0.6031 0.9330 0.0664  0.0839  0.1036  314 ILE D O   
11693 C  CB  . ILE D 313 ? 0.3891 0.5473 0.8585 0.0525  0.0774  0.1021  314 ILE D CB  
11694 C  CG1 . ILE D 313 ? 0.4010 0.5510 0.8555 0.0487  0.0729  0.1003  314 ILE D CG1 
11695 C  CG2 . ILE D 313 ? 0.3270 0.4870 0.7928 0.0588  0.0862  0.1004  314 ILE D CG2 
11696 C  CD1 . ILE D 313 ? 0.3208 0.4700 0.7634 0.0474  0.0770  0.0987  314 ILE D CD1 
11697 N  N   . GLY D 314 ? 0.4493 0.6240 0.9616 0.0568  0.0758  0.1084  315 GLY D N   
11698 C  CA  . GLY D 314 ? 0.3734 0.5584 0.9069 0.0602  0.0806  0.1123  315 GLY D CA  
11699 C  C   . GLY D 314 ? 0.3993 0.5861 0.9469 0.0627  0.0749  0.1129  315 GLY D C   
11700 O  O   . GLY D 314 ? 0.3705 0.5670 0.9405 0.0638  0.0759  0.1168  315 GLY D O   
11701 N  N   . SER D 315 ? 0.4480 0.6258 0.9843 0.0636  0.0691  0.1097  316 SER D N   
11702 C  CA  . SER D 315 ? 0.4067 0.5850 0.9542 0.0662  0.0629  0.1103  316 SER D CA  
11703 C  C   . SER D 315 ? 0.4789 0.6484 1.0169 0.0709  0.0627  0.1078  316 SER D C   
11704 O  O   . SER D 315 ? 0.4684 0.6359 1.0118 0.0728  0.0565  0.1083  316 SER D O   
11705 C  CB  . SER D 315 ? 0.3247 0.5013 0.8723 0.0622  0.0516  0.1105  316 SER D CB  
11706 O  OG  . SER D 315 ? 0.3192 0.5023 0.8767 0.0582  0.0494  0.1116  316 SER D OG  
11707 N  N   . VAL D 316 ? 0.4632 0.6268 0.9877 0.0731  0.0683  0.1048  317 VAL D N   
11708 C  CA  . VAL D 316 ? 0.4665 0.6197 0.9830 0.0777  0.0669  0.1013  317 VAL D CA  
11709 C  C   . VAL D 316 ? 0.4679 0.6243 0.9978 0.0848  0.0674  0.1018  317 VAL D C   
11710 O  O   . VAL D 316 ? 0.5026 0.6515 1.0325 0.0867  0.0619  0.1010  317 VAL D O   
11711 C  CB  . VAL D 316 ? 0.4719 0.6196 0.9746 0.0813  0.0725  0.0966  317 VAL D CB  
11712 C  CG1 . VAL D 316 ? 0.4771 0.6114 0.9722 0.0850  0.0679  0.0919  317 VAL D CG1 
11713 C  CG2 . VAL D 316 ? 0.4521 0.5989 0.9434 0.0748  0.0730  0.0965  317 VAL D CG2 
11714 N  N   . HIS D 317 ? 0.4521 0.6203 0.9951 0.0888  0.0745  0.1043  318 HIS D N   
11715 C  CA  . HIS D 317 ? 0.4749 0.6489 1.0328 0.0963  0.0768  0.1057  318 HIS D CA  
11716 C  C   . HIS D 317 ? 0.5018 0.6767 1.0723 0.0938  0.0674  0.1081  318 HIS D C   
11717 O  O   . HIS D 317 ? 0.6139 0.7881 1.1917 0.0998  0.0661  0.1079  318 HIS D O   
11718 C  CB  . HIS D 317 ? 0.4896 0.6788 1.0630 0.1001  0.0869  0.1107  318 HIS D CB  
11719 C  CG  . HIS D 317 ? 0.4737 0.6727 1.0633 0.0922  0.0844  0.1158  318 HIS D CG  
11720 N  ND1 . HIS D 317 ? 0.5061 0.7073 1.0910 0.0869  0.0877  0.1172  318 HIS D ND1 
11721 C  CD2 . HIS D 317 ? 0.4869 0.6932 1.0980 0.0891  0.0777  0.1192  318 HIS D CD2 
11722 C  CE1 . HIS D 317 ? 0.4919 0.7007 1.0952 0.0808  0.0829  0.1210  318 HIS D CE1 
11723 N  NE2 . HIS D 317 ? 0.4890 0.7009 1.1084 0.0821  0.0762  0.1220  318 HIS D NE2 
11724 N  N   . THR D 318 ? 0.5008 0.6770 1.0727 0.0862  0.0605  0.1099  319 THR D N   
11725 C  CA  . THR D 318 ? 0.4920 0.6686 1.0727 0.0853  0.0504  0.1115  319 THR D CA  
11726 C  C   . THR D 318 ? 0.4430 0.6070 1.0105 0.0868  0.0451  0.1102  319 THR D C   
11727 O  O   . THR D 318 ? 0.4991 0.6624 1.0742 0.0907  0.0402  0.1114  319 THR D O   
11728 C  CB  . THR D 318 ? 0.4409 0.6206 1.0228 0.0788  0.0432  0.1126  319 THR D CB  
11729 O  OG1 . THR D 318 ? 0.4709 0.6427 1.0321 0.0742  0.0434  0.1111  319 THR D OG1 
11730 C  CG2 . THR D 318 ? 0.4283 0.6205 1.0297 0.0769  0.0467  0.1149  319 THR D CG2 
11731 N  N   . TRP D 319 ? 0.4555 0.6098 1.0052 0.0838  0.0459  0.1086  320 TRP D N   
11732 C  CA  . TRP D 319 ? 0.4933 0.6354 1.0338 0.0848  0.0416  0.1088  320 TRP D CA  
11733 C  C   . TRP D 319 ? 0.4926 0.6294 1.0366 0.0918  0.0443  0.1058  320 TRP D C   
11734 O  O   . TRP D 319 ? 0.5494 0.6797 1.0962 0.0948  0.0395  0.1071  320 TRP D O   
11735 C  CB  . TRP D 319 ? 0.5656 0.6995 1.0903 0.0795  0.0418  0.1085  320 TRP D CB  
11736 C  CG  . TRP D 319 ? 0.6518 0.7876 1.1702 0.0746  0.0373  0.1124  320 TRP D CG  
11737 C  CD1 . TRP D 319 ? 0.6680 0.8010 1.1839 0.0754  0.0310  0.1173  320 TRP D CD1 
11738 C  CD2 . TRP D 319 ? 0.7247 0.8653 1.2368 0.0698  0.0389  0.1120  320 TRP D CD2 
11739 N  NE1 . TRP D 319 ? 0.7025 0.8384 1.2097 0.0724  0.0285  0.1196  320 TRP D NE1 
11740 C  CE2 . TRP D 319 ? 0.7523 0.8925 1.2576 0.0684  0.0329  0.1160  320 TRP D CE2 
11741 C  CE3 . TRP D 319 ? 0.7694 0.9145 1.2805 0.0674  0.0450  0.1091  320 TRP D CE3 
11742 C  CZ2 . TRP D 319 ? 0.7842 0.9278 1.2817 0.0648  0.0322  0.1160  320 TRP D CZ2 
11743 C  CZ3 . TRP D 319 ? 0.8079 0.9563 1.3128 0.0627  0.0443  0.1097  320 TRP D CZ3 
11744 C  CH2 . TRP D 319 ? 0.8049 0.9523 1.3031 0.0614  0.0376  0.1127  320 TRP D CH2 
11745 N  N   . LEU D 320 ? 0.4369 0.5761 0.9799 0.0955  0.0518  0.1019  321 LEU D N   
11746 C  CA  . LEU D 320 ? 0.5049 0.6396 1.0496 0.1045  0.0545  0.0980  321 LEU D CA  
11747 C  C   . LEU D 320 ? 0.4832 0.6244 1.0443 0.1098  0.0530  0.1008  321 LEU D C   
11748 O  O   . LEU D 320 ? 0.4712 0.6044 1.0340 0.1147  0.0492  0.0996  321 LEU D O   
11749 C  CB  . LEU D 320 ? 0.4436 0.5830 0.9837 0.1100  0.0640  0.0944  321 LEU D CB  
11750 C  CG  . LEU D 320 ? 0.4463 0.5788 0.9695 0.1066  0.0653  0.0905  321 LEU D CG  
11751 C  CD1 . LEU D 320 ? 0.4722 0.6104 0.9898 0.1144  0.0752  0.0876  321 LEU D CD1 
11752 C  CD2 . LEU D 320 ? 0.4139 0.5291 0.9274 0.1064  0.0580  0.0858  321 LEU D CD2 
11753 N  N   . ALA D 321 ? 0.4437 0.5996 1.0187 0.1086  0.0554  0.1046  322 ALA D N   
11754 C  CA  . ALA D 321 ? 0.4652 0.6299 1.0593 0.1131  0.0536  0.1077  322 ALA D CA  
11755 C  C   . ALA D 321 ? 0.5010 0.6596 1.0958 0.1112  0.0429  0.1097  322 ALA D C   
11756 O  O   . ALA D 321 ? 0.4887 0.6470 1.0926 0.1170  0.0402  0.1104  322 ALA D O   
11757 C  CB  . ALA D 321 ? 0.4355 0.6167 1.0473 0.1104  0.0564  0.1118  322 ALA D CB  
11758 N  N   . GLU D 322 ? 0.5416 0.6957 1.1260 0.1041  0.0373  0.1111  323 GLU D N   
11759 C  CA  . GLU D 322 ? 0.5658 0.7142 1.1474 0.1036  0.0281  0.1143  323 GLU D CA  
11760 C  C   . GLU D 322 ? 0.6452 0.7800 1.2205 0.1073  0.0270  0.1140  323 GLU D C   
11761 O  O   . GLU D 322 ? 0.6299 0.7616 1.2096 0.1111  0.0215  0.1170  323 GLU D O   
11762 C  CB  . GLU D 322 ? 0.5981 0.7446 1.1671 0.0970  0.0241  0.1163  323 GLU D CB  
11763 C  CG  . GLU D 322 ? 0.6740 0.8205 1.2418 0.0985  0.0146  0.1203  323 GLU D CG  
11764 C  CD  . GLU D 322 ? 0.7807 0.9287 1.3372 0.0941  0.0110  0.1214  323 GLU D CD  
11765 O  OE1 . GLU D 322 ? 0.7966 0.9459 1.3479 0.0889  0.0159  0.1193  323 GLU D OE1 
11766 O  OE2 . GLU D 322 ? 0.8220 0.9699 1.3737 0.0970  0.0030  0.1243  323 GLU D OE2 
11767 N  N   . ALA D 323 ? 0.6400 0.7664 1.2059 0.1066  0.0315  0.1104  324 ALA D N   
11768 C  CA  . ALA D 323 ? 0.6054 0.7173 1.1677 0.1100  0.0294  0.1090  324 ALA D CA  
11769 C  C   . ALA D 323 ? 0.5642 0.6763 1.1368 0.1193  0.0304  0.1062  324 ALA D C   
11770 O  O   . ALA D 323 ? 0.5143 0.6189 1.0912 0.1229  0.0254  0.1083  324 ALA D O   
11771 C  CB  . ALA D 323 ? 0.6233 0.7263 1.1745 0.1076  0.0323  0.1041  324 ALA D CB  
11772 N  N   . ILE D 324 ? 0.5400 0.6612 1.1167 0.1240  0.0376  0.1023  325 ILE D N   
11773 C  CA  . ILE D 324 ? 0.5412 0.6647 1.1276 0.1344  0.0402  0.1001  325 ILE D CA  
11774 C  C   . ILE D 324 ? 0.5345 0.6647 1.1356 0.1361  0.0351  0.1054  325 ILE D C   
11775 O  O   . ILE D 324 ? 0.5372 0.6614 1.1433 0.1428  0.0322  0.1050  325 ILE D O   
11776 C  CB  . ILE D 324 ? 0.5349 0.6713 1.1252 0.1397  0.0505  0.0981  325 ILE D CB  
11777 C  CG1 . ILE D 324 ? 0.5798 0.7095 1.1533 0.1399  0.0552  0.0925  325 ILE D CG1 
11778 C  CG2 . ILE D 324 ? 0.5399 0.6800 1.1402 0.1520  0.0541  0.0969  325 ILE D CG2 
11779 C  CD1 . ILE D 324 ? 0.5797 0.7227 1.1549 0.1458  0.0666  0.0923  325 ILE D CD1 
11780 N  N   . ASN D 325 ? 0.5714 0.7132 1.1794 0.1304  0.0330  0.1097  326 ASN D N   
11781 C  CA  . ASN D 325 ? 0.5991 0.7471 1.2200 0.1319  0.0261  0.1140  326 ASN D CA  
11782 C  C   . ASN D 325 ? 0.6071 0.7420 1.2204 0.1322  0.0181  0.1169  326 ASN D C   
11783 O  O   . ASN D 325 ? 0.6450 0.7789 1.2668 0.1383  0.0142  0.1186  326 ASN D O   
11784 C  CB  . ASN D 325 ? 0.5771 0.7369 1.2038 0.1256  0.0228  0.1166  326 ASN D CB  
11785 C  CG  . ASN D 325 ? 0.5862 0.7510 1.2240 0.1277  0.0130  0.1198  326 ASN D CG  
11786 O  OD1 . ASN D 325 ? 0.6207 0.7894 1.2725 0.1344  0.0119  0.1205  326 ASN D OD1 
11787 N  ND2 . ASN D 325 ? 0.5931 0.7575 1.2235 0.1233  0.0053  0.1216  326 ASN D ND2 
11788 N  N   . ALA D 326 ? 0.6600 0.7857 1.2585 0.1261  0.0164  0.1184  327 ALA D N   
11789 C  CA  . ALA D 326 ? 0.6725 0.7863 1.2646 0.1262  0.0104  0.1235  327 ALA D CA  
11790 C  C   . ALA D 326 ? 0.7007 0.8026 1.2968 0.1324  0.0101  0.1219  327 ALA D C   
11791 O  O   . ALA D 326 ? 0.6996 0.7961 1.2994 0.1363  0.0050  0.1267  327 ALA D O   
11792 C  CB  . ALA D 326 ? 0.6959 0.8026 1.2739 0.1189  0.0108  0.1259  327 ALA D CB  
11793 N  N   . LEU D 327 ? 0.6935 0.7911 1.2881 0.1344  0.0152  0.1149  328 LEU D N   
11794 C  CA  . LEU D 327 ? 0.6875 0.7727 1.2851 0.1417  0.0141  0.1112  328 LEU D CA  
11795 C  C   . LEU D 327 ? 0.7044 0.7968 1.3149 0.1507  0.0139  0.1111  328 LEU D C   
11796 O  O   . LEU D 327 ? 0.6869 0.7705 1.3022 0.1557  0.0090  0.1132  328 LEU D O   
11797 C  CB  . LEU D 327 ? 0.6584 0.7377 1.2488 0.1441  0.0187  0.1022  328 LEU D CB  
11798 C  CG  . LEU D 327 ? 0.6364 0.7035 1.2294 0.1543  0.0169  0.0960  328 LEU D CG  
11799 C  CD1 . LEU D 327 ? 0.5938 0.6422 1.1879 0.1521  0.0085  0.0988  328 LEU D CD1 
11800 C  CD2 . LEU D 327 ? 0.6273 0.6913 1.2109 0.1597  0.0217  0.0861  328 LEU D CD2 
11801 N  N   . GLN D 328 ? 0.7394 0.8483 1.3572 0.1529  0.0193  0.1096  329 GLN D N   
11802 C  CA  . GLN D 328 ? 0.7376 0.8564 1.3709 0.1612  0.0198  0.1104  329 GLN D CA  
11803 C  C   . GLN D 328 ? 0.7376 0.8569 1.3778 0.1612  0.0112  0.1168  329 GLN D C   
11804 O  O   . GLN D 328 ? 0.7248 0.8424 1.3739 0.1690  0.0085  0.1176  329 GLN D O   
11805 C  CB  . GLN D 328 ? 0.7954 0.9340 1.4397 0.1612  0.0265  0.1106  329 GLN D CB  
11806 C  CG  . GLN D 328 ? 0.8500 0.9921 1.4925 0.1678  0.0370  0.1055  329 GLN D CG  
11807 C  CD  . GLN D 328 ? 0.8894 1.0530 1.5494 0.1698  0.0444  0.1089  329 GLN D CD  
11808 O  OE1 . GLN D 328 ? 0.9113 1.0858 1.5904 0.1735  0.0426  0.1127  329 GLN D OE1 
11809 N  NE2 . GLN D 328 ? 0.8866 1.0568 1.5422 0.1672  0.0526  0.1082  329 GLN D NE2 
11810 N  N   . ASP D 329 ? 0.7485 0.8699 1.3831 0.1537  0.0066  0.1214  330 ASP D N   
11811 C  CA  . ASP D 329 ? 0.8023 0.9262 1.4407 0.1550  -0.0018 0.1274  330 ASP D CA  
11812 C  C   . ASP D 329 ? 0.8176 0.9256 1.4482 0.1568  -0.0066 0.1326  330 ASP D C   
11813 O  O   . ASP D 329 ? 0.8228 0.9314 1.4556 0.1605  -0.0132 0.1383  330 ASP D O   
11814 C  CB  . ASP D 329 ? 0.8455 0.9783 1.4794 0.1485  -0.0051 0.1295  330 ASP D CB  
11815 C  CG  . ASP D 329 ? 0.9015 1.0518 1.5510 0.1480  -0.0038 0.1267  330 ASP D CG  
11816 O  OD1 . ASP D 329 ? 0.9153 1.0713 1.5761 0.1513  0.0033  0.1236  330 ASP D OD1 
11817 O  OD2 . ASP D 329 ? 0.9027 1.0606 1.5535 0.1449  -0.0099 0.1279  330 ASP D OD2 
11818 N  N   . ASN D 330 ? 0.8757 0.9695 1.4984 0.1544  -0.0038 0.1311  331 ASN D N   
11819 C  CA  . ASN D 330 ? 0.9150 0.9930 1.5346 0.1553  -0.0079 0.1371  331 ASN D CA  
11820 C  C   . ASN D 330 ? 0.9299 0.9952 1.5557 0.1614  -0.0076 0.1321  331 ASN D C   
11821 O  O   . ASN D 330 ? 0.9221 0.9723 1.5492 0.1624  -0.0114 0.1363  331 ASN D O   
11822 C  CB  . ASN D 330 ? 0.9862 1.0566 1.5945 0.1469  -0.0069 0.1410  331 ASN D CB  
11823 C  CG  . ASN D 330 ? 1.0360 1.1152 1.6359 0.1434  -0.0087 0.1481  331 ASN D CG  
11824 O  OD1 . ASN D 330 ? 1.0836 1.1662 1.6840 0.1482  -0.0134 0.1546  331 ASN D OD1 
11825 N  ND2 . ASN D 330 ? 1.0212 1.1039 1.6120 0.1361  -0.0054 0.1466  331 ASN D ND2 
11826 N  N   . ARG D 331 ? 0.9335 1.0055 1.5640 0.1663  -0.0031 0.1236  332 ARG D N   
11827 C  CA  . ARG D 331 ? 0.9702 1.0314 1.6032 0.1739  -0.0019 0.1159  332 ARG D CA  
11828 C  C   . ARG D 331 ? 1.0149 1.0600 1.6536 0.1796  -0.0084 0.1186  332 ARG D C   
11829 O  O   . ARG D 331 ? 1.0513 1.0789 1.6879 0.1803  -0.0111 0.1148  332 ARG D O   
11830 C  CB  . ARG D 331 ? 0.9645 1.0404 1.6049 0.1820  0.0040  0.1105  332 ARG D CB  
11831 N  N   . ASP D 332 ? 1.0198 1.0704 1.6668 0.1840  -0.0117 0.1250  333 ASP D N   
11832 C  CA  . ASP D 332 ? 1.0489 1.0857 1.7032 0.1915  -0.0171 0.1270  333 ASP D CA  
11833 C  C   . ASP D 332 ? 1.0178 1.0417 1.6718 0.1871  -0.0227 0.1380  333 ASP D C   
11834 O  O   . ASP D 332 ? 1.0633 1.0700 1.7231 0.1907  -0.0271 0.1391  333 ASP D O   
11835 C  CB  . ASP D 332 ? 1.0674 1.1164 1.7324 0.2005  -0.0176 0.1279  333 ASP D CB  
11836 C  CG  . ASP D 332 ? 1.1009 1.1574 1.7705 0.2088  -0.0118 0.1181  333 ASP D CG  
11837 O  OD1 . ASP D 332 ? 1.1116 1.1674 1.7735 0.2071  -0.0065 0.1109  333 ASP D OD1 
11838 O  OD2 . ASP D 332 ? 1.1238 1.1872 1.8042 0.2179  -0.0121 0.1181  333 ASP D OD2 
11839 N  N   . THR D 333 ? 0.9657 0.9976 1.6135 0.1804  -0.0226 0.1466  334 THR D N   
11840 C  CA  . THR D 333 ? 0.9224 0.9433 1.5685 0.1761  -0.0256 0.1585  334 THR D CA  
11841 C  C   . THR D 333 ? 0.8720 0.8780 1.5177 0.1698  -0.0251 0.1550  334 THR D C   
11842 O  O   . THR D 333 ? 0.8551 0.8440 1.5089 0.1698  -0.0291 0.1598  334 THR D O   
11843 C  CB  . THR D 333 ? 0.9571 0.9903 1.5932 0.1717  -0.0246 0.1674  334 THR D CB  
11844 O  OG1 . THR D 333 ? 0.9835 1.0288 1.6208 0.1786  -0.0277 0.1700  334 THR D OG1 
11845 C  CG2 . THR D 333 ? 0.9725 0.9954 1.6068 0.1683  -0.0255 0.1813  334 THR D CG2 
11846 N  N   . LEU D 334 ? 0.7695 0.7823 1.4073 0.1646  -0.0208 0.1467  335 LEU D N   
11847 C  CA  . LEU D 334 ? 0.7723 0.7730 1.4084 0.1593  -0.0208 0.1405  335 LEU D CA  
11848 C  C   . LEU D 334 ? 0.7730 0.7559 1.4173 0.1660  -0.0257 0.1325  335 LEU D C   
11849 O  O   . LEU D 334 ? 0.8193 0.7851 1.4703 0.1628  -0.0308 0.1343  335 LEU D O   
11850 C  CB  . LEU D 334 ? 0.7137 0.7260 1.3396 0.1561  -0.0151 0.1308  335 LEU D CB  
11851 C  CG  . LEU D 334 ? 0.7389 0.7389 1.3619 0.1548  -0.0158 0.1201  335 LEU D CG  
11852 C  CD1 . LEU D 334 ? 0.7095 0.7027 1.3310 0.1443  -0.0172 0.1258  335 LEU D CD1 
11853 C  CD2 . LEU D 334 ? 0.7359 0.7475 1.3501 0.1578  -0.0095 0.1089  335 LEU D CD2 
11854 N  N   . THR D 335 ? 0.8053 0.7921 1.4505 0.1758  -0.0247 0.1236  336 THR D N   
11855 C  CA  . THR D 335 ? 0.8198 0.7897 1.4700 0.1843  -0.0295 0.1138  336 THR D CA  
11856 C  C   . THR D 335 ? 0.8154 0.7699 1.4787 0.1872  -0.0368 0.1220  336 THR D C   
11857 O  O   . THR D 335 ? 0.8518 0.7863 1.5218 0.1909  -0.0438 0.1163  336 THR D O   
11858 C  CB  . THR D 335 ? 0.9345 0.9142 1.5819 0.1960  -0.0250 0.1033  336 THR D CB  
11859 O  OG1 . THR D 335 ? 1.0178 0.9808 1.6636 0.2047  -0.0290 0.0907  336 THR D OG1 
11860 C  CG2 . THR D 335 ? 0.9617 0.9492 1.6181 0.2030  -0.0254 0.1095  336 THR D CG2 
11861 N  N   . ALA D 336 ? 0.7508 0.7140 1.4178 0.1862  -0.0361 0.1352  337 ALA D N   
11862 C  CA  . ALA D 336 ? 0.7286 0.6784 1.4079 0.1886  -0.0420 0.1458  337 ALA D CA  
11863 C  C   . ALA D 336 ? 0.6847 0.6192 1.3708 0.1796  -0.0457 0.1535  337 ALA D C   
11864 O  O   . ALA D 336 ? 0.7380 0.6522 1.4374 0.1813  -0.0528 0.1540  337 ALA D O   
11865 C  CB  . ALA D 336 ? 0.5978 0.5615 1.2765 0.1905  -0.0402 0.1586  337 ALA D CB  
11866 N  N   . LYS D 337 ? 0.6644 0.6085 1.3431 0.1701  -0.0411 0.1595  338 LYS D N   
11867 C  CA  . LYS D 337 ? 0.6336 0.5662 1.3204 0.1610  -0.0434 0.1680  338 LYS D CA  
11868 C  C   . LYS D 337 ? 0.6595 0.5752 1.3515 0.1591  -0.0493 0.1543  338 LYS D C   
11869 O  O   . LYS D 337 ? 0.6746 0.5731 1.3825 0.1549  -0.0558 0.1593  338 LYS D O   
11870 C  CB  . LYS D 337 ? 0.6212 0.5695 1.2969 0.1526  -0.0366 0.1761  338 LYS D CB  
11871 N  N   . VAL D 338 ? 0.6577 0.5784 1.3372 0.1630  -0.0476 0.1373  339 VAL D N   
11872 C  CA  . VAL D 338 ? 0.6973 0.6030 1.3768 0.1639  -0.0536 0.1221  339 VAL D CA  
11873 C  C   . VAL D 338 ? 0.7035 0.5883 1.3950 0.1733  -0.0633 0.1153  339 VAL D C   
11874 O  O   . VAL D 338 ? 0.7766 0.6414 1.4764 0.1730  -0.0729 0.1073  339 VAL D O   
11875 C  CB  . VAL D 338 ? 0.6278 0.5464 1.2883 0.1678  -0.0474 0.1072  339 VAL D CB  
11876 C  CG1 . VAL D 338 ? 0.6184 0.5205 1.2758 0.1734  -0.0544 0.0897  339 VAL D CG1 
11877 C  CG2 . VAL D 338 ? 0.6489 0.5843 1.2994 0.1575  -0.0398 0.1128  339 VAL D CG2 
11878 N  N   . ILE D 339 ? 0.6403 0.5291 1.3335 0.1818  -0.0618 0.1182  340 ILE D N   
11879 C  CA  . ILE D 339 ? 0.7073 0.5761 1.4131 0.1909  -0.0710 0.1141  340 ILE D CA  
11880 C  C   . ILE D 339 ? 0.7305 0.5833 1.4581 0.1838  -0.0780 0.1293  340 ILE D C   
11881 O  O   . ILE D 339 ? 0.7795 0.6090 1.5216 0.1851  -0.0892 0.1240  340 ILE D O   
11882 C  CB  . ILE D 339 ? 0.6643 0.5429 1.3673 0.2021  -0.0672 0.1144  340 ILE D CB  
11883 C  CG1 . ILE D 339 ? 0.6621 0.5507 1.3496 0.2123  -0.0624 0.0976  340 ILE D CG1 
11884 C  CG2 . ILE D 339 ? 0.6871 0.5453 1.4065 0.2094  -0.0765 0.1164  340 ILE D CG2 
11885 C  CD1 . ILE D 339 ? 0.7386 0.6379 1.4260 0.2239  -0.0586 0.0975  340 ILE D CD1 
11886 N  N   . GLN D 340 ? 0.7275 0.5926 1.4581 0.1771  -0.0717 0.1485  341 GLN D N   
11887 C  CA  . GLN D 340 ? 0.6721 0.5251 1.4240 0.1710  -0.0758 0.1667  341 GLN D CA  
11888 C  C   . GLN D 340 ? 0.6755 0.5158 1.4402 0.1606  -0.0814 0.1671  341 GLN D C   
11889 O  O   . GLN D 340 ? 0.6896 0.5136 1.4786 0.1567  -0.0882 0.1781  341 GLN D O   
11890 C  CB  . GLN D 340 ? 0.7554 0.6267 1.5032 0.1678  -0.0666 0.1873  341 GLN D CB  
11891 C  CG  . GLN D 340 ? 0.7707 0.6512 1.5124 0.1779  -0.0638 0.1909  341 GLN D CG  
11892 C  CD  . GLN D 340 ? 0.8115 0.7056 1.5502 0.1765  -0.0573 0.2122  341 GLN D CD  
11893 O  OE1 . GLN D 340 ? 0.8227 0.7362 1.5449 0.1798  -0.0516 0.2124  341 GLN D OE1 
11894 N  NE2 . GLN D 340 ? 0.8203 0.7044 1.5759 0.1725  -0.0584 0.2305  341 GLN D NE2 
11895 N  N   . GLY D 341 ? 0.6630 0.5112 1.4134 0.1562  -0.0787 0.1558  342 GLY D N   
11896 C  CA  . GLY D 341 ? 0.7079 0.5464 1.4695 0.1462  -0.0839 0.1558  342 GLY D CA  
11897 C  C   . GLY D 341 ? 0.7173 0.5352 1.4824 0.1502  -0.0965 0.1346  342 GLY D C   
11898 O  O   . GLY D 341 ? 0.7067 0.5070 1.4926 0.1442  -0.1069 0.1353  342 GLY D O   
11899 N  N   . CYS D 342 ? 0.7402 0.5604 1.4856 0.1614  -0.0960 0.1159  343 CYS D N   
11900 C  CA  . CYS D 342 ? 0.7830 0.5855 1.5245 0.1683  -0.1072 0.0937  343 CYS D CA  
11901 C  C   . CYS D 342 ? 0.8665 0.6508 1.6134 0.1820  -0.1165 0.0835  343 CYS D C   
11902 O  O   . CYS D 342 ? 0.8864 0.6501 1.6350 0.1890  -0.1294 0.0662  343 CYS D O   
11903 C  CB  . CYS D 342 ? 0.7506 0.5691 1.4634 0.1725  -0.0991 0.0793  343 CYS D CB  
11904 S  SG  . CYS D 342 ? 1.0037 0.8396 1.7092 0.1576  -0.0907 0.0868  343 CYS D SG  
11905 N  N   . GLY D 343 ? 0.9070 0.6986 1.6560 0.1867  -0.1108 0.0936  344 GLY D N   
11906 C  CA  . GLY D 343 ? 0.9697 0.7452 1.7244 0.2000  -0.1188 0.0856  344 GLY D CA  
11907 C  C   . GLY D 343 ? 0.9756 0.7662 1.7079 0.2137  -0.1101 0.0754  344 GLY D C   
11908 O  O   . GLY D 343 ? 0.9958 0.8095 1.7097 0.2123  -0.0980 0.0749  344 GLY D O   
11909 N  N   . ASN D 344 ? 1.0291 0.8065 1.7649 0.2271  -0.1164 0.0679  345 ASN D N   
11910 C  CA  . ASN D 344 ? 1.0354 0.8268 1.7539 0.2415  -0.1083 0.0595  345 ASN D CA  
11911 C  C   . ASN D 344 ? 1.0678 0.8516 1.7685 0.2556  -0.1121 0.0362  345 ASN D C   
11912 O  O   . ASN D 344 ? 1.1189 0.8764 1.8250 0.2630  -0.1264 0.0235  345 ASN D O   
11913 C  CB  . ASN D 344 ? 1.1167 0.9009 1.8479 0.2501  -0.1115 0.0654  345 ASN D CB  
11914 C  CG  . ASN D 344 ? 1.1541 0.9393 1.9022 0.2372  -0.1109 0.0879  345 ASN D CG  
11915 O  OD1 . ASN D 344 ? 1.1570 0.9637 1.9038 0.2330  -0.1004 0.1020  345 ASN D OD1 
11916 N  ND2 . ASN D 344 ? 1.1587 0.9220 1.9206 0.2308  -0.1220 0.0910  345 ASN D ND2 
11917 N  N   . PRO D 345 ? 1.0118 0.8181 1.6913 0.2601  -0.0994 0.0307  346 PRO D N   
11918 C  CA  . PRO D 345 ? 1.0815 0.8843 1.7406 0.2759  -0.1000 0.0104  346 PRO D CA  
11919 C  C   . PRO D 345 ? 1.1767 0.9821 1.8296 0.2955  -0.0968 0.0034  346 PRO D C   
11920 O  O   . PRO D 345 ? 1.1605 0.9708 1.8259 0.2957  -0.0945 0.0143  346 PRO D O   
11921 C  CB  . PRO D 345 ? 0.9945 0.8231 1.6372 0.2698  -0.0859 0.0122  346 PRO D CB  
11922 C  CG  . PRO D 345 ? 0.9550 0.8007 1.6093 0.2516  -0.0785 0.0329  346 PRO D CG  
11923 C  CD  . PRO D 345 ? 0.9779 0.8141 1.6518 0.2506  -0.0842 0.0438  346 PRO D CD  
11924 N  N   . LYS D 346 ? 1.3560 1.1589 1.9892 0.3130  -0.0962 -0.0141 347 LYS D N   
11925 C  CA  . LYS D 346 ? 1.4240 1.2307 2.0497 0.3340  -0.0919 -0.0211 347 LYS D CA  
11926 C  C   . LYS D 346 ? 1.4088 1.2504 2.0301 0.3346  -0.0724 -0.0106 347 LYS D C   
11927 O  O   . LYS D 346 ? 1.4359 1.2969 2.0506 0.3246  -0.0622 -0.0052 347 LYS D O   
11928 C  CB  . LYS D 346 ? 1.4632 1.2549 2.0674 0.3547  -0.0979 -0.0433 347 LYS D CB  
11929 N  N   . VAL D 347 ? 1.4007 1.2500 2.0274 0.3464  -0.0678 -0.0077 348 VAL D N   
11930 C  CA  . VAL D 347 ? 1.3364 1.2185 1.9654 0.3463  -0.0512 0.0036  348 VAL D CA  
11931 C  C   . VAL D 347 ? 1.3132 1.2074 1.9296 0.3693  -0.0412 -0.0051 348 VAL D C   
11932 O  O   . VAL D 347 ? 1.3402 1.2171 1.9509 0.3876  -0.0480 -0.0170 348 VAL D O   
11933 C  CB  . VAL D 347 ? 1.3373 1.2247 1.9873 0.3390  -0.0523 0.0185  348 VAL D CB  
11934 C  CG1 . VAL D 347 ? 1.3155 1.2368 1.9708 0.3351  -0.0376 0.0307  348 VAL D CG1 
11935 C  CG2 . VAL D 347 ? 1.3235 1.1963 1.9856 0.3198  -0.0623 0.0278  348 VAL D CG2 
11936 N  N   . ASN D 348 ? 1.2242 1.1485 1.8375 0.3686  -0.0250 0.0016  349 ASN D N   
11937 C  CA  . ASN D 348 ? 1.1746 1.1170 1.7794 0.3892  -0.0117 -0.0020 349 ASN D CA  
11938 C  C   . ASN D 348 ? 1.1938 1.1202 1.7735 0.4090  -0.0143 -0.0200 349 ASN D C   
11939 O  O   . ASN D 348 ? 1.1899 1.1335 1.7558 0.4220  -0.0009 -0.0223 349 ASN D O   
11940 C  CB  . ASN D 348 ? 1.1229 1.0703 1.7422 0.4005  -0.0107 0.0025  349 ASN D CB  
11941 C  CG  . ASN D 348 ? 1.0741 1.0435 1.6884 0.4220  0.0046  0.0015  349 ASN D CG  
11942 O  OD1 . ASN D 348 ? 1.0709 1.0577 1.6747 0.4257  0.0172  0.0018  349 ASN D OD1 
11943 N  ND2 . ASN D 348 ? 1.0478 1.0169 1.6706 0.4369  0.0043  0.0014  349 ASN D ND2 
11944 N  N   . ARG D 360 ? 0.9195 1.2429 1.8130 0.1452  0.0689  0.1676  361 ARG D N   
11945 C  CA  . ARG D 360 ? 0.9178 1.2314 1.7816 0.1503  0.0770  0.1628  361 ARG D CA  
11946 C  C   . ARG D 360 ? 0.9026 1.2042 1.7537 0.1430  0.0642  0.1556  361 ARG D C   
11947 O  O   . ARG D 360 ? 0.8993 1.1988 1.7604 0.1371  0.0480  0.1528  361 ARG D O   
11948 C  CB  . ARG D 360 ? 0.9197 1.2283 1.7691 0.1637  0.0820  0.1594  361 ARG D CB  
11949 N  N   . GLY D 361 ? 0.8934 1.1876 1.7222 0.1443  0.0714  0.1527  362 GLY D N   
11950 C  CA  . GLY D 361 ? 0.8937 1.1764 1.7082 0.1389  0.0613  0.1467  362 GLY D CA  
11951 C  C   . GLY D 361 ? 0.8839 1.1685 1.7079 0.1271  0.0516  0.1469  362 GLY D C   
11952 O  O   . GLY D 361 ? 0.9109 1.1877 1.7302 0.1224  0.0359  0.1421  362 GLY D O   
11953 N  N   . LYS D 362 ? 0.8546 1.1461 1.6849 0.1222  0.0604  0.1517  363 LYS D N   
11954 C  CA  . LYS D 362 ? 0.8446 1.1355 1.6811 0.1115  0.0519  0.1512  363 LYS D CA  
11955 C  C   . LYS D 362 ? 0.8050 1.0875 1.6152 0.1094  0.0579  0.1481  363 LYS D C   
11956 O  O   . LYS D 362 ? 0.8041 1.0907 1.6092 0.1123  0.0731  0.1521  363 LYS D O   
11957 C  CB  . LYS D 362 ? 0.8221 1.1234 1.6827 0.1059  0.0558  0.1589  363 LYS D CB  
11958 N  N   . LEU D 363 ? 0.7858 1.0534 1.5718 0.1040  0.0455  0.1403  364 LEU D N   
11959 C  CA  . LEU D 363 ? 0.7774 1.0324 1.5300 0.1004  0.0494  0.1360  364 LEU D CA  
11960 C  C   . LEU D 363 ? 0.7692 1.0203 1.5192 0.0913  0.0384  0.1333  364 LEU D C   
11961 O  O   . LEU D 363 ? 0.7696 1.0163 1.5203 0.0894  0.0232  0.1295  364 LEU D O   
11962 C  CB  . LEU D 363 ? 0.7585 0.9978 1.4796 0.1040  0.0472  0.1298  364 LEU D CB  
11963 C  CG  . LEU D 363 ? 0.7314 0.9693 1.4453 0.1136  0.0584  0.1300  364 LEU D CG  
11964 C  CD1 . LEU D 363 ? 0.7150 0.9373 1.4067 0.1163  0.0517  0.1246  364 LEU D CD1 
11965 C  CD2 . LEU D 363 ? 0.7135 0.9509 1.4130 0.1154  0.0723  0.1304  364 LEU D CD2 
11966 N  N   . ALA D 364 ? 0.8647 1.1169 1.6102 0.0869  0.0460  0.1351  365 ALA D N   
11967 C  CA  . ALA D 364 ? 0.9873 1.2348 1.7283 0.0789  0.0365  0.1321  365 ALA D CA  
11968 C  C   . ALA D 364 ? 1.1224 1.3538 1.8276 0.0778  0.0291  0.1248  365 ALA D C   
11969 O  O   . ALA D 364 ? 1.1611 1.3845 1.8414 0.0799  0.0371  0.1232  365 ALA D O   
11970 C  CB  . ALA D 364 ? 0.9897 1.2421 1.7335 0.0752  0.0476  0.1364  365 ALA D CB  
11971 N  N   . PRO D 365 ? 1.2108 1.4375 1.9142 0.0755  0.0135  0.1208  366 PRO D N   
11972 C  CA  . PRO D 365 ? 1.1925 1.4056 1.8627 0.0748  0.0078  0.1159  366 PRO D CA  
11973 C  C   . PRO D 365 ? 1.1199 1.3295 1.7747 0.0695  0.0146  0.1155  366 PRO D C   
11974 O  O   . PRO D 365 ? 1.1260 1.3435 1.7982 0.0661  0.0200  0.1184  366 PRO D O   
11975 C  CB  . PRO D 365 ? 1.2354 1.4469 1.9106 0.0755  -0.0103 0.1121  366 PRO D CB  
11976 C  CG  . PRO D 365 ? 1.2499 1.4729 1.9611 0.0771  -0.0153 0.1143  366 PRO D CG  
11977 C  CD  . PRO D 365 ? 1.2272 1.4609 1.9592 0.0746  -0.0004 0.1205  366 PRO D CD  
11978 N  N   . ARG D 366 ? 1.0482 1.2470 1.6731 0.0689  0.0147  0.1129  367 ARG D N   
11979 C  CA  . ARG D 366 ? 0.9895 1.1854 1.6008 0.0641  0.0198  0.1123  367 ARG D CA  
11980 C  C   . ARG D 366 ? 0.9824 1.1770 1.5944 0.0615  0.0074  0.1093  367 ARG D C   
11981 O  O   . ARG D 366 ? 0.9954 1.1837 1.5930 0.0644  -0.0031 0.1064  367 ARG D O   
11982 C  CB  . ARG D 366 ? 0.9673 1.1531 1.5495 0.0643  0.0252  0.1113  367 ARG D CB  
11983 C  CG  . ARG D 366 ? 0.9286 1.1065 1.4957 0.0678  0.0173  0.1106  367 ARG D CG  
11984 C  CD  . ARG D 366 ? 0.8767 1.0454 1.4188 0.0664  0.0216  0.1110  367 ARG D CD  
11985 N  NE  . ARG D 366 ? 0.8664 1.0299 1.3932 0.0685  0.0131  0.1118  367 ARG D NE  
11986 C  CZ  . ARG D 366 ? 0.8553 1.0136 1.3747 0.0730  0.0102  0.1145  367 ARG D CZ  
11987 N  NH1 . ARG D 366 ? 0.8613 1.0181 1.3881 0.0750  0.0139  0.1158  367 ARG D NH1 
11988 N  NH2 . ARG D 366 ? 0.8663 1.0212 1.3707 0.0764  0.0037  0.1166  367 ARG D NH2 
11989 N  N   . GLU D 367 ? 0.9402 1.1407 1.5691 0.0571  0.0084  0.1103  368 GLU D N   
11990 C  CA  . GLU D 367 ? 0.8978 1.0967 1.5319 0.0550  -0.0048 0.1066  368 GLU D CA  
11991 C  C   . GLU D 367 ? 0.9094 1.1076 1.5385 0.0497  0.0016  0.1073  368 GLU D C   
11992 O  O   . GLU D 367 ? 0.8495 1.0538 1.4888 0.0473  0.0145  0.1123  368 GLU D O   
11993 C  CB  . GLU D 367 ? 0.8792 1.0865 1.5496 0.0550  -0.0143 0.1072  368 GLU D CB  
11994 N  N   . ARG D 368 ? 0.9618 1.1526 1.5739 0.0492  -0.0071 0.1027  369 ARG D N   
11995 C  CA  . ARG D 368 ? 1.0351 1.2240 1.6377 0.0448  -0.0005 0.1032  369 ARG D CA  
11996 C  C   . ARG D 368 ? 1.1158 1.2994 1.7158 0.0441  -0.0140 0.0978  369 ARG D C   
11997 C  CB  . ARG D 368 ? 1.0276 1.2106 1.5986 0.0456  0.0093  0.1037  369 ARG D CB  
11998 N  N   . PRO D 369 ? 1.2382 1.4203 1.8331 0.0400  -0.0090 0.0984  370 PRO D N   
11999 C  CA  . PRO D 369 ? 1.2782 1.4660 1.8804 0.0355  0.0073  0.1048  370 PRO D CA  
12000 C  C   . PRO D 369 ? 1.2830 1.4810 1.9242 0.0329  0.0093  0.1104  370 PRO D C   
12001 O  O   . PRO D 369 ? 1.3068 1.5054 1.9708 0.0310  -0.0029 0.1087  370 PRO D O   
12002 C  CB  . PRO D 369 ? 1.3093 1.4918 1.8965 0.0328  0.0076  0.1029  370 PRO D CB  
12003 C  CG  . PRO D 369 ? 1.3208 1.4963 1.9036 0.0353  -0.0104 0.0956  370 PRO D CG  
12004 C  CD  . PRO D 369 ? 1.2927 1.4683 1.8813 0.0402  -0.0214 0.0926  370 PRO D CD  
12005 N  N   . PRO D 370 ? 1.2010 1.4069 1.8508 0.0336  0.0240  0.1171  371 PRO D N   
12006 C  CA  . PRO D 370 ? 1.2092 1.4269 1.8963 0.0320  0.0297  0.1253  371 PRO D CA  
12007 C  C   . PRO D 370 ? 1.1915 1.4110 1.8873 0.0275  0.0352  0.1298  371 PRO D C   
12008 O  O   . PRO D 370 ? 1.2237 1.4509 1.9548 0.0245  0.0345  0.1363  371 PRO D O   
12009 C  CB  . PRO D 370 ? 1.1960 1.4200 1.8793 0.0366  0.0454  0.1305  371 PRO D CB  
12010 C  CG  . PRO D 370 ? 1.2026 1.4173 1.8465 0.0383  0.0507  0.1258  371 PRO D CG  
12011 C  CD  . PRO D 370 ? 1.2009 1.4051 1.8266 0.0370  0.0358  0.1177  371 PRO D CD  
12012 N  N   . SER D 371 ? 1.1856 1.3978 1.8503 0.0271  0.0403  0.1270  372 SER D N   
12013 C  CA  . SER D 371 ? 1.1487 1.3612 1.8153 0.0236  0.0464  0.1309  372 SER D CA  
12014 C  C   . SER D 371 ? 1.0843 1.2863 1.7384 0.0208  0.0328  0.1233  372 SER D C   
12015 O  O   . SER D 371 ? 1.1237 1.3173 1.7525 0.0230  0.0242  0.1153  372 SER D O   
12016 C  CB  . SER D 371 ? 1.1772 1.3898 1.8181 0.0263  0.0631  0.1336  372 SER D CB  
12017 O  OG  . SER D 371 ? 1.1964 1.4202 1.8542 0.0297  0.0778  0.1431  372 SER D OG  
12018 N  N   . GLY D 372 ? 0.8687 1.0715 1.5413 0.0167  0.0313  0.1267  373 GLY D N   
12019 C  CA  . GLY D 372 ? 0.7300 0.9225 1.3870 0.0149  0.0216  0.1200  373 GLY D CA  
12020 C  C   . GLY D 372 ? 0.6140 0.8053 1.2459 0.0148  0.0359  0.1228  373 GLY D C   
12021 O  O   . GLY D 372 ? 0.5955 0.7792 1.2094 0.0140  0.0317  0.1183  373 GLY D O   
12022 N  N   . THR D 373 ? 0.4797 0.6786 1.1100 0.0167  0.0523  0.1298  374 THR D N   
12023 C  CA  . THR D 373 ? 0.4428 0.6419 1.0519 0.0179  0.0665  0.1330  374 THR D CA  
12024 C  C   . THR D 373 ? 0.2926 0.4820 0.8640 0.0188  0.0635  0.1248  374 THR D C   
12025 O  O   . THR D 373 ? 0.3823 0.5679 0.9407 0.0174  0.0654  0.1243  374 THR D O   
12026 C  CB  . THR D 373 ? 0.3740 0.5815 0.9828 0.0227  0.0821  0.1394  374 THR D CB  
12027 O  OG1 . THR D 373 ? 0.2914 0.5101 0.9361 0.0228  0.0881  0.1497  374 THR D OG1 
12028 C  CG2 . THR D 373 ? 0.3468 0.5531 0.9301 0.0256  0.0947  0.1408  374 THR D CG2 
12029 N  N   . LEU D 374 ? 0.3602 0.5463 0.9160 0.0213  0.0593  0.1195  375 LEU D N   
12030 C  CA  . LEU D 374 ? 0.3991 0.5778 0.9227 0.0225  0.0579  0.1139  375 LEU D CA  
12031 C  C   . LEU D 374 ? 0.4130 0.5849 0.9273 0.0211  0.0471  0.1091  375 LEU D C   
12032 O  O   . LEU D 374 ? 0.2966 0.4645 0.7894 0.0211  0.0497  0.1076  375 LEU D O   
12033 C  CB  . LEU D 374 ? 0.4170 0.5937 0.9307 0.0255  0.0546  0.1108  375 LEU D CB  
12034 C  CG  . LEU D 374 ? 0.3884 0.5587 0.8729 0.0267  0.0546  0.1074  375 LEU D CG  
12035 C  CD1 . LEU D 374 ? 0.3640 0.5347 0.8362 0.0267  0.0663  0.1092  375 LEU D CD1 
12036 C  CD2 . LEU D 374 ? 0.3581 0.5261 0.8367 0.0296  0.0500  0.1056  375 LEU D CD2 
12037 N  N   . GLU D 375 ? 0.4098 0.5801 0.9403 0.0208  0.0343  0.1063  376 GLU D N   
12038 C  CA  . GLU D 375 ? 0.4706 0.6333 0.9917 0.0215  0.0225  0.1005  376 GLU D CA  
12039 C  C   . GLU D 375 ? 0.4370 0.5989 0.9614 0.0183  0.0269  0.1031  376 GLU D C   
12040 O  O   . GLU D 375 ? 0.4550 0.6111 0.9590 0.0194  0.0245  0.0995  376 GLU D O   
12041 C  CB  . GLU D 375 ? 0.6220 0.7824 1.1619 0.0230  0.0059  0.0959  376 GLU D CB  
12042 C  CG  . GLU D 375 ? 0.7627 0.9160 1.3063 0.0230  -0.0065 0.0908  376 GLU D CG  
12043 C  CD  . GLU D 375 ? 0.8992 1.0456 1.4385 0.0290  -0.0256 0.0818  376 GLU D CD  
12044 O  OE1 . GLU D 375 ? 0.9275 1.0759 1.4679 0.0322  -0.0295 0.0806  376 GLU D OE1 
12045 O  OE2 . GLU D 375 ? 0.9424 1.0809 1.4759 0.0317  -0.0372 0.0754  376 GLU D OE2 
12046 N  N   . LYS D 376 ? 0.3574 0.5257 0.9076 0.0149  0.0342  0.1102  377 LYS D N   
12047 C  CA  . LYS D 376 ? 0.4156 0.5840 0.9713 0.0121  0.0401  0.1146  377 LYS D CA  
12048 C  C   . LYS D 376 ? 0.3671 0.5351 0.8939 0.0133  0.0523  0.1157  377 LYS D C   
12049 O  O   . LYS D 376 ? 0.4445 0.6075 0.9575 0.0129  0.0511  0.1137  377 LYS D O   
12050 C  CB  . LYS D 376 ? 0.4485 0.6258 1.0387 0.0094  0.0481  0.1248  377 LYS D CB  
12051 C  CG  . LYS D 376 ? 0.4114 0.5902 1.0369 0.0073  0.0356  0.1248  377 LYS D CG  
12052 C  CD  . LYS D 376 ? 0.4455 0.6136 1.0710 0.0068  0.0165  0.1156  377 LYS D CD  
12053 C  CE  . LYS D 376 ? 0.5094 0.6784 1.1772 0.0037  0.0038  0.1169  377 LYS D CE  
12054 N  NZ  . LYS D 376 ? 0.5173 0.6910 1.2157 -0.0011 0.0113  0.1279  377 LYS D NZ  
12055 N  N   . LEU D 377 ? 0.3811 0.5540 0.8997 0.0153  0.0629  0.1184  378 LEU D N   
12056 C  CA  . LEU D 377 ? 0.3848 0.5570 0.8777 0.0171  0.0729  0.1185  378 LEU D CA  
12057 C  C   . LEU D 377 ? 0.3685 0.5337 0.8355 0.0177  0.0662  0.1119  378 LEU D C   
12058 O  O   . LEU D 377 ? 0.3815 0.5444 0.8332 0.0175  0.0697  0.1116  378 LEU D O   
12059 C  CB  . LEU D 377 ? 0.2918 0.4684 0.7805 0.0202  0.0816  0.1201  378 LEU D CB  
12060 C  CG  . LEU D 377 ? 0.3730 0.5583 0.8820 0.0223  0.0922  0.1281  378 LEU D CG  
12061 C  CD1 . LEU D 377 ? 0.3594 0.5469 0.8595 0.0271  0.0987  0.1274  378 LEU D CD1 
12062 C  CD2 . LEU D 377 ? 0.2931 0.4812 0.8020 0.0230  0.1022  0.1343  378 LEU D CD2 
12063 N  N   . VAL D 378 ? 0.2956 0.4578 0.7580 0.0191  0.0570  0.1073  379 VAL D N   
12064 C  CA  . VAL D 378 ? 0.2982 0.4552 0.7373 0.0212  0.0515  0.1029  379 VAL D CA  
12065 C  C   . VAL D 378 ? 0.3944 0.5466 0.8294 0.0215  0.0442  0.1000  379 VAL D C   
12066 O  O   . VAL D 378 ? 0.4082 0.5579 0.8235 0.0229  0.0453  0.0988  379 VAL D O   
12067 C  CB  . VAL D 378 ? 0.3043 0.4598 0.7406 0.0243  0.0435  0.1001  379 VAL D CB  
12068 C  CG1 . VAL D 378 ? 0.3074 0.4583 0.7220 0.0283  0.0371  0.0970  379 VAL D CG1 
12069 C  CG2 . VAL D 378 ? 0.3201 0.4786 0.7551 0.0246  0.0506  0.1024  379 VAL D CG2 
12070 N  N   . SER D 379 ? 0.3553 0.5063 0.8107 0.0204  0.0363  0.0990  380 SER D N   
12071 C  CA  . SER D 379 ? 0.3121 0.4570 0.7664 0.0212  0.0275  0.0953  380 SER D CA  
12072 C  C   . SER D 379 ? 0.4151 0.5604 0.8641 0.0187  0.0368  0.0990  380 SER D C   
12073 O  O   . SER D 379 ? 0.4423 0.5837 0.8710 0.0210  0.0358  0.0963  380 SER D O   
12074 C  CB  . SER D 379 ? 0.4507 0.5938 0.9340 0.0196  0.0166  0.0939  380 SER D CB  
12075 O  OG  . SER D 379 ? 0.5117 0.6476 0.9963 0.0204  0.0071  0.0898  380 SER D OG  
12076 N  N   . GLU D 380 ? 0.3889 0.5395 0.8560 0.0151  0.0463  0.1057  381 GLU D N   
12077 C  CA  A GLU D 380 ? 0.4138 0.5655 0.8767 0.0138  0.0560  0.1103  381 GLU D CA  
12078 C  CA  B GLU D 380 ? 0.4153 0.5671 0.8783 0.0138  0.0561  0.1103  381 GLU D CA  
12079 C  C   . GLU D 380 ? 0.4020 0.5539 0.8360 0.0158  0.0629  0.1090  381 GLU D C   
12080 O  O   . GLU D 380 ? 0.4337 0.5828 0.8546 0.0163  0.0639  0.1084  381 GLU D O   
12081 C  CB  A GLU D 380 ? 0.4184 0.5776 0.9028 0.0119  0.0673  0.1193  381 GLU D CB  
12082 C  CB  B GLU D 380 ? 0.4184 0.5777 0.9026 0.0119  0.0675  0.1193  381 GLU D CB  
12083 C  CG  A GLU D 380 ? 0.4168 0.5757 0.9278 0.0090  0.0657  0.1247  381 GLU D CG  
12084 C  CG  B GLU D 380 ? 0.4575 0.6189 0.9354 0.0123  0.0791  0.1252  381 GLU D CG  
12085 C  CD  A GLU D 380 ? 0.4214 0.5753 0.9532 0.0073  0.0494  0.1199  381 GLU D CD  
12086 C  CD  B GLU D 380 ? 0.5193 0.6759 1.0075 0.0102  0.0743  0.1266  381 GLU D CD  
12087 O  OE1 A GLU D 380 ? 0.4273 0.5844 0.9737 0.0071  0.0454  0.1195  381 GLU D OE1 
12088 O  OE1 B GLU D 380 ? 0.5481 0.7000 1.0531 0.0083  0.0616  0.1232  381 GLU D OE1 
12089 O  OE2 A GLU D 380 ? 0.3996 0.5458 0.9328 0.0068  0.0396  0.1160  381 GLU D OE2 
12090 O  OE2 B GLU D 380 ? 0.5408 0.6977 1.0206 0.0109  0.0823  0.1306  381 GLU D OE2 
12091 N  N   . ALA D 381 ? 0.3332 0.4880 0.7589 0.0170  0.0667  0.1086  382 ALA D N   
12092 C  CA  . ALA D 381 ? 0.3472 0.5021 0.7501 0.0184  0.0718  0.1076  382 ALA D CA  
12093 C  C   . ALA D 381 ? 0.3593 0.5099 0.7447 0.0202  0.0649  0.1037  382 ALA D C   
12094 O  O   . ALA D 381 ? 0.3139 0.4643 0.6849 0.0207  0.0685  0.1039  382 ALA D O   
12095 C  CB  . ALA D 381 ? 0.3122 0.4695 0.7133 0.0194  0.0744  0.1074  382 ALA D CB  
12096 N  N   . LYS D 382 ? 0.3473 0.4951 0.7338 0.0224  0.0551  0.1003  383 LYS D N   
12097 C  CA  . LYS D 382 ? 0.3639 0.5082 0.7330 0.0265  0.0486  0.0971  383 LYS D CA  
12098 C  C   . LYS D 382 ? 0.4190 0.5598 0.7847 0.0269  0.0471  0.0959  383 LYS D C   
12099 O  O   . LYS D 382 ? 0.4576 0.5981 0.8061 0.0292  0.0489  0.0958  383 LYS D O   
12100 C  CB  . LYS D 382 ? 0.3538 0.4950 0.7245 0.0308  0.0373  0.0932  383 LYS D CB  
12101 C  CG  . LYS D 382 ? 0.3142 0.4580 0.6792 0.0329  0.0383  0.0947  383 LYS D CG  
12102 C  CD  . LYS D 382 ? 0.3809 0.5214 0.7417 0.0396  0.0267  0.0908  383 LYS D CD  
12103 C  CE  . LYS D 382 ? 0.5058 0.6491 0.8600 0.0424  0.0284  0.0938  383 LYS D CE  
12104 N  NZ  . LYS D 382 ? 0.5839 0.7241 0.9298 0.0511  0.0174  0.0905  383 LYS D NZ  
12105 N  N   . ALA D 383 ? 0.3605 0.4991 0.7447 0.0245  0.0438  0.0956  384 ALA D N   
12106 C  CA  . ALA D 383 ? 0.3798 0.5141 0.7641 0.0244  0.0419  0.0950  384 ALA D CA  
12107 C  C   . ALA D 383 ? 0.3562 0.4938 0.7297 0.0229  0.0534  0.0992  384 ALA D C   
12108 O  O   . ALA D 383 ? 0.3701 0.5054 0.7279 0.0254  0.0528  0.0977  384 ALA D O   
12109 C  CB  . ALA D 383 ? 0.3173 0.4495 0.7292 0.0210  0.0379  0.0963  384 ALA D CB  
12110 N  N   . GLN D 384 ? 0.3400 0.4829 0.7211 0.0198  0.0635  0.1042  385 GLN D N   
12111 C  CA  . GLN D 384 ? 0.3548 0.5007 0.7257 0.0195  0.0736  0.1076  385 GLN D CA  
12112 C  C   . GLN D 384 ? 0.3612 0.5078 0.7101 0.0216  0.0743  0.1054  385 GLN D C   
12113 O  O   . GLN D 384 ? 0.3801 0.5262 0.7176 0.0227  0.0763  0.1056  385 GLN D O   
12114 C  CB  . GLN D 384 ? 0.3960 0.5473 0.7754 0.0185  0.0832  0.1122  385 GLN D CB  
12115 C  CG  . GLN D 384 ? 0.4427 0.5958 0.8472 0.0168  0.0847  0.1169  385 GLN D CG  
12116 C  CD  . GLN D 384 ? 0.5384 0.6930 0.9495 0.0169  0.0926  0.1235  385 GLN D CD  
12117 O  OE1 . GLN D 384 ? 0.5176 0.6692 0.9175 0.0175  0.0925  0.1229  385 GLN D OE1 
12118 N  NE2 . GLN D 384 ? 0.5487 0.7087 0.9785 0.0170  0.1001  0.1308  385 GLN D NE2 
12119 N  N   . LEU D 385 ? 0.4040 0.5524 0.7493 0.0222  0.0728  0.1042  386 LEU D N   
12120 C  CA  . LEU D 385 ? 0.4173 0.5675 0.7470 0.0237  0.0739  0.1040  386 LEU D CA  
12121 C  C   . LEU D 385 ? 0.4483 0.5966 0.7659 0.0273  0.0689  0.1026  386 LEU D C   
12122 O  O   . LEU D 385 ? 0.4937 0.6441 0.8001 0.0283  0.0718  0.1039  386 LEU D O   
12123 C  CB  . LEU D 385 ? 0.3923 0.5441 0.7238 0.0238  0.0726  0.1041  386 LEU D CB  
12124 C  CG  . LEU D 385 ? 0.3685 0.5222 0.7085 0.0217  0.0778  0.1050  386 LEU D CG  
12125 C  CD1 . LEU D 385 ? 0.4052 0.5595 0.7457 0.0220  0.0758  0.1052  386 LEU D CD1 
12126 C  CD2 . LEU D 385 ? 0.3932 0.5483 0.7269 0.0213  0.0843  0.1057  386 LEU D CD2 
12127 N  N   . ARG D 386 ? 0.4506 0.5950 0.7704 0.0302  0.0608  0.0997  387 ARG D N   
12128 C  CA  . ARG D 386 ? 0.4963 0.6381 0.8024 0.0360  0.0554  0.0975  387 ARG D CA  
12129 C  C   . ARG D 386 ? 0.5688 0.7081 0.8724 0.0357  0.0568  0.0970  387 ARG D C   
12130 O  O   . ARG D 386 ? 0.5251 0.6644 0.8146 0.0401  0.0562  0.0967  387 ARG D O   
12131 C  CB  . ARG D 386 ? 0.5661 0.7028 0.8740 0.0408  0.0444  0.0928  387 ARG D CB  
12132 C  CG  . ARG D 386 ? 0.7008 0.8399 1.0051 0.0440  0.0424  0.0936  387 ARG D CG  
12133 C  CD  . ARG D 386 ? 0.7688 0.9135 1.0579 0.0472  0.0484  0.0985  387 ARG D CD  
12134 N  NE  . ARG D 386 ? 0.8548 1.0014 1.1391 0.0523  0.0460  0.1005  387 ARG D NE  
12135 C  CZ  . ARG D 386 ? 0.8809 1.0333 1.1637 0.0515  0.0523  0.1069  387 ARG D CZ  
12136 N  NH1 . ARG D 386 ? 0.9032 1.0595 1.1893 0.0457  0.0600  0.1106  387 ARG D NH1 
12137 N  NH2 . ARG D 386 ? 0.8632 1.0169 1.1421 0.0569  0.0501  0.1095  387 ARG D NH2 
12138 N  N   . ASP D 387 ? 0.5482 0.6861 0.8659 0.0310  0.0594  0.0981  388 ASP D N   
12139 C  CA  . ASP D 387 ? 0.5453 0.6808 0.8623 0.0306  0.0615  0.0989  388 ASP D CA  
12140 C  C   . ASP D 387 ? 0.5383 0.6788 0.8433 0.0301  0.0702  0.1021  388 ASP D C   
12141 O  O   . ASP D 387 ? 0.5865 0.7257 0.8831 0.0322  0.0707  0.1021  388 ASP D O   
12142 C  CB  . ASP D 387 ? 0.5754 0.7091 0.9130 0.0263  0.0631  0.1014  388 ASP D CB  
12143 C  CG  . ASP D 387 ? 0.6603 0.7917 0.9985 0.0260  0.0665  0.1040  388 ASP D CG  
12144 O  OD1 . ASP D 387 ? 0.7081 0.8334 1.0425 0.0289  0.0595  0.1007  388 ASP D OD1 
12145 O  OD2 . ASP D 387 ? 0.7042 0.8396 1.0457 0.0240  0.0760  0.1093  388 ASP D OD2 
12146 N  N   . VAL D 388 ? 0.5471 0.6927 0.8521 0.0279  0.0758  0.1042  389 VAL D N   
12147 C  CA  . VAL D 388 ? 0.4464 0.5961 0.7426 0.0275  0.0822  0.1062  389 VAL D CA  
12148 C  C   . VAL D 388 ? 0.4026 0.5563 0.6891 0.0290  0.0815  0.1066  389 VAL D C   
12149 O  O   . VAL D 388 ? 0.4118 0.5690 0.6948 0.0281  0.0850  0.1079  389 VAL D O   
12150 C  CB  . VAL D 388 ? 0.3802 0.5322 0.6829 0.0252  0.0883  0.1078  389 VAL D CB  
12151 C  CG1 . VAL D 388 ? 0.3420 0.4922 0.6552 0.0246  0.0917  0.1102  389 VAL D CG1 
12152 C  CG2 . VAL D 388 ? 0.2960 0.4492 0.6047 0.0239  0.0869  0.1070  389 VAL D CG2 
12153 N  N   . GLN D 389 ? 0.3033 0.4564 0.5864 0.0321  0.0765  0.1059  390 GLN D N   
12154 C  CA  . GLN D 389 ? 0.3035 0.4615 0.5794 0.0346  0.0768  0.1088  390 GLN D CA  
12155 C  C   . GLN D 389 ? 0.4031 0.5645 0.6697 0.0369  0.0792  0.1107  390 GLN D C   
12156 O  O   . GLN D 389 ? 0.3896 0.5569 0.6554 0.0367  0.0818  0.1146  390 GLN D O   
12157 C  CB  . GLN D 389 ? 0.3098 0.4667 0.5816 0.0400  0.0714  0.1083  390 GLN D CB  
12158 C  CG  . GLN D 389 ? 0.6141 0.7771 0.8820 0.0428  0.0732  0.1136  390 GLN D CG  
12159 C  CD  . GLN D 389 ? 0.6523 0.8153 0.9288 0.0406  0.0723  0.1146  390 GLN D CD  
12160 O  OE1 . GLN D 389 ? 0.6009 0.7604 0.8868 0.0361  0.0715  0.1113  390 GLN D OE1 
12161 N  NE2 . GLN D 389 ? 0.5875 0.7549 0.8614 0.0444  0.0731  0.1201  390 GLN D NE2 
12162 N  N   . ASP D 390 ? 0.4505 0.6080 0.7125 0.0390  0.0778  0.1084  391 ASP D N   
12163 C  CA  . ASP D 390 ? 0.4068 0.5669 0.6594 0.0423  0.0795  0.1099  391 ASP D CA  
12164 C  C   . ASP D 390 ? 0.3808 0.5418 0.6349 0.0387  0.0838  0.1103  391 ASP D C   
12165 O  O   . ASP D 390 ? 0.3356 0.4986 0.5829 0.0410  0.0851  0.1113  391 ASP D O   
12166 C  CB  . ASP D 390 ? 0.5212 0.6754 0.7665 0.0480  0.0745  0.1065  391 ASP D CB  
12167 C  CG  . ASP D 390 ? 0.6774 0.8234 0.9319 0.0450  0.0715  0.1029  391 ASP D CG  
12168 O  OD1 . ASP D 390 ? 0.7434 0.8898 1.0075 0.0393  0.0755  0.1042  391 ASP D OD1 
12169 O  OD2 . ASP D 390 ? 0.7522 0.8914 1.0052 0.0491  0.0647  0.0990  391 ASP D OD2 
12170 N  N   . PHE D 391 ? 0.3823 0.5421 0.6443 0.0342  0.0859  0.1096  392 PHE D N   
12171 C  CA  . PHE D 391 ? 0.3021 0.4613 0.5639 0.0329  0.0898  0.1095  392 PHE D CA  
12172 C  C   . PHE D 391 ? 0.3630 0.5267 0.6178 0.0341  0.0914  0.1107  392 PHE D C   
12173 O  O   . PHE D 391 ? 0.3767 0.5392 0.6266 0.0358  0.0932  0.1108  392 PHE D O   
12174 C  CB  . PHE D 391 ? 0.3000 0.4590 0.5690 0.0301  0.0923  0.1090  392 PHE D CB  
12175 C  CG  . PHE D 391 ? 0.3025 0.4613 0.5686 0.0312  0.0968  0.1093  392 PHE D CG  
12176 C  CD1 . PHE D 391 ? 0.3173 0.4730 0.5860 0.0322  0.1000  0.1112  392 PHE D CD1 
12177 C  CD2 . PHE D 391 ? 0.3034 0.4649 0.5649 0.0320  0.0973  0.1079  392 PHE D CD2 
12178 C  CE1 . PHE D 391 ? 0.3099 0.4660 0.5743 0.0349  0.1053  0.1128  392 PHE D CE1 
12179 C  CE2 . PHE D 391 ? 0.3085 0.4695 0.5642 0.0352  0.1009  0.1077  392 PHE D CE2 
12180 C  CZ  . PHE D 391 ? 0.3450 0.5038 0.6011 0.0371  0.1057  0.1107  392 PHE D CZ  
12181 N  N   . TRP D 392 ? 0.3525 0.5216 0.6087 0.0334  0.0904  0.1120  393 TRP D N   
12182 C  CA  . TRP D 392 ? 0.3921 0.5660 0.6462 0.0339  0.0907  0.1130  393 TRP D CA  
12183 C  C   . TRP D 392 ? 0.4497 0.6270 0.6972 0.0375  0.0909  0.1155  393 TRP D C   
12184 O  O   . TRP D 392 ? 0.4478 0.6274 0.6919 0.0387  0.0913  0.1155  393 TRP D O   
12185 C  CB  . TRP D 392 ? 0.3804 0.5587 0.6433 0.0312  0.0887  0.1144  393 TRP D CB  
12186 C  CG  . TRP D 392 ? 0.4040 0.5784 0.6720 0.0288  0.0879  0.1110  393 TRP D CG  
12187 C  CD1 . TRP D 392 ? 0.3743 0.5475 0.6496 0.0266  0.0869  0.1113  393 TRP D CD1 
12188 C  CD2 . TRP D 392 ? 0.3802 0.5515 0.6449 0.0297  0.0883  0.1068  393 TRP D CD2 
12189 N  NE1 . TRP D 392 ? 0.4006 0.5700 0.6780 0.0259  0.0866  0.1072  393 TRP D NE1 
12190 C  CE2 . TRP D 392 ? 0.3451 0.5133 0.6152 0.0284  0.0876  0.1044  393 TRP D CE2 
12191 C  CE3 . TRP D 392 ? 0.3457 0.5164 0.6019 0.0329  0.0893  0.1050  393 TRP D CE3 
12192 C  CZ2 . TRP D 392 ? 0.3330 0.4979 0.5995 0.0311  0.0880  0.1001  393 TRP D CZ2 
12193 C  CZ3 . TRP D 392 ? 0.3461 0.5135 0.5982 0.0356  0.0898  0.1012  393 TRP D CZ3 
12194 C  CH2 . TRP D 392 ? 0.3125 0.4771 0.5692 0.0351  0.0892  0.0986  393 TRP D CH2 
12195 N  N   . ILE D 393 ? 0.4066 0.5841 0.6511 0.0406  0.0901  0.1171  394 ILE D N   
12196 C  CA  . ILE D 393 ? 0.4050 0.5855 0.6415 0.0459  0.0905  0.1192  394 ILE D CA  
12197 C  C   . ILE D 393 ? 0.4200 0.5927 0.6489 0.0490  0.0893  0.1158  394 ILE D C   
12198 O  O   . ILE D 393 ? 0.4552 0.6287 0.6762 0.0543  0.0890  0.1165  394 ILE D O   
12199 C  CB  . ILE D 393 ? 0.4076 0.5933 0.6425 0.0506  0.0904  0.1235  394 ILE D CB  
12200 C  CG1 . ILE D 393 ? 0.3736 0.5526 0.6061 0.0523  0.0874  0.1205  394 ILE D CG1 
12201 C  CG2 . ILE D 393 ? 0.3400 0.5343 0.5858 0.0476  0.0919  0.1292  394 ILE D CG2 
12202 C  CD1 . ILE D 393 ? 0.3409 0.5239 0.5668 0.0600  0.0870  0.1241  394 ILE D CD1 
12203 N  N   . SER D 394 ? 0.4150 0.5804 0.6480 0.0460  0.0885  0.1128  395 SER D N   
12204 C  CA  . SER D 394 ? 0.4225 0.5799 0.6534 0.0481  0.0865  0.1104  395 SER D CA  
12205 C  C   . SER D 394 ? 0.4340 0.5890 0.6659 0.0463  0.0899  0.1111  395 SER D C   
12206 O  O   . SER D 394 ? 0.4984 0.6467 0.7313 0.0475  0.0889  0.1106  395 SER D O   
12207 C  CB  . SER D 394 ? 0.4283 0.5793 0.6667 0.0465  0.0828  0.1078  395 SER D CB  
12208 O  OG  . SER D 394 ? 0.4378 0.5888 0.6859 0.0411  0.0857  0.1085  395 SER D OG  
12209 N  N   . LEU D 395 ? 0.4082 0.5682 0.6400 0.0443  0.0933  0.1124  396 LEU D N   
12210 C  CA  . LEU D 395 ? 0.4485 0.6073 0.6780 0.0448  0.0969  0.1135  396 LEU D CA  
12211 C  C   . LEU D 395 ? 0.4808 0.6383 0.7028 0.0489  0.0969  0.1144  396 LEU D C   
12212 O  O   . LEU D 395 ? 0.4892 0.6415 0.7117 0.0499  0.0990  0.1160  396 LEU D O   
12213 C  CB  . LEU D 395 ? 0.5245 0.6887 0.7527 0.0441  0.0983  0.1130  396 LEU D CB  
12214 C  CG  . LEU D 395 ? 0.5447 0.7093 0.7795 0.0409  0.0983  0.1116  396 LEU D CG  
12215 C  CD1 . LEU D 395 ? 0.5315 0.7001 0.7646 0.0413  0.0970  0.1097  396 LEU D CD1 
12216 C  CD2 . LEU D 395 ? 0.5196 0.6794 0.7587 0.0406  0.1020  0.1126  396 LEU D CD2 
12217 N  N   . PRO D 396 ? 0.4623 0.6247 0.6785 0.0517  0.0950  0.1145  397 PRO D N   
12218 C  CA  . PRO D 396 ? 0.5037 0.6645 0.7126 0.0562  0.0950  0.1152  397 PRO D CA  
12219 C  C   . PRO D 396 ? 0.5361 0.6872 0.7457 0.0582  0.0925  0.1140  397 PRO D C   
12220 O  O   . PRO D 396 ? 0.5726 0.7188 0.7816 0.0595  0.0938  0.1153  397 PRO D O   
12221 C  CB  . PRO D 396 ? 0.4766 0.6454 0.6813 0.0595  0.0937  0.1162  397 PRO D CB  
12222 C  CG  . PRO D 396 ? 0.3189 0.4949 0.5302 0.0555  0.0941  0.1172  397 PRO D CG  
12223 C  CD  . PRO D 396 ? 0.4866 0.6572 0.7039 0.0513  0.0939  0.1153  397 PRO D CD  
12224 N  N   . GLY D 397 ? 0.5626 0.7106 0.7741 0.0589  0.0882  0.1115  398 GLY D N   
12225 C  CA  . GLY D 397 ? 0.5670 0.7045 0.7809 0.0612  0.0831  0.1088  398 GLY D CA  
12226 C  C   . GLY D 397 ? 0.6004 0.7313 0.8270 0.0564  0.0845  0.1106  398 GLY D C   
12227 O  O   . GLY D 397 ? 0.5997 0.7231 0.8300 0.0577  0.0832  0.1114  398 GLY D O   
12228 N  N   . THR D 398 ? 0.5948 0.7289 0.8292 0.0514  0.0877  0.1121  399 THR D N   
12229 C  CA  . THR D 398 ? 0.6396 0.7701 0.8875 0.0477  0.0909  0.1156  399 THR D CA  
12230 C  C   . THR D 398 ? 0.6461 0.7764 0.8920 0.0492  0.0970  0.1207  399 THR D C   
12231 O  O   . THR D 398 ? 0.7128 0.8364 0.9680 0.0493  0.0969  0.1240  399 THR D O   
12232 C  CB  . THR D 398 ? 0.6484 0.7843 0.9017 0.0438  0.0947  0.1166  399 THR D CB  
12233 O  OG1 . THR D 398 ? 0.6813 0.8168 0.9377 0.0425  0.0891  0.1126  399 THR D OG1 
12234 C  CG2 . THR D 398 ? 0.6275 0.7613 0.8947 0.0414  0.0997  0.1218  399 THR D CG2 
12235 N  N   . LEU D 399 ? 0.6180 0.7555 0.8529 0.0508  0.1016  0.1217  400 LEU D N   
12236 C  CA  . LEU D 399 ? 0.6161 0.7541 0.8462 0.0538  0.1074  0.1265  400 LEU D CA  
12237 C  C   . LEU D 399 ? 0.5998 0.7331 0.8254 0.0574  0.1052  0.1271  400 LEU D C   
12238 O  O   . LEU D 399 ? 0.5620 0.6923 0.7892 0.0595  0.1093  0.1325  400 LEU D O   
12239 C  CB  . LEU D 399 ? 0.6530 0.7990 0.8717 0.0557  0.1101  0.1254  400 LEU D CB  
12240 C  CG  . LEU D 399 ? 0.7128 0.8629 0.9341 0.0531  0.1109  0.1234  400 LEU D CG  
12241 C  CD1 . LEU D 399 ? 0.7126 0.8689 0.9236 0.0555  0.1105  0.1208  400 LEU D CD1 
12242 C  CD2 . LEU D 399 ? 0.7175 0.8656 0.9473 0.0528  0.1168  0.1279  400 LEU D CD2 
12243 N  N   . CYS D 400 ? 0.5935 0.7264 0.8131 0.0591  0.0992  0.1223  401 CYS D N   
12244 C  CA  . CYS D 400 ? 0.6712 0.7992 0.8854 0.0636  0.0965  0.1220  401 CYS D CA  
12245 C  C   . CYS D 400 ? 0.7391 0.8555 0.9659 0.0630  0.0927  0.1228  401 CYS D C   
12246 O  O   . CYS D 400 ? 0.7509 0.8621 0.9805 0.0648  0.0945  0.1270  401 CYS D O   
12247 C  CB  . CYS D 400 ? 0.6746 0.8061 0.8786 0.0674  0.0916  0.1171  401 CYS D CB  
12248 S  SG  . CYS D 400 ? 0.7783 0.9230 0.9710 0.0695  0.0951  0.1182  401 CYS D SG  
12249 N  N   . SER D 401 ? 0.7429 0.8548 0.9787 0.0606  0.0868  0.1189  402 SER D N   
12250 C  CA  . SER D 401 ? 0.8099 0.9098 1.0609 0.0598  0.0805  0.1185  402 SER D CA  
12251 C  C   . SER D 401 ? 0.8752 0.9736 1.1444 0.0553  0.0868  0.1272  402 SER D C   
12252 O  O   . SER D 401 ? 0.9161 1.0060 1.1987 0.0552  0.0849  0.1310  402 SER D O   
12253 C  CB  . SER D 401 ? 0.7608 0.8565 1.0168 0.0593  0.0713  0.1115  402 SER D CB  
12254 O  OG  . SER D 401 ? 0.7618 0.8589 1.0342 0.0531  0.0732  0.1143  402 SER D OG  
12255 N  N   . GLU D 402 ? 0.9135 1.0206 1.1841 0.0523  0.0946  0.1310  403 GLU D N   
12256 C  CA  . GLU D 402 ? 0.9759 1.0837 1.2623 0.0498  0.1025  0.1406  403 GLU D CA  
12257 C  C   . GLU D 402 ? 1.0250 1.1326 1.3070 0.0538  0.1096  0.1484  403 GLU D C   
12258 O  O   . GLU D 402 ? 1.0636 1.1671 1.3627 0.0531  0.1135  0.1574  403 GLU D O   
12259 C  CB  . GLU D 402 ? 0.9910 1.1083 1.2755 0.0480  0.1093  0.1420  403 GLU D CB  
12260 C  CG  . GLU D 402 ? 1.0298 1.1521 1.3178 0.0499  0.1212  0.1524  403 GLU D CG  
12261 C  CD  . GLU D 402 ? 1.0634 1.1909 1.3297 0.0559  0.1269  0.1535  403 GLU D CD  
12262 O  OE1 . GLU D 402 ? 1.0754 1.2056 1.3254 0.0570  0.1224  0.1458  403 GLU D OE1 
12263 O  OE2 . GLU D 402 ? 1.0765 1.2056 1.3431 0.0601  0.1357  0.1626  403 GLU D OE2 
12264 N  N   . LYS D 403 ? 1.0441 1.1562 1.3049 0.0582  0.1111  0.1457  404 LYS D N   
12265 C  CA  . LYS D 403 ? 1.0434 1.1564 1.2968 0.0630  0.1179  0.1526  404 LYS D CA  
12266 C  C   . LYS D 403 ? 1.0780 1.1857 1.3224 0.0668  0.1124  0.1494  404 LYS D C   
12267 O  O   . LYS D 403 ? 1.0947 1.1929 1.3502 0.0671  0.1094  0.1522  404 LYS D O   
12268 C  CB  . LYS D 403 ? 1.0188 1.1420 1.2548 0.0665  0.1244  0.1528  404 LYS D CB  
12269 C  CG  . LYS D 403 ? 1.0016 1.1273 1.2332 0.0723  0.1344  0.1626  404 LYS D CG  
12270 C  CD  . LYS D 403 ? 0.9506 1.0851 1.1689 0.0756  0.1391  0.1612  404 LYS D CD  
12271 C  CE  . LYS D 403 ? 0.9530 1.0902 1.1648 0.0837  0.1495  0.1711  404 LYS D CE  
12272 N  NZ  . LYS D 403 ? 0.9373 1.0687 1.1643 0.0842  0.1545  0.1826  404 LYS D NZ  
12273 N  N   . MET D 404 ? 1.0734 1.1874 1.2990 0.0697  0.1109  0.1434  405 MET D N   
12274 C  CA  . MET D 404 ? 1.0657 1.1787 1.2789 0.0750  0.1089  0.1422  405 MET D CA  
12275 C  C   . MET D 404 ? 1.0713 1.1757 1.2862 0.0765  0.0998  0.1364  405 MET D C   
12276 O  O   . MET D 404 ? 1.0911 1.1885 1.3061 0.0802  0.0982  0.1384  405 MET D O   
12277 C  CB  . MET D 404 ? 1.0264 1.1505 1.2228 0.0774  0.1098  0.1383  405 MET D CB  
12278 C  CG  . MET D 404 ? 1.0014 1.1331 1.1973 0.0749  0.1140  0.1386  405 MET D CG  
12279 S  SD  . MET D 404 ? 1.6318 1.7751 1.8139 0.0764  0.1119  0.1330  405 MET D SD  
12280 C  CE  . MET D 404 ? 0.3837 0.5312 0.5684 0.0737  0.1155  0.1330  405 MET D CE  
12281 N  N   . ALA D 405 ? 1.0301 1.1347 1.2454 0.0748  0.0936  0.1293  406 ALA D N   
12282 C  CA  . ALA D 405 ? 1.0171 1.1141 1.2292 0.0788  0.0843  0.1224  406 ALA D CA  
12283 C  C   . ALA D 405 ? 0.9853 1.0676 1.2119 0.0790  0.0787  0.1233  406 ALA D C   
12284 O  O   . ALA D 405 ? 0.9585 1.0350 1.1820 0.0835  0.0777  0.1248  406 ALA D O   
12285 C  CB  . ALA D 405 ? 1.0072 1.1066 1.2184 0.0776  0.0792  0.1158  406 ALA D CB  
12286 N  N   . ASP D 412 ? 1.2668 1.2599 1.4149 0.1647  0.0040  0.0662  413 ASP D N   
12287 C  CA  . ASP D 412 ? 1.2367 1.2528 1.3712 0.1633  0.0171  0.0715  413 ASP D CA  
12288 C  C   . ASP D 412 ? 1.1762 1.2050 1.3056 0.1622  0.0293  0.0810  413 ASP D C   
12289 O  O   . ASP D 412 ? 1.2110 1.2550 1.3239 0.1685  0.0361  0.0825  413 ASP D O   
12290 C  CB  . ASP D 412 ? 1.2565 1.2777 1.3680 0.1771  0.0135  0.0634  413 ASP D CB  
12291 N  N   . ARG D 413 ? 1.0837 1.1064 1.2283 0.1549  0.0321  0.0880  414 ARG D N   
12292 C  CA  . ARG D 413 ? 0.9674 1.0017 1.1079 0.1534  0.0433  0.0973  414 ARG D CA  
12293 C  C   . ARG D 413 ? 0.8643 0.9103 1.0150 0.1410  0.0535  0.1062  414 ARG D C   
12294 O  O   . ARG D 413 ? 0.8707 0.9092 1.0394 0.1329  0.0541  0.1112  414 ARG D O   
12295 C  CB  . ARG D 413 ? 0.9977 1.0180 1.1449 0.1562  0.0403  0.1002  414 ARG D CB  
12296 N  N   . CYS D 414 ? 0.7614 0.8261 0.9018 0.1403  0.0615  0.1085  415 CYS D N   
12297 C  CA  . CYS D 414 ? 0.6784 0.7543 0.8257 0.1302  0.0697  0.1147  415 CYS D CA  
12298 C  C   . CYS D 414 ? 0.6235 0.7159 0.7612 0.1312  0.0779  0.1198  415 CYS D C   
12299 O  O   . CYS D 414 ? 0.6977 0.7954 0.8242 0.1393  0.0777  0.1185  415 CYS D O   
12300 C  CB  . CYS D 414 ? 0.6423 0.7227 0.7915 0.1262  0.0680  0.1104  415 CYS D CB  
12301 S  SG  . CYS D 414 ? 0.9490 1.0440 1.0810 0.1343  0.0684  0.1062  415 CYS D SG  
12302 N  N   . TRP D 415 ? 0.5943 0.6947 0.7370 0.1238  0.0845  0.1251  416 TRP D N   
12303 C  CA  . TRP D 415 ? 0.5608 0.6755 0.6961 0.1246  0.0902  0.1290  416 TRP D CA  
12304 C  C   . TRP D 415 ? 0.5783 0.7079 0.7098 0.1239  0.0909  0.1263  416 TRP D C   
12305 O  O   . TRP D 415 ? 0.5548 0.6878 0.6919 0.1176  0.0916  0.1253  416 TRP D O   
12306 C  CB  . TRP D 415 ? 0.5978 0.7135 0.7384 0.1191  0.0960  0.1352  416 TRP D CB  
12307 C  CG  . TRP D 415 ? 0.6202 0.7498 0.7535 0.1199  0.0999  0.1373  416 TRP D CG  
12308 C  CD1 . TRP D 415 ? 0.6273 0.7669 0.7618 0.1151  0.1016  0.1364  416 TRP D CD1 
12309 C  CD2 . TRP D 415 ? 0.6574 0.7917 0.7821 0.1261  0.1009  0.1399  416 TRP D CD2 
12310 N  NE1 . TRP D 415 ? 0.6214 0.7710 0.7491 0.1181  0.1026  0.1376  416 TRP D NE1 
12311 C  CE2 . TRP D 415 ? 0.6585 0.8056 0.7800 0.1249  0.1023  0.1398  416 TRP D CE2 
12312 C  CE3 . TRP D 415 ? 0.6365 0.7650 0.7563 0.1331  0.1000  0.1418  416 TRP D CE3 
12313 C  CZ2 . TRP D 415 ? 0.6764 0.8309 0.7904 0.1304  0.1022  0.1414  416 TRP D CZ2 
12314 C  CZ3 . TRP D 415 ? 0.6627 0.7992 0.7743 0.1384  0.1011  0.1441  416 TRP D CZ3 
12315 C  CH2 . TRP D 415 ? 0.6684 0.8179 0.7772 0.1371  0.1020  0.1437  416 TRP D CH2 
12316 N  N   . ASN D 416 ? 0.5429 0.6821 0.6667 0.1305  0.0909  0.1261  417 ASN D N   
12317 C  CA  . ASN D 416 ? 0.5294 0.6840 0.6529 0.1306  0.0920  0.1257  417 ASN D CA  
12318 C  C   . ASN D 416 ? 0.5060 0.6745 0.6324 0.1273  0.0949  0.1292  417 ASN D C   
12319 O  O   . ASN D 416 ? 0.4901 0.6719 0.6206 0.1263  0.0956  0.1301  417 ASN D O   
12320 C  CB  . ASN D 416 ? 0.5351 0.6935 0.6508 0.1409  0.0905  0.1244  417 ASN D CB  
12321 C  CG  . ASN D 416 ? 0.5444 0.7043 0.6543 0.1481  0.0910  0.1265  417 ASN D CG  
12322 O  OD1 . ASN D 416 ? 0.4161 0.5826 0.5281 0.1457  0.0931  0.1301  417 ASN D OD1 
12323 N  ND2 . ASN D 416 ? 0.5652 0.7185 0.6669 0.1579  0.0882  0.1239  417 ASN D ND2 
12324 N  N   . GLY D 417 ? 0.5023 0.6675 0.6273 0.1264  0.0961  0.1315  418 GLY D N   
12325 C  CA  . GLY D 417 ? 0.4721 0.6486 0.5979 0.1253  0.0967  0.1333  418 GLY D CA  
12326 C  C   . GLY D 417 ? 0.5585 0.7389 0.6784 0.1327  0.0961  0.1353  418 GLY D C   
12327 O  O   . GLY D 417 ? 0.5652 0.7523 0.6841 0.1334  0.0953  0.1364  418 GLY D O   
12328 N  N   . MET D 418 ? 0.5688 0.7447 0.6842 0.1392  0.0956  0.1352  419 MET D N   
12329 C  CA  . MET D 418 ? 0.5612 0.7388 0.6705 0.1471  0.0951  0.1372  419 MET D CA  
12330 C  C   . MET D 418 ? 0.6463 0.8069 0.7501 0.1506  0.0953  0.1380  419 MET D C   
12331 O  O   . MET D 418 ? 0.6930 0.8500 0.7932 0.1522  0.0965  0.1413  419 MET D O   
12332 C  CB  . MET D 418 ? 0.5242 0.7121 0.6333 0.1539  0.0946  0.1373  419 MET D CB  
12333 C  CG  . MET D 418 ? 0.5112 0.7186 0.6288 0.1528  0.0945  0.1397  419 MET D CG  
12334 S  SD  . MET D 418 ? 1.3869 1.6094 1.5083 0.1605  0.0963  0.1425  419 MET D SD  
12335 C  CE  . MET D 418 ? 0.5749 0.7814 0.6845 0.1663  0.0966  0.1385  419 MET D CE  
12336 N  N   . ALA D 419 ? 0.6305 0.7803 0.7339 0.1524  0.0934  0.1352  420 ALA D N   
12337 C  CA  . ALA D 419 ? 0.6136 0.7456 0.7163 0.1547  0.0919  0.1357  420 ALA D CA  
12338 C  C   . ALA D 419 ? 0.6687 0.7881 0.7775 0.1507  0.0889  0.1319  420 ALA D C   
12339 O  O   . ALA D 419 ? 0.6272 0.7521 0.7390 0.1463  0.0886  0.1290  420 ALA D O   
12340 C  CB  . ALA D 419 ? 0.6561 0.7852 0.7514 0.1651  0.0895  0.1349  420 ALA D CB  
12341 N  N   . ARG D 420 ? 0.6442 0.7465 0.7566 0.1523  0.0859  0.1321  421 ARG D N   
12342 C  CA  . ARG D 420 ? 0.6387 0.7273 0.7584 0.1500  0.0802  0.1273  421 ARG D CA  
12343 C  C   . ARG D 420 ? 0.6200 0.7084 0.7303 0.1589  0.0745  0.1195  421 ARG D C   
12344 O  O   . ARG D 420 ? 0.6263 0.7138 0.7277 0.1683  0.0729  0.1185  421 ARG D O   
12345 C  CB  . ARG D 420 ? 0.6918 0.7619 0.8219 0.1492  0.0775  0.1303  421 ARG D CB  
12346 C  CG  . ARG D 420 ? 0.7600 0.8202 0.9064 0.1407  0.0754  0.1305  421 ARG D CG  
12347 C  CD  . ARG D 420 ? 0.8301 0.8733 0.9918 0.1395  0.0734  0.1361  421 ARG D CD  
12348 N  NE  . ARG D 420 ? 0.9142 0.9621 1.0779 0.1378  0.0829  0.1476  421 ARG D NE  
12349 C  CZ  . ARG D 420 ? 0.9941 1.0310 1.1732 0.1357  0.0849  0.1566  421 ARG D CZ  
12350 N  NH1 . ARG D 420 ? 1.0357 1.0557 1.2328 0.1337  0.0769  0.1550  421 ARG D NH1 
12351 N  NH2 . ARG D 420 ? 0.9948 1.0375 1.1721 0.1363  0.0946  0.1676  421 ARG D NH2 
12352 N  N   . GLY D 421 ? 0.5877 0.6773 0.6985 0.1572  0.0717  0.1144  422 GLY D N   
12353 C  CA  . GLY D 421 ? 0.6570 0.7510 0.7557 0.1673  0.0685  0.1087  422 GLY D CA  
12354 C  C   . GLY D 421 ? 0.6464 0.7460 0.7448 0.1654  0.0677  0.1052  422 GLY D C   
12355 O  O   . GLY D 421 ? 0.6687 0.7616 0.7767 0.1572  0.0655  0.1038  422 GLY D O   
12356 N  N   . ARG D 422 ? 0.6703 0.7823 0.7577 0.1742  0.0697  0.1045  423 ARG D N   
12357 C  CA  . ARG D 422 ? 0.6605 0.7804 0.7454 0.1749  0.0702  0.1028  423 ARG D CA  
12358 C  C   . ARG D 422 ? 0.6491 0.7887 0.7415 0.1663  0.0787  0.1102  423 ARG D C   
12359 O  O   . ARG D 422 ? 0.6413 0.7926 0.7356 0.1655  0.0838  0.1158  423 ARG D O   
12360 C  CB  . ARG D 422 ? 0.7094 0.8324 0.7781 0.1913  0.0685  0.0995  423 ARG D CB  
12361 C  CG  . ARG D 422 ? 0.7763 0.8888 0.8372 0.1981  0.0609  0.0914  423 ARG D CG  
12362 C  CD  . ARG D 422 ? 0.8475 0.9682 0.8899 0.2162  0.0622  0.0904  423 ARG D CD  
12363 N  NE  . ARG D 422 ? 0.8829 1.0094 0.9188 0.2251  0.0658  0.0936  423 ARG D NE  
12364 C  CZ  . ARG D 422 ? 0.9055 1.0482 0.9308 0.2381  0.0724  0.0985  423 ARG D CZ  
12365 N  NH1 . ARG D 422 ? 0.9120 1.0667 0.9316 0.2441  0.0766  0.1014  423 ARG D NH1 
12366 N  NH2 . ARG D 422 ? 0.9266 1.0742 0.9477 0.2457  0.0752  0.1014  423 ARG D NH2 
12367 N  N   . TYR D 423 ? 0.6444 0.7869 0.7419 0.1601  0.0791  0.1098  424 TYR D N   
12368 C  CA  . TYR D 423 ? 0.5937 0.7546 0.6986 0.1537  0.0859  0.1161  424 TYR D CA  
12369 C  C   . TYR D 423 ? 0.5855 0.7583 0.6841 0.1626  0.0884  0.1181  424 TYR D C   
12370 O  O   . TYR D 423 ? 0.6111 0.7790 0.7057 0.1650  0.0856  0.1145  424 TYR D O   
12371 C  CB  . TYR D 423 ? 0.5916 0.7493 0.7078 0.1406  0.0858  0.1159  424 TYR D CB  
12372 C  CG  . TYR D 423 ? 0.6110 0.7851 0.7363 0.1333  0.0912  0.1215  424 TYR D CG  
12373 C  CD1 . TYR D 423 ? 0.6082 0.7899 0.7397 0.1283  0.0940  0.1253  424 TYR D CD1 
12374 C  CD2 . TYR D 423 ? 0.5840 0.7650 0.7123 0.1320  0.0924  0.1226  424 TYR D CD2 
12375 C  CE1 . TYR D 423 ? 0.5807 0.7756 0.7222 0.1219  0.0966  0.1291  424 TYR D CE1 
12376 C  CE2 . TYR D 423 ? 0.5697 0.7645 0.7091 0.1251  0.0963  0.1277  424 TYR D CE2 
12377 C  CZ  . TYR D 423 ? 0.5723 0.7735 0.7189 0.1198  0.0977  0.1305  424 TYR D CZ  
12378 O  OH  . TYR D 423 ? 0.5137 0.7269 0.6727 0.1132  0.0994  0.1344  424 TYR D OH  
12379 N  N   . LEU D 424 ? 0.6397 0.8286 0.7380 0.1683  0.0939  0.1246  425 LEU D N   
12380 C  CA  . LEU D 424 ? 0.6260 0.8289 0.7194 0.1787  0.0985  0.1294  425 LEU D CA  
12381 C  C   . LEU D 424 ? 0.6057 0.8206 0.7098 0.1722  0.1027  0.1350  425 LEU D C   
12382 O  O   . LEU D 424 ? 0.6454 0.8609 0.7416 0.1798  0.1031  0.1348  425 LEU D O   
12383 C  CB  . LEU D 424 ? 0.7042 0.9228 0.7989 0.1860  0.1039  0.1366  425 LEU D CB  
12384 C  CG  . LEU D 424 ? 0.7746 0.9840 0.8547 0.1983  0.1009  0.1321  425 LEU D CG  
12385 C  CD1 . LEU D 424 ? 0.8130 1.0403 0.8963 0.2055  0.1069  0.1403  425 LEU D CD1 
12386 C  CD2 . LEU D 424 ? 0.8179 1.0163 0.8795 0.2125  0.0968  0.1255  425 LEU D CD2 
12387 N  N   . PRO D 425 ? 0.5305 0.7545 0.6518 0.1593  0.1051  0.1397  426 PRO D N   
12388 C  CA  . PRO D 425 ? 0.5418 0.7790 0.6753 0.1545  0.1093  0.1465  426 PRO D CA  
12389 C  C   . PRO D 425 ? 0.5875 0.8152 0.7172 0.1519  0.1067  0.1421  426 PRO D C   
12390 O  O   . PRO D 425 ? 0.6334 0.8442 0.7578 0.1480  0.1009  0.1336  426 PRO D O   
12391 C  CB  . PRO D 425 ? 0.4427 0.6855 0.5939 0.1409  0.1089  0.1487  426 PRO D CB  
12392 C  CG  . PRO D 425 ? 0.4266 0.6659 0.5739 0.1426  0.1070  0.1464  426 PRO D CG  
12393 C  CD  . PRO D 425 ? 0.4755 0.6976 0.6051 0.1498  0.1035  0.1390  426 PRO D CD  
12394 N  N   . GLU D 426 ? 0.6212 0.8605 0.7553 0.1545  0.1112  0.1489  427 GLU D N   
12395 C  CA  . GLU D 426 ? 0.6232 0.8555 0.7550 0.1521  0.1090  0.1458  427 GLU D CA  
12396 C  C   . GLU D 426 ? 0.5660 0.7961 0.7140 0.1356  0.1073  0.1447  427 GLU D C   
12397 O  O   . GLU D 426 ? 0.5216 0.7605 0.6842 0.1277  0.1092  0.1491  427 GLU D O   
12398 C  CB  . GLU D 426 ? 0.7326 0.9786 0.8631 0.1615  0.1153  0.1549  427 GLU D CB  
12399 C  CG  . GLU D 426 ? 0.8631 1.1104 0.9732 0.1811  0.1171  0.1553  427 GLU D CG  
12400 C  CD  . GLU D 426 ? 0.9859 1.2436 1.0905 0.1921  0.1229  0.1632  427 GLU D CD  
12401 O  OE1 . GLU D 426 ? 1.0225 1.2720 1.1232 0.1900  0.1192  0.1591  427 GLU D OE1 
12402 O  OE2 . GLU D 426 ? 1.0172 1.2919 1.1218 0.2034  0.1315  0.1746  427 GLU D OE2 
12403 N  N   . VAL D 427 ? 0.5462 0.7642 0.6914 0.1314  0.1031  0.1385  428 VAL D N   
12404 C  CA  . VAL D 427 ? 0.4927 0.7086 0.6517 0.1176  0.1019  0.1375  428 VAL D CA  
12405 C  C   . VAL D 427 ? 0.5133 0.7445 0.6860 0.1146  0.1068  0.1467  428 VAL D C   
12406 O  O   . VAL D 427 ? 0.5208 0.7618 0.6906 0.1238  0.1111  0.1536  428 VAL D O   
12407 C  CB  . VAL D 427 ? 0.5396 0.7403 0.6938 0.1149  0.0966  0.1297  428 VAL D CB  
12408 C  CG1 . VAL D 427 ? 0.5150 0.7129 0.6825 0.1015  0.0958  0.1284  428 VAL D CG1 
12409 C  CG2 . VAL D 427 ? 0.5678 0.7535 0.7109 0.1196  0.0910  0.1218  428 VAL D CG2 
12410 N  N   . MET D 428 ? 0.4802 0.7138 0.6685 0.1029  0.1062  0.1475  429 MET D N   
12411 C  CA  . MET D 428 ? 0.4533 0.6997 0.6584 0.0989  0.1093  0.1560  429 MET D CA  
12412 C  C   . MET D 428 ? 0.4771 0.7187 0.6825 0.0963  0.1087  0.1551  429 MET D C   
12413 O  O   . MET D 428 ? 0.4628 0.6914 0.6564 0.0973  0.1052  0.1474  429 MET D O   
12414 C  CB  . MET D 428 ? 0.4697 0.7199 0.6916 0.0885  0.1070  0.1562  429 MET D CB  
12415 C  CG  . MET D 428 ? 0.4813 0.7389 0.7062 0.0910  0.1071  0.1584  429 MET D CG  
12416 S  SD  . MET D 428 ? 0.6211 0.8996 0.8584 0.0987  0.1136  0.1726  429 MET D SD  
12417 C  CE  . MET D 428 ? 0.4369 0.7121 0.6493 0.1136  0.1169  0.1710  429 MET D CE  
12418 N  N   . GLY D 429 ? 0.4436 0.6957 0.6648 0.0930  0.1115  0.1633  430 GLY D N   
12419 C  CA  . GLY D 429 ? 0.3286 0.5767 0.5526 0.0895  0.1109  0.1631  430 GLY D CA  
12420 C  C   . GLY D 429 ? 0.3904 0.6316 0.6254 0.0770  0.1062  0.1571  430 GLY D C   
12421 O  O   . GLY D 429 ? 0.3148 0.5568 0.5566 0.0720  0.1040  0.1550  430 GLY D O   
12422 N  N   . ASP D 430 ? 0.3176 0.5519 0.5533 0.0731  0.1044  0.1541  431 ASP D N   
12423 C  CA  . ASP D 430 ? 0.5000 0.7280 0.7451 0.0629  0.1006  0.1486  431 ASP D CA  
12424 C  C   . ASP D 430 ? 0.3049 0.5421 0.5712 0.0570  0.1005  0.1552  431 ASP D C   
12425 O  O   . ASP D 430 ? 0.3324 0.5801 0.6079 0.0600  0.1042  0.1653  431 ASP D O   
12426 C  CB  . ASP D 430 ? 0.4636 0.6813 0.7031 0.0612  0.0986  0.1432  431 ASP D CB  
12427 C  CG  . ASP D 430 ? 0.5435 0.7514 0.7664 0.0666  0.0969  0.1368  431 ASP D CG  
12428 O  OD1 . ASP D 430 ? 0.5802 0.7801 0.7998 0.0636  0.0949  0.1307  431 ASP D OD1 
12429 O  OD2 . ASP D 430 ? 0.5645 0.7721 0.7778 0.0746  0.0973  0.1380  431 ASP D OD2 
12430 N  N   . GLY D 431 ? 0.3007 0.5338 0.5753 0.0496  0.0958  0.1498  432 GLY D N   
12431 C  CA  . GLY D 431 ? 0.3563 0.5955 0.6527 0.0438  0.0930  0.1540  432 GLY D CA  
12432 C  C   . GLY D 431 ? 0.3672 0.6133 0.6741 0.0428  0.0900  0.1553  432 GLY D C   
12433 O  O   . GLY D 431 ? 0.4605 0.7108 0.7595 0.0479  0.0924  0.1568  432 GLY D O   
12434 N  N   . LEU D 432 ? 0.3949 0.6416 0.7204 0.0366  0.0837  0.1543  433 LEU D N   
12435 C  CA  . LEU D 432 ? 0.3785 0.6307 0.7166 0.0353  0.0779  0.1539  433 LEU D CA  
12436 C  C   . LEU D 432 ? 0.3984 0.6660 0.7503 0.0384  0.0823  0.1663  433 LEU D C   
12437 O  O   . LEU D 432 ? 0.4624 0.7345 0.8104 0.0419  0.0821  0.1662  433 LEU D O   
12438 C  CB  . LEU D 432 ? 0.2971 0.5464 0.6554 0.0287  0.0685  0.1503  433 LEU D CB  
12439 C  CG  . LEU D 432 ? 0.3007 0.5524 0.6713 0.0275  0.0591  0.1465  433 LEU D CG  
12440 C  CD1 . LEU D 432 ? 0.3055 0.5480 0.6516 0.0315  0.0566  0.1349  433 LEU D CD1 
12441 C  CD2 . LEU D 432 ? 0.3033 0.5523 0.6982 0.0215  0.0484  0.1440  433 LEU D CD2 
12442 N  N   . ALA D 433 ? 0.2941 0.5704 0.6625 0.0379  0.0867  0.1779  434 ALA D N   
12443 C  CA  . ALA D 433 ? 0.3590 0.6521 0.7448 0.0414  0.0921  0.1926  434 ALA D CA  
12444 C  C   . ALA D 433 ? 0.4084 0.7063 0.7732 0.0512  0.0998  0.1950  434 ALA D C   
12445 O  O   . ALA D 433 ? 0.3237 0.6339 0.6987 0.0547  0.1021  0.2027  434 ALA D O   
12446 C  CB  . ALA D 433 ? 0.2941 0.5948 0.6967 0.0410  0.0977  0.2058  434 ALA D CB  
12447 N  N   . ASN D 434 ? 0.3562 0.6438 0.6929 0.0559  0.1030  0.1881  435 ASN D N   
12448 C  CA  . ASN D 434 ? 0.3600 0.6494 0.6754 0.0660  0.1088  0.1888  435 ASN D CA  
12449 C  C   . ASN D 434 ? 0.3057 0.5911 0.6112 0.0668  0.1049  0.1806  435 ASN D C   
12450 O  O   . ASN D 434 ? 0.3107 0.5970 0.6000 0.0751  0.1087  0.1807  435 ASN D O   
12451 C  CB  . ASN D 434 ? 0.3787 0.6569 0.6699 0.0707  0.1111  0.1831  435 ASN D CB  
12452 C  CG  . ASN D 434 ? 0.4054 0.6906 0.6989 0.0761  0.1175  0.1936  435 ASN D CG  
12453 O  OD1 . ASN D 434 ? 0.3843 0.6847 0.6906 0.0811  0.1235  0.2071  435 ASN D OD1 
12454 N  ND2 . ASN D 434 ? 0.4302 0.7052 0.7120 0.0760  0.1164  0.1883  435 ASN D ND2 
12455 N  N   . GLN D 435 ? 0.3025 0.5829 0.6166 0.0592  0.0970  0.1735  436 GLN D N   
12456 C  CA  . GLN D 435 ? 0.3045 0.5804 0.6080 0.0605  0.0931  0.1657  436 GLN D CA  
12457 C  C   . GLN D 435 ? 0.4659 0.7542 0.7890 0.0601  0.0898  0.1708  436 GLN D C   
12458 O  O   . GLN D 435 ? 0.4615 0.7467 0.7792 0.0606  0.0847  0.1644  436 GLN D O   
12459 C  CB  . GLN D 435 ? 0.3045 0.5661 0.5998 0.0551  0.0865  0.1536  436 GLN D CB  
12460 C  CG  . GLN D 435 ? 0.3314 0.5814 0.6121 0.0544  0.0891  0.1488  436 GLN D CG  
12461 C  CD  . GLN D 435 ? 0.3450 0.5914 0.6060 0.0615  0.0947  0.1489  436 GLN D CD  
12462 O  OE1 . GLN D 435 ? 0.3977 0.6438 0.6484 0.0663  0.0954  0.1475  436 GLN D OE1 
12463 N  NE2 . GLN D 435 ? 0.3084 0.5514 0.5642 0.0627  0.0977  0.1500  436 GLN D NE2 
12464 N  N   . ILE D 436 ? 0.3020 0.6048 0.6491 0.0596  0.0926  0.1833  437 ILE D N   
12465 C  CA  . ILE D 436 ? 0.3346 0.6508 0.7064 0.0586  0.0890  0.1899  437 ILE D CA  
12466 C  C   . ILE D 436 ? 0.3169 0.6389 0.6759 0.0672  0.0931  0.1914  437 ILE D C   
12467 O  O   . ILE D 436 ? 0.3614 0.6861 0.7269 0.0667  0.0868  0.1883  437 ILE D O   
12468 C  CB  . ILE D 436 ? 0.2991 0.6312 0.7027 0.0568  0.0931  0.2060  437 ILE D CB  
12469 C  CG1 . ILE D 436 ? 0.3034 0.6512 0.7370 0.0559  0.0896  0.2144  437 ILE D CG1 
12470 C  CG2 . ILE D 436 ? 0.3015 0.6404 0.6934 0.0656  0.1063  0.2167  437 ILE D CG2 
12471 C  CD1 . ILE D 436 ? 0.3051 0.6698 0.7750 0.0538  0.0941  0.2325  437 ILE D CD1 
12472 N  N   . ASN D 437 ? 0.3450 0.6682 0.6849 0.0759  0.1027  0.1955  438 ASN D N   
12473 C  CA  . ASN D 437 ? 0.3726 0.6999 0.6977 0.0856  0.1071  0.1968  438 ASN D CA  
12474 C  C   . ASN D 437 ? 0.4000 0.7102 0.6939 0.0885  0.1052  0.1837  438 ASN D C   
12475 O  O   . ASN D 437 ? 0.4189 0.7296 0.6977 0.0972  0.1087  0.1837  438 ASN D O   
12476 C  CB  . ASN D 437 ? 0.4308 0.7700 0.7535 0.0959  0.1183  0.2094  438 ASN D CB  
12477 C  CG  . ASN D 437 ? 0.4487 0.8096 0.8038 0.0965  0.1222  0.2257  438 ASN D CG  
12478 O  OD1 . ASN D 437 ? 0.4627 0.8308 0.8390 0.0917  0.1163  0.2268  438 ASN D OD1 
12479 N  ND2 . ASN D 437 ? 0.4697 0.8418 0.8300 0.1030  0.1321  0.2391  438 ASN D ND2 
12480 N  N   . ASN D 438 ? 0.3945 0.6897 0.6801 0.0818  0.1001  0.1734  439 ASN D N   
12481 C  CA  . ASN D 438 ? 0.4409 0.7202 0.7012 0.0838  0.0987  0.1628  439 ASN D CA  
12482 C  C   . ASN D 438 ? 0.4379 0.7178 0.6924 0.0876  0.0963  0.1601  439 ASN D C   
12483 O  O   . ASN D 438 ? 0.4658 0.7494 0.7322 0.0838  0.0902  0.1586  439 ASN D O   
12484 C  CB  . ASN D 438 ? 0.3166 0.5833 0.5748 0.0758  0.0936  0.1541  439 ASN D CB  
12485 C  CG  . ASN D 438 ? 0.4290 0.6801 0.6646 0.0776  0.0937  0.1456  439 ASN D CG  
12486 O  OD1 . ASN D 438 ? 0.3570 0.6040 0.5839 0.0799  0.0918  0.1418  439 ASN D OD1 
12487 N  ND2 . ASN D 438 ? 0.3788 0.6212 0.6066 0.0766  0.0958  0.1433  439 ASN D ND2 
12488 N  N   . PRO D 439 ? 0.4486 0.7242 0.6844 0.0958  0.1000  0.1590  440 PRO D N   
12489 C  CA  . PRO D 439 ? 0.3843 0.6610 0.6136 0.1010  0.0987  0.1578  440 PRO D CA  
12490 C  C   . PRO D 439 ? 0.4181 0.6831 0.6392 0.0973  0.0931  0.1492  440 PRO D C   
12491 O  O   . PRO D 439 ? 0.4368 0.7060 0.6607 0.0989  0.0896  0.1487  440 PRO D O   
12492 C  CB  . PRO D 439 ? 0.3858 0.6573 0.5960 0.1108  0.1037  0.1577  440 PRO D CB  
12493 C  CG  . PRO D 439 ? 0.4103 0.6710 0.6122 0.1087  0.1046  0.1541  440 PRO D CG  
12494 C  CD  . PRO D 439 ? 0.4079 0.6764 0.6278 0.1014  0.1046  0.1584  440 PRO D CD  
12495 N  N   . GLU D 440 ? 0.3751 0.6264 0.5862 0.0936  0.0927  0.1431  441 GLU D N   
12496 C  CA  . GLU D 440 ? 0.4243 0.6647 0.6258 0.0919  0.0893  0.1366  441 GLU D CA  
12497 C  C   . GLU D 440 ? 0.4042 0.6465 0.6159 0.0862  0.0832  0.1334  441 GLU D C   
12498 O  O   . GLU D 440 ? 0.5162 0.7566 0.7234 0.0881  0.0791  0.1299  441 GLU D O   
12499 C  CB  . GLU D 440 ? 0.4303 0.6560 0.6190 0.0909  0.0919  0.1328  441 GLU D CB  
12500 C  CG  . GLU D 440 ? 0.4020 0.6231 0.5806 0.0971  0.0954  0.1339  441 GLU D CG  
12501 C  CD  . GLU D 440 ? 0.4004 0.6246 0.5729 0.1045  0.0957  0.1356  441 GLU D CD  
12502 O  OE1 . GLU D 440 ? 0.4053 0.6271 0.5743 0.1050  0.0938  0.1341  441 GLU D OE1 
12503 O  OE2 . GLU D 440 ? 0.3556 0.5845 0.5256 0.1111  0.0979  0.1386  441 GLU D OE2 
12504 N  N   . VAL D 441 ? 0.4166 0.6620 0.6414 0.0803  0.0821  0.1343  442 VAL D N   
12505 C  CA  . VAL D 441 ? 0.3978 0.6423 0.6317 0.0754  0.0752  0.1298  442 VAL D CA  
12506 C  C   . VAL D 441 ? 0.3915 0.6491 0.6505 0.0718  0.0705  0.1343  442 VAL D C   
12507 O  O   . VAL D 441 ? 0.3766 0.6417 0.6473 0.0701  0.0747  0.1415  442 VAL D O   
12508 C  CB  . VAL D 441 ? 0.3851 0.6197 0.6148 0.0709  0.0764  0.1260  442 VAL D CB  
12509 C  CG1 . VAL D 441 ? 0.4137 0.6434 0.6437 0.0693  0.0692  0.1190  442 VAL D CG1 
12510 C  CG2 . VAL D 441 ? 0.3750 0.5988 0.5865 0.0736  0.0826  0.1248  442 VAL D CG2 
12511 N  N   . GLU D 442 ? 0.3844 0.6445 0.6525 0.0712  0.0613  0.1305  443 GLU D N   
12512 C  CA  . GLU D 442 ? 0.4589 0.7303 0.7557 0.0667  0.0547  0.1344  443 GLU D CA  
12513 C  C   . GLU D 442 ? 0.4733 0.7384 0.7789 0.0603  0.0499  0.1302  443 GLU D C   
12514 O  O   . GLU D 442 ? 0.4601 0.7149 0.7555 0.0608  0.0435  0.1206  443 GLU D O   
12515 C  CB  . GLU D 442 ? 0.5354 0.8121 0.8414 0.0691  0.0446  0.1315  443 GLU D CB  
12516 C  CG  . GLU D 442 ? 0.6385 0.9262 0.9460 0.0744  0.0486  0.1384  443 GLU D CG  
12517 C  CD  . GLU D 442 ? 0.7222 1.0239 1.0478 0.0734  0.0568  0.1513  443 GLU D CD  
12518 O  OE1 . GLU D 442 ? 0.7379 1.0449 1.0852 0.0675  0.0561  0.1563  443 GLU D OE1 
12519 O  OE2 . GLU D 442 ? 0.7835 1.0911 1.1012 0.0796  0.0642  0.1569  443 GLU D OE2 
12520 N  N   . VAL D 443 ? 0.4459 0.7178 0.7698 0.0556  0.0533  0.1380  444 VAL D N   
12521 C  CA  . VAL D 443 ? 0.4472 0.7134 0.7805 0.0496  0.0498  0.1353  444 VAL D CA  
12522 C  C   . VAL D 443 ? 0.4544 0.7317 0.8230 0.0441  0.0442  0.1427  444 VAL D C   
12523 O  O   . VAL D 443 ? 0.4852 0.7760 0.8694 0.0444  0.0505  0.1550  444 VAL D O   
12524 C  CB  . VAL D 443 ? 0.4454 0.7066 0.7660 0.0490  0.0601  0.1381  444 VAL D CB  
12525 C  CG1 . VAL D 443 ? 0.4211 0.6764 0.7515 0.0430  0.0564  0.1354  444 VAL D CG1 
12526 C  CG2 . VAL D 443 ? 0.4435 0.6937 0.7340 0.0537  0.0651  0.1320  444 VAL D CG2 
12527 N  N   . ASP D 444 ? 0.4851 0.7569 0.8674 0.0398  0.0324  0.1358  445 ASP D N   
12528 C  CA  . ASP D 444 ? 0.5172 0.7975 0.9369 0.0335  0.0260  0.1429  445 ASP D CA  
12529 C  C   . ASP D 444 ? 0.4304 0.7068 0.8538 0.0289  0.0313  0.1465  445 ASP D C   
12530 O  O   . ASP D 444 ? 0.3542 0.6176 0.7668 0.0276  0.0269  0.1366  445 ASP D O   
12531 C  CB  . ASP D 444 ? 0.5930 0.8684 1.0281 0.0317  0.0079  0.1325  445 ASP D CB  
12532 C  CG  . ASP D 444 ? 0.6752 0.9592 1.1545 0.0245  -0.0004 0.1404  445 ASP D CG  
12533 O  OD1 . ASP D 444 ? 0.6876 0.9866 1.1883 0.0223  0.0085  0.1564  445 ASP D OD1 
12534 O  OD2 . ASP D 444 ? 0.7102 0.9861 1.2036 0.0218  -0.0161 0.1309  445 ASP D OD2 
12535 N  N   . ILE D 445 ? 0.4359 0.7242 0.8742 0.0277  0.0412  0.1613  446 ILE D N   
12536 C  CA  . ILE D 445 ? 0.4600 0.7455 0.8983 0.0251  0.0481  0.1662  446 ILE D CA  
12537 C  C   . ILE D 445 ? 0.3555 0.6402 0.8260 0.0176  0.0387  0.1679  446 ILE D C   
12538 O  O   . ILE D 445 ? 0.4107 0.6910 0.8831 0.0148  0.0418  0.1701  446 ILE D O   
12539 C  CB  . ILE D 445 ? 0.3839 0.6822 0.8227 0.0291  0.0626  0.1817  446 ILE D CB  
12540 C  CG1 . ILE D 445 ? 0.3441 0.6604 0.8202 0.0274  0.0629  0.1971  446 ILE D CG1 
12541 C  CG2 . ILE D 445 ? 0.2973 0.5950 0.7052 0.0370  0.0702  0.1790  446 ILE D CG2 
12542 C  CD1 . ILE D 445 ? 0.2932 0.6233 0.7709 0.0330  0.0779  0.2142  446 ILE D CD1 
12543 N  N   . THR D 446 ? 0.3455 0.6340 0.8423 0.0146  0.0262  0.1666  447 THR D N   
12544 C  CA  . THR D 446 ? 0.3762 0.6625 0.9072 0.0074  0.0143  0.1669  447 THR D CA  
12545 C  C   . THR D 446 ? 0.4333 0.7015 0.9516 0.0073  -0.0004 0.1475  447 THR D C   
12546 O  O   . THR D 446 ? 0.4301 0.6929 0.9735 0.0025  -0.0136 0.1436  447 THR D O   
12547 C  CB  . THR D 446 ? 0.3303 0.6308 0.9033 0.0040  0.0066  0.1767  447 THR D CB  
12548 O  OG1 . THR D 446 ? 0.3319 0.6316 0.8958 0.0079  -0.0021 0.1668  447 THR D OG1 
12549 C  CG2 . THR D 446 ? 0.3628 0.6829 0.9511 0.0053  0.0224  0.1982  447 THR D CG2 
12550 N  N   . LYS D 447 ? 0.3945 0.6533 0.8741 0.0136  0.0021  0.1356  448 LYS D N   
12551 C  CA  . LYS D 447 ? 0.4418 0.6842 0.9038 0.0163  -0.0095 0.1179  448 LYS D CA  
12552 C  C   . LYS D 447 ? 0.4089 0.6407 0.8379 0.0192  0.0002  0.1125  448 LYS D C   
12553 O  O   . LYS D 447 ? 0.4811 0.7072 0.8790 0.0256  0.0040  0.1051  448 LYS D O   
12554 C  CB  . LYS D 447 ? 0.3423 0.5830 0.7901 0.0228  -0.0176 0.1080  448 LYS D CB  
12555 N  N   . PRO D 448 ? 0.3793 0.6088 0.8169 0.0147  0.0044  0.1172  449 PRO D N   
12556 C  CA  . PRO D 448 ? 0.3747 0.5950 0.7850 0.0170  0.0129  0.1128  449 PRO D CA  
12557 C  C   . PRO D 448 ? 0.3878 0.5934 0.7820 0.0211  0.0035  0.0969  449 PRO D C   
12558 O  O   . PRO D 448 ? 0.4085 0.6087 0.8192 0.0201  -0.0109 0.0899  449 PRO D O   
12559 C  CB  . PRO D 448 ? 0.3643 0.5876 0.7937 0.0111  0.0178  0.1229  449 PRO D CB  
12560 C  CG  . PRO D 448 ? 0.3607 0.5880 0.8279 0.0057  0.0059  0.1265  449 PRO D CG  
12561 C  CD  . PRO D 448 ? 0.3367 0.5722 0.8118 0.0074  0.0009  0.1273  449 PRO D CD  
12562 N  N   . ASP D 449 ? 0.4072 0.6063 0.7702 0.0264  0.0114  0.0916  450 ASP D N   
12563 C  CA  . ASP D 449 ? 0.4603 0.6465 0.8054 0.0321  0.0057  0.0785  450 ASP D CA  
12564 C  C   . ASP D 449 ? 0.4584 0.6383 0.8162 0.0280  0.0024  0.0772  450 ASP D C   
12565 O  O   . ASP D 449 ? 0.4534 0.6352 0.8117 0.0243  0.0125  0.0845  450 ASP D O   
12566 C  CB  . ASP D 449 ? 0.5491 0.7320 0.8624 0.0382  0.0173  0.0769  450 ASP D CB  
12567 C  CG  . ASP D 449 ? 0.6085 0.7799 0.9032 0.0453  0.0143  0.0659  450 ASP D CG  
12568 O  OD1 . ASP D 449 ? 0.6364 0.8032 0.9186 0.0533  0.0065  0.0569  450 ASP D OD1 
12569 O  OD2 . ASP D 449 ? 0.6356 0.8029 0.9273 0.0439  0.0199  0.0665  450 ASP D OD2 
12570 N  N   . MET D 450 ? 0.4538 0.6257 0.8219 0.0295  -0.0127 0.0674  451 MET D N   
12571 C  CA  . MET D 450 ? 0.4989 0.6648 0.8848 0.0252  -0.0182 0.0664  451 MET D CA  
12572 C  C   . MET D 450 ? 0.4677 0.6248 0.8319 0.0292  -0.0115 0.0613  451 MET D C   
12573 O  O   . MET D 450 ? 0.4501 0.6042 0.8266 0.0249  -0.0111 0.0639  451 MET D O   
12574 C  CB  . MET D 450 ? 0.5160 0.6743 0.9205 0.0262  -0.0386 0.0561  451 MET D CB  
12575 C  CG  . MET D 450 ? 0.5341 0.7008 0.9795 0.0169  -0.0457 0.0659  451 MET D CG  
12576 S  SD  . MET D 450 ? 1.3338 1.5047 1.8042 0.0071  -0.0370 0.0806  451 MET D SD  
12577 C  CE  . MET D 450 ? 0.6291 0.8180 1.1357 -0.0009 -0.0341 0.0991  451 MET D CE  
12578 N  N   . THR D 451 ? 0.4882 0.6418 0.8219 0.0378  -0.0060 0.0553  452 THR D N   
12579 C  CA  . THR D 451 ? 0.5013 0.6492 0.8158 0.0419  0.0028  0.0528  452 THR D CA  
12580 C  C   . THR D 451 ? 0.5162 0.6705 0.8368 0.0344  0.0159  0.0648  452 THR D C   
12581 O  O   . THR D 451 ? 0.4940 0.6446 0.8194 0.0322  0.0179  0.0655  452 THR D O   
12582 C  CB  . THR D 451 ? 0.5499 0.6958 0.8334 0.0522  0.0093  0.0483  452 THR D CB  
12583 O  OG1 . THR D 451 ? 0.5834 0.7225 0.8575 0.0617  -0.0035 0.0362  452 THR D OG1 
12584 C  CG2 . THR D 451 ? 0.5728 0.7149 0.8410 0.0559  0.0196  0.0483  452 THR D CG2 
12585 N  N   . ILE D 452 ? 0.4274 0.5910 0.7472 0.0316  0.0240  0.0737  453 ILE D N   
12586 C  CA  . ILE D 452 ? 0.4499 0.6195 0.7726 0.0265  0.0354  0.0842  453 ILE D CA  
12587 C  C   . ILE D 452 ? 0.4127 0.5854 0.7612 0.0193  0.0325  0.0912  453 ILE D C   
12588 O  O   . ILE D 452 ? 0.3623 0.5354 0.7127 0.0167  0.0389  0.0964  453 ILE D O   
12589 C  CB  . ILE D 452 ? 0.3260 0.5040 0.6418 0.0266  0.0428  0.0911  453 ILE D CB  
12590 C  CG1 . ILE D 452 ? 0.4157 0.5900 0.7067 0.0336  0.0474  0.0859  453 ILE D CG1 
12591 C  CG2 . ILE D 452 ? 0.3146 0.4985 0.6341 0.0228  0.0523  0.1012  453 ILE D CG2 
12592 C  CD1 . ILE D 452 ? 0.4320 0.6118 0.7136 0.0340  0.0566  0.0924  453 ILE D CD1 
12593 N  N   . ARG D 453 ? 0.3314 0.5062 0.7012 0.0164  0.0224  0.0918  454 ARG D N   
12594 C  CA  . ARG D 453 ? 0.3283 0.5059 0.7267 0.0098  0.0190  0.0995  454 ARG D CA  
12595 C  C   . ARG D 453 ? 0.5387 0.7060 0.9388 0.0096  0.0153  0.0938  454 ARG D C   
12596 O  O   . ARG D 453 ? 0.6265 0.7954 1.0357 0.0059  0.0205  0.1015  454 ARG D O   
12597 C  CB  . ARG D 453 ? 0.3334 0.5140 0.7578 0.0069  0.0068  0.1001  454 ARG D CB  
12598 N  N   . GLN D 454 ? 0.4881 0.6447 0.8778 0.0149  0.0062  0.0801  455 GLN D N   
12599 C  CA  . GLN D 454 ? 0.5746 0.7206 0.9632 0.0168  0.0021  0.0729  455 GLN D CA  
12600 C  C   . GLN D 454 ? 0.4911 0.6376 0.8634 0.0177  0.0153  0.0764  455 GLN D C   
12601 O  O   . GLN D 454 ? 0.5249 0.6684 0.9063 0.0150  0.0162  0.0789  455 GLN D O   
12602 C  CB  . GLN D 454 ? 0.6534 0.7884 1.0268 0.0257  -0.0086 0.0570  455 GLN D CB  
12603 C  CG  . GLN D 454 ? 0.7566 0.8870 1.1500 0.0252  -0.0265 0.0504  455 GLN D CG  
12604 C  CD  . GLN D 454 ? 0.8558 0.9752 1.2291 0.0367  -0.0376 0.0336  455 GLN D CD  
12605 O  OE1 . GLN D 454 ? 0.9033 1.0201 1.2469 0.0455  -0.0299 0.0286  455 GLN D OE1 
12606 N  NE2 . GLN D 454 ? 0.8907 1.0037 1.2809 0.0376  -0.0562 0.0252  455 GLN D NE2 
12607 N  N   . GLN D 455 ? 0.4294 0.5794 0.7795 0.0214  0.0250  0.0769  456 GLN D N   
12608 C  CA  . GLN D 455 ? 0.4358 0.5865 0.7731 0.0222  0.0365  0.0802  456 GLN D CA  
12609 C  C   . GLN D 455 ? 0.3669 0.5246 0.7170 0.0158  0.0426  0.0920  456 GLN D C   
12610 O  O   . GLN D 455 ? 0.4258 0.5820 0.7750 0.0151  0.0472  0.0942  456 GLN D O   
12611 C  CB  . GLN D 455 ? 0.4065 0.5596 0.7217 0.0271  0.0445  0.0792  456 GLN D CB  
12612 C  CG  . GLN D 455 ? 0.4361 0.5829 0.7350 0.0357  0.0405  0.0688  456 GLN D CG  
12613 C  CD  . GLN D 455 ? 0.4582 0.5961 0.7557 0.0402  0.0356  0.0608  456 GLN D CD  
12614 O  OE1 . GLN D 455 ? 0.4667 0.6034 0.7613 0.0405  0.0423  0.0625  456 GLN D OE1 
12615 N  NE2 . GLN D 455 ? 0.4901 0.6214 0.7901 0.0442  0.0231  0.0516  456 GLN D NE2 
12616 N  N   . ILE D 456 ? 0.3177 0.4835 0.6793 0.0124  0.0426  0.1000  457 ILE D N   
12617 C  CA  . ILE D 456 ? 0.3289 0.5023 0.7026 0.0084  0.0482  0.1122  457 ILE D CA  
12618 C  C   . ILE D 456 ? 0.3118 0.4816 0.7053 0.0048  0.0434  0.1148  457 ILE D C   
12619 O  O   . ILE D 456 ? 0.3335 0.5045 0.7283 0.0040  0.0488  0.1209  457 ILE D O   
12620 C  CB  . ILE D 456 ? 0.3060 0.4898 0.6902 0.0068  0.0492  0.1212  457 ILE D CB  
12621 C  CG1 . ILE D 456 ? 0.4021 0.5898 0.7658 0.0107  0.0558  0.1206  457 ILE D CG1 
12622 C  CG2 . ILE D 456 ? 0.3012 0.4931 0.7013 0.0043  0.0542  0.1351  457 ILE D CG2 
12623 C  CD1 . ILE D 456 ? 0.3697 0.5672 0.7416 0.0105  0.0558  0.1272  457 ILE D CD1 
12624 N  N   . MET D 457 ? 0.3197 0.4843 0.7287 0.0033  0.0323  0.1097  458 MET D N   
12625 C  CA  . MET D 457 ? 0.3819 0.5409 0.8113 0.0000  0.0259  0.1107  458 MET D CA  
12626 C  C   . MET D 457 ? 0.3645 0.5155 0.7803 0.0028  0.0286  0.1047  458 MET D C   
12627 O  O   . MET D 457 ? 0.3288 0.4797 0.7542 0.0005  0.0311  0.1112  458 MET D O   
12628 C  CB  . MET D 457 ? 0.3989 0.5508 0.8448 -0.0008 0.0109  0.1026  458 MET D CB  
12629 C  CG  . MET D 457 ? 0.3844 0.5299 0.8566 -0.0048 0.0024  0.1043  458 MET D CG  
12630 S  SD  . MET D 457 ? 0.6210 0.7786 1.1237 -0.0119 0.0088  0.1260  458 MET D SD  
12631 C  CE  . MET D 457 ? 0.5561 0.7178 1.0911 -0.0165 -0.0032 0.1290  458 MET D CE  
12632 N  N   . GLN D 458 ? 0.4042 0.5494 0.7981 0.0085  0.0287  0.0934  459 GLN D N   
12633 C  CA  . GLN D 458 ? 0.4214 0.5606 0.8022 0.0121  0.0325  0.0882  459 GLN D CA  
12634 C  C   . GLN D 458 ? 0.3883 0.5338 0.7649 0.0103  0.0433  0.0973  459 GLN D C   
12635 O  O   . GLN D 458 ? 0.3934 0.5359 0.7739 0.0099  0.0445  0.0986  459 GLN D O   
12636 C  CB  . GLN D 458 ? 0.3980 0.5332 0.7556 0.0195  0.0337  0.0778  459 GLN D CB  
12637 C  CG  . GLN D 458 ? 0.4822 0.6086 0.8392 0.0245  0.0218  0.0661  459 GLN D CG  
12638 C  CD  . GLN D 458 ? 0.5905 0.7075 0.9594 0.0250  0.0134  0.0610  459 GLN D CD  
12639 O  OE1 . GLN D 458 ? 0.6936 0.8069 1.0545 0.0285  0.0177  0.0587  459 GLN D OE1 
12640 N  NE2 . GLN D 458 ? 0.5909 0.7038 0.9812 0.0215  0.0009  0.0596  459 GLN D NE2 
12641 N  N   . LEU D 459 ? 0.4008 0.5543 0.7693 0.0101  0.0500  0.1029  460 LEU D N   
12642 C  CA  . LEU D 459 ? 0.4161 0.5749 0.7796 0.0097  0.0583  0.1106  460 LEU D CA  
12643 C  C   . LEU D 459 ? 0.4122 0.5739 0.7926 0.0066  0.0582  0.1202  460 LEU D C   
12644 O  O   . LEU D 459 ? 0.4461 0.6068 0.8250 0.0073  0.0612  0.1226  460 LEU D O   
12645 C  CB  . LEU D 459 ? 0.4091 0.5752 0.7626 0.0107  0.0636  0.1146  460 LEU D CB  
12646 C  CG  . LEU D 459 ? 0.4430 0.6072 0.7790 0.0142  0.0658  0.1075  460 LEU D CG  
12647 C  CD1 . LEU D 459 ? 0.4612 0.6321 0.7896 0.0151  0.0703  0.1122  460 LEU D CD1 
12648 C  CD2 . LEU D 459 ? 0.4204 0.5802 0.7470 0.0165  0.0695  0.1033  460 LEU D CD2 
12649 N  N   . LYS D 460 ? 0.4405 0.6061 0.8384 0.0036  0.0546  0.1266  461 LYS D N   
12650 C  CA  . LYS D 460 ? 0.4323 0.6016 0.8490 0.0011  0.0554  0.1384  461 LYS D CA  
12651 C  C   . LYS D 460 ? 0.4038 0.5645 0.8299 -0.0001 0.0507  0.1352  461 LYS D C   
12652 O  O   . LYS D 460 ? 0.3508 0.5128 0.7797 0.0004  0.0546  0.1423  461 LYS D O   
12653 C  CB  . LYS D 460 ? 0.4948 0.6700 0.9338 -0.0024 0.0517  0.1463  461 LYS D CB  
12654 C  CG  . LYS D 460 ? 0.5637 0.7497 0.9966 -0.0007 0.0575  0.1527  461 LYS D CG  
12655 C  CD  . LYS D 460 ? 0.6639 0.8578 1.1239 -0.0041 0.0550  0.1636  461 LYS D CD  
12656 C  CE  . LYS D 460 ? 0.7158 0.9233 1.1719 -0.0007 0.0645  0.1761  461 LYS D CE  
12657 N  NZ  . LYS D 460 ? 0.7571 0.9746 1.2434 -0.0037 0.0638  0.1898  461 LYS D NZ  
12658 N  N   . ILE D 461 ? 0.4035 0.5550 0.8332 -0.0005 0.0420  0.1242  462 ILE D N   
12659 C  CA  . ILE D 461 ? 0.3231 0.4649 0.7606 -0.0006 0.0365  0.1194  462 ILE D CA  
12660 C  C   . ILE D 461 ? 0.4286 0.5687 0.8497 0.0028  0.0429  0.1169  462 ILE D C   
12661 O  O   . ILE D 461 ? 0.4058 0.5448 0.8349 0.0022  0.0441  0.1223  462 ILE D O   
12662 C  CB  . ILE D 461 ? 0.3714 0.5027 0.8089 0.0014  0.0257  0.1053  462 ILE D CB  
12663 C  CG1 . ILE D 461 ? 0.4372 0.5693 0.8950 -0.0023 0.0166  0.1070  462 ILE D CG1 
12664 C  CG2 . ILE D 461 ? 0.3622 0.4828 0.8054 0.0029  0.0200  0.0994  462 ILE D CG2 
12665 C  CD1 . ILE D 461 ? 0.4862 0.6085 0.9392 0.0015  0.0050  0.0917  462 ILE D CD1 
12666 N  N   . MET D 462 ? 0.3612 0.5016 0.7615 0.0065  0.0470  0.1097  463 MET D N   
12667 C  CA  . MET D 462 ? 0.3354 0.4748 0.7232 0.0095  0.0525  0.1074  463 MET D CA  
12668 C  C   . MET D 462 ? 0.3594 0.5054 0.7481 0.0087  0.0583  0.1177  463 MET D C   
12669 O  O   . MET D 462 ? 0.3094 0.4536 0.6988 0.0098  0.0596  0.1187  463 MET D O   
12670 C  CB  . MET D 462 ? 0.3659 0.5061 0.7349 0.0132  0.0567  0.1006  463 MET D CB  
12671 C  CG  . MET D 462 ? 0.3131 0.4523 0.6739 0.0162  0.0616  0.0983  463 MET D CG  
12672 S  SD  . MET D 462 ? 0.4594 0.5898 0.8257 0.0192  0.0572  0.0914  463 MET D SD  
12673 C  CE  . MET D 462 ? 0.3239 0.4571 0.6944 0.0185  0.0615  0.0973  463 MET D CE  
12674 N  N   . THR D 463 ? 0.3459 0.4996 0.7336 0.0078  0.0615  0.1253  464 THR D N   
12675 C  CA  . THR D 463 ? 0.3619 0.5219 0.7474 0.0095  0.0666  0.1349  464 THR D CA  
12676 C  C   . THR D 463 ? 0.3969 0.5566 0.7987 0.0084  0.0653  0.1435  464 THR D C   
12677 O  O   . THR D 463 ? 0.3574 0.5183 0.7558 0.0112  0.0679  0.1480  464 THR D O   
12678 C  CB  . THR D 463 ? 0.3767 0.5453 0.7581 0.0105  0.0703  0.1418  464 THR D CB  
12679 O  OG1 . THR D 463 ? 0.3891 0.5574 0.7561 0.0115  0.0713  0.1341  464 THR D OG1 
12680 C  CG2 . THR D 463 ? 0.3006 0.4751 0.6753 0.0150  0.0752  0.1506  464 THR D CG2 
12681 N  N   . ASN D 464 ? 0.3754 0.5330 0.7957 0.0046  0.0604  0.1458  465 ASN D N   
12682 C  CA  . ASN D 464 ? 0.4363 0.5923 0.8757 0.0031  0.0585  0.1542  465 ASN D CA  
12683 C  C   . ASN D 464 ? 0.4060 0.5534 0.8433 0.0043  0.0559  0.1473  465 ASN D C   
12684 O  O   . ASN D 464 ? 0.3181 0.4661 0.7596 0.0058  0.0579  0.1545  465 ASN D O   
12685 C  CB  . ASN D 464 ? 0.5403 0.6941 1.0038 -0.0018 0.0516  0.1567  465 ASN D CB  
12686 C  CG  . ASN D 464 ? 0.6647 0.8292 1.1371 -0.0030 0.0551  0.1681  465 ASN D CG  
12687 O  OD1 . ASN D 464 ? 0.6866 0.8605 1.1498 0.0007  0.0635  0.1777  465 ASN D OD1 
12688 N  ND2 . ASN D 464 ? 0.6675 0.8306 1.1582 -0.0073 0.0481  0.1670  465 ASN D ND2 
12689 N  N   . ARG D 465 ? 0.3553 0.4952 0.7853 0.0047  0.0518  0.1338  466 ARG D N   
12690 C  CA  . ARG D 465 ? 0.3597 0.4924 0.7868 0.0069  0.0501  0.1268  466 ARG D CA  
12691 C  C   . ARG D 465 ? 0.4316 0.5686 0.8467 0.0101  0.0563  0.1294  466 ARG D C   
12692 O  O   . ARG D 465 ? 0.4543 0.5890 0.8742 0.0114  0.0559  0.1319  466 ARG D O   
12693 C  CB  . ARG D 465 ? 0.4089 0.5350 0.8265 0.0092  0.0468  0.1128  466 ARG D CB  
12694 C  CG  . ARG D 465 ? 0.5349 0.6544 0.9630 0.0079  0.0380  0.1073  466 ARG D CG  
12695 C  CD  . ARG D 465 ? 0.5968 0.7072 1.0158 0.0132  0.0335  0.0934  466 ARG D CD  
12696 N  NE  . ARG D 465 ? 0.7031 0.8068 1.1273 0.0137  0.0238  0.0857  466 ARG D NE  
12697 C  CZ  . ARG D 465 ? 0.7651 0.8607 1.2090 0.0117  0.0133  0.0845  466 ARG D CZ  
12698 N  NH1 . ARG D 465 ? 0.7915 0.8850 1.2515 0.0088  0.0125  0.0917  466 ARG D NH1 
12699 N  NH2 . ARG D 465 ? 0.7863 0.8754 1.2346 0.0129  0.0027  0.0761  466 ARG D NH2 
12700 N  N   . LEU D 466 ? 0.4928 0.6355 0.8931 0.0116  0.0608  0.1285  467 LEU D N   
12701 C  CA  . LEU D 466 ? 0.5166 0.6628 0.9065 0.0148  0.0645  0.1297  467 LEU D CA  
12702 C  C   . LEU D 466 ? 0.4899 0.6406 0.8829 0.0169  0.0661  0.1410  467 LEU D C   
12703 O  O   . LEU D 466 ? 0.5390 0.6891 0.9301 0.0198  0.0660  0.1420  467 LEU D O   
12704 C  CB  . LEU D 466 ? 0.3039 0.4541 0.6796 0.0159  0.0676  0.1264  467 LEU D CB  
12705 C  CG  . LEU D 466 ? 0.3107 0.4576 0.6804 0.0162  0.0681  0.1165  467 LEU D CG  
12706 C  CD1 . LEU D 466 ? 0.2997 0.4501 0.6590 0.0162  0.0706  0.1150  467 LEU D CD1 
12707 C  CD2 . LEU D 466 ? 0.3701 0.5161 0.7386 0.0184  0.0690  0.1136  467 LEU D CD2 
12708 N  N   . ARG D 467 ? 0.5156 0.6714 0.9133 0.0162  0.0678  0.1500  468 ARG D N   
12709 C  CA  . ARG D 467 ? 0.5578 0.7194 0.9568 0.0202  0.0710  0.1628  468 ARG D CA  
12710 C  C   . ARG D 467 ? 0.5717 0.7296 0.9860 0.0196  0.0691  0.1686  468 ARG D C   
12711 O  O   . ARG D 467 ? 0.5317 0.6923 0.9434 0.0246  0.0712  0.1765  468 ARG D O   
12712 C  CB  . ARG D 467 ? 0.6089 0.7783 1.0116 0.0202  0.0746  0.1726  468 ARG D CB  
12713 C  CG  . ARG D 467 ? 0.7001 0.8750 1.0840 0.0244  0.0778  0.1708  468 ARG D CG  
12714 C  CD  . ARG D 467 ? 0.7634 0.9472 1.1512 0.0257  0.0822  0.1816  468 ARG D CD  
12715 N  NE  . ARG D 467 ? 0.8425 1.0337 1.2196 0.0349  0.0874  0.1922  468 ARG D NE  
12716 C  CZ  . ARG D 467 ? 0.8971 1.0970 1.2674 0.0399  0.0924  0.1997  468 ARG D CZ  
12717 N  NH1 . ARG D 467 ? 0.8911 1.0936 1.2659 0.0356  0.0927  0.1978  468 ARG D NH1 
12718 N  NH2 . ARG D 467 ? 0.9216 1.1278 1.2796 0.0506  0.0971  0.2089  468 ARG D NH2 
12719 N  N   . SER D 468 ? 0.5834 0.7345 1.0129 0.0144  0.0645  0.1644  469 SER D N   
12720 C  CA  . SER D 468 ? 0.5915 0.7369 1.0360 0.0138  0.0614  0.1679  469 SER D CA  
12721 C  C   . SER D 468 ? 0.5776 0.7181 1.0127 0.0167  0.0601  0.1594  469 SER D C   
12722 O  O   . SER D 468 ? 0.6210 0.7597 1.0614 0.0190  0.0596  0.1643  469 SER D O   
12723 C  CB  . SER D 468 ? 0.6211 0.7588 1.0847 0.0082  0.0548  0.1643  469 SER D CB  
12724 O  OG  . SER D 468 ? 0.6713 0.8135 1.1535 0.0053  0.0553  0.1769  469 SER D OG  
12725 N  N   . ALA D 469 ? 0.5265 0.6657 0.9490 0.0168  0.0598  0.1475  470 ALA D N   
12726 C  CA  . ALA D 469 ? 0.4791 0.6152 0.8954 0.0195  0.0590  0.1399  470 ALA D CA  
12727 C  C   . ALA D 469 ? 0.4794 0.6207 0.8862 0.0242  0.0611  0.1444  470 ALA D C   
12728 O  O   . ALA D 469 ? 0.4858 0.6251 0.8929 0.0267  0.0595  0.1419  470 ALA D O   
12729 C  CB  . ALA D 469 ? 0.4572 0.5920 0.8647 0.0189  0.0594  0.1284  470 ALA D CB  
12730 N  N   . TYR D 470 ? 0.4337 0.5815 0.8318 0.0263  0.0639  0.1504  471 TYR D N   
12731 C  CA  . TYR D 470 ? 0.4807 0.6325 0.8672 0.0328  0.0643  0.1535  471 TYR D CA  
12732 C  C   . TYR D 470 ? 0.5476 0.6993 0.9395 0.0370  0.0639  0.1626  471 TYR D C   
12733 O  O   . TYR D 470 ? 0.5516 0.7031 0.9376 0.0421  0.0615  0.1612  471 TYR D O   
12734 C  CB  . TYR D 470 ? 0.4720 0.6302 0.8465 0.0360  0.0672  0.1581  471 TYR D CB  
12735 C  CG  . TYR D 470 ? 0.4452 0.6060 0.8043 0.0439  0.0655  0.1573  471 TYR D CG  
12736 C  CD1 . TYR D 470 ? 0.4494 0.6081 0.8017 0.0439  0.0620  0.1466  471 TYR D CD1 
12737 C  CD2 . TYR D 470 ? 0.4622 0.6272 0.8139 0.0524  0.0670  0.1674  471 TYR D CD2 
12738 C  CE1 . TYR D 470 ? 0.4733 0.6328 0.8133 0.0514  0.0580  0.1445  471 TYR D CE1 
12739 C  CE2 . TYR D 470 ? 0.4559 0.6218 0.7913 0.0615  0.0635  0.1651  471 TYR D CE2 
12740 C  CZ  . TYR D 470 ? 0.5125 0.6751 0.8428 0.0606  0.0581  0.1528  471 TYR D CZ  
12741 O  OH  . TYR D 470 ? 0.5216 0.6838 0.8376 0.0698  0.0523  0.1491  471 TYR D OH  
12742 N  N   . ASN D 471 ? 0.6734 0.8252 1.0784 0.0349  0.0657  0.1723  472 ASN D N   
12743 C  CA  . ASN D 471 ? 0.7719 0.9236 1.1843 0.0388  0.0662  0.1833  472 ASN D CA  
12744 C  C   . ASN D 471 ? 0.9019 1.0456 1.3254 0.0365  0.0619  0.1778  472 ASN D C   
12745 O  O   . ASN D 471 ? 0.9174 1.0601 1.3455 0.0404  0.0615  0.1848  472 ASN D O   
12746 C  CB  . ASN D 471 ? 0.7609 0.9161 1.1876 0.0371  0.0701  0.1977  472 ASN D CB  
12747 C  CG  . ASN D 471 ? 0.6982 0.8621 1.1155 0.0396  0.0751  0.2036  472 ASN D CG  
12748 O  OD1 . ASN D 471 ? 0.7495 0.9179 1.1470 0.0469  0.0766  0.2024  472 ASN D OD1 
12749 N  ND2 . ASN D 471 ? 0.6486 0.8146 1.0811 0.0342  0.0768  0.2096  472 ASN D ND2 
12750 N  N   . GLY D 472 ? 1.0532 1.1915 1.4800 0.0312  0.0591  0.1655  473 GLY D N   
12751 C  CA  . GLY D 472 ? 1.1164 1.2471 1.5524 0.0301  0.0553  0.1592  473 GLY D CA  
12752 C  C   . GLY D 472 ? 1.1031 1.2272 1.5578 0.0260  0.0527  0.1626  473 GLY D C   
12753 O  O   . GLY D 472 ? 1.1445 1.2646 1.6103 0.0274  0.0510  0.1686  473 GLY D O   
12754 N  N   . ASN D 473 ? 0.9957 1.1178 1.4548 0.0213  0.0515  0.1587  474 ASN D N   
12755 C  CA  . ASN D 473 ? 0.9426 1.0572 1.4215 0.0172  0.0467  0.1604  474 ASN D CA  
12756 C  C   . ASN D 473 ? 0.8830 0.9902 1.3614 0.0151  0.0415  0.1457  474 ASN D C   
12757 O  O   . ASN D 473 ? 0.8176 0.9281 1.2837 0.0146  0.0432  0.1391  474 ASN D O   
12758 C  CB  . ASN D 473 ? 0.9214 1.0417 1.4113 0.0143  0.0489  0.1736  474 ASN D CB  
12759 C  CG  . ASN D 473 ? 0.9075 1.0375 1.3916 0.0190  0.0559  0.1883  474 ASN D CG  
12760 O  OD1 . ASN D 473 ? 0.8829 1.0218 1.3575 0.0205  0.0609  0.1935  474 ASN D OD1 
12761 N  ND2 . ASN D 473 ? 0.9023 1.0304 1.3908 0.0227  0.0561  0.1950  474 ASN D ND2 
12762 C  C1  . NAG E .   ? 0.5266 0.6580 0.9758 -0.0022 0.0464  -0.0324 601 NAG A C1  
12763 C  C2  . NAG E .   ? 0.6318 0.7701 1.0917 -0.0042 0.0400  -0.0225 601 NAG A C2  
12764 C  C3  . NAG E .   ? 0.7355 0.8876 1.1939 -0.0150 0.0422  -0.0230 601 NAG A C3  
12765 C  C4  . NAG E .   ? 0.7731 0.9394 1.2304 -0.0253 0.0423  -0.0271 601 NAG A C4  
12766 C  C5  . NAG E .   ? 0.6936 0.8504 1.1431 -0.0200 0.0494  -0.0382 601 NAG A C5  
12767 C  C6  . NAG E .   ? 0.7038 0.8735 1.1540 -0.0297 0.0500  -0.0438 601 NAG A C6  
12768 C  C7  . NAG E .   ? 0.5987 0.7161 1.0644 0.0083  0.0349  -0.0152 601 NAG A C7  
12769 C  C8  . NAG E .   ? 0.6607 0.7877 1.1428 0.0073  0.0263  -0.0091 601 NAG A C8  
12770 N  N2  . NAG E .   ? 0.6066 0.7298 1.0628 0.0032  0.0409  -0.0211 601 NAG A N2  
12771 O  O3  . NAG E .   ? 0.7892 0.9479 1.2555 -0.0198 0.0338  -0.0110 601 NAG A O3  
12772 O  O4  . NAG E .   ? 0.8301 1.0017 1.2684 -0.0363 0.0452  -0.0301 601 NAG A O4  
12773 O  O5  . NAG E .   ? 0.6002 0.7461 1.0526 -0.0106 0.0462  -0.0352 601 NAG A O5  
12774 O  O6  . NAG E .   ? 0.7061 0.8875 1.1589 -0.0371 0.0389  -0.0337 601 NAG A O6  
12775 O  O7  . NAG E .   ? 0.6546 0.7596 1.1162 0.0129  0.0362  -0.0153 601 NAG A O7  
12776 CA CA  . CA  F .   ? 0.4381 0.4372 0.9191 0.0034  0.0524  -0.0592 602 CA  A CA  
12778 C  C1  . NAG H .   ? 0.6794 0.6812 1.2635 0.0670  0.1263  0.0266  601 NAG B C1  
12779 C  C2  . NAG H .   ? 0.6864 0.6892 1.2642 0.0696  0.1358  0.0326  601 NAG B C2  
12780 C  C3  . NAG H .   ? 0.7494 0.7498 1.3051 0.0814  0.1389  0.0280  601 NAG B C3  
12781 C  C4  . NAG H .   ? 0.7197 0.7213 1.2705 0.0933  0.1432  0.0235  601 NAG B C4  
12782 C  C5  . NAG H .   ? 0.7743 0.7740 1.3336 0.0887  0.1330  0.0177  601 NAG B C5  
12783 C  C6  . NAG H .   ? 0.8394 0.8401 1.3960 0.1002  0.1367  0.0129  601 NAG B C6  
12784 C  C7  . NAG H .   ? 0.7451 0.7474 1.3376 0.0546  0.1360  0.0429  601 NAG B C7  
12785 C  C8  . NAG H .   ? 0.7600 0.7664 1.3633 0.0599  0.1491  0.0501  601 NAG B C8  
12786 N  N2  . NAG H .   ? 0.7085 0.7094 1.2896 0.0593  0.1305  0.0352  601 NAG B N2  
12787 O  O3  . NAG H .   ? 0.7348 0.7368 1.2847 0.0854  0.1489  0.0347  601 NAG B O3  
12788 O  O4  . NAG H .   ? 0.6576 0.6553 1.1868 0.1053  0.1437  0.0170  601 NAG B O4  
12789 O  O5  . NAG H .   ? 0.7154 0.7186 1.2955 0.0779  0.1313  0.0232  601 NAG B O5  
12790 O  O6  . NAG H .   ? 0.8782 0.8854 1.4526 0.0992  0.1434  0.0184  601 NAG B O6  
12791 O  O7  . NAG H .   ? 0.7499 0.7499 1.3446 0.0467  0.1308  0.0441  601 NAG B O7  
12792 CA CA  . CA  I .   ? 0.8665 0.9591 1.5121 0.0559  0.0049  0.0037  602 CA  B CA  
12793 CA CA  . CA  J .   ? 0.3628 0.3577 0.9161 0.0053  0.0466  0.0078  603 CA  B CA  
12794 C  C1  . NAG K .   ? 0.8277 0.9937 1.2121 -0.1504 -0.0261 0.0904  601 NAG C C1  
12795 C  C2  . NAG K .   ? 0.8675 1.0340 1.2448 -0.1464 -0.0332 0.0931  601 NAG C C2  
12796 C  C3  . NAG K .   ? 0.9190 1.0690 1.2644 -0.1552 -0.0382 0.0893  601 NAG C C3  
12797 C  C4  . NAG K .   ? 0.9455 1.0936 1.2864 -0.1705 -0.0483 0.0894  601 NAG C C4  
12798 C  C5  . NAG K .   ? 0.9311 1.0786 1.2813 -0.1727 -0.0402 0.0862  601 NAG C C5  
12799 C  C6  . NAG K .   ? 0.9553 1.1018 1.3035 -0.1882 -0.0501 0.0863  601 NAG C C6  
12800 C  C7  . NAG K .   ? 0.8568 1.0332 1.2490 -0.1256 -0.0260 0.0964  601 NAG C C7  
12801 C  C8  . NAG K .   ? 0.8679 1.0565 1.2776 -0.1306 -0.0415 0.1038  601 NAG C C8  
12802 N  N2  . NAG K .   ? 0.8601 1.0264 1.2383 -0.1332 -0.0229 0.0920  601 NAG C N2  
12803 O  O3  . NAG K .   ? 0.9173 1.0686 1.2565 -0.1532 -0.0460 0.0930  601 NAG C O3  
12804 O  O4  . NAG K .   ? 0.9901 1.1210 1.2986 -0.1798 -0.0503 0.0838  601 NAG C O4  
12805 O  O5  . NAG K .   ? 0.8870 1.0517 1.2683 -0.1643 -0.0365 0.0910  601 NAG C O5  
12806 O  O6  . NAG K .   ? 0.9864 1.1235 1.3099 -0.1991 -0.0605 0.0851  601 NAG C O6  
12807 O  O7  . NAG K .   ? 0.8738 1.0492 1.2653 -0.1155 -0.0171 0.0948  601 NAG C O7  
12808 CA CA  . CA  L .   ? 0.8864 0.8773 0.9647 -0.2067 0.0248  0.1993  602 CA  C CA  
12809 CA CA  . CA  M .   ? 1.0039 1.2316 1.5349 -0.0359 0.0049  0.1632  603 CA  C CA  
12810 CA CA  . CA  N .   ? 0.6609 0.7755 0.8797 -0.0460 0.0733  0.0692  604 CA  C CA  
12811 C  C1  . NAG O .   ? 0.8402 1.0457 1.2694 0.1458  0.1722  0.1181  601 NAG D C1  
12812 C  C2  . NAG O .   ? 0.8836 1.0951 1.3015 0.1523  0.1830  0.1243  601 NAG D C2  
12813 C  C3  . NAG O .   ? 0.9529 1.1549 1.3367 0.1682  0.1831  0.1141  601 NAG D C3  
12814 C  C4  . NAG O .   ? 0.9983 1.2008 1.3764 0.1852  0.1872  0.1112  601 NAG D C4  
12815 C  C5  . NAG O .   ? 0.9806 1.1768 1.3734 0.1764  0.1760  0.1056  601 NAG D C5  
12816 C  C6  . NAG O .   ? 0.9863 1.1837 1.3769 0.1924  0.1801  0.1035  601 NAG D C6  
12817 C  C7  . NAG O .   ? 0.8138 1.0342 1.2488 0.1340  0.1869  0.1376  601 NAG D C7  
12818 C  C8  . NAG O .   ? 0.8183 1.0547 1.2670 0.1464  0.2040  0.1515  601 NAG D C8  
12819 N  N2  . NAG O .   ? 0.8589 1.0684 1.2804 0.1373  0.1779  0.1257  601 NAG D N2  
12820 O  O3  . NAG O .   ? 0.9921 1.2007 1.3644 0.1764  0.1943  0.1209  601 NAG D O3  
12821 O  O4  . NAG O .   ? 1.0383 1.2294 1.3835 0.2008  0.1840  0.0993  601 NAG D O4  
12822 O  O5  . NAG O .   ? 0.9237 1.1302 1.3479 0.1615  0.1770  0.1161  601 NAG D O5  
12823 O  O6  . NAG O .   ? 1.0230 1.2137 1.3830 0.2123  0.1825  0.0953  601 NAG D O6  
12824 O  O7  . NAG O .   ? 0.7976 1.0151 1.2347 0.1221  0.1816  0.1378  601 NAG D O7  
12825 CA CA  . CA  P .   ? 0.9540 1.2718 1.3118 0.0669  0.0727  0.1735  602 CA  D CA  
12826 CA CA  . CA  Q .   ? 0.9007 1.0345 1.1807 0.0392  0.0659  0.0994  603 CA  D CA  
# 
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   ALA 1   2   ?   ?   ?   A . n 
A 1 2   PRO 2   3   ?   ?   ?   A . n 
A 1 3   GLN 3   4   ?   ?   ?   A . n 
A 1 4   LEU 4   5   ?   ?   ?   A . n 
A 1 5   HIS 5   6   ?   ?   ?   A . n 
A 1 6   HIS 6   7   ?   ?   ?   A . n 
A 1 7   HIS 7   8   ?   ?   ?   A . n 
A 1 8   HIS 8   9   ?   ?   ?   A . n 
A 1 9   HIS 9   10  ?   ?   ?   A . n 
A 1 10  HIS 10  11  ?   ?   ?   A . n 
A 1 11  ASP 11  12  ?   ?   ?   A . n 
A 1 12  LEU 12  13  ?   ?   ?   A . n 
A 1 13  TYR 13  14  ?   ?   ?   A . n 
A 1 14  GLU 14  15  ?   ?   ?   A . n 
A 1 15  ASN 15  16  ?   ?   ?   A . n 
A 1 16  LEU 16  17  ?   ?   ?   A . n 
A 1 17  TYR 17  18  ?   ?   ?   A . n 
A 1 18  PHE 18  19  ?   ?   ?   A . n 
A 1 19  GLN 19  20  ?   ?   ?   A . n 
A 1 20  GLY 20  21  ?   ?   ?   A . n 
A 1 21  LYS 21  22  ?   ?   ?   A . n 
A 1 22  LEU 22  23  ?   ?   ?   A . n 
A 1 23  ASP 23  24  ?   ?   ?   A . n 
A 1 24  PRO 24  25  25  PRO PRO A . n 
A 1 25  ALA 25  26  26  ALA ALA A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  LYS 27  28  28  LYS LYS A . n 
A 1 28  SER 28  29  29  SER SER A . n 
A 1 29  ARG 29  30  30  ARG ARG A . n 
A 1 30  SER 30  31  31  SER SER A . n 
A 1 31  CYS 31  32  32  CYS CYS A . n 
A 1 32  GLY 32  33  33  GLY GLY A . n 
A 1 33  GLU 33  34  34  GLU GLU A . n 
A 1 34  VAL 34  35  35  VAL VAL A . n 
A 1 35  ARG 35  36  36  ARG ARG A . n 
A 1 36  GLN 36  37  37  GLN GLN A . n 
A 1 37  ILE 37  38  38  ILE ILE A . n 
A 1 38  TYR 38  39  39  TYR TYR A . n 
A 1 39  GLY 39  40  40  GLY GLY A . n 
A 1 40  ALA 40  41  41  ALA ALA A . n 
A 1 41  LYS 41  42  42  LYS LYS A . n 
A 1 42  GLY 42  43  43  GLY GLY A . n 
A 1 43  PHE 43  44  44  PHE PHE A . n 
A 1 44  SER 44  45  45  SER SER A . n 
A 1 45  LEU 45  46  46  LEU LEU A . n 
A 1 46  SER 46  47  47  SER SER A . n 
A 1 47  ASP 47  48  48  ASP ASP A . n 
A 1 48  VAL 48  49  49  VAL VAL A . n 
A 1 49  PRO 49  50  50  PRO PRO A . n 
A 1 50  GLN 50  51  51  GLN GLN A . n 
A 1 51  ALA 51  52  52  ALA ALA A . n 
A 1 52  GLU 52  53  53  GLU GLU A . n 
A 1 53  ILE 53  54  54  ILE ILE A . n 
A 1 54  SER 54  55  55  SER SER A . n 
A 1 55  GLY 55  56  56  GLY GLY A . n 
A 1 56  GLU 56  57  57  GLU GLU A . n 
A 1 57  HIS 57  58  58  HIS HIS A . n 
A 1 58  LEU 58  59  59  LEU LEU A . n 
A 1 59  ARG 59  60  60  ARG ARG A . n 
A 1 60  ILE 60  61  61  ILE ILE A . n 
A 1 61  CYS 61  62  62  CYS CYS A . n 
A 1 62  PRO 62  63  63  PRO PRO A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  GLY 64  65  65  GLY GLY A . n 
A 1 65  TYR 65  66  66  TYR TYR A . n 
A 1 66  THR 66  67  67  THR THR A . n 
A 1 67  CYS 67  68  68  CYS CYS A . n 
A 1 68  CYS 68  69  69  CYS CYS A . n 
A 1 69  THR 69  70  70  THR THR A . n 
A 1 70  SER 70  71  71  SER SER A . n 
A 1 71  GLU 71  72  72  GLU GLU A . n 
A 1 72  MET 72  73  73  MET MET A . n 
A 1 73  GLU 73  74  74  GLU GLU A . n 
A 1 74  GLU 74  75  75  GLU GLU A . n 
A 1 75  ASN 75  76  76  ASN ASN A . n 
A 1 76  LEU 76  77  77  LEU LEU A . n 
A 1 77  ALA 77  78  78  ALA ALA A . n 
A 1 78  ASN 78  79  79  ASN ASN A . n 
A 1 79  ARG 79  80  80  ARG ARG A . n 
A 1 80  SER 80  81  81  SER SER A . n 
A 1 81  HIS 81  82  82  HIS HIS A . n 
A 1 82  ALA 82  83  83  ALA ALA A . n 
A 1 83  GLU 83  84  84  GLU GLU A . n 
A 1 84  LEU 84  85  85  LEU LEU A . n 
A 1 85  GLU 85  86  86  GLU GLU A . n 
A 1 86  THR 86  87  87  THR THR A . n 
A 1 87  ALA 87  88  88  ALA ALA A . n 
A 1 88  LEU 88  89  89  LEU LEU A . n 
A 1 89  ARG 89  90  90  ARG ARG A . n 
A 1 90  ASP 90  91  91  ASP ASP A . n 
A 1 91  SER 91  92  92  SER SER A . n 
A 1 92  SER 92  93  93  SER SER A . n 
A 1 93  ARG 93  94  94  ARG ARG A . n 
A 1 94  VAL 94  95  95  VAL VAL A . n 
A 1 95  LEU 95  96  96  LEU LEU A . n 
A 1 96  GLN 96  97  97  GLN GLN A . n 
A 1 97  ALA 97  98  98  ALA ALA A . n 
A 1 98  MET 98  99  99  MET MET A . n 
A 1 99  LEU 99  100 100 LEU LEU A . n 
A 1 100 ALA 100 101 101 ALA ALA A . n 
A 1 101 THR 101 102 102 THR THR A . n 
A 1 102 GLN 102 103 103 GLN GLN A . n 
A 1 103 LEU 103 104 104 LEU LEU A . n 
A 1 104 ARG 104 105 105 ARG ARG A . n 
A 1 105 SER 105 106 106 SER SER A . n 
A 1 106 PHE 106 107 107 PHE PHE A . n 
A 1 107 ASP 107 108 108 ASP ASP A . n 
A 1 108 ASP 108 109 109 ASP ASP A . n 
A 1 109 HIS 109 110 110 HIS HIS A . n 
A 1 110 PHE 110 111 111 PHE PHE A . n 
A 1 111 GLN 111 112 112 GLN GLN A . n 
A 1 112 HIS 112 113 113 HIS HIS A . n 
A 1 113 LEU 113 114 114 LEU LEU A . n 
A 1 114 LEU 114 115 115 LEU LEU A . n 
A 1 115 ASN 115 116 116 ASN ASN A . n 
A 1 116 ASP 116 117 117 ASP ASP A . n 
A 1 117 SER 117 118 118 SER SER A . n 
A 1 118 GLU 118 119 119 GLU GLU A . n 
A 1 119 ARG 119 120 120 ARG ARG A . n 
A 1 120 THR 120 121 121 THR THR A . n 
A 1 121 LEU 121 122 122 LEU LEU A . n 
A 1 122 GLN 122 123 123 GLN GLN A . n 
A 1 123 ALA 123 124 124 ALA ALA A . n 
A 1 124 THR 124 125 125 THR THR A . n 
A 1 125 PHE 125 126 126 PHE PHE A . n 
A 1 126 PRO 126 127 127 PRO PRO A . n 
A 1 127 GLY 127 128 128 GLY GLY A . n 
A 1 128 ALA 128 129 129 ALA ALA A . n 
A 1 129 PHE 129 130 130 PHE PHE A . n 
A 1 130 GLY 130 131 131 GLY GLY A . n 
A 1 131 GLU 131 132 132 GLU GLU A . n 
A 1 132 LEU 132 133 133 LEU LEU A . n 
A 1 133 TYR 133 134 134 TYR TYR A . n 
A 1 134 THR 134 135 135 THR THR A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 ASN 136 137 137 ASN ASN A . n 
A 1 137 ALA 137 138 138 ALA ALA A . n 
A 1 138 ARG 138 139 139 ARG ARG A . n 
A 1 139 ALA 139 140 140 ALA ALA A . n 
A 1 140 PHE 140 141 141 PHE PHE A . n 
A 1 141 ARG 141 142 142 ARG ARG A . n 
A 1 142 ASP 142 143 143 ASP ASP A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 TYR 144 145 145 TYR TYR A . n 
A 1 145 SER 145 146 146 SER SER A . n 
A 1 146 GLU 146 147 147 GLU GLU A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 ARG 148 149 149 ARG ARG A . n 
A 1 149 LEU 149 150 150 LEU LEU A . n 
A 1 150 TYR 150 151 151 TYR TYR A . n 
A 1 151 TYR 151 152 152 TYR TYR A . n 
A 1 152 ARG 152 153 153 ARG ARG A . n 
A 1 153 GLY 153 154 154 GLY GLY A . n 
A 1 154 ALA 154 155 155 ALA ALA A . n 
A 1 155 ASN 155 156 156 ASN ASN A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 HIS 157 158 158 HIS HIS A . n 
A 1 158 LEU 158 159 159 LEU LEU A . n 
A 1 159 GLU 159 160 160 GLU GLU A . n 
A 1 160 GLU 160 161 161 GLU GLU A . n 
A 1 161 THR 161 162 162 THR THR A . n 
A 1 162 LEU 162 163 163 LEU LEU A . n 
A 1 163 ALA 163 164 164 ALA ALA A . n 
A 1 164 GLU 164 165 165 GLU GLU A . n 
A 1 165 PHE 165 166 166 PHE PHE A . n 
A 1 166 TRP 166 167 167 TRP TRP A . n 
A 1 167 ALA 167 168 168 ALA ALA A . n 
A 1 168 ARG 168 169 169 ARG ARG A . n 
A 1 169 LEU 169 170 170 LEU LEU A . n 
A 1 170 LEU 170 171 171 LEU LEU A . n 
A 1 171 GLU 171 172 172 GLU GLU A . n 
A 1 172 ARG 172 173 173 ARG ARG A . n 
A 1 173 LEU 173 174 174 LEU LEU A . n 
A 1 174 PHE 174 175 175 PHE PHE A . n 
A 1 175 LYS 175 176 176 LYS LYS A . n 
A 1 176 GLN 176 177 177 GLN GLN A . n 
A 1 177 LEU 177 178 178 LEU LEU A . n 
A 1 178 HIS 178 179 179 HIS HIS A . n 
A 1 179 PRO 179 180 180 PRO PRO A . n 
A 1 180 GLN 180 181 181 GLN GLN A . n 
A 1 181 LEU 181 182 182 LEU LEU A . n 
A 1 182 LEU 182 183 183 LEU LEU A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 PRO 184 185 185 PRO PRO A . n 
A 1 185 ASP 185 186 186 ASP ASP A . n 
A 1 186 ASP 186 187 ?   ?   ?   A . n 
A 1 187 TYR 187 188 ?   ?   ?   A . n 
A 1 188 LEU 188 189 ?   ?   ?   A . n 
A 1 189 ASP 189 190 ?   ?   ?   A . n 
A 1 190 CYS 190 191 ?   ?   ?   A . n 
A 1 191 LEU 191 192 ?   ?   ?   A . n 
A 1 192 GLY 192 193 193 GLY GLY A . n 
A 1 193 LYS 193 194 194 LYS LYS A . n 
A 1 194 GLN 194 195 195 GLN GLN A . n 
A 1 195 ALA 195 196 196 ALA ALA A . n 
A 1 196 GLU 196 197 197 GLU GLU A . n 
A 1 197 ALA 197 198 198 ALA ALA A . n 
A 1 198 LEU 198 199 199 LEU LEU A . n 
A 1 199 ARG 199 200 200 ARG ARG A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PHE 201 202 202 PHE PHE A . n 
A 1 202 GLY 202 203 203 GLY GLY A . n 
A 1 203 GLU 203 204 204 GLU GLU A . n 
A 1 204 ALA 204 205 205 ALA ALA A . n 
A 1 205 PRO 205 206 206 PRO PRO A . n 
A 1 206 ARG 206 207 207 ARG ARG A . n 
A 1 207 GLU 207 208 208 GLU GLU A . n 
A 1 208 LEU 208 209 209 LEU LEU A . n 
A 1 209 ARG 209 210 210 ARG ARG A . n 
A 1 210 LEU 210 211 211 LEU LEU A . n 
A 1 211 ARG 211 212 212 ARG ARG A . n 
A 1 212 ALA 212 213 213 ALA ALA A . n 
A 1 213 THR 213 214 214 THR THR A . n 
A 1 214 ARG 214 215 215 ARG ARG A . n 
A 1 215 ALA 215 216 216 ALA ALA A . n 
A 1 216 PHE 216 217 217 PHE PHE A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 ALA 218 219 219 ALA ALA A . n 
A 1 219 ALA 219 220 220 ALA ALA A . n 
A 1 220 ARG 220 221 221 ARG ARG A . n 
A 1 221 SER 221 222 222 SER SER A . n 
A 1 222 PHE 222 223 223 PHE PHE A . n 
A 1 223 VAL 223 224 224 VAL VAL A . n 
A 1 224 GLN 224 225 225 GLN GLN A . n 
A 1 225 GLY 225 226 226 GLY GLY A . n 
A 1 226 LEU 226 227 227 LEU LEU A . n 
A 1 227 GLY 227 228 228 GLY GLY A . n 
A 1 228 VAL 228 229 229 VAL VAL A . n 
A 1 229 ALA 229 230 230 ALA ALA A . n 
A 1 230 SER 230 231 231 SER SER A . n 
A 1 231 ASP 231 232 232 ASP ASP A . n 
A 1 232 VAL 232 233 233 VAL VAL A . n 
A 1 233 VAL 233 234 234 VAL VAL A . n 
A 1 234 ARG 234 235 235 ARG ARG A . n 
A 1 235 LYS 235 236 236 LYS LYS A . n 
A 1 236 VAL 236 237 237 VAL VAL A . n 
A 1 237 ALA 237 238 238 ALA ALA A . n 
A 1 238 GLN 238 239 239 GLN GLN A . n 
A 1 239 VAL 239 240 240 VAL VAL A . n 
A 1 240 PRO 240 241 241 PRO PRO A . n 
A 1 241 LEU 241 242 242 LEU LEU A . n 
A 1 242 GLY 242 243 243 GLY GLY A . n 
A 1 243 PRO 243 244 244 PRO PRO A . n 
A 1 244 GLU 244 245 245 GLU GLU A . n 
A 1 245 CYS 245 246 246 CYS CYS A . n 
A 1 246 SER 246 247 247 SER SER A . n 
A 1 247 ARG 247 248 248 ARG ARG A . n 
A 1 248 ALA 248 249 249 ALA ALA A . n 
A 1 249 VAL 249 250 250 VAL VAL A . n 
A 1 250 MET 250 251 251 MET MET A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 LEU 252 253 253 LEU LEU A . n 
A 1 253 VAL 253 254 254 VAL VAL A . n 
A 1 254 TYR 254 255 255 TYR TYR A . n 
A 1 255 CYS 255 256 256 CYS CYS A . n 
A 1 256 ALA 256 257 257 ALA ALA A . n 
A 1 257 HIS 257 258 258 HIS HIS A . n 
A 1 258 CYS 258 259 259 CYS CYS A . n 
A 1 259 LEU 259 260 260 LEU LEU A . n 
A 1 260 GLY 260 261 261 GLY GLY A . n 
A 1 261 VAL 261 262 262 VAL VAL A . n 
A 1 262 PRO 262 263 263 PRO PRO A . n 
A 1 263 GLY 263 264 264 GLY GLY A . n 
A 1 264 ALA 264 265 265 ALA ALA A . n 
A 1 265 ARG 265 266 266 ARG ARG A . n 
A 1 266 PRO 266 267 267 PRO PRO A . n 
A 1 267 CYS 267 268 268 CYS CYS A . n 
A 1 268 PRO 268 269 269 PRO PRO A . n 
A 1 269 ASP 269 270 270 ASP ASP A . n 
A 1 270 TYR 270 271 271 TYR TYR A . n 
A 1 271 CYS 271 272 272 CYS CYS A . n 
A 1 272 ARG 272 273 273 ARG ARG A . n 
A 1 273 ASN 273 274 274 ASN ASN A . n 
A 1 274 VAL 274 275 275 VAL VAL A . n 
A 1 275 LEU 275 276 276 LEU LEU A . n 
A 1 276 LYS 276 277 277 LYS LYS A . n 
A 1 277 GLY 277 278 278 GLY GLY A . n 
A 1 278 CYS 278 279 279 CYS CYS A . n 
A 1 279 LEU 279 280 280 LEU LEU A . n 
A 1 280 ALA 280 281 281 ALA ALA A . n 
A 1 281 ASN 281 282 282 ASN ASN A . n 
A 1 282 GLN 282 283 283 GLN GLN A . n 
A 1 283 ALA 283 284 284 ALA ALA A . n 
A 1 284 ASP 284 285 285 ASP ASP A . n 
A 1 285 LEU 285 286 286 LEU LEU A . n 
A 1 286 ASP 286 287 287 ASP ASP A . n 
A 1 287 ALA 287 288 288 ALA ALA A . n 
A 1 288 GLU 288 289 289 GLU GLU A . n 
A 1 289 TRP 289 290 290 TRP TRP A . n 
A 1 290 ARG 290 291 291 ARG ARG A . n 
A 1 291 ASN 291 292 292 ASN ASN A . n 
A 1 292 LEU 292 293 293 LEU LEU A . n 
A 1 293 LEU 293 294 294 LEU LEU A . n 
A 1 294 ASP 294 295 295 ASP ASP A . n 
A 1 295 SER 295 296 296 SER SER A . n 
A 1 296 MET 296 297 297 MET MET A . n 
A 1 297 VAL 297 298 298 VAL VAL A . n 
A 1 298 LEU 298 299 299 LEU LEU A . n 
A 1 299 ILE 299 300 300 ILE ILE A . n 
A 1 300 THR 300 301 301 THR THR A . n 
A 1 301 ASP 301 302 302 ASP ASP A . n 
A 1 302 LYS 302 303 303 LYS LYS A . n 
A 1 303 PHE 303 304 304 PHE PHE A . n 
A 1 304 TRP 304 305 305 TRP TRP A . n 
A 1 305 GLY 305 306 306 GLY GLY A . n 
A 1 306 THR 306 307 307 THR THR A . n 
A 1 307 SER 307 308 308 SER SER A . n 
A 1 308 GLY 308 309 309 GLY GLY A . n 
A 1 309 VAL 309 310 310 VAL VAL A . n 
A 1 310 GLU 310 311 311 GLU GLU A . n 
A 1 311 SER 311 312 312 SER SER A . n 
A 1 312 VAL 312 313 313 VAL VAL A . n 
A 1 313 ILE 313 314 314 ILE ILE A . n 
A 1 314 GLY 314 315 315 GLY GLY A . n 
A 1 315 SER 315 316 316 SER SER A . n 
A 1 316 VAL 316 317 317 VAL VAL A . n 
A 1 317 HIS 317 318 318 HIS HIS A . n 
A 1 318 THR 318 319 319 THR THR A . n 
A 1 319 TRP 319 320 320 TRP TRP A . n 
A 1 320 LEU 320 321 321 LEU LEU A . n 
A 1 321 ALA 321 322 322 ALA ALA A . n 
A 1 322 GLU 322 323 323 GLU GLU A . n 
A 1 323 ALA 323 324 324 ALA ALA A . n 
A 1 324 ILE 324 325 325 ILE ILE A . n 
A 1 325 ASN 325 326 326 ASN ASN A . n 
A 1 326 ALA 326 327 327 ALA ALA A . n 
A 1 327 LEU 327 328 328 LEU LEU A . n 
A 1 328 GLN 328 329 329 GLN GLN A . n 
A 1 329 ASP 329 330 330 ASP ASP A . n 
A 1 330 ASN 330 331 331 ASN ASN A . n 
A 1 331 ARG 331 332 332 ARG ARG A . n 
A 1 332 ASP 332 333 333 ASP ASP A . n 
A 1 333 THR 333 334 334 THR THR A . n 
A 1 334 LEU 334 335 335 LEU LEU A . n 
A 1 335 THR 335 336 336 THR THR A . n 
A 1 336 ALA 336 337 337 ALA ALA A . n 
A 1 337 LYS 337 338 338 LYS LYS A . n 
A 1 338 VAL 338 339 339 VAL VAL A . n 
A 1 339 ILE 339 340 ?   ?   ?   A . n 
A 1 340 GLN 340 341 ?   ?   ?   A . n 
A 1 341 GLY 341 342 ?   ?   ?   A . n 
A 1 342 CYS 342 343 ?   ?   ?   A . n 
A 1 343 GLY 343 344 ?   ?   ?   A . n 
A 1 344 ASN 344 345 ?   ?   ?   A . n 
A 1 345 PRO 345 346 ?   ?   ?   A . n 
A 1 346 LYS 346 347 ?   ?   ?   A . n 
A 1 347 VAL 347 348 ?   ?   ?   A . n 
A 1 348 ASN 348 349 ?   ?   ?   A . n 
A 1 349 PRO 349 350 ?   ?   ?   A . n 
A 1 350 GLN 350 351 ?   ?   ?   A . n 
A 1 351 GLY 351 352 ?   ?   ?   A . n 
A 1 352 PRO 352 353 ?   ?   ?   A . n 
A 1 353 GLY 353 354 ?   ?   ?   A . n 
A 1 354 PRO 354 355 ?   ?   ?   A . n 
A 1 355 GLU 355 356 ?   ?   ?   A . n 
A 1 356 GLU 356 357 ?   ?   ?   A . n 
A 1 357 LYS 357 358 ?   ?   ?   A . n 
A 1 358 ARG 358 359 ?   ?   ?   A . n 
A 1 359 ARG 359 360 ?   ?   ?   A . n 
A 1 360 ARG 360 361 ?   ?   ?   A . n 
A 1 361 GLY 361 362 ?   ?   ?   A . n 
A 1 362 LYS 362 363 ?   ?   ?   A . n 
A 1 363 LEU 363 364 ?   ?   ?   A . n 
A 1 364 ALA 364 365 ?   ?   ?   A . n 
A 1 365 PRO 365 366 366 PRO PRO A . n 
A 1 366 ARG 366 367 367 ARG ARG A . n 
A 1 367 GLU 367 368 368 GLU GLU A . n 
A 1 368 ARG 368 369 369 ARG ARG A . n 
A 1 369 PRO 369 370 370 PRO PRO A . n 
A 1 370 PRO 370 371 371 PRO PRO A . n 
A 1 371 SER 371 372 372 SER SER A . n 
A 1 372 GLY 372 373 373 GLY GLY A . n 
A 1 373 THR 373 374 374 THR THR A . n 
A 1 374 LEU 374 375 375 LEU LEU A . n 
A 1 375 GLU 375 376 376 GLU GLU A . n 
A 1 376 LYS 376 377 377 LYS LYS A . n 
A 1 377 LEU 377 378 378 LEU LEU A . n 
A 1 378 VAL 378 379 379 VAL VAL A . n 
A 1 379 SER 379 380 380 SER SER A . n 
A 1 380 GLU 380 381 381 GLU GLU A . n 
A 1 381 ALA 381 382 382 ALA ALA A . n 
A 1 382 LYS 382 383 383 LYS LYS A . n 
A 1 383 ALA 383 384 384 ALA ALA A . n 
A 1 384 GLN 384 385 385 GLN GLN A . n 
A 1 385 LEU 385 386 386 LEU LEU A . n 
A 1 386 ARG 386 387 387 ARG ARG A . n 
A 1 387 ASP 387 388 388 ASP ASP A . n 
A 1 388 VAL 388 389 389 VAL VAL A . n 
A 1 389 GLN 389 390 390 GLN GLN A . n 
A 1 390 ASP 390 391 391 ASP ASP A . n 
A 1 391 PHE 391 392 392 PHE PHE A . n 
A 1 392 TRP 392 393 393 TRP TRP A . n 
A 1 393 ILE 393 394 394 ILE ILE A . n 
A 1 394 SER 394 395 395 SER SER A . n 
A 1 395 LEU 395 396 396 LEU LEU A . n 
A 1 396 PRO 396 397 397 PRO PRO A . n 
A 1 397 GLY 397 398 398 GLY GLY A . n 
A 1 398 THR 398 399 399 THR THR A . n 
A 1 399 LEU 399 400 400 LEU LEU A . n 
A 1 400 CYS 400 401 401 CYS CYS A . n 
A 1 401 SER 401 402 402 SER SER A . n 
A 1 402 GLU 402 403 403 GLU GLU A . n 
A 1 403 LYS 403 404 404 LYS LYS A . n 
A 1 404 MET 404 405 405 MET MET A . n 
A 1 405 ALA 405 406 406 ALA ALA A . n 
A 1 406 LEU 406 407 ?   ?   ?   A . n 
A 1 407 SER 407 408 ?   ?   ?   A . n 
A 1 408 THR 408 409 ?   ?   ?   A . n 
A 1 409 ALA 409 410 ?   ?   ?   A . n 
A 1 410 SER 410 411 ?   ?   ?   A . n 
A 1 411 ASP 411 412 ?   ?   ?   A . n 
A 1 412 ASP 412 413 413 ASP ASP A . n 
A 1 413 ARG 413 414 414 ARG ARG A . n 
A 1 414 CYS 414 415 415 CYS CYS A . n 
A 1 415 TRP 415 416 416 TRP TRP A . n 
A 1 416 ASN 416 417 417 ASN ASN A . n 
A 1 417 GLY 417 418 418 GLY GLY A . n 
A 1 418 MET 418 419 419 MET MET A . n 
A 1 419 ALA 419 420 420 ALA ALA A . n 
A 1 420 ARG 420 421 421 ARG ARG A . n 
A 1 421 GLY 421 422 422 GLY GLY A . n 
A 1 422 ARG 422 423 423 ARG ARG A . n 
A 1 423 TYR 423 424 424 TYR TYR A . n 
A 1 424 LEU 424 425 425 LEU LEU A . n 
A 1 425 PRO 425 426 426 PRO PRO A . n 
A 1 426 GLU 426 427 427 GLU GLU A . n 
A 1 427 VAL 427 428 428 VAL VAL A . n 
A 1 428 MET 428 429 429 MET MET A . n 
A 1 429 GLY 429 430 430 GLY GLY A . n 
A 1 430 ASP 430 431 431 ASP ASP A . n 
A 1 431 GLY 431 432 432 GLY GLY A . n 
A 1 432 LEU 432 433 433 LEU LEU A . n 
A 1 433 ALA 433 434 434 ALA ALA A . n 
A 1 434 ASN 434 435 435 ASN ASN A . n 
A 1 435 GLN 435 436 436 GLN GLN A . n 
A 1 436 ILE 436 437 437 ILE ILE A . n 
A 1 437 ASN 437 438 438 ASN ASN A . n 
A 1 438 ASN 438 439 439 ASN ASN A . n 
A 1 439 PRO 439 440 440 PRO PRO A . n 
A 1 440 GLU 440 441 441 GLU GLU A . n 
A 1 441 VAL 441 442 442 VAL VAL A . n 
A 1 442 GLU 442 443 443 GLU GLU A . n 
A 1 443 VAL 443 444 444 VAL VAL A . n 
A 1 444 ASP 444 445 445 ASP ASP A . n 
A 1 445 ILE 445 446 446 ILE ILE A . n 
A 1 446 THR 446 447 447 THR THR A . n 
A 1 447 LYS 447 448 448 LYS LYS A . n 
A 1 448 PRO 448 449 449 PRO PRO A . n 
A 1 449 ASP 449 450 450 ASP ASP A . n 
A 1 450 MET 450 451 451 MET MET A . n 
A 1 451 THR 451 452 452 THR THR A . n 
A 1 452 ILE 452 453 453 ILE ILE A . n 
A 1 453 ARG 453 454 454 ARG ARG A . n 
A 1 454 GLN 454 455 455 GLN GLN A . n 
A 1 455 GLN 455 456 456 GLN GLN A . n 
A 1 456 ILE 456 457 457 ILE ILE A . n 
A 1 457 MET 457 458 458 MET MET A . n 
A 1 458 GLN 458 459 459 GLN GLN A . n 
A 1 459 LEU 459 460 460 LEU LEU A . n 
A 1 460 LYS 460 461 461 LYS LYS A . n 
A 1 461 ILE 461 462 462 ILE ILE A . n 
A 1 462 MET 462 463 463 MET MET A . n 
A 1 463 THR 463 464 464 THR THR A . n 
A 1 464 ASN 464 465 465 ASN ASN A . n 
A 1 465 ARG 465 466 466 ARG ARG A . n 
A 1 466 LEU 466 467 467 LEU LEU A . n 
A 1 467 ARG 467 468 468 ARG ARG A . n 
A 1 468 SER 468 469 469 SER SER A . n 
A 1 469 ALA 469 470 470 ALA ALA A . n 
A 1 470 TYR 470 471 471 TYR TYR A . n 
A 1 471 ASN 471 472 472 ASN ASN A . n 
A 1 472 GLY 472 473 473 GLY GLY A . n 
A 1 473 ASN 473 474 ?   ?   ?   A . n 
A 1 474 ASP 474 475 ?   ?   ?   A . n 
A 1 475 VAL 475 476 ?   ?   ?   A . n 
A 1 476 ASP 476 477 ?   ?   ?   A . n 
A 1 477 PHE 477 478 ?   ?   ?   A . n 
A 1 478 GLN 478 479 ?   ?   ?   A . n 
A 1 479 ASP 479 480 ?   ?   ?   A . n 
A 1 480 ALA 480 481 ?   ?   ?   A . n 
A 1 481 SER 481 482 ?   ?   ?   A . n 
A 1 482 ASP 482 483 ?   ?   ?   A . n 
A 1 483 ASP 483 484 ?   ?   ?   A . n 
A 1 484 GLY 484 485 ?   ?   ?   A . n 
A 1 485 ALA 485 486 ?   ?   ?   A . n 
A 1 486 GLY 486 487 ?   ?   ?   A . n 
A 1 487 ALA 487 488 ?   ?   ?   A . n 
A 1 488 GLY 488 489 ?   ?   ?   A . n 
A 1 489 ALA 489 490 ?   ?   ?   A . n 
A 1 490 GLY 490 491 ?   ?   ?   A . n 
A 1 491 ASP 491 492 ?   ?   ?   A . n 
A 1 492 GLY 492 493 ?   ?   ?   A . n 
A 1 493 CYS 493 494 ?   ?   ?   A . n 
A 1 494 LEU 494 495 ?   ?   ?   A . n 
A 1 495 ASP 495 496 ?   ?   ?   A . n 
A 1 496 ASP 496 497 ?   ?   ?   A . n 
A 1 497 LEU 497 498 ?   ?   ?   A . n 
A 1 498 CYS 498 499 ?   ?   ?   A . n 
A 1 499 SER 499 500 ?   ?   ?   A . n 
A 1 500 ARG 500 501 ?   ?   ?   A . n 
A 1 501 LYS 501 502 ?   ?   ?   A . n 
A 1 502 VAL 502 503 ?   ?   ?   A . n 
A 1 503 SER 503 504 ?   ?   ?   A . n 
A 1 504 ARG 504 505 ?   ?   ?   A . n 
A 1 505 LYS 505 506 ?   ?   ?   A . n 
A 1 506 SER 506 507 ?   ?   ?   A . n 
A 1 507 SER 507 508 ?   ?   ?   A . n 
A 1 508 SER 508 509 ?   ?   ?   A . n 
A 1 509 SER 509 510 ?   ?   ?   A . n 
A 1 510 ARG 510 511 ?   ?   ?   A . n 
A 1 511 THR 511 512 ?   ?   ?   A . n 
A 1 512 PRO 512 513 ?   ?   ?   A . n 
A 1 513 LEU 513 514 ?   ?   ?   A . n 
A 1 514 THR 514 515 ?   ?   ?   A . n 
A 1 515 HIS 515 516 ?   ?   ?   A . n 
A 1 516 ALA 516 517 ?   ?   ?   A . n 
A 1 517 LEU 517 518 ?   ?   ?   A . n 
A 1 518 PRO 518 519 ?   ?   ?   A . n 
A 1 519 GLY 519 520 ?   ?   ?   A . n 
A 1 520 LEU 520 521 ?   ?   ?   A . n 
A 1 521 SER 521 522 ?   ?   ?   A . n 
A 1 522 GLU 522 523 ?   ?   ?   A . n 
A 1 523 GLN 523 524 ?   ?   ?   A . n 
A 1 524 GLU 524 525 ?   ?   ?   A . n 
A 1 525 GLY 525 526 ?   ?   ?   A . n 
A 1 526 GLN 526 527 ?   ?   ?   A . n 
B 1 1   ALA 1   2   ?   ?   ?   B . n 
B 1 2   PRO 2   3   ?   ?   ?   B . n 
B 1 3   GLN 3   4   ?   ?   ?   B . n 
B 1 4   LEU 4   5   ?   ?   ?   B . n 
B 1 5   HIS 5   6   ?   ?   ?   B . n 
B 1 6   HIS 6   7   ?   ?   ?   B . n 
B 1 7   HIS 7   8   ?   ?   ?   B . n 
B 1 8   HIS 8   9   ?   ?   ?   B . n 
B 1 9   HIS 9   10  ?   ?   ?   B . n 
B 1 10  HIS 10  11  ?   ?   ?   B . n 
B 1 11  ASP 11  12  ?   ?   ?   B . n 
B 1 12  LEU 12  13  ?   ?   ?   B . n 
B 1 13  TYR 13  14  ?   ?   ?   B . n 
B 1 14  GLU 14  15  ?   ?   ?   B . n 
B 1 15  ASN 15  16  ?   ?   ?   B . n 
B 1 16  LEU 16  17  ?   ?   ?   B . n 
B 1 17  TYR 17  18  ?   ?   ?   B . n 
B 1 18  PHE 18  19  ?   ?   ?   B . n 
B 1 19  GLN 19  20  ?   ?   ?   B . n 
B 1 20  GLY 20  21  ?   ?   ?   B . n 
B 1 21  LYS 21  22  ?   ?   ?   B . n 
B 1 22  LEU 22  23  ?   ?   ?   B . n 
B 1 23  ASP 23  24  ?   ?   ?   B . n 
B 1 24  PRO 24  25  ?   ?   ?   B . n 
B 1 25  ALA 25  26  ?   ?   ?   B . n 
B 1 26  SER 26  27  ?   ?   ?   B . n 
B 1 27  LYS 27  28  ?   ?   ?   B . n 
B 1 28  SER 28  29  29  SER SER B . n 
B 1 29  ARG 29  30  30  ARG ARG B . n 
B 1 30  SER 30  31  31  SER SER B . n 
B 1 31  CYS 31  32  32  CYS CYS B . n 
B 1 32  GLY 32  33  33  GLY GLY B . n 
B 1 33  GLU 33  34  34  GLU GLU B . n 
B 1 34  VAL 34  35  35  VAL VAL B . n 
B 1 35  ARG 35  36  36  ARG ARG B . n 
B 1 36  GLN 36  37  37  GLN GLN B . n 
B 1 37  ILE 37  38  38  ILE ILE B . n 
B 1 38  TYR 38  39  39  TYR TYR B . n 
B 1 39  GLY 39  40  40  GLY GLY B . n 
B 1 40  ALA 40  41  41  ALA ALA B . n 
B 1 41  LYS 41  42  42  LYS LYS B . n 
B 1 42  GLY 42  43  43  GLY GLY B . n 
B 1 43  PHE 43  44  44  PHE PHE B . n 
B 1 44  SER 44  45  45  SER SER B . n 
B 1 45  LEU 45  46  46  LEU LEU B . n 
B 1 46  SER 46  47  47  SER SER B . n 
B 1 47  ASP 47  48  48  ASP ASP B . n 
B 1 48  VAL 48  49  49  VAL VAL B . n 
B 1 49  PRO 49  50  50  PRO PRO B . n 
B 1 50  GLN 50  51  51  GLN GLN B . n 
B 1 51  ALA 51  52  52  ALA ALA B . n 
B 1 52  GLU 52  53  53  GLU GLU B . n 
B 1 53  ILE 53  54  54  ILE ILE B . n 
B 1 54  SER 54  55  55  SER SER B . n 
B 1 55  GLY 55  56  56  GLY GLY B . n 
B 1 56  GLU 56  57  57  GLU GLU B . n 
B 1 57  HIS 57  58  58  HIS HIS B . n 
B 1 58  LEU 58  59  59  LEU LEU B . n 
B 1 59  ARG 59  60  60  ARG ARG B . n 
B 1 60  ILE 60  61  61  ILE ILE B . n 
B 1 61  CYS 61  62  62  CYS CYS B . n 
B 1 62  PRO 62  63  63  PRO PRO B . n 
B 1 63  GLN 63  64  64  GLN GLN B . n 
B 1 64  GLY 64  65  65  GLY GLY B . n 
B 1 65  TYR 65  66  66  TYR TYR B . n 
B 1 66  THR 66  67  67  THR THR B . n 
B 1 67  CYS 67  68  68  CYS CYS B . n 
B 1 68  CYS 68  69  69  CYS CYS B . n 
B 1 69  THR 69  70  70  THR THR B . n 
B 1 70  SER 70  71  71  SER SER B . n 
B 1 71  GLU 71  72  72  GLU GLU B . n 
B 1 72  MET 72  73  73  MET MET B . n 
B 1 73  GLU 73  74  74  GLU GLU B . n 
B 1 74  GLU 74  75  75  GLU GLU B . n 
B 1 75  ASN 75  76  76  ASN ASN B . n 
B 1 76  LEU 76  77  77  LEU LEU B . n 
B 1 77  ALA 77  78  78  ALA ALA B . n 
B 1 78  ASN 78  79  79  ASN ASN B . n 
B 1 79  ARG 79  80  80  ARG ARG B . n 
B 1 80  SER 80  81  81  SER SER B . n 
B 1 81  HIS 81  82  82  HIS HIS B . n 
B 1 82  ALA 82  83  83  ALA ALA B . n 
B 1 83  GLU 83  84  84  GLU GLU B . n 
B 1 84  LEU 84  85  85  LEU LEU B . n 
B 1 85  GLU 85  86  86  GLU GLU B . n 
B 1 86  THR 86  87  87  THR THR B . n 
B 1 87  ALA 87  88  88  ALA ALA B . n 
B 1 88  LEU 88  89  89  LEU LEU B . n 
B 1 89  ARG 89  90  90  ARG ARG B . n 
B 1 90  ASP 90  91  91  ASP ASP B . n 
B 1 91  SER 91  92  92  SER SER B . n 
B 1 92  SER 92  93  93  SER SER B . n 
B 1 93  ARG 93  94  94  ARG ARG B . n 
B 1 94  VAL 94  95  95  VAL VAL B . n 
B 1 95  LEU 95  96  96  LEU LEU B . n 
B 1 96  GLN 96  97  97  GLN GLN B . n 
B 1 97  ALA 97  98  98  ALA ALA B . n 
B 1 98  MET 98  99  99  MET MET B . n 
B 1 99  LEU 99  100 100 LEU LEU B . n 
B 1 100 ALA 100 101 101 ALA ALA B . n 
B 1 101 THR 101 102 102 THR THR B . n 
B 1 102 GLN 102 103 103 GLN GLN B . n 
B 1 103 LEU 103 104 104 LEU LEU B . n 
B 1 104 ARG 104 105 105 ARG ARG B . n 
B 1 105 SER 105 106 106 SER SER B . n 
B 1 106 PHE 106 107 107 PHE PHE B . n 
B 1 107 ASP 107 108 108 ASP ASP B . n 
B 1 108 ASP 108 109 109 ASP ASP B . n 
B 1 109 HIS 109 110 110 HIS HIS B . n 
B 1 110 PHE 110 111 111 PHE PHE B . n 
B 1 111 GLN 111 112 112 GLN GLN B . n 
B 1 112 HIS 112 113 113 HIS HIS B . n 
B 1 113 LEU 113 114 114 LEU LEU B . n 
B 1 114 LEU 114 115 115 LEU LEU B . n 
B 1 115 ASN 115 116 116 ASN ASN B . n 
B 1 116 ASP 116 117 117 ASP ASP B . n 
B 1 117 SER 117 118 118 SER SER B . n 
B 1 118 GLU 118 119 119 GLU GLU B . n 
B 1 119 ARG 119 120 120 ARG ARG B . n 
B 1 120 THR 120 121 121 THR THR B . n 
B 1 121 LEU 121 122 122 LEU LEU B . n 
B 1 122 GLN 122 123 123 GLN GLN B . n 
B 1 123 ALA 123 124 124 ALA ALA B . n 
B 1 124 THR 124 125 125 THR THR B . n 
B 1 125 PHE 125 126 126 PHE PHE B . n 
B 1 126 PRO 126 127 127 PRO PRO B . n 
B 1 127 GLY 127 128 128 GLY GLY B . n 
B 1 128 ALA 128 129 129 ALA ALA B . n 
B 1 129 PHE 129 130 130 PHE PHE B . n 
B 1 130 GLY 130 131 131 GLY GLY B . n 
B 1 131 GLU 131 132 132 GLU GLU B . n 
B 1 132 LEU 132 133 133 LEU LEU B . n 
B 1 133 TYR 133 134 134 TYR TYR B . n 
B 1 134 THR 134 135 135 THR THR B . n 
B 1 135 GLN 135 136 136 GLN GLN B . n 
B 1 136 ASN 136 137 137 ASN ASN B . n 
B 1 137 ALA 137 138 138 ALA ALA B . n 
B 1 138 ARG 138 139 139 ARG ARG B . n 
B 1 139 ALA 139 140 140 ALA ALA B . n 
B 1 140 PHE 140 141 141 PHE PHE B . n 
B 1 141 ARG 141 142 142 ARG ARG B . n 
B 1 142 ASP 142 143 143 ASP ASP B . n 
B 1 143 LEU 143 144 144 LEU LEU B . n 
B 1 144 TYR 144 145 145 TYR TYR B . n 
B 1 145 SER 145 146 146 SER SER B . n 
B 1 146 GLU 146 147 147 GLU GLU B . n 
B 1 147 LEU 147 148 148 LEU LEU B . n 
B 1 148 ARG 148 149 149 ARG ARG B . n 
B 1 149 LEU 149 150 150 LEU LEU B . n 
B 1 150 TYR 150 151 151 TYR TYR B . n 
B 1 151 TYR 151 152 152 TYR TYR B . n 
B 1 152 ARG 152 153 153 ARG ARG B . n 
B 1 153 GLY 153 154 154 GLY GLY B . n 
B 1 154 ALA 154 155 155 ALA ALA B . n 
B 1 155 ASN 155 156 156 ASN ASN B . n 
B 1 156 LEU 156 157 157 LEU LEU B . n 
B 1 157 HIS 157 158 158 HIS HIS B . n 
B 1 158 LEU 158 159 159 LEU LEU B . n 
B 1 159 GLU 159 160 160 GLU GLU B . n 
B 1 160 GLU 160 161 161 GLU GLU B . n 
B 1 161 THR 161 162 162 THR THR B . n 
B 1 162 LEU 162 163 163 LEU LEU B . n 
B 1 163 ALA 163 164 164 ALA ALA B . n 
B 1 164 GLU 164 165 165 GLU GLU B . n 
B 1 165 PHE 165 166 166 PHE PHE B . n 
B 1 166 TRP 166 167 167 TRP TRP B . n 
B 1 167 ALA 167 168 168 ALA ALA B . n 
B 1 168 ARG 168 169 169 ARG ARG B . n 
B 1 169 LEU 169 170 170 LEU LEU B . n 
B 1 170 LEU 170 171 171 LEU LEU B . n 
B 1 171 GLU 171 172 172 GLU GLU B . n 
B 1 172 ARG 172 173 173 ARG ARG B . n 
B 1 173 LEU 173 174 174 LEU LEU B . n 
B 1 174 PHE 174 175 175 PHE PHE B . n 
B 1 175 LYS 175 176 176 LYS LYS B . n 
B 1 176 GLN 176 177 177 GLN GLN B . n 
B 1 177 LEU 177 178 178 LEU LEU B . n 
B 1 178 HIS 178 179 179 HIS HIS B . n 
B 1 179 PRO 179 180 180 PRO PRO B . n 
B 1 180 GLN 180 181 181 GLN GLN B . n 
B 1 181 LEU 181 182 182 LEU LEU B . n 
B 1 182 LEU 182 183 183 LEU LEU B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 PRO 184 185 185 PRO PRO B . n 
B 1 185 ASP 185 186 186 ASP ASP B . n 
B 1 186 ASP 186 187 187 ASP ASP B . n 
B 1 187 TYR 187 188 188 TYR TYR B . n 
B 1 188 LEU 188 189 189 LEU LEU B . n 
B 1 189 ASP 189 190 190 ASP ASP B . n 
B 1 190 CYS 190 191 191 CYS CYS B . n 
B 1 191 LEU 191 192 192 LEU LEU B . n 
B 1 192 GLY 192 193 193 GLY GLY B . n 
B 1 193 LYS 193 194 194 LYS LYS B . n 
B 1 194 GLN 194 195 195 GLN GLN B . n 
B 1 195 ALA 195 196 196 ALA ALA B . n 
B 1 196 GLU 196 197 197 GLU GLU B . n 
B 1 197 ALA 197 198 198 ALA ALA B . n 
B 1 198 LEU 198 199 199 LEU LEU B . n 
B 1 199 ARG 199 200 200 ARG ARG B . n 
B 1 200 PRO 200 201 201 PRO PRO B . n 
B 1 201 PHE 201 202 202 PHE PHE B . n 
B 1 202 GLY 202 203 203 GLY GLY B . n 
B 1 203 GLU 203 204 204 GLU GLU B . n 
B 1 204 ALA 204 205 205 ALA ALA B . n 
B 1 205 PRO 205 206 206 PRO PRO B . n 
B 1 206 ARG 206 207 207 ARG ARG B . n 
B 1 207 GLU 207 208 208 GLU GLU B . n 
B 1 208 LEU 208 209 209 LEU LEU B . n 
B 1 209 ARG 209 210 210 ARG ARG B . n 
B 1 210 LEU 210 211 211 LEU LEU B . n 
B 1 211 ARG 211 212 212 ARG ARG B . n 
B 1 212 ALA 212 213 213 ALA ALA B . n 
B 1 213 THR 213 214 214 THR THR B . n 
B 1 214 ARG 214 215 215 ARG ARG B . n 
B 1 215 ALA 215 216 216 ALA ALA B . n 
B 1 216 PHE 216 217 217 PHE PHE B . n 
B 1 217 VAL 217 218 218 VAL VAL B . n 
B 1 218 ALA 218 219 219 ALA ALA B . n 
B 1 219 ALA 219 220 220 ALA ALA B . n 
B 1 220 ARG 220 221 221 ARG ARG B . n 
B 1 221 SER 221 222 222 SER SER B . n 
B 1 222 PHE 222 223 223 PHE PHE B . n 
B 1 223 VAL 223 224 224 VAL VAL B . n 
B 1 224 GLN 224 225 225 GLN GLN B . n 
B 1 225 GLY 225 226 226 GLY GLY B . n 
B 1 226 LEU 226 227 227 LEU LEU B . n 
B 1 227 GLY 227 228 228 GLY GLY B . n 
B 1 228 VAL 228 229 229 VAL VAL B . n 
B 1 229 ALA 229 230 230 ALA ALA B . n 
B 1 230 SER 230 231 231 SER SER B . n 
B 1 231 ASP 231 232 232 ASP ASP B . n 
B 1 232 VAL 232 233 233 VAL VAL B . n 
B 1 233 VAL 233 234 234 VAL VAL B . n 
B 1 234 ARG 234 235 235 ARG ARG B . n 
B 1 235 LYS 235 236 236 LYS LYS B . n 
B 1 236 VAL 236 237 237 VAL VAL B . n 
B 1 237 ALA 237 238 238 ALA ALA B . n 
B 1 238 GLN 238 239 239 GLN GLN B . n 
B 1 239 VAL 239 240 240 VAL VAL B . n 
B 1 240 PRO 240 241 241 PRO PRO B . n 
B 1 241 LEU 241 242 242 LEU LEU B . n 
B 1 242 GLY 242 243 243 GLY GLY B . n 
B 1 243 PRO 243 244 244 PRO PRO B . n 
B 1 244 GLU 244 245 245 GLU GLU B . n 
B 1 245 CYS 245 246 246 CYS CYS B . n 
B 1 246 SER 246 247 247 SER SER B . n 
B 1 247 ARG 247 248 248 ARG ARG B . n 
B 1 248 ALA 248 249 249 ALA ALA B . n 
B 1 249 VAL 249 250 250 VAL VAL B . n 
B 1 250 MET 250 251 251 MET MET B . n 
B 1 251 LYS 251 252 252 LYS LYS B . n 
B 1 252 LEU 252 253 253 LEU LEU B . n 
B 1 253 VAL 253 254 254 VAL VAL B . n 
B 1 254 TYR 254 255 255 TYR TYR B . n 
B 1 255 CYS 255 256 256 CYS CYS B . n 
B 1 256 ALA 256 257 257 ALA ALA B . n 
B 1 257 HIS 257 258 258 HIS HIS B . n 
B 1 258 CYS 258 259 259 CYS CYS B . n 
B 1 259 LEU 259 260 260 LEU LEU B . n 
B 1 260 GLY 260 261 261 GLY GLY B . n 
B 1 261 VAL 261 262 262 VAL VAL B . n 
B 1 262 PRO 262 263 263 PRO PRO B . n 
B 1 263 GLY 263 264 264 GLY GLY B . n 
B 1 264 ALA 264 265 265 ALA ALA B . n 
B 1 265 ARG 265 266 266 ARG ARG B . n 
B 1 266 PRO 266 267 267 PRO PRO B . n 
B 1 267 CYS 267 268 268 CYS CYS B . n 
B 1 268 PRO 268 269 269 PRO PRO B . n 
B 1 269 ASP 269 270 270 ASP ASP B . n 
B 1 270 TYR 270 271 271 TYR TYR B . n 
B 1 271 CYS 271 272 272 CYS CYS B . n 
B 1 272 ARG 272 273 273 ARG ARG B . n 
B 1 273 ASN 273 274 274 ASN ASN B . n 
B 1 274 VAL 274 275 275 VAL VAL B . n 
B 1 275 LEU 275 276 276 LEU LEU B . n 
B 1 276 LYS 276 277 277 LYS LYS B . n 
B 1 277 GLY 277 278 278 GLY GLY B . n 
B 1 278 CYS 278 279 279 CYS CYS B . n 
B 1 279 LEU 279 280 280 LEU LEU B . n 
B 1 280 ALA 280 281 281 ALA ALA B . n 
B 1 281 ASN 281 282 282 ASN ASN B . n 
B 1 282 GLN 282 283 283 GLN GLN B . n 
B 1 283 ALA 283 284 284 ALA ALA B . n 
B 1 284 ASP 284 285 285 ASP ASP B . n 
B 1 285 LEU 285 286 286 LEU LEU B . n 
B 1 286 ASP 286 287 287 ASP ASP B . n 
B 1 287 ALA 287 288 288 ALA ALA B . n 
B 1 288 GLU 288 289 289 GLU GLU B . n 
B 1 289 TRP 289 290 290 TRP TRP B . n 
B 1 290 ARG 290 291 291 ARG ARG B . n 
B 1 291 ASN 291 292 292 ASN ASN B . n 
B 1 292 LEU 292 293 293 LEU LEU B . n 
B 1 293 LEU 293 294 294 LEU LEU B . n 
B 1 294 ASP 294 295 295 ASP ASP B . n 
B 1 295 SER 295 296 296 SER SER B . n 
B 1 296 MET 296 297 297 MET MET B . n 
B 1 297 VAL 297 298 298 VAL VAL B . n 
B 1 298 LEU 298 299 299 LEU LEU B . n 
B 1 299 ILE 299 300 300 ILE ILE B . n 
B 1 300 THR 300 301 301 THR THR B . n 
B 1 301 ASP 301 302 302 ASP ASP B . n 
B 1 302 LYS 302 303 303 LYS LYS B . n 
B 1 303 PHE 303 304 304 PHE PHE B . n 
B 1 304 TRP 304 305 305 TRP TRP B . n 
B 1 305 GLY 305 306 306 GLY GLY B . n 
B 1 306 THR 306 307 307 THR THR B . n 
B 1 307 SER 307 308 308 SER SER B . n 
B 1 308 GLY 308 309 309 GLY GLY B . n 
B 1 309 VAL 309 310 310 VAL VAL B . n 
B 1 310 GLU 310 311 311 GLU GLU B . n 
B 1 311 SER 311 312 312 SER SER B . n 
B 1 312 VAL 312 313 313 VAL VAL B . n 
B 1 313 ILE 313 314 314 ILE ILE B . n 
B 1 314 GLY 314 315 315 GLY GLY B . n 
B 1 315 SER 315 316 316 SER SER B . n 
B 1 316 VAL 316 317 317 VAL VAL B . n 
B 1 317 HIS 317 318 318 HIS HIS B . n 
B 1 318 THR 318 319 319 THR THR B . n 
B 1 319 TRP 319 320 320 TRP TRP B . n 
B 1 320 LEU 320 321 321 LEU LEU B . n 
B 1 321 ALA 321 322 322 ALA ALA B . n 
B 1 322 GLU 322 323 323 GLU GLU B . n 
B 1 323 ALA 323 324 324 ALA ALA B . n 
B 1 324 ILE 324 325 325 ILE ILE B . n 
B 1 325 ASN 325 326 326 ASN ASN B . n 
B 1 326 ALA 326 327 327 ALA ALA B . n 
B 1 327 LEU 327 328 328 LEU LEU B . n 
B 1 328 GLN 328 329 329 GLN GLN B . n 
B 1 329 ASP 329 330 330 ASP ASP B . n 
B 1 330 ASN 330 331 331 ASN ASN B . n 
B 1 331 ARG 331 332 332 ARG ARG B . n 
B 1 332 ASP 332 333 333 ASP ASP B . n 
B 1 333 THR 333 334 334 THR THR B . n 
B 1 334 LEU 334 335 335 LEU LEU B . n 
B 1 335 THR 335 336 336 THR THR B . n 
B 1 336 ALA 336 337 337 ALA ALA B . n 
B 1 337 LYS 337 338 338 LYS LYS B . n 
B 1 338 VAL 338 339 339 VAL VAL B . n 
B 1 339 ILE 339 340 340 ILE ILE B . n 
B 1 340 GLN 340 341 341 GLN GLN B . n 
B 1 341 GLY 341 342 342 GLY GLY B . n 
B 1 342 CYS 342 343 343 CYS CYS B . n 
B 1 343 GLY 343 344 344 GLY GLY B . n 
B 1 344 ASN 344 345 345 ASN ASN B . n 
B 1 345 PRO 345 346 346 PRO PRO B . n 
B 1 346 LYS 346 347 347 LYS LYS B . n 
B 1 347 VAL 347 348 348 VAL VAL B . n 
B 1 348 ASN 348 349 349 ASN ASN B . n 
B 1 349 PRO 349 350 ?   ?   ?   B . n 
B 1 350 GLN 350 351 ?   ?   ?   B . n 
B 1 351 GLY 351 352 ?   ?   ?   B . n 
B 1 352 PRO 352 353 ?   ?   ?   B . n 
B 1 353 GLY 353 354 ?   ?   ?   B . n 
B 1 354 PRO 354 355 ?   ?   ?   B . n 
B 1 355 GLU 355 356 ?   ?   ?   B . n 
B 1 356 GLU 356 357 ?   ?   ?   B . n 
B 1 357 LYS 357 358 ?   ?   ?   B . n 
B 1 358 ARG 358 359 ?   ?   ?   B . n 
B 1 359 ARG 359 360 ?   ?   ?   B . n 
B 1 360 ARG 360 361 361 ARG ARG B . n 
B 1 361 GLY 361 362 362 GLY GLY B . n 
B 1 362 LYS 362 363 363 LYS LYS B . n 
B 1 363 LEU 363 364 364 LEU LEU B . n 
B 1 364 ALA 364 365 365 ALA ALA B . n 
B 1 365 PRO 365 366 366 PRO PRO B . n 
B 1 366 ARG 366 367 367 ARG ARG B . n 
B 1 367 GLU 367 368 368 GLU GLU B . n 
B 1 368 ARG 368 369 369 ARG ARG B . n 
B 1 369 PRO 369 370 370 PRO PRO B . n 
B 1 370 PRO 370 371 371 PRO PRO B . n 
B 1 371 SER 371 372 372 SER SER B . n 
B 1 372 GLY 372 373 373 GLY GLY B . n 
B 1 373 THR 373 374 374 THR THR B . n 
B 1 374 LEU 374 375 375 LEU LEU B . n 
B 1 375 GLU 375 376 376 GLU GLU B . n 
B 1 376 LYS 376 377 377 LYS LYS B . n 
B 1 377 LEU 377 378 378 LEU LEU B . n 
B 1 378 VAL 378 379 379 VAL VAL B . n 
B 1 379 SER 379 380 380 SER SER B . n 
B 1 380 GLU 380 381 381 GLU GLU B . n 
B 1 381 ALA 381 382 382 ALA ALA B . n 
B 1 382 LYS 382 383 383 LYS LYS B . n 
B 1 383 ALA 383 384 384 ALA ALA B . n 
B 1 384 GLN 384 385 385 GLN GLN B . n 
B 1 385 LEU 385 386 386 LEU LEU B . n 
B 1 386 ARG 386 387 387 ARG ARG B . n 
B 1 387 ASP 387 388 388 ASP ASP B . n 
B 1 388 VAL 388 389 389 VAL VAL B . n 
B 1 389 GLN 389 390 390 GLN GLN B . n 
B 1 390 ASP 390 391 391 ASP ASP B . n 
B 1 391 PHE 391 392 392 PHE PHE B . n 
B 1 392 TRP 392 393 393 TRP TRP B . n 
B 1 393 ILE 393 394 394 ILE ILE B . n 
B 1 394 SER 394 395 395 SER SER B . n 
B 1 395 LEU 395 396 396 LEU LEU B . n 
B 1 396 PRO 396 397 397 PRO PRO B . n 
B 1 397 GLY 397 398 398 GLY GLY B . n 
B 1 398 THR 398 399 399 THR THR B . n 
B 1 399 LEU 399 400 400 LEU LEU B . n 
B 1 400 CYS 400 401 401 CYS CYS B . n 
B 1 401 SER 401 402 402 SER SER B . n 
B 1 402 GLU 402 403 403 GLU GLU B . n 
B 1 403 LYS 403 404 404 LYS LYS B . n 
B 1 404 MET 404 405 405 MET MET B . n 
B 1 405 ALA 405 406 406 ALA ALA B . n 
B 1 406 LEU 406 407 407 LEU LEU B . n 
B 1 407 SER 407 408 ?   ?   ?   B . n 
B 1 408 THR 408 409 ?   ?   ?   B . n 
B 1 409 ALA 409 410 ?   ?   ?   B . n 
B 1 410 SER 410 411 ?   ?   ?   B . n 
B 1 411 ASP 411 412 ?   ?   ?   B . n 
B 1 412 ASP 412 413 413 ASP ASP B . n 
B 1 413 ARG 413 414 414 ARG ARG B . n 
B 1 414 CYS 414 415 415 CYS CYS B . n 
B 1 415 TRP 415 416 416 TRP TRP B . n 
B 1 416 ASN 416 417 417 ASN ASN B . n 
B 1 417 GLY 417 418 418 GLY GLY B . n 
B 1 418 MET 418 419 419 MET MET B . n 
B 1 419 ALA 419 420 420 ALA ALA B . n 
B 1 420 ARG 420 421 421 ARG ARG B . n 
B 1 421 GLY 421 422 422 GLY GLY B . n 
B 1 422 ARG 422 423 423 ARG ARG B . n 
B 1 423 TYR 423 424 424 TYR TYR B . n 
B 1 424 LEU 424 425 425 LEU LEU B . n 
B 1 425 PRO 425 426 426 PRO PRO B . n 
B 1 426 GLU 426 427 427 GLU GLU B . n 
B 1 427 VAL 427 428 428 VAL VAL B . n 
B 1 428 MET 428 429 429 MET MET B . n 
B 1 429 GLY 429 430 430 GLY GLY B . n 
B 1 430 ASP 430 431 431 ASP ASP B . n 
B 1 431 GLY 431 432 432 GLY GLY B . n 
B 1 432 LEU 432 433 433 LEU LEU B . n 
B 1 433 ALA 433 434 434 ALA ALA B . n 
B 1 434 ASN 434 435 435 ASN ASN B . n 
B 1 435 GLN 435 436 436 GLN GLN B . n 
B 1 436 ILE 436 437 437 ILE ILE B . n 
B 1 437 ASN 437 438 438 ASN ASN B . n 
B 1 438 ASN 438 439 439 ASN ASN B . n 
B 1 439 PRO 439 440 440 PRO PRO B . n 
B 1 440 GLU 440 441 441 GLU GLU B . n 
B 1 441 VAL 441 442 442 VAL VAL B . n 
B 1 442 GLU 442 443 443 GLU GLU B . n 
B 1 443 VAL 443 444 444 VAL VAL B . n 
B 1 444 ASP 444 445 445 ASP ASP B . n 
B 1 445 ILE 445 446 446 ILE ILE B . n 
B 1 446 THR 446 447 447 THR THR B . n 
B 1 447 LYS 447 448 448 LYS LYS B . n 
B 1 448 PRO 448 449 449 PRO PRO B . n 
B 1 449 ASP 449 450 450 ASP ASP B . n 
B 1 450 MET 450 451 451 MET MET B . n 
B 1 451 THR 451 452 452 THR THR B . n 
B 1 452 ILE 452 453 453 ILE ILE B . n 
B 1 453 ARG 453 454 454 ARG ARG B . n 
B 1 454 GLN 454 455 455 GLN GLN B . n 
B 1 455 GLN 455 456 456 GLN GLN B . n 
B 1 456 ILE 456 457 457 ILE ILE B . n 
B 1 457 MET 457 458 458 MET MET B . n 
B 1 458 GLN 458 459 459 GLN GLN B . n 
B 1 459 LEU 459 460 460 LEU LEU B . n 
B 1 460 LYS 460 461 461 LYS LYS B . n 
B 1 461 ILE 461 462 462 ILE ILE B . n 
B 1 462 MET 462 463 463 MET MET B . n 
B 1 463 THR 463 464 464 THR THR B . n 
B 1 464 ASN 464 465 465 ASN ASN B . n 
B 1 465 ARG 465 466 466 ARG ARG B . n 
B 1 466 LEU 466 467 467 LEU LEU B . n 
B 1 467 ARG 467 468 468 ARG ARG B . n 
B 1 468 SER 468 469 469 SER SER B . n 
B 1 469 ALA 469 470 470 ALA ALA B . n 
B 1 470 TYR 470 471 471 TYR TYR B . n 
B 1 471 ASN 471 472 472 ASN ASN B . n 
B 1 472 GLY 472 473 473 GLY GLY B . n 
B 1 473 ASN 473 474 474 ASN ASN B . n 
B 1 474 ASP 474 475 475 ASP ASP B . n 
B 1 475 VAL 475 476 ?   ?   ?   B . n 
B 1 476 ASP 476 477 ?   ?   ?   B . n 
B 1 477 PHE 477 478 ?   ?   ?   B . n 
B 1 478 GLN 478 479 ?   ?   ?   B . n 
B 1 479 ASP 479 480 ?   ?   ?   B . n 
B 1 480 ALA 480 481 ?   ?   ?   B . n 
B 1 481 SER 481 482 ?   ?   ?   B . n 
B 1 482 ASP 482 483 ?   ?   ?   B . n 
B 1 483 ASP 483 484 ?   ?   ?   B . n 
B 1 484 GLY 484 485 ?   ?   ?   B . n 
B 1 485 ALA 485 486 ?   ?   ?   B . n 
B 1 486 GLY 486 487 ?   ?   ?   B . n 
B 1 487 ALA 487 488 ?   ?   ?   B . n 
B 1 488 GLY 488 489 ?   ?   ?   B . n 
B 1 489 ALA 489 490 ?   ?   ?   B . n 
B 1 490 GLY 490 491 ?   ?   ?   B . n 
B 1 491 ASP 491 492 ?   ?   ?   B . n 
B 1 492 GLY 492 493 ?   ?   ?   B . n 
B 1 493 CYS 493 494 ?   ?   ?   B . n 
B 1 494 LEU 494 495 ?   ?   ?   B . n 
B 1 495 ASP 495 496 ?   ?   ?   B . n 
B 1 496 ASP 496 497 ?   ?   ?   B . n 
B 1 497 LEU 497 498 ?   ?   ?   B . n 
B 1 498 CYS 498 499 ?   ?   ?   B . n 
B 1 499 SER 499 500 ?   ?   ?   B . n 
B 1 500 ARG 500 501 ?   ?   ?   B . n 
B 1 501 LYS 501 502 ?   ?   ?   B . n 
B 1 502 VAL 502 503 ?   ?   ?   B . n 
B 1 503 SER 503 504 ?   ?   ?   B . n 
B 1 504 ARG 504 505 ?   ?   ?   B . n 
B 1 505 LYS 505 506 ?   ?   ?   B . n 
B 1 506 SER 506 507 ?   ?   ?   B . n 
B 1 507 SER 507 508 ?   ?   ?   B . n 
B 1 508 SER 508 509 ?   ?   ?   B . n 
B 1 509 SER 509 510 ?   ?   ?   B . n 
B 1 510 ARG 510 511 ?   ?   ?   B . n 
B 1 511 THR 511 512 ?   ?   ?   B . n 
B 1 512 PRO 512 513 ?   ?   ?   B . n 
B 1 513 LEU 513 514 ?   ?   ?   B . n 
B 1 514 THR 514 515 ?   ?   ?   B . n 
B 1 515 HIS 515 516 ?   ?   ?   B . n 
B 1 516 ALA 516 517 ?   ?   ?   B . n 
B 1 517 LEU 517 518 ?   ?   ?   B . n 
B 1 518 PRO 518 519 ?   ?   ?   B . n 
B 1 519 GLY 519 520 ?   ?   ?   B . n 
B 1 520 LEU 520 521 ?   ?   ?   B . n 
B 1 521 SER 521 522 ?   ?   ?   B . n 
B 1 522 GLU 522 523 ?   ?   ?   B . n 
B 1 523 GLN 523 524 ?   ?   ?   B . n 
B 1 524 GLU 524 525 ?   ?   ?   B . n 
B 1 525 GLY 525 526 ?   ?   ?   B . n 
B 1 526 GLN 526 527 ?   ?   ?   B . n 
C 1 1   ALA 1   2   ?   ?   ?   C . n 
C 1 2   PRO 2   3   ?   ?   ?   C . n 
C 1 3   GLN 3   4   ?   ?   ?   C . n 
C 1 4   LEU 4   5   ?   ?   ?   C . n 
C 1 5   HIS 5   6   ?   ?   ?   C . n 
C 1 6   HIS 6   7   ?   ?   ?   C . n 
C 1 7   HIS 7   8   ?   ?   ?   C . n 
C 1 8   HIS 8   9   ?   ?   ?   C . n 
C 1 9   HIS 9   10  ?   ?   ?   C . n 
C 1 10  HIS 10  11  ?   ?   ?   C . n 
C 1 11  ASP 11  12  ?   ?   ?   C . n 
C 1 12  LEU 12  13  ?   ?   ?   C . n 
C 1 13  TYR 13  14  ?   ?   ?   C . n 
C 1 14  GLU 14  15  ?   ?   ?   C . n 
C 1 15  ASN 15  16  ?   ?   ?   C . n 
C 1 16  LEU 16  17  ?   ?   ?   C . n 
C 1 17  TYR 17  18  ?   ?   ?   C . n 
C 1 18  PHE 18  19  ?   ?   ?   C . n 
C 1 19  GLN 19  20  ?   ?   ?   C . n 
C 1 20  GLY 20  21  ?   ?   ?   C . n 
C 1 21  LYS 21  22  ?   ?   ?   C . n 
C 1 22  LEU 22  23  ?   ?   ?   C . n 
C 1 23  ASP 23  24  ?   ?   ?   C . n 
C 1 24  PRO 24  25  ?   ?   ?   C . n 
C 1 25  ALA 25  26  ?   ?   ?   C . n 
C 1 26  SER 26  27  ?   ?   ?   C . n 
C 1 27  LYS 27  28  ?   ?   ?   C . n 
C 1 28  SER 28  29  29  SER SER C . n 
C 1 29  ARG 29  30  30  ARG ARG C . n 
C 1 30  SER 30  31  31  SER SER C . n 
C 1 31  CYS 31  32  32  CYS CYS C . n 
C 1 32  GLY 32  33  33  GLY GLY C . n 
C 1 33  GLU 33  34  34  GLU GLU C . n 
C 1 34  VAL 34  35  35  VAL VAL C . n 
C 1 35  ARG 35  36  36  ARG ARG C . n 
C 1 36  GLN 36  37  37  GLN GLN C . n 
C 1 37  ILE 37  38  38  ILE ILE C . n 
C 1 38  TYR 38  39  39  TYR TYR C . n 
C 1 39  GLY 39  40  40  GLY GLY C . n 
C 1 40  ALA 40  41  41  ALA ALA C . n 
C 1 41  LYS 41  42  42  LYS LYS C . n 
C 1 42  GLY 42  43  43  GLY GLY C . n 
C 1 43  PHE 43  44  44  PHE PHE C . n 
C 1 44  SER 44  45  45  SER SER C . n 
C 1 45  LEU 45  46  46  LEU LEU C . n 
C 1 46  SER 46  47  47  SER SER C . n 
C 1 47  ASP 47  48  48  ASP ASP C . n 
C 1 48  VAL 48  49  49  VAL VAL C . n 
C 1 49  PRO 49  50  50  PRO PRO C . n 
C 1 50  GLN 50  51  51  GLN GLN C . n 
C 1 51  ALA 51  52  52  ALA ALA C . n 
C 1 52  GLU 52  53  53  GLU GLU C . n 
C 1 53  ILE 53  54  54  ILE ILE C . n 
C 1 54  SER 54  55  55  SER SER C . n 
C 1 55  GLY 55  56  56  GLY GLY C . n 
C 1 56  GLU 56  57  57  GLU GLU C . n 
C 1 57  HIS 57  58  58  HIS HIS C . n 
C 1 58  LEU 58  59  59  LEU LEU C . n 
C 1 59  ARG 59  60  60  ARG ARG C . n 
C 1 60  ILE 60  61  61  ILE ILE C . n 
C 1 61  CYS 61  62  62  CYS CYS C . n 
C 1 62  PRO 62  63  63  PRO PRO C . n 
C 1 63  GLN 63  64  64  GLN GLN C . n 
C 1 64  GLY 64  65  65  GLY GLY C . n 
C 1 65  TYR 65  66  66  TYR TYR C . n 
C 1 66  THR 66  67  67  THR THR C . n 
C 1 67  CYS 67  68  68  CYS CYS C . n 
C 1 68  CYS 68  69  69  CYS CYS C . n 
C 1 69  THR 69  70  70  THR THR C . n 
C 1 70  SER 70  71  71  SER SER C . n 
C 1 71  GLU 71  72  72  GLU GLU C . n 
C 1 72  MET 72  73  73  MET MET C . n 
C 1 73  GLU 73  74  74  GLU GLU C . n 
C 1 74  GLU 74  75  75  GLU GLU C . n 
C 1 75  ASN 75  76  76  ASN ASN C . n 
C 1 76  LEU 76  77  77  LEU LEU C . n 
C 1 77  ALA 77  78  78  ALA ALA C . n 
C 1 78  ASN 78  79  79  ASN ASN C . n 
C 1 79  ARG 79  80  80  ARG ARG C . n 
C 1 80  SER 80  81  81  SER SER C . n 
C 1 81  HIS 81  82  82  HIS HIS C . n 
C 1 82  ALA 82  83  83  ALA ALA C . n 
C 1 83  GLU 83  84  84  GLU GLU C . n 
C 1 84  LEU 84  85  85  LEU LEU C . n 
C 1 85  GLU 85  86  86  GLU GLU C . n 
C 1 86  THR 86  87  87  THR THR C . n 
C 1 87  ALA 87  88  88  ALA ALA C . n 
C 1 88  LEU 88  89  89  LEU LEU C . n 
C 1 89  ARG 89  90  90  ARG ARG C . n 
C 1 90  ASP 90  91  91  ASP ASP C . n 
C 1 91  SER 91  92  92  SER SER C . n 
C 1 92  SER 92  93  93  SER SER C . n 
C 1 93  ARG 93  94  94  ARG ARG C . n 
C 1 94  VAL 94  95  95  VAL VAL C . n 
C 1 95  LEU 95  96  96  LEU LEU C . n 
C 1 96  GLN 96  97  97  GLN GLN C . n 
C 1 97  ALA 97  98  98  ALA ALA C . n 
C 1 98  MET 98  99  99  MET MET C . n 
C 1 99  LEU 99  100 100 LEU LEU C . n 
C 1 100 ALA 100 101 101 ALA ALA C . n 
C 1 101 THR 101 102 102 THR THR C . n 
C 1 102 GLN 102 103 103 GLN GLN C . n 
C 1 103 LEU 103 104 104 LEU LEU C . n 
C 1 104 ARG 104 105 105 ARG ARG C . n 
C 1 105 SER 105 106 106 SER SER C . n 
C 1 106 PHE 106 107 107 PHE PHE C . n 
C 1 107 ASP 107 108 108 ASP ASP C . n 
C 1 108 ASP 108 109 109 ASP ASP C . n 
C 1 109 HIS 109 110 110 HIS HIS C . n 
C 1 110 PHE 110 111 111 PHE PHE C . n 
C 1 111 GLN 111 112 112 GLN GLN C . n 
C 1 112 HIS 112 113 113 HIS HIS C . n 
C 1 113 LEU 113 114 114 LEU LEU C . n 
C 1 114 LEU 114 115 115 LEU LEU C . n 
C 1 115 ASN 115 116 116 ASN ASN C . n 
C 1 116 ASP 116 117 117 ASP ASP C . n 
C 1 117 SER 117 118 118 SER SER C . n 
C 1 118 GLU 118 119 119 GLU GLU C . n 
C 1 119 ARG 119 120 120 ARG ARG C . n 
C 1 120 THR 120 121 121 THR THR C . n 
C 1 121 LEU 121 122 122 LEU LEU C . n 
C 1 122 GLN 122 123 123 GLN GLN C . n 
C 1 123 ALA 123 124 124 ALA ALA C . n 
C 1 124 THR 124 125 125 THR THR C . n 
C 1 125 PHE 125 126 126 PHE PHE C . n 
C 1 126 PRO 126 127 127 PRO PRO C . n 
C 1 127 GLY 127 128 128 GLY GLY C . n 
C 1 128 ALA 128 129 129 ALA ALA C . n 
C 1 129 PHE 129 130 130 PHE PHE C . n 
C 1 130 GLY 130 131 131 GLY GLY C . n 
C 1 131 GLU 131 132 132 GLU GLU C . n 
C 1 132 LEU 132 133 133 LEU LEU C . n 
C 1 133 TYR 133 134 134 TYR TYR C . n 
C 1 134 THR 134 135 135 THR THR C . n 
C 1 135 GLN 135 136 136 GLN GLN C . n 
C 1 136 ASN 136 137 137 ASN ASN C . n 
C 1 137 ALA 137 138 138 ALA ALA C . n 
C 1 138 ARG 138 139 139 ARG ARG C . n 
C 1 139 ALA 139 140 140 ALA ALA C . n 
C 1 140 PHE 140 141 141 PHE PHE C . n 
C 1 141 ARG 141 142 142 ARG ARG C . n 
C 1 142 ASP 142 143 143 ASP ASP C . n 
C 1 143 LEU 143 144 144 LEU LEU C . n 
C 1 144 TYR 144 145 145 TYR TYR C . n 
C 1 145 SER 145 146 146 SER SER C . n 
C 1 146 GLU 146 147 147 GLU GLU C . n 
C 1 147 LEU 147 148 148 LEU LEU C . n 
C 1 148 ARG 148 149 149 ARG ARG C . n 
C 1 149 LEU 149 150 150 LEU LEU C . n 
C 1 150 TYR 150 151 151 TYR TYR C . n 
C 1 151 TYR 151 152 152 TYR TYR C . n 
C 1 152 ARG 152 153 153 ARG ARG C . n 
C 1 153 GLY 153 154 154 GLY GLY C . n 
C 1 154 ALA 154 155 155 ALA ALA C . n 
C 1 155 ASN 155 156 156 ASN ASN C . n 
C 1 156 LEU 156 157 157 LEU LEU C . n 
C 1 157 HIS 157 158 158 HIS HIS C . n 
C 1 158 LEU 158 159 159 LEU LEU C . n 
C 1 159 GLU 159 160 160 GLU GLU C . n 
C 1 160 GLU 160 161 161 GLU GLU C . n 
C 1 161 THR 161 162 162 THR THR C . n 
C 1 162 LEU 162 163 163 LEU LEU C . n 
C 1 163 ALA 163 164 164 ALA ALA C . n 
C 1 164 GLU 164 165 165 GLU GLU C . n 
C 1 165 PHE 165 166 166 PHE PHE C . n 
C 1 166 TRP 166 167 167 TRP TRP C . n 
C 1 167 ALA 167 168 168 ALA ALA C . n 
C 1 168 ARG 168 169 169 ARG ARG C . n 
C 1 169 LEU 169 170 170 LEU LEU C . n 
C 1 170 LEU 170 171 171 LEU LEU C . n 
C 1 171 GLU 171 172 172 GLU GLU C . n 
C 1 172 ARG 172 173 173 ARG ARG C . n 
C 1 173 LEU 173 174 174 LEU LEU C . n 
C 1 174 PHE 174 175 175 PHE PHE C . n 
C 1 175 LYS 175 176 176 LYS LYS C . n 
C 1 176 GLN 176 177 177 GLN GLN C . n 
C 1 177 LEU 177 178 178 LEU LEU C . n 
C 1 178 HIS 178 179 179 HIS HIS C . n 
C 1 179 PRO 179 180 180 PRO PRO C . n 
C 1 180 GLN 180 181 181 GLN GLN C . n 
C 1 181 LEU 181 182 182 LEU LEU C . n 
C 1 182 LEU 182 183 183 LEU LEU C . n 
C 1 183 LEU 183 184 184 LEU LEU C . n 
C 1 184 PRO 184 185 185 PRO PRO C . n 
C 1 185 ASP 185 186 ?   ?   ?   C . n 
C 1 186 ASP 186 187 ?   ?   ?   C . n 
C 1 187 TYR 187 188 ?   ?   ?   C . n 
C 1 188 LEU 188 189 ?   ?   ?   C . n 
C 1 189 ASP 189 190 ?   ?   ?   C . n 
C 1 190 CYS 190 191 ?   ?   ?   C . n 
C 1 191 LEU 191 192 ?   ?   ?   C . n 
C 1 192 GLY 192 193 ?   ?   ?   C . n 
C 1 193 LYS 193 194 ?   ?   ?   C . n 
C 1 194 GLN 194 195 ?   ?   ?   C . n 
C 1 195 ALA 195 196 ?   ?   ?   C . n 
C 1 196 GLU 196 197 ?   ?   ?   C . n 
C 1 197 ALA 197 198 198 ALA ALA C . n 
C 1 198 LEU 198 199 199 LEU LEU C . n 
C 1 199 ARG 199 200 200 ARG ARG C . n 
C 1 200 PRO 200 201 201 PRO PRO C . n 
C 1 201 PHE 201 202 202 PHE PHE C . n 
C 1 202 GLY 202 203 203 GLY GLY C . n 
C 1 203 GLU 203 204 204 GLU GLU C . n 
C 1 204 ALA 204 205 205 ALA ALA C . n 
C 1 205 PRO 205 206 206 PRO PRO C . n 
C 1 206 ARG 206 207 207 ARG ARG C . n 
C 1 207 GLU 207 208 208 GLU GLU C . n 
C 1 208 LEU 208 209 209 LEU LEU C . n 
C 1 209 ARG 209 210 210 ARG ARG C . n 
C 1 210 LEU 210 211 211 LEU LEU C . n 
C 1 211 ARG 211 212 212 ARG ARG C . n 
C 1 212 ALA 212 213 213 ALA ALA C . n 
C 1 213 THR 213 214 214 THR THR C . n 
C 1 214 ARG 214 215 215 ARG ARG C . n 
C 1 215 ALA 215 216 216 ALA ALA C . n 
C 1 216 PHE 216 217 217 PHE PHE C . n 
C 1 217 VAL 217 218 218 VAL VAL C . n 
C 1 218 ALA 218 219 219 ALA ALA C . n 
C 1 219 ALA 219 220 220 ALA ALA C . n 
C 1 220 ARG 220 221 221 ARG ARG C . n 
C 1 221 SER 221 222 222 SER SER C . n 
C 1 222 PHE 222 223 223 PHE PHE C . n 
C 1 223 VAL 223 224 224 VAL VAL C . n 
C 1 224 GLN 224 225 225 GLN GLN C . n 
C 1 225 GLY 225 226 226 GLY GLY C . n 
C 1 226 LEU 226 227 227 LEU LEU C . n 
C 1 227 GLY 227 228 228 GLY GLY C . n 
C 1 228 VAL 228 229 229 VAL VAL C . n 
C 1 229 ALA 229 230 230 ALA ALA C . n 
C 1 230 SER 230 231 231 SER SER C . n 
C 1 231 ASP 231 232 232 ASP ASP C . n 
C 1 232 VAL 232 233 233 VAL VAL C . n 
C 1 233 VAL 233 234 234 VAL VAL C . n 
C 1 234 ARG 234 235 235 ARG ARG C . n 
C 1 235 LYS 235 236 236 LYS LYS C . n 
C 1 236 VAL 236 237 237 VAL VAL C . n 
C 1 237 ALA 237 238 238 ALA ALA C . n 
C 1 238 GLN 238 239 239 GLN GLN C . n 
C 1 239 VAL 239 240 240 VAL VAL C . n 
C 1 240 PRO 240 241 241 PRO PRO C . n 
C 1 241 LEU 241 242 242 LEU LEU C . n 
C 1 242 GLY 242 243 243 GLY GLY C . n 
C 1 243 PRO 243 244 244 PRO PRO C . n 
C 1 244 GLU 244 245 245 GLU GLU C . n 
C 1 245 CYS 245 246 246 CYS CYS C . n 
C 1 246 SER 246 247 247 SER SER C . n 
C 1 247 ARG 247 248 248 ARG ARG C . n 
C 1 248 ALA 248 249 249 ALA ALA C . n 
C 1 249 VAL 249 250 250 VAL VAL C . n 
C 1 250 MET 250 251 251 MET MET C . n 
C 1 251 LYS 251 252 252 LYS LYS C . n 
C 1 252 LEU 252 253 253 LEU LEU C . n 
C 1 253 VAL 253 254 254 VAL VAL C . n 
C 1 254 TYR 254 255 255 TYR TYR C . n 
C 1 255 CYS 255 256 256 CYS CYS C . n 
C 1 256 ALA 256 257 257 ALA ALA C . n 
C 1 257 HIS 257 258 258 HIS HIS C . n 
C 1 258 CYS 258 259 259 CYS CYS C . n 
C 1 259 LEU 259 260 260 LEU LEU C . n 
C 1 260 GLY 260 261 261 GLY GLY C . n 
C 1 261 VAL 261 262 262 VAL VAL C . n 
C 1 262 PRO 262 263 263 PRO PRO C . n 
C 1 263 GLY 263 264 264 GLY GLY C . n 
C 1 264 ALA 264 265 265 ALA ALA C . n 
C 1 265 ARG 265 266 266 ARG ARG C . n 
C 1 266 PRO 266 267 267 PRO PRO C . n 
C 1 267 CYS 267 268 268 CYS CYS C . n 
C 1 268 PRO 268 269 269 PRO PRO C . n 
C 1 269 ASP 269 270 270 ASP ASP C . n 
C 1 270 TYR 270 271 271 TYR TYR C . n 
C 1 271 CYS 271 272 272 CYS CYS C . n 
C 1 272 ARG 272 273 273 ARG ARG C . n 
C 1 273 ASN 273 274 274 ASN ASN C . n 
C 1 274 VAL 274 275 275 VAL VAL C . n 
C 1 275 LEU 275 276 276 LEU LEU C . n 
C 1 276 LYS 276 277 277 LYS LYS C . n 
C 1 277 GLY 277 278 278 GLY GLY C . n 
C 1 278 CYS 278 279 279 CYS CYS C . n 
C 1 279 LEU 279 280 280 LEU LEU C . n 
C 1 280 ALA 280 281 281 ALA ALA C . n 
C 1 281 ASN 281 282 282 ASN ASN C . n 
C 1 282 GLN 282 283 283 GLN GLN C . n 
C 1 283 ALA 283 284 284 ALA ALA C . n 
C 1 284 ASP 284 285 285 ASP ASP C . n 
C 1 285 LEU 285 286 286 LEU LEU C . n 
C 1 286 ASP 286 287 287 ASP ASP C . n 
C 1 287 ALA 287 288 288 ALA ALA C . n 
C 1 288 GLU 288 289 289 GLU GLU C . n 
C 1 289 TRP 289 290 290 TRP TRP C . n 
C 1 290 ARG 290 291 291 ARG ARG C . n 
C 1 291 ASN 291 292 292 ASN ASN C . n 
C 1 292 LEU 292 293 293 LEU LEU C . n 
C 1 293 LEU 293 294 294 LEU LEU C . n 
C 1 294 ASP 294 295 295 ASP ASP C . n 
C 1 295 SER 295 296 296 SER SER C . n 
C 1 296 MET 296 297 297 MET MET C . n 
C 1 297 VAL 297 298 298 VAL VAL C . n 
C 1 298 LEU 298 299 299 LEU LEU C . n 
C 1 299 ILE 299 300 300 ILE ILE C . n 
C 1 300 THR 300 301 301 THR THR C . n 
C 1 301 ASP 301 302 302 ASP ASP C . n 
C 1 302 LYS 302 303 303 LYS LYS C . n 
C 1 303 PHE 303 304 304 PHE PHE C . n 
C 1 304 TRP 304 305 305 TRP TRP C . n 
C 1 305 GLY 305 306 306 GLY GLY C . n 
C 1 306 THR 306 307 307 THR THR C . n 
C 1 307 SER 307 308 308 SER SER C . n 
C 1 308 GLY 308 309 309 GLY GLY C . n 
C 1 309 VAL 309 310 310 VAL VAL C . n 
C 1 310 GLU 310 311 311 GLU GLU C . n 
C 1 311 SER 311 312 312 SER SER C . n 
C 1 312 VAL 312 313 313 VAL VAL C . n 
C 1 313 ILE 313 314 314 ILE ILE C . n 
C 1 314 GLY 314 315 315 GLY GLY C . n 
C 1 315 SER 315 316 316 SER SER C . n 
C 1 316 VAL 316 317 317 VAL VAL C . n 
C 1 317 HIS 317 318 318 HIS HIS C . n 
C 1 318 THR 318 319 319 THR THR C . n 
C 1 319 TRP 319 320 320 TRP TRP C . n 
C 1 320 LEU 320 321 321 LEU LEU C . n 
C 1 321 ALA 321 322 322 ALA ALA C . n 
C 1 322 GLU 322 323 323 GLU GLU C . n 
C 1 323 ALA 323 324 324 ALA ALA C . n 
C 1 324 ILE 324 325 325 ILE ILE C . n 
C 1 325 ASN 325 326 326 ASN ASN C . n 
C 1 326 ALA 326 327 327 ALA ALA C . n 
C 1 327 LEU 327 328 328 LEU LEU C . n 
C 1 328 GLN 328 329 329 GLN GLN C . n 
C 1 329 ASP 329 330 330 ASP ASP C . n 
C 1 330 ASN 330 331 331 ASN ASN C . n 
C 1 331 ARG 331 332 332 ARG ARG C . n 
C 1 332 ASP 332 333 333 ASP ASP C . n 
C 1 333 THR 333 334 334 THR THR C . n 
C 1 334 LEU 334 335 335 LEU LEU C . n 
C 1 335 THR 335 336 336 THR THR C . n 
C 1 336 ALA 336 337 337 ALA ALA C . n 
C 1 337 LYS 337 338 338 LYS LYS C . n 
C 1 338 VAL 338 339 339 VAL VAL C . n 
C 1 339 ILE 339 340 ?   ?   ?   C . n 
C 1 340 GLN 340 341 ?   ?   ?   C . n 
C 1 341 GLY 341 342 ?   ?   ?   C . n 
C 1 342 CYS 342 343 ?   ?   ?   C . n 
C 1 343 GLY 343 344 ?   ?   ?   C . n 
C 1 344 ASN 344 345 ?   ?   ?   C . n 
C 1 345 PRO 345 346 ?   ?   ?   C . n 
C 1 346 LYS 346 347 ?   ?   ?   C . n 
C 1 347 VAL 347 348 ?   ?   ?   C . n 
C 1 348 ASN 348 349 ?   ?   ?   C . n 
C 1 349 PRO 349 350 ?   ?   ?   C . n 
C 1 350 GLN 350 351 ?   ?   ?   C . n 
C 1 351 GLY 351 352 ?   ?   ?   C . n 
C 1 352 PRO 352 353 ?   ?   ?   C . n 
C 1 353 GLY 353 354 ?   ?   ?   C . n 
C 1 354 PRO 354 355 ?   ?   ?   C . n 
C 1 355 GLU 355 356 ?   ?   ?   C . n 
C 1 356 GLU 356 357 ?   ?   ?   C . n 
C 1 357 LYS 357 358 ?   ?   ?   C . n 
C 1 358 ARG 358 359 ?   ?   ?   C . n 
C 1 359 ARG 359 360 ?   ?   ?   C . n 
C 1 360 ARG 360 361 ?   ?   ?   C . n 
C 1 361 GLY 361 362 ?   ?   ?   C . n 
C 1 362 LYS 362 363 ?   ?   ?   C . n 
C 1 363 LEU 363 364 ?   ?   ?   C . n 
C 1 364 ALA 364 365 ?   ?   ?   C . n 
C 1 365 PRO 365 366 ?   ?   ?   C . n 
C 1 366 ARG 366 367 367 ARG ARG C . n 
C 1 367 GLU 367 368 368 GLU GLU C . n 
C 1 368 ARG 368 369 369 ARG ARG C . n 
C 1 369 PRO 369 370 370 PRO PRO C . n 
C 1 370 PRO 370 371 371 PRO PRO C . n 
C 1 371 SER 371 372 372 SER SER C . n 
C 1 372 GLY 372 373 373 GLY GLY C . n 
C 1 373 THR 373 374 374 THR THR C . n 
C 1 374 LEU 374 375 375 LEU LEU C . n 
C 1 375 GLU 375 376 376 GLU GLU C . n 
C 1 376 LYS 376 377 377 LYS LYS C . n 
C 1 377 LEU 377 378 378 LEU LEU C . n 
C 1 378 VAL 378 379 379 VAL VAL C . n 
C 1 379 SER 379 380 380 SER SER C . n 
C 1 380 GLU 380 381 381 GLU GLU C . n 
C 1 381 ALA 381 382 382 ALA ALA C . n 
C 1 382 LYS 382 383 383 LYS LYS C . n 
C 1 383 ALA 383 384 384 ALA ALA C . n 
C 1 384 GLN 384 385 385 GLN GLN C . n 
C 1 385 LEU 385 386 386 LEU LEU C . n 
C 1 386 ARG 386 387 387 ARG ARG C . n 
C 1 387 ASP 387 388 388 ASP ASP C . n 
C 1 388 VAL 388 389 389 VAL VAL C . n 
C 1 389 GLN 389 390 390 GLN GLN C . n 
C 1 390 ASP 390 391 391 ASP ASP C . n 
C 1 391 PHE 391 392 392 PHE PHE C . n 
C 1 392 TRP 392 393 393 TRP TRP C . n 
C 1 393 ILE 393 394 394 ILE ILE C . n 
C 1 394 SER 394 395 395 SER SER C . n 
C 1 395 LEU 395 396 396 LEU LEU C . n 
C 1 396 PRO 396 397 397 PRO PRO C . n 
C 1 397 GLY 397 398 398 GLY GLY C . n 
C 1 398 THR 398 399 399 THR THR C . n 
C 1 399 LEU 399 400 400 LEU LEU C . n 
C 1 400 CYS 400 401 401 CYS CYS C . n 
C 1 401 SER 401 402 402 SER SER C . n 
C 1 402 GLU 402 403 403 GLU GLU C . n 
C 1 403 LYS 403 404 404 LYS LYS C . n 
C 1 404 MET 404 405 405 MET MET C . n 
C 1 405 ALA 405 406 406 ALA ALA C . n 
C 1 406 LEU 406 407 ?   ?   ?   C . n 
C 1 407 SER 407 408 ?   ?   ?   C . n 
C 1 408 THR 408 409 ?   ?   ?   C . n 
C 1 409 ALA 409 410 ?   ?   ?   C . n 
C 1 410 SER 410 411 ?   ?   ?   C . n 
C 1 411 ASP 411 412 ?   ?   ?   C . n 
C 1 412 ASP 412 413 ?   ?   ?   C . n 
C 1 413 ARG 413 414 414 ARG ARG C . n 
C 1 414 CYS 414 415 415 CYS CYS C . n 
C 1 415 TRP 415 416 416 TRP TRP C . n 
C 1 416 ASN 416 417 417 ASN ASN C . n 
C 1 417 GLY 417 418 418 GLY GLY C . n 
C 1 418 MET 418 419 419 MET MET C . n 
C 1 419 ALA 419 420 420 ALA ALA C . n 
C 1 420 ARG 420 421 421 ARG ARG C . n 
C 1 421 GLY 421 422 422 GLY GLY C . n 
C 1 422 ARG 422 423 423 ARG ARG C . n 
C 1 423 TYR 423 424 424 TYR TYR C . n 
C 1 424 LEU 424 425 425 LEU LEU C . n 
C 1 425 PRO 425 426 426 PRO PRO C . n 
C 1 426 GLU 426 427 427 GLU GLU C . n 
C 1 427 VAL 427 428 428 VAL VAL C . n 
C 1 428 MET 428 429 429 MET MET C . n 
C 1 429 GLY 429 430 430 GLY GLY C . n 
C 1 430 ASP 430 431 431 ASP ASP C . n 
C 1 431 GLY 431 432 432 GLY GLY C . n 
C 1 432 LEU 432 433 433 LEU LEU C . n 
C 1 433 ALA 433 434 434 ALA ALA C . n 
C 1 434 ASN 434 435 435 ASN ASN C . n 
C 1 435 GLN 435 436 436 GLN GLN C . n 
C 1 436 ILE 436 437 437 ILE ILE C . n 
C 1 437 ASN 437 438 438 ASN ASN C . n 
C 1 438 ASN 438 439 439 ASN ASN C . n 
C 1 439 PRO 439 440 440 PRO PRO C . n 
C 1 440 GLU 440 441 441 GLU GLU C . n 
C 1 441 VAL 441 442 442 VAL VAL C . n 
C 1 442 GLU 442 443 443 GLU GLU C . n 
C 1 443 VAL 443 444 444 VAL VAL C . n 
C 1 444 ASP 444 445 445 ASP ASP C . n 
C 1 445 ILE 445 446 446 ILE ILE C . n 
C 1 446 THR 446 447 447 THR THR C . n 
C 1 447 LYS 447 448 448 LYS LYS C . n 
C 1 448 PRO 448 449 449 PRO PRO C . n 
C 1 449 ASP 449 450 450 ASP ASP C . n 
C 1 450 MET 450 451 451 MET MET C . n 
C 1 451 THR 451 452 452 THR THR C . n 
C 1 452 ILE 452 453 453 ILE ILE C . n 
C 1 453 ARG 453 454 454 ARG ARG C . n 
C 1 454 GLN 454 455 455 GLN GLN C . n 
C 1 455 GLN 455 456 456 GLN GLN C . n 
C 1 456 ILE 456 457 457 ILE ILE C . n 
C 1 457 MET 457 458 458 MET MET C . n 
C 1 458 GLN 458 459 459 GLN GLN C . n 
C 1 459 LEU 459 460 460 LEU LEU C . n 
C 1 460 LYS 460 461 461 LYS LYS C . n 
C 1 461 ILE 461 462 462 ILE ILE C . n 
C 1 462 MET 462 463 463 MET MET C . n 
C 1 463 THR 463 464 464 THR THR C . n 
C 1 464 ASN 464 465 465 ASN ASN C . n 
C 1 465 ARG 465 466 466 ARG ARG C . n 
C 1 466 LEU 466 467 467 LEU LEU C . n 
C 1 467 ARG 467 468 468 ARG ARG C . n 
C 1 468 SER 468 469 469 SER SER C . n 
C 1 469 ALA 469 470 470 ALA ALA C . n 
C 1 470 TYR 470 471 471 TYR TYR C . n 
C 1 471 ASN 471 472 472 ASN ASN C . n 
C 1 472 GLY 472 473 473 GLY GLY C . n 
C 1 473 ASN 473 474 474 ASN ASN C . n 
C 1 474 ASP 474 475 ?   ?   ?   C . n 
C 1 475 VAL 475 476 ?   ?   ?   C . n 
C 1 476 ASP 476 477 ?   ?   ?   C . n 
C 1 477 PHE 477 478 ?   ?   ?   C . n 
C 1 478 GLN 478 479 ?   ?   ?   C . n 
C 1 479 ASP 479 480 ?   ?   ?   C . n 
C 1 480 ALA 480 481 ?   ?   ?   C . n 
C 1 481 SER 481 482 ?   ?   ?   C . n 
C 1 482 ASP 482 483 ?   ?   ?   C . n 
C 1 483 ASP 483 484 ?   ?   ?   C . n 
C 1 484 GLY 484 485 ?   ?   ?   C . n 
C 1 485 ALA 485 486 ?   ?   ?   C . n 
C 1 486 GLY 486 487 ?   ?   ?   C . n 
C 1 487 ALA 487 488 ?   ?   ?   C . n 
C 1 488 GLY 488 489 ?   ?   ?   C . n 
C 1 489 ALA 489 490 ?   ?   ?   C . n 
C 1 490 GLY 490 491 ?   ?   ?   C . n 
C 1 491 ASP 491 492 ?   ?   ?   C . n 
C 1 492 GLY 492 493 ?   ?   ?   C . n 
C 1 493 CYS 493 494 ?   ?   ?   C . n 
C 1 494 LEU 494 495 ?   ?   ?   C . n 
C 1 495 ASP 495 496 ?   ?   ?   C . n 
C 1 496 ASP 496 497 ?   ?   ?   C . n 
C 1 497 LEU 497 498 ?   ?   ?   C . n 
C 1 498 CYS 498 499 ?   ?   ?   C . n 
C 1 499 SER 499 500 ?   ?   ?   C . n 
C 1 500 ARG 500 501 ?   ?   ?   C . n 
C 1 501 LYS 501 502 ?   ?   ?   C . n 
C 1 502 VAL 502 503 ?   ?   ?   C . n 
C 1 503 SER 503 504 ?   ?   ?   C . n 
C 1 504 ARG 504 505 ?   ?   ?   C . n 
C 1 505 LYS 505 506 ?   ?   ?   C . n 
C 1 506 SER 506 507 ?   ?   ?   C . n 
C 1 507 SER 507 508 ?   ?   ?   C . n 
C 1 508 SER 508 509 ?   ?   ?   C . n 
C 1 509 SER 509 510 ?   ?   ?   C . n 
C 1 510 ARG 510 511 ?   ?   ?   C . n 
C 1 511 THR 511 512 ?   ?   ?   C . n 
C 1 512 PRO 512 513 ?   ?   ?   C . n 
C 1 513 LEU 513 514 ?   ?   ?   C . n 
C 1 514 THR 514 515 ?   ?   ?   C . n 
C 1 515 HIS 515 516 ?   ?   ?   C . n 
C 1 516 ALA 516 517 ?   ?   ?   C . n 
C 1 517 LEU 517 518 ?   ?   ?   C . n 
C 1 518 PRO 518 519 ?   ?   ?   C . n 
C 1 519 GLY 519 520 ?   ?   ?   C . n 
C 1 520 LEU 520 521 ?   ?   ?   C . n 
C 1 521 SER 521 522 ?   ?   ?   C . n 
C 1 522 GLU 522 523 ?   ?   ?   C . n 
C 1 523 GLN 523 524 ?   ?   ?   C . n 
C 1 524 GLU 524 525 ?   ?   ?   C . n 
C 1 525 GLY 525 526 ?   ?   ?   C . n 
C 1 526 GLN 526 527 ?   ?   ?   C . n 
D 1 1   ALA 1   2   ?   ?   ?   D . n 
D 1 2   PRO 2   3   ?   ?   ?   D . n 
D 1 3   GLN 3   4   ?   ?   ?   D . n 
D 1 4   LEU 4   5   ?   ?   ?   D . n 
D 1 5   HIS 5   6   ?   ?   ?   D . n 
D 1 6   HIS 6   7   ?   ?   ?   D . n 
D 1 7   HIS 7   8   ?   ?   ?   D . n 
D 1 8   HIS 8   9   ?   ?   ?   D . n 
D 1 9   HIS 9   10  ?   ?   ?   D . n 
D 1 10  HIS 10  11  ?   ?   ?   D . n 
D 1 11  ASP 11  12  ?   ?   ?   D . n 
D 1 12  LEU 12  13  ?   ?   ?   D . n 
D 1 13  TYR 13  14  ?   ?   ?   D . n 
D 1 14  GLU 14  15  ?   ?   ?   D . n 
D 1 15  ASN 15  16  ?   ?   ?   D . n 
D 1 16  LEU 16  17  ?   ?   ?   D . n 
D 1 17  TYR 17  18  ?   ?   ?   D . n 
D 1 18  PHE 18  19  ?   ?   ?   D . n 
D 1 19  GLN 19  20  ?   ?   ?   D . n 
D 1 20  GLY 20  21  ?   ?   ?   D . n 
D 1 21  LYS 21  22  ?   ?   ?   D . n 
D 1 22  LEU 22  23  ?   ?   ?   D . n 
D 1 23  ASP 23  24  ?   ?   ?   D . n 
D 1 24  PRO 24  25  ?   ?   ?   D . n 
D 1 25  ALA 25  26  ?   ?   ?   D . n 
D 1 26  SER 26  27  ?   ?   ?   D . n 
D 1 27  LYS 27  28  ?   ?   ?   D . n 
D 1 28  SER 28  29  29  SER SER D . n 
D 1 29  ARG 29  30  30  ARG ARG D . n 
D 1 30  SER 30  31  31  SER SER D . n 
D 1 31  CYS 31  32  32  CYS CYS D . n 
D 1 32  GLY 32  33  33  GLY GLY D . n 
D 1 33  GLU 33  34  34  GLU GLU D . n 
D 1 34  VAL 34  35  35  VAL VAL D . n 
D 1 35  ARG 35  36  36  ARG ARG D . n 
D 1 36  GLN 36  37  37  GLN GLN D . n 
D 1 37  ILE 37  38  38  ILE ILE D . n 
D 1 38  TYR 38  39  39  TYR TYR D . n 
D 1 39  GLY 39  40  40  GLY GLY D . n 
D 1 40  ALA 40  41  41  ALA ALA D . n 
D 1 41  LYS 41  42  42  LYS LYS D . n 
D 1 42  GLY 42  43  43  GLY GLY D . n 
D 1 43  PHE 43  44  44  PHE PHE D . n 
D 1 44  SER 44  45  45  SER SER D . n 
D 1 45  LEU 45  46  46  LEU LEU D . n 
D 1 46  SER 46  47  47  SER SER D . n 
D 1 47  ASP 47  48  48  ASP ASP D . n 
D 1 48  VAL 48  49  49  VAL VAL D . n 
D 1 49  PRO 49  50  50  PRO PRO D . n 
D 1 50  GLN 50  51  51  GLN GLN D . n 
D 1 51  ALA 51  52  52  ALA ALA D . n 
D 1 52  GLU 52  53  53  GLU GLU D . n 
D 1 53  ILE 53  54  54  ILE ILE D . n 
D 1 54  SER 54  55  55  SER SER D . n 
D 1 55  GLY 55  56  56  GLY GLY D . n 
D 1 56  GLU 56  57  57  GLU GLU D . n 
D 1 57  HIS 57  58  58  HIS HIS D . n 
D 1 58  LEU 58  59  59  LEU LEU D . n 
D 1 59  ARG 59  60  60  ARG ARG D . n 
D 1 60  ILE 60  61  61  ILE ILE D . n 
D 1 61  CYS 61  62  62  CYS CYS D . n 
D 1 62  PRO 62  63  63  PRO PRO D . n 
D 1 63  GLN 63  64  64  GLN GLN D . n 
D 1 64  GLY 64  65  65  GLY GLY D . n 
D 1 65  TYR 65  66  66  TYR TYR D . n 
D 1 66  THR 66  67  67  THR THR D . n 
D 1 67  CYS 67  68  68  CYS CYS D . n 
D 1 68  CYS 68  69  69  CYS CYS D . n 
D 1 69  THR 69  70  70  THR THR D . n 
D 1 70  SER 70  71  71  SER SER D . n 
D 1 71  GLU 71  72  72  GLU GLU D . n 
D 1 72  MET 72  73  73  MET MET D . n 
D 1 73  GLU 73  74  74  GLU GLU D . n 
D 1 74  GLU 74  75  75  GLU GLU D . n 
D 1 75  ASN 75  76  76  ASN ASN D . n 
D 1 76  LEU 76  77  77  LEU LEU D . n 
D 1 77  ALA 77  78  78  ALA ALA D . n 
D 1 78  ASN 78  79  79  ASN ASN D . n 
D 1 79  ARG 79  80  80  ARG ARG D . n 
D 1 80  SER 80  81  81  SER SER D . n 
D 1 81  HIS 81  82  82  HIS HIS D . n 
D 1 82  ALA 82  83  83  ALA ALA D . n 
D 1 83  GLU 83  84  84  GLU GLU D . n 
D 1 84  LEU 84  85  85  LEU LEU D . n 
D 1 85  GLU 85  86  86  GLU GLU D . n 
D 1 86  THR 86  87  87  THR THR D . n 
D 1 87  ALA 87  88  88  ALA ALA D . n 
D 1 88  LEU 88  89  89  LEU LEU D . n 
D 1 89  ARG 89  90  90  ARG ARG D . n 
D 1 90  ASP 90  91  91  ASP ASP D . n 
D 1 91  SER 91  92  92  SER SER D . n 
D 1 92  SER 92  93  93  SER SER D . n 
D 1 93  ARG 93  94  94  ARG ARG D . n 
D 1 94  VAL 94  95  95  VAL VAL D . n 
D 1 95  LEU 95  96  96  LEU LEU D . n 
D 1 96  GLN 96  97  97  GLN GLN D . n 
D 1 97  ALA 97  98  98  ALA ALA D . n 
D 1 98  MET 98  99  99  MET MET D . n 
D 1 99  LEU 99  100 100 LEU LEU D . n 
D 1 100 ALA 100 101 101 ALA ALA D . n 
D 1 101 THR 101 102 102 THR THR D . n 
D 1 102 GLN 102 103 103 GLN GLN D . n 
D 1 103 LEU 103 104 104 LEU LEU D . n 
D 1 104 ARG 104 105 105 ARG ARG D . n 
D 1 105 SER 105 106 106 SER SER D . n 
D 1 106 PHE 106 107 107 PHE PHE D . n 
D 1 107 ASP 107 108 108 ASP ASP D . n 
D 1 108 ASP 108 109 109 ASP ASP D . n 
D 1 109 HIS 109 110 110 HIS HIS D . n 
D 1 110 PHE 110 111 111 PHE PHE D . n 
D 1 111 GLN 111 112 112 GLN GLN D . n 
D 1 112 HIS 112 113 113 HIS HIS D . n 
D 1 113 LEU 113 114 114 LEU LEU D . n 
D 1 114 LEU 114 115 115 LEU LEU D . n 
D 1 115 ASN 115 116 116 ASN ASN D . n 
D 1 116 ASP 116 117 117 ASP ASP D . n 
D 1 117 SER 117 118 118 SER SER D . n 
D 1 118 GLU 118 119 119 GLU GLU D . n 
D 1 119 ARG 119 120 120 ARG ARG D . n 
D 1 120 THR 120 121 121 THR THR D . n 
D 1 121 LEU 121 122 122 LEU LEU D . n 
D 1 122 GLN 122 123 123 GLN GLN D . n 
D 1 123 ALA 123 124 124 ALA ALA D . n 
D 1 124 THR 124 125 125 THR THR D . n 
D 1 125 PHE 125 126 126 PHE PHE D . n 
D 1 126 PRO 126 127 127 PRO PRO D . n 
D 1 127 GLY 127 128 128 GLY GLY D . n 
D 1 128 ALA 128 129 129 ALA ALA D . n 
D 1 129 PHE 129 130 130 PHE PHE D . n 
D 1 130 GLY 130 131 131 GLY GLY D . n 
D 1 131 GLU 131 132 132 GLU GLU D . n 
D 1 132 LEU 132 133 133 LEU LEU D . n 
D 1 133 TYR 133 134 134 TYR TYR D . n 
D 1 134 THR 134 135 135 THR THR D . n 
D 1 135 GLN 135 136 136 GLN GLN D . n 
D 1 136 ASN 136 137 137 ASN ASN D . n 
D 1 137 ALA 137 138 138 ALA ALA D . n 
D 1 138 ARG 138 139 139 ARG ARG D . n 
D 1 139 ALA 139 140 140 ALA ALA D . n 
D 1 140 PHE 140 141 141 PHE PHE D . n 
D 1 141 ARG 141 142 142 ARG ARG D . n 
D 1 142 ASP 142 143 143 ASP ASP D . n 
D 1 143 LEU 143 144 144 LEU LEU D . n 
D 1 144 TYR 144 145 145 TYR TYR D . n 
D 1 145 SER 145 146 146 SER SER D . n 
D 1 146 GLU 146 147 147 GLU GLU D . n 
D 1 147 LEU 147 148 148 LEU LEU D . n 
D 1 148 ARG 148 149 149 ARG ARG D . n 
D 1 149 LEU 149 150 150 LEU LEU D . n 
D 1 150 TYR 150 151 151 TYR TYR D . n 
D 1 151 TYR 151 152 152 TYR TYR D . n 
D 1 152 ARG 152 153 153 ARG ARG D . n 
D 1 153 GLY 153 154 154 GLY GLY D . n 
D 1 154 ALA 154 155 155 ALA ALA D . n 
D 1 155 ASN 155 156 156 ASN ASN D . n 
D 1 156 LEU 156 157 157 LEU LEU D . n 
D 1 157 HIS 157 158 158 HIS HIS D . n 
D 1 158 LEU 158 159 159 LEU LEU D . n 
D 1 159 GLU 159 160 160 GLU GLU D . n 
D 1 160 GLU 160 161 161 GLU GLU D . n 
D 1 161 THR 161 162 162 THR THR D . n 
D 1 162 LEU 162 163 163 LEU LEU D . n 
D 1 163 ALA 163 164 164 ALA ALA D . n 
D 1 164 GLU 164 165 165 GLU GLU D . n 
D 1 165 PHE 165 166 166 PHE PHE D . n 
D 1 166 TRP 166 167 167 TRP TRP D . n 
D 1 167 ALA 167 168 168 ALA ALA D . n 
D 1 168 ARG 168 169 169 ARG ARG D . n 
D 1 169 LEU 169 170 170 LEU LEU D . n 
D 1 170 LEU 170 171 171 LEU LEU D . n 
D 1 171 GLU 171 172 172 GLU GLU D . n 
D 1 172 ARG 172 173 173 ARG ARG D . n 
D 1 173 LEU 173 174 174 LEU LEU D . n 
D 1 174 PHE 174 175 175 PHE PHE D . n 
D 1 175 LYS 175 176 176 LYS LYS D . n 
D 1 176 GLN 176 177 177 GLN GLN D . n 
D 1 177 LEU 177 178 178 LEU LEU D . n 
D 1 178 HIS 178 179 179 HIS HIS D . n 
D 1 179 PRO 179 180 180 PRO PRO D . n 
D 1 180 GLN 180 181 181 GLN GLN D . n 
D 1 181 LEU 181 182 182 LEU LEU D . n 
D 1 182 LEU 182 183 183 LEU LEU D . n 
D 1 183 LEU 183 184 184 LEU LEU D . n 
D 1 184 PRO 184 185 185 PRO PRO D . n 
D 1 185 ASP 185 186 186 ASP ASP D . n 
D 1 186 ASP 186 187 187 ASP ASP D . n 
D 1 187 TYR 187 188 188 TYR TYR D . n 
D 1 188 LEU 188 189 189 LEU LEU D . n 
D 1 189 ASP 189 190 190 ASP ASP D . n 
D 1 190 CYS 190 191 191 CYS CYS D . n 
D 1 191 LEU 191 192 192 LEU LEU D . n 
D 1 192 GLY 192 193 193 GLY GLY D . n 
D 1 193 LYS 193 194 194 LYS LYS D . n 
D 1 194 GLN 194 195 195 GLN GLN D . n 
D 1 195 ALA 195 196 196 ALA ALA D . n 
D 1 196 GLU 196 197 197 GLU GLU D . n 
D 1 197 ALA 197 198 198 ALA ALA D . n 
D 1 198 LEU 198 199 199 LEU LEU D . n 
D 1 199 ARG 199 200 200 ARG ARG D . n 
D 1 200 PRO 200 201 201 PRO PRO D . n 
D 1 201 PHE 201 202 202 PHE PHE D . n 
D 1 202 GLY 202 203 203 GLY GLY D . n 
D 1 203 GLU 203 204 204 GLU GLU D . n 
D 1 204 ALA 204 205 205 ALA ALA D . n 
D 1 205 PRO 205 206 206 PRO PRO D . n 
D 1 206 ARG 206 207 207 ARG ARG D . n 
D 1 207 GLU 207 208 208 GLU GLU D . n 
D 1 208 LEU 208 209 209 LEU LEU D . n 
D 1 209 ARG 209 210 210 ARG ARG D . n 
D 1 210 LEU 210 211 211 LEU LEU D . n 
D 1 211 ARG 211 212 212 ARG ARG D . n 
D 1 212 ALA 212 213 213 ALA ALA D . n 
D 1 213 THR 213 214 214 THR THR D . n 
D 1 214 ARG 214 215 215 ARG ARG D . n 
D 1 215 ALA 215 216 216 ALA ALA D . n 
D 1 216 PHE 216 217 217 PHE PHE D . n 
D 1 217 VAL 217 218 218 VAL VAL D . n 
D 1 218 ALA 218 219 219 ALA ALA D . n 
D 1 219 ALA 219 220 220 ALA ALA D . n 
D 1 220 ARG 220 221 221 ARG ARG D . n 
D 1 221 SER 221 222 222 SER SER D . n 
D 1 222 PHE 222 223 223 PHE PHE D . n 
D 1 223 VAL 223 224 224 VAL VAL D . n 
D 1 224 GLN 224 225 225 GLN GLN D . n 
D 1 225 GLY 225 226 226 GLY GLY D . n 
D 1 226 LEU 226 227 227 LEU LEU D . n 
D 1 227 GLY 227 228 228 GLY GLY D . n 
D 1 228 VAL 228 229 229 VAL VAL D . n 
D 1 229 ALA 229 230 230 ALA ALA D . n 
D 1 230 SER 230 231 231 SER SER D . n 
D 1 231 ASP 231 232 232 ASP ASP D . n 
D 1 232 VAL 232 233 233 VAL VAL D . n 
D 1 233 VAL 233 234 234 VAL VAL D . n 
D 1 234 ARG 234 235 235 ARG ARG D . n 
D 1 235 LYS 235 236 236 LYS LYS D . n 
D 1 236 VAL 236 237 237 VAL VAL D . n 
D 1 237 ALA 237 238 238 ALA ALA D . n 
D 1 238 GLN 238 239 239 GLN GLN D . n 
D 1 239 VAL 239 240 240 VAL VAL D . n 
D 1 240 PRO 240 241 241 PRO PRO D . n 
D 1 241 LEU 241 242 242 LEU LEU D . n 
D 1 242 GLY 242 243 243 GLY GLY D . n 
D 1 243 PRO 243 244 244 PRO PRO D . n 
D 1 244 GLU 244 245 245 GLU GLU D . n 
D 1 245 CYS 245 246 246 CYS CYS D . n 
D 1 246 SER 246 247 247 SER SER D . n 
D 1 247 ARG 247 248 248 ARG ARG D . n 
D 1 248 ALA 248 249 249 ALA ALA D . n 
D 1 249 VAL 249 250 250 VAL VAL D . n 
D 1 250 MET 250 251 251 MET MET D . n 
D 1 251 LYS 251 252 252 LYS LYS D . n 
D 1 252 LEU 252 253 253 LEU LEU D . n 
D 1 253 VAL 253 254 254 VAL VAL D . n 
D 1 254 TYR 254 255 255 TYR TYR D . n 
D 1 255 CYS 255 256 256 CYS CYS D . n 
D 1 256 ALA 256 257 257 ALA ALA D . n 
D 1 257 HIS 257 258 258 HIS HIS D . n 
D 1 258 CYS 258 259 259 CYS CYS D . n 
D 1 259 LEU 259 260 260 LEU LEU D . n 
D 1 260 GLY 260 261 261 GLY GLY D . n 
D 1 261 VAL 261 262 262 VAL VAL D . n 
D 1 262 PRO 262 263 263 PRO PRO D . n 
D 1 263 GLY 263 264 264 GLY GLY D . n 
D 1 264 ALA 264 265 265 ALA ALA D . n 
D 1 265 ARG 265 266 266 ARG ARG D . n 
D 1 266 PRO 266 267 267 PRO PRO D . n 
D 1 267 CYS 267 268 268 CYS CYS D . n 
D 1 268 PRO 268 269 269 PRO PRO D . n 
D 1 269 ASP 269 270 270 ASP ASP D . n 
D 1 270 TYR 270 271 271 TYR TYR D . n 
D 1 271 CYS 271 272 272 CYS CYS D . n 
D 1 272 ARG 272 273 273 ARG ARG D . n 
D 1 273 ASN 273 274 274 ASN ASN D . n 
D 1 274 VAL 274 275 275 VAL VAL D . n 
D 1 275 LEU 275 276 276 LEU LEU D . n 
D 1 276 LYS 276 277 277 LYS LYS D . n 
D 1 277 GLY 277 278 278 GLY GLY D . n 
D 1 278 CYS 278 279 279 CYS CYS D . n 
D 1 279 LEU 279 280 280 LEU LEU D . n 
D 1 280 ALA 280 281 281 ALA ALA D . n 
D 1 281 ASN 281 282 282 ASN ASN D . n 
D 1 282 GLN 282 283 283 GLN GLN D . n 
D 1 283 ALA 283 284 284 ALA ALA D . n 
D 1 284 ASP 284 285 285 ASP ASP D . n 
D 1 285 LEU 285 286 286 LEU LEU D . n 
D 1 286 ASP 286 287 287 ASP ASP D . n 
D 1 287 ALA 287 288 288 ALA ALA D . n 
D 1 288 GLU 288 289 289 GLU GLU D . n 
D 1 289 TRP 289 290 290 TRP TRP D . n 
D 1 290 ARG 290 291 291 ARG ARG D . n 
D 1 291 ASN 291 292 292 ASN ASN D . n 
D 1 292 LEU 292 293 293 LEU LEU D . n 
D 1 293 LEU 293 294 294 LEU LEU D . n 
D 1 294 ASP 294 295 295 ASP ASP D . n 
D 1 295 SER 295 296 296 SER SER D . n 
D 1 296 MET 296 297 297 MET MET D . n 
D 1 297 VAL 297 298 298 VAL VAL D . n 
D 1 298 LEU 298 299 299 LEU LEU D . n 
D 1 299 ILE 299 300 300 ILE ILE D . n 
D 1 300 THR 300 301 301 THR THR D . n 
D 1 301 ASP 301 302 302 ASP ASP D . n 
D 1 302 LYS 302 303 303 LYS LYS D . n 
D 1 303 PHE 303 304 304 PHE PHE D . n 
D 1 304 TRP 304 305 305 TRP TRP D . n 
D 1 305 GLY 305 306 306 GLY GLY D . n 
D 1 306 THR 306 307 307 THR THR D . n 
D 1 307 SER 307 308 308 SER SER D . n 
D 1 308 GLY 308 309 309 GLY GLY D . n 
D 1 309 VAL 309 310 310 VAL VAL D . n 
D 1 310 GLU 310 311 311 GLU GLU D . n 
D 1 311 SER 311 312 312 SER SER D . n 
D 1 312 VAL 312 313 313 VAL VAL D . n 
D 1 313 ILE 313 314 314 ILE ILE D . n 
D 1 314 GLY 314 315 315 GLY GLY D . n 
D 1 315 SER 315 316 316 SER SER D . n 
D 1 316 VAL 316 317 317 VAL VAL D . n 
D 1 317 HIS 317 318 318 HIS HIS D . n 
D 1 318 THR 318 319 319 THR THR D . n 
D 1 319 TRP 319 320 320 TRP TRP D . n 
D 1 320 LEU 320 321 321 LEU LEU D . n 
D 1 321 ALA 321 322 322 ALA ALA D . n 
D 1 322 GLU 322 323 323 GLU GLU D . n 
D 1 323 ALA 323 324 324 ALA ALA D . n 
D 1 324 ILE 324 325 325 ILE ILE D . n 
D 1 325 ASN 325 326 326 ASN ASN D . n 
D 1 326 ALA 326 327 327 ALA ALA D . n 
D 1 327 LEU 327 328 328 LEU LEU D . n 
D 1 328 GLN 328 329 329 GLN GLN D . n 
D 1 329 ASP 329 330 330 ASP ASP D . n 
D 1 330 ASN 330 331 331 ASN ASN D . n 
D 1 331 ARG 331 332 332 ARG ARG D . n 
D 1 332 ASP 332 333 333 ASP ASP D . n 
D 1 333 THR 333 334 334 THR THR D . n 
D 1 334 LEU 334 335 335 LEU LEU D . n 
D 1 335 THR 335 336 336 THR THR D . n 
D 1 336 ALA 336 337 337 ALA ALA D . n 
D 1 337 LYS 337 338 338 LYS LYS D . n 
D 1 338 VAL 338 339 339 VAL VAL D . n 
D 1 339 ILE 339 340 340 ILE ILE D . n 
D 1 340 GLN 340 341 341 GLN GLN D . n 
D 1 341 GLY 341 342 342 GLY GLY D . n 
D 1 342 CYS 342 343 343 CYS CYS D . n 
D 1 343 GLY 343 344 344 GLY GLY D . n 
D 1 344 ASN 344 345 345 ASN ASN D . n 
D 1 345 PRO 345 346 346 PRO PRO D . n 
D 1 346 LYS 346 347 347 LYS LYS D . n 
D 1 347 VAL 347 348 348 VAL VAL D . n 
D 1 348 ASN 348 349 349 ASN ASN D . n 
D 1 349 PRO 349 350 ?   ?   ?   D . n 
D 1 350 GLN 350 351 ?   ?   ?   D . n 
D 1 351 GLY 351 352 ?   ?   ?   D . n 
D 1 352 PRO 352 353 ?   ?   ?   D . n 
D 1 353 GLY 353 354 ?   ?   ?   D . n 
D 1 354 PRO 354 355 ?   ?   ?   D . n 
D 1 355 GLU 355 356 ?   ?   ?   D . n 
D 1 356 GLU 356 357 ?   ?   ?   D . n 
D 1 357 LYS 357 358 ?   ?   ?   D . n 
D 1 358 ARG 358 359 ?   ?   ?   D . n 
D 1 359 ARG 359 360 ?   ?   ?   D . n 
D 1 360 ARG 360 361 361 ARG ARG D . n 
D 1 361 GLY 361 362 362 GLY GLY D . n 
D 1 362 LYS 362 363 363 LYS LYS D . n 
D 1 363 LEU 363 364 364 LEU LEU D . n 
D 1 364 ALA 364 365 365 ALA ALA D . n 
D 1 365 PRO 365 366 366 PRO PRO D . n 
D 1 366 ARG 366 367 367 ARG ARG D . n 
D 1 367 GLU 367 368 368 GLU GLU D . n 
D 1 368 ARG 368 369 369 ARG ARG D . n 
D 1 369 PRO 369 370 370 PRO PRO D . n 
D 1 370 PRO 370 371 371 PRO PRO D . n 
D 1 371 SER 371 372 372 SER SER D . n 
D 1 372 GLY 372 373 373 GLY GLY D . n 
D 1 373 THR 373 374 374 THR THR D . n 
D 1 374 LEU 374 375 375 LEU LEU D . n 
D 1 375 GLU 375 376 376 GLU GLU D . n 
D 1 376 LYS 376 377 377 LYS LYS D . n 
D 1 377 LEU 377 378 378 LEU LEU D . n 
D 1 378 VAL 378 379 379 VAL VAL D . n 
D 1 379 SER 379 380 380 SER SER D . n 
D 1 380 GLU 380 381 381 GLU GLU D . n 
D 1 381 ALA 381 382 382 ALA ALA D . n 
D 1 382 LYS 382 383 383 LYS LYS D . n 
D 1 383 ALA 383 384 384 ALA ALA D . n 
D 1 384 GLN 384 385 385 GLN GLN D . n 
D 1 385 LEU 385 386 386 LEU LEU D . n 
D 1 386 ARG 386 387 387 ARG ARG D . n 
D 1 387 ASP 387 388 388 ASP ASP D . n 
D 1 388 VAL 388 389 389 VAL VAL D . n 
D 1 389 GLN 389 390 390 GLN GLN D . n 
D 1 390 ASP 390 391 391 ASP ASP D . n 
D 1 391 PHE 391 392 392 PHE PHE D . n 
D 1 392 TRP 392 393 393 TRP TRP D . n 
D 1 393 ILE 393 394 394 ILE ILE D . n 
D 1 394 SER 394 395 395 SER SER D . n 
D 1 395 LEU 395 396 396 LEU LEU D . n 
D 1 396 PRO 396 397 397 PRO PRO D . n 
D 1 397 GLY 397 398 398 GLY GLY D . n 
D 1 398 THR 398 399 399 THR THR D . n 
D 1 399 LEU 399 400 400 LEU LEU D . n 
D 1 400 CYS 400 401 401 CYS CYS D . n 
D 1 401 SER 401 402 402 SER SER D . n 
D 1 402 GLU 402 403 403 GLU GLU D . n 
D 1 403 LYS 403 404 404 LYS LYS D . n 
D 1 404 MET 404 405 405 MET MET D . n 
D 1 405 ALA 405 406 406 ALA ALA D . n 
D 1 406 LEU 406 407 ?   ?   ?   D . n 
D 1 407 SER 407 408 ?   ?   ?   D . n 
D 1 408 THR 408 409 ?   ?   ?   D . n 
D 1 409 ALA 409 410 ?   ?   ?   D . n 
D 1 410 SER 410 411 ?   ?   ?   D . n 
D 1 411 ASP 411 412 ?   ?   ?   D . n 
D 1 412 ASP 412 413 413 ASP ASP D . n 
D 1 413 ARG 413 414 414 ARG ARG D . n 
D 1 414 CYS 414 415 415 CYS CYS D . n 
D 1 415 TRP 415 416 416 TRP TRP D . n 
D 1 416 ASN 416 417 417 ASN ASN D . n 
D 1 417 GLY 417 418 418 GLY GLY D . n 
D 1 418 MET 418 419 419 MET MET D . n 
D 1 419 ALA 419 420 420 ALA ALA D . n 
D 1 420 ARG 420 421 421 ARG ARG D . n 
D 1 421 GLY 421 422 422 GLY GLY D . n 
D 1 422 ARG 422 423 423 ARG ARG D . n 
D 1 423 TYR 423 424 424 TYR TYR D . n 
D 1 424 LEU 424 425 425 LEU LEU D . n 
D 1 425 PRO 425 426 426 PRO PRO D . n 
D 1 426 GLU 426 427 427 GLU GLU D . n 
D 1 427 VAL 427 428 428 VAL VAL D . n 
D 1 428 MET 428 429 429 MET MET D . n 
D 1 429 GLY 429 430 430 GLY GLY D . n 
D 1 430 ASP 430 431 431 ASP ASP D . n 
D 1 431 GLY 431 432 432 GLY GLY D . n 
D 1 432 LEU 432 433 433 LEU LEU D . n 
D 1 433 ALA 433 434 434 ALA ALA D . n 
D 1 434 ASN 434 435 435 ASN ASN D . n 
D 1 435 GLN 435 436 436 GLN GLN D . n 
D 1 436 ILE 436 437 437 ILE ILE D . n 
D 1 437 ASN 437 438 438 ASN ASN D . n 
D 1 438 ASN 438 439 439 ASN ASN D . n 
D 1 439 PRO 439 440 440 PRO PRO D . n 
D 1 440 GLU 440 441 441 GLU GLU D . n 
D 1 441 VAL 441 442 442 VAL VAL D . n 
D 1 442 GLU 442 443 443 GLU GLU D . n 
D 1 443 VAL 443 444 444 VAL VAL D . n 
D 1 444 ASP 444 445 445 ASP ASP D . n 
D 1 445 ILE 445 446 446 ILE ILE D . n 
D 1 446 THR 446 447 447 THR THR D . n 
D 1 447 LYS 447 448 448 LYS LYS D . n 
D 1 448 PRO 448 449 449 PRO PRO D . n 
D 1 449 ASP 449 450 450 ASP ASP D . n 
D 1 450 MET 450 451 451 MET MET D . n 
D 1 451 THR 451 452 452 THR THR D . n 
D 1 452 ILE 452 453 453 ILE ILE D . n 
D 1 453 ARG 453 454 454 ARG ARG D . n 
D 1 454 GLN 454 455 455 GLN GLN D . n 
D 1 455 GLN 455 456 456 GLN GLN D . n 
D 1 456 ILE 456 457 457 ILE ILE D . n 
D 1 457 MET 457 458 458 MET MET D . n 
D 1 458 GLN 458 459 459 GLN GLN D . n 
D 1 459 LEU 459 460 460 LEU LEU D . n 
D 1 460 LYS 460 461 461 LYS LYS D . n 
D 1 461 ILE 461 462 462 ILE ILE D . n 
D 1 462 MET 462 463 463 MET MET D . n 
D 1 463 THR 463 464 464 THR THR D . n 
D 1 464 ASN 464 465 465 ASN ASN D . n 
D 1 465 ARG 465 466 466 ARG ARG D . n 
D 1 466 LEU 466 467 467 LEU LEU D . n 
D 1 467 ARG 467 468 468 ARG ARG D . n 
D 1 468 SER 468 469 469 SER SER D . n 
D 1 469 ALA 469 470 470 ALA ALA D . n 
D 1 470 TYR 470 471 471 TYR TYR D . n 
D 1 471 ASN 471 472 472 ASN ASN D . n 
D 1 472 GLY 472 473 473 GLY GLY D . n 
D 1 473 ASN 473 474 474 ASN ASN D . n 
D 1 474 ASP 474 475 ?   ?   ?   D . n 
D 1 475 VAL 475 476 ?   ?   ?   D . n 
D 1 476 ASP 476 477 ?   ?   ?   D . n 
D 1 477 PHE 477 478 ?   ?   ?   D . n 
D 1 478 GLN 478 479 ?   ?   ?   D . n 
D 1 479 ASP 479 480 ?   ?   ?   D . n 
D 1 480 ALA 480 481 ?   ?   ?   D . n 
D 1 481 SER 481 482 ?   ?   ?   D . n 
D 1 482 ASP 482 483 ?   ?   ?   D . n 
D 1 483 ASP 483 484 ?   ?   ?   D . n 
D 1 484 GLY 484 485 ?   ?   ?   D . n 
D 1 485 ALA 485 486 ?   ?   ?   D . n 
D 1 486 GLY 486 487 ?   ?   ?   D . n 
D 1 487 ALA 487 488 ?   ?   ?   D . n 
D 1 488 GLY 488 489 ?   ?   ?   D . n 
D 1 489 ALA 489 490 ?   ?   ?   D . n 
D 1 490 GLY 490 491 ?   ?   ?   D . n 
D 1 491 ASP 491 492 ?   ?   ?   D . n 
D 1 492 GLY 492 493 ?   ?   ?   D . n 
D 1 493 CYS 493 494 ?   ?   ?   D . n 
D 1 494 LEU 494 495 ?   ?   ?   D . n 
D 1 495 ASP 495 496 ?   ?   ?   D . n 
D 1 496 ASP 496 497 ?   ?   ?   D . n 
D 1 497 LEU 497 498 ?   ?   ?   D . n 
D 1 498 CYS 498 499 ?   ?   ?   D . n 
D 1 499 SER 499 500 ?   ?   ?   D . n 
D 1 500 ARG 500 501 ?   ?   ?   D . n 
D 1 501 LYS 501 502 ?   ?   ?   D . n 
D 1 502 VAL 502 503 ?   ?   ?   D . n 
D 1 503 SER 503 504 ?   ?   ?   D . n 
D 1 504 ARG 504 505 ?   ?   ?   D . n 
D 1 505 LYS 505 506 ?   ?   ?   D . n 
D 1 506 SER 506 507 ?   ?   ?   D . n 
D 1 507 SER 507 508 ?   ?   ?   D . n 
D 1 508 SER 508 509 ?   ?   ?   D . n 
D 1 509 SER 509 510 ?   ?   ?   D . n 
D 1 510 ARG 510 511 ?   ?   ?   D . n 
D 1 511 THR 511 512 ?   ?   ?   D . n 
D 1 512 PRO 512 513 ?   ?   ?   D . n 
D 1 513 LEU 513 514 ?   ?   ?   D . n 
D 1 514 THR 514 515 ?   ?   ?   D . n 
D 1 515 HIS 515 516 ?   ?   ?   D . n 
D 1 516 ALA 516 517 ?   ?   ?   D . n 
D 1 517 LEU 517 518 ?   ?   ?   D . n 
D 1 518 PRO 518 519 ?   ?   ?   D . n 
D 1 519 GLY 519 520 ?   ?   ?   D . n 
D 1 520 LEU 520 521 ?   ?   ?   D . n 
D 1 521 SER 521 522 ?   ?   ?   D . n 
D 1 522 GLU 522 523 ?   ?   ?   D . n 
D 1 523 GLN 523 524 ?   ?   ?   D . n 
D 1 524 GLU 524 525 ?   ?   ?   D . n 
D 1 525 GLY 525 526 ?   ?   ?   D . n 
D 1 526 GLN 526 527 ?   ?   ?   D . 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 
E 2 NAG 1   601 501 NAG NAG A . 
F 3 CA  1   602 503 CA  CA  A . 
G 3 CA  1   603 3   CA  CA  A . 
H 2 NAG 1   601 501 NAG NAG B . 
I 3 CA  1   602 502 CA  CA  B . 
J 3 CA  1   603 503 CA  CA  B . 
K 2 NAG 1   601 501 NAG NAG C . 
L 3 CA  1   602 502 CA  CA  C . 
M 3 CA  1   603 503 CA  CA  C . 
N 3 CA  1   604 504 CA  CA  C . 
O 2 NAG 1   601 501 NAG NAG D . 
P 3 CA  1   602 502 CA  CA  D . 
Q 3 CA  1   603 503 CA  CA  D . 
R 4 HOH 1   701 283 HOH HOH A . 
R 4 HOH 2   702 89  HOH HOH A . 
R 4 HOH 3   703 164 HOH HOH A . 
R 4 HOH 4   704 186 HOH HOH A . 
R 4 HOH 5   705 191 HOH HOH A . 
R 4 HOH 6   706 249 HOH HOH A . 
R 4 HOH 7   707 272 HOH HOH A . 
R 4 HOH 8   708 114 HOH HOH A . 
R 4 HOH 9   709 38  HOH HOH A . 
R 4 HOH 10  710 224 HOH HOH A . 
R 4 HOH 11  711 61  HOH HOH A . 
R 4 HOH 12  712 260 HOH HOH A . 
R 4 HOH 13  713 203 HOH HOH A . 
R 4 HOH 14  714 63  HOH HOH A . 
R 4 HOH 15  715 105 HOH HOH A . 
R 4 HOH 16  716 107 HOH HOH A . 
R 4 HOH 17  717 138 HOH HOH A . 
R 4 HOH 18  718 154 HOH HOH A . 
R 4 HOH 19  719 9   HOH HOH A . 
R 4 HOH 20  720 225 HOH HOH A . 
R 4 HOH 21  721 15  HOH HOH A . 
R 4 HOH 22  722 120 HOH HOH A . 
R 4 HOH 23  723 25  HOH HOH A . 
R 4 HOH 24  724 160 HOH HOH A . 
R 4 HOH 25  725 232 HOH HOH A . 
R 4 HOH 26  726 16  HOH HOH A . 
R 4 HOH 27  727 202 HOH HOH A . 
R 4 HOH 28  728 250 HOH HOH A . 
R 4 HOH 29  729 18  HOH HOH A . 
R 4 HOH 30  730 5   HOH HOH A . 
R 4 HOH 31  731 284 HOH HOH A . 
R 4 HOH 32  732 177 HOH HOH A . 
R 4 HOH 33  733 7   HOH HOH A . 
R 4 HOH 34  734 28  HOH HOH A . 
R 4 HOH 35  735 1   HOH HOH A . 
R 4 HOH 36  736 237 HOH HOH A . 
R 4 HOH 37  737 124 HOH HOH A . 
R 4 HOH 38  738 24  HOH HOH A . 
R 4 HOH 39  739 162 HOH HOH A . 
R 4 HOH 40  740 8   HOH HOH A . 
R 4 HOH 41  741 267 HOH HOH A . 
R 4 HOH 42  742 148 HOH HOH A . 
R 4 HOH 43  743 72  HOH HOH A . 
R 4 HOH 44  744 205 HOH HOH A . 
R 4 HOH 45  745 101 HOH HOH A . 
R 4 HOH 46  746 65  HOH HOH A . 
R 4 HOH 47  747 220 HOH HOH A . 
R 4 HOH 48  748 170 HOH HOH A . 
R 4 HOH 49  749 12  HOH HOH A . 
R 4 HOH 50  750 121 HOH HOH A . 
R 4 HOH 51  751 178 HOH HOH A . 
R 4 HOH 52  752 223 HOH HOH A . 
R 4 HOH 53  753 30  HOH HOH A . 
R 4 HOH 54  754 231 HOH HOH A . 
R 4 HOH 55  755 87  HOH HOH A . 
R 4 HOH 56  756 27  HOH HOH A . 
R 4 HOH 57  757 45  HOH HOH A . 
R 4 HOH 58  758 125 HOH HOH A . 
R 4 HOH 59  759 163 HOH HOH A . 
R 4 HOH 60  760 53  HOH HOH A . 
R 4 HOH 61  761 149 HOH HOH A . 
R 4 HOH 62  762 206 HOH HOH A . 
R 4 HOH 63  763 188 HOH HOH A . 
R 4 HOH 64  764 56  HOH HOH A . 
R 4 HOH 65  765 116 HOH HOH A . 
R 4 HOH 66  766 240 HOH HOH A . 
R 4 HOH 67  767 198 HOH HOH A . 
R 4 HOH 68  768 273 HOH HOH A . 
R 4 HOH 69  769 229 HOH HOH A . 
R 4 HOH 70  770 155 HOH HOH A . 
R 4 HOH 71  771 13  HOH HOH A . 
R 4 HOH 72  772 253 HOH HOH A . 
R 4 HOH 73  773 161 HOH HOH A . 
R 4 HOH 74  774 215 HOH HOH A . 
R 4 HOH 75  775 200 HOH HOH A . 
R 4 HOH 76  776 212 HOH HOH A . 
R 4 HOH 77  777 180 HOH HOH A . 
R 4 HOH 78  778 92  HOH HOH A . 
R 4 HOH 79  779 187 HOH HOH A . 
R 4 HOH 80  780 193 HOH HOH A . 
R 4 HOH 81  781 14  HOH HOH A . 
R 4 HOH 82  782 144 HOH HOH A . 
R 4 HOH 83  783 126 HOH HOH A . 
R 4 HOH 84  784 133 HOH HOH A . 
R 4 HOH 85  785 132 HOH HOH A . 
R 4 HOH 86  786 185 HOH HOH A . 
R 4 HOH 87  787 268 HOH HOH A . 
R 4 HOH 88  788 93  HOH HOH A . 
R 4 HOH 89  789 97  HOH HOH A . 
R 4 HOH 90  790 145 HOH HOH A . 
R 4 HOH 91  791 139 HOH HOH A . 
R 4 HOH 92  792 199 HOH HOH A . 
R 4 HOH 93  793 86  HOH HOH A . 
R 4 HOH 94  794 274 HOH HOH A . 
R 4 HOH 95  795 96  HOH HOH A . 
R 4 HOH 96  796 84  HOH HOH A . 
R 4 HOH 97  797 243 HOH HOH A . 
R 4 HOH 98  798 282 HOH HOH A . 
R 4 HOH 99  799 245 HOH HOH A . 
R 4 HOH 100 800 147 HOH HOH A . 
R 4 HOH 101 801 176 HOH HOH A . 
R 4 HOH 102 802 241 HOH HOH A . 
S 4 HOH 1   701 252 HOH HOH B . 
S 4 HOH 2   702 78  HOH HOH B . 
S 4 HOH 3   703 36  HOH HOH B . 
S 4 HOH 4   704 171 HOH HOH B . 
S 4 HOH 5   705 239 HOH HOH B . 
S 4 HOH 6   706 235 HOH HOH B . 
S 4 HOH 7   707 85  HOH HOH B . 
S 4 HOH 8   708 244 HOH HOH B . 
S 4 HOH 9   709 42  HOH HOH B . 
S 4 HOH 10  710 209 HOH HOH B . 
S 4 HOH 11  711 152 HOH HOH B . 
S 4 HOH 12  712 278 HOH HOH B . 
S 4 HOH 13  713 266 HOH HOH B . 
S 4 HOH 14  714 183 HOH HOH B . 
S 4 HOH 15  715 271 HOH HOH B . 
S 4 HOH 16  716 6   HOH HOH B . 
S 4 HOH 17  717 40  HOH HOH B . 
S 4 HOH 18  718 3   HOH HOH B . 
S 4 HOH 19  719 201 HOH HOH B . 
S 4 HOH 20  720 118 HOH HOH B . 
S 4 HOH 21  721 17  HOH HOH B . 
S 4 HOH 22  722 234 HOH HOH B . 
S 4 HOH 23  723 151 HOH HOH B . 
S 4 HOH 24  724 207 HOH HOH B . 
S 4 HOH 25  725 179 HOH HOH B . 
S 4 HOH 26  726 20  HOH HOH B . 
S 4 HOH 27  727 70  HOH HOH B . 
S 4 HOH 28  728 270 HOH HOH B . 
S 4 HOH 29  729 29  HOH HOH B . 
S 4 HOH 30  730 64  HOH HOH B . 
S 4 HOH 31  731 44  HOH HOH B . 
S 4 HOH 32  732 4   HOH HOH B . 
S 4 HOH 33  733 255 HOH HOH B . 
S 4 HOH 34  734 43  HOH HOH B . 
S 4 HOH 35  735 74  HOH HOH B . 
S 4 HOH 36  736 216 HOH HOH B . 
S 4 HOH 37  737 159 HOH HOH B . 
S 4 HOH 38  738 117 HOH HOH B . 
S 4 HOH 39  739 77  HOH HOH B . 
S 4 HOH 40  740 174 HOH HOH B . 
S 4 HOH 41  741 242 HOH HOH B . 
S 4 HOH 42  742 172 HOH HOH B . 
S 4 HOH 43  743 88  HOH HOH B . 
S 4 HOH 44  744 10  HOH HOH B . 
S 4 HOH 45  745 233 HOH HOH B . 
S 4 HOH 46  746 150 HOH HOH B . 
S 4 HOH 47  747 130 HOH HOH B . 
S 4 HOH 48  748 127 HOH HOH B . 
S 4 HOH 49  749 143 HOH HOH B . 
S 4 HOH 50  750 31  HOH HOH B . 
S 4 HOH 51  751 51  HOH HOH B . 
S 4 HOH 52  752 11  HOH HOH B . 
S 4 HOH 53  753 221 HOH HOH B . 
S 4 HOH 54  754 213 HOH HOH B . 
S 4 HOH 55  755 69  HOH HOH B . 
S 4 HOH 56  756 236 HOH HOH B . 
S 4 HOH 57  757 113 HOH HOH B . 
S 4 HOH 58  758 115 HOH HOH B . 
S 4 HOH 59  759 48  HOH HOH B . 
S 4 HOH 60  760 265 HOH HOH B . 
S 4 HOH 61  761 214 HOH HOH B . 
S 4 HOH 62  762 19  HOH HOH B . 
S 4 HOH 63  763 227 HOH HOH B . 
S 4 HOH 64  764 112 HOH HOH B . 
S 4 HOH 65  765 111 HOH HOH B . 
S 4 HOH 66  766 81  HOH HOH B . 
S 4 HOH 67  767 37  HOH HOH B . 
S 4 HOH 68  768 219 HOH HOH B . 
S 4 HOH 69  769 254 HOH HOH B . 
S 4 HOH 70  770 194 HOH HOH B . 
S 4 HOH 71  771 60  HOH HOH B . 
S 4 HOH 72  772 226 HOH HOH B . 
S 4 HOH 73  773 246 HOH HOH B . 
S 4 HOH 74  774 46  HOH HOH B . 
S 4 HOH 75  775 83  HOH HOH B . 
S 4 HOH 76  776 58  HOH HOH B . 
S 4 HOH 77  777 110 HOH HOH B . 
S 4 HOH 78  778 182 HOH HOH B . 
S 4 HOH 79  779 109 HOH HOH B . 
S 4 HOH 80  780 108 HOH HOH B . 
S 4 HOH 81  781 261 HOH HOH B . 
S 4 HOH 82  782 175 HOH HOH B . 
S 4 HOH 83  783 98  HOH HOH B . 
S 4 HOH 84  784 71  HOH HOH B . 
S 4 HOH 85  785 67  HOH HOH B . 
S 4 HOH 86  786 128 HOH HOH B . 
T 4 HOH 1   701 184 HOH HOH C . 
T 4 HOH 2   702 181 HOH HOH C . 
T 4 HOH 3   703 23  HOH HOH C . 
T 4 HOH 4   704 217 HOH HOH C . 
T 4 HOH 5   705 157 HOH HOH C . 
T 4 HOH 6   706 256 HOH HOH C . 
T 4 HOH 7   707 156 HOH HOH C . 
T 4 HOH 8   708 75  HOH HOH C . 
T 4 HOH 9   709 204 HOH HOH C . 
T 4 HOH 10  710 137 HOH HOH C . 
T 4 HOH 11  711 140 HOH HOH C . 
T 4 HOH 12  712 35  HOH HOH C . 
T 4 HOH 13  713 258 HOH HOH C . 
T 4 HOH 14  714 106 HOH HOH C . 
T 4 HOH 15  715 230 HOH HOH C . 
T 4 HOH 16  716 90  HOH HOH C . 
T 4 HOH 17  717 280 HOH HOH C . 
T 4 HOH 18  718 94  HOH HOH C . 
T 4 HOH 19  719 210 HOH HOH C . 
T 4 HOH 20  720 57  HOH HOH C . 
T 4 HOH 21  721 247 HOH HOH C . 
T 4 HOH 22  722 2   HOH HOH C . 
T 4 HOH 23  723 262 HOH HOH C . 
T 4 HOH 24  724 276 HOH HOH C . 
T 4 HOH 25  725 146 HOH HOH C . 
T 4 HOH 26  726 73  HOH HOH C . 
T 4 HOH 27  727 59  HOH HOH C . 
T 4 HOH 28  728 33  HOH HOH C . 
T 4 HOH 29  729 136 HOH HOH C . 
T 4 HOH 30  730 39  HOH HOH C . 
T 4 HOH 31  731 26  HOH HOH C . 
T 4 HOH 32  732 264 HOH HOH C . 
T 4 HOH 33  733 21  HOH HOH C . 
T 4 HOH 34  734 228 HOH HOH C . 
T 4 HOH 35  735 79  HOH HOH C . 
T 4 HOH 36  736 66  HOH HOH C . 
T 4 HOH 37  737 189 HOH HOH C . 
T 4 HOH 38  738 192 HOH HOH C . 
T 4 HOH 39  739 34  HOH HOH C . 
T 4 HOH 40  740 131 HOH HOH C . 
T 4 HOH 41  741 269 HOH HOH C . 
T 4 HOH 42  742 251 HOH HOH C . 
T 4 HOH 43  743 82  HOH HOH C . 
T 4 HOH 44  744 119 HOH HOH C . 
T 4 HOH 45  745 91  HOH HOH C . 
T 4 HOH 46  746 259 HOH HOH C . 
T 4 HOH 47  747 102 HOH HOH C . 
T 4 HOH 48  748 76  HOH HOH C . 
T 4 HOH 49  749 238 HOH HOH C . 
T 4 HOH 50  750 103 HOH HOH C . 
T 4 HOH 51  751 95  HOH HOH C . 
T 4 HOH 52  752 218 HOH HOH C . 
T 4 HOH 53  753 257 HOH HOH C . 
U 4 HOH 1   701 168 HOH HOH D . 
U 4 HOH 2   702 122 HOH HOH D . 
U 4 HOH 3   703 190 HOH HOH D . 
U 4 HOH 4   704 275 HOH HOH D . 
U 4 HOH 5   705 208 HOH HOH D . 
U 4 HOH 6   706 279 HOH HOH D . 
U 4 HOH 7   707 32  HOH HOH D . 
U 4 HOH 8   708 47  HOH HOH D . 
U 4 HOH 9   709 281 HOH HOH D . 
U 4 HOH 10  710 222 HOH HOH D . 
U 4 HOH 11  711 99  HOH HOH D . 
U 4 HOH 12  712 169 HOH HOH D . 
U 4 HOH 13  713 50  HOH HOH D . 
U 4 HOH 14  714 22  HOH HOH D . 
U 4 HOH 15  715 195 HOH HOH D . 
U 4 HOH 16  716 211 HOH HOH D . 
U 4 HOH 17  717 141 HOH HOH D . 
U 4 HOH 18  718 62  HOH HOH D . 
U 4 HOH 19  719 129 HOH HOH D . 
U 4 HOH 20  720 123 HOH HOH D . 
U 4 HOH 21  721 263 HOH HOH D . 
U 4 HOH 22  722 277 HOH HOH D . 
U 4 HOH 23  723 165 HOH HOH D . 
U 4 HOH 24  724 100 HOH HOH D . 
U 4 HOH 25  725 196 HOH HOH D . 
U 4 HOH 26  726 104 HOH HOH D . 
U 4 HOH 27  727 52  HOH HOH D . 
U 4 HOH 28  728 55  HOH HOH D . 
U 4 HOH 29  729 54  HOH HOH D . 
U 4 HOH 30  730 41  HOH HOH D . 
U 4 HOH 31  731 134 HOH HOH D . 
U 4 HOH 32  732 80  HOH HOH D . 
U 4 HOH 33  733 158 HOH HOH D . 
U 4 HOH 34  734 142 HOH HOH D . 
U 4 HOH 35  735 49  HOH HOH D . 
U 4 HOH 36  736 68  HOH HOH D . 
U 4 HOH 37  737 197 HOH HOH D . 
U 4 HOH 38  738 167 HOH HOH D . 
U 4 HOH 39  739 153 HOH HOH D . 
U 4 HOH 40  740 173 HOH HOH D . 
U 4 HOH 41  741 248 HOH HOH D . 
U 4 HOH 42  742 166 HOH HOH D . 
U 4 HOH 43  743 135 HOH HOH D . 
# 
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 
3 author_and_software_defined_assembly PISA monomeric 1 
4 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,E,F,G,R   
2 1 B,H,I,J,S   
3 1 C,K,L,M,N,T 
4 1 D,O,P,Q,U   
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASP 387 ? A ASP 388 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 OD1 ? A ASP 390 ? A ASP 391 ? 1_555 90.6  ? 
2  O   ? A ASP 387 ? A ASP 388 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 OD2 ? A ASP 390 ? A ASP 391 ? 1_555 126.1 ? 
3  OD1 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 OD2 ? A ASP 390 ? A ASP 391 ? 1_555 55.2  ? 
4  O   ? A ASP 387 ? A ASP 388 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 741 ? 1_555 71.2  ? 
5  OD1 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 741 ? 1_555 89.4  ? 
6  OD2 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 741 ? 1_555 68.7  ? 
7  O   ? A ASP 387 ? A ASP 388 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 787 ? 1_555 131.1 ? 
8  OD1 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 787 ? 1_555 86.7  ? 
9  OD2 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 787 ? 1_555 91.0  ? 
10 O   ? R HOH .   ? A HOH 741 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 787 ? 1_555 157.3 ? 
11 O   ? A ASP 387 ? A ASP 388 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 731 ? 1_555 81.9  ? 
12 OD1 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 731 ? 1_555 67.0  ? 
13 OD2 ? A ASP 390 ? A ASP 391 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 731 ? 1_555 112.8 ? 
14 O   ? R HOH .   ? A HOH 741 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 731 ? 1_555 144.1 ? 
15 O   ? R HOH .   ? A HOH 787 ? 1_555 CA ? F CA . ? A CA 602 ? 1_555 O   ? R HOH .   ? A HOH 731 ? 1_555 52.3  ? 
16 O   ? A ILE 436 ? A ILE 437 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 766 ? 1_555 91.3  ? 
17 O   ? A ILE 436 ? A ILE 437 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 770 ? 1_555 74.6  ? 
18 O   ? R HOH .   ? A HOH 766 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 770 ? 1_555 70.2  ? 
19 O   ? A ILE 436 ? A ILE 437 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 780 ? 1_555 79.3  ? 
20 O   ? R HOH .   ? A HOH 766 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 780 ? 1_555 123.0 ? 
21 O   ? R HOH .   ? A HOH 770 ? 1_555 CA ? G CA . ? A CA 603 ? 1_555 O   ? R HOH .   ? A HOH 780 ? 1_555 151.2 ? 
22 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 84.9  ? 
23 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 133.2 ? 
24 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 55.3  ? 
25 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 702 ? 1_555 70.5  ? 
26 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 702 ? 1_555 55.6  ? 
27 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 702 ? 1_555 99.8  ? 
28 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 731 ? 1_555 73.2  ? 
29 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 731 ? 1_555 129.1 ? 
30 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 731 ? 1_555 150.2 ? 
31 O   ? S HOH .   ? B HOH 702 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 731 ? 1_555 73.8  ? 
32 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 741 ? 1_555 71.9  ? 
33 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 741 ? 1_555 79.0  ? 
34 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 741 ? 1_555 76.6  ? 
35 O   ? S HOH .   ? B HOH 702 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 741 ? 1_555 122.2 ? 
36 O   ? S HOH .   ? B HOH 731 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 741 ? 1_555 131.9 ? 
37 O   ? B ASP 387 ? B ASP 388 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 121.7 ? 
38 OD1 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 96.6  ? 
39 OD2 ? B ASP 390 ? B ASP 391 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 89.6  ? 
40 O   ? S HOH .   ? B HOH 702 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 63.6  ? 
41 O   ? S HOH .   ? B HOH 731 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 61.2  ? 
42 O   ? S HOH .   ? B HOH 741 ? 1_555 CA ? J CA . ? B CA 603 ? 1_555 O   ? S HOH .   ? B HOH 776 ? 1_555 165.6 ? 
43 O   ? B ILE 436 ? B ILE 437 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 OE1 ? B GLU 442 ? B GLU 443 ? 1_555 148.6 ? 
44 O   ? B ILE 436 ? B ILE 437 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 OE2 ? B GLU 442 ? B GLU 443 ? 1_555 142.4 ? 
45 OE1 ? B GLU 442 ? B GLU 443 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 OE2 ? B GLU 442 ? B GLU 443 ? 1_555 55.3  ? 
46 O   ? B ILE 436 ? B ILE 437 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 707 ? 1_555 59.6  ? 
47 OE1 ? B GLU 442 ? B GLU 443 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 707 ? 1_555 138.4 ? 
48 OE2 ? B GLU 442 ? B GLU 443 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 707 ? 1_555 129.1 ? 
49 O   ? B ILE 436 ? B ILE 437 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 716 ? 1_555 67.3  ? 
50 OE1 ? B GLU 442 ? B GLU 443 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 716 ? 1_555 96.9  ? 
51 OE2 ? B GLU 442 ? B GLU 443 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 716 ? 1_555 84.8  ? 
52 O   ? S HOH .   ? B HOH 707 ? 1_555 CA ? I CA . ? B CA 602 ? 1_555 O   ? S HOH .   ? B HOH 716 ? 1_555 123.9 ? 
53 OD1 ? C ASP 47  ? C ASP 48  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE1 ? C GLU 71  ? C GLU 72  ? 1_555 92.9  ? 
54 OD1 ? C ASP 47  ? C ASP 48  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE2 ? C GLU 71  ? C GLU 72  ? 1_555 119.5 ? 
55 OE1 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE2 ? C GLU 71  ? C GLU 72  ? 1_555 55.3  ? 
56 OD1 ? C ASP 47  ? C ASP 48  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? T HOH .   ? C HOH 703 ? 1_555 58.9  ? 
57 OE1 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? T HOH .   ? C HOH 703 ? 1_555 148.1 ? 
58 OE2 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? T HOH .   ? C HOH 703 ? 1_555 149.5 ? 
59 OD1 ? C ASP 47  ? C ASP 48  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE1 ? A GLU 164 ? A GLU 165 ? 1_555 105.8 ? 
60 OE1 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE1 ? A GLU 164 ? A GLU 165 ? 1_555 105.9 ? 
61 OE2 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE1 ? A GLU 164 ? A GLU 165 ? 1_555 53.2  ? 
62 O   ? T HOH .   ? C HOH 703 ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 OE1 ? A GLU 164 ? A GLU 165 ? 1_555 96.7  ? 
63 OD1 ? C ASP 47  ? C ASP 48  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? R HOH .   ? A HOH 782 ? 2_646 138.8 ? 
64 OE1 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? R HOH .   ? A HOH 782 ? 2_646 124.1 ? 
65 OE2 ? C GLU 71  ? C GLU 72  ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? R HOH .   ? A HOH 782 ? 2_646 98.2  ? 
66 O   ? T HOH .   ? C HOH 703 ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? R HOH .   ? A HOH 782 ? 2_646 80.3  ? 
67 OE1 ? A GLU 164 ? A GLU 165 ? 1_555 CA ? L CA . ? C CA 602 ? 1_555 O   ? R HOH .   ? A HOH 782 ? 2_646 82.9  ? 
68 O   ? C ASP 387 ? C ASP 388 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 OD1 ? C ASP 390 ? C ASP 391 ? 1_555 87.3  ? 
69 O   ? C ASP 387 ? C ASP 388 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 OD2 ? C ASP 390 ? C ASP 391 ? 1_555 128.9 ? 
70 OD1 ? C ASP 390 ? C ASP 391 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 OD2 ? C ASP 390 ? C ASP 391 ? 1_555 55.2  ? 
71 O   ? C ASP 387 ? C ASP 388 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 O   ? T HOH .   ? C HOH 717 ? 1_555 74.5  ? 
72 OD1 ? C ASP 390 ? C ASP 391 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 O   ? T HOH .   ? C HOH 717 ? 1_555 82.5  ? 
73 OD2 ? C ASP 390 ? C ASP 391 ? 1_555 CA ? N CA . ? C CA 604 ? 1_555 O   ? T HOH .   ? C HOH 717 ? 1_555 67.8  ? 
74 O   ? C ILE 436 ? C ILE 437 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 OE2 ? C GLU 442 ? C GLU 443 ? 1_555 151.3 ? 
75 O   ? C ILE 436 ? C ILE 437 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 O   ? T HOH .   ? C HOH 720 ? 1_555 68.1  ? 
76 OE2 ? C GLU 442 ? C GLU 443 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 O   ? T HOH .   ? C HOH 720 ? 1_555 86.9  ? 
77 O   ? C ILE 436 ? C ILE 437 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 O   ? T HOH .   ? C HOH 724 ? 1_555 70.1  ? 
78 OE2 ? C GLU 442 ? C GLU 443 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 O   ? T HOH .   ? C HOH 724 ? 1_555 86.0  ? 
79 O   ? T HOH .   ? C HOH 720 ? 1_555 CA ? M CA . ? C CA 603 ? 1_555 O   ? T HOH .   ? C HOH 724 ? 1_555 61.6  ? 
80 O   ? D ASP 387 ? D ASP 388 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 OD1 ? D ASP 390 ? D ASP 391 ? 1_555 86.8  ? 
81 O   ? D ASP 387 ? D ASP 388 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 OD2 ? D ASP 390 ? D ASP 391 ? 1_555 124.3 ? 
82 OD1 ? D ASP 390 ? D ASP 391 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 OD2 ? D ASP 390 ? D ASP 391 ? 1_555 55.2  ? 
83 O   ? D ASP 387 ? D ASP 388 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 O   ? U HOH .   ? D HOH 738 ? 1_555 116.9 ? 
84 OD1 ? D ASP 390 ? D ASP 391 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 O   ? U HOH .   ? D HOH 738 ? 1_555 85.0  ? 
85 OD2 ? D ASP 390 ? D ASP 391 ? 1_555 CA ? Q CA . ? D CA 603 ? 1_555 O   ? U HOH .   ? D HOH 738 ? 1_555 100.2 ? 
86 O   ? D ILE 436 ? D ILE 437 ? 1_555 CA ? P CA . ? D CA 602 ? 1_555 OE1 ? D GLU 442 ? D GLU 443 ? 1_555 167.2 ? 
87 O   ? D ILE 436 ? D ILE 437 ? 1_555 CA ? P CA . ? D CA 602 ? 1_555 O   ? U HOH .   ? D HOH 712 ? 1_555 74.3  ? 
88 OE1 ? D GLU 442 ? D GLU 443 ? 1_555 CA ? P CA . ? D CA 602 ? 1_555 O   ? U HOH .   ? D HOH 712 ? 1_555 97.9  ? 
# 
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 2015-07-29 
2 'Structure model' 1 1 2015-08-05 
3 'Structure model' 1 2 2015-09-30 
4 'Structure model' 1 3 2018-01-17 
# 
_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' 'Database references' 
2 3 'Structure model' 'Database references' 
3 4 'Structure model' 'Data collection'     
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            diffrn_source 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_diffrn_source.pdbx_synchrotron_site' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 39.3753 18.4302 90.4874 0.1120 0.1713 0.6150 0.0330  0.0776 -0.0377 2.0945 1.3878 0.7175 1.1982  
0.4069  0.2602  0.1028 -0.1900 -0.1268 0.0482  -0.0707 0.0396  0.0916  -0.0515 -0.0515 
'X-RAY DIFFRACTION' 2 ? refined 27.2065 13.5114 61.0112 0.1635 0.1477 0.7730 0.0388  0.0737 0.0251  1.6448 1.6361 0.5567 -0.9256 
0.1829  -0.0462 0.1049 0.1084  -0.0128 -0.1537 -0.0833 -0.1398 0.0441  0.0038  0.0028  
'X-RAY DIFFRACTION' 3 ? refined 16.2101 5.8868  21.9903 0.3499 0.4601 0.6238 -0.0295 0.0574 0.0835  1.3633 1.7378 0.6372 1.0232  
-0.0378 -0.1354 0.0154 0.0409  0.0985  0.0084  0.0173  -0.0756 -0.0873 0.0822  -0.0640 
'X-RAY DIFFRACTION' 4 ? refined 4.1933  1.5994  -7.6191 0.3093 0.4592 0.6299 0.0307  0.0911 0.0937  1.5457 1.5443 0.6130 -1.2393 
0.4565  -0.4453 0.1359 0.1363  -0.1363 -0.1607 -0.0938 -0.1263 0.0717  0.0214  -0.0402 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'chain A' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'chain B' 
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'chain C' 
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'chain D' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.9_1692 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15     2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 731 ? ? O A HOH 787 ? ? 2.11 
2 1 OG B SER 118 ? ? O B HOH 701 ? ? 2.16 
3 1 O  A HOH 756 ? ? O A HOH 793 ? ? 2.17 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             THR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              336 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             THR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              336 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             THR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              336 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                127.49 
_pdbx_validate_rmsd_angle.angle_target_value         111.00 
_pdbx_validate_rmsd_angle.angle_deviation            16.49 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.70 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 61  ? ? -107.51 -65.21  
2  1 SER A 316 ? ? -140.47 26.50   
3  1 THR A 336 ? ? -28.50  -29.87  
4  1 ALA A 337 ? ? -21.06  102.57  
5  1 PRO B 185 ? ? -72.29  -169.32 
6  1 ALA B 198 ? ? 67.70   -4.43   
7  1 ARG B 200 ? ? 64.22   65.50   
8  1 PRO B 366 ? ? -66.42  -173.93 
9  1 LYS B 404 ? ? -117.28 -93.15  
10 1 MET B 419 ? ? -108.96 -63.99  
11 1 HIS C 158 ? ? -55.59  107.34  
12 1 LYS C 404 ? ? -118.01 -82.76  
13 1 ALA D 198 ? ? 70.73   -11.54  
14 1 SER D 316 ? ? -141.91 14.34   
15 1 LYS D 404 ? ? -116.22 -85.00  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    198 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    199 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.05 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 28  ? CG  ? A LYS 27  CG  
2   1 Y 1 A LYS 28  ? CD  ? A LYS 27  CD  
3   1 Y 1 A LYS 28  ? CE  ? A LYS 27  CE  
4   1 Y 1 A LYS 28  ? NZ  ? A LYS 27  NZ  
5   1 Y 1 A ARG 36  ? CG  ? A ARG 35  CG  
6   1 Y 1 A ARG 36  ? CD  ? A ARG 35  CD  
7   1 Y 1 A ARG 36  ? NE  ? A ARG 35  NE  
8   1 Y 1 A ARG 36  ? CZ  ? A ARG 35  CZ  
9   1 Y 1 A ARG 36  ? NH1 ? A ARG 35  NH1 
10  1 Y 1 A ARG 36  ? NH2 ? A ARG 35  NH2 
11  1 Y 1 A ARG 105 ? CG  ? A ARG 104 CG  
12  1 Y 1 A ARG 105 ? CD  ? A ARG 104 CD  
13  1 Y 1 A ARG 105 ? NE  ? A ARG 104 NE  
14  1 Y 1 A ARG 105 ? CZ  ? A ARG 104 CZ  
15  1 Y 1 A ARG 105 ? NH1 ? A ARG 104 NH1 
16  1 Y 1 A ARG 105 ? NH2 ? A ARG 104 NH2 
17  1 Y 1 A GLU 132 ? CG  ? A GLU 131 CG  
18  1 Y 1 A GLU 132 ? CD  ? A GLU 131 CD  
19  1 Y 1 A GLU 132 ? OE1 ? A GLU 131 OE1 
20  1 Y 1 A GLU 132 ? OE2 ? A GLU 131 OE2 
21  1 Y 1 A ASN 156 ? CG  ? A ASN 155 CG  
22  1 Y 1 A ASN 156 ? OD1 ? A ASN 155 OD1 
23  1 Y 1 A ASN 156 ? ND2 ? A ASN 155 ND2 
24  1 Y 1 A GLU 160 ? CG  ? A GLU 159 CG  
25  1 Y 1 A GLU 160 ? CD  ? A GLU 159 CD  
26  1 Y 1 A GLU 160 ? OE1 ? A GLU 159 OE1 
27  1 Y 1 A GLU 160 ? OE2 ? A GLU 159 OE2 
28  1 Y 1 A GLN 181 ? CG  ? A GLN 180 CG  
29  1 Y 1 A GLN 181 ? CD  ? A GLN 180 CD  
30  1 Y 1 A GLN 181 ? OE1 ? A GLN 180 OE1 
31  1 Y 1 A GLN 181 ? NE2 ? A GLN 180 NE2 
32  1 Y 1 A LEU 182 ? CG  ? A LEU 181 CG  
33  1 Y 1 A LEU 182 ? CD1 ? A LEU 181 CD1 
34  1 Y 1 A LEU 182 ? CD2 ? A LEU 181 CD2 
35  1 Y 1 A LEU 184 ? CG  ? A LEU 183 CG  
36  1 Y 1 A LEU 184 ? CD1 ? A LEU 183 CD1 
37  1 Y 1 A LEU 184 ? CD2 ? A LEU 183 CD2 
38  1 Y 1 A GLU 197 ? CG  ? A GLU 196 CG  
39  1 Y 1 A GLU 197 ? CD  ? A GLU 196 CD  
40  1 Y 1 A GLU 197 ? OE1 ? A GLU 196 OE1 
41  1 Y 1 A GLU 197 ? OE2 ? A GLU 196 OE2 
42  1 Y 1 A ARG 332 ? CG  ? A ARG 331 CG  
43  1 Y 1 A ARG 332 ? CD  ? A ARG 331 CD  
44  1 Y 1 A ARG 332 ? NE  ? A ARG 331 NE  
45  1 Y 1 A ARG 332 ? CZ  ? A ARG 331 CZ  
46  1 Y 1 A ARG 332 ? NH1 ? A ARG 331 NH1 
47  1 Y 1 A ARG 332 ? NH2 ? A ARG 331 NH2 
48  1 Y 1 A LYS 338 ? CG  ? A LYS 337 CG  
49  1 Y 1 A LYS 338 ? CD  ? A LYS 337 CD  
50  1 Y 1 A LYS 338 ? CE  ? A LYS 337 CE  
51  1 Y 1 A LYS 338 ? NZ  ? A LYS 337 NZ  
52  1 Y 1 A GLU 368 ? CG  ? A GLU 367 CG  
53  1 Y 1 A GLU 368 ? CD  ? A GLU 367 CD  
54  1 Y 1 A GLU 368 ? OE1 ? A GLU 367 OE1 
55  1 Y 1 A GLU 368 ? OE2 ? A GLU 367 OE2 
56  1 Y 1 A ARG 414 ? CG  ? A ARG 413 CG  
57  1 Y 1 A ARG 414 ? CD  ? A ARG 413 CD  
58  1 Y 1 A ARG 414 ? NE  ? A ARG 413 NE  
59  1 Y 1 A ARG 414 ? CZ  ? A ARG 413 CZ  
60  1 Y 1 A ARG 414 ? NH1 ? A ARG 413 NH1 
61  1 Y 1 A ARG 414 ? NH2 ? A ARG 413 NH2 
62  1 Y 1 A ARG 421 ? CG  ? A ARG 420 CG  
63  1 Y 1 A ARG 421 ? CD  ? A ARG 420 CD  
64  1 Y 1 A ARG 421 ? NE  ? A ARG 420 NE  
65  1 Y 1 A ARG 421 ? CZ  ? A ARG 420 CZ  
66  1 Y 1 A ARG 421 ? NH1 ? A ARG 420 NH1 
67  1 Y 1 A ARG 421 ? NH2 ? A ARG 420 NH2 
68  1 Y 1 A ARG 423 ? CG  ? A ARG 422 CG  
69  1 Y 1 A ARG 423 ? CD  ? A ARG 422 CD  
70  1 Y 1 A ARG 423 ? NE  ? A ARG 422 NE  
71  1 Y 1 A ARG 423 ? CZ  ? A ARG 422 CZ  
72  1 Y 1 A ARG 423 ? NH1 ? A ARG 422 NH1 
73  1 Y 1 A ARG 423 ? NH2 ? A ARG 422 NH2 
74  1 Y 1 A LYS 448 ? CG  ? A LYS 447 CG  
75  1 Y 1 A LYS 448 ? CD  ? A LYS 447 CD  
76  1 Y 1 A LYS 448 ? CE  ? A LYS 447 CE  
77  1 Y 1 A LYS 448 ? NZ  ? A LYS 447 NZ  
78  1 Y 1 B ARG 36  ? CG  ? B ARG 35  CG  
79  1 Y 1 B ARG 36  ? CD  ? B ARG 35  CD  
80  1 Y 1 B ARG 36  ? NE  ? B ARG 35  NE  
81  1 Y 1 B ARG 36  ? CZ  ? B ARG 35  CZ  
82  1 Y 1 B ARG 36  ? NH1 ? B ARG 35  NH1 
83  1 Y 1 B ARG 36  ? NH2 ? B ARG 35  NH2 
84  1 Y 1 B ARG 60  ? CG  ? B ARG 59  CG  
85  1 Y 1 B ARG 60  ? CD  ? B ARG 59  CD  
86  1 Y 1 B ARG 60  ? NE  ? B ARG 59  NE  
87  1 Y 1 B ARG 60  ? CZ  ? B ARG 59  CZ  
88  1 Y 1 B ARG 60  ? NH1 ? B ARG 59  NH1 
89  1 Y 1 B ARG 60  ? NH2 ? B ARG 59  NH2 
90  1 Y 1 B GLU 72  ? CG  ? B GLU 71  CG  
91  1 Y 1 B GLU 72  ? CD  ? B GLU 71  CD  
92  1 Y 1 B GLU 72  ? OE1 ? B GLU 71  OE1 
93  1 Y 1 B GLU 72  ? OE2 ? B GLU 71  OE2 
94  1 Y 1 B GLN 136 ? CG  ? B GLN 135 CG  
95  1 Y 1 B GLN 136 ? CD  ? B GLN 135 CD  
96  1 Y 1 B GLN 136 ? OE1 ? B GLN 135 OE1 
97  1 Y 1 B GLN 136 ? NE2 ? B GLN 135 NE2 
98  1 Y 1 B ARG 139 ? CG  ? B ARG 138 CG  
99  1 Y 1 B ARG 139 ? CD  ? B ARG 138 CD  
100 1 Y 1 B ARG 139 ? NE  ? B ARG 138 NE  
101 1 Y 1 B ARG 139 ? CZ  ? B ARG 138 CZ  
102 1 Y 1 B ARG 139 ? NH1 ? B ARG 138 NH1 
103 1 Y 1 B ARG 139 ? NH2 ? B ARG 138 NH2 
104 1 Y 1 B ASN 156 ? CG  ? B ASN 155 CG  
105 1 Y 1 B ASN 156 ? OD1 ? B ASN 155 OD1 
106 1 Y 1 B ASN 156 ? ND2 ? B ASN 155 ND2 
107 1 Y 1 B HIS 158 ? CG  ? B HIS 157 CG  
108 1 Y 1 B HIS 158 ? ND1 ? B HIS 157 ND1 
109 1 Y 1 B HIS 158 ? CD2 ? B HIS 157 CD2 
110 1 Y 1 B HIS 158 ? CE1 ? B HIS 157 CE1 
111 1 Y 1 B HIS 158 ? NE2 ? B HIS 157 NE2 
112 1 Y 1 B GLN 181 ? CG  ? B GLN 180 CG  
113 1 Y 1 B GLN 181 ? CD  ? B GLN 180 CD  
114 1 Y 1 B GLN 181 ? OE1 ? B GLN 180 OE1 
115 1 Y 1 B GLN 181 ? NE2 ? B GLN 180 NE2 
116 1 Y 1 B ASP 186 ? CG  ? B ASP 185 CG  
117 1 Y 1 B ASP 186 ? OD1 ? B ASP 185 OD1 
118 1 Y 1 B ASP 186 ? OD2 ? B ASP 185 OD2 
119 1 Y 1 B ASP 187 ? CG  ? B ASP 186 CG  
120 1 Y 1 B ASP 187 ? OD1 ? B ASP 186 OD1 
121 1 Y 1 B ASP 187 ? OD2 ? B ASP 186 OD2 
122 1 Y 1 B ASP 190 ? CG  ? B ASP 189 CG  
123 1 Y 1 B ASP 190 ? OD1 ? B ASP 189 OD1 
124 1 Y 1 B ASP 190 ? OD2 ? B ASP 189 OD2 
125 1 Y 1 B ARG 210 ? CG  ? B ARG 209 CG  
126 1 Y 1 B ARG 210 ? CD  ? B ARG 209 CD  
127 1 Y 1 B ARG 210 ? NE  ? B ARG 209 NE  
128 1 Y 1 B ARG 210 ? CZ  ? B ARG 209 CZ  
129 1 Y 1 B ARG 210 ? NH1 ? B ARG 209 NH1 
130 1 Y 1 B ARG 210 ? NH2 ? B ARG 209 NH2 
131 1 Y 1 B GLU 245 ? CG  ? B GLU 244 CG  
132 1 Y 1 B GLU 245 ? CD  ? B GLU 244 CD  
133 1 Y 1 B GLU 245 ? OE1 ? B GLU 244 OE1 
134 1 Y 1 B GLU 245 ? OE2 ? B GLU 244 OE2 
135 1 Y 1 B ARG 266 ? CG  ? B ARG 265 CG  
136 1 Y 1 B ARG 266 ? CD  ? B ARG 265 CD  
137 1 Y 1 B ARG 266 ? NE  ? B ARG 265 NE  
138 1 Y 1 B ARG 266 ? CZ  ? B ARG 265 CZ  
139 1 Y 1 B ARG 266 ? NH1 ? B ARG 265 NH1 
140 1 Y 1 B ARG 266 ? NH2 ? B ARG 265 NH2 
141 1 Y 1 B ASP 333 ? CG  ? B ASP 332 CG  
142 1 Y 1 B ASP 333 ? OD1 ? B ASP 332 OD1 
143 1 Y 1 B ASP 333 ? OD2 ? B ASP 332 OD2 
144 1 Y 1 B ARG 361 ? CG  ? B ARG 360 CG  
145 1 Y 1 B ARG 361 ? CD  ? B ARG 360 CD  
146 1 Y 1 B ARG 361 ? NE  ? B ARG 360 NE  
147 1 Y 1 B ARG 361 ? CZ  ? B ARG 360 CZ  
148 1 Y 1 B ARG 361 ? NH1 ? B ARG 360 NH1 
149 1 Y 1 B ARG 361 ? NH2 ? B ARG 360 NH2 
150 1 Y 1 B LYS 363 ? CG  ? B LYS 362 CG  
151 1 Y 1 B LYS 363 ? CD  ? B LYS 362 CD  
152 1 Y 1 B LYS 363 ? CE  ? B LYS 362 CE  
153 1 Y 1 B LYS 363 ? NZ  ? B LYS 362 NZ  
154 1 Y 1 B GLU 368 ? CG  ? B GLU 367 CG  
155 1 Y 1 B GLU 368 ? CD  ? B GLU 367 CD  
156 1 Y 1 B GLU 368 ? OE1 ? B GLU 367 OE1 
157 1 Y 1 B GLU 368 ? OE2 ? B GLU 367 OE2 
158 1 Y 1 B ARG 369 ? CG  ? B ARG 368 CG  
159 1 Y 1 B ARG 369 ? CD  ? B ARG 368 CD  
160 1 Y 1 B ARG 369 ? NE  ? B ARG 368 NE  
161 1 Y 1 B ARG 369 ? CZ  ? B ARG 368 CZ  
162 1 Y 1 B ARG 369 ? NH1 ? B ARG 368 NH1 
163 1 Y 1 B ARG 369 ? NH2 ? B ARG 368 NH2 
164 1 Y 1 B GLU 376 ? CG  ? B GLU 375 CG  
165 1 Y 1 B GLU 376 ? CD  ? B GLU 375 CD  
166 1 Y 1 B GLU 376 ? OE1 ? B GLU 375 OE1 
167 1 Y 1 B GLU 376 ? OE2 ? B GLU 375 OE2 
168 1 Y 1 B ARG 387 ? CG  ? B ARG 386 CG  
169 1 Y 1 B ARG 387 ? CD  ? B ARG 386 CD  
170 1 Y 1 B ARG 387 ? NE  ? B ARG 386 NE  
171 1 Y 1 B ARG 387 ? CZ  ? B ARG 386 CZ  
172 1 Y 1 B ARG 387 ? NH1 ? B ARG 386 NH1 
173 1 Y 1 B ARG 387 ? NH2 ? B ARG 386 NH2 
174 1 Y 1 B MET 451 ? SD  ? B MET 450 SD  
175 1 Y 1 B MET 451 ? CE  ? B MET 450 CE  
176 1 Y 1 B ARG 454 ? CG  ? B ARG 453 CG  
177 1 Y 1 B ARG 454 ? CD  ? B ARG 453 CD  
178 1 Y 1 B ARG 454 ? NE  ? B ARG 453 NE  
179 1 Y 1 B ARG 454 ? CZ  ? B ARG 453 CZ  
180 1 Y 1 B ARG 454 ? NH1 ? B ARG 453 NH1 
181 1 Y 1 B ARG 454 ? NH2 ? B ARG 453 NH2 
182 1 Y 1 B ARG 468 ? CG  ? B ARG 467 CG  
183 1 Y 1 B ARG 468 ? CD  ? B ARG 467 CD  
184 1 Y 1 B ARG 468 ? NE  ? B ARG 467 NE  
185 1 Y 1 B ARG 468 ? CZ  ? B ARG 467 CZ  
186 1 Y 1 B ARG 468 ? NH1 ? B ARG 467 NH1 
187 1 Y 1 B ARG 468 ? NH2 ? B ARG 467 NH2 
188 1 Y 1 C GLU 34  ? CG  ? C GLU 33  CG  
189 1 Y 1 C GLU 34  ? CD  ? C GLU 33  CD  
190 1 Y 1 C GLU 34  ? OE1 ? C GLU 33  OE1 
191 1 Y 1 C GLU 34  ? OE2 ? C GLU 33  OE2 
192 1 Y 1 C GLU 57  ? CG  ? C GLU 56  CG  
193 1 Y 1 C GLU 57  ? CD  ? C GLU 56  CD  
194 1 Y 1 C GLU 57  ? OE1 ? C GLU 56  OE1 
195 1 Y 1 C GLU 57  ? OE2 ? C GLU 56  OE2 
196 1 Y 1 C ARG 60  ? CG  ? C ARG 59  CG  
197 1 Y 1 C ARG 60  ? CD  ? C ARG 59  CD  
198 1 Y 1 C ARG 60  ? NE  ? C ARG 59  NE  
199 1 Y 1 C ARG 60  ? CZ  ? C ARG 59  CZ  
200 1 Y 1 C ARG 60  ? NH1 ? C ARG 59  NH1 
201 1 Y 1 C ARG 60  ? NH2 ? C ARG 59  NH2 
202 1 Y 1 C ARG 105 ? CG  ? C ARG 104 CG  
203 1 Y 1 C ARG 105 ? CD  ? C ARG 104 CD  
204 1 Y 1 C ARG 105 ? NE  ? C ARG 104 NE  
205 1 Y 1 C ARG 105 ? CZ  ? C ARG 104 CZ  
206 1 Y 1 C ARG 105 ? NH1 ? C ARG 104 NH1 
207 1 Y 1 C ARG 105 ? NH2 ? C ARG 104 NH2 
208 1 Y 1 C ARG 139 ? CG  ? C ARG 138 CG  
209 1 Y 1 C ARG 139 ? CD  ? C ARG 138 CD  
210 1 Y 1 C ARG 139 ? NE  ? C ARG 138 NE  
211 1 Y 1 C ARG 139 ? CZ  ? C ARG 138 CZ  
212 1 Y 1 C ARG 139 ? NH1 ? C ARG 138 NH1 
213 1 Y 1 C ARG 139 ? NH2 ? C ARG 138 NH2 
214 1 Y 1 C HIS 158 ? CG  ? C HIS 157 CG  
215 1 Y 1 C HIS 158 ? ND1 ? C HIS 157 ND1 
216 1 Y 1 C HIS 158 ? CD2 ? C HIS 157 CD2 
217 1 Y 1 C HIS 158 ? CE1 ? C HIS 157 CE1 
218 1 Y 1 C HIS 158 ? NE2 ? C HIS 157 NE2 
219 1 Y 1 C GLU 161 ? CG  ? C GLU 160 CG  
220 1 Y 1 C GLU 161 ? CD  ? C GLU 160 CD  
221 1 Y 1 C GLU 161 ? OE1 ? C GLU 160 OE1 
222 1 Y 1 C GLU 161 ? OE2 ? C GLU 160 OE2 
223 1 Y 1 C ARG 169 ? CG  ? C ARG 168 CG  
224 1 Y 1 C ARG 169 ? CD  ? C ARG 168 CD  
225 1 Y 1 C ARG 169 ? NE  ? C ARG 168 NE  
226 1 Y 1 C ARG 169 ? CZ  ? C ARG 168 CZ  
227 1 Y 1 C ARG 169 ? NH1 ? C ARG 168 NH1 
228 1 Y 1 C ARG 169 ? NH2 ? C ARG 168 NH2 
229 1 Y 1 C LEU 182 ? CG  ? C LEU 181 CG  
230 1 Y 1 C LEU 182 ? CD1 ? C LEU 181 CD1 
231 1 Y 1 C LEU 182 ? CD2 ? C LEU 181 CD2 
232 1 Y 1 C LEU 183 ? CG  ? C LEU 182 CG  
233 1 Y 1 C LEU 183 ? CD1 ? C LEU 182 CD1 
234 1 Y 1 C LEU 183 ? CD2 ? C LEU 182 CD2 
235 1 Y 1 C LEU 184 ? CG  ? C LEU 183 CG  
236 1 Y 1 C LEU 184 ? CD1 ? C LEU 183 CD1 
237 1 Y 1 C LEU 184 ? CD2 ? C LEU 183 CD2 
238 1 Y 1 C ARG 200 ? CG  ? C ARG 199 CG  
239 1 Y 1 C ARG 200 ? CD  ? C ARG 199 CD  
240 1 Y 1 C ARG 200 ? NE  ? C ARG 199 NE  
241 1 Y 1 C ARG 200 ? CZ  ? C ARG 199 CZ  
242 1 Y 1 C ARG 200 ? NH1 ? C ARG 199 NH1 
243 1 Y 1 C ARG 200 ? NH2 ? C ARG 199 NH2 
244 1 Y 1 C ARG 210 ? CG  ? C ARG 209 CG  
245 1 Y 1 C ARG 210 ? CD  ? C ARG 209 CD  
246 1 Y 1 C ARG 210 ? NE  ? C ARG 209 NE  
247 1 Y 1 C ARG 210 ? CZ  ? C ARG 209 CZ  
248 1 Y 1 C ARG 210 ? NH1 ? C ARG 209 NH1 
249 1 Y 1 C ARG 210 ? NH2 ? C ARG 209 NH2 
250 1 Y 1 C ARG 248 ? NE  ? C ARG 247 NE  
251 1 Y 1 C ARG 248 ? CZ  ? C ARG 247 CZ  
252 1 Y 1 C ARG 248 ? NH1 ? C ARG 247 NH1 
253 1 Y 1 C ARG 248 ? NH2 ? C ARG 247 NH2 
254 1 Y 1 C GLU 311 ? CG  ? C GLU 310 CG  
255 1 Y 1 C GLU 311 ? CD  ? C GLU 310 CD  
256 1 Y 1 C GLU 311 ? OE1 ? C GLU 310 OE1 
257 1 Y 1 C GLU 311 ? OE2 ? C GLU 310 OE2 
258 1 Y 1 C ARG 332 ? CG  ? C ARG 331 CG  
259 1 Y 1 C ARG 332 ? CD  ? C ARG 331 CD  
260 1 Y 1 C ARG 332 ? NE  ? C ARG 331 NE  
261 1 Y 1 C ARG 332 ? CZ  ? C ARG 331 CZ  
262 1 Y 1 C ARG 332 ? NH1 ? C ARG 331 NH1 
263 1 Y 1 C ARG 332 ? NH2 ? C ARG 331 NH2 
264 1 Y 1 C LYS 338 ? CG  ? C LYS 337 CG  
265 1 Y 1 C LYS 338 ? CD  ? C LYS 337 CD  
266 1 Y 1 C LYS 338 ? CE  ? C LYS 337 CE  
267 1 Y 1 C LYS 338 ? NZ  ? C LYS 337 NZ  
268 1 Y 1 C ARG 367 ? CG  ? C ARG 366 CG  
269 1 Y 1 C ARG 367 ? CD  ? C ARG 366 CD  
270 1 Y 1 C ARG 367 ? NE  ? C ARG 366 NE  
271 1 Y 1 C ARG 367 ? CZ  ? C ARG 366 CZ  
272 1 Y 1 C ARG 367 ? NH1 ? C ARG 366 NH1 
273 1 Y 1 C ARG 367 ? NH2 ? C ARG 366 NH2 
274 1 Y 1 C GLU 368 ? CG  ? C GLU 367 CG  
275 1 Y 1 C GLU 368 ? CD  ? C GLU 367 CD  
276 1 Y 1 C GLU 368 ? OE1 ? C GLU 367 OE1 
277 1 Y 1 C GLU 368 ? OE2 ? C GLU 367 OE2 
278 1 Y 1 C ARG 369 ? CG  ? C ARG 368 CG  
279 1 Y 1 C ARG 369 ? CD  ? C ARG 368 CD  
280 1 Y 1 C ARG 369 ? NE  ? C ARG 368 NE  
281 1 Y 1 C ARG 369 ? CZ  ? C ARG 368 CZ  
282 1 Y 1 C ARG 369 ? NH1 ? C ARG 368 NH1 
283 1 Y 1 C ARG 369 ? NH2 ? C ARG 368 NH2 
284 1 Y 1 C ARG 421 ? CG  ? C ARG 420 CG  
285 1 Y 1 C ARG 421 ? CD  ? C ARG 420 CD  
286 1 Y 1 C ARG 421 ? NE  ? C ARG 420 NE  
287 1 Y 1 C ARG 421 ? CZ  ? C ARG 420 CZ  
288 1 Y 1 C ARG 421 ? NH1 ? C ARG 420 NH1 
289 1 Y 1 C ARG 421 ? NH2 ? C ARG 420 NH2 
290 1 Y 1 C MET 458 ? CG  ? C MET 457 CG  
291 1 Y 1 C MET 458 ? SD  ? C MET 457 SD  
292 1 Y 1 C MET 458 ? CE  ? C MET 457 CE  
293 1 Y 1 D ARG 36  ? CG  ? D ARG 35  CG  
294 1 Y 1 D ARG 36  ? CD  ? D ARG 35  CD  
295 1 Y 1 D ARG 36  ? NE  ? D ARG 35  NE  
296 1 Y 1 D ARG 36  ? CZ  ? D ARG 35  CZ  
297 1 Y 1 D ARG 36  ? NH1 ? D ARG 35  NH1 
298 1 Y 1 D ARG 36  ? NH2 ? D ARG 35  NH2 
299 1 Y 1 D GLU 57  ? CG  ? D GLU 56  CG  
300 1 Y 1 D GLU 57  ? CD  ? D GLU 56  CD  
301 1 Y 1 D GLU 57  ? OE1 ? D GLU 56  OE1 
302 1 Y 1 D GLU 57  ? OE2 ? D GLU 56  OE2 
303 1 Y 1 D ARG 60  ? CG  ? D ARG 59  CG  
304 1 Y 1 D ARG 60  ? CD  ? D ARG 59  CD  
305 1 Y 1 D ARG 60  ? NE  ? D ARG 59  NE  
306 1 Y 1 D ARG 60  ? CZ  ? D ARG 59  CZ  
307 1 Y 1 D ARG 60  ? NH1 ? D ARG 59  NH1 
308 1 Y 1 D ARG 60  ? NH2 ? D ARG 59  NH2 
309 1 Y 1 D GLU 72  ? CG  ? D GLU 71  CG  
310 1 Y 1 D GLU 72  ? CD  ? D GLU 71  CD  
311 1 Y 1 D GLU 72  ? OE1 ? D GLU 71  OE1 
312 1 Y 1 D GLU 72  ? OE2 ? D GLU 71  OE2 
313 1 Y 1 D GLU 75  ? CD  ? D GLU 74  CD  
314 1 Y 1 D GLU 75  ? OE1 ? D GLU 74  OE1 
315 1 Y 1 D GLU 75  ? OE2 ? D GLU 74  OE2 
316 1 Y 1 D ARG 120 ? NE  ? D ARG 119 NE  
317 1 Y 1 D ARG 120 ? CZ  ? D ARG 119 CZ  
318 1 Y 1 D ARG 120 ? NH1 ? D ARG 119 NH1 
319 1 Y 1 D ARG 120 ? NH2 ? D ARG 119 NH2 
320 1 Y 1 D ASN 156 ? CG  ? D ASN 155 CG  
321 1 Y 1 D ASN 156 ? OD1 ? D ASN 155 OD1 
322 1 Y 1 D ASN 156 ? ND2 ? D ASN 155 ND2 
323 1 Y 1 D HIS 158 ? CG  ? D HIS 157 CG  
324 1 Y 1 D HIS 158 ? ND1 ? D HIS 157 ND1 
325 1 Y 1 D HIS 158 ? CD2 ? D HIS 157 CD2 
326 1 Y 1 D HIS 158 ? CE1 ? D HIS 157 CE1 
327 1 Y 1 D HIS 158 ? NE2 ? D HIS 157 NE2 
328 1 Y 1 D ARG 173 ? CG  ? D ARG 172 CG  
329 1 Y 1 D ARG 173 ? CD  ? D ARG 172 CD  
330 1 Y 1 D ARG 173 ? NE  ? D ARG 172 NE  
331 1 Y 1 D ARG 173 ? CZ  ? D ARG 172 CZ  
332 1 Y 1 D ARG 173 ? NH1 ? D ARG 172 NH1 
333 1 Y 1 D ARG 173 ? NH2 ? D ARG 172 NH2 
334 1 Y 1 D GLN 181 ? CG  ? D GLN 180 CG  
335 1 Y 1 D GLN 181 ? CD  ? D GLN 180 CD  
336 1 Y 1 D GLN 181 ? OE1 ? D GLN 180 OE1 
337 1 Y 1 D GLN 181 ? NE2 ? D GLN 180 NE2 
338 1 Y 1 D LEU 182 ? CG  ? D LEU 181 CG  
339 1 Y 1 D LEU 182 ? CD1 ? D LEU 181 CD1 
340 1 Y 1 D LEU 182 ? CD2 ? D LEU 181 CD2 
341 1 Y 1 D LEU 183 ? CG  ? D LEU 182 CG  
342 1 Y 1 D LEU 183 ? CD1 ? D LEU 182 CD1 
343 1 Y 1 D LEU 183 ? CD2 ? D LEU 182 CD2 
344 1 Y 1 D ASP 186 ? CG  ? D ASP 185 CG  
345 1 Y 1 D ASP 186 ? OD1 ? D ASP 185 OD1 
346 1 Y 1 D ASP 186 ? OD2 ? D ASP 185 OD2 
347 1 Y 1 D GLU 197 ? CG  ? D GLU 196 CG  
348 1 Y 1 D GLU 197 ? CD  ? D GLU 196 CD  
349 1 Y 1 D GLU 197 ? OE1 ? D GLU 196 OE1 
350 1 Y 1 D GLU 197 ? OE2 ? D GLU 196 OE2 
351 1 Y 1 D ARG 210 ? CG  ? D ARG 209 CG  
352 1 Y 1 D ARG 210 ? CD  ? D ARG 209 CD  
353 1 Y 1 D ARG 210 ? NE  ? D ARG 209 NE  
354 1 Y 1 D ARG 210 ? CZ  ? D ARG 209 CZ  
355 1 Y 1 D ARG 210 ? NH1 ? D ARG 209 NH1 
356 1 Y 1 D ARG 210 ? NH2 ? D ARG 209 NH2 
357 1 Y 1 D ARG 215 ? NE  ? D ARG 214 NE  
358 1 Y 1 D ARG 215 ? CZ  ? D ARG 214 CZ  
359 1 Y 1 D ARG 215 ? NH1 ? D ARG 214 NH1 
360 1 Y 1 D ARG 215 ? NH2 ? D ARG 214 NH2 
361 1 Y 1 D ARG 266 ? NE  ? D ARG 265 NE  
362 1 Y 1 D ARG 266 ? CZ  ? D ARG 265 CZ  
363 1 Y 1 D ARG 266 ? NH1 ? D ARG 265 NH1 
364 1 Y 1 D ARG 266 ? NH2 ? D ARG 265 NH2 
365 1 Y 1 D ARG 332 ? CG  ? D ARG 331 CG  
366 1 Y 1 D ARG 332 ? CD  ? D ARG 331 CD  
367 1 Y 1 D ARG 332 ? NE  ? D ARG 331 NE  
368 1 Y 1 D ARG 332 ? CZ  ? D ARG 331 CZ  
369 1 Y 1 D ARG 332 ? NH1 ? D ARG 331 NH1 
370 1 Y 1 D ARG 332 ? NH2 ? D ARG 331 NH2 
371 1 Y 1 D LYS 338 ? CG  ? D LYS 337 CG  
372 1 Y 1 D LYS 338 ? CD  ? D LYS 337 CD  
373 1 Y 1 D LYS 338 ? CE  ? D LYS 337 CE  
374 1 Y 1 D LYS 338 ? NZ  ? D LYS 337 NZ  
375 1 Y 1 D LYS 347 ? CG  ? D LYS 346 CG  
376 1 Y 1 D LYS 347 ? CD  ? D LYS 346 CD  
377 1 Y 1 D LYS 347 ? CE  ? D LYS 346 CE  
378 1 Y 1 D LYS 347 ? NZ  ? D LYS 346 NZ  
379 1 Y 1 D ARG 361 ? CG  ? D ARG 360 CG  
380 1 Y 1 D ARG 361 ? CD  ? D ARG 360 CD  
381 1 Y 1 D ARG 361 ? NE  ? D ARG 360 NE  
382 1 Y 1 D ARG 361 ? CZ  ? D ARG 360 CZ  
383 1 Y 1 D ARG 361 ? NH1 ? D ARG 360 NH1 
384 1 Y 1 D ARG 361 ? NH2 ? D ARG 360 NH2 
385 1 Y 1 D LYS 363 ? CG  ? D LYS 362 CG  
386 1 Y 1 D LYS 363 ? CD  ? D LYS 362 CD  
387 1 Y 1 D LYS 363 ? CE  ? D LYS 362 CE  
388 1 Y 1 D LYS 363 ? NZ  ? D LYS 362 NZ  
389 1 Y 1 D GLU 368 ? CG  ? D GLU 367 CG  
390 1 Y 1 D GLU 368 ? CD  ? D GLU 367 CD  
391 1 Y 1 D GLU 368 ? OE1 ? D GLU 367 OE1 
392 1 Y 1 D GLU 368 ? OE2 ? D GLU 367 OE2 
393 1 Y 1 D ARG 369 ? O   ? D ARG 368 O   
394 1 Y 1 D ARG 369 ? CG  ? D ARG 368 CG  
395 1 Y 1 D ARG 369 ? CD  ? D ARG 368 CD  
396 1 Y 1 D ARG 369 ? NE  ? D ARG 368 NE  
397 1 Y 1 D ARG 369 ? CZ  ? D ARG 368 CZ  
398 1 Y 1 D ARG 369 ? NH1 ? D ARG 368 NH1 
399 1 Y 1 D ARG 369 ? NH2 ? D ARG 368 NH2 
400 1 Y 1 D ASP 413 ? CG  ? D ASP 412 CG  
401 1 Y 1 D ASP 413 ? OD1 ? D ASP 412 OD1 
402 1 Y 1 D ASP 413 ? OD2 ? D ASP 412 OD2 
403 1 Y 1 D ARG 414 ? CG  ? D ARG 413 CG  
404 1 Y 1 D ARG 414 ? CD  ? D ARG 413 CD  
405 1 Y 1 D ARG 414 ? NE  ? D ARG 413 NE  
406 1 Y 1 D ARG 414 ? CZ  ? D ARG 413 CZ  
407 1 Y 1 D ARG 414 ? NH1 ? D ARG 413 NH1 
408 1 Y 1 D ARG 414 ? NH2 ? D ARG 413 NH2 
409 1 Y 1 D LYS 448 ? CG  ? D LYS 447 CG  
410 1 Y 1 D LYS 448 ? CD  ? D LYS 447 CD  
411 1 Y 1 D LYS 448 ? CE  ? D LYS 447 CE  
412 1 Y 1 D LYS 448 ? NZ  ? D LYS 447 NZ  
413 1 Y 1 D ARG 454 ? CG  ? D ARG 453 CG  
414 1 Y 1 D ARG 454 ? CD  ? D ARG 453 CD  
415 1 Y 1 D ARG 454 ? NE  ? D ARG 453 NE  
416 1 Y 1 D ARG 454 ? CZ  ? D ARG 453 CZ  
417 1 Y 1 D ARG 454 ? NH1 ? D ARG 453 NH1 
418 1 Y 1 D ARG 454 ? NH2 ? D ARG 453 NH2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A ALA 2   ? A ALA 1   
2   1 Y 1 A PRO 3   ? A PRO 2   
3   1 Y 1 A GLN 4   ? A GLN 3   
4   1 Y 1 A LEU 5   ? A LEU 4   
5   1 Y 1 A HIS 6   ? A HIS 5   
6   1 Y 1 A HIS 7   ? A HIS 6   
7   1 Y 1 A HIS 8   ? A HIS 7   
8   1 Y 1 A HIS 9   ? A HIS 8   
9   1 Y 1 A HIS 10  ? A HIS 9   
10  1 Y 1 A HIS 11  ? A HIS 10  
11  1 Y 1 A ASP 12  ? A ASP 11  
12  1 Y 1 A LEU 13  ? A LEU 12  
13  1 Y 1 A TYR 14  ? A TYR 13  
14  1 Y 1 A GLU 15  ? A GLU 14  
15  1 Y 1 A ASN 16  ? A ASN 15  
16  1 Y 1 A LEU 17  ? A LEU 16  
17  1 Y 1 A TYR 18  ? A TYR 17  
18  1 Y 1 A PHE 19  ? A PHE 18  
19  1 Y 1 A GLN 20  ? A GLN 19  
20  1 Y 1 A GLY 21  ? A GLY 20  
21  1 Y 1 A LYS 22  ? A LYS 21  
22  1 Y 1 A LEU 23  ? A LEU 22  
23  1 Y 1 A ASP 24  ? A ASP 23  
24  1 Y 1 A ASP 187 ? A ASP 186 
25  1 Y 1 A TYR 188 ? A TYR 187 
26  1 Y 1 A LEU 189 ? A LEU 188 
27  1 Y 1 A ASP 190 ? A ASP 189 
28  1 Y 1 A CYS 191 ? A CYS 190 
29  1 Y 1 A LEU 192 ? A LEU 191 
30  1 Y 1 A ILE 340 ? A ILE 339 
31  1 Y 1 A GLN 341 ? A GLN 340 
32  1 Y 1 A GLY 342 ? A GLY 341 
33  1 Y 1 A CYS 343 ? A CYS 342 
34  1 Y 1 A GLY 344 ? A GLY 343 
35  1 Y 1 A ASN 345 ? A ASN 344 
36  1 Y 1 A PRO 346 ? A PRO 345 
37  1 Y 1 A LYS 347 ? A LYS 346 
38  1 Y 1 A VAL 348 ? A VAL 347 
39  1 Y 1 A ASN 349 ? A ASN 348 
40  1 Y 1 A PRO 350 ? A PRO 349 
41  1 Y 1 A GLN 351 ? A GLN 350 
42  1 Y 1 A GLY 352 ? A GLY 351 
43  1 Y 1 A PRO 353 ? A PRO 352 
44  1 Y 1 A GLY 354 ? A GLY 353 
45  1 Y 1 A PRO 355 ? A PRO 354 
46  1 Y 1 A GLU 356 ? A GLU 355 
47  1 Y 1 A GLU 357 ? A GLU 356 
48  1 Y 1 A LYS 358 ? A LYS 357 
49  1 Y 1 A ARG 359 ? A ARG 358 
50  1 Y 1 A ARG 360 ? A ARG 359 
51  1 Y 1 A ARG 361 ? A ARG 360 
52  1 Y 1 A GLY 362 ? A GLY 361 
53  1 Y 1 A LYS 363 ? A LYS 362 
54  1 Y 1 A LEU 364 ? A LEU 363 
55  1 Y 1 A ALA 365 ? A ALA 364 
56  1 Y 1 A LEU 407 ? A LEU 406 
57  1 Y 1 A SER 408 ? A SER 407 
58  1 Y 1 A THR 409 ? A THR 408 
59  1 Y 1 A ALA 410 ? A ALA 409 
60  1 Y 1 A SER 411 ? A SER 410 
61  1 Y 1 A ASP 412 ? A ASP 411 
62  1 Y 1 A ASN 474 ? A ASN 473 
63  1 Y 1 A ASP 475 ? A ASP 474 
64  1 Y 1 A VAL 476 ? A VAL 475 
65  1 Y 1 A ASP 477 ? A ASP 476 
66  1 Y 1 A PHE 478 ? A PHE 477 
67  1 Y 1 A GLN 479 ? A GLN 478 
68  1 Y 1 A ASP 480 ? A ASP 479 
69  1 Y 1 A ALA 481 ? A ALA 480 
70  1 Y 1 A SER 482 ? A SER 481 
71  1 Y 1 A ASP 483 ? A ASP 482 
72  1 Y 1 A ASP 484 ? A ASP 483 
73  1 Y 1 A GLY 485 ? A GLY 484 
74  1 Y 1 A ALA 486 ? A ALA 485 
75  1 Y 1 A GLY 487 ? A GLY 486 
76  1 Y 1 A ALA 488 ? A ALA 487 
77  1 Y 1 A GLY 489 ? A GLY 488 
78  1 Y 1 A ALA 490 ? A ALA 489 
79  1 Y 1 A GLY 491 ? A GLY 490 
80  1 Y 1 A ASP 492 ? A ASP 491 
81  1 Y 1 A GLY 493 ? A GLY 492 
82  1 Y 1 A CYS 494 ? A CYS 493 
83  1 Y 1 A LEU 495 ? A LEU 494 
84  1 Y 1 A ASP 496 ? A ASP 495 
85  1 Y 1 A ASP 497 ? A ASP 496 
86  1 Y 1 A LEU 498 ? A LEU 497 
87  1 Y 1 A CYS 499 ? A CYS 498 
88  1 Y 1 A SER 500 ? A SER 499 
89  1 Y 1 A ARG 501 ? A ARG 500 
90  1 Y 1 A LYS 502 ? A LYS 501 
91  1 Y 1 A VAL 503 ? A VAL 502 
92  1 Y 1 A SER 504 ? A SER 503 
93  1 Y 1 A ARG 505 ? A ARG 504 
94  1 Y 1 A LYS 506 ? A LYS 505 
95  1 Y 1 A SER 507 ? A SER 506 
96  1 Y 1 A SER 508 ? A SER 507 
97  1 Y 1 A SER 509 ? A SER 508 
98  1 Y 1 A SER 510 ? A SER 509 
99  1 Y 1 A ARG 511 ? A ARG 510 
100 1 Y 1 A THR 512 ? A THR 511 
101 1 Y 1 A PRO 513 ? A PRO 512 
102 1 Y 1 A LEU 514 ? A LEU 513 
103 1 Y 1 A THR 515 ? A THR 514 
104 1 Y 1 A HIS 516 ? A HIS 515 
105 1 Y 1 A ALA 517 ? A ALA 516 
106 1 Y 1 A LEU 518 ? A LEU 517 
107 1 Y 1 A PRO 519 ? A PRO 518 
108 1 Y 1 A GLY 520 ? A GLY 519 
109 1 Y 1 A LEU 521 ? A LEU 520 
110 1 Y 1 A SER 522 ? A SER 521 
111 1 Y 1 A GLU 523 ? A GLU 522 
112 1 Y 1 A GLN 524 ? A GLN 523 
113 1 Y 1 A GLU 525 ? A GLU 524 
114 1 Y 1 A GLY 526 ? A GLY 525 
115 1 Y 1 A GLN 527 ? A GLN 526 
116 1 Y 1 B ALA 2   ? B ALA 1   
117 1 Y 1 B PRO 3   ? B PRO 2   
118 1 Y 1 B GLN 4   ? B GLN 3   
119 1 Y 1 B LEU 5   ? B LEU 4   
120 1 Y 1 B HIS 6   ? B HIS 5   
121 1 Y 1 B HIS 7   ? B HIS 6   
122 1 Y 1 B HIS 8   ? B HIS 7   
123 1 Y 1 B HIS 9   ? B HIS 8   
124 1 Y 1 B HIS 10  ? B HIS 9   
125 1 Y 1 B HIS 11  ? B HIS 10  
126 1 Y 1 B ASP 12  ? B ASP 11  
127 1 Y 1 B LEU 13  ? B LEU 12  
128 1 Y 1 B TYR 14  ? B TYR 13  
129 1 Y 1 B GLU 15  ? B GLU 14  
130 1 Y 1 B ASN 16  ? B ASN 15  
131 1 Y 1 B LEU 17  ? B LEU 16  
132 1 Y 1 B TYR 18  ? B TYR 17  
133 1 Y 1 B PHE 19  ? B PHE 18  
134 1 Y 1 B GLN 20  ? B GLN 19  
135 1 Y 1 B GLY 21  ? B GLY 20  
136 1 Y 1 B LYS 22  ? B LYS 21  
137 1 Y 1 B LEU 23  ? B LEU 22  
138 1 Y 1 B ASP 24  ? B ASP 23  
139 1 Y 1 B PRO 25  ? B PRO 24  
140 1 Y 1 B ALA 26  ? B ALA 25  
141 1 Y 1 B SER 27  ? B SER 26  
142 1 Y 1 B LYS 28  ? B LYS 27  
143 1 Y 1 B PRO 350 ? B PRO 349 
144 1 Y 1 B GLN 351 ? B GLN 350 
145 1 Y 1 B GLY 352 ? B GLY 351 
146 1 Y 1 B PRO 353 ? B PRO 352 
147 1 Y 1 B GLY 354 ? B GLY 353 
148 1 Y 1 B PRO 355 ? B PRO 354 
149 1 Y 1 B GLU 356 ? B GLU 355 
150 1 Y 1 B GLU 357 ? B GLU 356 
151 1 Y 1 B LYS 358 ? B LYS 357 
152 1 Y 1 B ARG 359 ? B ARG 358 
153 1 Y 1 B ARG 360 ? B ARG 359 
154 1 Y 1 B SER 408 ? B SER 407 
155 1 Y 1 B THR 409 ? B THR 408 
156 1 Y 1 B ALA 410 ? B ALA 409 
157 1 Y 1 B SER 411 ? B SER 410 
158 1 Y 1 B ASP 412 ? B ASP 411 
159 1 Y 1 B VAL 476 ? B VAL 475 
160 1 Y 1 B ASP 477 ? B ASP 476 
161 1 Y 1 B PHE 478 ? B PHE 477 
162 1 Y 1 B GLN 479 ? B GLN 478 
163 1 Y 1 B ASP 480 ? B ASP 479 
164 1 Y 1 B ALA 481 ? B ALA 480 
165 1 Y 1 B SER 482 ? B SER 481 
166 1 Y 1 B ASP 483 ? B ASP 482 
167 1 Y 1 B ASP 484 ? B ASP 483 
168 1 Y 1 B GLY 485 ? B GLY 484 
169 1 Y 1 B ALA 486 ? B ALA 485 
170 1 Y 1 B GLY 487 ? B GLY 486 
171 1 Y 1 B ALA 488 ? B ALA 487 
172 1 Y 1 B GLY 489 ? B GLY 488 
173 1 Y 1 B ALA 490 ? B ALA 489 
174 1 Y 1 B GLY 491 ? B GLY 490 
175 1 Y 1 B ASP 492 ? B ASP 491 
176 1 Y 1 B GLY 493 ? B GLY 492 
177 1 Y 1 B CYS 494 ? B CYS 493 
178 1 Y 1 B LEU 495 ? B LEU 494 
179 1 Y 1 B ASP 496 ? B ASP 495 
180 1 Y 1 B ASP 497 ? B ASP 496 
181 1 Y 1 B LEU 498 ? B LEU 497 
182 1 Y 1 B CYS 499 ? B CYS 498 
183 1 Y 1 B SER 500 ? B SER 499 
184 1 Y 1 B ARG 501 ? B ARG 500 
185 1 Y 1 B LYS 502 ? B LYS 501 
186 1 Y 1 B VAL 503 ? B VAL 502 
187 1 Y 1 B SER 504 ? B SER 503 
188 1 Y 1 B ARG 505 ? B ARG 504 
189 1 Y 1 B LYS 506 ? B LYS 505 
190 1 Y 1 B SER 507 ? B SER 506 
191 1 Y 1 B SER 508 ? B SER 507 
192 1 Y 1 B SER 509 ? B SER 508 
193 1 Y 1 B SER 510 ? B SER 509 
194 1 Y 1 B ARG 511 ? B ARG 510 
195 1 Y 1 B THR 512 ? B THR 511 
196 1 Y 1 B PRO 513 ? B PRO 512 
197 1 Y 1 B LEU 514 ? B LEU 513 
198 1 Y 1 B THR 515 ? B THR 514 
199 1 Y 1 B HIS 516 ? B HIS 515 
200 1 Y 1 B ALA 517 ? B ALA 516 
201 1 Y 1 B LEU 518 ? B LEU 517 
202 1 Y 1 B PRO 519 ? B PRO 518 
203 1 Y 1 B GLY 520 ? B GLY 519 
204 1 Y 1 B LEU 521 ? B LEU 520 
205 1 Y 1 B SER 522 ? B SER 521 
206 1 Y 1 B GLU 523 ? B GLU 522 
207 1 Y 1 B GLN 524 ? B GLN 523 
208 1 Y 1 B GLU 525 ? B GLU 524 
209 1 Y 1 B GLY 526 ? B GLY 525 
210 1 Y 1 B GLN 527 ? B GLN 526 
211 1 Y 1 C ALA 2   ? C ALA 1   
212 1 Y 1 C PRO 3   ? C PRO 2   
213 1 Y 1 C GLN 4   ? C GLN 3   
214 1 Y 1 C LEU 5   ? C LEU 4   
215 1 Y 1 C HIS 6   ? C HIS 5   
216 1 Y 1 C HIS 7   ? C HIS 6   
217 1 Y 1 C HIS 8   ? C HIS 7   
218 1 Y 1 C HIS 9   ? C HIS 8   
219 1 Y 1 C HIS 10  ? C HIS 9   
220 1 Y 1 C HIS 11  ? C HIS 10  
221 1 Y 1 C ASP 12  ? C ASP 11  
222 1 Y 1 C LEU 13  ? C LEU 12  
223 1 Y 1 C TYR 14  ? C TYR 13  
224 1 Y 1 C GLU 15  ? C GLU 14  
225 1 Y 1 C ASN 16  ? C ASN 15  
226 1 Y 1 C LEU 17  ? C LEU 16  
227 1 Y 1 C TYR 18  ? C TYR 17  
228 1 Y 1 C PHE 19  ? C PHE 18  
229 1 Y 1 C GLN 20  ? C GLN 19  
230 1 Y 1 C GLY 21  ? C GLY 20  
231 1 Y 1 C LYS 22  ? C LYS 21  
232 1 Y 1 C LEU 23  ? C LEU 22  
233 1 Y 1 C ASP 24  ? C ASP 23  
234 1 Y 1 C PRO 25  ? C PRO 24  
235 1 Y 1 C ALA 26  ? C ALA 25  
236 1 Y 1 C SER 27  ? C SER 26  
237 1 Y 1 C LYS 28  ? C LYS 27  
238 1 Y 1 C ASP 186 ? C ASP 185 
239 1 Y 1 C ASP 187 ? C ASP 186 
240 1 Y 1 C TYR 188 ? C TYR 187 
241 1 Y 1 C LEU 189 ? C LEU 188 
242 1 Y 1 C ASP 190 ? C ASP 189 
243 1 Y 1 C CYS 191 ? C CYS 190 
244 1 Y 1 C LEU 192 ? C LEU 191 
245 1 Y 1 C GLY 193 ? C GLY 192 
246 1 Y 1 C LYS 194 ? C LYS 193 
247 1 Y 1 C GLN 195 ? C GLN 194 
248 1 Y 1 C ALA 196 ? C ALA 195 
249 1 Y 1 C GLU 197 ? C GLU 196 
250 1 Y 1 C ILE 340 ? C ILE 339 
251 1 Y 1 C GLN 341 ? C GLN 340 
252 1 Y 1 C GLY 342 ? C GLY 341 
253 1 Y 1 C CYS 343 ? C CYS 342 
254 1 Y 1 C GLY 344 ? C GLY 343 
255 1 Y 1 C ASN 345 ? C ASN 344 
256 1 Y 1 C PRO 346 ? C PRO 345 
257 1 Y 1 C LYS 347 ? C LYS 346 
258 1 Y 1 C VAL 348 ? C VAL 347 
259 1 Y 1 C ASN 349 ? C ASN 348 
260 1 Y 1 C PRO 350 ? C PRO 349 
261 1 Y 1 C GLN 351 ? C GLN 350 
262 1 Y 1 C GLY 352 ? C GLY 351 
263 1 Y 1 C PRO 353 ? C PRO 352 
264 1 Y 1 C GLY 354 ? C GLY 353 
265 1 Y 1 C PRO 355 ? C PRO 354 
266 1 Y 1 C GLU 356 ? C GLU 355 
267 1 Y 1 C GLU 357 ? C GLU 356 
268 1 Y 1 C LYS 358 ? C LYS 357 
269 1 Y 1 C ARG 359 ? C ARG 358 
270 1 Y 1 C ARG 360 ? C ARG 359 
271 1 Y 1 C ARG 361 ? C ARG 360 
272 1 Y 1 C GLY 362 ? C GLY 361 
273 1 Y 1 C LYS 363 ? C LYS 362 
274 1 Y 1 C LEU 364 ? C LEU 363 
275 1 Y 1 C ALA 365 ? C ALA 364 
276 1 Y 1 C PRO 366 ? C PRO 365 
277 1 Y 1 C LEU 407 ? C LEU 406 
278 1 Y 1 C SER 408 ? C SER 407 
279 1 Y 1 C THR 409 ? C THR 408 
280 1 Y 1 C ALA 410 ? C ALA 409 
281 1 Y 1 C SER 411 ? C SER 410 
282 1 Y 1 C ASP 412 ? C ASP 411 
283 1 Y 1 C ASP 413 ? C ASP 412 
284 1 Y 1 C ASP 475 ? C ASP 474 
285 1 Y 1 C VAL 476 ? C VAL 475 
286 1 Y 1 C ASP 477 ? C ASP 476 
287 1 Y 1 C PHE 478 ? C PHE 477 
288 1 Y 1 C GLN 479 ? C GLN 478 
289 1 Y 1 C ASP 480 ? C ASP 479 
290 1 Y 1 C ALA 481 ? C ALA 480 
291 1 Y 1 C SER 482 ? C SER 481 
292 1 Y 1 C ASP 483 ? C ASP 482 
293 1 Y 1 C ASP 484 ? C ASP 483 
294 1 Y 1 C GLY 485 ? C GLY 484 
295 1 Y 1 C ALA 486 ? C ALA 485 
296 1 Y 1 C GLY 487 ? C GLY 486 
297 1 Y 1 C ALA 488 ? C ALA 487 
298 1 Y 1 C GLY 489 ? C GLY 488 
299 1 Y 1 C ALA 490 ? C ALA 489 
300 1 Y 1 C GLY 491 ? C GLY 490 
301 1 Y 1 C ASP 492 ? C ASP 491 
302 1 Y 1 C GLY 493 ? C GLY 492 
303 1 Y 1 C CYS 494 ? C CYS 493 
304 1 Y 1 C LEU 495 ? C LEU 494 
305 1 Y 1 C ASP 496 ? C ASP 495 
306 1 Y 1 C ASP 497 ? C ASP 496 
307 1 Y 1 C LEU 498 ? C LEU 497 
308 1 Y 1 C CYS 499 ? C CYS 498 
309 1 Y 1 C SER 500 ? C SER 499 
310 1 Y 1 C ARG 501 ? C ARG 500 
311 1 Y 1 C LYS 502 ? C LYS 501 
312 1 Y 1 C VAL 503 ? C VAL 502 
313 1 Y 1 C SER 504 ? C SER 503 
314 1 Y 1 C ARG 505 ? C ARG 504 
315 1 Y 1 C LYS 506 ? C LYS 505 
316 1 Y 1 C SER 507 ? C SER 506 
317 1 Y 1 C SER 508 ? C SER 507 
318 1 Y 1 C SER 509 ? C SER 508 
319 1 Y 1 C SER 510 ? C SER 509 
320 1 Y 1 C ARG 511 ? C ARG 510 
321 1 Y 1 C THR 512 ? C THR 511 
322 1 Y 1 C PRO 513 ? C PRO 512 
323 1 Y 1 C LEU 514 ? C LEU 513 
324 1 Y 1 C THR 515 ? C THR 514 
325 1 Y 1 C HIS 516 ? C HIS 515 
326 1 Y 1 C ALA 517 ? C ALA 516 
327 1 Y 1 C LEU 518 ? C LEU 517 
328 1 Y 1 C PRO 519 ? C PRO 518 
329 1 Y 1 C GLY 520 ? C GLY 519 
330 1 Y 1 C LEU 521 ? C LEU 520 
331 1 Y 1 C SER 522 ? C SER 521 
332 1 Y 1 C GLU 523 ? C GLU 522 
333 1 Y 1 C GLN 524 ? C GLN 523 
334 1 Y 1 C GLU 525 ? C GLU 524 
335 1 Y 1 C GLY 526 ? C GLY 525 
336 1 Y 1 C GLN 527 ? C GLN 526 
337 1 Y 1 D ALA 2   ? D ALA 1   
338 1 Y 1 D PRO 3   ? D PRO 2   
339 1 Y 1 D GLN 4   ? D GLN 3   
340 1 Y 1 D LEU 5   ? D LEU 4   
341 1 Y 1 D HIS 6   ? D HIS 5   
342 1 Y 1 D HIS 7   ? D HIS 6   
343 1 Y 1 D HIS 8   ? D HIS 7   
344 1 Y 1 D HIS 9   ? D HIS 8   
345 1 Y 1 D HIS 10  ? D HIS 9   
346 1 Y 1 D HIS 11  ? D HIS 10  
347 1 Y 1 D ASP 12  ? D ASP 11  
348 1 Y 1 D LEU 13  ? D LEU 12  
349 1 Y 1 D TYR 14  ? D TYR 13  
350 1 Y 1 D GLU 15  ? D GLU 14  
351 1 Y 1 D ASN 16  ? D ASN 15  
352 1 Y 1 D LEU 17  ? D LEU 16  
353 1 Y 1 D TYR 18  ? D TYR 17  
354 1 Y 1 D PHE 19  ? D PHE 18  
355 1 Y 1 D GLN 20  ? D GLN 19  
356 1 Y 1 D GLY 21  ? D GLY 20  
357 1 Y 1 D LYS 22  ? D LYS 21  
358 1 Y 1 D LEU 23  ? D LEU 22  
359 1 Y 1 D ASP 24  ? D ASP 23  
360 1 Y 1 D PRO 25  ? D PRO 24  
361 1 Y 1 D ALA 26  ? D ALA 25  
362 1 Y 1 D SER 27  ? D SER 26  
363 1 Y 1 D LYS 28  ? D LYS 27  
364 1 Y 1 D PRO 350 ? D PRO 349 
365 1 Y 1 D GLN 351 ? D GLN 350 
366 1 Y 1 D GLY 352 ? D GLY 351 
367 1 Y 1 D PRO 353 ? D PRO 352 
368 1 Y 1 D GLY 354 ? D GLY 353 
369 1 Y 1 D PRO 355 ? D PRO 354 
370 1 Y 1 D GLU 356 ? D GLU 355 
371 1 Y 1 D GLU 357 ? D GLU 356 
372 1 Y 1 D LYS 358 ? D LYS 357 
373 1 Y 1 D ARG 359 ? D ARG 358 
374 1 Y 1 D ARG 360 ? D ARG 359 
375 1 Y 1 D LEU 407 ? D LEU 406 
376 1 Y 1 D SER 408 ? D SER 407 
377 1 Y 1 D THR 409 ? D THR 408 
378 1 Y 1 D ALA 410 ? D ALA 409 
379 1 Y 1 D SER 411 ? D SER 410 
380 1 Y 1 D ASP 412 ? D ASP 411 
381 1 Y 1 D ASP 475 ? D ASP 474 
382 1 Y 1 D VAL 476 ? D VAL 475 
383 1 Y 1 D ASP 477 ? D ASP 476 
384 1 Y 1 D PHE 478 ? D PHE 477 
385 1 Y 1 D GLN 479 ? D GLN 478 
386 1 Y 1 D ASP 480 ? D ASP 479 
387 1 Y 1 D ALA 481 ? D ALA 480 
388 1 Y 1 D SER 482 ? D SER 481 
389 1 Y 1 D ASP 483 ? D ASP 482 
390 1 Y 1 D ASP 484 ? D ASP 483 
391 1 Y 1 D GLY 485 ? D GLY 484 
392 1 Y 1 D ALA 486 ? D ALA 485 
393 1 Y 1 D GLY 487 ? D GLY 486 
394 1 Y 1 D ALA 488 ? D ALA 487 
395 1 Y 1 D GLY 489 ? D GLY 488 
396 1 Y 1 D ALA 490 ? D ALA 489 
397 1 Y 1 D GLY 491 ? D GLY 490 
398 1 Y 1 D ASP 492 ? D ASP 491 
399 1 Y 1 D GLY 493 ? D GLY 492 
400 1 Y 1 D CYS 494 ? D CYS 493 
401 1 Y 1 D LEU 495 ? D LEU 494 
402 1 Y 1 D ASP 496 ? D ASP 495 
403 1 Y 1 D ASP 497 ? D ASP 496 
404 1 Y 1 D LEU 498 ? D LEU 497 
405 1 Y 1 D CYS 499 ? D CYS 498 
406 1 Y 1 D SER 500 ? D SER 499 
407 1 Y 1 D ARG 501 ? D ARG 500 
408 1 Y 1 D LYS 502 ? D LYS 501 
409 1 Y 1 D VAL 503 ? D VAL 502 
410 1 Y 1 D SER 504 ? D SER 503 
411 1 Y 1 D ARG 505 ? D ARG 504 
412 1 Y 1 D LYS 506 ? D LYS 505 
413 1 Y 1 D SER 507 ? D SER 506 
414 1 Y 1 D SER 508 ? D SER 507 
415 1 Y 1 D SER 509 ? D SER 508 
416 1 Y 1 D SER 510 ? D SER 509 
417 1 Y 1 D ARG 511 ? D ARG 510 
418 1 Y 1 D THR 512 ? D THR 511 
419 1 Y 1 D PRO 513 ? D PRO 512 
420 1 Y 1 D LEU 514 ? D LEU 513 
421 1 Y 1 D THR 515 ? D THR 514 
422 1 Y 1 D HIS 516 ? D HIS 515 
423 1 Y 1 D ALA 517 ? D ALA 516 
424 1 Y 1 D LEU 518 ? D LEU 517 
425 1 Y 1 D PRO 519 ? D PRO 518 
426 1 Y 1 D GLY 520 ? D GLY 519 
427 1 Y 1 D LEU 521 ? D LEU 520 
428 1 Y 1 D SER 522 ? D SER 521 
429 1 Y 1 D GLU 523 ? D GLU 522 
430 1 Y 1 D GLN 524 ? D GLN 523 
431 1 Y 1 D GLU 525 ? D GLU 524 
432 1 Y 1 D GLY 526 ? D GLY 525 
433 1 Y 1 D GLN 527 ? D GLN 526 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'CALCIUM ION'          CA  
4 water                  HOH 
# 
