data_9GV8
# 
_entry.id   9GV8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GV8         pdb_00009gv8 10.2210/pdb9gv8/pdb 
WWPDB D_1292141932 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GV8 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sergio@ugr.es 
_pdbx_contact_author.name_first         Sergio 
_pdbx_contact_author.name_last          Martinez-Rodriguez 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6675-1550 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gavira, J.A.'           1 0000-0002-7386-6484 
'Martinez-Rodriguez, S.' 2 0000-0001-6675-1550 
# 
_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                        primary 
_citation.journal_abbrev            'Microb Biotechnol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1751-7915 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            18 
_citation.language                  ? 
_citation.page_first                e70179 
_citation.page_last                 e70179 
_citation.title                     'Revisiting D-Acylases for D-Amino Acid Production.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/1751-7915.70179 
_citation.pdbx_database_id_PubMed   40491232 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Martinez-Rodriguez, S.' 1 0000-0001-6675-1550 
primary 'Gavira, J.A.'           2 0000-0002-7386-6484 
# 
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 'Amidohydrolase family protein' 53568.617 1  3.5.1.-,3.5.1.81 ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                  62.068    4  ?                ? ? ? 
3 non-polymer syn 'SULFATE ION'                   96.063    4  ?                ? ? ? 
4 non-polymer syn 'NICKEL (II) ION'               58.693    2  ?                ? ? ? 
5 water       nat water                           18.015    66 ?                ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        D-aminoacylase 
# 
_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       
;MKVDWLFKNVTVIDGSGGPQYRADVAVKGDRIMAIAPALDVAAEQVIDGQGRVLAPGFIDVHTHDDINVIRMPEYLPKLS
QGVTTVIVGNCGISAATATMRGEVPDPMNLLGEQQHFIYPTVEAYAHAVEAARPSLNVGTLIGHTALRNNHMDDLFRPAN
ETEIAGMRVQLRDALRQGALGLSTGLAYASAFQSTTEEVMALAEELAAGKGVYTTHLRSEFEPILEALDEAFRIGRHGNV
PVVVSHHKCAGAKNWGRTKETLAFFDEMRQQQDIACDCYPYSASSSTLDMKQVTDEFDIVITWSEAQPEQAGKTLQQIAD
EWQVSLHDAAARLMPAGAIYHNMDEQDVRRVMRYPVTMIGSDGLPNDPMPHPRLWGAFPRVLGHYSRDEQLFPLTTAVHK
MTGLSAARFQLADRGLVKIGYFADLVLFDPQTVRDVASFSDPKRPADGIEAVMVNGVMSYGSDKKITGRAGRFLRRRMDH
HHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKVDWLFKNVTVIDGSGGPQYRADVAVKGDRIMAIAPALDVAAEQVIDGQGRVLAPGFIDVHTHDDINVIRMPEYLPKLS
QGVTTVIVGNCGISAATATMRGEVPDPMNLLGEQQHFIYPTVEAYAHAVEAARPSLNVGTLIGHTALRNNHMDDLFRPAN
ETEIAGMRVQLRDALRQGALGLSTGLAYASAFQSTTEEVMALAEELAAGKGVYTTHLRSEFEPILEALDEAFRIGRHGNV
PVVVSHHKCAGAKNWGRTKETLAFFDEMRQQQDIACDCYPYSASSSTLDMKQVTDEFDIVITWSEAQPEQAGKTLQQIAD
EWQVSLHDAAARLMPAGAIYHNMDEQDVRRVMRYPVTMIGSDGLPNDPMPHPRLWGAFPRVLGHYSRDEQLFPLTTAVHK
MTGLSAARFQLADRGLVKIGYFADLVLFDPQTVRDVASFSDPKRPADGIEAVMVNGVMSYGSDKKITGRAGRFLRRRMDH
HHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL    EDO 
3 'SULFATE ION'     SO4 
4 'NICKEL (II) ION' NI  
5 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   VAL n 
1 4   ASP n 
1 5   TRP n 
1 6   LEU n 
1 7   PHE n 
1 8   LYS n 
1 9   ASN n 
1 10  VAL n 
1 11  THR n 
1 12  VAL n 
1 13  ILE n 
1 14  ASP n 
1 15  GLY n 
1 16  SER n 
1 17  GLY n 
1 18  GLY n 
1 19  PRO n 
1 20  GLN n 
1 21  TYR n 
1 22  ARG n 
1 23  ALA n 
1 24  ASP n 
1 25  VAL n 
1 26  ALA n 
1 27  VAL n 
1 28  LYS n 
1 29  GLY n 
1 30  ASP n 
1 31  ARG n 
1 32  ILE n 
1 33  MET n 
1 34  ALA n 
1 35  ILE n 
1 36  ALA n 
1 37  PRO n 
1 38  ALA n 
1 39  LEU n 
1 40  ASP n 
1 41  VAL n 
1 42  ALA n 
1 43  ALA n 
1 44  GLU n 
1 45  GLN n 
1 46  VAL n 
1 47  ILE n 
1 48  ASP n 
1 49  GLY n 
1 50  GLN n 
1 51  GLY n 
1 52  ARG n 
1 53  VAL n 
1 54  LEU n 
1 55  ALA n 
1 56  PRO n 
1 57  GLY n 
1 58  PHE n 
1 59  ILE n 
1 60  ASP n 
1 61  VAL n 
1 62  HIS n 
1 63  THR n 
1 64  HIS n 
1 65  ASP n 
1 66  ASP n 
1 67  ILE n 
1 68  ASN n 
1 69  VAL n 
1 70  ILE n 
1 71  ARG n 
1 72  MET n 
1 73  PRO n 
1 74  GLU n 
1 75  TYR n 
1 76  LEU n 
1 77  PRO n 
1 78  LYS n 
1 79  LEU n 
1 80  SER n 
1 81  GLN n 
1 82  GLY n 
1 83  VAL n 
1 84  THR n 
1 85  THR n 
1 86  VAL n 
1 87  ILE n 
1 88  VAL n 
1 89  GLY n 
1 90  ASN n 
1 91  CYS n 
1 92  GLY n 
1 93  ILE n 
1 94  SER n 
1 95  ALA n 
1 96  ALA n 
1 97  THR n 
1 98  ALA n 
1 99  THR n 
1 100 MET n 
1 101 ARG n 
1 102 GLY n 
1 103 GLU n 
1 104 VAL n 
1 105 PRO n 
1 106 ASP n 
1 107 PRO n 
1 108 MET n 
1 109 ASN n 
1 110 LEU n 
1 111 LEU n 
1 112 GLY n 
1 113 GLU n 
1 114 GLN n 
1 115 GLN n 
1 116 HIS n 
1 117 PHE n 
1 118 ILE n 
1 119 TYR n 
1 120 PRO n 
1 121 THR n 
1 122 VAL n 
1 123 GLU n 
1 124 ALA n 
1 125 TYR n 
1 126 ALA n 
1 127 HIS n 
1 128 ALA n 
1 129 VAL n 
1 130 GLU n 
1 131 ALA n 
1 132 ALA n 
1 133 ARG n 
1 134 PRO n 
1 135 SER n 
1 136 LEU n 
1 137 ASN n 
1 138 VAL n 
1 139 GLY n 
1 140 THR n 
1 141 LEU n 
1 142 ILE n 
1 143 GLY n 
1 144 HIS n 
1 145 THR n 
1 146 ALA n 
1 147 LEU n 
1 148 ARG n 
1 149 ASN n 
1 150 ASN n 
1 151 HIS n 
1 152 MET n 
1 153 ASP n 
1 154 ASP n 
1 155 LEU n 
1 156 PHE n 
1 157 ARG n 
1 158 PRO n 
1 159 ALA n 
1 160 ASN n 
1 161 GLU n 
1 162 THR n 
1 163 GLU n 
1 164 ILE n 
1 165 ALA n 
1 166 GLY n 
1 167 MET n 
1 168 ARG n 
1 169 VAL n 
1 170 GLN n 
1 171 LEU n 
1 172 ARG n 
1 173 ASP n 
1 174 ALA n 
1 175 LEU n 
1 176 ARG n 
1 177 GLN n 
1 178 GLY n 
1 179 ALA n 
1 180 LEU n 
1 181 GLY n 
1 182 LEU n 
1 183 SER n 
1 184 THR n 
1 185 GLY n 
1 186 LEU n 
1 187 ALA n 
1 188 TYR n 
1 189 ALA n 
1 190 SER n 
1 191 ALA n 
1 192 PHE n 
1 193 GLN n 
1 194 SER n 
1 195 THR n 
1 196 THR n 
1 197 GLU n 
1 198 GLU n 
1 199 VAL n 
1 200 MET n 
1 201 ALA n 
1 202 LEU n 
1 203 ALA n 
1 204 GLU n 
1 205 GLU n 
1 206 LEU n 
1 207 ALA n 
1 208 ALA n 
1 209 GLY n 
1 210 LYS n 
1 211 GLY n 
1 212 VAL n 
1 213 TYR n 
1 214 THR n 
1 215 THR n 
1 216 HIS n 
1 217 LEU n 
1 218 ARG n 
1 219 SER n 
1 220 GLU n 
1 221 PHE n 
1 222 GLU n 
1 223 PRO n 
1 224 ILE n 
1 225 LEU n 
1 226 GLU n 
1 227 ALA n 
1 228 LEU n 
1 229 ASP n 
1 230 GLU n 
1 231 ALA n 
1 232 PHE n 
1 233 ARG n 
1 234 ILE n 
1 235 GLY n 
1 236 ARG n 
1 237 HIS n 
1 238 GLY n 
1 239 ASN n 
1 240 VAL n 
1 241 PRO n 
1 242 VAL n 
1 243 VAL n 
1 244 VAL n 
1 245 SER n 
1 246 HIS n 
1 247 HIS n 
1 248 LYS n 
1 249 CYS n 
1 250 ALA n 
1 251 GLY n 
1 252 ALA n 
1 253 LYS n 
1 254 ASN n 
1 255 TRP n 
1 256 GLY n 
1 257 ARG n 
1 258 THR n 
1 259 LYS n 
1 260 GLU n 
1 261 THR n 
1 262 LEU n 
1 263 ALA n 
1 264 PHE n 
1 265 PHE n 
1 266 ASP n 
1 267 GLU n 
1 268 MET n 
1 269 ARG n 
1 270 GLN n 
1 271 GLN n 
1 272 GLN n 
1 273 ASP n 
1 274 ILE n 
1 275 ALA n 
1 276 CYS n 
1 277 ASP n 
1 278 CYS n 
1 279 TYR n 
1 280 PRO n 
1 281 TYR n 
1 282 SER n 
1 283 ALA n 
1 284 SER n 
1 285 SER n 
1 286 SER n 
1 287 THR n 
1 288 LEU n 
1 289 ASP n 
1 290 MET n 
1 291 LYS n 
1 292 GLN n 
1 293 VAL n 
1 294 THR n 
1 295 ASP n 
1 296 GLU n 
1 297 PHE n 
1 298 ASP n 
1 299 ILE n 
1 300 VAL n 
1 301 ILE n 
1 302 THR n 
1 303 TRP n 
1 304 SER n 
1 305 GLU n 
1 306 ALA n 
1 307 GLN n 
1 308 PRO n 
1 309 GLU n 
1 310 GLN n 
1 311 ALA n 
1 312 GLY n 
1 313 LYS n 
1 314 THR n 
1 315 LEU n 
1 316 GLN n 
1 317 GLN n 
1 318 ILE n 
1 319 ALA n 
1 320 ASP n 
1 321 GLU n 
1 322 TRP n 
1 323 GLN n 
1 324 VAL n 
1 325 SER n 
1 326 LEU n 
1 327 HIS n 
1 328 ASP n 
1 329 ALA n 
1 330 ALA n 
1 331 ALA n 
1 332 ARG n 
1 333 LEU n 
1 334 MET n 
1 335 PRO n 
1 336 ALA n 
1 337 GLY n 
1 338 ALA n 
1 339 ILE n 
1 340 TYR n 
1 341 HIS n 
1 342 ASN n 
1 343 MET n 
1 344 ASP n 
1 345 GLU n 
1 346 GLN n 
1 347 ASP n 
1 348 VAL n 
1 349 ARG n 
1 350 ARG n 
1 351 VAL n 
1 352 MET n 
1 353 ARG n 
1 354 TYR n 
1 355 PRO n 
1 356 VAL n 
1 357 THR n 
1 358 MET n 
1 359 ILE n 
1 360 GLY n 
1 361 SER n 
1 362 ASP n 
1 363 GLY n 
1 364 LEU n 
1 365 PRO n 
1 366 ASN n 
1 367 ASP n 
1 368 PRO n 
1 369 MET n 
1 370 PRO n 
1 371 HIS n 
1 372 PRO n 
1 373 ARG n 
1 374 LEU n 
1 375 TRP n 
1 376 GLY n 
1 377 ALA n 
1 378 PHE n 
1 379 PRO n 
1 380 ARG n 
1 381 VAL n 
1 382 LEU n 
1 383 GLY n 
1 384 HIS n 
1 385 TYR n 
1 386 SER n 
1 387 ARG n 
1 388 ASP n 
1 389 GLU n 
1 390 GLN n 
1 391 LEU n 
1 392 PHE n 
1 393 PRO n 
1 394 LEU n 
1 395 THR n 
1 396 THR n 
1 397 ALA n 
1 398 VAL n 
1 399 HIS n 
1 400 LYS n 
1 401 MET n 
1 402 THR n 
1 403 GLY n 
1 404 LEU n 
1 405 SER n 
1 406 ALA n 
1 407 ALA n 
1 408 ARG n 
1 409 PHE n 
1 410 GLN n 
1 411 LEU n 
1 412 ALA n 
1 413 ASP n 
1 414 ARG n 
1 415 GLY n 
1 416 LEU n 
1 417 VAL n 
1 418 LYS n 
1 419 ILE n 
1 420 GLY n 
1 421 TYR n 
1 422 PHE n 
1 423 ALA n 
1 424 ASP n 
1 425 LEU n 
1 426 VAL n 
1 427 LEU n 
1 428 PHE n 
1 429 ASP n 
1 430 PRO n 
1 431 GLN n 
1 432 THR n 
1 433 VAL n 
1 434 ARG n 
1 435 ASP n 
1 436 VAL n 
1 437 ALA n 
1 438 SER n 
1 439 PHE n 
1 440 SER n 
1 441 ASP n 
1 442 PRO n 
1 443 LYS n 
1 444 ARG n 
1 445 PRO n 
1 446 ALA n 
1 447 ASP n 
1 448 GLY n 
1 449 ILE n 
1 450 GLU n 
1 451 ALA n 
1 452 VAL n 
1 453 MET n 
1 454 VAL n 
1 455 ASN n 
1 456 GLY n 
1 457 VAL n 
1 458 MET n 
1 459 SER n 
1 460 TYR n 
1 461 GLY n 
1 462 SER n 
1 463 ASP n 
1 464 LYS n 
1 465 LYS n 
1 466 ILE n 
1 467 THR n 
1 468 GLY n 
1 469 ARG n 
1 470 ALA n 
1 471 GLY n 
1 472 ARG n 
1 473 PHE n 
1 474 LEU n 
1 475 ARG n 
1 476 ARG n 
1 477 ARG n 
1 478 MET n 
1 479 ASP n 
1 480 HIS n 
1 481 HIS n 
1 482 HIS n 
1 483 HIS n 
1 484 HIS n 
1 485 HIS 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                   485 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;dan, B5L96_17380, B6I68_16395, BANRA_04485, BL124_00028775, DW281_07100, EAO17_17410, FXN67_23300, G4V31_23420, GJJ08_023370, GJJ13_021835, GJJ18_03715, GNF00_21165, NCTC11679_04932, NCTC13443_01470, NCTC5052_02702, NCTC9601_05682, NCTC9661_05441, QIG75_04865, SAMEA3499874_02915, SAMEA3499901_00964, SAMEA3512100_03687, SAMEA3515122_03158, SAMEA3538658_01149, SAMEA3538828_01003, SAMEA3673026_03520, SAMEA3720909_04521, SAMEA4364603_03367, SAMEA4873597_03320, SAMEA4873632_03948, VKR_04363
;
_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      'Klebsiella pneumoniae subsp. pneumoniae Kp13' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1123862 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE          ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL    'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
NI  non-polymer         . 'NICKEL (II) ION' ?                 'Ni 2'           58.693  
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 
SO4 non-polymer         . 'SULFATE ION'     ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE         ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE          ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE            ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ASN 9   9   9   ASN ASN A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  MET 33  33  33  MET MET A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  MET 72  72  72  MET MET A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 MET 108 108 108 MET MET A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 MET 167 167 167 MET MET A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 ARG 176 176 176 ARG ARG A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 PHE 192 192 192 PHE PHE A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 MET 200 200 200 MET MET A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ARG 218 218 218 ARG ARG A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 PHE 221 221 221 PHE PHE A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ARG 236 236 236 ARG ARG A . n 
A 1 237 HIS 237 237 237 HIS HIS A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 CYS 249 249 249 CYS CYS A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 TRP 255 255 255 TRP TRP A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 THR 261 261 261 THR THR A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 PHE 264 264 264 PHE PHE A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 CYS 276 276 276 CYS CYS A . n 
A 1 277 ASP 277 277 277 ASP ASP A . n 
A 1 278 CYS 278 278 278 CYS CYS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 MET 290 290 290 MET MET A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 GLN 292 292 292 GLN GLN A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 GLU 305 305 305 GLU GLU A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 GLN 307 307 307 GLN GLN A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 GLY 312 312 312 GLY GLY A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 GLN 316 316 316 GLN GLN A . n 
A 1 317 GLN 317 317 317 GLN GLN A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 TRP 322 322 322 TRP TRP A . n 
A 1 323 GLN 323 323 323 GLN GLN A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 HIS 327 327 327 HIS HIS A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 ARG 332 332 332 ARG ARG A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 MET 334 334 334 MET MET A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 TYR 340 340 340 TYR TYR A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 ASP 344 344 344 ASP ASP A . n 
A 1 345 GLU 345 345 345 GLU GLU A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 ARG 349 349 349 ARG ARG A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 MET 352 352 352 MET MET A . n 
A 1 353 ARG 353 353 353 ARG ARG A . n 
A 1 354 TYR 354 354 354 TYR TYR A . n 
A 1 355 PRO 355 355 355 PRO PRO A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 MET 358 358 358 MET MET A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 LEU 364 364 364 LEU LEU A . n 
A 1 365 PRO 365 365 365 PRO PRO A . n 
A 1 366 ASN 366 366 366 ASN ASN A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 PRO 368 368 368 PRO PRO A . n 
A 1 369 MET 369 369 369 MET MET A . n 
A 1 370 PRO 370 370 370 PRO PRO A . n 
A 1 371 HIS 371 371 371 HIS HIS A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 ARG 373 373 373 ARG ARG A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 TRP 375 375 375 TRP TRP A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 GLY 383 383 383 GLY GLY A . n 
A 1 384 HIS 384 384 384 HIS HIS A . n 
A 1 385 TYR 385 385 385 TYR TYR A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 ARG 387 387 387 ARG ARG A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 THR 396 396 396 THR THR A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 HIS 399 399 399 HIS HIS A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 MET 401 401 401 MET MET A . n 
A 1 402 THR 402 402 402 THR THR A . n 
A 1 403 GLY 403 403 403 GLY GLY A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 ARG 408 408 408 ARG ARG A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 GLN 410 410 410 GLN GLN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 GLY 415 415 415 GLY GLY A . n 
A 1 416 LEU 416 416 416 LEU LEU A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 ILE 419 419 419 ILE ILE A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 TYR 421 421 421 TYR TYR A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 PHE 428 428 428 PHE PHE A . n 
A 1 429 ASP 429 429 429 ASP ASP A . n 
A 1 430 PRO 430 430 430 PRO PRO A . n 
A 1 431 GLN 431 431 431 GLN GLN A . n 
A 1 432 THR 432 432 432 THR THR A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 ASP 435 435 435 ASP ASP A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 SER 438 438 438 SER SER A . n 
A 1 439 PHE 439 439 439 PHE PHE A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 ASP 441 441 441 ASP ASP A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ARG 444 444 444 ARG ARG A . n 
A 1 445 PRO 445 445 445 PRO PRO A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 ASP 447 447 447 ASP ASP A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 ALA 451 451 451 ALA ALA A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 MET 453 453 453 MET MET A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 GLY 456 456 456 GLY GLY A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 TYR 460 460 460 TYR TYR A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 ASP 463 463 463 ASP ASP A . n 
A 1 464 LYS 464 464 464 LYS LYS A . n 
A 1 465 LYS 465 465 465 LYS LYS A . n 
A 1 466 ILE 466 466 466 ILE ILE A . n 
A 1 467 THR 467 467 467 THR THR A . n 
A 1 468 GLY 468 468 468 GLY GLY A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 GLY 471 471 471 GLY GLY A . n 
A 1 472 ARG 472 472 472 ARG ARG A . n 
A 1 473 PHE 473 473 473 PHE PHE A . n 
A 1 474 LEU 474 474 474 LEU LEU A . n 
A 1 475 ARG 475 475 475 ARG ARG A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 ARG 477 477 477 ARG ARG A . n 
A 1 478 MET 478 478 478 MET MET A . n 
A 1 479 ASP 479 479 ?   ?   ?   A . n 
A 1 480 HIS 480 480 ?   ?   ?   A . n 
A 1 481 HIS 481 481 ?   ?   ?   A . n 
A 1 482 HIS 482 482 ?   ?   ?   A . n 
A 1 483 HIS 483 483 ?   ?   ?   A . n 
A 1 484 HIS 484 484 ?   ?   ?   A . n 
A 1 485 HIS 485 485 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NI  ? ? NI  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SO4 ? ? SO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EDO 1  501 501 EDO EDO A . 
C 2 EDO 1  502 502 EDO EDO A . 
D 2 EDO 1  503 503 EDO EDO A . 
E 2 EDO 1  504 505 EDO EDO A . 
F 3 SO4 1  505 1   SO4 SO4 A . 
G 3 SO4 1  506 2   SO4 SO4 A . 
H 3 SO4 1  507 3   SO4 SO4 A . 
I 3 SO4 1  508 4   SO4 SO4 A . 
J 4 NI  1  509 1   NI  NI  A . 
K 4 NI  1  510 2   NI  NI  A . 
L 5 HOH 1  601 17  HOH HOH A . 
L 5 HOH 2  602 61  HOH HOH A . 
L 5 HOH 3  603 2   HOH HOH A . 
L 5 HOH 4  604 14  HOH HOH A . 
L 5 HOH 5  605 31  HOH HOH A . 
L 5 HOH 6  606 12  HOH HOH A . 
L 5 HOH 7  607 56  HOH HOH A . 
L 5 HOH 8  608 5   HOH HOH A . 
L 5 HOH 9  609 3   HOH HOH A . 
L 5 HOH 10 610 44  HOH HOH A . 
L 5 HOH 11 611 50  HOH HOH A . 
L 5 HOH 12 612 10  HOH HOH A . 
L 5 HOH 13 613 41  HOH HOH A . 
L 5 HOH 14 614 36  HOH HOH A . 
L 5 HOH 15 615 9   HOH HOH A . 
L 5 HOH 16 616 16  HOH HOH A . 
L 5 HOH 17 617 29  HOH HOH A . 
L 5 HOH 18 618 1   HOH HOH A . 
L 5 HOH 19 619 21  HOH HOH A . 
L 5 HOH 20 620 13  HOH HOH A . 
L 5 HOH 21 621 20  HOH HOH A . 
L 5 HOH 22 622 22  HOH HOH A . 
L 5 HOH 23 623 42  HOH HOH A . 
L 5 HOH 24 624 60  HOH HOH A . 
L 5 HOH 25 625 64  HOH HOH A . 
L 5 HOH 26 626 58  HOH HOH A . 
L 5 HOH 27 627 4   HOH HOH A . 
L 5 HOH 28 628 45  HOH HOH A . 
L 5 HOH 29 629 25  HOH HOH A . 
L 5 HOH 30 630 34  HOH HOH A . 
L 5 HOH 31 631 38  HOH HOH A . 
L 5 HOH 32 632 8   HOH HOH A . 
L 5 HOH 33 633 62  HOH HOH A . 
L 5 HOH 34 634 43  HOH HOH A . 
L 5 HOH 35 635 23  HOH HOH A . 
L 5 HOH 36 636 35  HOH HOH A . 
L 5 HOH 37 637 24  HOH HOH A . 
L 5 HOH 38 638 49  HOH HOH A . 
L 5 HOH 39 639 28  HOH HOH A . 
L 5 HOH 40 640 7   HOH HOH A . 
L 5 HOH 41 641 33  HOH HOH A . 
L 5 HOH 42 642 55  HOH HOH A . 
L 5 HOH 43 643 40  HOH HOH A . 
L 5 HOH 44 644 37  HOH HOH A . 
L 5 HOH 45 645 11  HOH HOH A . 
L 5 HOH 46 646 32  HOH HOH A . 
L 5 HOH 47 647 6   HOH HOH A . 
L 5 HOH 48 648 19  HOH HOH A . 
L 5 HOH 49 649 48  HOH HOH A . 
L 5 HOH 50 650 51  HOH HOH A . 
L 5 HOH 51 651 27  HOH HOH A . 
L 5 HOH 52 652 26  HOH HOH A . 
L 5 HOH 53 653 47  HOH HOH A . 
L 5 HOH 54 654 59  HOH HOH A . 
L 5 HOH 55 655 39  HOH HOH A . 
L 5 HOH 56 656 15  HOH HOH A . 
L 5 HOH 57 657 18  HOH HOH A . 
L 5 HOH 58 658 54  HOH HOH A . 
L 5 HOH 59 659 67  HOH HOH A . 
L 5 HOH 60 660 30  HOH HOH A . 
L 5 HOH 61 661 52  HOH HOH A . 
L 5 HOH 62 662 66  HOH HOH A . 
L 5 HOH 63 663 53  HOH HOH A . 
L 5 HOH 64 664 63  HOH HOH A . 
L 5 HOH 65 665 57  HOH HOH A . 
L 5 HOH 66 666 68  HOH HOH A . 
# 
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  ? ? ? '(1.21.1_5286: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GV8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.422 
_cell.length_a_esd                 ? 
_cell.length_b                     101.422 
_cell.length_b_esd                 ? 
_cell.length_c                     124.940 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GV8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GV8 
_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             3.4 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'HRI: 0.2 M Ammonium sulfate, 0.1 M Sodium cacodylate trihydrate pH 6.5, 30% w/v Polyethylene glycol 8,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.5 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             100 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9792 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GV8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               50.91 
_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                                     23169 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.88 
_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                                0.185 
_reflns.pdbx_Rpim_I_all                                0.079 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       120947 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.167 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.60 
_reflns_shell.d_res_low                                     2.72 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2677 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.3 
_reflns_shell.pdbx_chi_squared                              0.88 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               3.117 
_reflns_shell.pdbx_Rpim_I_all                               1.446 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.460 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.739 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GV8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.60 
_refine.ls_d_res_low                             50.91 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     22989 
_refine.ls_number_reflns_R_free                  1119 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.42 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2282 
_refine.ls_R_factor_R_free                       0.2692 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2262 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.39 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.46 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        50.91 
_refine_hist.number_atoms_solvent             67 
_refine_hist.number_atoms_total               3796 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3691 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 3993 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.497  ? 5441 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.726 ? 1522 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043  ? 591  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 727  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.60 2.72  . . 127 2472 91.00  . . . . 0.4107 . . . . . . . . . . . 0.4279 
'X-RAY DIFFRACTION' 2.72 2.86  . . 127 2696 99.00  . . . . 0.3478 . . . . . . . . . . . 0.3365 
'X-RAY DIFFRACTION' 2.86 3.04  . . 144 2742 100.00 . . . . 0.3144 . . . . . . . . . . . 0.3635 
'X-RAY DIFFRACTION' 3.04 3.28  . . 144 2755 100.00 . . . . 0.2987 . . . . . . . . . . . 0.3489 
'X-RAY DIFFRACTION' 3.28 3.60  . . 169 2700 100.00 . . . . 0.2496 . . . . . . . . . . . 0.2968 
'X-RAY DIFFRACTION' 3.61 4.13  . . 157 2743 99.00  . . . . 0.2170 . . . . . . . . . . . 0.2561 
'X-RAY DIFFRACTION' 4.13 5.20  . . 94  2856 100.00 . . . . 0.1750 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 5.20 50.91 . . 157 2906 100.00 . . . . 0.1844 . . . . . . . . . . . 0.2077 
# 
_struct.entry_id                     9GV8 
_struct.title                        
'N-Acyl-D-amino-acid deacylase (D-acylase) from Klebsiella pneumoniae in the absence of glycerol' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9GV8 
_struct_keywords.text            'N-ACYL-D-AMINO-ACID DEACYLASE, D-ACYLASE, AMIDOHYDROLASE, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    W9BIW9_KLEPN 
_struct_ref.pdbx_db_accession          W9BIW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKVDWLFKNVTVIDGSGGPQYRADVAVKGDRIMAIAPALDVAAEQVIDGQGRVLAPGFIDVHTHDDINVIRMPEYLPKLS
QGVTTVIVGNCGISAATATMRGEVPDPMNLLGEQQHFIYPTVEAYAHAVEAARPSLNVGTLIGHTALRNNHMDDLFRPAN
ETEIAGMRVQLRDALRQGALGLSTGLAYASAFQSTTEEVMALAEELAAGKGVYTTHLRSEFEPILEALDEAFRIGRHGNV
PVVVSHHKCAGAKNWGRTKETLAFFDEMRQQQDIACDCYPYSASSSTLDMKQVTDEFDIVITWSEAQPEQAGKTLQQIAD
EWQVSLHDAAARLMPAGAIYHNMDEQDVRRVMRYPVTMIGSDGLPNDPMPHPRLWGAFPRVLGHYSRDEQLFPLTTAVHK
MTGLSAARFQLADRGLVKIGYFADLVLFDPQTVRDVASFSDPKRPADGIEAVMVNGVMSYGSDKKITGRAGRFLRRRMD
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GV8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 479 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             W9BIW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  479 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       479 
# 
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 9GV8 HIS A 480 ? UNP W9BIW9 ? ? 'expression tag' 480 1 
1 9GV8 HIS A 481 ? UNP W9BIW9 ? ? 'expression tag' 481 2 
1 9GV8 HIS A 482 ? UNP W9BIW9 ? ? 'expression tag' 482 3 
1 9GV8 HIS A 483 ? UNP W9BIW9 ? ? 'expression tag' 483 4 
1 9GV8 HIS A 484 ? UNP W9BIW9 ? ? 'expression tag' 484 5 
1 9GV8 HIS A 485 ? UNP W9BIW9 ? ? 'expression tag' 485 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1610  ? 
1 MORE         -71   ? 
1 'SSA (A^2)'  18200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ILE A 67  ? MET A 72  ? ILE A 67  MET A 72  1 ? 6  
HELX_P HELX_P2  AA2 TYR A 75  ? SER A 80  ? TYR A 75  SER A 80  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 107 ? LEU A 111 ? PRO A 107 LEU A 111 5 ? 5  
HELX_P HELX_P4  AA4 GLU A 113 ? PHE A 117 ? GLU A 113 PHE A 117 5 ? 5  
HELX_P HELX_P5  AA5 THR A 121 ? ARG A 133 ? THR A 121 ARG A 133 1 ? 13 
HELX_P HELX_P6  AA6 HIS A 144 ? MET A 152 ? HIS A 144 MET A 152 1 ? 9  
HELX_P HELX_P7  AA7 ASN A 160 ? GLN A 177 ? ASN A 160 GLN A 177 1 ? 18 
HELX_P HELX_P8  AA8 TYR A 188 ? GLN A 193 ? TYR A 188 GLN A 193 1 ? 6  
HELX_P HELX_P9  AA9 THR A 195 ? GLU A 204 ? THR A 195 GLU A 204 1 ? 10 
HELX_P HELX_P10 AB1 GLU A 205 ? ALA A 207 ? GLU A 205 ALA A 207 5 ? 3  
HELX_P HELX_P11 AB2 PRO A 223 ? ASN A 239 ? PRO A 223 ASN A 239 1 ? 17 
HELX_P HELX_P12 AB3 GLY A 251 ? GLY A 256 ? GLY A 251 GLY A 256 5 ? 6  
HELX_P HELX_P13 AB4 ARG A 257 ? ARG A 269 ? ARG A 257 ARG A 269 1 ? 13 
HELX_P HELX_P14 AB5 THR A 314 ? TRP A 322 ? THR A 314 TRP A 322 1 ? 9  
HELX_P HELX_P15 AB6 SER A 325 ? MET A 334 ? SER A 325 MET A 334 1 ? 10 
HELX_P HELX_P16 AB7 ASP A 344 ? TYR A 354 ? ASP A 344 TYR A 354 1 ? 11 
HELX_P HELX_P17 AB8 PRO A 372 ? HIS A 384 ? PRO A 372 HIS A 384 1 ? 13 
HELX_P HELX_P18 AB9 PRO A 393 ? LYS A 400 ? PRO A 393 LYS A 400 1 ? 8  
HELX_P HELX_P19 AC1 THR A 402 ? PHE A 409 ? THR A 402 PHE A 409 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 62  NE2 ? ? ? 1_555 J NI . NI ? ? A HIS 62  A NI 509 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc2 metalc ? ? A HIS 64  NE2 ? ? ? 1_555 J NI . NI ? ? A HIS 64  A NI 509 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc3 metalc ? ? A CYS 91  SG  ? ? ? 1_555 J NI . NI ? ? A CYS 91  A NI 509 1_555 ? ? ? ? ? ? ? 2.495 ? ? 
metalc4 metalc ? ? A CYS 91  SG  ? ? ? 1_555 K NI . NI ? ? A CYS 91  A NI 510 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc5 metalc ? ? A HIS 216 ND1 ? ? ? 1_555 K NI . NI ? ? A HIS 216 A NI 510 1_555 ? ? ? ? ? ? ? 2.121 ? ? 
metalc6 metalc ? ? A HIS 246 NE2 ? ? ? 1_555 K NI . NI ? ? A HIS 246 A NI 510 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
metalc7 metalc ? ? F SO4 .   O3  ? ? ? 1_555 J NI . NI ? ? A SO4 505 A NI 509 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc8 metalc ? ? F SO4 .   O4  ? ? ? 1_555 K NI . NI ? ? A SO4 505 A NI 510 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 62  ? A HIS 62  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 NE2 ? A HIS 64  ? A HIS 64  ? 1_555 131.3 ? 
2  NE2 ? A HIS 62  ? A HIS 62  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 SG  ? A CYS 91  ? A CYS 91  ? 1_555 90.2  ? 
3  NE2 ? A HIS 64  ? A HIS 64  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 SG  ? A CYS 91  ? A CYS 91  ? 1_555 112.5 ? 
4  NE2 ? A HIS 62  ? A HIS 62  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 O3  ? F SO4 .   ? A SO4 505 ? 1_555 125.7 ? 
5  NE2 ? A HIS 64  ? A HIS 64  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 O3  ? F SO4 .   ? A SO4 505 ? 1_555 89.6  ? 
6  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? J NI . ? A NI 509 ? 1_555 O3  ? F SO4 .   ? A SO4 505 ? 1_555 106.5 ? 
7  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 ND1 ? A HIS 216 ? A HIS 216 ? 1_555 119.3 ? 
8  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 116.9 ? 
9  ND1 ? A HIS 216 ? A HIS 216 ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 92.7  ? 
10 SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 O4  ? F SO4 .   ? A SO4 505 ? 1_555 117.1 ? 
11 ND1 ? A HIS 216 ? A HIS 216 ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 O4  ? F SO4 .   ? A SO4 505 ? 1_555 99.5  ? 
12 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 NI ? K NI . ? A NI 510 ? 1_555 O4  ? F SO4 .   ? A SO4 505 ? 1_555 107.6 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASP 106 A . ? ASP 106 A PRO 107 A ? PRO 107 A 1 -0.22 
2 ASP 106 A . ? ASP 106 A PRO 107 A ? PRO 107 A 1 -0.72 
3 MET 334 A . ? MET 334 A PRO 335 A ? PRO 335 A 1 -3.55 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 6 ? 
AA5 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? 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 ARG A 31  ? ALA A 36  ? ARG A 31  ALA A 36  
AA1 2 TYR A 21  ? LYS A 28  ? TYR A 21  LYS A 28  
AA1 3 VAL A 3   ? VAL A 12  ? VAL A 3   VAL A 12  
AA1 4 ALA A 43  ? ASP A 48  ? ALA A 43  ASP A 48  
AA2 1 ARG A 31  ? ALA A 36  ? ARG A 31  ALA A 36  
AA2 2 TYR A 21  ? LYS A 28  ? TYR A 21  LYS A 28  
AA2 3 VAL A 3   ? VAL A 12  ? VAL A 3   VAL A 12  
AA2 4 VAL A 53  ? PRO A 56  ? VAL A 53  PRO A 56  
AA2 5 LEU A 425 ? PHE A 428 ? LEU A 425 PHE A 428 
AA2 6 ILE A 449 ? VAL A 454 ? ILE A 449 VAL A 454 
AA2 7 VAL A 457 ? GLY A 461 ? VAL A 457 GLY A 461 
AA3 1 PHE A 58  ? ASP A 60  ? PHE A 58  ASP A 60  
AA3 2 VAL A 83  ? VAL A 88  ? VAL A 83  VAL A 88  
AA3 3 ASN A 137 ? THR A 140 ? ASN A 137 THR A 140 
AA4 1 ILE A 142 ? GLY A 143 ? ILE A 142 GLY A 143 
AA4 2 GLY A 181 ? GLY A 185 ? GLY A 181 GLY A 185 
AA4 3 VAL A 212 ? HIS A 216 ? VAL A 212 HIS A 216 
AA4 4 VAL A 242 ? VAL A 244 ? VAL A 242 VAL A 244 
AA4 5 ILE A 274 ? CYS A 278 ? ILE A 274 CYS A 278 
AA4 6 THR A 357 ? ILE A 359 ? THR A 357 ILE A 359 
AA5 1 SER A 284 ? THR A 287 ? SER A 284 THR A 287 
AA5 2 ALA A 336 ? TYR A 340 ? ALA A 336 TYR A 340 
AA5 3 ILE A 299 ? SER A 304 ? ILE A 299 SER A 304 
# 
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 O ALA A 36  ? O ALA A 36  N ASP A 24  ? N ASP A 24  
AA1 2 3 O TYR A 21  ? O TYR A 21  N VAL A 12  ? N VAL A 12  
AA1 3 4 N VAL A 3   ? N VAL A 3   O GLU A 44  ? O GLU A 44  
AA2 1 2 O ALA A 36  ? O ALA A 36  N ASP A 24  ? N ASP A 24  
AA2 2 3 O TYR A 21  ? O TYR A 21  N VAL A 12  ? N VAL A 12  
AA2 3 4 N THR A 11  ? N THR A 11  O LEU A 54  ? O LEU A 54  
AA2 4 5 N VAL A 53  ? N VAL A 53  O PHE A 428 ? O PHE A 428 
AA2 5 6 N LEU A 425 ? N LEU A 425 O MET A 453 ? O MET A 453 
AA2 6 7 N VAL A 454 ? N VAL A 454 O VAL A 457 ? O VAL A 457 
AA3 1 2 N ASP A 60  ? N ASP A 60  O ILE A 87  ? O ILE A 87  
AA3 2 3 N THR A 84  ? N THR A 84  O ASN A 137 ? O ASN A 137 
AA4 1 2 N ILE A 142 ? N ILE A 142 O SER A 183 ? O SER A 183 
AA4 2 3 N THR A 184 ? N THR A 184 O HIS A 216 ? O HIS A 216 
AA4 3 4 N TYR A 213 ? N TYR A 213 O VAL A 243 ? O VAL A 243 
AA4 4 5 N VAL A 244 ? N VAL A 244 O ALA A 275 ? O ALA A 275 
AA4 5 6 N CYS A 276 ? N CYS A 276 O MET A 358 ? O MET A 358 
AA5 1 2 N SER A 284 ? N SER A 284 O TYR A 340 ? O TYR A 340 
AA5 2 3 O ILE A 339 ? O ILE A 339 N VAL A 300 ? N VAL A 300 
# 
_pdbx_entry_details.entry_id                   9GV8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 65  ? ? -91.74  31.76   
2  1 ARG A 133 ? ? 53.86   70.96   
3  1 PHE A 221 ? ? -130.34 -118.51 
4  1 PHE A 221 ? ? -130.34 -118.66 
5  1 PRO A 223 ? ? -85.92  44.90   
6  1 PRO A 223 ? ? -85.39  44.90   
7  1 GLU A 230 ? ? -54.78  -75.54  
8  1 HIS A 246 ? ? 24.55   62.77   
9  1 MET A 369 ? ? 56.49   77.41   
10 1 THR A 402 ? ? -136.01 -90.09  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.6869 34.9112 20.3656 0.3575 ? -0.0486 ? -0.0057 ? 0.6392 ? 0.0716  ? 0.5081 ? 4.0635 ? 1.7722  
? 1.6370  ? 1.6351 ? 0.8073  ? 1.5772 ? 0.1968  ? -0.0058 ? -0.2653 ? 0.0371  ? -0.0892 ? -0.2292 ? 0.1105  ? 0.1973  ? -0.1219 ? 
2 'X-RAY DIFFRACTION' ? refined -45.9444 28.6487 5.0414  0.4701 ? -0.0307 ? -0.0363 ? 0.6620 ? -0.0300 ? 0.5887 ? 2.6024 ? -1.2555 
? -0.7575 ? 1.9785 ? -0.5757 ? 1.6609 ? 0.1321  ? 0.4811  ? -0.3133 ? -0.1717 ? -0.1574 ? 0.2605  ? 0.4708  ? -0.2308 ? 0.0422  ? 
3 'X-RAY DIFFRACTION' ? refined -45.5747 45.3874 -3.7892 0.4619 ? 0.0134  ? -0.0637 ? 0.7998 ? 0.1455  ? 0.5436 ? 1.6412 ? 0.6063  
? -1.2284 ? 0.5744 ? -0.1373 ? 2.1475 ? -0.0649 ? 0.7237  ? 0.2305  ? -0.2004 ? 0.1354  ? 0.1448  ? -0.2642 ? -0.4697 ? -0.0488 ? 
4 'X-RAY DIFFRACTION' ? refined -28.7008 38.2290 11.4549 0.3633 ? -0.0124 ? -0.0251 ? 0.5067 ? 0.0477  ? 0.4623 ? 1.7092 ? 0.4799  
? 0.7552  ? 2.7117 ? -0.3825 ? 3.1942 ? 0.0992  ? 0.3462  ? 0.0107  ? -0.2527 ? -0.0186 ? -0.1227 ? 0.0460  ? 0.4324  ? -0.1092 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 75 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 76 through 143 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 144 through 371 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 372 through 478 )
;
# 
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 ASP 479 ? A ASP 479 
2 1 Y 1 A HIS 480 ? A HIS 480 
3 1 Y 1 A HIS 481 ? A HIS 481 
4 1 Y 1 A HIS 482 ? A HIS 482 
5 1 Y 1 A HIS 483 ? A HIS 483 
6 1 Y 1 A HIS 484 ? A HIS 484 
7 1 Y 1 A HIS 485 ? A HIS 485 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
NI  NI   NI N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
SO4 S    S  N N 315 
SO4 O1   O  N N 316 
SO4 O2   O  N N 317 
SO4 O3   O  N N 318 
SO4 O4   O  N N 319 
THR N    N  N N 320 
THR CA   C  N S 321 
THR C    C  N N 322 
THR O    O  N N 323 
THR CB   C  N R 324 
THR OG1  O  N N 325 
THR CG2  C  N N 326 
THR OXT  O  N N 327 
THR H    H  N N 328 
THR H2   H  N N 329 
THR HA   H  N N 330 
THR HB   H  N N 331 
THR HG1  H  N N 332 
THR HG21 H  N N 333 
THR HG22 H  N N 334 
THR HG23 H  N N 335 
THR HXT  H  N N 336 
TRP N    N  N N 337 
TRP CA   C  N S 338 
TRP C    C  N N 339 
TRP O    O  N N 340 
TRP CB   C  N N 341 
TRP CG   C  Y N 342 
TRP CD1  C  Y N 343 
TRP CD2  C  Y N 344 
TRP NE1  N  Y N 345 
TRP CE2  C  Y N 346 
TRP CE3  C  Y N 347 
TRP CZ2  C  Y N 348 
TRP CZ3  C  Y N 349 
TRP CH2  C  Y N 350 
TRP OXT  O  N N 351 
TRP H    H  N N 352 
TRP H2   H  N N 353 
TRP HA   H  N N 354 
TRP HB2  H  N N 355 
TRP HB3  H  N N 356 
TRP HD1  H  N N 357 
TRP HE1  H  N N 358 
TRP HE3  H  N N 359 
TRP HZ2  H  N N 360 
TRP HZ3  H  N N 361 
TRP HH2  H  N N 362 
TRP HXT  H  N N 363 
TYR N    N  N N 364 
TYR CA   C  N S 365 
TYR C    C  N N 366 
TYR O    O  N N 367 
TYR CB   C  N N 368 
TYR CG   C  Y N 369 
TYR CD1  C  Y N 370 
TYR CD2  C  Y N 371 
TYR CE1  C  Y N 372 
TYR CE2  C  Y N 373 
TYR CZ   C  Y N 374 
TYR OH   O  N N 375 
TYR OXT  O  N N 376 
TYR H    H  N N 377 
TYR H2   H  N N 378 
TYR HA   H  N N 379 
TYR HB2  H  N N 380 
TYR HB3  H  N N 381 
TYR HD1  H  N N 382 
TYR HD2  H  N N 383 
TYR HE1  H  N N 384 
TYR HE2  H  N N 385 
TYR HH   H  N N 386 
TYR HXT  H  N N 387 
VAL N    N  N N 388 
VAL CA   C  N S 389 
VAL C    C  N N 390 
VAL O    O  N N 391 
VAL CB   C  N N 392 
VAL CG1  C  N N 393 
VAL CG2  C  N N 394 
VAL OXT  O  N N 395 
VAL H    H  N N 396 
VAL H2   H  N N 397 
VAL HA   H  N N 398 
VAL HB   H  N N 399 
VAL HG11 H  N N 400 
VAL HG12 H  N N 401 
VAL HG13 H  N N 402 
VAL HG21 H  N N 403 
VAL HG22 H  N N 404 
VAL HG23 H  N N 405 
VAL HXT  H  N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Ministerio de Ciencia e Innovacion (MCIN)' 
_pdbx_audit_support.country                Spain 
_pdbx_audit_support.grant_number           PID2020-116261GB-I00 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9G5M 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GV8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009860 
_atom_sites.fract_transf_matrix[1][2]   0.005693 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011385 
_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]   0.008004 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NI 
O  
S  
ZN 
# 
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   . MET A 1 1   ? -25.074 24.904 37.104  1.00 124.54 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? -24.164 25.976 37.495  1.00 132.88 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? -23.128 26.258 36.415  1.00 129.34 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? -22.777 27.412 36.169  1.00 132.03 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? -23.469 25.633 38.813  1.00 133.72 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? -24.390 25.715 40.014  1.00 137.86 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? -25.253 27.298 40.094  1.00 164.17 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? -23.961 28.367 40.729  1.00 124.18 ? 1   MET A CE  1 
ATOM   9    N  N   . LYS A 1 2   ? -22.635 25.203 35.772  1.00 117.94 ? 2   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 2   ? -21.660 25.354 34.698  1.00 107.66 ? 2   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 2   ? -22.388 25.829 33.446  1.00 97.86  ? 2   LYS A C   1 
ATOM   12   O  O   . LYS A 1 2   ? -23.207 25.098 32.881  1.00 94.75  ? 2   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 2   ? -20.926 24.041 34.448  1.00 99.48  ? 2   LYS A CB  1 
ATOM   14   C  CG  . LYS A 1 2   ? -19.570 24.218 33.790  1.00 93.98  ? 2   LYS A CG  1 
ATOM   15   C  CD  . LYS A 1 2   ? -18.895 22.885 33.526  1.00 93.95  ? 2   LYS A CD  1 
ATOM   16   C  CE  . LYS A 1 2   ? -17.505 23.089 32.945  1.00 95.67  ? 2   LYS A CE  1 
ATOM   17   N  NZ  . LYS A 1 2   ? -16.937 21.828 32.395  1.00 102.39 ? 2   LYS A NZ  1 
ATOM   18   N  N   . VAL A 1 3   ? -22.095 27.059 33.016  1.00 91.32  ? 3   VAL A N   1 
ATOM   19   C  CA  . VAL A 1 3   ? -22.777 27.616 31.854  1.00 81.38  ? 3   VAL A CA  1 
ATOM   20   C  C   . VAL A 1 3   ? -22.381 26.850 30.595  1.00 77.71  ? 3   VAL A C   1 
ATOM   21   O  O   . VAL A 1 3   ? -21.348 26.171 30.534  1.00 79.87  ? 3   VAL A O   1 
ATOM   22   C  CB  . VAL A 1 3   ? -22.478 29.117 31.709  1.00 77.62  ? 3   VAL A CB  1 
ATOM   23   C  CG1 . VAL A 1 3   ? -22.567 29.805 33.061  1.00 79.14  ? 3   VAL A CG1 1 
ATOM   24   C  CG2 . VAL A 1 3   ? -21.112 29.334 31.086  1.00 70.73  ? 3   VAL A CG2 1 
ATOM   25   N  N   . ASP A 1 4   ? -23.228 26.964 29.573  1.00 67.29  ? 4   ASP A N   1 
ATOM   26   C  CA  . ASP A 1 4   ? -23.019 26.260 28.314  1.00 66.14  ? 4   ASP A CA  1 
ATOM   27   C  C   . ASP A 1 4   ? -22.087 27.004 27.367  1.00 63.23  ? 4   ASP A C   1 
ATOM   28   O  O   . ASP A 1 4   ? -21.342 26.362 26.615  1.00 64.87  ? 4   ASP A O   1 
ATOM   29   C  CB  . ASP A 1 4   ? -24.364 26.017 27.622  1.00 66.01  ? 4   ASP A CB  1 
ATOM   30   C  CG  . ASP A 1 4   ? -25.319 25.201 28.473  1.00 69.60  ? 4   ASP A CG  1 
ATOM   31   O  OD1 . ASP A 1 4   ? -24.919 24.119 28.949  1.00 73.23  ? 4   ASP A OD1 1 
ATOM   32   O  OD2 . ASP A 1 4   ? -26.468 25.647 28.673  1.00 69.53  ? 4   ASP A OD2 1 
ATOM   33   N  N   . TRP A 1 5   ? -22.109 28.337 27.379  1.00 62.55  ? 5   TRP A N   1 
ATOM   34   C  CA  . TRP A 1 5   ? -21.281 29.126 26.478  1.00 62.37  ? 5   TRP A CA  1 
ATOM   35   C  C   . TRP A 1 5   ? -20.826 30.396 27.181  1.00 55.01  ? 5   TRP A C   1 
ATOM   36   O  O   . TRP A 1 5   ? -21.584 30.994 27.950  1.00 55.33  ? 5   TRP A O   1 
ATOM   37   C  CB  . TRP A 1 5   ? -22.036 29.480 25.190  1.00 61.70  ? 5   TRP A CB  1 
ATOM   38   C  CG  . TRP A 1 5   ? -22.220 28.317 24.264  1.00 63.62  ? 5   TRP A CG  1 
ATOM   39   C  CD1 . TRP A 1 5   ? -23.312 27.503 24.174  1.00 62.78  ? 5   TRP A CD1 1 
ATOM   40   C  CD2 . TRP A 1 5   ? -21.279 27.834 23.298  1.00 61.89  ? 5   TRP A CD2 1 
ATOM   41   N  NE1 . TRP A 1 5   ? -23.109 26.545 23.210  1.00 63.09  ? 5   TRP A NE1 1 
ATOM   42   C  CE2 . TRP A 1 5   ? -21.869 26.726 22.658  1.00 63.61  ? 5   TRP A CE2 1 
ATOM   43   C  CE3 . TRP A 1 5   ? -19.995 28.232 22.913  1.00 58.88  ? 5   TRP A CE3 1 
ATOM   44   C  CZ2 . TRP A 1 5   ? -21.219 26.012 21.653  1.00 62.79  ? 5   TRP A CZ2 1 
ATOM   45   C  CZ3 . TRP A 1 5   ? -19.352 27.522 21.914  1.00 64.53  ? 5   TRP A CZ3 1 
ATOM   46   C  CH2 . TRP A 1 5   ? -19.964 26.424 21.297  1.00 65.33  ? 5   TRP A CH2 1 
ATOM   47   N  N   . LEU A 1 6   ? -19.587 30.802 26.908  1.00 58.29  ? 6   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 6   ? -19.017 32.036 27.441  1.00 58.56  ? 6   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 6   ? -18.337 32.786 26.303  1.00 54.65  ? 6   LEU A C   1 
ATOM   50   O  O   . LEU A 1 6   ? -17.309 32.336 25.785  1.00 56.03  ? 6   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 6   ? -18.026 31.753 28.572  1.00 56.34  ? 6   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 6   ? -17.232 32.966 29.068  1.00 55.40  ? 6   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 6   ? -18.166 34.057 29.575  1.00 54.19  ? 6   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 6   ? -16.226 32.574 30.144  1.00 61.68  ? 6   LEU A CD2 1 
ATOM   55   N  N   . PHE A 1 7   ? -18.908 33.924 25.918  1.00 49.84  ? 7   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 7   ? -18.335 34.781 24.885  1.00 53.17  ? 7   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 7   ? -17.466 35.834 25.564  1.00 54.70  ? 7   PHE A C   1 
ATOM   58   O  O   . PHE A 1 7   ? -17.981 36.755 26.204  1.00 57.82  ? 7   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 7   ? -19.439 35.426 24.051  1.00 54.01  ? 7   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 7   ? -20.248 34.444 23.248  1.00 54.93  ? 7   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 7   ? -19.797 34.006 22.014  1.00 57.78  ? 7   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 7   ? -21.459 33.964 23.722  1.00 53.64  ? 7   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 7   ? -20.533 33.106 21.269  1.00 53.04  ? 7   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 7   ? -22.201 33.062 22.980  1.00 54.81  ? 7   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 7   ? -21.736 32.633 21.751  1.00 53.03  ? 7   PHE A CZ  1 
ATOM   66   N  N   . LYS A 1 8   ? -16.149 35.699 25.426  1.00 57.05  ? 8   LYS A N   1 
ATOM   67   C  CA  . LYS A 1 8   ? -15.213 36.567 26.126  1.00 56.51  ? 8   LYS A CA  1 
ATOM   68   C  C   . LYS A 1 8   ? -14.779 37.735 25.250  1.00 59.98  ? 8   LYS A C   1 
ATOM   69   O  O   . LYS A 1 8   ? -14.492 37.564 24.061  1.00 57.29  ? 8   LYS A O   1 
ATOM   70   C  CB  . LYS A 1 8   ? -13.976 35.786 26.573  1.00 56.99  ? 8   LYS A CB  1 
ATOM   71   C  CG  . LYS A 1 8   ? -14.258 34.613 27.492  1.00 57.14  ? 8   LYS A CG  1 
ATOM   72   C  CD  . LYS A 1 8   ? -12.958 33.999 27.988  1.00 57.97  ? 8   LYS A CD  1 
ATOM   73   C  CE  . LYS A 1 8   ? -12.046 33.630 26.828  1.00 58.40  ? 8   LYS A CE  1 
ATOM   74   N  NZ  . LYS A 1 8   ? -10.751 33.060 27.294  1.00 58.42  ? 8   LYS A NZ  1 
ATOM   75   N  N   . ASN A 1 9   ? -14.738 38.924 25.855  1.00 59.03  ? 9   ASN A N   1 
ATOM   76   C  CA  . ASN A 1 9   ? -14.106 40.106 25.266  1.00 58.51  ? 9   ASN A CA  1 
ATOM   77   C  C   . ASN A 1 9   ? -14.706 40.451 23.902  1.00 59.31  ? 9   ASN A C   1 
ATOM   78   O  O   . ASN A 1 9   ? -13.995 40.724 22.934  1.00 61.29  ? 9   ASN A O   1 
ATOM   79   C  CB  . ASN A 1 9   ? -12.591 39.910 25.166  1.00 56.25  ? 9   ASN A CB  1 
ATOM   80   C  CG  . ASN A 1 9   ? -11.843 41.215 24.979  1.00 54.59  ? 9   ASN A CG  1 
ATOM   81   O  OD1 . ASN A 1 9   ? -12.389 42.294 25.209  1.00 53.43  ? 9   ASN A OD1 1 
ATOM   82   N  ND2 . ASN A 1 9   ? -10.585 41.122 24.566  1.00 54.36  ? 9   ASN A ND2 1 
ATOM   83   N  N   . VAL A 1 10  ? -16.030 40.447 23.832  1.00 55.59  ? 10  VAL A N   1 
ATOM   84   C  CA  . VAL A 1 10  ? -16.739 40.764 22.599  1.00 58.40  ? 10  VAL A CA  1 
ATOM   85   C  C   . VAL A 1 10  ? -17.282 42.180 22.689  1.00 55.65  ? 10  VAL A C   1 
ATOM   86   O  O   . VAL A 1 10  ? -17.632 42.671 23.768  1.00 54.02  ? 10  VAL A O   1 
ATOM   87   C  CB  . VAL A 1 10  ? -17.875 39.755 22.321  1.00 56.73  ? 10  VAL A CB  1 
ATOM   88   C  CG1 . VAL A 1 10  ? -17.309 38.364 22.102  1.00 61.17  ? 10  VAL A CG1 1 
ATOM   89   C  CG2 . VAL A 1 10  ? -18.877 39.751 23.466  1.00 57.30  ? 10  VAL A CG2 1 
ATOM   90   N  N   . THR A 1 11  ? -17.346 42.852 21.541  1.00 58.02  ? 11  THR A N   1 
ATOM   91   C  CA  . THR A 1 11  ? -18.037 44.133 21.444  1.00 58.24  ? 11  THR A CA  1 
ATOM   92   C  C   . THR A 1 11  ? -19.533 43.855 21.397  1.00 53.44  ? 11  THR A C   1 
ATOM   93   O  O   . THR A 1 11  ? -20.039 43.306 20.413  1.00 57.71  ? 11  THR A O   1 
ATOM   94   C  CB  . THR A 1 11  ? -17.584 44.907 20.209  1.00 57.06  ? 11  THR A CB  1 
ATOM   95   O  OG1 . THR A 1 11  ? -16.184 45.198 20.307  1.00 61.33  ? 11  THR A OG1 1 
ATOM   96   C  CG2 . THR A 1 11  ? -18.359 46.212 20.088  1.00 53.13  ? 11  THR A CG2 1 
ATOM   97   N  N   . VAL A 1 12  ? -20.242 44.218 22.460  1.00 51.74  ? 12  VAL A N   1 
ATOM   98   C  CA  . VAL A 1 12  ? -21.671 43.947 22.565  1.00 54.12  ? 12  VAL A CA  1 
ATOM   99   C  C   . VAL A 1 12  ? -22.429 45.074 21.873  1.00 52.18  ? 12  VAL A C   1 
ATOM   100  O  O   . VAL A 1 12  ? -22.403 46.224 22.324  1.00 53.32  ? 12  VAL A O   1 
ATOM   101  C  CB  . VAL A 1 12  ? -22.114 43.801 24.025  1.00 50.69  ? 12  VAL A CB  1 
ATOM   102  C  CG1 . VAL A 1 12  ? -23.623 43.608 24.097  1.00 47.56  ? 12  VAL A CG1 1 
ATOM   103  C  CG2 . VAL A 1 12  ? -21.394 42.636 24.686  1.00 49.21  ? 12  VAL A CG2 1 
ATOM   104  N  N   . ILE A 1 13  ? -23.094 44.743 20.768  1.00 55.70  ? 13  ILE A N   1 
ATOM   105  C  CA  . ILE A 1 13  ? -24.081 45.615 20.144  1.00 57.41  ? 13  ILE A CA  1 
ATOM   106  C  C   . ILE A 1 13  ? -25.439 44.987 20.428  1.00 53.54  ? 13  ILE A C   1 
ATOM   107  O  O   . ILE A 1 13  ? -25.890 44.098 19.696  1.00 53.85  ? 13  ILE A O   1 
ATOM   108  C  CB  . ILE A 1 13  ? -23.835 45.785 18.641  1.00 55.73  ? 13  ILE A CB  1 
ATOM   109  C  CG1 . ILE A 1 13  ? -22.446 46.382 18.390  1.00 54.16  ? 13  ILE A CG1 1 
ATOM   110  C  CG2 . ILE A 1 13  ? -24.910 46.665 18.019  1.00 56.03  ? 13  ILE A CG2 1 
ATOM   111  C  CD1 . ILE A 1 13  ? -22.184 46.742 16.943  1.00 55.24  ? 13  ILE A CD1 1 
ATOM   112  N  N   . ASP A 1 14  ? -26.090 45.448 21.501  1.00 54.34  ? 14  ASP A N   1 
ATOM   113  C  CA  . ASP A 1 14  ? -27.261 44.780 22.061  1.00 50.62  ? 14  ASP A CA  1 
ATOM   114  C  C   . ASP A 1 14  ? -28.499 44.857 21.178  1.00 51.34  ? 14  ASP A C   1 
ATOM   115  O  O   . ASP A 1 14  ? -29.516 44.253 21.534  1.00 51.21  ? 14  ASP A O   1 
ATOM   116  C  CB  . ASP A 1 14  ? -27.571 45.358 23.443  1.00 53.49  ? 14  ASP A CB  1 
ATOM   117  C  CG  . ASP A 1 14  ? -27.695 46.875 23.437  1.00 57.54  ? 14  ASP A CG  1 
ATOM   118  O  OD1 . ASP A 1 14  ? -27.772 47.472 22.346  1.00 59.96  ? 14  ASP A OD1 1 
ATOM   119  O  OD2 . ASP A 1 14  ? -27.706 47.472 24.536  1.00 54.45  ? 14  ASP A OD2 1 
ATOM   120  N  N   . GLY A 1 15  ? -28.453 45.564 20.053  1.00 55.96  ? 15  GLY A N   1 
ATOM   121  C  CA  . GLY A 1 15  ? -29.600 45.675 19.180  1.00 54.78  ? 15  GLY A CA  1 
ATOM   122  C  C   . GLY A 1 15  ? -30.590 46.758 19.549  1.00 53.07  ? 15  GLY A C   1 
ATOM   123  O  O   . GLY A 1 15  ? -31.598 46.919 18.847  1.00 50.92  ? 15  GLY A O   1 
ATOM   124  N  N   . SER A 1 16  ? -30.343 47.502 20.626  1.00 53.00  ? 16  SER A N   1 
ATOM   125  C  CA  . SER A 1 16  ? -31.221 48.595 21.017  1.00 52.38  ? 16  SER A CA  1 
ATOM   126  C  C   . SER A 1 16  ? -30.933 49.883 20.260  1.00 54.27  ? 16  SER A C   1 
ATOM   127  O  O   . SER A 1 16  ? -31.705 50.840 20.383  1.00 54.86  ? 16  SER A O   1 
ATOM   128  C  CB  . SER A 1 16  ? -31.105 48.851 22.523  1.00 52.12  ? 16  SER A CB  1 
ATOM   129  O  OG  . SER A 1 16  ? -29.811 49.317 22.870  1.00 51.15  ? 16  SER A OG  1 
ATOM   130  N  N   . GLY A 1 17  ? -29.858 49.927 19.475  1.00 53.08  ? 17  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 17  ? -29.420 51.152 18.846  1.00 51.72  ? 17  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 17  ? -28.575 52.042 19.727  1.00 57.22  ? 17  GLY A C   1 
ATOM   133  O  O   . GLY A 1 17  ? -28.143 53.109 19.270  1.00 54.18  ? 17  GLY A O   1 
ATOM   134  N  N   . GLY A 1 18  ? -28.323 51.642 20.971  1.00 54.83  ? 18  GLY A N   1 
ATOM   135  C  CA  . GLY A 1 18  ? -27.541 52.431 21.890  1.00 54.17  ? 18  GLY A CA  1 
ATOM   136  C  C   . GLY A 1 18  ? -26.055 52.193 21.730  1.00 53.74  ? 18  GLY A C   1 
ATOM   137  O  O   . GLY A 1 18  ? -25.608 51.489 20.819  1.00 55.22  ? 18  GLY A O   1 
ATOM   138  N  N   . PRO A 1 19  ? -25.258 52.777 22.624  1.00 52.61  ? 19  PRO A N   1 
ATOM   139  C  CA  . PRO A 1 19  ? -23.801 52.667 22.502  1.00 55.61  ? 19  PRO A CA  1 
ATOM   140  C  C   . PRO A 1 19  ? -23.327 51.227 22.631  1.00 56.29  ? 19  PRO A C   1 
ATOM   141  O  O   . PRO A 1 19  ? -23.988 50.371 23.223  1.00 57.55  ? 19  PRO A O   1 
ATOM   142  C  CB  . PRO A 1 19  ? -23.278 53.526 23.661  1.00 56.12  ? 19  PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 19  ? -24.422 54.419 24.032  1.00 58.30  ? 19  PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 19  ? -25.658 53.621 23.761  1.00 56.71  ? 19  PRO A CD  1 
ATOM   145  N  N   . GLN A 1 20  ? -22.157 50.969 22.060  1.00 55.64  ? 20  GLN A N   1 
ATOM   146  C  CA  . GLN A 1 20  ? -21.521 49.664 22.117  1.00 54.38  ? 20  GLN A CA  1 
ATOM   147  C  C   . GLN A 1 20  ? -20.527 49.610 23.271  1.00 52.93  ? 20  GLN A C   1 
ATOM   148  O  O   . GLN A 1 20  ? -20.013 50.633 23.733  1.00 56.63  ? 20  GLN A O   1 
ATOM   149  C  CB  . GLN A 1 20  ? -20.813 49.346 20.797  1.00 55.26  ? 20  GLN A CB  1 
ATOM   150  C  CG  . GLN A 1 20  ? -19.750 50.358 20.401  1.00 58.83  ? 20  GLN A CG  1 
ATOM   151  C  CD  . GLN A 1 20  ? -19.047 49.989 19.109  1.00 60.27  ? 20  GLN A CD  1 
ATOM   152  O  OE1 . GLN A 1 20  ? -19.545 49.180 18.327  1.00 61.19  ? 20  GLN A OE1 1 
ATOM   153  N  NE2 . GLN A 1 20  ? -17.879 50.579 18.882  1.00 65.76  ? 20  GLN A NE2 1 
ATOM   154  N  N   . TYR A 1 21  ? -20.261 48.393 23.736  1.00 52.74  ? 21  TYR A N   1 
ATOM   155  C  CA  . TYR A 1 21  ? -19.350 48.187 24.851  1.00 52.40  ? 21  TYR A CA  1 
ATOM   156  C  C   . TYR A 1 21  ? -18.789 46.776 24.771  1.00 53.11  ? 21  TYR A C   1 
ATOM   157  O  O   . TYR A 1 21  ? -19.383 45.885 24.159  1.00 54.01  ? 21  TYR A O   1 
ATOM   158  C  CB  . TYR A 1 21  ? -20.047 48.421 26.197  1.00 51.69  ? 21  TYR A CB  1 
ATOM   159  C  CG  . TYR A 1 21  ? -21.204 47.482 26.465  1.00 56.76  ? 21  TYR A CG  1 
ATOM   160  C  CD1 . TYR A 1 21  ? -22.462 47.725 25.927  1.00 54.90  ? 21  TYR A CD1 1 
ATOM   161  C  CD2 . TYR A 1 21  ? -21.040 46.357 27.263  1.00 51.82  ? 21  TYR A CD2 1 
ATOM   162  C  CE1 . TYR A 1 21  ? -23.521 46.871 26.171  1.00 51.37  ? 21  TYR A CE1 1 
ATOM   163  C  CE2 . TYR A 1 21  ? -22.093 45.498 27.513  1.00 46.17  ? 21  TYR A CE2 1 
ATOM   164  C  CZ  . TYR A 1 21  ? -23.331 45.759 26.965  1.00 50.21  ? 21  TYR A CZ  1 
ATOM   165  O  OH  . TYR A 1 21  ? -24.382 44.906 27.213  1.00 48.34  ? 21  TYR A OH  1 
ATOM   166  N  N   . ARG A 1 22  ? -17.631 46.589 25.397  1.00 52.33  ? 22  ARG A N   1 
ATOM   167  C  CA  . ARG A 1 22  ? -16.968 45.294 25.452  1.00 55.07  ? 22  ARG A CA  1 
ATOM   168  C  C   . ARG A 1 22  ? -17.247 44.643 26.799  1.00 50.93  ? 22  ARG A C   1 
ATOM   169  O  O   . ARG A 1 22  ? -17.129 45.292 27.843  1.00 54.35  ? 22  ARG A O   1 
ATOM   170  C  CB  . ARG A 1 22  ? -15.463 45.439 25.230  1.00 52.58  ? 22  ARG A CB  1 
ATOM   171  C  CG  . ARG A 1 22  ? -15.094 46.056 23.893  1.00 53.92  ? 22  ARG A CG  1 
ATOM   172  C  CD  . ARG A 1 22  ? -13.588 46.120 23.718  1.00 61.60  ? 22  ARG A CD  1 
ATOM   173  N  NE  . ARG A 1 22  ? -13.203 46.961 22.591  1.00 62.45  ? 22  ARG A NE  1 
ATOM   174  C  CZ  . ARG A 1 22  ? -11.953 47.294 22.300  1.00 67.41  ? 22  ARG A CZ  1 
ATOM   175  N  NH1 . ARG A 1 22  ? -10.936 46.868 23.031  1.00 65.90  ? 22  ARG A NH1 1 
ATOM   176  N  NH2 . ARG A 1 22  ? -11.718 48.077 21.251  1.00 70.05  ? 22  ARG A NH2 1 
ATOM   177  N  N   . ALA A 1 23  ? -17.612 43.365 26.772  1.00 53.20  ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? -17.996 42.655 27.984  1.00 55.51  ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? -17.955 41.157 27.711  1.00 56.91  ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? -17.673 40.714 26.594  1.00 59.93  ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? -19.384 43.094 28.461  1.00 51.91  ? 23  ALA A CB  1 
ATOM   182  N  N   . ASP A 1 24  ? -18.233 40.379 28.753  1.00 52.76  ? 24  ASP A N   1 
ATOM   183  C  CA  . ASP A 1 24  ? -18.410 38.939 28.646  1.00 52.37  ? 24  ASP A CA  1 
ATOM   184  C  C   . ASP A 1 24  ? -19.894 38.607 28.702  1.00 53.20  ? 24  ASP A C   1 
ATOM   185  O  O   . ASP A 1 24  ? -20.649 39.220 29.462  1.00 51.64  ? 24  ASP A O   1 
ATOM   186  C  CB  . ASP A 1 24  ? -17.673 38.204 29.767  1.00 52.56  ? 24  ASP A CB  1 
ATOM   187  C  CG  . ASP A 1 24  ? -16.171 38.235 29.593  1.00 56.72  ? 24  ASP A CG  1 
ATOM   188  O  OD1 . ASP A 1 24  ? -15.703 38.768 28.566  1.00 57.23  ? 24  ASP A OD1 1 
ATOM   189  O  OD2 . ASP A 1 24  ? -15.458 37.725 30.482  1.00 57.23  ? 24  ASP A OD2 1 
ATOM   190  N  N   . VAL A 1 25  ? -20.308 37.639 27.891  1.00 50.37  ? 25  VAL A N   1 
ATOM   191  C  CA  . VAL A 1 25  ? -21.698 37.207 27.824  1.00 49.88  ? 25  VAL A CA  1 
ATOM   192  C  C   . VAL A 1 25  ? -21.743 35.705 28.054  1.00 54.34  ? 25  VAL A C   1 
ATOM   193  O  O   . VAL A 1 25  ? -21.045 34.946 27.371  1.00 56.38  ? 25  VAL A O   1 
ATOM   194  C  CB  . VAL A 1 25  ? -22.349 37.569 26.475  1.00 52.46  ? 25  VAL A CB  1 
ATOM   195  C  CG1 . VAL A 1 25  ? -23.819 37.179 26.476  1.00 47.93  ? 25  VAL A CG1 1 
ATOM   196  C  CG2 . VAL A 1 25  ? -22.185 39.054 26.186  1.00 51.32  ? 25  VAL A CG2 1 
ATOM   197  N  N   . ALA A 1 26  ? -22.560 35.278 29.013  1.00 56.61  ? 26  ALA A N   1 
ATOM   198  C  CA  . ALA A 1 26  ? -22.704 33.873 29.363  1.00 55.18  ? 26  ALA A CA  1 
ATOM   199  C  C   . ALA A 1 26  ? -24.110 33.397 29.031  1.00 55.97  ? 26  ALA A C   1 
ATOM   200  O  O   . ALA A 1 26  ? -25.085 34.135 29.210  1.00 52.96  ? 26  ALA A O   1 
ATOM   201  C  CB  . ALA A 1 26  ? -22.411 33.642 30.848  1.00 56.52  ? 26  ALA A CB  1 
ATOM   202  N  N   . VAL A 1 27  ? -24.210 32.161 28.550  1.00 53.87  ? 27  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 27  ? -25.476 31.561 28.151  1.00 53.98  ? 27  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 27  ? -25.652 30.256 28.913  1.00 58.95  ? 27  VAL A C   1 
ATOM   205  O  O   . VAL A 1 27  ? -24.722 29.445 28.990  1.00 59.96  ? 27  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 27  ? -25.535 31.321 26.631  1.00 52.67  ? 27  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 27  ? -26.734 30.458 26.272  1.00 54.00  ? 27  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 27  ? -25.591 32.649 25.889  1.00 53.81  ? 27  VAL A CG2 1 
ATOM   209  N  N   . LYS A 1 28  ? -26.840 30.062 29.480  1.00 60.78  ? 28  LYS A N   1 
ATOM   210  C  CA  . LYS A 1 28  ? -27.214 28.813 30.130  1.00 60.23  ? 28  LYS A CA  1 
ATOM   211  C  C   . LYS A 1 28  ? -28.553 28.371 29.562  1.00 60.00  ? 28  LYS A C   1 
ATOM   212  O  O   . LYS A 1 28  ? -29.560 29.066 29.734  1.00 59.60  ? 28  LYS A O   1 
ATOM   213  C  CB  . LYS A 1 28  ? -27.301 28.975 31.649  1.00 69.77  ? 28  LYS A CB  1 
ATOM   214  C  CG  . LYS A 1 28  ? -27.365 27.661 32.407  1.00 67.91  ? 28  LYS A CG  1 
ATOM   215  C  CD  . LYS A 1 28  ? -28.060 27.835 33.746  1.00 75.33  ? 28  LYS A CD  1 
ATOM   216  C  CE  . LYS A 1 28  ? -27.462 26.925 34.801  1.00 86.16  ? 28  LYS A CE  1 
ATOM   217  N  NZ  . LYS A 1 28  ? -26.080 27.350 35.155  1.00 93.76  ? 28  LYS A NZ  1 
ATOM   218  N  N   . GLY A 1 29  ? -28.565 27.226 28.889  1.00 59.78  ? 29  GLY A N   1 
ATOM   219  C  CA  . GLY A 1 29  ? -29.793 26.773 28.256  1.00 57.70  ? 29  GLY A CA  1 
ATOM   220  C  C   . GLY A 1 29  ? -30.101 27.624 27.040  1.00 55.22  ? 29  GLY A C   1 
ATOM   221  O  O   . GLY A 1 29  ? -29.227 27.900 26.211  1.00 60.65  ? 29  GLY A O   1 
ATOM   222  N  N   . ASP A 1 30  ? -31.358 28.054 26.928  1.00 53.94  ? 30  ASP A N   1 
ATOM   223  C  CA  . ASP A 1 30  ? -31.800 28.908 25.833  1.00 53.22  ? 30  ASP A CA  1 
ATOM   224  C  C   . ASP A 1 30  ? -31.903 30.374 26.242  1.00 53.67  ? 30  ASP A C   1 
ATOM   225  O  O   . ASP A 1 30  ? -32.534 31.165 25.534  1.00 49.48  ? 30  ASP A O   1 
ATOM   226  C  CB  . ASP A 1 30  ? -33.142 28.416 25.289  1.00 51.23  ? 30  ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 30  ? -34.225 28.372 26.352  1.00 53.72  ? 30  ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 30  ? -33.913 28.613 27.538  1.00 53.72  ? 30  ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 30  ? -35.391 28.096 26.001  1.00 52.38  ? 30  ASP A OD2 1 
ATOM   230  N  N   . ARG A 1 31  ? -31.297 30.751 27.364  1.00 56.33  ? 31  ARG A N   1 
ATOM   231  C  CA  . ARG A 1 31  ? -31.395 32.101 27.897  1.00 54.80  ? 31  ARG A CA  1 
ATOM   232  C  C   . ARG A 1 31  ? -30.011 32.712 28.055  1.00 53.58  ? 31  ARG A C   1 
ATOM   233  O  O   . ARG A 1 31  ? -29.028 32.011 28.315  1.00 58.00  ? 31  ARG A O   1 
ATOM   234  C  CB  . ARG A 1 31  ? -32.111 32.111 29.254  1.00 57.26  ? 31  ARG A CB  1 
ATOM   235  C  CG  . ARG A 1 31  ? -33.559 31.658 29.206  1.00 57.32  ? 31  ARG A CG  1 
ATOM   236  C  CD  . ARG A 1 31  ? -34.455 32.746 28.646  1.00 57.16  ? 31  ARG A CD  1 
ATOM   237  N  NE  . ARG A 1 31  ? -35.857 32.346 28.632  1.00 58.79  ? 31  ARG A NE  1 
ATOM   238  C  CZ  . ARG A 1 31  ? -36.861 33.156 28.327  1.00 55.71  ? 31  ARG A CZ  1 
ATOM   239  N  NH1 . ARG A 1 31  ? -36.656 34.426 28.021  1.00 56.02  ? 31  ARG A NH1 1 
ATOM   240  N  NH2 . ARG A 1 31  ? -38.103 32.680 28.332  1.00 53.70  ? 31  ARG A NH2 1 
ATOM   241  N  N   . ILE A 1 32  ? -29.944 34.032 27.897  1.00 55.04  ? 32  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 32  ? -28.725 34.785 28.172  1.00 53.87  ? 32  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 32  ? -28.628 34.962 29.684  1.00 53.35  ? 32  ILE A C   1 
ATOM   244  O  O   . ILE A 1 32  ? -29.452 35.648 30.292  1.00 54.84  ? 32  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 32  ? -28.719 36.137 27.450  1.00 52.16  ? 32  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 32  ? -28.720 35.931 25.934  1.00 49.69  ? 32  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 32  ? -27.520 36.967 27.883  1.00 54.01  ? 32  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 32  ? -28.803 37.218 25.144  1.00 50.59  ? 32  ILE A CD1 1 
ATOM   249  N  N   . MET A 1 33  ? -27.615 34.345 30.293  1.00 54.91  ? 33  MET A N   1 
ATOM   250  C  CA  . MET A 1 33  ? -27.546 34.285 31.749  1.00 54.33  ? 33  MET A CA  1 
ATOM   251  C  C   . MET A 1 33  ? -26.948 35.554 32.346  1.00 59.18  ? 33  MET A C   1 
ATOM   252  O  O   . MET A 1 33  ? -27.564 36.191 33.206  1.00 58.27  ? 33  MET A O   1 
ATOM   253  C  CB  . MET A 1 33  ? -26.734 33.066 32.183  1.00 56.88  ? 33  MET A CB  1 
ATOM   254  C  CG  . MET A 1 33  ? -26.600 32.925 33.687  1.00 69.52  ? 33  MET A CG  1 
ATOM   255  S  SD  . MET A 1 33  ? -25.280 31.788 34.136  1.00 101.60 ? 33  MET A SD  1 
ATOM   256  C  CE  . MET A 1 33  ? -26.119 30.745 35.326  1.00 97.95  ? 33  MET A CE  1 
ATOM   257  N  N   . ALA A 1 34  ? -25.743 35.926 31.917  1.00 60.06  ? 34  ALA A N   1 
ATOM   258  C  CA  . ALA A 1 34  ? -25.014 37.011 32.553  1.00 55.14  ? 34  ALA A CA  1 
ATOM   259  C  C   . ALA A 1 34  ? -24.311 37.863 31.507  1.00 55.72  ? 34  ALA A C   1 
ATOM   260  O  O   . ALA A 1 34  ? -23.889 37.370 30.457  1.00 55.53  ? 34  ALA A O   1 
ATOM   261  C  CB  . ALA A 1 34  ? -23.992 36.480 33.567  1.00 50.65  ? 34  ALA A CB  1 
ATOM   262  N  N   . ILE A 1 35  ? -24.199 39.156 31.810  1.00 53.72  ? 35  ILE A N   1 
ATOM   263  C  CA  . ILE A 1 35  ? -23.464 40.121 30.999  1.00 52.06  ? 35  ILE A CA  1 
ATOM   264  C  C   . ILE A 1 35  ? -22.722 41.042 31.956  1.00 53.61  ? 35  ILE A C   1 
ATOM   265  O  O   . ILE A 1 35  ? -23.350 41.743 32.757  1.00 53.91  ? 35  ILE A O   1 
ATOM   266  C  CB  . ILE A 1 35  ? -24.380 40.944 30.074  1.00 53.37  ? 35  ILE A CB  1 
ATOM   267  C  CG1 . ILE A 1 35  ? -25.080 40.046 29.051  1.00 52.43  ? 35  ILE A CG1 1 
ATOM   268  C  CG2 . ILE A 1 35  ? -23.579 42.024 29.363  1.00 51.10  ? 35  ILE A CG2 1 
ATOM   269  C  CD1 . ILE A 1 35  ? -26.091 40.780 28.194  1.00 49.64  ? 35  ILE A CD1 1 
ATOM   270  N  N   . ALA A 1 36  ? -21.396 41.040 31.880  1.00 56.11  ? 36  ALA A N   1 
ATOM   271  C  CA  . ALA A 1 36  ? -20.566 41.824 32.781  1.00 56.63  ? 36  ALA A CA  1 
ATOM   272  C  C   . ALA A 1 36  ? -19.242 42.100 32.085  1.00 54.24  ? 36  ALA A C   1 
ATOM   273  O  O   . ALA A 1 36  ? -18.884 41.400 31.133  1.00 56.56  ? 36  ALA A O   1 
ATOM   274  C  CB  . ALA A 1 36  ? -20.340 41.089 34.110  1.00 56.77  ? 36  ALA A CB  1 
ATOM   275  N  N   . PRO A 1 37  ? -18.501 43.124 32.527  1.00 55.36  ? 37  PRO A N   1 
ATOM   276  C  CA  . PRO A 1 37  ? -17.182 43.387 31.921  1.00 55.80  ? 37  PRO A CA  1 
ATOM   277  C  C   . PRO A 1 37  ? -16.264 42.178 31.910  1.00 56.66  ? 37  PRO A C   1 
ATOM   278  O  O   . PRO A 1 37  ? -15.386 42.080 31.042  1.00 57.75  ? 37  PRO A O   1 
ATOM   279  C  CB  . PRO A 1 37  ? -16.627 44.516 32.798  1.00 56.94  ? 37  PRO A CB  1 
ATOM   280  C  CG  . PRO A 1 37  ? -17.839 45.232 33.282  1.00 57.04  ? 37  PRO A CG  1 
ATOM   281  C  CD  . PRO A 1 37  ? -18.877 44.165 33.500  1.00 56.36  ? 37  PRO A CD  1 
ATOM   282  N  N   . ALA A 1 38  ? -16.438 41.254 32.851  1.00 56.28  ? 38  ALA A N   1 
ATOM   283  C  CA  . ALA A 1 38  ? -15.754 39.971 32.822  1.00 55.27  ? 38  ALA A CA  1 
ATOM   284  C  C   . ALA A 1 38  ? -16.589 38.964 33.593  1.00 62.35  ? 38  ALA A C   1 
ATOM   285  O  O   . ALA A 1 38  ? -17.366 39.329 34.480  1.00 65.65  ? 38  ALA A O   1 
ATOM   286  C  CB  . ALA A 1 38  ? -14.344 40.050 33.412  1.00 62.68  ? 38  ALA A CB  1 
ATOM   287  N  N   . LEU A 1 39  ? -16.424 37.692 33.244  1.00 62.81  ? 39  LEU A N   1 
ATOM   288  C  CA  . LEU A 1 39  ? -17.165 36.601 33.872  1.00 61.03  ? 39  LEU A CA  1 
ATOM   289  C  C   . LEU A 1 39  ? -16.180 35.478 34.179  1.00 69.21  ? 39  LEU A C   1 
ATOM   290  O  O   . LEU A 1 39  ? -15.818 34.699 33.293  1.00 69.48  ? 39  LEU A O   1 
ATOM   291  C  CB  . LEU A 1 39  ? -18.303 36.121 32.977  1.00 60.36  ? 39  LEU A CB  1 
ATOM   292  C  CG  . LEU A 1 39  ? -19.463 37.104 32.801  1.00 59.47  ? 39  LEU A CG  1 
ATOM   293  C  CD1 . LEU A 1 39  ? -20.468 36.576 31.792  1.00 56.69  ? 39  LEU A CD1 1 
ATOM   294  C  CD2 . LEU A 1 39  ? -20.136 37.381 34.136  1.00 55.48  ? 39  LEU A CD2 1 
ATOM   295  N  N   . ASP A 1 40  ? -15.739 35.408 35.436  1.00 66.95  ? 40  ASP A N   1 
ATOM   296  C  CA  . ASP A 1 40  ? -14.867 34.330 35.899  1.00 65.79  ? 40  ASP A CA  1 
ATOM   297  C  C   . ASP A 1 40  ? -15.737 33.126 36.263  1.00 65.90  ? 40  ASP A C   1 
ATOM   298  O  O   . ASP A 1 40  ? -15.931 32.773 37.428  1.00 71.50  ? 40  ASP A O   1 
ATOM   299  C  CB  . ASP A 1 40  ? -14.023 34.794 37.077  1.00 71.31  ? 40  ASP A CB  1 
ATOM   300  C  CG  . ASP A 1 40  ? -13.023 33.747 37.529  1.00 73.70  ? 40  ASP A CG  1 
ATOM   301  O  OD1 . ASP A 1 40  ? -12.755 32.801 36.758  1.00 74.43  ? 40  ASP A OD1 1 
ATOM   302  O  OD2 . ASP A 1 40  ? -12.509 33.868 38.661  1.00 78.22  ? 40  ASP A OD2 1 
ATOM   303  N  N   . VAL A 1 41  ? -16.280 32.498 35.224  1.00 67.49  ? 41  VAL A N   1 
ATOM   304  C  CA  . VAL A 1 41  ? -17.198 31.380 35.380  1.00 70.04  ? 41  VAL A CA  1 
ATOM   305  C  C   . VAL A 1 41  ? -16.678 30.192 34.585  1.00 71.69  ? 41  VAL A C   1 
ATOM   306  O  O   . VAL A 1 41  ? -16.014 30.347 33.555  1.00 73.76  ? 41  VAL A O   1 
ATOM   307  C  CB  . VAL A 1 41  ? -18.632 31.747 34.934  1.00 69.57  ? 41  VAL A CB  1 
ATOM   308  C  CG1 . VAL A 1 41  ? -19.180 32.880 35.787  1.00 68.89  ? 41  VAL A CG1 1 
ATOM   309  C  CG2 . VAL A 1 41  ? -18.656 32.124 33.459  1.00 62.31  ? 41  VAL A CG2 1 
ATOM   310  N  N   . ALA A 1 42  ? -16.976 28.995 35.082  1.00 76.45  ? 42  ALA A N   1 
ATOM   311  C  CA  . ALA A 1 42  ? -16.657 27.774 34.359  1.00 74.48  ? 42  ALA A CA  1 
ATOM   312  C  C   . ALA A 1 42  ? -17.708 27.519 33.288  1.00 73.66  ? 42  ALA A C   1 
ATOM   313  O  O   . ALA A 1 42  ? -18.910 27.658 33.533  1.00 74.83  ? 42  ALA A O   1 
ATOM   314  C  CB  . ALA A 1 42  ? -16.578 26.586 35.317  1.00 77.79  ? 42  ALA A CB  1 
ATOM   315  N  N   . ALA A 1 43  ? -17.250 27.149 32.096  1.00 74.69  ? 43  ALA A N   1 
ATOM   316  C  CA  . ALA A 1 43  ? -18.128 26.964 30.951  1.00 74.32  ? 43  ALA A CA  1 
ATOM   317  C  C   . ALA A 1 43  ? -17.840 25.635 30.272  1.00 76.04  ? 43  ALA A C   1 
ATOM   318  O  O   . ALA A 1 43  ? -16.712 25.135 30.298  1.00 85.59  ? 43  ALA A O   1 
ATOM   319  C  CB  . ALA A 1 43  ? -17.969 28.102 29.934  1.00 75.19  ? 43  ALA A CB  1 
ATOM   320  N  N   . GLU A 1 44  ? -18.882 25.064 29.662  1.00 73.69  ? 44  GLU A N   1 
ATOM   321  C  CA  . GLU A 1 44  ? -18.690 23.885 28.825  1.00 74.45  ? 44  GLU A CA  1 
ATOM   322  C  C   . GLU A 1 44  ? -17.878 24.224 27.583  1.00 74.08  ? 44  GLU A C   1 
ATOM   323  O  O   . GLU A 1 44  ? -16.997 23.455 27.180  1.00 74.21  ? 44  GLU A O   1 
ATOM   324  C  CB  . GLU A 1 44  ? -20.043 23.291 28.431  1.00 76.54  ? 44  GLU A CB  1 
ATOM   325  C  CG  . GLU A 1 44  ? -20.667 22.373 29.471  1.00 83.41  ? 44  GLU A CG  1 
ATOM   326  C  CD  . GLU A 1 44  ? -19.956 21.036 29.574  1.00 91.99  ? 44  GLU A CD  1 
ATOM   327  O  OE1 . GLU A 1 44  ? -18.853 20.986 30.158  1.00 91.07  ? 44  GLU A OE1 1 
ATOM   328  O  OE2 . GLU A 1 44  ? -20.498 20.034 29.062  1.00 99.29  ? 44  GLU A OE2 1 
ATOM   329  N  N   . GLN A 1 45  ? -18.157 25.369 26.966  1.00 68.70  ? 45  GLN A N   1 
ATOM   330  C  CA  . GLN A 1 45  ? -17.454 25.813 25.773  1.00 66.78  ? 45  GLN A CA  1 
ATOM   331  C  C   . GLN A 1 45  ? -17.203 27.309 25.868  1.00 66.07  ? 45  GLN A C   1 
ATOM   332  O  O   . GLN A 1 45  ? -18.094 28.073 26.249  1.00 63.96  ? 45  GLN A O   1 
ATOM   333  C  CB  . GLN A 1 45  ? -18.248 25.483 24.504  1.00 67.73  ? 45  GLN A CB  1 
ATOM   334  C  CG  . GLN A 1 45  ? -18.259 24.005 24.150  1.00 70.05  ? 45  GLN A CG  1 
ATOM   335  C  CD  . GLN A 1 45  ? -19.581 23.554 23.565  1.00 74.52  ? 45  GLN A CD  1 
ATOM   336  O  OE1 . GLN A 1 45  ? -20.641 23.782 24.150  1.00 73.63  ? 45  GLN A OE1 1 
ATOM   337  N  NE2 . GLN A 1 45  ? -19.528 22.912 22.404  1.00 74.73  ? 45  GLN A NE2 1 
ATOM   338  N  N   . VAL A 1 46  ? -15.985 27.719 25.524  1.00 62.33  ? 46  VAL A N   1 
ATOM   339  C  CA  . VAL A 1 46  ? -15.551 29.107 25.622  1.00 62.96  ? 46  VAL A CA  1 
ATOM   340  C  C   . VAL A 1 46  ? -15.085 29.569 24.250  1.00 61.53  ? 46  VAL A C   1 
ATOM   341  O  O   . VAL A 1 46  ? -14.465 28.802 23.504  1.00 66.29  ? 46  VAL A O   1 
ATOM   342  C  CB  . VAL A 1 46  ? -14.427 29.273 26.666  1.00 60.43  ? 46  VAL A CB  1 
ATOM   343  C  CG1 . VAL A 1 46  ? -14.111 30.739 26.879  1.00 58.65  ? 46  VAL A CG1 1 
ATOM   344  C  CG2 . VAL A 1 46  ? -14.816 28.613 27.980  1.00 62.46  ? 46  VAL A CG2 1 
ATOM   345  N  N   . ILE A 1 47  ? -15.384 30.824 23.917  1.00 61.75  ? 47  ILE A N   1 
ATOM   346  C  CA  . ILE A 1 47  ? -14.985 31.420 22.646  1.00 58.95  ? 47  ILE A CA  1 
ATOM   347  C  C   . ILE A 1 47  ? -14.374 32.786 22.924  1.00 58.87  ? 47  ILE A C   1 
ATOM   348  O  O   . ILE A 1 47  ? -15.037 33.663 23.492  1.00 56.21  ? 47  ILE A O   1 
ATOM   349  C  CB  . ILE A 1 47  ? -16.165 31.546 21.668  1.00 57.87  ? 47  ILE A CB  1 
ATOM   350  C  CG1 . ILE A 1 47  ? -16.630 30.160 21.214  1.00 61.60  ? 47  ILE A CG1 1 
ATOM   351  C  CG2 . ILE A 1 47  ? -15.779 32.411 20.476  1.00 56.81  ? 47  ILE A CG2 1 
ATOM   352  C  CD1 . ILE A 1 47  ? -17.496 30.176 19.971  1.00 61.71  ? 47  ILE A CD1 1 
ATOM   353  N  N   . ASP A 1 48  ? -13.117 32.965 22.525  1.00 56.90  ? 48  ASP A N   1 
ATOM   354  C  CA  . ASP A 1 48  ? -12.440 34.256 22.622  1.00 57.79  ? 48  ASP A CA  1 
ATOM   355  C  C   . ASP A 1 48  ? -12.893 35.114 21.448  1.00 59.18  ? 48  ASP A C   1 
ATOM   356  O  O   . ASP A 1 48  ? -12.360 35.008 20.342  1.00 59.54  ? 48  ASP A O   1 
ATOM   357  C  CB  . ASP A 1 48  ? -10.927 34.069 22.626  1.00 58.26  ? 48  ASP A CB  1 
ATOM   358  C  CG  . ASP A 1 48  ? -10.172 35.386 22.689  1.00 59.75  ? 48  ASP A CG  1 
ATOM   359  O  OD1 . ASP A 1 48  ? -10.784 36.419 23.036  1.00 56.87  ? 48  ASP A OD1 1 
ATOM   360  O  OD2 . ASP A 1 48  ? -8.959  35.388 22.385  1.00 61.61  ? 48  ASP A OD2 1 
ATOM   361  N  N   . GLY A 1 49  ? -13.881 35.972 21.686  1.00 56.17  ? 49  GLY A N   1 
ATOM   362  C  CA  . GLY A 1 49  ? -14.419 36.800 20.627  1.00 57.44  ? 49  GLY A CA  1 
ATOM   363  C  C   . GLY A 1 49  ? -13.830 38.194 20.585  1.00 58.97  ? 49  GLY A C   1 
ATOM   364  O  O   . GLY A 1 49  ? -14.548 39.166 20.332  1.00 58.63  ? 49  GLY A O   1 
ATOM   365  N  N   . GLN A 1 50  ? -12.525 38.306 20.831  1.00 60.35  ? 50  GLN A N   1 
ATOM   366  C  CA  . GLN A 1 50  ? -11.879 39.610 20.804  1.00 61.09  ? 50  GLN A CA  1 
ATOM   367  C  C   . GLN A 1 50  ? -11.914 40.181 19.392  1.00 62.43  ? 50  GLN A C   1 
ATOM   368  O  O   . GLN A 1 50  ? -11.814 39.450 18.404  1.00 61.71  ? 50  GLN A O   1 
ATOM   369  C  CB  . GLN A 1 50  ? -10.438 39.505 21.314  1.00 61.81  ? 50  GLN A CB  1 
ATOM   370  C  CG  . GLN A 1 50  ? -9.422  38.980 20.309  1.00 63.40  ? 50  GLN A CG  1 
ATOM   371  C  CD  . GLN A 1 50  ? -8.729  40.092 19.542  1.00 67.64  ? 50  GLN A CD  1 
ATOM   372  O  OE1 . GLN A 1 50  ? -8.875  41.270 19.868  1.00 72.58  ? 50  GLN A OE1 1 
ATOM   373  N  NE2 . GLN A 1 50  ? -7.973  39.721 18.514  1.00 75.28  ? 50  GLN A NE2 1 
ATOM   374  N  N   . GLY A 1 51  ? -12.087 41.497 19.302  1.00 63.55  ? 51  GLY A N   1 
ATOM   375  C  CA  . GLY A 1 51  ? -12.216 42.152 18.018  1.00 63.57  ? 51  GLY A CA  1 
ATOM   376  C  C   . GLY A 1 51  ? -13.475 41.829 17.243  1.00 60.23  ? 51  GLY A C   1 
ATOM   377  O  O   . GLY A 1 51  ? -13.641 42.343 16.131  1.00 62.42  ? 51  GLY A O   1 
ATOM   378  N  N   . ARG A 1 52  ? -14.365 40.999 17.781  1.00 61.68  ? 52  ARG A N   1 
ATOM   379  C  CA  . ARG A 1 52  ? -15.610 40.635 17.121  1.00 58.33  ? 52  ARG A CA  1 
ATOM   380  C  C   . ARG A 1 52  ? -16.783 41.346 17.784  1.00 59.47  ? 52  ARG A C   1 
ATOM   381  O  O   . ARG A 1 52  ? -16.669 41.903 18.879  1.00 60.55  ? 52  ARG A O   1 
ATOM   382  C  CB  . ARG A 1 52  ? -15.831 39.117 17.151  1.00 58.65  ? 52  ARG A CB  1 
ATOM   383  C  CG  . ARG A 1 52  ? -15.207 38.360 15.989  1.00 59.99  ? 52  ARG A CG  1 
ATOM   384  C  CD  . ARG A 1 52  ? -13.696 38.453 16.023  1.00 64.65  ? 52  ARG A CD  1 
ATOM   385  N  NE  . ARG A 1 52  ? -13.087 37.971 14.791  1.00 65.63  ? 52  ARG A NE  1 
ATOM   386  C  CZ  . ARG A 1 52  ? -11.806 38.126 14.485  1.00 66.91  ? 52  ARG A CZ  1 
ATOM   387  N  NH1 . ARG A 1 52  ? -10.971 38.749 15.300  1.00 64.81  ? 52  ARG A NH1 1 
ATOM   388  N  NH2 . ARG A 1 52  ? -11.354 37.648 13.329  1.00 71.19  ? 52  ARG A NH2 1 
ATOM   389  N  N   . VAL A 1 53  ? -17.925 41.315 17.103  1.00 57.67  ? 53  VAL A N   1 
ATOM   390  C  CA  . VAL A 1 53  ? -19.163 41.909 17.595  1.00 56.26  ? 53  VAL A CA  1 
ATOM   391  C  C   . VAL A 1 53  ? -20.146 40.791 17.910  1.00 52.60  ? 53  VAL A C   1 
ATOM   392  O  O   . VAL A 1 53  ? -20.416 39.934 17.059  1.00 54.40  ? 53  VAL A O   1 
ATOM   393  C  CB  . VAL A 1 53  ? -19.764 42.894 16.578  1.00 51.50  ? 53  VAL A CB  1 
ATOM   394  C  CG1 . VAL A 1 53  ? -21.205 43.219 16.946  1.00 49.84  ? 53  VAL A CG1 1 
ATOM   395  C  CG2 . VAL A 1 53  ? -18.934 44.164 16.516  1.00 54.09  ? 53  VAL A CG2 1 
ATOM   396  N  N   . LEU A 1 54  ? -20.677 40.798 19.129  1.00 51.90  ? 54  LEU A N   1 
ATOM   397  C  CA  . LEU A 1 54  ? -21.760 39.904 19.517  1.00 53.78  ? 54  LEU A CA  1 
ATOM   398  C  C   . LEU A 1 54  ? -23.069 40.679 19.437  1.00 52.26  ? 54  LEU A C   1 
ATOM   399  O  O   . LEU A 1 54  ? -23.261 41.660 20.165  1.00 53.21  ? 54  LEU A O   1 
ATOM   400  C  CB  . LEU A 1 54  ? -21.545 39.340 20.921  1.00 54.48  ? 54  LEU A CB  1 
ATOM   401  C  CG  . LEU A 1 54  ? -22.520 38.234 21.333  1.00 51.25  ? 54  LEU A CG  1 
ATOM   402  C  CD1 . LEU A 1 54  ? -22.454 37.067 20.360  1.00 50.47  ? 54  LEU A CD1 1 
ATOM   403  C  CD2 . LEU A 1 54  ? -22.237 37.764 22.749  1.00 54.06  ? 54  LEU A CD2 1 
ATOM   404  N  N   . ALA A 1 55  ? -23.954 40.245 18.553  1.00 48.42  ? 55  ALA A N   1 
ATOM   405  C  CA  . ALA A 1 55  ? -25.198 40.929 18.246  1.00 50.42  ? 55  ALA A CA  1 
ATOM   406  C  C   . ALA A 1 55  ? -26.358 39.958 18.386  1.00 49.62  ? 55  ALA A C   1 
ATOM   407  O  O   . ALA A 1 55  ? -26.164 38.738 18.353  1.00 49.12  ? 55  ALA A O   1 
ATOM   408  C  CB  . ALA A 1 55  ? -25.162 41.507 16.823  1.00 50.40  ? 55  ALA A CB  1 
ATOM   409  N  N   . PRO A 1 56  ? -27.580 40.465 18.558  1.00 51.62  ? 56  PRO A N   1 
ATOM   410  C  CA  . PRO A 1 56  ? -28.740 39.569 18.595  1.00 51.12  ? 56  PRO A CA  1 
ATOM   411  C  C   . PRO A 1 56  ? -28.941 38.893 17.248  1.00 48.63  ? 56  PRO A C   1 
ATOM   412  O  O   . PRO A 1 56  ? -28.516 39.396 16.205  1.00 49.53  ? 56  PRO A O   1 
ATOM   413  C  CB  . PRO A 1 56  ? -29.909 40.505 18.928  1.00 47.22  ? 56  PRO A CB  1 
ATOM   414  C  CG  . PRO A 1 56  ? -29.280 41.735 19.491  1.00 50.17  ? 56  PRO A CG  1 
ATOM   415  C  CD  . PRO A 1 56  ? -27.962 41.866 18.804  1.00 48.90  ? 56  PRO A CD  1 
ATOM   416  N  N   . GLY A 1 57  ? -29.593 37.733 17.282  1.00 47.57  ? 57  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 57  ? -29.908 37.014 16.063  1.00 50.37  ? 57  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 57  ? -30.719 37.859 15.103  1.00 50.52  ? 57  GLY A C   1 
ATOM   419  O  O   . GLY A 1 57  ? -31.679 38.520 15.508  1.00 50.13  ? 57  GLY A O   1 
ATOM   420  N  N   . PHE A 1 58  ? -30.336 37.856 13.830  1.00 49.85  ? 58  PHE A N   1 
ATOM   421  C  CA  . PHE A 1 58  ? -30.987 38.723 12.859  1.00 51.74  ? 58  PHE A CA  1 
ATOM   422  C  C   . PHE A 1 58  ? -32.393 38.221 12.554  1.00 49.50  ? 58  PHE A C   1 
ATOM   423  O  O   . PHE A 1 58  ? -32.628 37.017 12.424  1.00 48.81  ? 58  PHE A O   1 
ATOM   424  C  CB  . PHE A 1 58  ? -30.153 38.804 11.581  1.00 51.22  ? 58  PHE A CB  1 
ATOM   425  C  CG  . PHE A 1 58  ? -28.736 39.254 11.814  1.00 51.76  ? 58  PHE A CG  1 
ATOM   426  C  CD1 . PHE A 1 58  ? -28.435 40.142 12.836  1.00 51.12  ? 58  PHE A CD1 1 
ATOM   427  C  CD2 . PHE A 1 58  ? -27.706 38.783 11.018  1.00 53.94  ? 58  PHE A CD2 1 
ATOM   428  C  CE1 . PHE A 1 58  ? -27.134 40.555 13.055  1.00 48.13  ? 58  PHE A CE1 1 
ATOM   429  C  CE2 . PHE A 1 58  ? -26.402 39.192 11.233  1.00 53.23  ? 58  PHE A CE2 1 
ATOM   430  C  CZ  . PHE A 1 58  ? -26.117 40.078 12.254  1.00 50.26  ? 58  PHE A CZ  1 
ATOM   431  N  N   . ILE A 1 59  ? -33.331 39.157 12.449  1.00 48.64  ? 59  ILE A N   1 
ATOM   432  C  CA  . ILE A 1 59  ? -34.744 38.850 12.267  1.00 52.36  ? 59  ILE A CA  1 
ATOM   433  C  C   . ILE A 1 59  ? -35.145 39.329 10.879  1.00 50.86  ? 59  ILE A C   1 
ATOM   434  O  O   . ILE A 1 59  ? -35.148 40.536 10.605  1.00 55.92  ? 59  ILE A O   1 
ATOM   435  C  CB  . ILE A 1 59  ? -35.609 39.502 13.353  1.00 54.58  ? 59  ILE A CB  1 
ATOM   436  C  CG1 . ILE A 1 59  ? -35.053 39.176 14.741  1.00 47.07  ? 59  ILE A CG1 1 
ATOM   437  C  CG2 . ILE A 1 59  ? -37.054 39.043 13.230  1.00 53.66  ? 59  ILE A CG2 1 
ATOM   438  C  CD1 . ILE A 1 59  ? -35.788 39.861 15.867  1.00 49.46  ? 59  ILE A CD1 1 
ATOM   439  N  N   . ASP A 1 60  ? -35.487 38.388 10.002  1.00 51.60  ? 60  ASP A N   1 
ATOM   440  C  CA  . ASP A 1 60  ? -35.911 38.708 8.641   1.00 55.71  ? 60  ASP A CA  1 
ATOM   441  C  C   . ASP A 1 60  ? -37.420 38.922 8.659   1.00 54.91  ? 60  ASP A C   1 
ATOM   442  O  O   . ASP A 1 60  ? -38.197 37.965 8.635   1.00 51.03  ? 60  ASP A O   1 
ATOM   443  C  CB  . ASP A 1 60  ? -35.503 37.601 7.676   1.00 54.28  ? 60  ASP A CB  1 
ATOM   444  C  CG  . ASP A 1 60  ? -35.560 38.040 6.226   1.00 56.50  ? 60  ASP A CG  1 
ATOM   445  O  OD1 . ASP A 1 60  ? -35.974 39.189 5.962   1.00 58.01  ? 60  ASP A OD1 1 
ATOM   446  O  OD2 . ASP A 1 60  ? -35.191 37.233 5.347   1.00 55.03  ? 60  ASP A OD2 1 
ATOM   447  N  N   . VAL A 1 61  ? -37.836 40.191 8.696   1.00 54.45  ? 61  VAL A N   1 
ATOM   448  C  CA  . VAL A 1 61  ? -39.247 40.528 8.874   1.00 58.69  ? 61  VAL A CA  1 
ATOM   449  C  C   . VAL A 1 61  ? -40.084 40.339 7.621   1.00 61.86  ? 61  VAL A C   1 
ATOM   450  O  O   . VAL A 1 61  ? -41.317 40.406 7.702   1.00 65.17  ? 61  VAL A O   1 
ATOM   451  C  CB  . VAL A 1 61  ? -39.412 41.984 9.347   1.00 56.42  ? 61  VAL A CB  1 
ATOM   452  C  CG1 . VAL A 1 61  ? -38.749 42.173 10.693  1.00 53.57  ? 61  VAL A CG1 1 
ATOM   453  C  CG2 . VAL A 1 61  ? -38.830 42.943 8.321   1.00 56.69  ? 61  VAL A CG2 1 
ATOM   454  N  N   . HIS A 1 62  ? -39.463 40.109 6.466   1.00 56.75  ? 62  HIS A N   1 
ATOM   455  C  CA  . HIS A 1 62  ? -40.189 39.946 5.206   1.00 61.11  ? 62  HIS A CA  1 
ATOM   456  C  C   . HIS A 1 62  ? -39.629 38.728 4.478   1.00 62.43  ? 62  HIS A C   1 
ATOM   457  O  O   . HIS A 1 62  ? -38.631 38.827 3.758   1.00 66.64  ? 62  HIS A O   1 
ATOM   458  C  CB  . HIS A 1 62  ? -40.091 41.203 4.349   1.00 62.06  ? 62  HIS A CB  1 
ATOM   459  C  CG  . HIS A 1 62  ? -41.083 41.246 3.231   1.00 66.89  ? 62  HIS A CG  1 
ATOM   460  N  ND1 . HIS A 1 62  ? -42.206 42.045 3.264   1.00 68.63  ? 62  HIS A ND1 1 
ATOM   461  C  CD2 . HIS A 1 62  ? -41.131 40.576 2.056   1.00 71.63  ? 62  HIS A CD2 1 
ATOM   462  C  CE1 . HIS A 1 62  ? -42.898 41.872 2.152   1.00 75.68  ? 62  HIS A CE1 1 
ATOM   463  N  NE2 . HIS A 1 62  ? -42.267 40.986 1.402   1.00 81.02  ? 62  HIS A NE2 1 
ATOM   464  N  N   . THR A 1 63  ? -40.274 37.579 4.668   1.00 57.41  ? 63  THR A N   1 
ATOM   465  C  CA  . THR A 1 63  ? -39.903 36.344 3.996   1.00 58.38  ? 63  THR A CA  1 
ATOM   466  C  C   . THR A 1 63  ? -41.137 35.720 3.360   1.00 58.59  ? 63  THR A C   1 
ATOM   467  O  O   . THR A 1 63  ? -42.276 36.088 3.660   1.00 60.98  ? 63  THR A O   1 
ATOM   468  C  CB  . THR A 1 63  ? -39.263 35.333 4.960   1.00 59.26  ? 63  THR A CB  1 
ATOM   469  O  OG1 . THR A 1 63  ? -40.259 34.829 5.857   1.00 59.70  ? 63  THR A OG1 1 
ATOM   470  C  CG2 . THR A 1 63  ? -38.156 35.978 5.764   1.00 58.07  ? 63  THR A CG2 1 
ATOM   471  N  N   . HIS A 1 64  ? -40.892 34.766 2.467   1.00 63.05  ? 64  HIS A N   1 
ATOM   472  C  CA  . HIS A 1 64  ? -41.919 33.897 1.908   1.00 63.43  ? 64  HIS A CA  1 
ATOM   473  C  C   . HIS A 1 64  ? -41.556 32.440 2.161   1.00 61.66  ? 64  HIS A C   1 
ATOM   474  O  O   . HIS A 1 64  ? -41.772 31.563 1.322   1.00 62.07  ? 64  HIS A O   1 
ATOM   475  C  CB  . HIS A 1 64  ? -42.117 34.166 0.418   1.00 61.04  ? 64  HIS A CB  1 
ATOM   476  C  CG  . HIS A 1 64  ? -42.684 35.519 0.118   1.00 63.30  ? 64  HIS A CG  1 
ATOM   477  N  ND1 . HIS A 1 64  ? -44.025 35.810 0.251   1.00 64.94  ? 64  HIS A ND1 1 
ATOM   478  C  CD2 . HIS A 1 64  ? -42.094 36.658 -0.312  1.00 68.30  ? 64  HIS A CD2 1 
ATOM   479  C  CE1 . HIS A 1 64  ? -44.235 37.071 -0.081  1.00 66.86  ? 64  HIS A CE1 1 
ATOM   480  N  NE2 . HIS A 1 64  ? -43.080 37.608 -0.427  1.00 68.50  ? 64  HIS A NE2 1 
ATOM   481  N  N   . ASP A 1 65  ? -40.984 32.180 3.339   1.00 63.28  ? 65  ASP A N   1 
ATOM   482  C  CA  . ASP A 1 65  ? -40.504 30.860 3.729   1.00 64.19  ? 65  ASP A CA  1 
ATOM   483  C  C   . ASP A 1 65  ? -41.558 30.047 4.470   1.00 59.63  ? 65  ASP A C   1 
ATOM   484  O  O   . ASP A 1 65  ? -41.209 29.244 5.345   1.00 63.43  ? 65  ASP A O   1 
ATOM   485  C  CB  . ASP A 1 65  ? -39.245 31.000 4.586   1.00 61.23  ? 65  ASP A CB  1 
ATOM   486  C  CG  . ASP A 1 65  ? -38.201 31.894 3.947   1.00 64.50  ? 65  ASP A CG  1 
ATOM   487  O  OD1 . ASP A 1 65  ? -38.098 31.894 2.703   1.00 72.70  ? 65  ASP A OD1 1 
ATOM   488  O  OD2 . ASP A 1 65  ? -37.485 32.597 4.691   1.00 63.87  ? 65  ASP A OD2 1 
ATOM   489  N  N   . ASP A 1 66  ? -42.839 30.242 4.147   1.00 62.87  ? 66  ASP A N   1 
ATOM   490  C  CA  . ASP A 1 66  ? -43.905 29.508 4.823   1.00 58.73  ? 66  ASP A CA  1 
ATOM   491  C  C   . ASP A 1 66  ? -43.704 28.002 4.698   1.00 61.18  ? 66  ASP A C   1 
ATOM   492  O  O   . ASP A 1 66  ? -43.691 27.278 5.701   1.00 61.73  ? 66  ASP A O   1 
ATOM   493  C  CB  . ASP A 1 66  ? -45.262 29.913 4.248   1.00 60.78  ? 66  ASP A CB  1 
ATOM   494  C  CG  . ASP A 1 66  ? -45.538 31.395 4.391   1.00 55.88  ? 66  ASP A CG  1 
ATOM   495  O  OD1 . ASP A 1 66  ? -44.738 32.205 3.875   1.00 56.10  ? 66  ASP A OD1 1 
ATOM   496  O  OD2 . ASP A 1 66  ? -46.564 31.750 5.009   1.00 54.80  ? 66  ASP A OD2 1 
ATOM   497  N  N   . ILE A 1 67  ? -43.538 27.516 3.472   1.00 63.85  ? 67  ILE A N   1 
ATOM   498  C  CA  . ILE A 1 67  ? -43.402 26.083 3.242   1.00 66.83  ? 67  ILE A CA  1 
ATOM   499  C  C   . ILE A 1 67  ? -41.943 25.629 3.291   1.00 67.95  ? 67  ILE A C   1 
ATOM   500  O  O   . ILE A 1 67  ? -41.663 24.493 3.688   1.00 71.03  ? 67  ILE A O   1 
ATOM   501  C  CB  . ILE A 1 67  ? -44.054 25.709 1.898   1.00 69.04  ? 67  ILE A CB  1 
ATOM   502  C  CG1 . ILE A 1 67  ? -45.506 26.192 1.849   1.00 69.84  ? 67  ILE A CG1 1 
ATOM   503  C  CG2 . ILE A 1 67  ? -43.998 24.206 1.665   1.00 75.19  ? 67  ILE A CG2 1 
ATOM   504  C  CD1 . ILE A 1 67  ? -46.476 25.300 2.594   1.00 70.44  ? 67  ILE A CD1 1 
ATOM   505  N  N   . ASN A 1 68  ? -41.003 26.501 2.919   1.00 68.19  ? 68  ASN A N   1 
ATOM   506  C  CA  . ASN A 1 68  ? -39.620 26.069 2.741   1.00 73.19  ? 68  ASN A CA  1 
ATOM   507  C  C   . ASN A 1 68  ? -38.927 25.766 4.066   1.00 70.46  ? 68  ASN A C   1 
ATOM   508  O  O   . ASN A 1 68  ? -38.035 24.911 4.108   1.00 68.56  ? 68  ASN A O   1 
ATOM   509  C  CB  . ASN A 1 68  ? -38.836 27.123 1.957   1.00 69.64  ? 68  ASN A CB  1 
ATOM   510  C  CG  . ASN A 1 68  ? -39.191 27.138 0.481   1.00 75.00  ? 68  ASN A CG  1 
ATOM   511  O  OD1 . ASN A 1 68  ? -40.361 27.237 0.110   1.00 78.77  ? 68  ASN A OD1 1 
ATOM   512  N  ND2 . ASN A 1 68  ? -38.178 27.021 -0.370  1.00 77.58  ? 68  ASN A ND2 1 
ATOM   513  N  N   . VAL A 1 69  ? -39.310 26.443 5.153   1.00 66.21  ? 69  VAL A N   1 
ATOM   514  C  CA  . VAL A 1 69  ? -38.710 26.144 6.450   1.00 67.25  ? 69  VAL A CA  1 
ATOM   515  C  C   . VAL A 1 69  ? -39.073 24.743 6.919   1.00 66.88  ? 69  VAL A C   1 
ATOM   516  O  O   . VAL A 1 69  ? -38.377 24.173 7.766   1.00 64.48  ? 69  VAL A O   1 
ATOM   517  C  CB  . VAL A 1 69  ? -39.123 27.191 7.509   1.00 64.90  ? 69  VAL A CB  1 
ATOM   518  C  CG1 . VAL A 1 69  ? -38.619 28.572 7.124   1.00 64.71  ? 69  VAL A CG1 1 
ATOM   519  C  CG2 . VAL A 1 69  ? -40.633 27.193 7.710   1.00 62.10  ? 69  VAL A CG2 1 
ATOM   520  N  N   . ILE A 1 70  ? -40.143 24.166 6.378   1.00 66.38  ? 70  ILE A N   1 
ATOM   521  C  CA  . ILE A 1 70  ? -40.580 22.834 6.779   1.00 68.13  ? 70  ILE A CA  1 
ATOM   522  C  C   . ILE A 1 70  ? -39.877 21.746 5.974   1.00 69.22  ? 70  ILE A C   1 
ATOM   523  O  O   . ILE A 1 70  ? -39.451 20.734 6.535   1.00 74.67  ? 70  ILE A O   1 
ATOM   524  C  CB  . ILE A 1 70  ? -42.116 22.737 6.663   1.00 67.51  ? 70  ILE A CB  1 
ATOM   525  C  CG1 . ILE A 1 70  ? -42.780 23.547 7.778   1.00 63.70  ? 70  ILE A CG1 1 
ATOM   526  C  CG2 . ILE A 1 70  ? -42.574 21.286 6.696   1.00 67.64  ? 70  ILE A CG2 1 
ATOM   527  C  CD1 . ILE A 1 70  ? -44.283 23.400 7.839   1.00 61.71  ? 70  ILE A CD1 1 
ATOM   528  N  N   . ARG A 1 71  ? -39.730 21.923 4.661   1.00 68.49  ? 71  ARG A N   1 
ATOM   529  C  CA  . ARG A 1 71  ? -39.057 20.918 3.847   1.00 72.39  ? 71  ARG A CA  1 
ATOM   530  C  C   . ARG A 1 71  ? -37.557 21.147 3.722   1.00 70.76  ? 71  ARG A C   1 
ATOM   531  O  O   . ARG A 1 71  ? -36.854 20.266 3.219   1.00 72.49  ? 71  ARG A O   1 
ATOM   532  C  CB  . ARG A 1 71  ? -39.700 20.837 2.455   1.00 77.41  ? 71  ARG A CB  1 
ATOM   533  C  CG  . ARG A 1 71  ? -39.682 22.120 1.645   1.00 77.30  ? 71  ARG A CG  1 
ATOM   534  C  CD  . ARG A 1 71  ? -40.662 22.032 0.472   1.00 88.53  ? 71  ARG A CD  1 
ATOM   535  N  NE  . ARG A 1 71  ? -40.546 20.776 -0.264  1.00 92.07  ? 71  ARG A NE  1 
ATOM   536  C  CZ  . ARG A 1 71  ? -41.370 19.745 -0.129  1.00 92.87  ? 71  ARG A CZ  1 
ATOM   537  N  NH1 . ARG A 1 71  ? -42.399 19.786 0.702   1.00 91.11  ? 71  ARG A NH1 1 
ATOM   538  N  NH2 . ARG A 1 71  ? -41.151 18.642 -0.839  1.00 92.19  ? 71  ARG A NH2 1 
ATOM   539  N  N   . MET A 1 72  ? -37.058 22.298 4.157   1.00 72.29  ? 72  MET A N   1 
ATOM   540  C  CA  A MET A 1 72  ? -35.622 22.561 4.241   0.57 70.08  ? 72  MET A CA  1 
ATOM   541  C  CA  B MET A 1 72  ? -35.625 22.579 4.234   0.43 70.12  ? 72  MET A CA  1 
ATOM   542  C  C   . MET A 1 72  ? -35.327 23.140 5.621   1.00 67.67  ? 72  MET A C   1 
ATOM   543  O  O   . MET A 1 72  ? -35.014 24.327 5.762   1.00 66.50  ? 72  MET A O   1 
ATOM   544  C  CB  A MET A 1 72  ? -35.153 23.508 3.136   0.57 71.21  ? 72  MET A CB  1 
ATOM   545  C  CB  B MET A 1 72  ? -35.187 23.579 3.162   0.43 71.23  ? 72  MET A CB  1 
ATOM   546  C  CG  A MET A 1 72  ? -33.656 23.452 2.864   0.57 70.33  ? 72  MET A CG  1 
ATOM   547  C  CG  B MET A 1 72  ? -35.908 23.482 1.835   0.43 72.09  ? 72  MET A CG  1 
ATOM   548  S  SD  A MET A 1 72  ? -33.001 25.003 2.218   0.57 77.20  ? 72  MET A SD  1 
ATOM   549  S  SD  B MET A 1 72  ? -35.765 25.037 0.933   0.43 71.03  ? 72  MET A SD  1 
ATOM   550  C  CE  A MET A 1 72  ? -34.351 25.528 1.164   0.57 72.78  ? 72  MET A CE  1 
ATOM   551  C  CE  B MET A 1 72  ? -34.094 25.522 1.366   0.43 72.77  ? 72  MET A CE  1 
ATOM   552  N  N   . PRO A 1 73  ? -35.421 22.310 6.668   1.00 69.60  ? 73  PRO A N   1 
ATOM   553  C  CA  . PRO A 1 73  ? -35.231 22.842 8.033   1.00 67.17  ? 73  PRO A CA  1 
ATOM   554  C  C   . PRO A 1 73  ? -33.881 23.502 8.241   1.00 64.94  ? 73  PRO A C   1 
ATOM   555  O  O   . PRO A 1 73  ? -33.784 24.484 8.988   1.00 61.05  ? 73  PRO A O   1 
ATOM   556  C  CB  . PRO A 1 73  ? -35.400 21.597 8.915   1.00 68.10  ? 73  PRO A CB  1 
ATOM   557  C  CG  . PRO A 1 73  ? -36.170 20.631 8.079   1.00 65.70  ? 73  PRO A CG  1 
ATOM   558  C  CD  . PRO A 1 73  ? -35.711 20.868 6.675   1.00 68.54  ? 73  PRO A CD  1 
ATOM   559  N  N   . GLU A 1 74  ? -32.834 22.993 7.594   1.00 65.39  ? 74  GLU A N   1 
ATOM   560  C  CA  . GLU A 1 74  ? -31.502 23.585 7.688   1.00 63.24  ? 74  GLU A CA  1 
ATOM   561  C  C   . GLU A 1 74  ? -31.406 24.686 6.635   1.00 62.94  ? 74  GLU A C   1 
ATOM   562  O  O   . GLU A 1 74  ? -30.822 24.528 5.560   1.00 65.22  ? 74  GLU A O   1 
ATOM   563  C  CB  . GLU A 1 74  ? -30.433 22.516 7.515   1.00 66.84  ? 74  GLU A CB  1 
ATOM   564  C  CG  . GLU A 1 74  ? -30.538 21.400 8.545   1.00 65.77  ? 74  GLU A CG  1 
ATOM   565  C  CD  . GLU A 1 74  ? -29.458 20.352 8.394   1.00 72.31  ? 74  GLU A CD  1 
ATOM   566  O  OE1 . GLU A 1 74  ? -28.620 20.488 7.478   1.00 83.80  ? 74  GLU A OE1 1 
ATOM   567  O  OE2 . GLU A 1 74  ? -29.447 19.392 9.192   1.00 73.27  ? 74  GLU A OE2 1 
ATOM   568  N  N   . TYR A 1 75  ? -32.006 25.831 6.967   1.00 62.59  ? 75  TYR A N   1 
ATOM   569  C  CA  . TYR A 1 75  ? -32.166 26.945 6.032   1.00 63.77  ? 75  TYR A CA  1 
ATOM   570  C  C   . TYR A 1 75  ? -30.846 27.704 5.940   1.00 63.95  ? 75  TYR A C   1 
ATOM   571  O  O   . TYR A 1 75  ? -30.648 28.762 6.541   1.00 67.34  ? 75  TYR A O   1 
ATOM   572  C  CB  . TYR A 1 75  ? -33.307 27.849 6.476   1.00 62.88  ? 75  TYR A CB  1 
ATOM   573  C  CG  . TYR A 1 75  ? -34.160 28.394 5.352   1.00 68.11  ? 75  TYR A CG  1 
ATOM   574  C  CD1 . TYR A 1 75  ? -35.255 27.684 4.878   1.00 65.11  ? 75  TYR A CD1 1 
ATOM   575  C  CD2 . TYR A 1 75  ? -33.882 29.626 4.777   1.00 71.15  ? 75  TYR A CD2 1 
ATOM   576  C  CE1 . TYR A 1 75  ? -36.042 28.182 3.858   1.00 71.87  ? 75  TYR A CE1 1 
ATOM   577  C  CE2 . TYR A 1 75  ? -34.666 30.132 3.756   1.00 68.51  ? 75  TYR A CE2 1 
ATOM   578  C  CZ  . TYR A 1 75  ? -35.743 29.407 3.300   1.00 74.17  ? 75  TYR A CZ  1 
ATOM   579  O  OH  . TYR A 1 75  ? -36.524 29.908 2.283   1.00 72.99  ? 75  TYR A OH  1 
ATOM   580  N  N   . LEU A 1 76  ? -29.930 27.146 5.155   1.00 64.86  ? 76  LEU A N   1 
ATOM   581  C  CA  . LEU A 1 76  ? -28.620 27.768 4.992   1.00 68.70  ? 76  LEU A CA  1 
ATOM   582  C  C   . LEU A 1 76  ? -28.661 29.176 4.393   1.00 67.04  ? 76  LEU A C   1 
ATOM   583  O  O   . LEU A 1 76  ? -27.860 30.016 4.839   1.00 70.44  ? 76  LEU A O   1 
ATOM   584  C  CB  . LEU A 1 76  ? -27.719 26.853 4.152   1.00 68.48  ? 76  LEU A CB  1 
ATOM   585  C  CG  . LEU A 1 76  ? -26.294 27.360 3.922   1.00 70.80  ? 76  LEU A CG  1 
ATOM   586  C  CD1 . LEU A 1 76  ? -25.514 27.441 5.230   1.00 69.17  ? 76  LEU A CD1 1 
ATOM   587  C  CD2 . LEU A 1 76  ? -25.573 26.484 2.913   1.00 66.95  ? 76  LEU A CD2 1 
ATOM   588  N  N   . PRO A 1 77  ? -29.518 29.509 3.405   1.00 69.61  ? 77  PRO A N   1 
ATOM   589  C  CA  . PRO A 1 77  ? -29.477 30.879 2.851   1.00 71.77  ? 77  PRO A CA  1 
ATOM   590  C  C   . PRO A 1 77  ? -29.590 31.983 3.887   1.00 67.22  ? 77  PRO A C   1 
ATOM   591  O  O   . PRO A 1 77  ? -28.869 32.984 3.796   1.00 65.52  ? 77  PRO A O   1 
ATOM   592  C  CB  . PRO A 1 77  ? -30.669 30.894 1.890   1.00 70.21  ? 77  PRO A CB  1 
ATOM   593  C  CG  . PRO A 1 77  ? -30.785 29.517 1.430   1.00 70.92  ? 77  PRO A CG  1 
ATOM   594  C  CD  . PRO A 1 77  ? -30.396 28.636 2.597   1.00 80.46  ? 77  PRO A CD  1 
ATOM   595  N  N   . LYS A 1 78  ? -30.483 31.835 4.861   1.00 64.46  ? 78  LYS A N   1 
ATOM   596  C  CA  . LYS A 1 78  ? -30.643 32.845 5.898   1.00 63.08  ? 78  LYS A CA  1 
ATOM   597  C  C   . LYS A 1 78  ? -29.693 32.622 7.068   1.00 61.53  ? 78  LYS A C   1 
ATOM   598  O  O   . LYS A 1 78  ? -29.195 33.590 7.654   1.00 57.22  ? 78  LYS A O   1 
ATOM   599  C  CB  . LYS A 1 78  ? -32.088 32.858 6.400   1.00 59.29  ? 78  LYS A CB  1 
ATOM   600  C  CG  . LYS A 1 78  ? -33.131 32.874 5.295   1.00 62.05  ? 78  LYS A CG  1 
ATOM   601  C  CD  . LYS A 1 78  ? -33.587 34.276 4.938   1.00 61.65  ? 78  LYS A CD  1 
ATOM   602  C  CE  . LYS A 1 78  ? -34.681 34.228 3.880   1.00 63.59  ? 78  LYS A CE  1 
ATOM   603  N  NZ  . LYS A 1 78  ? -35.332 35.550 3.666   1.00 64.76  ? 78  LYS A NZ  1 
ATOM   604  N  N   . LEU A 1 79  ? -29.419 31.362 7.412   1.00 63.53  ? 79  LEU A N   1 
ATOM   605  C  CA  . LEU A 1 79  ? -28.591 31.082 8.580   1.00 61.83  ? 79  LEU A CA  1 
ATOM   606  C  C   . LEU A 1 79  ? -27.142 31.493 8.347   1.00 62.61  ? 79  LEU A C   1 
ATOM   607  O  O   . LEU A 1 79  ? -26.466 31.948 9.276   1.00 62.37  ? 79  LEU A O   1 
ATOM   608  C  CB  . LEU A 1 79  ? -28.684 29.601 8.947   1.00 63.43  ? 79  LEU A CB  1 
ATOM   609  C  CG  . LEU A 1 79  ? -28.259 29.231 10.371  1.00 59.68  ? 79  LEU A CG  1 
ATOM   610  C  CD1 . LEU A 1 79  ? -29.109 29.972 11.392  1.00 58.81  ? 79  LEU A CD1 1 
ATOM   611  C  CD2 . LEU A 1 79  ? -28.340 27.730 10.599  1.00 64.26  ? 79  LEU A CD2 1 
ATOM   612  N  N   . SER A 1 80  ? -26.652 31.350 7.112   1.00 66.55  ? 80  SER A N   1 
ATOM   613  C  CA  . SER A 1 80  ? -25.292 31.773 6.794   1.00 64.81  ? 80  SER A CA  1 
ATOM   614  C  C   . SER A 1 80  ? -25.117 33.283 6.901   1.00 63.49  ? 80  SER A C   1 
ATOM   615  O  O   . SER A 1 80  ? -23.988 33.751 7.090   1.00 61.64  ? 80  SER A O   1 
ATOM   616  C  CB  . SER A 1 80  ? -24.906 31.301 5.391   1.00 65.63  ? 80  SER A CB  1 
ATOM   617  O  OG  . SER A 1 80  ? -25.789 31.824 4.415   1.00 67.00  ? 80  SER A OG  1 
ATOM   618  N  N   . GLN A 1 81  ? -26.202 34.051 6.778   1.00 61.07  ? 81  GLN A N   1 
ATOM   619  C  CA  . GLN A 1 81  ? -26.147 35.488 7.011   1.00 60.80  ? 81  GLN A CA  1 
ATOM   620  C  C   . GLN A 1 81  ? -26.147 35.836 8.491   1.00 58.65  ? 81  GLN A C   1 
ATOM   621  O  O   . GLN A 1 81  ? -25.665 36.912 8.863   1.00 58.54  ? 81  GLN A O   1 
ATOM   622  C  CB  . GLN A 1 81  ? -27.335 36.184 6.346   1.00 57.56  ? 81  GLN A CB  1 
ATOM   623  C  CG  . GLN A 1 81  ? -27.492 35.910 4.866   1.00 61.64  ? 81  GLN A CG  1 
ATOM   624  C  CD  . GLN A 1 81  ? -28.703 36.609 4.278   1.00 63.53  ? 81  GLN A CD  1 
ATOM   625  O  OE1 . GLN A 1 81  ? -28.826 37.832 4.348   1.00 58.47  ? 81  GLN A OE1 1 
ATOM   626  N  NE2 . GLN A 1 81  ? -29.611 35.831 3.700   1.00 65.31  ? 81  GLN A NE2 1 
ATOM   627  N  N   . GLY A 1 82  ? -26.677 34.961 9.331   1.00 58.23  ? 82  GLY A N   1 
ATOM   628  C  CA  . GLY A 1 82  ? -26.912 35.258 10.721  1.00 58.33  ? 82  GLY A CA  1 
ATOM   629  C  C   . GLY A 1 82  ? -28.372 35.423 11.099  1.00 53.18  ? 82  GLY A C   1 
ATOM   630  O  O   . GLY A 1 82  ? -28.652 35.955 12.180  1.00 56.54  ? 82  GLY A O   1 
ATOM   631  N  N   . VAL A 1 83  ? -29.301 34.997 10.249  1.00 58.80  ? 83  VAL A N   1 
ATOM   632  C  CA  . VAL A 1 83  ? -30.724 35.105 10.547  1.00 58.26  ? 83  VAL A CA  1 
ATOM   633  C  C   . VAL A 1 83  ? -31.133 33.945 11.444  1.00 59.10  ? 83  VAL A C   1 
ATOM   634  O  O   . VAL A 1 83  ? -30.888 32.776 11.122  1.00 57.87  ? 83  VAL A O   1 
ATOM   635  C  CB  . VAL A 1 83  ? -31.554 35.124 9.253   1.00 56.93  ? 83  VAL A CB  1 
ATOM   636  C  CG1 . VAL A 1 83  ? -33.041 35.143 9.577   1.00 52.34  ? 83  VAL A CG1 1 
ATOM   637  C  CG2 . VAL A 1 83  ? -31.175 36.320 8.395   1.00 56.33  ? 83  VAL A CG2 1 
ATOM   638  N  N   . THR A 1 84  ? -31.755 34.267 12.578  1.00 50.87  ? 84  THR A N   1 
ATOM   639  C  CA  . THR A 1 84  ? -32.250 33.265 13.509  1.00 52.08  ? 84  THR A CA  1 
ATOM   640  C  C   . THR A 1 84  ? -33.769 33.209 13.580  1.00 52.30  ? 84  THR A C   1 
ATOM   641  O  O   . THR A 1 84  ? -34.309 32.288 14.204  1.00 53.06  ? 84  THR A O   1 
ATOM   642  C  CB  . THR A 1 84  ? -31.695 33.524 14.917  1.00 52.71  ? 84  THR A CB  1 
ATOM   643  O  OG1 . THR A 1 84  ? -32.145 34.804 15.380  1.00 51.75  ? 84  THR A OG1 1 
ATOM   644  C  CG2 . THR A 1 84  ? -30.175 33.501 14.906  1.00 51.94  ? 84  THR A CG2 1 
ATOM   645  N  N   . THR A 1 85  ? -34.468 34.161 12.966  1.00 51.91  ? 85  THR A N   1 
ATOM   646  C  CA  . THR A 1 85  ? -35.924 34.206 12.999  1.00 51.84  ? 85  THR A CA  1 
ATOM   647  C  C   . THR A 1 85  ? -36.424 34.813 11.698  1.00 50.68  ? 85  THR A C   1 
ATOM   648  O  O   . THR A 1 85  ? -35.923 35.856 11.269  1.00 51.04  ? 85  THR A O   1 
ATOM   649  C  CB  . THR A 1 85  ? -36.430 35.029 14.190  1.00 53.29  ? 85  THR A CB  1 
ATOM   650  O  OG1 . THR A 1 85  ? -35.992 34.428 15.415  1.00 54.44  ? 85  THR A OG1 1 
ATOM   651  C  CG2 . THR A 1 85  ? -37.949 35.106 14.179  1.00 49.09  ? 85  THR A CG2 1 
ATOM   652  N  N   . VAL A 1 86  ? -37.407 34.164 11.079  1.00 57.14  ? 86  VAL A N   1 
ATOM   653  C  CA  . VAL A 1 86  ? -38.021 34.649 9.850   1.00 58.90  ? 86  VAL A CA  1 
ATOM   654  C  C   . VAL A 1 86  ? -39.499 34.902 10.107  1.00 53.44  ? 86  VAL A C   1 
ATOM   655  O  O   . VAL A 1 86  ? -40.162 34.130 10.809  1.00 52.26  ? 86  VAL A O   1 
ATOM   656  C  CB  . VAL A 1 86  ? -37.830 33.660 8.680   1.00 54.54  ? 86  VAL A CB  1 
ATOM   657  C  CG1 . VAL A 1 86  ? -36.368 33.597 8.271   1.00 53.98  ? 86  VAL A CG1 1 
ATOM   658  C  CG2 . VAL A 1 86  ? -38.342 32.276 9.054   1.00 51.97  ? 86  VAL A CG2 1 
ATOM   659  N  N   . ILE A 1 87  ? -40.009 35.993 9.546   1.00 53.55  ? 87  ILE A N   1 
ATOM   660  C  CA  . ILE A 1 87  ? -41.428 36.318 9.594   1.00 53.19  ? 87  ILE A CA  1 
ATOM   661  C  C   . ILE A 1 87  ? -42.015 35.937 8.242   1.00 50.56  ? 87  ILE A C   1 
ATOM   662  O  O   . ILE A 1 87  ? -41.679 36.539 7.217   1.00 55.57  ? 87  ILE A O   1 
ATOM   663  C  CB  . ILE A 1 87  ? -41.665 37.800 9.913   1.00 52.98  ? 87  ILE A CB  1 
ATOM   664  C  CG1 . ILE A 1 87  ? -40.855 38.223 11.143  1.00 51.55  ? 87  ILE A CG1 1 
ATOM   665  C  CG2 . ILE A 1 87  ? -43.149 38.071 10.117  1.00 52.54  ? 87  ILE A CG2 1 
ATOM   666  C  CD1 . ILE A 1 87  ? -41.173 37.442 12.396  1.00 52.40  ? 87  ILE A CD1 1 
ATOM   667  N  N   . VAL A 1 88  ? -42.881 34.931 8.229   1.00 57.45  ? 88  VAL A N   1 
ATOM   668  C  CA  . VAL A 1 88  ? -43.441 34.412 6.999   1.00 61.17  ? 88  VAL A CA  1 
ATOM   669  C  C   . VAL A 1 88  ? -44.880 34.895 6.857   1.00 61.41  ? 88  VAL A C   1 
ATOM   670  O  O   . VAL A 1 88  ? -45.465 35.461 7.778   1.00 58.84  ? 88  VAL A O   1 
ATOM   671  C  CB  . VAL A 1 88  ? -43.355 32.868 6.936   1.00 57.27  ? 88  VAL A CB  1 
ATOM   672  C  CG1 . VAL A 1 88  ? -41.942 32.401 7.241   1.00 59.25  ? 88  VAL A CG1 1 
ATOM   673  C  CG2 . VAL A 1 88  ? -44.345 32.240 7.895   1.00 58.21  ? 88  VAL A CG2 1 
ATOM   674  N  N   . GLY A 1 89  ? -45.457 34.672 5.680   1.00 59.42  ? 89  GLY A N   1 
ATOM   675  C  CA  . GLY A 1 89  ? -46.828 35.071 5.436   1.00 54.79  ? 89  GLY A CA  1 
ATOM   676  C  C   . GLY A 1 89  ? -47.004 36.524 5.055   1.00 53.47  ? 89  GLY A C   1 
ATOM   677  O  O   . GLY A 1 89  ? -47.957 37.168 5.509   1.00 56.08  ? 89  GLY A O   1 
ATOM   678  N  N   . ASN A 1 90  ? -46.113 37.060 4.228   1.00 52.28  ? 90  ASN A N   1 
ATOM   679  C  CA  . ASN A 1 90  ? -46.180 38.454 3.818   1.00 56.14  ? 90  ASN A CA  1 
ATOM   680  C  C   . ASN A 1 90  ? -46.918 38.598 2.491   1.00 59.04  ? 90  ASN A C   1 
ATOM   681  O  O   . ASN A 1 90  ? -47.161 37.625 1.775   1.00 63.94  ? 90  ASN A O   1 
ATOM   682  C  CB  . ASN A 1 90  ? -44.777 39.051 3.696   1.00 56.77  ? 90  ASN A CB  1 
ATOM   683  C  CG  . ASN A 1 90  ? -44.080 39.178 5.032   1.00 62.10  ? 90  ASN A CG  1 
ATOM   684  O  OD1 . ASN A 1 90  ? -44.202 40.194 5.716   1.00 65.47  ? 90  ASN A OD1 1 
ATOM   685  N  ND2 . ASN A 1 90  ? -43.337 38.144 5.412   1.00 61.16  ? 90  ASN A ND2 1 
ATOM   686  N  N   . CYS A 1 91  ? -47.279 39.845 2.179   1.00 56.74  ? 91  CYS A N   1 
ATOM   687  C  CA  . CYS A 1 91  ? -47.858 40.217 0.886   1.00 61.58  ? 91  CYS A CA  1 
ATOM   688  C  C   . CYS A 1 91  ? -49.192 39.516 0.639   1.00 63.62  ? 91  CYS A C   1 
ATOM   689  O  O   . CYS A 1 91  ? -49.531 39.161 -0.492  1.00 61.22  ? 91  CYS A O   1 
ATOM   690  C  CB  . CYS A 1 91  ? -46.876 39.941 -0.253  1.00 63.92  ? 91  CYS A CB  1 
ATOM   691  S  SG  . CYS A 1 91  ? -45.273 40.731 -0.009  1.00 68.06  ? 91  CYS A SG  1 
ATOM   692  N  N   . GLY A 1 92  ? -49.962 39.322 1.706   1.00 61.95  ? 92  GLY A N   1 
ATOM   693  C  CA  . GLY A 1 92  ? -51.283 38.743 1.598   1.00 63.17  ? 92  GLY A CA  1 
ATOM   694  C  C   . GLY A 1 92  ? -51.323 37.257 1.331   1.00 65.07  ? 92  GLY A C   1 
ATOM   695  O  O   . GLY A 1 92  ? -52.419 36.687 1.270   1.00 60.94  ? 92  GLY A O   1 
ATOM   696  N  N   . ILE A 1 93  ? -50.174 36.605 1.181   1.00 60.73  ? 93  ILE A N   1 
ATOM   697  C  CA  . ILE A 1 93  ? -50.106 35.171 0.930   1.00 62.07  ? 93  ILE A CA  1 
ATOM   698  C  C   . ILE A 1 93  ? -49.457 34.503 2.133   1.00 58.92  ? 93  ILE A C   1 
ATOM   699  O  O   . ILE A 1 93  ? -48.413 34.958 2.616   1.00 62.71  ? 93  ILE A O   1 
ATOM   700  C  CB  . ILE A 1 93  ? -49.335 34.858 -0.365  1.00 66.22  ? 93  ILE A CB  1 
ATOM   701  C  CG1 . ILE A 1 93  ? -47.987 35.577 -0.371  1.00 64.57  ? 93  ILE A CG1 1 
ATOM   702  C  CG2 . ILE A 1 93  ? -50.149 35.276 -1.576  1.00 67.15  ? 93  ILE A CG2 1 
ATOM   703  C  CD1 . ILE A 1 93  ? -47.080 35.165 -1.495  1.00 68.01  ? 93  ILE A CD1 1 
ATOM   704  N  N   . SER A 1 94  ? -50.081 33.434 2.623   1.00 65.98  ? 94  SER A N   1 
ATOM   705  C  CA  . SER A 1 94  ? -49.555 32.689 3.756   1.00 62.97  ? 94  SER A CA  1 
ATOM   706  C  C   . SER A 1 94  ? -50.083 31.265 3.708   1.00 62.91  ? 94  SER A C   1 
ATOM   707  O  O   . SER A 1 94  ? -51.225 31.023 3.307   1.00 70.00  ? 94  SER A O   1 
ATOM   708  C  CB  . SER A 1 94  ? -49.933 33.339 5.092   1.00 62.13  ? 94  SER A CB  1 
ATOM   709  O  OG  . SER A 1 94  ? -51.328 33.255 5.322   1.00 61.29  ? 94  SER A OG  1 
ATOM   710  N  N   . ALA A 1 95  ? -49.232 30.324 4.120   1.00 57.67  ? 95  ALA A N   1 
ATOM   711  C  CA  . ALA A 1 95  ? -49.624 28.923 4.211   1.00 57.00  ? 95  ALA A CA  1 
ATOM   712  C  C   . ALA A 1 95  ? -50.471 28.629 5.442   1.00 54.69  ? 95  ALA A C   1 
ATOM   713  O  O   . ALA A 1 95  ? -51.265 27.684 5.418   1.00 59.24  ? 95  ALA A O   1 
ATOM   714  C  CB  . ALA A 1 95  ? -48.384 28.026 4.217   1.00 57.88  ? 95  ALA A CB  1 
ATOM   715  N  N   . ALA A 1 96  ? -50.318 29.404 6.511   1.00 52.33  ? 96  ALA A N   1 
ATOM   716  C  CA  . ALA A 1 96  ? -51.142 29.213 7.695   1.00 56.13  ? 96  ALA A CA  1 
ATOM   717  C  C   . ALA A 1 96  ? -52.578 29.633 7.410   1.00 57.75  ? 96  ALA A C   1 
ATOM   718  O  O   . ALA A 1 96  ? -52.828 30.638 6.737   1.00 61.21  ? 96  ALA A O   1 
ATOM   719  C  CB  . ALA A 1 96  ? -50.576 30.007 8.867   1.00 53.60  ? 96  ALA A CB  1 
ATOM   720  N  N   . THR A 1 97  ? -53.525 28.840 7.912   1.00 56.48  ? 97  THR A N   1 
ATOM   721  C  CA  . THR A 1 97  ? -54.972 28.989 7.738   1.00 58.92  ? 97  THR A CA  1 
ATOM   722  C  C   . THR A 1 97  ? -55.421 28.868 6.285   1.00 62.01  ? 97  THR A C   1 
ATOM   723  O  O   . THR A 1 97  ? -56.614 29.039 6.013   1.00 62.77  ? 97  THR A O   1 
ATOM   724  C  CB  . THR A 1 97  ? -55.518 30.313 8.300   1.00 59.55  ? 97  THR A CB  1 
ATOM   725  O  OG1 . THR A 1 97  ? -55.140 31.388 7.435   1.00 59.61  ? 97  THR A OG1 1 
ATOM   726  C  CG2 . THR A 1 97  ? -54.979 30.570 9.701   1.00 58.68  ? 97  THR A CG2 1 
ATOM   727  N  N   . ALA A 1 98  ? -54.522 28.575 5.347   1.00 66.25  ? 98  ALA A N   1 
ATOM   728  C  CA  . ALA A 1 98  ? -54.888 28.518 3.939   1.00 63.77  ? 98  ALA A CA  1 
ATOM   729  C  C   . ALA A 1 98  ? -55.536 27.180 3.607   1.00 67.61  ? 98  ALA A C   1 
ATOM   730  O  O   . ALA A 1 98  ? -55.024 26.121 3.980   1.00 66.90  ? 98  ALA A O   1 
ATOM   731  C  CB  . ALA A 1 98  ? -53.661 28.743 3.060   1.00 64.57  ? 98  ALA A CB  1 
ATOM   732  N  N   . THR A 1 99  ? -56.665 27.233 2.900   1.00 70.09  ? 99  THR A N   1 
ATOM   733  C  CA  . THR A 1 99  ? -57.367 26.045 2.435   1.00 73.28  ? 99  THR A CA  1 
ATOM   734  C  C   . THR A 1 99  ? -57.581 26.158 0.933   1.00 77.01  ? 99  THR A C   1 
ATOM   735  O  O   . THR A 1 99  ? -57.933 27.228 0.427   1.00 74.78  ? 99  THR A O   1 
ATOM   736  C  CB  . THR A 1 99  ? -58.713 25.871 3.156   1.00 71.15  ? 99  THR A CB  1 
ATOM   737  O  OG1 . THR A 1 99  ? -58.489 25.775 4.569   1.00 66.27  ? 99  THR A OG1 1 
ATOM   738  C  CG2 . THR A 1 99  ? -59.427 24.616 2.677   1.00 73.48  ? 99  THR A CG2 1 
ATOM   739  N  N   . MET A 1 100 ? -57.358 25.056 0.221   1.00 82.24  ? 100 MET A N   1 
ATOM   740  C  CA  . MET A 1 100 ? -57.427 25.034 -1.239  1.00 86.63  ? 100 MET A CA  1 
ATOM   741  C  C   . MET A 1 100 ? -58.500 24.043 -1.680  1.00 91.77  ? 100 MET A C   1 
ATOM   742  O  O   . MET A 1 100 ? -58.292 22.826 -1.638  1.00 93.71  ? 100 MET A O   1 
ATOM   743  C  CB  . MET A 1 100 ? -56.069 24.684 -1.838  1.00 85.46  ? 100 MET A CB  1 
ATOM   744  C  CG  . MET A 1 100 ? -55.053 25.803 -1.716  1.00 80.94  ? 100 MET A CG  1 
ATOM   745  S  SD  . MET A 1 100 ? -55.655 27.320 -2.479  1.00 89.74  ? 100 MET A SD  1 
ATOM   746  C  CE  . MET A 1 100 ? -54.436 28.494 -1.902  1.00 83.78  ? 100 MET A CE  1 
ATOM   747  N  N   . ARG A 1 101 ? -59.646 24.571 -2.107  1.00 97.70  ? 101 ARG A N   1 
ATOM   748  C  CA  . ARG A 1 101 ? -60.691 23.752 -2.704  1.00 99.82  ? 101 ARG A CA  1 
ATOM   749  C  C   . ARG A 1 101 ? -60.577 23.675 -4.219  1.00 104.95 ? 101 ARG A C   1 
ATOM   750  O  O   . ARG A 1 101 ? -61.078 22.717 -4.817  1.00 109.83 ? 101 ARG A O   1 
ATOM   751  C  CB  . ARG A 1 101 ? -62.071 24.295 -2.320  1.00 102.75 ? 101 ARG A CB  1 
ATOM   752  C  CG  . ARG A 1 101 ? -62.314 24.341 -0.821  1.00 104.03 ? 101 ARG A CG  1 
ATOM   753  C  CD  . ARG A 1 101 ? -63.636 25.012 -0.497  1.00 107.42 ? 101 ARG A CD  1 
ATOM   754  N  NE  . ARG A 1 101 ? -63.748 26.320 -1.132  1.00 107.73 ? 101 ARG A NE  1 
ATOM   755  C  CZ  . ARG A 1 101 ? -63.196 27.430 -0.664  1.00 113.90 ? 101 ARG A CZ  1 
ATOM   756  N  NH1 . ARG A 1 101 ? -62.471 27.429 0.443   1.00 101.28 ? 101 ARG A NH1 1 
ATOM   757  N  NH2 . ARG A 1 101 ? -63.374 28.571 -1.323  1.00 104.38 ? 101 ARG A NH2 1 
ATOM   758  N  N   . GLY A 1 102 ? -59.932 24.655 -4.846  1.00 102.47 ? 102 GLY A N   1 
ATOM   759  C  CA  . GLY A 1 102 ? -59.688 24.627 -6.274  1.00 102.31 ? 102 GLY A CA  1 
ATOM   760  C  C   . GLY A 1 102 ? -58.218 24.784 -6.601  1.00 101.33 ? 102 GLY A C   1 
ATOM   761  O  O   . GLY A 1 102 ? -57.366 24.145 -5.975  1.00 101.20 ? 102 GLY A O   1 
ATOM   762  N  N   . GLU A 1 103 ? -57.904 25.632 -7.576  1.00 98.15  ? 103 GLU A N   1 
ATOM   763  C  CA  A GLU A 1 103 ? -56.521 25.867 -7.952  0.67 98.66  ? 103 GLU A CA  1 
ATOM   764  C  CA  B GLU A 1 103 ? -56.521 25.869 -7.954  0.33 98.66  ? 103 GLU A CA  1 
ATOM   765  C  C   . GLU A 1 103 ? -55.896 26.929 -7.048  1.00 98.90  ? 103 GLU A C   1 
ATOM   766  O  O   . GLU A 1 103 ? -56.580 27.635 -6.302  1.00 97.89  ? 103 GLU A O   1 
ATOM   767  C  CB  A GLU A 1 103 ? -56.430 26.288 -9.418  0.67 98.41  ? 103 GLU A CB  1 
ATOM   768  C  CB  B GLU A 1 103 ? -56.430 26.297 -9.418  0.33 98.42  ? 103 GLU A CB  1 
ATOM   769  C  CG  A GLU A 1 103 ? -57.147 25.345 -10.371 0.67 99.43  ? 103 GLU A CG  1 
ATOM   770  C  CG  B GLU A 1 103 ? -56.948 27.700 -9.690  0.33 98.17  ? 103 GLU A CG  1 
ATOM   771  C  CD  A GLU A 1 103 ? -57.068 25.800 -11.813 0.67 96.38  ? 103 GLU A CD  1 
ATOM   772  C  CD  B GLU A 1 103 ? -56.899 28.065 -11.161 0.33 99.03  ? 103 GLU A CD  1 
ATOM   773  O  OE1 A GLU A 1 103 ? -55.954 26.125 -12.277 0.67 96.86  ? 103 GLU A OE1 1 
ATOM   774  O  OE1 B GLU A 1 103 ? -57.310 27.233 -11.997 0.33 97.10  ? 103 GLU A OE1 1 
ATOM   775  O  OE2 A GLU A 1 103 ? -58.122 25.840 -12.482 0.67 94.62  ? 103 GLU A OE2 1 
ATOM   776  O  OE2 B GLU A 1 103 ? -56.443 29.183 -11.482 0.33 99.78  ? 103 GLU A OE2 1 
ATOM   777  N  N   . VAL A 1 104 ? -54.573 27.035 -7.120  1.00 96.09  ? 104 VAL A N   1 
ATOM   778  C  CA  . VAL A 1 104 ? -53.831 27.991 -6.302  1.00 93.11  ? 104 VAL A CA  1 
ATOM   779  C  C   . VAL A 1 104 ? -53.862 29.357 -6.978  1.00 92.99  ? 104 VAL A C   1 
ATOM   780  O  O   . VAL A 1 104 ? -53.400 29.494 -8.120  1.00 98.40  ? 104 VAL A O   1 
ATOM   781  C  CB  . VAL A 1 104 ? -52.386 27.522 -6.069  1.00 93.00  ? 104 VAL A CB  1 
ATOM   782  C  CG1 . VAL A 1 104 ? -51.695 28.421 -5.057  1.00 88.81  ? 104 VAL A CG1 1 
ATOM   783  C  CG2 . VAL A 1 104 ? -52.367 26.073 -5.608  1.00 95.90  ? 104 VAL A CG2 1 
ATOM   784  N  N   . PRO A 1 105 ? -54.394 30.385 -6.325  1.00 89.62  ? 105 PRO A N   1 
ATOM   785  C  CA  . PRO A 1 105 ? -54.438 31.714 -6.939  1.00 87.71  ? 105 PRO A CA  1 
ATOM   786  C  C   . PRO A 1 105 ? -53.112 32.449 -6.810  1.00 84.58  ? 105 PRO A C   1 
ATOM   787  O  O   . PRO A 1 105 ? -52.292 32.174 -5.933  1.00 85.90  ? 105 PRO A O   1 
ATOM   788  C  CB  . PRO A 1 105 ? -55.539 32.426 -6.147  1.00 86.91  ? 105 PRO A CB  1 
ATOM   789  C  CG  . PRO A 1 105 ? -55.473 31.794 -4.798  1.00 86.73  ? 105 PRO A CG  1 
ATOM   790  C  CD  . PRO A 1 105 ? -55.092 30.351 -5.027  1.00 89.70  ? 105 PRO A CD  1 
ATOM   791  N  N   . ASP A 1 106 ? -52.915 33.406 -7.717  1.00 81.29  ? 106 ASP A N   1 
ATOM   792  C  CA  A ASP A 1 106 ? -51.707 34.217 -7.701  0.54 78.70  ? 106 ASP A CA  1 
ATOM   793  C  CA  B ASP A 1 106 ? -51.711 34.226 -7.711  0.46 78.70  ? 106 ASP A CA  1 
ATOM   794  C  C   . ASP A 1 106 ? -51.801 35.279 -6.607  1.00 78.83  ? 106 ASP A C   1 
ATOM   795  O  O   . ASP A 1 106 ? -52.859 35.885 -6.416  1.00 77.94  ? 106 ASP A O   1 
ATOM   796  C  CB  A ASP A 1 106 ? -51.487 34.888 -9.057  0.54 78.45  ? 106 ASP A CB  1 
ATOM   797  C  CB  B ASP A 1 106 ? -51.523 34.900 -9.074  0.46 78.45  ? 106 ASP A CB  1 
ATOM   798  C  CG  A ASP A 1 106 ? -51.216 33.889 -10.165 0.54 78.16  ? 106 ASP A CG  1 
ATOM   799  C  CG  B ASP A 1 106 ? -50.191 35.620 -9.203  0.46 77.07  ? 106 ASP A CG  1 
ATOM   800  O  OD1 A ASP A 1 106 ? -51.362 32.672 -9.922  0.54 78.98  ? 106 ASP A OD1 1 
ATOM   801  O  OD1 B ASP A 1 106 ? -50.011 36.675 -8.559  0.46 75.53  ? 106 ASP A OD1 1 
ATOM   802  O  OD2 A ASP A 1 106 ? -50.851 34.321 -11.279 0.54 77.88  ? 106 ASP A OD2 1 
ATOM   803  O  OD2 B ASP A 1 106 ? -49.321 35.128 -9.952  0.46 77.23  ? 106 ASP A OD2 1 
ATOM   804  N  N   . PRO A 1 107 ? -50.710 35.521 -5.868  1.00 80.40  ? 107 PRO A N   1 
ATOM   805  C  CA  . PRO A 1 107 ? -49.396 34.879 -5.969  1.00 81.75  ? 107 PRO A CA  1 
ATOM   806  C  C   . PRO A 1 107 ? -49.144 33.807 -4.914  1.00 84.91  ? 107 PRO A C   1 
ATOM   807  O  O   . PRO A 1 107 ? -48.009 33.656 -4.470  1.00 85.94  ? 107 PRO A O   1 
ATOM   808  C  CB  . PRO A 1 107 ? -48.447 36.065 -5.786  1.00 78.82  ? 107 PRO A CB  1 
ATOM   809  C  CG  . PRO A 1 107 ? -49.155 36.900 -4.746  1.00 76.88  ? 107 PRO A CG  1 
ATOM   810  C  CD  . PRO A 1 107 ? -50.644 36.723 -5.015  1.00 76.82  ? 107 PRO A CD  1 
ATOM   811  N  N   . MET A 1 108 ? -50.152 33.045 -4.481  1.00 80.97  ? 108 MET A N   1 
ATOM   812  C  CA  A MET A 1 108 ? -49.897 32.018 -3.480  0.77 81.81  ? 108 MET A CA  1 
ATOM   813  C  CA  B MET A 1 108 ? -49.935 31.993 -3.493  0.23 81.80  ? 108 MET A CA  1 
ATOM   814  C  C   . MET A 1 108 ? -49.085 30.852 -4.030  1.00 82.75  ? 108 MET A C   1 
ATOM   815  O  O   . MET A 1 108 ? -48.639 30.009 -3.245  1.00 84.88  ? 108 MET A O   1 
ATOM   816  C  CB  A MET A 1 108 ? -51.216 31.515 -2.892  0.77 84.26  ? 108 MET A CB  1 
ATOM   817  C  CB  B MET A 1 108 ? -51.273 31.436 -2.998  0.23 84.48  ? 108 MET A CB  1 
ATOM   818  C  CG  A MET A 1 108 ? -51.095 31.015 -1.462  0.77 81.07  ? 108 MET A CG  1 
ATOM   819  C  CG  B MET A 1 108 ? -52.220 32.480 -2.435  0.23 84.08  ? 108 MET A CG  1 
ATOM   820  S  SD  A MET A 1 108 ? -52.614 31.230 -0.521  0.77 88.80  ? 108 MET A SD  1 
ATOM   821  S  SD  B MET A 1 108 ? -53.346 31.809 -1.195  0.23 90.35  ? 108 MET A SD  1 
ATOM   822  C  CE  A MET A 1 108 ? -52.919 32.972 -0.797  0.77 79.22  ? 108 MET A CE  1 
ATOM   823  C  CE  B MET A 1 108 ? -52.181 31.208 0.027   0.23 80.73  ? 108 MET A CE  1 
ATOM   824  N  N   . ASN A 1 109 ? -48.866 30.793 -5.346  1.00 82.26  ? 109 ASN A N   1 
ATOM   825  C  CA  . ASN A 1 109 ? -48.014 29.764 -5.926  1.00 80.57  ? 109 ASN A CA  1 
ATOM   826  C  C   . ASN A 1 109 ? -46.541 29.977 -5.606  1.00 81.41  ? 109 ASN A C   1 
ATOM   827  O  O   . ASN A 1 109 ? -45.740 29.064 -5.830  1.00 81.83  ? 109 ASN A O   1 
ATOM   828  C  CB  . ASN A 1 109 ? -48.216 29.711 -7.442  1.00 83.09  ? 109 ASN A CB  1 
ATOM   829  C  CG  . ASN A 1 109 ? -48.340 31.089 -8.062  1.00 81.69  ? 109 ASN A CG  1 
ATOM   830  O  OD1 . ASN A 1 109 ? -47.381 31.859 -8.089  1.00 80.48  ? 109 ASN A OD1 1 
ATOM   831  N  ND2 . ASN A 1 109 ? -49.526 31.403 -8.573  1.00 80.79  ? 109 ASN A ND2 1 
ATOM   832  N  N   . LEU A 1 110 ? -46.167 31.155 -5.094  1.00 82.98  ? 110 LEU A N   1 
ATOM   833  C  CA  . LEU A 1 110 ? -44.787 31.379 -4.676  1.00 80.30  ? 110 LEU A CA  1 
ATOM   834  C  C   . LEU A 1 110 ? -44.418 30.499 -3.489  1.00 77.27  ? 110 LEU A C   1 
ATOM   835  O  O   . LEU A 1 110 ? -43.260 30.086 -3.359  1.00 78.90  ? 110 LEU A O   1 
ATOM   836  C  CB  . LEU A 1 110 ? -44.572 32.854 -4.324  1.00 76.59  ? 110 LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 110 ? -44.832 33.922 -5.394  1.00 77.40  ? 110 LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 110 ? -44.509 35.307 -4.846  1.00 77.47  ? 110 LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 110 ? -44.038 33.646 -6.661  1.00 78.41  ? 110 LEU A CD2 1 
ATOM   840  N  N   . LEU A 1 111 ? -45.386 30.198 -2.621  1.00 78.44  ? 111 LEU A N   1 
ATOM   841  C  CA  . LEU A 1 111 ? -45.124 29.365 -1.451  1.00 78.80  ? 111 LEU A CA  1 
ATOM   842  C  C   . LEU A 1 111 ? -44.926 27.904 -1.836  1.00 81.11  ? 111 LEU A C   1 
ATOM   843  O  O   . LEU A 1 111 ? -44.006 27.247 -1.335  1.00 79.31  ? 111 LEU A O   1 
ATOM   844  C  CB  . LEU A 1 111 ? -46.269 29.495 -0.444  1.00 74.47  ? 111 LEU A CB  1 
ATOM   845  C  CG  . LEU A 1 111 ? -46.252 30.668 0.540   1.00 67.57  ? 111 LEU A CG  1 
ATOM   846  C  CD1 . LEU A 1 111 ? -45.766 31.944 -0.123  1.00 64.98  ? 111 LEU A CD1 1 
ATOM   847  C  CD2 . LEU A 1 111 ? -47.640 30.871 1.132   1.00 65.49  ? 111 LEU A CD2 1 
ATOM   848  N  N   . GLY A 1 112 ? -45.776 27.382 -2.710  1.00 83.39  ? 112 GLY A N   1 
ATOM   849  C  CA  . GLY A 1 112 ? -45.659 25.999 -3.123  1.00 88.68  ? 112 GLY A CA  1 
ATOM   850  C  C   . GLY A 1 112 ? -46.916 25.537 -3.819  1.00 94.29  ? 112 GLY A C   1 
ATOM   851  O  O   . GLY A 1 112 ? -47.923 26.248 -3.890  1.00 93.66  ? 112 GLY A O   1 
ATOM   852  N  N   . GLU A 1 113 ? -46.833 24.318 -4.344  1.00 98.47  ? 113 GLU A N   1 
ATOM   853  C  CA  A GLU A 1 113 ? -47.967 23.692 -5.005  0.47 102.06 ? 113 GLU A CA  1 
ATOM   854  C  CA  B GLU A 1 113 ? -47.968 23.697 -5.008  0.53 102.08 ? 113 GLU A CA  1 
ATOM   855  C  C   . GLU A 1 113 ? -49.083 23.421 -3.998  1.00 102.02 ? 113 GLU A C   1 
ATOM   856  O  O   . GLU A 1 113 ? -48.878 23.467 -2.781  1.00 99.39  ? 113 GLU A O   1 
ATOM   857  C  CB  A GLU A 1 113 ? -47.528 22.393 -5.678  0.47 104.84 ? 113 GLU A CB  1 
ATOM   858  C  CB  B GLU A 1 113 ? -47.517 22.408 -5.710  0.53 104.84 ? 113 GLU A CB  1 
ATOM   859  C  CG  A GLU A 1 113 ? -46.272 22.538 -6.527  0.47 104.01 ? 113 GLU A CG  1 
ATOM   860  C  CG  B GLU A 1 113 ? -48.560 21.688 -6.573  0.53 106.09 ? 113 GLU A CG  1 
ATOM   861  C  CD  A GLU A 1 113 ? -45.347 21.341 -6.411  0.47 104.34 ? 113 GLU A CD  1 
ATOM   862  C  CD  B GLU A 1 113 ? -48.981 22.470 -7.808  0.53 105.62 ? 113 GLU A CD  1 
ATOM   863  O  OE1 A GLU A 1 113 ? -45.705 20.382 -5.694  0.47 105.99 ? 113 GLU A OE1 1 
ATOM   864  O  OE1 B GLU A 1 113 ? -48.394 23.537 -8.085  0.53 103.84 ? 113 GLU A OE1 1 
ATOM   865  O  OE2 A GLU A 1 113 ? -44.261 21.359 -7.030  0.47 102.86 ? 113 GLU A OE2 1 
ATOM   866  O  OE2 B GLU A 1 113 ? -49.905 22.006 -8.510  0.53 107.14 ? 113 GLU A OE2 1 
ATOM   867  N  N   . GLN A 1 114 ? -50.287 23.149 -4.524  1.00 107.88 ? 114 GLN A N   1 
ATOM   868  C  CA  . GLN A 1 114 ? -51.435 22.810 -3.682  1.00 107.03 ? 114 GLN A CA  1 
ATOM   869  C  C   . GLN A 1 114 ? -51.057 21.825 -2.599  1.00 103.33 ? 114 GLN A C   1 
ATOM   870  O  O   . GLN A 1 114 ? -51.335 22.044 -1.418  1.00 99.74  ? 114 GLN A O   1 
ATOM   871  C  CB  . GLN A 1 114 ? -52.575 22.211 -4.514  1.00 110.08 ? 114 GLN A CB  1 
ATOM   872  C  CG  . GLN A 1 114 ? -53.900 21.988 -3.732  1.00 110.52 ? 114 GLN A CG  1 
ATOM   873  C  CD  . GLN A 1 114 ? -54.130 20.564 -3.236  1.00 119.20 ? 114 GLN A CD  1 
ATOM   874  O  OE1 . GLN A 1 114 ? -53.257 19.974 -2.573  1.00 128.50 ? 114 GLN A OE1 1 
ATOM   875  N  NE2 . GLN A 1 114 ? -55.295 20.002 -3.556  1.00 116.72 ? 114 GLN A NE2 1 
ATOM   876  N  N   . GLN A 1 115 ? -50.360 20.760 -2.992  1.00 108.11 ? 115 GLN A N   1 
ATOM   877  C  CA  . GLN A 1 115 ? -50.150 19.604 -2.133  1.00 107.63 ? 115 GLN A CA  1 
ATOM   878  C  C   . GLN A 1 115 ? -49.532 19.972 -0.792  1.00 104.71 ? 115 GLN A C   1 
ATOM   879  O  O   . GLN A 1 115 ? -49.601 19.174 0.152   1.00 105.05 ? 115 GLN A O   1 
ATOM   880  C  CB  . GLN A 1 115 ? -49.256 18.601 -2.868  1.00 109.42 ? 115 GLN A CB  1 
ATOM   881  C  CG  . GLN A 1 115 ? -49.676 18.401 -4.312  1.00 113.70 ? 115 GLN A CG  1 
ATOM   882  C  CD  . GLN A 1 115 ? -48.610 17.742 -5.159  1.00 120.66 ? 115 GLN A CD  1 
ATOM   883  O  OE1 . GLN A 1 115 ? -47.716 17.068 -4.643  1.00 121.57 ? 115 GLN A OE1 1 
ATOM   884  N  NE2 . GLN A 1 115 ? -48.695 17.936 -6.469  1.00 116.53 ? 115 GLN A NE2 1 
ATOM   885  N  N   . HIS A 1 116 ? -48.964 21.174 -0.675  1.00 97.70  ? 116 HIS A N   1 
ATOM   886  C  CA  . HIS A 1 116 ? -48.237 21.601 0.507   1.00 93.21  ? 116 HIS A CA  1 
ATOM   887  C  C   . HIS A 1 116 ? -49.063 22.515 1.406   1.00 84.52  ? 116 HIS A C   1 
ATOM   888  O  O   . HIS A 1 116 ? -48.608 22.863 2.499   1.00 80.31  ? 116 HIS A O   1 
ATOM   889  C  CB  . HIS A 1 116 ? -46.936 22.294 0.075   1.00 94.92  ? 116 HIS A CB  1 
ATOM   890  C  CG  . HIS A 1 116 ? -46.060 21.449 -0.807  1.00 99.55  ? 116 HIS A CG  1 
ATOM   891  N  ND1 . HIS A 1 116 ? -46.552 20.724 -1.871  1.00 103.21 ? 116 HIS A ND1 1 
ATOM   892  C  CD2 . HIS A 1 116 ? -44.726 21.216 -0.782  1.00 100.36 ? 116 HIS A CD2 1 
ATOM   893  C  CE1 . HIS A 1 116 ? -45.563 20.076 -2.459  1.00 103.96 ? 116 HIS A CE1 1 
ATOM   894  N  NE2 . HIS A 1 116 ? -44.443 20.358 -1.818  1.00 99.16  ? 116 HIS A NE2 1 
ATOM   895  N  N   . PHE A 1 117 ? -50.272 22.896 0.982   1.00 86.64  ? 117 PHE A N   1 
ATOM   896  C  CA  . PHE A 1 117 ? -51.161 23.725 1.798   1.00 81.47  ? 117 PHE A CA  1 
ATOM   897  C  C   . PHE A 1 117 ? -52.042 22.808 2.643   1.00 72.97  ? 117 PHE A C   1 
ATOM   898  O  O   . PHE A 1 117 ? -53.179 22.481 2.298   1.00 74.75  ? 117 PHE A O   1 
ATOM   899  C  CB  . PHE A 1 117 ? -51.994 24.651 0.920   1.00 77.54  ? 117 PHE A CB  1 
ATOM   900  C  CG  . PHE A 1 117 ? -51.214 25.776 0.305   1.00 75.96  ? 117 PHE A CG  1 
ATOM   901  C  CD1 . PHE A 1 117 ? -50.976 26.943 1.012   1.00 75.92  ? 117 PHE A CD1 1 
ATOM   902  C  CD2 . PHE A 1 117 ? -50.725 25.669 -0.985  1.00 83.05  ? 117 PHE A CD2 1 
ATOM   903  C  CE1 . PHE A 1 117 ? -50.259 27.981 0.444   1.00 76.76  ? 117 PHE A CE1 1 
ATOM   904  C  CE2 . PHE A 1 117 ? -50.009 26.702 -1.559  1.00 84.77  ? 117 PHE A CE2 1 
ATOM   905  C  CZ  . PHE A 1 117 ? -49.774 27.858 -0.844  1.00 79.76  ? 117 PHE A CZ  1 
ATOM   906  N  N   . ILE A 1 118 ? -51.496 22.396 3.787   1.00 72.42  ? 118 ILE A N   1 
ATOM   907  C  CA  . ILE A 1 118 ? -52.188 21.479 4.685   1.00 71.37  ? 118 ILE A CA  1 
ATOM   908  C  C   . ILE A 1 118 ? -52.159 22.022 6.107   1.00 64.46  ? 118 ILE A C   1 
ATOM   909  O  O   . ILE A 1 118 ? -51.949 21.269 7.065   1.00 64.39  ? 118 ILE A O   1 
ATOM   910  C  CB  . ILE A 1 118 ? -51.562 20.074 4.631   1.00 71.04  ? 118 ILE A CB  1 
ATOM   911  C  CG1 . ILE A 1 118 ? -50.035 20.179 4.638   1.00 68.68  ? 118 ILE A CG1 1 
ATOM   912  C  CG2 . ILE A 1 118 ? -52.062 19.314 3.411   1.00 74.35  ? 118 ILE A CG2 1 
ATOM   913  C  CD1 . ILE A 1 118 ? -49.334 18.938 5.142   1.00 66.78  ? 118 ILE A CD1 1 
ATOM   914  N  N   . TYR A 1 119 ? -52.378 23.327 6.258   1.00 64.39  ? 119 TYR A N   1 
ATOM   915  C  CA  . TYR A 1 119 ? -52.301 23.999 7.555   1.00 62.55  ? 119 TYR A CA  1 
ATOM   916  C  C   . TYR A 1 119 ? -53.520 24.899 7.711   1.00 59.91  ? 119 TYR A C   1 
ATOM   917  O  O   . TYR A 1 119 ? -53.428 26.125 7.564   1.00 58.91  ? 119 TYR A O   1 
ATOM   918  C  CB  . TYR A 1 119 ? -50.996 24.786 7.682   1.00 59.11  ? 119 TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 119 ? -49.787 24.004 7.214   1.00 62.81  ? 119 TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 119 ? -49.339 22.896 7.921   1.00 60.94  ? 119 TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 119 ? -49.100 24.367 6.063   1.00 64.96  ? 119 TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 119 ? -48.242 22.173 7.495   1.00 62.83  ? 119 TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 119 ? -47.997 23.650 5.631   1.00 63.91  ? 119 TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 119 ? -47.573 22.554 6.353   1.00 63.98  ? 119 TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 119 ? -46.479 21.834 5.931   1.00 69.26  ? 119 TYR A OH  1 
ATOM   926  N  N   . PRO A 1 120 ? -54.686 24.320 8.019   1.00 59.05  ? 120 PRO A N   1 
ATOM   927  C  CA  . PRO A 1 120 ? -55.911 25.131 8.114   1.00 59.54  ? 120 PRO A CA  1 
ATOM   928  C  C   . PRO A 1 120 ? -55.984 26.010 9.354   1.00 57.68  ? 120 PRO A C   1 
ATOM   929  O  O   . PRO A 1 120 ? -56.852 26.892 9.406   1.00 58.55  ? 120 PRO A O   1 
ATOM   930  C  CB  . PRO A 1 120 ? -57.026 24.078 8.113   1.00 56.89  ? 120 PRO A CB  1 
ATOM   931  C  CG  . PRO A 1 120 ? -56.385 22.864 8.693   1.00 57.35  ? 120 PRO A CG  1 
ATOM   932  C  CD  . PRO A 1 120 ? -54.950 22.887 8.240   1.00 58.35  ? 120 PRO A CD  1 
ATOM   933  N  N   . THR A 1 121 ? -55.125 25.801 10.349  1.00 62.18  ? 121 THR A N   1 
ATOM   934  C  CA  . THR A 1 121 ? -55.065 26.661 11.523  1.00 60.88  ? 121 THR A CA  1 
ATOM   935  C  C   . THR A 1 121 ? -53.614 27.021 11.813  1.00 60.09  ? 121 THR A C   1 
ATOM   936  O  O   . THR A 1 121 ? -52.682 26.366 11.338  1.00 64.74  ? 121 THR A O   1 
ATOM   937  C  CB  . THR A 1 121 ? -55.684 26.000 12.768  1.00 60.23  ? 121 THR A CB  1 
ATOM   938  O  OG1 . THR A 1 121 ? -54.962 24.804 13.090  1.00 62.60  ? 121 THR A OG1 1 
ATOM   939  C  CG2 . THR A 1 121 ? -57.148 25.659 12.535  1.00 53.64  ? 121 THR A CG2 1 
ATOM   940  N  N   . VAL A 1 122 ? -53.435 28.082 12.605  1.00 60.90  ? 122 VAL A N   1 
ATOM   941  C  CA  . VAL A 1 122 ? -52.098 28.452 13.066  1.00 63.28  ? 122 VAL A CA  1 
ATOM   942  C  C   . VAL A 1 122 ? -51.512 27.342 13.925  1.00 62.74  ? 122 VAL A C   1 
ATOM   943  O  O   . VAL A 1 122 ? -50.300 27.085 13.900  1.00 62.25  ? 122 VAL A O   1 
ATOM   944  C  CB  . VAL A 1 122 ? -52.148 29.792 13.826  1.00 58.69  ? 122 VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 122 ? -50.830 30.063 14.537  1.00 57.35  ? 122 VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 122 ? -52.477 30.925 12.872  1.00 57.37  ? 122 VAL A CG2 1 
ATOM   947  N  N   A GLU A 1 123 ? -52.362 26.660 14.695  0.63 61.02  ? 123 GLU A N   1 
ATOM   948  N  N   B GLU A 1 123 ? -52.358 26.666 14.708  0.37 61.35  ? 123 GLU A N   1 
ATOM   949  C  CA  A GLU A 1 123 ? -51.893 25.572 15.544  0.63 65.62  ? 123 GLU A CA  1 
ATOM   950  C  CA  B GLU A 1 123 ? -51.878 25.571 15.546  0.37 65.39  ? 123 GLU A CA  1 
ATOM   951  C  C   A GLU A 1 123 ? -51.347 24.418 14.713  0.63 63.18  ? 123 GLU A C   1 
ATOM   952  C  C   B GLU A 1 123 ? -51.332 24.426 14.703  0.37 62.11  ? 123 GLU A C   1 
ATOM   953  O  O   A GLU A 1 123 ? -50.351 23.789 15.088  0.63 62.58  ? 123 GLU A O   1 
ATOM   954  O  O   B GLU A 1 123 ? -50.323 23.807 15.062  0.37 61.62  ? 123 GLU A O   1 
ATOM   955  C  CB  A GLU A 1 123 ? -53.032 25.096 16.447  0.63 68.81  ? 123 GLU A CB  1 
ATOM   956  C  CB  B GLU A 1 123 ? -52.999 25.074 16.459  0.37 70.10  ? 123 GLU A CB  1 
ATOM   957  C  CG  A GLU A 1 123 ? -52.609 24.150 17.551  0.63 68.79  ? 123 GLU A CG  1 
ATOM   958  C  CG  B GLU A 1 123 ? -53.115 25.830 17.772  0.37 68.39  ? 123 GLU A CG  1 
ATOM   959  C  CD  A GLU A 1 123 ? -51.871 24.851 18.676  0.63 71.40  ? 123 GLU A CD  1 
ATOM   960  C  CD  B GLU A 1 123 ? -54.188 25.258 18.676  0.37 70.82  ? 123 GLU A CD  1 
ATOM   961  O  OE1 A GLU A 1 123 ? -51.804 26.099 18.667  0.63 68.04  ? 123 GLU A OE1 1 
ATOM   962  O  OE1 B GLU A 1 123 ? -55.023 24.469 18.184  0.37 71.83  ? 123 GLU A OE1 1 
ATOM   963  O  OE2 A GLU A 1 123 ? -51.361 24.152 19.576  0.63 70.54  ? 123 GLU A OE2 1 
ATOM   964  O  OE2 B GLU A 1 123 ? -54.197 25.593 19.879  0.37 72.41  ? 123 GLU A OE2 1 
ATOM   965  N  N   . ALA A 1 124 ? -51.984 24.129 13.576  1.00 61.41  ? 124 ALA A N   1 
ATOM   966  C  CA  . ALA A 1 124 ? -51.509 23.050 12.715  1.00 62.48  ? 124 ALA A CA  1 
ATOM   967  C  C   . ALA A 1 124 ? -50.187 23.415 12.049  1.00 62.37  ? 124 ALA A C   1 
ATOM   968  O  O   . ALA A 1 124 ? -49.325 22.550 11.851  1.00 62.95  ? 124 ALA A O   1 
ATOM   969  C  CB  . ALA A 1 124 ? -52.567 22.713 11.664  1.00 63.76  ? 124 ALA A CB  1 
ATOM   970  N  N   . TYR A 1 125 ? -50.010 24.690 11.696  1.00 60.16  ? 125 TYR A N   1 
ATOM   971  C  CA  . TYR A 1 125 ? -48.743 25.133 11.122  1.00 59.93  ? 125 TYR A CA  1 
ATOM   972  C  C   . TYR A 1 125 ? -47.640 25.146 12.170  1.00 58.60  ? 125 TYR A C   1 
ATOM   973  O  O   . TYR A 1 125 ? -46.478 24.855 11.863  1.00 59.80  ? 125 TYR A O   1 
ATOM   974  C  CB  . TYR A 1 125 ? -48.910 26.520 10.499  1.00 57.53  ? 125 TYR A CB  1 
ATOM   975  C  CG  . TYR A 1 125 ? -47.647 27.092 9.890   1.00 56.77  ? 125 TYR A CG  1 
ATOM   976  C  CD1 . TYR A 1 125 ? -47.159 26.615 8.681   1.00 57.84  ? 125 TYR A CD1 1 
ATOM   977  C  CD2 . TYR A 1 125 ? -46.953 28.121 10.515  1.00 57.44  ? 125 TYR A CD2 1 
ATOM   978  C  CE1 . TYR A 1 125 ? -46.011 27.137 8.116   1.00 58.40  ? 125 TYR A CE1 1 
ATOM   979  C  CE2 . TYR A 1 125 ? -45.802 28.651 9.956   1.00 55.87  ? 125 TYR A CE2 1 
ATOM   980  C  CZ  . TYR A 1 125 ? -45.337 28.155 8.756   1.00 57.69  ? 125 TYR A CZ  1 
ATOM   981  O  OH  . TYR A 1 125 ? -44.194 28.675 8.192   1.00 58.35  ? 125 TYR A OH  1 
ATOM   982  N  N   . ALA A 1 126 ? -47.987 25.481 13.414  1.00 57.86  ? 126 ALA A N   1 
ATOM   983  C  CA  . ALA A 1 126 ? -46.993 25.534 14.482  1.00 58.06  ? 126 ALA A CA  1 
ATOM   984  C  C   . ALA A 1 126 ? -46.410 24.155 14.759  1.00 62.92  ? 126 ALA A C   1 
ATOM   985  O  O   . ALA A 1 126 ? -45.191 23.999 14.901  1.00 62.66  ? 126 ALA A O   1 
ATOM   986  C  CB  . ALA A 1 126 ? -47.622 26.117 15.747  1.00 58.94  ? 126 ALA A CB  1 
ATOM   987  N  N   . HIS A 1 127 ? -47.272 23.138 14.836  1.00 64.35  ? 127 HIS A N   1 
ATOM   988  C  CA  . HIS A 1 127 ? -46.803 21.784 15.112  1.00 68.39  ? 127 HIS A CA  1 
ATOM   989  C  C   . HIS A 1 127 ? -46.016 21.210 13.942  1.00 69.12  ? 127 HIS A C   1 
ATOM   990  O  O   . HIS A 1 127 ? -45.114 20.389 14.146  1.00 69.60  ? 127 HIS A O   1 
ATOM   991  C  CB  . HIS A 1 127 ? -47.988 20.884 15.451  1.00 72.77  ? 127 HIS A CB  1 
ATOM   992  C  CG  . HIS A 1 127 ? -48.783 21.358 16.627  1.00 73.00  ? 127 HIS A CG  1 
ATOM   993  N  ND1 . HIS A 1 127 ? -48.206 21.989 17.708  1.00 72.58  ? 127 HIS A ND1 1 
ATOM   994  C  CD2 . HIS A 1 127 ? -50.110 21.301 16.889  1.00 76.45  ? 127 HIS A CD2 1 
ATOM   995  C  CE1 . HIS A 1 127 ? -49.143 22.296 18.588  1.00 71.59  ? 127 HIS A CE1 1 
ATOM   996  N  NE2 . HIS A 1 127 ? -50.307 21.889 18.115  1.00 78.11  ? 127 HIS A NE2 1 
ATOM   997  N  N   . ALA A 1 128 ? -46.340 21.622 12.715  1.00 61.20  ? 128 ALA A N   1 
ATOM   998  C  CA  . ALA A 1 128 ? -45.570 21.170 11.563  1.00 59.84  ? 128 ALA A CA  1 
ATOM   999  C  C   . ALA A 1 128 ? -44.172 21.773 11.558  1.00 60.73  ? 128 ALA A C   1 
ATOM   1000 O  O   . ALA A 1 128 ? -43.220 21.125 11.107  1.00 59.43  ? 128 ALA A O   1 
ATOM   1001 C  CB  . ALA A 1 128 ? -46.306 21.513 10.270  1.00 57.81  ? 128 ALA A CB  1 
ATOM   1002 N  N   . VAL A 1 129 ? -44.028 23.006 12.048  1.00 62.40  ? 129 VAL A N   1 
ATOM   1003 C  CA  . VAL A 1 129 ? -42.701 23.593 12.207  1.00 61.29  ? 129 VAL A CA  1 
ATOM   1004 C  C   . VAL A 1 129 ? -41.920 22.846 13.280  1.00 60.32  ? 129 VAL A C   1 
ATOM   1005 O  O   . VAL A 1 129 ? -40.748 22.500 13.092  1.00 60.53  ? 129 VAL A O   1 
ATOM   1006 C  CB  . VAL A 1 129 ? -42.809 25.092 12.539  1.00 58.42  ? 129 VAL A CB  1 
ATOM   1007 C  CG1 . VAL A 1 129 ? -41.438 25.662 12.874  1.00 55.79  ? 129 VAL A CG1 1 
ATOM   1008 C  CG2 . VAL A 1 129 ? -43.437 25.853 11.383  1.00 56.88  ? 129 VAL A CG2 1 
ATOM   1009 N  N   . GLU A 1 130 ? -42.561 22.589 14.423  1.00 60.04  ? 130 GLU A N   1 
ATOM   1010 C  CA  . GLU A 1 130 ? -41.895 21.876 15.509  1.00 59.96  ? 130 GLU A CA  1 
ATOM   1011 C  C   . GLU A 1 130 ? -41.478 20.477 15.077  1.00 62.77  ? 130 GLU A C   1 
ATOM   1012 O  O   . GLU A 1 130 ? -40.425 19.977 15.493  1.00 62.60  ? 130 GLU A O   1 
ATOM   1013 C  CB  . GLU A 1 130 ? -42.816 21.808 16.728  1.00 64.16  ? 130 GLU A CB  1 
ATOM   1014 C  CG  . GLU A 1 130 ? -43.205 23.166 17.286  1.00 65.05  ? 130 GLU A CG  1 
ATOM   1015 C  CD  . GLU A 1 130 ? -44.385 23.091 18.235  1.00 78.34  ? 130 GLU A CD  1 
ATOM   1016 O  OE1 . GLU A 1 130 ? -44.943 21.987 18.409  1.00 68.84  ? 130 GLU A OE1 1 
ATOM   1017 O  OE2 . GLU A 1 130 ? -44.759 24.138 18.804  1.00 77.74  ? 130 GLU A OE2 1 
ATOM   1018 N  N   . ALA A 1 131 ? -42.289 19.830 14.238  1.00 63.74  ? 131 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 131 ? -41.950 18.493 13.764  1.00 65.41  ? 131 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 131 ? -40.804 18.536 12.760  1.00 62.08  ? 131 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 131 ? -39.957 17.636 12.738  1.00 65.06  ? 131 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 131 ? -43.180 17.827 13.148  1.00 68.25  ? 131 ALA A CB  1 
ATOM   1023 N  N   . ALA A 1 132 ? -40.762 19.574 11.921  1.00 63.59  ? 132 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 132 ? -39.676 19.707 10.959  1.00 64.90  ? 132 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 132 ? -38.342 20.001 11.631  1.00 65.23  ? 132 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 132 ? -37.293 19.712 11.046  1.00 67.07  ? 132 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 132 ? -40.000 20.805 9.945   1.00 66.97  ? 132 ALA A CB  1 
ATOM   1028 N  N   . ARG A 1 133 ? -38.364 20.559 12.844  1.00 62.66  ? 133 ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 133 ? -37.175 20.904 13.616  1.00 59.92  ? 133 ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 133 ? -36.244 21.788 12.793  1.00 61.33  ? 133 ARG A C   1 
ATOM   1031 O  O   . ARG A 1 133 ? -35.171 21.338 12.371  1.00 63.03  ? 133 ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 133 ? -36.452 19.639 14.083  1.00 62.17  ? 133 ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 133 ? -37.377 18.623 14.739  1.00 67.02  ? 133 ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 133 ? -36.614 17.523 15.463  1.00 73.18  ? 133 ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 133 ? -35.755 16.751 14.572  1.00 78.04  ? 133 ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 133 ? -34.429 16.807 14.576  1.00 82.26  ? 133 ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 133 ? -33.772 17.585 15.420  1.00 83.17  ? 133 ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 133 ? -33.746 16.057 13.716  1.00 74.84  ? 133 ARG A NH2 1 
ATOM   1039 N  N   . PRO A 1 134 ? -36.614 23.040 12.546  1.00 61.37  ? 134 PRO A N   1 
ATOM   1040 C  CA  . PRO A 1 134 ? -35.779 23.915 11.720  1.00 60.70  ? 134 PRO A CA  1 
ATOM   1041 C  C   . PRO A 1 134 ? -34.590 24.451 12.507  1.00 62.09  ? 134 PRO A C   1 
ATOM   1042 O  O   . PRO A 1 134 ? -34.508 24.335 13.730  1.00 60.13  ? 134 PRO A O   1 
ATOM   1043 C  CB  . PRO A 1 134 ? -36.739 25.041 11.331  1.00 58.87  ? 134 PRO A CB  1 
ATOM   1044 C  CG  . PRO A 1 134 ? -37.661 25.137 12.499  1.00 57.76  ? 134 PRO A CG  1 
ATOM   1045 C  CD  . PRO A 1 134 ? -37.821 23.732 13.032  1.00 58.74  ? 134 PRO A CD  1 
ATOM   1046 N  N   . SER A 1 135 ? -33.658 25.049 11.770  1.00 62.55  ? 135 SER A N   1 
ATOM   1047 C  CA  . SER A 1 135 ? -32.487 25.666 12.374  1.00 62.07  ? 135 SER A CA  1 
ATOM   1048 C  C   . SER A 1 135 ? -32.735 27.097 12.830  1.00 59.17  ? 135 SER A C   1 
ATOM   1049 O  O   . SER A 1 135 ? -31.864 27.680 13.482  1.00 59.55  ? 135 SER A O   1 
ATOM   1050 C  CB  . SER A 1 135 ? -31.309 25.639 11.394  1.00 58.64  ? 135 SER A CB  1 
ATOM   1051 O  OG  . SER A 1 135 ? -30.937 24.308 11.077  1.00 61.56  ? 135 SER A OG  1 
ATOM   1052 N  N   . LEU A 1 136 ? -33.893 27.673 12.513  1.00 57.74  ? 136 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 136 ? -34.197 29.052 12.868  1.00 55.45  ? 136 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 136 ? -35.640 29.153 13.346  1.00 55.00  ? 136 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 136 ? -36.475 28.293 13.057  1.00 54.76  ? 136 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 136 ? -33.948 30.004 11.683  1.00 54.61  ? 136 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 136 ? -34.353 29.539 10.278  1.00 56.91  ? 136 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 136 ? -35.859 29.622 10.059  1.00 68.13  ? 136 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 136 ? -33.610 30.329 9.205   1.00 59.43  ? 136 LEU A CD2 1 
ATOM   1060 N  N   . ASN A 1 137 ? -35.922 30.224 14.083  1.00 51.69  ? 137 ASN A N   1 
ATOM   1061 C  CA  . ASN A 1 137 ? -37.268 30.458 14.584  1.00 52.59  ? 137 ASN A CA  1 
ATOM   1062 C  C   . ASN A 1 137 ? -38.191 30.907 13.454  1.00 50.66  ? 137 ASN A C   1 
ATOM   1063 O  O   . ASN A 1 137 ? -37.753 31.486 12.457  1.00 50.63  ? 137 ASN A O   1 
ATOM   1064 C  CB  . ASN A 1 137 ? -37.246 31.505 15.699  1.00 51.00  ? 137 ASN A CB  1 
ATOM   1065 C  CG  . ASN A 1 137 ? -36.379 31.088 16.873  1.00 51.25  ? 137 ASN A CG  1 
ATOM   1066 O  OD1 . ASN A 1 137 ? -36.505 29.977 17.390  1.00 53.07  ? 137 ASN A OD1 1 
ATOM   1067 N  ND2 . ASN A 1 137 ? -35.485 31.976 17.294  1.00 53.98  ? 137 ASN A ND2 1 
ATOM   1068 N  N   . VAL A 1 138 ? -39.483 30.629 13.617  1.00 52.09  ? 138 VAL A N   1 
ATOM   1069 C  CA  . VAL A 1 138 ? -40.482 30.906 12.590  1.00 49.53  ? 138 VAL A CA  1 
ATOM   1070 C  C   . VAL A 1 138 ? -41.683 31.581 13.240  1.00 54.03  ? 138 VAL A C   1 
ATOM   1071 O  O   . VAL A 1 138 ? -42.289 31.025 14.164  1.00 51.65  ? 138 VAL A O   1 
ATOM   1072 C  CB  . VAL A 1 138 ? -40.920 29.630 11.850  1.00 48.79  ? 138 VAL A CB  1 
ATOM   1073 C  CG1 . VAL A 1 138 ? -42.107 29.923 10.943  1.00 53.95  ? 138 VAL A CG1 1 
ATOM   1074 C  CG2 . VAL A 1 138 ? -39.765 29.060 11.044  1.00 55.44  ? 138 VAL A CG2 1 
ATOM   1075 N  N   . GLY A 1 139 ? -42.016 32.776 12.763  1.00 49.59  ? 139 GLY A N   1 
ATOM   1076 C  CA  . GLY A 1 139 ? -43.265 33.426 13.107  1.00 47.93  ? 139 GLY A CA  1 
ATOM   1077 C  C   . GLY A 1 139 ? -44.007 33.772 11.830  1.00 50.66  ? 139 GLY A C   1 
ATOM   1078 O  O   . GLY A 1 139 ? -43.396 34.070 10.804  1.00 52.56  ? 139 GLY A O   1 
ATOM   1079 N  N   . THR A 1 140 ? -45.334 33.721 11.895  1.00 49.13  ? 140 THR A N   1 
ATOM   1080 C  CA  . THR A 1 140 ? -46.151 33.850 10.698  1.00 53.34  ? 140 THR A CA  1 
ATOM   1081 C  C   . THR A 1 140 ? -47.159 34.983 10.834  1.00 50.30  ? 140 THR A C   1 
ATOM   1082 O  O   . THR A 1 140 ? -47.694 35.235 11.919  1.00 50.90  ? 140 THR A O   1 
ATOM   1083 C  CB  . THR A 1 140 ? -46.889 32.539 10.380  1.00 51.44  ? 140 THR A CB  1 
ATOM   1084 O  OG1 . THR A 1 140 ? -47.626 32.690 9.160   1.00 51.71  ? 140 THR A OG1 1 
ATOM   1085 C  CG2 . THR A 1 140 ? -47.844 32.159 11.503  1.00 49.46  ? 140 THR A CG2 1 
ATOM   1086 N  N   . LEU A 1 141 ? -47.387 35.674 9.723   1.00 51.24  ? 141 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 141 ? -48.533 36.548 9.555   1.00 50.94  ? 141 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 141 ? -49.651 35.779 8.857   1.00 51.85  ? 141 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 141 ? -49.454 34.673 8.350   1.00 51.80  ? 141 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 141 ? -48.151 37.791 8.748   1.00 51.12  ? 141 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 141 ? -47.070 38.718 9.304   1.00 50.51  ? 141 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 141 ? -46.570 39.658 8.218   1.00 50.95  ? 141 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 141 ? -47.598 39.510 10.486  1.00 50.14  ? 141 LEU A CD2 1 
ATOM   1094 N  N   . ILE A 1 142 ? -50.839 36.372 8.832   1.00 50.31  ? 142 ILE A N   1 
ATOM   1095 C  CA  . ILE A 1 142 ? -51.979 35.800 8.127   1.00 55.07  ? 142 ILE A CA  1 
ATOM   1096 C  C   . ILE A 1 142 ? -52.180 36.574 6.834   1.00 53.96  ? 142 ILE A C   1 
ATOM   1097 O  O   . ILE A 1 142 ? -52.282 37.808 6.847   1.00 52.81  ? 142 ILE A O   1 
ATOM   1098 C  CB  . ILE A 1 142 ? -53.248 35.828 8.993   1.00 56.72  ? 142 ILE A CB  1 
ATOM   1099 C  CG1 . ILE A 1 142 ? -53.021 35.043 10.286  1.00 53.28  ? 142 ILE A CG1 1 
ATOM   1100 C  CG2 . ILE A 1 142 ? -54.427 35.254 8.221   1.00 53.51  ? 142 ILE A CG2 1 
ATOM   1101 C  CD1 . ILE A 1 142 ? -52.550 33.621 10.065  1.00 54.73  ? 142 ILE A CD1 1 
ATOM   1102 N  N   . GLY A 1 143 ? -52.229 35.852 5.716   1.00 55.68  ? 143 GLY A N   1 
ATOM   1103 C  CA  . GLY A 1 143 ? -52.353 36.494 4.420   1.00 62.47  ? 143 GLY A CA  1 
ATOM   1104 C  C   . GLY A 1 143 ? -53.796 36.828 4.095   1.00 63.08  ? 143 GLY A C   1 
ATOM   1105 O  O   . GLY A 1 143 ? -54.676 35.961 4.147   1.00 60.47  ? 143 GLY A O   1 
ATOM   1106 N  N   . HIS A 1 144 ? -54.041 38.097 3.756   1.00 55.46  ? 144 HIS A N   1 
ATOM   1107 C  CA  . HIS A 1 144 ? -55.390 38.527 3.400   1.00 57.55  ? 144 HIS A CA  1 
ATOM   1108 C  C   . HIS A 1 144 ? -55.913 37.763 2.190   1.00 61.54  ? 144 HIS A C   1 
ATOM   1109 O  O   . HIS A 1 144 ? -57.066 37.314 2.181   1.00 59.89  ? 144 HIS A O   1 
ATOM   1110 C  CB  . HIS A 1 144 ? -55.403 40.032 3.131   1.00 56.52  ? 144 HIS A CB  1 
ATOM   1111 C  CG  . HIS A 1 144 ? -56.687 40.533 2.545   1.00 60.63  ? 144 HIS A CG  1 
ATOM   1112 N  ND1 . HIS A 1 144 ? -56.731 41.537 1.602   1.00 61.74  ? 144 HIS A ND1 1 
ATOM   1113 C  CD2 . HIS A 1 144 ? -57.972 40.173 2.772   1.00 64.06  ? 144 HIS A CD2 1 
ATOM   1114 C  CE1 . HIS A 1 144 ? -57.988 41.771 1.270   1.00 61.74  ? 144 HIS A CE1 1 
ATOM   1115 N  NE2 . HIS A 1 144 ? -58.761 40.957 1.965   1.00 62.00  ? 144 HIS A NE2 1 
ATOM   1116 N  N   . THR A 1 145 ? -55.079 37.606 1.159   1.00 58.49  ? 145 THR A N   1 
ATOM   1117 C  CA  . THR A 1 145 ? -55.507 36.879 -0.031  1.00 60.94  ? 145 THR A CA  1 
ATOM   1118 C  C   . THR A 1 145 ? -55.839 35.427 0.292   1.00 61.81  ? 145 THR A C   1 
ATOM   1119 O  O   . THR A 1 145 ? -56.715 34.834 -0.347  1.00 65.54  ? 145 THR A O   1 
ATOM   1120 C  CB  . THR A 1 145 ? -54.426 36.956 -1.111  1.00 65.30  ? 145 THR A CB  1 
ATOM   1121 O  OG1 . THR A 1 145 ? -54.011 38.318 -1.278  1.00 59.21  ? 145 THR A OG1 1 
ATOM   1122 C  CG2 . THR A 1 145 ? -54.951 36.429 -2.432  1.00 62.74  ? 145 THR A CG2 1 
ATOM   1123 N  N   . ALA A 1 146 ? -55.162 34.843 1.283   1.00 66.63  ? 146 ALA A N   1 
ATOM   1124 C  CA  . ALA A 1 146 ? -55.504 33.489 1.705   1.00 65.64  ? 146 ALA A CA  1 
ATOM   1125 C  C   . ALA A 1 146 ? -56.846 33.459 2.425   1.00 69.01  ? 146 ALA A C   1 
ATOM   1126 O  O   . ALA A 1 146 ? -57.627 32.516 2.255   1.00 68.04  ? 146 ALA A O   1 
ATOM   1127 C  CB  . ALA A 1 146 ? -54.401 32.919 2.596   1.00 65.58  ? 146 ALA A CB  1 
ATOM   1128 N  N   . LEU A 1 147 ? -57.132 34.484 3.232   1.00 67.16  ? 147 LEU A N   1 
ATOM   1129 C  CA  . LEU A 1 147 ? -58.424 34.554 3.908   1.00 66.32  ? 147 LEU A CA  1 
ATOM   1130 C  C   . LEU A 1 147 ? -59.559 34.738 2.909   1.00 71.87  ? 147 LEU A C   1 
ATOM   1131 O  O   . LEU A 1 147 ? -60.652 34.189 3.095   1.00 72.39  ? 147 LEU A O   1 
ATOM   1132 C  CB  . LEU A 1 147 ? -58.423 35.685 4.939   1.00 64.98  ? 147 LEU A CB  1 
ATOM   1133 C  CG  . LEU A 1 147 ? -57.601 35.479 6.216   1.00 62.20  ? 147 LEU A CG  1 
ATOM   1134 C  CD1 . LEU A 1 147 ? -57.716 36.687 7.138   1.00 59.05  ? 147 LEU A CD1 1 
ATOM   1135 C  CD2 . LEU A 1 147 ? -58.031 34.210 6.939   1.00 62.98  ? 147 LEU A CD2 1 
ATOM   1136 N  N   . ARG A 1 148 ? -59.319 35.502 1.840   1.00 66.67  ? 148 ARG A N   1 
ATOM   1137 C  CA  . ARG A 1 148 ? -60.340 35.678 0.812   1.00 67.09  ? 148 ARG A CA  1 
ATOM   1138 C  C   . ARG A 1 148 ? -60.690 34.347 0.160   1.00 71.15  ? 148 ARG A C   1 
ATOM   1139 O  O   . ARG A 1 148 ? -61.869 34.003 0.013   1.00 74.91  ? 148 ARG A O   1 
ATOM   1140 C  CB  . ARG A 1 148 ? -59.857 36.678 -0.238  1.00 66.59  ? 148 ARG A CB  1 
ATOM   1141 C  CG  . ARG A 1 148 ? -59.636 38.072 0.307   1.00 64.43  ? 148 ARG A CG  1 
ATOM   1142 C  CD  . ARG A 1 148 ? -59.138 39.020 -0.768  1.00 63.77  ? 148 ARG A CD  1 
ATOM   1143 N  NE  . ARG A 1 148 ? -60.083 40.097 -1.041  1.00 70.77  ? 148 ARG A NE  1 
ATOM   1144 C  CZ  . ARG A 1 148 ? -60.835 40.178 -2.130  1.00 73.85  ? 148 ARG A CZ  1 
ATOM   1145 N  NH1 . ARG A 1 148 ? -60.786 39.253 -3.075  1.00 74.10  ? 148 ARG A NH1 1 
ATOM   1146 N  NH2 . ARG A 1 148 ? -61.650 41.218 -2.280  1.00 72.65  ? 148 ARG A NH2 1 
ATOM   1147 N  N   . ASN A 1 149 ? -59.671 33.576 -0.224  1.00 70.14  ? 149 ASN A N   1 
ATOM   1148 C  CA  . ASN A 1 149 ? -59.900 32.322 -0.929  1.00 73.45  ? 149 ASN A CA  1 
ATOM   1149 C  C   . ASN A 1 149 ? -60.612 31.292 -0.062  1.00 71.25  ? 149 ASN A C   1 
ATOM   1150 O  O   . ASN A 1 149 ? -61.241 30.375 -0.600  1.00 78.32  ? 149 ASN A O   1 
ATOM   1151 C  CB  . ASN A 1 149 ? -58.570 31.766 -1.437  1.00 69.66  ? 149 ASN A CB  1 
ATOM   1152 C  CG  . ASN A 1 149 ? -58.751 30.644 -2.435  1.00 74.03  ? 149 ASN A CG  1 
ATOM   1153 O  OD1 . ASN A 1 149 ? -58.385 29.499 -2.173  1.00 76.26  ? 149 ASN A OD1 1 
ATOM   1154 N  ND2 . ASN A 1 149 ? -59.327 30.966 -3.586  1.00 79.68  ? 149 ASN A ND2 1 
ATOM   1155 N  N   . ASN A 1 150 ? -60.533 31.423 1.263   1.00 71.03  ? 150 ASN A N   1 
ATOM   1156 C  CA  . ASN A 1 150 ? -61.238 30.509 2.150   1.00 75.28  ? 150 ASN A CA  1 
ATOM   1157 C  C   . ASN A 1 150 ? -62.723 30.824 2.261   1.00 72.55  ? 150 ASN A C   1 
ATOM   1158 O  O   . ASN A 1 150 ? -63.497 29.950 2.663   1.00 74.97  ? 150 ASN A O   1 
ATOM   1159 C  CB  . ASN A 1 150 ? -60.614 30.535 3.548   1.00 70.21  ? 150 ASN A CB  1 
ATOM   1160 C  CG  . ASN A 1 150 ? -59.148 30.151 3.543   1.00 70.05  ? 150 ASN A CG  1 
ATOM   1161 O  OD1 . ASN A 1 150 ? -58.687 29.418 2.668   1.00 68.98  ? 150 ASN A OD1 1 
ATOM   1162 N  ND2 . ASN A 1 150 ? -58.405 30.646 4.526   1.00 65.39  ? 150 ASN A ND2 1 
ATOM   1163 N  N   . HIS A 1 151 ? -63.141 32.045 1.915   1.00 69.42  ? 151 HIS A N   1 
ATOM   1164 C  CA  . HIS A 1 151 ? -64.526 32.456 2.099   1.00 73.20  ? 151 HIS A CA  1 
ATOM   1165 C  C   . HIS A 1 151 ? -65.219 32.955 0.839   1.00 73.69  ? 151 HIS A C   1 
ATOM   1166 O  O   . HIS A 1 151 ? -66.421 33.237 0.899   1.00 75.13  ? 151 HIS A O   1 
ATOM   1167 C  CB  . HIS A 1 151 ? -64.621 33.555 3.170   1.00 67.45  ? 151 HIS A CB  1 
ATOM   1168 C  CG  . HIS A 1 151 ? -64.136 33.127 4.520   1.00 67.01  ? 151 HIS A CG  1 
ATOM   1169 N  ND1 . HIS A 1 151 ? -64.963 32.554 5.463   1.00 68.64  ? 151 HIS A ND1 1 
ATOM   1170 C  CD2 . HIS A 1 151 ? -62.909 33.191 5.088   1.00 65.96  ? 151 HIS A CD2 1 
ATOM   1171 C  CE1 . HIS A 1 151 ? -64.266 32.283 6.551   1.00 64.35  ? 151 HIS A CE1 1 
ATOM   1172 N  NE2 . HIS A 1 151 ? -63.016 32.661 6.350   1.00 63.82  ? 151 HIS A NE2 1 
ATOM   1173 N  N   . MET A 1 152 ? -64.523 33.074 -0.288  1.00 73.30  ? 152 MET A N   1 
ATOM   1174 C  CA  . MET A 1 152 ? -65.110 33.609 -1.507  1.00 76.47  ? 152 MET A CA  1 
ATOM   1175 C  C   . MET A 1 152 ? -65.054 32.574 -2.623  1.00 82.62  ? 152 MET A C   1 
ATOM   1176 O  O   . MET A 1 152 ? -64.129 31.760 -2.693  1.00 81.67  ? 152 MET A O   1 
ATOM   1177 C  CB  . MET A 1 152 ? -64.393 34.893 -1.952  1.00 74.53  ? 152 MET A CB  1 
ATOM   1178 C  CG  . MET A 1 152 ? -64.548 36.054 -0.981  1.00 75.07  ? 152 MET A CG  1 
ATOM   1179 S  SD  . MET A 1 152 ? -63.364 37.391 -1.249  1.00 76.70  ? 152 MET A SD  1 
ATOM   1180 C  CE  . MET A 1 152 ? -63.846 37.977 -2.871  1.00 74.27  ? 152 MET A CE  1 
ATOM   1181 N  N   . ASP A 1 153 ? -66.065 32.610 -3.495  1.00 83.21  ? 153 ASP A N   1 
ATOM   1182 C  CA  . ASP A 1 153 ? -66.051 31.755 -4.678  1.00 82.96  ? 153 ASP A CA  1 
ATOM   1183 C  C   . ASP A 1 153 ? -65.048 32.269 -5.704  1.00 83.08  ? 153 ASP A C   1 
ATOM   1184 O  O   . ASP A 1 153 ? -64.197 31.514 -6.189  1.00 90.18  ? 153 ASP A O   1 
ATOM   1185 C  CB  . ASP A 1 153 ? -67.456 31.666 -5.274  1.00 85.47  ? 153 ASP A CB  1 
ATOM   1186 C  CG  . ASP A 1 153 ? -68.468 31.094 -4.296  1.00 93.54  ? 153 ASP A CG  1 
ATOM   1187 O  OD1 . ASP A 1 153 ? -68.127 30.127 -3.582  1.00 99.67  ? 153 ASP A OD1 1 
ATOM   1188 O  OD2 . ASP A 1 153 ? -69.602 31.615 -4.236  1.00 102.86 ? 153 ASP A OD2 1 
ATOM   1189 N  N   . ASP A 1 154 ? -65.134 33.552 -6.049  1.00 83.10  ? 154 ASP A N   1 
ATOM   1190 C  CA  A ASP A 1 154 ? -64.150 34.193 -6.905  0.45 82.64  ? 154 ASP A CA  1 
ATOM   1191 C  CA  B ASP A 1 154 ? -64.177 34.217 -6.922  0.55 82.65  ? 154 ASP A CA  1 
ATOM   1192 C  C   . ASP A 1 154 ? -63.529 35.373 -6.171  1.00 79.96  ? 154 ASP A C   1 
ATOM   1193 O  O   . ASP A 1 154 ? -64.173 36.032 -5.350  1.00 78.79  ? 154 ASP A O   1 
ATOM   1194 C  CB  A ASP A 1 154 ? -64.763 34.649 -8.240  0.45 84.47  ? 154 ASP A CB  1 
ATOM   1195 C  CB  B ASP A 1 154 ? -64.849 34.737 -8.202  0.55 84.59  ? 154 ASP A CB  1 
ATOM   1196 C  CG  A ASP A 1 154 ? -66.047 35.431 -8.062  0.45 83.00  ? 154 ASP A CG  1 
ATOM   1197 C  CG  B ASP A 1 154 ? -65.387 33.619 -9.078  0.55 83.81  ? 154 ASP A CG  1 
ATOM   1198 O  OD1 A ASP A 1 154 ? -66.460 35.651 -6.908  0.45 81.08  ? 154 ASP A OD1 1 
ATOM   1199 O  OD1 B ASP A 1 154 ? -65.163 32.437 -8.746  0.55 83.06  ? 154 ASP A OD1 1 
ATOM   1200 O  OD2 A ASP A 1 154 ? -66.649 35.824 -9.084  0.45 84.51  ? 154 ASP A OD2 1 
ATOM   1201 O  OD2 B ASP A 1 154 ? -66.035 33.925 -10.101 0.55 81.60  ? 154 ASP A OD2 1 
ATOM   1202 N  N   . LEU A 1 155 ? -62.255 35.623 -6.462  1.00 80.32  ? 155 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 155 ? -61.479 36.640 -5.763  1.00 81.35  ? 155 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 155 ? -61.444 37.978 -6.485  1.00 79.71  ? 155 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 155 ? -60.822 38.920 -5.985  1.00 78.35  ? 155 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 155 ? -60.048 36.142 -5.546  1.00 77.31  ? 155 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 155 ? -59.937 34.717 -5.006  1.00 76.50  ? 155 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 155 ? -58.485 34.278 -4.957  1.00 75.24  ? 155 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 155 ? -60.578 34.624 -3.634  1.00 77.07  ? 155 LEU A CD2 1 
ATOM   1210 N  N   . PHE A 1 156 ? -62.091 38.088 -7.643  1.00 77.82  ? 156 PHE A N   1 
ATOM   1211 C  CA  . PHE A 1 156 ? -62.018 39.282 -8.472  1.00 83.80  ? 156 PHE A CA  1 
ATOM   1212 C  C   . PHE A 1 156 ? -63.246 40.167 -8.320  1.00 78.08  ? 156 PHE A C   1 
ATOM   1213 O  O   . PHE A 1 156 ? -63.581 40.934 -9.228  1.00 73.14  ? 156 PHE A O   1 
ATOM   1214 C  CB  . PHE A 1 156 ? -61.800 38.874 -9.927  1.00 77.95  ? 156 PHE A CB  1 
ATOM   1215 C  CG  . PHE A 1 156 ? -60.685 37.880 -10.104 1.00 83.00  ? 156 PHE A CG  1 
ATOM   1216 C  CD1 . PHE A 1 156 ? -59.369 38.305 -10.190 1.00 73.40  ? 156 PHE A CD1 1 
ATOM   1217 C  CD2 . PHE A 1 156 ? -60.949 36.520 -10.152 1.00 82.53  ? 156 PHE A CD2 1 
ATOM   1218 C  CE1 . PHE A 1 156 ? -58.339 37.394 -10.341 1.00 73.78  ? 156 PHE A CE1 1 
ATOM   1219 C  CE2 . PHE A 1 156 ? -59.922 35.604 -10.300 1.00 81.77  ? 156 PHE A CE2 1 
ATOM   1220 C  CZ  . PHE A 1 156 ? -58.616 36.043 -10.395 1.00 78.04  ? 156 PHE A CZ  1 
ATOM   1221 N  N   A ARG A 1 157 ? -63.928 40.076 -7.183  0.43 79.63  ? 157 ARG A N   1 
ATOM   1222 N  N   B ARG A 1 157 ? -63.919 40.091 -7.178  0.57 79.64  ? 157 ARG A N   1 
ATOM   1223 C  CA  A ARG A 1 157 ? -65.105 40.852 -6.854  0.43 78.14  ? 157 ARG A CA  1 
ATOM   1224 C  CA  B ARG A 1 157 ? -65.099 40.867 -6.868  0.57 78.14  ? 157 ARG A CA  1 
ATOM   1225 C  C   A ARG A 1 157 ? -64.930 41.465 -5.473  0.43 78.56  ? 157 ARG A C   1 
ATOM   1226 C  C   B ARG A 1 157 ? -64.967 41.438 -5.463  0.57 78.58  ? 157 ARG A C   1 
ATOM   1227 O  O   A ARG A 1 157 ? -64.108 40.993 -4.679  0.43 78.50  ? 157 ARG A O   1 
ATOM   1228 O  O   B ARG A 1 157 ? -64.210 40.907 -4.643  0.57 78.72  ? 157 ARG A O   1 
ATOM   1229 C  CB  A ARG A 1 157 ? -66.369 39.978 -6.866  0.43 78.11  ? 157 ARG A CB  1 
ATOM   1230 C  CB  B ARG A 1 157 ? -66.366 40.003 -6.958  0.57 78.08  ? 157 ARG A CB  1 
ATOM   1231 C  CG  A ARG A 1 157 ? -66.333 38.850 -5.844  0.43 81.47  ? 157 ARG A CG  1 
ATOM   1232 C  CG  B ARG A 1 157 ? -66.299 38.757 -6.092  0.57 81.25  ? 157 ARG A CG  1 
ATOM   1233 C  CD  A ARG A 1 157 ? -67.723 38.514 -5.328  0.43 81.65  ? 157 ARG A CD  1 
ATOM   1234 C  CD  B ARG A 1 157 ? -67.505 37.861 -6.294  0.57 81.18  ? 157 ARG A CD  1 
ATOM   1235 N  NE  A ARG A 1 157 ? -67.683 37.498 -4.283  0.43 79.91  ? 157 ARG A NE  1 
ATOM   1236 N  NE  B ARG A 1 157 ? -67.373 36.610 -5.557  0.57 84.39  ? 157 ARG A NE  1 
ATOM   1237 C  CZ  A ARG A 1 157 ? -68.008 36.225 -4.463  0.43 80.70  ? 157 ARG A CZ  1 
ATOM   1238 C  CZ  B ARG A 1 157 ? -67.781 36.428 -4.309  0.57 80.41  ? 157 ARG A CZ  1 
ATOM   1239 N  NH1 A ARG A 1 157 ? -68.427 35.777 -5.635  0.43 82.65  ? 157 ARG A NH1 1 
ATOM   1240 N  NH1 B ARG A 1 157 ? -68.358 37.400 -3.622  0.57 80.60  ? 157 ARG A NH1 1 
ATOM   1241 N  NH2 A ARG A 1 157 ? -67.909 35.380 -3.442  0.43 79.58  ? 157 ARG A NH2 1 
ATOM   1242 N  NH2 B ARG A 1 157 ? -67.608 35.240 -3.736  0.57 79.81  ? 157 ARG A NH2 1 
ATOM   1243 N  N   . PRO A 1 158 ? -65.672 42.523 -5.162  1.00 79.20  ? 158 PRO A N   1 
ATOM   1244 C  CA  . PRO A 1 158 ? -65.710 43.003 -3.776  1.00 77.05  ? 158 PRO A CA  1 
ATOM   1245 C  C   . PRO A 1 158 ? -66.471 42.017 -2.904  1.00 77.22  ? 158 PRO A C   1 
ATOM   1246 O  O   . PRO A 1 158 ? -67.519 41.497 -3.295  1.00 77.30  ? 158 PRO A O   1 
ATOM   1247 C  CB  . PRO A 1 158 ? -66.439 44.348 -3.877  1.00 78.50  ? 158 PRO A CB  1 
ATOM   1248 C  CG  . PRO A 1 158 ? -66.337 44.739 -5.322  1.00 74.88  ? 158 PRO A CG  1 
ATOM   1249 C  CD  . PRO A 1 158 ? -66.354 43.449 -6.083  1.00 78.85  ? 158 PRO A CD  1 
ATOM   1250 N  N   . ALA A 1 159 ? -65.931 41.750 -1.720  1.00 76.18  ? 159 ALA A N   1 
ATOM   1251 C  CA  . ALA A 1 159 ? -66.523 40.758 -0.836  1.00 77.24  ? 159 ALA A CA  1 
ATOM   1252 C  C   . ALA A 1 159 ? -67.781 41.306 -0.177  1.00 71.99  ? 159 ALA A C   1 
ATOM   1253 O  O   . ALA A 1 159 ? -67.852 42.488 0.174   1.00 73.53  ? 159 ALA A O   1 
ATOM   1254 C  CB  . ALA A 1 159 ? -65.518 40.325 0.231   1.00 72.98  ? 159 ALA A CB  1 
ATOM   1255 N  N   . ASN A 1 160 ? -68.780 40.441 -0.015  1.00 68.08  ? 160 ASN A N   1 
ATOM   1256 C  CA  . ASN A 1 160 ? -69.995 40.839 0.675   1.00 70.60  ? 160 ASN A CA  1 
ATOM   1257 C  C   . ASN A 1 160 ? -69.758 40.845 2.184   1.00 71.39  ? 160 ASN A C   1 
ATOM   1258 O  O   . ASN A 1 160 ? -68.690 40.474 2.678   1.00 72.44  ? 160 ASN A O   1 
ATOM   1259 C  CB  . ASN A 1 160 ? -71.162 39.928 0.294   1.00 76.95  ? 160 ASN A CB  1 
ATOM   1260 C  CG  . ASN A 1 160 ? -70.912 38.471 0.636   1.00 72.97  ? 160 ASN A CG  1 
ATOM   1261 O  OD1 . ASN A 1 160 ? -70.793 38.103 1.804   1.00 72.10  ? 160 ASN A OD1 1 
ATOM   1262 N  ND2 . ASN A 1 160 ? -70.860 37.628 -0.388  1.00 72.79  ? 160 ASN A ND2 1 
ATOM   1263 N  N   . GLU A 1 161 ? -70.780 41.267 2.929   1.00 67.59  ? 161 GLU A N   1 
ATOM   1264 C  CA  A GLU A 1 161 ? -70.613 41.383 4.371   0.48 67.06  ? 161 GLU A CA  1 
ATOM   1265 C  CA  B GLU A 1 161 ? -70.665 41.382 4.381   0.52 66.99  ? 161 GLU A CA  1 
ATOM   1266 C  C   . GLU A 1 161 ? -70.512 40.018 5.042   1.00 64.63  ? 161 GLU A C   1 
ATOM   1267 O  O   . GLU A 1 161 ? -69.776 39.873 6.025   1.00 66.50  ? 161 GLU A O   1 
ATOM   1268 C  CB  A GLU A 1 161 ? -71.754 42.213 4.956   0.48 66.98  ? 161 GLU A CB  1 
ATOM   1269 C  CB  B GLU A 1 161 ? -71.888 42.111 4.938   0.52 67.09  ? 161 GLU A CB  1 
ATOM   1270 C  CG  A GLU A 1 161 ? -71.745 43.648 4.444   0.48 66.03  ? 161 GLU A CG  1 
ATOM   1271 C  CG  B GLU A 1 161 ? -72.131 41.877 6.419   0.52 64.82  ? 161 GLU A CG  1 
ATOM   1272 C  CD  A GLU A 1 161 ? -72.918 44.466 4.939   0.48 67.85  ? 161 GLU A CD  1 
ATOM   1273 C  CD  B GLU A 1 161 ? -73.429 42.485 6.905   0.52 65.34  ? 161 GLU A CD  1 
ATOM   1274 O  OE1 A GLU A 1 161 ? -73.706 43.947 5.757   0.48 67.87  ? 161 GLU A OE1 1 
ATOM   1275 O  OE1 B GLU A 1 161 ? -74.154 43.081 6.082   0.52 67.69  ? 161 GLU A OE1 1 
ATOM   1276 O  OE2 A GLU A 1 161 ? -73.052 45.630 4.507   0.48 69.37  ? 161 GLU A OE2 1 
ATOM   1277 O  OE2 B GLU A 1 161 ? -73.725 42.365 8.113   0.52 64.51  ? 161 GLU A OE2 1 
ATOM   1278 N  N   . THR A 1 162 ? -71.210 39.005 4.524   1.00 66.29  ? 162 THR A N   1 
ATOM   1279 C  CA  . THR A 1 162 ? -71.107 37.671 5.110   1.00 62.56  ? 162 THR A CA  1 
ATOM   1280 C  C   . THR A 1 162 ? -69.700 37.106 4.948   1.00 67.54  ? 162 THR A C   1 
ATOM   1281 O  O   . THR A 1 162 ? -69.145 36.522 5.886   1.00 66.99  ? 162 THR A O   1 
ATOM   1282 C  CB  . THR A 1 162 ? -72.137 36.733 4.478   1.00 63.72  ? 162 THR A CB  1 
ATOM   1283 O  OG1 . THR A 1 162 ? -73.458 37.200 4.777   1.00 70.49  ? 162 THR A OG1 1 
ATOM   1284 C  CG2 . THR A 1 162 ? -71.973 35.318 5.015   1.00 62.67  ? 162 THR A CG2 1 
ATOM   1285 N  N   . GLU A 1 163 ? -69.104 37.279 3.765   1.00 68.57  ? 163 GLU A N   1 
ATOM   1286 C  CA  . GLU A 1 163 ? -67.751 36.780 3.538   1.00 68.64  ? 163 GLU A CA  1 
ATOM   1287 C  C   . GLU A 1 163 ? -66.738 37.508 4.413   1.00 62.85  ? 163 GLU A C   1 
ATOM   1288 O  O   . GLU A 1 163 ? -65.798 36.893 4.931   1.00 61.41  ? 163 GLU A O   1 
ATOM   1289 C  CB  . GLU A 1 163 ? -67.383 36.923 2.062   1.00 67.91  ? 163 GLU A CB  1 
ATOM   1290 C  CG  . GLU A 1 163 ? -68.233 36.082 1.127   1.00 73.28  ? 163 GLU A CG  1 
ATOM   1291 C  CD  . GLU A 1 163 ? -68.040 36.459 -0.329  1.00 77.37  ? 163 GLU A CD  1 
ATOM   1292 O  OE1 . GLU A 1 163 ? -67.648 37.615 -0.599  1.00 73.70  ? 163 GLU A OE1 1 
ATOM   1293 O  OE2 . GLU A 1 163 ? -68.285 35.602 -1.203  1.00 75.96  ? 163 GLU A OE2 1 
ATOM   1294 N  N   . ILE A 1 164 ? -66.914 38.818 4.590   1.00 62.21  ? 164 ILE A N   1 
ATOM   1295 C  CA  . ILE A 1 164 ? -65.982 39.589 5.406   1.00 61.54  ? 164 ILE A CA  1 
ATOM   1296 C  C   . ILE A 1 164 ? -66.137 39.231 6.879   1.00 60.79  ? 164 ILE A C   1 
ATOM   1297 O  O   . ILE A 1 164 ? -65.151 39.178 7.626   1.00 61.26  ? 164 ILE A O   1 
ATOM   1298 C  CB  . ILE A 1 164 ? -66.182 41.096 5.158   1.00 66.54  ? 164 ILE A CB  1 
ATOM   1299 C  CG1 . ILE A 1 164 ? -65.878 41.438 3.698   1.00 67.54  ? 164 ILE A CG1 1 
ATOM   1300 C  CG2 . ILE A 1 164 ? -65.294 41.914 6.073   1.00 60.75  ? 164 ILE A CG2 1 
ATOM   1301 C  CD1 . ILE A 1 164 ? -66.137 42.886 3.343   1.00 66.03  ? 164 ILE A CD1 1 
ATOM   1302 N  N   . ALA A 1 165 ? -67.371 38.972 7.321   1.00 61.44  ? 165 ALA A N   1 
ATOM   1303 C  CA  . ALA A 1 165 ? -67.589 38.580 8.710   1.00 59.86  ? 165 ALA A CA  1 
ATOM   1304 C  C   . ALA A 1 165 ? -66.888 37.264 9.026   1.00 58.67  ? 165 ALA A C   1 
ATOM   1305 O  O   . ALA A 1 165 ? -66.316 37.101 10.111  1.00 56.73  ? 165 ALA A O   1 
ATOM   1306 C  CB  . ALA A 1 165 ? -69.086 38.475 9.000   1.00 55.76  ? 165 ALA A CB  1 
ATOM   1307 N  N   . GLY A 1 166 ? -66.917 36.317 8.087   1.00 59.15  ? 166 GLY A N   1 
ATOM   1308 C  CA  . GLY A 1 166 ? -66.219 35.060 8.292   1.00 58.20  ? 166 GLY A CA  1 
ATOM   1309 C  C   . GLY A 1 166 ? -64.712 35.211 8.338   1.00 59.69  ? 166 GLY A C   1 
ATOM   1310 O  O   . GLY A 1 166 ? -64.033 34.465 9.050   1.00 59.27  ? 166 GLY A O   1 
ATOM   1311 N  N   . MET A 1 167 ? -64.166 36.171 7.588   1.00 57.78  ? 167 MET A N   1 
ATOM   1312 C  CA  . MET A 1 167 ? -62.724 36.390 7.621   1.00 60.56  ? 167 MET A CA  1 
ATOM   1313 C  C   . MET A 1 167 ? -62.287 37.001 8.947   1.00 57.81  ? 167 MET A C   1 
ATOM   1314 O  O   . MET A 1 167 ? -61.184 36.721 9.431   1.00 60.23  ? 167 MET A O   1 
ATOM   1315 C  CB  . MET A 1 167 ? -62.295 37.277 6.453   1.00 60.70  ? 167 MET A CB  1 
ATOM   1316 C  CG  . MET A 1 167 ? -62.431 36.623 5.088   1.00 66.53  ? 167 MET A CG  1 
ATOM   1317 S  SD  . MET A 1 167 ? -61.630 37.580 3.784   1.00 65.48  ? 167 MET A SD  1 
ATOM   1318 C  CE  . MET A 1 167 ? -62.594 39.087 3.830   1.00 64.28  ? 167 MET A CE  1 
ATOM   1319 N  N   . ARG A 1 168 ? -63.139 37.833 9.551   1.00 58.83  ? 168 ARG A N   1 
ATOM   1320 C  CA  . ARG A 1 168 ? -62.802 38.430 10.840  1.00 56.21  ? 168 ARG A CA  1 
ATOM   1321 C  C   . ARG A 1 168 ? -62.731 37.375 11.938  1.00 58.74  ? 168 ARG A C   1 
ATOM   1322 O  O   . ARG A 1 168 ? -61.872 37.453 12.826  1.00 56.82  ? 168 ARG A O   1 
ATOM   1323 C  CB  . ARG A 1 168 ? -63.819 39.512 11.209  1.00 52.64  ? 168 ARG A CB  1 
ATOM   1324 C  CG  . ARG A 1 168 ? -63.723 40.777 10.371  1.00 56.60  ? 168 ARG A CG  1 
ATOM   1325 C  CD  . ARG A 1 168 ? -64.427 41.945 11.047  1.00 57.72  ? 168 ARG A CD  1 
ATOM   1326 N  NE  . ARG A 1 168 ? -63.806 42.291 12.321  1.00 57.92  ? 168 ARG A NE  1 
ATOM   1327 C  CZ  . ARG A 1 168 ? -64.120 43.357 13.045  1.00 52.22  ? 168 ARG A CZ  1 
ATOM   1328 N  NH1 . ARG A 1 168 ? -65.045 44.215 12.647  1.00 52.06  ? 168 ARG A NH1 1 
ATOM   1329 N  NH2 . ARG A 1 168 ? -63.489 43.568 14.196  1.00 51.70  ? 168 ARG A NH2 1 
ATOM   1330 N  N   . VAL A 1 169 ? -63.624 36.383 11.896  1.00 60.39  ? 169 VAL A N   1 
ATOM   1331 C  CA  . VAL A 1 169 ? -63.610 35.329 12.906  1.00 56.13  ? 169 VAL A CA  1 
ATOM   1332 C  C   . VAL A 1 169 ? -62.382 34.443 12.739  1.00 54.39  ? 169 VAL A C   1 
ATOM   1333 O  O   . VAL A 1 169 ? -61.724 34.080 13.722  1.00 59.53  ? 169 VAL A O   1 
ATOM   1334 C  CB  . VAL A 1 169 ? -64.911 34.508 12.841  1.00 56.49  ? 169 VAL A CB  1 
ATOM   1335 C  CG1 . VAL A 1 169 ? -64.823 33.295 13.754  1.00 55.65  ? 169 VAL A CG1 1 
ATOM   1336 C  CG2 . VAL A 1 169 ? -66.104 35.374 13.215  1.00 55.99  ? 169 VAL A CG2 1 
ATOM   1337 N  N   . GLN A 1 170 ? -62.051 34.083 11.497  1.00 56.98  ? 170 GLN A N   1 
ATOM   1338 C  CA  . GLN A 1 170 ? -60.899 33.218 11.264  1.00 56.98  ? 170 GLN A CA  1 
ATOM   1339 C  C   . GLN A 1 170 ? -59.595 33.933 11.595  1.00 55.88  ? 170 GLN A C   1 
ATOM   1340 O  O   . GLN A 1 170 ? -58.657 33.317 12.115  1.00 55.45  ? 170 GLN A O   1 
ATOM   1341 C  CB  . GLN A 1 170 ? -60.896 32.722 9.817   1.00 57.85  ? 170 GLN A CB  1 
ATOM   1342 C  CG  . GLN A 1 170 ? -59.817 31.689 9.524   1.00 56.66  ? 170 GLN A CG  1 
ATOM   1343 C  CD  . GLN A 1 170 ? -59.999 31.006 8.181   1.00 59.04  ? 170 GLN A CD  1 
ATOM   1344 O  OE1 . GLN A 1 170 ? -60.629 31.548 7.272   1.00 64.89  ? 170 GLN A OE1 1 
ATOM   1345 N  NE2 . GLN A 1 170 ? -59.448 29.805 8.052   1.00 62.79  ? 170 GLN A NE2 1 
ATOM   1346 N  N   . LEU A 1 171 ? -59.515 35.234 11.303  1.00 55.74  ? 171 LEU A N   1 
ATOM   1347 C  CA  . LEU A 1 171 ? -58.337 36.002 11.692  1.00 52.66  ? 171 LEU A CA  1 
ATOM   1348 C  C   . LEU A 1 171 ? -58.235 36.118 13.207  1.00 56.98  ? 171 LEU A C   1 
ATOM   1349 O  O   . LEU A 1 171 ? -57.133 36.064 13.766  1.00 58.37  ? 171 LEU A O   1 
ATOM   1350 C  CB  . LEU A 1 171 ? -58.376 37.389 11.046  1.00 52.07  ? 171 LEU A CB  1 
ATOM   1351 C  CG  . LEU A 1 171 ? -57.244 38.354 11.406  1.00 50.36  ? 171 LEU A CG  1 
ATOM   1352 C  CD1 . LEU A 1 171 ? -55.889 37.739 11.100  1.00 51.12  ? 171 LEU A CD1 1 
ATOM   1353 C  CD2 . LEU A 1 171 ? -57.406 39.674 10.675  1.00 52.30  ? 171 LEU A CD2 1 
ATOM   1354 N  N   . ARG A 1 172 ? -59.376 36.264 13.886  1.00 57.17  ? 172 ARG A N   1 
ATOM   1355 C  CA  . ARG A 1 172 ? -59.369 36.372 15.341  1.00 55.92  ? 172 ARG A CA  1 
ATOM   1356 C  C   . ARG A 1 172 ? -58.833 35.101 15.989  1.00 57.85  ? 172 ARG A C   1 
ATOM   1357 O  O   . ARG A 1 172 ? -58.061 35.165 16.953  1.00 56.36  ? 172 ARG A O   1 
ATOM   1358 C  CB  . ARG A 1 172 ? -60.779 36.677 15.841  1.00 56.10  ? 172 ARG A CB  1 
ATOM   1359 C  CG  . ARG A 1 172 ? -60.869 37.039 17.311  1.00 60.77  ? 172 ARG A CG  1 
ATOM   1360 C  CD  . ARG A 1 172 ? -62.313 37.302 17.685  1.00 59.76  ? 172 ARG A CD  1 
ATOM   1361 N  NE  . ARG A 1 172 ? -62.942 38.219 16.744  1.00 60.47  ? 172 ARG A NE  1 
ATOM   1362 C  CZ  . ARG A 1 172 ? -64.252 38.364 16.601  1.00 61.07  ? 172 ARG A CZ  1 
ATOM   1363 N  NH1 . ARG A 1 172 ? -65.108 37.652 17.316  1.00 64.84  ? 172 ARG A NH1 1 
ATOM   1364 N  NH2 . ARG A 1 172 ? -64.716 39.240 15.714  1.00 56.97  ? 172 ARG A NH2 1 
ATOM   1365 N  N   . ASP A 1 173 ? -59.233 33.934 15.475  1.00 55.72  ? 173 ASP A N   1 
ATOM   1366 C  CA  . ASP A 1 173 ? -58.710 32.680 16.006  1.00 56.71  ? 173 ASP A CA  1 
ATOM   1367 C  C   . ASP A 1 173 ? -57.229 32.513 15.695  1.00 57.74  ? 173 ASP A C   1 
ATOM   1368 O  O   . ASP A 1 173 ? -56.497 31.903 16.482  1.00 55.50  ? 173 ASP A O   1 
ATOM   1369 C  CB  . ASP A 1 173 ? -59.501 31.497 15.451  1.00 59.09  ? 173 ASP A CB  1 
ATOM   1370 C  CG  . ASP A 1 173 ? -60.901 31.413 16.022  1.00 70.40  ? 173 ASP A CG  1 
ATOM   1371 O  OD1 . ASP A 1 173 ? -61.092 31.805 17.193  1.00 71.74  ? 173 ASP A OD1 1 
ATOM   1372 O  OD2 . ASP A 1 173 ? -61.811 30.951 15.301  1.00 68.72  ? 173 ASP A OD2 1 
ATOM   1373 N  N   . ALA A 1 174 ? -56.773 33.042 14.557  1.00 57.39  ? 174 ALA A N   1 
ATOM   1374 C  CA  . ALA A 1 174 ? -55.359 32.947 14.216  1.00 52.91  ? 174 ALA A CA  1 
ATOM   1375 C  C   . ALA A 1 174 ? -54.507 33.787 15.158  1.00 55.46  ? 174 ALA A C   1 
ATOM   1376 O  O   . ALA A 1 174 ? -53.441 33.344 15.602  1.00 54.48  ? 174 ALA A O   1 
ATOM   1377 C  CB  . ALA A 1 174 ? -55.143 33.375 12.765  1.00 54.57  ? 174 ALA A CB  1 
ATOM   1378 N  N   . LEU A 1 175 ? -54.964 35.000 15.480  1.00 52.73  ? 175 LEU A N   1 
ATOM   1379 C  CA  . LEU A 1 175 ? -54.215 35.864 16.386  1.00 54.76  ? 175 LEU A CA  1 
ATOM   1380 C  C   . LEU A 1 175 ? -54.178 35.303 17.802  1.00 57.36  ? 175 LEU A C   1 
ATOM   1381 O  O   . LEU A 1 175 ? -53.187 35.493 18.516  1.00 56.57  ? 175 LEU A O   1 
ATOM   1382 C  CB  . LEU A 1 175 ? -54.821 37.267 16.391  1.00 54.60  ? 175 LEU A CB  1 
ATOM   1383 C  CG  . LEU A 1 175 ? -54.907 37.967 15.035  1.00 49.11  ? 175 LEU A CG  1 
ATOM   1384 C  CD1 . LEU A 1 175 ? -55.621 39.301 15.164  1.00 46.98  ? 175 LEU A CD1 1 
ATOM   1385 C  CD2 . LEU A 1 175 ? -53.522 38.150 14.438  1.00 50.54  ? 175 LEU A CD2 1 
ATOM   1386 N  N   . ARG A 1 176 ? -55.244 34.620 18.227  1.00 54.82  ? 176 ARG A N   1 
ATOM   1387 C  CA  . ARG A 1 176 ? -55.247 34.004 19.549  1.00 58.13  ? 176 ARG A CA  1 
ATOM   1388 C  C   . ARG A 1 176 ? -54.252 32.855 19.635  1.00 57.82  ? 176 ARG A C   1 
ATOM   1389 O  O   . ARG A 1 176 ? -53.709 32.586 20.713  1.00 56.71  ? 176 ARG A O   1 
ATOM   1390 C  CB  . ARG A 1 176 ? -56.652 33.513 19.900  1.00 57.63  ? 176 ARG A CB  1 
ATOM   1391 C  CG  . ARG A 1 176 ? -57.613 34.615 20.314  1.00 61.42  ? 176 ARG A CG  1 
ATOM   1392 C  CD  . ARG A 1 176 ? -59.047 34.113 20.380  1.00 59.70  ? 176 ARG A CD  1 
ATOM   1393 N  NE  . ARG A 1 176 ? -59.949 35.133 20.902  1.00 62.28  ? 176 ARG A NE  1 
ATOM   1394 C  CZ  . ARG A 1 176 ? -61.269 35.106 20.778  1.00 64.77  ? 176 ARG A CZ  1 
ATOM   1395 N  NH1 . ARG A 1 176 ? -61.883 34.125 20.136  1.00 64.87  ? 176 ARG A NH1 1 
ATOM   1396 N  NH2 . ARG A 1 176 ? -61.990 36.091 21.304  1.00 65.98  ? 176 ARG A NH2 1 
ATOM   1397 N  N   . GLN A 1 177 ? -53.999 32.173 18.521  1.00 56.72  ? 177 GLN A N   1 
ATOM   1398 C  CA  . GLN A 1 177 ? -53.074 31.051 18.484  1.00 55.31  ? 177 GLN A CA  1 
ATOM   1399 C  C   . GLN A 1 177 ? -51.636 31.475 18.210  1.00 55.42  ? 177 GLN A C   1 
ATOM   1400 O  O   . GLN A 1 177 ? -50.772 30.611 18.039  1.00 60.88  ? 177 GLN A O   1 
ATOM   1401 C  CB  . GLN A 1 177 ? -53.529 30.029 17.439  1.00 55.81  ? 177 GLN A CB  1 
ATOM   1402 C  CG  . GLN A 1 177 ? -54.781 29.270 17.843  1.00 59.28  ? 177 GLN A CG  1 
ATOM   1403 C  CD  . GLN A 1 177 ? -55.266 28.318 16.769  1.00 64.15  ? 177 GLN A CD  1 
ATOM   1404 O  OE1 . GLN A 1 177 ? -54.874 28.423 15.607  1.00 62.60  ? 177 GLN A OE1 1 
ATOM   1405 N  NE2 . GLN A 1 177 ? -56.121 27.378 17.154  1.00 64.22  ? 177 GLN A NE2 1 
ATOM   1406 N  N   . GLY A 1 178 ? -51.363 32.776 18.160  1.00 50.73  ? 178 GLY A N   1 
ATOM   1407 C  CA  . GLY A 1 178 ? -50.006 33.272 18.074  1.00 52.22  ? 178 GLY A CA  1 
ATOM   1408 C  C   . GLY A 1 178 ? -49.622 33.989 16.795  1.00 53.26  ? 178 GLY A C   1 
ATOM   1409 O  O   . GLY A 1 178 ? -48.433 34.275 16.608  1.00 52.49  ? 178 GLY A O   1 
ATOM   1410 N  N   . ALA A 1 179 ? -50.572 34.287 15.911  1.00 53.61  ? 179 ALA A N   1 
ATOM   1411 C  CA  . ALA A 1 179 ? -50.243 35.011 14.690  1.00 49.57  ? 179 ALA A CA  1 
ATOM   1412 C  C   . ALA A 1 179 ? -49.733 36.409 15.022  1.00 50.93  ? 179 ALA A C   1 
ATOM   1413 O  O   . ALA A 1 179 ? -50.091 36.999 16.045  1.00 49.47  ? 179 ALA A O   1 
ATOM   1414 C  CB  . ALA A 1 179 ? -51.462 35.097 13.771  1.00 50.78  ? 179 ALA A CB  1 
ATOM   1415 N  N   . LEU A 1 180 ? -48.879 36.939 14.146  1.00 51.59  ? 180 LEU A N   1 
ATOM   1416 C  CA  . LEU A 1 180 ? -48.251 38.230 14.395  1.00 51.66  ? 180 LEU A CA  1 
ATOM   1417 C  C   . LEU A 1 180 ? -49.013 39.400 13.792  1.00 55.25  ? 180 LEU A C   1 
ATOM   1418 O  O   . LEU A 1 180 ? -48.748 40.549 14.166  1.00 52.51  ? 180 LEU A O   1 
ATOM   1419 C  CB  . LEU A 1 180 ? -46.815 38.231 13.863  1.00 52.45  ? 180 LEU A CB  1 
ATOM   1420 C  CG  . LEU A 1 180 ? -45.864 37.195 14.468  1.00 52.03  ? 180 LEU A CG  1 
ATOM   1421 C  CD1 . LEU A 1 180 ? -44.464 37.369 13.908  1.00 49.93  ? 180 LEU A CD1 1 
ATOM   1422 C  CD2 . LEU A 1 180 ? -45.854 37.285 15.987  1.00 54.85  ? 180 LEU A CD2 1 
ATOM   1423 N  N   . GLY A 1 181 ? -49.940 39.146 12.878  1.00 53.32  ? 181 GLY A N   1 
ATOM   1424 C  CA  . GLY A 1 181 ? -50.716 40.221 12.288  1.00 52.71  ? 181 GLY A CA  1 
ATOM   1425 C  C   . GLY A 1 181 ? -51.291 39.795 10.949  1.00 53.11  ? 181 GLY A C   1 
ATOM   1426 O  O   . GLY A 1 181 ? -51.414 38.606 10.661  1.00 49.00  ? 181 GLY A O   1 
ATOM   1427 N  N   . LEU A 1 182 ? -51.633 40.798 10.144  1.00 53.70  ? 182 LEU A N   1 
ATOM   1428 C  CA  . LEU A 1 182 ? -52.258 40.594 8.844   1.00 51.52  ? 182 LEU A CA  1 
ATOM   1429 C  C   . LEU A 1 182 ? -51.407 41.239 7.761   1.00 52.13  ? 182 LEU A C   1 
ATOM   1430 O  O   . LEU A 1 182 ? -51.004 42.399 7.891   1.00 50.02  ? 182 LEU A O   1 
ATOM   1431 C  CB  . LEU A 1 182 ? -53.672 41.181 8.817   1.00 52.64  ? 182 LEU A CB  1 
ATOM   1432 C  CG  . LEU A 1 182 ? -54.416 41.084 7.482   1.00 50.37  ? 182 LEU A CG  1 
ATOM   1433 C  CD1 . LEU A 1 182 ? -54.949 39.675 7.255   1.00 51.65  ? 182 LEU A CD1 1 
ATOM   1434 C  CD2 . LEU A 1 182 ? -55.537 42.110 7.405   1.00 49.87  ? 182 LEU A CD2 1 
ATOM   1435 N  N   . SER A 1 183 ? -51.142 40.490 6.696   1.00 53.47  ? 183 SER A N   1 
ATOM   1436 C  CA  . SER A 1 183 ? -50.428 41.000 5.536   1.00 53.84  ? 183 SER A CA  1 
ATOM   1437 C  C   . SER A 1 183 ? -51.377 41.098 4.349   1.00 54.67  ? 183 SER A C   1 
ATOM   1438 O  O   . SER A 1 183 ? -52.292 40.285 4.198   1.00 55.91  ? 183 SER A O   1 
ATOM   1439 C  CB  . SER A 1 183 ? -49.236 40.107 5.178   1.00 53.05  ? 183 SER A CB  1 
ATOM   1440 O  OG  . SER A 1 183 ? -49.660 38.826 4.748   1.00 54.00  ? 183 SER A OG  1 
ATOM   1441 N  N   . THR A 1 184 ? -51.158 42.108 3.511   1.00 56.38  ? 184 THR A N   1 
ATOM   1442 C  CA  . THR A 1 184 ? -51.959 42.307 2.313   1.00 60.20  ? 184 THR A CA  1 
ATOM   1443 C  C   . THR A 1 184 ? -51.054 42.484 1.104   1.00 64.43  ? 184 THR A C   1 
ATOM   1444 O  O   . THR A 1 184 ? -49.944 43.011 1.207   1.00 63.28  ? 184 THR A O   1 
ATOM   1445 C  CB  . THR A 1 184 ? -52.888 43.527 2.434   1.00 58.06  ? 184 THR A CB  1 
ATOM   1446 O  OG1 . THR A 1 184 ? -52.112 44.699 2.710   1.00 57.81  ? 184 THR A OG1 1 
ATOM   1447 C  CG2 . THR A 1 184 ? -53.909 43.319 3.544   1.00 59.69  ? 184 THR A CG2 1 
ATOM   1448 N  N   . GLY A 1 185 ? -51.542 42.022 -0.042  1.00 61.95  ? 185 GLY A N   1 
ATOM   1449 C  CA  . GLY A 1 185 ? -50.891 42.246 -1.316  1.00 62.74  ? 185 GLY A CA  1 
ATOM   1450 C  C   . GLY A 1 185 ? -51.889 42.798 -2.311  1.00 63.67  ? 185 GLY A C   1 
ATOM   1451 O  O   . GLY A 1 185 ? -52.387 42.070 -3.174  1.00 66.77  ? 185 GLY A O   1 
ATOM   1452 N  N   . LEU A 1 186 ? -52.190 44.093 -2.194  1.00 68.93  ? 186 LEU A N   1 
ATOM   1453 C  CA  . LEU A 1 186 ? -53.330 44.656 -2.909  1.00 69.51  ? 186 LEU A CA  1 
ATOM   1454 C  C   . LEU A 1 186 ? -53.063 44.792 -4.403  1.00 69.44  ? 186 LEU A C   1 
ATOM   1455 O  O   . LEU A 1 186 ? -54.006 44.766 -5.200  1.00 69.81  ? 186 LEU A O   1 
ATOM   1456 C  CB  . LEU A 1 186 ? -53.698 46.010 -2.308  1.00 72.12  ? 186 LEU A CB  1 
ATOM   1457 C  CG  . LEU A 1 186 ? -54.002 46.003 -0.812  1.00 68.19  ? 186 LEU A CG  1 
ATOM   1458 C  CD1 . LEU A 1 186 ? -54.062 47.424 -0.281  1.00 70.83  ? 186 LEU A CD1 1 
ATOM   1459 C  CD2 . LEU A 1 186 ? -55.303 45.265 -0.527  1.00 63.31  ? 186 LEU A CD2 1 
ATOM   1460 N  N   . ALA A 1 187 ? -51.799 44.939 -4.805  1.00 71.61  ? 187 ALA A N   1 
ATOM   1461 C  CA  . ALA A 1 187 ? -51.480 45.104 -6.219  1.00 68.47  ? 187 ALA A CA  1 
ATOM   1462 C  C   . ALA A 1 187 ? -51.803 43.863 -7.039  1.00 65.70  ? 187 ALA A C   1 
ATOM   1463 O  O   . ALA A 1 187 ? -51.942 43.964 -8.262  1.00 71.17  ? 187 ALA A O   1 
ATOM   1464 C  CB  . ALA A 1 187 ? -50.003 45.467 -6.389  1.00 70.63  ? 187 ALA A CB  1 
ATOM   1465 N  N   . TYR A 1 188 ? -51.932 42.704 -6.400  1.00 64.41  ? 188 TYR A N   1 
ATOM   1466 C  CA  . TYR A 1 188 ? -52.228 41.474 -7.116  1.00 67.37  ? 188 TYR A CA  1 
ATOM   1467 C  C   . TYR A 1 188 ? -53.714 41.385 -7.442  1.00 73.90  ? 188 TYR A C   1 
ATOM   1468 O  O   . TYR A 1 188 ? -54.566 41.896 -6.710  1.00 72.10  ? 188 TYR A O   1 
ATOM   1469 C  CB  . TYR A 1 188 ? -51.781 40.264 -6.298  1.00 65.25  ? 188 TYR A CB  1 
ATOM   1470 C  CG  . TYR A 1 188 ? -50.285 40.226 -6.085  1.00 67.47  ? 188 TYR A CG  1 
ATOM   1471 C  CD1 . TYR A 1 188 ? -49.444 39.676 -7.043  1.00 68.57  ? 188 TYR A CD1 1 
ATOM   1472 C  CD2 . TYR A 1 188 ? -49.712 40.757 -4.938  1.00 69.64  ? 188 TYR A CD2 1 
ATOM   1473 C  CE1 . TYR A 1 188 ? -48.075 39.646 -6.861  1.00 67.67  ? 188 TYR A CE1 1 
ATOM   1474 C  CE2 . TYR A 1 188 ? -48.342 40.732 -4.746  1.00 66.79  ? 188 TYR A CE2 1 
ATOM   1475 C  CZ  . TYR A 1 188 ? -47.530 40.175 -5.711  1.00 71.03  ? 188 TYR A CZ  1 
ATOM   1476 O  OH  . TYR A 1 188 ? -46.166 40.147 -5.528  1.00 65.32  ? 188 TYR A OH  1 
ATOM   1477 N  N   . ALA A 1 189 ? -54.015 40.724 -8.564  1.00 69.32  ? 189 ALA A N   1 
ATOM   1478 C  CA  . ALA A 1 189 ? -55.385 40.686 -9.064  1.00 67.50  ? 189 ALA A CA  1 
ATOM   1479 C  C   . ALA A 1 189 ? -56.323 39.959 -8.110  1.00 72.75  ? 189 ALA A C   1 
ATOM   1480 O  O   . ALA A 1 189 ? -57.530 40.226 -8.105  1.00 72.78  ? 189 ALA A O   1 
ATOM   1481 C  CB  . ALA A 1 189 ? -55.420 40.029 -10.444 1.00 63.20  ? 189 ALA A CB  1 
ATOM   1482 N  N   . SER A 1 190 ? -55.794 39.042 -7.298  1.00 68.79  ? 190 SER A N   1 
ATOM   1483 C  CA  . SER A 1 190 ? -56.627 38.307 -6.355  1.00 72.05  ? 190 SER A CA  1 
ATOM   1484 C  C   . SER A 1 190 ? -57.134 39.175 -5.209  1.00 69.93  ? 190 SER A C   1 
ATOM   1485 O  O   . SER A 1 190 ? -58.031 38.740 -4.478  1.00 67.67  ? 190 SER A O   1 
ATOM   1486 C  CB  . SER A 1 190 ? -55.852 37.114 -5.795  1.00 71.25  ? 190 SER A CB  1 
ATOM   1487 O  OG  . SER A 1 190 ? -55.400 36.263 -6.834  1.00 82.97  ? 190 SER A OG  1 
ATOM   1488 N  N   . ALA A 1 191 ? -56.592 40.383 -5.035  1.00 68.72  ? 191 ALA A N   1 
ATOM   1489 C  CA  . ALA A 1 191 ? -57.046 41.267 -3.970  1.00 68.92  ? 191 ALA A CA  1 
ATOM   1490 C  C   . ALA A 1 191 ? -57.186 42.716 -4.421  1.00 75.35  ? 191 ALA A C   1 
ATOM   1491 O  O   . ALA A 1 191 ? -57.417 43.590 -3.576  1.00 79.03  ? 191 ALA A O   1 
ATOM   1492 C  CB  . ALA A 1 191 ? -56.095 41.194 -2.767  1.00 68.47  ? 191 ALA A CB  1 
ATOM   1493 N  N   . PHE A 1 192 ? -57.060 43.001 -5.719  1.00 71.56  ? 192 PHE A N   1 
ATOM   1494 C  CA  . PHE A 1 192 ? -57.146 44.382 -6.181  1.00 72.70  ? 192 PHE A CA  1 
ATOM   1495 C  C   . PHE A 1 192 ? -58.574 44.908 -6.130  1.00 75.31  ? 192 PHE A C   1 
ATOM   1496 O  O   . PHE A 1 192 ? -58.783 46.112 -5.943  1.00 79.12  ? 192 PHE A O   1 
ATOM   1497 C  CB  . PHE A 1 192 ? -56.586 44.497 -7.598  1.00 70.41  ? 192 PHE A CB  1 
ATOM   1498 C  CG  . PHE A 1 192 ? -56.500 45.908 -8.104  1.00 69.99  ? 192 PHE A CG  1 
ATOM   1499 C  CD1 . PHE A 1 192 ? -55.519 46.766 -7.636  1.00 71.41  ? 192 PHE A CD1 1 
ATOM   1500 C  CD2 . PHE A 1 192 ? -57.396 46.375 -9.052  1.00 68.67  ? 192 PHE A CD2 1 
ATOM   1501 C  CE1 . PHE A 1 192 ? -55.435 48.065 -8.100  1.00 70.09  ? 192 PHE A CE1 1 
ATOM   1502 C  CE2 . PHE A 1 192 ? -57.316 47.673 -9.521  1.00 65.35  ? 192 PHE A CE2 1 
ATOM   1503 C  CZ  . PHE A 1 192 ? -56.334 48.519 -9.044  1.00 65.85  ? 192 PHE A CZ  1 
ATOM   1504 N  N   . GLN A 1 193 ? -59.564 44.034 -6.292  1.00 72.52  ? 193 GLN A N   1 
ATOM   1505 C  CA  . GLN A 1 193 ? -60.962 44.440 -6.238  1.00 75.65  ? 193 GLN A CA  1 
ATOM   1506 C  C   . GLN A 1 193 ? -61.497 44.541 -4.815  1.00 85.11  ? 193 GLN A C   1 
ATOM   1507 O  O   . GLN A 1 193 ? -62.706 44.717 -4.634  1.00 84.39  ? 193 GLN A O   1 
ATOM   1508 C  CB  . GLN A 1 193 ? -61.824 43.472 -7.053  1.00 77.07  ? 193 GLN A CB  1 
ATOM   1509 C  CG  . GLN A 1 193 ? -61.627 43.603 -8.553  1.00 75.12  ? 193 GLN A CG  1 
ATOM   1510 C  CD  . GLN A 1 193 ? -61.820 45.027 -9.037  1.00 77.06  ? 193 GLN A CD  1 
ATOM   1511 O  OE1 . GLN A 1 193 ? -60.854 45.765 -9.233  1.00 69.94  ? 193 GLN A OE1 1 
ATOM   1512 N  NE2 . GLN A 1 193 ? -63.073 45.422 -9.229  1.00 71.11  ? 193 GLN A NE2 1 
ATOM   1513 N  N   . SER A 1 194 ? -60.633 44.436 -3.809  1.00 78.09  ? 194 SER A N   1 
ATOM   1514 C  CA  . SER A 1 194 ? -61.058 44.601 -2.427  1.00 73.52  ? 194 SER A CA  1 
ATOM   1515 C  C   . SER A 1 194 ? -61.208 46.079 -2.097  1.00 76.11  ? 194 SER A C   1 
ATOM   1516 O  O   . SER A 1 194 ? -60.353 46.899 -2.446  1.00 75.70  ? 194 SER A O   1 
ATOM   1517 C  CB  . SER A 1 194 ? -60.052 43.957 -1.473  1.00 72.31  ? 194 SER A CB  1 
ATOM   1518 O  OG  . SER A 1 194 ? -58.845 44.699 -1.429  1.00 72.95  ? 194 SER A OG  1 
ATOM   1519 N  N   . THR A 1 195 ? -62.304 46.418 -1.427  1.00 75.58  ? 195 THR A N   1 
ATOM   1520 C  CA  . THR A 1 195 ? -62.480 47.778 -0.949  1.00 73.42  ? 195 THR A CA  1 
ATOM   1521 C  C   . THR A 1 195 ? -61.590 48.031 0.265   1.00 75.56  ? 195 THR A C   1 
ATOM   1522 O  O   . THR A 1 195 ? -61.159 47.106 0.960   1.00 74.99  ? 195 THR A O   1 
ATOM   1523 C  CB  . THR A 1 195 ? -63.944 48.042 -0.590  1.00 79.53  ? 195 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 195 ? -64.506 46.877 0.030   1.00 77.68  ? 195 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 195 ? -64.747 48.394 -1.835  1.00 78.18  ? 195 THR A CG2 1 
ATOM   1526 N  N   . THR A 1 196 ? -61.299 49.312 0.504   1.00 78.17  ? 196 THR A N   1 
ATOM   1527 C  CA  . THR A 1 196 ? -60.613 49.691 1.734   1.00 78.74  ? 196 THR A CA  1 
ATOM   1528 C  C   . THR A 1 196 ? -61.425 49.282 2.956   1.00 82.26  ? 196 THR A C   1 
ATOM   1529 O  O   . THR A 1 196 ? -60.857 48.946 4.002   1.00 75.49  ? 196 THR A O   1 
ATOM   1530 C  CB  . THR A 1 196 ? -60.347 51.199 1.742   1.00 83.75  ? 196 THR A CB  1 
ATOM   1531 O  OG1 . THR A 1 196 ? -59.552 51.552 0.602   1.00 86.25  ? 196 THR A OG1 1 
ATOM   1532 C  CG2 . THR A 1 196 ? -59.615 51.619 3.008   1.00 78.75  ? 196 THR A CG2 1 
ATOM   1533 N  N   . GLU A 1 197 ? -62.755 49.278 2.825   1.00 84.53  ? 197 GLU A N   1 
ATOM   1534 C  CA  . GLU A 1 197 ? -63.627 48.884 3.926   1.00 78.15  ? 197 GLU A CA  1 
ATOM   1535 C  C   . GLU A 1 197 ? -63.389 47.435 4.334   1.00 79.01  ? 197 GLU A C   1 
ATOM   1536 O  O   . GLU A 1 197 ? -63.424 47.105 5.525   1.00 80.20  ? 197 GLU A O   1 
ATOM   1537 C  CB  . GLU A 1 197 ? -65.085 49.099 3.521   1.00 74.45  ? 197 GLU A CB  1 
ATOM   1538 C  CG  . GLU A 1 197 ? -66.049 49.300 4.673   1.00 70.89  ? 197 GLU A CG  1 
ATOM   1539 C  CD  . GLU A 1 197 ? -67.472 49.519 4.197   1.00 78.30  ? 197 GLU A CD  1 
ATOM   1540 O  OE1 . GLU A 1 197 ? -67.925 48.769 3.307   1.00 82.35  ? 197 GLU A OE1 1 
ATOM   1541 O  OE2 . GLU A 1 197 ? -68.136 50.449 4.702   1.00 85.68  ? 197 GLU A OE2 1 
ATOM   1542 N  N   . GLU A 1 198 ? -63.149 46.553 3.359   1.00 71.52  ? 198 GLU A N   1 
ATOM   1543 C  CA  . GLU A 1 198 ? -62.895 45.150 3.675   1.00 66.15  ? 198 GLU A CA  1 
ATOM   1544 C  C   . GLU A 1 198 ? -61.616 44.993 4.487   1.00 66.43  ? 198 GLU A C   1 
ATOM   1545 O  O   . GLU A 1 198 ? -61.585 44.264 5.486   1.00 61.26  ? 198 GLU A O   1 
ATOM   1546 C  CB  . GLU A 1 198 ? -62.819 44.325 2.389   1.00 72.54  ? 198 GLU A CB  1 
ATOM   1547 C  CG  . GLU A 1 198 ? -62.337 42.896 2.601   1.00 68.98  ? 198 GLU A CG  1 
ATOM   1548 C  CD  . GLU A 1 198 ? -62.136 42.144 1.299   1.00 68.87  ? 198 GLU A CD  1 
ATOM   1549 O  OE1 . GLU A 1 198 ? -62.555 42.658 0.241   1.00 74.71  ? 198 GLU A OE1 1 
ATOM   1550 O  OE2 . GLU A 1 198 ? -61.557 41.037 1.334   1.00 66.26  ? 198 GLU A OE2 1 
ATOM   1551 N  N   . VAL A 1 199 ? -60.545 45.672 4.069   1.00 67.50  ? 199 VAL A N   1 
ATOM   1552 C  CA  . VAL A 1 199 ? -59.292 45.622 4.817   1.00 64.88  ? 199 VAL A CA  1 
ATOM   1553 C  C   . VAL A 1 199 ? -59.466 46.244 6.196   1.00 62.30  ? 199 VAL A C   1 
ATOM   1554 O  O   . VAL A 1 199 ? -58.849 45.796 7.171   1.00 59.31  ? 199 VAL A O   1 
ATOM   1555 C  CB  . VAL A 1 199 ? -58.169 46.316 4.021   1.00 61.69  ? 199 VAL A CB  1 
ATOM   1556 C  CG1 . VAL A 1 199 ? -56.839 46.188 4.748   1.00 60.98  ? 199 VAL A CG1 1 
ATOM   1557 C  CG2 . VAL A 1 199 ? -58.073 45.733 2.620   1.00 64.84  ? 199 VAL A CG2 1 
ATOM   1558 N  N   . MET A 1 200 ? -60.308 47.276 6.304   1.00 61.62  ? 200 MET A N   1 
ATOM   1559 C  CA  . MET A 1 200 ? -60.560 47.899 7.600   1.00 61.35  ? 200 MET A CA  1 
ATOM   1560 C  C   . MET A 1 200 ? -61.180 46.911 8.580   1.00 61.47  ? 200 MET A C   1 
ATOM   1561 O  O   . MET A 1 200 ? -60.819 46.891 9.763   1.00 58.47  ? 200 MET A O   1 
ATOM   1562 C  CB  . MET A 1 200 ? -61.468 49.117 7.427   1.00 61.43  ? 200 MET A CB  1 
ATOM   1563 C  CG  . MET A 1 200 ? -60.770 50.357 6.894   1.00 60.28  ? 200 MET A CG  1 
ATOM   1564 S  SD  . MET A 1 200 ? -61.952 51.573 6.283   1.00 67.36  ? 200 MET A SD  1 
ATOM   1565 C  CE  . MET A 1 200 ? -61.159 53.106 6.761   1.00 67.47  ? 200 MET A CE  1 
ATOM   1566 N  N   . ALA A 1 201 ? -62.117 46.086 8.107   1.00 58.36  ? 201 ALA A N   1 
ATOM   1567 C  CA  . ALA A 1 201 ? -62.760 45.116 8.987   1.00 55.51  ? 201 ALA A CA  1 
ATOM   1568 C  C   . ALA A 1 201 ? -61.757 44.103 9.518   1.00 56.78  ? 201 ALA A C   1 
ATOM   1569 O  O   . ALA A 1 201 ? -61.797 43.737 10.699  1.00 54.74  ? 201 ALA A O   1 
ATOM   1570 C  CB  . ALA A 1 201 ? -63.895 44.409 8.248   1.00 57.60  ? 201 ALA A CB  1 
ATOM   1571 N  N   . LEU A 1 202 ? -60.845 43.641 8.661   1.00 57.78  ? 202 LEU A N   1 
ATOM   1572 C  CA  . LEU A 1 202 ? -59.850 42.669 9.100   1.00 56.20  ? 202 LEU A CA  1 
ATOM   1573 C  C   . LEU A 1 202 ? -58.803 43.316 9.998   1.00 54.68  ? 202 LEU A C   1 
ATOM   1574 O  O   . LEU A 1 202 ? -58.349 42.704 10.971  1.00 54.24  ? 202 LEU A O   1 
ATOM   1575 C  CB  . LEU A 1 202 ? -59.193 42.008 7.888   1.00 55.60  ? 202 LEU A CB  1 
ATOM   1576 C  CG  . LEU A 1 202 ? -60.141 41.276 6.933   1.00 56.92  ? 202 LEU A CG  1 
ATOM   1577 C  CD1 . LEU A 1 202 ? -59.372 40.387 5.966   1.00 58.09  ? 202 LEU A CD1 1 
ATOM   1578 C  CD2 . LEU A 1 202 ? -61.165 40.468 7.712   1.00 56.91  ? 202 LEU A CD2 1 
ATOM   1579 N  N   . ALA A 1 203 ? -58.414 44.557 9.696   1.00 57.22  ? 203 ALA A N   1 
ATOM   1580 C  CA  . ALA A 1 203 ? -57.416 45.238 10.512  1.00 55.18  ? 203 ALA A CA  1 
ATOM   1581 C  C   . ALA A 1 203 ? -57.937 45.581 11.902  1.00 52.92  ? 203 ALA A C   1 
ATOM   1582 O  O   . ALA A 1 203 ? -57.131 45.813 12.809  1.00 50.90  ? 203 ALA A O   1 
ATOM   1583 C  CB  . ALA A 1 203 ? -56.932 46.505 9.808   1.00 55.29  ? 203 ALA A CB  1 
ATOM   1584 N  N   . GLU A 1 204 ? -59.260 45.619 12.090  1.00 51.35  ? 204 GLU A N   1 
ATOM   1585 C  CA  . GLU A 1 204 ? -59.813 45.890 13.414  1.00 53.43  ? 204 GLU A CA  1 
ATOM   1586 C  C   . GLU A 1 204 ? -59.504 44.769 14.397  1.00 51.67  ? 204 GLU A C   1 
ATOM   1587 O  O   . GLU A 1 204 ? -59.447 45.009 15.609  1.00 53.57  ? 204 GLU A O   1 
ATOM   1588 C  CB  . GLU A 1 204 ? -61.323 46.109 13.327  1.00 52.41  ? 204 GLU A CB  1 
ATOM   1589 C  CG  . GLU A 1 204 ? -61.725 47.483 12.829  1.00 50.81  ? 204 GLU A CG  1 
ATOM   1590 C  CD  . GLU A 1 204 ? -63.222 47.711 12.888  1.00 55.99  ? 204 GLU A CD  1 
ATOM   1591 O  OE1 . GLU A 1 204 ? -63.957 46.778 13.276  1.00 53.95  ? 204 GLU A OE1 1 
ATOM   1592 O  OE2 . GLU A 1 204 ? -63.665 48.829 12.547  1.00 57.31  ? 204 GLU A OE2 1 
ATOM   1593 N  N   . GLU A 1 205 ? -59.308 43.545 13.903  1.00 50.64  ? 205 GLU A N   1 
ATOM   1594 C  CA  . GLU A 1 205 ? -58.937 42.442 14.779  1.00 52.56  ? 205 GLU A CA  1 
ATOM   1595 C  C   . GLU A 1 205 ? -57.554 42.631 15.385  1.00 55.91  ? 205 GLU A C   1 
ATOM   1596 O  O   . GLU A 1 205 ? -57.224 41.961 16.369  1.00 53.59  ? 205 GLU A O   1 
ATOM   1597 C  CB  . GLU A 1 205 ? -58.997 41.120 14.010  1.00 54.27  ? 205 GLU A CB  1 
ATOM   1598 C  CG  . GLU A 1 205 ? -60.361 40.809 13.414  1.00 57.35  ? 205 GLU A CG  1 
ATOM   1599 C  CD  . GLU A 1 205 ? -61.389 40.433 14.464  1.00 58.87  ? 205 GLU A CD  1 
ATOM   1600 O  OE1 . GLU A 1 205 ? -60.990 39.935 15.538  1.00 59.79  ? 205 GLU A OE1 1 
ATOM   1601 O  OE2 . GLU A 1 205 ? -62.596 40.639 14.218  1.00 55.71  ? 205 GLU A OE2 1 
ATOM   1602 N  N   . LEU A 1 206 ? -56.746 43.530 14.827  1.00 52.63  ? 206 LEU A N   1 
ATOM   1603 C  CA  . LEU A 1 206 ? -55.405 43.806 15.323  1.00 52.60  ? 206 LEU A CA  1 
ATOM   1604 C  C   . LEU A 1 206 ? -55.382 44.863 16.420  1.00 53.57  ? 206 LEU A C   1 
ATOM   1605 O  O   . LEU A 1 206 ? -54.301 45.191 16.920  1.00 53.91  ? 206 LEU A O   1 
ATOM   1606 C  CB  . LEU A 1 206 ? -54.500 44.248 14.167  1.00 51.38  ? 206 LEU A CB  1 
ATOM   1607 C  CG  . LEU A 1 206 ? -54.440 43.322 12.950  1.00 50.30  ? 206 LEU A CG  1 
ATOM   1608 C  CD1 . LEU A 1 206 ? -53.631 43.956 11.829  1.00 52.11  ? 206 LEU A CD1 1 
ATOM   1609 C  CD2 . LEU A 1 206 ? -53.859 41.969 13.330  1.00 49.41  ? 206 LEU A CD2 1 
ATOM   1610 N  N   . ALA A 1 207 ? -56.537 45.403 16.804  1.00 53.40  ? 207 ALA A N   1 
ATOM   1611 C  CA  . ALA A 1 207 ? -56.581 46.429 17.833  1.00 53.12  ? 207 ALA A CA  1 
ATOM   1612 C  C   . ALA A 1 207 ? -56.166 45.854 19.185  1.00 60.69  ? 207 ALA A C   1 
ATOM   1613 O  O   . ALA A 1 207 ? -56.156 44.638 19.399  1.00 59.56  ? 207 ALA A O   1 
ATOM   1614 C  CB  . ALA A 1 207 ? -57.979 47.039 17.927  1.00 55.62  ? 207 ALA A CB  1 
ATOM   1615 N  N   . ALA A 1 208 ? -55.817 46.759 20.103  1.00 55.25  ? 208 ALA A N   1 
ATOM   1616 C  CA  . ALA A 1 208 ? -55.350 46.400 21.444  1.00 54.85  ? 208 ALA A CA  1 
ATOM   1617 C  C   . ALA A 1 208 ? -54.101 45.524 21.386  1.00 53.20  ? 208 ALA A C   1 
ATOM   1618 O  O   . ALA A 1 208 ? -53.952 44.570 22.153  1.00 54.84  ? 208 ALA A O   1 
ATOM   1619 C  CB  . ALA A 1 208 ? -56.455 45.721 22.259  1.00 58.62  ? 208 ALA A CB  1 
ATOM   1620 N  N   . GLY A 1 209 ? -53.196 45.849 20.464  1.00 54.42  ? 209 GLY A N   1 
ATOM   1621 C  CA  . GLY A 1 209 ? -51.914 45.169 20.398  1.00 56.02  ? 209 GLY A CA  1 
ATOM   1622 C  C   . GLY A 1 209 ? -51.992 43.710 20.017  1.00 55.52  ? 209 GLY A C   1 
ATOM   1623 O  O   . GLY A 1 209 ? -51.143 42.918 20.440  1.00 61.18  ? 209 GLY A O   1 
ATOM   1624 N  N   . LYS A 1 210 ? -52.991 43.328 19.228  1.00 53.29  ? 210 LYS A N   1 
ATOM   1625 C  CA  . LYS A 1 210 ? -53.161 41.944 18.812  1.00 55.38  ? 210 LYS A CA  1 
ATOM   1626 C  C   . LYS A 1 210 ? -52.529 41.648 17.457  1.00 53.59  ? 210 LYS A C   1 
ATOM   1627 O  O   . LYS A 1 210 ? -52.832 40.609 16.862  1.00 53.99  ? 210 LYS A O   1 
ATOM   1628 C  CB  . LYS A 1 210 ? -54.647 41.578 18.783  1.00 54.88  ? 210 LYS A CB  1 
ATOM   1629 C  CG  . LYS A 1 210 ? -55.315 41.637 20.141  1.00 57.47  ? 210 LYS A CG  1 
ATOM   1630 C  CD  . LYS A 1 210 ? -56.470 40.657 20.228  1.00 63.63  ? 210 LYS A CD  1 
ATOM   1631 C  CE  . LYS A 1 210 ? -57.200 40.798 21.550  1.00 80.89  ? 210 LYS A CE  1 
ATOM   1632 N  NZ  . LYS A 1 210 ? -56.368 41.508 22.561  1.00 76.77  ? 210 LYS A NZ  1 
ATOM   1633 N  N   . GLY A 1 211 ? -51.669 42.520 16.963  1.00 53.76  ? 211 GLY A N   1 
ATOM   1634 C  CA  . GLY A 1 211 ? -50.995 42.278 15.704  1.00 50.99  ? 211 GLY A CA  1 
ATOM   1635 C  C   . GLY A 1 211 ? -50.614 43.579 15.030  1.00 51.26  ? 211 GLY A C   1 
ATOM   1636 O  O   . GLY A 1 211 ? -50.938 44.670 15.492  1.00 53.39  ? 211 GLY A O   1 
ATOM   1637 N  N   . VAL A 1 212 ? -49.909 43.432 13.910  1.00 50.78  ? 212 VAL A N   1 
ATOM   1638 C  CA  . VAL A 1 212 ? -49.452 44.552 13.099  1.00 49.52  ? 212 VAL A CA  1 
ATOM   1639 C  C   . VAL A 1 212 ? -49.943 44.346 11.673  1.00 53.26  ? 212 VAL A C   1 
ATOM   1640 O  O   . VAL A 1 212 ? -50.033 43.216 11.183  1.00 54.38  ? 212 VAL A O   1 
ATOM   1641 C  CB  . VAL A 1 212 ? -47.911 44.698 13.145  1.00 50.03  ? 212 VAL A CB  1 
ATOM   1642 C  CG1 . VAL A 1 212 ? -47.231 43.437 12.631  1.00 49.83  ? 212 VAL A CG1 1 
ATOM   1643 C  CG2 . VAL A 1 212 ? -47.454 45.921 12.363  1.00 57.05  ? 212 VAL A CG2 1 
ATOM   1644 N  N   . TYR A 1 213 ? -50.280 45.450 11.010  1.00 57.29  ? 213 TYR A N   1 
ATOM   1645 C  CA  . TYR A 1 213 ? -50.778 45.424 9.637   1.00 53.62  ? 213 TYR A CA  1 
ATOM   1646 C  C   . TYR A 1 213 ? -49.620 45.731 8.693   1.00 52.27  ? 213 TYR A C   1 
ATOM   1647 O  O   . TYR A 1 213 ? -49.217 46.887 8.540   1.00 52.99  ? 213 TYR A O   1 
ATOM   1648 C  CB  . TYR A 1 213 ? -51.923 46.416 9.456   1.00 50.75  ? 213 TYR A CB  1 
ATOM   1649 C  CG  . TYR A 1 213 ? -52.351 46.596 8.015   1.00 56.85  ? 213 TYR A CG  1 
ATOM   1650 C  CD1 . TYR A 1 213 ? -53.133 45.641 7.378   1.00 55.85  ? 213 TYR A CD1 1 
ATOM   1651 C  CD2 . TYR A 1 213 ? -51.974 47.722 7.294   1.00 57.91  ? 213 TYR A CD2 1 
ATOM   1652 C  CE1 . TYR A 1 213 ? -53.525 45.799 6.062   1.00 52.96  ? 213 TYR A CE1 1 
ATOM   1653 C  CE2 . TYR A 1 213 ? -52.361 47.891 5.979   1.00 57.58  ? 213 TYR A CE2 1 
ATOM   1654 C  CZ  . TYR A 1 213 ? -53.136 46.926 5.369   1.00 55.40  ? 213 TYR A CZ  1 
ATOM   1655 O  OH  . TYR A 1 213 ? -53.523 47.090 4.059   1.00 56.85  ? 213 TYR A OH  1 
ATOM   1656 N  N   . THR A 1 214 ? -49.082 44.690 8.064   1.00 50.04  ? 214 THR A N   1 
ATOM   1657 C  CA  . THR A 1 214 ? -48.088 44.852 7.014   1.00 52.48  ? 214 THR A CA  1 
ATOM   1658 C  C   . THR A 1 214 ? -48.791 44.852 5.664   1.00 55.34  ? 214 THR A C   1 
ATOM   1659 O  O   . THR A 1 214 ? -49.742 44.095 5.449   1.00 54.95  ? 214 THR A O   1 
ATOM   1660 C  CB  . THR A 1 214 ? -47.047 43.734 7.068   1.00 57.15  ? 214 THR A CB  1 
ATOM   1661 O  OG1 . THR A 1 214 ? -47.643 42.503 6.642   1.00 56.20  ? 214 THR A OG1 1 
ATOM   1662 C  CG2 . THR A 1 214 ? -46.525 43.567 8.486   1.00 52.54  ? 214 THR A CG2 1 
ATOM   1663 N  N   . THR A 1 215 ? -48.333 45.711 4.757   1.00 61.23  ? 215 THR A N   1 
ATOM   1664 C  CA  . THR A 1 215 ? -49.036 45.889 3.494   1.00 66.11  ? 215 THR A CA  1 
ATOM   1665 C  C   . THR A 1 215 ? -48.066 45.961 2.326   1.00 68.08  ? 215 THR A C   1 
ATOM   1666 O  O   . THR A 1 215 ? -47.123 46.758 2.335   1.00 62.23  ? 215 THR A O   1 
ATOM   1667 C  CB  . THR A 1 215 ? -49.912 47.150 3.517   1.00 63.21  ? 215 THR A CB  1 
ATOM   1668 O  OG1 . THR A 1 215 ? -50.369 47.440 2.190   1.00 63.71  ? 215 THR A OG1 1 
ATOM   1669 C  CG2 . THR A 1 215 ? -49.140 48.346 4.062   1.00 58.97  ? 215 THR A CG2 1 
ATOM   1670 N  N   . HIS A 1 216 ? -48.300 45.109 1.332   1.00 74.27  ? 216 HIS A N   1 
ATOM   1671 C  CA  . HIS A 1 216 ? -47.817 45.349 -0.022  1.00 71.18  ? 216 HIS A CA  1 
ATOM   1672 C  C   . HIS A 1 216 ? -48.779 46.348 -0.651  1.00 71.79  ? 216 HIS A C   1 
ATOM   1673 O  O   . HIS A 1 216 ? -49.948 46.023 -0.889  1.00 80.21  ? 216 HIS A O   1 
ATOM   1674 C  CB  . HIS A 1 216 ? -47.752 44.039 -0.805  1.00 73.94  ? 216 HIS A CB  1 
ATOM   1675 C  CG  . HIS A 1 216 ? -47.259 44.184 -2.212  1.00 83.43  ? 216 HIS A CG  1 
ATOM   1676 N  ND1 . HIS A 1 216 ? -46.426 43.257 -2.802  1.00 82.38  ? 216 HIS A ND1 1 
ATOM   1677 C  CD2 . HIS A 1 216 ? -47.496 45.127 -3.155  1.00 84.43  ? 216 HIS A CD2 1 
ATOM   1678 C  CE1 . HIS A 1 216 ? -46.161 43.631 -4.042  1.00 79.84  ? 216 HIS A CE1 1 
ATOM   1679 N  NE2 . HIS A 1 216 ? -46.799 44.762 -4.280  1.00 85.12  ? 216 HIS A NE2 1 
ATOM   1680 N  N   . LEU A 1 217 ? -48.299 47.565 -0.899  1.00 74.57  ? 217 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 217 ? -49.175 48.656 -1.307  1.00 75.85  ? 217 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 217 ? -49.928 48.310 -2.587  1.00 77.84  ? 217 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 217 ? -49.481 47.498 -3.401  1.00 72.95  ? 217 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 217 ? -48.367 49.940 -1.503  1.00 71.14  ? 217 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 217 ? -47.749 50.552 -0.244  1.00 69.95  ? 217 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 217 ? -46.875 51.743 -0.602  1.00 71.53  ? 217 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 217 ? -48.832 50.959 0.744   1.00 69.05  ? 217 LEU A CD2 1 
ATOM   1688 N  N   . ARG A 1 218 ? -51.097 48.936 -2.752  1.00 71.26  ? 218 ARG A N   1 
ATOM   1689 C  CA  . ARG A 1 218 ? -51.912 48.693 -3.937  1.00 71.68  ? 218 ARG A CA  1 
ATOM   1690 C  C   . ARG A 1 218 ? -51.209 49.143 -5.210  1.00 74.15  ? 218 ARG A C   1 
ATOM   1691 O  O   . ARG A 1 218 ? -51.529 48.642 -6.294  1.00 82.09  ? 218 ARG A O   1 
ATOM   1692 C  CB  . ARG A 1 218 ? -53.265 49.396 -3.794  1.00 73.81  ? 218 ARG A CB  1 
ATOM   1693 C  CG  . ARG A 1 218 ? -54.344 48.876 -4.736  1.00 73.85  ? 218 ARG A CG  1 
ATOM   1694 C  CD  . ARG A 1 218 ? -55.705 49.476 -4.412  1.00 72.96  ? 218 ARG A CD  1 
ATOM   1695 N  NE  . ARG A 1 218 ? -56.208 49.037 -3.115  1.00 76.44  ? 218 ARG A NE  1 
ATOM   1696 C  CZ  . ARG A 1 218 ? -57.024 48.007 -2.935  1.00 78.56  ? 218 ARG A CZ  1 
ATOM   1697 N  NH1 . ARG A 1 218 ? -57.457 47.282 -3.954  1.00 73.16  ? 218 ARG A NH1 1 
ATOM   1698 N  NH2 . ARG A 1 218 ? -57.417 47.697 -1.703  1.00 77.41  ? 218 ARG A NH2 1 
ATOM   1699 N  N   . SER A 1 219 ? -50.258 50.067 -5.102  1.00 72.40  ? 219 SER A N   1 
ATOM   1700 C  CA  . SER A 1 219 ? -49.423 50.465 -6.226  1.00 80.66  ? 219 SER A CA  1 
ATOM   1701 C  C   . SER A 1 219 ? -48.131 51.054 -5.685  1.00 83.20  ? 219 SER A C   1 
ATOM   1702 O  O   . SER A 1 219 ? -48.164 51.943 -4.829  1.00 78.40  ? 219 SER A O   1 
ATOM   1703 C  CB  . SER A 1 219 ? -50.135 51.482 -7.124  1.00 81.84  ? 219 SER A CB  1 
ATOM   1704 O  OG  . SER A 1 219 ? -49.318 51.834 -8.228  1.00 79.09  ? 219 SER A OG  1 
ATOM   1705 N  N   . GLU A 1 220 ? -47.002 50.552 -6.178  1.00 83.82  ? 220 GLU A N   1 
ATOM   1706 C  CA  . GLU A 1 220 ? -45.682 51.055 -5.816  1.00 83.66  ? 220 GLU A CA  1 
ATOM   1707 C  C   . GLU A 1 220 ? -45.061 51.848 -6.962  1.00 85.29  ? 220 GLU A C   1 
ATOM   1708 O  O   . GLU A 1 220 ? -43.854 51.783 -7.204  1.00 84.89  ? 220 GLU A O   1 
ATOM   1709 C  CB  . GLU A 1 220 ? -44.762 49.915 -5.391  1.00 82.11  ? 220 GLU A CB  1 
ATOM   1710 C  CG  . GLU A 1 220 ? -45.079 49.344 -4.021  1.00 80.37  ? 220 GLU A CG  1 
ATOM   1711 C  CD  . GLU A 1 220 ? -43.883 48.666 -3.387  1.00 86.30  ? 220 GLU A CD  1 
ATOM   1712 O  OE1 . GLU A 1 220 ? -43.369 47.688 -3.971  1.00 80.72  ? 220 GLU A OE1 1 
ATOM   1713 O  OE2 . GLU A 1 220 ? -43.446 49.123 -2.309  1.00 88.61  ? 220 GLU A OE2 1 
ATOM   1714 N  N   . PHE A 1 221 ? -45.886 52.608 -7.681  1.00 85.76  ? 221 PHE A N   1 
ATOM   1715 C  CA  . PHE A 1 221 ? -45.406 53.408 -8.801  1.00 90.43  ? 221 PHE A CA  1 
ATOM   1716 C  C   . PHE A 1 221 ? -45.902 54.844 -8.695  1.00 93.11  ? 221 PHE A C   1 
ATOM   1717 O  O   . PHE A 1 221 ? -45.584 55.546 -7.729  1.00 96.72  ? 221 PHE A O   1 
ATOM   1718 C  CB  . PHE A 1 221 ? -45.840 52.783 -10.129 1.00 89.60  ? 221 PHE A CB  1 
ATOM   1719 C  CG  . PHE A 1 221 ? -45.186 51.462 -10.416 1.00 90.17  ? 221 PHE A CG  1 
ATOM   1720 C  CD1 . PHE A 1 221 ? -45.741 50.282 -9.950  1.00 90.23  ? 221 PHE A CD1 1 
ATOM   1721 C  CD2 . PHE A 1 221 ? -44.012 51.400 -11.149 1.00 90.27  ? 221 PHE A CD2 1 
ATOM   1722 C  CE1 . PHE A 1 221 ? -45.140 49.065 -10.211 1.00 90.29  ? 221 PHE A CE1 1 
ATOM   1723 C  CE2 . PHE A 1 221 ? -43.406 50.186 -11.413 1.00 91.41  ? 221 PHE A CE2 1 
ATOM   1724 C  CZ  . PHE A 1 221 ? -43.971 49.018 -10.943 1.00 90.24  ? 221 PHE A CZ  1 
ATOM   1725 N  N   A GLU A 1 222 ? -46.684 55.291 -9.685  0.42 90.20  ? 222 GLU A N   1 
ATOM   1726 N  N   B GLU A 1 222 ? -46.682 55.294 -9.686  0.58 90.20  ? 222 GLU A N   1 
ATOM   1727 C  CA  A GLU A 1 222 ? -47.179 56.664 -9.663  0.42 89.76  ? 222 GLU A CA  1 
ATOM   1728 C  CA  B GLU A 1 222 ? -47.174 56.669 -9.657  0.58 89.76  ? 222 GLU A CA  1 
ATOM   1729 C  C   A GLU A 1 222 ? -48.154 56.915 -8.512  0.42 88.24  ? 222 GLU A C   1 
ATOM   1730 C  C   B GLU A 1 222 ? -48.148 56.911 -8.503  0.58 88.25  ? 222 GLU A C   1 
ATOM   1731 O  O   A GLU A 1 222 ? -47.944 57.876 -7.758  0.42 89.12  ? 222 GLU A O   1 
ATOM   1732 O  O   B GLU A 1 222 ? -47.932 57.860 -7.736  0.58 89.34  ? 222 GLU A O   1 
ATOM   1733 C  CB  A GLU A 1 222 ? -47.796 57.024 -11.019 0.42 89.85  ? 222 GLU A CB  1 
ATOM   1734 C  CB  B GLU A 1 222 ? -47.786 57.037 -11.013 0.58 89.84  ? 222 GLU A CB  1 
ATOM   1735 C  CG  A GLU A 1 222 ? -46.790 57.184 -12.150 0.42 92.90  ? 222 GLU A CG  1 
ATOM   1736 C  CG  B GLU A 1 222 ? -48.035 58.530 -11.215 0.58 91.26  ? 222 GLU A CG  1 
ATOM   1737 C  CD  A GLU A 1 222 ? -46.221 55.862 -12.628 0.42 92.93  ? 222 GLU A CD  1 
ATOM   1738 C  CD  B GLU A 1 222 ? -49.314 59.016 -10.557 0.58 90.30  ? 222 GLU A CD  1 
ATOM   1739 O  OE1 A GLU A 1 222 ? -46.927 54.838 -12.528 0.42 92.25  ? 222 GLU A OE1 1 
ATOM   1740 O  OE1 B GLU A 1 222 ? -50.307 58.258 -10.549 0.58 89.06  ? 222 GLU A OE1 1 
ATOM   1741 O  OE2 A GLU A 1 222 ? -45.063 55.848 -13.098 0.42 92.55  ? 222 GLU A OE2 1 
ATOM   1742 O  OE2 B GLU A 1 222 ? -49.323 60.154 -10.041 0.58 90.10  ? 222 GLU A OE2 1 
ATOM   1743 N  N   . PRO A 1 223 ? -49.216 56.107 -8.322  1.00 93.39  ? 223 PRO A N   1 
ATOM   1744 C  CA  . PRO A 1 223 ? -50.142 56.401 -7.214  1.00 90.07  ? 223 PRO A CA  1 
ATOM   1745 C  C   . PRO A 1 223 ? -49.700 55.797 -5.890  1.00 88.55  ? 223 PRO A C   1 
ATOM   1746 O  O   . PRO A 1 223 ? -50.517 55.225 -5.162  1.00 87.86  ? 223 PRO A O   1 
ATOM   1747 C  CB  . PRO A 1 223 ? -51.466 55.780 -7.693  1.00 87.93  ? 223 PRO A CB  1 
ATOM   1748 C  CG  . PRO A 1 223 ? -51.152 55.046 -8.988  1.00 85.40  ? 223 PRO A CG  1 
ATOM   1749 C  CD  . PRO A 1 223 ? -49.671 54.926 -9.066  1.00 88.24  ? 223 PRO A CD  1 
ATOM   1750 N  N   . ILE A 1 224 ? -48.415 55.925 -5.556  1.00 85.01  ? 224 ILE A N   1 
ATOM   1751 C  CA  . ILE A 1 224 ? -47.920 55.340 -4.314  1.00 82.27  ? 224 ILE A CA  1 
ATOM   1752 C  C   . ILE A 1 224 ? -48.322 56.193 -3.116  1.00 80.10  ? 224 ILE A C   1 
ATOM   1753 O  O   . ILE A 1 224 ? -48.597 55.667 -2.032  1.00 82.16  ? 224 ILE A O   1 
ATOM   1754 C  CB  . ILE A 1 224 ? -46.395 55.134 -4.385  1.00 82.38  ? 224 ILE A CB  1 
ATOM   1755 C  CG1 . ILE A 1 224 ? -45.903 54.390 -3.142  1.00 76.91  ? 224 ILE A CG1 1 
ATOM   1756 C  CG2 . ILE A 1 224 ? -45.669 56.464 -4.549  1.00 82.22  ? 224 ILE A CG2 1 
ATOM   1757 C  CD1 . ILE A 1 224 ? -44.420 54.111 -3.142  1.00 77.24  ? 224 ILE A CD1 1 
ATOM   1758 N  N   . LEU A 1 225 ? -48.365 57.518 -3.288  1.00 79.93  ? 225 LEU A N   1 
ATOM   1759 C  CA  . LEU A 1 225 ? -48.886 58.377 -2.231  1.00 79.65  ? 225 LEU A CA  1 
ATOM   1760 C  C   . LEU A 1 225 ? -50.366 58.114 -1.994  1.00 84.57  ? 225 LEU A C   1 
ATOM   1761 O  O   . LEU A 1 225 ? -50.852 58.261 -0.867  1.00 83.52  ? 225 LEU A O   1 
ATOM   1762 C  CB  . LEU A 1 225 ? -48.651 59.847 -2.580  1.00 74.85  ? 225 LEU A CB  1 
ATOM   1763 C  CG  . LEU A 1 225 ? -47.198 60.329 -2.596  1.00 76.05  ? 225 LEU A CG  1 
ATOM   1764 C  CD1 . LEU A 1 225 ? -47.114 61.780 -3.049  1.00 74.21  ? 225 LEU A CD1 1 
ATOM   1765 C  CD2 . LEU A 1 225 ? -46.558 60.157 -1.225  1.00 74.30  ? 225 LEU A CD2 1 
ATOM   1766 N  N   . GLU A 1 226 ? -51.094 57.724 -3.043  1.00 90.24  ? 226 GLU A N   1 
ATOM   1767 C  CA  . GLU A 1 226 ? -52.479 57.297 -2.873  1.00 87.59  ? 226 GLU A CA  1 
ATOM   1768 C  C   . GLU A 1 226 ? -52.558 56.020 -2.044  1.00 87.13  ? 226 GLU A C   1 
ATOM   1769 O  O   . GLU A 1 226 ? -53.347 55.927 -1.096  1.00 87.21  ? 226 GLU A O   1 
ATOM   1770 C  CB  . GLU A 1 226 ? -53.136 57.094 -4.239  1.00 95.54  ? 226 GLU A CB  1 
ATOM   1771 C  CG  . GLU A 1 226 ? -54.148 55.958 -4.273  1.00 115.30 ? 226 GLU A CG  1 
ATOM   1772 C  CD  . GLU A 1 226 ? -54.899 55.868 -5.585  1.00 121.07 ? 226 GLU A CD  1 
ATOM   1773 O  OE1 . GLU A 1 226 ? -54.339 56.270 -6.626  1.00 114.84 ? 226 GLU A OE1 1 
ATOM   1774 O  OE2 . GLU A 1 226 ? -56.055 55.401 -5.572  1.00 121.12 ? 226 GLU A OE2 1 
ATOM   1775 N  N   . ALA A 1 227 ? -51.738 55.023 -2.389  1.00 86.88  ? 227 ALA A N   1 
ATOM   1776 C  CA  . ALA A 1 227 ? -51.744 53.764 -1.651  1.00 87.84  ? 227 ALA A CA  1 
ATOM   1777 C  C   . ALA A 1 227 ? -51.228 53.944 -0.230  1.00 82.10  ? 227 ALA A C   1 
ATOM   1778 O  O   . ALA A 1 227 ? -51.691 53.256 0.688   1.00 81.81  ? 227 ALA A O   1 
ATOM   1779 C  CB  . ALA A 1 227 ? -50.912 52.717 -2.390  1.00 81.17  ? 227 ALA A CB  1 
ATOM   1780 N  N   . LEU A 1 228 ? -50.268 54.850 -0.033  1.00 73.51  ? 228 LEU A N   1 
ATOM   1781 C  CA  . LEU A 1 228 ? -49.811 55.164 1.316   1.00 77.07  ? 228 LEU A CA  1 
ATOM   1782 C  C   . LEU A 1 228 ? -50.903 55.860 2.118   1.00 82.23  ? 228 LEU A C   1 
ATOM   1783 O  O   . LEU A 1 228 ? -51.100 55.554 3.301   1.00 79.74  ? 228 LEU A O   1 
ATOM   1784 C  CB  . LEU A 1 228 ? -48.548 56.024 1.255   1.00 72.17  ? 228 LEU A CB  1 
ATOM   1785 C  CG  . LEU A 1 228 ? -47.219 55.278 1.145   1.00 67.77  ? 228 LEU A CG  1 
ATOM   1786 C  CD1 . LEU A 1 228 ? -46.135 56.201 0.611   1.00 68.18  ? 228 LEU A CD1 1 
ATOM   1787 C  CD2 . LEU A 1 228 ? -46.833 54.721 2.505   1.00 69.08  ? 228 LEU A CD2 1 
ATOM   1788 N  N   . ASP A 1 229 ? -51.627 56.793 1.491   1.00 89.54  ? 229 ASP A N   1 
ATOM   1789 C  CA  . ASP A 1 229 ? -52.743 57.441 2.174   1.00 88.07  ? 229 ASP A CA  1 
ATOM   1790 C  C   . ASP A 1 229 ? -53.813 56.430 2.552   1.00 82.37  ? 229 ASP A C   1 
ATOM   1791 O  O   . ASP A 1 229 ? -54.427 56.541 3.619   1.00 83.04  ? 229 ASP A O   1 
ATOM   1792 C  CB  . ASP A 1 229 ? -53.348 58.540 1.305   1.00 86.74  ? 229 ASP A CB  1 
ATOM   1793 C  CG  . ASP A 1 229 ? -54.626 59.102 1.899   1.00 90.98  ? 229 ASP A CG  1 
ATOM   1794 O  OD1 . ASP A 1 229 ? -54.559 59.713 2.986   1.00 95.24  ? 229 ASP A OD1 1 
ATOM   1795 O  OD2 . ASP A 1 229 ? -55.702 58.909 1.296   1.00 97.45  ? 229 ASP A OD2 1 
ATOM   1796 N  N   . GLU A 1 230 ? -54.069 55.452 1.682   1.00 80.86  ? 230 GLU A N   1 
ATOM   1797 C  CA  . GLU A 1 230 ? -54.887 54.311 2.080   1.00 79.62  ? 230 GLU A CA  1 
ATOM   1798 C  C   . GLU A 1 230 ? -54.299 53.668 3.329   1.00 78.02  ? 230 GLU A C   1 
ATOM   1799 O  O   . GLU A 1 230 ? -54.802 53.881 4.438   1.00 80.86  ? 230 GLU A O   1 
ATOM   1800 C  CB  . GLU A 1 230 ? -54.987 53.268 0.962   1.00 77.35  ? 230 GLU A CB  1 
ATOM   1801 C  CG  . GLU A 1 230 ? -56.124 52.264 1.146   1.00 77.37  ? 230 GLU A CG  1 
ATOM   1802 C  CD  . GLU A 1 230 ? -56.240 51.285 -0.016  1.00 80.79  ? 230 GLU A CD  1 
ATOM   1803 O  OE1 . GLU A 1 230 ? -55.401 51.321 -0.946  1.00 81.85  ? 230 GLU A OE1 1 
ATOM   1804 O  OE2 . GLU A 1 230 ? -57.185 50.472 0.003   1.00 77.86  ? 230 GLU A OE2 1 
ATOM   1805 N  N   . ALA A 1 231 ? -53.204 52.926 3.152   1.00 75.25  ? 231 ALA A N   1 
ATOM   1806 C  CA  . ALA A 1 231 ? -52.517 52.193 4.213   1.00 71.86  ? 231 ALA A CA  1 
ATOM   1807 C  C   . ALA A 1 231 ? -52.574 52.870 5.581   1.00 69.31  ? 231 ALA A C   1 
ATOM   1808 O  O   . ALA A 1 231 ? -52.777 52.203 6.601   1.00 70.80  ? 231 ALA A O   1 
ATOM   1809 C  CB  . ALA A 1 231 ? -51.051 51.974 3.819   1.00 71.06  ? 231 ALA A CB  1 
ATOM   1810 N  N   . PHE A 1 232 ? -52.411 54.196 5.612   1.00 70.89  ? 232 PHE A N   1 
ATOM   1811 C  CA  . PHE A 1 232 ? -52.457 54.925 6.875   1.00 72.47  ? 232 PHE A CA  1 
ATOM   1812 C  C   . PHE A 1 232 ? -53.883 55.090 7.388   1.00 79.32  ? 232 PHE A C   1 
ATOM   1813 O  O   . PHE A 1 232 ? -54.090 55.195 8.602   1.00 72.76  ? 232 PHE A O   1 
ATOM   1814 C  CB  . PHE A 1 232 ? -51.792 56.295 6.724   1.00 72.48  ? 232 PHE A CB  1 
ATOM   1815 C  CG  . PHE A 1 232 ? -50.339 56.229 6.346   1.00 72.48  ? 232 PHE A CG  1 
ATOM   1816 C  CD1 . PHE A 1 232 ? -49.615 55.062 6.520   1.00 72.46  ? 232 PHE A CD1 1 
ATOM   1817 C  CD2 . PHE A 1 232 ? -49.697 57.336 5.816   1.00 72.86  ? 232 PHE A CD2 1 
ATOM   1818 C  CE1 . PHE A 1 232 ? -48.285 54.997 6.167   1.00 66.98  ? 232 PHE A CE1 1 
ATOM   1819 C  CE2 . PHE A 1 232 ? -48.363 57.278 5.466   1.00 72.81  ? 232 PHE A CE2 1 
ATOM   1820 C  CZ  . PHE A 1 232 ? -47.656 56.107 5.644   1.00 68.12  ? 232 PHE A CZ  1 
ATOM   1821 N  N   . ARG A 1 233 ? -54.874 55.105 6.493   1.00 74.66  ? 233 ARG A N   1 
ATOM   1822 C  CA  . ARG A 1 233 ? -56.258 55.260 6.932   1.00 72.08  ? 233 ARG A CA  1 
ATOM   1823 C  C   . ARG A 1 233 ? -56.788 53.982 7.575   1.00 70.16  ? 233 ARG A C   1 
ATOM   1824 O  O   . ARG A 1 233 ? -57.548 54.048 8.549   1.00 80.92  ? 233 ARG A O   1 
ATOM   1825 C  CB  . ARG A 1 233 ? -57.137 55.675 5.753   1.00 75.56  ? 233 ARG A CB  1 
ATOM   1826 C  CG  . ARG A 1 233 ? -57.133 57.168 5.448   1.00 81.73  ? 233 ARG A CG  1 
ATOM   1827 C  CD  . ARG A 1 233 ? -57.458 57.409 3.982   1.00 86.94  ? 233 ARG A CD  1 
ATOM   1828 N  NE  . ARG A 1 233 ? -58.552 56.560 3.528   1.00 92.53  ? 233 ARG A NE  1 
ATOM   1829 C  CZ  . ARG A 1 233 ? -58.714 56.150 2.277   1.00 94.07  ? 233 ARG A CZ  1 
ATOM   1830 N  NH1 . ARG A 1 233 ? -57.860 56.484 1.324   1.00 93.44  ? 233 ARG A NH1 1 
ATOM   1831 N  NH2 . ARG A 1 233 ? -59.754 55.377 1.977   1.00 88.52  ? 233 ARG A NH2 1 
ATOM   1832 N  N   . ILE A 1 234 ? -56.416 52.813 7.041   1.00 67.00  ? 234 ILE A N   1 
ATOM   1833 C  CA  . ILE A 1 234 ? -56.858 51.556 7.641   1.00 72.18  ? 234 ILE A CA  1 
ATOM   1834 C  C   . ILE A 1 234 ? -56.229 51.384 9.023   1.00 65.04  ? 234 ILE A C   1 
ATOM   1835 O  O   . ILE A 1 234 ? -56.871 50.897 9.965   1.00 65.07  ? 234 ILE A O   1 
ATOM   1836 C  CB  . ILE A 1 234 ? -56.538 50.360 6.716   1.00 70.29  ? 234 ILE A CB  1 
ATOM   1837 C  CG1 . ILE A 1 234 ? -56.942 50.650 5.244   1.00 67.32  ? 234 ILE A CG1 1 
ATOM   1838 C  CG2 . ILE A 1 234 ? -57.197 49.090 7.303   1.00 66.23  ? 234 ILE A CG2 1 
ATOM   1839 C  CD1 . ILE A 1 234 ? -55.923 50.258 4.155   1.00 67.91  ? 234 ILE A CD1 1 
ATOM   1840 N  N   . GLY A 1 235 ? -54.962 51.780 9.163   1.00 66.22  ? 235 GLY A N   1 
ATOM   1841 C  CA  . GLY A 1 235 ? -54.342 51.795 10.476  1.00 73.34  ? 235 GLY A CA  1 
ATOM   1842 C  C   . GLY A 1 235 ? -54.993 52.801 11.400  1.00 72.61  ? 235 GLY A C   1 
ATOM   1843 O  O   . GLY A 1 235 ? -55.124 52.559 12.601  1.00 67.50  ? 235 GLY A O   1 
ATOM   1844 N  N   . ARG A 1 236 ? -55.427 53.936 10.850  1.00 66.84  ? 236 ARG A N   1 
ATOM   1845 C  CA  . ARG A 1 236 ? -56.111 54.939 11.654  1.00 65.61  ? 236 ARG A CA  1 
ATOM   1846 C  C   . ARG A 1 236 ? -57.546 54.542 11.970  1.00 63.97  ? 236 ARG A C   1 
ATOM   1847 O  O   . ARG A 1 236 ? -58.120 55.057 12.935  1.00 61.34  ? 236 ARG A O   1 
ATOM   1848 C  CB  . ARG A 1 236 ? -56.087 56.291 10.938  1.00 64.53  ? 236 ARG A CB  1 
ATOM   1849 C  CG  . ARG A 1 236 ? -55.362 57.382 11.711  1.00 71.14  ? 236 ARG A CG  1 
ATOM   1850 C  CD  . ARG A 1 236 ? -55.357 58.710 10.964  1.00 72.30  ? 236 ARG A CD  1 
ATOM   1851 N  NE  . ARG A 1 236 ? -54.679 58.628 9.675   1.00 75.05  ? 236 ARG A NE  1 
ATOM   1852 C  CZ  . ARG A 1 236 ? -55.276 58.791 8.501   1.00 74.88  ? 236 ARG A CZ  1 
ATOM   1853 N  NH1 . ARG A 1 236 ? -56.568 59.061 8.413   1.00 73.16  ? 236 ARG A NH1 1 
ATOM   1854 N  NH2 . ARG A 1 236 ? -54.555 58.690 7.388   1.00 77.21  ? 236 ARG A NH2 1 
ATOM   1855 N  N   . HIS A 1 237 ? -58.132 53.635 11.186  1.00 65.41  ? 237 HIS A N   1 
ATOM   1856 C  CA  . HIS A 1 237 ? -59.509 53.222 11.433  1.00 62.20  ? 237 HIS A CA  1 
ATOM   1857 C  C   . HIS A 1 237 ? -59.597 52.312 12.651  1.00 58.84  ? 237 HIS A C   1 
ATOM   1858 O  O   . HIS A 1 237 ? -60.465 52.491 13.512  1.00 60.55  ? 237 HIS A O   1 
ATOM   1859 C  CB  . HIS A 1 237 ? -60.077 52.528 10.195  1.00 62.44  ? 237 HIS A CB  1 
ATOM   1860 C  CG  . HIS A 1 237 ? -61.555 52.303 10.253  1.00 61.22  ? 237 HIS A CG  1 
ATOM   1861 N  ND1 . HIS A 1 237 ? -62.111 51.074 10.538  1.00 61.91  ? 237 HIS A ND1 1 
ATOM   1862 C  CD2 . HIS A 1 237 ? -62.594 53.151 10.067  1.00 59.01  ? 237 HIS A CD2 1 
ATOM   1863 C  CE1 . HIS A 1 237 ? -63.428 51.175 10.523  1.00 59.04  ? 237 HIS A CE1 1 
ATOM   1864 N  NE2 . HIS A 1 237 ? -63.747 52.425 10.240  1.00 57.71  ? 237 HIS A NE2 1 
ATOM   1865 N  N   . GLY A 1 238 ? -58.706 51.330 12.741  1.00 58.27  ? 238 GLY A N   1 
ATOM   1866 C  CA  . GLY A 1 238 ? -58.665 50.427 13.867  1.00 67.29  ? 238 GLY A CA  1 
ATOM   1867 C  C   . GLY A 1 238 ? -57.614 50.736 14.906  1.00 64.32  ? 238 GLY A C   1 
ATOM   1868 O  O   . GLY A 1 238 ? -57.476 49.972 15.867  1.00 65.97  ? 238 GLY A O   1 
ATOM   1869 N  N   . ASN A 1 239 ? -56.874 51.836 14.750  1.00 61.37  ? 239 ASN A N   1 
ATOM   1870 C  CA  . ASN A 1 239 ? -55.777 52.199 15.648  1.00 62.88  ? 239 ASN A CA  1 
ATOM   1871 C  C   . ASN A 1 239 ? -54.785 51.047 15.789  1.00 61.16  ? 239 ASN A C   1 
ATOM   1872 O  O   . ASN A 1 239 ? -54.458 50.598 16.890  1.00 63.72  ? 239 ASN A O   1 
ATOM   1873 C  CB  . ASN A 1 239 ? -56.306 52.650 17.010  1.00 65.56  ? 239 ASN A CB  1 
ATOM   1874 C  CG  . ASN A 1 239 ? -56.620 54.134 17.049  1.00 70.92  ? 239 ASN A CG  1 
ATOM   1875 O  OD1 . ASN A 1 239 ? -57.447 54.627 16.280  1.00 69.28  ? 239 ASN A OD1 1 
ATOM   1876 N  ND2 . ASN A 1 239 ? -55.962 54.855 17.950  1.00 88.66  ? 239 ASN A ND2 1 
ATOM   1877 N  N   . VAL A 1 240 ? -54.304 50.567 14.647  1.00 60.31  ? 240 VAL A N   1 
ATOM   1878 C  CA  . VAL A 1 240 ? -53.385 49.433 14.600  1.00 59.38  ? 240 VAL A CA  1 
ATOM   1879 C  C   . VAL A 1 240 ? -52.087 49.872 13.930  1.00 60.69  ? 240 VAL A C   1 
ATOM   1880 O  O   . VAL A 1 240 ? -52.099 50.794 13.101  1.00 59.60  ? 240 VAL A O   1 
ATOM   1881 C  CB  . VAL A 1 240 ? -54.017 48.238 13.869  1.00 59.03  ? 240 VAL A CB  1 
ATOM   1882 C  CG1 . VAL A 1 240 ? -55.291 47.809 14.573  1.00 57.94  ? 240 VAL A CG1 1 
ATOM   1883 C  CG2 . VAL A 1 240 ? -54.302 48.589 12.415  1.00 59.22  ? 240 VAL A CG2 1 
ATOM   1884 N  N   . PRO A 1 241 ? -50.952 49.263 14.264  1.00 59.89  ? 241 PRO A N   1 
ATOM   1885 C  CA  . PRO A 1 241 ? -49.693 49.653 13.622  1.00 56.33  ? 241 PRO A CA  1 
ATOM   1886 C  C   . PRO A 1 241 ? -49.661 49.241 12.160  1.00 58.82  ? 241 PRO A C   1 
ATOM   1887 O  O   . PRO A 1 241 ? -50.258 48.239 11.756  1.00 58.55  ? 241 PRO A O   1 
ATOM   1888 C  CB  . PRO A 1 241 ? -48.630 48.902 14.435  1.00 56.14  ? 241 PRO A CB  1 
ATOM   1889 C  CG  . PRO A 1 241 ? -49.311 48.535 15.723  1.00 58.78  ? 241 PRO A CG  1 
ATOM   1890 C  CD  . PRO A 1 241 ? -50.737 48.292 15.350  1.00 57.76  ? 241 PRO A CD  1 
ATOM   1891 N  N   . VAL A 1 242 ? -48.950 50.033 11.361  1.00 57.06  ? 242 VAL A N   1 
ATOM   1892 C  CA  . VAL A 1 242 ? -48.833 49.815 9.924   1.00 55.87  ? 242 VAL A CA  1 
ATOM   1893 C  C   . VAL A 1 242 ? -47.358 49.692 9.571   1.00 56.56  ? 242 VAL A C   1 
ATOM   1894 O  O   . VAL A 1 242 ? -46.535 50.492 10.030  1.00 57.56  ? 242 VAL A O   1 
ATOM   1895 C  CB  . VAL A 1 242 ? -49.487 50.953 9.118   1.00 60.84  ? 242 VAL A CB  1 
ATOM   1896 C  CG1 . VAL A 1 242 ? -49.425 50.652 7.627   1.00 56.16  ? 242 VAL A CG1 1 
ATOM   1897 C  CG2 . VAL A 1 242 ? -50.923 51.163 9.563   1.00 62.93  ? 242 VAL A CG2 1 
ATOM   1898 N  N   . VAL A 1 243 ? -47.029 48.693 8.758   1.00 60.27  ? 243 VAL A N   1 
ATOM   1899 C  CA  . VAL A 1 243 ? -45.679 48.498 8.240   1.00 60.34  ? 243 VAL A CA  1 
ATOM   1900 C  C   . VAL A 1 243 ? -45.772 48.381 6.726   1.00 56.66  ? 243 VAL A C   1 
ATOM   1901 O  O   . VAL A 1 243 ? -46.360 47.424 6.209   1.00 55.16  ? 243 VAL A O   1 
ATOM   1902 C  CB  . VAL A 1 243 ? -45.001 47.254 8.836   1.00 56.32  ? 243 VAL A CB  1 
ATOM   1903 C  CG1 . VAL A 1 243 ? -43.689 46.975 8.122   1.00 57.26  ? 243 VAL A CG1 1 
ATOM   1904 C  CG2 . VAL A 1 243 ? -44.767 47.443 10.326  1.00 57.96  ? 243 VAL A CG2 1 
ATOM   1905 N  N   . VAL A 1 244 ? -45.200 49.350 6.018   1.00 57.77  ? 244 VAL A N   1 
ATOM   1906 C  CA  . VAL A 1 244 ? -45.182 49.326 4.559   1.00 57.41  ? 244 VAL A CA  1 
ATOM   1907 C  C   . VAL A 1 244 ? -44.110 48.334 4.115   1.00 58.58  ? 244 VAL A C   1 
ATOM   1908 O  O   . VAL A 1 244 ? -42.915 48.565 4.315   1.00 61.03  ? 244 VAL A O   1 
ATOM   1909 C  CB  . VAL A 1 244 ? -44.927 50.721 3.977   1.00 57.65  ? 244 VAL A CB  1 
ATOM   1910 C  CG1 . VAL A 1 244 ? -44.809 50.654 2.465   1.00 59.29  ? 244 VAL A CG1 1 
ATOM   1911 C  CG2 . VAL A 1 244 ? -46.044 51.672 4.386   1.00 59.92  ? 244 VAL A CG2 1 
ATOM   1912 N  N   . SER A 1 245 ? -44.538 47.226 3.516   1.00 58.67  ? 245 SER A N   1 
ATOM   1913 C  CA  . SER A 1 245 ? -43.612 46.192 3.075   1.00 61.08  ? 245 SER A CA  1 
ATOM   1914 C  C   . SER A 1 245 ? -42.829 46.643 1.846   1.00 61.05  ? 245 SER A C   1 
ATOM   1915 O  O   . SER A 1 245 ? -43.337 47.384 0.999   1.00 65.71  ? 245 SER A O   1 
ATOM   1916 C  CB  . SER A 1 245 ? -44.367 44.899 2.761   1.00 62.92  ? 245 SER A CB  1 
ATOM   1917 O  OG  . SER A 1 245 ? -45.004 44.379 3.913   1.00 66.42  ? 245 SER A OG  1 
ATOM   1918 N  N   . HIS A 1 246 ? -41.584 46.154 1.754   1.00 62.90  ? 246 HIS A N   1 
ATOM   1919 C  CA  . HIS A 1 246 ? -40.597 46.475 0.721   1.00 68.63  ? 246 HIS A CA  1 
ATOM   1920 C  C   . HIS A 1 246 ? -40.830 47.831 0.066   1.00 71.43  ? 246 HIS A C   1 
ATOM   1921 O  O   . HIS A 1 246 ? -41.094 47.910 -1.139  1.00 74.64  ? 246 HIS A O   1 
ATOM   1922 C  CB  . HIS A 1 246 ? -40.559 45.377 -0.348  1.00 70.08  ? 246 HIS A CB  1 
ATOM   1923 C  CG  . HIS A 1 246 ? -41.909 44.977 -0.850  1.00 70.55  ? 246 HIS A CG  1 
ATOM   1924 N  ND1 . HIS A 1 246 ? -42.863 45.895 -1.231  1.00 72.46  ? 246 HIS A ND1 1 
ATOM   1925 C  CD2 . HIS A 1 246 ? -42.468 43.757 -1.032  1.00 69.23  ? 246 HIS A CD2 1 
ATOM   1926 C  CE1 . HIS A 1 246 ? -43.952 45.260 -1.625  1.00 79.14  ? 246 HIS A CE1 1 
ATOM   1927 N  NE2 . HIS A 1 246 ? -43.738 43.962 -1.515  1.00 73.74  ? 246 HIS A NE2 1 
ATOM   1928 N  N   . HIS A 1 247 ? -40.742 48.898 0.856   1.00 64.97  ? 247 HIS A N   1 
ATOM   1929 C  CA  . HIS A 1 247 ? -40.988 50.234 0.335   1.00 69.02  ? 247 HIS A CA  1 
ATOM   1930 C  C   . HIS A 1 247 ? -39.959 50.590 -0.727  1.00 72.77  ? 247 HIS A C   1 
ATOM   1931 O  O   . HIS A 1 247 ? -38.749 50.527 -0.489  1.00 68.37  ? 247 HIS A O   1 
ATOM   1932 C  CB  . HIS A 1 247 ? -40.957 51.263 1.461   1.00 64.69  ? 247 HIS A CB  1 
ATOM   1933 C  CG  . HIS A 1 247 ? -41.343 52.639 1.021   1.00 66.88  ? 247 HIS A CG  1 
ATOM   1934 N  ND1 . HIS A 1 247 ? -42.461 52.883 0.252   1.00 67.82  ? 247 HIS A ND1 1 
ATOM   1935 C  CD2 . HIS A 1 247 ? -40.758 53.842 1.228   1.00 66.89  ? 247 HIS A CD2 1 
ATOM   1936 C  CE1 . HIS A 1 247 ? -42.551 54.178 0.010   1.00 66.07  ? 247 HIS A CE1 1 
ATOM   1937 N  NE2 . HIS A 1 247 ? -41.531 54.783 0.591   1.00 64.88  ? 247 HIS A NE2 1 
ATOM   1938 N  N   . LYS A 1 248 ? -40.449 50.970 -1.903  1.00 74.65  ? 248 LYS A N   1 
ATOM   1939 C  CA  . LYS A 1 248 ? -39.590 51.277 -3.033  1.00 71.58  ? 248 LYS A CA  1 
ATOM   1940 C  C   . LYS A 1 248 ? -40.326 52.235 -3.954  1.00 77.19  ? 248 LYS A C   1 
ATOM   1941 O  O   . LYS A 1 248 ? -41.558 52.302 -3.956  1.00 76.75  ? 248 LYS A O   1 
ATOM   1942 C  CB  . LYS A 1 248 ? -39.188 50.005 -3.790  1.00 73.61  ? 248 LYS A CB  1 
ATOM   1943 C  CG  . LYS A 1 248 ? -40.334 49.374 -4.567  1.00 76.28  ? 248 LYS A CG  1 
ATOM   1944 C  CD  . LYS A 1 248 ? -39.992 47.982 -5.071  1.00 75.09  ? 248 LYS A CD  1 
ATOM   1945 C  CE  . LYS A 1 248 ? -39.874 46.993 -3.923  1.00 76.33  ? 248 LYS A CE  1 
ATOM   1946 N  NZ  . LYS A 1 248 ? -39.879 45.580 -4.395  1.00 80.56  ? 248 LYS A NZ  1 
ATOM   1947 N  N   . CYS A 1 249 ? -39.554 52.986 -4.732  1.00 79.55  ? 249 CYS A N   1 
ATOM   1948 C  CA  . CYS A 1 249 ? -40.090 53.857 -5.773  1.00 77.52  ? 249 CYS A CA  1 
ATOM   1949 C  C   . CYS A 1 249 ? -39.673 53.260 -7.113  1.00 77.08  ? 249 CYS A C   1 
ATOM   1950 O  O   . CYS A 1 249 ? -38.704 53.690 -7.740  1.00 77.41  ? 249 CYS A O   1 
ATOM   1951 C  CB  . CYS A 1 249 ? -39.599 55.298 -5.602  1.00 75.98  ? 249 CYS A CB  1 
ATOM   1952 S  SG  . CYS A 1 249 ? -40.488 56.234 -4.335  1.00 75.64  ? 249 CYS A SG  1 
ATOM   1953 N  N   . ALA A 1 250 ? -40.417 52.247 -7.546  1.00 78.07  ? 250 ALA A N   1 
ATOM   1954 C  CA  . ALA A 1 250 ? -40.114 51.558 -8.789  1.00 80.54  ? 250 ALA A CA  1 
ATOM   1955 C  C   . ALA A 1 250 ? -40.557 52.389 -9.986  1.00 80.72  ? 250 ALA A C   1 
ATOM   1956 O  O   . ALA A 1 250 ? -41.462 53.224 -9.892  1.00 80.52  ? 250 ALA A O   1 
ATOM   1957 C  CB  . ALA A 1 250 ? -40.790 50.188 -8.823  1.00 78.37  ? 250 ALA A CB  1 
ATOM   1958 N  N   . GLY A 1 251 ? -39.909 52.150 -11.121 1.00 84.15  ? 251 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 251 ? -40.198 52.905 -12.323 1.00 82.63  ? 251 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 251 ? -39.311 54.123 -12.459 1.00 83.65  ? 251 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 251 ? -39.093 54.851 -11.486 1.00 82.71  ? 251 GLY A O   1 
ATOM   1962 N  N   . ALA A 1 252 ? -38.797 54.357 -13.669 1.00 81.50  ? 252 ALA A N   1 
ATOM   1963 C  CA  . ALA A 1 252 ? -37.879 55.471 -13.885 1.00 81.45  ? 252 ALA A CA  1 
ATOM   1964 C  C   . ALA A 1 252 ? -38.550 56.815 -13.634 1.00 86.21  ? 252 ALA A C   1 
ATOM   1965 O  O   . ALA A 1 252 ? -37.873 57.789 -13.284 1.00 85.74  ? 252 ALA A O   1 
ATOM   1966 C  CB  . ALA A 1 252 ? -37.314 55.416 -15.303 1.00 84.40  ? 252 ALA A CB  1 
ATOM   1967 N  N   . LYS A 1 253 ? -39.871 56.891 -13.808 1.00 89.78  ? 253 LYS A N   1 
ATOM   1968 C  CA  A LYS A 1 253 ? -40.572 58.144 -13.550 0.96 88.02  ? 253 LYS A CA  1 
ATOM   1969 C  CA  B LYS A 1 253 ? -40.578 58.141 -13.550 0.04 88.00  ? 253 LYS A CA  1 
ATOM   1970 C  C   . LYS A 1 253 ? -40.572 58.482 -12.064 1.00 86.77  ? 253 LYS A C   1 
ATOM   1971 O  O   . LYS A 1 253 ? -40.447 59.654 -11.689 1.00 86.07  ? 253 LYS A O   1 
ATOM   1972 C  CB  A LYS A 1 253 ? -42.004 58.067 -14.078 0.96 92.93  ? 253 LYS A CB  1 
ATOM   1973 C  CB  B LYS A 1 253 ? -42.009 58.045 -14.084 0.04 92.31  ? 253 LYS A CB  1 
ATOM   1974 C  CG  A LYS A 1 253 ? -42.848 59.277 -13.711 0.96 95.55  ? 253 LYS A CG  1 
ATOM   1975 C  CG  B LYS A 1 253 ? -42.854 59.296 -13.892 0.04 95.30  ? 253 LYS A CG  1 
ATOM   1976 C  CD  A LYS A 1 253 ? -44.310 59.075 -14.054 0.96 99.93  ? 253 LYS A CD  1 
ATOM   1977 C  CD  B LYS A 1 253 ? -43.804 59.154 -12.712 0.04 95.33  ? 253 LYS A CD  1 
ATOM   1978 C  CE  A LYS A 1 253 ? -45.164 60.165 -13.431 0.96 100.59 ? 253 LYS A CE  1 
ATOM   1979 C  CE  B LYS A 1 253 ? -44.725 60.357 -12.595 0.04 98.39  ? 253 LYS A CE  1 
ATOM   1980 N  NZ  A LYS A 1 253 ? -45.054 60.164 -11.945 0.96 97.66  ? 253 LYS A NZ  1 
ATOM   1981 N  NZ  B LYS A 1 253 ? -45.603 60.500 -13.789 0.04 99.97  ? 253 LYS A NZ  1 
ATOM   1982 N  N   . ASN A 1 254 ? -40.701 57.473 -11.206 1.00 88.83  ? 254 ASN A N   1 
ATOM   1983 C  CA  . ASN A 1 254 ? -40.780 57.675 -9.767  1.00 88.27  ? 254 ASN A CA  1 
ATOM   1984 C  C   . ASN A 1 254 ? -39.418 57.668 -9.083  1.00 83.77  ? 254 ASN A C   1 
ATOM   1985 O  O   . ASN A 1 254 ? -39.361 57.613 -7.850  1.00 83.62  ? 254 ASN A O   1 
ATOM   1986 C  CB  . ASN A 1 254 ? -41.681 56.608 -9.141  1.00 86.54  ? 254 ASN A CB  1 
ATOM   1987 C  CG  . ASN A 1 254 ? -43.010 56.475 -9.859  1.00 89.09  ? 254 ASN A CG  1 
ATOM   1988 O  OD1 . ASN A 1 254 ? -43.910 57.296 -9.682  1.00 90.67  ? 254 ASN A OD1 1 
ATOM   1989 N  ND2 . ASN A 1 254 ? -43.139 55.436 -10.676 1.00 86.39  ? 254 ASN A ND2 1 
ATOM   1990 N  N   . TRP A 1 255 ? -38.326 57.722 -9.842  1.00 78.42  ? 255 TRP A N   1 
ATOM   1991 C  CA  . TRP A 1 255 ? -37.003 57.785 -9.236  1.00 76.40  ? 255 TRP A CA  1 
ATOM   1992 C  C   . TRP A 1 255 ? -36.823 59.110 -8.507  1.00 78.89  ? 255 TRP A C   1 
ATOM   1993 O  O   . TRP A 1 255 ? -37.114 60.178 -9.054  1.00 77.83  ? 255 TRP A O   1 
ATOM   1994 C  CB  . TRP A 1 255 ? -35.917 57.611 -10.296 1.00 77.96  ? 255 TRP A CB  1 
ATOM   1995 C  CG  . TRP A 1 255 ? -35.721 56.191 -10.721 1.00 78.39  ? 255 TRP A CG  1 
ATOM   1996 C  CD1 . TRP A 1 255 ? -36.355 55.092 -10.221 1.00 75.85  ? 255 TRP A CD1 1 
ATOM   1997 C  CD2 . TRP A 1 255 ? -34.827 55.714 -11.732 1.00 78.12  ? 255 TRP A CD2 1 
ATOM   1998 N  NE1 . TRP A 1 255 ? -35.914 53.959 -10.860 1.00 73.26  ? 255 TRP A NE1 1 
ATOM   1999 C  CE2 . TRP A 1 255 ? -34.975 54.314 -11.793 1.00 74.81  ? 255 TRP A CE2 1 
ATOM   2000 C  CE3 . TRP A 1 255 ? -33.917 56.334 -12.594 1.00 79.02  ? 255 TRP A CE3 1 
ATOM   2001 C  CZ2 . TRP A 1 255 ? -34.246 53.524 -12.679 1.00 75.11  ? 255 TRP A CZ2 1 
ATOM   2002 C  CZ3 . TRP A 1 255 ? -33.195 55.548 -13.474 1.00 80.67  ? 255 TRP A CZ3 1 
ATOM   2003 C  CH2 . TRP A 1 255 ? -33.364 54.158 -13.510 1.00 78.18  ? 255 TRP A CH2 1 
ATOM   2004 N  N   . GLY A 1 256 ? -36.342 59.039 -7.267  1.00 75.66  ? 256 GLY A N   1 
ATOM   2005 C  CA  . GLY A 1 256 ? -36.187 60.210 -6.438  1.00 75.66  ? 256 GLY A CA  1 
ATOM   2006 C  C   . GLY A 1 256 ? -37.410 60.587 -5.631  1.00 80.07  ? 256 GLY A C   1 
ATOM   2007 O  O   . GLY A 1 256 ? -37.307 61.447 -4.747  1.00 81.46  ? 256 GLY A O   1 
ATOM   2008 N  N   . ARG A 1 257 ? -38.561 59.967 -5.894  1.00 79.92  ? 257 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 257 ? -39.788 60.310 -5.184  1.00 78.75  ? 257 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 257 ? -39.822 59.787 -3.755  1.00 77.42  ? 257 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 257 ? -40.826 60.004 -3.067  1.00 79.24  ? 257 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 257 ? -41.003 59.796 -5.956  1.00 80.10  ? 257 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 257 ? -41.369 60.651 -7.157  1.00 84.27  ? 257 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 257 ? -42.831 61.054 -7.108  1.00 86.36  ? 257 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 257 ? -43.716 59.933 -7.398  1.00 84.71  ? 257 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 257 ? -44.999 59.888 -7.068  1.00 85.76  ? 257 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 257 ? -45.576 60.873 -6.398  1.00 85.19  ? 257 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 257 ? -45.721 58.826 -7.413  1.00 87.14  ? 257 ARG A NH2 1 
ATOM   2019 N  N   . THR A 1 258 ? -38.768 59.109 -3.292  1.00 78.86  ? 258 THR A N   1 
ATOM   2020 C  CA  . THR A 1 258 ? -38.682 58.767 -1.877  1.00 75.74  ? 258 THR A CA  1 
ATOM   2021 C  C   . THR A 1 258 ? -38.626 60.006 -0.995  1.00 77.22  ? 258 THR A C   1 
ATOM   2022 O  O   . THR A 1 258 ? -38.962 59.925 0.191   1.00 77.17  ? 258 THR A O   1 
ATOM   2023 C  CB  . THR A 1 258 ? -37.460 57.888 -1.608  1.00 72.35  ? 258 THR A CB  1 
ATOM   2024 O  OG1 . THR A 1 258 ? -36.326 58.411 -2.312  1.00 78.27  ? 258 THR A OG1 1 
ATOM   2025 C  CG2 . THR A 1 258 ? -37.718 56.456 -2.051  1.00 70.59  ? 258 THR A CG2 1 
ATOM   2026 N  N   . LYS A 1 259 ? -38.206 61.150 -1.544  1.00 76.54  ? 259 LYS A N   1 
ATOM   2027 C  CA  . LYS A 1 259 ? -38.263 62.394 -0.785  1.00 79.10  ? 259 LYS A CA  1 
ATOM   2028 C  C   . LYS A 1 259 ? -39.699 62.813 -0.506  1.00 81.23  ? 259 LYS A C   1 
ATOM   2029 O  O   . LYS A 1 259 ? -39.959 63.533 0.464   1.00 84.46  ? 259 LYS A O   1 
ATOM   2030 C  CB  . LYS A 1 259 ? -37.520 63.501 -1.532  1.00 80.26  ? 259 LYS A CB  1 
ATOM   2031 C  CG  . LYS A 1 259 ? -36.012 63.497 -1.325  1.00 80.68  ? 259 LYS A CG  1 
ATOM   2032 C  CD  . LYS A 1 259 ? -35.304 64.355 -2.363  1.00 80.99  ? 259 LYS A CD  1 
ATOM   2033 C  CE  . LYS A 1 259 ? -35.314 63.678 -3.724  1.00 90.59  ? 259 LYS A CE  1 
ATOM   2034 N  NZ  . LYS A 1 259 ? -34.516 64.412 -4.746  1.00 84.30  ? 259 LYS A NZ  1 
ATOM   2035 N  N   . GLU A 1 260 ? -40.642 62.371 -1.335  1.00 82.46  ? 260 GLU A N   1 
ATOM   2036 C  CA  . GLU A 1 260 ? -42.052 62.673 -1.128  1.00 83.12  ? 260 GLU A CA  1 
ATOM   2037 C  C   . GLU A 1 260 ? -42.725 61.672 -0.197  1.00 85.65  ? 260 GLU A C   1 
ATOM   2038 O  O   . GLU A 1 260 ? -43.511 62.067 0.672   1.00 92.02  ? 260 GLU A O   1 
ATOM   2039 C  CB  . GLU A 1 260 ? -42.793 62.705 -2.469  1.00 82.56  ? 260 GLU A CB  1 
ATOM   2040 C  CG  . GLU A 1 260 ? -42.215 63.681 -3.482  1.00 87.43  ? 260 GLU A CG  1 
ATOM   2041 C  CD  . GLU A 1 260 ? -43.032 63.739 -4.757  1.00 97.58  ? 260 GLU A CD  1 
ATOM   2042 O  OE1 . GLU A 1 260 ? -44.172 63.226 -4.756  1.00 94.69  ? 260 GLU A OE1 1 
ATOM   2043 O  OE2 . GLU A 1 260 ? -42.537 64.294 -5.761  1.00 98.62  ? 260 GLU A OE2 1 
ATOM   2044 N  N   . THR A 1 261 ? -42.432 60.380 -0.362  1.00 77.45  ? 261 THR A N   1 
ATOM   2045 C  CA  . THR A 1 261 ? -43.062 59.363 0.474   1.00 73.58  ? 261 THR A CA  1 
ATOM   2046 C  C   . THR A 1 261 ? -42.601 59.479 1.922   1.00 73.29  ? 261 THR A C   1 
ATOM   2047 O  O   . THR A 1 261 ? -43.425 59.529 2.843   1.00 76.78  ? 261 THR A O   1 
ATOM   2048 C  CB  . THR A 1 261 ? -42.761 57.967 -0.075  1.00 73.19  ? 261 THR A CB  1 
ATOM   2049 O  OG1 . THR A 1 261 ? -41.347 57.737 -0.051  1.00 71.39  ? 261 THR A OG1 1 
ATOM   2050 C  CG2 . THR A 1 261 ? -43.267 57.838 -1.504  1.00 73.76  ? 261 THR A CG2 1 
ATOM   2051 N  N   . LEU A 1 262 ? -41.284 59.528 2.142   1.00 73.23  ? 262 LEU A N   1 
ATOM   2052 C  CA  . LEU A 1 262 ? -40.762 59.629 3.501   1.00 73.07  ? 262 LEU A CA  1 
ATOM   2053 C  C   . LEU A 1 262 ? -41.219 60.910 4.187   1.00 76.45  ? 262 LEU A C   1 
ATOM   2054 O  O   . LEU A 1 262 ? -41.357 60.941 5.415   1.00 74.22  ? 262 LEU A O   1 
ATOM   2055 C  CB  . LEU A 1 262 ? -39.235 59.549 3.487   1.00 69.04  ? 262 LEU A CB  1 
ATOM   2056 C  CG  . LEU A 1 262 ? -38.640 58.248 2.943   1.00 67.34  ? 262 LEU A CG  1 
ATOM   2057 C  CD1 . LEU A 1 262 ? -37.126 58.251 3.084   1.00 65.41  ? 262 LEU A CD1 1 
ATOM   2058 C  CD2 . LEU A 1 262 ? -39.248 57.044 3.643   1.00 67.84  ? 262 LEU A CD2 1 
ATOM   2059 N  N   . ALA A 1 263 ? -41.453 61.975 3.417   1.00 74.67  ? 263 ALA A N   1 
ATOM   2060 C  CA  . ALA A 1 263 ? -42.047 63.177 3.991   1.00 76.02  ? 263 ALA A CA  1 
ATOM   2061 C  C   . ALA A 1 263 ? -43.492 62.927 4.402   1.00 76.13  ? 263 ALA A C   1 
ATOM   2062 O  O   . ALA A 1 263 ? -43.948 63.435 5.433   1.00 74.54  ? 263 ALA A O   1 
ATOM   2063 C  CB  . ALA A 1 263 ? -41.961 64.334 2.996   1.00 74.75  ? 263 ALA A CB  1 
ATOM   2064 N  N   . PHE A 1 264 ? -44.227 62.148 3.605   1.00 75.30  ? 264 PHE A N   1 
ATOM   2065 C  CA  . PHE A 1 264 ? -45.582 61.766 3.985   1.00 74.59  ? 264 PHE A CA  1 
ATOM   2066 C  C   . PHE A 1 264 ? -45.575 60.848 5.200   1.00 75.32  ? 264 PHE A C   1 
ATOM   2067 O  O   . PHE A 1 264 ? -46.522 60.864 5.994   1.00 76.50  ? 264 PHE A O   1 
ATOM   2068 C  CB  . PHE A 1 264 ? -46.284 61.100 2.800   1.00 75.19  ? 264 PHE A CB  1 
ATOM   2069 C  CG  . PHE A 1 264 ? -47.744 60.825 3.029   1.00 74.76  ? 264 PHE A CG  1 
ATOM   2070 C  CD1 . PHE A 1 264 ? -48.577 61.805 3.544   1.00 75.46  ? 264 PHE A CD1 1 
ATOM   2071 C  CD2 . PHE A 1 264 ? -48.288 59.594 2.703   1.00 72.80  ? 264 PHE A CD2 1 
ATOM   2072 C  CE1 . PHE A 1 264 ? -49.922 61.555 3.747   1.00 74.74  ? 264 PHE A CE1 1 
ATOM   2073 C  CE2 . PHE A 1 264 ? -49.632 59.339 2.901   1.00 74.71  ? 264 PHE A CE2 1 
ATOM   2074 C  CZ  . PHE A 1 264 ? -50.449 60.320 3.425   1.00 77.18  ? 264 PHE A CZ  1 
ATOM   2075 N  N   . PHE A 1 265 ? -44.518 60.048 5.363   1.00 74.88  ? 265 PHE A N   1 
ATOM   2076 C  CA  . PHE A 1 265 ? -44.357 59.267 6.585   1.00 74.52  ? 265 PHE A CA  1 
ATOM   2077 C  C   . PHE A 1 265 ? -44.221 60.178 7.799   1.00 77.13  ? 265 PHE A C   1 
ATOM   2078 O  O   . PHE A 1 265 ? -44.935 60.014 8.795   1.00 81.25  ? 265 PHE A O   1 
ATOM   2079 C  CB  . PHE A 1 265 ? -43.136 58.351 6.467   1.00 72.93  ? 265 PHE A CB  1 
ATOM   2080 C  CG  . PHE A 1 265 ? -43.407 57.049 5.764   1.00 69.86  ? 265 PHE A CG  1 
ATOM   2081 C  CD1 . PHE A 1 265 ? -43.279 56.945 4.389   1.00 67.61  ? 265 PHE A CD1 1 
ATOM   2082 C  CD2 . PHE A 1 265 ? -43.764 55.921 6.482   1.00 67.51  ? 265 PHE A CD2 1 
ATOM   2083 C  CE1 . PHE A 1 265 ? -43.518 55.748 3.743   1.00 66.55  ? 265 PHE A CE1 1 
ATOM   2084 C  CE2 . PHE A 1 265 ? -44.003 54.719 5.842   1.00 64.65  ? 265 PHE A CE2 1 
ATOM   2085 C  CZ  . PHE A 1 265 ? -43.880 54.633 4.471   1.00 67.36  ? 265 PHE A CZ  1 
ATOM   2086 N  N   . ASP A 1 266 ? -43.312 61.156 7.725   1.00 73.94  ? 266 ASP A N   1 
ATOM   2087 C  CA  . ASP A 1 266 ? -43.041 62.023 8.870   1.00 74.81  ? 266 ASP A CA  1 
ATOM   2088 C  C   . ASP A 1 266 ? -44.295 62.755 9.331   1.00 80.07  ? 266 ASP A C   1 
ATOM   2089 O  O   . ASP A 1 266 ? -44.554 62.859 10.536  1.00 81.92  ? 266 ASP A O   1 
ATOM   2090 C  CB  . ASP A 1 266 ? -41.944 63.029 8.519   1.00 73.89  ? 266 ASP A CB  1 
ATOM   2091 C  CG  . ASP A 1 266 ? -40.614 62.366 8.228   1.00 72.82  ? 266 ASP A CG  1 
ATOM   2092 O  OD1 . ASP A 1 266 ? -40.340 61.297 8.812   1.00 74.60  ? 266 ASP A OD1 1 
ATOM   2093 O  OD2 . ASP A 1 266 ? -39.840 62.916 7.416   1.00 71.66  ? 266 ASP A OD2 1 
ATOM   2094 N  N   . GLU A 1 267 ? -45.086 63.270 8.387   1.00 78.63  ? 267 GLU A N   1 
ATOM   2095 C  CA  A GLU A 1 267 ? -46.298 63.998 8.747   0.57 81.28  ? 267 GLU A CA  1 
ATOM   2096 C  CA  B GLU A 1 267 ? -46.292 63.999 8.763   0.43 81.28  ? 267 GLU A CA  1 
ATOM   2097 C  C   . GLU A 1 267 ? -47.342 63.079 9.369   1.00 83.76  ? 267 GLU A C   1 
ATOM   2098 O  O   . GLU A 1 267 ? -48.133 63.519 10.213  1.00 87.13  ? 267 GLU A O   1 
ATOM   2099 C  CB  A GLU A 1 267 ? -46.872 64.696 7.512   0.57 81.88  ? 267 GLU A CB  1 
ATOM   2100 C  CB  B GLU A 1 267 ? -46.862 64.732 7.549   0.43 81.87  ? 267 GLU A CB  1 
ATOM   2101 C  CG  A GLU A 1 267 ? -48.059 65.607 7.788   0.57 84.52  ? 267 GLU A CG  1 
ATOM   2102 C  CG  B GLU A 1 267 ? -45.889 65.711 6.917   0.43 83.42  ? 267 GLU A CG  1 
ATOM   2103 C  CD  A GLU A 1 267 ? -48.758 66.053 6.516   0.57 85.32  ? 267 GLU A CD  1 
ATOM   2104 C  CD  B GLU A 1 267 ? -45.391 66.754 7.899   0.43 84.78  ? 267 GLU A CD  1 
ATOM   2105 O  OE1 A GLU A 1 267 ? -48.090 66.136 5.464   0.57 84.60  ? 267 GLU A OE1 1 
ATOM   2106 O  OE1 B GLU A 1 267 ? -46.204 67.249 8.709   0.43 84.89  ? 267 GLU A OE1 1 
ATOM   2107 O  OE2 A GLU A 1 267 ? -49.979 66.312 6.566   0.57 86.69  ? 267 GLU A OE2 1 
ATOM   2108 O  OE2 B GLU A 1 267 ? -44.185 67.076 7.866   0.43 83.99  ? 267 GLU A OE2 1 
ATOM   2109 N  N   . MET A 1 268 ? -47.362 61.808 8.972   1.00 83.21  ? 268 MET A N   1 
ATOM   2110 C  CA  . MET A 1 268 ? -48.367 60.885 9.477   1.00 79.88  ? 268 MET A CA  1 
ATOM   2111 C  C   . MET A 1 268 ? -47.884 60.055 10.660  1.00 80.06  ? 268 MET A C   1 
ATOM   2112 O  O   . MET A 1 268 ? -48.715 59.465 11.360  1.00 80.19  ? 268 MET A O   1 
ATOM   2113 C  CB  . MET A 1 268 ? -48.844 59.966 8.349   1.00 77.79  ? 268 MET A CB  1 
ATOM   2114 C  CG  . MET A 1 268 ? -49.498 60.701 7.177   1.00 80.04  ? 268 MET A CG  1 
ATOM   2115 S  SD  . MET A 1 268 ? -51.123 61.417 7.526   1.00 91.15  ? 268 MET A SD  1 
ATOM   2116 C  CE  . MET A 1 268 ? -50.703 63.103 7.976   1.00 85.60  ? 268 MET A CE  1 
ATOM   2117 N  N   . ARG A 1 269 ? -46.575 59.998 10.911  1.00 78.45  ? 269 ARG A N   1 
ATOM   2118 C  CA  . ARG A 1 269 ? -46.084 59.360 12.126  1.00 79.60  ? 269 ARG A CA  1 
ATOM   2119 C  C   . ARG A 1 269 ? -46.282 60.227 13.362  1.00 80.30  ? 269 ARG A C   1 
ATOM   2120 O  O   . ARG A 1 269 ? -45.987 59.773 14.473  1.00 82.05  ? 269 ARG A O   1 
ATOM   2121 C  CB  . ARG A 1 269 ? -44.605 58.986 11.980  1.00 77.74  ? 269 ARG A CB  1 
ATOM   2122 C  CG  . ARG A 1 269 ? -44.357 57.876 10.970  1.00 73.96  ? 269 ARG A CG  1 
ATOM   2123 C  CD  . ARG A 1 269 ? -43.250 56.929 11.404  1.00 78.32  ? 269 ARG A CD  1 
ATOM   2124 N  NE  . ARG A 1 269 ? -41.965 57.599 11.567  1.00 82.41  ? 269 ARG A NE  1 
ATOM   2125 C  CZ  . ARG A 1 269 ? -41.393 57.845 12.737  1.00 85.17  ? 269 ARG A CZ  1 
ATOM   2126 N  NH1 . ARG A 1 269 ? -41.964 57.487 13.875  1.00 88.07  ? 269 ARG A NH1 1 
ATOM   2127 N  NH2 . ARG A 1 269 ? -40.214 58.461 12.766  1.00 80.81  ? 269 ARG A NH2 1 
ATOM   2128 N  N   . GLN A 1 270 ? -46.771 61.455 13.199  1.00 83.08  ? 270 GLN A N   1 
ATOM   2129 C  CA  . GLN A 1 270 ? -47.170 62.291 14.322  1.00 87.55  ? 270 GLN A CA  1 
ATOM   2130 C  C   . GLN A 1 270 ? -48.622 62.072 14.724  1.00 87.14  ? 270 GLN A C   1 
ATOM   2131 O  O   . GLN A 1 270 ? -49.096 62.719 15.664  1.00 85.79  ? 270 GLN A O   1 
ATOM   2132 C  CB  . GLN A 1 270 ? -46.937 63.770 13.996  1.00 87.82  ? 270 GLN A CB  1 
ATOM   2133 C  CG  . GLN A 1 270 ? -45.480 64.120 13.733  1.00 91.42  ? 270 GLN A CG  1 
ATOM   2134 C  CD  . GLN A 1 270 ? -45.134 65.537 14.150  1.00 100.17 ? 270 GLN A CD  1 
ATOM   2135 O  OE1 . GLN A 1 270 ? -45.988 66.281 14.633  1.00 110.70 ? 270 GLN A OE1 1 
ATOM   2136 N  NE2 . GLN A 1 270 ? -43.874 65.915 13.970  1.00 101.01 ? 270 GLN A NE2 1 
ATOM   2137 N  N   . GLN A 1 271 ? -49.335 61.187 14.032  1.00 82.74  ? 271 GLN A N   1 
ATOM   2138 C  CA  A GLN A 1 271 ? -50.710 60.840 14.366  0.39 82.33  ? 271 GLN A CA  1 
ATOM   2139 C  CA  B GLN A 1 271 ? -50.706 60.843 14.380  0.61 82.32  ? 271 GLN A CA  1 
ATOM   2140 C  C   . GLN A 1 271 ? -50.914 59.358 14.631  1.00 80.02  ? 271 GLN A C   1 
ATOM   2141 O  O   . GLN A 1 271 ? -51.782 59.003 15.431  1.00 81.15  ? 271 GLN A O   1 
ATOM   2142 C  CB  A GLN A 1 271 ? -51.664 61.269 13.239  0.39 84.63  ? 271 GLN A CB  1 
ATOM   2143 C  CB  B GLN A 1 271 ? -51.672 61.306 13.276  0.61 84.62  ? 271 GLN A CB  1 
ATOM   2144 C  CG  A GLN A 1 271 ? -51.631 62.751 12.910  0.39 87.00  ? 271 GLN A CG  1 
ATOM   2145 C  CG  B GLN A 1 271 ? -53.143 61.176 13.640  0.61 85.52  ? 271 GLN A CG  1 
ATOM   2146 C  CD  A GLN A 1 271 ? -52.615 63.122 11.817  0.39 89.83  ? 271 GLN A CD  1 
ATOM   2147 C  CD  B GLN A 1 271 ? -54.062 61.745 12.578  0.61 88.43  ? 271 GLN A CD  1 
ATOM   2148 O  OE1 A GLN A 1 271 ? -53.424 62.298 11.390  0.39 90.22  ? 271 GLN A OE1 1 
ATOM   2149 O  OE1 B GLN A 1 271 ? -53.606 62.308 11.582  0.61 89.90  ? 271 GLN A OE1 1 
ATOM   2150 N  NE2 A GLN A 1 271 ? -52.549 64.366 11.358  0.39 90.77  ? 271 GLN A NE2 1 
ATOM   2151 N  NE2 B GLN A 1 271 ? -55.365 61.603 12.786  0.61 86.75  ? 271 GLN A NE2 1 
ATOM   2152 N  N   . GLN A 1 272 ? -50.141 58.487 13.985  1.00 77.74  ? 272 GLN A N   1 
ATOM   2153 C  CA  . GLN A 1 272 ? -50.276 57.047 14.146  1.00 72.48  ? 272 GLN A CA  1 
ATOM   2154 C  C   . GLN A 1 272 ? -48.896 56.405 14.134  1.00 68.21  ? 272 GLN A C   1 
ATOM   2155 O  O   . GLN A 1 272 ? -47.883 57.053 13.855  1.00 74.59  ? 272 GLN A O   1 
ATOM   2156 C  CB  . GLN A 1 272 ? -51.162 56.448 13.046  1.00 72.64  ? 272 GLN A CB  1 
ATOM   2157 C  CG  . GLN A 1 272 ? -50.787 56.900 11.643  1.00 71.62  ? 272 GLN A CG  1 
ATOM   2158 C  CD  . GLN A 1 272 ? -51.762 56.416 10.587  1.00 69.54  ? 272 GLN A CD  1 
ATOM   2159 O  OE1 . GLN A 1 272 ? -52.441 57.213 9.940   1.00 71.20  ? 272 GLN A OE1 1 
ATOM   2160 N  NE2 . GLN A 1 272 ? -51.830 55.103 10.401  1.00 67.81  ? 272 GLN A NE2 1 
ATOM   2161 N  N   . ASP A 1 273 ? -48.866 55.110 14.442  1.00 65.78  ? 273 ASP A N   1 
ATOM   2162 C  CA  A ASP A 1 273 ? -47.630 54.338 14.468  0.56 68.49  ? 273 ASP A CA  1 
ATOM   2163 C  CA  B ASP A 1 273 ? -47.628 54.342 14.465  0.44 68.00  ? 273 ASP A CA  1 
ATOM   2164 C  C   . ASP A 1 273 ? -47.398 53.721 13.093  1.00 67.58  ? 273 ASP A C   1 
ATOM   2165 O  O   . ASP A 1 273 ? -48.195 52.894 12.637  1.00 64.67  ? 273 ASP A O   1 
ATOM   2166 C  CB  A ASP A 1 273 ? -47.700 53.255 15.544  0.56 67.21  ? 273 ASP A CB  1 
ATOM   2167 C  CB  B ASP A 1 273 ? -47.682 53.261 15.544  0.44 67.35  ? 273 ASP A CB  1 
ATOM   2168 C  CG  A ASP A 1 273 ? -46.373 52.549 15.755  0.56 66.21  ? 273 ASP A CG  1 
ATOM   2169 C  CG  B ASP A 1 273 ? -47.744 53.839 16.943  0.44 65.68  ? 273 ASP A CG  1 
ATOM   2170 O  OD1 A ASP A 1 273 ? -45.358 52.986 15.174  0.56 65.63  ? 273 ASP A OD1 1 
ATOM   2171 O  OD1 B ASP A 1 273 ? -47.633 55.075 17.082  0.44 66.29  ? 273 ASP A OD1 1 
ATOM   2172 O  OD2 A ASP A 1 273 ? -46.347 51.551 16.507  0.56 67.13  ? 273 ASP A OD2 1 
ATOM   2173 O  OD2 B ASP A 1 273 ? -47.906 53.057 17.903  0.44 61.72  ? 273 ASP A OD2 1 
ATOM   2174 N  N   . ILE A 1 274 ? -46.309 54.120 12.438  1.00 64.61  ? 274 ILE A N   1 
ATOM   2175 C  CA  . ILE A 1 274 ? -45.991 53.675 11.088  1.00 62.93  ? 274 ILE A CA  1 
ATOM   2176 C  C   . ILE A 1 274 ? -44.542 53.204 11.043  1.00 60.83  ? 274 ILE A C   1 
ATOM   2177 O  O   . ILE A 1 274 ? -43.675 53.766 11.720  1.00 63.19  ? 274 ILE A O   1 
ATOM   2178 C  CB  . ILE A 1 274 ? -46.227 54.798 10.055  1.00 64.66  ? 274 ILE A CB  1 
ATOM   2179 C  CG1 . ILE A 1 274 ? -47.622 55.403 10.227  1.00 65.54  ? 274 ILE A CG1 1 
ATOM   2180 C  CG2 . ILE A 1 274 ? -46.057 54.273 8.646   1.00 63.91  ? 274 ILE A CG2 1 
ATOM   2181 C  CD1 . ILE A 1 274 ? -47.891 56.589 9.331   1.00 69.77  ? 274 ILE A CD1 1 
ATOM   2182 N  N   . ALA A 1 275 ? -44.286 52.166 10.249  1.00 67.88  ? 275 ALA A N   1 
ATOM   2183 C  CA  . ALA A 1 275 ? -42.934 51.685 9.998   1.00 65.13  ? 275 ALA A CA  1 
ATOM   2184 C  C   . ALA A 1 275 ? -42.880 51.120 8.584   1.00 63.51  ? 275 ALA A C   1 
ATOM   2185 O  O   . ALA A 1 275 ? -43.852 51.198 7.826   1.00 61.07  ? 275 ALA A O   1 
ATOM   2186 C  CB  . ALA A 1 275 ? -42.508 50.642 11.037  1.00 64.68  ? 275 ALA A CB  1 
ATOM   2187 N  N   . CYS A 1 276 ? -41.731 50.548 8.230   1.00 60.63  ? 276 CYS A N   1 
ATOM   2188 C  CA  . CYS A 1 276 ? -41.549 49.959 6.909   1.00 60.50  ? 276 CYS A CA  1 
ATOM   2189 C  C   . CYS A 1 276 ? -40.302 49.087 6.924   1.00 58.12  ? 276 CYS A C   1 
ATOM   2190 O  O   . CYS A 1 276 ? -39.494 49.136 7.853   1.00 56.05  ? 276 CYS A O   1 
ATOM   2191 C  CB  . CYS A 1 276 ? -41.446 51.035 5.821   1.00 60.08  ? 276 CYS A CB  1 
ATOM   2192 S  SG  . CYS A 1 276 ? -39.969 52.073 5.920   1.00 60.07  ? 276 CYS A SG  1 
ATOM   2193 N  N   . ASP A 1 277 ? -40.158 48.281 5.873   1.00 59.04  ? 277 ASP A N   1 
ATOM   2194 C  CA  . ASP A 1 277 ? -38.957 47.491 5.650   1.00 58.68  ? 277 ASP A CA  1 
ATOM   2195 C  C   . ASP A 1 277 ? -38.568 47.591 4.182   1.00 61.01  ? 277 ASP A C   1 
ATOM   2196 O  O   . ASP A 1 277 ? -39.338 48.068 3.344   1.00 59.86  ? 277 ASP A O   1 
ATOM   2197 C  CB  . ASP A 1 277 ? -39.148 46.023 6.056   1.00 55.63  ? 277 ASP A CB  1 
ATOM   2198 C  CG  . ASP A 1 277 ? -40.188 45.313 5.215   1.00 60.09  ? 277 ASP A CG  1 
ATOM   2199 O  OD1 . ASP A 1 277 ? -41.374 45.310 5.607   1.00 62.36  ? 277 ASP A OD1 1 
ATOM   2200 O  OD2 . ASP A 1 277 ? -39.822 44.769 4.151   1.00 61.72  ? 277 ASP A OD2 1 
ATOM   2201 N  N   . CYS A 1 278 ? -37.356 47.133 3.877   1.00 60.20  ? 278 CYS A N   1 
ATOM   2202 C  CA  . CYS A 1 278 ? -36.840 47.164 2.515   1.00 60.50  ? 278 CYS A CA  1 
ATOM   2203 C  C   . CYS A 1 278 ? -35.586 46.307 2.453   1.00 60.56  ? 278 CYS A C   1 
ATOM   2204 O  O   . CYS A 1 278 ? -34.910 46.090 3.463   1.00 59.70  ? 278 CYS A O   1 
ATOM   2205 C  CB  . CYS A 1 278 ? -36.532 48.593 2.055   1.00 69.57  ? 278 CYS A CB  1 
ATOM   2206 S  SG  . CYS A 1 278 ? -35.112 49.346 2.884   1.00 62.79  ? 278 CYS A SG  1 
ATOM   2207 N  N   . TYR A 1 279 ? -35.282 45.816 1.239   1.00 61.42  ? 279 TYR A N   1 
ATOM   2208 C  CA  . TYR A 1 279 ? -34.032 45.099 1.044   1.00 61.15  ? 279 TYR A CA  1 
ATOM   2209 C  C   . TYR A 1 279 ? -32.977 46.028 0.452   1.00 62.56  ? 279 TYR A C   1 
ATOM   2210 O  O   . TYR A 1 279 ? -33.296 46.909 -0.353  1.00 63.74  ? 279 TYR A O   1 
ATOM   2211 C  CB  . TYR A 1 279 ? -34.228 43.885 0.128   1.00 64.67  ? 279 TYR A CB  1 
ATOM   2212 C  CG  . TYR A 1 279 ? -34.954 44.175 -1.165  1.00 64.64  ? 279 TYR A CG  1 
ATOM   2213 C  CD1 . TYR A 1 279 ? -36.340 44.107 -1.235  1.00 67.66  ? 279 TYR A CD1 1 
ATOM   2214 C  CD2 . TYR A 1 279 ? -34.255 44.499 -2.321  1.00 64.54  ? 279 TYR A CD2 1 
ATOM   2215 C  CE1 . TYR A 1 279 ? -37.008 44.364 -2.414  1.00 67.56  ? 279 TYR A CE1 1 
ATOM   2216 C  CE2 . TYR A 1 279 ? -34.917 44.758 -3.506  1.00 66.15  ? 279 TYR A CE2 1 
ATOM   2217 C  CZ  . TYR A 1 279 ? -36.293 44.690 -3.546  1.00 72.06  ? 279 TYR A CZ  1 
ATOM   2218 O  OH  . TYR A 1 279 ? -36.959 44.944 -4.723  1.00 77.98  ? 279 TYR A OH  1 
ATOM   2219 N  N   . PRO A 1 280 ? -31.705 45.858 0.840   1.00 59.88  ? 280 PRO A N   1 
ATOM   2220 C  CA  . PRO A 1 280 ? -30.640 46.793 0.451   1.00 61.33  ? 280 PRO A CA  1 
ATOM   2221 C  C   . PRO A 1 280 ? -30.129 46.604 -0.977  1.00 61.81  ? 280 PRO A C   1 
ATOM   2222 O  O   . PRO A 1 280 ? -28.930 46.450 -1.213  1.00 59.85  ? 280 PRO A O   1 
ATOM   2223 C  CB  . PRO A 1 280 ? -29.545 46.498 1.480   1.00 63.01  ? 280 PRO A CB  1 
ATOM   2224 C  CG  . PRO A 1 280 ? -29.717 45.050 1.769   1.00 61.06  ? 280 PRO A CG  1 
ATOM   2225 C  CD  . PRO A 1 280 ? -31.201 44.790 1.723   1.00 57.71  ? 280 PRO A CD  1 
ATOM   2226 N  N   . TYR A 1 281 ? -31.049 46.621 -1.939  1.00 61.62  ? 281 TYR A N   1 
ATOM   2227 C  CA  . TYR A 1 281 ? -30.699 46.485 -3.344  1.00 62.77  ? 281 TYR A CA  1 
ATOM   2228 C  C   . TYR A 1 281 ? -31.533 47.461 -4.161  1.00 66.65  ? 281 TYR A C   1 
ATOM   2229 O  O   . TYR A 1 281 ? -32.641 47.835 -3.769  1.00 66.07  ? 281 TYR A O   1 
ATOM   2230 C  CB  . TYR A 1 281 ? -30.917 45.052 -3.852  1.00 62.77  ? 281 TYR A CB  1 
ATOM   2231 C  CG  . TYR A 1 281 ? -30.048 44.016 -3.173  1.00 62.98  ? 281 TYR A CG  1 
ATOM   2232 C  CD1 . TYR A 1 281 ? -30.408 43.475 -1.945  1.00 64.90  ? 281 TYR A CD1 1 
ATOM   2233 C  CD2 . TYR A 1 281 ? -28.872 43.570 -3.764  1.00 64.30  ? 281 TYR A CD2 1 
ATOM   2234 C  CE1 . TYR A 1 281 ? -29.617 42.532 -1.320  1.00 61.42  ? 281 TYR A CE1 1 
ATOM   2235 C  CE2 . TYR A 1 281 ? -28.077 42.621 -3.147  1.00 66.23  ? 281 TYR A CE2 1 
ATOM   2236 C  CZ  . TYR A 1 281 ? -28.456 42.105 -1.926  1.00 65.23  ? 281 TYR A CZ  1 
ATOM   2237 O  OH  . TYR A 1 281 ? -27.670 41.162 -1.306  1.00 66.33  ? 281 TYR A OH  1 
ATOM   2238 N  N   . SER A 1 282 ? -30.985 47.873 -5.304  1.00 63.89  ? 282 SER A N   1 
ATOM   2239 C  CA  . SER A 1 282 ? -31.655 48.796 -6.212  1.00 66.07  ? 282 SER A CA  1 
ATOM   2240 C  C   . SER A 1 282 ? -32.097 48.104 -7.499  1.00 68.16  ? 282 SER A C   1 
ATOM   2241 O  O   . SER A 1 282 ? -32.221 48.745 -8.545  1.00 70.58  ? 282 SER A O   1 
ATOM   2242 C  CB  . SER A 1 282 ? -30.750 49.985 -6.531  1.00 65.61  ? 282 SER A CB  1 
ATOM   2243 O  OG  . SER A 1 282 ? -29.558 49.562 -7.169  1.00 69.17  ? 282 SER A OG  1 
ATOM   2244 N  N   . ALA A 1 283 ? -32.337 46.797 -7.436  1.00 70.45  ? 283 ALA A N   1 
ATOM   2245 C  CA  . ALA A 1 283 ? -32.764 46.028 -8.595  1.00 74.30  ? 283 ALA A CA  1 
ATOM   2246 C  C   . ALA A 1 283 ? -33.747 44.954 -8.158  1.00 79.48  ? 283 ALA A C   1 
ATOM   2247 O  O   . ALA A 1 283 ? -33.596 44.362 -7.086  1.00 74.63  ? 283 ALA A O   1 
ATOM   2248 C  CB  . ALA A 1 283 ? -31.572 45.386 -9.314  1.00 71.95  ? 283 ALA A CB  1 
ATOM   2249 N  N   . SER A 1 284 ? -34.752 44.708 -8.993  1.00 89.44  ? 284 SER A N   1 
ATOM   2250 C  CA  . SER A 1 284 ? -35.756 43.689 -8.730  1.00 82.50  ? 284 SER A CA  1 
ATOM   2251 C  C   . SER A 1 284 ? -35.407 42.394 -9.457  1.00 87.58  ? 284 SER A C   1 
ATOM   2252 O  O   . SER A 1 284 ? -34.499 42.338 -10.290 1.00 87.93  ? 284 SER A O   1 
ATOM   2253 C  CB  . SER A 1 284 ? -37.145 44.179 -9.150  1.00 83.46  ? 284 SER A CB  1 
ATOM   2254 O  OG  . SER A 1 284 ? -37.554 45.290 -8.372  1.00 88.68  ? 284 SER A OG  1 
ATOM   2255 N  N   . SER A 1 285 ? -36.149 41.340 -9.124  1.00 91.67  ? 285 SER A N   1 
ATOM   2256 C  CA  . SER A 1 285 ? -35.978 40.037 -9.762  1.00 93.35  ? 285 SER A CA  1 
ATOM   2257 C  C   . SER A 1 285 ? -37.352 39.393 -9.869  1.00 92.53  ? 285 SER A C   1 
ATOM   2258 O  O   . SER A 1 285 ? -37.960 39.057 -8.848  1.00 91.15  ? 285 SER A O   1 
ATOM   2259 C  CB  . SER A 1 285 ? -35.016 39.154 -8.971  1.00 85.62  ? 285 SER A CB  1 
ATOM   2260 O  OG  . SER A 1 285 ? -34.892 37.875 -9.568  1.00 84.73  ? 285 SER A OG  1 
ATOM   2261 N  N   . SER A 1 286 ? -37.836 39.222 -11.095 1.00 87.07  ? 286 SER A N   1 
ATOM   2262 C  CA  . SER A 1 286 ? -39.169 38.685 -11.332 1.00 84.47  ? 286 SER A CA  1 
ATOM   2263 C  C   . SER A 1 286 ? -39.171 37.959 -12.673 1.00 88.32  ? 286 SER A C   1 
ATOM   2264 O  O   . SER A 1 286 ? -38.128 37.802 -13.315 1.00 87.95  ? 286 SER A O   1 
ATOM   2265 C  CB  . SER A 1 286 ? -40.215 39.806 -11.280 1.00 87.43  ? 286 SER A CB  1 
ATOM   2266 O  OG  . SER A 1 286 ? -41.395 39.439 -11.973 1.00 87.30  ? 286 SER A OG  1 
ATOM   2267 N  N   . THR A 1 287 ? -40.350 37.509 -13.090 1.00 86.81  ? 287 THR A N   1 
ATOM   2268 C  CA  . THR A 1 287 ? -40.504 36.910 -14.407 1.00 86.53  ? 287 THR A CA  1 
ATOM   2269 C  C   . THR A 1 287 ? -40.461 37.989 -15.482 1.00 84.83  ? 287 THR A C   1 
ATOM   2270 O  O   . THR A 1 287 ? -40.815 39.148 -15.245 1.00 82.60  ? 287 THR A O   1 
ATOM   2271 C  CB  . THR A 1 287 ? -41.823 36.143 -14.500 1.00 88.53  ? 287 THR A CB  1 
ATOM   2272 O  OG1 . THR A 1 287 ? -42.918 37.056 -14.360 1.00 91.79  ? 287 THR A OG1 1 
ATOM   2273 C  CG2 . THR A 1 287 ? -41.907 35.089 -13.406 1.00 90.62  ? 287 THR A CG2 1 
ATOM   2274 N  N   . LEU A 1 288 ? -40.022 37.601 -16.676 1.00 89.24  ? 288 LEU A N   1 
ATOM   2275 C  CA  . LEU A 1 288 ? -39.957 38.543 -17.788 1.00 88.15  ? 288 LEU A CA  1 
ATOM   2276 C  C   . LEU A 1 288 ? -41.373 38.885 -18.236 1.00 92.63  ? 288 LEU A C   1 
ATOM   2277 O  O   . LEU A 1 288 ? -42.073 38.045 -18.812 1.00 91.07  ? 288 LEU A O   1 
ATOM   2278 C  CB  . LEU A 1 288 ? -39.132 37.963 -18.933 1.00 87.24  ? 288 LEU A CB  1 
ATOM   2279 C  CG  . LEU A 1 288 ? -38.678 38.948 -20.013 1.00 86.25  ? 288 LEU A CG  1 
ATOM   2280 C  CD1 . LEU A 1 288 ? -38.367 40.314 -19.415 1.00 87.13  ? 288 LEU A CD1 1 
ATOM   2281 C  CD2 . LEU A 1 288 ? -37.459 38.402 -20.739 1.00 80.92  ? 288 LEU A CD2 1 
ATOM   2282 N  N   . ASP A 1 289 ? -41.799 40.113 -17.955 1.00 96.93  ? 289 ASP A N   1 
ATOM   2283 C  CA  . ASP A 1 289 ? -43.140 40.591 -18.263 1.00 99.43  ? 289 ASP A CA  1 
ATOM   2284 C  C   . ASP A 1 289 ? -43.082 41.524 -19.464 1.00 98.12  ? 289 ASP A C   1 
ATOM   2285 O  O   . ASP A 1 289 ? -42.165 42.341 -19.584 1.00 98.64  ? 289 ASP A O   1 
ATOM   2286 C  CB  . ASP A 1 289 ? -43.742 41.314 -17.052 1.00 97.57  ? 289 ASP A CB  1 
ATOM   2287 C  CG  . ASP A 1 289 ? -45.181 41.778 -17.275 1.00 112.11 ? 289 ASP A CG  1 
ATOM   2288 O  OD1 . ASP A 1 289 ? -45.634 41.895 -18.434 1.00 113.10 ? 289 ASP A OD1 1 
ATOM   2289 O  OD2 . ASP A 1 289 ? -45.868 42.044 -16.266 1.00 109.09 ? 289 ASP A OD2 1 
ATOM   2290 N  N   . MET A 1 290 ? -44.078 41.403 -20.346 1.00 94.84  ? 290 MET A N   1 
ATOM   2291 C  CA  . MET A 1 290 ? -44.118 42.248 -21.534 1.00 92.52  ? 290 MET A CA  1 
ATOM   2292 C  C   . MET A 1 290 ? -44.405 43.699 -21.169 1.00 92.89  ? 290 MET A C   1 
ATOM   2293 O  O   . MET A 1 290 ? -43.872 44.620 -21.798 1.00 90.64  ? 290 MET A O   1 
ATOM   2294 C  CB  . MET A 1 290 ? -45.161 41.721 -22.518 1.00 87.79  ? 290 MET A CB  1 
ATOM   2295 C  CG  . MET A 1 290 ? -45.160 42.427 -23.864 1.00 81.14  ? 290 MET A CG  1 
ATOM   2296 S  SD  . MET A 1 290 ? -43.636 42.166 -24.794 1.00 78.55  ? 290 MET A SD  1 
ATOM   2297 C  CE  . MET A 1 290 ? -43.688 40.394 -25.047 1.00 77.10  ? 290 MET A CE  1 
ATOM   2298 N  N   . LYS A 1 291 ? -45.244 43.924 -20.155 1.00 96.10  ? 291 LYS A N   1 
ATOM   2299 C  CA  A LYS A 1 291 ? -45.540 45.284 -19.718 0.45 95.37  ? 291 LYS A CA  1 
ATOM   2300 C  CA  B LYS A 1 291 ? -45.535 45.284 -19.724 0.55 95.37  ? 291 LYS A CA  1 
ATOM   2301 C  C   . LYS A 1 291 ? -44.389 45.905 -18.937 1.00 93.88  ? 291 LYS A C   1 
ATOM   2302 O  O   . LYS A 1 291 ? -44.366 47.128 -18.762 1.00 92.70  ? 291 LYS A O   1 
ATOM   2303 C  CB  A LYS A 1 291 ? -46.815 45.300 -18.873 0.45 93.92  ? 291 LYS A CB  1 
ATOM   2304 C  CB  B LYS A 1 291 ? -46.818 45.312 -18.890 0.55 93.92  ? 291 LYS A CB  1 
ATOM   2305 C  CG  A LYS A 1 291 ? -48.056 44.818 -19.610 0.45 95.65  ? 291 LYS A CG  1 
ATOM   2306 C  CG  B LYS A 1 291 ? -48.102 45.152 -19.701 0.55 95.48  ? 291 LYS A CG  1 
ATOM   2307 C  CD  A LYS A 1 291 ? -49.269 44.780 -18.692 0.45 94.02  ? 291 LYS A CD  1 
ATOM   2308 C  CD  B LYS A 1 291 ? -48.486 46.440 -20.429 0.55 92.97  ? 291 LYS A CD  1 
ATOM   2309 C  CE  A LYS A 1 291 ? -49.651 46.171 -18.213 0.45 92.57  ? 291 LYS A CE  1 
ATOM   2310 C  CE  B LYS A 1 291 ? -48.028 46.443 -21.883 0.55 90.99  ? 291 LYS A CE  1 
ATOM   2311 N  NZ  A LYS A 1 291 ? -50.083 47.046 -19.338 0.45 88.82  ? 291 LYS A NZ  1 
ATOM   2312 N  NZ  B LYS A 1 291 ? -48.321 47.738 -22.558 0.55 88.43  ? 291 LYS A NZ  1 
ATOM   2313 N  N   A GLN A 1 292 ? -43.442 45.096 -18.466 0.40 93.60  ? 292 GLN A N   1 
ATOM   2314 N  N   B GLN A 1 292 ? -43.441 45.098 -18.462 0.60 93.60  ? 292 GLN A N   1 
ATOM   2315 C  CA  A GLN A 1 292 ? -42.261 45.599 -17.778 0.40 92.98  ? 292 GLN A CA  1 
ATOM   2316 C  CA  B GLN A 1 292 ? -42.263 45.616 -17.782 0.60 92.98  ? 292 GLN A CA  1 
ATOM   2317 C  C   A GLN A 1 292 ? -41.079 45.817 -18.714 0.40 89.42  ? 292 GLN A C   1 
ATOM   2318 C  C   B GLN A 1 292 ? -41.081 45.826 -18.718 0.60 89.42  ? 292 GLN A C   1 
ATOM   2319 O  O   A GLN A 1 292 ? -40.074 46.396 -18.291 0.40 90.08  ? 292 GLN A O   1 
ATOM   2320 O  O   B GLN A 1 292 ? -40.075 46.408 -18.298 0.60 90.17  ? 292 GLN A O   1 
ATOM   2321 C  CB  A GLN A 1 292 ? -41.851 44.637 -16.657 0.40 92.55  ? 292 GLN A CB  1 
ATOM   2322 C  CB  B GLN A 1 292 ? -41.844 44.678 -16.646 0.60 92.54  ? 292 GLN A CB  1 
ATOM   2323 C  CG  A GLN A 1 292 ? -42.937 44.376 -15.624 0.40 92.22  ? 292 GLN A CG  1 
ATOM   2324 C  CG  B GLN A 1 292 ? -42.850 44.575 -15.514 0.60 92.19  ? 292 GLN A CG  1 
ATOM   2325 C  CD  A GLN A 1 292 ? -43.131 45.529 -14.665 0.40 93.44  ? 292 GLN A CD  1 
ATOM   2326 C  CD  B GLN A 1 292 ? -42.280 43.871 -14.298 0.60 92.50  ? 292 GLN A CD  1 
ATOM   2327 O  OE1 A GLN A 1 292 ? -44.215 46.108 -14.583 0.40 93.85  ? 292 GLN A OE1 1 
ATOM   2328 O  OE1 B GLN A 1 292 ? -41.121 44.073 -13.937 0.60 89.55  ? 292 GLN A OE1 1 
ATOM   2329 N  NE2 A GLN A 1 292 ? -42.083 45.863 -13.921 0.40 93.20  ? 292 GLN A NE2 1 
ATOM   2330 N  NE2 B GLN A 1 292 ? -43.092 43.034 -13.664 0.60 92.68  ? 292 GLN A NE2 1 
ATOM   2331 N  N   . VAL A 1 293 ? -41.174 45.365 -19.966 1.00 95.92  ? 293 VAL A N   1 
ATOM   2332 C  CA  . VAL A 1 293 ? -40.092 45.559 -20.924 1.00 93.51  ? 293 VAL A CA  1 
ATOM   2333 C  C   . VAL A 1 293 ? -39.975 47.039 -21.259 1.00 92.11  ? 293 VAL A C   1 
ATOM   2334 O  O   . VAL A 1 293 ? -40.953 47.681 -21.663 1.00 93.17  ? 293 VAL A O   1 
ATOM   2335 C  CB  . VAL A 1 293 ? -40.332 44.721 -22.188 1.00 90.55  ? 293 VAL A CB  1 
ATOM   2336 C  CG1 . VAL A 1 293 ? -39.359 45.124 -23.285 1.00 86.70  ? 293 VAL A CG1 1 
ATOM   2337 C  CG2 . VAL A 1 293 ? -40.196 43.241 -21.879 1.00 90.94  ? 293 VAL A CG2 1 
ATOM   2338 N  N   . THR A 1 294 ? -38.775 47.587 -21.090 1.00 84.29  ? 294 THR A N   1 
ATOM   2339 C  CA  . THR A 1 294 ? -38.542 49.001 -21.345 1.00 87.98  ? 294 THR A CA  1 
ATOM   2340 C  C   . THR A 1 294 ? -37.061 49.205 -21.632 1.00 91.62  ? 294 THR A C   1 
ATOM   2341 O  O   . THR A 1 294 ? -36.232 48.324 -21.394 1.00 87.73  ? 294 THR A O   1 
ATOM   2342 C  CB  . THR A 1 294 ? -38.996 49.863 -20.162 1.00 92.36  ? 294 THR A CB  1 
ATOM   2343 O  OG1 . THR A 1 294 ? -38.934 51.248 -20.525 1.00 98.83  ? 294 THR A OG1 1 
ATOM   2344 C  CG2 . THR A 1 294 ? -38.104 49.621 -18.955 1.00 84.98  ? 294 THR A CG2 1 
ATOM   2345 N  N   . ASP A 1 295 ? -36.742 50.386 -22.156 1.00 91.58  ? 295 ASP A N   1 
ATOM   2346 C  CA  . ASP A 1 295 ? -35.371 50.768 -22.464 1.00 93.48  ? 295 ASP A CA  1 
ATOM   2347 C  C   . ASP A 1 295 ? -34.758 51.675 -21.408 1.00 95.00  ? 295 ASP A C   1 
ATOM   2348 O  O   . ASP A 1 295 ? -33.590 52.055 -21.539 1.00 94.56  ? 295 ASP A O   1 
ATOM   2349 C  CB  . ASP A 1 295 ? -35.313 51.469 -23.825 1.00 97.17  ? 295 ASP A CB  1 
ATOM   2350 C  CG  . ASP A 1 295 ? -36.189 52.707 -23.879 1.00 102.81 ? 295 ASP A CG  1 
ATOM   2351 O  OD1 . ASP A 1 295 ? -37.420 52.574 -23.712 1.00 101.49 ? 295 ASP A OD1 1 
ATOM   2352 O  OD2 . ASP A 1 295 ? -35.645 53.815 -24.070 1.00 111.93 ? 295 ASP A OD2 1 
ATOM   2353 N  N   . GLU A 1 296 ? -35.510 52.026 -20.366 1.00 93.33  ? 296 GLU A N   1 
ATOM   2354 C  CA  . GLU A 1 296 ? -35.063 53.020 -19.401 1.00 91.43  ? 296 GLU A CA  1 
ATOM   2355 C  C   . GLU A 1 296 ? -34.034 52.484 -18.413 1.00 84.53  ? 296 GLU A C   1 
ATOM   2356 O  O   . GLU A 1 296 ? -33.386 53.285 -17.730 1.00 96.22  ? 296 GLU A O   1 
ATOM   2357 C  CB  . GLU A 1 296 ? -36.269 53.584 -18.644 1.00 91.92  ? 296 GLU A CB  1 
ATOM   2358 C  CG  . GLU A 1 296 ? -37.449 53.917 -19.547 1.00 100.35 ? 296 GLU A CG  1 
ATOM   2359 C  CD  . GLU A 1 296 ? -38.506 54.751 -18.852 1.00 106.34 ? 296 GLU A CD  1 
ATOM   2360 O  OE1 . GLU A 1 296 ? -38.174 55.859 -18.383 1.00 107.40 ? 296 GLU A OE1 1 
ATOM   2361 O  OE2 . GLU A 1 296 ? -39.668 54.299 -18.773 1.00 103.96 ? 296 GLU A OE2 1 
ATOM   2362 N  N   . PHE A 1 297 ? -33.861 51.168 -18.320 1.00 85.59  ? 297 PHE A N   1 
ATOM   2363 C  CA  . PHE A 1 297 ? -32.860 50.594 -17.431 1.00 79.01  ? 297 PHE A CA  1 
ATOM   2364 C  C   . PHE A 1 297 ? -32.513 49.194 -17.918 1.00 77.30  ? 297 PHE A C   1 
ATOM   2365 O  O   . PHE A 1 297 ? -33.174 48.636 -18.797 1.00 81.65  ? 297 PHE A O   1 
ATOM   2366 C  CB  . PHE A 1 297 ? -33.346 50.570 -15.977 1.00 77.70  ? 297 PHE A CB  1 
ATOM   2367 C  CG  . PHE A 1 297 ? -34.743 50.044 -15.811 1.00 76.50  ? 297 PHE A CG  1 
ATOM   2368 C  CD1 . PHE A 1 297 ? -34.984 48.682 -15.751 1.00 73.69  ? 297 PHE A CD1 1 
ATOM   2369 C  CD2 . PHE A 1 297 ? -35.814 50.915 -15.709 1.00 76.72  ? 297 PHE A CD2 1 
ATOM   2370 C  CE1 . PHE A 1 297 ? -36.269 48.198 -15.599 1.00 74.21  ? 297 PHE A CE1 1 
ATOM   2371 C  CE2 . PHE A 1 297 ? -37.101 50.438 -15.556 1.00 72.79  ? 297 PHE A CE2 1 
ATOM   2372 C  CZ  . PHE A 1 297 ? -37.329 49.077 -15.502 1.00 73.64  ? 297 PHE A CZ  1 
ATOM   2373 N  N   . ASP A 1 298 ? -31.462 48.633 -17.327 1.00 69.51  ? 298 ASP A N   1 
ATOM   2374 C  CA  . ASP A 1 298 ? -31.002 47.306 -17.712 1.00 72.39  ? 298 ASP A CA  1 
ATOM   2375 C  C   . ASP A 1 298 ? -31.996 46.236 -17.276 1.00 75.45  ? 298 ASP A C   1 
ATOM   2376 O  O   . ASP A 1 298 ? -32.579 46.308 -16.191 1.00 75.19  ? 298 ASP A O   1 
ATOM   2377 C  CB  . ASP A 1 298 ? -29.628 47.023 -17.102 1.00 78.40  ? 298 ASP A CB  1 
ATOM   2378 C  CG  . ASP A 1 298 ? -28.490 47.541 -17.961 1.00 83.84  ? 298 ASP A CG  1 
ATOM   2379 O  OD1 . ASP A 1 298 ? -28.575 48.693 -18.436 1.00 94.84  ? 298 ASP A OD1 1 
ATOM   2380 O  OD2 . ASP A 1 298 ? -27.506 46.796 -18.155 1.00 87.91  ? 298 ASP A OD2 1 
ATOM   2381 N  N   . ILE A 1 299 ? -32.191 45.242 -18.139 1.00 74.76  ? 299 ILE A N   1 
ATOM   2382 C  CA  . ILE A 1 299 ? -33.031 44.081 -17.843 1.00 76.82  ? 299 ILE A CA  1 
ATOM   2383 C  C   . ILE A 1 299 ? -32.180 42.852 -18.156 1.00 79.33  ? 299 ILE A C   1 
ATOM   2384 O  O   . ILE A 1 299 ? -32.132 42.383 -19.298 1.00 80.37  ? 299 ILE A O   1 
ATOM   2385 C  CB  . ILE A 1 299 ? -34.339 44.074 -18.640 1.00 76.15  ? 299 ILE A CB  1 
ATOM   2386 C  CG1 . ILE A 1 299 ? -35.166 45.323 -18.327 1.00 74.54  ? 299 ILE A CG1 1 
ATOM   2387 C  CG2 . ILE A 1 299 ? -35.148 42.825 -18.327 1.00 76.16  ? 299 ILE A CG2 1 
ATOM   2388 C  CD1 . ILE A 1 299 ? -36.485 45.384 -19.071 1.00 76.88  ? 299 ILE A CD1 1 
ATOM   2389 N  N   . VAL A 1 300 ? -31.497 42.329 -17.144 1.00 76.34  ? 300 VAL A N   1 
ATOM   2390 C  CA  . VAL A 1 300 ? -30.602 41.187 -17.296 1.00 79.00  ? 300 VAL A CA  1 
ATOM   2391 C  C   . VAL A 1 300 ? -31.413 39.905 -17.195 1.00 78.89  ? 300 VAL A C   1 
ATOM   2392 O  O   . VAL A 1 300 ? -32.253 39.752 -16.300 1.00 78.11  ? 300 VAL A O   1 
ATOM   2393 C  CB  . VAL A 1 300 ? -29.484 41.220 -16.235 1.00 76.21  ? 300 VAL A CB  1 
ATOM   2394 C  CG1 . VAL A 1 300 ? -28.346 40.291 -16.632 1.00 78.67  ? 300 VAL A CG1 1 
ATOM   2395 C  CG2 . VAL A 1 300 ? -28.989 42.643 -16.030 1.00 76.41  ? 300 VAL A CG2 1 
ATOM   2396 N  N   . ILE A 1 301 ? -31.157 38.975 -18.109 1.00 78.42  ? 301 ILE A N   1 
ATOM   2397 C  CA  . ILE A 1 301 ? -31.851 37.692 -18.130 1.00 84.03  ? 301 ILE A CA  1 
ATOM   2398 C  C   . ILE A 1 301 ? -31.129 36.736 -17.188 1.00 86.75  ? 301 ILE A C   1 
ATOM   2399 O  O   . ILE A 1 301 ? -29.914 36.536 -17.299 1.00 85.15  ? 301 ILE A O   1 
ATOM   2400 C  CB  . ILE A 1 301 ? -31.926 37.118 -19.556 1.00 84.15  ? 301 ILE A CB  1 
ATOM   2401 C  CG1 . ILE A 1 301 ? -33.210 37.574 -20.257 1.00 78.36  ? 301 ILE A CG1 1 
ATOM   2402 C  CG2 . ILE A 1 301 ? -31.856 35.596 -19.538 1.00 90.11  ? 301 ILE A CG2 1 
ATOM   2403 C  CD1 . ILE A 1 301 ? -33.257 39.050 -20.578 1.00 76.38  ? 301 ILE A CD1 1 
ATOM   2404 N  N   . THR A 1 302 ? -31.875 36.164 -16.242 1.00 81.10  ? 302 THR A N   1 
ATOM   2405 C  CA  . THR A 1 302 ? -31.322 35.132 -15.372 1.00 80.95  ? 302 THR A CA  1 
ATOM   2406 C  C   . THR A 1 302 ? -31.444 33.761 -16.023 1.00 84.29  ? 302 THR A C   1 
ATOM   2407 O  O   . THR A 1 302 ? -30.444 33.068 -16.242 1.00 86.08  ? 302 THR A O   1 
ATOM   2408 C  CB  . THR A 1 302 ? -32.035 35.143 -14.018 1.00 82.12  ? 302 THR A CB  1 
ATOM   2409 O  OG1 . THR A 1 302 ? -33.434 34.903 -14.214 1.00 84.64  ? 302 THR A OG1 1 
ATOM   2410 C  CG2 . THR A 1 302 ? -31.855 36.480 -13.337 1.00 81.33  ? 302 THR A CG2 1 
ATOM   2411 N  N   . TRP A 1 303 ? -32.671 33.360 -16.341 1.00 89.20  ? 303 TRP A N   1 
ATOM   2412 C  CA  . TRP A 1 303 ? -32.941 32.102 -17.017 1.00 92.85  ? 303 TRP A CA  1 
ATOM   2413 C  C   . TRP A 1 303 ? -33.971 32.348 -18.108 1.00 94.91  ? 303 TRP A C   1 
ATOM   2414 O  O   . TRP A 1 303 ? -34.742 33.309 -18.056 1.00 91.09  ? 303 TRP A O   1 
ATOM   2415 C  CB  . TRP A 1 303 ? -33.442 31.031 -16.039 1.00 88.07  ? 303 TRP A CB  1 
ATOM   2416 C  CG  . TRP A 1 303 ? -34.640 31.460 -15.246 1.00 87.06  ? 303 TRP A CG  1 
ATOM   2417 C  CD1 . TRP A 1 303 ? -34.638 32.097 -14.040 1.00 89.97  ? 303 TRP A CD1 1 
ATOM   2418 C  CD2 . TRP A 1 303 ? -36.016 31.282 -15.604 1.00 87.03  ? 303 TRP A CD2 1 
ATOM   2419 N  NE1 . TRP A 1 303 ? -35.927 32.327 -13.624 1.00 89.83  ? 303 TRP A NE1 1 
ATOM   2420 C  CE2 . TRP A 1 303 ? -36.792 31.836 -14.566 1.00 87.27  ? 303 TRP A CE2 1 
ATOM   2421 C  CE3 . TRP A 1 303 ? -36.668 30.707 -16.700 1.00 91.75  ? 303 TRP A CE3 1 
ATOM   2422 C  CZ2 . TRP A 1 303 ? -38.185 31.833 -14.592 1.00 86.19  ? 303 TRP A CZ2 1 
ATOM   2423 C  CZ3 . TRP A 1 303 ? -38.051 30.705 -16.723 1.00 90.54  ? 303 TRP A CZ3 1 
ATOM   2424 C  CH2 . TRP A 1 303 ? -38.794 31.264 -15.676 1.00 86.95  ? 303 TRP A CH2 1 
ATOM   2425 N  N   . SER A 1 304 ? -33.971 31.465 -19.104 1.00 98.84  ? 304 SER A N   1 
ATOM   2426 C  CA  . SER A 1 304 ? -34.903 31.572 -20.225 1.00 109.75 ? 304 SER A CA  1 
ATOM   2427 C  C   . SER A 1 304 ? -35.127 30.163 -20.761 1.00 116.14 ? 304 SER A C   1 
ATOM   2428 O  O   . SER A 1 304 ? -34.251 29.605 -21.426 1.00 119.28 ? 304 SER A O   1 
ATOM   2429 C  CB  . SER A 1 304 ? -34.364 32.505 -21.302 1.00 119.97 ? 304 SER A CB  1 
ATOM   2430 O  OG  . SER A 1 304 ? -35.208 32.515 -22.440 1.00 112.58 ? 304 SER A OG  1 
ATOM   2431 N  N   . GLU A 1 305 ? -36.296 29.591 -20.460 1.00 117.35 ? 305 GLU A N   1 
ATOM   2432 C  CA  . GLU A 1 305 ? -36.578 28.233 -20.907 1.00 127.01 ? 305 GLU A CA  1 
ATOM   2433 C  C   . GLU A 1 305 ? -36.684 28.150 -22.424 1.00 124.11 ? 305 GLU A C   1 
ATOM   2434 O  O   . GLU A 1 305 ? -36.334 27.121 -23.013 1.00 126.12 ? 305 GLU A O   1 
ATOM   2435 C  CB  . GLU A 1 305 ? -37.863 27.720 -20.258 1.00 127.23 ? 305 GLU A CB  1 
ATOM   2436 C  CG  . GLU A 1 305 ? -37.994 26.210 -20.286 1.00 136.68 ? 305 GLU A CG  1 
ATOM   2437 C  CD  . GLU A 1 305 ? -36.887 25.524 -19.511 1.00 141.04 ? 305 GLU A CD  1 
ATOM   2438 O  OE1 . GLU A 1 305 ? -36.706 25.850 -18.319 1.00 143.97 ? 305 GLU A OE1 1 
ATOM   2439 O  OE2 . GLU A 1 305 ? -36.189 24.669 -20.096 1.00 139.44 ? 305 GLU A OE2 1 
ATOM   2440 N  N   . ALA A 1 306 ? -37.157 29.217 -23.071 1.00 121.84 ? 306 ALA A N   1 
ATOM   2441 C  CA  . ALA A 1 306 ? -37.269 29.213 -24.526 1.00 119.53 ? 306 ALA A CA  1 
ATOM   2442 C  C   . ALA A 1 306 ? -35.894 29.237 -25.182 1.00 121.79 ? 306 ALA A C   1 
ATOM   2443 O  O   . ALA A 1 306 ? -35.589 28.400 -26.040 1.00 122.71 ? 306 ALA A O   1 
ATOM   2444 C  CB  . ALA A 1 306 ? -38.111 30.402 -24.990 1.00 110.90 ? 306 ALA A CB  1 
ATOM   2445 N  N   . GLN A 1 307 ? -35.048 30.192 -24.790 1.00 123.19 ? 307 GLN A N   1 
ATOM   2446 C  CA  . GLN A 1 307 ? -33.703 30.356 -25.337 1.00 124.64 ? 307 GLN A CA  1 
ATOM   2447 C  C   . GLN A 1 307 ? -32.711 30.345 -24.179 1.00 131.83 ? 307 GLN A C   1 
ATOM   2448 O  O   . GLN A 1 307 ? -32.275 31.408 -23.712 1.00 122.30 ? 307 GLN A O   1 
ATOM   2449 C  CB  . GLN A 1 307 ? -33.583 31.646 -26.148 1.00 118.76 ? 307 GLN A CB  1 
ATOM   2450 C  CG  . GLN A 1 307 ? -34.783 31.955 -27.034 1.00 115.35 ? 307 GLN A CG  1 
ATOM   2451 C  CD  . GLN A 1 307 ? -35.014 30.905 -28.102 1.00 123.70 ? 307 GLN A CD  1 
ATOM   2452 O  OE1 . GLN A 1 307 ? -34.072 30.289 -28.600 1.00 129.16 ? 307 GLN A OE1 1 
ATOM   2453 N  NE2 . GLN A 1 307 ? -36.276 30.693 -28.459 1.00 121.77 ? 307 GLN A NE2 1 
ATOM   2454 N  N   . PRO A 1 308 ? -32.333 29.161 -23.684 1.00 127.91 ? 308 PRO A N   1 
ATOM   2455 C  CA  . PRO A 1 308 ? -31.386 29.106 -22.557 1.00 122.50 ? 308 PRO A CA  1 
ATOM   2456 C  C   . PRO A 1 308 ? -29.996 29.610 -22.898 1.00 120.09 ? 308 PRO A C   1 
ATOM   2457 O  O   . PRO A 1 308 ? -29.211 29.873 -21.978 1.00 119.54 ? 308 PRO A O   1 
ATOM   2458 C  CB  . PRO A 1 308 ? -31.357 27.614 -22.190 1.00 123.48 ? 308 PRO A CB  1 
ATOM   2459 C  CG  . PRO A 1 308 ? -32.606 27.042 -22.786 1.00 122.72 ? 308 PRO A CG  1 
ATOM   2460 C  CD  . PRO A 1 308 ? -32.853 27.829 -24.034 1.00 124.53 ? 308 PRO A CD  1 
ATOM   2461 N  N   . GLU A 1 309 ? -29.666 29.749 -24.182 1.00 119.47 ? 309 GLU A N   1 
ATOM   2462 C  CA  A GLU A 1 309 ? -28.338 30.221 -24.559 0.37 120.08 ? 309 GLU A CA  1 
ATOM   2463 C  CA  B GLU A 1 309 ? -28.340 30.223 -24.563 0.63 120.01 ? 309 GLU A CA  1 
ATOM   2464 C  C   . GLU A 1 309 ? -28.122 31.662 -24.110 1.00 120.37 ? 309 GLU A C   1 
ATOM   2465 O  O   . GLU A 1 309 ? -27.097 31.987 -23.499 1.00 117.24 ? 309 GLU A O   1 
ATOM   2466 C  CB  A GLU A 1 309 ? -28.145 30.082 -26.070 0.37 119.58 ? 309 GLU A CB  1 
ATOM   2467 C  CB  B GLU A 1 309 ? -28.155 30.102 -26.077 0.63 119.72 ? 309 GLU A CB  1 
ATOM   2468 C  CG  A GLU A 1 309 ? -26.849 30.677 -26.594 0.37 117.89 ? 309 GLU A CG  1 
ATOM   2469 C  CG  B GLU A 1 309 ? -29.042 29.056 -26.742 0.63 119.72 ? 309 GLU A CG  1 
ATOM   2470 C  CD  A GLU A 1 309 ? -27.027 32.085 -27.125 0.37 118.01 ? 309 GLU A CD  1 
ATOM   2471 C  CD  B GLU A 1 309 ? -30.421 29.590 -27.090 0.63 121.56 ? 309 GLU A CD  1 
ATOM   2472 O  OE1 A GLU A 1 309 ? -28.005 32.324 -27.865 0.37 117.91 ? 309 GLU A OE1 1 
ATOM   2473 O  OE1 B GLU A 1 309 ? -30.570 30.825 -27.200 0.63 120.93 ? 309 GLU A OE1 1 
ATOM   2474 O  OE2 A GLU A 1 309 ? -26.195 32.956 -26.796 0.37 117.50 ? 309 GLU A OE2 1 
ATOM   2475 O  OE2 B GLU A 1 309 ? -31.355 28.775 -27.247 0.63 122.39 ? 309 GLU A OE2 1 
ATOM   2476 N  N   . GLN A 1 310 ? -29.082 32.539 -24.400 1.00 125.15 ? 310 GLN A N   1 
ATOM   2477 C  CA  . GLN A 1 310 ? -28.987 33.940 -24.010 1.00 118.68 ? 310 GLN A CA  1 
ATOM   2478 C  C   . GLN A 1 310 ? -29.249 34.104 -22.518 1.00 112.61 ? 310 GLN A C   1 
ATOM   2479 O  O   . GLN A 1 310 ? -30.389 34.342 -22.106 1.00 119.03 ? 310 GLN A O   1 
ATOM   2480 C  CB  . GLN A 1 310 ? -29.972 34.788 -24.819 1.00 119.54 ? 310 GLN A CB  1 
ATOM   2481 C  CG  . GLN A 1 310 ? -29.721 34.790 -26.322 1.00 120.45 ? 310 GLN A CG  1 
ATOM   2482 C  CD  . GLN A 1 310 ? -28.565 35.687 -26.725 1.00 124.97 ? 310 GLN A CD  1 
ATOM   2483 O  OE1 . GLN A 1 310 ? -28.765 36.836 -27.119 1.00 125.79 ? 310 GLN A OE1 1 
ATOM   2484 N  NE2 . GLN A 1 310 ? -27.348 35.165 -26.633 1.00 120.23 ? 310 GLN A NE2 1 
ATOM   2485 N  N   . ALA A 1 311 ? -28.203 33.980 -21.703 1.00 108.81 ? 311 ALA A N   1 
ATOM   2486 C  CA  . ALA A 1 311 ? -28.319 34.107 -20.258 1.00 103.29 ? 311 ALA A CA  1 
ATOM   2487 C  C   . ALA A 1 311 ? -27.193 34.984 -19.735 1.00 97.73  ? 311 ALA A C   1 
ATOM   2488 O  O   . ALA A 1 311 ? -26.059 34.901 -20.213 1.00 101.20 ? 311 ALA A O   1 
ATOM   2489 C  CB  . ALA A 1 311 ? -28.281 32.737 -19.568 1.00 104.79 ? 311 ALA A CB  1 
ATOM   2490 N  N   . GLY A 1 312 ? -27.512 35.820 -18.749 1.00 91.61  ? 312 GLY A N   1 
ATOM   2491 C  CA  . GLY A 1 312 ? -26.541 36.742 -18.196 1.00 90.17  ? 312 GLY A CA  1 
ATOM   2492 C  C   . GLY A 1 312 ? -26.326 38.002 -19.001 1.00 89.19  ? 312 GLY A C   1 
ATOM   2493 O  O   . GLY A 1 312 ? -25.418 38.777 -18.680 1.00 84.31  ? 312 GLY A O   1 
ATOM   2494 N  N   . LYS A 1 313 ? -27.129 38.231 -20.035 1.00 89.53  ? 313 LYS A N   1 
ATOM   2495 C  CA  . LYS A 1 313 ? -27.018 39.405 -20.885 1.00 85.27  ? 313 LYS A CA  1 
ATOM   2496 C  C   . LYS A 1 313 ? -28.245 40.288 -20.706 1.00 85.93  ? 313 LYS A C   1 
ATOM   2497 O  O   . LYS A 1 313 ? -29.331 39.808 -20.369 1.00 84.72  ? 313 LYS A O   1 
ATOM   2498 C  CB  . LYS A 1 313 ? -26.874 39.001 -22.356 1.00 87.86  ? 313 LYS A CB  1 
ATOM   2499 C  CG  . LYS A 1 313 ? -26.595 37.518 -22.559 1.00 94.66  ? 313 LYS A CG  1 
ATOM   2500 C  CD  . LYS A 1 313 ? -26.380 37.174 -24.025 1.00 97.44  ? 313 LYS A CD  1 
ATOM   2501 C  CE  . LYS A 1 313 ? -25.092 37.784 -24.554 1.00 89.46  ? 313 LYS A CE  1 
ATOM   2502 N  NZ  . LYS A 1 313 ? -24.748 37.266 -25.909 1.00 94.59  ? 313 LYS A NZ  1 
ATOM   2503 N  N   . THR A 1 314 ? -28.063 41.587 -20.923 1.00 82.52  ? 314 THR A N   1 
ATOM   2504 C  CA  . THR A 1 314 ? -29.191 42.503 -20.860 1.00 85.03  ? 314 THR A CA  1 
ATOM   2505 C  C   . THR A 1 314 ? -30.089 42.318 -22.078 1.00 83.78  ? 314 THR A C   1 
ATOM   2506 O  O   . THR A 1 314 ? -29.650 41.868 -23.141 1.00 81.12  ? 314 THR A O   1 
ATOM   2507 C  CB  . THR A 1 314 ? -28.713 43.954 -20.774 1.00 83.05  ? 314 THR A CB  1 
ATOM   2508 O  OG1 . THR A 1 314 ? -29.825 44.838 -20.965 1.00 82.25  ? 314 THR A OG1 1 
ATOM   2509 C  CG2 . THR A 1 314 ? -27.665 44.238 -21.830 1.00 82.25  ? 314 THR A CG2 1 
ATOM   2510 N  N   . LEU A 1 315 ? -31.368 42.665 -21.908 1.00 84.65  ? 315 LEU A N   1 
ATOM   2511 C  CA  . LEU A 1 315 ? -32.329 42.502 -22.994 1.00 83.04  ? 315 LEU A CA  1 
ATOM   2512 C  C   . LEU A 1 315 ? -31.952 43.342 -24.208 1.00 81.91  ? 315 LEU A C   1 
ATOM   2513 O  O   . LEU A 1 315 ? -32.292 42.984 -25.341 1.00 82.28  ? 315 LEU A O   1 
ATOM   2514 C  CB  . LEU A 1 315 ? -33.733 42.864 -22.508 1.00 76.77  ? 315 LEU A CB  1 
ATOM   2515 C  CG  . LEU A 1 315 ? -34.896 42.580 -23.461 1.00 76.46  ? 315 LEU A CG  1 
ATOM   2516 C  CD1 . LEU A 1 315 ? -35.040 41.086 -23.705 1.00 78.66  ? 315 LEU A CD1 1 
ATOM   2517 C  CD2 . LEU A 1 315 ? -36.189 43.167 -22.920 1.00 76.56  ? 315 LEU A CD2 1 
ATOM   2518 N  N   . GLN A 1 316 ? -31.243 44.453 -23.994 1.00 80.39  ? 316 GLN A N   1 
ATOM   2519 C  CA  . GLN A 1 316 ? -30.814 45.280 -25.116 1.00 82.36  ? 316 GLN A CA  1 
ATOM   2520 C  C   . GLN A 1 316 ? -29.709 44.596 -25.913 1.00 83.28  ? 316 GLN A C   1 
ATOM   2521 O  O   . GLN A 1 316 ? -29.687 44.677 -27.147 1.00 82.29  ? 316 GLN A O   1 
ATOM   2522 C  CB  . GLN A 1 316 ? -30.351 46.647 -24.614 1.00 83.31  ? 316 GLN A CB  1 
ATOM   2523 C  CG  . GLN A 1 316 ? -30.229 47.690 -25.708 1.00 84.94  ? 316 GLN A CG  1 
ATOM   2524 C  CD  . GLN A 1 316 ? -31.555 47.975 -26.385 1.00 85.65  ? 316 GLN A CD  1 
ATOM   2525 O  OE1 . GLN A 1 316 ? -32.526 48.361 -25.734 1.00 87.69  ? 316 GLN A OE1 1 
ATOM   2526 N  NE2 . GLN A 1 316 ? -31.606 47.777 -27.697 1.00 85.52  ? 316 GLN A NE2 1 
ATOM   2527 N  N   . GLN A 1 317 ? -28.779 43.925 -25.227 1.00 82.79  ? 317 GLN A N   1 
ATOM   2528 C  CA  . GLN A 1 317 ? -27.759 43.150 -25.927 1.00 87.66  ? 317 GLN A CA  1 
ATOM   2529 C  C   . GLN A 1 317 ? -28.385 42.025 -26.739 1.00 82.91  ? 317 GLN A C   1 
ATOM   2530 O  O   . GLN A 1 317 ? -27.971 41.761 -27.875 1.00 81.44  ? 317 GLN A O   1 
ATOM   2531 C  CB  . GLN A 1 317 ? -26.747 42.582 -24.931 1.00 86.80  ? 317 GLN A CB  1 
ATOM   2532 C  CG  . GLN A 1 317 ? -25.571 43.492 -24.620 1.00 86.91  ? 317 GLN A CG  1 
ATOM   2533 C  CD  . GLN A 1 317 ? -24.683 42.928 -23.525 1.00 85.97  ? 317 GLN A CD  1 
ATOM   2534 O  OE1 . GLN A 1 317 ? -25.161 42.267 -22.603 1.00 84.74  ? 317 GLN A OE1 1 
ATOM   2535 N  NE2 . GLN A 1 317 ? -23.383 43.179 -23.627 1.00 85.01  ? 317 GLN A NE2 1 
ATOM   2536 N  N   . ILE A 1 318 ? -29.384 41.347 -26.170 1.00 88.20  ? 318 ILE A N   1 
ATOM   2537 C  CA  . ILE A 1 318 ? -30.048 40.259 -26.880 1.00 89.21  ? 318 ILE A CA  1 
ATOM   2538 C  C   . ILE A 1 318 ? -30.830 40.797 -28.070 1.00 84.76  ? 318 ILE A C   1 
ATOM   2539 O  O   . ILE A 1 318 ? -30.845 40.189 -29.148 1.00 84.95  ? 318 ILE A O   1 
ATOM   2540 C  CB  . ILE A 1 318 ? -30.951 39.473 -25.913 1.00 91.48  ? 318 ILE A CB  1 
ATOM   2541 C  CG1 . ILE A 1 318 ? -30.135 38.958 -24.725 1.00 89.53  ? 318 ILE A CG1 1 
ATOM   2542 C  CG2 . ILE A 1 318 ? -31.639 38.324 -26.635 1.00 92.26  ? 318 ILE A CG2 1 
ATOM   2543 C  CD1 . ILE A 1 318 ? -30.952 38.211 -23.699 1.00 92.18  ? 318 ILE A CD1 1 
ATOM   2544 N  N   . ALA A 1 319 ? -31.485 41.947 -27.899 1.00 86.48  ? 319 ALA A N   1 
ATOM   2545 C  CA  . ALA A 1 319 ? -32.249 42.535 -28.994 1.00 85.32  ? 319 ALA A CA  1 
ATOM   2546 C  C   . ALA A 1 319 ? -31.345 43.010 -30.124 1.00 87.80  ? 319 ALA A C   1 
ATOM   2547 O  O   . ALA A 1 319 ? -31.741 42.962 -31.294 1.00 88.85  ? 319 ALA A O   1 
ATOM   2548 C  CB  . ALA A 1 319 ? -33.104 43.689 -28.472 1.00 83.08  ? 319 ALA A CB  1 
ATOM   2549 N  N   . ASP A 1 320 ? -30.133 43.466 -29.800 1.00 80.27  ? 320 ASP A N   1 
ATOM   2550 C  CA  . ASP A 1 320 ? -29.210 43.922 -30.833 1.00 84.41  ? 320 ASP A CA  1 
ATOM   2551 C  C   . ASP A 1 320 ? -28.491 42.763 -31.511 1.00 86.58  ? 320 ASP A C   1 
ATOM   2552 O  O   . ASP A 1 320 ? -28.183 42.845 -32.706 1.00 87.11  ? 320 ASP A O   1 
ATOM   2553 C  CB  . ASP A 1 320 ? -28.191 44.896 -30.238 1.00 82.64  ? 320 ASP A CB  1 
ATOM   2554 C  CG  . ASP A 1 320 ? -28.838 46.154 -29.693 1.00 80.73  ? 320 ASP A CG  1 
ATOM   2555 O  OD1 . ASP A 1 320 ? -29.936 46.513 -30.170 1.00 79.71  ? 320 ASP A OD1 1 
ATOM   2556 O  OD2 . ASP A 1 320 ? -28.250 46.783 -28.790 1.00 80.62  ? 320 ASP A OD2 1 
ATOM   2557 N  N   . GLU A 1 321 ? -28.211 41.686 -30.772 1.00 84.81  ? 321 GLU A N   1 
ATOM   2558 C  CA  . GLU A 1 321 ? -27.605 40.509 -31.385 1.00 88.33  ? 321 GLU A CA  1 
ATOM   2559 C  C   . GLU A 1 321 ? -28.548 39.874 -32.398 1.00 87.39  ? 321 GLU A C   1 
ATOM   2560 O  O   . GLU A 1 321 ? -28.113 39.412 -33.460 1.00 88.22  ? 321 GLU A O   1 
ATOM   2561 C  CB  . GLU A 1 321 ? -27.213 39.503 -30.302 1.00 90.53  ? 321 GLU A CB  1 
ATOM   2562 C  CG  . GLU A 1 321 ? -26.740 38.157 -30.827 1.00 94.05  ? 321 GLU A CG  1 
ATOM   2563 C  CD  . GLU A 1 321 ? -26.366 37.200 -29.710 1.00 100.10 ? 321 GLU A CD  1 
ATOM   2564 O  OE1 . GLU A 1 321 ? -25.864 37.671 -28.667 1.00 99.14  ? 321 GLU A OE1 1 
ATOM   2565 O  OE2 . GLU A 1 321 ? -26.582 35.980 -29.870 1.00 104.59 ? 321 GLU A OE2 1 
ATOM   2566 N  N   . TRP A 1 322 ? -29.843 39.849 -32.092 1.00 87.51  ? 322 TRP A N   1 
ATOM   2567 C  CA  . TRP A 1 322 ? -30.845 39.328 -33.010 1.00 88.78  ? 322 TRP A CA  1 
ATOM   2568 C  C   . TRP A 1 322 ? -31.338 40.368 -34.007 1.00 91.56  ? 322 TRP A C   1 
ATOM   2569 O  O   . TRP A 1 322 ? -32.054 40.004 -34.947 1.00 90.27  ? 322 TRP A O   1 
ATOM   2570 C  CB  . TRP A 1 322 ? -32.034 38.761 -32.224 1.00 88.79  ? 322 TRP A CB  1 
ATOM   2571 C  CG  . TRP A 1 322 ? -31.712 37.492 -31.491 1.00 89.03  ? 322 TRP A CG  1 
ATOM   2572 C  CD1 . TRP A 1 322 ? -30.658 36.657 -31.725 1.00 92.15  ? 322 TRP A CD1 1 
ATOM   2573 C  CD2 . TRP A 1 322 ? -32.442 36.919 -30.399 1.00 86.04  ? 322 TRP A CD2 1 
ATOM   2574 N  NE1 . TRP A 1 322 ? -30.690 35.598 -30.851 1.00 93.17  ? 322 TRP A NE1 1 
ATOM   2575 C  CE2 . TRP A 1 322 ? -31.775 35.735 -30.026 1.00 88.88  ? 322 TRP A CE2 1 
ATOM   2576 C  CE3 . TRP A 1 322 ? -33.596 37.291 -29.702 1.00 85.00  ? 322 TRP A CE3 1 
ATOM   2577 C  CZ2 . TRP A 1 322 ? -32.223 34.921 -28.988 1.00 95.63  ? 322 TRP A CZ2 1 
ATOM   2578 C  CZ3 . TRP A 1 322 ? -34.038 36.481 -28.669 1.00 86.30  ? 322 TRP A CZ3 1 
ATOM   2579 C  CH2 . TRP A 1 322 ? -33.354 35.310 -28.324 1.00 92.11  ? 322 TRP A CH2 1 
ATOM   2580 N  N   . GLN A 1 323 ? -30.968 41.640 -33.828 1.00 92.86  ? 323 GLN A N   1 
ATOM   2581 C  CA  . GLN A 1 323 ? -31.364 42.724 -34.730 1.00 96.09  ? 323 GLN A CA  1 
ATOM   2582 C  C   . GLN A 1 323 ? -32.885 42.879 -34.762 1.00 90.25  ? 323 GLN A C   1 
ATOM   2583 O  O   . GLN A 1 323 ? -33.498 43.051 -35.818 1.00 93.19  ? 323 GLN A O   1 
ATOM   2584 C  CB  . GLN A 1 323 ? -30.796 42.502 -36.135 1.00 91.26  ? 323 GLN A CB  1 
ATOM   2585 C  CG  . GLN A 1 323 ? -29.289 42.259 -36.160 1.00 91.99  ? 323 GLN A CG  1 
ATOM   2586 C  CD  . GLN A 1 323 ? -28.855 41.366 -37.307 1.00 94.52  ? 323 GLN A CD  1 
ATOM   2587 O  OE1 . GLN A 1 323 ? -28.269 40.304 -37.094 1.00 104.20 ? 323 GLN A OE1 1 
ATOM   2588 N  NE2 . GLN A 1 323 ? -29.137 41.795 -38.532 1.00 86.08  ? 323 GLN A NE2 1 
ATOM   2589 N  N   . VAL A 1 324 ? -33.496 42.804 -33.576 1.00 91.89  ? 324 VAL A N   1 
ATOM   2590 C  CA  . VAL A 1 324 ? -34.943 42.879 -33.409 1.00 91.95  ? 324 VAL A CA  1 
ATOM   2591 C  C   . VAL A 1 324 ? -35.239 43.776 -32.208 1.00 85.98  ? 324 VAL A C   1 
ATOM   2592 O  O   . VAL A 1 324 ? -34.385 43.997 -31.349 1.00 83.34  ? 324 VAL A O   1 
ATOM   2593 C  CB  . VAL A 1 324 ? -35.565 41.468 -33.231 1.00 90.59  ? 324 VAL A CB  1 
ATOM   2594 C  CG1 . VAL A 1 324 ? -37.073 41.523 -33.247 1.00 90.27  ? 324 VAL A CG1 1 
ATOM   2595 C  CG2 . VAL A 1 324 ? -35.076 40.517 -34.321 1.00 90.04  ? 324 VAL A CG2 1 
ATOM   2596 N  N   . SER A 1 325 ? -36.462 44.309 -32.164 1.00 84.28  ? 325 SER A N   1 
ATOM   2597 C  CA  . SER A 1 325 ? -36.873 45.236 -31.116 1.00 82.43  ? 325 SER A CA  1 
ATOM   2598 C  C   . SER A 1 325 ? -36.862 44.561 -29.743 1.00 86.39  ? 325 SER A C   1 
ATOM   2599 O  O   . SER A 1 325 ? -36.728 43.341 -29.615 1.00 88.14  ? 325 SER A O   1 
ATOM   2600 C  CB  . SER A 1 325 ? -38.268 45.786 -31.408 1.00 86.09  ? 325 SER A CB  1 
ATOM   2601 O  OG  . SER A 1 325 ? -39.250 44.774 -31.262 1.00 88.87  ? 325 SER A OG  1 
ATOM   2602 N  N   . LEU A 1 326 ? -37.026 45.383 -28.701 1.00 84.93  ? 326 LEU A N   1 
ATOM   2603 C  CA  . LEU A 1 326 ? -37.008 44.873 -27.331 1.00 82.37  ? 326 LEU A CA  1 
ATOM   2604 C  C   . LEU A 1 326 ? -38.219 43.992 -27.046 1.00 82.22  ? 326 LEU A C   1 
ATOM   2605 O  O   . LEU A 1 326 ? -38.079 42.880 -26.524 1.00 83.71  ? 326 LEU A O   1 
ATOM   2606 C  CB  . LEU A 1 326 ? -36.952 46.031 -26.333 1.00 81.79  ? 326 LEU A CB  1 
ATOM   2607 C  CG  . LEU A 1 326 ? -35.593 46.676 -26.061 1.00 81.07  ? 326 LEU A CG  1 
ATOM   2608 C  CD1 . LEU A 1 326 ? -35.714 47.769 -25.007 1.00 82.59  ? 326 LEU A CD1 1 
ATOM   2609 C  CD2 . LEU A 1 326 ? -34.587 45.624 -25.630 1.00 80.65  ? 326 LEU A CD2 1 
ATOM   2610 N  N   . HIS A 1 327 ? -39.421 44.483 -27.362 1.00 84.05  ? 327 HIS A N   1 
ATOM   2611 C  CA  . HIS A 1 327 ? -40.631 43.719 -27.071 1.00 83.20  ? 327 HIS A CA  1 
ATOM   2612 C  C   . HIS A 1 327 ? -40.669 42.405 -27.839 1.00 82.54  ? 327 HIS A C   1 
ATOM   2613 O  O   . HIS A 1 327 ? -41.206 41.410 -27.339 1.00 84.42  ? 327 HIS A O   1 
ATOM   2614 C  CB  . HIS A 1 327 ? -41.873 44.555 -27.385 1.00 81.12  ? 327 HIS A CB  1 
ATOM   2615 C  CG  . HIS A 1 327 ? -42.181 45.593 -26.351 1.00 85.85  ? 327 HIS A CG  1 
ATOM   2616 N  ND1 . HIS A 1 327 ? -41.471 46.769 -26.238 1.00 85.30  ? 327 HIS A ND1 1 
ATOM   2617 C  CD2 . HIS A 1 327 ? -43.124 45.629 -25.379 1.00 83.28  ? 327 HIS A CD2 1 
ATOM   2618 C  CE1 . HIS A 1 327 ? -41.963 47.485 -25.243 1.00 85.87  ? 327 HIS A CE1 1 
ATOM   2619 N  NE2 . HIS A 1 327 ? -42.967 46.816 -24.705 1.00 84.98  ? 327 HIS A NE2 1 
ATOM   2620 N  N   . ASP A 1 328 ? -40.110 42.378 -29.050 1.00 83.67  ? 328 ASP A N   1 
ATOM   2621 C  CA  . ASP A 1 328 ? -40.045 41.130 -29.800 1.00 86.67  ? 328 ASP A CA  1 
ATOM   2622 C  C   . ASP A 1 328 ? -38.922 40.227 -29.307 1.00 85.44  ? 328 ASP A C   1 
ATOM   2623 O  O   . ASP A 1 328 ? -39.063 39.000 -29.340 1.00 91.48  ? 328 ASP A O   1 
ATOM   2624 C  CB  . ASP A 1 328 ? -39.871 41.414 -31.291 1.00 86.36  ? 328 ASP A CB  1 
ATOM   2625 C  CG  . ASP A 1 328 ? -41.122 41.981 -31.932 1.00 86.79  ? 328 ASP A CG  1 
ATOM   2626 O  OD1 . ASP A 1 328 ? -42.180 42.003 -31.267 1.00 84.74  ? 328 ASP A OD1 1 
ATOM   2627 O  OD2 . ASP A 1 328 ? -41.047 42.401 -33.106 1.00 89.60  ? 328 ASP A OD2 1 
ATOM   2628 N  N   . ALA A 1 329 ? -37.804 40.806 -28.858 1.00 87.40  ? 329 ALA A N   1 
ATOM   2629 C  CA  . ALA A 1 329 ? -36.745 39.994 -28.269 1.00 86.78  ? 329 ALA A CA  1 
ATOM   2630 C  C   . ALA A 1 329 ? -37.238 39.285 -27.017 1.00 88.51  ? 329 ALA A C   1 
ATOM   2631 O  O   . ALA A 1 329 ? -36.940 38.104 -26.804 1.00 90.76  ? 329 ALA A O   1 
ATOM   2632 C  CB  . ALA A 1 329 ? -35.526 40.860 -27.951 1.00 86.71  ? 329 ALA A CB  1 
ATOM   2633 N  N   . ALA A 1 330 ? -38.001 39.989 -26.178 1.00 86.16  ? 330 ALA A N   1 
ATOM   2634 C  CA  . ALA A 1 330 ? -38.578 39.354 -24.999 1.00 85.21  ? 330 ALA A CA  1 
ATOM   2635 C  C   . ALA A 1 330 ? -39.589 38.284 -25.391 1.00 88.54  ? 330 ALA A C   1 
ATOM   2636 O  O   . ALA A 1 330 ? -39.622 37.204 -24.791 1.00 90.21  ? 330 ALA A O   1 
ATOM   2637 C  CB  . ALA A 1 330 ? -39.230 40.405 -24.102 1.00 80.70  ? 330 ALA A CB  1 
ATOM   2638 N  N   . ALA A 1 331 ? -40.409 38.563 -26.410 1.00 89.20  ? 331 ALA A N   1 
ATOM   2639 C  CA  . ALA A 1 331 ? -41.472 37.640 -26.803 1.00 88.76  ? 331 ALA A CA  1 
ATOM   2640 C  C   . ALA A 1 331 ? -40.930 36.250 -27.110 1.00 94.23  ? 331 ALA A C   1 
ATOM   2641 O  O   . ALA A 1 331 ? -41.535 35.241 -26.729 1.00 93.84  ? 331 ALA A O   1 
ATOM   2642 C  CB  . ALA A 1 331 ? -42.228 38.197 -28.010 1.00 90.67  ? 331 ALA A CB  1 
ATOM   2643 N  N   . ARG A 1 332 ? -39.791 36.175 -27.797 1.00 90.32  ? 332 ARG A N   1 
ATOM   2644 C  CA  A ARG A 1 332 ? -39.198 34.878 -28.088 0.47 91.80  ? 332 ARG A CA  1 
ATOM   2645 C  CA  B ARG A 1 332 ? -39.142 34.910 -28.117 0.53 91.79  ? 332 ARG A CA  1 
ATOM   2646 C  C   . ARG A 1 332 ? -38.302 34.369 -26.966 1.00 92.11  ? 332 ARG A C   1 
ATOM   2647 O  O   . ARG A 1 332 ? -37.885 33.206 -27.013 1.00 98.42  ? 332 ARG A O   1 
ATOM   2648 C  CB  A ARG A 1 332 ? -38.413 34.922 -29.406 0.47 89.58  ? 332 ARG A CB  1 
ATOM   2649 C  CB  B ARG A 1 332 ? -38.266 35.084 -29.360 0.53 89.67  ? 332 ARG A CB  1 
ATOM   2650 C  CG  A ARG A 1 332 ? -37.467 36.095 -29.560 0.47 89.41  ? 332 ARG A CG  1 
ATOM   2651 C  CG  B ARG A 1 332 ? -38.974 35.797 -30.504 0.53 86.70  ? 332 ARG A CG  1 
ATOM   2652 C  CD  A ARG A 1 332 ? -36.663 35.966 -30.847 0.47 87.99  ? 332 ARG A CD  1 
ATOM   2653 C  CD  B ARG A 1 332 ? -37.996 36.279 -31.563 0.53 85.54  ? 332 ARG A CD  1 
ATOM   2654 N  NE  A ARG A 1 332 ? -35.861 34.747 -30.858 0.47 88.64  ? 332 ARG A NE  1 
ATOM   2655 N  NE  B ARG A 1 332 ? -38.656 37.097 -32.573 0.53 85.59  ? 332 ARG A NE  1 
ATOM   2656 C  CZ  A ARG A 1 332 ? -34.970 34.440 -31.791 0.47 86.23  ? 332 ARG A CZ  1 
ATOM   2657 C  CZ  B ARG A 1 332 ? -38.034 37.687 -33.585 0.53 85.15  ? 332 ARG A CZ  1 
ATOM   2658 N  NH1 A ARG A 1 332 ? -34.729 35.248 -32.811 0.47 85.26  ? 332 ARG A NH1 1 
ATOM   2659 N  NH1 B ARG A 1 332 ? -36.727 37.569 -33.756 0.53 84.73  ? 332 ARG A NH1 1 
ATOM   2660 N  NH2 A ARG A 1 332 ? -34.300 33.295 -31.696 0.47 87.13  ? 332 ARG A NH2 1 
ATOM   2661 N  NH2 B ARG A 1 332 ? -38.740 38.414 -34.446 0.53 82.51  ? 332 ARG A NH2 1 
ATOM   2662 N  N   A LEU A 1 333 ? -38.017 35.194 -25.958 0.48 89.75  ? 333 LEU A N   1 
ATOM   2663 N  N   B LEU A 1 333 ? -38.023 35.187 -25.951 0.52 89.75  ? 333 LEU A N   1 
ATOM   2664 C  CA  A LEU A 1 333 ? -37.321 34.734 -24.763 0.48 93.34  ? 333 LEU A CA  1 
ATOM   2665 C  CA  B LEU A 1 333 ? -37.324 34.724 -24.760 0.52 93.34  ? 333 LEU A CA  1 
ATOM   2666 C  C   A LEU A 1 333 ? -38.267 34.226 -23.684 0.48 96.40  ? 333 LEU A C   1 
ATOM   2667 C  C   B LEU A 1 333 ? -38.270 34.222 -23.681 0.52 96.41  ? 333 LEU A C   1 
ATOM   2668 O  O   A LEU A 1 333 ? -37.841 33.450 -22.821 0.48 98.26  ? 333 LEU A O   1 
ATOM   2669 O  O   B LEU A 1 333 ? -37.846 33.448 -22.816 0.52 98.26  ? 333 LEU A O   1 
ATOM   2670 C  CB  A LEU A 1 333 ? -36.460 35.860 -24.180 0.48 92.68  ? 333 LEU A CB  1 
ATOM   2671 C  CB  B LEU A 1 333 ? -36.456 35.846 -24.180 0.52 92.68  ? 333 LEU A CB  1 
ATOM   2672 C  CG  A LEU A 1 333 ? -35.125 36.165 -24.858 0.48 93.89  ? 333 LEU A CG  1 
ATOM   2673 C  CG  B LEU A 1 333 ? -35.123 36.153 -24.861 0.52 93.91  ? 333 LEU A CG  1 
ATOM   2674 C  CD1 A LEU A 1 333 ? -34.507 37.418 -24.261 0.48 86.91  ? 333 LEU A CD1 1 
ATOM   2675 C  CD1 B LEU A 1 333 ? -34.509 37.409 -24.268 0.52 86.91  ? 333 LEU A CD1 1 
ATOM   2676 C  CD2 A LEU A 1 333 ? -34.176 34.986 -24.723 0.48 97.72  ? 333 LEU A CD2 1 
ATOM   2677 C  CD2 B LEU A 1 333 ? -34.171 34.977 -24.722 0.52 97.73  ? 333 LEU A CD2 1 
ATOM   2678 N  N   . MET A 1 334 ? -39.532 34.639 -23.716 1.00 93.48  ? 334 MET A N   1 
ATOM   2679 C  CA  . MET A 1 334 ? -40.475 34.258 -22.680 1.00 89.28  ? 334 MET A CA  1 
ATOM   2680 C  C   . MET A 1 334 ? -40.870 32.788 -22.807 1.00 93.56  ? 334 MET A C   1 
ATOM   2681 O  O   . MET A 1 334 ? -40.886 32.232 -23.909 1.00 95.26  ? 334 MET A O   1 
ATOM   2682 C  CB  . MET A 1 334 ? -41.721 35.135 -22.752 1.00 85.72  ? 334 MET A CB  1 
ATOM   2683 C  CG  . MET A 1 334 ? -41.475 36.567 -22.331 1.00 87.40  ? 334 MET A CG  1 
ATOM   2684 S  SD  . MET A 1 334 ? -42.926 37.620 -22.482 1.00 89.79  ? 334 MET A SD  1 
ATOM   2685 C  CE  . MET A 1 334 ? -42.248 39.161 -21.876 1.00 92.61  ? 334 MET A CE  1 
ATOM   2686 N  N   . PRO A 1 335 ? -41.189 32.130 -21.683 1.00 104.04 ? 335 PRO A N   1 
ATOM   2687 C  CA  . PRO A 1 335 ? -41.136 32.643 -20.304 1.00 107.73 ? 335 PRO A CA  1 
ATOM   2688 C  C   . PRO A 1 335 ? -39.703 32.702 -19.784 1.00 103.14 ? 335 PRO A C   1 
ATOM   2689 O  O   . PRO A 1 335 ? -38.897 31.824 -20.083 1.00 98.93  ? 335 PRO A O   1 
ATOM   2690 C  CB  . PRO A 1 335 ? -42.001 31.637 -19.533 1.00 97.57  ? 335 PRO A CB  1 
ATOM   2691 C  CG  . PRO A 1 335 ? -41.834 30.355 -20.291 1.00 97.45  ? 335 PRO A CG  1 
ATOM   2692 C  CD  . PRO A 1 335 ? -41.751 30.769 -21.739 1.00 92.63  ? 335 PRO A CD  1 
ATOM   2693 N  N   . ALA A 1 336 ? -39.352 33.725 -19.008 1.00 92.40  ? 336 ALA A N   1 
ATOM   2694 C  CA  . ALA A 1 336 ? -37.976 33.907 -18.576 1.00 91.37  ? 336 ALA A CA  1 
ATOM   2695 C  C   . ALA A 1 336 ? -37.947 34.687 -17.270 1.00 88.51  ? 336 ALA A C   1 
ATOM   2696 O  O   . ALA A 1 336 ? -38.931 35.321 -16.878 1.00 89.61  ? 336 ALA A O   1 
ATOM   2697 C  CB  . ALA A 1 336 ? -37.146 34.626 -19.646 1.00 90.46  ? 336 ALA A CB  1 
ATOM   2698 N  N   . GLY A 1 337 ? -36.803 34.628 -16.599 1.00 90.75  ? 337 GLY A N   1 
ATOM   2699 C  CA  . GLY A 1 337 ? -36.559 35.388 -15.378 1.00 88.09  ? 337 GLY A CA  1 
ATOM   2700 C  C   . GLY A 1 337 ? -35.623 36.539 -15.664 1.00 82.85  ? 337 GLY A C   1 
ATOM   2701 O  O   . GLY A 1 337 ? -34.630 36.383 -16.385 1.00 80.82  ? 337 GLY A O   1 
ATOM   2702 N  N   . ALA A 1 338 ? -35.930 37.707 -15.096 1.00 83.15  ? 338 ALA A N   1 
ATOM   2703 C  CA  . ALA A 1 338 ? -35.203 38.924 -15.415 1.00 81.47  ? 338 ALA A CA  1 
ATOM   2704 C  C   . ALA A 1 338 ? -34.863 39.696 -14.149 1.00 84.51  ? 338 ALA A C   1 
ATOM   2705 O  O   . ALA A 1 338 ? -35.590 39.644 -13.153 1.00 84.30  ? 338 ALA A O   1 
ATOM   2706 C  CB  . ALA A 1 338 ? -36.005 39.823 -16.365 1.00 86.23  ? 338 ALA A CB  1 
ATOM   2707 N  N   . ILE A 1 339 ? -33.744 40.414 -14.204 1.00 79.69  ? 339 ILE A N   1 
ATOM   2708 C  CA  . ILE A 1 339 ? -33.348 41.360 -13.167 1.00 79.09  ? 339 ILE A CA  1 
ATOM   2709 C  C   . ILE A 1 339 ? -33.732 42.755 -13.640 1.00 76.08  ? 339 ILE A C   1 
ATOM   2710 O  O   . ILE A 1 339 ? -33.217 43.238 -14.655 1.00 75.74  ? 339 ILE A O   1 
ATOM   2711 C  CB  . ILE A 1 339 ? -31.842 41.281 -12.869 1.00 77.18  ? 339 ILE A CB  1 
ATOM   2712 C  CG1 . ILE A 1 339 ? -31.438 39.857 -12.490 1.00 77.54  ? 339 ILE A CG1 1 
ATOM   2713 C  CG2 . ILE A 1 339 ? -31.471 42.248 -11.753 1.00 76.48  ? 339 ILE A CG2 1 
ATOM   2714 C  CD1 . ILE A 1 339 ? -29.938 39.639 -12.447 1.00 76.99  ? 339 ILE A CD1 1 
ATOM   2715 N  N   . TYR A 1 340 ? -34.634 43.405 -12.909 1.00 78.36  ? 340 TYR A N   1 
ATOM   2716 C  CA  . TYR A 1 340 ? -35.111 44.739 -13.254 1.00 76.80  ? 340 TYR A CA  1 
ATOM   2717 C  C   . TYR A 1 340 ? -34.367 45.763 -12.402 1.00 77.85  ? 340 TYR A C   1 
ATOM   2718 O  O   . TYR A 1 340 ? -34.609 45.870 -11.196 1.00 77.37  ? 340 TYR A O   1 
ATOM   2719 C  CB  . TYR A 1 340 ? -36.621 44.847 -13.049 1.00 78.93  ? 340 TYR A CB  1 
ATOM   2720 C  CG  . TYR A 1 340 ? -37.443 43.903 -13.905 1.00 81.54  ? 340 TYR A CG  1 
ATOM   2721 C  CD1 . TYR A 1 340 ? -37.824 44.252 -15.196 1.00 80.11  ? 340 TYR A CD1 1 
ATOM   2722 C  CD2 . TYR A 1 340 ? -37.849 42.667 -13.416 1.00 82.72  ? 340 TYR A CD2 1 
ATOM   2723 C  CE1 . TYR A 1 340 ? -38.577 43.393 -15.976 1.00 84.90  ? 340 TYR A CE1 1 
ATOM   2724 C  CE2 . TYR A 1 340 ? -38.603 41.803 -14.189 1.00 83.64  ? 340 TYR A CE2 1 
ATOM   2725 C  CZ  . TYR A 1 340 ? -38.964 42.171 -15.468 1.00 87.24  ? 340 TYR A CZ  1 
ATOM   2726 O  OH  . TYR A 1 340 ? -39.716 41.319 -16.246 1.00 89.74  ? 340 TYR A OH  1 
ATOM   2727 N  N   . HIS A 1 341 ? -33.460 46.510 -13.032 1.00 72.00  ? 341 HIS A N   1 
ATOM   2728 C  CA  . HIS A 1 341 ? -32.757 47.617 -12.385 1.00 72.80  ? 341 HIS A CA  1 
ATOM   2729 C  C   . HIS A 1 341 ? -33.640 48.868 -12.392 1.00 69.48  ? 341 HIS A C   1 
ATOM   2730 O  O   . HIS A 1 341 ? -33.252 49.954 -12.824 1.00 72.79  ? 341 HIS A O   1 
ATOM   2731 C  CB  . HIS A 1 341 ? -31.427 47.872 -13.084 1.00 70.03  ? 341 HIS A CB  1 
ATOM   2732 C  CG  . HIS A 1 341 ? -30.402 46.807 -12.852 1.00 74.77  ? 341 HIS A CG  1 
ATOM   2733 N  ND1 . HIS A 1 341 ? -29.616 46.769 -11.720 1.00 74.18  ? 341 HIS A ND1 1 
ATOM   2734 C  CD2 . HIS A 1 341 ? -30.036 45.739 -13.601 1.00 74.63  ? 341 HIS A CD2 1 
ATOM   2735 C  CE1 . HIS A 1 341 ? -28.808 45.726 -11.784 1.00 72.55  ? 341 HIS A CE1 1 
ATOM   2736 N  NE2 . HIS A 1 341 ? -29.042 45.085 -12.915 1.00 73.64  ? 341 HIS A NE2 1 
ATOM   2737 N  N   . ASN A 1 342 ? -34.855 48.689 -11.882 1.00 69.97  ? 342 ASN A N   1 
ATOM   2738 C  CA  . ASN A 1 342 ? -35.905 49.696 -11.926 1.00 70.95  ? 342 ASN A CA  1 
ATOM   2739 C  C   . ASN A 1 342 ? -35.889 50.632 -10.722 1.00 73.55  ? 342 ASN A C   1 
ATOM   2740 O  O   . ASN A 1 342 ? -36.795 51.461 -10.589 1.00 72.07  ? 342 ASN A O   1 
ATOM   2741 C  CB  . ASN A 1 342 ? -37.277 49.017 -12.033 1.00 70.74  ? 342 ASN A CB  1 
ATOM   2742 C  CG  . ASN A 1 342 ? -37.586 48.122 -10.844 1.00 74.81  ? 342 ASN A CG  1 
ATOM   2743 O  OD1 . ASN A 1 342 ? -36.689 47.523 -10.247 1.00 73.23  ? 342 ASN A OD1 1 
ATOM   2744 N  ND2 . ASN A 1 342 ? -38.864 48.023 -10.498 1.00 74.45  ? 342 ASN A ND2 1 
ATOM   2745 N  N   . MET A 1 343 ? -34.885 50.534 -9.856  1.00 73.76  ? 343 MET A N   1 
ATOM   2746 C  CA  . MET A 1 343 ? -34.809 51.356 -8.658  1.00 69.80  ? 343 MET A CA  1 
ATOM   2747 C  C   . MET A 1 343 ? -33.545 52.206 -8.672  1.00 73.15  ? 343 MET A C   1 
ATOM   2748 O  O   . MET A 1 343 ? -32.518 51.819 -9.238  1.00 72.92  ? 343 MET A O   1 
ATOM   2749 C  CB  . MET A 1 343 ? -34.847 50.489 -7.393  1.00 70.69  ? 343 MET A CB  1 
ATOM   2750 C  CG  . MET A 1 343 ? -36.233 49.944 -7.074  1.00 72.18  ? 343 MET A CG  1 
ATOM   2751 S  SD  . MET A 1 343 ? -36.267 48.827 -5.660  1.00 71.23  ? 343 MET A SD  1 
ATOM   2752 C  CE  . MET A 1 343 ? -35.508 47.365 -6.361  1.00 70.31  ? 343 MET A CE  1 
ATOM   2753 N  N   . ASP A 1 344 ? -33.639 53.375 -8.043  1.00 76.57  ? 344 ASP A N   1 
ATOM   2754 C  CA  . ASP A 1 344 ? -32.523 54.301 -7.939  1.00 75.76  ? 344 ASP A CA  1 
ATOM   2755 C  C   . ASP A 1 344 ? -31.771 54.067 -6.636  1.00 72.52  ? 344 ASP A C   1 
ATOM   2756 O  O   . ASP A 1 344 ? -32.381 53.880 -5.578  1.00 75.45  ? 344 ASP A O   1 
ATOM   2757 C  CB  . ASP A 1 344 ? -33.020 55.747 -8.015  1.00 73.93  ? 344 ASP A CB  1 
ATOM   2758 C  CG  . ASP A 1 344 ? -31.895 56.761 -7.915  1.00 78.62  ? 344 ASP A CG  1 
ATOM   2759 O  OD1 . ASP A 1 344 ? -30.942 56.681 -8.718  1.00 79.94  ? 344 ASP A OD1 1 
ATOM   2760 O  OD2 . ASP A 1 344 ? -31.971 57.647 -7.039  1.00 74.51  ? 344 ASP A OD2 1 
ATOM   2761 N  N   . GLU A 1 345 ? -30.438 54.078 -6.722  1.00 71.40  ? 345 GLU A N   1 
ATOM   2762 C  CA  . GLU A 1 345 ? -29.614 53.795 -5.549  1.00 73.27  ? 345 GLU A CA  1 
ATOM   2763 C  C   . GLU A 1 345 ? -29.834 54.829 -4.452  1.00 71.67  ? 345 GLU A C   1 
ATOM   2764 O  O   . GLU A 1 345 ? -29.815 54.495 -3.262  1.00 72.11  ? 345 GLU A O   1 
ATOM   2765 C  CB  . GLU A 1 345 ? -28.138 53.739 -5.948  1.00 72.10  ? 345 GLU A CB  1 
ATOM   2766 C  CG  . GLU A 1 345 ? -27.172 53.539 -4.786  1.00 72.79  ? 345 GLU A CG  1 
ATOM   2767 C  CD  . GLU A 1 345 ? -27.223 52.137 -4.205  1.00 73.53  ? 345 GLU A CD  1 
ATOM   2768 O  OE1 . GLU A 1 345 ? -27.825 51.245 -4.837  1.00 70.79  ? 345 GLU A OE1 1 
ATOM   2769 O  OE2 . GLU A 1 345 ? -26.655 51.927 -3.112  1.00 70.33  ? 345 GLU A OE2 1 
ATOM   2770 N  N   . GLN A 1 346 ? -30.045 56.093 -4.832  1.00 71.00  ? 346 GLN A N   1 
ATOM   2771 C  CA  . GLN A 1 346 ? -30.310 57.125 -3.836  1.00 71.13  ? 346 GLN A CA  1 
ATOM   2772 C  C   . GLN A 1 346 ? -31.641 56.896 -3.133  1.00 73.03  ? 346 GLN A C   1 
ATOM   2773 O  O   . GLN A 1 346 ? -31.771 57.204 -1.942  1.00 74.82  ? 346 GLN A O   1 
ATOM   2774 C  CB  . GLN A 1 346 ? -30.283 58.508 -4.488  1.00 75.12  ? 346 GLN A CB  1 
ATOM   2775 C  CG  . GLN A 1 346 ? -28.980 58.829 -5.200  1.00 80.96  ? 346 GLN A CG  1 
ATOM   2776 C  CD  . GLN A 1 346 ? -27.786 58.798 -4.268  1.00 84.70  ? 346 GLN A CD  1 
ATOM   2777 O  OE1 . GLN A 1 346 ? -27.843 59.310 -3.149  1.00 83.92  ? 346 GLN A OE1 1 
ATOM   2778 N  NE2 . GLN A 1 346 ? -26.698 58.189 -4.722  1.00 86.49  ? 346 GLN A NE2 1 
ATOM   2779 N  N   . ASP A 1 347 ? -32.635 56.361 -3.847  1.00 72.25  ? 347 ASP A N   1 
ATOM   2780 C  CA  . ASP A 1 347 ? -33.906 56.029 -3.213  1.00 69.42  ? 347 ASP A CA  1 
ATOM   2781 C  C   . ASP A 1 347 ? -33.732 54.946 -2.159  1.00 67.74  ? 347 ASP A C   1 
ATOM   2782 O  O   . ASP A 1 347 ? -34.301 55.035 -1.066  1.00 63.89  ? 347 ASP A O   1 
ATOM   2783 C  CB  . ASP A 1 347 ? -34.921 55.587 -4.265  1.00 69.73  ? 347 ASP A CB  1 
ATOM   2784 C  CG  . ASP A 1 347 ? -35.511 56.749 -5.026  1.00 73.29  ? 347 ASP A CG  1 
ATOM   2785 O  OD1 . ASP A 1 347 ? -35.602 57.850 -4.446  1.00 73.18  ? 347 ASP A OD1 1 
ATOM   2786 O  OD2 . ASP A 1 347 ? -35.883 56.562 -6.203  1.00 76.27  ? 347 ASP A OD2 1 
ATOM   2787 N  N   . VAL A 1 348 ? -32.954 53.909 -2.473  1.00 70.25  ? 348 VAL A N   1 
ATOM   2788 C  CA  . VAL A 1 348 ? -32.708 52.849 -1.500  1.00 73.43  ? 348 VAL A CA  1 
ATOM   2789 C  C   . VAL A 1 348 ? -32.051 53.419 -0.247  1.00 70.90  ? 348 VAL A C   1 
ATOM   2790 O  O   . VAL A 1 348 ? -32.492 53.151 0.878   1.00 68.02  ? 348 VAL A O   1 
ATOM   2791 C  CB  . VAL A 1 348 ? -31.858 51.733 -2.135  1.00 66.80  ? 348 VAL A CB  1 
ATOM   2792 C  CG1 . VAL A 1 348 ? -31.581 50.635 -1.121  1.00 66.54  ? 348 VAL A CG1 1 
ATOM   2793 C  CG2 . VAL A 1 348 ? -32.562 51.163 -3.358  1.00 66.96  ? 348 VAL A CG2 1 
ATOM   2794 N  N   . ARG A 1 349 ? -31.015 54.245 -0.425  1.00 66.12  ? 349 ARG A N   1 
ATOM   2795 C  CA  . ARG A 1 349 ? -30.279 54.782 0.717   1.00 65.62  ? 349 ARG A CA  1 
ATOM   2796 C  C   . ARG A 1 349 ? -31.169 55.636 1.613   1.00 66.80  ? 349 ARG A C   1 
ATOM   2797 O  O   . ARG A 1 349 ? -31.050 55.586 2.843   1.00 70.81  ? 349 ARG A O   1 
ATOM   2798 C  CB  . ARG A 1 349 ? -29.075 55.586 0.228   1.00 69.29  ? 349 ARG A CB  1 
ATOM   2799 C  CG  . ARG A 1 349 ? -27.966 54.735 -0.375  1.00 70.60  ? 349 ARG A CG  1 
ATOM   2800 C  CD  . ARG A 1 349 ? -27.005 55.569 -1.205  1.00 73.30  ? 349 ARG A CD  1 
ATOM   2801 N  NE  . ARG A 1 349 ? -25.917 54.762 -1.745  1.00 75.25  ? 349 ARG A NE  1 
ATOM   2802 C  CZ  . ARG A 1 349 ? -24.669 54.788 -1.296  1.00 76.01  ? 349 ARG A CZ  1 
ATOM   2803 N  NH1 . ARG A 1 349 ? -24.304 55.598 -0.316  1.00 75.21  ? 349 ARG A NH1 1 
ATOM   2804 N  NH2 . ARG A 1 349 ? -23.764 53.987 -1.850  1.00 78.91  ? 349 ARG A NH2 1 
ATOM   2805 N  N   . ARG A 1 350 ? -32.066 56.431 1.019   1.00 65.59  ? 350 ARG A N   1 
ATOM   2806 C  CA  . ARG A 1 350 ? -32.966 57.251 1.825   1.00 68.75  ? 350 ARG A CA  1 
ATOM   2807 C  C   . ARG A 1 350 ? -33.903 56.388 2.660   1.00 63.91  ? 350 ARG A C   1 
ATOM   2808 O  O   . ARG A 1 350 ? -34.133 56.671 3.841   1.00 62.42  ? 350 ARG A O   1 
ATOM   2809 C  CB  . ARG A 1 350 ? -33.774 58.194 0.935   1.00 65.61  ? 350 ARG A CB  1 
ATOM   2810 C  CG  . ARG A 1 350 ? -32.968 59.289 0.267   1.00 69.20  ? 350 ARG A CG  1 
ATOM   2811 C  CD  . ARG A 1 350 ? -33.885 60.331 -0.353  1.00 71.66  ? 350 ARG A CD  1 
ATOM   2812 N  NE  . ARG A 1 350 ? -33.195 61.135 -1.354  1.00 74.91  ? 350 ARG A NE  1 
ATOM   2813 C  CZ  . ARG A 1 350 ? -33.128 60.825 -2.641  1.00 76.44  ? 350 ARG A CZ  1 
ATOM   2814 N  NH1 . ARG A 1 350 ? -33.709 59.737 -3.120  1.00 75.92  ? 350 ARG A NH1 1 
ATOM   2815 N  NH2 . ARG A 1 350 ? -32.462 61.626 -3.468  1.00 76.14  ? 350 ARG A NH2 1 
ATOM   2816 N  N   . VAL A 1 351 ? -34.466 55.338 2.057   1.00 64.40  ? 351 VAL A N   1 
ATOM   2817 C  CA  . VAL A 1 351 ? -35.348 54.441 2.797   1.00 66.79  ? 351 VAL A CA  1 
ATOM   2818 C  C   . VAL A 1 351 ? -34.576 53.734 3.900   1.00 65.51  ? 351 VAL A C   1 
ATOM   2819 O  O   . VAL A 1 351 ? -35.084 53.539 5.011   1.00 64.74  ? 351 VAL A O   1 
ATOM   2820 C  CB  . VAL A 1 351 ? -36.015 53.436 1.838   1.00 63.11  ? 351 VAL A CB  1 
ATOM   2821 C  CG1 . VAL A 1 351 ? -36.913 52.480 2.605   1.00 60.86  ? 351 VAL A CG1 1 
ATOM   2822 C  CG2 . VAL A 1 351 ? -36.805 54.168 0.766   1.00 61.97  ? 351 VAL A CG2 1 
ATOM   2823 N  N   . MET A 1 352 ? -33.329 53.356 3.618   1.00 64.05  ? 352 MET A N   1 
ATOM   2824 C  CA  . MET A 1 352 ? -32.529 52.645 4.608   1.00 62.12  ? 352 MET A CA  1 
ATOM   2825 C  C   . MET A 1 352 ? -32.154 53.549 5.776   1.00 61.08  ? 352 MET A C   1 
ATOM   2826 O  O   . MET A 1 352 ? -32.166 53.112 6.932   1.00 62.46  ? 352 MET A O   1 
ATOM   2827 C  CB  . MET A 1 352 ? -31.283 52.066 3.944   1.00 59.78  ? 352 MET A CB  1 
ATOM   2828 C  CG  . MET A 1 352 ? -31.571 50.891 3.027   1.00 65.97  ? 352 MET A CG  1 
ATOM   2829 S  SD  . MET A 1 352 ? -30.033 50.090 2.536   1.00 63.02  ? 352 MET A SD  1 
ATOM   2830 C  CE  . MET A 1 352 ? -29.331 49.740 4.146   1.00 60.74  ? 352 MET A CE  1 
ATOM   2831 N  N   . ARG A 1 353 ? -31.834 54.813 5.498   1.00 62.69  ? 353 ARG A N   1 
ATOM   2832 C  CA  A ARG A 1 353 ? -31.488 55.753 6.557   0.55 63.13  ? 353 ARG A CA  1 
ATOM   2833 C  CA  B ARG A 1 353 ? -31.489 55.758 6.553   0.45 62.75  ? 353 ARG A CA  1 
ATOM   2834 C  C   . ARG A 1 353 ? -32.697 56.215 7.360   1.00 63.10  ? 353 ARG A C   1 
ATOM   2835 O  O   . ARG A 1 353 ? -32.516 56.875 8.389   1.00 63.80  ? 353 ARG A O   1 
ATOM   2836 C  CB  A ARG A 1 353 ? -30.762 56.965 5.967   0.55 65.58  ? 353 ARG A CB  1 
ATOM   2837 C  CB  B ARG A 1 353 ? -30.783 56.977 5.958   0.45 65.58  ? 353 ARG A CB  1 
ATOM   2838 C  CG  A ARG A 1 353 ? -29.317 56.687 5.585   0.55 64.38  ? 353 ARG A CG  1 
ATOM   2839 C  CG  B ARG A 1 353 ? -29.372 56.703 5.475   0.45 64.38  ? 353 ARG A CG  1 
ATOM   2840 C  CD  A ARG A 1 353 ? -28.608 57.940 5.089   0.55 66.51  ? 353 ARG A CD  1 
ATOM   2841 C  CD  B ARG A 1 353 ? -28.724 57.973 4.954   0.45 66.39  ? 353 ARG A CD  1 
ATOM   2842 N  NE  A ARG A 1 353 ? -28.992 58.296 3.728   0.55 68.05  ? 353 ARG A NE  1 
ATOM   2843 N  NE  B ARG A 1 353 ? -28.810 59.062 5.920   0.45 67.98  ? 353 ARG A NE  1 
ATOM   2844 C  CZ  A ARG A 1 353 ? -29.899 59.212 3.415   0.55 67.44  ? 353 ARG A CZ  1 
ATOM   2845 C  CZ  B ARG A 1 353 ? -27.894 59.319 6.844   0.45 68.65  ? 353 ARG A CZ  1 
ATOM   2846 N  NH1 A ARG A 1 353 ? -30.545 59.892 4.348   0.55 66.41  ? 353 ARG A NH1 1 
ATOM   2847 N  NH1 B ARG A 1 353 ? -26.802 58.582 6.958   0.45 68.18  ? 353 ARG A NH1 1 
ATOM   2848 N  NH2 A ARG A 1 353 ? -30.162 59.453 2.134   0.55 67.37  ? 353 ARG A NH2 1 
ATOM   2849 N  NH2 B ARG A 1 353 ? -28.079 60.341 7.674   0.45 67.75  ? 353 ARG A NH2 1 
ATOM   2850 N  N   . TYR A 1 354 ? -33.910 55.887 6.925   1.00 64.65  ? 354 TYR A N   1 
ATOM   2851 C  CA  . TYR A 1 354 ? -35.094 56.288 7.669   1.00 61.72  ? 354 TYR A CA  1 
ATOM   2852 C  C   . TYR A 1 354 ? -35.132 55.559 9.012   1.00 60.66  ? 354 TYR A C   1 
ATOM   2853 O  O   . TYR A 1 354 ? -34.858 54.356 9.072   1.00 57.65  ? 354 TYR A O   1 
ATOM   2854 C  CB  . TYR A 1 354 ? -36.360 55.996 6.864   1.00 62.65  ? 354 TYR A CB  1 
ATOM   2855 C  CG  . TYR A 1 354 ? -37.556 56.810 7.298   1.00 64.72  ? 354 TYR A CG  1 
ATOM   2856 C  CD1 . TYR A 1 354 ? -37.562 58.192 7.164   1.00 64.97  ? 354 TYR A CD1 1 
ATOM   2857 C  CD2 . TYR A 1 354 ? -38.681 56.199 7.835   1.00 63.91  ? 354 TYR A CD2 1 
ATOM   2858 C  CE1 . TYR A 1 354 ? -38.650 58.943 7.560   1.00 63.96  ? 354 TYR A CE1 1 
ATOM   2859 C  CE2 . TYR A 1 354 ? -39.776 56.944 8.232   1.00 66.46  ? 354 TYR A CE2 1 
ATOM   2860 C  CZ  . TYR A 1 354 ? -39.754 58.315 8.092   1.00 66.74  ? 354 TYR A CZ  1 
ATOM   2861 O  OH  . TYR A 1 354 ? -40.840 59.061 8.487   1.00 69.29  ? 354 TYR A OH  1 
ATOM   2862 N  N   . PRO A 1 355 ? -35.461 56.259 10.102  1.00 60.23  ? 355 PRO A N   1 
ATOM   2863 C  CA  . PRO A 1 355 ? -35.276 55.663 11.439  1.00 61.45  ? 355 PRO A CA  1 
ATOM   2864 C  C   . PRO A 1 355 ? -36.098 54.411 11.700  1.00 62.76  ? 355 PRO A C   1 
ATOM   2865 O  O   . PRO A 1 355 ? -35.610 53.496 12.371  1.00 61.54  ? 355 PRO A O   1 
ATOM   2866 C  CB  . PRO A 1 355 ? -35.674 56.809 12.381  1.00 62.52  ? 355 PRO A CB  1 
ATOM   2867 C  CG  . PRO A 1 355 ? -35.463 58.050 11.580  1.00 60.65  ? 355 PRO A CG  1 
ATOM   2868 C  CD  . PRO A 1 355 ? -35.835 57.681 10.178  1.00 58.97  ? 355 PRO A CD  1 
ATOM   2869 N  N   . VAL A 1 356 ? -37.329 54.339 11.201  1.00 62.09  ? 356 VAL A N   1 
ATOM   2870 C  CA  . VAL A 1 356 ? -38.215 53.229 11.543  1.00 60.52  ? 356 VAL A CA  1 
ATOM   2871 C  C   . VAL A 1 356 ? -38.197 52.166 10.454  1.00 60.77  ? 356 VAL A C   1 
ATOM   2872 O  O   . VAL A 1 356 ? -39.127 51.359 10.346  1.00 60.47  ? 356 VAL A O   1 
ATOM   2873 C  CB  . VAL A 1 356 ? -39.652 53.720 11.801  1.00 63.42  ? 356 VAL A CB  1 
ATOM   2874 C  CG1 . VAL A 1 356 ? -39.687 54.663 12.991  1.00 68.73  ? 356 VAL A CG1 1 
ATOM   2875 C  CG2 . VAL A 1 356 ? -40.207 54.394 10.559  1.00 64.31  ? 356 VAL A CG2 1 
ATOM   2876 N  N   . THR A 1 357 ? -37.144 52.155 9.646   1.00 60.93  ? 357 THR A N   1 
ATOM   2877 C  CA  . THR A 1 357 ? -37.027 51.201 8.553   1.00 57.65  ? 357 THR A CA  1 
ATOM   2878 C  C   . THR A 1 357 ? -36.292 49.952 9.020   1.00 55.97  ? 357 THR A C   1 
ATOM   2879 O  O   . THR A 1 357 ? -35.188 50.040 9.564   1.00 55.13  ? 357 THR A O   1 
ATOM   2880 C  CB  . THR A 1 357 ? -36.300 51.821 7.361   1.00 57.58  ? 357 THR A CB  1 
ATOM   2881 O  OG1 . THR A 1 357 ? -37.130 52.828 6.768   1.00 58.46  ? 357 THR A OG1 1 
ATOM   2882 C  CG2 . THR A 1 357 ? -35.974 50.759 6.326   1.00 58.46  ? 357 THR A CG2 1 
ATOM   2883 N  N   . MET A 1 358 ? -36.907 48.795 8.802   1.00 54.77  ? 358 MET A N   1 
ATOM   2884 C  CA  . MET A 1 358 ? -36.320 47.509 9.139   1.00 54.83  ? 358 MET A CA  1 
ATOM   2885 C  C   . MET A 1 358 ? -35.713 46.870 7.894   1.00 54.45  ? 358 MET A C   1 
ATOM   2886 O  O   . MET A 1 358 ? -35.948 47.300 6.762   1.00 55.13  ? 358 MET A O   1 
ATOM   2887 C  CB  . MET A 1 358 ? -37.377 46.593 9.763   1.00 53.27  ? 358 MET A CB  1 
ATOM   2888 C  CG  . MET A 1 358 ? -37.996 47.150 11.037  1.00 53.95  ? 358 MET A CG  1 
ATOM   2889 S  SD  . MET A 1 358 ? -39.344 46.144 11.687  1.00 57.94  ? 358 MET A SD  1 
ATOM   2890 C  CE  . MET A 1 358 ? -40.657 46.518 10.529  1.00 55.79  ? 358 MET A CE  1 
ATOM   2891 N  N   . ILE A 1 359 ? -34.912 45.832 8.115   1.00 52.47  ? 359 ILE A N   1 
ATOM   2892 C  CA  . ILE A 1 359 ? -34.242 45.118 7.036   1.00 51.59  ? 359 ILE A CA  1 
ATOM   2893 C  C   . ILE A 1 359 ? -35.020 43.842 6.746   1.00 54.47  ? 359 ILE A C   1 
ATOM   2894 O  O   . ILE A 1 359 ? -35.157 42.974 7.617   1.00 56.28  ? 359 ILE A O   1 
ATOM   2895 C  CB  . ILE A 1 359 ? -32.780 44.804 7.386   1.00 53.26  ? 359 ILE A CB  1 
ATOM   2896 C  CG1 . ILE A 1 359 ? -32.038 46.083 7.777   1.00 53.05  ? 359 ILE A CG1 1 
ATOM   2897 C  CG2 . ILE A 1 359 ? -32.087 44.139 6.207   1.00 52.47  ? 359 ILE A CG2 1 
ATOM   2898 C  CD1 . ILE A 1 359 ? -31.953 47.105 6.663   1.00 54.05  ? 359 ILE A CD1 1 
ATOM   2899 N  N   . GLY A 1 360 ? -35.534 43.733 5.524   1.00 56.69  ? 360 GLY A N   1 
ATOM   2900 C  CA  . GLY A 1 360 ? -36.209 42.530 5.080   1.00 56.56  ? 360 GLY A CA  1 
ATOM   2901 C  C   . GLY A 1 360 ? -35.613 42.012 3.790   1.00 57.11  ? 360 GLY A C   1 
ATOM   2902 O  O   . GLY A 1 360 ? -35.562 42.736 2.792   1.00 61.85  ? 360 GLY A O   1 
ATOM   2903 N  N   . SER A 1 361 ? -35.149 40.760 3.795   1.00 62.62  ? 361 SER A N   1 
ATOM   2904 C  CA  . SER A 1 361 ? -34.496 40.218 2.608   1.00 63.04  ? 361 SER A CA  1 
ATOM   2905 C  C   . SER A 1 361 ? -35.470 40.095 1.444   1.00 67.59  ? 361 SER A C   1 
ATOM   2906 O  O   . SER A 1 361 ? -35.127 40.436 0.307   1.00 72.26  ? 361 SER A O   1 
ATOM   2907 C  CB  . SER A 1 361 ? -33.866 38.860 2.923   1.00 63.26  ? 361 SER A CB  1 
ATOM   2908 O  OG  . SER A 1 361 ? -34.857 37.878 3.171   1.00 65.24  ? 361 SER A OG  1 
ATOM   2909 N  N   . ASP A 1 362 ? -36.692 39.634 1.713   1.00 64.07  ? 362 ASP A N   1 
ATOM   2910 C  CA  . ASP A 1 362 ? -37.669 39.322 0.671   1.00 71.10  ? 362 ASP A CA  1 
ATOM   2911 C  C   . ASP A 1 362 ? -37.061 38.358 -0.345  1.00 71.92  ? 362 ASP A C   1 
ATOM   2912 O  O   . ASP A 1 362 ? -37.137 38.552 -1.561  1.00 71.06  ? 362 ASP A O   1 
ATOM   2913 C  CB  . ASP A 1 362 ? -38.190 40.594 -0.004  1.00 72.74  ? 362 ASP A CB  1 
ATOM   2914 C  CG  . ASP A 1 362 ? -39.416 40.340 -0.863  1.00 74.08  ? 362 ASP A CG  1 
ATOM   2915 O  OD1 . ASP A 1 362 ? -39.908 39.192 -0.878  1.00 74.61  ? 362 ASP A OD1 1 
ATOM   2916 O  OD2 . ASP A 1 362 ? -39.885 41.289 -1.525  1.00 75.26  ? 362 ASP A OD2 1 
ATOM   2917 N  N   . GLY A 1 363 ? -36.429 37.310 0.178   1.00 70.57  ? 363 GLY A N   1 
ATOM   2918 C  CA  . GLY A 1 363 ? -35.796 36.329 -0.673  1.00 68.46  ? 363 GLY A CA  1 
ATOM   2919 C  C   . GLY A 1 363 ? -36.786 35.314 -1.212  1.00 75.44  ? 363 GLY A C   1 
ATOM   2920 O  O   . GLY A 1 363 ? -37.772 34.959 -0.567  1.00 78.26  ? 363 GLY A O   1 
ATOM   2921 N  N   . LEU A 1 364 ? -36.507 34.844 -2.425  1.00 80.15  ? 364 LEU A N   1 
ATOM   2922 C  CA  . LEU A 1 364 ? -37.363 33.886 -3.116  1.00 80.31  ? 364 LEU A CA  1 
ATOM   2923 C  C   . LEU A 1 364 ? -36.620 32.561 -3.230  1.00 84.18  ? 364 LEU A C   1 
ATOM   2924 O  O   . LEU A 1 364 ? -35.828 32.372 -4.167  1.00 84.69  ? 364 LEU A O   1 
ATOM   2925 C  CB  . LEU A 1 364 ? -37.753 34.410 -4.503  1.00 81.50  ? 364 LEU A CB  1 
ATOM   2926 C  CG  . LEU A 1 364 ? -38.816 35.508 -4.686  1.00 79.27  ? 364 LEU A CG  1 
ATOM   2927 C  CD1 . LEU A 1 364 ? -40.207 35.013 -4.299  1.00 78.52  ? 364 LEU A CD1 1 
ATOM   2928 C  CD2 . LEU A 1 364 ? -38.478 36.805 -3.949  1.00 76.11  ? 364 LEU A CD2 1 
ATOM   2929 N  N   . PRO A 1 365 ? -36.834 31.614 -2.310  1.00 84.80  ? 365 PRO A N   1 
ATOM   2930 C  CA  . PRO A 1 365 ? -36.007 30.397 -2.290  1.00 86.20  ? 365 PRO A CA  1 
ATOM   2931 C  C   . PRO A 1 365 ? -36.264 29.463 -3.463  1.00 88.86  ? 365 PRO A C   1 
ATOM   2932 O  O   . PRO A 1 365 ? -35.319 28.994 -4.105  1.00 85.55  ? 365 PRO A O   1 
ATOM   2933 C  CB  . PRO A 1 365 ? -36.392 29.740 -0.958  1.00 82.87  ? 365 PRO A CB  1 
ATOM   2934 C  CG  . PRO A 1 365 ? -37.775 30.236 -0.683  1.00 83.81  ? 365 PRO A CG  1 
ATOM   2935 C  CD  . PRO A 1 365 ? -37.824 31.636 -1.219  1.00 81.67  ? 365 PRO A CD  1 
ATOM   2936 N  N   . ASN A 1 366 ? -37.537 29.180 -3.751  1.00 88.33  ? 366 ASN A N   1 
ATOM   2937 C  CA  . ASN A 1 366 ? -37.870 28.276 -4.845  1.00 92.26  ? 366 ASN A CA  1 
ATOM   2938 C  C   . ASN A 1 366 ? -37.513 28.857 -6.207  1.00 93.28  ? 366 ASN A C   1 
ATOM   2939 O  O   . ASN A 1 366 ? -37.443 28.107 -7.187  1.00 93.22  ? 366 ASN A O   1 
ATOM   2940 C  CB  . ASN A 1 366 ? -39.358 27.927 -4.805  1.00 89.84  ? 366 ASN A CB  1 
ATOM   2941 C  CG  . ASN A 1 366 ? -39.781 27.322 -3.481  1.00 86.60  ? 366 ASN A CG  1 
ATOM   2942 O  OD1 . ASN A 1 366 ? -39.099 26.454 -2.934  1.00 87.69  ? 366 ASN A OD1 1 
ATOM   2943 N  ND2 . ASN A 1 366 ? -40.909 27.784 -2.954  1.00 84.15  ? 366 ASN A ND2 1 
ATOM   2944 N  N   . ASP A 1 367 ? -37.288 30.162 -6.286  1.00 98.13  ? 367 ASP A N   1 
ATOM   2945 C  CA  . ASP A 1 367 ? -36.958 30.829 -7.537  1.00 92.88  ? 367 ASP A CA  1 
ATOM   2946 C  C   . ASP A 1 367 ? -35.660 30.269 -8.110  1.00 91.83  ? 367 ASP A C   1 
ATOM   2947 O  O   . ASP A 1 367 ? -34.605 30.400 -7.472  1.00 97.27  ? 367 ASP A O   1 
ATOM   2948 C  CB  . ASP A 1 367 ? -36.830 32.334 -7.290  1.00 90.84  ? 367 ASP A CB  1 
ATOM   2949 C  CG  . ASP A 1 367 ? -36.787 33.148 -8.572  1.00 92.47  ? 367 ASP A CG  1 
ATOM   2950 O  OD1 . ASP A 1 367 ? -35.940 32.865 -9.443  1.00 94.08  ? 367 ASP A OD1 1 
ATOM   2951 O  OD2 . ASP A 1 367 ? -37.603 34.084 -8.705  1.00 94.85  ? 367 ASP A OD2 1 
ATOM   2952 N  N   . PRO A 1 368 ? -35.685 29.638 -9.285  1.00 95.29  ? 368 PRO A N   1 
ATOM   2953 C  CA  . PRO A 1 368 ? -34.425 29.214 -9.912  1.00 94.38  ? 368 PRO A CA  1 
ATOM   2954 C  C   . PRO A 1 368 ? -33.621 30.436 -10.335 1.00 94.96  ? 368 PRO A C   1 
ATOM   2955 O  O   . PRO A 1 368 ? -34.159 31.366 -10.940 1.00 108.49 ? 368 PRO A O   1 
ATOM   2956 C  CB  . PRO A 1 368 ? -34.886 28.388 -11.118 1.00 97.96  ? 368 PRO A CB  1 
ATOM   2957 C  CG  . PRO A 1 368 ? -36.244 28.940 -11.446 1.00 96.80  ? 368 PRO A CG  1 
ATOM   2958 C  CD  . PRO A 1 368 ? -36.856 29.332 -10.125 1.00 97.87  ? 368 PRO A CD  1 
ATOM   2959 N  N   . MET A 1 369 ? -32.322 30.432 -10.006 1.00 88.81  ? 369 MET A N   1 
ATOM   2960 C  CA  . MET A 1 369 ? -31.470 31.615 -10.121 1.00 87.78  ? 369 MET A CA  1 
ATOM   2961 C  C   . MET A 1 369 ? -32.089 32.746 -9.306  1.00 85.22  ? 369 MET A C   1 
ATOM   2962 O  O   . MET A 1 369 ? -32.702 33.662 -9.872  1.00 83.70  ? 369 MET A O   1 
ATOM   2963 C  CB  . MET A 1 369 ? -31.288 32.054 -11.578 1.00 86.23  ? 369 MET A CB  1 
ATOM   2964 C  CG  . MET A 1 369 ? -30.110 31.430 -12.318 1.00 89.28  ? 369 MET A CG  1 
ATOM   2965 S  SD  . MET A 1 369 ? -28.475 31.804 -11.631 1.00 98.75  ? 369 MET A SD  1 
ATOM   2966 C  CE  . MET A 1 369 ? -28.624 33.553 -11.232 1.00 86.02  ? 369 MET A CE  1 
ATOM   2967 N  N   . PRO A 1 370 ? -31.946 32.724 -7.984  1.00 89.09  ? 370 PRO A N   1 
ATOM   2968 C  CA  . PRO A 1 370 ? -32.632 33.702 -7.140  1.00 84.42  ? 370 PRO A CA  1 
ATOM   2969 C  C   . PRO A 1 370 ? -31.861 35.009 -7.004  1.00 78.16  ? 370 PRO A C   1 
ATOM   2970 O  O   . PRO A 1 370 ? -30.670 35.104 -7.304  1.00 75.30  ? 370 PRO A O   1 
ATOM   2971 C  CB  . PRO A 1 370 ? -32.728 32.987 -5.780  1.00 85.51  ? 370 PRO A CB  1 
ATOM   2972 C  CG  . PRO A 1 370 ? -31.952 31.683 -5.926  1.00 85.12  ? 370 PRO A CG  1 
ATOM   2973 C  CD  . PRO A 1 370 ? -31.159 31.773 -7.187  1.00 87.72  ? 370 PRO A CD  1 
ATOM   2974 N  N   . HIS A 1 371 ? -32.583 36.024 -6.542  1.00 72.68  ? 371 HIS A N   1 
ATOM   2975 C  CA  . HIS A 1 371 ? -31.975 37.313 -6.254  1.00 69.28  ? 371 HIS A CA  1 
ATOM   2976 C  C   . HIS A 1 371 ? -30.911 37.147 -5.171  1.00 72.12  ? 371 HIS A C   1 
ATOM   2977 O  O   . HIS A 1 371 ? -31.116 36.393 -4.211  1.00 79.26  ? 371 HIS A O   1 
ATOM   2978 C  CB  . HIS A 1 371 ? -33.048 38.307 -5.799  1.00 72.42  ? 371 HIS A CB  1 
ATOM   2979 C  CG  . HIS A 1 371 ? -32.604 39.737 -5.806  1.00 69.40  ? 371 HIS A CG  1 
ATOM   2980 N  ND1 . HIS A 1 371 ? -31.701 40.243 -4.896  1.00 68.82  ? 371 HIS A ND1 1 
ATOM   2981 C  CD2 . HIS A 1 371 ? -32.956 40.775 -6.602  1.00 72.65  ? 371 HIS A CD2 1 
ATOM   2982 C  CE1 . HIS A 1 371 ? -31.506 41.527 -5.138  1.00 68.80  ? 371 HIS A CE1 1 
ATOM   2983 N  NE2 . HIS A 1 371 ? -32.256 41.875 -6.168  1.00 68.47  ? 371 HIS A NE2 1 
ATOM   2984 N  N   . PRO A 1 372 ? -29.763 37.822 -5.291  1.00 71.86  ? 372 PRO A N   1 
ATOM   2985 C  CA  . PRO A 1 372 ? -28.705 37.665 -4.277  1.00 72.57  ? 372 PRO A CA  1 
ATOM   2986 C  C   . PRO A 1 372 ? -29.115 38.098 -2.877  1.00 68.75  ? 372 PRO A C   1 
ATOM   2987 O  O   . PRO A 1 372 ? -28.376 37.813 -1.925  1.00 69.73  ? 372 PRO A O   1 
ATOM   2988 C  CB  . PRO A 1 372 ? -27.563 38.539 -4.817  1.00 72.24  ? 372 PRO A CB  1 
ATOM   2989 C  CG  . PRO A 1 372 ? -28.214 39.473 -5.790  1.00 70.32  ? 372 PRO A CG  1 
ATOM   2990 C  CD  . PRO A 1 372 ? -29.336 38.691 -6.399  1.00 69.67  ? 372 PRO A CD  1 
ATOM   2991 N  N   . ARG A 1 373 ? -30.259 38.768 -2.718  1.00 68.76  ? 373 ARG A N   1 
ATOM   2992 C  CA  . ARG A 1 373 ? -30.736 39.126 -1.387  1.00 68.23  ? 373 ARG A CA  1 
ATOM   2993 C  C   . ARG A 1 373 ? -31.062 37.900 -0.545  1.00 69.82  ? 373 ARG A C   1 
ATOM   2994 O  O   . ARG A 1 373 ? -31.085 37.997 0.686   1.00 65.47  ? 373 ARG A O   1 
ATOM   2995 C  CB  . ARG A 1 373 ? -31.968 40.024 -1.496  1.00 66.50  ? 373 ARG A CB  1 
ATOM   2996 C  CG  . ARG A 1 373 ? -33.177 39.354 -2.126  1.00 68.83  ? 373 ARG A CG  1 
ATOM   2997 C  CD  . ARG A 1 373 ? -34.139 40.386 -2.685  1.00 70.32  ? 373 ARG A CD  1 
ATOM   2998 N  NE  . ARG A 1 373 ? -35.318 39.773 -3.283  1.00 68.57  ? 373 ARG A NE  1 
ATOM   2999 C  CZ  . ARG A 1 373 ? -36.194 40.422 -4.038  1.00 75.09  ? 373 ARG A CZ  1 
ATOM   3000 N  NH1 . ARG A 1 373 ? -36.043 41.705 -4.323  1.00 75.67  ? 373 ARG A NH1 1 
ATOM   3001 N  NH2 . ARG A 1 373 ? -37.244 39.768 -4.524  1.00 80.05  ? 373 ARG A NH2 1 
ATOM   3002 N  N   . LEU A 1 374 ? -31.311 36.751 -1.180  1.00 66.01  ? 374 LEU A N   1 
ATOM   3003 C  CA  . LEU A 1 374 ? -31.612 35.536 -0.431  1.00 68.68  ? 374 LEU A CA  1 
ATOM   3004 C  C   . LEU A 1 374 ? -30.423 35.082 0.405   1.00 69.20  ? 374 LEU A C   1 
ATOM   3005 O  O   . LEU A 1 374 ? -30.604 34.420 1.433   1.00 69.18  ? 374 LEU A O   1 
ATOM   3006 C  CB  . LEU A 1 374 ? -32.041 34.424 -1.391  1.00 71.15  ? 374 LEU A CB  1 
ATOM   3007 C  CG  . LEU A 1 374 ? -32.526 33.098 -0.795  1.00 74.30  ? 374 LEU A CG  1 
ATOM   3008 C  CD1 . LEU A 1 374 ? -33.982 33.192 -0.359  1.00 74.26  ? 374 LEU A CD1 1 
ATOM   3009 C  CD2 . LEU A 1 374 ? -32.323 31.950 -1.777  1.00 76.44  ? 374 LEU A CD2 1 
ATOM   3010 N  N   . TRP A 1 375 ? -29.204 35.435 -0.008  1.00 70.53  ? 375 TRP A N   1 
ATOM   3011 C  CA  . TRP A 1 375 ? -27.997 34.958 0.648   1.00 71.06  ? 375 TRP A CA  1 
ATOM   3012 C  C   . TRP A 1 375 ? -27.134 36.053 1.260   1.00 67.58  ? 375 TRP A C   1 
ATOM   3013 O  O   . TRP A 1 375 ? -26.142 35.727 1.921   1.00 66.73  ? 375 TRP A O   1 
ATOM   3014 C  CB  . TRP A 1 375 ? -27.136 34.154 -0.340  1.00 71.96  ? 375 TRP A CB  1 
ATOM   3015 C  CG  . TRP A 1 375 ? -27.683 32.797 -0.660  1.00 74.83  ? 375 TRP A CG  1 
ATOM   3016 C  CD1 . TRP A 1 375 ? -28.689 32.502 -1.533  1.00 79.36  ? 375 TRP A CD1 1 
ATOM   3017 C  CD2 . TRP A 1 375 ? -27.244 31.547 -0.117  1.00 74.89  ? 375 TRP A CD2 1 
ATOM   3018 N  NE1 . TRP A 1 375 ? -28.907 31.146 -1.563  1.00 79.54  ? 375 TRP A NE1 1 
ATOM   3019 C  CE2 . TRP A 1 375 ? -28.032 30.537 -0.702  1.00 79.19  ? 375 TRP A CE2 1 
ATOM   3020 C  CE3 . TRP A 1 375 ? -26.262 31.185 0.810   1.00 73.17  ? 375 TRP A CE3 1 
ATOM   3021 C  CZ2 . TRP A 1 375 ? -27.867 29.188 -0.392  1.00 77.34  ? 375 TRP A CZ2 1 
ATOM   3022 C  CZ3 . TRP A 1 375 ? -26.101 29.846 1.118   1.00 73.44  ? 375 TRP A CZ3 1 
ATOM   3023 C  CH2 . TRP A 1 375 ? -26.900 28.864 0.519   1.00 75.10  ? 375 TRP A CH2 1 
ATOM   3024 N  N   . GLY A 1 376 ? -27.466 37.327 1.068   1.00 64.94  ? 376 GLY A N   1 
ATOM   3025 C  CA  . GLY A 1 376 ? -26.601 38.376 1.573   1.00 63.77  ? 376 GLY A CA  1 
ATOM   3026 C  C   . GLY A 1 376 ? -27.262 39.716 1.818   1.00 58.90  ? 376 GLY A C   1 
ATOM   3027 O  O   . GLY A 1 376 ? -26.596 40.753 1.769   1.00 59.43  ? 376 GLY A O   1 
ATOM   3028 N  N   . ALA A 1 377 ? -28.567 39.715 2.095   1.00 59.41  ? 377 ALA A N   1 
ATOM   3029 C  CA  . ALA A 1 377 ? -29.260 40.973 2.352   1.00 60.59  ? 377 ALA A CA  1 
ATOM   3030 C  C   . ALA A 1 377 ? -28.785 41.615 3.650   1.00 57.82  ? 377 ALA A C   1 
ATOM   3031 O  O   . ALA A 1 377 ? -28.588 42.834 3.711   1.00 55.20  ? 377 ALA A O   1 
ATOM   3032 C  CB  . ALA A 1 377 ? -30.771 40.746 2.392   1.00 58.24  ? 377 ALA A CB  1 
ATOM   3033 N  N   . PHE A 1 378 ? -28.588 40.815 4.691   1.00 59.49  ? 378 PHE A N   1 
ATOM   3034 C  CA  . PHE A 1 378 ? -28.232 41.345 6.002   1.00 57.63  ? 378 PHE A CA  1 
ATOM   3035 C  C   . PHE A 1 378 ? -26.735 41.626 6.135   1.00 55.03  ? 378 PHE A C   1 
ATOM   3036 O  O   . PHE A 1 378 ? -26.367 42.664 6.699   1.00 53.58  ? 378 PHE A O   1 
ATOM   3037 C  CB  . PHE A 1 378 ? -28.713 40.395 7.102   1.00 56.25  ? 378 PHE A CB  1 
ATOM   3038 C  CG  . PHE A 1 378 ? -30.211 40.315 7.215   1.00 56.36  ? 378 PHE A CG  1 
ATOM   3039 C  CD1 . PHE A 1 378 ? -30.905 41.200 8.024   1.00 55.22  ? 378 PHE A CD1 1 
ATOM   3040 C  CD2 . PHE A 1 378 ? -30.925 39.363 6.506   1.00 56.43  ? 378 PHE A CD2 1 
ATOM   3041 C  CE1 . PHE A 1 378 ? -32.282 41.133 8.129   1.00 54.64  ? 378 PHE A CE1 1 
ATOM   3042 C  CE2 . PHE A 1 378 ? -32.303 39.291 6.608   1.00 56.40  ? 378 PHE A CE2 1 
ATOM   3043 C  CZ  . PHE A 1 378 ? -32.981 40.178 7.420   1.00 55.58  ? 378 PHE A CZ  1 
ATOM   3044 N  N   . PRO A 1 379 ? -25.835 40.756 5.656   1.00 56.81  ? 379 PRO A N   1 
ATOM   3045 C  CA  . PRO A 1 379 ? -24.412 41.135 5.672   1.00 53.76  ? 379 PRO A CA  1 
ATOM   3046 C  C   . PRO A 1 379 ? -24.105 42.339 4.798   1.00 57.78  ? 379 PRO A C   1 
ATOM   3047 O  O   . PRO A 1 379 ? -23.124 43.049 5.055   1.00 60.71  ? 379 PRO A O   1 
ATOM   3048 C  CB  . PRO A 1 379 ? -23.706 39.870 5.166   1.00 56.51  ? 379 PRO A CB  1 
ATOM   3049 C  CG  . PRO A 1 379 ? -24.632 38.768 5.506   1.00 59.78  ? 379 PRO A CG  1 
ATOM   3050 C  CD  . PRO A 1 379 ? -25.999 39.341 5.272   1.00 60.32  ? 379 PRO A CD  1 
ATOM   3051 N  N   . ARG A 1 380 ? -24.922 42.592 3.773   1.00 58.77  ? 380 ARG A N   1 
ATOM   3052 C  CA  . ARG A 1 380 ? -24.717 43.762 2.924   1.00 60.99  ? 380 ARG A CA  1 
ATOM   3053 C  C   . ARG A 1 380 ? -24.913 45.054 3.705   1.00 57.06  ? 380 ARG A C   1 
ATOM   3054 O  O   . ARG A 1 380 ? -24.194 46.036 3.484   1.00 56.99  ? 380 ARG A O   1 
ATOM   3055 C  CB  . ARG A 1 380 ? -25.667 43.708 1.729   1.00 64.67  ? 380 ARG A CB  1 
ATOM   3056 C  CG  . ARG A 1 380 ? -25.483 44.824 0.720   1.00 63.82  ? 380 ARG A CG  1 
ATOM   3057 C  CD  . ARG A 1 380 ? -26.358 44.587 -0.498  1.00 65.83  ? 380 ARG A CD  1 
ATOM   3058 N  NE  . ARG A 1 380 ? -26.254 45.666 -1.473  1.00 64.70  ? 380 ARG A NE  1 
ATOM   3059 C  CZ  . ARG A 1 380 ? -25.307 45.750 -2.397  1.00 69.18  ? 380 ARG A CZ  1 
ATOM   3060 N  NH1 . ARG A 1 380 ? -24.344 44.848 -2.483  1.00 75.50  ? 380 ARG A NH1 1 
ATOM   3061 N  NH2 . ARG A 1 380 ? -25.329 46.765 -3.256  1.00 79.74  ? 380 ARG A NH2 1 
ATOM   3062 N  N   . VAL A 1 381 ? -25.885 45.076 4.618   1.00 55.21  ? 381 VAL A N   1 
ATOM   3063 C  CA  . VAL A 1 381 ? -26.104 46.259 5.443   1.00 57.82  ? 381 VAL A CA  1 
ATOM   3064 C  C   . VAL A 1 381 ? -24.957 46.442 6.428   1.00 56.85  ? 381 VAL A C   1 
ATOM   3065 O  O   . VAL A 1 381 ? -24.447 47.554 6.609   1.00 57.78  ? 381 VAL A O   1 
ATOM   3066 C  CB  . VAL A 1 381 ? -27.460 46.160 6.166   1.00 54.71  ? 381 VAL A CB  1 
ATOM   3067 C  CG1 . VAL A 1 381 ? -27.679 47.370 7.061   1.00 50.45  ? 381 VAL A CG1 1 
ATOM   3068 C  CG2 . VAL A 1 381 ? -28.591 46.019 5.157   1.00 56.77  ? 381 VAL A CG2 1 
ATOM   3069 N  N   . LEU A 1 382 ? -24.526 45.354 7.070   1.00 55.65  ? 382 LEU A N   1 
ATOM   3070 C  CA  . LEU A 1 382 ? -23.474 45.448 8.077   1.00 58.42  ? 382 LEU A CA  1 
ATOM   3071 C  C   . LEU A 1 382 ? -22.124 45.793 7.463   1.00 60.54  ? 382 LEU A C   1 
ATOM   3072 O  O   . LEU A 1 382 ? -21.327 46.502 8.087   1.00 62.33  ? 382 LEU A O   1 
ATOM   3073 C  CB  . LEU A 1 382 ? -23.374 44.134 8.853   1.00 56.43  ? 382 LEU A CB  1 
ATOM   3074 C  CG  . LEU A 1 382 ? -24.640 43.649 9.563   1.00 53.49  ? 382 LEU A CG  1 
ATOM   3075 C  CD1 . LEU A 1 382 ? -24.395 42.292 10.195  1.00 51.13  ? 382 LEU A CD1 1 
ATOM   3076 C  CD2 . LEU A 1 382 ? -25.090 44.658 10.606  1.00 52.66  ? 382 LEU A CD2 1 
ATOM   3077 N  N   . GLY A 1 383 ? -21.846 45.306 6.258   1.00 57.35  ? 383 GLY A N   1 
ATOM   3078 C  CA  . GLY A 1 383 ? -20.540 45.499 5.663   1.00 55.00  ? 383 GLY A CA  1 
ATOM   3079 C  C   . GLY A 1 383 ? -20.457 46.636 4.667   1.00 63.14  ? 383 GLY A C   1 
ATOM   3080 O  O   . GLY A 1 383 ? -19.727 47.608 4.882   1.00 64.23  ? 383 GLY A O   1 
ATOM   3081 N  N   . HIS A 1 384 ? -21.203 46.527 3.567   1.00 63.17  ? 384 HIS A N   1 
ATOM   3082 C  CA  . HIS A 1 384 ? -21.079 47.506 2.492   1.00 61.95  ? 384 HIS A CA  1 
ATOM   3083 C  C   . HIS A 1 384 ? -21.632 48.865 2.905   1.00 64.08  ? 384 HIS A C   1 
ATOM   3084 O  O   . HIS A 1 384 ? -20.985 49.898 2.696   1.00 68.17  ? 384 HIS A O   1 
ATOM   3085 C  CB  . HIS A 1 384 ? -21.786 47.000 1.236   1.00 64.22  ? 384 HIS A CB  1 
ATOM   3086 C  CG  . HIS A 1 384 ? -21.830 48.004 0.127   1.00 64.60  ? 384 HIS A CG  1 
ATOM   3087 N  ND1 . HIS A 1 384 ? -20.692 48.492 -0.479  1.00 71.63  ? 384 HIS A ND1 1 
ATOM   3088 C  CD2 . HIS A 1 384 ? -22.873 48.618 -0.479  1.00 64.32  ? 384 HIS A CD2 1 
ATOM   3089 C  CE1 . HIS A 1 384 ? -21.033 49.361 -1.414  1.00 74.58  ? 384 HIS A CE1 1 
ATOM   3090 N  NE2 . HIS A 1 384 ? -22.351 49.456 -1.434  1.00 72.67  ? 384 HIS A NE2 1 
ATOM   3091 N  N   . TYR A 1 385 ? -22.825 48.888 3.498   1.00 61.34  ? 385 TYR A N   1 
ATOM   3092 C  CA  . TYR A 1 385 ? -23.494 50.154 3.770   1.00 60.51  ? 385 TYR A CA  1 
ATOM   3093 C  C   . TYR A 1 385 ? -23.106 50.761 5.114   1.00 65.31  ? 385 TYR A C   1 
ATOM   3094 O  O   . TYR A 1 385 ? -22.987 51.986 5.223   1.00 67.78  ? 385 TYR A O   1 
ATOM   3095 C  CB  . TYR A 1 385 ? -25.012 49.973 3.694   1.00 62.30  ? 385 TYR A CB  1 
ATOM   3096 C  CG  . TYR A 1 385 ? -25.532 49.853 2.277   1.00 67.65  ? 385 TYR A CG  1 
ATOM   3097 C  CD1 . TYR A 1 385 ? -25.555 50.955 1.432   1.00 64.02  ? 385 TYR A CD1 1 
ATOM   3098 C  CD2 . TYR A 1 385 ? -26.000 48.641 1.785   1.00 66.11  ? 385 TYR A CD2 1 
ATOM   3099 C  CE1 . TYR A 1 385 ? -26.026 50.855 0.138   1.00 68.22  ? 385 TYR A CE1 1 
ATOM   3100 C  CE2 . TYR A 1 385 ? -26.474 48.532 0.490   1.00 65.87  ? 385 TYR A CE2 1 
ATOM   3101 C  CZ  . TYR A 1 385 ? -26.485 49.642 -0.328  1.00 68.85  ? 385 TYR A CZ  1 
ATOM   3102 O  OH  . TYR A 1 385 ? -26.957 49.541 -1.618  1.00 72.68  ? 385 TYR A OH  1 
ATOM   3103 N  N   . SER A 1 386 ? -22.904 49.937 6.145   1.00 62.32  ? 386 SER A N   1 
ATOM   3104 C  CA  . SER A 1 386 ? -22.554 50.479 7.454   1.00 57.19  ? 386 SER A CA  1 
ATOM   3105 C  C   . SER A 1 386 ? -21.063 50.778 7.555   1.00 58.97  ? 386 SER A C   1 
ATOM   3106 O  O   . SER A 1 386 ? -20.668 51.870 7.978   1.00 61.14  ? 386 SER A O   1 
ATOM   3107 C  CB  . SER A 1 386 ? -22.981 49.512 8.559   1.00 59.42  ? 386 SER A CB  1 
ATOM   3108 O  OG  . SER A 1 386 ? -22.639 50.016 9.838   1.00 57.47  ? 386 SER A OG  1 
ATOM   3109 N  N   . ARG A 1 387 ? -20.219 49.820 7.169   1.00 59.40  ? 387 ARG A N   1 
ATOM   3110 C  CA  . ARG A 1 387 ? -18.777 50.006 7.283   1.00 64.52  ? 387 ARG A CA  1 
ATOM   3111 C  C   . ARG A 1 387 ? -18.218 50.796 6.104   1.00 67.58  ? 387 ARG A C   1 
ATOM   3112 O  O   . ARG A 1 387 ? -17.674 51.892 6.278   1.00 70.85  ? 387 ARG A O   1 
ATOM   3113 C  CB  . ARG A 1 387 ? -18.074 48.649 7.393   1.00 61.88  ? 387 ARG A CB  1 
ATOM   3114 C  CG  . ARG A 1 387 ? -16.558 48.755 7.399   1.00 58.73  ? 387 ARG A CG  1 
ATOM   3115 C  CD  . ARG A 1 387 ? -15.884 47.402 7.232   1.00 58.62  ? 387 ARG A CD  1 
ATOM   3116 N  NE  . ARG A 1 387 ? -16.288 46.730 6.003   1.00 61.35  ? 387 ARG A NE  1 
ATOM   3117 C  CZ  . ARG A 1 387 ? -16.936 45.574 5.959   1.00 63.01  ? 387 ARG A CZ  1 
ATOM   3118 N  NH1 . ARG A 1 387 ? -17.247 44.915 7.063   1.00 65.16  ? 387 ARG A NH1 1 
ATOM   3119 N  NH2 . ARG A 1 387 ? -17.271 45.062 4.778   1.00 67.58  ? 387 ARG A NH2 1 
ATOM   3120 N  N   . ASP A 1 388 ? -18.346 50.250 4.893   1.00 61.30  ? 388 ASP A N   1 
ATOM   3121 C  CA  . ASP A 1 388 ? -17.681 50.842 3.737   1.00 65.35  ? 388 ASP A CA  1 
ATOM   3122 C  C   . ASP A 1 388 ? -18.327 52.163 3.334   1.00 69.90  ? 388 ASP A C   1 
ATOM   3123 O  O   . ASP A 1 388 ? -17.640 53.180 3.186   1.00 79.30  ? 388 ASP A O   1 
ATOM   3124 C  CB  . ASP A 1 388 ? -17.687 49.853 2.570   1.00 64.98  ? 388 ASP A CB  1 
ATOM   3125 C  CG  . ASP A 1 388 ? -16.942 48.569 2.891   1.00 66.32  ? 388 ASP A CG  1 
ATOM   3126 O  OD1 . ASP A 1 388 ? -16.003 48.614 3.714   1.00 64.64  ? 388 ASP A OD1 1 
ATOM   3127 O  OD2 . ASP A 1 388 ? -17.294 47.514 2.321   1.00 69.03  ? 388 ASP A OD2 1 
ATOM   3128 N  N   . GLU A 1 389 ? -19.649 52.171 3.151   1.00 68.27  ? 389 GLU A N   1 
ATOM   3129 C  CA  . GLU A 1 389 ? -20.331 53.376 2.694   1.00 69.99  ? 389 GLU A CA  1 
ATOM   3130 C  C   . GLU A 1 389 ? -20.663 54.340 3.825   1.00 67.05  ? 389 GLU A C   1 
ATOM   3131 O  O   . GLU A 1 389 ? -20.922 55.518 3.554   1.00 66.94  ? 389 GLU A O   1 
ATOM   3132 C  CB  . GLU A 1 389 ? -21.612 53.006 1.943   1.00 70.88  ? 389 GLU A CB  1 
ATOM   3133 C  CG  . GLU A 1 389 ? -21.368 52.313 0.611   1.00 71.04  ? 389 GLU A CG  1 
ATOM   3134 C  CD  . GLU A 1 389 ? -20.666 53.206 -0.393  1.00 77.99  ? 389 GLU A CD  1 
ATOM   3135 O  OE1 . GLU A 1 389 ? -20.865 54.438 -0.339  1.00 79.62  ? 389 GLU A OE1 1 
ATOM   3136 O  OE2 . GLU A 1 389 ? -19.910 52.676 -1.235  1.00 86.83  ? 389 GLU A OE2 1 
ATOM   3137 N  N   . GLN A 1 390 ? -20.667 53.870 5.074   1.00 69.92  ? 390 GLN A N   1 
ATOM   3138 C  CA  . GLN A 1 390 ? -20.911 54.714 6.246   1.00 67.57  ? 390 GLN A CA  1 
ATOM   3139 C  C   . GLN A 1 390 ? -22.285 55.382 6.179   1.00 64.29  ? 390 GLN A C   1 
ATOM   3140 O  O   . GLN A 1 390 ? -22.428 56.588 6.389   1.00 63.48  ? 390 GLN A O   1 
ATOM   3141 C  CB  . GLN A 1 390 ? -19.802 55.757 6.414   1.00 68.16  ? 390 GLN A CB  1 
ATOM   3142 C  CG  . GLN A 1 390 ? -18.431 55.170 6.693   1.00 72.98  ? 390 GLN A CG  1 
ATOM   3143 C  CD  . GLN A 1 390 ? -17.362 56.235 6.834   1.00 87.10  ? 390 GLN A CD  1 
ATOM   3144 O  OE1 . GLN A 1 390 ? -16.811 56.713 5.842   1.00 85.15  ? 390 GLN A OE1 1 
ATOM   3145 N  NE2 . GLN A 1 390 ? -17.065 56.615 8.071   1.00 91.60  ? 390 GLN A NE2 1 
ATOM   3146 N  N   . LEU A 1 391 ? -23.310 54.577 5.883   1.00 63.75  ? 391 LEU A N   1 
ATOM   3147 C  CA  . LEU A 1 391 ? -24.676 55.089 5.901   1.00 62.82  ? 391 LEU A CA  1 
ATOM   3148 C  C   . LEU A 1 391 ? -25.161 55.337 7.323   1.00 66.69  ? 391 LEU A C   1 
ATOM   3149 O  O   . LEU A 1 391 ? -25.911 56.289 7.566   1.00 66.61  ? 391 LEU A O   1 
ATOM   3150 C  CB  . LEU A 1 391 ? -25.614 54.116 5.185   1.00 62.38  ? 391 LEU A CB  1 
ATOM   3151 C  CG  . LEU A 1 391 ? -26.215 54.585 3.858   1.00 65.70  ? 391 LEU A CG  1 
ATOM   3152 C  CD1 . LEU A 1 391 ? -25.122 54.853 2.839   1.00 70.92  ? 391 LEU A CD1 1 
ATOM   3153 C  CD2 . LEU A 1 391 ? -27.210 53.561 3.331   1.00 68.16  ? 391 LEU A CD2 1 
ATOM   3154 N  N   . PHE A 1 392 ? -24.746 54.496 8.268   1.00 61.69  ? 392 PHE A N   1 
ATOM   3155 C  CA  . PHE A 1 392 ? -25.133 54.625 9.666   1.00 57.74  ? 392 PHE A CA  1 
ATOM   3156 C  C   . PHE A 1 392 ? -24.135 53.847 10.506  1.00 58.90  ? 392 PHE A C   1 
ATOM   3157 O  O   . PHE A 1 392 ? -23.490 52.924 9.993   1.00 59.61  ? 392 PHE A O   1 
ATOM   3158 C  CB  . PHE A 1 392 ? -26.558 54.102 9.901   1.00 56.92  ? 392 PHE A CB  1 
ATOM   3159 C  CG  . PHE A 1 392 ? -26.988 53.057 8.914   1.00 55.75  ? 392 PHE A CG  1 
ATOM   3160 C  CD1 . PHE A 1 392 ? -26.296 51.863 8.801   1.00 59.01  ? 392 PHE A CD1 1 
ATOM   3161 C  CD2 . PHE A 1 392 ? -28.088 53.269 8.101   1.00 59.59  ? 392 PHE A CD2 1 
ATOM   3162 C  CE1 . PHE A 1 392 ? -26.688 50.904 7.890   1.00 58.27  ? 392 PHE A CE1 1 
ATOM   3163 C  CE2 . PHE A 1 392 ? -28.487 52.311 7.191   1.00 60.82  ? 392 PHE A CE2 1 
ATOM   3164 C  CZ  . PHE A 1 392 ? -27.786 51.127 7.086   1.00 58.06  ? 392 PHE A CZ  1 
ATOM   3165 N  N   . PRO A 1 393 ? -23.970 54.197 11.781  1.00 60.16  ? 393 PRO A N   1 
ATOM   3166 C  CA  . PRO A 1 393 ? -23.086 53.414 12.649  1.00 56.39  ? 393 PRO A CA  1 
ATOM   3167 C  C   . PRO A 1 393 ? -23.559 51.971 12.753  1.00 57.81  ? 393 PRO A C   1 
ATOM   3168 O  O   . PRO A 1 393 ? -24.724 51.649 12.512  1.00 59.93  ? 393 PRO A O   1 
ATOM   3169 C  CB  . PRO A 1 393 ? -23.182 54.134 14.000  1.00 54.26  ? 393 PRO A CB  1 
ATOM   3170 C  CG  . PRO A 1 393 ? -23.616 55.524 13.656  1.00 57.74  ? 393 PRO A CG  1 
ATOM   3171 C  CD  . PRO A 1 393 ? -24.517 55.380 12.468  1.00 60.99  ? 393 PRO A CD  1 
ATOM   3172 N  N   . LEU A 1 394 ? -22.623 51.091 13.116  1.00 55.68  ? 394 LEU A N   1 
ATOM   3173 C  CA  . LEU A 1 394 ? -22.936 49.666 13.158  1.00 55.15  ? 394 LEU A CA  1 
ATOM   3174 C  C   . LEU A 1 394 ? -23.995 49.353 14.206  1.00 54.86  ? 394 LEU A C   1 
ATOM   3175 O  O   . LEU A 1 394 ? -24.746 48.381 14.058  1.00 53.22  ? 394 LEU A O   1 
ATOM   3176 C  CB  . LEU A 1 394 ? -21.667 48.855 13.419  1.00 53.52  ? 394 LEU A CB  1 
ATOM   3177 C  CG  . LEU A 1 394 ? -21.771 47.348 13.186  1.00 52.78  ? 394 LEU A CG  1 
ATOM   3178 C  CD1 . LEU A 1 394 ? -22.491 47.060 11.879  1.00 51.50  ? 394 LEU A CD1 1 
ATOM   3179 C  CD2 . LEU A 1 394 ? -20.388 46.725 13.180  1.00 56.99  ? 394 LEU A CD2 1 
ATOM   3180 N  N   . THR A 1 395 ? -24.076 50.160 15.266  1.00 58.23  ? 395 THR A N   1 
ATOM   3181 C  CA  . THR A 1 395 ? -25.136 49.979 16.252  1.00 53.53  ? 395 THR A CA  1 
ATOM   3182 C  C   . THR A 1 395 ? -26.505 50.208 15.623  1.00 53.89  ? 395 THR A C   1 
ATOM   3183 O  O   . THR A 1 395 ? -27.439 49.426 15.832  1.00 62.84  ? 395 THR A O   1 
ATOM   3184 C  CB  . THR A 1 395 ? -24.920 50.924 17.435  1.00 54.60  ? 395 THR A CB  1 
ATOM   3185 O  OG1 . THR A 1 395 ? -24.931 52.281 16.972  1.00 56.78  ? 395 THR A OG1 1 
ATOM   3186 C  CG2 . THR A 1 395 ? -23.585 50.635 18.106  1.00 54.73  ? 395 THR A CG2 1 
ATOM   3187 N  N   . THR A 1 396 ? -26.638 51.282 14.840  1.00 54.64  ? 396 THR A N   1 
ATOM   3188 C  CA  . THR A 1 396 ? -27.897 51.543 14.150  1.00 54.91  ? 396 THR A CA  1 
ATOM   3189 C  C   . THR A 1 396 ? -28.198 50.458 13.123  1.00 55.66  ? 396 THR A C   1 
ATOM   3190 O  O   . THR A 1 396 ? -29.354 50.050 12.959  1.00 53.11  ? 396 THR A O   1 
ATOM   3191 C  CB  . THR A 1 396 ? -27.852 52.916 13.477  1.00 56.08  ? 396 THR A CB  1 
ATOM   3192 O  OG1 . THR A 1 396 ? -27.524 53.916 14.449  1.00 59.77  ? 396 THR A OG1 1 
ATOM   3193 C  CG2 . THR A 1 396 ? -29.197 53.250 12.850  1.00 53.10  ? 396 THR A CG2 1 
ATOM   3194 N  N   . ALA A 1 397 ? -27.167 49.974 12.423  1.00 60.24  ? 397 ALA A N   1 
ATOM   3195 C  CA  . ALA A 1 397 ? -27.379 48.945 11.410  1.00 57.85  ? 397 ALA A CA  1 
ATOM   3196 C  C   . ALA A 1 397 ? -27.881 47.648 12.033  1.00 56.14  ? 397 ALA A C   1 
ATOM   3197 O  O   . ALA A 1 397 ? -28.809 47.017 11.511  1.00 55.00  ? 397 ALA A O   1 
ATOM   3198 C  CB  . ALA A 1 397 ? -26.088 48.703 10.630  1.00 56.74  ? 397 ALA A CB  1 
ATOM   3199 N  N   . VAL A 1 398 ? -27.281 47.232 13.151  1.00 57.11  ? 398 VAL A N   1 
ATOM   3200 C  CA  . VAL A 1 398 ? -27.743 46.031 13.841  1.00 53.60  ? 398 VAL A CA  1 
ATOM   3201 C  C   . VAL A 1 398 ? -29.145 46.240 14.398  1.00 53.72  ? 398 VAL A C   1 
ATOM   3202 O  O   . VAL A 1 398 ? -29.981 45.328 14.376  1.00 50.07  ? 398 VAL A O   1 
ATOM   3203 C  CB  . VAL A 1 398 ? -26.751 45.635 14.949  1.00 51.62  ? 398 VAL A CB  1 
ATOM   3204 C  CG1 . VAL A 1 398 ? -27.306 44.488 15.783  1.00 53.03  ? 398 VAL A CG1 1 
ATOM   3205 C  CG2 . VAL A 1 398 ? -25.409 45.256 14.349  1.00 51.03  ? 398 VAL A CG2 1 
ATOM   3206 N  N   . HIS A 1 399 ? -29.424 47.444 14.904  1.00 52.88  ? 399 HIS A N   1 
ATOM   3207 C  CA  . HIS A 1 399 ? -30.733 47.726 15.483  1.00 50.79  ? 399 HIS A CA  1 
ATOM   3208 C  C   . HIS A 1 399 ? -31.845 47.558 14.454  1.00 53.29  ? 399 HIS A C   1 
ATOM   3209 O  O   . HIS A 1 399 ? -32.949 47.112 14.789  1.00 52.26  ? 399 HIS A O   1 
ATOM   3210 C  CB  . HIS A 1 399 ? -30.741 49.138 16.071  1.00 50.52  ? 399 HIS A CB  1 
ATOM   3211 C  CG  . HIS A 1 399 ? -32.078 49.581 16.578  1.00 52.19  ? 399 HIS A CG  1 
ATOM   3212 N  ND1 . HIS A 1 399 ? -32.825 48.837 17.466  1.00 55.51  ? 399 HIS A ND1 1 
ATOM   3213 C  CD2 . HIS A 1 399 ? -32.795 50.704 16.334  1.00 51.17  ? 399 HIS A CD2 1 
ATOM   3214 C  CE1 . HIS A 1 399 ? -33.948 49.477 17.739  1.00 53.45  ? 399 HIS A CE1 1 
ATOM   3215 N  NE2 . HIS A 1 399 ? -33.954 50.613 17.065  1.00 53.90  ? 399 HIS A NE2 1 
ATOM   3216 N  N   . LYS A 1 400 ? -31.568 47.888 13.192  1.00 52.76  ? 400 LYS A N   1 
ATOM   3217 C  CA  . LYS A 1 400 ? -32.572 47.806 12.138  1.00 53.40  ? 400 LYS A CA  1 
ATOM   3218 C  C   . LYS A 1 400 ? -32.884 46.377 11.708  1.00 52.03  ? 400 LYS A C   1 
ATOM   3219 O  O   . LYS A 1 400 ? -33.793 46.185 10.892  1.00 52.49  ? 400 LYS A O   1 
ATOM   3220 C  CB  . LYS A 1 400 ? -32.121 48.626 10.928  1.00 53.17  ? 400 LYS A CB  1 
ATOM   3221 C  CG  . LYS A 1 400 ? -32.169 50.126 11.156  1.00 53.62  ? 400 LYS A CG  1 
ATOM   3222 C  CD  . LYS A 1 400 ? -31.719 50.881 9.921   1.00 53.17  ? 400 LYS A CD  1 
ATOM   3223 C  CE  . LYS A 1 400 ? -31.954 52.372 10.075  1.00 58.69  ? 400 LYS A CE  1 
ATOM   3224 N  NZ  . LYS A 1 400 ? -33.400 52.684 10.244  1.00 59.28  ? 400 LYS A NZ  1 
ATOM   3225 N  N   . MET A 1 401 ? -32.167 45.375 12.222  1.00 51.85  ? 401 MET A N   1 
ATOM   3226 C  CA  . MET A 1 401 ? -32.474 43.980 11.933  1.00 49.43  ? 401 MET A CA  1 
ATOM   3227 C  C   . MET A 1 401 ? -32.640 43.150 13.203  1.00 50.77  ? 401 MET A C   1 
ATOM   3228 O  O   . MET A 1 401 ? -32.653 41.916 13.126  1.00 49.84  ? 401 MET A O   1 
ATOM   3229 C  CB  . MET A 1 401 ? -31.390 43.363 11.038  1.00 48.12  ? 401 MET A CB  1 
ATOM   3230 C  CG  . MET A 1 401 ? -29.971 43.753 11.434  1.00 51.30  ? 401 MET A CG  1 
ATOM   3231 S  SD  . MET A 1 401 ? -28.663 42.807 10.621  1.00 53.74  ? 401 MET A SD  1 
ATOM   3232 C  CE  . MET A 1 401 ? -28.458 43.714 9.088   1.00 49.05  ? 401 MET A CE  1 
ATOM   3233 N  N   . THR A 1 402 ? -32.765 43.791 14.368  1.00 55.68  ? 402 THR A N   1 
ATOM   3234 C  CA  . THR A 1 402 ? -32.892 43.074 15.632  1.00 55.60  ? 402 THR A CA  1 
ATOM   3235 C  C   . THR A 1 402 ? -33.975 43.672 16.523  1.00 56.81  ? 402 THR A C   1 
ATOM   3236 O  O   . THR A 1 402 ? -35.140 43.270 16.448  1.00 54.78  ? 402 THR A O   1 
ATOM   3237 C  CB  . THR A 1 402 ? -31.557 43.068 16.387  1.00 49.20  ? 402 THR A CB  1 
ATOM   3238 O  OG1 . THR A 1 402 ? -31.049 44.406 16.476  1.00 52.85  ? 402 THR A OG1 1 
ATOM   3239 C  CG2 . THR A 1 402 ? -30.538 42.180 15.687  1.00 49.97  ? 402 THR A CG2 1 
ATOM   3240 N  N   . GLY A 1 403 ? -33.592 44.633 17.368  1.00 55.39  ? 403 GLY A N   1 
ATOM   3241 C  CA  . GLY A 1 403 ? -34.519 45.145 18.367  1.00 58.46  ? 403 GLY A CA  1 
ATOM   3242 C  C   . GLY A 1 403 ? -35.711 45.860 17.761  1.00 61.25  ? 403 GLY A C   1 
ATOM   3243 O  O   . GLY A 1 403 ? -36.855 45.640 18.168  1.00 63.43  ? 403 GLY A O   1 
ATOM   3244 N  N   . LEU A 1 404 ? -35.458 46.739 16.786  1.00 53.30  ? 404 LEU A N   1 
ATOM   3245 C  CA  . LEU A 1 404 ? -36.552 47.431 16.110  1.00 55.08  ? 404 LEU A CA  1 
ATOM   3246 C  C   . LEU A 1 404 ? -37.511 46.443 15.461  1.00 57.76  ? 404 LEU A C   1 
ATOM   3247 O  O   . LEU A 1 404 ? -38.725 46.676 15.421  1.00 57.34  ? 404 LEU A O   1 
ATOM   3248 C  CB  . LEU A 1 404 ? -35.994 48.398 15.066  1.00 57.15  ? 404 LEU A CB  1 
ATOM   3249 C  CG  . LEU A 1 404 ? -37.002 49.219 14.257  1.00 57.50  ? 404 LEU A CG  1 
ATOM   3250 C  CD1 . LEU A 1 404 ? -37.687 50.252 15.139  1.00 53.78  ? 404 LEU A CD1 1 
ATOM   3251 C  CD2 . LEU A 1 404 ? -36.329 49.884 13.064  1.00 55.63  ? 404 LEU A CD2 1 
ATOM   3252 N  N   . SER A 1 405 ? -36.984 45.328 14.956  1.00 55.11  ? 405 SER A N   1 
ATOM   3253 C  CA  . SER A 1 405 ? -37.832 44.323 14.327  1.00 54.13  ? 405 SER A CA  1 
ATOM   3254 C  C   . SER A 1 405 ? -38.589 43.506 15.365  1.00 55.63  ? 405 SER A C   1 
ATOM   3255 O  O   . SER A 1 405 ? -39.791 43.256 15.213  1.00 53.71  ? 405 SER A O   1 
ATOM   3256 C  CB  . SER A 1 405 ? -36.982 43.414 13.442  1.00 51.62  ? 405 SER A CB  1 
ATOM   3257 O  OG  . SER A 1 405 ? -36.275 44.170 12.474  1.00 52.12  ? 405 SER A OG  1 
ATOM   3258 N  N   . ALA A 1 406 ? -37.903 43.086 16.430  1.00 58.11  ? 406 ALA A N   1 
ATOM   3259 C  CA  . ALA A 1 406 ? -38.548 42.283 17.463  1.00 58.10  ? 406 ALA A CA  1 
ATOM   3260 C  C   . ALA A 1 406 ? -39.631 43.073 18.188  1.00 60.57  ? 406 ALA A C   1 
ATOM   3261 O  O   . ALA A 1 406 ? -40.693 42.528 18.512  1.00 58.45  ? 406 ALA A O   1 
ATOM   3262 C  CB  . ALA A 1 406 ? -37.505 41.771 18.455  1.00 53.95  ? 406 ALA A CB  1 
ATOM   3263 N  N   . ALA A 1 407 ? -39.381 44.357 18.451  1.00 55.11  ? 407 ALA A N   1 
ATOM   3264 C  CA  . ALA A 1 407 ? -40.374 45.171 19.143  1.00 55.42  ? 407 ALA A CA  1 
ATOM   3265 C  C   . ALA A 1 407 ? -41.581 45.458 18.261  1.00 60.81  ? 407 ALA A C   1 
ATOM   3266 O  O   . ALA A 1 407 ? -42.708 45.546 18.763  1.00 59.74  ? 407 ALA A O   1 
ATOM   3267 C  CB  . ALA A 1 407 ? -39.742 46.480 19.619  1.00 54.67  ? 407 ALA A CB  1 
ATOM   3268 N  N   . ARG A 1 408 ? -41.369 45.601 16.951  1.00 58.40  ? 408 ARG A N   1 
ATOM   3269 C  CA  A ARG A 1 408 ? -42.474 45.910 16.049  0.33 58.91  ? 408 ARG A CA  1 
ATOM   3270 C  CA  B ARG A 1 408 ? -42.475 45.912 16.052  0.67 59.22  ? 408 ARG A CA  1 
ATOM   3271 C  C   . ARG A 1 408 ? -43.456 44.749 15.957  1.00 57.08  ? 408 ARG A C   1 
ATOM   3272 O  O   . ARG A 1 408 ? -44.675 44.953 16.007  1.00 57.37  ? 408 ARG A O   1 
ATOM   3273 C  CB  A ARG A 1 408 ? -41.935 46.267 14.665  0.33 62.73  ? 408 ARG A CB  1 
ATOM   3274 C  CB  B ARG A 1 408 ? -41.937 46.278 14.669  0.67 63.41  ? 408 ARG A CB  1 
ATOM   3275 C  CG  A ARG A 1 408 ? -43.000 46.374 13.585  0.33 61.83  ? 408 ARG A CG  1 
ATOM   3276 C  CG  B ARG A 1 408 ? -42.764 47.325 13.944  0.67 62.75  ? 408 ARG A CG  1 
ATOM   3277 C  CD  A ARG A 1 408 ? -44.018 47.456 13.907  0.33 61.66  ? 408 ARG A CD  1 
ATOM   3278 C  CD  B ARG A 1 408 ? -42.714 48.657 14.676  0.67 63.53  ? 408 ARG A CD  1 
ATOM   3279 N  NE  A ARG A 1 408 ? -43.396 48.763 14.071  0.33 64.08  ? 408 ARG A NE  1 
ATOM   3280 N  NE  B ARG A 1 408 ? -43.656 49.626 14.129  0.67 64.40  ? 408 ARG A NE  1 
ATOM   3281 C  CZ  A ARG A 1 408 ? -44.066 49.901 14.187  0.33 65.81  ? 408 ARG A CZ  1 
ATOM   3282 C  CZ  B ARG A 1 408 ? -44.871 49.844 14.612  0.67 66.75  ? 408 ARG A CZ  1 
ATOM   3283 N  NH1 A ARG A 1 408 ? -45.388 49.931 14.146  0.33 68.38  ? 408 ARG A NH1 1 
ATOM   3284 N  NH1 B ARG A 1 408 ? -45.331 49.173 15.656  0.67 64.74  ? 408 ARG A NH1 1 
ATOM   3285 N  NH2 A ARG A 1 408 ? -43.394 51.038 14.345  0.33 64.25  ? 408 ARG A NH2 1 
ATOM   3286 N  NH2 B ARG A 1 408 ? -45.645 50.759 14.035  0.67 72.10  ? 408 ARG A NH2 1 
ATOM   3287 N  N   . PHE A 1 409 ? -42.949 43.527 15.822  1.00 57.98  ? 409 PHE A N   1 
ATOM   3288 C  CA  . PHE A 1 409 ? -43.788 42.345 15.686  1.00 56.06  ? 409 PHE A CA  1 
ATOM   3289 C  C   . PHE A 1 409 ? -44.047 41.648 17.017  1.00 58.03  ? 409 PHE A C   1 
ATOM   3290 O  O   . PHE A 1 409 ? -44.647 40.568 17.030  1.00 54.28  ? 409 PHE A O   1 
ATOM   3291 C  CB  . PHE A 1 409 ? -43.158 41.370 14.689  1.00 53.98  ? 409 PHE A CB  1 
ATOM   3292 C  CG  . PHE A 1 409 ? -43.077 41.910 13.287  1.00 59.38  ? 409 PHE A CG  1 
ATOM   3293 C  CD1 . PHE A 1 409 ? -42.042 42.751 12.911  1.00 55.41  ? 409 PHE A CD1 1 
ATOM   3294 C  CD2 . PHE A 1 409 ? -44.040 41.582 12.347  1.00 57.01  ? 409 PHE A CD2 1 
ATOM   3295 C  CE1 . PHE A 1 409 ? -41.969 43.253 11.626  1.00 52.90  ? 409 PHE A CE1 1 
ATOM   3296 C  CE2 . PHE A 1 409 ? -43.970 42.080 11.058  1.00 55.08  ? 409 PHE A CE2 1 
ATOM   3297 C  CZ  . PHE A 1 409 ? -42.933 42.916 10.699  1.00 53.42  ? 409 PHE A CZ  1 
ATOM   3298 N  N   . GLN A 1 410 ? -43.610 42.246 18.128  1.00 61.54  ? 410 GLN A N   1 
ATOM   3299 C  CA  . GLN A 1 410 ? -43.872 41.733 19.474  1.00 56.42  ? 410 GLN A CA  1 
ATOM   3300 C  C   . GLN A 1 410 ? -43.339 40.311 19.647  1.00 52.09  ? 410 GLN A C   1 
ATOM   3301 O  O   . GLN A 1 410 ? -44.037 39.410 20.115  1.00 54.89  ? 410 GLN A O   1 
ATOM   3302 C  CB  . GLN A 1 410 ? -45.364 41.808 19.811  1.00 56.99  ? 410 GLN A CB  1 
ATOM   3303 C  CG  . GLN A 1 410 ? -45.934 43.215 19.750  1.00 57.40  ? 410 GLN A CG  1 
ATOM   3304 C  CD  . GLN A 1 410 ? -47.383 43.279 20.188  1.00 61.46  ? 410 GLN A CD  1 
ATOM   3305 O  OE1 . GLN A 1 410 ? -47.794 42.590 21.121  1.00 64.50  ? 410 GLN A OE1 1 
ATOM   3306 N  NE2 . GLN A 1 410 ? -48.169 44.109 19.511  1.00 59.61  ? 410 GLN A NE2 1 
ATOM   3307 N  N   . LEU A 1 411 ? -42.082 40.115 19.258  1.00 54.97  ? 411 LEU A N   1 
ATOM   3308 C  CA  . LEU A 1 411 ? -41.394 38.856 19.513  1.00 55.84  ? 411 LEU A CA  1 
ATOM   3309 C  C   . LEU A 1 411 ? -40.873 38.864 20.945  1.00 52.62  ? 411 LEU A C   1 
ATOM   3310 O  O   . LEU A 1 411 ? -40.019 39.685 21.297  1.00 52.93  ? 411 LEU A O   1 
ATOM   3311 C  CB  . LEU A 1 411 ? -40.257 38.652 18.515  1.00 54.32  ? 411 LEU A CB  1 
ATOM   3312 C  CG  . LEU A 1 411 ? -40.676 38.556 17.047  1.00 48.91  ? 411 LEU A CG  1 
ATOM   3313 C  CD1 . LEU A 1 411 ? -39.474 38.281 16.157  1.00 48.29  ? 411 LEU A CD1 1 
ATOM   3314 C  CD2 . LEU A 1 411 ? -41.739 37.485 16.864  1.00 47.61  ? 411 LEU A CD2 1 
ATOM   3315 N  N   . ALA A 1 412 ? -41.388 37.955 21.769  1.00 55.51  ? 412 ALA A N   1 
ATOM   3316 C  CA  . ALA A 1 412 ? -41.110 37.996 23.199  1.00 55.80  ? 412 ALA A CA  1 
ATOM   3317 C  C   . ALA A 1 412 ? -39.671 37.591 23.491  1.00 51.80  ? 412 ALA A C   1 
ATOM   3318 O  O   . ALA A 1 412 ? -39.215 36.524 23.067  1.00 50.43  ? 412 ALA A O   1 
ATOM   3319 C  CB  . ALA A 1 412 ? -42.078 37.085 23.950  1.00 59.36  ? 412 ALA A CB  1 
ATOM   3320 N  N   . ASP A 1 413 ? -38.958 38.457 24.215  1.00 50.90  ? 413 ASP A N   1 
ATOM   3321 C  CA  . ASP A 1 413 ? -37.626 38.157 24.744  1.00 50.95  ? 413 ASP A CA  1 
ATOM   3322 C  C   . ASP A 1 413 ? -36.631 37.819 23.637  1.00 50.96  ? 413 ASP A C   1 
ATOM   3323 O  O   . ASP A 1 413 ? -35.785 36.936 23.789  1.00 51.27  ? 413 ASP A O   1 
ATOM   3324 C  CB  . ASP A 1 413 ? -37.684 37.029 25.775  1.00 50.98  ? 413 ASP A CB  1 
ATOM   3325 C  CG  . ASP A 1 413 ? -38.453 37.420 27.019  1.00 53.48  ? 413 ASP A CG  1 
ATOM   3326 O  OD1 . ASP A 1 413 ? -38.494 38.628 27.335  1.00 56.11  ? 413 ASP A OD1 1 
ATOM   3327 O  OD2 . ASP A 1 413 ? -39.013 36.520 27.680  1.00 53.39  ? 413 ASP A OD2 1 
ATOM   3328 N  N   . ARG A 1 414 ? -36.723 38.529 22.515  1.00 54.59  ? 414 ARG A N   1 
ATOM   3329 C  CA  . ARG A 1 414 ? -35.806 38.329 21.404  1.00 47.22  ? 414 ARG A CA  1 
ATOM   3330 C  C   . ARG A 1 414 ? -35.433 39.682 20.815  1.00 47.16  ? 414 ARG A C   1 
ATOM   3331 O  O   . ARG A 1 414 ? -36.063 40.704 21.097  1.00 54.41  ? 414 ARG A O   1 
ATOM   3332 C  CB  . ARG A 1 414 ? -36.410 37.408 20.334  1.00 49.20  ? 414 ARG A CB  1 
ATOM   3333 C  CG  . ARG A 1 414 ? -36.739 36.014 20.852  1.00 51.92  ? 414 ARG A CG  1 
ATOM   3334 C  CD  . ARG A 1 414 ? -37.209 35.075 19.760  1.00 48.63  ? 414 ARG A CD  1 
ATOM   3335 N  NE  . ARG A 1 414 ? -37.651 33.806 20.325  1.00 50.17  ? 414 ARG A NE  1 
ATOM   3336 C  CZ  . ARG A 1 414 ? -36.842 32.802 20.636  1.00 51.28  ? 414 ARG A CZ  1 
ATOM   3337 N  NH1 . ARG A 1 414 ? -35.538 32.873 20.424  1.00 52.61  ? 414 ARG A NH1 1 
ATOM   3338 N  NH2 . ARG A 1 414 ? -37.353 31.700 21.179  1.00 50.20  ? 414 ARG A NH2 1 
ATOM   3339 N  N   . GLY A 1 415 ? -34.384 39.680 19.996  1.00 47.39  ? 415 GLY A N   1 
ATOM   3340 C  CA  . GLY A 1 415 ? -33.918 40.891 19.353  1.00 47.95  ? 415 GLY A CA  1 
ATOM   3341 C  C   . GLY A 1 415 ? -32.976 41.740 20.175  1.00 49.36  ? 415 GLY A C   1 
ATOM   3342 O  O   . GLY A 1 415 ? -32.613 42.836 19.732  1.00 49.90  ? 415 GLY A O   1 
ATOM   3343 N  N   . LEU A 1 416 ? -32.567 41.275 21.354  1.00 49.98  ? 416 LEU A N   1 
ATOM   3344 C  CA  . LEU A 1 416 ? -31.695 42.039 22.234  1.00 50.60  ? 416 LEU A CA  1 
ATOM   3345 C  C   . LEU A 1 416 ? -30.731 41.103 22.946  1.00 53.52  ? 416 LEU A C   1 
ATOM   3346 O  O   . LEU A 1 416 ? -31.102 39.990 23.329  1.00 58.09  ? 416 LEU A O   1 
ATOM   3347 C  CB  . LEU A 1 416 ? -32.499 42.831 23.274  1.00 52.00  ? 416 LEU A CB  1 
ATOM   3348 C  CG  . LEU A 1 416 ? -33.391 43.975 22.786  1.00 50.58  ? 416 LEU A CG  1 
ATOM   3349 C  CD1 . LEU A 1 416 ? -34.283 44.471 23.911  1.00 49.76  ? 416 LEU A CD1 1 
ATOM   3350 C  CD2 . LEU A 1 416 ? -32.548 45.110 22.233  1.00 51.46  ? 416 LEU A CD2 1 
ATOM   3351 N  N   . VAL A 1 417 ? -29.492 41.560 23.115  1.00 53.64  ? 417 VAL A N   1 
ATOM   3352 C  CA  . VAL A 1 417 ? -28.521 40.892 23.975  1.00 52.24  ? 417 VAL A CA  1 
ATOM   3353 C  C   . VAL A 1 417 ? -28.749 41.442 25.379  1.00 52.60  ? 417 VAL A C   1 
ATOM   3354 O  O   . VAL A 1 417 ? -28.292 42.536 25.713  1.00 51.95  ? 417 VAL A O   1 
ATOM   3355 C  CB  . VAL A 1 417 ? -27.084 41.117 23.500  1.00 49.58  ? 417 VAL A CB  1 
ATOM   3356 C  CG1 . VAL A 1 417 ? -26.102 40.425 24.433  1.00 50.79  ? 417 VAL A CG1 1 
ATOM   3357 C  CG2 . VAL A 1 417 ? -26.913 40.617 22.077  1.00 52.08  ? 417 VAL A CG2 1 
ATOM   3358 N  N   . LYS A 1 418 ? -29.465 40.682 26.202  1.00 54.34  ? 418 LYS A N   1 
ATOM   3359 C  CA  . LYS A 1 418 ? -29.945 41.202 27.473  1.00 53.79  ? 418 LYS A CA  1 
ATOM   3360 C  C   . LYS A 1 418 ? -30.148 40.045 28.441  1.00 53.15  ? 418 LYS A C   1 
ATOM   3361 O  O   . LYS A 1 418 ? -30.392 38.909 28.027  1.00 53.16  ? 418 LYS A O   1 
ATOM   3362 C  CB  . LYS A 1 418 ? -31.250 41.984 27.274  1.00 57.00  ? 418 LYS A CB  1 
ATOM   3363 C  CG  . LYS A 1 418 ? -31.728 42.768 28.481  1.00 67.83  ? 418 LYS A CG  1 
ATOM   3364 C  CD  . LYS A 1 418 ? -33.036 43.477 28.171  1.00 62.93  ? 418 LYS A CD  1 
ATOM   3365 C  CE  . LYS A 1 418 ? -33.523 44.290 29.358  1.00 65.92  ? 418 LYS A CE  1 
ATOM   3366 N  NZ  . LYS A 1 418 ? -34.814 44.971 29.068  1.00 70.44  ? 418 LYS A NZ  1 
ATOM   3367 N  N   . ILE A 1 419 ? -30.037 40.350 29.736  1.00 56.83  ? 419 ILE A N   1 
ATOM   3368 C  CA  . ILE A 1 419 ? -30.252 39.340 30.765  1.00 53.91  ? 419 ILE A CA  1 
ATOM   3369 C  C   . ILE A 1 419 ? -31.702 38.886 30.735  1.00 53.71  ? 419 ILE A C   1 
ATOM   3370 O  O   . ILE A 1 419 ? -32.629 39.705 30.784  1.00 58.59  ? 419 ILE A O   1 
ATOM   3371 C  CB  . ILE A 1 419 ? -29.876 39.893 32.147  1.00 55.63  ? 419 ILE A CB  1 
ATOM   3372 C  CG1 . ILE A 1 419 ? -28.488 40.533 32.112  1.00 56.04  ? 419 ILE A CG1 1 
ATOM   3373 C  CG2 . ILE A 1 419 ? -29.926 38.790 33.193  1.00 58.73  ? 419 ILE A CG2 1 
ATOM   3374 C  CD1 . ILE A 1 419 ? -27.393 39.565 31.792  1.00 56.26  ? 419 ILE A CD1 1 
ATOM   3375 N  N   . GLY A 1 420 ? -31.908 37.573 30.654  1.00 52.88  ? 420 GLY A N   1 
ATOM   3376 C  CA  . GLY A 1 420 ? -33.233 37.002 30.646  1.00 61.91  ? 420 GLY A CA  1 
ATOM   3377 C  C   . GLY A 1 420 ? -33.833 36.789 29.273  1.00 59.24  ? 420 GLY A C   1 
ATOM   3378 O  O   . GLY A 1 420 ? -34.783 36.009 29.142  1.00 60.13  ? 420 GLY A O   1 
ATOM   3379 N  N   . TYR A 1 421 ? -33.317 37.462 28.249  1.00 50.19  ? 421 TYR A N   1 
ATOM   3380 C  CA  . TYR A 1 421 ? -33.793 37.260 26.892  1.00 52.61  ? 421 TYR A CA  1 
ATOM   3381 C  C   . TYR A 1 421 ? -33.280 35.932 26.341  1.00 51.69  ? 421 TYR A C   1 
ATOM   3382 O  O   . TYR A 1 421 ? -32.353 35.321 26.880  1.00 53.71  ? 421 TYR A O   1 
ATOM   3383 C  CB  . TYR A 1 421 ? -33.353 38.416 25.990  1.00 55.68  ? 421 TYR A CB  1 
ATOM   3384 C  CG  . TYR A 1 421 ? -34.302 39.593 26.005  1.00 57.01  ? 421 TYR A CG  1 
ATOM   3385 C  CD1 . TYR A 1 421 ? -34.755 40.129 27.203  1.00 55.12  ? 421 TYR A CD1 1 
ATOM   3386 C  CD2 . TYR A 1 421 ? -34.738 40.175 24.823  1.00 52.77  ? 421 TYR A CD2 1 
ATOM   3387 C  CE1 . TYR A 1 421 ? -35.623 41.203 27.223  1.00 55.50  ? 421 TYR A CE1 1 
ATOM   3388 C  CE2 . TYR A 1 421 ? -35.608 41.249 24.831  1.00 52.31  ? 421 TYR A CE2 1 
ATOM   3389 C  CZ  . TYR A 1 421 ? -36.045 41.760 26.035  1.00 55.59  ? 421 TYR A CZ  1 
ATOM   3390 O  OH  . TYR A 1 421 ? -36.908 42.831 26.052  1.00 56.05  ? 421 TYR A OH  1 
ATOM   3391 N  N   . PHE A 1 422 ? -33.905 35.484 25.255  1.00 51.46  ? 422 PHE A N   1 
ATOM   3392 C  CA  . PHE A 1 422 ? -33.500 34.234 24.633  1.00 54.75  ? 422 PHE A CA  1 
ATOM   3393 C  C   . PHE A 1 422 ? -32.104 34.360 24.032  1.00 53.27  ? 422 PHE A C   1 
ATOM   3394 O  O   . PHE A 1 422 ? -31.626 35.453 23.715  1.00 55.60  ? 422 PHE A O   1 
ATOM   3395 C  CB  . PHE A 1 422 ? -34.502 33.811 23.558  1.00 54.25  ? 422 PHE A CB  1 
ATOM   3396 C  CG  . PHE A 1 422 ? -35.764 33.212 24.110  1.00 52.00  ? 422 PHE A CG  1 
ATOM   3397 C  CD1 . PHE A 1 422 ? -35.757 31.945 24.670  1.00 48.55  ? 422 PHE A CD1 1 
ATOM   3398 C  CD2 . PHE A 1 422 ? -36.958 33.912 24.064  1.00 50.79  ? 422 PHE A CD2 1 
ATOM   3399 C  CE1 . PHE A 1 422 ? -36.914 31.388 25.178  1.00 45.28  ? 422 PHE A CE1 1 
ATOM   3400 C  CE2 . PHE A 1 422 ? -38.121 33.360 24.570  1.00 53.93  ? 422 PHE A CE2 1 
ATOM   3401 C  CZ  . PHE A 1 422 ? -38.098 32.096 25.127  1.00 50.59  ? 422 PHE A CZ  1 
ATOM   3402 N  N   . ALA A 1 423 ? -31.446 33.214 23.877  1.00 51.26  ? 423 ALA A N   1 
ATOM   3403 C  CA  . ALA A 1 423 ? -30.053 33.174 23.435  1.00 51.67  ? 423 ALA A CA  1 
ATOM   3404 C  C   . ALA A 1 423 ? -29.966 32.982 21.919  1.00 50.28  ? 423 ALA A C   1 
ATOM   3405 O  O   . ALA A 1 423 ? -29.422 32.004 21.407  1.00 50.42  ? 423 ALA A O   1 
ATOM   3406 C  CB  . ALA A 1 423 ? -29.296 32.083 24.183  1.00 49.94  ? 423 ALA A CB  1 
ATOM   3407 N  N   . ASP A 1 424 ? -30.530 33.952 21.202  1.00 46.25  ? 424 ASP A N   1 
ATOM   3408 C  CA  . ASP A 1 424 ? -30.366 34.071 19.755  1.00 50.57  ? 424 ASP A CA  1 
ATOM   3409 C  C   . ASP A 1 424 ? -29.251 35.083 19.519  1.00 51.41  ? 424 ASP A C   1 
ATOM   3410 O  O   . ASP A 1 424 ? -29.454 36.292 19.660  1.00 53.75  ? 424 ASP A O   1 
ATOM   3411 C  CB  . ASP A 1 424 ? -31.667 34.498 19.082  1.00 50.23  ? 424 ASP A CB  1 
ATOM   3412 C  CG  . ASP A 1 424 ? -32.706 33.395 19.065  1.00 50.42  ? 424 ASP A CG  1 
ATOM   3413 O  OD1 . ASP A 1 424 ? -32.365 32.248 19.425  1.00 52.19  ? 424 ASP A OD1 1 
ATOM   3414 O  OD2 . ASP A 1 424 ? -33.865 33.676 18.693  1.00 50.72  ? 424 ASP A OD2 1 
ATOM   3415 N  N   . LEU A 1 425 ? -28.068 34.584 19.168  1.00 51.00  ? 425 LEU A N   1 
ATOM   3416 C  CA  . LEU A 1 425 ? -26.878 35.411 19.042  1.00 51.60  ? 425 LEU A CA  1 
ATOM   3417 C  C   . LEU A 1 425 ? -26.188 35.140 17.713  1.00 53.11  ? 425 LEU A C   1 
ATOM   3418 O  O   . LEU A 1 425 ? -26.337 34.071 17.114  1.00 51.86  ? 425 LEU A O   1 
ATOM   3419 C  CB  . LEU A 1 425 ? -25.896 35.157 20.195  1.00 51.03  ? 425 LEU A CB  1 
ATOM   3420 C  CG  . LEU A 1 425 ? -26.416 35.413 21.611  1.00 48.02  ? 425 LEU A CG  1 
ATOM   3421 C  CD1 . LEU A 1 425 ? -25.389 34.984 22.646  1.00 49.21  ? 425 LEU A CD1 1 
ATOM   3422 C  CD2 . LEU A 1 425 ? -26.775 36.878 21.783  1.00 48.10  ? 425 LEU A CD2 1 
ATOM   3423 N  N   . VAL A 1 426 ? -25.424 36.132 17.261  1.00 48.96  ? 426 VAL A N   1 
ATOM   3424 C  CA  . VAL A 1 426 ? -24.584 36.012 16.075  1.00 53.09  ? 426 VAL A CA  1 
ATOM   3425 C  C   . VAL A 1 426 ? -23.276 36.741 16.347  1.00 54.46  ? 426 VAL A C   1 
ATOM   3426 O  O   . VAL A 1 426 ? -23.280 37.894 16.791  1.00 49.00  ? 426 VAL A O   1 
ATOM   3427 C  CB  . VAL A 1 426 ? -25.273 36.571 14.813  1.00 54.95  ? 426 VAL A CB  1 
ATOM   3428 C  CG1 . VAL A 1 426 ? -25.909 37.917 15.101  1.00 54.21  ? 426 VAL A CG1 1 
ATOM   3429 C  CG2 . VAL A 1 426 ? -24.275 36.686 13.668  1.00 53.64  ? 426 VAL A CG2 1 
ATOM   3430 N  N   . LEU A 1 427 ? -22.160 36.065 16.094  1.00 54.75  ? 427 LEU A N   1 
ATOM   3431 C  CA  . LEU A 1 427 ? -20.824 36.605 16.319  1.00 52.76  ? 427 LEU A CA  1 
ATOM   3432 C  C   . LEU A 1 427 ? -20.166 36.813 14.961  1.00 59.26  ? 427 LEU A C   1 
ATOM   3433 O  O   . LEU A 1 427 ? -19.881 35.843 14.251  1.00 56.62  ? 427 LEU A O   1 
ATOM   3434 C  CB  . LEU A 1 427 ? -20.004 35.657 17.191  1.00 52.74  ? 427 LEU A CB  1 
ATOM   3435 C  CG  . LEU A 1 427 ? -18.537 36.001 17.444  1.00 51.98  ? 427 LEU A CG  1 
ATOM   3436 C  CD1 . LEU A 1 427 ? -18.407 37.011 18.573  1.00 52.72  ? 427 LEU A CD1 1 
ATOM   3437 C  CD2 . LEU A 1 427 ? -17.743 34.740 17.745  1.00 52.41  ? 427 LEU A CD2 1 
ATOM   3438 N  N   . PHE A 1 428 ? -19.924 38.071 14.597  1.00 58.51  ? 428 PHE A N   1 
ATOM   3439 C  CA  . PHE A 1 428 ? -19.354 38.386 13.296  1.00 61.05  ? 428 PHE A CA  1 
ATOM   3440 C  C   . PHE A 1 428 ? -18.207 39.376 13.433  1.00 61.43  ? 428 PHE A C   1 
ATOM   3441 O  O   . PHE A 1 428 ? -18.159 40.181 14.368  1.00 55.72  ? 428 PHE A O   1 
ATOM   3442 C  CB  . PHE A 1 428 ? -20.418 38.944 12.330  1.00 62.57  ? 428 PHE A CB  1 
ATOM   3443 C  CG  . PHE A 1 428 ? -20.968 40.286 12.727  1.00 54.40  ? 428 PHE A CG  1 
ATOM   3444 C  CD1 . PHE A 1 428 ? -22.028 40.381 13.614  1.00 58.59  ? 428 PHE A CD1 1 
ATOM   3445 C  CD2 . PHE A 1 428 ? -20.441 41.451 12.194  1.00 54.86  ? 428 PHE A CD2 1 
ATOM   3446 C  CE1 . PHE A 1 428 ? -22.541 41.614 13.972  1.00 54.86  ? 428 PHE A CE1 1 
ATOM   3447 C  CE2 . PHE A 1 428 ? -20.950 42.685 12.548  1.00 54.16  ? 428 PHE A CE2 1 
ATOM   3448 C  CZ  . PHE A 1 428 ? -22.002 42.767 13.438  1.00 51.82  ? 428 PHE A CZ  1 
ATOM   3449 N  N   . ASP A 1 429 ? -17.280 39.298 12.484  1.00 62.40  ? 429 ASP A N   1 
ATOM   3450 C  CA  . ASP A 1 429 ? -16.169 40.238 12.407  1.00 60.43  ? 429 ASP A CA  1 
ATOM   3451 C  C   . ASP A 1 429 ? -16.636 41.509 11.709  1.00 60.90  ? 429 ASP A C   1 
ATOM   3452 O  O   . ASP A 1 429 ? -17.015 41.453 10.534  1.00 60.95  ? 429 ASP A O   1 
ATOM   3453 C  CB  . ASP A 1 429 ? -15.002 39.609 11.648  1.00 65.40  ? 429 ASP A CB  1 
ATOM   3454 C  CG  . ASP A 1 429 ? -13.752 40.478 11.648  1.00 66.87  ? 429 ASP A CG  1 
ATOM   3455 O  OD1 . ASP A 1 429 ? -13.785 41.607 12.180  1.00 66.16  ? 429 ASP A OD1 1 
ATOM   3456 O  OD2 . ASP A 1 429 ? -12.721 40.021 11.112  1.00 66.33  ? 429 ASP A OD2 1 
ATOM   3457 N  N   . PRO A 1 430 ? -16.629 42.663 12.383  1.00 60.66  ? 430 PRO A N   1 
ATOM   3458 C  CA  . PRO A 1 430 ? -17.126 43.888 11.736  1.00 60.83  ? 430 PRO A CA  1 
ATOM   3459 C  C   . PRO A 1 430 ? -16.223 44.409 10.631  1.00 64.57  ? 430 PRO A C   1 
ATOM   3460 O  O   . PRO A 1 430 ? -16.668 45.251 9.842   1.00 61.48  ? 430 PRO A O   1 
ATOM   3461 C  CB  . PRO A 1 430 ? -17.215 44.885 12.898  1.00 59.43  ? 430 PRO A CB  1 
ATOM   3462 C  CG  . PRO A 1 430 ? -16.193 44.402 13.873  1.00 58.16  ? 430 PRO A CG  1 
ATOM   3463 C  CD  . PRO A 1 430 ? -16.213 42.902 13.775  1.00 59.95  ? 430 PRO A CD  1 
ATOM   3464 N  N   . GLN A 1 431 ? -14.978 43.942 10.545  1.00 66.30  ? 431 GLN A N   1 
ATOM   3465 C  CA  . GLN A 1 431 ? -14.057 44.421 9.523   1.00 66.09  ? 431 GLN A CA  1 
ATOM   3466 C  C   . GLN A 1 431 ? -14.106 43.607 8.238   1.00 67.28  ? 431 GLN A C   1 
ATOM   3467 O  O   . GLN A 1 431 ? -13.687 44.111 7.189   1.00 66.73  ? 431 GLN A O   1 
ATOM   3468 C  CB  . GLN A 1 431 ? -12.621 44.427 10.061  1.00 67.06  ? 431 GLN A CB  1 
ATOM   3469 C  CG  . GLN A 1 431 ? -12.328 45.538 11.060  1.00 70.74  ? 431 GLN A CG  1 
ATOM   3470 C  CD  . GLN A 1 431 ? -10.902 45.495 11.584  1.00 81.77  ? 431 GLN A CD  1 
ATOM   3471 O  OE1 . GLN A 1 431 ? -10.223 44.473 11.488  1.00 80.17  ? 431 GLN A OE1 1 
ATOM   3472 N  NE2 . GLN A 1 431 ? -10.442 46.611 12.139  1.00 81.78  ? 431 GLN A NE2 1 
ATOM   3473 N  N   . THR A 1 432 ? -14.604 42.370 8.287   1.00 65.82  ? 432 THR A N   1 
ATOM   3474 C  CA  . THR A 1 432 ? -14.616 41.497 7.121   1.00 67.86  ? 432 THR A CA  1 
ATOM   3475 C  C   . THR A 1 432 ? -16.009 41.049 6.704   1.00 67.13  ? 432 THR A C   1 
ATOM   3476 O  O   . THR A 1 432 ? -16.137 40.377 5.674   1.00 76.43  ? 432 THR A O   1 
ATOM   3477 C  CB  . THR A 1 432 ? -13.751 40.253 7.373   1.00 66.12  ? 432 THR A CB  1 
ATOM   3478 O  OG1 . THR A 1 432 ? -14.385 39.418 8.350   1.00 71.38  ? 432 THR A OG1 1 
ATOM   3479 C  CG2 . THR A 1 432 ? -12.372 40.654 7.874   1.00 66.79  ? 432 THR A CG2 1 
ATOM   3480 N  N   . VAL A 1 433 ? -17.050 41.387 7.466   1.00 65.18  ? 433 VAL A N   1 
ATOM   3481 C  CA  . VAL A 1 433 ? -18.396 40.956 7.109   1.00 67.00  ? 433 VAL A CA  1 
ATOM   3482 C  C   . VAL A 1 433 ? -18.803 41.606 5.794   1.00 72.00  ? 433 VAL A C   1 
ATOM   3483 O  O   . VAL A 1 433 ? -18.656 42.820 5.605   1.00 73.71  ? 433 VAL A O   1 
ATOM   3484 C  CB  . VAL A 1 433 ? -19.385 41.281 8.240   1.00 63.78  ? 433 VAL A CB  1 
ATOM   3485 C  CG1 . VAL A 1 433 ? -19.317 42.755 8.624   1.00 62.15  ? 433 VAL A CG1 1 
ATOM   3486 C  CG2 . VAL A 1 433 ? -20.802 40.891 7.839   1.00 61.81  ? 433 VAL A CG2 1 
ATOM   3487 N  N   . ARG A 1 434 ? -19.295 40.790 4.866   1.00 65.16  ? 434 ARG A N   1 
ATOM   3488 C  CA  . ARG A 1 434 ? -19.747 41.296 3.579   1.00 69.08  ? 434 ARG A CA  1 
ATOM   3489 C  C   . ARG A 1 434 ? -20.633 40.249 2.925   1.00 71.41  ? 434 ARG A C   1 
ATOM   3490 O  O   . ARG A 1 434 ? -20.561 39.058 3.242   1.00 69.51  ? 434 ARG A O   1 
ATOM   3491 C  CB  . ARG A 1 434 ? -18.574 41.642 2.656   1.00 73.90  ? 434 ARG A CB  1 
ATOM   3492 C  CG  . ARG A 1 434 ? -18.044 40.452 1.873   1.00 76.39  ? 434 ARG A CG  1 
ATOM   3493 C  CD  . ARG A 1 434 ? -17.027 40.883 0.834   1.00 90.28  ? 434 ARG A CD  1 
ATOM   3494 N  NE  . ARG A 1 434 ? -16.727 39.821 -0.119  1.00 100.45 ? 434 ARG A NE  1 
ATOM   3495 C  CZ  . ARG A 1 434 ? -15.723 38.963 0.002   1.00 95.23  ? 434 ARG A CZ  1 
ATOM   3496 N  NH1 . ARG A 1 434 ? -14.903 39.001 1.039   1.00 98.01  ? 434 ARG A NH1 1 
ATOM   3497 N  NH2 . ARG A 1 434 ? -15.535 38.048 -0.944  1.00 96.17  ? 434 ARG A NH2 1 
ATOM   3498 N  N   . ASP A 1 435 ? -21.472 40.714 2.004   1.00 68.02  ? 435 ASP A N   1 
ATOM   3499 C  CA  . ASP A 1 435 ? -22.282 39.819 1.192   1.00 65.44  ? 435 ASP A CA  1 
ATOM   3500 C  C   . ASP A 1 435 ? -21.457 39.343 0.002   1.00 70.67  ? 435 ASP A C   1 
ATOM   3501 O  O   . ASP A 1 435 ? -20.987 40.156 -0.802  1.00 73.20  ? 435 ASP A O   1 
ATOM   3502 C  CB  . ASP A 1 435 ? -23.556 40.520 0.727   1.00 62.82  ? 435 ASP A CB  1 
ATOM   3503 C  CG  . ASP A 1 435 ? -23.278 41.847 0.047   1.00 68.65  ? 435 ASP A CG  1 
ATOM   3504 O  OD1 . ASP A 1 435 ? -22.391 42.583 0.526   1.00 70.03  ? 435 ASP A OD1 1 
ATOM   3505 O  OD2 . ASP A 1 435 ? -23.943 42.151 -0.966  1.00 69.71  ? 435 ASP A OD2 1 
ATOM   3506 N  N   . VAL A 1 436 ? -21.264 38.029 -0.099  1.00 76.39  ? 436 VAL A N   1 
ATOM   3507 C  CA  . VAL A 1 436 ? -20.545 37.464 -1.233  1.00 75.27  ? 436 VAL A CA  1 
ATOM   3508 C  C   . VAL A 1 436 ? -21.473 37.183 -2.409  1.00 77.57  ? 436 VAL A C   1 
ATOM   3509 O  O   . VAL A 1 436 ? -21.000 37.062 -3.549  1.00 79.36  ? 436 VAL A O   1 
ATOM   3510 C  CB  . VAL A 1 436 ? -19.801 36.184 -0.807  1.00 77.23  ? 436 VAL A CB  1 
ATOM   3511 C  CG1 . VAL A 1 436 ? -18.773 35.778 -1.852  1.00 80.12  ? 436 VAL A CG1 1 
ATOM   3512 C  CG2 . VAL A 1 436 ? -19.135 36.390 0.543   1.00 76.74  ? 436 VAL A CG2 1 
ATOM   3513 N  N   . ALA A 1 437 ? -22.779 37.099 -2.170  1.00 70.28  ? 437 ALA A N   1 
ATOM   3514 C  CA  . ALA A 1 437 ? -23.727 36.807 -3.234  1.00 75.17  ? 437 ALA A CA  1 
ATOM   3515 C  C   . ALA A 1 437 ? -23.758 37.936 -4.256  1.00 77.26  ? 437 ALA A C   1 
ATOM   3516 O  O   . ALA A 1 437 ? -23.897 39.111 -3.901  1.00 76.71  ? 437 ALA A O   1 
ATOM   3517 C  CB  . ALA A 1 437 ? -25.121 36.589 -2.649  1.00 71.19  ? 437 ALA A CB  1 
ATOM   3518 N  N   . SER A 1 438 ? -23.623 37.574 -5.525  1.00 76.34  ? 438 SER A N   1 
ATOM   3519 C  CA  . SER A 1 438 ? -23.735 38.502 -6.638  1.00 78.06  ? 438 SER A CA  1 
ATOM   3520 C  C   . SER A 1 438 ? -24.955 38.135 -7.475  1.00 80.03  ? 438 SER A C   1 
ATOM   3521 O  O   . SER A 1 438 ? -25.641 37.143 -7.218  1.00 82.94  ? 438 SER A O   1 
ATOM   3522 C  CB  . SER A 1 438 ? -22.460 38.487 -7.484  1.00 82.23  ? 438 SER A CB  1 
ATOM   3523 O  OG  . SER A 1 438 ? -22.306 37.247 -8.152  1.00 84.28  ? 438 SER A OG  1 
ATOM   3524 N  N   . PHE A 1 439 ? -25.230 38.954 -8.490  1.00 77.84  ? 439 PHE A N   1 
ATOM   3525 C  CA  . PHE A 1 439 ? -26.321 38.629 -9.401  1.00 80.76  ? 439 PHE A CA  1 
ATOM   3526 C  C   . PHE A 1 439 ? -25.956 37.473 -10.322 1.00 84.31  ? 439 PHE A C   1 
ATOM   3527 O  O   . PHE A 1 439 ? -26.842 36.735 -10.768 1.00 81.53  ? 439 PHE A O   1 
ATOM   3528 C  CB  . PHE A 1 439 ? -26.718 39.862 -10.214 1.00 79.07  ? 439 PHE A CB  1 
ATOM   3529 C  CG  . PHE A 1 439 ? -27.437 40.908 -9.413  1.00 77.45  ? 439 PHE A CG  1 
ATOM   3530 C  CD1 . PHE A 1 439 ? -28.799 40.806 -9.183  1.00 75.16  ? 439 PHE A CD1 1 
ATOM   3531 C  CD2 . PHE A 1 439 ? -26.753 41.992 -8.889  1.00 77.25  ? 439 PHE A CD2 1 
ATOM   3532 C  CE1 . PHE A 1 439 ? -29.467 41.765 -8.445  1.00 73.99  ? 439 PHE A CE1 1 
ATOM   3533 C  CE2 . PHE A 1 439 ? -27.415 42.956 -8.150  1.00 76.95  ? 439 PHE A CE2 1 
ATOM   3534 C  CZ  . PHE A 1 439 ? -28.774 42.842 -7.929  1.00 73.05  ? 439 PHE A CZ  1 
ATOM   3535 N  N   . SER A 1 440 ? -24.666 37.297 -10.615 1.00 82.71  ? 440 SER A N   1 
ATOM   3536 C  CA  . SER A 1 440 ? -24.246 36.174 -11.443 1.00 84.64  ? 440 SER A CA  1 
ATOM   3537 C  C   . SER A 1 440 ? -24.024 34.911 -10.622 1.00 88.07  ? 440 SER A C   1 
ATOM   3538 O  O   . SER A 1 440 ? -24.236 33.803 -11.129 1.00 88.10  ? 440 SER A O   1 
ATOM   3539 C  CB  . SER A 1 440 ? -22.974 36.535 -12.211 1.00 86.72  ? 440 SER A CB  1 
ATOM   3540 O  OG  . SER A 1 440 ? -21.930 36.909 -11.328 1.00 96.85  ? 440 SER A OG  1 
ATOM   3541 N  N   . ASP A 1 441 ? -23.613 35.055 -9.364  1.00 85.44  ? 441 ASP A N   1 
ATOM   3542 C  CA  . ASP A 1 441 ? -23.370 33.930 -8.460  1.00 84.28  ? 441 ASP A CA  1 
ATOM   3543 C  C   . ASP A 1 441 ? -24.117 34.208 -7.162  1.00 84.18  ? 441 ASP A C   1 
ATOM   3544 O  O   . ASP A 1 441 ? -23.543 34.731 -6.196  1.00 85.10  ? 441 ASP A O   1 
ATOM   3545 C  CB  . ASP A 1 441 ? -21.876 33.735 -8.207  1.00 86.64  ? 441 ASP A CB  1 
ATOM   3546 C  CG  . ASP A 1 441 ? -21.525 32.302 -7.866  1.00 92.24  ? 441 ASP A CG  1 
ATOM   3547 O  OD1 . ASP A 1 441 ? -20.322 32.011 -7.696  1.00 91.15  ? 441 ASP A OD1 1 
ATOM   3548 O  OD2 . ASP A 1 441 ? -22.449 31.465 -7.791  1.00 107.33 ? 441 ASP A OD2 1 
ATOM   3549 N  N   . PRO A 1 442 ? -25.407 33.867 -7.100  1.00 88.65  ? 442 PRO A N   1 
ATOM   3550 C  CA  . PRO A 1 442 ? -26.231 34.291 -5.958  1.00 84.51  ? 442 PRO A CA  1 
ATOM   3551 C  C   . PRO A 1 442 ? -26.192 33.349 -4.763  1.00 85.85  ? 442 PRO A C   1 
ATOM   3552 O  O   . PRO A 1 442 ? -26.189 33.801 -3.615  1.00 86.98  ? 442 PRO A O   1 
ATOM   3553 C  CB  . PRO A 1 442 ? -27.636 34.352 -6.564  1.00 84.36  ? 442 PRO A CB  1 
ATOM   3554 C  CG  . PRO A 1 442 ? -27.621 33.269 -7.603  1.00 84.09  ? 442 PRO A CG  1 
ATOM   3555 C  CD  . PRO A 1 442 ? -26.212 33.223 -8.154  1.00 85.73  ? 442 PRO A CD  1 
ATOM   3556 N  N   . LYS A 1 443 ? -26.173 32.042 -5.012  1.00 91.13  ? 443 LYS A N   1 
ATOM   3557 C  CA  . LYS A 1 443 ? -26.295 31.057 -3.937  1.00 95.03  ? 443 LYS A CA  1 
ATOM   3558 C  C   . LYS A 1 443 ? -24.914 30.765 -3.346  1.00 87.33  ? 443 LYS A C   1 
ATOM   3559 O  O   . LYS A 1 443 ? -24.333 29.692 -3.510  1.00 93.78  ? 443 LYS A O   1 
ATOM   3560 C  CB  . LYS A 1 443 ? -26.977 29.799 -4.453  1.00 99.12  ? 443 LYS A CB  1 
ATOM   3561 C  CG  . LYS A 1 443 ? -28.278 30.089 -5.181  1.00 93.20  ? 443 LYS A CG  1 
ATOM   3562 C  CD  . LYS A 1 443 ? -29.269 28.957 -5.010  1.00 97.99  ? 443 LYS A CD  1 
ATOM   3563 C  CE  . LYS A 1 443 ? -29.381 28.120 -6.268  1.00 97.90  ? 443 LYS A CE  1 
ATOM   3564 N  NZ  . LYS A 1 443 ? -30.066 26.828 -5.992  1.00 97.21  ? 443 LYS A NZ  1 
ATOM   3565 N  N   . ARG A 1 444 ? -24.400 31.765 -2.625  1.00 80.97  ? 444 ARG A N   1 
ATOM   3566 C  CA  . ARG A 1 444 ? -23.051 31.739 -2.079  1.00 78.25  ? 444 ARG A CA  1 
ATOM   3567 C  C   . ARG A 1 444 ? -23.084 32.273 -0.649  1.00 77.35  ? 444 ARG A C   1 
ATOM   3568 O  O   . ARG A 1 444 ? -23.724 33.311 -0.393  1.00 76.36  ? 444 ARG A O   1 
ATOM   3569 C  CB  . ARG A 1 444 ? -22.111 32.577 -2.949  1.00 81.21  ? 444 ARG A CB  1 
ATOM   3570 C  CG  . ARG A 1 444 ? -20.653 32.161 -2.906  1.00 84.82  ? 444 ARG A CG  1 
ATOM   3571 C  CD  . ARG A 1 444 ? -20.073 32.130 -4.312  1.00 87.32  ? 444 ARG A CD  1 
ATOM   3572 N  NE  . ARG A 1 444 ? -20.397 33.338 -5.063  1.00 86.34  ? 444 ARG A NE  1 
ATOM   3573 C  CZ  . ARG A 1 444 ? -19.554 34.338 -5.277  1.00 85.87  ? 444 ARG A CZ  1 
ATOM   3574 N  NH1 . ARG A 1 444 ? -18.310 34.302 -4.827  1.00 91.99  ? 444 ARG A NH1 1 
ATOM   3575 N  NH2 . ARG A 1 444 ? -19.967 35.399 -5.964  1.00 82.05  ? 444 ARG A NH2 1 
ATOM   3576 N  N   . PRO A 1 445 ? -22.420 31.610 0.295   1.00 77.74  ? 445 PRO A N   1 
ATOM   3577 C  CA  . PRO A 1 445 ? -22.477 32.058 1.690   1.00 72.25  ? 445 PRO A CA  1 
ATOM   3578 C  C   . PRO A 1 445 ? -21.653 33.317 1.918   1.00 71.86  ? 445 PRO A C   1 
ATOM   3579 O  O   . PRO A 1 445 ? -20.704 33.619 1.192   1.00 76.12  ? 445 PRO A O   1 
ATOM   3580 C  CB  . PRO A 1 445 ? -21.900 30.871 2.466   1.00 73.74  ? 445 PRO A CB  1 
ATOM   3581 C  CG  . PRO A 1 445 ? -20.972 30.223 1.497   1.00 77.62  ? 445 PRO A CG  1 
ATOM   3582 C  CD  . PRO A 1 445 ? -21.604 30.393 0.138   1.00 78.12  ? 445 PRO A CD  1 
ATOM   3583 N  N   . ALA A 1 446 ? -22.032 34.049 2.963   1.00 69.73  ? 446 ALA A N   1 
ATOM   3584 C  CA  . ALA A 1 446 ? -21.403 35.320 3.287   1.00 71.71  ? 446 ALA A CA  1 
ATOM   3585 C  C   . ALA A 1 446 ? -20.128 35.107 4.102   1.00 76.46  ? 446 ALA A C   1 
ATOM   3586 O  O   . ALA A 1 446 ? -19.862 34.024 4.630   1.00 76.44  ? 446 ALA A O   1 
ATOM   3587 C  CB  . ALA A 1 446 ? -22.376 36.218 4.049   1.00 66.27  ? 446 ALA A CB  1 
ATOM   3588 N  N   . ASP A 1 447 ? -19.334 36.170 4.201   1.00 71.48  ? 447 ASP A N   1 
ATOM   3589 C  CA  . ASP A 1 447 ? -18.093 36.175 4.960   1.00 74.73  ? 447 ASP A CA  1 
ATOM   3590 C  C   . ASP A 1 447 ? -18.253 37.013 6.222   1.00 71.15  ? 447 ASP A C   1 
ATOM   3591 O  O   . ASP A 1 447 ? -19.150 37.854 6.329   1.00 72.63  ? 447 ASP A O   1 
ATOM   3592 C  CB  . ASP A 1 447 ? -16.934 36.717 4.115   1.00 77.16  ? 447 ASP A CB  1 
ATOM   3593 C  CG  . ASP A 1 447 ? -16.521 35.764 3.009   1.00 82.56  ? 447 ASP A CG  1 
ATOM   3594 O  OD1 . ASP A 1 447 ? -16.996 34.609 3.008   1.00 81.70  ? 447 ASP A OD1 1 
ATOM   3595 O  OD2 . ASP A 1 447 ? -15.720 36.171 2.141   1.00 82.71  ? 447 ASP A OD2 1 
ATOM   3596 N  N   . GLY A 1 448 ? -17.365 36.772 7.186   1.00 70.22  ? 448 GLY A N   1 
ATOM   3597 C  CA  . GLY A 1 448 ? -17.378 37.479 8.445   1.00 65.41  ? 448 GLY A CA  1 
ATOM   3598 C  C   . GLY A 1 448 ? -18.257 36.868 9.515   1.00 64.35  ? 448 GLY A C   1 
ATOM   3599 O  O   . GLY A 1 448 ? -18.025 37.119 10.702  1.00 67.22  ? 448 GLY A O   1 
ATOM   3600 N  N   . ILE A 1 449 ? -19.257 36.078 9.134   1.00 66.18  ? 449 ILE A N   1 
ATOM   3601 C  CA  . ILE A 1 449 ? -20.135 35.418 10.097  1.00 63.25  ? 449 ILE A CA  1 
ATOM   3602 C  C   . ILE A 1 449 ? -19.363 34.257 10.714  1.00 63.06  ? 449 ILE A C   1 
ATOM   3603 O  O   . ILE A 1 449 ? -19.043 33.279 10.033  1.00 71.45  ? 449 ILE A O   1 
ATOM   3604 C  CB  . ILE A 1 449 ? -21.431 34.936 9.438   1.00 64.67  ? 449 ILE A CB  1 
ATOM   3605 C  CG1 . ILE A 1 449 ? -22.090 36.079 8.664   1.00 62.54  ? 449 ILE A CG1 1 
ATOM   3606 C  CG2 . ILE A 1 449 ? -22.386 34.384 10.484  1.00 60.96  ? 449 ILE A CG2 1 
ATOM   3607 C  CD1 . ILE A 1 449 ? -22.445 37.271 9.523   1.00 59.17  ? 449 ILE A CD1 1 
ATOM   3608 N  N   . GLU A 1 450 ? -19.064 34.360 12.008  1.00 60.55  ? 450 GLU A N   1 
ATOM   3609 C  CA  . GLU A 1 450 ? -18.223 33.379 12.681  1.00 65.40  ? 450 GLU A CA  1 
ATOM   3610 C  C   . GLU A 1 450 ? -19.001 32.416 13.566  1.00 64.09  ? 450 GLU A C   1 
ATOM   3611 O  O   . GLU A 1 450 ? -18.541 31.290 13.784  1.00 64.15  ? 450 GLU A O   1 
ATOM   3612 C  CB  . GLU A 1 450 ? -17.155 34.091 13.518  1.00 60.17  ? 450 GLU A CB  1 
ATOM   3613 C  CG  . GLU A 1 450 ? -16.406 35.160 12.739  1.00 63.82  ? 450 GLU A CG  1 
ATOM   3614 C  CD  . GLU A 1 450 ? -14.963 35.308 13.174  1.00 71.33  ? 450 GLU A CD  1 
ATOM   3615 O  OE1 . GLU A 1 450 ? -14.671 35.093 14.369  1.00 70.82  ? 450 GLU A OE1 1 
ATOM   3616 O  OE2 . GLU A 1 450 ? -14.117 35.634 12.313  1.00 75.98  ? 450 GLU A OE2 1 
ATOM   3617 N  N   . ALA A 1 451 ? -20.162 32.822 14.075  1.00 60.54  ? 451 ALA A N   1 
ATOM   3618 C  CA  . ALA A 1 451 ? -20.966 31.946 14.914  1.00 56.37  ? 451 ALA A CA  1 
ATOM   3619 C  C   . ALA A 1 451 ? -22.406 32.434 14.907  1.00 53.68  ? 451 ALA A C   1 
ATOM   3620 O  O   . ALA A 1 451 ? -22.659 33.641 14.925  1.00 55.17  ? 451 ALA A O   1 
ATOM   3621 C  CB  . ALA A 1 451 ? -20.429 31.895 16.349  1.00 55.61  ? 451 ALA A CB  1 
ATOM   3622 N  N   . VAL A 1 452 ? -23.341 31.486 14.873  1.00 58.16  ? 452 VAL A N   1 
ATOM   3623 C  CA  . VAL A 1 452 ? -24.769 31.765 14.956  1.00 58.60  ? 452 VAL A CA  1 
ATOM   3624 C  C   . VAL A 1 452 ? -25.376 30.801 15.965  1.00 58.17  ? 452 VAL A C   1 
ATOM   3625 O  O   . VAL A 1 452 ? -25.184 29.585 15.859  1.00 59.80  ? 452 VAL A O   1 
ATOM   3626 C  CB  . VAL A 1 452 ? -25.470 31.628 13.590  1.00 60.21  ? 452 VAL A CB  1 
ATOM   3627 C  CG1 . VAL A 1 452 ? -26.965 31.868 13.736  1.00 61.37  ? 452 VAL A CG1 1 
ATOM   3628 C  CG2 . VAL A 1 452 ? -24.870 32.592 12.578  1.00 54.03  ? 452 VAL A CG2 1 
ATOM   3629 N  N   . MET A 1 453 ? -26.101 31.339 16.941  1.00 54.39  ? 453 MET A N   1 
ATOM   3630 C  CA  . MET A 1 453 ? -26.696 30.545 18.007  1.00 54.19  ? 453 MET A CA  1 
ATOM   3631 C  C   . MET A 1 453 ? -28.202 30.762 18.015  1.00 53.74  ? 453 MET A C   1 
ATOM   3632 O  O   . MET A 1 453 ? -28.670 31.904 17.953  1.00 49.30  ? 453 MET A O   1 
ATOM   3633 C  CB  . MET A 1 453 ? -26.092 30.912 19.365  1.00 54.00  ? 453 MET A CB  1 
ATOM   3634 C  CG  . MET A 1 453 ? -25.853 29.720 20.276  1.00 54.72  ? 453 MET A CG  1 
ATOM   3635 S  SD  . MET A 1 453 ? -25.031 30.173 21.814  1.00 56.36  ? 453 MET A SD  1 
ATOM   3636 C  CE  . MET A 1 453 ? -26.224 31.316 22.496  1.00 50.56  ? 453 MET A CE  1 
ATOM   3637 N  N   . VAL A 1 454 ? -28.955 29.667 18.088  1.00 54.22  ? 454 VAL A N   1 
ATOM   3638 C  CA  . VAL A 1 454 ? -30.413 29.696 18.073  1.00 51.65  ? 454 VAL A CA  1 
ATOM   3639 C  C   . VAL A 1 454 ? -30.900 29.003 19.338  1.00 55.65  ? 454 VAL A C   1 
ATOM   3640 O  O   . VAL A 1 454 ? -30.714 27.789 19.499  1.00 56.24  ? 454 VAL A O   1 
ATOM   3641 C  CB  . VAL A 1 454 ? -30.991 29.023 16.821  1.00 52.14  ? 454 VAL A CB  1 
ATOM   3642 C  CG1 . VAL A 1 454 ? -32.510 29.111 16.823  1.00 53.99  ? 454 VAL A CG1 1 
ATOM   3643 C  CG2 . VAL A 1 454 ? -30.414 29.656 15.565  1.00 54.37  ? 454 VAL A CG2 1 
ATOM   3644 N  N   . ASN A 1 455 ? -31.524 29.772 20.234  1.00 51.96  ? 455 ASN A N   1 
ATOM   3645 C  CA  . ASN A 1 455 ? -32.057 29.251 21.495  1.00 51.87  ? 455 ASN A CA  1 
ATOM   3646 C  C   . ASN A 1 455 ? -30.976 28.537 22.305  1.00 51.94  ? 455 ASN A C   1 
ATOM   3647 O  O   . ASN A 1 455 ? -31.203 27.467 22.873  1.00 52.02  ? 455 ASN A O   1 
ATOM   3648 C  CB  . ASN A 1 455 ? -33.254 28.330 21.251  1.00 51.21  ? 455 ASN A CB  1 
ATOM   3649 C  CG  . ASN A 1 455 ? -34.421 29.050 20.605  1.00 53.28  ? 455 ASN A CG  1 
ATOM   3650 O  OD1 . ASN A 1 455 ? -34.753 30.176 20.975  1.00 52.20  ? 455 ASN A OD1 1 
ATOM   3651 N  ND2 . ASN A 1 455 ? -35.047 28.404 19.628  1.00 54.36  ? 455 ASN A ND2 1 
ATOM   3652 N  N   . GLY A 1 456 ? -29.786 29.133 22.352  1.00 52.34  ? 456 GLY A N   1 
ATOM   3653 C  CA  . GLY A 1 456 ? -28.683 28.582 23.108  1.00 53.63  ? 456 GLY A CA  1 
ATOM   3654 C  C   . GLY A 1 456 ? -27.943 27.442 22.444  1.00 54.00  ? 456 GLY A C   1 
ATOM   3655 O  O   . GLY A 1 456 ? -26.998 26.912 23.041  1.00 51.67  ? 456 GLY A O   1 
ATOM   3656 N  N   . VAL A 1 457 ? -28.332 27.047 21.235  1.00 51.71  ? 457 VAL A N   1 
ATOM   3657 C  CA  . VAL A 1 457 ? -27.692 25.955 20.511  1.00 54.79  ? 457 VAL A CA  1 
ATOM   3658 C  C   . VAL A 1 457 ? -26.881 26.554 19.371  1.00 58.28  ? 457 VAL A C   1 
ATOM   3659 O  O   . VAL A 1 457 ? -27.436 27.215 18.484  1.00 59.85  ? 457 VAL A O   1 
ATOM   3660 C  CB  . VAL A 1 457 ? -28.720 24.944 19.983  1.00 57.34  ? 457 VAL A CB  1 
ATOM   3661 C  CG1 . VAL A 1 457 ? -28.029 23.861 19.168  1.00 56.10  ? 457 VAL A CG1 1 
ATOM   3662 C  CG2 . VAL A 1 457 ? -29.502 24.333 21.135  1.00 55.97  ? 457 VAL A CG2 1 
ATOM   3663 N  N   . MET A 1 458 ? -25.569 26.327 19.395  1.00 56.35  ? 458 MET A N   1 
ATOM   3664 C  CA  . MET A 1 458 ? -24.690 26.791 18.325  1.00 57.38  ? 458 MET A CA  1 
ATOM   3665 C  C   . MET A 1 458 ? -25.058 26.071 17.033  1.00 57.65  ? 458 MET A C   1 
ATOM   3666 O  O   . MET A 1 458 ? -24.825 24.866 16.897  1.00 59.09  ? 458 MET A O   1 
ATOM   3667 C  CB  . MET A 1 458 ? -23.230 26.546 18.697  1.00 55.02  ? 458 MET A CB  1 
ATOM   3668 C  CG  . MET A 1 458 ? -22.234 27.275 17.811  1.00 55.59  ? 458 MET A CG  1 
ATOM   3669 S  SD  . MET A 1 458 ? -22.277 29.065 18.028  1.00 59.02  ? 458 MET A SD  1 
ATOM   3670 C  CE  . MET A 1 458 ? -21.442 29.243 19.606  1.00 58.99  ? 458 MET A CE  1 
ATOM   3671 N  N   . SER A 1 459 ? -25.633 26.809 16.080  1.00 60.20  ? 459 SER A N   1 
ATOM   3672 C  CA  . SER A 1 459 ? -26.219 26.212 14.888  1.00 63.32  ? 459 SER A CA  1 
ATOM   3673 C  C   . SER A 1 459 ? -25.416 26.429 13.614  1.00 64.84  ? 459 SER A C   1 
ATOM   3674 O  O   . SER A 1 459 ? -25.656 25.720 12.632  1.00 66.51  ? 459 SER A O   1 
ATOM   3675 C  CB  . SER A 1 459 ? -27.638 26.756 14.668  1.00 59.14  ? 459 SER A CB  1 
ATOM   3676 O  OG  . SER A 1 459 ? -28.468 26.487 15.785  1.00 61.35  ? 459 SER A OG  1 
ATOM   3677 N  N   . TYR A 1 460 ? -24.482 27.377 13.596  1.00 65.08  ? 460 TYR A N   1 
ATOM   3678 C  CA  . TYR A 1 460 ? -23.733 27.677 12.382  1.00 66.58  ? 460 TYR A CA  1 
ATOM   3679 C  C   . TYR A 1 460 ? -22.373 28.242 12.754  1.00 70.48  ? 460 TYR A C   1 
ATOM   3680 O  O   . TYR A 1 460 ? -22.281 29.142 13.594  1.00 66.33  ? 460 TYR A O   1 
ATOM   3681 C  CB  . TYR A 1 460 ? -24.501 28.666 11.496  1.00 68.92  ? 460 TYR A CB  1 
ATOM   3682 C  CG  . TYR A 1 460 ? -23.793 29.035 10.210  1.00 69.67  ? 460 TYR A CG  1 
ATOM   3683 C  CD1 . TYR A 1 460 ? -23.830 28.192 9.107   1.00 73.17  ? 460 TYR A CD1 1 
ATOM   3684 C  CD2 . TYR A 1 460 ? -23.100 30.233 10.095  1.00 71.54  ? 460 TYR A CD2 1 
ATOM   3685 C  CE1 . TYR A 1 460 ? -23.188 28.527 7.929   1.00 74.40  ? 460 TYR A CE1 1 
ATOM   3686 C  CE2 . TYR A 1 460 ? -22.455 30.577 8.921   1.00 69.85  ? 460 TYR A CE2 1 
ATOM   3687 C  CZ  . TYR A 1 460 ? -22.502 29.720 7.842   1.00 75.06  ? 460 TYR A CZ  1 
ATOM   3688 O  OH  . TYR A 1 460 ? -21.862 30.058 6.672   1.00 76.42  ? 460 TYR A OH  1 
ATOM   3689 N  N   . GLY A 1 461 ? -21.322 27.713 12.126  1.00 74.06  ? 461 GLY A N   1 
ATOM   3690 C  CA  . GLY A 1 461 ? -19.972 28.179 12.334  1.00 80.10  ? 461 GLY A CA  1 
ATOM   3691 C  C   . GLY A 1 461 ? -19.374 28.763 11.064  1.00 82.68  ? 461 GLY A C   1 
ATOM   3692 O  O   . GLY A 1 461 ? -20.029 28.868 10.023  1.00 88.54  ? 461 GLY A O   1 
ATOM   3693 N  N   . SER A 1 462 ? -18.102 29.147 11.173  1.00 86.51  ? 462 SER A N   1 
ATOM   3694 C  CA  . SER A 1 462 ? -17.374 29.709 10.043  1.00 90.53  ? 462 SER A CA  1 
ATOM   3695 C  C   . SER A 1 462 ? -16.965 28.660 9.019   1.00 98.69  ? 462 SER A C   1 
ATOM   3696 O  O   . SER A 1 462 ? -16.406 29.020 7.979   1.00 93.83  ? 462 SER A O   1 
ATOM   3697 C  CB  . SER A 1 462 ? -16.136 30.461 10.535  1.00 91.13  ? 462 SER A CB  1 
ATOM   3698 O  OG  . SER A 1 462 ? -15.332 29.632 11.354  1.00 100.31 ? 462 SER A OG  1 
ATOM   3699 N  N   . ASP A 1 463 ? -17.221 27.380 9.286   1.00 94.85  ? 463 ASP A N   1 
ATOM   3700 C  CA  . ASP A 1 463 ? -16.972 26.326 8.313   1.00 91.40  ? 463 ASP A CA  1 
ATOM   3701 C  C   . ASP A 1 463 ? -18.096 26.189 7.297   1.00 92.01  ? 463 ASP A C   1 
ATOM   3702 O  O   . ASP A 1 463 ? -18.040 25.287 6.454   1.00 96.59  ? 463 ASP A O   1 
ATOM   3703 C  CB  . ASP A 1 463 ? -16.756 24.990 9.028   1.00 90.29  ? 463 ASP A CB  1 
ATOM   3704 C  CG  . ASP A 1 463 ? -17.923 24.613 9.921   1.00 94.50  ? 463 ASP A CG  1 
ATOM   3705 O  OD1 . ASP A 1 463 ? -18.837 25.445 10.099  1.00 89.24  ? 463 ASP A OD1 1 
ATOM   3706 O  OD2 . ASP A 1 463 ? -17.926 23.479 10.446  1.00 95.19  ? 463 ASP A OD2 1 
ATOM   3707 N  N   . LYS A 1 464 ? -19.110 27.056 7.368   1.00 90.85  ? 464 LYS A N   1 
ATOM   3708 C  CA  . LYS A 1 464 ? -20.239 27.047 6.436   1.00 85.56  ? 464 LYS A CA  1 
ATOM   3709 C  C   . LYS A 1 464 ? -21.007 25.731 6.523   1.00 86.27  ? 464 LYS A C   1 
ATOM   3710 O  O   . LYS A 1 464 ? -21.390 25.141 5.511   1.00 88.32  ? 464 LYS A O   1 
ATOM   3711 C  CB  . LYS A 1 464 ? -19.784 27.333 5.000   1.00 87.51  ? 464 LYS A CB  1 
ATOM   3712 C  CG  . LYS A 1 464 ? -19.562 28.817 4.677   1.00 87.24  ? 464 LYS A CG  1 
ATOM   3713 C  CD  . LYS A 1 464 ? -18.478 29.438 5.551   1.00 92.57  ? 464 LYS A CD  1 
ATOM   3714 C  CE  . LYS A 1 464 ? -18.044 30.809 5.062   1.00 91.05  ? 464 LYS A CE  1 
ATOM   3715 N  NZ  . LYS A 1 464 ? -16.992 31.365 5.958   1.00 85.95  ? 464 LYS A NZ  1 
ATOM   3716 N  N   A LYS A 1 465 ? -21.230 25.264 7.750   0.52 83.37  ? 465 LYS A N   1 
ATOM   3717 N  N   B LYS A 1 465 ? -21.233 25.269 7.752   0.48 83.38  ? 465 LYS A N   1 
ATOM   3718 C  CA  A LYS A 1 465 ? -21.972 24.038 8.001   0.52 82.99  ? 465 LYS A CA  1 
ATOM   3719 C  CA  B LYS A 1 465 ? -21.953 24.035 8.028   0.48 82.99  ? 465 LYS A CA  1 
ATOM   3720 C  C   A LYS A 1 465 ? -22.957 24.275 9.135   0.52 81.84  ? 465 LYS A C   1 
ATOM   3721 C  C   B LYS A 1 465 ? -22.961 24.283 9.140   0.48 81.83  ? 465 LYS A C   1 
ATOM   3722 O  O   A LYS A 1 465 ? -22.631 24.937 10.124  0.52 80.13  ? 465 LYS A O   1 
ATOM   3723 O  O   B LYS A 1 465 ? -22.655 24.964 10.124  0.48 80.13  ? 465 LYS A O   1 
ATOM   3724 C  CB  A LYS A 1 465 ? -21.036 22.873 8.350   0.52 84.17  ? 465 LYS A CB  1 
ATOM   3725 C  CB  B LYS A 1 465 ? -20.991 22.909 8.433   0.48 84.19  ? 465 LYS A CB  1 
ATOM   3726 C  CG  A LYS A 1 465 ? -20.142 22.428 7.204   0.52 85.64  ? 465 LYS A CG  1 
ATOM   3727 C  CG  B LYS A 1 465 ? -21.679 21.640 8.913   0.48 82.95  ? 465 LYS A CG  1 
ATOM   3728 C  CD  A LYS A 1 465 ? -20.965 21.918 6.031   0.52 82.96  ? 465 LYS A CD  1 
ATOM   3729 C  CD  B LYS A 1 465 ? -20.688 20.671 9.535   0.48 81.92  ? 465 LYS A CD  1 
ATOM   3730 C  CE  A LYS A 1 465 ? -20.077 21.501 4.871   0.52 80.62  ? 465 LYS A CE  1 
ATOM   3731 C  CE  B LYS A 1 465 ? -21.400 19.477 10.147  0.48 79.20  ? 465 LYS A CE  1 
ATOM   3732 N  NZ  A LYS A 1 465 ? -19.133 20.416 5.256   0.52 77.83  ? 465 LYS A NZ  1 
ATOM   3733 N  NZ  B LYS A 1 465 ? -20.453 18.553 10.828  0.48 73.67  ? 465 LYS A NZ  1 
ATOM   3734 N  N   . ILE A 1 466 ? -24.160 23.733 8.982   1.00 79.34  ? 466 ILE A N   1 
ATOM   3735 C  CA  . ILE A 1 466 ? -25.215 23.873 9.978   1.00 75.56  ? 466 ILE A CA  1 
ATOM   3736 C  C   . ILE A 1 466 ? -25.082 22.736 10.984  1.00 75.16  ? 466 ILE A C   1 
ATOM   3737 O  O   . ILE A 1 466 ? -25.085 21.559 10.609  1.00 77.03  ? 466 ILE A O   1 
ATOM   3738 C  CB  . ILE A 1 466 ? -26.603 23.876 9.322   1.00 72.62  ? 466 ILE A CB  1 
ATOM   3739 C  CG1 . ILE A 1 466 ? -26.764 25.119 8.444   1.00 72.54  ? 466 ILE A CG1 1 
ATOM   3740 C  CG2 . ILE A 1 466 ? -27.695 23.811 10.380  1.00 69.62  ? 466 ILE A CG2 1 
ATOM   3741 C  CD1 . ILE A 1 466 ? -28.133 25.265 7.826   1.00 68.95  ? 466 ILE A CD1 1 
ATOM   3742 N  N   . THR A 1 467 ? -24.964 23.090 12.265  1.00 71.02  ? 467 THR A N   1 
ATOM   3743 C  CA  . THR A 1 467 ? -24.725 22.120 13.323  1.00 73.21  ? 467 THR A CA  1 
ATOM   3744 C  C   . THR A 1 467 ? -25.855 22.031 14.339  1.00 70.03  ? 467 THR A C   1 
ATOM   3745 O  O   . THR A 1 467 ? -25.737 21.267 15.304  1.00 69.15  ? 467 THR A O   1 
ATOM   3746 C  CB  . THR A 1 467 ? -23.417 22.447 14.058  1.00 74.42  ? 467 THR A CB  1 
ATOM   3747 O  OG1 . THR A 1 467 ? -23.542 23.715 14.715  1.00 67.63  ? 467 THR A OG1 1 
ATOM   3748 C  CG2 . THR A 1 467 ? -22.254 22.503 13.078  1.00 74.25  ? 467 THR A CG2 1 
ATOM   3749 N  N   . GLY A 1 468 ? -26.939 22.782 14.158  1.00 69.72  ? 468 GLY A N   1 
ATOM   3750 C  CA  . GLY A 1 468 ? -28.026 22.771 15.114  1.00 61.80  ? 468 GLY A CA  1 
ATOM   3751 C  C   . GLY A 1 468 ? -29.366 22.922 14.427  1.00 64.64  ? 468 GLY A C   1 
ATOM   3752 O  O   . GLY A 1 468 ? -29.475 23.469 13.326  1.00 66.46  ? 468 GLY A O   1 
ATOM   3753 N  N   . ARG A 1 469 ? -30.398 22.416 15.105  1.00 63.48  ? 469 ARG A N   1 
ATOM   3754 C  CA  A ARG A 1 469 ? -31.774 22.468 14.632  0.42 61.04  ? 469 ARG A CA  1 
ATOM   3755 C  CA  B ARG A 1 469 ? -31.772 22.504 14.623  0.58 61.12  ? 469 ARG A CA  1 
ATOM   3756 C  C   . ARG A 1 469 ? -32.691 22.825 15.805  1.00 60.24  ? 469 ARG A C   1 
ATOM   3757 O  O   . ARG A 1 469 ? -33.619 22.096 16.144  1.00 60.26  ? 469 ARG A O   1 
ATOM   3758 C  CB  A ARG A 1 469 ? -32.193 21.137 14.008  0.42 63.12  ? 469 ARG A CB  1 
ATOM   3759 C  CB  B ARG A 1 469 ? -32.178 21.221 13.900  0.58 63.14  ? 469 ARG A CB  1 
ATOM   3760 C  CG  A ARG A 1 469 ? -31.500 20.780 12.703  0.42 64.32  ? 469 ARG A CG  1 
ATOM   3761 C  CG  B ARG A 1 469 ? -31.738 21.187 12.440  0.58 63.95  ? 469 ARG A CG  1 
ATOM   3762 C  CD  A ARG A 1 469 ? -31.679 19.299 12.386  0.42 68.15  ? 469 ARG A CD  1 
ATOM   3763 C  CD  B ARG A 1 469 ? -31.323 19.793 11.995  0.58 67.37  ? 469 ARG A CD  1 
ATOM   3764 N  NE  A ARG A 1 469 ? -32.044 19.064 10.994  0.42 68.73  ? 469 ARG A NE  1 
ATOM   3765 N  NE  B ARG A 1 469 ? -32.424 18.840 12.056  0.58 68.58  ? 469 ARG A NE  1 
ATOM   3766 C  CZ  A ARG A 1 469 ? -33.289 18.913 10.563  0.42 68.47  ? 469 ARG A CZ  1 
ATOM   3767 C  CZ  B ARG A 1 469 ? -33.297 18.641 11.078  0.58 68.43  ? 469 ARG A CZ  1 
ATOM   3768 N  NH1 A ARG A 1 469 ? -34.319 18.967 11.392  0.42 67.70  ? 469 ARG A NH1 1 
ATOM   3769 N  NH1 B ARG A 1 469 ? -33.233 19.321 9.945   0.58 68.44  ? 469 ARG A NH1 1 
ATOM   3770 N  NH2 A ARG A 1 469 ? -33.507 18.702 9.268   0.42 68.34  ? 469 ARG A NH2 1 
ATOM   3771 N  NH2 B ARG A 1 469 ? -34.260 17.738 11.241  0.58 68.91  ? 469 ARG A NH2 1 
ATOM   3772 N  N   . ALA A 1 470 ? -32.426 23.965 16.446  1.00 60.13  ? 470 ALA A N   1 
ATOM   3773 C  CA  . ALA A 1 470 ? -33.165 24.391 17.629  1.00 56.18  ? 470 ALA A CA  1 
ATOM   3774 C  C   . ALA A 1 470 ? -34.164 25.505 17.331  1.00 57.30  ? 470 ALA A C   1 
ATOM   3775 O  O   . ALA A 1 470 ? -34.488 26.300 18.219  1.00 58.27  ? 470 ALA A O   1 
ATOM   3776 C  CB  . ALA A 1 470 ? -32.197 24.833 18.725  1.00 56.25  ? 470 ALA A CB  1 
ATOM   3777 N  N   . GLY A 1 471 ? -34.662 25.579 16.100  1.00 56.66  ? 471 GLY A N   1 
ATOM   3778 C  CA  . GLY A 1 471 ? -35.679 26.561 15.781  1.00 53.94  ? 471 GLY A CA  1 
ATOM   3779 C  C   . GLY A 1 471 ? -37.012 26.222 16.423  1.00 52.95  ? 471 GLY A C   1 
ATOM   3780 O  O   . GLY A 1 471 ? -37.361 25.059 16.622  1.00 59.01  ? 471 GLY A O   1 
ATOM   3781 N  N   . ARG A 1 472 ? -37.764 27.266 16.761  1.00 50.36  ? 472 ARG A N   1 
ATOM   3782 C  CA  . ARG A 1 472 ? -39.068 27.121 17.387  1.00 54.77  ? 472 ARG A CA  1 
ATOM   3783 C  C   . ARG A 1 472 ? -40.077 28.008 16.672  1.00 55.65  ? 472 ARG A C   1 
ATOM   3784 O  O   . ARG A 1 472 ? -39.720 28.987 16.014  1.00 54.91  ? 472 ARG A O   1 
ATOM   3785 C  CB  . ARG A 1 472 ? -39.029 27.493 18.877  1.00 54.64  ? 472 ARG A CB  1 
ATOM   3786 C  CG  . ARG A 1 472 ? -38.071 26.668 19.717  1.00 54.69  ? 472 ARG A CG  1 
ATOM   3787 C  CD  . ARG A 1 472 ? -37.889 27.290 21.092  1.00 54.99  ? 472 ARG A CD  1 
ATOM   3788 N  NE  . ARG A 1 472 ? -37.002 26.503 21.941  1.00 58.28  ? 472 ARG A NE  1 
ATOM   3789 C  CZ  . ARG A 1 472 ? -36.554 26.897 23.125  1.00 55.80  ? 472 ARG A CZ  1 
ATOM   3790 N  NH1 . ARG A 1 472 ? -36.880 28.076 23.630  1.00 53.54  ? 472 ARG A NH1 1 
ATOM   3791 N  NH2 . ARG A 1 472 ? -35.757 26.091 23.819  1.00 55.03  ? 472 ARG A NH2 1 
ATOM   3792 N  N   . PHE A 1 473 ? -41.352 27.656 16.810  1.00 54.25  ? 473 PHE A N   1 
ATOM   3793 C  CA  . PHE A 1 473 ? -42.416 28.529 16.338  1.00 52.86  ? 473 PHE A CA  1 
ATOM   3794 C  C   . PHE A 1 473 ? -42.667 29.613 17.377  1.00 53.34  ? 473 PHE A C   1 
ATOM   3795 O  O   . PHE A 1 473 ? -42.834 29.320 18.565  1.00 56.11  ? 473 PHE A O   1 
ATOM   3796 C  CB  . PHE A 1 473 ? -43.696 27.741 16.068  1.00 53.35  ? 473 PHE A CB  1 
ATOM   3797 C  CG  . PHE A 1 473 ? -44.819 28.584 15.532  1.00 53.18  ? 473 PHE A CG  1 
ATOM   3798 C  CD1 . PHE A 1 473 ? -44.868 28.924 14.190  1.00 53.63  ? 473 PHE A CD1 1 
ATOM   3799 C  CD2 . PHE A 1 473 ? -45.822 29.042 16.371  1.00 51.96  ? 473 PHE A CD2 1 
ATOM   3800 C  CE1 . PHE A 1 473 ? -45.898 29.702 13.693  1.00 49.86  ? 473 PHE A CE1 1 
ATOM   3801 C  CE2 . PHE A 1 473 ? -46.855 29.818 15.881  1.00 56.89  ? 473 PHE A CE2 1 
ATOM   3802 C  CZ  . PHE A 1 473 ? -46.892 30.149 14.539  1.00 51.67  ? 473 PHE A CZ  1 
ATOM   3803 N  N   . LEU A 1 474 ? -42.683 30.863 16.930  1.00 54.26  ? 474 LEU A N   1 
ATOM   3804 C  CA  . LEU A 1 474 ? -42.835 32.004 17.818  1.00 52.22  ? 474 LEU A CA  1 
ATOM   3805 C  C   . LEU A 1 474 ? -44.268 32.512 17.764  1.00 53.44  ? 474 LEU A C   1 
ATOM   3806 O  O   . LEU A 1 474 ? -44.814 32.739 16.679  1.00 51.38  ? 474 LEU A O   1 
ATOM   3807 C  CB  . LEU A 1 474 ? -41.866 33.122 17.439  1.00 52.20  ? 474 LEU A CB  1 
ATOM   3808 C  CG  . LEU A 1 474 ? -40.388 32.734 17.419  1.00 54.95  ? 474 LEU A CG  1 
ATOM   3809 C  CD1 . LEU A 1 474 ? -39.534 33.969 17.217  1.00 50.17  ? 474 LEU A CD1 1 
ATOM   3810 C  CD2 . LEU A 1 474 ? -40.000 32.007 18.698  1.00 51.20  ? 474 LEU A CD2 1 
ATOM   3811 N  N   . ARG A 1 475 ? -44.871 32.681 18.934  1.00 57.38  ? 475 ARG A N   1 
ATOM   3812 C  CA  . ARG A 1 475 ? -46.202 33.250 19.049  1.00 52.55  ? 475 ARG A CA  1 
ATOM   3813 C  C   . ARG A 1 475 ? -46.104 34.686 19.541  1.00 52.57  ? 475 ARG A C   1 
ATOM   3814 O  O   . ARG A 1 475 ? -45.168 35.052 20.257  1.00 53.01  ? 475 ARG A O   1 
ATOM   3815 C  CB  . ARG A 1 475 ? -47.070 32.421 19.998  1.00 51.16  ? 475 ARG A CB  1 
ATOM   3816 C  CG  . ARG A 1 475 ? -47.204 30.969 19.578  1.00 53.54  ? 475 ARG A CG  1 
ATOM   3817 C  CD  . ARG A 1 475 ? -47.937 30.147 20.622  1.00 60.04  ? 475 ARG A CD  1 
ATOM   3818 N  NE  . ARG A 1 475 ? -47.783 28.717 20.381  1.00 61.28  ? 475 ARG A NE  1 
ATOM   3819 C  CZ  . ARG A 1 475 ? -48.639 27.974 19.693  1.00 63.84  ? 475 ARG A CZ  1 
ATOM   3820 N  NH1 . ARG A 1 475 ? -49.742 28.489 19.175  1.00 65.09  ? 475 ARG A NH1 1 
ATOM   3821 N  NH2 . ARG A 1 475 ? -48.381 26.680 19.521  1.00 63.25  ? 475 ARG A NH2 1 
ATOM   3822 N  N   . ARG A 1 476 ? -47.077 35.500 19.138  1.00 56.85  ? 476 ARG A N   1 
ATOM   3823 C  CA  . ARG A 1 476 ? -47.085 36.904 19.518  1.00 60.00  ? 476 ARG A CA  1 
ATOM   3824 C  C   . ARG A 1 476 ? -47.080 37.044 21.036  1.00 60.91  ? 476 ARG A C   1 
ATOM   3825 O  O   . ARG A 1 476 ? -47.616 36.203 21.763  1.00 67.11  ? 476 ARG A O   1 
ATOM   3826 C  CB  . ARG A 1 476 ? -48.308 37.607 18.927  1.00 60.26  ? 476 ARG A CB  1 
ATOM   3827 C  CG  . ARG A 1 476 ? -48.258 39.126 19.012  1.00 54.94  ? 476 ARG A CG  1 
ATOM   3828 C  CD  . ARG A 1 476 ? -49.539 39.767 18.500  1.00 54.82  ? 476 ARG A CD  1 
ATOM   3829 N  NE  . ARG A 1 476 ? -50.659 39.561 19.411  1.00 57.49  ? 476 ARG A NE  1 
ATOM   3830 C  CZ  . ARG A 1 476 ? -51.578 38.617 19.270  1.00 53.39  ? 476 ARG A CZ  1 
ATOM   3831 N  NH1 . ARG A 1 476 ? -51.551 37.771 18.254  1.00 57.93  ? 476 ARG A NH1 1 
ATOM   3832 N  NH2 . ARG A 1 476 ? -52.551 38.519 20.172  1.00 54.24  ? 476 ARG A NH2 1 
ATOM   3833 N  N   A ARG A 1 477 ? -46.456 38.120 21.508  0.51 61.77  ? 477 ARG A N   1 
ATOM   3834 N  N   B ARG A 1 477 ? -46.450 38.114 21.514  0.49 61.77  ? 477 ARG A N   1 
ATOM   3835 C  CA  A ARG A 1 477 ? -46.421 38.410 22.935  0.51 65.30  ? 477 ARG A CA  1 
ATOM   3836 C  CA  B ARG A 1 477 ? -46.399 38.376 22.946  0.49 65.22  ? 477 ARG A CA  1 
ATOM   3837 C  C   A ARG A 1 477 ? -47.832 38.672 23.444  0.51 69.29  ? 477 ARG A C   1 
ATOM   3838 C  C   B ARG A 1 477 ? -47.800 38.686 23.464  0.49 69.26  ? 477 ARG A C   1 
ATOM   3839 O  O   A ARG A 1 477 ? -48.564 39.498 22.890  0.51 67.92  ? 477 ARG A O   1 
ATOM   3840 O  O   B ARG A 1 477 ? -48.493 39.560 22.933  0.49 67.93  ? 477 ARG A O   1 
ATOM   3841 C  CB  A ARG A 1 477 ? -45.518 39.617 23.195  0.51 64.58  ? 477 ARG A CB  1 
ATOM   3842 C  CB  B ARG A 1 477 ? -45.441 39.533 23.237  0.49 64.62  ? 477 ARG A CB  1 
ATOM   3843 C  CG  A ARG A 1 477 ? -44.899 39.687 24.584  0.51 69.50  ? 477 ARG A CG  1 
ATOM   3844 C  CG  B ARG A 1 477 ? -45.188 39.789 24.718  0.49 69.58  ? 477 ARG A CG  1 
ATOM   3845 C  CD  A ARG A 1 477 ? -43.846 40.788 24.627  0.51 69.08  ? 477 ARG A CD  1 
ATOM   3846 C  CD  B ARG A 1 477 ? -44.112 40.851 24.937  0.49 69.40  ? 477 ARG A CD  1 
ATOM   3847 N  NE  A ARG A 1 477 ? -43.538 41.236 25.980  0.51 69.55  ? 477 ARG A NE  1 
ATOM   3848 N  NE  B ARG A 1 477 ? -44.178 41.913 23.940  0.49 66.12  ? 477 ARG A NE  1 
ATOM   3849 C  CZ  A ARG A 1 477 ? -42.845 42.331 26.262  0.51 70.58  ? 477 ARG A CZ  1 
ATOM   3850 C  CZ  B ARG A 1 477 ? -45.105 42.861 23.913  0.49 67.76  ? 477 ARG A CZ  1 
ATOM   3851 N  NH1 A ARG A 1 477 ? -42.376 43.117 25.307  0.51 71.00  ? 477 ARG A NH1 1 
ATOM   3852 N  NH1 B ARG A 1 477 ? -46.068 42.913 24.819  0.49 68.45  ? 477 ARG A NH1 1 
ATOM   3853 N  NH2 A ARG A 1 477 ? -42.621 42.649 27.534  0.51 71.27  ? 477 ARG A NH2 1 
ATOM   3854 N  NH2 B ARG A 1 477 ? -45.071 43.773 22.945  0.49 65.94  ? 477 ARG A NH2 1 
ATOM   3855 N  N   . MET A 1 478 ? -48.221 37.957 24.493  1.00 69.20  ? 478 MET A N   1 
ATOM   3856 C  CA  . MET A 1 478 ? -49.578 38.073 25.011  1.00 73.03  ? 478 MET A CA  1 
ATOM   3857 C  C   . MET A 1 478 ? -49.634 38.868 26.311  1.00 78.57  ? 478 MET A C   1 
ATOM   3858 O  O   . MET A 1 478 ? -50.700 39.031 26.902  1.00 81.36  ? 478 MET A O   1 
ATOM   3859 C  CB  . MET A 1 478 ? -50.178 36.682 25.220  1.00 83.31  ? 478 MET A CB  1 
ATOM   3860 C  CG  . MET A 1 478 ? -49.931 35.733 24.058  1.00 92.11  ? 478 MET A CG  1 
ATOM   3861 S  SD  . MET A 1 478 ? -50.719 36.257 22.522  1.00 83.26  ? 478 MET A SD  1 
ATOM   3862 C  CE  . MET A 1 478 ? -52.108 35.129 22.455  1.00 62.17  ? 478 MET A CE  1 
HETATM 3863 C  C1  . EDO B 2 .   ? -60.121 59.803 8.786   1.00 73.62  ? 501 EDO A C1  1 
HETATM 3864 O  O1  . EDO B 2 .   ? -59.124 59.775 7.789   1.00 74.46  ? 501 EDO A O1  1 
HETATM 3865 C  C2  . EDO B 2 .   ? -59.517 59.450 10.122  1.00 69.70  ? 501 EDO A C2  1 
HETATM 3866 O  O2  . EDO B 2 .   ? -58.609 60.456 10.513  1.00 72.27  ? 501 EDO A O2  1 
HETATM 3867 C  C1  . EDO C 2 .   ? -35.108 14.061 9.812   1.00 77.07  ? 502 EDO A C1  1 
HETATM 3868 O  O1  . EDO C 2 .   ? -33.999 14.777 9.318   1.00 75.39  ? 502 EDO A O1  1 
HETATM 3869 C  C2  . EDO C 2 .   ? -35.856 14.902 10.817  1.00 75.75  ? 502 EDO A C2  1 
HETATM 3870 O  O2  . EDO C 2 .   ? -36.883 14.141 11.413  1.00 78.46  ? 502 EDO A O2  1 
HETATM 3871 C  C1  . EDO D 2 .   ? -38.053 49.370 -28.958 1.00 83.84  ? 503 EDO A C1  1 
HETATM 3872 O  O1  . EDO D 2 .   ? -36.938 48.526 -29.137 1.00 83.16  ? 503 EDO A O1  1 
HETATM 3873 C  C2  . EDO D 2 .   ? -39.025 48.728 -28.002 1.00 82.43  ? 503 EDO A C2  1 
HETATM 3874 O  O2  . EDO D 2 .   ? -39.412 47.467 -28.501 1.00 81.98  ? 503 EDO A O2  1 
HETATM 3875 C  C1  . EDO E 2 .   ? -15.659 46.418 16.875  1.00 65.37  ? 504 EDO A C1  1 
HETATM 3876 O  O1  . EDO E 2 .   ? -14.284 46.376 17.188  1.00 69.19  ? 504 EDO A O1  1 
HETATM 3877 C  C2  . EDO E 2 .   ? -16.140 47.847 16.878  1.00 64.90  ? 504 EDO A C2  1 
HETATM 3878 O  O2  . EDO E 2 .   ? -17.454 47.913 16.373  1.00 62.16  ? 504 EDO A O2  1 
HETATM 3879 S  S   . SO4 F 3 .   ? -43.370 40.035 -3.596  1.00 60.60  ? 505 SO4 A S   1 
HETATM 3880 O  O1  . SO4 F 3 .   ? -42.608 39.940 -4.881  1.00 71.52  ? 505 SO4 A O1  1 
HETATM 3881 O  O2  . SO4 F 3 .   ? -44.397 38.946 -3.545  1.00 58.40  ? 505 SO4 A O2  1 
HETATM 3882 O  O3  . SO4 F 3 .   ? -42.417 39.889 -2.448  1.00 73.85  ? 505 SO4 A O3  1 
HETATM 3883 O  O4  . SO4 F 3 .   ? -44.049 41.368 -3.509  1.00 69.70  ? 505 SO4 A O4  1 
HETATM 3884 S  S   . SO4 G 3 .   ? -39.125 41.891 -6.557  1.00 104.25 ? 506 SO4 A S   1 
HETATM 3885 O  O1  . SO4 G 3 .   ? -37.793 41.384 -7.018  1.00 90.55  ? 506 SO4 A O1  1 
HETATM 3886 O  O2  . SO4 G 3 .   ? -40.095 41.857 -7.698  1.00 94.86  ? 506 SO4 A O2  1 
HETATM 3887 O  O3  . SO4 G 3 .   ? -39.629 41.021 -5.446  1.00 97.78  ? 506 SO4 A O3  1 
HETATM 3888 O  O4  . SO4 G 3 .   ? -38.981 43.299 -6.064  1.00 85.61  ? 506 SO4 A O4  1 
HETATM 3889 S  S   . SO4 H 3 .   ? -65.813 35.702 20.553  1.00 74.94  ? 507 SO4 A S   1 
HETATM 3890 O  O1  . SO4 H 3 .   ? -64.647 35.511 19.632  1.00 68.50  ? 507 SO4 A O1  1 
HETATM 3891 O  O2  . SO4 H 3 .   ? -66.954 36.306 19.793  1.00 75.22  ? 507 SO4 A O2  1 
HETATM 3892 O  O3  . SO4 H 3 .   ? -66.230 34.373 21.109  1.00 73.71  ? 507 SO4 A O3  1 
HETATM 3893 O  O4  . SO4 H 3 .   ? -65.420 36.613 21.677  1.00 69.54  ? 507 SO4 A O4  1 
HETATM 3894 S  S   . SO4 I 3 .   ? -59.782 38.105 23.206  1.00 93.80  ? 508 SO4 A S   1 
HETATM 3895 O  O1  . SO4 I 3 .   ? -59.505 38.054 21.734  1.00 83.27  ? 508 SO4 A O1  1 
HETATM 3896 O  O2  . SO4 I 3 .   ? -61.173 38.612 23.434  1.00 82.17  ? 508 SO4 A O2  1 
HETATM 3897 O  O3  . SO4 I 3 .   ? -59.649 36.729 23.785  1.00 78.18  ? 508 SO4 A O3  1 
HETATM 3898 O  O4  . SO4 I 3 .   ? -58.801 39.024 23.868  1.00 85.18  ? 508 SO4 A O4  1 
HETATM 3899 NI NI  . NI  J 4 .   ? -43.006 39.711 -0.225  1.00 118.44 ? 509 NI  A NI  1 
HETATM 3900 NI NI  . NI  K 4 .   ? -44.823 42.195 -1.907  1.00 72.61  ? 510 NI  A NI  1 
HETATM 3901 O  O   . HOH L 5 .   ? -32.346 38.311 22.385  1.00 52.93  ? 601 HOH A O   1 
HETATM 3902 O  O   . HOH L 5 .   ? -21.041 43.804 1.949   1.00 64.81  ? 602 HOH A O   1 
HETATM 3903 O  O   . HOH L 5 .   ? -25.641 40.357 -2.097  1.00 67.21  ? 603 HOH A O   1 
HETATM 3904 O  O   . HOH L 5 .   ? -27.243 26.694 25.866  1.00 58.02  ? 604 HOH A O   1 
HETATM 3905 O  O   . HOH L 5 .   ? -14.672 43.463 19.759  1.00 62.49  ? 605 HOH A O   1 
HETATM 3906 O  O   . HOH L 5 .   ? -26.537 45.766 26.702  1.00 48.27  ? 606 HOH A O   1 
HETATM 3907 O  O   . HOH L 5 .   ? -59.551 60.363 5.509   1.00 76.68  ? 607 HOH A O   1 
HETATM 3908 O  O   . HOH L 5 .   ? -35.297 43.280 10.465  1.00 52.12  ? 608 HOH A O   1 
HETATM 3909 O  O   . HOH L 5 .   ? -40.245 34.447 27.657  1.00 58.71  ? 609 HOH A O   1 
HETATM 3910 O  O   . HOH L 5 .   ? -24.060 35.519 0.532   1.00 67.40  ? 610 HOH A O   1 
HETATM 3911 O  O   . HOH L 5 .   ? -38.297 44.157 2.377   1.00 62.21  ? 611 HOH A O   1 
HETATM 3912 O  O   . HOH L 5 .   ? -31.482 37.473 20.274  1.00 50.19  ? 612 HOH A O   1 
HETATM 3913 O  O   . HOH L 5 .   ? -42.028 25.964 18.424  1.00 62.09  ? 613 HOH A O   1 
HETATM 3914 O  O   . HOH L 5 .   ? -30.915 62.836 -4.930  1.00 67.43  ? 614 HOH A O   1 
HETATM 3915 O  O   . HOH L 5 .   ? -42.392 29.201 1.564   1.00 64.14  ? 615 HOH A O   1 
HETATM 3916 O  O   . HOH L 5 .   ? -55.649 29.462 13.514  1.00 56.93  ? 616 HOH A O   1 
HETATM 3917 O  O   . HOH L 5 .   ? -25.073 34.174 3.539   1.00 62.31  ? 617 HOH A O   1 
HETATM 3918 O  O   . HOH L 5 .   ? -53.947 40.531 -0.092  1.00 59.51  ? 618 HOH A O   1 
HETATM 3919 O  O   . HOH L 5 .   ? -58.568 39.964 17.098  1.00 50.73  ? 619 HOH A O   1 
HETATM 3920 O  O   . HOH L 5 .   ? -47.070 41.032 16.014  1.00 51.99  ? 620 HOH A O   1 
HETATM 3921 O  O   . HOH L 5 .   ? -9.810  37.994 24.782  1.00 62.40  ? 621 HOH A O   1 
HETATM 3922 O  O   . HOH L 5 .   ? -7.224  37.126 21.707  1.00 62.04  ? 622 HOH A O   1 
HETATM 3923 O  O   . HOH L 5 .   ? -18.130 34.272 7.733   1.00 71.53  ? 623 HOH A O   1 
HETATM 3924 O  O   . HOH L 5 .   ? -64.087 44.583 -1.000  1.00 73.07  ? 624 HOH A O   1 
HETATM 3925 O  O   . HOH L 5 .   ? -17.326 41.777 35.212  1.00 63.81  ? 625 HOH A O   1 
HETATM 3926 O  O   . HOH L 5 .   ? -18.012 46.803 29.708  1.00 53.48  ? 626 HOH A O   1 
HETATM 3927 O  O   . HOH L 5 .   ? -34.314 35.567 16.986  1.00 51.00  ? 627 HOH A O   1 
HETATM 3928 O  O   . HOH L 5 .   ? -27.569 56.363 13.680  1.00 60.68  ? 628 HOH A O   1 
HETATM 3929 O  O   . HOH L 5 .   ? -47.900 30.594 6.887   1.00 56.37  ? 629 HOH A O   1 
HETATM 3930 O  O   . HOH L 5 .   ? -46.696 33.648 14.790  1.00 53.18  ? 630 HOH A O   1 
HETATM 3931 O  O   . HOH L 5 .   ? -10.666 44.671 24.406  1.00 54.72  ? 631 HOH A O   1 
HETATM 3932 O  O   . HOH L 5 .   ? -46.159 42.044 4.173   1.00 55.17  ? 632 HOH A O   1 
HETATM 3933 O  O   . HOH L 5 .   ? -61.000 56.366 4.472   1.00 81.36  ? 633 HOH A O   1 
HETATM 3934 O  O   . HOH L 5 .   ? -42.592 35.590 20.323  1.00 58.17  ? 634 HOH A O   1 
HETATM 3935 O  O   . HOH L 5 .   ? -11.604 36.817 18.300  1.00 62.78  ? 635 HOH A O   1 
HETATM 3936 O  O   . HOH L 5 .   ? -50.989 53.164 12.709  1.00 62.13  ? 636 HOH A O   1 
HETATM 3937 O  O   . HOH L 5 .   ? -40.127 34.547 21.553  1.00 51.27  ? 637 HOH A O   1 
HETATM 3938 O  O   . HOH L 5 .   ? -70.132 35.131 7.925   1.00 61.93  ? 638 HOH A O   1 
HETATM 3939 O  O   . HOH L 5 .   ? -58.407 28.800 10.419  1.00 57.12  ? 639 HOH A O   1 
HETATM 3940 O  O   . HOH L 5 .   ? -24.602 47.797 22.697  1.00 52.91  ? 640 HOH A O   1 
HETATM 3941 O  O   . HOH L 5 .   ? -45.767 34.362 2.296   1.00 56.09  ? 641 HOH A O   1 
HETATM 3942 O  O   . HOH L 5 .   ? -36.999 26.812 27.802  1.00 53.25  ? 642 HOH A O   1 
HETATM 3943 O  O   . HOH L 5 .   ? -19.271 46.154 9.880   1.00 57.92  ? 643 HOH A O   1 
HETATM 3944 O  O   . HOH L 5 .   ? -52.832 47.560 18.338  1.00 50.91  ? 644 HOH A O   1 
HETATM 3945 O  O   . HOH L 5 .   ? -67.307 38.745 14.787  1.00 56.25  ? 645 HOH A O   1 
HETATM 3946 O  O   . HOH L 5 .   ? -33.041 38.072 17.962  1.00 52.74  ? 646 HOH A O   1 
HETATM 3947 O  O   . HOH L 5 .   ? -57.803 37.630 18.360  1.00 55.97  ? 647 HOH A O   1 
HETATM 3948 O  O   . HOH L 5 .   ? -26.439 48.861 20.069  1.00 55.11  ? 648 HOH A O   1 
HETATM 3949 O  O   . HOH L 5 .   ? -56.582 29.756 0.472   1.00 70.56  ? 649 HOH A O   1 
HETATM 3950 O  O   . HOH L 5 .   ? -36.702 45.841 21.075  1.00 54.84  ? 650 HOH A O   1 
HETATM 3951 O  O   . HOH L 5 .   ? -26.828 37.905 35.495  1.00 55.46  ? 651 HOH A O   1 
HETATM 3952 O  O   . HOH L 5 .   ? -30.189 20.588 17.422  1.00 59.82  ? 652 HOH A O   1 
HETATM 3953 O  O   . HOH L 5 .   ? -58.849 43.401 19.233  1.00 55.12  ? 653 HOH A O   1 
HETATM 3954 O  O   . HOH L 5 .   ? -57.485 30.516 12.064  1.00 54.59  ? 654 HOH A O   1 
HETATM 3955 O  O   . HOH L 5 .   ? -29.064 53.885 -9.451  1.00 70.28  ? 655 HOH A O   1 
HETATM 3956 O  O   . HOH L 5 .   ? -28.729 43.125 30.236  1.00 51.12  ? 656 HOH A O   1 
HETATM 3957 O  O   . HOH L 5 .   ? -68.080 38.331 12.359  1.00 57.08  ? 657 HOH A O   1 
HETATM 3958 O  O   . HOH L 5 .   ? -9.772  31.149 24.974  1.00 56.64  ? 658 HOH A O   1 
HETATM 3959 O  O   . HOH L 5 .   ? -28.895 45.083 27.659  1.00 56.04  ? 659 HOH A O   1 
HETATM 3960 O  O   . HOH L 5 .   ? -51.147 39.146 -10.511 1.00 62.96  ? 660 HOH A O   1 
HETATM 3961 O  O   . HOH L 5 .   ? -19.503 50.922 11.038  1.00 54.31  ? 661 HOH A O   1 
HETATM 3962 O  O   . HOH L 5 .   ? -18.088 48.207 11.225  1.00 55.83  ? 662 HOH A O   1 
HETATM 3963 O  O   . HOH L 5 .   ? -19.073 52.155 13.340  1.00 57.62  ? 663 HOH A O   1 
HETATM 3964 O  O   . HOH L 5 .   ? -50.917 41.449 -10.915 1.00 65.26  ? 664 HOH A O   1 
HETATM 3965 O  O   . HOH L 5 .   ? -44.547 28.984 23.171  1.00 63.69  ? 665 HOH A O   1 
HETATM 3966 O  O   . HOH L 5 .   ? -18.400 54.316 13.741  1.00 54.82  ? 666 HOH A 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   . MET A 1   ? 1.4625 1.7583 1.5112 -0.3258 -0.2732 0.3596  1   MET A N   
2    C CA  . MET A 1   ? 1.5625 1.8801 1.6064 -0.3222 -0.2614 0.3475  1   MET A CA  
3    C C   . MET A 1   ? 1.5111 1.8079 1.5954 -0.2815 -0.2557 0.3273  1   MET A C   
4    O O   . MET A 1   ? 1.5406 1.8538 1.6222 -0.2682 -0.2309 0.3031  1   MET A O   
5    C CB  . MET A 1   ? 1.5737 1.9025 1.6045 -0.3536 -0.2909 0.3797  1   MET A CB  
6    C CG  . MET A 1   ? 1.6303 1.9955 1.6122 -0.3990 -0.2893 0.3941  1   MET A CG  
7    S SD  . MET A 1   ? 1.9589 2.3704 1.9084 -0.4013 -0.2404 0.3524  1   MET A SD  
8    C CE  . MET A 1   ? 1.4459 1.8790 1.3933 -0.4006 -0.2366 0.3435  1   MET A CE  
9    N N   . LYS A 2   ? 1.3649 1.6277 1.4887 -0.2631 -0.2793 0.3363  2   LYS A N   
10   C CA  . LYS A 2   ? 1.2259 1.4738 1.3910 -0.2260 -0.2741 0.3151  2   LYS A CA  
11   C C   . LYS A 2   ? 1.1022 1.3481 1.2680 -0.2029 -0.2425 0.2847  2   LYS A C   
12   O O   . LYS A 2   ? 1.0669 1.2953 1.2380 -0.1990 -0.2452 0.2848  2   LYS A O   
13   C CB  . LYS A 2   ? 1.1173 1.3332 1.3291 -0.2143 -0.3105 0.3306  2   LYS A CB  
14   C CG  . LYS A 2   ? 1.0345 1.2463 1.2899 -0.1842 -0.3116 0.3130  2   LYS A CG  
15   C CD  . LYS A 2   ? 1.0261 1.2077 1.3357 -0.1710 -0.3488 0.3236  2   LYS A CD  
16   C CE  . LYS A 2   ? 1.0316 1.2166 1.3869 -0.1427 -0.3491 0.3033  2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.1050 1.2626 1.5226 -0.1224 -0.3798 0.3015  2   LYS A NZ  
18   N N   . VAL A 3   ? 1.0154 1.2785 1.1758 -0.1890 -0.2142 0.2600  3   VAL A N   
19   C CA  . VAL A 3   ? 0.8902 1.1528 1.0491 -0.1698 -0.1859 0.2337  3   VAL A CA  
20   C C   . VAL A 3   ? 0.8384 1.0778 1.0366 -0.1420 -0.1919 0.2230  3   VAL A C   
21   O O   . VAL A 3   ? 0.8582 1.0861 1.0905 -0.1320 -0.2129 0.2284  3   VAL A O   
22   C CB  . VAL A 3   ? 0.8392 1.1237 0.9864 -0.1634 -0.1588 0.2128  3   VAL A CB  
23   C CG1 . VAL A 3   ? 0.8603 1.1699 0.9767 -0.1903 -0.1572 0.2211  3   VAL A CG1 
24   C CG2 . VAL A 3   ? 0.7425 1.0243 0.9208 -0.1416 -0.1596 0.2029  3   VAL A CG2 
25   N N   . ASP A 4   ? 0.7090 0.9436 0.9040 -0.1297 -0.1734 0.2058  4   ASP A N   
26   C CA  . ASP A 4   ? 0.6892 0.9064 0.9174 -0.1054 -0.1758 0.1917  4   ASP A CA  
27   C C   . ASP A 4   ? 0.6427 0.8712 0.8887 -0.0836 -0.1586 0.1684  4   ASP A C   
28   O O   . ASP A 4   ? 0.6536 0.8749 0.9362 -0.0652 -0.1668 0.1576  4   ASP A O   
29   C CB  . ASP A 4   ? 0.6945 0.9036 0.9099 -0.1042 -0.1648 0.1844  4   ASP A CB  
30   C CG  . ASP A 4   ? 0.7485 0.9481 0.9479 -0.1272 -0.1818 0.2072  4   ASP A CG  
31   O OD1 . ASP A 4   ? 0.7936 0.9763 1.0128 -0.1332 -0.2113 0.2261  4   ASP A OD1 
32   O OD2 . ASP A 4   ? 0.7542 0.9645 0.9232 -0.1404 -0.1669 0.2064  4   ASP A OD2 
33   N N   . TRP A 5   ? 0.6354 0.8828 0.8585 -0.0861 -0.1357 0.1593  5   TRP A N   
34   C CA  . TRP A 5   ? 0.6248 0.8845 0.8605 -0.0696 -0.1192 0.1399  5   TRP A CA  
35   C C   . TRP A 5   ? 0.5314 0.8095 0.7492 -0.0794 -0.1087 0.1412  5   TRP A C   
36   O O   . TRP A 5   ? 0.5430 0.8272 0.7319 -0.0955 -0.1026 0.1472  5   TRP A O   
37   C CB  . TRP A 5   ? 0.6186 0.8782 0.8475 -0.0587 -0.0987 0.1220  5   TRP A CB  
38   C CG  . TRP A 5   ? 0.6396 0.8855 0.8920 -0.0454 -0.1064 0.1139  5   TRP A CG  
39   C CD1 . TRP A 5   ? 0.6363 0.8658 0.8833 -0.0487 -0.1132 0.1188  5   TRP A CD1 
40   C CD2 . TRP A 5   ? 0.6048 0.8549 0.8920 -0.0272 -0.1081 0.0968  5   TRP A CD2 
41   N NE1 . TRP A 5   ? 0.6333 0.8539 0.9100 -0.0331 -0.1199 0.1058  5   TRP A NE1 
42   C CE2 . TRP A 5   ? 0.6267 0.8614 0.9290 -0.0195 -0.1164 0.0906  5   TRP A CE2 
43   C CE3 . TRP A 5   ? 0.5535 0.8220 0.8619 -0.0175 -0.1030 0.0842  5   TRP A CE3 
44   C CZ2 . TRP A 5   ? 0.6027 0.8409 0.9420 -0.0019 -0.1193 0.0695  5   TRP A CZ2 
45   C CZ3 . TRP A 5   ? 0.6110 0.8856 0.9553 -0.0008 -0.1050 0.0637  5   TRP A CZ3 
46   C CH2 . TRP A 5   ? 0.6208 0.8807 0.9809 0.0072  -0.1130 0.0553  5   TRP A CH2 
47   N N   . LEU A 6   ? 0.5629 0.8520 0.7999 -0.0700 -0.1066 0.1335  6   LEU A N   
48   C CA  . LEU A 6   ? 0.5647 0.8709 0.7893 -0.0775 -0.0969 0.1326  6   LEU A CA  
49   C C   . LEU A 6   ? 0.5073 0.8251 0.7440 -0.0638 -0.0801 0.1150  6   LEU A C   
50   O O   . LEU A 6   ? 0.5130 0.8367 0.7793 -0.0519 -0.0852 0.1080  6   LEU A O   
51   C CB  . LEU A 6   ? 0.5315 0.8426 0.7665 -0.0861 -0.1164 0.1469  6   LEU A CB  
52   C CG  . LEU A 6   ? 0.5158 0.8456 0.7435 -0.0924 -0.1080 0.1442  6   LEU A CG  
53   C CD1 . LEU A 6   ? 0.5097 0.8465 0.7028 -0.1067 -0.0926 0.1419  6   LEU A CD1 
54   C CD2 . LEU A 6   ? 0.5896 0.9243 0.8296 -0.1008 -0.1299 0.1592  6   LEU A CD2 
55   N N   . PHE A 7   ? 0.4517 0.7744 0.6676 -0.0667 -0.0613 0.1077  7   PHE A N   
56   C CA  . PHE A 7   ? 0.4880 0.8225 0.7098 -0.0592 -0.0463 0.0950  7   PHE A CA  
57   C C   . PHE A 7   ? 0.5035 0.8515 0.7232 -0.0672 -0.0441 0.0972  7   PHE A C   
58   O O   . PHE A 7   ? 0.5496 0.8977 0.7495 -0.0780 -0.0390 0.0994  7   PHE A O   
59   C CB  . PHE A 7   ? 0.5064 0.8358 0.7098 -0.0590 -0.0315 0.0886  7   PHE A CB  
60   C CG  . PHE A 7   ? 0.5210 0.8392 0.7268 -0.0510 -0.0325 0.0848  7   PHE A CG  
61   C CD1 . PHE A 7   ? 0.5494 0.8743 0.7715 -0.0396 -0.0282 0.0733  7   PHE A CD1 
62   C CD2 . PHE A 7   ? 0.5140 0.8183 0.7060 -0.0562 -0.0371 0.0910  7   PHE A CD2 
63   C CE1 . PHE A 7   ? 0.4915 0.8071 0.7165 -0.0326 -0.0293 0.0676  7   PHE A CE1 
64   C CE2 . PHE A 7   ? 0.5313 0.8248 0.7263 -0.0493 -0.0386 0.0874  7   PHE A CE2 
65   C CZ  . PHE A 7   ? 0.5018 0.7998 0.7134 -0.0370 -0.0351 0.0755  7   PHE A CZ  
66   N N   . LYS A 8   ? 0.5212 0.8822 0.7642 -0.0618 -0.0482 0.0943  8   LYS A N   
67   C CA  . LYS A 8   ? 0.5095 0.8838 0.7536 -0.0695 -0.0487 0.0971  8   LYS A CA  
68   C C   . LYS A 8   ? 0.5496 0.9366 0.7929 -0.0694 -0.0328 0.0882  8   LYS A C   
69   O O   . LYS A 8   ? 0.5089 0.9044 0.7637 -0.0612 -0.0251 0.0790  8   LYS A O   
70   C CB  . LYS A 8   ? 0.5031 0.8862 0.7759 -0.0652 -0.0646 0.1004  8   LYS A CB  
71   C CG  . LYS A 8   ? 0.5082 0.8777 0.7851 -0.0679 -0.0857 0.1137  8   LYS A CG  
72   C CD  . LYS A 8   ? 0.5052 0.8830 0.8143 -0.0644 -0.1046 0.1182  8   LYS A CD  
73   C CE  . LYS A 8   ? 0.4938 0.8849 0.8400 -0.0467 -0.1006 0.1006  8   LYS A CE  
74   N NZ  . LYS A 8   ? 0.4780 0.8794 0.8625 -0.0416 -0.1199 0.1021  8   LYS A NZ  
75   N N   . ASN A 9   ? 0.5412 0.9308 0.7709 -0.0803 -0.0287 0.0907  9   ASN A N   
76   C CA  . ASN A 9   ? 0.5300 0.9313 0.7617 -0.0838 -0.0184 0.0861  9   ASN A CA  
77   C C   . ASN A 9   ? 0.5434 0.9416 0.7684 -0.0808 -0.0066 0.0812  9   ASN A C   
78   O O   . ASN A 9   ? 0.5604 0.9740 0.7942 -0.0803 0.0003  0.0771  9   ASN A O   
79   C CB  . ASN A 9   ? 0.4862 0.9087 0.7424 -0.0810 -0.0215 0.0838  9   ASN A CB  
80   C CG  . ASN A 9   ? 0.4607 0.8963 0.7171 -0.0898 -0.0141 0.0827  9   ASN A CG  
81   O OD1 . ASN A 9   ? 0.4547 0.8806 0.6948 -0.0987 -0.0102 0.0849  9   ASN A OD1 
82   N ND2 . ASN A 9   ? 0.4429 0.9016 0.7209 -0.0878 -0.0129 0.0782  9   ASN A ND2 
83   N N   . VAL A 10  ? 0.5075 0.8883 0.7164 -0.0807 -0.0048 0.0820  10  VAL A N   
84   C CA  . VAL A 10  ? 0.5475 0.9231 0.7484 -0.0791 0.0036  0.0795  10  VAL A CA  
85   C C   . VAL A 10  ? 0.5192 0.8856 0.7096 -0.0881 0.0063  0.0816  10  VAL A C   
86   O O   . VAL A 10  ? 0.5021 0.8619 0.6885 -0.0931 0.0027  0.0813  10  VAL A O   
87   C CB  . VAL A 10  ? 0.5328 0.8952 0.7273 -0.0717 0.0023  0.0780  10  VAL A CB  
88   C CG1 . VAL A 10  ? 0.5813 0.9508 0.7923 -0.0620 -0.0025 0.0742  10  VAL A CG1 
89   C CG2 . VAL A 10  ? 0.5487 0.8970 0.7315 -0.0760 -0.0028 0.0811  10  VAL A CG2 
90   N N   . THR A 11  ? 0.5498 0.9173 0.7375 -0.0912 0.0114  0.0832  11  THR A N   
91   C CA  . THR A 11  ? 0.5590 0.9126 0.7413 -0.0985 0.0103  0.0861  11  THR A CA  
92   C C   . THR A 11  ? 0.5067 0.8429 0.6809 -0.0935 0.0092  0.0836  11  THR A C   
93   O O   . THR A 11  ? 0.5632 0.8975 0.7319 -0.0894 0.0117  0.0846  11  THR A O   
94   C CB  . THR A 11  ? 0.5420 0.9023 0.7238 -0.1066 0.0127  0.0927  11  THR A CB  
95   O OG1 . THR A 11  ? 0.5867 0.9663 0.7771 -0.1128 0.0143  0.0942  11  THR A OG1 
96   C CG2 . THR A 11  ? 0.4988 0.8399 0.6799 -0.1139 0.0067  0.0976  11  THR A CG2 
97   N N   . VAL A 12  ? 0.4882 0.8151 0.6625 -0.0948 0.0060  0.0786  12  VAL A N   
98   C CA  . VAL A 12  ? 0.5241 0.8389 0.6932 -0.0909 0.0055  0.0738  12  VAL A CA  
99   C C   . VAL A 12  ? 0.5024 0.8039 0.6764 -0.0931 0.0027  0.0740  12  VAL A C   
100  O O   . VAL A 12  ? 0.5149 0.8118 0.6994 -0.0983 -0.0014 0.0703  12  VAL A O   
101  C CB  . VAL A 12  ? 0.4803 0.7979 0.6480 -0.0936 0.0041  0.0659  12  VAL A CB  
102  C CG1 . VAL A 12  ? 0.4443 0.7540 0.6087 -0.0912 0.0047  0.0592  12  VAL A CG1 
103  C CG2 . VAL A 12  ? 0.4593 0.7876 0.6227 -0.0933 0.0025  0.0701  12  VAL A CG2 
104  N N   . ILE A 13  ? 0.5510 0.8458 0.7196 -0.0896 0.0030  0.0783  13  ILE A N   
105  C CA  . ILE A 13  ? 0.5758 0.8555 0.7500 -0.0908 -0.0030 0.0796  13  ILE A CA  
106  C C   . ILE A 13  ? 0.5292 0.8030 0.7019 -0.0840 -0.0022 0.0712  13  ILE A C   
107  O O   . ILE A 13  ? 0.5366 0.8097 0.6996 -0.0797 0.0000  0.0743  13  ILE A O   
108  C CB  . ILE A 13  ? 0.5568 0.8361 0.7246 -0.0953 -0.0047 0.0926  13  ILE A CB  
109  C CG1 . ILE A 13  ? 0.5329 0.8233 0.7018 -0.1048 -0.0044 0.1008  13  ILE A CG1 
110  C CG2 . ILE A 13  ? 0.5641 0.8253 0.7393 -0.0974 -0.0150 0.0968  13  ILE A CG2 
111  C CD1 . ILE A 13  ? 0.5479 0.8424 0.7087 -0.1149 -0.0069 0.1147  13  ILE A CD1 
112  N N   . ASP A 14  ? 0.5365 0.8088 0.7195 -0.0841 -0.0037 0.0587  14  ASP A N   
113  C CA  . ASP A 14  ? 0.4893 0.7637 0.6704 -0.0805 -0.0010 0.0484  14  ASP A CA  
114  C C   . ASP A 14  ? 0.5006 0.7634 0.6866 -0.0758 -0.0050 0.0481  14  ASP A C   
115  O O   . ASP A 14  ? 0.4983 0.7643 0.6830 -0.0732 -0.0024 0.0399  14  ASP A O   
116  C CB  . ASP A 14  ? 0.5190 0.8025 0.7109 -0.0846 -0.0003 0.0317  14  ASP A CB  
117  C CG  . ASP A 14  ? 0.5652 0.8402 0.7809 -0.0857 -0.0075 0.0234  14  ASP A CG  
118  O OD1 . ASP A 14  ? 0.5985 0.8576 0.8222 -0.0839 -0.0151 0.0330  14  ASP A OD1 
119  O OD2 . ASP A 14  ? 0.5189 0.8038 0.7462 -0.0897 -0.0067 0.0072  14  ASP A OD2 
120  N N   . GLY A 15  ? 0.5615 0.8123 0.7527 -0.0764 -0.0121 0.0579  15  GLY A N   
121  C CA  . GLY A 15  ? 0.5485 0.7878 0.7450 -0.0730 -0.0185 0.0598  15  GLY A CA  
122  C C   . GLY A 15  ? 0.5205 0.7509 0.7449 -0.0710 -0.0278 0.0474  15  GLY A C   
123  O O   . GLY A 15  ? 0.4936 0.7139 0.7272 -0.0678 -0.0356 0.0486  15  GLY A O   
124  N N   . SER A 16  ? 0.5126 0.7477 0.7534 -0.0728 -0.0279 0.0337  16  SER A N   
125  C CA  . SER A 16  ? 0.4956 0.7243 0.7702 -0.0699 -0.0374 0.0167  16  SER A CA  
126  C C   . SER A 16  ? 0.5197 0.7273 0.8151 -0.0727 -0.0545 0.0276  16  SER A C   
127  O O   . SER A 16  ? 0.5189 0.7163 0.8491 -0.0690 -0.0671 0.0148  16  SER A O   
128  C CB  . SER A 16  ? 0.4830 0.7294 0.7679 -0.0719 -0.0301 -0.0065 16  SER A CB  
129  O OG  . SER A 16  ? 0.4718 0.7190 0.7527 -0.0780 -0.0300 -0.0010 16  SER A OG  
130  N N   . GLY A 17  ? 0.5124 0.7146 0.7898 -0.0800 -0.0565 0.0503  17  GLY A N   
131  C CA  . GLY A 17  ? 0.4957 0.6799 0.7896 -0.0872 -0.0735 0.0640  17  GLY A CA  
132  C C   . GLY A 17  ? 0.5598 0.7444 0.8698 -0.0914 -0.0756 0.0556  17  GLY A C   
133  O O   . GLY A 17  ? 0.5215 0.6898 0.8472 -0.0990 -0.0912 0.0678  17  GLY A O   
134  N N   . GLY A 18  ? 0.5247 0.7278 0.8309 -0.0886 -0.0617 0.0364  18  GLY A N   
135  C CA  . GLY A 18  ? 0.5103 0.7170 0.8307 -0.0931 -0.0627 0.0258  18  GLY A CA  
136  C C   . GLY A 18  ? 0.5104 0.7248 0.8068 -0.1019 -0.0566 0.0436  18  GLY A C   
137  O O   . GLY A 18  ? 0.5364 0.7538 0.8078 -0.1048 -0.0521 0.0633  18  GLY A O   
138  N N   . PRO A 19  ? 0.4911 0.7115 0.7965 -0.1066 -0.0560 0.0344  19  PRO A N   
139  C CA  . PRO A 19  ? 0.5320 0.7611 0.8198 -0.1154 -0.0516 0.0501  19  PRO A CA  
140  C C   . PRO A 19  ? 0.5440 0.7938 0.8009 -0.1130 -0.0356 0.0546  19  PRO A C   
141  O O   . PRO A 19  ? 0.5596 0.8189 0.8083 -0.1066 -0.0274 0.0430  19  PRO A O   
142  C CB  . PRO A 19  ? 0.5309 0.7639 0.8376 -0.1193 -0.0541 0.0334  19  PRO A CB  
143  C CG  . PRO A 19  ? 0.5513 0.7713 0.8927 -0.1139 -0.0649 0.0120  19  PRO A CG  
144  C CD  . PRO A 19  ? 0.5325 0.7544 0.8680 -0.1047 -0.0600 0.0070  19  PRO A CD  
145  N N   . GLN A 20  ? 0.5380 0.7957 0.7802 -0.1193 -0.0324 0.0714  20  GLN A N   
146  C CA  . GLN A 20  ? 0.5230 0.7998 0.7433 -0.1166 -0.0201 0.0752  20  GLN A CA  
147  C C   . GLN A 20  ? 0.4995 0.7916 0.7201 -0.1198 -0.0160 0.0684  20  GLN A C   
148  O O   . GLN A 20  ? 0.5426 0.8324 0.7766 -0.1265 -0.0215 0.0651  20  GLN A O   
149  C CB  . GLN A 20  ? 0.5363 0.8192 0.7440 -0.1213 -0.0181 0.0932  20  GLN A CB  
150  C CG  . GLN A 20  ? 0.5788 0.8633 0.7930 -0.1342 -0.0238 0.1047  20  GLN A CG  
151  C CD  . GLN A 20  ? 0.5970 0.8961 0.7969 -0.1419 -0.0197 0.1201  20  GLN A CD  
152  O OE1 . GLN A 20  ? 0.6116 0.9144 0.7989 -0.1376 -0.0151 0.1224  20  GLN A OE1 
153  N NE2 . GLN A 20  ? 0.6619 0.9725 0.8640 -0.1545 -0.0207 0.1291  20  GLN A NE2 
154  N N   . TYR A 21  ? 0.4968 0.8035 0.7037 -0.1155 -0.0083 0.0669  21  TYR A N   
155  C CA  . TYR A 21  ? 0.4877 0.8097 0.6934 -0.1191 -0.0064 0.0626  21  TYR A CA  
156  C C   . TYR A 21  ? 0.4962 0.8313 0.6902 -0.1144 -0.0017 0.0693  21  TYR A C   
157  O O   . TYR A 21  ? 0.5113 0.8431 0.6978 -0.1075 0.0009  0.0721  21  TYR A O   
158  C CB  . TYR A 21  ? 0.4767 0.8017 0.6855 -0.1209 -0.0070 0.0458  21  TYR A CB  
159  C CG  . TYR A 21  ? 0.5440 0.8701 0.7427 -0.1159 -0.0033 0.0401  21  TYR A CG  
160  C CD1 . TYR A 21  ? 0.5227 0.8361 0.7273 -0.1109 -0.0041 0.0345  21  TYR A CD1 
161  C CD2 . TYR A 21  ? 0.4815 0.8212 0.6662 -0.1175 -0.0010 0.0416  21  TYR A CD2 
162  C CE1 . TYR A 21  ? 0.4799 0.7964 0.6758 -0.1075 -0.0005 0.0291  21  TYR A CE1 
163  C CE2 . TYR A 21  ? 0.4127 0.7539 0.5876 -0.1156 0.0012  0.0384  21  TYR A CE2 
164  C CZ  . TYR A 21  ? 0.4657 0.7963 0.6458 -0.1106 0.0026  0.0314  21  TYR A CZ  
165  O OH  . TYR A 21  ? 0.4440 0.7780 0.6149 -0.1099 0.0051  0.0280  21  TYR A OH  
166  N N   . ARG A 22  ? 0.4810 0.8306 0.6768 -0.1180 -0.0023 0.0712  22  ARG A N   
167  C CA  . ARG A 22  ? 0.5127 0.8745 0.7052 -0.1131 -0.0016 0.0763  22  ARG A CA  
168  C C   . ARG A 22  ? 0.4609 0.8272 0.6468 -0.1152 -0.0054 0.0729  22  ARG A C   
169  O O   . ARG A 22  ? 0.5026 0.8742 0.6884 -0.1236 -0.0078 0.0671  22  ARG A O   
170  C CB  . ARG A 22  ? 0.4726 0.8500 0.6750 -0.1161 -0.0017 0.0811  22  ARG A CB  
171  C CG  . ARG A 22  ? 0.4878 0.8670 0.6940 -0.1188 0.0023  0.0861  22  ARG A CG  
172  C CD  . ARG A 22  ? 0.5742 0.9751 0.7912 -0.1231 0.0034  0.0891  22  ARG A CD  
173  N NE  . ARG A 22  ? 0.5828 0.9888 0.8012 -0.1319 0.0066  0.0951  22  ARG A NE  
174  C CZ  . ARG A 22  ? 0.6356 1.0625 0.8631 -0.1397 0.0085  0.0980  22  ARG A CZ  
175  N NH1 . ARG A 22  ? 0.6070 1.0511 0.8460 -0.1376 0.0073  0.0942  22  ARG A NH1 
176  N NH2 . ARG A 22  ? 0.6681 1.1002 0.8934 -0.1513 0.0106  0.1058  22  ARG A NH2 
177  N N   . ALA A 23  ? 0.4919 0.8572 0.6722 -0.1093 -0.0070 0.0767  23  ALA A N   
178  C CA  . ALA A 23  ? 0.5229 0.8922 0.6941 -0.1146 -0.0126 0.0773  23  ALA A CA  
179  C C   . ALA A 23  ? 0.5411 0.9079 0.7132 -0.1073 -0.0180 0.0857  23  ALA A C   
180  O O   . ALA A 23  ? 0.5774 0.9412 0.7585 -0.0972 -0.0156 0.0868  23  ALA A O   
181  C CB  . ALA A 23  ? 0.4822 0.8471 0.6433 -0.1196 -0.0090 0.0677  23  ALA A CB  
182  N N   . ASP A 24  ? 0.4904 0.8600 0.6541 -0.1142 -0.0263 0.0911  24  ASP A N   
183  C CA  . ASP A 24  ? 0.4871 0.8501 0.6528 -0.1094 -0.0350 0.1000  24  ASP A CA  
184  C C   . ASP A 24  ? 0.5053 0.8600 0.6560 -0.1123 -0.0321 0.0983  24  ASP A C   
185  O O   . ASP A 24  ? 0.4879 0.8490 0.6251 -0.1234 -0.0280 0.0924  24  ASP A O   
186  C CB  . ASP A 24  ? 0.4864 0.8568 0.6541 -0.1178 -0.0507 0.1119  24  ASP A CB  
187  C CG  . ASP A 24  ? 0.5292 0.9078 0.7180 -0.1120 -0.0560 0.1138  24  ASP A CG  
188  O OD1 . ASP A 24  ? 0.5310 0.9118 0.7315 -0.1024 -0.0461 0.1057  24  ASP A OD1 
189  O OD2 . ASP A 24  ? 0.5318 0.9167 0.7260 -0.1185 -0.0708 0.1241  24  ASP A OD2 
190  N N   . VAL A 25  ? 0.4719 0.8149 0.6272 -0.1026 -0.0339 0.1010  25  VAL A N   
191  C CA  . VAL A 25  ? 0.4724 0.8073 0.6156 -0.1046 -0.0318 0.1001  25  VAL A CA  
192  C C   . VAL A 25  ? 0.5304 0.8576 0.6768 -0.1050 -0.0461 0.1124  25  VAL A C   
193  O O   . VAL A 25  ? 0.5523 0.8728 0.7170 -0.0932 -0.0525 0.1145  25  VAL A O   
194  C CB  . VAL A 25  ? 0.5074 0.8329 0.6532 -0.0931 -0.0209 0.0911  25  VAL A CB  
195  C CG1 . VAL A 25  ? 0.4558 0.7747 0.5905 -0.0958 -0.0190 0.0893  25  VAL A CG1 
196  C CG2 . VAL A 25  ? 0.4910 0.8207 0.6382 -0.0934 -0.0113 0.0823  25  VAL A CG2 
197  N N   . ALA A 26  ? 0.5636 0.8933 0.6941 -0.1197 -0.0519 0.1194  26  ALA A N   
198  C CA  . ALA A 26  ? 0.5479 0.8686 0.6801 -0.1244 -0.0688 0.1347  26  ALA A CA  
199  C C   . ALA A 26  ? 0.5640 0.8768 0.6859 -0.1262 -0.0650 0.1331  26  ALA A C   
200  O O   . ALA A 26  ? 0.5277 0.8499 0.6347 -0.1330 -0.0523 0.1234  26  ALA A O   
201  C CB  . ALA A 26  ? 0.5650 0.8978 0.6849 -0.1457 -0.0826 0.1495  26  ALA A CB  
202  N N   . VAL A 27  ? 0.5390 0.8352 0.6725 -0.1196 -0.0769 0.1411  27  VAL A N   
203  C CA  . VAL A 27  ? 0.5458 0.8326 0.6724 -0.1205 -0.0754 0.1407  27  VAL A CA  
204  C C   . VAL A 27  ? 0.6119 0.8903 0.7375 -0.1343 -0.0971 0.1609  27  VAL A C   
205  O O   . VAL A 27  ? 0.6219 0.8893 0.7671 -0.1300 -0.1156 0.1717  27  VAL A O   
206  C CB  . VAL A 27  ? 0.5285 0.8014 0.6713 -0.0991 -0.0691 0.1290  27  VAL A CB  
207  C CG1 . VAL A 27  ? 0.5506 0.8116 0.6896 -0.1005 -0.0721 0.1310  27  VAL A CG1 
208  C CG2 . VAL A 27  ? 0.5415 0.8225 0.6807 -0.0907 -0.0495 0.1130  27  VAL A CG2 
209  N N   . LYS A 28  ? 0.6399 0.9245 0.7450 -0.1518 -0.0961 0.1661  28  LYS A N   
210  C CA  . LYS A 28  ? 0.6369 0.9133 0.7381 -0.1686 -0.1171 0.1876  28  LYS A CA  
211  C C   . LYS A 28  ? 0.6383 0.9077 0.7340 -0.1686 -0.1114 0.1833  28  LYS A C   
212  O O   . LYS A 28  ? 0.6333 0.9205 0.7107 -0.1772 -0.0946 0.1726  28  LYS A O   
213  C CB  . LYS A 28  ? 0.7584 1.0575 0.8349 -0.1988 -0.1236 0.2021  28  LYS A CB  
214  C CG  . LYS A 28  ? 0.7389 1.0285 0.8126 -0.2196 -0.1515 0.2311  28  LYS A CG  
215  C CD  . LYS A 28  ? 0.8344 1.1541 0.8739 -0.2553 -0.1514 0.2420  28  LYS A CD  
216  C CE  . LYS A 28  ? 0.9739 1.2907 1.0089 -0.2797 -0.1825 0.2749  28  LYS A CE  
217  N NZ  . LYS A 28  ? 1.0660 1.3849 1.1114 -0.2738 -0.1900 0.2777  28  LYS A NZ  
218  N N   . GLY A 29  ? 0.6374 0.8819 0.7521 -0.1588 -0.1259 0.1896  29  GLY A N   
219  C CA  . GLY A 29  ? 0.6148 0.8513 0.7262 -0.1575 -0.1211 0.1848  29  GLY A CA  
220  C C   . GLY A 29  ? 0.5816 0.8198 0.6968 -0.1363 -0.0984 0.1602  29  GLY A C   
221  O O   . GLY A 29  ? 0.6467 0.8788 0.7789 -0.1164 -0.0942 0.1493  29  GLY A O   
222  N N   . ASP A 30  ? 0.5669 0.8157 0.6668 -0.1422 -0.0843 0.1516  30  ASP A N   
223  C CA  . ASP A 30  ? 0.5565 0.8069 0.6588 -0.1254 -0.0655 0.1312  30  ASP A CA  
224  C C   . ASP A 30  ? 0.5582 0.8307 0.6501 -0.1288 -0.0488 0.1191  30  ASP A C   
225  O O   . ASP A 30  ? 0.5038 0.7796 0.5967 -0.1198 -0.0353 0.1042  30  ASP A O   
226  C CB  . ASP A 30  ? 0.5340 0.7792 0.6333 -0.1265 -0.0631 0.1277  30  ASP A CB  
227  C CG  . ASP A 30  ? 0.5653 0.8292 0.6466 -0.1507 -0.0621 0.1335  30  ASP A CG  
228  O OD1 . ASP A 30  ? 0.5635 0.8446 0.6330 -0.1683 -0.0645 0.1413  30  ASP A OD1 
229  O OD2 . ASP A 30  ? 0.5490 0.8135 0.6275 -0.1535 -0.0585 0.1293  30  ASP A OD2 
230  N N   . ARG A 31  ? 0.5897 0.8769 0.6737 -0.1418 -0.0512 0.1249  31  ARG A N   
231  C CA  . ARG A 31  ? 0.5653 0.8750 0.6420 -0.1470 -0.0370 0.1115  31  ARG A CA  
232  C C   . ARG A 31  ? 0.5475 0.8578 0.6304 -0.1408 -0.0379 0.1119  31  ARG A C   
233  O O   . ARG A 31  ? 0.6046 0.9066 0.6925 -0.1415 -0.0517 0.1260  31  ARG A O   
234  C CB  . ARG A 31  ? 0.5937 0.9299 0.6521 -0.1734 -0.0364 0.1139  31  ARG A CB  
235  C CG  . ARG A 31  ? 0.5943 0.9374 0.6463 -0.1827 -0.0331 0.1109  31  ARG A CG  
236  C CD  . ARG A 31  ? 0.5864 0.9393 0.6462 -0.1723 -0.0158 0.0865  31  ARG A CD  
237  N NE  . ARG A 31  ? 0.6048 0.9680 0.6611 -0.1813 -0.0122 0.0818  31  ARG A NE  
238  C CZ  . ARG A 31  ? 0.5583 0.9348 0.6236 -0.1763 0.0005  0.0605  31  ARG A CZ  
239  N NH1 . ARG A 31  ? 0.5569 0.9358 0.6359 -0.1630 0.0093  0.0429  31  ARG A NH1 
240  N NH2 . ARG A 31  ? 0.5298 0.9172 0.5932 -0.1854 0.0027  0.0572  31  ARG A NH2 
241  N N   . ILE A 32  ? 0.5620 0.8818 0.6476 -0.1350 -0.0248 0.0962  32  ILE A N   
242  C CA  . ILE A 32  ? 0.5441 0.8685 0.6343 -0.1324 -0.0242 0.0950  32  ILE A CA  
243  C C   . ILE A 32  ? 0.5344 0.8818 0.6107 -0.1543 -0.0269 0.0981  32  ILE A C   
244  O O   . ILE A 32  ? 0.5490 0.9171 0.6177 -0.1653 -0.0174 0.0846  32  ILE A O   
245  C CB  . ILE A 32  ? 0.5193 0.8437 0.6189 -0.1203 -0.0118 0.0788  32  ILE A CB  
246  C CG1 . ILE A 32  ? 0.4911 0.7962 0.6008 -0.1023 -0.0104 0.0783  32  ILE A CG1 
247  C CG2 . ILE A 32  ? 0.5390 0.8706 0.6426 -0.1211 -0.0114 0.0775  32  ILE A CG2 
248  C CD1 . ILE A 32  ? 0.5004 0.8036 0.6182 -0.0934 -0.0016 0.0668  32  ILE A CD1 
249  N N   . MET A 33  ? 0.5552 0.9015 0.6297 -0.1611 -0.0405 0.1145  33  MET A N   
250  C CA  . MET A 33  ? 0.5460 0.9150 0.6032 -0.1861 -0.0465 0.1221  33  MET A CA  
251  C C   . MET A 33  ? 0.6015 0.9895 0.6574 -0.1900 -0.0381 0.1089  33  MET A C   
252  O O   . MET A 33  ? 0.5852 0.9999 0.6289 -0.2063 -0.0295 0.0961  33  MET A O   
253  C CB  . MET A 33  ? 0.5817 0.9400 0.6394 -0.1935 -0.0689 0.1478  33  MET A CB  
254  C CG  . MET A 33  ? 0.7409 1.1230 0.7777 -0.2229 -0.0787 0.1606  33  MET A CG  
255  S SD  . MET A 33  ? 1.1493 1.5156 1.1955 -0.2276 -0.1088 0.1911  33  MET A SD  
256  C CE  . MET A 33  ? 1.1076 1.4870 1.1271 -0.2641 -0.1260 0.2159  33  MET A CE  
257  N N   . ALA A 34  ? 0.6116 0.9888 0.6815 -0.1762 -0.0403 0.1101  34  ALA A N   
258  C CA  . ALA A 34  ? 0.5440 0.9375 0.6135 -0.1814 -0.0358 0.1009  34  ALA A CA  
259  C C   . ALA A 34  ? 0.5495 0.9293 0.6383 -0.1605 -0.0287 0.0915  34  ALA A C   
260  O O   . ALA A 34  ? 0.5492 0.9099 0.6508 -0.1442 -0.0317 0.0979  34  ALA A O   
261  C CB  . ALA A 34  ? 0.4866 0.8886 0.5491 -0.1962 -0.0518 0.1190  34  ALA A CB  
262  N N   . ILE A 35  ? 0.5192 0.9112 0.6106 -0.1628 -0.0195 0.0753  35  ILE A N   
263  C CA  . ILE A 35  ? 0.4960 0.8781 0.6039 -0.1485 -0.0145 0.0683  35  ILE A CA  
264  C C   . ILE A 35  ? 0.5101 0.9094 0.6175 -0.1592 -0.0144 0.0611  35  ILE A C   
265  O O   . ILE A 35  ? 0.5096 0.9267 0.6119 -0.1707 -0.0085 0.0449  35  ILE A O   
266  C CB  . ILE A 35  ? 0.5125 0.8851 0.6302 -0.1376 -0.0042 0.0533  35  ILE A CB  
267  C CG1 . ILE A 35  ? 0.5060 0.8622 0.6237 -0.1271 -0.0044 0.0602  35  ILE A CG1 
268  C CG2 . ILE A 35  ? 0.4815 0.8456 0.6144 -0.1283 -0.0017 0.0492  35  ILE A CG2 
269  C CD1 . ILE A 35  ? 0.4708 0.8184 0.5971 -0.1185 0.0031  0.0475  35  ILE A CD1 
270  N N   . ALA A 36  ? 0.5401 0.9367 0.6549 -0.1558 -0.0207 0.0708  36  ALA A N   
271  C CA  . ALA A 36  ? 0.5415 0.9540 0.6561 -0.1663 -0.0224 0.0660  36  ALA A CA  
272  C C   . ALA A 36  ? 0.5087 0.9125 0.6397 -0.1552 -0.0250 0.0724  36  ALA A C   
273  O O   . ALA A 36  ? 0.5394 0.9303 0.6793 -0.1425 -0.0276 0.0823  36  ALA A O   
274  C CB  . ALA A 36  ? 0.5429 0.9739 0.6403 -0.1856 -0.0330 0.0769  36  ALA A CB  
275  N N   . PRO A 37  ? 0.5178 0.9312 0.6544 -0.1606 -0.0241 0.0650  37  PRO A N   
276  C CA  . PRO A 37  ? 0.5195 0.9290 0.6717 -0.1528 -0.0265 0.0714  37  PRO A CA  
277  C C   . PRO A 37  ? 0.5284 0.9390 0.6853 -0.1493 -0.0377 0.0884  37  PRO A C   
278  O O   . PRO A 37  ? 0.5379 0.9451 0.7113 -0.1385 -0.0379 0.0923  37  PRO A O   
279  C CB  . PRO A 37  ? 0.5288 0.9522 0.6825 -0.1643 -0.0265 0.0614  37  PRO A CB  
280  C CG  . PRO A 37  ? 0.5308 0.9585 0.6781 -0.1710 -0.0193 0.0427  37  PRO A CG  
281  C CD  . PRO A 37  ? 0.5267 0.9560 0.6586 -0.1737 -0.0196 0.0471  37  PRO A CD  
282  N N   . ALA A 38  ? 0.5253 0.9424 0.6706 -0.1594 -0.0483 0.0983  38  ALA A N   
283  C CA  . ALA A 38  ? 0.5107 0.9242 0.6653 -0.1551 -0.0630 0.1151  38  ALA A CA  
284  C C   . ALA A 38  ? 0.6062 1.0194 0.7436 -0.1669 -0.0731 0.1261  38  ALA A C   
285  O O   . ALA A 38  ? 0.6510 1.0764 0.7671 -0.1834 -0.0696 0.1213  38  ALA A O   
286  C CB  . ALA A 38  ? 0.5966 1.0224 0.7627 -0.1596 -0.0742 0.1221  38  ALA A CB  
287  N N   . LEU A 39  ? 0.6122 1.0132 0.7610 -0.1593 -0.0860 0.1397  39  LEU A N   
288  C CA  . LEU A 39  ? 0.5954 0.9925 0.7308 -0.1711 -0.0991 0.1544  39  LEU A CA  
289  C C   . LEU A 39  ? 0.6947 1.0863 0.8487 -0.1706 -0.1241 0.1741  39  LEU A C   
290  O O   . LEU A 39  ? 0.6944 1.0710 0.8747 -0.1526 -0.1305 0.1755  39  LEU A O   
291  C CB  . LEU A 39  ? 0.5928 0.9740 0.7265 -0.1611 -0.0911 0.1499  39  LEU A CB  
292  C CG  . LEU A 39  ? 0.5854 0.9718 0.7025 -0.1636 -0.0707 0.1322  39  LEU A CG  
293  C CD1 . LEU A 39  ? 0.5549 0.9248 0.6741 -0.1518 -0.0646 0.1289  39  LEU A CD1 
294  C CD2 . LEU A 39  ? 0.5365 0.9436 0.6278 -0.1883 -0.0706 0.1317  39  LEU A CD2 
295  N N   . ASP A 40  ? 0.6652 1.0705 0.8080 -0.1907 -0.1393 0.1879  40  ASP A N   
296  C CA  . ASP A 40  ? 0.6464 1.0459 0.8073 -0.1937 -0.1682 0.2100  40  ASP A CA  
297  C C   . ASP A 40  ? 0.6555 1.0427 0.8058 -0.2058 -0.1852 0.2295  40  ASP A C   
298  O O   . ASP A 40  ? 0.7304 1.1273 0.8590 -0.2320 -0.2016 0.2489  40  ASP A O   
299  C CB  . ASP A 40  ? 0.7125 1.1324 0.8646 -0.2123 -0.1792 0.2187  40  ASP A CB  
300  C CG  . ASP A 40  ? 0.7368 1.1502 0.9131 -0.2143 -0.2120 0.2423  40  ASP A CG  
301  O OD1 . ASP A 40  ? 0.7418 1.1350 0.9513 -0.1953 -0.2240 0.2460  40  ASP A OD1 
302  O OD2 . ASP A 40  ? 0.7929 1.2220 0.9569 -0.2352 -0.2272 0.2564  40  ASP A OD2 
303  N N   . VAL A 41  ? 0.6775 1.0444 0.8426 -0.1881 -0.1815 0.2243  41  VAL A N   
304  C CA  . VAL A 41  ? 0.7171 1.0695 0.8747 -0.1974 -0.1957 0.2405  41  VAL A CA  
305  C C   . VAL A 41  ? 0.7325 1.0596 0.9318 -0.1766 -0.2150 0.2460  41  VAL A C   
306  O O   . VAL A 41  ? 0.7500 1.0731 0.9794 -0.1514 -0.2062 0.2283  41  VAL A O   
307  C CB  . VAL A 41  ? 0.7189 1.0720 0.8523 -0.1984 -0.1719 0.2262  41  VAL A CB  
308  C CG1 . VAL A 41  ? 0.7128 1.0934 0.8111 -0.2190 -0.1545 0.2170  41  VAL A CG1 
309  C CG2 . VAL A 41  ? 0.6240 0.9662 0.7773 -0.1695 -0.1516 0.2031  41  VAL A CG2 
310  N N   . ALA A 42  ? 0.7968 1.1088 0.9993 -0.1889 -0.2426 0.2701  42  ALA A N   
311  C CA  . ALA A 42  ? 0.7663 1.0518 1.0117 -0.1699 -0.2635 0.2738  42  ALA A CA  
312  C C   . ALA A 42  ? 0.7608 1.0329 1.0051 -0.1564 -0.2465 0.2584  42  ALA A C   
313  O O   . ALA A 42  ? 0.7862 1.0613 0.9957 -0.1719 -0.2356 0.2617  42  ALA A O   
314  C CB  . ALA A 42  ? 0.8108 1.0817 1.0630 -0.1898 -0.3038 0.3081  42  ALA A CB  
315  N N   . ALA A 43  ? 0.7646 1.0252 1.0479 -0.1280 -0.2439 0.2399  43  ALA A N   
316  C CA  . ALA A 43  ? 0.7631 1.0134 1.0473 -0.1134 -0.2266 0.2223  43  ALA A CA  
317  C C   . ALA A 43  ? 0.7769 1.0042 1.1080 -0.0957 -0.2488 0.2201  43  ALA A C   
318  O O   . ALA A 43  ? 0.8851 1.1092 1.2579 -0.0848 -0.2692 0.2204  43  ALA A O   
319  C CB  . ALA A 43  ? 0.7699 1.0364 1.0506 -0.0965 -0.1931 0.1937  43  ALA A CB  
320  N N   . GLU A 44  ? 0.7536 0.9655 1.0807 -0.0925 -0.2453 0.2161  44  GLU A N   
321  C CA  . GLU A 44  ? 0.7547 0.9459 1.1281 -0.0729 -0.2620 0.2065  44  GLU A CA  
322  C C   . GLU A 44  ? 0.7349 0.9401 1.1396 -0.0454 -0.2436 0.1728  44  GLU A C   
323  O O   . GLU A 44  ? 0.7212 0.9212 1.1774 -0.0280 -0.2610 0.1619  44  GLU A O   
324  C CB  . GLU A 44  ? 0.7919 0.9659 1.1504 -0.0771 -0.2600 0.2083  44  GLU A CB  
325  C CG  . GLU A 44  ? 0.8888 1.0429 1.2376 -0.1014 -0.2902 0.2418  44  GLU A CG  
326  C CD  . GLU A 44  ? 0.9882 1.1163 1.3907 -0.0940 -0.3307 0.2527  44  GLU A CD  
327  O OE1 . GLU A 44  ? 0.9679 1.0987 1.3938 -0.0939 -0.3503 0.2621  44  GLU A OE1 
328  O OE2 . GLU A 44  ? 1.0812 1.1857 1.5056 -0.0879 -0.3445 0.2511  44  GLU A OE2 
329  N N   . GLN A 45  ? 0.6699 0.8946 1.0459 -0.0423 -0.2094 0.1557  45  GLN A N   
330  C CA  . GLN A 45  ? 0.6323 0.8755 1.0295 -0.0218 -0.1894 0.1258  45  GLN A CA  
331  C C   . GLN A 45  ? 0.6258 0.8927 0.9919 -0.0283 -0.1641 0.1222  45  GLN A C   
332  O O   . GLN A 45  ? 0.6129 0.8806 0.9368 -0.0426 -0.1505 0.1309  45  GLN A O   
333  C CB  . GLN A 45  ? 0.6453 0.8841 1.0440 -0.0099 -0.1751 0.1056  45  GLN A CB  
334  C CG  . GLN A 45  ? 0.6672 0.8855 1.1089 0.0019  -0.1991 0.1001  45  GLN A CG  
335  C CD  . GLN A 45  ? 0.7347 0.9373 1.1595 0.0008  -0.1935 0.0974  45  GLN A CD  
336  O OE1 . GLN A 45  ? 0.7397 0.9327 1.1252 -0.0165 -0.1910 0.1168  45  GLN A OE1 
337  N NE2 . GLN A 45  ? 0.7269 0.9301 1.1826 0.0186  -0.1910 0.0711  45  GLN A NE2 
338  N N   . VAL A 46  ? 0.5636 0.8506 0.9539 -0.0179 -0.1587 0.1081  46  VAL A N   
339  C CA  . VAL A 46  ? 0.5718 0.8807 0.9396 -0.0241 -0.1384 0.1052  46  VAL A CA  
340  C C   . VAL A 46  ? 0.5426 0.8726 0.9229 -0.0103 -0.1163 0.0787  46  VAL A C   
341  O O   . VAL A 46  ? 0.5871 0.9244 1.0071 0.0051  -0.1213 0.0607  46  VAL A O   
342  C CB  . VAL A 46  ? 0.5324 0.8498 0.9139 -0.0301 -0.1541 0.1171  46  VAL A CB  
343  C CG1 . VAL A 46  ? 0.5122 0.8492 0.8671 -0.0391 -0.1342 0.1157  46  VAL A CG1 
344  C CG2 . VAL A 46  ? 0.5675 0.8660 0.9397 -0.0459 -0.1803 0.1448  46  VAL A CG2 
345  N N   . ILE A 47  ? 0.5521 0.8938 0.9003 -0.0172 -0.0930 0.0757  47  ILE A N   
346  C CA  . ILE A 47  ? 0.5077 0.8719 0.8600 -0.0101 -0.0720 0.0553  47  ILE A CA  
347  C C   . ILE A 47  ? 0.5063 0.8876 0.8428 -0.0198 -0.0600 0.0589  47  ILE A C   
348  O O   . ILE A 47  ? 0.4864 0.8590 0.7902 -0.0320 -0.0544 0.0710  47  ILE A O   
349  C CB  . ILE A 47  ? 0.5041 0.8618 0.8328 -0.0098 -0.0570 0.0487  47  ILE A CB  
350  C CG1 . ILE A 47  ? 0.5489 0.8932 0.8986 0.0012  -0.0680 0.0406  47  ILE A CG1 
351  C CG2 . ILE A 47  ? 0.4840 0.8671 0.8075 -0.0094 -0.0357 0.0336  47  ILE A CG2 
352  C CD1 . ILE A 47  ? 0.5545 0.9005 0.8899 0.0042  -0.0527 0.0277  47  ILE A CD1 
353  N N   . ASP A 48  ? 0.4643 0.8711 0.8268 -0.0146 -0.0565 0.0465  48  ASP A N   
354  C CA  . ASP A 48  ? 0.4731 0.8984 0.8242 -0.0240 -0.0448 0.0483  48  ASP A CA  
355  C C   . ASP A 48  ? 0.4949 0.9301 0.8237 -0.0284 -0.0234 0.0407  48  ASP A C   
356  O O   . ASP A 48  ? 0.4863 0.9459 0.8302 -0.0238 -0.0132 0.0240  48  ASP A O   
357  C CB  . ASP A 48  ? 0.4576 0.9091 0.8469 -0.0181 -0.0498 0.0380  48  ASP A CB  
358  C CG  . ASP A 48  ? 0.4731 0.9451 0.8522 -0.0289 -0.0381 0.0399  48  ASP A CG  
359  O OD1 . ASP A 48  ? 0.4519 0.9123 0.7966 -0.0412 -0.0312 0.0521  48  ASP A OD1 
360  O OD2 . ASP A 48  ? 0.4773 0.9779 0.8859 -0.0253 -0.0365 0.0277  48  ASP A OD2 
361  N N   . GLY A 49  ? 0.4738 0.8923 0.7680 -0.0385 -0.0175 0.0524  49  GLY A N   
362  C CA  . GLY A 49  ? 0.4954 0.9183 0.7688 -0.0440 -0.0017 0.0493  49  GLY A CA  
363  C C   . GLY A 49  ? 0.5136 0.9495 0.7776 -0.0559 0.0065  0.0538  49  GLY A C   
364  O O   . GLY A 49  ? 0.5202 0.9463 0.7613 -0.0645 0.0126  0.0605  49  GLY A O   
365  N N   . GLN A 50  ? 0.5170 0.9745 0.8014 -0.0565 0.0050  0.0502  50  GLN A N   
366  C CA  . GLN A 50  ? 0.5243 0.9948 0.8020 -0.0691 0.0116  0.0549  50  GLN A CA  
367  C C   . GLN A 50  ? 0.5390 1.0262 0.8067 -0.0766 0.0252  0.0508  50  GLN A C   
368  O O   . GLN A 50  ? 0.5209 1.0260 0.7978 -0.0711 0.0313  0.0380  50  GLN A O   
369  C CB  . GLN A 50  ? 0.5169 1.0103 0.8213 -0.0682 0.0069  0.0507  50  GLN A CB  
370  C CG  . GLN A 50  ? 0.5160 1.0454 0.8476 -0.0631 0.0140  0.0334  50  GLN A CG  
371  C CD  . GLN A 50  ? 0.5624 1.1194 0.8881 -0.0778 0.0270  0.0326  50  GLN A CD  
372  O OE1 . GLN A 50  ? 0.6354 1.1812 0.9411 -0.0907 0.0278  0.0464  50  GLN A OE1 
373  N NE2 . GLN A 50  ? 0.6403 1.2350 0.9848 -0.0771 0.0368  0.0154  50  GLN A NE2 
374  N N   . GLY A 51  ? 0.5611 1.0429 0.8106 -0.0904 0.0286  0.0616  51  GLY A N   
375  C CA  . GLY A 51  ? 0.5617 1.0559 0.7977 -0.1019 0.0379  0.0636  51  GLY A CA  
376  C C   . GLY A 51  ? 0.5301 1.0093 0.7490 -0.0993 0.0399  0.0641  51  GLY A C   
377  O O   . GLY A 51  ? 0.5589 1.0486 0.7642 -0.1108 0.0458  0.0677  51  GLY A O   
378  N N   . ARG A 52  ? 0.5564 1.0125 0.7745 -0.0866 0.0342  0.0619  52  ARG A N   
379  C CA  . ARG A 52  ? 0.5240 0.9650 0.7273 -0.0834 0.0353  0.0618  52  ARG A CA  
380  C C   . ARG A 52  ? 0.5544 0.9629 0.7424 -0.0858 0.0290  0.0733  52  ARG A C   
381  O O   . ARG A 52  ? 0.5709 0.9688 0.7611 -0.0878 0.0238  0.0781  52  ARG A O   
382  C CB  . ARG A 52  ? 0.5241 0.9642 0.7402 -0.0681 0.0330  0.0495  52  ARG A CB  
383  C CG  . ARG A 52  ? 0.5262 0.9977 0.7554 -0.0649 0.0410  0.0325  52  ARG A CG  
384  C CD  . ARG A 52  ? 0.5670 1.0710 0.8183 -0.0671 0.0446  0.0240  52  ARG A CD  
385  N NE  . ARG A 52  ? 0.5627 1.1055 0.8255 -0.0681 0.0553  0.0048  52  ARG A NE  
386  C CZ  . ARG A 52  ? 0.5600 1.1414 0.8410 -0.0732 0.0622  -0.0063 52  ARG A CZ  
387  N NH1 . ARG A 52  ? 0.5295 1.1136 0.8194 -0.0772 0.0586  0.0017  52  ARG A NH1 
388  N NH2 . ARG A 52  ? 0.5974 1.2189 0.8886 -0.0752 0.0735  -0.0275 52  ARG A NH2 
389  N N   . VAL A 53  ? 0.5405 0.9360 0.7147 -0.0857 0.0295  0.0755  53  VAL A N   
390  C CA  . VAL A 53  ? 0.5352 0.9029 0.6994 -0.0865 0.0237  0.0825  53  VAL A CA  
391  C C   . VAL A 53  ? 0.4939 0.8482 0.6565 -0.0754 0.0216  0.0770  53  VAL A C   
392  O O   . VAL A 53  ? 0.5156 0.8751 0.6763 -0.0704 0.0245  0.0716  53  VAL A O   
393  C CB  . VAL A 53  ? 0.4808 0.8425 0.6333 -0.0968 0.0228  0.0916  53  VAL A CB  
394  C CG1 . VAL A 53  ? 0.4701 0.8049 0.6185 -0.0936 0.0163  0.0940  53  VAL A CG1 
395  C CG2 . VAL A 53  ? 0.5108 0.8790 0.6656 -0.1104 0.0209  0.1006  53  VAL A CG2 
396  N N   . LEU A 54  ? 0.4898 0.8292 0.6529 -0.0732 0.0164  0.0778  54  LEU A N   
397  C CA  . LEU A 54  ? 0.5194 0.8455 0.6785 -0.0667 0.0135  0.0753  54  LEU A CA  
398  C C   . LEU A 54  ? 0.5080 0.8188 0.6589 -0.0698 0.0124  0.0770  54  LEU A C   
399  O O   . LEU A 54  ? 0.5211 0.8265 0.6740 -0.0748 0.0102  0.0773  54  LEU A O   
400  C CB  . LEU A 54  ? 0.5272 0.8518 0.6909 -0.0658 0.0079  0.0755  54  LEU A CB  
401  C CG  . LEU A 54  ? 0.4911 0.8051 0.6510 -0.0620 0.0034  0.0751  54  LEU A CG  
402  C CD1 . LEU A 54  ? 0.4788 0.7939 0.6449 -0.0531 0.0031  0.0712  54  LEU A CD1 
403  C CD2 . LEU A 54  ? 0.5258 0.8408 0.6875 -0.0660 -0.0043 0.0792  54  LEU A CD2 
404  N N   . ALA A 55  ? 0.4635 0.7682 0.6082 -0.0664 0.0132  0.0762  55  ALA A N   
405  C CA  . ALA A 55  ? 0.4945 0.7859 0.6352 -0.0682 0.0108  0.0776  55  ALA A CA  
406  C C   . ALA A 55  ? 0.4883 0.7717 0.6252 -0.0625 0.0099  0.0734  55  ALA A C   
407  O O   . ALA A 55  ? 0.4812 0.7679 0.6173 -0.0576 0.0106  0.0711  55  ALA A O   
408  C CB  . ALA A 55  ? 0.4953 0.7888 0.6307 -0.0732 0.0107  0.0839  55  ALA A CB  
409  N N   . PRO A 56  ? 0.5168 0.7898 0.6546 -0.0632 0.0072  0.0714  56  PRO A N   
410  C CA  . PRO A 56  ? 0.5135 0.7810 0.6477 -0.0593 0.0067  0.0676  56  PRO A CA  
411  C C   . PRO A 56  ? 0.4846 0.7511 0.6121 -0.0557 0.0072  0.0695  56  PRO A C   
412  O O   . PRO A 56  ? 0.4958 0.7660 0.6201 -0.0584 0.0076  0.0739  56  PRO A O   
413  C CB  . PRO A 56  ? 0.4639 0.7248 0.6055 -0.0611 0.0038  0.0628  56  PRO A CB  
414  C CG  . PRO A 56  ? 0.4976 0.7601 0.6486 -0.0655 0.0024  0.0617  56  PRO A CG  
415  C CD  . PRO A 56  ? 0.4815 0.7483 0.6282 -0.0674 0.0034  0.0706  56  PRO A CD  
416  N N   . GLY A 57  ? 0.4732 0.7365 0.5979 -0.0517 0.0068  0.0663  57  GLY A N   
417  C CA  . GLY A 57  ? 0.5105 0.7736 0.6298 -0.0483 0.0071  0.0650  57  GLY A CA  
418  C C   . GLY A 57  ? 0.5152 0.7738 0.6303 -0.0512 0.0048  0.0684  57  GLY A C   
419  O O   . GLY A 57  ? 0.5114 0.7619 0.6316 -0.0523 0.0010  0.0684  57  GLY A O   
420  N N   . PHE A 58  ? 0.5068 0.7730 0.6142 -0.0537 0.0059  0.0706  58  PHE A N   
421  C CA  . PHE A 58  ? 0.5338 0.7963 0.6358 -0.0597 0.0006  0.0780  58  PHE A CA  
422  C C   . PHE A 58  ? 0.5089 0.7623 0.6097 -0.0562 -0.0035 0.0754  58  PHE A C   
423  O O   . PHE A 58  ? 0.5006 0.7557 0.5981 -0.0514 -0.0005 0.0681  58  PHE A O   
424  C CB  . PHE A 58  ? 0.5256 0.8046 0.6158 -0.0675 0.0032  0.0819  58  PHE A CB  
425  C CG  . PHE A 58  ? 0.5274 0.8194 0.6198 -0.0720 0.0079  0.0837  58  PHE A CG  
426  C CD1 . PHE A 58  ? 0.5187 0.8023 0.6213 -0.0726 0.0053  0.0879  58  PHE A CD1 
427  C CD2 . PHE A 58  ? 0.5492 0.8649 0.6354 -0.0760 0.0153  0.0786  58  PHE A CD2 
428  C CE1 . PHE A 58  ? 0.4759 0.7718 0.5810 -0.0772 0.0091  0.0898  58  PHE A CE1 
429  C CE2 . PHE A 58  ? 0.5338 0.8644 0.6241 -0.0806 0.0198  0.0793  58  PHE A CE2 
430  C CZ  . PHE A 58  ? 0.4970 0.8164 0.5961 -0.0812 0.0163  0.0862  58  PHE A CZ  
431  N N   . ILE A 59  ? 0.4995 0.7425 0.6063 -0.0586 -0.0117 0.0806  59  ILE A N   
432  C CA  . ILE A 59  ? 0.5481 0.7831 0.6583 -0.0553 -0.0167 0.0777  59  ILE A CA  
433  C C   . ILE A 59  ? 0.5320 0.7660 0.6344 -0.0620 -0.0254 0.0877  59  ILE A C   
434  O O   . ILE A 59  ? 0.5960 0.8241 0.7048 -0.0680 -0.0351 0.0981  59  ILE A O   
435  C CB  . ILE A 59  ? 0.5724 0.7995 0.7018 -0.0521 -0.0206 0.0723  59  ILE A CB  
436  C CG1 . ILE A 59  ? 0.4744 0.7067 0.6074 -0.0502 -0.0125 0.0647  59  ILE A CG1 
437  C CG2 . ILE A 59  ? 0.5603 0.7836 0.6950 -0.0488 -0.0242 0.0668  59  ILE A CG2 
438  C CD1 . ILE A 59  ? 0.4987 0.7308 0.6500 -0.0495 -0.0140 0.0555  59  ILE A CD1 
439  N N   . ASP A 60  ? 0.5438 0.7835 0.6332 -0.0623 -0.0238 0.0852  60  ASP A N   
440  C CA  . ASP A 60  ? 0.5988 0.8411 0.6768 -0.0711 -0.0325 0.0949  60  ASP A CA  
441  C C   . ASP A 60  ? 0.5890 0.8178 0.6795 -0.0676 -0.0433 0.0957  60  ASP A C   
442  O O   . ASP A 60  ? 0.5403 0.7689 0.6297 -0.0624 -0.0409 0.0870  60  ASP A O   
443  C CB  . ASP A 60  ? 0.5813 0.8406 0.6403 -0.0741 -0.0248 0.0883  60  ASP A CB  
444  C CG  . ASP A 60  ? 0.6119 0.8821 0.6529 -0.0886 -0.0320 0.0997  60  ASP A CG  
445  O OD1 . ASP A 60  ? 0.6330 0.8936 0.6774 -0.0964 -0.0457 0.1160  60  ASP A OD1 
446  O OD2 . ASP A 60  ? 0.5920 0.8818 0.6170 -0.0934 -0.0251 0.0918  60  ASP A OD2 
447  N N   . VAL A 61  ? 0.5817 0.7994 0.6876 -0.0705 -0.0566 0.1054  61  VAL A N   
448  C CA  . VAL A 61  ? 0.6323 0.8386 0.7592 -0.0653 -0.0680 0.1030  61  VAL A CA  
449  C C   . VAL A 61  ? 0.6756 0.8816 0.7933 -0.0709 -0.0792 0.1114  61  VAL A C   
450  O O   . VAL A 61  ? 0.7140 0.9129 0.8495 -0.0658 -0.0880 0.1075  61  VAL A O   
451  C CB  . VAL A 61  ? 0.5984 0.7921 0.7531 -0.0650 -0.0813 0.1076  61  VAL A CB  
452  C CG1 . VAL A 61  ? 0.5580 0.7537 0.7237 -0.0594 -0.0704 0.0961  61  VAL A CG1 
453  C CG2 . VAL A 61  ? 0.6060 0.7952 0.7527 -0.0784 -0.0955 0.1293  61  VAL A CG2 
454  N N   . HIS A 62  ? 0.6163 0.8330 0.7072 -0.0825 -0.0790 0.1215  62  HIS A N   
455  C CA  . HIS A 62  ? 0.6748 0.8947 0.7526 -0.0912 -0.0902 0.1305  62  HIS A CA  
456  C C   . HIS A 62  ? 0.6943 0.9345 0.7432 -0.0958 -0.0762 0.1224  62  HIS A C   
457  O O   . HIS A 62  ? 0.7492 1.0057 0.7771 -0.1082 -0.0723 0.1285  62  HIS A O   
458  C CB  . HIS A 62  ? 0.6889 0.9040 0.7649 -0.1065 -0.1102 0.1545  62  HIS A CB  
459  C CG  . HIS A 62  ? 0.7526 0.9667 0.8222 -0.1154 -0.1275 0.1664  62  HIS A CG  
460  N ND1 . HIS A 62  ? 0.7713 0.9667 0.8695 -0.1123 -0.1496 0.1746  62  HIS A ND1 
461  C CD2 . HIS A 62  ? 0.8168 1.0481 0.8566 -0.1276 -0.1267 0.1699  62  HIS A CD2 
462  C CE1 . HIS A 62  ? 0.8638 1.0631 0.9487 -0.1225 -0.1629 0.1856  62  HIS A CE1 
463  N NE2 . HIS A 62  ? 0.9363 1.1581 0.9840 -0.1327 -0.1488 0.1830  62  HIS A NE2 
464  N N   . THR A 63  ? 0.6302 0.8710 0.6801 -0.0865 -0.0690 0.1070  63  THR A N   
465  C CA  . THR A 63  ? 0.6435 0.9015 0.6731 -0.0886 -0.0580 0.0950  63  THR A CA  
466  C C   . THR A 63  ? 0.6477 0.9042 0.6745 -0.0886 -0.0650 0.0916  63  THR A C   
467  O O   . THR A 63  ? 0.6770 0.9192 0.7207 -0.0842 -0.0760 0.0960  63  THR A O   
468  C CB  . THR A 63  ? 0.6521 0.9110 0.6885 -0.0765 -0.0422 0.0773  63  THR A CB  
469  O OG1 . THR A 63  ? 0.6568 0.9012 0.7104 -0.0656 -0.0430 0.0701  63  THR A OG1 
470  C CG2 . THR A 63  ? 0.6350 0.8935 0.6778 -0.0751 -0.0365 0.0806  63  THR A CG2 
471  N N   . HIS A 64  ? 0.7048 0.9787 0.7123 -0.0938 -0.0586 0.0815  64  HIS A N   
472  C CA  . HIS A 64  ? 0.7105 0.9852 0.7145 -0.0931 -0.0623 0.0734  64  HIS A CA  
473  C C   . HIS A 64  ? 0.6858 0.9658 0.6912 -0.0841 -0.0487 0.0505  64  HIS A C   
474  O O   . HIS A 64  ? 0.6906 0.9825 0.6853 -0.0875 -0.0474 0.0386  64  HIS A O   
475  C CB  . HIS A 64  ? 0.6825 0.9742 0.6624 -0.1108 -0.0717 0.0828  64  HIS A CB  
476  C CG  . HIS A 64  ? 0.7136 0.9953 0.6963 -0.1202 -0.0912 0.1080  64  HIS A CG  
477  N ND1 . HIS A 64  ? 0.7341 0.9986 0.7348 -0.1154 -0.1065 0.1148  64  HIS A ND1 
478  C CD2 . HIS A 64  ? 0.7786 1.0647 0.7519 -0.1347 -0.1001 0.1283  64  HIS A CD2 
479  C CE1 . HIS A 64  ? 0.7594 1.0164 0.7647 -0.1249 -0.1253 0.1375  64  HIS A CE1 
480  N NE2 . HIS A 64  ? 0.7822 1.0506 0.7700 -0.1375 -0.1225 0.1475  64  HIS A NE2 
481  N N   . ASP A 65  ? 0.7042 0.9751 0.7249 -0.0730 -0.0402 0.0443  65  ASP A N   
482  C CA  . ASP A 65  ? 0.7131 0.9850 0.7410 -0.0642 -0.0309 0.0253  65  ASP A CA  
483  C C   . ASP A 65  ? 0.6563 0.9103 0.6991 -0.0560 -0.0344 0.0206  65  ASP A C   
484  O O   . ASP A 65  ? 0.7029 0.9488 0.7583 -0.0483 -0.0302 0.0127  65  ASP A O   
485  C CB  . ASP A 65  ? 0.6727 0.9453 0.7086 -0.0590 -0.0224 0.0236  65  ASP A CB  
486  C CG  . ASP A 65  ? 0.7122 1.0038 0.7346 -0.0688 -0.0188 0.0298  65  ASP A CG  
487  O OD1 . ASP A 65  ? 0.8153 1.1272 0.8198 -0.0799 -0.0188 0.0272  65  ASP A OD1 
488  O OD2 . ASP A 65  ? 0.7033 0.9915 0.7318 -0.0673 -0.0161 0.0373  65  ASP A OD2 
489  N N   . ASP A 66  ? 0.6992 0.9478 0.7417 -0.0589 -0.0433 0.0265  66  ASP A N   
490  C CA  . ASP A 66  ? 0.6465 0.8819 0.7029 -0.0537 -0.0465 0.0224  66  ASP A CA  
491  C C   . ASP A 66  ? 0.6772 0.9117 0.7358 -0.0503 -0.0434 0.0062  66  ASP A C   
492  O O   . ASP A 66  ? 0.6835 0.9064 0.7555 -0.0452 -0.0422 0.0030  66  ASP A O   
493  C CB  . ASP A 66  ? 0.6729 0.9073 0.7292 -0.0582 -0.0571 0.0289  66  ASP A CB  
494  C CG  . ASP A 66  ? 0.6095 0.8419 0.6719 -0.0603 -0.0642 0.0439  66  ASP A CG  
495  O OD1 . ASP A 66  ? 0.6138 0.8525 0.6652 -0.0658 -0.0651 0.0524  66  ASP A OD1 
496  O OD2 . ASP A 66  ? 0.5920 0.8177 0.6724 -0.0573 -0.0698 0.0462  66  ASP A OD2 
497  N N   . ILE A 67  ? 0.7107 0.9580 0.7573 -0.0543 -0.0434 -0.0045 67  ILE A N   
498  C CA  . ILE A 67  ? 0.7464 0.9928 0.8000 -0.0503 -0.0425 -0.0237 67  ILE A CA  
499  C C   . ILE A 67  ? 0.7558 1.0107 0.8154 -0.0453 -0.0347 -0.0374 67  ILE A C   
500  O O   . ILE A 67  ? 0.7919 1.0376 0.8692 -0.0382 -0.0361 -0.0505 67  ILE A O   
501  C CB  . ILE A 67  ? 0.7745 1.0333 0.8152 -0.0573 -0.0467 -0.0330 67  ILE A CB  
502  C CG1 . ILE A 67  ? 0.7880 1.0390 0.8265 -0.0617 -0.0561 -0.0191 67  ILE A CG1 
503  C CG2 . ILE A 67  ? 0.8493 1.1057 0.9019 -0.0526 -0.0473 -0.0557 67  ILE A CG2 
504  C CD1 . ILE A 67  ? 0.7958 1.0291 0.8513 -0.0573 -0.0609 -0.0217 67  ILE A CD1 
505  N N   . ASN A 68  ? 0.7568 1.0292 0.8049 -0.0494 -0.0281 -0.0343 68  ASN A N   
506  C CA  . ASN A 68  ? 0.8127 1.1009 0.8674 -0.0458 -0.0200 -0.0513 68  ASN A CA  
507  C C   . ASN A 68  ? 0.7764 1.0481 0.8526 -0.0355 -0.0194 -0.0495 68  ASN A C   
508  O O   . ASN A 68  ? 0.7450 1.0213 0.8386 -0.0284 -0.0175 -0.0675 68  ASN A O   
509  C CB  . ASN A 68  ? 0.7654 1.0804 0.8001 -0.0564 -0.0131 -0.0469 68  ASN A CB  
510  C CG  . ASN A 68  ? 0.8324 1.1721 0.8451 -0.0694 -0.0133 -0.0542 68  ASN A CG  
511  O OD1 . ASN A 68  ? 0.8860 1.2178 0.8893 -0.0743 -0.0217 -0.0455 68  ASN A OD1 
512  N ND2 . ASN A 68  ? 0.8565 1.2296 0.8615 -0.0762 -0.0041 -0.0715 68  ASN A ND2 
513  N N   . VAL A 69  ? 0.7279 0.9823 0.8053 -0.0349 -0.0221 -0.0293 69  VAL A N   
514  C CA  . VAL A 69  ? 0.7399 0.9804 0.8348 -0.0280 -0.0228 -0.0257 69  VAL A CA  
515  C C   . VAL A 69  ? 0.7348 0.9577 0.8486 -0.0228 -0.0312 -0.0336 69  VAL A C   
516  O O   . VAL A 69  ? 0.7018 0.9150 0.8332 -0.0176 -0.0347 -0.0344 69  VAL A O   
517  C CB  . VAL A 69  ? 0.7148 0.9452 0.8059 -0.0308 -0.0232 -0.0051 69  VAL A CB  
518  C CG1 . VAL A 69  ? 0.7124 0.9563 0.7901 -0.0357 -0.0179 0.0033  69  VAL A CG1 
519  C CG2 . VAL A 69  ? 0.6836 0.9031 0.7729 -0.0343 -0.0292 0.0024  69  VAL A CG2 
520  N N   . ILE A 70  ? 0.7309 0.9488 0.8424 -0.0252 -0.0364 -0.0383 70  ILE A N   
521  C CA  . ILE A 70  ? 0.7531 0.9525 0.8830 -0.0224 -0.0465 -0.0440 70  ILE A CA  
522  C C   . ILE A 70  ? 0.7593 0.9645 0.9062 -0.0157 -0.0488 -0.0698 70  ILE A C   
523  O O   . ILE A 70  ? 0.8250 1.0149 0.9971 -0.0097 -0.0580 -0.0758 70  ILE A O   
524  C CB  . ILE A 70  ? 0.7505 0.9420 0.8725 -0.0289 -0.0517 -0.0370 70  ILE A CB  
525  C CG1 . ILE A 70  ? 0.7062 0.8914 0.8229 -0.0342 -0.0512 -0.0160 70  ILE A CG1 
526  C CG2 . ILE A 70  ? 0.7518 0.9270 0.8914 -0.0278 -0.0629 -0.0462 70  ILE A CG2 
527  C CD1 . ILE A 70  ? 0.6833 0.8634 0.7979 -0.0407 -0.0563 -0.0103 70  ILE A CD1 
528  N N   . ARG A 71  ? 0.7461 0.9747 0.8815 -0.0174 -0.0418 -0.0863 71  ARG A N   
529  C CA  . ARG A 71  ? 0.7852 1.0260 0.9391 -0.0114 -0.0421 -0.1168 71  ARG A CA  
530  C C   . ARG A 71  ? 0.7542 1.0165 0.9178 -0.0062 -0.0336 -0.1304 71  ARG A C   
531  O O   . ARG A 71  ? 0.7643 1.0382 0.9520 0.0009  -0.0342 -0.1593 71  ARG A O   
532  C CB  . ARG A 71  ? 0.8479 1.1086 0.9848 -0.0183 -0.0389 -0.1319 71  ARG A CB  
533  C CG  . ARG A 71  ? 0.8487 1.1363 0.9522 -0.0295 -0.0285 -0.1232 71  ARG A CG  
534  C CD  . ARG A 71  ? 0.9931 1.2935 1.0773 -0.0391 -0.0302 -0.1297 71  ARG A CD  
535  N NE  . ARG A 71  ? 1.0292 1.3392 1.1300 -0.0355 -0.0319 -0.1628 71  ARG A NE  
536  C CZ  . ARG A 71  ? 1.0410 1.3293 1.1583 -0.0313 -0.0426 -0.1698 71  ARG A CZ  
537  N NH1 . ARG A 71  ? 1.0286 1.2872 1.1459 -0.0316 -0.0516 -0.1459 71  ARG A NH1 
538  N NH2 . ARG A 71  ? 1.0227 1.3213 1.1587 -0.0275 -0.0445 -0.2033 71  ARG A NH2 
539  N N   . MET A 72  ? 0.7763 1.0455 0.9249 -0.0096 -0.0260 -0.1124 72  MET A N   
540  C CA  A MET A 72  ? 0.7384 1.0264 0.8979 -0.0054 -0.0185 -0.1218 72  MET A CA  
541  C CA  B MET A 72  ? 0.7390 1.0272 0.8980 -0.0055 -0.0184 -0.1215 72  MET A CA  
542  C C   . MET A 72  ? 0.7135 0.9821 0.8756 -0.0034 -0.0213 -0.0968 72  MET A C   
543  O O   . MET A 72  ? 0.7016 0.9801 0.8452 -0.0092 -0.0134 -0.0819 72  MET A O   
544  C CB  A MET A 72  ? 0.7486 1.0741 0.8828 -0.0156 -0.0047 -0.1274 72  MET A CB  
545  C CB  B MET A 72  ? 0.7496 1.0745 0.8822 -0.0161 -0.0046 -0.1255 72  MET A CB  
546  C CG  A MET A 72  ? 0.7223 1.0776 0.8724 -0.0121 0.0044  -0.1488 72  MET A CG  
547  C CG  B MET A 72  ? 0.7608 1.1050 0.8734 -0.0258 -0.0021 -0.1371 72  MET A CG  
548  S SD  A MET A 72  ? 0.8086 1.1997 0.9250 -0.0283 0.0188  -0.1370 72  MET A SD  
549  S SD  B MET A 72  ? 0.7504 1.1262 0.8223 -0.0449 0.0080  -0.1213 72  MET A SD  
550  C CE  A MET A 72  ? 0.7637 1.1597 0.8419 -0.0445 0.0174  -0.1247 72  MET A CE  
551  C CE  B MET A 72  ? 0.7621 1.1575 0.8455 -0.0422 0.0181  -0.1254 72  MET A CE  
552  N N   . PRO A 73  ? 0.7395 0.9805 0.9246 0.0030  -0.0338 -0.0912 73  PRO A N   
553  C CA  . PRO A 73  ? 0.7143 0.9394 0.8986 0.0018  -0.0369 -0.0669 73  PRO A CA  
554  C C   . PRO A 73  ? 0.6790 0.9210 0.8674 0.0045  -0.0292 -0.0683 73  PRO A C   
555  O O   . PRO A 73  ? 0.6352 0.8748 0.8098 -0.0001 -0.0256 -0.0486 73  PRO A O   
556  C CB  . PRO A 73  ? 0.7264 0.9236 0.9375 0.0061  -0.0540 -0.0644 73  PRO A CB  
557  C CG  . PRO A 73  ? 0.6951 0.8874 0.9137 0.0074  -0.0599 -0.0805 73  PRO A CG  
558  C CD  . PRO A 73  ? 0.7227 0.9461 0.9355 0.0096  -0.0473 -0.1056 73  PRO A CD  
559  N N   . GLU A 74  ? 0.6714 0.9326 0.8804 0.0118  -0.0264 -0.0933 74  GLU A N   
560  C CA  . GLU A 74  ? 0.6351 0.9175 0.8503 0.0138  -0.0183 -0.0975 74  GLU A CA  
561  C C   . GLU A 74  ? 0.6308 0.9444 0.8163 0.0036  -0.0024 -0.0994 74  GLU A C   
562  O O   . GLU A 74  ? 0.6481 0.9934 0.8366 0.0026  0.0062  -0.1234 74  GLU A O   
563  C CB  . GLU A 74  ? 0.6638 0.9557 0.9203 0.0261  -0.0236 -0.1256 74  GLU A CB  
564  C CG  . GLU A 74  ? 0.6511 0.9085 0.9394 0.0344  -0.0443 -0.1201 74  GLU A CG  
565  C CD  . GLU A 74  ? 0.7152 0.9796 1.0526 0.0483  -0.0533 -0.1487 74  GLU A CD  
566  O OE1 . GLU A 74  ? 0.8455 1.1462 1.1922 0.0517  -0.0407 -0.1764 74  GLU A OE1 
567  O OE2 . GLU A 74  ? 0.7268 0.9618 1.0953 0.0547  -0.0741 -0.1437 74  GLU A OE2 
568  N N   . TYR A 75  ? 0.6384 0.9440 0.7957 -0.0056 0.0003  -0.0736 75  TYR A N   
569  C CA  . TYR A 75  ? 0.6560 0.9833 0.7836 -0.0180 0.0100  -0.0677 75  TYR A CA  
570  C C   . TYR A 75  ? 0.6500 1.0028 0.7769 -0.0218 0.0194  -0.0694 75  TYR A C   
571  O O   . TYR A 75  ? 0.6981 1.0455 0.8148 -0.0266 0.0206  -0.0493 75  TYR A O   
572  C CB  . TYR A 75  ? 0.6587 0.9652 0.7653 -0.0247 0.0059  -0.0413 75  TYR A CB  
573  C CG  . TYR A 75  ? 0.7298 1.0465 0.8115 -0.0357 0.0071  -0.0371 75  TYR A CG  
574  C CD1 . TYR A 75  ? 0.6954 1.0038 0.7747 -0.0353 0.0017  -0.0429 75  TYR A CD1 
575  C CD2 . TYR A 75  ? 0.7696 1.1032 0.8307 -0.0479 0.0115  -0.0254 75  TYR A CD2 
576  C CE1 . TYR A 75  ? 0.7853 1.1033 0.8422 -0.0462 0.0007  -0.0377 75  TYR A CE1 
577  C CE2 . TYR A 75  ? 0.7408 1.0825 0.7797 -0.0598 0.0089  -0.0181 75  TYR A CE2 
578  C CZ  . TYR A 75  ? 0.8157 1.1501 0.8525 -0.0586 0.0036  -0.0246 75  TYR A CZ  
579  O OH  . TYR A 75  ? 0.8051 1.1480 0.8201 -0.0713 -0.0008 -0.0162 75  TYR A OH  
580  N N   . LEU A 76  ? 0.7320 0.8985 0.8341 0.1062  0.0131  0.0590  76  LEU A N   
581  C CA  . LEU A 76  ? 0.7652 0.9546 0.8905 0.1162  0.0171  0.0740  76  LEU A CA  
582  C C   . LEU A 76  ? 0.7286 0.9429 0.8759 0.1143  0.0188  0.0808  76  LEU A C   
583  O O   . LEU A 76  ? 0.7552 0.9890 0.9322 0.1127  0.0179  0.0913  76  LEU A O   
584  C CB  . LEU A 76  ? 0.7685 0.9522 0.8812 0.1357  0.0265  0.0789  76  LEU A CB  
585  C CG  . LEU A 76  ? 0.7810 0.9896 0.9196 0.1481  0.0326  0.0966  76  LEU A CG  
586  C CD1 . LEU A 76  ? 0.7500 0.9677 0.9104 0.1433  0.0259  0.1036  76  LEU A CD1 
587  C CD2 . LEU A 76  ? 0.7399 0.9419 0.8619 0.1693  0.0442  0.1010  76  LEU A CD2 
588  N N   . PRO A 77  ? 0.7640 0.9801 0.9006 0.1149  0.0215  0.0761  77  PRO A N   
589  C CA  . PRO A 77  ? 0.7756 1.0159 0.9353 0.1154  0.0255  0.0860  77  PRO A CA  
590  C C   . PRO A 77  ? 0.7054 0.9554 0.8932 0.1001  0.0195  0.0884  77  PRO A C   
591  O O   . PRO A 77  ? 0.6673 0.9367 0.8856 0.1015  0.0235  0.1005  77  PRO A O   
592  C CB  . PRO A 77  ? 0.7642 1.0016 0.9020 0.1163  0.0262  0.0774  77  PRO A CB  
593  C CG  . PRO A 77  ? 0.7905 1.0078 0.8963 0.1243  0.0263  0.0666  77  PRO A CG  
594  C CD  . PRO A 77  ? 0.9180 1.1167 1.0224 0.1184  0.0220  0.0631  77  PRO A CD  
595  N N   . LYS A 78  ? 0.6779 0.9143 0.8571 0.0858  0.0107  0.0772  78  LYS A N   
596  C CA  . LYS A 78  ? 0.6509 0.8937 0.8520 0.0723  0.0048  0.0771  78  LYS A CA  
597  C C   . LYS A 78  ? 0.6274 0.8705 0.8399 0.0699  -0.0016 0.0787  78  LYS A C   
598  O O   . LYS A 78  ? 0.5593 0.8158 0.7991 0.0637  -0.0052 0.0823  78  LYS A O   
599  C CB  . LYS A 78  ? 0.6123 0.8423 0.7984 0.0598  -0.0005 0.0654  78  LYS A CB  
600  C CG  . LYS A 78  ? 0.6518 0.8823 0.8236 0.0622  0.0033  0.0619  78  LYS A CG  
601  C CD  . LYS A 78  ? 0.6349 0.8817 0.8259 0.0592  0.0068  0.0678  78  LYS A CD  
602  C CE  . LYS A 78  ? 0.6637 0.9140 0.8384 0.0627  0.0091  0.0643  78  LYS A CE  
603  N NZ  . LYS A 78  ? 0.6681 0.9327 0.8596 0.0597  0.0127  0.0702  78  LYS A NZ  
604  N N   . LEU A 79  ? 0.6641 0.8932 0.8568 0.0752  -0.0032 0.0759  79  LEU A N   
605  C CA  . LEU A 79  ? 0.6394 0.8703 0.8396 0.0745  -0.0100 0.0779  79  LEU A CA  
606  C C   . LEU A 79  ? 0.6320 0.8857 0.8614 0.0826  -0.0082 0.0904  79  LEU A C   
607  O O   . LEU A 79  ? 0.6177 0.8842 0.8678 0.0779  -0.0164 0.0921  79  LEU A O   
608  C CB  . LEU A 79  ? 0.6762 0.8855 0.8483 0.0801  -0.0098 0.0741  79  LEU A CB  
609  C CG  . LEU A 79  ? 0.6297 0.8370 0.8008 0.0785  -0.0177 0.0744  79  LEU A CG  
610  C CD1 . LEU A 79  ? 0.6189 0.8249 0.7908 0.0644  -0.0257 0.0665  79  LEU A CD1 
611  C CD2 . LEU A 79  ? 0.7043 0.8885 0.8489 0.0862  -0.0140 0.0735  79  LEU A CD2 
612  N N   . SER A 80  ? 0.6787 0.9391 0.9107 0.0952  0.0023  0.0991  80  SER A N   
613  C CA  . SER A 80  ? 0.6381 0.9223 0.9020 0.1037  0.0064  0.1134  80  SER A CA  
614  C C   . SER A 80  ? 0.6020 0.9063 0.9041 0.0934  0.0046  0.1177  80  SER A C   
615  O O   . SER A 80  ? 0.5600 0.8854 0.8967 0.0946  0.0035  0.1273  80  SER A O   
616  C CB  . SER A 80  ? 0.6510 0.9367 0.9060 0.1214  0.0203  0.1225  80  SER A CB  
617  O OG  . SER A 80  ? 0.6720 0.9558 0.9180 0.1213  0.0266  0.1204  80  SER A OG  
618  N N   . GLN A 81  ? 0.5744 0.8728 0.8732 0.0836  0.0046  0.1110  81  GLN A N   
619  C CA  . GLN A 81  ? 0.5547 0.8669 0.8887 0.0726  0.0031  0.1132  81  GLN A CA  
620  C C   . GLN A 81  ? 0.5251 0.8357 0.8678 0.0584  -0.0116 0.1025  81  GLN A C   
621  O O   . GLN A 81  ? 0.5073 0.8314 0.8855 0.0499  -0.0152 0.1037  81  GLN A O   
622  C CB  . GLN A 81  ? 0.5181 0.8244 0.8445 0.0692  0.0095  0.1110  81  GLN A CB  
623  C CG  . GLN A 81  ? 0.5734 0.8824 0.8862 0.0842  0.0228  0.1199  81  GLN A CG  
624  C CD  . GLN A 81  ? 0.6008 0.9074 0.9058 0.0814  0.0275  0.1180  81  GLN A CD  
625  O OE1 . GLN A 81  ? 0.5249 0.8397 0.8571 0.0747  0.0304  0.1226  81  GLN A OE1 
626  N NE2 . GLN A 81  ? 0.6390 0.9343 0.9080 0.0867  0.0281  0.1108  81  GLN A NE2 
627  N N   . GLY A 82  ? 0.5358 0.8297 0.8471 0.0562  -0.0196 0.0919  82  GLY A N   
628  C CA  . GLY A 82  ? 0.5387 0.8286 0.8490 0.0447  -0.0326 0.0806  82  GLY A CA  
629  C C   . GLY A 82  ? 0.4878 0.7588 0.7739 0.0361  -0.0336 0.0695  82  GLY A C   
630  O O   . GLY A 82  ? 0.5309 0.7991 0.8183 0.0267  -0.0426 0.0603  82  GLY A O   
631  N N   . VAL A 83  ? 0.5701 0.8293 0.8348 0.0394  -0.0251 0.0697  83  VAL A N   
632  C CA  . VAL A 83  ? 0.5750 0.8190 0.8196 0.0316  -0.0254 0.0606  83  VAL A CA  
633  C C   . VAL A 83  ? 0.6012 0.8281 0.8162 0.0315  -0.0304 0.0539  83  VAL A C   
634  O O   . VAL A 83  ? 0.5937 0.8130 0.7924 0.0398  -0.0276 0.0564  83  VAL A O   
635  C CB  . VAL A 83  ? 0.5615 0.8037 0.7978 0.0351  -0.0156 0.0633  83  VAL A CB  
636  C CG1 . VAL A 83  ? 0.5139 0.7431 0.7318 0.0270  -0.0164 0.0546  83  VAL A CG1 
637  C CG2 . VAL A 83  ? 0.5385 0.7978 0.8042 0.0370  -0.0085 0.0726  83  VAL A CG2 
638  N N   . THR A 84  ? 0.5017 0.7214 0.7095 0.0233  -0.0364 0.0461  84  THR A N   
639  C CA  . THR A 84  ? 0.5316 0.7351 0.7122 0.0237  -0.0392 0.0417  84  THR A CA  
640  C C   . THR A 84  ? 0.5446 0.7338 0.7089 0.0172  -0.0350 0.0364  84  THR A C   
641  O O   . THR A 84  ? 0.5662 0.7405 0.7093 0.0176  -0.0344 0.0345  84  THR A O   
642  C CB  . THR A 84  ? 0.5378 0.7457 0.7194 0.0225  -0.0496 0.0380  84  THR A CB  
643  O OG1 . THR A 84  ? 0.5208 0.7320 0.7135 0.0135  -0.0530 0.0310  84  THR A OG1 
644  C CG2 . THR A 84  ? 0.5158 0.7412 0.7164 0.0288  -0.0552 0.0435  84  THR A CG2 
645  N N   . THR A 85  ? 0.5343 0.7286 0.7096 0.0118  -0.0312 0.0353  85  THR A N   
646  C CA  . THR A 85  ? 0.5402 0.7253 0.7041 0.0057  -0.0274 0.0313  85  THR A CA  
647  C C   . THR A 85  ? 0.5186 0.7132 0.6937 0.0054  -0.0215 0.0341  85  THR A C   
648  O O   . THR A 85  ? 0.5120 0.7193 0.7079 0.0062  -0.0200 0.0380  85  THR A O   
649  C CB  . THR A 85  ? 0.5597 0.7418 0.7234 -0.0005 -0.0304 0.0262  85  THR A CB  
650  O OG1 . THR A 85  ? 0.5813 0.7563 0.7307 0.0021  -0.0361 0.0241  85  THR A OG1 
651  C CG2 . THR A 85  ? 0.5117 0.6867 0.6667 -0.0058 -0.0248 0.0243  85  THR A CG2 
652  N N   . VAL A 86  ? 0.6065 0.7956 0.7690 0.0046  -0.0181 0.0323  86  VAL A N   
653  C CA  . VAL A 86  ? 0.6230 0.8232 0.7918 0.0058  -0.0136 0.0345  86  VAL A CA  
654  C C   . VAL A 86  ? 0.5558 0.7539 0.7209 -0.0017 -0.0122 0.0311  86  VAL A C   
655  O O   . VAL A 86  ? 0.5492 0.7346 0.7017 -0.0067 -0.0134 0.0267  86  VAL A O   
656  C CB  . VAL A 86  ? 0.5716 0.7715 0.7293 0.0129  -0.0122 0.0343  86  VAL A CB  
657  C CG1 . VAL A 86  ? 0.5602 0.7660 0.7248 0.0225  -0.0111 0.0404  86  VAL A CG1 
658  C CG2 . VAL A 86  ? 0.5515 0.7331 0.6898 0.0096  -0.0143 0.0272  86  VAL A CG2 
659  N N   . ILE A 87  ? 0.5485 0.7597 0.7266 -0.0017 -0.0083 0.0349  87  ILE A N   
660  C CA  . ILE A 87  ? 0.5430 0.7572 0.7209 -0.0069 -0.0061 0.0337  87  ILE A CA  
661  C C   . ILE A 87  ? 0.5070 0.7330 0.6812 -0.0034 -0.0057 0.0340  87  ILE A C   
662  O O   . ILE A 87  ? 0.5630 0.8036 0.7449 0.0044  -0.0026 0.0400  87  ILE A O   
663  C CB  . ILE A 87  ? 0.5327 0.7533 0.7269 -0.0079 -0.0015 0.0380  87  ILE A CB  
664  C CG1 . ILE A 87  ? 0.5170 0.7270 0.7147 -0.0105 -0.0039 0.0351  87  ILE A CG1 
665  C CG2 . ILE A 87  ? 0.5266 0.7498 0.7200 -0.0124 0.0017  0.0377  87  ILE A CG2 
666  C CD1 . ILE A 87  ? 0.5386 0.7334 0.7189 -0.0148 -0.0076 0.0289  87  ILE A CD1 
667  N N   . VAL A 88  ? 0.5999 0.8202 0.7628 -0.0085 -0.0088 0.0275  88  VAL A N   
668  C CA  . VAL A 88  ? 0.6454 0.8762 0.8027 -0.0061 -0.0113 0.0240  88  VAL A CA  
669  C C   . VAL A 88  ? 0.6412 0.8859 0.8062 -0.0110 -0.0109 0.0247  88  VAL A C   
670  O O   . VAL A 88  ? 0.6067 0.8492 0.7796 -0.0164 -0.0075 0.0277  88  VAL A O   
671  C CB  . VAL A 88  ? 0.6065 0.8210 0.7486 -0.0088 -0.0159 0.0145  88  VAL A CB  
672  C CG1 . VAL A 88  ? 0.6385 0.8391 0.7738 -0.0030 -0.0152 0.0157  88  VAL A CG1 
673  C CG2 . VAL A 88  ? 0.6225 0.8246 0.7645 -0.0204 -0.0166 0.0101  88  VAL A CG2 
674  N N   . GLY A 89  ? 0.6116 0.8723 0.7739 -0.0079 -0.0145 0.0218  89  GLY A N   
675  C CA  . GLY A 89  ? 0.5439 0.8227 0.7151 -0.0116 -0.0155 0.0228  89  GLY A CA  
676  C C   . GLY A 89  ? 0.5164 0.8153 0.7000 -0.0035 -0.0090 0.0348  89  GLY A C   
677  O O   . GLY A 89  ? 0.5431 0.8497 0.7382 -0.0073 -0.0056 0.0395  89  GLY A O   
678  N N   . ASN A 90  ? 0.4989 0.8060 0.6815 0.0085  -0.0058 0.0413  90  ASN A N   
679  C CA  . ASN A 90  ? 0.5375 0.8617 0.7339 0.0175  0.0027  0.0548  90  ASN A CA  
680  C C   . ASN A 90  ? 0.5659 0.9183 0.7592 0.0271  0.0004  0.0580  90  ASN A C   
681  O O   . ASN A 90  ? 0.6307 0.9893 0.8096 0.0277  -0.0088 0.0481  90  ASN A O   
682  C CB  . ASN A 90  ? 0.5455 0.8640 0.7476 0.0257  0.0096  0.0628  90  ASN A CB  
683  C CG  . ASN A 90  ? 0.6185 0.9143 0.8269 0.0172  0.0110  0.0604  90  ASN A CG  
684  O OD1 . ASN A 90  ? 0.6576 0.9499 0.8802 0.0147  0.0170  0.0654  90  ASN A OD1 
685  N ND2 . ASN A 90  ? 0.6157 0.8957 0.8125 0.0137  0.0054  0.0524  90  ASN A ND2 
686  N N   . CYS A 91  ? 0.5264 0.8960 0.7334 0.0353  0.0090  0.0718  91  CYS A N   
687  C CA  . CYS A 91  ? 0.5783 0.9786 0.7831 0.0487  0.0089  0.0791  91  CYS A CA  
688  C C   . CYS A 91  ? 0.6001 1.0170 0.7999 0.0425  -0.0027 0.0693  91  CYS A C   
689  O O   . CYS A 91  ? 0.5661 1.0054 0.7545 0.0509  -0.0102 0.0660  91  CYS A O   
690  C CB  . CYS A 91  ? 0.6105 1.0172 0.8010 0.0629  0.0090  0.0810  91  CYS A CB  
691  S SG  . CYS A 91  ? 0.6642 1.0548 0.8671 0.0694  0.0229  0.0938  91  CYS A SG  
692  N N   . GLY A 92  ? 0.5792 0.9862 0.7883 0.0280  -0.0043 0.0644  92  GLY A N   
693  C CA  . GLY A 92  ? 0.5880 1.0118 0.8002 0.0201  -0.0140 0.0568  92  GLY A CA  
694  C C   . GLY A 92  ? 0.6189 1.0359 0.8177 0.0111  -0.0279 0.0383  92  GLY A C   
695  O O   . GLY A 92  ? 0.5602 0.9902 0.7652 0.0020  -0.0370 0.0303  92  GLY A O   
696  N N   . ILE A 93  ? 0.5761 0.9727 0.7587 0.0131  -0.0293 0.0312  93  ILE A N   
697  C CA  . ILE A 93  ? 0.6016 0.9864 0.7703 0.0056  -0.0408 0.0130  93  ILE A CA  
698  C C   . ILE A 93  ? 0.5740 0.9231 0.7417 -0.0055 -0.0373 0.0085  93  ILE A C   
699  O O   . ILE A 93  ? 0.6276 0.9615 0.7938 -0.0007 -0.0288 0.0163  93  ILE A O   
700  C CB  . ILE A 93  ? 0.6590 1.0508 0.8062 0.0202  -0.0451 0.0082  93  ILE A CB  
701  C CG1 . ILE A 93  ? 0.6425 1.0248 0.7862 0.0329  -0.0329 0.0215  93  ILE A CG1 
702  C CG2 . ILE A 93  ? 0.6591 1.0885 0.8036 0.0310  -0.0516 0.0097  93  ILE A CG2 
703  C CD1 . ILE A 93  ? 0.6925 1.0769 0.8145 0.0479  -0.0344 0.0182  93  ILE A CD1 
704  N N   . SER A 94  ? 0.6666 1.0034 0.8368 -0.0200 -0.0437 -0.0033 94  SER A N   
705  C CA  . SER A 94  ? 0.6402 0.9441 0.8083 -0.0292 -0.0400 -0.0066 94  SER A CA  
706  C C   . SER A 94  ? 0.6438 0.9358 0.8105 -0.0414 -0.0484 -0.0224 94  SER A C   
707  O O   . SER A 94  ? 0.7240 1.0337 0.9017 -0.0489 -0.0561 -0.0289 94  SER A O   
708  C CB  . SER A 94  ? 0.6270 0.9243 0.8094 -0.0354 -0.0309 0.0039  94  SER A CB  
709  O OG  . SER A 94  ? 0.6065 0.9172 0.8051 -0.0452 -0.0329 0.0034  94  SER A OG  
710  N N   . ALA A 95  ? 0.5913 0.8533 0.7466 -0.0434 -0.0469 -0.0282 95  ALA A N   
711  C CA  . ALA A 95  ? 0.5889 0.8323 0.7445 -0.0553 -0.0522 -0.0424 95  ALA A CA  
712  C C   . ALA A 95  ? 0.5568 0.7900 0.7311 -0.0696 -0.0470 -0.0382 95  ALA A C   
713  O O   . ALA A 95  ? 0.6125 0.8405 0.7977 -0.0823 -0.0517 -0.0482 95  ALA A O   
714  C CB  . ALA A 95  ? 0.6162 0.8302 0.7529 -0.0500 -0.0501 -0.0480 95  ALA A CB  
715  N N   . ALA A 96  ? 0.5264 0.7566 0.7052 -0.0676 -0.0372 -0.0239 96  ALA A N   
716  C CA  . ALA A 96  ? 0.5720 0.7943 0.7662 -0.0783 -0.0305 -0.0178 96  ALA A CA  
717  C C   . ALA A 96  ? 0.5759 0.8266 0.7919 -0.0855 -0.0337 -0.0166 96  ALA A C   
718  O O   . ALA A 96  ? 0.6099 0.8875 0.8284 -0.0785 -0.0365 -0.0127 96  ALA A O   
719  C CB  . ALA A 96  ? 0.5449 0.7578 0.7340 -0.0719 -0.0201 -0.0046 96  ALA A CB  
720  N N   . THR A 97  ? 0.5555 0.8009 0.7896 -0.0991 -0.0325 -0.0186 97  THR A N   
721  C CA  . THR A 97  ? 0.5686 0.8407 0.8294 -0.1087 -0.0356 -0.0176 97  THR A CA  
722  C C   . THR A 97  ? 0.5976 0.8961 0.8625 -0.1103 -0.0513 -0.0311 97  THR A C   
723  O O   . THR A 97  ? 0.5900 0.9166 0.8783 -0.1175 -0.0563 -0.0309 97  THR A O   
724  C CB  . THR A 97  ? 0.5669 0.8588 0.8368 -0.1028 -0.0269 -0.0014 97  THR A CB  
725  O OG1 . THR A 97  ? 0.5641 0.8769 0.8238 -0.0900 -0.0310 0.0006  97  THR A OG1 
726  C CG2 . THR A 97  ? 0.5675 0.8345 0.8275 -0.0983 -0.0128 0.0101  97  THR A CG2 
727  N N   . ALA A 98  ? 0.6607 0.9532 0.9034 -0.1028 -0.0593 -0.0426 98  ALA A N   
728  C CA  . ALA A 98  ? 0.6211 0.9400 0.8620 -0.1010 -0.0746 -0.0558 98  ALA A CA  
729  C C   . ALA A 98  ? 0.6676 0.9796 0.9216 -0.1174 -0.0854 -0.0748 98  ALA A C   
730  O O   . ALA A 98  ? 0.6722 0.9494 0.9205 -0.1236 -0.0825 -0.0826 98  ALA A O   
731  C CB  . ALA A 98  ? 0.6426 0.9576 0.8530 -0.0845 -0.0773 -0.0598 98  ALA A CB  
732  N N   . THR A 99  ? 0.6815 1.0271 0.9545 -0.1243 -0.0980 -0.0823 99  THR A N   
733  C CA  . THR A 99  ? 0.7168 1.0614 1.0062 -0.1411 -0.1115 -0.1033 99  THR A CA  
734  C C   . THR A 99  ? 0.7574 1.1335 1.0352 -0.1345 -0.1309 -0.1199 99  THR A C   
735  O O   . THR A 99  ? 0.7168 1.1307 0.9940 -0.1233 -0.1343 -0.1105 99  THR A O   
736  C CB  . THR A 99  ? 0.6712 1.0293 1.0030 -0.1593 -0.1093 -0.0973 99  THR A CB  
737  O OG1 . THR A 99  ? 0.6171 0.9456 0.9552 -0.1624 -0.0899 -0.0808 99  THR A OG1 
738  C CG2 . THR A 99  ? 0.6940 1.0499 1.0479 -0.1789 -0.1236 -0.1202 99  THR A CG2 
739  N N   . MET A 100 ? 0.8326 1.1926 1.0998 -0.1401 -0.1431 -0.1443 100 MET A N   
740  C CA  . MET A 100 ? 0.8857 1.2714 1.1344 -0.1317 -0.1624 -0.1634 100 MET A CA  
741  C C   . MET A 100 ? 0.9389 1.3345 1.2132 -0.1523 -0.1811 -0.1880 100 MET A C   
742  O O   . MET A 100 ? 0.9750 1.3357 1.2498 -0.1646 -0.1839 -0.2070 100 MET A O   
743  C CB  . MET A 100 ? 0.8942 1.2523 1.1007 -0.1158 -0.1612 -0.1728 100 MET A CB  
744  C CG  . MET A 100 ? 0.8441 1.2038 1.0273 -0.0937 -0.1468 -0.1501 100 MET A CG  
745  S SD  . MET A 100 ? 0.9361 1.3533 1.1202 -0.0778 -0.1518 -0.1356 100 MET A SD  
746  C CE  . MET A 100 ? 0.8699 1.2751 1.0383 -0.0588 -0.1298 -0.1074 100 MET A CE  
747  N N   . ARG A 101 ? 0.9904 1.4341 1.2879 -0.1562 -0.1936 -0.1876 101 ARG A N   
748  C CA  . ARG A 101 ? 1.0024 1.4649 1.3254 -0.1748 -0.2153 -0.2128 101 ARG A CA  
749  C C   . ARG A 101 ? 1.0695 1.5560 1.3622 -0.1626 -0.2379 -0.2367 101 ARG A C   
750  O O   . ARG A 101 ? 1.1277 1.6154 1.4299 -0.1770 -0.2575 -0.2660 101 ARG A O   
751  C CB  . ARG A 101 ? 1.0097 1.5153 1.3789 -0.1865 -0.2180 -0.1997 101 ARG A CB  
752  C CG  . ARG A 101 ? 1.0228 1.5073 1.4226 -0.1981 -0.1956 -0.1765 101 ARG A CG  
753  C CD  . ARG A 101 ? 1.0364 1.5665 1.4787 -0.2054 -0.1963 -0.1607 101 ARG A CD  
754  N NE  . ARG A 101 ? 1.0306 1.6049 1.4576 -0.1842 -0.1999 -0.1475 101 ARG A NE  
755  C CZ  . ARG A 101 ? 1.1160 1.6875 1.5244 -0.1656 -0.1816 -0.1223 101 ARG A CZ  
756  N NH1 . ARG A 101 ? 0.9729 1.5021 1.3732 -0.1649 -0.1602 -0.1084 101 ARG A NH1 
757  N NH2 . ARG A 101 ? 0.9852 1.5974 1.3832 -0.1468 -0.1849 -0.1109 101 ARG A NH2 
758  N N   . GLY A 102 ? 1.0438 1.5490 1.3008 -0.1360 -0.2352 -0.2250 102 GLY A N   
759  C CA  . GLY A 102 ? 1.0466 1.5728 1.2678 -0.1194 -0.2536 -0.2447 102 GLY A CA  
760  C C   . GLY A 102 ? 1.0598 1.5574 1.2328 -0.0959 -0.2415 -0.2401 102 GLY A C   
761  O O   . GLY A 102 ? 1.0773 1.5257 1.2422 -0.1001 -0.2282 -0.2410 102 GLY A O   
762  N N   . GLU A 103 ? 1.0193 1.5485 1.1615 -0.0700 -0.2449 -0.2336 103 GLU A N   
763  C CA  A GLU A 103 ? 1.0474 1.5546 1.1467 -0.0459 -0.2323 -0.2265 103 GLU A CA  
764  C CA  B GLU A 103 ? 1.0474 1.5547 1.1466 -0.0458 -0.2323 -0.2265 103 GLU A CA  
765  C C   . GLU A 103 ? 1.0511 1.5501 1.1565 -0.0369 -0.2071 -0.1914 103 GLU A C   
766  O O   . GLU A 103 ? 1.0221 1.5383 1.1589 -0.0449 -0.2004 -0.1724 103 GLU A O   
767  C CB  A GLU A 103 ? 1.0439 1.5882 1.1070 -0.0203 -0.2454 -0.2338 103 GLU A CB  
768  C CB  B GLU A 103 ? 1.0439 1.5884 1.1070 -0.0202 -0.2453 -0.2336 103 GLU A CB  
769  C CG  A GLU A 103 ? 1.0543 1.6135 1.1102 -0.0281 -0.2736 -0.2707 103 GLU A CG  
770  C CG  B GLU A 103 ? 1.0212 1.6172 1.0918 -0.0044 -0.2427 -0.2079 103 GLU A CG  
771  C CD  A GLU A 103 ? 1.0157 1.6146 1.0318 0.0003  -0.2867 -0.2770 103 GLU A CD  
772  C CD  B GLU A 103 ? 1.0315 1.6661 1.0651 0.0227  -0.2556 -0.2143 103 GLU A CD  
773  O OE1 A GLU A 103 ? 1.0385 1.6258 1.0158 0.0259  -0.2739 -0.2670 103 GLU A OE1 
774  O OE1 B GLU A 103 ? 1.0084 1.6531 1.0277 0.0197  -0.2788 -0.2456 103 GLU A OE1 
775  O OE2 A GLU A 103 ? 0.9758 1.6195 1.0000 -0.0021 -0.3093 -0.2908 103 GLU A OE2 
776  O OE2 B GLU A 103 ? 1.0393 1.6937 1.0580 0.0476  -0.2421 -0.1881 103 GLU A OE2 
777  N N   . VAL A 104 ? 1.0344 1.5067 1.1099 -0.0200 -0.1931 -0.1834 104 VAL A N   
778  C CA  . VAL A 104 ? 0.9987 1.4602 1.0788 -0.0116 -0.1704 -0.1531 104 VAL A CA  
779  C C   . VAL A 104 ? 0.9861 1.4891 1.0580 0.0112  -0.1664 -0.1324 104 VAL A C   
780  O O   . VAL A 104 ? 1.0601 1.5780 1.1006 0.0328  -0.1706 -0.1362 104 VAL A O   
781  C CB  . VAL A 104 ? 1.0198 1.4376 1.0763 -0.0039 -0.1572 -0.1525 104 VAL A CB  
782  C CG1 . VAL A 104 ? 0.9671 1.3727 1.0348 -0.0002 -0.1360 -0.1240 104 VAL A CG1 
783  C CG2 . VAL A 104 ? 1.0687 1.4460 1.1291 -0.0233 -0.1619 -0.1749 104 VAL A CG2 
784  N N   . PRO A 105 ? 0.9284 1.4500 1.0269 0.0089  -0.1572 -0.1097 105 PRO A N   
785  C CA  . PRO A 105 ? 0.8934 1.4524 0.9869 0.0311  -0.1511 -0.0880 105 PRO A CA  
786  C C   . PRO A 105 ? 0.8647 1.4052 0.9438 0.0486  -0.1305 -0.0673 105 PRO A C   
787  O O   . PRO A 105 ? 0.8934 1.3956 0.9750 0.0409  -0.1191 -0.0644 105 PRO A O   
788  C CB  . PRO A 105 ? 0.8639 1.4435 0.9946 0.0194  -0.1478 -0.0731 105 PRO A CB  
789  C CG  . PRO A 105 ? 0.8682 1.4082 1.0188 -0.0037 -0.1409 -0.0763 105 PRO A CG  
790  C CD  . PRO A 105 ? 0.9208 1.4318 1.0558 -0.0137 -0.1519 -0.1033 105 PRO A CD  
791  N N   . ASP A 106 ? 0.8177 1.3881 0.8829 0.0731  -0.1257 -0.0518 106 ASP A N   
792  C CA  A ASP A 106 ? 0.7918 1.3500 0.8484 0.0906  -0.1055 -0.0299 106 ASP A CA  
793  C CA  B ASP A 106 ? 0.7917 1.3503 0.8482 0.0908  -0.1055 -0.0298 106 ASP A CA  
794  C C   . ASP A 106 ? 0.7848 1.3381 0.8722 0.0842  -0.0891 -0.0066 106 ASP A C   
795  O O   . ASP A 106 ? 0.7583 1.3368 0.8664 0.0803  -0.0908 0.0014  106 ASP A O   
796  C CB  A ASP A 106 ? 0.7852 1.3771 0.8183 0.1203  -0.1038 -0.0192 106 ASP A CB  
797  C CB  B ASP A 106 ? 0.7847 1.3779 0.8179 0.1204  -0.1042 -0.0192 106 ASP A CB  
798  C CG  A ASP A 106 ? 0.7932 1.3869 0.7894 0.1307  -0.1182 -0.0422 106 ASP A CG  
799  C CG  B ASP A 106 ? 0.7744 1.3548 0.7992 0.1394  -0.0829 0.0027  106 ASP A CG  
800  O OD1 A ASP A 106 ? 0.8126 1.3836 0.8047 0.1130  -0.1314 -0.0684 106 ASP A OD1 
801  O OD1 B ASP A 106 ? 0.7477 1.3259 0.7961 0.1397  -0.0664 0.0259  106 ASP A OD1 
802  O OD2 A ASP A 106 ? 0.7904 1.4073 0.7614 0.1576  -0.1152 -0.0339 106 ASP A OD2 
803  O OD2 B ASP A 106 ? 0.7889 1.3610 0.7846 0.1540  -0.0824 -0.0037 106 ASP A OD2 
804  N N   . PRO A 107 ? 0.8140 1.3356 0.9051 0.0832  -0.0734 0.0039  107 PRO A N   
805  C CA  . PRO A 107 ? 0.8477 1.3397 0.9188 0.0881  -0.0691 -0.0020 107 PRO A CA  
806  C C   . PRO A 107 ? 0.8991 1.3523 0.9749 0.0666  -0.0721 -0.0172 107 PRO A C   
807  O O   . PRO A 107 ? 0.9226 1.3485 0.9944 0.0680  -0.0625 -0.0132 107 PRO A O   
808  C CB  . PRO A 107 ? 0.8086 1.2977 0.8886 0.1013  -0.0489 0.0237  107 PRO A CB  
809  C CG  . PRO A 107 ? 0.7732 1.2641 0.8837 0.0888  -0.0428 0.0354  107 PRO A CG  
810  C CD  . PRO A 107 ? 0.7614 1.2801 0.8773 0.0824  -0.0568 0.0267  107 PRO A CD  
811  N N   . MET A 108 ? 0.8467 1.2972 0.9327 0.0473  -0.0845 -0.0333 108 MET A N   
812  C CA  A MET A 108 ? 0.8683 1.2810 0.9591 0.0287  -0.0850 -0.0452 108 MET A CA  
813  C CA  B MET A 108 ? 0.8681 1.2812 0.9589 0.0284  -0.0856 -0.0459 108 MET A CA  
814  C C   . MET A 108 ? 0.8967 1.2864 0.9610 0.0328  -0.0901 -0.0629 108 MET A C   
815  O O   . MET A 108 ? 0.9347 1.2902 1.0002 0.0213  -0.0876 -0.0700 108 MET A O   
816  C CB  A MET A 108 ? 0.8909 1.3072 1.0032 0.0073  -0.0948 -0.0558 108 MET A CB  
817  C CB  B MET A 108 ? 0.8936 1.3114 1.0046 0.0073  -0.0965 -0.0578 108 MET A CB  
818  C CG  A MET A 108 ? 0.8569 1.2389 0.9845 -0.0106 -0.0878 -0.0553 108 MET A CG  
819  C CG  B MET A 108 ? 0.8719 1.3129 1.0097 0.0029  -0.0917 -0.0415 108 MET A CG  
820  S SD  A MET A 108 ? 0.9389 1.3342 1.1009 -0.0296 -0.0891 -0.0511 108 MET A SD  
821  S SD  B MET A 108 ? 0.9455 1.3746 1.1128 -0.0241 -0.0949 -0.0482 108 MET A SD  
822  C CE  A MET A 108 ? 0.8027 1.2341 0.9733 -0.0141 -0.0810 -0.0280 108 MET A CE  
823  C CE  B MET A 108 ? 0.8424 1.2208 1.0041 -0.0311 -0.0827 -0.0471 108 MET A CE  
824  N N   . ASN A 109 ? 0.8931 1.3003 0.9322 0.0507  -0.0959 -0.0691 109 ASN A N   
825  C CA  . ASN A 109 ? 0.8887 1.2732 0.8994 0.0582  -0.0986 -0.0849 109 ASN A CA  
826  C C   . ASN A 109 ? 0.9089 1.2711 0.9131 0.0695  -0.0819 -0.0699 109 ASN A C   
827  O O   . ASN A 109 ? 0.9291 1.2665 0.9134 0.0742  -0.0813 -0.0809 109 ASN A O   
828  C CB  . ASN A 109 ? 0.9208 1.3327 0.9034 0.0769  -0.1093 -0.0955 109 ASN A CB  
829  C CG  . ASN A 109 ? 0.8897 1.3407 0.8733 0.0962  -0.1028 -0.0731 109 ASN A CG  
830  O OD1 . ASN A 109 ? 0.8752 1.3253 0.8573 0.1115  -0.0864 -0.0518 109 ASN A OD1 
831  N ND2 . ASN A 109 ? 0.8649 1.3515 0.8534 0.0958  -0.1154 -0.0771 109 ASN A ND2 
832  N N   . LEU A 110 ? 0.9200 1.2907 0.9420 0.0739  -0.0685 -0.0457 110 LEU A N   
833  C CA  . LEU A 110 ? 0.8923 1.2437 0.9149 0.0816  -0.0539 -0.0317 110 LEU A CA  
834  C C   . LEU A 110 ? 0.8637 1.1786 0.8936 0.0648  -0.0529 -0.0390 110 LEU A C   
835  O O   . LEU A 110 ? 0.8940 1.1885 0.9153 0.0714  -0.0458 -0.0367 110 LEU A O   
836  C CB  . LEU A 110 ? 0.8326 1.2002 0.8772 0.0868  -0.0411 -0.0064 110 LEU A CB  
837  C CG  . LEU A 110 ? 0.8319 1.2353 0.8736 0.1058  -0.0372 0.0077  110 LEU A CG  
838  C CD1 . LEU A 110 ? 0.8216 1.2319 0.8899 0.1081  -0.0223 0.0322  110 LEU A CD1 
839  C CD2 . LEU A 110 ? 0.8519 1.2624 0.8650 0.1292  -0.0346 0.0074  110 LEU A CD2 
840  N N   . LEU A 111 ? 0.8754 1.1833 0.9217 0.0444  -0.0591 -0.0462 111 LEU A N   
841  C CA  . LEU A 111 ? 0.8887 1.1631 0.9420 0.0296  -0.0571 -0.0512 111 LEU A CA  
842  C C   . LEU A 111 ? 0.9327 1.1826 0.9666 0.0280  -0.0634 -0.0716 111 LEU A C   
843  O O   . LEU A 111 ? 0.9211 1.1430 0.9492 0.0289  -0.0572 -0.0715 111 LEU A O   
844  C CB  . LEU A 111 ? 0.8257 1.1012 0.9025 0.0102  -0.0598 -0.0509 111 LEU A CB  
845  C CG  . LEU A 111 ? 0.7295 1.0113 0.8266 0.0076  -0.0503 -0.0318 111 LEU A CG  
846  C CD1 . LEU A 111 ? 0.6886 0.9942 0.7862 0.0241  -0.0437 -0.0163 111 LEU A CD1 
847  C CD2 . LEU A 111 ? 0.6931 0.9854 0.8100 -0.0073 -0.0539 -0.0324 111 LEU A CD2 
848  N N   . GLY A 112 ? 0.9614 1.2214 0.9857 0.0258  -0.0760 -0.0897 112 GLY A N   
849  C CA  . GLY A 112 ? 1.0428 1.2776 1.0490 0.0235  -0.0827 -0.1121 112 GLY A CA  
850  C C   . GLY A 112 ? 1.1092 1.3583 1.1151 0.0142  -0.0994 -0.1334 112 GLY A C   
851  O O   . GLY A 112 ? 1.0858 1.3655 1.1076 0.0086  -0.1057 -0.1295 112 GLY A O   
852  N N   . GLU A 113 ? 1.1756 1.4021 1.1636 0.0129  -0.1067 -0.1567 113 GLU A N   
853  C CA  A GLU A 113 ? 1.2178 1.4538 1.2062 0.0020  -0.1247 -0.1818 113 GLU A CA  
854  C CA  B GLU A 113 ? 1.2181 1.4542 1.2064 0.0020  -0.1247 -0.1818 113 GLU A CA  
855  C C   . GLU A 113 ? 1.2065 1.4385 1.2311 -0.0248 -0.1283 -0.1837 113 GLU A C   
856  O O   . GLU A 113 ? 1.1731 1.3868 1.2164 -0.0338 -0.1162 -0.1686 113 GLU A O   
857  C CB  A GLU A 113 ? 1.2721 1.4773 1.2339 0.0058  -0.1301 -0.2077 113 GLU A CB  
858  C CB  B GLU A 113 ? 1.2722 1.4781 1.2332 0.0064  -0.1301 -0.2077 113 GLU A CB  
859  C CG  A GLU A 113 ? 1.2746 1.4772 1.2000 0.0337  -0.1224 -0.2036 113 GLU A CG  
860  C CG  B GLU A 113 ? 1.2867 1.5009 1.2434 -0.0031 -0.1512 -0.2390 113 GLU A CG  
861  C CD  A GLU A 113 ? 1.3000 1.4562 1.2081 0.0369  -0.1150 -0.2148 113 GLU A CD  
862  C CD  B GLU A 113 ? 1.2714 1.5318 1.2100 0.0129  -0.1637 -0.2424 113 GLU A CD  
863  O OE1 A GLU A 113 ? 1.3260 1.4511 1.2500 0.0173  -0.1161 -0.2263 113 GLU A OE1 
864  O OE1 B GLU A 113 ? 1.2450 1.5283 1.1723 0.0334  -0.1541 -0.2198 113 GLU A OE1 
865  O OE2 A GLU A 113 ? 1.2925 1.4434 1.1722 0.0600  -0.1068 -0.2105 113 GLU A OE2 
866  O OE2 B GLU A 113 ? 1.2864 1.5611 1.2232 0.0052  -0.1834 -0.2677 113 GLU A OE2 
867  N N   . GLN A 114 ? 1.2705 1.5226 1.3056 -0.0367 -0.1455 -0.2021 114 GLN A N   
868  C CA  . GLN A 114 ? 1.2476 1.4987 1.3204 -0.0625 -0.1494 -0.2051 114 GLN A CA  
869  C C   . GLN A 114 ? 1.2127 1.4167 1.2967 -0.0758 -0.1380 -0.2051 114 GLN A C   
870  O O   . GLN A 114 ? 1.1606 1.3588 1.2702 -0.0869 -0.1276 -0.1882 114 GLN A O   
871  C CB  . GLN A 114 ? 1.2776 1.5466 1.3582 -0.0748 -0.1713 -0.2326 114 GLN A CB  
872  C CG  . GLN A 114 ? 1.2652 1.5424 1.3914 -0.1016 -0.1759 -0.2334 114 GLN A CG  
873  C CD  . GLN A 114 ? 1.3830 1.6190 1.5269 -0.1233 -0.1765 -0.2518 114 GLN A CD  
874  O OE1 . GLN A 114 ? 1.5179 1.7109 1.6538 -0.1222 -0.1616 -0.2467 114 GLN A OE1 
875  N NE2 . GLN A 114 ? 1.3384 1.5879 1.5083 -0.1428 -0.1934 -0.2725 114 GLN A NE2 
876  N N   . GLN A 115 ? 1.2920 1.4614 1.3542 -0.0719 -0.1382 -0.2227 115 GLN A N   
877  C CA  . GLN A 115 ? 1.2976 1.4208 1.3711 -0.0852 -0.1292 -0.2273 115 GLN A CA  
878  C C   . GLN A 115 ? 1.2623 1.3703 1.3457 -0.0837 -0.1098 -0.1993 115 GLN A C   
879  O O   . GLN A 115 ? 1.2717 1.3480 1.3717 -0.0964 -0.1010 -0.1972 115 GLN A O   
880  C CB  . GLN A 115 ? 1.3422 1.4317 1.3837 -0.0742 -0.1297 -0.2470 115 GLN A CB  
881  C CG  . GLN A 115 ? 1.3970 1.5046 1.4185 -0.0695 -0.1493 -0.2748 115 GLN A CG  
882  C CD  . GLN A 115 ? 1.5076 1.5886 1.4882 -0.0503 -0.1476 -0.2899 115 GLN A CD  
883  O OE1 . GLN A 115 ? 1.5352 1.5757 1.5083 -0.0463 -0.1331 -0.2855 115 GLN A OE1 
884  N NE2 . GLN A 115 ? 1.4568 1.5615 1.4094 -0.0365 -0.1618 -0.3070 115 GLN A NE2 
885  N N   . HIS A 116 ? 1.1690 1.2996 1.2437 -0.0685 -0.1031 -0.1777 116 HIS A N   
886  C CA  . HIS A 116 ? 1.1144 1.2330 1.1940 -0.0645 -0.0868 -0.1534 116 HIS A CA  
887  C C   . HIS A 116 ? 0.9877 1.1290 1.0946 -0.0744 -0.0837 -0.1361 116 HIS A C   
888  O O   . HIS A 116 ? 0.9358 1.0674 1.0481 -0.0729 -0.0713 -0.1176 116 HIS A O   
889  C CB  . HIS A 116 ? 1.1425 1.2675 1.1964 -0.0412 -0.0805 -0.1419 116 HIS A CB  
890  C CG  . HIS A 116 ? 1.2179 1.3215 1.2430 -0.0282 -0.0814 -0.1566 116 HIS A CG  
891  N ND1 . HIS A 116 ? 1.2691 1.3705 1.2820 -0.0302 -0.0942 -0.1824 116 HIS A ND1 
892  C CD2 . HIS A 116 ? 1.2413 1.3249 1.2471 -0.0124 -0.0710 -0.1496 116 HIS A CD2 
893  C CE1 . HIS A 116 ? 1.2954 1.3741 1.2806 -0.0153 -0.0906 -0.1909 116 HIS A CE1 
894  N NE2 . HIS A 116 ? 1.2393 1.3076 1.2207 -0.0041 -0.0760 -0.1702 116 HIS A NE2 
895  N N   . PHE A 117 ? 0.9989 1.1707 1.1225 -0.0837 -0.0947 -0.1420 117 PHE A N   
896  C CA  . PHE A 117 ? 0.9171 1.1108 1.0676 -0.0926 -0.0911 -0.1260 117 PHE A CA  
897  C C   . PHE A 117 ? 0.8062 0.9816 0.9847 -0.1138 -0.0889 -0.1300 117 PHE A C   
898  O O   . PHE A 117 ? 0.8166 1.0070 1.0167 -0.1282 -0.0995 -0.1420 117 PHE A O   
899  C CB  . PHE A 117 ? 0.8504 1.0892 1.0064 -0.0896 -0.1025 -0.1272 117 PHE A CB  
900  C CG  . PHE A 117 ? 0.8307 1.0899 0.9654 -0.0682 -0.1000 -0.1158 117 PHE A CG  
901  C CD1 . PHE A 117 ? 0.8247 1.0940 0.9659 -0.0618 -0.0886 -0.0932 117 PHE A CD1 
902  C CD2 . PHE A 117 ? 0.9264 1.1939 1.0350 -0.0540 -0.1083 -0.1278 117 PHE A CD2 
903  C CE1 . PHE A 117 ? 0.8346 1.1212 0.9609 -0.0431 -0.0849 -0.0819 117 PHE A CE1 
904  C CE2 . PHE A 117 ? 0.9476 1.2341 1.0391 -0.0336 -0.1037 -0.1148 117 PHE A CE2 
905  C CZ  . PHE A 117 ? 0.8774 1.1732 0.9800 -0.0289 -0.0918 -0.0915 117 PHE A CZ  
906  N N   . ILE A 118 ? 0.8093 0.9533 0.9891 -0.1151 -0.0746 -0.1186 118 ILE A N   
907  C CA  . ILE A 118 ? 0.7948 0.9168 1.0000 -0.1326 -0.0683 -0.1185 118 ILE A CA  
908  C C   . ILE A 118 ? 0.7055 0.8240 0.9196 -0.1314 -0.0529 -0.0943 118 ILE A C   
909  O O   . ILE A 118 ? 0.7132 0.8014 0.9319 -0.1352 -0.0410 -0.0875 118 ILE A O   
910  C CB  . ILE A 118 ? 0.8081 0.8874 1.0037 -0.1348 -0.0652 -0.1314 118 ILE A CB  
911  C CG1 . ILE A 118 ? 0.7951 0.8569 0.9577 -0.1149 -0.0580 -0.1248 118 ILE A CG1 
912  C CG2 . ILE A 118 ? 0.8493 0.9293 1.0466 -0.1434 -0.0812 -0.1593 118 ILE A CG2 
913  C CD1 . ILE A 118 ? 0.7881 0.8050 0.9442 -0.1145 -0.0476 -0.1265 118 ILE A CD1 
914  N N   . TYR A 119 ? 0.6940 0.8427 0.9097 -0.1250 -0.0523 -0.0811 119 TYR A N   
915  C CA  . TYR A 119 ? 0.6702 0.8172 0.8895 -0.1214 -0.0387 -0.0600 119 TYR A CA  
916  C C   . TYR A 119 ? 0.6180 0.7979 0.8604 -0.1273 -0.0396 -0.0519 119 TYR A C   
917  O O   . TYR A 119 ? 0.5996 0.8029 0.8359 -0.1174 -0.0400 -0.0436 119 TYR A O   
918  C CB  . TYR A 119 ? 0.6361 0.7808 0.8291 -0.1036 -0.0347 -0.0510 119 TYR A CB  
919  C CG  . TYR A 119 ? 0.6986 0.8188 0.8690 -0.0954 -0.0359 -0.0597 119 TYR A CG  
920  C CD1 . TYR A 119 ? 0.6875 0.7731 0.8547 -0.0975 -0.0277 -0.0590 119 TYR A CD1 
921  C CD2 . TYR A 119 ? 0.7280 0.8600 0.8803 -0.0839 -0.0436 -0.0671 119 TYR A CD2 
922  C CE1 . TYR A 119 ? 0.7258 0.7888 0.8728 -0.0886 -0.0276 -0.0661 119 TYR A CE1 
923  C CE2 . TYR A 119 ? 0.7289 0.8389 0.8606 -0.0748 -0.0433 -0.0741 119 TYR A CE2 
924  C CZ  . TYR A 119 ? 0.7421 0.8175 0.8714 -0.0774 -0.0354 -0.0739 119 TYR A CZ  
925  O OH  . TYR A 119 ? 0.8231 0.8764 0.9322 -0.0671 -0.0339 -0.0799 119 TYR A OH  
926  N N   . PRO A 120 ? 0.5965 0.7789 0.8681 -0.1432 -0.0387 -0.0531 120 PRO A N   
927  C CA  . PRO A 120 ? 0.5830 0.7996 0.8796 -0.1485 -0.0395 -0.0449 120 PRO A CA  
928  C C   . PRO A 120 ? 0.5589 0.7768 0.8559 -0.1417 -0.0243 -0.0235 120 PRO A C   
929  O O   . PRO A 120 ? 0.5551 0.8018 0.8677 -0.1417 -0.0235 -0.0150 120 PRO A O   
930  C CB  . PRO A 120 ? 0.5385 0.7540 0.8691 -0.1685 -0.0423 -0.0530 120 PRO A CB  
931  C CG  . PRO A 120 ? 0.5609 0.7330 0.8853 -0.1721 -0.0336 -0.0554 120 PRO A CG  
932  C CD  . PRO A 120 ? 0.5921 0.7466 0.8783 -0.1571 -0.0365 -0.0618 120 PRO A CD  
933  N N   . THR A 121 ? 0.6315 0.8199 0.9111 -0.1348 -0.0126 -0.0148 121 THR A N   
934  C CA  . THR A 121 ? 0.6171 0.8052 0.8909 -0.1261 0.0004  0.0029  121 THR A CA  
935  C C   . THR A 121 ? 0.6234 0.7943 0.8654 -0.1116 0.0024  0.0049  121 THR A C   
936  O O   . THR A 121 ? 0.6930 0.8470 0.9197 -0.1089 -0.0026 -0.0042 121 THR A O   
937  C CB  . THR A 121 ? 0.6094 0.7810 0.8983 -0.1327 0.0150  0.0146  121 THR A CB  
938  O OG1 . THR A 121 ? 0.6538 0.7916 0.9330 -0.1338 0.0190  0.0115  121 THR A OG1 
939  C CG2 . THR A 121 ? 0.5069 0.6977 0.8336 -0.1482 0.0139  0.0143  121 THR A CG2 
940  N N   . VAL A 122 ? 0.6350 0.8108 0.8681 -0.1021 0.0097  0.0166  122 VAL A N   
941  C CA  . VAL A 122 ? 0.6788 0.8395 0.8858 -0.0895 0.0115  0.0191  122 VAL A CA  
942  C C   . VAL A 122 ? 0.6856 0.8160 0.8821 -0.0887 0.0183  0.0217  122 VAL A C   
943  O O   . VAL A 122 ? 0.6906 0.8066 0.8682 -0.0810 0.0159  0.0189  122 VAL A O   
944  C CB  . VAL A 122 ? 0.6192 0.7898 0.8212 -0.0811 0.0177  0.0291  122 VAL A CB  
945  C CG1 . VAL A 122 ? 0.6156 0.7696 0.7938 -0.0701 0.0193  0.0311  122 VAL A CG1 
946  C CG2 . VAL A 122 ? 0.5905 0.7886 0.8005 -0.0789 0.0118  0.0274  122 VAL A CG2 
947  N N   A GLU A 123 ? 0.6623 0.7836 0.8724 -0.0957 0.0280  0.0288  123 GLU A N   
948  N N   B GLU A 123 ? 0.6666 0.7879 0.8765 -0.0956 0.0281  0.0289  123 GLU A N   
949  C CA  A GLU A 123 ? 0.7331 0.8255 0.9346 -0.0937 0.0369  0.0341  123 GLU A CA  
950  C CA  B GLU A 123 ? 0.7303 0.8226 0.9316 -0.0936 0.0368  0.0341  123 GLU A CA  
951  C C   A GLU A 123 ? 0.7083 0.7835 0.9089 -0.0982 0.0308  0.0224  123 GLU A C   
952  C C   B GLU A 123 ? 0.6948 0.7701 0.8951 -0.0981 0.0307  0.0223  123 GLU A C   
953  O O   A GLU A 123 ? 0.7140 0.7667 0.8972 -0.0904 0.0341  0.0242  123 GLU A O   
954  O O   B GLU A 123 ? 0.7018 0.7549 0.8846 -0.0902 0.0338  0.0239  123 GLU A O   
955  C CB  A GLU A 123 ? 0.7686 0.8567 0.9894 -0.1003 0.0504  0.0459  123 GLU A CB  
956  C CB  B GLU A 123 ? 0.7853 0.8726 1.0054 -0.1001 0.0505  0.0460  123 GLU A CB  
957  C CG  A GLU A 123 ? 0.7812 0.8409 0.9915 -0.0945 0.0634  0.0567  123 GLU A CG  
958  C CG  B GLU A 123 ? 0.7671 0.8562 0.9753 -0.0892 0.0618  0.0608  123 GLU A CG  
959  C CD  A GLU A 123 ? 0.8248 0.8815 1.0067 -0.0777 0.0687  0.0667  123 GLU A CD  
960  C CD  B GLU A 123 ? 0.7937 0.8773 1.0201 -0.0936 0.0778  0.0749  123 GLU A CD  
961  O OE1 A GLU A 123 ? 0.7790 0.8537 0.9527 -0.0725 0.0636  0.0650  123 GLU A OE1 
962  O OE1 B GLU A 123 ? 0.7964 0.8807 1.0522 -0.1081 0.0787  0.0727  123 GLU A OE1 
963  O OE2 A GLU A 123 ? 0.8254 0.8614 0.9933 -0.0694 0.0780  0.0759  123 GLU A OE2 
964  O OE2 B GLU A 123 ? 0.8201 0.8990 1.0321 -0.0824 0.0896  0.0880  123 GLU A OE2 
965  N N   . ALA A 124 ? 0.6765 0.7623 0.8946 -0.1096 0.0217  0.0098  124 ALA A N   
966  C CA  . ALA A 124 ? 0.6968 0.7650 0.9122 -0.1136 0.0154  -0.0042 124 ALA A CA  
967  C C   . ALA A 124 ? 0.7042 0.7723 0.8935 -0.1008 0.0074  -0.0107 124 ALA A C   
968  O O   . ALA A 124 ? 0.7234 0.7685 0.8999 -0.0965 0.0079  -0.0158 124 ALA A O   
969  C CB  . ALA A 124 ? 0.7002 0.7826 0.9399 -0.1288 0.0056  -0.0182 124 ALA A CB  
970  N N   . TYR A 125 ? 0.6698 0.7631 0.8527 -0.0940 0.0015  -0.0094 125 TYR A N   
971  C CA  . TYR A 125 ? 0.6732 0.7686 0.8353 -0.0815 -0.0041 -0.0127 125 TYR A CA  
972  C C   . TYR A 125 ? 0.6674 0.7465 0.8128 -0.0704 0.0031  -0.0023 125 TYR A C   
973  O O   . TYR A 125 ? 0.6908 0.7601 0.8211 -0.0614 0.0011  -0.0048 125 TYR A O   
974  C CB  . TYR A 125 ? 0.6319 0.7582 0.7960 -0.0775 -0.0102 -0.0120 125 TYR A CB  
975  C CG  . TYR A 125 ? 0.6261 0.7573 0.7736 -0.0646 -0.0143 -0.0130 125 TYR A CG  
976  C CD1 . TYR A 125 ? 0.6427 0.7734 0.7815 -0.0609 -0.0212 -0.0238 125 TYR A CD1 
977  C CD2 . TYR A 125 ? 0.6346 0.7714 0.7763 -0.0559 -0.0110 -0.0033 125 TYR A CD2 
978  C CE1 . TYR A 125 ? 0.6521 0.7887 0.7781 -0.0482 -0.0230 -0.0224 125 TYR A CE1 
979  C CE2 . TYR A 125 ? 0.6160 0.7587 0.7482 -0.0452 -0.0140 -0.0029 125 TYR A CE2 
980  C CZ  . TYR A 125 ? 0.6414 0.7845 0.7663 -0.0410 -0.0191 -0.0112 125 TYR A CZ  
981  O OH  . TYR A 125 ? 0.6498 0.7999 0.7673 -0.0293 -0.0201 -0.0086 125 TYR A OH  
982  N N   . ALA A 126 ? 0.6578 0.7354 0.8050 -0.0699 0.0113  0.0095  126 ALA A N   
983  C CA  . ALA A 126 ? 0.6701 0.7357 0.8002 -0.0586 0.0165  0.0186  126 ALA A CA  
984  C C   . ALA A 126 ? 0.7435 0.7814 0.8657 -0.0558 0.0218  0.0198  126 ALA A C   
985  O O   . ALA A 126 ? 0.7481 0.7783 0.8546 -0.0448 0.0208  0.0217  126 ALA A O   
986  C CB  . ALA A 126 ? 0.6796 0.7490 0.8109 -0.0577 0.0245  0.0298  126 ALA A CB  
987  N N   . HIS A 127 ? 0.7622 0.7851 0.8977 -0.0656 0.0282  0.0194  127 HIS A N   
988  C CA  . HIS A 127 ? 0.8248 0.8182 0.9554 -0.0630 0.0356  0.0215  127 HIS A CA  
989  C C   . HIS A 127 ? 0.8396 0.8237 0.9630 -0.0608 0.0284  0.0086  127 HIS A C   
990  O O   . HIS A 127 ? 0.8569 0.8195 0.9682 -0.0519 0.0333  0.0115  127 HIS A O   
991  C CB  . HIS A 127 ? 0.8780 0.8570 1.0298 -0.0756 0.0453  0.0245  127 HIS A CB  
992  C CG  . HIS A 127 ? 0.8761 0.8631 1.0345 -0.0758 0.0550  0.0392  127 HIS A CG  
993  N ND1 . HIS A 127 ? 0.8761 0.8670 1.0147 -0.0619 0.0592  0.0514  127 HIS A ND1 
994  C CD2 . HIS A 127 ? 0.9099 0.9026 1.0922 -0.0874 0.0615  0.0436  127 HIS A CD2 
995  C CE1 . HIS A 127 ? 0.8589 0.8557 1.0056 -0.0637 0.0686  0.0624  127 HIS A CE1 
996  N NE2 . HIS A 127 ? 0.9316 0.9300 1.1061 -0.0790 0.0710  0.0592  127 HIS A NE2 
997  N N   . ALA A 128 ? 0.7318 0.7324 0.8611 -0.0669 0.0176  -0.0050 128 ALA A N   
998  C CA  . ALA A 128 ? 0.7205 0.7142 0.8391 -0.0622 0.0111  -0.0176 128 ALA A CA  
999  C C   . ALA A 128 ? 0.7355 0.7365 0.8354 -0.0460 0.0090  -0.0120 128 ALA A C   
1000 O O   . ALA A 128 ? 0.7280 0.7146 0.8156 -0.0372 0.0095  -0.0154 128 ALA A O   
1001 C CB  . ALA A 128 ? 0.6855 0.6983 0.8127 -0.0707 -0.0002 -0.0328 128 ALA A CB  
1002 N N   . VAL A 129 ? 0.7494 0.7726 0.8488 -0.0421 0.0070  -0.0036 129 VAL A N   
1003 C CA  . VAL A 129 ? 0.7369 0.7678 0.8239 -0.0284 0.0052  0.0025  129 VAL A CA  
1004 C C   . VAL A 129 ? 0.7346 0.7458 0.8114 -0.0196 0.0125  0.0126  129 VAL A C   
1005 O O   . VAL A 129 ? 0.7426 0.7481 0.8093 -0.0084 0.0124  0.0143  129 VAL A O   
1006 C CB  . VAL A 129 ? 0.6904 0.7470 0.7823 -0.0280 0.0014  0.0076  129 VAL A CB  
1007 C CG1 . VAL A 129 ? 0.6574 0.7212 0.7412 -0.0158 -0.0007 0.0138  129 VAL A CG1 
1008 C CG2 . VAL A 129 ? 0.6609 0.7386 0.7619 -0.0331 -0.0050 -0.0001 129 VAL A CG2 
1009 N N   . GLU A 130 ? 0.7333 0.7355 0.8126 -0.0231 0.0199  0.0209  130 GLU A N   
1010 C CA  . GLU A 130 ? 0.7416 0.7269 0.8097 -0.0129 0.0277  0.0325  130 GLU A CA  
1011 C C   . GLU A 130 ? 0.7874 0.7456 0.8519 -0.0096 0.0336  0.0303  130 GLU A C   
1012 O O   . GLU A 130 ? 0.7925 0.7411 0.8450 0.0037  0.0372  0.0381  130 GLU A O   
1013 C CB  . GLU A 130 ? 0.7955 0.7757 0.8666 -0.0165 0.0365  0.0425  130 GLU A CB  
1014 C CG  . GLU A 130 ? 0.7988 0.8024 0.8705 -0.0176 0.0324  0.0448  130 GLU A CG  
1015 C CD  . GLU A 130 ? 0.9665 0.9660 1.0439 -0.0227 0.0423  0.0531  130 GLU A CD  
1016 O OE1 . GLU A 130 ? 0.8505 0.8299 0.9351 -0.0269 0.0524  0.0575  130 GLU A OE1 
1017 O OE2 . GLU A 130 ? 0.9543 0.9696 1.0299 -0.0220 0.0409  0.0556  130 GLU A OE2 
1018 N N   . ALA A 131 ? 0.8004 0.7460 0.8755 -0.0212 0.0344  0.0191  131 ALA A N   
1019 C CA  . ALA A 131 ? 0.8323 0.7485 0.9044 -0.0189 0.0402  0.0142  131 ALA A CA  
1020 C C   . ALA A 131 ? 0.7932 0.7128 0.8526 -0.0080 0.0340  0.0070  131 ALA A C   
1021 O O   . ALA A 131 ? 0.8412 0.7398 0.8909 0.0028  0.0403  0.0098  131 ALA A O   
1022 C CB  . ALA A 131 ? 0.8672 0.7697 0.9562 -0.0359 0.0410  0.0015  131 ALA A CB  
1023 N N   . ALA A 132 ? 0.8034 0.7494 0.8634 -0.0094 0.0232  -0.0006 132 ALA A N   
1024 C CA  . ALA A 132 ? 0.8215 0.7738 0.8705 0.0024  0.0189  -0.0052 132 ALA A CA  
1025 C C   . ALA A 132 ? 0.8258 0.7859 0.8669 0.0179  0.0207  0.0090  132 ALA A C   
1026 O O   . ALA A 132 ? 0.8527 0.8103 0.8854 0.0303  0.0214  0.0090  132 ALA A O   
1027 C CB  . ALA A 132 ? 0.8371 0.8175 0.8901 -0.0017 0.0087  -0.0138 132 ALA A CB  
1028 N N   . ARG A 133 ? 0.7888 0.7594 0.8326 0.0181  0.0211  0.0206  133 ARG A N   
1029 C CA  . ARG A 133 ? 0.7522 0.7341 0.7903 0.0315  0.0203  0.0329  133 ARG A CA  
1030 C C   . ARG A 133 ? 0.7612 0.7670 0.8019 0.0380  0.0128  0.0310  133 ARG A C   
1031 O O   . ARG A 133 ? 0.7855 0.7884 0.8212 0.0503  0.0147  0.0339  133 ARG A O   
1032 C CB  . ARG A 133 ? 0.7920 0.7499 0.8203 0.0436  0.0296  0.0413  133 ARG A CB  
1033 C CG  . ARG A 133 ? 0.8627 0.7927 0.8911 0.0376  0.0401  0.0441  133 ARG A CG  
1034 C CD  . ARG A 133 ? 0.9509 0.8598 0.9696 0.0523  0.0508  0.0573  133 ARG A CD  
1035 N NE  . ARG A 133 ? 1.0194 0.9135 1.0324 0.0622  0.0541  0.0536  133 ARG A NE  
1036 C CZ  . ARG A 133 ? 1.0713 0.9766 1.0778 0.0786  0.0527  0.0617  133 ARG A CZ  
1037 N NH1 . ARG A 133 ? 1.0740 1.0060 1.0799 0.0860  0.0464  0.0724  133 ARG A NH1 
1038 N NH2 . ARG A 133 ? 0.9843 0.8739 0.9853 0.0881  0.0577  0.0583  133 ARG A NH2 
1039 N N   . PRO A 134 ? 0.7508 0.7802 0.8008 0.0309  0.0056  0.0276  134 PRO A N   
1040 C CA  . PRO A 134 ? 0.7328 0.7847 0.7889 0.0368  0.0005  0.0275  134 PRO A CA  
1041 C C   . PRO A 134 ? 0.7435 0.8114 0.8042 0.0458  -0.0029 0.0378  134 PRO A C   
1042 O O   . PRO A 134 ? 0.7209 0.7860 0.7778 0.0471  -0.0032 0.0438  134 PRO A O   
1043 C CB  . PRO A 134 ? 0.7005 0.7695 0.7667 0.0257  -0.0043 0.0218  134 PRO A CB  
1044 C CG  . PRO A 134 ? 0.6880 0.7516 0.7549 0.0168  -0.0034 0.0236  134 PRO A CG  
1045 C CD  . PRO A 134 ? 0.7129 0.7493 0.7698 0.0182  0.0037  0.0254  134 PRO A CD  
1046 N N   . SER A 135 ? 0.7403 0.8265 0.8097 0.0526  -0.0054 0.0400  135 SER A N   
1047 C CA  . SER A 135 ? 0.7242 0.8300 0.8041 0.0595  -0.0102 0.0486  135 SER A CA  
1048 C C   . SER A 135 ? 0.6758 0.8020 0.7702 0.0506  -0.0175 0.0472  135 SER A C   
1049 O O   . SER A 135 ? 0.6717 0.8142 0.7767 0.0537  -0.0235 0.0519  135 SER A O   
1050 C CB  . SER A 135 ? 0.6746 0.7916 0.7620 0.0712  -0.0081 0.0535  135 SER A CB  
1051 O OG  . SER A 135 ? 0.7231 0.8200 0.7960 0.0817  -0.0008 0.0551  135 SER A OG  
1052 N N   . LEU A 136 ? 0.6573 0.7831 0.7534 0.0399  -0.0173 0.0406  136 LEU A N   
1053 C CA  . LEU A 136 ? 0.6184 0.7605 0.7281 0.0321  -0.0222 0.0391  136 LEU A CA  
1054 C C   . LEU A 136 ? 0.6184 0.7507 0.7208 0.0218  -0.0208 0.0339  136 LEU A C   
1055 O O   . LEU A 136 ? 0.6238 0.7406 0.7161 0.0188  -0.0162 0.0308  136 LEU A O   
1056 C CB  . LEU A 136 ? 0.5962 0.7559 0.7229 0.0324  -0.0215 0.0398  136 LEU A CB  
1057 C CG  . LEU A 136 ? 0.6288 0.7845 0.7491 0.0352  -0.0161 0.0373  136 LEU A CG  
1058 C CD1 . LEU A 136 ? 0.7748 0.9247 0.8893 0.0254  -0.0153 0.0301  136 LEU A CD1 
1059 C CD2 . LEU A 136 ? 0.6489 0.8242 0.7849 0.0419  -0.0139 0.0429  136 LEU A CD2 
1060 N N   . ASN A 137 ? 0.5711 0.7124 0.6804 0.0164  -0.0245 0.0326  137 ASN A N   
1061 C CA  . ASN A 137 ? 0.5865 0.7211 0.6906 0.0081  -0.0221 0.0293  137 ASN A CA  
1062 C C   . ASN A 137 ? 0.5572 0.6976 0.6698 0.0020  -0.0191 0.0262  137 ASN A C   
1063 O O   . ASN A 137 ? 0.5488 0.7022 0.6729 0.0044  -0.0197 0.0270  137 ASN A O   
1064 C CB  . ASN A 137 ? 0.5632 0.7047 0.6700 0.0060  -0.0265 0.0279  137 ASN A CB  
1065 C CG  . ASN A 137 ? 0.5707 0.7099 0.6668 0.0132  -0.0313 0.0302  137 ASN A CG  
1066 O OD1 . ASN A 137 ? 0.6035 0.7291 0.6837 0.0176  -0.0277 0.0339  137 ASN A OD1 
1067 N ND2 . ASN A 137 ? 0.5973 0.7504 0.7033 0.0147  -0.0394 0.0281  137 ASN A ND2 
1068 N N   . VAL A 138 ? 0.5796 0.7121 0.6874 -0.0049 -0.0155 0.0238  138 VAL A N   
1069 C CA  . VAL A 138 ? 0.5424 0.6823 0.6575 -0.0105 -0.0138 0.0207  138 VAL A CA  
1070 C C   . VAL A 138 ? 0.5971 0.7396 0.7162 -0.0176 -0.0113 0.0209  138 VAL A C   
1071 O O   . VAL A 138 ? 0.5735 0.7040 0.6851 -0.0206 -0.0081 0.0219  138 VAL A O   
1072 C CB  . VAL A 138 ? 0.5391 0.6677 0.6471 -0.0122 -0.0123 0.0164  138 VAL A CB  
1073 C CG1 . VAL A 138 ? 0.5983 0.7376 0.7138 -0.0187 -0.0126 0.0120  138 VAL A CG1 
1074 C CG2 . VAL A 138 ? 0.6257 0.7521 0.7287 -0.0032 -0.0135 0.0159  138 VAL A CG2 
1075 N N   . GLY A 139 ? 0.5316 0.6896 0.6628 -0.0189 -0.0111 0.0215  139 GLY A N   
1076 C CA  . GLY A 139 ? 0.5072 0.6698 0.6439 -0.0245 -0.0075 0.0222  139 GLY A CA  
1077 C C   . GLY A 139 ? 0.5331 0.7115 0.6803 -0.0262 -0.0070 0.0221  139 GLY A C   
1078 O O   . GLY A 139 ? 0.5522 0.7410 0.7038 -0.0211 -0.0088 0.0227  139 GLY A O   
1079 N N   . THR A 140 ? 0.5111 0.6932 0.6625 -0.0322 -0.0043 0.0222  140 THR A N   
1080 C CA  . THR A 140 ? 0.5556 0.7551 0.7159 -0.0338 -0.0057 0.0213  140 THR A CA  
1081 C C   . THR A 140 ? 0.5082 0.7222 0.6808 -0.0349 -0.0010 0.0266  140 THR A C   
1082 O O   . THR A 140 ? 0.5180 0.7251 0.6909 -0.0377 0.0039  0.0292  140 THR A O   
1083 C CB  . THR A 140 ? 0.5340 0.7283 0.6921 -0.0409 -0.0084 0.0153  140 THR A CB  
1084 O OG1 . THR A 140 ? 0.5281 0.7428 0.6940 -0.0417 -0.0123 0.0126  140 THR A OG1 
1085 C CG2 . THR A 140 ? 0.5110 0.6960 0.6723 -0.0485 -0.0034 0.0176  140 THR A CG2 
1086 N N   . LEU A 141 ? 0.5105 0.7445 0.6918 -0.0308 -0.0016 0.0292  141 LEU A N   
1087 C CA  . LEU A 141 ? 0.4965 0.7482 0.6906 -0.0310 0.0025  0.0348  141 LEU A CA  
1088 C C   . LEU A 141 ? 0.5019 0.7675 0.7005 -0.0366 -0.0023 0.0312  141 LEU A C   
1089 O O   . LEU A 141 ? 0.5052 0.7662 0.6966 -0.0396 -0.0091 0.0231  141 LEU A O   
1090 C CB  . LEU A 141 ? 0.4910 0.7581 0.6934 -0.0216 0.0057  0.0417  141 LEU A CB  
1091 C CG  . LEU A 141 ? 0.4861 0.7421 0.6910 -0.0173 0.0103  0.0449  141 LEU A CG  
1092 C CD1 . LEU A 141 ? 0.4832 0.7544 0.6984 -0.0079 0.0138  0.0525  141 LEU A CD1 
1093 C CD2 . LEU A 141 ? 0.4829 0.7302 0.6919 -0.0197 0.0169  0.0469  141 LEU A CD2 
1094 N N   . ILE A 142 ? 0.4722 0.7553 0.6841 -0.0378 0.0010  0.0368  142 ILE A N   
1095 C CA  . ILE A 142 ? 0.5228 0.8256 0.7442 -0.0434 -0.0049 0.0336  142 ILE A CA  
1096 C C   . ILE A 142 ? 0.4975 0.8289 0.7238 -0.0341 -0.0076 0.0377  142 ILE A C   
1097 O O   . ILE A 142 ? 0.4772 0.8186 0.7107 -0.0262 0.0001  0.0482  142 ILE A O   
1098 C CB  . ILE A 142 ? 0.5376 0.8443 0.7732 -0.0507 0.0008  0.0386  142 ILE A CB  
1099 C CG1 . ILE A 142 ? 0.5058 0.7842 0.7343 -0.0574 0.0051  0.0366  142 ILE A CG1 
1100 C CG2 . ILE A 142 ? 0.4838 0.8147 0.7345 -0.0577 -0.0069 0.0350  142 ILE A CG2 
1101 C CD1 . ILE A 142 ? 0.5321 0.7950 0.7525 -0.0640 -0.0021 0.0262  142 ILE A CD1 
1102 N N   . GLY A 143 ? 0.5168 0.8606 0.7383 -0.0340 -0.0181 0.0293  143 GLY A N   
1103 C CA  . GLY A 143 ? 0.5931 0.9656 0.8148 -0.0226 -0.0213 0.0332  143 GLY A CA  
1104 C C   . GLY A 143 ? 0.5849 0.9883 0.8235 -0.0241 -0.0237 0.0374  143 GLY A C   
1105 O O   . GLY A 143 ? 0.5470 0.9566 0.7941 -0.0357 -0.0316 0.0289  143 GLY A O   
1106 N N   . HIS A 144 ? 0.5173 0.9108 0.6793 -0.0086 -0.0566 0.0491  144 HIS A N   
1107 C CA  . HIS A 144 ? 0.5288 0.9598 0.6982 -0.0046 -0.0625 0.0557  144 HIS A CA  
1108 C C   . HIS A 144 ? 0.5686 1.0381 0.7315 -0.0190 -0.0646 0.0487  144 HIS A C   
1109 O O   . HIS A 144 ? 0.5362 1.0358 0.7037 -0.0253 -0.0660 0.0431  144 HIS A O   
1110 C CB  . HIS A 144 ? 0.5132 0.9474 0.6870 0.0124  -0.0675 0.0757  144 HIS A CB  
1111 C CG  . HIS A 144 ? 0.5483 1.0256 0.7297 0.0187  -0.0738 0.0860  144 HIS A CG  
1112 N ND1 . HIS A 144 ? 0.5565 1.0522 0.7371 0.0289  -0.0790 0.1037  144 HIS A ND1 
1113 C CD2 . HIS A 144 ? 0.5785 1.0866 0.7690 0.0167  -0.0756 0.0821  144 HIS A CD2 
1114 C CE1 . HIS A 144 ? 0.5397 1.0771 0.7291 0.0341  -0.0840 0.1113  144 HIS A CE1 
1115 N NE2 . HIS A 144 ? 0.5376 1.0844 0.7336 0.0264  -0.0822 0.0980  144 HIS A NE2 
1116 N N   . THR A 145 ? 0.5334 1.0040 0.6850 -0.0258 -0.0645 0.0482  145 THR A N   
1117 C CA  . THR A 145 ? 0.5550 1.0621 0.6983 -0.0418 -0.0656 0.0402  145 THR A CA  
1118 C C   . THR A 145 ? 0.5680 1.0729 0.7076 -0.0596 -0.0576 0.0189  145 THR A C   
1119 O O   . THR A 145 ? 0.6040 1.1455 0.7406 -0.0736 -0.0582 0.0107  145 THR A O   
1120 C CB  . THR A 145 ? 0.6158 1.1188 0.7466 -0.0462 -0.0652 0.0423  145 THR A CB  
1121 O OG1 . THR A 145 ? 0.5398 1.0368 0.6730 -0.0295 -0.0709 0.0621  145 THR A OG1 
1122 C CG2 . THR A 145 ? 0.5719 1.1184 0.6936 -0.0623 -0.0674 0.0366  145 THR A CG2 
1123 N N   . ALA A 146 ? 0.6429 1.1063 0.7824 -0.0599 -0.0494 0.0102  146 ALA A N   
1124 C CA  . ALA A 146 ? 0.6338 1.0902 0.7700 -0.0753 -0.0402 -0.0087 146 ALA A CA  
1125 C C   . ALA A 146 ? 0.6668 1.1423 0.8130 -0.0751 -0.0424 -0.0105 146 ALA A C   
1126 O O   . ALA A 146 ? 0.6494 1.1437 0.7921 -0.0915 -0.0379 -0.0246 146 ALA A O   
1127 C CB  . ALA A 146 ? 0.6499 1.0578 0.7840 -0.0732 -0.0309 -0.0144 146 ALA A CB  
1128 N N   . LEU A 147 ? 0.6409 1.1118 0.7992 -0.0576 -0.0482 0.0028  147 LEU A N   
1129 C CA  . LEU A 147 ? 0.6198 1.1110 0.7889 -0.0559 -0.0502 0.0021  147 LEU A CA  
1130 C C   . LEU A 147 ? 0.6706 1.2178 0.8422 -0.0611 -0.0573 0.0051  147 LEU A C   
1131 O O   . LEU A 147 ? 0.6672 1.2406 0.8426 -0.0708 -0.0563 -0.0037 147 LEU A O   
1132 C CB  . LEU A 147 ? 0.6050 1.0778 0.7861 -0.0356 -0.0535 0.0159  147 LEU A CB  
1133 C CG  . LEU A 147 ? 0.5859 1.0107 0.7669 -0.0317 -0.0469 0.0121  147 LEU A CG  
1134 C CD1 . LEU A 147 ? 0.5467 0.9586 0.7385 -0.0138 -0.0498 0.0250  147 LEU A CD1 
1135 C CD2 . LEU A 147 ? 0.5991 1.0155 0.7783 -0.0452 -0.0391 -0.0044 147 LEU A CD2 
1136 N N   . ARG A 148 ? 0.5986 1.1668 0.7676 -0.0552 -0.0644 0.0180  148 ARG A N   
1137 C CA  . ARG A 148 ? 0.5841 1.2103 0.7547 -0.0602 -0.0717 0.0227  148 ARG A CA  
1138 C C   . ARG A 148 ? 0.6317 1.2809 0.7909 -0.0868 -0.0666 0.0024  148 ARG A C   
1139 O O   . ARG A 148 ? 0.6639 1.3553 0.8270 -0.0967 -0.0686 -0.0031 148 ARG A O   
1140 C CB  . ARG A 148 ? 0.5743 1.2143 0.7417 -0.0497 -0.0792 0.0406  148 ARG A CB  
1141 C CG  . ARG A 148 ? 0.5500 1.1702 0.7279 -0.0242 -0.0830 0.0613  148 ARG A CG  
1142 C CD  . ARG A 148 ? 0.5395 1.1710 0.7124 -0.0150 -0.0889 0.0791  148 ARG A CD  
1143 N NE  . ARG A 148 ? 0.6123 1.2798 0.7968 0.0020  -0.0965 0.0998  148 ARG A NE  
1144 C CZ  . ARG A 148 ? 0.6330 1.3561 0.8170 -0.0014 -0.1037 0.1075  148 ARG A CZ  
1145 N NH1 . ARG A 148 ? 0.6315 1.3813 0.8027 -0.0233 -0.1044 0.0948  148 ARG A NH1 
1146 N NH2 . ARG A 148 ? 0.6037 1.3568 0.8000 0.0177  -0.1097 0.1290  148 ARG A NH2 
1147 N N   . ASN A 149 ? 0.6330 1.2545 0.7777 -0.0994 -0.0589 -0.0096 149 ASN A N   
1148 C CA  . ASN A 149 ? 0.6735 1.3121 0.8051 -0.1259 -0.0515 -0.0299 149 ASN A CA  
1149 C C   . ASN A 149 ? 0.6476 1.2788 0.7805 -0.1390 -0.0427 -0.0474 149 ASN A C   
1150 O O   . ASN A 149 ? 0.7311 1.3891 0.8555 -0.1620 -0.0375 -0.0637 149 ASN A O   
1151 C CB  . ASN A 149 ? 0.6418 1.2461 0.7589 -0.1337 -0.0431 -0.0381 149 ASN A CB  
1152 C CG  . ASN A 149 ? 0.6953 1.3207 0.7968 -0.1612 -0.0352 -0.0575 149 ASN A CG  
1153 O OD1 . ASN A 149 ? 0.7367 1.3313 0.8294 -0.1753 -0.0211 -0.0759 149 ASN A OD1 
1154 N ND2 . ASN A 149 ? 0.7505 1.4289 0.8480 -0.1692 -0.0432 -0.0534 149 ASN A ND2 
1155 N N   . ASN A 150 ? 0.6534 1.2494 0.7958 -0.1262 -0.0402 -0.0449 150 ASN A N   
1156 C CA  . ASN A 150 ? 0.7095 1.2977 0.8533 -0.1376 -0.0319 -0.0599 150 ASN A CA  
1157 C C   . ASN A 150 ? 0.6544 1.2924 0.8096 -0.1386 -0.0390 -0.0574 150 ASN A C   
1158 O O   . ASN A 150 ? 0.6829 1.3287 0.8368 -0.1545 -0.0321 -0.0727 150 ASN A O   
1159 C CB  . ASN A 150 ? 0.6611 1.1961 0.8103 -0.1240 -0.0268 -0.0576 150 ASN A CB  
1160 C CG  . ASN A 150 ? 0.6781 1.1661 0.8176 -0.1225 -0.0191 -0.0598 150 ASN A CG  
1161 O OD1 . ASN A 150 ? 0.6692 1.1558 0.7958 -0.1370 -0.0123 -0.0703 150 ASN A OD1 
1162 N ND2 . ASN A 150 ? 0.6294 1.0800 0.7750 -0.1054 -0.0196 -0.0503 150 ASN A ND2 
1163 N N   . HIS A 151 ? 0.5996 1.2716 0.7663 -0.1217 -0.0517 -0.0381 151 HIS A N   
1164 C CA  . HIS A 151 ? 0.6269 1.3468 0.8076 -0.1182 -0.0586 -0.0326 151 HIS A CA  
1165 C C   . HIS A 151 ? 0.6107 1.3958 0.7932 -0.1201 -0.0690 -0.0228 151 HIS A C   
1166 O O   . HIS A 151 ? 0.6091 1.4416 0.8039 -0.1180 -0.0747 -0.0181 151 HIS A O   
1167 C CB  . HIS A 151 ? 0.5547 1.2559 0.7523 -0.0915 -0.0629 -0.0159 151 HIS A CB  
1168 C CG  . HIS A 151 ? 0.5675 1.2135 0.7650 -0.0895 -0.0539 -0.0244 151 HIS A CG  
1169 N ND1 . HIS A 151 ? 0.5860 1.2328 0.7890 -0.0967 -0.0487 -0.0353 151 HIS A ND1 
1170 C CD2 . HIS A 151 ? 0.5742 1.1653 0.7667 -0.0815 -0.0493 -0.0228 151 HIS A CD2 
1171 C CE1 . HIS A 151 ? 0.5501 1.1440 0.7508 -0.0929 -0.0414 -0.0394 151 HIS A CE1 
1172 N NE2 . HIS A 151 ? 0.5564 1.1173 0.7512 -0.0836 -0.0419 -0.0318 151 HIS A NE2 
1173 N N   . MET A 152 ? 0.6074 1.3992 0.7786 -0.1239 -0.0717 -0.0190 152 MET A N   
1174 C CA  . MET A 152 ? 0.6263 1.4808 0.7982 -0.1247 -0.0823 -0.0072 152 MET A CA  
1175 C C   . MET A 152 ? 0.7022 1.5818 0.8554 -0.1547 -0.0779 -0.0253 152 MET A C   
1176 O O   . MET A 152 ? 0.7089 1.5467 0.8473 -0.1681 -0.0674 -0.0408 152 MET A O   
1177 C CB  . MET A 152 ? 0.6036 1.4496 0.7786 -0.1006 -0.0905 0.0174  152 MET A CB  
1178 C CG  . MET A 152 ? 0.6107 1.4378 0.8038 -0.0711 -0.0942 0.0366  152 MET A CG  
1179 S SD  . MET A 152 ? 0.6434 1.4354 0.8357 -0.0460 -0.0981 0.0600  152 MET A SD  
1180 C CE  . MET A 152 ? 0.5909 1.4506 0.7804 -0.0453 -0.1094 0.0775  152 MET A CE  
1181 N N   . ASP A 153 ? 0.6858 1.6357 0.8400 -0.1654 -0.0854 -0.0231 153 ASP A N   
1182 C CA  . ASP A 153 ? 0.6786 1.6597 0.8140 -0.1951 -0.0820 -0.0391 153 ASP A CA  
1183 C C   . ASP A 153 ? 0.6854 1.6609 0.8102 -0.1898 -0.0861 -0.0279 153 ASP A C   
1184 O O   . ASP A 153 ? 0.7903 1.7387 0.8974 -0.2072 -0.0767 -0.0437 153 ASP A O   
1185 C CB  . ASP A 153 ? 0.6835 1.7424 0.8216 -0.2082 -0.0884 -0.0394 153 ASP A CB  
1186 C CG  . ASP A 153 ? 0.7828 1.8434 0.9280 -0.2150 -0.0822 -0.0520 153 ASP A CG  
1187 O OD1 . ASP A 153 ? 0.8747 1.8963 1.0159 -0.2307 -0.0706 -0.0738 153 ASP A OD1 
1188 O OD2 . ASP A 153 ? 0.8863 1.9824 1.0394 -0.2035 -0.0875 -0.0394 153 ASP A OD2 
1189 N N   . ASP A 154 ? 0.6739 1.6740 0.8093 -0.1655 -0.0990 -0.0004 154 ASP A N   
1190 C CA  A ASP A 154 ? 0.6745 1.6643 0.8010 -0.1569 -0.1031 0.0133  154 ASP A CA  
1191 C CA  B ASP A 154 ? 0.6739 1.6655 0.8007 -0.1566 -0.1035 0.0139  154 ASP A CA  
1192 C C   . ASP A 154 ? 0.6513 1.5965 0.7904 -0.1236 -0.1066 0.0353  154 ASP A C   
1193 O O   . ASP A 154 ? 0.6296 1.5775 0.7865 -0.1039 -0.1105 0.0479  154 ASP A O   
1194 C CB  A ASP A 154 ? 0.6739 1.7384 0.7971 -0.1616 -0.1147 0.0269  154 ASP A CB  
1195 C CB  B ASP A 154 ? 0.6738 1.7413 0.7989 -0.1595 -0.1156 0.0290  154 ASP A CB  
1196 C CG  A ASP A 154 ? 0.6387 1.7395 0.7755 -0.1427 -0.1211 0.0464  154 ASP A CG  
1197 C CG  B ASP A 154 ? 0.6597 1.7600 0.7647 -0.1928 -0.1083 0.0072  154 ASP A CG  
1198 O OD1 A ASP A 154 ? 0.6133 1.6992 0.7680 -0.1284 -0.1212 0.0489  154 ASP A OD1 
1199 O OD1 B ASP A 154 ? 0.6596 1.7392 0.7569 -0.2171 -0.0975 -0.0205 154 ASP A OD1 
1200 O OD2 A ASP A 154 ? 0.6463 1.7891 0.7756 -0.1419 -0.1248 0.0593  154 ASP A OD2 
1201 O OD2 B ASP A 154 ? 0.6198 1.7644 0.7160 -0.1948 -0.1116 0.0179  154 ASP A OD2 
1202 N N   . LEU A 155 ? 0.6731 1.5764 0.8022 -0.1186 -0.1039 0.0388  155 LEU A N   
1203 C CA  . LEU A 155 ? 0.6998 1.5538 0.8372 -0.0914 -0.1047 0.0558  155 LEU A CA  
1204 C C   . LEU A 155 ? 0.6702 1.5473 0.8111 -0.0711 -0.1149 0.0843  155 LEU A C   
1205 O O   . LEU A 155 ? 0.6642 1.5019 0.8109 -0.0491 -0.1149 0.0994  155 LEU A O   
1206 C CB  . LEU A 155 ? 0.6732 1.4655 0.7988 -0.0970 -0.0947 0.0431  155 LEU A CB  
1207 C CG  . LEU A 155 ? 0.6737 1.4405 0.7925 -0.1182 -0.0825 0.0153  155 LEU A CG  
1208 C CD1 . LEU A 155 ? 0.6796 1.3918 0.7872 -0.1218 -0.0729 0.0059  155 LEU A CD1 
1209 C CD2 . LEU A 155 ? 0.6817 1.4318 0.8149 -0.1100 -0.0801 0.0123  155 LEU A CD2 
1210 N N   . PHE A 156 ? 0.6266 1.5667 0.7634 -0.0785 -0.1230 0.0922  156 PHE A N   
1211 C CA  . PHE A 156 ? 0.6942 1.6583 0.8316 -0.0608 -0.1321 0.1200  156 PHE A CA  
1212 C C   . PHE A 156 ? 0.6003 1.6098 0.7565 -0.0401 -0.1408 0.1428  156 PHE A C   
1213 O O   . PHE A 156 ? 0.5263 1.5719 0.6809 -0.0301 -0.1473 0.1644  156 PHE A O   
1214 C CB  . PHE A 156 ? 0.6129 1.6168 0.7318 -0.0818 -0.1352 0.1161  156 PHE A CB  
1215 C CG  . PHE A 156 ? 0.6966 1.6596 0.7977 -0.1038 -0.1248 0.0914  156 PHE A CG  
1216 C CD1 . PHE A 156 ? 0.5939 1.5074 0.6874 -0.0956 -0.1212 0.0964  156 PHE A CD1 
1217 C CD2 . PHE A 156 ? 0.6902 1.6629 0.7826 -0.1325 -0.1174 0.0631  156 PHE A CD2 
1218 C CE1 . PHE A 156 ? 0.6157 1.4931 0.6945 -0.1139 -0.1110 0.0747  156 PHE A CE1 
1219 C CE2 . PHE A 156 ? 0.6992 1.6318 0.7760 -0.1508 -0.1059 0.0412  156 PHE A CE2 
1220 C CZ  . PHE A 156 ? 0.6694 1.5555 0.7402 -0.1406 -0.1030 0.0475  156 PHE A CZ  
1221 N N   A ARG A 157 ? 0.6177 1.6181 0.7897 -0.0326 -0.1381 0.1382  157 ARG A N   
1222 N N   B ARG A 157 ? 0.6180 1.6179 0.7900 -0.0323 -0.1381 0.1384  157 ARG A N   
1223 C CA  A ARG A 157 ? 0.5822 1.6143 0.7725 -0.0119 -0.1425 0.1569  157 ARG A CA  
1224 C CA  B ARG A 157 ? 0.5822 1.6144 0.7724 -0.0116 -0.1425 0.1572  157 ARG A CA  
1225 C C   A ARG A 157 ? 0.5989 1.5808 0.8054 0.0106  -0.1379 0.1623  157 ARG A C   
1226 C C   B ARG A 157 ? 0.5985 1.5818 0.8052 0.0101  -0.1380 0.1618  157 ARG A C   
1227 O O   A ARG A 157 ? 0.6196 1.5424 0.8205 0.0042  -0.1295 0.1452  157 ARG A O   
1228 O O   B ARG A 157 ? 0.6212 1.5473 0.8227 0.0028  -0.1295 0.1436  157 ARG A O   
1229 C CB  A ARG A 157 ? 0.5684 1.6411 0.7584 -0.0298 -0.1403 0.1412  157 ARG A CB  
1230 C CB  B ARG A 157 ? 0.5677 1.6424 0.7568 -0.0299 -0.1406 0.1421  157 ARG A CB  
1231 C CG  A ARG A 157 ? 0.6161 1.6696 0.8099 -0.0478 -0.1348 0.1135  157 ARG A CG  
1232 C CG  B ARG A 157 ? 0.6129 1.6715 0.8029 -0.0516 -0.1350 0.1124  157 ARG A CG  
1233 C CD  A ARG A 157 ? 0.6060 1.6875 0.8087 -0.0507 -0.1324 0.1072  157 ARG A CD  
1234 C CD  B ARG A 157 ? 0.5999 1.6996 0.7848 -0.0727 -0.1318 0.0965  157 ARG A CD  
1235 N NE  A ARG A 157 ? 0.5900 1.6495 0.7969 -0.0666 -0.1262 0.0821  157 ARG A NE  
1236 N NE  B ARG A 157 ? 0.6477 1.7284 0.8305 -0.0960 -0.1245 0.0671  157 ARG A NE  
1237 C CZ  A ARG A 157 ? 0.5993 1.6730 0.7940 -0.0969 -0.1205 0.0566  157 ARG A CZ  
1238 C CZ  B ARG A 157 ? 0.5978 1.6618 0.7955 -0.0912 -0.1212 0.0600  157 ARG A CZ  
1239 N NH1 A ARG A 157 ? 0.6170 1.7292 0.7943 -0.1158 -0.1202 0.0515  157 ARG A NH1 
1240 N NH1 B ARG A 157 ? 0.5943 1.6578 0.8105 -0.0641 -0.1242 0.0787  157 ARG A NH1 
1241 N NH2 A ARG A 157 ? 0.5934 1.6387 0.7917 -0.1090 -0.1131 0.0355  157 ARG A NH2 
1242 N NH2 B ARG A 157 ? 0.5999 1.6410 0.7917 -0.1140 -0.1123 0.0330  157 ARG A NH2 
1243 N N   . PRO A 158 ? 0.5970 1.5919 0.8202 0.0369  -0.1403 0.1850  158 PRO A N   
1244 C CA  . PRO A 158 ? 0.5793 1.5303 0.8180 0.0554  -0.1342 0.1867  158 PRO A CA  
1245 C C   . PRO A 158 ? 0.5759 1.5361 0.8221 0.0409  -0.1309 0.1645  158 PRO A C   
1246 O O   . PRO A 158 ? 0.5591 1.5714 0.8067 0.0293  -0.1339 0.1592  158 PRO A O   
1247 C CB  . PRO A 158 ? 0.5881 1.5546 0.8401 0.0854  -0.1355 0.2161  158 PRO A CB  
1248 C CG  . PRO A 158 ? 0.5385 1.5309 0.7758 0.0846  -0.1397 0.2312  158 PRO A CG  
1249 C CD  . PRO A 158 ? 0.5828 1.6086 0.8046 0.0521  -0.1428 0.2094  158 PRO A CD  
1250 N N   . ALA A 159 ? 0.5826 1.4828 0.8289 0.0400  -0.1222 0.1500  159 ALA A N   
1251 C CA  . ALA A 159 ? 0.5944 1.4951 0.8453 0.0250  -0.1177 0.1279  159 ALA A CA  
1252 C C   . ALA A 159 ? 0.5105 1.4412 0.7837 0.0422  -0.1189 0.1385  159 ALA A C   
1253 O O   . ALA A 159 ? 0.5306 1.4472 0.8159 0.0690  -0.1181 0.1590  159 ALA A O   
1254 C CB  . ALA A 159 ? 0.5669 1.3953 0.8106 0.0199  -0.1081 0.1113  159 ALA A CB  
1255 N N   . ASN A 160 ? 0.4456 1.4174 0.7239 0.0260  -0.1196 0.1240  160 ASN A N   
1256 C CA  . ASN A 160 ? 0.4616 1.4606 0.7604 0.0400  -0.1194 0.1310  160 ASN A CA  
1257 C C   . ASN A 160 ? 0.4882 1.4302 0.7939 0.0463  -0.1102 0.1213  160 ASN A C   
1258 O O   . ASN A 160 ? 0.5259 1.4080 0.8186 0.0384  -0.1041 0.1086  160 ASN A O   
1259 C CB  . ASN A 160 ? 0.5283 1.5743 0.8211 0.0185  -0.1195 0.1168  160 ASN A CB  
1260 C CG  . ASN A 160 ? 0.4835 1.5221 0.7670 -0.0130 -0.1153 0.0865  160 ASN A CG  
1261 O OD1 . ASN A 160 ? 0.4813 1.4869 0.7713 -0.0153 -0.1091 0.0738  160 ASN A OD1 
1262 N ND2 . ASN A 160 ? 0.4799 1.5416 0.7442 -0.0381 -0.1161 0.0743  160 ASN A ND2 
1263 N N   . GLU A 161 ? 0.4271 1.3882 0.7526 0.0605  -0.1087 0.1273  161 GLU A N   
1264 C CA  A GLU A 161 ? 0.4365 1.3438 0.7678 0.0674  -0.0995 0.1194  161 GLU A CA  
1265 C CA  B GLU A 161 ? 0.4348 1.3440 0.7667 0.0676  -0.0996 0.1194  161 GLU A CA  
1266 C C   . GLU A 161 ? 0.4157 1.3031 0.7368 0.0402  -0.0942 0.0907  161 GLU A C   
1267 O O   . GLU A 161 ? 0.4613 1.2889 0.7766 0.0392  -0.0867 0.0811  161 GLU A O   
1268 C CB  A GLU A 161 ? 0.4184 1.3526 0.7739 0.0901  -0.0982 0.1335  161 GLU A CB  
1269 C CB  B GLU A 161 ? 0.4173 1.3585 0.7735 0.0882  -0.0987 0.1322  161 GLU A CB  
1270 C CG  A GLU A 161 ? 0.4009 1.3415 0.7664 0.1207  -0.1003 0.1635  161 GLU A CG  
1271 C CG  B GLU A 161 ? 0.3977 1.3041 0.7610 0.0873  -0.0896 0.1180  161 GLU A CG  
1272 C CD  A GLU A 161 ? 0.4133 1.3682 0.7965 0.1424  -0.0957 0.1762  161 GLU A CD  
1273 C CD  B GLU A 161 ? 0.3833 1.3281 0.7711 0.1055  -0.0882 0.1286  161 GLU A CD  
1274 O OE1 A GLU A 161 ? 0.4063 1.3737 0.7989 0.1353  -0.0925 0.1627  161 GLU A OE1 
1275 O OE1 B GLU A 161 ? 0.3986 1.3823 0.7909 0.1179  -0.0925 0.1459  161 GLU A OE1 
1276 O OE2 A GLU A 161 ? 0.4323 1.3843 0.8191 0.1664  -0.0945 0.1997  161 GLU A OE2 
1277 O OE2 B GLU A 161 ? 0.3785 1.2991 0.7734 0.1057  -0.0805 0.1180  161 GLU A OE2 
1278 N N   . THR A 162 ? 0.4218 1.3576 0.7393 0.0173  -0.0971 0.0770  162 THR A N   
1279 C CA  . THR A 162 ? 0.3857 1.2997 0.6917 -0.0093 -0.0901 0.0499  162 THR A CA  
1280 C C   . THR A 162 ? 0.4741 1.3333 0.7587 -0.0216 -0.0860 0.0393  162 THR A C   
1281 O O   . THR A 162 ? 0.4865 1.2948 0.7641 -0.0291 -0.0778 0.0251  162 THR A O   
1282 C CB  . THR A 162 ? 0.3792 1.3578 0.6842 -0.0332 -0.0929 0.0371  162 THR A CB  
1283 O OG1 . THR A 162 ? 0.4418 1.4691 0.7673 -0.0218 -0.0957 0.0458  162 THR A OG1 
1284 C CG2 . THR A 162 ? 0.3799 1.3308 0.6704 -0.0620 -0.0836 0.0089  162 THR A CG2 
1285 N N   . GLU A 163 ? 0.4869 1.3571 0.7613 -0.0231 -0.0913 0.0468  163 GLU A N   
1286 C CA  . GLU A 163 ? 0.5105 1.3318 0.7656 -0.0337 -0.0871 0.0377  163 GLU A CA  
1287 C C   . GLU A 163 ? 0.4582 1.2156 0.7143 -0.0150 -0.0831 0.0456  163 GLU A C   
1288 O O   . GLU A 163 ? 0.4603 1.1680 0.7050 -0.0238 -0.0762 0.0331  163 GLU A O   
1289 C CB  . GLU A 163 ? 0.4949 1.3456 0.7399 -0.0382 -0.0937 0.0455  163 GLU A CB  
1290 C CG  . GLU A 163 ? 0.5439 1.4567 0.7836 -0.0618 -0.0968 0.0345  163 GLU A CG  
1291 C CD  . GLU A 163 ? 0.5853 1.5369 0.8176 -0.0627 -0.1051 0.0467  163 GLU A CD  
1292 O OE1 . GLU A 163 ? 0.5393 1.4843 0.7768 -0.0393 -0.1104 0.0694  163 GLU A OE1 
1293 O OE2 . GLU A 163 ? 0.5591 1.5474 0.7795 -0.0877 -0.1054 0.0334  163 GLU A OE2 
1294 N N   . ILE A 164 ? 0.4452 1.2037 0.7146 0.0106  -0.0864 0.0666  164 ILE A N   
1295 C CA  . ILE A 164 ? 0.4563 1.1562 0.7259 0.0269  -0.0818 0.0738  164 ILE A CA  
1296 C C   . ILE A 164 ? 0.4562 1.1232 0.7306 0.0250  -0.0741 0.0614  164 ILE A C   
1297 O O   . ILE A 164 ? 0.4821 1.0962 0.7493 0.0250  -0.0686 0.0562  164 ILE A O   
1298 C CB  . ILE A 164 ? 0.5126 1.2215 0.7941 0.0540  -0.0852 0.0992  164 ILE A CB  
1299 C CG1 . ILE A 164 ? 0.5184 1.2552 0.7925 0.0554  -0.0925 0.1124  164 ILE A CG1 
1300 C CG2 . ILE A 164 ? 0.4596 1.1080 0.7407 0.0685  -0.0787 0.1047  164 ILE A CG2 
1301 C CD1 . ILE A 164 ? 0.4918 1.2403 0.7768 0.0824  -0.0953 0.1394  164 ILE A CD1 
1302 N N   . ALA A 165 ? 0.4492 1.1494 0.7358 0.0227  -0.0737 0.0566  165 ALA A N   
1303 C CA  . ALA A 165 ? 0.4374 1.1093 0.7278 0.0193  -0.0663 0.0443  165 ALA A CA  
1304 C C   . ALA A 165 ? 0.4385 1.0783 0.7125 -0.0033 -0.0606 0.0238  165 ALA A C   
1305 O O   . ALA A 165 ? 0.4305 1.0241 0.7010 -0.0033 -0.0542 0.0175  165 ALA A O   
1306 C CB  . ALA A 165 ? 0.3644 1.0837 0.6706 0.0190  -0.0669 0.0422  165 ALA A CB  
1307 N N   . GLY A 166 ? 0.4401 1.1039 0.7032 -0.0228 -0.0621 0.0135  166 GLY A N   
1308 C CA  . GLY A 166 ? 0.4445 1.0756 0.6914 -0.0431 -0.0548 -0.0050 166 GLY A CA  
1309 C C   . GLY A 166 ? 0.4839 1.0641 0.7198 -0.0381 -0.0525 -0.0017 166 GLY A C   
1310 O O   . GLY A 166 ? 0.4951 1.0346 0.7224 -0.0461 -0.0451 -0.0126 166 GLY A O   
1311 N N   . MET A 167 ? 0.4587 1.0416 0.6950 -0.0246 -0.0586 0.0139  167 MET A N   
1312 C CA  . MET A 167 ? 0.5124 1.0498 0.7389 -0.0198 -0.0566 0.0174  167 MET A CA  
1313 C C   . MET A 167 ? 0.4897 0.9853 0.7216 -0.0065 -0.0528 0.0217  167 MET A C   
1314 O O   . MET A 167 ? 0.5369 0.9913 0.7602 -0.0087 -0.0483 0.0177  167 MET A O   
1315 C CB  . MET A 167 ? 0.5097 1.0622 0.7344 -0.0100 -0.0635 0.0328  167 MET A CB  
1316 C CG  . MET A 167 ? 0.5747 1.1633 0.7899 -0.0255 -0.0667 0.0276  167 MET A CG  
1317 S SD  . MET A 167 ? 0.5608 1.1569 0.7701 -0.0155 -0.0735 0.0451  167 MET A SD  
1318 C CE  . MET A 167 ? 0.5300 1.1552 0.7572 0.0094  -0.0804 0.0685  167 MET A CE  
1319 N N   . ARG A 168 ? 0.4940 1.0012 0.7401 0.0069  -0.0540 0.0299  168 ARG A N   
1320 C CA  . ARG A 168 ? 0.4720 0.9411 0.7225 0.0176  -0.0492 0.0326  168 ARG A CA  
1321 C C   . ARG A 168 ? 0.5136 0.9589 0.7595 0.0046  -0.0425 0.0167  168 ARG A C   
1322 O O   . ARG A 168 ? 0.5041 0.9095 0.7454 0.0067  -0.0383 0.0156  168 ARG A O   
1323 C CB  . ARG A 168 ? 0.4149 0.9030 0.6820 0.0345  -0.0501 0.0439  168 ARG A CB  
1324 C CG  . ARG A 168 ? 0.4599 0.9591 0.7316 0.0522  -0.0545 0.0632  168 ARG A CG  
1325 C CD  . ARG A 168 ? 0.4691 0.9680 0.7560 0.0717  -0.0512 0.0746  168 ARG A CD  
1326 N NE  . ARG A 168 ? 0.4883 0.9393 0.7731 0.0745  -0.0436 0.0706  168 ARG A NE  
1327 C CZ  . ARG A 168 ? 0.4176 0.8544 0.7121 0.0900  -0.0379 0.0785  168 ARG A CZ  
1328 N NH1 . ARG A 168 ? 0.4016 0.8662 0.7100 0.1068  -0.0384 0.0924  168 ARG A NH1 
1329 N NH2 . ARG A 168 ? 0.4268 0.8211 0.7167 0.0886  -0.0309 0.0726  168 ARG A NH2 
1330 N N   . VAL A 169 ? 0.5259 0.9962 0.7724 -0.0094 -0.0411 0.0047  169 VAL A N   
1331 C CA  . VAL A 169 ? 0.4815 0.9287 0.7225 -0.0223 -0.0336 -0.0098 169 VAL A CA  
1332 C C   . VAL A 169 ? 0.4754 0.8903 0.7009 -0.0325 -0.0294 -0.0167 169 VAL A C   
1333 O O   . VAL A 169 ? 0.5543 0.9329 0.7748 -0.0338 -0.0239 -0.0204 169 VAL A O   
1334 C CB  . VAL A 169 ? 0.4729 0.9559 0.7176 -0.0360 -0.0320 -0.0213 169 VAL A CB  
1335 C CG1 . VAL A 169 ? 0.4740 0.9303 0.7101 -0.0512 -0.0230 -0.0365 169 VAL A CG1 
1336 C CG2 . VAL A 169 ? 0.4507 0.9640 0.7129 -0.0242 -0.0349 -0.0142 169 VAL A CG2 
1337 N N   . GLN A 170 ? 0.5062 0.9351 0.7239 -0.0397 -0.0316 -0.0180 170 GLN A N   
1338 C CA  . GLN A 170 ? 0.5206 0.9200 0.7244 -0.0487 -0.0263 -0.0247 170 GLN A CA  
1339 C C   . GLN A 170 ? 0.5187 0.8840 0.7205 -0.0359 -0.0274 -0.0143 170 GLN A C   
1340 O O   . GLN A 170 ? 0.5267 0.8591 0.7209 -0.0391 -0.0216 -0.0183 170 GLN A O   
1341 C CB  . GLN A 170 ? 0.5259 0.9504 0.7217 -0.0601 -0.0276 -0.0293 170 GLN A CB  
1342 C CG  . GLN A 170 ? 0.5253 0.9207 0.7069 -0.0709 -0.0196 -0.0382 170 GLN A CG  
1343 C CD  . GLN A 170 ? 0.5500 0.9709 0.7225 -0.0867 -0.0182 -0.0472 170 GLN A CD  
1344 O OE1 . GLN A 170 ? 0.6095 1.0707 0.7855 -0.0866 -0.0259 -0.0424 170 GLN A OE1 
1345 N NE2 . GLN A 170 ? 0.6092 1.0070 0.7694 -0.1004 -0.0073 -0.0600 170 GLN A NE2 
1346 N N   . LEU A 171 ? 0.5120 0.8854 0.7204 -0.0213 -0.0341 -0.0004 171 LEU A N   
1347 C CA  . LEU A 171 ? 0.4841 0.8261 0.6905 -0.0106 -0.0344 0.0087  171 LEU A CA  
1348 C C   . LEU A 171 ? 0.5468 0.8619 0.7563 -0.0070 -0.0301 0.0074  171 LEU A C   
1349 O O   . LEU A 171 ? 0.5763 0.8615 0.7801 -0.0061 -0.0274 0.0083  171 LEU A O   
1350 C CB  . LEU A 171 ? 0.4704 0.8256 0.6824 0.0034  -0.0408 0.0236  171 LEU A CB  
1351 C CG  . LEU A 171 ? 0.4598 0.7843 0.6694 0.0137  -0.0404 0.0332  171 LEU A CG  
1352 C CD1 . LEU A 171 ? 0.4802 0.7837 0.6783 0.0068  -0.0384 0.0296  171 LEU A CD1 
1353 C CD2 . LEU A 171 ? 0.4785 0.8159 0.6927 0.0269  -0.0450 0.0480  171 LEU A CD2 
1354 N N   . ARG A 172 ? 0.5419 0.8699 0.7605 -0.0055 -0.0294 0.0052  172 ARG A N   
1355 C CA  . ARG A 172 ? 0.5329 0.8378 0.7539 -0.0034 -0.0249 0.0032  172 ARG A CA  
1356 C C   . ARG A 172 ? 0.5679 0.8504 0.7797 -0.0150 -0.0189 -0.0067 172 ARG A C   
1357 O O   . ARG A 172 ? 0.5593 0.8146 0.7676 -0.0131 -0.0160 -0.0052 172 ARG A O   
1358 C CB  . ARG A 172 ? 0.5240 0.8507 0.7568 -0.0006 -0.0246 0.0016  172 ARG A CB  
1359 C CG  . ARG A 172 ? 0.5891 0.8946 0.8253 0.0029  -0.0200 0.0006  172 ARG A CG  
1360 C CD  . ARG A 172 ? 0.5638 0.8943 0.8126 0.0057  -0.0191 -0.0014 172 ARG A CD  
1361 N NE  . ARG A 172 ? 0.5596 0.9195 0.8186 0.0172  -0.0240 0.0085  172 ARG A NE  
1362 C CZ  . ARG A 172 ? 0.5516 0.9460 0.8228 0.0201  -0.0250 0.0087  172 ARG A CZ  
1363 N NH1 . ARG A 172 ? 0.5949 0.9992 0.8695 0.0111  -0.0214 -0.0020 172 ARG A NH1 
1364 N NH2 . ARG A 172 ? 0.4877 0.9090 0.7680 0.0327  -0.0295 0.0205  172 ARG A NH2 
1365 N N   . ASP A 173 ? 0.5387 0.8326 0.7458 -0.0275 -0.0161 -0.0166 173 ASP A N   
1366 C CA  . ASP A 173 ? 0.5624 0.8322 0.7600 -0.0376 -0.0084 -0.0249 173 ASP A CA  
1367 C C   . ASP A 173 ? 0.5860 0.8326 0.7753 -0.0352 -0.0073 -0.0206 173 ASP A C   
1368 O O   . ASP A 173 ? 0.5681 0.7889 0.7520 -0.0366 -0.0018 -0.0214 173 ASP A O   
1369 C CB  . ASP A 173 ? 0.5888 0.8744 0.7821 -0.0527 -0.0035 -0.0374 173 ASP A CB  
1370 C CG  . ASP A 173 ? 0.7230 1.0285 0.9235 -0.0575 -0.0025 -0.0436 173 ASP A CG  
1371 O OD1 . ASP A 173 ? 0.7420 1.0363 0.9475 -0.0520 -0.0017 -0.0411 173 ASP A OD1 
1372 O OD2 . ASP A 173 ? 0.6921 1.0262 0.8930 -0.0679 -0.0021 -0.0514 173 ASP A OD2 
1373 N N   . ALA A 174 ? 0.5783 0.8354 0.7668 -0.0313 -0.0123 -0.0152 174 ALA A N   
1374 C CA  . ALA A 174 ? 0.5304 0.7681 0.7120 -0.0288 -0.0113 -0.0110 174 ALA A CA  
1375 C C   . ALA A 174 ? 0.5687 0.7864 0.7522 -0.0190 -0.0131 -0.0019 174 ALA A C   
1376 O O   . ALA A 174 ? 0.5650 0.7618 0.7434 -0.0189 -0.0095 -0.0006 174 ALA A O   
1377 C CB  . ALA A 174 ? 0.5458 0.8016 0.7258 -0.0279 -0.0163 -0.0074 174 ALA A CB  
1378 N N   . LEU A 175 ? 0.5294 0.7541 0.7200 -0.0110 -0.0179 0.0044  175 LEU A N   
1379 C CA  . LEU A 175 ? 0.5611 0.7674 0.7523 -0.0041 -0.0183 0.0113  175 LEU A CA  
1380 C C   . LEU A 175 ? 0.5998 0.7899 0.7897 -0.0077 -0.0135 0.0074  175 LEU A C   
1381 O O   . LEU A 175 ? 0.5965 0.7699 0.7829 -0.0061 -0.0125 0.0114  175 LEU A O   
1382 C CB  . LEU A 175 ? 0.5537 0.7686 0.7523 0.0048  -0.0219 0.0179  175 LEU A CB  
1383 C CG  . LEU A 175 ? 0.4780 0.7097 0.6781 0.0103  -0.0268 0.0247  175 LEU A CG  
1384 C CD1 . LEU A 175 ? 0.4462 0.6844 0.6545 0.0209  -0.0282 0.0323  175 LEU A CD1 
1385 C CD2 . LEU A 175 ? 0.5027 0.7223 0.6952 0.0109  -0.0279 0.0297  175 LEU A CD2 
1386 N N   . ARG A 176 ? 0.5645 0.7615 0.7568 -0.0134 -0.0104 -0.0002 176 ARG A N   
1387 C CA  . ARG A 176 ? 0.6123 0.7941 0.8021 -0.0175 -0.0053 -0.0035 176 ARG A CA  
1388 C C   . ARG A 176 ? 0.6168 0.7819 0.7983 -0.0216 -0.0005 -0.0041 176 ARG A C   
1389 O O   . ARG A 176 ? 0.6088 0.7588 0.7871 -0.0217 0.0025  -0.0017 176 ARG A O   
1390 C CB  . ARG A 176 ? 0.6006 0.7945 0.7945 -0.0235 -0.0025 -0.0119 176 ARG A CB  
1391 C CG  . ARG A 176 ? 0.6412 0.8478 0.8447 -0.0180 -0.0051 -0.0105 176 ARG A CG  
1392 C CD  . ARG A 176 ? 0.6113 0.8370 0.8200 -0.0241 -0.0030 -0.0188 176 ARG A CD  
1393 N NE  . ARG A 176 ? 0.6367 0.8738 0.8558 -0.0175 -0.0040 -0.0172 176 ARG A NE  
1394 C CZ  . ARG A 176 ? 0.6571 0.9190 0.8847 -0.0190 -0.0039 -0.0218 176 ARG A CZ  
1395 N NH1 . ARG A 176 ? 0.6530 0.9327 0.8792 -0.0288 -0.0031 -0.0293 176 ARG A NH1 
1396 N NH2 . ARG A 176 ? 0.6663 0.9363 0.9042 -0.0110 -0.0036 -0.0191 176 ARG A NH2 
1397 N N   . GLN A 177 ? 0.6030 0.7713 0.7808 -0.0247 0.0011  -0.0069 177 GLN A N   
1398 C CA  . GLN A 177 ? 0.5932 0.7446 0.7637 -0.0272 0.0076  -0.0073 177 GLN A CA  
1399 C C   . GLN A 177 ? 0.5975 0.7417 0.7664 -0.0203 0.0051  0.0015  177 GLN A C   
1400 O O   . GLN A 177 ? 0.6722 0.8046 0.8365 -0.0203 0.0106  0.0025  177 GLN A O   
1401 C CB  . GLN A 177 ? 0.5991 0.7557 0.7655 -0.0357 0.0131  -0.0165 177 GLN A CB  
1402 C CG  . GLN A 177 ? 0.6422 0.8023 0.8080 -0.0454 0.0187  -0.0264 177 GLN A CG  
1403 C CD  . GLN A 177 ? 0.7034 0.8705 0.8637 -0.0566 0.0249  -0.0373 177 GLN A CD  
1404 O OE1 . GLN A 177 ? 0.6814 0.8570 0.8399 -0.0570 0.0230  -0.0376 177 GLN A OE1 
1405 N NE2 . GLN A 177 ? 0.7065 0.8702 0.8633 -0.0673 0.0330  -0.0469 177 GLN A NE2 
1406 N N   . GLY A 178 ? 0.5347 0.6854 0.7072 -0.0144 -0.0021 0.0078  178 GLY A N   
1407 C CA  . GLY A 178 ? 0.5562 0.7009 0.7269 -0.0093 -0.0044 0.0157  178 GLY A CA  
1408 C C   . GLY A 178 ? 0.5663 0.7203 0.7370 -0.0066 -0.0090 0.0186  178 GLY A C   
1409 O O   . GLY A 178 ? 0.5586 0.7083 0.7273 -0.0036 -0.0100 0.0244  178 GLY A O   
1410 N N   . ALA A 179 ? 0.5651 0.7339 0.7381 -0.0077 -0.0118 0.0155  179 ALA A N   
1411 C CA  . ALA A 179 ? 0.5108 0.6896 0.6831 -0.0049 -0.0164 0.0196  179 ALA A CA  
1412 C C   . ALA A 179 ? 0.5289 0.7033 0.7027 0.0014  -0.0205 0.0281  179 ALA A C   
1413 O O   . ALA A 179 ? 0.5113 0.6803 0.6882 0.0033  -0.0205 0.0293  179 ALA A O   
1414 C CB  . ALA A 179 ? 0.5182 0.7181 0.6931 -0.0071 -0.0191 0.0161  179 ALA A CB  
1415 N N   . LEU A 180 ? 0.5380 0.7136 0.7087 0.0036  -0.0228 0.0334  180 LEU A N   
1416 C CA  . LEU A 180 ? 0.5414 0.7101 0.7115 0.0078  -0.0249 0.0408  180 LEU A CA  
1417 C C   . LEU A 180 ? 0.5833 0.7599 0.7560 0.0130  -0.0282 0.0458  180 LEU A C   
1418 O O   . LEU A 180 ? 0.5519 0.7191 0.7242 0.0164  -0.0278 0.0512  180 LEU A O   
1419 C CB  . LEU A 180 ? 0.5544 0.7191 0.7193 0.0070  -0.0248 0.0444  180 LEU A CB  
1420 C CG  . LEU A 180 ? 0.5519 0.7096 0.7153 0.0045  -0.0210 0.0426  180 LEU A CG  
1421 C CD1 . LEU A 180 ? 0.5266 0.6841 0.6865 0.0047  -0.0211 0.0470  180 LEU A CD1 
1422 C CD2 . LEU A 180 ? 0.5899 0.7393 0.7549 0.0039  -0.0196 0.0429  180 LEU A CD2 
1423 N N   . GLY A 181 ? 0.5523 0.7463 0.7273 0.0135  -0.0305 0.0445  181 GLY A N   
1424 C CA  . GLY A 181 ? 0.5396 0.7447 0.7182 0.0204  -0.0335 0.0515  181 GLY A CA  
1425 C C   . GLY A 181 ? 0.5368 0.7661 0.7149 0.0188  -0.0371 0.0512  181 GLY A C   
1426 O O   . GLY A 181 ? 0.4828 0.7201 0.6589 0.0110  -0.0360 0.0427  181 GLY A O   
1427 N N   . LEU A 182 ? 0.5402 0.7807 0.7196 0.0258  -0.0404 0.0608  182 LEU A N   
1428 C CA  . LEU A 182 ? 0.5033 0.7721 0.6823 0.0248  -0.0448 0.0627  182 LEU A CA  
1429 C C   . LEU A 182 ? 0.5134 0.7821 0.6853 0.0269  -0.0469 0.0715  182 LEU A C   
1430 O O   . LEU A 182 ? 0.4917 0.7460 0.6629 0.0347  -0.0461 0.0812  182 LEU A O   
1431 C CB  . LEU A 182 ? 0.5072 0.7973 0.6957 0.0328  -0.0473 0.0684  182 LEU A CB  
1432 C CG  . LEU A 182 ? 0.4662 0.7926 0.6551 0.0323  -0.0527 0.0725  182 LEU A CG  
1433 C CD1 . LEU A 182 ? 0.4763 0.8223 0.6638 0.0188  -0.0527 0.0587  182 LEU A CD1 
1434 C CD2 . LEU A 182 ? 0.4503 0.7954 0.6492 0.0455  -0.0552 0.0846  182 LEU A CD2 
1435 N N   . SER A 183 ? 0.5274 0.8111 0.6930 0.0191  -0.0486 0.0675  183 SER A N   
1436 C CA  . SER A 183 ? 0.5331 0.8213 0.6912 0.0196  -0.0508 0.0752  183 SER A CA  
1437 C C   . SER A 183 ? 0.5321 0.8551 0.6902 0.0200  -0.0562 0.0803  183 SER A C   
1438 O O   . SER A 183 ? 0.5393 0.8849 0.7003 0.0138  -0.0573 0.0726  183 SER A O   
1439 C CB  . SER A 183 ? 0.5290 0.8078 0.6789 0.0099  -0.0477 0.0669  183 SER A CB  
1440 O OG  . SER A 183 ? 0.5364 0.8309 0.6845 -0.0003 -0.0463 0.0552  183 SER A OG  
1441 N N   . THR A 184 ? 0.5530 0.8815 0.7075 0.0266  -0.0591 0.0937  184 THR A N   
1442 C CA  . THR A 184 ? 0.5898 0.9542 0.7435 0.0278  -0.0648 0.1016  184 THR A CA  
1443 C C   . THR A 184 ? 0.6460 1.0141 0.7880 0.0236  -0.0662 0.1063  184 THR A C   
1444 O O   . THR A 184 ? 0.6420 0.9837 0.7787 0.0255  -0.0633 0.1099  184 THR A O   
1445 C CB  . THR A 184 ? 0.5568 0.9302 0.7191 0.0438  -0.0672 0.1178  184 THR A CB  
1446 O OG1 . THR A 184 ? 0.5648 0.9074 0.7244 0.0533  -0.0636 0.1287  184 THR A OG1 
1447 C CG2 . THR A 184 ? 0.5727 0.9480 0.7472 0.0475  -0.0657 0.1126  184 THR A CG2 
1448 N N   . GLY A 185 ? 0.6044 1.0074 0.7420 0.0163  -0.0704 0.1055  185 GLY A N   
1449 C CA  . GLY A 185 ? 0.6146 1.0282 0.7409 0.0122  -0.0725 0.1114  185 GLY A CA  
1450 C C   . GLY A 185 ? 0.6128 1.0668 0.7396 0.0172  -0.0795 0.1253  185 GLY A C   
1451 O O   . GLY A 185 ? 0.6417 1.1309 0.7642 0.0058  -0.0828 0.1194  185 GLY A O   
1452 N N   . LEU A 186 ? 0.6792 1.1290 0.8110 0.0340  -0.0812 0.1442  186 LEU A N   
1453 C CA  . LEU A 186 ? 0.6717 1.1615 0.8078 0.0429  -0.0876 0.1601  186 LEU A CA  
1454 C C   . LEU A 186 ? 0.6657 1.1830 0.7896 0.0376  -0.0923 0.1687  186 LEU A C   
1455 O O   . LEU A 186 ? 0.6546 1.2179 0.7798 0.0376  -0.0988 0.1764  186 LEU A O   
1456 C CB  . LEU A 186 ? 0.7074 1.1801 0.8526 0.0642  -0.0857 0.1786  186 LEU A CB  
1457 C CG  . LEU A 186 ? 0.6627 1.1088 0.8196 0.0698  -0.0805 0.1710  186 LEU A CG  
1458 C CD1 . LEU A 186 ? 0.7031 1.1227 0.8654 0.0891  -0.0755 0.1880  186 LEU A CD1 
1459 C CD2 . LEU A 186 ? 0.5857 1.0662 0.7538 0.0674  -0.0841 0.1637  186 LEU A CD2 
1460 N N   . ALA A 187 ? 0.7054 1.1982 0.8174 0.0324  -0.0891 0.1678  187 ALA A N   
1461 C CA  . ALA A 187 ? 0.6618 1.1788 0.7610 0.0268  -0.0929 0.1761  187 ALA A CA  
1462 C C   . ALA A 187 ? 0.6160 1.1714 0.7088 0.0074  -0.0960 0.1611  187 ALA A C   
1463 O O   . ALA A 187 ? 0.6771 1.2666 0.7607 0.0023  -0.1008 0.1688  187 ALA A O   
1464 C CB  . ALA A 187 ? 0.7049 1.1857 0.7930 0.0240  -0.0878 0.1761  187 ALA A CB  
1465 N N   . TYR A 188 ? 0.6002 1.1504 0.6967 -0.0041 -0.0924 0.1399  188 TYR A N   
1466 C CA  . TYR A 188 ? 0.6296 1.2113 0.7189 -0.0245 -0.0926 0.1231  188 TYR A CA  
1467 C C   . TYR A 188 ? 0.6931 1.3262 0.7885 -0.0251 -0.0997 0.1277  188 TYR A C   
1468 O O   . TYR A 188 ? 0.6644 1.3017 0.7735 -0.0110 -0.1023 0.1369  188 TYR A O   
1469 C CB  . TYR A 188 ? 0.6118 1.1651 0.7021 -0.0362 -0.0841 0.0994  188 TYR A CB  
1470 C CG  . TYR A 188 ? 0.6562 1.1667 0.7405 -0.0370 -0.0772 0.0944  188 TYR A CG  
1471 C CD1 . TYR A 188 ? 0.6736 1.1868 0.7448 -0.0508 -0.0735 0.0858  188 TYR A CD1 
1472 C CD2 . TYR A 188 ? 0.6947 1.1648 0.7866 -0.0245 -0.0741 0.0983  188 TYR A CD2 
1473 C CE1 . TYR A 188 ? 0.6754 1.1532 0.7426 -0.0509 -0.0671 0.0819  188 TYR A CE1 
1474 C CE2 . TYR A 188 ? 0.6715 1.1078 0.7586 -0.0257 -0.0683 0.0943  188 TYR A CE2 
1475 C CZ  . TYR A 188 ? 0.7275 1.1685 0.8029 -0.0383 -0.0650 0.0865  188 TYR A CZ  
1476 O OH  . TYR A 188 ? 0.6663 1.0772 0.7383 -0.0390 -0.0590 0.0830  188 TYR A OH  
1477 N N   . ALA A 189 ? 0.6247 1.2992 0.7098 -0.0426 -0.1022 0.1207  189 ALA A N   
1478 C CA  . ALA A 189 ? 0.5809 1.3135 0.6702 -0.0451 -0.1099 0.1266  189 ALA A CA  
1479 C C   . ALA A 189 ? 0.6416 1.3798 0.7427 -0.0490 -0.1079 0.1128  189 ALA A C   
1480 O O   . ALA A 189 ? 0.6251 1.4043 0.7361 -0.0432 -0.1144 0.1219  189 ALA A O   
1481 C CB  . ALA A 189 ? 0.5175 1.2928 0.5910 -0.0672 -0.1118 0.1186  189 ALA A CB  
1482 N N   . SER A 190 ? 0.6048 1.3037 0.7051 -0.0583 -0.0987 0.0918  190 SER A N   
1483 C CA  . SER A 190 ? 0.6424 1.3426 0.7524 -0.0630 -0.0956 0.0781  190 SER A CA  
1484 C C   . SER A 190 ? 0.6150 1.3000 0.7422 -0.0405 -0.0981 0.0917  190 SER A C   
1485 O O   . SER A 190 ? 0.5799 1.2746 0.7167 -0.0424 -0.0972 0.0839  190 SER A O   
1486 C CB  . SER A 190 ? 0.6481 1.3071 0.7519 -0.0775 -0.0840 0.0541  190 SER A CB  
1487 O OG  . SER A 190 ? 0.7981 1.4685 0.8858 -0.0987 -0.0793 0.0400  190 SER A OG  
1488 N N   . ALA A 191 ? 0.6065 1.2672 0.7373 -0.0204 -0.1001 0.1108  191 ALA A N   
1489 C CA  . ALA A 191 ? 0.6096 1.2533 0.7557 0.0006  -0.1005 0.1233  191 ALA A CA  
1490 C C   . ALA A 191 ? 0.6865 1.3399 0.8364 0.0215  -0.1058 0.1506  191 ALA A C   
1491 O O   . ALA A 191 ? 0.7363 1.3687 0.8976 0.0403  -0.1041 0.1622  191 ALA A O   
1492 C CB  . ALA A 191 ? 0.6234 1.2073 0.7708 0.0041  -0.0925 0.1145  191 ALA A CB  
1493 N N   . PHE A 192 ? 0.6318 1.3152 0.7719 0.0188  -0.1110 0.1615  192 PHE A N   
1494 C CA  . PHE A 192 ? 0.6433 1.3331 0.7857 0.0394  -0.1148 0.1892  192 PHE A CA  
1495 C C   . PHE A 192 ? 0.6570 1.3900 0.8147 0.0545  -0.1204 0.2054  192 PHE A C   
1496 O O   . PHE A 192 ? 0.7056 1.4293 0.8714 0.0775  -0.1199 0.2277  192 PHE A O   
1497 C CB  . PHE A 192 ? 0.6127 1.3235 0.7391 0.0314  -0.1187 0.1966  192 PHE A CB  
1498 C CG  . PHE A 192 ? 0.6077 1.3181 0.7336 0.0521  -0.1211 0.2257  192 PHE A CG  
1499 C CD1 . PHE A 192 ? 0.6448 1.3005 0.7681 0.0637  -0.1145 0.2331  192 PHE A CD1 
1500 C CD2 . PHE A 192 ? 0.5720 1.3375 0.6997 0.0595  -0.1292 0.2460  192 PHE A CD2 
1501 C CE1 . PHE A 192 ? 0.6300 1.2813 0.7516 0.0821  -0.1146 0.2597  192 PHE A CE1 
1502 C CE2 . PHE A 192 ? 0.5312 1.2940 0.6580 0.0798  -0.1301 0.2744  192 PHE A CE2 
1503 C CZ  . PHE A 192 ? 0.5585 1.2618 0.6818 0.0911  -0.1222 0.2810  192 PHE A CZ  
1504 N N   . GLN A 193 ? 0.6044 1.3846 0.7665 0.0418  -0.1247 0.1947  193 GLN A N   
1505 C CA  . GLN A 193 ? 0.6228 1.4507 0.8009 0.0549  -0.1302 0.2089  193 GLN A CA  
1506 C C   . GLN A 193 ? 0.7452 1.5485 0.9402 0.0663  -0.1250 0.2043  193 GLN A C   
1507 O O   . GLN A 193 ? 0.7178 1.5608 0.9278 0.0755  -0.1286 0.2124  193 GLN A O   
1508 C CB  . GLN A 193 ? 0.6197 1.5142 0.7946 0.0343  -0.1370 0.1989  193 GLN A CB  
1509 C CG  . GLN A 193 ? 0.5861 1.5210 0.7470 0.0268  -0.1439 0.2098  193 GLN A CG  
1510 C CD  . GLN A 193 ? 0.6043 1.5528 0.7708 0.0538  -0.1486 0.2441  193 GLN A CD  
1511 O OE1 . GLN A 193 ? 0.5300 1.4390 0.6883 0.0635  -0.1455 0.2554  193 GLN A OE1 
1512 N NE2 . GLN A 193 ? 0.5131 1.4999 0.6890 0.0645  -0.1500 0.2571  193 GLN A NE2 
1513 N N   . SER A 194 ? 0.6774 1.4192 0.8704 0.0656  -0.1168 0.1919  194 SER A N   
1514 C CA  . SER A 194 ? 0.6235 1.3389 0.8310 0.0761  -0.1113 0.1879  194 SER A CA  
1515 C C   . SER A 194 ? 0.6588 1.3563 0.8766 0.1043  -0.1086 0.2124  194 SER A C   
1516 O O   . SER A 194 ? 0.6660 1.3346 0.8756 0.1130  -0.1062 0.2251  194 SER A O   
1517 C CB  . SER A 194 ? 0.6293 1.2881 0.8300 0.0646  -0.1035 0.1667  194 SER A CB  
1518 O OG  . SER A 194 ? 0.6557 1.2678 0.8483 0.0721  -0.0992 0.1740  194 SER A OG  
1519 N N   . THR A 195 ? 0.6407 1.3546 0.8762 0.1182  -0.1077 0.2188  195 THR A N   
1520 C CA  . THR A 195 ? 0.6176 1.3080 0.8638 0.1453  -0.1019 0.2399  195 THR A CA  
1521 C C   . THR A 195 ? 0.6687 1.2898 0.9123 0.1465  -0.0915 0.2294  195 THR A C   
1522 O O   . THR A 195 ? 0.6705 1.2694 0.9094 0.1294  -0.0893 0.2066  195 THR A O   
1523 C CB  . THR A 195 ? 0.6746 1.4054 0.9418 0.1603  -0.1031 0.2494  195 THR A CB  
1524 O OG1 . THR A 195 ? 0.6438 1.3917 0.9159 0.1429  -0.1044 0.2263  195 THR A OG1 
1525 C CG2 . THR A 195 ? 0.6342 1.4302 0.9060 0.1697  -0.1121 0.2716  195 THR A CG2 
1526 N N   . THR A 196 ? 0.7125 1.2993 0.9581 0.1666  -0.0842 0.2469  196 THR A N   
1527 C CA  . THR A 196 ? 0.7406 1.2660 0.9852 0.1686  -0.0733 0.2381  196 THR A CA  
1528 C C   . THR A 196 ? 0.7804 1.3060 1.0391 0.1686  -0.0699 0.2253  196 THR A C   
1529 O O   . THR A 196 ? 0.7090 1.1950 0.9642 0.1592  -0.0641 0.2083  196 THR A O   
1530 C CB  . THR A 196 ? 0.8151 1.3073 1.0599 0.1904  -0.0643 0.2599  196 THR A CB  
1531 O OG1 . THR A 196 ? 0.8520 1.3429 1.0823 0.1890  -0.0673 0.2715  196 THR A OG1 
1532 C CG2 . THR A 196 ? 0.7734 1.2034 1.0154 0.1898  -0.0523 0.2495  196 THR A CG2 
1533 N N   . GLU A 197 ? 0.7882 1.3612 1.0626 0.1784  -0.0736 0.2333  197 GLU A N   
1534 C CA  . GLU A 197 ? 0.7007 1.2793 0.9892 0.1783  -0.0704 0.2216  197 GLU A CA  
1535 C C   . GLU A 197 ? 0.7137 1.2930 0.9953 0.1522  -0.0738 0.1946  197 GLU A C   
1536 O O   . GLU A 197 ? 0.7362 1.2897 1.0213 0.1473  -0.0680 0.1800  197 GLU A O   
1537 C CB  . GLU A 197 ? 0.6279 1.2662 0.9346 0.1927  -0.0749 0.2362  197 GLU A CB  
1538 C CG  . GLU A 197 ? 0.5768 1.2147 0.9018 0.2035  -0.0680 0.2334  197 GLU A CG  
1539 C CD  . GLU A 197 ? 0.6428 1.3452 0.9869 0.2185  -0.0728 0.2494  197 GLU A CD  
1540 O OE1 . GLU A 197 ? 0.6759 1.4343 1.0189 0.2068  -0.0840 0.2479  197 GLU A OE1 
1541 O OE2 . GLU A 197 ? 0.7322 1.4308 1.0924 0.2419  -0.0648 0.2635  197 GLU A OE2 
1542 N N   . GLU A 198 ? 0.6130 1.2207 0.8839 0.1351  -0.0821 0.1879  198 GLU A N   
1543 C CA  . GLU A 198 ? 0.5484 1.1538 0.8114 0.1105  -0.0833 0.1628  198 GLU A CA  
1544 C C   . GLU A 198 ? 0.5757 1.1205 0.8278 0.1031  -0.0765 0.1504  198 GLU A C   
1545 O O   . GLU A 198 ? 0.5163 1.0422 0.7690 0.0929  -0.0726 0.1333  198 GLU A O   
1546 C CB  . GLU A 198 ? 0.6198 1.2643 0.8720 0.0937  -0.0914 0.1584  198 GLU A CB  
1547 C CG  . GLU A 198 ? 0.5823 1.2154 0.8233 0.0682  -0.0900 0.1329  198 GLU A CG  
1548 C CD  . GLU A 198 ? 0.5743 1.2399 0.8025 0.0507  -0.0957 0.1277  198 GLU A CD  
1549 O OE1 . GLU A 198 ? 0.6343 1.3408 0.8635 0.0571  -0.1024 0.1434  198 GLU A OE1 
1550 O OE2 . GLU A 198 ? 0.5502 1.2004 0.7670 0.0308  -0.0927 0.1081  198 GLU A OE2 
1551 N N   . VAL A 199 ? 0.6025 1.1180 0.8443 0.1077  -0.0750 0.1594  199 VAL A N   
1552 C CA  . VAL A 199 ? 0.5905 1.0524 0.8224 0.1013  -0.0687 0.1494  199 VAL A CA  
1553 C C   . VAL A 199 ? 0.5659 0.9948 0.8065 0.1113  -0.0603 0.1487  199 VAL A C   
1554 O O   . VAL A 199 ? 0.5402 0.9367 0.7766 0.1020  -0.0558 0.1346  199 VAL A O   
1555 C CB  . VAL A 199 ? 0.5609 1.0028 0.7804 0.1042  -0.0685 0.1603  199 VAL A CB  
1556 C CG1 . VAL A 199 ? 0.5716 0.9645 0.7810 0.0957  -0.0627 0.1493  199 VAL A CG1 
1557 C CG2 . VAL A 199 ? 0.5916 1.0694 0.8024 0.0940  -0.0765 0.1613  199 VAL A CG2 
1558 N N   . MET A 200 ? 0.5503 0.9878 0.8031 0.1306  -0.0575 0.1642  200 MET A N   
1559 C CA  . MET A 200 ? 0.5542 0.9613 0.8154 0.1400  -0.0480 0.1629  200 MET A CA  
1560 C C   . MET A 200 ? 0.5508 0.9660 0.8188 0.1294  -0.0477 0.1451  200 MET A C   
1561 O O   . MET A 200 ? 0.5249 0.9052 0.7916 0.1255  -0.0409 0.1347  200 MET A O   
1562 C CB  . MET A 200 ? 0.5467 0.9660 0.8212 0.1638  -0.0440 0.1835  200 MET A CB  
1563 C CG  . MET A 200 ? 0.5436 0.9356 0.8110 0.1768  -0.0387 0.2013  200 MET A CG  
1564 S SD  . MET A 200 ? 0.6188 1.0388 0.9019 0.2060  -0.0360 0.2295  200 MET A SD  
1565 C CE  . MET A 200 ? 0.6438 0.9995 0.9204 0.2199  -0.0196 0.2407  200 MET A CE  
1566 N N   . ALA A 201 ? 0.4936 0.9557 0.7679 0.1235  -0.0548 0.1412  201 ALA A N   
1567 C CA  . ALA A 201 ? 0.4527 0.9236 0.7326 0.1124  -0.0539 0.1242  201 ALA A CA  
1568 C C   . ALA A 201 ? 0.4837 0.9237 0.7501 0.0931  -0.0525 0.1059  201 ALA A C   
1569 O O   . ALA A 201 ? 0.4643 0.8834 0.7322 0.0878  -0.0474 0.0942  201 ALA A O   
1570 C CB  . ALA A 201 ? 0.4574 0.9867 0.7446 0.1071  -0.0614 0.1231  201 ALA A CB  
1571 N N   . LEU A 202 ? 0.5016 0.9390 0.7548 0.0830  -0.0565 0.1038  202 LEU A N   
1572 C CA  . LEU A 202 ? 0.4949 0.9042 0.7361 0.0667  -0.0544 0.0882  202 LEU A CA  
1573 C C   . LEU A 202 ? 0.4933 0.8546 0.7296 0.0709  -0.0482 0.0891  202 LEU A C   
1574 O O   . LEU A 202 ? 0.4969 0.8344 0.7295 0.0619  -0.0444 0.0771  202 LEU A O   
1575 C CB  . LEU A 202 ? 0.4873 0.9088 0.7166 0.0554  -0.0592 0.0857  202 LEU A CB  
1576 C CG  . LEU A 202 ? 0.4870 0.9576 0.7181 0.0470  -0.0649 0.0825  202 LEU A CG  
1577 C CD1 . LEU A 202 ? 0.5053 0.9797 0.7222 0.0313  -0.0668 0.0744  202 LEU A CD1 
1578 C CD2 . LEU A 202 ? 0.4794 0.9648 0.7182 0.0392  -0.0629 0.0698  202 LEU A CD2 
1579 N N   . ALA A 203 ? 0.5303 0.8778 0.7661 0.0838  -0.0466 0.1035  203 ALA A N   
1580 C CA  . ALA A 203 ? 0.5210 0.8248 0.7510 0.0857  -0.0398 0.1036  203 ALA A CA  
1581 C C   . ALA A 203 ? 0.4954 0.7820 0.7333 0.0899  -0.0326 0.0992  203 ALA A C   
1582 O O   . ALA A 203 ? 0.4830 0.7358 0.7150 0.0859  -0.0270 0.0941  203 ALA A O   
1583 C CB  . ALA A 203 ? 0.5275 0.8197 0.7538 0.0974  -0.0381 0.1198  203 ALA A CB  
1584 N N   . GLU A 204 ? 0.4628 0.7744 0.7140 0.0971  -0.0325 0.1008  204 GLU A N   
1585 C CA  . GLU A 204 ? 0.4913 0.7883 0.7503 0.1003  -0.0251 0.0954  204 GLU A CA  
1586 C C   . GLU A 204 ? 0.4748 0.7600 0.7286 0.0842  -0.0245 0.0783  204 GLU A C   
1587 O O   . GLU A 204 ? 0.5064 0.7681 0.7608 0.0831  -0.0176 0.0726  204 GLU A O   
1588 C CB  . GLU A 204 ? 0.4616 0.7927 0.7370 0.1117  -0.0253 0.1010  204 GLU A CB  
1589 C CG  . GLU A 204 ? 0.4380 0.7715 0.7213 0.1325  -0.0215 0.1198  204 GLU A CG  
1590 C CD  . GLU A 204 ? 0.4858 0.8540 0.7875 0.1454  -0.0206 0.1258  204 GLU A CD  
1591 O OE1 . GLU A 204 ? 0.4499 0.8423 0.7576 0.1364  -0.0237 0.1144  204 GLU A OE1 
1592 O OE2 . GLU A 204 ? 0.4985 0.8700 0.8088 0.1649  -0.0162 0.1426  204 GLU A OE2 
1593 N N   . GLU A 205 ? 0.4585 0.7591 0.7066 0.0715  -0.0305 0.0703  205 GLU A N   
1594 C CA  . GLU A 205 ? 0.4893 0.7763 0.7315 0.0572  -0.0289 0.0559  205 GLU A CA  
1595 C C   . GLU A 205 ? 0.5475 0.7979 0.7789 0.0529  -0.0255 0.0543  205 GLU A C   
1596 O O   . GLU A 205 ? 0.5244 0.7598 0.7519 0.0440  -0.0228 0.0449  205 GLU A O   
1597 C CB  . GLU A 205 ? 0.5053 0.8139 0.7428 0.0450  -0.0339 0.0482  205 GLU A CB  
1598 C CG  . GLU A 205 ? 0.5274 0.8774 0.7743 0.0453  -0.0374 0.0478  205 GLU A CG  
1599 C CD  . GLU A 205 ? 0.5416 0.8983 0.7970 0.0426  -0.0336 0.0394  205 GLU A CD  
1600 O OE1 . GLU A 205 ? 0.5634 0.8945 0.8140 0.0353  -0.0290 0.0304  205 GLU A OE1 
1601 O OE2 . GLU A 205 ? 0.4867 0.8764 0.7537 0.0480  -0.0353 0.0423  205 GLU A OE2 
1602 N N   . LEU A 206 ? 0.5119 0.7493 0.7383 0.0588  -0.0255 0.0636  206 LEU A N   
1603 C CA  . LEU A 206 ? 0.5252 0.7319 0.7415 0.0541  -0.0223 0.0626  206 LEU A CA  
1604 C C   . LEU A 206 ? 0.5452 0.7275 0.7627 0.0584  -0.0143 0.0636  206 LEU A C   
1605 O O   . LEU A 206 ? 0.5602 0.7189 0.7690 0.0532  -0.0111 0.0623  206 LEU A O   
1606 C CB  . LEU A 206 ? 0.5129 0.7174 0.7218 0.0561  -0.0253 0.0711  206 LEU A CB  
1607 C CG  . LEU A 206 ? 0.4923 0.7203 0.6985 0.0513  -0.0322 0.0703  206 LEU A CG  
1608 C CD1 . LEU A 206 ? 0.5182 0.7441 0.7175 0.0544  -0.0344 0.0799  206 LEU A CD1 
1609 C CD2 . LEU A 206 ? 0.4844 0.7081 0.6850 0.0386  -0.0325 0.0586  206 LEU A CD2 
1610 N N   . ALA A 207 ? 0.5374 0.7261 0.7653 0.0672  -0.0104 0.0655  207 ALA A N   
1611 C CA  . ALA A 207 ? 0.5418 0.7060 0.7707 0.0709  -0.0007 0.0654  207 ALA A CA  
1612 C C   . ALA A 207 ? 0.6444 0.7937 0.8679 0.0583  0.0022  0.0533  207 ALA A C   
1613 O O   . ALA A 207 ? 0.6269 0.7870 0.8490 0.0494  -0.0026 0.0459  207 ALA A O   
1614 C CB  . ALA A 207 ? 0.5646 0.7414 0.8074 0.0842  0.0036  0.0700  207 ALA A CB  
1615 N N   . ALA A 208 ? 0.5853 0.7091 0.8049 0.0571  0.0112  0.0516  208 ALA A N   
1616 C CA  . ALA A 208 ? 0.5871 0.6970 0.8001 0.0446  0.0147  0.0413  208 ALA A CA  
1617 C C   . ALA A 208 ? 0.5698 0.6789 0.7725 0.0332  0.0084  0.0387  208 ALA A C   
1618 O O   . ALA A 208 ? 0.5905 0.7027 0.7906 0.0243  0.0066  0.0318  208 ALA A O   
1619 C CB  . ALA A 208 ? 0.6280 0.7504 0.8490 0.0430  0.0155  0.0337  208 ALA A CB  
1620 N N   . GLY A 209 ? 0.5885 0.6938 0.7854 0.0343  0.0056  0.0452  209 GLY A N   
1621 C CA  . GLY A 209 ? 0.6123 0.7163 0.8000 0.0248  0.0011  0.0437  209 GLY A CA  
1622 C C   . GLY A 209 ? 0.5993 0.7213 0.7889 0.0221  -0.0062 0.0411  209 GLY A C   
1623 O O   . GLY A 209 ? 0.6734 0.7939 0.8573 0.0141  -0.0079 0.0380  209 GLY A O   
1624 N N   . LYS A 210 ? 0.5626 0.7022 0.7598 0.0282  -0.0096 0.0423  210 LYS A N   
1625 C CA  . LYS A 210 ? 0.5837 0.7390 0.7816 0.0240  -0.0145 0.0382  210 LYS A CA  
1626 C C   . LYS A 210 ? 0.5595 0.7230 0.7537 0.0246  -0.0193 0.0425  210 LYS A C   
1627 O O   . LYS A 210 ? 0.5595 0.7374 0.7544 0.0216  -0.0222 0.0391  210 LYS A O   
1628 C CB  . LYS A 210 ? 0.5682 0.7414 0.7755 0.0269  -0.0148 0.0349  210 LYS A CB  
1629 C CG  . LYS A 210 ? 0.6019 0.7690 0.8128 0.0249  -0.0097 0.0290  210 LYS A CG  
1630 C CD  . LYS A 210 ? 0.6717 0.8572 0.8888 0.0220  -0.0105 0.0225  210 LYS A CD  
1631 C CE  . LYS A 210 ? 0.8907 1.0712 1.1118 0.0203  -0.0050 0.0168  210 LYS A CE  
1632 N NZ  . LYS A 210 ? 0.8484 1.0054 1.0631 0.0180  -0.0004 0.0171  210 LYS A NZ  
1633 N N   . GLY A 211 ? 0.5663 0.7207 0.7557 0.0271  -0.0193 0.0491  211 GLY A N   
1634 C CA  . GLY A 211 ? 0.5302 0.6919 0.7153 0.0269  -0.0235 0.0530  211 GLY A CA  
1635 C C   . GLY A 211 ? 0.5369 0.6917 0.7192 0.0329  -0.0228 0.0622  211 GLY A C   
1636 O O   . GLY A 211 ? 0.5671 0.7103 0.7512 0.0380  -0.0182 0.0657  211 GLY A O   
1637 N N   . VAL A 212 ? 0.5304 0.6911 0.7077 0.0320  -0.0262 0.0660  212 VAL A N   
1638 C CA  . VAL A 212 ? 0.5179 0.6728 0.6909 0.0367  -0.0257 0.0753  212 VAL A CA  
1639 C C   . VAL A 212 ? 0.5575 0.7344 0.7316 0.0408  -0.0309 0.0805  212 VAL A C   
1640 O O   . VAL A 212 ? 0.5663 0.7593 0.7405 0.0357  -0.0346 0.0750  212 VAL A O   
1641 C CB  . VAL A 212 ? 0.5320 0.6730 0.6958 0.0297  -0.0242 0.0752  212 VAL A CB  
1642 C CG1 . VAL A 212 ? 0.5266 0.6789 0.6880 0.0236  -0.0280 0.0707  212 VAL A CG1 
1643 C CG2 . VAL A 212 ? 0.6259 0.7580 0.7839 0.0334  -0.0223 0.0847  212 VAL A CG2 
1644 N N   . TYR A 213 ? 0.6083 0.7859 0.7828 0.0496  -0.0304 0.0914  213 TYR A N   
1645 C CA  . TYR A 213 ? 0.5536 0.7551 0.7286 0.0542  -0.0356 0.0987  213 TYR A CA  
1646 C C   . TYR A 213 ? 0.5417 0.7379 0.7065 0.0511  -0.0365 0.1039  213 TYR A C   
1647 O O   . TYR A 213 ? 0.5576 0.7376 0.7180 0.0560  -0.0328 0.1130  213 TYR A O   
1648 C CB  . TYR A 213 ? 0.5122 0.7213 0.6948 0.0677  -0.0344 0.1098  213 TYR A CB  
1649 C CG  . TYR A 213 ? 0.5807 0.8162 0.7630 0.0734  -0.0399 0.1207  213 TYR A CG  
1650 C CD1 . TYR A 213 ? 0.5553 0.8252 0.7416 0.0701  -0.0465 0.1171  213 TYR A CD1 
1651 C CD2 . TYR A 213 ? 0.5988 0.8255 0.7758 0.0812  -0.0380 0.1347  213 TYR A CD2 
1652 C CE1 . TYR A 213 ? 0.5096 0.8079 0.6948 0.0738  -0.0519 0.1270  213 TYR A CE1 
1653 C CE2 . TYR A 213 ? 0.5863 0.8393 0.7622 0.0865  -0.0433 0.1461  213 TYR A CE2 
1654 C CZ  . TYR A 213 ? 0.5448 0.8352 0.7250 0.0826  -0.0507 0.1422  213 TYR A CZ  
1655 O OH  . TYR A 213 ? 0.5536 0.8743 0.7320 0.0865  -0.0565 0.1535  213 TYR A OH  
1656 N N   . THR A 214 ? 0.5109 0.7191 0.6713 0.0426  -0.0402 0.0977  214 THR A N   
1657 C CA  . THR A 214 ? 0.5447 0.7534 0.6959 0.0392  -0.0415 0.1020  214 THR A CA  
1658 C C   . THR A 214 ? 0.5720 0.8082 0.7226 0.0424  -0.0467 0.1090  214 THR A C   
1659 O O   . THR A 214 ? 0.5575 0.8170 0.7132 0.0411  -0.0501 0.1046  214 THR A O   
1660 C CB  . THR A 214 ? 0.6061 0.8125 0.7530 0.0286  -0.0412 0.0915  214 THR A CB  
1661 O OG1 . THR A 214 ? 0.5864 0.8133 0.7356 0.0239  -0.0438 0.0836  214 THR A OG1 
1662 C CG2 . THR A 214 ? 0.5535 0.7401 0.7025 0.0256  -0.0371 0.0850  214 THR A CG2 
1663 N N   . THR A 215 ? 0.6494 0.8841 0.7930 0.0457  -0.0470 0.1201  215 THR A N   
1664 C CA  . THR A 215 ? 0.7022 0.9649 0.8448 0.0499  -0.0521 0.1297  215 THR A CA  
1665 C C   . THR A 215 ? 0.7299 0.9959 0.8609 0.0443  -0.0534 0.1334  215 THR A C   
1666 O O   . THR A 215 ? 0.6656 0.9090 0.7899 0.0449  -0.0495 0.1387  215 THR A O   
1667 C CB  . THR A 215 ? 0.6639 0.9260 0.8118 0.0650  -0.0508 0.1453  215 THR A CB  
1668 O OG1 . THR A 215 ? 0.6620 0.9517 0.8070 0.0697  -0.0559 0.1578  215 THR A OG1 
1669 C CG2 . THR A 215 ? 0.6241 0.8494 0.7672 0.0695  -0.0431 0.1518  215 THR A CG2 
1670 N N   . HIS A 216 ? 0.7998 1.0943 0.9279 0.0374  -0.0581 0.1294  216 HIS A N   
1671 C CA  . HIS A 216 ? 0.7597 1.0675 0.8775 0.0343  -0.0606 0.1366  216 HIS A CA  
1672 C C   . HIS A 216 ? 0.7608 1.0866 0.8803 0.0465  -0.0641 0.1548  216 HIS A C   
1673 O O   . HIS A 216 ? 0.8552 1.2112 0.9811 0.0490  -0.0688 0.1562  216 HIS A O   
1674 C CB  . HIS A 216 ? 0.7880 1.1198 0.9014 0.0210  -0.0629 0.1242  216 HIS A CB  
1675 C CG  . HIS A 216 ? 0.9069 1.2545 1.0087 0.0158  -0.0651 0.1299  216 HIS A CG  
1676 N ND1 . HIS A 216 ? 0.8950 1.2458 0.9891 0.0028  -0.0630 0.1180  216 HIS A ND1 
1677 C CD2 . HIS A 216 ? 0.9166 1.2784 1.0131 0.0221  -0.0686 0.1464  216 HIS A CD2 
1678 C CE1 . HIS A 216 ? 0.8610 1.2275 0.9450 0.0000  -0.0654 0.1259  216 HIS A CE1 
1679 N NE2 . HIS A 216 ? 0.9251 1.2990 1.0101 0.0115  -0.0692 0.1437  216 HIS A NE2 
1680 N N   . LEU A 217 ? 0.8040 1.1117 0.9178 0.0542  -0.0611 0.1691  217 LEU A N   
1681 C CA  . LEU A 217 ? 0.8160 1.1335 0.9325 0.0694  -0.0621 0.1890  217 LEU A CA  
1682 C C   . LEU A 217 ? 0.8265 1.1898 0.9412 0.0686  -0.0703 0.1961  217 LEU A C   
1683 O O   . LEU A 217 ? 0.7614 1.1426 0.8679 0.0552  -0.0737 0.1877  217 LEU A O   
1684 C CB  . LEU A 217 ? 0.7694 1.0569 0.8769 0.0753  -0.0559 0.2026  217 LEU A CB  
1685 C CG  . LEU A 217 ? 0.7686 1.0121 0.8771 0.0766  -0.0466 0.1981  217 LEU A CG  
1686 C CD1 . LEU A 217 ? 0.8019 1.0174 0.8985 0.0788  -0.0396 0.2099  217 LEU A CD1 
1687 C CD2 . LEU A 217 ? 0.7550 0.9922 0.8764 0.0892  -0.0435 0.2013  217 LEU A CD2 
1688 N N   . ARG A 218 ? 0.7335 1.1177 0.8563 0.0831  -0.0728 0.2117  218 ARG A N   
1689 C CA  . ARG A 218 ? 0.7226 1.1564 0.8445 0.0830  -0.0812 0.2206  218 ARG A CA  
1690 C C   . ARG A 218 ? 0.7567 1.1969 0.8637 0.0803  -0.0828 0.2323  218 ARG A C   
1691 O O   . ARG A 218 ? 0.8454 1.3267 0.9470 0.0727  -0.0899 0.2337  218 ARG A O   
1692 C CB  . ARG A 218 ? 0.7381 1.1933 0.8731 0.1019  -0.0829 0.2378  218 ARG A CB  
1693 C CG  . ARG A 218 ? 0.7174 1.2332 0.8556 0.0999  -0.0926 0.2428  218 ARG A CG  
1694 C CD  . ARG A 218 ? 0.6930 1.2318 0.8475 0.1192  -0.0939 0.2583  218 ARG A CD  
1695 N NE  . ARG A 218 ? 0.7370 1.2630 0.9045 0.1194  -0.0905 0.2438  218 ARG A NE  
1696 C CZ  . ARG A 218 ? 0.7500 1.3098 0.9251 0.1097  -0.0954 0.2301  218 ARG A CZ  
1697 N NH1 . ARG A 218 ? 0.6664 1.2761 0.8373 0.0979  -0.1036 0.2277  218 ARG A NH1 
1698 N NH2 . ARG A 218 ? 0.7373 1.2806 0.9233 0.1105  -0.0913 0.2180  218 ARG A NH2 
1699 N N   . SER A 219 ? 0.7501 1.1512 0.8495 0.0848  -0.0760 0.2401  219 SER A N   
1700 C CA  . SER A 219 ? 0.8598 1.2612 0.9437 0.0802  -0.0763 0.2491  219 SER A CA  
1701 C C   . SER A 219 ? 0.9112 1.2623 0.9877 0.0776  -0.0671 0.2459  219 SER A C   
1702 O O   . SER A 219 ? 0.8600 1.1780 0.9410 0.0888  -0.0597 0.2524  219 SER A O   
1703 C CB  . SER A 219 ? 0.8680 1.2913 0.9502 0.0958  -0.0788 0.2765  219 SER A CB  
1704 O OG  . SER A 219 ? 0.8384 1.2625 0.9043 0.0901  -0.0790 0.2853  219 SER A OG  
1705 N N   . GLU A 220 ? 0.9244 1.2710 0.9895 0.0622  -0.0668 0.2351  220 GLU A N   
1706 C CA  . GLU A 220 ? 0.9387 1.2445 0.9955 0.0572  -0.0587 0.2317  220 GLU A CA  
1707 C C   . GLU A 220 ? 0.9648 1.2692 1.0064 0.0566  -0.0573 0.2468  220 GLU A C   
1708 O O   . GLU A 220 ? 0.9682 1.2576 0.9997 0.0450  -0.0538 0.2397  220 GLU A O   
1709 C CB  . GLU A 220 ? 0.9212 1.2207 0.9779 0.0410  -0.0580 0.2083  220 GLU A CB  
1710 C CG  . GLU A 220 ? 0.8988 1.1862 0.9686 0.0418  -0.0565 0.1944  220 GLU A CG  
1711 C CD  . GLU A 220 ? 0.9808 1.2486 1.0495 0.0297  -0.0525 0.1768  220 GLU A CD  
1712 O OE1 . GLU A 220 ? 0.9064 1.1896 0.9711 0.0183  -0.0544 0.1658  220 GLU A OE1 
1713 O OE2 . GLU A 220 ? 1.0191 1.2570 1.0908 0.0316  -0.0468 0.1741  220 GLU A OE2 
1714 N N   . PHE A 221 ? 0.9656 1.2872 1.0056 0.0696  -0.0597 0.2686  221 PHE A N   
1715 C CA  . PHE A 221 ? 1.0299 1.3514 1.0547 0.0704  -0.0582 0.2858  221 PHE A CA  
1716 C C   . PHE A 221 ? 1.0710 1.3710 1.0958 0.0902  -0.0516 0.3105  221 PHE A C   
1717 O O   . PHE A 221 ? 1.1302 1.3874 1.1571 0.0951  -0.0415 0.3098  221 PHE A O   
1718 C CB  . PHE A 221 ? 1.0044 1.3766 1.0235 0.0644  -0.0683 0.2899  221 PHE A CB  
1719 C CG  . PHE A 221 ? 1.0075 1.3957 1.0228 0.0437  -0.0718 0.2663  221 PHE A CG  
1720 C CD1 . PHE A 221 ? 0.9980 1.4060 1.0241 0.0375  -0.0761 0.2483  221 PHE A CD1 
1721 C CD2 . PHE A 221 ? 1.0157 1.3975 1.0165 0.0306  -0.0693 0.2621  221 PHE A CD2 
1722 C CE1 . PHE A 221 ? 0.9966 1.4152 1.0189 0.0194  -0.0769 0.2270  221 PHE A CE1 
1723 C CE2 . PHE A 221 ? 1.0268 1.4216 1.0248 0.0129  -0.0706 0.2406  221 PHE A CE2 
1724 C CZ  . PHE A 221 ? 1.0026 1.4146 1.0113 0.0077  -0.0739 0.2232  221 PHE A CZ  
1725 N N   A GLU A 222 ? 1.0250 1.3551 1.0473 0.1014  -0.0563 0.3329  222 GLU A N   
1726 N N   B GLU A 222 ? 1.0250 1.3550 1.0472 0.1014  -0.0562 0.3329  222 GLU A N   
1727 C CA  A GLU A 222 ? 1.0261 1.3358 1.0485 0.1226  -0.0486 0.3591  222 GLU A CA  
1728 C CA  B GLU A 222 ? 1.0263 1.3356 1.0486 0.1226  -0.0485 0.3591  222 GLU A CA  
1729 C C   A GLU A 222 ? 1.0046 1.3030 1.0450 0.1385  -0.0447 0.3603  222 GLU A C   
1730 C C   B GLU A 222 ? 1.0048 1.3030 1.0452 0.1384  -0.0447 0.3601  222 GLU A C   
1731 O O   A GLU A 222 ? 1.0313 1.2833 1.0717 0.1474  -0.0320 0.3656  222 GLU A O   
1732 O O   B GLU A 222 ? 1.0342 1.2857 1.0747 0.1471  -0.0320 0.3650  222 GLU A O   
1733 C CB  A GLU A 222 ? 1.0161 1.3657 1.0321 0.1318  -0.0552 0.3845  222 GLU A CB  
1734 C CB  B GLU A 222 ? 1.0162 1.3652 1.0321 0.1319  -0.0550 0.3845  222 GLU A CB  
1735 C CG  A GLU A 222 ? 1.0614 1.4115 1.0569 0.1194  -0.0552 0.3891  222 GLU A CG  
1736 C CG  B GLU A 222 ? 1.0442 1.3675 1.0557 0.1532  -0.0450 0.4148  222 GLU A CG  
1737 C CD  A GLU A 222 ? 1.0537 1.4329 1.0442 0.0958  -0.0640 0.3656  222 GLU A CD  
1738 C CD  B GLU A 222 ? 1.0251 1.3514 1.0546 0.1770  -0.0424 0.4288  222 GLU A CD  
1739 O OE1 A GLU A 222 ? 1.0294 1.4452 1.0305 0.0912  -0.0730 0.3533  222 GLU A OE1 
1740 O OE1 B GLU A 222 ? 0.9893 1.3619 1.0326 0.1797  -0.0532 0.4254  222 GLU A OE1 
1741 O OE2 A GLU A 222 ? 1.0588 1.4232 1.0346 0.0814  -0.0608 0.3591  222 GLU A OE2 
1742 O OE2 B GLU A 222 ? 1.0373 1.3191 1.0669 0.1924  -0.0284 0.4424  222 GLU A OE2 
1743 N N   . PRO A 223 ? 1.0517 1.3897 1.1069 0.1415  -0.0541 0.3548  223 PRO A N   
1744 C CA  . PRO A 223 ? 1.0078 1.3344 1.0802 0.1570  -0.0495 0.3563  223 PRO A CA  
1745 C C   . PRO A 223 ? 0.9960 1.2938 1.0747 0.1455  -0.0456 0.3296  223 PRO A C   
1746 O O   . PRO A 223 ? 0.9773 1.2900 1.0708 0.1483  -0.0489 0.3203  223 PRO A O   
1747 C CB  . PRO A 223 ? 0.9563 1.3437 1.0409 0.1636  -0.0617 0.3626  223 PRO A CB  
1748 C CG  . PRO A 223 ? 0.9144 1.3436 0.9869 0.1479  -0.0726 0.3604  223 PRO A CG  
1749 C CD  . PRO A 223 ? 0.9671 1.3614 1.0240 0.1304  -0.0678 0.3464  223 PRO A CD  
1750 N N   . ILE A 224 ? 0.9680 1.2265 1.0356 0.1325  -0.0386 0.3177  224 ILE A N   
1751 C CA  . ILE A 224 ? 0.9395 1.1738 1.0123 0.1211  -0.0354 0.2936  224 ILE A CA  
1752 C C   . ILE A 224 ? 0.9215 1.1192 1.0026 0.1337  -0.0239 0.2966  224 ILE A C   
1753 O O   . ILE A 224 ? 0.9456 1.1384 1.0375 0.1310  -0.0237 0.2812  224 ILE A O   
1754 C CB  . ILE A 224 ? 0.9532 1.1647 1.0122 0.1023  -0.0324 0.2800  224 ILE A CB  
1755 C CG1 . ILE A 224 ? 0.8874 1.0823 0.9527 0.0907  -0.0308 0.2560  224 ILE A CG1 
1756 C CG2 . ILE A 224 ? 0.9688 1.1406 1.0146 0.1057  -0.0205 0.2934  224 ILE A CG2 
1757 C CD1 . ILE A 224 ? 0.9008 1.0788 0.9551 0.0730  -0.0282 0.2426  224 ILE A CD1 
1758 N N   . LEU A 225 ? 0.9305 1.1004 1.0061 0.1473  -0.0132 0.3165  225 LEU A N   
1759 C CA  . LEU A 225 ? 0.9356 1.0715 1.0193 0.1609  -0.0005 0.3207  225 LEU A CA  
1760 C C   . LEU A 225 ? 0.9809 1.1489 1.0834 0.1772  -0.0058 0.3270  225 LEU A C   
1761 O O   . LEU A 225 ? 0.9700 1.1201 1.0833 0.1829  0.0010  0.3203  225 LEU A O   
1762 C CB  . LEU A 225 ? 0.8910 0.9894 0.9637 0.1728  0.0140  0.3420  225 LEU A CB  
1763 C CG  . LEU A 225 ? 0.9259 0.9839 0.9797 0.1565  0.0233  0.3352  225 LEU A CG  
1764 C CD1 . LEU A 225 ? 0.9182 0.9407 0.9607 0.1694  0.0384  0.3584  225 LEU A CD1 
1765 C CD2 . LEU A 225 ? 0.9141 0.9400 0.9689 0.1422  0.0305  0.3114  225 LEU A CD2 
1766 N N   . GLU A 226 ? 1.0348 1.2525 1.1412 0.1838  -0.0177 0.3396  226 GLU A N   
1767 C CA  . GLU A 226 ? 0.9820 1.2394 1.1067 0.1959  -0.0247 0.3432  226 GLU A CA  
1768 C C   . GLU A 226 ? 0.9690 1.2396 1.1021 0.1804  -0.0317 0.3162  226 GLU A C   
1769 O O   . GLU A 226 ? 0.9654 1.2354 1.1128 0.1876  -0.0291 0.3109  226 GLU A O   
1770 C CB  . GLU A 226 ? 1.0641 1.3769 1.1890 0.2024  -0.0367 0.3612  226 GLU A CB  
1771 C CG  . GLU A 226 ? 1.2913 1.6597 1.4300 0.1989  -0.0499 0.3521  226 GLU A CG  
1772 C CD  . GLU A 226 ? 1.3446 1.7715 1.4838 0.2057  -0.0610 0.3713  226 GLU A CD  
1773 O OE1 . GLU A 226 ? 1.2696 1.6992 1.3945 0.2045  -0.0622 0.3848  226 GLU A OE1 
1774 O OE2 . GLU A 226 ? 1.3252 1.7979 1.4791 0.2115  -0.0685 0.3731  226 GLU A OE2 
1775 N N   . ALA A 227 ? 0.9651 1.2467 1.0891 0.1595  -0.0395 0.2992  227 ALA A N   
1776 C CA  . ALA A 227 ? 0.9718 1.2635 1.1023 0.1448  -0.0450 0.2744  227 ALA A CA  
1777 C C   . ALA A 227 ? 0.9136 1.1597 1.0460 0.1408  -0.0351 0.2601  227 ALA A C   
1778 O O   . ALA A 227 ? 0.9049 1.1557 1.0478 0.1375  -0.0365 0.2458  227 ALA A O   
1779 C CB  . ALA A 227 ? 0.8848 1.1946 1.0045 0.1247  -0.0532 0.2610  227 ALA A CB  
1780 N N   . LEU A 228 ? 0.8228 1.0260 0.9443 0.1396  -0.0247 0.2633  228 LEU A N   
1781 C CA  . LEU A 228 ? 0.8817 1.0429 1.0039 0.1354  -0.0141 0.2510  228 LEU A CA  
1782 C C   . LEU A 228 ? 0.9465 1.0966 1.0814 0.1527  -0.0061 0.2585  228 LEU A C   
1783 O O   . LEU A 228 ? 0.9162 1.0547 1.0587 0.1491  -0.0029 0.2443  228 LEU A O   
1784 C CB  . LEU A 228 ? 0.8384 0.9591 0.9447 0.1285  -0.0041 0.2529  228 LEU A CB  
1785 C CG  . LEU A 228 ? 0.7867 0.9056 0.8825 0.1075  -0.0083 0.2368  228 LEU A CG  
1786 C CD1 . LEU A 228 ? 0.8067 0.8978 0.8861 0.1027  -0.0002 0.2445  228 LEU A CD1 
1787 C CD2 . LEU A 228 ? 0.8070 0.9105 0.9074 0.0964  -0.0059 0.2163  228 LEU A CD2 
1788 N N   . ASP A 229 ? 1.0367 1.1911 1.1743 0.1721  -0.0021 0.2815  229 ASP A N   
1789 C CA  . ASP A 229 ? 1.0158 1.1632 1.1674 0.1910  0.0062  0.2902  229 ASP A CA  
1790 C C   . ASP A 229 ? 0.9245 1.1124 1.0929 0.1921  -0.0039 0.2813  229 ASP A C   
1791 O O   . ASP A 229 ? 0.9330 1.1095 1.1125 0.1978  0.0026  0.2752  229 ASP A O   
1792 C CB  . ASP A 229 ? 0.9976 1.1480 1.1502 0.2135  0.0116  0.3191  229 ASP A CB  
1793 C CG  . ASP A 229 ? 1.0449 1.1968 1.2150 0.2356  0.0193  0.3298  229 ASP A CG  
1794 O OD1 . ASP A 229 ? 1.1127 1.2218 1.2842 0.2379  0.0342  0.3233  229 ASP A OD1 
1795 O OD2 . ASP A 229 ? 1.1074 1.3052 1.2899 0.2499  0.0109  0.3439  229 ASP A OD2 
1796 N N   . GLU A 230 ? 0.8889 1.1245 1.0587 0.1859  -0.0188 0.2800  230 GLU A N   
1797 C CA  . GLU A 230 ? 0.8571 1.1287 1.0396 0.1807  -0.0280 0.2665  230 GLU A CA  
1798 C C   . GLU A 230 ? 0.8461 1.0906 1.0275 0.1648  -0.0250 0.2421  230 GLU A C   
1799 O O   . GLU A 230 ? 0.8844 1.1128 1.0753 0.1701  -0.0179 0.2368  230 GLU A O   
1800 C CB  . GLU A 230 ? 0.8129 1.1337 0.9923 0.1702  -0.0427 0.2643  230 GLU A CB  
1801 C CG  . GLU A 230 ? 0.7938 1.1590 0.9871 0.1681  -0.0513 0.2556  230 GLU A CG  
1802 C CD  . GLU A 230 ? 0.8225 1.2362 1.0109 0.1560  -0.0641 0.2529  230 GLU A CD  
1803 O OE1 . GLU A 230 ? 0.8410 1.2537 1.0154 0.1488  -0.0667 0.2566  230 GLU A OE1 
1804 O OE2 . GLU A 230 ? 0.7690 1.2224 0.9671 0.1525  -0.0708 0.2462  230 GLU A OE2 
1805 N N   . ALA A 231 ? 0.8168 1.0560 0.9866 0.1460  -0.0295 0.2283  231 ALA A N   
1806 C CA  . ALA A 231 ? 0.7814 1.0000 0.9491 0.1302  -0.0280 0.2064  231 ALA A CA  
1807 C C   . ALA A 231 ? 0.7601 0.9415 0.9319 0.1343  -0.0162 0.2020  231 ALA A C   
1808 O O   . ALA A 231 ? 0.7773 0.9573 0.9553 0.1276  -0.0163 0.1870  231 ALA A O   
1809 C CB  . ALA A 231 ? 0.7817 0.9843 0.9340 0.1151  -0.0287 0.1998  231 ALA A CB  
1810 N N   . PHE A 232 ? 0.7917 0.9422 0.9594 0.1448  -0.0049 0.2147  232 PHE A N   
1811 C CA  . PHE A 232 ? 0.8236 0.9365 0.9935 0.1475  0.0085  0.2100  232 PHE A CA  
1812 C C   . PHE A 232 ? 0.9004 1.0264 1.0872 0.1633  0.0113  0.2146  232 PHE A C   
1813 O O   . PHE A 232 ? 0.8223 0.9283 1.0139 0.1616  0.0192  0.2042  232 PHE A O   
1814 C CB  . PHE A 232 ? 0.8412 0.9132 0.9995 0.1520  0.0222  0.2209  232 PHE A CB  
1815 C CG  . PHE A 232 ? 0.8519 0.9087 0.9935 0.1354  0.0212  0.2152  232 PHE A CG  
1816 C CD1 . PHE A 232 ? 0.8478 0.9188 0.9865 0.1177  0.0116  0.1985  232 PHE A CD1 
1817 C CD2 . PHE A 232 ? 0.8703 0.8986 0.9993 0.1378  0.0309  0.2271  232 PHE A CD2 
1818 C CE1 . PHE A 232 ? 0.7866 0.8468 0.9116 0.1035  0.0110  0.1938  232 PHE A CE1 
1819 C CE2 . PHE A 232 ? 0.8786 0.8954 0.9927 0.1218  0.0302  0.2215  232 PHE A CE2 
1820 C CZ  . PHE A 232 ? 0.8137 0.8479 0.9265 0.1050  0.0200  0.2048  232 PHE A CZ  
1821 N N   . ARG A 233 ? 0.8261 0.9882 1.0223 0.1781  0.0050  0.2301  233 ARG A N   
1822 C CA  . ARG A 233 ? 0.7816 0.9614 0.9956 0.1940  0.0075  0.2357  233 ARG A CA  
1823 C C   . ARG A 233 ? 0.7452 0.9524 0.9683 0.1833  -0.0013 0.2176  233 ARG A C   
1824 O O   . ARG A 233 ? 0.8788 1.0825 1.1134 0.1886  0.0044  0.2124  233 ARG A O   
1825 C CB  . ARG A 233 ? 0.8114 1.0267 1.0330 0.2133  0.0030  0.2593  233 ARG A CB  
1826 C CG  . ARG A 233 ? 0.9003 1.0856 1.1194 0.2326  0.0168  0.2811  233 ARG A CG  
1827 C CD  . ARG A 233 ? 0.9547 1.1751 1.1734 0.2451  0.0090  0.3044  233 ARG A CD  
1828 N NE  . ARG A 233 ? 1.0003 1.2822 1.2331 0.2487  -0.0050 0.3067  233 ARG A NE  
1829 C CZ  . ARG A 233 ? 1.0055 1.3327 1.2360 0.2480  -0.0180 0.3170  233 ARG A CZ  
1830 N NH1 . ARG A 233 ? 1.0057 1.3241 1.2206 0.2446  -0.0194 0.3266  233 ARG A NH1 
1831 N NH2 . ARG A 233 ? 0.9120 1.2959 1.1554 0.2492  -0.0295 0.3170  233 ARG A NH2 
1832 N N   . ILE A 234 ? 0.6980 0.9316 0.9160 0.1679  -0.0141 0.2078  234 ILE A N   
1833 C CA  . ILE A 234 ? 0.7541 1.0096 0.9788 0.1564  -0.0209 0.1903  234 ILE A CA  
1834 C C   . ILE A 234 ? 0.6772 0.8959 0.8981 0.1449  -0.0138 0.1730  234 ILE A C   
1835 O O   . ILE A 234 ? 0.6731 0.8966 0.9028 0.1427  -0.0128 0.1624  234 ILE A O   
1836 C CB  . ILE A 234 ? 0.7216 1.0092 0.9400 0.1420  -0.0337 0.1835  234 ILE A CB  
1837 C CG1 . ILE A 234 ? 0.6723 0.9951 0.8906 0.1511  -0.0405 0.2016  234 ILE A CG1 
1838 C CG2 . ILE A 234 ? 0.6597 0.9708 0.8858 0.1316  -0.0389 0.1668  234 ILE A CG2 
1839 C CD1 . ILE A 234 ? 0.6831 1.0109 0.8863 0.1391  -0.0468 0.2011  234 ILE A CD1 
1840 N N   . GLY A 235 ? 0.7084 0.8921 0.9156 0.1367  -0.0088 0.1702  235 GLY A N   
1841 C CA  . GLY A 235 ? 0.8111 0.9614 1.0140 0.1264  -0.0012 0.1560  235 GLY A CA  
1842 C C   . GLY A 235 ? 0.8073 0.9343 1.0171 0.1376  0.0118  0.1590  235 GLY A C   
1843 O O   . GLY A 235 ? 0.7456 0.8608 0.9582 0.1313  0.0162  0.1463  235 GLY A O   
1844 N N   . ARG A 236 ? 0.7356 0.8556 0.9482 0.1548  0.0189  0.1764  236 ARG A N   
1845 C CA  . ARG A 236 ? 0.7253 0.8220 0.9455 0.1677  0.0335  0.1804  236 ARG A CA  
1846 C C   . ARG A 236 ? 0.6879 0.8161 0.9266 0.1785  0.0308  0.1808  236 ARG A C   
1847 O O   . ARG A 236 ? 0.6578 0.7688 0.9040 0.1849  0.0423  0.1778  236 ARG A O   
1848 C CB  . ARG A 236 ? 0.7195 0.7959 0.9365 0.1840  0.0439  0.2004  236 ARG A CB  
1849 C CG  . ARG A 236 ? 0.8250 0.8471 1.0308 0.1802  0.0621  0.1968  236 ARG A CG  
1850 C CD  . ARG A 236 ? 0.8490 0.8476 1.0506 0.1968  0.0741  0.2175  236 ARG A CD  
1851 N NE  . ARG A 236 ? 0.8830 0.8939 1.0746 0.1948  0.0648  0.2281  236 ARG A NE  
1852 C CZ  . ARG A 236 ? 0.8696 0.9085 1.0671 0.2115  0.0587  0.2485  236 ARG A CZ  
1853 N NH1 . ARG A 236 ? 0.8352 0.8950 1.0495 0.2328  0.0606  0.2618  236 ARG A NH1 
1854 N NH2 . ARG A 236 ? 0.8997 0.9479 1.0859 0.2066  0.0507  0.2561  236 ARG A NH2 
1855 N N   . HIS A 237 ? 0.6882 0.8628 0.9342 0.1792  0.0165  0.1834  237 HIS A N   
1856 C CA  . HIS A 237 ? 0.6301 0.8395 0.8938 0.1880  0.0135  0.1835  237 HIS A CA  
1857 C C   . HIS A 237 ? 0.5879 0.7945 0.8534 0.1729  0.0129  0.1623  237 HIS A C   
1858 O O   . HIS A 237 ? 0.6056 0.8123 0.8826 0.1795  0.0197  0.1590  237 HIS A O   
1859 C CB  . HIS A 237 ? 0.6138 0.8758 0.8828 0.1904  -0.0010 0.1917  237 HIS A CB  
1860 C CG  . HIS A 237 ? 0.5783 0.8816 0.8663 0.2018  -0.0037 0.1958  237 HIS A CG  
1861 N ND1 . HIS A 237 ? 0.5745 0.9096 0.8681 0.1894  -0.0122 0.1813  237 HIS A ND1 
1862 C CD2 . HIS A 237 ? 0.5400 0.8591 0.8430 0.2245  0.0018  0.2132  237 HIS A CD2 
1863 C CE1 . HIS A 237 ? 0.5204 0.8911 0.8316 0.2027  -0.0125 0.1886  237 HIS A CE1 
1864 N NE2 . HIS A 237 ? 0.5038 0.8670 0.8219 0.2250  -0.0044 0.2085  237 HIS A NE2 
1865 N N   . GLY A 238 ? 0.5852 0.7894 0.8394 0.1533  0.0053  0.1485  238 GLY A N   
1866 C CA  . GLY A 238 ? 0.7011 0.9009 0.9549 0.1387  0.0048  0.1299  238 GLY A CA  
1867 C C   . GLY A 238 ? 0.6814 0.8387 0.9236 0.1277  0.0132  0.1197  238 GLY A C   
1868 O O   . GLY A 238 ? 0.7042 0.8578 0.9447 0.1150  0.0125  0.1052  238 GLY A O   
1869 N N   . ASN A 239 ? 0.6573 0.7836 0.8909 0.1314  0.0216  0.1271  239 ASN A N   
1870 C CA  . ASN A 239 ? 0.6934 0.7817 0.9141 0.1187  0.0298  0.1176  239 ASN A CA  
1871 C C   . ASN A 239 ? 0.6729 0.7668 0.8842 0.1001  0.0203  0.1057  239 ASN A C   
1872 O O   . ASN A 239 ? 0.7097 0.7937 0.9176 0.0880  0.0222  0.0929  239 ASN A O   
1873 C CB  . ASN A 239 ? 0.7324 0.8010 0.9577 0.1190  0.0420  0.1094  239 ASN A CB  
1874 C CG  . ASN A 239 ? 0.8089 0.8499 1.0359 0.1333  0.0578  0.1195  239 ASN A CG  
1875 O OD1 . ASN A 239 ? 0.7803 0.8344 1.0175 0.1520  0.0589  0.1344  239 ASN A OD1 
1876 N ND2 . ASN A 239 ? 1.0497 1.0528 1.2663 0.1244  0.0710  0.1117  239 ASN A ND2 
1877 N N   . VAL A 240 ? 0.6579 0.7686 0.8650 0.0984  0.0106  0.1108  240 VAL A N   
1878 C CA  . VAL A 240 ? 0.6463 0.7643 0.8457 0.0832  0.0022  0.1014  240 VAL A CA  
1879 C C   . VAL A 240 ? 0.6720 0.7752 0.8587 0.0783  0.0024  0.1060  240 VAL A C   
1880 O O   . VAL A 240 ? 0.6607 0.7584 0.8455 0.0877  0.0053  0.1183  240 VAL A O   
1881 C CB  . VAL A 240 ? 0.6275 0.7818 0.8334 0.0830  -0.0089 0.1001  240 VAL A CB  
1882 C CG1 . VAL A 240 ? 0.6047 0.7743 0.8226 0.0862  -0.0084 0.0947  240 VAL A CG1 
1883 C CG2 . VAL A 240 ? 0.6230 0.7967 0.8302 0.0928  -0.0136 0.1137  240 VAL A CG2 
1884 N N   . PRO A 241 ? 0.6668 0.7638 0.8449 0.0644  -0.0001 0.0973  241 PRO A N   
1885 C CA  . PRO A 241 ? 0.6293 0.7151 0.7959 0.0589  0.0001  0.1011  241 PRO A CA  
1886 C C   . PRO A 241 ? 0.6536 0.7615 0.8197 0.0626  -0.0083 0.1086  241 PRO A C   
1887 O O   . PRO A 241 ? 0.6395 0.7733 0.8118 0.0633  -0.0160 0.1061  241 PRO A O   
1888 C CB  . PRO A 241 ? 0.6303 0.7119 0.7910 0.0440  -0.0013 0.0897  241 PRO A CB  
1889 C CG  . PRO A 241 ? 0.6621 0.7424 0.8289 0.0421  0.0012  0.0810  241 PRO A CG  
1890 C CD  . PRO A 241 ? 0.6392 0.7377 0.8176 0.0534  -0.0017 0.0845  241 PRO A CD  
1891 N N   . VAL A 242 ? 0.6377 0.7351 0.7953 0.0637  -0.0061 0.1171  242 VAL A N   
1892 C CA  . VAL A 242 ? 0.6170 0.7337 0.7720 0.0665  -0.0130 0.1252  242 VAL A CA  
1893 C C   . VAL A 242 ? 0.6323 0.7409 0.7758 0.0551  -0.0137 0.1224  242 VAL A C   
1894 O O   . VAL A 242 ? 0.6557 0.7396 0.7915 0.0501  -0.0063 0.1220  242 VAL A O   
1895 C CB  . VAL A 242 ? 0.6802 0.7952 0.8362 0.0809  -0.0096 0.1415  242 VAL A CB  
1896 C CG1 . VAL A 242 ? 0.6138 0.7536 0.7665 0.0827  -0.0178 0.1500  242 VAL A CG1 
1897 C CG2 . VAL A 242 ? 0.6996 0.8229 0.8685 0.0935  -0.0076 0.1450  242 VAL A CG2 
1898 N N   . VAL A 243 ? 0.6725 0.8028 0.8148 0.0504  -0.0216 0.1198  243 VAL A N   
1899 C CA  . VAL A 243 ? 0.6774 0.8051 0.8102 0.0410  -0.0226 0.1180  243 VAL A CA  
1900 C C   . VAL A 243 ? 0.6254 0.7727 0.7549 0.0439  -0.0279 0.1259  243 VAL A C   
1901 O O   . VAL A 243 ? 0.5966 0.7685 0.7306 0.0440  -0.0342 0.1229  243 VAL A O   
1902 C CB  . VAL A 243 ? 0.6240 0.7578 0.7581 0.0309  -0.0252 0.1054  243 VAL A CB  
1903 C CG1 . VAL A 243 ? 0.6376 0.7743 0.7639 0.0232  -0.0264 0.1046  243 VAL A CG1 
1904 C CG2 . VAL A 243 ? 0.6502 0.7665 0.7856 0.0266  -0.0201 0.0988  243 VAL A CG2 
1905 N N   . VAL A 244 ? 0.6460 0.7826 0.7666 0.0450  -0.0249 0.1355  244 VAL A N   
1906 C CA  . VAL A 244 ? 0.6370 0.7919 0.7525 0.0467  -0.0296 0.1439  244 VAL A CA  
1907 C C   . VAL A 244 ? 0.6501 0.8151 0.7607 0.0349  -0.0330 0.1347  244 VAL A C   
1908 O O   . VAL A 244 ? 0.6882 0.8385 0.7923 0.0273  -0.0292 0.1318  244 VAL A O   
1909 C CB  . VAL A 244 ? 0.6486 0.7863 0.7554 0.0522  -0.0240 0.1583  244 VAL A CB  
1910 C CG1 . VAL A 244 ? 0.6648 0.8230 0.7648 0.0525  -0.0292 0.1671  244 VAL A CG1 
1911 C CG2 . VAL A 244 ? 0.6790 0.8061 0.7918 0.0662  -0.0190 0.1684  244 VAL A CG2 
1912 N N   . SER A 245 ? 0.6415 0.8323 0.7553 0.0328  -0.0391 0.1297  245 SER A N   
1913 C CA  . SER A 245 ? 0.6702 0.8701 0.7803 0.0226  -0.0406 0.1203  245 SER A CA  
1914 C C   . SER A 245 ? 0.6722 0.8757 0.7716 0.0193  -0.0407 0.1272  245 SER A C   
1915 O O   . SER A 245 ? 0.7303 0.9409 0.8255 0.0250  -0.0424 0.1392  245 SER A O   
1916 C CB  . SER A 245 ? 0.6839 0.9077 0.7990 0.0200  -0.0448 0.1120  245 SER A CB  
1917 O OG  . SER A 245 ? 0.7265 0.9464 0.8507 0.0216  -0.0441 0.1047  245 SER A OG  
1918 N N   . HIS A 246 ? 0.6982 0.8985 0.7934 0.0105  -0.0386 0.1201  246 HIS A N   
1919 C CA  . HIS A 246 ? 0.7735 0.9758 0.8584 0.0050  -0.0376 0.1239  246 HIS A CA  
1920 C C   . HIS A 246 ? 0.8137 1.0094 0.8908 0.0104  -0.0368 0.1391  246 HIS A C   
1921 O O   . HIS A 246 ? 0.8509 1.0632 0.9220 0.0110  -0.0400 0.1461  246 HIS A O   
1922 C CB  . HIS A 246 ? 0.7847 1.0107 0.8674 -0.0007 -0.0405 0.1178  246 HIS A CB  
1923 C CG  . HIS A 246 ? 0.7825 1.0300 0.8682 0.0028  -0.0455 0.1191  246 HIS A CG  
1924 N ND1 . HIS A 246 ? 0.8049 1.0587 0.8896 0.0111  -0.0486 0.1323  246 HIS A ND1 
1925 C CD2 . HIS A 246 ? 0.7586 1.0240 0.8479 -0.0014 -0.0471 0.1088  246 HIS A CD2 
1926 C CE1 . HIS A 246 ? 0.8799 1.1587 0.9684 0.0117  -0.0532 0.1304  246 HIS A CE1 
1927 N NE2 . HIS A 246 ? 0.8087 1.0940 0.8992 0.0030  -0.0521 0.1153  246 HIS A NE2 
1928 N N   . HIS A 247 ? 0.7404 0.9114 0.8167 0.0140  -0.0317 0.1444  247 HIS A N   
1929 C CA  . HIS A 247 ? 0.7982 0.9572 0.8670 0.0204  -0.0285 0.1597  247 HIS A CA  
1930 C C   . HIS A 247 ? 0.8499 1.0092 0.9060 0.0133  -0.0270 0.1644  247 HIS A C   
1931 O O   . HIS A 247 ? 0.7984 0.9489 0.8504 0.0033  -0.0234 0.1572  247 HIS A O   
1932 C CB  . HIS A 247 ? 0.7537 0.8816 0.8228 0.0232  -0.0205 0.1618  247 HIS A CB  
1933 C CG  . HIS A 247 ? 0.7894 0.9003 0.8515 0.0319  -0.0147 0.1782  247 HIS A CG  
1934 N ND1 . HIS A 247 ? 0.7956 0.9212 0.8599 0.0445  -0.0184 0.1916  247 HIS A ND1 
1935 C CD2 . HIS A 247 ? 0.8029 0.8833 0.8554 0.0299  -0.0047 0.1838  247 HIS A CD2 
1936 C CE1 . HIS A 247 ? 0.7831 0.8868 0.8402 0.0518  -0.0107 0.2063  247 HIS A CE1 
1937 N NE2 . HIS A 247 ? 0.7807 0.8546 0.8299 0.0425  -0.0016 0.2012  247 HIS A NE2 
1938 N N   . LYS A 248 ? 0.8714 1.0436 0.9215 0.0184  -0.0297 0.1770  248 LYS A N   
1939 C CA  . LYS A 248 ? 0.8357 1.0112 0.8728 0.0117  -0.0287 0.1823  248 LYS A CA  
1940 C C   . LYS A 248 ? 0.9080 1.0865 0.9383 0.0217  -0.0291 0.2019  248 LYS A C   
1941 O O   . LYS A 248 ? 0.8962 1.0863 0.9335 0.0333  -0.0327 0.2098  248 LYS A O   
1942 C CB  . LYS A 248 ? 0.8523 1.0556 0.8891 0.0025  -0.0342 0.1716  248 LYS A CB  
1943 C CG  . LYS A 248 ? 0.8747 1.1090 0.9145 0.0067  -0.0417 0.1743  248 LYS A CG  
1944 C CD  . LYS A 248 ? 0.8518 1.1091 0.8923 -0.0038 -0.0446 0.1596  248 LYS A CD  
1945 C CE  . LYS A 248 ? 0.8657 1.1168 0.9176 -0.0061 -0.0433 0.1438  248 LYS A CE  
1946 N NZ  . LYS A 248 ? 0.9116 1.1841 0.9652 -0.0140 -0.0447 0.1303  248 LYS A NZ  
1947 N N   . CYS A 249 ? 0.9456 1.1145 0.9623 0.0174  -0.0249 0.2106  249 CYS A N   
1948 C CA  . CYS A 249 ? 0.9214 1.0947 0.9292 0.0262  -0.0250 0.2310  249 CYS A CA  
1949 C C   . CYS A 249 ? 0.9091 1.1116 0.9080 0.0173  -0.0308 0.2307  249 CYS A C   
1950 O O   . CYS A 249 ? 0.9204 1.1144 0.9064 0.0092  -0.0267 0.2336  249 CYS A O   
1951 C CB  . CYS A 249 ? 0.9182 1.0533 0.9154 0.0286  -0.0136 0.2428  249 CYS A CB  
1952 S SG  . CYS A 249 ? 0.9218 1.0246 0.9275 0.0431  -0.0051 0.2493  249 CYS A SG  
1953 N N   . ALA A 250 ? 0.9079 1.1454 0.9131 0.0174  -0.0397 0.2259  250 ALA A N   
1954 C CA  . ALA A 250 ? 0.9319 1.1995 0.9288 0.0073  -0.0447 0.2230  250 ALA A CA  
1955 C C   . ALA A 250 ? 0.9333 1.2147 0.9188 0.0135  -0.0468 0.2447  250 ALA A C   
1956 O O   . ALA A 250 ? 0.9312 1.2090 0.9192 0.0283  -0.0468 0.2622  250 ALA A O   
1957 C CB  . ALA A 250 ? 0.8908 1.1900 0.8969 0.0034  -0.0518 0.2092  250 ALA A CB  
1958 N N   . GLY A 251 ? 0.9754 1.2735 0.9483 0.0024  -0.0481 0.2442  251 GLY A N   
1959 C CA  . GLY A 251 ? 0.9556 1.2685 0.9156 0.0064  -0.0501 0.2652  251 GLY A CA  
1960 C C   . GLY A 251 ? 0.9842 1.2630 0.9313 0.0068  -0.0411 0.2773  251 GLY A C   
1961 O O   . GLY A 251 ? 0.9835 1.2252 0.9339 0.0125  -0.0333 0.2787  251 GLY A O   
1962 N N   . ALA A 252 ? 0.9582 1.2491 0.8894 -0.0007 -0.0412 0.2853  252 ALA A N   
1963 C CA  . ALA A 252 ? 0.9730 1.2318 0.8899 -0.0030 -0.0317 0.2959  252 ALA A CA  
1964 C C   . ALA A 252 ? 1.0425 1.2756 0.9576 0.0148  -0.0261 0.3197  252 ALA A C   
1965 O O   . ALA A 252 ? 1.0525 1.2457 0.9596 0.0143  -0.0149 0.3248  252 ALA A O   
1966 C CB  . ALA A 252 ? 1.0089 1.2895 0.9087 -0.0142 -0.0334 0.3009  252 ALA A CB  
1967 N N   . LYS A 253 ? 1.0778 1.3332 1.0001 0.0304  -0.0325 0.3345  253 LYS A N   
1968 C CA  A LYS A 253 ? 1.0635 1.2947 0.9860 0.0501  -0.0259 0.3583  253 LYS A CA  
1969 C CA  B LYS A 253 ? 1.0632 1.2946 0.9858 0.0501  -0.0259 0.3584  253 LYS A CA  
1970 C C   . LYS A 253 ? 1.0574 1.2481 0.9912 0.0555  -0.0172 0.3493  253 LYS A C   
1971 O O   . LYS A 253 ? 1.0640 1.2139 0.9924 0.0636  -0.0050 0.3617  253 LYS A O   
1972 C CB  A LYS A 253 ? 1.1100 1.3813 1.0398 0.0661  -0.0354 0.3763  253 LYS A CB  
1973 C CB  B LYS A 253 ? 1.1019 1.3739 1.0318 0.0659  -0.0356 0.3760  253 LYS A CB  
1974 C CG  A LYS A 253 ? 1.1495 1.3976 1.0834 0.0897  -0.0280 0.4011  253 LYS A CG  
1975 C CG  B LYS A 253 ? 1.1455 1.3976 1.0777 0.0897  -0.0287 0.4034  253 LYS A CG  
1976 C CD  A LYS A 253 ? 1.1860 1.4791 1.1317 0.1062  -0.0382 0.4166  253 LYS A CD  
1977 C CD  B LYS A 253 ? 1.1407 1.3879 1.0934 0.1029  -0.0287 0.3984  253 LYS A CD  
1978 C CE  A LYS A 253 ? 1.2001 1.4674 1.1546 0.1313  -0.0293 0.4377  253 LYS A CE  
1979 C CE  B LYS A 253 ? 1.1835 1.4147 1.1400 0.1284  -0.0212 0.4268  253 LYS A CE  
1980 N NZ  A LYS A 253 ? 1.1721 1.3999 1.1386 0.1316  -0.0212 0.4197  253 LYS A NZ  
1981 N NZ  B LYS A 253 ? 1.1890 1.4665 1.1431 0.1408  -0.0301 0.4525  253 LYS A NZ  
1982 N N   . ASN A 254 ? 1.0754 1.2756 1.0240 0.0504  -0.0223 0.3276  254 ASN A N   
1983 C CA  . ASN A 254 ? 1.0754 1.2431 1.0354 0.0547  -0.0154 0.3179  254 ASN A CA  
1984 C C   . ASN A 254 ? 1.0304 1.1670 0.9854 0.0382  -0.0074 0.2996  254 ASN A C   
1985 O O   . ASN A 254 ? 1.0324 1.1479 0.9968 0.0377  -0.0030 0.2873  254 ASN A O   
1986 C CB  . ASN A 254 ? 1.0384 1.2329 1.0168 0.0582  -0.0247 0.3052  254 ASN A CB  
1987 C CG  . ASN A 254 ? 1.0556 1.2898 1.0396 0.0717  -0.0339 0.3212  254 ASN A CG  
1988 O OD1 . ASN A 254 ? 1.0762 1.3034 1.0653 0.0900  -0.0306 0.3396  254 ASN A OD1 
1989 N ND2 . ASN A 254 ? 1.0072 1.2847 0.9905 0.0623  -0.0447 0.3140  254 ASN A ND2 
1990 N N   . TRP A 255 ? 0.9677 1.1036 0.9083 0.0244  -0.0054 0.2976  255 TRP A N   
1991 C CA  . TRP A 255 ? 0.9522 1.0625 0.8882 0.0087  0.0025  0.2817  255 TRP A CA  
1992 C C   . TRP A 255 ? 1.0018 1.0644 0.9315 0.0123  0.0170  0.2894  255 TRP A C   
1993 O O   . TRP A 255 ? 0.9979 1.0427 0.9167 0.0212  0.0241  0.3100  255 TRP A O   
1994 C CB  . TRP A 255 ? 0.9727 1.0950 0.8945 -0.0063 0.0021  0.2793  255 TRP A CB  
1995 C CG  . TRP A 255 ? 0.9631 1.1243 0.8912 -0.0153 -0.0083 0.2635  255 TRP A CG  
1996 C CD1 . TRP A 255 ? 0.9183 1.1013 0.8622 -0.0124 -0.0164 0.2512  255 TRP A CD1 
1997 C CD2 . TRP A 255 ? 0.9564 1.1372 0.8746 -0.0293 -0.0101 0.2578  255 TRP A CD2 
1998 N NE1 . TRP A 255 ? 0.8757 1.0884 0.8196 -0.0235 -0.0221 0.2381  255 TRP A NE1 
1999 C CE2 . TRP A 255 ? 0.9003 1.1129 0.8291 -0.0337 -0.0185 0.2417  255 TRP A CE2 
2000 C CE3 . TRP A 255 ? 0.9761 1.1496 0.8769 -0.0388 -0.0044 0.2645  255 TRP A CE3 
2001 C CZ2 . TRP A 255 ? 0.8981 1.1345 0.8211 -0.0468 -0.0206 0.2318  255 TRP A CZ2 
2002 C CZ3 . TRP A 255 ? 0.9899 1.1896 0.8854 -0.0520 -0.0077 0.2547  255 TRP A CZ3 
2003 C CH2 . TRP A 255 ? 0.9444 1.1749 0.8512 -0.0556 -0.0154 0.2384  255 TRP A CH2 
2004 N N   . GLY A 256 ? 0.9657 1.0075 0.9017 0.0050  0.0225  0.2730  256 GLY A N   
2005 C CA  . GLY A 256 ? 0.9827 0.9791 0.9130 0.0058  0.0374  0.2763  256 GLY A CA  
2006 C C   . GLY A 256 ? 1.0396 1.0217 0.9811 0.0232  0.0404  0.2831  256 GLY A C   
2007 O O   . GLY A 256 ? 1.0710 1.0144 1.0095 0.0226  0.0539  0.2819  256 GLY A O   
2008 N N   . ARG A 257 ? 1.0232 1.0361 0.9773 0.0376  0.0291  0.2894  257 ARG A N   
2009 C CA  . ARG A 257 ? 1.0076 1.0109 0.9736 0.0554  0.0318  0.2968  257 ARG A CA  
2010 C C   . ARG A 257 ? 0.9888 0.9850 0.9678 0.0506  0.0321  0.2768  257 ARG A C   
2011 O O   . ARG A 257 ? 1.0106 0.9995 1.0005 0.0642  0.0346  0.2805  257 ARG A O   
2012 C CB  . ARG A 257 ? 1.0080 1.0521 0.9835 0.0710  0.0191  0.3098  257 ARG A CB  
2013 C CG  . ARG A 257 ? 1.0637 1.1099 1.0283 0.0831  0.0215  0.3366  257 ARG A CG  
2014 C CD  . ARG A 257 ? 1.0836 1.1380 1.0597 0.1073  0.0211  0.3555  257 ARG A CD  
2015 N NE  . ARG A 257 ? 1.0407 1.1472 1.0306 0.1113  0.0046  0.3521  257 ARG A NE  
2016 C CZ  . ARG A 257 ? 1.0433 1.1665 1.0486 0.1286  0.0013  0.3601  257 ARG A CZ  
2017 N NH1 . ARG A 257 ? 1.0451 1.1365 1.0554 0.1451  0.0135  0.3718  257 ARG A NH1 
2018 N NH2 . ARG A 257 ? 1.0406 1.2137 1.0565 0.1286  -0.0135 0.3555  257 ARG A NH2 
2019 N N   . THR A 258 ? 1.0060 1.0058 0.9845 0.0324  0.0299  0.2566  258 THR A N   
2020 C CA  . THR A 258 ? 0.9667 0.9561 0.9549 0.0268  0.0321  0.2392  258 THR A CA  
2021 C C   . THR A 258 ? 1.0029 0.9463 0.9849 0.0270  0.0490  0.2411  258 THR A C   
2022 O O   . THR A 258 ? 1.0028 0.9357 0.9936 0.0274  0.0521  0.2312  258 THR A O   
2023 C CB  . THR A 258 ? 0.9193 0.9223 0.9073 0.0079  0.0276  0.2199  258 THR A CB  
2024 O OG1 . THR A 258 ? 1.0027 0.9961 0.9749 -0.0043 0.0333  0.2223  258 THR A OG1 
2025 C CG2 . THR A 258 ? 0.8794 0.9245 0.8781 0.0088  0.0126  0.2131  258 THR A CG2 
2026 N N   . LYS A 259 ? 1.0092 0.9239 0.9752 0.0256  0.0611  0.2533  259 LYS A N   
2027 C CA  . LYS A 259 ? 1.0599 0.9270 1.0185 0.0265  0.0798  0.2562  259 LYS A CA  
2028 C C   . LYS A 259 ? 1.0865 0.9444 1.0556 0.0494  0.0834  0.2694  259 LYS A C   
2029 O O   . LYS A 259 ? 1.1389 0.9621 1.1080 0.0512  0.0975  0.2664  259 LYS A O   
2030 C CB  . LYS A 259 ? 1.0915 0.9286 1.0294 0.0202  0.0930  0.2673  259 LYS A CB  
2031 C CG  . LYS A 259 ? 1.1032 0.9334 1.0290 -0.0057 0.0974  0.2511  259 LYS A CG  
2032 C CD  . LYS A 259 ? 1.1200 0.9315 1.0258 -0.0120 0.1066  0.2632  259 LYS A CD  
2033 C CE  . LYS A 259 ? 1.2286 1.0787 1.1346 -0.0070 0.0916  0.2731  259 LYS A CE  
2034 N NZ  . LYS A 259 ? 1.1605 0.9962 1.0464 -0.0155 0.0996  0.2835  259 LYS A NZ  
2035 N N   . GLU A 260 ? 1.0883 0.9785 1.0664 0.0664  0.0714  0.2835  260 GLU A N   
2036 C CA  . GLU A 260 ? 1.0924 0.9826 1.0830 0.0894  0.0732  0.2970  260 GLU A CA  
2037 C C   . GLU A 260 ? 1.1103 1.0244 1.1197 0.0912  0.0633  0.2821  260 GLU A C   
2038 O O   . GLU A 260 ? 1.1938 1.0904 1.2120 0.1018  0.0712  0.2826  260 GLU A O   
2039 C CB  . GLU A 260 ? 1.0756 0.9943 1.0671 0.1066  0.0649  0.3205  260 GLU A CB  
2040 C CG  . GLU A 260 ? 1.1508 1.0480 1.1232 0.1066  0.0741  0.3381  260 GLU A CG  
2041 C CD  . GLU A 260 ? 1.2686 1.1970 1.2422 0.1248  0.0658  0.3633  260 GLU A CD  
2042 O OE1 . GLU A 260 ? 1.2153 1.1772 1.2054 0.1397  0.0556  0.3688  260 GLU A OE1 
2043 O OE2 . GLU A 260 ? 1.2891 1.2109 1.2470 0.1234  0.0693  0.3778  260 GLU A OE2 
2044 N N   . THR A 261 ? 0.9916 0.9440 1.0070 0.0811  0.0472  0.2689  261 THR A N   
2045 C CA  . THR A 261 ? 0.9295 0.9047 0.9617 0.0822  0.0380  0.2552  261 THR A CA  
2046 C C   . THR A 261 ? 0.9348 0.8821 0.9678 0.0709  0.0470  0.2374  261 THR A C   
2047 O O   . THR A 261 ? 0.9777 0.9181 1.0215 0.0789  0.0504  0.2343  261 THR A O   
2048 C CB  . THR A 261 ? 0.9089 0.9268 0.9451 0.0729  0.0213  0.2450  261 THR A CB  
2049 O OG1 . THR A 261 ? 0.8919 0.9027 0.9178 0.0535  0.0224  0.2323  261 THR A OG1 
2050 C CG2 . THR A 261 ? 0.9064 0.9552 0.9408 0.0822  0.0125  0.2615  261 THR A CG2 
2051 N N   . LEU A 262 ? 0.9424 0.8759 0.9640 0.0516  0.0510  0.2257  262 LEU A N   
2052 C CA  . LEU A 262 ? 0.9478 0.8596 0.9688 0.0385  0.0590  0.2087  262 LEU A CA  
2053 C C   . LEU A 262 ? 1.0064 0.8751 1.0233 0.0447  0.0773  0.2139  262 LEU A C   
2054 O O   . LEU A 262 ? 0.9812 0.8363 1.0024 0.0399  0.0833  0.2016  262 LEU A O   
2055 C CB  . LEU A 262 ? 0.9019 0.8105 0.9108 0.0167  0.0605  0.1974  262 LEU A CB  
2056 C CG  . LEU A 262 ? 0.8657 0.8140 0.8790 0.0093  0.0448  0.1899  262 LEU A CG  
2057 C CD1 . LEU A 262 ? 0.8457 0.7907 0.8487 -0.0114 0.0480  0.1788  262 LEU A CD1 
2058 C CD2 . LEU A 262 ? 0.8579 0.8319 0.8877 0.0129  0.0339  0.1796  262 LEU A CD2 
2059 N N   . ALA A 263 ? 0.9944 0.8403 1.0023 0.0553  0.0875  0.2321  263 ALA A N   
2060 C CA  . ALA A 263 ? 1.0265 0.8300 1.0318 0.0650  0.1066  0.2392  263 ALA A CA  
2061 C C   . ALA A 263 ? 1.0175 0.8339 1.0413 0.0854  0.1032  0.2445  263 ALA A C   
2062 O O   . ALA A 263 ? 1.0050 0.7948 1.0322 0.0882  0.1158  0.2392  263 ALA A O   
2063 C CB  . ALA A 263 ? 1.0243 0.8004 1.0156 0.0733  0.1189  0.2597  263 ALA A CB  
2064 N N   . PHE A 264 ? 0.9891 0.8475 1.0246 0.0987  0.0867  0.2541  264 PHE A N   
2065 C CA  . PHE A 264 ? 0.9671 0.8455 1.0213 0.1161  0.0814  0.2575  264 PHE A CA  
2066 C C   . PHE A 264 ? 0.9696 0.8589 1.0333 0.1046  0.0757  0.2352  264 PHE A C   
2067 O O   . PHE A 264 ? 0.9811 0.8684 1.0570 0.1145  0.0791  0.2332  264 PHE A O   
2068 C CB  . PHE A 264 ? 0.9564 0.8814 1.0191 0.1292  0.0648  0.2716  264 PHE A CB  
2069 C CG  . PHE A 264 ? 0.9367 0.8856 1.0183 0.1483  0.0601  0.2783  264 PHE A CG  
2070 C CD1 . PHE A 264 ? 0.9525 0.8747 1.0401 0.1656  0.0750  0.2887  264 PHE A CD1 
2071 C CD2 . PHE A 264 ? 0.8914 0.8897 0.9848 0.1487  0.0419  0.2740  264 PHE A CD2 
2072 C CE1 . PHE A 264 ? 0.9287 0.8762 1.0349 0.1836  0.0707  0.2952  264 PHE A CE1 
2073 C CE2 . PHE A 264 ? 0.9015 0.9248 1.0121 0.1648  0.0376  0.2796  264 PHE A CE2 
2074 C CZ  . PHE A 264 ? 0.9385 0.9380 1.0562 0.1827  0.0515  0.2905  264 PHE A CZ  
2075 N N   . PHE A 265 ? 0.9618 0.8632 1.0203 0.0845  0.0674  0.2190  265 PHE A N   
2076 C CA  . PHE A 265 ? 0.9528 0.8605 1.0180 0.0725  0.0639  0.1988  265 PHE A CA  
2077 C C   . PHE A 265 ? 1.0013 0.8680 1.0611 0.0662  0.0817  0.1907  265 PHE A C   
2078 O O   . PHE A 265 ? 1.0508 0.9158 1.1206 0.0697  0.0840  0.1833  265 PHE A O   
2079 C CB  . PHE A 265 ? 0.9282 0.8549 0.9879 0.0534  0.0538  0.1858  265 PHE A CB  
2080 C CG  . PHE A 265 ? 0.8718 0.8420 0.9408 0.0564  0.0360  0.1855  265 PHE A CG  
2081 C CD1 . PHE A 265 ? 0.8387 0.8269 0.9033 0.0603  0.0292  0.1969  265 PHE A CD1 
2082 C CD2 . PHE A 265 ? 0.8308 0.8229 0.9116 0.0541  0.0271  0.1731  265 PHE A CD2 
2083 C CE1 . PHE A 265 ? 0.8100 0.8370 0.8816 0.0609  0.0145  0.1947  265 PHE A CE1 
2084 C CE2 . PHE A 265 ? 0.7800 0.8087 0.8679 0.0553  0.0130  0.1715  265 PHE A CE2 
2085 C CZ  . PHE A 265 ? 0.8100 0.8561 0.8932 0.0582  0.0070  0.1817  265 PHE A CZ  
2086 N N   . ASP A 266 ? 0.9777 0.8108 1.0209 0.0556  0.0954  0.1911  266 ASP A N   
2087 C CA  . ASP A 266 ? 1.0047 0.7979 1.0397 0.0450  0.1139  0.1808  266 ASP A CA  
2088 C C   . ASP A 266 ? 1.0764 0.8467 1.1193 0.0634  0.1267  0.1884  266 ASP A C   
2089 O O   . ASP A 266 ? 1.1035 0.8595 1.1493 0.0582  0.1349  0.1759  266 ASP A O   
2090 C CB  . ASP A 266 ? 1.0109 0.7712 1.0255 0.0313  0.1279  0.1821  266 ASP A CB  
2091 C CG  . ASP A 266 ? 0.9924 0.7748 0.9995 0.0111  0.1173  0.1723  266 ASP A CG  
2092 O OD1 . ASP A 266 ? 1.0026 0.8142 1.0176 0.0021  0.1048  0.1589  266 ASP A OD1 
2093 O OD2 . ASP A 266 ? 0.9864 0.7569 0.9797 0.0047  0.1222  0.1787  266 ASP A OD2 
2094 N N   . GLU A 267 ? 1.0577 0.8256 1.1043 0.0855  0.1290  0.2096  267 GLU A N   
2095 C CA  A GLU A 267 ? 1.0950 0.8426 1.1507 0.1060  0.1421  0.2195  267 GLU A CA  
2096 C CA  B GLU A 267 ? 1.0951 0.8425 1.1508 0.1057  0.1422  0.2192  267 GLU A CA  
2097 C C   . GLU A 267 ? 1.1089 0.8889 1.1848 0.1149  0.1306  0.2135  267 GLU A C   
2098 O O   . GLU A 267 ? 1.1552 0.9169 1.2384 0.1234  0.1426  0.2115  267 GLU A O   
2099 C CB  A GLU A 267 ? 1.1036 0.8477 1.1596 0.1289  0.1456  0.2462  267 GLU A CB  
2100 C CB  B GLU A 267 ? 1.1043 0.8465 1.1599 0.1286  0.1465  0.2459  267 GLU A CB  
2101 C CG  A GLU A 267 ? 1.1423 0.8619 1.2072 0.1528  0.1622  0.2600  267 GLU A CG  
2102 C CG  B GLU A 267 ? 1.1429 0.8493 1.1775 0.1206  0.1599  0.2533  267 GLU A CG  
2103 C CD  A GLU A 267 ? 1.1473 0.8779 1.2166 0.1786  0.1609  0.2890  267 GLU A CD  
2104 C CD  B GLU A 267 ? 1.1833 0.8341 1.2040 0.1072  0.1850  0.2418  267 GLU A CD  
2105 O OE1 A GLU A 267 ? 1.1404 0.8760 1.1980 0.1749  0.1557  0.2989  267 GLU A OE1 
2106 O OE1 B GLU A 267 ? 1.1900 0.8179 1.2178 0.1174  0.1991  0.2407  267 GLU A OE1 
2107 O OE2 A GLU A 267 ? 1.1574 0.8942 1.2422 0.2027  0.1648  0.3025  267 GLU A OE2 
2108 O OE2 B GLU A 267 ? 1.1861 0.8169 1.1884 0.0855  0.1914  0.2330  267 GLU A OE2 
2109 N N   . MET A 268 ? 1.0835 0.9101 1.1679 0.1125  0.1087  0.2102  268 MET A N   
2110 C CA  . MET A 268 ? 1.0246 0.8833 1.1273 0.1201  0.0977  0.2048  268 MET A CA  
2111 C C   . MET A 268 ? 1.0248 0.8892 1.1280 0.1005  0.0931  0.1817  268 MET A C   
2112 O O   . MET A 268 ? 1.0166 0.8973 1.1330 0.1050  0.0887  0.1752  268 MET A O   
2113 C CB  . MET A 268 ? 0.9790 0.8857 1.0911 0.1298  0.0781  0.2151  268 MET A CB  
2114 C CG  . MET A 268 ? 1.0058 0.9159 1.1196 0.1514  0.0806  0.2401  268 MET A CG  
2115 S SD  . MET A 268 ? 1.1421 1.0479 1.2731 0.1792  0.0914  0.2547  268 MET A SD  
2116 C CE  . MET A 268 ? 1.0991 0.9370 1.2162 0.1818  0.1201  0.2601  268 MET A CE  
2117 N N   . ARG A 269 ? 1.0127 0.8660 1.1019 0.0791  0.0941  0.1699  269 ARG A N   
2118 C CA  . ARG A 269 ? 1.0263 0.8831 1.1151 0.0609  0.0920  0.1498  269 ARG A CA  
2119 C C   . ARG A 269 ? 1.0484 0.8692 1.1334 0.0561  0.1106  0.1410  269 ARG A C   
2120 O O   . ARG A 269 ? 1.0697 0.8936 1.1542 0.0414  0.1100  0.1247  269 ARG A O   
2121 C CB  . ARG A 269 ? 1.0050 0.8674 1.0814 0.0401  0.0865  0.1411  269 ARG A CB  
2122 C CG  . ARG A 269 ? 0.9427 0.8436 1.0238 0.0418  0.0677  0.1451  269 ARG A CG  
2123 C CD  . ARG A 269 ? 0.9930 0.9119 1.0710 0.0231  0.0589  0.1309  269 ARG A CD  
2124 N NE  . ARG A 269 ? 1.0566 0.9555 1.1191 0.0057  0.0678  0.1256  269 ARG A NE  
2125 C CZ  . ARG A 269 ? 1.0981 0.9838 1.1544 -0.0105 0.0758  0.1124  269 ARG A CZ  
2126 N NH1 . ARG A 269 ? 1.1313 1.0197 1.1951 -0.0112 0.0760  0.1034  269 ARG A NH1 
2127 N NH2 . ARG A 269 ? 1.0524 0.9238 1.0941 -0.0274 0.0837  0.1080  269 ARG A NH2 
2128 N N   . GLN A 270 ? 1.0961 0.8828 1.1779 0.0680  0.1280  0.1515  270 GLN A N   
2129 C CA  . GLN A 270 ? 1.1651 0.9165 1.2450 0.0663  0.1478  0.1437  270 GLN A CA  
2130 C C   . GLN A 270 ? 1.1498 0.9129 1.2484 0.0857  0.1473  0.1473  270 GLN A C   
2131 O O   . GLN A 270 ? 1.1417 0.8772 1.2408 0.0865  0.1641  0.1410  270 GLN A O   
2132 C CB  . GLN A 270 ? 1.1891 0.8924 1.2552 0.0692  0.1704  0.1526  270 GLN A CB  
2133 C CG  . GLN A 270 ? 1.2468 0.9343 1.2925 0.0470  0.1743  0.1468  270 GLN A CG  
2134 C CD  . GLN A 270 ? 1.3818 1.0137 1.4106 0.0384  0.2021  0.1437  270 GLN A CD  
2135 O OE1 . GLN A 270 ? 1.5238 1.1262 1.5562 0.0502  0.2196  0.1462  270 GLN A OE1 
2136 N NE2 . GLN A 270 ? 1.4036 1.0207 1.4137 0.0171  0.2074  0.1376  270 GLN A NE2 
2137 N N   . GLN A 271 ? 1.0755 0.8792 1.1890 0.1002  0.1294  0.1566  271 GLN A N   
2138 C CA  A GLN A 271 ? 1.0576 0.8804 1.1900 0.1172  0.1266  0.1594  271 GLN A CA  
2139 C CA  B GLN A 271 ? 1.0576 0.8801 1.1899 0.1170  0.1267  0.1593  271 GLN A CA  
2140 C C   . GLN A 271 ? 1.0105 0.8767 1.1531 0.1109  0.1065  0.1494  271 GLN A C   
2141 O O   . GLN A 271 ? 1.0178 0.8935 1.1721 0.1149  0.1066  0.1428  271 GLN A O   
2142 C CB  A GLN A 271 ? 1.0797 0.9131 1.2225 0.1440  0.1261  0.1829  271 GLN A CB  
2143 C CB  B GLN A 271 ? 1.0802 0.9120 1.2229 0.1441  0.1269  0.1827  271 GLN A CB  
2144 C CG  A GLN A 271 ? 1.1273 0.9167 1.2617 0.1550  0.1475  0.1967  271 GLN A CG  
2145 C CG  B GLN A 271 ? 1.0791 0.9285 1.2419 0.1633  0.1276  0.1872  271 GLN A CG  
2146 C CD  A GLN A 271 ? 1.1539 0.9590 1.3000 0.1835  0.1461  0.2222  271 GLN A CD  
2147 C CD  B GLN A 271 ? 1.1090 0.9689 1.2821 0.1908  0.1293  0.2122  271 GLN A CD  
2148 O OE1 A GLN A 271 ? 1.1385 0.9893 1.3000 0.1945  0.1297  0.2282  271 GLN A OE1 
2149 O OE1 B GLN A 271 ? 1.1338 0.9841 1.2979 0.1960  0.1312  0.2270  271 GLN A OE1 
2150 N NE2 A GLN A 271 ? 1.1808 0.9490 1.3190 0.1952  0.1639  0.2377  271 GLN A NE2 
2151 N NE2 B GLN A 271 ? 1.0740 0.9560 1.2663 0.2087  0.1286  0.2179  271 GLN A NE2 
2152 N N   . GLN A 272 ? 0.9749 0.8659 1.1130 0.1010  0.0905  0.1477  272 GLN A N   
2153 C CA  . GLN A 272 ? 0.8928 0.8220 1.0393 0.0951  0.0729  0.1389  272 GLN A CA  
2154 C C   . GLN A 272 ? 0.8408 0.7753 0.9757 0.0749  0.0649  0.1290  272 GLN A C   
2155 O O   . GLN A 272 ? 0.9331 0.8468 1.0543 0.0661  0.0712  0.1301  272 GLN A O   
2156 C CB  . GLN A 272 ? 0.8782 0.8446 1.0371 0.1110  0.0596  0.1515  272 GLN A CB  
2157 C CG  . GLN A 272 ? 0.8667 0.8353 1.0190 0.1179  0.0572  0.1675  272 GLN A CG  
2158 C CD  . GLN A 272 ? 0.8234 0.8312 0.9876 0.1334  0.0453  0.1807  272 GLN A CD  
2159 O OE1 . GLN A 272 ? 0.8432 0.8502 1.0118 0.1515  0.0504  0.1981  272 GLN A OE1 
2160 N NE2 . GLN A 272 ? 0.7882 0.8311 0.9573 0.1262  0.0301  0.1727  272 GLN A NE2 
2161 N N   . ASP A 273 ? 0.7988 0.7614 0.9393 0.0677  0.0518  0.1195  273 ASP A N   
2162 C CA  A ASP A 273 ? 0.8325 0.8049 0.9649 0.0510  0.0436  0.1110  273 ASP A CA  
2163 C CA  B ASP A 273 ? 0.8264 0.7987 0.9587 0.0510  0.0437  0.1110  273 ASP A CA  
2164 C C   . ASP A 273 ? 0.8125 0.8096 0.9455 0.0551  0.0314  0.1192  273 ASP A C   
2165 O O   . ASP A 273 ? 0.7632 0.7875 0.9064 0.0631  0.0216  0.1217  273 ASP A O   
2166 C CB  A ASP A 273 ? 0.8095 0.7970 0.9472 0.0420  0.0377  0.0976  273 ASP A CB  
2167 C CB  B ASP A 273 ? 0.8114 0.7986 0.9489 0.0418  0.0377  0.0975  273 ASP A CB  
2168 C CG  A ASP A 273 ? 0.7968 0.7923 0.9266 0.0256  0.0316  0.0895  273 ASP A CG  
2169 C CG  B ASP A 273 ? 0.7988 0.7633 0.9332 0.0341  0.0497  0.0878  273 ASP A CG  
2170 O OD1 A ASP A 273 ? 0.7953 0.7833 0.9151 0.0194  0.0332  0.0925  273 ASP A OD1 
2171 O OD1 B ASP A 273 ? 0.8189 0.7538 0.9460 0.0340  0.0636  0.0899  273 ASP A OD1 
2172 O OD2 A ASP A 273 ? 0.8023 0.8124 0.9360 0.0193  0.0258  0.0809  273 ASP A OD2 
2173 O OD2 B ASP A 273 ? 0.7438 0.7192 0.8822 0.0275  0.0461  0.0779  273 ASP A OD2 
2174 N N   . ILE A 274 ? 0.7817 0.7699 0.9031 0.0481  0.0327  0.1226  274 ILE A N   
2175 C CA  . ILE A 274 ? 0.7542 0.7629 0.8739 0.0508  0.0230  0.1304  274 ILE A CA  
2176 C C   . ILE A 274 ? 0.7296 0.7415 0.8402 0.0346  0.0194  0.1228  274 ILE A C   
2177 O O   . ILE A 274 ? 0.7692 0.7611 0.8708 0.0228  0.0274  0.1168  274 ILE A O   
2178 C CB  . ILE A 274 ? 0.7819 0.7778 0.8969 0.0622  0.0290  0.1466  274 ILE A CB  
2179 C CG1 . ILE A 274 ? 0.7915 0.7823 0.9165 0.0797  0.0349  0.1554  274 ILE A CG1 
2180 C CG2 . ILE A 274 ? 0.7643 0.7859 0.8780 0.0651  0.0181  0.1547  274 ILE A CG2 
2181 C CD1 . ILE A 274 ? 0.8516 0.8268 0.9724 0.0932  0.0430  0.1734  274 ILE A CD1 
2182 N N   . ALA A 275 ? 0.8092 0.8476 0.9221 0.0336  0.0082  0.1226  275 ALA A N   
2183 C CA  . ALA A 275 ? 0.7746 0.8196 0.8803 0.0210  0.0048  0.1175  275 ALA A CA  
2184 C C   . ALA A 275 ? 0.7469 0.8137 0.8524 0.0249  -0.0035 0.1237  275 ALA A C   
2185 O O   . ALA A 275 ? 0.7113 0.7881 0.8210 0.0361  -0.0066 0.1323  275 ALA A O   
2186 C CB  . ALA A 275 ? 0.7641 0.8194 0.8742 0.0120  0.0011  0.1050  275 ALA A CB  
2187 N N   . CYS A 276 ? 0.7088 0.7851 0.8097 0.0152  -0.0068 0.1193  276 CYS A N   
2188 C CA  . CYS A 276 ? 0.7009 0.7974 0.8003 0.0164  -0.0136 0.1231  276 CYS A CA  
2189 C C   . CYS A 276 ? 0.6678 0.7749 0.7655 0.0057  -0.0161 0.1147  276 CYS A C   
2190 O O   . CYS A 276 ? 0.6447 0.7440 0.7411 -0.0025 -0.0126 0.1085  276 CYS A O   
2191 C CB  . CYS A 276 ? 0.7016 0.7896 0.7917 0.0200  -0.0104 0.1355  276 CYS A CB  
2192 S SG  . CYS A 276 ? 0.7140 0.7781 0.7901 0.0078  -0.0013 0.1357  276 CYS A SG  
2193 N N   . ASP A 277 ? 0.6728 0.7996 0.7707 0.0058  -0.0215 0.1148  277 ASP A N   
2194 C CA  . ASP A 277 ? 0.6653 0.8026 0.7616 -0.0025 -0.0227 0.1086  277 ASP A CA  
2195 C C   . ASP A 277 ? 0.6941 0.8410 0.7830 -0.0037 -0.0242 0.1139  277 ASP A C   
2196 O O   . ASP A 277 ? 0.6796 0.8292 0.7655 0.0022  -0.0258 0.1223  277 ASP A O   
2197 C CB  . ASP A 277 ? 0.6188 0.7706 0.7242 -0.0022 -0.0262 0.0996  277 ASP A CB  
2198 C CG  . ASP A 277 ? 0.6691 0.8365 0.7776 0.0029  -0.0307 0.0997  277 ASP A CG  
2199 O OD1 . ASP A 277 ? 0.6958 0.8637 0.8098 0.0088  -0.0323 0.1002  277 ASP A OD1 
2200 O OD2 . ASP A 277 ? 0.6863 0.8670 0.7916 0.0002  -0.0322 0.0987  277 ASP A OD2 
2201 N N   . CYS A 278 ? 0.6823 0.8366 0.7686 -0.0113 -0.0234 0.1096  278 CYS A N   
2202 C CA  . CYS A 278 ? 0.6853 0.8495 0.7641 -0.0143 -0.0241 0.1132  278 CYS A CA  
2203 C C   . CYS A 278 ? 0.6819 0.8570 0.7622 -0.0213 -0.0228 0.1055  278 CYS A C   
2204 O O   . CYS A 278 ? 0.6702 0.8428 0.7552 -0.0244 -0.0207 0.1006  278 CYS A O   
2205 C CB  . CYS A 278 ? 0.8089 0.9580 0.8764 -0.0161 -0.0201 0.1230  278 CYS A CB  
2206 S SG  . CYS A 278 ? 0.7299 0.8637 0.7921 -0.0272 -0.0130 0.1199  278 CYS A SG  
2207 N N   . TYR A 279 ? 0.6893 0.8785 0.7658 -0.0235 -0.0237 0.1050  279 TYR A N   
2208 C CA  . TYR A 279 ? 0.6820 0.8815 0.7600 -0.0293 -0.0210 0.0988  279 TYR A CA  
2209 C C   . TYR A 279 ? 0.7039 0.9010 0.7721 -0.0365 -0.0179 0.1034  279 TYR A C   
2210 O O   . TYR A 279 ? 0.7239 0.9157 0.7823 -0.0369 -0.0182 0.1113  279 TYR A O   
2211 C CB  . TYR A 279 ? 0.7207 0.9363 0.8004 -0.0289 -0.0215 0.0929  279 TYR A CB  
2212 C CG  . TYR A 279 ? 0.7206 0.9438 0.7917 -0.0292 -0.0244 0.0978  279 TYR A CG  
2213 C CD1 . TYR A 279 ? 0.7573 0.9837 0.8298 -0.0240 -0.0287 0.0999  279 TYR A CD1 
2214 C CD2 . TYR A 279 ? 0.7202 0.9503 0.7816 -0.0350 -0.0229 0.1006  279 TYR A CD2 
2215 C CE1 . TYR A 279 ? 0.7545 0.9930 0.8193 -0.0243 -0.0319 0.1055  279 TYR A CE1 
2216 C CE2 . TYR A 279 ? 0.7402 0.9803 0.7930 -0.0356 -0.0259 0.1061  279 TYR A CE2 
2217 C CZ  . TYR A 279 ? 0.8126 1.0580 0.8672 -0.0301 -0.0306 0.1089  279 TYR A CZ  
2218 O OH  . TYR A 279 ? 0.8855 1.1458 0.9317 -0.0307 -0.0342 0.1156  279 TYR A OH  
2219 N N   . PRO A 280 ? 0.6675 0.8696 0.7381 -0.0423 -0.0144 0.0994  280 PRO A N   
2220 C CA  . PRO A 280 ? 0.6896 0.8895 0.7510 -0.0511 -0.0107 0.1028  280 PRO A CA  
2221 C C   . PRO A 280 ? 0.6940 0.9059 0.7486 -0.0549 -0.0096 0.1034  280 PRO A C   
2222 O O   . PRO A 280 ? 0.6655 0.8881 0.7202 -0.0613 -0.0062 0.1003  280 PRO A O   
2223 C CB  . PRO A 280 ? 0.7059 0.9134 0.7749 -0.0555 -0.0082 0.0975  280 PRO A CB  
2224 C CG  . PRO A 280 ? 0.6728 0.8928 0.7542 -0.0483 -0.0097 0.0917  280 PRO A CG  
2225 C CD  . PRO A 280 ? 0.6330 0.8444 0.7154 -0.0406 -0.0135 0.0923  280 PRO A CD  
2226 N N   . TYR A 281 ? 0.6933 0.9059 0.7423 -0.0513 -0.0125 0.1074  281 TYR A N   
2227 C CA  . TYR A 281 ? 0.7066 0.9312 0.7473 -0.0558 -0.0117 0.1083  281 TYR A CA  
2228 C C   . TYR A 281 ? 0.7620 0.9796 0.7907 -0.0542 -0.0141 0.1195  281 TYR A C   
2229 O O   . TYR A 281 ? 0.7573 0.9658 0.7874 -0.0469 -0.0173 0.1251  281 TYR A O   
2230 C CB  . TYR A 281 ? 0.6988 0.9404 0.7457 -0.0539 -0.0122 0.0995  281 TYR A CB  
2231 C CG  . TYR A 281 ? 0.6953 0.9438 0.7541 -0.0535 -0.0082 0.0902  281 TYR A CG  
2232 C CD1 . TYR A 281 ? 0.7173 0.9609 0.7875 -0.0473 -0.0091 0.0869  281 TYR A CD1 
2233 C CD2 . TYR A 281 ? 0.7077 0.9686 0.7667 -0.0586 -0.0030 0.0856  281 TYR A CD2 
2234 C CE1 . TYR A 281 ? 0.6673 0.9180 0.7485 -0.0453 -0.0051 0.0807  281 TYR A CE1 
2235 C CE2 . TYR A 281 ? 0.7254 0.9942 0.7967 -0.0559 0.0015  0.0790  281 TYR A CE2 
2236 C CZ  . TYR A 281 ? 0.7109 0.9745 0.7932 -0.0489 0.0003  0.0773  281 TYR A CZ  
2237 O OH  . TYR A 281 ? 0.7179 0.9900 0.8124 -0.0447 0.0049  0.0730  281 TYR A OH  
2238 N N   . SER A 282 ? 0.7290 0.9521 0.7462 -0.0606 -0.0123 0.1237  282 SER A N   
2239 C CA  . SER A 282 ? 0.7623 0.9813 0.7669 -0.0589 -0.0141 0.1366  282 SER A CA  
2240 C C   . SER A 282 ? 0.7828 1.0242 0.7827 -0.0601 -0.0175 0.1361  282 SER A C   
2241 O O   . SER A 282 ? 0.8165 1.0617 0.8037 -0.0622 -0.0182 0.1460  282 SER A O   
2242 C CB  . SER A 282 ? 0.7652 0.9707 0.7571 -0.0664 -0.0085 0.1439  282 SER A CB  
2243 O OG  . SER A 282 ? 0.8068 1.0260 0.7955 -0.0764 -0.0052 0.1371  282 SER A OG  
2244 N N   . ALA A 283 ? 0.8038 1.0602 0.8129 -0.0596 -0.0190 0.1244  283 ALA A N   
2245 C CA  . ALA A 283 ? 0.8467 1.1252 0.8511 -0.0631 -0.0210 0.1209  283 ALA A CA  
2246 C C   . ALA A 283 ? 0.9063 1.1927 0.9209 -0.0587 -0.0237 0.1124  283 ALA A C   
2247 O O   . ALA A 283 ? 0.8438 1.1217 0.8703 -0.0554 -0.0218 0.1044  283 ALA A O   
2248 C CB  . ALA A 283 ? 0.8144 1.1039 0.8156 -0.0729 -0.0151 0.1114  283 ALA A CB  
2249 N N   . SER A 284 ? 1.0282 1.3326 1.0376 -0.0594 -0.0281 0.1145  284 SER A N   
2250 C CA  . SER A 284 ? 0.9343 1.2492 0.9513 -0.0578 -0.0302 0.1058  284 SER A CA  
2251 C C   . SER A 284 ? 0.9942 1.3241 1.0092 -0.0678 -0.0249 0.0906  284 SER A C   
2252 O O   . SER A 284 ? 0.9995 1.3349 1.0067 -0.0755 -0.0205 0.0879  284 SER A O   
2253 C CB  . SER A 284 ? 0.9429 1.2721 0.9562 -0.0533 -0.0378 0.1168  284 SER A CB  
2254 O OG  . SER A 284 ? 1.0135 1.3257 1.0304 -0.0424 -0.0407 0.1299  284 SER A OG  
2255 N N   . SER A 285 ? 1.0419 1.3772 1.0637 -0.0682 -0.0241 0.0799  285 SER A N   
2256 C CA  . SER A 285 ? 1.0604 1.4069 1.0798 -0.0782 -0.0170 0.0640  285 SER A CA  
2257 C C   . SER A 285 ? 1.0448 1.4064 1.0644 -0.0810 -0.0199 0.0586  285 SER A C   
2258 O O   . SER A 285 ? 1.0271 1.3794 1.0569 -0.0749 -0.0208 0.0559  285 SER A O   
2259 C CB  . SER A 285 ? 0.9647 1.2942 0.9944 -0.0762 -0.0076 0.0528  285 SER A CB  
2260 O OG  . SER A 285 ? 0.9518 1.2881 0.9793 -0.0850 0.0016  0.0372  285 SER A OG  
2261 N N   . SER A 286 ? 0.9712 1.3581 0.9790 -0.0915 -0.0213 0.0567  286 SER A N   
2262 C CA  . SER A 286 ? 0.9317 1.3397 0.9380 -0.0968 -0.0246 0.0518  286 SER A CA  
2263 C C   . SER A 286 ? 0.9770 1.4089 0.9698 -0.1138 -0.0197 0.0405  286 SER A C   
2264 O O   . SER A 286 ? 0.9756 1.4043 0.9617 -0.1203 -0.0128 0.0355  286 SER A O   
2265 C CB  . SER A 286 ? 0.9646 1.3860 0.9713 -0.0880 -0.0368 0.0700  286 SER A CB  
2266 O OG  . SER A 286 ? 0.9539 1.4079 0.9551 -0.0961 -0.0411 0.0677  286 SER A OG  
2267 N N   . THR A 287 ? 0.9507 1.4083 0.9393 -0.1222 -0.0227 0.0356  287 THR A N   
2268 C CA  . THR A 287 ? 0.9429 1.4283 0.9166 -0.1407 -0.0189 0.0252  287 THR A CA  
2269 C C   . THR A 287 ? 0.9173 1.4268 0.8789 -0.1421 -0.0276 0.0417  287 THR A C   
2270 O O   . THR A 287 ? 0.8872 1.3990 0.8520 -0.1290 -0.0381 0.0620  287 THR A O   
2271 C CB  . THR A 287 ? 0.9606 1.4701 0.9330 -0.1510 -0.0198 0.0150  287 THR A CB  
2272 O OG1 . THR A 287 ? 0.9935 1.5248 0.9693 -0.1420 -0.0339 0.0327  287 THR A OG1 
2273 C CG2 . THR A 287 ? 0.9921 1.4753 0.9756 -0.1495 -0.0105 -0.0003 287 THR A CG2 
2274 N N   . LEU A 288 ? 0.9723 1.4988 0.9194 -0.1580 -0.0221 0.0332  288 LEU A N   
2275 C CA  . LEU A 288 ? 0.9549 1.5062 0.8884 -0.1611 -0.0295 0.0485  288 LEU A CA  
2276 C C   . LEU A 288 ? 0.9997 1.5909 0.9290 -0.1631 -0.0412 0.0592  288 LEU A C   
2277 O O   . LEU A 288 ? 0.9727 1.5927 0.8948 -0.1794 -0.0393 0.0459  288 LEU A O   
2278 C CB  . LEU A 288 ? 0.9452 1.5057 0.8639 -0.1792 -0.0197 0.0349  288 LEU A CB  
2279 C CG  . LEU A 288 ? 0.9317 1.5092 0.8361 -0.1819 -0.0250 0.0504  288 LEU A CG  
2280 C CD1 . LEU A 288 ? 0.9473 1.5047 0.8584 -0.1622 -0.0330 0.0738  288 LEU A CD1 
2281 C CD2 . LEU A 288 ? 0.8697 1.4401 0.7647 -0.1951 -0.0123 0.0357  288 LEU A CD2 
2282 N N   . ASP A 289 ? 1.0519 1.6453 0.9858 -0.1465 -0.0524 0.0832  289 ASP A N   
2283 C CA  . ASP A 289 ? 1.0713 1.7025 1.0043 -0.1433 -0.0641 0.0978  289 ASP A CA  
2284 C C   . ASP A 289 ? 1.0504 1.7092 0.9686 -0.1447 -0.0710 0.1172  289 ASP A C   
2285 O O   . ASP A 289 ? 1.0656 1.7024 0.9798 -0.1375 -0.0698 0.1287  289 ASP A O   
2286 C CB  . ASP A 289 ? 1.0480 1.6614 0.9978 -0.1216 -0.0705 0.1123  289 ASP A CB  
2287 C CG  . ASP A 289 ? 1.2179 1.8715 1.1701 -0.1158 -0.0819 0.1280  289 ASP A CG  
2288 O OD1 . ASP A 289 ? 1.2203 1.9169 1.1601 -0.1251 -0.0874 0.1351  289 ASP A OD1 
2289 O OD2 . ASP A 289 ? 1.1780 1.8220 1.1450 -0.1014 -0.0854 0.1340  289 ASP A OD2 
2290 N N   . MET A 290 ? 0.9951 1.7037 0.9047 -0.1544 -0.0780 0.1212  290 MET A N   
2291 C CA  . MET A 290 ? 0.9602 1.7005 0.8548 -0.1560 -0.0851 0.1412  290 MET A CA  
2292 C C   . MET A 290 ? 0.9656 1.6968 0.8669 -0.1312 -0.0936 0.1723  290 MET A C   
2293 O O   . MET A 290 ? 0.9414 1.6701 0.8323 -0.1266 -0.0951 0.1902  290 MET A O   
2294 C CB  . MET A 290 ? 0.8836 1.6843 0.7678 -0.1732 -0.0908 0.1379  290 MET A CB  
2295 C CG  . MET A 290 ? 0.7926 1.6317 0.6588 -0.1785 -0.0975 0.1567  290 MET A CG  
2296 S SD  . MET A 290 ? 0.7716 1.5939 0.6188 -0.1964 -0.0866 0.1435  290 MET A SD  
2297 C CE  . MET A 290 ? 0.7509 1.5861 0.5925 -0.2259 -0.0750 0.1044  290 MET A CE  
2298 N N   . LYS A 291 ? 1.0029 1.7273 0.9211 -0.1152 -0.0979 0.1789  291 LYS A N   
2299 C CA  A LYS A 291 ? 0.9956 1.7067 0.9212 -0.0907 -0.1034 0.2073  291 LYS A CA  
2300 C CA  B LYS A 291 ? 0.9957 1.7068 0.9212 -0.0908 -0.1034 0.2073  291 LYS A CA  
2301 C C   . LYS A 291 ? 0.9948 1.6476 0.9244 -0.0799 -0.0960 0.2092  291 LYS A C   
2302 O O   . LYS A 291 ? 0.9851 1.6211 0.9158 -0.0625 -0.0977 0.2324  291 LYS A O   
2303 C CB  A LYS A 291 ? 0.9675 1.6908 0.9103 -0.0777 -0.1092 0.2124  291 LYS A CB  
2304 C CB  B LYS A 291 ? 0.9674 1.6912 0.9100 -0.0777 -0.1093 0.2127  291 LYS A CB  
2305 C CG  A LYS A 291 ? 0.9693 1.7558 0.9094 -0.0873 -0.1176 0.2134  291 LYS A CG  
2306 C CG  B LYS A 291 ? 0.9666 1.7549 0.9063 -0.0827 -0.1191 0.2213  291 LYS A CG  
2307 C CD  A LYS A 291 ? 0.9387 1.7362 0.8973 -0.0748 -0.1223 0.2165  291 LYS A CD  
2308 C CD  B LYS A 291 ? 0.9287 1.7410 0.8629 -0.0673 -0.1270 0.2554  291 LYS A CD  
2309 C CE  A LYS A 291 ? 0.9214 1.7053 0.8904 -0.0464 -0.1263 0.2465  291 LYS A CE  
2310 C CE  B LYS A 291 ? 0.9005 1.7437 0.8129 -0.0834 -0.1287 0.2594  291 LYS A CE  
2311 N NZ  A LYS A 291 ? 0.8633 1.6885 0.8228 -0.0396 -0.1343 0.2747  291 LYS A NZ  
2312 N NZ  B LYS A 291 ? 0.8638 1.7259 0.7702 -0.0668 -0.1353 0.2949  291 LYS A NZ  
2313 N N   A GLN A 292 ? 1.0007 1.6234 0.9321 -0.0898 -0.0870 0.1857  292 GLN A N   
2314 N N   B GLN A 292 ? 1.0008 1.6234 0.9323 -0.0897 -0.0870 0.1858  292 GLN A N   
2315 C CA  A GLN A 292 ? 1.0084 1.5817 0.9428 -0.0826 -0.0799 0.1857  292 GLN A CA  
2316 C CA  B GLN A 292 ? 1.0084 1.5818 0.9428 -0.0824 -0.0799 0.1860  292 GLN A CA  
2317 C C   A GLN A 292 ? 0.9702 1.5388 0.8886 -0.0932 -0.0751 0.1858  292 GLN A C   
2318 C C   B GLN A 292 ? 0.9702 1.5389 0.8885 -0.0931 -0.0752 0.1860  292 GLN A C   
2319 O O   A GLN A 292 ? 0.9906 1.5228 0.9092 -0.0880 -0.0696 0.1886  292 GLN A O   
2320 O O   B GLN A 292 ? 0.9917 1.5240 0.9102 -0.0880 -0.0697 0.1889  292 GLN A O   
2321 C CB  A GLN A 292 ? 1.0082 1.5528 0.9555 -0.0853 -0.0728 0.1624  292 GLN A CB  
2322 C CB  B GLN A 292 ? 1.0083 1.5522 0.9556 -0.0848 -0.0728 0.1630  292 GLN A CB  
2323 C CG  A GLN A 292 ? 0.9985 1.5436 0.9617 -0.0757 -0.0763 0.1604  292 GLN A CG  
2324 C CG  B GLN A 292 ? 0.9998 1.5390 0.9638 -0.0730 -0.0762 0.1631  292 GLN A CG  
2325 C CD  A GLN A 292 ? 1.0198 1.5375 0.9932 -0.0551 -0.0783 0.1783  292 GLN A CD  
2326 C CD  B GLN A 292 ? 1.0116 1.5156 0.9876 -0.0726 -0.0688 0.1448  292 GLN A CD  
2327 O OE1 A GLN A 292 ? 1.0177 1.5521 0.9962 -0.0433 -0.0849 0.1941  292 GLN A OE1 
2328 O OE1 B GLN A 292 ? 0.9847 1.4573 0.9606 -0.0717 -0.0626 0.1418  292 GLN A OE1 
2329 N NE2 A GLN A 292 ? 1.0295 1.5059 1.0060 -0.0510 -0.0717 0.1755  292 GLN A NE2 
2330 N NE2 B GLN A 292 ? 1.0081 1.5192 0.9943 -0.0737 -0.0693 0.1329  292 GLN A NE2 
2331 N N   . VAL A 293 ? 1.0449 1.6507 0.9488 -0.1090 -0.0767 0.1821  293 VAL A N   
2332 C CA  . VAL A 293 ? 1.0203 1.6246 0.9079 -0.1202 -0.0719 0.1820  293 VAL A CA  
2333 C C   . VAL A 293 ? 1.0077 1.6047 0.8875 -0.1075 -0.0757 0.2108  293 VAL A C   
2334 O O   . VAL A 293 ? 1.0132 1.6366 0.8903 -0.0987 -0.0841 0.2320  293 VAL A O   
2335 C CB  . VAL A 293 ? 0.9730 1.6216 0.8460 -0.1413 -0.0725 0.1708  293 VAL A CB  
2336 C CG1 . VAL A 293 ? 0.9291 1.5812 0.7837 -0.1515 -0.0690 0.1756  293 VAL A CG1 
2337 C CG2 . VAL A 293 ? 0.9770 1.6230 0.8555 -0.1556 -0.0644 0.1400  293 VAL A CG2 
2338 N N   . THR A 294 ? 0.9216 1.4831 0.7978 -0.1063 -0.0687 0.2121  294 THR A N   
2339 C CA  . THR A 294 ? 0.9761 1.5228 0.8437 -0.0954 -0.0694 0.2380  294 THR A CA  
2340 C C   . THR A 294 ? 1.0337 1.5560 0.8913 -0.1052 -0.0606 0.2318  294 THR A C   
2341 O O   . THR A 294 ? 0.9864 1.4989 0.8481 -0.1161 -0.0539 0.2087  294 THR A O   
2342 C CB  . THR A 294 ? 1.0375 1.5531 0.9189 -0.0743 -0.0701 0.2518  294 THR A CB  
2343 O OG1 . THR A 294 ? 1.1269 1.6299 0.9982 -0.0635 -0.0696 0.2788  294 THR A OG1 
2344 C CG2 . THR A 294 ? 0.9540 1.4274 0.8473 -0.0738 -0.0621 0.2349  294 THR A CG2 
2345 N N   . ASP A 295 ? 1.0406 1.5536 0.8854 -0.1006 -0.0598 0.2535  295 ASP A N   
2346 C CA  . ASP A 295 ? 1.0759 1.5662 0.9098 -0.1096 -0.0514 0.2508  295 ASP A CA  
2347 C C   . ASP A 295 ? 1.1089 1.5514 0.9494 -0.0989 -0.0449 0.2566  295 ASP A C   
2348 O O   . ASP A 295 ? 1.1127 1.5348 0.9453 -0.1065 -0.0373 0.2541  295 ASP A O   
2349 C CB  . ASP A 295 ? 1.1230 1.6340 0.9351 -0.1149 -0.0532 0.2701  295 ASP A CB  
2350 C CG  . ASP A 295 ? 1.1965 1.7048 1.0050 -0.0967 -0.0579 0.3017  295 ASP A CG  
2351 O OD1 . ASP A 295 ? 1.1694 1.7003 0.9866 -0.0862 -0.0660 0.3096  295 ASP A OD1 
2352 O OD2 . ASP A 295 ? 1.3242 1.8072 1.1215 -0.0925 -0.0527 0.3190  295 ASP A OD2 
2353 N N   . GLU A 296 ? 1.0888 1.5143 0.9432 -0.0828 -0.0472 0.2633  296 GLU A N   
2354 C CA  . GLU A 296 ? 1.0782 1.4590 0.9366 -0.0731 -0.0405 0.2708  296 GLU A CA  
2355 C C   . GLU A 296 ? 0.9954 1.3517 0.8646 -0.0799 -0.0338 0.2482  296 GLU A C   
2356 O O   . GLU A 296 ? 1.1551 1.4765 1.0243 -0.0774 -0.0268 0.2514  296 GLU A O   
2357 C CB  . GLU A 296 ? 1.0838 1.4559 0.9530 -0.0536 -0.0442 0.2858  296 GLU A CB  
2358 C CG  . GLU A 296 ? 1.1815 1.5870 1.0443 -0.0448 -0.0524 0.3078  296 GLU A CG  
2359 C CD  . GLU A 296 ? 1.2587 1.6506 1.1311 -0.0231 -0.0535 0.3272  296 GLU A CD  
2360 O OE1 . GLU A 296 ? 1.2866 1.6383 1.1559 -0.0142 -0.0452 0.3397  296 GLU A OE1 
2361 O OE2 . GLU A 296 ? 1.2154 1.6366 1.0981 -0.0154 -0.0617 0.3293  296 GLU A OE2 
2362 N N   . PHE A 297 ? 1.0000 1.3741 0.8779 -0.0888 -0.0349 0.2259  297 PHE A N   
2363 C CA  . PHE A 297 ? 0.9194 1.2745 0.8082 -0.0941 -0.0286 0.2060  297 PHE A CA  
2364 C C   . PHE A 297 ? 0.8887 1.2687 0.7798 -0.1066 -0.0276 0.1849  297 PHE A C   
2365 O O   . PHE A 297 ? 0.9356 1.3459 0.8207 -0.1115 -0.0321 0.1838  297 PHE A O   
2366 C CB  . PHE A 297 ? 0.9038 1.2382 0.8102 -0.0821 -0.0294 0.2027  297 PHE A CB  
2367 C CG  . PHE A 297 ? 0.8793 1.2329 0.7945 -0.0737 -0.0373 0.2038  297 PHE A CG  
2368 C CD1 . PHE A 297 ? 0.8341 1.2077 0.7580 -0.0795 -0.0391 0.1852  297 PHE A CD1 
2369 C CD2 . PHE A 297 ? 0.8829 1.2344 0.7979 -0.0600 -0.0418 0.2235  297 PHE A CD2 
2370 C CE1 . PHE A 297 ? 0.8320 1.2244 0.7633 -0.0736 -0.0458 0.1852  297 PHE A CE1 
2371 C CE2 . PHE A 297 ? 0.8229 1.1958 0.7470 -0.0526 -0.0491 0.2245  297 PHE A CE2 
2372 C CZ  . PHE A 297 ? 0.8240 1.2181 0.7559 -0.0604 -0.0514 0.2049  297 PHE A CZ  
2373 N N   . ASP A 298 ? 0.7914 1.1588 0.6910 -0.1118 -0.0209 0.1682  298 ASP A N   
2374 C CA  . ASP A 298 ? 0.8208 1.2062 0.7237 -0.1224 -0.0170 0.1477  298 ASP A CA  
2375 C C   . ASP A 298 ? 0.8518 1.2487 0.7664 -0.1186 -0.0205 0.1370  298 ASP A C   
2376 O O   . ASP A 298 ? 0.8489 1.2320 0.7761 -0.1076 -0.0236 0.1389  298 ASP A O   
2377 C CB  . ASP A 298 ? 0.8994 1.2690 0.8105 -0.1260 -0.0084 0.1350  298 ASP A CB  
2378 C CG  . ASP A 298 ? 0.9722 1.3434 0.8699 -0.1369 -0.0026 0.1373  298 ASP A CG  
2379 O OD1 . ASP A 298 ? 1.1180 1.4835 1.0020 -0.1370 -0.0046 0.1544  298 ASP A OD1 
2380 O OD2 . ASP A 298 ? 1.0204 1.3982 0.9215 -0.1449 0.0047  0.1225  298 ASP A OD2 
2381 N N   . ILE A 299 ? 0.8363 1.2583 0.7459 -0.1292 -0.0191 0.1250  299 ILE A N   
2382 C CA  . ILE A 299 ? 0.8556 1.2890 0.7742 -0.1295 -0.0199 0.1115  299 ILE A CA  
2383 C C   . ILE A 299 ? 0.8857 1.3229 0.8058 -0.1409 -0.0092 0.0897  299 ILE A C   
2384 O O   . ILE A 299 ? 0.8956 1.3546 0.8035 -0.1542 -0.0060 0.0826  299 ILE A O   
2385 C CB  . ILE A 299 ? 0.8400 1.3036 0.7496 -0.1325 -0.0280 0.1186  299 ILE A CB  
2386 C CG1 . ILE A 299 ? 0.8211 1.2806 0.7306 -0.1186 -0.0374 0.1422  299 ILE A CG1 
2387 C CG2 . ILE A 299 ? 0.8336 1.3086 0.7516 -0.1357 -0.0272 0.1021  299 ILE A CG2 
2388 C CD1 . ILE A 299 ? 0.8416 1.3355 0.7439 -0.1193 -0.0462 0.1521  299 ILE A CD1 
2389 N N   . VAL A 300 ? 0.8497 1.2662 0.7848 -0.1355 -0.0028 0.0793  300 VAL A N   
2390 C CA  . VAL A 300 ? 0.8820 1.2981 0.8215 -0.1426 0.0092  0.0602  300 VAL A CA  
2391 C C   . VAL A 300 ? 0.8768 1.2996 0.8210 -0.1457 0.0127  0.0450  300 VAL A C   
2392 O O   . VAL A 300 ? 0.8662 1.2816 0.8202 -0.1372 0.0079  0.0463  300 VAL A O   
2393 C CB  . VAL A 300 ? 0.8493 1.2432 0.8033 -0.1343 0.0146  0.0582  300 VAL A CB  
2394 C CG1 . VAL A 300 ? 0.8786 1.2753 0.8353 -0.1410 0.0278  0.0426  300 VAL A CG1 
2395 C CG2 . VAL A 300 ? 0.8565 1.2403 0.8066 -0.1304 0.0096  0.0748  300 VAL A CG2 
2396 N N   . ILE A 301 ? 0.8690 1.3047 0.8057 -0.1588 0.0222  0.0296  301 ILE A N   
2397 C CA  . ILE A 301 ? 0.9378 1.3784 0.8764 -0.1651 0.0287  0.0126  301 ILE A CA  
2398 C C   . ILE A 301 ? 0.9747 1.3916 0.9298 -0.1577 0.0406  0.0001  301 ILE A C   
2399 O O   . ILE A 301 ? 0.9557 1.3653 0.9141 -0.1575 0.0503  -0.0049 301 ILE A O   
2400 C CB  . ILE A 301 ? 0.9372 1.4015 0.8586 -0.1843 0.0354  0.0006  301 ILE A CB  
2401 C CG1 . ILE A 301 ? 0.8588 1.3518 0.7667 -0.1918 0.0234  0.0093  301 ILE A CG1 
2402 C CG2 . ILE A 301 ? 1.0137 1.4710 0.9388 -0.1918 0.0513  -0.0229 301 ILE A CG2 
2403 C CD1 . ILE A 301 ? 0.8333 1.3352 0.7336 -0.1862 0.0105  0.0330  301 ILE A CD1 
2404 N N   . THR A 302 ? 0.9033 1.3093 0.8690 -0.1507 0.0400  -0.0039 302 THR A N   
2405 C CA  . THR A 302 ? 0.9036 1.2881 0.8841 -0.1436 0.0522  -0.0153 302 THR A CA  
2406 C C   . THR A 302 ? 0.9470 1.3334 0.9220 -0.1560 0.0676  -0.0361 302 THR A C   
2407 O O   . THR A 302 ? 0.9716 1.3495 0.9497 -0.1571 0.0824  -0.0465 302 THR A O   
2408 C CB  . THR A 302 ? 0.9188 1.2889 0.9125 -0.1308 0.0455  -0.0098 302 THR A CB  
2409 O OG1 . THR A 302 ? 0.9489 1.3308 0.9363 -0.1374 0.0402  -0.0128 302 THR A OG1 
2410 C CG2 . THR A 302 ? 0.9087 1.2739 0.9074 -0.1195 0.0327  0.0090  302 THR A CG2 
2411 N N   . TRP A 303 ? 1.0082 1.4063 0.9748 -0.1659 0.0654  -0.0426 303 TRP A N   
2412 C CA  . TRP A 303 ? 1.0562 1.4571 1.0144 -0.1813 0.0805  -0.0637 303 TRP A CA  
2413 C C   . TRP A 303 ? 1.0778 1.5107 1.0177 -0.1989 0.0729  -0.0650 303 TRP A C   
2414 O O   . TRP A 303 ? 1.0246 1.4742 0.9622 -0.1955 0.0559  -0.0494 303 TRP A O   
2415 C CB  . TRP A 303 ? 0.9993 1.3787 0.9681 -0.1764 0.0893  -0.0741 303 TRP A CB  
2416 C CG  . TRP A 303 ? 0.9837 1.3669 0.9572 -0.1703 0.0746  -0.0645 303 TRP A CG  
2417 C CD1 . TRP A 303 ? 1.0202 1.3901 1.0080 -0.1524 0.0643  -0.0498 303 TRP A CD1 
2418 C CD2 . TRP A 303 ? 0.9797 1.3833 0.9437 -0.1828 0.0691  -0.0693 303 TRP A CD2 
2419 N NE1 . TRP A 303 ? 1.0154 1.3941 1.0037 -0.1521 0.0533  -0.0452 303 TRP A NE1 
2420 C CE2 . TRP A 303 ? 0.9802 1.3809 0.9546 -0.1701 0.0557  -0.0566 303 TRP A CE2 
2421 C CE3 . TRP A 303 ? 1.0374 1.4636 0.9849 -0.2045 0.0746  -0.0837 303 TRP A CE3 
2422 C CZ2 . TRP A 303 ? 0.9614 1.3819 0.9316 -0.1770 0.0475  -0.0569 303 TRP A CZ2 
2423 C CZ3 . TRP A 303 ? 1.0165 1.4643 0.9592 -0.2125 0.0659  -0.0841 303 TRP A CZ3 
2424 C CH2 . TRP A 303 ? 0.9680 1.4132 0.9227 -0.1981 0.0523  -0.0704 303 TRP A CH2 
2425 N N   . SER A 304 ? 1.1288 1.5712 1.0555 -0.2178 0.0866  -0.0837 304 SER A N   
2426 C CA  . SER A 304 ? 1.2616 1.7393 1.1693 -0.2376 0.0809  -0.0872 304 SER A CA  
2427 C C   . SER A 304 ? 1.3463 1.8223 1.2444 -0.2573 0.1006  -0.1138 304 SER A C   
2428 O O   . SER A 304 ? 1.3904 1.8595 1.2823 -0.2662 0.1168  -0.1273 304 SER A O   
2429 C CB  . SER A 304 ? 1.3878 1.8881 1.2826 -0.2435 0.0742  -0.0768 304 SER A CB  
2430 O OG  . SER A 304 ? 1.2881 1.8256 1.1636 -0.2638 0.0699  -0.0806 304 SER A OG  
2431 N N   . GLU A 305 ? 1.3602 1.8417 1.2569 -0.2647 0.1003  -0.1220 305 GLU A N   
2432 C CA  . GLU A 305 ? 1.4874 1.9645 1.3740 -0.2851 0.1206  -0.1487 305 GLU A CA  
2433 C C   . GLU A 305 ? 1.4470 1.9578 1.3106 -0.3112 0.1245  -0.1597 305 GLU A C   
2434 O O   . GLU A 305 ? 1.4789 1.9802 1.3326 -0.3280 0.1461  -0.1827 305 GLU A O   
2435 C CB  . GLU A 305 ? 1.4888 1.9674 1.3778 -0.2891 0.1184  -0.1545 305 GLU A CB  
2436 C CG  . GLU A 305 ? 1.6176 2.0747 1.5010 -0.3047 0.1433  -0.1820 305 GLU A CG  
2437 C CD  . GLU A 305 ? 1.6840 2.0931 1.5819 -0.2884 0.1614  -0.1869 305 GLU A CD  
2438 O OE1 . GLU A 305 ? 1.7219 2.1101 1.6382 -0.2649 0.1537  -0.1722 305 GLU A OE1 
2439 O OE2 . GLU A 305 ? 1.6713 2.0646 1.5620 -0.2986 0.1838  -0.2050 305 GLU A OE2 
2440 N N   . ALA A 306 ? 1.4084 1.9581 1.2628 -0.3149 0.1049  -0.1433 306 ALA A N   
2441 C CA  . ALA A 306 ? 1.3745 1.9608 1.2061 -0.3398 0.1069  -0.1515 306 ALA A CA  
2442 C C   . ALA A 306 ? 1.4087 1.9831 1.2357 -0.3413 0.1187  -0.1557 306 ALA A C   
2443 O O   . ALA A 306 ? 1.4243 2.0010 1.2372 -0.3623 0.1371  -0.1777 306 ALA A O   
2444 C CB  . ALA A 306 ? 1.2526 1.8841 1.0771 -0.3401 0.0824  -0.1291 306 ALA A CB  
2445 N N   . GLN A 307 ? 1.4269 1.9885 1.2653 -0.3201 0.1093  -0.1356 307 GLN A N   
2446 C CA  . GLN A 307 ? 1.4492 2.0013 1.2851 -0.3194 0.1185  -0.1368 307 GLN A CA  
2447 C C   . GLN A 307 ? 1.5463 2.0577 1.4051 -0.2945 0.1236  -0.1311 307 GLN A C   
2448 O O   . GLN A 307 ? 1.4236 1.9315 1.2918 -0.2770 0.1098  -0.1099 307 GLN A O   
2449 C CB  . GLN A 307 ? 1.3683 1.9513 1.1928 -0.3210 0.1016  -0.1166 307 GLN A CB  
2450 C CG  . GLN A 307 ? 1.3160 1.9452 1.1217 -0.3390 0.0891  -0.1127 307 GLN A CG  
2451 C CD  . GLN A 307 ? 1.4219 2.0705 1.2078 -0.3692 0.1052  -0.1391 307 GLN A CD  
2452 O OE1 . GLN A 307 ? 1.4975 2.1317 1.2782 -0.3785 0.1240  -0.1561 307 GLN A OE1 
2453 N NE2 . GLN A 307 ? 1.3898 2.0724 1.1646 -0.3852 0.0986  -0.1431 307 GLN A NE2 
2454 N N   . PRO A 308 ? 1.5039 1.9846 1.3717 -0.2925 0.1440  -0.1493 308 PRO A N   
2455 C CA  . PRO A 308 ? 1.4394 1.8855 1.3297 -0.2682 0.1488  -0.1427 308 PRO A CA  
2456 C C   . PRO A 308 ? 1.4086 1.8521 1.3021 -0.2616 0.1521  -0.1364 308 PRO A C   
2457 O O   . PRO A 308 ? 1.4021 1.8258 1.3140 -0.2410 0.1509  -0.1259 308 PRO A O   
2458 C CB  . PRO A 308 ? 1.4597 1.8769 1.3550 -0.2708 0.1727  -0.1648 308 PRO A CB  
2459 C CG  . PRO A 308 ? 1.4499 1.8850 1.3278 -0.2943 0.1752  -0.1800 308 PRO A CG  
2460 C CD  . PRO A 308 ? 1.4659 1.9418 1.3241 -0.3118 0.1633  -0.1754 308 PRO A CD  
2461 N N   . GLU A 309 ? 1.3995 1.8645 1.2754 -0.2793 0.1565  -0.1428 309 GLU A N   
2462 C CA  A GLU A 309 ? 1.4067 1.8710 1.2850 -0.2746 0.1604  -0.1377 309 GLU A CA  
2463 C CA  B GLU A 309 ? 1.4058 1.8702 1.2840 -0.2746 0.1604  -0.1377 309 GLU A CA  
2464 C C   . GLU A 309 ? 1.4060 1.8769 1.2906 -0.2597 0.1387  -0.1113 309 GLU A C   
2465 O O   . GLU A 309 ? 1.3663 1.8223 1.2659 -0.2439 0.1399  -0.1032 309 GLU A O   
2466 C CB  A GLU A 309 ? 1.3999 1.8878 1.2558 -0.2989 0.1692  -0.1504 309 GLU A CB  
2467 C CB  B GLU A 309 ? 1.4016 1.8899 1.2572 -0.2989 0.1688  -0.1501 309 GLU A CB  
2468 C CG  A GLU A 309 ? 1.3772 1.8695 1.2326 -0.2968 0.1719  -0.1446 309 GLU A CG  
2469 C CG  B GLU A 309 ? 1.4041 1.9009 1.2437 -0.3220 0.1812  -0.1728 309 GLU A CG  
2470 C CD  A GLU A 309 ? 1.3739 1.8930 1.2170 -0.3000 0.1505  -0.1236 309 GLU A CD  
2471 C CD  B GLU A 309 ? 1.4215 1.9506 1.2465 -0.3341 0.1620  -0.1648 309 GLU A CD  
2472 O OE1 A GLU A 309 ? 1.3699 1.9158 1.1944 -0.3158 0.1412  -0.1223 309 GLU A OE1 
2473 O OE1 B GLU A 309 ? 1.4079 1.9569 1.2300 -0.3282 0.1411  -0.1423 309 GLU A OE1 
2474 O OE2 A GLU A 309 ? 1.3663 1.8803 1.2180 -0.2868 0.1435  -0.1080 309 GLU A OE2 
2475 O OE2 B GLU A 309 ? 1.4330 1.9677 1.2494 -0.3493 0.1686  -0.1806 309 GLU A OE2 
2476 N N   . GLN A 310 ? 1.4627 1.9566 1.3358 -0.2647 0.1197  -0.0976 310 GLN A N   
2477 C CA  . GLN A 310 ? 1.3782 1.8758 1.2552 -0.2515 0.1005  -0.0724 310 GLN A CA  
2478 C C   . GLN A 310 ? 1.3021 1.7770 1.1995 -0.2304 0.0928  -0.0623 310 GLN A C   
2479 O O   . GLN A 310 ? 1.3815 1.8618 1.2791 -0.2275 0.0807  -0.0550 310 GLN A O   
2480 C CB  . GLN A 310 ? 1.3848 1.9140 1.2432 -0.2621 0.0842  -0.0598 310 GLN A CB  
2481 C CG  . GLN A 310 ? 1.3949 1.9507 1.2311 -0.2836 0.0894  -0.0666 310 GLN A CG  
2482 C CD  . GLN A 310 ? 1.4533 2.0087 1.2863 -0.2809 0.0883  -0.0553 310 GLN A CD  
2483 O OE1 . GLN A 310 ? 1.4619 2.0329 1.2848 -0.2805 0.0741  -0.0356 310 GLN A OE1 
2484 N NE2 . GLN A 310 ? 1.3962 1.9341 1.2379 -0.2788 0.1042  -0.0672 310 GLN A NE2 
2485 N N   . ALA A 311 ? 1.2559 1.7079 1.1705 -0.2159 0.0998  -0.0618 311 ALA A N   
2486 C CA  . ALA A 311 ? 1.1864 1.6177 1.1203 -0.1966 0.0937  -0.0528 311 ALA A CA  
2487 C C   . ALA A 311 ? 1.1153 1.5386 1.0594 -0.1841 0.0897  -0.0391 311 ALA A C   
2488 O O   . ALA A 311 ? 1.1586 1.5838 1.1027 -0.1870 0.0996  -0.0438 311 ALA A O   
2489 C CB  . ALA A 311 ? 1.2082 1.6184 1.1551 -0.1914 0.1093  -0.0687 311 ALA A CB  
2490 N N   . GLY A 312 ? 1.0376 1.4529 0.9902 -0.1712 0.0759  -0.0232 312 GLY A N   
2491 C CA  . GLY A 312 ? 1.0189 1.4274 0.9796 -0.1614 0.0715  -0.0103 312 GLY A CA  
2492 C C   . GLY A 312 ? 1.0072 1.4288 0.9528 -0.1686 0.0628  0.0027  312 GLY A C   
2493 O O   . GLY A 312 ? 0.9456 1.3624 0.8955 -0.1639 0.0611  0.0117  312 GLY A O   
2494 N N   . LYS A 313 ? 1.0117 1.4507 0.9394 -0.1805 0.0576  0.0044  313 LYS A N   
2495 C CA  . LYS A 313 ? 0.9589 1.4108 0.8702 -0.1873 0.0499  0.0183  313 LYS A CA  
2496 C C   . LYS A 313 ? 0.9679 1.4235 0.8735 -0.1825 0.0343  0.0353  313 LYS A C   
2497 O O   . LYS A 313 ? 0.9505 1.4086 0.8596 -0.1800 0.0303  0.0324  313 LYS A O   
2498 C CB  . LYS A 313 ? 0.9904 1.4640 0.8839 -0.2055 0.0571  0.0083  313 LYS A CB  
2499 C CG  . LYS A 313 ? 1.0753 1.5480 0.9735 -0.2120 0.0735  -0.0152 313 LYS A CG  
2500 C CD  . LYS A 313 ? 1.1097 1.6036 0.9891 -0.2316 0.0820  -0.0262 313 LYS A CD  
2501 C CE  . LYS A 313 ? 1.0091 1.5058 0.8842 -0.2350 0.0864  -0.0222 313 LYS A CE  
2502 N NZ  . LYS A 313 ? 1.0734 1.5885 0.9321 -0.2542 0.0980  -0.0363 313 LYS A NZ  
2503 N N   . THR A 314 ? 0.9277 1.3830 0.8246 -0.1809 0.0266  0.0533  314 THR A N   
2504 C CA  . THR A 314 ? 0.9602 1.4193 0.8510 -0.1751 0.0133  0.0716  314 THR A CA  
2505 C C   . THR A 314 ? 0.9402 1.4292 0.8140 -0.1870 0.0094  0.0722  314 THR A C   
2506 O O   . THR A 314 ? 0.9049 1.4107 0.7667 -0.2016 0.0162  0.0623  314 THR A O   
2507 C CB  . THR A 314 ? 0.9411 1.3880 0.8262 -0.1701 0.0086  0.0911  314 THR A CB  
2508 O OG1 . THR A 314 ? 0.9318 1.3849 0.8084 -0.1648 -0.0025 0.1101  314 THR A OG1 
2509 C CG2 . THR A 314 ? 0.9329 1.3884 0.8039 -0.1826 0.0150  0.0903  314 THR A CG2 
2510 N N   . LEU A 315 ? 0.9484 1.4465 0.8215 -0.1808 -0.0015 0.0837  315 LEU A N   
2511 C CA  . LEU A 315 ? 0.9216 1.4539 0.7797 -0.1917 -0.0067 0.0857  315 LEU A CA  
2512 C C   . LEU A 315 ? 0.9084 1.4572 0.7464 -0.2003 -0.0087 0.0988  315 LEU A C   
2513 O O   . LEU A 315 ? 0.9078 1.4877 0.7305 -0.2152 -0.0088 0.0947  315 LEU A O   
2514 C CB  . LEU A 315 ? 0.8377 1.3782 0.7009 -0.1809 -0.0187 0.0989  315 LEU A CB  
2515 C CG  . LEU A 315 ? 0.8243 1.4056 0.6751 -0.1914 -0.0252 0.1004  315 LEU A CG  
2516 C CD1 . LEU A 315 ? 0.8480 1.4418 0.6989 -0.2070 -0.0163 0.0735  315 LEU A CD1 
2517 C CD2 . LEU A 315 ? 0.8207 1.4100 0.6784 -0.1773 -0.0375 0.1178  315 LEU A CD2 
2518 N N   . GLN A 316 ? 0.8964 1.4251 0.7331 -0.1926 -0.0097 0.1142  316 GLN A N   
2519 C CA  . GLN A 316 ? 0.9239 1.4648 0.7407 -0.2008 -0.0104 0.1274  316 GLN A CA  
2520 C C   . GLN A 316 ? 0.9357 1.4840 0.7447 -0.2177 0.0012  0.1092  316 GLN A C   
2521 O O   . GLN A 316 ? 0.9210 1.4945 0.7112 -0.2314 0.0014  0.1114  316 GLN A O   
2522 C CB  . GLN A 316 ? 0.9450 1.4584 0.7620 -0.1888 -0.0125 0.1476  316 GLN A CB  
2523 C CG  . GLN A 316 ? 0.9691 1.4936 0.7645 -0.1940 -0.0152 0.1674  316 GLN A CG  
2524 C CD  . GLN A 316 ? 0.9714 1.5262 0.7565 -0.1919 -0.0259 0.1841  316 GLN A CD  
2525 O OE1 . GLN A 316 ? 0.9958 1.5464 0.7898 -0.1770 -0.0335 0.1968  316 GLN A OE1 
2526 N NE2 . GLN A 316 ? 0.9649 1.5528 0.7315 -0.2071 -0.0264 0.1843  316 GLN A NE2 
2527 N N   . GLN A 317 ? 0.9315 1.4594 0.7550 -0.2165 0.0113  0.0918  317 GLN A N   
2528 C CA  . GLN A 317 ? 0.9923 1.5273 0.8112 -0.2310 0.0241  0.0729  317 GLN A CA  
2529 C C   . GLN A 317 ? 0.9260 1.4876 0.7368 -0.2455 0.0280  0.0562  317 GLN A C   
2530 O O   . GLN A 317 ? 0.9061 1.4867 0.7015 -0.2620 0.0345  0.0483  317 GLN A O   
2531 C CB  . GLN A 317 ? 0.9829 1.4932 0.8219 -0.2239 0.0342  0.0589  317 GLN A CB  
2532 C CG  . GLN A 317 ? 0.9892 1.4824 0.8305 -0.2199 0.0366  0.0678  317 GLN A CG  
2533 C CD  . GLN A 317 ? 0.9765 1.4505 0.8395 -0.2113 0.0448  0.0559  317 GLN A CD  
2534 O OE1 . GLN A 317 ? 0.9588 1.4233 0.8374 -0.2017 0.0442  0.0494  317 GLN A OE1 
2535 N NE2 . GLN A 317 ? 0.9651 1.4356 0.8294 -0.2150 0.0526  0.0534  317 GLN A NE2 
2536 N N   . ILE A 318 ? 0.9892 1.5525 0.8095 -0.2410 0.0249  0.0497  318 ILE A N   
2537 C CA  . ILE A 318 ? 0.9965 1.5844 0.8085 -0.2567 0.0295  0.0323  318 ILE A CA  
2538 C C   . ILE A 318 ? 0.9353 1.5600 0.7252 -0.2684 0.0200  0.0448  318 ILE A C   
2539 O O   . ILE A 318 ? 0.9344 1.5846 0.7089 -0.2882 0.0262  0.0318  318 ILE A O   
2540 C CB  . ILE A 318 ? 1.0230 1.6027 0.8502 -0.2491 0.0284  0.0234  318 ILE A CB  
2541 C CG1 . ILE A 318 ? 1.0028 1.5474 0.8516 -0.2366 0.0378  0.0132  318 ILE A CG1 
2542 C CG2 . ILE A 318 ? 1.0279 1.6320 0.8454 -0.2677 0.0349  0.0037  318 ILE A CG2 
2543 C CD1 . ILE A 318 ? 1.0352 1.5683 0.8990 -0.2283 0.0374  0.0055  318 ILE A CD1 
2544 N N   . ALA A 319 ? 0.9563 1.5851 0.7443 -0.2565 0.0055  0.0707  319 ALA A N   
2545 C CA  . ALA A 319 ? 0.9360 1.6019 0.7040 -0.2649 -0.0044 0.0867  319 ALA A CA  
2546 C C   . ALA A 319 ? 0.9704 1.6463 0.7191 -0.2775 -0.0001 0.0909  319 ALA A C   
2547 O O   . ALA A 319 ? 0.9780 1.6906 0.7071 -0.2932 -0.0026 0.0928  319 ALA A O   
2548 C CB  . ALA A 319 ? 0.9069 1.5707 0.6793 -0.2458 -0.0191 0.1152  319 ALA A CB  
2549 N N   . ASP A 320 ? 0.8834 1.5296 0.6369 -0.2719 0.0065  0.0923  320 ASP A N   
2550 C CA  . ASP A 320 ? 0.9393 1.5932 0.6748 -0.2843 0.0116  0.0957  320 ASP A CA  
2551 C C   . ASP A 320 ? 0.9651 1.6290 0.6955 -0.3038 0.0265  0.0677  320 ASP A C   
2552 O O   . ASP A 320 ? 0.9708 1.6580 0.6810 -0.3207 0.0296  0.0668  320 ASP A O   
2553 C CB  . ASP A 320 ? 0.9260 1.5461 0.6678 -0.2725 0.0135  0.1077  320 ASP A CB  
2554 C CG  . ASP A 320 ? 0.9055 1.5131 0.6488 -0.2548 0.0013  0.1361  320 ASP A CG  
2555 O OD1 . ASP A 320 ? 0.8877 1.5197 0.6212 -0.2534 -0.0091 0.1520  320 ASP A OD1 
2556 O OD2 . ASP A 320 ? 0.9114 1.4859 0.6657 -0.2425 0.0029  0.1425  320 ASP A OD2 
2557 N N   . GLU A 321 ? 0.9428 1.5888 0.6908 -0.3015 0.0367  0.0452  321 GLU A N   
2558 C CA  . GLU A 321 ? 0.9863 1.6393 0.7305 -0.3189 0.0531  0.0178  321 GLU A CA  
2559 C C   . GLU A 321 ? 0.9681 1.6581 0.6943 -0.3387 0.0527  0.0082  321 GLU A C   
2560 O O   . GLU A 321 ? 0.9778 1.6861 0.6882 -0.3588 0.0629  -0.0058 321 GLU A O   
2561 C CB  . GLU A 321 ? 1.0159 1.6402 0.7836 -0.3094 0.0644  -0.0015 321 GLU A CB  
2562 C CG  . GLU A 321 ? 1.0600 1.6876 0.8258 -0.3250 0.0836  -0.0307 321 GLU A CG  
2563 C CD  . GLU A 321 ? 1.1387 1.7361 0.9285 -0.3127 0.0951  -0.0464 321 GLU A CD  
2564 O OE1 . GLU A 321 ? 1.1285 1.7021 0.9362 -0.2939 0.0915  -0.0360 321 GLU A OE1 
2565 O OE2 . GLU A 321 ? 1.1954 1.7929 0.9856 -0.3223 0.1085  -0.0688 321 GLU A OE2 
2566 N N   . TRP A 322 ? 0.9644 1.6682 0.6925 -0.3345 0.0412  0.0153  322 TRP A N   
2567 C CA  . TRP A 322 ? 0.9726 1.7170 0.6835 -0.3539 0.0389  0.0081  322 TRP A CA  
2568 C C   . TRP A 322 ? 1.0028 1.7836 0.6924 -0.3597 0.0249  0.0325  322 TRP A C   
2569 O O   . TRP A 322 ? 0.9786 1.8003 0.6508 -0.3788 0.0229  0.0275  322 TRP A O   
2570 C CB  . TRP A 322 ? 0.9680 1.7144 0.6912 -0.3478 0.0335  0.0035  322 TRP A CB  
2571 C CG  . TRP A 322 ? 0.9752 1.6932 0.7142 -0.3480 0.0495  -0.0238 322 TRP A CG  
2572 C CD1 . TRP A 322 ? 1.0203 1.7214 0.7597 -0.3574 0.0689  -0.0468 322 TRP A CD1 
2573 C CD2 . TRP A 322 ? 0.9368 1.6391 0.6933 -0.3373 0.0484  -0.0299 322 TRP A CD2 
2574 N NE1 . TRP A 322 ? 1.0363 1.7113 0.7924 -0.3523 0.0804  -0.0658 322 TRP A NE1 
2575 C CE2 . TRP A 322 ? 0.9785 1.6536 0.7447 -0.3407 0.0679  -0.0561 322 TRP A CE2 
2576 C CE3 . TRP A 322 ? 0.9186 1.6273 0.6837 -0.3249 0.0336  -0.0154 322 TRP A CE3 
2577 C CZ2 . TRP A 322 ? 1.0658 1.7189 0.8487 -0.3325 0.0727  -0.0675 322 TRP A CZ2 
2578 C CZ3 . TRP A 322 ? 0.9363 1.6246 0.7182 -0.3178 0.0380  -0.0281 322 TRP A CZ3 
2579 C CH2 . TRP A 322 ? 1.0164 1.6768 0.8065 -0.3219 0.0573  -0.0536 322 TRP A CH2 
2580 N N   . GLN A 323 ? 1.0236 1.7910 0.7137 -0.3443 0.0162  0.0587  323 GLN A N   
2581 C CA  . GLN A 323 ? 1.0612 1.8583 0.7315 -0.3466 0.0039  0.0855  323 GLN A CA  
2582 C C   . GLN A 323 ? 0.9766 1.8076 0.6450 -0.3429 -0.0110 0.1001  323 GLN A C   
2583 O O   . GLN A 323 ? 1.0054 1.8813 0.6540 -0.3562 -0.0179 0.1093  323 GLN A O   
2584 C CB  . GLN A 323 ? 0.9990 1.8238 0.6448 -0.3717 0.0117  0.0763  323 GLN A CB  
2585 C CG  . GLN A 323 ? 1.0171 1.8126 0.6655 -0.3765 0.0279  0.0599  323 GLN A CG  
2586 C CD  . GLN A 323 ? 1.0470 1.8667 0.6778 -0.4043 0.0415  0.0355  323 GLN A CD  
2587 O OE1 . GLN A 323 ? 1.1720 1.9753 0.8118 -0.4110 0.0576  0.0075  323 GLN A OE1 
2588 N NE2 . GLN A 323 ? 0.9356 1.7944 0.5408 -0.4204 0.0359  0.0464  323 GLN A NE2 
2589 N N   . VAL A 324 ? 0.9968 1.8082 0.6864 -0.3248 -0.0160 0.1022  324 VAL A N   
2590 C CA  . VAL A 324 ? 0.9868 1.8275 0.6793 -0.3190 -0.0293 0.1142  324 VAL A CA  
2591 C C   . VAL A 324 ? 0.9152 1.7245 0.6270 -0.2899 -0.0380 0.1359  324 VAL A C   
2592 O O   . VAL A 324 ? 0.8924 1.6565 0.6175 -0.2775 -0.0319 0.1336  324 VAL A O   
2593 C CB  . VAL A 324 ? 0.9631 1.8177 0.6611 -0.3331 -0.0232 0.0853  324 VAL A CB  
2594 C CG1 . VAL A 324 ? 0.9456 1.8403 0.6438 -0.3314 -0.0370 0.0969  324 VAL A CG1 
2595 C CG2 . VAL A 324 ? 0.9554 1.8309 0.6350 -0.3626 -0.0101 0.0593  324 VAL A CG2 
2596 N N   . SER A 325 ? 0.8845 1.7203 0.5974 -0.2796 -0.0519 0.1574  325 SER A N   
2597 C CA  . SER A 325 ? 0.8644 1.6740 0.5937 -0.2522 -0.0599 0.1800  325 SER A CA  
2598 C C   . SER A 325 ? 0.9185 1.6922 0.6716 -0.2425 -0.0548 0.1616  325 SER A C   
2599 O O   . SER A 325 ? 0.9394 1.7126 0.6967 -0.2560 -0.0462 0.1332  325 SER A O   
2600 C CB  . SER A 325 ? 0.8977 1.7491 0.6244 -0.2438 -0.0747 0.2048  325 SER A CB  
2601 O OG  . SER A 325 ? 0.9208 1.8021 0.6539 -0.2527 -0.0773 0.1882  325 SER A OG  
2602 N N   . LEU A 326 ? 0.9052 1.6480 0.6736 -0.2189 -0.0595 0.1787  326 LEU A N   
2603 C CA  . LEU A 326 ? 0.8770 1.5851 0.6677 -0.2082 -0.0555 0.1644  326 LEU A CA  
2604 C C   . LEU A 326 ? 0.8637 1.5977 0.6627 -0.2114 -0.0598 0.1533  326 LEU A C   
2605 O O   . LEU A 326 ? 0.8836 1.6052 0.6919 -0.2186 -0.0517 0.1278  326 LEU A O   
2606 C CB  . LEU A 326 ? 0.8777 1.5493 0.6805 -0.1838 -0.0592 0.1858  326 LEU A CB  
2607 C CG  . LEU A 326 ? 0.8826 1.5130 0.6845 -0.1799 -0.0513 0.1882  326 LEU A CG  
2608 C CD1 . LEU A 326 ? 0.9096 1.5052 0.7231 -0.1576 -0.0542 0.2075  326 LEU A CD1 
2609 C CD2 . LEU A 326 ? 0.8817 1.4909 0.6918 -0.1895 -0.0395 0.1592  326 LEU A CD2 
2610 N N   . HIS A 327 ? 0.8757 1.6460 0.6719 -0.2057 -0.0720 0.1731  327 HIS A N   
2611 C CA  . HIS A 327 ? 0.8528 1.6511 0.6573 -0.2089 -0.0767 0.1638  327 HIS A CA  
2612 C C   . HIS A 327 ? 0.8384 1.6662 0.6315 -0.2369 -0.0698 0.1358  327 HIS A C   
2613 O O   . HIS A 327 ? 0.8583 1.6889 0.6602 -0.2435 -0.0664 0.1158  327 HIS A O   
2614 C CB  . HIS A 327 ? 0.8136 1.6518 0.6168 -0.1975 -0.0912 0.1924  327 HIS A CB  
2615 C CG  . HIS A 327 ? 0.8780 1.6864 0.6975 -0.1690 -0.0963 0.2151  327 HIS A CG  
2616 N ND1 . HIS A 327 ? 0.8829 1.6579 0.7001 -0.1540 -0.0951 0.2356  327 HIS A ND1 
2617 C CD2 . HIS A 327 ? 0.8402 1.6462 0.6778 -0.1537 -0.1014 0.2195  327 HIS A CD2 
2618 C CE1 . HIS A 327 ? 0.8925 1.6447 0.7254 -0.1309 -0.0985 0.2513  327 HIS A CE1 
2619 N NE2 . HIS A 327 ? 0.8707 1.6416 0.7166 -0.1298 -0.1027 0.2421  327 HIS A NE2 
2620 N N   . ASP A 328 ? 0.8526 1.7013 0.6253 -0.2545 -0.0665 0.1334  328 ASP A N   
2621 C CA  . ASP A 328 ? 0.8867 1.7593 0.6471 -0.2829 -0.0571 0.1047  328 ASP A CA  
2622 C C   . ASP A 328 ? 0.8839 1.7114 0.6508 -0.2887 -0.0400 0.0766  328 ASP A C   
2623 O O   . ASP A 328 ? 0.9593 1.7910 0.7254 -0.3058 -0.0299 0.0493  328 ASP A O   
2624 C CB  . ASP A 328 ? 0.8775 1.7910 0.6127 -0.3008 -0.0592 0.1118  328 ASP A CB  
2625 C CG  . ASP A 328 ? 0.8664 1.8377 0.5934 -0.3004 -0.0750 0.1352  328 ASP A CG  
2626 O OD1 . ASP A 328 ? 0.8319 1.8150 0.5728 -0.2889 -0.0833 0.1422  328 ASP A OD1 
2627 O OD2 . ASP A 328 ? 0.8970 1.9038 0.6036 -0.3115 -0.0790 0.1471  328 ASP A OD2 
2628 N N   . ALA A 329 ? 0.9207 1.7059 0.6940 -0.2752 -0.0357 0.0831  329 ALA A N   
2629 C CA  . ALA A 329 ? 0.9235 1.6674 0.7065 -0.2770 -0.0201 0.0593  329 ALA A CA  
2630 C C   . ALA A 329 ? 0.9461 1.6675 0.7493 -0.2676 -0.0177 0.0473  329 ALA A C   
2631 O O   . ALA A 329 ? 0.9781 1.6854 0.7851 -0.2777 -0.0042 0.0213  329 ALA A O   
2632 C CB  . ALA A 329 ? 0.9332 1.6409 0.7204 -0.2633 -0.0178 0.0712  329 ALA A CB  
2633 N N   . ALA A 330 ? 0.9137 1.6304 0.7296 -0.2480 -0.0297 0.0662  330 ALA A N   
2634 C CA  . ALA A 330 ? 0.9015 1.6004 0.7356 -0.2396 -0.0284 0.0560  330 ALA A CA  
2635 C C   . ALA A 330 ? 0.9345 1.6668 0.7629 -0.2583 -0.0264 0.0380  330 ALA A C   
2636 O O   . ALA A 330 ? 0.9590 1.6731 0.7956 -0.2632 -0.0160 0.0160  330 ALA A O   
2637 C CB  . ALA A 330 ? 0.8429 1.5329 0.6904 -0.2157 -0.0415 0.0807  330 ALA A CB  
2638 N N   . ALA A 331 ? 0.9312 1.7133 0.7445 -0.2698 -0.0356 0.0473  331 ALA A N   
2639 C CA  . ALA A 331 ? 0.9150 1.7357 0.7219 -0.2893 -0.0350 0.0316  331 ALA A CA  
2640 C C   . ALA A 331 ? 0.9905 1.7998 0.7899 -0.3123 -0.0160 -0.0025 331 ALA A C   
2641 O O   . ALA A 331 ? 0.9842 1.7939 0.7874 -0.3222 -0.0091 -0.0223 331 ALA A O   
2642 C CB  . ALA A 331 ? 0.9250 1.8056 0.7144 -0.3000 -0.0472 0.0476  331 ALA A CB  
2643 N N   . ARG A 332 ? 0.9485 1.7462 0.7369 -0.3213 -0.0059 -0.0099 332 ARG A N   
2644 C CA  A ARG A 332 ? 0.9744 1.7573 0.7563 -0.3414 0.0146  -0.0419 332 ARG A CA  
2645 C CA  B ARG A 332 ? 0.9745 1.7570 0.7560 -0.3412 0.0146  -0.0414 332 ARG A CA  
2646 C C   . ARG A 332 ? 0.9912 1.7170 0.7916 -0.3268 0.0275  -0.0531 332 ARG A C   
2647 O O   . ARG A 332 ? 1.0776 1.7855 0.8763 -0.3398 0.0462  -0.0794 332 ARG A O   
2648 C CB  A ARG A 332 ? 0.9474 1.7477 0.7085 -0.3598 0.0213  -0.0470 332 ARG A CB  
2649 C CB  B ARG A 332 ? 0.9495 1.7457 0.7118 -0.3564 0.0205  -0.0438 332 ARG A CB  
2650 C CG  A ARG A 332 ? 0.9496 1.7369 0.7107 -0.3445 0.0149  -0.0246 332 ARG A CG  
2651 C CG  B ARG A 332 ? 0.8994 1.7523 0.6426 -0.3679 0.0062  -0.0270 332 ARG A CG  
2652 C CD  A ARG A 332 ? 0.9334 1.7362 0.6735 -0.3651 0.0242  -0.0339 332 ARG A CD  
2653 C CD  B ARG A 332 ? 0.8879 1.7481 0.6143 -0.3765 0.0092  -0.0221 332 ARG A CD  
2654 N NE  A ARG A 332 ? 0.9504 1.7264 0.6910 -0.3777 0.0467  -0.0648 332 ARG A NE  
2655 N NE  B ARG A 332 ? 0.8766 1.7898 0.5857 -0.3835 -0.0060 -0.0008 332 ARG A NE  
2656 C CZ  A ARG A 332 ? 0.9239 1.7024 0.6501 -0.3943 0.0598  -0.0781 332 ARG A CZ  
2657 C CZ  B ARG A 332 ? 0.8714 1.8005 0.5633 -0.3911 -0.0071 0.0090  332 ARG A CZ  
2658 N NH1 A ARG A 332 ? 0.9079 1.7147 0.6169 -0.4017 0.0524  -0.0639 332 ARG A NH1 
2659 N NH1 B ARG A 332 ? 0.8775 1.7747 0.5670 -0.3934 0.0062  -0.0014 332 ARG A NH1 
2660 N NH2 A ARG A 332 ? 0.9434 1.6946 0.6726 -0.4030 0.0818  -0.1059 332 ARG A NH2 
2661 N NH2 B ARG A 332 ? 0.8262 1.8057 0.5030 -0.3961 -0.0216 0.0304  332 ARG A NH2 
2662 N N   A LEU A 333 ? 0.9648 1.6625 0.7827 -0.3004 0.0189  -0.0339 333 LEU A N   
2663 N N   B LEU A 333 ? 0.9648 1.6624 0.7827 -0.3004 0.0189  -0.0340 333 LEU A N   
2664 C CA  A LEU A 333 ? 1.0203 1.6692 0.8572 -0.2854 0.0288  -0.0422 333 LEU A CA  
2665 C CA  B LEU A 333 ? 1.0203 1.6691 0.8572 -0.2855 0.0289  -0.0424 333 LEU A CA  
2666 C C   A LEU A 333 ? 1.0576 1.6966 0.9087 -0.2781 0.0270  -0.0468 333 LEU A C   
2667 C C   B LEU A 333 ? 1.0577 1.6967 0.9088 -0.2781 0.0270  -0.0468 333 LEU A C   
2668 O O   A LEU A 333 ? 1.0888 1.6921 0.9525 -0.2720 0.0390  -0.0602 333 LEU A O   
2669 O O   B LEU A 333 ? 1.0888 1.6920 0.9525 -0.2720 0.0390  -0.0602 333 LEU A O   
2670 C CB  A LEU A 333 ? 1.0167 1.6402 0.8644 -0.2629 0.0217  -0.0210 333 LEU A CB  
2671 C CB  B LEU A 333 ? 1.0168 1.6401 0.8645 -0.2630 0.0219  -0.0213 333 LEU A CB  
2672 C CG  A LEU A 333 ? 1.0373 1.6528 0.8773 -0.2665 0.0290  -0.0209 333 LEU A CG  
2673 C CG  B LEU A 333 ? 1.0377 1.6531 0.8775 -0.2666 0.0291  -0.0212 333 LEU A CG  
2674 C CD1 A LEU A 333 ? 0.9525 1.5479 0.8016 -0.2458 0.0197  0.0022  333 LEU A CD1 
2675 C CD1 B LEU A 333 ? 0.9526 1.5481 0.8016 -0.2460 0.0198  0.0020  333 LEU A CD1 
2676 C CD2 A LEU A 333 ? 1.0931 1.6822 0.9378 -0.2725 0.0496  -0.0457 333 LEU A CD2 
2677 C CD2 B LEU A 333 ? 1.0931 1.6821 0.9379 -0.2725 0.0498  -0.0459 333 LEU A CD2 
2678 N N   . MET A 334 ? 1.0103 1.6815 0.8598 -0.2782 0.0126  -0.0352 334 MET A N   
2679 C CA  . MET A 334 ? 0.9550 1.6192 0.8181 -0.2708 0.0097  -0.0379 334 MET A CA  
2680 C C   . MET A 334 ? 1.0106 1.6761 0.8682 -0.2920 0.0253  -0.0672 334 MET A C   
2681 O O   . MET A 334 ? 1.0301 1.7198 0.8697 -0.3159 0.0333  -0.0823 334 MET A O   
2682 C CB  . MET A 334 ? 0.8970 1.5994 0.7604 -0.2649 -0.0095 -0.0168 334 MET A CB  
2683 C CG  . MET A 334 ? 0.9190 1.6109 0.7910 -0.2405 -0.0230 0.0124  334 MET A CG  
2684 S SD  . MET A 334 ? 0.9339 1.6709 0.8068 -0.2312 -0.0435 0.0394  334 MET A SD  
2685 C CE  . MET A 334 ? 0.9772 1.6820 0.8597 -0.2027 -0.0517 0.0685  334 MET A CE  
2686 N N   . PRO A 335 ? 1.1477 1.7858 1.0194 -0.2846 0.0309  -0.0762 335 PRO A N   
2687 C CA  . PRO A 335 ? 1.1979 1.8049 1.0905 -0.2583 0.0237  -0.0617 335 PRO A CA  
2688 C C   . PRO A 335 ? 1.1510 1.7149 1.0530 -0.2441 0.0324  -0.0609 335 PRO A C   
2689 O O   . PRO A 335 ? 1.1050 1.6513 1.0028 -0.2535 0.0496  -0.0790 335 PRO A O   
2690 C CB  . PRO A 335 ? 1.0697 1.6683 0.9691 -0.2631 0.0303  -0.0773 335 PRO A CB  
2691 C CG  . PRO A 335 ? 1.0728 1.6722 0.9577 -0.2885 0.0497  -0.1052 335 PRO A CG  
2692 C CD  . PRO A 335 ? 1.0050 1.6439 0.8708 -0.3051 0.0457  -0.1030 335 PRO A CD  
2693 N N   . ALA A 336 ? 1.0162 1.5635 0.9309 -0.2219 0.0217  -0.0403 336 ALA A N   
2694 C CA  . ALA A 336 ? 1.0118 1.5253 0.9346 -0.2096 0.0284  -0.0378 336 ALA A CA  
2695 C C   . ALA A 336 ? 0.9774 1.4683 0.9175 -0.1865 0.0188  -0.0209 336 ALA A C   
2696 O O   . ALA A 336 ? 0.9859 1.4888 0.9300 -0.1791 0.0057  -0.0079 336 ALA A O   
2697 C CB  . ALA A 336 ? 1.0000 1.5266 0.9105 -0.2145 0.0267  -0.0299 336 ALA A CB  
2698 N N   . GLY A 337 ? 1.0127 1.4722 0.9633 -0.1755 0.0259  -0.0215 337 GLY A N   
2699 C CA  . GLY A 337 ? 0.9813 1.4187 0.9470 -0.1555 0.0184  -0.0066 337 GLY A CA  
2700 C C   . GLY A 337 ? 0.9166 1.3519 0.8795 -0.1494 0.0133  0.0085  337 GLY A C   
2701 O O   . GLY A 337 ? 0.8929 1.3286 0.8493 -0.1564 0.0214  0.0029  337 GLY A O   
2702 N N   . ALA A 338 ? 0.9198 1.3518 0.8875 -0.1367 0.0010  0.0274  338 ALA A N   
2703 C CA  . ALA A 338 ? 0.9009 1.3311 0.8636 -0.1322 -0.0040 0.0432  338 ALA A CA  
2704 C C   . ALA A 338 ? 0.9436 1.3483 0.9192 -0.1162 -0.0080 0.0545  338 ALA A C   
2705 O O   . ALA A 338 ? 0.9403 1.3361 0.9264 -0.1074 -0.0120 0.0563  338 ALA A O   
2706 C CB  . ALA A 338 ? 0.9567 1.4138 0.9059 -0.1358 -0.0148 0.0580  338 ALA A CB  
2707 N N   . ILE A 339 ? 0.8867 1.2807 0.8606 -0.1141 -0.0063 0.0613  339 ILE A N   
2708 C CA  . ILE A 339 ? 0.8835 1.2561 0.8657 -0.1021 -0.0099 0.0731  339 ILE A CA  
2709 C C   . ILE A 339 ? 0.8473 1.2244 0.8191 -0.0996 -0.0183 0.0924  339 ILE A C   
2710 O O   . ILE A 339 ? 0.8441 1.2305 0.8030 -0.1068 -0.0175 0.0975  339 ILE A O   
2711 C CB  . ILE A 339 ? 0.8620 1.2211 0.8492 -0.1024 -0.0016 0.0682  339 ILE A CB  
2712 C CG1 . ILE A 339 ? 0.8644 1.2197 0.8621 -0.1032 0.0083  0.0507  339 ILE A CG1 
2713 C CG2 . ILE A 339 ? 0.8573 1.1964 0.8520 -0.0926 -0.0050 0.0789  339 ILE A CG2 
2714 C CD1 . ILE A 339 ? 0.8577 1.2076 0.8601 -0.1041 0.0176  0.0455  339 ILE A CD1 
2715 N N   . TYR A 340 ? 0.8768 1.2467 0.8539 -0.0890 -0.0255 0.1035  340 TYR A N   
2716 C CA  . TYR A 340 ? 0.8595 1.2304 0.8281 -0.0835 -0.0322 0.1236  340 TYR A CA  
2717 C C   . TYR A 340 ? 0.8813 1.2235 0.8533 -0.0765 -0.0301 0.1321  340 TYR A C   
2718 O O   . TYR A 340 ? 0.8772 1.2019 0.8608 -0.0680 -0.0306 0.1319  340 TYR A O   
2719 C CB  . TYR A 340 ? 0.8812 1.2640 0.8538 -0.0758 -0.0401 0.1312  340 TYR A CB  
2720 C CG  . TYR A 340 ? 0.9049 1.3201 0.8729 -0.0848 -0.0425 0.1228  340 TYR A CG  
2721 C CD1 . TYR A 340 ? 0.8823 1.3254 0.8360 -0.0909 -0.0468 0.1322  340 TYR A CD1 
2722 C CD2 . TYR A 340 ? 0.9158 1.3344 0.8929 -0.0882 -0.0398 0.1057  340 TYR A CD2 
2723 C CE1 . TYR A 340 ? 0.9338 1.4097 0.8822 -0.1017 -0.0487 0.1236  340 TYR A CE1 
2724 C CE2 . TYR A 340 ? 0.9196 1.3673 0.8911 -0.0990 -0.0405 0.0964  340 TYR A CE2 
2725 C CZ  . TYR A 340 ? 0.9599 1.4376 0.9171 -0.1064 -0.0452 0.1049  340 TYR A CZ  
2726 O OH  . TYR A 340 ? 0.9830 1.4930 0.9336 -0.1195 -0.0458 0.0948  340 TYR A OH  
2727 N N   . HIS A 341 ? 0.8124 1.1501 0.7731 -0.0817 -0.0270 0.1389  341 HIS A N   
2728 C CA  . HIS A 341 ? 0.8315 1.1430 0.7917 -0.0780 -0.0240 0.1476  341 HIS A CA  
2729 C C   . HIS A 341 ? 0.7945 1.0966 0.7488 -0.0685 -0.0281 0.1677  341 HIS A C   
2730 O O   . HIS A 341 ? 0.8440 1.1351 0.7865 -0.0694 -0.0257 0.1806  341 HIS A O   
2731 C CB  . HIS A 341 ? 0.7998 1.1110 0.7499 -0.0888 -0.0179 0.1460  341 HIS A CB  
2732 C CG  . HIS A 341 ? 0.8555 1.1712 0.8141 -0.0953 -0.0119 0.1280  341 HIS A CG  
2733 N ND1 . HIS A 341 ? 0.8494 1.1497 0.8193 -0.0932 -0.0079 0.1221  341 HIS A ND1 
2734 C CD2 . HIS A 341 ? 0.8479 1.1823 0.8055 -0.1034 -0.0082 0.1152  341 HIS A CD2 
2735 C CE1 . HIS A 341 ? 0.8232 1.1335 0.7998 -0.0980 -0.0025 0.1080  341 HIS A CE1 
2736 N NE2 . HIS A 341 ? 0.8332 1.1621 0.8026 -0.1041 -0.0018 0.1031  341 HIS A NE2 
2737 N N   . ASN A 342 ? 0.7964 1.1025 0.7595 -0.0589 -0.0335 0.1702  342 ASN A N   
2738 C CA  . ASN A 342 ? 0.8110 1.1137 0.7712 -0.0474 -0.0375 0.1893  342 ASN A CA  
2739 C C   . ASN A 342 ? 0.8531 1.1222 0.8191 -0.0382 -0.0336 0.1956  342 ASN A C   
2740 O O   . ASN A 342 ? 0.8367 1.0989 0.8027 -0.0265 -0.0352 0.2109  342 ASN A O   
2741 C CB  . ASN A 342 ? 0.7973 1.1260 0.7645 -0.0421 -0.0450 0.1887  342 ASN A CB  
2742 C CG  . ASN A 342 ? 0.8453 1.1683 0.8289 -0.0396 -0.0451 0.1735  342 ASN A CG  
2743 O OD1 . ASN A 342 ? 0.8275 1.1383 0.8165 -0.0452 -0.0403 0.1591  342 ASN A OD1 
2744 N ND2 . ASN A 342 ? 0.8346 1.1680 0.8262 -0.0308 -0.0504 0.1775  342 ASN A ND2 
2745 N N   . MET A 343 ? 0.8607 1.1101 0.8316 -0.0433 -0.0279 0.1844  343 MET A N   
2746 C CA  . MET A 343 ? 0.8194 1.0380 0.7948 -0.0377 -0.0233 0.1875  343 MET A CA  
2747 C C   . MET A 343 ? 0.8722 1.0700 0.8373 -0.0464 -0.0152 0.1892  343 MET A C   
2748 O O   . MET A 343 ? 0.8675 1.0753 0.8276 -0.0575 -0.0132 0.1819  343 MET A O   
2749 C CB  . MET A 343 ? 0.8262 1.0420 0.8175 -0.0366 -0.0240 0.1723  343 MET A CB  
2750 C CG  . MET A 343 ? 0.8376 1.0655 0.8394 -0.0268 -0.0303 0.1723  343 MET A CG  
2751 S SD  . MET A 343 ? 0.8207 1.0460 0.8396 -0.0263 -0.0306 0.1547  343 MET A SD  
2752 C CE  . MET A 343 ? 0.8011 1.0496 0.8206 -0.0371 -0.0306 0.1392  343 MET A CE  
2753 N N   . ASP A 344 ? 0.9265 1.0948 0.8881 -0.0419 -0.0094 0.1985  344 ASP A N   
2754 C CA  . ASP A 344 ? 0.9275 1.0726 0.8783 -0.0514 -0.0001 0.2000  344 ASP A CA  
2755 C C   . ASP A 344 ? 0.8872 1.0213 0.8470 -0.0580 0.0037  0.1853  344 ASP A C   
2756 O O   . ASP A 344 ? 0.9228 1.0500 0.8938 -0.0513 0.0024  0.1812  344 ASP A O   
2757 C CB  . ASP A 344 ? 0.9176 1.0339 0.8575 -0.0441 0.0065  0.2183  344 ASP A CB  
2758 C CG  . ASP A 344 ? 0.9906 1.0796 0.9171 -0.0559 0.0179  0.2193  344 ASP A CG  
2759 O OD1 . ASP A 344 ? 1.0071 1.1060 0.9241 -0.0675 0.0193  0.2171  344 ASP A OD1 
2760 O OD2 . ASP A 344 ? 0.9496 1.0071 0.8744 -0.0545 0.0265  0.2217  344 ASP A OD2 
2761 N N   . GLU A 345 ? 0.8743 1.0095 0.8291 -0.0717 0.0085  0.1776  345 GLU A N   
2762 C CA  . GLU A 345 ? 0.8960 1.0284 0.8595 -0.0791 0.0115  0.1641  345 GLU A CA  
2763 C C   . GLU A 345 ? 0.8868 0.9882 0.8483 -0.0786 0.0184  0.1669  345 GLU A C   
2764 O O   . GLU A 345 ? 0.8893 0.9892 0.8614 -0.0789 0.0181  0.1576  345 GLU A O   
2765 C CB  . GLU A 345 ? 0.8797 1.0222 0.8376 -0.0939 0.0159  0.1573  345 GLU A CB  
2766 C CG  . GLU A 345 ? 0.8851 1.0295 0.8512 -0.1026 0.0193  0.1451  345 GLU A CG  
2767 C CD  . GLU A 345 ? 0.8807 1.0480 0.8650 -0.0971 0.0128  0.1342  345 GLU A CD  
2768 O OE1 . GLU A 345 ? 0.8393 1.0218 0.8287 -0.0892 0.0069  0.1339  345 GLU A OE1 
2769 O OE2 . GLU A 345 ? 0.8363 1.0068 0.8292 -0.1011 0.0142  0.1263  345 GLU A OE2 
2770 N N   . GLN A 346 ? 0.8917 0.9672 0.8388 -0.0782 0.0257  0.1796  346 GLN A N   
2771 C CA  . GLN A 346 ? 0.9057 0.9477 0.8494 -0.0779 0.0348  0.1820  346 GLN A CA  
2772 C C   . GLN A 346 ? 0.9270 0.9649 0.8828 -0.0624 0.0305  0.1842  346 GLN A C   
2773 O O   . GLN A 346 ? 0.9541 0.9746 0.9141 -0.0635 0.0354  0.1785  346 GLN A O   
2774 C CB  . GLN A 346 ? 0.9724 0.9845 0.8973 -0.0795 0.0455  0.1964  346 GLN A CB  
2775 C CG  . GLN A 346 ? 1.0502 1.0644 0.9614 -0.0961 0.0510  0.1946  346 GLN A CG  
2776 C CD  . GLN A 346 ? 1.0970 1.1118 1.0095 -0.1137 0.0563  0.1785  346 GLN A CD  
2777 O OE1 . GLN A 346 ? 1.0939 1.0877 1.0071 -0.1174 0.0632  0.1735  346 GLN A OE1 
2778 N NE2 . GLN A 346 ? 1.1106 1.1519 1.0239 -0.1250 0.0533  0.1703  346 GLN A NE2 
2779 N N   . ASP A 347 ? 0.9094 0.9651 0.8706 -0.0491 0.0216  0.1919  347 ASP A N   
2780 C CA  . ASP A 347 ? 0.8687 0.9261 0.8427 -0.0350 0.0168  0.1931  347 ASP A CA  
2781 C C   . ASP A 347 ? 0.8378 0.9095 0.8265 -0.0383 0.0117  0.1764  347 ASP A C   
2782 O O   . ASP A 347 ? 0.7904 0.8502 0.7870 -0.0336 0.0133  0.1731  347 ASP A O   
2783 C CB  . ASP A 347 ? 0.8641 0.9448 0.8406 -0.0229 0.0077  0.2036  347 ASP A CB  
2784 C CG  . ASP A 347 ? 0.9182 0.9830 0.8834 -0.0135 0.0126  0.2240  347 ASP A CG  
2785 O OD1 . ASP A 347 ? 0.9298 0.9606 0.8899 -0.0108 0.0233  0.2303  347 ASP A OD1 
2786 O OD2 . ASP A 347 ? 0.9502 1.0366 0.9112 -0.0090 0.0065  0.2341  347 ASP A OD2 
2787 N N   . VAL A 348 ? 0.8598 0.9568 0.8525 -0.0459 0.0065  0.1664  348 VAL A N   
2788 C CA  . VAL A 348 ? 0.8910 1.0015 0.8974 -0.0482 0.0027  0.1522  348 VAL A CA  
2789 C C   . VAL A 348 ? 0.8652 0.9575 0.8711 -0.0568 0.0098  0.1458  348 VAL A C   
2790 O O   . VAL A 348 ? 0.8267 0.9155 0.8420 -0.0536 0.0089  0.1401  348 VAL A O   
2791 C CB  . VAL A 348 ? 0.7969 0.9348 0.8065 -0.0544 -0.0015 0.1440  348 VAL A CB  
2792 C CG1 . VAL A 348 ? 0.7846 0.9351 0.8085 -0.0550 -0.0042 0.1314  348 VAL A CG1 
2793 C CG2 . VAL A 348 ? 0.7931 0.9495 0.8017 -0.0481 -0.0077 0.1488  348 VAL A CG2 
2794 N N   . ARG A 349 ? 0.8124 0.8936 0.8064 -0.0690 0.0175  0.1463  349 ARG A N   
2795 C CA  . ARG A 349 ? 0.8111 0.8792 0.8030 -0.0809 0.0249  0.1387  349 ARG A CA  
2796 C C   . ARG A 349 ? 0.8364 0.8749 0.8267 -0.0761 0.0311  0.1416  349 ARG A C   
2797 O O   . ARG A 349 ? 0.8866 0.9218 0.8820 -0.0812 0.0332  0.1328  349 ARG A O   
2798 C CB  . ARG A 349 ? 0.8646 0.9260 0.8421 -0.0962 0.0330  0.1391  349 ARG A CB  
2799 C CG  . ARG A 349 ? 0.8698 0.9621 0.8505 -0.1035 0.0286  0.1331  349 ARG A CG  
2800 C CD  . ARG A 349 ? 0.9114 0.9973 0.8764 -0.1165 0.0361  0.1364  349 ARG A CD  
2801 N NE  . ARG A 349 ? 0.9243 1.0412 0.8935 -0.1234 0.0328  0.1301  349 ARG A NE  
2802 C CZ  . ARG A 349 ? 0.9295 1.0595 0.8990 -0.1379 0.0367  0.1218  349 ARG A CZ  
2803 N NH1 . ARG A 349 ? 0.9260 1.0415 0.8901 -0.1495 0.0440  0.1177  349 ARG A NH1 
2804 N NH2 . ARG A 349 ? 0.9544 1.1142 0.9297 -0.1413 0.0339  0.1172  349 ARG A NH2 
2805 N N   . ARG A 350 ? 0.8302 0.8481 0.8137 -0.0660 0.0346  0.1544  350 ARG A N   
2806 C CA  . ARG A 350 ? 0.8802 0.8689 0.8632 -0.0594 0.0421  0.1579  350 ARG A CA  
2807 C C   . ARG A 350 ? 0.8092 0.8103 0.8086 -0.0491 0.0344  0.1527  350 ARG A C   
2808 O O   . ARG A 350 ? 0.7945 0.7807 0.7966 -0.0513 0.0396  0.1465  350 ARG A O   
2809 C CB  . ARG A 350 ? 0.8503 0.8180 0.8246 -0.0475 0.0473  0.1752  350 ARG A CB  
2810 C CG  . ARG A 350 ? 0.9094 0.8547 0.8650 -0.0575 0.0585  0.1818  350 ARG A CG  
2811 C CD  . ARG A 350 ? 0.9522 0.8707 0.8997 -0.0434 0.0661  0.2006  350 ARG A CD  
2812 N NE  . ARG A 350 ? 1.0040 0.9084 0.9338 -0.0503 0.0738  0.2100  350 ARG A NE  
2813 C CZ  . ARG A 350 ? 1.0176 0.9431 0.9438 -0.0466 0.0662  0.2195  350 ARG A CZ  
2814 N NH1 . ARG A 350 ? 0.9948 0.9562 0.9334 -0.0367 0.0512  0.2203  350 ARG A NH1 
2815 N NH2 . ARG A 350 ? 1.0248 0.9347 0.9335 -0.0543 0.0746  0.2279  350 ARG A NH2 
2816 N N   . VAL A 351 ? 0.8033 0.8312 0.8126 -0.0389 0.0227  0.1545  351 VAL A N   
2817 C CA  . VAL A 351 ? 0.8243 0.8650 0.8485 -0.0302 0.0156  0.1490  351 VAL A CA  
2818 C C   . VAL A 351 ? 0.8025 0.8532 0.8333 -0.0406 0.0143  0.1347  351 VAL A C   
2819 O O   . VAL A 351 ? 0.7915 0.8382 0.8299 -0.0383 0.0144  0.1292  351 VAL A O   
2820 C CB  . VAL A 351 ? 0.7660 0.8343 0.7975 -0.0204 0.0047  0.1525  351 VAL A CB  
2821 C CG1 . VAL A 351 ? 0.7286 0.8093 0.7745 -0.0131 -0.0016 0.1460  351 VAL A CG1 
2822 C CG2 . VAL A 351 ? 0.7556 0.8186 0.7805 -0.0100 0.0054  0.1684  351 VAL A CG2 
2823 N N   . MET A 352 ? 0.7801 0.8457 0.8081 -0.0517 0.0134  0.1294  352 MET A N   
2824 C CA  . MET A 352 ? 0.7483 0.8286 0.7834 -0.0603 0.0117  0.1180  352 MET A CA  
2825 C C   . MET A 352 ? 0.7434 0.8048 0.7727 -0.0713 0.0205  0.1131  352 MET A C   
2826 O O   . MET A 352 ? 0.7563 0.8238 0.7930 -0.0736 0.0192  0.1057  352 MET A O   
2827 C CB  . MET A 352 ? 0.7114 0.8143 0.7458 -0.0682 0.0094  0.1148  352 MET A CB  
2828 C CG  . MET A 352 ? 0.7799 0.9047 0.8218 -0.0593 0.0014  0.1155  352 MET A CG  
2829 S SD  . MET A 352 ? 0.7329 0.8846 0.7770 -0.0681 0.0006  0.1097  352 MET A SD  
2830 C CE  . MET A 352 ? 0.6981 0.8588 0.7512 -0.0743 0.0016  0.1013  352 MET A CE  
2831 N N   . ARG A 353 ? 0.7764 0.8140 0.7916 -0.0790 0.0304  0.1171  353 ARG A N   
2832 C CA  A ARG A 353 ? 0.7916 0.8083 0.7987 -0.0920 0.0412  0.1112  353 ARG A CA  
2833 C CA  B ARG A 353 ? 0.7868 0.8034 0.7939 -0.0919 0.0412  0.1112  353 ARG A CA  
2834 C C   . ARG A 353 ? 0.7985 0.7912 0.8079 -0.0836 0.0458  0.1121  353 ARG A C   
2835 O O   . ARG A 353 ? 0.8148 0.7909 0.8185 -0.0946 0.0550  0.1051  353 ARG A O   
2836 C CB  A ARG A 353 ? 0.8355 0.8310 0.8252 -0.1040 0.0525  0.1145  353 ARG A CB  
2837 C CB  B ARG A 353 ? 0.8358 0.8307 0.8253 -0.1037 0.0525  0.1147  353 ARG A CB  
2838 C CG  A ARG A 353 ? 0.8137 0.8327 0.7998 -0.1186 0.0510  0.1096  353 ARG A CG  
2839 C CG  B ARG A 353 ? 0.8140 0.8321 0.7999 -0.1175 0.0509  0.1107  353 ARG A CG  
2840 C CD  A ARG A 353 ? 0.8545 0.8505 0.8220 -0.1328 0.0636  0.1119  353 ARG A CD  
2841 C CD  B ARG A 353 ? 0.8539 0.8477 0.8210 -0.1308 0.0635  0.1135  353 ARG A CD  
2842 N NE  A ARG A 353 ? 0.8804 0.8644 0.8409 -0.1230 0.0641  0.1247  353 ARG A NE  
2843 N NE  B ARG A 353 ? 0.8880 0.8503 0.8447 -0.1417 0.0773  0.1086  353 ARG A NE  
2844 C CZ  A ARG A 353 ? 0.8865 0.8370 0.8390 -0.1137 0.0718  0.1351  353 ARG A CZ  
2845 C CZ  B ARG A 353 ? 0.8962 0.8640 0.8480 -0.1621 0.0832  0.0968  353 ARG A CZ  
2846 N NH1 A ARG A 353 ? 0.8834 0.8057 0.8340 -0.1127 0.0809  0.1334  353 ARG A NH1 
2847 N NH1 B ARG A 353 ? 0.8758 0.8812 0.8334 -0.1723 0.0761  0.0899  353 ARG A NH1 
2848 N NH2 A ARG A 353 ? 0.8891 0.8350 0.8355 -0.1050 0.0709  0.1480  353 ARG A NH2 
2849 N NH2 B ARG A 353 ? 0.8990 0.8351 0.8399 -0.1726 0.0972  0.0917  353 ARG A NH2 
2850 N N   . TYR A 354 ? 0.8156 0.8080 0.8329 -0.0655 0.0403  0.1198  354 TYR A N   
2851 C CA  . TYR A 354 ? 0.7839 0.7562 0.8051 -0.0563 0.0447  0.1210  354 TYR A CA  
2852 C C   . TYR A 354 ? 0.7630 0.7481 0.7938 -0.0607 0.0411  0.1094  354 TYR A C   
2853 O O   . TYR A 354 ? 0.7119 0.7262 0.7524 -0.0599 0.0305  0.1052  354 TYR A O   
2854 C CB  . TYR A 354 ? 0.7913 0.7685 0.8205 -0.0362 0.0382  0.1322  354 TYR A CB  
2855 C CG  . TYR A 354 ? 0.8259 0.7770 0.8563 -0.0249 0.0463  0.1379  354 TYR A CG  
2856 C CD1 . TYR A 354 ? 0.8448 0.7608 0.8629 -0.0257 0.0609  0.1448  354 TYR A CD1 
2857 C CD2 . TYR A 354 ? 0.8078 0.7686 0.8518 -0.0132 0.0407  0.1366  354 TYR A CD2 
2858 C CE1 . TYR A 354 ? 0.8397 0.7307 0.8598 -0.0138 0.0700  0.1507  354 TYR A CE1 
2859 C CE2 . TYR A 354 ? 0.8467 0.7854 0.8931 -0.0020 0.0487  0.1421  354 TYR A CE2 
2860 C CZ  . TYR A 354 ? 0.8657 0.7695 0.9006 -0.0016 0.0636  0.1493  354 TYR A CZ  
2861 O OH  . TYR A 354 ? 0.9046 0.7852 0.9428 0.0111  0.0733  0.1554  354 TYR A OH  
2862 N N   . PRO A 355 ? 0.7661 0.7289 0.7936 -0.0655 0.0508  0.1042  355 PRO A N   
2863 C CA  . PRO A 355 ? 0.7751 0.7511 0.8086 -0.0738 0.0484  0.0926  355 PRO A CA  
2864 C C   . PRO A 355 ? 0.7791 0.7771 0.8285 -0.0609 0.0365  0.0921  355 PRO A C   
2865 O O   . PRO A 355 ? 0.7539 0.7748 0.8094 -0.0665 0.0301  0.0853  355 PRO A O   
2866 C CB  . PRO A 355 ? 0.8024 0.7453 0.8277 -0.0802 0.0631  0.0882  355 PRO A CB  
2867 C CG  . PRO A 355 ? 0.7933 0.7066 0.8047 -0.0824 0.0752  0.0951  355 PRO A CG  
2868 C CD  . PRO A 355 ? 0.7669 0.6906 0.7831 -0.0662 0.0663  0.1081  355 PRO A CD  
2869 N N   . VAL A 356 ? 0.7702 0.7628 0.8262 -0.0440 0.0340  0.0996  356 VAL A N   
2870 C CA  . VAL A 356 ? 0.7396 0.7504 0.8095 -0.0336 0.0246  0.0978  356 VAL A CA  
2871 C C   . VAL A 356 ? 0.7321 0.7684 0.8085 -0.0260 0.0133  0.1020  356 VAL A C   
2872 O O   . VAL A 356 ? 0.7208 0.7696 0.8072 -0.0155 0.0066  0.1029  356 VAL A O   
2873 C CB  . VAL A 356 ? 0.7803 0.7742 0.8551 -0.0208 0.0290  0.1019  356 VAL A CB  
2874 C CG1 . VAL A 356 ? 0.8582 0.8262 0.9268 -0.0292 0.0416  0.0955  356 VAL A CG1 
2875 C CG2 . VAL A 356 ? 0.7957 0.7799 0.8678 -0.0086 0.0310  0.1150  356 VAL A CG2 
2876 N N   . THR A 357 ? 0.7336 0.7778 0.8038 -0.0325 0.0122  0.1038  357 THR A N   
2877 C CA  . THR A 357 ? 0.6831 0.7498 0.7575 -0.0271 0.0033  0.1067  357 THR A CA  
2878 C C   . THR A 357 ? 0.6518 0.7415 0.7333 -0.0321 -0.0024 0.0988  357 THR A C   
2879 O O   . THR A 357 ? 0.6409 0.7346 0.7192 -0.0433 0.0001  0.0942  357 THR A O   
2880 C CB  . THR A 357 ? 0.6867 0.7505 0.7508 -0.0308 0.0057  0.1131  357 THR A CB  
2881 O OG1 . THR A 357 ? 0.7059 0.7507 0.7646 -0.0225 0.0103  0.1234  357 THR A OG1 
2882 C CG2 . THR A 357 ? 0.6881 0.7771 0.7558 -0.0285 -0.0023 0.1135  357 THR A CG2 
2883 N N   . MET A 358 ? 0.6282 0.7337 0.7192 -0.0239 -0.0093 0.0976  358 MET A N   
2884 C CA  . MET A 358 ? 0.6200 0.7450 0.7183 -0.0257 -0.0134 0.0917  358 MET A CA  
2885 C C   . MET A 358 ? 0.6103 0.7507 0.7080 -0.0252 -0.0163 0.0930  358 MET A C   
2886 O O   . MET A 358 ? 0.6214 0.7598 0.7136 -0.0228 -0.0166 0.0983  358 MET A O   
2887 C CB  . MET A 358 ? 0.5955 0.7248 0.7035 -0.0183 -0.0169 0.0882  358 MET A CB  
2888 C CG  . MET A 358 ? 0.6086 0.7240 0.7175 -0.0191 -0.0138 0.0860  358 MET A CG  
2889 S SD  . MET A 358 ? 0.6539 0.7740 0.7735 -0.0108 -0.0174 0.0823  358 MET A SD  
2890 C CE  . MET A 358 ? 0.6270 0.7452 0.7474 -0.0005 -0.0193 0.0884  358 MET A CE  
2891 N N   . ILE A 359 ? 0.5780 0.7343 0.6813 -0.0271 -0.0176 0.0887  359 ILE A N   
2892 C CA  . ILE A 359 ? 0.5619 0.7328 0.6656 -0.0269 -0.0186 0.0885  359 ILE A CA  
2893 C C   . ILE A 359 ? 0.5934 0.7720 0.7043 -0.0195 -0.0212 0.0851  359 ILE A C   
2894 O O   . ILE A 359 ? 0.6127 0.7943 0.7312 -0.0168 -0.0213 0.0814  359 ILE A O   
2895 C CB  . ILE A 359 ? 0.5779 0.7622 0.6837 -0.0331 -0.0165 0.0865  359 ILE A CB  
2896 C CG1 . ILE A 359 ? 0.5800 0.7578 0.6777 -0.0433 -0.0132 0.0882  359 ILE A CG1 
2897 C CG2 . ILE A 359 ? 0.5631 0.7611 0.6693 -0.0325 -0.0160 0.0861  359 ILE A CG2 
2898 C CD1 . ILE A 359 ? 0.5997 0.7675 0.6863 -0.0470 -0.0109 0.0926  359 ILE A CD1 
2899 N N   . GLY A 360 ? 0.6215 0.8034 0.7289 -0.0172 -0.0227 0.0865  360 GLY A N   
2900 C CA  . GLY A 360 ? 0.6155 0.8060 0.7275 -0.0132 -0.0238 0.0818  360 GLY A CA  
2901 C C   . GLY A 360 ? 0.6198 0.8218 0.7282 -0.0159 -0.0223 0.0801  360 GLY A C   
2902 O O   . GLY A 360 ? 0.6820 0.8858 0.7823 -0.0184 -0.0233 0.0846  360 GLY A O   
2903 N N   . SER A 361 ? 0.6854 0.8944 0.7993 -0.0153 -0.0188 0.0739  361 SER A N   
2904 C CA  . SER A 361 ? 0.6886 0.9075 0.7991 -0.0184 -0.0154 0.0709  361 SER A CA  
2905 C C   . SER A 361 ? 0.7464 0.9711 0.8506 -0.0202 -0.0173 0.0692  361 SER A C   
2906 O O   . SER A 361 ? 0.8057 1.0376 0.9022 -0.0245 -0.0172 0.0709  361 SER A O   
2907 C CB  . SER A 361 ? 0.6875 0.9099 0.8060 -0.0159 -0.0091 0.0648  361 SER A CB  
2908 O OG  . SER A 361 ? 0.7128 0.9313 0.8348 -0.0131 -0.0076 0.0590  361 SER A OG  
2909 N N   . ASP A 362 ? 0.7013 0.9250 0.8082 -0.0179 -0.0191 0.0661  362 ASP A N   
2910 C CA  . ASP A 362 ? 0.7883 1.0230 0.8901 -0.0209 -0.0207 0.0632  362 ASP A CA  
2911 C C   . ASP A 362 ? 0.7971 1.0402 0.8952 -0.0267 -0.0145 0.0552  362 ASP A C   
2912 O O   . ASP A 362 ? 0.7852 1.0400 0.8747 -0.0320 -0.0154 0.0556  362 ASP A O   
2913 C CB  . ASP A 362 ? 0.8099 1.0494 0.9044 -0.0206 -0.0269 0.0730  362 ASP A CB  
2914 C CG  . ASP A 362 ? 0.8227 1.0784 0.9136 -0.0226 -0.0303 0.0718  362 ASP A CG  
2915 O OD1 . ASP A 362 ? 0.8266 1.0880 0.9200 -0.0259 -0.0275 0.0618  362 ASP A OD1 
2916 O OD2 . ASP A 362 ? 0.8371 1.1003 0.9222 -0.0213 -0.0352 0.0813  362 ASP A OD2 
2917 N N   . GLY A 363 ? 0.7800 1.0169 0.8844 -0.0252 -0.0072 0.0486  363 GLY A N   
2918 C CA  . GLY A 363 ? 0.7525 0.9939 0.8546 -0.0296 0.0014  0.0403  363 GLY A CA  
2919 C C   . GLY A 363 ? 0.8409 1.0860 0.9396 -0.0352 0.0055  0.0299  363 GLY A C   
2920 O O   . GLY A 363 ? 0.8768 1.1178 0.9788 -0.0340 0.0042  0.0273  363 GLY A O   
2921 N N   . LEU A 364 ? 0.9002 1.1538 0.9914 -0.0430 0.0112  0.0230  364 LEU A N   
2922 C CA  . LEU A 364 ? 0.9023 1.1618 0.9875 -0.0520 0.0167  0.0111  364 LEU A CA  
2923 C C   . LEU A 364 ? 0.9544 1.2028 1.0414 -0.0535 0.0320  0.0000  364 LEU A C   
2924 O O   . LEU A 364 ? 0.9609 1.2141 1.0429 -0.0583 0.0384  -0.0040 364 LEU A O   
2925 C CB  . LEU A 364 ? 0.9143 1.1947 0.9874 -0.0618 0.0119  0.0114  364 LEU A CB  
2926 C CG  . LEU A 364 ? 0.8822 1.1778 0.9518 -0.0614 -0.0013 0.0214  364 LEU A CG  
2927 C CD1 . LEU A 364 ? 0.8703 1.1712 0.9420 -0.0637 -0.0032 0.0162  364 LEU A CD1 
2928 C CD2 . LEU A 364 ? 0.8433 1.1307 0.9179 -0.0509 -0.0095 0.0363  364 LEU A CD2 
2929 N N   . PRO A 365 ? 0.9652 1.1977 1.0591 -0.0492 0.0393  -0.0050 365 PRO A N   
2930 C CA  . PRO A 365 ? 0.9867 1.2047 1.0839 -0.0472 0.0555  -0.0128 365 PRO A CA  
2931 C C   . PRO A 365 ? 1.0233 1.2430 1.1101 -0.0602 0.0677  -0.0281 365 PRO A C   
2932 O O   . PRO A 365 ? 0.9827 1.1996 1.0682 -0.0612 0.0789  -0.0330 365 PRO A O   
2933 C CB  . PRO A 365 ? 0.9474 1.1481 1.0532 -0.0393 0.0589  -0.0122 365 PRO A CB  
2934 C CG  . PRO A 365 ? 0.9579 1.1657 1.0608 -0.0438 0.0479  -0.0116 365 PRO A CG  
2935 C CD  . PRO A 365 ? 0.9259 1.1521 1.0250 -0.0452 0.0338  -0.0026 365 PRO A CD  
2936 N N   . ASN A 366 ? 1.0171 1.2427 1.0964 -0.0710 0.0665  -0.0364 366 ASN A N   
2937 C CA  . ASN A 366 ? 1.0697 1.2984 1.1374 -0.0865 0.0788  -0.0527 366 ASN A CA  
2938 C C   . ASN A 366 ? 1.0789 1.3290 1.1364 -0.0958 0.0754  -0.0535 366 ASN A C   
2939 O O   . ASN A 366 ? 1.0808 1.3328 1.1284 -0.1087 0.0878  -0.0674 366 ASN A O   
2940 C CB  . ASN A 366 ? 1.0388 1.2742 1.1006 -0.0975 0.0768  -0.0610 366 ASN A CB  
2941 C CG  . ASN A 366 ? 1.0019 1.2160 1.0723 -0.0899 0.0807  -0.0610 366 ASN A CG  
2942 O OD1 . ASN A 366 ? 1.0222 1.2116 1.0980 -0.0828 0.0946  -0.0636 366 ASN A OD1 
2943 N ND2 . ASN A 366 ? 0.9670 1.1914 1.0391 -0.0906 0.0690  -0.0572 366 ASN A ND2 
2944 N N   . ASP A 367 ? 1.1350 1.3996 1.1937 -0.0903 0.0602  -0.0392 367 ASP A N   
2945 C CA  . ASP A 367 ? 1.0651 1.3502 1.1137 -0.0984 0.0558  -0.0374 367 ASP A CA  
2946 C C   . ASP A 367 ? 1.0548 1.3318 1.1025 -0.0994 0.0699  -0.0440 367 ASP A C   
2947 O O   . ASP A 367 ? 1.1243 1.3891 1.1825 -0.0868 0.0721  -0.0369 367 ASP A O   
2948 C CB  . ASP A 367 ? 1.0351 1.3297 1.0867 -0.0896 0.0391  -0.0193 367 ASP A CB  
2949 C CG  . ASP A 367 ? 1.0521 1.3697 1.0915 -0.0982 0.0325  -0.0149 367 ASP A CG  
2950 O OD1 . ASP A 367 ? 1.0736 1.3941 1.1068 -0.1046 0.0408  -0.0209 367 ASP A OD1 
2951 O OD2 . ASP A 367 ? 1.0782 1.4113 1.1143 -0.0979 0.0194  -0.0047 367 ASP A OD2 
2952 N N   . PRO A 368 ? 1.1000 1.3850 1.1356 -0.1143 0.0803  -0.0577 368 PRO A N   
2953 C CA  . PRO A 368 ? 1.0907 1.3698 1.1254 -0.1152 0.0939  -0.0636 368 PRO A CA  
2954 C C   . PRO A 368 ? 1.0934 1.3872 1.1273 -0.1115 0.0830  -0.0504 368 PRO A C   
2955 O O   . PRO A 368 ? 1.2610 1.5754 1.2857 -0.1180 0.0699  -0.0437 368 PRO A O   
2956 C CB  . PRO A 368 ? 1.1385 1.4259 1.1576 -0.1353 0.1059  -0.0821 368 PRO A CB  
2957 C CG  . PRO A 368 ? 1.1189 1.4304 1.1286 -0.1458 0.0914  -0.0800 368 PRO A CG  
2958 C CD  . PRO A 368 ? 1.1313 1.4343 1.1531 -0.1322 0.0800  -0.0686 368 PRO A CD  
2959 N N   . MET A 369 ? 1.0156 1.2994 1.0592 -0.1009 0.0891  -0.0462 369 MET A N   
2960 C CA  . MET A 369 ? 0.9986 1.2929 1.0439 -0.0959 0.0791  -0.0327 369 MET A CA  
2961 C C   . MET A 369 ? 0.9641 1.2610 1.0128 -0.0888 0.0611  -0.0176 369 MET A C   
2962 O O   . MET A 369 ? 0.9431 1.2551 0.9820 -0.0949 0.0494  -0.0111 369 MET A O   
2963 C CB  . MET A 369 ? 0.9775 1.2913 1.0074 -0.1098 0.0784  -0.0355 369 MET A CB  
2964 C CG  . MET A 369 ? 1.0167 1.3295 1.0458 -0.1134 0.0945  -0.0451 369 MET A CG  
2965 S SD  . MET A 369 ? 1.1332 1.4405 1.1784 -0.0979 0.0969  -0.0348 369 MET A SD  
2966 C CE  . MET A 369 ? 0.9691 1.2866 1.0125 -0.0945 0.0748  -0.0152 369 MET A CE  
2967 N N   . PRO A 370 ? 1.0133 1.2962 1.0756 -0.0758 0.0592  -0.0113 370 PRO A N   
2968 C CA  . PRO A 370 ? 0.9531 1.2359 1.0185 -0.0698 0.0442  0.0009  370 PRO A CA  
2969 C C   . PRO A 370 ? 0.8720 1.1596 0.9383 -0.0656 0.0353  0.0144  370 PRO A C   
2970 O O   . PRO A 370 ? 0.8343 1.1247 0.9020 -0.0653 0.0404  0.0151  370 PRO A O   
2971 C CB  . PRO A 370 ? 0.9684 1.2338 1.0470 -0.0591 0.0482  0.0002  370 PRO A CB  
2972 C CG  . PRO A 370 ? 0.9651 1.2208 1.0482 -0.0577 0.0658  -0.0103 370 PRO A CG  
2973 C CD  . PRO A 370 ? 0.9969 1.2639 1.0722 -0.0656 0.0715  -0.0146 370 PRO A CD  
2974 N N   . HIS A 371 ? 0.8028 1.0909 0.8680 -0.0629 0.0228  0.0248  371 HIS A N   
2975 C CA  . HIS A 371 ? 0.7597 1.0476 0.8250 -0.0595 0.0154  0.0373  371 HIS A CA  
2976 C C   . HIS A 371 ? 0.7943 1.0737 0.8723 -0.0513 0.0194  0.0391  371 HIS A C   
2977 O O   . HIS A 371 ? 0.8844 1.1548 0.9723 -0.0446 0.0224  0.0361  371 HIS A O   
2978 C CB  . HIS A 371 ? 0.8010 1.0866 0.8642 -0.0564 0.0039  0.0472  371 HIS A CB  
2979 C CG  . HIS A 371 ? 0.7647 1.0488 0.8232 -0.0558 -0.0023 0.0596  371 HIS A CG  
2980 N ND1 . HIS A 371 ? 0.7582 1.0333 0.8232 -0.0517 -0.0018 0.0642  371 HIS A ND1 
2981 C CD2 . HIS A 371 ? 0.8077 1.0978 0.8549 -0.0592 -0.0081 0.0687  371 HIS A CD2 
2982 C CE1 . HIS A 371 ? 0.7612 1.0343 0.8185 -0.0538 -0.0061 0.0741  371 HIS A CE1 
2983 N NE2 . HIS A 371 ? 0.7581 1.0389 0.8047 -0.0574 -0.0098 0.0778  371 HIS A NE2 
2984 N N   . PRO A 372 ? 0.9766 1.0635 0.6901 -0.0176 -0.0090 0.0487  372 PRO A N   
2985 C CA  . PRO A 372 ? 0.9630 1.0788 0.7155 -0.0099 0.0079  0.0426  372 PRO A CA  
2986 C C   . PRO A 372 ? 0.8979 1.0159 0.6985 -0.0126 -0.0013 0.0499  372 PRO A C   
2987 O O   . PRO A 372 ? 0.8932 1.0305 0.7256 -0.0057 0.0080  0.0437  372 PRO A O   
2988 C CB  . PRO A 372 ? 0.9521 1.0962 0.6964 -0.0184 0.0302  0.0515  372 PRO A CB  
2989 C CG  . PRO A 372 ? 0.9453 1.0711 0.6554 -0.0339 0.0212  0.0680  372 PRO A CG  
2990 C CD  . PRO A 372 ? 0.9587 1.0510 0.6373 -0.0292 0.0012  0.0604  372 PRO A CD  
2991 N N   . ARG A 373 ? 0.9023 1.0016 0.7086 -0.0214 -0.0193 0.0625  373 ARG A N   
2992 C CA  . ARG A 373 ? 0.8813 0.9809 0.7302 -0.0224 -0.0270 0.0675  373 ARG A CA  
2993 C C   . ARG A 373 ? 0.8974 0.9912 0.7643 -0.0113 -0.0338 0.0534  373 ARG A C   
2994 O O   . ARG A 373 ? 0.8287 0.9285 0.7302 -0.0103 -0.0342 0.0541  373 ARG A O   
2995 C CB  . ARG A 373 ? 0.8650 0.9462 0.7153 -0.0310 -0.0446 0.0826  373 ARG A CB  
2996 C CG  . ARG A 373 ? 0.9083 0.9677 0.7392 -0.0292 -0.0644 0.0798  373 ARG A CG  
2997 C CD  . ARG A 373 ? 0.9343 0.9802 0.7573 -0.0377 -0.0797 0.0971  373 ARG A CD  
2998 N NE  . ARG A 373 ? 0.9230 0.9515 0.7307 -0.0374 -0.1012 0.0958  373 ARG A NE  
2999 C CZ  . ARG A 373 ? 1.0148 1.0303 0.8081 -0.0435 -0.1182 0.1093  373 ARG A CZ  
3000 N NH1 . ARG A 373 ? 1.0241 1.0379 0.8131 -0.0497 -0.1163 0.1254  373 ARG A NH1 
3001 N NH2 . ARG A 373 ? 1.0855 1.0882 0.8679 -0.0441 -0.1391 0.1074  373 ARG A NH2 
3002 N N   . LEU A 374 ? 0.8628 0.9419 0.7036 -0.0040 -0.0397 0.0407  374 LEU A N   
3003 C CA  . LEU A 374 ? 0.8958 0.9644 0.7494 0.0051  -0.0475 0.0279  374 LEU A CA  
3004 C C   . LEU A 374 ? 0.8887 0.9763 0.7641 0.0154  -0.0325 0.0188  374 LEU A C   
3005 O O   . LEU A 374 ? 0.8829 0.9653 0.7803 0.0203  -0.0384 0.0136  374 LEU A O   
3006 C CB  . LEU A 374 ? 0.9481 0.9921 0.7632 0.0098  -0.0574 0.0157  374 LEU A CB  
3007 C CG  . LEU A 374 ? 0.9929 1.0169 0.8132 0.0164  -0.0697 0.0034  374 LEU A CG  
3008 C CD1 . LEU A 374 ? 0.9911 1.0025 0.8279 0.0058  -0.0907 0.0126  374 LEU A CD1 
3009 C CD2 . LEU A 374 ? 1.0421 1.0435 0.8189 0.0251  -0.0716 -0.0134 374 LEU A CD2 
3010 N N   . TRP A 375 ? 0.8994 1.0105 0.7699 0.0180  -0.0136 0.0180  375 TRP A N   
3011 C CA  . TRP A 375 ? 0.8914 1.0251 0.7832 0.0293  0.0001  0.0092  375 TRP A CA  
3012 C C   . TRP A 375 ? 0.8272 0.9922 0.7485 0.0214  0.0125  0.0203  375 TRP A C   
3013 O O   . TRP A 375 ? 0.8011 0.9884 0.7459 0.0294  0.0217  0.0149  375 TRP A O   
3014 C CB  . TRP A 375 ? 0.9101 1.0501 0.7740 0.0430  0.0134  -0.0054 375 TRP A CB  
3015 C CG  . TRP A 375 ? 0.9658 1.0732 0.8041 0.0548  0.0019  -0.0212 375 TRP A CG  
3016 C CD1 . TRP A 375 ? 1.0459 1.1220 0.8476 0.0501  -0.0118 -0.0233 375 TRP A CD1 
3017 C CD2 . TRP A 375 ? 0.9666 1.0665 0.8124 0.0727  0.0012  -0.0368 375 TRP A CD2 
3018 N NE1 . TRP A 375 ? 1.0630 1.1112 0.8478 0.0624  -0.0208 -0.0398 375 TRP A NE1 
3019 C CE2 . TRP A 375 ? 1.0459 1.1064 0.8566 0.0771  -0.0129 -0.0483 375 TRP A CE2 
3020 C CE3 . TRP A 375 ? 0.9270 1.0480 0.8050 0.0851  0.0093  -0.0417 375 TRP A CE3 
3021 C CZ2 . TRP A 375 ? 1.0319 1.0699 0.8370 0.0935  -0.0186 -0.0645 375 TRP A CZ2 
3022 C CZ3 . TRP A 375 ? 0.9386 1.0392 0.8127 0.1029  0.0034  -0.0572 375 TRP A CZ3 
3023 C CH2 . TRP A 375 ? 0.9862 1.0440 0.8233 0.1070  -0.0101 -0.0685 375 TRP A CH2 
3024 N N   . GLY A 376 ? 0.7936 0.9595 0.7144 0.0057  0.0116  0.0360  376 GLY A N   
3025 C CA  . GLY A 376 ? 0.7622 0.9542 0.7066 -0.0040 0.0226  0.0464  376 GLY A CA  
3026 C C   . GLY A 376 ? 0.7026 0.8828 0.6524 -0.0200 0.0151  0.0630  376 GLY A C   
3027 O O   . GLY A 376 ? 0.7026 0.8979 0.6576 -0.0319 0.0240  0.0739  376 GLY A O   
3028 N N   . ALA A 377 ? 0.7181 0.8714 0.6679 -0.0203 -0.0014 0.0653  377 ALA A N   
3029 C CA  . ALA A 377 ? 0.7352 0.8754 0.6916 -0.0318 -0.0089 0.0800  377 ALA A CA  
3030 C C   . ALA A 377 ? 0.6869 0.8360 0.6741 -0.0367 -0.0052 0.0834  377 ALA A C   
3031 O O   . ALA A 377 ? 0.6534 0.8010 0.6428 -0.0485 -0.0030 0.0954  377 ALA A O   
3032 C CB  . ALA A 377 ? 0.7143 0.8296 0.6691 -0.0288 -0.0266 0.0807  377 ALA A CB  
3033 N N   . PHE A 378 ? 0.6989 0.8542 0.7071 -0.0288 -0.0055 0.0735  378 PHE A N   
3034 C CA  . PHE A 378 ? 0.6653 0.8254 0.6991 -0.0337 -0.0044 0.0758  378 PHE A CA  
3035 C C   . PHE A 378 ? 0.6194 0.8082 0.6635 -0.0391 0.0082  0.0769  378 PHE A C   
3036 O O   . PHE A 378 ? 0.5968 0.7874 0.6515 -0.0511 0.0096  0.0852  378 PHE A O   
3037 C CB  . PHE A 378 ? 0.6451 0.7978 0.6944 -0.0247 -0.0116 0.0665  378 PHE A CB  
3038 C CG  . PHE A 378 ? 0.6549 0.7843 0.7022 -0.0230 -0.0234 0.0678  378 PHE A CG  
3039 C CD1 . PHE A 378 ? 0.6403 0.7578 0.7001 -0.0281 -0.0272 0.0741  378 PHE A CD1 
3040 C CD2 . PHE A 378 ? 0.6635 0.7836 0.6969 -0.0162 -0.0307 0.0624  378 PHE A CD2 
3041 C CE1 . PHE A 378 ? 0.6368 0.7393 0.6998 -0.0254 -0.0367 0.0756  378 PHE A CE1 
3042 C CE2 . PHE A 378 ? 0.6676 0.7717 0.7037 -0.0162 -0.0423 0.0647  378 PHE A CE2 
3043 C CZ  . PHE A 378 ? 0.6536 0.7517 0.7067 -0.0203 -0.0446 0.0717  378 PHE A CZ  
3044 N N   . PRO A 379 ? 0.6346 0.8468 0.6772 -0.0306 0.0171  0.0687  379 PRO A N   
3045 C CA  . PRO A 379 ? 0.5800 0.8265 0.6362 -0.0370 0.0299  0.0718  379 PRO A CA  
3046 C C   . PRO A 379 ? 0.6336 0.8858 0.6758 -0.0536 0.0375  0.0853  379 PRO A C   
3047 O O   . PRO A 379 ? 0.6584 0.9333 0.7151 -0.0662 0.0448  0.0926  379 PRO A O   
3048 C CB  . PRO A 379 ? 0.6079 0.8763 0.6628 -0.0203 0.0384  0.0589  379 PRO A CB  
3049 C CG  . PRO A 379 ? 0.6600 0.9020 0.7094 -0.0062 0.0264  0.0482  379 PRO A CG  
3050 C CD  . PRO A 379 ? 0.6831 0.8928 0.7160 -0.0140 0.0157  0.0553  379 PRO A CD  
3051 N N   . ARG A 380 ? 0.6628 0.8938 0.6763 -0.0555 0.0345  0.0900  380 ARG A N   
3052 C CA  . ARG A 380 ? 0.6971 0.9275 0.6926 -0.0724 0.0396  0.1049  380 ARG A CA  
3053 C C   . ARG A 380 ? 0.6496 0.8625 0.6559 -0.0876 0.0324  0.1171  380 ARG A C   
3054 O O   . ARG A 380 ? 0.6463 0.8683 0.6507 -0.1049 0.0388  0.1290  380 ARG A O   
3055 C CB  . ARG A 380 ? 0.7634 0.9700 0.7239 -0.0701 0.0340  0.1076  380 ARG A CB  
3056 C CG  . ARG A 380 ? 0.7624 0.9650 0.6975 -0.0872 0.0385  0.1239  380 ARG A CG  
3057 C CD  . ARG A 380 ? 0.8075 0.9884 0.7053 -0.0835 0.0317  0.1253  380 ARG A CD  
3058 N NE  . ARG A 380 ? 0.8056 0.9779 0.6747 -0.1005 0.0339  0.1427  380 ARG A NE  
3059 C CZ  . ARG A 380 ? 0.8615 1.0569 0.7100 -0.1093 0.0507  0.1466  380 ARG A CZ  
3060 N NH1 . ARG A 380 ? 0.9271 1.1583 0.7834 -0.1008 0.0679  0.1335  380 ARG A NH1 
3061 N NH2 . ARG A 380 ? 1.0096 1.1917 0.8287 -0.1266 0.0505  0.1644  380 ARG A NH2 
3062 N N   . VAL A 381 ? 0.6316 0.8184 0.6479 -0.0818 0.0194  0.1142  381 VAL A N   
3063 C CA  . VAL A 381 ? 0.6686 0.8349 0.6933 -0.0934 0.0130  0.1229  381 VAL A CA  
3064 C C   . VAL A 381 ? 0.6414 0.8295 0.6892 -0.1019 0.0183  0.1216  381 VAL A C   
3065 O O   . VAL A 381 ? 0.6544 0.8387 0.7025 -0.1194 0.0191  0.1320  381 VAL A O   
3066 C CB  . VAL A 381 ? 0.6374 0.7741 0.6674 -0.0829 0.0002  0.1185  381 VAL A CB  
3067 C CG1 . VAL A 381 ? 0.5891 0.7022 0.6256 -0.0921 -0.0050 0.1251  381 VAL A CG1 
3068 C CG2 . VAL A 381 ? 0.6760 0.7947 0.6863 -0.0760 -0.0074 0.1214  381 VAL A CG2 
3069 N N   . LEU A 382 ? 0.6128 0.8224 0.6793 -0.0906 0.0204  0.1095  382 LEU A N   
3070 C CA  . LEU A 382 ? 0.6328 0.8639 0.7229 -0.0976 0.0224  0.1082  382 LEU A CA  
3071 C C   . LEU A 382 ? 0.6453 0.9138 0.7414 -0.1106 0.0345  0.1153  382 LEU A C   
3072 O O   . LEU A 382 ? 0.6593 0.9391 0.7698 -0.1265 0.0342  0.1215  382 LEU A O   
3073 C CB  . LEU A 382 ? 0.5979 0.8412 0.7049 -0.0808 0.0200  0.0946  382 LEU A CB  
3074 C CG  . LEU A 382 ? 0.5723 0.7841 0.6761 -0.0695 0.0094  0.0876  382 LEU A CG  
3075 C CD1 . LEU A 382 ? 0.5338 0.7580 0.6508 -0.0548 0.0072  0.0758  382 LEU A CD1 
3076 C CD2 . LEU A 382 ? 0.5698 0.7557 0.6754 -0.0798 0.0023  0.0920  382 LEU A CD2 
3077 N N   . GLY A 383 ? 0.6018 0.8907 0.6866 -0.1051 0.0453  0.1145  383 GLY A N   
3078 C CA  . GLY A 383 ? 0.5550 0.8868 0.6481 -0.1156 0.0599  0.1202  383 GLY A CA  
3079 C C   . GLY A 383 ? 0.6677 0.9935 0.7379 -0.1360 0.0657  0.1362  383 GLY A C   
3080 O O   . GLY A 383 ? 0.6751 1.0116 0.7539 -0.1580 0.0676  0.1481  383 GLY A O   
3081 N N   . HIS A 384 ? 0.6848 0.9916 0.7237 -0.1306 0.0671  0.1374  384 HIS A N   
3082 C CA  . HIS A 384 ? 0.6800 0.9816 0.6923 -0.1496 0.0730  0.1535  384 HIS A CA  
3083 C C   . HIS A 384 ? 0.7236 0.9839 0.7274 -0.1671 0.0596  0.1675  384 HIS A C   
3084 O O   . HIS A 384 ? 0.7754 1.0395 0.7750 -0.1907 0.0634  0.1824  384 HIS A O   
3085 C CB  . HIS A 384 ? 0.7247 1.0131 0.7022 -0.1387 0.0753  0.1509  384 HIS A CB  
3086 C CG  . HIS A 384 ? 0.7452 1.0204 0.6890 -0.1579 0.0784  0.1686  384 HIS A CG  
3087 N ND1 . HIS A 384 ? 0.8241 1.1327 0.7646 -0.1767 0.0952  0.1794  384 HIS A ND1 
3088 C CD2 . HIS A 384 ? 0.7664 0.9988 0.6785 -0.1617 0.0662  0.1786  384 HIS A CD2 
3089 C CE1 . HIS A 384 ? 0.8818 1.1657 0.7863 -0.1925 0.0933  0.1957  384 HIS A CE1 
3090 N NE2 . HIS A 384 ? 0.8793 1.1158 0.7659 -0.1829 0.0749  0.1955  384 HIS A NE2 
3091 N N   . TYR A 385 ? 0.7030 0.9231 0.7043 -0.1560 0.0441  0.1629  385 TYR A N   
3092 C CA  . TYR A 385 ? 0.7112 0.8871 0.7008 -0.1679 0.0314  0.1748  385 TYR A CA  
3093 C C   . TYR A 385 ? 0.7670 0.9359 0.7785 -0.1777 0.0259  0.1745  385 TYR A C   
3094 O O   . TYR A 385 ? 0.8097 0.9538 0.8117 -0.1965 0.0208  0.1871  385 TYR A O   
3095 C CB  . TYR A 385 ? 0.7505 0.8888 0.7277 -0.1507 0.0182  0.1709  385 TYR A CB  
3096 C CG  . TYR A 385 ? 0.8311 0.9618 0.7775 -0.1480 0.0180  0.1771  385 TYR A CG  
3097 C CD1 . TYR A 385 ? 0.8012 0.9108 0.7204 -0.1646 0.0156  0.1952  385 TYR A CD1 
3098 C CD2 . TYR A 385 ? 0.8100 0.9510 0.7508 -0.1301 0.0188  0.1654  385 TYR A CD2 
3099 C CE1 . TYR A 385 ? 0.8680 0.9689 0.7550 -0.1632 0.0140  0.2017  385 TYR A CE1 
3100 C CE2 . TYR A 385 ? 0.8208 0.9525 0.7294 -0.1288 0.0171  0.1706  385 TYR A CE2 
3101 C CZ  . TYR A 385 ? 0.8740 0.9866 0.7555 -0.1453 0.0147  0.1890  385 TYR A CZ  
3102 O OH  . TYR A 385 ? 0.9380 1.0398 0.7837 -0.1450 0.0115  0.1951  385 TYR A OH  
3103 N N   . SER A 386 ? 0.7148 0.9011 0.7520 -0.1661 0.0255  0.1605  386 SER A N   
3104 C CA  . SER A 386 ? 0.6472 0.8247 0.7010 -0.1757 0.0189  0.1594  386 SER A CA  
3105 C C   . SER A 386 ? 0.6516 0.8672 0.7216 -0.1962 0.0264  0.1659  386 SER A C   
3106 O O   . SER A 386 ? 0.6851 0.8850 0.7530 -0.2178 0.0211  0.1754  386 SER A O   
3107 C CB  . SER A 386 ? 0.6695 0.8474 0.7410 -0.1566 0.0138  0.1434  386 SER A CB  
3108 O OG  . SER A 386 ? 0.6443 0.8121 0.7273 -0.1663 0.0071  0.1418  386 SER A OG  
3109 N N   . ARG A 387 ? 0.6347 0.9007 0.7215 -0.1898 0.0382  0.1608  387 ARG A N   
3110 C CA  . ARG A 387 ? 0.6767 0.9884 0.7862 -0.2075 0.0460  0.1667  387 ARG A CA  
3111 C C   . ARG A 387 ? 0.7160 1.0412 0.8104 -0.2291 0.0568  0.1832  387 ARG A C   
3112 O O   . ARG A 387 ? 0.7594 1.0793 0.8533 -0.2561 0.0538  0.1965  387 ARG A O   
3113 C CB  . ARG A 387 ? 0.6171 0.9798 0.7544 -0.1890 0.0547  0.1542  387 ARG A CB  
3114 C CG  . ARG A 387 ? 0.5482 0.9683 0.7149 -0.2046 0.0642  0.1605  387 ARG A CG  
3115 C CD  . ARG A 387 ? 0.5210 0.9929 0.7134 -0.1823 0.0752  0.1484  387 ARG A CD  
3116 N NE  . ARG A 387 ? 0.5618 1.0364 0.7327 -0.1652 0.0882  0.1431  387 ARG A NE  
3117 C CZ  . ARG A 387 ? 0.5889 1.0517 0.7535 -0.1373 0.0866  0.1279  387 ARG A CZ  
3118 N NH1 . ARG A 387 ? 0.6157 1.0653 0.7949 -0.1228 0.0738  0.1173  387 ARG A NH1 
3119 N NH2 . ARG A 387 ? 0.6550 1.1175 0.7953 -0.1251 0.0976  0.1236  387 ARG A NH2 
3120 N N   . ASP A 388 ? 0.6365 0.9771 0.7154 -0.2189 0.0692  0.1826  388 ASP A N   
3121 C CA  . ASP A 388 ? 0.6856 1.0478 0.7499 -0.2393 0.0828  0.1977  388 ASP A CA  
3122 C C   . ASP A 388 ? 0.7721 1.0817 0.8021 -0.2590 0.0733  0.2145  388 ASP A C   
3123 O O   . ASP A 388 ? 0.8911 1.2040 0.9181 -0.2880 0.0751  0.2309  388 ASP A O   
3124 C CB  . ASP A 388 ? 0.6762 1.0651 0.7275 -0.2215 0.0987  0.1907  388 ASP A CB  
3125 C CG  . ASP A 388 ? 0.6648 1.1054 0.7495 -0.2010 0.1090  0.1745  388 ASP A CG  
3126 O OD1 . ASP A 388 ? 0.6202 1.0949 0.7410 -0.2088 0.1093  0.1747  388 ASP A OD1 
3127 O OD2 . ASP A 388 ? 0.7012 1.1465 0.7753 -0.1771 0.1154  0.1616  388 ASP A OD2 
3128 N N   . GLU A 389 ? 0.7761 1.0367 0.7811 -0.2440 0.0621  0.2115  389 GLU A N   
3129 C CA  . GLU A 389 ? 0.8261 1.0349 0.7982 -0.2585 0.0517  0.2274  389 GLU A CA  
3130 C C   . GLU A 389 ? 0.8021 0.9669 0.7787 -0.2675 0.0351  0.2301  389 GLU A C   
3131 O O   . GLU A 389 ? 0.8225 0.9459 0.7751 -0.2846 0.0267  0.2453  389 GLU A O   
3132 C CB  . GLU A 389 ? 0.8568 1.0346 0.8017 -0.2383 0.0456  0.2243  389 GLU A CB  
3133 C CG  . GLU A 389 ? 0.8553 1.0630 0.7809 -0.2340 0.0603  0.2247  389 GLU A CG  
3134 C CD  . GLU A 389 ? 0.9495 1.1637 0.8501 -0.2619 0.0698  0.2453  389 GLU A CD  
3135 O OE1 . GLU A 389 ? 0.9885 1.1633 0.8735 -0.2813 0.0587  0.2617  389 GLU A OE1 
3136 O OE2 . GLU A 389 ? 1.0487 1.3064 0.9440 -0.2646 0.0887  0.2452  389 GLU A OE2 
3137 N N   . GLN A 390 ? 0.8277 0.9975 0.8314 -0.2561 0.0299  0.2155  390 GLN A N   
3138 C CA  . GLN A 390 ? 0.8105 0.9400 0.8168 -0.2638 0.0156  0.2152  390 GLN A CA  
3139 C C   . GLN A 390 ? 0.7984 0.8653 0.7791 -0.2538 0.0025  0.2176  390 GLN A C   
3140 O O   . GLN A 390 ? 0.8082 0.8311 0.7726 -0.2690 -0.0073 0.2276  390 GLN A O   
3141 C CB  . GLN A 390 ? 0.8161 0.9500 0.8238 -0.2977 0.0152  0.2294  390 GLN A CB  
3142 C CG  . GLN A 390 ? 0.8443 1.0432 0.8853 -0.3077 0.0259  0.2269  390 GLN A CG  
3143 C CD  . GLN A 390 ? 1.0201 1.2252 1.0641 -0.3445 0.0240  0.2426  390 GLN A CD  
3144 O OE1 . GLN A 390 ? 0.9937 1.2149 1.0268 -0.3653 0.0331  0.2588  390 GLN A OE1 
3145 N NE2 . GLN A 390 ? 1.0773 1.2688 1.1341 -0.3544 0.0119  0.2384  390 GLN A NE2 
3146 N N   . LEU A 391 ? 0.7936 0.8567 0.7719 -0.2277 0.0016  0.2083  391 LEU A N   
3147 C CA  . LEU A 391 ? 0.8046 0.8159 0.7666 -0.2144 -0.0111 0.2092  391 LEU A CA  
3148 C C   . LEU A 391 ? 0.8588 0.8420 0.8330 -0.2061 -0.0196 0.1980  391 LEU A C   
3149 O O   . LEU A 391 ? 0.8788 0.8130 0.8392 -0.2046 -0.0300 0.2020  391 LEU A O   
3150 C CB  . LEU A 391 ? 0.7973 0.8171 0.7558 -0.1910 -0.0106 0.2029  391 LEU A CB  
3151 C CG  . LEU A 391 ? 0.8567 0.8544 0.7852 -0.1926 -0.0154 0.2172  391 LEU A CG  
3152 C CD1 . LEU A 391 ? 0.9208 0.9415 0.8323 -0.2153 -0.0047 0.2311  391 LEU A CD1 
3153 C CD2 . LEU A 391 ? 0.8858 0.8907 0.8132 -0.1693 -0.0180 0.2088  391 LEU A CD2 
3154 N N   . PHE A 392 ? 0.7779 0.7901 0.7760 -0.2000 -0.0153 0.1840  392 PHE A N   
3155 C CA  . PHE A 392 ? 0.7327 0.7217 0.7396 -0.1930 -0.0218 0.1725  392 PHE A CA  
3156 C C   . PHE A 392 ? 0.7265 0.7552 0.7564 -0.1971 -0.0169 0.1632  392 PHE A C   
3157 O O   . PHE A 392 ? 0.7157 0.7903 0.7588 -0.1950 -0.0083 0.1619  392 PHE A O   
3158 C CB  . PHE A 392 ? 0.7270 0.6992 0.7366 -0.1660 -0.0253 0.1622  392 PHE A CB  
3159 C CG  . PHE A 392 ? 0.7023 0.7014 0.7145 -0.1515 -0.0210 0.1610  392 PHE A CG  
3160 C CD1 . PHE A 392 ? 0.7237 0.7680 0.7503 -0.1484 -0.0126 0.1540  392 PHE A CD1 
3161 C CD2 . PHE A 392 ? 0.7624 0.7397 0.7619 -0.1405 -0.0268 0.1666  392 PHE A CD2 
3162 C CE1 . PHE A 392 ? 0.7087 0.7720 0.7332 -0.1353 -0.0094 0.1515  392 PHE A CE1 
3163 C CE2 . PHE A 392 ? 0.7710 0.7701 0.7696 -0.1290 -0.0248 0.1651  392 PHE A CE2 
3164 C CZ  . PHE A 392 ? 0.7188 0.7591 0.7281 -0.1268 -0.0158 0.1570  392 PHE A CZ  
3165 N N   . PRO A 393 ? 0.7471 0.7582 0.7806 -0.2023 -0.0228 0.1564  393 PRO A N   
3166 C CA  . PRO A 393 ? 0.6801 0.7273 0.7351 -0.2047 -0.0211 0.1479  393 PRO A CA  
3167 C C   . PRO A 393 ? 0.6845 0.7576 0.7544 -0.1803 -0.0167 0.1359  393 PRO A C   
3168 O O   . PRO A 393 ? 0.7191 0.7752 0.7828 -0.1620 -0.0168 0.1316  393 PRO A O   
3169 C CB  . PRO A 393 ? 0.6684 0.6780 0.7153 -0.2119 -0.0304 0.1420  393 PRO A CB  
3170 C CG  . PRO A 393 ? 0.7375 0.6968 0.7594 -0.2222 -0.0359 0.1513  393 PRO A CG  
3171 C CD  . PRO A 393 ? 0.7822 0.7375 0.7975 -0.2070 -0.0320 0.1567  393 PRO A CD  
3172 N N   . LEU A 394 ? 0.6366 0.7515 0.7274 -0.1807 -0.0139 0.1311  394 LEU A N   
3173 C CA  . LEU A 394 ? 0.6179 0.7563 0.7214 -0.1588 -0.0105 0.1205  394 LEU A CA  
3174 C C   . LEU A 394 ? 0.6254 0.7345 0.7245 -0.1447 -0.0161 0.1098  394 LEU A C   
3175 O O   . LEU A 394 ? 0.6024 0.7153 0.7042 -0.1263 -0.0144 0.1030  394 LEU A O   
3176 C CB  . LEU A 394 ? 0.5734 0.7595 0.7007 -0.1611 -0.0080 0.1180  394 LEU A CB  
3177 C CG  . LEU A 394 ? 0.5511 0.7638 0.6906 -0.1389 -0.0037 0.1086  394 LEU A CG  
3178 C CD1 . LEU A 394 ? 0.5403 0.7498 0.6667 -0.1277 0.0031  0.1098  394 LEU A CD1 
3179 C CD2 . LEU A 394 ? 0.5792 0.8422 0.7438 -0.1408 0.0000  0.1084  394 LEU A CD2 
3180 N N   . THR A 395 ? 0.6809 0.7600 0.7715 -0.1540 -0.0225 0.1081  395 THR A N   
3181 C CA  . THR A 395 ? 0.6333 0.6837 0.7168 -0.1412 -0.0253 0.0982  395 THR A CA  
3182 C C   . THR A 395 ? 0.6491 0.6752 0.7233 -0.1273 -0.0231 0.0988  395 THR A C   
3183 O O   . THR A 395 ? 0.7611 0.7870 0.8395 -0.1108 -0.0217 0.0918  395 THR A O   
3184 C CB  . THR A 395 ? 0.6614 0.6808 0.7321 -0.1545 -0.0317 0.0956  395 THR A CB  
3185 O OG1 . THR A 395 ? 0.7042 0.6938 0.7595 -0.1673 -0.0337 0.1040  395 THR A OG1 
3186 C CG2 . THR A 395 ? 0.6504 0.6966 0.7323 -0.1688 -0.0367 0.0955  395 THR A CG2 
3187 N N   . THR A 396 ? 0.6693 0.6751 0.7317 -0.1347 -0.0240 0.1084  396 THR A N   
3188 C CA  . THR A 396 ? 0.6821 0.6668 0.7375 -0.1212 -0.0241 0.1109  396 THR A CA  
3189 C C   . THR A 396 ? 0.6791 0.6930 0.7429 -0.1095 -0.0209 0.1116  396 THR A C   
3190 O O   . THR A 396 ? 0.6480 0.6557 0.7143 -0.0938 -0.0220 0.1084  396 THR A O   
3191 C CB  . THR A 396 ? 0.7124 0.6675 0.7510 -0.1328 -0.0278 0.1228  396 THR A CB  
3192 O OG1 . THR A 396 ? 0.7734 0.6966 0.8010 -0.1449 -0.0319 0.1211  396 THR A OG1 
3193 C CG2 . THR A 396 ? 0.6846 0.6156 0.7173 -0.1171 -0.0306 0.1260  396 THR A CG2 
3194 N N   . ALA A 397 ? 0.7246 0.7713 0.7928 -0.1170 -0.0170 0.1155  397 ALA A N   
3195 C CA  . ALA A 397 ? 0.6854 0.7562 0.7564 -0.1060 -0.0137 0.1147  397 ALA A CA  
3196 C C   . ALA A 397 ? 0.6562 0.7379 0.7390 -0.0904 -0.0141 0.1027  397 ALA A C   
3197 O O   . ALA A 397 ? 0.6425 0.7229 0.7242 -0.0779 -0.0157 0.1004  397 ALA A O   
3198 C CB  . ALA A 397 ? 0.6593 0.7643 0.7324 -0.1161 -0.0069 0.1195  397 ALA A CB  
3199 N N   . VAL A 398 ? 0.6618 0.7531 0.7550 -0.0923 -0.0141 0.0958  398 VAL A N   
3200 C CA  . VAL A 398 ? 0.6127 0.7098 0.7143 -0.0795 -0.0156 0.0858  398 VAL A CA  
3201 C C   . VAL A 398 ? 0.6241 0.6943 0.7226 -0.0715 -0.0181 0.0827  398 VAL A C   
3202 O O   . VAL A 398 ? 0.5756 0.6484 0.6783 -0.0602 -0.0192 0.0781  398 VAL A O   
3203 C CB  . VAL A 398 ? 0.5799 0.6907 0.6908 -0.0846 -0.0169 0.0809  398 VAL A CB  
3204 C CG1 . VAL A 398 ? 0.5968 0.7061 0.7119 -0.0731 -0.0197 0.0722  398 VAL A CG1 
3205 C CG2 . VAL A 398 ? 0.5575 0.7032 0.6782 -0.0889 -0.0137 0.0834  398 VAL A CG2 
3206 N N   . HIS A 399 ? 0.6246 0.6687 0.7159 -0.0772 -0.0188 0.0851  399 HIS A N   
3207 C CA  . HIS A 399 ? 0.6061 0.6271 0.6966 -0.0678 -0.0191 0.0814  399 HIS A CA  
3208 C C   . HIS A 399 ? 0.6365 0.6577 0.7304 -0.0567 -0.0209 0.0853  399 HIS A C   
3209 O O   . HIS A 399 ? 0.6213 0.6410 0.7233 -0.0461 -0.0208 0.0812  399 HIS A O   
3210 C CB  . HIS A 399 ? 0.6169 0.6063 0.6963 -0.0746 -0.0194 0.0827  399 HIS A CB  
3211 C CG  . HIS A 399 ? 0.6459 0.6119 0.7252 -0.0624 -0.0177 0.0786  399 HIS A CG  
3212 N ND1 . HIS A 399 ? 0.6838 0.6550 0.7704 -0.0533 -0.0139 0.0702  399 HIS A ND1 
3213 C CD2 . HIS A 399 ? 0.6441 0.5824 0.7178 -0.0573 -0.0189 0.0821  399 HIS A CD2 
3214 C CE1 . HIS A 399 ? 0.6636 0.6157 0.7515 -0.0426 -0.0111 0.0681  399 HIS A CE1 
3215 N NE2 . HIS A 399 ? 0.6787 0.6098 0.7594 -0.0435 -0.0146 0.0749  399 HIS A NE2 
3216 N N   . LYS A 400 ? 0.6308 0.6555 0.7183 -0.0602 -0.0228 0.0939  400 LYS A N   
3217 C CA  . LYS A 400 ? 0.6396 0.6626 0.7269 -0.0513 -0.0272 0.0990  400 LYS A CA  
3218 C C   . LYS A 400 ? 0.6129 0.6578 0.7062 -0.0440 -0.0287 0.0943  400 LYS A C   
3219 O O   . LYS A 400 ? 0.6189 0.6633 0.7123 -0.0373 -0.0343 0.0978  400 LYS A O   
3220 C CB  . LYS A 400 ? 0.6437 0.6605 0.7162 -0.0594 -0.0295 0.1106  400 LYS A CB  
3221 C CG  . LYS A 400 ? 0.6626 0.6481 0.7264 -0.0651 -0.0316 0.1173  400 LYS A CG  
3222 C CD  . LYS A 400 ? 0.6653 0.6433 0.7118 -0.0753 -0.0345 0.1307  400 LYS A CD  
3223 C CE  . LYS A 400 ? 0.7517 0.6908 0.7873 -0.0794 -0.0393 0.1383  400 LYS A CE  
3224 N NZ  . LYS A 400 ? 0.7634 0.6822 0.8066 -0.0616 -0.0453 0.1372  400 LYS A NZ  
3225 N N   . MET A 401 ? 0.6036 0.6654 0.7010 -0.0451 -0.0255 0.0869  401 MET A N   
3226 C CA  . MET A 401 ? 0.5671 0.6431 0.6679 -0.0379 -0.0279 0.0814  401 MET A CA  
3227 C C   . MET A 401 ? 0.5802 0.6582 0.6906 -0.0351 -0.0272 0.0732  401 MET A C   
3228 O O   . MET A 401 ? 0.5651 0.6520 0.6765 -0.0308 -0.0296 0.0682  401 MET A O   
3229 C CB  . MET A 401 ? 0.5474 0.6411 0.6398 -0.0396 -0.0257 0.0806  401 MET A CB  
3230 C CG  . MET A 401 ? 0.5834 0.6885 0.6774 -0.0482 -0.0196 0.0810  401 MET A CG  
3231 S SD  . MET A 401 ? 0.6052 0.7396 0.6969 -0.0463 -0.0142 0.0774  401 MET A SD  
3232 C CE  . MET A 401 ? 0.5510 0.6870 0.6255 -0.0537 -0.0103 0.0880  401 MET A CE  
3233 N N   . THR A 402 ? 0.6451 0.7117 0.7589 -0.0377 -0.0242 0.0717  402 THR A N   
3234 C CA  . THR A 402 ? 0.6426 0.7092 0.7608 -0.0370 -0.0230 0.0650  402 THR A CA  
3235 C C   . THR A 402 ? 0.6614 0.7136 0.7836 -0.0345 -0.0195 0.0637  402 THR A C   
3236 O O   . THR A 402 ? 0.6317 0.6867 0.7630 -0.0284 -0.0202 0.0637  402 THR A O   
3237 C CB  . THR A 402 ? 0.5615 0.6321 0.6759 -0.0443 -0.0217 0.0623  402 THR A CB  
3238 O OG1 . THR A 402 ? 0.6129 0.6731 0.7219 -0.0523 -0.0197 0.0660  402 THR A OG1 
3239 C CG2 . THR A 402 ? 0.5642 0.6547 0.6796 -0.0432 -0.0238 0.0616  402 THR A CG2 
3240 N N   . GLY A 403 ? 0.6504 0.6881 0.7660 -0.0393 -0.0156 0.0622  403 GLY A N   
3241 C CA  . GLY A 403 ? 0.6939 0.7172 0.8102 -0.0356 -0.0100 0.0584  403 GLY A CA  
3242 C C   . GLY A 403 ? 0.7281 0.7455 0.8537 -0.0261 -0.0092 0.0621  403 GLY A C   
3243 O O   . GLY A 403 ? 0.7506 0.7720 0.8875 -0.0186 -0.0053 0.0599  403 GLY A O   
3244 N N   . LEU A 404 ? 0.6315 0.6405 0.7532 -0.0266 -0.0132 0.0686  404 LEU A N   
3245 C CA  . LEU A 404 ? 0.6533 0.6556 0.7838 -0.0165 -0.0154 0.0738  404 LEU A CA  
3246 C C   . LEU A 404 ? 0.6747 0.6987 0.8214 -0.0099 -0.0199 0.0762  404 LEU A C   
3247 O O   . LEU A 404 ? 0.6632 0.6900 0.8257 0.0001  -0.0201 0.0778  404 LEU A O   
3248 C CB  . LEU A 404 ? 0.6879 0.6764 0.8071 -0.0206 -0.0211 0.0825  404 LEU A CB  
3249 C CG  . LEU A 404 ? 0.6940 0.6713 0.8193 -0.0103 -0.0267 0.0901  404 LEU A CG  
3250 C CD1 . LEU A 404 ? 0.6539 0.6076 0.7821 -0.0007 -0.0218 0.0860  404 LEU A CD1 
3251 C CD2 . LEU A 404 ? 0.6791 0.6457 0.7888 -0.0179 -0.0336 0.1008  404 LEU A CD2 
3252 N N   . SER A 405 ? 0.6368 0.6767 0.7804 -0.0153 -0.0240 0.0761  405 SER A N   
3253 C CA  . SER A 405 ? 0.6151 0.6716 0.7699 -0.0116 -0.0303 0.0778  405 SER A CA  
3254 C C   . SER A 405 ? 0.6266 0.6929 0.7942 -0.0104 -0.0259 0.0725  405 SER A C   
3255 O O   . SER A 405 ? 0.5928 0.6702 0.7778 -0.0056 -0.0284 0.0749  405 SER A O   
3256 C CB  . SER A 405 ? 0.5846 0.6494 0.7274 -0.0167 -0.0357 0.0779  405 SER A CB  
3257 O OG  . SER A 405 ? 0.5974 0.6559 0.7270 -0.0195 -0.0377 0.0836  405 SER A OG  
3258 N N   . ALA A 406 ? 0.6617 0.7251 0.8211 -0.0159 -0.0200 0.0663  406 ALA A N   
3259 C CA  . ALA A 406 ? 0.6568 0.7274 0.8235 -0.0172 -0.0154 0.0625  406 ALA A CA  
3260 C C   . ALA A 406 ? 0.6839 0.7540 0.8636 -0.0106 -0.0062 0.0615  406 ALA A C   
3261 O O   . ALA A 406 ? 0.6468 0.7317 0.8425 -0.0092 -0.0035 0.0620  406 ALA A O   
3262 C CB  . ALA A 406 ? 0.6115 0.6757 0.7628 -0.0245 -0.0126 0.0572  406 ALA A CB  
3263 N N   . ALA A 407 ? 0.6226 0.6757 0.7957 -0.0065 -0.0010 0.0599  407 ALA A N   
3264 C CA  . ALA A 407 ? 0.6241 0.6738 0.8078 0.0030  0.0090  0.0571  407 ALA A CA  
3265 C C   . ALA A 407 ? 0.6792 0.7429 0.8883 0.0141  0.0046  0.0635  407 ALA A C   
3266 O O   . ALA A 407 ? 0.6545 0.7315 0.8837 0.0223  0.0124  0.0621  407 ALA A O   
3267 C CB  . ALA A 407 ? 0.6300 0.6512 0.7959 0.0046  0.0138  0.0529  407 ALA A CB  
3268 N N   . ARG A 408 ? 0.6492 0.7119 0.8579 0.0144  -0.0078 0.0708  408 ARG A N   
3269 C CA  A ARG A 408 ? 0.6443 0.7188 0.8754 0.0245  -0.0154 0.0783  408 ARG A CA  
3270 C CA  B ARG A 408 ? 0.6482 0.7227 0.8793 0.0245  -0.0154 0.0782  408 ARG A CA  
3271 C C   . ARG A 408 ? 0.6035 0.7080 0.8572 0.0225  -0.0188 0.0804  408 ARG A C   
3272 O O   . ARG A 408 ? 0.5920 0.7145 0.8735 0.0317  -0.0176 0.0832  408 ARG A O   
3273 C CB  A ARG A 408 ? 0.7003 0.7643 0.9189 0.0226  -0.0288 0.0862  408 ARG A CB  
3274 C CB  B ARG A 408 ? 0.7089 0.7728 0.9275 0.0227  -0.0287 0.0862  408 ARG A CB  
3275 C CG  A ARG A 408 ? 0.6783 0.7550 0.9161 0.0305  -0.0412 0.0955  408 ARG A CG  
3276 C CG  B ARG A 408 ? 0.6980 0.7565 0.9297 0.0354  -0.0358 0.0941  408 ARG A CG  
3277 C CD  A ARG A 408 ? 0.6695 0.7441 0.9291 0.0469  -0.0378 0.0971  408 ARG A CD  
3278 C CD  B ARG A 408 ? 0.7178 0.7509 0.9452 0.0447  -0.0269 0.0904  408 ARG A CD  
3279 N NE  A ARG A 408 ? 0.7173 0.7586 0.9587 0.0514  -0.0342 0.0963  408 ARG A NE  
3280 N NE  B ARG A 408 ? 0.7252 0.7528 0.9691 0.0606  -0.0336 0.0973  408 ARG A NE  
3281 C CZ  A ARG A 408 ? 0.7399 0.7679 0.9925 0.0672  -0.0332 0.0978  408 ARG A CZ  
3282 C CZ  B ARG A 408 ? 0.7399 0.7826 1.0136 0.0762  -0.0284 0.0954  408 ARG A CZ  
3283 N NH1 A ARG A 408 ? 0.7538 0.8042 1.0401 0.0818  -0.0348 0.1005  408 ARG A NH1 
3284 N NH1 B ARG A 408 ? 0.7021 0.7670 0.9908 0.0763  -0.0150 0.0872  408 ARG A NH1 
3285 N NH2 A ARG A 408 ? 0.7397 0.7313 0.9703 0.0686  -0.0312 0.0968  408 ARG A NH2 
3286 N NH2 B ARG A 408 ? 0.8046 0.8411 1.0938 0.0923  -0.0366 0.1026  408 ARG A NH2 
3287 N N   . PHE A 409 ? 0.6166 0.7268 0.8595 0.0105  -0.0236 0.0794  409 PHE A N   
3288 C CA  . PHE A 409 ? 0.5790 0.7123 0.8386 0.0050  -0.0292 0.0819  409 PHE A CA  
3289 C C   . PHE A 409 ? 0.5996 0.7419 0.8634 -0.0011 -0.0173 0.0769  409 PHE A C   
3290 O O   . PHE A 409 ? 0.5432 0.7019 0.8175 -0.0092 -0.0216 0.0793  409 PHE A O   
3291 C CB  . PHE A 409 ? 0.5598 0.6892 0.8021 -0.0039 -0.0428 0.0835  409 PHE A CB  
3292 C CG  . PHE A 409 ? 0.6319 0.7557 0.8686 0.0002  -0.0551 0.0897  409 PHE A CG  
3293 C CD1 . PHE A 409 ? 0.5950 0.6996 0.8108 0.0020  -0.0536 0.0897  409 PHE A CD1 
3294 C CD2 . PHE A 409 ? 0.5925 0.7302 0.8433 0.0004  -0.0690 0.0964  409 PHE A CD2 
3295 C CE1 . PHE A 409 ? 0.5683 0.6665 0.7752 0.0040  -0.0643 0.0967  409 PHE A CE1 
3296 C CE2 . PHE A 409 ? 0.5738 0.7042 0.8149 0.0033  -0.0813 0.1028  409 PHE A CE2 
3297 C CZ  . PHE A 409 ? 0.5673 0.6773 0.7852 0.0051  -0.0783 0.1032  409 PHE A CZ  
3298 N N   . GLN A 410 ? 0.6520 0.7815 0.9047 0.0011  -0.0032 0.0704  410 GLN A N   
3299 C CA  . GLN A 410 ? 0.5853 0.7210 0.8375 -0.0045 0.0098  0.0659  410 GLN A CA  
3300 C C   . GLN A 410 ? 0.5360 0.6700 0.7732 -0.0189 0.0034  0.0661  410 GLN A C   
3301 O O   . GLN A 410 ? 0.5634 0.7123 0.8101 -0.0269 0.0054  0.0683  410 GLN A O   
3302 C CB  . GLN A 410 ? 0.5723 0.7361 0.8571 0.0010  0.0181  0.0685  410 GLN A CB  
3303 C CG  . GLN A 410 ? 0.5720 0.7361 0.8729 0.0188  0.0252  0.0673  410 GLN A CG  
3304 C CD  . GLN A 410 ? 0.6003 0.7976 0.9374 0.0264  0.0360  0.0689  410 GLN A CD  
3305 O OE1 . GLN A 410 ? 0.6321 0.8455 0.9731 0.0181  0.0476  0.0673  410 GLN A OE1 
3306 N NE2 . GLN A 410 ? 0.5638 0.7729 0.9283 0.0421  0.0321  0.0730  410 GLN A NE2 
3307 N N   . LEU A 411 ? 0.5862 0.7020 0.8004 -0.0222 -0.0044 0.0642  411 LEU A N   
3308 C CA  . LEU A 411 ? 0.6051 0.7140 0.8025 -0.0325 -0.0103 0.0630  411 LEU A CA  
3309 C C   . LEU A 411 ? 0.5736 0.6714 0.7541 -0.0372 0.0000  0.0584  411 LEU A C   
3310 O O   . LEU A 411 ? 0.5869 0.6706 0.7535 -0.0345 0.0040  0.0543  411 LEU A O   
3311 C CB  . LEU A 411 ? 0.5945 0.6925 0.7769 -0.0317 -0.0215 0.0624  411 LEU A CB  
3312 C CG  . LEU A 411 ? 0.5207 0.6259 0.7117 -0.0285 -0.0329 0.0666  411 LEU A CG  
3313 C CD1 . LEU A 411 ? 0.5226 0.6175 0.6948 -0.0278 -0.0406 0.0646  411 LEU A CD1 
3314 C CD2 . LEU A 411 ? 0.4961 0.6131 0.6996 -0.0348 -0.0401 0.0701  411 LEU A CD2 
3315 N N   . ALA A 412 ? 0.6088 0.7115 0.7886 -0.0460 0.0032  0.0597  412 ALA A N   
3316 C CA  . ALA A 412 ? 0.6218 0.7146 0.7838 -0.0513 0.0139  0.0562  412 ALA A CA  
3317 C C   . ALA A 412 ? 0.5865 0.6590 0.7227 -0.0555 0.0058  0.0538  412 ALA A C   
3318 O O   . ALA A 412 ? 0.5722 0.6406 0.7032 -0.0593 -0.0065 0.0560  412 ALA A O   
3319 C CB  . ALA A 412 ? 0.6614 0.7657 0.8282 -0.0617 0.0194  0.0603  412 ALA A CB  
3320 N N   . ASP A 413 ? 0.5847 0.6442 0.7052 -0.0542 0.0118  0.0488  413 ASP A N   
3321 C CA  . ASP A 413 ? 0.5982 0.6418 0.6960 -0.0592 0.0046  0.0470  413 ASP A CA  
3322 C C   . ASP A 413 ? 0.5967 0.6414 0.6980 -0.0554 -0.0088 0.0480  413 ASP A C   
3323 O O   . ASP A 413 ? 0.6060 0.6449 0.6970 -0.0583 -0.0184 0.0487  413 ASP A O   
3324 C CB  . ASP A 413 ? 0.6061 0.6429 0.6880 -0.0694 0.0030  0.0495  413 ASP A CB  
3325 C CG  . ASP A 413 ? 0.6419 0.6767 0.7136 -0.0744 0.0185  0.0477  413 ASP A CG  
3326 O OD1 . ASP A 413 ? 0.6776 0.7083 0.7461 -0.0694 0.0287  0.0419  413 ASP A OD1 
3327 O OD2 . ASP A 413 ? 0.6426 0.6783 0.7076 -0.0836 0.0207  0.0519  413 ASP A OD2 
3328 N N   . ARG A 414 ? 0.6357 0.6877 0.7506 -0.0483 -0.0092 0.0483  414 ARG A N   
3329 C CA  . ARG A 414 ? 0.5409 0.5960 0.6574 -0.0446 -0.0188 0.0490  414 ARG A CA  
3330 C C   . ARG A 414 ? 0.5392 0.5939 0.6586 -0.0408 -0.0156 0.0487  414 ARG A C   
3331 O O   . ARG A 414 ? 0.6315 0.6818 0.7539 -0.0389 -0.0076 0.0481  414 ARG A O   
3332 C CB  . ARG A 414 ? 0.5601 0.6231 0.6863 -0.0420 -0.0261 0.0516  414 ARG A CB  
3333 C CG  . ARG A 414 ? 0.5977 0.6563 0.7186 -0.0476 -0.0315 0.0526  414 ARG A CG  
3334 C CD  . ARG A 414 ? 0.5535 0.6146 0.6797 -0.0465 -0.0412 0.0542  414 ARG A CD  
3335 N NE  . ARG A 414 ? 0.5777 0.6306 0.6978 -0.0542 -0.0467 0.0562  414 ARG A NE  
3336 C CZ  . ARG A 414 ? 0.6018 0.6397 0.7067 -0.0549 -0.0552 0.0549  414 ARG A CZ  
3337 N NH1 . ARG A 414 ? 0.6221 0.6569 0.7201 -0.0472 -0.0585 0.0509  414 ARG A NH1 
3338 N NH2 . ARG A 414 ? 0.5944 0.6210 0.6920 -0.0636 -0.0608 0.0582  414 ARG A NH2 
3339 N N   . GLY A 415 ? 0.5414 0.6000 0.6592 -0.0396 -0.0215 0.0493  415 GLY A N   
3340 C CA  . GLY A 415 ? 0.5485 0.6062 0.6670 -0.0389 -0.0196 0.0509  415 GLY A CA  
3341 C C   . GLY A 415 ? 0.5727 0.6214 0.6813 -0.0454 -0.0175 0.0492  415 GLY A C   
3342 O O   . GLY A 415 ? 0.5815 0.6256 0.6887 -0.0472 -0.0161 0.0512  415 GLY A O   
3343 N N   . LEU A 416 ? 0.5852 0.6290 0.6846 -0.0503 -0.0186 0.0461  416 LEU A N   
3344 C CA  . LEU A 416 ? 0.6005 0.6340 0.6879 -0.0584 -0.0188 0.0442  416 LEU A CA  
3345 C C   . LEU A 416 ? 0.6376 0.6762 0.7196 -0.0626 -0.0268 0.0436  416 LEU A C   
3346 O O   . LEU A 416 ? 0.6960 0.7351 0.7762 -0.0604 -0.0292 0.0433  416 LEU A O   
3347 C CB  . LEU A 416 ? 0.6289 0.6425 0.7044 -0.0601 -0.0105 0.0401  416 LEU A CB  
3348 C CG  . LEU A 416 ? 0.6125 0.6167 0.6926 -0.0542 -0.0031 0.0400  416 LEU A CG  
3349 C CD1 . LEU A 416 ? 0.6112 0.5987 0.6806 -0.0524 0.0071  0.0341  416 LEU A CD1 
3350 C CD2 . LEU A 416 ? 0.6277 0.6235 0.7042 -0.0589 -0.0063 0.0423  416 LEU A CD2 
3351 N N   . VAL A 417 ? 0.6386 0.6809 0.7186 -0.0694 -0.0321 0.0444  417 VAL A N   
3352 C CA  . VAL A 417 ? 0.6213 0.6673 0.6962 -0.0740 -0.0415 0.0443  417 VAL A CA  
3353 C C   . VAL A 417 ? 0.6409 0.6639 0.6937 -0.0831 -0.0403 0.0411  417 VAL A C   
3354 O O   . VAL A 417 ? 0.6389 0.6519 0.6829 -0.0918 -0.0406 0.0399  417 VAL A O   
3355 C CB  . VAL A 417 ? 0.5769 0.6431 0.6638 -0.0777 -0.0482 0.0472  417 VAL A CB  
3356 C CG1 . VAL A 417 ? 0.5909 0.6630 0.6758 -0.0811 -0.0600 0.0479  417 VAL A CG1 
3357 C CG2 . VAL A 417 ? 0.5954 0.6834 0.7002 -0.0678 -0.0463 0.0491  417 VAL A CG2 
3358 N N   . LYS A 418 ? 0.6703 0.6831 0.7112 -0.0822 -0.0389 0.0397  418 LYS A N   
3359 C CA  . LYS A 418 ? 0.6793 0.6690 0.6955 -0.0894 -0.0338 0.0356  418 LYS A CA  
3360 C C   . LYS A 418 ? 0.6779 0.6618 0.6796 -0.0918 -0.0378 0.0370  418 LYS A C   
3361 O O   . LYS A 418 ? 0.6712 0.6649 0.6836 -0.0861 -0.0411 0.0406  418 LYS A O   
3362 C CB  . LYS A 418 ? 0.7231 0.7033 0.7394 -0.0842 -0.0186 0.0319  418 LYS A CB  
3363 C CG  . LYS A 418 ? 0.8773 0.8328 0.8673 -0.0893 -0.0100 0.0253  418 LYS A CG  
3364 C CD  . LYS A 418 ? 0.8145 0.7654 0.8112 -0.0799 0.0054  0.0216  418 LYS A CD  
3365 C CE  . LYS A 418 ? 0.8699 0.7953 0.8393 -0.0822 0.0164  0.0130  418 LYS A CE  
3366 N NZ  . LYS A 418 ? 0.9242 0.8480 0.9042 -0.0698 0.0320  0.0090  418 LYS A NZ  
3367 N N   . ILE A 419 ? 0.7403 0.7048 0.7142 -0.1014 -0.0384 0.0343  419 ILE A N   
3368 C CA  . ILE A 419 ? 0.7132 0.6681 0.6671 -0.1061 -0.0420 0.0368  419 ILE A CA  
3369 C C   . ILE A 419 ? 0.7102 0.6650 0.6656 -0.1021 -0.0278 0.0368  419 ILE A C   
3370 O O   . ILE A 419 ? 0.7739 0.7244 0.7277 -0.1000 -0.0121 0.0317  419 ILE A O   
3371 C CB  . ILE A 419 ? 0.7544 0.6863 0.6730 -0.1183 -0.0447 0.0333  419 ILE A CB  
3372 C CG1 . ILE A 419 ? 0.7581 0.6925 0.6787 -0.1245 -0.0591 0.0335  419 ILE A CG1 
3373 C CG2 . ILE A 419 ? 0.8052 0.7263 0.6999 -0.1248 -0.0515 0.0381  419 ILE A CG2 
3374 C CD1 . ILE A 419 ? 0.7483 0.7022 0.6870 -0.1222 -0.0773 0.0409  419 ILE A CD1 
3375 N N   . GLY A 420 ? 0.6967 0.6563 0.6561 -0.1011 -0.0338 0.0428  420 GLY A N   
3376 C CA  . GLY A 420 ? 0.8094 0.7713 0.7718 -0.1007 -0.0226 0.0448  420 GLY A CA  
3377 C C   . GLY A 420 ? 0.7589 0.7391 0.7527 -0.0911 -0.0200 0.0459  420 GLY A C   
3378 O O   . GLY A 420 ? 0.7668 0.7514 0.7665 -0.0922 -0.0164 0.0497  420 GLY A O   
3379 N N   . TYR A 421 ? 0.6348 0.6252 0.6470 -0.0834 -0.0222 0.0436  421 TYR A N   
3380 C CA  . TYR A 421 ? 0.6519 0.6577 0.6895 -0.0748 -0.0217 0.0449  421 TYR A CA  
3381 C C   . TYR A 421 ? 0.6374 0.6463 0.6803 -0.0719 -0.0355 0.0487  421 TYR A C   
3382 O O   . TYR A 421 ? 0.6691 0.6708 0.7008 -0.0739 -0.0466 0.0503  421 TYR A O   
3383 C CB  . TYR A 421 ? 0.6839 0.6969 0.7345 -0.0689 -0.0198 0.0421  421 TYR A CB  
3384 C CG  . TYR A 421 ? 0.7006 0.7111 0.7545 -0.0665 -0.0060 0.0389  421 TYR A CG  
3385 C CD1 . TYR A 421 ? 0.6872 0.6841 0.7231 -0.0710 0.0041  0.0349  421 TYR A CD1 
3386 C CD2 . TYR A 421 ? 0.6373 0.6574 0.7104 -0.0587 -0.0033 0.0397  421 TYR A CD2 
3387 C CE1 . TYR A 421 ? 0.6918 0.6855 0.7315 -0.0656 0.0173  0.0306  421 TYR A CE1 
3388 C CE2 . TYR A 421 ? 0.6312 0.6476 0.7088 -0.0540 0.0078  0.0371  421 TYR A CE2 
3389 C CZ  . TYR A 421 ? 0.6823 0.6856 0.7443 -0.0564 0.0185  0.0321  421 TYR A CZ  
3390 O OH  . TYR A 421 ? 0.6879 0.6866 0.7551 -0.0487 0.0302  0.0283  421 TYR A OH  
3391 N N   . PHE A 422 ? 0.6259 0.6441 0.6853 -0.0663 -0.0359 0.0498  422 PHE A N   
3392 C CA  . PHE A 422 ? 0.6672 0.6839 0.7290 -0.0620 -0.0484 0.0515  422 PHE A CA  
3393 C C   . PHE A 422 ? 0.6442 0.6684 0.7115 -0.0539 -0.0559 0.0491  422 PHE A C   
3394 O O   . PHE A 422 ? 0.6680 0.7022 0.7422 -0.0525 -0.0511 0.0471  422 PHE A O   
3395 C CB  . PHE A 422 ? 0.6544 0.6774 0.7295 -0.0590 -0.0478 0.0524  422 PHE A CB  
3396 C CG  . PHE A 422 ? 0.6283 0.6468 0.7008 -0.0683 -0.0445 0.0566  422 PHE A CG  
3397 C CD1 . PHE A 422 ? 0.5946 0.5972 0.6529 -0.0747 -0.0536 0.0605  422 PHE A CD1 
3398 C CD2 . PHE A 422 ? 0.6046 0.6355 0.6897 -0.0707 -0.0325 0.0574  422 PHE A CD2 
3399 C CE1 . PHE A 422 ? 0.5549 0.5549 0.6107 -0.0862 -0.0501 0.0658  422 PHE A CE1 
3400 C CE2 . PHE A 422 ? 0.6431 0.6762 0.7298 -0.0802 -0.0281 0.0621  422 PHE A CE2 
3401 C CZ  . PHE A 422 ? 0.6110 0.6290 0.6824 -0.0895 -0.0366 0.0666  422 PHE A CZ  
3402 N N   . ALA A 423 ? 0.6212 0.6405 0.6859 -0.0486 -0.0679 0.0495  423 ALA A N   
3403 C CA  . ALA A 423 ? 0.6201 0.6505 0.6925 -0.0396 -0.0747 0.0473  423 ALA A CA  
3404 C C   . ALA A 423 ? 0.5945 0.6365 0.6793 -0.0289 -0.0738 0.0437  423 ALA A C   
3405 O O   . ALA A 423 ? 0.5966 0.6370 0.6822 -0.0187 -0.0817 0.0413  423 ALA A O   
3406 C CB  . ALA A 423 ? 0.6052 0.6241 0.6683 -0.0370 -0.0886 0.0493  423 ALA A CB  
3407 N N   . ASP A 424 ? 0.5379 0.5894 0.6300 -0.0306 -0.0640 0.0433  424 ASP A N   
3408 C CA  . ASP A 424 ? 0.5858 0.6495 0.6862 -0.0225 -0.0617 0.0406  424 ASP A CA  
3409 C C   . ASP A 424 ? 0.5873 0.6698 0.6963 -0.0222 -0.0572 0.0407  424 ASP A C   
3410 O O   . ASP A 424 ? 0.6154 0.7005 0.7262 -0.0294 -0.0504 0.0430  424 ASP A O   
3411 C CB  . ASP A 424 ? 0.5813 0.6433 0.6838 -0.0255 -0.0562 0.0420  424 ASP A CB  
3412 C CG  . ASP A 424 ? 0.5902 0.6383 0.6873 -0.0270 -0.0621 0.0424  424 ASP A CG  
3413 O OD1 . ASP A 424 ? 0.6194 0.6553 0.7083 -0.0247 -0.0707 0.0412  424 ASP A OD1 
3414 O OD2 . ASP A 424 ? 0.5920 0.6412 0.6939 -0.0308 -0.0591 0.0446  424 ASP A OD2 
3415 N N   . LEU A 425 ? 0.5758 0.6714 0.6908 -0.0137 -0.0612 0.0384  425 LEU A N   
3416 C CA  . LEU A 425 ? 0.5720 0.6902 0.6983 -0.0152 -0.0580 0.0396  425 LEU A CA  
3417 C C   . LEU A 425 ? 0.5819 0.7200 0.7160 -0.0044 -0.0542 0.0364  425 LEU A C   
3418 O O   . LEU A 425 ? 0.5696 0.7017 0.6991 0.0072  -0.0572 0.0315  425 LEU A O   
3419 C CB  . LEU A 425 ? 0.5622 0.6846 0.6921 -0.0167 -0.0665 0.0409  425 LEU A CB  
3420 C CG  . LEU A 425 ? 0.5352 0.6373 0.6520 -0.0283 -0.0701 0.0437  425 LEU A CG  
3421 C CD1 . LEU A 425 ? 0.5489 0.6542 0.6668 -0.0288 -0.0818 0.0455  425 LEU A CD1 
3422 C CD2 . LEU A 425 ? 0.5379 0.6378 0.6517 -0.0405 -0.0616 0.0455  425 LEU A CD2 
3423 N N   . VAL A 426 ? 0.5186 0.6791 0.6626 -0.0091 -0.0474 0.0391  426 VAL A N   
3424 C CA  . VAL A 426 ? 0.5598 0.7455 0.7120 -0.0006 -0.0411 0.0369  426 VAL A CA  
3425 C C   . VAL A 426 ? 0.5612 0.7768 0.7313 -0.0073 -0.0389 0.0411  426 VAL A C   
3426 O O   . VAL A 426 ? 0.4924 0.7066 0.6627 -0.0226 -0.0377 0.0469  426 VAL A O   
3427 C CB  . VAL A 426 ? 0.5876 0.7704 0.7297 -0.0028 -0.0327 0.0379  426 VAL A CB  
3428 C CG1 . VAL A 426 ? 0.5830 0.7552 0.7214 -0.0178 -0.0301 0.0449  426 VAL A CG1 
3429 C CG2 . VAL A 426 ? 0.5593 0.7713 0.7075 0.0023  -0.0235 0.0370  426 VAL A CG2 
3430 N N   . LEU A 427 ? 0.5508 0.7932 0.7364 0.0045  -0.0390 0.0380  427 LEU A N   
3431 C CA  . LEU A 427 ? 0.5059 0.7845 0.7144 -0.0011 -0.0378 0.0424  427 LEU A CA  
3432 C C   . LEU A 427 ? 0.5744 0.8855 0.7919 0.0033  -0.0239 0.0419  427 LEU A C   
3433 O O   . LEU A 427 ? 0.5367 0.8582 0.7563 0.0219  -0.0199 0.0345  427 LEU A O   
3434 C CB  . LEU A 427 ? 0.4968 0.7862 0.7209 0.0100  -0.0494 0.0403  427 LEU A CB  
3435 C CG  . LEU A 427 ? 0.4625 0.7960 0.7166 0.0069  -0.0509 0.0447  427 LEU A CG  
3436 C CD1 . LEU A 427 ? 0.4736 0.8017 0.7277 -0.0153 -0.0595 0.0525  427 LEU A CD1 
3437 C CD2 . LEU A 427 ? 0.4568 0.8058 0.7286 0.0282  -0.0597 0.0402  427 LEU A CD2 
3438 N N   . PHE A 428 ? 0.5595 0.8842 0.7795 -0.0140 -0.0163 0.0496  428 PHE A N   
3439 C CA  . PHE A 428 ? 0.5801 0.9348 0.8046 -0.0137 -0.0017 0.0510  428 PHE A CA  
3440 C C   . PHE A 428 ? 0.5652 0.9570 0.8119 -0.0309 0.0020  0.0603  428 PHE A C   
3441 O O   . PHE A 428 ? 0.4951 0.8776 0.7445 -0.0482 -0.0066 0.0667  428 PHE A O   
3442 C CB  . PHE A 428 ? 0.6168 0.9461 0.8144 -0.0195 0.0051  0.0529  428 PHE A CB  
3443 C CG  . PHE A 428 ? 0.5237 0.8314 0.7120 -0.0406 0.0021  0.0622  428 PHE A CG  
3444 C CD1 . PHE A 428 ? 0.5932 0.8634 0.7696 -0.0430 -0.0075 0.0612  428 PHE A CD1 
3445 C CD2 . PHE A 428 ? 0.5236 0.8472 0.7138 -0.0577 0.0097  0.0718  428 PHE A CD2 
3446 C CE1 . PHE A 428 ? 0.5563 0.8046 0.7234 -0.0592 -0.0094 0.0680  428 PHE A CE1 
3447 C CE2 . PHE A 428 ? 0.5271 0.8248 0.7062 -0.0757 0.0058  0.0796  428 PHE A CE2 
3448 C CZ  . PHE A 428 ? 0.5138 0.7734 0.6815 -0.0750 -0.0035 0.0769  428 PHE A CZ  
3449 N N   . ASP A 429 ? 0.5585 0.9925 0.8201 -0.0265 0.0152  0.0607  429 ASP A N   
3450 C CA  . ASP A 429 ? 0.5121 0.9875 0.7965 -0.0450 0.0210  0.0709  429 ASP A CA  
3451 C C   . ASP A 429 ? 0.5305 0.9900 0.7935 -0.0667 0.0283  0.0804  429 ASP A C   
3452 O O   . ASP A 429 ? 0.5384 0.9945 0.7828 -0.0616 0.0402  0.0792  429 ASP A O   
3453 C CB  . ASP A 429 ? 0.5476 1.0788 0.8583 -0.0308 0.0344  0.0676  429 ASP A CB  
3454 C CG  . ASP A 429 ? 0.5387 1.1219 0.8803 -0.0507 0.0400  0.0790  429 ASP A CG  
3455 O OD1 . ASP A 429 ? 0.5346 1.1059 0.8735 -0.0772 0.0326  0.0896  429 ASP A OD1 
3456 O OD2 . ASP A 429 ? 0.5048 1.1414 0.8739 -0.0397 0.0521  0.0771  429 ASP A OD2 
3457 N N   . PRO A 430 ? 0.5323 0.9783 0.7941 -0.0906 0.0206  0.0900  430 PRO A N   
3458 C CA  . PRO A 430 ? 0.5496 0.9732 0.7884 -0.1101 0.0256  0.0996  430 PRO A CA  
3459 C C   . PRO A 430 ? 0.5807 1.0451 0.8276 -0.1224 0.0410  0.1087  430 PRO A C   
3460 O O   . PRO A 430 ? 0.5558 1.0011 0.7791 -0.1353 0.0466  0.1167  430 PRO A O   
3461 C CB  . PRO A 430 ? 0.5412 0.9387 0.7780 -0.1308 0.0119  0.1055  430 PRO A CB  
3462 C CG  . PRO A 430 ? 0.5042 0.9343 0.7714 -0.1300 0.0037  0.1036  430 PRO A CG  
3463 C CD  . PRO A 430 ? 0.5186 0.9634 0.7957 -0.1008 0.0055  0.0921  430 PRO A CD  
3464 N N   . GLN A 431 ? 0.5730 1.0939 0.8524 -0.1188 0.0482  0.1083  431 GLN A N   
3465 C CA  . GLN A 431 ? 0.5515 1.1182 0.8414 -0.1316 0.0653  0.1175  431 GLN A CA  
3466 C C   . GLN A 431 ? 0.5642 1.1487 0.8434 -0.1110 0.0835  0.1100  431 GLN A C   
3467 O O   . GLN A 431 ? 0.5513 1.1601 0.8241 -0.1228 0.0997  0.1180  431 GLN A O   
3468 C CB  . GLN A 431 ? 0.5287 1.1553 0.8641 -0.1400 0.0650  0.1222  431 GLN A CB  
3469 C CG  . GLN A 431 ? 0.5762 1.1923 0.9192 -0.1700 0.0496  0.1335  431 GLN A CG  
3470 C CD  . GLN A 431 ? 0.6792 1.3581 1.0697 -0.1791 0.0469  0.1388  431 GLN A CD  
3471 O OE1 . GLN A 431 ? 0.6328 1.3590 1.0542 -0.1570 0.0530  0.1317  431 GLN A OE1 
3472 N NE2 . GLN A 431 ? 0.6771 1.3561 1.0740 -0.2115 0.0368  0.1513  431 GLN A NE2 
3473 N N   . THR A 432 ? 0.5523 1.1227 0.8260 -0.0819 0.0811  0.0949  432 THR A N   
3474 C CA  . THR A 432 ? 0.5779 1.1616 0.8388 -0.0605 0.0971  0.0851  432 THR A CA  
3475 C C   . THR A 432 ? 0.6007 1.1287 0.8212 -0.0479 0.0917  0.0770  432 THR A C   
3476 O O   . THR A 432 ? 0.7238 1.2544 0.9256 -0.0322 0.1034  0.0686  432 THR A O   
3477 C CB  . THR A 432 ? 0.5318 1.1558 0.8249 -0.0339 0.1006  0.0728  432 THR A CB  
3478 O OG1 . THR A 432 ? 0.6108 1.1988 0.9027 -0.0171 0.0823  0.0631  432 THR A OG1 
3479 C CG2 . THR A 432 ? 0.5046 1.1888 0.8442 -0.0458 0.1032  0.0814  432 THR A CG2 
3480 N N   . VAL A 433 ? 0.5969 1.0761 0.8035 -0.0543 0.0747  0.0789  433 VAL A N   
3481 C CA  . VAL A 433 ? 0.6470 1.0782 0.8205 -0.0434 0.0685  0.0722  433 VAL A CA  
3482 C C   . VAL A 433 ? 0.7241 1.1455 0.8662 -0.0534 0.0782  0.0793  433 VAL A C   
3483 O O   . VAL A 433 ? 0.7469 1.1689 0.8848 -0.0761 0.0805  0.0934  433 VAL A O   
3484 C CB  . VAL A 433 ? 0.6221 1.0098 0.7916 -0.0493 0.0503  0.0740  433 VAL A CB  
3485 C CG1 . VAL A 433 ? 0.6035 0.9836 0.7741 -0.0755 0.0469  0.0882  433 VAL A CG1 
3486 C CG2 . VAL A 433 ? 0.6216 0.9655 0.7614 -0.0400 0.0439  0.0688  433 VAL A CG2 
3487 N N   . ARG A 434 ? 0.6495 1.0594 0.7669 -0.0371 0.0829  0.0698  434 ARG A N   
3488 C CA  . ARG A 434 ? 0.7151 1.1122 0.7973 -0.0453 0.0902  0.0759  434 ARG A CA  
3489 C C   . ARG A 434 ? 0.7636 1.1327 0.8170 -0.0260 0.0866  0.0630  434 ARG A C   
3490 O O   . ARG A 434 ? 0.7365 1.1065 0.7979 -0.0054 0.0842  0.0484  434 ARG A O   
3491 C CB  . ARG A 434 ? 0.7603 1.2035 0.8442 -0.0534 0.1116  0.0815  434 ARG A CB  
3492 C CG  . ARG A 434 ? 0.7851 1.2538 0.8634 -0.0304 0.1267  0.0662  434 ARG A CG  
3493 C CD  . ARG A 434 ? 0.9474 1.4609 1.0217 -0.0399 0.1505  0.0726  434 ARG A CD  
3494 N NE  . ARG A 434 ? 1.0771 1.6057 1.1338 -0.0172 0.1664  0.0569  434 ARG A NE  
3495 C CZ  . ARG A 434 ? 0.9874 1.5589 1.0721 0.0030  0.1793  0.0446  434 ARG A CZ  
3496 N NH1 . ARG A 434 ? 0.9945 1.6010 1.1284 0.0030  0.1766  0.0471  434 ARG A NH1 
3497 N NH2 . ARG A 434 ? 1.0045 1.5831 1.0665 0.0244  0.1944  0.0292  434 ARG A NH2 
3498 N N   . ASP A 435 ? 0.7414 1.0833 0.7598 -0.0339 0.0843  0.0691  435 ASP A N   
3499 C CA  . ASP A 435 ? 0.7282 1.0441 0.7141 -0.0195 0.0804  0.0582  435 ASP A CA  
3500 C C   . ASP A 435 ? 0.7921 1.1349 0.7583 -0.0117 0.1003  0.0512  435 ASP A C   
3501 O O   . ASP A 435 ? 0.8228 1.1832 0.7751 -0.0264 0.1132  0.0621  435 ASP A O   
3502 C CB  . ASP A 435 ? 0.7177 0.9940 0.6753 -0.0310 0.0671  0.0685  435 ASP A CB  
3503 C CG  . ASP A 435 ? 0.7941 1.0766 0.7376 -0.0523 0.0743  0.0862  435 ASP A CG  
3504 O OD1 . ASP A 435 ? 0.7953 1.1032 0.7622 -0.0648 0.0822  0.0948  435 ASP A OD1 
3505 O OD2 . ASP A 435 ? 0.8268 1.0873 0.7346 -0.0577 0.0708  0.0922  435 ASP A OD2 
3506 N N   . VAL A 436 ? 0.8645 1.2095 0.8284 0.0113  0.1033  0.0329  436 VAL A N   
3507 C CA  . VAL A 436 ? 0.8504 1.2174 0.7922 0.0229  0.1231  0.0227  436 VAL A CA  
3508 C C   . VAL A 436 ? 0.9097 1.2396 0.7980 0.0241  0.1187  0.0182  436 VAL A C   
3509 O O   . VAL A 436 ? 0.9378 1.2813 0.7962 0.0268  0.1360  0.0139  436 VAL A O   
3510 C CB  . VAL A 436 ? 0.8616 1.2475 0.8253 0.0496  0.1289  0.0040  436 VAL A CB  
3511 C CG1 . VAL A 436 ? 0.8903 1.3122 0.8415 0.0621  0.1548  -0.0058 436 VAL A CG1 
3512 C CG2 . VAL A 436 ? 0.8288 1.2420 0.8450 0.0481  0.1251  0.0091  436 VAL A CG2 
3513 N N   . ALA A 437 ? 0.8366 1.1218 0.7120 0.0212  0.0960  0.0197  437 ALA A N   
3514 C CA  . ALA A 437 ? 0.9269 1.1760 0.7533 0.0212  0.0876  0.0161  437 ALA A CA  
3515 C C   . ALA A 437 ? 0.9624 1.2142 0.7591 0.0015  0.0944  0.0322  437 ALA A C   
3516 O O   . ALA A 437 ? 0.9496 1.2038 0.7613 -0.0167 0.0900  0.0506  437 ALA A O   
3517 C CB  . ALA A 437 ? 0.8897 1.0975 0.7178 0.0197  0.0609  0.0172  437 ALA A CB  
3518 N N   . SER A 438 ? 0.9671 1.2152 0.7181 0.0052  0.1047  0.0252  438 SER A N   
3519 C CA  . SER A 438 ? 1.0032 1.2475 0.7152 -0.0131 0.1097  0.0399  438 SER A CA  
3520 C C   . SER A 438 ? 1.0599 1.2578 0.7230 -0.0131 0.0905  0.0368  438 SER A C   
3521 O O   . SER A 438 ? 1.1062 1.2780 0.7669 0.0003  0.0752  0.0227  438 SER A O   
3522 C CB  . SER A 438 ? 1.0484 1.3320 0.7441 -0.0117 0.1405  0.0362  438 SER A CB  
3523 O OG  . SER A 438 ? 1.0869 1.3639 0.7516 0.0094  0.1489  0.0134  438 SER A OG  
3524 N N   . PHE A 439 ? 1.0492 1.2362 0.6723 -0.0299 0.0898  0.0514  439 PHE A N   
3525 C CA  . PHE A 439 ? 1.1167 1.2620 0.6897 -0.0313 0.0709  0.0494  439 PHE A CA  
3526 C C   . PHE A 439 ? 1.1783 1.3186 0.7065 -0.0162 0.0831  0.0273  439 PHE A C   
3527 O O   . PHE A 439 ? 1.1665 1.2697 0.6615 -0.0109 0.0648  0.0172  439 PHE A O   
3528 C CB  . PHE A 439 ? 1.1102 1.2427 0.6513 -0.0535 0.0645  0.0728  439 PHE A CB  
3529 C CG  . PHE A 439 ? 1.0817 1.2033 0.6578 -0.0654 0.0451  0.0926  439 PHE A CG  
3530 C CD1 . PHE A 439 ? 1.0627 1.1511 0.6420 -0.0640 0.0158  0.0951  439 PHE A CD1 
3531 C CD2 . PHE A 439 ? 1.0614 1.2062 0.6673 -0.0780 0.0563  0.1083  439 PHE A CD2 
3532 C CE1 . PHE A 439 ? 1.0400 1.1193 0.6521 -0.0720 -0.0002 0.1119  439 PHE A CE1 
3533 C CE2 . PHE A 439 ? 1.0530 1.1831 0.6875 -0.0872 0.0388  0.1246  439 PHE A CE2 
3534 C CZ  . PHE A 439 ? 1.0134 1.1111 0.6512 -0.0827 0.0114  0.1259  439 PHE A CZ  
3535 N N   . SER A 440 ? 1.1462 1.3235 0.6731 -0.0092 0.1138  0.0191  440 SER A N   
3536 C CA  . SER A 440 ? 1.1859 1.3590 0.6710 0.0088  0.1283  -0.0045 440 SER A CA  
3537 C C   . SER A 440 ? 1.2192 1.3921 0.7349 0.0346  0.1276  -0.0276 440 SER A C   
3538 O O   . SER A 440 ? 1.2412 1.3862 0.7201 0.0505  0.1247  -0.0487 440 SER A O   
3539 C CB  . SER A 440 ? 1.2037 1.4192 0.6718 0.0062  0.1638  -0.0034 440 SER A CB  
3540 O OG  . SER A 440 ? 1.2951 1.5613 0.8235 0.0076  0.1818  0.0017  440 SER A OG  
3541 N N   . ASP A 441 ? 1.1560 1.3554 0.7351 0.0384  0.1286  -0.0237 441 ASP A N   
3542 C CA  . ASP A 441 ? 1.1303 1.3297 0.7422 0.0617  0.1262  -0.0424 441 ASP A CA  
3543 C C   . ASP A 441 ? 1.1176 1.3051 0.7757 0.0544  0.1022  -0.0314 441 ASP A C   
3544 O O   . ASP A 441 ? 1.1017 1.3213 0.8102 0.0513  0.1080  -0.0223 441 ASP A O   
3545 C CB  . ASP A 441 ? 1.1319 1.3840 0.7762 0.0768  0.1557  -0.0505 441 ASP A CB  
3546 C CG  . ASP A 441 ? 1.2029 1.4472 0.8545 0.1072  0.1574  -0.0760 441 ASP A CG  
3547 O OD1 . ASP A 441 ? 1.1658 1.4529 0.8445 0.1238  0.1804  -0.0847 441 ASP A OD1 
3548 O OD2 . ASP A 441 ? 1.4175 1.6126 1.0478 0.1142  0.1353  -0.0869 441 ASP A OD2 
3549 N N   . PRO A 442 ? 1.1944 1.3372 0.8366 0.0507  0.0750  -0.0319 442 PRO A N   
3550 C CA  . PRO A 442 ? 1.1316 1.2649 0.8143 0.0411  0.0538  -0.0191 442 PRO A CA  
3551 C C   . PRO A 442 ? 1.1378 1.2671 0.8571 0.0562  0.0465  -0.0308 442 PRO A C   
3552 O O   . PRO A 442 ? 1.1325 1.2754 0.8970 0.0514  0.0421  -0.0211 442 PRO A O   
3553 C CB  . PRO A 442 ? 1.1552 1.2471 0.8031 0.0296  0.0291  -0.0135 442 PRO A CB  
3554 C CG  . PRO A 442 ? 1.1775 1.2451 0.7725 0.0414  0.0307  -0.0332 442 PRO A CG  
3555 C CD  . PRO A 442 ? 1.1910 1.2917 0.7747 0.0519  0.0625  -0.0420 442 PRO A CD  
3556 N N   . LYS A 443 ? 1.2195 1.3264 0.9166 0.0741  0.0441  -0.0514 443 LYS A N   
3557 C CA  . LYS A 443 ? 1.2644 1.3574 0.9890 0.0872  0.0328  -0.0616 443 LYS A CA  
3558 C C   . LYS A 443 ? 1.1435 1.2732 0.9016 0.1048  0.0528  -0.0693 443 LYS A C   
3559 O O   . LYS A 443 ? 1.2305 1.3545 0.9783 0.1269  0.0596  -0.0883 443 LYS A O   
3560 C CB  . LYS A 443 ? 1.3456 1.3912 1.0292 0.0965  0.0177  -0.0790 443 LYS A CB  
3561 C CG  . LYS A 443 ? 1.2927 1.3066 0.9417 0.0785  -0.0024 -0.0712 443 LYS A CG  
3562 C CD  . LYS A 443 ? 1.3740 1.3417 1.0074 0.0803  -0.0273 -0.0815 443 LYS A CD  
3563 C CE  . LYS A 443 ? 1.4055 1.3381 0.9762 0.0870  -0.0300 -0.0993 443 LYS A CE  
3564 N NZ  . LYS A 443 ? 1.4166 1.3031 0.9738 0.0918  -0.0519 -0.1128 443 LYS A NZ  
3565 N N   . ARG A 444 ? 1.0363 1.2037 0.8364 0.0949  0.0607  -0.0539 444 ARG A N   
3566 C CA  . ARG A 444 ? 0.9749 1.1862 0.8122 0.1070  0.0790  -0.0568 444 ARG A CA  
3567 C C   . ARG A 444 ? 0.9428 1.1669 0.8293 0.0976  0.0693  -0.0436 444 ARG A C   
3568 O O   . ARG A 444 ? 0.9292 1.1498 0.8224 0.0767  0.0613  -0.0269 444 ARG A O   
3569 C CB  . ARG A 444 ? 1.0005 1.2538 0.8314 0.1009  0.1043  -0.0507 444 ARG A CB  
3570 C CG  . ARG A 444 ? 1.0228 1.3219 0.8780 0.1203  0.1275  -0.0610 444 ARG A CG  
3571 C CD  . ARG A 444 ? 1.0617 1.3775 0.8788 0.1258  0.1515  -0.0690 444 ARG A CD  
3572 N NE  . ARG A 444 ? 1.0560 1.3755 0.8490 0.0994  0.1558  -0.0512 444 ARG A NE  
3573 C CZ  . ARG A 444 ? 1.0290 1.3953 0.8382 0.0853  0.1754  -0.0373 444 ARG A CZ  
3574 N NH1 . ARG A 444 ? 1.0746 1.4937 0.9270 0.0944  0.1935  -0.0391 444 ARG A NH1 
3575 N NH2 . ARG A 444 ? 0.9920 1.3518 0.7737 0.0606  0.1757  -0.0203 444 ARG A NH2 
3576 N N   . PRO A 445 ? 0.9326 1.1694 0.8518 0.1130  0.0692  -0.0507 445 PRO A N   
3577 C CA  . PRO A 445 ? 0.8466 1.0914 0.8072 0.1036  0.0586  -0.0391 445 PRO A CA  
3578 C C   . PRO A 445 ? 0.8169 1.1070 0.8065 0.0890  0.0718  -0.0243 445 PRO A C   
3579 O O   . PRO A 445 ? 0.8588 1.1851 0.8484 0.0909  0.0918  -0.0246 445 PRO A O   
3580 C CB  . PRO A 445 ? 0.8591 1.1030 0.8396 0.1263  0.0546  -0.0520 445 PRO A CB  
3581 C CG  . PRO A 445 ? 0.9069 1.1690 0.8733 0.1477  0.0729  -0.0673 445 PRO A CG  
3582 C CD  . PRO A 445 ? 0.9363 1.1776 0.8540 0.1409  0.0775  -0.0701 445 PRO A CD  
3583 N N   . ALA A 446 ? 0.7829 1.0700 0.7964 0.0733  0.0606  -0.0112 446 ALA A N   
3584 C CA  . ALA A 446 ? 0.7886 1.1093 0.8268 0.0556  0.0687  0.0039  446 ALA A CA  
3585 C C   . ALA A 446 ? 0.8218 1.1827 0.9006 0.0639  0.0749  0.0021  446 ALA A C   
3586 O O   . ALA A 446 ? 0.8186 1.1766 0.9092 0.0835  0.0696  -0.0093 446 ALA A O   
3587 C CB  . ALA A 446 ? 0.7263 1.0225 0.7693 0.0364  0.0537  0.0172  446 ALA A CB  
3588 N N   . ASP A 447 ? 0.7391 1.1372 0.8395 0.0480  0.0848  0.0145  447 ASP A N   
3589 C CA  . ASP A 447 ? 0.7514 1.1939 0.8940 0.0511  0.0895  0.0161  447 ASP A CA  
3590 C C   . ASP A 447 ? 0.7010 1.1373 0.8653 0.0321  0.0756  0.0285  447 ASP A C   
3591 O O   . ASP A 447 ? 0.7350 1.1414 0.8832 0.0145  0.0679  0.0377  447 ASP A O   
3592 C CB  . ASP A 447 ? 0.7609 1.2567 0.9141 0.0456  0.1123  0.0208  447 ASP A CB  
3593 C CG  . ASP A 447 ? 0.8301 1.3401 0.9667 0.0689  0.1291  0.0057  447 ASP A CG  
3594 O OD1 . ASP A 447 ? 0.8347 1.3137 0.9558 0.0911  0.1213  -0.0095 447 ASP A OD1 
3595 O OD2 . ASP A 447 ? 0.8181 1.3691 0.9555 0.0645  0.1504  0.0087  447 ASP A OD2 
3596 N N   . GLY A 448 ? 0.6677 1.1320 0.8682 0.0370  0.0718  0.0282  448 GLY A N   
3597 C CA  . GLY A 448 ? 0.6021 1.0616 0.8216 0.0200  0.0582  0.0383  448 GLY A CA  
3598 C C   . GLY A 448 ? 0.6047 1.0218 0.8184 0.0265  0.0392  0.0336  448 GLY A C   
3599 O O   . GLY A 448 ? 0.6345 1.0527 0.8667 0.0187  0.0279  0.0385  448 GLY A O   
3600 N N   . ILE A 449 ? 0.6494 1.0290 0.8360 0.0389  0.0349  0.0248  449 ILE A N   
3601 C CA  . ILE A 449 ? 0.6277 0.9680 0.8075 0.0439  0.0179  0.0210  449 ILE A CA  
3602 C C   . ILE A 449 ? 0.6149 0.9671 0.8141 0.0641  0.0120  0.0128  449 ILE A C   
3603 O O   . ILE A 449 ? 0.7211 1.0779 0.9158 0.0851  0.0173  0.0018  449 ILE A O   
3604 C CB  . ILE A 449 ? 0.6705 0.9697 0.8171 0.0484  0.0143  0.0153  449 ILE A CB  
3605 C CG1 . ILE A 449 ? 0.6520 0.9436 0.7808 0.0311  0.0200  0.0240  449 ILE A CG1 
3606 C CG2 . ILE A 449 ? 0.6377 0.8995 0.7793 0.0488  -0.0022 0.0140  449 ILE A CG2 
3607 C CD1 . ILE A 449 ? 0.6091 0.8929 0.7461 0.0110  0.0143  0.0359  449 ILE A CD1 
3608 N N   . GLU A 450 ? 0.5758 0.9304 0.7944 0.0585  0.0002  0.0179  450 GLU A N   
3609 C CA  . GLU A 450 ? 0.6253 0.9940 0.8655 0.0765  -0.0077 0.0128  450 GLU A CA  
3610 C C   . GLU A 450 ? 0.6283 0.9527 0.8541 0.0840  -0.0250 0.0090  450 GLU A C   
3611 O O   . GLU A 450 ? 0.6273 0.9502 0.8601 0.1047  -0.0319 0.0020  450 GLU A O   
3612 C CB  . GLU A 450 ? 0.5353 0.9424 0.8086 0.0650  -0.0109 0.0222  450 GLU A CB  
3613 C CG  . GLU A 450 ? 0.5619 1.0129 0.8501 0.0518  0.0053  0.0288  450 GLU A CG  
3614 C CD  . GLU A 450 ? 0.6251 1.1304 0.9549 0.0519  0.0051  0.0336  450 GLU A CD  
3615 O OE1 . GLU A 450 ? 0.6143 1.1176 0.9590 0.0513  -0.0116 0.0365  450 GLU A OE1 
3616 O OE2 . GLU A 450 ? 0.6626 1.2141 1.0101 0.0519  0.0214  0.0351  450 GLU A OE2 
3617 N N   . ALA A 451 ? 0.6019 0.8904 0.8080 0.0680  -0.0319 0.0138  451 ALA A N   
3618 C CA  . ALA A 451 ? 0.5677 0.8154 0.7588 0.0716  -0.0468 0.0117  451 ALA A CA  
3619 C C   . ALA A 451 ? 0.5523 0.7670 0.7203 0.0559  -0.0473 0.0150  451 ALA A C   
3620 O O   . ALA A 451 ? 0.5687 0.7900 0.7376 0.0391  -0.0416 0.0220  451 ALA A O   
3621 C CB  . ALA A 451 ? 0.5519 0.8028 0.7581 0.0676  -0.0601 0.0175  451 ALA A CB  
3622 N N   . VAL A 452 ? 0.6274 0.8068 0.7756 0.0618  -0.0547 0.0102  452 VAL A N   
3623 C CA  . VAL A 452 ? 0.6486 0.7991 0.7790 0.0485  -0.0569 0.0134  452 VAL A CA  
3624 C C   . VAL A 452 ? 0.6570 0.7757 0.7777 0.0487  -0.0705 0.0136  452 VAL A C   
3625 O O   . VAL A 452 ? 0.6849 0.7883 0.7989 0.0628  -0.0782 0.0073  452 VAL A O   
3626 C CB  . VAL A 452 ? 0.6778 0.8189 0.7911 0.0517  -0.0515 0.0085  452 VAL A CB  
3627 C CG1 . VAL A 452 ? 0.7053 0.8208 0.8058 0.0385  -0.0557 0.0129  452 VAL A CG1 
3628 C CG2 . VAL A 452 ? 0.5877 0.7587 0.7064 0.0498  -0.0376 0.0099  452 VAL A CG2 
3629 N N   . MET A 453 ? 0.6137 0.7209 0.7319 0.0331  -0.0732 0.0206  453 MET A N   
3630 C CA  . MET A 453 ? 0.6241 0.7031 0.7317 0.0294  -0.0844 0.0229  453 MET A CA  
3631 C C   . MET A 453 ? 0.6285 0.6888 0.7247 0.0166  -0.0827 0.0259  453 MET A C   
3632 O O   . MET A 453 ? 0.5675 0.6376 0.6681 0.0066  -0.0741 0.0296  453 MET A O   
3633 C CB  . MET A 453 ? 0.6176 0.7023 0.7319 0.0224  -0.0891 0.0287  453 MET A CB  
3634 C CG  . MET A 453 ? 0.6364 0.7000 0.7428 0.0280  -0.1037 0.0296  453 MET A CG  
3635 S SD  . MET A 453 ? 0.6529 0.7241 0.7643 0.0195  -0.1115 0.0368  453 MET A SD  
3636 C CE  . MET A 453 ? 0.5870 0.6481 0.6859 -0.0028 -0.1023 0.0417  453 MET A CE  
3637 N N   . VAL A 454 ? 0.6480 0.6815 0.7307 0.0170  -0.0913 0.0248  454 VAL A N   
3638 C CA  . VAL A 454 ? 0.6227 0.6419 0.6980 0.0048  -0.0910 0.0282  454 VAL A CA  
3639 C C   . VAL A 454 ? 0.6836 0.6811 0.7497 -0.0043 -0.0989 0.0334  454 VAL A C   
3640 O O   . VAL A 454 ? 0.7023 0.6775 0.7570 0.0009  -0.1104 0.0319  454 VAL A O   
3641 C CB  . VAL A 454 ? 0.6359 0.6435 0.7018 0.0096  -0.0946 0.0229  454 VAL A CB  
3642 C CG1 . VAL A 454 ? 0.6629 0.6619 0.7267 -0.0045 -0.0955 0.0279  454 VAL A CG1 
3643 C CG2 . VAL A 454 ? 0.6559 0.6839 0.7260 0.0185  -0.0863 0.0180  454 VAL A CG2 
3644 N N   . ASN A 455 ? 0.6346 0.6365 0.7031 -0.0176 -0.0925 0.0394  455 ASN A N   
3645 C CA  . ASN A 455 ? 0.6433 0.6271 0.7005 -0.0288 -0.0970 0.0454  455 ASN A CA  
3646 C C   . ASN A 455 ? 0.6512 0.6229 0.6996 -0.0233 -0.1080 0.0464  455 ASN A C   
3647 O O   . ASN A 455 ? 0.6655 0.6120 0.6991 -0.0268 -0.1185 0.0499  455 ASN A O   
3648 C CB  . ASN A 455 ? 0.6437 0.6092 0.6930 -0.0365 -0.1024 0.0477  455 ASN A CB  
3649 C CG  . ASN A 455 ? 0.6609 0.6413 0.7220 -0.0430 -0.0933 0.0486  455 ASN A CG  
3650 O OD1 . ASN A 455 ? 0.6385 0.6358 0.7093 -0.0476 -0.0817 0.0507  455 ASN A OD1 
3651 N ND2 . ASN A 455 ? 0.6778 0.6504 0.7372 -0.0430 -0.0998 0.0469  455 ASN A ND2 
3652 N N   . GLY A 456 ? 0.6470 0.6367 0.7051 -0.0154 -0.1067 0.0441  456 GLY A N   
3653 C CA  . GLY A 456 ? 0.6662 0.6505 0.7210 -0.0091 -0.1183 0.0457  456 GLY A CA  
3654 C C   . GLY A 456 ? 0.6733 0.6493 0.7293 0.0091  -0.1292 0.0407  456 GLY A C   
3655 O O   . GLY A 456 ? 0.6451 0.6169 0.7010 0.0173  -0.1406 0.0423  456 GLY A O   
3656 N N   . VAL A 457 ? 0.6456 0.6178 0.7016 0.0167  -0.1268 0.0344  457 VAL A N   
3657 C CA  . VAL A 457 ? 0.6893 0.6498 0.7427 0.0359  -0.1356 0.0272  457 VAL A CA  
3658 C C   . VAL A 457 ? 0.7170 0.7097 0.7876 0.0495  -0.1250 0.0194  457 VAL A C   
3659 O O   . VAL A 457 ? 0.7324 0.7367 0.8048 0.0448  -0.1141 0.0170  457 VAL A O   
3660 C CB  . VAL A 457 ? 0.7393 0.6658 0.7736 0.0334  -0.1422 0.0248  457 VAL A CB  
3661 C CG1 . VAL A 457 ? 0.7311 0.6413 0.7591 0.0554  -0.1506 0.0150  457 VAL A CG1 
3662 C CG2 . VAL A 457 ? 0.7376 0.6340 0.7549 0.0174  -0.1520 0.0343  457 VAL A CG2 
3663 N N   . MET A 458 ? 0.6828 0.6915 0.7666 0.0661  -0.1283 0.0163  458 MET A N   
3664 C CA  . MET A 458 ? 0.6787 0.7215 0.7798 0.0795  -0.1170 0.0092  458 MET A CA  
3665 C C   . MET A 458 ? 0.6923 0.7190 0.7792 0.0914  -0.1147 -0.0011 458 MET A C   
3666 O O   . MET A 458 ? 0.7223 0.7241 0.7987 0.1073  -0.1247 -0.0075 458 MET A O   
3667 C CB  . MET A 458 ? 0.6347 0.7001 0.7559 0.0957  -0.1222 0.0084  458 MET A CB  
3668 C CG  . MET A 458 ? 0.6185 0.7301 0.7634 0.1046  -0.1081 0.0041  458 MET A CG  
3669 S SD  . MET A 458 ? 0.6468 0.7909 0.8049 0.0806  -0.0958 0.0129  458 MET A SD  
3670 C CE  . MET A 458 ? 0.6382 0.7924 0.8107 0.0745  -0.1093 0.0219  458 MET A CE  
3671 N N   . SER A 459 ? 0.7219 0.7597 0.8059 0.0839  -0.1027 -0.0029 459 SER A N   
3672 C CA  . SER A 459 ? 0.7744 0.7924 0.8389 0.0901  -0.1021 -0.0117 459 SER A CA  
3673 C C   . SER A 459 ? 0.7840 0.8273 0.8522 0.1052  -0.0894 -0.0210 459 SER A C   
3674 O O   . SER A 459 ? 0.8184 0.8420 0.8664 0.1151  -0.0901 -0.0309 459 SER A O   
3675 C CB  . SER A 459 ? 0.7285 0.7359 0.7827 0.0699  -0.1004 -0.0064 459 SER A CB  
3676 O OG  . SER A 459 ? 0.7652 0.7507 0.8151 0.0556  -0.1099 0.0016  459 SER A OG  
3677 N N   . TYR A 460 ? 0.7655 0.8508 0.8565 0.1060  -0.0778 -0.0179 460 TYR A N   
3678 C CA  . TYR A 460 ? 0.7737 0.8877 0.8682 0.1174  -0.0631 -0.0251 460 TYR A CA  
3679 C C   . TYR A 460 ? 0.7976 0.9569 0.9235 0.1227  -0.0556 -0.0217 460 TYR A C   
3680 O O   . TYR A 460 ? 0.7343 0.9096 0.8762 0.1070  -0.0563 -0.0111 460 TYR A O   
3681 C CB  . TYR A 460 ? 0.8052 0.9247 0.8887 0.1021  -0.0533 -0.0216 460 TYR A CB  
3682 C CG  . TYR A 460 ? 0.8059 0.9535 0.8877 0.1105  -0.0371 -0.0274 460 TYR A CG  
3683 C CD1 . TYR A 460 ? 0.8636 0.9952 0.9212 0.1256  -0.0347 -0.0402 460 TYR A CD1 
3684 C CD2 . TYR A 460 ? 0.8095 0.9978 0.9107 0.1020  -0.0242 -0.0199 460 TYR A CD2 
3685 C CE1 . TYR A 460 ? 0.8723 1.0300 0.9245 0.1329  -0.0181 -0.0457 460 TYR A CE1 
3686 C CE2 . TYR A 460 ? 0.7802 0.9956 0.8783 0.1075  -0.0082 -0.0237 460 TYR A CE2 
3687 C CZ  . TYR A 460 ? 0.8591 1.0603 0.9324 0.1233  -0.0043 -0.0367 460 TYR A CZ  
3688 O OH  . TYR A 460 ? 0.8694 1.0980 0.9361 0.1284  0.0135  -0.0408 460 TYR A OH  
3689 N N   . GLY A 461 ? 0.8330 1.0133 0.9676 0.1448  -0.0485 -0.0311 461 GLY A N   
3690 C CA  . GLY A 461 ? 0.8814 1.1118 1.0500 0.1510  -0.0407 -0.0283 461 GLY A CA  
3691 C C   . GLY A 461 ? 0.9000 1.1685 1.0730 0.1545  -0.0196 -0.0322 461 GLY A C   
3692 O O   . GLY A 461 ? 0.9880 1.2418 1.1344 0.1514  -0.0117 -0.0367 461 GLY A O   
3693 N N   . SER A 462 ? 0.9201 1.2396 1.1270 0.1598  -0.0112 -0.0295 462 SER A N   
3694 C CA  . SER A 462 ? 0.9538 1.3172 1.1689 0.1622  0.0106  -0.0317 462 SER A CA  
3695 C C   . SER A 462 ? 1.0607 1.4247 1.2644 0.1914  0.0209  -0.0485 462 SER A C   
3696 O O   . SER A 462 ? 0.9871 1.3858 1.1921 0.1949  0.0413  -0.0520 462 SER A O   
3697 C CB  . SER A 462 ? 0.9274 1.3493 1.1860 0.1561  0.0160  -0.0222 462 SER A CB  
3698 O OG  . SER A 462 ? 1.0304 1.4646 1.3164 0.1756  0.0047  -0.0250 462 SER A OG  
3699 N N   . ASP A 463 ? 1.0297 1.3543 1.2200 0.2120  0.0075  -0.0591 463 ASP A N   
3700 C CA  . ASP A 463 ? 0.9962 1.3090 1.1676 0.2406  0.0156  -0.0773 463 ASP A CA  
3701 C C   . ASP A 463 ? 1.0346 1.3040 1.1572 0.2339  0.0180  -0.0846 463 ASP A C   
3702 O O   . ASP A 463 ? 1.1077 1.3570 1.2054 0.2558  0.0230  -0.1011 463 ASP A O   
3703 C CB  . ASP A 463 ? 0.9909 1.2736 1.1659 0.2659  -0.0021 -0.0855 463 ASP A CB  
3704 C CG  . ASP A 463 ? 1.0712 1.2951 1.2241 0.2514  -0.0259 -0.0795 463 ASP A CG  
3705 O OD1 . ASP A 463 ? 1.0118 1.2253 1.1536 0.2228  -0.0282 -0.0687 463 ASP A OD1 
3706 O OD2 . ASP A 463 ? 1.0940 1.2822 1.2407 0.2688  -0.0421 -0.0853 463 ASP A OD2 
3707 N N   . LYS A 464 ? 1.0299 1.2838 1.1383 0.2050  0.0137  -0.0729 464 LYS A N   
3708 C CA  . LYS A 464 ? 0.9897 1.2061 1.0550 0.1954  0.0134  -0.0770 464 LYS A CA  
3709 C C   . LYS A 464 ? 1.0285 1.1853 1.0641 0.2069  -0.0042 -0.0881 464 LYS A C   
3710 O O   . LYS A 464 ? 1.0759 1.2045 1.0752 0.2154  -0.0022 -0.1009 464 LYS A O   
3711 C CB  . LYS A 464 ? 1.0120 1.2528 1.0603 0.2016  0.0357  -0.0847 464 LYS A CB  
3712 C CG  . LYS A 464 ? 0.9902 1.2732 1.0512 0.1788  0.0503  -0.0702 464 LYS A CG  
3713 C CD  . LYS A 464 ? 1.0243 1.3587 1.1344 0.1756  0.0551  -0.0598 464 LYS A CD  
3714 C CE  . LYS A 464 ? 0.9869 1.3649 1.1077 0.1551  0.0720  -0.0471 464 LYS A CE  
3715 N NZ  . LYS A 464 ? 0.8902 1.3164 1.0590 0.1501  0.0739  -0.0370 464 LYS A NZ  
3716 N N   A LYS A 465 ? 0.9946 1.1301 1.0431 0.2056  -0.0224 -0.0829 465 LYS A N   
3717 N N   B LYS A 465 ? 0.9946 1.1302 1.0432 0.2055  -0.0224 -0.0828 465 LYS A N   
3718 C CA  A LYS A 465 ? 1.0179 1.0951 1.0402 0.2124  -0.0414 -0.0903 465 LYS A CA  
3719 C CA  B LYS A 465 ? 1.0175 1.0952 1.0406 0.2126  -0.0416 -0.0902 465 LYS A CA  
3720 C C   A LYS A 465 ? 1.0095 1.0643 1.0356 0.1885  -0.0583 -0.0758 465 LYS A C   
3721 C C   B LYS A 465 ? 1.0093 1.0643 1.0356 0.1883  -0.0583 -0.0757 465 LYS A C   
3722 O O   A LYS A 465 ? 0.9694 1.0504 1.0249 0.1788  -0.0592 -0.0636 465 LYS A O   
3723 O O   B LYS A 465 ? 0.9693 1.0504 1.0247 0.1781  -0.0592 -0.0633 465 LYS A O   
3724 C CB  A LYS A 465 ? 1.0326 1.1018 1.0639 0.2429  -0.0468 -0.1014 465 LYS A CB  
3725 C CB  B LYS A 465 ? 1.0310 1.1026 1.0652 0.2426  -0.0470 -0.1004 465 LYS A CB  
3726 C CG  A LYS A 465 ? 1.0485 1.1335 1.0719 0.2711  -0.0297 -0.1192 465 LYS A CG  
3727 C CG  B LYS A 465 ? 1.0450 1.0527 1.0539 0.2479  -0.0696 -0.1053 465 LYS A CG  
3728 C CD  A LYS A 465 ? 1.0461 1.0869 1.0192 0.2718  -0.0295 -0.1325 465 LYS A CD  
3729 C CD  B LYS A 465 ? 1.0280 1.0311 1.0535 0.2764  -0.0777 -0.1114 465 LYS A CD  
3730 C CE  A LYS A 465 ? 1.0157 1.0712 0.9760 0.3003  -0.0101 -0.1517 465 LYS A CE  
3731 C CE  B LYS A 465 ? 1.0248 0.9604 1.0242 0.2774  -0.1025 -0.1128 465 LYS A CE  
3732 N NZ  A LYS A 465 ? 0.9777 1.0274 0.9522 0.3350  -0.0136 -0.1639 465 LYS A NZ  
3733 N NZ  B LYS A 465 ? 0.9523 0.8795 0.9674 0.3053  -0.1132 -0.1166 465 LYS A NZ  
3734 N N   . ILE A 466 ? 1.0038 1.0111 0.9996 0.1785  -0.0715 -0.0774 466 ILE A N   
3735 C CA  . ILE A 466 ? 0.9626 0.9484 0.9598 0.1557  -0.0859 -0.0645 466 ILE A CA  
3736 C C   . ILE A 466 ? 0.9688 0.9217 0.9653 0.1648  -0.1030 -0.0652 466 ILE A C   
3737 O O   . ILE A 466 ? 1.0132 0.9274 0.9861 0.1802  -0.1120 -0.0770 466 ILE A O   
3738 C CB  . ILE A 466 ? 0.9446 0.9010 0.9137 0.1382  -0.0921 -0.0639 466 ILE A CB  
3739 C CG1 . ILE A 466 ? 0.9323 0.9208 0.9032 0.1275  -0.0773 -0.0599 466 ILE A CG1 
3740 C CG2 . ILE A 466 ? 0.9131 0.8473 0.8849 0.1171  -0.1066 -0.0518 466 ILE A CG2 
3741 C CD1 . ILE A 466 ? 0.9019 0.8676 0.8502 0.1097  -0.0848 -0.0571 466 ILE A CD1 
3742 N N   . THR A 467 ? 0.9049 0.8696 0.9238 0.1550  -0.1083 -0.0526 467 THR A N   
3743 C CA  . THR A 467 ? 0.9418 0.8787 0.9610 0.1626  -0.1249 -0.0505 467 THR A CA  
3744 C C   . THR A 467 ? 0.9142 0.8223 0.9243 0.1382  -0.1382 -0.0380 467 THR A C   
3745 O O   . THR A 467 ? 0.9127 0.7951 0.9196 0.1405  -0.1528 -0.0336 467 THR A O   
3746 C CB  . THR A 467 ? 0.9333 0.9087 0.9855 0.1747  -0.1219 -0.0464 467 THR A CB  
3747 O OG1 . THR A 467 ? 0.8297 0.8381 0.9017 0.1531  -0.1155 -0.0333 467 THR A OG1 
3748 C CG2 . THR A 467 ? 0.9150 0.9254 0.9807 0.1993  -0.1070 -0.0583 467 THR A CG2 
3749 N N   . GLY A 468 ? 0.9101 0.8226 0.9162 0.1153  -0.1334 -0.0315 468 GLY A N   
3750 C CA  . GLY A 468 ? 0.8181 0.7108 0.8191 0.0922  -0.1426 -0.0197 468 GLY A CA  
3751 C C   . GLY A 468 ? 0.8630 0.7434 0.8498 0.0751  -0.1426 -0.0189 468 GLY A C   
3752 O O   . GLY A 468 ? 0.8811 0.7777 0.8663 0.0767  -0.1332 -0.0242 468 GLY A O   
3753 N N   . ARG A 469 ? 0.8611 0.7133 0.8376 0.0575  -0.1540 -0.0111 469 ARG A N   
3754 C CA  A ARG A 469 ? 0.8366 0.6785 0.8039 0.0386  -0.1570 -0.0079 469 ARG A CA  
3755 C CA  B ARG A 469 ? 0.8372 0.6803 0.8050 0.0385  -0.1566 -0.0079 469 ARG A CA  
3756 C C   . ARG A 469 ? 0.8215 0.6681 0.7991 0.0158  -0.1576 0.0064  469 ARG A C   
3757 O O   . ARG A 469 ? 0.8347 0.6545 0.8006 0.0007  -0.1686 0.0117  469 ARG A O   
3758 C CB  A ARG A 469 ? 0.8884 0.6833 0.8265 0.0405  -0.1728 -0.0157 469 ARG A CB  
3759 C CB  B ARG A 469 ? 0.8876 0.6853 0.8262 0.0412  -0.1716 -0.0164 469 ARG A CB  
3760 C CG  A ARG A 469 ? 0.9119 0.6985 0.8336 0.0622  -0.1709 -0.0320 469 ARG A CG  
3761 C CG  B ARG A 469 ? 0.9020 0.7004 0.8272 0.0578  -0.1669 -0.0309 469 ARG A CG  
3762 C CD  A ARG A 469 ? 0.9900 0.7201 0.8792 0.0675  -0.1890 -0.0409 469 ARG A CD  
3763 C CD  B ARG A 469 ? 0.9709 0.7222 0.8668 0.0743  -0.1798 -0.0441 469 ARG A CD  
3764 N NE  A ARG A 469 ? 1.0107 0.7251 0.8756 0.0700  -0.1910 -0.0528 469 ARG A NE  
3765 N NE  B ARG A 469 ? 1.0092 0.7146 0.8819 0.0570  -0.1984 -0.0416 469 ARG A NE  
3766 C CZ  A ARG A 469 ? 1.0177 0.7150 0.8690 0.0487  -0.2011 -0.0494 469 ARG A CZ  
3767 C CZ  B ARG A 469 ? 1.0196 0.7080 0.8725 0.0464  -0.2052 -0.0461 469 ARG A CZ  
3768 N NH1 A ARG A 469 ? 1.0042 0.7013 0.8668 0.0236  -0.2083 -0.0346 469 ARG A NH1 
3769 N NH1 B ARG A 469 ? 1.0128 0.7240 0.8634 0.0519  -0.1949 -0.0532 469 ARG A NH1 
3770 N NH2 A ARG A 469 ? 1.0296 0.7115 0.8554 0.0522  -0.2040 -0.0611 469 ARG A NH2 
3771 N NH2 B ARG A 469 ? 1.0457 0.6930 0.8797 0.0283  -0.2237 -0.0424 469 ARG A NH2 
3772 N N   . ALA A 470 ? 0.8016 0.6827 0.8004 0.0125  -0.1451 0.0128  470 ALA A N   
3773 C CA  . ALA A 470 ? 0.7466 0.6343 0.7537 -0.0063 -0.1424 0.0247  470 ALA A CA  
3774 C C   . ALA A 470 ? 0.7468 0.6613 0.7690 -0.0190 -0.1315 0.0293  470 ALA A C   
3775 O O   . ALA A 470 ? 0.7493 0.6811 0.7837 -0.0288 -0.1228 0.0367  470 ALA A O   
3776 C CB  . ALA A 470 ? 0.7401 0.6410 0.7560 -0.0018 -0.1381 0.0283  470 ALA A CB  
3777 N N   . GLY A 471 ? 0.7387 0.6554 0.7589 -0.0180 -0.1324 0.0248  471 GLY A N   
3778 C CA  . GLY A 471 ? 0.6913 0.6314 0.7267 -0.0289 -0.1250 0.0302  471 GLY A CA  
3779 C C   . GLY A 471 ? 0.6791 0.6139 0.7188 -0.0482 -0.1295 0.0392  471 GLY A C   
3780 O O   . GLY A 471 ? 0.7698 0.6770 0.7952 -0.0559 -0.1419 0.0404  471 GLY A O   
3781 N N   . ARG A 472 ? 0.6305 0.5922 0.6905 -0.0564 -0.1189 0.0459  472 ARG A N   
3782 C CA  . ARG A 472 ? 0.6811 0.6483 0.7517 -0.0742 -0.1190 0.0550  472 ARG A CA  
3783 C C   . ARG A 472 ? 0.6763 0.6702 0.7680 -0.0776 -0.1149 0.0582  472 ARG A C   
3784 O O   . ARG A 472 ? 0.6597 0.6687 0.7580 -0.0668 -0.1087 0.0551  472 ARG A O   
3785 C CB  . ARG A 472 ? 0.6753 0.6500 0.7509 -0.0802 -0.1080 0.0608  472 ARG A CB  
3786 C CG  . ARG A 472 ? 0.6914 0.6402 0.7465 -0.0780 -0.1138 0.0600  472 ARG A CG  
3787 C CD  . ARG A 472 ? 0.6913 0.6496 0.7484 -0.0823 -0.1021 0.0646  472 ARG A CD  
3788 N NE  . ARG A 472 ? 0.7480 0.6815 0.7849 -0.0810 -0.1100 0.0656  472 ARG A NE  
3789 C CZ  . ARG A 472 ? 0.7179 0.6530 0.7490 -0.0834 -0.1038 0.0686  472 ARG A CZ  
3790 N NH1 . ARG A 472 ? 0.6780 0.6361 0.7201 -0.0866 -0.0883 0.0696  472 ARG A NH1 
3791 N NH2 . ARG A 472 ? 0.7228 0.6334 0.7348 -0.0819 -0.1146 0.0705  472 ARG A NH2 
3792 N N   . PHE A 473 ? 0.6525 0.6531 0.7557 -0.0932 -0.1192 0.0655  473 PHE A N   
3793 C CA  . PHE A 473 ? 0.6161 0.6470 0.7455 -0.0962 -0.1153 0.0704  473 PHE A CA  
3794 C C   . PHE A 473 ? 0.6069 0.6631 0.7565 -0.0950 -0.0967 0.0745  473 PHE A C   
3795 O O   . PHE A 473 ? 0.6426 0.6978 0.7915 -0.1039 -0.0898 0.0783  473 PHE A O   
3796 C CB  . PHE A 473 ? 0.6184 0.6519 0.7568 -0.1139 -0.1276 0.0771  473 PHE A CB  
3797 C CG  . PHE A 473 ? 0.5944 0.6624 0.7638 -0.1160 -0.1262 0.0830  473 PHE A CG  
3798 C CD1 . PHE A 473 ? 0.6001 0.6697 0.7681 -0.1089 -0.1361 0.0803  473 PHE A CD1 
3799 C CD2 . PHE A 473 ? 0.5586 0.6578 0.7580 -0.1240 -0.1148 0.0913  473 PHE A CD2 
3800 C CE1 . PHE A 473 ? 0.5323 0.6327 0.7293 -0.1097 -0.1373 0.0868  473 PHE A CE1 
3801 C CE2 . PHE A 473 ? 0.5989 0.7319 0.8307 -0.1232 -0.1142 0.0968  473 PHE A CE2 
3802 C CZ  . PHE A 473 ? 0.5330 0.6660 0.7641 -0.1159 -0.1268 0.0951  473 PHE A CZ  
3803 N N   . LEU A 474 ? 0.6072 0.6828 0.7715 -0.0842 -0.0888 0.0735  474 LEU A N   
3804 C CA  . LEU A 474 ? 0.5701 0.6643 0.7499 -0.0800 -0.0713 0.0751  474 LEU A CA  
3805 C C   . LEU A 474 ? 0.5649 0.6890 0.7765 -0.0840 -0.0673 0.0819  474 LEU A C   
3806 O O   . LEU A 474 ? 0.5310 0.6657 0.7554 -0.0815 -0.0765 0.0842  474 LEU A O   
3807 C CB  . LEU A 474 ? 0.5720 0.6647 0.7466 -0.0652 -0.0653 0.0700  474 LEU A CB  
3808 C CG  . LEU A 474 ? 0.6224 0.6935 0.7718 -0.0596 -0.0683 0.0636  474 LEU A CG  
3809 C CD1 . LEU A 474 ? 0.5609 0.6359 0.7094 -0.0489 -0.0602 0.0605  474 LEU A CD1 
3810 C CD2 . LEU A 474 ? 0.5836 0.6415 0.7204 -0.0663 -0.0661 0.0635  474 LEU A CD2 
3811 N N   . ARG A 475 ? 0.6058 0.7445 0.8298 -0.0898 -0.0536 0.0853  475 ARG A N   
3812 C CA  . ARG A 475 ? 0.5218 0.6945 0.7805 -0.0909 -0.0458 0.0911  475 ARG A CA  
3813 C C   . ARG A 475 ? 0.5157 0.6982 0.7836 -0.0760 -0.0283 0.0874  475 ARG A C   
3814 O O   . ARG A 475 ? 0.5343 0.6989 0.7808 -0.0715 -0.0193 0.0816  475 ARG A O   
3815 C CB  . ARG A 475 ? 0.4967 0.6826 0.7645 -0.1085 -0.0405 0.0976  475 ARG A CB  
3816 C CG  . ARG A 475 ? 0.5359 0.7065 0.7919 -0.1255 -0.0592 0.1018  475 ARG A CG  
3817 C CD  . ARG A 475 ? 0.6140 0.7934 0.8740 -0.1457 -0.0533 0.1096  475 ARG A CD  
3818 N NE  . ARG A 475 ? 0.6464 0.7975 0.8844 -0.1622 -0.0719 0.1127  475 ARG A NE  
3819 C CZ  . ARG A 475 ? 0.6723 0.8304 0.9230 -0.1771 -0.0876 0.1191  475 ARG A CZ  
3820 N NH1 . ARG A 475 ? 0.6622 0.8597 0.9511 -0.1781 -0.0875 0.1243  475 ARG A NH1 
3821 N NH2 . ARG A 475 ? 0.6852 0.8087 0.9094 -0.1912 -0.1051 0.1204  475 ARG A NH2 
3822 N N   . ARG A 476 ? 0.5502 0.7599 0.8499 -0.0681 -0.0252 0.0908  476 ARG A N   
3823 C CA  . ARG A 476 ? 0.5851 0.8006 0.8939 -0.0521 -0.0100 0.0869  476 ARG A CA  
3824 C C   . ARG A 476 ? 0.5990 0.8148 0.9003 -0.0546 0.0105  0.0831  476 ARG A C   
3825 O O   . ARG A 476 ? 0.6727 0.9000 0.9772 -0.0684 0.0156  0.0868  476 ARG A O   
3826 C CB  . ARG A 476 ? 0.5646 0.8118 0.9131 -0.0428 -0.0107 0.0923  476 ARG A CB  
3827 C CG  . ARG A 476 ? 0.4955 0.7409 0.8512 -0.0229 0.0002  0.0882  476 ARG A CG  
3828 C CD  . ARG A 476 ? 0.4687 0.7471 0.8671 -0.0117 -0.0012 0.0943  476 ARG A CD  
3829 N NE  . ARG A 476 ? 0.4804 0.7945 0.9095 -0.0144 0.0140  0.0964  476 ARG A NE  
3830 C CZ  . ARG A 476 ? 0.4097 0.7549 0.8641 -0.0285 0.0076  0.1045  476 ARG A CZ  
3831 N NH1 . ARG A 476 ? 0.4695 0.8110 0.9204 -0.0408 -0.0153 0.1105  476 ARG A NH1 
3832 N NH2 . ARG A 476 ? 0.3991 0.7798 0.8820 -0.0312 0.0248  0.1066  476 ARG A NH2 
3833 N N   A ARG A 477 ? 0.6194 0.8200 0.9074 -0.0426 0.0218  0.0760  477 ARG A N   
3834 N N   B ARG A 477 ? 0.6196 0.8201 0.9074 -0.0427 0.0218  0.0760  477 ARG A N   
3835 C CA  A ARG A 477 ? 0.6694 0.8666 0.9451 -0.0435 0.0414  0.0708  477 ARG A CA  
3836 C CA  B ARG A 477 ? 0.6689 0.8655 0.9438 -0.0440 0.0412  0.0708  477 ARG A CA  
3837 C C   A ARG A 477 ? 0.6972 0.9297 1.0056 -0.0405 0.0574  0.0732  477 ARG A C   
3838 C C   B ARG A 477 ? 0.6976 0.9292 1.0050 -0.0404 0.0576  0.0730  477 ARG A C   
3839 O O   A ARG A 477 ? 0.6634 0.9152 1.0019 -0.0262 0.0591  0.0741  477 ARG A O   
3840 O O   B ARG A 477 ? 0.6652 0.9146 1.0014 -0.0256 0.0597  0.0734  477 ARG A O   
3841 C CB  A ARG A 477 ? 0.6756 0.8473 0.9308 -0.0312 0.0477  0.0623  477 ARG A CB  
3842 C CB  B ARG A 477 ? 0.6774 0.8476 0.9301 -0.0324 0.0472  0.0623  477 ARG A CB  
3843 C CG  A ARG A 477 ? 0.7547 0.9071 0.9789 -0.0364 0.0606  0.0556  477 ARG A CG  
3844 C CG  B ARG A 477 ? 0.7522 0.9101 0.9815 -0.0351 0.0647  0.0555  477 ARG A CG  
3845 C CD  A ARG A 477 ? 0.7663 0.8900 0.9684 -0.0276 0.0606  0.0481  477 ARG A CD  
3846 C CD  B ARG A 477 ? 0.7687 0.8959 0.9723 -0.0272 0.0662  0.0473  477 ARG A CD  
3847 N NE  A ARG A 477 ? 0.7866 0.8935 0.9625 -0.0291 0.0753  0.0403  477 ARG A NE  
3848 N NE  B ARG A 477 ? 0.7225 0.8479 0.9416 -0.0125 0.0613  0.0469  477 ARG A NE  
3849 C CZ  A ARG A 477 ? 0.8146 0.8963 0.9711 -0.0223 0.0784  0.0327  477 ARG A CZ  
3850 C CZ  B ARG A 477 ? 0.7323 0.8690 0.9733 0.0022  0.0716  0.0450  477 ARG A CZ  
3851 N NH1 A ARG A 477 ? 0.8218 0.8929 0.9830 -0.0141 0.0689  0.0329  477 ARG A NH1 
3852 N NH1 B ARG A 477 ? 0.7310 0.8860 0.9837 0.0053  0.0897  0.0422  477 ARG A NH1 
3853 N NH2 A ARG A 477 ? 0.8380 0.9029 0.9671 -0.0255 0.0909  0.0251  477 ARG A NH2 
3854 N NH2 B ARG A 477 ? 0.7080 0.8380 0.9593 0.0146  0.0637  0.0464  477 ARG A NH2 
3855 N N   . MET A 478 ? 0.6944 0.9369 0.9979 -0.0540 0.0691  0.0750  478 MET A N   
3856 C CA  . MET A 478 ? 0.7186 1.0010 1.0552 -0.0534 0.0864  0.0780  478 MET A CA  
3857 C C   . MET A 478 ? 0.7943 1.0738 1.1172 -0.0454 0.1125  0.0690  478 MET A C   
3858 O O   . MET A 478 ? 0.8103 1.1234 1.1576 -0.0431 0.1317  0.0696  478 MET A O   
3859 C CB  . MET A 478 ? 0.8400 1.1414 1.1840 -0.0767 0.0825  0.0882  478 MET A CB  
3860 C CG  . MET A 478 ? 0.9544 1.2466 1.2989 -0.0873 0.0552  0.0952  478 MET A CG  
3861 S SD  . MET A 478 ? 0.8185 1.1380 1.2069 -0.0747 0.0400  0.0997  478 MET A SD  
3862 C CE  . MET A 478 ? 0.5250 0.8874 0.9497 -0.0965 0.0354  0.1128  478 MET A CE  
# 
