data_9G5M
# 
_entry.id   9G5M 
# 
_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   9G5M         pdb_00009g5m 10.2210/pdb9g5m/pdb 
WWPDB D_1292140318 ?            ?                   
# 
_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                        9G5M 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-17 
_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 'SULFATE ION'                   96.063    6   ?                ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'         106.120   4   ?                ? ? ? 
4 non-polymer nat 1,2-ETHANEDIOL                  62.068    5   ?                ? ? ? 
5 non-polymer syn GLYCEROL                        92.094    4   ?                ? ? ? 
6 non-polymer syn 'TRIETHYLENE GLYCOL'            150.173   2   ?                ? ? ? 
7 non-polymer syn 'NICKEL (II) ION'               58.693    2   ?                ? ? ? 
8 water       nat water                           18.015    374 ?                ? ? ? 
# 
_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 'SULFATE ION'           SO4 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 1,2-ETHANEDIOL          EDO 
5 GLYCEROL                GOL 
6 'TRIETHYLENE GLYCOL'    PGE 
7 'NICKEL (II) ION'       NI  
8 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                       pET22b+ 
_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  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'    ?                               'C6 H14 O4'      150.173 
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 479 479 479 ASP ASP 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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 SO4 1   501 501 SO4 SO4 A . 
C 2 SO4 1   502 502 SO4 SO4 A . 
D 3 PEG 1   503 503 PEG PEG A . 
E 4 EDO 1   504 504 EDO EDO A . 
F 5 GOL 1   505 505 GOL GOL A . 
G 4 EDO 1   506 506 EDO EDO A . 
H 6 PGE 1   507 507 PGE PGE A . 
I 5 GOL 1   508 508 GOL GOL A . 
J 3 PEG 1   509 509 PEG PEG A . 
K 5 GOL 1   510 510 GOL GOL A . 
L 3 PEG 1   511 511 PEG PEG A . 
M 2 SO4 1   512 512 SO4 SO4 A . 
N 2 SO4 1   513 513 SO4 SO4 A . 
O 2 SO4 1   514 514 SO4 SO4 A . 
P 2 SO4 1   515 515 SO4 SO4 A . 
Q 4 EDO 1   516 516 EDO EDO A . 
R 5 GOL 1   517 517 GOL GOL A . 
S 3 PEG 1   518 518 PEG PEG A . 
T 4 EDO 1   519 519 EDO EDO A . 
U 4 EDO 1   520 520 EDO EDO A . 
V 6 PGE 1   521 521 PGE PGE A . 
W 7 NI  1   522 522 NI  NI  A . 
X 7 NI  1   523 523 NI  NI  A . 
Y 8 HOH 1   601 601 HOH HOH A . 
Y 8 HOH 2   602 602 HOH HOH A . 
Y 8 HOH 3   603 603 HOH HOH A . 
Y 8 HOH 4   604 604 HOH HOH A . 
Y 8 HOH 5   605 605 HOH HOH A . 
Y 8 HOH 6   606 606 HOH HOH A . 
Y 8 HOH 7   607 607 HOH HOH A . 
Y 8 HOH 8   608 608 HOH HOH A . 
Y 8 HOH 9   609 609 HOH HOH A . 
Y 8 HOH 10  610 610 HOH HOH A . 
Y 8 HOH 11  611 611 HOH HOH A . 
Y 8 HOH 12  612 612 HOH HOH A . 
Y 8 HOH 13  613 613 HOH HOH A . 
Y 8 HOH 14  615 615 HOH HOH A . 
Y 8 HOH 15  616 616 HOH HOH A . 
Y 8 HOH 16  617 617 HOH HOH A . 
Y 8 HOH 17  618 618 HOH HOH A . 
Y 8 HOH 18  619 619 HOH HOH A . 
Y 8 HOH 19  620 620 HOH HOH A . 
Y 8 HOH 20  621 621 HOH HOH A . 
Y 8 HOH 21  622 622 HOH HOH A . 
Y 8 HOH 22  623 623 HOH HOH A . 
Y 8 HOH 23  624 624 HOH HOH A . 
Y 8 HOH 24  625 625 HOH HOH A . 
Y 8 HOH 25  626 626 HOH HOH A . 
Y 8 HOH 26  627 627 HOH HOH A . 
Y 8 HOH 27  628 628 HOH HOH A . 
Y 8 HOH 28  629 629 HOH HOH A . 
Y 8 HOH 29  630 630 HOH HOH A . 
Y 8 HOH 30  631 631 HOH HOH A . 
Y 8 HOH 31  632 632 HOH HOH A . 
Y 8 HOH 32  633 633 HOH HOH A . 
Y 8 HOH 33  634 634 HOH HOH A . 
Y 8 HOH 34  635 635 HOH HOH A . 
Y 8 HOH 35  636 636 HOH HOH A . 
Y 8 HOH 36  637 637 HOH HOH A . 
Y 8 HOH 37  638 638 HOH HOH A . 
Y 8 HOH 38  639 639 HOH HOH A . 
Y 8 HOH 39  640 640 HOH HOH A . 
Y 8 HOH 40  641 641 HOH HOH A . 
Y 8 HOH 41  642 642 HOH HOH A . 
Y 8 HOH 42  643 643 HOH HOH A . 
Y 8 HOH 43  644 644 HOH HOH A . 
Y 8 HOH 44  645 645 HOH HOH A . 
Y 8 HOH 45  646 646 HOH HOH A . 
Y 8 HOH 46  647 647 HOH HOH A . 
Y 8 HOH 47  648 648 HOH HOH A . 
Y 8 HOH 48  649 649 HOH HOH A . 
Y 8 HOH 49  650 650 HOH HOH A . 
Y 8 HOH 50  651 651 HOH HOH A . 
Y 8 HOH 51  652 652 HOH HOH A . 
Y 8 HOH 52  653 653 HOH HOH A . 
Y 8 HOH 53  654 654 HOH HOH A . 
Y 8 HOH 54  655 655 HOH HOH A . 
Y 8 HOH 55  656 656 HOH HOH A . 
Y 8 HOH 56  657 657 HOH HOH A . 
Y 8 HOH 57  658 658 HOH HOH A . 
Y 8 HOH 58  659 659 HOH HOH A . 
Y 8 HOH 59  660 660 HOH HOH A . 
Y 8 HOH 60  661 661 HOH HOH A . 
Y 8 HOH 61  662 662 HOH HOH A . 
Y 8 HOH 62  663 663 HOH HOH A . 
Y 8 HOH 63  664 664 HOH HOH A . 
Y 8 HOH 64  665 665 HOH HOH A . 
Y 8 HOH 65  666 666 HOH HOH A . 
Y 8 HOH 66  667 667 HOH HOH A . 
Y 8 HOH 67  668 668 HOH HOH A . 
Y 8 HOH 68  669 669 HOH HOH A . 
Y 8 HOH 69  670 670 HOH HOH A . 
Y 8 HOH 70  671 671 HOH HOH A . 
Y 8 HOH 71  672 672 HOH HOH A . 
Y 8 HOH 72  673 673 HOH HOH A . 
Y 8 HOH 73  674 674 HOH HOH A . 
Y 8 HOH 74  675 675 HOH HOH A . 
Y 8 HOH 75  676 676 HOH HOH A . 
Y 8 HOH 76  677 677 HOH HOH A . 
Y 8 HOH 77  678 678 HOH HOH A . 
Y 8 HOH 78  679 679 HOH HOH A . 
Y 8 HOH 79  680 680 HOH HOH A . 
Y 8 HOH 80  681 681 HOH HOH A . 
Y 8 HOH 81  682 682 HOH HOH A . 
Y 8 HOH 82  683 683 HOH HOH A . 
Y 8 HOH 83  684 684 HOH HOH A . 
Y 8 HOH 84  685 685 HOH HOH A . 
Y 8 HOH 85  686 686 HOH HOH A . 
Y 8 HOH 86  687 687 HOH HOH A . 
Y 8 HOH 87  688 688 HOH HOH A . 
Y 8 HOH 88  689 689 HOH HOH A . 
Y 8 HOH 89  690 690 HOH HOH A . 
Y 8 HOH 90  691 691 HOH HOH A . 
Y 8 HOH 91  692 692 HOH HOH A . 
Y 8 HOH 92  693 693 HOH HOH A . 
Y 8 HOH 93  694 694 HOH HOH A . 
Y 8 HOH 94  695 695 HOH HOH A . 
Y 8 HOH 95  696 696 HOH HOH A . 
Y 8 HOH 96  697 697 HOH HOH A . 
Y 8 HOH 97  698 698 HOH HOH A . 
Y 8 HOH 98  699 699 HOH HOH A . 
Y 8 HOH 99  700 700 HOH HOH A . 
Y 8 HOH 100 701 701 HOH HOH A . 
Y 8 HOH 101 702 702 HOH HOH A . 
Y 8 HOH 102 703 703 HOH HOH A . 
Y 8 HOH 103 704 704 HOH HOH A . 
Y 8 HOH 104 705 705 HOH HOH A . 
Y 8 HOH 105 706 706 HOH HOH A . 
Y 8 HOH 106 707 707 HOH HOH A . 
Y 8 HOH 107 708 708 HOH HOH A . 
Y 8 HOH 108 709 709 HOH HOH A . 
Y 8 HOH 109 710 710 HOH HOH A . 
Y 8 HOH 110 711 711 HOH HOH A . 
Y 8 HOH 111 712 712 HOH HOH A . 
Y 8 HOH 112 713 713 HOH HOH A . 
Y 8 HOH 113 714 714 HOH HOH A . 
Y 8 HOH 114 715 715 HOH HOH A . 
Y 8 HOH 115 716 716 HOH HOH A . 
Y 8 HOH 116 717 717 HOH HOH A . 
Y 8 HOH 117 718 718 HOH HOH A . 
Y 8 HOH 118 719 719 HOH HOH A . 
Y 8 HOH 119 720 720 HOH HOH A . 
Y 8 HOH 120 721 721 HOH HOH A . 
Y 8 HOH 121 722 722 HOH HOH A . 
Y 8 HOH 122 723 723 HOH HOH A . 
Y 8 HOH 123 724 724 HOH HOH A . 
Y 8 HOH 124 725 725 HOH HOH A . 
Y 8 HOH 125 726 726 HOH HOH A . 
Y 8 HOH 126 727 727 HOH HOH A . 
Y 8 HOH 127 728 728 HOH HOH A . 
Y 8 HOH 128 729 729 HOH HOH A . 
Y 8 HOH 129 730 730 HOH HOH A . 
Y 8 HOH 130 731 731 HOH HOH A . 
Y 8 HOH 131 732 732 HOH HOH A . 
Y 8 HOH 132 733 733 HOH HOH A . 
Y 8 HOH 133 734 734 HOH HOH A . 
Y 8 HOH 134 735 735 HOH HOH A . 
Y 8 HOH 135 736 736 HOH HOH A . 
Y 8 HOH 136 737 737 HOH HOH A . 
Y 8 HOH 137 738 738 HOH HOH A . 
Y 8 HOH 138 739 739 HOH HOH A . 
Y 8 HOH 139 740 740 HOH HOH A . 
Y 8 HOH 140 741 741 HOH HOH A . 
Y 8 HOH 141 742 742 HOH HOH A . 
Y 8 HOH 142 743 743 HOH HOH A . 
Y 8 HOH 143 744 744 HOH HOH A . 
Y 8 HOH 144 745 745 HOH HOH A . 
Y 8 HOH 145 746 746 HOH HOH A . 
Y 8 HOH 146 747 747 HOH HOH A . 
Y 8 HOH 147 748 748 HOH HOH A . 
Y 8 HOH 148 749 749 HOH HOH A . 
Y 8 HOH 149 750 750 HOH HOH A . 
Y 8 HOH 150 751 751 HOH HOH A . 
Y 8 HOH 151 752 752 HOH HOH A . 
Y 8 HOH 152 753 753 HOH HOH A . 
Y 8 HOH 153 754 754 HOH HOH A . 
Y 8 HOH 154 755 755 HOH HOH A . 
Y 8 HOH 155 756 756 HOH HOH A . 
Y 8 HOH 156 757 757 HOH HOH A . 
Y 8 HOH 157 758 758 HOH HOH A . 
Y 8 HOH 158 759 759 HOH HOH A . 
Y 8 HOH 159 760 760 HOH HOH A . 
Y 8 HOH 160 761 761 HOH HOH A . 
Y 8 HOH 161 762 762 HOH HOH A . 
Y 8 HOH 162 763 763 HOH HOH A . 
Y 8 HOH 163 764 764 HOH HOH A . 
Y 8 HOH 164 765 765 HOH HOH A . 
Y 8 HOH 165 766 766 HOH HOH A . 
Y 8 HOH 166 767 767 HOH HOH A . 
Y 8 HOH 167 768 768 HOH HOH A . 
Y 8 HOH 168 769 769 HOH HOH A . 
Y 8 HOH 169 770 770 HOH HOH A . 
Y 8 HOH 170 771 771 HOH HOH A . 
Y 8 HOH 171 772 772 HOH HOH A . 
Y 8 HOH 172 773 773 HOH HOH A . 
Y 8 HOH 173 774 774 HOH HOH A . 
Y 8 HOH 174 775 775 HOH HOH A . 
Y 8 HOH 175 776 776 HOH HOH A . 
Y 8 HOH 176 777 777 HOH HOH A . 
Y 8 HOH 177 778 778 HOH HOH A . 
Y 8 HOH 178 779 779 HOH HOH A . 
Y 8 HOH 179 780 780 HOH HOH A . 
Y 8 HOH 180 781 781 HOH HOH A . 
Y 8 HOH 181 782 782 HOH HOH A . 
Y 8 HOH 182 783 783 HOH HOH A . 
Y 8 HOH 183 784 784 HOH HOH A . 
Y 8 HOH 184 785 785 HOH HOH A . 
Y 8 HOH 185 786 786 HOH HOH A . 
Y 8 HOH 186 787 787 HOH HOH A . 
Y 8 HOH 187 788 788 HOH HOH A . 
Y 8 HOH 188 789 789 HOH HOH A . 
Y 8 HOH 189 790 790 HOH HOH A . 
Y 8 HOH 190 791 791 HOH HOH A . 
Y 8 HOH 191 792 792 HOH HOH A . 
Y 8 HOH 192 793 793 HOH HOH A . 
Y 8 HOH 193 794 794 HOH HOH A . 
Y 8 HOH 194 795 795 HOH HOH A . 
Y 8 HOH 195 796 796 HOH HOH A . 
Y 8 HOH 196 797 797 HOH HOH A . 
Y 8 HOH 197 798 798 HOH HOH A . 
Y 8 HOH 198 799 799 HOH HOH A . 
Y 8 HOH 199 800 800 HOH HOH A . 
Y 8 HOH 200 801 801 HOH HOH A . 
Y 8 HOH 201 802 802 HOH HOH A . 
Y 8 HOH 202 803 803 HOH HOH A . 
Y 8 HOH 203 804 804 HOH HOH A . 
Y 8 HOH 204 805 805 HOH HOH A . 
Y 8 HOH 205 806 806 HOH HOH A . 
Y 8 HOH 206 807 807 HOH HOH A . 
Y 8 HOH 207 808 808 HOH HOH A . 
Y 8 HOH 208 809 809 HOH HOH A . 
Y 8 HOH 209 810 810 HOH HOH A . 
Y 8 HOH 210 811 811 HOH HOH A . 
Y 8 HOH 211 812 812 HOH HOH A . 
Y 8 HOH 212 813 813 HOH HOH A . 
Y 8 HOH 213 814 814 HOH HOH A . 
Y 8 HOH 214 815 815 HOH HOH A . 
Y 8 HOH 215 816 816 HOH HOH A . 
Y 8 HOH 216 817 817 HOH HOH A . 
Y 8 HOH 217 818 818 HOH HOH A . 
Y 8 HOH 218 819 819 HOH HOH A . 
Y 8 HOH 219 820 820 HOH HOH A . 
Y 8 HOH 220 821 821 HOH HOH A . 
Y 8 HOH 221 822 822 HOH HOH A . 
Y 8 HOH 222 823 823 HOH HOH A . 
Y 8 HOH 223 824 824 HOH HOH A . 
Y 8 HOH 224 825 825 HOH HOH A . 
Y 8 HOH 225 826 826 HOH HOH A . 
Y 8 HOH 226 827 827 HOH HOH A . 
Y 8 HOH 227 828 828 HOH HOH A . 
Y 8 HOH 228 829 829 HOH HOH A . 
Y 8 HOH 229 830 830 HOH HOH A . 
Y 8 HOH 230 831 831 HOH HOH A . 
Y 8 HOH 231 832 832 HOH HOH A . 
Y 8 HOH 232 833 833 HOH HOH A . 
Y 8 HOH 233 834 834 HOH HOH A . 
Y 8 HOH 234 835 835 HOH HOH A . 
Y 8 HOH 235 836 836 HOH HOH A . 
Y 8 HOH 236 837 837 HOH HOH A . 
Y 8 HOH 237 838 838 HOH HOH A . 
Y 8 HOH 238 839 839 HOH HOH A . 
Y 8 HOH 239 840 840 HOH HOH A . 
Y 8 HOH 240 841 841 HOH HOH A . 
Y 8 HOH 241 842 842 HOH HOH A . 
Y 8 HOH 242 843 843 HOH HOH A . 
Y 8 HOH 243 844 844 HOH HOH A . 
Y 8 HOH 244 845 845 HOH HOH A . 
Y 8 HOH 245 846 846 HOH HOH A . 
Y 8 HOH 246 847 847 HOH HOH A . 
Y 8 HOH 247 848 848 HOH HOH A . 
Y 8 HOH 248 849 849 HOH HOH A . 
Y 8 HOH 249 850 850 HOH HOH A . 
Y 8 HOH 250 851 851 HOH HOH A . 
Y 8 HOH 251 852 852 HOH HOH A . 
Y 8 HOH 252 853 853 HOH HOH A . 
Y 8 HOH 253 854 854 HOH HOH A . 
Y 8 HOH 254 855 855 HOH HOH A . 
Y 8 HOH 255 856 856 HOH HOH A . 
Y 8 HOH 256 857 857 HOH HOH A . 
Y 8 HOH 257 858 858 HOH HOH A . 
Y 8 HOH 258 859 859 HOH HOH A . 
Y 8 HOH 259 860 860 HOH HOH A . 
Y 8 HOH 260 861 861 HOH HOH A . 
Y 8 HOH 261 862 862 HOH HOH A . 
Y 8 HOH 262 863 863 HOH HOH A . 
Y 8 HOH 263 864 864 HOH HOH A . 
Y 8 HOH 264 865 865 HOH HOH A . 
Y 8 HOH 265 866 866 HOH HOH A . 
Y 8 HOH 266 867 867 HOH HOH A . 
Y 8 HOH 267 868 868 HOH HOH A . 
Y 8 HOH 268 869 869 HOH HOH A . 
Y 8 HOH 269 870 870 HOH HOH A . 
Y 8 HOH 270 871 871 HOH HOH A . 
Y 8 HOH 271 872 872 HOH HOH A . 
Y 8 HOH 272 873 873 HOH HOH A . 
Y 8 HOH 273 874 874 HOH HOH A . 
Y 8 HOH 274 875 875 HOH HOH A . 
Y 8 HOH 275 876 876 HOH HOH A . 
Y 8 HOH 276 877 877 HOH HOH A . 
Y 8 HOH 277 878 878 HOH HOH A . 
Y 8 HOH 278 879 879 HOH HOH A . 
Y 8 HOH 279 880 880 HOH HOH A . 
Y 8 HOH 280 881 881 HOH HOH A . 
Y 8 HOH 281 882 882 HOH HOH A . 
Y 8 HOH 282 883 883 HOH HOH A . 
Y 8 HOH 283 884 884 HOH HOH A . 
Y 8 HOH 284 885 885 HOH HOH A . 
Y 8 HOH 285 886 886 HOH HOH A . 
Y 8 HOH 286 887 887 HOH HOH A . 
Y 8 HOH 287 888 888 HOH HOH A . 
Y 8 HOH 288 889 889 HOH HOH A . 
Y 8 HOH 289 890 890 HOH HOH A . 
Y 8 HOH 290 891 891 HOH HOH A . 
Y 8 HOH 291 892 892 HOH HOH A . 
Y 8 HOH 292 893 893 HOH HOH A . 
Y 8 HOH 293 894 894 HOH HOH A . 
Y 8 HOH 294 895 895 HOH HOH A . 
Y 8 HOH 295 896 896 HOH HOH A . 
Y 8 HOH 296 897 897 HOH HOH A . 
Y 8 HOH 297 898 898 HOH HOH A . 
Y 8 HOH 298 899 899 HOH HOH A . 
Y 8 HOH 299 900 900 HOH HOH A . 
Y 8 HOH 300 901 901 HOH HOH A . 
Y 8 HOH 301 902 902 HOH HOH A . 
Y 8 HOH 302 903 903 HOH HOH A . 
Y 8 HOH 303 904 904 HOH HOH A . 
Y 8 HOH 304 905 905 HOH HOH A . 
Y 8 HOH 305 906 906 HOH HOH A . 
Y 8 HOH 306 907 907 HOH HOH A . 
Y 8 HOH 307 908 908 HOH HOH A . 
Y 8 HOH 308 909 909 HOH HOH A . 
Y 8 HOH 309 910 910 HOH HOH A . 
Y 8 HOH 310 911 911 HOH HOH A . 
Y 8 HOH 311 912 912 HOH HOH A . 
Y 8 HOH 312 913 913 HOH HOH A . 
Y 8 HOH 313 914 914 HOH HOH A . 
Y 8 HOH 314 915 915 HOH HOH A . 
Y 8 HOH 315 916 916 HOH HOH A . 
Y 8 HOH 316 917 917 HOH HOH A . 
Y 8 HOH 317 918 918 HOH HOH A . 
Y 8 HOH 318 919 919 HOH HOH A . 
Y 8 HOH 319 920 920 HOH HOH A . 
Y 8 HOH 320 921 921 HOH HOH A . 
Y 8 HOH 321 922 922 HOH HOH A . 
Y 8 HOH 322 923 923 HOH HOH A . 
Y 8 HOH 323 924 924 HOH HOH A . 
Y 8 HOH 324 925 925 HOH HOH A . 
Y 8 HOH 325 926 926 HOH HOH A . 
Y 8 HOH 326 927 927 HOH HOH A . 
Y 8 HOH 327 928 928 HOH HOH A . 
Y 8 HOH 328 929 929 HOH HOH A . 
Y 8 HOH 329 930 930 HOH HOH A . 
Y 8 HOH 330 931 931 HOH HOH A . 
Y 8 HOH 331 932 932 HOH HOH A . 
Y 8 HOH 332 933 933 HOH HOH A . 
Y 8 HOH 333 934 934 HOH HOH A . 
Y 8 HOH 334 935 935 HOH HOH A . 
Y 8 HOH 335 936 936 HOH HOH A . 
Y 8 HOH 336 937 937 HOH HOH A . 
Y 8 HOH 337 938 938 HOH HOH A . 
Y 8 HOH 338 939 939 HOH HOH A . 
Y 8 HOH 339 940 940 HOH HOH A . 
Y 8 HOH 340 941 941 HOH HOH A . 
Y 8 HOH 341 942 942 HOH HOH A . 
Y 8 HOH 342 943 943 HOH HOH A . 
Y 8 HOH 343 944 944 HOH HOH A . 
Y 8 HOH 344 945 945 HOH HOH A . 
Y 8 HOH 345 946 946 HOH HOH A . 
Y 8 HOH 346 947 947 HOH HOH A . 
Y 8 HOH 347 949 949 HOH HOH A . 
Y 8 HOH 348 950 950 HOH HOH A . 
Y 8 HOH 349 951 951 HOH HOH A . 
Y 8 HOH 350 952 952 HOH HOH A . 
Y 8 HOH 351 953 953 HOH HOH A . 
Y 8 HOH 352 954 954 HOH HOH A . 
Y 8 HOH 353 955 955 HOH HOH A . 
Y 8 HOH 354 956 956 HOH HOH A . 
Y 8 HOH 355 957 957 HOH HOH A . 
Y 8 HOH 356 958 958 HOH HOH A . 
Y 8 HOH 357 959 959 HOH HOH A . 
Y 8 HOH 358 960 960 HOH HOH A . 
Y 8 HOH 359 961 961 HOH HOH A . 
Y 8 HOH 360 962 962 HOH HOH A . 
Y 8 HOH 361 963 963 HOH HOH A . 
Y 8 HOH 362 964 964 HOH HOH A . 
Y 8 HOH 363 965 965 HOH HOH A . 
Y 8 HOH 364 966 966 HOH HOH A . 
Y 8 HOH 365 967 967 HOH HOH A . 
Y 8 HOH 366 968 968 HOH HOH A . 
Y 8 HOH 367 969 969 HOH HOH A . 
Y 8 HOH 368 970 970 HOH HOH A . 
Y 8 HOH 369 971 971 HOH HOH A . 
Y 8 HOH 370 972 972 HOH HOH A . 
Y 8 HOH 371 973 973 HOH HOH A . 
Y 8 HOH 372 974 974 HOH HOH A . 
Y 8 HOH 373 975 975 HOH HOH A . 
Y 8 HOH 374 976 976 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' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           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                     9G5M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.774 
_cell.length_a_esd                 ? 
_cell.length_b                     100.774 
_cell.length_b_esd                 ? 
_cell.length_c                     125.721 
_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                         9G5M 
_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                   9G5M 
_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             3.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.25 
_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    
'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 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 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         2022-08-03 
_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                                       9G5M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.270 
_reflns.d_resolution_low                               125.720 
_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                                     34890 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.800 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7000 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.21400 
_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                                    2.27 
_reflns_shell.d_res_low                                     2.33 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             820 
_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                               7.90 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.24600 
_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                               34.00 
_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                                 9G5M 
_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                            2.27 
_refine.ls_d_res_low                             71.69 
_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                     34842 
_refine.ls_number_reflns_R_free                  1729 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.194 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.157 
_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                    ? 
_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                          ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            randown 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_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                       2.27 
_refine_hist.d_res_low                        71.69 
_refine_hist.number_atoms_solvent             378 
_refine_hist.number_atoms_total               4201 
_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        3699 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         124 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.27 
_refine_ls_shell.d_res_low                        2.33 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                2881 
_refine_ls_shell.number_reflns_R_free             154 
_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                  0.2281 
_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                  0.2576 
# 
_struct.entry_id                     9G5M 
_struct.title                        'N-Acyl-D-amino-acid deacylase (D-acylase) from Klebsiella pneumoniae in an open conformation' 
_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        9G5M 
_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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 4 ? 
H N N 6 ? 
I N N 5 ? 
J N N 3 ? 
K N N 5 ? 
L N N 3 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 3 ? 
T N N 4 ? 
U N N 4 ? 
V N N 6 ? 
W N N 7 ? 
X N N 7 ? 
Y N N 8 ? 
# 
_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              9G5M 
_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 9G5M HIS A 480 ? UNP W9BIW9 ? ? 'expression tag' 480 1 
1 9G5M HIS A 481 ? UNP W9BIW9 ? ? 'expression tag' 481 2 
1 9G5M HIS A 482 ? UNP W9BIW9 ? ? 'expression tag' 482 3 
1 9G5M HIS A 483 ? UNP W9BIW9 ? ? 'expression tag' 483 4 
1 9G5M HIS A 484 ? UNP W9BIW9 ? ? 'expression tag' 484 5 
1 9G5M 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)' 4650  ? 
1 MORE         -70   ? 
1 'SSA (A^2)'  18130 ? 
# 
_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,M,N,O,P,Q,R,S,T,U,V,W,X,Y 
# 
_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 ASP A 289 ? VAL A 293 ? ASP A 289 VAL A 293 5 ? 5  
HELX_P HELX_P15 AB6 GLN A 307 ? ALA A 311 ? GLN A 307 ALA A 311 5 ? 5  
HELX_P HELX_P16 AB7 THR A 314 ? GLN A 323 ? THR A 314 GLN A 323 1 ? 10 
HELX_P HELX_P17 AB8 SER A 325 ? MET A 334 ? SER A 325 MET A 334 1 ? 10 
HELX_P HELX_P18 AB9 ASP A 344 ? TYR A 354 ? ASP A 344 TYR A 354 1 ? 11 
HELX_P HELX_P19 AC1 PRO A 372 ? GLY A 383 ? PRO A 372 GLY A 383 1 ? 12 
HELX_P HELX_P20 AC2 PRO A 393 ? LYS A 400 ? PRO A 393 LYS A 400 1 ? 8  
HELX_P HELX_P21 AC3 THR A 402 ? GLN A 410 ? THR A 402 GLN A 410 1 ? 9  
# 
_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 64  NE2 ? ? ? 1_555 W NI . NI ? ? A HIS 64  A NI 522 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc2 metalc ? ? A CYS 91  SG  ? ? ? 1_555 W NI . NI ? ? A CYS 91  A NI 522 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc3 metalc ? ? A CYS 91  SG  ? ? ? 1_555 X NI . NI ? ? A CYS 91  A NI 523 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc4 metalc ? ? A HIS 216 ND1 ? ? ? 1_555 X NI . NI ? ? A HIS 216 A NI 523 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc5 metalc ? ? A HIS 246 NE2 ? ? ? 1_555 X NI . NI ? ? A HIS 246 A NI 523 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc6 metalc ? ? A ASP 362 OD1 ? ? ? 1_555 W NI . NI ? ? A ASP 362 A NI 522 1_555 ? ? ? ? ? ? ? 2.671 ? ? 
metalc7 metalc ? ? O SO4 .   O3  ? ? ? 1_555 W NI . NI ? ? A SO4 514 A NI 522 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc8 metalc ? ? O SO4 .   O4  ? ? ? 1_555 X NI . NI ? ? A SO4 514 A NI 523 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
# 
_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 64  ? A HIS 64  ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 SG  ? A CYS 91  ? A CYS 91  ? 1_555 115.3 ? 
2  NE2 ? A HIS 64  ? A HIS 64  ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 OD1 ? A ASP 362 ? A ASP 362 ? 1_555 88.2  ? 
3  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 OD1 ? A ASP 362 ? A ASP 362 ? 1_555 155.0 ? 
4  NE2 ? A HIS 64  ? A HIS 64  ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 O3  ? O SO4 .   ? A SO4 514 ? 1_555 98.0  ? 
5  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 O3  ? O SO4 .   ? A SO4 514 ? 1_555 100.3 ? 
6  OD1 ? A ASP 362 ? A ASP 362 ? 1_555 NI ? W NI . ? A NI 522 ? 1_555 O3  ? O SO4 .   ? A SO4 514 ? 1_555 66.2  ? 
7  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 ND1 ? A HIS 216 ? A HIS 216 ? 1_555 124.8 ? 
8  SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 111.0 ? 
9  ND1 ? A HIS 216 ? A HIS 216 ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 95.4  ? 
10 SG  ? A CYS 91  ? A CYS 91  ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 O4  ? O SO4 .   ? A SO4 514 ? 1_555 116.3 ? 
11 ND1 ? A HIS 216 ? A HIS 216 ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 O4  ? O SO4 .   ? A SO4 514 ? 1_555 94.4  ? 
12 NE2 ? A HIS 246 ? A HIS 246 ? 1_555 NI ? X NI . ? A NI 523 ? 1_555 O4  ? O SO4 .   ? A SO4 514 ? 1_555 112.6 ? 
# 
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 -1.43 
2 ASP 106 A . ? ASP 106 A PRO 107 A ? PRO 107 A 1 -0.92 
3 MET 334 A . ? MET 334 A PRO 335 A ? PRO 335 A 1 -5.11 
# 
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 VAL A 25  ? O VAL A 25  N PHE A 7   ? N PHE A 7   
AA1 3 4 N LYS A 8   ? N LYS A 8   O ILE A 47  ? O ILE A 47  
AA2 1 2 O ALA A 36  ? O ALA A 36  N ASP A 24  ? N ASP A 24  
AA2 2 3 O VAL A 25  ? O VAL A 25  N PHE A 7   ? N PHE A 7   
AA2 3 4 N THR A 11  ? N THR A 11  O LEU A 54  ? O LEU A 54  
AA2 4 5 N ALA A 55  ? N ALA A 55  O VAL A 426 ? O VAL A 426 
AA2 5 6 N LEU A 427 ? N LEU A 427 O ALA A 451 ? O ALA A 451 
AA2 6 7 N VAL A 452 ? N VAL A 452 O SER A 459 ? O SER A 459 
AA3 1 2 N ASP A 60  ? N ASP A 60  O THR A 85  ? O THR A 85  
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 GLY A 181 ? O GLY A 181 
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 242 ? N VAL A 242 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 286 ? N SER A 286 O ALA A 338 ? O ALA A 338 
AA5 2 3 O ILE A 339 ? O ILE A 339 N VAL A 300 ? N VAL A 300 
# 
_pdbx_entry_details.entry_id                   9G5M 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 97  ? ? 74.17   -3.94   
2 1 PHE A 156 ? ? -95.18  43.97   
3 1 PHE A 221 ? ? -118.80 -134.62 
4 1 PRO A 223 ? ? -85.31  34.81   
5 1 HIS A 246 ? ? 24.01   59.83   
6 1 THR A 402 ? ? -141.07 -91.14  
# 
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 -28.8483 38.1881 11.5890  0.1576 ? -0.0065 ? -0.0063 ? 0.2569 ? -0.0125 ? 0.1584 ? 1.4302 ? 0.3316 
? 0.0473  ? 1.9865 ? -0.6590 ? 2.2426 ? -0.0189 ? 0.0546  ? 0.0067  ? -0.0316 ? -0.0275 ? -0.1424 ? -0.0346 ? 0.2054  ? 0.0437  ? 
2 'X-RAY DIFFRACTION' ? refined -21.1927 36.3316 27.0062  0.1840 ? -0.0400 ? -0.0155 ? 0.2914 ? 0.0294  ? 0.1301 ? 4.9200 ? 0.2389 
? 1.0319  ? 2.4751 ? 1.4492  ? 1.1243 ? 0.1820  ? -0.2258 ? -0.2573 ? 0.1713  ? -0.1160 ? -0.2587 ? 0.1784  ? 0.0283  ? -0.0501 ? 
3 'X-RAY DIFFRACTION' ? refined -43.2241 29.0565 5.8206   0.2637 ? 0.0019  ? -0.0094 ? 0.2572 ? -0.0145 ? 0.1573 ? 2.3313 ? 0.1869 
? -0.3080 ? 1.3437 ? -0.7415 ? 0.7326 ? 0.0615  ? 0.2763  ? -0.1938 ? -0.2271 ? -0.0296 ? 0.1046  ? 0.2299  ? 0.0004  ? -0.0441 ? 
4 'X-RAY DIFFRACTION' ? refined -52.5570 46.9651 3.5028   0.2563 ? 0.0322  ? -0.0005 ? 0.3032 ? 0.0257  ? 0.1962 ? 1.5230 ? 0.2991 
? -0.2943 ? 0.8586 ? -0.0212 ? 0.9265 ? 0.0131  ? 0.2002  ? 0.1166  ? -0.1106 ? -0.0069 ? 0.0349  ? -0.1369 ? -0.1558 ? -0.0106 ? 
5 'X-RAY DIFFRACTION' ? refined -35.0871 42.2951 -14.7307 0.2169 ? -0.0631 ? -0.0095 ? 0.2990 ? 0.0090  ? 0.2109 ? 0.2995 ? 
-0.0444 ? -0.4137 ? 0.1859 ? 1.1256  ? 6.4662 ? -0.0131 ? 0.0944  ? -0.0075 ? -0.0822 ? 0.0267  ? -0.0141 ? 0.1159  ? -0.1162 ? 
-0.0206 ? 
# 
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 372 through 479 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 52 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 53 through 143 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 144 through 283 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 284 through 371 )
;
# 
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 HIS 480 ? A HIS 480 
2 1 Y 1 A HIS 481 ? A HIS 481 
3 1 Y 1 A HIS 482 ? A HIS 482 
4 1 Y 1 A HIS 483 ? A HIS 483 
5 1 Y 1 A HIS 484 ? A HIS 484 
6 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 
GOL C1   C  N N 147 
GOL O1   O  N N 148 
GOL C2   C  N N 149 
GOL O2   O  N N 150 
GOL C3   C  N N 151 
GOL O3   O  N N 152 
GOL H11  H  N N 153 
GOL H12  H  N N 154 
GOL HO1  H  N N 155 
GOL H2   H  N N 156 
GOL HO2  H  N N 157 
GOL H31  H  N N 158 
GOL H32  H  N N 159 
GOL HO3  H  N N 160 
HIS N    N  N N 161 
HIS CA   C  N S 162 
HIS C    C  N N 163 
HIS O    O  N N 164 
HIS CB   C  N N 165 
HIS CG   C  Y N 166 
HIS ND1  N  Y N 167 
HIS CD2  C  Y N 168 
HIS CE1  C  Y N 169 
HIS NE2  N  Y N 170 
HIS OXT  O  N N 171 
HIS H    H  N N 172 
HIS H2   H  N N 173 
HIS HA   H  N N 174 
HIS HB2  H  N N 175 
HIS HB3  H  N N 176 
HIS HD1  H  N N 177 
HIS HD2  H  N N 178 
HIS HE1  H  N N 179 
HIS HE2  H  N N 180 
HIS HXT  H  N N 181 
HOH O    O  N N 182 
HOH H1   H  N N 183 
HOH H2   H  N N 184 
ILE N    N  N N 185 
ILE CA   C  N S 186 
ILE C    C  N N 187 
ILE O    O  N N 188 
ILE CB   C  N S 189 
ILE CG1  C  N N 190 
ILE CG2  C  N N 191 
ILE CD1  C  N N 192 
ILE OXT  O  N N 193 
ILE H    H  N N 194 
ILE H2   H  N N 195 
ILE HA   H  N N 196 
ILE HB   H  N N 197 
ILE HG12 H  N N 198 
ILE HG13 H  N N 199 
ILE HG21 H  N N 200 
ILE HG22 H  N N 201 
ILE HG23 H  N N 202 
ILE HD11 H  N N 203 
ILE HD12 H  N N 204 
ILE HD13 H  N N 205 
ILE HXT  H  N N 206 
LEU N    N  N N 207 
LEU CA   C  N S 208 
LEU C    C  N N 209 
LEU O    O  N N 210 
LEU CB   C  N N 211 
LEU CG   C  N N 212 
LEU CD1  C  N N 213 
LEU CD2  C  N N 214 
LEU OXT  O  N N 215 
LEU H    H  N N 216 
LEU H2   H  N N 217 
LEU HA   H  N N 218 
LEU HB2  H  N N 219 
LEU HB3  H  N N 220 
LEU HG   H  N N 221 
LEU HD11 H  N N 222 
LEU HD12 H  N N 223 
LEU HD13 H  N N 224 
LEU HD21 H  N N 225 
LEU HD22 H  N N 226 
LEU HD23 H  N N 227 
LEU HXT  H  N N 228 
LYS N    N  N N 229 
LYS CA   C  N S 230 
LYS C    C  N N 231 
LYS O    O  N N 232 
LYS CB   C  N N 233 
LYS CG   C  N N 234 
LYS CD   C  N N 235 
LYS CE   C  N N 236 
LYS NZ   N  N N 237 
LYS OXT  O  N N 238 
LYS H    H  N N 239 
LYS H2   H  N N 240 
LYS HA   H  N N 241 
LYS HB2  H  N N 242 
LYS HB3  H  N N 243 
LYS HG2  H  N N 244 
LYS HG3  H  N N 245 
LYS HD2  H  N N 246 
LYS HD3  H  N N 247 
LYS HE2  H  N N 248 
LYS HE3  H  N N 249 
LYS HZ1  H  N N 250 
LYS HZ2  H  N N 251 
LYS HZ3  H  N N 252 
LYS HXT  H  N N 253 
MET N    N  N N 254 
MET CA   C  N S 255 
MET C    C  N N 256 
MET O    O  N N 257 
MET CB   C  N N 258 
MET CG   C  N N 259 
MET SD   S  N N 260 
MET CE   C  N N 261 
MET OXT  O  N N 262 
MET H    H  N N 263 
MET H2   H  N N 264 
MET HA   H  N N 265 
MET HB2  H  N N 266 
MET HB3  H  N N 267 
MET HG2  H  N N 268 
MET HG3  H  N N 269 
MET HE1  H  N N 270 
MET HE2  H  N N 271 
MET HE3  H  N N 272 
MET HXT  H  N N 273 
NI  NI   NI N N 274 
PEG C1   C  N N 275 
PEG O1   O  N N 276 
PEG C2   C  N N 277 
PEG O2   O  N N 278 
PEG C3   C  N N 279 
PEG C4   C  N N 280 
PEG O4   O  N N 281 
PEG H11  H  N N 282 
PEG H12  H  N N 283 
PEG HO1  H  N N 284 
PEG H21  H  N N 285 
PEG H22  H  N N 286 
PEG H31  H  N N 287 
PEG H32  H  N N 288 
PEG H41  H  N N 289 
PEG H42  H  N N 290 
PEG HO4  H  N N 291 
PGE C1   C  N N 292 
PGE O1   O  N N 293 
PGE C2   C  N N 294 
PGE O2   O  N N 295 
PGE C3   C  N N 296 
PGE C4   C  N N 297 
PGE O4   O  N N 298 
PGE C6   C  N N 299 
PGE C5   C  N N 300 
PGE O3   O  N N 301 
PGE H1   H  N N 302 
PGE H12  H  N N 303 
PGE HO1  H  N N 304 
PGE H2   H  N N 305 
PGE H22  H  N N 306 
PGE H3   H  N N 307 
PGE H32  H  N N 308 
PGE H4   H  N N 309 
PGE H42  H  N N 310 
PGE HO4  H  N N 311 
PGE H6   H  N N 312 
PGE H62  H  N N 313 
PGE H5   H  N N 314 
PGE H52  H  N N 315 
PHE N    N  N N 316 
PHE CA   C  N S 317 
PHE C    C  N N 318 
PHE O    O  N N 319 
PHE CB   C  N N 320 
PHE CG   C  Y N 321 
PHE CD1  C  Y N 322 
PHE CD2  C  Y N 323 
PHE CE1  C  Y N 324 
PHE CE2  C  Y N 325 
PHE CZ   C  Y N 326 
PHE OXT  O  N N 327 
PHE H    H  N N 328 
PHE H2   H  N N 329 
PHE HA   H  N N 330 
PHE HB2  H  N N 331 
PHE HB3  H  N N 332 
PHE HD1  H  N N 333 
PHE HD2  H  N N 334 
PHE HE1  H  N N 335 
PHE HE2  H  N N 336 
PHE HZ   H  N N 337 
PHE HXT  H  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
SO4 S    S  N N 370 
SO4 O1   O  N N 371 
SO4 O2   O  N N 372 
SO4 O3   O  N N 373 
SO4 O4   O  N N 374 
THR N    N  N N 375 
THR CA   C  N S 376 
THR C    C  N N 377 
THR O    O  N N 378 
THR CB   C  N R 379 
THR OG1  O  N N 380 
THR CG2  C  N N 381 
THR OXT  O  N N 382 
THR H    H  N N 383 
THR H2   H  N N 384 
THR HA   H  N N 385 
THR HB   H  N N 386 
THR HG1  H  N N 387 
THR HG21 H  N N 388 
THR HG22 H  N N 389 
THR HG23 H  N N 390 
THR HXT  H  N N 391 
TRP N    N  N N 392 
TRP CA   C  N S 393 
TRP C    C  N N 394 
TRP O    O  N N 395 
TRP CB   C  N N 396 
TRP CG   C  Y N 397 
TRP CD1  C  Y N 398 
TRP CD2  C  Y N 399 
TRP NE1  N  Y N 400 
TRP CE2  C  Y N 401 
TRP CE3  C  Y N 402 
TRP CZ2  C  Y N 403 
TRP CZ3  C  Y N 404 
TRP CH2  C  Y N 405 
TRP OXT  O  N N 406 
TRP H    H  N N 407 
TRP H2   H  N N 408 
TRP HA   H  N N 409 
TRP HB2  H  N N 410 
TRP HB3  H  N N 411 
TRP HD1  H  N N 412 
TRP HE1  H  N N 413 
TRP HE3  H  N N 414 
TRP HZ2  H  N N 415 
TRP HZ3  H  N N 416 
TRP HH2  H  N N 417 
TRP HXT  H  N N 418 
TYR N    N  N N 419 
TYR CA   C  N S 420 
TYR C    C  N N 421 
TYR O    O  N N 422 
TYR CB   C  N N 423 
TYR CG   C  Y N 424 
TYR CD1  C  Y N 425 
TYR CD2  C  Y N 426 
TYR CE1  C  Y N 427 
TYR CE2  C  Y N 428 
TYR CZ   C  Y N 429 
TYR OH   O  N N 430 
TYR OXT  O  N N 431 
TYR H    H  N N 432 
TYR H2   H  N N 433 
TYR HA   H  N N 434 
TYR HB2  H  N N 435 
TYR HB3  H  N N 436 
TYR HD1  H  N N 437 
TYR HD2  H  N N 438 
TYR HE1  H  N N 439 
TYR HE2  H  N N 440 
TYR HH   H  N N 441 
TYR HXT  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
# 
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 
GOL C1  O1   sing N N 138 
GOL C1  C2   sing N N 139 
GOL C1  H11  sing N N 140 
GOL C1  H12  sing N N 141 
GOL O1  HO1  sing N N 142 
GOL C2  O2   sing N N 143 
GOL C2  C3   sing N N 144 
GOL C2  H2   sing N N 145 
GOL O2  HO2  sing N N 146 
GOL C3  O3   sing N N 147 
GOL C3  H31  sing N N 148 
GOL C3  H32  sing N N 149 
GOL O3  HO3  sing N N 150 
HIS N   CA   sing N N 151 
HIS N   H    sing N N 152 
HIS N   H2   sing N N 153 
HIS CA  C    sing N N 154 
HIS CA  CB   sing N N 155 
HIS CA  HA   sing N N 156 
HIS C   O    doub N N 157 
HIS C   OXT  sing N N 158 
HIS CB  CG   sing N N 159 
HIS CB  HB2  sing N N 160 
HIS CB  HB3  sing N N 161 
HIS CG  ND1  sing Y N 162 
HIS CG  CD2  doub Y N 163 
HIS ND1 CE1  doub Y N 164 
HIS ND1 HD1  sing N N 165 
HIS CD2 NE2  sing Y N 166 
HIS CD2 HD2  sing N N 167 
HIS CE1 NE2  sing Y N 168 
HIS CE1 HE1  sing N N 169 
HIS NE2 HE2  sing N N 170 
HIS OXT HXT  sing N N 171 
HOH O   H1   sing N N 172 
HOH O   H2   sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
PEG C1  O1   sing N N 259 
PEG C1  C2   sing N N 260 
PEG C1  H11  sing N N 261 
PEG C1  H12  sing N N 262 
PEG O1  HO1  sing N N 263 
PEG C2  O2   sing N N 264 
PEG C2  H21  sing N N 265 
PEG C2  H22  sing N N 266 
PEG O2  C3   sing N N 267 
PEG C3  C4   sing N N 268 
PEG C3  H31  sing N N 269 
PEG C3  H32  sing N N 270 
PEG C4  O4   sing N N 271 
PEG C4  H41  sing N N 272 
PEG C4  H42  sing N N 273 
PEG O4  HO4  sing N N 274 
PGE C1  O1   sing N N 275 
PGE C1  C2   sing N N 276 
PGE C1  H1   sing N N 277 
PGE C1  H12  sing N N 278 
PGE O1  HO1  sing N N 279 
PGE C2  O2   sing N N 280 
PGE C2  H2   sing N N 281 
PGE C2  H22  sing N N 282 
PGE O2  C3   sing N N 283 
PGE C3  C4   sing N N 284 
PGE C3  H3   sing N N 285 
PGE C3  H32  sing N N 286 
PGE C4  O3   sing N N 287 
PGE C4  H4   sing N N 288 
PGE C4  H42  sing N N 289 
PGE O4  C6   sing N N 290 
PGE O4  HO4  sing N N 291 
PGE C6  C5   sing N N 292 
PGE C6  H6   sing N N 293 
PGE C6  H62  sing N N 294 
PGE C5  O3   sing N N 295 
PGE C5  H5   sing N N 296 
PGE C5  H52  sing N N 297 
PHE N   CA   sing N N 298 
PHE N   H    sing N N 299 
PHE N   H2   sing N N 300 
PHE CA  C    sing N N 301 
PHE CA  CB   sing N N 302 
PHE CA  HA   sing N N 303 
PHE C   O    doub N N 304 
PHE C   OXT  sing N N 305 
PHE CB  CG   sing N N 306 
PHE CB  HB2  sing N N 307 
PHE CB  HB3  sing N N 308 
PHE CG  CD1  doub Y N 309 
PHE CG  CD2  sing Y N 310 
PHE CD1 CE1  sing Y N 311 
PHE CD1 HD1  sing N N 312 
PHE CD2 CE2  doub Y N 313 
PHE CD2 HD2  sing N N 314 
PHE CE1 CZ   doub Y N 315 
PHE CE1 HE1  sing N N 316 
PHE CE2 CZ   sing Y N 317 
PHE CE2 HE2  sing N N 318 
PHE CZ  HZ   sing N N 319 
PHE OXT HXT  sing N N 320 
PRO N   CA   sing N N 321 
PRO N   CD   sing N N 322 
PRO N   H    sing N N 323 
PRO CA  C    sing N N 324 
PRO CA  CB   sing N N 325 
PRO CA  HA   sing N N 326 
PRO C   O    doub N N 327 
PRO C   OXT  sing N N 328 
PRO CB  CG   sing N N 329 
PRO CB  HB2  sing N N 330 
PRO CB  HB3  sing N N 331 
PRO CG  CD   sing N N 332 
PRO CG  HG2  sing N N 333 
PRO CG  HG3  sing N N 334 
PRO CD  HD2  sing N N 335 
PRO CD  HD3  sing N N 336 
PRO OXT HXT  sing N N 337 
SER N   CA   sing N N 338 
SER N   H    sing N N 339 
SER N   H2   sing N N 340 
SER CA  C    sing N N 341 
SER CA  CB   sing N N 342 
SER CA  HA   sing N N 343 
SER C   O    doub N N 344 
SER C   OXT  sing N N 345 
SER CB  OG   sing N N 346 
SER CB  HB2  sing N N 347 
SER CB  HB3  sing N N 348 
SER OG  HG   sing N N 349 
SER OXT HXT  sing N N 350 
SO4 S   O1   doub N N 351 
SO4 S   O2   doub N N 352 
SO4 S   O3   sing N N 353 
SO4 S   O4   sing N N 354 
THR N   CA   sing N N 355 
THR N   H    sing N N 356 
THR N   H2   sing N N 357 
THR CA  C    sing N N 358 
THR CA  CB   sing N N 359 
THR CA  HA   sing N N 360 
THR C   O    doub N N 361 
THR C   OXT  sing N N 362 
THR CB  OG1  sing N N 363 
THR CB  CG2  sing N N 364 
THR CB  HB   sing N N 365 
THR OG1 HG1  sing N N 366 
THR CG2 HG21 sing N N 367 
THR CG2 HG22 sing N N 368 
THR CG2 HG23 sing N N 369 
THR OXT HXT  sing N N 370 
TRP N   CA   sing N N 371 
TRP N   H    sing N N 372 
TRP N   H2   sing N N 373 
TRP CA  C    sing N N 374 
TRP CA  CB   sing N N 375 
TRP CA  HA   sing N N 376 
TRP C   O    doub N N 377 
TRP C   OXT  sing N N 378 
TRP CB  CG   sing N N 379 
TRP CB  HB2  sing N N 380 
TRP CB  HB3  sing N N 381 
TRP CG  CD1  doub Y N 382 
TRP CG  CD2  sing Y N 383 
TRP CD1 NE1  sing Y N 384 
TRP CD1 HD1  sing N N 385 
TRP CD2 CE2  doub Y N 386 
TRP CD2 CE3  sing Y N 387 
TRP NE1 CE2  sing Y N 388 
TRP NE1 HE1  sing N N 389 
TRP CE2 CZ2  sing Y N 390 
TRP CE3 CZ3  doub Y N 391 
TRP CE3 HE3  sing N N 392 
TRP CZ2 CH2  doub Y N 393 
TRP CZ2 HZ2  sing N N 394 
TRP CZ3 CH2  sing Y N 395 
TRP CZ3 HZ3  sing N N 396 
TRP CH2 HH2  sing N N 397 
TRP OXT HXT  sing N N 398 
TYR N   CA   sing N N 399 
TYR N   H    sing N N 400 
TYR N   H2   sing N N 401 
TYR CA  C    sing N N 402 
TYR CA  CB   sing N N 403 
TYR CA  HA   sing N N 404 
TYR C   O    doub N N 405 
TYR C   OXT  sing N N 406 
TYR CB  CG   sing N N 407 
TYR CB  HB2  sing N N 408 
TYR CB  HB3  sing N N 409 
TYR CG  CD1  doub Y N 410 
TYR CG  CD2  sing Y N 411 
TYR CD1 CE1  sing Y N 412 
TYR CD1 HD1  sing N N 413 
TYR CD2 CE2  doub Y N 414 
TYR CD2 HD2  sing N N 415 
TYR CE1 CZ   doub Y N 416 
TYR CE1 HE1  sing N N 417 
TYR CE2 CZ   sing Y N 418 
TYR CE2 HE2  sing N N 419 
TYR CZ  OH   sing N N 420 
TYR OH  HH   sing N N 421 
TYR OXT HXT  sing N N 422 
VAL N   CA   sing N N 423 
VAL N   H    sing N N 424 
VAL N   H2   sing N N 425 
VAL CA  C    sing N N 426 
VAL CA  CB   sing N N 427 
VAL CA  HA   sing N N 428 
VAL C   O    doub N N 429 
VAL C   OXT  sing N N 430 
VAL CB  CG1  sing N N 431 
VAL CB  CG2  sing N N 432 
VAL CB  HB   sing N N 433 
VAL CG1 HG11 sing N N 434 
VAL CG1 HG12 sing N N 435 
VAL CG1 HG13 sing N N 436 
VAL CG2 HG21 sing N N 437 
VAL CG2 HG22 sing N N 438 
VAL CG2 HG23 sing N N 439 
VAL OXT HXT  sing N N 440 
# 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G5M 
_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]   0.009923 
_atom_sites.fract_transf_matrix[1][2]   0.005729 
_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]   0.011458 
_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]   0.007954 
_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  
H  
N  
NI 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 1   ? -21.451 30.041 38.779  1.00 73.76  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? -22.336 29.063 38.158  1.00 76.59  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? -21.658 28.411 36.975  1.00 69.06  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? -20.959 29.081 36.215  1.00 77.34  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? -23.643 29.711 37.683  1.00 65.79  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? -24.173 30.799 38.587  1.00 72.25  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? -23.125 32.261 38.545  1.00 101.66 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? -23.608 33.015 37.002  1.00 58.45  ? 1   MET A CE  1 
ATOM   9    N  N   . LYS A 1 2   ? -21.855 27.106 36.819  1.00 67.47  ? 2   LYS A N   1 
ATOM   10   C  CA  . LYS A 1 2   ? -21.576 26.475 35.536  1.00 69.29  ? 2   LYS A CA  1 
ATOM   11   C  C   . LYS A 1 2   ? -22.581 26.978 34.506  1.00 56.21  ? 2   LYS A C   1 
ATOM   12   O  O   . LYS A 1 2   ? -23.790 26.993 34.761  1.00 60.65  ? 2   LYS A O   1 
ATOM   13   C  CB  . LYS A 1 2   ? -21.654 24.953 35.658  1.00 73.63  ? 2   LYS A CB  1 
ATOM   14   C  CG  . LYS A 1 2   ? -21.329 24.199 34.366  1.00 65.53  ? 2   LYS A CG  1 
ATOM   15   C  CD  . LYS A 1 2   ? -19.825 24.136 34.122  1.00 52.42  ? 2   LYS A CD  1 
ATOM   16   C  CE  . LYS A 1 2   ? -19.451 22.927 33.268  1.00 53.83  ? 2   LYS A CE  1 
ATOM   17   N  NZ  . LYS A 1 2   ? -18.011 22.543 33.390  1.00 54.64  ? 2   LYS A NZ  1 
ATOM   18   N  N   . VAL A 1 3   ? -22.087 27.415 33.350  1.00 45.07  ? 3   VAL A N   1 
ATOM   19   C  CA  . VAL A 1 3   ? -22.955 27.844 32.264  1.00 36.13  ? 3   VAL A CA  1 
ATOM   20   C  C   . VAL A 1 3   ? -22.706 26.944 31.055  1.00 33.03  ? 3   VAL A C   1 
ATOM   21   O  O   . VAL A 1 3   ? -21.774 26.141 31.026  1.00 33.87  ? 3   VAL A O   1 
ATOM   22   C  CB  . VAL A 1 3   ? -22.766 29.332 31.908  1.00 33.45  ? 3   VAL A CB  1 
ATOM   23   C  CG1 . VAL A 1 3   ? -22.919 30.195 33.159  1.00 33.63  ? 3   VAL A CG1 1 
ATOM   24   C  CG2 . VAL A 1 3   ? -21.409 29.560 31.261  1.00 29.80  ? 3   VAL A CG2 1 
ATOM   25   N  N   . ASP A 1 4   ? -23.579 27.065 30.059  1.00 28.43  ? 4   ASP A N   1 
ATOM   26   C  CA  . ASP A 1 4   ? -23.395 26.274 28.845  1.00 37.44  ? 4   ASP A CA  1 
ATOM   27   C  C   . ASP A 1 4   ? -22.417 26.940 27.891  1.00 31.19  ? 4   ASP A C   1 
ATOM   28   O  O   . ASP A 1 4   ? -21.514 26.282 27.360  1.00 31.17  ? 4   ASP A O   1 
ATOM   29   C  CB  . ASP A 1 4   ? -24.739 26.047 28.153  1.00 31.08  ? 4   ASP A CB  1 
ATOM   30   C  CG  . ASP A 1 4   ? -25.637 25.131 28.947  1.00 35.48  ? 4   ASP A CG  1 
ATOM   31   O  OD1 . ASP A 1 4   ? -25.154 24.063 29.353  1.00 40.98  ? 4   ASP A OD1 1 
ATOM   32   O  OD2 . ASP A 1 4   ? -26.806 25.480 29.193  1.00 39.18  ? 4   ASP A OD2 1 
ATOM   33   N  N   . TRP A 1 5   ? -22.576 28.240 27.675  1.00 27.65  ? 5   TRP A N   1 
ATOM   34   C  CA  . TRP A 1 5   ? -21.749 28.972 26.732  1.00 29.50  ? 5   TRP A CA  1 
ATOM   35   C  C   . TRP A 1 5   ? -21.299 30.268 27.375  1.00 23.48  ? 5   TRP A C   1 
ATOM   36   O  O   . TRP A 1 5   ? -22.102 30.985 27.985  1.00 24.36  ? 5   TRP A O   1 
ATOM   37   C  CB  . TRP A 1 5   ? -22.504 29.265 25.430  1.00 29.20  ? 5   TRP A CB  1 
ATOM   38   C  CG  . TRP A 1 5   ? -22.630 28.081 24.521  1.00 30.96  ? 5   TRP A CG  1 
ATOM   39   C  CD1 . TRP A 1 5   ? -23.659 27.192 24.479  1.00 27.28  ? 5   TRP A CD1 1 
ATOM   40   C  CD2 . TRP A 1 5   ? -21.692 27.662 23.515  1.00 25.51  ? 5   TRP A CD2 1 
ATOM   41   N  NE1 . TRP A 1 5   ? -23.421 26.241 23.516  1.00 32.57  ? 5   TRP A NE1 1 
ATOM   42   C  CE2 . TRP A 1 5   ? -22.221 26.503 22.911  1.00 26.90  ? 5   TRP A CE2 1 
ATOM   43   C  CE3 . TRP A 1 5   ? -20.454 28.153 23.076  1.00 29.09  ? 5   TRP A CE3 1 
ATOM   44   C  CZ2 . TRP A 1 5   ? -21.563 25.826 21.877  1.00 27.93  ? 5   TRP A CZ2 1 
ATOM   45   C  CZ3 . TRP A 1 5   ? -19.794 27.482 22.057  1.00 27.95  ? 5   TRP A CZ3 1 
ATOM   46   C  CH2 . TRP A 1 5   ? -20.356 26.328 21.462  1.00 28.49  ? 5   TRP A CH2 1 
ATOM   47   N  N   . LEU A 1 6   ? -20.017 30.564 27.235  1.00 23.48  ? 6   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 6   ? -19.464 31.842 27.648  1.00 22.16  ? 6   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 6   ? -18.837 32.508 26.432  1.00 30.43  ? 6   LEU A C   1 
ATOM   50   O  O   . LEU A 1 6   ? -17.936 31.943 25.802  1.00 26.90  ? 6   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 6   ? -18.437 31.654 28.762  1.00 24.76  ? 6   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 6   ? -17.690 32.929 29.144  1.00 34.78  ? 6   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 6   ? -18.685 33.928 29.699  1.00 20.49  ? 6   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 6   ? -16.551 32.636 30.136  1.00 23.92  ? 6   LEU A CD2 1 
ATOM   55   N  N   . PHE A 1 7   ? -19.320 33.695 26.098  1.00 29.81  ? 7   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 7   ? -18.727 34.510 25.045  1.00 26.90  ? 7   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 7   ? -17.806 35.524 25.716  1.00 29.52  ? 7   PHE A C   1 
ATOM   58   O  O   . PHE A 1 7   ? -18.279 36.438 26.396  1.00 30.36  ? 7   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 7   ? -19.802 35.209 24.215  1.00 27.17  ? 7   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 7   ? -20.669 34.272 23.406  1.00 23.55  ? 7   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 7   ? -20.321 33.928 22.106  1.00 26.91  ? 7   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 7   ? -21.832 33.757 23.935  1.00 23.76  ? 7   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 7   ? -21.119 33.079 21.356  1.00 25.07  ? 7   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 7   ? -22.634 32.910 23.193  1.00 24.74  ? 7   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 7   ? -22.290 32.573 21.907  1.00 24.69  ? 7   PHE A CZ  1 
ATOM   66   N  N   . LYS A 1 8   ? -16.494 35.367 25.535  1.00 27.99  ? 8   LYS A N   1 
ATOM   67   C  CA  . LYS A 1 8   ? -15.533 36.229 26.211  1.00 26.28  ? 8   LYS A CA  1 
ATOM   68   C  C   . LYS A 1 8   ? -15.188 37.430 25.350  1.00 29.49  ? 8   LYS A C   1 
ATOM   69   O  O   . LYS A 1 8   ? -14.954 37.296 24.145  1.00 26.78  ? 8   LYS A O   1 
ATOM   70   C  CB  . LYS A 1 8   ? -14.245 35.476 26.548  1.00 24.77  ? 8   LYS A CB  1 
ATOM   71   C  CG  . LYS A 1 8   ? -14.386 34.436 27.634  1.00 27.21  ? 8   LYS A CG  1 
ATOM   72   C  CD  . LYS A 1 8   ? -13.021 33.925 28.080  1.00 26.41  ? 8   LYS A CD  1 
ATOM   73   C  CE  . LYS A 1 8   ? -12.238 33.374 26.896  1.00 28.06  ? 8   LYS A CE  1 
ATOM   74   N  NZ  . LYS A 1 8   ? -10.914 32.873 27.291  1.00 32.38  ? 8   LYS A NZ  1 
ATOM   75   N  N   . ASN A 1 9   ? -15.159 38.608 25.978  1.00 25.65  ? 9   ASN A N   1 
ATOM   76   C  CA  . ASN A 1 9   ? -14.500 39.775 25.402  1.00 27.84  ? 9   ASN A CA  1 
ATOM   77   C  C   . ASN A 1 9   ? -15.124 40.174 24.064  1.00 26.83  ? 9   ASN A C   1 
ATOM   78   O  O   . ASN A 1 9   ? -14.422 40.531 23.120  1.00 27.31  ? 9   ASN A O   1 
ATOM   79   C  CB  . ASN A 1 9   ? -12.997 39.509 25.245  1.00 24.67  ? 9   ASN A CB  1 
ATOM   80   C  CG  . ASN A 1 9   ? -12.173 40.780 25.173  1.00 25.57  ? 9   ASN A CG  1 
ATOM   81   O  OD1 . ASN A 1 9   ? -12.693 41.881 25.339  1.00 29.87  ? 9   ASN A OD1 1 
ATOM   82   N  ND2 . ASN A 1 9   ? -10.864 40.631 24.942  1.00 28.54  ? 9   ASN A ND2 1 
ATOM   83   N  N   . VAL A 1 10  ? -16.457 40.110 23.978  1.00 24.46  ? 10  VAL A N   1 
ATOM   84   C  CA  . VAL A 1 10  ? -17.166 40.475 22.757  1.00 25.20  ? 10  VAL A CA  1 
ATOM   85   C  C   . VAL A 1 10  ? -17.558 41.939 22.827  1.00 27.50  ? 10  VAL A C   1 
ATOM   86   O  O   . VAL A 1 10  ? -17.773 42.491 23.910  1.00 27.57  ? 10  VAL A O   1 
ATOM   87   C  CB  . VAL A 1 10  ? -18.400 39.579 22.529  1.00 28.12  ? 10  VAL A CB  1 
ATOM   88   C  CG1 . VAL A 1 10  ? -17.961 38.173 22.085  1.00 24.28  ? 10  VAL A CG1 1 
ATOM   89   C  CG2 . VAL A 1 10  ? -19.280 39.526 23.796  1.00 22.37  ? 10  VAL A CG2 1 
ATOM   90   N  N   . THR A 1 11  ? -17.623 42.586 21.661  1.00 24.84  ? 11  THR A N   1 
ATOM   91   C  CA  . THR A 1 11  ? -18.300 43.873 21.553  1.00 25.63  ? 11  THR A CA  1 
ATOM   92   C  C   . THR A 1 11  ? -19.797 43.598 21.470  1.00 23.89  ? 11  THR A C   1 
ATOM   93   O  O   . THR A 1 11  ? -20.289 43.090 20.459  1.00 27.88  ? 11  THR A O   1 
ATOM   94   C  CB  . THR A 1 11  ? -17.817 44.662 20.339  1.00 26.15  ? 11  THR A CB  1 
ATOM   95   O  OG1 . THR A 1 11  ? -16.420 44.956 20.467  1.00 27.87  ? 11  THR A OG1 1 
ATOM   96   C  CG2 . THR A 1 11  ? -18.580 45.957 20.232  1.00 24.58  ? 11  THR A CG2 1 
ATOM   97   N  N   . VAL A 1 12  ? -20.515 43.885 22.548  1.00 29.28  ? 12  VAL A N   1 
ATOM   98   C  CA  . VAL A 1 12  ? -21.953 43.670 22.570  1.00 31.55  ? 12  VAL A CA  1 
ATOM   99   C  C   . VAL A 1 12  ? -22.618 44.812 21.816  1.00 27.70  ? 12  VAL A C   1 
ATOM   100  O  O   . VAL A 1 12  ? -22.494 45.977 22.202  1.00 29.72  ? 12  VAL A O   1 
ATOM   101  C  CB  . VAL A 1 12  ? -22.487 43.577 24.004  1.00 27.53  ? 12  VAL A CB  1 
ATOM   102  C  CG1 . VAL A 1 12  ? -24.010 43.458 23.962  1.00 27.10  ? 12  VAL A CG1 1 
ATOM   103  C  CG2 . VAL A 1 12  ? -21.864 42.402 24.743  1.00 20.82  ? 12  VAL A CG2 1 
ATOM   104  N  N   . ILE A 1 13  ? -23.297 44.484 20.725  1.00 23.27  ? 13  ILE A N   1 
ATOM   105  C  CA  . ILE A 1 13  ? -24.222 45.398 20.076  1.00 22.27  ? 13  ILE A CA  1 
ATOM   106  C  C   . ILE A 1 13  ? -25.602 44.815 20.347  1.00 25.50  ? 13  ILE A C   1 
ATOM   107  O  O   . ILE A 1 13  ? -26.009 43.838 19.711  1.00 26.38  ? 13  ILE A O   1 
ATOM   108  C  CB  . ILE A 1 13  ? -23.921 45.546 18.584  1.00 26.87  ? 13  ILE A CB  1 
ATOM   109  C  CG1 . ILE A 1 13  ? -22.526 46.169 18.406  1.00 26.95  ? 13  ILE A CG1 1 
ATOM   110  C  CG2 . ILE A 1 13  ? -25.003 46.353 17.892  1.00 21.77  ? 13  ILE A CG2 1 
ATOM   111  C  CD1 . ILE A 1 13  ? -22.243 46.623 16.997  1.00 26.43  ? 13  ILE A CD1 1 
ATOM   112  N  N   . ASP A 1 14  ? -26.305 45.379 21.333  1.00 24.96  ? 14  ASP A N   1 
ATOM   113  C  CA  . ASP A 1 14  ? -27.374 44.649 22.006  1.00 21.85  ? 14  ASP A CA  1 
ATOM   114  C  C   . ASP A 1 14  ? -28.717 44.714 21.296  1.00 24.98  ? 14  ASP A C   1 
ATOM   115  O  O   . ASP A 1 14  ? -29.670 44.100 21.786  1.00 28.57  ? 14  ASP A O   1 
ATOM   116  C  CB  . ASP A 1 14  ? -27.536 45.154 23.446  1.00 22.66  ? 14  ASP A CB  1 
ATOM   117  C  CG  . ASP A 1 14  ? -27.982 46.609 23.523  1.00 27.13  ? 14  ASP A CG  1 
ATOM   118  O  OD1 . ASP A 1 14  ? -28.358 47.192 22.484  1.00 29.31  ? 14  ASP A OD1 1 
ATOM   119  O  OD2 . ASP A 1 14  ? -27.950 47.181 24.635  1.00 31.22  ? 14  ASP A OD2 1 
ATOM   120  N  N   . GLY A 1 15  ? -28.834 45.457 20.195  1.00 23.51  ? 15  GLY A N   1 
ATOM   121  C  CA  . GLY A 1 15  ? -30.037 45.456 19.388  1.00 21.54  ? 15  GLY A CA  1 
ATOM   122  C  C   . GLY A 1 15  ? -30.950 46.636 19.616  1.00 24.51  ? 15  GLY A C   1 
ATOM   123  O  O   . GLY A 1 15  ? -31.896 46.839 18.835  1.00 23.79  ? 15  GLY A O   1 
ATOM   124  N  N   . SER A 1 16  ? -30.693 47.412 20.662  1.00 20.99  ? 16  SER A N   1 
ATOM   125  C  CA  . SER A 1 16  ? -31.521 48.548 21.025  1.00 27.46  ? 16  SER A CA  1 
ATOM   126  C  C   . SER A 1 16  ? -31.182 49.793 20.241  1.00 29.33  ? 16  SER A C   1 
ATOM   127  O  O   . SER A 1 16  ? -31.919 50.780 20.338  1.00 26.80  ? 16  SER A O   1 
ATOM   128  C  CB  . SER A 1 16  ? -31.349 48.882 22.501  1.00 20.68  ? 16  SER A CB  1 
ATOM   129  O  OG  . SER A 1 16  ? -30.003 49.252 22.756  1.00 28.08  ? 16  SER A OG  1 
ATOM   130  N  N   . GLY A 1 17  ? -30.082 49.776 19.493  1.00 27.05  ? 17  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 17  ? -29.600 50.972 18.853  1.00 24.58  ? 17  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 17  ? -28.786 51.852 19.763  1.00 29.28  ? 17  GLY A C   1 
ATOM   133  O  O   . GLY A 1 17  ? -28.274 52.882 19.307  1.00 30.14  ? 17  GLY A O   1 
ATOM   134  N  N   . GLY A 1 18  ? -28.634 51.468 21.036  1.00 22.93  ? 18  GLY A N   1 
ATOM   135  C  CA  . GLY A 1 18  ? -27.787 52.193 21.946  1.00 22.68  ? 18  GLY A CA  1 
ATOM   136  C  C   . GLY A 1 18  ? -26.323 51.880 21.724  1.00 31.58  ? 18  GLY A C   1 
ATOM   137  O  O   . GLY A 1 18  ? -25.938 51.070 20.871  1.00 30.32  ? 18  GLY A O   1 
ATOM   138  N  N   . PRO A 1 19  ? -25.478 52.529 22.517  1.00 24.97  ? 19  PRO A N   1 
ATOM   139  C  CA  . PRO A 1 19  ? -24.028 52.350 22.370  1.00 30.90  ? 19  PRO A CA  1 
ATOM   140  C  C   . PRO A 1 19  ? -23.589 50.904 22.569  1.00 34.06  ? 19  PRO A C   1 
ATOM   141  O  O   . PRO A 1 19  ? -24.226 50.120 23.280  1.00 35.79  ? 19  PRO A O   1 
ATOM   142  C  CB  . PRO A 1 19  ? -23.446 53.249 23.466  1.00 25.28  ? 19  PRO A CB  1 
ATOM   143  C  CG  . PRO A 1 19  ? -24.549 54.192 23.833  1.00 40.72  ? 19  PRO A CG  1 
ATOM   144  C  CD  . PRO A 1 19  ? -25.820 53.423 23.632  1.00 31.63  ? 19  PRO A CD  1 
ATOM   145  N  N   . GLN A 1 20  ? -22.469 50.567 21.938  1.00 28.43  ? 20  GLN A N   1 
ATOM   146  C  CA  . GLN A 1 20  ? -21.847 49.267 22.108  1.00 30.34  ? 20  GLN A CA  1 
ATOM   147  C  C   . GLN A 1 20  ? -20.936 49.283 23.330  1.00 25.91  ? 20  GLN A C   1 
ATOM   148  O  O   . GLN A 1 20  ? -20.580 50.336 23.860  1.00 28.64  ? 20  GLN A O   1 
ATOM   149  C  CB  . GLN A 1 20  ? -21.041 48.890 20.865  1.00 28.97  ? 20  GLN A CB  1 
ATOM   150  C  CG  . GLN A 1 20  ? -19.963 49.895 20.557  1.00 25.14  ? 20  GLN A CG  1 
ATOM   151  C  CD  . GLN A 1 20  ? -19.221 49.615 19.245  1.00 34.14  ? 20  GLN A CD  1 
ATOM   152  O  OE1 . GLN A 1 20  ? -19.827 49.307 18.224  1.00 40.75  ? 20  GLN A OE1 1 
ATOM   153  N  NE2 . GLN A 1 20  ? -17.909 49.751 19.274  1.00 33.09  ? 20  GLN A NE2 1 
ATOM   154  N  N   . TYR A 1 21  ? -20.567 48.091 23.780  1.00 25.47  ? 21  TYR A N   1 
ATOM   155  C  CA  . TYR A 1 21  ? -19.680 47.952 24.925  1.00 28.75  ? 21  TYR A CA  1 
ATOM   156  C  C   . TYR A 1 21  ? -19.058 46.570 24.873  1.00 24.40  ? 21  TYR A C   1 
ATOM   157  O  O   . TYR A 1 21  ? -19.532 45.687 24.154  1.00 31.31  ? 21  TYR A O   1 
ATOM   158  C  CB  . TYR A 1 21  ? -20.416 48.167 26.252  1.00 21.07  ? 21  TYR A CB  1 
ATOM   159  C  CG  . TYR A 1 21  ? -21.586 47.230 26.475  1.00 31.11  ? 21  TYR A CG  1 
ATOM   160  C  CD1 . TYR A 1 21  ? -22.851 47.542 25.995  1.00 23.91  ? 21  TYR A CD1 1 
ATOM   161  C  CD2 . TYR A 1 21  ? -21.431 46.043 27.187  1.00 25.71  ? 21  TYR A CD2 1 
ATOM   162  C  CE1 . TYR A 1 21  ? -23.931 46.695 26.209  1.00 26.63  ? 21  TYR A CE1 1 
ATOM   163  C  CE2 . TYR A 1 21  ? -22.502 45.192 27.404  1.00 25.17  ? 21  TYR A CE2 1 
ATOM   164  C  CZ  . TYR A 1 21  ? -23.752 45.526 26.918  1.00 36.10  ? 21  TYR A CZ  1 
ATOM   165  O  OH  . TYR A 1 21  ? -24.829 44.696 27.139  1.00 30.27  ? 21  TYR A OH  1 
ATOM   166  N  N   . ARG A 1 22  ? -17.972 46.400 25.620  1.00 24.19  ? 22  ARG A N   1 
ATOM   167  C  CA  . ARG A 1 22  ? -17.276 45.122 25.695  1.00 24.96  ? 22  ARG A CA  1 
ATOM   168  C  C   . ARG A 1 22  ? -17.646 44.413 26.987  1.00 24.71  ? 22  ARG A C   1 
ATOM   169  O  O   . ARG A 1 22  ? -17.717 45.037 28.051  1.00 26.62  ? 22  ARG A O   1 
ATOM   170  C  CB  . ARG A 1 22  ? -15.766 45.324 25.588  1.00 24.11  ? 22  ARG A CB  1 
ATOM   171  C  CG  . ARG A 1 22  ? -15.383 45.929 24.239  1.00 28.92  ? 22  ARG A CG  1 
ATOM   172  C  CD  . ARG A 1 22  ? -13.905 45.819 23.935  1.00 32.46  ? 22  ARG A CD  1 
ATOM   173  N  NE  . ARG A 1 22  ? -13.542 46.769 22.890  1.00 33.53  ? 22  ARG A NE  1 
ATOM   174  C  CZ  . ARG A 1 22  ? -12.307 47.179 22.641  1.00 38.92  ? 22  ARG A CZ  1 
ATOM   175  N  NH1 . ARG A 1 22  ? -11.271 46.707 23.318  1.00 39.24  ? 22  ARG A NH1 1 
ATOM   176  N  NH2 . ARG A 1 22  ? -12.107 48.098 21.702  1.00 31.30  ? 22  ARG A NH2 1 
ATOM   177  N  N   . ALA A 1 23  ? -17.895 43.114 26.888  1.00 24.39  ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? -18.348 42.343 28.036  1.00 25.15  ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? -18.133 40.858 27.755  1.00 29.82  ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? -17.763 40.459 26.643  1.00 29.38  ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? -19.816 42.645 28.341  1.00 18.97  ? 23  ALA A CB  1 
ATOM   182  N  N   . ASP A 1 24  ? -18.301 40.052 28.801  1.00 24.10  ? 24  ASP A N   1 
ATOM   183  C  CA  . ASP A 1 24  ? -18.557 38.623 28.682  1.00 21.94  ? 24  ASP A CA  1 
ATOM   184  C  C   . ASP A 1 24  ? -20.065 38.400 28.752  1.00 29.83  ? 24  ASP A C   1 
ATOM   185  O  O   . ASP A 1 24  ? -20.773 39.054 29.529  1.00 24.11  ? 24  ASP A O   1 
ATOM   186  C  CB  . ASP A 1 24  ? -17.902 37.810 29.812  1.00 25.94  ? 24  ASP A CB  1 
ATOM   187  C  CG  . ASP A 1 24  ? -16.377 37.822 29.788  1.00 25.97  ? 24  ASP A CG  1 
ATOM   188  O  OD1 . ASP A 1 24  ? -15.768 38.287 28.812  1.00 24.37  ? 24  ASP A OD1 1 
ATOM   189  O  OD2 . ASP A 1 24  ? -15.776 37.347 30.784  1.00 24.26  ? 24  ASP A OD2 1 
ATOM   190  N  N   . VAL A 1 25  ? -20.544 37.443 27.965  1.00 28.85  ? 25  VAL A N   1 
ATOM   191  C  CA  . VAL A 1 25  ? -21.951 37.064 27.935  1.00 25.73  ? 25  VAL A CA  1 
ATOM   192  C  C   . VAL A 1 25  ? -22.028 35.560 28.164  1.00 30.40  ? 25  VAL A C   1 
ATOM   193  O  O   . VAL A 1 25  ? -21.317 34.794 27.503  1.00 29.25  ? 25  VAL A O   1 
ATOM   194  C  CB  . VAL A 1 25  ? -22.618 37.446 26.593  1.00 23.59  ? 25  VAL A CB  1 
ATOM   195  C  CG1 . VAL A 1 25  ? -24.096 37.008 26.563  1.00 19.02  ? 25  VAL A CG1 1 
ATOM   196  C  CG2 . VAL A 1 25  ? -22.502 38.953 26.317  1.00 21.55  ? 25  VAL A CG2 1 
ATOM   197  N  N   . ALA A 1 26  ? -22.873 35.139 29.102  1.00 24.81  ? 26  ALA A N   1 
ATOM   198  C  CA  . ALA A 1 26  ? -23.027 33.728 29.426  1.00 23.71  ? 26  ALA A CA  1 
ATOM   199  C  C   . ALA A 1 26  ? -24.441 33.267 29.098  1.00 25.54  ? 26  ALA A C   1 
ATOM   200  O  O   . ALA A 1 26  ? -25.412 34.021 29.235  1.00 20.84  ? 26  ALA A O   1 
ATOM   201  C  CB  . ALA A 1 26  ? -22.723 33.441 30.906  1.00 19.83  ? 26  ALA A CB  1 
ATOM   202  N  N   . VAL A 1 27  ? -24.541 32.016 28.662  1.00 27.14  ? 27  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 27  ? -25.798 31.407 28.263  1.00 20.49  ? 27  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 27  ? -25.985 30.131 29.046  1.00 25.95  ? 27  VAL A C   1 
ATOM   205  O  O   . VAL A 1 27  ? -25.038 29.358 29.227  1.00 33.60  ? 27  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 27  ? -25.840 31.119 26.748  1.00 24.35  ? 27  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 27  ? -26.977 30.171 26.413  1.00 19.21  ? 27  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 27  ? -25.946 32.443 25.955  1.00 19.75  ? 27  VAL A CG2 1 
ATOM   209  N  N   . LYS A 1 28  ? -27.213 29.907 29.510  1.00 27.77  ? 28  LYS A N   1 
ATOM   210  C  CA  . LYS A 1 28  ? -27.576 28.679 30.190  1.00 23.81  ? 28  LYS A CA  1 
ATOM   211  C  C   . LYS A 1 28  ? -28.941 28.245 29.687  1.00 29.15  ? 28  LYS A C   1 
ATOM   212  O  O   . LYS A 1 28  ? -29.887 29.039 29.715  1.00 27.73  ? 28  LYS A O   1 
ATOM   213  C  CB  . LYS A 1 28  ? -27.602 28.869 31.714  1.00 25.28  ? 28  LYS A CB  1 
ATOM   214  C  CG  . LYS A 1 28  ? -27.580 27.576 32.480  1.00 27.90  ? 28  LYS A CG  1 
ATOM   215  C  CD  . LYS A 1 28  ? -27.486 27.791 34.010  1.00 37.88  ? 28  LYS A CD  1 
ATOM   216  C  CE  . LYS A 1 28  ? -28.854 27.687 34.694  1.00 37.20  ? 28  LYS A CE  1 
ATOM   217  N  NZ  . LYS A 1 28  ? -28.774 27.556 36.209  1.00 45.29  ? 28  LYS A NZ  1 
ATOM   218  N  N   . GLY A 1 29  ? -29.046 26.989 29.250  1.00 27.21  ? 29  GLY A N   1 
ATOM   219  C  CA  . GLY A 1 29  ? -30.258 26.563 28.571  1.00 28.01  ? 29  GLY A CA  1 
ATOM   220  C  C   . GLY A 1 29  ? -30.492 27.456 27.363  1.00 26.61  ? 29  GLY A C   1 
ATOM   221  O  O   . GLY A 1 29  ? -29.554 27.801 26.635  1.00 27.11  ? 29  GLY A O   1 
ATOM   222  N  N   . ASP A 1 30  ? -31.741 27.888 27.176  1.00 22.99  ? 30  ASP A N   1 
ATOM   223  C  CA  . ASP A 1 30  ? -32.110 28.764 26.068  1.00 22.10  ? 30  ASP A CA  1 
ATOM   224  C  C   . ASP A 1 30  ? -32.085 30.246 26.423  1.00 25.15  ? 30  ASP A C   1 
ATOM   225  O  O   . ASP A 1 30  ? -32.604 31.055 25.652  1.00 27.75  ? 30  ASP A O   1 
ATOM   226  C  CB  . ASP A 1 30  ? -33.498 28.392 25.537  1.00 23.41  ? 30  ASP A CB  1 
ATOM   227  C  CG  . ASP A 1 30  ? -34.583 28.391 26.613  1.00 28.10  ? 30  ASP A CG  1 
ATOM   228  O  OD1 . ASP A 1 30  ? -34.311 28.752 27.776  1.00 37.51  ? 30  ASP A OD1 1 
ATOM   229  O  OD2 . ASP A 1 30  ? -35.728 28.001 26.289  1.00 29.09  ? 30  ASP A OD2 1 
ATOM   230  N  N   . ARG A 1 31  ? -31.485 30.627 27.550  1.00 26.33  ? 31  ARG A N   1 
ATOM   231  C  CA  . ARG A 1 31  ? -31.561 32.001 28.014  1.00 26.70  ? 31  ARG A CA  1 
ATOM   232  C  C   . ARG A 1 31  ? -30.176 32.608 28.156  1.00 23.04  ? 31  ARG A C   1 
ATOM   233  O  O   . ARG A 1 31  ? -29.210 31.934 28.527  1.00 28.16  ? 31  ARG A O   1 
ATOM   234  C  CB  . ARG A 1 31  ? -32.298 32.110 29.366  1.00 25.69  ? 31  ARG A CB  1 
ATOM   235  C  CG  . ARG A 1 31  ? -33.746 31.692 29.327  1.00 25.59  ? 31  ARG A CG  1 
ATOM   236  C  CD  . ARG A 1 31  ? -34.627 32.705 28.607  1.00 23.86  ? 31  ARG A CD  1 
ATOM   237  N  NE  . ARG A 1 31  ? -36.025 32.277 28.672  1.00 28.78  ? 31  ARG A NE  1 
ATOM   238  C  CZ  . ARG A 1 31  ? -37.072 33.065 28.460  1.00 28.52  ? 31  ARG A CZ  1 
ATOM   239  N  NH1 . ARG A 1 31  ? -36.924 34.349 28.162  1.00 27.04  ? 31  ARG A NH1 1 
ATOM   240  N  NH2 . ARG A 1 31  ? -38.299 32.553 28.556  1.00 23.11  ? 31  ARG A NH2 1 
ATOM   241  N  N   . ILE A 1 32  ? -30.104 33.899 27.848  1.00 26.96  ? 32  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 32  ? -28.964 34.729 28.216  1.00 25.91  ? 32  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 32  ? -29.049 34.967 29.714  1.00 25.50  ? 32  ILE A C   1 
ATOM   244  O  O   . ILE A 1 32  ? -29.989 35.609 30.195  1.00 29.67  ? 32  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 32  ? -28.971 36.048 27.435  1.00 27.00  ? 32  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 32  ? -29.054 35.752 25.945  1.00 21.54  ? 32  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 32  ? -27.743 36.877 27.769  1.00 28.67  ? 32  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 32  ? -29.259 36.970 25.088  1.00 24.13  ? 32  ILE A CD1 1 
ATOM   249  N  N   A MET A 1 33  ? -28.079 34.443 30.467  0.70 26.44  ? 33  MET A N   1 
ATOM   250  N  N   B MET A 1 33  ? -28.069 34.445 30.452  0.30 26.13  ? 33  MET A N   1 
ATOM   251  C  CA  A MET A 1 33  ? -28.188 34.456 31.919  0.70 27.58  ? 33  MET A CA  1 
ATOM   252  C  CA  B MET A 1 33  ? -28.123 34.390 31.906  0.30 28.01  ? 33  MET A CA  1 
ATOM   253  C  C   A MET A 1 33  ? -27.318 35.503 32.599  0.70 28.23  ? 33  MET A C   1 
ATOM   254  C  C   B MET A 1 33  ? -27.309 35.477 32.592  0.30 28.35  ? 33  MET A C   1 
ATOM   255  O  O   A MET A 1 33  ? -27.604 35.859 33.743  0.70 28.16  ? 33  MET A O   1 
ATOM   256  O  O   B MET A 1 33  ? -27.628 35.842 33.726  0.30 28.07  ? 33  MET A O   1 
ATOM   257  C  CB  A MET A 1 33  ? -27.841 33.076 32.497  0.70 28.24  ? 33  MET A CB  1 
ATOM   258  C  CB  B MET A 1 33  ? -27.632 33.022 32.396  0.30 28.25  ? 33  MET A CB  1 
ATOM   259  C  CG  A MET A 1 33  ? -26.377 32.685 32.356  0.70 22.71  ? 33  MET A CG  1 
ATOM   260  C  CG  B MET A 1 33  ? -27.802 32.794 33.882  0.30 27.55  ? 33  MET A CG  1 
ATOM   261  S  SD  A MET A 1 33  ? -25.852 31.852 33.872  0.70 47.54  ? 33  MET A SD  1 
ATOM   262  S  SD  B MET A 1 33  ? -26.905 31.339 34.472  0.30 34.37  ? 33  MET A SD  1 
ATOM   263  C  CE  A MET A 1 33  ? -25.870 33.212 35.033  0.70 38.41  ? 33  MET A CE  1 
ATOM   264  C  CE  B MET A 1 33  ? -25.235 31.973 34.524  0.30 38.09  ? 33  MET A CE  1 
ATOM   265  N  N   . ALA A 1 34  ? -26.261 35.991 31.953  1.00 28.34  ? 34  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 34  ? -25.408 36.986 32.590  1.00 27.58  ? 34  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 34  ? -24.668 37.804 31.545  1.00 28.77  ? 34  ALA A C   1 
ATOM   268  O  O   . ALA A 1 34  ? -24.272 37.285 30.500  1.00 27.77  ? 34  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 34  ? -24.403 36.330 33.539  1.00 22.26  ? 34  ALA A CB  1 
ATOM   270  N  N   . ILE A 1 35  ? -24.494 39.092 31.853  1.00 28.15  ? 35  ILE A N   1 
ATOM   271  C  CA  . ILE A 1 35  ? -23.686 40.030 31.074  1.00 27.23  ? 35  ILE A CA  1 
ATOM   272  C  C   . ILE A 1 35  ? -22.936 40.905 32.073  1.00 29.18  ? 35  ILE A C   1 
ATOM   273  O  O   . ILE A 1 35  ? -23.560 41.545 32.927  1.00 31.25  ? 35  ILE A O   1 
ATOM   274  C  CB  . ILE A 1 35  ? -24.535 40.912 30.135  1.00 30.76  ? 35  ILE A CB  1 
ATOM   275  C  CG1 . ILE A 1 35  ? -25.399 40.061 29.197  1.00 25.81  ? 35  ILE A CG1 1 
ATOM   276  C  CG2 . ILE A 1 35  ? -23.639 41.866 29.326  1.00 26.06  ? 35  ILE A CG2 1 
ATOM   277  C  CD1 . ILE A 1 35  ? -26.422 40.858 28.431  1.00 20.60  ? 35  ILE A CD1 1 
ATOM   278  N  N   . ALA A 1 36  ? -21.611 40.934 31.987  1.00 24.49  ? 36  ALA A N   1 
ATOM   279  C  CA  . ALA A 1 36  ? -20.822 41.705 32.943  1.00 31.28  ? 36  ALA A CA  1 
ATOM   280  C  C   . ALA A 1 36  ? -19.484 42.039 32.305  1.00 24.62  ? 36  ALA A C   1 
ATOM   281  O  O   . ALA A 1 36  ? -19.062 41.366 31.360  1.00 23.71  ? 36  ALA A O   1 
ATOM   282  C  CB  . ALA A 1 36  ? -20.615 40.935 34.266  1.00 23.29  ? 36  ALA A CB  1 
ATOM   283  N  N   . PRO A 1 37  ? -18.804 43.085 32.787  1.00 30.65  ? 37  PRO A N   1 
ATOM   284  C  CA  . PRO A 1 37  ? -17.448 43.378 32.283  1.00 28.06  ? 37  PRO A CA  1 
ATOM   285  C  C   . PRO A 1 37  ? -16.548 42.151 32.197  1.00 32.94  ? 37  PRO A C   1 
ATOM   286  O  O   . PRO A 1 37  ? -15.741 42.054 31.260  1.00 31.38  ? 37  PRO A O   1 
ATOM   287  C  CB  . PRO A 1 37  ? -16.928 44.414 33.289  1.00 28.30  ? 37  PRO A CB  1 
ATOM   288  C  CG  . PRO A 1 37  ? -18.199 45.133 33.749  1.00 27.73  ? 37  PRO A CG  1 
ATOM   289  C  CD  . PRO A 1 37  ? -19.269 44.072 33.780  1.00 29.81  ? 37  PRO A CD  1 
ATOM   290  N  N   . ALA A 1 38  ? -16.652 41.220 33.151  1.00 26.97  ? 38  ALA A N   1 
ATOM   291  C  CA  . ALA A 1 38  ? -16.107 39.876 32.989  1.00 26.61  ? 38  ALA A CA  1 
ATOM   292  C  C   . ALA A 1 38  ? -16.930 38.906 33.818  1.00 29.61  ? 38  ALA A C   1 
ATOM   293  O  O   . ALA A 1 38  ? -17.538 39.292 34.818  1.00 31.95  ? 38  ALA A O   1 
ATOM   294  C  CB  . ALA A 1 38  ? -14.642 39.776 33.406  1.00 26.74  ? 38  ALA A CB  1 
ATOM   295  N  N   . LEU A 1 39  ? -16.941 37.643 33.396  1.00 25.70  ? 39  LEU A N   1 
ATOM   296  C  CA  . LEU A 1 39  ? -17.674 36.572 34.073  1.00 27.52  ? 39  LEU A CA  1 
ATOM   297  C  C   . LEU A 1 39  ? -16.698 35.439 34.378  1.00 28.04  ? 39  LEU A C   1 
ATOM   298  O  O   . LEU A 1 39  ? -16.305 34.678 33.493  1.00 30.54  ? 39  LEU A O   1 
ATOM   299  C  CB  . LEU A 1 39  ? -18.850 36.089 33.221  1.00 21.42  ? 39  LEU A CB  1 
ATOM   300  C  CG  . LEU A 1 39  ? -19.999 37.082 33.025  1.00 28.88  ? 39  LEU A CG  1 
ATOM   301  C  CD1 . LEU A 1 39  ? -20.937 36.596 31.944  1.00 26.94  ? 39  LEU A CD1 1 
ATOM   302  C  CD2 . LEU A 1 39  ? -20.782 37.310 34.328  1.00 23.73  ? 39  LEU A CD2 1 
ATOM   303  N  N   . ASP A 1 40  ? -16.299 35.314 35.635  1.00 28.74  ? 40  ASP A N   1 
ATOM   304  C  CA  . ASP A 1 40  ? -15.368 34.261 36.018  1.00 29.66  ? 40  ASP A CA  1 
ATOM   305  C  C   . ASP A 1 40  ? -16.180 33.026 36.399  1.00 33.09  ? 40  ASP A C   1 
ATOM   306  O  O   . ASP A 1 40  ? -16.373 32.713 37.570  1.00 37.54  ? 40  ASP A O   1 
ATOM   307  C  CB  . ASP A 1 40  ? -14.483 34.728 37.161  1.00 31.68  ? 40  ASP A CB  1 
ATOM   308  C  CG  . ASP A 1 40  ? -13.456 33.690 37.562  1.00 34.07  ? 40  ASP A CG  1 
ATOM   309  O  OD1 . ASP A 1 40  ? -13.275 32.681 36.839  1.00 41.47  ? 40  ASP A OD1 1 
ATOM   310  O  OD2 . ASP A 1 40  ? -12.817 33.901 38.605  1.00 34.24  ? 40  ASP A OD2 1 
ATOM   311  N  N   . VAL A 1 41  ? -16.647 32.306 35.377  1.00 36.01  ? 41  VAL A N   1 
ATOM   312  C  CA  . VAL A 1 41  ? -17.525 31.151 35.542  1.00 37.16  ? 41  VAL A CA  1 
ATOM   313  C  C   . VAL A 1 41  ? -17.008 29.989 34.702  1.00 42.67  ? 41  VAL A C   1 
ATOM   314  O  O   . VAL A 1 41  ? -16.438 30.179 33.621  1.00 48.48  ? 41  VAL A O   1 
ATOM   315  C  CB  . VAL A 1 41  ? -18.988 31.469 35.143  1.00 33.52  ? 41  VAL A CB  1 
ATOM   316  C  CG1 . VAL A 1 41  ? -19.509 32.664 35.914  1.00 35.73  ? 41  VAL A CG1 1 
ATOM   317  C  CG2 . VAL A 1 41  ? -19.066 31.758 33.655  1.00 30.34  ? 41  VAL A CG2 1 
ATOM   318  N  N   . ALA A 1 42  ? -17.227 28.771 35.197  1.00 42.05  ? 42  ALA A N   1 
ATOM   319  C  CA  . ALA A 1 42  ? -16.968 27.590 34.387  1.00 41.81  ? 42  ALA A CA  1 
ATOM   320  C  C   . ALA A 1 42  ? -18.071 27.420 33.349  1.00 39.81  ? 42  ALA A C   1 
ATOM   321  O  O   . ALA A 1 42  ? -19.262 27.540 33.658  1.00 43.67  ? 42  ALA A O   1 
ATOM   322  C  CB  . ALA A 1 42  ? -16.866 26.349 35.268  1.00 39.06  ? 42  ALA A CB  1 
ATOM   323  N  N   . ALA A 1 43  ? -17.675 27.156 32.112  1.00 32.53  ? 43  ALA A N   1 
ATOM   324  C  CA  . ALA A 1 43  ? -18.610 26.937 31.025  1.00 28.48  ? 43  ALA A CA  1 
ATOM   325  C  C   . ALA A 1 43  ? -18.309 25.609 30.345  1.00 31.46  ? 43  ALA A C   1 
ATOM   326  O  O   . ALA A 1 43  ? -17.155 25.184 30.257  1.00 40.85  ? 43  ALA A O   1 
ATOM   327  C  CB  . ALA A 1 43  ? -18.534 28.068 30.015  1.00 30.82  ? 43  ALA A CB  1 
ATOM   328  N  N   . GLU A 1 44  ? -19.358 24.936 29.882  1.00 31.82  ? 44  GLU A N   1 
ATOM   329  C  CA  . GLU A 1 44  ? -19.151 23.786 29.008  1.00 37.48  ? 44  GLU A CA  1 
ATOM   330  C  C   . GLU A 1 44  ? -18.382 24.184 27.747  1.00 37.93  ? 44  GLU A C   1 
ATOM   331  O  O   . GLU A 1 44  ? -17.540 23.424 27.259  1.00 41.47  ? 44  GLU A O   1 
ATOM   332  C  CB  . GLU A 1 44  ? -20.495 23.166 28.631  1.00 37.86  ? 44  GLU A CB  1 
ATOM   333  C  CG  . GLU A 1 44  ? -21.339 22.733 29.806  1.00 54.48  ? 44  GLU A CG  1 
ATOM   334  C  CD  . GLU A 1 44  ? -20.853 21.443 30.423  1.00 64.83  ? 44  GLU A CD  1 
ATOM   335  O  OE1 . GLU A 1 44  ? -19.962 20.808 29.818  1.00 69.10  ? 44  GLU A OE1 1 
ATOM   336  O  OE2 . GLU A 1 44  ? -21.360 21.066 31.507  1.00 71.01  ? 44  GLU A OE2 1 
ATOM   337  N  N   . GLN A 1 45  ? -18.666 25.366 27.199  1.00 32.16  ? 45  GLN A N   1 
ATOM   338  C  CA  . GLN A 1 45  ? -18.026 25.854 25.981  1.00 31.82  ? 45  GLN A CA  1 
ATOM   339  C  C   . GLN A 1 45  ? -17.678 27.326 26.140  1.00 31.17  ? 45  GLN A C   1 
ATOM   340  O  O   . GLN A 1 45  ? -18.502 28.123 26.609  1.00 27.77  ? 45  GLN A O   1 
ATOM   341  C  CB  . GLN A 1 45  ? -18.939 25.680 24.767  1.00 30.74  ? 45  GLN A CB  1 
ATOM   342  C  CG  . GLN A 1 45  ? -19.480 24.284 24.608  1.00 40.82  ? 45  GLN A CG  1 
ATOM   343  C  CD  . GLN A 1 45  ? -18.693 23.490 23.605  1.00 57.05  ? 45  GLN A CD  1 
ATOM   344  O  OE1 . GLN A 1 45  ? -17.460 23.527 23.587  1.00 58.46  ? 45  GLN A OE1 1 
ATOM   345  N  NE2 . GLN A 1 45  ? -19.402 22.769 22.745  1.00 73.81  ? 45  GLN A NE2 1 
ATOM   346  N  N   . VAL A 1 46  ? -16.452 27.678 25.755  1.00 33.62  ? 46  VAL A N   1 
ATOM   347  C  CA  . VAL A 1 46  ? -15.952 29.048 25.814  1.00 31.00  ? 46  VAL A CA  1 
ATOM   348  C  C   . VAL A 1 46  ? -15.575 29.486 24.404  1.00 36.79  ? 46  VAL A C   1 
ATOM   349  O  O   . VAL A 1 46  ? -14.945 28.727 23.657  1.00 34.24  ? 46  VAL A O   1 
ATOM   350  C  CB  . VAL A 1 46  ? -14.746 29.172 26.767  1.00 32.11  ? 46  VAL A CB  1 
ATOM   351  C  CG1 . VAL A 1 46  ? -14.258 30.605 26.806  1.00 28.04  ? 46  VAL A CG1 1 
ATOM   352  C  CG2 . VAL A 1 46  ? -15.130 28.708 28.176  1.00 35.76  ? 46  VAL A CG2 1 
ATOM   353  N  N   . ILE A 1 47  ? -15.962 30.705 24.042  1.00 34.12  ? 47  ILE A N   1 
ATOM   354  C  CA  . ILE A 1 47  ? -15.551 31.331 22.791  1.00 32.67  ? 47  ILE A CA  1 
ATOM   355  C  C   . ILE A 1 47  ? -14.825 32.616 23.135  1.00 34.66  ? 47  ILE A C   1 
ATOM   356  O  O   . ILE A 1 47  ? -15.397 33.499 23.790  1.00 31.88  ? 47  ILE A O   1 
ATOM   357  C  CB  . ILE A 1 47  ? -16.740 31.620 21.862  1.00 38.82  ? 47  ILE A CB  1 
ATOM   358  C  CG1 . ILE A 1 47  ? -17.336 30.319 21.331  1.00 31.45  ? 47  ILE A CG1 1 
ATOM   359  C  CG2 . ILE A 1 47  ? -16.299 32.503 20.707  1.00 31.19  ? 47  ILE A CG2 1 
ATOM   360  C  CD1 . ILE A 1 47  ? -18.641 30.526 20.628  1.00 39.41  ? 47  ILE A CD1 1 
ATOM   361  N  N   . ASP A 1 48  ? -13.563 32.709 22.724  1.00 31.77  ? 48  ASP A N   1 
ATOM   362  C  CA  . ASP A 1 48  ? -12.828 33.964 22.810  1.00 29.45  ? 48  ASP A CA  1 
ATOM   363  C  C   . ASP A 1 48  ? -13.354 34.867 21.703  1.00 34.42  ? 48  ASP A C   1 
ATOM   364  O  O   . ASP A 1 48  ? -13.026 34.684 20.530  1.00 31.42  ? 48  ASP A O   1 
ATOM   365  C  CB  . ASP A 1 48  ? -11.325 33.735 22.676  1.00 25.75  ? 48  ASP A CB  1 
ATOM   366  C  CG  . ASP A 1 48  ? -10.517 35.014 22.904  1.00 33.64  ? 48  ASP A CG  1 
ATOM   367  O  OD1 . ASP A 1 48  ? -11.138 36.084 23.074  1.00 35.51  ? 48  ASP A OD1 1 
ATOM   368  O  OD2 . ASP A 1 48  ? -9.266  34.953 22.932  1.00 42.82  ? 48  ASP A OD2 1 
ATOM   369  N  N   . GLY A 1 49  ? -14.180 35.844 22.069  1.00 32.57  ? 49  GLY A N   1 
ATOM   370  C  CA  . GLY A 1 49  ? -14.811 36.694 21.075  1.00 28.16  ? 49  GLY A CA  1 
ATOM   371  C  C   . GLY A 1 49  ? -14.047 37.961 20.742  1.00 29.70  ? 49  GLY A C   1 
ATOM   372  O  O   . GLY A 1 49  ? -14.597 38.880 20.135  1.00 29.16  ? 49  GLY A O   1 
ATOM   373  N  N   . GLN A 1 50  ? -12.775 38.031 21.110  1.00 30.71  ? 50  GLN A N   1 
ATOM   374  C  CA  . GLN A 1 50  ? -12.028 39.258 20.879  1.00 25.70  ? 50  GLN A CA  1 
ATOM   375  C  C   . GLN A 1 50  ? -12.155 39.694 19.424  1.00 32.53  ? 50  GLN A C   1 
ATOM   376  O  O   . GLN A 1 50  ? -12.056 38.882 18.495  1.00 29.37  ? 50  GLN A O   1 
ATOM   377  C  CB  . GLN A 1 50  ? -10.557 39.052 21.255  1.00 24.08  ? 50  GLN A CB  1 
ATOM   378  C  CG  . GLN A 1 50  ? -9.793  38.101 20.352  1.00 35.38  ? 50  GLN A CG  1 
ATOM   379  C  CD  . GLN A 1 50  ? -8.342  37.932 20.776  1.00 39.32  ? 50  GLN A CD  1 
ATOM   380  O  OE1 . GLN A 1 50  ? -7.433  38.503 20.173  1.00 36.90  ? 50  GLN A OE1 1 
ATOM   381  N  NE2 . GLN A 1 50  ? -8.120  37.138 21.816  1.00 35.76  ? 50  GLN A NE2 1 
ATOM   382  N  N   . GLY A 1 51  ? -12.362 40.989 19.224  1.00 33.79  ? 51  GLY A N   1 
ATOM   383  C  CA  . GLY A 1 51  ? -12.430 41.505 17.870  1.00 37.61  ? 51  GLY A CA  1 
ATOM   384  C  C   . GLY A 1 51  ? -13.705 41.205 17.108  1.00 35.65  ? 51  GLY A C   1 
ATOM   385  O  O   . GLY A 1 51  ? -13.791 41.561 15.930  1.00 36.55  ? 51  GLY A O   1 
ATOM   386  N  N   . ARG A 1 52  ? -14.698 40.580 17.733  1.00 26.40  ? 52  ARG A N   1 
ATOM   387  C  CA  . ARG A 1 52  ? -15.962 40.257 17.085  1.00 32.87  ? 52  ARG A CA  1 
ATOM   388  C  C   . ARG A 1 52  ? -17.105 40.994 17.766  1.00 24.95  ? 52  ARG A C   1 
ATOM   389  O  O   . ARG A 1 52  ? -16.983 41.481 18.896  1.00 30.69  ? 52  ARG A O   1 
ATOM   390  C  CB  . ARG A 1 52  ? -16.258 38.751 17.115  1.00 31.14  ? 52  ARG A CB  1 
ATOM   391  C  CG  . ARG A 1 52  ? -15.111 37.876 16.630  1.00 39.48  ? 52  ARG A CG  1 
ATOM   392  C  CD  . ARG A 1 52  ? -14.804 38.169 15.214  1.00 38.49  ? 52  ARG A CD  1 
ATOM   393  N  NE  . ARG A 1 52  ? -13.778 37.283 14.673  1.00 55.92  ? 52  ARG A NE  1 
ATOM   394  C  CZ  . ARG A 1 52  ? -12.481 37.558 14.641  1.00 58.85  ? 52  ARG A CZ  1 
ATOM   395  N  NH1 . ARG A 1 52  ? -11.995 38.668 15.178  1.00 51.00  ? 52  ARG A NH1 1 
ATOM   396  N  NH2 . ARG A 1 52  ? -11.652 36.704 14.042  1.00 54.08  ? 52  ARG A NH2 1 
ATOM   397  N  N   . VAL A 1 53  ? -18.230 41.058 17.067  1.00 30.51  ? 53  VAL A N   1 
ATOM   398  C  CA  . VAL A 1 53  ? -19.466 41.608 17.613  1.00 27.04  ? 53  VAL A CA  1 
ATOM   399  C  C   . VAL A 1 53  ? -20.396 40.468 17.998  1.00 28.64  ? 53  VAL A C   1 
ATOM   400  O  O   . VAL A 1 53  ? -20.634 39.552 17.200  1.00 33.43  ? 53  VAL A O   1 
ATOM   401  C  CB  . VAL A 1 53  ? -20.147 42.543 16.607  1.00 24.19  ? 53  VAL A CB  1 
ATOM   402  C  CG1 . VAL A 1 53  ? -21.603 42.733 16.989  1.00 23.46  ? 53  VAL A CG1 1 
ATOM   403  C  CG2 . VAL A 1 53  ? -19.386 43.863 16.557  1.00 25.18  ? 53  VAL A CG2 1 
ATOM   404  N  N   . LEU A 1 54  ? -20.919 40.514 19.219  1.00 25.18  ? 54  LEU A N   1 
ATOM   405  C  CA  . LEU A 1 54  ? -22.038 39.671 19.605  1.00 23.66  ? 54  LEU A CA  1 
ATOM   406  C  C   . LEU A 1 54  ? -23.313 40.500 19.497  1.00 26.91  ? 54  LEU A C   1 
ATOM   407  O  O   . LEU A 1 54  ? -23.436 41.555 20.132  1.00 27.29  ? 54  LEU A O   1 
ATOM   408  C  CB  . LEU A 1 54  ? -21.860 39.109 21.016  1.00 26.39  ? 54  LEU A CB  1 
ATOM   409  C  CG  . LEU A 1 54  ? -22.857 38.002 21.366  1.00 26.15  ? 54  LEU A CG  1 
ATOM   410  C  CD1 . LEU A 1 54  ? -22.591 36.792 20.472  1.00 23.33  ? 54  LEU A CD1 1 
ATOM   411  C  CD2 . LEU A 1 54  ? -22.811 37.631 22.870  1.00 24.91  ? 54  LEU A CD2 1 
ATOM   412  N  N   . ALA A 1 55  ? -24.235 40.039 18.673  1.00 22.14  ? 55  ALA A N   1 
ATOM   413  C  CA  . ALA A 1 55  ? -25.493 40.707 18.400  1.00 21.25  ? 55  ALA A CA  1 
ATOM   414  C  C   . ALA A 1 55  ? -26.634 39.727 18.602  1.00 24.00  ? 55  ALA A C   1 
ATOM   415  O  O   . ALA A 1 55  ? -26.429 38.507 18.564  1.00 27.88  ? 55  ALA A O   1 
ATOM   416  C  CB  . ALA A 1 55  ? -25.507 41.241 16.958  1.00 21.46  ? 55  ALA A CB  1 
ATOM   417  N  N   . PRO A 1 56  ? -27.861 40.220 18.786  1.00 25.69  ? 56  PRO A N   1 
ATOM   418  C  CA  . PRO A 1 56  ? -29.011 39.311 18.764  1.00 22.58  ? 56  PRO A CA  1 
ATOM   419  C  C   . PRO A 1 56  ? -29.094 38.627 17.408  1.00 25.21  ? 56  PRO A C   1 
ATOM   420  O  O   . PRO A 1 56  ? -28.606 39.140 16.403  1.00 27.59  ? 56  PRO A O   1 
ATOM   421  C  CB  . PRO A 1 56  ? -30.219 40.235 18.998  1.00 21.08  ? 56  PRO A CB  1 
ATOM   422  C  CG  . PRO A 1 56  ? -29.650 41.587 19.391  1.00 23.24  ? 56  PRO A CG  1 
ATOM   423  C  CD  . PRO A 1 56  ? -28.277 41.638 18.785  1.00 21.20  ? 56  PRO A CD  1 
ATOM   424  N  N   . GLY A 1 57  ? -29.688 37.439 17.385  1.00 23.03  ? 57  GLY A N   1 
ATOM   425  C  CA  . GLY A 1 57  ? -29.950 36.799 16.112  1.00 22.96  ? 57  GLY A CA  1 
ATOM   426  C  C   . GLY A 1 57  ? -30.804 37.702 15.236  1.00 24.07  ? 57  GLY A C   1 
ATOM   427  O  O   . GLY A 1 57  ? -31.695 38.403 15.718  1.00 25.96  ? 57  GLY A O   1 
ATOM   428  N  N   . PHE A 1 58  ? -30.505 37.707 13.944  1.00 24.97  ? 58  PHE A N   1 
ATOM   429  C  CA  . PHE A 1 58  ? -31.219 38.593 13.035  1.00 24.17  ? 58  PHE A CA  1 
ATOM   430  C  C   . PHE A 1 58  ? -32.629 38.078 12.785  1.00 19.42  ? 58  PHE A C   1 
ATOM   431  O  O   . PHE A 1 58  ? -32.874 36.866 12.735  1.00 25.45  ? 58  PHE A O   1 
ATOM   432  C  CB  . PHE A 1 58  ? -30.444 38.733 11.728  1.00 22.56  ? 58  PHE A CB  1 
ATOM   433  C  CG  . PHE A 1 58  ? -29.015 39.143 11.929  1.00 24.74  ? 58  PHE A CG  1 
ATOM   434  C  CD1 . PHE A 1 58  ? -28.652 39.923 13.029  1.00 24.93  ? 58  PHE A CD1 1 
ATOM   435  C  CD2 . PHE A 1 58  ? -28.023 38.726 11.047  1.00 22.63  ? 58  PHE A CD2 1 
ATOM   436  C  CE1 . PHE A 1 58  ? -27.328 40.303 13.234  1.00 25.00  ? 58  PHE A CE1 1 
ATOM   437  C  CE2 . PHE A 1 58  ? -26.683 39.085 11.249  1.00 22.30  ? 58  PHE A CE2 1 
ATOM   438  C  CZ  . PHE A 1 58  ? -26.336 39.887 12.335  1.00 26.36  ? 58  PHE A CZ  1 
ATOM   439  N  N   . ILE A 1 59  ? -33.568 39.009 12.654  1.00 23.03  ? 59  ILE A N   1 
ATOM   440  C  CA  . ILE A 1 59  ? -34.978 38.681 12.487  1.00 24.01  ? 59  ILE A CA  1 
ATOM   441  C  C   . ILE A 1 59  ? -35.375 39.090 11.078  1.00 23.99  ? 59  ILE A C   1 
ATOM   442  O  O   . ILE A 1 59  ? -35.393 40.286 10.755  1.00 23.45  ? 59  ILE A O   1 
ATOM   443  C  CB  . ILE A 1 59  ? -35.847 39.388 13.535  1.00 29.05  ? 59  ILE A CB  1 
ATOM   444  C  CG1 . ILE A 1 59  ? -35.400 39.035 14.952  1.00 23.70  ? 59  ILE A CG1 1 
ATOM   445  C  CG2 . ILE A 1 59  ? -37.306 39.039 13.342  1.00 30.58  ? 59  ILE A CG2 1 
ATOM   446  C  CD1 . ILE A 1 59  ? -36.099 39.846 16.001  1.00 18.51  ? 59  ILE A CD1 1 
ATOM   447  N  N   . ASP A 1 60  ? -35.690 38.112 10.228  1.00 21.29  ? 60  ASP A N   1 
ATOM   448  C  CA  . ASP A 1 60  ? -36.078 38.414 8.850   1.00 19.84  ? 60  ASP A CA  1 
ATOM   449  C  C   . ASP A 1 60  ? -37.576 38.676 8.837   1.00 22.63  ? 60  ASP A C   1 
ATOM   450  O  O   . ASP A 1 60  ? -38.379 37.742 8.790   1.00 22.31  ? 60  ASP A O   1 
ATOM   451  C  CB  . ASP A 1 60  ? -35.692 37.290 7.896   1.00 20.37  ? 60  ASP A CB  1 
ATOM   452  C  CG  . ASP A 1 60  ? -35.775 37.727 6.439   1.00 27.61  ? 60  ASP A CG  1 
ATOM   453  O  OD1 . ASP A 1 60  ? -36.246 38.853 6.199   1.00 26.16  ? 60  ASP A OD1 1 
ATOM   454  O  OD2 . ASP A 1 60  ? -35.360 36.971 5.535   1.00 28.97  ? 60  ASP A OD2 1 
ATOM   455  N  N   . VAL A 1 61  ? -37.953 39.956 8.902   1.00 21.79  ? 61  VAL A N   1 
ATOM   456  C  CA  . VAL A 1 61  ? -39.362 40.307 9.049   1.00 23.28  ? 61  VAL A CA  1 
ATOM   457  C  C   . VAL A 1 61  ? -40.156 40.127 7.760   1.00 27.70  ? 61  VAL A C   1 
ATOM   458  O  O   . VAL A 1 61  ? -41.391 40.133 7.804   1.00 24.08  ? 61  VAL A O   1 
ATOM   459  C  CB  . VAL A 1 61  ? -39.544 41.756 9.557   1.00 21.83  ? 61  VAL A CB  1 
ATOM   460  C  CG1 . VAL A 1 61  ? -38.825 41.952 10.864  1.00 24.41  ? 61  VAL A CG1 1 
ATOM   461  C  CG2 . VAL A 1 61  ? -39.092 42.786 8.517   1.00 19.99  ? 61  VAL A CG2 1 
ATOM   462  N  N   . HIS A 1 62  ? -39.503 39.975 6.605   1.00 26.31  ? 62  HIS A N   1 
ATOM   463  C  CA  . HIS A 1 62  ? -40.233 39.809 5.348   1.00 22.98  ? 62  HIS A CA  1 
ATOM   464  C  C   . HIS A 1 62  ? -39.730 38.581 4.598   1.00 26.55  ? 62  HIS A C   1 
ATOM   465  O  O   . HIS A 1 62  ? -38.776 38.657 3.817   1.00 26.22  ? 62  HIS A O   1 
ATOM   466  C  CB  . HIS A 1 62  ? -40.126 41.055 4.499   1.00 26.96  ? 62  HIS A CB  1 
ATOM   467  C  CG  . HIS A 1 62  ? -41.199 41.147 3.466   1.00 31.84  ? 62  HIS A CG  1 
ATOM   468  N  ND1 . HIS A 1 62  ? -41.191 40.388 2.313   1.00 28.46  ? 62  HIS A ND1 1 
ATOM   469  C  CD2 . HIS A 1 62  ? -42.328 41.887 3.421   1.00 28.79  ? 62  HIS A CD2 1 
ATOM   470  C  CE1 . HIS A 1 62  ? -42.256 40.681 1.590   1.00 26.75  ? 62  HIS A CE1 1 
ATOM   471  N  NE2 . HIS A 1 62  ? -42.964 41.586 2.239   1.00 33.98  ? 62  HIS A NE2 1 
ATOM   472  N  N   . THR A 1 63  ? -40.383 37.446 4.823   1.00 27.12  ? 63  THR A N   1 
ATOM   473  C  CA  . THR A 1 63  ? -40.012 36.215 4.150   1.00 23.97  ? 63  THR A CA  1 
ATOM   474  C  C   . THR A 1 63  ? -41.238 35.580 3.524   1.00 26.50  ? 63  THR A C   1 
ATOM   475  O  O   . THR A 1 63  ? -42.386 35.872 3.876   1.00 23.31  ? 63  THR A O   1 
ATOM   476  C  CB  . THR A 1 63  ? -39.368 35.182 5.091   1.00 28.30  ? 63  THR A CB  1 
ATOM   477  O  OG1 . THR A 1 63  ? -40.401 34.481 5.791   1.00 26.83  ? 63  THR A OG1 1 
ATOM   478  C  CG2 . THR A 1 63  ? -38.444 35.857 6.108   1.00 24.25  ? 63  THR A CG2 1 
ATOM   479  N  N   . HIS A 1 64  ? -40.956 34.693 2.585   1.00 23.66  ? 64  HIS A N   1 
ATOM   480  C  CA  . HIS A 1 64  ? -41.943 33.784 2.039   1.00 28.43  ? 64  HIS A CA  1 
ATOM   481  C  C   . HIS A 1 64  ? -41.472 32.351 2.271   1.00 26.57  ? 64  HIS A C   1 
ATOM   482  O  O   . HIS A 1 64  ? -41.548 31.509 1.374   1.00 27.67  ? 64  HIS A O   1 
ATOM   483  C  CB  . HIS A 1 64  ? -42.160 34.115 0.559   1.00 19.31  ? 64  HIS A CB  1 
ATOM   484  C  CG  . HIS A 1 64  ? -42.734 35.478 0.355   1.00 25.73  ? 64  HIS A CG  1 
ATOM   485  N  ND1 . HIS A 1 64  ? -44.015 35.805 0.749   1.00 26.47  ? 64  HIS A ND1 1 
ATOM   486  C  CD2 . HIS A 1 64  ? -42.182 36.619 -0.119  1.00 29.32  ? 64  HIS A CD2 1 
ATOM   487  C  CE1 . HIS A 1 64  ? -44.244 37.077 0.475   1.00 28.31  ? 64  HIS A CE1 1 
ATOM   488  N  NE2 . HIS A 1 64  ? -43.149 37.593 -0.054  1.00 32.85  ? 64  HIS A NE2 1 
ATOM   489  N  N   . ASP A 1 65  ? -40.997 32.072 3.485   1.00 26.22  ? 65  ASP A N   1 
ATOM   490  C  CA  . ASP A 1 65  ? -40.446 30.773 3.846   1.00 24.85  ? 65  ASP A CA  1 
ATOM   491  C  C   . ASP A 1 65  ? -41.486 29.825 4.423   1.00 26.15  ? 65  ASP A C   1 
ATOM   492  O  O   . ASP A 1 65  ? -41.116 28.755 4.915   1.00 27.69  ? 65  ASP A O   1 
ATOM   493  C  CB  . ASP A 1 65  ? -39.300 30.952 4.848   1.00 24.14  ? 65  ASP A CB  1 
ATOM   494  C  CG  . ASP A 1 65  ? -38.150 31.786 4.289   1.00 30.13  ? 65  ASP A CG  1 
ATOM   495  O  OD1 . ASP A 1 65  ? -37.897 31.713 3.063   1.00 26.37  ? 65  ASP A OD1 1 
ATOM   496  O  OD2 . ASP A 1 65  ? -37.499 32.518 5.073   1.00 26.94  ? 65  ASP A OD2 1 
ATOM   497  N  N   . ASP A 1 66  ? -42.768 30.195 4.356   1.00 25.26  ? 66  ASP A N   1 
ATOM   498  C  CA  . ASP A 1 66  ? -43.871 29.456 4.966   1.00 27.81  ? 66  ASP A CA  1 
ATOM   499  C  C   . ASP A 1 66  ? -43.706 27.951 4.878   1.00 28.50  ? 66  ASP A C   1 
ATOM   500  O  O   . ASP A 1 66  ? -43.735 27.244 5.890   1.00 26.17  ? 66  ASP A O   1 
ATOM   501  C  CB  . ASP A 1 66  ? -45.190 29.852 4.292   1.00 25.38  ? 66  ASP A CB  1 
ATOM   502  C  CG  . ASP A 1 66  ? -45.477 31.330 4.400   1.00 27.55  ? 66  ASP A CG  1 
ATOM   503  O  OD1 . ASP A 1 66  ? -44.609 32.150 4.023   1.00 26.28  ? 66  ASP A OD1 1 
ATOM   504  O  OD2 . ASP A 1 66  ? -46.585 31.670 4.842   1.00 22.60  ? 66  ASP A OD2 1 
ATOM   505  N  N   . ILE A 1 67  ? -43.542 27.452 3.660   1.00 26.98  ? 67  ILE A N   1 
ATOM   506  C  CA  . ILE A 1 67  ? -43.542 26.021 3.415   1.00 31.33  ? 67  ILE A CA  1 
ATOM   507  C  C   . ILE A 1 67  ? -42.112 25.504 3.305   1.00 26.11  ? 67  ILE A C   1 
ATOM   508  O  O   . ILE A 1 67  ? -41.813 24.373 3.710   1.00 26.58  ? 67  ILE A O   1 
ATOM   509  C  CB  . ILE A 1 67  ? -44.385 25.710 2.161   1.00 33.46  ? 67  ILE A CB  1 
ATOM   510  C  CG1 . ILE A 1 67  ? -45.869 25.694 2.549   1.00 33.02  ? 67  ILE A CG1 1 
ATOM   511  C  CG2 . ILE A 1 67  ? -43.984 24.380 1.537   1.00 28.59  ? 67  ILE A CG2 1 
ATOM   512  C  CD1 . ILE A 1 67  ? -46.811 25.589 1.402   1.00 39.59  ? 67  ILE A CD1 1 
ATOM   513  N  N   . ASN A 1 68  ? -41.207 26.342 2.796   1.00 32.25  ? 68  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 68  ? -39.841 25.884 2.535   1.00 32.52  ? 68  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 68  ? -39.068 25.631 3.818   1.00 29.97  ? 68  ASN A C   1 
ATOM   516  O  O   . ASN A 1 68  ? -38.213 24.739 3.859   1.00 30.98  ? 68  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 68  ? -39.105 26.900 1.670   1.00 25.86  ? 68  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 68  ? -39.508 26.815 0.218   1.00 36.97  ? 68  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 68  ? -40.637 27.147 -0.152  1.00 36.68  ? 68  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 68  ? -38.587 26.356 -0.618  1.00 33.91  ? 68  ASN A ND2 1 
ATOM   521  N  N   . VAL A 1 69  ? -39.347 26.395 4.874   1.00 24.90  ? 69  VAL A N   1 
ATOM   522  C  CA  . VAL A 1 69  ? -38.664 26.133 6.134   1.00 30.77  ? 69  VAL A CA  1 
ATOM   523  C  C   . VAL A 1 69  ? -39.063 24.764 6.695   1.00 32.53  ? 69  VAL A C   1 
ATOM   524  O  O   . VAL A 1 69  ? -38.273 24.111 7.387   1.00 33.50  ? 69  VAL A O   1 
ATOM   525  C  CB  . VAL A 1 69  ? -38.938 27.276 7.129   1.00 26.66  ? 69  VAL A CB  1 
ATOM   526  C  CG1 . VAL A 1 69  ? -40.372 27.189 7.665   1.00 24.57  ? 69  VAL A CG1 1 
ATOM   527  C  CG2 . VAL A 1 69  ? -37.926 27.223 8.256   1.00 33.19  ? 69  VAL A CG2 1 
ATOM   528  N  N   . ILE A 1 70  ? -40.270 24.291 6.389   1.00 31.53  ? 70  ILE A N   1 
ATOM   529  C  CA  . ILE A 1 70  ? -40.668 22.946 6.792   1.00 26.51  ? 70  ILE A CA  1 
ATOM   530  C  C   . ILE A 1 70  ? -40.017 21.894 5.901   1.00 34.97  ? 70  ILE A C   1 
ATOM   531  O  O   . ILE A 1 70  ? -39.584 20.838 6.376   1.00 37.59  ? 70  ILE A O   1 
ATOM   532  C  CB  . ILE A 1 70  ? -42.203 22.832 6.767   1.00 30.20  ? 70  ILE A CB  1 
ATOM   533  C  CG1 . ILE A 1 70  ? -42.819 23.776 7.798   1.00 31.44  ? 70  ILE A CG1 1 
ATOM   534  C  CG2 . ILE A 1 70  ? -42.633 21.396 6.999   1.00 31.25  ? 70  ILE A CG2 1 
ATOM   535  C  CD1 . ILE A 1 70  ? -44.307 23.719 7.839   1.00 31.02  ? 70  ILE A CD1 1 
ATOM   536  N  N   A ARG A 1 71  ? -39.905 22.178 4.606   0.47 34.25  ? 71  ARG A N   1 
ATOM   537  N  N   B ARG A 1 71  ? -39.938 22.168 4.597   0.53 34.26  ? 71  ARG A N   1 
ATOM   538  C  CA  A ARG A 1 71  ? -39.355 21.171 3.662   0.47 34.61  ? 71  ARG A CA  1 
ATOM   539  C  CA  B ARG A 1 71  ? -39.364 21.215 3.655   0.53 34.62  ? 71  ARG A CA  1 
ATOM   540  C  C   A ARG A 1 71  ? -37.827 21.093 3.813   0.47 34.01  ? 71  ARG A C   1 
ATOM   541  C  C   B ARG A 1 71  ? -37.852 21.110 3.813   0.53 34.02  ? 71  ARG A C   1 
ATOM   542  O  O   A ARG A 1 71  ? -37.304 19.966 3.796   0.47 33.94  ? 71  ARG A O   1 
ATOM   543  O  O   B ARG A 1 71  ? -37.279 20.037 3.595   0.53 33.97  ? 71  ARG A O   1 
ATOM   544  C  CB  A ARG A 1 71  ? -39.781 21.524 2.235   0.47 37.75  ? 71  ARG A CB  1 
ATOM   545  C  CB  B ARG A 1 71  ? -39.764 21.625 2.232   0.53 37.70  ? 71  ARG A CB  1 
ATOM   546  C  CG  A ARG A 1 71  ? -38.819 22.456 1.515   0.47 38.62  ? 71  ARG A CG  1 
ATOM   547  C  CG  B ARG A 1 71  ? -38.949 21.054 1.060   0.53 43.55  ? 71  ARG A CG  1 
ATOM   548  C  CD  A ARG A 1 71  ? -39.557 23.408 0.592   0.47 45.13  ? 71  ARG A CD  1 
ATOM   549  C  CD  B ARG A 1 71  ? -39.523 21.608 -0.262  0.53 43.35  ? 71  ARG A CD  1 
ATOM   550  N  NE  A ARG A 1 71  ? -40.659 22.750 -0.116  0.47 47.66  ? 71  ARG A NE  1 
ATOM   551  N  NE  B ARG A 1 71  ? -38.813 21.178 -1.460  0.53 54.94  ? 71  ARG A NE  1 
ATOM   552  C  CZ  A ARG A 1 71  ? -40.694 22.584 -1.429  0.47 46.73  ? 71  ARG A CZ  1 
ATOM   553  C  CZ  B ARG A 1 71  ? -38.240 21.999 -2.332  0.53 58.50  ? 71  ARG A CZ  1 
ATOM   554  N  NH1 A ARG A 1 71  ? -39.684 23.000 -2.169  0.47 55.30  ? 71  ARG A NH1 1 
ATOM   555  N  NH1 B ARG A 1 71  ? -38.229 23.311 -2.144  0.53 47.75  ? 71  ARG A NH1 1 
ATOM   556  N  NH2 A ARG A 1 71  ? -41.742 22.015 -1.997  0.47 50.11  ? 71  ARG A NH2 1 
ATOM   557  N  NH2 B ARG A 1 71  ? -37.679 21.493 -3.429  0.53 51.82  ? 71  ARG A NH2 1 
ATOM   558  N  N   . MET A 1 72  ? -37.195 22.196 4.209   1.00 32.08  ? 72  MET A N   1 
ATOM   559  C  CA  . MET A 1 72  ? -35.744 22.231 4.392   1.00 32.10  ? 72  MET A CA  1 
ATOM   560  C  C   . MET A 1 72  ? -35.460 22.867 5.746   1.00 32.86  ? 72  MET A C   1 
ATOM   561  O  O   . MET A 1 72  ? -35.043 24.029 5.829   1.00 28.43  ? 72  MET A O   1 
ATOM   562  C  CB  . MET A 1 72  ? -35.061 22.991 3.252   1.00 33.91  ? 72  MET A CB  1 
ATOM   563  C  CG  . MET A 1 72  ? -33.531 22.997 3.303   1.00 44.87  ? 72  MET A CG  1 
ATOM   564  S  SD  . MET A 1 72  ? -32.765 23.985 1.986   1.00 48.72  ? 72  MET A SD  1 
ATOM   565  C  CE  . MET A 1 72  ? -32.273 25.431 2.904   1.00 39.77  ? 72  MET A CE  1 
ATOM   566  N  N   . PRO A 1 73  ? -35.701 22.127 6.836   1.00 29.41  ? 73  PRO A N   1 
ATOM   567  C  CA  . PRO A 1 73  ? -35.489 22.689 8.183   1.00 27.49  ? 73  PRO A CA  1 
ATOM   568  C  C   . PRO A 1 73  ? -34.096 23.259 8.415   1.00 30.35  ? 73  PRO A C   1 
ATOM   569  O  O   . PRO A 1 73  ? -33.951 24.258 9.129   1.00 30.55  ? 73  PRO A O   1 
ATOM   570  C  CB  . PRO A 1 73  ? -35.764 21.489 9.104   1.00 25.95  ? 73  PRO A CB  1 
ATOM   571  C  CG  . PRO A 1 73  ? -35.694 20.269 8.209   1.00 30.91  ? 73  PRO A CG  1 
ATOM   572  C  CD  . PRO A 1 73  ? -36.169 20.734 6.877   1.00 28.62  ? 73  PRO A CD  1 
ATOM   573  N  N   . GLU A 1 74  ? -33.057 22.641 7.860   1.00 29.00  ? 74  GLU A N   1 
ATOM   574  C  CA  . GLU A 1 74  ? -31.712 23.210 7.946   1.00 32.53  ? 74  GLU A CA  1 
ATOM   575  C  C   . GLU A 1 74  ? -31.621 24.318 6.908   1.00 30.49  ? 74  GLU A C   1 
ATOM   576  O  O   . GLU A 1 74  ? -31.024 24.176 5.839   1.00 30.47  ? 74  GLU A O   1 
ATOM   577  C  CB  . GLU A 1 74  ? -30.662 22.131 7.748   1.00 30.16  ? 74  GLU A CB  1 
ATOM   578  C  CG  . GLU A 1 74  ? -30.830 21.012 8.778   1.00 33.87  ? 74  GLU A CG  1 
ATOM   579  C  CD  . GLU A 1 74  ? -29.664 20.063 8.792   1.00 36.92  ? 74  GLU A CD  1 
ATOM   580  O  OE1 . GLU A 1 74  ? -28.672 20.340 8.086   1.00 43.84  ? 74  GLU A OE1 1 
ATOM   581  O  OE2 . GLU A 1 74  ? -29.739 19.044 9.505   1.00 41.23  ? 74  GLU A OE2 1 
ATOM   582  N  N   . TYR A 1 75  ? -32.244 25.445 7.248   1.00 26.69  ? 75  TYR A N   1 
ATOM   583  C  CA  . TYR A 1 75  ? -32.574 26.491 6.282   1.00 29.90  ? 75  TYR A CA  1 
ATOM   584  C  C   . TYR A 1 75  ? -31.367 27.408 6.066   1.00 28.82  ? 75  TYR A C   1 
ATOM   585  O  O   . TYR A 1 75  ? -31.319 28.560 6.494   1.00 30.21  ? 75  TYR A O   1 
ATOM   586  C  CB  . TYR A 1 75  ? -33.805 27.248 6.756   1.00 23.14  ? 75  TYR A CB  1 
ATOM   587  C  CG  . TYR A 1 75  ? -34.555 27.921 5.631   1.00 25.88  ? 75  TYR A CG  1 
ATOM   588  C  CD1 . TYR A 1 75  ? -35.042 27.184 4.568   1.00 27.04  ? 75  TYR A CD1 1 
ATOM   589  C  CD2 . TYR A 1 75  ? -34.781 29.294 5.641   1.00 25.04  ? 75  TYR A CD2 1 
ATOM   590  C  CE1 . TYR A 1 75  ? -35.719 27.794 3.530   1.00 32.82  ? 75  TYR A CE1 1 
ATOM   591  C  CE2 . TYR A 1 75  ? -35.460 29.907 4.622   1.00 25.01  ? 75  TYR A CE2 1 
ATOM   592  C  CZ  . TYR A 1 75  ? -35.924 29.157 3.563   1.00 33.81  ? 75  TYR A CZ  1 
ATOM   593  O  OH  . TYR A 1 75  ? -36.601 29.776 2.535   1.00 40.00  ? 75  TYR A OH  1 
ATOM   594  N  N   . LEU A 1 76  ? -30.391 26.869 5.347   1.00 30.29  ? 76  LEU A N   1 
ATOM   595  C  CA  . LEU A 1 76  ? -29.120 27.550 5.114   1.00 31.27  ? 76  LEU A CA  1 
ATOM   596  C  C   . LEU A 1 76  ? -29.218 28.965 4.544   1.00 34.09  ? 76  LEU A C   1 
ATOM   597  O  O   . LEU A 1 76  ? -28.422 29.821 4.968   1.00 29.88  ? 76  LEU A O   1 
ATOM   598  C  CB  . LEU A 1 76  ? -28.279 26.684 4.171   1.00 31.18  ? 76  LEU A CB  1 
ATOM   599  C  CG  . LEU A 1 76  ? -26.816 27.072 4.019   1.00 35.25  ? 76  LEU A CG  1 
ATOM   600  C  CD1 . LEU A 1 76  ? -26.129 27.045 5.365   1.00 29.39  ? 76  LEU A CD1 1 
ATOM   601  C  CD2 . LEU A 1 76  ? -26.161 26.106 3.061   1.00 27.06  ? 76  LEU A CD2 1 
ATOM   602  N  N   . PRO A 1 77  ? -30.087 29.271 3.572   1.00 34.74  ? 77  PRO A N   1 
ATOM   603  C  CA  . PRO A 1 77  ? -30.074 30.633 3.008   1.00 26.42  ? 77  PRO A CA  1 
ATOM   604  C  C   . PRO A 1 77  ? -30.216 31.711 4.066   1.00 28.72  ? 77  PRO A C   1 
ATOM   605  O  O   . PRO A 1 77  ? -29.608 32.779 3.947   1.00 28.51  ? 77  PRO A O   1 
ATOM   606  C  CB  . PRO A 1 77  ? -31.273 30.627 2.046   1.00 28.19  ? 77  PRO A CB  1 
ATOM   607  C  CG  . PRO A 1 77  ? -31.534 29.187 1.753   1.00 30.81  ? 77  PRO A CG  1 
ATOM   608  C  CD  . PRO A 1 77  ? -31.187 28.462 3.016   1.00 34.13  ? 77  PRO A CD  1 
ATOM   609  N  N   . LYS A 1 78  ? -31.020 31.469 5.101   1.00 25.78  ? 78  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 78  ? -31.201 32.479 6.130   1.00 25.15  ? 78  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 78  ? -30.210 32.300 7.274   1.00 30.07  ? 78  LYS A C   1 
ATOM   612  O  O   . LYS A 1 78  ? -29.624 33.281 7.752   1.00 30.64  ? 78  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 78  ? -32.643 32.446 6.643   1.00 24.66  ? 78  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 78  ? -33.665 32.744 5.555   1.00 30.01  ? 78  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 78  ? -33.337 34.046 4.847   1.00 27.50  ? 78  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 78  ? -34.297 34.354 3.686   1.00 23.38  ? 78  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 78  ? -35.668 34.648 4.169   1.00 23.94  ? 78  LYS A NZ  1 
ATOM   618  N  N   . LEU A 1 79  ? -29.981 31.056 7.690   1.00 26.60  ? 79  LEU A N   1 
ATOM   619  C  CA  . LEU A 1 79  ? -29.118 30.804 8.836   1.00 27.90  ? 79  LEU A CA  1 
ATOM   620  C  C   . LEU A 1 79  ? -27.689 31.260 8.575   1.00 30.32  ? 79  LEU A C   1 
ATOM   621  O  O   . LEU A 1 79  ? -27.037 31.813 9.468   1.00 29.82  ? 79  LEU A O   1 
ATOM   622  C  CB  . LEU A 1 79  ? -29.154 29.320 9.198   1.00 26.14  ? 79  LEU A CB  1 
ATOM   623  C  CG  . LEU A 1 79  ? -28.591 28.948 10.576  1.00 31.75  ? 79  LEU A CG  1 
ATOM   624  C  CD1 . LEU A 1 79  ? -29.351 29.633 11.690  1.00 21.76  ? 79  LEU A CD1 1 
ATOM   625  C  CD2 . LEU A 1 79  ? -28.591 27.438 10.775  1.00 33.19  ? 79  LEU A CD2 1 
ATOM   626  N  N   . SER A 1 80  ? -27.176 31.023 7.367   1.00 26.70  ? 80  SER A N   1 
ATOM   627  C  CA  . SER A 1 80  ? -25.819 31.450 7.025   1.00 26.18  ? 80  SER A CA  1 
ATOM   628  C  C   . SER A 1 80  ? -25.670 32.969 6.999   1.00 26.23  ? 80  SER A C   1 
ATOM   629  O  O   . SER A 1 80  ? -24.539 33.463 6.969   1.00 24.26  ? 80  SER A O   1 
ATOM   630  C  CB  . SER A 1 80  ? -25.394 30.881 5.660   1.00 27.69  ? 80  SER A CB  1 
ATOM   631  O  OG  . SER A 1 80  ? -26.243 31.353 4.603   1.00 24.62  ? 80  SER A OG  1 
ATOM   632  N  N   . GLN A 1 81  ? -26.774 33.716 6.982   1.00 26.11  ? 81  GLN A N   1 
ATOM   633  C  CA  . GLN A 1 81  ? -26.731 35.168 7.074   1.00 23.32  ? 81  GLN A CA  1 
ATOM   634  C  C   . GLN A 1 81  ? -26.702 35.676 8.504   1.00 30.93  ? 81  GLN A C   1 
ATOM   635  O  O   . GLN A 1 81  ? -26.556 36.884 8.692   1.00 28.08  ? 81  GLN A O   1 
ATOM   636  C  CB  . GLN A 1 81  ? -27.952 35.805 6.410   1.00 29.46  ? 81  GLN A CB  1 
ATOM   637  C  CG  . GLN A 1 81  ? -28.204 35.444 4.982   1.00 24.51  ? 81  GLN A CG  1 
ATOM   638  C  CD  . GLN A 1 81  ? -29.265 36.346 4.379   1.00 26.71  ? 81  GLN A CD  1 
ATOM   639  O  OE1 . GLN A 1 81  ? -29.260 37.565 4.592   1.00 25.73  ? 81  GLN A OE1 1 
ATOM   640  N  NE2 . GLN A 1 81  ? -30.195 35.748 3.639   1.00 27.64  ? 81  GLN A NE2 1 
ATOM   641  N  N   . GLY A 1 82  ? -26.868 34.797 9.503   1.00 21.89  ? 82  GLY A N   1 
ATOM   642  C  CA  . GLY A 1 82  ? -27.102 35.213 10.871  1.00 22.80  ? 82  GLY A CA  1 
ATOM   643  C  C   . GLY A 1 82  ? -28.559 35.307 11.276  1.00 25.40  ? 82  GLY A C   1 
ATOM   644  O  O   . GLY A 1 82  ? -28.849 35.769 12.389  1.00 22.24  ? 82  GLY A O   1 
ATOM   645  N  N   . VAL A 1 83  ? -29.484 34.909 10.408  1.00 21.68  ? 83  VAL A N   1 
ATOM   646  C  CA  . VAL A 1 83  ? -30.907 34.995 10.715  1.00 25.09  ? 83  VAL A CA  1 
ATOM   647  C  C   . VAL A 1 83  ? -31.290 33.852 11.644  1.00 22.02  ? 83  VAL A C   1 
ATOM   648  O  O   . VAL A 1 83  ? -31.047 32.679 11.333  1.00 22.45  ? 83  VAL A O   1 
ATOM   649  C  CB  . VAL A 1 83  ? -31.748 34.957 9.428   1.00 32.91  ? 83  VAL A CB  1 
ATOM   650  C  CG1 . VAL A 1 83  ? -33.240 34.922 9.779   1.00 19.33  ? 83  VAL A CG1 1 
ATOM   651  C  CG2 . VAL A 1 83  ? -31.413 36.153 8.507   1.00 19.03  ? 83  VAL A CG2 1 
ATOM   652  N  N   . THR A 1 84  ? -31.921 34.182 12.775  1.00 22.15  ? 84  THR A N   1 
ATOM   653  C  CA  . THR A 1 84  ? -32.385 33.158 13.706  1.00 27.23  ? 84  THR A CA  1 
ATOM   654  C  C   . THR A 1 84  ? -33.905 33.074 13.810  1.00 25.98  ? 84  THR A C   1 
ATOM   655  O  O   . THR A 1 84  ? -34.418 32.124 14.420  1.00 24.27  ? 84  THR A O   1 
ATOM   656  C  CB  . THR A 1 84  ? -31.795 33.385 15.117  1.00 27.97  ? 84  THR A CB  1 
ATOM   657  O  OG1 . THR A 1 84  ? -32.078 34.722 15.556  1.00 24.19  ? 84  THR A OG1 1 
ATOM   658  C  CG2 . THR A 1 84  ? -30.294 33.149 15.116  1.00 23.39  ? 84  THR A CG2 1 
ATOM   659  N  N   . THR A 1 85  ? -34.631 34.037 13.248  1.00 21.98  ? 85  THR A N   1 
ATOM   660  C  CA  . THR A 1 85  ? -36.086 33.984 13.182  1.00 27.51  ? 85  THR A CA  1 
ATOM   661  C  C   . THR A 1 85  ? -36.531 34.486 11.818  1.00 28.69  ? 85  THR A C   1 
ATOM   662  O  O   . THR A 1 85  ? -36.048 35.523 11.356  1.00 22.38  ? 85  THR A O   1 
ATOM   663  C  CB  . THR A 1 85  ? -36.739 34.841 14.270  1.00 23.55  ? 85  THR A CB  1 
ATOM   664  O  OG1 . THR A 1 85  ? -36.425 34.306 15.552  1.00 28.78  ? 85  THR A OG1 1 
ATOM   665  C  CG2 . THR A 1 85  ? -38.242 34.842 14.106  1.00 22.76  ? 85  THR A CG2 1 
ATOM   666  N  N   . VAL A 1 86  ? -37.452 33.760 11.184  1.00 27.05  ? 86  VAL A N   1 
ATOM   667  C  CA  . VAL A 1 86  ? -38.107 34.203 9.959   1.00 24.33  ? 86  VAL A CA  1 
ATOM   668  C  C   . VAL A 1 86  ? -39.570 34.488 10.275  1.00 24.84  ? 86  VAL A C   1 
ATOM   669  O  O   . VAL A 1 86  ? -40.223 33.737 11.013  1.00 23.43  ? 86  VAL A O   1 
ATOM   670  C  CB  . VAL A 1 86  ? -37.980 33.176 8.811   1.00 24.69  ? 86  VAL A CB  1 
ATOM   671  C  CG1 . VAL A 1 86  ? -36.508 33.005 8.390   1.00 18.55  ? 86  VAL A CG1 1 
ATOM   672  C  CG2 . VAL A 1 86  ? -38.612 31.831 9.189   1.00 23.90  ? 86  VAL A CG2 1 
ATOM   673  N  N   . ILE A 1 87  ? -40.079 35.586 9.729   1.00 26.36  ? 87  ILE A N   1 
ATOM   674  C  CA  . ILE A 1 87  ? -41.498 35.904 9.801   1.00 29.63  ? 87  ILE A CA  1 
ATOM   675  C  C   . ILE A 1 87  ? -42.108 35.576 8.452   1.00 25.39  ? 87  ILE A C   1 
ATOM   676  O  O   . ILE A 1 87  ? -41.750 36.183 7.437   1.00 24.56  ? 87  ILE A O   1 
ATOM   677  C  CB  . ILE A 1 87  ? -41.734 37.372 10.177  1.00 28.29  ? 87  ILE A CB  1 
ATOM   678  C  CG1 . ILE A 1 87  ? -41.099 37.659 11.537  1.00 25.51  ? 87  ILE A CG1 1 
ATOM   679  C  CG2 . ILE A 1 87  ? -43.234 37.684 10.146  1.00 17.70  ? 87  ILE A CG2 1 
ATOM   680  C  CD1 . ILE A 1 87  ? -41.655 38.886 12.235  1.00 24.99  ? 87  ILE A CD1 1 
ATOM   681  N  N   . VAL A 1 88  ? -43.032 34.625 8.441   1.00 26.62  ? 88  VAL A N   1 
ATOM   682  C  CA  . VAL A 1 88  ? -43.602 34.119 7.208   1.00 26.36  ? 88  VAL A CA  1 
ATOM   683  C  C   . VAL A 1 88  ? -45.010 34.675 7.028   1.00 22.70  ? 88  VAL A C   1 
ATOM   684  O  O   . VAL A 1 88  ? -45.549 35.363 7.891   1.00 23.13  ? 88  VAL A O   1 
ATOM   685  C  CB  . VAL A 1 88  ? -43.587 32.574 7.174   1.00 28.64  ? 88  VAL A CB  1 
ATOM   686  C  CG1 . VAL A 1 88  ? -42.189 32.066 7.488   1.00 18.57  ? 88  VAL A CG1 1 
ATOM   687  C  CG2 . VAL A 1 88  ? -44.583 32.008 8.164   1.00 19.21  ? 88  VAL A CG2 1 
ATOM   688  N  N   . GLY A 1 89  ? -45.600 34.418 5.861   1.00 26.01  ? 89  GLY A N   1 
ATOM   689  C  CA  . GLY A 1 89  ? -46.969 34.806 5.583   1.00 17.18  ? 89  GLY A CA  1 
ATOM   690  C  C   . GLY A 1 89  ? -47.157 36.234 5.125   1.00 26.47  ? 89  GLY A C   1 
ATOM   691  O  O   . GLY A 1 89  ? -48.170 36.866 5.478   1.00 21.90  ? 89  GLY A O   1 
ATOM   692  N  N   . ASN A 1 90  ? -46.221 36.758 4.331   1.00 26.03  ? 90  ASN A N   1 
ATOM   693  C  CA  . ASN A 1 90  ? -46.233 38.152 3.908   1.00 23.20  ? 90  ASN A CA  1 
ATOM   694  C  C   . ASN A 1 90  ? -46.976 38.360 2.591   1.00 27.07  ? 90  ASN A C   1 
ATOM   695  O  O   . ASN A 1 90  ? -47.372 37.414 1.907   1.00 24.32  ? 90  ASN A O   1 
ATOM   696  C  CB  . ASN A 1 90  ? -44.802 38.678 3.797   1.00 22.88  ? 90  ASN A CB  1 
ATOM   697  C  CG  . ASN A 1 90  ? -44.210 38.955 5.150   1.00 29.57  ? 90  ASN A CG  1 
ATOM   698  O  OD1 . ASN A 1 90  ? -44.423 40.020 5.728   1.00 27.06  ? 90  ASN A OD1 1 
ATOM   699  N  ND2 . ASN A 1 90  ? -43.504 37.976 5.690   1.00 27.11  ? 90  ASN A ND2 1 
ATOM   700  N  N   . CYS A 1 91  ? -47.185 39.642 2.264   1.00 24.78  ? 91  CYS A N   1 
ATOM   701  C  CA  . CYS A 1 91  ? -47.801 40.083 1.004   1.00 27.58  ? 91  CYS A CA  1 
ATOM   702  C  C   . CYS A 1 91  ? -49.151 39.423 0.740   1.00 28.27  ? 91  CYS A C   1 
ATOM   703  O  O   . CYS A 1 91  ? -49.515 39.162 -0.411  1.00 27.48  ? 91  CYS A O   1 
ATOM   704  C  CB  . CYS A 1 91  ? -46.859 39.848 -0.170  1.00 24.02  ? 91  CYS A CB  1 
ATOM   705  S  SG  . CYS A 1 91  ? -45.304 40.689 0.102   1.00 25.93  ? 91  CYS A SG  1 
ATOM   706  N  N   . GLY A 1 92  ? -49.913 39.160 1.794   1.00 24.02  ? 92  GLY A N   1 
ATOM   707  C  CA  . GLY A 1 92  ? -51.242 38.618 1.635   1.00 24.95  ? 92  GLY A CA  1 
ATOM   708  C  C   . GLY A 1 92  ? -51.319 37.117 1.447   1.00 26.40  ? 92  GLY A C   1 
ATOM   709  O  O   . GLY A 1 92  ? -52.426 36.593 1.271   1.00 23.94  ? 92  GLY A O   1 
ATOM   710  N  N   . ILE A 1 93  ? -50.191 36.403 1.489   1.00 22.69  ? 93  ILE A N   1 
ATOM   711  C  CA  . ILE A 1 93  ? -50.159 34.969 1.197   1.00 25.31  ? 93  ILE A CA  1 
ATOM   712  C  C   . ILE A 1 93  ? -49.467 34.247 2.345   1.00 28.29  ? 93  ILE A C   1 
ATOM   713  O  O   . ILE A 1 93  ? -48.321 34.568 2.699   1.00 28.71  ? 93  ILE A O   1 
ATOM   714  C  CB  . ILE A 1 93  ? -49.463 34.651 -0.141  1.00 28.13  ? 93  ILE A CB  1 
ATOM   715  C  CG1 . ILE A 1 93  ? -48.053 35.266 -0.198  1.00 24.66  ? 93  ILE A CG1 1 
ATOM   716  C  CG2 . ILE A 1 93  ? -50.318 35.131 -1.303  1.00 27.56  ? 93  ILE A CG2 1 
ATOM   717  C  CD1 . ILE A 1 93  ? -47.155 34.655 -1.253  1.00 33.04  ? 93  ILE A CD1 1 
ATOM   718  N  N   . SER A 1 94  ? -50.158 33.273 2.922   1.00 22.74  ? 94  SER A N   1 
ATOM   719  C  CA  . SER A 1 94  ? -49.608 32.500 4.020   1.00 26.68  ? 94  SER A CA  1 
ATOM   720  C  C   . SER A 1 94  ? -50.048 31.059 3.850   1.00 20.78  ? 94  SER A C   1 
ATOM   721  O  O   . SER A 1 94  ? -51.151 30.788 3.358   1.00 26.97  ? 94  SER A O   1 
ATOM   722  C  CB  . SER A 1 94  ? -50.059 33.045 5.395   1.00 24.23  ? 94  SER A CB  1 
ATOM   723  O  OG  . SER A 1 94  ? -51.477 32.955 5.584   1.00 23.36  ? 94  SER A OG  1 
ATOM   724  N  N   . ALA A 1 95  ? -49.175 30.135 4.240   1.00 24.19  ? 95  ALA A N   1 
ATOM   725  C  CA  . ALA A 1 95  ? -49.594 28.739 4.321   1.00 24.46  ? 95  ALA A CA  1 
ATOM   726  C  C   . ALA A 1 95  ? -50.557 28.522 5.486   1.00 26.60  ? 95  ALA A C   1 
ATOM   727  O  O   . ALA A 1 95  ? -51.560 27.811 5.342   1.00 24.93  ? 95  ALA A O   1 
ATOM   728  C  CB  . ALA A 1 95  ? -48.374 27.830 4.459   1.00 28.66  ? 95  ALA A CB  1 
ATOM   729  N  N   . ALA A 1 96  ? -50.272 29.129 6.643   1.00 22.59  ? 96  ALA A N   1 
ATOM   730  C  CA  . ALA A 1 96  ? -51.132 28.973 7.815   1.00 29.39  ? 96  ALA A CA  1 
ATOM   731  C  C   . ALA A 1 96  ? -52.539 29.465 7.515   1.00 29.76  ? 96  ALA A C   1 
ATOM   732  O  O   . ALA A 1 96  ? -52.722 30.573 7.000   1.00 27.39  ? 96  ALA A O   1 
ATOM   733  C  CB  . ALA A 1 96  ? -50.561 29.743 9.012   1.00 25.58  ? 96  ALA A CB  1 
ATOM   734  N  N   . THR A 1 97  ? -53.529 28.632 7.848   1.00 29.43  ? 97  THR A N   1 
ATOM   735  C  CA  . THR A 1 97  ? -54.974 28.816 7.648   1.00 27.35  ? 97  THR A CA  1 
ATOM   736  C  C   . THR A 1 97  ? -55.428 28.643 6.199   1.00 31.11  ? 97  THR A C   1 
ATOM   737  O  O   . THR A 1 97  ? -56.636 28.698 5.948   1.00 28.26  ? 97  THR A O   1 
ATOM   738  C  CB  . THR A 1 97  ? -55.503 30.177 8.152   1.00 26.12  ? 97  THR A CB  1 
ATOM   739  O  OG1 . THR A 1 97  ? -55.290 31.202 7.167   1.00 26.66  ? 97  THR A OG1 1 
ATOM   740  C  CG2 . THR A 1 97  ? -54.822 30.575 9.454   1.00 25.37  ? 97  THR A CG2 1 
ATOM   741  N  N   . ALA A 1 98  ? -54.525 28.429 5.240   1.00 28.21  ? 98  ALA A N   1 
ATOM   742  C  CA  . ALA A 1 98  ? -54.929 28.383 3.837   1.00 29.76  ? 98  ALA A CA  1 
ATOM   743  C  C   . ALA A 1 98  ? -55.479 27.009 3.494   1.00 35.53  ? 98  ALA A C   1 
ATOM   744  O  O   . ALA A 1 98  ? -54.795 25.992 3.663   1.00 35.17  ? 98  ALA A O   1 
ATOM   745  C  CB  . ALA A 1 98  ? -53.771 28.729 2.907   1.00 27.55  ? 98  ALA A CB  1 
ATOM   746  N  N   . THR A 1 99  ? -56.714 26.989 3.014   1.00 35.35  ? 99  THR A N   1 
ATOM   747  C  CA  . THR A 1 99  ? -57.336 25.818 2.423   1.00 37.03  ? 99  THR A CA  1 
ATOM   748  C  C   . THR A 1 99  ? -57.493 26.067 0.930   1.00 43.50  ? 99  THR A C   1 
ATOM   749  O  O   . THR A 1 99  ? -57.928 27.150 0.525   1.00 43.11  ? 99  THR A O   1 
ATOM   750  C  CB  . THR A 1 99  ? -58.689 25.550 3.080   1.00 37.10  ? 99  THR A CB  1 
ATOM   751  O  OG1 . THR A 1 99  ? -58.470 25.122 4.429   1.00 42.05  ? 99  THR A OG1 1 
ATOM   752  C  CG2 . THR A 1 99  ? -59.467 24.467 2.324   1.00 42.45  ? 99  THR A CG2 1 
ATOM   753  N  N   . MET A 1 100 ? -57.119 25.081 0.118   1.00 42.72  ? 100 MET A N   1 
ATOM   754  C  CA  . MET A 1 100 ? -57.220 25.164 -1.341  1.00 47.54  ? 100 MET A CA  1 
ATOM   755  C  C   . MET A 1 100 ? -58.374 24.291 -1.811  1.00 49.02  ? 100 MET A C   1 
ATOM   756  O  O   . MET A 1 100 ? -58.244 23.067 -1.884  1.00 56.63  ? 100 MET A O   1 
ATOM   757  C  CB  . MET A 1 100 ? -55.921 24.730 -2.009  1.00 48.67  ? 100 MET A CB  1 
ATOM   758  C  CG  . MET A 1 100 ? -54.761 25.648 -1.725  1.00 51.04  ? 100 MET A CG  1 
ATOM   759  S  SD  . MET A 1 100 ? -55.113 27.315 -2.313  1.00 54.47  ? 100 MET A SD  1 
ATOM   760  C  CE  . MET A 1 100 ? -53.717 28.195 -1.616  1.00 42.31  ? 100 MET A CE  1 
ATOM   761  N  N   . ARG A 1 101 ? -59.502 24.915 -2.136  1.00 53.16  ? 101 ARG A N   1 
ATOM   762  C  CA  A ARG A 1 101 ? -60.649 24.199 -2.675  0.57 53.98  ? 101 ARG A CA  1 
ATOM   763  C  CA  B ARG A 1 101 ? -60.629 24.163 -2.670  0.43 53.99  ? 101 ARG A CA  1 
ATOM   764  C  C   . ARG A 1 101 ? -60.541 23.975 -4.176  1.00 63.89  ? 101 ARG A C   1 
ATOM   765  O  O   . ARG A 1 101 ? -61.488 23.460 -4.779  1.00 71.24  ? 101 ARG A O   1 
ATOM   766  C  CB  A ARG A 1 101 ? -61.939 24.960 -2.348  0.57 54.00  ? 101 ARG A CB  1 
ATOM   767  C  CB  B ARG A 1 101 ? -61.949 24.845 -2.304  0.43 54.00  ? 101 ARG A CB  1 
ATOM   768  C  CG  A ARG A 1 101 ? -62.180 25.154 -0.850  0.57 55.25  ? 101 ARG A CG  1 
ATOM   769  C  CG  B ARG A 1 101 ? -63.070 23.874 -1.966  0.43 54.83  ? 101 ARG A CG  1 
ATOM   770  C  CD  A ARG A 1 101 ? -63.400 26.030 -0.579  0.57 53.78  ? 101 ARG A CD  1 
ATOM   771  C  CD  B ARG A 1 101 ? -64.189 24.601 -1.251  0.43 55.88  ? 101 ARG A CD  1 
ATOM   772  N  NE  A ARG A 1 101 ? -63.139 27.442 -0.837  0.57 53.33  ? 101 ARG A NE  1 
ATOM   773  N  NE  B ARG A 1 101 ? -63.652 25.680 -0.432  0.43 53.66  ? 101 ARG A NE  1 
ATOM   774  C  CZ  A ARG A 1 101 ? -64.079 28.364 -1.007  0.57 48.95  ? 101 ARG A CZ  1 
ATOM   775  C  CZ  B ARG A 1 101 ? -63.237 25.543 0.820   0.43 50.77  ? 101 ARG A CZ  1 
ATOM   776  N  NH1 A ARG A 1 101 ? -65.366 28.058 -0.975  0.57 44.30  ? 101 ARG A NH1 1 
ATOM   777  N  NH1 B ARG A 1 101 ? -63.320 24.383 1.453   0.43 51.40  ? 101 ARG A NH1 1 
ATOM   778  N  NH2 A ARG A 1 101 ? -63.717 29.624 -1.219  0.57 44.41  ? 101 ARG A NH2 1 
ATOM   779  N  NH2 B ARG A 1 101 ? -62.723 26.595 1.450   0.43 45.61  ? 101 ARG A NH2 1 
ATOM   780  N  N   . GLY A 1 102 ? -59.423 24.360 -4.784  1.00 65.43  ? 102 GLY A N   1 
ATOM   781  C  CA  . GLY A 1 102 ? -59.217 24.223 -6.209  1.00 55.12  ? 102 GLY A CA  1 
ATOM   782  C  C   . GLY A 1 102 ? -57.881 24.802 -6.627  1.00 56.97  ? 102 GLY A C   1 
ATOM   783  O  O   . GLY A 1 102 ? -56.871 24.596 -5.948  1.00 66.17  ? 102 GLY A O   1 
ATOM   784  N  N   . GLU A 1 103 ? -57.867 25.545 -7.729  1.00 53.71  ? 103 GLU A N   1 
ATOM   785  C  CA  A GLU A 1 103 ? -56.630 26.132 -8.224  0.57 56.94  ? 103 GLU A CA  1 
ATOM   786  C  CA  B GLU A 1 103 ? -56.627 26.127 -8.220  0.43 56.91  ? 103 GLU A CA  1 
ATOM   787  C  C   . GLU A 1 103 ? -56.002 27.035 -7.166  1.00 53.65  ? 103 GLU A C   1 
ATOM   788  O  O   . GLU A 1 103 ? -56.695 27.704 -6.393  1.00 56.03  ? 103 GLU A O   1 
ATOM   789  C  CB  A GLU A 1 103 ? -56.890 26.933 -9.506  0.57 55.13  ? 103 GLU A CB  1 
ATOM   790  C  CB  B GLU A 1 103 ? -56.885 26.905 -9.516  0.43 55.14  ? 103 GLU A CB  1 
ATOM   791  C  CG  A GLU A 1 103 ? -57.389 26.112 -10.696 0.57 58.83  ? 103 GLU A CG  1 
ATOM   792  C  CG  B GLU A 1 103 ? -58.054 27.887 -9.447  0.43 55.16  ? 103 GLU A CG  1 
ATOM   793  C  CD  A GLU A 1 103 ? -56.310 25.235 -11.303 0.57 66.47  ? 103 GLU A CD  1 
ATOM   794  C  CD  B GLU A 1 103 ? -57.617 29.304 -9.124  0.43 58.08  ? 103 GLU A CD  1 
ATOM   795  O  OE1 A GLU A 1 103 ? -55.273 25.018 -10.635 0.57 69.36  ? 103 GLU A OE1 1 
ATOM   796  O  OE1 B GLU A 1 103 ? -56.655 29.788 -9.755  0.43 63.38  ? 103 GLU A OE1 1 
ATOM   797  O  OE2 A GLU A 1 103 ? -56.498 24.771 -12.451 0.57 65.63  ? 103 GLU A OE2 1 
ATOM   798  O  OE2 B GLU A 1 103 ? -58.234 29.935 -8.238  0.43 57.97  ? 103 GLU A OE2 1 
ATOM   799  N  N   . VAL A 1 104 ? -54.673 27.046 -7.138  1.00 45.75  ? 104 VAL A N   1 
ATOM   800  C  CA  . VAL A 1 104 ? -53.912 27.918 -6.248  1.00 49.16  ? 104 VAL A CA  1 
ATOM   801  C  C   . VAL A 1 104 ? -53.850 29.305 -6.870  1.00 44.38  ? 104 VAL A C   1 
ATOM   802  O  O   . VAL A 1 104 ? -53.372 29.455 -8.001  1.00 53.61  ? 104 VAL A O   1 
ATOM   803  C  CB  . VAL A 1 104 ? -52.504 27.367 -5.992  1.00 48.71  ? 104 VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 104 ? -51.590 28.474 -5.502  1.00 47.06  ? 104 VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 104 ? -52.574 26.243 -4.977  1.00 55.10  ? 104 VAL A CG2 1 
ATOM   806  N  N   . PRO A 1 105 ? -54.334 30.336 -6.187  1.00 44.41  ? 105 PRO A N   1 
ATOM   807  C  CA  . PRO A 1 105 ? -54.348 31.672 -6.790  1.00 38.28  ? 105 PRO A CA  1 
ATOM   808  C  C   . PRO A 1 105 ? -53.001 32.371 -6.672  1.00 41.28  ? 105 PRO A C   1 
ATOM   809  O  O   . PRO A 1 105 ? -52.326 32.303 -5.641  1.00 35.79  ? 105 PRO A O   1 
ATOM   810  C  CB  . PRO A 1 105 ? -55.426 32.403 -5.981  1.00 42.51  ? 105 PRO A CB  1 
ATOM   811  C  CG  . PRO A 1 105 ? -55.373 31.726 -4.611  1.00 40.96  ? 105 PRO A CG  1 
ATOM   812  C  CD  . PRO A 1 105 ? -55.045 30.286 -4.892  1.00 42.07  ? 105 PRO A CD  1 
ATOM   813  N  N   . ASP A 1 106 ? -52.604 33.022 -7.762  1.00 39.14  ? 106 ASP A N   1 
ATOM   814  C  CA  A ASP A 1 106 ? -51.430 33.880 -7.734  0.59 38.59  ? 106 ASP A CA  1 
ATOM   815  C  CA  B ASP A 1 106 ? -51.425 33.871 -7.723  0.41 38.58  ? 106 ASP A CA  1 
ATOM   816  C  C   . ASP A 1 106 ? -51.593 34.915 -6.625  1.00 38.06  ? 106 ASP A C   1 
ATOM   817  O  O   . ASP A 1 106 ? -52.685 35.480 -6.464  1.00 39.96  ? 106 ASP A O   1 
ATOM   818  C  CB  A ASP A 1 106 ? -51.256 34.565 -9.101  0.59 35.30  ? 106 ASP A CB  1 
ATOM   819  C  CB  B ASP A 1 106 ? -51.208 34.559 -9.076  0.41 35.41  ? 106 ASP A CB  1 
ATOM   820  C  CG  A ASP A 1 106 ? -49.891 35.234 -9.269  0.59 39.87  ? 106 ASP A CG  1 
ATOM   821  C  CG  B ASP A 1 106 ? -50.913 33.577 -10.195 0.41 37.25  ? 106 ASP A CG  1 
ATOM   822  O  OD1 A ASP A 1 106 ? -48.861 34.531 -9.208  0.59 43.79  ? 106 ASP A OD1 1 
ATOM   823  O  OD1 B ASP A 1 106 ? -50.879 32.356 -9.932  0.41 40.70  ? 106 ASP A OD1 1 
ATOM   824  O  OD2 A ASP A 1 106 ? -49.846 36.465 -9.484  0.59 43.28  ? 106 ASP A OD2 1 
ATOM   825  O  OD2 B ASP A 1 106 ? -50.712 34.024 -11.341 0.41 43.56  ? 106 ASP A OD2 1 
ATOM   826  N  N   . PRO A 1 107 ? -50.557 35.197 -5.840  1.00 37.18  ? 107 PRO A N   1 
ATOM   827  C  CA  . PRO A 1 107 ? -49.241 34.556 -5.936  1.00 35.71  ? 107 PRO A CA  1 
ATOM   828  C  C   . PRO A 1 107 ? -48.980 33.505 -4.860  1.00 35.83  ? 107 PRO A C   1 
ATOM   829  O  O   . PRO A 1 107 ? -47.825 33.337 -4.472  1.00 38.37  ? 107 PRO A O   1 
ATOM   830  C  CB  . PRO A 1 107 ? -48.290 35.745 -5.763  1.00 35.43  ? 107 PRO A CB  1 
ATOM   831  C  CG  . PRO A 1 107 ? -49.008 36.583 -4.700  1.00 33.80  ? 107 PRO A CG  1 
ATOM   832  C  CD  . PRO A 1 107 ? -50.502 36.426 -5.023  1.00 35.90  ? 107 PRO A CD  1 
ATOM   833  N  N   . MET A 1 108 ? -50.006 32.804 -4.361  1.00 33.24  ? 108 MET A N   1 
ATOM   834  C  CA  . MET A 1 108 ? -49.752 31.736 -3.391  1.00 32.16  ? 108 MET A CA  1 
ATOM   835  C  C   . MET A 1 108 ? -48.780 30.696 -3.934  1.00 42.79  ? 108 MET A C   1 
ATOM   836  O  O   . MET A 1 108 ? -48.150 29.969 -3.152  1.00 38.19  ? 108 MET A O   1 
ATOM   837  C  CB  . MET A 1 108 ? -51.053 31.035 -2.992  1.00 33.44  ? 108 MET A CB  1 
ATOM   838  C  CG  . MET A 1 108 ? -52.074 31.903 -2.260  1.00 33.77  ? 108 MET A CG  1 
ATOM   839  S  SD  . MET A 1 108 ? -51.707 32.065 -0.513  1.00 49.46  ? 108 MET A SD  1 
ATOM   840  C  CE  . MET A 1 108 ? -52.262 30.480 0.119   1.00 36.37  ? 108 MET A CE  1 
ATOM   841  N  N   . ASN A 1 109 ? -48.655 30.601 -5.258  1.00 30.48  ? 109 ASN A N   1 
ATOM   842  C  CA  . ASN A 1 109 ? -47.743 29.645 -5.866  1.00 34.74  ? 109 ASN A CA  1 
ATOM   843  C  C   . ASN A 1 109 ? -46.289 29.963 -5.562  1.00 34.69  ? 109 ASN A C   1 
ATOM   844  O  O   . ASN A 1 109 ? -45.432 29.103 -5.784  1.00 42.13  ? 109 ASN A O   1 
ATOM   845  C  CB  . ASN A 1 109 ? -47.973 29.603 -7.378  1.00 39.27  ? 109 ASN A CB  1 
ATOM   846  C  CG  . ASN A 1 109 ? -47.790 30.973 -8.026  1.00 47.23  ? 109 ASN A CG  1 
ATOM   847  O  OD1 . ASN A 1 109 ? -48.630 31.864 -7.879  1.00 47.39  ? 109 ASN A OD1 1 
ATOM   848  N  ND2 . ASN A 1 109 ? -46.685 31.149 -8.730  1.00 50.12  ? 109 ASN A ND2 1 
ATOM   849  N  N   . LEU A 1 110 ? -45.987 31.167 -5.059  1.00 33.68  ? 110 LEU A N   1 
ATOM   850  C  CA  . LEU A 1 110 ? -44.631 31.452 -4.592  1.00 33.92  ? 110 LEU A CA  1 
ATOM   851  C  C   . LEU A 1 110 ? -44.218 30.519 -3.462  1.00 44.17  ? 110 LEU A C   1 
ATOM   852  O  O   . LEU A 1 110 ? -43.024 30.244 -3.297  1.00 43.86  ? 110 LEU A O   1 
ATOM   853  C  CB  . LEU A 1 110 ? -44.499 32.904 -4.110  1.00 38.97  ? 110 LEU A CB  1 
ATOM   854  C  CG  . LEU A 1 110 ? -44.517 34.065 -5.116  1.00 46.16  ? 110 LEU A CG  1 
ATOM   855  C  CD1 . LEU A 1 110 ? -44.285 35.393 -4.404  1.00 38.15  ? 110 LEU A CD1 1 
ATOM   856  C  CD2 . LEU A 1 110 ? -43.483 33.862 -6.189  1.00 36.69  ? 110 LEU A CD2 1 
ATOM   857  N  N   . LEU A 1 111 ? -45.181 30.049 -2.659  1.00 36.84  ? 111 LEU A N   1 
ATOM   858  C  CA  . LEU A 1 111 ? -44.898 29.226 -1.485  1.00 37.34  ? 111 LEU A CA  1 
ATOM   859  C  C   . LEU A 1 111 ? -44.830 27.740 -1.816  1.00 42.86  ? 111 LEU A C   1 
ATOM   860  O  O   . LEU A 1 111 ? -43.959 27.031 -1.299  1.00 38.03  ? 111 LEU A O   1 
ATOM   861  C  CB  . LEU A 1 111 ? -45.965 29.444 -0.409  1.00 31.47  ? 111 LEU A CB  1 
ATOM   862  C  CG  . LEU A 1 111 ? -46.306 30.891 -0.091  1.00 29.40  ? 111 LEU A CG  1 
ATOM   863  C  CD1 . LEU A 1 111 ? -47.325 30.948 1.031   1.00 22.99  ? 111 LEU A CD1 1 
ATOM   864  C  CD2 . LEU A 1 111 ? -45.048 31.640 0.275   1.00 27.62  ? 111 LEU A CD2 1 
ATOM   865  N  N   . GLY A 1 112 ? -45.730 27.263 -2.669  1.00 41.05  ? 112 GLY A N   1 
ATOM   866  C  CA  . GLY A 1 112 ? -45.792 25.856 -3.001  1.00 41.56  ? 112 GLY A CA  1 
ATOM   867  C  C   . GLY A 1 112 ? -47.028 25.573 -3.829  1.00 42.15  ? 112 GLY A C   1 
ATOM   868  O  O   . GLY A 1 112 ? -47.737 26.491 -4.248  1.00 43.15  ? 112 GLY A O   1 
ATOM   869  N  N   . GLU A 1 113 ? -47.275 24.288 -4.060  1.00 47.95  ? 113 GLU A N   1 
ATOM   870  C  CA  A GLU A 1 113 ? -48.386 23.865 -4.900  0.49 47.30  ? 113 GLU A CA  1 
ATOM   871  C  CA  B GLU A 1 113 ? -48.383 23.857 -4.901  0.51 47.29  ? 113 GLU A CA  1 
ATOM   872  C  C   . GLU A 1 113 ? -49.573 23.457 -4.038  1.00 41.36  ? 113 GLU A C   1 
ATOM   873  O  O   . GLU A 1 113 ? -49.471 23.327 -2.820  1.00 50.90  ? 113 GLU A O   1 
ATOM   874  C  CB  A GLU A 1 113 ? -47.953 22.720 -5.821  0.49 50.26  ? 113 GLU A CB  1 
ATOM   875  C  CB  B GLU A 1 113 ? -47.958 22.699 -5.814  0.51 50.26  ? 113 GLU A CB  1 
ATOM   876  C  CG  A GLU A 1 113 ? -46.676 23.021 -6.584  0.49 51.94  ? 113 GLU A CG  1 
ATOM   877  C  CG  B GLU A 1 113 ? -48.944 22.414 -6.934  0.51 50.60  ? 113 GLU A CG  1 
ATOM   878  C  CD  A GLU A 1 113 ? -46.004 21.772 -7.103  0.49 58.72  ? 113 GLU A CD  1 
ATOM   879  C  CD  B GLU A 1 113 ? -49.395 23.683 -7.629  0.51 52.02  ? 113 GLU A CD  1 
ATOM   880  O  OE1 A GLU A 1 113 ? -46.586 21.101 -7.980  0.49 55.90  ? 113 GLU A OE1 1 
ATOM   881  O  OE1 B GLU A 1 113 ? -48.526 24.526 -7.936  0.51 59.99  ? 113 GLU A OE1 1 
ATOM   882  O  OE2 A GLU A 1 113 ? -44.895 21.458 -6.620  0.49 56.10  ? 113 GLU A OE2 1 
ATOM   883  O  OE2 B GLU A 1 113 ? -50.614 23.847 -7.852  0.51 45.73  ? 113 GLU A OE2 1 
ATOM   884  N  N   . GLN A 1 114 ? -50.719 23.268 -4.694  1.00 45.57  ? 114 GLN A N   1 
ATOM   885  C  CA  . GLN A 1 114 ? -51.954 22.960 -3.981  1.00 47.13  ? 114 GLN A CA  1 
ATOM   886  C  C   . GLN A 1 114 ? -51.748 21.947 -2.858  1.00 48.70  ? 114 GLN A C   1 
ATOM   887  O  O   . GLN A 1 114 ? -52.250 22.124 -1.742  1.00 47.19  ? 114 GLN A O   1 
ATOM   888  C  CB  . GLN A 1 114 ? -52.995 22.445 -4.969  1.00 48.21  ? 114 GLN A CB  1 
ATOM   889  C  CG  . GLN A 1 114 ? -54.365 22.230 -4.357  1.00 62.39  ? 114 GLN A CG  1 
ATOM   890  C  CD  . GLN A 1 114 ? -54.984 20.918 -4.779  1.00 72.93  ? 114 GLN A CD  1 
ATOM   891  O  OE1 . GLN A 1 114 ? -55.694 20.848 -5.785  1.00 70.51  ? 114 GLN A OE1 1 
ATOM   892  N  NE2 . GLN A 1 114 ? -54.715 19.863 -4.011  1.00 74.73  ? 114 GLN A NE2 1 
ATOM   893  N  N   . GLN A 1 115 ? -51.008 20.872 -3.139  1.00 44.64  ? 115 GLN A N   1 
ATOM   894  C  CA  . GLN A 1 115 ? -50.895 19.773 -2.191  1.00 45.99  ? 115 GLN A CA  1 
ATOM   895  C  C   . GLN A 1 115 ? -50.111 20.154 -0.940  1.00 39.91  ? 115 GLN A C   1 
ATOM   896  O  O   . GLN A 1 115 ? -50.194 19.443 0.065   1.00 41.38  ? 115 GLN A O   1 
ATOM   897  C  CB  . GLN A 1 115 ? -50.242 18.561 -2.860  1.00 45.05  ? 115 GLN A CB  1 
ATOM   898  C  CG  . GLN A 1 115 ? -48.751 18.725 -3.147  1.00 52.86  ? 115 GLN A CG  1 
ATOM   899  C  CD  . GLN A 1 115 ? -48.463 19.159 -4.573  1.00 58.67  ? 115 GLN A CD  1 
ATOM   900  O  OE1 . GLN A 1 115 ? -49.312 19.761 -5.238  1.00 59.11  ? 115 GLN A OE1 1 
ATOM   901  N  NE2 . GLN A 1 115 ? -47.264 18.844 -5.056  1.00 62.31  ? 115 GLN A NE2 1 
ATOM   902  N  N   . HIS A 1 116 ? -49.350 21.245 -0.976  1.00 37.34  ? 116 HIS A N   1 
ATOM   903  C  CA  . HIS A 1 116 ? -48.549 21.646 0.169   1.00 43.88  ? 116 HIS A CA  1 
ATOM   904  C  C   . HIS A 1 116 ? -49.339 22.456 1.194   1.00 42.80  ? 116 HIS A C   1 
ATOM   905  O  O   . HIS A 1 116 ? -48.859 22.635 2.320   1.00 33.26  ? 116 HIS A O   1 
ATOM   906  C  CB  . HIS A 1 116 ? -47.327 22.439 -0.303  1.00 42.16  ? 116 HIS A CB  1 
ATOM   907  C  CG  . HIS A 1 116 ? -46.366 21.638 -1.127  1.00 49.24  ? 116 HIS A CG  1 
ATOM   908  N  ND1 . HIS A 1 116 ? -46.101 21.919 -2.451  1.00 61.15  ? 116 HIS A ND1 1 
ATOM   909  C  CD2 . HIS A 1 116 ? -45.618 20.552 -0.819  1.00 53.20  ? 116 HIS A CD2 1 
ATOM   910  C  CE1 . HIS A 1 116 ? -45.226 21.046 -2.919  1.00 65.35  ? 116 HIS A CE1 1 
ATOM   911  N  NE2 . HIS A 1 116 ? -44.919 20.204 -1.949  1.00 60.24  ? 116 HIS A NE2 1 
ATOM   912  N  N   . PHE A 1 117 ? -50.542 22.923 0.854   1.00 35.56  ? 117 PHE A N   1 
ATOM   913  C  CA  . PHE A 1 117 ? -51.318 23.766 1.766   1.00 43.37  ? 117 PHE A CA  1 
ATOM   914  C  C   . PHE A 1 117 ? -52.188 22.890 2.664   1.00 41.45  ? 117 PHE A C   1 
ATOM   915  O  O   . PHE A 1 117 ? -53.404 22.769 2.492   1.00 43.34  ? 117 PHE A O   1 
ATOM   916  C  CB  . PHE A 1 117 ? -52.144 24.774 0.982   1.00 34.41  ? 117 PHE A CB  1 
ATOM   917  C  CG  . PHE A 1 117 ? -51.311 25.797 0.280   1.00 38.12  ? 117 PHE A CG  1 
ATOM   918  C  CD1 . PHE A 1 117 ? -50.794 26.874 0.979   1.00 24.02  ? 117 PHE A CD1 1 
ATOM   919  C  CD2 . PHE A 1 117 ? -51.034 25.679 -1.079  1.00 39.57  ? 117 PHE A CD2 1 
ATOM   920  C  CE1 . PHE A 1 117 ? -50.013 27.827 0.344   1.00 26.71  ? 117 PHE A CE1 1 
ATOM   921  C  CE2 . PHE A 1 117 ? -50.252 26.624 -1.722  1.00 37.66  ? 117 PHE A CE2 1 
ATOM   922  C  CZ  . PHE A 1 117 ? -49.741 27.703 -1.010  1.00 35.94  ? 117 PHE A CZ  1 
ATOM   923  N  N   . ILE A 1 118 ? -51.543 22.302 3.671   1.00 28.77  ? 118 ILE A N   1 
ATOM   924  C  CA  . ILE A 1 118 ? -52.211 21.365 4.568   1.00 31.63  ? 118 ILE A CA  1 
ATOM   925  C  C   . ILE A 1 118 ? -52.222 21.876 6.005   1.00 34.41  ? 118 ILE A C   1 
ATOM   926  O  O   . ILE A 1 118 ? -52.117 21.083 6.944   1.00 36.64  ? 118 ILE A O   1 
ATOM   927  C  CB  . ILE A 1 118 ? -51.533 19.985 4.503   1.00 35.47  ? 118 ILE A CB  1 
ATOM   928  C  CG1 . ILE A 1 118 ? -50.052 20.109 4.876   1.00 31.30  ? 118 ILE A CG1 1 
ATOM   929  C  CG2 . ILE A 1 118 ? -51.689 19.377 3.126   1.00 28.98  ? 118 ILE A CG2 1 
ATOM   930  C  CD1 . ILE A 1 118 ? -49.350 18.761 4.991   1.00 30.85  ? 118 ILE A CD1 1 
ATOM   931  N  N   . TYR A 1 119 ? -52.350 23.190 6.198   1.00 30.26  ? 119 TYR A N   1 
ATOM   932  C  CA  . TYR A 1 119 ? -52.286 23.810 7.527   1.00 25.19  ? 119 TYR A CA  1 
ATOM   933  C  C   . TYR A 1 119 ? -53.497 24.713 7.699   1.00 28.92  ? 119 TYR A C   1 
ATOM   934  O  O   . TYR A 1 119 ? -53.382 25.946 7.635   1.00 33.19  ? 119 TYR A O   1 
ATOM   935  C  CB  . TYR A 1 119 ? -50.989 24.602 7.721   1.00 22.52  ? 119 TYR A CB  1 
ATOM   936  C  CG  . TYR A 1 119 ? -49.781 23.853 7.229   1.00 29.81  ? 119 TYR A CG  1 
ATOM   937  C  CD1 . TYR A 1 119 ? -49.289 22.766 7.935   1.00 24.23  ? 119 TYR A CD1 1 
ATOM   938  C  CD2 . TYR A 1 119 ? -49.149 24.209 6.041   1.00 27.35  ? 119 TYR A CD2 1 
ATOM   939  C  CE1 . TYR A 1 119 ? -48.208 22.065 7.490   1.00 27.06  ? 119 TYR A CE1 1 
ATOM   940  C  CE2 . TYR A 1 119 ? -48.042 23.512 5.593   1.00 30.45  ? 119 TYR A CE2 1 
ATOM   941  C  CZ  . TYR A 1 119 ? -47.580 22.432 6.323   1.00 33.24  ? 119 TYR A CZ  1 
ATOM   942  O  OH  . TYR A 1 119 ? -46.499 21.692 5.899   1.00 33.39  ? 119 TYR A OH  1 
ATOM   943  N  N   . PRO A 1 120 ? -54.674 24.129 7.951   1.00 32.70  ? 120 PRO A N   1 
ATOM   944  C  CA  . PRO A 1 120 ? -55.908 24.930 7.988   1.00 28.58  ? 120 PRO A CA  1 
ATOM   945  C  C   . PRO A 1 120 ? -56.038 25.817 9.220   1.00 34.37  ? 120 PRO A C   1 
ATOM   946  O  O   . PRO A 1 120 ? -56.926 26.681 9.237   1.00 34.27  ? 120 PRO A O   1 
ATOM   947  C  CB  . PRO A 1 120 ? -57.018 23.868 7.940   1.00 32.00  ? 120 PRO A CB  1 
ATOM   948  C  CG  . PRO A 1 120 ? -56.400 22.637 8.509   1.00 32.32  ? 120 PRO A CG  1 
ATOM   949  C  CD  . PRO A 1 120 ? -54.907 22.706 8.265   1.00 27.85  ? 120 PRO A CD  1 
ATOM   950  N  N   . THR A 1 121 ? -55.195 25.637 10.242  1.00 29.17  ? 121 THR A N   1 
ATOM   951  C  CA  . THR A 1 121 ? -55.130 26.545 11.384  1.00 30.13  ? 121 THR A CA  1 
ATOM   952  C  C   . THR A 1 121 ? -53.680 26.903 11.664  1.00 27.90  ? 121 THR A C   1 
ATOM   953  O  O   . THR A 1 121 ? -52.754 26.193 11.258  1.00 25.41  ? 121 THR A O   1 
ATOM   954  C  CB  . THR A 1 121 ? -55.725 25.943 12.665  1.00 26.05  ? 121 THR A CB  1 
ATOM   955  O  OG1 . THR A 1 121 ? -54.986 24.768 13.014  1.00 30.88  ? 121 THR A OG1 1 
ATOM   956  C  CG2 . THR A 1 121 ? -57.195 25.576 12.481  1.00 27.22  ? 121 THR A CG2 1 
ATOM   957  N  N   . VAL A 1 122 ? -53.504 28.017 12.378  1.00 25.67  ? 122 VAL A N   1 
ATOM   958  C  CA  . VAL A 1 122 ? -52.191 28.377 12.901  1.00 26.80  ? 122 VAL A CA  1 
ATOM   959  C  C   . VAL A 1 122 ? -51.661 27.263 13.793  1.00 33.04  ? 122 VAL A C   1 
ATOM   960  O  O   . VAL A 1 122 ? -50.479 26.903 13.736  1.00 29.03  ? 122 VAL A O   1 
ATOM   961  C  CB  . VAL A 1 122 ? -52.269 29.718 13.652  1.00 25.84  ? 122 VAL A CB  1 
ATOM   962  C  CG1 . VAL A 1 122 ? -50.990 29.955 14.438  1.00 25.73  ? 122 VAL A CG1 1 
ATOM   963  C  CG2 . VAL A 1 122 ? -52.516 30.863 12.674  1.00 23.51  ? 122 VAL A CG2 1 
ATOM   964  N  N   . GLU A 1 123 ? -52.534 26.674 14.609  1.00 28.85  ? 123 GLU A N   1 
ATOM   965  C  CA  . GLU A 1 123 ? -52.112 25.567 15.458  1.00 32.81  ? 123 GLU A CA  1 
ATOM   966  C  C   . GLU A 1 123 ? -51.514 24.435 14.623  1.00 29.74  ? 123 GLU A C   1 
ATOM   967  O  O   . GLU A 1 123 ? -50.439 23.916 14.939  1.00 25.81  ? 123 GLU A O   1 
ATOM   968  C  CB  . GLU A 1 123 ? -53.297 25.072 16.289  1.00 29.24  ? 123 GLU A CB  1 
ATOM   969  C  CG  . GLU A 1 123 ? -52.921 24.198 17.478  1.00 39.83  ? 123 GLU A CG  1 
ATOM   970  C  CD  . GLU A 1 123 ? -52.397 25.004 18.668  1.00 59.85  ? 123 GLU A CD  1 
ATOM   971  O  OE1 . GLU A 1 123 ? -52.884 26.137 18.897  1.00 64.81  ? 123 GLU A OE1 1 
ATOM   972  O  OE2 . GLU A 1 123 ? -51.496 24.506 19.379  1.00 60.12  ? 123 GLU A OE2 1 
ATOM   973  N  N   . ALA A 1 124 ? -52.211 24.028 13.558  1.00 23.94  ? 124 ALA A N   1 
ATOM   974  C  CA  . ALA A 1 124 ? -51.704 22.960 12.694  1.00 29.02  ? 124 ALA A CA  1 
ATOM   975  C  C   . ALA A 1 124 ? -50.369 23.335 12.064  1.00 27.36  ? 124 ALA A C   1 
ATOM   976  O  O   . ALA A 1 124 ? -49.472 22.491 11.947  1.00 29.91  ? 124 ALA A O   1 
ATOM   977  C  CB  . ALA A 1 124 ? -52.726 22.625 11.603  1.00 22.73  ? 124 ALA A CB  1 
ATOM   978  N  N   . TYR A 1 125 ? -50.222 24.597 11.647  1.00 25.28  ? 125 TYR A N   1 
ATOM   979  C  CA  . TYR A 1 125 ? -48.949 25.067 11.104  1.00 26.93  ? 125 TYR A CA  1 
ATOM   980  C  C   . TYR A 1 125 ? -47.842 25.040 12.158  1.00 30.51  ? 125 TYR A C   1 
ATOM   981  O  O   . TYR A 1 125 ? -46.716 24.608 11.880  1.00 23.81  ? 125 TYR A O   1 
ATOM   982  C  CB  . TYR A 1 125 ? -49.113 26.481 10.537  1.00 25.04  ? 125 TYR A CB  1 
ATOM   983  C  CG  . TYR A 1 125 ? -47.843 27.014 9.912   1.00 25.75  ? 125 TYR A CG  1 
ATOM   984  C  CD1 . TYR A 1 125 ? -47.389 26.524 8.696   1.00 24.63  ? 125 TYR A CD1 1 
ATOM   985  C  CD2 . TYR A 1 125 ? -47.080 27.977 10.555  1.00 25.09  ? 125 TYR A CD2 1 
ATOM   986  C  CE1 . TYR A 1 125 ? -46.224 26.994 8.121   1.00 19.57  ? 125 TYR A CE1 1 
ATOM   987  C  CE2 . TYR A 1 125 ? -45.899 28.454 9.992   1.00 25.77  ? 125 TYR A CE2 1 
ATOM   988  C  CZ  . TYR A 1 125 ? -45.480 27.954 8.776   1.00 29.66  ? 125 TYR A CZ  1 
ATOM   989  O  OH  . TYR A 1 125 ? -44.318 28.403 8.194   1.00 25.74  ? 125 TYR A OH  1 
ATOM   990  N  N   . ALA A 1 126 ? -48.149 25.502 13.374  1.00 23.34  ? 126 ALA A N   1 
ATOM   991  C  CA  . ALA A 1 126 ? -47.163 25.525 14.450  1.00 25.22  ? 126 ALA A CA  1 
ATOM   992  C  C   . ALA A 1 126 ? -46.601 24.133 14.720  1.00 28.75  ? 126 ALA A C   1 
ATOM   993  O  O   . ALA A 1 126 ? -45.382 23.944 14.816  1.00 28.56  ? 126 ALA A O   1 
ATOM   994  C  CB  . ALA A 1 126 ? -47.796 26.101 15.718  1.00 24.85  ? 126 ALA A CB  1 
ATOM   995  N  N   . HIS A 1 127 ? -47.476 23.140 14.851  1.00 24.79  ? 127 HIS A N   1 
ATOM   996  C  CA  . HIS A 1 127 ? -46.984 21.802 15.148  1.00 26.92  ? 127 HIS A CA  1 
ATOM   997  C  C   . HIS A 1 127 ? -46.240 21.204 13.971  1.00 28.05  ? 127 HIS A C   1 
ATOM   998  O  O   . HIS A 1 127 ? -45.295 20.432 14.174  1.00 28.48  ? 127 HIS A O   1 
ATOM   999  C  CB  . HIS A 1 127 ? -48.146 20.912 15.577  1.00 33.39  ? 127 HIS A CB  1 
ATOM   1000 C  CG  . HIS A 1 127 ? -48.864 21.439 16.776  1.00 31.19  ? 127 HIS A CG  1 
ATOM   1001 N  ND1 . HIS A 1 127 ? -48.199 22.005 17.844  1.00 27.93  ? 127 HIS A ND1 1 
ATOM   1002 C  CD2 . HIS A 1 127 ? -50.184 21.543 17.055  1.00 25.75  ? 127 HIS A CD2 1 
ATOM   1003 C  CE1 . HIS A 1 127 ? -49.079 22.412 18.739  1.00 29.05  ? 127 HIS A CE1 1 
ATOM   1004 N  NE2 . HIS A 1 127 ? -50.290 22.140 18.287  1.00 31.86  ? 127 HIS A NE2 1 
ATOM   1005 N  N   . ALA A 1 128 ? -46.633 21.558 12.740  1.00 26.73  ? 128 ALA A N   1 
ATOM   1006 C  CA  . ALA A 1 128 ? -45.897 21.078 11.576  1.00 26.28  ? 128 ALA A CA  1 
ATOM   1007 C  C   . ALA A 1 128 ? -44.492 21.665 11.548  1.00 27.43  ? 128 ALA A C   1 
ATOM   1008 O  O   . ALA A 1 128 ? -43.523 20.956 11.271  1.00 25.51  ? 128 ALA A O   1 
ATOM   1009 C  CB  . ALA A 1 128 ? -46.650 21.420 10.288  1.00 27.08  ? 128 ALA A CB  1 
ATOM   1010 N  N   . VAL A 1 129 ? -44.361 22.960 11.839  1.00 24.52  ? 129 VAL A N   1 
ATOM   1011 C  CA  . VAL A 1 129 ? -43.033 23.550 11.974  1.00 26.10  ? 129 VAL A CA  1 
ATOM   1012 C  C   . VAL A 1 129 ? -42.193 22.761 12.974  1.00 28.35  ? 129 VAL A C   1 
ATOM   1013 O  O   . VAL A 1 129 ? -41.081 22.323 12.669  1.00 26.40  ? 129 VAL A O   1 
ATOM   1014 C  CB  . VAL A 1 129 ? -43.138 25.029 12.384  1.00 25.47  ? 129 VAL A CB  1 
ATOM   1015 C  CG1 . VAL A 1 129 ? -41.774 25.526 12.848  1.00 22.46  ? 129 VAL A CG1 1 
ATOM   1016 C  CG2 . VAL A 1 129 ? -43.663 25.869 11.225  1.00 19.48  ? 129 VAL A CG2 1 
ATOM   1017 N  N   A GLU A 1 130 ? -42.712 22.561 14.183  0.52 26.14  ? 130 GLU A N   1 
ATOM   1018 N  N   B GLU A 1 130 ? -42.709 22.575 14.192  0.48 26.41  ? 130 GLU A N   1 
ATOM   1019 C  CA  A GLU A 1 130 ? -41.884 21.948 15.213  0.52 29.18  ? 130 GLU A CA  1 
ATOM   1020 C  CA  B GLU A 1 130 ? -41.895 21.935 15.220  0.48 29.17  ? 130 GLU A CA  1 
ATOM   1021 C  C   A GLU A 1 130 ? -41.622 20.473 14.926  0.52 29.93  ? 130 GLU A C   1 
ATOM   1022 C  C   B GLU A 1 130 ? -41.581 20.492 14.853  0.48 29.92  ? 130 GLU A C   1 
ATOM   1023 O  O   A GLU A 1 130 ? -40.581 19.948 15.330  0.52 30.15  ? 130 GLU A O   1 
ATOM   1024 O  O   B GLU A 1 130 ? -40.481 20.004 15.132  0.48 29.89  ? 130 GLU A O   1 
ATOM   1025 C  CB  A GLU A 1 130 ? -42.523 22.175 16.584  0.52 26.72  ? 130 GLU A CB  1 
ATOM   1026 C  CB  B GLU A 1 130 ? -42.575 22.027 16.591  0.48 26.68  ? 130 GLU A CB  1 
ATOM   1027 C  CG  A GLU A 1 130 ? -42.716 23.676 16.863  0.52 22.00  ? 130 GLU A CG  1 
ATOM   1028 C  CG  B GLU A 1 130 ? -43.957 21.405 16.738  0.48 30.46  ? 130 GLU A CG  1 
ATOM   1029 C  CD  A GLU A 1 130 ? -42.883 24.024 18.320  0.52 28.07  ? 130 GLU A CD  1 
ATOM   1030 C  CD  B GLU A 1 130 ? -44.687 21.927 17.985  0.48 29.25  ? 130 GLU A CD  1 
ATOM   1031 O  OE1 A GLU A 1 130 ? -43.605 23.278 19.017  0.52 35.22  ? 130 GLU A OE1 1 
ATOM   1032 O  OE1 B GLU A 1 130 ? -44.459 23.096 18.356  0.48 30.15  ? 130 GLU A OE1 1 
ATOM   1033 O  OE2 A GLU A 1 130 ? -42.302 25.052 18.768  0.52 21.39  ? 130 GLU A OE2 1 
ATOM   1034 O  OE2 B GLU A 1 130 ? -45.477 21.182 18.598  0.48 20.27  ? 130 GLU A OE2 1 
ATOM   1035 N  N   . ALA A 1 131 ? -42.519 19.800 14.200  1.00 28.29  ? 131 ALA A N   1 
ATOM   1036 C  CA  . ALA A 1 131 ? -42.235 18.434 13.767  1.00 30.14  ? 131 ALA A CA  1 
ATOM   1037 C  C   . ALA A 1 131 ? -41.059 18.388 12.807  1.00 30.62  ? 131 ALA A C   1 
ATOM   1038 O  O   . ALA A 1 131 ? -40.351 17.379 12.744  1.00 36.42  ? 131 ALA A O   1 
ATOM   1039 C  CB  . ALA A 1 131 ? -43.464 17.809 13.102  1.00 32.07  ? 131 ALA A CB  1 
ATOM   1040 N  N   . ALA A 1 132 ? -40.842 19.462 12.044  1.00 27.58  ? 132 ALA A N   1 
ATOM   1041 C  CA  . ALA A 1 132 ? -39.736 19.503 11.100  1.00 30.01  ? 132 ALA A CA  1 
ATOM   1042 C  C   . ALA A 1 132 ? -38.403 19.820 11.769  1.00 36.16  ? 132 ALA A C   1 
ATOM   1043 O  O   . ALA A 1 132 ? -37.349 19.582 11.158  1.00 25.94  ? 132 ALA A O   1 
ATOM   1044 C  CB  . ALA A 1 132 ? -40.028 20.521 9.996   1.00 27.07  ? 132 ALA A CB  1 
ATOM   1045 N  N   A ARG A 1 133 ? -38.422 20.349 12.999  0.54 31.67  ? 133 ARG A N   1 
ATOM   1046 N  N   B ARG A 1 133 ? -38.423 20.338 13.003  0.46 31.67  ? 133 ARG A N   1 
ATOM   1047 C  CA  A ARG A 1 133 ? -37.209 20.643 13.757  0.54 29.13  ? 133 ARG A CA  1 
ATOM   1048 C  CA  B ARG A 1 133 ? -37.212 20.648 13.758  0.46 29.08  ? 133 ARG A CA  1 
ATOM   1049 C  C   A ARG A 1 133 ? -36.320 21.627 12.998  0.54 31.64  ? 133 ARG A C   1 
ATOM   1050 C  C   B ARG A 1 133 ? -36.328 21.621 12.983  0.46 31.62  ? 133 ARG A C   1 
ATOM   1051 O  O   A ARG A 1 133 ? -35.172 21.306 12.661  0.54 30.77  ? 133 ARG A O   1 
ATOM   1052 O  O   B ARG A 1 133 ? -35.193 21.286 12.619  0.46 30.77  ? 133 ARG A O   1 
ATOM   1053 C  CB  A ARG A 1 133 ? -36.459 19.344 14.070  0.54 34.81  ? 133 ARG A CB  1 
ATOM   1054 C  CB  B ARG A 1 133 ? -36.452 19.363 14.094  0.46 34.80  ? 133 ARG A CB  1 
ATOM   1055 C  CG  A ARG A 1 133 ? -37.343 18.260 14.713  0.54 36.02  ? 133 ARG A CG  1 
ATOM   1056 C  CG  B ARG A 1 133 ? -37.256 18.390 14.968  0.46 35.53  ? 133 ARG A CG  1 
ATOM   1057 C  CD  A ARG A 1 133 ? -36.537 17.061 15.214  0.54 39.93  ? 133 ARG A CD  1 
ATOM   1058 C  CD  B ARG A 1 133 ? -36.441 17.174 15.406  0.46 39.75  ? 133 ARG A CD  1 
ATOM   1059 N  NE  A ARG A 1 133 ? -35.583 16.543 14.234  0.54 49.73  ? 133 ARG A NE  1 
ATOM   1060 N  NE  B ARG A 1 133 ? -35.910 16.398 14.288  0.46 49.10  ? 133 ARG A NE  1 
ATOM   1061 C  CZ  A ARG A 1 133 ? -35.807 15.511 13.427  0.54 54.92  ? 133 ARG A CZ  1 
ATOM   1062 C  CZ  B ARG A 1 133 ? -34.620 16.152 14.081  0.46 48.55  ? 133 ARG A CZ  1 
ATOM   1063 N  NH1 A ARG A 1 133 ? -36.960 14.858 13.443  0.54 44.89  ? 133 ARG A NH1 1 
ATOM   1064 N  NH1 B ARG A 1 133 ? -33.689 16.577 14.923  0.46 29.25  ? 133 ARG A NH1 1 
ATOM   1065 N  NH2 A ARG A 1 133 ? -34.849 15.125 12.583  0.54 55.56  ? 133 ARG A NH2 1 
ATOM   1066 N  NH2 B ARG A 1 133 ? -34.255 15.457 13.004  0.46 53.58  ? 133 ARG A NH2 1 
ATOM   1067 N  N   . PRO A 1 134 ? -36.806 22.833 12.715  1.00 29.43  ? 134 PRO A N   1 
ATOM   1068 C  CA  . PRO A 1 134 ? -36.016 23.774 11.920  1.00 30.32  ? 134 PRO A CA  1 
ATOM   1069 C  C   . PRO A 1 134 ? -34.844 24.311 12.725  1.00 31.21  ? 134 PRO A C   1 
ATOM   1070 O  O   . PRO A 1 134 ? -34.809 24.224 13.954  1.00 25.62  ? 134 PRO A O   1 
ATOM   1071 C  CB  . PRO A 1 134 ? -37.019 24.878 11.586  1.00 23.80  ? 134 PRO A CB  1 
ATOM   1072 C  CG  . PRO A 1 134 ? -37.940 24.879 12.794  1.00 29.58  ? 134 PRO A CG  1 
ATOM   1073 C  CD  . PRO A 1 134 ? -38.063 23.432 13.198  1.00 26.15  ? 134 PRO A CD  1 
ATOM   1074 N  N   . SER A 1 135 ? -33.870 24.866 12.003  1.00 26.30  ? 135 SER A N   1 
ATOM   1075 C  CA  . SER A 1 135 ? -32.660 25.409 12.610  1.00 26.69  ? 135 SER A CA  1 
ATOM   1076 C  C   . SER A 1 135 ? -32.815 26.848 13.068  1.00 25.99  ? 135 SER A C   1 
ATOM   1077 O  O   . SER A 1 135 ? -31.944 27.347 13.782  1.00 33.66  ? 135 SER A O   1 
ATOM   1078 C  CB  . SER A 1 135 ? -31.485 25.327 11.633  1.00 28.29  ? 135 SER A CB  1 
ATOM   1079 O  OG  . SER A 1 135 ? -31.229 23.986 11.288  1.00 28.20  ? 135 SER A OG  1 
ATOM   1080 N  N   . LEU A 1 136 ? -33.881 27.529 12.659  1.00 22.46  ? 136 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 136 ? -34.197 28.864 13.148  1.00 24.99  ? 136 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 136 ? -35.667 28.917 13.523  1.00 26.28  ? 136 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 136 ? -36.451 28.029 13.172  1.00 24.91  ? 136 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 136 ? -33.867 29.946 12.107  1.00 23.92  ? 136 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 136 ? -33.954 29.525 10.645  1.00 24.24  ? 136 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 136 ? -35.404 29.250 10.251  1.00 22.80  ? 136 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 136 ? -33.319 30.566 9.757   1.00 25.65  ? 136 LEU A CD2 1 
ATOM   1088 N  N   . ASN A 1 137 ? -36.043 29.982 14.220  1.00 21.62  ? 137 ASN A N   1 
ATOM   1089 C  CA  . ASN A 1 137 ? -37.421 30.124 14.661  1.00 23.29  ? 137 ASN A CA  1 
ATOM   1090 C  C   . ASN A 1 137 ? -38.318 30.620 13.522  1.00 26.40  ? 137 ASN A C   1 
ATOM   1091 O  O   . ASN A 1 137 ? -37.860 31.236 12.554  1.00 24.04  ? 137 ASN A O   1 
ATOM   1092 C  CB  . ASN A 1 137 ? -37.516 31.092 15.841  1.00 21.24  ? 137 ASN A CB  1 
ATOM   1093 C  CG  . ASN A 1 137 ? -36.599 30.722 16.980  1.00 26.52  ? 137 ASN A CG  1 
ATOM   1094 O  OD1 . ASN A 1 137 ? -36.755 29.671 17.598  1.00 25.98  ? 137 ASN A OD1 1 
ATOM   1095 N  ND2 . ASN A 1 137 ? -35.646 31.602 17.285  1.00 23.57  ? 137 ASN A ND2 1 
ATOM   1096 N  N   . VAL A 1 138 ? -39.621 30.369 13.672  1.00 23.74  ? 138 VAL A N   1 
ATOM   1097 C  CA  . VAL A 1 138 ? -40.638 30.738 12.696  1.00 23.35  ? 138 VAL A CA  1 
ATOM   1098 C  C   . VAL A 1 138 ? -41.811 31.378 13.426  1.00 24.26  ? 138 VAL A C   1 
ATOM   1099 O  O   . VAL A 1 138 ? -42.363 30.778 14.352  1.00 24.13  ? 138 VAL A O   1 
ATOM   1100 C  CB  . VAL A 1 138 ? -41.135 29.516 11.902  1.00 24.04  ? 138 VAL A CB  1 
ATOM   1101 C  CG1 . VAL A 1 138 ? -42.285 29.914 10.968  1.00 21.10  ? 138 VAL A CG1 1 
ATOM   1102 C  CG2 . VAL A 1 138 ? -40.004 28.863 11.143  1.00 20.92  ? 138 VAL A CG2 1 
ATOM   1103 N  N   . GLY A 1 139 ? -42.203 32.579 12.992  1.00 24.70  ? 139 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 139 ? -43.504 33.147 13.313  1.00 20.26  ? 139 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 139 ? -44.273 33.505 12.051  1.00 24.40  ? 139 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 139 ? -43.662 33.752 11.005  1.00 22.29  ? 139 GLY A O   1 
ATOM   1107 N  N   . THR A 1 140 ? -45.603 33.554 12.112  1.00 21.36  ? 140 THR A N   1 
ATOM   1108 C  CA  . THR A 1 140 ? -46.375 33.735 10.890  1.00 22.76  ? 140 THR A CA  1 
ATOM   1109 C  C   . THR A 1 140 ? -47.367 34.882 11.003  1.00 23.32  ? 140 THR A C   1 
ATOM   1110 O  O   . THR A 1 140 ? -48.057 35.035 12.017  1.00 22.61  ? 140 THR A O   1 
ATOM   1111 C  CB  . THR A 1 140 ? -47.142 32.461 10.529  1.00 22.61  ? 140 THR A CB  1 
ATOM   1112 O  OG1 . THR A 1 140 ? -47.736 32.614 9.232   1.00 20.43  ? 140 THR A OG1 1 
ATOM   1113 C  CG2 . THR A 1 140 ? -48.265 32.181 11.582  1.00 21.75  ? 140 THR A CG2 1 
ATOM   1114 N  N   . LEU A 1 141 ? -47.426 35.690 9.959   1.00 23.67  ? 141 LEU A N   1 
ATOM   1115 C  CA  . LEU A 1 141 ? -48.595 36.514 9.705   1.00 21.97  ? 141 LEU A CA  1 
ATOM   1116 C  C   . LEU A 1 141 ? -49.662 35.682 8.995   1.00 23.45  ? 141 LEU A C   1 
ATOM   1117 O  O   . LEU A 1 141 ? -49.394 34.595 8.478   1.00 25.30  ? 141 LEU A O   1 
ATOM   1118 C  CB  . LEU A 1 141 ? -48.211 37.725 8.859   1.00 20.89  ? 141 LEU A CB  1 
ATOM   1119 C  CG  . LEU A 1 141 ? -47.172 38.654 9.502   1.00 23.63  ? 141 LEU A CG  1 
ATOM   1120 C  CD1 . LEU A 1 141 ? -46.357 39.340 8.428   1.00 25.05  ? 141 LEU A CD1 1 
ATOM   1121 C  CD2 . LEU A 1 141 ? -47.860 39.688 10.418  1.00 20.50  ? 141 LEU A CD2 1 
ATOM   1122 N  N   . ILE A 1 142 ? -50.881 36.206 8.957   1.00 22.48  ? 142 ILE A N   1 
ATOM   1123 C  CA  . ILE A 1 142 ? -51.980 35.581 8.230   1.00 23.79  ? 142 ILE A CA  1 
ATOM   1124 C  C   . ILE A 1 142 ? -52.184 36.339 6.923   1.00 22.58  ? 142 ILE A C   1 
ATOM   1125 O  O   . ILE A 1 142 ? -52.283 37.572 6.924   1.00 26.96  ? 142 ILE A O   1 
ATOM   1126 C  CB  . ILE A 1 142 ? -53.269 35.557 9.073   1.00 31.09  ? 142 ILE A CB  1 
ATOM   1127 C  CG1 . ILE A 1 142 ? -53.051 34.717 10.331  1.00 27.12  ? 142 ILE A CG1 1 
ATOM   1128 C  CG2 . ILE A 1 142 ? -54.438 34.973 8.256   1.00 22.05  ? 142 ILE A CG2 1 
ATOM   1129 C  CD1 . ILE A 1 142 ? -52.500 33.314 10.037  1.00 23.58  ? 142 ILE A CD1 1 
ATOM   1130 N  N   . GLY A 1 143 ? -52.221 35.609 5.806   1.00 28.35  ? 143 GLY A N   1 
ATOM   1131 C  CA  . GLY A 1 143 ? -52.325 36.222 4.486   1.00 24.91  ? 143 GLY A CA  1 
ATOM   1132 C  C   . GLY A 1 143 ? -53.731 36.649 4.114   1.00 25.90  ? 143 GLY A C   1 
ATOM   1133 O  O   . GLY A 1 143 ? -54.639 35.814 4.047   1.00 26.75  ? 143 GLY A O   1 
ATOM   1134 N  N   . HIS A 1 144 ? -53.930 37.945 3.861   1.00 22.79  ? 144 HIS A N   1 
ATOM   1135 C  CA  . HIS A 1 144 ? -55.265 38.435 3.514   1.00 26.32  ? 144 HIS A CA  1 
ATOM   1136 C  C   . HIS A 1 144 ? -55.848 37.671 2.330   1.00 26.50  ? 144 HIS A C   1 
ATOM   1137 O  O   . HIS A 1 144 ? -57.001 37.225 2.368   1.00 27.42  ? 144 HIS A O   1 
ATOM   1138 C  CB  . HIS A 1 144 ? -55.221 39.932 3.206   1.00 24.55  ? 144 HIS A CB  1 
ATOM   1139 C  CG  . HIS A 1 144 ? -56.492 40.463 2.607   1.00 33.10  ? 144 HIS A CG  1 
ATOM   1140 N  ND1 . HIS A 1 144 ? -56.507 41.417 1.611   1.00 24.19  ? 144 HIS A ND1 1 
ATOM   1141 C  CD2 . HIS A 1 144 ? -57.792 40.181 2.875   1.00 27.33  ? 144 HIS A CD2 1 
ATOM   1142 C  CE1 . HIS A 1 144 ? -57.758 41.699 1.291   1.00 25.95  ? 144 HIS A CE1 1 
ATOM   1143 N  NE2 . HIS A 1 144 ? -58.557 40.962 2.042   1.00 31.87  ? 144 HIS A NE2 1 
ATOM   1144 N  N   . THR A 1 145 ? -55.058 37.505 1.266   1.00 24.49  ? 145 THR A N   1 
ATOM   1145 C  CA  . THR A 1 145 ? -55.534 36.793 0.087   1.00 24.65  ? 145 THR A CA  1 
ATOM   1146 C  C   . THR A 1 145 ? -55.837 35.329 0.382   1.00 29.86  ? 145 THR A C   1 
ATOM   1147 O  O   . THR A 1 145 ? -56.781 34.758 -0.185  1.00 28.46  ? 145 THR A O   1 
ATOM   1148 C  CB  . THR A 1 145 ? -54.501 36.911 -1.028  1.00 32.44  ? 145 THR A CB  1 
ATOM   1149 O  OG1 . THR A 1 145 ? -54.086 38.282 -1.131  1.00 27.49  ? 145 THR A OG1 1 
ATOM   1150 C  CG2 . THR A 1 145 ? -55.101 36.436 -2.357  1.00 24.08  ? 145 THR A CG2 1 
ATOM   1151 N  N   . ALA A 1 146 ? -55.053 34.696 1.253   1.00 28.26  ? 146 ALA A N   1 
ATOM   1152 C  CA  . ALA A 1 146 ? -55.391 33.337 1.664   1.00 30.51  ? 146 ALA A CA  1 
ATOM   1153 C  C   . ALA A 1 146 ? -56.742 33.294 2.376   1.00 31.34  ? 146 ALA A C   1 
ATOM   1154 O  O   . ALA A 1 146 ? -57.549 32.394 2.125   1.00 31.21  ? 146 ALA A O   1 
ATOM   1155 C  CB  . ALA A 1 146 ? -54.289 32.762 2.553   1.00 26.34  ? 146 ALA A CB  1 
ATOM   1156 N  N   . LEU A 1 147 ? -57.015 34.271 3.252   1.00 28.74  ? 147 LEU A N   1 
ATOM   1157 C  CA  . LEU A 1 147 ? -58.340 34.382 3.869   1.00 24.28  ? 147 LEU A CA  1 
ATOM   1158 C  C   . LEU A 1 147 ? -59.425 34.611 2.822   1.00 28.33  ? 147 LEU A C   1 
ATOM   1159 O  O   . LEU A 1 147 ? -60.481 33.969 2.863   1.00 28.87  ? 147 LEU A O   1 
ATOM   1160 C  CB  . LEU A 1 147 ? -58.371 35.521 4.891   1.00 24.83  ? 147 LEU A CB  1 
ATOM   1161 C  CG  . LEU A 1 147 ? -57.577 35.403 6.184   1.00 34.31  ? 147 LEU A CG  1 
ATOM   1162 C  CD1 . LEU A 1 147 ? -57.817 36.638 7.038   1.00 28.35  ? 147 LEU A CD1 1 
ATOM   1163 C  CD2 . LEU A 1 147 ? -57.943 34.133 6.941   1.00 29.49  ? 147 LEU A CD2 1 
ATOM   1164 N  N   . ARG A 1 148 ? -59.211 35.577 1.917   1.00 28.95  ? 148 ARG A N   1 
ATOM   1165 C  CA  . ARG A 1 148 ? -60.147 35.780 0.810   1.00 27.36  ? 148 ARG A CA  1 
ATOM   1166 C  C   . ARG A 1 148 ? -60.467 34.454 0.151   1.00 28.71  ? 148 ARG A C   1 
ATOM   1167 O  O   . ARG A 1 148 ? -61.636 34.096 -0.024  1.00 32.28  ? 148 ARG A O   1 
ATOM   1168 C  CB  . ARG A 1 148 ? -59.571 36.746 -0.234  1.00 29.34  ? 148 ARG A CB  1 
ATOM   1169 C  CG  . ARG A 1 148 ? -59.425 38.191 0.244   1.00 33.94  ? 148 ARG A CG  1 
ATOM   1170 C  CD  . ARG A 1 148 ? -59.116 39.158 -0.918  1.00 22.68  ? 148 ARG A CD  1 
ATOM   1171 N  NE  . ARG A 1 148 ? -60.259 40.027 -1.186  1.00 35.57  ? 148 ARG A NE  1 
ATOM   1172 C  CZ  . ARG A 1 148 ? -60.925 40.069 -2.331  1.00 36.81  ? 148 ARG A CZ  1 
ATOM   1173 N  NH1 . ARG A 1 148 ? -60.534 39.367 -3.384  1.00 30.33  ? 148 ARG A NH1 1 
ATOM   1174 N  NH2 . ARG A 1 148 ? -62.003 40.849 -2.428  1.00 31.92  ? 148 ARG A NH2 1 
ATOM   1175 N  N   . ASN A 1 149 ? -59.423 33.688 -0.177  1.00 32.12  ? 149 ASN A N   1 
ATOM   1176 C  CA  . ASN A 1 149 ? -59.608 32.452 -0.928  1.00 31.35  ? 149 ASN A CA  1 
ATOM   1177 C  C   . ASN A 1 149 ? -60.376 31.409 -0.125  1.00 33.76  ? 149 ASN A C   1 
ATOM   1178 O  O   . ASN A 1 149 ? -61.121 30.606 -0.705  1.00 33.84  ? 149 ASN A O   1 
ATOM   1179 C  CB  . ASN A 1 149 ? -58.254 31.900 -1.355  1.00 30.53  ? 149 ASN A CB  1 
ATOM   1180 C  CG  . ASN A 1 149 ? -58.378 30.806 -2.382  1.00 38.78  ? 149 ASN A CG  1 
ATOM   1181 O  OD1 . ASN A 1 149 ? -58.946 31.015 -3.461  1.00 37.34  ? 149 ASN A OD1 1 
ATOM   1182 N  ND2 . ASN A 1 149 ? -57.829 29.638 -2.071  1.00 28.56  ? 149 ASN A ND2 1 
ATOM   1183 N  N   . ASN A 1 150 ? -60.201 31.395 1.199   1.00 28.69  ? 150 ASN A N   1 
ATOM   1184 C  CA  . ASN A 1 150 ? -60.970 30.474 2.036   1.00 32.39  ? 150 ASN A CA  1 
ATOM   1185 C  C   . ASN A 1 150 ? -62.455 30.787 2.000   1.00 32.75  ? 150 ASN A C   1 
ATOM   1186 O  O   . ASN A 1 150 ? -63.273 29.898 2.244   1.00 30.82  ? 150 ASN A O   1 
ATOM   1187 C  CB  . ASN A 1 150 ? -60.512 30.527 3.496   1.00 29.88  ? 150 ASN A CB  1 
ATOM   1188 C  CG  . ASN A 1 150 ? -59.113 30.009 3.696   1.00 31.64  ? 150 ASN A CG  1 
ATOM   1189 O  OD1 . ASN A 1 150 ? -58.574 29.275 2.870   1.00 29.83  ? 150 ASN A OD1 1 
ATOM   1190 N  ND2 . ASN A 1 150 ? -58.516 30.389 4.807   1.00 27.51  ? 150 ASN A ND2 1 
ATOM   1191 N  N   . HIS A 1 151 ? -62.830 32.037 1.721   1.00 31.95  ? 151 HIS A N   1 
ATOM   1192 C  CA  . HIS A 1 151 ? -64.196 32.467 1.967   1.00 30.99  ? 151 HIS A CA  1 
ATOM   1193 C  C   . HIS A 1 151 ? -64.962 32.928 0.735   1.00 32.68  ? 151 HIS A C   1 
ATOM   1194 O  O   . HIS A 1 151 ? -66.185 33.094 0.814   1.00 35.41  ? 151 HIS A O   1 
ATOM   1195 C  CB  . HIS A 1 151 ? -64.199 33.583 3.021   1.00 28.70  ? 151 HIS A CB  1 
ATOM   1196 C  CG  . HIS A 1 151 ? -63.885 33.094 4.396   1.00 31.29  ? 151 HIS A CG  1 
ATOM   1197 N  ND1 . HIS A 1 151 ? -64.858 32.672 5.273   1.00 31.15  ? 151 HIS A ND1 1 
ATOM   1198 C  CD2 . HIS A 1 151 ? -62.703 32.924 5.034   1.00 28.50  ? 151 HIS A CD2 1 
ATOM   1199 C  CE1 . HIS A 1 151 ? -64.292 32.281 6.399   1.00 28.21  ? 151 HIS A CE1 1 
ATOM   1200 N  NE2 . HIS A 1 151 ? -62.986 32.418 6.278   1.00 29.51  ? 151 HIS A NE2 1 
ATOM   1201 N  N   . MET A 1 152 ? -64.302 33.122 -0.390  1.00 36.49  ? 152 MET A N   1 
ATOM   1202 C  CA  . MET A 1 152 ? -64.922 33.678 -1.578  1.00 31.04  ? 152 MET A CA  1 
ATOM   1203 C  C   . MET A 1 152 ? -64.898 32.650 -2.702  1.00 37.67  ? 152 MET A C   1 
ATOM   1204 O  O   . MET A 1 152 ? -63.896 31.958 -2.896  1.00 33.93  ? 152 MET A O   1 
ATOM   1205 C  CB  . MET A 1 152 ? -64.174 34.942 -2.018  1.00 28.04  ? 152 MET A CB  1 
ATOM   1206 C  CG  . MET A 1 152 ? -64.178 36.067 -1.019  1.00 28.59  ? 152 MET A CG  1 
ATOM   1207 S  SD  . MET A 1 152 ? -63.229 37.436 -1.654  1.00 33.60  ? 152 MET A SD  1 
ATOM   1208 C  CE  . MET A 1 152 ? -64.396 38.060 -2.933  1.00 33.42  ? 152 MET A CE  1 
ATOM   1209 N  N   . ASP A 1 153 ? -66.002 32.555 -3.451  1.00 43.24  ? 153 ASP A N   1 
ATOM   1210 C  CA  . ASP A 1 153 ? -66.027 31.681 -4.625  1.00 44.34  ? 153 ASP A CA  1 
ATOM   1211 C  C   . ASP A 1 153 ? -65.171 32.225 -5.770  1.00 43.02  ? 153 ASP A C   1 
ATOM   1212 O  O   . ASP A 1 153 ? -64.652 31.450 -6.585  1.00 41.54  ? 153 ASP A O   1 
ATOM   1213 C  CB  . ASP A 1 153 ? -67.468 31.467 -5.078  1.00 52.56  ? 153 ASP A CB  1 
ATOM   1214 C  CG  . ASP A 1 153 ? -68.164 30.404 -4.268  1.00 64.30  ? 153 ASP A CG  1 
ATOM   1215 O  OD1 . ASP A 1 153 ? -67.475 29.446 -3.848  1.00 70.31  ? 153 ASP A OD1 1 
ATOM   1216 O  OD2 . ASP A 1 153 ? -69.389 30.523 -4.046  1.00 71.62  ? 153 ASP A OD2 1 
ATOM   1217 N  N   . ASP A 1 154 ? -65.017 33.538 -5.862  1.00 37.01  ? 154 ASP A N   1 
ATOM   1218 C  CA  A ASP A 1 154 ? -64.095 34.132 -6.818  0.76 39.93  ? 154 ASP A CA  1 
ATOM   1219 C  CA  B ASP A 1 154 ? -64.116 34.150 -6.828  0.24 39.95  ? 154 ASP A CA  1 
ATOM   1220 C  C   . ASP A 1 154 ? -63.469 35.374 -6.197  1.00 35.02  ? 154 ASP A C   1 
ATOM   1221 O  O   . ASP A 1 154 ? -64.112 36.099 -5.436  1.00 33.30  ? 154 ASP A O   1 
ATOM   1222 C  CB  A ASP A 1 154 ? -64.789 34.473 -8.154  0.76 42.09  ? 154 ASP A CB  1 
ATOM   1223 C  CB  B ASP A 1 154 ? -64.853 34.528 -8.124  0.24 42.07  ? 154 ASP A CB  1 
ATOM   1224 C  CG  A ASP A 1 154 ? -65.987 35.375 -7.976  0.76 44.89  ? 154 ASP A CG  1 
ATOM   1225 C  CG  B ASP A 1 154 ? -66.305 34.900 -7.883  0.24 44.44  ? 154 ASP A CG  1 
ATOM   1226 O  OD1 A ASP A 1 154 ? -66.828 35.092 -7.090  0.76 48.00  ? 154 ASP A OD1 1 
ATOM   1227 O  OD1 B ASP A 1 154 ? -66.554 35.898 -7.172  0.24 44.95  ? 154 ASP A OD1 1 
ATOM   1228 O  OD2 A ASP A 1 154 ? -66.086 36.373 -8.722  0.76 42.24  ? 154 ASP A OD2 1 
ATOM   1229 O  OD2 B ASP A 1 154 ? -67.197 34.198 -8.405  0.24 46.09  ? 154 ASP A OD2 1 
ATOM   1230 N  N   . LEU A 1 155 ? -62.201 35.599 -6.528  1.00 37.70  ? 155 LEU A N   1 
ATOM   1231 C  CA  . LEU A 1 155 ? -61.386 36.620 -5.890  1.00 31.11  ? 155 LEU A CA  1 
ATOM   1232 C  C   . LEU A 1 155 ? -61.446 37.993 -6.550  1.00 38.53  ? 155 LEU A C   1 
ATOM   1233 O  O   . LEU A 1 155 ? -61.027 38.978 -5.927  1.00 30.09  ? 155 LEU A O   1 
ATOM   1234 C  CB  . LEU A 1 155 ? -59.935 36.147 -5.871  1.00 26.77  ? 155 LEU A CB  1 
ATOM   1235 C  CG  . LEU A 1 155 ? -59.740 34.873 -5.054  1.00 38.50  ? 155 LEU A CG  1 
ATOM   1236 C  CD1 . LEU A 1 155 ? -58.372 34.278 -5.313  1.00 35.09  ? 155 LEU A CD1 1 
ATOM   1237 C  CD2 . LEU A 1 155 ? -59.929 35.189 -3.571  1.00 29.32  ? 155 LEU A CD2 1 
ATOM   1238 N  N   . PHE A 1 156 ? -61.957 38.094 -7.776  1.00 33.43  ? 156 PHE A N   1 
ATOM   1239 C  CA  . PHE A 1 156 ? -61.757 39.290 -8.599  1.00 40.47  ? 156 PHE A CA  1 
ATOM   1240 C  C   . PHE A 1 156 ? -62.908 40.275 -8.490  1.00 36.92  ? 156 PHE A C   1 
ATOM   1241 O  O   . PHE A 1 156 ? -63.359 40.866 -9.475  1.00 30.06  ? 156 PHE A O   1 
ATOM   1242 C  CB  . PHE A 1 156 ? -61.497 38.868 -10.035 1.00 31.24  ? 156 PHE A CB  1 
ATOM   1243 C  CG  . PHE A 1 156 ? -60.342 37.926 -10.134 1.00 39.74  ? 156 PHE A CG  1 
ATOM   1244 C  CD1 . PHE A 1 156 ? -59.051 38.383 -9.912  1.00 31.14  ? 156 PHE A CD1 1 
ATOM   1245 C  CD2 . PHE A 1 156 ? -60.541 36.582 -10.371 1.00 31.64  ? 156 PHE A CD2 1 
ATOM   1246 C  CE1 . PHE A 1 156 ? -57.987 37.526 -9.967  1.00 36.00  ? 156 PHE A CE1 1 
ATOM   1247 C  CE2 . PHE A 1 156 ? -59.471 35.721 -10.431 1.00 34.82  ? 156 PHE A CE2 1 
ATOM   1248 C  CZ  . PHE A 1 156 ? -58.197 36.191 -10.226 1.00 34.04  ? 156 PHE A CZ  1 
ATOM   1249 N  N   . ARG A 1 157 ? -63.359 40.490 -7.261  1.00 34.25  ? 157 ARG A N   1 
ATOM   1250 C  CA  . ARG A 1 157 ? -64.464 41.383 -6.965  1.00 28.69  ? 157 ARG A CA  1 
ATOM   1251 C  C   . ARG A 1 157 ? -64.356 41.787 -5.511  1.00 33.35  ? 157 ARG A C   1 
ATOM   1252 O  O   . ARG A 1 157 ? -63.614 41.158 -4.747  1.00 35.00  ? 157 ARG A O   1 
ATOM   1253 C  CB  . ARG A 1 157 ? -65.801 40.693 -7.214  1.00 30.03  ? 157 ARG A CB  1 
ATOM   1254 C  CG  . ARG A 1 157 ? -65.899 39.361 -6.510  1.00 31.65  ? 157 ARG A CG  1 
ATOM   1255 C  CD  . ARG A 1 157 ? -67.347 38.904 -6.435  1.00 35.65  ? 157 ARG A CD  1 
ATOM   1256 N  NE  . ARG A 1 157 ? -67.460 37.578 -5.838  1.00 39.09  ? 157 ARG A NE  1 
ATOM   1257 C  CZ  . ARG A 1 157 ? -67.663 37.342 -4.549  1.00 38.59  ? 157 ARG A CZ  1 
ATOM   1258 N  NH1 . ARG A 1 157 ? -67.824 38.330 -3.680  1.00 29.92  ? 157 ARG A NH1 1 
ATOM   1259 N  NH2 . ARG A 1 157 ? -67.687 36.081 -4.118  1.00 32.55  ? 157 ARG A NH2 1 
ATOM   1260 N  N   . PRO A 1 158 ? -65.072 42.831 -5.097  1.00 31.85  ? 158 PRO A N   1 
ATOM   1261 C  CA  . PRO A 1 158 ? -65.183 43.102 -3.663  1.00 30.13  ? 158 PRO A CA  1 
ATOM   1262 C  C   . PRO A 1 158 ? -65.873 41.925 -2.997  1.00 33.13  ? 158 PRO A C   1 
ATOM   1263 O  O   . PRO A 1 158 ? -66.689 41.235 -3.610  1.00 32.27  ? 158 PRO A O   1 
ATOM   1264 C  CB  . PRO A 1 158 ? -66.033 44.379 -3.598  1.00 32.34  ? 158 PRO A CB  1 
ATOM   1265 C  CG  . PRO A 1 158 ? -65.914 45.004 -4.995  1.00 30.30  ? 158 PRO A CG  1 
ATOM   1266 C  CD  . PRO A 1 158 ? -65.761 43.842 -5.925  1.00 31.35  ? 158 PRO A CD  1 
ATOM   1267 N  N   . ALA A 1 159 ? -65.499 41.666 -1.751  1.00 27.45  ? 159 ALA A N   1 
ATOM   1268 C  CA  . ALA A 1 159 ? -66.171 40.634 -0.970  1.00 33.53  ? 159 ALA A CA  1 
ATOM   1269 C  C   . ALA A 1 159 ? -67.476 41.176 -0.400  1.00 26.51  ? 159 ALA A C   1 
ATOM   1270 O  O   . ALA A 1 159 ? -67.617 42.379 -0.176  1.00 32.18  ? 159 ALA A O   1 
ATOM   1271 C  CB  . ALA A 1 159 ? -65.265 40.146 0.161   1.00 30.08  ? 159 ALA A CB  1 
ATOM   1272 N  N   . ASN A 1 160 ? -68.439 40.283 -0.173  1.00 28.35  ? 160 ASN A N   1 
ATOM   1273 C  CA  . ASN A 1 160 ? -69.687 40.690 0.467   1.00 31.89  ? 160 ASN A CA  1 
ATOM   1274 C  C   . ASN A 1 160 ? -69.553 40.596 1.989   1.00 30.94  ? 160 ASN A C   1 
ATOM   1275 O  O   . ASN A 1 160 ? -68.541 40.131 2.521   1.00 32.89  ? 160 ASN A O   1 
ATOM   1276 C  CB  . ASN A 1 160 ? -70.872 39.871 -0.058  1.00 28.19  ? 160 ASN A CB  1 
ATOM   1277 C  CG  . ASN A 1 160 ? -70.789 38.406 0.299   1.00 37.33  ? 160 ASN A CG  1 
ATOM   1278 O  OD1 . ASN A 1 160 ? -70.466 38.027 1.436   1.00 34.43  ? 160 ASN A OD1 1 
ATOM   1279 N  ND2 . ASN A 1 160 ? -71.102 37.564 -0.674  1.00 28.68  ? 160 ASN A ND2 1 
ATOM   1280 N  N   A GLU A 1 161 ? -70.588 41.078 2.688   0.51 31.12  ? 161 GLU A N   1 
ATOM   1281 N  N   B GLU A 1 161 ? -70.598 41.008 2.708   0.49 31.13  ? 161 GLU A N   1 
ATOM   1282 C  CA  A GLU A 1 161 ? -70.540 41.123 4.149   0.51 32.25  ? 161 GLU A CA  1 
ATOM   1283 C  CA  B GLU A 1 161 ? -70.471 41.143 4.158   0.49 32.23  ? 161 GLU A CA  1 
ATOM   1284 C  C   A GLU A 1 161 ? -70.292 39.741 4.731   0.51 32.93  ? 161 GLU A C   1 
ATOM   1285 C  C   B GLU A 1 161 ? -70.474 39.796 4.882   0.49 32.81  ? 161 GLU A C   1 
ATOM   1286 O  O   A GLU A 1 161 ? -69.406 39.556 5.576   0.51 31.32  ? 161 GLU A O   1 
ATOM   1287 O  O   B GLU A 1 161 ? -69.901 39.692 5.971   0.49 31.14  ? 161 GLU A O   1 
ATOM   1288 C  CB  A GLU A 1 161 ? -71.842 41.690 4.720   0.51 31.13  ? 161 GLU A CB  1 
ATOM   1289 C  CB  B GLU A 1 161 ? -71.570 42.068 4.691   0.49 32.20  ? 161 GLU A CB  1 
ATOM   1290 C  CG  A GLU A 1 161 ? -72.098 41.197 6.145   0.51 37.19  ? 161 GLU A CG  1 
ATOM   1291 C  CG  B GLU A 1 161 ? -71.331 43.540 4.309   0.49 31.81  ? 161 GLU A CG  1 
ATOM   1292 C  CD  A GLU A 1 161 ? -73.289 41.852 6.822   0.51 38.50  ? 161 GLU A CD  1 
ATOM   1293 C  CD  B GLU A 1 161 ? -72.431 44.486 4.769   0.49 37.72  ? 161 GLU A CD  1 
ATOM   1294 O  OE1 A GLU A 1 161 ? -73.913 42.745 6.217   0.51 42.17  ? 161 GLU A OE1 1 
ATOM   1295 O  OE1 B GLU A 1 161 ? -73.179 44.145 5.714   0.49 40.51  ? 161 GLU A OE1 1 
ATOM   1296 O  OE2 A GLU A 1 161 ? -73.594 41.467 7.968   0.51 37.88  ? 161 GLU A OE2 1 
ATOM   1297 O  OE2 B GLU A 1 161 ? -72.539 45.581 4.182   0.49 35.76  ? 161 GLU A OE2 1 
ATOM   1298 N  N   . THR A 1 162 ? -71.085 38.759 4.297   1.00 32.99  ? 162 THR A N   1 
ATOM   1299 C  CA  . THR A 1 162 ? -70.975 37.412 4.855   1.00 29.27  ? 162 THR A CA  1 
ATOM   1300 C  C   . THR A 1 162 ? -69.563 36.861 4.704   1.00 32.45  ? 162 THR A C   1 
ATOM   1301 O  O   . THR A 1 162 ? -69.037 36.228 5.623   1.00 31.29  ? 162 THR A O   1 
ATOM   1302 C  CB  . THR A 1 162 ? -71.967 36.472 4.168   1.00 34.30  ? 162 THR A CB  1 
ATOM   1303 O  OG1 . THR A 1 162 ? -73.305 36.898 4.431   1.00 37.51  ? 162 THR A OG1 1 
ATOM   1304 C  CG2 . THR A 1 162 ? -71.796 35.073 4.692   1.00 33.85  ? 162 THR A CG2 1 
ATOM   1305 N  N   . GLU A 1 163 ? -68.945 37.072 3.539   1.00 34.32  ? 163 GLU A N   1 
ATOM   1306 C  CA  . GLU A 1 163 ? -67.565 36.644 3.340   1.00 28.71  ? 163 GLU A CA  1 
ATOM   1307 C  C   . GLU A 1 163 ? -66.623 37.380 4.281   1.00 25.92  ? 163 GLU A C   1 
ATOM   1308 O  O   . GLU A 1 163 ? -65.702 36.782 4.846   1.00 29.05  ? 163 GLU A O   1 
ATOM   1309 C  CB  . GLU A 1 163 ? -67.161 36.866 1.880   1.00 30.91  ? 163 GLU A CB  1 
ATOM   1310 C  CG  . GLU A 1 163 ? -68.044 36.100 0.885   1.00 37.51  ? 163 GLU A CG  1 
ATOM   1311 C  CD  . GLU A 1 163 ? -67.909 36.567 -0.562  1.00 40.27  ? 163 GLU A CD  1 
ATOM   1312 O  OE1 . GLU A 1 163 ? -67.642 37.768 -0.802  1.00 36.55  ? 163 GLU A OE1 1 
ATOM   1313 O  OE2 . GLU A 1 163 ? -68.085 35.722 -1.465  1.00 40.73  ? 163 GLU A OE2 1 
ATOM   1314 N  N   . ILE A 1 164 ? -66.838 38.680 4.469   1.00 30.46  ? 164 ILE A N   1 
ATOM   1315 C  CA  . ILE A 1 164 ? -65.933 39.445 5.317   1.00 31.14  ? 164 ILE A CA  1 
ATOM   1316 C  C   . ILE A 1 164 ? -66.119 39.063 6.784   1.00 26.69  ? 164 ILE A C   1 
ATOM   1317 O  O   . ILE A 1 164 ? -65.147 38.970 7.540   1.00 29.89  ? 164 ILE A O   1 
ATOM   1318 C  CB  . ILE A 1 164 ? -66.130 40.953 5.077   1.00 30.35  ? 164 ILE A CB  1 
ATOM   1319 C  CG1 . ILE A 1 164 ? -65.814 41.310 3.624   1.00 27.62  ? 164 ILE A CG1 1 
ATOM   1320 C  CG2 . ILE A 1 164 ? -65.245 41.766 6.013   1.00 23.44  ? 164 ILE A CG2 1 
ATOM   1321 C  CD1 . ILE A 1 164 ? -66.231 42.736 3.252   1.00 24.14  ? 164 ILE A CD1 1 
ATOM   1322 N  N   . ALA A 1 165 ? -67.360 38.808 7.208   1.00 28.58  ? 165 ALA A N   1 
ATOM   1323 C  CA  . ALA A 1 165 ? -67.582 38.403 8.599   1.00 26.64  ? 165 ALA A CA  1 
ATOM   1324 C  C   . ALA A 1 165 ? -66.880 37.087 8.900   1.00 29.32  ? 165 ALA A C   1 
ATOM   1325 O  O   . ALA A 1 165 ? -66.263 36.927 9.965   1.00 31.34  ? 165 ALA A O   1 
ATOM   1326 C  CB  . ALA A 1 165 ? -69.075 38.290 8.899   1.00 24.04  ? 165 ALA A CB  1 
ATOM   1327 N  N   . GLY A 1 166 ? -66.962 36.135 7.968   1.00 29.49  ? 166 GLY A N   1 
ATOM   1328 C  CA  . GLY A 1 166 ? -66.228 34.893 8.123   1.00 27.42  ? 166 GLY A CA  1 
ATOM   1329 C  C   . GLY A 1 166 ? -64.734 35.113 8.241   1.00 32.99  ? 166 GLY A C   1 
ATOM   1330 O  O   . GLY A 1 166 ? -64.074 34.520 9.100   1.00 28.06  ? 166 GLY A O   1 
ATOM   1331 N  N   . MET A 1 167 ? -64.175 35.987 7.397   1.00 26.50  ? 167 MET A N   1 
ATOM   1332 C  CA  A MET A 1 167 ? -62.741 36.251 7.450   0.80 28.13  ? 167 MET A CA  1 
ATOM   1333 C  CA  B MET A 1 167 ? -62.736 36.208 7.466   0.20 28.03  ? 167 MET A CA  1 
ATOM   1334 C  C   . MET A 1 167 ? -62.332 36.816 8.805   1.00 28.85  ? 167 MET A C   1 
ATOM   1335 O  O   . MET A 1 167 ? -61.288 36.449 9.356   1.00 27.93  ? 167 MET A O   1 
ATOM   1336 C  CB  A MET A 1 167 ? -62.350 37.207 6.326   0.80 26.45  ? 167 MET A CB  1 
ATOM   1337 C  CB  B MET A 1 167 ? -62.246 37.068 6.295   0.20 26.77  ? 167 MET A CB  1 
ATOM   1338 C  CG  A MET A 1 167 ? -62.483 36.590 4.927   0.80 30.63  ? 167 MET A CG  1 
ATOM   1339 C  CG  B MET A 1 167 ? -63.252 38.005 5.689   0.20 28.00  ? 167 MET A CG  1 
ATOM   1340 S  SD  A MET A 1 167 ? -61.647 37.556 3.653   0.80 31.65  ? 167 MET A SD  1 
ATOM   1341 S  SD  B MET A 1 167 ? -62.714 38.552 4.053   0.20 29.18  ? 167 MET A SD  1 
ATOM   1342 C  CE  A MET A 1 167 ? -62.872 38.787 3.279   0.80 27.62  ? 167 MET A CE  1 
ATOM   1343 C  CE  B MET A 1 167 ? -63.054 37.089 3.084   0.20 28.19  ? 167 MET A CE  1 
ATOM   1344 N  N   . ARG A 1 168 ? -63.151 37.722 9.360   1.00 26.19  ? 168 ARG A N   1 
ATOM   1345 C  CA  . ARG A 1 168 ? -62.864 38.265 10.687  1.00 25.70  ? 168 ARG A CA  1 
ATOM   1346 C  C   . ARG A 1 168 ? -62.751 37.153 11.721  1.00 23.54  ? 168 ARG A C   1 
ATOM   1347 O  O   . ARG A 1 168 ? -61.806 37.126 12.512  1.00 26.42  ? 168 ARG A O   1 
ATOM   1348 C  CB  . ARG A 1 168 ? -63.943 39.268 11.109  1.00 27.09  ? 168 ARG A CB  1 
ATOM   1349 C  CG  . ARG A 1 168 ? -63.766 40.667 10.526  1.00 24.05  ? 168 ARG A CG  1 
ATOM   1350 C  CD  . ARG A 1 168 ? -64.563 41.711 11.297  1.00 26.51  ? 168 ARG A CD  1 
ATOM   1351 N  NE  . ARG A 1 168 ? -64.005 41.945 12.621  1.00 24.80  ? 168 ARG A NE  1 
ATOM   1352 C  CZ  . ARG A 1 168 ? -64.135 43.078 13.294  1.00 27.14  ? 168 ARG A CZ  1 
ATOM   1353 N  NH1 . ARG A 1 168 ? -64.831 44.100 12.805  1.00 22.46  ? 168 ARG A NH1 1 
ATOM   1354 N  NH2 . ARG A 1 168 ? -63.554 43.191 14.484  1.00 24.61  ? 168 ARG A NH2 1 
ATOM   1355 N  N   . VAL A 1 169 ? -63.703 36.215 11.720  1.00 25.58  ? 169 VAL A N   1 
ATOM   1356 C  CA  . VAL A 1 169 ? -63.697 35.149 12.725  1.00 24.16  ? 169 VAL A CA  1 
ATOM   1357 C  C   . VAL A 1 169 ? -62.484 34.236 12.545  1.00 31.64  ? 169 VAL A C   1 
ATOM   1358 O  O   . VAL A 1 169 ? -61.830 33.847 13.521  1.00 25.58  ? 169 VAL A O   1 
ATOM   1359 C  CB  . VAL A 1 169 ? -65.023 34.364 12.665  1.00 30.18  ? 169 VAL A CB  1 
ATOM   1360 C  CG1 . VAL A 1 169 ? -64.949 33.091 13.513  1.00 22.57  ? 169 VAL A CG1 1 
ATOM   1361 C  CG2 . VAL A 1 169 ? -66.182 35.243 13.121  1.00 24.64  ? 169 VAL A CG2 1 
ATOM   1362 N  N   . GLN A 1 170 ? -62.145 33.895 11.300  1.00 27.30  ? 170 GLN A N   1 
ATOM   1363 C  CA  . GLN A 1 170 ? -60.996 33.020 11.075  1.00 31.58  ? 170 GLN A CA  1 
ATOM   1364 C  C   . GLN A 1 170 ? -59.689 33.705 11.478  1.00 27.25  ? 170 GLN A C   1 
ATOM   1365 O  O   . GLN A 1 170 ? -58.795 33.077 12.060  1.00 26.75  ? 170 GLN A O   1 
ATOM   1366 C  CB  . GLN A 1 170 ? -60.960 32.569 9.610   1.00 25.06  ? 170 GLN A CB  1 
ATOM   1367 C  CG  . GLN A 1 170 ? -59.843 31.594 9.300   1.00 26.11  ? 170 GLN A CG  1 
ATOM   1368 C  CD  . GLN A 1 170 ? -59.975 30.948 7.928   1.00 29.73  ? 170 GLN A CD  1 
ATOM   1369 O  OE1 . GLN A 1 170 ? -60.384 31.578 6.959   1.00 25.69  ? 170 GLN A OE1 1 
ATOM   1370 N  NE2 . GLN A 1 170 ? -59.612 29.684 7.846   1.00 29.67  ? 170 GLN A NE2 1 
ATOM   1371 N  N   . LEU A 1 171 ? -59.560 34.990 11.182  1.00 26.11  ? 171 LEU A N   1 
ATOM   1372 C  CA  . LEU A 1 171 ? -58.367 35.716 11.599  1.00 26.14  ? 171 LEU A CA  1 
ATOM   1373 C  C   . LEU A 1 171 ? -58.291 35.815 13.117  1.00 27.22  ? 171 LEU A C   1 
ATOM   1374 O  O   . LEU A 1 171 ? -57.208 35.676 13.707  1.00 25.43  ? 171 LEU A O   1 
ATOM   1375 C  CB  . LEU A 1 171 ? -58.360 37.103 10.959  1.00 24.60  ? 171 LEU A CB  1 
ATOM   1376 C  CG  . LEU A 1 171 ? -57.250 38.014 11.431  1.00 23.80  ? 171 LEU A CG  1 
ATOM   1377 C  CD1 . LEU A 1 171 ? -55.894 37.405 11.095  1.00 22.58  ? 171 LEU A CD1 1 
ATOM   1378 C  CD2 . LEU A 1 171 ? -57.443 39.352 10.767  1.00 19.07  ? 171 LEU A CD2 1 
ATOM   1379 N  N   . ARG A 1 172 ? -59.437 36.033 13.769  1.00 24.41  ? 172 ARG A N   1 
ATOM   1380 C  CA  . ARG A 1 172 ? -59.463 36.118 15.224  1.00 25.61  ? 172 ARG A CA  1 
ATOM   1381 C  C   . ARG A 1 172 ? -58.913 34.845 15.851  1.00 26.42  ? 172 ARG A C   1 
ATOM   1382 O  O   . ARG A 1 172 ? -58.088 34.897 16.776  1.00 26.39  ? 172 ARG A O   1 
ATOM   1383 C  CB  . ARG A 1 172 ? -60.892 36.379 15.707  1.00 25.40  ? 172 ARG A CB  1 
ATOM   1384 C  CG  . ARG A 1 172 ? -61.011 36.603 17.230  1.00 28.87  ? 172 ARG A CG  1 
ATOM   1385 C  CD  . ARG A 1 172 ? -62.456 36.905 17.628  1.00 25.93  ? 172 ARG A CD  1 
ATOM   1386 N  NE  . ARG A 1 172 ? -63.059 37.828 16.668  1.00 31.29  ? 172 ARG A NE  1 
ATOM   1387 C  CZ  . ARG A 1 172 ? -64.349 37.867 16.355  1.00 29.68  ? 172 ARG A CZ  1 
ATOM   1388 N  NH1 . ARG A 1 172 ? -65.229 37.086 16.954  1.00 30.28  ? 172 ARG A NH1 1 
ATOM   1389 N  NH2 . ARG A 1 172 ? -64.763 38.702 15.404  1.00 28.69  ? 172 ARG A NH2 1 
ATOM   1390 N  N   . ASP A 1 173 ? -59.365 33.685 15.359  1.00 27.07  ? 173 ASP A N   1 
ATOM   1391 C  CA  A ASP A 1 173 ? -58.882 32.413 15.889  0.31 27.85  ? 173 ASP A CA  1 
ATOM   1392 C  CA  B ASP A 1 173 ? -58.881 32.417 15.895  0.69 27.55  ? 173 ASP A CA  1 
ATOM   1393 C  C   . ASP A 1 173 ? -57.389 32.240 15.634  1.00 26.06  ? 173 ASP A C   1 
ATOM   1394 O  O   . ASP A 1 173 ? -56.667 31.686 16.472  1.00 30.49  ? 173 ASP A O   1 
ATOM   1395 C  CB  A ASP A 1 173 ? -59.674 31.256 15.275  0.31 29.18  ? 173 ASP A CB  1 
ATOM   1396 C  CB  B ASP A 1 173 ? -59.678 31.257 15.298  0.69 29.13  ? 173 ASP A CB  1 
ATOM   1397 C  CG  A ASP A 1 173 ? -59.233 29.901 15.804  0.31 34.02  ? 173 ASP A CG  1 
ATOM   1398 C  CG  B ASP A 1 173 ? -61.031 31.079 15.958  0.69 36.42  ? 173 ASP A CG  1 
ATOM   1399 O  OD1 A ASP A 1 173 ? -59.391 29.654 17.020  0.31 39.63  ? 173 ASP A OD1 1 
ATOM   1400 O  OD1 B ASP A 1 173 ? -61.171 31.465 17.146  0.69 43.47  ? 173 ASP A OD1 1 
ATOM   1401 O  OD2 A ASP A 1 173 ? -58.724 29.082 15.007  0.31 36.35  ? 173 ASP A OD2 1 
ATOM   1402 O  OD2 B ASP A 1 173 ? -61.949 30.545 15.297  0.69 39.31  ? 173 ASP A OD2 1 
ATOM   1403 N  N   . ALA A 1 174 ? -56.905 32.711 14.481  1.00 24.81  ? 174 ALA A N   1 
ATOM   1404 C  CA  . ALA A 1 174 ? -55.480 32.612 14.189  1.00 22.47  ? 174 ALA A CA  1 
ATOM   1405 C  C   . ALA A 1 174 ? -54.667 33.497 15.122  1.00 24.78  ? 174 ALA A C   1 
ATOM   1406 O  O   . ALA A 1 174 ? -53.595 33.094 15.587  1.00 23.53  ? 174 ALA A O   1 
ATOM   1407 C  CB  . ALA A 1 174 ? -55.206 32.968 12.729  1.00 22.70  ? 174 ALA A CB  1 
ATOM   1408 N  N   . LEU A 1 175 ? -55.151 34.707 15.408  1.00 22.78  ? 175 LEU A N   1 
ATOM   1409 C  CA  . LEU A 1 175 ? -54.407 35.574 16.314  1.00 22.32  ? 175 LEU A CA  1 
ATOM   1410 C  C   . LEU A 1 175 ? -54.425 35.011 17.730  1.00 28.04  ? 175 LEU A C   1 
ATOM   1411 O  O   . LEU A 1 175 ? -53.434 35.141 18.464  1.00 22.42  ? 175 LEU A O   1 
ATOM   1412 C  CB  . LEU A 1 175 ? -54.973 37.002 16.282  1.00 21.39  ? 175 LEU A CB  1 
ATOM   1413 C  CG  . LEU A 1 175 ? -54.967 37.768 14.943  1.00 29.37  ? 175 LEU A CG  1 
ATOM   1414 C  CD1 . LEU A 1 175 ? -55.784 39.059 15.027  1.00 22.69  ? 175 LEU A CD1 1 
ATOM   1415 C  CD2 . LEU A 1 175 ? -53.544 38.078 14.461  1.00 22.07  ? 175 LEU A CD2 1 
ATOM   1416 N  N   . ARG A 1 176 ? -55.537 34.370 18.118  1.00 27.20  ? 176 ARG A N   1 
ATOM   1417 C  CA  . ARG A 1 176 ? -55.594 33.673 19.399  1.00 26.80  ? 176 ARG A CA  1 
ATOM   1418 C  C   . ARG A 1 176 ? -54.570 32.552 19.481  1.00 28.40  ? 176 ARG A C   1 
ATOM   1419 O  O   . ARG A 1 176 ? -54.096 32.222 20.572  1.00 29.80  ? 176 ARG A O   1 
ATOM   1420 C  CB  . ARG A 1 176 ? -56.993 33.111 19.636  1.00 22.72  ? 176 ARG A CB  1 
ATOM   1421 C  CG  . ARG A 1 176 ? -57.979 34.154 20.136  1.00 29.81  ? 176 ARG A CG  1 
ATOM   1422 C  CD  . ARG A 1 176 ? -59.371 33.579 20.224  1.00 29.45  ? 176 ARG A CD  1 
ATOM   1423 N  NE  . ARG A 1 176 ? -60.303 34.529 20.814  1.00 34.54  ? 176 ARG A NE  1 
ATOM   1424 C  CZ  . ARG A 1 176 ? -61.600 34.560 20.546  1.00 32.32  ? 176 ARG A CZ  1 
ATOM   1425 N  NH1 . ARG A 1 176 ? -62.139 33.756 19.647  1.00 33.22  ? 176 ARG A NH1 1 
ATOM   1426 N  NH2 . ARG A 1 176 ? -62.375 35.421 21.197  1.00 31.92  ? 176 ARG A NH2 1 
ATOM   1427 N  N   . GLN A 1 177 ? -54.225 31.946 18.354  1.00 29.61  ? 177 GLN A N   1 
ATOM   1428 C  CA  . GLN A 1 177 ? -53.270 30.853 18.365  1.00 30.68  ? 177 GLN A CA  1 
ATOM   1429 C  C   . GLN A 1 177 ? -51.844 31.335 18.156  1.00 21.88  ? 177 GLN A C   1 
ATOM   1430 O  O   . GLN A 1 177 ? -50.942 30.510 18.002  1.00 29.17  ? 177 GLN A O   1 
ATOM   1431 C  CB  . GLN A 1 177 ? -53.664 29.800 17.326  1.00 25.65  ? 177 GLN A CB  1 
ATOM   1432 C  CG  . GLN A 1 177 ? -54.961 29.084 17.709  1.00 26.98  ? 177 GLN A CG  1 
ATOM   1433 C  CD  . GLN A 1 177 ? -55.439 28.090 16.667  1.00 35.86  ? 177 GLN A CD  1 
ATOM   1434 O  OE1 . GLN A 1 177 ? -54.947 28.059 15.535  1.00 30.51  ? 177 GLN A OE1 1 
ATOM   1435 N  NE2 . GLN A 1 177 ? -56.400 27.264 17.050  1.00 40.25  ? 177 GLN A NE2 1 
ATOM   1436 N  N   . GLY A 1 178 ? -51.620 32.646 18.181  1.00 21.58  ? 178 GLY A N   1 
ATOM   1437 C  CA  . GLY A 1 178 ? -50.281 33.198 18.202  1.00 23.61  ? 178 GLY A CA  1 
ATOM   1438 C  C   . GLY A 1 178 ? -49.819 33.891 16.930  1.00 29.19  ? 178 GLY A C   1 
ATOM   1439 O  O   . GLY A 1 178 ? -48.652 34.299 16.867  1.00 25.09  ? 178 GLY A O   1 
ATOM   1440 N  N   . ALA A 1 179 ? -50.675 34.023 15.912  1.00 25.03  ? 179 ALA A N   1 
ATOM   1441 C  CA  . ALA A 1 179 ? -50.271 34.726 14.698  1.00 26.16  ? 179 ALA A CA  1 
ATOM   1442 C  C   . ALA A 1 179 ? -49.850 36.147 15.041  1.00 26.09  ? 179 ALA A C   1 
ATOM   1443 O  O   . ALA A 1 179 ? -50.327 36.738 16.012  1.00 25.99  ? 179 ALA A O   1 
ATOM   1444 C  CB  . ALA A 1 179 ? -51.410 34.754 13.678  1.00 20.47  ? 179 ALA A CB  1 
ATOM   1445 N  N   . LEU A 1 180 ? -48.935 36.694 14.244  1.00 21.55  ? 180 LEU A N   1 
ATOM   1446 C  CA  . LEU A 1 180 ? -48.340 37.988 14.544  1.00 18.44  ? 180 LEU A CA  1 
ATOM   1447 C  C   . LEU A 1 180 ? -49.122 39.151 13.949  1.00 27.73  ? 180 LEU A C   1 
ATOM   1448 O  O   . LEU A 1 180 ? -48.840 40.304 14.285  1.00 25.87  ? 180 LEU A O   1 
ATOM   1449 C  CB  . LEU A 1 180 ? -46.895 38.030 14.036  1.00 22.66  ? 180 LEU A CB  1 
ATOM   1450 C  CG  . LEU A 1 180 ? -45.979 36.932 14.569  1.00 26.23  ? 180 LEU A CG  1 
ATOM   1451 C  CD1 . LEU A 1 180 ? -44.560 37.147 14.062  1.00 18.87  ? 180 LEU A CD1 1 
ATOM   1452 C  CD2 . LEU A 1 180 ? -46.009 36.920 16.089  1.00 21.90  ? 180 LEU A CD2 1 
ATOM   1453 N  N   . GLY A 1 181 ? -50.091 38.884 13.090  1.00 27.38  ? 181 GLY A N   1 
ATOM   1454 C  CA  . GLY A 1 181 ? -50.872 39.932 12.473  1.00 22.68  ? 181 GLY A CA  1 
ATOM   1455 C  C   . GLY A 1 181 ? -51.331 39.511 11.093  1.00 26.39  ? 181 GLY A C   1 
ATOM   1456 O  O   . GLY A 1 181 ? -51.361 38.326 10.759  1.00 26.70  ? 181 GLY A O   1 
ATOM   1457 N  N   . LEU A 1 182 ? -51.670 40.518 10.303  1.00 25.38  ? 182 LEU A N   1 
ATOM   1458 C  CA  . LEU A 1 182 ? -52.311 40.343 9.010   1.00 24.04  ? 182 LEU A CA  1 
ATOM   1459 C  C   . LEU A 1 182 ? -51.451 40.996 7.937   1.00 25.72  ? 182 LEU A C   1 
ATOM   1460 O  O   . LEU A 1 182 ? -51.053 42.158 8.083   1.00 24.21  ? 182 LEU A O   1 
ATOM   1461 C  CB  . LEU A 1 182 ? -53.710 40.977 9.019   1.00 20.07  ? 182 LEU A CB  1 
ATOM   1462 C  CG  . LEU A 1 182 ? -54.474 41.054 7.686   1.00 26.20  ? 182 LEU A CG  1 
ATOM   1463 C  CD1 . LEU A 1 182 ? -55.157 39.742 7.393   1.00 25.70  ? 182 LEU A CD1 1 
ATOM   1464 C  CD2 . LEU A 1 182 ? -55.490 42.168 7.739   1.00 24.16  ? 182 LEU A CD2 1 
ATOM   1465 N  N   . SER A 1 183 ? -51.159 40.259 6.865   1.00 23.17  ? 183 SER A N   1 
ATOM   1466 C  CA  . SER A 1 183 ? -50.469 40.842 5.723   1.00 20.45  ? 183 SER A CA  1 
ATOM   1467 C  C   . SER A 1 183 ? -51.438 41.003 4.553   1.00 29.77  ? 183 SER A C   1 
ATOM   1468 O  O   . SER A 1 183 ? -52.369 40.204 4.370   1.00 24.98  ? 183 SER A O   1 
ATOM   1469 C  CB  . SER A 1 183 ? -49.269 39.995 5.305   1.00 20.19  ? 183 SER A CB  1 
ATOM   1470 O  OG  . SER A 1 183 ? -49.680 38.837 4.610   1.00 21.67  ? 183 SER A OG  1 
ATOM   1471 N  N   . THR A 1 184 ? -51.234 42.070 3.779   1.00 24.51  ? 184 THR A N   1 
ATOM   1472 C  CA  . THR A 1 184 ? -51.955 42.260 2.531   1.00 28.55  ? 184 THR A CA  1 
ATOM   1473 C  C   . THR A 1 184 ? -50.979 42.354 1.369   1.00 32.49  ? 184 THR A C   1 
ATOM   1474 O  O   . THR A 1 184 ? -49.815 42.741 1.533   1.00 26.21  ? 184 THR A O   1 
ATOM   1475 C  CB  . THR A 1 184 ? -52.847 43.514 2.544   1.00 29.40  ? 184 THR A CB  1 
ATOM   1476 O  OG1 . THR A 1 184 ? -52.047 44.681 2.785   1.00 26.63  ? 184 THR A OG1 1 
ATOM   1477 C  CG2 . THR A 1 184 ? -53.941 43.387 3.601   1.00 24.58  ? 184 THR A CG2 1 
ATOM   1478 N  N   . GLY A 1 185 ? -51.472 41.963 0.193   1.00 29.06  ? 185 GLY A N   1 
ATOM   1479 C  CA  . GLY A 1 185 ? -50.775 42.147 -1.062  1.00 28.48  ? 185 GLY A CA  1 
ATOM   1480 C  C   . GLY A 1 185 ? -51.748 42.707 -2.074  1.00 30.50  ? 185 GLY A C   1 
ATOM   1481 O  O   . GLY A 1 185 ? -52.194 42.002 -2.987  1.00 30.90  ? 185 GLY A O   1 
ATOM   1482 N  N   . LEU A 1 186 ? -52.084 43.987 -1.906  1.00 25.06  ? 186 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 186 ? -53.216 44.583 -2.596  1.00 27.66  ? 186 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 186 ? -52.933 44.879 -4.064  1.00 27.81  ? 186 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 186 ? -53.876 45.100 -4.828  1.00 29.99  ? 186 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 186 ? -53.631 45.863 -1.865  1.00 29.22  ? 186 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 186 ? -54.031 45.659 -0.399  1.00 29.83  ? 186 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 186 ? -54.319 46.994 0.305   1.00 24.08  ? 186 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 186 ? -55.227 44.709 -0.290  1.00 22.00  ? 186 LEU A CD2 1 
ATOM   1490 N  N   . ALA A 1 187 ? -51.669 44.903 -4.477  1.00 29.56  ? 187 ALA A N   1 
ATOM   1491 C  CA  . ALA A 1 187 ? -51.374 45.115 -5.889  1.00 33.88  ? 187 ALA A CA  1 
ATOM   1492 C  C   . ALA A 1 187 ? -51.645 43.878 -6.736  1.00 33.96  ? 187 ALA A C   1 
ATOM   1493 O  O   . ALA A 1 187 ? -51.804 44.006 -7.953  1.00 36.53  ? 187 ALA A O   1 
ATOM   1494 C  CB  . ALA A 1 187 ? -49.919 45.554 -6.075  1.00 30.15  ? 187 ALA A CB  1 
ATOM   1495 N  N   . TYR A 1 188 ? -51.710 42.696 -6.128  1.00 31.82  ? 188 TYR A N   1 
ATOM   1496 C  CA  . TYR A 1 188 ? -51.945 41.476 -6.888  1.00 28.02  ? 188 TYR A CA  1 
ATOM   1497 C  C   . TYR A 1 188 ? -53.398 41.375 -7.318  1.00 31.19  ? 188 TYR A C   1 
ATOM   1498 O  O   . TYR A 1 188 ? -54.314 41.741 -6.575  1.00 29.65  ? 188 TYR A O   1 
ATOM   1499 C  CB  . TYR A 1 188 ? -51.552 40.241 -6.065  1.00 27.89  ? 188 TYR A CB  1 
ATOM   1500 C  CG  . TYR A 1 188 ? -50.055 40.126 -5.927  1.00 36.96  ? 188 TYR A CG  1 
ATOM   1501 C  CD1 . TYR A 1 188 ? -49.281 39.648 -6.981  1.00 37.00  ? 188 TYR A CD1 1 
ATOM   1502 C  CD2 . TYR A 1 188 ? -49.405 40.517 -4.758  1.00 33.82  ? 188 TYR A CD2 1 
ATOM   1503 C  CE1 . TYR A 1 188 ? -47.905 39.553 -6.872  1.00 36.47  ? 188 TYR A CE1 1 
ATOM   1504 C  CE2 . TYR A 1 188 ? -48.017 40.425 -4.643  1.00 34.90  ? 188 TYR A CE2 1 
ATOM   1505 C  CZ  . TYR A 1 188 ? -47.273 39.944 -5.704  1.00 36.58  ? 188 TYR A CZ  1 
ATOM   1506 O  OH  . TYR A 1 188 ? -45.894 39.847 -5.611  1.00 41.51  ? 188 TYR A OH  1 
ATOM   1507 N  N   . ALA A 1 189 ? -53.600 40.853 -8.530  1.00 31.92  ? 189 ALA A N   1 
ATOM   1508 C  CA  . ALA A 1 189 ? -54.944 40.730 -9.083  1.00 33.65  ? 189 ALA A CA  1 
ATOM   1509 C  C   . ALA A 1 189 ? -55.913 40.061 -8.115  1.00 32.80  ? 189 ALA A C   1 
ATOM   1510 O  O   . ALA A 1 189 ? -57.097 40.420 -8.076  1.00 29.98  ? 189 ALA A O   1 
ATOM   1511 C  CB  . ALA A 1 189 ? -54.902 39.955 -10.411 1.00 27.55  ? 189 ALA A CB  1 
ATOM   1512 N  N   . SER A 1 190 ? -55.446 39.096 -7.323  1.00 31.22  ? 190 SER A N   1 
ATOM   1513 C  CA  . SER A 1 190 ? -56.387 38.330 -6.514  1.00 32.09  ? 190 SER A CA  1 
ATOM   1514 C  C   . SER A 1 190 ? -56.874 39.091 -5.285  1.00 31.01  ? 190 SER A C   1 
ATOM   1515 O  O   . SER A 1 190 ? -57.835 38.654 -4.644  1.00 28.59  ? 190 SER A O   1 
ATOM   1516 C  CB  . SER A 1 190 ? -55.760 36.995 -6.111  1.00 33.06  ? 190 SER A CB  1 
ATOM   1517 O  OG  . SER A 1 190 ? -54.469 37.202 -5.588  1.00 37.63  ? 190 SER A OG  1 
ATOM   1518 N  N   . ALA A 1 191 ? -56.253 40.221 -4.958  1.00 28.07  ? 191 ALA A N   1 
ATOM   1519 C  CA  . ALA A 1 191 ? -56.719 41.089 -3.890  1.00 28.60  ? 191 ALA A CA  1 
ATOM   1520 C  C   . ALA A 1 191 ? -56.978 42.518 -4.348  1.00 28.12  ? 191 ALA A C   1 
ATOM   1521 O  O   . ALA A 1 191 ? -57.519 43.311 -3.568  1.00 29.65  ? 191 ALA A O   1 
ATOM   1522 C  CB  . ALA A 1 191 ? -55.699 41.114 -2.736  1.00 24.82  ? 191 ALA A CB  1 
ATOM   1523 N  N   . PHE A 1 192 ? -56.609 42.872 -5.582  1.00 28.75  ? 192 PHE A N   1 
ATOM   1524 C  CA  . PHE A 1 192 ? -56.757 44.248 -6.041  1.00 28.51  ? 192 PHE A CA  1 
ATOM   1525 C  C   . PHE A 1 192 ? -58.203 44.722 -5.993  1.00 33.64  ? 192 PHE A C   1 
ATOM   1526 O  O   . PHE A 1 192 ? -58.450 45.922 -5.815  1.00 33.74  ? 192 PHE A O   1 
ATOM   1527 C  CB  . PHE A 1 192 ? -56.223 44.389 -7.464  1.00 28.31  ? 192 PHE A CB  1 
ATOM   1528 C  CG  . PHE A 1 192 ? -56.175 45.811 -7.960  1.00 29.48  ? 192 PHE A CG  1 
ATOM   1529 C  CD1 . PHE A 1 192 ? -55.313 46.730 -7.384  1.00 27.88  ? 192 PHE A CD1 1 
ATOM   1530 C  CD2 . PHE A 1 192 ? -56.967 46.221 -9.018  1.00 28.18  ? 192 PHE A CD2 1 
ATOM   1531 C  CE1 . PHE A 1 192 ? -55.255 48.046 -7.847  1.00 34.33  ? 192 PHE A CE1 1 
ATOM   1532 C  CE2 . PHE A 1 192 ? -56.909 47.537 -9.495  1.00 29.87  ? 192 PHE A CE2 1 
ATOM   1533 C  CZ  . PHE A 1 192 ? -56.060 48.445 -8.910  1.00 37.60  ? 192 PHE A CZ  1 
ATOM   1534 N  N   . GLN A 1 193 ? -59.172 43.817 -6.158  1.00 25.89  ? 193 GLN A N   1 
ATOM   1535 C  CA  . GLN A 1 193 ? -60.560 44.267 -6.177  1.00 30.21  ? 193 GLN A CA  1 
ATOM   1536 C  C   . GLN A 1 193 ? -61.140 44.474 -4.780  1.00 33.10  ? 193 GLN A C   1 
ATOM   1537 O  O   . GLN A 1 193 ? -62.255 44.988 -4.660  1.00 34.46  ? 193 GLN A O   1 
ATOM   1538 C  CB  . GLN A 1 193 ? -61.440 43.290 -6.962  1.00 27.79  ? 193 GLN A CB  1 
ATOM   1539 C  CG  . GLN A 1 193 ? -61.117 43.204 -8.462  1.00 30.34  ? 193 GLN A CG  1 
ATOM   1540 C  CD  . GLN A 1 193 ? -61.095 44.567 -9.177  1.00 37.07  ? 193 GLN A CD  1 
ATOM   1541 O  OE1 . GLN A 1 193 ? -61.964 45.420 -8.977  1.00 35.63  ? 193 GLN A OE1 1 
ATOM   1542 N  NE2 . GLN A 1 193 ? -60.098 44.758 -10.029 1.00 30.54  ? 193 GLN A NE2 1 
ATOM   1543 N  N   . SER A 1 194 ? -60.415 44.116 -3.725  1.00 33.05  ? 194 SER A N   1 
ATOM   1544 C  CA  . SER A 1 194 ? -60.913 44.369 -2.383  1.00 33.91  ? 194 SER A CA  1 
ATOM   1545 C  C   . SER A 1 194 ? -61.017 45.871 -2.121  1.00 32.05  ? 194 SER A C   1 
ATOM   1546 O  O   . SER A 1 194 ? -60.194 46.663 -2.587  1.00 36.50  ? 194 SER A O   1 
ATOM   1547 C  CB  . SER A 1 194 ? -59.997 43.713 -1.352  1.00 31.75  ? 194 SER A CB  1 
ATOM   1548 O  OG  . SER A 1 194 ? -58.747 44.376 -1.269  1.00 33.26  ? 194 SER A OG  1 
ATOM   1549 N  N   . THR A 1 195 ? -62.044 46.262 -1.379  1.00 28.08  ? 195 THR A N   1 
ATOM   1550 C  CA  . THR A 1 195 ? -62.177 47.646 -0.966  1.00 28.23  ? 195 THR A CA  1 
ATOM   1551 C  C   . THR A 1 195 ? -61.349 47.910 0.295   1.00 25.12  ? 195 THR A C   1 
ATOM   1552 O  O   . THR A 1 195 ? -60.973 46.993 1.028   1.00 25.18  ? 195 THR A O   1 
ATOM   1553 C  CB  . THR A 1 195 ? -63.642 47.990 -0.687  1.00 35.37  ? 195 THR A CB  1 
ATOM   1554 O  OG1 . THR A 1 195 ? -64.133 47.161 0.375   1.00 35.03  ? 195 THR A OG1 1 
ATOM   1555 C  CG2 . THR A 1 195 ? -64.479 47.765 -1.906  1.00 31.90  ? 195 THR A CG2 1 
ATOM   1556 N  N   . THR A 1 196 ? -61.076 49.191 0.551   1.00 25.76  ? 196 THR A N   1 
ATOM   1557 C  CA  . THR A 1 196 ? -60.453 49.553 1.824   1.00 31.25  ? 196 THR A CA  1 
ATOM   1558 C  C   . THR A 1 196 ? -61.308 49.107 3.004   1.00 27.02  ? 196 THR A C   1 
ATOM   1559 O  O   . THR A 1 196 ? -60.777 48.764 4.061   1.00 29.16  ? 196 THR A O   1 
ATOM   1560 C  CB  . THR A 1 196 ? -60.220 51.064 1.901   1.00 36.32  ? 196 THR A CB  1 
ATOM   1561 O  OG1 . THR A 1 196 ? -59.570 51.518 0.708   1.00 31.11  ? 196 THR A OG1 1 
ATOM   1562 C  CG2 . THR A 1 196 ? -59.351 51.400 3.105   1.00 27.23  ? 196 THR A CG2 1 
ATOM   1563 N  N   . GLU A 1 197 ? -62.632 49.111 2.844   1.00 27.91  ? 197 GLU A N   1 
ATOM   1564 C  CA  . GLU A 1 197 ? -63.516 48.694 3.927   1.00 29.66  ? 197 GLU A CA  1 
ATOM   1565 C  C   . GLU A 1 197 ? -63.261 47.240 4.314   1.00 30.96  ? 197 GLU A C   1 
ATOM   1566 O  O   . GLU A 1 197 ? -63.181 46.905 5.501   1.00 27.69  ? 197 GLU A O   1 
ATOM   1567 C  CB  . GLU A 1 197 ? -64.965 48.896 3.503   1.00 27.92  ? 197 GLU A CB  1 
ATOM   1568 C  CG  . GLU A 1 197 ? -65.983 48.851 4.625   1.00 33.65  ? 197 GLU A CG  1 
ATOM   1569 C  CD  . GLU A 1 197 ? -67.385 49.109 4.101   1.00 35.54  ? 197 GLU A CD  1 
ATOM   1570 O  OE1 . GLU A 1 197 ? -67.969 48.202 3.481   1.00 40.00  ? 197 GLU A OE1 1 
ATOM   1571 O  OE2 . GLU A 1 197 ? -67.899 50.229 4.285   1.00 33.81  ? 197 GLU A OE2 1 
ATOM   1572 N  N   . GLU A 1 198 ? -63.143 46.359 3.319   1.00 27.46  ? 198 GLU A N   1 
ATOM   1573 C  CA  . GLU A 1 198 ? -62.889 44.950 3.600   1.00 29.95  ? 198 GLU A CA  1 
ATOM   1574 C  C   . GLU A 1 198 ? -61.631 44.784 4.443   1.00 27.09  ? 198 GLU A C   1 
ATOM   1575 O  O   . GLU A 1 198 ? -61.632 44.075 5.450   1.00 26.55  ? 198 GLU A O   1 
ATOM   1576 C  CB  . GLU A 1 198 ? -62.763 44.168 2.290   1.00 26.28  ? 198 GLU A CB  1 
ATOM   1577 C  CG  . GLU A 1 198 ? -61.937 42.890 2.437   1.00 29.57  ? 198 GLU A CG  1 
ATOM   1578 C  CD  . GLU A 1 198 ? -61.924 42.024 1.187   1.00 29.59  ? 198 GLU A CD  1 
ATOM   1579 O  OE1 . GLU A 1 198 ? -62.580 42.365 0.176   1.00 33.43  ? 198 GLU A OE1 1 
ATOM   1580 O  OE2 . GLU A 1 198 ? -61.245 40.981 1.223   1.00 30.79  ? 198 GLU A OE2 1 
ATOM   1581 N  N   . VAL A 1 199 ? -60.542 45.431 4.036   1.00 26.74  ? 199 VAL A N   1 
ATOM   1582 C  CA  . VAL A 1 199 ? -59.289 45.326 4.782   1.00 26.10  ? 199 VAL A CA  1 
ATOM   1583 C  C   . VAL A 1 199 ? -59.439 45.933 6.167   1.00 23.82  ? 199 VAL A C   1 
ATOM   1584 O  O   . VAL A 1 199 ? -58.909 45.403 7.148   1.00 25.51  ? 199 VAL A O   1 
ATOM   1585 C  CB  . VAL A 1 199 ? -58.143 45.994 3.995   1.00 25.47  ? 199 VAL A CB  1 
ATOM   1586 C  CG1 . VAL A 1 199 ? -56.816 45.842 4.739   1.00 22.63  ? 199 VAL A CG1 1 
ATOM   1587 C  CG2 . VAL A 1 199 ? -58.049 45.394 2.587   1.00 24.94  ? 199 VAL A CG2 1 
ATOM   1588 N  N   . MET A 1 200 ? -60.166 47.058 6.266   1.00 26.03  ? 200 MET A N   1 
ATOM   1589 C  CA  . MET A 1 200 ? -60.437 47.675 7.562   1.00 24.14  ? 200 MET A CA  1 
ATOM   1590 C  C   . MET A 1 200 ? -61.108 46.696 8.517   1.00 28.06  ? 200 MET A C   1 
ATOM   1591 O  O   . MET A 1 200 ? -60.762 46.634 9.705   1.00 28.64  ? 200 MET A O   1 
ATOM   1592 C  CB  . MET A 1 200 ? -61.308 48.908 7.381   1.00 24.27  ? 200 MET A CB  1 
ATOM   1593 C  CG  . MET A 1 200 ? -60.558 50.179 7.013   1.00 23.93  ? 200 MET A CG  1 
ATOM   1594 S  SD  . MET A 1 200 ? -61.741 51.515 6.624   1.00 31.71  ? 200 MET A SD  1 
ATOM   1595 C  CE  . MET A 1 200 ? -60.603 52.890 6.378   1.00 27.24  ? 200 MET A CE  1 
ATOM   1596 N  N   . ALA A 1 201 ? -62.065 45.917 8.015   1.00 25.82  ? 201 ALA A N   1 
ATOM   1597 C  CA  . ALA A 1 201 ? -62.747 44.950 8.864   1.00 24.26  ? 201 ALA A CA  1 
ATOM   1598 C  C   . ALA A 1 201 ? -61.762 43.945 9.448   1.00 26.60  ? 201 ALA A C   1 
ATOM   1599 O  O   . ALA A 1 201 ? -61.845 43.596 10.628  1.00 25.19  ? 201 ALA A O   1 
ATOM   1600 C  CB  . ALA A 1 201 ? -63.843 44.239 8.065   1.00 21.90  ? 201 ALA A CB  1 
ATOM   1601 N  N   . LEU A 1 202 ? -60.823 43.461 8.634   1.00 27.94  ? 202 LEU A N   1 
ATOM   1602 C  CA  . LEU A 1 202 ? -59.865 42.483 9.141   1.00 23.88  ? 202 LEU A CA  1 
ATOM   1603 C  C   . LEU A 1 202 ? -58.850 43.134 10.066  1.00 23.95  ? 202 LEU A C   1 
ATOM   1604 O  O   . LEU A 1 202 ? -58.478 42.555 11.089  1.00 26.13  ? 202 LEU A O   1 
ATOM   1605 C  CB  . LEU A 1 202 ? -59.158 41.782 7.981   1.00 21.57  ? 202 LEU A CB  1 
ATOM   1606 C  CG  . LEU A 1 202 ? -60.152 41.185 6.979   1.00 30.73  ? 202 LEU A CG  1 
ATOM   1607 C  CD1 . LEU A 1 202 ? -59.425 40.430 5.896   1.00 25.84  ? 202 LEU A CD1 1 
ATOM   1608 C  CD2 . LEU A 1 202 ? -61.117 40.265 7.711   1.00 22.89  ? 202 LEU A CD2 1 
ATOM   1609 N  N   . ALA A 1 203 ? -58.369 44.323 9.711   1.00 22.64  ? 203 ALA A N   1 
ATOM   1610 C  CA  . ALA A 1 203 ? -57.411 45.013 10.567  1.00 28.53  ? 203 ALA A CA  1 
ATOM   1611 C  C   . ALA A 1 203 ? -57.986 45.295 11.951  1.00 22.96  ? 203 ALA A C   1 
ATOM   1612 O  O   . ALA A 1 203 ? -57.220 45.468 12.906  1.00 23.25  ? 203 ALA A O   1 
ATOM   1613 C  CB  . ALA A 1 203 ? -56.951 46.320 9.904   1.00 19.60  ? 203 ALA A CB  1 
ATOM   1614 N  N   . GLU A 1 204 ? -59.314 45.333 12.087  1.00 23.58  ? 204 GLU A N   1 
ATOM   1615 C  CA  . GLU A 1 204 ? -59.901 45.575 13.400  1.00 25.77  ? 204 GLU A CA  1 
ATOM   1616 C  C   . GLU A 1 204 ? -59.612 44.429 14.358  1.00 22.27  ? 204 GLU A C   1 
ATOM   1617 O  O   . GLU A 1 204 ? -59.527 44.646 15.571  1.00 26.44  ? 204 GLU A O   1 
ATOM   1618 C  CB  . GLU A 1 204 ? -61.411 45.799 13.277  1.00 27.40  ? 204 GLU A CB  1 
ATOM   1619 C  CG  . GLU A 1 204 ? -61.760 47.201 12.856  1.00 24.54  ? 204 GLU A CG  1 
ATOM   1620 C  CD  . GLU A 1 204 ? -63.234 47.534 13.002  1.00 31.51  ? 204 GLU A CD  1 
ATOM   1621 O  OE1 . GLU A 1 204 ? -63.985 46.735 13.611  1.00 28.43  ? 204 GLU A OE1 1 
ATOM   1622 O  OE2 . GLU A 1 204 ? -63.640 48.610 12.501  1.00 28.13  ? 204 GLU A OE2 1 
ATOM   1623 N  N   . GLU A 1 205 ? -59.463 43.207 13.839  1.00 21.03  ? 205 GLU A N   1 
ATOM   1624 C  CA  . GLU A 1 205 ? -59.085 42.092 14.697  1.00 23.35  ? 205 GLU A CA  1 
ATOM   1625 C  C   . GLU A 1 205 ? -57.735 42.308 15.358  1.00 30.52  ? 205 GLU A C   1 
ATOM   1626 O  O   . GLU A 1 205 ? -57.422 41.608 16.330  1.00 24.53  ? 205 GLU A O   1 
ATOM   1627 C  CB  . GLU A 1 205 ? -59.061 40.792 13.902  1.00 19.51  ? 205 GLU A CB  1 
ATOM   1628 C  CG  . GLU A 1 205 ? -60.421 40.370 13.395  1.00 24.51  ? 205 GLU A CG  1 
ATOM   1629 C  CD  . GLU A 1 205 ? -61.396 40.073 14.521  1.00 31.42  ? 205 GLU A CD  1 
ATOM   1630 O  OE1 . GLU A 1 205 ? -60.939 39.630 15.605  1.00 28.42  ? 205 GLU A OE1 1 
ATOM   1631 O  OE2 . GLU A 1 205 ? -62.616 40.276 14.320  1.00 27.83  ? 205 GLU A OE2 1 
ATOM   1632 N  N   . LEU A 1 206 ? -56.926 43.249 14.851  1.00 30.74  ? 206 LEU A N   1 
ATOM   1633 C  CA  . LEU A 1 206 ? -55.572 43.460 15.353  1.00 26.95  ? 206 LEU A CA  1 
ATOM   1634 C  C   . LEU A 1 206 ? -55.506 44.451 16.508  1.00 29.28  ? 206 LEU A C   1 
ATOM   1635 O  O   . LEU A 1 206 ? -54.436 44.622 17.102  1.00 29.00  ? 206 LEU A O   1 
ATOM   1636 C  CB  . LEU A 1 206 ? -54.663 43.950 14.221  1.00 21.24  ? 206 LEU A CB  1 
ATOM   1637 C  CG  . LEU A 1 206 ? -54.620 43.111 12.941  1.00 26.06  ? 206 LEU A CG  1 
ATOM   1638 C  CD1 . LEU A 1 206 ? -54.012 43.934 11.806  1.00 24.56  ? 206 LEU A CD1 1 
ATOM   1639 C  CD2 . LEU A 1 206 ? -53.846 41.813 13.142  1.00 24.96  ? 206 LEU A CD2 1 
ATOM   1640 N  N   . ALA A 1 207 ? -56.610 45.113 16.831  1.00 28.69  ? 207 ALA A N   1 
ATOM   1641 C  CA  . ALA A 1 207 ? -56.566 46.185 17.804  1.00 24.08  ? 207 ALA A CA  1 
ATOM   1642 C  C   . ALA A 1 207 ? -56.222 45.644 19.195  1.00 31.24  ? 207 ALA A C   1 
ATOM   1643 O  O   . ALA A 1 207 ? -56.266 44.437 19.462  1.00 29.89  ? 207 ALA A O   1 
ATOM   1644 C  CB  . ALA A 1 207 ? -57.902 46.925 17.832  1.00 27.26  ? 207 ALA A CB  1 
ATOM   1645 N  N   . ALA A 1 208 ? -55.885 46.568 20.094  1.00 26.06  ? 208 ALA A N   1 
ATOM   1646 C  CA  . ALA A 1 208 ? -55.578 46.223 21.481  1.00 36.55  ? 208 ALA A CA  1 
ATOM   1647 C  C   . ALA A 1 208 ? -54.368 45.297 21.560  1.00 30.97  ? 208 ALA A C   1 
ATOM   1648 O  O   . ALA A 1 208 ? -54.309 44.395 22.396  1.00 27.91  ? 208 ALA A O   1 
ATOM   1649 C  CB  . ALA A 1 208 ? -56.786 45.593 22.179  1.00 29.22  ? 208 ALA A CB  1 
ATOM   1650 N  N   . GLY A 1 209 ? -53.404 45.507 20.666  1.00 30.28  ? 209 GLY A N   1 
ATOM   1651 C  CA  . GLY A 1 209 ? -52.161 44.769 20.706  1.00 24.13  ? 209 GLY A CA  1 
ATOM   1652 C  C   . GLY A 1 209 ? -52.212 43.375 20.131  1.00 30.61  ? 209 GLY A C   1 
ATOM   1653 O  O   . GLY A 1 209 ? -51.238 42.628 20.285  1.00 29.03  ? 209 GLY A O   1 
ATOM   1654 N  N   . LYS A 1 210 ? -53.298 42.996 19.458  1.00 24.24  ? 210 LYS A N   1 
ATOM   1655 C  CA  . LYS A 1 210 ? -53.399 41.636 18.941  1.00 28.14  ? 210 LYS A CA  1 
ATOM   1656 C  C   . LYS A 1 210 ? -52.645 41.410 17.628  1.00 31.90  ? 210 LYS A C   1 
ATOM   1657 O  O   . LYS A 1 210 ? -52.697 40.297 17.097  1.00 30.67  ? 210 LYS A O   1 
ATOM   1658 C  CB  . LYS A 1 210 ? -54.871 41.241 18.779  1.00 25.71  ? 210 LYS A CB  1 
ATOM   1659 C  CG  . LYS A 1 210 ? -55.634 41.246 20.098  1.00 32.53  ? 210 LYS A CG  1 
ATOM   1660 C  CD  . LYS A 1 210 ? -56.878 40.369 20.027  1.00 47.17  ? 210 LYS A CD  1 
ATOM   1661 C  CE  . LYS A 1 210 ? -58.128 41.093 20.525  1.00 46.73  ? 210 LYS A CE  1 
ATOM   1662 N  NZ  . LYS A 1 210 ? -58.042 41.489 21.953  1.00 54.60  ? 210 LYS A NZ  1 
ATOM   1663 N  N   . GLY A 1 211 ? -51.936 42.397 17.094  1.00 26.90  ? 211 GLY A N   1 
ATOM   1664 C  CA  . GLY A 1 211 ? -51.071 42.138 15.962  1.00 25.01  ? 211 GLY A CA  1 
ATOM   1665 C  C   . GLY A 1 211 ? -50.719 43.417 15.229  1.00 29.11  ? 211 GLY A C   1 
ATOM   1666 O  O   . GLY A 1 211 ? -51.089 44.509 15.640  1.00 29.81  ? 211 GLY A O   1 
ATOM   1667 N  N   . VAL A 1 212 ? -49.984 43.247 14.128  1.00 20.89  ? 212 VAL A N   1 
ATOM   1668 C  CA  . VAL A 1 212 ? -49.553 44.361 13.292  1.00 23.81  ? 212 VAL A CA  1 
ATOM   1669 C  C   . VAL A 1 212 ? -50.171 44.189 11.912  1.00 24.44  ? 212 VAL A C   1 
ATOM   1670 O  O   . VAL A 1 212 ? -50.354 43.060 11.442  1.00 25.73  ? 212 VAL A O   1 
ATOM   1671 C  CB  . VAL A 1 212 ? -48.008 44.457 13.208  1.00 29.24  ? 212 VAL A CB  1 
ATOM   1672 C  CG1 . VAL A 1 212 ? -47.409 43.191 12.625  1.00 21.82  ? 212 VAL A CG1 1 
ATOM   1673 C  CG2 . VAL A 1 212 ? -47.600 45.637 12.345  1.00 30.09  ? 212 VAL A CG2 1 
ATOM   1674 N  N   . TYR A 1 213 ? -50.518 45.307 11.273  1.00 22.06  ? 213 TYR A N   1 
ATOM   1675 C  CA  . TYR A 1 213 ? -50.964 45.291 9.882   1.00 22.11  ? 213 TYR A CA  1 
ATOM   1676 C  C   . TYR A 1 213 ? -49.760 45.524 8.964   1.00 22.97  ? 213 TYR A C   1 
ATOM   1677 O  O   . TYR A 1 213 ? -49.166 46.609 8.975   1.00 28.17  ? 213 TYR A O   1 
ATOM   1678 C  CB  . TYR A 1 213 ? -52.040 46.347 9.649   1.00 24.81  ? 213 TYR A CB  1 
ATOM   1679 C  CG  . TYR A 1 213 ? -52.421 46.487 8.188   1.00 24.39  ? 213 TYR A CG  1 
ATOM   1680 C  CD1 . TYR A 1 213 ? -53.113 45.479 7.531   1.00 26.41  ? 213 TYR A CD1 1 
ATOM   1681 C  CD2 . TYR A 1 213 ? -52.070 47.621 7.454   1.00 23.68  ? 213 TYR A CD2 1 
ATOM   1682 C  CE1 . TYR A 1 213 ? -53.446 45.592 6.180   1.00 21.18  ? 213 TYR A CE1 1 
ATOM   1683 C  CE2 . TYR A 1 213 ? -52.418 47.741 6.098   1.00 26.84  ? 213 TYR A CE2 1 
ATOM   1684 C  CZ  . TYR A 1 213 ? -53.105 46.712 5.472   1.00 27.35  ? 213 TYR A CZ  1 
ATOM   1685 O  OH  . TYR A 1 213 ? -53.453 46.786 4.127   1.00 26.88  ? 213 TYR A OH  1 
ATOM   1686 N  N   . THR A 1 214 ? -49.388 44.515 8.176   1.00 22.44  ? 214 THR A N   1 
ATOM   1687 C  CA  . THR A 1 214 ? -48.303 44.653 7.203   1.00 24.06  ? 214 THR A CA  1 
ATOM   1688 C  C   . THR A 1 214 ? -48.888 44.623 5.800   1.00 25.36  ? 214 THR A C   1 
ATOM   1689 O  O   . THR A 1 214 ? -49.826 43.870 5.524   1.00 28.68  ? 214 THR A O   1 
ATOM   1690 C  CB  . THR A 1 214 ? -47.246 43.549 7.347   1.00 25.62  ? 214 THR A CB  1 
ATOM   1691 O  OG1 . THR A 1 214 ? -47.683 42.380 6.649   1.00 36.17  ? 214 THR A OG1 1 
ATOM   1692 C  CG2 . THR A 1 214 ? -47.047 43.187 8.803   1.00 25.93  ? 214 THR A CG2 1 
ATOM   1693 N  N   . THR A 1 215 ? -48.343 45.439 4.908   1.00 21.59  ? 215 THR A N   1 
ATOM   1694 C  CA  . THR A 1 215 ? -48.989 45.618 3.619   1.00 25.10  ? 215 THR A CA  1 
ATOM   1695 C  C   . THR A 1 215 ? -47.972 45.764 2.497   1.00 27.56  ? 215 THR A C   1 
ATOM   1696 O  O   . THR A 1 215 ? -47.089 46.630 2.530   1.00 21.54  ? 215 THR A O   1 
ATOM   1697 C  CB  . THR A 1 215 ? -49.934 46.824 3.635   1.00 30.69  ? 215 THR A CB  1 
ATOM   1698 O  OG1 . THR A 1 215 ? -50.436 47.025 2.313   1.00 29.41  ? 215 THR A OG1 1 
ATOM   1699 C  CG2 . THR A 1 215 ? -49.226 48.094 4.122   1.00 25.69  ? 215 THR A CG2 1 
ATOM   1700 N  N   . HIS A 1 216 ? -48.097 44.891 1.515   1.00 30.77  ? 216 HIS A N   1 
ATOM   1701 C  CA  . HIS A 1 216 ? -47.681 45.213 0.165   1.00 24.89  ? 216 HIS A CA  1 
ATOM   1702 C  C   . HIS A 1 216 ? -48.711 46.193 -0.383  1.00 28.83  ? 216 HIS A C   1 
ATOM   1703 O  O   . HIS A 1 216 ? -49.883 45.837 -0.535  1.00 28.52  ? 216 HIS A O   1 
ATOM   1704 C  CB  . HIS A 1 216 ? -47.607 43.927 -0.648  1.00 28.97  ? 216 HIS A CB  1 
ATOM   1705 C  CG  . HIS A 1 216 ? -47.201 44.119 -2.073  1.00 32.50  ? 216 HIS A CG  1 
ATOM   1706 N  ND1 . HIS A 1 216 ? -46.366 43.239 -2.725  1.00 29.90  ? 216 HIS A ND1 1 
ATOM   1707 C  CD2 . HIS A 1 216 ? -47.526 45.071 -2.980  1.00 33.06  ? 216 HIS A CD2 1 
ATOM   1708 C  CE1 . HIS A 1 216 ? -46.189 43.643 -3.971  1.00 28.10  ? 216 HIS A CE1 1 
ATOM   1709 N  NE2 . HIS A 1 216 ? -46.879 44.754 -4.151  1.00 34.39  ? 216 HIS A NE2 1 
ATOM   1710 N  N   . LEU A 1 217 ? -48.287 47.434 -0.634  1.00 27.49  ? 217 LEU A N   1 
ATOM   1711 C  CA  . LEU A 1 217 ? -49.200 48.512 -1.014  1.00 28.05  ? 217 LEU A CA  1 
ATOM   1712 C  C   . LEU A 1 217 ? -49.997 48.183 -2.272  1.00 30.66  ? 217 LEU A C   1 
ATOM   1713 O  O   . LEU A 1 217 ? -49.552 47.435 -3.145  1.00 34.81  ? 217 LEU A O   1 
ATOM   1714 C  CB  . LEU A 1 217 ? -48.432 49.807 -1.265  1.00 27.26  ? 217 LEU A CB  1 
ATOM   1715 C  CG  . LEU A 1 217 ? -47.719 50.442 -0.075  1.00 30.83  ? 217 LEU A CG  1 
ATOM   1716 C  CD1 . LEU A 1 217 ? -46.981 51.675 -0.576  1.00 27.29  ? 217 LEU A CD1 1 
ATOM   1717 C  CD2 . LEU A 1 217 ? -48.708 50.795 1.055   1.00 21.30  ? 217 LEU A CD2 1 
ATOM   1718 N  N   . ARG A 1 218 ? -51.179 48.799 -2.378  1.00 27.69  ? 218 ARG A N   1 
ATOM   1719 C  CA  . ARG A 1 218 ? -51.989 48.620 -3.574  1.00 32.16  ? 218 ARG A CA  1 
ATOM   1720 C  C   . ARG A 1 218 ? -51.238 49.050 -4.828  1.00 30.65  ? 218 ARG A C   1 
ATOM   1721 O  O   . ARG A 1 218 ? -51.540 48.565 -5.923  1.00 34.55  ? 218 ARG A O   1 
ATOM   1722 C  CB  . ARG A 1 218 ? -53.305 49.384 -3.447  1.00 30.64  ? 218 ARG A CB  1 
ATOM   1723 C  CG  . ARG A 1 218 ? -54.365 48.860 -4.409  1.00 36.76  ? 218 ARG A CG  1 
ATOM   1724 C  CD  . ARG A 1 218 ? -55.738 49.356 -4.070  1.00 37.11  ? 218 ARG A CD  1 
ATOM   1725 N  NE  . ARG A 1 218 ? -56.225 48.914 -2.762  1.00 35.96  ? 218 ARG A NE  1 
ATOM   1726 C  CZ  . ARG A 1 218 ? -57.097 47.929 -2.566  1.00 38.17  ? 218 ARG A CZ  1 
ATOM   1727 N  NH1 . ARG A 1 218 ? -57.437 47.092 -3.544  1.00 25.82  ? 218 ARG A NH1 1 
ATOM   1728 N  NH2 . ARG A 1 218 ? -57.670 47.802 -1.370  1.00 29.07  ? 218 ARG A NH2 1 
ATOM   1729 N  N   . SER A 1 219 ? -50.264 49.951 -4.692  1.00 26.74  ? 219 SER A N   1 
ATOM   1730 C  CA  . SER A 1 219 ? -49.390 50.330 -5.794  1.00 32.58  ? 219 SER A CA  1 
ATOM   1731 C  C   . SER A 1 219 ? -48.063 50.817 -5.235  1.00 32.52  ? 219 SER A C   1 
ATOM   1732 O  O   . SER A 1 219 ? -48.031 51.547 -4.241  1.00 39.51  ? 219 SER A O   1 
ATOM   1733 C  CB  . SER A 1 219 ? -50.010 51.428 -6.676  1.00 33.40  ? 219 SER A CB  1 
ATOM   1734 O  OG  . SER A 1 219 ? -49.114 51.807 -7.718  1.00 36.51  ? 219 SER A OG  1 
ATOM   1735 N  N   . GLU A 1 220 ? -46.970 50.413 -5.877  1.00 33.92  ? 220 GLU A N   1 
ATOM   1736 C  CA  . GLU A 1 220 ? -45.644 50.936 -5.557  1.00 39.58  ? 220 GLU A CA  1 
ATOM   1737 C  C   . GLU A 1 220 ? -45.101 51.818 -6.679  1.00 40.03  ? 220 GLU A C   1 
ATOM   1738 O  O   . GLU A 1 220 ? -43.881 52.022 -6.780  1.00 34.56  ? 220 GLU A O   1 
ATOM   1739 C  CB  . GLU A 1 220 ? -44.671 49.794 -5.242  1.00 32.36  ? 220 GLU A CB  1 
ATOM   1740 C  CG  . GLU A 1 220 ? -45.089 48.930 -4.060  1.00 36.08  ? 220 GLU A CG  1 
ATOM   1741 C  CD  . GLU A 1 220 ? -43.953 48.062 -3.528  1.00 41.27  ? 220 GLU A CD  1 
ATOM   1742 O  OE1 . GLU A 1 220 ? -43.380 47.291 -4.318  1.00 36.28  ? 220 GLU A OE1 1 
ATOM   1743 O  OE2 . GLU A 1 220 ? -43.623 48.161 -2.320  1.00 32.45  ? 220 GLU A OE2 1 
ATOM   1744 N  N   . PHE A 1 221 ? -45.993 52.349 -7.521  1.00 35.11  ? 221 PHE A N   1 
ATOM   1745 C  CA  . PHE A 1 221 ? -45.604 53.139 -8.683  1.00 33.22  ? 221 PHE A CA  1 
ATOM   1746 C  C   . PHE A 1 221 ? -46.167 54.556 -8.568  1.00 34.01  ? 221 PHE A C   1 
ATOM   1747 O  O   . PHE A 1 221 ? -46.084 55.159 -7.493  1.00 36.86  ? 221 PHE A O   1 
ATOM   1748 C  CB  . PHE A 1 221 ? -46.041 52.422 -9.963  1.00 34.81  ? 221 PHE A CB  1 
ATOM   1749 C  CG  . PHE A 1 221 ? -45.315 51.109 -10.186 1.00 33.73  ? 221 PHE A CG  1 
ATOM   1750 C  CD1 . PHE A 1 221 ? -45.743 49.943 -9.565  1.00 37.01  ? 221 PHE A CD1 1 
ATOM   1751 C  CD2 . PHE A 1 221 ? -44.186 51.048 -10.989 1.00 38.26  ? 221 PHE A CD2 1 
ATOM   1752 C  CE1 . PHE A 1 221 ? -45.067 48.741 -9.750  1.00 35.58  ? 221 PHE A CE1 1 
ATOM   1753 C  CE2 . PHE A 1 221 ? -43.511 49.846 -11.181 1.00 37.45  ? 221 PHE A CE2 1 
ATOM   1754 C  CZ  . PHE A 1 221 ? -43.954 48.694 -10.555 1.00 30.93  ? 221 PHE A CZ  1 
ATOM   1755 N  N   . GLU A 1 222 ? -46.750 55.101 -9.639  1.00 36.78  ? 222 GLU A N   1 
ATOM   1756 C  CA  A GLU A 1 222 ? -47.171 56.502 -9.621  0.51 41.35  ? 222 GLU A CA  1 
ATOM   1757 C  CA  B GLU A 1 222 ? -47.165 56.502 -9.615  0.49 41.35  ? 222 GLU A CA  1 
ATOM   1758 C  C   . GLU A 1 222 ? -48.109 56.816 -8.465  1.00 41.52  ? 222 GLU A C   1 
ATOM   1759 O  O   . GLU A 1 222 ? -47.862 57.798 -7.747  1.00 44.22  ? 222 GLU A O   1 
ATOM   1760 C  CB  A GLU A 1 222 ? -47.802 56.875 -10.970 0.51 41.51  ? 222 GLU A CB  1 
ATOM   1761 C  CB  B GLU A 1 222 ? -47.782 56.892 -10.962 0.49 41.52  ? 222 GLU A CB  1 
ATOM   1762 C  CG  A GLU A 1 222 ? -47.900 58.383 -11.214 0.51 47.30  ? 222 GLU A CG  1 
ATOM   1763 C  CG  B GLU A 1 222 ? -47.967 58.396 -11.139 0.49 47.30  ? 222 GLU A CG  1 
ATOM   1764 C  CD  A GLU A 1 222 ? -48.581 58.742 -12.535 0.51 57.52  ? 222 GLU A CD  1 
ATOM   1765 C  CD  B GLU A 1 222 ? -49.330 58.893 -10.679 0.49 53.28  ? 222 GLU A CD  1 
ATOM   1766 O  OE1 A GLU A 1 222 ? -49.673 58.200 -12.821 0.51 65.55  ? 222 GLU A OE1 1 
ATOM   1767 O  OE1 B GLU A 1 222 ? -50.237 58.057 -10.477 0.49 46.84  ? 222 GLU A OE1 1 
ATOM   1768 O  OE2 A GLU A 1 222 ? -48.024 59.569 -13.292 0.51 53.13  ? 222 GLU A OE2 1 
ATOM   1769 O  OE2 B GLU A 1 222 ? -49.496 60.125 -10.529 0.49 54.88  ? 222 GLU A OE2 1 
ATOM   1770 N  N   . PRO A 1 223 ? -49.188 56.057 -8.229  1.00 40.35  ? 223 PRO A N   1 
ATOM   1771 C  CA  . PRO A 1 223 ? -50.112 56.433 -7.149  1.00 40.18  ? 223 PRO A CA  1 
ATOM   1772 C  C   . PRO A 1 223 ? -49.704 55.918 -5.778  1.00 36.80  ? 223 PRO A C   1 
ATOM   1773 O  O   . PRO A 1 223 ? -50.568 55.622 -4.948  1.00 39.43  ? 223 PRO A O   1 
ATOM   1774 C  CB  . PRO A 1 223 ? -51.445 55.823 -7.608  1.00 35.92  ? 223 PRO A CB  1 
ATOM   1775 C  CG  . PRO A 1 223 ? -51.060 54.656 -8.435  1.00 35.61  ? 223 PRO A CG  1 
ATOM   1776 C  CD  . PRO A 1 223 ? -49.744 54.994 -9.091  1.00 37.07  ? 223 PRO A CD  1 
ATOM   1777 N  N   . ILE A 1 224 ? -48.400 55.853 -5.500  1.00 35.18  ? 224 ILE A N   1 
ATOM   1778 C  CA  . ILE A 1 224 ? -47.961 55.242 -4.244  1.00 35.15  ? 224 ILE A CA  1 
ATOM   1779 C  C   . ILE A 1 224 ? -48.393 56.074 -3.038  1.00 29.39  ? 224 ILE A C   1 
ATOM   1780 O  O   . ILE A 1 224 ? -48.666 55.517 -1.970  1.00 32.99  ? 224 ILE A O   1 
ATOM   1781 C  CB  . ILE A 1 224 ? -46.436 55.007 -4.244  1.00 36.28  ? 224 ILE A CB  1 
ATOM   1782 C  CG1 . ILE A 1 224 ? -46.011 54.274 -2.967  1.00 30.34  ? 224 ILE A CG1 1 
ATOM   1783 C  CG2 . ILE A 1 224 ? -45.676 56.326 -4.364  1.00 31.40  ? 224 ILE A CG2 1 
ATOM   1784 C  CD1 . ILE A 1 224 ? -44.591 53.829 -2.981  1.00 31.65  ? 224 ILE A CD1 1 
ATOM   1785 N  N   . LEU A 1 225 ? -48.464 57.405 -3.169  1.00 29.45  ? 225 LEU A N   1 
ATOM   1786 C  CA  . LEU A 1 225 ? -48.929 58.216 -2.044  1.00 34.31  ? 225 LEU A CA  1 
ATOM   1787 C  C   . LEU A 1 225 ? -50.374 57.892 -1.707  1.00 33.98  ? 225 LEU A C   1 
ATOM   1788 O  O   . LEU A 1 225 ? -50.735 57.793 -0.533  1.00 37.69  ? 225 LEU A O   1 
ATOM   1789 C  CB  . LEU A 1 225 ? -48.780 59.707 -2.340  1.00 27.55  ? 225 LEU A CB  1 
ATOM   1790 C  CG  . LEU A 1 225 ? -47.328 60.181 -2.476  1.00 37.33  ? 225 LEU A CG  1 
ATOM   1791 C  CD1 . LEU A 1 225 ? -47.276 61.618 -2.948  1.00 29.07  ? 225 LEU A CD1 1 
ATOM   1792 C  CD2 . LEU A 1 225 ? -46.547 60.007 -1.184  1.00 26.96  ? 225 LEU A CD2 1 
ATOM   1793 N  N   . GLU A 1 226 ? -51.215 57.717 -2.728  1.00 31.99  ? 226 GLU A N   1 
ATOM   1794 C  CA  A GLU A 1 226 ? -52.591 57.295 -2.491  0.54 36.21  ? 226 GLU A CA  1 
ATOM   1795 C  CA  C GLU A 1 226 ? -52.591 57.296 -2.487  0.46 36.22  ? 226 GLU A CA  1 
ATOM   1796 C  C   . GLU A 1 226 ? -52.626 55.947 -1.784  1.00 33.42  ? 226 GLU A C   1 
ATOM   1797 O  O   . GLU A 1 226 ? -53.395 55.752 -0.837  1.00 34.54  ? 226 GLU A O   1 
ATOM   1798 C  CB  A GLU A 1 226 ? -53.348 57.246 -3.822  0.54 37.52  ? 226 GLU A CB  1 
ATOM   1799 C  CB  C GLU A 1 226 ? -53.370 57.231 -3.803  0.46 37.54  ? 226 GLU A CB  1 
ATOM   1800 C  CG  A GLU A 1 226 ? -54.800 56.791 -3.762  0.54 40.32  ? 226 GLU A CG  1 
ATOM   1801 C  CG  C GLU A 1 226 ? -52.819 58.106 -4.926  0.46 40.07  ? 226 GLU A CG  1 
ATOM   1802 C  CD  A GLU A 1 226 ? -55.445 56.793 -5.145  0.54 52.93  ? 226 GLU A CD  1 
ATOM   1803 C  CD  C GLU A 1 226 ? -52.934 59.578 -4.625  0.46 43.97  ? 226 GLU A CD  1 
ATOM   1804 O  OE1 A GLU A 1 226 ? -54.854 57.382 -6.083  0.54 45.06  ? 226 GLU A OE1 1 
ATOM   1805 O  OE1 C GLU A 1 226 ? -53.674 59.925 -3.677  0.46 45.71  ? 226 GLU A OE1 1 
ATOM   1806 O  OE2 A GLU A 1 226 ? -56.538 56.205 -5.301  0.54 60.57  ? 226 GLU A OE2 1 
ATOM   1807 O  OE2 C GLU A 1 226 ? -52.283 60.381 -5.332  0.46 42.77  ? 226 GLU A OE2 1 
ATOM   1808 N  N   . ALA A 1 227 ? -51.782 55.012 -2.222  1.00 31.33  ? 227 ALA A N   1 
ATOM   1809 C  CA  . ALA A 1 227 ? -51.734 53.701 -1.591  1.00 30.76  ? 227 ALA A CA  1 
ATOM   1810 C  C   . ALA A 1 227 ? -51.191 53.799 -0.171  1.00 30.35  ? 227 ALA A C   1 
ATOM   1811 O  O   . ALA A 1 227 ? -51.657 53.095 0.729   1.00 30.36  ? 227 ALA A O   1 
ATOM   1812 C  CB  . ALA A 1 227 ? -50.885 52.749 -2.432  1.00 28.40  ? 227 ALA A CB  1 
ATOM   1813 N  N   . LEU A 1 228 ? -50.191 54.651 0.048   1.00 28.61  ? 228 LEU A N   1 
ATOM   1814 C  CA  . LEU A 1 228 ? -49.727 54.880 1.411   1.00 29.81  ? 228 LEU A CA  1 
ATOM   1815 C  C   . LEU A 1 228 ? -50.849 55.446 2.269   1.00 35.00  ? 228 LEU A C   1 
ATOM   1816 O  O   . LEU A 1 228 ? -51.025 55.044 3.424   1.00 27.78  ? 228 LEU A O   1 
ATOM   1817 C  CB  . LEU A 1 228 ? -48.530 55.829 1.415   1.00 28.63  ? 228 LEU A CB  1 
ATOM   1818 C  CG  . LEU A 1 228 ? -47.179 55.213 1.099   1.00 30.61  ? 228 LEU A CG  1 
ATOM   1819 C  CD1 . LEU A 1 228 ? -46.177 56.312 0.845   1.00 27.58  ? 228 LEU A CD1 1 
ATOM   1820 C  CD2 . LEU A 1 228 ? -46.732 54.330 2.245   1.00 24.73  ? 228 LEU A CD2 1 
ATOM   1821 N  N   . ASP A 1 229 ? -51.621 56.384 1.709   1.00 34.11  ? 229 ASP A N   1 
ATOM   1822 C  CA  . ASP A 1 229 ? -52.715 56.996 2.450   1.00 34.59  ? 229 ASP A CA  1 
ATOM   1823 C  C   . ASP A 1 229 ? -53.765 55.961 2.856   1.00 34.26  ? 229 ASP A C   1 
ATOM   1824 O  O   . ASP A 1 229 ? -54.273 55.992 3.983   1.00 38.91  ? 229 ASP A O   1 
ATOM   1825 C  CB  . ASP A 1 229 ? -53.336 58.107 1.612   1.00 33.97  ? 229 ASP A CB  1 
ATOM   1826 C  CG  . ASP A 1 229 ? -54.444 58.830 2.343   1.00 41.82  ? 229 ASP A CG  1 
ATOM   1827 O  OD1 . ASP A 1 229 ? -54.136 59.566 3.297   1.00 50.41  ? 229 ASP A OD1 1 
ATOM   1828 O  OD2 . ASP A 1 229 ? -55.621 58.658 1.970   1.00 49.84  ? 229 ASP A OD2 1 
ATOM   1829 N  N   . GLU A 1 230 ? -54.086 55.024 1.960   1.00 29.54  ? 230 GLU A N   1 
ATOM   1830 C  CA  . GLU A 1 230 ? -55.014 53.949 2.304   1.00 33.78  ? 230 GLU A CA  1 
ATOM   1831 C  C   . GLU A 1 230 ? -54.480 53.085 3.445   1.00 31.74  ? 230 GLU A C   1 
ATOM   1832 O  O   . GLU A 1 230 ? -55.217 52.741 4.374   1.00 31.34  ? 230 GLU A O   1 
ATOM   1833 C  CB  . GLU A 1 230 ? -55.292 53.084 1.079   1.00 28.98  ? 230 GLU A CB  1 
ATOM   1834 C  CG  . GLU A 1 230 ? -56.140 51.862 1.411   1.00 31.03  ? 230 GLU A CG  1 
ATOM   1835 C  CD  . GLU A 1 230 ? -56.293 50.884 0.240   1.00 37.00  ? 230 GLU A CD  1 
ATOM   1836 O  OE1 . GLU A 1 230 ? -55.350 50.744 -0.575  1.00 37.25  ? 230 GLU A OE1 1 
ATOM   1837 O  OE2 . GLU A 1 230 ? -57.364 50.247 0.141   1.00 34.11  ? 230 GLU A OE2 1 
ATOM   1838 N  N   . ALA A 1 231 ? -53.213 52.681 3.374   1.00 28.06  ? 231 ALA A N   1 
ATOM   1839 C  CA  . ALA A 1 231 ? -52.648 51.888 4.459   1.00 29.33  ? 231 ALA A CA  1 
ATOM   1840 C  C   . ALA A 1 231 ? -52.814 52.604 5.796   1.00 31.61  ? 231 ALA A C   1 
ATOM   1841 O  O   . ALA A 1 231 ? -53.286 52.016 6.776   1.00 32.36  ? 231 ALA A O   1 
ATOM   1842 C  CB  . ALA A 1 231 ? -51.171 51.581 4.192   1.00 26.85  ? 231 ALA A CB  1 
ATOM   1843 N  N   . PHE A 1 232 ? -52.448 53.886 5.848   1.00 24.92  ? 232 PHE A N   1 
ATOM   1844 C  CA  . PHE A 1 232 ? -52.526 54.626 7.106   1.00 29.99  ? 232 PHE A CA  1 
ATOM   1845 C  C   . PHE A 1 232 ? -53.972 54.761 7.587   1.00 30.47  ? 232 PHE A C   1 
ATOM   1846 O  O   . PHE A 1 232 ? -54.249 54.662 8.789   1.00 30.76  ? 232 PHE A O   1 
ATOM   1847 C  CB  . PHE A 1 232 ? -51.875 55.999 6.929   1.00 25.50  ? 232 PHE A CB  1 
ATOM   1848 C  CG  . PHE A 1 232 ? -50.425 55.940 6.503   1.00 31.21  ? 232 PHE A CG  1 
ATOM   1849 C  CD1 . PHE A 1 232 ? -49.689 54.772 6.627   1.00 25.15  ? 232 PHE A CD1 1 
ATOM   1850 C  CD2 . PHE A 1 232 ? -49.794 57.059 5.998   1.00 29.33  ? 232 PHE A CD2 1 
ATOM   1851 C  CE1 . PHE A 1 232 ? -48.368 54.722 6.244   1.00 26.69  ? 232 PHE A CE1 1 
ATOM   1852 C  CE2 . PHE A 1 232 ? -48.465 57.013 5.618   1.00 28.28  ? 232 PHE A CE2 1 
ATOM   1853 C  CZ  . PHE A 1 232 ? -47.755 55.850 5.735   1.00 27.56  ? 232 PHE A CZ  1 
ATOM   1854 N  N   . ARG A 1 233 ? -54.905 54.995 6.658   1.00 27.46  ? 233 ARG A N   1 
ATOM   1855 C  CA  . ARG A 1 233 ? -56.324 55.040 6.998   1.00 25.31  ? 233 ARG A CA  1 
ATOM   1856 C  C   . ARG A 1 233 ? -56.792 53.723 7.606   1.00 27.37  ? 233 ARG A C   1 
ATOM   1857 O  O   . ARG A 1 233 ? -57.560 53.710 8.574   1.00 29.39  ? 233 ARG A O   1 
ATOM   1858 C  CB  . ARG A 1 233 ? -57.141 55.376 5.747   1.00 28.99  ? 233 ARG A CB  1 
ATOM   1859 C  CG  . ARG A 1 233 ? -57.755 56.771 5.768   1.00 41.81  ? 233 ARG A CG  1 
ATOM   1860 C  CD  . ARG A 1 233 ? -58.282 57.233 4.410   1.00 42.63  ? 233 ARG A CD  1 
ATOM   1861 N  NE  . ARG A 1 233 ? -58.961 56.180 3.660   1.00 44.32  ? 233 ARG A NE  1 
ATOM   1862 C  CZ  . ARG A 1 233 ? -60.224 55.799 3.823   1.00 52.16  ? 233 ARG A CZ  1 
ATOM   1863 N  NH1 . ARG A 1 233 ? -61.010 56.348 4.747   1.00 35.34  ? 233 ARG A NH1 1 
ATOM   1864 N  NH2 . ARG A 1 233 ? -60.713 54.842 3.034   1.00 46.01  ? 233 ARG A NH2 1 
ATOM   1865 N  N   . ILE A 1 234 ? -56.363 52.602 7.035   1.00 28.33  ? 234 ILE A N   1 
ATOM   1866 C  CA  . ILE A 1 234 ? -56.701 51.314 7.614   1.00 23.31  ? 234 ILE A CA  1 
ATOM   1867 C  C   . ILE A 1 234 ? -56.140 51.228 9.020   1.00 31.28  ? 234 ILE A C   1 
ATOM   1868 O  O   . ILE A 1 234 ? -56.806 50.756 9.946   1.00 32.64  ? 234 ILE A O   1 
ATOM   1869 C  CB  . ILE A 1 234 ? -56.169 50.188 6.711   1.00 26.13  ? 234 ILE A CB  1 
ATOM   1870 C  CG1 . ILE A 1 234 ? -56.950 50.174 5.394   1.00 22.63  ? 234 ILE A CG1 1 
ATOM   1871 C  CG2 . ILE A 1 234 ? -56.204 48.835 7.448   1.00 23.49  ? 234 ILE A CG2 1 
ATOM   1872 C  CD1 . ILE A 1 234 ? -56.183 49.525 4.247   1.00 28.02  ? 234 ILE A CD1 1 
ATOM   1873 N  N   . GLY A 1 235 ? -54.911 51.711 9.201   1.00 26.74  ? 235 GLY A N   1 
ATOM   1874 C  CA  . GLY A 1 235 ? -54.322 51.735 10.519  1.00 29.37  ? 235 GLY A CA  1 
ATOM   1875 C  C   . GLY A 1 235 ? -55.119 52.575 11.498  1.00 30.21  ? 235 GLY A C   1 
ATOM   1876 O  O   . GLY A 1 235 ? -55.289 52.187 12.654  1.00 30.81  ? 235 GLY A O   1 
ATOM   1877 N  N   . ARG A 1 236 ? -55.613 53.738 11.053  1.00 27.89  ? 236 ARG A N   1 
ATOM   1878 C  CA  . ARG A 1 236 ? -56.369 54.597 11.961  1.00 33.38  ? 236 ARG A CA  1 
ATOM   1879 C  C   . ARG A 1 236 ? -57.753 54.028 12.254  1.00 33.82  ? 236 ARG A C   1 
ATOM   1880 O  O   . ARG A 1 236 ? -58.253 54.191 13.374  1.00 30.58  ? 236 ARG A O   1 
ATOM   1881 C  CB  . ARG A 1 236 ? -56.480 56.017 11.398  1.00 27.63  ? 236 ARG A CB  1 
ATOM   1882 C  CG  . ARG A 1 236 ? -55.158 56.762 11.386  1.00 28.27  ? 236 ARG A CG  1 
ATOM   1883 C  CD  . ARG A 1 236 ? -55.326 58.255 11.188  1.00 28.26  ? 236 ARG A CD  1 
ATOM   1884 N  NE  . ARG A 1 236 ? -56.047 58.585 9.959   1.00 40.37  ? 236 ARG A NE  1 
ATOM   1885 C  CZ  . ARG A 1 236 ? -55.499 58.615 8.749   1.00 38.16  ? 236 ARG A CZ  1 
ATOM   1886 N  NH1 . ARG A 1 236 ? -54.226 58.304 8.558   1.00 31.30  ? 236 ARG A NH1 1 
ATOM   1887 N  NH2 . ARG A 1 236 ? -56.248 58.964 7.702   1.00 30.69  ? 236 ARG A NH2 1 
ATOM   1888 N  N   . HIS A 1 237 ? -58.381 53.351 11.281  1.00 28.88  ? 237 HIS A N   1 
ATOM   1889 C  CA  . HIS A 1 237 ? -59.717 52.811 11.516  1.00 30.15  ? 237 HIS A CA  1 
ATOM   1890 C  C   . HIS A 1 237 ? -59.678 51.748 12.603  1.00 27.11  ? 237 HIS A C   1 
ATOM   1891 O  O   . HIS A 1 237 ? -60.442 51.803 13.572  1.00 29.21  ? 237 HIS A O   1 
ATOM   1892 C  CB  . HIS A 1 237 ? -60.302 52.233 10.232  1.00 25.10  ? 237 HIS A CB  1 
ATOM   1893 C  CG  . HIS A 1 237 ? -61.791 52.070 10.269  1.00 30.49  ? 237 HIS A CG  1 
ATOM   1894 N  ND1 . HIS A 1 237 ? -62.404 50.938 10.762  1.00 32.64  ? 237 HIS A ND1 1 
ATOM   1895 C  CD2 . HIS A 1 237 ? -62.790 52.896 9.873   1.00 24.69  ? 237 HIS A CD2 1 
ATOM   1896 C  CE1 . HIS A 1 237 ? -63.716 51.077 10.677  1.00 24.47  ? 237 HIS A CE1 1 
ATOM   1897 N  NE2 . HIS A 1 237 ? -63.975 52.257 10.144  1.00 32.10  ? 237 HIS A NE2 1 
ATOM   1898 N  N   . GLY A 1 238 ? -58.769 50.784 12.465  1.00 27.49  ? 238 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 238 ? -58.633 49.730 13.448  1.00 36.24  ? 238 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 238 ? -57.890 50.134 14.699  1.00 35.53  ? 238 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 238 ? -58.025 49.464 15.727  1.00 38.01  ? 238 GLY A O   1 
ATOM   1902 N  N   . ASN A 1 239 ? -57.147 51.238 14.646  1.00 29.81  ? 239 ASN A N   1 
ATOM   1903 C  CA  . ASN A 1 239 ? -56.216 51.628 15.704  1.00 37.10  ? 239 ASN A CA  1 
ATOM   1904 C  C   . ASN A 1 239 ? -55.137 50.554 15.890  1.00 34.45  ? 239 ASN A C   1 
ATOM   1905 O  O   . ASN A 1 239 ? -54.941 49.993 16.969  1.00 36.98  ? 239 ASN A O   1 
ATOM   1906 C  CB  . ASN A 1 239 ? -56.969 51.907 17.006  1.00 31.85  ? 239 ASN A CB  1 
ATOM   1907 C  CG  . ASN A 1 239 ? -56.175 52.757 17.970  1.00 42.66  ? 239 ASN A CG  1 
ATOM   1908 O  OD1 . ASN A 1 239 ? -54.989 53.012 17.769  1.00 49.67  ? 239 ASN A OD1 1 
ATOM   1909 N  ND2 . ASN A 1 239 ? -56.828 53.192 19.037  1.00 53.15  ? 239 ASN A ND2 1 
ATOM   1910 N  N   . VAL A 1 240 ? -54.428 50.285 14.802  1.00 29.40  ? 240 VAL A N   1 
ATOM   1911 C  CA  . VAL A 1 240 ? -53.443 49.209 14.754  1.00 30.69  ? 240 VAL A CA  1 
ATOM   1912 C  C   . VAL A 1 240 ? -52.165 49.732 14.107  1.00 25.91  ? 240 VAL A C   1 
ATOM   1913 O  O   . VAL A 1 240 ? -52.223 50.590 13.213  1.00 26.47  ? 240 VAL A O   1 
ATOM   1914 C  CB  . VAL A 1 240 ? -53.998 47.990 13.996  1.00 28.68  ? 240 VAL A CB  1 
ATOM   1915 C  CG1 . VAL A 1 240 ? -55.366 47.633 14.547  1.00 26.50  ? 240 VAL A CG1 1 
ATOM   1916 C  CG2 . VAL A 1 240 ? -54.099 48.274 12.503  1.00 24.21  ? 240 VAL A CG2 1 
ATOM   1917 N  N   . PRO A 1 241 ? -50.998 49.245 14.517  1.00 26.84  ? 241 PRO A N   1 
ATOM   1918 C  CA  . PRO A 1 241 ? -49.756 49.682 13.875  1.00 24.60  ? 241 PRO A CA  1 
ATOM   1919 C  C   . PRO A 1 241 ? -49.626 49.127 12.460  1.00 31.53  ? 241 PRO A C   1 
ATOM   1920 O  O   . PRO A 1 241 ? -50.106 48.033 12.140  1.00 24.59  ? 241 PRO A O   1 
ATOM   1921 C  CB  . PRO A 1 241 ? -48.667 49.126 14.797  1.00 26.90  ? 241 PRO A CB  1 
ATOM   1922 C  CG  . PRO A 1 241 ? -49.315 47.949 15.479  1.00 30.48  ? 241 PRO A CG  1 
ATOM   1923 C  CD  . PRO A 1 241 ? -50.775 48.261 15.596  1.00 21.41  ? 241 PRO A CD  1 
ATOM   1924 N  N   . VAL A 1 242 ? -48.954 49.901 11.608  1.00 27.01  ? 242 VAL A N   1 
ATOM   1925 C  CA  . VAL A 1 242 ? -48.801 49.577 10.195  1.00 26.14  ? 242 VAL A CA  1 
ATOM   1926 C  C   . VAL A 1 242 ? -47.328 49.355 9.894   1.00 29.55  ? 242 VAL A C   1 
ATOM   1927 O  O   . VAL A 1 242 ? -46.469 50.104 10.374  1.00 26.53  ? 242 VAL A O   1 
ATOM   1928 C  CB  . VAL A 1 242 ? -49.361 50.699 9.300   1.00 28.14  ? 242 VAL A CB  1 
ATOM   1929 C  CG1 . VAL A 1 242 ? -49.122 50.368 7.818   1.00 21.74  ? 242 VAL A CG1 1 
ATOM   1930 C  CG2 . VAL A 1 242 ? -50.819 50.922 9.593   1.00 25.81  ? 242 VAL A CG2 1 
ATOM   1931 N  N   . VAL A 1 243 ? -47.036 48.334 9.091   1.00 24.83  ? 243 VAL A N   1 
ATOM   1932 C  CA  . VAL A 1 243 ? -45.715 48.152 8.497   1.00 25.65  ? 243 VAL A CA  1 
ATOM   1933 C  C   . VAL A 1 243 ? -45.891 48.115 6.987   1.00 23.27  ? 243 VAL A C   1 
ATOM   1934 O  O   . VAL A 1 243 ? -46.633 47.274 6.463   1.00 25.93  ? 243 VAL A O   1 
ATOM   1935 C  CB  . VAL A 1 243 ? -45.009 46.875 8.988   1.00 26.14  ? 243 VAL A CB  1 
ATOM   1936 C  CG1 . VAL A 1 243 ? -43.647 46.757 8.300   1.00 26.46  ? 243 VAL A CG1 1 
ATOM   1937 C  CG2 . VAL A 1 243 ? -44.835 46.876 10.510  1.00 23.77  ? 243 VAL A CG2 1 
ATOM   1938 N  N   . VAL A 1 244 ? -45.214 49.017 6.288   1.00 27.21  ? 244 VAL A N   1 
ATOM   1939 C  CA  . VAL A 1 244 ? -45.209 49.013 4.828   1.00 22.59  ? 244 VAL A CA  1 
ATOM   1940 C  C   . VAL A 1 244 ? -44.104 48.073 4.370   1.00 26.04  ? 244 VAL A C   1 
ATOM   1941 O  O   . VAL A 1 244 ? -42.920 48.340 4.594   1.00 28.39  ? 244 VAL A O   1 
ATOM   1942 C  CB  . VAL A 1 244 ? -45.013 50.421 4.259   1.00 28.97  ? 244 VAL A CB  1 
ATOM   1943 C  CG1 . VAL A 1 244 ? -44.865 50.361 2.737   1.00 20.48  ? 244 VAL A CG1 1 
ATOM   1944 C  CG2 . VAL A 1 244 ? -46.206 51.326 4.669   1.00 20.34  ? 244 VAL A CG2 1 
ATOM   1945 N  N   . SER A 1 245 ? -44.497 46.973 3.730   1.00 24.88  ? 245 SER A N   1 
ATOM   1946 C  CA  . SER A 1 245 ? -43.551 45.955 3.301   1.00 26.74  ? 245 SER A CA  1 
ATOM   1947 C  C   . SER A 1 245 ? -42.708 46.446 2.129   1.00 28.44  ? 245 SER A C   1 
ATOM   1948 O  O   . SER A 1 245 ? -43.159 47.232 1.294   1.00 26.30  ? 245 SER A O   1 
ATOM   1949 C  CB  . SER A 1 245 ? -44.278 44.670 2.893   1.00 24.87  ? 245 SER A CB  1 
ATOM   1950 O  OG  . SER A 1 245 ? -45.137 44.209 3.915   1.00 28.67  ? 245 SER A OG  1 
ATOM   1951 N  N   . HIS A 1 246 ? -41.476 45.935 2.067   1.00 31.19  ? 246 HIS A N   1 
ATOM   1952 C  CA  . HIS A 1 246 ? -40.491 46.261 1.040   1.00 30.06  ? 246 HIS A CA  1 
ATOM   1953 C  C   . HIS A 1 246 ? -40.748 47.625 0.398   1.00 28.69  ? 246 HIS A C   1 
ATOM   1954 O  O   . HIS A 1 246 ? -40.940 47.728 -0.822  1.00 29.57  ? 246 HIS A O   1 
ATOM   1955 C  CB  . HIS A 1 246 ? -40.432 45.144 -0.024  1.00 27.58  ? 246 HIS A CB  1 
ATOM   1956 C  CG  . HIS A 1 246 ? -41.768 44.715 -0.568  1.00 31.24  ? 246 HIS A CG  1 
ATOM   1957 N  ND1 . HIS A 1 246 ? -42.643 45.584 -1.184  1.00 27.40  ? 246 HIS A ND1 1 
ATOM   1958 C  CD2 . HIS A 1 246 ? -42.352 43.491 -0.630  1.00 31.60  ? 246 HIS A CD2 1 
ATOM   1959 C  CE1 . HIS A 1 246 ? -43.712 44.917 -1.589  1.00 29.16  ? 246 HIS A CE1 1 
ATOM   1960 N  NE2 . HIS A 1 246 ? -43.559 43.646 -1.268  1.00 29.22  ? 246 HIS A NE2 1 
ATOM   1961 N  N   . HIS A 1 247 ? -40.732 48.681 1.213   1.00 29.34  ? 247 HIS A N   1 
ATOM   1962 C  CA  . HIS A 1 247 ? -40.999 50.016 0.698   1.00 30.86  ? 247 HIS A CA  1 
ATOM   1963 C  C   . HIS A 1 247 ? -39.974 50.393 -0.362  1.00 32.04  ? 247 HIS A C   1 
ATOM   1964 O  O   . HIS A 1 247 ? -38.764 50.291 -0.137  1.00 28.75  ? 247 HIS A O   1 
ATOM   1965 C  CB  . HIS A 1 247 ? -40.988 51.043 1.826   1.00 27.13  ? 247 HIS A CB  1 
ATOM   1966 C  CG  . HIS A 1 247 ? -41.366 52.419 1.372   1.00 34.32  ? 247 HIS A CG  1 
ATOM   1967 N  ND1 . HIS A 1 247 ? -42.438 52.655 0.537   1.00 31.77  ? 247 HIS A ND1 1 
ATOM   1968 C  CD2 . HIS A 1 247 ? -40.805 53.628 1.615   1.00 27.01  ? 247 HIS A CD2 1 
ATOM   1969 C  CE1 . HIS A 1 247 ? -42.526 53.951 0.294   1.00 28.62  ? 247 HIS A CE1 1 
ATOM   1970 N  NE2 . HIS A 1 247 ? -41.548 54.563 0.939   1.00 31.40  ? 247 HIS A NE2 1 
ATOM   1971 N  N   . LYS A 1 248 ? -40.475 50.829 -1.518  1.00 34.76  ? 248 LYS A N   1 
ATOM   1972 C  CA  . LYS A 1 248 ? -39.668 51.216 -2.665  1.00 28.47  ? 248 LYS A CA  1 
ATOM   1973 C  C   . LYS A 1 248 ? -40.494 52.167 -3.515  1.00 29.63  ? 248 LYS A C   1 
ATOM   1974 O  O   . LYS A 1 248 ? -41.724 52.206 -3.410  1.00 34.07  ? 248 LYS A O   1 
ATOM   1975 C  CB  . LYS A 1 248 ? -39.262 50.005 -3.513  1.00 31.87  ? 248 LYS A CB  1 
ATOM   1976 C  CG  . LYS A 1 248 ? -40.474 49.274 -4.111  1.00 29.91  ? 248 LYS A CG  1 
ATOM   1977 C  CD  . LYS A 1 248 ? -40.096 48.192 -5.104  1.00 31.97  ? 248 LYS A CD  1 
ATOM   1978 C  CE  . LYS A 1 248 ? -39.601 46.931 -4.425  1.00 30.75  ? 248 LYS A CE  1 
ATOM   1979 N  NZ  . LYS A 1 248 ? -40.676 46.325 -3.577  1.00 37.08  ? 248 LYS A NZ  1 
ATOM   1980 N  N   . CYS A 1 249 ? -39.806 52.930 -4.362  1.00 28.97  ? 249 CYS A N   1 
ATOM   1981 C  CA  . CYS A 1 249 ? -40.431 53.689 -5.450  1.00 28.92  ? 249 CYS A CA  1 
ATOM   1982 C  C   . CYS A 1 249 ? -39.973 53.067 -6.769  1.00 34.01  ? 249 CYS A C   1 
ATOM   1983 O  O   . CYS A 1 249 ? -38.867 53.344 -7.244  1.00 35.18  ? 249 CYS A O   1 
ATOM   1984 C  CB  . CYS A 1 249 ? -40.062 55.167 -5.380  1.00 33.65  ? 249 CYS A CB  1 
ATOM   1985 S  SG  . CYS A 1 249 ? -40.993 56.040 -4.118  1.00 34.43  ? 249 CYS A SG  1 
ATOM   1986 N  N   . ALA A 1 250 ? -40.826 52.229 -7.355  1.00 30.95  ? 250 ALA A N   1 
ATOM   1987 C  CA  . ALA A 1 250 ? -40.459 51.443 -8.522  1.00 35.69  ? 250 ALA A CA  1 
ATOM   1988 C  C   . ALA A 1 250 ? -40.814 52.175 -9.815  1.00 37.95  ? 250 ALA A C   1 
ATOM   1989 O  O   . ALA A 1 250 ? -41.795 52.926 -9.886  1.00 32.84  ? 250 ALA A O   1 
ATOM   1990 C  CB  . ALA A 1 250 ? -41.147 50.074 -8.474  1.00 31.04  ? 250 ALA A CB  1 
ATOM   1991 N  N   . GLY A 1 251 ? -40.002 51.947 -10.845 1.00 34.85  ? 251 GLY A N   1 
ATOM   1992 C  CA  . GLY A 1 251 ? -40.240 52.583 -12.130 1.00 31.43  ? 251 GLY A CA  1 
ATOM   1993 C  C   . GLY A 1 251 ? -39.493 53.891 -12.291 1.00 34.48  ? 251 GLY A C   1 
ATOM   1994 O  O   . GLY A 1 251 ? -39.426 54.696 -11.358 1.00 33.54  ? 251 GLY A O   1 
ATOM   1995 N  N   . ALA A 1 252 ? -38.924 54.104 -13.478 1.00 31.58  ? 252 ALA A N   1 
ATOM   1996 C  CA  . ALA A 1 252 ? -38.087 55.274 -13.722 1.00 36.08  ? 252 ALA A CA  1 
ATOM   1997 C  C   . ALA A 1 252 ? -38.806 56.569 -13.375 1.00 40.81  ? 252 ALA A C   1 
ATOM   1998 O  O   . ALA A 1 252 ? -38.187 57.510 -12.869 1.00 41.16  ? 252 ALA A O   1 
ATOM   1999 C  CB  . ALA A 1 252 ? -37.629 55.299 -15.186 1.00 33.81  ? 252 ALA A CB  1 
ATOM   2000 N  N   . LYS A 1 253 ? -40.116 56.639 -13.648 1.00 42.83  ? 253 LYS A N   1 
ATOM   2001 C  CA  A LYS A 1 253 ? -40.894 57.846 -13.382 0.54 39.63  ? 253 LYS A CA  1 
ATOM   2002 C  CA  B LYS A 1 253 ? -40.873 57.859 -13.382 0.46 39.63  ? 253 LYS A CA  1 
ATOM   2003 C  C   . LYS A 1 253 ? -40.993 58.172 -11.893 1.00 38.91  ? 253 LYS A C   1 
ATOM   2004 O  O   . LYS A 1 253 ? -41.307 59.311 -11.532 1.00 36.94  ? 253 LYS A O   1 
ATOM   2005 C  CB  A LYS A 1 253 ? -42.297 57.687 -13.971 0.54 41.88  ? 253 LYS A CB  1 
ATOM   2006 C  CB  B LYS A 1 253 ? -42.268 57.757 -14.007 0.46 41.88  ? 253 LYS A CB  1 
ATOM   2007 C  CG  A LYS A 1 253 ? -43.196 58.896 -13.808 0.54 44.99  ? 253 LYS A CG  1 
ATOM   2008 C  CG  B LYS A 1 253 ? -42.325 58.140 -15.483 0.46 41.39  ? 253 LYS A CG  1 
ATOM   2009 C  CD  A LYS A 1 253 ? -44.607 58.464 -13.420 0.54 52.92  ? 253 LYS A CD  1 
ATOM   2010 C  CD  B LYS A 1 253 ? -43.597 57.619 -16.143 0.46 45.92  ? 253 LYS A CD  1 
ATOM   2011 C  CE  A LYS A 1 253 ? -45.119 57.347 -14.320 0.54 50.07  ? 253 LYS A CE  1 
ATOM   2012 C  CE  B LYS A 1 253 ? -44.835 57.947 -15.318 0.46 51.03  ? 253 LYS A CE  1 
ATOM   2013 N  NZ  A LYS A 1 253 ? -46.427 56.805 -13.849 0.54 49.99  ? 253 LYS A NZ  1 
ATOM   2014 N  NZ  B LYS A 1 253 ? -45.007 59.413 -15.098 0.46 49.08  ? 253 LYS A NZ  1 
ATOM   2015 N  N   . ASN A 1 254 ? -40.739 57.209 -11.016 1.00 32.60  ? 254 ASN A N   1 
ATOM   2016 C  CA  . ASN A 1 254 ? -40.869 57.442 -9.585  1.00 33.79  ? 254 ASN A CA  1 
ATOM   2017 C  C   . ASN A 1 254 ? -39.527 57.537 -8.871  1.00 33.50  ? 254 ASN A C   1 
ATOM   2018 O  O   . ASN A 1 254 ? -39.489 57.606 -7.638  1.00 35.41  ? 254 ASN A O   1 
ATOM   2019 C  CB  . ASN A 1 254 ? -41.740 56.351 -8.977  1.00 28.96  ? 254 ASN A CB  1 
ATOM   2020 C  CG  . ASN A 1 254 ? -43.052 56.212 -9.715  1.00 39.30  ? 254 ASN A CG  1 
ATOM   2021 O  OD1 . ASN A 1 254 ? -43.893 57.107 -9.664  1.00 32.90  ? 254 ASN A OD1 1 
ATOM   2022 N  ND2 . ASN A 1 254 ? -43.219 55.110 -10.436 1.00 35.72  ? 254 ASN A ND2 1 
ATOM   2023 N  N   . TRP A 1 255 ? -38.430 57.566 -9.614  1.00 34.33  ? 255 TRP A N   1 
ATOM   2024 C  CA  . TRP A 1 255 ? -37.122 57.675 -8.994  1.00 39.87  ? 255 TRP A CA  1 
ATOM   2025 C  C   . TRP A 1 255 ? -36.986 59.014 -8.272  1.00 38.04  ? 255 TRP A C   1 
ATOM   2026 O  O   . TRP A 1 255 ? -37.380 60.062 -8.791  1.00 35.79  ? 255 TRP A O   1 
ATOM   2027 C  CB  . TRP A 1 255 ? -36.044 57.500 -10.063 1.00 30.98  ? 255 TRP A CB  1 
ATOM   2028 C  CG  . TRP A 1 255 ? -35.958 56.085 -10.530 1.00 32.85  ? 255 TRP A CG  1 
ATOM   2029 C  CD1 . TRP A 1 255 ? -36.597 55.012 -9.987  1.00 32.82  ? 255 TRP A CD1 1 
ATOM   2030 C  CD2 . TRP A 1 255 ? -35.192 55.583 -11.628 1.00 33.23  ? 255 TRP A CD2 1 
ATOM   2031 N  NE1 . TRP A 1 255 ? -36.281 53.868 -10.676 1.00 29.64  ? 255 TRP A NE1 1 
ATOM   2032 C  CE2 . TRP A 1 255 ? -35.416 54.189 -11.687 1.00 33.63  ? 255 TRP A CE2 1 
ATOM   2033 C  CE3 . TRP A 1 255 ? -34.342 56.174 -12.572 1.00 33.43  ? 255 TRP A CE3 1 
ATOM   2034 C  CZ2 . TRP A 1 255 ? -34.811 53.373 -12.648 1.00 34.98  ? 255 TRP A CZ2 1 
ATOM   2035 C  CZ3 . TRP A 1 255 ? -33.747 55.364 -13.530 1.00 42.72  ? 255 TRP A CZ3 1 
ATOM   2036 C  CH2 . TRP A 1 255 ? -33.984 53.978 -13.558 1.00 38.47  ? 255 TRP A CH2 1 
ATOM   2037 N  N   . GLY A 1 256 ? -36.434 58.972 -7.063  1.00 39.92  ? 256 GLY A N   1 
ATOM   2038 C  CA  . GLY A 1 256 ? -36.316 60.148 -6.239  1.00 35.63  ? 256 GLY A CA  1 
ATOM   2039 C  C   . GLY A 1 256 ? -37.497 60.408 -5.335  1.00 37.39  ? 256 GLY A C   1 
ATOM   2040 O  O   . GLY A 1 256 ? -37.376 61.212 -4.404  1.00 37.14  ? 256 GLY A O   1 
ATOM   2041 N  N   . ARG A 1 257 ? -38.624 59.732 -5.551  1.00 33.45  ? 257 ARG A N   1 
ATOM   2042 C  CA  . ARG A 1 257 ? -39.843 60.078 -4.835  1.00 33.21  ? 257 ARG A CA  1 
ATOM   2043 C  C   . ARG A 1 257 ? -39.900 59.530 -3.414  1.00 36.18  ? 257 ARG A C   1 
ATOM   2044 O  O   . ARG A 1 257 ? -40.862 59.841 -2.701  1.00 30.70  ? 257 ARG A O   1 
ATOM   2045 C  CB  . ARG A 1 257 ? -41.071 59.617 -5.621  1.00 32.47  ? 257 ARG A CB  1 
ATOM   2046 C  CG  . ARG A 1 257 ? -41.215 60.337 -6.973  1.00 37.44  ? 257 ARG A CG  1 
ATOM   2047 C  CD  . ARG A 1 257 ? -42.519 59.952 -7.687  1.00 37.33  ? 257 ARG A CD  1 
ATOM   2048 N  NE  . ARG A 1 257 ? -43.680 60.493 -6.989  1.00 37.25  ? 257 ARG A NE  1 
ATOM   2049 C  CZ  . ARG A 1 257 ? -44.864 59.901 -6.908  1.00 41.67  ? 257 ARG A CZ  1 
ATOM   2050 N  NH1 . ARG A 1 257 ? -45.091 58.719 -7.462  1.00 36.43  ? 257 ARG A NH1 1 
ATOM   2051 N  NH2 . ARG A 1 257 ? -45.845 60.504 -6.240  1.00 39.59  ? 257 ARG A NH2 1 
ATOM   2052 N  N   . THR A 1 258 ? -38.914 58.740 -2.963  1.00 31.71  ? 258 THR A N   1 
ATOM   2053 C  CA  . THR A 1 258 ? -38.893 58.432 -1.533  1.00 32.46  ? 258 THR A CA  1 
ATOM   2054 C  C   . THR A 1 258 ? -38.785 59.702 -0.703  1.00 33.79  ? 258 THR A C   1 
ATOM   2055 O  O   . THR A 1 258 ? -39.188 59.699 0.466   1.00 40.09  ? 258 THR A O   1 
ATOM   2056 C  CB  . THR A 1 258 ? -37.755 57.474 -1.149  1.00 28.06  ? 258 THR A CB  1 
ATOM   2057 O  OG1 . THR A 1 258 ? -36.484 58.022 -1.531  1.00 32.41  ? 258 THR A OG1 1 
ATOM   2058 C  CG2 . THR A 1 258 ? -37.960 56.096 -1.782  1.00 26.05  ? 258 THR A CG2 1 
ATOM   2059 N  N   . LYS A 1 259 ? -38.262 60.792 -1.281  1.00 33.51  ? 259 LYS A N   1 
ATOM   2060 C  CA  . LYS A 1 259 ? -38.331 62.080 -0.601  1.00 35.03  ? 259 LYS A CA  1 
ATOM   2061 C  C   . LYS A 1 259 ? -39.774 62.445 -0.276  1.00 37.03  ? 259 LYS A C   1 
ATOM   2062 O  O   . LYS A 1 259 ? -40.048 63.056 0.764   1.00 40.47  ? 259 LYS A O   1 
ATOM   2063 C  CB  . LYS A 1 259 ? -37.687 63.173 -1.451  1.00 31.75  ? 259 LYS A CB  1 
ATOM   2064 C  CG  . LYS A 1 259 ? -36.210 62.965 -1.719  1.00 39.77  ? 259 LYS A CG  1 
ATOM   2065 C  CD  . LYS A 1 259 ? -35.569 64.227 -2.282  1.00 42.15  ? 259 LYS A CD  1 
ATOM   2066 C  CE  . LYS A 1 259 ? -34.804 63.952 -3.572  1.00 61.33  ? 259 LYS A CE  1 
ATOM   2067 N  NZ  . LYS A 1 259 ? -35.721 63.683 -4.716  1.00 68.59  ? 259 LYS A NZ  1 
ATOM   2068 N  N   . GLU A 1 260 ? -40.711 62.072 -1.153  1.00 33.66  ? 260 GLU A N   1 
ATOM   2069 C  CA  . GLU A 1 260 ? -42.128 62.332 -0.907  1.00 29.47  ? 260 GLU A CA  1 
ATOM   2070 C  C   . GLU A 1 260 ? -42.722 61.318 0.057   1.00 32.75  ? 260 GLU A C   1 
ATOM   2071 O  O   . GLU A 1 260 ? -43.418 61.687 1.007   1.00 39.57  ? 260 GLU A O   1 
ATOM   2072 C  CB  . GLU A 1 260 ? -42.909 62.323 -2.225  1.00 36.29  ? 260 GLU A CB  1 
ATOM   2073 C  CG  . GLU A 1 260 ? -42.454 63.394 -3.224  1.00 44.29  ? 260 GLU A CG  1 
ATOM   2074 C  CD  . GLU A 1 260 ? -43.101 63.246 -4.596  1.00 46.75  ? 260 GLU A CD  1 
ATOM   2075 O  OE1 . GLU A 1 260 ? -44.294 62.869 -4.669  1.00 47.48  ? 260 GLU A OE1 1 
ATOM   2076 O  OE2 . GLU A 1 260 ? -42.410 63.508 -5.606  1.00 57.55  ? 260 GLU A OE2 1 
ATOM   2077 N  N   . THR A 1 261 ? -42.463 60.032 -0.172  1.00 32.20  ? 261 THR A N   1 
ATOM   2078 C  CA  . THR A 1 261 ? -43.071 59.010 0.666   1.00 34.90  ? 261 THR A CA  1 
ATOM   2079 C  C   . THR A 1 261 ? -42.597 59.139 2.109   1.00 30.94  ? 261 THR A C   1 
ATOM   2080 O  O   . THR A 1 261 ? -43.402 59.102 3.047   1.00 26.96  ? 261 THR A O   1 
ATOM   2081 C  CB  . THR A 1 261 ? -42.765 57.617 0.112   1.00 29.42  ? 261 THR A CB  1 
ATOM   2082 O  OG1 . THR A 1 261 ? -41.366 57.345 0.258   1.00 31.77  ? 261 THR A OG1 1 
ATOM   2083 C  CG2 . THR A 1 261 ? -43.127 57.551 -1.362  1.00 31.20  ? 261 THR A CG2 1 
ATOM   2084 N  N   . LEU A 1 262 ? -41.289 59.292 2.311   1.00 29.25  ? 262 LEU A N   1 
ATOM   2085 C  CA  . LEU A 1 262 ? -40.797 59.380 3.681   1.00 31.83  ? 262 LEU A CA  1 
ATOM   2086 C  C   . LEU A 1 262 ? -41.266 60.664 4.354   1.00 31.73  ? 262 LEU A C   1 
ATOM   2087 O  O   . LEU A 1 262 ? -41.458 60.691 5.573   1.00 34.41  ? 262 LEU A O   1 
ATOM   2088 C  CB  . LEU A 1 262 ? -39.278 59.269 3.698   1.00 27.75  ? 262 LEU A CB  1 
ATOM   2089 C  CG  . LEU A 1 262 ? -38.759 57.937 3.158   1.00 31.76  ? 262 LEU A CG  1 
ATOM   2090 C  CD1 . LEU A 1 262 ? -37.242 57.895 3.138   1.00 29.35  ? 262 LEU A CD1 1 
ATOM   2091 C  CD2 . LEU A 1 262 ? -39.300 56.806 3.988   1.00 23.89  ? 262 LEU A CD2 1 
ATOM   2092 N  N   . ALA A 1 263 ? -41.464 61.731 3.578   1.00 31.98  ? 263 ALA A N   1 
ATOM   2093 C  CA  . ALA A 1 263 ? -42.092 62.929 4.118   1.00 28.76  ? 263 ALA A CA  1 
ATOM   2094 C  C   . ALA A 1 263 ? -43.508 62.632 4.576   1.00 32.29  ? 263 ALA A C   1 
ATOM   2095 O  O   . ALA A 1 263 ? -43.955 63.135 5.611   1.00 33.07  ? 263 ALA A O   1 
ATOM   2096 C  CB  . ALA A 1 263 ? -42.097 64.039 3.071   1.00 31.48  ? 263 ALA A CB  1 
ATOM   2097 N  N   . PHE A 1 264 ? -44.233 61.822 3.806   1.00 31.30  ? 264 PHE A N   1 
ATOM   2098 C  CA  . PHE A 1 264 ? -45.564 61.419 4.224   1.00 30.72  ? 264 PHE A CA  1 
ATOM   2099 C  C   . PHE A 1 264 ? -45.503 60.608 5.510   1.00 29.58  ? 264 PHE A C   1 
ATOM   2100 O  O   . PHE A 1 264 ? -46.339 60.789 6.400   1.00 31.87  ? 264 PHE A O   1 
ATOM   2101 C  CB  . PHE A 1 264 ? -46.240 60.621 3.108   1.00 33.08  ? 264 PHE A CB  1 
ATOM   2102 C  CG  . PHE A 1 264 ? -47.738 60.505 3.268   1.00 35.28  ? 264 PHE A CG  1 
ATOM   2103 C  CD1 . PHE A 1 264 ? -48.455 61.503 3.900   1.00 31.24  ? 264 PHE A CD1 1 
ATOM   2104 C  CD2 . PHE A 1 264 ? -48.423 59.397 2.786   1.00 34.39  ? 264 PHE A CD2 1 
ATOM   2105 C  CE1 . PHE A 1 264 ? -49.820 61.399 4.054   1.00 36.71  ? 264 PHE A CE1 1 
ATOM   2106 C  CE2 . PHE A 1 264 ? -49.785 59.288 2.931   1.00 31.96  ? 264 PHE A CE2 1 
ATOM   2107 C  CZ  . PHE A 1 264 ? -50.488 60.290 3.575   1.00 32.70  ? 264 PHE A CZ  1 
ATOM   2108 N  N   . PHE A 1 265 ? -44.518 59.707 5.626   1.00 27.35  ? 265 PHE A N   1 
ATOM   2109 C  CA  . PHE A 1 265 ? -44.347 58.941 6.860   1.00 31.58  ? 265 PHE A CA  1 
ATOM   2110 C  C   . PHE A 1 265 ? -44.124 59.869 8.045   1.00 33.35  ? 265 PHE A C   1 
ATOM   2111 O  O   . PHE A 1 265 ? -44.755 59.716 9.098   1.00 35.54  ? 265 PHE A O   1 
ATOM   2112 C  CB  . PHE A 1 265 ? -43.160 57.980 6.744   1.00 28.42  ? 265 PHE A CB  1 
ATOM   2113 C  CG  . PHE A 1 265 ? -43.468 56.661 6.078   1.00 29.05  ? 265 PHE A CG  1 
ATOM   2114 C  CD1 . PHE A 1 265 ? -43.533 56.555 4.691   1.00 33.83  ? 265 PHE A CD1 1 
ATOM   2115 C  CD2 . PHE A 1 265 ? -43.620 55.513 6.834   1.00 32.93  ? 265 PHE A CD2 1 
ATOM   2116 C  CE1 . PHE A 1 265 ? -43.777 55.322 4.075   1.00 34.26  ? 265 PHE A CE1 1 
ATOM   2117 C  CE2 . PHE A 1 265 ? -43.861 54.286 6.227   1.00 33.09  ? 265 PHE A CE2 1 
ATOM   2118 C  CZ  . PHE A 1 265 ? -43.939 54.192 4.843   1.00 29.62  ? 265 PHE A CZ  1 
ATOM   2119 N  N   . ASP A 1 266 ? -43.179 60.805 7.901   1.00 32.90  ? 266 ASP A N   1 
ATOM   2120 C  CA  . ASP A 1 266 ? -42.901 61.786 8.951   1.00 35.67  ? 266 ASP A CA  1 
ATOM   2121 C  C   . ASP A 1 266 ? -44.180 62.453 9.425   1.00 35.31  ? 266 ASP A C   1 
ATOM   2122 O  O   . ASP A 1 266 ? -44.447 62.542 10.628  1.00 40.88  ? 266 ASP A O   1 
ATOM   2123 C  CB  . ASP A 1 266 ? -41.928 62.856 8.433   1.00 31.71  ? 266 ASP A CB  1 
ATOM   2124 C  CG  . ASP A 1 266 ? -40.474 62.403 8.461   1.00 42.93  ? 266 ASP A CG  1 
ATOM   2125 O  OD1 . ASP A 1 266 ? -40.169 61.382 9.126   1.00 39.73  ? 266 ASP A OD1 1 
ATOM   2126 O  OD2 . ASP A 1 266 ? -39.635 63.076 7.813   1.00 42.33  ? 266 ASP A OD2 1 
ATOM   2127 N  N   . GLU A 1 267 ? -44.973 62.949 8.477   1.00 36.30  ? 267 GLU A N   1 
ATOM   2128 C  CA  . GLU A 1 267 ? -46.206 63.644 8.813   1.00 40.97  ? 267 GLU A CA  1 
ATOM   2129 C  C   . GLU A 1 267 ? -47.165 62.734 9.581   1.00 38.06  ? 267 GLU A C   1 
ATOM   2130 O  O   . GLU A 1 267 ? -47.733 63.132 10.605  1.00 38.42  ? 267 GLU A O   1 
ATOM   2131 C  CB  . GLU A 1 267 ? -46.851 64.165 7.526   1.00 34.39  ? 267 GLU A CB  1 
ATOM   2132 C  CG  . GLU A 1 267 ? -48.040 65.089 7.753   1.00 57.62  ? 267 GLU A CG  1 
ATOM   2133 C  CD  . GLU A 1 267 ? -48.899 65.248 6.513   1.00 63.52  ? 267 GLU A CD  1 
ATOM   2134 O  OE1 . GLU A 1 267 ? -48.383 65.050 5.390   1.00 63.50  ? 267 GLU A OE1 1 
ATOM   2135 O  OE2 . GLU A 1 267 ? -50.096 65.563 6.665   1.00 77.66  ? 267 GLU A OE2 1 
ATOM   2136 N  N   . MET A 1 268 ? -47.361 61.505 9.098   1.00 34.10  ? 268 MET A N   1 
ATOM   2137 C  CA  . MET A 1 268 ? -48.403 60.648 9.651   1.00 31.80  ? 268 MET A CA  1 
ATOM   2138 C  C   . MET A 1 268 ? -47.954 59.934 10.914  1.00 34.89  ? 268 MET A C   1 
ATOM   2139 O  O   . MET A 1 268 ? -48.785 59.629 11.773  1.00 33.55  ? 268 MET A O   1 
ATOM   2140 C  CB  . MET A 1 268 ? -48.864 59.631 8.605   1.00 32.55  ? 268 MET A CB  1 
ATOM   2141 C  CG  . MET A 1 268 ? -49.536 60.280 7.384   1.00 41.10  ? 268 MET A CG  1 
ATOM   2142 S  SD  . MET A 1 268 ? -50.714 61.572 7.836   1.00 41.51  ? 268 MET A SD  1 
ATOM   2143 C  CE  . MET A 1 268 ? -51.955 60.577 8.659   1.00 39.45  ? 268 MET A CE  1 
ATOM   2144 N  N   . ARG A 1 269 ? -46.658 59.671 11.066  1.00 37.18  ? 269 ARG A N   1 
ATOM   2145 C  CA  . ARG A 1 269 ? -46.213 59.077 12.319  1.00 30.35  ? 269 ARG A CA  1 
ATOM   2146 C  C   . ARG A 1 269 ? -46.424 59.999 13.516  1.00 39.46  ? 269 ARG A C   1 
ATOM   2147 O  O   . ARG A 1 269 ? -46.275 59.546 14.656  1.00 36.30  ? 269 ARG A O   1 
ATOM   2148 C  CB  . ARG A 1 269 ? -44.746 58.672 12.213  1.00 28.03  ? 269 ARG A CB  1 
ATOM   2149 C  CG  . ARG A 1 269 ? -44.513 57.527 11.244  1.00 38.37  ? 269 ARG A CG  1 
ATOM   2150 C  CD  . ARG A 1 269 ? -43.035 57.199 11.087  1.00 36.27  ? 269 ARG A CD  1 
ATOM   2151 N  NE  . ARG A 1 269 ? -42.391 56.938 12.368  1.00 38.53  ? 269 ARG A NE  1 
ATOM   2152 C  CZ  . ARG A 1 269 ? -41.290 57.541 12.789  1.00 38.83  ? 269 ARG A CZ  1 
ATOM   2153 N  NH1 . ARG A 1 269 ? -40.634 58.394 12.018  1.00 39.78  ? 269 ARG A NH1 1 
ATOM   2154 N  NH2 . ARG A 1 269 ? -40.830 57.277 14.013  1.00 40.86  ? 269 ARG A NH2 1 
ATOM   2155 N  N   . GLN A 1 270 ? -46.775 61.272 13.299  1.00 33.54  ? 270 GLN A N   1 
ATOM   2156 C  CA  . GLN A 1 270 ? -47.094 62.138 14.425  1.00 40.29  ? 270 GLN A CA  1 
ATOM   2157 C  C   . GLN A 1 270 ? -48.437 61.798 15.061  1.00 40.80  ? 270 GLN A C   1 
ATOM   2158 O  O   . GLN A 1 270 ? -48.675 62.181 16.206  1.00 42.18  ? 270 GLN A O   1 
ATOM   2159 C  CB  . GLN A 1 270 ? -47.066 63.602 13.986  1.00 39.81  ? 270 GLN A CB  1 
ATOM   2160 C  CG  . GLN A 1 270 ? -45.652 64.146 13.879  1.00 44.76  ? 270 GLN A CG  1 
ATOM   2161 C  CD  . GLN A 1 270 ? -45.582 65.428 13.102  1.00 66.20  ? 270 GLN A CD  1 
ATOM   2162 O  OE1 . GLN A 1 270 ? -46.468 65.728 12.300  1.00 68.56  ? 270 GLN A OE1 1 
ATOM   2163 N  NE2 . GLN A 1 270 ? -44.526 66.202 13.332  1.00 83.03  ? 270 GLN A NE2 1 
ATOM   2164 N  N   . GLN A 1 271 ? -49.312 61.079 14.363  1.00 35.49  ? 271 GLN A N   1 
ATOM   2165 C  CA  A GLN A 1 271 ? -50.603 60.722 14.924  0.50 35.76  ? 271 GLN A CA  1 
ATOM   2166 C  CA  B GLN A 1 271 ? -50.615 60.725 14.898  0.50 35.77  ? 271 GLN A CA  1 
ATOM   2167 C  C   . GLN A 1 271 ? -50.855 59.224 15.003  1.00 33.96  ? 271 GLN A C   1 
ATOM   2168 O  O   . GLN A 1 271 ? -51.839 58.826 15.624  1.00 37.39  ? 271 GLN A O   1 
ATOM   2169 C  CB  A GLN A 1 271 ? -51.748 61.388 14.134  0.50 35.03  ? 271 GLN A CB  1 
ATOM   2170 C  CB  B GLN A 1 271 ? -51.731 61.365 14.048  0.50 35.04  ? 271 GLN A CB  1 
ATOM   2171 C  CG  A GLN A 1 271 ? -51.868 60.996 12.664  0.50 36.79  ? 271 GLN A CG  1 
ATOM   2172 C  CG  B GLN A 1 271 ? -51.837 62.880 14.231  0.50 37.75  ? 271 GLN A CG  1 
ATOM   2173 C  CD  A GLN A 1 271 ? -53.165 61.504 12.037  0.50 44.20  ? 271 GLN A CD  1 
ATOM   2174 C  CD  B GLN A 1 271 ? -52.523 63.589 13.071  0.50 47.18  ? 271 GLN A CD  1 
ATOM   2175 O  OE1 A GLN A 1 271 ? -53.152 62.167 10.999  0.50 43.96  ? 271 GLN A OE1 1 
ATOM   2176 O  OE1 B GLN A 1 271 ? -52.134 63.434 11.907  0.50 42.88  ? 271 GLN A OE1 1 
ATOM   2177 N  NE2 A GLN A 1 271 ? -54.290 61.192 12.670  0.50 41.19  ? 271 GLN A NE2 1 
ATOM   2178 N  NE2 B GLN A 1 271 ? -53.544 64.383 13.387  0.50 53.32  ? 271 GLN A NE2 1 
ATOM   2179 N  N   . GLN A 1 272 ? -49.989 58.381 14.429  1.00 33.30  ? 272 GLN A N   1 
ATOM   2180 C  CA  . GLN A 1 272 ? -50.212 56.941 14.482  1.00 30.40  ? 272 GLN A CA  1 
ATOM   2181 C  C   . GLN A 1 272 ? -48.887 56.198 14.370  1.00 31.31  ? 272 GLN A C   1 
ATOM   2182 O  O   . GLN A 1 272 ? -47.858 56.768 13.999  1.00 34.60  ? 272 GLN A O   1 
ATOM   2183 C  CB  . GLN A 1 272 ? -51.178 56.501 13.387  1.00 29.47  ? 272 GLN A CB  1 
ATOM   2184 C  CG  . GLN A 1 272 ? -50.609 56.634 11.992  1.00 33.09  ? 272 GLN A CG  1 
ATOM   2185 C  CD  . GLN A 1 272 ? -51.640 56.369 10.908  1.00 30.91  ? 272 GLN A CD  1 
ATOM   2186 O  OE1 . GLN A 1 272 ? -52.205 57.301 10.342  1.00 32.94  ? 272 GLN A OE1 1 
ATOM   2187 N  NE2 . GLN A 1 272 ? -51.887 55.094 10.614  1.00 26.59  ? 272 GLN A NE2 1 
ATOM   2188 N  N   . ASP A 1 273 ? -48.927 54.901 14.691  1.00 27.12  ? 273 ASP A N   1 
ATOM   2189 C  CA  A ASP A 1 273 ? -47.734 54.054 14.707  0.62 29.95  ? 273 ASP A CA  1 
ATOM   2190 C  CA  B ASP A 1 273 ? -47.739 54.050 14.709  0.38 30.01  ? 273 ASP A CA  1 
ATOM   2191 C  C   . ASP A 1 273 ? -47.517 53.455 13.319  1.00 31.17  ? 273 ASP A C   1 
ATOM   2192 O  O   . ASP A 1 273 ? -48.327 52.647 12.844  1.00 28.58  ? 273 ASP A O   1 
ATOM   2193 C  CB  A ASP A 1 273 ? -47.854 52.946 15.755  0.62 30.48  ? 273 ASP A CB  1 
ATOM   2194 C  CB  B ASP A 1 273 ? -47.897 52.952 15.759  0.38 30.52  ? 273 ASP A CB  1 
ATOM   2195 C  CG  A ASP A 1 273 ? -47.833 53.472 17.189  0.62 34.65  ? 273 ASP A CG  1 
ATOM   2196 C  CG  B ASP A 1 273 ? -46.594 52.257 16.080  0.38 32.05  ? 273 ASP A CG  1 
ATOM   2197 O  OD1 A ASP A 1 273 ? -47.308 54.585 17.429  0.62 31.50  ? 273 ASP A OD1 1 
ATOM   2198 O  OD1 B ASP A 1 273 ? -45.543 52.713 15.588  0.38 32.35  ? 273 ASP A OD1 1 
ATOM   2199 O  OD2 A ASP A 1 273 ? -48.343 52.753 18.082  0.62 39.73  ? 273 ASP A OD2 1 
ATOM   2200 O  OD2 B ASP A 1 273 ? -46.620 51.252 16.825  0.38 39.18  ? 273 ASP A OD2 1 
ATOM   2201 N  N   . ILE A 1 274 ? -46.418 53.844 12.672  1.00 27.03  ? 274 ILE A N   1 
ATOM   2202 C  CA  . ILE A 1 274 ? -46.079 53.379 11.330  1.00 29.21  ? 274 ILE A CA  1 
ATOM   2203 C  C   . ILE A 1 274 ? -44.598 53.032 11.278  1.00 25.52  ? 274 ILE A C   1 
ATOM   2204 O  O   . ILE A 1 274 ? -43.757 53.753 11.825  1.00 30.45  ? 274 ILE A O   1 
ATOM   2205 C  CB  . ILE A 1 274 ? -46.388 54.426 10.234  1.00 29.16  ? 274 ILE A CB  1 
ATOM   2206 C  CG1 . ILE A 1 274 ? -47.822 54.933 10.320  1.00 32.78  ? 274 ILE A CG1 1 
ATOM   2207 C  CG2 . ILE A 1 274 ? -46.183 53.812 8.860   1.00 31.59  ? 274 ILE A CG2 1 
ATOM   2208 C  CD1 . ILE A 1 274 ? -48.070 56.152 9.458   1.00 30.72  ? 274 ILE A CD1 1 
ATOM   2209 N  N   . ALA A 1 275 ? -44.279 51.933 10.604  1.00 23.80  ? 275 ALA A N   1 
ATOM   2210 C  CA  . ALA A 1 275 ? -42.905 51.602 10.274  1.00 26.99  ? 275 ALA A CA  1 
ATOM   2211 C  C   . ALA A 1 275 ? -42.916 51.005 8.877   1.00 24.90  ? 275 ALA A C   1 
ATOM   2212 O  O   . ALA A 1 275 ? -43.936 51.037 8.185   1.00 28.93  ? 275 ALA A O   1 
ATOM   2213 C  CB  . ALA A 1 275 ? -42.289 50.666 11.326  1.00 25.53  ? 275 ALA A CB  1 
ATOM   2214 N  N   . CYS A 1 276 ? -41.776 50.456 8.459   1.00 29.39  ? 276 CYS A N   1 
ATOM   2215 C  CA  . CYS A 1 276 ? -41.683 49.787 7.167   1.00 26.26  ? 276 CYS A CA  1 
ATOM   2216 C  C   . CYS A 1 276 ? -40.440 48.910 7.156   1.00 24.80  ? 276 CYS A C   1 
ATOM   2217 O  O   . CYS A 1 276 ? -39.591 48.996 8.043   1.00 24.85  ? 276 CYS A O   1 
ATOM   2218 C  CB  . CYS A 1 276 ? -41.634 50.800 6.018   1.00 32.61  ? 276 CYS A CB  1 
ATOM   2219 S  SG  . CYS A 1 276 ? -40.114 51.767 6.003   1.00 38.57  ? 276 CYS A SG  1 
ATOM   2220 N  N   . ASP A 1 277 ? -40.337 48.057 6.139   1.00 25.92  ? 277 ASP A N   1 
ATOM   2221 C  CA  . ASP A 1 277 ? -39.092 47.334 5.899   1.00 31.05  ? 277 ASP A CA  1 
ATOM   2222 C  C   . ASP A 1 277 ? -38.700 47.491 4.434   1.00 33.04  ? 277 ASP A C   1 
ATOM   2223 O  O   . ASP A 1 277 ? -39.479 47.966 3.607   1.00 32.10  ? 277 ASP A O   1 
ATOM   2224 C  CB  . ASP A 1 277 ? -39.199 45.848 6.281   1.00 25.15  ? 277 ASP A CB  1 
ATOM   2225 C  CG  . ASP A 1 277 ? -40.323 45.122 5.546   1.00 32.51  ? 277 ASP A CG  1 
ATOM   2226 O  OD1 . ASP A 1 277 ? -40.163 44.788 4.351   1.00 36.09  ? 277 ASP A OD1 1 
ATOM   2227 O  OD2 . ASP A 1 277 ? -41.368 44.876 6.173   1.00 37.65  ? 277 ASP A OD2 1 
ATOM   2228 N  N   . CYS A 1 278 ? -37.470 47.095 4.117   1.00 25.04  ? 278 CYS A N   1 
ATOM   2229 C  CA  . CYS A 1 278 ? -36.992 47.182 2.751   1.00 31.70  ? 278 CYS A CA  1 
ATOM   2230 C  C   . CYS A 1 278 ? -35.891 46.154 2.555   1.00 31.54  ? 278 CYS A C   1 
ATOM   2231 O  O   . CYS A 1 278 ? -35.226 45.744 3.514   1.00 25.92  ? 278 CYS A O   1 
ATOM   2232 C  CB  . CYS A 1 278 ? -36.466 48.589 2.427   1.00 35.72  ? 278 CYS A CB  1 
ATOM   2233 S  SG  . CYS A 1 278 ? -34.813 48.888 3.078   1.00 45.16  ? 278 CYS A SG  1 
ATOM   2234 N  N   . TYR A 1 279 ? -35.708 45.748 1.297   1.00 27.74  ? 279 TYR A N   1 
ATOM   2235 C  CA  . TYR A 1 279 ? -34.502 44.971 1.081   1.00 24.21  ? 279 TYR A CA  1 
ATOM   2236 C  C   . TYR A 1 279 ? -33.427 45.855 0.480   1.00 25.97  ? 279 TYR A C   1 
ATOM   2237 O  O   . TYR A 1 279 ? -33.733 46.761 -0.300  1.00 32.16  ? 279 TYR A O   1 
ATOM   2238 C  CB  . TYR A 1 279 ? -34.750 43.764 0.173   1.00 24.24  ? 279 TYR A CB  1 
ATOM   2239 C  CG  . TYR A 1 279 ? -35.354 44.024 -1.194  1.00 29.41  ? 279 TYR A CG  1 
ATOM   2240 C  CD1 . TYR A 1 279 ? -34.546 44.330 -2.288  1.00 29.27  ? 279 TYR A CD1 1 
ATOM   2241 C  CD2 . TYR A 1 279 ? -36.724 43.892 -1.411  1.00 30.29  ? 279 TYR A CD2 1 
ATOM   2242 C  CE1 . TYR A 1 279 ? -35.089 44.535 -3.560  1.00 26.17  ? 279 TYR A CE1 1 
ATOM   2243 C  CE2 . TYR A 1 279 ? -37.283 44.082 -2.686  1.00 22.32  ? 279 TYR A CE2 1 
ATOM   2244 C  CZ  . TYR A 1 279 ? -36.463 44.407 -3.753  1.00 36.54  ? 279 TYR A CZ  1 
ATOM   2245 O  OH  . TYR A 1 279 ? -37.015 44.592 -5.016  1.00 27.20  ? 279 TYR A OH  1 
ATOM   2246 N  N   . PRO A 1 280 ? -32.183 45.590 0.842   1.00 28.01  ? 280 PRO A N   1 
ATOM   2247 C  CA  . PRO A 1 280 ? -31.067 46.498 0.557   1.00 30.48  ? 280 PRO A CA  1 
ATOM   2248 C  C   . PRO A 1 280 ? -30.459 46.338 -0.841  1.00 28.51  ? 280 PRO A C   1 
ATOM   2249 O  O   . PRO A 1 280 ? -29.244 46.169 -0.998  1.00 26.76  ? 280 PRO A O   1 
ATOM   2250 C  CB  . PRO A 1 280 ? -30.066 46.135 1.658   1.00 25.66  ? 280 PRO A CB  1 
ATOM   2251 C  CG  . PRO A 1 280 ? -30.256 44.651 1.795   1.00 23.81  ? 280 PRO A CG  1 
ATOM   2252 C  CD  . PRO A 1 280 ? -31.739 44.405 1.594   1.00 22.66  ? 280 PRO A CD  1 
ATOM   2253 N  N   . TYR A 1 281 ? -31.315 46.393 -1.866  1.00 31.20  ? 281 TYR A N   1 
ATOM   2254 C  CA  . TYR A 1 281 ? -30.881 46.369 -3.259  1.00 25.83  ? 281 TYR A CA  1 
ATOM   2255 C  C   . TYR A 1 281 ? -31.748 47.313 -4.087  1.00 30.84  ? 281 TYR A C   1 
ATOM   2256 O  O   . TYR A 1 281 ? -32.907 47.565 -3.751  1.00 24.47  ? 281 TYR A O   1 
ATOM   2257 C  CB  . TYR A 1 281 ? -30.965 44.973 -3.868  1.00 25.00  ? 281 TYR A CB  1 
ATOM   2258 C  CG  . TYR A 1 281 ? -30.241 43.877 -3.128  1.00 27.56  ? 281 TYR A CG  1 
ATOM   2259 C  CD1 . TYR A 1 281 ? -30.749 43.352 -1.944  1.00 25.01  ? 281 TYR A CD1 1 
ATOM   2260 C  CD2 . TYR A 1 281 ? -29.069 43.324 -3.644  1.00 27.47  ? 281 TYR A CD2 1 
ATOM   2261 C  CE1 . TYR A 1 281 ? -30.092 42.329 -1.281  1.00 24.33  ? 281 TYR A CE1 1 
ATOM   2262 C  CE2 . TYR A 1 281 ? -28.410 42.304 -2.988  1.00 27.71  ? 281 TYR A CE2 1 
ATOM   2263 C  CZ  . TYR A 1 281 ? -28.927 41.812 -1.808  1.00 29.20  ? 281 TYR A CZ  1 
ATOM   2264 O  OH  . TYR A 1 281 ? -28.269 40.799 -1.158  1.00 27.18  ? 281 TYR A OH  1 
ATOM   2265 N  N   . SER A 1 282 ? -31.183 47.821 -5.186  1.00 25.86  ? 282 SER A N   1 
ATOM   2266 C  CA  . SER A 1 282 ? -31.891 48.733 -6.077  1.00 26.89  ? 282 SER A CA  1 
ATOM   2267 C  C   . SER A 1 282 ? -32.294 48.075 -7.401  1.00 33.35  ? 282 SER A C   1 
ATOM   2268 O  O   . SER A 1 282 ? -32.639 48.771 -8.361  1.00 35.05  ? 282 SER A O   1 
ATOM   2269 C  CB  . SER A 1 282 ? -31.041 49.974 -6.343  1.00 26.97  ? 282 SER A CB  1 
ATOM   2270 O  OG  . SER A 1 282 ? -29.771 49.609 -6.845  1.00 35.77  ? 282 SER A OG  1 
ATOM   2271 N  N   . ALA A 1 283 ? -32.238 46.753 -7.478  1.00 27.84  ? 283 ALA A N   1 
ATOM   2272 C  CA  . ALA A 1 283 ? -32.754 46.003 -8.611  1.00 29.76  ? 283 ALA A CA  1 
ATOM   2273 C  C   . ALA A 1 283 ? -33.768 45.006 -8.080  1.00 34.42  ? 283 ALA A C   1 
ATOM   2274 O  O   . ALA A 1 283 ? -33.591 44.455 -6.985  1.00 34.53  ? 283 ALA A O   1 
ATOM   2275 C  CB  . ALA A 1 283 ? -31.635 45.279 -9.377  1.00 27.91  ? 283 ALA A CB  1 
ATOM   2276 N  N   . SER A 1 284 ? -34.851 44.813 -8.828  1.00 31.88  ? 284 SER A N   1 
ATOM   2277 C  CA  . SER A 1 284 ? -35.824 43.772 -8.543  1.00 25.30  ? 284 SER A CA  1 
ATOM   2278 C  C   . SER A 1 284 ? -35.567 42.581 -9.467  1.00 33.83  ? 284 SER A C   1 
ATOM   2279 O  O   . SER A 1 284 ? -34.679 42.598 -10.320 1.00 28.87  ? 284 SER A O   1 
ATOM   2280 C  CB  . SER A 1 284 ? -37.251 44.307 -8.700  1.00 29.59  ? 284 SER A CB  1 
ATOM   2281 O  OG  . SER A 1 284 ? -37.452 44.854 -10.000 1.00 34.77  ? 284 SER A OG  1 
ATOM   2282 N  N   . SER A 1 285 ? -36.361 41.529 -9.300  1.00 31.36  ? 285 SER A N   1 
ATOM   2283 C  CA  . SER A 1 285 ? -36.129 40.296 -10.040 1.00 36.05  ? 285 SER A CA  1 
ATOM   2284 C  C   . SER A 1 285 ? -37.443 39.530 -10.124 1.00 44.41  ? 285 SER A C   1 
ATOM   2285 O  O   . SER A 1 285 ? -38.125 39.356 -9.112  1.00 36.51  ? 285 SER A O   1 
ATOM   2286 C  CB  . SER A 1 285 ? -35.040 39.462 -9.355  1.00 31.75  ? 285 SER A CB  1 
ATOM   2287 O  OG  . SER A 1 285 ? -34.996 38.146 -9.857  1.00 41.77  ? 285 SER A OG  1 
ATOM   2288 N  N   . SER A 1 286 ? -37.798 39.085 -11.324 1.00 31.75  ? 286 SER A N   1 
ATOM   2289 C  CA  . SER A 1 286 ? -39.100 38.478 -11.539 1.00 30.36  ? 286 SER A CA  1 
ATOM   2290 C  C   . SER A 1 286 ? -39.061 37.731 -12.863 1.00 34.29  ? 286 SER A C   1 
ATOM   2291 O  O   . SER A 1 286 ? -38.029 37.691 -13.538 1.00 39.61  ? 286 SER A O   1 
ATOM   2292 C  CB  . SER A 1 286 ? -40.200 39.544 -11.515 1.00 36.58  ? 286 SER A CB  1 
ATOM   2293 O  OG  . SER A 1 286 ? -41.467 38.932 -11.364 1.00 53.36  ? 286 SER A OG  1 
ATOM   2294 N  N   . THR A 1 287 ? -40.191 37.122 -13.226 1.00 34.61  ? 287 THR A N   1 
ATOM   2295 C  CA  . THR A 1 287 ? -40.337 36.601 -14.580 1.00 38.88  ? 287 THR A CA  1 
ATOM   2296 C  C   . THR A 1 287 ? -40.229 37.734 -15.594 1.00 32.46  ? 287 THR A C   1 
ATOM   2297 O  O   . THR A 1 287 ? -40.549 38.894 -15.313 1.00 36.19  ? 287 THR A O   1 
ATOM   2298 C  CB  . THR A 1 287 ? -41.684 35.896 -14.768 1.00 38.68  ? 287 THR A CB  1 
ATOM   2299 O  OG1 . THR A 1 287 ? -42.744 36.834 -14.546 1.00 44.97  ? 287 THR A OG1 1 
ATOM   2300 C  CG2 . THR A 1 287 ? -41.834 34.705 -13.815 1.00 33.89  ? 287 THR A CG2 1 
ATOM   2301 N  N   . LEU A 1 288 ? -39.761 37.391 -16.785 1.00 33.99  ? 288 LEU A N   1 
ATOM   2302 C  CA  . LEU A 1 288 ? -39.778 38.340 -17.884 1.00 26.72  ? 288 LEU A CA  1 
ATOM   2303 C  C   . LEU A 1 288 ? -41.210 38.453 -18.385 1.00 33.40  ? 288 LEU A C   1 
ATOM   2304 O  O   . LEU A 1 288 ? -41.812 37.453 -18.795 1.00 31.93  ? 288 LEU A O   1 
ATOM   2305 C  CB  . LEU A 1 288 ? -38.833 37.884 -18.987 1.00 32.55  ? 288 LEU A CB  1 
ATOM   2306 C  CG  . LEU A 1 288 ? -38.660 38.858 -20.156 1.00 33.01  ? 288 LEU A CG  1 
ATOM   2307 C  CD1 . LEU A 1 288 ? -38.080 40.184 -19.658 1.00 25.80  ? 288 LEU A CD1 1 
ATOM   2308 C  CD2 . LEU A 1 288 ? -37.770 38.237 -21.222 1.00 22.77  ? 288 LEU A CD2 1 
ATOM   2309 N  N   . ASP A 1 289 ? -41.776 39.657 -18.283 1.00 33.23  ? 289 ASP A N   1 
ATOM   2310 C  CA  A ASP A 1 289 ? -43.154 39.901 -18.681 0.42 39.12  ? 289 ASP A CA  1 
ATOM   2311 C  CA  B ASP A 1 289 ? -43.158 39.921 -18.653 0.58 39.15  ? 289 ASP A CA  1 
ATOM   2312 C  C   . ASP A 1 289 ? -43.208 41.046 -19.676 1.00 35.70  ? 289 ASP A C   1 
ATOM   2313 O  O   . ASP A 1 289 ? -42.552 42.081 -19.500 1.00 33.89  ? 289 ASP A O   1 
ATOM   2314 C  CB  A ASP A 1 289 ? -44.070 40.211 -17.483 0.42 41.61  ? 289 ASP A CB  1 
ATOM   2315 C  CB  B ASP A 1 289 ? -43.994 40.289 -17.416 0.58 41.65  ? 289 ASP A CB  1 
ATOM   2316 C  CG  A ASP A 1 289 ? -45.547 40.228 -17.869 0.42 41.90  ? 289 ASP A CG  1 
ATOM   2317 C  CG  B ASP A 1 289 ? -43.913 39.234 -16.322 0.58 35.63  ? 289 ASP A CG  1 
ATOM   2318 O  OD1 A ASP A 1 289 ? -45.919 40.938 -18.830 0.42 43.22  ? 289 ASP A OD1 1 
ATOM   2319 O  OD1 B ASP A 1 289 ? -44.211 38.050 -16.595 0.58 41.70  ? 289 ASP A OD1 1 
ATOM   2320 O  OD2 A ASP A 1 289 ? -46.341 39.517 -17.216 0.42 47.84  ? 289 ASP A OD2 1 
ATOM   2321 O  OD2 B ASP A 1 289 ? -43.542 39.594 -15.192 0.58 45.06  ? 289 ASP A OD2 1 
ATOM   2322 N  N   . MET A 1 290 ? -44.005 40.841 -20.725 1.00 31.57  ? 290 MET A N   1 
ATOM   2323 C  CA  . MET A 1 290 ? -44.073 41.803 -21.820 1.00 35.95  ? 290 MET A CA  1 
ATOM   2324 C  C   . MET A 1 290 ? -44.407 43.201 -21.315 1.00 40.62  ? 290 MET A C   1 
ATOM   2325 O  O   . MET A 1 290 ? -43.887 44.196 -21.834 1.00 38.81  ? 290 MET A O   1 
ATOM   2326 C  CB  . MET A 1 290 ? -45.101 41.339 -22.855 1.00 34.85  ? 290 MET A CB  1 
ATOM   2327 C  CG  . MET A 1 290 ? -44.899 41.973 -24.202 1.00 33.38  ? 290 MET A CG  1 
ATOM   2328 S  SD  . MET A 1 290 ? -43.243 41.572 -24.819 1.00 34.62  ? 290 MET A SD  1 
ATOM   2329 C  CE  . MET A 1 290 ? -43.560 39.895 -25.342 1.00 31.45  ? 290 MET A CE  1 
ATOM   2330 N  N   . LYS A 1 291 ? -45.261 43.294 -20.289 1.00 38.16  ? 291 LYS A N   1 
ATOM   2331 C  CA  A LYS A 1 291 ? -45.689 44.587 -19.764 0.48 39.97  ? 291 LYS A CA  1 
ATOM   2332 C  CA  B LYS A 1 291 ? -45.684 44.597 -19.790 0.52 39.97  ? 291 LYS A CA  1 
ATOM   2333 C  C   . LYS A 1 291 ? -44.562 45.335 -19.069 1.00 40.69  ? 291 LYS A C   1 
ATOM   2334 O  O   . LYS A 1 291 ? -44.645 46.556 -18.917 1.00 39.50  ? 291 LYS A O   1 
ATOM   2335 C  CB  A LYS A 1 291 ? -46.846 44.411 -18.777 0.48 40.82  ? 291 LYS A CB  1 
ATOM   2336 C  CB  B LYS A 1 291 ? -46.890 44.439 -18.859 0.52 40.81  ? 291 LYS A CB  1 
ATOM   2337 C  CG  A LYS A 1 291 ? -46.395 44.053 -17.368 0.48 42.91  ? 291 LYS A CG  1 
ATOM   2338 C  CG  B LYS A 1 291 ? -48.059 43.638 -19.456 0.52 46.04  ? 291 LYS A CG  1 
ATOM   2339 C  CD  A LYS A 1 291 ? -47.553 44.031 -16.379 0.48 45.41  ? 291 LYS A CD  1 
ATOM   2340 C  CD  B LYS A 1 291 ? -48.842 44.431 -20.513 0.52 50.21  ? 291 LYS A CD  1 
ATOM   2341 C  CE  A LYS A 1 291 ? -48.152 42.643 -16.241 0.48 41.83  ? 291 LYS A CE  1 
ATOM   2342 C  CE  B LYS A 1 291 ? -50.078 43.662 -20.987 0.52 53.80  ? 291 LYS A CE  1 
ATOM   2343 N  NZ  A LYS A 1 291 ? -48.743 42.446 -14.875 0.48 44.44  ? 291 LYS A NZ  1 
ATOM   2344 N  NZ  B LYS A 1 291 ? -50.946 44.444 -21.922 0.52 37.04  ? 291 LYS A NZ  1 
ATOM   2345 N  N   A GLN A 1 292 ? -43.524 44.631 -18.618 0.57 41.07  ? 292 GLN A N   1 
ATOM   2346 N  N   B GLN A 1 292 ? -43.520 44.634 -18.633 0.43 41.02  ? 292 GLN A N   1 
ATOM   2347 C  CA  A GLN A 1 292 ? -42.405 45.263 -17.929 0.57 40.46  ? 292 GLN A CA  1 
ATOM   2348 C  CA  B GLN A 1 292 ? -42.415 45.268 -17.930 0.43 40.43  ? 292 GLN A CA  1 
ATOM   2349 C  C   A GLN A 1 292 ? -41.308 45.735 -18.872 0.57 37.55  ? 292 GLN A C   1 
ATOM   2350 C  C   B GLN A 1 292 ? -41.237 45.583 -18.844 0.43 37.58  ? 292 GLN A C   1 
ATOM   2351 O  O   A GLN A 1 292 ? -40.386 46.425 -18.423 0.57 35.98  ? 292 GLN A O   1 
ATOM   2352 O  O   B GLN A 1 292 ? -40.190 46.019 -18.353 0.43 36.20  ? 292 GLN A O   1 
ATOM   2353 C  CB  A GLN A 1 292 ? -41.797 44.299 -16.905 0.57 37.39  ? 292 GLN A CB  1 
ATOM   2354 C  CB  B GLN A 1 292 ? -41.965 44.386 -16.763 0.43 37.75  ? 292 GLN A CB  1 
ATOM   2355 C  CG  A GLN A 1 292 ? -42.716 43.982 -15.740 0.57 39.84  ? 292 GLN A CG  1 
ATOM   2356 C  CG  B GLN A 1 292 ? -43.106 44.009 -15.831 0.43 39.90  ? 292 GLN A CG  1 
ATOM   2357 C  CD  A GLN A 1 292 ? -43.147 45.225 -14.986 0.57 41.75  ? 292 GLN A CD  1 
ATOM   2358 C  CD  B GLN A 1 292 ? -42.632 43.498 -14.484 0.43 37.75  ? 292 GLN A CD  1 
ATOM   2359 O  OE1 A GLN A 1 292 ? -44.281 45.684 -15.129 0.57 44.97  ? 292 GLN A OE1 1 
ATOM   2360 O  OE1 B GLN A 1 292 ? -41.443 43.532 -14.173 0.43 39.81  ? 292 GLN A OE1 1 
ATOM   2361 N  NE2 A GLN A 1 292 ? -42.245 45.774 -14.171 0.57 41.10  ? 292 GLN A NE2 1 
ATOM   2362 N  NE2 B GLN A 1 292 ? -43.567 43.024 -13.674 0.43 41.35  ? 292 GLN A NE2 1 
ATOM   2363 N  N   . VAL A 1 293 ? -41.388 45.384 -20.158 1.00 38.24  ? 293 VAL A N   1 
ATOM   2364 C  CA  . VAL A 1 293 ? -40.302 45.659 -21.096 1.00 31.69  ? 293 VAL A CA  1 
ATOM   2365 C  C   . VAL A 1 293 ? -40.159 47.161 -21.311 1.00 28.80  ? 293 VAL A C   1 
ATOM   2366 O  O   . VAL A 1 293 ? -41.138 47.863 -21.599 1.00 35.83  ? 293 VAL A O   1 
ATOM   2367 C  CB  . VAL A 1 293 ? -40.549 44.930 -22.426 1.00 36.79  ? 293 VAL A CB  1 
ATOM   2368 C  CG1 . VAL A 1 293 ? -39.566 45.384 -23.458 1.00 29.95  ? 293 VAL A CG1 1 
ATOM   2369 C  CG2 . VAL A 1 293 ? -40.450 43.430 -22.244 1.00 33.16  ? 293 VAL A CG2 1 
ATOM   2370 N  N   . THR A 1 294 ? -38.928 47.658 -21.201 1.00 28.03  ? 294 THR A N   1 
ATOM   2371 C  CA  . THR A 1 294 ? -38.657 49.079 -21.380 1.00 28.82  ? 294 THR A CA  1 
ATOM   2372 C  C   . THR A 1 294 ? -37.192 49.248 -21.739 1.00 29.59  ? 294 THR A C   1 
ATOM   2373 O  O   . THR A 1 294 ? -36.359 48.385 -21.448 1.00 37.34  ? 294 THR A O   1 
ATOM   2374 C  CB  . THR A 1 294 ? -38.983 49.891 -20.113 1.00 37.92  ? 294 THR A CB  1 
ATOM   2375 O  OG1 . THR A 1 294 ? -38.591 51.254 -20.303 1.00 34.47  ? 294 THR A OG1 1 
ATOM   2376 C  CG2 . THR A 1 294 ? -38.228 49.335 -18.907 1.00 27.79  ? 294 THR A CG2 1 
ATOM   2377 N  N   . ASP A 1 295 ? -36.877 50.388 -22.348 1.00 33.64  ? 295 ASP A N   1 
ATOM   2378 C  CA  . ASP A 1 295 ? -35.489 50.744 -22.603 1.00 38.80  ? 295 ASP A CA  1 
ATOM   2379 C  C   . ASP A 1 295 ? -34.945 51.719 -21.564 1.00 35.62  ? 295 ASP A C   1 
ATOM   2380 O  O   . ASP A 1 295 ? -33.845 52.255 -21.746 1.00 35.37  ? 295 ASP A O   1 
ATOM   2381 C  CB  . ASP A 1 295 ? -35.335 51.316 -24.016 1.00 36.26  ? 295 ASP A CB  1 
ATOM   2382 C  CG  . ASP A 1 295 ? -35.982 52.681 -24.174 1.00 40.20  ? 295 ASP A CG  1 
ATOM   2383 O  OD1 . ASP A 1 295 ? -36.725 53.111 -23.263 1.00 43.25  ? 295 ASP A OD1 1 
ATOM   2384 O  OD2 . ASP A 1 295 ? -35.737 53.327 -25.216 1.00 55.19  ? 295 ASP A OD2 1 
ATOM   2385 N  N   . GLU A 1 296 ? -35.682 51.931 -20.466 1.00 34.77  ? 296 GLU A N   1 
ATOM   2386 C  CA  . GLU A 1 296 ? -35.323 52.908 -19.440 1.00 40.39  ? 296 GLU A CA  1 
ATOM   2387 C  C   . GLU A 1 296 ? -34.189 52.450 -18.525 1.00 34.39  ? 296 GLU A C   1 
ATOM   2388 O  O   . GLU A 1 296 ? -33.550 53.284 -17.885 1.00 42.83  ? 296 GLU A O   1 
ATOM   2389 C  CB  . GLU A 1 296 ? -36.556 53.237 -18.594 1.00 34.11  ? 296 GLU A CB  1 
ATOM   2390 C  CG  . GLU A 1 296 ? -37.596 54.081 -19.348 1.00 46.30  ? 296 GLU A CG  1 
ATOM   2391 C  CD  . GLU A 1 296 ? -38.968 54.058 -18.696 1.00 56.01  ? 296 GLU A CD  1 
ATOM   2392 O  OE1 . GLU A 1 296 ? -39.462 52.947 -18.395 1.00 49.39  ? 296 GLU A OE1 1 
ATOM   2393 O  OE2 . GLU A 1 296 ? -39.551 55.148 -18.493 1.00 59.99  ? 296 GLU A OE2 1 
ATOM   2394 N  N   . PHE A 1 297 ? -33.919 51.156 -18.444 1.00 33.48  ? 297 PHE A N   1 
ATOM   2395 C  CA  . PHE A 1 297 ? -32.868 50.664 -17.571 1.00 40.67  ? 297 PHE A CA  1 
ATOM   2396 C  C   . PHE A 1 297 ? -32.550 49.247 -18.004 1.00 35.28  ? 297 PHE A C   1 
ATOM   2397 O  O   . PHE A 1 297 ? -33.303 48.633 -18.760 1.00 30.74  ? 297 PHE A O   1 
ATOM   2398 C  CB  . PHE A 1 297 ? -33.296 50.705 -16.094 1.00 33.59  ? 297 PHE A CB  1 
ATOM   2399 C  CG  . PHE A 1 297 ? -34.686 50.187 -15.865 1.00 26.08  ? 297 PHE A CG  1 
ATOM   2400 C  CD1 . PHE A 1 297 ? -34.963 48.829 -15.973 1.00 29.70  ? 297 PHE A CD1 1 
ATOM   2401 C  CD2 . PHE A 1 297 ? -35.726 51.055 -15.577 1.00 29.78  ? 297 PHE A CD2 1 
ATOM   2402 C  CE1 . PHE A 1 297 ? -36.255 48.342 -15.782 1.00 24.16  ? 297 PHE A CE1 1 
ATOM   2403 C  CE2 . PHE A 1 297 ? -37.018 50.575 -15.389 1.00 28.28  ? 297 PHE A CE2 1 
ATOM   2404 C  CZ  . PHE A 1 297 ? -37.278 49.216 -15.493 1.00 29.92  ? 297 PHE A CZ  1 
ATOM   2405 N  N   . ASP A 1 298 ? -31.434 48.732 -17.507 1.00 37.05  ? 298 ASP A N   1 
ATOM   2406 C  CA  . ASP A 1 298 ? -31.051 47.362 -17.813 1.00 33.28  ? 298 ASP A CA  1 
ATOM   2407 C  C   . ASP A 1 298 ? -32.116 46.368 -17.354 1.00 31.34  ? 298 ASP A C   1 
ATOM   2408 O  O   . ASP A 1 298 ? -32.640 46.449 -16.241 1.00 30.95  ? 298 ASP A O   1 
ATOM   2409 C  CB  . ASP A 1 298 ? -29.711 47.028 -17.156 1.00 34.01  ? 298 ASP A CB  1 
ATOM   2410 C  CG  . ASP A 1 298 ? -28.521 47.562 -17.930 1.00 42.70  ? 298 ASP A CG  1 
ATOM   2411 O  OD1 . ASP A 1 298 ? -28.708 48.256 -18.963 1.00 40.57  ? 298 ASP A OD1 1 
ATOM   2412 O  OD2 . ASP A 1 298 ? -27.382 47.268 -17.497 1.00 42.30  ? 298 ASP A OD2 1 
ATOM   2413 N  N   . ILE A 1 299 ? -32.444 45.437 -18.233 1.00 29.66  ? 299 ILE A N   1 
ATOM   2414 C  CA  . ILE A 1 299 ? -33.190 44.237 -17.901 1.00 26.75  ? 299 ILE A CA  1 
ATOM   2415 C  C   . ILE A 1 299 ? -32.257 43.086 -18.227 1.00 29.59  ? 299 ILE A C   1 
ATOM   2416 O  O   . ILE A 1 299 ? -31.825 42.941 -19.379 1.00 32.12  ? 299 ILE A O   1 
ATOM   2417 C  CB  . ILE A 1 299 ? -34.507 44.141 -18.689 1.00 28.66  ? 299 ILE A CB  1 
ATOM   2418 C  CG1 . ILE A 1 299 ? -35.403 45.342 -18.377 1.00 26.65  ? 299 ILE A CG1 1 
ATOM   2419 C  CG2 . ILE A 1 299 ? -35.212 42.809 -18.409 1.00 26.08  ? 299 ILE A CG2 1 
ATOM   2420 C  CD1 . ILE A 1 299 ? -36.694 45.352 -19.175 1.00 30.63  ? 299 ILE A CD1 1 
ATOM   2421 N  N   . VAL A 1 300 ? -31.889 42.309 -17.215 1.00 25.33  ? 300 VAL A N   1 
ATOM   2422 C  CA  . VAL A 1 300 ? -30.854 41.294 -17.359 1.00 26.72  ? 300 VAL A CA  1 
ATOM   2423 C  C   . VAL A 1 300 ? -31.500 39.929 -17.217 1.00 26.26  ? 300 VAL A C   1 
ATOM   2424 O  O   . VAL A 1 300 ? -32.206 39.668 -16.235 1.00 29.47  ? 300 VAL A O   1 
ATOM   2425 C  CB  . VAL A 1 300 ? -29.730 41.486 -16.334 1.00 32.75  ? 300 VAL A CB  1 
ATOM   2426 C  CG1 . VAL A 1 300 ? -28.648 40.424 -16.541 1.00 30.88  ? 300 VAL A CG1 1 
ATOM   2427 C  CG2 . VAL A 1 300 ? -29.161 42.877 -16.447 1.00 26.19  ? 300 VAL A CG2 1 
ATOM   2428 N  N   . ILE A 1 301 ? -31.273 39.068 -18.199 1.00 21.85  ? 301 ILE A N   1 
ATOM   2429 C  CA  . ILE A 1 301 ? -31.931 37.770 -18.223 1.00 26.75  ? 301 ILE A CA  1 
ATOM   2430 C  C   . ILE A 1 301 ? -31.226 36.857 -17.233 1.00 29.71  ? 301 ILE A C   1 
ATOM   2431 O  O   . ILE A 1 301 ? -30.000 36.723 -17.261 1.00 30.99  ? 301 ILE A O   1 
ATOM   2432 C  CB  . ILE A 1 301 ? -31.925 37.170 -19.639 1.00 27.81  ? 301 ILE A CB  1 
ATOM   2433 C  CG1 . ILE A 1 301 ? -32.576 38.132 -20.634 1.00 24.79  ? 301 ILE A CG1 1 
ATOM   2434 C  CG2 . ILE A 1 301 ? -32.620 35.797 -19.649 1.00 27.33  ? 301 ILE A CG2 1 
ATOM   2435 C  CD1 . ILE A 1 301 ? -33.993 38.498 -20.296 1.00 22.35  ? 301 ILE A CD1 1 
ATOM   2436 N  N   . THR A 1 302 ? -31.996 36.257 -16.332 1.00 27.52  ? 302 THR A N   1 
ATOM   2437 C  CA  . THR A 1 302 ? -31.423 35.310 -15.384 1.00 37.05  ? 302 THR A CA  1 
ATOM   2438 C  C   . THR A 1 302 ? -31.482 33.880 -15.912 1.00 39.13  ? 302 THR A C   1 
ATOM   2439 O  O   . THR A 1 302 ? -30.567 33.088 -15.673 1.00 43.89  ? 302 THR A O   1 
ATOM   2440 C  CB  . THR A 1 302 ? -32.155 35.402 -14.039 1.00 34.50  ? 302 THR A CB  1 
ATOM   2441 O  OG1 . THR A 1 302 ? -33.559 35.215 -14.248 1.00 35.13  ? 302 THR A OG1 1 
ATOM   2442 C  CG2 . THR A 1 302 ? -31.937 36.762 -13.379 1.00 29.78  ? 302 THR A CG2 1 
ATOM   2443 N  N   . TRP A 1 303 ? -32.549 33.532 -16.626 1.00 36.20  ? 303 TRP A N   1 
ATOM   2444 C  CA  . TRP A 1 303 ? -32.671 32.220 -17.242 1.00 37.57  ? 303 TRP A CA  1 
ATOM   2445 C  C   . TRP A 1 303 ? -33.705 32.321 -18.351 1.00 37.94  ? 303 TRP A C   1 
ATOM   2446 O  O   . TRP A 1 303 ? -34.563 33.207 -18.343 1.00 38.28  ? 303 TRP A O   1 
ATOM   2447 C  CB  . TRP A 1 303 ? -33.068 31.155 -16.215 1.00 32.98  ? 303 TRP A CB  1 
ATOM   2448 C  CG  . TRP A 1 303 ? -34.362 31.472 -15.542 1.00 38.26  ? 303 TRP A CG  1 
ATOM   2449 C  CD1 . TRP A 1 303 ? -34.535 32.212 -14.406 1.00 40.78  ? 303 TRP A CD1 1 
ATOM   2450 C  CD2 . TRP A 1 303 ? -35.672 31.096 -15.978 1.00 37.16  ? 303 TRP A CD2 1 
ATOM   2451 N  NE1 . TRP A 1 303 ? -35.868 32.305 -14.102 1.00 38.54  ? 303 TRP A NE1 1 
ATOM   2452 C  CE2 . TRP A 1 303 ? -36.588 31.626 -15.050 1.00 34.98  ? 303 TRP A CE2 1 
ATOM   2453 C  CE3 . TRP A 1 303 ? -36.159 30.347 -17.054 1.00 37.80  ? 303 TRP A CE3 1 
ATOM   2454 C  CZ2 . TRP A 1 303 ? -37.964 31.441 -15.171 1.00 32.65  ? 303 TRP A CZ2 1 
ATOM   2455 C  CZ3 . TRP A 1 303 ? -37.518 30.159 -17.165 1.00 36.04  ? 303 TRP A CZ3 1 
ATOM   2456 C  CH2 . TRP A 1 303 ? -38.406 30.708 -16.235 1.00 34.07  ? 303 TRP A CH2 1 
ATOM   2457 N  N   . SER A 1 304 ? -33.620 31.401 -19.306 1.00 33.89  ? 304 SER A N   1 
ATOM   2458 C  CA  . SER A 1 304 ? -34.595 31.367 -20.391 1.00 36.94  ? 304 SER A CA  1 
ATOM   2459 C  C   . SER A 1 304 ? -34.777 29.934 -20.862 1.00 35.10  ? 304 SER A C   1 
ATOM   2460 O  O   . SER A 1 304 ? -33.827 29.298 -21.328 1.00 42.24  ? 304 SER A O   1 
ATOM   2461 C  CB  . SER A 1 304 ? -34.166 32.262 -21.557 1.00 35.49  ? 304 SER A CB  1 
ATOM   2462 O  OG  . SER A 1 304 ? -34.985 32.041 -22.697 1.00 35.20  ? 304 SER A OG  1 
ATOM   2463 N  N   . GLU A 1 305 ? -36.005 29.435 -20.752 1.00 45.99  ? 305 GLU A N   1 
ATOM   2464 C  CA  . GLU A 1 305 ? -36.314 28.125 -21.309 1.00 45.67  ? 305 GLU A CA  1 
ATOM   2465 C  C   . GLU A 1 305 ? -36.123 28.118 -22.819 1.00 42.43  ? 305 GLU A C   1 
ATOM   2466 O  O   . GLU A 1 305 ? -35.523 27.189 -23.373 1.00 51.07  ? 305 GLU A O   1 
ATOM   2467 C  CB  . GLU A 1 305 ? -37.742 27.738 -20.935 1.00 50.77  ? 305 GLU A CB  1 
ATOM   2468 C  CG  . GLU A 1 305 ? -38.240 26.471 -21.583 1.00 61.55  ? 305 GLU A CG  1 
ATOM   2469 C  CD  . GLU A 1 305 ? -39.536 25.990 -20.960 1.00 77.19  ? 305 GLU A CD  1 
ATOM   2470 O  OE1 . GLU A 1 305 ? -39.688 26.120 -19.720 1.00 74.20  ? 305 GLU A OE1 1 
ATOM   2471 O  OE2 . GLU A 1 305 ? -40.401 25.489 -21.712 1.00 77.48  ? 305 GLU A OE2 1 
ATOM   2472 N  N   . ALA A 1 306 ? -36.584 29.174 -23.500 1.00 37.25  ? 306 ALA A N   1 
ATOM   2473 C  CA  . ALA A 1 306 ? -36.557 29.185 -24.961 1.00 41.24  ? 306 ALA A CA  1 
ATOM   2474 C  C   . ALA A 1 306 ? -35.139 29.319 -25.505 1.00 41.92  ? 306 ALA A C   1 
ATOM   2475 O  O   . ALA A 1 306 ? -34.806 28.708 -26.526 1.00 42.71  ? 306 ALA A O   1 
ATOM   2476 C  CB  . ALA A 1 306 ? -37.440 30.311 -25.498 1.00 31.31  ? 306 ALA A CB  1 
ATOM   2477 N  N   . GLN A 1 307 ? -34.298 30.130 -24.859 1.00 42.25  ? 307 GLN A N   1 
ATOM   2478 C  CA  . GLN A 1 307 ? -32.943 30.420 -25.339 1.00 35.50  ? 307 GLN A CA  1 
ATOM   2479 C  C   . GLN A 1 307 ? -31.998 30.481 -24.147 1.00 43.47  ? 307 GLN A C   1 
ATOM   2480 O  O   . GLN A 1 307 ? -31.517 31.557 -23.764 1.00 40.62  ? 307 GLN A O   1 
ATOM   2481 C  CB  . GLN A 1 307 ? -32.915 31.728 -26.131 1.00 33.51  ? 307 GLN A CB  1 
ATOM   2482 C  CG  . GLN A 1 307 ? -33.907 31.792 -27.311 1.00 31.98  ? 307 GLN A CG  1 
ATOM   2483 C  CD  . GLN A 1 307 ? -33.461 30.960 -28.492 1.00 41.02  ? 307 GLN A CD  1 
ATOM   2484 O  OE1 . GLN A 1 307 ? -32.271 30.800 -28.728 1.00 46.19  ? 307 GLN A OE1 1 
ATOM   2485 N  NE2 . GLN A 1 307 ? -34.415 30.417 -29.237 1.00 36.44  ? 307 GLN A NE2 1 
ATOM   2486 N  N   . PRO A 1 308 ? -31.680 29.324 -23.553 1.00 42.45  ? 308 PRO A N   1 
ATOM   2487 C  CA  . PRO A 1 308 ? -31.016 29.330 -22.238 1.00 43.46  ? 308 PRO A CA  1 
ATOM   2488 C  C   . PRO A 1 308 ? -29.648 29.993 -22.243 1.00 39.91  ? 308 PRO A C   1 
ATOM   2489 O  O   . PRO A 1 308 ? -29.189 30.432 -21.184 1.00 41.77  ? 308 PRO A O   1 
ATOM   2490 C  CB  . PRO A 1 308 ? -30.904 27.838 -21.887 1.00 36.38  ? 308 PRO A CB  1 
ATOM   2491 C  CG  . PRO A 1 308 ? -31.701 27.108 -22.946 1.00 41.19  ? 308 PRO A CG  1 
ATOM   2492 C  CD  . PRO A 1 308 ? -31.723 27.977 -24.139 1.00 33.06  ? 308 PRO A CD  1 
ATOM   2493 N  N   . GLU A 1 309 ? -28.986 30.077 -23.392 1.00 39.95  ? 309 GLU A N   1 
ATOM   2494 C  CA  . GLU A 1 309 ? -27.646 30.644 -23.485 1.00 45.16  ? 309 GLU A CA  1 
ATOM   2495 C  C   . GLU A 1 309 ? -27.641 32.166 -23.497 1.00 38.92  ? 309 GLU A C   1 
ATOM   2496 O  O   . GLU A 1 309 ? -26.564 32.765 -23.496 1.00 44.69  ? 309 GLU A O   1 
ATOM   2497 C  CB  . GLU A 1 309 ? -26.939 30.129 -24.743 1.00 39.78  ? 309 GLU A CB  1 
ATOM   2498 C  CG  . GLU A 1 309 ? -27.529 30.638 -26.053 1.00 55.28  ? 309 GLU A CG  1 
ATOM   2499 C  CD  . GLU A 1 309 ? -28.906 30.062 -26.358 1.00 63.72  ? 309 GLU A CD  1 
ATOM   2500 O  OE1 . GLU A 1 309 ? -29.663 30.703 -27.136 1.00 53.46  ? 309 GLU A OE1 1 
ATOM   2501 O  OE2 . GLU A 1 309 ? -29.222 28.974 -25.824 1.00 52.98  ? 309 GLU A OE2 1 
ATOM   2502 N  N   . GLN A 1 310 ? -28.799 32.812 -23.523 1.00 41.62  ? 310 GLN A N   1 
ATOM   2503 C  CA  . GLN A 1 310 ? -28.834 34.267 -23.458 1.00 36.21  ? 310 GLN A CA  1 
ATOM   2504 C  C   . GLN A 1 310 ? -28.716 34.806 -22.039 1.00 36.07  ? 310 GLN A C   1 
ATOM   2505 O  O   . GLN A 1 310 ? -28.613 36.028 -21.870 1.00 36.62  ? 310 GLN A O   1 
ATOM   2506 C  CB  . GLN A 1 310 ? -30.124 34.784 -24.100 1.00 33.58  ? 310 GLN A CB  1 
ATOM   2507 C  CG  . GLN A 1 310 ? -30.259 34.371 -25.559 1.00 36.29  ? 310 GLN A CG  1 
ATOM   2508 C  CD  . GLN A 1 310 ? -29.046 34.766 -26.391 1.00 34.83  ? 310 GLN A CD  1 
ATOM   2509 O  OE1 . GLN A 1 310 ? -28.478 35.837 -26.206 1.00 37.39  ? 310 GLN A OE1 1 
ATOM   2510 N  NE2 . GLN A 1 310 ? -28.651 33.898 -27.315 1.00 44.51  ? 310 GLN A NE2 1 
ATOM   2511 N  N   . ALA A 1 311 ? -28.723 33.939 -21.025 1.00 33.16  ? 311 ALA A N   1 
ATOM   2512 C  CA  . ALA A 1 311 ? -28.738 34.406 -19.643 1.00 39.48  ? 311 ALA A CA  1 
ATOM   2513 C  C   . ALA A 1 311 ? -27.458 35.167 -19.309 1.00 38.76  ? 311 ALA A C   1 
ATOM   2514 O  O   . ALA A 1 311 ? -26.360 34.785 -19.718 1.00 31.33  ? 311 ALA A O   1 
ATOM   2515 C  CB  . ALA A 1 311 ? -28.917 33.228 -18.689 1.00 33.45  ? 311 ALA A CB  1 
ATOM   2516 N  N   . GLY A 1 312 ? -27.602 36.253 -18.554 1.00 29.47  ? 312 GLY A N   1 
ATOM   2517 C  CA  . GLY A 1 312 ? -26.488 37.105 -18.214 1.00 34.44  ? 312 GLY A CA  1 
ATOM   2518 C  C   . GLY A 1 312 ? -26.378 38.357 -19.059 1.00 36.86  ? 312 GLY A C   1 
ATOM   2519 O  O   . GLY A 1 312 ? -25.739 39.321 -18.625 1.00 35.36  ? 312 GLY A O   1 
ATOM   2520 N  N   . LYS A 1 313 ? -26.988 38.365 -20.245 1.00 36.42  ? 313 LYS A N   1 
ATOM   2521 C  CA  . LYS A 1 313 ? -26.995 39.512 -21.137 1.00 33.62  ? 313 LYS A CA  1 
ATOM   2522 C  C   . LYS A 1 313 ? -28.203 40.395 -20.843 1.00 30.17  ? 313 LYS A C   1 
ATOM   2523 O  O   . LYS A 1 313 ? -29.227 39.932 -20.340 1.00 29.42  ? 313 LYS A O   1 
ATOM   2524 C  CB  . LYS A 1 313 ? -27.045 39.066 -22.598 1.00 31.43  ? 313 LYS A CB  1 
ATOM   2525 C  CG  . LYS A 1 313 ? -25.993 38.070 -23.023 1.00 33.07  ? 313 LYS A CG  1 
ATOM   2526 C  CD  . LYS A 1 313 ? -26.100 37.824 -24.540 1.00 40.35  ? 313 LYS A CD  1 
ATOM   2527 C  CE  . LYS A 1 313 ? -25.153 36.742 -25.025 1.00 51.10  ? 313 LYS A CE  1 
ATOM   2528 N  NZ  . LYS A 1 313 ? -25.235 36.565 -26.495 1.00 43.74  ? 313 LYS A NZ  1 
ATOM   2529 N  N   . THR A 1 314 ? -28.083 41.677 -21.182 1.00 25.69  ? 314 THR A N   1 
ATOM   2530 C  CA  . THR A 1 314 ? -29.234 42.564 -21.084 1.00 25.60  ? 314 THR A CA  1 
ATOM   2531 C  C   . THR A 1 314 ? -30.189 42.339 -22.256 1.00 28.93  ? 314 THR A C   1 
ATOM   2532 O  O   . THR A 1 314 ? -29.789 41.929 -23.357 1.00 26.66  ? 314 THR A O   1 
ATOM   2533 C  CB  . THR A 1 314 ? -28.799 44.037 -21.027 1.00 33.51  ? 314 THR A CB  1 
ATOM   2534 O  OG1 . THR A 1 314 ? -28.440 44.505 -22.330 1.00 31.52  ? 314 THR A OG1 1 
ATOM   2535 C  CG2 . THR A 1 314 ? -27.597 44.218 -20.092 1.00 26.31  ? 314 THR A CG2 1 
ATOM   2536 N  N   . LEU A 1 315 ? -31.478 42.579 -21.995 1.00 26.33  ? 315 LEU A N   1 
ATOM   2537 C  CA  . LEU A 1 315 ? -32.479 42.468 -23.051 1.00 24.21  ? 315 LEU A CA  1 
ATOM   2538 C  C   . LEU A 1 315 ? -32.070 43.269 -24.285 1.00 24.91  ? 315 LEU A C   1 
ATOM   2539 O  O   . LEU A 1 315 ? -32.207 42.798 -25.422 1.00 24.34  ? 315 LEU A O   1 
ATOM   2540 C  CB  . LEU A 1 315 ? -33.836 42.945 -22.528 1.00 22.69  ? 315 LEU A CB  1 
ATOM   2541 C  CG  . LEU A 1 315 ? -35.045 42.671 -23.431 1.00 24.40  ? 315 LEU A CG  1 
ATOM   2542 C  CD1 . LEU A 1 315 ? -35.112 41.205 -23.788 1.00 23.11  ? 315 LEU A CD1 1 
ATOM   2543 C  CD2 . LEU A 1 315 ? -36.341 43.117 -22.776 1.00 25.83  ? 315 LEU A CD2 1 
ATOM   2544 N  N   . GLN A 1 316 ? -31.567 44.490 -24.073 1.00 28.49  ? 316 GLN A N   1 
ATOM   2545 C  CA  . GLN A 1 316 ? -31.109 45.326 -25.177 1.00 32.35  ? 316 GLN A CA  1 
ATOM   2546 C  C   . GLN A 1 316 ? -29.996 44.636 -25.965 1.00 30.96  ? 316 GLN A C   1 
ATOM   2547 O  O   . GLN A 1 316 ? -30.046 44.566 -27.195 1.00 29.12  ? 316 GLN A O   1 
ATOM   2548 C  CB  . GLN A 1 316 ? -30.642 46.676 -24.630 1.00 27.04  ? 316 GLN A CB  1 
ATOM   2549 C  CG  . GLN A 1 316 ? -30.362 47.712 -25.681 1.00 32.94  ? 316 GLN A CG  1 
ATOM   2550 C  CD  . GLN A 1 316 ? -31.580 48.016 -26.536 1.00 41.59  ? 316 GLN A CD  1 
ATOM   2551 O  OE1 . GLN A 1 316 ? -32.555 48.593 -26.068 1.00 42.02  ? 316 GLN A OE1 1 
ATOM   2552 N  NE2 . GLN A 1 316 ? -31.531 47.609 -27.797 1.00 41.00  ? 316 GLN A NE2 1 
ATOM   2553 N  N   . GLN A 1 317 ? -28.979 44.115 -25.268 1.00 28.45  ? 317 GLN A N   1 
ATOM   2554 C  CA  . GLN A 1 317 ? -27.921 43.365 -25.947 1.00 29.87  ? 317 GLN A CA  1 
ATOM   2555 C  C   . GLN A 1 317 ? -28.500 42.242 -26.790 1.00 33.70  ? 317 GLN A C   1 
ATOM   2556 O  O   . GLN A 1 317 ? -28.076 42.024 -27.928 1.00 34.01  ? 317 GLN A O   1 
ATOM   2557 C  CB  . GLN A 1 317 ? -26.949 42.762 -24.936 1.00 29.26  ? 317 GLN A CB  1 
ATOM   2558 C  CG  . GLN A 1 317 ? -25.967 43.701 -24.307 1.00 31.84  ? 317 GLN A CG  1 
ATOM   2559 C  CD  . GLN A 1 317 ? -24.981 42.942 -23.428 1.00 36.61  ? 317 GLN A CD  1 
ATOM   2560 O  OE1 . GLN A 1 317 ? -25.381 42.261 -22.481 1.00 33.76  ? 317 GLN A OE1 1 
ATOM   2561 N  NE2 . GLN A 1 317 ? -23.692 43.025 -23.762 1.00 33.12  ? 317 GLN A NE2 1 
ATOM   2562 N  N   . ILE A 1 318 ? -29.444 41.488 -26.223 1.00 27.50  ? 318 ILE A N   1 
ATOM   2563 C  CA  . ILE A 1 318 ? -30.023 40.355 -26.930 1.00 30.74  ? 318 ILE A CA  1 
ATOM   2564 C  C   . ILE A 1 318 ? -30.804 40.833 -28.149 1.00 31.12  ? 318 ILE A C   1 
ATOM   2565 O  O   . ILE A 1 318 ? -30.663 40.278 -29.247 1.00 30.92  ? 318 ILE A O   1 
ATOM   2566 C  CB  . ILE A 1 318 ? -30.890 39.520 -25.968 1.00 24.08  ? 318 ILE A CB  1 
ATOM   2567 C  CG1 . ILE A 1 318 ? -30.032 38.964 -24.833 1.00 26.03  ? 318 ILE A CG1 1 
ATOM   2568 C  CG2 . ILE A 1 318 ? -31.576 38.384 -26.699 1.00 24.12  ? 318 ILE A CG2 1 
ATOM   2569 C  CD1 . ILE A 1 318 ? -30.828 38.495 -23.629 1.00 28.61  ? 318 ILE A CD1 1 
ATOM   2570 N  N   . ALA A 1 319 ? -31.611 41.890 -27.989 1.00 30.05  ? 319 ALA A N   1 
ATOM   2571 C  CA  . ALA A 1 319 ? -32.319 42.464 -29.134 1.00 26.89  ? 319 ALA A CA  1 
ATOM   2572 C  C   . ALA A 1 319 ? -31.349 42.897 -30.228 1.00 35.42  ? 319 ALA A C   1 
ATOM   2573 O  O   . ALA A 1 319 ? -31.592 42.651 -31.417 1.00 31.27  ? 319 ALA A O   1 
ATOM   2574 C  CB  . ALA A 1 319 ? -33.171 43.649 -28.690 1.00 26.73  ? 319 ALA A CB  1 
ATOM   2575 N  N   . ASP A 1 320 ? -30.246 43.551 -29.844 1.00 26.46  ? 320 ASP A N   1 
ATOM   2576 C  CA  . ASP A 1 320 ? -29.269 44.019 -30.825 1.00 31.90  ? 320 ASP A CA  1 
ATOM   2577 C  C   . ASP A 1 320 ? -28.602 42.859 -31.543 1.00 32.04  ? 320 ASP A C   1 
ATOM   2578 O  O   . ASP A 1 320 ? -28.476 42.862 -32.771 1.00 32.44  ? 320 ASP A O   1 
ATOM   2579 C  CB  . ASP A 1 320 ? -28.217 44.879 -30.141 1.00 32.60  ? 320 ASP A CB  1 
ATOM   2580 C  CG  . ASP A 1 320 ? -28.801 46.129 -29.569 1.00 37.48  ? 320 ASP A CG  1 
ATOM   2581 O  OD1 . ASP A 1 320 ? -29.926 46.465 -30.004 1.00 39.79  ? 320 ASP A OD1 1 
ATOM   2582 O  OD2 . ASP A 1 320 ? -28.154 46.759 -28.698 1.00 44.15  ? 320 ASP A OD2 1 
ATOM   2583 N  N   . GLU A 1 321 ? -28.151 41.861 -30.788 1.00 30.19  ? 321 GLU A N   1 
ATOM   2584 C  CA  . GLU A 1 321 ? -27.550 40.683 -31.400 1.00 35.25  ? 321 GLU A CA  1 
ATOM   2585 C  C   . GLU A 1 321 ? -28.513 40.006 -32.374 1.00 33.69  ? 321 GLU A C   1 
ATOM   2586 O  O   . GLU A 1 321 ? -28.105 39.563 -33.449 1.00 28.77  ? 321 GLU A O   1 
ATOM   2587 C  CB  . GLU A 1 321 ? -27.102 39.712 -30.307 1.00 34.47  ? 321 GLU A CB  1 
ATOM   2588 C  CG  . GLU A 1 321 ? -26.699 38.332 -30.799 1.00 38.87  ? 321 GLU A CG  1 
ATOM   2589 C  CD  . GLU A 1 321 ? -26.200 37.464 -29.661 1.00 51.80  ? 321 GLU A CD  1 
ATOM   2590 O  OE1 . GLU A 1 321 ? -25.664 38.038 -28.681 1.00 47.70  ? 321 GLU A OE1 1 
ATOM   2591 O  OE2 . GLU A 1 321 ? -26.354 36.221 -29.740 1.00 53.22  ? 321 GLU A OE2 1 
ATOM   2592 N  N   . TRP A 1 322 ? -29.789 39.894 -32.006 1.00 35.55  ? 322 TRP A N   1 
ATOM   2593 C  CA  . TRP A 1 322 ? -30.775 39.273 -32.880 1.00 32.98  ? 322 TRP A CA  1 
ATOM   2594 C  C   . TRP A 1 322 ? -31.313 40.232 -33.932 1.00 33.31  ? 322 TRP A C   1 
ATOM   2595 O  O   . TRP A 1 322 ? -32.012 39.790 -34.854 1.00 29.05  ? 322 TRP A O   1 
ATOM   2596 C  CB  . TRP A 1 322 ? -31.947 38.727 -32.056 1.00 24.56  ? 322 TRP A CB  1 
ATOM   2597 C  CG  . TRP A 1 322 ? -31.624 37.507 -31.239 1.00 34.70  ? 322 TRP A CG  1 
ATOM   2598 C  CD1 . TRP A 1 322 ? -30.532 36.690 -31.367 1.00 27.52  ? 322 TRP A CD1 1 
ATOM   2599 C  CD2 . TRP A 1 322 ? -32.413 36.960 -30.163 1.00 27.07  ? 322 TRP A CD2 1 
ATOM   2600 N  NE1 . TRP A 1 322 ? -30.601 35.665 -30.443 1.00 37.52  ? 322 TRP A NE1 1 
ATOM   2601 C  CE2 . TRP A 1 322 ? -31.744 35.807 -29.696 1.00 28.73  ? 322 TRP A CE2 1 
ATOM   2602 C  CE3 . TRP A 1 322 ? -33.624 37.330 -29.561 1.00 27.75  ? 322 TRP A CE3 1 
ATOM   2603 C  CZ2 . TRP A 1 322 ? -32.239 35.023 -28.639 1.00 31.30  ? 322 TRP A CZ2 1 
ATOM   2604 C  CZ3 . TRP A 1 322 ? -34.122 36.544 -28.500 1.00 27.70  ? 322 TRP A CZ3 1 
ATOM   2605 C  CH2 . TRP A 1 322 ? -33.430 35.405 -28.060 1.00 26.06  ? 322 TRP A CH2 1 
ATOM   2606 N  N   . GLN A 1 323 ? -31.040 41.527 -33.797 1.00 30.59  ? 323 GLN A N   1 
ATOM   2607 C  CA  . GLN A 1 323 ? -31.544 42.528 -34.735 1.00 38.07  ? 323 GLN A CA  1 
ATOM   2608 C  C   . GLN A 1 323 ? -33.076 42.571 -34.732 1.00 37.37  ? 323 GLN A C   1 
ATOM   2609 O  O   . GLN A 1 323 ? -33.721 42.587 -35.780 1.00 40.02  ? 323 GLN A O   1 
ATOM   2610 C  CB  . GLN A 1 323 ? -30.986 42.273 -36.143 1.00 30.29  ? 323 GLN A CB  1 
ATOM   2611 C  CG  . GLN A 1 323 ? -29.459 42.252 -36.161 1.00 36.95  ? 323 GLN A CG  1 
ATOM   2612 C  CD  . GLN A 1 323 ? -28.872 42.074 -37.547 1.00 41.53  ? 323 GLN A CD  1 
ATOM   2613 O  OE1 . GLN A 1 323 ? -28.808 43.010 -38.329 1.00 48.43  ? 323 GLN A OE1 1 
ATOM   2614 N  NE2 . GLN A 1 323 ? -28.430 40.867 -37.848 1.00 42.00  ? 323 GLN A NE2 1 
ATOM   2615 N  N   . VAL A 1 324 ? -33.661 42.605 -33.529 1.00 34.36  ? 324 VAL A N   1 
ATOM   2616 C  CA  . VAL A 1 324 ? -35.103 42.748 -33.356 1.00 37.11  ? 324 VAL A CA  1 
ATOM   2617 C  C   . VAL A 1 324 ? -35.371 43.785 -32.276 1.00 31.38  ? 324 VAL A C   1 
ATOM   2618 O  O   . VAL A 1 324 ? -34.460 44.307 -31.633 1.00 32.64  ? 324 VAL A O   1 
ATOM   2619 C  CB  . VAL A 1 324 ? -35.812 41.427 -32.989 1.00 32.35  ? 324 VAL A CB  1 
ATOM   2620 C  CG1 . VAL A 1 324 ? -35.740 40.445 -34.130 1.00 26.25  ? 324 VAL A CG1 1 
ATOM   2621 C  CG2 . VAL A 1 324 ? -35.198 40.832 -31.712 1.00 31.75  ? 324 VAL A CG2 1 
ATOM   2622 N  N   . SER A 1 325 ? -36.650 44.080 -32.090 1.00 33.82  ? 325 SER A N   1 
ATOM   2623 C  CA  . SER A 1 325 ? -37.057 45.027 -31.067 1.00 36.78  ? 325 SER A CA  1 
ATOM   2624 C  C   . SER A 1 325 ? -36.977 44.379 -29.684 1.00 33.59  ? 325 SER A C   1 
ATOM   2625 O  O   . SER A 1 325 ? -36.928 43.149 -29.540 1.00 29.69  ? 325 SER A O   1 
ATOM   2626 C  CB  . SER A 1 325 ? -38.476 45.519 -31.343 1.00 29.60  ? 325 SER A CB  1 
ATOM   2627 O  OG  . SER A 1 325 ? -39.402 44.452 -31.167 1.00 31.89  ? 325 SER A OG  1 
ATOM   2628 N  N   . LEU A 1 326 ? -36.940 45.235 -28.659 1.00 34.20  ? 326 LEU A N   1 
ATOM   2629 C  CA  . LEU A 1 326 ? -36.967 44.755 -27.278 1.00 33.99  ? 326 LEU A CA  1 
ATOM   2630 C  C   . LEU A 1 326 ? -38.135 43.803 -27.044 1.00 30.31  ? 326 LEU A C   1 
ATOM   2631 O  O   . LEU A 1 326 ? -37.965 42.735 -26.450 1.00 31.67  ? 326 LEU A O   1 
ATOM   2632 C  CB  . LEU A 1 326 ? -37.042 45.939 -26.302 1.00 31.35  ? 326 LEU A CB  1 
ATOM   2633 C  CG  . LEU A 1 326 ? -35.786 46.789 -26.082 1.00 37.35  ? 326 LEU A CG  1 
ATOM   2634 C  CD1 . LEU A 1 326 ? -36.098 47.940 -25.129 1.00 37.66  ? 326 LEU A CD1 1 
ATOM   2635 C  CD2 . LEU A 1 326 ? -34.628 45.945 -25.539 1.00 34.01  ? 326 LEU A CD2 1 
ATOM   2636 N  N   . HIS A 1 327 ? -39.328 44.166 -27.514 1.00 36.94  ? 327 HIS A N   1 
ATOM   2637 C  CA  . HIS A 1 327 ? -40.491 43.310 -27.294 1.00 32.33  ? 327 HIS A CA  1 
ATOM   2638 C  C   . HIS A 1 327 ? -40.346 41.987 -28.017 1.00 33.15  ? 327 HIS A C   1 
ATOM   2639 O  O   . HIS A 1 327 ? -40.662 40.933 -27.453 1.00 34.19  ? 327 HIS A O   1 
ATOM   2640 C  CB  . HIS A 1 327 ? -41.769 44.014 -27.745 1.00 31.65  ? 327 HIS A CB  1 
ATOM   2641 C  CG  . HIS A 1 327 ? -42.231 45.065 -26.787 1.00 40.80  ? 327 HIS A CG  1 
ATOM   2642 N  ND1 . HIS A 1 327 ? -41.654 46.313 -26.721 1.00 38.39  ? 327 HIS A ND1 1 
ATOM   2643 C  CD2 . HIS A 1 327 ? -43.186 45.041 -25.829 1.00 46.43  ? 327 HIS A CD2 1 
ATOM   2644 C  CE1 . HIS A 1 327 ? -42.249 47.022 -25.780 1.00 40.18  ? 327 HIS A CE1 1 
ATOM   2645 N  NE2 . HIS A 1 327 ? -43.181 46.273 -25.223 1.00 39.21  ? 327 HIS A NE2 1 
ATOM   2646 N  N   . ASP A 1 328 ? -39.885 42.024 -29.274 1.00 31.01  ? 328 ASP A N   1 
ATOM   2647 C  CA  . ASP A 1 328 ? -39.679 40.790 -30.020 1.00 33.22  ? 328 ASP A CA  1 
ATOM   2648 C  C   . ASP A 1 328 ? -38.634 39.927 -29.347 1.00 31.24  ? 328 ASP A C   1 
ATOM   2649 O  O   . ASP A 1 328 ? -38.798 38.706 -29.255 1.00 33.69  ? 328 ASP A O   1 
ATOM   2650 C  CB  . ASP A 1 328 ? -39.256 41.087 -31.461 1.00 37.23  ? 328 ASP A CB  1 
ATOM   2651 C  CG  . ASP A 1 328 ? -40.421 41.360 -32.362 1.00 47.08  ? 328 ASP A CG  1 
ATOM   2652 O  OD1 . ASP A 1 328 ? -41.572 41.197 -31.914 1.00 57.78  ? 328 ASP A OD1 1 
ATOM   2653 O  OD2 . ASP A 1 328 ? -40.188 41.744 -33.525 1.00 69.01  ? 328 ASP A OD2 1 
ATOM   2654 N  N   . ALA A 1 329 ? -37.543 40.537 -28.877 1.00 25.62  ? 329 ALA A N   1 
ATOM   2655 C  CA  . ALA A 1 329 ? -36.554 39.748 -28.152 1.00 28.15  ? 329 ALA A CA  1 
ATOM   2656 C  C   . ALA A 1 329 ? -37.164 39.157 -26.885 1.00 29.72  ? 329 ALA A C   1 
ATOM   2657 O  O   . ALA A 1 329 ? -36.895 38.002 -26.540 1.00 33.33  ? 329 ALA A O   1 
ATOM   2658 C  CB  . ALA A 1 329 ? -35.324 40.593 -27.817 1.00 24.91  ? 329 ALA A CB  1 
ATOM   2659 N  N   . ALA A 1 330 ? -37.992 39.935 -26.182 1.00 28.50  ? 330 ALA A N   1 
ATOM   2660 C  CA  . ALA A 1 330 ? -38.656 39.425 -24.985 1.00 29.10  ? 330 ALA A CA  1 
ATOM   2661 C  C   . ALA A 1 330 ? -39.486 38.194 -25.314 1.00 32.65  ? 330 ALA A C   1 
ATOM   2662 O  O   . ALA A 1 330 ? -39.362 37.156 -24.653 1.00 26.51  ? 330 ALA A O   1 
ATOM   2663 C  CB  . ALA A 1 330 ? -39.528 40.514 -24.353 1.00 28.96  ? 330 ALA A CB  1 
ATOM   2664 N  N   . ALA A 1 331 ? -40.320 38.286 -26.362 1.00 27.61  ? 331 ALA A N   1 
ATOM   2665 C  CA  . ALA A 1 331 ? -41.155 37.157 -26.759 1.00 29.60  ? 331 ALA A CA  1 
ATOM   2666 C  C   . ALA A 1 331 ? -40.315 35.922 -27.056 1.00 32.28  ? 331 ALA A C   1 
ATOM   2667 O  O   . ALA A 1 331 ? -40.681 34.804 -26.677 1.00 33.04  ? 331 ALA A O   1 
ATOM   2668 C  CB  . ALA A 1 331 ? -41.998 37.525 -27.983 1.00 31.11  ? 331 ALA A CB  1 
ATOM   2669 N  N   . ARG A 1 332 ? -39.183 36.101 -27.740 1.00 29.68  ? 332 ARG A N   1 
ATOM   2670 C  CA  . ARG A 1 332 ? -38.353 34.959 -28.110 1.00 32.60  ? 332 ARG A CA  1 
ATOM   2671 C  C   . ARG A 1 332 ? -37.621 34.348 -26.921 1.00 35.77  ? 332 ARG A C   1 
ATOM   2672 O  O   . ARG A 1 332 ? -37.156 33.210 -27.014 1.00 37.89  ? 332 ARG A O   1 
ATOM   2673 C  CB  . ARG A 1 332 ? -37.351 35.370 -29.181 1.00 31.82  ? 332 ARG A CB  1 
ATOM   2674 C  CG  . ARG A 1 332 ? -38.025 35.701 -30.510 1.00 39.03  ? 332 ARG A CG  1 
ATOM   2675 C  CD  . ARG A 1 332 ? -37.031 36.255 -31.508 1.00 52.47  ? 332 ARG A CD  1 
ATOM   2676 N  NE  . ARG A 1 332 ? -37.700 36.939 -32.606 1.00 51.32  ? 332 ARG A NE  1 
ATOM   2677 C  CZ  . ARG A 1 332 ? -37.912 36.406 -33.797 1.00 58.53  ? 332 ARG A CZ  1 
ATOM   2678 N  NH1 . ARG A 1 332 ? -37.513 35.175 -34.082 1.00 65.34  ? 332 ARG A NH1 1 
ATOM   2679 N  NH2 . ARG A 1 332 ? -38.537 37.126 -34.725 1.00 61.65  ? 332 ARG A NH2 1 
ATOM   2680 N  N   A LEU A 1 333 ? -37.508 35.071 -25.809 0.35 31.45  ? 333 LEU A N   1 
ATOM   2681 N  N   B LEU A 1 333 ? -37.501 35.076 -25.813 0.65 31.42  ? 333 LEU A N   1 
ATOM   2682 C  CA  A LEU A 1 333 ? -36.879 34.526 -24.615 0.35 30.57  ? 333 LEU A CA  1 
ATOM   2683 C  CA  B LEU A 1 333 ? -36.877 34.524 -24.621 0.65 30.54  ? 333 LEU A CA  1 
ATOM   2684 C  C   A LEU A 1 333 ? -37.851 33.793 -23.706 0.35 30.04  ? 333 LEU A C   1 
ATOM   2685 C  C   B LEU A 1 333 ? -37.852 33.760 -23.740 0.65 29.94  ? 333 LEU A C   1 
ATOM   2686 O  O   A LEU A 1 333 ? -37.413 32.982 -22.882 0.35 35.28  ? 333 LEU A O   1 
ATOM   2687 O  O   B LEU A 1 333 ? -37.417 32.900 -22.968 0.65 35.42  ? 333 LEU A O   1 
ATOM   2688 C  CB  A LEU A 1 333 ? -36.209 35.644 -23.814 0.35 31.58  ? 333 LEU A CB  1 
ATOM   2689 C  CB  B LEU A 1 333 ? -36.245 35.645 -23.798 0.65 31.61  ? 333 LEU A CB  1 
ATOM   2690 C  CG  A LEU A 1 333 ? -34.983 36.282 -24.460 0.35 30.43  ? 333 LEU A CG  1 
ATOM   2691 C  CG  B LEU A 1 333 ? -35.041 36.309 -24.457 0.65 30.45  ? 333 LEU A CG  1 
ATOM   2692 C  CD1 A LEU A 1 333 ? -34.621 37.579 -23.755 0.35 27.82  ? 333 LEU A CD1 1 
ATOM   2693 C  CD1 B LEU A 1 333 ? -34.828 37.703 -23.896 0.65 27.32  ? 333 LEU A CD1 1 
ATOM   2694 C  CD2 A LEU A 1 333 ? -33.816 35.305 -24.442 0.35 29.49  ? 333 LEU A CD2 1 
ATOM   2695 C  CD2 B LEU A 1 333 ? -33.814 35.432 -24.259 0.65 29.38  ? 333 LEU A CD2 1 
ATOM   2696 N  N   . MET A 1 334 ? -39.146 34.050 -23.831 1.00 28.66  ? 334 MET A N   1 
ATOM   2697 C  CA  . MET A 1 334 ? -40.088 33.551 -22.840 1.00 30.83  ? 334 MET A CA  1 
ATOM   2698 C  C   . MET A 1 334 ? -40.357 32.056 -23.008 1.00 32.92  ? 334 MET A C   1 
ATOM   2699 O  O   . MET A 1 334 ? -40.289 31.524 -24.118 1.00 32.47  ? 334 MET A O   1 
ATOM   2700 C  CB  . MET A 1 334 ? -41.383 34.331 -22.931 1.00 32.58  ? 334 MET A CB  1 
ATOM   2701 C  CG  . MET A 1 334 ? -41.201 35.770 -22.508 1.00 33.00  ? 334 MET A CG  1 
ATOM   2702 S  SD  . MET A 1 334 ? -42.676 36.706 -22.834 1.00 40.76  ? 334 MET A SD  1 
ATOM   2703 C  CE  . MET A 1 334 ? -42.228 38.320 -22.242 1.00 31.70  ? 334 MET A CE  1 
ATOM   2704 N  N   . PRO A 1 335 ? -40.628 31.345 -21.904 1.00 32.13  ? 335 PRO A N   1 
ATOM   2705 C  CA  . PRO A 1 335 ? -40.601 31.809 -20.500 1.00 33.86  ? 335 PRO A CA  1 
ATOM   2706 C  C   . PRO A 1 335 ? -39.186 32.101 -20.026 1.00 35.94  ? 335 PRO A C   1 
ATOM   2707 O  O   . PRO A 1 335 ? -38.249 31.345 -20.295 1.00 36.05  ? 335 PRO A O   1 
ATOM   2708 C  CB  . PRO A 1 335 ? -41.231 30.637 -19.727 1.00 34.41  ? 335 PRO A CB  1 
ATOM   2709 C  CG  . PRO A 1 335 ? -41.007 29.432 -20.603 1.00 43.46  ? 335 PRO A CG  1 
ATOM   2710 C  CD  . PRO A 1 335 ? -41.125 29.960 -22.011 1.00 37.17  ? 335 PRO A CD  1 
ATOM   2711 N  N   . ALA A 1 336 ? -39.012 33.209 -19.309 1.00 28.96  ? 336 ALA A N   1 
ATOM   2712 C  CA  . ALA A 1 336 ? -37.698 33.625 -18.853 1.00 31.91  ? 336 ALA A CA  1 
ATOM   2713 C  C   . ALA A 1 336 ? -37.833 34.356 -17.525 1.00 30.99  ? 336 ALA A C   1 
ATOM   2714 O  O   . ALA A 1 336 ? -38.931 34.732 -17.100 1.00 31.09  ? 336 ALA A O   1 
ATOM   2715 C  CB  . ALA A 1 336 ? -37.008 34.514 -19.891 1.00 27.48  ? 336 ALA A CB  1 
ATOM   2716 N  N   . GLY A 1 337 ? -36.694 34.539 -16.866 1.00 35.59  ? 337 GLY A N   1 
ATOM   2717 C  CA  . GLY A 1 337 ? -36.611 35.365 -15.674 1.00 33.99  ? 337 GLY A CA  1 
ATOM   2718 C  C   . GLY A 1 337 ? -35.695 36.545 -15.935 1.00 34.68  ? 337 GLY A C   1 
ATOM   2719 O  O   . GLY A 1 337 ? -34.775 36.467 -16.754 1.00 28.75  ? 337 GLY A O   1 
ATOM   2720 N  N   . ALA A 1 338 ? -35.956 37.650 -15.242 1.00 28.23  ? 338 ALA A N   1 
ATOM   2721 C  CA  . ALA A 1 338 ? -35.144 38.829 -15.475 1.00 26.30  ? 338 ALA A CA  1 
ATOM   2722 C  C   . ALA A 1 338 ? -34.941 39.619 -14.191 1.00 30.04  ? 338 ALA A C   1 
ATOM   2723 O  O   . ALA A 1 338 ? -35.801 39.659 -13.306 1.00 25.81  ? 338 ALA A O   1 
ATOM   2724 C  CB  . ALA A 1 338 ? -35.758 39.742 -16.539 1.00 23.50  ? 338 ALA A CB  1 
ATOM   2725 N  N   . ILE A 1 339 ? -33.785 40.255 -14.124 1.00 26.33  ? 339 ILE A N   1 
ATOM   2726 C  CA  . ILE A 1 339 ? -33.494 41.308 -13.165 1.00 31.20  ? 339 ILE A CA  1 
ATOM   2727 C  C   . ILE A 1 339 ? -33.901 42.636 -13.793 1.00 33.95  ? 339 ILE A C   1 
ATOM   2728 O  O   . ILE A 1 339 ? -33.585 42.909 -14.957 1.00 32.35  ? 339 ILE A O   1 
ATOM   2729 C  CB  . ILE A 1 339 ? -32.000 41.305 -12.805 1.00 28.89  ? 339 ILE A CB  1 
ATOM   2730 C  CG1 . ILE A 1 339 ? -31.644 40.001 -12.103 1.00 22.06  ? 339 ILE A CG1 1 
ATOM   2731 C  CG2 . ILE A 1 339 ? -31.634 42.540 -11.983 1.00 30.30  ? 339 ILE A CG2 1 
ATOM   2732 C  CD1 . ILE A 1 339 ? -30.249 39.519 -12.409 1.00 29.66  ? 339 ILE A CD1 1 
ATOM   2733 N  N   . TYR A 1 340 ? -34.622 43.455 -13.041 1.00 28.79  ? 340 TYR A N   1 
ATOM   2734 C  CA  . TYR A 1 340 ? -35.050 44.764 -13.513 1.00 30.89  ? 340 TYR A CA  1 
ATOM   2735 C  C   . TYR A 1 340 ? -34.369 45.831 -12.669 1.00 30.80  ? 340 TYR A C   1 
ATOM   2736 O  O   . TYR A 1 340 ? -34.632 45.925 -11.465 1.00 29.79  ? 340 TYR A O   1 
ATOM   2737 C  CB  . TYR A 1 340 ? -36.568 44.910 -13.409 1.00 29.95  ? 340 TYR A CB  1 
ATOM   2738 C  CG  . TYR A 1 340 ? -37.386 43.900 -14.172 1.00 30.45  ? 340 TYR A CG  1 
ATOM   2739 C  CD1 . TYR A 1 340 ? -37.743 42.692 -13.601 1.00 29.34  ? 340 TYR A CD1 1 
ATOM   2740 C  CD2 . TYR A 1 340 ? -37.850 44.184 -15.456 1.00 26.31  ? 340 TYR A CD2 1 
ATOM   2741 C  CE1 . TYR A 1 340 ? -38.518 41.780 -14.293 1.00 31.88  ? 340 TYR A CE1 1 
ATOM   2742 C  CE2 . TYR A 1 340 ? -38.625 43.278 -16.150 1.00 31.82  ? 340 TYR A CE2 1 
ATOM   2743 C  CZ  . TYR A 1 340 ? -38.956 42.082 -15.570 1.00 37.74  ? 340 TYR A CZ  1 
ATOM   2744 O  OH  . TYR A 1 340 ? -39.736 41.193 -16.272 1.00 34.62  ? 340 TYR A OH  1 
ATOM   2745 N  N   . HIS A 1 341 ? -33.512 46.643 -13.294 1.00 25.99  ? 341 HIS A N   1 
ATOM   2746 C  CA  . HIS A 1 341 ? -32.855 47.739 -12.578 1.00 33.43  ? 341 HIS A CA  1 
ATOM   2747 C  C   . HIS A 1 341 ? -33.774 48.965 -12.497 1.00 31.73  ? 341 HIS A C   1 
ATOM   2748 O  O   . HIS A 1 341 ? -33.451 50.063 -12.949 1.00 33.04  ? 341 HIS A O   1 
ATOM   2749 C  CB  . HIS A 1 341 ? -31.512 48.061 -13.222 1.00 28.61  ? 341 HIS A CB  1 
ATOM   2750 C  CG  . HIS A 1 341 ? -30.462 47.022 -12.951 1.00 36.59  ? 341 HIS A CG  1 
ATOM   2751 N  ND1 . HIS A 1 341 ? -29.544 47.133 -11.925 1.00 36.62  ? 341 HIS A ND1 1 
ATOM   2752 C  CD2 . HIS A 1 341 ? -30.215 45.828 -13.545 1.00 32.97  ? 341 HIS A CD2 1 
ATOM   2753 C  CE1 . HIS A 1 341 ? -28.764 46.064 -11.916 1.00 40.08  ? 341 HIS A CE1 1 
ATOM   2754 N  NE2 . HIS A 1 341 ? -29.153 45.255 -12.887 1.00 31.74  ? 341 HIS A NE2 1 
ATOM   2755 N  N   . ASN A 1 342 ? -34.932 48.758 -11.855 1.00 27.83  ? 342 ASN A N   1 
ATOM   2756 C  CA  . ASN A 1 342 ? -36.034 49.712 -11.885 1.00 32.86  ? 342 ASN A CA  1 
ATOM   2757 C  C   . ASN A 1 342 ? -36.169 50.502 -10.586 1.00 33.27  ? 342 ASN A C   1 
ATOM   2758 O  O   . ASN A 1 342 ? -37.159 51.225 -10.402 1.00 27.72  ? 342 ASN A O   1 
ATOM   2759 C  CB  . ASN A 1 342 ? -37.352 48.997 -12.227 1.00 26.43  ? 342 ASN A CB  1 
ATOM   2760 C  CG  . ASN A 1 342 ? -37.825 48.052 -11.126 1.00 31.96  ? 342 ASN A CG  1 
ATOM   2761 O  OD1 . ASN A 1 342 ? -37.042 47.578 -10.292 1.00 29.88  ? 342 ASN A OD1 1 
ATOM   2762 N  ND2 . ASN A 1 342 ? -39.115 47.767 -11.130 1.00 33.57  ? 342 ASN A ND2 1 
ATOM   2763 N  N   . MET A 1 343 ? -35.175 50.423 -9.708  1.00 32.14  ? 343 MET A N   1 
ATOM   2764 C  CA  . MET A 1 343 ? -35.106 51.281 -8.542  1.00 28.15  ? 343 MET A CA  1 
ATOM   2765 C  C   . MET A 1 343 ? -33.828 52.113 -8.591  1.00 32.28  ? 343 MET A C   1 
ATOM   2766 O  O   . MET A 1 343 ? -32.848 51.758 -9.251  1.00 36.19  ? 343 MET A O   1 
ATOM   2767 C  CB  . MET A 1 343 ? -35.185 50.457 -7.246  1.00 30.15  ? 343 MET A CB  1 
ATOM   2768 C  CG  . MET A 1 343 ? -36.549 49.792 -6.996  1.00 29.99  ? 343 MET A CG  1 
ATOM   2769 S  SD  . MET A 1 343 ? -36.489 48.580 -5.635  1.00 39.17  ? 343 MET A SD  1 
ATOM   2770 C  CE  . MET A 1 343 ? -35.655 47.219 -6.440  1.00 28.30  ? 343 MET A CE  1 
ATOM   2771 N  N   . ASP A 1 344 ? -33.860 53.245 -7.893  1.00 30.76  ? 344 ASP A N   1 
ATOM   2772 C  CA  . ASP A 1 344 ? -32.735 54.164 -7.823  1.00 30.45  ? 344 ASP A CA  1 
ATOM   2773 C  C   . ASP A 1 344 ? -32.002 53.956 -6.500  1.00 36.81  ? 344 ASP A C   1 
ATOM   2774 O  O   . ASP A 1 344 ? -32.611 54.053 -5.429  1.00 27.81  ? 344 ASP A O   1 
ATOM   2775 C  CB  . ASP A 1 344 ? -33.210 55.610 -7.946  1.00 31.60  ? 344 ASP A CB  1 
ATOM   2776 C  CG  . ASP A 1 344 ? -32.099 56.606 -7.683  1.00 37.92  ? 344 ASP A CG  1 
ATOM   2777 O  OD1 . ASP A 1 344 ? -30.934 56.304 -8.018  1.00 56.84  ? 344 ASP A OD1 1 
ATOM   2778 O  OD2 . ASP A 1 344 ? -32.379 57.680 -7.113  1.00 56.25  ? 344 ASP A OD2 1 
ATOM   2779 N  N   . GLU A 1 345 ? -30.691 53.702 -6.579  1.00 35.37  ? 345 GLU A N   1 
ATOM   2780 C  CA  . GLU A 1 345 ? -29.889 53.447 -5.382  1.00 27.77  ? 345 GLU A CA  1 
ATOM   2781 C  C   . GLU A 1 345 ? -30.076 54.517 -4.303  1.00 27.87  ? 345 GLU A C   1 
ATOM   2782 O  O   . GLU A 1 345 ? -30.031 54.211 -3.111  1.00 30.14  ? 345 GLU A O   1 
ATOM   2783 C  CB  . GLU A 1 345 ? -28.412 53.332 -5.771  1.00 27.41  ? 345 GLU A CB  1 
ATOM   2784 C  CG  . GLU A 1 345 ? -27.476 53.053 -4.600  1.00 39.82  ? 345 GLU A CG  1 
ATOM   2785 C  CD  . GLU A 1 345 ? -27.654 51.652 -4.023  1.00 46.84  ? 345 GLU A CD  1 
ATOM   2786 O  OE1 . GLU A 1 345 ? -28.212 50.789 -4.725  1.00 35.76  ? 345 GLU A OE1 1 
ATOM   2787 O  OE2 . GLU A 1 345 ? -27.239 51.407 -2.869  1.00 47.04  ? 345 GLU A OE2 1 
ATOM   2788 N  N   . GLN A 1 346 ? -30.252 55.783 -4.688  1.00 31.88  ? 346 GLN A N   1 
ATOM   2789 C  CA  . GLN A 1 346 ? -30.419 56.811 -3.663  1.00 32.79  ? 346 GLN A CA  1 
ATOM   2790 C  C   . GLN A 1 346 ? -31.747 56.658 -2.946  1.00 31.64  ? 346 GLN A C   1 
ATOM   2791 O  O   . GLN A 1 346 ? -31.836 56.930 -1.744  1.00 36.49  ? 346 GLN A O   1 
ATOM   2792 C  CB  . GLN A 1 346 ? -30.313 58.222 -4.261  1.00 36.94  ? 346 GLN A CB  1 
ATOM   2793 C  CG  . GLN A 1 346 ? -28.956 58.569 -4.834  1.00 40.02  ? 346 GLN A CG  1 
ATOM   2794 C  CD  . GLN A 1 346 ? -27.820 58.217 -3.890  1.00 56.15  ? 346 GLN A CD  1 
ATOM   2795 O  OE1 . GLN A 1 346 ? -27.840 58.580 -2.712  1.00 55.39  ? 346 GLN A OE1 1 
ATOM   2796 N  NE2 . GLN A 1 346 ? -26.824 57.491 -4.402  1.00 54.79  ? 346 GLN A NE2 1 
ATOM   2797 N  N   . ASP A 1 347 ? -32.793 56.246 -3.661  1.00 28.83  ? 347 ASP A N   1 
ATOM   2798 C  CA  . ASP A 1 347 ? -34.053 55.937 -2.994  1.00 29.70  ? 347 ASP A CA  1 
ATOM   2799 C  C   . ASP A 1 347 ? -33.852 54.846 -1.958  1.00 28.62  ? 347 ASP A C   1 
ATOM   2800 O  O   . ASP A 1 347 ? -34.273 54.978 -0.805  1.00 33.36  ? 347 ASP A O   1 
ATOM   2801 C  CB  . ASP A 1 347 ? -35.098 55.490 -4.017  1.00 31.52  ? 347 ASP A CB  1 
ATOM   2802 C  CG  . ASP A 1 347 ? -35.730 56.644 -4.749  1.00 34.87  ? 347 ASP A CG  1 
ATOM   2803 O  OD1 . ASP A 1 347 ? -35.843 57.744 -4.160  1.00 35.97  ? 347 ASP A OD1 1 
ATOM   2804 O  OD2 . ASP A 1 347 ? -36.134 56.442 -5.910  1.00 33.31  ? 347 ASP A OD2 1 
ATOM   2805 N  N   . VAL A 1 348 ? -33.219 53.743 -2.369  1.00 25.66  ? 348 VAL A N   1 
ATOM   2806 C  CA  . VAL A 1 348 ? -33.043 52.611 -1.472  1.00 27.44  ? 348 VAL A CA  1 
ATOM   2807 C  C   . VAL A 1 348 ? -32.266 53.044 -0.238  1.00 33.22  ? 348 VAL A C   1 
ATOM   2808 O  O   . VAL A 1 348 ? -32.599 52.662 0.892   1.00 27.72  ? 348 VAL A O   1 
ATOM   2809 C  CB  . VAL A 1 348 ? -32.366 51.446 -2.223  1.00 27.12  ? 348 VAL A CB  1 
ATOM   2810 C  CG1 . VAL A 1 348 ? -32.219 50.238 -1.336  1.00 23.46  ? 348 VAL A CG1 1 
ATOM   2811 C  CG2 . VAL A 1 348 ? -33.201 51.069 -3.460  1.00 22.78  ? 348 VAL A CG2 1 
ATOM   2812 N  N   . ARG A 1 349 ? -31.251 53.891 -0.427  1.00 27.96  ? 349 ARG A N   1 
ATOM   2813 C  CA  . ARG A 1 349 ? -30.464 54.346 0.711   1.00 29.17  ? 349 ARG A CA  1 
ATOM   2814 C  C   . ARG A 1 349 ? -31.291 55.237 1.621   1.00 32.63  ? 349 ARG A C   1 
ATOM   2815 O  O   . ARG A 1 349 ? -31.199 55.126 2.847   1.00 32.68  ? 349 ARG A O   1 
ATOM   2816 C  CB  . ARG A 1 349 ? -29.206 55.079 0.238   1.00 29.25  ? 349 ARG A CB  1 
ATOM   2817 C  CG  . ARG A 1 349 ? -28.215 54.174 -0.474  1.00 35.97  ? 349 ARG A CG  1 
ATOM   2818 C  CD  . ARG A 1 349 ? -26.918 54.904 -0.880  1.00 33.63  ? 349 ARG A CD  1 
ATOM   2819 N  NE  . ARG A 1 349 ? -26.023 53.970 -1.552  1.00 40.57  ? 349 ARG A NE  1 
ATOM   2820 C  CZ  . ARG A 1 349 ? -24.702 54.002 -1.468  1.00 48.93  ? 349 ARG A CZ  1 
ATOM   2821 N  NH1 . ARG A 1 349 ? -24.084 54.904 -0.728  1.00 50.38  ? 349 ARG A NH1 1 
ATOM   2822 N  NH2 . ARG A 1 349 ? -23.987 53.096 -2.135  1.00 45.08  ? 349 ARG A NH2 1 
ATOM   2823 N  N   . ARG A 1 350 ? -32.092 56.141 1.047   1.00 28.90  ? 350 ARG A N   1 
ATOM   2824 C  CA  . ARG A 1 350 ? -32.938 56.985 1.886   1.00 32.61  ? 350 ARG A CA  1 
ATOM   2825 C  C   . ARG A 1 350 ? -33.881 56.139 2.729   1.00 30.50  ? 350 ARG A C   1 
ATOM   2826 O  O   . ARG A 1 350 ? -34.133 56.450 3.899   1.00 32.33  ? 350 ARG A O   1 
ATOM   2827 C  CB  . ARG A 1 350 ? -33.730 57.974 1.034   1.00 25.51  ? 350 ARG A CB  1 
ATOM   2828 C  CG  . ARG A 1 350 ? -33.071 59.322 0.865   1.00 37.00  ? 350 ARG A CG  1 
ATOM   2829 C  CD  . ARG A 1 350 ? -33.986 60.292 0.131   1.00 34.31  ? 350 ARG A CD  1 
ATOM   2830 N  NE  . ARG A 1 350 ? -34.268 59.834 -1.224  1.00 35.75  ? 350 ARG A NE  1 
ATOM   2831 C  CZ  . ARG A 1 350 ? -33.586 60.218 -2.292  1.00 41.52  ? 350 ARG A CZ  1 
ATOM   2832 N  NH1 . ARG A 1 350 ? -32.569 61.062 -2.197  1.00 46.93  ? 350 ARG A NH1 1 
ATOM   2833 N  NH2 . ARG A 1 350 ? -33.934 59.750 -3.486  1.00 40.22  ? 350 ARG A NH2 1 
ATOM   2834 N  N   . VAL A 1 351 ? -34.410 55.062 2.152   1.00 27.21  ? 351 VAL A N   1 
ATOM   2835 C  CA  . VAL A 1 351 ? -35.351 54.221 2.883   1.00 30.69  ? 351 VAL A CA  1 
ATOM   2836 C  C   . VAL A 1 351 ? -34.616 53.407 3.942   1.00 32.91  ? 351 VAL A C   1 
ATOM   2837 O  O   . VAL A 1 351 ? -35.115 53.217 5.055   1.00 29.32  ? 351 VAL A O   1 
ATOM   2838 C  CB  . VAL A 1 351 ? -36.138 53.318 1.908   1.00 26.57  ? 351 VAL A CB  1 
ATOM   2839 C  CG1 . VAL A 1 351 ? -36.929 52.238 2.678   1.00 28.48  ? 351 VAL A CG1 1 
ATOM   2840 C  CG2 . VAL A 1 351 ? -37.078 54.153 1.044   1.00 28.35  ? 351 VAL A CG2 1 
ATOM   2841 N  N   . MET A 1 352 ? -33.424 52.907 3.614   1.00 29.61  ? 352 MET A N   1 
ATOM   2842 C  CA  . MET A 1 352 ? -32.654 52.164 4.603   1.00 25.05  ? 352 MET A CA  1 
ATOM   2843 C  C   . MET A 1 352 ? -32.300 53.025 5.803   1.00 28.44  ? 352 MET A C   1 
ATOM   2844 O  O   . MET A 1 352 ? -32.300 52.541 6.942   1.00 28.61  ? 352 MET A O   1 
ATOM   2845 C  CB  . MET A 1 352 ? -31.389 51.599 3.978   1.00 31.23  ? 352 MET A CB  1 
ATOM   2846 C  CG  . MET A 1 352 ? -31.571 50.215 3.399   1.00 32.59  ? 352 MET A CG  1 
ATOM   2847 S  SD  . MET A 1 352 ? -29.969 49.577 2.891   1.00 44.15  ? 352 MET A SD  1 
ATOM   2848 C  CE  . MET A 1 352 ? -29.536 50.777 1.647   1.00 40.83  ? 352 MET A CE  1 
ATOM   2849 N  N   . ARG A 1 353 ? -31.977 54.296 5.577   1.00 27.37  ? 353 ARG A N   1 
ATOM   2850 C  CA  . ARG A 1 353 ? -31.583 55.147 6.694   1.00 28.84  ? 353 ARG A CA  1 
ATOM   2851 C  C   . ARG A 1 353 ? -32.769 55.661 7.496   1.00 28.66  ? 353 ARG A C   1 
ATOM   2852 O  O   . ARG A 1 353 ? -32.570 56.145 8.617   1.00 34.82  ? 353 ARG A O   1 
ATOM   2853 C  CB  . ARG A 1 353 ? -30.739 56.327 6.192   1.00 34.20  ? 353 ARG A CB  1 
ATOM   2854 C  CG  . ARG A 1 353 ? -29.465 55.885 5.516   1.00 37.07  ? 353 ARG A CG  1 
ATOM   2855 C  CD  . ARG A 1 353 ? -28.830 57.000 4.728   1.00 39.03  ? 353 ARG A CD  1 
ATOM   2856 N  NE  . ARG A 1 353 ? -28.525 58.118 5.607   1.00 59.21  ? 353 ARG A NE  1 
ATOM   2857 C  CZ  . ARG A 1 353 ? -29.221 59.245 5.652   1.00 71.54  ? 353 ARG A CZ  1 
ATOM   2858 N  NH1 . ARG A 1 353 ? -30.238 59.467 4.823   1.00 58.62  ? 353 ARG A NH1 1 
ATOM   2859 N  NH2 . ARG A 1 353 ? -28.887 60.174 6.548   1.00 64.75  ? 353 ARG A NH2 1 
ATOM   2860 N  N   . TYR A 1 354 ? -33.985 55.555 6.970   1.00 30.03  ? 354 TYR A N   1 
ATOM   2861 C  CA  . TYR A 1 354 ? -35.148 56.057 7.690   1.00 27.43  ? 354 TYR A CA  1 
ATOM   2862 C  C   . TYR A 1 354 ? -35.239 55.366 9.051   1.00 29.02  ? 354 TYR A C   1 
ATOM   2863 O  O   . TYR A 1 354 ? -35.063 54.145 9.133   1.00 24.78  ? 354 TYR A O   1 
ATOM   2864 C  CB  . TYR A 1 354 ? -36.423 55.840 6.863   1.00 27.93  ? 354 TYR A CB  1 
ATOM   2865 C  CG  . TYR A 1 354 ? -37.603 56.625 7.381   1.00 29.01  ? 354 TYR A CG  1 
ATOM   2866 C  CD1 . TYR A 1 354 ? -37.614 58.014 7.332   1.00 31.44  ? 354 TYR A CD1 1 
ATOM   2867 C  CD2 . TYR A 1 354 ? -38.691 55.982 7.942   1.00 27.99  ? 354 TYR A CD2 1 
ATOM   2868 C  CE1 . TYR A 1 354 ? -38.682 58.738 7.828   1.00 32.74  ? 354 TYR A CE1 1 
ATOM   2869 C  CE2 . TYR A 1 354 ? -39.769 56.698 8.447   1.00 38.63  ? 354 TYR A CE2 1 
ATOM   2870 C  CZ  . TYR A 1 354 ? -39.755 58.071 8.386   1.00 35.34  ? 354 TYR A CZ  1 
ATOM   2871 O  OH  . TYR A 1 354 ? -40.819 58.776 8.881   1.00 39.41  ? 354 TYR A OH  1 
ATOM   2872 N  N   . PRO A 1 355 ? -35.489 56.105 10.139  1.00 33.68  ? 355 PRO A N   1 
ATOM   2873 C  CA  . PRO A 1 355 ? -35.271 55.532 11.483  1.00 32.98  ? 355 PRO A CA  1 
ATOM   2874 C  C   . PRO A 1 355 ? -36.111 54.300 11.806  1.00 34.35  ? 355 PRO A C   1 
ATOM   2875 O  O   . PRO A 1 355 ? -35.638 53.430 12.551  1.00 33.96  ? 355 PRO A O   1 
ATOM   2876 C  CB  . PRO A 1 355 ? -35.607 56.704 12.421  1.00 30.46  ? 355 PRO A CB  1 
ATOM   2877 C  CG  . PRO A 1 355 ? -35.349 57.917 11.603  1.00 33.85  ? 355 PRO A CG  1 
ATOM   2878 C  CD  . PRO A 1 355 ? -35.783 57.545 10.199  1.00 25.73  ? 355 PRO A CD  1 
ATOM   2879 N  N   . VAL A 1 356 ? -37.333 54.193 11.293  1.00 27.66  ? 356 VAL A N   1 
ATOM   2880 C  CA  . VAL A 1 356 ? -38.193 53.055 11.597  1.00 32.41  ? 356 VAL A CA  1 
ATOM   2881 C  C   . VAL A 1 356 ? -38.166 52.002 10.486  1.00 32.86  ? 356 VAL A C   1 
ATOM   2882 O  O   . VAL A 1 356 ? -39.071 51.177 10.402  1.00 30.74  ? 356 VAL A O   1 
ATOM   2883 C  CB  . VAL A 1 356 ? -39.632 53.494 11.898  1.00 32.79  ? 356 VAL A CB  1 
ATOM   2884 C  CG1 . VAL A 1 356 ? -39.665 54.327 13.164  1.00 36.51  ? 356 VAL A CG1 1 
ATOM   2885 C  CG2 . VAL A 1 356 ? -40.214 54.251 10.718  1.00 31.81  ? 356 VAL A CG2 1 
ATOM   2886 N  N   . THR A 1 357 ? -37.146 52.004 9.639   1.00 25.35  ? 357 THR A N   1 
ATOM   2887 C  CA  . THR A 1 357 ? -37.065 51.010 8.583   1.00 24.35  ? 357 THR A CA  1 
ATOM   2888 C  C   . THR A 1 357 ? -36.375 49.759 9.106   1.00 23.93  ? 357 THR A C   1 
ATOM   2889 O  O   . THR A 1 357 ? -35.232 49.822 9.571   1.00 24.32  ? 357 THR A O   1 
ATOM   2890 C  CB  . THR A 1 357 ? -36.319 51.542 7.362   1.00 27.86  ? 357 THR A CB  1 
ATOM   2891 O  OG1 . THR A 1 357 ? -37.069 52.611 6.772   1.00 27.64  ? 357 THR A OG1 1 
ATOM   2892 C  CG2 . THR A 1 357 ? -36.151 50.437 6.339   1.00 24.52  ? 357 THR A CG2 1 
ATOM   2893 N  N   . MET A 1 358 ? -37.060 48.625 9.002   1.00 20.28  ? 358 MET A N   1 
ATOM   2894 C  CA  . MET A 1 358 ? -36.484 47.318 9.287   1.00 25.14  ? 358 MET A CA  1 
ATOM   2895 C  C   . MET A 1 358 ? -35.917 46.696 8.009   1.00 26.95  ? 358 MET A C   1 
ATOM   2896 O  O   . MET A 1 358 ? -36.309 47.038 6.889   1.00 26.14  ? 358 MET A O   1 
ATOM   2897 C  CB  . MET A 1 358 ? -37.542 46.391 9.896   1.00 20.46  ? 358 MET A CB  1 
ATOM   2898 C  CG  . MET A 1 358 ? -38.069 46.871 11.253  1.00 24.13  ? 358 MET A CG  1 
ATOM   2899 S  SD  . MET A 1 358 ? -39.643 46.126 11.705  1.00 30.31  ? 358 MET A SD  1 
ATOM   2900 C  CE  . MET A 1 358 ? -40.778 47.083 10.698  1.00 33.88  ? 358 MET A CE  1 
ATOM   2901 N  N   . ILE A 1 359 ? -34.994 45.768 8.189   1.00 22.13  ? 359 ILE A N   1 
ATOM   2902 C  CA  . ILE A 1 359 ? -34.462 44.980 7.087   1.00 21.02  ? 359 ILE A CA  1 
ATOM   2903 C  C   . ILE A 1 359 ? -35.292 43.716 6.930   1.00 28.46  ? 359 ILE A C   1 
ATOM   2904 O  O   . ILE A 1 359 ? -35.485 42.964 7.894   1.00 25.64  ? 359 ILE A O   1 
ATOM   2905 C  CB  . ILE A 1 359 ? -32.988 44.632 7.327   1.00 26.11  ? 359 ILE A CB  1 
ATOM   2906 C  CG1 . ILE A 1 359 ? -32.198 45.909 7.639   1.00 30.29  ? 359 ILE A CG1 1 
ATOM   2907 C  CG2 . ILE A 1 359 ? -32.424 43.910 6.101   1.00 17.29  ? 359 ILE A CG2 1 
ATOM   2908 C  CD1 . ILE A 1 359 ? -32.242 46.957 6.507   1.00 26.48  ? 359 ILE A CD1 1 
ATOM   2909 N  N   . GLY A 1 360 ? -35.779 43.480 5.718   1.00 23.86  ? 360 GLY A N   1 
ATOM   2910 C  CA  . GLY A 1 360 ? -36.315 42.188 5.352   1.00 24.98  ? 360 GLY A CA  1 
ATOM   2911 C  C   . GLY A 1 360 ? -35.746 41.733 4.023   1.00 29.36  ? 360 GLY A C   1 
ATOM   2912 O  O   . GLY A 1 360 ? -35.549 42.557 3.128   1.00 32.21  ? 360 GLY A O   1 
ATOM   2913 N  N   . SER A 1 361 ? -35.468 40.436 3.873   1.00 26.73  ? 361 SER A N   1 
ATOM   2914 C  CA  . SER A 1 361 ? -34.829 39.970 2.647   1.00 27.84  ? 361 SER A CA  1 
ATOM   2915 C  C   . SER A 1 361 ? -35.813 39.889 1.489   1.00 29.91  ? 361 SER A C   1 
ATOM   2916 O  O   . SER A 1 361 ? -35.424 40.086 0.330   1.00 25.78  ? 361 SER A O   1 
ATOM   2917 C  CB  . SER A 1 361 ? -34.198 38.596 2.859   1.00 22.33  ? 361 SER A CB  1 
ATOM   2918 O  OG  . SER A 1 361 ? -35.222 37.613 3.011   1.00 28.09  ? 361 SER A OG  1 
ATOM   2919 N  N   . ASP A 1 362 ? -37.080 39.612 1.779   1.00 26.23  ? 362 ASP A N   1 
ATOM   2920 C  CA  . ASP A 1 362 ? -38.053 39.332 0.732   1.00 31.89  ? 362 ASP A CA  1 
ATOM   2921 C  C   . ASP A 1 362 ? -37.504 38.264 -0.212  1.00 32.25  ? 362 ASP A C   1 
ATOM   2922 O  O   . ASP A 1 362 ? -37.721 38.299 -1.422  1.00 29.52  ? 362 ASP A O   1 
ATOM   2923 C  CB  . ASP A 1 362 ? -38.445 40.600 -0.039  1.00 27.48  ? 362 ASP A CB  1 
ATOM   2924 C  CG  . ASP A 1 362 ? -39.726 40.411 -0.857  1.00 31.44  ? 362 ASP A CG  1 
ATOM   2925 O  OD1 . ASP A 1 362 ? -40.495 39.468 -0.555  1.00 36.63  ? 362 ASP A OD1 1 
ATOM   2926 O  OD2 . ASP A 1 362 ? -39.973 41.199 -1.790  1.00 32.56  ? 362 ASP A OD2 1 
ATOM   2927 N  N   . GLY A 1 363 ? -36.801 37.289 0.359   1.00 34.51  ? 363 GLY A N   1 
ATOM   2928 C  CA  . GLY A 1 363 ? -36.271 36.200 -0.438  1.00 25.14  ? 363 GLY A CA  1 
ATOM   2929 C  C   . GLY A 1 363 ? -37.367 35.289 -0.961  1.00 31.02  ? 363 GLY A C   1 
ATOM   2930 O  O   . GLY A 1 363 ? -38.373 35.031 -0.295  1.00 31.29  ? 363 GLY A O   1 
ATOM   2931 N  N   . LEU A 1 364 ? -37.155 34.785 -2.175  1.00 32.26  ? 364 LEU A N   1 
ATOM   2932 C  CA  . LEU A 1 364 ? -38.084 33.873 -2.834  1.00 33.18  ? 364 LEU A CA  1 
ATOM   2933 C  C   . LEU A 1 364 ? -37.400 32.522 -3.002  1.00 32.50  ? 364 LEU A C   1 
ATOM   2934 O  O   . LEU A 1 364 ? -36.641 32.324 -3.964  1.00 39.38  ? 364 LEU A O   1 
ATOM   2935 C  CB  . LEU A 1 364 ? -38.530 34.431 -4.190  1.00 27.54  ? 364 LEU A CB  1 
ATOM   2936 C  CG  . LEU A 1 364 ? -39.192 35.814 -4.116  1.00 34.11  ? 364 LEU A CG  1 
ATOM   2937 C  CD1 . LEU A 1 364 ? -39.793 36.213 -5.460  1.00 28.80  ? 364 LEU A CD1 1 
ATOM   2938 C  CD2 . LEU A 1 364 ? -40.265 35.864 -3.039  1.00 25.45  ? 364 LEU A CD2 1 
ATOM   2939 N  N   . PRO A 1 365 ? -37.625 31.571 -2.093  1.00 33.89  ? 365 PRO A N   1 
ATOM   2940 C  CA  . PRO A 1 365 ? -36.812 30.346 -2.082  1.00 34.77  ? 365 PRO A CA  1 
ATOM   2941 C  C   . PRO A 1 365 ? -37.122 29.360 -3.188  1.00 40.59  ? 365 PRO A C   1 
ATOM   2942 O  O   . PRO A 1 365 ? -36.319 28.441 -3.399  1.00 45.80  ? 365 PRO A O   1 
ATOM   2943 C  CB  . PRO A 1 365 ? -37.131 29.726 -0.705  1.00 40.26  ? 365 PRO A CB  1 
ATOM   2944 C  CG  . PRO A 1 365 ? -38.452 30.330 -0.295  1.00 34.71  ? 365 PRO A CG  1 
ATOM   2945 C  CD  . PRO A 1 365 ? -38.430 31.724 -0.862  1.00 33.86  ? 365 PRO A CD  1 
ATOM   2946 N  N   . ASN A 1 366 ? -38.250 29.491 -3.882  1.00 36.46  ? 366 ASN A N   1 
ATOM   2947 C  CA  . ASN A 1 366 ? -38.590 28.556 -4.946  1.00 35.38  ? 366 ASN A CA  1 
ATOM   2948 C  C   . ASN A 1 366 ? -38.224 29.086 -6.319  1.00 31.68  ? 366 ASN A C   1 
ATOM   2949 O  O   . ASN A 1 366 ? -38.379 28.375 -7.312  1.00 42.61  ? 366 ASN A O   1 
ATOM   2950 C  CB  . ASN A 1 366 ? -40.074 28.198 -4.873  1.00 34.31  ? 366 ASN A CB  1 
ATOM   2951 C  CG  . ASN A 1 366 ? -40.414 27.443 -3.603  1.00 38.19  ? 366 ASN A CG  1 
ATOM   2952 O  OD1 . ASN A 1 366 ? -39.812 26.412 -3.306  1.00 46.70  ? 366 ASN A OD1 1 
ATOM   2953 N  ND2 . ASN A 1 366 ? -41.360 27.967 -2.828  1.00 35.84  ? 366 ASN A ND2 1 
ATOM   2954 N  N   . ASP A 1 367 ? -37.713 30.294 -6.384  1.00 32.80  ? 367 ASP A N   1 
ATOM   2955 C  CA  . ASP A 1 367 ? -37.257 30.872 -7.630  1.00 36.75  ? 367 ASP A CA  1 
ATOM   2956 C  C   . ASP A 1 367 ? -36.100 30.051 -8.200  1.00 44.43  ? 367 ASP A C   1 
ATOM   2957 O  O   . ASP A 1 367 ? -35.155 29.731 -7.468  1.00 35.47  ? 367 ASP A O   1 
ATOM   2958 C  CB  . ASP A 1 367 ? -36.831 32.306 -7.350  1.00 34.63  ? 367 ASP A CB  1 
ATOM   2959 C  CG  . ASP A 1 367 ? -36.545 33.103 -8.596  1.00 40.26  ? 367 ASP A CG  1 
ATOM   2960 O  OD1 . ASP A 1 367 ? -36.195 32.520 -9.652  1.00 50.59  ? 367 ASP A OD1 1 
ATOM   2961 O  OD2 . ASP A 1 367 ? -36.643 34.344 -8.498  1.00 43.59  ? 367 ASP A OD2 1 
ATOM   2962 N  N   . PRO A 1 368 ? -36.134 29.687 -9.487  1.00 46.29  ? 368 PRO A N   1 
ATOM   2963 C  CA  . PRO A 1 368 ? -35.030 28.888 -10.054 1.00 50.98  ? 368 PRO A CA  1 
ATOM   2964 C  C   . PRO A 1 368 ? -33.683 29.603 -10.046 1.00 52.54  ? 368 PRO A C   1 
ATOM   2965 O  O   . PRO A 1 368 ? -32.645 28.940 -9.899  1.00 48.27  ? 368 PRO A O   1 
ATOM   2966 C  CB  . PRO A 1 368 ? -35.499 28.606 -11.490 1.00 54.32  ? 368 PRO A CB  1 
ATOM   2967 C  CG  . PRO A 1 368 ? -36.951 28.899 -11.508 1.00 48.13  ? 368 PRO A CG  1 
ATOM   2968 C  CD  . PRO A 1 368 ? -37.189 29.958 -10.474 1.00 40.86  ? 368 PRO A CD  1 
ATOM   2969 N  N   . MET A 1 369 ? -33.667 30.927 -10.229 1.00 38.88  ? 369 MET A N   1 
ATOM   2970 C  CA  . MET A 1 369 ? -32.450 31.739 -10.155 1.00 39.62  ? 369 MET A CA  1 
ATOM   2971 C  C   . MET A 1 369 ? -32.733 32.875 -9.184  1.00 32.26  ? 369 MET A C   1 
ATOM   2972 O  O   . MET A 1 369 ? -33.166 33.961 -9.594  1.00 34.13  ? 369 MET A O   1 
ATOM   2973 C  CB  . MET A 1 369 ? -32.045 32.271 -11.532 1.00 38.46  ? 369 MET A CB  1 
ATOM   2974 C  CG  . MET A 1 369 ? -30.811 31.626 -12.112 1.00 45.73  ? 369 MET A CG  1 
ATOM   2975 S  SD  . MET A 1 369 ? -29.334 32.234 -11.283 1.00 51.76  ? 369 MET A SD  1 
ATOM   2976 C  CE  . MET A 1 369 ? -29.834 33.932 -11.023 1.00 42.42  ? 369 MET A CE  1 
ATOM   2977 N  N   . PRO A 1 370 ? -32.508 32.660 -7.887  1.00 36.27  ? 370 PRO A N   1 
ATOM   2978 C  CA  . PRO A 1 370 ? -33.020 33.609 -6.888  1.00 34.63  ? 370 PRO A CA  1 
ATOM   2979 C  C   . PRO A 1 370 ? -32.267 34.930 -6.896  1.00 30.96  ? 370 PRO A C   1 
ATOM   2980 O  O   . PRO A 1 370 ? -31.055 34.974 -7.118  1.00 28.92  ? 370 PRO A O   1 
ATOM   2981 C  CB  . PRO A 1 370 ? -32.822 32.868 -5.559  1.00 30.61  ? 370 PRO A CB  1 
ATOM   2982 C  CG  . PRO A 1 370 ? -31.699 31.906 -5.825  1.00 34.68  ? 370 PRO A CG  1 
ATOM   2983 C  CD  . PRO A 1 370 ? -31.912 31.464 -7.259  1.00 33.10  ? 370 PRO A CD  1 
ATOM   2984 N  N   . HIS A 1 371 ? -33.019 36.011 -6.672  1.00 23.07  ? 371 HIS A N   1 
ATOM   2985 C  CA  . HIS A 1 371 ? -32.449 37.292 -6.288  1.00 23.66  ? 371 HIS A CA  1 
ATOM   2986 C  C   . HIS A 1 371 ? -31.522 37.093 -5.087  1.00 26.34  ? 371 HIS A C   1 
ATOM   2987 O  O   . HIS A 1 371 ? -31.903 36.405 -4.127  1.00 28.58  ? 371 HIS A O   1 
ATOM   2988 C  CB  . HIS A 1 371 ? -33.584 38.262 -5.945  1.00 25.40  ? 371 HIS A CB  1 
ATOM   2989 C  CG  . HIS A 1 371 ? -33.156 39.687 -5.792  1.00 24.83  ? 371 HIS A CG  1 
ATOM   2990 N  ND1 . HIS A 1 371 ? -32.158 40.079 -4.923  1.00 25.43  ? 371 HIS A ND1 1 
ATOM   2991 C  CD2 . HIS A 1 371 ? -33.618 40.821 -6.373  1.00 25.35  ? 371 HIS A CD2 1 
ATOM   2992 C  CE1 . HIS A 1 371 ? -32.013 41.392 -4.987  1.00 27.51  ? 371 HIS A CE1 1 
ATOM   2993 N  NE2 . HIS A 1 371 ? -32.887 41.867 -5.861  1.00 26.62  ? 371 HIS A NE2 1 
ATOM   2994 N  N   . PRO A 1 372 ? -30.306 37.652 -5.107  1.00 28.45  ? 372 PRO A N   1 
ATOM   2995 C  CA  . PRO A 1 372 ? -29.326 37.326 -4.060  1.00 24.96  ? 372 PRO A CA  1 
ATOM   2996 C  C   . PRO A 1 372 ? -29.728 37.799 -2.673  1.00 31.34  ? 372 PRO A C   1 
ATOM   2997 O  O   . PRO A 1 372 ? -29.096 37.383 -1.691  1.00 24.92  ? 372 PRO A O   1 
ATOM   2998 C  CB  . PRO A 1 372 ? -28.049 38.029 -4.543  1.00 29.35  ? 372 PRO A CB  1 
ATOM   2999 C  CG  . PRO A 1 372 ? -28.543 39.155 -5.412  1.00 28.61  ? 372 PRO A CG  1 
ATOM   3000 C  CD  . PRO A 1 372 ? -29.760 38.589 -6.106  1.00 25.62  ? 372 PRO A CD  1 
ATOM   3001 N  N   . ARG A 1 373 ? -30.749 38.652 -2.554  1.00 26.43  ? 373 ARG A N   1 
ATOM   3002 C  CA  . ARG A 1 373 ? -31.219 39.042 -1.231  1.00 23.58  ? 373 ARG A CA  1 
ATOM   3003 C  C   . ARG A 1 373 ? -31.605 37.821 -0.402  1.00 25.30  ? 373 ARG A C   1 
ATOM   3004 O  O   . ARG A 1 373 ? -31.558 37.864 0.831   1.00 26.09  ? 373 ARG A O   1 
ATOM   3005 C  CB  . ARG A 1 373 ? -32.411 39.988 -1.360  1.00 20.70  ? 373 ARG A CB  1 
ATOM   3006 C  CG  . ARG A 1 373 ? -33.632 39.353 -2.027  1.00 25.08  ? 373 ARG A CG  1 
ATOM   3007 C  CD  . ARG A 1 373 ? -34.605 40.416 -2.497  1.00 28.02  ? 373 ARG A CD  1 
ATOM   3008 N  NE  . ARG A 1 373 ? -35.908 39.854 -2.841  1.00 25.21  ? 373 ARG A NE  1 
ATOM   3009 C  CZ  . ARG A 1 373 ? -36.723 40.384 -3.748  1.00 31.95  ? 373 ARG A CZ  1 
ATOM   3010 N  NH1 . ARG A 1 373 ? -36.379 41.456 -4.450  1.00 27.14  ? 373 ARG A NH1 1 
ATOM   3011 N  NH2 . ARG A 1 373 ? -37.907 39.821 -3.970  1.00 24.42  ? 373 ARG A NH2 1 
ATOM   3012 N  N   . LEU A 1 374 ? -32.003 36.733 -1.070  1.00 27.17  ? 374 LEU A N   1 
ATOM   3013 C  CA  . LEU A 1 374 ? -32.350 35.500 -0.377  1.00 26.54  ? 374 LEU A CA  1 
ATOM   3014 C  C   . LEU A 1 374 ? -31.191 34.993 0.470   1.00 26.71  ? 374 LEU A C   1 
ATOM   3015 O  O   . LEU A 1 374 ? -31.410 34.423 1.549   1.00 30.13  ? 374 LEU A O   1 
ATOM   3016 C  CB  . LEU A 1 374 ? -32.781 34.451 -1.398  1.00 21.29  ? 374 LEU A CB  1 
ATOM   3017 C  CG  . LEU A 1 374 ? -32.934 33.010 -0.924  1.00 31.59  ? 374 LEU A CG  1 
ATOM   3018 C  CD1 . LEU A 1 374 ? -34.022 32.917 0.125   1.00 25.41  ? 374 LEU A CD1 1 
ATOM   3019 C  CD2 . LEU A 1 374 ? -33.219 32.090 -2.136  1.00 28.50  ? 374 LEU A CD2 1 
ATOM   3020 N  N   . TRP A 1 375 ? -29.960 35.233 0.022   1.00 26.20  ? 375 TRP A N   1 
ATOM   3021 C  CA  . TRP A 1 375 ? -28.750 34.781 0.693   1.00 28.37  ? 375 TRP A CA  1 
ATOM   3022 C  C   . TRP A 1 375 ? -27.875 35.910 1.219   1.00 25.42  ? 375 TRP A C   1 
ATOM   3023 O  O   . TRP A 1 375 ? -26.845 35.626 1.842   1.00 24.81  ? 375 TRP A O   1 
ATOM   3024 C  CB  . TRP A 1 375 ? -27.903 33.938 -0.268  1.00 31.03  ? 375 TRP A CB  1 
ATOM   3025 C  CG  . TRP A 1 375 ? -28.418 32.573 -0.589  1.00 31.26  ? 375 TRP A CG  1 
ATOM   3026 C  CD1 . TRP A 1 375 ? -29.383 32.245 -1.503  1.00 28.28  ? 375 TRP A CD1 1 
ATOM   3027 C  CD2 . TRP A 1 375 ? -27.943 31.334 -0.040  1.00 35.88  ? 375 TRP A CD2 1 
ATOM   3028 N  NE1 . TRP A 1 375 ? -29.552 30.880 -1.540  1.00 30.98  ? 375 TRP A NE1 1 
ATOM   3029 C  CE2 . TRP A 1 375 ? -28.684 30.297 -0.649  1.00 34.01  ? 375 TRP A CE2 1 
ATOM   3030 C  CE3 . TRP A 1 375 ? -26.970 31.002 0.918   1.00 32.85  ? 375 TRP A CE3 1 
ATOM   3031 C  CZ2 . TRP A 1 375 ? -28.487 28.950 -0.329  1.00 30.30  ? 375 TRP A CZ2 1 
ATOM   3032 C  CZ3 . TRP A 1 375 ? -26.773 29.663 1.237   1.00 28.55  ? 375 TRP A CZ3 1 
ATOM   3033 C  CH2 . TRP A 1 375 ? -27.526 28.654 0.610   1.00 31.70  ? 375 TRP A CH2 1 
ATOM   3034 N  N   . GLY A 1 376 ? -28.221 37.175 0.973   1.00 28.94  ? 376 GLY A N   1 
ATOM   3035 C  CA  . GLY A 1 376 ? -27.257 38.222 1.279   1.00 25.21  ? 376 GLY A CA  1 
ATOM   3036 C  C   . GLY A 1 376 ? -27.741 39.485 1.964   1.00 23.51  ? 376 GLY A C   1 
ATOM   3037 O  O   . GLY A 1 376 ? -26.918 40.319 2.354   1.00 26.41  ? 376 GLY A O   1 
ATOM   3038 N  N   . ALA A 1 377 ? -29.055 39.646 2.126   1.00 23.13  ? 377 ALA A N   1 
ATOM   3039 C  CA  . ALA A 1 377 ? -29.604 40.920 2.599   1.00 25.94  ? 377 ALA A CA  1 
ATOM   3040 C  C   . ALA A 1 377 ? -28.949 41.405 3.891   1.00 28.97  ? 377 ALA A C   1 
ATOM   3041 O  O   . ALA A 1 377 ? -28.551 42.573 3.997   1.00 26.20  ? 377 ALA A O   1 
ATOM   3042 C  CB  . ALA A 1 377 ? -31.112 40.800 2.811   1.00 21.37  ? 377 ALA A CB  1 
ATOM   3043 N  N   . PHE A 1 378 ? -28.864 40.535 4.912   1.00 20.27  ? 378 PHE A N   1 
ATOM   3044 C  CA  . PHE A 1 378 ? -28.451 41.022 6.231   1.00 21.42  ? 378 PHE A CA  1 
ATOM   3045 C  C   . PHE A 1 378 ? -26.967 41.332 6.296   1.00 23.05  ? 378 PHE A C   1 
ATOM   3046 O  O   . PHE A 1 378 ? -26.614 42.466 6.668   1.00 24.68  ? 378 PHE A O   1 
ATOM   3047 C  CB  . PHE A 1 378 ? -28.924 40.045 7.316   1.00 24.07  ? 378 PHE A CB  1 
ATOM   3048 C  CG  . PHE A 1 378 ? -30.424 39.990 7.394   1.00 24.03  ? 378 PHE A CG  1 
ATOM   3049 C  CD1 . PHE A 1 378 ? -31.129 40.908 8.170   1.00 20.39  ? 378 PHE A CD1 1 
ATOM   3050 C  CD2 . PHE A 1 378 ? -31.129 39.126 6.581   1.00 19.19  ? 378 PHE A CD2 1 
ATOM   3051 C  CE1 . PHE A 1 378 ? -32.517 40.920 8.173   1.00 27.83  ? 378 PHE A CE1 1 
ATOM   3052 C  CE2 . PHE A 1 378 ? -32.515 39.135 6.582   1.00 26.56  ? 378 PHE A CE2 1 
ATOM   3053 C  CZ  . PHE A 1 378 ? -33.212 40.028 7.384   1.00 22.50  ? 378 PHE A CZ  1 
ATOM   3054 N  N   . PRO A 1 379 ? -26.051 40.439 5.911   1.00 24.78  ? 379 PRO A N   1 
ATOM   3055 C  CA  . PRO A 1 379 ? -24.639 40.842 5.851   1.00 20.63  ? 379 PRO A CA  1 
ATOM   3056 C  C   . PRO A 1 379 ? -24.392 42.001 4.909   1.00 25.46  ? 379 PRO A C   1 
ATOM   3057 O  O   . PRO A 1 379 ? -23.411 42.728 5.096   1.00 26.40  ? 379 PRO A O   1 
ATOM   3058 C  CB  . PRO A 1 379 ? -23.915 39.568 5.388   1.00 27.70  ? 379 PRO A CB  1 
ATOM   3059 C  CG  . PRO A 1 379 ? -24.988 38.634 4.915   1.00 26.53  ? 379 PRO A CG  1 
ATOM   3060 C  CD  . PRO A 1 379 ? -26.235 38.999 5.655   1.00 24.43  ? 379 PRO A CD  1 
ATOM   3061 N  N   . ARG A 1 380 ? -25.254 42.214 3.912   1.00 25.17  ? 380 ARG A N   1 
ATOM   3062 C  CA  . ARG A 1 380 ? -25.067 43.356 3.023   1.00 25.79  ? 380 ARG A CA  1 
ATOM   3063 C  C   . ARG A 1 380 ? -25.315 44.664 3.758   1.00 25.51  ? 380 ARG A C   1 
ATOM   3064 O  O   . ARG A 1 380 ? -24.649 45.670 3.495   1.00 26.40  ? 380 ARG A O   1 
ATOM   3065 C  CB  . ARG A 1 380 ? -25.987 43.225 1.804   1.00 24.90  ? 380 ARG A CB  1 
ATOM   3066 C  CG  . ARG A 1 380 ? -25.937 44.400 0.825   1.00 23.81  ? 380 ARG A CG  1 
ATOM   3067 C  CD  . ARG A 1 380 ? -26.717 44.069 -0.454  1.00 27.32  ? 380 ARG A CD  1 
ATOM   3068 N  NE  . ARG A 1 380 ? -26.705 45.162 -1.420  1.00 32.63  ? 380 ARG A NE  1 
ATOM   3069 C  CZ  . ARG A 1 380 ? -25.638 45.527 -2.121  1.00 29.29  ? 380 ARG A CZ  1 
ATOM   3070 N  NH1 . ARG A 1 380 ? -24.474 44.915 -1.975  1.00 29.83  ? 380 ARG A NH1 1 
ATOM   3071 N  NH2 . ARG A 1 380 ? -25.739 46.536 -2.981  1.00 28.83  ? 380 ARG A NH2 1 
ATOM   3072 N  N   . VAL A 1 381 ? -26.240 44.661 4.710   1.00 27.16  ? 381 VAL A N   1 
ATOM   3073 C  CA  . VAL A 1 381 ? -26.478 45.859 5.498   1.00 22.11  ? 381 VAL A CA  1 
ATOM   3074 C  C   . VAL A 1 381 ? -25.330 46.089 6.476   1.00 27.58  ? 381 VAL A C   1 
ATOM   3075 O  O   . VAL A 1 381 ? -24.860 47.221 6.657   1.00 30.38  ? 381 VAL A O   1 
ATOM   3076 C  CB  . VAL A 1 381 ? -27.841 45.750 6.207   1.00 26.02  ? 381 VAL A CB  1 
ATOM   3077 C  CG1 . VAL A 1 381 ? -27.972 46.812 7.273   1.00 23.35  ? 381 VAL A CG1 1 
ATOM   3078 C  CG2 . VAL A 1 381 ? -28.990 45.861 5.178   1.00 21.69  ? 381 VAL A CG2 1 
ATOM   3079 N  N   . LEU A 1 382 ? -24.836 45.020 7.097   1.00 23.99  ? 382 LEU A N   1 
ATOM   3080 C  CA  . LEU A 1 382 ? -23.800 45.183 8.115   1.00 25.50  ? 382 LEU A CA  1 
ATOM   3081 C  C   . LEU A 1 382 ? -22.464 45.536 7.488   1.00 30.39  ? 382 LEU A C   1 
ATOM   3082 O  O   . LEU A 1 382 ? -21.692 46.309 8.066   1.00 29.95  ? 382 LEU A O   1 
ATOM   3083 C  CB  . LEU A 1 382 ? -23.659 43.906 8.942   1.00 26.33  ? 382 LEU A CB  1 
ATOM   3084 C  CG  . LEU A 1 382 ? -24.933 43.384 9.595   1.00 26.14  ? 382 LEU A CG  1 
ATOM   3085 C  CD1 . LEU A 1 382 ? -24.657 42.032 10.234  1.00 33.10  ? 382 LEU A CD1 1 
ATOM   3086 C  CD2 . LEU A 1 382 ? -25.385 44.380 10.629  1.00 18.54  ? 382 LEU A CD2 1 
ATOM   3087 N  N   . GLY A 1 383 ? -22.169 44.967 6.315   1.00 22.16  ? 383 GLY A N   1 
ATOM   3088 C  CA  . GLY A 1 383 ? -20.874 45.146 5.695   1.00 22.20  ? 383 GLY A CA  1 
ATOM   3089 C  C   . GLY A 1 383 ? -20.877 46.265 4.680   1.00 32.09  ? 383 GLY A C   1 
ATOM   3090 O  O   . GLY A 1 383 ? -20.277 47.318 4.911   1.00 29.78  ? 383 GLY A O   1 
ATOM   3091 N  N   . HIS A 1 384 ? -21.573 46.059 3.558   1.00 30.47  ? 384 HIS A N   1 
ATOM   3092 C  CA  . HIS A 1 384 ? -21.524 47.030 2.468   1.00 27.24  ? 384 HIS A CA  1 
ATOM   3093 C  C   . HIS A 1 384 ? -22.071 48.394 2.898   1.00 29.81  ? 384 HIS A C   1 
ATOM   3094 O  O   . HIS A 1 384 ? -21.425 49.429 2.692   1.00 27.91  ? 384 HIS A O   1 
ATOM   3095 C  CB  . HIS A 1 384 ? -22.287 46.494 1.257   1.00 24.18  ? 384 HIS A CB  1 
ATOM   3096 C  CG  . HIS A 1 384 ? -22.385 47.472 0.131   1.00 33.14  ? 384 HIS A CG  1 
ATOM   3097 N  ND1 . HIS A 1 384 ? -21.290 47.869 -0.607  1.00 32.51  ? 384 HIS A ND1 1 
ATOM   3098 C  CD2 . HIS A 1 384 ? -23.447 48.137 -0.384  1.00 27.67  ? 384 HIS A CD2 1 
ATOM   3099 C  CE1 . HIS A 1 384 ? -21.671 48.740 -1.521  1.00 29.18  ? 384 HIS A CE1 1 
ATOM   3100 N  NE2 . HIS A 1 384 ? -22.975 48.921 -1.407  1.00 30.81  ? 384 HIS A NE2 1 
ATOM   3101 N  N   . TYR A 1 385 ? -23.261 48.422 3.495   1.00 26.62  ? 385 TYR A N   1 
ATOM   3102 C  CA  . TYR A 1 385 ? -23.901 49.712 3.743   1.00 27.76  ? 385 TYR A CA  1 
ATOM   3103 C  C   . TYR A 1 385 ? -23.431 50.376 5.037   1.00 27.92  ? 385 TYR A C   1 
ATOM   3104 O  O   . TYR A 1 385 ? -23.242 51.594 5.063   1.00 30.93  ? 385 TYR A O   1 
ATOM   3105 C  CB  . TYR A 1 385 ? -25.421 49.552 3.740   1.00 31.49  ? 385 TYR A CB  1 
ATOM   3106 C  CG  . TYR A 1 385 ? -25.968 49.407 2.332   1.00 30.90  ? 385 TYR A CG  1 
ATOM   3107 C  CD1 . TYR A 1 385 ? -25.821 50.427 1.403   1.00 33.31  ? 385 TYR A CD1 1 
ATOM   3108 C  CD2 . TYR A 1 385 ? -26.602 48.241 1.929   1.00 25.13  ? 385 TYR A CD2 1 
ATOM   3109 C  CE1 . TYR A 1 385 ? -26.294 50.293 0.108   1.00 32.93  ? 385 TYR A CE1 1 
ATOM   3110 C  CE2 . TYR A 1 385 ? -27.088 48.095 0.647   1.00 29.96  ? 385 TYR A CE2 1 
ATOM   3111 C  CZ  . TYR A 1 385 ? -26.935 49.119 -0.262  1.00 32.88  ? 385 TYR A CZ  1 
ATOM   3112 O  OH  . TYR A 1 385 ? -27.420 48.957 -1.531  1.00 36.31  ? 385 TYR A OH  1 
ATOM   3113 N  N   . SER A 1 386 ? -23.239 49.616 6.120   1.00 30.92  ? 386 SER A N   1 
ATOM   3114 C  CA  . SER A 1 386 ? -22.827 50.237 7.379   1.00 26.92  ? 386 SER A CA  1 
ATOM   3115 C  C   . SER A 1 386 ? -21.321 50.473 7.411   1.00 29.41  ? 386 SER A C   1 
ATOM   3116 O  O   . SER A 1 386 ? -20.863 51.606 7.574   1.00 25.85  ? 386 SER A O   1 
ATOM   3117 C  CB  . SER A 1 386 ? -23.257 49.375 8.572   1.00 28.53  ? 386 SER A CB  1 
ATOM   3118 O  OG  . SER A 1 386 ? -22.913 50.004 9.807   1.00 28.76  ? 386 SER A OG  1 
ATOM   3119 N  N   . ARG A 1 387 ? -20.533 49.407 7.257   1.00 28.78  ? 387 ARG A N   1 
ATOM   3120 C  CA  . ARG A 1 387 ? -19.080 49.551 7.267   1.00 29.66  ? 387 ARG A CA  1 
ATOM   3121 C  C   . ARG A 1 387 ? -18.583 50.381 6.084   1.00 36.96  ? 387 ARG A C   1 
ATOM   3122 O  O   . ARG A 1 387 ? -17.987 51.450 6.267   1.00 33.60  ? 387 ARG A O   1 
ATOM   3123 C  CB  . ARG A 1 387 ? -18.409 48.179 7.262   1.00 29.29  ? 387 ARG A CB  1 
ATOM   3124 C  CG  . ARG A 1 387 ? -16.891 48.242 7.514   1.00 26.85  ? 387 ARG A CG  1 
ATOM   3125 C  CD  . ARG A 1 387 ? -16.220 46.904 7.163   1.00 31.66  ? 387 ARG A CD  1 
ATOM   3126 N  NE  . ARG A 1 387 ? -16.678 46.398 5.872   1.00 32.73  ? 387 ARG A NE  1 
ATOM   3127 C  CZ  . ARG A 1 387 ? -17.249 45.218 5.664   1.00 32.40  ? 387 ARG A CZ  1 
ATOM   3128 N  NH1 . ARG A 1 387 ? -17.390 44.331 6.638   1.00 28.84  ? 387 ARG A NH1 1 
ATOM   3129 N  NH2 . ARG A 1 387 ? -17.683 44.918 4.445   1.00 28.34  ? 387 ARG A NH2 1 
ATOM   3130 N  N   . ASP A 1 388 ? -18.811 49.898 4.855   1.00 35.09  ? 388 ASP A N   1 
ATOM   3131 C  CA  . ASP A 1 388 ? -18.137 50.476 3.692   1.00 35.47  ? 388 ASP A CA  1 
ATOM   3132 C  C   . ASP A 1 388 ? -18.753 51.807 3.271   1.00 37.82  ? 388 ASP A C   1 
ATOM   3133 O  O   . ASP A 1 388 ? -18.033 52.787 3.063   1.00 36.38  ? 388 ASP A O   1 
ATOM   3134 C  CB  . ASP A 1 388 ? -18.143 49.477 2.530   1.00 34.39  ? 388 ASP A CB  1 
ATOM   3135 C  CG  . ASP A 1 388 ? -17.457 48.170 2.894   1.00 35.85  ? 388 ASP A CG  1 
ATOM   3136 O  OD1 . ASP A 1 388 ? -16.524 48.227 3.712   1.00 35.06  ? 388 ASP A OD1 1 
ATOM   3137 O  OD2 . ASP A 1 388 ? -17.849 47.090 2.393   1.00 40.75  ? 388 ASP A OD2 1 
ATOM   3138 N  N   . GLU A 1 389 ? -20.078 51.877 3.142   1.00 37.23  ? 389 GLU A N   1 
ATOM   3139 C  CA  . GLU A 1 389 ? -20.684 53.134 2.707   1.00 35.83  ? 389 GLU A CA  1 
ATOM   3140 C  C   . GLU A 1 389 ? -21.009 54.078 3.865   1.00 35.52  ? 389 GLU A C   1 
ATOM   3141 O  O   . GLU A 1 389 ? -21.273 55.258 3.625   1.00 33.14  ? 389 GLU A O   1 
ATOM   3142 C  CB  . GLU A 1 389 ? -21.953 52.865 1.884   1.00 37.38  ? 389 GLU A CB  1 
ATOM   3143 C  CG  . GLU A 1 389 ? -21.742 52.034 0.619   1.00 39.88  ? 389 GLU A CG  1 
ATOM   3144 C  CD  . GLU A 1 389 ? -20.963 52.770 -0.458  1.00 48.50  ? 389 GLU A CD  1 
ATOM   3145 O  OE1 . GLU A 1 389 ? -21.216 53.970 -0.680  1.00 50.49  ? 389 GLU A OE1 1 
ATOM   3146 O  OE2 . GLU A 1 389 ? -20.081 52.142 -1.080  1.00 60.69  ? 389 GLU A OE2 1 
ATOM   3147 N  N   . GLN A 1 390 ? -20.999 53.597 5.107   1.00 33.86  ? 390 GLN A N   1 
ATOM   3148 C  CA  . GLN A 1 390 ? -21.182 54.461 6.275   1.00 35.80  ? 390 GLN A CA  1 
ATOM   3149 C  C   . GLN A 1 390 ? -22.553 55.129 6.270   1.00 28.52  ? 390 GLN A C   1 
ATOM   3150 O  O   . GLN A 1 390 ? -22.691 56.297 6.649   1.00 28.22  ? 390 GLN A O   1 
ATOM   3151 C  CB  . GLN A 1 390 ? -20.067 55.509 6.369   1.00 29.90  ? 390 GLN A CB  1 
ATOM   3152 C  CG  . GLN A 1 390 ? -18.675 54.880 6.346   1.00 41.81  ? 390 GLN A CG  1 
ATOM   3153 C  CD  . GLN A 1 390 ? -17.549 55.871 6.620   1.00 48.87  ? 390 GLN A CD  1 
ATOM   3154 O  OE1 . GLN A 1 390 ? -16.995 55.895 7.716   1.00 73.20  ? 390 GLN A OE1 1 
ATOM   3155 N  NE2 . GLN A 1 390 ? -17.187 56.667 5.615   1.00 49.75  ? 390 GLN A NE2 1 
ATOM   3156 N  N   . LEU A 1 391 ? -23.576 54.370 5.859   1.00 25.97  ? 391 LEU A N   1 
ATOM   3157 C  CA  . LEU A 1 391 ? -24.957 54.855 5.893   1.00 32.60  ? 391 LEU A CA  1 
ATOM   3158 C  C   . LEU A 1 391 ? -25.456 55.056 7.315   1.00 30.77  ? 391 LEU A C   1 
ATOM   3159 O  O   . LEU A 1 391 ? -26.332 55.891 7.556   1.00 34.20  ? 391 LEU A O   1 
ATOM   3160 C  CB  . LEU A 1 391 ? -25.887 53.871 5.187   1.00 25.10  ? 391 LEU A CB  1 
ATOM   3161 C  CG  . LEU A 1 391 ? -26.383 54.250 3.806   1.00 40.95  ? 391 LEU A CG  1 
ATOM   3162 C  CD1 . LEU A 1 391 ? -25.194 54.435 2.872   1.00 40.07  ? 391 LEU A CD1 1 
ATOM   3163 C  CD2 . LEU A 1 391 ? -27.345 53.191 3.283   1.00 32.16  ? 391 LEU A CD2 1 
ATOM   3164 N  N   . PHE A 1 392 ? -24.945 54.285 8.247   1.00 32.24  ? 392 PHE A N   1 
ATOM   3165 C  CA  . PHE A 1 392 ? -25.337 54.374 9.641   1.00 31.94  ? 392 PHE A CA  1 
ATOM   3166 C  C   . PHE A 1 392 ? -24.321 53.589 10.455  1.00 29.54  ? 392 PHE A C   1 
ATOM   3167 O  O   . PHE A 1 392 ? -23.702 52.661 9.924   1.00 28.18  ? 392 PHE A O   1 
ATOM   3168 C  CB  . PHE A 1 392 ? -26.759 53.839 9.855   1.00 25.98  ? 392 PHE A CB  1 
ATOM   3169 C  CG  . PHE A 1 392 ? -27.172 52.764 8.883   1.00 28.92  ? 392 PHE A CG  1 
ATOM   3170 C  CD1 . PHE A 1 392 ? -26.391 51.627 8.702   1.00 29.35  ? 392 PHE A CD1 1 
ATOM   3171 C  CD2 . PHE A 1 392 ? -28.359 52.885 8.157   1.00 34.91  ? 392 PHE A CD2 1 
ATOM   3172 C  CE1 . PHE A 1 392 ? -26.768 50.630 7.806   1.00 28.66  ? 392 PHE A CE1 1 
ATOM   3173 C  CE2 . PHE A 1 392 ? -28.755 51.892 7.249   1.00 25.47  ? 392 PHE A CE2 1 
ATOM   3174 C  CZ  . PHE A 1 392 ? -27.956 50.761 7.075   1.00 32.57  ? 392 PHE A CZ  1 
ATOM   3175 N  N   . PRO A 1 393 ? -24.122 53.925 11.731  1.00 31.06  ? 393 PRO A N   1 
ATOM   3176 C  CA  . PRO A 1 393 ? -23.217 53.132 12.573  1.00 24.75  ? 393 PRO A CA  1 
ATOM   3177 C  C   . PRO A 1 393 ? -23.705 51.698 12.728  1.00 25.14  ? 393 PRO A C   1 
ATOM   3178 O  O   . PRO A 1 393 ? -24.872 51.368 12.499  1.00 26.93  ? 393 PRO A O   1 
ATOM   3179 C  CB  . PRO A 1 393 ? -23.222 53.878 13.917  1.00 29.36  ? 393 PRO A CB  1 
ATOM   3180 C  CG  . PRO A 1 393 ? -24.499 54.673 13.915  1.00 33.09  ? 393 PRO A CG  1 
ATOM   3181 C  CD  . PRO A 1 393 ? -24.761 55.030 12.470  1.00 32.36  ? 393 PRO A CD  1 
ATOM   3182 N  N   . LEU A 1 394 ? -22.782 50.826 13.121  1.00 23.18  ? 394 LEU A N   1 
ATOM   3183 C  CA  . LEU A 1 394 ? -23.123 49.413 13.175  1.00 23.37  ? 394 LEU A CA  1 
ATOM   3184 C  C   . LEU A 1 394 ? -24.191 49.122 14.231  1.00 26.81  ? 394 LEU A C   1 
ATOM   3185 O  O   . LEU A 1 394 ? -24.981 48.180 14.067  1.00 23.23  ? 394 LEU A O   1 
ATOM   3186 C  CB  . LEU A 1 394 ? -21.859 48.591 13.423  1.00 27.11  ? 394 LEU A CB  1 
ATOM   3187 C  CG  . LEU A 1 394 ? -22.031 47.078 13.278  1.00 27.47  ? 394 LEU A CG  1 
ATOM   3188 C  CD1 . LEU A 1 394 ? -22.474 46.739 11.854  1.00 22.51  ? 394 LEU A CD1 1 
ATOM   3189 C  CD2 . LEU A 1 394 ? -20.741 46.366 13.626  1.00 23.38  ? 394 LEU A CD2 1 
ATOM   3190 N  N   . THR A 1 395 ? -24.233 49.903 15.318  1.00 25.43  ? 395 THR A N   1 
ATOM   3191 C  CA  . THR A 1 395 ? -25.287 49.712 16.313  1.00 27.15  ? 395 THR A CA  1 
ATOM   3192 C  C   . THR A 1 395 ? -26.654 49.983 15.703  1.00 30.51  ? 395 THR A C   1 
ATOM   3193 O  O   . THR A 1 395 ? -27.623 49.259 15.970  1.00 29.45  ? 395 THR A O   1 
ATOM   3194 C  CB  . THR A 1 395 ? -25.062 50.619 17.528  1.00 25.71  ? 395 THR A CB  1 
ATOM   3195 O  OG1 . THR A 1 395 ? -24.899 51.972 17.085  1.00 25.98  ? 395 THR A OG1 1 
ATOM   3196 C  CG2 . THR A 1 395 ? -23.813 50.179 18.363  1.00 23.47  ? 395 THR A CG2 1 
ATOM   3197 N  N   . THR A 1 396 ? -26.753 51.015 14.863  1.00 24.58  ? 396 THR A N   1 
ATOM   3198 C  CA  . THR A 1 396 ? -28.013 51.267 14.179  1.00 25.02  ? 396 THR A CA  1 
ATOM   3199 C  C   . THR A 1 396 ? -28.334 50.158 13.190  1.00 21.26  ? 396 THR A C   1 
ATOM   3200 O  O   . THR A 1 396 ? -29.477 49.679 13.128  1.00 24.16  ? 396 THR A O   1 
ATOM   3201 C  CB  . THR A 1 396 ? -27.962 52.613 13.472  1.00 26.84  ? 396 THR A CB  1 
ATOM   3202 O  OG1 . THR A 1 396 ? -27.798 53.645 14.447  1.00 27.16  ? 396 THR A OG1 1 
ATOM   3203 C  CG2 . THR A 1 396 ? -29.228 52.838 12.677  1.00 22.35  ? 396 THR A CG2 1 
ATOM   3204 N  N   . ALA A 1 397 ? -27.339 49.737 12.407  1.00 23.84  ? 397 ALA A N   1 
ATOM   3205 C  CA  . ALA A 1 397 ? -27.553 48.659 11.442  1.00 24.63  ? 397 ALA A CA  1 
ATOM   3206 C  C   . ALA A 1 397 ? -28.110 47.411 12.122  1.00 29.69  ? 397 ALA A C   1 
ATOM   3207 O  O   . ALA A 1 397 ? -29.087 46.815 11.650  1.00 24.21  ? 397 ALA A O   1 
ATOM   3208 C  CB  . ALA A 1 397 ? -26.241 48.338 10.717  1.00 22.82  ? 397 ALA A CB  1 
ATOM   3209 N  N   . VAL A 1 398 ? -27.493 46.996 13.238  1.00 22.44  ? 398 VAL A N   1 
ATOM   3210 C  CA  . VAL A 1 398 ? -27.980 45.822 13.961  1.00 18.95  ? 398 VAL A CA  1 
ATOM   3211 C  C   . VAL A 1 398 ? -29.367 46.088 14.538  1.00 25.44  ? 398 VAL A C   1 
ATOM   3212 O  O   . VAL A 1 398 ? -30.258 45.229 14.490  1.00 22.19  ? 398 VAL A O   1 
ATOM   3213 C  CB  . VAL A 1 398 ? -26.979 45.419 15.062  1.00 29.41  ? 398 VAL A CB  1 
ATOM   3214 C  CG1 . VAL A 1 398 ? -27.621 44.415 16.044  1.00 21.47  ? 398 VAL A CG1 1 
ATOM   3215 C  CG2 . VAL A 1 398 ? -25.695 44.868 14.438  1.00 25.78  ? 398 VAL A CG2 1 
ATOM   3216 N  N   . HIS A 1 399 ? -29.569 47.274 15.107  1.00 24.90  ? 399 HIS A N   1 
ATOM   3217 C  CA  . HIS A 1 399 ? -30.893 47.619 15.615  1.00 25.09  ? 399 HIS A CA  1 
ATOM   3218 C  C   . HIS A 1 399 ? -31.980 47.295 14.593  1.00 26.37  ? 399 HIS A C   1 
ATOM   3219 O  O   . HIS A 1 399 ? -33.001 46.675 14.924  1.00 24.04  ? 399 HIS A O   1 
ATOM   3220 C  CB  . HIS A 1 399 ? -30.924 49.099 15.987  1.00 20.17  ? 399 HIS A CB  1 
ATOM   3221 C  CG  . HIS A 1 399 ? -32.235 49.557 16.534  1.00 27.18  ? 399 HIS A CG  1 
ATOM   3222 N  ND1 . HIS A 1 399 ? -32.844 48.956 17.617  1.00 32.79  ? 399 HIS A ND1 1 
ATOM   3223 C  CD2 . HIS A 1 399 ? -33.045 50.576 16.166  1.00 23.17  ? 399 HIS A CD2 1 
ATOM   3224 C  CE1 . HIS A 1 399 ? -33.973 49.582 17.888  1.00 24.85  ? 399 HIS A CE1 1 
ATOM   3225 N  NE2 . HIS A 1 399 ? -34.114 50.574 17.028  1.00 29.14  ? 399 HIS A NE2 1 
ATOM   3226 N  N   . LYS A 1 400 ? -31.760 47.692 13.333  1.00 23.78  ? 400 LYS A N   1 
ATOM   3227 C  CA  . LYS A 1 400 ? -32.772 47.584 12.284  1.00 24.51  ? 400 LYS A CA  1 
ATOM   3228 C  C   . LYS A 1 400 ? -33.087 46.151 11.875  1.00 25.15  ? 400 LYS A C   1 
ATOM   3229 O  O   . LYS A 1 400 ? -34.004 45.943 11.073  1.00 28.11  ? 400 LYS A O   1 
ATOM   3230 C  CB  . LYS A 1 400 ? -32.328 48.370 11.051  1.00 22.90  ? 400 LYS A CB  1 
ATOM   3231 C  CG  . LYS A 1 400 ? -32.390 49.867 11.253  1.00 25.29  ? 400 LYS A CG  1 
ATOM   3232 C  CD  . LYS A 1 400 ? -31.658 50.573 10.128  1.00 23.30  ? 400 LYS A CD  1 
ATOM   3233 C  CE  . LYS A 1 400 ? -32.029 52.043 10.085  1.00 30.56  ? 400 LYS A CE  1 
ATOM   3234 N  NZ  . LYS A 1 400 ? -33.442 52.223 9.669   1.00 35.54  ? 400 LYS A NZ  1 
ATOM   3235 N  N   . MET A 1 401 ? -32.354 45.163 12.378  1.00 23.43  ? 401 MET A N   1 
ATOM   3236 C  CA  . MET A 1 401 ? -32.662 43.775 12.079  1.00 24.12  ? 401 MET A CA  1 
ATOM   3237 C  C   . MET A 1 401 ? -32.850 42.948 13.351  1.00 27.92  ? 401 MET A C   1 
ATOM   3238 O  O   . MET A 1 401 ? -32.884 41.709 13.278  1.00 21.87  ? 401 MET A O   1 
ATOM   3239 C  CB  . MET A 1 401 ? -31.572 43.172 11.183  1.00 20.68  ? 401 MET A CB  1 
ATOM   3240 C  CG  . MET A 1 401 ? -30.154 43.251 11.765  1.00 24.86  ? 401 MET A CG  1 
ATOM   3241 S  SD  . MET A 1 401 ? -28.879 42.613 10.644  1.00 28.34  ? 401 MET A SD  1 
ATOM   3242 C  CE  . MET A 1 401 ? -28.803 43.860 9.368   1.00 22.99  ? 401 MET A CE  1 
ATOM   3243 N  N   . THR A 1 402 ? -33.001 43.598 14.509  1.00 23.05  ? 402 THR A N   1 
ATOM   3244 C  CA  . THR A 1 402 ? -33.147 42.890 15.778  1.00 24.37  ? 402 THR A CA  1 
ATOM   3245 C  C   . THR A 1 402 ? -34.165 43.568 16.689  1.00 23.42  ? 402 THR A C   1 
ATOM   3246 O  O   . THR A 1 402 ? -35.356 43.249 16.637  1.00 27.13  ? 402 THR A O   1 
ATOM   3247 C  CB  . THR A 1 402 ? -31.798 42.767 16.504  1.00 22.40  ? 402 THR A CB  1 
ATOM   3248 O  OG1 . THR A 1 402 ? -31.224 44.063 16.688  1.00 23.41  ? 402 THR A OG1 1 
ATOM   3249 C  CG2 . THR A 1 402 ? -30.840 41.896 15.704  1.00 21.57  ? 402 THR A CG2 1 
ATOM   3250 N  N   . GLY A 1 403 ? -33.707 44.487 17.540  1.00 24.77  ? 403 GLY A N   1 
ATOM   3251 C  CA  . GLY A 1 403 ? -34.600 45.055 18.542  1.00 24.96  ? 403 GLY A CA  1 
ATOM   3252 C  C   . GLY A 1 403 ? -35.783 45.783 17.930  1.00 27.30  ? 403 GLY A C   1 
ATOM   3253 O  O   . GLY A 1 403 ? -36.902 45.701 18.434  1.00 25.24  ? 403 GLY A O   1 
ATOM   3254 N  N   . LEU A 1 404 ? -35.544 46.531 16.849  1.00 29.90  ? 404 LEU A N   1 
ATOM   3255 C  CA  . LEU A 1 404 ? -36.632 47.233 16.172  1.00 28.97  ? 404 LEU A CA  1 
ATOM   3256 C  C   . LEU A 1 404 ? -37.670 46.243 15.672  1.00 24.48  ? 404 LEU A C   1 
ATOM   3257 O  O   . LEU A 1 404 ? -38.881 46.438 15.848  1.00 28.16  ? 404 LEU A O   1 
ATOM   3258 C  CB  . LEU A 1 404 ? -36.081 48.054 15.000  1.00 23.13  ? 404 LEU A CB  1 
ATOM   3259 C  CG  . LEU A 1 404 ? -37.094 48.855 14.164  1.00 28.17  ? 404 LEU A CG  1 
ATOM   3260 C  CD1 . LEU A 1 404 ? -37.841 49.857 15.041  1.00 25.60  ? 404 LEU A CD1 1 
ATOM   3261 C  CD2 . LEU A 1 404 ? -36.423 49.582 12.994  1.00 26.57  ? 404 LEU A CD2 1 
ATOM   3262 N  N   . SER A 1 405 ? -37.197 45.172 15.039  1.00 19.69  ? 405 SER A N   1 
ATOM   3263 C  CA  . SER A 1 405 ? -38.087 44.198 14.433  1.00 25.27  ? 405 SER A CA  1 
ATOM   3264 C  C   . SER A 1 405 ? -38.836 43.410 15.494  1.00 26.45  ? 405 SER A C   1 
ATOM   3265 O  O   . SER A 1 405 ? -40.047 43.206 15.371  1.00 29.24  ? 405 SER A O   1 
ATOM   3266 C  CB  . SER A 1 405 ? -37.285 43.272 13.518  1.00 24.82  ? 405 SER A CB  1 
ATOM   3267 O  OG  . SER A 1 405 ? -36.468 44.025 12.631  1.00 29.11  ? 405 SER A OG  1 
ATOM   3268 N  N   . ALA A 1 406 ? -38.134 42.962 16.546  1.00 24.45  ? 406 ALA A N   1 
ATOM   3269 C  CA  . ALA A 1 406 ? -38.794 42.224 17.619  1.00 23.85  ? 406 ALA A CA  1 
ATOM   3270 C  C   . ALA A 1 406 ? -39.856 43.077 18.297  1.00 28.91  ? 406 ALA A C   1 
ATOM   3271 O  O   . ALA A 1 406 ? -40.952 42.598 18.606  1.00 28.32  ? 406 ALA A O   1 
ATOM   3272 C  CB  . ALA A 1 406 ? -37.768 41.737 18.640  1.00 21.59  ? 406 ALA A CB  1 
ATOM   3273 N  N   . ALA A 1 407 ? -39.559 44.350 18.532  1.00 28.49  ? 407 ALA A N   1 
ATOM   3274 C  CA  . ALA A 1 407 ? -40.575 45.205 19.127  1.00 32.79  ? 407 ALA A CA  1 
ATOM   3275 C  C   . ALA A 1 407 ? -41.776 45.356 18.196  1.00 30.30  ? 407 ALA A C   1 
ATOM   3276 O  O   . ALA A 1 407 ? -42.924 45.167 18.617  1.00 33.43  ? 407 ALA A O   1 
ATOM   3277 C  CB  . ALA A 1 407 ? -39.971 46.558 19.488  1.00 27.79  ? 407 ALA A CB  1 
ATOM   3278 N  N   . ARG A 1 408 ? -41.535 45.664 16.912  1.00 28.27  ? 408 ARG A N   1 
ATOM   3279 C  CA  . ARG A 1 408 ? -42.652 45.948 15.999  1.00 25.67  ? 408 ARG A CA  1 
ATOM   3280 C  C   . ARG A 1 408 ? -43.561 44.740 15.798  1.00 33.40  ? 408 ARG A C   1 
ATOM   3281 O  O   . ARG A 1 408 ? -44.761 44.904 15.554  1.00 31.28  ? 408 ARG A O   1 
ATOM   3282 C  CB  . ARG A 1 408 ? -42.143 46.413 14.633  1.00 31.88  ? 408 ARG A CB  1 
ATOM   3283 C  CG  . ARG A 1 408 ? -41.536 47.810 14.609  1.00 39.94  ? 408 ARG A CG  1 
ATOM   3284 C  CD  . ARG A 1 408 ? -42.578 48.917 14.797  1.00 36.67  ? 408 ARG A CD  1 
ATOM   3285 N  NE  . ARG A 1 408 ? -41.904 50.185 15.067  1.00 42.13  ? 408 ARG A NE  1 
ATOM   3286 C  CZ  . ARG A 1 408 ? -42.467 51.388 15.004  1.00 45.78  ? 408 ARG A CZ  1 
ATOM   3287 N  NH1 . ARG A 1 408 ? -43.737 51.545 14.666  1.00 41.57  ? 408 ARG A NH1 1 
ATOM   3288 N  NH2 . ARG A 1 408 ? -41.735 52.462 15.286  1.00 41.05  ? 408 ARG A NH2 1 
ATOM   3289 N  N   . PHE A 1 409 ? -43.015 43.526 15.855  1.00 26.79  ? 409 PHE A N   1 
ATOM   3290 C  CA  . PHE A 1 409 ? -43.809 42.330 15.628  1.00 29.83  ? 409 PHE A CA  1 
ATOM   3291 C  C   . PHE A 1 409 ? -44.149 41.605 16.917  1.00 30.27  ? 409 PHE A C   1 
ATOM   3292 O  O   . PHE A 1 409 ? -44.738 40.520 16.869  1.00 26.90  ? 409 PHE A O   1 
ATOM   3293 C  CB  . PHE A 1 409 ? -43.094 41.401 14.643  1.00 24.19  ? 409 PHE A CB  1 
ATOM   3294 C  CG  . PHE A 1 409 ? -43.151 41.902 13.218  1.00 27.52  ? 409 PHE A CG  1 
ATOM   3295 C  CD1 . PHE A 1 409 ? -42.177 42.768 12.731  1.00 21.42  ? 409 PHE A CD1 1 
ATOM   3296 C  CD2 . PHE A 1 409 ? -44.205 41.546 12.382  1.00 25.12  ? 409 PHE A CD2 1 
ATOM   3297 C  CE1 . PHE A 1 409 ? -42.246 43.256 11.435  1.00 23.15  ? 409 PHE A CE1 1 
ATOM   3298 C  CE2 . PHE A 1 409 ? -44.272 42.026 11.085  1.00 27.20  ? 409 PHE A CE2 1 
ATOM   3299 C  CZ  . PHE A 1 409 ? -43.279 42.889 10.613  1.00 20.03  ? 409 PHE A CZ  1 
ATOM   3300 N  N   . GLN A 1 410 ? -43.805 42.188 18.067  1.00 33.27  ? 410 GLN A N   1 
ATOM   3301 C  CA  . GLN A 1 410 ? -44.202 41.654 19.365  1.00 26.38  ? 410 GLN A CA  1 
ATOM   3302 C  C   . GLN A 1 410 ? -43.682 40.238 19.579  1.00 25.23  ? 410 GLN A C   1 
ATOM   3303 O  O   . GLN A 1 410 ? -44.416 39.339 19.986  1.00 28.72  ? 410 GLN A O   1 
ATOM   3304 C  CB  . GLN A 1 410 ? -45.719 41.692 19.527  1.00 30.16  ? 410 GLN A CB  1 
ATOM   3305 C  CG  . GLN A 1 410 ? -46.314 43.089 19.614  1.00 33.33  ? 410 GLN A CG  1 
ATOM   3306 C  CD  . GLN A 1 410 ? -47.759 43.045 20.039  1.00 44.50  ? 410 GLN A CD  1 
ATOM   3307 O  OE1 . GLN A 1 410 ? -48.067 42.767 21.207  1.00 48.92  ? 410 GLN A OE1 1 
ATOM   3308 N  NE2 . GLN A 1 410 ? -48.661 43.287 19.093  1.00 29.47  ? 410 GLN A NE2 1 
ATOM   3309 N  N   . LEU A 1 411 ? -42.400 40.044 19.313  1.00 29.04  ? 411 LEU A N   1 
ATOM   3310 C  CA  . LEU A 1 411 ? -41.726 38.794 19.637  1.00 29.45  ? 411 LEU A CA  1 
ATOM   3311 C  C   . LEU A 1 411 ? -41.249 38.853 21.086  1.00 30.10  ? 411 LEU A C   1 
ATOM   3312 O  O   . LEU A 1 411 ? -40.446 39.721 21.444  1.00 37.96  ? 411 LEU A O   1 
ATOM   3313 C  CB  . LEU A 1 411 ? -40.550 38.557 18.687  1.00 24.93  ? 411 LEU A CB  1 
ATOM   3314 C  CG  . LEU A 1 411 ? -40.915 38.339 17.216  1.00 25.96  ? 411 LEU A CG  1 
ATOM   3315 C  CD1 . LEU A 1 411 ? -39.678 37.971 16.439  1.00 26.10  ? 411 LEU A CD1 1 
ATOM   3316 C  CD2 . LEU A 1 411 ? -41.985 37.266 17.063  1.00 20.58  ? 411 LEU A CD2 1 
ATOM   3317 N  N   . ALA A 1 412 ? -41.721 37.919 21.902  1.00 30.75  ? 412 ALA A N   1 
ATOM   3318 C  CA  . ALA A 1 412 ? -41.432 37.926 23.332  1.00 29.95  ? 412 ALA A CA  1 
ATOM   3319 C  C   . ALA A 1 412 ? -39.988 37.516 23.600  1.00 26.46  ? 412 ALA A C   1 
ATOM   3320 O  O   . ALA A 1 412 ? -39.550 36.434 23.185  1.00 25.41  ? 412 ALA A O   1 
ATOM   3321 C  CB  . ALA A 1 412 ? -42.394 36.986 24.050  1.00 31.64  ? 412 ALA A CB  1 
ATOM   3322 N  N   . ASP A 1 413 ? -39.238 38.385 24.277  1.00 27.08  ? 413 ASP A N   1 
ATOM   3323 C  CA  . ASP A 1 413 ? -37.928 38.019 24.822  1.00 25.25  ? 413 ASP A CA  1 
ATOM   3324 C  C   . ASP A 1 413 ? -36.905 37.706 23.736  1.00 27.30  ? 413 ASP A C   1 
ATOM   3325 O  O   . ASP A 1 413 ? -36.024 36.868 23.943  1.00 27.18  ? 413 ASP A O   1 
ATOM   3326 C  CB  . ASP A 1 413 ? -38.047 36.819 25.772  1.00 23.21  ? 413 ASP A CB  1 
ATOM   3327 C  CG  . ASP A 1 413 ? -38.768 37.155 27.078  1.00 32.96  ? 413 ASP A CG  1 
ATOM   3328 O  OD1 . ASP A 1 413 ? -39.092 38.346 27.315  1.00 34.91  ? 413 ASP A OD1 1 
ATOM   3329 O  OD2 . ASP A 1 413 ? -39.009 36.213 27.879  1.00 31.32  ? 413 ASP A OD2 1 
ATOM   3330 N  N   . ARG A 1 414 ? -37.002 38.366 22.579  1.00 23.48  ? 414 ARG A N   1 
ATOM   3331 C  CA  . ARG A 1 414 ? -36.072 38.164 21.480  1.00 26.99  ? 414 ARG A CA  1 
ATOM   3332 C  C   . ARG A 1 414 ? -35.627 39.507 20.916  1.00 23.83  ? 414 ARG A C   1 
ATOM   3333 O  O   . ARG A 1 414 ? -36.196 40.551 21.227  1.00 31.21  ? 414 ARG A O   1 
ATOM   3334 C  CB  . ARG A 1 414 ? -36.698 37.274 20.397  1.00 22.46  ? 414 ARG A CB  1 
ATOM   3335 C  CG  . ARG A 1 414 ? -36.994 35.893 20.976  1.00 30.46  ? 414 ARG A CG  1 
ATOM   3336 C  CD  . ARG A 1 414 ? -37.376 34.847 19.956  1.00 25.47  ? 414 ARG A CD  1 
ATOM   3337 N  NE  . ARG A 1 414 ? -37.852 33.640 20.633  1.00 25.45  ? 414 ARG A NE  1 
ATOM   3338 C  CZ  . ARG A 1 414 ? -37.118 32.561 20.890  1.00 26.59  ? 414 ARG A CZ  1 
ATOM   3339 N  NH1 . ARG A 1 414 ? -35.839 32.491 20.546  1.00 22.90  ? 414 ARG A NH1 1 
ATOM   3340 N  NH2 . ARG A 1 414 ? -37.685 31.517 21.500  1.00 20.51  ? 414 ARG A NH2 1 
ATOM   3341 N  N   . GLY A 1 415 ? -34.549 39.482 20.135  1.00 21.86  ? 415 GLY A N   1 
ATOM   3342 C  CA  . GLY A 1 415 ? -34.085 40.681 19.462  1.00 23.41  ? 415 GLY A CA  1 
ATOM   3343 C  C   . GLY A 1 415 ? -33.171 41.583 20.257  1.00 30.43  ? 415 GLY A C   1 
ATOM   3344 O  O   . GLY A 1 415 ? -32.766 42.637 19.740  1.00 23.51  ? 415 GLY A O   1 
ATOM   3345 N  N   . LEU A 1 416 ? -32.824 41.206 21.486  1.00 25.06  ? 416 LEU A N   1 
ATOM   3346 C  CA  . LEU A 1 416 ? -31.916 41.977 22.315  1.00 20.53  ? 416 LEU A CA  1 
ATOM   3347 C  C   . LEU A 1 416 ? -30.949 41.024 22.990  1.00 28.92  ? 416 LEU A C   1 
ATOM   3348 O  O   . LEU A 1 416 ? -31.356 39.961 23.461  1.00 25.41  ? 416 LEU A O   1 
ATOM   3349 C  CB  . LEU A 1 416 ? -32.653 42.774 23.391  1.00 23.87  ? 416 LEU A CB  1 
ATOM   3350 C  CG  . LEU A 1 416 ? -33.699 43.815 22.987  1.00 33.22  ? 416 LEU A CG  1 
ATOM   3351 C  CD1 . LEU A 1 416 ? -34.396 44.333 24.276  1.00 21.86  ? 416 LEU A CD1 1 
ATOM   3352 C  CD2 . LEU A 1 416 ? -33.074 44.957 22.196  1.00 21.07  ? 416 LEU A CD2 1 
ATOM   3353 N  N   . VAL A 1 417 ? -29.670 41.399 23.027  1.00 27.33  ? 417 VAL A N   1 
ATOM   3354 C  CA  . VAL A 1 417 ? -28.720 40.769 23.943  1.00 26.40  ? 417 VAL A CA  1 
ATOM   3355 C  C   . VAL A 1 417 ? -29.010 41.344 25.325  1.00 28.36  ? 417 VAL A C   1 
ATOM   3356 O  O   . VAL A 1 417 ? -28.540 42.424 25.677  1.00 29.71  ? 417 VAL A O   1 
ATOM   3357 C  CB  . VAL A 1 417 ? -27.264 41.002 23.533  1.00 28.15  ? 417 VAL A CB  1 
ATOM   3358 C  CG1 . VAL A 1 417 ? -26.332 40.298 24.524  1.00 26.61  ? 417 VAL A CG1 1 
ATOM   3359 C  CG2 . VAL A 1 417 ? -27.019 40.510 22.112  1.00 21.52  ? 417 VAL A CG2 1 
ATOM   3360 N  N   . LYS A 1 418 ? -29.797 40.623 26.110  1.00 28.57  ? 418 LYS A N   1 
ATOM   3361 C  CA  . LYS A 1 418 ? -30.286 41.153 27.369  1.00 31.11  ? 418 LYS A CA  1 
ATOM   3362 C  C   . LYS A 1 418 ? -30.468 40.004 28.352  1.00 21.93  ? 418 LYS A C   1 
ATOM   3363 O  O   . LYS A 1 418 ? -31.028 38.964 27.994  1.00 25.09  ? 418 LYS A O   1 
ATOM   3364 C  CB  . LYS A 1 418 ? -31.607 41.900 27.144  1.00 27.51  ? 418 LYS A CB  1 
ATOM   3365 C  CG  . LYS A 1 418 ? -32.218 42.391 28.423  1.00 26.91  ? 418 LYS A CG  1 
ATOM   3366 C  CD  . LYS A 1 418 ? -33.459 43.214 28.172  1.00 36.87  ? 418 LYS A CD  1 
ATOM   3367 C  CE  . LYS A 1 418 ? -33.789 44.021 29.428  1.00 41.97  ? 418 LYS A CE  1 
ATOM   3368 N  NZ  . LYS A 1 418 ? -35.137 44.610 29.342  1.00 46.92  ? 418 LYS A NZ  1 
ATOM   3369 N  N   . ILE A 1 419 ? -29.999 40.189 29.583  1.00 30.11  ? 419 ILE A N   1 
ATOM   3370 C  CA  . ILE A 1 419 ? -30.175 39.147 30.583  1.00 31.03  ? 419 ILE A CA  1 
ATOM   3371 C  C   . ILE A 1 419 ? -31.652 38.800 30.691  1.00 29.59  ? 419 ILE A C   1 
ATOM   3372 O  O   . ILE A 1 419 ? -32.501 39.682 30.870  1.00 30.87  ? 419 ILE A O   1 
ATOM   3373 C  CB  . ILE A 1 419 ? -29.612 39.603 31.932  1.00 31.69  ? 419 ILE A CB  1 
ATOM   3374 C  CG1 . ILE A 1 419 ? -28.130 39.947 31.802  1.00 29.65  ? 419 ILE A CG1 1 
ATOM   3375 C  CG2 . ILE A 1 419 ? -29.852 38.530 33.002  1.00 25.77  ? 419 ILE A CG2 1 
ATOM   3376 C  CD1 . ILE A 1 419 ? -27.595 40.701 33.028  1.00 27.24  ? 419 ILE A CD1 1 
ATOM   3377 N  N   . GLY A 1 420 ? -31.966 37.511 30.577  1.00 26.44  ? 420 GLY A N   1 
ATOM   3378 C  CA  . GLY A 1 420 ? -33.320 37.036 30.650  1.00 26.53  ? 420 GLY A CA  1 
ATOM   3379 C  C   . GLY A 1 420 ? -33.994 36.834 29.306  1.00 30.37  ? 420 GLY A C   1 
ATOM   3380 O  O   . GLY A 1 420 ? -35.039 36.177 29.258  1.00 29.49  ? 420 GLY A O   1 
ATOM   3381 N  N   . TYR A 1 421 ? -33.445 37.391 28.220  1.00 22.06  ? 421 TYR A N   1 
ATOM   3382 C  CA  . TYR A 1 421 ? -33.989 37.085 26.905  1.00 24.75  ? 421 TYR A CA  1 
ATOM   3383 C  C   . TYR A 1 421 ? -33.449 35.751 26.399  1.00 28.31  ? 421 TYR A C   1 
ATOM   3384 O  O   . TYR A 1 421 ? -32.481 35.204 26.928  1.00 27.52  ? 421 TYR A O   1 
ATOM   3385 C  CB  . TYR A 1 421 ? -33.666 38.184 25.896  1.00 26.34  ? 421 TYR A CB  1 
ATOM   3386 C  CG  . TYR A 1 421 ? -34.629 39.349 25.949  1.00 28.75  ? 421 TYR A CG  1 
ATOM   3387 C  CD1 . TYR A 1 421 ? -35.204 39.758 27.157  1.00 32.01  ? 421 TYR A CD1 1 
ATOM   3388 C  CD2 . TYR A 1 421 ? -34.969 40.034 24.795  1.00 26.78  ? 421 TYR A CD2 1 
ATOM   3389 C  CE1 . TYR A 1 421 ? -36.100 40.826 27.195  1.00 29.42  ? 421 TYR A CE1 1 
ATOM   3390 C  CE2 . TYR A 1 421 ? -35.856 41.101 24.819  1.00 29.22  ? 421 TYR A CE2 1 
ATOM   3391 C  CZ  . TYR A 1 421 ? -36.418 41.490 26.015  1.00 32.52  ? 421 TYR A CZ  1 
ATOM   3392 O  OH  . TYR A 1 421 ? -37.286 42.548 26.015  1.00 36.60  ? 421 TYR A OH  1 
ATOM   3393 N  N   . PHE A 1 422 ? -34.110 35.223 25.373  1.00 24.77  ? 422 PHE A N   1 
ATOM   3394 C  CA  . PHE A 1 422 ? -33.686 33.980 24.748  1.00 23.52  ? 422 PHE A CA  1 
ATOM   3395 C  C   . PHE A 1 422 ? -32.324 34.157 24.081  1.00 26.58  ? 422 PHE A C   1 
ATOM   3396 O  O   . PHE A 1 422 ? -32.009 35.214 23.524  1.00 27.43  ? 422 PHE A O   1 
ATOM   3397 C  CB  . PHE A 1 422 ? -34.716 33.530 23.696  1.00 24.60  ? 422 PHE A CB  1 
ATOM   3398 C  CG  . PHE A 1 422 ? -35.965 32.912 24.272  1.00 24.33  ? 422 PHE A CG  1 
ATOM   3399 C  CD1 . PHE A 1 422 ? -35.927 31.666 24.880  1.00 23.19  ? 422 PHE A CD1 1 
ATOM   3400 C  CD2 . PHE A 1 422 ? -37.184 33.565 24.171  1.00 24.24  ? 422 PHE A CD2 1 
ATOM   3401 C  CE1 . PHE A 1 422 ? -37.096 31.084 25.402  1.00 21.64  ? 422 PHE A CE1 1 
ATOM   3402 C  CE2 . PHE A 1 422 ? -38.342 33.003 24.690  1.00 20.45  ? 422 PHE A CE2 1 
ATOM   3403 C  CZ  . PHE A 1 422 ? -38.301 31.759 25.299  1.00 21.16  ? 422 PHE A CZ  1 
ATOM   3404 N  N   . ALA A 1 423 ? -31.537 33.084 24.087  1.00 21.03  ? 423 ALA A N   1 
ATOM   3405 C  CA  . ALA A 1 423 ? -30.190 33.098 23.511  1.00 26.31  ? 423 ALA A CA  1 
ATOM   3406 C  C   . ALA A 1 423 ? -30.223 32.785 22.009  1.00 24.51  ? 423 ALA A C   1 
ATOM   3407 O  O   . ALA A 1 423 ? -29.734 31.755 21.541  1.00 26.55  ? 423 ALA A O   1 
ATOM   3408 C  CB  . ALA A 1 423 ? -29.295 32.118 24.258  1.00 20.03  ? 423 ALA A CB  1 
ATOM   3409 N  N   . ASP A 1 424 ? -30.823 33.707 21.255  1.00 22.21  ? 424 ASP A N   1 
ATOM   3410 C  CA  . ASP A 1 424 ? -30.611 33.837 19.812  1.00 24.02  ? 424 ASP A CA  1 
ATOM   3411 C  C   . ASP A 1 424 ? -29.510 34.868 19.595  1.00 26.79  ? 424 ASP A C   1 
ATOM   3412 O  O   . ASP A 1 424 ? -29.695 36.041 19.921  1.00 24.81  ? 424 ASP A O   1 
ATOM   3413 C  CB  . ASP A 1 424 ? -31.878 34.298 19.080  1.00 26.26  ? 424 ASP A CB  1 
ATOM   3414 C  CG  . ASP A 1 424 ? -33.031 33.323 19.206  1.00 28.71  ? 424 ASP A CG  1 
ATOM   3415 O  OD1 . ASP A 1 424 ? -32.803 32.169 19.639  1.00 38.42  ? 424 ASP A OD1 1 
ATOM   3416 O  OD2 . ASP A 1 424 ? -34.170 33.723 18.874  1.00 28.37  ? 424 ASP A OD2 1 
ATOM   3417 N  N   . LEU A 1 425 ? -28.389 34.446 19.014  1.00 24.89  ? 425 LEU A N   1 
ATOM   3418 C  CA  . LEU A 1 425 ? -27.190 35.266 19.037  1.00 25.74  ? 425 LEU A CA  1 
ATOM   3419 C  C   . LEU A 1 425 ? -26.387 35.069 17.758  1.00 27.94  ? 425 LEU A C   1 
ATOM   3420 O  O   . LEU A 1 425 ? -26.356 33.968 17.202  1.00 27.51  ? 425 LEU A O   1 
ATOM   3421 C  CB  . LEU A 1 425 ? -26.329 34.911 20.251  1.00 19.89  ? 425 LEU A CB  1 
ATOM   3422 C  CG  . LEU A 1 425 ? -26.904 35.286 21.617  1.00 25.81  ? 425 LEU A CG  1 
ATOM   3423 C  CD1 . LEU A 1 425 ? -26.046 34.658 22.707  1.00 18.59  ? 425 LEU A CD1 1 
ATOM   3424 C  CD2 . LEU A 1 425 ? -26.962 36.800 21.784  1.00 20.37  ? 425 LEU A CD2 1 
ATOM   3425 N  N   . VAL A 1 426 ? -25.740 36.140 17.300  1.00 24.21  ? 426 VAL A N   1 
ATOM   3426 C  CA  . VAL A 1 426 ? -24.832 36.098 16.158  1.00 25.49  ? 426 VAL A CA  1 
ATOM   3427 C  C   . VAL A 1 426 ? -23.484 36.660 16.581  1.00 27.01  ? 426 VAL A C   1 
ATOM   3428 O  O   . VAL A 1 426 ? -23.408 37.765 17.131  1.00 25.16  ? 426 VAL A O   1 
ATOM   3429 C  CB  . VAL A 1 426 ? -25.367 36.890 14.955  1.00 26.50  ? 426 VAL A CB  1 
ATOM   3430 C  CG1 . VAL A 1 426 ? -24.319 36.855 13.817  1.00 26.09  ? 426 VAL A CG1 1 
ATOM   3431 C  CG2 . VAL A 1 426 ? -26.688 36.324 14.500  1.00 27.17  ? 426 VAL A CG2 1 
ATOM   3432 N  N   . LEU A 1 427 ? -22.428 35.904 16.324  1.00 20.05  ? 427 LEU A N   1 
ATOM   3433 C  CA  . LEU A 1 427 ? -21.063 36.381 16.465  1.00 21.62  ? 427 LEU A CA  1 
ATOM   3434 C  C   . LEU A 1 427 ? -20.525 36.607 15.060  1.00 27.06  ? 427 LEU A C   1 
ATOM   3435 O  O   . LEU A 1 427 ? -20.430 35.657 14.275  1.00 30.99  ? 427 LEU A O   1 
ATOM   3436 C  CB  . LEU A 1 427 ? -20.205 35.371 17.237  1.00 24.50  ? 427 LEU A CB  1 
ATOM   3437 C  CG  . LEU A 1 427 ? -18.770 35.788 17.583  1.00 34.35  ? 427 LEU A CG  1 
ATOM   3438 C  CD1 . LEU A 1 427 ? -18.745 36.797 18.730  1.00 23.66  ? 427 LEU A CD1 1 
ATOM   3439 C  CD2 . LEU A 1 427 ? -17.901 34.588 17.895  1.00 30.56  ? 427 LEU A CD2 1 
ATOM   3440 N  N   . PHE A 1 428 ? -20.200 37.855 14.731  1.00 22.90  ? 428 PHE A N   1 
ATOM   3441 C  CA  . PHE A 1 428 ? -19.683 38.140 13.400  1.00 30.39  ? 428 PHE A CA  1 
ATOM   3442 C  C   . PHE A 1 428 ? -18.489 39.077 13.490  1.00 33.48  ? 428 PHE A C   1 
ATOM   3443 O  O   . PHE A 1 428 ? -18.326 39.824 14.465  1.00 27.42  ? 428 PHE A O   1 
ATOM   3444 C  CB  . PHE A 1 428 ? -20.765 38.715 12.461  1.00 23.87  ? 428 PHE A CB  1 
ATOM   3445 C  CG  . PHE A 1 428 ? -21.282 40.092 12.840  1.00 27.56  ? 428 PHE A CG  1 
ATOM   3446 C  CD1 . PHE A 1 428 ? -22.313 40.245 13.757  1.00 26.17  ? 428 PHE A CD1 1 
ATOM   3447 C  CD2 . PHE A 1 428 ? -20.773 41.230 12.227  1.00 26.63  ? 428 PHE A CD2 1 
ATOM   3448 C  CE1 . PHE A 1 428 ? -22.809 41.525 14.081  1.00 21.73  ? 428 PHE A CE1 1 
ATOM   3449 C  CE2 . PHE A 1 428 ? -21.267 42.497 12.537  1.00 19.97  ? 428 PHE A CE2 1 
ATOM   3450 C  CZ  . PHE A 1 428 ? -22.285 42.643 13.460  1.00 20.64  ? 428 PHE A CZ  1 
ATOM   3451 N  N   . ASP A 1 429 ? -17.633 38.995 12.469  1.00 30.66  ? 429 ASP A N   1 
ATOM   3452 C  CA  . ASP A 1 429 ? -16.475 39.870 12.360  1.00 32.59  ? 429 ASP A CA  1 
ATOM   3453 C  C   . ASP A 1 429 ? -16.921 41.114 11.608  1.00 32.93  ? 429 ASP A C   1 
ATOM   3454 O  O   . ASP A 1 429 ? -17.268 41.011 10.424  1.00 32.13  ? 429 ASP A O   1 
ATOM   3455 C  CB  . ASP A 1 429 ? -15.334 39.169 11.631  1.00 33.95  ? 429 ASP A CB  1 
ATOM   3456 C  CG  . ASP A 1 429 ? -14.050 39.995 11.595  1.00 39.49  ? 429 ASP A CG  1 
ATOM   3457 O  OD1 . ASP A 1 429 ? -14.130 41.240 11.671  1.00 34.98  ? 429 ASP A OD1 1 
ATOM   3458 O  OD2 . ASP A 1 429 ? -12.957 39.393 11.481  1.00 41.83  ? 429 ASP A OD2 1 
ATOM   3459 N  N   . PRO A 1 430 ? -16.976 42.288 12.251  1.00 35.42  ? 430 PRO A N   1 
ATOM   3460 C  CA  . PRO A 1 430 ? -17.488 43.479 11.554  1.00 30.52  ? 430 PRO A CA  1 
ATOM   3461 C  C   . PRO A 1 430 ? -16.601 43.944 10.415  1.00 29.36  ? 430 PRO A C   1 
ATOM   3462 O  O   . PRO A 1 430 ? -17.106 44.546 9.461   1.00 30.45  ? 430 PRO A O   1 
ATOM   3463 C  CB  . PRO A 1 430 ? -17.564 44.531 12.665  1.00 29.71  ? 430 PRO A CB  1 
ATOM   3464 C  CG  . PRO A 1 430 ? -16.555 44.081 13.676  1.00 30.14  ? 430 PRO A CG  1 
ATOM   3465 C  CD  . PRO A 1 430 ? -16.595 42.578 13.644  1.00 29.02  ? 430 PRO A CD  1 
ATOM   3466 N  N   . GLN A 1 431 ? -15.298 43.684 10.469  1.00 32.04  ? 431 GLN A N   1 
ATOM   3467 C  CA  A GLN A 1 431 ? -14.446 44.139 9.381   0.36 33.12  ? 431 GLN A CA  1 
ATOM   3468 C  CA  B GLN A 1 431 ? -14.406 44.110 9.400   0.64 33.07  ? 431 GLN A CA  1 
ATOM   3469 C  C   . GLN A 1 431 ? -14.479 43.212 8.170   1.00 34.48  ? 431 GLN A C   1 
ATOM   3470 O  O   . GLN A 1 431 ? -14.075 43.634 7.087   1.00 35.80  ? 431 GLN A O   1 
ATOM   3471 C  CB  A GLN A 1 431 ? -13.007 44.324 9.870   0.36 34.80  ? 431 GLN A CB  1 
ATOM   3472 C  CB  B GLN A 1 431 ? -12.965 44.174 9.915   0.64 34.49  ? 431 GLN A CB  1 
ATOM   3473 C  CG  A GLN A 1 431 ? -12.240 43.052 10.133  0.36 40.28  ? 431 GLN A CG  1 
ATOM   3474 C  CG  B GLN A 1 431 ? -12.745 45.247 10.978  0.64 36.20  ? 431 GLN A CG  1 
ATOM   3475 C  CD  A GLN A 1 431 ? -10.850 43.330 10.676  0.36 47.28  ? 431 GLN A CD  1 
ATOM   3476 C  CD  B GLN A 1 431 ? -11.287 45.604 11.175  0.64 47.31  ? 431 GLN A CD  1 
ATOM   3477 O  OE1 A GLN A 1 431 ? -10.571 43.083 11.850  0.36 41.06  ? 431 GLN A OE1 1 
ATOM   3478 O  OE1 B GLN A 1 431 ? -10.399 45.002 10.569  0.64 56.03  ? 431 GLN A OE1 1 
ATOM   3479 N  NE2 A GLN A 1 431 ? -9.969  43.845 9.822   0.36 47.74  ? 431 GLN A NE2 1 
ATOM   3480 N  NE2 B GLN A 1 431 ? -11.031 46.597 12.022  0.64 55.63  ? 431 GLN A NE2 1 
ATOM   3481 N  N   . THR A 1 432 ? -14.983 41.979 8.300   1.00 33.14  ? 432 THR A N   1 
ATOM   3482 C  CA  . THR A 1 432 ? -15.041 41.079 7.155   1.00 29.97  ? 432 THR A CA  1 
ATOM   3483 C  C   . THR A 1 432 ? -16.439 40.611 6.788   1.00 31.94  ? 432 THR A C   1 
ATOM   3484 O  O   . THR A 1 432 ? -16.591 39.944 5.756   1.00 33.67  ? 432 THR A O   1 
ATOM   3485 C  CB  . THR A 1 432 ? -14.178 39.831 7.388   1.00 33.54  ? 432 THR A CB  1 
ATOM   3486 O  OG1 . THR A 1 432 ? -14.793 39.023 8.399   1.00 30.85  ? 432 THR A OG1 1 
ATOM   3487 C  CG2 . THR A 1 432 ? -12.764 40.214 7.816   1.00 29.67  ? 432 THR A CG2 1 
ATOM   3488 N  N   . VAL A 1 433 ? -17.458 40.910 7.595   1.00 25.31  ? 433 VAL A N   1 
ATOM   3489 C  CA  . VAL A 1 433 ? -18.794 40.453 7.252   1.00 27.86  ? 433 VAL A CA  1 
ATOM   3490 C  C   . VAL A 1 433 ? -19.163 40.973 5.866   1.00 29.93  ? 433 VAL A C   1 
ATOM   3491 O  O   . VAL A 1 433 ? -18.908 42.138 5.526   1.00 30.99  ? 433 VAL A O   1 
ATOM   3492 C  CB  . VAL A 1 433 ? -19.815 40.896 8.312   1.00 22.42  ? 433 VAL A CB  1 
ATOM   3493 C  CG1 . VAL A 1 433 ? -19.840 42.401 8.436   1.00 21.68  ? 433 VAL A CG1 1 
ATOM   3494 C  CG2 . VAL A 1 433 ? -21.197 40.355 7.963   1.00 20.23  ? 433 VAL A CG2 1 
ATOM   3495 N  N   . ARG A 1 434 ? -19.758 40.108 5.047   1.00 30.21  ? 434 ARG A N   1 
ATOM   3496 C  CA  . ARG A 1 434 ? -20.043 40.567 3.696   1.00 33.56  ? 434 ARG A CA  1 
ATOM   3497 C  C   . ARG A 1 434 ? -20.975 39.594 2.993   1.00 32.05  ? 434 ARG A C   1 
ATOM   3498 O  O   . ARG A 1 434 ? -20.914 38.378 3.223   1.00 29.67  ? 434 ARG A O   1 
ATOM   3499 C  CB  . ARG A 1 434 ? -18.744 40.751 2.897   1.00 32.13  ? 434 ARG A CB  1 
ATOM   3500 C  CG  . ARG A 1 434 ? -18.551 39.800 1.755   1.00 43.83  ? 434 ARG A CG  1 
ATOM   3501 C  CD  . ARG A 1 434 ? -17.305 40.166 0.944   1.00 38.50  ? 434 ARG A CD  1 
ATOM   3502 N  NE  . ARG A 1 434 ? -16.840 39.047 0.125   1.00 49.74  ? 434 ARG A NE  1 
ATOM   3503 C  CZ  . ARG A 1 434 ? -17.225 38.809 -1.124  1.00 52.94  ? 434 ARG A CZ  1 
ATOM   3504 N  NH1 . ARG A 1 434 ? -18.079 39.606 -1.752  1.00 55.43  ? 434 ARG A NH1 1 
ATOM   3505 N  NH2 . ARG A 1 434 ? -16.741 37.745 -1.759  1.00 63.85  ? 434 ARG A NH2 1 
ATOM   3506 N  N   . ASP A 1 435 ? -21.847 40.155 2.153   1.00 27.02  ? 435 ASP A N   1 
ATOM   3507 C  CA  . ASP A 1 435 ? -22.754 39.381 1.315   1.00 27.71  ? 435 ASP A CA  1 
ATOM   3508 C  C   . ASP A 1 435 ? -21.984 38.867 0.104   1.00 29.26  ? 435 ASP A C   1 
ATOM   3509 O  O   . ASP A 1 435 ? -21.552 39.654 -0.740  1.00 35.97  ? 435 ASP A O   1 
ATOM   3510 C  CB  . ASP A 1 435 ? -23.950 40.232 0.891   1.00 28.50  ? 435 ASP A CB  1 
ATOM   3511 C  CG  . ASP A 1 435 ? -23.548 41.505 0.144   1.00 33.86  ? 435 ASP A CG  1 
ATOM   3512 O  OD1 . ASP A 1 435 ? -22.662 42.251 0.620   1.00 31.66  ? 435 ASP A OD1 1 
ATOM   3513 O  OD2 . ASP A 1 435 ? -24.128 41.770 -0.932  1.00 31.16  ? 435 ASP A OD2 1 
ATOM   3514 N  N   . VAL A 1 436 ? -21.782 37.549 0.034   1.00 28.98  ? 436 VAL A N   1 
ATOM   3515 C  CA  . VAL A 1 436 ? -21.109 36.942 -1.114  1.00 33.10  ? 436 VAL A CA  1 
ATOM   3516 C  C   . VAL A 1 436 ? -22.096 36.717 -2.265  1.00 30.41  ? 436 VAL A C   1 
ATOM   3517 O  O   . VAL A 1 436 ? -21.707 36.736 -3.438  1.00 28.20  ? 436 VAL A O   1 
ATOM   3518 C  CB  . VAL A 1 436 ? -20.423 35.622 -0.694  1.00 26.23  ? 436 VAL A CB  1 
ATOM   3519 C  CG1 . VAL A 1 436 ? -19.687 35.004 -1.853  1.00 27.74  ? 436 VAL A CG1 1 
ATOM   3520 C  CG2 . VAL A 1 436 ? -19.473 35.845 0.487   1.00 29.52  ? 436 VAL A CG2 1 
ATOM   3521 N  N   . ALA A 1 437 ? -23.366 36.484 -1.952  1.00 24.90  ? 437 ALA A N   1 
ATOM   3522 C  CA  . ALA A 1 437 ? -24.384 36.303 -2.973  1.00 28.16  ? 437 ALA A CA  1 
ATOM   3523 C  C   . ALA A 1 437 ? -24.371 37.461 -3.966  1.00 33.99  ? 437 ALA A C   1 
ATOM   3524 O  O   . ALA A 1 437 ? -24.334 38.630 -3.572  1.00 29.81  ? 437 ALA A O   1 
ATOM   3525 C  CB  . ALA A 1 437 ? -25.754 36.191 -2.308  1.00 26.21  ? 437 ALA A CB  1 
ATOM   3526 N  N   . SER A 1 438 ? -24.392 37.123 -5.258  1.00 28.90  ? 438 SER A N   1 
ATOM   3527 C  CA  . SER A 1 438 ? -24.435 38.091 -6.337  1.00 28.38  ? 438 SER A CA  1 
ATOM   3528 C  C   . SER A 1 438 ? -25.561 37.723 -7.298  1.00 35.39  ? 438 SER A C   1 
ATOM   3529 O  O   . SER A 1 438 ? -26.139 36.635 -7.231  1.00 36.58  ? 438 SER A O   1 
ATOM   3530 C  CB  . SER A 1 438 ? -23.091 38.157 -7.076  1.00 30.06  ? 438 SER A CB  1 
ATOM   3531 O  OG  . SER A 1 438 ? -22.896 36.995 -7.859  1.00 38.72  ? 438 SER A OG  1 
ATOM   3532 N  N   . PHE A 1 439 ? -25.872 38.638 -8.216  1.00 32.78  ? 439 PHE A N   1 
ATOM   3533 C  CA  . PHE A 1 439 ? -26.944 38.350 -9.168  1.00 31.62  ? 439 PHE A CA  1 
ATOM   3534 C  C   . PHE A 1 439 ? -26.589 37.191 -10.094 1.00 34.38  ? 439 PHE A C   1 
ATOM   3535 O  O   . PHE A 1 439 ? -27.468 36.412 -10.473 1.00 38.02  ? 439 PHE A O   1 
ATOM   3536 C  CB  . PHE A 1 439 ? -27.294 39.610 -9.962  1.00 29.89  ? 439 PHE A CB  1 
ATOM   3537 C  CG  . PHE A 1 439 ? -28.119 40.579 -9.181  1.00 35.71  ? 439 PHE A CG  1 
ATOM   3538 C  CD1 . PHE A 1 439 ? -29.493 40.417 -9.093  1.00 29.15  ? 439 PHE A CD1 1 
ATOM   3539 C  CD2 . PHE A 1 439 ? -27.519 41.627 -8.487  1.00 38.40  ? 439 PHE A CD2 1 
ATOM   3540 C  CE1 . PHE A 1 439 ? -30.269 41.304 -8.347  1.00 33.48  ? 439 PHE A CE1 1 
ATOM   3541 C  CE2 . PHE A 1 439 ? -28.285 42.520 -7.731  1.00 36.30  ? 439 PHE A CE2 1 
ATOM   3542 C  CZ  . PHE A 1 439 ? -29.663 42.359 -7.662  1.00 31.20  ? 439 PHE A CZ  1 
ATOM   3543 N  N   . SER A 1 440 ? -25.324 37.047 -10.469 1.00 32.04  ? 440 SER A N   1 
ATOM   3544 C  CA  . SER A 1 440 ? -24.949 35.919 -11.315 1.00 45.96  ? 440 SER A CA  1 
ATOM   3545 C  C   . SER A 1 440 ? -24.703 34.647 -10.523 1.00 37.52  ? 440 SER A C   1 
ATOM   3546 O  O   . SER A 1 440 ? -24.754 33.554 -11.101 1.00 38.82  ? 440 SER A O   1 
ATOM   3547 C  CB  . SER A 1 440 ? -23.697 36.254 -12.128 1.00 38.04  ? 440 SER A CB  1 
ATOM   3548 O  OG  . SER A 1 440 ? -22.765 36.871 -11.261 1.00 50.65  ? 440 SER A OG  1 
ATOM   3549 N  N   . ASP A 1 441 ? -24.446 34.765 -9.224  1.00 37.61  ? 441 ASP A N   1 
ATOM   3550 C  CA  . ASP A 1 441 ? -24.086 33.621 -8.388  1.00 40.99  ? 441 ASP A CA  1 
ATOM   3551 C  C   . ASP A 1 441 ? -24.714 33.830 -7.021  1.00 35.20  ? 441 ASP A C   1 
ATOM   3552 O  O   . ASP A 1 441 ? -24.039 34.199 -6.050  1.00 36.00  ? 441 ASP A O   1 
ATOM   3553 C  CB  . ASP A 1 441 ? -22.568 33.485 -8.292  1.00 46.66  ? 441 ASP A CB  1 
ATOM   3554 C  CG  . ASP A 1 441 ? -22.129 32.123 -7.819  1.00 49.82  ? 441 ASP A CG  1 
ATOM   3555 O  OD1 . ASP A 1 441 ? -22.989 31.299 -7.416  1.00 43.59  ? 441 ASP A OD1 1 
ATOM   3556 O  OD2 . ASP A 1 441 ? -20.902 31.878 -7.846  1.00 52.41  ? 441 ASP A OD2 1 
ATOM   3557 N  N   . PRO A 1 442 ? -26.024 33.624 -6.909  1.00 37.35  ? 442 PRO A N   1 
ATOM   3558 C  CA  . PRO A 1 442 ? -26.750 34.109 -5.723  1.00 31.97  ? 442 PRO A CA  1 
ATOM   3559 C  C   . PRO A 1 442 ? -26.737 33.169 -4.522  1.00 27.15  ? 442 PRO A C   1 
ATOM   3560 O  O   . PRO A 1 442 ? -26.903 33.614 -3.379  1.00 34.42  ? 442 PRO A O   1 
ATOM   3561 C  CB  . PRO A 1 442 ? -28.173 34.300 -6.258  1.00 33.45  ? 442 PRO A CB  1 
ATOM   3562 C  CG  . PRO A 1 442 ? -28.297 33.230 -7.316  1.00 30.10  ? 442 PRO A CG  1 
ATOM   3563 C  CD  . PRO A 1 442 ? -26.930 33.137 -7.965  1.00 31.21  ? 442 PRO A CD  1 
ATOM   3564 N  N   . LYS A 1 443 ? -26.557 31.871 -4.745  1.00 30.92  ? 443 LYS A N   1 
ATOM   3565 C  CA  . LYS A 1 443 ? -26.716 30.887 -3.670  1.00 37.95  ? 443 LYS A CA  1 
ATOM   3566 C  C   . LYS A 1 443 ? -25.374 30.647 -2.974  1.00 34.45  ? 443 LYS A C   1 
ATOM   3567 O  O   . LYS A 1 443 ? -24.791 29.566 -3.016  1.00 41.32  ? 443 LYS A O   1 
ATOM   3568 C  CB  . LYS A 1 443 ? -27.288 29.589 -4.221  1.00 38.73  ? 443 LYS A CB  1 
ATOM   3569 C  CG  . LYS A 1 443 ? -28.585 29.742 -4.962  1.00 41.59  ? 443 LYS A CG  1 
ATOM   3570 C  CD  . LYS A 1 443 ? -29.101 28.387 -5.403  1.00 36.95  ? 443 LYS A CD  1 
ATOM   3571 C  CE  . LYS A 1 443 ? -30.346 28.542 -6.253  1.00 49.92  ? 443 LYS A CE  1 
ATOM   3572 N  NZ  . LYS A 1 443 ? -31.082 27.261 -6.398  1.00 49.46  ? 443 LYS A NZ  1 
ATOM   3573 N  N   . ARG A 1 444 ? -24.881 31.690 -2.315  1.00 36.93  ? 444 ARG A N   1 
ATOM   3574 C  CA  . ARG A 1 444 ? -23.572 31.614 -1.684  1.00 27.35  ? 444 ARG A CA  1 
ATOM   3575 C  C   . ARG A 1 444 ? -23.645 32.171 -0.266  1.00 34.48  ? 444 ARG A C   1 
ATOM   3576 O  O   . ARG A 1 444 ? -24.187 33.274 -0.049  1.00 29.68  ? 444 ARG A O   1 
ATOM   3577 C  CB  . ARG A 1 444 ? -22.522 32.352 -2.521  1.00 26.94  ? 444 ARG A CB  1 
ATOM   3578 C  CG  . ARG A 1 444 ? -22.150 31.584 -3.768  1.00 35.48  ? 444 ARG A CG  1 
ATOM   3579 C  CD  . ARG A 1 444 ? -20.976 32.205 -4.507  1.00 38.37  ? 444 ARG A CD  1 
ATOM   3580 N  NE  . ARG A 1 444 ? -21.310 33.554 -4.937  1.00 46.75  ? 444 ARG A NE  1 
ATOM   3581 C  CZ  . ARG A 1 444 ? -20.458 34.414 -5.479  1.00 46.77  ? 444 ARG A CZ  1 
ATOM   3582 N  NH1 . ARG A 1 444 ? -19.185 34.101 -5.678  1.00 40.92  ? 444 ARG A NH1 1 
ATOM   3583 N  NH2 . ARG A 1 444 ? -20.897 35.618 -5.832  1.00 41.06  ? 444 ARG A NH2 1 
ATOM   3584 N  N   . PRO A 1 445 ? -23.156 31.429 0.722   1.00 37.77  ? 445 PRO A N   1 
ATOM   3585 C  CA  . PRO A 1 445 ? -23.238 31.897 2.111   1.00 29.34  ? 445 PRO A CA  1 
ATOM   3586 C  C   . PRO A 1 445 ? -22.327 33.087 2.354   1.00 27.31  ? 445 PRO A C   1 
ATOM   3587 O  O   . PRO A 1 445 ? -21.228 33.172 1.800   1.00 28.63  ? 445 PRO A O   1 
ATOM   3588 C  CB  . PRO A 1 445 ? -22.789 30.677 2.925   1.00 32.14  ? 445 PRO A CB  1 
ATOM   3589 C  CG  . PRO A 1 445 ? -22.020 29.821 1.953   1.00 29.59  ? 445 PRO A CG  1 
ATOM   3590 C  CD  . PRO A 1 445 ? -22.637 30.052 0.616   1.00 35.46  ? 445 PRO A CD  1 
ATOM   3591 N  N   . ALA A 1 446 ? -22.799 34.006 3.197   1.00 27.90  ? 446 ALA A N   1 
ATOM   3592 C  CA  . ALA A 1 446 ? -22.024 35.188 3.542   1.00 29.64  ? 446 ALA A CA  1 
ATOM   3593 C  C   . ALA A 1 446 ? -20.698 34.813 4.198   1.00 30.05  ? 446 ALA A C   1 
ATOM   3594 O  O   . ALA A 1 446 ? -20.505 33.705 4.704   1.00 30.57  ? 446 ALA A O   1 
ATOM   3595 C  CB  . ALA A 1 446 ? -22.815 36.090 4.486   1.00 25.92  ? 446 ALA A CB  1 
ATOM   3596 N  N   . ASP A 1 447 ? -19.777 35.765 4.186   1.00 27.94  ? 447 ASP A N   1 
ATOM   3597 C  CA  . ASP A 1 447 ? -18.548 35.678 4.958   1.00 33.68  ? 447 ASP A CA  1 
ATOM   3598 C  C   . ASP A 1 447 ? -18.695 36.459 6.258   1.00 32.75  ? 447 ASP A C   1 
ATOM   3599 O  O   . ASP A 1 447 ? -19.568 37.314 6.396   1.00 30.29  ? 447 ASP A O   1 
ATOM   3600 C  CB  . ASP A 1 447 ? -17.358 36.229 4.167   1.00 29.29  ? 447 ASP A CB  1 
ATOM   3601 C  CG  . ASP A 1 447 ? -16.926 35.315 3.032   1.00 36.95  ? 447 ASP A CG  1 
ATOM   3602 O  OD1 . ASP A 1 447 ? -17.089 34.073 3.136   1.00 43.77  ? 447 ASP A OD1 1 
ATOM   3603 O  OD2 . ASP A 1 447 ? -16.414 35.853 2.032   1.00 51.72  ? 447 ASP A OD2 1 
ATOM   3604 N  N   . GLY A 1 448 ? -17.800 36.175 7.200   1.00 30.63  ? 448 GLY A N   1 
ATOM   3605 C  CA  . GLY A 1 448 ? -17.702 36.923 8.429   1.00 28.69  ? 448 GLY A CA  1 
ATOM   3606 C  C   . GLY A 1 448 ? -18.740 36.592 9.473   1.00 27.36  ? 448 GLY A C   1 
ATOM   3607 O  O   . GLY A 1 448 ? -18.760 37.243 10.516  1.00 30.50  ? 448 GLY A O   1 
ATOM   3608 N  N   . ILE A 1 449 ? -19.620 35.630 9.215   1.00 29.94  ? 449 ILE A N   1 
ATOM   3609 C  CA  . ILE A 1 449 ? -20.586 35.161 10.198  1.00 28.66  ? 449 ILE A CA  1 
ATOM   3610 C  C   . ILE A 1 449 ? -19.924 33.999 10.931  1.00 32.58  ? 449 ILE A C   1 
ATOM   3611 O  O   . ILE A 1 449 ? -19.798 32.902 10.390  1.00 32.12  ? 449 ILE A O   1 
ATOM   3612 C  CB  . ILE A 1 449 ? -21.897 34.736 9.540   1.00 33.01  ? 449 ILE A CB  1 
ATOM   3613 C  CG1 . ILE A 1 449 ? -22.464 35.875 8.679   1.00 30.51  ? 449 ILE A CG1 1 
ATOM   3614 C  CG2 . ILE A 1 449 ? -22.887 34.265 10.619  1.00 25.33  ? 449 ILE A CG2 1 
ATOM   3615 C  CD1 . ILE A 1 449 ? -23.145 37.004 9.499   1.00 26.90  ? 449 ILE A CD1 1 
ATOM   3616 N  N   . GLU A 1 450 ? -19.478 34.237 12.162  1.00 33.05  ? 450 GLU A N   1 
ATOM   3617 C  CA  . GLU A 1 450 ? -18.613 33.249 12.797  1.00 29.72  ? 450 GLU A CA  1 
ATOM   3618 C  C   . GLU A 1 450 ? -19.353 32.263 13.696  1.00 29.17  ? 450 GLU A C   1 
ATOM   3619 O  O   . GLU A 1 450 ? -18.889 31.133 13.861  1.00 34.00  ? 450 GLU A O   1 
ATOM   3620 C  CB  . GLU A 1 450 ? -17.494 33.957 13.560  1.00 36.19  ? 450 GLU A CB  1 
ATOM   3621 C  CG  . GLU A 1 450 ? -16.257 34.054 12.683  1.00 43.98  ? 450 GLU A CG  1 
ATOM   3622 C  CD  . GLU A 1 450 ? -15.290 35.109 13.118  1.00 60.09  ? 450 GLU A CD  1 
ATOM   3623 O  OE1 . GLU A 1 450 ? -14.827 35.070 14.283  1.00 74.66  ? 450 GLU A OE1 1 
ATOM   3624 O  OE2 . GLU A 1 450 ? -14.987 35.979 12.276  1.00 70.67  ? 450 GLU A OE2 1 
ATOM   3625 N  N   . ALA A 1 451 ? -20.505 32.626 14.249  1.00 23.23  ? 451 ALA A N   1 
ATOM   3626 C  CA  . ALA A 1 451 ? -21.271 31.661 15.024  1.00 24.24  ? 451 ALA A CA  1 
ATOM   3627 C  C   . ALA A 1 451 ? -22.701 32.149 15.098  1.00 26.69  ? 451 ALA A C   1 
ATOM   3628 O  O   . ALA A 1 451 ? -22.940 33.353 15.213  1.00 28.20  ? 451 ALA A O   1 
ATOM   3629 C  CB  . ALA A 1 451 ? -20.695 31.470 16.436  1.00 22.69  ? 451 ALA A CB  1 
ATOM   3630 N  N   . VAL A 1 452 ? -23.642 31.216 15.007  1.00 23.28  ? 452 VAL A N   1 
ATOM   3631 C  CA  . VAL A 1 452 ? -25.058 31.519 15.139  1.00 21.91  ? 452 VAL A CA  1 
ATOM   3632 C  C   . VAL A 1 452 ? -25.646 30.548 16.146  1.00 27.91  ? 452 VAL A C   1 
ATOM   3633 O  O   . VAL A 1 452 ? -25.439 29.333 16.038  1.00 25.40  ? 452 VAL A O   1 
ATOM   3634 C  CB  . VAL A 1 452 ? -25.830 31.436 13.803  1.00 27.57  ? 452 VAL A CB  1 
ATOM   3635 C  CG1 . VAL A 1 452 ? -27.273 31.897 14.027  1.00 19.99  ? 452 VAL A CG1 1 
ATOM   3636 C  CG2 . VAL A 1 452 ? -25.161 32.282 12.698  1.00 20.67  ? 452 VAL A CG2 1 
ATOM   3637 N  N   . MET A 1 453 ? -26.385 31.089 17.116  1.00 26.86  ? 453 MET A N   1 
ATOM   3638 C  CA  . MET A 1 453 ? -26.941 30.339 18.227  1.00 26.45  ? 453 MET A CA  1 
ATOM   3639 C  C   . MET A 1 453 ? -28.443 30.566 18.240  1.00 24.03  ? 453 MET A C   1 
ATOM   3640 O  O   . MET A 1 453 ? -28.897 31.709 18.130  1.00 21.31  ? 453 MET A O   1 
ATOM   3641 C  CB  . MET A 1 453 ? -26.305 30.789 19.548  1.00 22.40  ? 453 MET A CB  1 
ATOM   3642 C  CG  . MET A 1 453 ? -26.963 30.220 20.805  1.00 22.60  ? 453 MET A CG  1 
ATOM   3643 S  SD  . MET A 1 453 ? -25.873 30.425 22.221  1.00 26.27  ? 453 MET A SD  1 
ATOM   3644 C  CE  . MET A 1 453 ? -24.672 29.088 21.949  1.00 24.31  ? 453 MET A CE  1 
ATOM   3645 N  N   . VAL A 1 454 ? -29.206 29.481 18.371  1.00 27.43  ? 454 VAL A N   1 
ATOM   3646 C  CA  . VAL A 1 454 ? -30.665 29.522 18.347  1.00 25.67  ? 454 VAL A CA  1 
ATOM   3647 C  C   . VAL A 1 454 ? -31.162 28.835 19.601  1.00 22.03  ? 454 VAL A C   1 
ATOM   3648 O  O   . VAL A 1 454 ? -30.917 27.640 19.784  1.00 28.35  ? 454 VAL A O   1 
ATOM   3649 C  CB  . VAL A 1 454 ? -31.249 28.830 17.103  1.00 26.84  ? 454 VAL A CB  1 
ATOM   3650 C  CG1 . VAL A 1 454 ? -32.784 28.937 17.102  1.00 23.38  ? 454 VAL A CG1 1 
ATOM   3651 C  CG2 . VAL A 1 454 ? -30.654 29.421 15.836  1.00 21.19  ? 454 VAL A CG2 1 
ATOM   3652 N  N   . ASN A 1 455 ? -31.868 29.578 20.454  1.00 23.16  ? 455 ASN A N   1 
ATOM   3653 C  CA  . ASN A 1 455 ? -32.390 29.035 21.705  1.00 26.43  ? 455 ASN A CA  1 
ATOM   3654 C  C   . ASN A 1 455 ? -31.292 28.341 22.498  1.00 24.79  ? 455 ASN A C   1 
ATOM   3655 O  O   . ASN A 1 455 ? -31.494 27.261 23.061  1.00 23.52  ? 455 ASN A O   1 
ATOM   3656 C  CB  . ASN A 1 455 ? -33.556 28.086 21.442  1.00 20.54  ? 455 ASN A CB  1 
ATOM   3657 C  CG  . ASN A 1 455 ? -34.757 28.808 20.902  1.00 25.97  ? 455 ASN A CG  1 
ATOM   3658 O  OD1 . ASN A 1 455 ? -35.197 29.794 21.492  1.00 25.68  ? 455 ASN A OD1 1 
ATOM   3659 N  ND2 . ASN A 1 455 ? -35.278 28.356 19.755  1.00 19.42  ? 455 ASN A ND2 1 
ATOM   3660 N  N   . GLY A 1 456 ? -30.116 28.972 22.533  1.00 25.73  ? 456 GLY A N   1 
ATOM   3661 C  CA  . GLY A 1 456 ? -28.969 28.483 23.271  1.00 19.24  ? 456 GLY A CA  1 
ATOM   3662 C  C   . GLY A 1 456 ? -28.210 27.349 22.605  1.00 29.05  ? 456 GLY A C   1 
ATOM   3663 O  O   . GLY A 1 456 ? -27.240 26.850 23.188  1.00 25.46  ? 456 GLY A O   1 
ATOM   3664 N  N   . VAL A 1 457 ? -28.616 26.913 21.416  1.00 23.97  ? 457 VAL A N   1 
ATOM   3665 C  CA  . VAL A 1 457 ? -27.952 25.812 20.725  1.00 23.61  ? 457 VAL A CA  1 
ATOM   3666 C  C   . VAL A 1 457 ? -27.097 26.385 19.600  1.00 27.67  ? 457 VAL A C   1 
ATOM   3667 O  O   . VAL A 1 457 ? -27.600 27.083 18.708  1.00 25.58  ? 457 VAL A O   1 
ATOM   3668 C  CB  . VAL A 1 457 ? -28.960 24.784 20.192  1.00 28.01  ? 457 VAL A CB  1 
ATOM   3669 C  CG1 . VAL A 1 457 ? -28.237 23.745 19.342  1.00 26.71  ? 457 VAL A CG1 1 
ATOM   3670 C  CG2 . VAL A 1 457 ? -29.699 24.106 21.360  1.00 21.25  ? 457 VAL A CG2 1 
ATOM   3671 N  N   . MET A 1 458 ? -25.796 26.114 19.660  1.00 30.69  ? 458 MET A N   1 
ATOM   3672 C  CA  . MET A 1 458 ? -24.895 26.565 18.611  1.00 25.88  ? 458 MET A CA  1 
ATOM   3673 C  C   . MET A 1 458 ? -25.273 25.867 17.316  1.00 29.83  ? 458 MET A C   1 
ATOM   3674 O  O   . MET A 1 458 ? -25.233 24.638 17.235  1.00 27.44  ? 458 MET A O   1 
ATOM   3675 C  CB  . MET A 1 458 ? -23.440 26.273 18.992  1.00 29.48  ? 458 MET A CB  1 
ATOM   3676 C  CG  . MET A 1 458 ? -22.427 27.024 18.115  1.00 29.18  ? 458 MET A CG  1 
ATOM   3677 S  SD  . MET A 1 458 ? -22.608 28.833 18.110  1.00 35.25  ? 458 MET A SD  1 
ATOM   3678 C  CE  . MET A 1 458 ? -21.732 29.249 19.655  1.00 27.91  ? 458 MET A CE  1 
ATOM   3679 N  N   . SER A 1 459 ? -25.677 26.643 16.310  1.00 26.74  ? 459 SER A N   1 
ATOM   3680 C  CA  . SER A 1 459 ? -26.281 26.054 15.125  1.00 32.66  ? 459 SER A CA  1 
ATOM   3681 C  C   . SER A 1 459 ? -25.522 26.274 13.828  1.00 31.43  ? 459 SER A C   1 
ATOM   3682 O  O   . SER A 1 459 ? -25.798 25.563 12.861  1.00 34.56  ? 459 SER A O   1 
ATOM   3683 C  CB  . SER A 1 459 ? -27.709 26.579 14.936  1.00 23.01  ? 459 SER A CB  1 
ATOM   3684 O  OG  . SER A 1 459 ? -28.480 26.282 16.084  1.00 30.47  ? 459 SER A OG  1 
ATOM   3685 N  N   . TYR A 1 460 ? -24.586 27.215 13.773  1.00 28.14  ? 460 TYR A N   1 
ATOM   3686 C  CA  . TYR A 1 460 ? -23.907 27.537 12.526  1.00 31.81  ? 460 TYR A CA  1 
ATOM   3687 C  C   . TYR A 1 460 ? -22.587 28.204 12.860  1.00 27.63  ? 460 TYR A C   1 
ATOM   3688 O  O   . TYR A 1 460 ? -22.452 28.829 13.917  1.00 29.85  ? 460 TYR A O   1 
ATOM   3689 C  CB  . TYR A 1 460 ? -24.757 28.461 11.649  1.00 28.57  ? 460 TYR A CB  1 
ATOM   3690 C  CG  . TYR A 1 460 ? -24.146 28.763 10.283  1.00 31.25  ? 460 TYR A CG  1 
ATOM   3691 C  CD1 . TYR A 1 460 ? -24.296 27.880 9.221   1.00 28.26  ? 460 TYR A CD1 1 
ATOM   3692 C  CD2 . TYR A 1 460 ? -23.442 29.945 10.060  1.00 25.31  ? 460 TYR A CD2 1 
ATOM   3693 C  CE1 . TYR A 1 460 ? -23.756 28.160 7.968   1.00 32.48  ? 460 TYR A CE1 1 
ATOM   3694 C  CE2 . TYR A 1 460 ? -22.899 30.234 8.828   1.00 28.33  ? 460 TYR A CE2 1 
ATOM   3695 C  CZ  . TYR A 1 460 ? -23.060 29.342 7.779   1.00 34.54  ? 460 TYR A CZ  1 
ATOM   3696 O  OH  . TYR A 1 460 ? -22.511 29.637 6.555   1.00 28.29  ? 460 TYR A OH  1 
ATOM   3697 N  N   . GLY A 1 461 ? -21.626 28.083 11.946  1.00 38.43  ? 461 GLY A N   1 
ATOM   3698 C  CA  . GLY A 1 461 ? -20.276 28.542 12.220  1.00 41.34  ? 461 GLY A CA  1 
ATOM   3699 C  C   . GLY A 1 461 ? -19.474 28.810 10.963  1.00 39.86  ? 461 GLY A C   1 
ATOM   3700 O  O   . GLY A 1 461 ? -19.934 28.597 9.838   1.00 36.61  ? 461 GLY A O   1 
ATOM   3701 N  N   . SER A 1 462 ? -18.231 29.252 11.187  1.00 42.89  ? 462 SER A N   1 
ATOM   3702 C  CA  A SER A 1 462 ? -17.388 29.713 10.088  0.52 44.95  ? 462 SER A CA  1 
ATOM   3703 C  CA  B SER A 1 462 ? -17.375 29.711 10.096  0.48 44.95  ? 462 SER A CA  1 
ATOM   3704 C  C   . SER A 1 462 ? -17.123 28.627 9.053   1.00 46.14  ? 462 SER A C   1 
ATOM   3705 O  O   . SER A 1 462 ? -16.845 28.949 7.892   1.00 46.39  ? 462 SER A O   1 
ATOM   3706 C  CB  A SER A 1 462 ? -16.061 30.245 10.630  0.52 39.57  ? 462 SER A CB  1 
ATOM   3707 C  CB  B SER A 1 462 ? -16.043 30.213 10.653  0.48 39.58  ? 462 SER A CB  1 
ATOM   3708 O  OG  A SER A 1 462 ? -16.276 31.277 11.571  0.52 40.66  ? 462 SER A OG  1 
ATOM   3709 O  OG  B SER A 1 462 ? -15.301 29.145 11.222  0.48 47.97  ? 462 SER A OG  1 
ATOM   3710 N  N   . ASP A 1 463 ? -17.189 27.348 9.439   1.00 39.64  ? 463 ASP A N   1 
ATOM   3711 C  CA  . ASP A 1 463 ? -17.042 26.281 8.450   1.00 44.06  ? 463 ASP A CA  1 
ATOM   3712 C  C   . ASP A 1 463 ? -18.278 26.120 7.548   1.00 43.43  ? 463 ASP A C   1 
ATOM   3713 O  O   . ASP A 1 463 ? -18.272 25.266 6.654   1.00 47.95  ? 463 ASP A O   1 
ATOM   3714 C  CB  . ASP A 1 463 ? -16.723 24.961 9.153   1.00 36.96  ? 463 ASP A CB  1 
ATOM   3715 C  CG  . ASP A 1 463 ? -17.809 24.541 10.114  1.00 51.18  ? 463 ASP A CG  1 
ATOM   3716 O  OD1 . ASP A 1 463 ? -18.817 25.280 10.235  1.00 45.93  ? 463 ASP A OD1 1 
ATOM   3717 O  OD2 . ASP A 1 463 ? -17.655 23.475 10.751  1.00 49.75  ? 463 ASP A OD2 1 
ATOM   3718 N  N   . LYS A 1 464 ? -19.329 26.907 7.760   1.00 37.64  ? 464 LYS A N   1 
ATOM   3719 C  CA  . LYS A 1 464 ? -20.520 26.929 6.917   1.00 41.72  ? 464 LYS A CA  1 
ATOM   3720 C  C   . LYS A 1 464 ? -21.392 25.687 7.078   1.00 41.69  ? 464 LYS A C   1 
ATOM   3721 O  O   . LYS A 1 464 ? -22.267 25.445 6.247   1.00 48.38  ? 464 LYS A O   1 
ATOM   3722 C  CB  . LYS A 1 464 ? -20.162 27.113 5.437   1.00 42.36  ? 464 LYS A CB  1 
ATOM   3723 C  CG  . LYS A 1 464 ? -19.132 28.193 5.139   1.00 43.58  ? 464 LYS A CG  1 
ATOM   3724 C  CD  . LYS A 1 464 ? -19.599 29.574 5.535   1.00 45.79  ? 464 LYS A CD  1 
ATOM   3725 C  CE  . LYS A 1 464 ? -18.488 30.609 5.324   1.00 47.59  ? 464 LYS A CE  1 
ATOM   3726 N  NZ  . LYS A 1 464 ? -18.715 31.481 4.142   1.00 45.15  ? 464 LYS A NZ  1 
ATOM   3727 N  N   . LYS A 1 465 ? -21.194 24.893 8.128   1.00 36.30  ? 465 LYS A N   1 
ATOM   3728 C  CA  A LYS A 1 465 ? -22.018 23.721 8.382   0.49 37.02  ? 465 LYS A CA  1 
ATOM   3729 C  CA  B LYS A 1 465 ? -22.016 23.719 8.385   0.51 37.02  ? 465 LYS A CA  1 
ATOM   3730 C  C   . LYS A 1 465 ? -23.082 24.035 9.429   1.00 39.16  ? 465 LYS A C   1 
ATOM   3731 O  O   . LYS A 1 465 ? -22.834 24.774 10.388  1.00 31.31  ? 465 LYS A O   1 
ATOM   3732 C  CB  A LYS A 1 465 ? -21.156 22.542 8.836   0.49 35.27  ? 465 LYS A CB  1 
ATOM   3733 C  CB  B LYS A 1 465 ? -21.159 22.546 8.859   0.51 35.26  ? 465 LYS A CB  1 
ATOM   3734 C  CG  A LYS A 1 465 ? -20.194 22.060 7.766   0.49 41.33  ? 465 LYS A CG  1 
ATOM   3735 C  CG  B LYS A 1 465 ? -20.000 22.212 7.944   0.51 41.03  ? 465 LYS A CG  1 
ATOM   3736 C  CD  A LYS A 1 465 ? -19.363 20.869 8.223   0.49 36.73  ? 465 LYS A CD  1 
ATOM   3737 C  CD  B LYS A 1 465 ? -20.428 22.189 6.479   0.51 45.67  ? 465 LYS A CD  1 
ATOM   3738 C  CE  A LYS A 1 465 ? -18.455 20.371 7.092   0.49 40.97  ? 465 LYS A CE  1 
ATOM   3739 C  CE  B LYS A 1 465 ? -19.252 21.842 5.571   0.51 39.47  ? 465 LYS A CE  1 
ATOM   3740 N  NZ  A LYS A 1 465 ? -17.504 19.320 7.554   0.49 39.16  ? 465 LYS A NZ  1 
ATOM   3741 N  NZ  B LYS A 1 465 ? -19.530 22.218 4.160   0.51 39.77  ? 465 LYS A NZ  1 
ATOM   3742 N  N   . ILE A 1 466 ? -24.269 23.474 9.238   1.00 34.29  ? 466 ILE A N   1 
ATOM   3743 C  CA  . ILE A 1 466 ? -25.361 23.610 10.192  1.00 31.55  ? 466 ILE A CA  1 
ATOM   3744 C  C   . ILE A 1 466 ? -25.237 22.505 11.235  1.00 32.93  ? 466 ILE A C   1 
ATOM   3745 O  O   . ILE A 1 466 ? -25.089 21.327 10.887  1.00 30.85  ? 466 ILE A O   1 
ATOM   3746 C  CB  . ILE A 1 466 ? -26.723 23.549 9.482   1.00 29.75  ? 466 ILE A CB  1 
ATOM   3747 C  CG1 . ILE A 1 466 ? -26.887 24.766 8.573   1.00 32.08  ? 466 ILE A CG1 1 
ATOM   3748 C  CG2 . ILE A 1 466 ? -27.856 23.493 10.508  1.00 28.32  ? 466 ILE A CG2 1 
ATOM   3749 C  CD1 . ILE A 1 466 ? -28.282 24.935 7.990   1.00 28.78  ? 466 ILE A CD1 1 
ATOM   3750 N  N   . THR A 1 467 ? -25.340 22.878 12.519  1.00 31.12  ? 467 THR A N   1 
ATOM   3751 C  CA  . THR A 1 467 ? -25.142 21.948 13.628  1.00 27.11  ? 467 THR A CA  1 
ATOM   3752 C  C   . THR A 1 467 ? -26.263 21.977 14.661  1.00 32.01  ? 467 THR A C   1 
ATOM   3753 O  O   . THR A 1 467 ? -26.144 21.317 15.693  1.00 37.26  ? 467 THR A O   1 
ATOM   3754 C  CB  . THR A 1 467 ? -23.817 22.239 14.339  1.00 35.06  ? 467 THR A CB  1 
ATOM   3755 O  OG1 . THR A 1 467 ? -23.817 23.606 14.787  1.00 32.04  ? 467 THR A OG1 1 
ATOM   3756 C  CG2 . THR A 1 467 ? -22.631 22.004 13.382  1.00 32.21  ? 467 THR A CG2 1 
ATOM   3757 N  N   . GLY A 1 468 ? -27.329 22.725 14.430  1.00 30.97  ? 468 GLY A N   1 
ATOM   3758 C  CA  . GLY A 1 468 ? -28.429 22.772 15.371  1.00 25.52  ? 468 GLY A CA  1 
ATOM   3759 C  C   . GLY A 1 468 ? -29.758 22.704 14.652  1.00 29.07  ? 468 GLY A C   1 
ATOM   3760 O  O   . GLY A 1 468 ? -29.903 23.173 13.522  1.00 33.54  ? 468 GLY A O   1 
ATOM   3761 N  N   . ARG A 1 469 ? -30.735 22.095 15.326  1.00 28.45  ? 469 ARG A N   1 
ATOM   3762 C  CA  . ARG A 1 469 ? -32.122 22.047 14.862  1.00 28.06  ? 469 ARG A CA  1 
ATOM   3763 C  C   . ARG A 1 469 ? -33.049 22.499 15.994  1.00 29.64  ? 469 ARG A C   1 
ATOM   3764 O  O   . ARG A 1 469 ? -33.996 21.807 16.370  1.00 30.55  ? 469 ARG A O   1 
ATOM   3765 C  CB  . ARG A 1 469 ? -32.509 20.647 14.397  1.00 25.99  ? 469 ARG A CB  1 
ATOM   3766 C  CG  . ARG A 1 469 ? -31.525 19.996 13.459  1.00 32.60  ? 469 ARG A CG  1 
ATOM   3767 C  CD  . ARG A 1 469 ? -31.940 20.168 12.026  1.00 33.56  ? 469 ARG A CD  1 
ATOM   3768 N  NE  . ARG A 1 469 ? -33.288 19.673 11.757  1.00 36.04  ? 469 ARG A NE  1 
ATOM   3769 C  CZ  . ARG A 1 469 ? -33.579 18.478 11.257  1.00 34.98  ? 469 ARG A CZ  1 
ATOM   3770 N  NH1 . ARG A 1 469 ? -32.640 17.583 11.003  1.00 46.11  ? 469 ARG A NH1 1 
ATOM   3771 N  NH2 . ARG A 1 469 ? -34.847 18.177 11.000  1.00 39.10  ? 469 ARG A NH2 1 
ATOM   3772 N  N   . ALA A 1 470 ? -32.778 23.690 16.529  1.00 28.89  ? 470 ALA A N   1 
ATOM   3773 C  CA  . ALA A 1 470 ? -33.401 24.159 17.759  1.00 28.49  ? 470 ALA A CA  1 
ATOM   3774 C  C   . ALA A 1 470 ? -34.400 25.294 17.535  1.00 30.55  ? 470 ALA A C   1 
ATOM   3775 O  O   . ALA A 1 470 ? -34.791 25.959 18.501  1.00 27.34  ? 470 ALA A O   1 
ATOM   3776 C  CB  . ALA A 1 470 ? -32.313 24.584 18.754  1.00 22.71  ? 470 ALA A CB  1 
ATOM   3777 N  N   . GLY A 1 471 ? -34.821 25.538 16.291  1.00 27.68  ? 471 GLY A N   1 
ATOM   3778 C  CA  . GLY A 1 471 ? -35.825 26.559 16.045  1.00 27.90  ? 471 GLY A CA  1 
ATOM   3779 C  C   . GLY A 1 471 ? -37.173 26.177 16.630  1.00 25.84  ? 471 GLY A C   1 
ATOM   3780 O  O   . GLY A 1 471 ? -37.489 24.998 16.817  1.00 28.83  ? 471 GLY A O   1 
ATOM   3781 N  N   . ARG A 1 472 ? -37.973 27.193 16.951  1.00 21.85  ? 472 ARG A N   1 
ATOM   3782 C  CA  . ARG A 1 472 ? -39.315 26.979 17.478  1.00 22.90  ? 472 ARG A CA  1 
ATOM   3783 C  C   . ARG A 1 472 ? -40.321 27.801 16.688  1.00 24.77  ? 472 ARG A C   1 
ATOM   3784 O  O   . ARG A 1 472 ? -39.979 28.805 16.049  1.00 22.98  ? 472 ARG A O   1 
ATOM   3785 C  CB  . ARG A 1 472 ? -39.419 27.351 18.959  1.00 23.62  ? 472 ARG A CB  1 
ATOM   3786 C  CG  . ARG A 1 472 ? -38.311 26.768 19.808  1.00 24.85  ? 472 ARG A CG  1 
ATOM   3787 C  CD  . ARG A 1 472 ? -38.335 27.385 21.186  1.00 23.38  ? 472 ARG A CD  1 
ATOM   3788 N  NE  . ARG A 1 472 ? -37.359 26.754 22.071  1.00 25.77  ? 472 ARG A NE  1 
ATOM   3789 C  CZ  . ARG A 1 472 ? -37.049 27.206 23.279  1.00 31.43  ? 472 ARG A CZ  1 
ATOM   3790 N  NH1 . ARG A 1 472 ? -37.620 28.292 23.777  1.00 27.55  ? 472 ARG A NH1 1 
ATOM   3791 N  NH2 . ARG A 1 472 ? -36.151 26.549 24.010  1.00 32.24  ? 472 ARG A NH2 1 
ATOM   3792 N  N   . PHE A 1 473 ? -41.578 27.364 16.730  1.00 23.03  ? 473 PHE A N   1 
ATOM   3793 C  CA  . PHE A 1 473 ? -42.643 28.254 16.302  1.00 23.52  ? 473 PHE A CA  1 
ATOM   3794 C  C   . PHE A 1 473 ? -42.881 29.306 17.372  1.00 28.63  ? 473 PHE A C   1 
ATOM   3795 O  O   . PHE A 1 473 ? -43.118 28.971 18.536  1.00 20.94  ? 473 PHE A O   1 
ATOM   3796 C  CB  . PHE A 1 473 ? -43.930 27.492 16.032  1.00 19.81  ? 473 PHE A CB  1 
ATOM   3797 C  CG  . PHE A 1 473 ? -45.037 28.378 15.554  1.00 26.81  ? 473 PHE A CG  1 
ATOM   3798 C  CD1 . PHE A 1 473 ? -45.019 28.892 14.262  1.00 23.52  ? 473 PHE A CD1 1 
ATOM   3799 C  CD2 . PHE A 1 473 ? -46.067 28.740 16.400  1.00 23.51  ? 473 PHE A CD2 1 
ATOM   3800 C  CE1 . PHE A 1 473 ? -46.033 29.729 13.817  1.00 22.75  ? 473 PHE A CE1 1 
ATOM   3801 C  CE2 . PHE A 1 473 ? -47.085 29.566 15.960  1.00 23.10  ? 473 PHE A CE2 1 
ATOM   3802 C  CZ  . PHE A 1 473 ? -47.065 30.066 14.667  1.00 21.99  ? 473 PHE A CZ  1 
ATOM   3803 N  N   . LEU A 1 474 ? -42.813 30.577 16.985  1.00 22.26  ? 474 LEU A N   1 
ATOM   3804 C  CA  . LEU A 1 474 ? -42.997 31.688 17.912  1.00 24.67  ? 474 LEU A CA  1 
ATOM   3805 C  C   . LEU A 1 474 ? -44.436 32.192 17.866  1.00 26.64  ? 474 LEU A C   1 
ATOM   3806 O  O   . LEU A 1 474 ? -44.981 32.459 16.791  1.00 28.66  ? 474 LEU A O   1 
ATOM   3807 C  CB  . LEU A 1 474 ? -42.033 32.832 17.599  1.00 21.10  ? 474 LEU A CB  1 
ATOM   3808 C  CG  . LEU A 1 474 ? -40.556 32.461 17.532  1.00 22.19  ? 474 LEU A CG  1 
ATOM   3809 C  CD1 . LEU A 1 474 ? -39.719 33.726 17.347  1.00 18.17  ? 474 LEU A CD1 1 
ATOM   3810 C  CD2 . LEU A 1 474 ? -40.113 31.722 18.782  1.00 22.86  ? 474 LEU A CD2 1 
ATOM   3811 N  N   . ARG A 1 475 ? -45.045 32.315 19.031  1.00 25.73  ? 475 ARG A N   1 
ATOM   3812 C  CA  . ARG A 1 475 ? -46.349 32.935 19.160  1.00 24.81  ? 475 ARG A CA  1 
ATOM   3813 C  C   . ARG A 1 475 ? -46.177 34.387 19.580  1.00 27.01  ? 475 ARG A C   1 
ATOM   3814 O  O   . ARG A 1 475 ? -45.196 34.747 20.235  1.00 25.63  ? 475 ARG A O   1 
ATOM   3815 C  CB  . ARG A 1 475 ? -47.206 32.167 20.160  1.00 21.80  ? 475 ARG A CB  1 
ATOM   3816 C  CG  . ARG A 1 475 ? -47.639 30.830 19.581  1.00 31.41  ? 475 ARG A CG  1 
ATOM   3817 C  CD  . ARG A 1 475 ? -48.276 29.878 20.594  1.00 34.10  ? 475 ARG A CD  1 
ATOM   3818 N  NE  . ARG A 1 475 ? -47.913 28.496 20.284  1.00 48.34  ? 475 ARG A NE  1 
ATOM   3819 C  CZ  . ARG A 1 475 ? -48.639 27.647 19.563  1.00 56.53  ? 475 ARG A CZ  1 
ATOM   3820 N  NH1 . ARG A 1 475 ? -49.837 27.977 19.089  1.00 46.79  ? 475 ARG A NH1 1 
ATOM   3821 N  NH2 . ARG A 1 475 ? -48.154 26.432 19.315  1.00 52.22  ? 475 ARG A NH2 1 
ATOM   3822 N  N   . ARG A 1 476 ? -47.117 35.226 19.148  1.00 24.59  ? 476 ARG A N   1 
ATOM   3823 C  CA  . ARG A 1 476 ? -47.132 36.621 19.571  1.00 27.07  ? 476 ARG A CA  1 
ATOM   3824 C  C   . ARG A 1 476 ? -47.096 36.727 21.093  1.00 27.09  ? 476 ARG A C   1 
ATOM   3825 O  O   . ARG A 1 476 ? -47.730 35.940 21.801  1.00 32.29  ? 476 ARG A O   1 
ATOM   3826 C  CB  . ARG A 1 476 ? -48.388 37.310 19.044  1.00 22.65  ? 476 ARG A CB  1 
ATOM   3827 C  CG  . ARG A 1 476 ? -48.404 38.807 19.227  1.00 26.25  ? 476 ARG A CG  1 
ATOM   3828 C  CD  . ARG A 1 476 ? -49.726 39.415 18.748  1.00 25.62  ? 476 ARG A CD  1 
ATOM   3829 N  NE  . ARG A 1 476 ? -50.860 39.115 19.620  1.00 28.02  ? 476 ARG A NE  1 
ATOM   3830 C  CZ  . ARG A 1 476 ? -51.790 38.194 19.384  1.00 31.93  ? 476 ARG A CZ  1 
ATOM   3831 N  NH1 . ARG A 1 476 ? -51.731 37.397 18.325  1.00 26.18  ? 476 ARG A NH1 1 
ATOM   3832 N  NH2 . ARG A 1 476 ? -52.815 38.075 20.229  1.00 28.52  ? 476 ARG A NH2 1 
ATOM   3833 N  N   . ARG A 1 477 ? -46.353 37.705 21.599  1.00 29.42  ? 477 ARG A N   1 
ATOM   3834 C  CA  A ARG A 1 477 ? -46.397 37.971 23.027  0.45 35.97  ? 477 ARG A CA  1 
ATOM   3835 C  CA  B ARG A 1 477 ? -46.390 38.003 23.024  0.55 35.92  ? 477 ARG A CA  1 
ATOM   3836 C  C   . ARG A 1 477 ? -47.805 38.391 23.422  1.00 34.15  ? 477 ARG A C   1 
ATOM   3837 O  O   . ARG A 1 477 ? -48.362 39.336 22.867  1.00 49.95  ? 477 ARG A O   1 
ATOM   3838 C  CB  A ARG A 1 477 ? -45.376 39.042 23.400  0.45 38.17  ? 477 ARG A CB  1 
ATOM   3839 C  CB  B ARG A 1 477 ? -45.407 39.129 23.350  0.55 38.12  ? 477 ARG A CB  1 
ATOM   3840 C  CG  A ARG A 1 477 ? -45.709 40.421 22.882  0.45 40.63  ? 477 ARG A CG  1 
ATOM   3841 C  CG  B ARG A 1 477 ? -45.273 39.432 24.844  0.55 49.91  ? 477 ARG A CG  1 
ATOM   3842 C  CD  A ARG A 1 477 ? -44.806 41.465 23.510  0.45 49.91  ? 477 ARG A CD  1 
ATOM   3843 C  CD  B ARG A 1 477 ? -44.544 40.745 25.102  0.55 50.19  ? 477 ARG A CD  1 
ATOM   3844 N  NE  A ARG A 1 477 ? -45.173 42.818 23.105  0.45 55.18  ? 477 ARG A NE  1 
ATOM   3845 N  NE  B ARG A 1 477 ? -45.298 41.885 24.593  0.55 58.77  ? 477 ARG A NE  1 
ATOM   3846 C  CZ  A ARG A 1 477 ? -46.195 43.501 23.605  0.45 56.13  ? 477 ARG A CZ  1 
ATOM   3847 C  CZ  B ARG A 1 477 ? -44.917 42.651 23.578  0.55 55.64  ? 477 ARG A CZ  1 
ATOM   3848 N  NH1 A ARG A 1 477 ? -46.995 42.978 24.523  0.45 53.65  ? 477 ARG A NH1 1 
ATOM   3849 N  NH1 B ARG A 1 477 ? -43.757 42.463 22.966  0.55 54.21  ? 477 ARG A NH1 1 
ATOM   3850 N  NH2 A ARG A 1 477 ? -46.426 44.738 23.168  0.45 52.24  ? 477 ARG A NH2 1 
ATOM   3851 N  NH2 B ARG A 1 477 ? -45.719 43.633 23.168  0.55 56.93  ? 477 ARG A NH2 1 
ATOM   3852 N  N   . MET A 1 478 ? -48.392 37.665 24.373  1.00 49.15  ? 478 MET A N   1 
ATOM   3853 C  CA  . MET A 1 478 ? -49.761 37.947 24.788  1.00 67.38  ? 478 MET A CA  1 
ATOM   3854 C  C   . MET A 1 478 ? -49.746 38.933 25.946  1.00 72.66  ? 478 MET A C   1 
ATOM   3855 O  O   . MET A 1 478 ? -49.108 38.677 26.972  1.00 85.78  ? 478 MET A O   1 
ATOM   3856 C  CB  . MET A 1 478 ? -50.503 36.668 25.180  1.00 65.46  ? 478 MET A CB  1 
ATOM   3857 C  CG  . MET A 1 478 ? -50.497 35.588 24.093  1.00 68.56  ? 478 MET A CG  1 
ATOM   3858 S  SD  . MET A 1 478 ? -51.741 35.743 22.785  1.00 68.95  ? 478 MET A SD  1 
ATOM   3859 C  CE  . MET A 1 478 ? -50.948 34.809 21.467  1.00 26.72  ? 478 MET A CE  1 
ATOM   3860 N  N   . ASP A 1 479 ? -50.444 40.058 25.762  1.00 81.94  ? 479 ASP A N   1 
ATOM   3861 C  CA  . ASP A 1 479 ? -50.520 41.163 26.723  1.00 91.31  ? 479 ASP A CA  1 
ATOM   3862 C  C   . ASP A 1 479 ? -49.365 41.205 27.732  1.00 94.54  ? 479 ASP A C   1 
ATOM   3863 O  O   . ASP A 1 479 ? -49.170 42.203 28.435  1.00 79.77  ? 479 ASP A O   1 
ATOM   3864 C  CB  . ASP A 1 479 ? -51.851 41.109 27.476  1.00 72.18  ? 479 ASP A CB  1 
ATOM   3865 C  CG  . ASP A 1 479 ? -52.210 42.441 28.109  1.00 94.01  ? 479 ASP A CG  1 
ATOM   3866 O  OD1 . ASP A 1 479 ? -52.356 43.428 27.354  1.00 96.05  ? 479 ASP A OD1 1 
ATOM   3867 O  OD2 . ASP A 1 479 ? -52.342 42.508 29.353  1.00 96.01  ? 479 ASP A OD2 1 
HETATM 3868 S  S   . SO4 B 2 .   ? -59.747 37.190 23.368  1.00 66.07  ? 501 SO4 A S   1 
HETATM 3869 O  O1  . SO4 B 2 .   ? -58.747 36.930 22.378  1.00 71.90  ? 501 SO4 A O1  1 
HETATM 3870 O  O2  . SO4 B 2 .   ? -61.049 37.076 22.779  1.00 62.26  ? 501 SO4 A O2  1 
HETATM 3871 O  O3  . SO4 B 2 .   ? -59.618 36.240 24.430  1.00 59.61  ? 501 SO4 A O3  1 
HETATM 3872 O  O4  . SO4 B 2 .   ? -59.576 38.516 23.882  1.00 63.87  ? 501 SO4 A O4  1 
HETATM 3873 S  S   . SO4 C 2 .   ? -34.750 46.997 -35.188 1.00 112.16 ? 502 SO4 A S   1 
HETATM 3874 O  O1  . SO4 C 2 .   ? -33.308 46.574 -35.175 1.00 100.33 ? 502 SO4 A O1  1 
HETATM 3875 O  O2  . SO4 C 2 .   ? -34.965 47.992 -36.291 1.00 104.23 ? 502 SO4 A O2  1 
HETATM 3876 O  O3  . SO4 C 2 .   ? -35.614 45.798 -35.454 1.00 89.09  ? 502 SO4 A O3  1 
HETATM 3877 O  O4  . SO4 C 2 .   ? -35.116 47.608 -33.863 1.00 89.44  ? 502 SO4 A O4  1 
HETATM 3878 C  C1  . PEG D 3 .   ? -33.953 36.362 -34.645 1.00 61.64  ? 503 PEG A C1  1 
HETATM 3879 O  O1  . PEG D 3 .   ? -33.381 36.883 -35.824 1.00 60.93  ? 503 PEG A O1  1 
HETATM 3880 C  C2  . PEG D 3 .   ? -33.109 35.227 -34.114 1.00 58.73  ? 503 PEG A C2  1 
HETATM 3881 O  O2  . PEG D 3 .   ? -33.688 34.719 -32.928 1.00 58.42  ? 503 PEG A O2  1 
HETATM 3882 C  C3  . PEG D 3 .   ? -33.156 33.473 -32.540 1.00 47.62  ? 503 PEG A C3  1 
HETATM 3883 C  C4  . PEG D 3 .   ? -34.104 32.841 -31.562 1.00 49.79  ? 503 PEG A C4  1 
HETATM 3884 O  O4  . PEG D 3 .   ? -35.432 32.934 -32.040 1.00 62.68  ? 503 PEG A O4  1 
HETATM 3885 C  C1  . EDO E 4 .   ? -55.486 21.871 -0.123  1.00 56.25  ? 504 EDO A C1  1 
HETATM 3886 O  O1  . EDO E 4 .   ? -55.931 22.871 0.773   1.00 55.19  ? 504 EDO A O1  1 
HETATM 3887 C  C2  . EDO E 4 .   ? -55.258 20.573 0.614   1.00 48.04  ? 504 EDO A C2  1 
HETATM 3888 O  O2  . EDO E 4 .   ? -54.750 19.606 -0.277  1.00 59.35  ? 504 EDO A O2  1 
HETATM 3889 C  C1  . GOL F 5 .   ? -43.179 45.611 -7.744  1.00 52.27  ? 505 GOL A C1  1 
HETATM 3890 O  O1  . GOL F 5 .   ? -43.992 46.308 -6.819  1.00 36.54  ? 505 GOL A O1  1 
HETATM 3891 C  C2  . GOL F 5 .   ? -41.711 45.780 -7.392  1.00 49.68  ? 505 GOL A C2  1 
HETATM 3892 O  O2  . GOL F 5 .   ? -41.471 45.092 -6.189  1.00 50.84  ? 505 GOL A O2  1 
HETATM 3893 C  C3  . GOL F 5 .   ? -40.806 45.217 -8.476  1.00 49.94  ? 505 GOL A C3  1 
HETATM 3894 O  O3  . GOL F 5 .   ? -40.807 46.117 -9.557  1.00 39.10  ? 505 GOL A O3  1 
HETATM 3895 C  C1  . EDO G 4 .   ? -43.552 54.766 15.407  1.00 40.32  ? 506 EDO A C1  1 
HETATM 3896 O  O1  . EDO G 4 .   ? -44.431 55.642 14.743  1.00 39.41  ? 506 EDO A O1  1 
HETATM 3897 C  C2  . EDO G 4 .   ? -42.912 55.437 16.607  1.00 60.29  ? 506 EDO A C2  1 
HETATM 3898 O  O2  . EDO G 4 .   ? -42.070 56.510 16.220  1.00 50.92  ? 506 EDO A O2  1 
HETATM 3899 C  C1  . PGE H 6 .   ? -24.933 39.913 -15.051 1.00 46.21  ? 507 PGE A C1  1 
HETATM 3900 O  O1  . PGE H 6 .   ? -23.824 39.118 -15.450 1.00 47.72  ? 507 PGE A O1  1 
HETATM 3901 C  C2  . PGE H 6 .   ? -25.793 39.205 -14.021 1.00 42.04  ? 507 PGE A C2  1 
HETATM 3902 O  O2  . PGE H 6 .   ? -26.527 38.170 -14.628 1.00 43.41  ? 507 PGE A O2  1 
HETATM 3903 C  C3  . PGE H 6 .   ? -27.307 37.369 -13.783 1.00 34.87  ? 507 PGE A C3  1 
HETATM 3904 C  C4  . PGE H 6 .   ? -27.696 36.025 -14.362 1.00 36.78  ? 507 PGE A C4  1 
HETATM 3905 O  O4  . PGE H 6 .   ? -24.916 33.697 -16.008 1.00 52.63  ? 507 PGE A O4  1 
HETATM 3906 C  C6  . PGE H 6 .   ? -26.234 33.217 -15.839 1.00 49.91  ? 507 PGE A C6  1 
HETATM 3907 C  C5  . PGE H 6 .   ? -26.851 33.837 -14.593 1.00 41.22  ? 507 PGE A C5  1 
HETATM 3908 O  O3  . PGE H 6 .   ? -26.566 35.221 -14.593 1.00 53.54  ? 507 PGE A O3  1 
HETATM 3909 C  C1  . GOL I 5 .   ? -39.074 47.287 -28.715 1.00 41.66  ? 508 GOL A C1  1 
HETATM 3910 O  O1  . GOL I 5 .   ? -40.450 47.068 -28.830 1.00 49.36  ? 508 GOL A O1  1 
HETATM 3911 C  C2  . GOL I 5 .   ? -38.802 48.765 -28.690 1.00 44.46  ? 508 GOL A C2  1 
HETATM 3912 O  O2  . GOL I 5 .   ? -39.534 49.316 -27.617 1.00 59.87  ? 508 GOL A O2  1 
HETATM 3913 C  C3  . GOL I 5 .   ? -37.302 48.999 -28.524 1.00 58.55  ? 508 GOL A C3  1 
HETATM 3914 O  O3  . GOL I 5 .   ? -36.628 48.416 -29.629 1.00 42.92  ? 508 GOL A O3  1 
HETATM 3915 C  C1  . PEG J 3 .   ? -34.178 26.453 30.157  1.00 46.68  ? 509 PEG A C1  1 
HETATM 3916 O  O1  . PEG J 3 .   ? -33.707 25.761 29.015  1.00 43.49  ? 509 PEG A O1  1 
HETATM 3917 C  C2  . PEG J 3 .   ? -35.540 25.938 30.575  1.00 52.91  ? 509 PEG A C2  1 
HETATM 3918 O  O2  . PEG J 3 .   ? -35.498 24.663 31.178  1.00 58.99  ? 509 PEG A O2  1 
HETATM 3919 C  C3  . PEG J 3 .   ? -34.986 23.656 30.336  1.00 61.05  ? 509 PEG A C3  1 
HETATM 3920 C  C4  . PEG J 3 .   ? -35.283 22.290 30.916  1.00 72.16  ? 509 PEG A C4  1 
HETATM 3921 O  O4  . PEG J 3 .   ? -34.421 21.993 31.997  1.00 48.50  ? 509 PEG A O4  1 
HETATM 3922 C  C1  . GOL K 5 .   ? -13.143 30.990 33.629  1.00 56.23  ? 510 GOL A C1  1 
HETATM 3923 O  O1  . GOL K 5 .   ? -12.991 32.155 34.406  1.00 49.68  ? 510 GOL A O1  1 
HETATM 3924 C  C2  . GOL K 5 .   ? -12.791 31.277 32.183  1.00 60.65  ? 510 GOL A C2  1 
HETATM 3925 O  O2  . GOL K 5 .   ? -11.417 31.616 32.102  1.00 52.32  ? 510 GOL A O2  1 
HETATM 3926 C  C3  . GOL K 5 .   ? -13.141 30.085 31.301  1.00 55.07  ? 510 GOL A C3  1 
HETATM 3927 O  O3  . GOL K 5 .   ? -14.394 29.571 31.707  1.00 54.01  ? 510 GOL A O3  1 
HETATM 3928 C  C1  . PEG L 3 .   ? -41.184 33.080 -31.956 1.00 54.69  ? 511 PEG A C1  1 
HETATM 3929 O  O1  . PEG L 3 .   ? -40.425 32.085 -32.607 1.00 63.12  ? 511 PEG A O1  1 
HETATM 3930 C  C2  . PEG L 3 .   ? -41.372 34.248 -32.890 1.00 58.62  ? 511 PEG A C2  1 
HETATM 3931 O  O2  . PEG L 3 .   ? -41.597 35.441 -32.174 1.00 62.11  ? 511 PEG A O2  1 
HETATM 3932 C  C3  . PEG L 3 .   ? -41.321 36.570 -32.975 1.00 67.68  ? 511 PEG A C3  1 
HETATM 3933 C  C4  . PEG L 3 .   ? -41.022 37.778 -32.118 1.00 67.39  ? 511 PEG A C4  1 
HETATM 3934 O  O4  . PEG L 3 .   ? -42.210 38.244 -31.511 1.00 51.09  ? 511 PEG A O4  1 
HETATM 3935 S  S   . SO4 M 2 .   ? -65.907 35.185 20.325  1.00 53.63  ? 512 SO4 A S   1 
HETATM 3936 O  O1  . SO4 M 2 .   ? -64.751 35.233 19.371  1.00 45.39  ? 512 SO4 A O1  1 
HETATM 3937 O  O2  . SO4 M 2 .   ? -67.165 35.570 19.604  1.00 63.54  ? 512 SO4 A O2  1 
HETATM 3938 O  O3  . SO4 M 2 .   ? -66.049 33.789 20.850  1.00 51.93  ? 512 SO4 A O3  1 
HETATM 3939 O  O4  . SO4 M 2 .   ? -65.660 36.161 21.434  1.00 44.95  ? 512 SO4 A O4  1 
HETATM 3940 S  S   . SO4 N 2 .   ? -39.378 42.139 -6.513  1.00 31.21  ? 513 SO4 A S   1 
HETATM 3941 O  O1  . SO4 N 2 .   ? -37.979 41.779 -6.924  1.00 31.83  ? 513 SO4 A O1  1 
HETATM 3942 O  O2  . SO4 N 2 .   ? -40.273 42.367 -7.707  1.00 35.86  ? 513 SO4 A O2  1 
HETATM 3943 O  O3  . SO4 N 2 .   ? -39.886 41.007 -5.686  1.00 41.82  ? 513 SO4 A O3  1 
HETATM 3944 O  O4  . SO4 N 2 .   ? -39.392 43.402 -5.717  1.00 29.97  ? 513 SO4 A O4  1 
HETATM 3945 S  S   . SO4 O 2 .   ? -43.576 39.767 -3.286  1.00 16.73  ? 514 SO4 A S   1 
HETATM 3946 O  O1  . SO4 O 2 .   ? -42.772 39.452 -4.529  1.00 45.48  ? 514 SO4 A O1  1 
HETATM 3947 O  O2  . SO4 O 2 .   ? -44.589 38.687 -3.051  1.00 30.16  ? 514 SO4 A O2  1 
HETATM 3948 O  O3  . SO4 O 2 .   ? -42.616 39.933 -2.156  1.00 31.34  ? 514 SO4 A O3  1 
HETATM 3949 O  O4  . SO4 O 2 .   ? -44.352 41.023 -3.483  1.00 30.60  ? 514 SO4 A O4  1 
HETATM 3950 S  S   . SO4 P 2 .   ? -59.741 59.781 8.909   1.00 89.39  ? 515 SO4 A S   1 
HETATM 3951 O  O1  . SO4 P 2 .   ? -59.631 58.742 7.832   1.00 70.26  ? 515 SO4 A O1  1 
HETATM 3952 O  O2  . SO4 P 2 .   ? -61.189 60.101 9.135   1.00 82.35  ? 515 SO4 A O2  1 
HETATM 3953 O  O3  . SO4 P 2 .   ? -59.125 59.280 10.183  1.00 51.93  ? 515 SO4 A O3  1 
HETATM 3954 O  O4  . SO4 P 2 .   ? -59.015 61.018 8.473   1.00 88.22  ? 515 SO4 A O4  1 
HETATM 3955 C  C1  . EDO Q 4 .   ? -47.664 43.846 -9.050  1.00 61.82  ? 516 EDO A C1  1 
HETATM 3956 O  O1  . EDO Q 4 .   ? -46.973 43.196 -8.001  1.00 52.29  ? 516 EDO A O1  1 
HETATM 3957 C  C2  . EDO Q 4 .   ? -48.804 42.985 -9.541  1.00 53.73  ? 516 EDO A C2  1 
HETATM 3958 O  O2  . EDO Q 4 .   ? -48.348 41.668 -9.752  1.00 66.45  ? 516 EDO A O2  1 
HETATM 3959 C  C1  . GOL R 5 .   ? -53.933 39.201 23.276  1.00 54.02  ? 517 GOL A C1  1 
HETATM 3960 O  O1  . GOL R 5 .   ? -53.945 39.282 24.682  1.00 77.75  ? 517 GOL A O1  1 
HETATM 3961 C  C2  . GOL R 5 .   ? -53.002 40.265 22.713  1.00 58.80  ? 517 GOL A C2  1 
HETATM 3962 O  O2  . GOL R 5 .   ? -53.274 41.508 23.334  1.00 75.87  ? 517 GOL A O2  1 
HETATM 3963 C  C3  . GOL R 5 .   ? -51.539 39.858 22.879  1.00 58.53  ? 517 GOL A C3  1 
HETATM 3964 O  O3  . GOL R 5 .   ? -50.695 40.872 22.357  1.00 58.10  ? 517 GOL A O3  1 
HETATM 3965 C  C1  . PEG S 3 .   ? -18.972 26.959 15.520  1.00 57.78  ? 518 PEG A C1  1 
HETATM 3966 O  O1  . PEG S 3 .   ? -17.740 26.973 14.825  1.00 65.56  ? 518 PEG A O1  1 
HETATM 3967 C  C2  . PEG S 3 .   ? -18.927 27.833 16.757  1.00 67.03  ? 518 PEG A C2  1 
HETATM 3968 O  O2  . PEG S 3 .   ? -17.629 28.309 17.043  1.00 74.79  ? 518 PEG A O2  1 
HETATM 3969 C  C3  . PEG S 3 .   ? -17.339 29.441 16.264  1.00 69.38  ? 518 PEG A C3  1 
HETATM 3970 C  C4  . PEG S 3 .   ? -16.120 30.172 16.766  1.00 74.92  ? 518 PEG A C4  1 
HETATM 3971 O  O4  . PEG S 3 .   ? -15.665 31.075 15.774  1.00 77.48  ? 518 PEG A O4  1 
HETATM 3972 H  H11 . PEG S 3 .   ? -19.203 26.057 15.792  1.00 69.34  ? 518 PEG A H11 1 
HETATM 3973 H  H12 . PEG S 3 .   ? -19.692 27.272 14.951  1.00 69.34  ? 518 PEG A H12 1 
HETATM 3974 H  HO1 . PEG S 3 .   ? -17.786 26.402 14.197  1.00 78.67  ? 518 PEG A HO1 1 
HETATM 3975 H  H21 . PEG S 3 .   ? -19.276 27.314 17.499  1.00 80.44  ? 518 PEG A H21 1 
HETATM 3976 H  H22 . PEG S 3 .   ? -19.542 28.571 16.620  1.00 80.44  ? 518 PEG A H22 1 
HETATM 3977 H  H31 . PEG S 3 .   ? -18.095 30.049 16.266  1.00 83.26  ? 518 PEG A H31 1 
HETATM 3978 H  H32 . PEG S 3 .   ? -17.195 29.181 15.341  1.00 83.26  ? 518 PEG A H32 1 
HETATM 3979 H  H41 . PEG S 3 .   ? -15.453 29.506 16.995  1.00 89.90  ? 518 PEG A H41 1 
HETATM 3980 H  H42 . PEG S 3 .   ? -16.364 30.619 17.591  1.00 89.90  ? 518 PEG A H42 1 
HETATM 3981 H  HO4 . PEG S 3 .   ? -15.000 31.500 16.089  1.00 92.98  ? 518 PEG A HO4 1 
HETATM 3982 C  C1  . EDO T 4 .   ? -18.107 47.557 16.132  1.00 48.46  ? 519 EDO A C1  1 
HETATM 3983 O  O1  . EDO T 4 .   ? -16.738 47.439 16.469  1.00 63.63  ? 519 EDO A O1  1 
HETATM 3984 C  C2  . EDO T 4 .   ? -18.416 48.891 15.484  1.00 54.29  ? 519 EDO A C2  1 
HETATM 3985 O  O2  . EDO T 4 .   ? -17.644 49.103 14.316  1.00 57.90  ? 519 EDO A O2  1 
HETATM 3986 H  H11 . EDO T 4 .   ? -18.665 47.468 16.920  1.00 58.16  ? 519 EDO A H11 1 
HETATM 3987 H  H12 . EDO T 4 .   ? -18.374 46.854 15.520  1.00 58.16  ? 519 EDO A H12 1 
HETATM 3988 H  HO1 . EDO T 4 .   ? -16.636 46.721 16.912  1.00 76.36  ? 519 EDO A HO1 1 
HETATM 3989 H  H21 . EDO T 4 .   ? -18.256 49.575 16.152  1.00 65.15  ? 519 EDO A H21 1 
HETATM 3990 H  H22 . EDO T 4 .   ? -19.367 48.901 15.295  1.00 65.15  ? 519 EDO A H22 1 
HETATM 3991 H  HO2 . EDO T 4 .   ? -17.799 48.464 13.777  1.00 69.48  ? 519 EDO A HO2 1 
HETATM 3992 C  C1  . EDO U 4 .   ? -32.055 27.751 -14.648 1.00 62.93  ? 520 EDO A C1  1 
HETATM 3993 O  O1  . EDO U 4 .   ? -31.248 28.407 -13.694 1.00 59.83  ? 520 EDO A O1  1 
HETATM 3994 C  C2  . EDO U 4 .   ? -33.458 27.661 -14.107 1.00 43.12  ? 520 EDO A C2  1 
HETATM 3995 O  O2  . EDO U 4 .   ? -34.407 27.392 -15.122 1.00 60.16  ? 520 EDO A O2  1 
HETATM 3996 H  H11 . EDO U 4 .   ? -31.729 26.857 -14.837 1.00 75.51  ? 520 EDO A H11 1 
HETATM 3997 H  H12 . EDO U 4 .   ? -32.069 28.227 -15.492 1.00 75.51  ? 520 EDO A H12 1 
HETATM 3998 H  HO1 . EDO U 4 .   ? -31.342 28.008 -12.949 1.00 71.79  ? 520 EDO A HO1 1 
HETATM 3999 H  H21 . EDO U 4 .   ? -33.642 28.500 -13.655 1.00 51.75  ? 520 EDO A H21 1 
HETATM 4000 H  H22 . EDO U 4 .   ? -33.455 26.972 -13.424 1.00 51.75  ? 520 EDO A H22 1 
HETATM 4001 H  HO2 . EDO U 4 .   ? -34.435 28.064 -15.642 1.00 72.19  ? 520 EDO A HO2 1 
HETATM 4002 C  C1  . PGE V 6 .   ? -41.537 18.258 -0.835  1.00 70.65  ? 521 PGE A C1  1 
HETATM 4003 O  O1  . PGE V 6 .   ? -42.452 17.641 -1.725  1.00 81.66  ? 521 PGE A O1  1 
HETATM 4004 C  C2  . PGE V 6 .   ? -42.238 19.392 -0.132  1.00 75.03  ? 521 PGE A C2  1 
HETATM 4005 O  O2  . PGE V 6 .   ? -42.471 19.014 1.207   1.00 83.60  ? 521 PGE A O2  1 
HETATM 4006 C  C3  . PGE V 6 .   ? -43.480 19.756 1.844   1.00 72.20  ? 521 PGE A C3  1 
HETATM 4007 C  C4  . PGE V 6 .   ? -43.871 19.167 3.174   1.00 72.32  ? 521 PGE A C4  1 
HETATM 4008 O  O4  . PGE V 6 .   ? -47.960 17.853 1.189   1.00 63.16  ? 521 PGE A O4  1 
HETATM 4009 C  C6  . PGE V 6 .   ? -46.667 17.466 1.596   1.00 81.52  ? 521 PGE A C6  1 
HETATM 4010 C  C5  . PGE V 6 .   ? -46.022 18.645 2.305   1.00 71.90  ? 521 PGE A C5  1 
HETATM 4011 O  O3  . PGE V 6 .   ? -44.860 18.183 2.969   1.00 94.57  ? 521 PGE A O3  1 
HETATM 4012 H  H1  . PGE V 6 .   ? -40.762 18.621 -1.291  1.00 84.78  ? 521 PGE A H1  1 
HETATM 4013 H  H12 . PGE V 6 .   ? -41.204 17.646 -0.160  1.00 84.78  ? 521 PGE A H12 1 
HETATM 4014 H  HO1 . PGE V 6 .   ? -42.747 18.234 -2.257  1.00 97.99  ? 521 PGE A HO1 1 
HETATM 4015 H  H2  . PGE V 6 .   ? -43.068 19.589 -0.594  1.00 90.04  ? 521 PGE A H2  1 
HETATM 4016 H  H22 . PGE V 6 .   ? -41.688 20.189 -0.185  1.00 90.04  ? 521 PGE A H22 1 
HETATM 4017 H  H3  . PGE V 6 .   ? -44.268 19.799 1.279   1.00 86.64  ? 521 PGE A H3  1 
HETATM 4018 H  H32 . PGE V 6 .   ? -43.184 20.669 1.983   1.00 86.64  ? 521 PGE A H32 1 
HETATM 4019 H  H4  . PGE V 6 .   ? -44.189 19.879 3.750   1.00 86.78  ? 521 PGE A H4  1 
HETATM 4020 H  H42 . PGE V 6 .   ? -43.081 18.797 3.597   1.00 86.78  ? 521 PGE A H42 1 
HETATM 4021 H  HO4 . PGE V 6 .   ? -48.302 17.214 0.745   1.00 75.79  ? 521 PGE A HO4 1 
HETATM 4022 H  H6  . PGE V 6 .   ? -46.115 17.210 0.840   1.00 97.83  ? 521 PGE A H6  1 
HETATM 4023 H  H62 . PGE V 6 .   ? -46.693 16.708 2.200   1.00 97.83  ? 521 PGE A H62 1 
HETATM 4024 H  H5  . PGE V 6 .   ? -46.650 19.033 2.934   1.00 86.28  ? 521 PGE A H5  1 
HETATM 4025 H  H52 . PGE V 6 .   ? -45.802 19.335 1.660   1.00 86.28  ? 521 PGE A H52 1 
HETATM 4026 NI NI  . NI  W 7 .   ? -43.108 39.597 -0.018  1.00 39.54  ? 522 NI  A NI  1 
HETATM 4027 NI NI  . NI  X 7 .   ? -44.899 42.013 -1.754  1.00 34.47  ? 523 NI  A NI  1 
HETATM 4028 O  O   . HOH Y 8 .   ? -15.578 38.104 1.726   1.00 58.66  ? 601 HOH A O   1 
HETATM 4029 O  O   . HOH Y 8 .   ? -42.735 40.623 -13.327 1.00 45.67  ? 602 HOH A O   1 
HETATM 4030 O  O   . HOH Y 8 .   ? -43.064 43.482 5.554   1.00 30.32  ? 603 HOH A O   1 
HETATM 4031 O  O   . HOH Y 8 .   ? -24.030 39.650 -28.631 1.00 43.54  ? 604 HOH A O   1 
HETATM 4032 O  O   . HOH Y 8 .   ? -38.566 43.131 -34.484 1.00 35.90  ? 605 HOH A O   1 
HETATM 4033 O  O   . HOH Y 8 .   ? -31.180 46.074 -34.332 1.00 59.05  ? 606 HOH A O   1 
HETATM 4034 O  O   . HOH Y 8 .   ? -33.143 20.405 33.162  1.00 38.06  ? 607 HOH A O   1 
HETATM 4035 O  O   . HOH Y 8 .   ? -9.244  31.229 32.999  1.00 54.83  ? 608 HOH A O   1 
HETATM 4036 O  O   . HOH Y 8 .   ? -67.384 45.953 2.934   1.00 39.70  ? 609 HOH A O   1 
HETATM 4037 O  O   . HOH Y 8 .   ? -31.135 61.522 3.960   1.00 52.77  ? 610 HOH A O   1 
HETATM 4038 O  O   . HOH Y 8 .   ? -14.984 43.493 19.206  1.00 39.32  ? 611 HOH A O   1 
HETATM 4039 O  O   . HOH Y 8 .   ? -59.655 38.317 20.607  1.00 34.99  ? 612 HOH A O   1 
HETATM 4040 O  O   . HOH Y 8 .   ? -64.721 38.264 22.217  1.00 58.00  ? 613 HOH A O   1 
HETATM 4041 O  O   . HOH Y 8 .   ? -46.321 45.582 -6.801  1.00 35.68  ? 615 HOH A O   1 
HETATM 4042 O  O   . HOH Y 8 .   ? -27.508 53.565 16.878  1.00 33.45  ? 616 HOH A O   1 
HETATM 4043 O  O   . HOH Y 8 .   ? -35.178 37.797 -37.263 1.00 47.49  ? 617 HOH A O   1 
HETATM 4044 O  O   . HOH Y 8 .   ? -28.345 24.256 30.708  1.00 48.28  ? 618 HOH A O   1 
HETATM 4045 O  O   . HOH Y 8 .   ? -73.146 42.183 10.309  1.00 45.83  ? 619 HOH A O   1 
HETATM 4046 O  O   . HOH Y 8 .   ? -34.437 35.230 16.758  1.00 26.75  ? 620 HOH A O   1 
HETATM 4047 O  O   . HOH Y 8 .   ? -58.552 26.840 6.247   1.00 35.95  ? 621 HOH A O   1 
HETATM 4048 O  O   . HOH Y 8 .   ? -29.436 26.708 -14.010 1.00 59.57  ? 622 HOH A O   1 
HETATM 4049 O  O   . HOH Y 8 .   ? -68.566 33.266 -1.576  1.00 47.63  ? 623 HOH A O   1 
HETATM 4050 O  O   . HOH Y 8 .   ? -46.284 41.992 4.131   1.00 32.05  ? 624 HOH A O   1 
HETATM 4051 O  O   . HOH Y 8 .   ? -12.319 36.412 18.149  1.00 34.09  ? 625 HOH A O   1 
HETATM 4052 O  O   . HOH Y 8 .   ? -32.874 36.775 -9.837  1.00 36.93  ? 626 HOH A O   1 
HETATM 4053 O  O   . HOH Y 8 .   ? -58.435 28.387 10.369  1.00 32.40  ? 627 HOH A O   1 
HETATM 4054 O  O   . HOH Y 8 .   ? -67.443 38.065 19.181  1.00 42.43  ? 628 HOH A O   1 
HETATM 4055 O  O   . HOH Y 8 .   ? -53.182 45.718 26.609  1.00 72.35  ? 629 HOH A O   1 
HETATM 4056 O  O   . HOH Y 8 .   ? -45.940 54.518 -12.821 1.00 39.65  ? 630 HOH A O   1 
HETATM 4057 O  O   . HOH Y 8 .   ? -25.887 40.173 -1.872  1.00 27.82  ? 631 HOH A O   1 
HETATM 4058 O  O   . HOH Y 8 .   ? -50.858 52.876 12.575  1.00 28.05  ? 632 HOH A O   1 
HETATM 4059 O  O   . HOH Y 8 .   ? -27.271 37.498 35.676  1.00 28.02  ? 633 HOH A O   1 
HETATM 4060 O  O   . HOH Y 8 .   ? -63.962 44.272 -0.820  1.00 34.29  ? 634 HOH A O   1 
HETATM 4061 O  O   . HOH Y 8 .   ? -35.634 14.182 10.338  1.00 55.61  ? 635 HOH A O   1 
HETATM 4062 O  O   . HOH Y 8 .   ? -50.939 30.057 -8.808  1.00 42.55  ? 636 HOH A O   1 
HETATM 4063 O  O   . HOH Y 8 .   ? -58.859 39.570 17.102  1.00 24.63  ? 637 HOH A O   1 
HETATM 4064 O  O   . HOH Y 8 .   ? -10.051 37.782 24.671  1.00 35.09  ? 638 HOH A O   1 
HETATM 4065 O  O   . HOH Y 8 .   ? -25.428 30.488 -7.221  1.00 35.73  ? 639 HOH A O   1 
HETATM 4066 O  O   . HOH Y 8 .   ? -33.812 58.768 4.985   1.00 36.09  ? 640 HOH A O   1 
HETATM 4067 O  O   . HOH Y 8 .   ? -50.745 45.540 17.983  1.00 35.77  ? 641 HOH A O   1 
HETATM 4068 O  O   . HOH Y 8 .   ? -38.021 34.474 2.204   1.00 25.82  ? 642 HOH A O   1 
HETATM 4069 O  O   . HOH Y 8 .   ? -26.636 48.610 20.448  1.00 26.55  ? 643 HOH A O   1 
HETATM 4070 O  O   . HOH Y 8 .   ? -5.234  37.596 19.141  1.00 54.74  ? 644 HOH A O   1 
HETATM 4071 O  O   . HOH Y 8 .   ? -41.763 45.396 -31.710 1.00 58.89  ? 645 HOH A O   1 
HETATM 4072 O  O   . HOH Y 8 .   ? -38.142 27.481 27.133  1.00 52.99  ? 646 HOH A O   1 
HETATM 4073 O  O   . HOH Y 8 .   ? -48.327 59.023 -5.489  1.00 32.97  ? 647 HOH A O   1 
HETATM 4074 O  O   . HOH Y 8 .   ? -52.293 25.532 4.298   1.00 26.06  ? 648 HOH A O   1 
HETATM 4075 O  O   . HOH Y 8 .   ? -37.026 38.540 -6.884  1.00 31.16  ? 649 HOH A O   1 
HETATM 4076 O  O   . HOH Y 8 .   ? -22.154 32.369 6.236   1.00 24.24  ? 650 HOH A O   1 
HETATM 4077 O  O   . HOH Y 8 .   ? -49.751 50.935 -10.106 1.00 41.60  ? 651 HOH A O   1 
HETATM 4078 O  O   . HOH Y 8 .   ? -42.690 24.796 -1.817  1.00 64.45  ? 652 HOH A O   1 
HETATM 4079 O  O   . HOH Y 8 .   ? -35.218 42.971 10.561  1.00 20.73  ? 653 HOH A O   1 
HETATM 4080 O  O   . HOH Y 8 .   ? -45.526 34.565 2.524   1.00 23.57  ? 654 HOH A O   1 
HETATM 4081 O  O   . HOH Y 8 .   ? -56.777 32.397 -10.176 1.00 53.64  ? 655 HOH A O   1 
HETATM 4082 O  O   . HOH Y 8 .   ? -40.837 43.581 -3.507  1.00 29.38  ? 656 HOH A O   1 
HETATM 4083 O  O   . HOH Y 8 .   ? -36.521 22.514 16.770  1.00 31.65  ? 657 HOH A O   1 
HETATM 4084 O  O   . HOH Y 8 .   ? -59.274 41.176 -6.406  1.00 24.59  ? 658 HOH A O   1 
HETATM 4085 O  O   . HOH Y 8 .   ? -18.819 46.996 -0.182  1.00 30.75  ? 659 HOH A O   1 
HETATM 4086 O  O   . HOH Y 8 .   ? -43.240 50.688 -1.596  1.00 32.94  ? 660 HOH A O   1 
HETATM 4087 O  O   . HOH Y 8 .   ? -52.328 48.872 2.576   1.00 25.74  ? 661 HOH A O   1 
HETATM 4088 O  O   . HOH Y 8 .   ? -57.822 55.938 1.271   1.00 52.15  ? 662 HOH A O   1 
HETATM 4089 O  O   . HOH Y 8 .   ? -30.990 25.486 15.640  1.00 25.52  ? 663 HOH A O   1 
HETATM 4090 O  O   . HOH Y 8 .   ? -60.474 27.561 -0.714  1.00 45.50  ? 664 HOH A O   1 
HETATM 4091 O  O   . HOH Y 8 .   ? -11.183 44.394 24.653  1.00 30.00  ? 665 HOH A O   1 
HETATM 4092 O  O   . HOH Y 8 .   ? -36.340 53.843 -6.512  1.00 25.26  ? 666 HOH A O   1 
HETATM 4093 O  O   . HOH Y 8 .   ? -30.867 30.258 -19.107 1.00 41.68  ? 667 HOH A O   1 
HETATM 4094 O  O   . HOH Y 8 .   ? -51.869 39.191 -2.336  1.00 32.00  ? 668 HOH A O   1 
HETATM 4095 O  O   . HOH Y 8 .   ? -33.717 47.729 -21.259 1.00 30.19  ? 669 HOH A O   1 
HETATM 4096 O  O   . HOH Y 8 .   ? -27.344 45.644 26.992  1.00 36.68  ? 670 HOH A O   1 
HETATM 4097 O  O   . HOH Y 8 .   ? -73.621 48.000 4.656   1.00 51.18  ? 671 HOH A O   1 
HETATM 4098 O  O   . HOH Y 8 .   ? -40.318 34.304 21.486  1.00 26.91  ? 672 HOH A O   1 
HETATM 4099 O  O   . HOH Y 8 .   ? -67.475 36.324 -11.031 1.00 36.72  ? 673 HOH A O   1 
HETATM 4100 O  O   . HOH Y 8 .   ? -32.001 37.425 20.112  1.00 26.40  ? 674 HOH A O   1 
HETATM 4101 O  O   . HOH Y 8 .   ? -39.962 52.519 -15.778 1.00 32.24  ? 675 HOH A O   1 
HETATM 4102 O  O   . HOH Y 8 .   ? -47.960 30.856 7.194   1.00 23.08  ? 676 HOH A O   1 
HETATM 4103 O  O   . HOH Y 8 .   ? -32.340 45.941 -31.263 1.00 43.48  ? 677 HOH A O   1 
HETATM 4104 O  O   . HOH Y 8 .   ? -61.797 31.120 -4.377  1.00 50.32  ? 678 HOH A O   1 
HETATM 4105 O  O   . HOH Y 8 .   ? -41.611 47.815 -31.154 1.00 65.66  ? 679 HOH A O   1 
HETATM 4106 O  O   . HOH Y 8 .   ? -41.669 34.767 -19.067 1.00 34.53  ? 680 HOH A O   1 
HETATM 4107 O  O   . HOH Y 8 .   ? -43.429 43.096 -4.963  1.00 45.65  ? 681 HOH A O   1 
HETATM 4108 O  O   . HOH Y 8 .   ? -28.758 49.393 -28.480 1.00 40.11  ? 682 HOH A O   1 
HETATM 4109 O  O   . HOH Y 8 .   ? -55.050 52.425 -2.681  1.00 46.00  ? 683 HOH A O   1 
HETATM 4110 O  O   . HOH Y 8 .   ? -47.375 41.049 16.524  1.00 22.88  ? 684 HOH A O   1 
HETATM 4111 O  O   . HOH Y 8 .   ? -33.408 37.858 17.749  1.00 26.96  ? 685 HOH A O   1 
HETATM 4112 O  O   . HOH Y 8 .   ? -24.116 35.799 0.944   1.00 23.45  ? 686 HOH A O   1 
HETATM 4113 O  O   . HOH Y 8 .   ? -55.571 49.258 19.508  1.00 32.67  ? 687 HOH A O   1 
HETATM 4114 O  O   . HOH Y 8 .   ? -24.208 36.352 -15.351 1.00 42.06  ? 688 HOH A O   1 
HETATM 4115 O  O   . HOH Y 8 .   ? -38.335 43.782 2.592   1.00 26.67  ? 689 HOH A O   1 
HETATM 4116 O  O   . HOH Y 8 .   ? -25.491 33.866 3.625   1.00 28.62  ? 690 HOH A O   1 
HETATM 4117 O  O   . HOH Y 8 .   ? -48.571 62.054 -8.833  1.00 62.29  ? 691 HOH A O   1 
HETATM 4118 O  O   . HOH Y 8 .   ? -29.351 30.657 -15.937 1.00 47.11  ? 692 HOH A O   1 
HETATM 4119 O  O   . HOH Y 8 .   ? -20.765 24.859 12.171  1.00 34.41  ? 693 HOH A O   1 
HETATM 4120 O  O   . HOH Y 8 .   ? -42.527 28.957 1.407   1.00 30.44  ? 694 HOH A O   1 
HETATM 4121 O  O   . HOH Y 8 .   ? -42.885 23.374 -4.078  1.00 56.34  ? 695 HOH A O   1 
HETATM 4122 O  O   . HOH Y 8 .   ? -29.500 22.592 4.207   1.00 40.92  ? 696 HOH A O   1 
HETATM 4123 O  O   . HOH Y 8 .   ? -57.904 30.484 12.042  1.00 33.15  ? 697 HOH A O   1 
HETATM 4124 O  O   . HOH Y 8 .   ? -27.935 56.227 13.529  1.00 36.32  ? 698 HOH A O   1 
HETATM 4125 O  O   . HOH Y 8 .   ? -12.405 42.833 13.882  1.00 46.28  ? 699 HOH A O   1 
HETATM 4126 O  O   . HOH Y 8 .   ? -55.848 54.855 20.995  1.00 48.95  ? 700 HOH A O   1 
HETATM 4127 O  O   . HOH Y 8 .   ? -24.797 47.298 22.931  1.00 25.43  ? 701 HOH A O   1 
HETATM 4128 O  O   . HOH Y 8 .   ? -37.491 26.104 -8.591  1.00 53.66  ? 702 HOH A O   1 
HETATM 4129 O  O   . HOH Y 8 .   ? -25.268 43.528 33.786  1.00 56.01  ? 703 HOH A O   1 
HETATM 4130 O  O   . HOH Y 8 .   ? -27.227 26.472 25.996  1.00 29.40  ? 704 HOH A O   1 
HETATM 4131 O  O   . HOH Y 8 .   ? -41.217 43.828 -11.442 1.00 51.14  ? 705 HOH A O   1 
HETATM 4132 O  O   . HOH Y 8 .   ? -53.981 40.823 0.258   1.00 25.37  ? 706 HOH A O   1 
HETATM 4133 O  O   . HOH Y 8 .   ? -49.663 19.747 12.155  1.00 36.70  ? 707 HOH A O   1 
HETATM 4134 O  O   . HOH Y 8 .   ? -29.949 36.510 -9.270  1.00 30.68  ? 708 HOH A O   1 
HETATM 4135 O  O   . HOH Y 8 .   ? -45.669 49.871 13.010  1.00 32.13  ? 709 HOH A O   1 
HETATM 4136 O  O   . HOH Y 8 .   ? -24.823 24.164 21.363  1.00 35.37  ? 710 HOH A O   1 
HETATM 4137 O  O   . HOH Y 8 .   ? -36.134 35.926 -6.287  1.00 30.64  ? 711 HOH A O   1 
HETATM 4138 O  O   . HOH Y 8 .   ? -35.394 48.173 -2.003  1.00 33.15  ? 712 HOH A O   1 
HETATM 4139 O  O   . HOH Y 8 .   ? -36.397 29.551 29.410  1.00 26.56  ? 713 HOH A O   1 
HETATM 4140 O  O   . HOH Y 8 .   ? -40.525 39.062 -7.554  1.00 39.27  ? 714 HOH A O   1 
HETATM 4141 O  O   . HOH Y 8 .   ? -21.282 43.427 2.739   1.00 31.30  ? 715 HOH A O   1 
HETATM 4142 O  O   . HOH Y 8 .   ? -55.468 37.263 20.203  1.00 26.40  ? 716 HOH A O   1 
HETATM 4143 O  O   . HOH Y 8 .   ? -32.880 37.757 22.735  1.00 25.39  ? 717 HOH A O   1 
HETATM 4144 O  O   . HOH Y 8 .   ? -56.790 29.765 0.799   1.00 31.13  ? 718 HOH A O   1 
HETATM 4145 O  O   . HOH Y 8 .   ? -26.349 48.781 -20.331 1.00 32.47  ? 719 HOH A O   1 
HETATM 4146 O  O   . HOH Y 8 .   ? -32.711 42.020 32.354  1.00 43.53  ? 720 HOH A O   1 
HETATM 4147 O  O   . HOH Y 8 .   ? -10.319 40.501 10.853  1.00 46.45  ? 721 HOH A O   1 
HETATM 4148 O  O   . HOH Y 8 .   ? -19.541 32.972 7.622   1.00 34.26  ? 722 HOH A O   1 
HETATM 4149 O  O   . HOH Y 8 .   ? -45.466 47.938 -0.247  1.00 26.00  ? 723 HOH A O   1 
HETATM 4150 O  O   . HOH Y 8 .   ? -67.460 38.465 14.759  1.00 28.43  ? 724 HOH A O   1 
HETATM 4151 O  O   . HOH Y 8 .   ? -43.693 41.708 7.820   1.00 21.74  ? 725 HOH A O   1 
HETATM 4152 O  O   . HOH Y 8 .   ? -39.185 20.837 17.571  1.00 38.90  ? 726 HOH A O   1 
HETATM 4153 O  O   . HOH Y 8 .   ? -36.990 31.591 -29.277 1.00 40.65  ? 727 HOH A O   1 
HETATM 4154 O  O   . HOH Y 8 .   ? -32.868 24.879 23.533  1.00 41.02  ? 728 HOH A O   1 
HETATM 4155 O  O   . HOH Y 8 .   ? -43.425 54.940 -6.672  1.00 32.48  ? 729 HOH A O   1 
HETATM 4156 O  O   . HOH Y 8 .   ? -34.144 50.486 -27.368 1.00 41.51  ? 730 HOH A O   1 
HETATM 4157 O  O   . HOH Y 8 .   ? -53.099 47.092 18.386  1.00 32.08  ? 731 HOH A O   1 
HETATM 4158 O  O   . HOH Y 8 .   ? -46.701 33.511 14.856  1.00 18.08  ? 732 HOH A O   1 
HETATM 4159 O  O   . HOH Y 8 .   ? -40.180 47.877 -16.038 1.00 43.83  ? 733 HOH A O   1 
HETATM 4160 O  O   . HOH Y 8 .   ? -19.581 45.739 10.001  1.00 28.39  ? 734 HOH A O   1 
HETATM 4161 O  O   . HOH Y 8 .   ? -38.256 63.919 2.739   1.00 44.25  ? 735 HOH A O   1 
HETATM 4162 O  O   . HOH Y 8 .   ? -25.338 42.099 -28.527 1.00 38.72  ? 736 HOH A O   1 
HETATM 4163 O  O   . HOH Y 8 .   ? -53.499 58.639 5.870   1.00 34.62  ? 737 HOH A O   1 
HETATM 4164 O  O   . HOH Y 8 .   ? -40.319 31.387 -3.887  1.00 36.21  ? 738 HOH A O   1 
HETATM 4165 O  O   . HOH Y 8 .   ? -40.769 34.036 27.682  1.00 30.41  ? 739 HOH A O   1 
HETATM 4166 O  O   . HOH Y 8 .   ? -59.246 54.284 0.346   1.00 43.88  ? 740 HOH A O   1 
HETATM 4167 O  O   . HOH Y 8 .   ? -56.158 36.201 23.190  1.00 48.63  ? 741 HOH A O   1 
HETATM 4168 O  O   . HOH Y 8 .   ? -45.967 19.271 7.230   1.00 37.21  ? 742 HOH A O   1 
HETATM 4169 O  O   . HOH Y 8 .   ? -57.800 37.229 18.333  1.00 27.45  ? 743 HOH A O   1 
HETATM 4170 O  O   . HOH Y 8 .   ? -46.413 21.423 3.034   1.00 40.57  ? 744 HOH A O   1 
HETATM 4171 O  O   . HOH Y 8 .   ? -52.478 50.476 0.066   1.00 29.79  ? 745 HOH A O   1 
HETATM 4172 O  O   . HOH Y 8 .   ? -22.542 37.373 -26.767 1.00 43.87  ? 746 HOH A O   1 
HETATM 4173 O  O   . HOH Y 8 .   ? -47.312 48.066 -7.422  1.00 37.86  ? 747 HOH A O   1 
HETATM 4174 O  O   . HOH Y 8 .   ? -26.689 56.332 -6.981  1.00 54.38  ? 748 HOH A O   1 
HETATM 4175 O  O   . HOH Y 8 .   ? -41.709 29.576 -25.610 1.00 53.17  ? 749 HOH A O   1 
HETATM 4176 O  O   . HOH Y 8 .   ? -14.398 26.744 31.481  1.00 40.91  ? 750 HOH A O   1 
HETATM 4177 O  O   . HOH Y 8 .   ? -27.952 42.680 -12.892 1.00 32.70  ? 751 HOH A O   1 
HETATM 4178 O  O   . HOH Y 8 .   ? -67.132 33.803 -11.218 1.00 51.18  ? 752 HOH A O   1 
HETATM 4179 O  O   . HOH Y 8 .   ? -30.222 55.628 10.137  1.00 39.57  ? 753 HOH A O   1 
HETATM 4180 O  O   . HOH Y 8 .   ? -43.496 44.989 21.398  1.00 46.36  ? 754 HOH A O   1 
HETATM 4181 O  O   . HOH Y 8 .   ? -55.809 29.462 13.210  1.00 27.52  ? 755 HOH A O   1 
HETATM 4182 O  O   . HOH Y 8 .   ? -14.530 45.735 17.034  1.00 47.81  ? 756 HOH A O   1 
HETATM 4183 O  O   . HOH Y 8 .   ? -15.603 47.661 21.135  1.00 36.28  ? 757 HOH A O   1 
HETATM 4184 O  O   . HOH Y 8 .   ? -13.521 35.702 40.699  1.00 30.30  ? 758 HOH A O   1 
HETATM 4185 O  O   . HOH Y 8 .   ? -34.929 35.689 -3.713  1.00 28.64  ? 759 HOH A O   1 
HETATM 4186 O  O   . HOH Y 8 .   ? -29.765 50.471 -15.981 1.00 39.94  ? 760 HOH A O   1 
HETATM 4187 O  O   . HOH Y 8 .   ? -14.902 39.149 3.595   1.00 40.22  ? 761 HOH A O   1 
HETATM 4188 O  O   . HOH Y 8 .   ? -18.191 46.477 30.477  1.00 25.80  ? 762 HOH A O   1 
HETATM 4189 O  O   . HOH Y 8 .   ? -34.033 44.158 -38.152 1.00 51.95  ? 763 HOH A O   1 
HETATM 4190 O  O   . HOH Y 8 .   ? -33.311 15.030 9.895   1.00 55.48  ? 764 HOH A O   1 
HETATM 4191 O  O   . HOH Y 8 .   ? -37.415 62.437 6.122   1.00 47.50  ? 765 HOH A O   1 
HETATM 4192 O  O   . HOH Y 8 .   ? -26.855 49.949 24.410  1.00 39.13  ? 766 HOH A O   1 
HETATM 4193 O  O   . HOH Y 8 .   ? -28.194 47.835 18.547  1.00 26.69  ? 767 HOH A O   1 
HETATM 4194 O  O   . HOH Y 8 .   ? -26.742 45.672 -15.199 1.00 34.04  ? 768 HOH A O   1 
HETATM 4195 O  O   . HOH Y 8 .   ? -25.470 39.888 -34.554 1.00 44.69  ? 769 HOH A O   1 
HETATM 4196 O  O   . HOH Y 8 .   ? -36.995 52.579 -3.867  1.00 30.20  ? 770 HOH A O   1 
HETATM 4197 O  O   . HOH Y 8 .   ? -57.883 42.272 -10.135 1.00 32.28  ? 771 HOH A O   1 
HETATM 4198 O  O   . HOH Y 8 .   ? -40.604 65.555 6.716   1.00 47.40  ? 772 HOH A O   1 
HETATM 4199 O  O   . HOH Y 8 .   ? -55.657 23.431 4.658   1.00 41.74  ? 773 HOH A O   1 
HETATM 4200 O  O   . HOH Y 8 .   ? -44.976 27.280 19.950  1.00 41.99  ? 774 HOH A O   1 
HETATM 4201 O  O   . HOH Y 8 .   ? -10.202 31.027 25.186  1.00 49.14  ? 775 HOH A O   1 
HETATM 4202 O  O   . HOH Y 8 .   ? -21.566 25.405 14.547  1.00 50.26  ? 776 HOH A O   1 
HETATM 4203 O  O   . HOH Y 8 .   ? -62.028 29.971 12.461  1.00 59.04  ? 777 HOH A O   1 
HETATM 4204 O  O   . HOH Y 8 .   ? -45.169 36.150 -18.559 1.00 58.49  ? 778 HOH A O   1 
HETATM 4205 O  O   . HOH Y 8 .   ? -18.366 49.901 -1.737  1.00 53.37  ? 779 HOH A O   1 
HETATM 4206 O  O   . HOH Y 8 .   ? -42.300 29.090 21.318  1.00 41.29  ? 780 HOH A O   1 
HETATM 4207 O  O   . HOH Y 8 .   ? -44.605 20.357 21.242  1.00 36.93  ? 781 HOH A O   1 
HETATM 4208 O  O   . HOH Y 8 .   ? -21.193 43.676 -1.445  1.00 38.11  ? 782 HOH A O   1 
HETATM 4209 O  O   . HOH Y 8 .   ? -53.979 61.011 -0.994  1.00 46.47  ? 783 HOH A O   1 
HETATM 4210 O  O   . HOH Y 8 .   ? -51.988 17.164 0.327   1.00 44.24  ? 784 HOH A O   1 
HETATM 4211 O  O   . HOH Y 8 .   ? -55.022 33.073 23.200  1.00 43.74  ? 785 HOH A O   1 
HETATM 4212 O  O   . HOH Y 8 .   ? -33.807 47.981 -30.224 1.00 47.34  ? 786 HOH A O   1 
HETATM 4213 O  O   . HOH Y 8 .   ? -30.817 49.622 -10.481 1.00 38.28  ? 787 HOH A O   1 
HETATM 4214 O  O   . HOH Y 8 .   ? -17.657 41.912 36.110  1.00 39.01  ? 788 HOH A O   1 
HETATM 4215 O  O   . HOH Y 8 .   ? -36.816 45.572 21.355  1.00 27.57  ? 789 HOH A O   1 
HETATM 4216 O  O   . HOH Y 8 .   ? -64.895 31.797 9.787   1.00 38.94  ? 790 HOH A O   1 
HETATM 4217 O  O   . HOH Y 8 .   ? -27.973 47.874 -4.573  1.00 42.13  ? 791 HOH A O   1 
HETATM 4218 O  O   . HOH Y 8 .   ? -29.269 53.610 -9.142  1.00 32.85  ? 792 HOH A O   1 
HETATM 4219 O  O   . HOH Y 8 .   ? -21.434 52.800 20.340  1.00 32.90  ? 793 HOH A O   1 
HETATM 4220 O  O   . HOH Y 8 .   ? -19.421 38.249 -4.515  1.00 41.69  ? 794 HOH A O   1 
HETATM 4221 O  O   . HOH Y 8 .   ? -40.212 49.505 17.381  1.00 56.06  ? 795 HOH A O   1 
HETATM 4222 O  O   . HOH Y 8 .   ? -29.216 42.914 30.397  1.00 30.53  ? 796 HOH A O   1 
HETATM 4223 O  O   . HOH Y 8 .   ? -75.887 45.112 6.419   1.00 47.43  ? 797 HOH A O   1 
HETATM 4224 O  O   . HOH Y 8 .   ? -67.638 38.437 12.115  1.00 28.40  ? 798 HOH A O   1 
HETATM 4225 O  O   . HOH Y 8 .   ? -39.346 42.636 -10.541 1.00 43.59  ? 799 HOH A O   1 
HETATM 4226 O  O   . HOH Y 8 .   ? -12.410 30.624 20.954  1.00 36.08  ? 800 HOH A O   1 
HETATM 4227 O  O   . HOH Y 8 .   ? -42.946 65.762 6.558   1.00 50.82  ? 801 HOH A O   1 
HETATM 4228 O  O   A HOH Y 8 .   ? -30.662 20.896 18.042  0.58 18.47  ? 802 HOH A O   1 
HETATM 4229 O  O   B HOH Y 8 .   ? -29.243 19.927 17.576  0.42 25.87  ? 802 HOH A O   1 
HETATM 4230 O  O   . HOH Y 8 .   ? -34.223 40.585 -37.917 1.00 43.14  ? 803 HOH A O   1 
HETATM 4231 O  O   . HOH Y 8 .   ? -40.773 48.941 -13.298 1.00 44.70  ? 804 HOH A O   1 
HETATM 4232 O  O   . HOH Y 8 .   ? -45.463 47.675 14.733  1.00 38.51  ? 805 HOH A O   1 
HETATM 4233 O  O   . HOH Y 8 .   ? -31.391 28.852 -2.703  1.00 35.02  ? 806 HOH A O   1 
HETATM 4234 O  O   . HOH Y 8 .   ? -44.030 64.345 -7.962  1.00 50.84  ? 807 HOH A O   1 
HETATM 4235 O  O   . HOH Y 8 .   ? -44.011 18.844 9.220   1.00 29.38  ? 808 HOH A O   1 
HETATM 4236 O  O   . HOH Y 8 .   ? -73.738 38.869 2.224   1.00 39.64  ? 809 HOH A O   1 
HETATM 4237 O  O   . HOH Y 8 .   ? -23.112 39.785 -10.657 1.00 34.73  ? 810 HOH A O   1 
HETATM 4238 O  O   . HOH Y 8 .   ? -53.750 44.237 -20.885 1.00 38.48  ? 811 HOH A O   1 
HETATM 4239 O  O   . HOH Y 8 .   ? -52.918 37.707 -8.465  1.00 36.32  ? 812 HOH A O   1 
HETATM 4240 O  O   . HOH Y 8 .   ? -32.538 60.509 -6.110  1.00 47.33  ? 813 HOH A O   1 
HETATM 4241 O  O   . HOH Y 8 .   ? -42.213 35.371 20.377  1.00 30.70  ? 814 HOH A O   1 
HETATM 4242 O  O   . HOH Y 8 .   ? -40.001 40.134 29.569  1.00 51.27  ? 815 HOH A O   1 
HETATM 4243 O  O   . HOH Y 8 .   ? -56.399 60.726 4.924   1.00 48.26  ? 816 HOH A O   1 
HETATM 4244 O  O   . HOH Y 8 .   ? -20.778 55.169 -3.424  1.00 56.57  ? 817 HOH A O   1 
HETATM 4245 O  O   . HOH Y 8 .   ? -35.349 34.888 -11.829 1.00 47.13  ? 818 HOH A O   1 
HETATM 4246 O  O   . HOH Y 8 .   ? -8.819  32.788 25.001  1.00 42.78  ? 819 HOH A O   1 
HETATM 4247 O  O   . HOH Y 8 .   ? -27.509 21.906 5.768   1.00 45.97  ? 820 HOH A O   1 
HETATM 4248 O  O   . HOH Y 8 .   ? -37.661 47.216 -0.506  1.00 27.52  ? 821 HOH A O   1 
HETATM 4249 O  O   . HOH Y 8 .   ? -57.136 55.389 15.934  1.00 41.80  ? 822 HOH A O   1 
HETATM 4250 O  O   . HOH Y 8 .   ? -58.776 27.307 -3.868  1.00 42.51  ? 823 HOH A O   1 
HETATM 4251 O  O   . HOH Y 8 .   ? -35.713 25.736 0.167   1.00 36.18  ? 824 HOH A O   1 
HETATM 4252 O  O   . HOH Y 8 .   ? -19.500 31.520 -0.090  1.00 53.29  ? 825 HOH A O   1 
HETATM 4253 O  O   . HOH Y 8 .   ? -31.829 45.886 -21.376 1.00 28.14  ? 826 HOH A O   1 
HETATM 4254 O  O   . HOH Y 8 .   ? -59.087 43.388 18.933  1.00 48.79  ? 827 HOH A O   1 
HETATM 4255 O  O   . HOH Y 8 .   ? -38.353 62.795 -7.824  1.00 56.44  ? 828 HOH A O   1 
HETATM 4256 O  O   . HOH Y 8 .   ? -66.530 45.191 0.342   1.00 39.19  ? 829 HOH A O   1 
HETATM 4257 O  O   . HOH Y 8 .   ? -13.029 42.804 21.619  1.00 38.29  ? 830 HOH A O   1 
HETATM 4258 O  O   . HOH Y 8 .   ? -43.555 31.545 21.593  1.00 27.32  ? 831 HOH A O   1 
HETATM 4259 O  O   . HOH Y 8 .   ? -22.648 34.996 -26.982 1.00 54.39  ? 832 HOH A O   1 
HETATM 4260 O  O   . HOH Y 8 .   ? -33.022 20.446 5.716   1.00 32.90  ? 833 HOH A O   1 
HETATM 4261 O  O   . HOH Y 8 .   ? -41.534 31.416 -26.921 1.00 59.41  ? 834 HOH A O   1 
HETATM 4262 O  O   . HOH Y 8 .   ? -36.202 50.853 -1.740  1.00 27.34  ? 835 HOH A O   1 
HETATM 4263 O  O   . HOH Y 8 .   ? -28.068 57.066 9.809   1.00 46.17  ? 836 HOH A O   1 
HETATM 4264 O  O   . HOH Y 8 .   ? -19.939 49.917 10.628  1.00 32.92  ? 837 HOH A O   1 
HETATM 4265 O  O   . HOH Y 8 .   ? -71.422 38.382 -3.638  1.00 43.23  ? 838 HOH A O   1 
HETATM 4266 O  O   . HOH Y 8 .   ? -24.810 21.976 18.749  1.00 40.14  ? 839 HOH A O   1 
HETATM 4267 O  O   . HOH Y 8 .   ? -25.016 22.089 6.575   1.00 42.66  ? 840 HOH A O   1 
HETATM 4268 O  O   . HOH Y 8 .   ? -29.721 51.093 -19.684 1.00 46.05  ? 841 HOH A O   1 
HETATM 4269 O  O   . HOH Y 8 .   ? -22.644 28.428 -6.300  1.00 51.01  ? 842 HOH A O   1 
HETATM 4270 O  O   . HOH Y 8 .   ? -37.427 61.447 10.573  1.00 46.94  ? 843 HOH A O   1 
HETATM 4271 O  O   . HOH Y 8 .   ? -27.152 20.271 18.433  1.00 42.07  ? 844 HOH A O   1 
HETATM 4272 O  O   . HOH Y 8 .   ? -35.535 35.651 -37.685 1.00 59.67  ? 845 HOH A O   1 
HETATM 4273 O  O   . HOH Y 8 .   ? -10.825 30.461 29.251  1.00 44.59  ? 846 HOH A O   1 
HETATM 4274 O  O   . HOH Y 8 .   ? -70.154 34.832 8.168   1.00 48.91  ? 847 HOH A O   1 
HETATM 4275 O  O   . HOH Y 8 .   ? -36.950 43.636 -37.251 1.00 55.02  ? 848 HOH A O   1 
HETATM 4276 O  O   . HOH Y 8 .   ? -61.921 51.084 -1.777  1.00 40.41  ? 849 HOH A O   1 
HETATM 4277 O  O   . HOH Y 8 .   ? -25.553 49.586 -5.821  1.00 49.83  ? 850 HOH A O   1 
HETATM 4278 O  O   . HOH Y 8 .   ? -41.642 54.300 -15.044 1.00 42.22  ? 851 HOH A O   1 
HETATM 4279 O  O   . HOH Y 8 .   ? -40.254 30.094 22.577  1.00 36.27  ? 852 HOH A O   1 
HETATM 4280 O  O   . HOH Y 8 .   ? -51.621 53.951 15.986  1.00 36.63  ? 853 HOH A O   1 
HETATM 4281 O  O   . HOH Y 8 .   ? -24.543 50.167 -3.898  1.00 47.08  ? 854 HOH A O   1 
HETATM 4282 O  O   . HOH Y 8 .   ? -25.088 39.317 34.931  1.00 27.38  ? 855 HOH A O   1 
HETATM 4283 O  O   . HOH Y 8 .   ? -30.939 62.301 0.191   1.00 49.37  ? 856 HOH A O   1 
HETATM 4284 O  O   . HOH Y 8 .   ? -51.190 39.990 -10.359 1.00 32.08  ? 857 HOH A O   1 
HETATM 4285 O  O   A HOH Y 8 .   ? -19.835 51.873 13.515  0.57 26.96  ? 858 HOH A O   1 
HETATM 4286 O  O   B HOH Y 8 .   ? -19.217 54.025 13.655  0.43 31.47  ? 858 HOH A O   1 
HETATM 4287 O  O   . HOH Y 8 .   ? -67.926 32.271 5.904   1.00 40.25  ? 859 HOH A O   1 
HETATM 4288 O  O   . HOH Y 8 .   ? -54.643 33.731 -10.088 1.00 49.55  ? 860 HOH A O   1 
HETATM 4289 O  O   . HOH Y 8 .   ? -39.243 29.518 28.467  1.00 34.90  ? 861 HOH A O   1 
HETATM 4290 O  O   . HOH Y 8 .   ? -31.252 62.159 -4.876  1.00 52.79  ? 862 HOH A O   1 
HETATM 4291 O  O   . HOH Y 8 .   ? -44.326 16.794 -4.152  1.00 66.61  ? 863 HOH A O   1 
HETATM 4292 O  O   . HOH Y 8 .   ? -39.592 42.613 22.459  1.00 52.88  ? 864 HOH A O   1 
HETATM 4293 O  O   . HOH Y 8 .   ? -43.379 43.803 -32.267 1.00 53.52  ? 865 HOH A O   1 
HETATM 4294 O  O   . HOH Y 8 .   ? -22.041 53.316 17.561  1.00 40.27  ? 866 HOH A O   1 
HETATM 4295 O  O   . HOH Y 8 .   ? -28.613 33.159 -30.429 1.00 40.52  ? 867 HOH A O   1 
HETATM 4296 O  O   . HOH Y 8 .   ? -31.264 52.411 -11.954 1.00 47.30  ? 868 HOH A O   1 
HETATM 4297 O  O   . HOH Y 8 .   ? -32.746 53.566 13.929  1.00 43.28  ? 869 HOH A O   1 
HETATM 4298 O  O   . HOH Y 8 .   ? -68.210 36.075 16.314  1.00 36.92  ? 870 HOH A O   1 
HETATM 4299 O  O   . HOH Y 8 .   ? -21.268 51.318 16.168  1.00 34.96  ? 871 HOH A O   1 
HETATM 4300 O  O   . HOH Y 8 .   ? -24.159 41.252 -8.990  1.00 36.40  ? 872 HOH A O   1 
HETATM 4301 O  O   . HOH Y 8 .   ? -69.452 42.090 -5.042  1.00 38.03  ? 873 HOH A O   1 
HETATM 4302 O  O   . HOH Y 8 .   ? -18.686 44.266 1.072   1.00 42.80  ? 874 HOH A O   1 
HETATM 4303 O  O   . HOH Y 8 .   ? -39.746 31.428 -29.502 1.00 59.85  ? 875 HOH A O   1 
HETATM 4304 O  O   . HOH Y 8 .   ? -28.493 46.253 -6.138  1.00 34.12  ? 876 HOH A O   1 
HETATM 4305 O  O   . HOH Y 8 .   ? -37.042 25.817 28.544  1.00 55.88  ? 877 HOH A O   1 
HETATM 4306 O  O   . HOH Y 8 .   ? -40.676 31.660 -6.500  1.00 35.41  ? 878 HOH A O   1 
HETATM 4307 O  O   . HOH Y 8 .   ? -68.045 32.798 3.487   1.00 38.38  ? 879 HOH A O   1 
HETATM 4308 O  O   . HOH Y 8 .   ? -53.672 27.977 21.490  1.00 58.83  ? 880 HOH A O   1 
HETATM 4309 O  O   . HOH Y 8 .   ? -44.590 38.311 -8.217  1.00 44.04  ? 881 HOH A O   1 
HETATM 4310 O  O   . HOH Y 8 .   ? -31.640 59.214 9.450   1.00 51.62  ? 882 HOH A O   1 
HETATM 4311 O  O   . HOH Y 8 .   ? -18.644 55.168 -2.415  1.00 60.15  ? 883 HOH A O   1 
HETATM 4312 O  O   . HOH Y 8 .   ? -14.794 45.900 1.761   1.00 51.88  ? 884 HOH A O   1 
HETATM 4313 O  O   . HOH Y 8 .   ? -22.908 41.570 -4.302  1.00 50.10  ? 885 HOH A O   1 
HETATM 4314 O  O   . HOH Y 8 .   ? -44.341 26.010 -6.468  1.00 53.64  ? 886 HOH A O   1 
HETATM 4315 O  O   . HOH Y 8 .   ? -30.960 15.165 13.575  1.00 48.01  ? 887 HOH A O   1 
HETATM 4316 O  O   . HOH Y 8 .   ? -27.359 30.466 37.138  1.00 48.42  ? 888 HOH A O   1 
HETATM 4317 O  O   . HOH Y 8 .   ? -44.199 42.195 -33.770 1.00 44.74  ? 889 HOH A O   1 
HETATM 4318 O  O   . HOH Y 8 .   ? -53.945 55.331 15.554  1.00 39.57  ? 890 HOH A O   1 
HETATM 4319 O  O   . HOH Y 8 .   ? -33.928 27.554 -1.184  1.00 52.54  ? 891 HOH A O   1 
HETATM 4320 O  O   . HOH Y 8 .   ? -22.318 56.271 10.096  1.00 54.96  ? 892 HOH A O   1 
HETATM 4321 O  O   . HOH Y 8 .   ? -35.682 53.853 15.922  1.00 49.52  ? 893 HOH A O   1 
HETATM 4322 O  O   . HOH Y 8 .   ? -15.848 47.403 10.805  1.00 42.36  ? 894 HOH A O   1 
HETATM 4323 O  O   . HOH Y 8 .   ? -60.053 25.657 8.359   1.00 50.73  ? 895 HOH A O   1 
HETATM 4324 O  O   . HOH Y 8 .   ? -20.677 54.242 10.071  1.00 54.31  ? 896 HOH A O   1 
HETATM 4325 O  O   . HOH Y 8 .   ? -42.209 37.569 -8.318  1.00 56.87  ? 897 HOH A O   1 
HETATM 4326 O  O   . HOH Y 8 .   ? -18.242 47.973 11.137  1.00 30.65  ? 898 HOH A O   1 
HETATM 4327 O  O   . HOH Y 8 .   ? -56.756 56.467 -0.731  1.00 67.76  ? 899 HOH A O   1 
HETATM 4328 O  O   . HOH Y 8 .   ? -27.040 26.007 38.744  1.00 51.04  ? 900 HOH A O   1 
HETATM 4329 O  O   . HOH Y 8 .   ? -60.409 27.435 12.498  1.00 63.03  ? 901 HOH A O   1 
HETATM 4330 O  O   . HOH Y 8 .   ? -55.734 29.359 21.630  1.00 55.94  ? 902 HOH A O   1 
HETATM 4331 O  O   . HOH Y 8 .   ? -37.465 43.463 22.638  1.00 47.25  ? 903 HOH A O   1 
HETATM 4332 O  O   . HOH Y 8 .   ? -23.924 33.369 -26.098 1.00 46.65  ? 904 HOH A O   1 
HETATM 4333 O  O   . HOH Y 8 .   ? -24.177 44.111 -27.036 1.00 37.94  ? 905 HOH A O   1 
HETATM 4334 O  O   . HOH Y 8 .   ? -54.752 61.845 5.867   1.00 51.38  ? 906 HOH A O   1 
HETATM 4335 O  O   . HOH Y 8 .   ? -42.513 25.320 -5.239  1.00 46.50  ? 907 HOH A O   1 
HETATM 4336 O  O   . HOH Y 8 .   ? -28.733 45.713 -34.837 1.00 49.13  ? 908 HOH A O   1 
HETATM 4337 O  O   . HOH Y 8 .   ? -69.612 32.890 1.693   1.00 55.25  ? 909 HOH A O   1 
HETATM 4338 O  O   . HOH Y 8 .   ? -46.212 47.731 17.218  1.00 44.75  ? 910 HOH A O   1 
HETATM 4339 O  O   . HOH Y 8 .   ? -51.646 51.855 17.022  1.00 39.75  ? 911 HOH A O   1 
HETATM 4340 O  O   . HOH Y 8 .   ? -52.814 48.942 19.729  1.00 60.51  ? 912 HOH A O   1 
HETATM 4341 O  O   . HOH Y 8 .   ? -45.507 61.936 -9.751  1.00 59.38  ? 913 HOH A O   1 
HETATM 4342 O  O   . HOH Y 8 .   ? -33.352 59.605 7.860   1.00 38.98  ? 914 HOH A O   1 
HETATM 4343 O  O   . HOH Y 8 .   ? -75.950 46.551 3.414   1.00 53.63  ? 915 HOH A O   1 
HETATM 4344 O  O   . HOH Y 8 .   ? -37.762 59.208 14.173  1.00 50.61  ? 916 HOH A O   1 
HETATM 4345 O  O   . HOH Y 8 .   ? -35.042 47.849 20.694  1.00 45.69  ? 917 HOH A O   1 
HETATM 4346 O  O   . HOH Y 8 .   ? -34.700 25.591 -1.823  1.00 63.96  ? 918 HOH A O   1 
HETATM 4347 O  O   . HOH Y 8 .   ? -28.553 22.303 29.684  1.00 58.70  ? 919 HOH A O   1 
HETATM 4348 O  O   . HOH Y 8 .   ? -50.824 28.288 -10.357 1.00 55.05  ? 920 HOH A O   1 
HETATM 4349 O  O   . HOH Y 8 .   ? -14.408 47.237 13.627  1.00 46.65  ? 921 HOH A O   1 
HETATM 4350 O  O   . HOH Y 8 .   ? -53.532 53.360 -5.086  1.00 38.99  ? 922 HOH A O   1 
HETATM 4351 O  O   . HOH Y 8 .   ? -69.293 34.399 10.370  1.00 30.29  ? 923 HOH A O   1 
HETATM 4352 O  O   . HOH Y 8 .   ? -60.568 43.925 20.534  1.00 53.58  ? 924 HOH A O   1 
HETATM 4353 O  O   . HOH Y 8 .   ? -14.030 42.621 3.430   1.00 66.08  ? 925 HOH A O   1 
HETATM 4354 O  O   . HOH Y 8 .   ? -33.407 50.676 -32.421 1.00 54.09  ? 926 HOH A O   1 
HETATM 4355 O  O   . HOH Y 8 .   ? -41.274 32.077 22.705  1.00 44.61  ? 927 HOH A O   1 
HETATM 4356 O  O   . HOH Y 8 .   ? -15.301 43.636 1.702   1.00 53.86  ? 928 HOH A O   1 
HETATM 4357 O  O   . HOH Y 8 .   ? -30.905 23.169 29.604  1.00 48.91  ? 929 HOH A O   1 
HETATM 4358 O  O   . HOH Y 8 .   ? -25.146 55.150 19.502  1.00 43.93  ? 930 HOH A O   1 
HETATM 4359 O  O   . HOH Y 8 .   ? -27.216 23.778 25.736  1.00 51.98  ? 931 HOH A O   1 
HETATM 4360 O  O   . HOH Y 8 .   ? -56.382 21.142 4.363   1.00 52.45  ? 932 HOH A O   1 
HETATM 4361 O  O   . HOH Y 8 .   ? -34.849 16.555 7.452   1.00 54.39  ? 933 HOH A O   1 
HETATM 4362 O  O   . HOH Y 8 .   ? -22.954 36.849 -19.789 1.00 52.57  ? 934 HOH A O   1 
HETATM 4363 O  O   . HOH Y 8 .   ? -57.377 53.567 -2.524  1.00 56.89  ? 935 HOH A O   1 
HETATM 4364 O  O   . HOH Y 8 .   ? -25.753 45.576 30.848  1.00 57.19  ? 936 HOH A O   1 
HETATM 4365 O  O   . HOH Y 8 .   ? -26.463 23.029 23.712  1.00 44.99  ? 937 HOH A O   1 
HETATM 4366 O  O   . HOH Y 8 .   ? -63.351 30.055 9.404   1.00 50.29  ? 938 HOH A O   1 
HETATM 4367 O  O   . HOH Y 8 .   ? -54.539 36.192 -9.866  1.00 39.58  ? 939 HOH A O   1 
HETATM 4368 O  O   . HOH Y 8 .   ? -24.714 43.794 -30.824 1.00 42.29  ? 940 HOH A O   1 
HETATM 4369 O  O   . HOH Y 8 .   ? -25.093 44.445 -6.263  1.00 52.72  ? 941 HOH A O   1 
HETATM 4370 O  O   . HOH Y 8 .   ? -11.000 28.667 23.736  1.00 50.00  ? 942 HOH A O   1 
HETATM 4371 O  O   . HOH Y 8 .   ? -71.081 40.673 10.955  1.00 40.26  ? 943 HOH A O   1 
HETATM 4372 O  O   . HOH Y 8 .   ? -44.275 34.460 -19.720 1.00 47.97  ? 944 HOH A O   1 
HETATM 4373 O  O   . HOH Y 8 .   ? -37.356 57.032 16.012  1.00 55.11  ? 945 HOH A O   1 
HETATM 4374 O  O   . HOH Y 8 .   ? -69.794 36.093 11.719  1.00 44.64  ? 946 HOH A O   1 
HETATM 4375 O  O   . HOH Y 8 .   ? -32.378 20.980 19.990  1.00 46.00  ? 947 HOH A O   1 
HETATM 4376 O  O   . HOH Y 8 .   ? -24.460 42.103 -5.860  1.00 42.10  ? 949 HOH A O   1 
HETATM 4377 O  O   . HOH Y 8 .   ? -32.714 17.329 6.799   1.00 49.92  ? 950 HOH A O   1 
HETATM 4378 O  O   . HOH Y 8 .   ? -44.889 30.080 22.765  1.00 60.72  ? 951 HOH A O   1 
HETATM 4379 O  O   . HOH Y 8 .   ? -22.919 32.048 42.260  1.00 46.38  ? 952 HOH A O   1 
HETATM 4380 O  O   . HOH Y 8 .   ? -51.956 61.975 -0.300  1.00 45.47  ? 953 HOH A O   1 
HETATM 4381 O  O   . HOH Y 8 .   ? -68.533 46.381 -1.538  1.00 49.95  ? 954 HOH A O   1 
HETATM 4382 O  O   . HOH Y 8 .   ? -30.321 23.642 25.181  1.00 47.02  ? 955 HOH A O   1 
HETATM 4383 O  O   . HOH Y 8 .   ? -35.764 61.280 8.693   1.00 52.72  ? 956 HOH A O   1 
HETATM 4384 O  O   . HOH Y 8 .   ? -25.457 35.988 37.620  1.00 48.72  ? 957 HOH A O   1 
HETATM 4385 O  O   . HOH Y 8 .   ? -30.448 20.384 3.603   1.00 47.21  ? 958 HOH A O   1 
HETATM 4386 O  O   . HOH Y 8 .   ? -41.411 29.410 29.148  1.00 45.91  ? 959 HOH A O   1 
HETATM 4387 O  O   . HOH Y 8 .   ? -31.524 55.922 12.953  1.00 41.95  ? 960 HOH A O   1 
HETATM 4388 O  O   . HOH Y 8 .   ? -31.361 44.476 31.751  1.00 44.04  ? 961 HOH A O   1 
HETATM 4389 O  O   . HOH Y 8 .   ? -26.033 56.727 17.461  1.00 57.56  ? 962 HOH A O   1 
HETATM 4390 O  O   . HOH Y 8 .   ? -22.674 36.364 -22.118 1.00 55.18  ? 963 HOH A O   1 
HETATM 4391 O  O   . HOH Y 8 .   ? -54.365 52.002 -7.359  1.00 56.22  ? 964 HOH A O   1 
HETATM 4392 O  O   . HOH Y 8 .   ? -35.129 56.009 16.419  1.00 58.68  ? 965 HOH A O   1 
HETATM 4393 O  O   . HOH Y 8 .   ? -67.769 32.005 10.536  1.00 43.08  ? 966 HOH A O   1 
HETATM 4394 O  O   . HOH Y 8 .   ? -41.933 32.967 25.342  1.00 44.10  ? 967 HOH A O   1 
HETATM 4395 O  O   . HOH Y 8 .   ? -42.874 33.560 29.194  1.00 47.09  ? 968 HOH A O   1 
HETATM 4396 O  O   . HOH Y 8 .   ? -34.684 48.404 23.727  1.00 45.25  ? 969 HOH A O   1 
HETATM 4397 O  O   . HOH Y 8 .   ? -33.204 62.905 2.841   1.00 54.65  ? 970 HOH A O   1 
HETATM 4398 O  O   . HOH Y 8 .   ? -35.174 61.424 3.611   1.00 56.99  ? 971 HOH A O   1 
HETATM 4399 O  O   . HOH Y 8 .   ? -23.647 50.507 28.398  1.00 54.05  ? 972 HOH A O   1 
HETATM 4400 O  O   . HOH Y 8 .   ? -29.088 25.237 0.500   1.00 49.01  ? 973 HOH A O   1 
HETATM 4401 O  O   . HOH Y 8 .   ? -72.375 38.264 11.935  1.00 47.53  ? 974 HOH A O   1 
HETATM 4402 O  O   . HOH Y 8 .   ? -31.546 25.959 -1.092  1.00 53.03  ? 975 HOH A O   1 
HETATM 4403 O  O   . HOH Y 8 .   ? -50.008 63.080 0.559   1.00 45.02  ? 976 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   ? 0.9624 1.0664 0.7736 -0.1179 -0.0934 0.1835  1   MET A N   
2    C CA  . MET A 1   ? 0.9999 1.0863 0.8238 -0.1255 -0.0898 0.1961  1   MET A CA  
3    C C   . MET A 1   ? 0.9030 0.9633 0.7576 -0.1157 -0.1033 0.2008  1   MET A C   
4    O O   . MET A 1   ? 1.0034 1.0662 0.8690 -0.1039 -0.1053 0.1849  1   MET A O   
5    C CB  . MET A 1   ? 0.8588 0.9601 0.6807 -0.1314 -0.0682 0.1777  1   MET A CB  
6    C CG  . MET A 1   ? 0.9371 1.0696 0.7386 -0.1361 -0.0551 0.1607  1   MET A CG  
7    S SD  . MET A 1   ? 1.3039 1.4521 1.1068 -0.1222 -0.0571 0.1365  1   MET A SD  
8    C CE  . MET A 1   ? 0.7504 0.8961 0.5742 -0.1152 -0.0454 0.1140  1   MET A CE  
9    N N   . LYS A 2   ? 0.8850 0.9210 0.7574 -0.1202 -0.1132 0.2219  2   LYS A N   
10   C CA  . LYS A 2   ? 0.9037 0.9161 0.8127 -0.1118 -0.1230 0.2222  2   LYS A CA  
11   C C   . LYS A 2   ? 0.7352 0.7544 0.6460 -0.1139 -0.1047 0.2063  2   LYS A C   
12   O O   . LYS A 2   ? 0.7927 0.8207 0.6912 -0.1263 -0.0886 0.2060  2   LYS A O   
13   C CB  . LYS A 2   ? 0.9593 0.9435 0.8949 -0.1164 -0.1381 0.2460  2   LYS A CB  
14   C CG  . LYS A 2   ? 0.8488 0.8070 0.8340 -0.1054 -0.1513 0.2428  2   LYS A CG  
15   C CD  . LYS A 2   ? 0.6768 0.6278 0.6873 -0.0877 -0.1722 0.2353  2   LYS A CD  
16   C CE  . LYS A 2   ? 0.6830 0.6083 0.7541 -0.0770 -0.1881 0.2298  2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.6870 0.6021 0.7870 -0.0632 -0.2143 0.2303  2   LYS A NZ  
18   N N   . VAL A 3   ? 0.5857 0.6054 0.5214 -0.0974 -0.1013 0.1788  3   VAL A N   
19   C CA  . VAL A 3   ? 0.4671 0.4933 0.4125 -0.0939 -0.0830 0.1545  3   VAL A CA  
20   C C   . VAL A 3   ? 0.4190 0.4272 0.4087 -0.0819 -0.0894 0.1432  3   VAL A C   
21   O O   . VAL A 3   ? 0.4261 0.4190 0.4420 -0.0748 -0.1072 0.1500  3   VAL A O   
22   C CB  . VAL A 3   ? 0.4308 0.4789 0.3612 -0.0867 -0.0704 0.1309  3   VAL A CB  
23   C CG1 . VAL A 3   ? 0.4387 0.5075 0.3317 -0.0973 -0.0665 0.1375  3   VAL A CG1 
24   C CG2 . VAL A 3   ? 0.3783 0.4244 0.3295 -0.0708 -0.0785 0.1186  3   VAL A CG2 
25   N N   . ASP A 4   ? 0.3559 0.3681 0.3561 -0.0791 -0.0760 0.1239  4   ASP A N   
26   C CA  . ASP A 4   ? 0.4598 0.4616 0.5012 -0.0669 -0.0810 0.1076  4   ASP A CA  
27   C C   . ASP A 4   ? 0.3741 0.3877 0.4232 -0.0509 -0.0789 0.0847  4   ASP A C   
28   O O   . ASP A 4   ? 0.3649 0.3725 0.4467 -0.0402 -0.0901 0.0766  4   ASP A O   
29   C CB  . ASP A 4   ? 0.3756 0.3789 0.4262 -0.0701 -0.0695 0.0953  4   ASP A CB  
30   C CG  . ASP A 4   ? 0.4341 0.4239 0.4899 -0.0864 -0.0719 0.1173  4   ASP A CG  
31   O OD1 . ASP A 4   ? 0.5026 0.4725 0.5819 -0.0887 -0.0882 0.1357  4   ASP A OD1 
32   O OD2 . ASP A 4   ? 0.4836 0.4829 0.5223 -0.0976 -0.0581 0.1170  4   ASP A OD2 
33   N N   . TRP A 5   ? 0.3324 0.3637 0.3547 -0.0498 -0.0647 0.0738  5   TRP A N   
34   C CA  . TRP A 5   ? 0.3500 0.3938 0.3770 -0.0374 -0.0596 0.0548  5   TRP A CA  
35   C C   . TRP A 5   ? 0.2787 0.3345 0.2787 -0.0402 -0.0545 0.0584  5   TRP A C   
36   O O   . TRP A 5   ? 0.2963 0.3585 0.2707 -0.0491 -0.0469 0.0630  5   TRP A O   
37   C CB  . TRP A 5   ? 0.3425 0.3955 0.3713 -0.0314 -0.0474 0.0347  5   TRP A CB  
38   C CG  . TRP A 5   ? 0.3554 0.4031 0.4181 -0.0240 -0.0530 0.0219  5   TRP A CG  
39   C CD1 . TRP A 5   ? 0.3070 0.3450 0.3846 -0.0282 -0.0556 0.0222  5   TRP A CD1 
40   C CD2 . TRP A 5   ? 0.2746 0.3299 0.3649 -0.0112 -0.0565 0.0035  5   TRP A CD2 
41   N NE1 . TRP A 5   ? 0.3616 0.3995 0.4764 -0.0179 -0.0621 0.0042  5   TRP A NE1 
42   C CE2 . TRP A 5   ? 0.2833 0.3333 0.4055 -0.0073 -0.0626 -0.0084 5   TRP A CE2 
43   C CE3 . TRP A 5   ? 0.3141 0.3828 0.4083 -0.0035 -0.0545 -0.0059 5   TRP A CE3 
44   C CZ2 . TRP A 5   ? 0.2813 0.3414 0.4386 0.0052  -0.0671 -0.0320 5   TRP A CZ2 
45   C CZ3 . TRP A 5   ? 0.2853 0.3647 0.4120 0.0076  -0.0573 -0.0276 5   TRP A CZ3 
46   C CH2 . TRP A 5   ? 0.2829 0.3590 0.4405 0.0124  -0.0638 -0.0417 5   TRP A CH2 
47   N N   . LEU A 6   ? 0.2735 0.3344 0.2841 -0.0327 -0.0587 0.0535  6   LEU A N   
48   C CA  . LEU A 6   ? 0.2581 0.3317 0.2522 -0.0336 -0.0538 0.0521  6   LEU A CA  
49   C C   . LEU A 6   ? 0.3554 0.4402 0.3608 -0.0247 -0.0438 0.0353  6   LEU A C   
50   O O   . LEU A 6   ? 0.3017 0.3879 0.3324 -0.0167 -0.0478 0.0268  6   LEU A O   
51   C CB  . LEU A 6   ? 0.2909 0.3623 0.2876 -0.0345 -0.0687 0.0634  6   LEU A CB  
52   C CG  . LEU A 6   ? 0.4154 0.5017 0.4042 -0.0338 -0.0654 0.0578  6   LEU A CG  
53   C CD1 . LEU A 6   ? 0.2408 0.3365 0.2012 -0.0426 -0.0556 0.0587  6   LEU A CD1 
54   C CD2 . LEU A 6   ? 0.2757 0.3613 0.2721 -0.0321 -0.0831 0.0656  6   LEU A CD2 
55   N N   . PHE A 7   ? 0.3501 0.4439 0.3387 -0.0265 -0.0313 0.0306  7   PHE A N   
56   C CA  . PHE A 7   ? 0.3077 0.4125 0.3021 -0.0210 -0.0210 0.0201  7   PHE A CA  
57   C C   . PHE A 7   ? 0.3378 0.4497 0.3339 -0.0232 -0.0213 0.0220  7   PHE A C   
58   O O   . PHE A 7   ? 0.3526 0.4666 0.3344 -0.0288 -0.0195 0.0251  7   PHE A O   
59   C CB  . PHE A 7   ? 0.3154 0.4231 0.2939 -0.0214 -0.0098 0.0162  7   PHE A CB  
60   C CG  . PHE A 7   ? 0.2701 0.3744 0.2502 -0.0177 -0.0095 0.0101  7   PHE A CG  
61   C CD1 . PHE A 7   ? 0.3064 0.4197 0.2962 -0.0099 -0.0050 -0.0013 7   PHE A CD1 
62   C CD2 . PHE A 7   ? 0.2779 0.3734 0.2513 -0.0227 -0.0131 0.0138  7   PHE A CD2 
63   C CE1 . PHE A 7   ? 0.2819 0.3950 0.2758 -0.0055 -0.0060 -0.0107 7   PHE A CE1 
64   C CE2 . PHE A 7   ? 0.2889 0.3820 0.2692 -0.0192 -0.0134 0.0060  7   PHE A CE2 
65   C CZ  . PHE A 7   ? 0.2819 0.3835 0.2729 -0.0099 -0.0109 -0.0072 7   PHE A CZ  
66   N N   . LYS A 8   ? 0.3092 0.4270 0.3272 -0.0185 -0.0240 0.0169  8   LYS A N   
67   C CA  . LYS A 8   ? 0.2823 0.4075 0.3084 -0.0200 -0.0261 0.0164  8   LYS A CA  
68   C C   . LYS A 8   ? 0.3179 0.4535 0.3490 -0.0207 -0.0113 0.0111  8   LYS A C   
69   O O   . LYS A 8   ? 0.2792 0.4213 0.3171 -0.0176 -0.0014 0.0058  8   LYS A O   
70   C CB  . LYS A 8   ? 0.2540 0.3809 0.3063 -0.0149 -0.0383 0.0128  8   LYS A CB  
71   C CG  . LYS A 8   ? 0.2901 0.4049 0.3388 -0.0153 -0.0570 0.0232  8   LYS A CG  
72   C CD  . LYS A 8   ? 0.2701 0.3866 0.3469 -0.0093 -0.0725 0.0197  8   LYS A CD  
73   C CE  . LYS A 8   ? 0.2776 0.4006 0.3880 -0.0014 -0.0682 0.0041  8   LYS A CE  
74   N NZ  . LYS A 8   ? 0.3200 0.4460 0.4645 0.0054  -0.0842 -0.0028 8   LYS A NZ  
75   N N   . ASN A 9   ? 0.2689 0.4078 0.2979 -0.0253 -0.0101 0.0124  9   ASN A N   
76   C CA  . ASN A 9   ? 0.2887 0.4362 0.3327 -0.0271 0.0008  0.0095  9   ASN A CA  
77   C C   . ASN A 9   ? 0.2799 0.4269 0.3128 -0.0278 0.0146  0.0131  9   ASN A C   
78   O O   . ASN A 9   ? 0.2792 0.4351 0.3232 -0.0284 0.0257  0.0126  9   ASN A O   
79   C CB  . ASN A 9   ? 0.2355 0.3934 0.3086 -0.0242 0.0005  0.0020  9   ASN A CB  
80   C CG  . ASN A 9   ? 0.2364 0.4037 0.3313 -0.0285 0.0085  -0.0008 9   ASN A CG  
81   O OD1 . ASN A 9   ? 0.2934 0.4576 0.3839 -0.0332 0.0118  0.0033  9   ASN A OD1 
82   N ND2 . ASN A 9   ? 0.2603 0.4397 0.3845 -0.0270 0.0108  -0.0092 9   ASN A ND2 
83   N N   . VAL A 10  ? 0.2601 0.3986 0.2705 -0.0281 0.0138  0.0169  10  VAL A N   
84   C CA  . VAL A 10  ? 0.2744 0.4119 0.2714 -0.0276 0.0232  0.0208  10  VAL A CA  
85   C C   . VAL A 10  ? 0.3044 0.4380 0.3024 -0.0321 0.0257  0.0263  10  VAL A C   
86   O O   . VAL A 10  ? 0.3040 0.4353 0.3081 -0.0349 0.0189  0.0235  10  VAL A O   
87   C CB  . VAL A 10  ? 0.3198 0.4507 0.2978 -0.0243 0.0195  0.0192  10  VAL A CB  
88   C CG1 . VAL A 10  ? 0.2677 0.4028 0.2520 -0.0190 0.0180  0.0126  10  VAL A CG1 
89   C CG2 . VAL A 10  ? 0.2519 0.3753 0.2226 -0.0277 0.0105  0.0193  10  VAL A CG2 
90   N N   . THR A 11  ? 0.2719 0.4064 0.2655 -0.0329 0.0346  0.0340  11  THR A N   
91   C CA  . THR A 11  ? 0.2845 0.4105 0.2787 -0.0359 0.0338  0.0414  11  THR A CA  
92   C C   . THR A 11  ? 0.2717 0.3900 0.2459 -0.0322 0.0276  0.0392  11  THR A C   
93   O O   . THR A 11  ? 0.3280 0.4472 0.2840 -0.0282 0.0302  0.0416  11  THR A O   
94   C CB  . THR A 11  ? 0.2898 0.4181 0.2855 -0.0392 0.0441  0.0550  11  THR A CB  
95   O OG1 . THR A 11  ? 0.3006 0.4380 0.3203 -0.0441 0.0513  0.0554  11  THR A OG1 
96   C CG2 . THR A 11  ? 0.2728 0.3883 0.2730 -0.0417 0.0395  0.0647  11  THR A CG2 
97   N N   . VAL A 12  ? 0.3397 0.4540 0.3187 -0.0336 0.0195  0.0319  12  VAL A N   
98   C CA  . VAL A 12  ? 0.3746 0.4841 0.3401 -0.0312 0.0143  0.0269  12  VAL A CA  
99   C C   . VAL A 12  ? 0.3275 0.4291 0.2958 -0.0301 0.0122  0.0333  12  VAL A C   
100  O O   . VAL A 12  ? 0.3474 0.4456 0.3363 -0.0331 0.0090  0.0339  12  VAL A O   
101  C CB  . VAL A 12  ? 0.3210 0.4342 0.2908 -0.0346 0.0082  0.0155  12  VAL A CB  
102  C CG1 . VAL A 12  ? 0.3193 0.4302 0.2801 -0.0333 0.0047  0.0085  12  VAL A CG1 
103  C CG2 . VAL A 12  ? 0.2361 0.3546 0.2005 -0.0360 0.0075  0.0140  12  VAL A CG2 
104  N N   . ILE A 13  ? 0.2785 0.3773 0.2285 -0.0252 0.0123  0.0376  13  ILE A N   
105  C CA  . ILE A 13  ? 0.2690 0.3588 0.2185 -0.0225 0.0058  0.0429  13  ILE A CA  
106  C C   . ILE A 13  ? 0.3121 0.4021 0.2549 -0.0185 -0.0009 0.0287  13  ILE A C   
107  O O   . ILE A 13  ? 0.3280 0.4214 0.2530 -0.0140 0.0002  0.0259  13  ILE A O   
108  C CB  . ILE A 13  ? 0.3332 0.4226 0.2651 -0.0201 0.0098  0.0597  13  ILE A CB  
109  C CG1 . ILE A 13  ? 0.3298 0.4215 0.2729 -0.0267 0.0189  0.0736  13  ILE A CG1 
110  C CG2 . ILE A 13  ? 0.2735 0.3522 0.2015 -0.0158 -0.0008 0.0667  13  ILE A CG2 
111  C CD1 . ILE A 13  ? 0.3283 0.4209 0.2549 -0.0277 0.0239  0.0943  13  ILE A CD1 
112  N N   . ASP A 14  ? 0.2996 0.3888 0.2600 -0.0208 -0.0072 0.0168  14  ASP A N   
113  C CA  . ASP A 14  ? 0.2588 0.3543 0.2169 -0.0210 -0.0092 0.0003  14  ASP A CA  
114  C C   . ASP A 14  ? 0.3007 0.3923 0.2562 -0.0148 -0.0167 -0.0058 14  ASP A C   
115  O O   . ASP A 14  ? 0.3436 0.4417 0.3002 -0.0158 -0.0173 -0.0205 14  ASP A O   
116  C CB  . ASP A 14  ? 0.2600 0.3640 0.2370 -0.0273 -0.0107 -0.0135 14  ASP A CB  
117  C CG  . ASP A 14  ? 0.3090 0.4093 0.3126 -0.0259 -0.0194 -0.0196 14  ASP A CG  
118  O OD1 . ASP A 14  ? 0.3398 0.4279 0.3460 -0.0202 -0.0261 -0.0111 14  ASP A OD1 
119  O OD2 . ASP A 14  ? 0.3506 0.4612 0.3743 -0.0304 -0.0209 -0.0334 14  ASP A OD2 
120  N N   . GLY A 15  ? 0.2859 0.3680 0.2392 -0.0090 -0.0231 0.0055  15  GLY A N   
121  C CA  . GLY A 15  ? 0.2637 0.3425 0.2122 -0.0012 -0.0328 0.0007  15  GLY A CA  
122  C C   . GLY A 15  ? 0.2948 0.3671 0.2694 0.0013  -0.0460 -0.0071 15  GLY A C   
123  O O   . GLY A 15  ? 0.2877 0.3548 0.2613 0.0092  -0.0576 -0.0089 15  GLY A O   
124  N N   . SER A 16  ? 0.2409 0.3148 0.2416 -0.0045 -0.0461 -0.0142 16  SER A N   
125  C CA  . SER A 16  ? 0.3126 0.3833 0.3475 -0.0022 -0.0592 -0.0273 16  SER A CA  
126  C C   . SER A 16  ? 0.3379 0.3898 0.3866 0.0013  -0.0707 -0.0076 16  SER A C   
127  O O   . SER A 16  ? 0.2973 0.3424 0.3787 0.0052  -0.0857 -0.0167 16  SER A O   
128  C CB  . SER A 16  ? 0.2136 0.2985 0.2737 -0.0098 -0.0548 -0.0467 16  SER A CB  
129  O OG  . SER A 16  ? 0.3075 0.3894 0.3699 -0.0148 -0.0490 -0.0333 16  SER A OG  
130  N N   . GLY A 17  ? 0.3186 0.3627 0.3466 -0.0007 -0.0641 0.0187  17  GLY A N   
131  C CA  . GLY A 17  ? 0.2884 0.3150 0.3306 -0.0010 -0.0722 0.0418  17  GLY A CA  
132  C C   . GLY A 17  ? 0.3362 0.3615 0.4147 -0.0082 -0.0703 0.0391  17  GLY A C   
133  O O   . GLY A 17  ? 0.3462 0.3558 0.4432 -0.0104 -0.0761 0.0594  17  GLY A O   
134  N N   . GLY A 18  ? 0.2465 0.2888 0.3358 -0.0125 -0.0626 0.0153  18  GLY A N   
135  C CA  . GLY A 18  ? 0.2313 0.2773 0.3532 -0.0186 -0.0605 0.0091  18  GLY A CA  
136  C C   . GLY A 18  ? 0.3490 0.3956 0.4550 -0.0248 -0.0466 0.0283  18  GLY A C   
137  O O   . GLY A 18  ? 0.3454 0.3915 0.4149 -0.0245 -0.0375 0.0454  18  GLY A O   
138  N N   . PRO A 19  ? 0.2535 0.3042 0.3911 -0.0301 -0.0452 0.0221  19  PRO A N   
139  C CA  . PRO A 19  ? 0.3299 0.3826 0.4616 -0.0362 -0.0327 0.0374  19  PRO A CA  
140  C C   . PRO A 19  ? 0.3775 0.4450 0.4714 -0.0367 -0.0201 0.0342  19  PRO A C   
141  O O   . PRO A 19  ? 0.4002 0.4794 0.4803 -0.0348 -0.0204 0.0163  19  PRO A O   
142  C CB  . PRO A 19  ? 0.2410 0.3000 0.4194 -0.0402 -0.0367 0.0210  19  PRO A CB  
143  C CG  . PRO A 19  ? 0.4261 0.4808 0.6401 -0.0361 -0.0527 0.0038  19  PRO A CG  
144  C CD  . PRO A 19  ? 0.3202 0.3781 0.5036 -0.0303 -0.0551 -0.0039 19  PRO A CD  
145  N N   . GLN A 20  ? 0.3105 0.3782 0.3913 -0.0402 -0.0090 0.0516  20  GLN A N   
146  C CA  . GLN A 20  ? 0.3391 0.4199 0.3939 -0.0403 0.0012  0.0482  20  GLN A CA  
147  C C   . GLN A 20  ? 0.2719 0.3645 0.3480 -0.0440 0.0024  0.0344  20  GLN A C   
148  O O   . GLN A 20  ? 0.2950 0.3869 0.4064 -0.0470 -0.0021 0.0291  20  GLN A O   
149  C CB  . GLN A 20  ? 0.3283 0.4090 0.3635 -0.0419 0.0125  0.0686  20  GLN A CB  
150  C CG  . GLN A 20  ? 0.2723 0.3494 0.3335 -0.0491 0.0178  0.0832  20  GLN A CG  
151  C CD  . GLN A 20  ? 0.3916 0.4733 0.4321 -0.0526 0.0313  0.1039  20  GLN A CD  
152  O OE1 . GLN A 20  ? 0.4861 0.5663 0.4960 -0.0493 0.0319  0.1147  20  GLN A OE1 
153  N NE2 . GLN A 20  ? 0.3696 0.4600 0.4279 -0.0595 0.0421  0.1074  20  GLN A NE2 
154  N N   . TYR A 21  ? 0.2692 0.3727 0.3257 -0.0432 0.0067  0.0280  21  TYR A N   
155  C CA  . TYR A 21  ? 0.3019 0.4176 0.3728 -0.0456 0.0056  0.0161  21  TYR A CA  
156  C C   . TYR A 21  ? 0.2522 0.3740 0.3009 -0.0440 0.0106  0.0186  21  TYR A C   
157  O O   . TYR A 21  ? 0.3492 0.4675 0.3729 -0.0410 0.0139  0.0245  21  TYR A O   
158  C CB  . TYR A 21  ? 0.1991 0.3247 0.2769 -0.0458 -0.0033 -0.0040 21  TYR A CB  
159  C CG  . TYR A 21  ? 0.3351 0.4633 0.3836 -0.0442 -0.0045 -0.0090 21  TYR A CG  
160  C CD1 . TYR A 21  ? 0.2472 0.3685 0.2928 -0.0420 -0.0072 -0.0107 21  TYR A CD1 
161  C CD2 . TYR A 21  ? 0.2708 0.4082 0.2979 -0.0452 -0.0040 -0.0116 21  TYR A CD2 
162  C CE1 . TYR A 21  ? 0.2876 0.4129 0.3114 -0.0415 -0.0074 -0.0171 21  TYR A CE1 
163  C CE2 . TYR A 21  ? 0.2709 0.4102 0.2751 -0.0457 -0.0041 -0.0146 21  TYR A CE2 
164  C CZ  . TYR A 21  ? 0.4112 0.5457 0.4148 -0.0442 -0.0048 -0.0185 21  TYR A CZ  
165  O OH  . TYR A 21  ? 0.3421 0.4801 0.3278 -0.0456 -0.0040 -0.0232 21  TYR A OH  
166  N N   . ARG A 22  ? 0.2418 0.3732 0.3041 -0.0454 0.0095  0.0125  22  ARG A N   
167  C CA  . ARG A 22  ? 0.2540 0.3907 0.3036 -0.0432 0.0107  0.0133  22  ARG A CA  
168  C C   . ARG A 22  ? 0.2530 0.3961 0.2897 -0.0428 0.0012  0.0043  22  ARG A C   
169  O O   . ARG A 22  ? 0.2709 0.4227 0.3177 -0.0449 -0.0054 -0.0063 22  ARG A O   
170  C CB  . ARG A 22  ? 0.2327 0.3762 0.3073 -0.0445 0.0146  0.0132  22  ARG A CB  
171  C CG  . ARG A 22  ? 0.2919 0.4319 0.3752 -0.0474 0.0271  0.0255  22  ARG A CG  
172  C CD  . ARG A 22  ? 0.3257 0.4764 0.4311 -0.0495 0.0347  0.0249  22  ARG A CD  
173  N NE  . ARG A 22  ? 0.3353 0.4847 0.4541 -0.0559 0.0470  0.0378  22  ARG A NE  
174  C CZ  . ARG A 22  ? 0.3906 0.5496 0.5386 -0.0614 0.0560  0.0384  22  ARG A CZ  
175  N NH1 . ARG A 22  ? 0.3837 0.5548 0.5526 -0.0595 0.0528  0.0242  22  ARG A NH1 
176  N NH2 . ARG A 22  ? 0.2916 0.4482 0.4495 -0.0695 0.0677  0.0544  22  ARG A NH2 
177  N N   . ALA A 23  ? 0.2571 0.3973 0.2724 -0.0406 0.0002  0.0084  23  ALA A N   
178  C CA  . ALA A 23  ? 0.2706 0.4151 0.2698 -0.0422 -0.0082 0.0056  23  ALA A CA  
179  C C   . ALA A 23  ? 0.3355 0.4737 0.3236 -0.0393 -0.0102 0.0129  23  ALA A C   
180  O O   . ALA A 23  ? 0.3299 0.4635 0.3229 -0.0354 -0.0045 0.0159  23  ALA A O   
181  C CB  . ALA A 23  ? 0.1966 0.3419 0.1821 -0.0455 -0.0077 0.0011  23  ALA A CB  
182  N N   . ASP A 24  ? 0.2668 0.4068 0.2423 -0.0417 -0.0191 0.0154  24  ASP A N   
183  C CA  . ASP A 24  ? 0.2459 0.3766 0.2111 -0.0408 -0.0230 0.0236  24  ASP A CA  
184  C C   . ASP A 24  ? 0.3529 0.4808 0.2995 -0.0456 -0.0193 0.0250  24  ASP A C   
185  O O   . ASP A 24  ? 0.2806 0.4179 0.2177 -0.0514 -0.0184 0.0205  24  ASP A O   
186  C CB  . ASP A 24  ? 0.2970 0.4289 0.2597 -0.0420 -0.0368 0.0303  24  ASP A CB  
187  C CG  . ASP A 24  ? 0.2887 0.4237 0.2744 -0.0360 -0.0433 0.0270  24  ASP A CG  
188  O OD1 . ASP A 24  ? 0.2616 0.3982 0.2663 -0.0319 -0.0350 0.0203  24  ASP A OD1 
189  O OD2 . ASP A 24  ? 0.2667 0.4038 0.2515 -0.0360 -0.0574 0.0316  24  ASP A OD2 
190  N N   . VAL A 25  ? 0.3444 0.4622 0.2895 -0.0433 -0.0174 0.0284  25  VAL A N   
191  C CA  . VAL A 25  ? 0.3100 0.4247 0.2428 -0.0476 -0.0140 0.0285  25  VAL A CA  
192  C C   . VAL A 25  ? 0.3723 0.4772 0.3054 -0.0493 -0.0208 0.0381  25  VAL A C   
193  O O   . VAL A 25  ? 0.3553 0.4527 0.3034 -0.0426 -0.0247 0.0388  25  VAL A O   
194  C CB  . VAL A 25  ? 0.2831 0.3949 0.2184 -0.0422 -0.0061 0.0213  25  VAL A CB  
195  C CG1 . VAL A 25  ? 0.2285 0.3383 0.1560 -0.0460 -0.0039 0.0184  25  VAL A CG1 
196  C CG2 . VAL A 25  ? 0.2540 0.3716 0.1930 -0.0409 -0.0016 0.0158  25  VAL A CG2 
197  N N   . ALA A 26  ? 0.3056 0.4117 0.2253 -0.0589 -0.0222 0.0449  26  ALA A N   
198  C CA  . ALA A 26  ? 0.2949 0.3893 0.2168 -0.0631 -0.0293 0.0581  26  ALA A CA  
199  C C   . ALA A 26  ? 0.3193 0.4106 0.2404 -0.0683 -0.0224 0.0556  26  ALA A C   
200  O O   . ALA A 26  ? 0.2595 0.3620 0.1705 -0.0731 -0.0136 0.0471  26  ALA A O   
201  C CB  . ALA A 26  ? 0.2496 0.3480 0.1559 -0.0725 -0.0380 0.0738  26  ALA A CB  
202  N N   . VAL A 27  ? 0.3390 0.4160 0.2764 -0.0668 -0.0274 0.0608  27  VAL A N   
203  C CA  . VAL A 27  ? 0.2537 0.3266 0.1983 -0.0709 -0.0224 0.0571  27  VAL A CA  
204  C C   . VAL A 27  ? 0.3248 0.3856 0.2757 -0.0813 -0.0297 0.0763  27  VAL A C   
205  O O   . VAL A 27  ? 0.4217 0.4699 0.3851 -0.0783 -0.0423 0.0880  27  VAL A O   
206  C CB  . VAL A 27  ? 0.2971 0.3655 0.2624 -0.0579 -0.0216 0.0409  27  VAL A CB  
207  C CG1 . VAL A 27  ? 0.2289 0.2909 0.2101 -0.0615 -0.0207 0.0372  27  VAL A CG1 
208  C CG2 . VAL A 27  ? 0.2385 0.3188 0.1933 -0.0504 -0.0134 0.0259  27  VAL A CG2 
209  N N   . LYS A 28  ? 0.3485 0.4130 0.2935 -0.0940 -0.0223 0.0799  28  LYS A N   
210  C CA  . LYS A 28  ? 0.2999 0.3522 0.2526 -0.1068 -0.0272 0.1007  28  LYS A CA  
211  C C   . LYS A 28  ? 0.3620 0.4139 0.3315 -0.1121 -0.0182 0.0907  28  LYS A C   
212  O O   . LYS A 28  ? 0.3423 0.4114 0.3001 -0.1165 -0.0057 0.0772  28  LYS A O   
213  C CB  . LYS A 28  ? 0.3254 0.3885 0.2467 -0.1232 -0.0260 0.1217  28  LYS A CB  
214  C CG  . LYS A 28  ? 0.3624 0.4091 0.2886 -0.1359 -0.0355 0.1518  28  LYS A CG  
215  C CD  . LYS A 28  ? 0.4963 0.5575 0.3855 -0.1506 -0.0355 0.1728  28  LYS A CD  
216  C CE  . LYS A 28  ? 0.4856 0.5613 0.3666 -0.1648 -0.0202 0.1709  28  LYS A CE  
217  N NZ  . LYS A 28  ? 0.5924 0.6792 0.4493 -0.1727 -0.0220 0.1850  28  LYS A NZ  
218  N N   . GLY A 29  ? 0.3329 0.3662 0.3349 -0.1114 -0.0258 0.0954  29  GLY A N   
219  C CA  . GLY A 29  ? 0.3350 0.3683 0.3609 -0.1132 -0.0190 0.0805  29  GLY A CA  
220  C C   . GLY A 29  ? 0.3132 0.3588 0.3390 -0.0972 -0.0137 0.0501  29  GLY A C   
221  O O   . GLY A 29  ? 0.3197 0.3650 0.3452 -0.0820 -0.0192 0.0411  29  GLY A O   
222  N N   . ASP A 30  ? 0.2633 0.3216 0.2885 -0.1013 -0.0031 0.0351  30  ASP A N   
223  C CA  . ASP A 30  ? 0.2489 0.3183 0.2726 -0.0870 -0.0001 0.0090  30  ASP A CA  
224  C C   . ASP A 30  ? 0.2923 0.3773 0.2858 -0.0867 0.0065  0.0049  30  ASP A C   
225  O O   . ASP A 30  ? 0.3228 0.4165 0.3150 -0.0776 0.0086  -0.0140 30  ASP A O   
226  C CB  . ASP A 30  ? 0.2562 0.3300 0.3033 -0.0888 0.0041  -0.0089 30  ASP A CB  
227  C CG  . ASP A 30  ? 0.3132 0.3966 0.3579 -0.1089 0.0154  -0.0028 30  ASP A CG  
228  O OD1 . ASP A 30  ? 0.4385 0.5281 0.4585 -0.1216 0.0205  0.0146  30  ASP A OD1 
229  O OD2 . ASP A 30  ? 0.3163 0.4038 0.3852 -0.1125 0.0194  -0.0171 30  ASP A OD2 
230  N N   . ARG A 31  ? 0.3133 0.4022 0.2849 -0.0957 0.0079  0.0213  31  ARG A N   
231  C CA  . ARG A 31  ? 0.3195 0.4255 0.2695 -0.0969 0.0137  0.0144  31  ARG A CA  
232  C C   . ARG A 31  ? 0.2786 0.3827 0.2142 -0.0896 0.0080  0.0220  31  ARG A C   
233  O O   . ARG A 31  ? 0.3471 0.4410 0.2819 -0.0905 0.0008  0.0384  31  ARG A O   
234  C CB  . ARG A 31  ? 0.3055 0.4281 0.2426 -0.1160 0.0229  0.0203  31  ARG A CB  
235  C CG  . ARG A 31  ? 0.2964 0.4263 0.2497 -0.1255 0.0316  0.0099  31  ARG A CG  
236  C CD  . ARG A 31  ? 0.2674 0.4096 0.2297 -0.1166 0.0349  -0.0181 31  ARG A CD  
237  N NE  . ARG A 31  ? 0.3199 0.4720 0.3014 -0.1267 0.0433  -0.0300 31  ARG A NE  
238  C CZ  . ARG A 31  ? 0.3075 0.4763 0.2997 -0.1251 0.0479  -0.0546 31  ARG A CZ  
239  N NH1 . ARG A 31  ? 0.2885 0.4640 0.2747 -0.1136 0.0438  -0.0686 31  ARG A NH1 
240  N NH2 . ARG A 31  ? 0.2287 0.4072 0.2422 -0.1354 0.0559  -0.0657 31  ARG A NH2 
241  N N   . ILE A 32  ? 0.3274 0.4411 0.2560 -0.0824 0.0101  0.0093  32  ILE A N   
242  C CA  . ILE A 32  ? 0.3167 0.4339 0.2337 -0.0789 0.0070  0.0138  32  ILE A CA  
243  C C   . ILE A 32  ? 0.3118 0.4442 0.2129 -0.0927 0.0098  0.0202  32  ILE A C   
244  O O   . ILE A 32  ? 0.3598 0.5096 0.2578 -0.0997 0.0169  0.0082  32  ILE A O   
245  C CB  . ILE A 32  ? 0.3283 0.4499 0.2475 -0.0686 0.0081  -0.0004 32  ILE A CB  
246  C CG1 . ILE A 32  ? 0.2594 0.3706 0.1885 -0.0565 0.0060  -0.0061 32  ILE A CG1 
247  C CG2 . ILE A 32  ? 0.3503 0.4746 0.2643 -0.0656 0.0052  0.0039  32  ILE A CG2 
248  C CD1 . ILE A 32  ? 0.2912 0.4050 0.2206 -0.0476 0.0059  -0.0161 32  ILE A CD1 
249  N N   A MET A 33  ? 0.3282 0.4568 0.2198 -0.0965 0.0034  0.0376  33  MET A N   
250  N N   B MET A 33  ? 0.3242 0.4526 0.2160 -0.0962 0.0034  0.0375  33  MET A N   
251  C CA  A MET A 33  ? 0.3431 0.4864 0.2183 -0.1091 0.0045  0.0454  33  MET A CA  
252  C CA  B MET A 33  ? 0.3491 0.4912 0.2240 -0.1091 0.0039  0.0468  33  MET A CA  
253  C C   A MET A 33  ? 0.3487 0.5020 0.2219 -0.1035 0.0004  0.0388  33  MET A C   
254  C C   B MET A 33  ? 0.3504 0.5034 0.2235 -0.1035 0.0003  0.0392  33  MET A C   
255  O O   A MET A 33  ? 0.3443 0.5141 0.2117 -0.1101 0.0025  0.0352  33  MET A O   
256  O O   B MET A 33  ? 0.3431 0.5127 0.2106 -0.1102 0.0026  0.0352  33  MET A O   
257  C CB  A MET A 33  ? 0.3578 0.4889 0.2262 -0.1179 -0.0023 0.0715  33  MET A CB  
258  C CB  B MET A 33  ? 0.3586 0.4871 0.2275 -0.1164 -0.0041 0.0733  33  MET A CB  
259  C CG  A MET A 33  ? 0.2918 0.4078 0.1633 -0.1091 -0.0162 0.0846  33  MET A CG  
260  C CG  B MET A 33  ? 0.3506 0.4890 0.2072 -0.1266 -0.0048 0.0826  33  MET A CG  
261  S SD  A MET A 33  ? 0.6117 0.7258 0.4687 -0.1189 -0.0269 0.1099  33  MET A SD  
262  S SD  B MET A 33  ? 0.4453 0.5634 0.2973 -0.1314 -0.0199 0.1160  33  MET A SD  
263  C CE  A MET A 33  ? 0.4910 0.6329 0.3354 -0.1189 -0.0208 0.0919  33  MET A CE  
264  C CE  B MET A 33  ? 0.4930 0.6103 0.3437 -0.1176 -0.0328 0.1139  33  MET A CE  
265  N N   . ALA A 34  ? 0.3504 0.4974 0.2290 -0.0927 -0.0048 0.0367  34  ALA A N   
266  C CA  . ALA A 34  ? 0.3367 0.4947 0.2163 -0.0890 -0.0083 0.0302  34  ALA A CA  
267  C C   . ALA A 34  ? 0.3496 0.5035 0.2399 -0.0785 -0.0095 0.0223  34  ALA A C   
268  O O   . ALA A 34  ? 0.3398 0.4785 0.2370 -0.0719 -0.0111 0.0278  34  ALA A O   
269  C CB  . ALA A 34  ? 0.2733 0.4299 0.1424 -0.0914 -0.0182 0.0461  34  ALA A CB  
270  N N   . ILE A 35  ? 0.3349 0.5025 0.2323 -0.0768 -0.0085 0.0083  35  ILE A N   
271  C CA  . ILE A 35  ? 0.3193 0.4845 0.2310 -0.0686 -0.0100 0.0020  35  ILE A CA  
272  C C   . ILE A 35  ? 0.3366 0.5194 0.2528 -0.0698 -0.0151 -0.0066 35  ILE A C   
273  O O   . ILE A 35  ? 0.3567 0.5578 0.2728 -0.0746 -0.0131 -0.0197 35  ILE A O   
274  C CB  . ILE A 35  ? 0.3607 0.5224 0.2855 -0.0646 -0.0042 -0.0095 35  ILE A CB  
275  C CG1 . ILE A 35  ? 0.3040 0.4525 0.2241 -0.0629 -0.0004 -0.0048 35  ILE A CG1 
276  C CG2 . ILE A 35  ? 0.2973 0.4516 0.2414 -0.0567 -0.0051 -0.0107 35  ILE A CG2 
277  C CD1 . ILE A 35  ? 0.2351 0.3825 0.1649 -0.0593 0.0025  -0.0163 35  ILE A CD1 
278  N N   . ALA A 36  ? 0.2754 0.4534 0.2018 -0.0644 -0.0210 -0.0019 36  ALA A N   
279  C CA  . ALA A 36  ? 0.3529 0.5486 0.2868 -0.0647 -0.0276 -0.0119 36  ALA A CA  
280  C C   . ALA A 36  ? 0.2636 0.4501 0.2217 -0.0570 -0.0304 -0.0107 36  ALA A C   
281  O O   . ALA A 36  ? 0.2565 0.4262 0.2182 -0.0526 -0.0283 0.0002  36  ALA A O   
282  C CB  . ALA A 36  ? 0.2554 0.4635 0.1659 -0.0702 -0.0358 -0.0046 36  ALA A CB  
283  N N   . PRO A 37  ? 0.3288 0.5286 0.3073 -0.0556 -0.0343 -0.0241 37  PRO A N   
284  C CA  . PRO A 37  ? 0.2891 0.4830 0.2940 -0.0500 -0.0361 -0.0236 37  PRO A CA  
285  C C   . PRO A 37  ? 0.3558 0.5413 0.3546 -0.0465 -0.0423 -0.0107 37  PRO A C   
286  O O   . PRO A 37  ? 0.3329 0.5088 0.3506 -0.0421 -0.0384 -0.0074 37  PRO A O   
287  C CB  . PRO A 37  ? 0.2787 0.4938 0.3028 -0.0503 -0.0434 -0.0418 37  PRO A CB  
288  C CG  . PRO A 37  ? 0.2688 0.4969 0.2880 -0.0549 -0.0404 -0.0555 37  PRO A CG  
289  C CD  . PRO A 37  ? 0.3087 0.5321 0.2920 -0.0593 -0.0366 -0.0436 37  PRO A CD  
290  N N   . ALA A 38  ? 0.2866 0.4767 0.2616 -0.0489 -0.0522 -0.0034 38  ALA A N   
291  C CA  . ALA A 38  ? 0.2883 0.4650 0.2579 -0.0457 -0.0597 0.0114  38  ALA A CA  
292  C C   . ALA A 38  ? 0.3372 0.5135 0.2742 -0.0523 -0.0657 0.0248  38  ALA A C   
293  O O   . ALA A 38  ? 0.3676 0.5614 0.2849 -0.0590 -0.0667 0.0209  38  ALA A O   
294  C CB  . ALA A 38  ? 0.2817 0.4635 0.2706 -0.0399 -0.0728 0.0085  38  ALA A CB  
295  N N   . LEU A 39  ? 0.2947 0.4530 0.2288 -0.0509 -0.0693 0.0398  39  LEU A N   
296  C CA  . LEU A 39  ? 0.3281 0.4813 0.2362 -0.0584 -0.0751 0.0573  39  LEU A CA  
297  C C   . LEU A 39  ? 0.3365 0.4773 0.2516 -0.0540 -0.0935 0.0721  39  LEU A C   
298  O O   . LEU A 39  ? 0.3666 0.4901 0.3038 -0.0474 -0.0956 0.0746  39  LEU A O   
299  C CB  . LEU A 39  ? 0.2564 0.3965 0.1610 -0.0616 -0.0629 0.0611  39  LEU A CB  
300  C CG  . LEU A 39  ? 0.3496 0.5010 0.2467 -0.0663 -0.0478 0.0479  39  LEU A CG  
301  C CD1 . LEU A 39  ? 0.3284 0.4656 0.2295 -0.0659 -0.0382 0.0489  39  LEU A CD1 
302  C CD2 . LEU A 39  ? 0.2860 0.4531 0.1626 -0.0757 -0.0453 0.0468  39  LEU A CD2 
303  N N   . ASP A 40  ? 0.3477 0.4990 0.2453 -0.0570 -0.1085 0.0805  40  ASP A N   
304  C CA  . ASP A 40  ? 0.3611 0.4990 0.2667 -0.0520 -0.1295 0.0957  40  ASP A CA  
305  C C   . ASP A 40  ? 0.4165 0.5353 0.3053 -0.0593 -0.1307 0.1182  40  ASP A C   
306  O O   . ASP A 40  ? 0.4800 0.6000 0.3463 -0.0645 -0.1340 0.1291  40  ASP A O   
307  C CB  . ASP A 40  ? 0.3840 0.5353 0.2844 -0.0477 -0.1411 0.0895  40  ASP A CB  
308  C CG  . ASP A 40  ? 0.4155 0.5521 0.3270 -0.0404 -0.1644 0.1031  40  ASP A CG  
309  O OD1 . ASP A 40  ? 0.5090 0.6250 0.4418 -0.0372 -0.1725 0.1139  40  ASP A OD1 
310  O OD2 . ASP A 40  ? 0.4176 0.5638 0.3197 -0.0366 -0.1757 0.1007  40  ASP A OD2 
311  N N   . VAL A 41  ? 0.4543 0.5571 0.3569 -0.0601 -0.1286 0.1252  41  VAL A N   
312  C CA  . VAL A 41  ? 0.4775 0.5621 0.3722 -0.0684 -0.1286 0.1454  41  VAL A CA  
313  C C   . VAL A 41  ? 0.5434 0.6031 0.4746 -0.0602 -0.1424 0.1520  41  VAL A C   
314  O O   . VAL A 41  ? 0.6072 0.6652 0.5697 -0.0487 -0.1376 0.1316  41  VAL A O   
315  C CB  . VAL A 41  ? 0.4341 0.5245 0.3149 -0.0779 -0.1067 0.1400  41  VAL A CB  
316  C CG1 . VAL A 41  ? 0.4614 0.5760 0.3202 -0.0828 -0.0913 0.1247  41  VAL A CG1 
317  C CG2 . VAL A 41  ? 0.3868 0.4721 0.2938 -0.0689 -0.0954 0.1207  41  VAL A CG2 
318  N N   . ALA A 42  ? 0.5419 0.5822 0.4735 -0.0660 -0.1560 0.1769  42  ALA A N   
319  C CA  . ALA A 42  ? 0.5334 0.5486 0.5068 -0.0588 -0.1678 0.1802  42  ALA A CA  
320  C C   . ALA A 42  ? 0.5060 0.5168 0.4899 -0.0613 -0.1483 0.1689  42  ALA A C   
321  O O   . ALA A 42  ? 0.5622 0.5774 0.5198 -0.0744 -0.1350 0.1772  42  ALA A O   
322  C CB  . ALA A 42  ? 0.5047 0.4982 0.4813 -0.0643 -0.1870 0.2080  42  ALA A CB  
323  N N   . ALA A 43  ? 0.4024 0.4081 0.4254 -0.0488 -0.1464 0.1475  43  ALA A N   
324  C CA  . ALA A 43  ? 0.3475 0.3508 0.3838 -0.0484 -0.1310 0.1335  43  ALA A CA  
325  C C   . ALA A 43  ? 0.3753 0.3593 0.4607 -0.0404 -0.1452 0.1301  43  ALA A C   
326  O O   . ALA A 43  ? 0.4856 0.4644 0.6020 -0.0298 -0.1619 0.1254  43  ALA A O   
327  C CB  . ALA A 43  ? 0.3714 0.3945 0.4050 -0.0407 -0.1118 0.1056  43  ALA A CB  
328  N N   . GLU A 44  ? 0.3791 0.3534 0.4765 -0.0451 -0.1397 0.1303  44  GLU A N   
329  C CA  . GLU A 44  ? 0.4375 0.3984 0.5882 -0.0355 -0.1506 0.1177  44  GLU A CA  
330  C C   . GLU A 44  ? 0.4294 0.4087 0.6031 -0.0194 -0.1435 0.0825  44  GLU A C   
331  O O   . GLU A 44  ? 0.4603 0.4355 0.6800 -0.0081 -0.1575 0.0689  44  GLU A O   
332  C CB  . GLU A 44  ? 0.4420 0.3944 0.6022 -0.0431 -0.1428 0.1182  44  GLU A CB  
333  C CG  . GLU A 44  ? 0.6644 0.6015 0.8039 -0.0617 -0.1462 0.1531  44  GLU A CG  
334  C CD  . GLU A 44  ? 0.7938 0.7025 0.9669 -0.0640 -0.1728 0.1784  44  GLU A CD  
335  O OE1 . GLU A 44  ? 0.8346 0.7350 1.0558 -0.0494 -0.1890 0.1633  44  GLU A OE1 
336  O OE2 . GLU A 44  ? 0.8831 0.7789 1.0359 -0.0807 -0.1779 0.2133  44  GLU A OE2 
337  N N   . GLN A 45  ? 0.3591 0.3600 0.5031 -0.0187 -0.1219 0.0674  45  GLN A N   
338  C CA  . GLN A 45  ? 0.3432 0.3647 0.5009 -0.0064 -0.1116 0.0377  45  GLN A CA  
339  C C   . GLN A 45  ? 0.3411 0.3801 0.4630 -0.0082 -0.0976 0.0368  45  GLN A C   
340  O O   . GLN A 45  ? 0.3097 0.3510 0.3945 -0.0174 -0.0871 0.0472  45  GLN A O   
341  C CB  . GLN A 45  ? 0.3244 0.3542 0.4893 -0.0030 -0.0989 0.0174  45  GLN A CB  
342  C CG  . GLN A 45  ? 0.4449 0.4581 0.6481 -0.0024 -0.1114 0.0162  45  GLN A CG  
343  C CD  . GLN A 45  ? 0.6306 0.6522 0.8849 0.0119  -0.1196 -0.0120 45  GLN A CD  
344  O OE1 . GLN A 45  ? 0.6400 0.6689 0.9124 0.0193  -0.1264 -0.0199 45  GLN A OE1 
345  N NE2 . GLN A 45  ? 0.8331 0.8572 1.1142 0.0162  -0.1189 -0.0309 45  GLN A NE2 
346  N N   . VAL A 46  ? 0.3623 0.4146 0.5004 0.0002  -0.0978 0.0226  46  VAL A N   
347  C CA  . VAL A 46  ? 0.3314 0.4003 0.4463 -0.0010 -0.0854 0.0197  46  VAL A CA  
348  C C   . VAL A 46  ? 0.3942 0.4843 0.5196 0.0062  -0.0695 -0.0042 46  VAL A C   
349  O O   . VAL A 46  ? 0.3477 0.4451 0.5084 0.0148  -0.0734 -0.0221 46  VAL A O   
350  C CB  . VAL A 46  ? 0.3426 0.4106 0.4669 0.0005  -0.0998 0.0266  46  VAL A CB  
351  C CG1 . VAL A 46  ? 0.2911 0.3765 0.3977 -0.0012 -0.0868 0.0216  46  VAL A CG1 
352  C CG2 . VAL A 46  ? 0.4005 0.4500 0.5081 -0.0074 -0.1165 0.0531  46  VAL A CG2 
353  N N   . ILE A 47  ? 0.3663 0.4677 0.4624 0.0023  -0.0521 -0.0046 47  ILE A N   
354  C CA  . ILE A 47  ? 0.3400 0.4630 0.4383 0.0064  -0.0358 -0.0211 47  ILE A CA  
355  C C   . ILE A 47  ? 0.3657 0.4974 0.4540 0.0024  -0.0283 -0.0165 47  ILE A C   
356  O O   . ILE A 47  ? 0.3410 0.4666 0.4037 -0.0044 -0.0256 -0.0038 47  ILE A O   
357  C CB  . ILE A 47  ? 0.4241 0.5515 0.4993 0.0057  -0.0231 -0.0246 47  ILE A CB  
358  C CG1 . ILE A 47  ? 0.3259 0.4494 0.4195 0.0111  -0.0300 -0.0356 47  ILE A CG1 
359  C CG2 . ILE A 47  ? 0.3225 0.4724 0.3901 0.0074  -0.0061 -0.0344 47  ILE A CG2 
360  C CD1 . ILE A 47  ? 0.4335 0.5590 0.5048 0.0105  -0.0216 -0.0383 47  ILE A CD1 
361  N N   . ASP A 48  ? 0.3154 0.4629 0.4289 0.0064  -0.0252 -0.0289 48  ASP A N   
362  C CA  . ASP A 48  ? 0.2831 0.4421 0.3940 0.0021  -0.0151 -0.0274 48  ASP A CA  
363  C C   . ASP A 48  ? 0.3496 0.5198 0.4384 -0.0013 0.0049  -0.0272 48  ASP A C   
364  O O   . ASP A 48  ? 0.3029 0.4916 0.3992 0.0015  0.0161  -0.0396 48  ASP A O   
365  C CB  . ASP A 48  ? 0.2183 0.3928 0.3672 0.0066  -0.0170 -0.0422 48  ASP A CB  
366  C CG  . ASP A 48  ? 0.3133 0.4986 0.4661 0.0012  -0.0079 -0.0405 48  ASP A CG  
367  O OD1 . ASP A 48  ? 0.3474 0.5275 0.4743 -0.0056 -0.0001 -0.0282 48  ASP A OD1 
368  O OD2 . ASP A 48  ? 0.4140 0.6128 0.6002 0.0037  -0.0095 -0.0529 48  ASP A OD2 
369  N N   . GLY A 49  ? 0.3382 0.4990 0.4001 -0.0074 0.0084  -0.0136 49  GLY A N   
370  C CA  . GLY A 49  ? 0.2876 0.4543 0.3279 -0.0102 0.0232  -0.0099 49  GLY A CA  
371  C C   . GLY A 49  ? 0.3020 0.4796 0.3468 -0.0158 0.0358  -0.0057 49  GLY A C   
372  O O   . GLY A 49  ? 0.3013 0.4789 0.3278 -0.0197 0.0451  0.0033  49  GLY A O   
373  N N   . GLN A 50  ? 0.3027 0.4893 0.3750 -0.0165 0.0355  -0.0118 50  GLN A N   
374  C CA  . GLN A 50  ? 0.2325 0.4288 0.3151 -0.0234 0.0477  -0.0075 50  GLN A CA  
375  C C   . GLN A 50  ? 0.3192 0.5295 0.3873 -0.0270 0.0660  -0.0033 50  GLN A C   
376  O O   . GLN A 50  ? 0.2746 0.5008 0.3404 -0.0230 0.0720  -0.0135 50  GLN A O   
377  C CB  . GLN A 50  ? 0.1951 0.4045 0.3151 -0.0226 0.0459  -0.0197 50  GLN A CB  
378  C CG  . GLN A 50  ? 0.3248 0.5556 0.4637 -0.0181 0.0524  -0.0364 50  GLN A CG  
379  C CD  . GLN A 50  ? 0.3561 0.6005 0.5375 -0.0168 0.0491  -0.0510 50  GLN A CD  
380  O OE1 . GLN A 50  ? 0.3119 0.5775 0.5127 -0.0225 0.0652  -0.0566 50  GLN A OE1 
381  N NE2 . GLN A 50  ? 0.3096 0.5424 0.5066 -0.0096 0.0277  -0.0564 50  GLN A NE2 
382  N N   . GLY A 51  ? 0.3393 0.5453 0.3991 -0.0346 0.0739  0.0117  51  GLY A N   
383  C CA  . GLY A 51  ? 0.3890 0.6078 0.4322 -0.0396 0.0905  0.0210  51  GLY A CA  
384  C C   . GLY A 51  ? 0.3776 0.5920 0.3850 -0.0352 0.0890  0.0259  51  GLY A C   
385  O O   . GLY A 51  ? 0.3910 0.6184 0.3794 -0.0385 0.1011  0.0344  51  GLY A O   
386  N N   . ARG A 52  ? 0.2691 0.4672 0.2667 -0.0284 0.0744  0.0214  52  ARG A N   
387  C CA  . ARG A 52  ? 0.3621 0.5559 0.3309 -0.0234 0.0712  0.0229  52  ARG A CA  
388  C C   . ARG A 52  ? 0.2731 0.4436 0.2311 -0.0245 0.0611  0.0336  52  ARG A C   
389  O O   . ARG A 52  ? 0.3448 0.5036 0.3176 -0.0277 0.0548  0.0355  52  ARG A O   
390  C CB  . ARG A 52  ? 0.3381 0.5354 0.3098 -0.0147 0.0634  0.0051  52  ARG A CB  
391  C CG  . ARG A 52  ? 0.4288 0.6497 0.4216 -0.0118 0.0697  -0.0119 52  ARG A CG  
392  C CD  . ARG A 52  ? 0.4123 0.6597 0.3905 -0.0139 0.0860  -0.0125 52  ARG A CD  
393  N NE  . ARG A 52  ? 0.6159 0.8921 0.6165 -0.0108 0.0931  -0.0344 52  ARG A NE  
394  C CZ  . ARG A 52  ? 0.6394 0.9332 0.6634 -0.0163 0.1040  -0.0386 52  ARG A CZ  
395  N NH1 . ARG A 52  ? 0.5411 0.8250 0.5717 -0.0253 0.1083  -0.0220 52  ARG A NH1 
396  N NH2 . ARG A 52  ? 0.5621 0.8849 0.6079 -0.0126 0.1101  -0.0625 52  ARG A NH2 
397  N N   . VAL A 53  ? 0.2885 0.4965 0.3741 -0.0661 -0.0319 0.1136  53  VAL A N   
398  C CA  . VAL A 53  ? 0.2561 0.4489 0.3223 -0.0733 -0.0321 0.0954  53  VAL A CA  
399  C C   . VAL A 53  ? 0.2859 0.4717 0.3307 -0.0684 -0.0306 0.0913  53  VAL A C   
400  O O   . VAL A 53  ? 0.3486 0.5298 0.3918 -0.0552 -0.0236 0.0966  53  VAL A O   
401  C CB  . VAL A 53  ? 0.2239 0.4017 0.2935 -0.0688 -0.0231 0.0881  53  VAL A CB  
402  C CG1 . VAL A 53  ? 0.2272 0.3880 0.2763 -0.0712 -0.0204 0.0715  53  VAL A CG1 
403  C CG2 . VAL A 53  ? 0.2277 0.4107 0.3182 -0.0777 -0.0261 0.0892  53  VAL A CG2 
404  N N   . LEU A 54  ? 0.2477 0.4329 0.2761 -0.0792 -0.0369 0.0816  54  LEU A N   
405  C CA  . LEU A 54  ? 0.2382 0.4145 0.2462 -0.0758 -0.0344 0.0755  54  LEU A CA  
406  C C   . LEU A 54  ? 0.2892 0.4473 0.2858 -0.0778 -0.0286 0.0587  54  LEU A C   
407  O O   . LEU A 54  ? 0.2956 0.4516 0.2897 -0.0892 -0.0314 0.0478  54  LEU A O   
408  C CB  . LEU A 54  ? 0.2722 0.4613 0.2690 -0.0854 -0.0438 0.0775  54  LEU A CB  
409  C CG  . LEU A 54  ? 0.2769 0.4598 0.2569 -0.0802 -0.0410 0.0763  54  LEU A CG  
410  C CD1 . LEU A 54  ? 0.2378 0.4204 0.2282 -0.0655 -0.0360 0.0895  54  LEU A CD1 
411  C CD2 . LEU A 54  ? 0.2611 0.4578 0.2276 -0.0913 -0.0502 0.0774  54  LEU A CD2 
412  N N   . ALA A 55  ? 0.2349 0.3801 0.2261 -0.0668 -0.0204 0.0568  55  ALA A N   
413  C CA  . ALA A 55  ? 0.2317 0.3605 0.2153 -0.0663 -0.0140 0.0438  55  ALA A CA  
414  C C   . ALA A 55  ? 0.2746 0.3954 0.2419 -0.0615 -0.0113 0.0403  55  ALA A C   
415  O O   . ALA A 55  ? 0.3229 0.4483 0.2881 -0.0554 -0.0124 0.0490  55  ALA A O   
416  C CB  . ALA A 55  ? 0.2320 0.3545 0.2287 -0.0574 -0.0069 0.0468  55  ALA A CB  
417  N N   . PRO A 56  ? 0.3032 0.4117 0.2611 -0.0636 -0.0070 0.0284  56  PRO A N   
418  C CA  . PRO A 56  ? 0.2705 0.3709 0.2165 -0.0578 -0.0035 0.0264  56  PRO A CA  
419  C C   . PRO A 56  ? 0.3034 0.3992 0.2553 -0.0452 0.0007  0.0333  56  PRO A C   
420  O O   . PRO A 56  ? 0.3298 0.4258 0.2928 -0.0406 0.0033  0.0368  56  PRO A O   
421  C CB  . PRO A 56  ? 0.2573 0.3458 0.1979 -0.0619 0.0015  0.0132  56  PRO A CB  
422  C CG  . PRO A 56  ? 0.2817 0.3719 0.2294 -0.0713 0.0002  0.0067  56  PRO A CG  
423  C CD  . PRO A 56  ? 0.2477 0.3479 0.2100 -0.0695 -0.0036 0.0175  56  PRO A CD  
424  N N   . GLY A 57  ? 0.2796 0.3718 0.2238 -0.0397 0.0014  0.0353  57  GLY A N   
425  C CA  . GLY A 57  ? 0.2800 0.3656 0.2267 -0.0286 0.0057  0.0385  57  GLY A CA  
426  C C   . GLY A 57  ? 0.2967 0.3732 0.2447 -0.0264 0.0106  0.0322  57  GLY A C   
427  O O   . GLY A 57  ? 0.3236 0.3946 0.2682 -0.0318 0.0120  0.0243  57  GLY A O   
428  N N   . PHE A 58  ? 0.3063 0.3824 0.2601 -0.0183 0.0138  0.0364  58  PHE A N   
429  C CA  . PHE A 58  ? 0.2970 0.3675 0.2538 -0.0160 0.0180  0.0333  58  PHE A CA  
430  C C   . PHE A 58  ? 0.2429 0.3040 0.1909 -0.0134 0.0194  0.0281  58  PHE A C   
431  O O   . PHE A 58  ? 0.3227 0.3809 0.2635 -0.0097 0.0182  0.0285  58  PHE A O   
432  C CB  . PHE A 58  ? 0.2724 0.3481 0.2367 -0.0083 0.0210  0.0407  58  PHE A CB  
433  C CG  . PHE A 58  ? 0.2927 0.3789 0.2683 -0.0104 0.0197  0.0476  58  PHE A CG  
434  C CD1 . PHE A 58  ? 0.2922 0.3818 0.2732 -0.0206 0.0160  0.0452  58  PHE A CD1 
435  C CD2 . PHE A 58  ? 0.2618 0.3552 0.2429 -0.0026 0.0221  0.0563  58  PHE A CD2 
436  C CE1 . PHE A 58  ? 0.2855 0.3860 0.2785 -0.0237 0.0135  0.0520  58  PHE A CE1 
437  C CE2 . PHE A 58  ? 0.2494 0.3541 0.2437 -0.0046 0.0207  0.0643  58  PHE A CE2 
438  C CZ  . PHE A 58  ? 0.2974 0.4059 0.2984 -0.0155 0.0158  0.0626  58  PHE A CZ  
439  N N   . ILE A 59  ? 0.2894 0.3456 0.2401 -0.0157 0.0220  0.0238  59  ILE A N   
440  C CA  . ILE A 59  ? 0.3062 0.3548 0.2514 -0.0144 0.0231  0.0197  59  ILE A CA  
441  C C   . ILE A 59  ? 0.3045 0.3531 0.2539 -0.0085 0.0254  0.0228  59  ILE A C   
442  O O   . ILE A 59  ? 0.2936 0.3440 0.2534 -0.0096 0.0283  0.0245  59  ILE A O   
443  C CB  . ILE A 59  ? 0.3712 0.4154 0.3173 -0.0216 0.0248  0.0129  59  ILE A CB  
444  C CG1 . ILE A 59  ? 0.3047 0.3515 0.2441 -0.0282 0.0222  0.0101  59  ILE A CG1 
445  C CG2 . ILE A 59  ? 0.3936 0.4315 0.3369 -0.0199 0.0261  0.0105  59  ILE A CG2 
446  C CD1 . ILE A 59  ? 0.2405 0.2838 0.1791 -0.0356 0.0251  0.0021  59  ILE A CD1 
447  N N   . ASP A 60  ? 0.2733 0.3205 0.2152 -0.0026 0.0242  0.0238  60  ASP A N   
448  C CA  . ASP A 60  ? 0.2539 0.3033 0.1966 0.0026  0.0256  0.0270  60  ASP A CA  
449  C C   . ASP A 60  ? 0.2902 0.3352 0.2344 0.0004  0.0253  0.0244  60  ASP A C   
450  O O   . ASP A 60  ? 0.2902 0.3306 0.2269 0.0009  0.0225  0.0211  60  ASP A O   
451  C CB  . ASP A 60  ? 0.2637 0.3140 0.1964 0.0095  0.0246  0.0277  60  ASP A CB  
452  C CG  . ASP A 60  ? 0.3537 0.4101 0.2853 0.0147  0.0263  0.0321  60  ASP A CG  
453  O OD1 . ASP A 60  ? 0.3311 0.3911 0.2717 0.0130  0.0276  0.0359  60  ASP A OD1 
454  O OD2 . ASP A 60  ? 0.3734 0.4315 0.2957 0.0206  0.0268  0.0320  60  ASP A OD2 
455  N N   . VAL A 61  ? 0.2752 0.3214 0.2313 -0.0022 0.0283  0.0263  61  VAL A N   
456  C CA  . VAL A 61  ? 0.2936 0.3361 0.2550 -0.0044 0.0292  0.0248  61  VAL A CA  
457  C C   . VAL A 61  ? 0.3487 0.3951 0.3088 -0.0002 0.0270  0.0294  61  VAL A C   
458  O O   . VAL A 61  ? 0.3022 0.3466 0.2661 -0.0017 0.0262  0.0291  61  VAL A O   
459  C CB  . VAL A 61  ? 0.2701 0.3116 0.2476 -0.0082 0.0343  0.0250  61  VAL A CB  
460  C CG1 . VAL A 61  ? 0.3043 0.3424 0.2807 -0.0138 0.0357  0.0187  61  VAL A CG1 
461  C CG2 . VAL A 61  ? 0.2404 0.2889 0.2303 -0.0050 0.0367  0.0336  61  VAL A CG2 
462  N N   . HIS A 62  ? 0.3304 0.3837 0.2854 0.0049  0.0259  0.0341  62  HIS A N   
463  C CA  . HIS A 62  ? 0.2878 0.3468 0.2388 0.0081  0.0230  0.0382  62  HIS A CA  
464  C C   . HIS A 62  ? 0.3387 0.3982 0.2719 0.0123  0.0198  0.0349  62  HIS A C   
465  O O   . HIS A 62  ? 0.3338 0.4000 0.2625 0.0169  0.0218  0.0385  62  HIS A O   
466  C CB  . HIS A 62  ? 0.3307 0.3998 0.2939 0.0103  0.0259  0.0485  62  HIS A CB  
467  C CG  . HIS A 62  ? 0.3899 0.4665 0.3534 0.0116  0.0225  0.0544  62  HIS A CG  
468  N ND1 . HIS A 62  ? 0.3504 0.4335 0.2976 0.0150  0.0182  0.0548  62  HIS A ND1 
469  C CD2 . HIS A 62  ? 0.3455 0.4248 0.3237 0.0096  0.0226  0.0601  62  HIS A CD2 
470  C CE1 . HIS A 62  ? 0.3248 0.4158 0.2758 0.0144  0.0147  0.0611  62  HIS A CE1 
471  N NE2 . HIS A 62  ? 0.4103 0.4995 0.3814 0.0115  0.0173  0.0654  62  HIS A NE2 
472  N N   . THR A 63  ? 0.3513 0.4036 0.2755 0.0108  0.0156  0.0279  63  THR A N   
473  C CA  . THR A 63  ? 0.3174 0.3675 0.2259 0.0144  0.0131  0.0226  63  THR A CA  
474  C C   . THR A 63  ? 0.3520 0.4008 0.2539 0.0127  0.0070  0.0192  63  THR A C   
475  O O   . THR A 63  ? 0.3090 0.3572 0.2194 0.0084  0.0045  0.0207  63  THR A O   
476  C CB  . THR A 63  ? 0.3766 0.4173 0.2816 0.0142  0.0136  0.0166  63  THR A CB  
477  O OG1 . THR A 63  ? 0.3604 0.3928 0.2662 0.0098  0.0099  0.0120  63  THR A OG1 
478  C CG2 . THR A 63  ? 0.3218 0.3637 0.2360 0.0128  0.0177  0.0199  63  THR A CG2 
479  N N   . HIS A 64  ? 0.3213 0.3697 0.2081 0.0160  0.0049  0.0142  64  HIS A N   
480  C CA  . HIS A 64  ? 0.3857 0.4306 0.2637 0.0136  -0.0018 0.0077  64  HIS A CA  
481  C C   . HIS A 64  ? 0.3693 0.4016 0.2385 0.0150  -0.0020 -0.0025 64  HIS A C   
482  O O   . HIS A 64  ? 0.3886 0.4182 0.2443 0.0163  -0.0048 -0.0102 64  HIS A O   
483  C CB  . HIS A 64  ? 0.2698 0.3269 0.1372 0.0154  -0.0046 0.0104  64  HIS A CB  
484  C CG  . HIS A 64  ? 0.3426 0.4123 0.2227 0.0140  -0.0047 0.0225  64  HIS A CG  
485  N ND1 . HIS A 64  ? 0.3475 0.4178 0.2403 0.0087  -0.0089 0.0261  64  HIS A ND1 
486  C CD2 . HIS A 64  ? 0.3823 0.4640 0.2678 0.0173  -0.0002 0.0329  64  HIS A CD2 
487  C CE1 . HIS A 64  ? 0.3628 0.4447 0.2682 0.0092  -0.0069 0.0379  64  HIS A CE1 
488  N NE2 . HIS A 64  ? 0.4192 0.5081 0.3207 0.0141  -0.0019 0.0424  64  HIS A NE2 
489  N N   . ASP A 65  ? 0.3648 0.3895 0.2422 0.0145  0.0011  -0.0027 65  ASP A N   
490  C CA  . ASP A 65  ? 0.3523 0.3658 0.2262 0.0164  0.0021  -0.0096 65  ASP A CA  
491  C C   . ASP A 65  ? 0.3707 0.3740 0.2489 0.0113  -0.0031 -0.0144 65  ASP A C   
492  O O   . ASP A 65  ? 0.3929 0.3864 0.2727 0.0123  -0.0022 -0.0183 65  ASP A O   
493  C CB  . ASP A 65  ? 0.3407 0.3543 0.2223 0.0185  0.0076  -0.0049 65  ASP A CB  
494  C CG  . ASP A 65  ? 0.4138 0.4372 0.2937 0.0236  0.0129  0.0004  65  ASP A CG  
495  O OD1 . ASP A 65  ? 0.3684 0.3957 0.2377 0.0280  0.0141  -0.0017 65  ASP A OD1 
496  O OD2 . ASP A 65  ? 0.3689 0.3968 0.2580 0.0227  0.0158  0.0066  65  ASP A OD2 
497  N N   . ASP A 66  ? 0.3570 0.3633 0.2393 0.0061  -0.0082 -0.0128 66  ASP A N   
498  C CA  . ASP A 66  ? 0.3894 0.3882 0.2792 0.0005  -0.0130 -0.0150 66  ASP A CA  
499  C C   . ASP A 66  ? 0.4035 0.3895 0.2898 0.0011  -0.0150 -0.0237 66  ASP A C   
500  O O   . ASP A 66  ? 0.3735 0.3518 0.2689 -0.0005 -0.0141 -0.0229 66  ASP A O   
501  C CB  . ASP A 66  ? 0.3560 0.3610 0.2473 -0.0040 -0.0196 -0.0137 66  ASP A CB  
502  C CG  . ASP A 66  ? 0.3769 0.3937 0.2761 -0.0043 -0.0171 -0.0041 66  ASP A CG  
503  O OD1 . ASP A 66  ? 0.3598 0.3835 0.2552 -0.0001 -0.0126 -0.0006 66  ASP A OD1 
504  O OD2 . ASP A 66  ? 0.3094 0.3287 0.2206 -0.0087 -0.0191 0.0003  66  ASP A OD2 
505  N N   . ILE A 67  ? 0.3893 0.3732 0.2627 0.0032  -0.0172 -0.0319 67  ILE A N   
506  C CA  . ILE A 67  ? 0.4499 0.4198 0.3205 0.0030  -0.0192 -0.0424 67  ILE A CA  
507  C C   . ILE A 67  ? 0.3875 0.3517 0.2531 0.0107  -0.0116 -0.0460 67  ILE A C   
508  O O   . ILE A 67  ? 0.3955 0.3470 0.2673 0.0119  -0.0100 -0.0504 67  ILE A O   
509  C CB  . ILE A 67  ? 0.4807 0.4507 0.3398 -0.0007 -0.0270 -0.0515 67  ILE A CB  
510  C CG1 . ILE A 67  ? 0.4708 0.4418 0.3419 -0.0091 -0.0352 -0.0482 67  ILE A CG1 
511  C CG2 . ILE A 67  ? 0.4267 0.3824 0.2771 0.0012  -0.0268 -0.0657 67  ILE A CG2 
512  C CD1 . ILE A 67  ? 0.5556 0.5310 0.4177 -0.0144 -0.0446 -0.0542 67  ILE A CD1 
513  N N   . ASN A 68  ? 0.4647 0.4388 0.3219 0.0161  -0.0065 -0.0426 68  ASN A N   
514  C CA  . ASN A 68  ? 0.4707 0.4412 0.3235 0.0240  0.0014  -0.0455 68  ASN A CA  
515  C C   . ASN A 68  ? 0.4344 0.4018 0.3023 0.0259  0.0060  -0.0380 68  ASN A C   
516  O O   . ASN A 68  ? 0.4490 0.4083 0.3197 0.0311  0.0110  -0.0410 68  ASN A O   
517  C CB  . ASN A 68  ? 0.3855 0.3696 0.2276 0.0290  0.0058  -0.0417 68  ASN A CB  
518  C CG  . ASN A 68  ? 0.5314 0.5185 0.3547 0.0293  0.0030  -0.0506 68  ASN A CG  
519  O OD1 . ASN A 68  ? 0.5274 0.5193 0.3471 0.0232  -0.0047 -0.0510 68  ASN A OD1 
520  N ND2 . ASN A 68  ? 0.4973 0.4825 0.3085 0.0363  0.0096  -0.0575 68  ASN A ND2 
521  N N   . VAL A 69  ? 0.3647 0.3388 0.2425 0.0218  0.0045  -0.0283 69  VAL A N   
522  C CA  . VAL A 69  ? 0.4352 0.4083 0.3255 0.0224  0.0077  -0.0210 69  VAL A CA  
523  C C   . VAL A 69  ? 0.4589 0.4189 0.3583 0.0207  0.0058  -0.0239 69  VAL A C   
524  O O   . VAL A 69  ? 0.4690 0.4259 0.3779 0.0236  0.0092  -0.0194 69  VAL A O   
525  C CB  . VAL A 69  ? 0.3779 0.3610 0.2742 0.0175  0.0067  -0.0120 69  VAL A CB  
526  C CG1 . VAL A 69  ? 0.3508 0.3308 0.2520 0.0105  0.0014  -0.0123 69  VAL A CG1 
527  C CG2 . VAL A 69  ? 0.4566 0.4430 0.3616 0.0186  0.0100  -0.0041 69  VAL A CG2 
528  N N   . ILE A 70  ? 0.4488 0.4017 0.3474 0.0158  0.0001  -0.0303 70  ILE A N   
529  C CA  . ILE A 70  ? 0.3862 0.3257 0.2954 0.0140  -0.0018 -0.0335 70  ILE A CA  
530  C C   . ILE A 70  ? 0.4987 0.4258 0.4042 0.0198  0.0017  -0.0440 70  ILE A C   
531  O O   . ILE A 70  ? 0.5310 0.4482 0.4491 0.0223  0.0047  -0.0432 70  ILE A O   
532  C CB  . ILE A 70  ? 0.4329 0.3697 0.3448 0.0062  -0.0094 -0.0363 70  ILE A CB  
533  C CG1 . ILE A 70  ? 0.4429 0.3906 0.3611 0.0014  -0.0106 -0.0256 70  ILE A CG1 
534  C CG2 . ILE A 70  ? 0.4472 0.3689 0.3711 0.0040  -0.0117 -0.0405 70  ILE A CG2 
535  C CD1 . ILE A 70  ? 0.4360 0.3829 0.3597 -0.0057 -0.0170 -0.0261 70  ILE A CD1 
536  N N   A ARG A 71  ? 0.4948 0.4228 0.3838 0.0221  0.0019  -0.0537 71  ARG A N   
537  N N   B ARG A 71  ? 0.4949 0.4230 0.3838 0.0221  0.0019  -0.0536 71  ARG A N   
538  C CA  A ARG A 71  ? 0.5054 0.4210 0.3887 0.0276  0.0063  -0.0659 71  ARG A CA  
539  C CA  B ARG A 71  ? 0.5056 0.4218 0.3879 0.0276  0.0062  -0.0661 71  ARG A CA  
540  C C   A ARG A 71  ? 0.4957 0.4132 0.3832 0.0369  0.0162  -0.0608 71  ARG A C   
541  C C   B ARG A 71  ? 0.4961 0.4138 0.3827 0.0369  0.0162  -0.0612 71  ARG A C   
542  O O   A ARG A 71  ? 0.4971 0.4018 0.3907 0.0421  0.0218  -0.0668 71  ARG A O   
543  O O   B ARG A 71  ? 0.4979 0.4027 0.3899 0.0421  0.0217  -0.0677 71  ARG A O   
544  C CB  A ARG A 71  ? 0.5515 0.4696 0.4132 0.0271  0.0036  -0.0779 71  ARG A CB  
545  C CB  B ARG A 71  ? 0.5506 0.4706 0.4112 0.0268  0.0033  -0.0771 71  ARG A CB  
546  C CG  A ARG A 71  ? 0.5612 0.4964 0.4096 0.0313  0.0072  -0.0722 71  ARG A CG  
547  C CG  B ARG A 71  ? 0.6317 0.5449 0.4780 0.0340  0.0101  -0.0902 71  ARG A CG  
548  C CD  A ARG A 71  ? 0.6502 0.5885 0.4760 0.0313  0.0051  -0.0839 71  ARG A CD  
549  C CD  B ARG A 71  ? 0.6343 0.5557 0.4569 0.0313  0.0053  -0.0989 71  ARG A CD  
550  N NE  A ARG A 71  ? 0.6848 0.6184 0.5076 0.0223  -0.0055 -0.0914 71  ARG A NE  
551  N NE  B ARG A 71  ? 0.7885 0.7060 0.5929 0.0378  0.0120  -0.1122 71  ARG A NE  
552  C CZ  A ARG A 71  ? 0.6778 0.6158 0.4818 0.0191  -0.0109 -0.1008 71  ARG A CZ  
553  C CZ  B ARG A 71  ? 0.8346 0.7664 0.6217 0.0427  0.0165  -0.1105 71  ARG A CZ  
554  N NH1 A ARG A 71  ? 0.7896 0.7372 0.5744 0.0246  -0.0061 -0.1036 71  ARG A NH1 
555  N NH1 B ARG A 71  ? 0.6921 0.6424 0.4800 0.0421  0.0150  -0.0957 71  ARG A NH1 
556  N NH2 A ARG A 71  ? 0.7214 0.6560 0.5264 0.0100  -0.0216 -0.1060 71  ARG A NH2 
557  N NH2 B ARG A 71  ? 0.7575 0.6849 0.5266 0.0484  0.0232  -0.1242 71  ARG A NH2 
558  N N   . MET A 72  ? 0.4664 0.3994 0.3530 0.0389  0.0188  -0.0496 72  MET A N   
559  C CA  . MET A 72  ? 0.4632 0.4008 0.3557 0.0470  0.0274  -0.0426 72  MET A CA  
560  C C   . MET A 72  ? 0.4648 0.4135 0.3703 0.0440  0.0259  -0.0271 72  MET A C   
561  O O   . MET A 72  ? 0.4053 0.3679 0.3071 0.0439  0.0265  -0.0200 72  MET A O   
562  C CB  . MET A 72  ? 0.4882 0.4353 0.3651 0.0527  0.0325  -0.0453 72  MET A CB  
563  C CG  . MET A 72  ? 0.6226 0.5753 0.5068 0.0616  0.0421  -0.0381 72  MET A CG  
564  S SD  . MET A 72  ? 0.6725 0.6390 0.5397 0.0682  0.0487  -0.0387 72  MET A SD  
565  C CE  . MET A 72  ? 0.5494 0.5346 0.4270 0.0651  0.0467  -0.0208 72  MET A CE  
566  N N   . PRO A 73  ? 0.4179 0.3610 0.3386 0.0410  0.0237  -0.0216 73  PRO A N   
567  C CA  . PRO A 73  ? 0.3864 0.3412 0.3168 0.0371  0.0218  -0.0076 73  PRO A CA  
568  C C   . PRO A 73  ? 0.4174 0.3845 0.3515 0.0419  0.0266  0.0018  73  PRO A C   
569  O O   . PRO A 73  ? 0.4156 0.3954 0.3497 0.0377  0.0243  0.0098  73  PRO A O   
570  C CB  . PRO A 73  ? 0.3643 0.3104 0.3111 0.0354  0.0205  -0.0032 73  PRO A CB  
571  C CG  . PRO A 73  ? 0.4319 0.3610 0.3814 0.0407  0.0241  -0.0141 73  PRO A CG  
572  C CD  . PRO A 73  ? 0.4103 0.3367 0.3403 0.0407  0.0232  -0.0279 73  PRO A CD  
573  N N   . GLU A 74  ? 0.3999 0.3635 0.3384 0.0503  0.0335  0.0010  74  GLU A N   
574  C CA  . GLU A 74  ? 0.4387 0.4154 0.3821 0.0551  0.0383  0.0105  74  GLU A CA  
575  C C   . GLU A 74  ? 0.4155 0.3995 0.3436 0.0566  0.0399  0.0058  74  GLU A C   
576  O O   . GLU A 74  ? 0.4176 0.4001 0.3400 0.0641  0.0466  0.0009  74  GLU A O   
577  C CB  . GLU A 74  ? 0.4060 0.3771 0.3627 0.0642  0.0461  0.0128  74  GLU A CB  
578  C CG  . GLU A 74  ? 0.4494 0.4136 0.4240 0.0626  0.0443  0.0193  74  GLU A CG  
579  C CD  . GLU A 74  ? 0.4826 0.4444 0.4759 0.0717  0.0523  0.0259  74  GLU A CD  
580  O OE1 . GLU A 74  ? 0.5688 0.5357 0.5612 0.0791  0.0594  0.0262  74  GLU A OE1 
581  O OE2 . GLU A 74  ? 0.5334 0.4888 0.5441 0.0718  0.0519  0.0319  74  GLU A OE2 
582  N N   . TYR A 75  ? 0.3667 0.3588 0.2886 0.0493  0.0343  0.0080  75  TYR A N   
583  C CA  . TYR A 75  ? 0.4101 0.4078 0.3184 0.0490  0.0342  0.0036  75  TYR A CA  
584  C C   . TYR A 75  ? 0.3906 0.4022 0.3020 0.0528  0.0388  0.0120  75  TYR A C   
585  O O   . TYR A 75  ? 0.4041 0.4261 0.3178 0.0481  0.0363  0.0182  75  TYR A O   
586  C CB  . TYR A 75  ? 0.3251 0.3245 0.2297 0.0401  0.0272  0.0029  75  TYR A CB  
587  C CG  . TYR A 75  ? 0.3636 0.3646 0.2550 0.0395  0.0258  -0.0033 75  TYR A CG  
588  C CD1 . TYR A 75  ? 0.3847 0.3772 0.2653 0.0421  0.0258  -0.0137 75  TYR A CD1 
589  C CD2 . TYR A 75  ? 0.3498 0.3613 0.2404 0.0359  0.0243  0.0016  75  TYR A CD2 
590  C CE1 . TYR A 75  ? 0.4608 0.4576 0.3287 0.0410  0.0236  -0.0180 75  TYR A CE1 
591  C CE2 . TYR A 75  ? 0.3515 0.3665 0.2324 0.0355  0.0229  -0.0015 75  TYR A CE2 
592  C CZ  . TYR A 75  ? 0.4689 0.4778 0.3379 0.0380  0.0222  -0.0107 75  TYR A CZ  
593  O OH  . TYR A 75  ? 0.5488 0.5638 0.4074 0.0371  0.0198  -0.0125 75  TYR A OH  
594  N N   . LEU A 76  ? 0.4091 0.4203 0.3217 0.0616  0.0464  0.0116  76  LEU A N   
595  C CA  . LEU A 76  ? 0.4150 0.4395 0.3338 0.0664  0.0519  0.0209  76  LEU A CA  
596  C C   . LEU A 76  ? 0.4491 0.4852 0.3610 0.0643  0.0513  0.0236  76  LEU A C   
597  O O   . LEU A 76  ? 0.3882 0.4365 0.3107 0.0629  0.0516  0.0339  76  LEU A O   
598  C CB  . LEU A 76  ? 0.4153 0.4359 0.3336 0.0774  0.0618  0.0175  76  LEU A CB  
599  C CG  . LEU A 76  ? 0.4586 0.4926 0.3883 0.0840  0.0691  0.0289  76  LEU A CG  
600  C CD1 . LEU A 76  ? 0.3752 0.4162 0.3252 0.0805  0.0656  0.0418  76  LEU A CD1 
601  C CD2 . LEU A 76  ? 0.3574 0.3851 0.2855 0.0954  0.0803  0.0233  76  LEU A CD2 
602  N N   . PRO A 77  ? 0.4631 0.4971 0.3596 0.0639  0.0504  0.0158  77  PRO A N   
603  C CA  . PRO A 77  ? 0.3544 0.4012 0.2481 0.0628  0.0506  0.0213  77  PRO A CA  
604  C C   . PRO A 77  ? 0.3777 0.4308 0.2829 0.0545  0.0452  0.0289  77  PRO A C   
605  O O   . PRO A 77  ? 0.3687 0.4333 0.2810 0.0543  0.0471  0.0372  77  PRO A O   
606  C CB  . PRO A 77  ? 0.3840 0.4267 0.2604 0.0615  0.0478  0.0120  77  PRO A CB  
607  C CG  . PRO A 77  ? 0.4246 0.4532 0.2927 0.0647  0.0488  0.0003  77  PRO A CG  
608  C CD  . PRO A 77  ? 0.4641 0.4854 0.3471 0.0632  0.0478  0.0030  77  PRO A CD  
609  N N   . LYS A 78  ? 0.3422 0.3878 0.2496 0.0475  0.0390  0.0259  78  LYS A N   
610  C CA  . LYS A 78  ? 0.3296 0.3801 0.2457 0.0394  0.0347  0.0309  78  LYS A CA  
611  C C   . LYS A 78  ? 0.3864 0.4412 0.3148 0.0375  0.0341  0.0376  78  LYS A C   
612  O O   . LYS A 78  ? 0.3877 0.4517 0.3249 0.0336  0.0333  0.0440  78  LYS A O   
613  C CB  . LYS A 78  ? 0.3277 0.3702 0.2392 0.0327  0.0291  0.0247  78  LYS A CB  
614  C CG  . LYS A 78  ? 0.3991 0.4402 0.3008 0.0334  0.0283  0.0199  78  LYS A CG  
615  C CD  . LYS A 78  ? 0.3627 0.4151 0.2671 0.0346  0.0310  0.0263  78  LYS A CD  
616  C CE  . LYS A 78  ? 0.3130 0.3673 0.2079 0.0356  0.0298  0.0240  78  LYS A CE  
617  N NZ  . LYS A 78  ? 0.3210 0.3708 0.2178 0.0289  0.0246  0.0214  78  LYS A NZ  
618  N N   . LEU A 79  ? 0.3439 0.3927 0.2741 0.0399  0.0342  0.0369  79  LEU A N   
619  C CA  . LEU A 79  ? 0.3544 0.4091 0.2967 0.0375  0.0325  0.0449  79  LEU A CA  
620  C C   . LEU A 79  ? 0.3774 0.4445 0.3303 0.0415  0.0364  0.0543  79  LEU A C   
621  O O   . LEU A 79  ? 0.3645 0.4415 0.3273 0.0360  0.0330  0.0617  79  LEU A O   
622  C CB  . LEU A 79  ? 0.3340 0.3802 0.2789 0.0406  0.0327  0.0441  79  LEU A CB  
623  C CG  . LEU A 79  ? 0.3991 0.4517 0.3556 0.0364  0.0290  0.0534  79  LEU A CG  
624  C CD1 . LEU A 79  ? 0.2729 0.3282 0.2255 0.0257  0.0223  0.0526  79  LEU A CD1 
625  C CD2 . LEU A 79  ? 0.4182 0.4623 0.3808 0.0410  0.0305  0.0543  79  LEU A CD2 
626  N N   . SER A 80  ? 0.3320 0.3995 0.2831 0.0507  0.0435  0.0541  80  SER A N   
627  C CA  . SER A 80  ? 0.3173 0.3976 0.2800 0.0554  0.0484  0.0641  80  SER A CA  
628  C C   . SER A 80  ? 0.3130 0.4038 0.2799 0.0499  0.0464  0.0688  80  SER A C   
629  O O   . SER A 80  ? 0.2795 0.3824 0.2597 0.0512  0.0487  0.0787  80  SER A O   
630  C CB  . SER A 80  ? 0.3386 0.4172 0.2963 0.0670  0.0581  0.0619  80  SER A CB  
631  O OG  . SER A 80  ? 0.3062 0.3816 0.2479 0.0680  0.0594  0.0541  80  SER A OG  
632  N N   . GLN A 81  ? 0.3158 0.4021 0.2740 0.0440  0.0427  0.0625  81  GLN A N   
633  C CA  . GLN A 81  ? 0.2757 0.3697 0.2407 0.0380  0.0409  0.0663  81  GLN A CA  
634  C C   . GLN A 81  ? 0.3689 0.4649 0.3415 0.0273  0.0340  0.0672  81  GLN A C   
635  O O   . GLN A 81  ? 0.3283 0.4296 0.3089 0.0216  0.0326  0.0696  81  GLN A O   
636  C CB  . GLN A 81  ? 0.3586 0.4474 0.3136 0.0367  0.0407  0.0602  81  GLN A CB  
637  C CG  . GLN A 81  ? 0.2999 0.3879 0.2434 0.0453  0.0460  0.0580  81  GLN A CG  
638  C CD  . GLN A 81  ? 0.3295 0.4175 0.2678 0.0428  0.0448  0.0560  81  GLN A CD  
639  O OE1 . GLN A 81  ? 0.3117 0.4051 0.2609 0.0380  0.0440  0.0612  81  GLN A OE1 
640  N NE2 . GLN A 81  ? 0.3485 0.4303 0.2717 0.0456  0.0445  0.0488  81  GLN A NE2 
641  N N   . GLY A 82  ? 0.2567 0.3484 0.2267 0.0243  0.0299  0.0651  82  GLY A N   
642  C CA  . GLY A 82  ? 0.2673 0.3603 0.2389 0.0136  0.0233  0.0636  82  GLY A CA  
643  C C   . GLY A 82  ? 0.3075 0.3899 0.2677 0.0086  0.0210  0.0539  82  GLY A C   
644  O O   . GLY A 82  ? 0.2674 0.3506 0.2271 -0.0004 0.0168  0.0512  82  GLY A O   
645  N N   . VAL A 83  ? 0.2663 0.3397 0.2176 0.0137  0.0238  0.0484  83  VAL A N   
646  C CA  . VAL A 83  ? 0.3154 0.3798 0.2583 0.0094  0.0218  0.0404  83  VAL A CA  
647  C C   . VAL A 83  ? 0.2795 0.3390 0.2183 0.0074  0.0187  0.0388  83  VAL A C   
648  O O   . VAL A 83  ? 0.2862 0.3424 0.2242 0.0133  0.0198  0.0402  83  VAL A O   
649  C CB  . VAL A 83  ? 0.4187 0.4772 0.3546 0.0149  0.0245  0.0364  83  VAL A CB  
650  C CG1 . VAL A 83  ? 0.2514 0.3016 0.1813 0.0105  0.0221  0.0296  83  VAL A CG1 
651  C CG2 . VAL A 83  ? 0.2387 0.3042 0.1800 0.0168  0.0278  0.0403  83  VAL A CG2 
652  N N   . THR A 84  ? 0.2821 0.3409 0.2186 -0.0007 0.0157  0.0359  84  THR A N   
653  C CA  . THR A 84  ? 0.3486 0.4043 0.2815 -0.0030 0.0130  0.0358  84  THR A CA  
654  C C   . THR A 84  ? 0.3379 0.3846 0.2644 -0.0053 0.0131  0.0291  84  THR A C   
655  O O   . THR A 84  ? 0.3182 0.3614 0.2427 -0.0063 0.0115  0.0296  84  THR A O   
656  C CB  . THR A 84  ? 0.3544 0.4196 0.2888 -0.0108 0.0093  0.0397  84  THR A CB  
657  O OG1 . THR A 84  ? 0.3064 0.3734 0.2392 -0.0181 0.0093  0.0345  84  THR A OG1 
658  C CG2 . THR A 84  ? 0.2900 0.3655 0.2332 -0.0085 0.0081  0.0488  84  THR A CG2 
659  N N   . THR A 85  ? 0.2886 0.3324 0.2142 -0.0061 0.0150  0.0244  85  THR A N   
660  C CA  . THR A 85  ? 0.3622 0.3985 0.2844 -0.0074 0.0153  0.0194  85  THR A CA  
661  C C   . THR A 85  ? 0.3778 0.4117 0.3004 -0.0031 0.0169  0.0176  85  THR A C   
662  O O   . THR A 85  ? 0.2949 0.3336 0.2217 -0.0026 0.0189  0.0193  85  THR A O   
663  C CB  . THR A 85  ? 0.3118 0.3489 0.2339 -0.0150 0.0162  0.0161  85  THR A CB  
664  O OG1 . THR A 85  ? 0.3779 0.4189 0.2969 -0.0195 0.0142  0.0181  85  THR A OG1 
665  C CG2 . THR A 85  ? 0.3041 0.3347 0.2259 -0.0155 0.0174  0.0125  85  THR A CG2 
666  N N   . VAL A 86  ? 0.3603 0.3881 0.2795 -0.0006 0.0156  0.0150  86  VAL A N   
667  C CA  . VAL A 86  ? 0.3264 0.3536 0.2446 0.0021  0.0159  0.0137  86  VAL A CA  
668  C C   . VAL A 86  ? 0.3330 0.3570 0.2539 -0.0021 0.0151  0.0115  86  VAL A C   
669  O O   . VAL A 86  ? 0.3168 0.3363 0.2373 -0.0049 0.0135  0.0099  86  VAL A O   
670  C CB  . VAL A 86  ? 0.3343 0.3583 0.2455 0.0081  0.0146  0.0116  86  VAL A CB  
671  C CG1 . VAL A 86  ? 0.2555 0.2837 0.1657 0.0135  0.0173  0.0145  86  VAL A CG1 
672  C CG2 . VAL A 86  ? 0.3280 0.3432 0.2371 0.0071  0.0116  0.0080  86  VAL A CG2 
673  N N   . ILE A 87  ? 0.3494 0.3767 0.2754 -0.0024 0.0166  0.0130  87  ILE A N   
674  C CA  . ILE A 87  ? 0.3896 0.4152 0.3210 -0.0052 0.0163  0.0126  87  ILE A CA  
675  C C   . ILE A 87  ? 0.3364 0.3635 0.2648 -0.0022 0.0126  0.0134  87  ILE A C   
676  O O   . ILE A 87  ? 0.3239 0.3571 0.2521 0.0010  0.0131  0.0168  87  ILE A O   
677  C CB  . ILE A 87  ? 0.3680 0.3965 0.3102 -0.0079 0.0211  0.0143  87  ILE A CB  
678  C CG1 . ILE A 87  ? 0.3333 0.3605 0.2756 -0.0121 0.0241  0.0113  87  ILE A CG1 
679  C CG2 . ILE A 87  ? 0.2314 0.2589 0.1820 -0.0097 0.0217  0.0153  87  ILE A CG2 
680  C CD1 . ILE A 87  ? 0.3237 0.3499 0.2758 -0.0161 0.0296  0.0095  87  ILE A CD1 
681  N N   . VAL A 88  ? 0.3543 0.3767 0.2806 -0.0037 0.0085  0.0108  88  VAL A N   
682  C CA  . VAL A 88  ? 0.3524 0.3758 0.2735 -0.0021 0.0033  0.0099  88  VAL A CA  
683  C C   . VAL A 88  ? 0.3015 0.3287 0.2324 -0.0053 0.0014  0.0135  88  VAL A C   
684  O O   . VAL A 88  ? 0.3032 0.3306 0.2452 -0.0079 0.0052  0.0161  88  VAL A O   
685  C CB  . VAL A 88  ? 0.3865 0.4016 0.3000 -0.0019 -0.0007 0.0038  88  VAL A CB  
686  C CG1 . VAL A 88  ? 0.2619 0.2738 0.1698 0.0016  0.0024  0.0021  88  VAL A CG1 
687  C CG2 . VAL A 88  ? 0.2665 0.2761 0.1874 -0.0067 -0.0023 0.0034  88  VAL A CG2 
688  N N   . GLY A 89  ? 0.3434 0.3746 0.2704 -0.0049 -0.0044 0.0139  89  GLY A N   
689  C CA  . GLY A 89  ? 0.2262 0.2628 0.1637 -0.0081 -0.0078 0.0188  89  GLY A CA  
690  C C   . GLY A 89  ? 0.3368 0.3840 0.2850 -0.0068 -0.0048 0.0278  89  GLY A C   
691  O O   . GLY A 89  ? 0.2726 0.3228 0.2367 -0.0090 -0.0033 0.0334  89  GLY A O   
692  N N   . ASN A 90  ? 0.3312 0.3845 0.2731 -0.0028 -0.0031 0.0304  90  ASN A N   
693  C CA  . ASN A 90  ? 0.2879 0.3513 0.2423 -0.0010 0.0006  0.0403  90  ASN A CA  
694  C C   . ASN A 90  ? 0.3324 0.4090 0.2871 -0.0009 -0.0057 0.0481  90  ASN A C   
695  O O   . ASN A 90  ? 0.3014 0.3794 0.2432 -0.0024 -0.0135 0.0441  90  ASN A O   
696  C CB  . ASN A 90  ? 0.2847 0.3495 0.2352 0.0029  0.0060  0.0412  90  ASN A CB  
697  C CG  . ASN A 90  ? 0.3705 0.4262 0.3269 0.0015  0.0123  0.0369  90  ASN A CG  
698  O OD1 . ASN A 90  ? 0.3334 0.3891 0.3056 0.0001  0.0177  0.0404  90  ASN A OD1 
699  N ND2 . ASN A 90  ? 0.3458 0.3940 0.2903 0.0015  0.0117  0.0292  90  ASN A ND2 
700  N N   . CYS A 91  ? 0.2947 0.3812 0.2655 0.0005  -0.0023 0.0597  91  CYS A N   
701  C CA  . CYS A 91  ? 0.3237 0.4266 0.2978 0.0010  -0.0076 0.0710  91  CYS A CA  
702  C C   . CYS A 91  ? 0.3309 0.4373 0.3059 -0.0035 -0.0166 0.0714  91  CYS A C   
703  O O   . CYS A 91  ? 0.3199 0.4387 0.2855 -0.0045 -0.0249 0.0753  91  CYS A O   
704  C CB  . CYS A 91  ? 0.2824 0.3938 0.2365 0.0046  -0.0100 0.0713  91  CYS A CB  
705  S SG  . CYS A 91  ? 0.3060 0.4156 0.2636 0.0096  0.0004  0.0735  91  CYS A SG  
706  N N   . GLY A 92  ? 0.2765 0.3734 0.2628 -0.0068 -0.0153 0.0678  92  GLY A N   
707  C CA  . GLY A 92  ? 0.2850 0.3860 0.2772 -0.0115 -0.0234 0.0699  92  GLY A CA  
708  C C   . GLY A 92  ? 0.3121 0.4061 0.2847 -0.0150 -0.0320 0.0579  92  GLY A C   
709  O O   . GLY A 92  ? 0.2781 0.3756 0.2559 -0.0198 -0.0400 0.0592  92  GLY A O   
710  N N   . ILE A 93  ? 0.2750 0.3594 0.2277 -0.0127 -0.0305 0.0467  93  ILE A N   
711  C CA  . ILE A 93  ? 0.3168 0.3934 0.2515 -0.0154 -0.0378 0.0346  93  ILE A CA  
712  C C   . ILE A 93  ? 0.3612 0.4209 0.2926 -0.0144 -0.0321 0.0249  93  ILE A C   
713  O O   . ILE A 93  ? 0.3694 0.4252 0.2962 -0.0099 -0.0246 0.0234  93  ILE A O   
714  C CB  . ILE A 93  ? 0.3580 0.4411 0.2699 -0.0133 -0.0422 0.0305  93  ILE A CB  
715  C CG1 . ILE A 93  ? 0.3161 0.3996 0.2213 -0.0064 -0.0330 0.0316  93  ILE A CG1 
716  C CG2 . ILE A 93  ? 0.3442 0.4459 0.2571 -0.0160 -0.0506 0.0400  93  ILE A CG2 
717  C CD1 . ILE A 93  ? 0.4299 0.5151 0.3104 -0.0032 -0.0345 0.0240  93  ILE A CD1 
718  N N   . SER A 94  ? 0.2927 0.3436 0.2277 -0.0187 -0.0360 0.0198  94  SER A N   
719  C CA  . SER A 94  ? 0.3479 0.3845 0.2813 -0.0182 -0.0314 0.0126  94  SER A CA  
720  C C   . SER A 94  ? 0.2778 0.3057 0.2060 -0.0222 -0.0390 0.0042  94  SER A C   
721  O O   . SER A 94  ? 0.3531 0.3854 0.2864 -0.0273 -0.0473 0.0055  94  SER A O   
722  C CB  . SER A 94  ? 0.3118 0.3462 0.2627 -0.0193 -0.0244 0.0181  94  SER A CB  
723  O OG  . SER A 94  ? 0.2946 0.3323 0.2607 -0.0241 -0.0283 0.0230  94  SER A OG  
724  N N   . ALA A 95  ? 0.3279 0.3436 0.2476 -0.0202 -0.0365 -0.0040 95  ALA A N   
725  C CA  . ALA A 95  ? 0.3350 0.3397 0.2548 -0.0241 -0.0422 -0.0116 95  ALA A CA  
726  C C   . ALA A 95  ? 0.3566 0.3587 0.2953 -0.0285 -0.0418 -0.0061 95  ALA A C   
727  O O   . ALA A 95  ? 0.3336 0.3336 0.2799 -0.0341 -0.0491 -0.0072 95  ALA A O   
728  C CB  . ALA A 95  ? 0.3957 0.3884 0.3051 -0.0199 -0.0384 -0.0202 95  ALA A CB  
729  N N   . ALA A 96  ? 0.3032 0.3060 0.2492 -0.0263 -0.0332 -0.0002 96  ALA A N   
730  C CA  . ALA A 96  ? 0.3843 0.3859 0.3464 -0.0298 -0.0309 0.0055  96  ALA A CA  
731  C C   . ALA A 96  ? 0.3813 0.3920 0.3574 -0.0340 -0.0352 0.0122  96  ALA A C   
732  O O   . ALA A 96  ? 0.3474 0.3681 0.3252 -0.0326 -0.0343 0.0170  96  ALA A O   
733  C CB  . ALA A 96  ? 0.3348 0.3379 0.2991 -0.0270 -0.0206 0.0097  96  ALA A CB  
734  N N   . THR A 97  ? 0.3739 0.3818 0.3625 -0.0391 -0.0397 0.0137  97  THR A N   
735  C CA  . THR A 97  ? 0.3391 0.3554 0.3448 -0.0441 -0.0449 0.0210  97  THR A CA  
736  C C   . THR A 97  ? 0.3864 0.4082 0.3875 -0.0478 -0.0570 0.0183  97  THR A C   
737  O O   . THR A 97  ? 0.3425 0.3725 0.3587 -0.0528 -0.0633 0.0249  97  THR A O   
738  C CB  . THR A 97  ? 0.3155 0.3424 0.3344 -0.0421 -0.0369 0.0312  97  THR A CB  
739  O OG1 . THR A 97  ? 0.3211 0.3570 0.3349 -0.0396 -0.0382 0.0332  97  THR A OG1 
740  C CG2 . THR A 97  ? 0.3082 0.3307 0.3252 -0.0383 -0.0245 0.0313  97  THR A CG2 
741  N N   . ALA A 98  ? 0.3574 0.3763 0.3382 -0.0457 -0.0605 0.0093  98  ALA A N   
742  C CA  . ALA A 98  ? 0.3770 0.4038 0.3499 -0.0493 -0.0717 0.0066  98  ALA A CA  
743  C C   . ALA A 98  ? 0.4527 0.4711 0.4263 -0.0564 -0.0822 -0.0019 98  ALA A C   
744  O O   . ALA A 98  ? 0.4559 0.4593 0.4212 -0.0556 -0.0812 -0.0124 98  ALA A O   
745  C CB  . ALA A 98  ? 0.3562 0.3846 0.3061 -0.0441 -0.0703 0.0004  98  ALA A CB  
746  N N   . THR A 99  ? 0.4432 0.4713 0.4287 -0.0636 -0.0924 0.0031  99  THR A N   
747  C CA  . THR A 99  ? 0.4661 0.4889 0.4520 -0.0721 -0.1051 -0.0054 99  THR A CA  
748  C C   . THR A 99  ? 0.5494 0.5843 0.5190 -0.0756 -0.1163 -0.0093 99  THR A C   
749  O O   . THR A 99  ? 0.5370 0.5901 0.5110 -0.0751 -0.1177 0.0025  99  THR A O   
750  C CB  . THR A 99  ? 0.4564 0.4828 0.4706 -0.0788 -0.1093 0.0045  99  THR A CB  
751  O OG1 . THR A 99  ? 0.5191 0.5337 0.5450 -0.0759 -0.0992 0.0066  99  THR A OG1 
752  C CG2 . THR A 99  ? 0.5241 0.5479 0.5410 -0.0894 -0.1248 -0.0034 99  THR A CG2 
753  N N   . MET A 100 ? 0.5490 0.5742 0.5000 -0.0790 -0.1235 -0.0255 100 MET A N   
754  C CA  . MET A 100 ? 0.6131 0.6495 0.5439 -0.0832 -0.1346 -0.0319 100 MET A CA  
755  C C   . MET A 100 ? 0.6289 0.6660 0.5678 -0.0957 -0.1506 -0.0368 100 MET A C   
756  O O   . MET A 100 ? 0.7326 0.7522 0.6668 -0.1000 -0.1544 -0.0525 100 MET A O   
757  C CB  . MET A 100 ? 0.6409 0.6666 0.5418 -0.0780 -0.1305 -0.0484 100 MET A CB  
758  C CG  . MET A 100 ? 0.6731 0.7010 0.5654 -0.0665 -0.1164 -0.0429 100 MET A CG  
759  S SD  . MET A 100 ? 0.7066 0.7625 0.6005 -0.0645 -0.1174 -0.0245 100 MET A SD  
760  C CE  . MET A 100 ? 0.5549 0.6070 0.4456 -0.0518 -0.0995 -0.0194 100 MET A CE  
761  N N   . ARG A 101 ? 0.6698 0.7273 0.6228 -0.1018 -0.1599 -0.0232 101 ARG A N   
762  C CA  A ARG A 101 ? 0.6756 0.7379 0.6373 -0.1148 -0.1770 -0.0262 101 ARG A CA  
763  C CA  B ARG A 101 ? 0.6761 0.7376 0.6375 -0.1148 -0.1770 -0.0268 101 ARG A CA  
764  C C   . ARG A 101 ? 0.8081 0.8786 0.7407 -0.1209 -0.1900 -0.0388 101 ARG A C   
765  O O   . ARG A 101 ? 0.8976 0.9750 0.8342 -0.1330 -0.2063 -0.0419 101 ARG A O   
766  C CB  A ARG A 101 ? 0.6590 0.7415 0.6514 -0.1188 -0.1816 -0.0042 101 ARG A CB  
767  C CB  B ARG A 101 ? 0.6594 0.7401 0.6524 -0.1193 -0.1818 -0.0054 101 ARG A CB  
768  C CG  A ARG A 101 ? 0.6675 0.7431 0.6886 -0.1136 -0.1686 0.0078  101 ARG A CG  
769  C CG  B ARG A 101 ? 0.6634 0.7393 0.6807 -0.1305 -0.1924 -0.0056 101 ARG A CG  
770  C CD  A ARG A 101 ? 0.6318 0.7284 0.6832 -0.1158 -0.1707 0.0299  101 ARG A CD  
771  C CD  B ARG A 101 ? 0.6595 0.7514 0.7123 -0.1311 -0.1908 0.0175  101 ARG A CD  
772  N NE  A ARG A 101 ? 0.6216 0.7346 0.6701 -0.1081 -0.1638 0.0425  101 ARG A NE  
773  N NE  B ARG A 101 ? 0.6292 0.7229 0.6866 -0.1186 -0.1729 0.0290  101 ARG A NE  
774  C CZ  A ARG A 101 ? 0.5515 0.6865 0.6217 -0.1094 -0.1669 0.0616  101 ARG A CZ  
775  C CZ  B ARG A 101 ? 0.5947 0.6734 0.6611 -0.1118 -0.1583 0.0296  101 ARG A CZ  
776  N NH1 A ARG A 101 ? 0.4807 0.6258 0.5767 -0.1184 -0.1773 0.0710  101 ARG A NH1 
777  N NH1 B ARG A 101 ? 0.6056 0.6671 0.6803 -0.1156 -0.1586 0.0219  101 ARG A NH1 
778  N NH2 A ARG A 101 ? 0.4906 0.6380 0.5589 -0.1016 -0.1592 0.0723  101 ARG A NH2 
779  N NH2 B ARG A 101 ? 0.5281 0.6095 0.5956 -0.1015 -0.1432 0.0382  101 ARG A NH2 
780  N N   . GLY A 102 ? 0.8371 0.9082 0.7409 -0.1131 -0.1832 -0.0458 102 GLY A N   
781  C CA  . GLY A 102 ? 0.7138 0.7943 0.5862 -0.1176 -0.1933 -0.0577 102 GLY A CA  
782  C C   . GLY A 102 ? 0.7460 0.8274 0.5914 -0.1060 -0.1812 -0.0610 102 GLY A C   
783  O O   . GLY A 102 ? 0.8693 0.9323 0.7124 -0.0968 -0.1669 -0.0670 102 GLY A O   
784  N N   . GLU A 103 ? 0.7033 0.8078 0.5298 -0.1065 -0.1869 -0.0555 103 GLU A N   
785  C CA  A GLU A 103 ? 0.7512 0.8595 0.5527 -0.0959 -0.1757 -0.0571 103 GLU A CA  
786  C CA  B GLU A 103 ? 0.7509 0.8591 0.5524 -0.0959 -0.1757 -0.0572 103 GLU A CA  
787  C C   . GLU A 103 ? 0.7045 0.8095 0.5243 -0.0841 -0.1589 -0.0424 103 GLU A C   
788  O O   . GLU A 103 ? 0.7227 0.8346 0.5715 -0.0840 -0.1576 -0.0248 103 GLU A O   
789  C CB  A GLU A 103 ? 0.7240 0.8609 0.5098 -0.0973 -0.1836 -0.0476 103 GLU A CB  
790  C CB  B GLU A 103 ? 0.7244 0.8610 0.5098 -0.0973 -0.1836 -0.0482 103 GLU A CB  
791  C CG  A GLU A 103 ? 0.7764 0.9137 0.5451 -0.1033 -0.1953 -0.0629 103 GLU A CG  
792  C CG  B GLU A 103 ? 0.7073 0.8682 0.5204 -0.1011 -0.1911 -0.0231 103 GLU A CG  
793  C CD  A GLU A 103 ? 0.8904 1.0085 0.6266 -0.0984 -0.1892 -0.0876 103 GLU A CD  
794  C CD  B GLU A 103 ? 0.7356 0.9118 0.5593 -0.0921 -0.1806 -0.0013 103 GLU A CD  
795  O OE1 A GLU A 103 ? 0.9343 1.0353 0.6657 -0.0919 -0.1765 -0.0949 103 GLU A OE1 
796  O OE1 B GLU A 103 ? 0.8081 0.9888 0.6114 -0.0835 -0.1721 -0.0017 103 GLU A OE1 
797  O OE2 A GLU A 103 ? 0.8859 1.0059 0.6019 -0.1009 -0.1969 -0.0991 103 GLU A OE2 
798  O OE2 B GLU A 103 ? 0.7222 0.9015 0.5790 -0.0908 -0.1772 0.0157  103 GLU A OE2 
799  N N   . VAL A 104 ? 0.6138 0.7082 0.4164 -0.0741 -0.1458 -0.0501 104 VAL A N   
800  C CA  . VAL A 104 ? 0.6534 0.7454 0.4691 -0.0633 -0.1303 -0.0381 104 VAL A CA  
801  C C   . VAL A 104 ? 0.5848 0.7024 0.3990 -0.0593 -0.1290 -0.0201 104 VAL A C   
802  O O   . VAL A 104 ? 0.7063 0.8359 0.4949 -0.0580 -0.1310 -0.0233 104 VAL A O   
803  C CB  . VAL A 104 ? 0.6594 0.7317 0.4598 -0.0547 -0.1175 -0.0521 104 VAL A CB  
804  C CG1 . VAL A 104 ? 0.6348 0.7119 0.4412 -0.0441 -0.1036 -0.0392 104 VAL A CG1 
805  C CG2 . VAL A 104 ? 0.7441 0.7915 0.5579 -0.0566 -0.1155 -0.0627 104 VAL A CG2 
806  N N   . PRO A 105 ? 0.5731 0.6999 0.4145 -0.0574 -0.1254 -0.0008 105 PRO A N   
807  C CA  . PRO A 105 ? 0.4862 0.6374 0.3309 -0.0539 -0.1243 0.0180  105 PRO A CA  
808  C C   . PRO A 105 ? 0.5274 0.6763 0.3648 -0.0429 -0.1096 0.0207  105 PRO A C   
809  O O   . PRO A 105 ? 0.4610 0.5922 0.3065 -0.0374 -0.0983 0.0166  105 PRO A O   
810  C CB  . PRO A 105 ? 0.5255 0.6835 0.4062 -0.0560 -0.1248 0.0360  105 PRO A CB  
811  C CG  . PRO A 105 ? 0.5096 0.6428 0.4039 -0.0553 -0.1177 0.0270  105 PRO A CG  
812  C CD  . PRO A 105 ? 0.5366 0.6533 0.4086 -0.0592 -0.1230 0.0052  105 PRO A CD  
813  N N   . ASP A 106 ? 0.4989 0.6674 0.3208 -0.0401 -0.1102 0.0280  106 ASP A N   
814  C CA  A ASP A 106 ? 0.4917 0.6627 0.3117 -0.0302 -0.0969 0.0350  106 ASP A CA  
815  C CA  B ASP A 106 ? 0.4917 0.6624 0.3117 -0.0302 -0.0969 0.0348  106 ASP A CA  
816  C C   . ASP A 106 ? 0.4746 0.6435 0.3280 -0.0265 -0.0882 0.0502  106 ASP A C   
817  O O   . ASP A 106 ? 0.4874 0.6671 0.3638 -0.0305 -0.0933 0.0639  106 ASP A O   
818  C CB  A ASP A 106 ? 0.4467 0.6442 0.2505 -0.0289 -0.1004 0.0459  106 ASP A CB  
819  C CB  B ASP A 106 ? 0.4483 0.6450 0.2519 -0.0285 -0.0999 0.0455  106 ASP A CB  
820  C CG  A ASP A 106 ? 0.5061 0.7060 0.3026 -0.0187 -0.0869 0.0504  106 ASP A CG  
821  C CG  B ASP A 106 ? 0.4837 0.6791 0.2526 -0.0308 -0.1053 0.0280  106 ASP A CG  
822  O OD1 A ASP A 106 ? 0.5671 0.7518 0.3449 -0.0143 -0.0798 0.0347  106 ASP A OD1 
823  O OD1 B ASP A 106 ? 0.5378 0.7152 0.2935 -0.0345 -0.1084 0.0078  106 ASP A OD1 
824  O OD2 A ASP A 106 ? 0.5385 0.7560 0.3499 -0.0151 -0.0832 0.0706  106 ASP A OD2 
825  O OD2 B ASP A 106 ? 0.5630 0.7711 0.3210 -0.0284 -0.1048 0.0339  106 ASP A OD2 
826  N N   . PRO A 107 ? 0.4664 0.6221 0.3243 -0.0194 -0.0751 0.0481  107 PRO A N   
827  C CA  . PRO A 107 ? 0.4594 0.6026 0.2947 -0.0140 -0.0681 0.0338  107 PRO A CA  
828  C C   . PRO A 107 ? 0.4690 0.5869 0.3055 -0.0145 -0.0647 0.0182  107 PRO A C   
829  O O   . PRO A 107 ? 0.5069 0.6137 0.3374 -0.0085 -0.0552 0.0122  107 PRO A O   
830  C CB  . PRO A 107 ? 0.4507 0.5999 0.2957 -0.0062 -0.0563 0.0462  107 PRO A CB  
831  C CG  . PRO A 107 ? 0.4199 0.5671 0.2974 -0.0076 -0.0535 0.0578  107 PRO A CG  
832  C CD  . PRO A 107 ? 0.4404 0.5976 0.3261 -0.0152 -0.0657 0.0629  107 PRO A CD  
833  N N   . MET A 108 ? 0.4359 0.5455 0.2817 -0.0214 -0.0721 0.0133  108 MET A N   
834  C CA  . MET A 108 ? 0.4294 0.5160 0.2765 -0.0219 -0.0691 -0.0002 108 MET A CA  
835  C C   . MET A 108 ? 0.5760 0.6517 0.3979 -0.0191 -0.0673 -0.0171 108 MET A C   
836  O O   . MET A 108 ? 0.5234 0.5811 0.3466 -0.0164 -0.0613 -0.0260 108 MET A O   
837  C CB  . MET A 108 ? 0.4431 0.5246 0.3028 -0.0305 -0.0787 -0.0028 108 MET A CB  
838  C CG  . MET A 108 ? 0.4353 0.5246 0.3233 -0.0329 -0.0787 0.0127  108 MET A CG  
839  S SD  . MET A 108 ? 0.6330 0.7062 0.5401 -0.0291 -0.0661 0.0142  108 MET A SD  
840  C CE  . MET A 108 ? 0.4723 0.5278 0.3817 -0.0352 -0.0718 0.0018  108 MET A CE  
841  N N   . ASN A 109 ? 0.4240 0.5109 0.2232 -0.0194 -0.0721 -0.0212 109 ASN A N   
842  C CA  . ASN A 109 ? 0.4896 0.5664 0.2638 -0.0162 -0.0691 -0.0382 109 ASN A CA  
843  C C   . ASN A 109 ? 0.4913 0.5637 0.2632 -0.0060 -0.0550 -0.0368 109 ASN A C   
844  O O   . ASN A 109 ? 0.5945 0.6550 0.3513 -0.0019 -0.0498 -0.0504 109 ASN A O   
845  C CB  . ASN A 109 ? 0.5502 0.6432 0.2988 -0.0190 -0.0769 -0.0422 109 ASN A CB  
846  C CG  . ASN A 109 ? 0.6430 0.7610 0.3907 -0.0152 -0.0747 -0.0239 109 ASN A CG  
847  O OD1 . ASN A 109 ? 0.6340 0.7661 0.4004 -0.0185 -0.0796 -0.0075 109 ASN A OD1 
848  N ND2 . ASN A 109 ? 0.6840 0.8079 0.4125 -0.0079 -0.0666 -0.0256 109 ASN A ND2 
849  N N   . LEU A 110 ? 0.4700 0.5515 0.2580 -0.0020 -0.0486 -0.0207 110 LEU A N   
850  C CA  . LEU A 110 ? 0.4741 0.5506 0.2642 0.0064  -0.0362 -0.0188 110 LEU A CA  
851  C C   . LEU A 110 ? 0.6085 0.6633 0.4065 0.0072  -0.0319 -0.0282 110 LEU A C   
852  O O   . LEU A 110 ? 0.6083 0.6563 0.4020 0.0138  -0.0231 -0.0320 110 LEU A O   
853  C CB  . LEU A 110 ? 0.5277 0.6156 0.3374 0.0087  -0.0312 -0.0008 110 LEU A CB  
854  C CG  . LEU A 110 ? 0.6120 0.7227 0.4193 0.0106  -0.0314 0.0134  110 LEU A CG  
855  C CD1 . LEU A 110 ? 0.5006 0.6166 0.3323 0.0130  -0.0248 0.0291  110 LEU A CD1 
856  C CD2 . LEU A 110 ? 0.4976 0.6152 0.2814 0.0166  -0.0266 0.0094  110 LEU A CD2 
857  N N   . LEU A 111 ? 0.5143 0.5596 0.3257 0.0009  -0.0378 -0.0303 111 LEU A N   
858  C CA  . LEU A 111 ? 0.5233 0.5503 0.3452 0.0011  -0.0341 -0.0361 111 LEU A CA  
859  C C   . LEU A 111 ? 0.6021 0.6137 0.4126 0.0001  -0.0366 -0.0526 111 LEU A C   
860  O O   . LEU A 111 ? 0.5449 0.5433 0.3569 0.0045  -0.0299 -0.0582 111 LEU A O   
861  C CB  . LEU A 111 ? 0.4425 0.4675 0.2857 -0.0048 -0.0379 -0.0291 111 LEU A CB  
862  C CG  . LEU A 111 ? 0.4072 0.4458 0.2642 -0.0050 -0.0359 -0.0141 111 LEU A CG  
863  C CD1 . LEU A 111 ? 0.3205 0.3551 0.1977 -0.0102 -0.0378 -0.0093 111 LEU A CD1 
864  C CD2 . LEU A 111 ? 0.3834 0.4241 0.2420 0.0017  -0.0258 -0.0087 111 LEU A CD2 
865  N N   . GLY A 112 ? 0.5821 0.5953 0.3825 -0.0060 -0.0463 -0.0603 112 GLY A N   
866  C CA  . GLY A 112 ? 0.5969 0.5940 0.3881 -0.0084 -0.0494 -0.0777 112 GLY A CA  
867  C C   . GLY A 112 ? 0.6052 0.6076 0.3888 -0.0177 -0.0627 -0.0835 112 GLY A C   
868  O O   . GLY A 112 ? 0.6116 0.6322 0.3957 -0.0213 -0.0690 -0.0729 112 GLY A O   
869  N N   . GLU A 113 ? 0.6857 0.6721 0.4642 -0.0220 -0.0672 -0.1000 113 GLU A N   
870  C CA  A GLU A 113 ? 0.6791 0.6691 0.4488 -0.0320 -0.0809 -0.1084 113 GLU A CA  
871  C CA  B GLU A 113 ? 0.6791 0.6690 0.4488 -0.0320 -0.0809 -0.1085 113 GLU A CA  
872  C C   . GLU A 113 ? 0.5978 0.5814 0.3924 -0.0407 -0.0892 -0.1044 113 GLU A C   
873  O O   . GLU A 113 ? 0.7148 0.6888 0.5305 -0.0385 -0.0835 -0.0977 113 GLU A O   
874  C CB  A GLU A 113 ? 0.7287 0.7052 0.4759 -0.0323 -0.0810 -0.1312 113 GLU A CB  
875  C CB  B GLU A 113 ? 0.7288 0.7049 0.4760 -0.0324 -0.0811 -0.1314 113 GLU A CB  
876  C CG  A GLU A 113 ? 0.7561 0.7376 0.4799 -0.0223 -0.0701 -0.1354 113 GLU A CG  
877  C CG  B GLU A 113 ? 0.7360 0.7199 0.4667 -0.0429 -0.0957 -0.1416 113 GLU A CG  
878  C CD  A GLU A 113 ? 0.8539 0.8155 0.5618 -0.0197 -0.0648 -0.1582 113 GLU A CD  
879  C CD  B GLU A 113 ? 0.7473 0.7602 0.4692 -0.0447 -0.1018 -0.1267 113 GLU A CD  
880  O OE1 A GLU A 113 ? 0.8248 0.7830 0.5161 -0.0272 -0.0737 -0.1747 113 GLU A OE1 
881  O OE1 B GLU A 113 ? 0.8478 0.8727 0.5591 -0.0360 -0.0927 -0.1186 113 GLU A OE1 
882  O OE2 A GLU A 113 ? 0.8229 0.7724 0.5362 -0.0102 -0.0517 -0.1596 113 GLU A OE2 
883  O OE2 B GLU A 113 ? 0.6617 0.6860 0.3899 -0.0548 -0.1156 -0.1216 113 GLU A OE2 
884  N N   . GLN A 114 ? 0.6496 0.6403 0.4415 -0.0509 -0.1032 -0.1078 114 GLN A N   
885  C CA  . GLN A 114 ? 0.6619 0.6499 0.4789 -0.0598 -0.1120 -0.1020 114 GLN A CA  
886  C C   . GLN A 114 ? 0.6832 0.6481 0.5189 -0.0588 -0.1063 -0.1066 114 GLN A C   
887  O O   . GLN A 114 ? 0.6560 0.6206 0.5164 -0.0598 -0.1048 -0.0939 114 GLN A O   
888  C CB  . GLN A 114 ? 0.6767 0.6697 0.4852 -0.0717 -0.1282 -0.1116 114 GLN A CB  
889  C CG  . GLN A 114 ? 0.8466 0.8411 0.6827 -0.0816 -0.1385 -0.1034 114 GLN A CG  
890  C CD  . GLN A 114 ? 0.9851 0.9657 0.8204 -0.0924 -0.1501 -0.1210 114 GLN A CD  
891  O OE1 . GLN A 114 ? 0.9546 0.9464 0.7781 -0.1018 -0.1640 -0.1267 114 GLN A OE1 
892  N NE2 . GLN A 114 ? 1.0113 0.9679 0.8601 -0.0916 -0.1449 -0.1294 114 GLN A NE2 
893  N N   . GLN A 115 ? 0.6418 0.5877 0.4667 -0.0565 -0.1024 -0.1243 115 GLN A N   
894  C CA  . GLN A 115 ? 0.6597 0.5836 0.5042 -0.0565 -0.0985 -0.1287 115 GLN A CA  
895  C C   . GLN A 115 ? 0.5785 0.5004 0.4376 -0.0474 -0.0856 -0.1151 115 GLN A C   
896  O O   . GLN A 115 ? 0.5944 0.5033 0.4744 -0.0480 -0.0829 -0.1123 115 GLN A O   
897  C CB  . GLN A 115 ? 0.6592 0.5627 0.4898 -0.0555 -0.0962 -0.1512 115 GLN A CB  
898  C CG  . GLN A 115 ? 0.7649 0.6656 0.5778 -0.0432 -0.0824 -0.1558 115 GLN A CG  
899  C CD  . GLN A 115 ? 0.8455 0.7580 0.6257 -0.0422 -0.0842 -0.1658 115 GLN A CD  
900  O OE1 . GLN A 115 ? 0.8484 0.7783 0.6192 -0.0494 -0.0952 -0.1626 115 GLN A OE1 
901  N NE2 . GLN A 115 ? 0.8999 0.8042 0.6634 -0.0333 -0.0731 -0.1769 115 GLN A NE2 
902  N N   . HIS A 116 ? 0.5449 0.4798 0.3939 -0.0396 -0.0779 -0.1062 116 HIS A N   
903  C CA  . HIS A 116 ? 0.6240 0.5582 0.4848 -0.0318 -0.0666 -0.0944 116 HIS A CA  
904  C C   . HIS A 116 ? 0.6003 0.5454 0.4807 -0.0348 -0.0677 -0.0771 116 HIS A C   
905  O O   . HIS A 116 ? 0.4762 0.4193 0.3684 -0.0305 -0.0597 -0.0681 116 HIS A O   
906  C CB  . HIS A 116 ? 0.6053 0.5479 0.4485 -0.0225 -0.0576 -0.0930 116 HIS A CB  
907  C CG  . HIS A 116 ? 0.7046 0.6358 0.5304 -0.0174 -0.0527 -0.1089 116 HIS A CG  
908  N ND1 . HIS A 116 ? 0.8612 0.8005 0.6619 -0.0159 -0.0538 -0.1174 116 HIS A ND1 
909  C CD2 . HIS A 116 ? 0.7593 0.6719 0.5900 -0.0131 -0.0460 -0.1177 116 HIS A CD2 
910  C CE1 . HIS A 116 ? 0.9226 0.8481 0.7123 -0.0107 -0.0471 -0.1319 116 HIS A CE1 
911  N NE2 . HIS A 116 ? 0.8572 0.7658 0.6661 -0.0087 -0.0422 -0.1322 116 HIS A NE2 
912  N N   . PHE A 117 ? 0.5032 0.4600 0.3877 -0.0420 -0.0772 -0.0722 117 PHE A N   
913  C CA  . PHE A 117 ? 0.5922 0.5600 0.4957 -0.0440 -0.0768 -0.0560 117 PHE A CA  
914  C C   . PHE A 117 ? 0.5637 0.5220 0.4894 -0.0502 -0.0801 -0.0538 117 PHE A C   
915  O O   . PHE A 117 ? 0.5822 0.5454 0.5191 -0.0582 -0.0895 -0.0512 117 PHE A O   
916  C CB  . PHE A 117 ? 0.4733 0.4601 0.3740 -0.0478 -0.0840 -0.0490 117 PHE A CB  
917  C CG  . PHE A 117 ? 0.5222 0.5207 0.4055 -0.0412 -0.0791 -0.0466 117 PHE A CG  
918  C CD1 . PHE A 117 ? 0.3393 0.3444 0.2290 -0.0351 -0.0695 -0.0351 117 PHE A CD1 
919  C CD2 . PHE A 117 ? 0.5466 0.5497 0.4072 -0.0414 -0.0841 -0.0560 117 PHE A CD2 
920  C CE1 . PHE A 117 ? 0.3741 0.3900 0.2508 -0.0293 -0.0649 -0.0317 117 PHE A CE1 
921  C CE2 . PHE A 117 ? 0.5232 0.5386 0.3692 -0.0351 -0.0789 -0.0519 117 PHE A CE2 
922  C CZ  . PHE A 117 ? 0.4961 0.5177 0.3517 -0.0290 -0.0694 -0.0391 117 PHE A CZ  
923  N N   . ILE A 118 ? 0.4042 0.3506 0.3383 -0.0463 -0.0722 -0.0529 118 ILE A N   
924  C CA  . ILE A 118 ? 0.4363 0.3732 0.3921 -0.0511 -0.0740 -0.0499 118 ILE A CA  
925  C C   . ILE A 118 ? 0.4649 0.4073 0.4353 -0.0484 -0.0656 -0.0350 118 ILE A C   
926  O O   . ILE A 118 ? 0.4917 0.4252 0.4754 -0.0483 -0.0620 -0.0318 118 ILE A O   
927  C CB  . ILE A 118 ? 0.4916 0.4088 0.4473 -0.0498 -0.0726 -0.0617 118 ILE A CB  
928  C CG1 . ILE A 118 ? 0.4431 0.3565 0.3898 -0.0399 -0.0612 -0.0614 118 ILE A CG1 
929  C CG2 . ILE A 118 ? 0.4164 0.3266 0.3582 -0.0540 -0.0812 -0.0787 118 ILE A CG2 
930  C CD1 . ILE A 118 ? 0.4420 0.3363 0.3941 -0.0374 -0.0579 -0.0699 118 ILE A CD1 
931  N N   . TYR A 119 ? 0.4082 0.3652 0.3764 -0.0463 -0.0620 -0.0260 119 TYR A N   
932  C CA  . TYR A 119 ? 0.3389 0.3015 0.3169 -0.0436 -0.0531 -0.0141 119 TYR A CA  
933  C C   . TYR A 119 ? 0.3777 0.3535 0.3678 -0.0473 -0.0546 -0.0043 119 TYR A C   
934  O O   . TYR A 119 ? 0.4297 0.4160 0.4154 -0.0443 -0.0504 0.0004  119 TYR A O   
935  C CB  . TYR A 119 ? 0.3086 0.2742 0.2728 -0.0361 -0.0444 -0.0137 119 TYR A CB  
936  C CG  . TYR A 119 ? 0.4088 0.3638 0.3603 -0.0316 -0.0431 -0.0234 119 TYR A CG  
937  C CD1 . TYR A 119 ? 0.3394 0.2831 0.2981 -0.0304 -0.0402 -0.0240 119 TYR A CD1 
938  C CD2 . TYR A 119 ? 0.3827 0.3398 0.3166 -0.0282 -0.0442 -0.0310 119 TYR A CD2 
939  C CE1 . TYR A 119 ? 0.3814 0.3151 0.3318 -0.0257 -0.0380 -0.0322 119 TYR A CE1 
940  C CE2 . TYR A 119 ? 0.4288 0.3761 0.3520 -0.0234 -0.0415 -0.0399 119 TYR A CE2 
941  C CZ  . TYR A 119 ? 0.4651 0.4002 0.3975 -0.0220 -0.0382 -0.0407 119 TYR A CZ  
942  O OH  . TYR A 119 ? 0.4729 0.3977 0.3981 -0.0166 -0.0345 -0.0490 119 TYR A OH  
943  N N   . PRO A 120 ? 0.4196 0.3952 0.4276 -0.0538 -0.0600 -0.0002 120 PRO A N   
944  C CA  . PRO A 120 ? 0.3582 0.3472 0.3804 -0.0573 -0.0619 0.0097  120 PRO A CA  
945  C C   . PRO A 120 ? 0.4263 0.4224 0.4574 -0.0540 -0.0504 0.0204  120 PRO A C   
946  O O   . PRO A 120 ? 0.4173 0.4248 0.4598 -0.0551 -0.0495 0.0286  120 PRO A O   
947  C CB  . PRO A 120 ? 0.3967 0.3821 0.4369 -0.0654 -0.0710 0.0106  120 PRO A CB  
948  C CG  . PRO A 120 ? 0.4056 0.3757 0.4468 -0.0649 -0.0689 0.0057  120 PRO A CG  
949  C CD  . PRO A 120 ? 0.3586 0.3217 0.3779 -0.0578 -0.0638 -0.0031 120 PRO A CD  
950  N N   . THR A 121 ? 0.3638 0.3543 0.3903 -0.0501 -0.0417 0.0207  121 THR A N   
951  C CA  . THR A 121 ? 0.3728 0.3699 0.4022 -0.0469 -0.0304 0.0281  121 THR A CA  
952  C C   . THR A 121 ? 0.3515 0.3454 0.3630 -0.0414 -0.0240 0.0234  121 THR A C   
953  O O   . THR A 121 ? 0.3263 0.3120 0.3272 -0.0396 -0.0270 0.0165  121 THR A O   
954  C CB  . THR A 121 ? 0.3161 0.3132 0.3604 -0.0492 -0.0256 0.0361  121 THR A CB  
955  O OG1 . THR A 121 ? 0.3819 0.3689 0.4226 -0.0489 -0.0267 0.0332  121 THR A OG1 
956  C CG2 . THR A 121 ? 0.3225 0.3236 0.3881 -0.0549 -0.0314 0.0425  121 THR A CG2 
957  N N   . VAL A 122 ? 0.3217 0.3222 0.3316 -0.0388 -0.0150 0.0270  122 VAL A N   
958  C CA  . VAL A 122 ? 0.3411 0.3401 0.3369 -0.0348 -0.0087 0.0239  122 VAL A CA  
959  C C   . VAL A 122 ? 0.4224 0.4159 0.4172 -0.0351 -0.0076 0.0252  122 VAL A C   
960  O O   . VAL A 122 ? 0.3766 0.3657 0.3608 -0.0323 -0.0078 0.0215  122 VAL A O   
961  C CB  . VAL A 122 ? 0.3264 0.3327 0.3229 -0.0335 0.0008  0.0269  122 VAL A CB  
962  C CG1 . VAL A 122 ? 0.3296 0.3351 0.3130 -0.0313 0.0065  0.0243  122 VAL A CG1 
963  C CG2 . VAL A 122 ? 0.2946 0.3059 0.2928 -0.0320 0.0001  0.0264  122 VAL A CG2 
964  N N   . GLU A 123 ? 0.3645 0.3591 0.3723 -0.0384 -0.0063 0.0318  123 GLU A N   
965  C CA  . GLU A 123 ? 0.4153 0.4061 0.4252 -0.0388 -0.0054 0.0356  123 GLU A CA  
966  C C   . GLU A 123 ? 0.3805 0.3603 0.3891 -0.0380 -0.0128 0.0300  123 GLU A C   
967  O O   . GLU A 123 ? 0.3339 0.3100 0.3367 -0.0353 -0.0114 0.0297  123 GLU A O   
968  C CB  . GLU A 123 ? 0.3631 0.3577 0.3902 -0.0426 -0.0035 0.0449  123 GLU A CB  
969  C CG  . GLU A 123 ? 0.4960 0.4913 0.5259 -0.0429 0.0002  0.0525  123 GLU A CG  
970  C CD  . GLU A 123 ? 0.7504 0.7554 0.7684 -0.0415 0.0095  0.0556  123 GLU A CD  
971  O OE1 . GLU A 123 ? 0.8120 0.8234 0.8272 -0.0416 0.0154  0.0544  123 GLU A OE1 
972  O OE2 . GLU A 123 ? 0.7553 0.7617 0.7673 -0.0406 0.0110  0.0591  123 GLU A OE2 
973  N N   . ALA A 124 ? 0.3068 0.2815 0.3215 -0.0406 -0.0207 0.0255  124 ALA A N   
974  C CA  . ALA A 124 ? 0.3757 0.3384 0.3883 -0.0402 -0.0271 0.0175  124 ALA A CA  
975  C C   . ALA A 124 ? 0.3616 0.3220 0.3560 -0.0346 -0.0256 0.0099  124 ALA A C   
976  O O   . ALA A 124 ? 0.3977 0.3493 0.3895 -0.0318 -0.0255 0.0062  124 ALA A O   
977  C CB  . ALA A 124 ? 0.2950 0.2543 0.3143 -0.0451 -0.0365 0.0124  124 ALA A CB  
978  N N   . TYR A 125 ? 0.3361 0.3046 0.3199 -0.0327 -0.0237 0.0083  125 TYR A N   
979  C CA  . TYR A 125 ? 0.3623 0.3307 0.3303 -0.0274 -0.0214 0.0029  125 TYR A CA  
980  C C   . TYR A 125 ? 0.4081 0.3778 0.3733 -0.0241 -0.0148 0.0073  125 TYR A C   
981  O O   . TYR A 125 ? 0.3270 0.2920 0.2858 -0.0200 -0.0139 0.0039  125 TYR A O   
982  C CB  . TYR A 125 ? 0.3373 0.3153 0.2987 -0.0265 -0.0204 0.0027  125 TYR A CB  
983  C CG  . TYR A 125 ? 0.3507 0.3299 0.2977 -0.0212 -0.0180 -0.0015 125 TYR A CG  
984  C CD1 . TYR A 125 ? 0.3414 0.3156 0.2788 -0.0188 -0.0221 -0.0094 125 TYR A CD1 
985  C CD2 . TYR A 125 ? 0.3416 0.3270 0.2848 -0.0187 -0.0114 0.0020  125 TYR A CD2 
986  C CE1 . TYR A 125 ? 0.2806 0.2572 0.2059 -0.0135 -0.0189 -0.0121 125 TYR A CE1 
987  C CE2 . TYR A 125 ? 0.3531 0.3404 0.2857 -0.0141 -0.0093 -0.0005 125 TYR A CE2 
988  C CZ  . TYR A 125 ? 0.4065 0.3898 0.3306 -0.0111 -0.0126 -0.0068 125 TYR A CZ  
989  O OH  . TYR A 125 ? 0.3590 0.3453 0.2736 -0.0060 -0.0096 -0.0084 125 TYR A OH  
990  N N   . ALA A 126 ? 0.3134 0.2903 0.2833 -0.0261 -0.0100 0.0149  126 ALA A N   
991  C CA  . ALA A 126 ? 0.3372 0.3180 0.3032 -0.0244 -0.0048 0.0197  126 ALA A CA  
992  C C   . ALA A 126 ? 0.3822 0.3560 0.3544 -0.0231 -0.0062 0.0224  126 ALA A C   
993  O O   . ALA A 126 ? 0.3813 0.3551 0.3487 -0.0194 -0.0046 0.0230  126 ALA A O   
994  C CB  . ALA A 126 ? 0.3284 0.3181 0.2978 -0.0278 0.0004  0.0266  126 ALA A CB  
995  N N   . HIS A 127 ? 0.3294 0.2976 0.3150 -0.0261 -0.0091 0.0252  127 HIS A N   
996  C CA  . HIS A 127 ? 0.3555 0.3164 0.3509 -0.0248 -0.0098 0.0289  127 HIS A CA  
997  C C   . HIS A 127 ? 0.3749 0.3240 0.3670 -0.0207 -0.0124 0.0192  127 HIS A C   
998  O O   . HIS A 127 ? 0.3804 0.3250 0.3769 -0.0170 -0.0105 0.0217  127 HIS A O   
999  C CB  . HIS A 127 ? 0.4326 0.3901 0.4459 -0.0294 -0.0121 0.0348  127 HIS A CB  
1000 C CG  . HIS A 127 ? 0.3996 0.3695 0.4160 -0.0328 -0.0079 0.0450  127 HIS A CG  
1001 N ND1 . HIS A 127 ? 0.3574 0.3387 0.3651 -0.0318 -0.0023 0.0515  127 HIS A ND1 
1002 C CD2 . HIS A 127 ? 0.3262 0.2997 0.3526 -0.0371 -0.0080 0.0491  127 HIS A CD2 
1003 C CE1 . HIS A 127 ? 0.3675 0.3581 0.3781 -0.0352 0.0016  0.0581  127 HIS A CE1 
1004 N NE2 . HIS A 127 ? 0.4004 0.3866 0.4234 -0.0380 -0.0013 0.0575  127 HIS A NE2 
1005 N N   . ALA A 128 ? 0.3620 0.3069 0.3465 -0.0210 -0.0163 0.0086  128 ALA A N   
1006 C CA  . ALA A 128 ? 0.3621 0.2969 0.3397 -0.0168 -0.0176 -0.0020 128 ALA A CA  
1007 C C   . ALA A 128 ? 0.3786 0.3188 0.3448 -0.0106 -0.0124 -0.0016 128 ALA A C   
1008 O O   . ALA A 128 ? 0.3563 0.2894 0.3235 -0.0057 -0.0101 -0.0040 128 ALA A O   
1009 C CB  . ALA A 128 ? 0.3756 0.3083 0.3450 -0.0193 -0.0234 -0.0125 128 ALA A CB  
1010 N N   . VAL A 129 ? 0.3406 0.2931 0.2980 -0.0108 -0.0102 0.0018  129 VAL A N   
1011 C CA  . VAL A 129 ? 0.3610 0.3200 0.3105 -0.0061 -0.0057 0.0040  129 VAL A CA  
1012 C C   . VAL A 129 ? 0.3864 0.3457 0.3449 -0.0042 -0.0029 0.0126  129 VAL A C   
1013 O O   . VAL A 129 ? 0.3627 0.3191 0.3215 0.0012  -0.0005 0.0121  129 VAL A O   
1014 C CB  . VAL A 129 ? 0.3513 0.3226 0.2938 -0.0082 -0.0038 0.0071  129 VAL A CB  
1015 C CG1 . VAL A 129 ? 0.3121 0.2910 0.2502 -0.0051 0.0002  0.0114  129 VAL A CG1 
1016 C CG2 . VAL A 129 ? 0.2776 0.2502 0.2123 -0.0083 -0.0058 0.0005  129 VAL A CG2 
1017 N N   A GLU A 130 ? 0.3541 0.3182 0.3209 -0.0084 -0.0028 0.0217  130 GLU A N   
1018 N N   B GLU A 130 ? 0.3575 0.3217 0.3242 -0.0085 -0.0028 0.0217  130 GLU A N   
1019 C CA  A GLU A 130 ? 0.3885 0.3571 0.3632 -0.0071 -0.0006 0.0324  130 GLU A CA  
1020 C CA  B GLU A 130 ? 0.3883 0.3568 0.3631 -0.0072 -0.0006 0.0324  130 GLU A CA  
1021 C C   A GLU A 130 ? 0.3974 0.3536 0.3864 -0.0037 -0.0008 0.0331  130 GLU A C   
1022 C C   B GLU A 130 ? 0.3976 0.3534 0.3859 -0.0034 -0.0008 0.0324  130 GLU A C   
1023 O O   A GLU A 130 ? 0.3971 0.3554 0.3931 0.0001  0.0016  0.0404  130 GLU A O   
1024 O O   B GLU A 130 ? 0.3947 0.3520 0.3891 0.0009  0.0018  0.0386  130 GLU A O   
1025 C CB  A GLU A 130 ? 0.3528 0.3320 0.3304 -0.0127 0.0001  0.0423  130 GLU A CB  
1026 C CB  B GLU A 130 ? 0.3521 0.3303 0.3313 -0.0127 -0.0001 0.0427  130 GLU A CB  
1027 C CG  A GLU A 130 ? 0.2942 0.2838 0.2581 -0.0156 0.0017  0.0397  130 GLU A CG  
1028 C CG  B GLU A 130 ? 0.3982 0.3708 0.3885 -0.0168 -0.0021 0.0440  130 GLU A CG  
1029 C CD  A GLU A 130 ? 0.3673 0.3696 0.3294 -0.0202 0.0040  0.0486  130 GLU A CD  
1030 C CD  B GLU A 130 ? 0.3790 0.3639 0.3685 -0.0219 0.0002  0.0524  130 GLU A CD  
1031 O OE1 A GLU A 130 ? 0.4545 0.4575 0.4261 -0.0227 0.0041  0.0560  130 GLU A OE1 
1032 O OE1 B GLU A 130 ? 0.3915 0.3862 0.3680 -0.0231 0.0026  0.0511  130 GLU A OE1 
1033 O OE2 A GLU A 130 ? 0.2832 0.2951 0.2344 -0.0215 0.0059  0.0480  130 GLU A OE2 
1034 O OE2 B GLU A 130 ? 0.2611 0.2459 0.2632 -0.0247 0.0000  0.0601  130 GLU A OE2 
1035 N N   . ALA A 131 ? 0.3790 0.3222 0.3738 -0.0052 -0.0037 0.0253  131 ALA A N   
1036 C CA  . ALA A 131 ? 0.4028 0.3312 0.4113 -0.0018 -0.0033 0.0227  131 ALA A CA  
1037 C C   . ALA A 131 ? 0.4132 0.3360 0.4145 0.0055  0.0000  0.0146  131 ALA A C   
1038 O O   . ALA A 131 ? 0.4853 0.3994 0.4991 0.0103  0.0032  0.0161  131 ALA A O   
1039 C CB  . ALA A 131 ? 0.4296 0.3448 0.4442 -0.0061 -0.0081 0.0137  131 ALA A CB  
1040 N N   . ALA A 132 ? 0.3790 0.3071 0.3620 0.0067  0.0001  0.0069  132 ALA A N   
1041 C CA  . ALA A 132 ? 0.4134 0.3382 0.3886 0.0140  0.0042  -0.0001 132 ALA A CA  
1042 C C   . ALA A 132 ? 0.4866 0.4229 0.4645 0.0184  0.0087  0.0110  132 ALA A C   
1043 O O   . ALA A 132 ? 0.3581 0.2915 0.3360 0.0255  0.0135  0.0084  132 ALA A O   
1044 C CB  . ALA A 132 ? 0.3816 0.3094 0.3376 0.0135  0.0025  -0.0107 132 ALA A CB  
1045 N N   A ARG A 133 ? 0.4244 0.3743 0.4047 0.0143  0.0075  0.0231  133 ARG A N   
1046 N N   B ARG A 133 ? 0.4244 0.3742 0.4048 0.0143  0.0075  0.0231  133 ARG A N   
1047 C CA  A ARG A 133 ? 0.3868 0.3497 0.3702 0.0166  0.0100  0.0346  133 ARG A CA  
1048 C CA  B ARG A 133 ? 0.3862 0.3491 0.3695 0.0166  0.0099  0.0346  133 ARG A CA  
1049 C C   A ARG A 133 ? 0.4207 0.3897 0.3919 0.0205  0.0124  0.0300  133 ARG A C   
1050 C C   B ARG A 133 ? 0.4206 0.3893 0.3917 0.0206  0.0124  0.0298  133 ARG A C   
1051 O O   A ARG A 133 ? 0.4079 0.3770 0.3842 0.0271  0.0166  0.0323  133 ARG A O   
1052 O O   B ARG A 133 ? 0.4081 0.3767 0.3844 0.0273  0.0166  0.0318  133 ARG A O   
1053 C CB  A ARG A 133 ? 0.4541 0.4119 0.4566 0.0217  0.0129  0.0429  133 ARG A CB  
1054 C CB  B ARG A 133 ? 0.4538 0.4121 0.4563 0.0216  0.0129  0.0432  133 ARG A CB  
1055 C CG  A ARG A 133 ? 0.4667 0.4171 0.4849 0.0183  0.0110  0.0482  133 ARG A CG  
1056 C CG  B ARG A 133 ? 0.4592 0.4136 0.4771 0.0176  0.0107  0.0512  133 ARG A CG  
1057 C CD  A ARG A 133 ? 0.5093 0.4577 0.5501 0.0231  0.0142  0.0604  133 ARG A CD  
1058 C CD  B ARG A 133 ? 0.5060 0.4579 0.5464 0.0227  0.0140  0.0629  133 ARG A CD  
1059 N NE  A ARG A 133 ? 0.6352 0.5730 0.6814 0.0319  0.0198  0.0539  133 ARG A NE  
1060 N NE  B ARG A 133 ? 0.6275 0.5629 0.6751 0.0305  0.0189  0.0532  133 ARG A NE  
1061 C CZ  A ARG A 133 ? 0.7044 0.6222 0.7603 0.0357  0.0228  0.0439  133 ARG A CZ  
1062 C CZ  B ARG A 133 ? 0.6172 0.5545 0.6728 0.0382  0.0243  0.0578  133 ARG A CZ  
1063 N NH1 A ARG A 133 ? 0.5790 0.4848 0.6418 0.0309  0.0195  0.0394  133 ARG A NH1 
1064 N NH1 B ARG A 133 ? 0.3653 0.3213 0.4246 0.0386  0.0242  0.0731  133 ARG A NH1 
1065 N NH2 A ARG A 133 ? 0.7140 0.6236 0.7734 0.0443  0.0295  0.0378  133 ARG A NH2 
1066 N NH2 B ARG A 133 ? 0.6849 0.6055 0.7454 0.0454  0.0301  0.0465  133 ARG A NH2 
1067 N N   . PRO A 134 ? 0.3955 0.3699 0.3527 0.0169  0.0106  0.0246  134 PRO A N   
1068 C CA  . PRO A 134 ? 0.4081 0.3883 0.3556 0.0206  0.0131  0.0211  134 PRO A CA  
1069 C C   . PRO A 134 ? 0.4134 0.4077 0.3646 0.0207  0.0142  0.0318  134 PRO A C   
1070 O O   . PRO A 134 ? 0.3382 0.3402 0.2951 0.0163  0.0121  0.0410  134 PRO A O   
1071 C CB  . PRO A 134 ? 0.3287 0.3112 0.2645 0.0157  0.0104  0.0149  134 PRO A CB  
1072 C CG  . PRO A 134 ? 0.3996 0.3848 0.3396 0.0086  0.0074  0.0199  134 PRO A CG  
1073 C CD  . PRO A 134 ? 0.3548 0.3318 0.3070 0.0096  0.0069  0.0235  134 PRO A CD  
1074 N N   . SER A 135 ? 0.3507 0.3498 0.2988 0.0255  0.0175  0.0310  135 SER A N   
1075 C CA  . SER A 135 ? 0.3492 0.3625 0.3024 0.0256  0.0181  0.0410  135 SER A CA  
1076 C C   . SER A 135 ? 0.3395 0.3633 0.2848 0.0187  0.0154  0.0413  135 SER A C   
1077 O O   . SER A 135 ? 0.4312 0.4674 0.3805 0.0162  0.0142  0.0491  135 SER A O   
1078 C CB  . SER A 135 ? 0.3681 0.3824 0.3244 0.0342  0.0237  0.0413  135 SER A CB  
1079 O OG  . SER A 135 ? 0.3675 0.3713 0.3328 0.0410  0.0276  0.0407  135 SER A OG  
1080 N N   . LEU A 136 ? 0.2994 0.3189 0.2353 0.0156  0.0143  0.0330  136 LEU A N   
1081 C CA  . LEU A 136 ? 0.3306 0.3575 0.2613 0.0090  0.0127  0.0324  136 LEU A CA  
1082 C C   . LEU A 136 ? 0.3502 0.3715 0.2768 0.0037  0.0107  0.0277  136 LEU A C   
1083 O O   . LEU A 136 ? 0.3358 0.3477 0.2631 0.0053  0.0101  0.0244  136 LEU A O   
1084 C CB  . LEU A 136 ? 0.3173 0.3471 0.2443 0.0115  0.0151  0.0291  136 LEU A CB  
1085 C CG  . LEU A 136 ? 0.3252 0.3479 0.2481 0.0188  0.0178  0.0237  136 LEU A CG  
1086 C CD1 . LEU A 136 ? 0.3120 0.3253 0.2289 0.0168  0.0155  0.0162  136 LEU A CD1 
1087 C CD2 . LEU A 136 ? 0.3412 0.3710 0.2623 0.0217  0.0207  0.0245  136 LEU A CD2 
1088 N N   . ASN A 137 ? 0.2903 0.3173 0.2138 -0.0025 0.0102  0.0271  137 ASN A N   
1089 C CA  . ASN A 137 ? 0.3135 0.3367 0.2347 -0.0072 0.0097  0.0236  137 ASN A CA  
1090 C C   . ASN A 137 ? 0.3556 0.3728 0.2747 -0.0055 0.0104  0.0172  137 ASN A C   
1091 O O   . ASN A 137 ? 0.3256 0.3444 0.2434 -0.0021 0.0116  0.0156  137 ASN A O   
1092 C CB  . ASN A 137 ? 0.2859 0.3167 0.2044 -0.0143 0.0104  0.0241  137 ASN A CB  
1093 C CG  . ASN A 137 ? 0.3497 0.3897 0.2684 -0.0173 0.0085  0.0309  137 ASN A CG  
1094 O OD1 . ASN A 137 ? 0.3420 0.3823 0.2629 -0.0176 0.0071  0.0363  137 ASN A OD1 
1095 N ND2 . ASN A 137 ? 0.3099 0.3584 0.2274 -0.0201 0.0081  0.0317  137 ASN A ND2 
1096 N N   . VAL A 138 ? 0.3232 0.3356 0.2433 -0.0081 0.0095  0.0151  138 VAL A N   
1097 C CA  . VAL A 138 ? 0.3196 0.3281 0.2394 -0.0075 0.0088  0.0107  138 VAL A CA  
1098 C C   . VAL A 138 ? 0.3297 0.3395 0.2527 -0.0127 0.0102  0.0106  138 VAL A C   
1099 O O   . VAL A 138 ? 0.3275 0.3364 0.2530 -0.0158 0.0102  0.0127  138 VAL A O   
1100 C CB  . VAL A 138 ? 0.3311 0.3311 0.2512 -0.0049 0.0055  0.0079  138 VAL A CB  
1101 C CG1 . VAL A 138 ? 0.2944 0.2929 0.2143 -0.0058 0.0033  0.0043  138 VAL A CG1 
1102 C CG2 . VAL A 138 ? 0.2935 0.2909 0.2105 0.0011  0.0058  0.0066  138 VAL A CG2 
1103 N N   . GLY A 139 ? 0.3338 0.3462 0.2585 -0.0132 0.0123  0.0091  139 GLY A N   
1104 C CA  . GLY A 139 ? 0.2755 0.2879 0.2062 -0.0166 0.0143  0.0089  139 GLY A CA  
1105 C C   . GLY A 139 ? 0.3267 0.3390 0.2614 -0.0146 0.0122  0.0087  139 GLY A C   
1106 O O   . GLY A 139 ? 0.3005 0.3146 0.2318 -0.0110 0.0108  0.0085  139 GLY A O   
1107 N N   . THR A 140 ? 0.2858 0.2977 0.2280 -0.0169 0.0120  0.0099  140 THR A N   
1108 C CA  . THR A 140 ? 0.3016 0.3153 0.2480 -0.0157 0.0083  0.0112  140 THR A CA  
1109 C C   . THR A 140 ? 0.3030 0.3210 0.2618 -0.0172 0.0123  0.0148  140 THR A C   
1110 O O   . THR A 140 ? 0.2920 0.3092 0.2577 -0.0199 0.0167  0.0155  140 THR A O   
1111 C CB  . THR A 140 ? 0.3009 0.3105 0.2476 -0.0170 0.0018  0.0103  140 THR A CB  
1112 O OG1 . THR A 140 ? 0.2718 0.2848 0.2195 -0.0164 -0.0035 0.0110  140 THR A OG1 
1113 C CG2 . THR A 140 ? 0.2870 0.2955 0.2438 -0.0211 0.0036  0.0131  140 THR A CG2 
1114 N N   . LEU A 141 ? 0.3045 0.3277 0.2670 -0.0150 0.0114  0.0178  141 LEU A N   
1115 C CA  . LEU A 141 ? 0.2763 0.3045 0.2539 -0.0159 0.0130  0.0234  141 LEU A CA  
1116 C C   . LEU A 141 ? 0.2934 0.3238 0.2736 -0.0175 0.0050  0.0257  141 LEU A C   
1117 O O   . LEU A 141 ? 0.3216 0.3490 0.2906 -0.0176 -0.0018 0.0219  141 LEU A O   
1118 C CB  . LEU A 141 ? 0.2587 0.2934 0.2416 -0.0130 0.0150  0.0279  141 LEU A CB  
1119 C CG  . LEU A 141 ? 0.2940 0.3265 0.2774 -0.0123 0.0225  0.0256  141 LEU A CG  
1120 C CD1 . LEU A 141 ? 0.3101 0.3486 0.2930 -0.0088 0.0218  0.0298  141 LEU A CD1 
1121 C CD2 . LEU A 141 ? 0.2496 0.2804 0.2487 -0.0141 0.0312  0.0261  141 LEU A CD2 
1122 N N   . ILE A 142 ? 0.2741 0.3096 0.2706 -0.0189 0.0059  0.0320  142 ILE A N   
1123 C CA  . ILE A 142 ? 0.2873 0.3273 0.2894 -0.0214 -0.0026 0.0358  142 ILE A CA  
1124 C C   . ILE A 142 ? 0.2669 0.3178 0.2731 -0.0199 -0.0068 0.0427  142 ILE A C   
1125 O O   . ILE A 142 ? 0.3163 0.3725 0.3354 -0.0178 -0.0006 0.0492  142 ILE A O   
1126 C CB  . ILE A 142 ? 0.3737 0.4143 0.3934 -0.0243 0.0006  0.0403  142 ILE A CB  
1127 C CG1 . ILE A 142 ? 0.3282 0.3599 0.3422 -0.0259 0.0043  0.0349  142 ILE A CG1 
1128 C CG2 . ILE A 142 ? 0.2540 0.3011 0.2825 -0.0278 -0.0095 0.0456  142 ILE A CG2 
1129 C CD1 . ILE A 142 ? 0.2904 0.3158 0.2898 -0.0271 -0.0039 0.0289  142 ILE A CD1 
1130 N N   . GLY A 143 ? 0.3424 0.3969 0.3378 -0.0211 -0.0171 0.0413  143 GLY A N   
1131 C CA  . GLY A 143 ? 0.2946 0.3620 0.2899 -0.0200 -0.0222 0.0482  143 GLY A CA  
1132 C C   . GLY A 143 ? 0.2967 0.3758 0.3117 -0.0228 -0.0264 0.0594  143 GLY A C   
1133 O O   . GLY A 143 ? 0.3062 0.3859 0.3244 -0.0276 -0.0341 0.0589  143 GLY A O   
1134 N N   . HIS A 144 ? 0.2766 0.3504 0.2389 0.0076  0.0011  -0.0062 144 HIS A N   
1135 C CA  . HIS A 144 ? 0.3187 0.4025 0.2789 0.0090  -0.0022 -0.0061 144 HIS A CA  
1136 C C   . HIS A 144 ? 0.3187 0.4111 0.2771 0.0054  -0.0032 -0.0118 144 HIS A C   
1137 O O   . HIS A 144 ? 0.3264 0.4273 0.2882 0.0034  -0.0051 -0.0144 144 HIS A O   
1138 C CB  . HIS A 144 ? 0.2981 0.3821 0.2524 0.0141  -0.0039 -0.0008 144 HIS A CB  
1139 C CG  . HIS A 144 ? 0.4032 0.4985 0.3558 0.0164  -0.0076 0.0002  144 HIS A CG  
1140 N ND1 . HIS A 144 ? 0.2917 0.3901 0.2376 0.0197  -0.0095 0.0041  144 HIS A ND1 
1141 C CD2 . HIS A 144 ? 0.3253 0.4304 0.2828 0.0160  -0.0098 -0.0014 144 HIS A CD2 
1142 C CE1 . HIS A 144 ? 0.3096 0.4195 0.2567 0.0218  -0.0133 0.0052  144 HIS A CE1 
1143 N NE2 . HIS A 144 ? 0.3806 0.4952 0.3351 0.0195  -0.0135 0.0014  144 HIS A NE2 
1144 N N   . THR A 145 ? 0.2955 0.3864 0.2485 0.0042  -0.0015 -0.0142 145 THR A N   
1145 C CA  . THR A 145 ? 0.2959 0.3953 0.2455 0.0000  -0.0022 -0.0207 145 THR A CA  
1146 C C   . THR A 145 ? 0.3596 0.4578 0.3171 -0.0055 -0.0001 -0.0279 145 THR A C   
1147 O O   . THR A 145 ? 0.3387 0.4464 0.2964 -0.0095 -0.0019 -0.0334 145 THR A O   
1148 C CB  . THR A 145 ? 0.3978 0.4951 0.3395 -0.0004 0.0004  -0.0222 145 THR A CB  
1149 O OG1 . THR A 145 ? 0.3376 0.4333 0.2734 0.0045  -0.0007 -0.0144 145 THR A OG1 
1150 C CG2 . THR A 145 ? 0.2904 0.3991 0.2253 -0.0046 -0.0010 -0.0288 145 THR A CG2 
1151 N N   . ALA A 146 ? 0.3408 0.4278 0.3054 -0.0060 0.0035  -0.0276 146 ALA A N   
1152 C CA  . ALA A 146 ? 0.3671 0.4514 0.3406 -0.0109 0.0057  -0.0327 146 ALA A CA  
1153 C C   . ALA A 146 ? 0.3738 0.4654 0.3517 -0.0123 0.0027  -0.0315 146 ALA A C   
1154 O O   . ALA A 146 ? 0.3692 0.4656 0.3512 -0.0176 0.0027  -0.0375 146 ALA A O   
1155 C CB  . ALA A 146 ? 0.3161 0.3875 0.2971 -0.0102 0.0095  -0.0303 146 ALA A CB  
1156 N N   . LEU A 147 ? 0.3406 0.4335 0.3181 -0.0079 0.0006  -0.0245 147 LEU A N   
1157 C CA  . LEU A 147 ? 0.2797 0.3814 0.2612 -0.0085 -0.0018 -0.0234 147 LEU A CA  
1158 C C   . LEU A 147 ? 0.3270 0.4435 0.3058 -0.0095 -0.0056 -0.0269 147 LEU A C   
1159 O O   . LEU A 147 ? 0.3291 0.4541 0.3135 -0.0139 -0.0066 -0.0307 147 LEU A O   
1160 C CB  . LEU A 147 ? 0.2874 0.3879 0.2680 -0.0030 -0.0027 -0.0162 147 LEU A CB  
1161 C CG  . LEU A 147 ? 0.4101 0.4999 0.3934 -0.0024 -0.0001 -0.0121 147 LEU A CG  
1162 C CD1 . LEU A 147 ? 0.3350 0.4261 0.3161 0.0024  -0.0012 -0.0070 147 LEU A CD1 
1163 C CD2 . LEU A 147 ? 0.3471 0.4352 0.3383 -0.0075 0.0020  -0.0134 147 LEU A CD2 
1164 N N   . ARG A 148 ? 0.3364 0.4569 0.3068 -0.0056 -0.0081 -0.0248 148 ARG A N   
1165 C CA  . ARG A 148 ? 0.3124 0.4481 0.2791 -0.0066 -0.0125 -0.0273 148 ARG A CA  
1166 C C   . ARG A 148 ? 0.3273 0.4674 0.2961 -0.0146 -0.0117 -0.0367 148 ARG A C   
1167 O O   . ARG A 148 ? 0.3669 0.5198 0.3398 -0.0183 -0.0146 -0.0402 148 ARG A O   
1168 C CB  . ARG A 148 ? 0.3407 0.4777 0.2966 -0.0026 -0.0142 -0.0239 148 ARG A CB  
1169 C CG  . ARG A 148 ? 0.4006 0.5343 0.3546 0.0052  -0.0154 -0.0147 148 ARG A CG  
1170 C CD  . ARG A 148 ? 0.2602 0.3975 0.2040 0.0087  -0.0178 -0.0103 148 ARG A CD  
1171 N NE  . ARG A 148 ? 0.4189 0.5691 0.3633 0.0131  -0.0231 -0.0053 148 ARG A NE  
1172 C CZ  . ARG A 148 ? 0.4314 0.5964 0.3708 0.0122  -0.0277 -0.0055 148 ARG A CZ  
1173 N NH1 . ARG A 148 ? 0.3509 0.5194 0.2823 0.0065  -0.0275 -0.0112 148 ARG A NH1 
1174 N NH2 . ARG A 148 ? 0.3643 0.5416 0.3071 0.0171  -0.0328 0.0000  148 ARG A NH2 
1175 N N   . ASN A 149 ? 0.3747 0.5040 0.3417 -0.0177 -0.0074 -0.0415 149 ASN A N   
1176 C CA  . ASN A 149 ? 0.3637 0.4954 0.3320 -0.0255 -0.0058 -0.0519 149 ASN A CA  
1177 C C   . ASN A 149 ? 0.3905 0.5216 0.3706 -0.0309 -0.0044 -0.0554 149 ASN A C   
1178 O O   . ASN A 149 ? 0.3882 0.5272 0.3706 -0.0379 -0.0052 -0.0637 149 ASN A O   
1179 C CB  . ASN A 149 ? 0.3585 0.4774 0.3242 -0.0266 -0.0003 -0.0560 149 ASN A CB  
1180 C CG  . ASN A 149 ? 0.4623 0.5843 0.4269 -0.0342 0.0018  -0.0680 149 ASN A CG  
1181 O OD1 . ASN A 149 ? 0.4423 0.5780 0.3986 -0.0369 -0.0018 -0.0722 149 ASN A OD1 
1182 N ND2 . ASN A 149 ? 0.3344 0.4435 0.3072 -0.0378 0.0075  -0.0737 149 ASN A ND2 
1183 N N   . ASN A 150 ? 0.3270 0.4489 0.3141 -0.0285 -0.0023 -0.0494 150 ASN A N   
1184 C CA  . ASN A 150 ? 0.3704 0.4919 0.3683 -0.0336 -0.0007 -0.0511 150 ASN A CA  
1185 C C   . ASN A 150 ? 0.3682 0.5074 0.3688 -0.0353 -0.0052 -0.0515 150 ASN A C   
1186 O O   . ASN A 150 ? 0.3395 0.4828 0.3486 -0.0419 -0.0043 -0.0558 150 ASN A O   
1187 C CB  . ASN A 150 ? 0.3407 0.4510 0.3437 -0.0304 0.0020  -0.0431 150 ASN A CB  
1188 C CG  . ASN A 150 ? 0.3681 0.4619 0.3720 -0.0294 0.0064  -0.0423 150 ASN A CG  
1189 O OD1 . ASN A 150 ? 0.3469 0.4355 0.3509 -0.0324 0.0089  -0.0490 150 ASN A OD1 
1190 N ND2 . ASN A 150 ? 0.3181 0.4042 0.3230 -0.0251 0.0073  -0.0342 150 ASN A ND2 
1191 N N   . HIS A 151 ? 0.3563 0.5064 0.3513 -0.0293 -0.0098 -0.0466 151 HIS A N   
1192 C CA  . HIS A 151 ? 0.3369 0.5034 0.3373 -0.0288 -0.0137 -0.0449 151 HIS A CA  
1193 C C   . HIS A 151 ? 0.3535 0.5386 0.3495 -0.0289 -0.0197 -0.0473 151 HIS A C   
1194 O O   . HIS A 151 ? 0.3805 0.5818 0.3831 -0.0296 -0.0233 -0.0471 151 HIS A O   
1195 C CB  . HIS A 151 ? 0.3084 0.4727 0.3095 -0.0208 -0.0136 -0.0357 151 HIS A CB  
1196 C CG  . HIS A 151 ? 0.3432 0.4956 0.3500 -0.0220 -0.0087 -0.0331 151 HIS A CG  
1197 N ND1 . HIS A 151 ? 0.3364 0.4950 0.3523 -0.0254 -0.0074 -0.0330 151 HIS A ND1 
1198 C CD2 . HIS A 151 ? 0.3142 0.4499 0.3187 -0.0207 -0.0050 -0.0301 151 HIS A CD2 
1199 C CE1 . HIS A 151 ? 0.3027 0.4486 0.3206 -0.0261 -0.0031 -0.0295 151 HIS A CE1 
1200 N NE2 . HIS A 151 ? 0.3259 0.4582 0.3373 -0.0231 -0.0019 -0.0277 151 HIS A NE2 
1201 N N   . MET A 152 ? 0.4055 0.5900 0.3910 -0.0284 -0.0211 -0.0494 152 MET A N   
1202 C CA  . MET A 152 ? 0.3326 0.5350 0.3118 -0.0278 -0.0274 -0.0498 152 MET A CA  
1203 C C   . MET A 152 ? 0.4164 0.6237 0.3911 -0.0369 -0.0276 -0.0609 152 MET A C   
1204 O O   . MET A 152 ? 0.3750 0.5680 0.3462 -0.0401 -0.0225 -0.0662 152 MET A O   
1205 C CB  . MET A 152 ? 0.2993 0.4982 0.2678 -0.0194 -0.0290 -0.0418 152 MET A CB  
1206 C CG  . MET A 152 ? 0.3068 0.5006 0.2789 -0.0105 -0.0288 -0.0318 152 MET A CG  
1207 S SD  . MET A 152 ? 0.3764 0.5641 0.3363 -0.0023 -0.0299 -0.0233 152 MET A SD  
1208 C CE  . MET A 152 ? 0.3671 0.5795 0.3231 -0.0006 -0.0385 -0.0206 152 MET A CE  
1209 N N   . ASP A 153 ? 0.4798 0.7080 0.4551 -0.0411 -0.0335 -0.0648 153 ASP A N   
1210 C CA  . ASP A 153 ? 0.4934 0.7286 0.4626 -0.0503 -0.0343 -0.0762 153 ASP A CA  
1211 C C   . ASP A 153 ? 0.4822 0.7173 0.4350 -0.0478 -0.0353 -0.0754 153 ASP A C   
1212 O O   . ASP A 153 ? 0.4668 0.6989 0.4126 -0.0546 -0.0325 -0.0854 153 ASP A O   
1213 C CB  . ASP A 153 ? 0.5875 0.8474 0.5621 -0.0560 -0.0410 -0.0804 153 ASP A CB  
1214 C CG  . ASP A 153 ? 0.7316 0.9904 0.7212 -0.0636 -0.0380 -0.0867 153 ASP A CG  
1215 O OD1 . ASP A 153 ? 0.8130 1.0528 0.8056 -0.0682 -0.0308 -0.0924 153 ASP A OD1 
1216 O OD2 . ASP A 153 ? 0.8150 1.0919 0.8141 -0.0649 -0.0426 -0.0855 153 ASP A OD2 
1217 N N   . ASP A 154 ? 0.4072 0.6452 0.3539 -0.0385 -0.0387 -0.0640 154 ASP A N   
1218 C CA  A ASP A 154 ? 0.4501 0.6856 0.3814 -0.0357 -0.0386 -0.0612 154 ASP A CA  
1219 C CA  B ASP A 154 ? 0.4502 0.6862 0.3815 -0.0356 -0.0388 -0.0611 154 ASP A CA  
1220 C C   . ASP A 154 ? 0.3920 0.6162 0.3224 -0.0249 -0.0376 -0.0482 154 ASP A C   
1221 O O   . ASP A 154 ? 0.3665 0.5938 0.3049 -0.0187 -0.0403 -0.0402 154 ASP A O   
1222 C CB  A ASP A 154 ? 0.4731 0.7320 0.3939 -0.0380 -0.0464 -0.0616 154 ASP A CB  
1223 C CB  B ASP A 154 ? 0.4725 0.7321 0.3938 -0.0376 -0.0468 -0.0610 154 ASP A CB  
1224 C CG  A ASP A 154 ? 0.5006 0.7774 0.4278 -0.0321 -0.0545 -0.0520 154 ASP A CG  
1225 C CG  B ASP A 154 ? 0.4925 0.7722 0.4237 -0.0358 -0.0545 -0.0565 154 ASP A CG  
1226 O OD1 A ASP A 154 ? 0.5340 0.8142 0.4758 -0.0326 -0.0550 -0.0528 154 ASP A OD1 
1227 O OD1 B ASP A 154 ? 0.4974 0.7757 0.4348 -0.0264 -0.0561 -0.0452 154 ASP A OD1 
1228 O OD2 A ASP A 154 ? 0.4665 0.7540 0.3845 -0.0268 -0.0599 -0.0432 154 ASP A OD2 
1229 O OD2 B ASP A 154 ? 0.5069 0.8041 0.4403 -0.0438 -0.0586 -0.0648 154 ASP A OD2 
1230 N N   . LEU A 155 ? 0.4335 0.6445 0.3545 -0.0231 -0.0331 -0.0470 155 LEU A N   
1231 C CA  . LEU A 155 ? 0.3548 0.5517 0.2753 -0.0146 -0.0306 -0.0366 155 LEU A CA  
1232 C C   . LEU A 155 ? 0.4494 0.6538 0.3608 -0.0078 -0.0352 -0.0256 155 LEU A C   
1233 O O   . LEU A 155 ? 0.3453 0.5395 0.2585 -0.0005 -0.0340 -0.0163 155 LEU A O   
1234 C CB  . LEU A 155 ? 0.3070 0.4862 0.2240 -0.0164 -0.0229 -0.0406 155 LEU A CB  
1235 C CG  . LEU A 155 ? 0.4556 0.6238 0.3835 -0.0214 -0.0177 -0.0490 155 LEU A CG  
1236 C CD1 . LEU A 155 ? 0.4180 0.5723 0.3428 -0.0236 -0.0106 -0.0543 155 LEU A CD1 
1237 C CD2 . LEU A 155 ? 0.3383 0.4982 0.2776 -0.0166 -0.0172 -0.0424 155 LEU A CD2 
1238 N N   . PHE A 156 ? 0.3822 0.6040 0.2839 -0.0103 -0.0406 -0.0261 156 PHE A N   
1239 C CA  . PHE A 156 ? 0.4734 0.7005 0.3637 -0.0048 -0.0440 -0.0153 156 PHE A CA  
1240 C C   . PHE A 156 ? 0.4221 0.6627 0.3179 0.0023  -0.0516 -0.0048 156 PHE A C   
1241 O O   . PHE A 156 ? 0.3329 0.5888 0.2203 0.0040  -0.0578 0.0016  156 PHE A O   
1242 C CB  . PHE A 156 ? 0.3582 0.5961 0.2327 -0.0115 -0.0450 -0.0209 156 PHE A CB  
1243 C CG  . PHE A 156 ? 0.4717 0.6958 0.3424 -0.0176 -0.0365 -0.0316 156 PHE A CG  
1244 C CD1 . PHE A 156 ? 0.3696 0.5764 0.2374 -0.0140 -0.0301 -0.0272 156 PHE A CD1 
1245 C CD2 . PHE A 156 ? 0.3673 0.5952 0.2397 -0.0267 -0.0346 -0.0461 156 PHE A CD2 
1246 C CE1 . PHE A 156 ? 0.4354 0.6304 0.3020 -0.0187 -0.0222 -0.0366 156 PHE A CE1 
1247 C CE2 . PHE A 156 ? 0.4126 0.6268 0.2836 -0.0313 -0.0262 -0.0558 156 PHE A CE2 
1248 C CZ  . PHE A 156 ? 0.4089 0.6072 0.2774 -0.0269 -0.0201 -0.0508 156 PHE A CZ  
1249 N N   . ARG A 157 ? 0.3855 0.6202 0.2957 0.0069  -0.0508 -0.0024 157 ARG A N   
1250 C CA  . ARG A 157 ? 0.3083 0.5543 0.2274 0.0143  -0.0566 0.0066  157 ARG A CA  
1251 C C   . ARG A 157 ? 0.3684 0.5990 0.2998 0.0199  -0.0520 0.0093  157 ARG A C   
1252 O O   . ARG A 157 ? 0.3938 0.6088 0.3274 0.0165  -0.0457 0.0032  157 ARG A O   
1253 C CB  . ARG A 157 ? 0.3155 0.5841 0.2415 0.0097  -0.0627 0.0009  157 ARG A CB  
1254 C CG  . ARG A 157 ? 0.3346 0.5989 0.2689 0.0014  -0.0584 -0.0117 157 ARG A CG  
1255 C CD  . ARG A 157 ? 0.3744 0.6600 0.3201 -0.0017 -0.0639 -0.0154 157 ARG A CD  
1256 N NE  . ARG A 157 ? 0.4169 0.6981 0.3701 -0.0107 -0.0595 -0.0273 157 ARG A NE  
1257 C CZ  . ARG A 157 ? 0.4093 0.6816 0.3753 -0.0097 -0.0552 -0.0281 157 ARG A CZ  
1258 N NH1 . ARG A 157 ? 0.2987 0.5663 0.2717 -0.0005 -0.0544 -0.0191 157 ARG A NH1 
1259 N NH2 . ARG A 157 ? 0.3325 0.6000 0.3042 -0.0185 -0.0510 -0.0382 157 ARG A NH2 
1260 N N   . PRO A 158 ? 0.3453 0.5800 0.2849 0.0286  -0.0550 0.0183  158 PRO A N   
1261 C CA  . PRO A 158 ? 0.3231 0.5466 0.2752 0.0328  -0.0506 0.0187  158 PRO A CA  
1262 C C   . PRO A 158 ? 0.3556 0.5858 0.3175 0.0263  -0.0497 0.0090  158 PRO A C   
1263 O O   . PRO A 158 ? 0.3382 0.5863 0.3015 0.0211  -0.0542 0.0043  158 PRO A O   
1264 C CB  . PRO A 158 ? 0.3460 0.5772 0.3057 0.0431  -0.0547 0.0293  158 PRO A CB  
1265 C CG  . PRO A 158 ? 0.3212 0.5606 0.2694 0.0455  -0.0601 0.0375  158 PRO A CG  
1266 C CD  . PRO A 158 ? 0.3346 0.5841 0.2726 0.0354  -0.0620 0.0290  158 PRO A CD  
1267 N N   . ALA A 159 ? 0.2864 0.5021 0.2543 0.0257  -0.0436 0.0060  159 ALA A N   
1268 C CA  . ALA A 159 ? 0.3584 0.5791 0.3365 0.0200  -0.0419 -0.0015 159 ALA A CA  
1269 C C   . ALA A 159 ? 0.2605 0.4950 0.2519 0.0253  -0.0443 0.0018  159 ALA A C   
1270 O O   . ALA A 159 ? 0.3320 0.5647 0.3260 0.0344  -0.0449 0.0095  159 ALA A O   
1271 C CB  . ALA A 159 ? 0.3210 0.5221 0.3000 0.0174  -0.0348 -0.0049 159 ALA A CB  
1272 N N   . ASN A 160 ? 0.2762 0.5243 0.2768 0.0195  -0.0453 -0.0043 160 ASN A N   
1273 C CA  . ASN A 160 ? 0.3115 0.5737 0.3266 0.0239  -0.0465 -0.0020 160 ASN A CA  
1274 C C   . ASN A 160 ? 0.3015 0.5510 0.3232 0.0242  -0.0393 -0.0036 160 ASN A C   
1275 O O   . ASN A 160 ? 0.3344 0.5657 0.3498 0.0205  -0.0342 -0.0061 160 ASN A O   
1276 C CB  . ASN A 160 ? 0.2540 0.5399 0.2770 0.0174  -0.0515 -0.0073 160 ASN A CB  
1277 C CG  . ASN A 160 ? 0.3705 0.6528 0.3951 0.0058  -0.0477 -0.0171 160 ASN A CG  
1278 O OD1 . ASN A 160 ? 0.3372 0.6058 0.3651 0.0039  -0.0412 -0.0190 160 ASN A OD1 
1279 N ND2 . ASN A 160 ? 0.2576 0.5523 0.2797 -0.0024 -0.0519 -0.0234 160 ASN A ND2 
1280 N N   A GLU A 161 ? 0.2959 0.5561 0.3304 0.0290  -0.0388 -0.0017 161 GLU A N   
1281 N N   B GLU A 161 ? 0.2958 0.5562 0.3306 0.0285  -0.0386 -0.0021 161 GLU A N   
1282 C CA  A GLU A 161 ? 0.3117 0.5620 0.3517 0.0298  -0.0317 -0.0028 161 GLU A CA  
1283 C CA  B GLU A 161 ? 0.3120 0.5611 0.3514 0.0299  -0.0315 -0.0027 161 GLU A CA  
1284 C C   A GLU A 161 ? 0.3225 0.5670 0.3619 0.0191  -0.0277 -0.0095 161 GLU A C   
1285 C C   B GLU A 161 ? 0.3196 0.5660 0.3612 0.0196  -0.0273 -0.0094 161 GLU A C   
1286 O O   A GLU A 161 ? 0.3097 0.5366 0.3439 0.0176  -0.0224 -0.0100 161 GLU A O   
1287 O O   B GLU A 161 ? 0.3038 0.5358 0.3434 0.0187  -0.0214 -0.0098 161 GLU A O   
1288 C CB  A GLU A 161 ? 0.2870 0.5535 0.3423 0.0354  -0.0314 -0.0013 161 GLU A CB  
1289 C CB  B GLU A 161 ? 0.3031 0.5646 0.3558 0.0382  -0.0312 0.0006  161 GLU A CB  
1290 C CG  A GLU A 161 ? 0.3628 0.6259 0.4245 0.0315  -0.0242 -0.0053 161 GLU A CG  
1291 C CG  B GLU A 161 ? 0.3005 0.5569 0.3512 0.0496  -0.0330 0.0083  161 GLU A CG  
1292 C CD  A GLU A 161 ? 0.3694 0.6471 0.4462 0.0377  -0.0221 -0.0042 161 GLU A CD  
1293 C CD  B GLU A 161 ? 0.3664 0.6348 0.4321 0.0589  -0.0324 0.0116  161 GLU A CD  
1294 O OE1 A GLU A 161 ? 0.4097 0.6993 0.4934 0.0461  -0.0263 0.0001  161 GLU A OE1 
1295 O OE1 B GLU A 161 ? 0.3955 0.6718 0.4719 0.0570  -0.0282 0.0074  161 GLU A OE1 
1296 O OE2 A GLU A 161 ? 0.3600 0.6374 0.4418 0.0343  -0.0159 -0.0075 161 GLU A OE2 
1297 O OE2 B GLU A 161 ? 0.3404 0.6103 0.4079 0.0683  -0.0356 0.0186  161 GLU A OE2 
1298 N N   . THR A 162 ? 0.3161 0.5759 0.3616 0.0116  -0.0302 -0.0145 162 THR A N   
1299 C CA  . THR A 162 ? 0.2701 0.5246 0.3173 0.0012  -0.0261 -0.0205 162 THR A CA  
1300 C C   . THR A 162 ? 0.3215 0.5549 0.3565 -0.0025 -0.0237 -0.0220 162 THR A C   
1301 O O   . THR A 162 ? 0.3114 0.5316 0.3460 -0.0065 -0.0184 -0.0230 162 THR A O   
1302 C CB  . THR A 162 ? 0.3250 0.5985 0.3799 -0.0070 -0.0298 -0.0263 162 THR A CB  
1303 O OG1 . THR A 162 ? 0.3540 0.6486 0.4227 -0.0040 -0.0314 -0.0249 162 THR A OG1 
1304 C CG2 . THR A 162 ? 0.3213 0.5867 0.3782 -0.0179 -0.0250 -0.0321 162 THR A CG2 
1305 N N   . GLU A 163 ? 0.3491 0.5803 0.3746 -0.0013 -0.0276 -0.0218 163 GLU A N   
1306 C CA  . GLU A 163 ? 0.2879 0.5001 0.3027 -0.0038 -0.0250 -0.0231 163 GLU A CA  
1307 C C   . GLU A 163 ? 0.2598 0.4547 0.2704 0.0021  -0.0208 -0.0178 163 GLU A C   
1308 O O   . GLU A 163 ? 0.3055 0.4851 0.3131 -0.0012 -0.0167 -0.0189 163 GLU A O   
1309 C CB  . GLU A 163 ? 0.3179 0.5335 0.3230 -0.0033 -0.0296 -0.0237 163 GLU A CB  
1310 C CG  . GLU A 163 ? 0.3946 0.6285 0.4023 -0.0104 -0.0341 -0.0301 163 GLU A CG  
1311 C CD  . GLU A 163 ? 0.4299 0.6727 0.4275 -0.0087 -0.0399 -0.0292 163 GLU A CD  
1312 O OE1 . GLU A 163 ? 0.3849 0.6264 0.3773 -0.0001 -0.0420 -0.0212 163 GLU A OE1 
1313 O OE2 . GLU A 163 ? 0.4340 0.6851 0.4286 -0.0166 -0.0422 -0.0366 163 GLU A OE2 
1314 N N   . ILE A 164 ? 0.3164 0.5135 0.3273 0.0108  -0.0220 -0.0122 164 ILE A N   
1315 C CA  . ILE A 164 ? 0.3319 0.5128 0.3385 0.0158  -0.0182 -0.0081 164 ILE A CA  
1316 C C   . ILE A 164 ? 0.2750 0.4520 0.2871 0.0133  -0.0131 -0.0091 164 ILE A C   
1317 O O   . ILE A 164 ? 0.3221 0.4842 0.3294 0.0125  -0.0096 -0.0082 164 ILE A O   
1318 C CB  . ILE A 164 ? 0.3213 0.5043 0.3274 0.0255  -0.0203 -0.0023 164 ILE A CB  
1319 C CG1 . ILE A 164 ? 0.2883 0.4742 0.2869 0.0274  -0.0252 0.0002  164 ILE A CG1 
1320 C CG2 . ILE A 164 ? 0.2407 0.4071 0.2429 0.0297  -0.0161 0.0006  164 ILE A CG2 
1321 C CD1 . ILE A 164 ? 0.2422 0.4327 0.2423 0.0370  -0.0280 0.0072  164 ILE A CD1 
1322 N N   . ALA A 165 ? 0.2909 0.4820 0.3130 0.0118  -0.0128 -0.0109 165 ALA A N   
1323 C CA  . ALA A 165 ? 0.2656 0.4542 0.2922 0.0088  -0.0075 -0.0115 165 ALA A CA  
1324 C C   . ALA A 165 ? 0.3040 0.4822 0.3278 0.0004  -0.0050 -0.0136 165 ALA A C   
1325 O O   . ALA A 165 ? 0.3342 0.5014 0.3551 -0.0009 -0.0010 -0.0117 165 ALA A O   
1326 C CB  . ALA A 165 ? 0.2223 0.4298 0.2612 0.0079  -0.0071 -0.0132 165 ALA A CB  
1327 N N   . GLY A 166 ? 0.3047 0.4862 0.3296 -0.0055 -0.0073 -0.0174 166 GLY A N   
1328 C CA  . GLY A 166 ? 0.2829 0.4527 0.3063 -0.0127 -0.0047 -0.0195 166 GLY A CA  
1329 C C   . GLY A 166 ? 0.3624 0.5144 0.3766 -0.0100 -0.0035 -0.0166 166 GLY A C   
1330 O O   . GLY A 166 ? 0.3039 0.4448 0.3177 -0.0127 0.0000  -0.0148 166 GLY A O   
1331 N N   . MET A 167 ? 0.2832 0.4331 0.2906 -0.0045 -0.0063 -0.0155 167 MET A N   
1332 C CA  A MET A 167 ? 0.3115 0.4460 0.3112 -0.0021 -0.0051 -0.0130 167 MET A CA  
1333 C CA  B MET A 167 ? 0.3103 0.4446 0.3101 -0.0024 -0.0050 -0.0131 167 MET A CA  
1334 C C   . MET A 167 ? 0.3236 0.4505 0.3220 0.0007  -0.0023 -0.0087 167 MET A C   
1335 O O   . MET A 167 ? 0.3168 0.4319 0.3124 -0.0008 -0.0002 -0.0068 167 MET A O   
1336 C CB  A MET A 167 ? 0.2924 0.4275 0.2852 0.0030  -0.0083 -0.0119 167 MET A CB  
1337 C CB  B MET A 167 ? 0.2968 0.4308 0.2894 0.0023  -0.0081 -0.0123 167 MET A CB  
1338 C CG  A MET A 167 ? 0.3438 0.4853 0.3348 -0.0006 -0.0109 -0.0165 167 MET A CG  
1339 C CG  B MET A 167 ? 0.3075 0.4551 0.3012 0.0070  -0.0119 -0.0110 167 MET A CG  
1340 S SD  A MET A 167 ? 0.3612 0.5001 0.3415 0.0043  -0.0135 -0.0141 167 MET A SD  
1341 S SD  B MET A 167 ? 0.3252 0.4740 0.3097 0.0097  -0.0158 -0.0102 167 MET A SD  
1342 C CE  A MET A 167 ? 0.3044 0.4587 0.2863 0.0107  -0.0183 -0.0100 167 MET A CE  
1343 C CE  B MET A 167 ? 0.3096 0.4663 0.2951 0.0009  -0.0170 -0.0181 167 MET A CE  
1344 N N   . ARG A 168 ? 0.2866 0.4210 0.2873 0.0048  -0.0022 -0.0072 168 ARG A N   
1345 C CA  . ARG A 168 ? 0.2831 0.4117 0.2819 0.0067  0.0009  -0.0045 168 ARG A CA  
1346 C C   . ARG A 168 ? 0.2561 0.3814 0.2569 0.0004  0.0041  -0.0039 168 ARG A C   
1347 O O   . ARG A 168 ? 0.2974 0.4128 0.2935 -0.0002 0.0056  -0.0011 168 ARG A O   
1348 C CB  . ARG A 168 ? 0.2959 0.4345 0.2988 0.0116  0.0016  -0.0045 168 ARG A CB  
1349 C CG  . ARG A 168 ? 0.2591 0.3957 0.2591 0.0195  -0.0003 -0.0028 168 ARG A CG  
1350 C CD  . ARG A 168 ? 0.2871 0.4289 0.2912 0.0248  0.0021  -0.0029 168 ARG A CD  
1351 N NE  . ARG A 168 ? 0.2698 0.4029 0.2695 0.0237  0.0063  -0.0031 168 ARG A NE  
1352 C CZ  . ARG A 168 ? 0.3003 0.4312 0.2998 0.0286  0.0091  -0.0037 168 ARG A CZ  
1353 N NH1 . ARG A 168 ? 0.2375 0.3733 0.2425 0.0358  0.0085  -0.0035 168 ARG A NH1 
1354 N NH2 . ARG A 168 ? 0.2724 0.3962 0.2664 0.0262  0.0125  -0.0046 168 ARG A NH2 
1355 N N   . VAL A 169 ? 0.2766 0.4106 0.2845 -0.0047 0.0049  -0.0060 169 VAL A N   
1356 C CA  . VAL A 169 ? 0.2589 0.3897 0.2693 -0.0110 0.0082  -0.0042 169 VAL A CA  
1357 C C   . VAL A 169 ? 0.3589 0.4763 0.3671 -0.0141 0.0083  -0.0027 169 VAL A C   
1358 O O   . VAL A 169 ? 0.2854 0.3950 0.2915 -0.0159 0.0103  0.0016  169 VAL A O   
1359 C CB  . VAL A 169 ? 0.3279 0.4711 0.3476 -0.0164 0.0094  -0.0070 169 VAL A CB  
1360 C CG1 . VAL A 169 ? 0.2323 0.3703 0.2551 -0.0238 0.0129  -0.0045 169 VAL A CG1 
1361 C CG2 . VAL A 169 ? 0.2519 0.4090 0.2754 -0.0130 0.0104  -0.0077 169 VAL A CG2 
1362 N N   . GLN A 170 ? 0.3045 0.4195 0.3131 -0.0144 0.0061  -0.0061 170 GLN A N   
1363 C CA  . GLN A 170 ? 0.3632 0.4656 0.3713 -0.0168 0.0069  -0.0054 170 GLN A CA  
1364 C C   . GLN A 170 ? 0.3137 0.4065 0.3151 -0.0122 0.0065  -0.0012 170 GLN A C   
1365 O O   . GLN A 170 ? 0.3101 0.3938 0.3123 -0.0138 0.0079  0.0025  170 GLN A O   
1366 C CB  . GLN A 170 ? 0.2799 0.3830 0.2892 -0.0183 0.0054  -0.0114 170 GLN A CB  
1367 C CG  . GLN A 170 ? 0.2969 0.3874 0.3077 -0.0206 0.0072  -0.0120 170 GLN A CG  
1368 C CD  . GLN A 170 ? 0.3418 0.4338 0.3542 -0.0239 0.0069  -0.0197 170 GLN A CD  
1369 O OE1 . GLN A 170 ? 0.2889 0.3898 0.2972 -0.0223 0.0040  -0.0233 170 GLN A OE1 
1370 N NE2 . GLN A 170 ? 0.3419 0.4251 0.3604 -0.0286 0.0099  -0.0221 170 GLN A NE2 
1371 N N   . LEU A 171 ? 0.3004 0.3954 0.2963 -0.0068 0.0046  -0.0012 171 LEU A N   
1372 C CA  . LEU A 171 ? 0.3055 0.3922 0.2956 -0.0033 0.0044  0.0022  171 LEU A CA  
1373 C C   . LEU A 171 ? 0.3200 0.4056 0.3086 -0.0043 0.0059  0.0063  171 LEU A C   
1374 O O   . LEU A 171 ? 0.3005 0.3789 0.2869 -0.0046 0.0059  0.0100  171 LEU A O   
1375 C CB  . LEU A 171 ? 0.2869 0.3756 0.2721 0.0023  0.0025  0.0013  171 LEU A CB  
1376 C CG  . LEU A 171 ? 0.2812 0.3621 0.2609 0.0053  0.0024  0.0042  171 LEU A CG  
1377 C CD1 . LEU A 171 ? 0.2687 0.3410 0.2482 0.0039  0.0025  0.0054  171 LEU A CD1 
1378 C CD2 . LEU A 171 ? 0.2220 0.3044 0.1981 0.0105  0.0011  0.0036  171 LEU A CD2 
1379 N N   . ARG A 172 ? 0.2812 0.3753 0.2710 -0.0050 0.0073  0.0058  172 ARG A N   
1380 C CA  . ARG A 172 ? 0.2970 0.3918 0.2841 -0.0066 0.0093  0.0091  172 ARG A CA  
1381 C C   . ARG A 172 ? 0.3085 0.3978 0.2976 -0.0116 0.0102  0.0138  172 ARG A C   
1382 O O   . ARG A 172 ? 0.3109 0.3961 0.2956 -0.0121 0.0101  0.0183  172 ARG A O   
1383 C CB  . ARG A 172 ? 0.2897 0.3958 0.2795 -0.0072 0.0116  0.0070  172 ARG A CB  
1384 C CG  . ARG A 172 ? 0.3345 0.4429 0.3197 -0.0090 0.0145  0.0095  172 ARG A CG  
1385 C CD  . ARG A 172 ? 0.2918 0.4126 0.2809 -0.0091 0.0177  0.0066  172 ARG A CD  
1386 N NE  . ARG A 172 ? 0.3568 0.4826 0.3495 -0.0033 0.0162  0.0022  172 ARG A NE  
1387 C CZ  . ARG A 172 ? 0.3298 0.4676 0.3302 -0.0027 0.0172  -0.0006 172 ARG A CZ  
1388 N NH1 . ARG A 172 ? 0.3328 0.4792 0.3383 -0.0079 0.0203  -0.0004 172 ARG A NH1 
1389 N NH2 . ARG A 172 ? 0.3147 0.4569 0.3185 0.0031  0.0149  -0.0032 172 ARG A NH2 
1390 N N   . ASP A 173 ? 0.3142 0.4037 0.3105 -0.0155 0.0111  0.0130  173 ASP A N   
1391 C CA  A ASP A 173 ? 0.3251 0.4080 0.3252 -0.0199 0.0124  0.0181  173 ASP A CA  
1392 C CA  B ASP A 173 ? 0.3213 0.4042 0.3213 -0.0199 0.0124  0.0181  173 ASP A CA  
1393 C C   . ASP A 173 ? 0.3061 0.3786 0.3055 -0.0176 0.0106  0.0209  173 ASP A C   
1394 O O   . ASP A 173 ? 0.3638 0.4313 0.3635 -0.0190 0.0107  0.0275  173 ASP A O   
1395 C CB  A ASP A 173 ? 0.3386 0.4224 0.3475 -0.0247 0.0141  0.0153  173 ASP A CB  
1396 C CB  B ASP A 173 ? 0.3381 0.4219 0.3470 -0.0247 0.0141  0.0154  173 ASP A CB  
1397 C CG  A ASP A 173 ? 0.4009 0.4762 0.4154 -0.0291 0.0161  0.0210  173 ASP A CG  
1398 C CG  B ASP A 173 ? 0.4261 0.5200 0.4377 -0.0288 0.0167  0.0154  173 ASP A CG  
1399 O OD1 A ASP A 173 ? 0.4721 0.5486 0.4851 -0.0317 0.0177  0.0275  173 ASP A OD1 
1400 O OD1 B ASP A 173 ? 0.5158 0.6133 0.5226 -0.0290 0.0181  0.0196  173 ASP A OD1 
1401 O OD2 A ASP A 173 ? 0.4313 0.4983 0.4517 -0.0300 0.0164  0.0191  173 ASP A OD2 
1402 O OD2 B ASP A 173 ? 0.4587 0.5578 0.4772 -0.0322 0.0175  0.0108  173 ASP A OD2 
1403 N N   . ALA A 174 ? 0.2913 0.3614 0.2900 -0.0141 0.0090  0.0164  174 ALA A N   
1404 C CA  . ALA A 174 ? 0.2644 0.3260 0.2633 -0.0119 0.0079  0.0184  174 ALA A CA  
1405 C C   . ALA A 174 ? 0.2958 0.3572 0.2883 -0.0096 0.0062  0.0229  174 ALA A C   
1406 O O   . ALA A 174 ? 0.2811 0.3375 0.2753 -0.0095 0.0053  0.0280  174 ALA A O   
1407 C CB  . ALA A 174 ? 0.2678 0.3283 0.2665 -0.0092 0.0072  0.0124  174 ALA A CB  
1408 N N   . LEU A 175 ? 0.2710 0.3378 0.2567 -0.0077 0.0057  0.0207  175 LEU A N   
1409 C CA  . LEU A 175 ? 0.2675 0.3339 0.2467 -0.0065 0.0043  0.0235  175 LEU A CA  
1410 C C   . LEU A 175 ? 0.3397 0.4084 0.3173 -0.0101 0.0047  0.0295  175 LEU A C   
1411 O O   . LEU A 175 ? 0.2700 0.3373 0.2445 -0.0104 0.0027  0.0339  175 LEU A O   
1412 C CB  . LEU A 175 ? 0.2563 0.3267 0.2296 -0.0036 0.0045  0.0190  175 LEU A CB  
1413 C CG  . LEU A 175 ? 0.3579 0.4266 0.3313 0.0004  0.0038  0.0147  175 LEU A CG  
1414 C CD1 . LEU A 175 ? 0.2732 0.3460 0.2430 0.0035  0.0045  0.0113  175 LEU A CD1 
1415 C CD2 . LEU A 175 ? 0.2680 0.3300 0.2405 0.0020  0.0023  0.0158  175 LEU A CD2 
1416 N N   . ARG A 176 ? 0.3270 0.4000 0.3066 -0.0133 0.0070  0.0301  176 ARG A N   
1417 C CA  . ARG A 176 ? 0.3217 0.3968 0.2998 -0.0174 0.0078  0.0370  176 ARG A CA  
1418 C C   . ARG A 176 ? 0.3424 0.4105 0.3263 -0.0183 0.0064  0.0442  176 ARG A C   
1419 O O   . ARG A 176 ? 0.3607 0.4298 0.3418 -0.0204 0.0052  0.0518  176 ARG A O   
1420 C CB  . ARG A 176 ? 0.2672 0.3480 0.2482 -0.0211 0.0113  0.0362  176 ARG A CB  
1421 C CG  . ARG A 176 ? 0.3559 0.4459 0.3309 -0.0206 0.0133  0.0317  176 ARG A CG  
1422 C CD  . ARG A 176 ? 0.3472 0.4444 0.3273 -0.0242 0.0169  0.0305  176 ARG A CD  
1423 N NE  . ARG A 176 ? 0.4099 0.5169 0.3855 -0.0235 0.0196  0.0264  176 ARG A NE  
1424 C CZ  . ARG A 176 ? 0.3771 0.4926 0.3582 -0.0240 0.0224  0.0221  176 ARG A CZ  
1425 N NH1 . ARG A 176 ? 0.3852 0.5012 0.3756 -0.0258 0.0222  0.0207  176 ARG A NH1 
1426 N NH2 . ARG A 176 ? 0.3701 0.4946 0.3480 -0.0230 0.0255  0.0187  176 ARG A NH2 
1427 N N   . GLN A 177 ? 0.3572 0.4186 0.3494 -0.0168 0.0065  0.0420  177 GLN A N   
1428 C CA  . GLN A 177 ? 0.3705 0.4245 0.3705 -0.0169 0.0059  0.0483  177 GLN A CA  
1429 C C   . GLN A 177 ? 0.2600 0.3113 0.2600 -0.0131 0.0029  0.0495  177 GLN A C   
1430 O O   . GLN A 177 ? 0.3514 0.3969 0.3598 -0.0119 0.0025  0.0540  177 GLN A O   
1431 C CB  . GLN A 177 ? 0.3055 0.3533 0.3157 -0.0180 0.0087  0.0446  177 GLN A CB  
1432 C CG  . GLN A 177 ? 0.3208 0.3711 0.3334 -0.0231 0.0117  0.0453  177 GLN A CG  
1433 C CD  . GLN A 177 ? 0.4317 0.4765 0.4542 -0.0254 0.0145  0.0400  177 GLN A CD  
1434 O OE1 . GLN A 177 ? 0.3643 0.4047 0.3902 -0.0230 0.0144  0.0341  177 GLN A OE1 
1435 N NE2 . GLN A 177 ? 0.4857 0.5310 0.5125 -0.0307 0.0173  0.0417  177 GLN A NE2 
1436 N N   . GLY A 178 ? 0.2575 0.3129 0.2493 -0.0112 0.0011  0.0458  178 GLY A N   
1437 C CA  . GLY A 178 ? 0.2837 0.3383 0.2749 -0.0087 -0.0018 0.0475  178 GLY A CA  
1438 C C   . GLY A 178 ? 0.3550 0.4066 0.3473 -0.0054 -0.0015 0.0408  178 GLY A C   
1439 O O   . GLY A 178 ? 0.3030 0.3541 0.2963 -0.0037 -0.0035 0.0422  178 GLY A O   
1440 N N   . ALA A 179 ? 0.3027 0.3535 0.2949 -0.0047 0.0008  0.0341  179 ALA A N   
1441 C CA  . ALA A 179 ? 0.3179 0.3667 0.3095 -0.0018 0.0010  0.0287  179 ALA A CA  
1442 C C   . ALA A 179 ? 0.3187 0.3697 0.3028 -0.0006 -0.0008 0.0279  179 ALA A C   
1443 O O   . ALA A 179 ? 0.3183 0.3730 0.2962 -0.0018 -0.0014 0.0286  179 ALA A O   
1444 C CB  . ALA A 179 ? 0.2456 0.2957 0.2365 -0.0017 0.0029  0.0224  179 ALA A CB  
1445 N N   . LEU A 180 ? 0.2619 0.3102 0.2467 0.0015  -0.0010 0.0262  180 LEU A N   
1446 C CA  . LEU A 180 ? 0.2242 0.2730 0.2035 0.0020  -0.0024 0.0257  180 LEU A CA  
1447 C C   . LEU A 180 ? 0.3440 0.3925 0.3172 0.0038  -0.0013 0.0208  180 LEU A C   
1448 O O   . LEU A 180 ? 0.3222 0.3700 0.2906 0.0040  -0.0019 0.0199  180 LEU A O   
1449 C CB  . LEU A 180 ? 0.2767 0.3234 0.2610 0.0029  -0.0029 0.0270  180 LEU A CB  
1450 C CG  . LEU A 180 ? 0.3188 0.3663 0.3116 0.0023  -0.0041 0.0326  180 LEU A CG  
1451 C CD1 . LEU A 180 ? 0.2237 0.2708 0.2223 0.0035  -0.0043 0.0333  180 LEU A CD1 
1452 C CD2 . LEU A 180 ? 0.2636 0.3156 0.2529 -0.0002 -0.0072 0.0374  180 LEU A CD2 
1453 N N   . GLY A 181 ? 0.3391 0.3883 0.3128 0.0050  0.0001  0.0180  181 GLY A N   
1454 C CA  . GLY A 181 ? 0.2810 0.3309 0.2501 0.0075  0.0007  0.0147  181 GLY A CA  
1455 C C   . GLY A 181 ? 0.3270 0.3779 0.2978 0.0087  0.0014  0.0122  181 GLY A C   
1456 O O   . GLY A 181 ? 0.3292 0.3805 0.3046 0.0070  0.0021  0.0116  181 GLY A O   
1457 N N   . LEU A 182 ? 0.3155 0.3666 0.2824 0.0115  0.0014  0.0108  182 LEU A N   
1458 C CA  . LEU A 182 ? 0.2975 0.3520 0.2639 0.0126  0.0014  0.0086  182 LEU A CA  
1459 C C   . LEU A 182 ? 0.3211 0.3721 0.2842 0.0142  0.0019  0.0092  182 LEU A C   
1460 O O   . LEU A 182 ? 0.3041 0.3514 0.2642 0.0160  0.0019  0.0112  182 LEU A O   
1461 C CB  . LEU A 182 ? 0.2458 0.3060 0.2107 0.0150  0.0004  0.0077  182 LEU A CB  
1462 C CG  . LEU A 182 ? 0.3220 0.3880 0.2855 0.0167  -0.0007 0.0063  182 LEU A CG  
1463 C CD1 . LEU A 182 ? 0.3124 0.3845 0.2798 0.0133  -0.0009 0.0030  182 LEU A CD1 
1464 C CD2 . LEU A 182 ? 0.2951 0.3651 0.2577 0.0210  -0.0018 0.0074  182 LEU A CD2 
1465 N N   . SER A 183 ? 0.2883 0.3403 0.2519 0.0131  0.0028  0.0072  183 SER A N   
1466 C CA  . SER A 183 ? 0.2557 0.3061 0.2151 0.0141  0.0038  0.0078  183 SER A CA  
1467 C C   . SER A 183 ? 0.3732 0.4300 0.3278 0.0153  0.0027  0.0064  183 SER A C   
1468 O O   . SER A 183 ? 0.3101 0.3729 0.2663 0.0139  0.0017  0.0032  183 SER A O   
1469 C CB  . SER A 183 ? 0.2521 0.2999 0.2150 0.0120  0.0064  0.0063  183 SER A CB  
1470 O OG  . SER A 183 ? 0.2691 0.3204 0.2338 0.0101  0.0074  0.0017  183 SER A OG  
1471 N N   . THR A 184 ? 0.3089 0.3649 0.2576 0.0176  0.0026  0.0093  184 THR A N   
1472 C CA  . THR A 184 ? 0.3595 0.4225 0.3026 0.0186  0.0011  0.0094  184 THR A CA  
1473 C C   . THR A 184 ? 0.4117 0.4736 0.3492 0.0174  0.0034  0.0098  184 THR A C   
1474 O O   . THR A 184 ? 0.3342 0.3893 0.2723 0.0171  0.0060  0.0118  184 THR A O   
1475 C CB  . THR A 184 ? 0.3705 0.4353 0.3112 0.0232  -0.0015 0.0140  184 THR A CB  
1476 O OG1 . THR A 184 ? 0.3390 0.3948 0.2781 0.0252  0.0000  0.0185  184 THR A OG1 
1477 C CG2 . THR A 184 ? 0.3065 0.3746 0.2529 0.0244  -0.0032 0.0127  184 THR A CG2 
1478 N N   . GLY A 185 ? 0.3674 0.4373 0.2995 0.0162  0.0026  0.0075  185 GLY A N   
1479 C CA  . GLY A 185 ? 0.3622 0.4335 0.2866 0.0150  0.0048  0.0081  185 GLY A CA  
1480 C C   . GLY A 185 ? 0.3874 0.4679 0.3034 0.0167  0.0012  0.0111  185 GLY A C   
1481 O O   . GLY A 185 ? 0.3910 0.4807 0.3023 0.0139  0.0004  0.0066  185 GLY A O   
1482 N N   . LEU A 186 ? 0.3198 0.3981 0.2344 0.0212  -0.0009 0.0188  186 LEU A N   
1483 C CA  . LEU A 186 ? 0.3513 0.4388 0.2610 0.0243  -0.0055 0.0233  186 LEU A CA  
1484 C C   . LEU A 186 ? 0.3552 0.4484 0.2533 0.0232  -0.0054 0.0267  186 LEU A C   
1485 O O   . LEU A 186 ? 0.3807 0.4850 0.2736 0.0247  -0.0099 0.0298  186 LEU A O   
1486 C CB  . LEU A 186 ? 0.3716 0.4531 0.2855 0.0301  -0.0071 0.0305  186 LEU A CB  
1487 C CG  . LEU A 186 ? 0.3773 0.4548 0.3013 0.0311  -0.0070 0.0271  186 LEU A CG  
1488 C CD1 . LEU A 186 ? 0.3056 0.3759 0.2334 0.0366  -0.0073 0.0329  186 LEU A CD1 
1489 C CD2 . LEU A 186 ? 0.2730 0.3622 0.2009 0.0299  -0.0102 0.0220  186 LEU A CD2 
1490 N N   . ALA A 187 ? 0.3806 0.4679 0.2745 0.0205  -0.0006 0.0267  187 ALA A N   
1491 C CA  . ALA A 187 ? 0.4373 0.5311 0.3189 0.0187  0.0003  0.0295  187 ALA A CA  
1492 C C   . ALA A 187 ? 0.4363 0.5416 0.3124 0.0137  0.0002  0.0206  187 ALA A C   
1493 O O   . ALA A 187 ? 0.4696 0.5846 0.3338 0.0120  -0.0009 0.0224  187 ALA A O   
1494 C CB  . ALA A 187 ? 0.3939 0.4784 0.2733 0.0170  0.0063  0.0321  187 ALA A CB  
1495 N N   . TYR A 188 ? 0.4068 0.5114 0.2908 0.0109  0.0014  0.0110  188 TYR A N   
1496 C CA  . TYR A 188 ? 0.3568 0.4707 0.2370 0.0055  0.0021  0.0010  188 TYR A CA  
1497 C C   . TYR A 188 ? 0.3935 0.5214 0.2702 0.0053  -0.0047 0.0006  188 TYR A C   
1498 O O   . TYR A 188 ? 0.3712 0.5003 0.2549 0.0090  -0.0092 0.0044  188 TYR A O   
1499 C CB  . TYR A 188 ? 0.3537 0.4607 0.2451 0.0027  0.0058  -0.0084 188 TYR A CB  
1500 C CG  . TYR A 188 ? 0.4710 0.5680 0.3655 0.0020  0.0127  -0.0094 188 TYR A CG  
1501 C CD1 . TYR A 188 ? 0.4727 0.5725 0.3605 -0.0018 0.0179  -0.0149 188 TYR A CD1 
1502 C CD2 . TYR A 188 ? 0.4317 0.5176 0.3358 0.0049  0.0139  -0.0051 188 TYR A CD2 
1503 C CE1 . TYR A 188 ? 0.4671 0.5593 0.3593 -0.0021 0.0245  -0.0158 188 TYR A CE1 
1504 C CE2 . TYR A 188 ? 0.4464 0.5251 0.3544 0.0042  0.0197  -0.0058 188 TYR A CE2 
1505 C CZ  . TYR A 188 ? 0.4683 0.5504 0.3712 0.0010  0.0250  -0.0109 188 TYR A CZ  
1506 O OH  . TYR A 188 ? 0.5308 0.6073 0.4393 0.0005  0.0311  -0.0116 188 TYR A OH  
1507 N N   . ALA A 189 ? 0.4023 0.5421 0.2684 0.0006  -0.0052 -0.0047 189 ALA A N   
1508 C CA  . ALA A 189 ? 0.4201 0.5762 0.2821 -0.0005 -0.0122 -0.0054 189 ALA A CA  
1509 C C   . ALA A 189 ? 0.4046 0.5620 0.2796 -0.0008 -0.0151 -0.0104 189 ALA A C   
1510 O O   . ALA A 189 ? 0.3646 0.5329 0.2416 0.0015  -0.0217 -0.0065 189 ALA A O   
1511 C CB  . ALA A 189 ? 0.3430 0.5111 0.1925 -0.0076 -0.0112 -0.0142 189 ALA A CB  
1512 N N   . SER A 190 ? 0.3848 0.5319 0.2695 -0.0035 -0.0103 -0.0184 190 SER A N   
1513 C CA  . SER A 190 ? 0.3912 0.5407 0.2872 -0.0051 -0.0126 -0.0236 190 SER A CA  
1514 C C   . SER A 190 ? 0.3759 0.5207 0.2815 0.0011  -0.0151 -0.0155 190 SER A C   
1515 O O   . SER A 190 ? 0.3409 0.4903 0.2552 0.0003  -0.0176 -0.0180 190 SER A O   
1516 C CB  . SER A 190 ? 0.4044 0.5442 0.3077 -0.0101 -0.0065 -0.0340 190 SER A CB  
1517 O OG  . SER A 190 ? 0.4661 0.5913 0.3722 -0.0075 -0.0010 -0.0311 190 SER A OG  
1518 N N   . ALA A 191 ? 0.3421 0.4781 0.2464 0.0068  -0.0141 -0.0064 191 ALA A N   
1519 C CA  . ALA A 191 ? 0.3476 0.4794 0.2596 0.0128  -0.0162 0.0008  191 ALA A CA  
1520 C C   . ALA A 191 ? 0.3424 0.4772 0.2490 0.0189  -0.0195 0.0115  191 ALA A C   
1521 O O   . ALA A 191 ? 0.3601 0.4928 0.2735 0.0244  -0.0213 0.0171  191 ALA A O   
1522 C CB  . ALA A 191 ? 0.3030 0.4184 0.2215 0.0138  -0.0112 0.0012  191 ALA A CB  
1523 N N   . PHE A 192 ? 0.3526 0.4922 0.2475 0.0181  -0.0201 0.0146  192 PHE A N   
1524 C CA  . PHE A 192 ? 0.3509 0.4917 0.2407 0.0241  -0.0228 0.0263  192 PHE A CA  
1525 C C   . PHE A 192 ? 0.4101 0.5632 0.3048 0.0288  -0.0296 0.0312  192 PHE A C   
1526 O O   . PHE A 192 ? 0.4117 0.5615 0.3089 0.0358  -0.0313 0.0412  192 PHE A O   
1527 C CB  . PHE A 192 ? 0.3514 0.4979 0.2264 0.0214  -0.0225 0.0288  192 PHE A CB  
1528 C CG  . PHE A 192 ? 0.3687 0.5137 0.2379 0.0271  -0.0244 0.0424  192 PHE A CG  
1529 C CD1 . PHE A 192 ? 0.3528 0.4813 0.2250 0.0305  -0.0201 0.0486  192 PHE A CD1 
1530 C CD2 . PHE A 192 ? 0.3499 0.5103 0.2108 0.0287  -0.0304 0.0491  192 PHE A CD2 
1531 C CE1 . PHE A 192 ? 0.4372 0.5625 0.3049 0.0355  -0.0212 0.0614  192 PHE A CE1 
1532 C CE2 . PHE A 192 ? 0.3736 0.5318 0.2296 0.0343  -0.0320 0.0631  192 PHE A CE2 
1533 C CZ  . PHE A 192 ? 0.4764 0.6161 0.3360 0.0377  -0.0271 0.0692  192 PHE A CZ  
1534 N N   . GLN A 193 ? 0.3062 0.4738 0.2037 0.0253  -0.0334 0.0245  193 GLN A N   
1535 C CA  . GLN A 193 ? 0.3541 0.5362 0.2576 0.0299  -0.0401 0.0293  193 GLN A CA  
1536 C C   . GLN A 193 ? 0.3875 0.5642 0.3059 0.0342  -0.0392 0.0293  193 GLN A C   
1537 O O   . GLN A 193 ? 0.3987 0.5862 0.3245 0.0394  -0.0438 0.0340  193 GLN A O   
1538 C CB  . GLN A 193 ? 0.3176 0.5199 0.2185 0.0238  -0.0450 0.0223  193 GLN A CB  
1539 C CG  . GLN A 193 ? 0.3520 0.5643 0.2366 0.0198  -0.0472 0.0229  193 GLN A CG  
1540 C CD  . GLN A 193 ? 0.4389 0.6539 0.3159 0.0266  -0.0506 0.0375  193 GLN A CD  
1541 O OE1 . GLN A 193 ? 0.4162 0.6372 0.3004 0.0340  -0.0556 0.0467  193 GLN A OE1 
1542 N NE2 . GLN A 193 ? 0.3624 0.5728 0.2252 0.0242  -0.0477 0.0398  193 GLN A NE2 
1543 N N   . SER A 194 ? 0.3904 0.5518 0.3136 0.0324  -0.0334 0.0244  194 SER A N   
1544 C CA  . SER A 194 ? 0.3988 0.5553 0.3342 0.0362  -0.0321 0.0245  194 SER A CA  
1545 C C   . SER A 194 ? 0.3765 0.5269 0.3146 0.0450  -0.0324 0.0344  194 SER A C   
1546 O O   . SER A 194 ? 0.4383 0.5794 0.3693 0.0472  -0.0310 0.0406  194 SER A O   
1547 C CB  . SER A 194 ? 0.3755 0.5172 0.3136 0.0322  -0.0261 0.0183  194 SER A CB  
1548 O OG  . SER A 194 ? 0.4014 0.5279 0.3345 0.0337  -0.0223 0.0221  194 SER A OG  
1549 N N   . THR A 195 ? 0.3208 0.4762 0.2700 0.0500  -0.0338 0.0357  195 THR A N   
1550 C CA  . THR A 195 ? 0.3236 0.4713 0.2778 0.0586  -0.0330 0.0436  195 THR A CA  
1551 C C   . THR A 195 ? 0.2896 0.4185 0.2464 0.0584  -0.0266 0.0407  195 THR A C   
1552 O O   . THR A 195 ? 0.2914 0.4166 0.2489 0.0526  -0.0237 0.0332  195 THR A O   
1553 C CB  . THR A 195 ? 0.4054 0.5670 0.3717 0.0646  -0.0365 0.0458  195 THR A CB  
1554 O OG1 . THR A 195 ? 0.3971 0.5620 0.3718 0.0610  -0.0342 0.0373  195 THR A OG1 
1555 C CG2 . THR A 195 ? 0.3552 0.5374 0.3196 0.0647  -0.0437 0.0491  195 THR A CG2 
1556 N N   . THR A 196 ? 0.3011 0.4183 0.2595 0.0646  -0.0246 0.0469  196 THR A N   
1557 C CA  . THR A 196 ? 0.3748 0.4762 0.3365 0.0645  -0.0190 0.0436  196 THR A CA  
1558 C C   . THR A 196 ? 0.3161 0.4230 0.2874 0.0644  -0.0177 0.0372  196 THR A C   
1559 O O   . THR A 196 ? 0.3458 0.4444 0.3175 0.0606  -0.0137 0.0317  196 THR A O   
1560 C CB  . THR A 196 ? 0.4425 0.5311 0.4062 0.0713  -0.0170 0.0506  196 THR A CB  
1561 O OG1 . THR A 196 ? 0.3806 0.4659 0.3356 0.0716  -0.0184 0.0581  196 THR A OG1 
1562 C CG2 . THR A 196 ? 0.3328 0.4046 0.2974 0.0693  -0.0113 0.0460  196 THR A CG2 
1563 N N   . GLU A 197 ? 0.3197 0.4418 0.2990 0.0685  -0.0209 0.0383  197 GLU A N   
1564 C CA  . GLU A 197 ? 0.3362 0.4653 0.3252 0.0682  -0.0191 0.0325  197 GLU A CA  
1565 C C   . GLU A 197 ? 0.3527 0.4848 0.3389 0.0590  -0.0182 0.0250  197 GLU A C   
1566 O O   . GLU A 197 ? 0.3119 0.4394 0.3008 0.0563  -0.0143 0.0201  197 GLU A O   
1567 C CB  . GLU A 197 ? 0.3048 0.4523 0.3037 0.0738  -0.0233 0.0355  197 GLU A CB  
1568 C CG  . GLU A 197 ? 0.3708 0.5255 0.3821 0.0759  -0.0205 0.0310  197 GLU A CG  
1569 C CD  . GLU A 197 ? 0.3844 0.5590 0.4071 0.0821  -0.0250 0.0347  197 GLU A CD  
1570 O OE1 . GLU A 197 ? 0.4349 0.6264 0.4585 0.0778  -0.0297 0.0332  197 GLU A OE1 
1571 O OE2 . GLU A 197 ? 0.3598 0.5334 0.3915 0.0914  -0.0239 0.0391  197 GLU A OE2 
1572 N N   . GLU A 198 ? 0.3076 0.4473 0.2882 0.0541  -0.0217 0.0242  198 GLU A N   
1573 C CA  . GLU A 198 ? 0.3392 0.4804 0.3183 0.0455  -0.0206 0.0172  198 GLU A CA  
1574 C C   . GLU A 198 ? 0.3102 0.4344 0.2849 0.0422  -0.0158 0.0150  198 GLU A C   
1575 O O   . GLU A 198 ? 0.3028 0.4253 0.2806 0.0382  -0.0131 0.0108  198 GLU A O   
1576 C CB  . GLU A 198 ? 0.2922 0.4414 0.2648 0.0408  -0.0243 0.0160  198 GLU A CB  
1577 C CG  . GLU A 198 ? 0.3373 0.4801 0.3061 0.0325  -0.0216 0.0096  198 GLU A CG  
1578 C CD  . GLU A 198 ? 0.3366 0.4880 0.2998 0.0272  -0.0244 0.0062  198 GLU A CD  
1579 O OE1 . GLU A 198 ? 0.3816 0.5457 0.3427 0.0292  -0.0291 0.0088  198 GLU A OE1 
1580 O OE2 . GLU A 198 ? 0.3544 0.4999 0.3156 0.0210  -0.0217 0.0007  198 GLU A OE2 
1581 N N   . VAL A 199 ? 0.3120 0.4246 0.2795 0.0435  -0.0149 0.0185  199 VAL A N   
1582 C CA  . VAL A 199 ? 0.3099 0.4080 0.2739 0.0404  -0.0110 0.0168  199 VAL A CA  
1583 C C   . VAL A 199 ? 0.2813 0.3735 0.2501 0.0426  -0.0079 0.0159  199 VAL A C   
1584 O O   . VAL A 199 ? 0.3046 0.3914 0.2732 0.0385  -0.0054 0.0127  199 VAL A O   
1585 C CB  . VAL A 199 ? 0.3075 0.3960 0.2641 0.0412  -0.0106 0.0210  199 VAL A CB  
1586 C CG1 . VAL A 199 ? 0.2766 0.3522 0.2309 0.0376  -0.0070 0.0191  199 VAL A CG1 
1587 C CG2 . VAL A 199 ? 0.3004 0.3963 0.2510 0.0387  -0.0132 0.0213  199 VAL A CG2 
1588 N N   . MET A 200 ? 0.3076 0.4009 0.2806 0.0493  -0.0079 0.0188  200 MET A N   
1589 C CA  . MET A 200 ? 0.2837 0.3723 0.2614 0.0516  -0.0043 0.0165  200 MET A CA  
1590 C C   . MET A 200 ? 0.3290 0.4260 0.3110 0.0476  -0.0030 0.0115  200 MET A C   
1591 O O   . MET A 200 ? 0.3386 0.4299 0.3197 0.0450  0.0005  0.0084  200 MET A O   
1592 C CB  . MET A 200 ? 0.2826 0.3730 0.2665 0.0600  -0.0044 0.0200  200 MET A CB  
1593 C CG  . MET A 200 ? 0.2840 0.3605 0.2649 0.0641  -0.0032 0.0247  200 MET A CG  
1594 S SD  . MET A 200 ? 0.3781 0.4580 0.3687 0.0752  -0.0039 0.0303  200 MET A SD  
1595 C CE  . MET A 200 ? 0.3300 0.3890 0.3162 0.0778  -0.0012 0.0352  200 MET A CE  
1596 N N   . ALA A 201 ? 0.2946 0.4057 0.2809 0.0465  -0.0056 0.0108  201 ALA A N   
1597 C CA  . ALA A 201 ? 0.2704 0.3899 0.2616 0.0421  -0.0040 0.0065  201 ALA A CA  
1598 C C   . ALA A 201 ? 0.3044 0.4160 0.2903 0.0348  -0.0023 0.0044  201 ALA A C   
1599 O O   . ALA A 201 ? 0.2863 0.3974 0.2734 0.0319  0.0007  0.0022  201 ALA A O   
1600 C CB  . ALA A 201 ? 0.2331 0.3691 0.2300 0.0410  -0.0076 0.0060  201 ALA A CB  
1601 N N   . LEU A 202 ? 0.3250 0.4313 0.3054 0.0319  -0.0041 0.0053  202 LEU A N   
1602 C CA  . LEU A 202 ? 0.2769 0.3761 0.2543 0.0259  -0.0026 0.0039  202 LEU A CA  
1603 C C   . LEU A 202 ? 0.2831 0.3706 0.2564 0.0263  -0.0003 0.0049  202 LEU A C   
1604 O O   . LEU A 202 ? 0.3117 0.3966 0.2846 0.0224  0.0015  0.0041  202 LEU A O   
1605 C CB  . LEU A 202 ? 0.2494 0.3467 0.2234 0.0231  -0.0044 0.0037  202 LEU A CB  
1606 C CG  . LEU A 202 ? 0.3603 0.4700 0.3372 0.0219  -0.0072 0.0017  202 LEU A CG  
1607 C CD1 . LEU A 202 ? 0.3005 0.4081 0.2732 0.0183  -0.0081 0.0000  202 LEU A CD1 
1608 C CD2 . LEU A 202 ? 0.2560 0.3738 0.2399 0.0179  -0.0062 -0.0012 202 LEU A CD2 
1609 N N   . ALA A 203 ? 0.2697 0.3505 0.2399 0.0306  -0.0004 0.0070  203 ALA A N   
1610 C CA  . ALA A 203 ? 0.3491 0.4192 0.3158 0.0303  0.0018  0.0071  203 ALA A CA  
1611 C C   . ALA A 203 ? 0.2774 0.3493 0.2457 0.0302  0.0045  0.0044  203 ALA A C   
1612 O O   . ALA A 203 ? 0.2843 0.3500 0.2491 0.0275  0.0061  0.0034  203 ALA A O   
1613 C CB  . ALA A 203 ? 0.2393 0.3018 0.2037 0.0347  0.0017  0.0096  203 ALA A CB  
1614 N N   . GLU A 204 ? 0.2803 0.3617 0.2540 0.0327  0.0052  0.0030  204 GLU A N   
1615 C CA  . GLU A 204 ? 0.3067 0.3908 0.2818 0.0324  0.0088  -0.0001 204 GLU A CA  
1616 C C   . GLU A 204 ? 0.2625 0.3486 0.2351 0.0255  0.0096  -0.0008 204 GLU A C   
1617 O O   . GLU A 204 ? 0.3167 0.4017 0.2863 0.0236  0.0124  -0.0028 204 GLU A O   
1618 C CB  . GLU A 204 ? 0.3208 0.4165 0.3040 0.0367  0.0096  -0.0013 204 GLU A CB  
1619 C CG  . GLU A 204 ? 0.2844 0.3770 0.2710 0.0446  0.0103  -0.0007 204 GLU A CG  
1620 C CD  . GLU A 204 ? 0.3655 0.4700 0.3619 0.0496  0.0120  -0.0022 204 GLU A CD  
1621 O OE1 . GLU A 204 ? 0.3217 0.4370 0.3217 0.0463  0.0135  -0.0046 204 GLU A OE1 
1622 O OE2 . GLU A 204 ? 0.3213 0.4246 0.3228 0.0571  0.0119  -0.0005 204 GLU A OE2 
1623 N N   . GLU A 205 ? 0.2455 0.3343 0.2192 0.0218  0.0074  0.0010  205 GLU A N   
1624 C CA  . GLU A 205 ? 0.2755 0.3644 0.2475 0.0156  0.0081  0.0019  205 GLU A CA  
1625 C C   . GLU A 205 ? 0.3713 0.4511 0.3371 0.0135  0.0080  0.0033  205 GLU A C   
1626 O O   . GLU A 205 ? 0.2961 0.3764 0.2597 0.0090  0.0086  0.0049  205 GLU A O   
1627 C CB  . GLU A 205 ? 0.2249 0.3159 0.2004 0.0123  0.0062  0.0032  205 GLU A CB  
1628 C CG  . GLU A 205 ? 0.2823 0.3844 0.2645 0.0124  0.0061  0.0014  205 GLU A CG  
1629 C CD  . GLU A 205 ? 0.3661 0.4763 0.3514 0.0099  0.0093  0.0005  205 GLU A CD  
1630 O OE1 . GLU A 205 ? 0.3304 0.4372 0.3121 0.0060  0.0111  0.0023  205 GLU A OE1 
1631 O OE2 . GLU A 205 ? 0.3151 0.4358 0.3064 0.0118  0.0099  -0.0015 205 GLU A OE2 
1632 N N   . LEU A 206 ? 0.3776 0.4497 0.3407 0.0164  0.0070  0.0033  206 LEU A N   
1633 C CA  . LEU A 206 ? 0.3337 0.3983 0.2919 0.0139  0.0063  0.0045  206 LEU A CA  
1634 C C   . LEU A 206 ? 0.3653 0.4280 0.3190 0.0135  0.0085  0.0015  206 LEU A C   
1635 O O   . LEU A 206 ? 0.3647 0.4231 0.3142 0.0105  0.0076  0.0019  206 LEU A O   
1636 C CB  . LEU A 206 ? 0.2638 0.3213 0.2218 0.0161  0.0047  0.0058  206 LEU A CB  
1637 C CG  . LEU A 206 ? 0.3233 0.3823 0.2844 0.0164  0.0030  0.0075  206 LEU A CG  
1638 C CD1 . LEU A 206 ? 0.3068 0.3601 0.2663 0.0193  0.0024  0.0084  206 LEU A CD1 
1639 C CD2 . LEU A 206 ? 0.3091 0.3676 0.2718 0.0121  0.0022  0.0094  206 LEU A CD2 
1640 N N   . ALA A 207 ? 0.3563 0.4226 0.3113 0.0165  0.0113  -0.0019 207 ALA A N   
1641 C CA  . ALA A 207 ? 0.3003 0.3636 0.2512 0.0165  0.0142  -0.0064 207 ALA A CA  
1642 C C   . ALA A 207 ? 0.3917 0.4588 0.3364 0.0103  0.0148  -0.0068 207 ALA A C   
1643 O O   . ALA A 207 ? 0.3727 0.4454 0.3174 0.0068  0.0135  -0.0030 207 ALA A O   
1644 C CB  . ALA A 207 ? 0.3377 0.4048 0.2931 0.0216  0.0179  -0.0102 207 ALA A CB  
1645 N N   . ALA A 208 ? 0.3291 0.3930 0.2681 0.0088  0.0169  -0.0115 208 ALA A N   
1646 C CA  . ALA A 208 ? 0.4629 0.5318 0.3941 0.0026  0.0174  -0.0124 208 ALA A CA  
1647 C C   . ALA A 208 ? 0.3931 0.4619 0.3219 -0.0020 0.0125  -0.0061 208 ALA A C   
1648 O O   . ALA A 208 ? 0.3532 0.4287 0.2784 -0.0064 0.0116  -0.0026 208 ALA A O   
1649 C CB  . ALA A 208 ? 0.3666 0.4459 0.2978 0.0015  0.0207  -0.0128 208 ALA A CB  
1650 N N   . GLY A 209 ? 0.3856 0.4473 0.3174 -0.0006 0.0095  -0.0041 209 GLY A N   
1651 C CA  . GLY A 209 ? 0.3079 0.3695 0.2394 -0.0041 0.0052  0.0013  209 GLY A CA  
1652 C C   . GLY A 209 ? 0.3872 0.4515 0.3245 -0.0037 0.0033  0.0077  209 GLY A C   
1653 O O   . GLY A 209 ? 0.3665 0.4315 0.3048 -0.0063 0.0001  0.0128  209 GLY A O   
1654 N N   . LYS A 210 ? 0.3044 0.3703 0.2463 -0.0007 0.0052  0.0074  210 LYS A N   
1655 C CA  . LYS A 210 ? 0.3513 0.4191 0.2989 -0.0012 0.0039  0.0123  210 LYS A CA  
1656 C C   . LYS A 210 ? 0.3991 0.4612 0.3518 0.0011  0.0020  0.0138  210 LYS A C   
1657 O O   . LYS A 210 ? 0.3816 0.4442 0.3396 0.0007  0.0015  0.0166  210 LYS A O   
1658 C CB  . LYS A 210 ? 0.3176 0.3909 0.2684 -0.0001 0.0065  0.0108  210 LYS A CB  
1659 C CG  . LYS A 210 ? 0.4032 0.4834 0.3493 -0.0030 0.0093  0.0098  210 LYS A CG  
1660 C CD  . LYS A 210 ? 0.5846 0.6717 0.5358 -0.0039 0.0115  0.0107  210 LYS A CD  
1661 C CE  . LYS A 210 ? 0.5770 0.6709 0.5274 -0.0024 0.0157  0.0055  210 LYS A CE  
1662 N NZ  . LYS A 210 ? 0.6786 0.7758 0.6203 -0.0058 0.0181  0.0042  210 LYS A NZ  
1663 N N   . GLY A 211 ? 0.3379 0.3946 0.2896 0.0030  0.0015  0.0120  211 GLY A N   
1664 C CA  . GLY A 211 ? 0.3140 0.3665 0.2699 0.0043  0.0001  0.0138  211 GLY A CA  
1665 C C   . GLY A 211 ? 0.3683 0.4151 0.3227 0.0070  0.0007  0.0114  211 GLY A C   
1666 O O   . GLY A 211 ? 0.3790 0.4239 0.3298 0.0079  0.0021  0.0083  211 GLY A O   
1667 N N   . VAL A 212 ? 0.2642 0.3078 0.2216 0.0080  0.0002  0.0129  212 VAL A N   
1668 C CA  . VAL A 212 ? 0.3035 0.3415 0.2596 0.0101  0.0010  0.0120  212 VAL A CA  
1669 C C   . VAL A 212 ? 0.3109 0.3494 0.2682 0.0134  0.0017  0.0123  212 VAL A C   
1670 O O   . VAL A 212 ? 0.3251 0.3672 0.2853 0.0129  0.0013  0.0128  212 VAL A O   
1671 C CB  . VAL A 212 ? 0.3726 0.4078 0.3305 0.0077  0.0002  0.0138  212 VAL A CB  
1672 C CG1 . VAL A 212 ? 0.2761 0.3136 0.2393 0.0071  -0.0003 0.0162  212 VAL A CG1 
1673 C CG2 . VAL A 212 ? 0.3860 0.4148 0.3426 0.0092  0.0017  0.0134  212 VAL A CG2 
1674 N N   . TYR A 213 ? 0.2826 0.3177 0.2378 0.0166  0.0026  0.0119  213 TYR A N   
1675 C CA  . TYR A 213 ? 0.2829 0.3193 0.2378 0.0196  0.0025  0.0131  213 TYR A CA  
1676 C C   . TYR A 213 ? 0.2956 0.3276 0.2497 0.0187  0.0032  0.0151  213 TYR A C   
1677 O O   . TYR A 213 ? 0.3640 0.3897 0.3166 0.0189  0.0043  0.0162  213 TYR A O   
1678 C CB  . TYR A 213 ? 0.3177 0.3537 0.2715 0.0241  0.0029  0.0132  213 TYR A CB  
1679 C CG  . TYR A 213 ? 0.3119 0.3502 0.2644 0.0272  0.0021  0.0156  213 TYR A CG  
1680 C CD1 . TYR A 213 ? 0.3345 0.3813 0.2878 0.0269  0.0006  0.0149  213 TYR A CD1 
1681 C CD2 . TYR A 213 ? 0.3058 0.3380 0.2559 0.0297  0.0028  0.0190  213 TYR A CD2 
1682 C CE1 . TYR A 213 ? 0.2677 0.3184 0.2185 0.0290  -0.0006 0.0169  213 TYR A CE1 
1683 C CE2 . TYR A 213 ? 0.3456 0.3811 0.2931 0.0322  0.0018  0.0223  213 TYR A CE2 
1684 C CZ  . TYR A 213 ? 0.3488 0.3944 0.2962 0.0318  -0.0002 0.0210  213 TYR A CZ  
1685 O OH  . TYR A 213 ? 0.3422 0.3931 0.2858 0.0336  -0.0018 0.0238  213 TYR A OH  
1686 N N   . THR A 214 ? 0.2873 0.3224 0.2427 0.0175  0.0033  0.0151  214 THR A N   
1687 C CA  . THR A 214 ? 0.3091 0.3416 0.2637 0.0167  0.0048  0.0166  214 THR A CA  
1688 C C   . THR A 214 ? 0.3257 0.3615 0.2764 0.0186  0.0051  0.0171  214 THR A C   
1689 O O   . THR A 214 ? 0.3657 0.4075 0.3165 0.0191  0.0039  0.0151  214 THR A O   
1690 C CB  . THR A 214 ? 0.3266 0.3604 0.2864 0.0137  0.0056  0.0158  214 THR A CB  
1691 O OG1 . THR A 214 ? 0.4583 0.4965 0.4194 0.0136  0.0060  0.0136  214 THR A OG1 
1692 C CG2 . THR A 214 ? 0.3292 0.3633 0.2927 0.0118  0.0040  0.0158  214 THR A CG2 
1693 N N   . THR A 215 ? 0.2802 0.3129 0.2272 0.0193  0.0065  0.0198  215 THR A N   
1694 C CA  . THR A 215 ? 0.3252 0.3619 0.2667 0.0213  0.0061  0.0215  215 THR A CA  
1695 C C   . THR A 215 ? 0.3580 0.3937 0.2957 0.0197  0.0088  0.0233  215 THR A C   
1696 O O   . THR A 215 ? 0.2838 0.3133 0.2215 0.0190  0.0108  0.0263  215 THR A O   
1697 C CB  . THR A 215 ? 0.3973 0.4322 0.3365 0.0256  0.0045  0.0251  215 THR A CB  
1698 O OG1 . THR A 215 ? 0.3814 0.4213 0.3148 0.0276  0.0036  0.0282  215 THR A OG1 
1699 C CG2 . THR A 215 ? 0.3372 0.3618 0.2769 0.0259  0.0063  0.0281  215 THR A CG2 
1700 N N   . HIS A 216 ? 0.3974 0.4397 0.3322 0.0185  0.0094  0.0208  216 HIS A N   
1701 C CA  . HIS A 216 ? 0.3246 0.3688 0.2522 0.0179  0.0114  0.0232  216 HIS A CA  
1702 C C   . HIS A 216 ? 0.3759 0.4221 0.2972 0.0216  0.0086  0.0286  216 HIS A C   
1703 O O   . HIS A 216 ? 0.3700 0.4233 0.2902 0.0232  0.0052  0.0273  216 HIS A O   
1704 C CB  . HIS A 216 ? 0.3743 0.4257 0.3005 0.0152  0.0130  0.0174  216 HIS A CB  
1705 C CG  . HIS A 216 ? 0.4208 0.4761 0.3381 0.0138  0.0156  0.0187  216 HIS A CG  
1706 N ND1 . HIS A 216 ? 0.3870 0.4450 0.3042 0.0106  0.0200  0.0135  216 HIS A ND1 
1707 C CD2 . HIS A 216 ? 0.4303 0.4878 0.3382 0.0153  0.0147  0.0247  216 HIS A CD2 
1708 C CE1 . HIS A 216 ? 0.3661 0.4283 0.2732 0.0095  0.0220  0.0157  216 HIS A CE1 
1709 N NE2 . HIS A 216 ? 0.4479 0.5099 0.3489 0.0123  0.0185  0.0232  216 HIS A NE2 
1710 N N   . LEU A 217 ? 0.3622 0.4019 0.2806 0.0229  0.0098  0.0351  217 LEU A N   
1711 C CA  . LEU A 217 ? 0.3706 0.4100 0.2851 0.0274  0.0073  0.0419  217 LEU A CA  
1712 C C   . LEU A 217 ? 0.4026 0.4534 0.3090 0.0282  0.0047  0.0435  217 LEU A C   
1713 O O   . LEU A 217 ? 0.4550 0.5119 0.3558 0.0246  0.0064  0.0405  217 LEU A O   
1714 C CB  . LEU A 217 ? 0.3646 0.3942 0.2771 0.0277  0.0101  0.0490  217 LEU A CB  
1715 C CG  . LEU A 217 ? 0.4112 0.4291 0.3309 0.0266  0.0122  0.0481  217 LEU A CG  
1716 C CD1 . LEU A 217 ? 0.3703 0.3791 0.2876 0.0260  0.0154  0.0553  217 LEU A CD1 
1717 C CD2 . LEU A 217 ? 0.2897 0.3047 0.2151 0.0305  0.0096  0.0464  217 LEU A CD2 
1718 N N   . ARG A 218 ? 0.3639 0.4182 0.2699 0.0331  0.0006  0.0482  218 ARG A N   
1719 C CA  . ARG A 218 ? 0.4190 0.4859 0.3171 0.0340  -0.0029 0.0509  218 ARG A CA  
1720 C C   . ARG A 218 ? 0.4033 0.4706 0.2907 0.0321  -0.0006 0.0568  218 ARG A C   
1721 O O   . ARG A 218 ? 0.4516 0.5308 0.3302 0.0303  -0.0024 0.0565  218 ARG A O   
1722 C CB  . ARG A 218 ? 0.3975 0.4680 0.2988 0.0406  -0.0077 0.0568  218 ARG A CB  
1723 C CG  . ARG A 218 ? 0.4710 0.5587 0.3672 0.0409  -0.0129 0.0570  218 ARG A CG  
1724 C CD  . ARG A 218 ? 0.4710 0.5648 0.3741 0.0473  -0.0178 0.0608  218 ARG A CD  
1725 N NE  . ARG A 218 ? 0.4534 0.5454 0.3676 0.0478  -0.0175 0.0538  218 ARG A NE  
1726 C CZ  . ARG A 218 ? 0.4761 0.5801 0.3942 0.0460  -0.0202 0.0472  218 ARG A CZ  
1727 N NH1 . ARG A 218 ? 0.3171 0.4349 0.2290 0.0422  -0.0232 0.0442  218 ARG A NH1 
1728 N NH2 . ARG A 218 ? 0.3579 0.4603 0.2862 0.0476  -0.0198 0.0432  218 ARG A NH2 
1729 N N   . SER A 219 ? 0.3577 0.4130 0.2455 0.0320  0.0034  0.0619  219 SER A N   
1730 C CA  . SER A 219 ? 0.4349 0.4898 0.3132 0.0291  0.0069  0.0674  219 SER A CA  
1731 C C   . SER A 219 ? 0.4369 0.4786 0.3202 0.0264  0.0126  0.0677  219 SER A C   
1732 O O   . SER A 219 ? 0.5263 0.5571 0.4178 0.0286  0.0128  0.0691  219 SER A O   
1733 C CB  . SER A 219 ? 0.4471 0.5038 0.3182 0.0334  0.0041  0.0798  219 SER A CB  
1734 O OG  . SER A 219 ? 0.4900 0.5461 0.3510 0.0300  0.0081  0.0858  219 SER A OG  
1735 N N   . GLU A 220 ? 0.4556 0.4992 0.3342 0.0213  0.0175  0.0657  220 GLU A N   
1736 C CA  . GLU A 220 ? 0.5291 0.5626 0.4121 0.0180  0.0230  0.0670  220 GLU A CA  
1737 C C   . GLU A 220 ? 0.5384 0.5704 0.4122 0.0164  0.0266  0.0766  220 GLU A C   
1738 O O   . GLU A 220 ? 0.4700 0.4978 0.3454 0.0120  0.0323  0.0770  220 GLU A O   
1739 C CB  . GLU A 220 ? 0.4348 0.4714 0.3233 0.0135  0.0267  0.0571  220 GLU A CB  
1740 C CG  . GLU A 220 ? 0.4787 0.5155 0.3768 0.0147  0.0237  0.0489  220 GLU A CG  
1741 C CD  . GLU A 220 ? 0.5416 0.5783 0.4482 0.0110  0.0274  0.0417  220 GLU A CD  
1742 O OE1 . GLU A 220 ? 0.4771 0.5203 0.3810 0.0082  0.0311  0.0378  220 GLU A OE1 
1743 O OE2 . GLU A 220 ? 0.4288 0.4593 0.3449 0.0110  0.0266  0.0399  220 GLU A OE2 
1744 N N   . PHE A 221 ? 0.4777 0.5140 0.3423 0.0197  0.0232  0.0851  221 PHE A N   
1745 C CA  . PHE A 221 ? 0.4573 0.4937 0.3112 0.0183  0.0260  0.0958  221 PHE A CA  
1746 C C   . PHE A 221 ? 0.4703 0.4960 0.3258 0.0235  0.0237  0.1083  221 PHE A C   
1747 O O   . PHE A 221 ? 0.5070 0.5196 0.3738 0.0254  0.0242  0.1077  221 PHE A O   
1748 C CB  . PHE A 221 ? 0.4766 0.5296 0.3163 0.0168  0.0244  0.0955  221 PHE A CB  
1749 C CG  . PHE A 221 ? 0.4606 0.5220 0.2990 0.0111  0.0287  0.0831  221 PHE A CG  
1750 C CD1 . PHE A 221 ? 0.4984 0.5645 0.3433 0.0113  0.0261  0.0712  221 PHE A CD1 
1751 C CD2 . PHE A 221 ? 0.5194 0.5831 0.3512 0.0057  0.0358  0.0834  221 PHE A CD2 
1752 C CE1 . PHE A 221 ? 0.4781 0.5502 0.3236 0.0067  0.0305  0.0601  221 PHE A CE1 
1753 C CE2 . PHE A 221 ? 0.5065 0.5774 0.3389 0.0012  0.0405  0.0715  221 PHE A CE2 
1754 C CZ  . PHE A 221 ? 0.4203 0.4948 0.2600 0.0020  0.0377  0.0599  221 PHE A CZ  
1755 N N   . GLU A 222 ? 0.5072 0.5383 0.3520 0.0260  0.0213  0.1196  222 GLU A N   
1756 C CA  A GLU A 222 ? 0.5682 0.5876 0.4154 0.0313  0.0200  0.1330  222 GLU A CA  
1757 C CA  B GLU A 222 ? 0.5681 0.5874 0.4154 0.0313  0.0201  0.1330  222 GLU A CA  
1758 C C   . GLU A 222 ? 0.5684 0.5806 0.4286 0.0380  0.0157  0.1306  222 GLU A C   
1759 O O   . GLU A 222 ? 0.6051 0.6007 0.4745 0.0397  0.0183  0.1339  222 GLU A O   
1760 C CB  A GLU A 222 ? 0.5714 0.6009 0.4049 0.0337  0.0167  0.1461  222 GLU A CB  
1761 C CB  B GLU A 222 ? 0.5716 0.6008 0.4052 0.0337  0.0168  0.1462  222 GLU A CB  
1762 C CG  A GLU A 222 ? 0.6489 0.6649 0.4834 0.0380  0.0174  0.1627  222 GLU A CG  
1763 C CG  B GLU A 222 ? 0.6487 0.6644 0.4842 0.0385  0.0170  0.1625  222 GLU A CG  
1764 C CD  A GLU A 222 ? 0.7791 0.8066 0.5998 0.0410  0.0130  0.1773  222 GLU A CD  
1765 C CD  B GLU A 222 ? 0.7221 0.7362 0.5660 0.0481  0.0102  0.1673  222 GLU A CD  
1766 O OE1 A GLU A 222 ? 0.8767 0.9198 0.6940 0.0449  0.0057  0.1762  222 GLU A OE1 
1767 O OE1 B GLU A 222 ? 0.6357 0.6632 0.4809 0.0507  0.0044  0.1597  222 GLU A OE1 
1768 O OE2 A GLU A 222 ? 0.7279 0.7495 0.5413 0.0391  0.0168  0.1903  222 GLU A OE2 
1769 O OE2 B GLU A 222 ? 0.7452 0.7447 0.5953 0.0531  0.0110  0.1785  222 GLU A OE2 
1770 N N   . PRO A 223 ? 0.5492 0.5730 0.4110 0.0416  0.0098  0.1246  223 PRO A N   
1771 C CA  . PRO A 223 ? 0.5449 0.5625 0.4192 0.0481  0.0065  0.1229  223 PRO A CA  
1772 C C   . PRO A 223 ? 0.5008 0.5118 0.3856 0.0455  0.0088  0.1099  223 PRO A C   
1773 O O   . PRO A 223 ? 0.5307 0.5441 0.4232 0.0492  0.0055  0.1041  223 PRO A O   
1774 C CB  . PRO A 223 ? 0.4861 0.5216 0.3572 0.0524  -0.0009 0.1230  223 PRO A CB  
1775 C CG  . PRO A 223 ? 0.4811 0.5311 0.3407 0.0458  -0.0007 0.1169  223 PRO A CG  
1776 C CD  . PRO A 223 ? 0.5044 0.5481 0.3561 0.0402  0.0057  0.1212  223 PRO A CD  
1777 N N   . ILE A 224 ? 0.4825 0.4858 0.3683 0.0392  0.0144  0.1057  224 ILE A N   
1778 C CA  . ILE A 224 ? 0.4803 0.4801 0.3750 0.0362  0.0158  0.0937  224 ILE A CA  
1779 C C   . ILE A 224 ? 0.4080 0.3952 0.3134 0.0402  0.0155  0.0928  224 ILE A C   
1780 O O   . ILE A 224 ? 0.4510 0.4394 0.3629 0.0403  0.0142  0.0837  224 ILE A O   
1781 C CB  . ILE A 224 ? 0.4959 0.4921 0.3904 0.0287  0.0215  0.0901  224 ILE A CB  
1782 C CG1 . ILE A 224 ? 0.4181 0.4132 0.3217 0.0259  0.0219  0.0786  224 ILE A CG1 
1783 C CG2 . ILE A 224 ? 0.4384 0.4202 0.3343 0.0271  0.0261  0.0983  224 ILE A CG2 
1784 C CD1 . ILE A 224 ? 0.4340 0.4294 0.3390 0.0191  0.0266  0.0745  224 ILE A CD1 
1785 N N   . LEU A 225 ? 0.4124 0.3870 0.3198 0.0434  0.0172  0.1020  225 LEU A N   
1786 C CA  . LEU A 225 ? 0.4746 0.4367 0.3924 0.0474  0.0176  0.0999  225 LEU A CA  
1787 C C   . LEU A 225 ? 0.4662 0.4372 0.3879 0.0545  0.0126  0.0978  225 LEU A C   
1788 O O   . LEU A 225 ? 0.5115 0.4797 0.4408 0.0556  0.0125  0.0897  225 LEU A O   
1789 C CB  . LEU A 225 ? 0.3936 0.3394 0.3138 0.0500  0.0208  0.1105  225 LEU A CB  
1790 C CG  . LEU A 225 ? 0.5215 0.4565 0.4405 0.0422  0.0266  0.1119  225 LEU A CG  
1791 C CD1 . LEU A 225 ? 0.4215 0.3406 0.3422 0.0447  0.0298  0.1241  225 LEU A CD1 
1792 C CD2 . LEU A 225 ? 0.3897 0.3186 0.3161 0.0365  0.0292  0.0999  225 LEU A CD2 
1793 N N   . GLU A 226 ? 0.4389 0.4217 0.3550 0.0588  0.0083  0.1051  226 GLU A N   
1794 C CA  A GLU A 226 ? 0.4870 0.4815 0.4074 0.0648  0.0032  0.1028  226 GLU A CA  
1795 C CA  C GLU A 226 ? 0.4871 0.4815 0.4074 0.0648  0.0032  0.1028  226 GLU A CA  
1796 C C   . GLU A 226 ? 0.4480 0.4524 0.3693 0.0605  0.0020  0.0900  226 GLU A C   
1797 O O   . GLU A 226 ? 0.4589 0.4653 0.3880 0.0634  0.0008  0.0840  226 GLU A O   
1798 C CB  A GLU A 226 ? 0.5014 0.5096 0.4145 0.0687  -0.0019 0.1128  226 GLU A CB  
1799 C CB  C GLU A 226 ? 0.5015 0.5099 0.4148 0.0688  -0.0019 0.1126  226 GLU A CB  
1800 C CG  A GLU A 226 ? 0.5302 0.5538 0.4479 0.0745  -0.0079 0.1115  226 GLU A CG  
1801 C CG  C GLU A 226 ? 0.5381 0.5405 0.4437 0.0688  -0.0004 0.1259  226 GLU A CG  
1802 C CD  A GLU A 226 ? 0.6877 0.7262 0.5972 0.0775  -0.0134 0.1220  226 GLU A CD  
1803 C CD  C GLU A 226 ? 0.5907 0.5752 0.5046 0.0747  0.0022  0.1346  226 GLU A CD  
1804 O OE1 A GLU A 226 ? 0.5923 0.6266 0.4933 0.0765  -0.0122 0.1321  226 GLU A OE1 
1805 O OE1 C GLU A 226 ? 0.6106 0.5901 0.5362 0.0803  0.0019  0.1308  226 GLU A OE1 
1806 O OE2 A GLU A 226 ? 0.7783 0.8336 0.6896 0.0803  -0.0191 0.1202  226 GLU A OE2 
1807 O OE2 C GLU A 226 ? 0.5803 0.5554 0.4894 0.0736  0.0051  0.1450  226 GLU A OE2 
1808 N N   . ALA A 227 ? 0.4220 0.4324 0.3359 0.0536  0.0030  0.0859  227 ALA A N   
1809 C CA  . ALA A 227 ? 0.4116 0.4300 0.3271 0.0495  0.0023  0.0747  227 ALA A CA  
1810 C C   . ALA A 227 ? 0.4074 0.4152 0.3307 0.0472  0.0054  0.0675  227 ALA A C   
1811 O O   . ALA A 227 ? 0.4045 0.4168 0.3324 0.0470  0.0041  0.0600  227 ALA A O   
1812 C CB  . ALA A 227 ? 0.3820 0.4079 0.2891 0.0432  0.0035  0.0722  227 ALA A CB  
1813 N N   . LEU A 228 ? 0.3895 0.3838 0.3138 0.0449  0.0095  0.0696  228 LEU A N   
1814 C CA  . LEU A 228 ? 0.4056 0.3904 0.3368 0.0425  0.0119  0.0629  228 LEU A CA  
1815 C C   . LEU A 228 ? 0.4701 0.4516 0.4081 0.0483  0.0109  0.0613  228 LEU A C   
1816 O O   . LEU A 228 ? 0.3770 0.3594 0.3192 0.0471  0.0109  0.0533  228 LEU A O   
1817 C CB  . LEU A 228 ? 0.3950 0.3662 0.3268 0.0386  0.0163  0.0657  228 LEU A CB  
1818 C CG  . LEU A 228 ? 0.4201 0.3939 0.3489 0.0314  0.0186  0.0638  228 LEU A CG  
1819 C CD1 . LEU A 228 ? 0.3857 0.3471 0.3151 0.0282  0.0230  0.0688  228 LEU A CD1 
1820 C CD2 . LEU A 228 ? 0.3430 0.3203 0.2763 0.0274  0.0181  0.0541  228 LEU A CD2 
1821 N N   . ASP A 229 ? 0.4596 0.4377 0.3988 0.0549  0.0102  0.0692  229 ASP A N   
1822 C CA  . ASP A 229 ? 0.4639 0.4390 0.4113 0.0615  0.0100  0.0680  229 ASP A CA  
1823 C C   . ASP A 229 ? 0.4539 0.4443 0.4034 0.0633  0.0064  0.0622  229 ASP A C   
1824 O O   . ASP A 229 ? 0.5112 0.5004 0.4669 0.0646  0.0075  0.0556  229 ASP A O   
1825 C CB  . ASP A 229 ? 0.4571 0.4272 0.4063 0.0690  0.0095  0.0792  229 ASP A CB  
1826 C CG  . ASP A 229 ? 0.5544 0.5206 0.5141 0.0768  0.0101  0.0782  229 ASP A CG  
1827 O OD1 . ASP A 229 ? 0.6661 0.6180 0.6313 0.0761  0.0146  0.0732  229 ASP A OD1 
1828 O OD2 . ASP A 229 ? 0.6510 0.6290 0.6138 0.0833  0.0062  0.0817  229 ASP A OD2 
1829 N N   . GLU A 230 ? 0.3911 0.3960 0.3354 0.0627  0.0025  0.0641  230 GLU A N   
1830 C CA  . GLU A 230 ? 0.4391 0.4586 0.3857 0.0629  -0.0007 0.0583  230 GLU A CA  
1831 C C   . GLU A 230 ? 0.4132 0.4320 0.3608 0.0568  0.0012  0.0485  230 GLU A C   
1832 O O   . GLU A 230 ? 0.4049 0.4281 0.3577 0.0578  0.0010  0.0430  230 GLU A O   
1833 C CB  . GLU A 230 ? 0.3756 0.4098 0.3156 0.0617  -0.0048 0.0611  230 GLU A CB  
1834 C CG  . GLU A 230 ? 0.3959 0.4446 0.3385 0.0602  -0.0077 0.0542  230 GLU A CG  
1835 C CD  . GLU A 230 ? 0.4692 0.5320 0.4047 0.0571  -0.0112 0.0545  230 GLU A CD  
1836 O OE1 . GLU A 230 ? 0.4758 0.5364 0.4031 0.0533  -0.0101 0.0564  230 GLU A OE1 
1837 O OE2 . GLU A 230 ? 0.4270 0.5036 0.3655 0.0581  -0.0149 0.0522  230 GLU A OE2 
1838 N N   . ALA A 231 ? 0.3696 0.3840 0.3124 0.0505  0.0030  0.0467  231 ALA A N   
1839 C CA  . ALA A 231 ? 0.3853 0.3994 0.3297 0.0451  0.0042  0.0389  231 ALA A CA  
1840 C C   . ALA A 231 ? 0.4152 0.4212 0.3648 0.0461  0.0065  0.0349  231 ALA A C   
1841 O O   . ALA A 231 ? 0.4221 0.4330 0.3744 0.0451  0.0062  0.0292  231 ALA A O   
1842 C CB  . ALA A 231 ? 0.3566 0.3665 0.2972 0.0391  0.0061  0.0385  231 ALA A CB  
1843 N N   . PHE A 232 ? 0.3343 0.3276 0.2851 0.0478  0.0092  0.0376  232 PHE A N   
1844 C CA  . PHE A 232 ? 0.4000 0.3845 0.3552 0.0480  0.0121  0.0324  232 PHE A CA  
1845 C C   . PHE A 232 ? 0.4023 0.3922 0.3630 0.0541  0.0118  0.0304  232 PHE A C   
1846 O O   . PHE A 232 ? 0.4051 0.3955 0.3681 0.0529  0.0135  0.0234  232 PHE A O   
1847 C CB  . PHE A 232 ? 0.3480 0.3167 0.3042 0.0483  0.0154  0.0357  232 PHE A CB  
1848 C CG  . PHE A 232 ? 0.4231 0.3873 0.3753 0.0418  0.0164  0.0374  232 PHE A CG  
1849 C CD1 . PHE A 232 ? 0.3446 0.3172 0.2938 0.0360  0.0148  0.0342  232 PHE A CD1 
1850 C CD2 . PHE A 232 ? 0.4035 0.3549 0.3560 0.0414  0.0192  0.0425  232 PHE A CD2 
1851 C CE1 . PHE A 232 ? 0.3657 0.3354 0.3129 0.0305  0.0160  0.0357  232 PHE A CE1 
1852 C CE2 . PHE A 232 ? 0.3921 0.3405 0.3419 0.0350  0.0205  0.0440  232 PHE A CE2 
1853 C CZ  . PHE A 232 ? 0.3805 0.3387 0.3279 0.0298  0.0189  0.0404  232 PHE A CZ  
1854 N N   . ARG A 233 ? 0.3618 0.3569 0.3247 0.0607  0.0098  0.0367  233 ARG A N   
1855 C CA  . ARG A 233 ? 0.3296 0.3328 0.2994 0.0670  0.0091  0.0353  233 ARG A CA  
1856 C C   . ARG A 233 ? 0.3512 0.3681 0.3208 0.0634  0.0075  0.0292  233 ARG A C   
1857 O O   . ARG A 233 ? 0.3739 0.3943 0.3485 0.0650  0.0093  0.0239  233 ARG A O   
1858 C CB  . ARG A 233 ? 0.3733 0.3828 0.3453 0.0740  0.0059  0.0444  233 ARG A CB  
1859 C CG  . ARG A 233 ? 0.5360 0.5363 0.5162 0.0825  0.0082  0.0487  233 ARG A CG  
1860 C CD  . ARG A 233 ? 0.5446 0.5493 0.5258 0.0892  0.0045  0.0604  233 ARG A CD  
1861 N NE  . ARG A 233 ? 0.5602 0.5848 0.5389 0.0890  -0.0013 0.0624  233 ARG A NE  
1862 C CZ  . ARG A 233 ? 0.6521 0.6916 0.6382 0.0933  -0.0038 0.0608  233 ARG A CZ  
1863 N NH1 . ARG A 233 ? 0.4360 0.4737 0.4329 0.0987  -0.0007 0.0571  233 ARG A NH1 
1864 N NH2 . ARG A 233 ? 0.5695 0.6265 0.5522 0.0917  -0.0092 0.0624  233 ARG A NH2 
1865 N N   . ILE A 234 ? 0.3626 0.3871 0.3267 0.0586  0.0045  0.0298  234 ILE A N   
1866 C CA  . ILE A 234 ? 0.2953 0.3307 0.2596 0.0545  0.0034  0.0244  234 ILE A CA  
1867 C C   . ILE A 234 ? 0.3984 0.4280 0.3621 0.0500  0.0064  0.0181  234 ILE A C   
1868 O O   . ILE A 234 ? 0.4127 0.4486 0.3790 0.0492  0.0073  0.0136  234 ILE A O   
1869 C CB  . ILE A 234 ? 0.3307 0.3724 0.2896 0.0500  0.0006  0.0257  234 ILE A CB  
1870 C CG1 . ILE A 234 ? 0.2833 0.3344 0.2420 0.0539  -0.0030 0.0309  234 ILE A CG1 
1871 C CG2 . ILE A 234 ? 0.2949 0.3435 0.2543 0.0446  0.0003  0.0202  234 ILE A CG2 
1872 C CD1 . ILE A 234 ? 0.3532 0.4066 0.3047 0.0500  -0.0046 0.0329  234 ILE A CD1 
1873 N N   . GLY A 235 ? 0.3460 0.3641 0.3061 0.0466  0.0081  0.0180  235 GLY A N   
1874 C CA  . GLY A 235 ? 0.3812 0.3946 0.3401 0.0419  0.0104  0.0122  235 GLY A CA  
1875 C C   . GLY A 235 ? 0.3916 0.4022 0.3542 0.0451  0.0137  0.0077  235 GLY A C   
1876 O O   . GLY A 235 ? 0.3981 0.4125 0.3599 0.0420  0.0150  0.0022  235 GLY A O   
1877 N N   . ARG A 236 ? 0.3630 0.3669 0.3299 0.0515  0.0154  0.0101  236 ARG A N   
1878 C CA  . ARG A 236 ? 0.4321 0.4323 0.4040 0.0552  0.0196  0.0050  236 ARG A CA  
1879 C C   . ARG A 236 ? 0.4314 0.4454 0.4083 0.0589  0.0194  0.0032  236 ARG A C   
1880 O O   . ARG A 236 ? 0.3892 0.4048 0.3681 0.0587  0.0231  -0.0035 236 ARG A O   
1881 C CB  . ARG A 236 ? 0.3617 0.3493 0.3386 0.0616  0.0220  0.0086  236 ARG A CB  
1882 C CG  . ARG A 236 ? 0.3763 0.3485 0.3494 0.0570  0.0238  0.0085  236 ARG A CG  
1883 C CD  . ARG A 236 ? 0.3791 0.3363 0.3584 0.0626  0.0277  0.0102  236 ARG A CD  
1884 N NE  . ARG A 236 ? 0.5303 0.4892 0.5144 0.0709  0.0257  0.0200  236 ARG A NE  
1885 C CZ  . ARG A 236 ? 0.5041 0.4611 0.4848 0.0709  0.0229  0.0291  236 ARG A CZ  
1886 N NH1 . ARG A 236 ? 0.4209 0.3742 0.3944 0.0632  0.0223  0.0294  236 ARG A NH1 
1887 N NH2 . ARG A 236 ? 0.4072 0.3670 0.3918 0.0786  0.0208  0.0384  236 ARG A NH2 
1888 N N   . HIS A 237 ? 0.3644 0.3896 0.3434 0.0616  0.0154  0.0086  237 HIS A N   
1889 C CA  . HIS A 237 ? 0.3736 0.4133 0.3588 0.0645  0.0151  0.0069  237 HIS A CA  
1890 C C   . HIS A 237 ? 0.3340 0.3806 0.3156 0.0576  0.0161  0.0011  237 HIS A C   
1891 O O   . HIS A 237 ? 0.3576 0.4094 0.3429 0.0583  0.0196  -0.0039 237 HIS A O   
1892 C CB  . HIS A 237 ? 0.3051 0.3563 0.2925 0.0672  0.0100  0.0132  237 HIS A CB  
1893 C CG  . HIS A 237 ? 0.3653 0.4312 0.3622 0.0722  0.0097  0.0128  237 HIS A CG  
1894 N ND1 . HIS A 237 ? 0.3876 0.4667 0.3859 0.0681  0.0093  0.0090  237 HIS A ND1 
1895 C CD2 . HIS A 237 ? 0.2873 0.3572 0.2937 0.0810  0.0097  0.0160  237 HIS A CD2 
1896 C CE1 . HIS A 237 ? 0.2766 0.3681 0.2850 0.0737  0.0092  0.0093  237 HIS A CE1 
1897 N NE2 . HIS A 237 ? 0.3731 0.4597 0.3869 0.0819  0.0092  0.0136  237 HIS A NE2 
1898 N N   . GLY A 238 ? 0.3409 0.3879 0.3158 0.0510  0.0134  0.0022  238 GLY A N   
1899 C CA  . GLY A 238 ? 0.4509 0.5035 0.4225 0.0444  0.0139  -0.0014 238 GLY A CA  
1900 C C   . GLY A 238 ? 0.4461 0.4912 0.4126 0.0402  0.0170  -0.0062 238 GLY A C   
1901 O O   . GLY A 238 ? 0.4764 0.5273 0.4403 0.0357  0.0181  -0.0093 238 GLY A O   
1902 N N   . ASN A 239 ? 0.3784 0.4111 0.3432 0.0412  0.0183  -0.0069 239 ASN A N   
1903 C CA  . ASN A 239 ? 0.4751 0.5004 0.4341 0.0358  0.0204  -0.0117 239 ASN A CA  
1904 C C   . ASN A 239 ? 0.4425 0.4705 0.3959 0.0287  0.0169  -0.0096 239 ASN A C   
1905 O O   . ASN A 239 ? 0.4745 0.5071 0.4236 0.0235  0.0171  -0.0123 239 ASN A O   
1906 C CB  . ASN A 239 ? 0.4075 0.4365 0.3663 0.0354  0.0249  -0.0188 239 ASN A CB  
1907 C CG  . ASN A 239 ? 0.5492 0.5689 0.5027 0.0312  0.0277  -0.0252 239 ASN A CG  
1908 O OD1 . ASN A 239 ? 0.6417 0.6535 0.5919 0.0276  0.0258  -0.0240 239 ASN A OD1 
1909 N ND2 . ASN A 239 ? 0.6817 0.7033 0.6346 0.0312  0.0326  -0.0326 239 ASN A ND2 
1910 N N   . VAL A 240 ? 0.3794 0.4047 0.3330 0.0286  0.0139  -0.0044 240 VAL A N   
1911 C CA  . VAL A 240 ? 0.3957 0.4237 0.3465 0.0233  0.0108  -0.0018 240 VAL A CA  
1912 C C   . VAL A 240 ? 0.3384 0.3577 0.2882 0.0219  0.0099  0.0005  240 VAL A C   
1913 O O   . VAL A 240 ? 0.3471 0.3599 0.2985 0.0258  0.0108  0.0025  240 VAL A O   
1914 C CB  . VAL A 240 ? 0.3665 0.4032 0.3200 0.0243  0.0085  0.0017  240 VAL A CB  
1915 C CG1 . VAL A 240 ? 0.3351 0.3806 0.2911 0.0258  0.0099  -0.0005 240 VAL A CG1 
1916 C CG2 . VAL A 240 ? 0.3098 0.3446 0.2654 0.0285  0.0073  0.0055  240 VAL A CG2 
1917 N N   . PRO A 241 ? 0.3509 0.3704 0.2986 0.0164  0.0082  0.0009  241 PRO A N   
1918 C CA  . PRO A 241 ? 0.3246 0.3375 0.2727 0.0146  0.0077  0.0031  241 PRO A CA  
1919 C C   . PRO A 241 ? 0.4111 0.4255 0.3612 0.0169  0.0066  0.0080  241 PRO A C   
1920 O O   . PRO A 241 ? 0.3205 0.3421 0.2717 0.0177  0.0052  0.0094  241 PRO A O   
1921 C CB  . PRO A 241 ? 0.3530 0.3693 0.2998 0.0084  0.0057  0.0024  241 PRO A CB  
1922 C CG  . PRO A 241 ? 0.3955 0.4211 0.3416 0.0077  0.0044  0.0027  241 PRO A CG  
1923 C CD  . PRO A 241 ? 0.2804 0.3072 0.2261 0.0117  0.0067  0.0002  241 PRO A CD  
1924 N N   . VAL A 242 ? 0.3563 0.3636 0.3065 0.0175  0.0076  0.0103  242 VAL A N   
1925 C CA  . VAL A 242 ? 0.3448 0.3532 0.2953 0.0194  0.0073  0.0147  242 VAL A CA  
1926 C C   . VAL A 242 ? 0.3880 0.3951 0.3395 0.0151  0.0074  0.0162  242 VAL A C   
1927 O O   . VAL A 242 ? 0.3513 0.3531 0.3035 0.0119  0.0083  0.0151  242 VAL A O   
1928 C CB  . VAL A 242 ? 0.3724 0.3747 0.3221 0.0242  0.0088  0.0177  242 VAL A CB  
1929 C CG1 . VAL A 242 ? 0.2911 0.2958 0.2390 0.0253  0.0083  0.0225  242 VAL A CG1 
1930 C CG2 . VAL A 242 ? 0.3417 0.3466 0.2925 0.0291  0.0087  0.0164  242 VAL A CG2 
1931 N N   . VAL A 243 ? 0.3262 0.3388 0.2786 0.0149  0.0068  0.0180  243 VAL A N   
1932 C CA  . VAL A 243 ? 0.3359 0.3482 0.2903 0.0120  0.0078  0.0197  243 VAL A CA  
1933 C C   . VAL A 243 ? 0.3065 0.3195 0.2582 0.0144  0.0092  0.0226  243 VAL A C   
1934 O O   . VAL A 243 ? 0.3387 0.3574 0.2892 0.0163  0.0083  0.0221  243 VAL A O   
1935 C CB  . VAL A 243 ? 0.3385 0.3572 0.2976 0.0092  0.0065  0.0188  243 VAL A CB  
1936 C CG1 . VAL A 243 ? 0.3412 0.3603 0.3040 0.0069  0.0083  0.0204  243 VAL A CG1 
1937 C CG2 . VAL A 243 ? 0.3076 0.3275 0.2681 0.0065  0.0044  0.0169  243 VAL A CG2 
1938 N N   . VAL A 244 ? 0.3586 0.3662 0.3089 0.0137  0.0115  0.0255  244 VAL A N   
1939 C CA  . VAL A 244 ? 0.3010 0.3101 0.2473 0.0150  0.0132  0.0289  244 VAL A CA  
1940 C C   . VAL A 244 ? 0.3420 0.3562 0.2912 0.0119  0.0149  0.0278  244 VAL A C   
1941 O O   . VAL A 244 ? 0.3711 0.3833 0.3244 0.0085  0.0167  0.0281  244 VAL A O   
1942 C CB  . VAL A 244 ? 0.3856 0.3864 0.3289 0.0156  0.0153  0.0337  244 VAL A CB  
1943 C CG1 . VAL A 244 ? 0.2789 0.2826 0.2168 0.0162  0.0172  0.0380  244 VAL A CG1 
1944 C CG2 . VAL A 244 ? 0.2785 0.2739 0.2206 0.0200  0.0140  0.0348  244 VAL A CG2 
1945 N N   . SER A 245 ? 0.3255 0.3465 0.2735 0.0128  0.0147  0.0260  245 SER A N   
1946 C CA  . SER A 245 ? 0.3462 0.3718 0.2981 0.0106  0.0171  0.0238  245 SER A CA  
1947 C C   . SER A 245 ? 0.3688 0.3941 0.3176 0.0090  0.0212  0.0264  245 SER A C   
1948 O O   . SER A 245 ? 0.3449 0.3685 0.2860 0.0103  0.0218  0.0300  245 SER A O   
1949 C CB  . SER A 245 ? 0.3206 0.3523 0.2719 0.0116  0.0164  0.0201  245 SER A CB  
1950 O OG  . SER A 245 ? 0.3677 0.4001 0.3215 0.0127  0.0131  0.0184  245 SER A OG  
1951 N N   . HIS A 246 ? 0.4006 0.4285 0.3560 0.0064  0.0241  0.0249  246 HIS A N   
1952 C CA  . HIS A 246 ? 0.3862 0.4154 0.3405 0.0042  0.0291  0.0266  246 HIS A CA  
1953 C C   . HIS A 246 ? 0.3735 0.3974 0.3192 0.0042  0.0300  0.0323  246 HIS A C   
1954 O O   . HIS A 246 ? 0.3866 0.4129 0.3240 0.0044  0.0324  0.0344  246 HIS A O   
1955 C CB  . HIS A 246 ? 0.3532 0.3892 0.3057 0.0043  0.0324  0.0228  246 HIS A CB  
1956 C CG  . HIS A 246 ? 0.4016 0.4400 0.3455 0.0065  0.0300  0.0210  246 HIS A CG  
1957 N ND1 . HIS A 246 ? 0.3568 0.3942 0.2902 0.0080  0.0283  0.0252  246 HIS A ND1 
1958 C CD2 . HIS A 246 ? 0.4043 0.4469 0.3495 0.0072  0.0292  0.0155  246 HIS A CD2 
1959 C CE1 . HIS A 246 ? 0.3790 0.4214 0.3075 0.0094  0.0260  0.0222  246 HIS A CE1 
1960 N NE2 . HIS A 246 ? 0.3766 0.4218 0.3120 0.0085  0.0267  0.0159  246 HIS A NE2 
1961 N N   . HIS A 247 ? 0.3836 0.4000 0.3311 0.0037  0.0284  0.0350  247 HIS A N   
1962 C CA  . HIS A 247 ? 0.4074 0.4166 0.3485 0.0042  0.0294  0.0410  247 HIS A CA  
1963 C C   . HIS A 247 ? 0.4227 0.4327 0.3619 0.0008  0.0349  0.0446  247 HIS A C   
1964 O O   . HIS A 247 ? 0.3780 0.3897 0.3248 -0.0032 0.0378  0.0431  247 HIS A O   
1965 C CB  . HIS A 247 ? 0.3619 0.3618 0.3071 0.0034  0.0278  0.0416  247 HIS A CB  
1966 C CG  . HIS A 247 ? 0.4578 0.4482 0.3980 0.0046  0.0291  0.0478  247 HIS A CG  
1967 N ND1 . HIS A 247 ? 0.4282 0.4185 0.3603 0.0092  0.0280  0.0524  247 HIS A ND1 
1968 C CD2 . HIS A 247 ? 0.3678 0.3481 0.3105 0.0017  0.0314  0.0507  247 HIS A CD2 
1969 C CE1 . HIS A 247 ? 0.3923 0.3725 0.3227 0.0098  0.0296  0.0586  247 HIS A CE1 
1970 N NE2 . HIS A 247 ? 0.4278 0.4010 0.3645 0.0052  0.0320  0.0574  247 HIS A NE2 
1971 N N   . LYS A 248 ? 0.4606 0.4705 0.3897 0.0022  0.0362  0.0498  248 LYS A N   
1972 C CA  . LYS A 248 ? 0.3819 0.3933 0.3065 -0.0010 0.0417  0.0544  248 LYS A CA  
1973 C C   . LYS A 248 ? 0.4017 0.4088 0.3153 0.0016  0.0411  0.0629  248 LYS A C   
1974 O O   . LYS A 248 ? 0.4595 0.4661 0.3691 0.0063  0.0364  0.0639  248 LYS A O   
1975 C CB  . LYS A 248 ? 0.4219 0.4447 0.3443 -0.0022 0.0449  0.0497  248 LYS A CB  
1976 C CG  . LYS A 248 ? 0.3981 0.4272 0.3114 0.0013  0.0417  0.0477  248 LYS A CG  
1977 C CD  . LYS A 248 ? 0.4219 0.4614 0.3314 -0.0007 0.0459  0.0425  248 LYS A CD  
1978 C CE  . LYS A 248 ? 0.4014 0.4444 0.3225 -0.0011 0.0466  0.0336  248 LYS A CE  
1979 N NZ  . LYS A 248 ? 0.4809 0.5231 0.4047 0.0023  0.0404  0.0299  248 LYS A NZ  
1980 N N   . CYS A 249 ? 0.3955 0.4002 0.3049 -0.0016 0.0460  0.0696  249 CYS A N   
1981 C CA  . CYS A 249 ? 0.3994 0.4025 0.2968 0.0004  0.0462  0.0793  249 CYS A CA  
1982 C C   . CYS A 249 ? 0.4632 0.4778 0.3512 -0.0025 0.0505  0.0796  249 CYS A C   
1983 O O   . CYS A 249 ? 0.4778 0.4927 0.3662 -0.0075 0.0569  0.0818  249 CYS A O   
1984 C CB  . CYS A 249 ? 0.4632 0.4528 0.3625 -0.0011 0.0488  0.0881  249 CYS A CB  
1985 S SG  . CYS A 249 ? 0.4753 0.4511 0.3818 0.0038  0.0437  0.0886  249 CYS A SG  
1986 N N   . ALA A 250 ? 0.4239 0.4486 0.3036 0.0000  0.0475  0.0766  250 ALA A N   
1987 C CA  . ALA A 250 ? 0.4829 0.5197 0.3534 -0.0030 0.0516  0.0738  250 ALA A CA  
1988 C C   . ALA A 250 ? 0.5157 0.5555 0.3706 -0.0033 0.0525  0.0845  250 ALA A C   
1989 O O   . ALA A 250 ? 0.4539 0.4898 0.3040 0.0010  0.0473  0.0928  250 ALA A O   
1990 C CB  . ALA A 250 ? 0.4210 0.4675 0.2909 -0.0013 0.0483  0.0636  250 ALA A CB  
1991 N N   . GLY A 251 ? 0.4765 0.5240 0.3236 -0.0081 0.0591  0.0847  251 GLY A N   
1992 C CA  . GLY A 251 ? 0.4372 0.4892 0.2678 -0.0092 0.0604  0.0953  251 GLY A CA  
1993 C C   . GLY A 251 ? 0.4791 0.5207 0.3102 -0.0118 0.0652  0.1072  251 GLY A C   
1994 O O   . GLY A 251 ? 0.4680 0.4960 0.3102 -0.0102 0.0637  0.1107  251 GLY A O   
1995 N N   . ALA A 252 ? 0.4442 0.4925 0.2632 -0.0164 0.0713  0.1130  252 ALA A N   
1996 C CA  . ALA A 252 ? 0.5040 0.5432 0.3235 -0.0203 0.0773  0.1243  252 ALA A CA  
1997 C C   . ALA A 252 ? 0.5684 0.5929 0.3893 -0.0159 0.0724  0.1373  252 ALA A C   
1998 O O   . ALA A 252 ? 0.5742 0.5850 0.4047 -0.0180 0.0756  0.1425  252 ALA A O   
1999 C CB  . ALA A 252 ? 0.4773 0.5276 0.2798 -0.0255 0.0840  0.1302  252 ALA A CB  
2000 N N   . LYS A 253 ? 0.5958 0.6231 0.4083 -0.0098 0.0647  0.1423  253 LYS A N   
2001 C CA  A LYS A 253 ? 0.5591 0.5731 0.3736 -0.0043 0.0600  0.1551  253 LYS A CA  
2002 C CA  B LYS A 253 ? 0.5591 0.5729 0.3737 -0.0044 0.0601  0.1552  253 LYS A CA  
2003 C C   . LYS A 253 ? 0.5488 0.5480 0.3817 -0.0012 0.0575  0.1494  253 LYS A C   
2004 O O   . LYS A 253 ? 0.5271 0.5114 0.3653 0.0021  0.0563  0.1587  253 LYS A O   
2005 C CB  A LYS A 253 ? 0.5880 0.6119 0.3913 0.0020  0.0517  0.1603  253 LYS A CB  
2006 C CB  B LYS A 253 ? 0.5883 0.6116 0.3913 0.0019  0.0520  0.1612  253 LYS A CB  
2007 C CG  A LYS A 253 ? 0.6305 0.6424 0.4364 0.0090  0.0467  0.1744  253 LYS A CG  
2008 C CG  B LYS A 253 ? 0.5854 0.6178 0.3693 -0.0001 0.0534  0.1747  253 LYS A CG  
2009 C CD  A LYS A 253 ? 0.7280 0.7465 0.5363 0.0168  0.0372  0.1707  253 LYS A CD  
2010 C CD  B LYS A 253 ? 0.6415 0.6900 0.4131 0.0044  0.0450  0.1761  253 LYS A CD  
2011 C CE  A LYS A 253 ? 0.6893 0.7299 0.4833 0.0156  0.0335  0.1656  253 LYS A CE  
2012 C CE  B LYS A 253 ? 0.7049 0.7472 0.4870 0.0134  0.0361  0.1779  253 LYS A CE  
2013 N NZ  A LYS A 253 ? 0.6843 0.7324 0.4826 0.0219  0.0247  0.1599  253 LYS A NZ  
2014 N NZ  B LYS A 253 ? 0.6839 0.7086 0.4724 0.0181  0.0359  0.1937  253 LYS A NZ  
2015 N N   . ASN A 254 ? 0.4644 0.4671 0.3070 -0.0021 0.0569  0.1346  254 ASN A N   
2016 C CA  . ASN A 254 ? 0.4783 0.4691 0.3364 0.0004  0.0542  0.1287  254 ASN A CA  
2017 C C   . ASN A 254 ? 0.4728 0.4571 0.3428 -0.0059 0.0601  0.1228  254 ASN A C   
2018 O O   . ASN A 254 ? 0.4954 0.4721 0.3779 -0.0052 0.0581  0.1161  254 ASN A O   
2019 C CB  . ASN A 254 ? 0.4135 0.4127 0.2742 0.0047  0.0478  0.1178  254 ASN A CB  
2020 C CG  . ASN A 254 ? 0.5451 0.5532 0.3949 0.0103  0.0418  0.1230  254 ASN A CG  
2021 O OD1 . ASN A 254 ? 0.4664 0.4674 0.3164 0.0158  0.0380  0.1323  254 ASN A OD1 
2022 N ND2 . ASN A 254 ? 0.4975 0.5216 0.3381 0.0087  0.0410  0.1172  254 ASN A ND2 
2023 N N   . TRP A 255 ? 0.4831 0.4715 0.3498 -0.0124 0.0673  0.1251  255 TRP A N   
2024 C CA  . TRP A 255 ? 0.5504 0.5349 0.4296 -0.0189 0.0728  0.1200  255 TRP A CA  
2025 C C   . TRP A 255 ? 0.5304 0.4964 0.4186 -0.0198 0.0733  0.1258  255 TRP A C   
2026 O O   . TRP A 255 ? 0.5071 0.4631 0.3895 -0.0184 0.0740  0.1381  255 TRP A O   
2027 C CB  . TRP A 255 ? 0.4367 0.4304 0.3101 -0.0255 0.0811  0.1224  255 TRP A CB  
2028 C CG  . TRP A 255 ? 0.4562 0.4671 0.3250 -0.0255 0.0818  0.1127  255 TRP A CG  
2029 C CD1 . TRP A 255 ? 0.4528 0.4699 0.3243 -0.0211 0.0762  0.1024  255 TRP A CD1 
2030 C CD2 . TRP A 255 ? 0.4592 0.4829 0.3204 -0.0303 0.0893  0.1119  255 TRP A CD2 
2031 N NE1 . TRP A 255 ? 0.4093 0.4409 0.2759 -0.0227 0.0796  0.0949  255 TRP A NE1 
2032 C CE2 . TRP A 255 ? 0.4605 0.4968 0.3206 -0.0283 0.0878  0.1001  255 TRP A CE2 
2033 C CE3 . TRP A 255 ? 0.4632 0.4888 0.3183 -0.0364 0.0976  0.1199  255 TRP A CE3 
2034 C CZ2 . TRP A 255 ? 0.4751 0.5254 0.3287 -0.0319 0.0946  0.0950  255 TRP A CZ2 
2035 C CZ3 . TRP A 255 ? 0.5782 0.6190 0.4261 -0.0401 0.1044  0.1153  255 TRP A CZ3 
2036 C CH2 . TRP A 255 ? 0.5205 0.5733 0.3678 -0.0377 0.1029  0.1024  255 TRP A CH2 
2037 N N   . GLY A 256 ? 0.5510 0.5123 0.4534 -0.0223 0.0729  0.1170  256 GLY A N   
2038 C CA  . GLY A 256 ? 0.4995 0.4434 0.4111 -0.0239 0.0733  0.1195  256 GLY A CA  
2039 C C   . GLY A 256 ? 0.5238 0.4587 0.4381 -0.0169 0.0666  0.1172  256 GLY A C   
2040 O O   . GLY A 256 ? 0.5220 0.4434 0.4457 -0.0185 0.0667  0.1152  256 GLY A O   
2041 N N   . ARG A 257 ? 0.4737 0.4164 0.3807 -0.0097 0.0611  0.1164  257 ARG A N   
2042 C CA  . ARG A 257 ? 0.4726 0.4073 0.3819 -0.0025 0.0555  0.1158  257 ARG A CA  
2043 C C   . ARG A 257 ? 0.5067 0.4421 0.4258 -0.0024 0.0521  0.1030  257 ARG A C   
2044 O O   . ARG A 257 ? 0.4386 0.3674 0.3606 0.0030  0.0482  0.1013  257 ARG A O   
2045 C CB  . ARG A 257 ? 0.4636 0.4077 0.3622 0.0048  0.0507  0.1205  257 ARG A CB  
2046 C CG  . ARG A 257 ? 0.5307 0.4734 0.4185 0.0056  0.0529  0.1353  257 ARG A CG  
2047 C CD  . ARG A 257 ? 0.5292 0.4823 0.4068 0.0130  0.0469  0.1402  257 ARG A CD  
2048 N NE  . ARG A 257 ? 0.5288 0.4736 0.4129 0.0208  0.0419  0.1416  257 ARG A NE  
2049 C CZ  . ARG A 257 ? 0.5822 0.5367 0.4645 0.0272  0.0354  0.1389  257 ARG A CZ  
2050 N NH1 . ARG A 257 ? 0.5125 0.4850 0.3866 0.0265  0.0327  0.1340  257 ARG A NH1 
2051 N NH2 . ARG A 257 ? 0.5560 0.5024 0.4460 0.0343  0.0320  0.1404  257 ARG A NH2 
2052 N N   . THR A 258 ? 0.4455 0.3892 0.3702 -0.0079 0.0534  0.0943  258 THR A N   
2053 C CA  . THR A 258 ? 0.4523 0.3949 0.3862 -0.0084 0.0502  0.0839  258 THR A CA  
2054 C C   . THR A 258 ? 0.4724 0.3983 0.4134 -0.0106 0.0515  0.0840  258 THR A C   
2055 O O   . THR A 258 ? 0.5515 0.4741 0.4976 -0.0092 0.0483  0.0767  258 THR A O   
2056 C CB  . THR A 258 ? 0.3906 0.3446 0.3310 -0.0140 0.0512  0.0760  258 THR A CB  
2057 O OG1 . THR A 258 ? 0.4449 0.3970 0.3895 -0.0213 0.0571  0.0790  258 THR A OG1 
2058 C CG2 . THR A 258 ? 0.3617 0.3312 0.2969 -0.0114 0.0499  0.0734  258 THR A CG2 
2059 N N   . LYS A 259 ? 0.4723 0.3873 0.4136 -0.0142 0.0566  0.0920  259 LYS A N   
2060 C CA  . LYS A 259 ? 0.4956 0.3921 0.4433 -0.0156 0.0583  0.0926  259 LYS A CA  
2061 C C   . LYS A 259 ? 0.5241 0.4128 0.4702 -0.0065 0.0546  0.0937  259 LYS A C   
2062 O O   . LYS A 259 ? 0.5691 0.4467 0.5217 -0.0063 0.0543  0.0880  259 LYS A O   
2063 C CB  . LYS A 259 ? 0.4579 0.3431 0.4054 -0.0201 0.0646  0.1030  259 LYS A CB  
2064 C CG  . LYS A 259 ? 0.5559 0.4482 0.5071 -0.0298 0.0693  0.1017  259 LYS A CG  
2065 C CD  . LYS A 259 ? 0.5901 0.4680 0.5435 -0.0357 0.0760  0.1110  259 LYS A CD  
2066 C CE  . LYS A 259 ? 0.8317 0.7197 0.7790 -0.0397 0.0810  0.1190  259 LYS A CE  
2067 N NZ  . LYS A 259 ? 0.9266 0.8195 0.8602 -0.0321 0.0796  0.1288  259 LYS A NZ  
2068 N N   . GLU A 260 ? 0.4820 0.3774 0.4196 0.0008  0.0520  0.1006  260 GLU A N   
2069 C CA  . GLU A 260 ? 0.4304 0.3215 0.3676 0.0100  0.0481  0.1021  260 GLU A CA  
2070 C C   . GLU A 260 ? 0.4679 0.3696 0.4069 0.0126  0.0432  0.0908  260 GLU A C   
2071 O O   . GLU A 260 ? 0.5548 0.4495 0.4991 0.0162  0.0418  0.0858  260 GLU A O   
2072 C CB  . GLU A 260 ? 0.5182 0.4147 0.4461 0.0163  0.0465  0.1143  260 GLU A CB  
2073 C CG  . GLU A 260 ? 0.6241 0.5096 0.5492 0.0144  0.0513  0.1278  260 GLU A CG  
2074 C CD  . GLU A 260 ? 0.6560 0.5507 0.5697 0.0196  0.0491  0.1402  260 GLU A CD  
2075 O OE1 . GLU A 260 ? 0.6635 0.5659 0.5746 0.0274  0.0435  0.1408  260 GLU A OE1 
2076 O OE2 . GLU A 260 ? 0.7949 0.6900 0.7019 0.0153  0.0530  0.1493  260 GLU A OE2 
2077 N N   . THR A 261 ? 0.4567 0.3750 0.3916 0.0110  0.0409  0.0867  261 THR A N   
2078 C CA  . THR A 261 ? 0.4871 0.4154 0.4234 0.0135  0.0363  0.0775  261 THR A CA  
2079 C C   . THR A 261 ? 0.4361 0.3593 0.3804 0.0092  0.0366  0.0676  261 THR A C   
2080 O O   . THR A 261 ? 0.3851 0.3071 0.3320 0.0126  0.0341  0.0620  261 THR A O   
2081 C CB  . THR A 261 ? 0.4137 0.3589 0.3452 0.0119  0.0348  0.0750  261 THR A CB  
2082 O OG1 . THR A 261 ? 0.4415 0.3890 0.3767 0.0043  0.0380  0.0715  261 THR A OG1 
2083 C CG2 . THR A 261 ? 0.4375 0.3884 0.3595 0.0147  0.0350  0.0841  261 THR A CG2 
2084 N N   . LEU A 262 ? 0.4139 0.3354 0.3621 0.0013  0.0396  0.0653  262 LEU A N   
2085 C CA  . LEU A 262 ? 0.4451 0.3641 0.4001 -0.0036 0.0390  0.0559  262 LEU A CA  
2086 C C   . LEU A 262 ? 0.4482 0.3503 0.4069 -0.0027 0.0408  0.0544  262 LEU A C   
2087 O O   . LEU A 262 ? 0.4816 0.3823 0.4434 -0.0038 0.0393  0.0457  262 LEU A O   
2088 C CB  . LEU A 262 ? 0.3907 0.3134 0.3503 -0.0125 0.0415  0.0541  262 LEU A CB  
2089 C CG  . LEU A 262 ? 0.4363 0.3758 0.3944 -0.0132 0.0403  0.0539  262 LEU A CG  
2090 C CD1 . LEU A 262 ? 0.4022 0.3463 0.3669 -0.0214 0.0433  0.0527  262 LEU A CD1 
2091 C CD2 . LEU A 262 ? 0.3332 0.2829 0.2916 -0.0102 0.0353  0.0471  262 LEU A CD2 
2092 N N   . ALA A 263 ? 0.4560 0.3450 0.4141 -0.0005 0.0443  0.0630  263 ALA A N   
2093 C CA  . ALA A 263 ? 0.4194 0.2913 0.3819 0.0023  0.0464  0.0622  263 ALA A CA  
2094 C C   . ALA A 263 ? 0.4634 0.3384 0.4250 0.0111  0.0430  0.0593  263 ALA A C   
2095 O O   . ALA A 263 ? 0.4745 0.3415 0.4405 0.0120  0.0438  0.0519  263 ALA A O   
2096 C CB  . ALA A 263 ? 0.4587 0.3164 0.4212 0.0040  0.0507  0.0741  263 ALA A CB  
2097 N N   . PHE A 264 ? 0.4487 0.3360 0.4047 0.0173  0.0395  0.0646  264 PHE A N   
2098 C CA  . PHE A 264 ? 0.4393 0.3325 0.3953 0.0250  0.0360  0.0617  264 PHE A CA  
2099 C C   . PHE A 264 ? 0.4217 0.3233 0.3790 0.0217  0.0338  0.0497  264 PHE A C   
2100 O O   . PHE A 264 ? 0.4505 0.3498 0.4107 0.0252  0.0334  0.0438  264 PHE A O   
2101 C CB  . PHE A 264 ? 0.4669 0.3736 0.4165 0.0305  0.0324  0.0691  264 PHE A CB  
2102 C CG  . PHE A 264 ? 0.4927 0.4041 0.4438 0.0394  0.0293  0.0693  264 PHE A CG  
2103 C CD1 . PHE A 264 ? 0.4432 0.3424 0.4012 0.0444  0.0312  0.0680  264 PHE A CD1 
2104 C CD2 . PHE A 264 ? 0.4774 0.4055 0.4238 0.0426  0.0247  0.0701  264 PHE A CD2 
2105 C CE1 . PHE A 264 ? 0.5096 0.4145 0.4705 0.0528  0.0287  0.0680  264 PHE A CE1 
2106 C CE2 . PHE A 264 ? 0.4438 0.3777 0.3928 0.0502  0.0218  0.0701  264 PHE A CE2 
2107 C CZ  . PHE A 264 ? 0.4544 0.3772 0.4109 0.0556  0.0238  0.0693  264 PHE A CZ  
2108 N N   . PHE A 265 ? 0.3906 0.3023 0.3461 0.0150  0.0325  0.0463  265 PHE A N   
2109 C CA  . PHE A 265 ? 0.4412 0.3610 0.3979 0.0114  0.0301  0.0363  265 PHE A CA  
2110 C C   . PHE A 265 ? 0.4659 0.3744 0.4268 0.0075  0.0324  0.0287  265 PHE A C   
2111 O O   . PHE A 265 ? 0.4929 0.4034 0.4541 0.0087  0.0313  0.0214  265 PHE A O   
2112 C CB  . PHE A 265 ? 0.3976 0.3284 0.3539 0.0050  0.0288  0.0352  265 PHE A CB  
2113 C CG  . PHE A 265 ? 0.4021 0.3471 0.3545 0.0081  0.0259  0.0377  265 PHE A CG  
2114 C CD1 . PHE A 265 ? 0.4632 0.4105 0.4116 0.0106  0.0268  0.0454  265 PHE A CD1 
2115 C CD2 . PHE A 265 ? 0.4474 0.4036 0.4002 0.0076  0.0225  0.0321  265 PHE A CD2 
2116 C CE1 . PHE A 265 ? 0.4655 0.4259 0.4104 0.0125  0.0245  0.0460  265 PHE A CE1 
2117 C CE2 . PHE A 265 ? 0.4463 0.4141 0.3967 0.0098  0.0204  0.0336  265 PHE A CE2 
2118 C CZ  . PHE A 265 ? 0.4030 0.3728 0.3494 0.0121  0.0215  0.0398  265 PHE A CZ  
2119 N N   . ASP A 266 ? 0.4629 0.3602 0.4269 0.0018  0.0360  0.0297  266 ASP A N   
2120 C CA  . ASP A 266 ? 0.5007 0.3859 0.4688 -0.0032 0.0388  0.0217  266 ASP A CA  
2121 C C   . ASP A 266 ? 0.4988 0.3745 0.4684 0.0039  0.0406  0.0187  266 ASP A C   
2122 O O   . ASP A 266 ? 0.5693 0.4446 0.5394 0.0021  0.0407  0.0086  266 ASP A O   
2123 C CB  . ASP A 266 ? 0.4537 0.3253 0.4257 -0.0090 0.0434  0.0254  266 ASP A CB  
2124 C CG  . ASP A 266 ? 0.5924 0.4730 0.5659 -0.0186 0.0425  0.0239  266 ASP A CG  
2125 O OD1 . ASP A 266 ? 0.5472 0.4427 0.5196 -0.0212 0.0384  0.0185  266 ASP A OD1 
2126 O OD2 . ASP A 266 ? 0.5863 0.4592 0.5629 -0.0234 0.0462  0.0287  266 ASP A OD2 
2127 N N   . GLU A 267 ? 0.5134 0.3820 0.4838 0.0120  0.0421  0.0276  267 GLU A N   
2128 C CA  . GLU A 267 ? 0.5743 0.4338 0.5484 0.0199  0.0441  0.0260  267 GLU A CA  
2129 C C   . GLU A 267 ? 0.5335 0.4069 0.5055 0.0239  0.0408  0.0196  267 GLU A C   
2130 O O   . GLU A 267 ? 0.5387 0.4076 0.5134 0.0250  0.0430  0.0109  267 GLU A O   
2131 C CB  . GLU A 267 ? 0.4926 0.3459 0.4682 0.0284  0.0450  0.0391  267 GLU A CB  
2132 C CG  . GLU A 267 ? 0.7885 0.6301 0.7709 0.0374  0.0478  0.0393  267 GLU A CG  
2133 C CD  . GLU A 267 ? 0.8626 0.7053 0.8457 0.0474  0.0462  0.0531  267 GLU A CD  
2134 O OE1 . GLU A 267 ? 0.8627 0.7089 0.8409 0.0460  0.0447  0.0634  267 GLU A OE1 
2135 O OE2 . GLU A 267 ? 1.0402 0.8817 1.0288 0.0566  0.0465  0.0537  267 GLU A OE2 
2136 N N   . MET A 268 ? 0.4794 0.3695 0.4467 0.0257  0.0361  0.0235  268 MET A N   
2137 C CA  . MET A 268 ? 0.4464 0.3492 0.4125 0.0301  0.0333  0.0194  268 MET A CA  
2138 C C   . MET A 268 ? 0.4837 0.3949 0.4471 0.0232  0.0318  0.0093  268 MET A C   
2139 O O   . MET A 268 ? 0.4649 0.3817 0.4281 0.0254  0.0315  0.0033  268 MET A O   
2140 C CB  . MET A 268 ? 0.4525 0.3692 0.4151 0.0345  0.0291  0.0273  268 MET A CB  
2141 C CG  . MET A 268 ? 0.5619 0.4736 0.5263 0.0424  0.0295  0.0380  268 MET A CG  
2142 S SD  . MET A 268 ? 0.5685 0.4672 0.5416 0.0510  0.0333  0.0370  268 MET A SD  
2143 C CE  . MET A 268 ? 0.5366 0.4518 0.5104 0.0549  0.0305  0.0298  268 MET A CE  
2144 N N   . ARG A 269 ? 0.5127 0.4257 0.4742 0.0147  0.0309  0.0078  269 ARG A N   
2145 C CA  . ARG A 269 ? 0.4243 0.3455 0.3834 0.0082  0.0290  -0.0009 269 ARG A CA  
2146 C C   . ARG A 269 ? 0.5423 0.4545 0.5024 0.0057  0.0324  -0.0109 269 ARG A C   
2147 O O   . ARG A 269 ? 0.5008 0.4209 0.4575 0.0008  0.0308  -0.0185 269 ARG A O   
2148 C CB  . ARG A 269 ? 0.3935 0.3194 0.3522 0.0000  0.0270  0.0001  269 ARG A CB  
2149 C CG  . ARG A 269 ? 0.5210 0.4585 0.4785 0.0018  0.0239  0.0075  269 ARG A CG  
2150 C CD  . ARG A 269 ? 0.4922 0.4343 0.4515 -0.0055 0.0229  0.0086  269 ARG A CD  
2151 N NE  . ARG A 269 ? 0.5187 0.4669 0.4783 -0.0124 0.0206  0.0014  269 ARG A NE  
2152 C CZ  . ARG A 269 ? 0.5225 0.4677 0.4851 -0.0202 0.0213  -0.0020 269 ARG A CZ  
2153 N NH1 . ARG A 269 ? 0.5366 0.4723 0.5026 -0.0226 0.0247  0.0013  269 ARG A NH1 
2154 N NH2 . ARG A 269 ? 0.5459 0.4987 0.5078 -0.0262 0.0184  -0.0085 269 ARG A NH2 
2155 N N   . GLN A 270 ? 0.4714 0.3672 0.4358 0.0088  0.0372  -0.0112 270 GLN A N   
2156 C CA  . GLN A 270 ? 0.5595 0.4461 0.5253 0.0071  0.0414  -0.0221 270 GLN A CA  
2157 C C   . GLN A 270 ? 0.5638 0.4573 0.5289 0.0136  0.0420  -0.0265 270 GLN A C   
2158 O O   . GLN A 270 ? 0.5825 0.4737 0.5465 0.0108  0.0449  -0.0373 270 GLN A O   
2159 C CB  . GLN A 270 ? 0.5582 0.4236 0.5306 0.0089  0.0472  -0.0210 270 GLN A CB  
2160 C CG  . GLN A 270 ? 0.6234 0.4806 0.5968 -0.0009 0.0481  -0.0218 270 GLN A CG  
2161 C CD  . GLN A 270 ? 0.8995 0.7360 0.8796 0.0013  0.0534  -0.0165 270 GLN A CD  
2162 O OE1 . GLN A 270 ? 0.9301 0.7610 0.9138 0.0112  0.0548  -0.0082 270 GLN A OE1 
2163 N NE2 . GLN A 270 ? 1.1155 0.9410 1.0981 -0.0080 0.0562  -0.0209 270 GLN A NE2 
2164 N N   . GLN A 271 ? 0.4933 0.3961 0.4589 0.0214  0.0394  -0.0189 271 GLN A N   
2165 C CA  A GLN A 271 ? 0.4939 0.4047 0.4601 0.0272  0.0401  -0.0226 271 GLN A CA  
2166 C CA  B GLN A 271 ? 0.4940 0.4048 0.4603 0.0274  0.0401  -0.0224 271 GLN A CA  
2167 C C   . GLN A 271 ? 0.4664 0.3963 0.4278 0.0267  0.0350  -0.0203 271 GLN A C   
2168 O O   . GLN A 271 ? 0.5071 0.4453 0.4683 0.0298  0.0356  -0.0241 271 GLN A O   
2169 C CB  A GLN A 271 ? 0.4843 0.3885 0.4583 0.0384  0.0427  -0.0169 271 GLN A CB  
2170 C CB  B GLN A 271 ? 0.4843 0.3886 0.4583 0.0385  0.0424  -0.0161 271 GLN A CB  
2171 C CG  A GLN A 271 ? 0.5048 0.4133 0.4798 0.0436  0.0388  -0.0038 271 GLN A CG  
2172 C CG  B GLN A 271 ? 0.5230 0.4075 0.5039 0.0409  0.0490  -0.0200 271 GLN A CG  
2173 C CD  A GLN A 271 ? 0.5967 0.5033 0.5794 0.0550  0.0401  0.0019  271 GLN A CD  
2174 C CD  B GLN A 271 ? 0.6426 0.5184 0.6317 0.0512  0.0502  -0.0094 271 GLN A CD  
2175 O OE1 A GLN A 271 ? 0.5953 0.4933 0.5817 0.0596  0.0404  0.0111  271 GLN A OE1 
2176 O OE1 B GLN A 271 ? 0.5884 0.4646 0.5764 0.0522  0.0469  0.0017  271 GLN A OE1 
2177 N NE2 A GLN A 271 ? 0.5545 0.4703 0.5402 0.0595  0.0409  -0.0029 271 GLN A NE2 
2178 N NE2 B GLN A 271 ? 0.7199 0.5885 0.7176 0.0590  0.0550  -0.0127 271 GLN A NE2 
2179 N N   . GLN A 272 ? 0.4568 0.3936 0.4149 0.0228  0.0305  -0.0145 272 GLN A N   
2180 C CA  . GLN A 272 ? 0.4158 0.3689 0.3704 0.0223  0.0261  -0.0122 272 GLN A CA  
2181 C C   . GLN A 272 ? 0.4266 0.3849 0.3781 0.0152  0.0225  -0.0099 272 GLN A C   
2182 O O   . GLN A 272 ? 0.4706 0.4211 0.4230 0.0114  0.0231  -0.0085 272 GLN A O   
2183 C CB  . GLN A 272 ? 0.4012 0.3599 0.3586 0.0302  0.0245  -0.0047 272 GLN A CB  
2184 C CG  . GLN A 272 ? 0.4482 0.4029 0.4063 0.0315  0.0231  0.0040  272 GLN A CG  
2185 C CD  . GLN A 272 ? 0.4180 0.3784 0.3781 0.0393  0.0214  0.0111  272 GLN A CD  
2186 O OE1 . GLN A 272 ? 0.4448 0.3978 0.4090 0.0454  0.0232  0.0150  272 GLN A OE1 
2187 N NE2 . GLN A 272 ? 0.3594 0.3334 0.3173 0.0389  0.0178  0.0128  272 GLN A NE2 
2188 N N   . ASP A 273 ? 0.3700 0.3416 0.3188 0.0134  0.0189  -0.0092 273 ASP A N   
2189 C CA  A ASP A 273 ? 0.4042 0.3823 0.3515 0.0075  0.0154  -0.0071 273 ASP A CA  
2190 C CA  B ASP A 273 ? 0.4049 0.3831 0.3522 0.0075  0.0154  -0.0071 273 ASP A CA  
2191 C C   . ASP A 273 ? 0.4181 0.3987 0.3675 0.0103  0.0138  0.0007  273 ASP A C   
2192 O O   . ASP A 273 ? 0.3830 0.3705 0.3325 0.0145  0.0125  0.0036  273 ASP A O   
2193 C CB  A ASP A 273 ? 0.4079 0.3982 0.3520 0.0044  0.0127  -0.0094 273 ASP A CB  
2194 C CB  B ASP A 273 ? 0.4084 0.3987 0.3526 0.0046  0.0128  -0.0094 273 ASP A CB  
2195 C CG  A ASP A 273 ? 0.4621 0.4521 0.4023 -0.0003 0.0139  -0.0173 273 ASP A CG  
2196 C CG  B ASP A 273 ? 0.4258 0.4223 0.3696 -0.0018 0.0092  -0.0079 273 ASP A CG  
2197 O OD1 A ASP A 273 ? 0.4253 0.4060 0.3655 -0.0034 0.0162  -0.0219 273 ASP A OD1 
2198 O OD1 B ASP A 273 ? 0.4303 0.4222 0.3767 -0.0046 0.0092  -0.0065 273 ASP A OD1 
2199 O OD2 A ASP A 273 ? 0.5247 0.5239 0.4612 -0.0014 0.0129  -0.0193 273 ASP A OD2 
2200 O OD2 B ASP A 273 ? 0.5135 0.5200 0.4553 -0.0040 0.0065  -0.0077 273 ASP A OD2 
2201 N N   . ILE A 274 ? 0.3669 0.3424 0.3178 0.0074  0.0143  0.0035  274 ILE A N   
2202 C CA  . ILE A 274 ? 0.3935 0.3711 0.3454 0.0093  0.0137  0.0102  274 ILE A CA  
2203 C C   . ILE A 274 ? 0.3450 0.3255 0.2990 0.0032  0.0127  0.0111  274 ILE A C   
2204 O O   . ILE A 274 ? 0.4086 0.3844 0.3640 -0.0020 0.0136  0.0082  274 ILE A O   
2205 C CB  . ILE A 274 ? 0.3960 0.3636 0.3483 0.0135  0.0164  0.0148  274 ILE A CB  
2206 C CG1 . ILE A 274 ? 0.4428 0.4074 0.3952 0.0202  0.0174  0.0143  274 ILE A CG1 
2207 C CG2 . ILE A 274 ? 0.4256 0.3980 0.3768 0.0153  0.0157  0.0213  274 ILE A CG2 
2208 C CD1 . ILE A 274 ? 0.4201 0.3731 0.3741 0.0244  0.0202  0.0193  274 ILE A CD1 
2209 N N   . ALA A 275 ? 0.3203 0.3088 0.2753 0.0037  0.0113  0.0145  275 ALA A N   
2210 C CA  . ALA A 275 ? 0.3583 0.3501 0.3170 -0.0007 0.0112  0.0163  275 ALA A CA  
2211 C C   . ALA A 275 ? 0.3309 0.3257 0.2893 0.0024  0.0124  0.0208  275 ALA A C   
2212 O O   . ALA A 275 ? 0.3836 0.3772 0.3383 0.0072  0.0128  0.0227  275 ALA A O   
2213 C CB  . ALA A 275 ? 0.3357 0.3369 0.2974 -0.0044 0.0079  0.0140  275 ALA A CB  
2214 N N   . CYS A 276 ? 0.3848 0.3845 0.3473 -0.0006 0.0130  0.0222  276 CYS A N   
2215 C CA  . CYS A 276 ? 0.3440 0.3477 0.3060 0.0015  0.0147  0.0251  276 CYS A CA  
2216 C C   . CYS A 276 ? 0.3207 0.3318 0.2898 -0.0015 0.0150  0.0248  276 CYS A C   
2217 O O   . CYS A 276 ? 0.3187 0.3321 0.2933 -0.0054 0.0136  0.0236  276 CYS A O   
2218 C CB  . CYS A 276 ? 0.4281 0.4250 0.3861 0.0022  0.0182  0.0292  276 CYS A CB  
2219 S SG  . CYS A 276 ? 0.5034 0.4957 0.4664 -0.0041 0.0213  0.0305  276 CYS A SG  
2220 N N   . ASP A 277 ? 0.3332 0.3491 0.3026 0.0002  0.0169  0.0257  277 ASP A N   
2221 C CA  . ASP A 277 ? 0.3932 0.4157 0.3707 -0.0020 0.0187  0.0256  277 ASP A CA  
2222 C C   . ASP A 277 ? 0.4193 0.4420 0.3942 -0.0021 0.0236  0.0274  277 ASP A C   
2223 O O   . ASP A 277 ? 0.4115 0.4304 0.3777 -0.0001 0.0248  0.0292  277 ASP A O   
2224 C CB  . ASP A 277 ? 0.3146 0.3437 0.2973 -0.0002 0.0168  0.0237  277 ASP A CB  
2225 C CG  . ASP A 277 ? 0.4096 0.4390 0.3866 0.0034  0.0173  0.0223  277 ASP A CG  
2226 O OD1 . ASP A 277 ? 0.4549 0.4862 0.4303 0.0040  0.0209  0.0218  277 ASP A OD1 
2227 O OD2 . ASP A 277 ? 0.4759 0.5046 0.4500 0.0051  0.0142  0.0214  277 ASP A OD2 
2228 N N   . CYS A 278 ? 0.3134 0.3417 0.2963 -0.0044 0.0266  0.0272  278 CYS A N   
2229 C CA  . CYS A 278 ? 0.3980 0.4279 0.3785 -0.0051 0.0322  0.0285  278 CYS A CA  
2230 C C   . CYS A 278 ? 0.3894 0.4280 0.3809 -0.0057 0.0352  0.0262  278 CYS A C   
2231 O O   . CYS A 278 ? 0.3132 0.3560 0.3156 -0.0066 0.0328  0.0255  278 CYS A O   
2232 C CB  . CYS A 278 ? 0.4515 0.4759 0.4296 -0.0087 0.0349  0.0324  278 CYS A CB  
2233 S SG  . CYS A 278 ? 0.5649 0.5939 0.5569 -0.0143 0.0362  0.0322  278 CYS A SG  
2234 N N   . TYR A 279 ? 0.3412 0.3831 0.3298 -0.0053 0.0405  0.0252  279 TYR A N   
2235 C CA  . TYR A 279 ? 0.2897 0.3397 0.2906 -0.0060 0.0447  0.0230  279 TYR A CA  
2236 C C   . TYR A 279 ? 0.3105 0.3625 0.3136 -0.0102 0.0499  0.0257  279 TYR A C   
2237 O O   . TYR A 279 ? 0.3942 0.4416 0.3862 -0.0118 0.0523  0.0287  279 TYR A O   
2238 C CB  . TYR A 279 ? 0.2892 0.3430 0.2889 -0.0034 0.0485  0.0183  279 TYR A CB  
2239 C CG  . TYR A 279 ? 0.3597 0.4127 0.3449 -0.0037 0.0524  0.0179  279 TYR A CG  
2240 C CD1 . TYR A 279 ? 0.3572 0.4143 0.3405 -0.0063 0.0595  0.0183  279 TYR A CD1 
2241 C CD2 . TYR A 279 ? 0.3759 0.4256 0.3494 -0.0016 0.0489  0.0171  279 TYR A CD2 
2242 C CE1 . TYR A 279 ? 0.3227 0.3805 0.2911 -0.0070 0.0627  0.0184  279 TYR A CE1 
2243 C CE2 . TYR A 279 ? 0.2791 0.3301 0.2388 -0.0020 0.0516  0.0170  279 TYR A CE2 
2244 C CZ  . TYR A 279 ? 0.4589 0.5139 0.4154 -0.0048 0.0584  0.0179  279 TYR A CZ  
2245 O OH  . TYR A 279 ? 0.3448 0.4024 0.2862 -0.0056 0.0607  0.0184  279 TYR A OH  
2246 N N   . PRO A 280 ? 0.3291 0.3883 0.3470 -0.0120 0.0516  0.0251  280 PRO A N   
2247 C CA  . PRO A 280 ? 0.3576 0.4197 0.3807 -0.0171 0.0558  0.0278  280 PRO A CA  
2248 C C   . PRO A 280 ? 0.3312 0.3987 0.3532 -0.0182 0.0648  0.0270  280 PRO A C   
2249 O O   . PRO A 280 ? 0.3018 0.3783 0.3368 -0.0203 0.0695  0.0263  280 PRO A O   
2250 C CB  . PRO A 280 ? 0.2880 0.3581 0.3289 -0.0181 0.0527  0.0273  280 PRO A CB  
2251 C CG  . PRO A 280 ? 0.2609 0.3354 0.3083 -0.0126 0.0519  0.0239  280 PRO A CG  
2252 C CD  . PRO A 280 ? 0.2543 0.3202 0.2866 -0.0093 0.0494  0.0226  280 PRO A CD  
2253 N N   . TYR A 281 ? 0.3718 0.4353 0.3782 -0.0170 0.0673  0.0271  281 TYR A N   
2254 C CA  . TYR A 281 ? 0.3039 0.3724 0.3051 -0.0188 0.0759  0.0266  281 TYR A CA  
2255 C C   . TYR A 281 ? 0.3761 0.4375 0.3581 -0.0200 0.0762  0.0316  281 TYR A C   
2256 O O   . TYR A 281 ? 0.3010 0.3549 0.2738 -0.0174 0.0701  0.0333  281 TYR A O   
2257 C CB  . TYR A 281 ? 0.2908 0.3656 0.2935 -0.0153 0.0796  0.0196  281 TYR A CB  
2258 C CG  . TYR A 281 ? 0.3147 0.3957 0.3368 -0.0126 0.0794  0.0151  281 TYR A CG  
2259 C CD1 . TYR A 281 ? 0.2816 0.3592 0.3096 -0.0093 0.0716  0.0146  281 TYR A CD1 
2260 C CD2 . TYR A 281 ? 0.3061 0.3969 0.3410 -0.0131 0.0873  0.0117  281 TYR A CD2 
2261 C CE1 . TYR A 281 ? 0.2650 0.3483 0.3110 -0.0064 0.0711  0.0121  281 TYR A CE1 
2262 C CE2 . TYR A 281 ? 0.3006 0.3972 0.3549 -0.0097 0.0870  0.0085  281 TYR A CE2 
2263 C CZ  . TYR A 281 ? 0.3191 0.4116 0.3787 -0.0063 0.0786  0.0092  281 TYR A CZ  
2264 O OH  . TYR A 281 ? 0.2850 0.3834 0.3642 -0.0025 0.0781  0.0076  281 TYR A OH  
2265 N N   . SER A 282 ? 0.3138 0.3784 0.2902 -0.0237 0.0836  0.0345  282 SER A N   
2266 C CA  . SER A 282 ? 0.3348 0.3937 0.2931 -0.0249 0.0844  0.0410  282 SER A CA  
2267 C C   . SER A 282 ? 0.4189 0.4845 0.3638 -0.0241 0.0890  0.0382  282 SER A C   
2268 O O   . SER A 282 ? 0.4458 0.5103 0.3756 -0.0259 0.0913  0.0442  282 SER A O   
2269 C CB  . SER A 282 ? 0.3363 0.3927 0.2958 -0.0307 0.0892  0.0482  282 SER A CB  
2270 O OG  . SER A 282 ? 0.4410 0.5081 0.4098 -0.0342 0.0975  0.0455  282 SER A OG  
2271 N N   . ALA A 283 ? 0.3451 0.4177 0.2952 -0.0216 0.0906  0.0292  283 ALA A N   
2272 C CA  . ALA A 283 ? 0.3715 0.4502 0.3089 -0.0210 0.0941  0.0242  283 ALA A CA  
2273 C C   . ALA A 283 ? 0.4311 0.5077 0.3691 -0.0164 0.0876  0.0179  283 ALA A C   
2274 O O   . ALA A 283 ? 0.4282 0.5028 0.3811 -0.0139 0.0842  0.0148  283 ALA A O   
2275 C CB  . ALA A 283 ? 0.3425 0.4317 0.2861 -0.0233 0.1044  0.0177  283 ALA A CB  
2276 N N   . SER A 284 ? 0.3688 0.4569 0.3857 -0.0555 -0.0098 0.0122  284 SER A N   
2277 C CA  . SER A 284 ? 0.2842 0.3758 0.3012 -0.0574 -0.0120 0.0119  284 SER A CA  
2278 C C   . SER A 284 ? 0.3971 0.4817 0.4064 -0.0603 -0.0114 0.0103  284 SER A C   
2279 O O   . SER A 284 ? 0.3357 0.4177 0.3434 -0.0581 -0.0100 0.0095  284 SER A O   
2280 C CB  . SER A 284 ? 0.3346 0.4386 0.3513 -0.0562 -0.0144 0.0126  284 SER A CB  
2281 O OG  . SER A 284 ? 0.4019 0.5062 0.4129 -0.0526 -0.0148 0.0134  284 SER A OG  
2282 N N   . SER A 285 ? 0.3703 0.4506 0.3708 -0.0668 -0.0118 0.0091  285 SER A N   
2283 C CA  . SER A 285 ? 0.4406 0.5041 0.4249 -0.0703 -0.0105 0.0073  285 SER A CA  
2284 C C   . SER A 285 ? 0.5507 0.6143 0.5225 -0.0849 -0.0100 0.0053  285 SER A C   
2285 O O   . SER A 285 ? 0.4505 0.5173 0.4195 -0.0922 -0.0099 0.0044  285 SER A O   
2286 C CB  . SER A 285 ? 0.3973 0.4402 0.3688 -0.0624 -0.0096 0.0064  285 SER A CB  
2287 O OG  . SER A 285 ? 0.5421 0.5581 0.4868 -0.0642 -0.0083 0.0046  285 SER A OG  
2288 N N   . SER A 286 ? 0.3932 0.4565 0.3566 -0.0915 -0.0093 0.0035  286 SER A N   
2289 C CA  . SER A 286 ? 0.3762 0.4495 0.3279 -0.1096 -0.0081 -0.0003 286 SER A CA  
2290 C C   . SER A 286 ? 0.4350 0.4964 0.3714 -0.1163 -0.0063 -0.0023 286 SER A C   
2291 O O   . SER A 286 ? 0.5079 0.5534 0.4436 -0.1047 -0.0064 -0.0005 286 SER A O   
2292 C CB  . SER A 286 ? 0.4339 0.5509 0.4052 -0.1089 -0.0108 -0.0013 286 SER A CB  
2293 O OG  . SER A 286 ? 0.6428 0.7808 0.6038 -0.1285 -0.0093 -0.0070 286 SER A OG  
2294 N N   . THR A 287 ? 0.4399 0.5126 0.3626 -0.1365 -0.0042 -0.0072 287 THR A N   
2295 C CA  . THR A 287 ? 0.4988 0.5687 0.4099 -0.1442 -0.0027 -0.0098 287 THR A CA  
2296 C C   . THR A 287 ? 0.3987 0.4985 0.3361 -0.1285 -0.0063 -0.0075 287 THR A C   
2297 O O   . THR A 287 ? 0.4292 0.5580 0.3877 -0.1172 -0.0096 -0.0057 287 THR A O   
2298 C CB  . THR A 287 ? 0.4960 0.5842 0.3893 -0.1726 0.0006  -0.0172 287 THR A CB  
2299 O OG1 . THR A 287 ? 0.5481 0.6948 0.4659 -0.1723 -0.0023 -0.0199 287 THR A OG1 
2300 C CG2 . THR A 287 ? 0.4612 0.5095 0.3168 -0.1936 0.0058  -0.0200 287 THR A CG2 
2301 N N   . LEU A 288 ? 0.4246 0.5118 0.3552 -0.1270 -0.0055 -0.0075 288 LEU A N   
2302 C CA  . LEU A 288 ? 0.3186 0.4302 0.2666 -0.1157 -0.0081 -0.0059 288 LEU A CA  
2303 C C   . LEU A 288 ? 0.3886 0.5420 0.3385 -0.1261 -0.0089 -0.0109 288 LEU A C   
2304 O O   . LEU A 288 ? 0.3751 0.5304 0.3077 -0.1464 -0.0058 -0.0166 288 LEU A O   
2305 C CB  . LEU A 288 ? 0.4030 0.4910 0.3428 -0.1118 -0.0069 -0.0050 288 LEU A CB  
2306 C CG  . LEU A 288 ? 0.3983 0.5039 0.3520 -0.1006 -0.0089 -0.0028 288 LEU A CG  
2307 C CD1 . LEU A 288 ? 0.3012 0.4095 0.2697 -0.0852 -0.0108 0.0019  288 LEU A CD1 
2308 C CD2 . LEU A 288 ? 0.2786 0.3636 0.2228 -0.0995 -0.0073 -0.0032 288 LEU A CD2 
2309 N N   . ASP A 289 ? 0.3697 0.5570 0.3359 -0.1121 -0.0127 -0.0099 289 ASP A N   
2310 C CA  A ASP A 289 ? 0.4264 0.6651 0.3951 -0.1151 -0.0147 -0.0159 289 ASP A CA  
2311 C CA  B ASP A 289 ? 0.4265 0.6655 0.3955 -0.1148 -0.0147 -0.0158 289 ASP A CA  
2312 C C   . ASP A 289 ? 0.3758 0.6299 0.3508 -0.0922 -0.0186 -0.0130 289 ASP A C   
2313 O O   . ASP A 289 ? 0.3585 0.5921 0.3369 -0.0727 -0.0205 -0.0066 289 ASP A O   
2314 C CB  A ASP A 289 ? 0.4449 0.7170 0.4191 -0.1164 -0.0162 -0.0194 289 ASP A CB  
2315 C CB  B ASP A 289 ? 0.4460 0.7155 0.4210 -0.1146 -0.0164 -0.0187 289 ASP A CB  
2316 C CG  A ASP A 289 ? 0.4265 0.7641 0.4012 -0.1227 -0.0177 -0.0288 289 ASP A CG  
2317 C CG  B ASP A 289 ? 0.3804 0.6285 0.3447 -0.1372 -0.0122 -0.0208 289 ASP A CG  
2318 O OD1 A ASP A 289 ? 0.4329 0.7982 0.4111 -0.1048 -0.0213 -0.0294 289 ASP A OD1 
2319 O OD1 B ASP A 289 ? 0.4661 0.7071 0.4113 -0.1629 -0.0076 -0.0262 289 ASP A OD1 
2320 O OD2 A ASP A 289 ? 0.4951 0.8588 0.4638 -0.1460 -0.0150 -0.0364 289 ASP A OD2 
2321 O OD2 B ASP A 289 ? 0.5027 0.7366 0.4728 -0.1298 -0.0130 -0.0171 289 ASP A OD2 
2322 N N   . MET A 290 ? 0.3132 0.6013 0.2849 -0.0961 -0.0192 -0.0184 290 MET A N   
2323 C CA  . MET A 290 ? 0.3655 0.6638 0.3367 -0.0738 -0.0227 -0.0159 290 MET A CA  
2324 C C   . MET A 290 ? 0.4214 0.7301 0.3920 -0.0457 -0.0274 -0.0128 290 MET A C   
2325 O O   . MET A 290 ? 0.4103 0.6924 0.3718 -0.0252 -0.0289 -0.0067 290 MET A O   
2326 C CB  . MET A 290 ? 0.3367 0.6829 0.3047 -0.0820 -0.0231 -0.0240 290 MET A CB  
2327 C CG  . MET A 290 ? 0.3208 0.6635 0.2840 -0.0637 -0.0254 -0.0208 290 MET A CG  
2328 S SD  . MET A 290 ? 0.3598 0.6355 0.3203 -0.0710 -0.0213 -0.0131 290 MET A SD  
2329 C CE  . MET A 290 ? 0.3182 0.6035 0.2733 -0.1034 -0.0168 -0.0211 290 MET A CE  
2330 N N   . LYS A 291 ? 0.3772 0.7204 0.3522 -0.0450 -0.0292 -0.0174 291 LYS A N   
2331 C CA  A LYS A 291 ? 0.3984 0.7524 0.3680 -0.0154 -0.0339 -0.0156 291 LYS A CA  
2332 C CA  B LYS A 291 ? 0.3985 0.7522 0.3678 -0.0151 -0.0340 -0.0155 291 LYS A CA  
2333 C C   . LYS A 291 ? 0.4285 0.7238 0.3937 -0.0064 -0.0328 -0.0064 291 LYS A C   
2334 O O   . LYS A 291 ? 0.4227 0.7052 0.3728 0.0197  -0.0358 -0.0029 291 LYS A O   
2335 C CB  A LYS A 291 ? 0.3880 0.7983 0.3646 -0.0188 -0.0358 -0.0239 291 LYS A CB  
2336 C CB  B LYS A 291 ? 0.3874 0.7999 0.3634 -0.0176 -0.0361 -0.0242 291 LYS A CB  
2337 C CG  A LYS A 291 ? 0.4197 0.8062 0.4046 -0.0342 -0.0331 -0.0218 291 LYS A CG  
2338 C CG  B LYS A 291 ? 0.4294 0.9114 0.4086 -0.0335 -0.0360 -0.0361 291 LYS A CG  
2339 C CD  A LYS A 291 ? 0.4305 0.8743 0.4206 -0.0359 -0.0351 -0.0302 291 LYS A CD  
2340 C CD  B LYS A 291 ? 0.4735 0.9881 0.4462 -0.0032 -0.0378 -0.0387 291 LYS A CD  
2341 C CE  A LYS A 291 ? 0.3741 0.8478 0.3675 -0.0734 -0.0291 -0.0391 291 LYS A CE  
2342 C CE  B LYS A 291 ? 0.4958 1.0696 0.4786 -0.0188 -0.0289 -0.0500 291 LYS A CE  
2343 N NZ  A LYS A 291 ? 0.4009 0.8897 0.3978 -0.0825 -0.0243 -0.0427 291 LYS A NZ  
2344 N NZ  B LYS A 291 ? 0.2715 0.8845 0.2515 0.0133  -0.0294 -0.0541 291 LYS A NZ  
2345 N N   A GLN A 292 ? 0.4424 0.7018 0.4161 -0.0267 -0.0284 -0.0033 292 GLN A N   
2346 N N   B GLN A 292 ? 0.4420 0.7012 0.4156 -0.0266 -0.0284 -0.0033 292 GLN A N   
2347 C CA  A GLN A 292 ? 0.4511 0.6640 0.4223 -0.0220 -0.0267 0.0035  292 GLN A CA  
2348 C CA  B GLN A 292 ? 0.4505 0.6638 0.4218 -0.0218 -0.0267 0.0035  292 GLN A CA  
2349 C C   A GLN A 292 ? 0.4309 0.6041 0.3917 -0.0186 -0.0244 0.0089  292 GLN A C   
2350 C C   B GLN A 292 ? 0.4308 0.6037 0.3935 -0.0213 -0.0241 0.0086  292 GLN A C   
2351 O O   A GLN A 292 ? 0.4248 0.5633 0.3790 -0.0161 -0.0224 0.0133  292 GLN A O   
2352 O O   B GLN A 292 ? 0.4254 0.5646 0.3855 -0.0227 -0.0215 0.0127  292 GLN A O   
2353 C CB  A GLN A 292 ? 0.4125 0.6124 0.3959 -0.0420 -0.0234 0.0032  292 GLN A CB  
2354 C CB  B GLN A 292 ? 0.4153 0.6199 0.3990 -0.0405 -0.0239 0.0028  292 GLN A CB  
2355 C CG  A GLN A 292 ? 0.4312 0.6613 0.4213 -0.0476 -0.0246 -0.0013 292 GLN A CG  
2356 C CG  B GLN A 292 ? 0.4275 0.6713 0.4173 -0.0463 -0.0255 -0.0030 292 GLN A CG  
2357 C CD  A GLN A 292 ? 0.4540 0.6917 0.4408 -0.0263 -0.0280 0.0002  292 GLN A CD  
2358 C CD  B GLN A 292 ? 0.4039 0.6304 0.3999 -0.0586 -0.0232 -0.0021 292 GLN A CD  
2359 O OE1 A GLN A 292 ? 0.4830 0.7601 0.4656 -0.0123 -0.0319 -0.0040 292 GLN A OE1 
2360 O OE1 B GLN A 292 ? 0.4424 0.6311 0.4392 -0.0589 -0.0210 0.0027  292 GLN A OE1 
2361 N NE2 A GLN A 292 ? 0.4577 0.6601 0.4438 -0.0227 -0.0266 0.0053  292 GLN A NE2 
2362 N NE2 B GLN A 292 ? 0.4381 0.6960 0.4371 -0.0690 -0.0234 -0.0076 292 GLN A NE2 
2363 N N   . VAL A 293 ? 0.4384 0.6184 0.3961 -0.0208 -0.0243 0.0077  293 VAL A N   
2364 C CA  . VAL A 293 ? 0.3698 0.5157 0.3186 -0.0221 -0.0215 0.0117  293 VAL A CA  
2365 C C   . VAL A 293 ? 0.3514 0.4685 0.2743 -0.0034 -0.0220 0.0165  293 VAL A C   
2366 O O   . VAL A 293 ? 0.4420 0.5710 0.3485 0.0173  -0.0259 0.0161  293 VAL A O   
2367 C CB  . VAL A 293 ? 0.4286 0.5906 0.3788 -0.0280 -0.0215 0.0090  293 VAL A CB  
2368 C CG1 . VAL A 293 ? 0.3561 0.4872 0.2946 -0.0269 -0.0191 0.0129  293 VAL A CG1 
2369 C CG2 . VAL A 293 ? 0.3746 0.5466 0.3387 -0.0492 -0.0194 0.0048  293 VAL A CG2 
2370 N N   . THR A 294 ? 0.3575 0.4359 0.2714 -0.0105 -0.0177 0.0200  294 THR A N   
2371 C CA  . THR A 294 ? 0.3928 0.4306 0.2718 0.0010  -0.0161 0.0243  294 THR A CA  
2372 C C   . THR A 294 ? 0.4150 0.4222 0.2870 -0.0174 -0.0098 0.0256  294 THR A C   
2373 O O   . THR A 294 ? 0.5005 0.5210 0.3973 -0.0340 -0.0075 0.0231  294 THR A O   
2374 C CB  . THR A 294 ? 0.5160 0.5414 0.3834 0.0117  -0.0172 0.0255  294 THR A CB  
2375 O OG1 . THR A 294 ? 0.5046 0.4773 0.3279 0.0194  -0.0141 0.0295  294 THR A OG1 
2376 C CG2 . THR A 294 ? 0.3775 0.4081 0.2703 -0.0061 -0.0145 0.0241  294 THR A CG2 
2377 N N   . ASP A 295 ? 0.4931 0.4588 0.3262 -0.0138 -0.0067 0.0287  295 ASP A N   
2378 C CA  . ASP A 295 ? 0.5720 0.5102 0.3919 -0.0352 0.0005  0.0285  295 ASP A CA  
2379 C C   . ASP A 295 ? 0.5507 0.4555 0.3472 -0.0427 0.0051  0.0292  295 ASP A C   
2380 O O   . ASP A 295 ? 0.5629 0.4424 0.3385 -0.0631 0.0123  0.0280  295 ASP A O   
2381 C CB  . ASP A 295 ? 0.5607 0.4702 0.3469 -0.0348 0.0031  0.0307  295 ASP A CB  
2382 C CG  . ASP A 295 ? 0.6460 0.5048 0.3766 -0.0156 0.0029  0.0352  295 ASP A CG  
2383 O OD1 . ASP A 295 ? 0.6892 0.5429 0.4114 0.0019  -0.0005 0.0364  295 ASP A OD1 
2384 O OD2 . ASP A 295 ? 0.8616 0.6827 0.5526 -0.0168 0.0064  0.0375  295 ASP A OD2 
2385 N N   . GLU A 296 ? 0.5380 0.4458 0.3374 -0.0289 0.0015  0.0301  296 GLU A N   
2386 C CA  . GLU A 296 ? 0.6295 0.5025 0.4029 -0.0334 0.0054  0.0308  296 GLU A CA  
2387 C C   . GLU A 296 ? 0.5375 0.4303 0.3389 -0.0574 0.0097  0.0267  296 GLU A C   
2388 O O   . GLU A 296 ? 0.6623 0.5260 0.4390 -0.0703 0.0154  0.0259  296 GLU A O   
2389 C CB  . GLU A 296 ? 0.5508 0.4261 0.3193 -0.0074 -0.0007 0.0326  296 GLU A CB  
2390 C CG  . GLU A 296 ? 0.7293 0.5763 0.4535 0.0219  -0.0044 0.0359  296 GLU A CG  
2391 C CD  . GLU A 296 ? 0.8398 0.7164 0.5718 0.0515  -0.0124 0.0352  296 GLU A CD  
2392 O OE1 . GLU A 296 ? 0.7199 0.6562 0.5007 0.0495  -0.0168 0.0318  296 GLU A OE1 
2393 O OE2 . GLU A 296 ? 0.9184 0.7576 0.6034 0.0764  -0.0140 0.0374  296 GLU A OE2 
2394 N N   . PHE A 297 ? 0.4951 0.4347 0.3421 -0.0629 0.0074  0.0235  297 PHE A N   
2395 C CA  . PHE A 297 ? 0.5707 0.5329 0.4418 -0.0792 0.0104  0.0190  297 PHE A CA  
2396 C C   . PHE A 297 ? 0.4777 0.4791 0.3837 -0.0807 0.0080  0.0160  297 PHE A C   
2397 O O   . PHE A 297 ? 0.4146 0.4251 0.3285 -0.0707 0.0038  0.0175  297 PHE A O   
2398 C CB  . PHE A 297 ? 0.4753 0.4433 0.3579 -0.0724 0.0079  0.0195  297 PHE A CB  
2399 C CG  . PHE A 297 ? 0.3697 0.3539 0.2674 -0.0523 0.0006  0.0219  297 PHE A CG  
2400 C CD1 . PHE A 297 ? 0.3933 0.4123 0.3228 -0.0511 -0.0031 0.0201  297 PHE A CD1 
2401 C CD2 . PHE A 297 ? 0.4305 0.3956 0.3055 -0.0351 -0.0023 0.0250  297 PHE A CD2 
2402 C CE1 . PHE A 297 ? 0.3132 0.3516 0.2533 -0.0388 -0.0086 0.0206  297 PHE A CE1 
2403 C CE2 . PHE A 297 ? 0.3974 0.3899 0.2871 -0.0180 -0.0088 0.0251  297 PHE A CE2 
2404 C CZ  . PHE A 297 ? 0.3941 0.4253 0.3173 -0.0229 -0.0115 0.0225  297 PHE A CZ  
2405 N N   . ASP A 298 ? 0.4867 0.5113 0.4098 -0.0920 0.0106  0.0109  298 ASP A N   
2406 C CA  . ASP A 298 ? 0.4203 0.4758 0.3686 -0.0892 0.0083  0.0075  298 ASP A CA  
2407 C C   . ASP A 298 ? 0.3874 0.4506 0.3527 -0.0757 0.0023  0.0098  298 ASP A C   
2408 O O   . ASP A 298 ? 0.3811 0.4434 0.3515 -0.0712 0.0004  0.0112  298 ASP A O   
2409 C CB  . ASP A 298 ? 0.4168 0.4991 0.3765 -0.0974 0.0113  0.0008  298 ASP A CB  
2410 C CG  . ASP A 298 ? 0.5278 0.6197 0.4750 -0.1144 0.0176  -0.0047 298 ASP A CG  
2411 O OD1 . ASP A 298 ? 0.5157 0.5845 0.4415 -0.1218 0.0202  -0.0023 298 ASP A OD1 
2412 O OD2 . ASP A 298 ? 0.5082 0.6340 0.4650 -0.1203 0.0200  -0.0123 298 ASP A OD2 
2413 N N   . ILE A 299 ? 0.3618 0.4322 0.3328 -0.0718 0.0000  0.0095  299 ILE A N   
2414 C CA  . ILE A 299 ? 0.3190 0.3969 0.3006 -0.0659 -0.0038 0.0094  299 ILE A CA  
2415 C C   . ILE A 299 ? 0.3512 0.4370 0.3363 -0.0655 -0.0031 0.0052  299 ILE A C   
2416 O O   . ILE A 299 ? 0.3836 0.4720 0.3649 -0.0671 -0.0020 0.0037  299 ILE A O   
2417 C CB  . ILE A 299 ? 0.3445 0.4223 0.3222 -0.0627 -0.0066 0.0115  299 ILE A CB  
2418 C CG1 . ILE A 299 ? 0.3237 0.3960 0.2928 -0.0562 -0.0081 0.0148  299 ILE A CG1 
2419 C CG2 . ILE A 299 ? 0.3077 0.3927 0.2905 -0.0642 -0.0087 0.0096  299 ILE A CG2 
2420 C CD1 . ILE A 299 ? 0.3724 0.4551 0.3365 -0.0491 -0.0114 0.0154  299 ILE A CD1 
2421 N N   . VAL A 300 ? 0.2950 0.3836 0.2838 -0.0611 -0.0038 0.0030  300 VAL A N   
2422 C CA  . VAL A 300 ? 0.3119 0.4064 0.2971 -0.0541 -0.0035 -0.0017 300 VAL A CA  
2423 C C   . VAL A 300 ? 0.3163 0.3916 0.2897 -0.0494 -0.0055 -0.0015 300 VAL A C   
2424 O O   . VAL A 300 ? 0.3613 0.4261 0.3324 -0.0507 -0.0065 0.0002  300 VAL A O   
2425 C CB  . VAL A 300 ? 0.3809 0.4927 0.3709 -0.0496 -0.0023 -0.0056 300 VAL A CB  
2426 C CG1 . VAL A 300 ? 0.3558 0.4792 0.3383 -0.0358 -0.0029 -0.0117 300 VAL A CG1 
2427 C CG2 . VAL A 300 ? 0.2913 0.4178 0.2861 -0.0612 0.0013  -0.0067 300 VAL A CG2 
2428 N N   . ILE A 301 ? 0.2669 0.3348 0.2285 -0.0459 -0.0055 -0.0038 301 ILE A N   
2429 C CA  . ILE A 301 ? 0.3453 0.3855 0.2856 -0.0458 -0.0060 -0.0041 301 ILE A CA  
2430 C C   . ILE A 301 ? 0.3944 0.4181 0.3163 -0.0317 -0.0065 -0.0066 301 ILE A C   
2431 O O   . ILE A 301 ? 0.4071 0.4435 0.3270 -0.0161 -0.0069 -0.0105 301 ILE A O   
2432 C CB  . ILE A 301 ? 0.3651 0.3978 0.2938 -0.0468 -0.0055 -0.0058 301 ILE A CB  
2433 C CG1 . ILE A 301 ? 0.3156 0.3658 0.2606 -0.0577 -0.0053 -0.0033 301 ILE A CG1 
2434 C CG2 . ILE A 301 ? 0.3815 0.3779 0.2792 -0.0510 -0.0047 -0.0069 301 ILE A CG2 
2435 C CD1 . ILE A 301 ? 0.2822 0.3348 0.2320 -0.0686 -0.0061 -0.0005 301 ILE A CD1 
2436 N N   . THR A 302 ? 0.3804 0.3786 0.2865 -0.0363 -0.0063 -0.0051 302 THR A N   
2437 C CA  . THR A 302 ? 0.5189 0.4909 0.3979 -0.0213 -0.0067 -0.0070 302 THR A CA  
2438 C C   . THR A 302 ? 0.5756 0.5013 0.4097 -0.0166 -0.0055 -0.0091 302 THR A C   
2439 O O   . THR A 302 ? 0.6523 0.5574 0.4577 0.0061  -0.0063 -0.0120 302 THR A O   
2440 C CB  . THR A 302 ? 0.4898 0.4524 0.3685 -0.0296 -0.0065 -0.0044 302 THR A CB  
2441 O OG1 . THR A 302 ? 0.5038 0.4546 0.3765 -0.0520 -0.0048 -0.0028 302 THR A OG1 
2442 C CG2 . THR A 302 ? 0.4047 0.4062 0.3205 -0.0303 -0.0076 -0.0028 302 THR A CG2 
2443 N N   . TRP A 303 ? 0.5477 0.4566 0.3711 -0.0369 -0.0033 -0.0084 303 TRP A N   
2444 C CA  . TRP A 303 ? 0.5971 0.4573 0.3730 -0.0376 -0.0010 -0.0108 303 TRP A CA  
2445 C C   . TRP A 303 ? 0.5962 0.4656 0.3796 -0.0620 0.0009  -0.0111 303 TRP A C   
2446 O O   . TRP A 303 ? 0.5778 0.4828 0.3938 -0.0782 0.0005  -0.0093 303 TRP A O   
2447 C CB  . TRP A 303 ? 0.5744 0.3781 0.3007 -0.0414 0.0016  -0.0110 303 TRP A CB  
2448 C CG  . TRP A 303 ? 0.6350 0.4469 0.3719 -0.0700 0.0037  -0.0095 303 TRP A CG  
2449 C CD1 . TRP A 303 ? 0.6496 0.4867 0.4133 -0.0708 0.0021  -0.0071 303 TRP A CD1 
2450 C CD2 . TRP A 303 ? 0.6291 0.4321 0.3509 -0.1023 0.0077  -0.0115 303 TRP A CD2 
2451 N NE1 . TRP A 303 ? 0.6179 0.4626 0.3839 -0.0992 0.0045  -0.0075 303 TRP A NE1 
2452 C CE2 . TRP A 303 ? 0.5867 0.4145 0.3277 -0.1198 0.0081  -0.0107 303 TRP A CE2 
2453 C CE3 . TRP A 303 ? 0.6545 0.4345 0.3471 -0.1189 0.0113  -0.0148 303 TRP A CE3 
2454 C CZ2 . TRP A 303 ? 0.5564 0.3943 0.2899 -0.1529 0.0118  -0.0142 303 TRP A CZ2 
2455 C CZ3 . TRP A 303 ? 0.6326 0.4200 0.3169 -0.1541 0.0155  -0.0182 303 TRP A CZ3 
2456 C CH2 . TRP A 303 ? 0.5897 0.4095 0.2952 -0.1706 0.0156  -0.0183 303 TRP A CH2 
2457 N N   . SER A 304 ? 0.5667 0.4043 0.3168 -0.0622 0.0028  -0.0138 304 SER A N   
2458 C CA  . SER A 304 ? 0.6015 0.4478 0.3542 -0.0859 0.0051  -0.0151 304 SER A CA  
2459 C C   . SER A 304 ? 0.6186 0.4040 0.3111 -0.0940 0.0094  -0.0189 304 SER A C   
2460 O O   . SER A 304 ? 0.7280 0.4838 0.3932 -0.0723 0.0088  -0.0204 304 SER A O   
2461 C CB  . SER A 304 ? 0.5551 0.4461 0.3471 -0.0783 0.0024  -0.0144 304 SER A CB  
2462 O OG  . SER A 304 ? 0.5519 0.4464 0.3392 -0.0969 0.0044  -0.0163 304 SER A OG  
2463 N N   . GLU A 305 ? 0.7703 0.5383 0.4387 -0.1259 0.0141  -0.0213 305 GLU A N   
2464 C CA  . GLU A 305 ? 0.8074 0.5148 0.4131 -0.1415 0.0198  -0.0257 305 GLU A CA  
2465 C C   . GLU A 305 ? 0.7588 0.4803 0.3732 -0.1392 0.0192  -0.0275 305 GLU A C   
2466 O O   . GLU A 305 ? 0.9005 0.5708 0.4691 -0.1277 0.0209  -0.0296 305 GLU A O   
2467 C CB  . GLU A 305 ? 0.8819 0.5824 0.4648 -0.1837 0.0259  -0.0297 305 GLU A CB  
2468 C CG  . GLU A 305 ? 1.0604 0.7019 0.5765 -0.2102 0.0335  -0.0357 305 GLU A CG  
2469 C CD  . GLU A 305 ? 1.2731 0.9032 0.7565 -0.2552 0.0410  -0.0411 305 GLU A CD  
2470 O OE1 . GLU A 305 ? 1.2372 0.8630 0.7191 -0.2572 0.0411  -0.0394 305 GLU A OE1 
2471 O OE2 . GLU A 305 ? 1.2777 0.9150 0.7514 -0.2846 0.0479  -0.0431 305 GLU A OE2 
2472 N N   . ALA A 306 ? 0.6520 0.4410 0.3223 -0.1465 0.0166  -0.0267 306 ALA A N   
2473 C CA  . ALA A 306 ? 0.6948 0.4992 0.3729 -0.1481 0.0164  -0.0285 306 ALA A CA  
2474 C C   . ALA A 306 ? 0.7011 0.5038 0.3881 -0.1142 0.0125  -0.0266 306 ALA A C   
2475 O O   . ALA A 306 ? 0.7259 0.5072 0.3899 -0.1102 0.0137  -0.0293 306 ALA A O   
2476 C CB  . ALA A 306 ? 0.5284 0.4030 0.2582 -0.1612 0.0143  -0.0281 306 ALA A CB  
2477 N N   . GLN A 307 ? 0.6853 0.5151 0.4051 -0.0912 0.0082  -0.0231 307 GLN A N   
2478 C CA  . GLN A 307 ? 0.5896 0.4353 0.3240 -0.0622 0.0047  -0.0230 307 GLN A CA  
2479 C C   . GLN A 307 ? 0.6925 0.5341 0.4249 -0.0383 0.0024  -0.0223 307 GLN A C   
2480 O O   . GLN A 307 ? 0.6273 0.5145 0.4015 -0.0306 -0.0003 -0.0204 307 GLN A O   
2481 C CB  . GLN A 307 ? 0.5267 0.4323 0.3143 -0.0648 0.0023  -0.0208 307 GLN A CB  
2482 C CG  . GLN A 307 ? 0.5014 0.4193 0.2943 -0.0859 0.0039  -0.0216 307 GLN A CG  
2483 C CD  . GLN A 307 ? 0.6321 0.5276 0.3990 -0.0808 0.0052  -0.0252 307 GLN A CD  
2484 O OE1 . GLN A 307 ? 0.7000 0.5927 0.4624 -0.0578 0.0035  -0.0266 307 GLN A OE1 
2485 N NE2 . GLN A 307 ? 0.5841 0.4675 0.3329 -0.1024 0.0082  -0.0277 307 GLN A NE2 
2486 N N   . PRO A 308 ? 0.7165 0.5011 0.3953 -0.0253 0.0037  -0.0244 308 PRO A N   
2487 C CA  . PRO A 308 ? 0.7332 0.5120 0.4059 -0.0044 0.0016  -0.0237 308 PRO A CA  
2488 C C   . PRO A 308 ? 0.6611 0.4897 0.3654 0.0246  -0.0027 -0.0257 308 PRO A C   
2489 O O   . PRO A 308 ? 0.6731 0.5216 0.3924 0.0360  -0.0047 -0.0251 308 PRO A O   
2490 C CB  . PRO A 308 ? 0.6964 0.3940 0.2920 0.0076  0.0041  -0.0261 308 PRO A CB  
2491 C CG  . PRO A 308 ? 0.7810 0.4405 0.3434 -0.0158 0.0086  -0.0280 308 PRO A CG  
2492 C CD  . PRO A 308 ? 0.6398 0.3603 0.2559 -0.0236 0.0068  -0.0279 308 PRO A CD  
2493 N N   . GLU A 309 ? 0.6504 0.5031 0.3643 0.0348  -0.0039 -0.0289 309 GLU A N   
2494 C CA  . GLU A 309 ? 0.6899 0.5962 0.4298 0.0588  -0.0071 -0.0331 309 GLU A CA  
2495 C C   . GLU A 309 ? 0.5703 0.5391 0.3694 0.0414  -0.0072 -0.0308 309 GLU A C   
2496 O O   . GLU A 309 ? 0.6196 0.6376 0.4409 0.0536  -0.0085 -0.0352 309 GLU A O   
2497 C CB  . GLU A 309 ? 0.6259 0.5356 0.3500 0.0751  -0.0078 -0.0384 309 GLU A CB  
2498 C CG  . GLU A 309 ? 0.8077 0.7350 0.5576 0.0500  -0.0060 -0.0364 309 GLU A CG  
2499 C CD  . GLU A 309 ? 0.9393 0.8163 0.6656 0.0247  -0.0028 -0.0326 309 GLU A CD  
2500 O OE1 . GLU A 309 ? 0.7926 0.6913 0.5473 0.0005  -0.0015 -0.0299 309 GLU A OE1 
2501 O OE2 . GLU A 309 ? 0.8404 0.6569 0.5159 0.0287  -0.0012 -0.0331 309 GLU A OE2 
2502 N N   . GLN A 310 ? 0.5975 0.5661 0.4179 0.0133  -0.0055 -0.0251 310 GLN A N   
2503 C CA  . GLN A 310 ? 0.4986 0.5135 0.3638 -0.0004 -0.0054 -0.0225 310 GLN A CA  
2504 C C   . GLN A 310 ? 0.4888 0.5149 0.3668 0.0014  -0.0060 -0.0211 310 GLN A C   
2505 O O   . GLN A 310 ? 0.4745 0.5340 0.3828 -0.0085 -0.0054 -0.0196 310 GLN A O   
2506 C CB  . GLN A 310 ? 0.4616 0.4741 0.3404 -0.0250 -0.0041 -0.0177 310 GLN A CB  
2507 C CG  . GLN A 310 ? 0.5006 0.5076 0.3705 -0.0287 -0.0034 -0.0192 310 GLN A CG  
2508 C CD  . GLN A 310 ? 0.4674 0.5068 0.3493 -0.0180 -0.0036 -0.0230 310 GLN A CD  
2509 O OE1 . GLN A 310 ? 0.4801 0.5543 0.3864 -0.0203 -0.0033 -0.0232 310 GLN A OE1 
2510 N NE2 . GLN A 310 ? 0.6008 0.6284 0.4621 -0.0084 -0.0037 -0.0270 310 GLN A NE2 
2511 N N   . ALA A 311 ? 0.4714 0.4661 0.3224 0.0134  -0.0067 -0.0215 311 ALA A N   
2512 C CA  . ALA A 311 ? 0.5449 0.5477 0.4073 0.0137  -0.0073 -0.0198 311 ALA A CA  
2513 C C   . ALA A 311 ? 0.5115 0.5645 0.3967 0.0260  -0.0082 -0.0243 311 ALA A C   
2514 O O   . ALA A 311 ? 0.4136 0.4865 0.2901 0.0456  -0.0092 -0.0309 311 ALA A O   
2515 C CB  . ALA A 311 ? 0.4985 0.4525 0.3198 0.0258  -0.0077 -0.0198 311 ALA A CB  
2516 N N   . GLY A 312 ? 0.3771 0.4535 0.2893 0.0137  -0.0074 -0.0220 312 GLY A N   
2517 C CA  . GLY A 312 ? 0.4168 0.5423 0.3494 0.0169  -0.0068 -0.0271 312 GLY A CA  
2518 C C   . GLY A 312 ? 0.4302 0.5845 0.3860 -0.0037 -0.0038 -0.0269 312 GLY A C   
2519 O O   . GLY A 312 ? 0.3950 0.5827 0.3658 -0.0119 -0.0016 -0.0300 312 GLY A O   
2520 N N   . LYS A 313 ? 0.4301 0.5692 0.3844 -0.0134 -0.0033 -0.0238 313 LYS A N   
2521 C CA  . LYS A 313 ? 0.3849 0.5399 0.3524 -0.0319 -0.0004 -0.0227 313 LYS A CA  
2522 C C   . LYS A 313 ? 0.3462 0.4801 0.3202 -0.0469 0.0001  -0.0149 313 LYS A C   
2523 O O   . LYS A 313 ? 0.3460 0.4556 0.3162 -0.0452 -0.0021 -0.0106 313 LYS A O   
2524 C CB  . LYS A 313 ? 0.3612 0.5114 0.3217 -0.0318 -0.0004 -0.0234 313 LYS A CB  
2525 C CG  . LYS A 313 ? 0.3803 0.5470 0.3292 -0.0127 -0.0015 -0.0312 313 LYS A CG  
2526 C CD  . LYS A 313 ? 0.4756 0.6382 0.4195 -0.0161 -0.0011 -0.0314 313 LYS A CD  
2527 C CE  . LYS A 313 ? 0.6131 0.7876 0.5409 0.0064  -0.0027 -0.0392 313 LYS A CE  
2528 N NZ  . LYS A 313 ? 0.5219 0.6941 0.4460 0.0019  -0.0021 -0.0397 313 LYS A NZ  
2529 N N   . THR A 314 ? 0.2849 0.4274 0.2638 -0.0616 0.0032  -0.0138 314 THR A N   
2530 C CA  . THR A 314 ? 0.2914 0.4117 0.2695 -0.0702 0.0032  -0.0068 314 THR A CA  
2531 C C   . THR A 314 ? 0.3404 0.4457 0.3133 -0.0706 0.0016  -0.0031 314 THR A C   
2532 O O   . THR A 314 ? 0.3107 0.4217 0.2804 -0.0704 0.0022  -0.0055 314 THR A O   
2533 C CB  . THR A 314 ? 0.3928 0.5149 0.3655 -0.0844 0.0077  -0.0068 314 THR A CB  
2534 O OG1 . THR A 314 ? 0.3708 0.4932 0.3336 -0.0938 0.0107  -0.0078 314 THR A OG1 
2535 C CG2 . THR A 314 ? 0.2911 0.4398 0.2686 -0.0882 0.0104  -0.0134 314 THR A CG2 
2536 N N   . LEU A 315 ? 0.3124 0.4034 0.2846 -0.0703 -0.0006 0.0019  315 LEU A N   
2537 C CA  . LEU A 315 ? 0.2891 0.3741 0.2566 -0.0705 -0.0023 0.0044  315 LEU A CA  
2538 C C   . LEU A 315 ? 0.3014 0.3848 0.2604 -0.0749 0.0001  0.0050  315 LEU A C   
2539 O O   . LEU A 315 ? 0.2944 0.3797 0.2509 -0.0749 -0.0003 0.0043  315 LEU A O   
2540 C CB  . LEU A 315 ? 0.2712 0.3526 0.2383 -0.0681 -0.0048 0.0081  315 LEU A CB  
2541 C CG  . LEU A 315 ? 0.2921 0.3792 0.2558 -0.0670 -0.0072 0.0087  315 LEU A CG  
2542 C CD1 . LEU A 315 ? 0.2751 0.3640 0.2389 -0.0718 -0.0073 0.0051  315 LEU A CD1 
2543 C CD2 . LEU A 315 ? 0.3072 0.4031 0.2712 -0.0624 -0.0100 0.0102  315 LEU A CD2 
2544 N N   . GLN A 316 ? 0.3520 0.4283 0.3021 -0.0807 0.0033  0.0060  316 GLN A N   
2545 C CA  . GLN A 316 ? 0.4095 0.4768 0.3430 -0.0887 0.0069  0.0063  316 GLN A CA  
2546 C C   . GLN A 316 ? 0.3830 0.4709 0.3225 -0.0939 0.0090  0.0006  316 GLN A C   
2547 O O   . GLN A 316 ? 0.3623 0.4485 0.2955 -0.0954 0.0094  0.0008  316 GLN A O   
2548 C CB  . GLN A 316 ? 0.3543 0.4040 0.2690 -0.0988 0.0116  0.0071  316 GLN A CB  
2549 C CG  . GLN A 316 ? 0.4468 0.4729 0.3316 -0.1092 0.0163  0.0084  316 GLN A CG  
2550 C CD  . GLN A 316 ? 0.5691 0.5729 0.4382 -0.0959 0.0128  0.0144  316 GLN A CD  
2551 O OE1 . GLN A 316 ? 0.5850 0.5699 0.4416 -0.0836 0.0101  0.0188  316 GLN A OE1 
2552 N NE2 . GLN A 316 ? 0.5594 0.5699 0.4287 -0.0963 0.0125  0.0138  316 GLN A NE2 
2553 N N   . GLN A 317 ? 0.3399 0.4505 0.2904 -0.0944 0.0100  -0.0053 317 GLN A N   
2554 C CA  . GLN A 317 ? 0.3477 0.4846 0.3027 -0.0937 0.0111  -0.0122 317 GLN A CA  
2555 C C   . GLN A 317 ? 0.3974 0.5285 0.3545 -0.0829 0.0073  -0.0111 317 GLN A C   
2556 O O   . GLN A 317 ? 0.3995 0.5395 0.3533 -0.0847 0.0084  -0.0138 317 GLN A O   
2557 C CB  . GLN A 317 ? 0.3274 0.4921 0.2922 -0.0867 0.0108  -0.0189 317 GLN A CB  
2558 C CG  . GLN A 317 ? 0.3533 0.5400 0.3165 -0.1007 0.0158  -0.0241 317 GLN A CG  
2559 C CD  . GLN A 317 ? 0.3978 0.6221 0.3713 -0.0887 0.0145  -0.0324 317 GLN A CD  
2560 O OE1 . GLN A 317 ? 0.3632 0.5779 0.3417 -0.0733 0.0105  -0.0302 317 GLN A OE1 
2561 N NE2 . GLN A 317 ? 0.3383 0.6080 0.3122 -0.0946 0.0180  -0.0426 317 GLN A NE2 
2562 N N   . ILE A 318 ? 0.3227 0.4395 0.2828 -0.0739 0.0035  -0.0081 318 ILE A N   
2563 C CA  . ILE A 318 ? 0.3681 0.4758 0.3241 -0.0681 0.0011  -0.0083 318 ILE A CA  
2564 C C   . ILE A 318 ? 0.3762 0.4778 0.3284 -0.0741 0.0011  -0.0047 318 ILE A C   
2565 O O   . ILE A 318 ? 0.3742 0.4781 0.3225 -0.0736 0.0011  -0.0067 318 ILE A O   
2566 C CB  . ILE A 318 ? 0.2898 0.3818 0.2435 -0.0635 -0.0015 -0.0068 318 ILE A CB  
2567 C CG1 . ILE A 318 ? 0.3140 0.4086 0.2664 -0.0538 -0.0017 -0.0104 318 ILE A CG1 
2568 C CG2 . ILE A 318 ? 0.2989 0.3766 0.2411 -0.0636 -0.0025 -0.0077 318 ILE A CG2 
2569 C CD1 . ILE A 318 ? 0.3539 0.4308 0.3023 -0.0527 -0.0032 -0.0082 318 ILE A CD1 
2570 N N   . ALA A 319 ? 0.3660 0.4596 0.3162 -0.0774 0.0009  0.0003  319 ALA A N   
2571 C CA  . ALA A 319 ? 0.3306 0.4188 0.2723 -0.0786 0.0005  0.0035  319 ALA A CA  
2572 C C   . ALA A 319 ? 0.4407 0.5307 0.3745 -0.0849 0.0039  0.0019  319 ALA A C   
2573 O O   . ALA A 319 ? 0.3890 0.4801 0.3189 -0.0848 0.0035  0.0019  319 ALA A O   
2574 C CB  . ALA A 319 ? 0.3355 0.4119 0.2684 -0.0754 -0.0004 0.0085  319 ALA A CB  
2575 N N   . ASP A 320 ? 0.3272 0.4206 0.2576 -0.0928 0.0079  -0.0004 320 ASP A N   
2576 C CA  . ASP A 320 ? 0.3975 0.4969 0.3176 -0.1039 0.0124  -0.0035 320 ASP A CA  
2577 C C   . ASP A 320 ? 0.3879 0.5111 0.3184 -0.1001 0.0116  -0.0094 320 ASP A C   
2578 O O   . ASP A 320 ? 0.3945 0.5194 0.3187 -0.1037 0.0127  -0.0100 320 ASP A O   
2579 C CB  . ASP A 320 ? 0.4069 0.5122 0.3197 -0.1177 0.0177  -0.0070 320 ASP A CB  
2580 C CG  . ASP A 320 ? 0.4863 0.5587 0.3792 -0.1222 0.0194  -0.0012 320 ASP A CG  
2581 O OD1 . ASP A 320 ? 0.5279 0.5751 0.4089 -0.1130 0.0166  0.0052  320 ASP A OD1 
2582 O OD2 . ASP A 320 ? 0.5727 0.6457 0.4593 -0.1334 0.0234  -0.0038 320 ASP A OD2 
2583 N N   . GLU A 321 ? 0.3553 0.4943 0.2975 -0.0907 0.0096  -0.0140 321 GLU A N   
2584 C CA  . GLU A 321 ? 0.4132 0.5684 0.3577 -0.0815 0.0084  -0.0199 321 GLU A CA  
2585 C C   . GLU A 321 ? 0.4007 0.5383 0.3409 -0.0777 0.0058  -0.0168 321 GLU A C   
2586 O O   . GLU A 321 ? 0.3367 0.4829 0.2735 -0.0765 0.0062  -0.0201 321 GLU A O   
2587 C CB  . GLU A 321 ? 0.3997 0.5626 0.3475 -0.0668 0.0061  -0.0242 321 GLU A CB  
2588 C CG  . GLU A 321 ? 0.4574 0.6225 0.3971 -0.0506 0.0038  -0.0295 321 GLU A CG  
2589 C CD  . GLU A 321 ? 0.6228 0.7889 0.5563 -0.0323 0.0017  -0.0336 321 GLU A CD  
2590 O OE1 . GLU A 321 ? 0.5614 0.7475 0.5035 -0.0333 0.0026  -0.0355 321 GLU A OE1 
2591 O OE2 . GLU A 321 ? 0.6544 0.7977 0.5700 -0.0171 -0.0006 -0.0352 321 GLU A OE2 
2592 N N   . TRP A 322 ? 0.4310 0.5488 0.3709 -0.0768 0.0034  -0.0115 322 TRP A N   
2593 C CA  . TRP A 322 ? 0.4033 0.5113 0.3385 -0.0767 0.0015  -0.0101 322 TRP A CA  
2594 C C   . TRP A 322 ? 0.4086 0.5165 0.3404 -0.0825 0.0021  -0.0061 322 TRP A C   
2595 O O   . TRP A 322 ? 0.3559 0.4632 0.2844 -0.0828 0.0009  -0.0060 322 TRP A O   
2596 C CB  . TRP A 322 ? 0.3012 0.3968 0.2352 -0.0763 -0.0007 -0.0082 322 TRP A CB  
2597 C CG  . TRP A 322 ? 0.4363 0.5197 0.3625 -0.0705 -0.0011 -0.0120 322 TRP A CG  
2598 C CD1 . TRP A 322 ? 0.3490 0.4304 0.2660 -0.0605 -0.0007 -0.0170 322 TRP A CD1 
2599 C CD2 . TRP A 322 ? 0.3465 0.4150 0.2669 -0.0724 -0.0020 -0.0113 322 TRP A CD2 
2600 N NE1 . TRP A 322 ? 0.4884 0.5474 0.3897 -0.0538 -0.0013 -0.0189 322 TRP A NE1 
2601 C CE2 . TRP A 322 ? 0.3797 0.4291 0.2827 -0.0635 -0.0017 -0.0153 322 TRP A CE2 
2602 C CE3 . TRP A 322 ? 0.3529 0.4235 0.2779 -0.0799 -0.0029 -0.0084 322 TRP A CE3 
2603 C CZ2 . TRP A 322 ? 0.4257 0.4506 0.3127 -0.0647 -0.0016 -0.0157 322 TRP A CZ2 
2604 C CZ3 . TRP A 322 ? 0.3610 0.4159 0.2755 -0.0834 -0.0028 -0.0096 322 TRP A CZ3 
2605 C CH2 . TRP A 322 ? 0.3558 0.3844 0.2499 -0.0772 -0.0018 -0.0129 322 TRP A CH2 
2606 N N   . GLN A 323 ? 0.3766 0.4816 0.3042 -0.0870 0.0042  -0.0031 323 GLN A N   
2607 C CA  . GLN A 323 ? 0.4792 0.5738 0.3933 -0.0893 0.0049  0.0012  323 GLN A CA  
2608 C C   . GLN A 323 ? 0.4721 0.5633 0.3844 -0.0811 0.0009  0.0050  323 GLN A C   
2609 O O   . GLN A 323 ? 0.5068 0.6009 0.4129 -0.0782 -0.0005 0.0060  323 GLN A O   
2610 C CB  . GLN A 323 ? 0.3798 0.4814 0.2896 -0.0935 0.0066  -0.0014 323 GLN A CB  
2611 C CG  . GLN A 323 ? 0.4586 0.5753 0.3702 -0.1015 0.0106  -0.0071 323 GLN A CG  
2612 C CD  . GLN A 323 ? 0.5146 0.6420 0.4214 -0.1063 0.0126  -0.0104 323 GLN A CD  
2613 O OE1 . GLN A 323 ? 0.6110 0.7276 0.5014 -0.1153 0.0156  -0.0079 323 GLN A OE1 
2614 N NE2 . GLN A 323 ? 0.5116 0.6564 0.4280 -0.0995 0.0110  -0.0160 323 GLN A NE2 
2615 N N   . VAL A 324 ? 0.4322 0.5231 0.3501 -0.0772 -0.0010 0.0062  324 VAL A N   
2616 C CA  . VAL A 324 ? 0.4653 0.5630 0.3817 -0.0693 -0.0048 0.0081  324 VAL A CA  
2617 C C   . VAL A 324 ? 0.3988 0.4852 0.3084 -0.0628 -0.0053 0.0117  324 VAL A C   
2618 O O   . VAL A 324 ? 0.4207 0.4923 0.3271 -0.0674 -0.0024 0.0126  324 VAL A O   
2619 C CB  . VAL A 324 ? 0.3953 0.5098 0.3239 -0.0732 -0.0067 0.0038  324 VAL A CB  
2620 C CG1 . VAL A 324 ? 0.3164 0.4368 0.2443 -0.0791 -0.0060 0.0001  324 VAL A CG1 
2621 C CG2 . VAL A 324 ? 0.3876 0.4947 0.3240 -0.0770 -0.0056 0.0021  324 VAL A CG2 
2622 N N   . SER A 325 ? 0.4271 0.5247 0.3331 -0.0519 -0.0091 0.0127  325 SER A N   
2623 C CA  . SER A 325 ? 0.4709 0.5587 0.3678 -0.0420 -0.0104 0.0157  325 SER A CA  
2624 C C   . SER A 325 ? 0.4213 0.5178 0.3373 -0.0487 -0.0104 0.0135  325 SER A C   
2625 O O   . SER A 325 ? 0.3620 0.4723 0.2936 -0.0584 -0.0103 0.0096  325 SER A O   
2626 C CB  . SER A 325 ? 0.3781 0.4832 0.2635 -0.0236 -0.0151 0.0161  325 SER A CB  
2627 O OG  . SER A 325 ? 0.3869 0.5326 0.2922 -0.0281 -0.0177 0.0105  325 SER A OG  
2628 N N   . LEU A 326 ? 0.4361 0.5184 0.3451 -0.0432 -0.0103 0.0162  326 LEU A N   
2629 C CA  . LEU A 326 ? 0.4254 0.5157 0.3504 -0.0474 -0.0108 0.0146  326 LEU A CA  
2630 C C   . LEU A 326 ? 0.3641 0.4857 0.3018 -0.0484 -0.0139 0.0106  326 LEU A C   
2631 O O   . LEU A 326 ? 0.3760 0.5021 0.3254 -0.0596 -0.0129 0.0075  326 LEU A O   
2632 C CB  . LEU A 326 ? 0.4022 0.4746 0.3144 -0.0388 -0.0109 0.0180  326 LEU A CB  
2633 C CG  . LEU A 326 ? 0.4936 0.5341 0.3914 -0.0462 -0.0059 0.0202  326 LEU A CG  
2634 C CD1 . LEU A 326 ? 0.5111 0.5299 0.3898 -0.0372 -0.0060 0.0232  326 LEU A CD1 
2635 C CD2 . LEU A 326 ? 0.4415 0.4910 0.3599 -0.0607 -0.0030 0.0166  326 LEU A CD2 
2636 N N   . HIS A 327 ? 0.4430 0.5867 0.3739 -0.0373 -0.0174 0.0096  327 HIS A N   
2637 C CA  . HIS A 327 ? 0.3682 0.5509 0.3092 -0.0429 -0.0195 0.0037  327 HIS A CA  
2638 C C   . HIS A 327 ? 0.3748 0.5634 0.3212 -0.0610 -0.0172 -0.0006 327 HIS A C   
2639 O O   . HIS A 327 ? 0.3836 0.5811 0.3344 -0.0766 -0.0157 -0.0052 327 HIS A O   
2640 C CB  . HIS A 327 ? 0.3516 0.5678 0.2832 -0.0246 -0.0240 0.0018  327 HIS A CB  
2641 C CG  . HIS A 327 ? 0.4701 0.6867 0.3933 -0.0056 -0.0270 0.0039  327 HIS A CG  
2642 N ND1 . HIS A 327 ? 0.4605 0.6355 0.3624 0.0104  -0.0267 0.0105  327 HIS A ND1 
2643 C CD2 . HIS A 327 ? 0.5278 0.7789 0.4574 -0.0015 -0.0297 -0.0004 327 HIS A CD2 
2644 C CE1 . HIS A 327 ? 0.4841 0.6644 0.3781 0.0264  -0.0295 0.0107  327 HIS A CE1 
2645 N NE2 . HIS A 327 ? 0.4488 0.6788 0.3621 0.0206  -0.0317 0.0041  327 HIS A NE2 
2646 N N   . ASP A 328 ? 0.3527 0.5321 0.2935 -0.0597 -0.0163 0.0006  328 ASP A N   
2647 C CA  . ASP A 328 ? 0.3802 0.5599 0.3220 -0.0753 -0.0139 -0.0034 328 ASP A CA  
2648 C C   . ASP A 328 ? 0.3642 0.5152 0.3076 -0.0855 -0.0108 -0.0036 328 ASP A C   
2649 O O   . ASP A 328 ? 0.3984 0.5456 0.3361 -0.0994 -0.0088 -0.0081 328 ASP A O   
2650 C CB  . ASP A 328 ? 0.4350 0.6087 0.3708 -0.0704 -0.0136 -0.0017 328 ASP A CB  
2651 C CG  . ASP A 328 ? 0.5501 0.7576 0.4811 -0.0635 -0.0165 -0.0043 328 ASP A CG  
2652 O OD1 . ASP A 328 ? 0.6728 0.9158 0.6067 -0.0646 -0.0185 -0.0091 328 ASP A OD1 
2653 O OD2 . ASP A 328 ? 0.8319 1.0346 0.7555 -0.0568 -0.0167 -0.0023 328 ASP A OD2 
2654 N N   . ALA A 329 ? 0.2993 0.4288 0.2452 -0.0785 -0.0099 0.0006  329 ALA A N   
2655 C CA  . ALA A 329 ? 0.3379 0.4475 0.2844 -0.0830 -0.0078 -0.0005 329 ALA A CA  
2656 C C   . ALA A 329 ? 0.3578 0.4675 0.3038 -0.0891 -0.0079 -0.0024 329 ALA A C   
2657 O O   . ALA A 329 ? 0.4129 0.5051 0.3485 -0.0961 -0.0061 -0.0054 329 ALA A O   
2658 C CB  . ALA A 329 ? 0.2994 0.3975 0.2495 -0.0763 -0.0066 0.0025  329 ALA A CB  
2659 N N   . ALA A 330 ? 0.3348 0.4611 0.2869 -0.0854 -0.0100 -0.0010 330 ALA A N   
2660 C CA  . ALA A 330 ? 0.3409 0.4721 0.2926 -0.0932 -0.0100 -0.0034 330 ALA A CA  
2661 C C   . ALA A 330 ? 0.3877 0.5259 0.3271 -0.1112 -0.0081 -0.0096 330 ALA A C   
2662 O O   . ALA A 330 ? 0.3220 0.4378 0.2474 -0.1229 -0.0054 -0.0120 330 ALA A O   
2663 C CB  . ALA A 330 ? 0.3285 0.4838 0.2879 -0.0842 -0.0130 -0.0020 330 ALA A CB  
2664 N N   . ALA A 331 ? 0.3145 0.4808 0.2536 -0.1144 -0.0090 -0.0126 331 ALA A N   
2665 C CA  . ALA A 331 ? 0.3409 0.5182 0.2655 -0.1364 -0.0062 -0.0200 331 ALA A CA  
2666 C C   . ALA A 331 ? 0.3970 0.5289 0.3004 -0.1465 -0.0022 -0.0211 331 ALA A C   
2667 O O   . ALA A 331 ? 0.4207 0.5345 0.3001 -0.1669 0.0018  -0.0261 331 ALA A O   
2668 C CB  . ALA A 331 ? 0.3450 0.5632 0.2738 -0.1351 -0.0080 -0.0233 331 ALA A CB  
2669 N N   . ARG A 332 ? 0.3700 0.4812 0.2765 -0.1325 -0.0028 -0.0171 332 ARG A N   
2670 C CA  . ARG A 332 ? 0.4281 0.4989 0.3116 -0.1360 0.0003  -0.0188 332 ARG A CA  
2671 C C   . ARG A 332 ? 0.4860 0.5190 0.3540 -0.1321 0.0016  -0.0179 332 ARG A C   
2672 O O   . ARG A 332 ? 0.5366 0.5295 0.3736 -0.1346 0.0044  -0.0205 332 ARG A O   
2673 C CB  . ARG A 332 ? 0.4157 0.4848 0.3084 -0.1212 -0.0010 -0.0160 332 ARG A CB  
2674 C CG  . ARG A 332 ? 0.4956 0.5927 0.3946 -0.1254 -0.0018 -0.0174 332 ARG A CG  
2675 C CD  . ARG A 332 ? 0.6634 0.7591 0.5711 -0.1118 -0.0028 -0.0143 332 ARG A CD  
2676 N NE  . ARG A 332 ? 0.6368 0.7608 0.5524 -0.1109 -0.0044 -0.0138 332 ARG A NE  
2677 C CZ  . ARG A 332 ? 0.7292 0.8576 0.6370 -0.1175 -0.0034 -0.0170 332 ARG A CZ  
2678 N NH1 . ARG A 332 ? 0.8303 0.9327 0.7195 -0.1261 -0.0005 -0.0210 332 ARG A NH1 
2679 N NH2 . ARG A 332 ? 0.7571 0.9137 0.6717 -0.1135 -0.0054 -0.0164 332 ARG A NH2 
2680 N N   A LEU A 333 ? 0.4228 0.4648 0.3072 -0.1240 -0.0003 -0.0146 333 LEU A N   
2681 N N   B LEU A 333 ? 0.4225 0.4645 0.3070 -0.1239 -0.0003 -0.0145 333 LEU A N   
2682 C CA  A LEU A 333 ? 0.4273 0.4374 0.2970 -0.1191 0.0007  -0.0140 333 LEU A CA  
2683 C CA  B LEU A 333 ? 0.4269 0.4369 0.2965 -0.1190 0.0007  -0.0140 333 LEU A CA  
2684 C C   A LEU A 333 ? 0.4322 0.4290 0.2800 -0.1385 0.0034  -0.0171 333 LEU A C   
2685 C C   B LEU A 333 ? 0.4316 0.4276 0.2785 -0.1388 0.0035  -0.0173 333 LEU A C   
2686 O O   A LEU A 333 ? 0.5212 0.4775 0.3417 -0.1372 0.0054  -0.0176 333 LEU A O   
2687 O O   B LEU A 333 ? 0.5246 0.4787 0.3426 -0.1380 0.0056  -0.0179 333 LEU A O   
2688 C CB  A LEU A 333 ? 0.4260 0.4518 0.3222 -0.1029 -0.0022 -0.0094 333 LEU A CB  
2689 C CB  B LEU A 333 ? 0.4262 0.4523 0.3224 -0.1033 -0.0021 -0.0094 333 LEU A CB  
2690 C CG  A LEU A 333 ? 0.4041 0.4375 0.3144 -0.0870 -0.0034 -0.0075 333 LEU A CG  
2691 C CG  B LEU A 333 ? 0.4040 0.4383 0.3148 -0.0876 -0.0034 -0.0075 333 LEU A CG  
2692 C CD1 A LEU A 333 ? 0.3571 0.4095 0.2903 -0.0794 -0.0049 -0.0039 333 LEU A CD1 
2693 C CD1 B LEU A 333 ? 0.3490 0.4051 0.2839 -0.0809 -0.0051 -0.0037 333 LEU A CD1 
2694 C CD2 A LEU A 333 ? 0.4082 0.4146 0.2978 -0.0755 -0.0024 -0.0102 333 LEU A CD2 
2695 C CD2 B LEU A 333 ? 0.4051 0.4137 0.2975 -0.0750 -0.0026 -0.0097 333 LEU A CD2 
2696 N N   . MET A 334 ? 0.4007 0.4319 0.2563 -0.1559 0.0038  -0.0202 334 MET A N   
2697 C CA  . MET A 334 ? 0.4340 0.4642 0.2730 -0.1769 0.0067  -0.0241 334 MET A CA  
2698 C C   . MET A 334 ? 0.4921 0.4774 0.2814 -0.2014 0.0130  -0.0299 334 MET A C   
2699 O O   . MET A 334 ? 0.4958 0.4689 0.2690 -0.2072 0.0150  -0.0326 334 MET A O   
2700 C CB  . MET A 334 ? 0.4277 0.5199 0.2904 -0.1861 0.0048  -0.0274 334 MET A CB  
2701 C CG  . MET A 334 ? 0.4110 0.5334 0.3095 -0.1620 -0.0007 -0.0216 334 MET A CG  
2702 S SD  . MET A 334 ? 0.4784 0.6728 0.3973 -0.1627 -0.0040 -0.0260 334 MET A SD  
2703 C CE  . MET A 334 ? 0.3520 0.5554 0.2971 -0.1313 -0.0096 -0.0180 334 MET A CE  
2704 N N   . PRO A 335 ? 0.5031 0.4563 0.2614 -0.2166 0.0169  -0.0320 335 PRO A N   
2705 C CA  . PRO A 335 ? 0.5188 0.4773 0.2902 -0.2097 0.0150  -0.0288 335 PRO A CA  
2706 C C   . PRO A 335 ? 0.5512 0.4827 0.3317 -0.1770 0.0113  -0.0219 335 PRO A C   
2707 O O   . PRO A 335 ? 0.5783 0.4620 0.3296 -0.1650 0.0124  -0.0212 335 PRO A O   
2708 C CB  . PRO A 335 ? 0.5568 0.4739 0.2766 -0.2402 0.0220  -0.0343 335 PRO A CB  
2709 C CG  . PRO A 335 ? 0.7070 0.5684 0.3757 -0.2524 0.0273  -0.0378 335 PRO A CG  
2710 C CD  . PRO A 335 ? 0.6018 0.5082 0.3021 -0.2476 0.0246  -0.0387 335 PRO A CD  
2711 N N   . ALA A 336 ? 0.4390 0.4037 0.2576 -0.1617 0.0070  -0.0176 336 ALA A N   
2712 C CA  . ALA A 336 ? 0.4761 0.4286 0.3076 -0.1340 0.0039  -0.0126 336 ALA A CA  
2713 C C   . ALA A 336 ? 0.4517 0.4221 0.3037 -0.1297 0.0019  -0.0100 336 ALA A C   
2714 O O   . ALA A 336 ? 0.4398 0.4390 0.3026 -0.1442 0.0020  -0.0116 336 ALA A O   
2715 C CB  . ALA A 336 ? 0.4010 0.3805 0.2627 -0.1171 0.0006  -0.0101 336 ALA A CB  
2716 N N   . GLY A 337 ? 0.5130 0.4701 0.3693 -0.1090 0.0001  -0.0070 337 GLY A N   
2717 C CA  . GLY A 337 ? 0.4791 0.4545 0.3580 -0.1020 -0.0020 -0.0042 337 GLY A CA  
2718 C C   . GLY A 337 ? 0.4680 0.4704 0.3792 -0.0843 -0.0049 -0.0014 337 GLY A C   
2719 O O   . GLY A 337 ? 0.3942 0.3937 0.3045 -0.0738 -0.0050 -0.0020 337 GLY A O   
2720 N N   . ALA A 338 ? 0.3698 0.3975 0.3055 -0.0827 -0.0066 0.0009  338 ALA A N   
2721 C CA  . ALA A 338 ? 0.3315 0.3783 0.2894 -0.0715 -0.0078 0.0029  338 ALA A CA  
2722 C C   . ALA A 338 ? 0.3716 0.4270 0.3426 -0.0669 -0.0086 0.0047  338 ALA A C   
2723 O O   . ALA A 338 ? 0.3168 0.3750 0.2889 -0.0725 -0.0092 0.0053  338 ALA A O   
2724 C CB  . ALA A 338 ? 0.2854 0.3523 0.2551 -0.0744 -0.0087 0.0042  338 ALA A CB  
2725 N N   . ILE A 339 ? 0.3192 0.3819 0.2992 -0.0585 -0.0082 0.0046  339 ILE A N   
2726 C CA  . ILE A 339 ? 0.3730 0.4467 0.3656 -0.0566 -0.0081 0.0059  339 ILE A CA  
2727 C C   . ILE A 339 ? 0.4033 0.4846 0.4019 -0.0598 -0.0079 0.0082  339 ILE A C   
2728 O O   . ILE A 339 ? 0.3838 0.4659 0.3796 -0.0609 -0.0069 0.0080  339 ILE A O   
2729 C CB  . ILE A 339 ? 0.3405 0.4224 0.3349 -0.0492 -0.0067 0.0026  339 ILE A CB  
2730 C CG1 . ILE A 339 ? 0.2628 0.3319 0.2434 -0.0395 -0.0077 0.0005  339 ILE A CG1 
2731 C CG2 . ILE A 339 ? 0.3506 0.4449 0.3557 -0.0521 -0.0054 0.0029  339 ILE A CG2 
2732 C CD1 . ILE A 339 ? 0.3577 0.4374 0.3320 -0.0261 -0.0073 -0.0046 339 ILE A CD1 
2733 N N   . TYR A 340 ? 0.3361 0.4196 0.3382 -0.0596 -0.0089 0.0104  340 TYR A N   
2734 C CA  . TYR A 340 ? 0.3649 0.4464 0.3623 -0.0577 -0.0089 0.0129  340 TYR A CA  
2735 C C   . TYR A 340 ? 0.3670 0.4414 0.3620 -0.0584 -0.0066 0.0134  340 TYR A C   
2736 O O   . TYR A 340 ? 0.3516 0.4284 0.3517 -0.0566 -0.0076 0.0137  340 TYR A O   
2737 C CB  . TYR A 340 ? 0.3503 0.4412 0.3467 -0.0533 -0.0123 0.0139  340 TYR A CB  
2738 C CG  . TYR A 340 ? 0.3524 0.4557 0.3489 -0.0574 -0.0138 0.0119  340 TYR A CG  
2739 C CD1 . TYR A 340 ? 0.3366 0.4437 0.3344 -0.0659 -0.0137 0.0093  340 TYR A CD1 
2740 C CD2 . TYR A 340 ? 0.3002 0.4090 0.2905 -0.0542 -0.0147 0.0121  340 TYR A CD2 
2741 C CE1 . TYR A 340 ? 0.3679 0.4837 0.3595 -0.0748 -0.0138 0.0064  340 TYR A CE1 
2742 C CE2 . TYR A 340 ? 0.3651 0.4892 0.3547 -0.0605 -0.0155 0.0091  340 TYR A CE2 
2743 C CZ  . TYR A 340 ? 0.4389 0.5665 0.4286 -0.0725 -0.0147 0.0059  340 TYR A CZ  
2744 O OH  . TYR A 340 ? 0.3972 0.5376 0.3805 -0.0836 -0.0143 0.0019  340 TYR A OH  
2745 N N   . HIS A 341 ? 0.3126 0.3778 0.2970 -0.0636 -0.0030 0.0129  341 HIS A N   
2746 C CA  . HIS A 341 ? 0.4135 0.4684 0.3881 -0.0697 0.0007  0.0123  341 HIS A CA  
2747 C C   . HIS A 341 ? 0.4077 0.4374 0.3607 -0.0634 0.0002  0.0162  341 HIS A C   
2748 O O   . HIS A 341 ? 0.4423 0.4451 0.3680 -0.0685 0.0041  0.0170  341 HIS A O   
2749 C CB  . HIS A 341 ? 0.3544 0.4117 0.3210 -0.0829 0.0062  0.0083  341 HIS A CB  
2750 C CG  . HIS A 341 ? 0.4393 0.5270 0.4240 -0.0842 0.0065  0.0028  341 HIS A CG  
2751 N ND1 . HIS A 341 ? 0.4317 0.5376 0.4222 -0.0892 0.0089  -0.0020 341 HIS A ND1 
2752 C CD2 . HIS A 341 ? 0.3853 0.4879 0.3796 -0.0777 0.0044  0.0007  341 HIS A CD2 
2753 C CE1 . HIS A 341 ? 0.4624 0.5957 0.4649 -0.0828 0.0078  -0.0068 341 HIS A CE1 
2754 N NE2 . HIS A 341 ? 0.3584 0.4863 0.3614 -0.0753 0.0051  -0.0050 341 HIS A NE2 
2755 N N   . ASN A 342 ? 0.3532 0.3905 0.3138 -0.0517 -0.0045 0.0180  342 ASN A N   
2756 C CA  . ASN A 342 ? 0.4287 0.4509 0.3690 -0.0376 -0.0071 0.0209  342 ASN A CA  
2757 C C   . ASN A 342 ? 0.4405 0.4508 0.3726 -0.0339 -0.0067 0.0215  342 ASN A C   
2758 O O   . ASN A 342 ? 0.3792 0.3802 0.2938 -0.0174 -0.0097 0.0232  342 ASN A O   
2759 C CB  . ASN A 342 ? 0.3344 0.3836 0.2864 -0.0264 -0.0127 0.0206  342 ASN A CB  
2760 C CG  . ASN A 342 ? 0.3872 0.4638 0.3633 -0.0292 -0.0152 0.0185  342 ASN A CG  
2761 O OD1 . ASN A 342 ? 0.3568 0.4334 0.3451 -0.0386 -0.0131 0.0176  342 ASN A OD1 
2762 N ND2 . ASN A 342 ? 0.3978 0.5000 0.3777 -0.0215 -0.0193 0.0169  342 ASN A ND2 
2763 N N   . MET A 343 ? 0.4226 0.4344 0.3642 -0.0469 -0.0032 0.0194  343 MET A N   
2764 C CA  . MET A 343 ? 0.3812 0.3774 0.3112 -0.0468 -0.0015 0.0195  343 MET A CA  
2765 C C   . MET A 343 ? 0.4489 0.4208 0.3568 -0.0652 0.0061  0.0173  343 MET A C   
2766 O O   . MET A 343 ? 0.4933 0.4754 0.4064 -0.0792 0.0097  0.0144  343 MET A O   
2767 C CB  . MET A 343 ? 0.3869 0.4117 0.3468 -0.0472 -0.0040 0.0180  343 MET A CB  
2768 C CG  . MET A 343 ? 0.3725 0.4200 0.3469 -0.0343 -0.0102 0.0189  343 MET A CG  
2769 S SD  . MET A 343 ? 0.4702 0.5444 0.4736 -0.0400 -0.0117 0.0169  343 MET A SD  
2770 C CE  . MET A 343 ? 0.3259 0.4087 0.3405 -0.0488 -0.0105 0.0151  343 MET A CE  
2771 N N   . ASP A 344 ? 0.4496 0.3899 0.3292 -0.0661 0.0090  0.0179  344 ASP A N   
2772 C CA  . ASP A 344 ? 0.4647 0.3777 0.3145 -0.0886 0.0176  0.0146  344 ASP A CA  
2773 C C   . ASP A 344 ? 0.5295 0.4682 0.4008 -0.1008 0.0198  0.0102  344 ASP A C   
2774 O O   . ASP A 344 ? 0.4131 0.3523 0.2911 -0.0898 0.0165  0.0117  344 ASP A O   
2775 C CB  . ASP A 344 ? 0.5196 0.3694 0.3115 -0.0832 0.0207  0.0177  344 ASP A CB  
2776 C CG  . ASP A 344 ? 0.6242 0.4394 0.3773 -0.1122 0.0311  0.0134  344 ASP A CG  
2777 O OD1 . ASP A 344 ? 0.8520 0.6915 0.6161 -0.1379 0.0368  0.0078  344 ASP A OD1 
2778 O OD2 . ASP A 344 ? 0.8874 0.6532 0.5968 -0.1101 0.0341  0.0147  344 ASP A OD2 
2779 N N   . GLU A 345 ? 0.4998 0.4636 0.3806 -0.1227 0.0253  0.0038  345 GLU A N   
2780 C CA  . GLU A 345 ? 0.3855 0.3826 0.2871 -0.1330 0.0272  -0.0018 345 GLU A CA  
2781 C C   . GLU A 345 ? 0.4055 0.3717 0.2818 -0.1382 0.0304  -0.0017 345 GLU A C   
2782 O O   . GLU A 345 ? 0.4189 0.4088 0.3175 -0.1348 0.0284  -0.0032 345 GLU A O   
2783 C CB  . GLU A 345 ? 0.3695 0.3988 0.2732 -0.1570 0.0339  -0.0108 345 GLU A CB  
2784 C CG  . GLU A 345 ? 0.5047 0.5790 0.4293 -0.1660 0.0359  -0.0185 345 GLU A CG  
2785 C CD  . GLU A 345 ? 0.5663 0.6806 0.5329 -0.1424 0.0277  -0.0174 345 GLU A CD  
2786 O OE1 . GLU A 345 ? 0.4216 0.5359 0.4011 -0.1258 0.0221  -0.0128 345 GLU A OE1 
2787 O OE2 . GLU A 345 ? 0.5543 0.6966 0.5363 -0.1412 0.0272  -0.0213 345 GLU A OE2 
2788 N N   . GLN A 346 ? 0.4924 0.4015 0.3172 -0.1465 0.0358  -0.0002 346 GLN A N   
2789 C CA  . GLN A 346 ? 0.5267 0.3991 0.3201 -0.1509 0.0393  -0.0003 346 GLN A CA  
2790 C C   . GLN A 346 ? 0.5093 0.3773 0.3157 -0.1195 0.0305  0.0060  346 GLN A C   
2791 O O   . GLN A 346 ? 0.5699 0.4382 0.3785 -0.1187 0.0305  0.0049  346 GLN A O   
2792 C CB  . GLN A 346 ? 0.6278 0.4264 0.3495 -0.1660 0.0479  -0.0001 346 GLN A CB  
2793 C CG  . GLN A 346 ? 0.6737 0.4740 0.3729 -0.2055 0.0590  -0.0082 346 GLN A CG  
2794 C CD  . GLN A 346 ? 0.8478 0.7072 0.5784 -0.2297 0.0633  -0.0180 346 GLN A CD  
2795 O OE1 . GLN A 346 ? 0.8404 0.6960 0.5681 -0.2324 0.0644  -0.0197 346 GLN A OE1 
2796 N NE2 . GLN A 346 ? 0.8012 0.7192 0.5614 -0.2448 0.0652  -0.0252 346 GLN A NE2 
2797 N N   . ASP A 347 ? 0.4710 0.3390 0.2852 -0.0946 0.0232  0.0115  347 ASP A N   
2798 C CA  . ASP A 347 ? 0.4715 0.3527 0.3041 -0.0671 0.0147  0.0153  347 ASP A CA  
2799 C C   . ASP A 347 ? 0.4230 0.3576 0.3070 -0.0694 0.0114  0.0131  347 ASP A C   
2800 O O   . ASP A 347 ? 0.4792 0.4185 0.3698 -0.0622 0.0092  0.0133  347 ASP A O   
2801 C CB  . ASP A 347 ? 0.4902 0.3791 0.3283 -0.0449 0.0080  0.0192  347 ASP A CB  
2802 C CG  . ASP A 347 ? 0.5697 0.4034 0.3519 -0.0291 0.0085  0.0224  347 ASP A CG  
2803 O OD1 . ASP A 347 ? 0.6130 0.4010 0.3525 -0.0248 0.0113  0.0228  347 ASP A OD1 
2804 O OD2 . ASP A 347 ? 0.5516 0.3853 0.3289 -0.0191 0.0060  0.0244  347 ASP A OD2 
2805 N N   . VAL A 348 ? 0.3620 0.3344 0.2787 -0.0775 0.0109  0.0110  348 VAL A N   
2806 C CA  . VAL A 348 ? 0.3568 0.3720 0.3136 -0.0759 0.0076  0.0093  348 VAL A CA  
2807 C C   . VAL A 348 ? 0.4284 0.4488 0.3852 -0.0880 0.0117  0.0053  348 VAL A C   
2808 O O   . VAL A 348 ? 0.3468 0.3838 0.3225 -0.0808 0.0084  0.0057  348 VAL A O   
2809 C CB  . VAL A 348 ? 0.3354 0.3802 0.3147 -0.0800 0.0071  0.0072  348 VAL A CB  
2810 C CG1 . VAL A 348 ? 0.2682 0.3458 0.2775 -0.0746 0.0036  0.0059  348 VAL A CG1 
2811 C CG2 . VAL A 348 ? 0.2835 0.3215 0.2606 -0.0697 0.0034  0.0109  348 VAL A CG2 
2812 N N   . ARG A 349 ? 0.3746 0.3807 0.3071 -0.1088 0.0195  0.0007  349 ARG A N   
2813 C CA  . ARG A 349 ? 0.3876 0.4030 0.3178 -0.1241 0.0243  -0.0047 349 ARG A CA  
2814 C C   . ARG A 349 ? 0.4501 0.4306 0.3593 -0.1164 0.0237  -0.0015 349 ARG A C   
2815 O O   . ARG A 349 ? 0.4393 0.4380 0.3643 -0.1161 0.0229  -0.0033 349 ARG A O   
2816 C CB  . ARG A 349 ? 0.3988 0.4097 0.3026 -0.1539 0.0342  -0.0121 349 ARG A CB  
2817 C CG  . ARG A 349 ? 0.4599 0.5190 0.3876 -0.1610 0.0349  -0.0177 349 ARG A CG  
2818 C CD  . ARG A 349 ? 0.4361 0.5034 0.3384 -0.1949 0.0456  -0.0275 349 ARG A CD  
2819 N NE  . ARG A 349 ? 0.4973 0.6192 0.4249 -0.1965 0.0450  -0.0336 349 ARG A NE  
2820 C CZ  . ARG A 349 ? 0.5880 0.7552 0.5160 -0.2136 0.0498  -0.0456 349 ARG A CZ  
2821 N NH1 . ARG A 349 ? 0.6158 0.7785 0.5198 -0.2304 0.0547  -0.0531 349 ARG A NH1 
2822 N NH2 . ARG A 349 ? 0.5171 0.7308 0.4649 -0.2054 0.0471  -0.0507 349 ARG A NH2 
2823 N N   . ARG A 350 ? 0.4327 0.3623 0.3031 -0.1077 0.0238  0.0028  350 ARG A N   
2824 C CA  . ARG A 350 ? 0.4992 0.3949 0.3451 -0.0944 0.0224  0.0055  350 ARG A CA  
2825 C C   . ARG A 350 ? 0.4467 0.3794 0.3328 -0.0725 0.0135  0.0083  350 ARG A C   
2826 O O   . ARG A 350 ? 0.4700 0.4019 0.3567 -0.0686 0.0128  0.0077  350 ARG A O   
2827 C CB  . ARG A 350 ? 0.4466 0.2827 0.2401 -0.0800 0.0225  0.0097  350 ARG A CB  
2828 C CG  . ARG A 350 ? 0.6350 0.4065 0.3641 -0.1007 0.0327  0.0073  350 ARG A CG  
2829 C CD  . ARG A 350 ? 0.6439 0.3476 0.3123 -0.0782 0.0317  0.0122  350 ARG A CD  
2830 N NE  . ARG A 350 ? 0.6577 0.3686 0.3320 -0.0684 0.0284  0.0152  350 ARG A NE  
2831 C CZ  . ARG A 350 ? 0.7533 0.4311 0.3931 -0.0877 0.0354  0.0143  350 ARG A CZ  
2832 N NH1 . ARG A 350 ? 0.8508 0.4867 0.4455 -0.1210 0.0469  0.0097  350 ARG A NH1 
2833 N NH2 . ARG A 350 ? 0.7306 0.4185 0.3792 -0.0758 0.0315  0.0173  350 ARG A NH2 
2834 N N   . VAL A 351 ? 0.3843 0.3485 0.3011 -0.0605 0.0074  0.0107  351 VAL A N   
2835 C CA  . VAL A 351 ? 0.4067 0.4041 0.3554 -0.0449 0.0002  0.0124  351 VAL A CA  
2836 C C   . VAL A 351 ? 0.4130 0.4439 0.3936 -0.0554 0.0008  0.0096  351 VAL A C   
2837 O O   . VAL A 351 ? 0.3585 0.4031 0.3526 -0.0488 -0.0022 0.0099  351 VAL A O   
2838 C CB  . VAL A 351 ? 0.3424 0.3600 0.3070 -0.0339 -0.0051 0.0146  351 VAL A CB  
2839 C CG1 . VAL A 351 ? 0.3435 0.3989 0.3397 -0.0272 -0.0106 0.0147  351 VAL A CG1 
2840 C CG2 . VAL A 351 ? 0.3844 0.3756 0.3172 -0.0166 -0.0072 0.0169  351 VAL A CG2 
2841 N N   . MET A 352 ? 0.3623 0.4092 0.3535 -0.0698 0.0044  0.0063  352 MET A N   
2842 C CA  . MET A 352 ? 0.2856 0.3649 0.3013 -0.0749 0.0046  0.0029  352 MET A CA  
2843 C C   . MET A 352 ? 0.3332 0.4072 0.3403 -0.0828 0.0081  0.0000  352 MET A C   
2844 O O   . MET A 352 ? 0.3220 0.4172 0.3480 -0.0788 0.0059  -0.0006 352 MET A O   
2845 C CB  . MET A 352 ? 0.3537 0.4557 0.3770 -0.0850 0.0078  -0.0017 352 MET A CB  
2846 C CG  . MET A 352 ? 0.3594 0.4782 0.4006 -0.0740 0.0031  0.0002  352 MET A CG  
2847 S SD  . MET A 352 ? 0.4926 0.6445 0.5405 -0.0802 0.0062  -0.0070 352 MET A SD  
2848 C CE  . MET A 352 ? 0.4647 0.5980 0.4885 -0.0988 0.0127  -0.0092 352 MET A CE  
2849 N N   . ARG A 353 ? 0.3413 0.3833 0.3153 -0.0954 0.0142  -0.0019 353 ARG A N   
2850 C CA  . ARG A 353 ? 0.3674 0.4005 0.3277 -0.1065 0.0187  -0.0056 353 ARG A CA  
2851 C C   . ARG A 353 ? 0.3761 0.3859 0.3269 -0.0900 0.0147  -0.0013 353 ARG A C   
2852 O O   . ARG A 353 ? 0.4562 0.4642 0.4027 -0.0956 0.0170  -0.0038 353 ARG A O   
2853 C CB  . ARG A 353 ? 0.4599 0.4610 0.3786 -0.1314 0.0284  -0.0104 353 ARG A CB  
2854 C CG  . ARG A 353 ? 0.4814 0.5170 0.4101 -0.1507 0.0331  -0.0171 353 ARG A CG  
2855 C CD  . ARG A 353 ? 0.5340 0.5331 0.4159 -0.1775 0.0429  -0.0215 353 ARG A CD  
2856 N NE  . ARG A 353 ? 0.8103 0.7813 0.6579 -0.1973 0.0503  -0.0260 353 ARG A NE  
2857 C CZ  . ARG A 353 ? 1.0063 0.9078 0.8042 -0.1955 0.0530  -0.0221 353 ARG A CZ  
2858 N NH1 . ARG A 353 ? 0.8650 0.7214 0.6408 -0.1735 0.0487  -0.0141 353 ARG A NH1 
2859 N NH2 . ARG A 353 ? 0.9394 0.8155 0.7052 -0.2145 0.0600  -0.0268 353 ARG A NH2 
2860 N N   . TYR A 354 ? 0.3985 0.3962 0.3463 -0.0694 0.0088  0.0040  354 TYR A N   
2861 C CA  . TYR A 354 ? 0.3735 0.3575 0.3112 -0.0506 0.0046  0.0066  354 TYR A CA  
2862 C C   . TYR A 354 ? 0.3700 0.3908 0.3418 -0.0492 0.0015  0.0056  354 TYR A C   
2863 O O   . TYR A 354 ? 0.2932 0.3501 0.2984 -0.0508 -0.0012 0.0057  354 TYR A O   
2864 C CB  . TYR A 354 ? 0.3803 0.3649 0.3160 -0.0282 -0.0020 0.0104  354 TYR A CB  
2865 C CG  . TYR A 354 ? 0.4065 0.3755 0.3202 -0.0052 -0.0060 0.0114  354 TYR A CG  
2866 C CD1 . TYR A 354 ? 0.4736 0.3866 0.3345 0.0010  -0.0024 0.0114  354 TYR A CD1 
2867 C CD2 . TYR A 354 ? 0.3714 0.3804 0.3117 0.0101  -0.0129 0.0116  354 TYR A CD2 
2868 C CE1 . TYR A 354 ? 0.5033 0.4013 0.3393 0.0274  -0.0066 0.0118  354 TYR A CE1 
2869 C CE2 . TYR A 354 ? 0.5142 0.5184 0.4351 0.0335  -0.0171 0.0110  354 TYR A CE2 
2870 C CZ  . TYR A 354 ? 0.5082 0.4572 0.3774 0.0448  -0.0144 0.0112  354 TYR A CZ  
2871 O OH  . TYR A 354 ? 0.5694 0.5131 0.4150 0.0733  -0.0191 0.0102  354 TYR A OH  
2872 N N   . PRO A 355 ? 0.4374 0.4454 0.3969 -0.0461 0.0020  0.0047  355 PRO A N   
2873 C CA  . PRO A 355 ? 0.4078 0.4484 0.3969 -0.0497 0.0008  0.0030  355 PRO A CA  
2874 C C   . PRO A 355 ? 0.4016 0.4792 0.4242 -0.0381 -0.0062 0.0054  355 PRO A C   
2875 O O   . PRO A 355 ? 0.3796 0.4840 0.4269 -0.0440 -0.0066 0.0044  355 PRO A O   
2876 C CB  . PRO A 355 ? 0.3941 0.4068 0.3566 -0.0455 0.0024  0.0019  355 PRO A CB  
2877 C CG  . PRO A 355 ? 0.4715 0.4304 0.3843 -0.0504 0.0080  0.0014  355 PRO A CG  
2878 C CD  . PRO A 355 ? 0.3698 0.3265 0.2811 -0.0408 0.0051  0.0045  355 PRO A CD  
2879 N N   . VAL A 356 ? 0.3168 0.3972 0.3370 -0.0227 -0.0112 0.0077  356 VAL A N   
2880 C CA  . VAL A 356 ? 0.3566 0.4722 0.4025 -0.0178 -0.0164 0.0085  356 VAL A CA  
2881 C C   . VAL A 356 ? 0.3553 0.4817 0.4114 -0.0221 -0.0173 0.0096  356 VAL A C   
2882 O O   . VAL A 356 ? 0.3173 0.4664 0.3842 -0.0199 -0.0208 0.0097  356 VAL A O   
2883 C CB  . VAL A 356 ? 0.3600 0.4867 0.3991 -0.0003 -0.0212 0.0078  356 VAL A CB  
2884 C CG1 . VAL A 356 ? 0.4125 0.5310 0.4437 0.0043  -0.0207 0.0065  356 VAL A CG1 
2885 C CG2 . VAL A 356 ? 0.3622 0.4710 0.3752 0.0149  -0.0227 0.0083  356 VAL A CG2 
2886 N N   . THR A 357 ? 0.2667 0.3788 0.3176 -0.0303 -0.0136 0.0097  357 THR A N   
2887 C CA  . THR A 357 ? 0.2489 0.3689 0.3074 -0.0334 -0.0144 0.0107  357 THR A CA  
2888 C C   . THR A 357 ? 0.2331 0.3679 0.3081 -0.0404 -0.0140 0.0101  357 THR A C   
2889 O O   . THR A 357 ? 0.2367 0.3729 0.3144 -0.0454 -0.0111 0.0081  357 THR A O   
2890 C CB  . THR A 357 ? 0.3051 0.4049 0.3485 -0.0375 -0.0109 0.0106  357 THR A CB  
2891 O OG1 . THR A 357 ? 0.3175 0.3957 0.3370 -0.0273 -0.0117 0.0117  357 THR A OG1 
2892 C CG2 . THR A 357 ? 0.2566 0.3659 0.3091 -0.0404 -0.0118 0.0112  357 THR A CG2 
2893 N N   . MET A 358 ? 0.1816 0.3266 0.2624 -0.0406 -0.0167 0.0110  358 MET A N   
2894 C CA  . MET A 358 ? 0.2417 0.3879 0.3255 -0.0442 -0.0163 0.0110  358 MET A CA  
2895 C C   . MET A 358 ? 0.2690 0.4075 0.3474 -0.0450 -0.0153 0.0111  358 MET A C   
2896 O O   . MET A 358 ? 0.2610 0.3964 0.3359 -0.0452 -0.0155 0.0117  358 MET A O   
2897 C CB  . MET A 358 ? 0.1811 0.3329 0.2634 -0.0481 -0.0183 0.0115  358 MET A CB  
2898 C CG  . MET A 358 ? 0.2216 0.3849 0.3101 -0.0474 -0.0193 0.0109  358 MET A CG  
2899 S SD  . MET A 358 ? 0.2955 0.4755 0.3806 -0.0564 -0.0211 0.0094  358 MET A SD  
2900 C CE  . MET A 358 ? 0.3328 0.5345 0.4199 -0.0498 -0.0237 0.0073  358 MET A CE  
2901 N N   . ILE A 359 ? 0.2101 0.3456 0.2852 -0.0428 -0.0145 0.0103  359 ILE A N   
2902 C CA  . ILE A 359 ? 0.2014 0.3291 0.2682 -0.0408 -0.0140 0.0099  359 ILE A CA  
2903 C C   . ILE A 359 ? 0.3059 0.4176 0.3580 -0.0441 -0.0151 0.0115  359 ILE A C   
2904 O O   . ILE A 359 ? 0.2769 0.3788 0.3186 -0.0444 -0.0153 0.0120  359 ILE A O   
2905 C CB  . ILE A 359 ? 0.2638 0.3992 0.3289 -0.0325 -0.0128 0.0068  359 ILE A CB  
2906 C CG1 . ILE A 359 ? 0.3063 0.4615 0.3829 -0.0362 -0.0103 0.0034  359 ILE A CG1 
2907 C CG2 . ILE A 359 ? 0.1573 0.2871 0.2126 -0.0278 -0.0125 0.0057  359 ILE A CG2 
2908 C CD1 . ILE A 359 ? 0.2592 0.4114 0.3355 -0.0449 -0.0080 0.0031  359 ILE A CD1 
2909 N N   . GLY A 360 ? 0.2510 0.3576 0.2981 -0.0485 -0.0151 0.0120  360 GLY A N   
2910 C CA  . GLY A 360 ? 0.2785 0.3658 0.3049 -0.0549 -0.0147 0.0123  360 GLY A CA  
2911 C C   . GLY A 360 ? 0.3404 0.4170 0.3581 -0.0514 -0.0140 0.0119  360 GLY A C   
2912 O O   . GLY A 360 ? 0.3676 0.4574 0.3986 -0.0500 -0.0141 0.0117  360 GLY A O   
2913 N N   . SER A 361 ? 0.3257 0.3738 0.3161 -0.0495 -0.0131 0.0117  361 SER A N   
2914 C CA  . SER A 361 ? 0.3466 0.3842 0.3268 -0.0433 -0.0126 0.0109  361 SER A CA  
2915 C C   . SER A 361 ? 0.3734 0.4108 0.3520 -0.0572 -0.0120 0.0109  361 SER A C   
2916 O O   . SER A 361 ? 0.3178 0.3602 0.3017 -0.0538 -0.0121 0.0105  361 SER A O   
2917 C CB  . SER A 361 ? 0.3016 0.3022 0.2446 -0.0324 -0.0120 0.0104  361 SER A CB  
2918 O OG  . SER A 361 ? 0.3966 0.3629 0.3077 -0.0479 -0.0098 0.0112  361 SER A OG  
2919 N N   . ASP A 362 ? 0.3296 0.3662 0.3008 -0.0737 -0.0112 0.0105  362 ASP A N   
2920 C CA  . ASP A 362 ? 0.4020 0.4428 0.3670 -0.0884 -0.0102 0.0089  362 ASP A CA  
2921 C C   . ASP A 362 ? 0.4270 0.4342 0.3642 -0.0871 -0.0084 0.0085  362 ASP A C   
2922 O O   . ASP A 362 ? 0.3892 0.4032 0.3292 -0.0910 -0.0082 0.0076  362 ASP A O   
2923 C CB  . ASP A 362 ? 0.3243 0.4013 0.3185 -0.0852 -0.0125 0.0088  362 ASP A CB  
2924 C CG  . ASP A 362 ? 0.3696 0.4649 0.3600 -0.1001 -0.0121 0.0057  362 ASP A CG  
2925 O OD1 . ASP A 362 ? 0.4445 0.5331 0.4140 -0.1186 -0.0096 0.0027  362 ASP A OD1 
2926 O OD2 . ASP A 362 ? 0.3719 0.4887 0.3765 -0.0944 -0.0139 0.0056  362 ASP A OD2 
2927 N N   . GLY A 363 ? 0.4790 0.4473 0.3851 -0.0794 -0.0071 0.0090  363 GLY A N   
2928 C CA  . GLY A 363 ? 0.3853 0.3141 0.2559 -0.0742 -0.0054 0.0084  363 GLY A CA  
2929 C C   . GLY A 363 ? 0.4793 0.3824 0.3168 -0.0999 -0.0014 0.0062  363 GLY A C   
2930 O O   . GLY A 363 ? 0.4878 0.3884 0.3126 -0.1217 0.0011  0.0047  363 GLY A O   
2931 N N   . LEU A 364 ? 0.5059 0.3922 0.3276 -0.0993 -0.0004 0.0052  364 LEU A N   
2932 C CA  . LEU A 364 ? 0.5381 0.3983 0.3241 -0.1254 0.0042  0.0021  364 LEU A CA  
2933 C C   . LEU A 364 ? 0.5739 0.3625 0.2985 -0.1170 0.0071  0.0022  364 LEU A C   
2934 O O   . LEU A 364 ? 0.6659 0.4444 0.3859 -0.1002 0.0058  0.0023  364 LEU A O   
2935 C CB  . LEU A 364 ? 0.4441 0.3432 0.2590 -0.1325 0.0032  0.0004  364 LEU A CB  
2936 C CG  . LEU A 364 ? 0.4883 0.4524 0.3554 -0.1343 -0.0002 0.0003  364 LEU A CG  
2937 C CD1 . LEU A 364 ? 0.4045 0.4011 0.2887 -0.1416 -0.0008 -0.0020 364 LEU A CD1 
2938 C CD2 . LEU A 364 ? 0.3732 0.3545 0.2393 -0.1535 0.0013  -0.0022 364 LEU A CD2 
2939 N N   . PRO A 365 ? 0.6273 0.3615 0.2988 -0.1266 0.0112  0.0019  365 PRO A N   
2940 C CA  . PRO A 365 ? 0.6869 0.3432 0.2909 -0.1089 0.0132  0.0026  365 PRO A CA  
2941 C C   . PRO A 365 ? 0.7934 0.4014 0.3473 -0.1247 0.0181  -0.0002 365 PRO A C   
2942 O O   . PRO A 365 ? 0.8990 0.4434 0.3976 -0.1027 0.0188  0.0003  365 PRO A O   
2943 C CB  . PRO A 365 ? 0.7875 0.3968 0.3453 -0.1186 0.0168  0.0033  365 PRO A CB  
2944 C CG  . PRO A 365 ? 0.6899 0.3479 0.2809 -0.1555 0.0190  0.0010  365 PRO A CG  
2945 C CD  . PRO A 365 ? 0.6237 0.3669 0.2960 -0.1461 0.0130  0.0014  365 PRO A CD  
2946 N N   . ASN A 366 ? 0.7277 0.3631 0.2945 -0.1604 0.0216  -0.0039 366 ASN A N   
2947 C CA  . ASN A 366 ? 0.7449 0.3363 0.2630 -0.1796 0.0270  -0.0075 366 ASN A CA  
2948 C C   . ASN A 366 ? 0.6701 0.3032 0.2304 -0.1661 0.0230  -0.0076 366 ASN A C   
2949 O O   . ASN A 366 ? 0.8312 0.4318 0.3561 -0.1777 0.0268  -0.0104 366 ASN A O   
2950 C CB  . ASN A 366 ? 0.7379 0.3322 0.2336 -0.2315 0.0346  -0.0135 366 ASN A CB  
2951 C CG  . ASN A 366 ? 0.8250 0.3634 0.2626 -0.2487 0.0402  -0.0147 366 ASN A CG  
2952 O OD1 . ASN A 366 ? 0.9816 0.4383 0.3544 -0.2336 0.0417  -0.0156 366 ASN A OD1 
2953 N ND2 . ASN A 366 ? 0.7654 0.3611 0.2354 -0.2697 0.0404  -0.0183 366 ASN A ND2 
2954 N N   . ASP A 367 ? 0.6395 0.3381 0.2687 -0.1430 0.0162  -0.0048 367 ASP A N   
2955 C CA  . ASP A 367 ? 0.6643 0.4004 0.3317 -0.1289 0.0125  -0.0045 367 ASP A CA  
2956 C C   . ASP A 367 ? 0.7917 0.4772 0.4191 -0.1015 0.0120  -0.0042 367 ASP A C   
2957 O O   . ASP A 367 ? 0.6953 0.3519 0.3004 -0.0733 0.0100  -0.0025 367 ASP A O   
2958 C CB  . ASP A 367 ? 0.5922 0.3953 0.3283 -0.1105 0.0064  -0.0016 367 ASP A CB  
2959 C CG  . ASP A 367 ? 0.6355 0.4818 0.4125 -0.1023 0.0034  -0.0015 367 ASP A CG  
2960 O OD1 . ASP A 367 ? 0.7805 0.6049 0.5369 -0.0983 0.0044  -0.0029 367 ASP A OD1 
2961 O OD2 . ASP A 367 ? 0.6436 0.5423 0.4701 -0.0990 0.0001  0.0000  367 ASP A OD2 
2962 N N   . PRO A 368 ? 0.8223 0.4986 0.4380 -0.1063 0.0134  -0.0063 368 PRO A N   
2963 C CA  . PRO A 368 ? 0.9109 0.5403 0.4857 -0.0771 0.0126  -0.0067 368 PRO A CA  
2964 C C   . PRO A 368 ? 0.9033 0.5745 0.5184 -0.0376 0.0059  -0.0054 368 PRO A C   
2965 O O   . PRO A 368 ? 0.8735 0.5096 0.4509 -0.0052 0.0042  -0.0063 368 PRO A O   
2966 C CB  . PRO A 368 ? 0.9559 0.5837 0.5244 -0.0953 0.0152  -0.0096 368 PRO A CB  
2967 C CG  . PRO A 368 ? 0.8624 0.5190 0.4475 -0.1375 0.0190  -0.0117 368 PRO A CG  
2968 C CD  . PRO A 368 ? 0.7352 0.4454 0.3717 -0.1367 0.0156  -0.0092 368 PRO A CD  
2969 N N   . MET A 369 ? 0.6823 0.4273 0.3676 -0.0395 0.0024  -0.0043 369 MET A N   
2970 C CA  . MET A 369 ? 0.6631 0.4547 0.3876 -0.0107 -0.0024 -0.0043 369 MET A CA  
2971 C C   . MET A 369 ? 0.5394 0.3760 0.3102 -0.0184 -0.0040 -0.0020 369 MET A C   
2972 O O   . MET A 369 ? 0.5325 0.4153 0.3490 -0.0319 -0.0048 -0.0009 369 MET A O   
2973 C CB  . MET A 369 ? 0.6257 0.4546 0.3808 -0.0075 -0.0039 -0.0058 369 MET A CB  
2974 C CG  . MET A 369 ? 0.7306 0.5468 0.4603 0.0230  -0.0056 -0.0094 369 MET A CG  
2975 S SD  . MET A 369 ? 0.7828 0.6467 0.5371 0.0559  -0.0099 -0.0124 369 MET A SD  
2976 C CE  . MET A 369 ? 0.6211 0.5471 0.4436 0.0304  -0.0099 -0.0094 369 MET A CE  
2977 N N   . PRO A 370 ? 0.6005 0.4213 0.3564 -0.0087 -0.0045 -0.0012 370 PRO A N   
2978 C CA  . PRO A 370 ? 0.5563 0.4108 0.3488 -0.0208 -0.0052 0.0010  370 PRO A CA  
2979 C C   . PRO A 370 ? 0.4724 0.3868 0.3173 -0.0103 -0.0082 0.0007  370 PRO A C   
2980 O O   . PRO A 370 ? 0.4400 0.3708 0.2880 0.0120  -0.0100 -0.0021 370 PRO A O   
2981 C CB  . PRO A 370 ? 0.5313 0.3460 0.2858 -0.0101 -0.0047 0.0016  370 PRO A CB  
2982 C CG  . PRO A 370 ? 0.6091 0.3885 0.3200 0.0213  -0.0058 -0.0008 370 PRO A CG  
2983 C CD  . PRO A 370 ? 0.5992 0.3626 0.2958 0.0134  -0.0041 -0.0022 370 PRO A CD  
2984 N N   . HIS A 371 ? 0.3492 0.2964 0.2308 -0.0275 -0.0083 0.0028  371 HIS A N   
2985 C CA  . HIS A 371 ? 0.3291 0.3201 0.2497 -0.0221 -0.0099 0.0028  371 HIS A CA  
2986 C C   . HIS A 371 ? 0.3652 0.3568 0.2786 -0.0039 -0.0110 0.0012  371 HIS A C   
2987 O O   . HIS A 371 ? 0.4116 0.3735 0.3009 -0.0033 -0.0107 0.0025  371 HIS A O   
2988 C CB  . HIS A 371 ? 0.3365 0.3465 0.2819 -0.0402 -0.0098 0.0054  371 HIS A CB  
2989 C CG  . HIS A 371 ? 0.3070 0.3519 0.2845 -0.0384 -0.0104 0.0057  371 HIS A CG  
2990 N ND1 . HIS A 371 ? 0.3067 0.3667 0.2927 -0.0282 -0.0106 0.0040  371 HIS A ND1 
2991 C CD2 . HIS A 371 ? 0.3009 0.3645 0.2976 -0.0464 -0.0104 0.0071  371 HIS A CD2 
2992 C CE1 . HIS A 371 ? 0.3181 0.4016 0.3256 -0.0338 -0.0099 0.0041  371 HIS A CE1 
2993 N NE2 . HIS A 371 ? 0.3060 0.3878 0.3177 -0.0433 -0.0098 0.0064  371 HIS A NE2 
2994 N N   . PRO A 372 ? 0.4079 0.4606 0.2124 -0.0347 0.0210  -0.0139 372 PRO A N   
2995 C CA  . PRO A 372 ? 0.3528 0.4148 0.1810 -0.0271 0.0301  -0.0171 372 PRO A CA  
2996 C C   . PRO A 372 ? 0.4221 0.4904 0.2782 -0.0257 0.0220  -0.0133 372 PRO A C   
2997 O O   . PRO A 372 ? 0.3326 0.4071 0.2072 -0.0199 0.0265  -0.0163 372 PRO A O   
2998 C CB  . PRO A 372 ? 0.4042 0.4780 0.2332 -0.0276 0.0425  -0.0120 372 PRO A CB  
2999 C CG  . PRO A 372 ? 0.4006 0.4718 0.2147 -0.0362 0.0364  -0.0025 372 PRO A CG  
3000 C CD  . PRO A 372 ? 0.3756 0.4319 0.1659 -0.0395 0.0263  -0.0063 372 PRO A CD  
3001 N N   . ARG A 373 ? 0.3594 0.4261 0.2186 -0.0300 0.0105  -0.0065 373 ARG A N   
3002 C CA  . ARG A 373 ? 0.3142 0.3848 0.1968 -0.0277 0.0042  -0.0043 373 ARG A CA  
3003 C C   . ARG A 373 ? 0.3346 0.4022 0.2244 -0.0235 0.0026  -0.0120 373 ARG A C   
3004 O O   . ARG A 373 ? 0.3369 0.4089 0.2455 -0.0202 0.0018  -0.0121 373 ARG A O   
3005 C CB  . ARG A 373 ? 0.2785 0.3466 0.1616 -0.0310 -0.0072 0.0034  373 ARG A CB  
3006 C CG  . ARG A 373 ? 0.3404 0.4027 0.2100 -0.0340 -0.0164 0.0021  373 ARG A CG  
3007 C CD  . ARG A 373 ? 0.3779 0.4404 0.2463 -0.0369 -0.0267 0.0122  373 ARG A CD  
3008 N NE  . ARG A 373 ? 0.3442 0.4060 0.2078 -0.0398 -0.0380 0.0123  373 ARG A NE  
3009 C CZ  . ARG A 373 ? 0.4329 0.4947 0.2865 -0.0440 -0.0481 0.0203  373 ARG A CZ  
3010 N NH1 . ARG A 373 ? 0.3756 0.4353 0.2201 -0.0454 -0.0479 0.0289  373 ARG A NH1 
3011 N NH2 . ARG A 373 ? 0.3369 0.4011 0.1896 -0.0476 -0.0594 0.0208  373 ARG A NH2 
3012 N N   . LEU A 374 ? 0.3671 0.4254 0.2399 -0.0246 0.0018  -0.0184 374 LEU A N   
3013 C CA  . LEU A 374 ? 0.3598 0.4119 0.2368 -0.0218 0.0005  -0.0253 374 LEU A CA  
3014 C C   . LEU A 374 ? 0.3562 0.4123 0.2464 -0.0143 0.0099  -0.0289 374 LEU A C   
3015 O O   . LEU A 374 ? 0.3954 0.4508 0.2984 -0.0113 0.0076  -0.0306 374 LEU A O   
3016 C CB  . LEU A 374 ? 0.3064 0.3440 0.1584 -0.0254 -0.0011 -0.0322 374 LEU A CB  
3017 C CG  . LEU A 374 ? 0.4416 0.4670 0.2917 -0.0232 -0.0006 -0.0406 374 LEU A CG  
3018 C CD1 . LEU A 374 ? 0.3563 0.3851 0.2239 -0.0257 -0.0103 -0.0374 374 LEU A CD1 
3019 C CD2 . LEU A 374 ? 0.4190 0.4258 0.2383 -0.0280 -0.0014 -0.0485 374 LEU A CD2 
3020 N N   . TRP A 375 ? 0.3482 0.4105 0.2368 -0.0114 0.0201  -0.0287 375 TRP A N   
3021 C CA  . TRP A 375 ? 0.3684 0.4383 0.2714 -0.0037 0.0290  -0.0306 375 TRP A CA  
3022 C C   . TRP A 375 ? 0.3191 0.4062 0.2407 -0.0044 0.0315  -0.0233 375 TRP A C   
3023 O O   . TRP A 375 ? 0.3028 0.4001 0.2397 0.0011  0.0372  -0.0233 375 TRP A O   
3024 C CB  . TRP A 375 ? 0.4085 0.4738 0.2966 0.0015  0.0410  -0.0369 375 TRP A CB  
3025 C CG  . TRP A 375 ? 0.4241 0.4692 0.2946 0.0039  0.0407  -0.0461 375 TRP A CG  
3026 C CD1 . TRP A 375 ? 0.4002 0.4289 0.2455 -0.0027 0.0352  -0.0504 375 TRP A CD1 
3027 C CD2 . TRP A 375 ? 0.4836 0.5208 0.3590 0.0131  0.0459  -0.0522 375 TRP A CD2 
3028 N NE1 . TRP A 375 ? 0.4449 0.4543 0.2780 0.0007  0.0366  -0.0595 375 TRP A NE1 
3029 C CE2 . TRP A 375 ? 0.4760 0.4892 0.3272 0.0111  0.0436  -0.0606 375 TRP A CE2 
3030 C CE3 . TRP A 375 ? 0.4342 0.4819 0.3320 0.0226  0.0513  -0.0505 375 TRP A CE3 
3031 C CZ2 . TRP A 375 ? 0.4357 0.4320 0.2837 0.0186  0.0472  -0.0678 375 TRP A CZ2 
3032 C CZ3 . TRP A 375 ? 0.3852 0.4183 0.2811 0.0312  0.0547  -0.0567 375 TRP A CZ3 
3033 C CH2 . TRP A 375 ? 0.4426 0.4487 0.3133 0.0294  0.0532  -0.0655 375 TRP A CH2 
3034 N N   . GLY A 376 ? 0.3629 0.4528 0.2837 -0.0111 0.0268  -0.0167 376 GLY A N   
3035 C CA  . GLY A 376 ? 0.3067 0.4100 0.2413 -0.0135 0.0300  -0.0102 376 GLY A CA  
3036 C C   . GLY A 376 ? 0.2824 0.3851 0.2258 -0.0188 0.0216  -0.0040 376 GLY A C   
3037 O O   . GLY A 376 ? 0.3124 0.4238 0.2671 -0.0221 0.0232  0.0007  376 GLY A O   
3038 N N   . ALA A 377 ? 0.2825 0.3750 0.2213 -0.0196 0.0129  -0.0040 377 ALA A N   
3039 C CA  . ALA A 377 ? 0.3174 0.4064 0.2617 -0.0230 0.0062  0.0017  377 ALA A CA  
3040 C C   . ALA A 377 ? 0.3490 0.4426 0.3092 -0.0231 0.0061  0.0022  377 ALA A C   
3041 O O   . ALA A 377 ? 0.3131 0.4060 0.2763 -0.0280 0.0052  0.0073  377 ALA A O   
3042 C CB  . ALA A 377 ? 0.2627 0.3441 0.2052 -0.0212 -0.0020 0.0011  377 ALA A CB  
3043 N N   . PHE A 378 ? 0.2349 0.3315 0.2039 -0.0186 0.0059  -0.0026 378 PHE A N   
3044 C CA  . PHE A 378 ? 0.2447 0.3436 0.2254 -0.0196 0.0034  -0.0022 378 PHE A CA  
3045 C C   . PHE A 378 ? 0.2584 0.3695 0.2479 -0.0232 0.0073  0.0006  378 PHE A C   
3046 O O   . PHE A 378 ? 0.2784 0.3881 0.2711 -0.0295 0.0046  0.0043  378 PHE A O   
3047 C CB  . PHE A 378 ? 0.2773 0.3749 0.2625 -0.0144 0.0011  -0.0068 378 PHE A CB  
3048 C CG  . PHE A 378 ? 0.2814 0.3699 0.2616 -0.0127 -0.0030 -0.0079 378 PHE A CG  
3049 C CD1 . PHE A 378 ? 0.2367 0.3191 0.2189 -0.0130 -0.0067 -0.0066 378 PHE A CD1 
3050 C CD2 . PHE A 378 ? 0.2234 0.3095 0.1965 -0.0112 -0.0032 -0.0097 378 PHE A CD2 
3051 C CE1 . PHE A 378 ? 0.3328 0.4108 0.3139 -0.0105 -0.0096 -0.0063 378 PHE A CE1 
3052 C CE2 . PHE A 378 ? 0.3187 0.4003 0.2902 -0.0108 -0.0079 -0.0091 378 PHE A CE2 
3053 C CZ  . PHE A 378 ? 0.2660 0.3454 0.2433 -0.0099 -0.0107 -0.0069 378 PHE A CZ  
3054 N N   . PRO A 379 ? 0.2748 0.3980 0.2689 -0.0200 0.0138  -0.0004 379 PRO A N   
3055 C CA  . PRO A 379 ? 0.2129 0.3523 0.2186 -0.0240 0.0180  0.0041  379 PRO A CA  
3056 C C   . PRO A 379 ? 0.2761 0.4152 0.2762 -0.0324 0.0202  0.0100  379 PRO A C   
3057 O O   . PRO A 379 ? 0.2810 0.4308 0.2914 -0.0395 0.0208  0.0152  379 PRO A O   
3058 C CB  . PRO A 379 ? 0.2970 0.4482 0.3072 -0.0160 0.0265  0.0016  379 PRO A CB  
3059 C CG  . PRO A 379 ? 0.2922 0.4284 0.2872 -0.0100 0.0268  -0.0046 379 PRO A CG  
3060 C CD  . PRO A 379 ? 0.2717 0.3942 0.2623 -0.0121 0.0174  -0.0057 379 PRO A CD  
3061 N N   . ARG A 380 ? 0.2818 0.4091 0.2656 -0.0327 0.0206  0.0104  380 ARG A N   
3062 C CA  . ARG A 380 ? 0.2928 0.4177 0.2694 -0.0409 0.0220  0.0175  380 ARG A CA  
3063 C C   . ARG A 380 ? 0.2921 0.4058 0.2713 -0.0477 0.0141  0.0213  380 ARG A C   
3064 O O   . ARG A 380 ? 0.3025 0.4174 0.2831 -0.0568 0.0149  0.0280  380 ARG A O   
3065 C CB  . ARG A 380 ? 0.2916 0.4059 0.2486 -0.0394 0.0226  0.0177  380 ARG A CB  
3066 C CG  . ARG A 380 ? 0.2832 0.3921 0.2292 -0.0476 0.0230  0.0264  380 ARG A CG  
3067 C CD  . ARG A 380 ? 0.3373 0.4385 0.2620 -0.0461 0.0235  0.0267  380 ARG A CD  
3068 N NE  . ARG A 380 ? 0.4109 0.5060 0.3229 -0.0539 0.0233  0.0363  380 ARG A NE  
3069 C CZ  . ARG A 380 ? 0.3664 0.4709 0.2757 -0.0604 0.0321  0.0421  380 ARG A CZ  
3070 N NH1 . ARG A 380 ? 0.3633 0.4860 0.2840 -0.0593 0.0423  0.0392  380 ARG A NH1 
3071 N NH2 . ARG A 380 ? 0.3678 0.4641 0.2635 -0.0680 0.0310  0.0519  380 ARG A NH2 
3072 N N   . VAL A 381 ? 0.3168 0.4189 0.2963 -0.0436 0.0072  0.0171  381 VAL A N   
3073 C CA  . VAL A 381 ? 0.2573 0.3457 0.2371 -0.0485 0.0009  0.0189  381 VAL A CA  
3074 C C   . VAL A 381 ? 0.3197 0.4169 0.3114 -0.0548 -0.0003 0.0189  381 VAL A C   
3075 O O   . VAL A 381 ? 0.3574 0.4478 0.3491 -0.0643 -0.0032 0.0230  381 VAL A O   
3076 C CB  . VAL A 381 ? 0.3125 0.3874 0.2887 -0.0410 -0.0042 0.0142  381 VAL A CB  
3077 C CG1 . VAL A 381 ? 0.2836 0.3439 0.2598 -0.0441 -0.0090 0.0135  381 VAL A CG1 
3078 C CG2 . VAL A 381 ? 0.2638 0.3305 0.2298 -0.0373 -0.0054 0.0169  381 VAL A CG2 
3079 N N   . LEU A 382 ? 0.2659 0.3778 0.2678 -0.0503 0.0009  0.0149  382 LEU A N   
3080 C CA  . LEU A 382 ? 0.2777 0.3997 0.2916 -0.0563 -0.0025 0.0156  382 LEU A CA  
3081 C C   . LEU A 382 ? 0.3299 0.4704 0.3545 -0.0650 0.0016  0.0226  382 LEU A C   
3082 O O   . LEU A 382 ? 0.3209 0.4646 0.3524 -0.0757 -0.0031 0.0260  382 LEU A O   
3083 C CB  . LEU A 382 ? 0.2818 0.4148 0.3039 -0.0482 -0.0030 0.0110  382 LEU A CB  
3084 C CG  . LEU A 382 ? 0.2871 0.4055 0.3003 -0.0401 -0.0059 0.0049  382 LEU A CG  
3085 C CD1 . LEU A 382 ? 0.3690 0.4987 0.3901 -0.0327 -0.0055 0.0022  382 LEU A CD1 
3086 C CD2 . LEU A 382 ? 0.1988 0.3005 0.2050 -0.0448 -0.0125 0.0030  382 LEU A CD2 
3087 N N   . GLY A 383 ? 0.2212 0.3741 0.2467 -0.0612 0.0107  0.0249  383 GLY A N   
3088 C CA  . GLY A 383 ? 0.2101 0.3852 0.2480 -0.0679 0.0173  0.0318  383 GLY A CA  
3089 C C   . GLY A 383 ? 0.3415 0.5084 0.3692 -0.0778 0.0199  0.0388  383 GLY A C   
3090 O O   . GLY A 383 ? 0.3107 0.4776 0.3433 -0.0908 0.0162  0.0447  383 GLY A O   
3091 N N   . HIS A 384 ? 0.3292 0.4875 0.3411 -0.0727 0.0253  0.0385  384 HIS A N   
3092 C CA  . HIS A 384 ? 0.2942 0.4461 0.2948 -0.0817 0.0285  0.0466  384 HIS A CA  
3093 C C   . HIS A 384 ? 0.3375 0.4648 0.3304 -0.0902 0.0187  0.0499  384 HIS A C   
3094 O O   . HIS A 384 ? 0.3134 0.4394 0.3078 -0.1031 0.0184  0.0580  384 HIS A O   
3095 C CB  . HIS A 384 ? 0.2639 0.4091 0.2457 -0.0743 0.0339  0.0451  384 HIS A CB  
3096 C CG  . HIS A 384 ? 0.3857 0.5215 0.3520 -0.0829 0.0359  0.0542  384 HIS A CG  
3097 N ND1 . HIS A 384 ? 0.3715 0.5229 0.3409 -0.0921 0.0449  0.0626  384 HIS A ND1 
3098 C CD2 . HIS A 384 ? 0.3299 0.4432 0.2780 -0.0836 0.0300  0.0574  384 HIS A CD2 
3099 C CE1 . HIS A 384 ? 0.3401 0.4769 0.2916 -0.0989 0.0444  0.0706  384 HIS A CE1 
3100 N NE2 . HIS A 384 ? 0.3729 0.4862 0.3115 -0.0934 0.0348  0.0678  384 HIS A NE2 
3101 N N   . TYR A 385 ? 0.3067 0.4134 0.2914 -0.0831 0.0112  0.0441  385 TYR A N   
3102 C CA  . TYR A 385 ? 0.3333 0.4134 0.3082 -0.0883 0.0038  0.0470  385 TYR A CA  
3103 C C   . TYR A 385 ? 0.3352 0.4082 0.3175 -0.0959 -0.0029 0.0450  385 TYR A C   
3104 O O   . TYR A 385 ? 0.3806 0.4368 0.3577 -0.1065 -0.0067 0.0501  385 TYR A O   
3105 C CB  . TYR A 385 ? 0.3901 0.4525 0.3540 -0.0768 -0.0003 0.0428  385 TYR A CB  
3106 C CG  . TYR A 385 ? 0.3871 0.4486 0.3383 -0.0739 0.0028  0.0477  385 TYR A CG  
3107 C CD1 . TYR A 385 ? 0.4243 0.4760 0.3653 -0.0821 0.0032  0.0579  385 TYR A CD1 
3108 C CD2 . TYR A 385 ? 0.3127 0.3819 0.2602 -0.0643 0.0048  0.0426  385 TYR A CD2 
3109 C CE1 . TYR A 385 ? 0.4246 0.4755 0.3511 -0.0803 0.0052  0.0631  385 TYR A CE1 
3110 C CE2 . TYR A 385 ? 0.3793 0.4469 0.3122 -0.0631 0.0063  0.0467  385 TYR A CE2 
3111 C CZ  . TYR A 385 ? 0.4227 0.4817 0.3447 -0.0709 0.0064  0.0570  385 TYR A CZ  
3112 O OH  . TYR A 385 ? 0.4724 0.5297 0.3773 -0.0702 0.0071  0.0615  385 TYR A OH  
3113 N N   . SER A 386 ? 0.3664 0.4497 0.3586 -0.0916 -0.0052 0.0377  386 SER A N   
3114 C CA  . SER A 386 ? 0.3175 0.3925 0.3128 -0.0997 -0.0127 0.0352  386 SER A CA  
3115 C C   . SER A 386 ? 0.3371 0.4331 0.3471 -0.1138 -0.0127 0.0413  386 SER A C   
3116 O O   . SER A 386 ? 0.2970 0.3809 0.3042 -0.1280 -0.0174 0.0457  386 SER A O   
3117 C CB  . SER A 386 ? 0.3366 0.4132 0.3343 -0.0903 -0.0160 0.0260  386 SER A CB  
3118 O OG  . SER A 386 ? 0.3436 0.4095 0.3396 -0.0986 -0.0239 0.0229  386 SER A OG  
3119 N N   . ARG A 387 ? 0.3132 0.4407 0.3396 -0.1102 -0.0074 0.0422  387 ARG A N   
3120 C CA  . ARG A 387 ? 0.3093 0.4631 0.3545 -0.1224 -0.0067 0.0494  387 ARG A CA  
3121 C C   . ARG A 387 ? 0.4013 0.5577 0.4454 -0.1338 -0.0007 0.0595  387 ARG A C   
3122 O O   . ARG A 387 ? 0.3599 0.5110 0.4058 -0.1505 -0.0058 0.0655  387 ARG A O   
3123 C CB  . ARG A 387 ? 0.2871 0.4743 0.3514 -0.1127 -0.0006 0.0487  387 ARG A CB  
3124 C CG  . ARG A 387 ? 0.2369 0.4567 0.3265 -0.1238 -0.0013 0.0564  387 ARG A CG  
3125 C CD  . ARG A 387 ? 0.2800 0.5336 0.3893 -0.1112 0.0085  0.0574  387 ARG A CD  
3126 N NE  . ARG A 387 ? 0.2977 0.5493 0.3965 -0.1007 0.0216  0.0563  387 ARG A NE  
3127 C CZ  . ARG A 387 ? 0.2961 0.5457 0.3893 -0.0839 0.0271  0.0493  387 ARG A CZ  
3128 N NH1 . ARG A 387 ? 0.2482 0.4998 0.3477 -0.0743 0.0219  0.0437  387 ARG A NH1 
3129 N NH2 . ARG A 387 ? 0.2512 0.4953 0.3305 -0.0775 0.0376  0.0482  387 ARG A NH2 
3130 N N   . ASP A 388 ? 0.3768 0.5404 0.4161 -0.1260 0.0100  0.0619  388 ASP A N   
3131 C CA  . ASP A 388 ? 0.3781 0.5517 0.4181 -0.1365 0.0180  0.0727  388 ASP A CA  
3132 C C   . ASP A 388 ? 0.4253 0.5663 0.4454 -0.1458 0.0135  0.0778  388 ASP A C   
3133 O O   . ASP A 388 ? 0.4063 0.5469 0.4293 -0.1626 0.0127  0.0871  388 ASP A O   
3134 C CB  . ASP A 388 ? 0.3594 0.5503 0.3972 -0.1249 0.0315  0.0727  388 ASP A CB  
3135 C CG  . ASP A 388 ? 0.3609 0.5822 0.4189 -0.1145 0.0371  0.0683  388 ASP A CG  
3136 O OD1 . ASP A 388 ? 0.3373 0.5780 0.4170 -0.1212 0.0331  0.0709  388 ASP A OD1 
3137 O OD2 . ASP A 388 ? 0.4237 0.6485 0.4759 -0.1000 0.0446  0.0624  388 ASP A OD2 
3138 N N   . GLU A 389 ? 0.4334 0.5468 0.4343 -0.1356 0.0103  0.0730  389 GLU A N   
3139 C CA  . GLU A 389 ? 0.4322 0.5140 0.4151 -0.1424 0.0060  0.0790  389 GLU A CA  
3140 C C   . GLU A 389 ? 0.4394 0.4923 0.4178 -0.1478 -0.0053 0.0752  389 GLU A C   
3141 O O   . GLU A 389 ? 0.4228 0.4478 0.3885 -0.1557 -0.0092 0.0810  389 GLU A O   
3142 C CB  . GLU A 389 ? 0.4626 0.5299 0.4279 -0.1291 0.0076  0.0779  389 GLU A CB  
3143 C CG  . GLU A 389 ? 0.4883 0.5769 0.4502 -0.1247 0.0184  0.0810  389 GLU A CG  
3144 C CD  . GLU A 389 ? 0.5974 0.6912 0.5543 -0.1384 0.0249  0.0941  389 GLU A CD  
3145 O OE1 . GLU A 389 ? 0.6345 0.7038 0.5802 -0.1473 0.0197  0.1022  389 GLU A OE1 
3146 O OE2 . GLU A 389 ? 0.7399 0.8618 0.7041 -0.1400 0.0361  0.0966  389 GLU A OE2 
3147 N N   . GLN A 390 ? 0.4145 0.4710 0.4009 -0.1436 -0.0105 0.0656  390 GLN A N   
3148 C CA  . GLN A 390 ? 0.4505 0.4797 0.4301 -0.1498 -0.0204 0.0607  390 GLN A CA  
3149 C C   . GLN A 390 ? 0.3773 0.3689 0.3374 -0.1405 -0.0233 0.0578  390 GLN A C   
3150 O O   . GLN A 390 ? 0.3878 0.3479 0.3365 -0.1482 -0.0290 0.0584  390 GLN A O   
3151 C CB  . GLN A 390 ? 0.3755 0.4017 0.3587 -0.1719 -0.0245 0.0684  390 GLN A CB  
3152 C CG  . GLN A 390 ? 0.5043 0.5730 0.5115 -0.1810 -0.0214 0.0732  390 GLN A CG  
3153 C CD  . GLN A 390 ? 0.5912 0.6604 0.6052 -0.2049 -0.0274 0.0807  390 GLN A CD  
3154 O OE1 . GLN A 390 ? 0.8952 0.9693 0.9169 -0.2132 -0.0361 0.0766  390 GLN A OE1 
3155 N NE2 . GLN A 390 ? 0.6047 0.6700 0.6158 -0.2173 -0.0233 0.0924  390 GLN A NE2 
3156 N N   . LEU A 391 ? 0.3450 0.3398 0.3020 -0.1237 -0.0196 0.0546  391 LEU A N   
3157 C CA  . LEU A 391 ? 0.4433 0.4088 0.3867 -0.1122 -0.0222 0.0522  391 LEU A CA  
3158 C C   . LEU A 391 ? 0.4278 0.3742 0.3671 -0.1074 -0.0272 0.0416  391 LEU A C   
3159 O O   . LEU A 391 ? 0.4854 0.4010 0.4130 -0.1019 -0.0296 0.0401  391 LEU A O   
3160 C CB  . LEU A 391 ? 0.3437 0.3223 0.2875 -0.0971 -0.0182 0.0513  391 LEU A CB  
3161 C CG  . LEU A 391 ? 0.5498 0.5220 0.4840 -0.0955 -0.0166 0.0613  391 LEU A CG  
3162 C CD1 . LEU A 391 ? 0.5336 0.5202 0.4687 -0.1095 -0.0119 0.0708  391 LEU A CD1 
3163 C CD2 . LEU A 391 ? 0.4344 0.4195 0.3682 -0.0816 -0.0148 0.0586  391 LEU A CD2 
3164 N N   . PHE A 392 ? 0.4377 0.4017 0.3857 -0.1083 -0.0281 0.0344  392 PHE A N   
3165 C CA  . PHE A 392 ? 0.4412 0.3894 0.3831 -0.1046 -0.0322 0.0241  392 PHE A CA  
3166 C C   . PHE A 392 ? 0.3988 0.3718 0.3517 -0.1112 -0.0346 0.0204  392 PHE A C   
3167 O O   . PHE A 392 ? 0.3662 0.3707 0.3337 -0.1110 -0.0311 0.0242  392 PHE A O   
3168 C CB  . PHE A 392 ? 0.3686 0.3115 0.3071 -0.0859 -0.0293 0.0182  392 PHE A CB  
3169 C CG  . PHE A 392 ? 0.3946 0.3620 0.3421 -0.0764 -0.0245 0.0216  392 PHE A CG  
3170 C CD1 . PHE A 392 ? 0.3858 0.3839 0.3454 -0.0783 -0.0220 0.0217  392 PHE A CD1 
3171 C CD2 . PHE A 392 ? 0.4747 0.4334 0.4182 -0.0654 -0.0229 0.0245  392 PHE A CD2 
3172 C CE1 . PHE A 392 ? 0.3696 0.3857 0.3337 -0.0700 -0.0174 0.0235  392 PHE A CE1 
3173 C CE2 . PHE A 392 ? 0.3465 0.3258 0.2954 -0.0586 -0.0198 0.0271  392 PHE A CE2 
3174 C CZ  . PHE A 392 ? 0.4246 0.4307 0.3821 -0.0612 -0.0168 0.0258  392 PHE A CZ  
3175 N N   . PRO A 393 ? 0.4252 0.3844 0.3706 -0.1167 -0.0407 0.0133  393 PRO A N   
3176 C CA  . PRO A 393 ? 0.3336 0.3173 0.2894 -0.1221 -0.0447 0.0107  393 PRO A CA  
3177 C C   . PRO A 393 ? 0.3284 0.3341 0.2927 -0.1067 -0.0403 0.0071  393 PRO A C   
3178 O O   . PRO A 393 ? 0.3552 0.3534 0.3146 -0.0927 -0.0354 0.0042  393 PRO A O   
3179 C CB  . PRO A 393 ? 0.4069 0.3632 0.3454 -0.1294 -0.0524 0.0025  393 PRO A CB  
3180 C CG  . PRO A 393 ? 0.4727 0.3921 0.3926 -0.1196 -0.0491 -0.0023 393 PRO A CG  
3181 C CD  . PRO A 393 ? 0.4617 0.3807 0.3870 -0.1171 -0.0440 0.0070  393 PRO A CD  
3182 N N   . LEU A 394 ? 0.2895 0.3234 0.2679 -0.1099 -0.0425 0.0082  394 LEU A N   
3183 C CA  . LEU A 394 ? 0.2823 0.3363 0.2694 -0.0961 -0.0383 0.0061  394 LEU A CA  
3184 C C   . LEU A 394 ? 0.3359 0.3733 0.3096 -0.0864 -0.0393 -0.0026 394 LEU A C   
3185 O O   . LEU A 394 ? 0.2877 0.3314 0.2636 -0.0736 -0.0342 -0.0045 394 LEU A O   
3186 C CB  . LEU A 394 ? 0.3127 0.3989 0.3185 -0.1006 -0.0409 0.0101  394 LEU A CB  
3187 C CG  . LEU A 394 ? 0.3068 0.4138 0.3233 -0.0865 -0.0356 0.0094  394 LEU A CG  
3188 C CD1 . LEU A 394 ? 0.2416 0.3529 0.2606 -0.0786 -0.0260 0.0120  394 LEU A CD1 
3189 C CD2 . LEU A 394 ? 0.2383 0.3756 0.2743 -0.0898 -0.0388 0.0141  394 LEU A CD2 
3190 N N   . THR A 395 ? 0.3307 0.3464 0.2892 -0.0930 -0.0452 -0.0080 395 THR A N   
3191 C CA  . THR A 395 ? 0.3630 0.3619 0.3066 -0.0835 -0.0441 -0.0163 395 THR A CA  
3192 C C   . THR A 395 ? 0.4126 0.3957 0.3509 -0.0712 -0.0365 -0.0177 395 THR A C   
3193 O O   . THR A 395 ? 0.3985 0.3841 0.3362 -0.0592 -0.0320 -0.0209 395 THR A O   
3194 C CB  . THR A 395 ? 0.3595 0.3341 0.2835 -0.0934 -0.0510 -0.0227 395 THR A CB  
3195 O OG1 . THR A 395 ? 0.3734 0.3246 0.2891 -0.1026 -0.0527 -0.0218 395 THR A OG1 
3196 C CG2 . THR A 395 ? 0.3232 0.3164 0.2520 -0.1051 -0.0607 -0.0213 395 THR A CG2 
3197 N N   . THR A 396 ? 0.3435 0.3115 0.2790 -0.0744 -0.0356 -0.0142 396 THR A N   
3198 C CA  . THR A 396 ? 0.3537 0.3099 0.2870 -0.0623 -0.0297 -0.0135 396 THR A CA  
3199 C C   . THR A 396 ? 0.2930 0.2743 0.2406 -0.0543 -0.0255 -0.0087 396 THR A C   
3200 O O   . THR A 396 ? 0.3291 0.3113 0.2777 -0.0424 -0.0217 -0.0103 396 THR A O   
3201 C CB  . THR A 396 ? 0.3865 0.3201 0.3131 -0.0681 -0.0308 -0.0091 396 THR A CB  
3202 O OG1 . THR A 396 ? 0.4060 0.3102 0.3157 -0.0748 -0.0345 -0.0152 396 THR A OG1 
3203 C CG2 . THR A 396 ? 0.3324 0.2573 0.2592 -0.0549 -0.0261 -0.0061 396 THR A CG2 
3204 N N   . ALA A 397 ? 0.3151 0.3171 0.2737 -0.0610 -0.0259 -0.0029 397 ALA A N   
3205 C CA  . ALA A 397 ? 0.3148 0.3377 0.2834 -0.0540 -0.0215 0.0004  397 ALA A CA  
3206 C C   . ALA A 397 ? 0.3743 0.4076 0.3462 -0.0448 -0.0201 -0.0047 397 ALA A C   
3207 O O   . ALA A 397 ? 0.3036 0.3397 0.2767 -0.0359 -0.0170 -0.0048 397 ALA A O   
3208 C CB  . ALA A 397 ? 0.2812 0.3254 0.2605 -0.0621 -0.0206 0.0061  397 ALA A CB  
3209 N N   . VAL A 398 ? 0.2803 0.3193 0.2531 -0.0478 -0.0231 -0.0081 398 VAL A N   
3210 C CA  . VAL A 398 ? 0.2329 0.2798 0.2073 -0.0400 -0.0220 -0.0118 398 VAL A CA  
3211 C C   . VAL A 398 ? 0.3239 0.3543 0.2886 -0.0324 -0.0197 -0.0162 398 VAL A C   
3212 O O   . VAL A 398 ? 0.2797 0.3161 0.2475 -0.0243 -0.0165 -0.0170 398 VAL A O   
3213 C CB  . VAL A 398 ? 0.3620 0.4175 0.3379 -0.0455 -0.0270 -0.0129 398 VAL A CB  
3214 C CG1 . VAL A 398 ? 0.2622 0.3190 0.2345 -0.0381 -0.0264 -0.0166 398 VAL A CG1 
3215 C CG2 . VAL A 398 ? 0.3032 0.3818 0.2945 -0.0495 -0.0277 -0.0074 398 VAL A CG2 
3216 N N   . HIS A 399 ? 0.3279 0.3373 0.2810 -0.0350 -0.0209 -0.0193 399 HIS A N   
3217 C CA  . HIS A 399 ? 0.3379 0.3322 0.2831 -0.0259 -0.0168 -0.0234 399 HIS A CA  
3218 C C   . HIS A 399 ? 0.3487 0.3500 0.3031 -0.0168 -0.0129 -0.0195 399 HIS A C   
3219 O O   . HIS A 399 ? 0.3166 0.3230 0.2738 -0.0088 -0.0093 -0.0209 399 HIS A O   
3220 C CB  . HIS A 399 ? 0.2893 0.2563 0.2207 -0.0290 -0.0176 -0.0265 399 HIS A CB  
3221 C CG  . HIS A 399 ? 0.3861 0.3368 0.3098 -0.0179 -0.0118 -0.0310 399 HIS A CG  
3222 N ND1 . HIS A 399 ? 0.4581 0.4111 0.3768 -0.0121 -0.0077 -0.0362 399 HIS A ND1 
3223 C CD2 . HIS A 399 ? 0.3425 0.2745 0.2632 -0.0110 -0.0086 -0.0304 399 HIS A CD2 
3224 C CE1 . HIS A 399 ? 0.3640 0.3024 0.2779 -0.0018 -0.0012 -0.0390 399 HIS A CE1 
3225 N NE2 . HIS A 399 ? 0.4222 0.3473 0.3378 -0.0002 -0.0018 -0.0357 399 HIS A NE2 
3226 N N   . LYS A 400 ? 0.3140 0.3166 0.2728 -0.0192 -0.0141 -0.0138 400 LYS A N   
3227 C CA  . LYS A 400 ? 0.3198 0.3266 0.2847 -0.0121 -0.0125 -0.0092 400 LYS A CA  
3228 C C   . LYS A 400 ? 0.3184 0.3455 0.2917 -0.0092 -0.0116 -0.0084 400 LYS A C   
3229 O O   . LYS A 400 ? 0.3527 0.3847 0.3305 -0.0044 -0.0116 -0.0049 400 LYS A O   
3230 C CB  . LYS A 400 ? 0.3014 0.3034 0.2652 -0.0171 -0.0146 -0.0027 400 LYS A CB  
3231 C CG  . LYS A 400 ? 0.3429 0.3199 0.2980 -0.0182 -0.0155 -0.0021 400 LYS A CG  
3232 C CD  . LYS A 400 ? 0.3198 0.2926 0.2728 -0.0265 -0.0179 0.0053  400 LYS A CD  
3233 C CE  . LYS A 400 ? 0.4240 0.3686 0.3684 -0.0254 -0.0191 0.0078  400 LYS A CE  
3234 N NZ  . LYS A 400 ? 0.4873 0.4281 0.4351 -0.0122 -0.0180 0.0112  400 LYS A NZ  
3235 N N   . MET A 401 ? 0.2924 0.3304 0.2676 -0.0122 -0.0117 -0.0110 401 MET A N   
3236 C CA  . MET A 401 ? 0.2943 0.3467 0.2754 -0.0093 -0.0108 -0.0109 401 MET A CA  
3237 C C   . MET A 401 ? 0.3416 0.3968 0.3225 -0.0072 -0.0097 -0.0147 401 MET A C   
3238 O O   . MET A 401 ? 0.2606 0.3253 0.2453 -0.0061 -0.0093 -0.0147 401 MET A O   
3239 C CB  . MET A 401 ? 0.2463 0.3093 0.2301 -0.0136 -0.0110 -0.0089 401 MET A CB  
3240 C CG  . MET A 401 ? 0.2975 0.3645 0.2827 -0.0193 -0.0121 -0.0095 401 MET A CG  
3241 S SD  . MET A 401 ? 0.3341 0.4168 0.3258 -0.0223 -0.0097 -0.0063 401 MET A SD  
3242 C CE  . MET A 401 ? 0.2698 0.3467 0.2569 -0.0274 -0.0090 -0.0012 401 MET A CE  
3243 N N   . THR A 402 ? 0.2855 0.3305 0.2598 -0.0067 -0.0090 -0.0180 402 THR A N   
3244 C CA  . THR A 402 ? 0.3029 0.3495 0.2736 -0.0054 -0.0078 -0.0210 402 THR A CA  
3245 C C   . THR A 402 ? 0.2968 0.3323 0.2606 -0.0006 -0.0035 -0.0242 402 THR A C   
3246 O O   . THR A 402 ? 0.3404 0.3806 0.3097 0.0054  0.0005  -0.0230 402 THR A O   
3247 C CB  . THR A 402 ? 0.2791 0.3267 0.2453 -0.0118 -0.0119 -0.0222 402 THR A CB  
3248 O OG1 . THR A 402 ? 0.2984 0.3337 0.2573 -0.0171 -0.0143 -0.0239 402 THR A OG1 
3249 C CG2 . THR A 402 ? 0.2606 0.3224 0.2365 -0.0140 -0.0141 -0.0188 402 THR A CG2 
3250 N N   . GLY A 403 ? 0.3230 0.3439 0.2742 -0.0034 -0.0041 -0.0284 403 GLY A N   
3251 C CA  . GLY A 403 ? 0.3329 0.3413 0.2740 0.0021  0.0017  -0.0329 403 GLY A CA  
3252 C C   . GLY A 403 ? 0.3619 0.3657 0.3096 0.0110  0.0067  -0.0314 403 GLY A C   
3253 O O   . GLY A 403 ? 0.3346 0.3404 0.2841 0.0188  0.0136  -0.0323 403 GLY A O   
3254 N N   . LEU A 404 ? 0.3951 0.3939 0.3471 0.0099  0.0034  -0.0282 404 LEU A N   
3255 C CA  . LEU A 404 ? 0.3820 0.3772 0.3416 0.0188  0.0064  -0.0249 404 LEU A CA  
3256 C C   . LEU A 404 ? 0.3125 0.3294 0.2882 0.0239  0.0079  -0.0200 404 LEU A C   
3257 O O   . LEU A 404 ? 0.3555 0.3758 0.3388 0.0332  0.0132  -0.0186 404 LEU A O   
3258 C CB  . LEU A 404 ? 0.3104 0.2977 0.2708 0.0150  0.0012  -0.0205 404 LEU A CB  
3259 C CG  . LEU A 404 ? 0.3734 0.3558 0.3413 0.0239  0.0022  -0.0150 404 LEU A CG  
3260 C CD1 . LEU A 404 ? 0.3494 0.3123 0.3110 0.0339  0.0088  -0.0193 404 LEU A CD1 
3261 C CD2 . LEU A 404 ? 0.3564 0.3306 0.3224 0.0182  -0.0035 -0.0093 404 LEU A CD2 
3262 N N   . SER A 405 ? 0.2450 0.2767 0.2263 0.0178  0.0034  -0.0172 405 SER A N   
3263 C CA  . SER A 405 ? 0.3054 0.3551 0.2997 0.0198  0.0029  -0.0127 405 SER A CA  
3264 C C   . SER A 405 ? 0.3165 0.3747 0.3136 0.0225  0.0083  -0.0144 405 SER A C   
3265 O O   . SER A 405 ? 0.3441 0.4137 0.3533 0.0274  0.0109  -0.0107 405 SER A O   
3266 C CB  . SER A 405 ? 0.2966 0.3546 0.2918 0.0124  -0.0025 -0.0110 405 SER A CB  
3267 O OG  . SER A 405 ? 0.3547 0.4055 0.3457 0.0090  -0.0059 -0.0093 405 SER A OG  
3268 N N   . ALA A 406 ? 0.2962 0.3502 0.2828 0.0186  0.0096  -0.0187 406 ALA A N   
3269 C CA  . ALA A 406 ? 0.2865 0.3471 0.2728 0.0203  0.0152  -0.0195 406 ALA A CA  
3270 C C   . ALA A 406 ? 0.3517 0.4086 0.3383 0.0291  0.0238  -0.0210 406 ALA A C   
3271 O O   . ALA A 406 ? 0.3364 0.4065 0.3329 0.0329  0.0295  -0.0181 406 ALA A O   
3272 C CB  . ALA A 406 ? 0.2645 0.3190 0.2366 0.0147  0.0140  -0.0231 406 ALA A CB  
3273 N N   . ALA A 407 ? 0.3559 0.3946 0.3321 0.0326  0.0255  -0.0253 407 ALA A N   
3274 C CA  . ALA A 407 ? 0.4124 0.4451 0.3884 0.0433  0.0351  -0.0273 407 ALA A CA  
3275 C C   . ALA A 407 ? 0.3683 0.4161 0.3668 0.0514  0.0363  -0.0201 407 ALA A C   
3276 O O   . ALA A 407 ? 0.3997 0.4609 0.4096 0.0586  0.0443  -0.0178 407 ALA A O   
3277 C CB  . ALA A 407 ? 0.3642 0.3693 0.3223 0.0449  0.0359  -0.0339 407 ALA A CB  
3278 N N   . ARG A 408 ? 0.3401 0.3881 0.3460 0.0496  0.0281  -0.0155 408 ARG A N   
3279 C CA  . ARG A 408 ? 0.2961 0.3573 0.3221 0.0573  0.0272  -0.0077 408 ARG A CA  
3280 C C   . ARG A 408 ? 0.3788 0.4676 0.4228 0.0552  0.0266  -0.0019 408 ARG A C   
3281 O O   . ARG A 408 ? 0.3404 0.4449 0.4033 0.0629  0.0291  0.0043  408 ARG A O   
3282 C CB  . ARG A 408 ? 0.3763 0.4320 0.4030 0.0538  0.0174  -0.0032 408 ARG A CB  
3283 C CG  . ARG A 408 ? 0.4916 0.5206 0.5053 0.0568  0.0175  -0.0060 408 ARG A CG  
3284 C CD  . ARG A 408 ? 0.4504 0.4716 0.4713 0.0718  0.0239  -0.0040 408 ARG A CD  
3285 N NE  . ARG A 408 ? 0.5362 0.5253 0.5394 0.0734  0.0252  -0.0091 408 ARG A NE  
3286 C CZ  . ARG A 408 ? 0.5878 0.5597 0.5921 0.0855  0.0289  -0.0075 408 ARG A CZ  
3287 N NH1 . ARG A 408 ? 0.5225 0.5092 0.5476 0.0989  0.0318  -0.0002 408 ARG A NH1 
3288 N NH2 . ARG A 408 ? 0.5454 0.4842 0.5300 0.0842  0.0293  -0.0130 408 ARG A NH2 
3289 N N   . PHE A 409 ? 0.2944 0.3895 0.3338 0.0446  0.0228  -0.0030 409 PHE A N   
3290 C CA  . PHE A 409 ? 0.3207 0.4380 0.3747 0.0401  0.0211  0.0024  409 PHE A CA  
3291 C C   . PHE A 409 ? 0.3249 0.4483 0.3770 0.0392  0.0296  0.0005  409 PHE A C   
3292 O O   . PHE A 409 ? 0.2732 0.4131 0.3357 0.0335  0.0285  0.0050  409 PHE A O   
3293 C CB  . PHE A 409 ? 0.2502 0.3684 0.3004 0.0293  0.0109  0.0033  409 PHE A CB  
3294 C CG  . PHE A 409 ? 0.2905 0.4096 0.3455 0.0294  0.0027  0.0078  409 PHE A CG  
3295 C CD1 . PHE A 409 ? 0.2228 0.3253 0.2659 0.0297  0.0000  0.0056  409 PHE A CD1 
3296 C CD2 . PHE A 409 ? 0.2488 0.3859 0.3197 0.0283  -0.0027 0.0150  409 PHE A CD2 
3297 C CE1 . PHE A 409 ? 0.2439 0.3464 0.2892 0.0294  -0.0072 0.0107  409 PHE A CE1 
3298 C CE2 . PHE A 409 ? 0.2745 0.4119 0.3472 0.0280  -0.0112 0.0199  409 PHE A CE2 
3299 C CZ  . PHE A 409 ? 0.1942 0.3136 0.2531 0.0289  -0.0129 0.0178  409 PHE A CZ  
3300 N N   . GLN A 410 ? 0.3725 0.4817 0.4099 0.0437  0.0378  -0.0057 410 GLN A N   
3301 C CA  . GLN A 410 ? 0.2852 0.3992 0.3179 0.0438  0.0474  -0.0071 410 GLN A CA  
3302 C C   . GLN A 410 ? 0.2714 0.3889 0.2983 0.0323  0.0427  -0.0059 410 GLN A C   
3303 O O   . GLN A 410 ? 0.3080 0.4402 0.3429 0.0290  0.0466  -0.0014 410 GLN A O   
3304 C CB  . GLN A 410 ? 0.3187 0.4545 0.3728 0.0513  0.0562  -0.0012 410 GLN A CB  
3305 C CG  . GLN A 410 ? 0.3588 0.4898 0.4180 0.0660  0.0642  -0.0025 410 GLN A CG  
3306 C CD  . GLN A 410 ? 0.4848 0.6401 0.5656 0.0745  0.0757  0.0032  410 GLN A CD  
3307 O OE1 . GLN A 410 ? 0.5422 0.7005 0.6161 0.0758  0.0876  0.0010  410 GLN A OE1 
3308 N NE2 . GLN A 410 ? 0.2791 0.4539 0.3868 0.0798  0.0720  0.0116  410 GLN A NE2 
3309 N N   . LEU A 411 ? 0.3285 0.4325 0.3422 0.0263  0.0347  -0.0094 411 LEU A N   
3310 C CA  . LEU A 411 ? 0.3368 0.4397 0.3426 0.0176  0.0307  -0.0088 411 LEU A CA  
3311 C C   . LEU A 411 ? 0.3549 0.4472 0.3414 0.0174  0.0360  -0.0128 411 LEU A C   
3312 O O   . LEU A 411 ? 0.4643 0.5418 0.4364 0.0190  0.0353  -0.0185 411 LEU A O   
3313 C CB  . LEU A 411 ? 0.2832 0.3787 0.2854 0.0128  0.0206  -0.0101 411 LEU A CB  
3314 C CG  . LEU A 411 ? 0.2889 0.3927 0.3047 0.0111  0.0144  -0.0066 411 LEU A CG  
3315 C CD1 . LEU A 411 ? 0.2954 0.3915 0.3046 0.0066  0.0071  -0.0085 411 LEU A CD1 
3316 C CD2 . LEU A 411 ? 0.2119 0.3301 0.2400 0.0070  0.0145  -0.0012 411 LEU A CD2 
3317 N N   . ALA A 412 ? 0.3614 0.4606 0.3462 0.0142  0.0406  -0.0094 412 ALA A N   
3318 C CA  . ALA A 412 ? 0.3611 0.4514 0.3255 0.0137  0.0463  -0.0121 412 ALA A CA  
3319 C C   . ALA A 412 ? 0.3263 0.4041 0.2751 0.0079  0.0371  -0.0138 412 ALA A C   
3320 O O   . ALA A 412 ? 0.3104 0.3909 0.2641 0.0027  0.0302  -0.0097 412 ALA A O   
3321 C CB  . ALA A 412 ? 0.3773 0.4798 0.3451 0.0110  0.0540  -0.0060 412 ALA A CB  
3322 N N   . ASP A 413 ? 0.3450 0.4086 0.2753 0.0088  0.0366  -0.0199 413 ASP A N   
3323 C CA  . ASP A 413 ? 0.3299 0.3846 0.2448 0.0030  0.0282  -0.0205 413 ASP A CA  
3324 C C   . ASP A 413 ? 0.3515 0.4083 0.2777 0.0003  0.0175  -0.0190 413 ASP A C   
3325 O O   . ASP A 413 ? 0.3510 0.4078 0.2741 -0.0036 0.0106  -0.0158 413 ASP A O   
3326 C CB  . ASP A 413 ? 0.3059 0.3636 0.2123 -0.0012 0.0294  -0.0148 413 ASP A CB  
3327 C CG  . ASP A 413 ? 0.4368 0.4905 0.3249 0.0003  0.0402  -0.0167 413 ASP A CG  
3328 O OD1 . ASP A 413 ? 0.4666 0.5131 0.3469 0.0053  0.0468  -0.0237 413 ASP A OD1 
3329 O OD2 . ASP A 413 ? 0.4179 0.4743 0.2979 -0.0035 0.0427  -0.0110 413 ASP A OD2 
3330 N N   . ARG A 414 ? 0.2982 0.3567 0.2370 0.0030  0.0164  -0.0207 414 ARG A N   
3331 C CA  . ARG A 414 ? 0.3387 0.3996 0.2870 0.0008  0.0083  -0.0196 414 ARG A CA  
3332 C C   . ARG A 414 ? 0.3012 0.3552 0.2490 0.0017  0.0065  -0.0237 414 ARG A C   
3333 O O   . ARG A 414 ? 0.3992 0.4455 0.3413 0.0051  0.0116  -0.0273 414 ARG A O   
3334 C CB  . ARG A 414 ? 0.2728 0.3435 0.2371 0.0012  0.0081  -0.0155 414 ARG A CB  
3335 C CG  . ARG A 414 ? 0.3734 0.4472 0.3367 -0.0014 0.0088  -0.0110 414 ARG A CG  
3336 C CD  . ARG A 414 ? 0.3045 0.3834 0.2797 -0.0032 0.0065  -0.0076 414 ARG A CD  
3337 N NE  . ARG A 414 ? 0.3048 0.3841 0.2780 -0.0066 0.0080  -0.0029 414 ARG A NE  
3338 C CZ  . ARG A 414 ? 0.3230 0.3960 0.2913 -0.0086 0.0039  -0.0001 414 ARG A CZ  
3339 N NH1 . ARG A 414 ? 0.2781 0.3469 0.2451 -0.0067 -0.0016 -0.0017 414 ARG A NH1 
3340 N NH2 . ARG A 414 ? 0.2474 0.3188 0.2132 -0.0123 0.0056  0.0051  414 ARG A NH2 
3341 N N   . GLY A 415 ? 0.2741 0.3298 0.2269 -0.0014 -0.0001 -0.0229 415 GLY A N   
3342 C CA  . GLY A 415 ? 0.2954 0.3452 0.2488 -0.0022 -0.0021 -0.0252 415 GLY A CA  
3343 C C   . GLY A 415 ? 0.3926 0.4313 0.3323 -0.0070 -0.0057 -0.0289 415 GLY A C   
3344 O O   . GLY A 415 ? 0.3075 0.3389 0.2467 -0.0092 -0.0076 -0.0304 415 GLY A O   
3345 N N   . LEU A 416 ? 0.3295 0.3658 0.2569 -0.0098 -0.0074 -0.0298 416 LEU A N   
3346 C CA  . LEU A 416 ? 0.2807 0.3066 0.1929 -0.0163 -0.0128 -0.0334 416 LEU A CA  
3347 C C   . LEU A 416 ? 0.3845 0.4193 0.2949 -0.0209 -0.0202 -0.0295 416 LEU A C   
3348 O O   . LEU A 416 ? 0.3384 0.3787 0.2483 -0.0180 -0.0182 -0.0264 416 LEU A O   
3349 C CB  . LEU A 416 ? 0.3356 0.3442 0.2272 -0.0148 -0.0071 -0.0398 416 LEU A CB  
3350 C CG  . LEU A 416 ? 0.4580 0.4548 0.3493 -0.0079 0.0012  -0.0439 416 LEU A CG  
3351 C CD1 . LEU A 416 ? 0.3271 0.3077 0.1958 -0.0048 0.0089  -0.0506 416 LEU A CD1 
3352 C CD2 . LEU A 416 ? 0.3069 0.2936 0.2002 -0.0116 -0.0033 -0.0453 416 LEU A CD2 
3353 N N   . VAL A 417 ? 0.3636 0.4007 0.2743 -0.0282 -0.0291 -0.0286 417 VAL A N   
3354 C CA  . VAL A 417 ? 0.3511 0.3950 0.2568 -0.0332 -0.0378 -0.0250 417 VAL A CA  
3355 C C   . VAL A 417 ? 0.3907 0.4179 0.2688 -0.0374 -0.0384 -0.0304 417 VAL A C   
3356 O O   . VAL A 417 ? 0.4163 0.4314 0.2813 -0.0449 -0.0431 -0.0352 417 VAL A O   
3357 C CB  . VAL A 417 ? 0.3653 0.4211 0.2833 -0.0401 -0.0474 -0.0213 417 VAL A CB  
3358 C CG1 . VAL A 417 ? 0.3436 0.4090 0.2585 -0.0442 -0.0575 -0.0160 417 VAL A CG1 
3359 C CG2 . VAL A 417 ? 0.2683 0.3389 0.2105 -0.0351 -0.0442 -0.0171 417 VAL A CG2 
3360 N N   . LYS A 418 ? 0.3977 0.4226 0.2651 -0.0333 -0.0334 -0.0297 418 LYS A N   
3361 C CA  . LYS A 418 ? 0.4452 0.4531 0.2839 -0.0356 -0.0305 -0.0356 418 LYS A CA  
3362 C C   . LYS A 418 ? 0.3307 0.3432 0.1593 -0.0350 -0.0309 -0.0303 418 LYS A C   
3363 O O   . LYS A 418 ? 0.3627 0.3854 0.2051 -0.0291 -0.0259 -0.0247 418 LYS A O   
3364 C CB  . LYS A 418 ? 0.4052 0.4006 0.2395 -0.0285 -0.0171 -0.0424 418 LYS A CB  
3365 C CG  . LYS A 418 ? 0.4136 0.3911 0.2176 -0.0286 -0.0107 -0.0492 418 LYS A CG  
3366 C CD  . LYS A 418 ? 0.5439 0.5102 0.3466 -0.0196 0.0032  -0.0556 418 LYS A CD  
3367 C CE  . LYS A 418 ? 0.6279 0.5707 0.3960 -0.0203 0.0091  -0.0651 418 LYS A CE  
3368 N NZ  . LYS A 418 ? 0.6931 0.6282 0.4614 -0.0086 0.0254  -0.0701 418 LYS A NZ  
3369 N N   . ILE A 419 ? 0.4458 0.4495 0.2487 -0.0421 -0.0374 -0.0317 419 ILE A N   
3370 C CA  . ILE A 419 ? 0.4610 0.4672 0.2507 -0.0422 -0.0380 -0.0256 419 ILE A CA  
3371 C C   . ILE A 419 ? 0.4448 0.4480 0.2316 -0.0346 -0.0221 -0.0267 419 ILE A C   
3372 O O   . ILE A 419 ? 0.4692 0.4601 0.2438 -0.0318 -0.0114 -0.0350 419 ILE A O   
3373 C CB  . ILE A 419 ? 0.4847 0.4783 0.2409 -0.0517 -0.0464 -0.0285 419 ILE A CB  
3374 C CG1 . ILE A 419 ? 0.4545 0.4549 0.2172 -0.0608 -0.0636 -0.0261 419 ILE A CG1 
3375 C CG2 . ILE A 419 ? 0.4149 0.4100 0.1542 -0.0520 -0.0467 -0.0211 419 ILE A CG2 
3376 C CD1 . ILE A 419 ? 0.4411 0.4256 0.1683 -0.0727 -0.0733 -0.0313 419 ILE A CD1 
3377 N N   . GLY A 420 ? 0.3969 0.4116 0.1962 -0.0312 -0.0204 -0.0177 420 GLY A N   
3378 C CA  . GLY A 420 ? 0.3973 0.4131 0.1977 -0.0259 -0.0065 -0.0165 420 GLY A CA  
3379 C C   . GLY A 420 ? 0.4327 0.4585 0.2627 -0.0197 -0.0003 -0.0158 420 GLY A C   
3380 O O   . GLY A 420 ? 0.4176 0.4487 0.2541 -0.0168 0.0087  -0.0121 420 GLY A O   
3381 N N   . TYR A 421 ? 0.3209 0.3496 0.1679 -0.0186 -0.0051 -0.0187 421 TYR A N   
3382 C CA  . TYR A 421 ? 0.3432 0.3812 0.2158 -0.0137 -0.0012 -0.0171 421 TYR A CA  
3383 C C   . TYR A 421 ? 0.3803 0.4274 0.2678 -0.0139 -0.0076 -0.0092 421 TYR A C   
3384 O O   . TYR A 421 ? 0.3719 0.4195 0.2541 -0.0165 -0.0162 -0.0047 421 TYR A O   
3385 C CB  . TYR A 421 ? 0.3604 0.3969 0.2433 -0.0126 -0.0028 -0.0226 421 TYR A CB  
3386 C CG  . TYR A 421 ? 0.3961 0.4237 0.2726 -0.0087 0.0067  -0.0295 421 TYR A CG  
3387 C CD1 . TYR A 421 ? 0.4483 0.4655 0.3025 -0.0081 0.0140  -0.0336 421 TYR A CD1 
3388 C CD2 . TYR A 421 ? 0.3655 0.3944 0.2575 -0.0047 0.0090  -0.0316 421 TYR A CD2 
3389 C CE1 . TYR A 421 ? 0.4200 0.4283 0.2695 -0.0021 0.0243  -0.0402 421 TYR A CE1 
3390 C CE2 . TYR A 421 ? 0.4006 0.4209 0.2887 0.0008  0.0176  -0.0368 421 TYR A CE2 
3391 C CZ  . TYR A 421 ? 0.4526 0.4626 0.3205 0.0028  0.0257  -0.0414 421 TYR A CZ  
3392 O OH  . TYR A 421 ? 0.5083 0.5090 0.3735 0.0103  0.0353  -0.0468 421 TYR A OH  
3393 N N   . PHE A 422 ? 0.3274 0.3807 0.2330 -0.0106 -0.0036 -0.0074 422 PHE A N   
3394 C CA  . PHE A 422 ? 0.3057 0.3635 0.2242 -0.0099 -0.0083 -0.0016 422 PHE A CA  
3395 C C   . PHE A 422 ? 0.3403 0.4017 0.2678 -0.0092 -0.0165 -0.0021 422 PHE A C   
3396 O O   . PHE A 422 ? 0.3495 0.4122 0.2807 -0.0095 -0.0171 -0.0070 422 PHE A O   
3397 C CB  . PHE A 422 ? 0.3131 0.3748 0.2466 -0.0081 -0.0028 -0.0012 422 PHE A CB  
3398 C CG  . PHE A 422 ? 0.3106 0.3729 0.2409 -0.0099 0.0042  0.0026  422 PHE A CG  
3399 C CD1 . PHE A 422 ? 0.2992 0.3578 0.2242 -0.0126 0.0025  0.0096  422 PHE A CD1 
3400 C CD2 . PHE A 422 ? 0.3065 0.3739 0.2408 -0.0089 0.0126  0.0002  422 PHE A CD2 
3401 C CE1 . PHE A 422 ? 0.2798 0.3398 0.2025 -0.0160 0.0095  0.0143  422 PHE A CE1 
3402 C CE2 . PHE A 422 ? 0.2568 0.3288 0.1913 -0.0111 0.0199  0.0047  422 PHE A CE2 
3403 C CZ  . PHE A 422 ? 0.2691 0.3375 0.1975 -0.0155 0.0185  0.0117  422 PHE A CZ  
3404 N N   . ALA A 423 ? 0.2677 0.3311 0.2001 -0.0078 -0.0223 0.0038  423 ALA A N   
3405 C CA  . ALA A 423 ? 0.3284 0.3989 0.2723 -0.0059 -0.0291 0.0049  423 ALA A CA  
3406 C C   . ALA A 423 ? 0.2992 0.3728 0.2592 -0.0018 -0.0257 0.0030  423 ALA A C   
3407 O O   . ALA A 423 ? 0.3220 0.3962 0.2905 0.0026  -0.0271 0.0064  423 ALA A O   
3408 C CB  . ALA A 423 ? 0.2488 0.3209 0.1915 -0.0044 -0.0365 0.0127  423 ALA A CB  
3409 N N   . ASP A 424 ? 0.2692 0.3431 0.2317 -0.0030 -0.0212 -0.0025 424 ASP A N   
3410 C CA  . ASP A 424 ? 0.2868 0.3646 0.2613 -0.0007 -0.0194 -0.0050 424 ASP A CA  
3411 C C   . ASP A 424 ? 0.3181 0.4030 0.2967 -0.0027 -0.0229 -0.0062 424 ASP A C   
3412 O O   . ASP A 424 ? 0.2962 0.3783 0.2681 -0.0066 -0.0230 -0.0093 424 ASP A O   
3413 C CB  . ASP A 424 ? 0.3159 0.3910 0.2909 -0.0014 -0.0139 -0.0085 424 ASP A CB  
3414 C CG  . ASP A 424 ? 0.3488 0.4197 0.3224 -0.0016 -0.0109 -0.0066 424 ASP A CG  
3415 O OD1 . ASP A 424 ? 0.4736 0.5407 0.4455 -0.0008 -0.0126 -0.0029 424 ASP A OD1 
3416 O OD2 . ASP A 424 ? 0.3437 0.4153 0.3188 -0.0026 -0.0071 -0.0081 424 ASP A OD2 
3417 N N   . LEU A 425 ? 0.2875 0.3809 0.2772 0.0001  -0.0250 -0.0038 425 LEU A N   
3418 C CA  . LEU A 425 ? 0.2927 0.3965 0.2886 -0.0032 -0.0294 -0.0028 425 LEU A CA  
3419 C C   . LEU A 425 ? 0.3124 0.4265 0.3228 0.0004  -0.0264 -0.0019 425 LEU A C   
3420 O O   . LEU A 425 ? 0.3054 0.4190 0.3208 0.0071  -0.0231 -0.0011 425 LEU A O   
3421 C CB  . LEU A 425 ? 0.2171 0.3265 0.2120 -0.0043 -0.0373 0.0024  425 LEU A CB  
3422 C CG  . LEU A 425 ? 0.3015 0.4011 0.2780 -0.0094 -0.0406 0.0014  425 LEU A CG  
3423 C CD1 . LEU A 425 ? 0.2086 0.3141 0.1837 -0.0097 -0.0494 0.0082  425 LEU A CD1 
3424 C CD2 . LEU A 425 ? 0.2371 0.3321 0.2049 -0.0170 -0.0416 -0.0037 425 LEU A CD2 
3425 N N   . VAL A 426 ? 0.2608 0.3827 0.2764 -0.0046 -0.0272 -0.0023 426 VAL A N   
3426 C CA  . VAL A 426 ? 0.2681 0.4028 0.2975 -0.0023 -0.0235 -0.0007 426 VAL A CA  
3427 C C   . VAL A 426 ? 0.2779 0.4297 0.3189 -0.0074 -0.0294 0.0041  426 VAL A C   
3428 O O   . VAL A 426 ? 0.2572 0.4065 0.2922 -0.0167 -0.0346 0.0035  426 VAL A O   
3429 C CB  . VAL A 426 ? 0.2837 0.4135 0.3095 -0.0049 -0.0179 -0.0041 426 VAL A CB  
3430 C CG1 . VAL A 426 ? 0.2695 0.4139 0.3079 -0.0032 -0.0130 -0.0018 426 VAL A CG1 
3431 C CG2 . VAL A 426 ? 0.2999 0.4160 0.3163 -0.0010 -0.0138 -0.0079 426 VAL A CG2 
3432 N N   . LEU A 427 ? 0.1786 0.3471 0.2361 -0.0014 -0.0285 0.0090  427 LEU A N   
3433 C CA  . LEU A 427 ? 0.1854 0.3764 0.2599 -0.0060 -0.0331 0.0149  427 LEU A CA  
3434 C C   . LEU A 427 ? 0.2463 0.4493 0.3327 -0.0045 -0.0240 0.0154  427 LEU A C   
3435 O O   . LEU A 427 ? 0.2933 0.4988 0.3854 0.0063  -0.0156 0.0149  427 LEU A O   
3436 C CB  . LEU A 427 ? 0.2126 0.4179 0.3006 0.0009  -0.0387 0.0219  427 LEU A CB  
3437 C CG  . LEU A 427 ? 0.3211 0.5542 0.4299 -0.0043 -0.0461 0.0300  427 LEU A CG  
3438 C CD1 . LEU A 427 ? 0.1908 0.4201 0.2883 -0.0189 -0.0588 0.0303  427 LEU A CD1 
3439 C CD2 . LEU A 427 ? 0.2608 0.5113 0.3889 0.0076  -0.0482 0.0379  427 LEU A CD2 
3440 N N   . PHE A 428 ? 0.1913 0.3995 0.2792 -0.0155 -0.0249 0.0162  428 PHE A N   
3441 C CA  . PHE A 428 ? 0.2791 0.4991 0.3765 -0.0155 -0.0157 0.0177  428 PHE A CA  
3442 C C   . PHE A 428 ? 0.3056 0.5475 0.4192 -0.0268 -0.0199 0.0245  428 PHE A C   
3443 O O   . PHE A 428 ? 0.2303 0.4704 0.3410 -0.0378 -0.0308 0.0258  428 PHE A O   
3444 C CB  . PHE A 428 ? 0.2093 0.4091 0.2887 -0.0178 -0.0097 0.0121  428 PHE A CB  
3445 C CG  . PHE A 428 ? 0.2650 0.4503 0.3318 -0.0299 -0.0158 0.0106  428 PHE A CG  
3446 C CD1 . PHE A 428 ? 0.2594 0.4246 0.3105 -0.0306 -0.0213 0.0059  428 PHE A CD1 
3447 C CD2 . PHE A 428 ? 0.2506 0.4408 0.3204 -0.0402 -0.0149 0.0139  428 PHE A CD2 
3448 C CE1 . PHE A 428 ? 0.2127 0.3617 0.2512 -0.0398 -0.0254 0.0037  428 PHE A CE1 
3449 C CE2 . PHE A 428 ? 0.1766 0.3489 0.2334 -0.0505 -0.0202 0.0123  428 PHE A CE2 
3450 C CZ  . PHE A 428 ? 0.1975 0.3485 0.2384 -0.0494 -0.0252 0.0067  428 PHE A CZ  
3451 N N   . ASP A 429 ? 0.2573 0.5201 0.3874 -0.0245 -0.0109 0.0288  429 ASP A N   
3452 C CA  . ASP A 429 ? 0.2676 0.5547 0.4160 -0.0363 -0.0132 0.0365  429 ASP A CA  
3453 C C   . ASP A 429 ? 0.2815 0.5540 0.4156 -0.0481 -0.0104 0.0348  429 ASP A C   
3454 O O   . ASP A 429 ? 0.2753 0.5428 0.4027 -0.0433 0.0009  0.0328  429 ASP A O   
3455 C CB  . ASP A 429 ? 0.2654 0.5845 0.4401 -0.0274 -0.0031 0.0428  429 ASP A CB  
3456 C CG  . ASP A 429 ? 0.3170 0.6675 0.5159 -0.0402 -0.0057 0.0527  429 ASP A CG  
3457 O OD1 . ASP A 429 ? 0.2653 0.6079 0.4560 -0.0573 -0.0117 0.0536  429 ASP A OD1 
3458 O OD2 . ASP A 429 ? 0.3263 0.7097 0.5534 -0.0331 -0.0015 0.0601  429 ASP A OD2 
3459 N N   . PRO A 430 ? 0.3190 0.5813 0.4455 -0.0633 -0.0206 0.0353  430 PRO A N   
3460 C CA  . PRO A 430 ? 0.2683 0.5118 0.3795 -0.0733 -0.0182 0.0341  430 PRO A CA  
3461 C C   . PRO A 430 ? 0.2423 0.5061 0.3672 -0.0799 -0.0098 0.0416  430 PRO A C   
3462 O O   . PRO A 430 ? 0.2652 0.5147 0.3769 -0.0827 -0.0036 0.0411  430 PRO A O   
3463 C CB  . PRO A 430 ? 0.2666 0.4945 0.3677 -0.0876 -0.0316 0.0329  430 PRO A CB  
3464 C CG  . PRO A 430 ? 0.2581 0.5098 0.3772 -0.0903 -0.0408 0.0374  430 PRO A CG  
3465 C CD  . PRO A 430 ? 0.2365 0.5010 0.3652 -0.0720 -0.0351 0.0368  430 PRO A CD  
3466 N N   . GLN A 431 ? 0.2558 0.5540 0.4077 -0.0823 -0.0091 0.0495  431 GLN A N   
3467 C CA  A GLN A 431 ? 0.2575 0.5775 0.4234 -0.0890 0.0005  0.0575  431 GLN A CA  
3468 C CA  B GLN A 431 ? 0.2561 0.5774 0.4230 -0.0889 0.0005  0.0576  431 GLN A CA  
3469 C C   . GLN A 431 ? 0.2712 0.6003 0.4386 -0.0736 0.0175  0.0563  431 GLN A C   
3470 O O   . GLN A 431 ? 0.2836 0.6230 0.4536 -0.0783 0.0280  0.0613  431 GLN A O   
3471 C CB  A GLN A 431 ? 0.2561 0.6131 0.4531 -0.0992 -0.0049 0.0677  431 GLN A CB  
3472 C CB  B GLN A 431 ? 0.2507 0.6101 0.4496 -0.0973 -0.0047 0.0676  431 GLN A CB  
3473 C CG  A GLN A 431 ? 0.3060 0.6951 0.5293 -0.0844 -0.0017 0.0710  431 GLN A CG  
3474 C CG  B GLN A 431 ? 0.2758 0.6275 0.4722 -0.1172 -0.0220 0.0697  431 GLN A CG  
3475 C CD  A GLN A 431 ? 0.3738 0.7961 0.6266 -0.0944 -0.0093 0.0814  431 GLN A CD  
3476 C CD  B GLN A 431 ? 0.3947 0.7821 0.6206 -0.1299 -0.0266 0.0810  431 GLN A CD  
3477 O OE1 A GLN A 431 ? 0.2926 0.7169 0.5505 -0.0947 -0.0229 0.0819  431 GLN A OE1 
3478 O OE1 B GLN A 431 ? 0.4887 0.9036 0.7366 -0.1204 -0.0161 0.0866  431 GLN A OE1 
3479 N NE2 A GLN A 431 ? 0.3703 0.8084 0.6353 -0.1007 -0.0007 0.0882  431 GLN A NE2 
3480 N NE2 B GLN A 431 ? 0.5070 0.8810 0.7255 -0.1476 -0.0415 0.0817  431 GLN A NE2 
3481 N N   . THR A 432 ? 0.2579 0.5806 0.4209 -0.0560 0.0208  0.0496  432 THR A N   
3482 C CA  . THR A 432 ? 0.2174 0.5438 0.3776 -0.0417 0.0367  0.0469  432 THR A CA  
3483 C C   . THR A 432 ? 0.2631 0.5560 0.3943 -0.0330 0.0385  0.0368  432 THR A C   
3484 O O   . THR A 432 ? 0.2886 0.5792 0.4115 -0.0233 0.0508  0.0334  432 THR A O   
3485 C CB  . THR A 432 ? 0.2459 0.5985 0.4302 -0.0266 0.0421  0.0489  432 THR A CB  
3486 O OG1 . THR A 432 ? 0.2191 0.5558 0.3974 -0.0176 0.0329  0.0433  432 THR A OG1 
3487 C CG2 . THR A 432 ? 0.1726 0.5641 0.3906 -0.0345 0.0390  0.0603  432 THR A CG2 
3488 N N   . VAL A 433 ? 0.1930 0.4604 0.3084 -0.0363 0.0269  0.0319  433 VAL A N   
3489 C CA  . VAL A 433 ? 0.2424 0.4821 0.3340 -0.0289 0.0282  0.0237  433 VAL A CA  
3490 C C   . VAL A 433 ? 0.2767 0.5079 0.3526 -0.0323 0.0365  0.0239  433 VAL A C   
3491 O O   . VAL A 433 ? 0.2900 0.5226 0.3650 -0.0445 0.0357  0.0296  433 VAL A O   
3492 C CB  . VAL A 433 ? 0.1853 0.4021 0.2644 -0.0332 0.0157  0.0198  433 VAL A CB  
3493 C CG1 . VAL A 433 ? 0.1801 0.3892 0.2545 -0.0480 0.0097  0.0233  433 VAL A CG1 
3494 C CG2 . VAL A 433 ? 0.1722 0.3652 0.2311 -0.0255 0.0171  0.0125  433 VAL A CG2 
3495 N N   . ARG A 434 ? 0.2885 0.5093 0.3501 -0.0224 0.0439  0.0182  434 ARG A N   
3496 C CA  . ARG A 434 ? 0.3389 0.5529 0.3835 -0.0261 0.0513  0.0191  434 ARG A CA  
3497 C C   . ARG A 434 ? 0.3325 0.5287 0.3565 -0.0166 0.0553  0.0111  434 ARG A C   
3498 O O   . ARG A 434 ? 0.3014 0.4978 0.3283 -0.0055 0.0584  0.0056  434 ARG A O   
3499 C CB  . ARG A 434 ? 0.3080 0.5476 0.3651 -0.0285 0.0636  0.0257  434 ARG A CB  
3500 C CG  . ARG A 434 ? 0.4583 0.7010 0.5059 -0.0180 0.0783  0.0217  434 ARG A CG  
3501 C CD  . ARG A 434 ? 0.3780 0.6474 0.4375 -0.0217 0.0919  0.0294  434 ARG A CD  
3502 N NE  . ARG A 434 ? 0.5188 0.7960 0.5752 -0.0080 0.1081  0.0247  434 ARG A NE  
3503 C CZ  . ARG A 434 ? 0.5725 0.8367 0.6021 -0.0056 0.1182  0.0204  434 ARG A CZ  
3504 N NH1 . ARG A 434 ? 0.6188 0.8637 0.6235 -0.0159 0.1131  0.0216  434 ARG A NH1 
3505 N NH2 . ARG A 434 ? 0.7102 0.9796 0.7364 0.0080  0.1335  0.0148  434 ARG A NH2 
3506 N N   . ASP A 435 ? 0.2814 0.4612 0.2842 -0.0218 0.0541  0.0110  435 ASP A N   
3507 C CA  . ASP A 435 ? 0.3032 0.4662 0.2835 -0.0162 0.0564  0.0043  435 ASP A CA  
3508 C C   . ASP A 435 ? 0.3225 0.4944 0.2949 -0.0122 0.0712  0.0034  435 ASP A C   
3509 O O   . ASP A 435 ? 0.4071 0.5858 0.3739 -0.0192 0.0771  0.0094  435 ASP A O   
3510 C CB  . ASP A 435 ? 0.3251 0.4701 0.2875 -0.0234 0.0481  0.0063  435 ASP A CB  
3511 C CG  . ASP A 435 ? 0.3932 0.5421 0.3512 -0.0335 0.0505  0.0152  435 ASP A CG  
3512 O OD1 . ASP A 435 ? 0.3555 0.5173 0.3300 -0.0395 0.0510  0.0213  435 ASP A OD1 
3513 O OD2 . ASP A 435 ? 0.3695 0.5079 0.3064 -0.0365 0.0510  0.0168  435 ASP A OD2 
3514 N N   . VAL A 436 ? 0.3198 0.4904 0.2908 -0.0007 0.0781  -0.0041 436 VAL A N   
3515 C CA  . VAL A 436 ? 0.3740 0.5495 0.3343 0.0054  0.0940  -0.0071 436 VAL A CA  
3516 C C   . VAL A 436 ? 0.3593 0.5115 0.2845 0.0032  0.0942  -0.0128 436 VAL A C   
3517 O O   . VAL A 436 ? 0.3365 0.4903 0.2447 0.0028  0.1058  -0.0131 436 VAL A O   
3518 C CB  . VAL A 436 ? 0.2806 0.4620 0.2540 0.0202  0.1019  -0.0128 436 VAL A CB  
3519 C CG1 . VAL A 436 ? 0.3020 0.4878 0.2643 0.0284  0.1203  -0.0168 436 VAL A CG1 
3520 C CG2 . VAL A 436 ? 0.3022 0.5084 0.3109 0.0217  0.0991  -0.0058 436 VAL A CG2 
3521 N N   . ALA A 437 ? 0.3001 0.4319 0.2140 0.0014  0.0814  -0.0171 437 ALA A N   
3522 C CA  . ALA A 437 ? 0.3588 0.4702 0.2411 -0.0025 0.0783  -0.0214 437 ALA A CA  
3523 C C   . ALA A 437 ? 0.4362 0.5508 0.3045 -0.0123 0.0796  -0.0135 437 ALA A C   
3524 O O   . ALA A 437 ? 0.3760 0.4988 0.2576 -0.0195 0.0737  -0.0043 437 ALA A O   
3525 C CB  . ALA A 437 ? 0.3396 0.4358 0.2204 -0.0054 0.0622  -0.0233 437 ALA A CB  
3526 N N   . SER A 438 ? 0.3844 0.4901 0.2235 -0.0130 0.0874  -0.0172 438 SER A N   
3527 C CA  . SER A 438 ? 0.3843 0.4902 0.2040 -0.0224 0.0889  -0.0096 438 SER A CA  
3528 C C   . SER A 438 ? 0.4922 0.5759 0.2764 -0.0264 0.0818  -0.0144 438 SER A C   
3529 O O   . SER A 438 ? 0.5159 0.5846 0.2895 -0.0220 0.0784  -0.0247 438 SER A O   
3530 C CB  . SER A 438 ? 0.4008 0.5228 0.2187 -0.0206 0.1084  -0.0073 438 SER A CB  
3531 O OG  . SER A 438 ? 0.5215 0.6337 0.3159 -0.0127 0.1205  -0.0184 438 SER A OG  
3532 N N   . PHE A 439 ? 0.4668 0.5475 0.2314 -0.0358 0.0785  -0.0061 439 PHE A N   
3533 C CA  . PHE A 439 ? 0.4700 0.5314 0.2000 -0.0410 0.0697  -0.0092 439 PHE A CA  
3534 C C   . PHE A 439 ? 0.5191 0.5691 0.2183 -0.0369 0.0822  -0.0213 439 PHE A C   
3535 O O   . PHE A 439 ? 0.5794 0.6103 0.2550 -0.0385 0.0741  -0.0296 439 PHE A O   
3536 C CB  . PHE A 439 ? 0.4532 0.5141 0.1684 -0.0515 0.0632  0.0039  439 PHE A CB  
3537 C CG  . PHE A 439 ? 0.5194 0.5814 0.2560 -0.0549 0.0467  0.0134  439 PHE A CG  
3538 C CD1 . PHE A 439 ? 0.4417 0.4928 0.1732 -0.0566 0.0297  0.0127  439 PHE A CD1 
3539 C CD2 . PHE A 439 ? 0.5406 0.6147 0.3035 -0.0561 0.0485  0.0227  439 PHE A CD2 
3540 C CE1 . PHE A 439 ? 0.4888 0.5417 0.2417 -0.0575 0.0162  0.0213  439 PHE A CE1 
3541 C CE2 . PHE A 439 ? 0.5090 0.5806 0.2898 -0.0579 0.0345  0.0301  439 PHE A CE2 
3542 C CZ  . PHE A 439 ? 0.4492 0.5107 0.2254 -0.0575 0.0192  0.0294  439 PHE A CZ  
3543 N N   . SER A 440 ? 0.4860 0.5469 0.1846 -0.0317 0.1021  -0.0228 440 SER A N   
3544 C CA  . SER A 440 ? 0.6766 0.7246 0.3451 -0.0256 0.1164  -0.0357 440 SER A CA  
3545 C C   . SER A 440 ? 0.5665 0.6090 0.2499 -0.0128 0.1211  -0.0480 440 SER A C   
3546 O O   . SER A 440 ? 0.5987 0.6212 0.2551 -0.0076 0.1276  -0.0608 440 SER A O   
3547 C CB  . SER A 440 ? 0.5731 0.6344 0.2380 -0.0221 0.1363  -0.0310 440 SER A CB  
3548 O OG  . SER A 440 ? 0.7105 0.8009 0.4132 -0.0210 0.1441  -0.0230 440 SER A OG  
3549 N N   . ASP A 441 ? 0.5491 0.6066 0.2732 -0.0078 0.1173  -0.0442 441 ASP A N   
3550 C CA  . ASP A 441 ? 0.5869 0.6417 0.3287 0.0049  0.1220  -0.0534 441 ASP A CA  
3551 C C   . ASP A 441 ? 0.5021 0.5609 0.2743 0.0033  0.1053  -0.0490 441 ASP A C   
3552 O O   . ASP A 441 ? 0.4940 0.5732 0.3006 0.0072  0.1068  -0.0428 441 ASP A O   
3553 C CB  . ASP A 441 ? 0.6445 0.7214 0.4068 0.0162  0.1426  -0.0524 441 ASP A CB  
3554 C CG  . ASP A 441 ? 0.6847 0.7535 0.4547 0.0317  0.1510  -0.0633 441 ASP A CG  
3555 O OD1 . ASP A 441 ? 0.6164 0.6617 0.3781 0.0328  0.1401  -0.0712 441 ASP A OD1 
3556 O OD2 . ASP A 441 ? 0.7063 0.7930 0.4920 0.0431  0.1689  -0.0630 441 ASP A OD2 
3557 N N   . PRO A 442 ? 0.5393 0.5801 0.2995 -0.0031 0.0889  -0.0516 442 PRO A N   
3558 C CA  . PRO A 442 ? 0.4605 0.5072 0.2472 -0.0067 0.0731  -0.0453 442 PRO A CA  
3559 C C   . PRO A 442 ? 0.3934 0.4372 0.2009 0.0016  0.0712  -0.0506 442 PRO A C   
3560 O O   . PRO A 442 ? 0.4730 0.5274 0.3072 0.0012  0.0632  -0.0447 442 PRO A O   
3561 C CB  . PRO A 442 ? 0.4915 0.5232 0.2562 -0.0173 0.0575  -0.0446 442 PRO A CB  
3562 C CG  . PRO A 442 ? 0.4685 0.4784 0.1967 -0.0170 0.0626  -0.0561 442 PRO A CG  
3563 C CD  . PRO A 442 ? 0.4829 0.4995 0.2035 -0.0097 0.0834  -0.0587 442 PRO A CD  
3564 N N   . LYS A 443 ? 0.4513 0.4785 0.2450 0.0091  0.0782  -0.0615 443 LYS A N   
3565 C CA  . LYS A 443 ? 0.5381 0.5572 0.3468 0.0159  0.0744  -0.0660 443 LYS A CA  
3566 C C   . LYS A 443 ? 0.4793 0.5151 0.3147 0.0288  0.0866  -0.0644 443 LYS A C   
3567 O O   . LYS A 443 ? 0.5706 0.5966 0.4029 0.0402  0.0966  -0.0718 443 LYS A O   
3568 C CB  . LYS A 443 ? 0.5679 0.5564 0.3474 0.0166  0.0740  -0.0782 443 LYS A CB  
3569 C CG  . LYS A 443 ? 0.6179 0.5915 0.3709 0.0028  0.0608  -0.0796 443 LYS A CG  
3570 C CD  . LYS A 443 ? 0.5794 0.5208 0.3039 0.0020  0.0593  -0.0922 443 LYS A CD  
3571 C CE  . LYS A 443 ? 0.7571 0.6858 0.4539 -0.0133 0.0452  -0.0931 443 LYS A CE  
3572 N NZ  . LYS A 443 ? 0.7690 0.6669 0.4433 -0.0179 0.0386  -0.1039 443 LYS A NZ  
3573 N N   . ARG A 444 ? 0.4931 0.5544 0.3557 0.0269  0.0849  -0.0540 444 ARG A N   
3574 C CA  . ARG A 444 ? 0.3555 0.4379 0.2458 0.0371  0.0946  -0.0504 444 ARG A CA  
3575 C C   . ARG A 444 ? 0.4314 0.5279 0.3509 0.0343  0.0832  -0.0424 444 ARG A C   
3576 O O   . ARG A 444 ? 0.3677 0.4697 0.2905 0.0237  0.0737  -0.0361 444 ARG A O   
3577 C CB  . ARG A 444 ? 0.3429 0.4458 0.2350 0.0369  0.1082  -0.0456 444 ARG A CB  
3578 C CG  . ARG A 444 ? 0.4639 0.5547 0.3294 0.0439  0.1238  -0.0545 444 ARG A CG  
3579 C CD  . ARG A 444 ? 0.4908 0.6057 0.3616 0.0454  0.1402  -0.0491 444 ARG A CD  
3580 N NE  . ARG A 444 ? 0.5962 0.7192 0.4609 0.0304  0.1340  -0.0403 444 ARG A NE  
3581 C CZ  . ARG A 444 ? 0.5872 0.7321 0.4578 0.0264  0.1444  -0.0321 444 ARG A CZ  
3582 N NH1 . ARG A 444 ? 0.5012 0.6669 0.3866 0.0363  0.1624  -0.0313 444 ARG A NH1 
3583 N NH2 . ARG A 444 ? 0.5169 0.6635 0.3796 0.0123  0.1367  -0.0237 444 ARG A NH2 
3584 N N   . PRO A 445 ? 0.4653 0.5655 0.4041 0.0437  0.0835  -0.0426 445 PRO A N   
3585 C CA  . PRO A 445 ? 0.3470 0.4586 0.3094 0.0406  0.0722  -0.0356 445 PRO A CA  
3586 C C   . PRO A 445 ? 0.3050 0.4442 0.2885 0.0361  0.0736  -0.0264 445 PRO A C   
3587 O O   . PRO A 445 ? 0.3132 0.4697 0.3049 0.0405  0.0854  -0.0241 445 PRO A O   
3588 C CB  . PRO A 445 ? 0.3795 0.4875 0.3541 0.0530  0.0738  -0.0377 445 PRO A CB  
3589 C CG  . PRO A 445 ? 0.3515 0.4554 0.3176 0.0648  0.0894  -0.0437 445 PRO A CG  
3590 C CD  . PRO A 445 ? 0.4407 0.5300 0.3767 0.0579  0.0931  -0.0497 445 PRO A CD  
3591 N N   . ALA A 446 ? 0.3084 0.4514 0.3003 0.0270  0.0618  -0.0211 446 ALA A N   
3592 C CA  . ALA A 446 ? 0.3172 0.4820 0.3271 0.0201  0.0605  -0.0126 446 ALA A CA  
3593 C C   . ALA A 446 ? 0.3058 0.4936 0.3421 0.0275  0.0647  -0.0083 446 ALA A C   
3594 O O   . ALA A 446 ? 0.3112 0.4963 0.3539 0.0383  0.0656  -0.0110 446 ALA A O   
3595 C CB  . ALA A 446 ? 0.2712 0.4305 0.2832 0.0108  0.0470  -0.0095 446 ALA A CB  
3596 N N   . ASP A 447 ? 0.2661 0.4770 0.3186 0.0210  0.0667  -0.0006 447 ASP A N   
3597 C CA  . ASP A 447 ? 0.3202 0.5577 0.4019 0.0244  0.0668  0.0060  447 ASP A CA  
3598 C C   . ASP A 447 ? 0.3044 0.5442 0.3957 0.0145  0.0517  0.0106  447 ASP A C   
3599 O O   . ASP A 447 ? 0.2830 0.5074 0.3605 0.0044  0.0440  0.0096  447 ASP A O   
3600 C CB  . ASP A 447 ? 0.2507 0.5155 0.3466 0.0218  0.0783  0.0126  447 ASP A CB  
3601 C CG  . ASP A 447 ? 0.3489 0.6161 0.4390 0.0347  0.0958  0.0082  447 ASP A CG  
3602 O OD1 . ASP A 447 ? 0.4407 0.6957 0.5267 0.0487  0.0990  0.0017  447 ASP A OD1 
3603 O OD2 . ASP A 447 ? 0.5324 0.8122 0.6206 0.0306  0.1069  0.0114  447 ASP A OD2 
3604 N N   . GLY A 448 ? 0.2631 0.5227 0.3781 0.0178  0.0476  0.0158  448 GLY A N   
3605 C CA  . GLY A 448 ? 0.2338 0.4985 0.3577 0.0075  0.0337  0.0205  448 GLY A CA  
3606 C C   . GLY A 448 ? 0.2290 0.4709 0.3396 0.0083  0.0228  0.0160  448 GLY A C   
3607 O O   . GLY A 448 ? 0.2680 0.5102 0.3808 -0.0005 0.0116  0.0185  448 GLY A O   
3608 N N   . ILE A 449 ? 0.2736 0.4950 0.3690 0.0175  0.0261  0.0092  449 ILE A N   
3609 C CA  . ILE A 449 ? 0.2675 0.4695 0.3520 0.0188  0.0174  0.0058  449 ILE A CA  
3610 C C   . ILE A 449 ? 0.3096 0.5199 0.4082 0.0299  0.0161  0.0088  449 ILE A C   
3611 O O   . ILE A 449 ? 0.3054 0.5113 0.4039 0.0420  0.0241  0.0062  449 ILE A O   
3612 C CB  . ILE A 449 ? 0.3385 0.5152 0.4007 0.0209  0.0206  -0.0017 449 ILE A CB  
3613 C CG1 . ILE A 449 ? 0.3128 0.4835 0.3628 0.0114  0.0219  -0.0029 449 ILE A CG1 
3614 C CG2 . ILE A 449 ? 0.2497 0.4095 0.3032 0.0212  0.0122  -0.0038 449 ILE A CG2 
3615 C CD1 . ILE A 449 ? 0.2713 0.4345 0.3164 0.0012  0.0122  -0.0018 449 ILE A CD1 
3616 N N   . GLU A 450 ? 0.3086 0.5294 0.4179 0.0261  0.0057  0.0144  450 GLU A N   
3617 C CA  . GLU A 450 ? 0.2560 0.4903 0.3829 0.0367  0.0037  0.0201  450 GLU A CA  
3618 C C   . GLU A 450 ? 0.2595 0.4736 0.3751 0.0425  -0.0021 0.0187  450 GLU A C   
3619 O O   . GLU A 450 ? 0.3170 0.5330 0.4419 0.0551  -0.0003 0.0216  450 GLU A O   
3620 C CB  . GLU A 450 ? 0.3217 0.5838 0.4695 0.0293  -0.0051 0.0290  450 GLU A CB  
3621 C CG  . GLU A 450 ? 0.4026 0.6941 0.5745 0.0332  0.0041  0.0342  450 GLU A CG  
3622 C CD  . GLU A 450 ? 0.5911 0.9101 0.7818 0.0202  -0.0039 0.0424  450 GLU A CD  
3623 O OE1 . GLU A 450 ? 0.7686 1.0987 0.9694 0.0172  -0.0168 0.0487  450 GLU A OE1 
3624 O OE2 . GLU A 450 ? 0.7206 1.0496 0.9148 0.0119  0.0023  0.0430  450 GLU A OE2 
3625 N N   . ALA A 451 ? 0.1975 0.3917 0.2936 0.0343  -0.0080 0.0147  451 ALA A N   
3626 C CA  . ALA A 451 ? 0.2204 0.3956 0.3051 0.0389  -0.0119 0.0139  451 ALA A CA  
3627 C C   . ALA A 451 ? 0.2653 0.4199 0.3289 0.0304  -0.0130 0.0078  451 ALA A C   
3628 O O   . ALA A 451 ? 0.2853 0.4419 0.3444 0.0204  -0.0159 0.0065  451 ALA A O   
3629 C CB  . ALA A 451 ? 0.1951 0.3796 0.2873 0.0386  -0.0230 0.0218  451 ALA A CB  
3630 N N   . VAL A 452 ? 0.2328 0.3674 0.2842 0.0345  -0.0106 0.0043  452 VAL A N   
3631 C CA  . VAL A 452 ? 0.2265 0.3446 0.2612 0.0275  -0.0115 -0.0001 452 VAL A CA  
3632 C C   . VAL A 452 ? 0.3093 0.4143 0.3366 0.0295  -0.0154 0.0022  452 VAL A C   
3633 O O   . VAL A 452 ? 0.2797 0.3770 0.3085 0.0375  -0.0136 0.0036  452 VAL A O   
3634 C CB  . VAL A 452 ? 0.3046 0.4120 0.3309 0.0274  -0.0046 -0.0065 452 VAL A CB  
3635 C CG1 . VAL A 452 ? 0.2166 0.3125 0.2303 0.0199  -0.0068 -0.0093 452 VAL A CG1 
3636 C CG2 . VAL A 452 ? 0.2112 0.3309 0.2432 0.0261  0.0005  -0.0078 452 VAL A CG2 
3637 N N   . MET A 453 ? 0.3004 0.4015 0.3185 0.0222  -0.0200 0.0028  453 MET A N   
3638 C CA  . MET A 453 ? 0.3016 0.3922 0.3111 0.0220  -0.0236 0.0062  453 MET A CA  
3639 C C   . MET A 453 ? 0.2787 0.3580 0.2762 0.0160  -0.0209 0.0024  453 MET A C   
3640 O O   . MET A 453 ? 0.2441 0.3267 0.2388 0.0107  -0.0199 -0.0010 453 MET A O   
3641 C CB  . MET A 453 ? 0.2476 0.3470 0.2565 0.0188  -0.0314 0.0116  453 MET A CB  
3642 C CG  . MET A 453 ? 0.2581 0.3468 0.2537 0.0167  -0.0349 0.0156  453 MET A CG  
3643 S SD  . MET A 453 ? 0.3013 0.4008 0.2961 0.0148  -0.0459 0.0233  453 MET A SD  
3644 C CE  . MET A 453 ? 0.2685 0.3742 0.2810 0.0271  -0.0486 0.0315  453 MET A CE  
3645 N N   . VAL A 454 ? 0.3282 0.3943 0.3197 0.0168  -0.0196 0.0035  454 VAL A N   
3646 C CA  . VAL A 454 ? 0.3111 0.3695 0.2949 0.0109  -0.0169 0.0013  454 VAL A CA  
3647 C C   . VAL A 454 ? 0.2700 0.3213 0.2458 0.0086  -0.0188 0.0069  454 VAL A C   
3648 O O   . VAL A 454 ? 0.3537 0.3951 0.3283 0.0118  -0.0202 0.0110  454 VAL A O   
3649 C CB  . VAL A 454 ? 0.3290 0.3780 0.3127 0.0112  -0.0136 -0.0025 454 VAL A CB  
3650 C CG1 . VAL A 454 ? 0.2877 0.3337 0.2670 0.0039  -0.0122 -0.0033 454 VAL A CG1 
3651 C CG2 . VAL A 454 ? 0.2537 0.3091 0.2425 0.0138  -0.0113 -0.0073 454 VAL A CG2 
3652 N N   . ASN A 455 ? 0.2855 0.3401 0.2545 0.0034  -0.0180 0.0072  455 ASN A N   
3653 C CA  . ASN A 455 ? 0.3321 0.3812 0.2910 0.0003  -0.0183 0.0128  455 ASN A CA  
3654 C C   . ASN A 455 ? 0.3131 0.3596 0.2693 0.0040  -0.0245 0.0194  455 ASN A C   
3655 O O   . ASN A 455 ? 0.3022 0.3386 0.2527 0.0038  -0.0256 0.0257  455 ASN A O   
3656 C CB  . ASN A 455 ? 0.2608 0.3009 0.2186 -0.0033 -0.0149 0.0145  455 ASN A CB  
3657 C CG  . ASN A 455 ? 0.3262 0.3727 0.2878 -0.0075 -0.0099 0.0102  455 ASN A CG  
3658 O OD1 . ASN A 455 ? 0.3210 0.3750 0.2796 -0.0089 -0.0069 0.0089  455 ASN A OD1 
3659 N ND2 . ASN A 455 ? 0.2424 0.2856 0.2100 -0.0091 -0.0093 0.0078  455 ASN A ND2 
3660 N N   . GLY A 456 ? 0.3201 0.3764 0.2813 0.0069  -0.0290 0.0189  456 GLY A N   
3661 C CA  . GLY A 456 ? 0.2367 0.2956 0.1987 0.0107  -0.0365 0.0261  456 GLY A CA  
3662 C C   . GLY A 456 ? 0.3582 0.4135 0.3320 0.0197  -0.0376 0.0295  456 GLY A C   
3663 O O   . GLY A 456 ? 0.3104 0.3691 0.2879 0.0247  -0.0441 0.0369  456 GLY A O   
3664 N N   . VAL A 457 ? 0.2946 0.3426 0.2736 0.0223  -0.0316 0.0244  457 VAL A N   
3665 C CA  . VAL A 457 ? 0.2899 0.3302 0.2770 0.0318  -0.0307 0.0259  457 VAL A CA  
3666 C C   . VAL A 457 ? 0.3325 0.3858 0.3330 0.0370  -0.0277 0.0206  457 VAL A C   
3667 O O   . VAL A 457 ? 0.3054 0.3611 0.3054 0.0329  -0.0230 0.0132  457 VAL A O   
3668 C CB  . VAL A 457 ? 0.3553 0.3741 0.3349 0.0304  -0.0264 0.0238  457 VAL A CB  
3669 C CG1 . VAL A 457 ? 0.3407 0.3480 0.3261 0.0411  -0.0242 0.0229  457 VAL A CG1 
3670 C CG2 . VAL A 457 ? 0.2777 0.2844 0.2452 0.0249  -0.0291 0.0313  457 VAL A CG2 
3671 N N   . MET A 458 ? 0.3631 0.4266 0.3765 0.0460  -0.0304 0.0253  458 MET A N   
3672 C CA  . MET A 458 ? 0.2925 0.3706 0.3203 0.0514  -0.0261 0.0216  458 MET A CA  
3673 C C   . MET A 458 ? 0.3488 0.4113 0.3733 0.0563  -0.0174 0.0145  458 MET A C   
3674 O O   . MET A 458 ? 0.3251 0.3704 0.3471 0.0641  -0.0158 0.0159  458 MET A O   
3675 C CB  . MET A 458 ? 0.3268 0.4213 0.3721 0.0610  -0.0304 0.0297  458 MET A CB  
3676 C CG  . MET A 458 ? 0.3094 0.4269 0.3723 0.0639  -0.0264 0.0277  458 MET A CG  
3677 S SD  . MET A 458 ? 0.3819 0.5150 0.4425 0.0488  -0.0287 0.0236  458 MET A SD  
3678 C CE  . MET A 458 ? 0.2808 0.4317 0.3479 0.0444  -0.0426 0.0337  458 MET A CE  
3679 N N   . SER A 459 ? 0.3094 0.3751 0.3313 0.0512  -0.0122 0.0068  459 SER A N   
3680 C CA  . SER A 459 ? 0.3933 0.4416 0.4061 0.0525  -0.0055 -0.0006 459 SER A CA  
3681 C C   . SER A 459 ? 0.3731 0.4291 0.3918 0.0585  0.0023  -0.0058 459 SER A C   
3682 O O   . SER A 459 ? 0.4217 0.4607 0.4308 0.0619  0.0081  -0.0120 459 SER A O   
3683 C CB  . SER A 459 ? 0.2776 0.3188 0.2780 0.0405  -0.0063 -0.0051 459 SER A CB  
3684 O OG  . SER A 459 ? 0.3764 0.4104 0.3708 0.0351  -0.0113 -0.0004 459 SER A OG  
3685 N N   . TYR A 460 ? 0.3189 0.3990 0.3514 0.0592  0.0027  -0.0033 460 TYR A N   
3686 C CA  . TYR A 460 ? 0.3605 0.4502 0.3980 0.0633  0.0114  -0.0074 460 TYR A CA  
3687 C C   . TYR A 460 ? 0.2908 0.4093 0.3497 0.0661  0.0104  -0.0007 460 TYR A C   
3688 O O   . TYR A 460 ? 0.3131 0.4432 0.3780 0.0599  0.0017  0.0050  460 TYR A O   
3689 C CB  . TYR A 460 ? 0.3242 0.4115 0.3498 0.0530  0.0133  -0.0134 460 TYR A CB  
3690 C CG  . TYR A 460 ? 0.3555 0.4503 0.3818 0.0562  0.0229  -0.0174 460 TYR A CG  
3691 C CD1 . TYR A 460 ? 0.3277 0.4051 0.3411 0.0621  0.0307  -0.0244 460 TYR A CD1 
3692 C CD2 . TYR A 460 ? 0.2689 0.3865 0.3064 0.0521  0.0241  -0.0143 460 TYR A CD2 
3693 C CE1 . TYR A 460 ? 0.3800 0.4636 0.3905 0.0647  0.0406  -0.0282 460 TYR A CE1 
3694 C CE2 . TYR A 460 ? 0.3048 0.4299 0.3417 0.0540  0.0337  -0.0168 460 TYR A CE2 
3695 C CZ  . TYR A 460 ? 0.3936 0.5023 0.4166 0.0607  0.0424  -0.0239 460 TYR A CZ  
3696 O OH  . TYR A 460 ? 0.3131 0.4290 0.3327 0.0626  0.0529  -0.0265 460 TYR A OH  
3697 N N   . GLY A 461 ? 0.4202 0.5505 0.4896 0.0746  0.0196  -0.0016 461 GLY A N   
3698 C CA  . GLY A 461 ? 0.4387 0.5994 0.5325 0.0781  0.0192  0.0061  461 GLY A CA  
3699 C C   . GLY A 461 ? 0.4120 0.5880 0.5144 0.0828  0.0317  0.0040  461 GLY A C   
3700 O O   . GLY A 461 ? 0.3812 0.5420 0.4677 0.0842  0.0409  -0.0041 461 GLY A O   
3701 N N   . SER A 462 ? 0.4314 0.6390 0.5593 0.0849  0.0316  0.0120  462 SER A N   
3702 C CA  A SER A 462 ? 0.4467 0.6752 0.5859 0.0869  0.0436  0.0121  462 SER A CA  
3703 C CA  B SER A 462 ? 0.4464 0.6753 0.5860 0.0870  0.0435  0.0122  462 SER A CA  
3704 C C   . SER A 462 ? 0.4665 0.6850 0.6018 0.1033  0.0590  0.0063  462 SER A C   
3705 O O   . SER A 462 ? 0.4686 0.6934 0.6005 0.1037  0.0714  0.0026  462 SER A O   
3706 C CB  A SER A 462 ? 0.3551 0.6221 0.5264 0.0863  0.0399  0.0234  462 SER A CB  
3707 C CB  B SER A 462 ? 0.3550 0.6222 0.5268 0.0867  0.0398  0.0236  462 SER A CB  
3708 O OG  A SER A 462 ? 0.3669 0.6400 0.5382 0.0701  0.0255  0.0276  462 SER A OG  
3709 O OG  B SER A 462 ? 0.4520 0.7279 0.6427 0.1025  0.0392  0.0296  462 SER A OG  
3710 N N   . ASP A 463 ? 0.3905 0.5914 0.5240 0.1169  0.0591  0.0053  463 ASP A N   
3711 C CA  . ASP A 463 ? 0.4553 0.6390 0.5797 0.1325  0.0740  -0.0023 463 ASP A CA  
3712 C C   . ASP A 463 ? 0.4709 0.6196 0.5595 0.1257  0.0776  -0.0148 463 ASP A C   
3713 O O   . ASP A 463 ? 0.5397 0.6685 0.6139 0.1365  0.0896  -0.0231 463 ASP A O   
3714 C CB  . ASP A 463 ? 0.3665 0.5385 0.4994 0.1493  0.0723  0.0011  463 ASP A CB  
3715 C CG  . ASP A 463 ? 0.5615 0.7056 0.6775 0.1422  0.0585  0.0008  463 ASP A CG  
3716 O OD1 . ASP A 463 ? 0.5032 0.6391 0.6027 0.1252  0.0509  -0.0023 463 ASP A OD1 
3717 O OD2 . ASP A 463 ? 0.5464 0.6773 0.6664 0.1541  0.0556  0.0045  463 ASP A OD2 
3718 N N   . LYS A 464 ? 0.4053 0.5457 0.4790 0.1086  0.0675  -0.0163 464 LYS A N   
3719 C CA  . LYS A 464 ? 0.4762 0.5896 0.5194 0.0999  0.0686  -0.0262 464 LYS A CA  
3720 C C   . LYS A 464 ? 0.4942 0.5718 0.5181 0.1037  0.0658  -0.0324 464 LYS A C   
3721 O O   . LYS A 464 ? 0.5954 0.6490 0.5938 0.0984  0.0678  -0.0412 464 LYS A O   
3722 C CB  . LYS A 464 ? 0.4872 0.6026 0.5197 0.1025  0.0832  -0.0324 464 LYS A CB  
3723 C CG  . LYS A 464 ? 0.4840 0.6353 0.5367 0.1001  0.0890  -0.0255 464 LYS A CG  
3724 C CD  . LYS A 464 ? 0.5073 0.6704 0.5621 0.0824  0.0778  -0.0204 464 LYS A CD  
3725 C CE  . LYS A 464 ? 0.5112 0.7093 0.5878 0.0787  0.0826  -0.0124 464 LYS A CE  
3726 N NZ  . LYS A 464 ? 0.4856 0.6838 0.5462 0.0692  0.0892  -0.0146 464 LYS A NZ  
3727 N N   . LYS A 465 ? 0.4240 0.4966 0.4586 0.1113  0.0603  -0.0273 465 LYS A N   
3728 C CA  A LYS A 465 ? 0.4507 0.4882 0.4676 0.1132  0.0567  -0.0315 465 LYS A CA  
3729 C CA  B LYS A 465 ? 0.4507 0.4882 0.4676 0.1133  0.0567  -0.0315 465 LYS A CA  
3730 C C   . LYS A 465 ? 0.4808 0.5135 0.4936 0.0993  0.0425  -0.0273 465 LYS A C   
3731 O O   . LYS A 465 ? 0.3687 0.4236 0.3975 0.0948  0.0349  -0.0190 465 LYS A O   
3732 C CB  A LYS A 465 ? 0.4268 0.4575 0.4557 0.1317  0.0604  -0.0279 465 LYS A CB  
3733 C CB  B LYS A 465 ? 0.4265 0.4575 0.4557 0.1316  0.0602  -0.0277 465 LYS A CB  
3734 C CG  A LYS A 465 ? 0.5028 0.5339 0.5337 0.1481  0.0769  -0.0334 465 LYS A CG  
3735 C CG  B LYS A 465 ? 0.4940 0.5334 0.5317 0.1485  0.0760  -0.0308 465 LYS A CG  
3736 C CD  A LYS A 465 ? 0.4427 0.4658 0.4870 0.1687  0.0809  -0.0293 465 LYS A CD  
3737 C CD  B LYS A 465 ? 0.5679 0.5886 0.5787 0.1457  0.0870  -0.0439 465 LYS A CD  
3738 C CE  A LYS A 465 ? 0.4968 0.5184 0.5415 0.1867  0.0999  -0.0361 465 LYS A CE  
3739 C CE  B LYS A 465 ? 0.4843 0.5133 0.5019 0.1637  0.1051  -0.0474 465 LYS A CE  
3740 N NZ  A LYS A 465 ? 0.4682 0.4876 0.5320 0.2098  0.1048  -0.0304 465 LYS A NZ  
3741 N NZ  B LYS A 465 ? 0.4988 0.5203 0.4918 0.1579  0.1156  -0.0582 465 LYS A NZ  
3742 N N   . ILE A 466 ? 0.4361 0.4399 0.4270 0.0920  0.0393  -0.0332 466 ILE A N   
3743 C CA  . ILE A 466 ? 0.4048 0.4026 0.3913 0.0797  0.0279  -0.0293 466 ILE A CA  
3744 C C   . ILE A 466 ? 0.4261 0.4092 0.4159 0.0866  0.0236  -0.0234 466 ILE A C   
3745 O O   . ILE A 466 ? 0.4110 0.3689 0.3921 0.0957  0.0282  -0.0271 466 ILE A O   
3746 C CB  . ILE A 466 ? 0.3962 0.3738 0.3604 0.0672  0.0258  -0.0368 466 ILE A CB  
3747 C CG1 . ILE A 466 ? 0.4211 0.4151 0.3827 0.0597  0.0280  -0.0402 466 ILE A CG1 
3748 C CG2 . ILE A 466 ? 0.3809 0.3525 0.3428 0.0560  0.0158  -0.0321 466 ILE A CG2 
3749 C CD1 . ILE A 466 ? 0.3895 0.3707 0.3333 0.0461  0.0231  -0.0450 466 ILE A CD1 
3750 N N   . THR A 467 ? 0.3956 0.3916 0.3953 0.0819  0.0148  -0.0144 467 THR A N   
3751 C CA  . THR A 467 ? 0.3471 0.3326 0.3504 0.0879  0.0096  -0.0063 467 THR A CA  
3752 C C   . THR A 467 ? 0.4144 0.3926 0.4091 0.0750  0.0008  -0.0017 467 THR A C   
3753 O O   . THR A 467 ? 0.4829 0.4538 0.4789 0.0780  -0.0044 0.0066  467 THR A O   
3754 C CB  . THR A 467 ? 0.4314 0.4433 0.4574 0.0979  0.0075  0.0030  467 THR A CB  
3755 O OG1 . THR A 467 ? 0.3816 0.4206 0.4152 0.0874  0.0024  0.0057  467 THR A OG1 
3756 C CG2 . THR A 467 ? 0.3885 0.4088 0.4266 0.1132  0.0179  0.0000  467 THR A CG2 
3757 N N   . GLY A 468 ? 0.4031 0.3841 0.3894 0.0613  -0.0007 -0.0059 468 GLY A N   
3758 C CA  . GLY A 468 ? 0.3379 0.3145 0.3173 0.0498  -0.0069 -0.0015 468 GLY A CA  
3759 C C   . GLY A 468 ? 0.3916 0.3550 0.3580 0.0384  -0.0061 -0.0080 468 GLY A C   
3760 O O   . GLY A 468 ? 0.4483 0.4144 0.4117 0.0365  -0.0027 -0.0155 468 GLY A O   
3761 N N   . ARG A 469 ? 0.3908 0.3405 0.3497 0.0302  -0.0099 -0.0040 469 ARG A N   
3762 C CA  . ARG A 469 ? 0.3915 0.3332 0.3414 0.0171  -0.0110 -0.0076 469 ARG A CA  
3763 C C   . ARG A 469 ? 0.4067 0.3602 0.3592 0.0074  -0.0142 -0.0006 469 ARG A C   
3764 O O   . ARG A 469 ? 0.4242 0.3656 0.3708 -0.0015 -0.0161 0.0029  469 ARG A O   
3765 C CB  . ARG A 469 ? 0.3803 0.2900 0.3171 0.0149  -0.0114 -0.0102 469 ARG A CB  
3766 C CG  . ARG A 469 ? 0.4715 0.3641 0.4029 0.0269  -0.0066 -0.0170 469 ARG A CG  
3767 C CD  . ARG A 469 ? 0.4894 0.3758 0.4101 0.0220  -0.0044 -0.0277 469 ARG A CD  
3768 N NE  . ARG A 469 ? 0.5301 0.4004 0.4388 0.0065  -0.0093 -0.0294 469 ARG A NE  
3769 C CZ  . ARG A 469 ? 0.5335 0.3702 0.4255 0.0031  -0.0102 -0.0342 469 ARG A CZ  
3770 N NH1 . ARG A 469 ? 0.6852 0.4975 0.5694 0.0161  -0.0054 -0.0379 469 ARG A NH1 
3771 N NH2 . ARG A 469 ? 0.5917 0.4188 0.4751 -0.0136 -0.0161 -0.0350 469 ARG A NH2 
3772 N N   . ALA A 470 ? 0.3868 0.3636 0.3474 0.0086  -0.0142 0.0012  470 ALA A N   
3773 C CA  . ALA A 470 ? 0.3780 0.3654 0.3393 0.0025  -0.0155 0.0075  470 ALA A CA  
3774 C C   . ALA A 470 ? 0.3975 0.4010 0.3623 -0.0048 -0.0140 0.0047  470 ALA A C   
3775 O O   . ALA A 470 ? 0.3528 0.3677 0.3183 -0.0076 -0.0132 0.0082  470 ALA A O   
3776 C CB  . ALA A 470 ? 0.3000 0.2981 0.2648 0.0095  -0.0175 0.0123  470 ALA A CB  
3777 N N   . GLY A 471 ? 0.3606 0.3646 0.3264 -0.0073 -0.0133 -0.0014 471 GLY A N   
3778 C CA  . GLY A 471 ? 0.3568 0.3758 0.3276 -0.0132 -0.0126 -0.0027 471 GLY A CA  
3779 C C   . GLY A 471 ? 0.3300 0.3501 0.3017 -0.0225 -0.0126 0.0023  471 GLY A C   
3780 O O   . GLY A 471 ? 0.3743 0.3800 0.3411 -0.0273 -0.0140 0.0053  471 GLY A O   
3781 N N   . ARG A 472 ? 0.2714 0.3088 0.2500 -0.0248 -0.0103 0.0036  472 ARG A N   
3782 C CA  . ARG A 472 ? 0.2808 0.3253 0.2640 -0.0331 -0.0087 0.0089  472 ARG A CA  
3783 C C   . ARG A 472 ? 0.2956 0.3559 0.2895 -0.0361 -0.0089 0.0076  472 ARG A C   
3784 O O   . ARG A 472 ? 0.2700 0.3366 0.2664 -0.0308 -0.0092 0.0033  472 ARG A O   
3785 C CB  . ARG A 472 ? 0.2879 0.3399 0.2695 -0.0316 -0.0037 0.0137  472 ARG A CB  
3786 C CG  . ARG A 472 ? 0.3114 0.3507 0.2823 -0.0275 -0.0049 0.0161  472 ARG A CG  
3787 C CD  . ARG A 472 ? 0.2919 0.3390 0.2574 -0.0260 -0.0007 0.0194  472 ARG A CD  
3788 N NE  . ARG A 472 ? 0.3296 0.3655 0.2842 -0.0233 -0.0035 0.0236  472 ARG A NE  
3789 C CZ  . ARG A 472 ? 0.4034 0.4425 0.3485 -0.0219 -0.0021 0.0262  472 ARG A CZ  
3790 N NH1 . ARG A 472 ? 0.3508 0.4014 0.2944 -0.0221 0.0035  0.0238  472 ARG A NH1 
3791 N NH2 . ARG A 472 ? 0.4199 0.4494 0.3558 -0.0197 -0.0067 0.0313  472 ARG A NH2 
3792 N N   . PHE A 473 ? 0.2687 0.3361 0.2700 -0.0452 -0.0091 0.0124  473 PHE A N   
3793 C CA  . PHE A 473 ? 0.2633 0.3514 0.2788 -0.0467 -0.0086 0.0137  473 PHE A CA  
3794 C C   . PHE A 473 ? 0.3214 0.4241 0.3423 -0.0400 -0.0005 0.0158  473 PHE A C   
3795 O O   . PHE A 473 ? 0.2244 0.3284 0.2430 -0.0416 0.0050  0.0202  473 PHE A O   
3796 C CB  . PHE A 473 ? 0.2108 0.3062 0.2358 -0.0591 -0.0117 0.0193  473 PHE A CB  
3797 C CG  . PHE A 473 ? 0.2852 0.4052 0.3282 -0.0599 -0.0123 0.0222  473 PHE A CG  
3798 C CD1 . PHE A 473 ? 0.2423 0.3644 0.2869 -0.0589 -0.0190 0.0186  473 PHE A CD1 
3799 C CD2 . PHE A 473 ? 0.2310 0.3728 0.2895 -0.0604 -0.0054 0.0291  473 PHE A CD2 
3800 C CE1 . PHE A 473 ? 0.2189 0.3642 0.2812 -0.0585 -0.0206 0.0228  473 PHE A CE1 
3801 C CE2 . PHE A 473 ? 0.2112 0.3773 0.2893 -0.0591 -0.0056 0.0327  473 PHE A CE2 
3802 C CZ  . PHE A 473 ? 0.1958 0.3636 0.2763 -0.0580 -0.0140 0.0299  473 PHE A CZ  
3803 N N   . LEU A 474 ? 0.2362 0.3476 0.2620 -0.0326 0.0005  0.0126  474 LEU A N   
3804 C CA  . LEU A 474 ? 0.2627 0.3836 0.2909 -0.0251 0.0085  0.0127  474 LEU A CA  
3805 C C   . LEU A 474 ? 0.2744 0.4169 0.3210 -0.0253 0.0125  0.0176  474 LEU A C   
3806 O O   . LEU A 474 ? 0.2931 0.4447 0.3513 -0.0264 0.0071  0.0187  474 LEU A O   
3807 C CB  . LEU A 474 ? 0.2217 0.3364 0.2437 -0.0167 0.0077  0.0067  474 LEU A CB  
3808 C CG  . LEU A 474 ? 0.2455 0.3439 0.2538 -0.0157 0.0037  0.0026  474 LEU A CG  
3809 C CD1 . LEU A 474 ? 0.1967 0.2925 0.2012 -0.0091 0.0037  -0.0021 474 LEU A CD1 
3810 C CD2 . LEU A 474 ? 0.2598 0.3508 0.2580 -0.0170 0.0061  0.0046  474 LEU A CD2 
3811 N N   . ARG A 475 ? 0.2589 0.4105 0.3082 -0.0238 0.0219  0.0211  475 ARG A N   
3812 C CA  . ARG A 475 ? 0.2332 0.4078 0.3017 -0.0208 0.0285  0.0258  475 ARG A CA  
3813 C C   . ARG A 475 ? 0.2623 0.4362 0.3278 -0.0077 0.0359  0.0211  475 ARG A C   
3814 O O   . ARG A 475 ? 0.2567 0.4139 0.3033 -0.0036 0.0382  0.0153  475 ARG A O   
3815 C CB  . ARG A 475 ? 0.1894 0.3757 0.2631 -0.0272 0.0364  0.0330  475 ARG A CB  
3816 C CG  . ARG A 475 ? 0.3080 0.4965 0.3887 -0.0416 0.0283  0.0387  475 ARG A CG  
3817 C CD  . ARG A 475 ? 0.3396 0.5344 0.4215 -0.0508 0.0350  0.0465  475 ARG A CD  
3818 N NE  . ARG A 475 ? 0.5290 0.7063 0.6015 -0.0633 0.0260  0.0483  475 ARG A NE  
3819 C CZ  . ARG A 475 ? 0.6270 0.8099 0.7111 -0.0764 0.0185  0.0533  475 ARG A CZ  
3820 N NH1 . ARG A 475 ? 0.4861 0.6967 0.5950 -0.0799 0.0181  0.0588  475 ARG A NH1 
3821 N NH2 . ARG A 475 ? 0.5846 0.7443 0.6552 -0.0863 0.0108  0.0531  475 ARG A NH2 
3822 N N   . ARG A 476 ? 0.2195 0.4107 0.3040 -0.0013 0.0385  0.0239  476 ARG A N   
3823 C CA  . ARG A 476 ? 0.2523 0.4412 0.3349 0.0121  0.0468  0.0198  476 ARG A CA  
3824 C C   . ARG A 476 ? 0.2590 0.4429 0.3275 0.0156  0.0598  0.0173  476 ARG A C   
3825 O O   . ARG A 476 ? 0.3195 0.5152 0.3920 0.0103  0.0662  0.0226  476 ARG A O   
3826 C CB  . ARG A 476 ? 0.1798 0.3919 0.2890 0.0192  0.0494  0.0257  476 ARG A CB  
3827 C CG  . ARG A 476 ? 0.2279 0.4337 0.3359 0.0344  0.0565  0.0215  476 ARG A CG  
3828 C CD  . ARG A 476 ? 0.2015 0.4328 0.3393 0.0431  0.0594  0.0291  476 ARG A CD  
3829 N NE  . ARG A 476 ? 0.2182 0.4738 0.3726 0.0453  0.0723  0.0350  476 ARG A NE  
3830 C CZ  . ARG A 476 ? 0.2511 0.5341 0.4282 0.0360  0.0699  0.0446  476 ARG A CZ  
3831 N NH1 . ARG A 476 ? 0.1750 0.4619 0.3579 0.0231  0.0543  0.0486  476 ARG A NH1 
3832 N NH2 . ARG A 476 ? 0.1944 0.5013 0.3880 0.0393  0.0838  0.0504  476 ARG A NH2 
3833 N N   . ARG A 477 ? 0.3007 0.4663 0.3510 0.0235  0.0636  0.0094  477 ARG A N   
3834 C CA  A ARG A 477 ? 0.3911 0.5506 0.4249 0.0276  0.0763  0.0060  477 ARG A CA  
3835 C CA  B ARG A 477 ? 0.3906 0.5498 0.4242 0.0279  0.0763  0.0059  477 ARG A CA  
3836 C C   . ARG A 477 ? 0.3549 0.5358 0.4068 0.0360  0.0903  0.0103  477 ARG A C   
3837 O O   . ARG A 477 ? 0.5475 0.7353 0.6151 0.0463  0.0926  0.0104  477 ARG A O   
3838 C CB  A ARG A 477 ? 0.4352 0.5696 0.4456 0.0335  0.0762  -0.0038 477 ARG A CB  
3839 C CB  B ARG A 477 ? 0.4342 0.5687 0.4454 0.0343  0.0763  -0.0040 477 ARG A CB  
3840 C CG  A ARG A 477 ? 0.4647 0.5959 0.4831 0.0454  0.0790  -0.0071 477 ARG A CG  
3841 C CG  B ARG A 477 ? 0.5958 0.7183 0.5824 0.0371  0.0878  -0.0093 477 ARG A CG  
3842 C CD  A ARG A 477 ? 0.6002 0.7040 0.5920 0.0497  0.0809  -0.0172 477 ARG A CD  
3843 C CD  B ARG A 477 ? 0.6142 0.7122 0.5806 0.0439  0.0883  -0.0194 477 ARG A CD  
3844 N NE  A ARG A 477 ? 0.6676 0.7640 0.6650 0.0618  0.0848  -0.0203 477 ARG A NE  
3845 N NE  B ARG A 477 ? 0.7174 0.8176 0.6982 0.0564  0.0944  -0.0208 477 ARG A NE  
3846 C CZ  A ARG A 477 ? 0.6760 0.7771 0.6794 0.0743  0.0989  -0.0210 477 ARG A CZ  
3847 C CZ  B ARG A 477 ? 0.6785 0.7701 0.6656 0.0593  0.0860  -0.0223 477 ARG A CZ  
3848 N NH1 A ARG A 477 ? 0.6391 0.7550 0.6444 0.0759  0.1115  -0.0187 477 ARG A NH1 
3849 N NH1 B ARG A 477 ? 0.6662 0.7472 0.6463 0.0507  0.0724  -0.0236 477 ARG A NH1 
3850 N NH2 A ARG A 477 ? 0.6288 0.7194 0.6367 0.0860  0.1011  -0.0235 477 ARG A NH2 
3851 N NH2 B ARG A 477 ? 0.6891 0.7834 0.6905 0.0718  0.0920  -0.0218 477 ARG A NH2 
3852 N N   . MET A 478 ? 0.5413 0.7338 0.5923 0.0318  0.1002  0.0148  478 MET A N   
3853 C CA  . MET A 478 ? 0.7571 0.9747 0.8283 0.0394  0.1153  0.0202  478 MET A CA  
3854 C C   . MET A 478 ? 0.8353 1.0397 0.8856 0.0515  0.1314  0.0121  478 MET A C   
3855 O O   . MET A 478 ? 1.0172 1.2044 1.0379 0.0472  0.1351  0.0076  478 MET A O   
3856 C CB  . MET A 478 ? 0.7217 0.9609 0.8044 0.0276  0.1191  0.0304  478 MET A CB  
3857 C CG  . MET A 478 ? 0.7531 1.0003 0.8516 0.0137  0.1028  0.0374  478 MET A CG  
3858 S SD  . MET A 478 ? 0.7328 1.0130 0.8740 0.0146  0.0970  0.0464  478 MET A SD  
3859 C CE  . MET A 478 ? 0.2041 0.4701 0.3412 0.0000  0.0744  0.0463  478 MET A CE  
3860 N N   . ASP A 479 ? 0.9458 1.1570 1.0104 0.0669  0.1404  0.0104  479 ASP A N   
3861 C CA  . ASP A 479 ? 1.0761 1.2717 1.1214 0.0811  0.1566  0.0013  479 ASP A CA  
3862 C C   . ASP A 479 ? 1.1426 1.3054 1.1440 0.0758  0.1564  -0.0090 479 ASP A C   
3863 O O   . ASP A 479 ? 0.9707 1.1117 0.9487 0.0856  0.1662  -0.0191 479 ASP A O   
3864 C CB  . ASP A 479 ? 0.8194 1.0423 0.8809 0.0890  0.1774  0.0069  479 ASP A CB  
3865 C CG  . ASP A 479 ? 1.1034 1.3140 1.1546 0.1087  0.1952  -0.0019 479 ASP A CG  
3866 O OD1 . ASP A 479 ? 1.1262 1.3320 1.1914 0.1210  0.1923  -0.0039 479 ASP A OD1 
3867 O OD2 . ASP A 479 ? 1.1402 1.3401 1.1678 0.1088  0.2078  -0.0080 479 ASP A OD2 
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