data_9IZL
# 
_entry.id   9IZL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9IZL         pdb_00009izl 10.2210/pdb9izl/pdb 
WWPDB D_1300050048 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-11 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IZL 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              15651628766@163.com 
_pdbx_contact_author.name_first         Tao 
_pdbx_contact_author.name_last          Xie 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6615-4219 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fan, S.'  1 0000-0001-9272-2438 
'Zhen, L.' 2 0000-0002-1854-0764 
'Xie, T.'  3 0000-0002-6615-4219 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                20372 
_citation.page_last                 20398 
_citation.title                     
'Discovery of Thiazole Carboxamides as Novel Vanin-1 Inhibitors for Inflammatory Bowel Disease Treatment.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01838 
_citation.pdbx_database_id_PubMed   39514323 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xie, T.'   1 ? 
primary 'Cao, G.Y.' 2 ? 
primary 'Zhang, S.' 3 ? 
primary 'Li, M.K.'  4 ? 
primary 'Jin, X.'   5 ? 
primary 'Liu, L.'   6 ? 
primary 'Wang, G.'  7 ? 
primary 'Zhen, L.'  8 ? 
# 
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 Pantetheinase                                                                                       51585.840 2 
3.5.1.92 ? ? ? 
2 non-polymer syn '8-oxa-2-azaspiro[4.5]decan-2-yl-[2-[(3~{S})-3-oxidanylpyrrolidin-1-yl]-1,3-thiazol-5-yl]methanone' 337.437   2 
?        ? ? ? 
3 water       nat water                                                                                               18.015    
130 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Pantetheine hydrolase,Tiff66,Vascular non-inflammatory molecule 1,Vanin-1' 
# 
_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       
;QDTFIAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPD
PEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNL
FMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVN
FLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDE
FTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTR
FEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QDTFIAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPD
PEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNL
FMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVN
FLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDE
FTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTR
FEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKD
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '8-oxa-2-azaspiro[4.5]decan-2-yl-[2-[(3~{S})-3-oxidanylpyrrolidin-1-yl]-1,3-thiazol-5-yl]methanone' A1EAG 
3 water                                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   ASP n 
1 3   THR n 
1 4   PHE n 
1 5   ILE n 
1 6   ALA n 
1 7   ALA n 
1 8   VAL n 
1 9   TYR n 
1 10  GLU n 
1 11  HIS n 
1 12  ALA n 
1 13  ALA n 
1 14  ILE n 
1 15  LEU n 
1 16  PRO n 
1 17  ASN n 
1 18  ALA n 
1 19  THR n 
1 20  LEU n 
1 21  THR n 
1 22  PRO n 
1 23  VAL n 
1 24  SER n 
1 25  ARG n 
1 26  GLU n 
1 27  GLU n 
1 28  ALA n 
1 29  LEU n 
1 30  ALA n 
1 31  LEU n 
1 32  MET n 
1 33  ASN n 
1 34  ARG n 
1 35  ASN n 
1 36  LEU n 
1 37  ASP n 
1 38  ILE n 
1 39  LEU n 
1 40  GLU n 
1 41  GLY n 
1 42  ALA n 
1 43  ILE n 
1 44  THR n 
1 45  SER n 
1 46  ALA n 
1 47  ALA n 
1 48  ASP n 
1 49  GLN n 
1 50  GLY n 
1 51  ALA n 
1 52  HIS n 
1 53  ILE n 
1 54  ILE n 
1 55  VAL n 
1 56  THR n 
1 57  PRO n 
1 58  GLU n 
1 59  ASP n 
1 60  ALA n 
1 61  ILE n 
1 62  TYR n 
1 63  GLY n 
1 64  TRP n 
1 65  ASN n 
1 66  PHE n 
1 67  ASN n 
1 68  ARG n 
1 69  ASP n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  PRO n 
1 74  TYR n 
1 75  LEU n 
1 76  GLU n 
1 77  ASP n 
1 78  ILE n 
1 79  PRO n 
1 80  ASP n 
1 81  PRO n 
1 82  GLU n 
1 83  VAL n 
1 84  ASN n 
1 85  TRP n 
1 86  ILE n 
1 87  PRO n 
1 88  CYS n 
1 89  ASN n 
1 90  ASN n 
1 91  ARG n 
1 92  ASN n 
1 93  ARG n 
1 94  PHE n 
1 95  GLY n 
1 96  GLN n 
1 97  THR n 
1 98  PRO n 
1 99  VAL n 
1 100 GLN n 
1 101 GLU n 
1 102 ARG n 
1 103 LEU n 
1 104 SER n 
1 105 CYS n 
1 106 LEU n 
1 107 ALA n 
1 108 LYS n 
1 109 ASN n 
1 110 ASN n 
1 111 SER n 
1 112 ILE n 
1 113 TYR n 
1 114 VAL n 
1 115 VAL n 
1 116 ALA n 
1 117 ASN n 
1 118 ILE n 
1 119 GLY n 
1 120 ASP n 
1 121 LYS n 
1 122 LYS n 
1 123 PRO n 
1 124 CYS n 
1 125 ASP n 
1 126 THR n 
1 127 SER n 
1 128 ASP n 
1 129 PRO n 
1 130 GLN n 
1 131 CYS n 
1 132 PRO n 
1 133 PRO n 
1 134 ASP n 
1 135 GLY n 
1 136 ARG n 
1 137 TYR n 
1 138 GLN n 
1 139 TYR n 
1 140 ASN n 
1 141 THR n 
1 142 ASP n 
1 143 VAL n 
1 144 VAL n 
1 145 PHE n 
1 146 ASP n 
1 147 SER n 
1 148 GLN n 
1 149 GLY n 
1 150 LYS n 
1 151 LEU n 
1 152 VAL n 
1 153 ALA n 
1 154 ARG n 
1 155 TYR n 
1 156 HIS n 
1 157 LYS n 
1 158 GLN n 
1 159 ASN n 
1 160 LEU n 
1 161 PHE n 
1 162 MET n 
1 163 GLY n 
1 164 GLU n 
1 165 ASN n 
1 166 GLN n 
1 167 PHE n 
1 168 ASN n 
1 169 VAL n 
1 170 PRO n 
1 171 LYS n 
1 172 GLU n 
1 173 PRO n 
1 174 GLU n 
1 175 ILE n 
1 176 VAL n 
1 177 THR n 
1 178 PHE n 
1 179 ASN n 
1 180 THR n 
1 181 THR n 
1 182 PHE n 
1 183 GLY n 
1 184 SER n 
1 185 PHE n 
1 186 GLY n 
1 187 ILE n 
1 188 PHE n 
1 189 THR n 
1 190 CYS n 
1 191 PHE n 
1 192 ASP n 
1 193 ILE n 
1 194 LEU n 
1 195 PHE n 
1 196 HIS n 
1 197 ASP n 
1 198 PRO n 
1 199 ALA n 
1 200 VAL n 
1 201 THR n 
1 202 LEU n 
1 203 VAL n 
1 204 LYS n 
1 205 ASP n 
1 206 PHE n 
1 207 HIS n 
1 208 VAL n 
1 209 ASP n 
1 210 THR n 
1 211 ILE n 
1 212 VAL n 
1 213 PHE n 
1 214 PRO n 
1 215 THR n 
1 216 ALA n 
1 217 TRP n 
1 218 MET n 
1 219 ASN n 
1 220 VAL n 
1 221 LEU n 
1 222 PRO n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ALA n 
1 227 VAL n 
1 228 GLU n 
1 229 PHE n 
1 230 HIS n 
1 231 SER n 
1 232 ALA n 
1 233 TRP n 
1 234 ALA n 
1 235 MET n 
1 236 GLY n 
1 237 MET n 
1 238 ARG n 
1 239 VAL n 
1 240 ASN n 
1 241 PHE n 
1 242 LEU n 
1 243 ALA n 
1 244 SER n 
1 245 ASN n 
1 246 ILE n 
1 247 HIS n 
1 248 TYR n 
1 249 PRO n 
1 250 SER n 
1 251 LYS n 
1 252 LYS n 
1 253 MET n 
1 254 THR n 
1 255 GLY n 
1 256 SER n 
1 257 GLY n 
1 258 ILE n 
1 259 TYR n 
1 260 ALA n 
1 261 PRO n 
1 262 ASN n 
1 263 SER n 
1 264 SER n 
1 265 ARG n 
1 266 ALA n 
1 267 PHE n 
1 268 HIS n 
1 269 TYR n 
1 270 ASP n 
1 271 MET n 
1 272 LYS n 
1 273 THR n 
1 274 GLU n 
1 275 GLU n 
1 276 GLY n 
1 277 LYS n 
1 278 LEU n 
1 279 LEU n 
1 280 LEU n 
1 281 SER n 
1 282 GLN n 
1 283 LEU n 
1 284 ASP n 
1 285 SER n 
1 286 HIS n 
1 287 PRO n 
1 288 SER n 
1 289 HIS n 
1 290 SER n 
1 291 ALA n 
1 292 VAL n 
1 293 VAL n 
1 294 ASN n 
1 295 TRP n 
1 296 THR n 
1 297 SER n 
1 298 TYR n 
1 299 ALA n 
1 300 SER n 
1 301 SER n 
1 302 ILE n 
1 303 GLU n 
1 304 ALA n 
1 305 LEU n 
1 306 SER n 
1 307 SER n 
1 308 GLY n 
1 309 ASN n 
1 310 LYS n 
1 311 GLU n 
1 312 PHE n 
1 313 LYS n 
1 314 GLY n 
1 315 THR n 
1 316 VAL n 
1 317 PHE n 
1 318 PHE n 
1 319 ASP n 
1 320 GLU n 
1 321 PHE n 
1 322 THR n 
1 323 PHE n 
1 324 VAL n 
1 325 LYS n 
1 326 LEU n 
1 327 THR n 
1 328 GLY n 
1 329 VAL n 
1 330 ALA n 
1 331 GLY n 
1 332 ASN n 
1 333 TYR n 
1 334 THR n 
1 335 VAL n 
1 336 CYS n 
1 337 GLN n 
1 338 LYS n 
1 339 ASP n 
1 340 LEU n 
1 341 CYS n 
1 342 CYS n 
1 343 HIS n 
1 344 LEU n 
1 345 SER n 
1 346 TYR n 
1 347 LYS n 
1 348 MET n 
1 349 SER n 
1 350 GLU n 
1 351 ASN n 
1 352 ILE n 
1 353 PRO n 
1 354 ASN n 
1 355 GLU n 
1 356 VAL n 
1 357 TYR n 
1 358 ALA n 
1 359 LEU n 
1 360 GLY n 
1 361 ALA n 
1 362 PHE n 
1 363 ASP n 
1 364 GLY n 
1 365 LEU n 
1 366 HIS n 
1 367 THR n 
1 368 VAL n 
1 369 GLU n 
1 370 GLY n 
1 371 ARG n 
1 372 TYR n 
1 373 TYR n 
1 374 LEU n 
1 375 GLN n 
1 376 ILE n 
1 377 CYS n 
1 378 THR n 
1 379 LEU n 
1 380 LEU n 
1 381 LYS n 
1 382 CYS n 
1 383 LYS n 
1 384 THR n 
1 385 THR n 
1 386 ASN n 
1 387 LEU n 
1 388 ASN n 
1 389 THR n 
1 390 CYS n 
1 391 GLY n 
1 392 ASP n 
1 393 SER n 
1 394 ALA n 
1 395 GLU n 
1 396 THR n 
1 397 ALA n 
1 398 SER n 
1 399 THR n 
1 400 ARG n 
1 401 PHE n 
1 402 GLU n 
1 403 MET n 
1 404 PHE n 
1 405 SER n 
1 406 LEU n 
1 407 SER n 
1 408 GLY n 
1 409 THR n 
1 410 PHE n 
1 411 GLY n 
1 412 THR n 
1 413 GLN n 
1 414 TYR n 
1 415 VAL n 
1 416 PHE n 
1 417 PRO n 
1 418 GLU n 
1 419 VAL n 
1 420 LEU n 
1 421 LEU n 
1 422 SER n 
1 423 GLU n 
1 424 ASN n 
1 425 GLN n 
1 426 LEU n 
1 427 ALA n 
1 428 PRO n 
1 429 GLY n 
1 430 GLU n 
1 431 PHE n 
1 432 GLN n 
1 433 VAL n 
1 434 SER n 
1 435 THR n 
1 436 ASP n 
1 437 GLY n 
1 438 ARG n 
1 439 LEU n 
1 440 PHE n 
1 441 SER n 
1 442 LEU n 
1 443 LYS n 
1 444 PRO n 
1 445 THR n 
1 446 SER n 
1 447 GLY n 
1 448 PRO n 
1 449 VAL n 
1 450 LEU n 
1 451 THR n 
1 452 VAL n 
1 453 THR n 
1 454 LEU n 
1 455 PHE n 
1 456 GLY n 
1 457 ARG n 
1 458 LEU n 
1 459 TYR n 
1 460 GLU n 
1 461 LYS n 
1 462 ASP 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                   462 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 VNN1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EAG non-polymer         . '8-oxa-2-azaspiro[4.5]decan-2-yl-[2-[(3~{S})-3-oxidanylpyrrolidin-1-yl]-1,3-thiazol-5-yl]methanone' ? 
'C16 H23 N3 O3 S' 337.437 
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 
GLN   'L-peptide linking' y GLUTAMINE                                                                                           ? 
'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                     ? 
'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                                             ? 
'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                           ? 
'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                                                               ? 
'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                          ? 
'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                             ? 
'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                              ? 
'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                          ? 
'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                       ? 
'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                             ? 
'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                              ? 
'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                           ? 
'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                          ? 
'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                            ? 
'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                              ? 
'C5 H11 N O2'     117.146 
# 
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   GLN 1   1   1   GLN GLN A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TRP 64  64  64  TRP TRP A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  TRP 85  85  85  TRP TRP A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 CYS 105 105 105 CYS CYS A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 CYS 124 124 124 CYS CYS A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 CYS 131 131 131 CYS CYS A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 HIS 156 156 156 HIS HIS A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASN 179 179 179 ASN ASN A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 ILE 193 193 193 ILE ILE A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 ASP 209 209 209 ASP ASP A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 THR 215 215 215 THR THR A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 TRP 217 217 217 TRP TRP A . n 
A 1 218 MET 218 218 218 MET MET A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 TRP 233 233 233 TRP TRP A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 MET 237 237 237 MET MET A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 ASN 240 240 240 ASN ASN A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 TYR 248 248 248 TYR TYR A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 MET 253 253 253 MET MET A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 TYR 259 259 259 TYR TYR A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 MET 271 271 271 MET MET A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 HIS 286 286 286 HIS HIS A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 VAL 292 292 292 VAL VAL A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 TRP 295 295 295 TRP TRP A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 ASN 309 309 309 ASN ASN A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 ASP 319 319 319 ASP ASP A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 THR 322 322 322 THR THR A . n 
A 1 323 PHE 323 323 323 PHE PHE A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 GLY 328 328 328 GLY GLY A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 CYS 336 336 336 CYS CYS A . n 
A 1 337 GLN 337 337 337 GLN GLN A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 CYS 341 341 341 CYS CYS A . n 
A 1 342 CYS 342 342 342 CYS CYS A . n 
A 1 343 HIS 343 343 343 HIS HIS A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 TYR 346 346 346 TYR TYR A . n 
A 1 347 LYS 347 347 347 LYS LYS A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 SER 349 349 349 SER SER A . n 
A 1 350 GLU 350 350 350 GLU GLU A . n 
A 1 351 ASN 351 351 351 ASN ASN A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 PRO 353 353 353 PRO PRO A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 GLU 355 355 355 GLU GLU A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 PHE 362 362 362 PHE PHE A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 HIS 366 366 366 HIS HIS A . n 
A 1 367 THR 367 367 367 THR THR A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 ARG 371 371 371 ARG ARG A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 GLN 375 375 375 GLN GLN A . n 
A 1 376 ILE 376 376 376 ILE ILE A . n 
A 1 377 CYS 377 377 377 CYS CYS A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 CYS 382 382 382 CYS CYS A . n 
A 1 383 LYS 383 383 383 LYS LYS A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 ASN 386 386 386 ASN ASN A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 THR 389 389 389 THR THR A . n 
A 1 390 CYS 390 390 390 CYS CYS A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 GLU 395 395 395 GLU GLU 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 SER 398 398 398 SER SER A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 ARG 400 400 400 ARG ARG A . n 
A 1 401 PHE 401 401 401 PHE PHE A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 MET 403 403 403 MET MET A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 PHE 410 410 410 PHE PHE A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 GLN 413 413 413 GLN GLN A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 VAL 415 415 415 VAL VAL A . n 
A 1 416 PHE 416 416 416 PHE PHE A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 GLU 418 418 418 GLU GLU A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 LEU 420 420 420 LEU LEU A . n 
A 1 421 LEU 421 421 421 LEU LEU A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 ASN 424 424 424 ASN ASN A . n 
A 1 425 GLN 425 425 425 GLN GLN A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 PRO 428 428 428 PRO PRO A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 GLU 430 430 430 GLU GLU A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 GLN 432 432 432 GLN GLN A . n 
A 1 433 VAL 433 433 433 VAL VAL A . n 
A 1 434 SER 434 434 434 SER SER A . n 
A 1 435 THR 435 435 435 THR THR A . n 
A 1 436 ASP 436 436 436 ASP ASP A . n 
A 1 437 GLY 437 437 437 GLY GLY A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 PHE 440 440 440 PHE PHE A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 PRO 444 444 444 PRO PRO A . n 
A 1 445 THR 445 445 445 THR THR A . n 
A 1 446 SER 446 446 446 SER SER A . n 
A 1 447 GLY 447 447 447 GLY GLY A . n 
A 1 448 PRO 448 448 448 PRO PRO A . n 
A 1 449 VAL 449 449 449 VAL VAL A . n 
A 1 450 LEU 450 450 450 LEU LEU A . n 
A 1 451 THR 451 451 451 THR THR A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 THR 453 453 453 THR THR A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 GLY 456 456 456 GLY GLY A . n 
A 1 457 ARG 457 457 457 ARG ARG A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 GLU 460 460 460 GLU GLU A . n 
A 1 461 LYS 461 461 461 LYS LYS A . n 
A 1 462 ASP 462 462 462 ASP ASP A . n 
B 1 1   GLN 1   1   1   GLN GLN B . n 
B 1 2   ASP 2   2   2   ASP ASP B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   PHE 4   4   4   PHE PHE B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  GLU 10  10  10  GLU GLU B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  ILE 14  14  14  ILE ILE B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  PRO 16  16  16  PRO PRO B . n 
B 1 17  ASN 17  17  17  ASN ASN B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  MET 32  32  32  MET MET B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  ILE 54  54  54  ILE ILE B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  THR 56  56  56  THR THR B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  ASP 59  59  59  ASP ASP B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  TRP 64  64  64  TRP TRP B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  TYR 74  74  74  TYR TYR B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  PRO 81  81  81  PRO PRO B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  TRP 85  85  85  TRP TRP B . n 
B 1 86  ILE 86  86  86  ILE ILE B . n 
B 1 87  PRO 87  87  87  PRO PRO B . n 
B 1 88  CYS 88  88  88  CYS CYS B . n 
B 1 89  ASN 89  89  89  ASN ASN B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  ASN 92  92  92  ASN ASN B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 GLU 101 101 101 GLU GLU B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 CYS 105 105 105 CYS CYS B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 ALA 107 107 107 ALA ALA B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 PRO 123 123 123 PRO PRO B . n 
B 1 124 CYS 124 124 124 CYS CYS B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 GLN 130 130 130 GLN GLN B . n 
B 1 131 CYS 131 131 131 CYS CYS B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 TYR 139 139 139 TYR TYR B . n 
B 1 140 ASN 140 140 140 ASN ASN B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 PHE 145 145 145 PHE PHE B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 GLN 148 148 148 GLN GLN B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 LYS 150 150 150 LYS LYS B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 ARG 154 154 154 ARG ARG B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 HIS 156 156 156 HIS HIS B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 ASN 165 165 165 ASN ASN B . n 
B 1 166 GLN 166 166 166 GLN GLN B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 ASN 168 168 168 ASN ASN B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 PRO 173 173 173 PRO PRO B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 ILE 175 175 175 ILE ILE B . n 
B 1 176 VAL 176 176 176 VAL VAL B . n 
B 1 177 THR 177 177 177 THR THR B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 ASN 179 179 179 ASN ASN B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 THR 181 181 181 THR THR B . n 
B 1 182 PHE 182 182 182 PHE PHE B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 PHE 188 188 188 PHE PHE B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 CYS 190 190 190 CYS CYS B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 ILE 193 193 193 ILE ILE B . n 
B 1 194 LEU 194 194 194 LEU LEU B . n 
B 1 195 PHE 195 195 195 PHE PHE B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 VAL 200 200 200 VAL VAL B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 PHE 206 206 206 PHE PHE B . n 
B 1 207 HIS 207 207 207 HIS HIS B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 ASP 209 209 209 ASP ASP B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 THR 215 215 215 THR THR B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 TRP 217 217 217 TRP TRP B . n 
B 1 218 MET 218 218 218 MET MET B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 VAL 220 220 220 VAL VAL B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 HIS 223 223 223 HIS HIS B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 ALA 226 226 226 ALA ALA B . n 
B 1 227 VAL 227 227 227 VAL VAL B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 PHE 229 229 229 PHE PHE B . n 
B 1 230 HIS 230 230 230 HIS HIS B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 TRP 233 233 233 TRP TRP B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 MET 237 237 237 MET MET B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 ASN 240 240 240 ASN ASN B . n 
B 1 241 PHE 241 241 241 PHE PHE B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 HIS 247 247 247 HIS HIS B . n 
B 1 248 TYR 248 248 248 TYR TYR B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 SER 250 250 250 SER SER B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 MET 253 253 253 MET MET B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 GLY 257 257 257 GLY GLY B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 TYR 259 259 259 TYR TYR B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 PRO 261 261 261 PRO PRO B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 SER 263 263 263 SER SER B . n 
B 1 264 SER 264 264 264 SER SER B . n 
B 1 265 ARG 265 265 265 ARG ARG B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 PHE 267 267 267 PHE PHE B . n 
B 1 268 HIS 268 268 268 HIS HIS B . n 
B 1 269 TYR 269 269 269 TYR TYR B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 MET 271 271 271 MET MET B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 THR 273 273 273 THR THR B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 GLU 275 275 275 GLU GLU B . n 
B 1 276 GLY 276 276 276 GLY GLY B . n 
B 1 277 LYS 277 277 277 LYS LYS B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 LEU 279 279 279 LEU LEU B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 SER 281 281 281 SER SER B . n 
B 1 282 GLN 282 282 282 GLN GLN B . n 
B 1 283 LEU 283 283 283 LEU LEU B . n 
B 1 284 ASP 284 284 284 ASP ASP B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 HIS 286 286 286 HIS HIS B . n 
B 1 287 PRO 287 287 287 PRO PRO B . n 
B 1 288 SER 288 288 288 SER SER B . n 
B 1 289 HIS 289 289 289 HIS HIS B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 VAL 292 292 292 VAL VAL B . n 
B 1 293 VAL 293 293 293 VAL VAL B . n 
B 1 294 ASN 294 294 294 ASN ASN B . n 
B 1 295 TRP 295 295 295 TRP TRP B . n 
B 1 296 THR 296 296 296 THR THR B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 TYR 298 298 298 TYR TYR B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 GLU 303 303 303 GLU GLU B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 LEU 305 305 305 LEU LEU B . n 
B 1 306 SER 306 306 306 SER SER B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 GLY 308 308 308 GLY GLY B . n 
B 1 309 ASN 309 309 309 ASN ASN B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 PHE 312 312 312 PHE PHE B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 GLY 314 314 314 GLY GLY B . n 
B 1 315 THR 315 315 315 THR THR B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 PHE 318 318 318 PHE PHE B . n 
B 1 319 ASP 319 319 319 ASP ASP B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 PHE 321 321 321 PHE PHE B . n 
B 1 322 THR 322 322 322 THR THR B . n 
B 1 323 PHE 323 323 323 PHE PHE B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 LEU 326 326 326 LEU LEU B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 GLY 328 328 328 GLY GLY B . n 
B 1 329 VAL 329 329 329 VAL VAL B . n 
B 1 330 ALA 330 330 330 ALA ALA B . n 
B 1 331 GLY 331 331 331 GLY GLY B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 TYR 333 333 333 TYR TYR B . n 
B 1 334 THR 334 334 334 THR THR B . n 
B 1 335 VAL 335 335 335 VAL VAL B . n 
B 1 336 CYS 336 336 336 CYS CYS B . n 
B 1 337 GLN 337 337 337 GLN GLN B . n 
B 1 338 LYS 338 338 338 LYS LYS B . n 
B 1 339 ASP 339 339 339 ASP ASP B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 CYS 341 341 341 CYS CYS B . n 
B 1 342 CYS 342 342 342 CYS CYS B . n 
B 1 343 HIS 343 343 343 HIS HIS B . n 
B 1 344 LEU 344 344 344 LEU LEU B . n 
B 1 345 SER 345 345 345 SER SER B . n 
B 1 346 TYR 346 346 346 TYR TYR B . n 
B 1 347 LYS 347 347 347 LYS LYS B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 SER 349 349 349 SER SER B . n 
B 1 350 GLU 350 350 350 GLU GLU B . n 
B 1 351 ASN 351 351 351 ASN ASN B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 PRO 353 353 353 PRO PRO B . n 
B 1 354 ASN 354 354 354 ASN ASN B . n 
B 1 355 GLU 355 355 355 GLU GLU B . n 
B 1 356 VAL 356 356 356 VAL VAL B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 ALA 358 358 358 ALA ALA B . n 
B 1 359 LEU 359 359 359 LEU LEU B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 ALA 361 361 361 ALA ALA B . n 
B 1 362 PHE 362 362 362 PHE PHE B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 LEU 365 365 365 LEU LEU B . n 
B 1 366 HIS 366 366 366 HIS HIS B . n 
B 1 367 THR 367 367 367 THR THR B . n 
B 1 368 VAL 368 368 368 VAL VAL B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 GLY 370 370 370 GLY GLY B . n 
B 1 371 ARG 371 371 371 ARG ARG B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 TYR 373 373 373 TYR TYR B . n 
B 1 374 LEU 374 374 374 LEU LEU B . n 
B 1 375 GLN 375 375 375 GLN GLN B . n 
B 1 376 ILE 376 376 376 ILE ILE B . n 
B 1 377 CYS 377 377 377 CYS CYS B . n 
B 1 378 THR 378 378 378 THR THR B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 LEU 380 380 380 LEU LEU B . n 
B 1 381 LYS 381 381 381 LYS LYS B . n 
B 1 382 CYS 382 382 382 CYS CYS B . n 
B 1 383 LYS 383 383 383 LYS LYS B . n 
B 1 384 THR 384 384 384 THR THR B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 ASN 386 386 386 ASN ASN B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 ASN 388 388 388 ASN ASN B . n 
B 1 389 THR 389 389 389 THR THR B . n 
B 1 390 CYS 390 390 390 CYS CYS B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 ASP 392 392 392 ASP ASP B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 ALA 394 394 394 ALA ALA B . n 
B 1 395 GLU 395 395 395 GLU GLU B . n 
B 1 396 THR 396 396 396 THR THR B . n 
B 1 397 ALA 397 397 397 ALA ALA B . n 
B 1 398 SER 398 398 398 SER SER B . n 
B 1 399 THR 399 399 399 THR THR B . n 
B 1 400 ARG 400 400 400 ARG ARG B . n 
B 1 401 PHE 401 401 401 PHE PHE B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 MET 403 403 403 MET MET B . n 
B 1 404 PHE 404 404 404 PHE PHE B . n 
B 1 405 SER 405 405 405 SER SER B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 SER 407 407 407 SER SER B . n 
B 1 408 GLY 408 408 408 GLY GLY B . n 
B 1 409 THR 409 409 409 THR THR B . n 
B 1 410 PHE 410 410 410 PHE PHE B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 THR 412 412 412 THR THR B . n 
B 1 413 GLN 413 413 413 GLN GLN B . n 
B 1 414 TYR 414 414 414 TYR TYR B . n 
B 1 415 VAL 415 415 415 VAL VAL B . n 
B 1 416 PHE 416 416 416 PHE PHE B . n 
B 1 417 PRO 417 417 417 PRO PRO B . n 
B 1 418 GLU 418 418 418 GLU GLU B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 LEU 420 420 420 LEU LEU B . n 
B 1 421 LEU 421 421 421 LEU LEU B . n 
B 1 422 SER 422 422 422 SER SER B . n 
B 1 423 GLU 423 423 423 GLU GLU B . n 
B 1 424 ASN 424 424 424 ASN ASN B . n 
B 1 425 GLN 425 425 425 GLN GLN B . n 
B 1 426 LEU 426 426 426 LEU LEU B . n 
B 1 427 ALA 427 427 427 ALA ALA B . n 
B 1 428 PRO 428 428 428 PRO PRO B . n 
B 1 429 GLY 429 429 429 GLY GLY B . n 
B 1 430 GLU 430 430 430 GLU GLU B . n 
B 1 431 PHE 431 431 431 PHE PHE B . n 
B 1 432 GLN 432 432 432 GLN GLN B . n 
B 1 433 VAL 433 433 433 VAL VAL B . n 
B 1 434 SER 434 434 434 SER SER B . n 
B 1 435 THR 435 435 435 THR THR B . n 
B 1 436 ASP 436 436 436 ASP ASP B . n 
B 1 437 GLY 437 437 437 GLY GLY B . n 
B 1 438 ARG 438 438 438 ARG ARG B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 PHE 440 440 440 PHE PHE B . n 
B 1 441 SER 441 441 441 SER SER B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 LYS 443 443 443 LYS LYS B . n 
B 1 444 PRO 444 444 444 PRO PRO B . n 
B 1 445 THR 445 445 445 THR THR B . n 
B 1 446 SER 446 446 446 SER SER B . n 
B 1 447 GLY 447 447 447 GLY GLY B . n 
B 1 448 PRO 448 448 448 PRO PRO B . n 
B 1 449 VAL 449 449 449 VAL VAL B . n 
B 1 450 LEU 450 450 450 LEU LEU B . n 
B 1 451 THR 451 451 451 THR THR B . n 
B 1 452 VAL 452 452 452 VAL VAL B . n 
B 1 453 THR 453 453 453 THR THR B . n 
B 1 454 LEU 454 454 454 LEU LEU B . n 
B 1 455 PHE 455 455 455 PHE PHE B . n 
B 1 456 GLY 456 456 456 GLY GLY B . n 
B 1 457 ARG 457 457 457 ARG ARG B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 TYR 459 459 459 TYR TYR B . n 
B 1 460 GLU 460 460 460 GLU GLU B . n 
B 1 461 LYS 461 461 461 LYS LYS B . n 
B 1 462 ASP 462 462 462 ASP ASP B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EAG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EAG 
_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 
C 2 A1EAG 1  501 1   A1EAG LIG A . 
D 2 A1EAG 1  501 2   A1EAG LIG B . 
E 3 HOH   1  601 22  HOH   HOH A . 
E 3 HOH   2  602 19  HOH   HOH A . 
E 3 HOH   3  603 2   HOH   HOH A . 
E 3 HOH   4  604 11  HOH   HOH A . 
E 3 HOH   5  605 78  HOH   HOH A . 
E 3 HOH   6  606 39  HOH   HOH A . 
E 3 HOH   7  607 17  HOH   HOH A . 
E 3 HOH   8  608 65  HOH   HOH A . 
E 3 HOH   9  609 163 HOH   HOH A . 
E 3 HOH   10 610 63  HOH   HOH A . 
E 3 HOH   11 611 6   HOH   HOH A . 
E 3 HOH   12 612 24  HOH   HOH A . 
E 3 HOH   13 613 164 HOH   HOH A . 
E 3 HOH   14 614 86  HOH   HOH A . 
E 3 HOH   15 615 100 HOH   HOH A . 
E 3 HOH   16 616 36  HOH   HOH A . 
E 3 HOH   17 617 139 HOH   HOH A . 
E 3 HOH   18 618 69  HOH   HOH A . 
E 3 HOH   19 619 29  HOH   HOH A . 
E 3 HOH   20 620 45  HOH   HOH A . 
E 3 HOH   21 621 150 HOH   HOH A . 
E 3 HOH   22 622 31  HOH   HOH A . 
E 3 HOH   23 623 125 HOH   HOH A . 
E 3 HOH   24 624 88  HOH   HOH A . 
E 3 HOH   25 625 8   HOH   HOH A . 
E 3 HOH   26 626 33  HOH   HOH A . 
E 3 HOH   27 627 9   HOH   HOH A . 
E 3 HOH   28 628 73  HOH   HOH A . 
E 3 HOH   29 629 64  HOH   HOH A . 
E 3 HOH   30 630 53  HOH   HOH A . 
E 3 HOH   31 631 67  HOH   HOH A . 
E 3 HOH   32 632 44  HOH   HOH A . 
E 3 HOH   33 633 120 HOH   HOH A . 
E 3 HOH   34 634 26  HOH   HOH A . 
E 3 HOH   35 635 92  HOH   HOH A . 
E 3 HOH   36 636 137 HOH   HOH A . 
E 3 HOH   37 637 105 HOH   HOH A . 
E 3 HOH   38 638 62  HOH   HOH A . 
E 3 HOH   39 639 161 HOH   HOH A . 
E 3 HOH   40 640 160 HOH   HOH A . 
E 3 HOH   41 641 109 HOH   HOH A . 
E 3 HOH   42 642 83  HOH   HOH A . 
E 3 HOH   43 643 155 HOH   HOH A . 
E 3 HOH   44 644 71  HOH   HOH A . 
E 3 HOH   45 645 151 HOH   HOH A . 
E 3 HOH   46 646 116 HOH   HOH A . 
E 3 HOH   47 647 85  HOH   HOH A . 
E 3 HOH   48 648 50  HOH   HOH A . 
E 3 HOH   49 649 122 HOH   HOH A . 
E 3 HOH   50 650 101 HOH   HOH A . 
E 3 HOH   51 651 140 HOH   HOH A . 
E 3 HOH   52 652 51  HOH   HOH A . 
E 3 HOH   53 653 60  HOH   HOH A . 
E 3 HOH   54 654 136 HOH   HOH A . 
E 3 HOH   55 655 129 HOH   HOH A . 
F 3 HOH   1  601 66  HOH   HOH B . 
F 3 HOH   2  602 99  HOH   HOH B . 
F 3 HOH   3  603 35  HOH   HOH B . 
F 3 HOH   4  604 107 HOH   HOH B . 
F 3 HOH   5  605 32  HOH   HOH B . 
F 3 HOH   6  606 118 HOH   HOH B . 
F 3 HOH   7  607 1   HOH   HOH B . 
F 3 HOH   8  608 148 HOH   HOH B . 
F 3 HOH   9  609 21  HOH   HOH B . 
F 3 HOH   10 610 102 HOH   HOH B . 
F 3 HOH   11 611 25  HOH   HOH B . 
F 3 HOH   12 612 10  HOH   HOH B . 
F 3 HOH   13 613 141 HOH   HOH B . 
F 3 HOH   14 614 3   HOH   HOH B . 
F 3 HOH   15 615 90  HOH   HOH B . 
F 3 HOH   16 616 149 HOH   HOH B . 
F 3 HOH   17 617 147 HOH   HOH B . 
F 3 HOH   18 618 23  HOH   HOH B . 
F 3 HOH   19 619 93  HOH   HOH B . 
F 3 HOH   20 620 162 HOH   HOH B . 
F 3 HOH   21 621 27  HOH   HOH B . 
F 3 HOH   22 622 18  HOH   HOH B . 
F 3 HOH   23 623 126 HOH   HOH B . 
F 3 HOH   24 624 13  HOH   HOH B . 
F 3 HOH   25 625 132 HOH   HOH B . 
F 3 HOH   26 626 14  HOH   HOH B . 
F 3 HOH   27 627 56  HOH   HOH B . 
F 3 HOH   28 628 89  HOH   HOH B . 
F 3 HOH   29 629 52  HOH   HOH B . 
F 3 HOH   30 630 7   HOH   HOH B . 
F 3 HOH   31 631 98  HOH   HOH B . 
F 3 HOH   32 632 79  HOH   HOH B . 
F 3 HOH   33 633 42  HOH   HOH B . 
F 3 HOH   34 634 5   HOH   HOH B . 
F 3 HOH   35 635 117 HOH   HOH B . 
F 3 HOH   36 636 61  HOH   HOH B . 
F 3 HOH   37 637 47  HOH   HOH B . 
F 3 HOH   38 638 37  HOH   HOH B . 
F 3 HOH   39 639 108 HOH   HOH B . 
F 3 HOH   40 640 81  HOH   HOH B . 
F 3 HOH   41 641 15  HOH   HOH B . 
F 3 HOH   42 642 43  HOH   HOH B . 
F 3 HOH   43 643 82  HOH   HOH B . 
F 3 HOH   44 644 4   HOH   HOH B . 
F 3 HOH   45 645 28  HOH   HOH B . 
F 3 HOH   46 646 119 HOH   HOH B . 
F 3 HOH   47 647 41  HOH   HOH B . 
F 3 HOH   48 648 111 HOH   HOH B . 
F 3 HOH   49 649 103 HOH   HOH B . 
F 3 HOH   50 650 70  HOH   HOH B . 
F 3 HOH   51 651 40  HOH   HOH B . 
F 3 HOH   52 652 34  HOH   HOH B . 
F 3 HOH   53 653 124 HOH   HOH B . 
F 3 HOH   54 654 74  HOH   HOH B . 
F 3 HOH   55 655 143 HOH   HOH B . 
F 3 HOH   56 656 46  HOH   HOH B . 
F 3 HOH   57 657 84  HOH   HOH B . 
F 3 HOH   58 658 157 HOH   HOH B . 
F 3 HOH   59 659 77  HOH   HOH B . 
F 3 HOH   60 660 49  HOH   HOH B . 
F 3 HOH   61 661 58  HOH   HOH B . 
F 3 HOH   62 662 12  HOH   HOH B . 
F 3 HOH   63 663 96  HOH   HOH B . 
F 3 HOH   64 664 159 HOH   HOH B . 
F 3 HOH   65 665 104 HOH   HOH B . 
F 3 HOH   66 666 131 HOH   HOH B . 
F 3 HOH   67 667 59  HOH   HOH B . 
F 3 HOH   68 668 106 HOH   HOH B . 
F 3 HOH   69 669 48  HOH   HOH B . 
F 3 HOH   70 670 72  HOH   HOH B . 
F 3 HOH   71 671 142 HOH   HOH B . 
F 3 HOH   72 672 156 HOH   HOH B . 
F 3 HOH   73 673 114 HOH   HOH B . 
F 3 HOH   74 674 158 HOH   HOH B . 
F 3 HOH   75 675 153 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IZL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.823 
_cell.length_a_esd                 ? 
_cell.length_b                     92.980 
_cell.length_b_esd                 ? 
_cell.length_c                     218.923 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IZL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IZL 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.43 
_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 TMAO, 0.1 M Tris 8.5, 20% w/v PEG 2000 MME.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-20 
_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   0.9789 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9789 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IZL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.28 
_reflns.d_resolution_low                               50.00 
_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                                     53547 
_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                           95.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.787 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.174 
_reflns.pdbx_Rpim_I_all                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       583939 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.166 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_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 
_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 
2.28 2.32  ? ? ? ? ? ? 1820 ? ? ? ? ? ? ? ? ? ? ? 6.5  0.458 ? ? 0.930 0.307 ? 1  1 0.874 0.966 ? 67.1  ? 0.873 ? ? ? ? ? ? ? ? ? 
2.32 2.36  ? ? ? ? ? ? 2079 ? ? ? ? ? ? ? ? ? ? ? 6.8  0.452 ? ? 0.965 0.315 ? 2  1 0.879 0.967 ? 74.8  ? 0.907 ? ? ? ? ? ? ? ? ? 
2.36 2.41  ? ? ? ? ? ? 2312 ? ? ? ? ? ? ? ? ? ? ? 7.2  0.459 ? ? 1.060 0.345 ? 3  1 0.851 0.959 ? 84.1  ? 0.996 ? ? ? ? ? ? ? ? ? 
2.41 2.46  ? ? ? ? ? ? 2624 ? ? ? ? ? ? ? ? ? ? ? 7.5  0.464 ? ? 1.029 0.337 ? 4  1 0.840 0.955 ? 94.4  ? 0.965 ? ? ? ? ? ? ? ? ? 
2.46 2.51  ? ? ? ? ? ? 2722 ? ? ? ? ? ? ? ? ? ? ? 8.9  0.456 ? ? 1.146 0.363 ? 5  1 0.886 0.969 ? 99.1  ? 1.083 ? ? ? ? ? ? ? ? ? 
2.51 2.57  ? ? ? ? ? ? 2783 ? ? ? ? ? ? ? ? ? ? ? 10.9 0.440 ? ? 1.223 0.360 ? 6  1 0.914 0.977 ? 100.0 ? 1.167 ? ? ? ? ? ? ? ? ? 
2.57 2.63  ? ? ? ? ? ? 2736 ? ? ? ? ? ? ? ? ? ? ? 12.3 0.471 ? ? 1.064 0.299 ? 7  1 0.950 0.987 ? 100.0 ? 1.020 ? ? ? ? ? ? ? ? ? 
2.63 2.70  ? ? ? ? ? ? 2781 ? ? ? ? ? ? ? ? ? ? ? 12.7 0.476 ? ? 0.952 0.263 ? 8  1 0.947 0.986 ? 100.0 ? 0.914 ? ? ? ? ? ? ? ? ? 
2.70 2.78  ? ? ? ? ? ? 2753 ? ? ? ? ? ? ? ? ? ? ? 12.8 0.482 ? ? 0.811 0.224 ? 9  1 0.960 0.990 ? 100.0 ? 0.779 ? ? ? ? ? ? ? ? ? 
2.78 2.87  ? ? ? ? ? ? 2767 ? ? ? ? ? ? ? ? ? ? ? 12.2 0.534 ? ? 0.623 0.176 ? 10 1 0.971 0.993 ? 100.0 ? 0.598 ? ? ? ? ? ? ? ? ? 
2.87 2.98  ? ? ? ? ? ? 2799 ? ? ? ? ? ? ? ? ? ? ? 11.8 0.572 ? ? 0.491 0.142 ? 11 1 0.974 0.994 ? 100.0 ? 0.470 ? ? ? ? ? ? ? ? ? 
2.98 3.09  ? ? ? ? ? ? 2798 ? ? ? ? ? ? ? ? ? ? ? 13.3 0.606 ? ? 0.424 0.115 ? 12 1 0.987 0.997 ? 99.9  ? 0.408 ? ? ? ? ? ? ? ? ? 
3.09 3.24  ? ? ? ? ? ? 2776 ? ? ? ? ? ? ? ? ? ? ? 13.2 0.674 ? ? 0.321 0.088 ? 13 1 0.991 0.998 ? 100.0 ? 0.308 ? ? ? ? ? ? ? ? ? 
3.24 3.41  ? ? ? ? ? ? 2786 ? ? ? ? ? ? ? ? ? ? ? 12.8 0.811 ? ? 0.237 0.066 ? 14 1 0.993 0.998 ? 99.8  ? 0.227 ? ? ? ? ? ? ? ? ? 
3.41 3.62  ? ? ? ? ? ? 2782 ? ? ? ? ? ? ? ? ? ? ? 12.5 0.967 ? ? 0.185 0.052 ? 15 1 0.995 0.999 ? 99.5  ? 0.177 ? ? ? ? ? ? ? ? ? 
3.62 3.90  ? ? ? ? ? ? 2816 ? ? ? ? ? ? ? ? ? ? ? 11.7 1.159 ? ? 0.136 0.040 ? 16 1 0.996 0.999 ? 99.3  ? 0.130 ? ? ? ? ? ? ? ? ? 
3.90 4.29  ? ? ? ? ? ? 2779 ? ? ? ? ? ? ? ? ? ? ? 10.6 1.272 ? ? 0.103 0.031 ? 17 1 0.997 0.999 ? 98.3  ? 0.097 ? ? ? ? ? ? ? ? ? 
4.29 4.91  ? ? ? ? ? ? 2770 ? ? ? ? ? ? ? ? ? ? ? 9.9  1.438 ? ? 0.078 0.025 ? 18 1 0.997 0.999 ? 96.7  ? 0.073 ? ? ? ? ? ? ? ? ? 
4.91 6.19  ? ? ? ? ? ? 2841 ? ? ? ? ? ? ? ? ? ? ? 10.5 1.377 ? ? 0.074 0.023 ? 19 1 0.997 0.999 ? 98.9  ? 0.070 ? ? ? ? ? ? ? ? ? 
6.19 50.00 ? ? ? ? ? ? 3023 ? ? ? ? ? ? ? ? ? ? ? 10.5 1.671 ? ? 0.056 0.018 ? 20 1 0.998 0.999 ? 98.7  ? 0.053 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IZL 
_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                            2.28 
_refine.ls_d_res_low                             31.87 
_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                     52274 
_refine.ls_number_reflns_R_free                  1995 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.26 
_refine.ls_percent_reflns_R_free                 3.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2167 
_refine.ls_R_factor_R_free                       0.2597 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2150 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.59 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.33 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.28 
_refine_hist.d_res_low                        31.87 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               7438 
_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        7262 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 11.304 ? 1018 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061  ? 1124 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 1330 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.28 2.33 . . 93  2362 62.00 . . . . 0.3346 . . . . . . . . . . . 0.3656 
'X-RAY DIFFRACTION' 2.33 2.40 . . 115 2888 76.00 . . . . 0.3204 . . . . . . . . . . . 0.4012 
'X-RAY DIFFRACTION' 2.40 2.47 . . 136 3404 90.00 . . . . 0.3113 . . . . . . . . . . . 0.3819 
'X-RAY DIFFRACTION' 2.47 2.55 . . 145 3657 96.00 . . . . 0.2892 . . . . . . . . . . . 0.3401 
'X-RAY DIFFRACTION' 2.55 2.64 . . 147 3678 96.00 . . . . 0.2730 . . . . . . . . . . . 0.3373 
'X-RAY DIFFRACTION' 2.64 2.74 . . 146 3708 97.00 . . . . 0.2570 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 2.74 2.87 . . 146 3691 98.00 . . . . 0.2509 . . . . . . . . . . . 0.3269 
'X-RAY DIFFRACTION' 2.87 3.02 . . 149 3781 98.00 . . . . 0.2393 . . . . . . . . . . . 0.3246 
'X-RAY DIFFRACTION' 3.02 3.21 . . 149 3773 99.00 . . . . 0.2390 . . . . . . . . . . . 0.3015 
'X-RAY DIFFRACTION' 3.21 3.45 . . 153 3845 99.00 . . . . 0.2126 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 3.45 3.80 . . 151 3793 99.00 . . . . 0.2078 . . . . . . . . . . . 0.2462 
'X-RAY DIFFRACTION' 3.80 4.35 . . 152 3809 98.00 . . . . 0.1825 . . . . . . . . . . . 0.2191 
'X-RAY DIFFRACTION' 4.35 5.48 . . 152 3818 97.00 . . . . 0.1640 . . . . . . . . . . . 0.2033 
# 
_struct.entry_id                     9IZL 
_struct.title                        'hVanin-1 complexed with X17' 
_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        9IZL 
_struct_keywords.text            'Inhibitor, complex, hVanin-1, HYDROLASE, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    VNN1_HUMAN 
_struct_ref.pdbx_db_accession          O95497 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPD
PEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNL
FMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVN
FLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDE
FTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTR
FEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKD
;
_struct_ref.pdbx_align_begin           22 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IZL A 1 ? 462 ? O95497 22 ? 483 ? 1 462 
2 1 9IZL B 1 ? 462 ? O95497 22 ? 483 ? 1 462 
# 
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 9IZL ILE A 5 ? UNP O95497 THR 26 variant 5 1 
2 9IZL ILE B 5 ? UNP O95497 THR 26 variant 5 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 24  ? GLN A 49  ? SER A 24  GLN A 49  1 ? 26 
HELX_P HELX_P2  AA2 ASN A 67  ? TYR A 72  ? ASN A 67  TYR A 72  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 73  ? LEU A 75  ? PRO A 73  LEU A 75  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 80  ? ASN A 84  ? ASP A 80  ASN A 84  5 ? 5  
HELX_P HELX_P5  AA5 THR A 97  ? ASN A 110 ? THR A 97  ASN A 110 1 ? 14 
HELX_P HELX_P6  AA6 THR A 189 ? PHE A 195 ? THR A 189 PHE A 195 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 198 ? ASP A 205 ? PRO A 198 ASP A 205 1 ? 8  
HELX_P HELX_P8  AA8 SER A 225 ? ARG A 238 ? SER A 225 ARG A 238 1 ? 14 
HELX_P HELX_P9  AA9 TYR A 248 ? LYS A 252 ? TYR A 248 LYS A 252 5 ? 5  
HELX_P HELX_P10 AB1 THR A 296 ? ILE A 302 ? THR A 296 ILE A 302 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 386 ? CYS A 390 ? ASN A 386 CYS A 390 5 ? 5  
HELX_P HELX_P12 AB3 TYR A 459 ? ASP A 462 ? TYR A 459 ASP A 462 5 ? 4  
HELX_P HELX_P13 AB4 SER B 24  ? GLN B 49  ? SER B 24  GLN B 49  1 ? 26 
HELX_P HELX_P14 AB5 ASN B 67  ? TYR B 72  ? ASN B 67  TYR B 72  1 ? 6  
HELX_P HELX_P15 AB6 PRO B 73  ? LEU B 75  ? PRO B 73  LEU B 75  5 ? 3  
HELX_P HELX_P16 AB7 ASP B 80  ? ASN B 84  ? ASP B 80  ASN B 84  5 ? 5  
HELX_P HELX_P17 AB8 THR B 97  ? ASN B 110 ? THR B 97  ASN B 110 1 ? 14 
HELX_P HELX_P18 AB9 THR B 189 ? PHE B 195 ? THR B 189 PHE B 195 5 ? 7  
HELX_P HELX_P19 AC1 PRO B 198 ? ASP B 205 ? PRO B 198 ASP B 205 1 ? 8  
HELX_P HELX_P20 AC2 SER B 225 ? ARG B 238 ? SER B 225 ARG B 238 1 ? 14 
HELX_P HELX_P21 AC3 TYR B 248 ? LYS B 252 ? TYR B 248 LYS B 252 5 ? 5  
HELX_P HELX_P22 AC4 THR B 296 ? ILE B 302 ? THR B 296 ILE B 302 1 ? 7  
HELX_P HELX_P23 AC5 ASN B 386 ? CYS B 390 ? ASN B 386 CYS B 390 5 ? 5  
HELX_P HELX_P24 AC6 TYR B 459 ? ASP B 462 ? TYR B 459 ASP B 462 5 ? 4  
# 
_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 
disulf1  disulf ? ? A CYS 88  SG ? ? ? 1_555 A CYS 105 SG ? ? A CYS 88  A CYS 105 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
disulf2  disulf ? ? A CYS 124 SG ? ? ? 1_555 A CYS 131 SG ? ? A CYS 124 A CYS 131 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf3  disulf ? ? A CYS 336 SG ? ? ? 1_555 A CYS 341 SG ? ? A CYS 336 A CYS 341 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf4  disulf ? ? A CYS 342 SG ? ? ? 1_555 A CYS 377 SG ? ? A CYS 342 A CYS 377 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf5  disulf ? ? A CYS 382 SG ? ? ? 1_555 A CYS 390 SG ? ? A CYS 382 A CYS 390 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf6  disulf ? ? B CYS 88  SG ? ? ? 1_555 B CYS 105 SG ? ? B CYS 88  B CYS 105 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf7  disulf ? ? B CYS 124 SG ? ? ? 1_555 B CYS 131 SG ? ? B CYS 124 B CYS 131 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf8  disulf ? ? B CYS 336 SG ? ? ? 1_555 B CYS 341 SG ? ? B CYS 336 B CYS 341 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf9  disulf ? ? B CYS 342 SG ? ? ? 1_555 B CYS 377 SG ? ? B CYS 342 B CYS 377 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf10 disulf ? ? B CYS 382 SG ? ? ? 1_555 B CYS 390 SG ? ? B CYS 382 B CYS 390 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 88  ? CYS A 105 ? CYS A 88  ? 1_555 CYS A 105 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 124 ? CYS A 131 ? CYS A 124 ? 1_555 CYS A 131 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 336 ? CYS A 341 ? CYS A 336 ? 1_555 CYS A 341 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 342 ? CYS A 377 ? CYS A 342 ? 1_555 CYS A 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 382 ? CYS A 390 ? CYS A 382 ? 1_555 CYS A 390 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS B 88  ? CYS B 105 ? CYS B 88  ? 1_555 CYS B 105 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS B 124 ? CYS B 131 ? CYS B 124 ? 1_555 CYS B 131 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 336 ? CYS B 341 ? CYS B 336 ? 1_555 CYS B 341 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS B 342 ? CYS B 377 ? CYS B 342 ? 1_555 CYS B 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS B 382 ? CYS B 390 ? CYS B 382 ? 1_555 CYS B 390 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
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 197 A . ? ASP 197 A PRO 198 A ? PRO 198 A 1 0.21  
2 LEU 221 A . ? LEU 221 A PRO 222 A ? PRO 222 A 1 4.02  
3 ASP 197 B . ? ASP 197 B PRO 198 B ? PRO 198 B 1 -0.12 
4 LEU 221 B . ? LEU 221 B PRO 222 B ? PRO 222 B 1 4.85  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
AA7 ? 6 ? 
AA8 ? 5 ? 
# 
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      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? 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 LEU A 151 ? HIS A 156 ? LEU A 151 HIS A 156 
AA1 2 ARG A 136 ? PHE A 145 ? ARG A 136 PHE A 145 
AA1 3 TYR A 113 ? PRO A 123 ? TYR A 113 PRO A 123 
AA1 4 ILE A 53  ? VAL A 55  ? ILE A 53  VAL A 55  
AA1 5 THR A 3   ? GLU A 10  ? THR A 3   GLU A 10  
AA1 6 LYS A 277 ? ASP A 284 ? LYS A 277 ASP A 284 
AA2 1 THR A 177 ? THR A 180 ? THR A 177 THR A 180 
AA2 2 GLY A 183 ? ILE A 187 ? GLY A 183 ILE A 187 
AA2 3 THR A 210 ? THR A 215 ? THR A 210 THR A 215 
AA2 4 ASN A 240 ? ASN A 245 ? ASN A 240 ASN A 245 
AA2 5 SER A 256 ? TYR A 259 ? SER A 256 TYR A 259 
AA2 6 SER A 264 ? HIS A 268 ? SER A 264 HIS A 268 
AA3 1 GLU A 311 ? VAL A 316 ? GLU A 311 VAL A 316 
AA3 2 ASP A 319 ? LYS A 325 ? ASP A 319 LYS A 325 
AA3 3 TYR A 357 ? HIS A 366 ? TYR A 357 HIS A 366 
AA3 4 TYR A 372 ? LYS A 381 ? TYR A 372 LYS A 381 
AA3 5 VAL A 449 ? ARG A 457 ? VAL A 449 ARG A 457 
AA3 6 VAL A 415 ? LEU A 421 ? VAL A 415 LEU A 421 
AA3 7 GLN A 425 ? LEU A 426 ? GLN A 425 LEU A 426 
AA4 1 ALA A 330 ? GLN A 337 ? ALA A 330 GLN A 337 
AA4 2 LEU A 340 ? MET A 348 ? LEU A 340 MET A 348 
AA4 3 PHE A 401 ? GLY A 408 ? PHE A 401 GLY A 408 
AA4 4 LEU A 439 ? SER A 441 ? LEU A 439 SER A 441 
AA4 5 PHE A 431 ? VAL A 433 ? PHE A 431 VAL A 433 
AA5 1 LEU B 151 ? HIS B 156 ? LEU B 151 HIS B 156 
AA5 2 ARG B 136 ? PHE B 145 ? ARG B 136 PHE B 145 
AA5 3 TYR B 113 ? PRO B 123 ? TYR B 113 PRO B 123 
AA5 4 ILE B 53  ? VAL B 55  ? ILE B 53  VAL B 55  
AA5 5 THR B 3   ? GLU B 10  ? THR B 3   GLU B 10  
AA5 6 LYS B 277 ? ASP B 284 ? LYS B 277 ASP B 284 
AA6 1 THR B 177 ? THR B 180 ? THR B 177 THR B 180 
AA6 2 GLY B 183 ? ILE B 187 ? GLY B 183 ILE B 187 
AA6 3 THR B 210 ? THR B 215 ? THR B 210 THR B 215 
AA6 4 ASN B 240 ? ASN B 245 ? ASN B 240 ASN B 245 
AA6 5 SER B 256 ? TYR B 259 ? SER B 256 TYR B 259 
AA6 6 SER B 264 ? HIS B 268 ? SER B 264 HIS B 268 
AA7 1 GLU B 311 ? VAL B 316 ? GLU B 311 VAL B 316 
AA7 2 ASP B 319 ? LEU B 326 ? ASP B 319 LEU B 326 
AA7 3 TYR B 357 ? HIS B 366 ? TYR B 357 HIS B 366 
AA7 4 TYR B 372 ? LYS B 381 ? TYR B 372 LYS B 381 
AA7 5 VAL B 449 ? ARG B 457 ? VAL B 449 ARG B 457 
AA7 6 VAL B 415 ? LEU B 421 ? VAL B 415 LEU B 421 
AA8 1 ALA B 330 ? GLN B 337 ? ALA B 330 GLN B 337 
AA8 2 LEU B 340 ? MET B 348 ? LEU B 340 MET B 348 
AA8 3 PHE B 401 ? GLY B 408 ? PHE B 401 GLY B 408 
AA8 4 LEU B 439 ? SER B 441 ? LEU B 439 SER B 441 
AA8 5 PHE B 431 ? VAL B 433 ? PHE B 431 VAL B 433 
# 
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 TYR A 155 ? O TYR A 155 N ASP A 142 ? N ASP A 142 
AA1 2 3 O THR A 141 ? O THR A 141 N ILE A 118 ? N ILE A 118 
AA1 3 4 O TYR A 113 ? O TYR A 113 N ILE A 54  ? N ILE A 54  
AA1 4 5 O VAL A 55  ? O VAL A 55  N TYR A 9   ? N TYR A 9   
AA1 5 6 N VAL A 8   ? N VAL A 8   O LEU A 279 ? O LEU A 279 
AA2 1 2 N PHE A 178 ? N PHE A 178 O PHE A 185 ? O PHE A 185 
AA2 2 3 N GLY A 186 ? N GLY A 186 O THR A 210 ? O THR A 210 
AA2 3 4 N THR A 215 ? N THR A 215 O SER A 244 ? O SER A 244 
AA2 4 5 N PHE A 241 ? N PHE A 241 O TYR A 259 ? O TYR A 259 
AA2 5 6 N SER A 256 ? N SER A 256 O HIS A 268 ? O HIS A 268 
AA3 1 2 N PHE A 312 ? N PHE A 312 O PHE A 323 ? O PHE A 323 
AA3 2 3 N THR A 322 ? N THR A 322 O ALA A 361 ? O ALA A 361 
AA3 3 4 N GLY A 364 ? N GLY A 364 O LEU A 374 ? O LEU A 374 
AA3 4 5 N CYS A 377 ? N CYS A 377 O LEU A 454 ? O LEU A 454 
AA3 5 6 O PHE A 455 ? O PHE A 455 N PHE A 416 ? N PHE A 416 
AA3 6 7 N LEU A 421 ? N LEU A 421 O GLN A 425 ? O GLN A 425 
AA4 1 2 N VAL A 335 ? N VAL A 335 O CYS A 342 ? O CYS A 342 
AA4 2 3 N LYS A 347 ? N LYS A 347 O MET A 403 ? O MET A 403 
AA4 3 4 N LEU A 406 ? N LEU A 406 O LEU A 439 ? O LEU A 439 
AA4 4 5 O PHE A 440 ? O PHE A 440 N GLN A 432 ? N GLN A 432 
AA5 1 2 O VAL B 152 ? O VAL B 152 N VAL B 144 ? N VAL B 144 
AA5 2 3 O THR B 141 ? O THR B 141 N ILE B 118 ? N ILE B 118 
AA5 3 4 O VAL B 115 ? O VAL B 115 N ILE B 54  ? N ILE B 54  
AA5 4 5 O VAL B 55  ? O VAL B 55  N TYR B 9   ? N TYR B 9   
AA5 5 6 N ALA B 6   ? N ALA B 6   O SER B 281 ? O SER B 281 
AA6 1 2 N PHE B 178 ? N PHE B 178 O PHE B 185 ? O PHE B 185 
AA6 2 3 N GLY B 186 ? N GLY B 186 O THR B 210 ? O THR B 210 
AA6 3 4 N PHE B 213 ? N PHE B 213 O LEU B 242 ? O LEU B 242 
AA6 4 5 N PHE B 241 ? N PHE B 241 O TYR B 259 ? O TYR B 259 
AA6 5 6 N SER B 256 ? N SER B 256 O HIS B 268 ? O HIS B 268 
AA7 1 2 N PHE B 312 ? N PHE B 312 O PHE B 323 ? O PHE B 323 
AA7 2 3 N LEU B 326 ? N LEU B 326 O TYR B 357 ? O TYR B 357 
AA7 3 4 N GLY B 364 ? N GLY B 364 O LEU B 374 ? O LEU B 374 
AA7 4 5 N LEU B 379 ? N LEU B 379 O VAL B 452 ? O VAL B 452 
AA7 5 6 O PHE B 455 ? O PHE B 455 N PHE B 416 ? N PHE B 416 
AA8 1 2 N VAL B 335 ? N VAL B 335 O CYS B 342 ? O CYS B 342 
AA8 2 3 N LYS B 347 ? N LYS B 347 O MET B 403 ? O MET B 403 
AA8 3 4 N LEU B 406 ? N LEU B 406 O LEU B 439 ? O LEU B 439 
AA8 4 5 O PHE B 440 ? O PHE B 440 N GLN B 432 ? N GLN B 432 
# 
_pdbx_entry_details.entry_id                   9IZL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 B GLU 430 ? ? N   B SER 446 ? ? 2.15 
2 1 OG  A SER 434 ? ? OD1 A ASP 436 ? ? 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              347 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              347 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              347 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                130.30 
_pdbx_validate_rmsd_angle.angle_target_value         113.40 
_pdbx_validate_rmsd_angle.angle_deviation            16.90 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 90  ? ? -109.84 72.58   
2  1 GLU A 164 ? ? -102.40 43.60   
3  1 CYS A 190 ? ? 41.92   -107.10 
4  1 TYR A 248 ? ? -159.17 74.82   
5  1 THR A 254 ? ? -173.55 146.07  
6  1 SER A 263 ? ? 179.20  161.74  
7  1 LYS A 338 ? ? 46.56   -110.22 
8  1 GLU A 350 ? ? -176.47 149.14  
9  1 ASN B 90  ? ? -112.93 78.84   
10 1 ASN B 92  ? ? 73.81   -0.91   
11 1 GLU B 164 ? ? -100.20 47.71   
12 1 CYS B 190 ? ? 42.06   -106.80 
13 1 TYR B 248 ? ? -160.14 72.78   
14 1 THR B 254 ? ? -174.20 145.77  
15 1 LYS B 338 ? ? 46.53   -111.43 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     400 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.236 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 -17.7271 12.9431  14.0561  0.4034 ? 0.0323  ? -0.0122 ? 0.5337 ? 0.0613  ? 0.3606 ? 2.7893 ? 
0.2339  ? 0.3632  ? 2.8289 ? 1.0767  ? 3.5686 ? 0.1599  ? 0.0696  ? 0.3305  ? -0.6571 ? -0.0567 ? 0.5260  ? -0.1231 ? -0.3274 ? 
-0.0918 ? 
2  'X-RAY DIFFRACTION' ? refined -8.7038  15.3060  18.7066  0.2756 ? 0.0272  ? 0.0011  ? 0.4053 ? 0.0459  ? 0.3176 ? 1.5185 ? 
0.8068  ? 0.7759  ? 3.2645 ? 0.9027  ? 2.6574 ? 0.1033  ? -0.1149 ? 0.1001  ? -0.0934 ? -0.0156 ? 0.0938  ? 0.0133  ? -0.0582 ? 
-0.0560 ? 
3  'X-RAY DIFFRACTION' ? refined 0.5511   13.5071  11.8518  0.3758 ? -0.0078 ? 0.0130  ? 0.4419 ? 0.0025  ? 0.3781 ? 2.6879 ? 
-0.2382 ? 0.5028  ? 3.6326 ? -0.6716 ? 4.0680 ? 0.2013  ? 0.2310  ? 0.1418  ? -0.0510 ? 0.0373  ? -0.3120 ? -0.1592 ? 0.4696  ? 
-0.1244 ? 
4  'X-RAY DIFFRACTION' ? refined -3.2621  -0.7456  3.5867   0.6292 ? 0.0907  ? -0.0333 ? 0.4193 ? 0.0213  ? 0.4482 ? 1.5675 ? 
0.6762  ? -0.0277 ? 1.6180 ? 0.8706  ? 3.5375 ? -0.0515 ? -0.0883 ? -0.1174 ? -0.1102 ? 0.1931  ? -0.2817 ? 0.4384  ? 0.0007  ? 
-0.1556 ? 
5  'X-RAY DIFFRACTION' ? refined -11.3547 -5.4879  3.5879   0.6820 ? -0.0698 ? -0.1149 ? 0.4288 ? -0.0090 ? 0.4303 ? 1.9174 ? 
-0.2304 ? -1.5210 ? 1.0791 ? 0.9003  ? 4.2849 ? -0.0460 ? -0.0433 ? -0.1920 ? 0.1205  ? 0.0471  ? -0.0371 ? 0.6381  ? -0.0043 ? 
-0.0029 ? 
6  'X-RAY DIFFRACTION' ? refined -4.2671  -9.0131  -18.4027 1.0917 ? 0.1645  ? -0.0399 ? 0.6438 ? -0.0365 ? 0.4509 ? 2.4706 ? 
0.9335  ? -0.3322 ? 2.6502 ? 1.4030  ? 4.3277 ? -0.0514 ? 0.4787  ? -0.1884 ? -0.8228 ? 0.2083  ? -0.1086 ? 0.2870  ? 0.5482  ? 
-0.1212 ? 
7  'X-RAY DIFFRACTION' ? refined -16.5640 -5.1428  -18.8549 0.7165 ? 0.0515  ? -0.0692 ? 0.4563 ? 0.0228  ? 0.5149 ? 3.6643 ? 
0.9872  ? -0.7032 ? 1.5721 ? -0.6819 ? 7.2111 ? -0.0030 ? 0.1324  ? 0.2782  ? -0.6667 ? -0.1780 ? 0.1995  ? -0.3642 ? -0.1519 ? 
0.2504  ? 
8  'X-RAY DIFFRACTION' ? refined -5.7287  -12.3177 -6.2482  0.9411 ? 0.1503  ? -0.0931 ? 0.4348 ? -0.0135 ? 0.4843 ? 4.2688 ? 
0.6894  ? 0.7582  ? 2.0153 ? 1.2107  ? 4.3032 ? 0.3724  ? 0.0281  ? -0.7922 ? -0.3150 ? -0.0519 ? -0.1693 ? 1.0236  ? 0.3318  ? 
-0.2406 ? 
9  'X-RAY DIFFRACTION' ? refined -26.4244 2.6264   -44.1735 0.6884 ? -0.0569 ? -0.0538 ? 0.3924 ? -0.0274 ? 0.3190 ? 1.8696 ? 
-0.3648 ? -1.7486 ? 2.3727 ? -0.2059 ? 1.8011 ? 0.3495  ? 0.5179  ? -0.6738 ? 0.0392  ? -0.0778 ? 0.2532  ? 0.8874  ? -0.1390 ? 
-0.2478 ? 
10 'X-RAY DIFFRACTION' ? refined -31.1292 9.8046   -37.4710 0.4863 ? -0.1085 ? 0.0130  ? 0.4027 ? 0.0042  ? 0.3533 ? 1.4316 ? 
-1.1420 ? 0.1158  ? 3.1653 ? 1.2509  ? 3.8610 ? -0.1026 ? 0.0075  ? -0.1069 ? 0.3481  ? 0.0608  ? 0.1797  ? 0.4508  ? -0.3490 ? 
0.0221  ? 
11 'X-RAY DIFFRACTION' ? refined -23.5182 16.9316  -42.1613 0.3997 ? -0.0024 ? -0.0472 ? 0.3298 ? -0.0771 ? 0.3417 ? 3.0131 ? 
-0.8526 ? -0.8251 ? 2.8806 ? 0.2117  ? 2.5511 ? -0.0547 ? 0.1498  ? -0.1042 ? 0.2193  ? 0.2551  ? -0.0119 ? 0.1066  ? 0.0724  ? 
-0.0913 ? 
12 'X-RAY DIFFRACTION' ? refined -13.2593 7.2322   -49.9990 0.4362 ? -0.0084 ? -0.0982 ? 0.4327 ? -0.0731 ? 0.3832 ? 1.8121 ? 
-1.0677 ? -1.1462 ? 2.8293 ? -0.8765 ? 3.6407 ? -0.1241 ? -0.0308 ? -0.0801 ? 0.1494  ? 0.2763  ? -0.3423 ? 0.4875  ? 0.3622  ? 
-0.1478 ? 
13 'X-RAY DIFFRACTION' ? refined 0.7899   15.6891  -68.0553 0.6170 ? -0.1290 ? -0.0010 ? 0.6286 ? -0.0487 ? 0.6030 ? 3.7484 ? 
1.4101  ? 1.0874  ? 1.9771 ? 0.9584  ? 2.5586 ? -0.0901 ? -0.1199 ? -0.0227 ? -0.2090 ? 0.2558  ? -0.4291 ? -0.4179 ? 0.3575  ? 
-0.0908 ? 
14 'X-RAY DIFFRACTION' ? refined -1.4133  11.7230  -74.9586 0.5577 ? -0.1587 ? 0.0149  ? 0.7376 ? -0.0591 ? 0.5315 ? 2.9869 ? 
-0.7724 ? -0.6920 ? 4.6141 ? 1.1738  ? 2.6547 ? -0.0540 ? 0.3357  ? 0.3311  ? -0.4828 ? -0.0708 ? -0.3254 ? -0.5870 ? 0.5159  ? 
0.0998  ? 
15 'X-RAY DIFFRACTION' ? refined -5.4144  9.5290   -69.6968 0.3701 ? -0.0601 ? -0.0299 ? 0.5358 ? -0.0700 ? 0.3665 ? 3.2616 ? 
-1.3631 ? -0.6953 ? 4.7648 ? 0.7285  ? 3.0546 ? 0.1044  ? 0.0106  ? -0.0427 ? -0.1984 ? 0.1917  ? -0.2895 ? -0.0599 ? 0.3987  ? 
-0.2371 ? 
16 'X-RAY DIFFRACTION' ? refined -9.5568  -0.4589  -73.5190 0.5844 ? -0.1037 ? -0.0008 ? 0.6293 ? -0.1094 ? 0.4536 ? 3.8990 ? 
-0.9775 ? 0.8830  ? 4.1936 ? -0.1997 ? 3.9041 ? 0.2448  ? -0.0873 ? 0.0067  ? 0.0445  ? 0.0826  ? -0.2628 ? 0.3568  ? 0.1873  ? 
-0.2319 ? 
17 'X-RAY DIFFRACTION' ? refined -0.2544  7.9012   -59.5634 0.4596 ? -0.0018 ? -0.0880 ? 0.6067 ? -0.1095 ? 0.5222 ? 3.3488 ? 
0.4440  ? -1.0548 ? 1.4391 ? -0.2213 ? 1.9587 ? 0.1453  ? -0.4284 ? 0.3521  ? 0.2160  ? -0.1561 ? -0.5634 ? 0.1840  ? 0.6370  ? 
-0.0523 ? 
18 'X-RAY DIFFRACTION' ? refined -3.5723  9.8440   -61.1288 0.4415 ? -0.0257 ? -0.1276 ? 0.6059 ? -0.1105 ? 0.5221 ? 2.6951 ? 
-0.7602 ? -1.4113 ? 3.9205 ? 1.3511  ? 2.0036 ? -0.1265 ? 0.0182  ? 0.4528  ? 0.5855  ? 0.3727  ? -1.0267 ? -0.0144 ? 0.6264  ? 
-0.3110 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 48 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 49 through 123 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 124 through 189 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 245 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 246 through 301 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 302 through 381 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 382 through 400 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 401 through 462 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 24 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 25 through 135 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 136 through 189 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 190 through 288 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 289 through 318 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 319 through 339 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 340 through 381 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 382 through 400 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 401 through 438 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 439 through 462 )
;
# 
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 
A1EAG C10  C N N 1   
A1EAG C13  C N N 2   
A1EAG C15  C Y N 3   
A1EAG C17  C Y N 4   
A1EAG C20  C N S 5   
A1EAG C21  C N N 6   
A1EAG C22  C N N 7   
A1EAG C01  C Y N 8   
A1EAG C02  C N N 9   
A1EAG C05  C N N 10  
A1EAG C06  C N N 11  
A1EAG C07  C N N 12  
A1EAG C08  C N N 13  
A1EAG C09  C N N 14  
A1EAG C12  C N N 15  
A1EAG C19  C N N 16  
A1EAG N03  N N N 17  
A1EAG N16  N Y N 18  
A1EAG N18  N N N 19  
A1EAG O04  O N N 20  
A1EAG O11  O N N 21  
A1EAG O23  O N N 22  
A1EAG S14  S Y N 23  
A1EAG H102 H N N 24  
A1EAG H101 H N N 25  
A1EAG H131 H N N 26  
A1EAG H132 H N N 27  
A1EAG H171 H N N 28  
A1EAG H201 H N N 29  
A1EAG H211 H N N 30  
A1EAG H212 H N N 31  
A1EAG H222 H N N 32  
A1EAG H221 H N N 33  
A1EAG H052 H N N 34  
A1EAG H051 H N N 35  
A1EAG H072 H N N 36  
A1EAG H071 H N N 37  
A1EAG H082 H N N 38  
A1EAG H081 H N N 39  
A1EAG H091 H N N 40  
A1EAG H092 H N N 41  
A1EAG H121 H N N 42  
A1EAG H122 H N N 43  
A1EAG H192 H N N 44  
A1EAG H191 H N N 45  
A1EAG H231 H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
GLN   N    N N N 134 
GLN   CA   C N S 135 
GLN   C    C N N 136 
GLN   O    O N N 137 
GLN   CB   C N N 138 
GLN   CG   C N N 139 
GLN   CD   C N N 140 
GLN   OE1  O N N 141 
GLN   NE2  N N N 142 
GLN   OXT  O N N 143 
GLN   H    H N N 144 
GLN   H2   H N N 145 
GLN   HA   H N N 146 
GLN   HB2  H N N 147 
GLN   HB3  H N N 148 
GLN   HG2  H N N 149 
GLN   HG3  H N N 150 
GLN   HE21 H N N 151 
GLN   HE22 H N N 152 
GLN   HXT  H N N 153 
GLU   N    N N N 154 
GLU   CA   C N S 155 
GLU   C    C N N 156 
GLU   O    O N N 157 
GLU   CB   C N N 158 
GLU   CG   C N N 159 
GLU   CD   C N N 160 
GLU   OE1  O N N 161 
GLU   OE2  O N N 162 
GLU   OXT  O N N 163 
GLU   H    H N N 164 
GLU   H2   H N N 165 
GLU   HA   H N N 166 
GLU   HB2  H N N 167 
GLU   HB3  H N N 168 
GLU   HG2  H N N 169 
GLU   HG3  H N N 170 
GLU   HE2  H N N 171 
GLU   HXT  H N N 172 
GLY   N    N N N 173 
GLY   CA   C N N 174 
GLY   C    C N N 175 
GLY   O    O N N 176 
GLY   OXT  O N N 177 
GLY   H    H N N 178 
GLY   H2   H N N 179 
GLY   HA2  H N N 180 
GLY   HA3  H N N 181 
GLY   HXT  H N N 182 
HIS   N    N N N 183 
HIS   CA   C N S 184 
HIS   C    C N N 185 
HIS   O    O N N 186 
HIS   CB   C N N 187 
HIS   CG   C Y N 188 
HIS   ND1  N Y N 189 
HIS   CD2  C Y N 190 
HIS   CE1  C Y N 191 
HIS   NE2  N Y N 192 
HIS   OXT  O N N 193 
HIS   H    H N N 194 
HIS   H2   H N N 195 
HIS   HA   H N N 196 
HIS   HB2  H N N 197 
HIS   HB3  H N N 198 
HIS   HD1  H N N 199 
HIS   HD2  H N N 200 
HIS   HE1  H N N 201 
HIS   HE2  H N N 202 
HIS   HXT  H N N 203 
HOH   O    O N N 204 
HOH   H1   H N N 205 
HOH   H2   H N N 206 
ILE   N    N N N 207 
ILE   CA   C N S 208 
ILE   C    C N N 209 
ILE   O    O N N 210 
ILE   CB   C N S 211 
ILE   CG1  C N N 212 
ILE   CG2  C N N 213 
ILE   CD1  C N N 214 
ILE   OXT  O N N 215 
ILE   H    H N N 216 
ILE   H2   H N N 217 
ILE   HA   H N N 218 
ILE   HB   H N N 219 
ILE   HG12 H N N 220 
ILE   HG13 H N N 221 
ILE   HG21 H N N 222 
ILE   HG22 H N N 223 
ILE   HG23 H N N 224 
ILE   HD11 H N N 225 
ILE   HD12 H N N 226 
ILE   HD13 H N N 227 
ILE   HXT  H N N 228 
LEU   N    N N N 229 
LEU   CA   C N S 230 
LEU   C    C N N 231 
LEU   O    O N N 232 
LEU   CB   C N N 233 
LEU   CG   C N N 234 
LEU   CD1  C N N 235 
LEU   CD2  C N N 236 
LEU   OXT  O N N 237 
LEU   H    H N N 238 
LEU   H2   H N N 239 
LEU   HA   H N N 240 
LEU   HB2  H N N 241 
LEU   HB3  H N N 242 
LEU   HG   H N N 243 
LEU   HD11 H N N 244 
LEU   HD12 H N N 245 
LEU   HD13 H N N 246 
LEU   HD21 H N N 247 
LEU   HD22 H N N 248 
LEU   HD23 H N N 249 
LEU   HXT  H N N 250 
LYS   N    N N N 251 
LYS   CA   C N S 252 
LYS   C    C N N 253 
LYS   O    O N N 254 
LYS   CB   C N N 255 
LYS   CG   C N N 256 
LYS   CD   C N N 257 
LYS   CE   C N N 258 
LYS   NZ   N N N 259 
LYS   OXT  O N N 260 
LYS   H    H N N 261 
LYS   H2   H N N 262 
LYS   HA   H N N 263 
LYS   HB2  H N N 264 
LYS   HB3  H N N 265 
LYS   HG2  H N N 266 
LYS   HG3  H N N 267 
LYS   HD2  H N N 268 
LYS   HD3  H N N 269 
LYS   HE2  H N N 270 
LYS   HE3  H N N 271 
LYS   HZ1  H N N 272 
LYS   HZ2  H N N 273 
LYS   HZ3  H N N 274 
LYS   HXT  H N N 275 
MET   N    N N N 276 
MET   CA   C N S 277 
MET   C    C N N 278 
MET   O    O N N 279 
MET   CB   C N N 280 
MET   CG   C N N 281 
MET   SD   S N N 282 
MET   CE   C N N 283 
MET   OXT  O N N 284 
MET   H    H N N 285 
MET   H2   H N N 286 
MET   HA   H N N 287 
MET   HB2  H N N 288 
MET   HB3  H N N 289 
MET   HG2  H N N 290 
MET   HG3  H N N 291 
MET   HE1  H N N 292 
MET   HE2  H N N 293 
MET   HE3  H N N 294 
MET   HXT  H N N 295 
PHE   N    N N N 296 
PHE   CA   C N S 297 
PHE   C    C N N 298 
PHE   O    O N N 299 
PHE   CB   C N N 300 
PHE   CG   C Y N 301 
PHE   CD1  C Y N 302 
PHE   CD2  C Y N 303 
PHE   CE1  C Y N 304 
PHE   CE2  C Y N 305 
PHE   CZ   C Y N 306 
PHE   OXT  O N N 307 
PHE   H    H N N 308 
PHE   H2   H N N 309 
PHE   HA   H N N 310 
PHE   HB2  H N N 311 
PHE   HB3  H N N 312 
PHE   HD1  H N N 313 
PHE   HD2  H N N 314 
PHE   HE1  H N N 315 
PHE   HE2  H N N 316 
PHE   HZ   H N N 317 
PHE   HXT  H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
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 
A1EAG O23 C20  sing N N 1   
A1EAG C20 C19  sing N N 2   
A1EAG C20 C21  sing N N 3   
A1EAG C19 N18  sing N N 4   
A1EAG C21 C22  sing N N 5   
A1EAG N18 C22  sing N N 6   
A1EAG N18 C15  sing N N 7   
A1EAG C15 N16  doub Y N 8   
A1EAG C15 S14  sing Y N 9   
A1EAG N16 C17  sing Y N 10  
A1EAG C12 O11  sing N N 11  
A1EAG C12 C13  sing N N 12  
A1EAG O11 C10  sing N N 13  
A1EAG S14 C01  sing Y N 14  
A1EAG C17 C01  doub Y N 15  
A1EAG C13 C06  sing N N 16  
A1EAG C01 C02  sing N N 17  
A1EAG C10 C09  sing N N 18  
A1EAG C05 C06  sing N N 19  
A1EAG C05 N03  sing N N 20  
A1EAG C06 C09  sing N N 21  
A1EAG C06 C07  sing N N 22  
A1EAG C02 N03  sing N N 23  
A1EAG C02 O04  doub N N 24  
A1EAG N03 C08  sing N N 25  
A1EAG C07 C08  sing N N 26  
A1EAG C10 H102 sing N N 27  
A1EAG C10 H101 sing N N 28  
A1EAG C13 H131 sing N N 29  
A1EAG C13 H132 sing N N 30  
A1EAG C17 H171 sing N N 31  
A1EAG C20 H201 sing N N 32  
A1EAG C21 H211 sing N N 33  
A1EAG C21 H212 sing N N 34  
A1EAG C22 H222 sing N N 35  
A1EAG C22 H221 sing N N 36  
A1EAG C05 H052 sing N N 37  
A1EAG C05 H051 sing N N 38  
A1EAG C07 H072 sing N N 39  
A1EAG C07 H071 sing N N 40  
A1EAG C08 H082 sing N N 41  
A1EAG C08 H081 sing N N 42  
A1EAG C09 H091 sing N N 43  
A1EAG C09 H092 sing N N 44  
A1EAG C12 H121 sing N N 45  
A1EAG C12 H122 sing N N 46  
A1EAG C19 H192 sing N N 47  
A1EAG C19 H191 sing N N 48  
A1EAG O23 H231 sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82173686 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7SLV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IZL 
_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]   0.017000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010755 
_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]   0.004568 
_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 
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    . GLN   A 1 1   ? -4.843  -11.011 26.682  1.00 71.38  ? 1   GLN   A N    1 
ATOM   2    C CA   . GLN   A 1 1   ? -6.045  -11.460 25.979  1.00 72.48  ? 1   GLN   A CA   1 
ATOM   3    C C    . GLN   A 1 1   ? -5.754  -11.832 24.514  1.00 69.53  ? 1   GLN   A C    1 
ATOM   4    O O    . GLN   A 1 1   ? -5.054  -11.114 23.802  1.00 67.85  ? 1   GLN   A O    1 
ATOM   5    C CB   . GLN   A 1 1   ? -7.142  -10.389 26.067  1.00 64.11  ? 1   GLN   A CB   1 
ATOM   6    C CG   . GLN   A 1 1   ? -7.020  -9.250  25.098  1.00 65.82  ? 1   GLN   A CG   1 
ATOM   7    C CD   . GLN   A 1 1   ? -8.022  -8.136  25.398  1.00 62.80  ? 1   GLN   A CD   1 
ATOM   8    O OE1  . GLN   A 1 1   ? -7.865  -7.387  26.355  1.00 63.92  ? 1   GLN   A OE1  1 
ATOM   9    N NE2  . GLN   A 1 1   ? -9.082  -8.056  24.594  1.00 62.08  ? 1   GLN   A NE2  1 
ATOM   10   N N    . ASP   A 1 2   ? -6.285  -12.980 24.085  1.00 65.39  ? 2   ASP   A N    1 
ATOM   11   C CA   . ASP   A 1 2   ? -5.935  -13.571 22.801  1.00 64.70  ? 2   ASP   A CA   1 
ATOM   12   C C    . ASP   A 1 2   ? -6.778  -13.062 21.638  1.00 66.89  ? 2   ASP   A C    1 
ATOM   13   O O    . ASP   A 1 2   ? -6.374  -13.231 20.480  1.00 64.63  ? 2   ASP   A O    1 
ATOM   14   C CB   . ASP   A 1 2   ? -6.069  -15.086 22.872  1.00 66.58  ? 2   ASP   A CB   1 
ATOM   15   C CG   . ASP   A 1 2   ? -5.121  -15.682 23.845  1.00 73.64  ? 2   ASP   A CG   1 
ATOM   16   O OD1  . ASP   A 1 2   ? -4.062  -15.058 24.058  1.00 79.63  ? 2   ASP   A OD1  1 
ATOM   17   O OD2  . ASP   A 1 2   ? -5.435  -16.748 24.409  1.00 78.86  ? 2   ASP   A OD2  1 
ATOM   18   N N    . THR   A 1 3   ? -7.929  -12.452 21.917  1.00 58.83  ? 3   THR   A N    1 
ATOM   19   C CA   . THR   A 1 3   ? -8.822  -11.930 20.892  1.00 58.73  ? 3   THR   A CA   1 
ATOM   20   C C    . THR   A 1 3   ? -9.408  -10.612 21.387  1.00 56.30  ? 3   THR   A C    1 
ATOM   21   O O    . THR   A 1 3   ? -9.416  -10.334 22.590  1.00 52.26  ? 3   THR   A O    1 
ATOM   22   C CB   . THR   A 1 3   ? -9.942  -12.922 20.569  1.00 58.10  ? 3   THR   A CB   1 
ATOM   23   O OG1  . THR   A 1 3   ? -10.798 -13.050 21.715  1.00 56.39  ? 3   THR   A OG1  1 
ATOM   24   C CG2  . THR   A 1 3   ? -9.363  -14.291 20.217  1.00 58.69  ? 3   THR   A CG2  1 
ATOM   25   N N    . PHE   A 1 4   ? -9.921  -9.808  20.450  1.00 62.56  ? 4   PHE   A N    1 
ATOM   26   C CA   . PHE   A 1 4   ? -10.540 -8.531  20.800  1.00 60.64  ? 4   PHE   A CA   1 
ATOM   27   C C    . PHE   A 1 4   ? -11.671 -8.189  19.823  1.00 64.27  ? 4   PHE   A C    1 
ATOM   28   O O    . PHE   A 1 4   ? -11.695 -8.663  18.683  1.00 62.34  ? 4   PHE   A O    1 
ATOM   29   C CB   . PHE   A 1 4   ? -9.486  -7.408  20.853  1.00 59.45  ? 4   PHE   A CB   1 
ATOM   30   C CG   . PHE   A 1 4   ? -8.855  -7.077  19.517  1.00 60.21  ? 4   PHE   A CG   1 
ATOM   31   C CD1  . PHE   A 1 4   ? -7.808  -7.848  19.015  1.00 61.53  ? 4   PHE   A CD1  1 
ATOM   32   C CD2  . PHE   A 1 4   ? -9.279  -5.967  18.780  1.00 54.93  ? 4   PHE   A CD2  1 
ATOM   33   C CE1  . PHE   A 1 4   ? -7.217  -7.540  17.771  1.00 57.91  ? 4   PHE   A CE1  1 
ATOM   34   C CE2  . PHE   A 1 4   ? -8.686  -5.647  17.567  1.00 52.68  ? 4   PHE   A CE2  1 
ATOM   35   C CZ   . PHE   A 1 4   ? -7.655  -6.433  17.062  1.00 56.21  ? 4   PHE   A CZ   1 
ATOM   36   N N    . ILE   A 1 5   ? -12.596 -7.331  20.285  1.00 66.52  ? 5   ILE   A N    1 
ATOM   37   C CA   . ILE   A 1 5   ? -13.745 -6.878  19.498  1.00 66.33  ? 5   ILE   A CA   1 
ATOM   38   C C    . ILE   A 1 5   ? -13.284 -5.661  18.731  1.00 64.43  ? 5   ILE   A C    1 
ATOM   39   O O    . ILE   A 1 5   ? -12.999 -4.623  19.335  1.00 63.19  ? 5   ILE   A O    1 
ATOM   40   C CB   . ILE   A 1 5   ? -14.930 -6.448  20.374  1.00 68.00  ? 5   ILE   A CB   1 
ATOM   41   C CG1  . ILE   A 1 5   ? -15.453 -7.579  21.206  1.00 70.06  ? 5   ILE   A CG1  1 
ATOM   42   C CG2  . ILE   A 1 5   ? -16.097 -6.079  19.467  1.00 68.06  ? 5   ILE   A CG2  1 
ATOM   43   C CD1  . ILE   A 1 5   ? -15.261 -8.872  20.590  1.00 75.72  ? 5   ILE   A CD1  1 
ATOM   44   N N    . ALA   A 1 6   ? -13.268 -5.748  17.414  1.00 51.04  ? 6   ALA   A N    1 
ATOM   45   C CA   . ALA   A 1 6   ? -12.889 -4.598  16.616  1.00 44.12  ? 6   ALA   A CA   1 
ATOM   46   C C    . ALA   A 1 6   ? -14.140 -3.964  16.024  1.00 42.27  ? 6   ALA   A C    1 
ATOM   47   O O    . ALA   A 1 6   ? -15.094 -4.658  15.677  1.00 45.66  ? 6   ALA   A O    1 
ATOM   48   C CB   . ALA   A 1 6   ? -11.910 -5.005  15.522  1.00 45.21  ? 6   ALA   A CB   1 
ATOM   49   N N    . ALA   A 1 7   ? -14.133 -2.638  15.899  1.00 47.03  ? 7   ALA   A N    1 
ATOM   50   C CA   . ALA   A 1 7   ? -15.249 -1.936  15.275  1.00 48.55  ? 7   ALA   A CA   1 
ATOM   51   C C    . ALA   A 1 7   ? -14.724 -0.910  14.284  1.00 46.21  ? 7   ALA   A C    1 
ATOM   52   O O    . ALA   A 1 7   ? -13.644 -0.344  14.477  1.00 43.80  ? 7   ALA   A O    1 
ATOM   53   C CB   . ALA   A 1 7   ? -16.149 -1.246  16.306  1.00 46.88  ? 7   ALA   A CB   1 
ATOM   54   N N    . VAL   A 1 8   ? -15.461 -0.718  13.195  1.00 48.59  ? 8   VAL   A N    1 
ATOM   55   C CA   . VAL   A 1 8   ? -15.201 0.384   12.274  1.00 47.28  ? 8   VAL   A CA   1 
ATOM   56   C C    . VAL   A 1 8   ? -16.531 1.038   11.925  1.00 47.86  ? 8   VAL   A C    1 
ATOM   57   O O    . VAL   A 1 8   ? -17.583 0.385   11.871  1.00 47.89  ? 8   VAL   A O    1 
ATOM   58   C CB   . VAL   A 1 8   ? -14.447 -0.048  11.002  1.00 45.57  ? 8   VAL   A CB   1 
ATOM   59   C CG1  . VAL   A 1 8   ? -13.040 -0.515  11.359  1.00 45.56  ? 8   VAL   A CG1  1 
ATOM   60   C CG2  . VAL   A 1 8   ? -15.231 -1.135  10.252  1.00 47.72  ? 8   VAL   A CG2  1 
ATOM   61   N N    . TYR   A 1 9   ? -16.489 2.351   11.730  1.00 43.26  ? 9   TYR   A N    1 
ATOM   62   C CA   . TYR   A 1 9   ? -17.681 3.112   11.407  1.00 42.84  ? 9   TYR   A CA   1 
ATOM   63   C C    . TYR   A 1 9   ? -17.483 3.770   10.048  1.00 42.95  ? 9   TYR   A C    1 
ATOM   64   O O    . TYR   A 1 9   ? -16.429 4.362   9.786   1.00 40.50  ? 9   TYR   A O    1 
ATOM   65   C CB   . TYR   A 1 9   ? -18.006 4.141   12.496  1.00 41.88  ? 9   TYR   A CB   1 
ATOM   66   C CG   . TYR   A 1 9   ? -19.336 4.783   12.268  1.00 42.28  ? 9   TYR   A CG   1 
ATOM   67   C CD1  . TYR   A 1 9   ? -20.483 4.005   12.158  1.00 42.92  ? 9   TYR   A CD1  1 
ATOM   68   C CD2  . TYR   A 1 9   ? -19.452 6.158   12.144  1.00 40.77  ? 9   TYR   A CD2  1 
ATOM   69   C CE1  . TYR   A 1 9   ? -21.718 4.579   11.909  1.00 44.66  ? 9   TYR   A CE1  1 
ATOM   70   C CE2  . TYR   A 1 9   ? -20.679 6.748   11.914  1.00 43.66  ? 9   TYR   A CE2  1 
ATOM   71   C CZ   . TYR   A 1 9   ? -21.816 5.952   11.782  1.00 45.95  ? 9   TYR   A CZ   1 
ATOM   72   O OH   . TYR   A 1 9   ? -23.056 6.519   11.529  1.00 46.87  ? 9   TYR   A OH   1 
ATOM   73   N N    . GLU   A 1 10  ? -18.455 3.566   9.157   1.00 45.56  ? 10  GLU   A N    1 
ATOM   74   C CA   . GLU   A 1 10  ? -18.537 4.286   7.892   1.00 44.29  ? 10  GLU   A CA   1 
ATOM   75   C C    . GLU   A 1 10  ? -19.468 5.476   8.116   1.00 46.67  ? 10  GLU   A C    1 
ATOM   76   O O    . GLU   A 1 10  ? -20.645 5.299   8.470   1.00 45.33  ? 10  GLU   A O    1 
ATOM   77   C CB   . GLU   A 1 10  ? -19.026 3.383   6.750   1.00 44.20  ? 10  GLU   A CB   1 
ATOM   78   C CG   . GLU   A 1 10  ? -19.288 4.119   5.396   1.00 46.44  ? 10  GLU   A CG   1 
ATOM   79   C CD   . GLU   A 1 10  ? -19.080 3.242   4.140   1.00 49.30  ? 10  GLU   A CD   1 
ATOM   80   O OE1  . GLU   A 1 10  ? -18.103 2.465   4.085   1.00 49.59  ? 10  GLU   A OE1  1 
ATOM   81   O OE2  . GLU   A 1 10  ? -19.882 3.346   3.186   1.00 49.36  ? 10  GLU   A OE2  1 
ATOM   82   N N    . HIS   A 1 11  ? -18.933 6.684   7.936   1.00 47.15  ? 11  HIS   A N    1 
ATOM   83   C CA   . HIS   A 1 11  ? -19.572 7.910   8.388   1.00 46.79  ? 11  HIS   A CA   1 
ATOM   84   C C    . HIS   A 1 11  ? -20.018 8.743   7.188   1.00 49.53  ? 11  HIS   A C    1 
ATOM   85   O O    . HIS   A 1 11  ? -19.184 9.173   6.378   1.00 49.51  ? 11  HIS   A O    1 
ATOM   86   C CB   . HIS   A 1 11  ? -18.610 8.696   9.279   1.00 43.73  ? 11  HIS   A CB   1 
ATOM   87   C CG   . HIS   A 1 11  ? -19.134 10.035  9.681   1.00 47.29  ? 11  HIS   A CG   1 
ATOM   88   N ND1  . HIS   A 1 11  ? -20.441 10.227  10.083  1.00 47.88  ? 11  HIS   A ND1  1 
ATOM   89   C CD2  . HIS   A 1 11  ? -18.541 11.256  9.712   1.00 46.70  ? 11  HIS   A CD2  1 
ATOM   90   C CE1  . HIS   A 1 11  ? -20.623 11.506  10.368  1.00 50.63  ? 11  HIS   A CE1  1 
ATOM   91   N NE2  . HIS   A 1 11  ? -19.486 12.151  10.154  1.00 48.84  ? 11  HIS   A NE2  1 
ATOM   92   N N    . ALA   A 1 12  ? -21.330 8.972   7.077   1.00 49.48  ? 12  ALA   A N    1 
ATOM   93   C CA   . ALA   A 1 12  ? -21.892 9.947   6.138   1.00 50.99  ? 12  ALA   A CA   1 
ATOM   94   C C    . ALA   A 1 12  ? -21.671 11.327  6.741   1.00 54.87  ? 12  ALA   A C    1 
ATOM   95   O O    . ALA   A 1 12  ? -22.405 11.754  7.643   1.00 53.16  ? 12  ALA   A O    1 
ATOM   96   C CB   . ALA   A 1 12  ? -23.372 9.677   5.895   1.00 51.25  ? 12  ALA   A CB   1 
ATOM   97   N N    . ALA   A 1 13  ? -20.609 12.005  6.316   1.00 53.56  ? 13  ALA   A N    1 
ATOM   98   C CA   . ALA   A 1 13  ? -20.157 13.182  7.049   1.00 54.37  ? 13  ALA   A CA   1 
ATOM   99   C C    . ALA   A 1 13  ? -20.934 14.425  6.656   1.00 58.08  ? 13  ALA   A C    1 
ATOM   100  O O    . ALA   A 1 13  ? -21.303 14.616  5.494   1.00 59.07  ? 13  ALA   A O    1 
ATOM   101  C CB   . ALA   A 1 13  ? -18.662 13.434  6.851   1.00 50.85  ? 13  ALA   A CB   1 
ATOM   102  N N    . ILE   A 1 14  ? -21.166 15.275  7.647   1.00 59.17  ? 14  ILE   A N    1 
ATOM   103  C CA   . ILE   A 1 14  ? -21.740 16.600  7.446   1.00 59.96  ? 14  ILE   A CA   1 
ATOM   104  C C    . ILE   A 1 14  ? -20.622 17.536  6.998   1.00 61.27  ? 14  ILE   A C    1 
ATOM   105  O O    . ILE   A 1 14  ? -19.656 17.767  7.736   1.00 57.56  ? 14  ILE   A O    1 
ATOM   106  C CB   . ILE   A 1 14  ? -22.390 17.107  8.739   1.00 64.51  ? 14  ILE   A CB   1 
ATOM   107  C CG1  . ILE   A 1 14  ? -23.331 16.038  9.302   1.00 62.32  ? 14  ILE   A CG1  1 
ATOM   108  C CG2  . ILE   A 1 14  ? -23.086 18.429  8.507   1.00 61.56  ? 14  ILE   A CG2  1 
ATOM   109  C CD1  . ILE   A 1 14  ? -23.924 16.411  10.618  1.00 62.05  ? 14  ILE   A CD1  1 
ATOM   110  N N    . LEU   A 1 15  ? -20.741 18.060  5.781   1.00 65.18  ? 15  LEU   A N    1 
ATOM   111  C CA   . LEU   A 1 15  ? -19.729 18.934  5.201   1.00 67.47  ? 15  LEU   A CA   1 
ATOM   112  C C    . LEU   A 1 15  ? -20.042 20.390  5.534   1.00 71.92  ? 15  LEU   A C    1 
ATOM   113  O O    . LEU   A 1 15  ? -21.207 20.799  5.486   1.00 77.34  ? 15  LEU   A O    1 
ATOM   114  C CB   . LEU   A 1 15  ? -19.669 18.760  3.680   1.00 67.96  ? 15  LEU   A CB   1 
ATOM   115  C CG   . LEU   A 1 15  ? -19.250 17.365  3.213   1.00 65.49  ? 15  LEU   A CG   1 
ATOM   116  C CD1  . LEU   A 1 15  ? -19.122 17.276  1.686   1.00 65.03  ? 15  LEU   A CD1  1 
ATOM   117  C CD2  . LEU   A 1 15  ? -17.952 16.977  3.919   1.00 63.36  ? 15  LEU   A CD2  1 
ATOM   118  N N    . PRO   A 1 16  ? -19.027 21.186  5.869   1.00 67.46  ? 16  PRO   A N    1 
ATOM   119  C CA   . PRO   A 1 16  ? -19.272 22.605  6.180   1.00 71.86  ? 16  PRO   A CA   1 
ATOM   120  C C    . PRO   A 1 16  ? -19.845 23.380  4.995   1.00 77.40  ? 16  PRO   A C    1 
ATOM   121  O O    . PRO   A 1 16  ? -19.421 23.204  3.850   1.00 79.66  ? 16  PRO   A O    1 
ATOM   122  C CB   . PRO   A 1 16  ? -17.888 23.131  6.586   1.00 69.99  ? 16  PRO   A CB   1 
ATOM   123  C CG   . PRO   A 1 16  ? -16.908 22.022  6.325   1.00 69.35  ? 16  PRO   A CG   1 
ATOM   124  C CD   . PRO   A 1 16  ? -17.664 20.746  6.212   1.00 66.27  ? 16  PRO   A CD   1 
ATOM   125  N N    . ASN   A 1 17  ? -20.832 24.242  5.285   1.00 87.99  ? 17  ASN   A N    1 
ATOM   126  C CA   . ASN   A 1 17  ? -21.419 25.120  4.271   1.00 89.56  ? 17  ASN   A CA   1 
ATOM   127  C C    . ASN   A 1 17  ? -20.328 25.841  3.489   1.00 86.06  ? 17  ASN   A C    1 
ATOM   128  O O    . ASN   A 1 17  ? -19.253 26.139  4.018   1.00 87.24  ? 17  ASN   A O    1 
ATOM   129  C CB   . ASN   A 1 17  ? -22.368 26.144  4.920   1.00 92.14  ? 17  ASN   A CB   1 
ATOM   130  C CG   . ASN   A 1 17  ? -23.780 25.596  5.153   1.00 90.51  ? 17  ASN   A CG   1 
ATOM   131  O OD1  . ASN   A 1 17  ? -24.530 25.365  4.207   1.00 90.67  ? 17  ASN   A OD1  1 
ATOM   132  N ND2  . ASN   A 1 17  ? -24.144 25.399  6.423   1.00 86.21  ? 17  ASN   A ND2  1 
ATOM   133  N N    . ALA   A 1 18  ? -20.587 26.070  2.208   1.00 112.93 ? 18  ALA   A N    1 
ATOM   134  C CA   . ALA   A 1 18  ? -19.670 26.834  1.369   1.00 114.54 ? 18  ALA   A CA   1 
ATOM   135  C C    . ALA   A 1 18  ? -19.616 28.294  1.819   1.00 115.77 ? 18  ALA   A C    1 
ATOM   136  O O    . ALA   A 1 18  ? -20.652 28.961  1.898   1.00 118.71 ? 18  ALA   A O    1 
ATOM   137  C CB   . ALA   A 1 18  ? -20.092 26.736  -0.094  1.00 110.40 ? 18  ALA   A CB   1 
ATOM   138  N N    . THR   A 1 19  ? -18.419 28.779  2.157   1.00 98.47  ? 19  THR   A N    1 
ATOM   139  C CA   . THR   A 1 19  ? -18.204 30.185  2.481   1.00 97.56  ? 19  THR   A CA   1 
ATOM   140  C C    . THR   A 1 19  ? -16.950 30.672  1.769   1.00 99.24  ? 19  THR   A C    1 
ATOM   141  O O    . THR   A 1 19  ? -16.004 29.908  1.551   1.00 93.43  ? 19  THR   A O    1 
ATOM   142  C CB   . THR   A 1 19  ? -18.072 30.453  4.000   1.00 99.04  ? 19  THR   A CB   1 
ATOM   143  O OG1  . THR   A 1 19  ? -16.840 29.909  4.490   1.00 97.57  ? 19  THR   A OG1  1 
ATOM   144  C CG2  . THR   A 1 19  ? -19.245 29.853  4.770   1.00 97.57  ? 19  THR   A CG2  1 
ATOM   145  N N    . LEU   A 1 20  ? -16.954 31.959  1.410   1.00 121.49 ? 20  LEU   A N    1 
ATOM   146  C CA   . LEU   A 1 20  ? -15.816 32.537  0.702   1.00 119.86 ? 20  LEU   A CA   1 
ATOM   147  C C    . LEU   A 1 20  ? -14.643 32.754  1.646   1.00 122.48 ? 20  LEU   A C    1 
ATOM   148  O O    . LEU   A 1 20  ? -13.489 32.509  1.276   1.00 123.34 ? 20  LEU   A O    1 
ATOM   149  C CB   . LEU   A 1 20  ? -16.213 33.846  0.019   1.00 117.83 ? 20  LEU   A CB   1 
ATOM   150  C CG   . LEU   A 1 20  ? -17.278 33.772  -1.083  1.00 130.56 ? 20  LEU   A CG   1 
ATOM   151  C CD1  . LEU   A 1 20  ? -17.605 35.159  -1.638  1.00 127.25 ? 20  LEU   A CD1  1 
ATOM   152  C CD2  . LEU   A 1 20  ? -16.855 32.832  -2.213  1.00 128.93 ? 20  LEU   A CD2  1 
ATOM   153  N N    . THR   A 1 21  ? -14.911 33.230  2.853   1.00 107.65 ? 21  THR   A N    1 
ATOM   154  C CA   . THR   A 1 21  ? -13.878 33.526  3.832   1.00 104.47 ? 21  THR   A CA   1 
ATOM   155  C C    . THR   A 1 21  ? -13.961 32.574  5.026   1.00 100.89 ? 21  THR   A C    1 
ATOM   156  O O    . THR   A 1 21  ? -15.012 31.979  5.299   1.00 99.60  ? 21  THR   A O    1 
ATOM   157  C CB   . THR   A 1 21  ? -14.023 34.979  4.309   1.00 103.95 ? 21  THR   A CB   1 
ATOM   158  O OG1  . THR   A 1 21  ? -15.150 35.077  5.190   1.00 101.00 ? 21  THR   A OG1  1 
ATOM   159  C CG2  . THR   A 1 21  ? -14.232 35.900  3.112   1.00 102.72 ? 21  THR   A CG2  1 
ATOM   160  N N    . PRO   A 1 22  ? -12.864 32.429  5.773   1.00 85.55  ? 22  PRO   A N    1 
ATOM   161  C CA   . PRO   A 1 22  ? -12.840 31.473  6.891   1.00 79.32  ? 22  PRO   A CA   1 
ATOM   162  C C    . PRO   A 1 22  ? -13.878 31.808  7.951   1.00 80.55  ? 22  PRO   A C    1 
ATOM   163  O O    . PRO   A 1 22  ? -14.133 32.977  8.251   1.00 84.39  ? 22  PRO   A O    1 
ATOM   164  C CB   . PRO   A 1 22  ? -11.417 31.619  7.452   1.00 74.01  ? 22  PRO   A CB   1 
ATOM   165  C CG   . PRO   A 1 22  ? -10.588 32.111  6.309   1.00 79.12  ? 22  PRO   A CG   1 
ATOM   166  C CD   . PRO   A 1 22  ? -11.520 32.676  5.228   1.00 84.17  ? 22  PRO   A CD   1 
ATOM   167  N N    . VAL   A 1 23  ? -14.476 30.764  8.526   1.00 62.56  ? 23  VAL   A N    1 
ATOM   168  C CA   . VAL   A 1 23  ? -15.461 30.912  9.596   1.00 62.77  ? 23  VAL   A CA   1 
ATOM   169  C C    . VAL   A 1 23  ? -14.766 31.163  10.930  1.00 64.67  ? 23  VAL   A C    1 
ATOM   170  O O    . VAL   A 1 23  ? -13.544 31.015  11.049  1.00 65.06  ? 23  VAL   A O    1 
ATOM   171  C CB   . VAL   A 1 23  ? -16.358 29.669  9.680   1.00 61.29  ? 23  VAL   A CB   1 
ATOM   172  C CG1  . VAL   A 1 23  ? -17.080 29.441  8.362   1.00 64.08  ? 23  VAL   A CG1  1 
ATOM   173  C CG2  . VAL   A 1 23  ? -15.529 28.440  10.080  1.00 57.41  ? 23  VAL   A CG2  1 
ATOM   174  N N    . SER   A 1 24  ? -15.539 31.544  11.940  1.00 72.12  ? 24  SER   A N    1 
ATOM   175  C CA   . SER   A 1 24  ? -14.992 31.716  13.277  1.00 73.73  ? 24  SER   A CA   1 
ATOM   176  C C    . SER   A 1 24  ? -14.664 30.361  13.894  1.00 71.66  ? 24  SER   A C    1 
ATOM   177  O O    . SER   A 1 24  ? -15.099 29.308  13.419  1.00 72.32  ? 24  SER   A O    1 
ATOM   178  C CB   . SER   A 1 24  ? -15.982 32.454  14.172  1.00 75.13  ? 24  SER   A CB   1 
ATOM   179  O OG   . SER   A 1 24  ? -17.116 31.640  14.415  1.00 75.38  ? 24  SER   A OG   1 
ATOM   180  N N    . ARG   A 1 25  ? -13.894 30.394  14.985  1.00 78.03  ? 25  ARG   A N    1 
ATOM   181  C CA   . ARG   A 1 25  ? -13.584 29.158  15.697  1.00 73.97  ? 25  ARG   A CA   1 
ATOM   182  C C    . ARG   A 1 25  ? -14.833 28.531  16.299  1.00 73.86  ? 25  ARG   A C    1 
ATOM   183  O O    . ARG   A 1 25  ? -14.921 27.300  16.402  1.00 74.12  ? 25  ARG   A O    1 
ATOM   184  C CB   . ARG   A 1 25  ? -12.528 29.422  16.768  1.00 75.83  ? 25  ARG   A CB   1 
ATOM   185  C CG   . ARG   A 1 25  ? -11.105 29.299  16.224  1.00 73.02  ? 25  ARG   A CG   1 
ATOM   186  C CD   . ARG   A 1 25  ? -10.067 29.255  17.335  1.00 74.74  ? 25  ARG   A CD   1 
ATOM   187  N NE   . ARG   A 1 25  ? -10.583 28.581  18.513  1.00 67.58  ? 25  ARG   A NE   1 
ATOM   188  C CZ   . ARG   A 1 25  ? -10.139 27.413  18.958  1.00 70.19  ? 25  ARG   A CZ   1 
ATOM   189  N NH1  . ARG   A 1 25  ? -9.151  26.768  18.346  1.00 63.44  ? 25  ARG   A NH1  1 
ATOM   190  N NH2  . ARG   A 1 25  ? -10.718 26.864  20.028  1.00 64.15  ? 25  ARG   A NH2  1 
ATOM   191  N N    . GLU   A 1 26  ? -15.815 29.349  16.678  1.00 73.88  ? 26  GLU   A N    1 
ATOM   192  C CA   . GLU   A 1 26  ? -17.047 28.806  17.244  1.00 76.29  ? 26  GLU   A CA   1 
ATOM   193  C C    . GLU   A 1 26  ? -17.879 28.090  16.186  1.00 70.20  ? 26  GLU   A C    1 
ATOM   194  O O    . GLU   A 1 26  ? -18.414 27.005  16.441  1.00 68.72  ? 26  GLU   A O    1 
ATOM   195  C CB   . GLU   A 1 26  ? -17.862 29.918  17.901  1.00 75.59  ? 26  GLU   A CB   1 
ATOM   196  C CG   . GLU   A 1 26  ? -17.318 30.358  19.245  1.00 78.72  ? 26  GLU   A CG   1 
ATOM   197  C CD   . GLU   A 1 26  ? -15.993 31.115  19.122  1.00 84.70  ? 26  GLU   A CD   1 
ATOM   198  O OE1  . GLU   A 1 26  ? -15.764 31.803  18.091  1.00 81.76  ? 26  GLU   A OE1  1 
ATOM   199  O OE2  . GLU   A 1 26  ? -15.179 31.023  20.066  1.00 85.17  ? 26  GLU   A OE2  1 
ATOM   200  N N    . GLU   A 1 27  ? -18.007 28.676  14.994  1.00 79.69  ? 27  GLU   A N    1 
ATOM   201  C CA   . GLU   A 1 27  ? -18.713 27.979  13.922  1.00 76.77  ? 27  GLU   A CA   1 
ATOM   202  C C    . GLU   A 1 27  ? -17.999 26.684  13.551  1.00 73.90  ? 27  GLU   A C    1 
ATOM   203  O O    . GLU   A 1 27  ? -18.642 25.646  13.329  1.00 74.26  ? 27  GLU   A O    1 
ATOM   204  C CB   . GLU   A 1 27  ? -18.868 28.894  12.707  1.00 76.60  ? 27  GLU   A CB   1 
ATOM   205  C CG   . GLU   A 1 27  ? -20.134 28.611  11.884  1.00 83.75  ? 27  GLU   A CG   1 
ATOM   206  C CD   . GLU   A 1 27  ? -20.200 27.161  11.364  1.00 87.67  ? 27  GLU   A CD   1 
ATOM   207  O OE1  . GLU   A 1 27  ? -19.600 26.851  10.301  1.00 87.47  ? 27  GLU   A OE1  1 
ATOM   208  O OE2  . GLU   A 1 27  ? -20.832 26.319  12.050  1.00 79.46  ? 27  GLU   A OE2  1 
ATOM   209  N N    . ALA   A 1 28  ? -16.666 26.728  13.483  1.00 49.29  ? 28  ALA   A N    1 
ATOM   210  C CA   . ALA   A 1 28  ? -15.893 25.526  13.179  1.00 46.93  ? 28  ALA   A CA   1 
ATOM   211  C C    . ALA   A 1 28  ? -16.167 24.426  14.193  1.00 46.23  ? 28  ALA   A C    1 
ATOM   212  O O    . ALA   A 1 28  ? -16.403 23.264  13.821  1.00 44.65  ? 28  ALA   A O    1 
ATOM   213  C CB   . ALA   A 1 28  ? -14.400 25.857  13.131  1.00 47.56  ? 28  ALA   A CB   1 
ATOM   214  N N    . LEU   A 1 29  ? -16.116 24.775  15.486  1.00 58.14  ? 29  LEU   A N    1 
ATOM   215  C CA   . LEU   A 1 29  ? -16.388 23.802  16.541  1.00 55.43  ? 29  LEU   A CA   1 
ATOM   216  C C    . LEU   A 1 29  ? -17.823 23.289  16.460  1.00 54.21  ? 29  LEU   A C    1 
ATOM   217  O O    . LEU   A 1 29  ? -18.089 22.118  16.751  1.00 53.83  ? 29  LEU   A O    1 
ATOM   218  C CB   . LEU   A 1 29  ? -16.109 24.414  17.916  1.00 52.75  ? 29  LEU   A CB   1 
ATOM   219  C CG   . LEU   A 1 29  ? -16.227 23.408  19.057  1.00 47.87  ? 29  LEU   A CG   1 
ATOM   220  C CD1  . LEU   A 1 29  ? -15.069 22.440  18.992  1.00 45.29  ? 29  LEU   A CD1  1 
ATOM   221  C CD2  . LEU   A 1 29  ? -16.274 24.119  20.395  1.00 48.51  ? 29  LEU   A CD2  1 
ATOM   222  N N    . ALA   A 1 30  ? -18.769 24.163  16.115  1.00 49.93  ? 30  ALA   A N    1 
ATOM   223  C CA   . ALA   A 1 30  ? -20.160 23.741  15.983  1.00 50.96  ? 30  ALA   A CA   1 
ATOM   224  C C    . ALA   A 1 30  ? -20.317 22.670  14.900  1.00 52.12  ? 30  ALA   A C    1 
ATOM   225  O O    . ALA   A 1 30  ? -21.001 21.655  15.099  1.00 51.38  ? 30  ALA   A O    1 
ATOM   226  C CB   . ALA   A 1 30  ? -21.032 24.956  15.676  1.00 51.22  ? 30  ALA   A CB   1 
ATOM   227  N N    . LEU   A 1 31  ? -19.688 22.876  13.740  1.00 51.27  ? 31  LEU   A N    1 
ATOM   228  C CA   . LEU   A 1 31  ? -19.795 21.857  12.692  1.00 50.02  ? 31  LEU   A CA   1 
ATOM   229  C C    . LEU   A 1 31  ? -19.093 20.559  13.091  1.00 47.20  ? 31  LEU   A C    1 
ATOM   230  O O    . LEU   A 1 31  ? -19.651 19.453  12.921  1.00 46.48  ? 31  LEU   A O    1 
ATOM   231  C CB   . LEU   A 1 31  ? -19.246 22.375  11.368  1.00 48.20  ? 31  LEU   A CB   1 
ATOM   232  C CG   . LEU   A 1 31  ? -19.275 21.169  10.431  1.00 46.91  ? 31  LEU   A CG   1 
ATOM   233  C CD1  . LEU   A 1 31  ? -20.194 21.398  9.269   1.00 48.80  ? 31  LEU   A CD1  1 
ATOM   234  C CD2  . LEU   A 1 31  ? -17.866 20.783  10.005  1.00 44.66  ? 31  LEU   A CD2  1 
ATOM   235  N N    . MET   A 1 32  ? -17.874 20.668  13.638  1.00 55.35  ? 32  MET   A N    1 
ATOM   236  C CA   . MET   A 1 32  ? -17.188 19.463  14.103  1.00 54.84  ? 32  MET   A CA   1 
ATOM   237  C C    . MET   A 1 32  ? -18.020 18.722  15.147  1.00 52.52  ? 32  MET   A C    1 
ATOM   238  O O    . MET   A 1 32  ? -18.040 17.487  15.153  1.00 52.33  ? 32  MET   A O    1 
ATOM   239  C CB   . MET   A 1 32  ? -15.807 19.817  14.667  1.00 50.94  ? 32  MET   A CB   1 
ATOM   240  C CG   . MET   A 1 32  ? -14.764 20.117  13.592  1.00 52.62  ? 32  MET   A CG   1 
ATOM   241  S SD   . MET   A 1 32  ? -13.118 20.579  14.214  1.00 49.40  ? 32  MET   A SD   1 
ATOM   242  C CE   . MET   A 1 32  ? -13.558 21.927  15.308  1.00 50.03  ? 32  MET   A CE   1 
ATOM   243  N N    . ASN   A 1 33  ? -18.750 19.451  16.001  1.00 54.59  ? 33  ASN   A N    1 
ATOM   244  C CA   . ASN   A 1 33  ? -19.590 18.835  17.028  1.00 51.16  ? 33  ASN   A CA   1 
ATOM   245  C C    . ASN   A 1 33  ? -20.807 18.152  16.424  1.00 52.40  ? 33  ASN   A C    1 
ATOM   246  O O    . ASN   A 1 33  ? -21.295 17.149  16.965  1.00 49.19  ? 33  ASN   A O    1 
ATOM   247  C CB   . ASN   A 1 33  ? -20.041 19.889  18.040  1.00 52.79  ? 33  ASN   A CB   1 
ATOM   248  C CG   . ASN   A 1 33  ? -19.088 20.018  19.219  1.00 52.34  ? 33  ASN   A CG   1 
ATOM   249  O OD1  . ASN   A 1 33  ? -18.523 19.025  19.689  1.00 50.37  ? 33  ASN   A OD1  1 
ATOM   250  N ND2  . ASN   A 1 33  ? -18.907 21.246  19.707  1.00 51.78  ? 33  ASN   A ND2  1 
ATOM   251  N N    . ARG   A 1 34  ? -21.334 18.703  15.330  1.00 59.11  ? 34  ARG   A N    1 
ATOM   252  C CA   . ARG   A 1 34  ? -22.388 18.008  14.595  1.00 56.74  ? 34  ARG   A CA   1 
ATOM   253  C C    . ARG   A 1 34  ? -21.902 16.645  14.112  1.00 53.28  ? 34  ARG   A C    1 
ATOM   254  O O    . ARG   A 1 34  ? -22.645 15.657  14.148  1.00 52.87  ? 34  ARG   A O    1 
ATOM   255  C CB   . ARG   A 1 34  ? -22.857 18.863  13.421  1.00 57.46  ? 34  ARG   A CB   1 
ATOM   256  C CG   . ARG   A 1 34  ? -23.539 20.137  13.850  1.00 57.64  ? 34  ARG   A CG   1 
ATOM   257  C CD   . ARG   A 1 34  ? -24.153 20.847  12.658  1.00 64.58  ? 34  ARG   A CD   1 
ATOM   258  N NE   . ARG   A 1 34  ? -25.176 20.034  12.013  1.00 63.18  ? 34  ARG   A NE   1 
ATOM   259  C CZ   . ARG   A 1 34  ? -25.684 20.288  10.814  1.00 69.84  ? 34  ARG   A CZ   1 
ATOM   260  N NH1  . ARG   A 1 34  ? -25.285 21.331  10.098  1.00 66.30  ? 34  ARG   A NH1  1 
ATOM   261  N NH2  . ARG   A 1 34  ? -26.615 19.477  10.322  1.00 68.36  ? 34  ARG   A NH2  1 
ATOM   262  N N    . ASN   A 1 35  ? -20.660 16.580  13.635  1.00 47.96  ? 35  ASN   A N    1 
ATOM   263  C CA   . ASN   A 1 35  ? -20.119 15.281  13.222  1.00 44.56  ? 35  ASN   A CA   1 
ATOM   264  C C    . ASN   A 1 35  ? -19.833 14.369  14.422  1.00 46.61  ? 35  ASN   A C    1 
ATOM   265  O O    . ASN   A 1 35  ? -20.038 13.143  14.356  1.00 44.17  ? 35  ASN   A O    1 
ATOM   266  C CB   . ASN   A 1 35  ? -18.862 15.489  12.394  1.00 44.35  ? 35  ASN   A CB   1 
ATOM   267  C CG   . ASN   A 1 35  ? -19.176 15.752  10.949  1.00 46.04  ? 35  ASN   A CG   1 
ATOM   268  O OD1  . ASN   A 1 35  ? -19.740 14.889  10.265  1.00 43.55  ? 35  ASN   A OD1  1 
ATOM   269  N ND2  . ASN   A 1 35  ? -18.853 16.958  10.478  1.00 43.47  ? 35  ASN   A ND2  1 
ATOM   270  N N    . LEU   A 1 36  ? -19.304 14.942  15.507  1.00 52.52  ? 36  LEU   A N    1 
ATOM   271  C CA   . LEU   A 1 36  ? -18.974 14.147  16.687  1.00 50.05  ? 36  LEU   A CA   1 
ATOM   272  C C    . LEU   A 1 36  ? -20.216 13.568  17.358  1.00 49.49  ? 36  LEU   A C    1 
ATOM   273  O O    . LEU   A 1 36  ? -20.136 12.492  17.955  1.00 47.19  ? 36  LEU   A O    1 
ATOM   274  C CB   . LEU   A 1 36  ? -18.174 14.983  17.689  1.00 46.10  ? 36  LEU   A CB   1 
ATOM   275  C CG   . LEU   A 1 36  ? -16.779 15.337  17.170  1.00 48.68  ? 36  LEU   A CG   1 
ATOM   276  C CD1  . LEU   A 1 36  ? -16.210 16.542  17.895  1.00 48.71  ? 36  LEU   A CD1  1 
ATOM   277  C CD2  . LEU   A 1 36  ? -15.835 14.140  17.246  1.00 46.21  ? 36  LEU   A CD2  1 
ATOM   278  N N    . ASP   A 1 37  ? -21.371 14.233  17.258  1.00 49.49  ? 37  ASP   A N    1 
ATOM   279  C CA   . ASP   A 1 37  ? -22.596 13.638  17.787  1.00 47.55  ? 37  ASP   A CA   1 
ATOM   280  C C    . ASP   A 1 37  ? -22.872 12.286  17.125  1.00 51.51  ? 37  ASP   A C    1 
ATOM   281  O O    . ASP   A 1 37  ? -23.114 11.280  17.811  1.00 48.99  ? 37  ASP   A O    1 
ATOM   282  C CB   . ASP   A 1 37  ? -23.782 14.586  17.582  1.00 47.48  ? 37  ASP   A CB   1 
ATOM   283  C CG   . ASP   A 1 37  ? -23.664 15.896  18.379  1.00 51.23  ? 37  ASP   A CG   1 
ATOM   284  O OD1  . ASP   A 1 37  ? -22.799 16.011  19.286  1.00 49.67  ? 37  ASP   A OD1  1 
ATOM   285  O OD2  . ASP   A 1 37  ? -24.461 16.820  18.103  1.00 52.97  ? 37  ASP   A OD2  1 
ATOM   286  N N    . ILE   A 1 38  ? -22.828 12.248  15.781  1.00 42.53  ? 38  ILE   A N    1 
ATOM   287  C CA   . ILE   A 1 38  ? -23.054 11.009  15.034  1.00 42.19  ? 38  ILE   A CA   1 
ATOM   288  C C    . ILE   A 1 38  ? -21.976 9.988   15.372  1.00 42.58  ? 38  ILE   A C    1 
ATOM   289  O O    . ILE   A 1 38  ? -22.248 8.785   15.565  1.00 41.88  ? 38  ILE   A O    1 
ATOM   290  C CB   . ILE   A 1 38  ? -23.081 11.300  13.518  1.00 43.30  ? 38  ILE   A CB   1 
ATOM   291  C CG1  . ILE   A 1 38  ? -24.298 12.143  13.146  1.00 43.48  ? 38  ILE   A CG1  1 
ATOM   292  C CG2  . ILE   A 1 38  ? -23.044 10.012  12.702  1.00 41.45  ? 38  ILE   A CG2  1 
ATOM   293  C CD1  . ILE   A 1 38  ? -24.105 12.972  11.885  1.00 46.59  ? 38  ILE   A CD1  1 
ATOM   294  N N    . LEU   A 1 39  ? -20.723 10.446  15.405  1.00 46.46  ? 39  LEU   A N    1 
ATOM   295  C CA   . LEU   A 1 39  ? -19.641 9.525   15.714  1.00 48.20  ? 39  LEU   A CA   1 
ATOM   296  C C    . LEU   A 1 39  ? -19.811 8.938   17.113  1.00 47.42  ? 39  LEU   A C    1 
ATOM   297  O O    . LEU   A 1 39  ? -19.587 7.739   17.317  1.00 46.10  ? 39  LEU   A O    1 
ATOM   298  C CB   . LEU   A 1 39  ? -18.288 10.229  15.563  1.00 50.11  ? 39  LEU   A CB   1 
ATOM   299  C CG   . LEU   A 1 39  ? -17.759 10.602  14.163  1.00 46.83  ? 39  LEU   A CG   1 
ATOM   300  C CD1  . LEU   A 1 39  ? -16.280 10.994  14.266  1.00 46.03  ? 39  LEU   A CD1  1 
ATOM   301  C CD2  . LEU   A 1 39  ? -17.942 9.477   13.114  1.00 44.03  ? 39  LEU   A CD2  1 
ATOM   302  N N    . GLU   A 1 40  ? -20.287 9.743   18.067  1.00 56.66  ? 40  GLU   A N    1 
ATOM   303  C CA   . GLU   A 1 40  ? -20.520 9.261   19.426  1.00 55.62  ? 40  GLU   A CA   1 
ATOM   304  C C    . GLU   A 1 40  ? -21.642 8.235   19.457  1.00 56.42  ? 40  GLU   A C    1 
ATOM   305  O O    . GLU   A 1 40  ? -21.573 7.253   20.203  1.00 54.04  ? 40  GLU   A O    1 
ATOM   306  C CB   . GLU   A 1 40  ? -20.829 10.434  20.353  1.00 53.65  ? 40  GLU   A CB   1 
ATOM   307  C CG   . GLU   A 1 40  ? -21.776 10.106  21.499  1.00 57.05  ? 40  GLU   A CG   1 
ATOM   308  C CD   . GLU   A 1 40  ? -21.721 11.146  22.621  1.00 56.95  ? 40  GLU   A CD   1 
ATOM   309  O OE1  . GLU   A 1 40  ? -21.839 10.768  23.814  1.00 58.97  ? 40  GLU   A OE1  1 
ATOM   310  O OE2  . GLU   A 1 40  ? -21.539 12.348  22.299  1.00 56.56  ? 40  GLU   A OE2  1 
ATOM   311  N N    . GLY   A 1 41  ? -22.685 8.438   18.648  1.00 47.28  ? 41  GLY   A N    1 
ATOM   312  C CA   . GLY   A 1 41  ? -23.699 7.398   18.523  1.00 47.54  ? 41  GLY   A CA   1 
ATOM   313  C C    . GLY   A 1 41  ? -23.086 6.063   18.137  1.00 52.03  ? 41  GLY   A C    1 
ATOM   314  O O    . GLY   A 1 41  ? -23.420 5.014   18.708  1.00 50.95  ? 41  GLY   A O    1 
ATOM   315  N N    . ALA   A 1 42  ? -22.165 6.090   17.162  1.00 45.87  ? 42  ALA   A N    1 
ATOM   316  C CA   . ALA   A 1 42  ? -21.454 4.863   16.777  1.00 45.73  ? 42  ALA   A CA   1 
ATOM   317  C C    . ALA   A 1 42  ? -20.587 4.307   17.917  1.00 45.74  ? 42  ALA   A C    1 
ATOM   318  O O    . ALA   A 1 42  ? -20.523 3.085   18.131  1.00 44.67  ? 42  ALA   A O    1 
ATOM   319  C CB   . ALA   A 1 42  ? -20.586 5.122   15.542  1.00 42.95  ? 42  ALA   A CB   1 
ATOM   320  N N    . ILE   A 1 43  ? -19.850 5.182   18.603  1.00 45.67  ? 43  ILE   A N    1 
ATOM   321  C CA   . ILE   A 1 43  ? -18.932 4.742   19.649  1.00 44.12  ? 43  ILE   A CA   1 
ATOM   322  C C    . ILE   A 1 43  ? -19.714 4.094   20.787  1.00 46.09  ? 43  ILE   A C    1 
ATOM   323  O O    . ILE   A 1 43  ? -19.315 3.055   21.333  1.00 44.82  ? 43  ILE   A O    1 
ATOM   324  C CB   . ILE   A 1 43  ? -18.067 5.924   20.127  1.00 41.20  ? 43  ILE   A CB   1 
ATOM   325  C CG1  . ILE   A 1 43  ? -17.153 6.393   18.988  1.00 43.86  ? 43  ILE   A CG1  1 
ATOM   326  C CG2  . ILE   A 1 43  ? -17.212 5.517   21.304  1.00 39.19  ? 43  ILE   A CG2  1 
ATOM   327  C CD1  . ILE   A 1 43  ? -16.588 7.780   19.177  1.00 39.32  ? 43  ILE   A CD1  1 
ATOM   328  N N    . THR   A 1 44  ? -20.838 4.706   21.168  1.00 45.26  ? 44  THR   A N    1 
ATOM   329  C CA   . THR   A 1 44  ? -21.683 4.136   22.204  1.00 43.24  ? 44  THR   A CA   1 
ATOM   330  C C    . THR   A 1 44  ? -22.260 2.799   21.762  1.00 48.07  ? 44  THR   A C    1 
ATOM   331  O O    . THR   A 1 44  ? -22.235 1.827   22.521  1.00 47.63  ? 44  THR   A O    1 
ATOM   332  C CB   . THR   A 1 44  ? -22.797 5.117   22.567  1.00 44.90  ? 44  THR   A CB   1 
ATOM   333  O OG1  . THR   A 1 44  ? -23.364 5.675   21.370  1.00 49.40  ? 44  THR   A OG1  1 
ATOM   334  C CG2  . THR   A 1 44  ? -22.238 6.275   23.434  1.00 41.60  ? 44  THR   A CG2  1 
ATOM   335  N N    . SER   A 1 45  ? -22.731 2.701   20.514  1.00 42.84  ? 45  SER   A N    1 
ATOM   336  C CA   . SER   A 1 45  ? -23.232 1.405   20.060  1.00 43.25  ? 45  SER   A CA   1 
ATOM   337  C C    . SER   A 1 45  ? -22.147 0.329   20.161  1.00 44.31  ? 45  SER   A C    1 
ATOM   338  O O    . SER   A 1 45  ? -22.408 -0.787  20.628  1.00 46.60  ? 45  SER   A O    1 
ATOM   339  C CB   . SER   A 1 45  ? -23.744 1.506   18.620  1.00 43.56  ? 45  SER   A CB   1 
ATOM   340  O OG   . SER   A 1 45  ? -24.265 0.253   18.197  1.00 44.40  ? 45  SER   A OG   1 
ATOM   341  N N    . ALA   A 1 46  ? -20.926 0.643   19.715  1.00 43.78  ? 46  ALA   A N    1 
ATOM   342  C CA   . ALA   A 1 46  ? -19.823 -0.316  19.775  1.00 45.78  ? 46  ALA   A CA   1 
ATOM   343  C C    . ALA   A 1 46  ? -19.481 -0.709  21.214  1.00 50.50  ? 46  ALA   A C    1 
ATOM   344  O O    . ALA   A 1 46  ? -19.198 -1.883  21.493  1.00 48.66  ? 46  ALA   A O    1 
ATOM   345  C CB   . ALA   A 1 46  ? -18.599 0.265   19.066  1.00 43.87  ? 46  ALA   A CB   1 
ATOM   346  N N    . ALA   A 1 47  ? -19.461 0.265   22.137  1.00 49.01  ? 47  ALA   A N    1 
ATOM   347  C CA   . ALA   A 1 47  ? -19.213 -0.063  23.539  1.00 47.95  ? 47  ALA   A CA   1 
ATOM   348  C C    . ALA   A 1 47  ? -20.297 -0.986  24.087  1.00 47.12  ? 47  ALA   A C    1 
ATOM   349  O O    . ALA   A 1 47  ? -19.997 -1.986  24.748  1.00 49.33  ? 47  ALA   A O    1 
ATOM   350  C CB   . ALA   A 1 47  ? -19.113 1.218   24.376  1.00 43.35  ? 47  ALA   A CB   1 
ATOM   351  N N    . ASP   A 1 48  ? -21.565 -0.691  23.795  1.00 59.96  ? 48  ASP   A N    1 
ATOM   352  C CA   . ASP   A 1 48  ? -22.633 -1.560  24.279  1.00 62.51  ? 48  ASP   A CA   1 
ATOM   353  C C    . ASP   A 1 48  ? -22.504 -2.983  23.752  1.00 65.96  ? 48  ASP   A C    1 
ATOM   354  O O    . ASP   A 1 48  ? -23.046 -3.909  24.364  1.00 67.98  ? 48  ASP   A O    1 
ATOM   355  C CB   . ASP   A 1 48  ? -24.011 -0.997  23.913  1.00 63.30  ? 48  ASP   A CB   1 
ATOM   356  C CG   . ASP   A 1 48  ? -25.152 -1.775  24.578  1.00 69.07  ? 48  ASP   A CG   1 
ATOM   357  O OD1  . ASP   A 1 48  ? -25.622 -2.772  23.983  1.00 72.73  ? 48  ASP   A OD1  1 
ATOM   358  O OD2  . ASP   A 1 48  ? -25.546 -1.423  25.715  1.00 69.96  ? 48  ASP   A OD2  1 
ATOM   359  N N    . GLN   A 1 49  ? -21.814 -3.182  22.631  1.00 53.30  ? 49  GLN   A N    1 
ATOM   360  C CA   . GLN   A 1 49  ? -21.541 -4.515  22.117  1.00 53.17  ? 49  GLN   A CA   1 
ATOM   361  C C    . GLN   A 1 49  ? -20.155 -5.021  22.510  1.00 51.88  ? 49  GLN   A C    1 
ATOM   362  O O    . GLN   A 1 49  ? -19.705 -6.032  21.968  1.00 55.71  ? 49  GLN   A O    1 
ATOM   363  C CB   . GLN   A 1 49  ? -21.702 -4.529  20.579  1.00 56.24  ? 49  GLN   A CB   1 
ATOM   364  C CG   . GLN   A 1 49  ? -23.090 -4.079  20.106  1.00 52.74  ? 49  GLN   A CG   1 
ATOM   365  C CD   . GLN   A 1 49  ? -23.215 -3.905  18.598  1.00 55.68  ? 49  GLN   A CD   1 
ATOM   366  O OE1  . GLN   A 1 49  ? -23.136 -4.864  17.835  1.00 56.06  ? 49  GLN   A OE1  1 
ATOM   367  N NE2  . GLN   A 1 49  ? -23.427 -2.670  18.168  1.00 53.40  ? 49  GLN   A NE2  1 
ATOM   368  N N    . GLY   A 1 50  ? -19.484 -4.371  23.462  1.00 55.54  ? 50  GLY   A N    1 
ATOM   369  C CA   . GLY   A 1 50  ? -18.234 -4.898  23.963  1.00 54.95  ? 50  GLY   A CA   1 
ATOM   370  C C    . GLY   A 1 50  ? -17.008 -4.674  23.107  1.00 54.93  ? 50  GLY   A C    1 
ATOM   371  O O    . GLY   A 1 50  ? -16.019 -5.390  23.281  1.00 56.17  ? 50  GLY   A O    1 
ATOM   372  N N    . ALA   A 1 51  ? -17.028 -3.702  22.197  1.00 53.20  ? 51  ALA   A N    1 
ATOM   373  C CA   . ALA   A 1 51  ? -15.854 -3.427  21.375  1.00 51.26  ? 51  ALA   A CA   1 
ATOM   374  C C    . ALA   A 1 51  ? -14.681 -2.917  22.219  1.00 50.01  ? 51  ALA   A C    1 
ATOM   375  O O    . ALA   A 1 51  ? -14.857 -2.163  23.181  1.00 47.13  ? 51  ALA   A O    1 
ATOM   376  C CB   . ALA   A 1 51  ? -16.204 -2.414  20.282  1.00 47.79  ? 51  ALA   A CB   1 
ATOM   377  N N    . HIS   A 1 52  ? -13.467 -3.323  21.838  1.00 45.04  ? 52  HIS   A N    1 
ATOM   378  C CA   . HIS   A 1 52  ? -12.251 -2.827  22.470  1.00 43.05  ? 52  HIS   A CA   1 
ATOM   379  C C    . HIS   A 1 52  ? -11.679 -1.607  21.770  1.00 44.82  ? 52  HIS   A C    1 
ATOM   380  O O    . HIS   A 1 52  ? -10.986 -0.806  22.412  1.00 44.00  ? 52  HIS   A O    1 
ATOM   381  C CB   . HIS   A 1 52  ? -11.179 -3.916  22.491  1.00 43.22  ? 52  HIS   A CB   1 
ATOM   382  C CG   . HIS   A 1 52  ? -11.549 -5.098  23.320  1.00 45.11  ? 52  HIS   A CG   1 
ATOM   383  N ND1  . HIS   A 1 52  ? -12.190 -6.201  22.792  1.00 50.03  ? 52  HIS   A ND1  1 
ATOM   384  C CD2  . HIS   A 1 52  ? -11.388 -5.351  24.640  1.00 42.58  ? 52  HIS   A CD2  1 
ATOM   385  C CE1  . HIS   A 1 52  ? -12.405 -7.081  23.757  1.00 48.14  ? 52  HIS   A CE1  1 
ATOM   386  N NE2  . HIS   A 1 52  ? -11.923 -6.591  24.881  1.00 44.40  ? 52  HIS   A NE2  1 
ATOM   387  N N    . ILE   A 1 53  ? -11.919 -1.468  20.463  1.00 52.89  ? 53  ILE   A N    1 
ATOM   388  C CA   . ILE   A 1 53  ? -11.369 -0.373  19.669  1.00 51.92  ? 53  ILE   A CA   1 
ATOM   389  C C    . ILE   A 1 53  ? -12.317 -0.079  18.505  1.00 51.06  ? 53  ILE   A C    1 
ATOM   390  O O    . ILE   A 1 53  ? -12.888 -0.994  17.893  1.00 48.75  ? 53  ILE   A O    1 
ATOM   391  C CB   . ILE   A 1 53  ? -9.946  -0.715  19.165  1.00 51.58  ? 53  ILE   A CB   1 
ATOM   392  C CG1  . ILE   A 1 53  ? -9.351  0.465   18.388  1.00 46.62  ? 53  ILE   A CG1  1 
ATOM   393  C CG2  . ILE   A 1 53  ? -9.962  -2.012  18.316  1.00 49.99  ? 53  ILE   A CG2  1 
ATOM   394  C CD1  . ILE   A 1 53  ? -7.827  0.483   18.424  1.00 42.68  ? 53  ILE   A CD1  1 
ATOM   395  N N    . ILE   A 1 54  ? -12.486 1.208   18.201  1.00 43.49  ? 54  ILE   A N    1 
ATOM   396  C CA   . ILE   A 1 54  ? -13.315 1.643   17.080  1.00 43.78  ? 54  ILE   A CA   1 
ATOM   397  C C    . ILE   A 1 54  ? -12.533 2.659   16.240  1.00 42.00  ? 54  ILE   A C    1 
ATOM   398  O O    . ILE   A 1 54  ? -11.945 3.604   16.783  1.00 39.67  ? 54  ILE   A O    1 
ATOM   399  C CB   . ILE   A 1 54  ? -14.661 2.239   17.547  1.00 42.60  ? 54  ILE   A CB   1 
ATOM   400  C CG1  . ILE   A 1 54  ? -15.460 2.724   16.320  1.00 45.12  ? 54  ILE   A CG1  1 
ATOM   401  C CG2  . ILE   A 1 54  ? -14.435 3.379   18.546  1.00 40.51  ? 54  ILE   A CG2  1 
ATOM   402  C CD1  . ILE   A 1 54  ? -16.844 3.299   16.630  1.00 42.80  ? 54  ILE   A CD1  1 
ATOM   403  N N    . VAL   A 1 55  ? -12.530 2.477   14.920  1.00 41.50  ? 55  VAL   A N    1 
ATOM   404  C CA   . VAL   A 1 55  ? -11.890 3.423   13.998  1.00 39.29  ? 55  VAL   A CA   1 
ATOM   405  C C    . VAL   A 1 55  ? -12.975 4.223   13.292  1.00 37.00  ? 55  VAL   A C    1 
ATOM   406  O O    . VAL   A 1 55  ? -14.043 3.691   12.970  1.00 38.86  ? 55  VAL   A O    1 
ATOM   407  C CB   . VAL   A 1 55  ? -10.950 2.752   12.974  1.00 36.43  ? 55  VAL   A CB   1 
ATOM   408  C CG1  . VAL   A 1 55  ? -10.273 3.838   12.120  1.00 37.90  ? 55  VAL   A CG1  1 
ATOM   409  C CG2  . VAL   A 1 55  ? -9.875  1.919   13.690  1.00 36.25  ? 55  VAL   A CG2  1 
ATOM   410  N N    . THR   A 1 56  ? -12.723 5.512   13.113  1.00 38.24  ? 56  THR   A N    1 
ATOM   411  C CA   . THR   A 1 56  ? -13.580 6.412   12.355  1.00 43.12  ? 56  THR   A CA   1 
ATOM   412  C C    . THR   A 1 56  ? -12.848 7.023   11.156  1.00 38.57  ? 56  THR   A C    1 
ATOM   413  O O    . THR   A 1 56  ? -11.615 6.992   11.085  1.00 41.10  ? 56  THR   A O    1 
ATOM   414  C CB   . THR   A 1 56  ? -14.119 7.505   13.290  1.00 40.77  ? 56  THR   A CB   1 
ATOM   415  O OG1  . THR   A 1 56  ? -13.028 8.173   13.944  1.00 37.15  ? 56  THR   A OG1  1 
ATOM   416  C CG2  . THR   A 1 56  ? -15.019 6.879   14.320  1.00 40.35  ? 56  THR   A CG2  1 
ATOM   417  N N    . PRO   A 1 57  ? -13.566 7.566   10.189  1.00 40.85  ? 57  PRO   A N    1 
ATOM   418  C CA   . PRO   A 1 57  ? -12.949 7.836   8.878   1.00 43.40  ? 57  PRO   A CA   1 
ATOM   419  C C    . PRO   A 1 57  ? -12.048 9.064   8.873   1.00 43.81  ? 57  PRO   A C    1 
ATOM   420  O O    . PRO   A 1 57  ? -12.081 9.913   9.765   1.00 41.33  ? 57  PRO   A O    1 
ATOM   421  C CB   . PRO   A 1 57  ? -14.145 8.048   7.941   1.00 39.30  ? 57  PRO   A CB   1 
ATOM   422  C CG   . PRO   A 1 57  ? -15.357 7.608   8.698   1.00 44.18  ? 57  PRO   A CG   1 
ATOM   423  C CD   . PRO   A 1 57  ? -15.012 7.820   10.181  1.00 43.30  ? 57  PRO   A CD   1 
ATOM   424  N N    . GLU   A 1 58  ? -11.231 9.140   7.824   1.00 46.94  ? 58  GLU   A N    1 
ATOM   425  C CA   . GLU   A 1 58  ? -10.429 10.330  7.578   1.00 47.03  ? 58  GLU   A CA   1 
ATOM   426  C C    . GLU   A 1 58  ? -11.348 11.481  7.208   1.00 46.44  ? 58  GLU   A C    1 
ATOM   427  O O    . GLU   A 1 58  ? -12.385 11.276  6.576   1.00 49.72  ? 58  GLU   A O    1 
ATOM   428  C CB   . GLU   A 1 58  ? -9.402  10.074  6.465   1.00 49.57  ? 58  GLU   A CB   1 
ATOM   429  C CG   . GLU   A 1 58  ? -8.630  11.302  6.001   1.00 51.60  ? 58  GLU   A CG   1 
ATOM   430  C CD   . GLU   A 1 58  ? -7.789  11.040  4.740   1.00 54.41  ? 58  GLU   A CD   1 
ATOM   431  O OE1  . GLU   A 1 58  ? -8.146  10.125  3.956   1.00 55.38  ? 58  GLU   A OE1  1 
ATOM   432  O OE2  . GLU   A 1 58  ? -6.776  11.754  4.526   1.00 53.80  ? 58  GLU   A OE2  1 
ATOM   433  N N    . ASP   A 1 59  ? -11.014 12.686  7.676   1.00 47.75  ? 59  ASP   A N    1 
ATOM   434  C CA   . ASP   A 1 59  ? -11.796 13.891  7.388   1.00 48.76  ? 59  ASP   A CA   1 
ATOM   435  C C    . ASP   A 1 59  ? -13.225 13.789  7.919   1.00 46.98  ? 59  ASP   A C    1 
ATOM   436  O O    . ASP   A 1 59  ? -14.095 14.600  7.548   1.00 45.64  ? 59  ASP   A O    1 
ATOM   437  C CB   . ASP   A 1 59  ? -11.833 14.190  5.871   1.00 48.96  ? 59  ASP   A CB   1 
ATOM   438  C CG   . ASP   A 1 59  ? -10.512 14.736  5.328   1.00 49.18  ? 59  ASP   A CG   1 
ATOM   439  O OD1  . ASP   A 1 59  ? -9.690  15.283  6.093   1.00 48.57  ? 59  ASP   A OD1  1 
ATOM   440  O OD2  . ASP   A 1 59  ? -10.302 14.632  4.099   1.00 55.39  ? 59  ASP   A OD2  1 
ATOM   441  N N    . ALA   A 1 60  ? -13.478 12.818  8.802   1.00 48.45  ? 60  ALA   A N    1 
ATOM   442  C CA   . ALA   A 1 60  ? -14.844 12.514  9.233   1.00 46.92  ? 60  ALA   A CA   1 
ATOM   443  C C    . ALA   A 1 60  ? -15.468 13.646  10.041  1.00 45.01  ? 60  ALA   A C    1 
ATOM   444  O O    . ALA   A 1 60  ? -16.699 13.702  10.174  1.00 42.98  ? 60  ALA   A O    1 
ATOM   445  C CB   . ALA   A 1 60  ? -14.858 11.212  10.044  1.00 46.81  ? 60  ALA   A CB   1 
ATOM   446  N N    . ILE   A 1 61  ? -14.657 14.557  10.567  1.00 45.85  ? 61  ILE   A N    1 
ATOM   447  C CA   . ILE   A 1 61  ? -15.144 15.521  11.536  1.00 51.35  ? 61  ILE   A CA   1 
ATOM   448  C C    . ILE   A 1 61  ? -15.325 16.910  10.936  1.00 51.20  ? 61  ILE   A C    1 
ATOM   449  O O    . ILE   A 1 61  ? -16.195 17.661  11.398  1.00 51.36  ? 61  ILE   A O    1 
ATOM   450  C CB   . ILE   A 1 61  ? -14.213 15.561  12.774  1.00 48.85  ? 61  ILE   A CB   1 
ATOM   451  C CG1  . ILE   A 1 61  ? -14.288 14.208  13.472  1.00 45.99  ? 61  ILE   A CG1  1 
ATOM   452  C CG2  . ILE   A 1 61  ? -14.604 16.660  13.750  1.00 47.09  ? 61  ILE   A CG2  1 
ATOM   453  C CD1  . ILE   A 1 61  ? -13.032 13.815  14.208  1.00 48.46  ? 61  ILE   A CD1  1 
ATOM   454  N N    . TYR   A 1 62  ? -14.564 17.266  9.890   1.00 50.79  ? 62  TYR   A N    1 
ATOM   455  C CA   . TYR   A 1 62  ? -14.725 18.575  9.285   1.00 48.55  ? 62  TYR   A CA   1 
ATOM   456  C C    . TYR   A 1 62  ? -14.731 18.572  7.765   1.00 51.72  ? 62  TYR   A C    1 
ATOM   457  O O    . TYR   A 1 62  ? -14.903 19.644  7.172   1.00 54.05  ? 62  TYR   A O    1 
ATOM   458  C CB   . TYR   A 1 62  ? -13.648 19.534  9.815   1.00 49.16  ? 62  TYR   A CB   1 
ATOM   459  C CG   . TYR   A 1 62  ? -12.228 19.033  9.740   1.00 50.29  ? 62  TYR   A CG   1 
ATOM   460  C CD1  . TYR   A 1 62  ? -11.790 18.262  8.659   1.00 52.53  ? 62  TYR   A CD1  1 
ATOM   461  C CD2  . TYR   A 1 62  ? -11.307 19.385  10.705  1.00 47.83  ? 62  TYR   A CD2  1 
ATOM   462  C CE1  . TYR   A 1 62  ? -10.483 17.830  8.575   1.00 50.29  ? 62  TYR   A CE1  1 
ATOM   463  C CE2  . TYR   A 1 62  ? -9.989  18.963  10.623  1.00 49.42  ? 62  TYR   A CE2  1 
ATOM   464  C CZ   . TYR   A 1 62  ? -9.587  18.182  9.557   1.00 48.22  ? 62  TYR   A CZ   1 
ATOM   465  O OH   . TYR   A 1 62  ? -8.281  17.764  9.479   1.00 48.60  ? 62  TYR   A OH   1 
ATOM   466  N N    . GLY   A 1 63  ? -14.577 17.417  7.111   1.00 51.81  ? 63  GLY   A N    1 
ATOM   467  C CA   . GLY   A 1 63  ? -14.705 17.360  5.659   1.00 51.01  ? 63  GLY   A CA   1 
ATOM   468  C C    . GLY   A 1 63  ? -13.400 17.554  4.919   1.00 50.76  ? 63  GLY   A C    1 
ATOM   469  O O    . GLY   A 1 63  ? -12.306 17.564  5.487   1.00 49.38  ? 63  GLY   A O    1 
ATOM   470  N N    . TRP   A 1 64  ? -13.523 17.730  3.611   1.00 53.43  ? 64  TRP   A N    1 
ATOM   471  C CA   . TRP   A 1 64  ? -12.337 17.757  2.775   1.00 52.98  ? 64  TRP   A CA   1 
ATOM   472  C C    . TRP   A 1 64  ? -12.256 18.970  1.858   1.00 56.69  ? 64  TRP   A C    1 
ATOM   473  O O    . TRP   A 1 64  ? -11.325 19.047  1.053   1.00 55.72  ? 64  TRP   A O    1 
ATOM   474  C CB   . TRP   A 1 64  ? -12.257 16.466  1.950   1.00 52.26  ? 64  TRP   A CB   1 
ATOM   475  C CG   . TRP   A 1 64  ? -13.515 16.228  1.219   1.00 55.49  ? 64  TRP   A CG   1 
ATOM   476  C CD1  . TRP   A 1 64  ? -13.895 16.815  0.060   1.00 53.39  ? 64  TRP   A CD1  1 
ATOM   477  C CD2  . TRP   A 1 64  ? -14.586 15.359  1.601   1.00 55.51  ? 64  TRP   A CD2  1 
ATOM   478  N NE1  . TRP   A 1 64  ? -15.139 16.377  -0.312  1.00 55.92  ? 64  TRP   A NE1  1 
ATOM   479  C CE2  . TRP   A 1 64  ? -15.582 15.472  0.616   1.00 53.49  ? 64  TRP   A CE2  1 
ATOM   480  C CE3  . TRP   A 1 64  ? -14.794 14.486  2.675   1.00 54.16  ? 64  TRP   A CE3  1 
ATOM   481  C CZ2  . TRP   A 1 64  ? -16.777 14.754  0.668   1.00 53.00  ? 64  TRP   A CZ2  1 
ATOM   482  C CZ3  . TRP   A 1 64  ? -15.993 13.765  2.725   1.00 53.27  ? 64  TRP   A CZ3  1 
ATOM   483  C CH2  . TRP   A 1 64  ? -16.969 13.917  1.728   1.00 54.45  ? 64  TRP   A CH2  1 
ATOM   484  N N    . ASN   A 1 65  ? -13.172 19.928  1.972   1.00 61.42  ? 65  ASN   A N    1 
ATOM   485  C CA   . ASN   A 1 65  ? -13.197 21.099  1.096   1.00 62.28  ? 65  ASN   A CA   1 
ATOM   486  C C    . ASN   A 1 65  ? -12.550 22.293  1.791   1.00 61.45  ? 65  ASN   A C    1 
ATOM   487  O O    . ASN   A 1 65  ? -13.230 23.142  2.364   1.00 64.75  ? 65  ASN   A O    1 
ATOM   488  C CB   . ASN   A 1 65  ? -14.636 21.392  0.704   1.00 65.78  ? 65  ASN   A CB   1 
ATOM   489  C CG   . ASN   A 1 65  ? -15.109 20.509  -0.429  1.00 66.65  ? 65  ASN   A CG   1 
ATOM   490  O OD1  . ASN   A 1 65  ? -16.244 20.014  -0.413  1.00 65.66  ? 65  ASN   A OD1  1 
ATOM   491  N ND2  . ASN   A 1 65  ? -14.251 20.323  -1.440  1.00 72.00  ? 65  ASN   A ND2  1 
ATOM   492  N N    . PHE   A 1 66  ? -11.232 22.413  1.662   1.00 55.79  ? 66  PHE   A N    1 
ATOM   493  C CA   . PHE   A 1 66  ? -10.505 23.431  2.406   1.00 57.89  ? 66  PHE   A CA   1 
ATOM   494  C C    . PHE   A 1 66  ? -9.359  24.006  1.593   1.00 56.23  ? 66  PHE   A C    1 
ATOM   495  O O    . PHE   A 1 66  ? -8.714  23.295  0.817   1.00 58.65  ? 66  PHE   A O    1 
ATOM   496  C CB   . PHE   A 1 66  ? -9.917  22.855  3.712   1.00 58.33  ? 66  PHE   A CB   1 
ATOM   497  C CG   . PHE   A 1 66  ? -10.913 22.666  4.816   1.00 55.33  ? 66  PHE   A CG   1 
ATOM   498  C CD1  . PHE   A 1 66  ? -11.523 23.758  5.415   1.00 54.13  ? 66  PHE   A CD1  1 
ATOM   499  C CD2  . PHE   A 1 66  ? -11.210 21.392  5.285   1.00 56.62  ? 66  PHE   A CD2  1 
ATOM   500  C CE1  . PHE   A 1 66  ? -12.431 23.587  6.455   1.00 53.99  ? 66  PHE   A CE1  1 
ATOM   501  C CE2  . PHE   A 1 66  ? -12.116 21.210  6.328   1.00 55.19  ? 66  PHE   A CE2  1 
ATOM   502  C CZ   . PHE   A 1 66  ? -12.726 22.310  6.913   1.00 53.54  ? 66  PHE   A CZ   1 
ATOM   503  N N    . ASN   A 1 67  ? -9.121  25.300  1.762   1.00 59.92  ? 67  ASN   A N    1 
ATOM   504  C CA   . ASN   A 1 67  ? -7.793  25.861  1.587   1.00 59.47  ? 67  ASN   A CA   1 
ATOM   505  C C    . ASN   A 1 67  ? -7.193  26.092  2.972   1.00 58.97  ? 67  ASN   A C    1 
ATOM   506  O O    . ASN   A 1 67  ? -7.838  25.870  4.001   1.00 57.67  ? 67  ASN   A O    1 
ATOM   507  C CB   . ASN   A 1 67  ? -7.834  27.147  0.767   1.00 57.63  ? 67  ASN   A CB   1 
ATOM   508  C CG   . ASN   A 1 67  ? -8.639  28.213  1.431   1.00 60.94  ? 67  ASN   A CG   1 
ATOM   509  O OD1  . ASN   A 1 67  ? -8.313  28.649  2.530   1.00 62.22  ? 67  ASN   A OD1  1 
ATOM   510  N ND2  . ASN   A 1 67  ? -9.704  28.643  0.778   1.00 60.92  ? 67  ASN   A ND2  1 
ATOM   511  N N    . ARG   A 1 68  ? -5.945  26.560  3.001   1.00 56.91  ? 68  ARG   A N    1 
ATOM   512  C CA   . ARG   A 1 68  ? -5.225  26.662  4.266   1.00 59.21  ? 68  ARG   A CA   1 
ATOM   513  C C    . ARG   A 1 68  ? -5.975  27.536  5.261   1.00 60.29  ? 68  ARG   A C    1 
ATOM   514  O O    . ARG   A 1 68  ? -6.169  27.157  6.430   1.00 62.91  ? 68  ARG   A O    1 
ATOM   515  C CB   . ARG   A 1 68  ? -3.819  27.200  4.012   1.00 57.96  ? 68  ARG   A CB   1 
ATOM   516  C CG   . ARG   A 1 68  ? -2.890  26.160  3.417   1.00 60.87  ? 68  ARG   A CG   1 
ATOM   517  C CD   . ARG   A 1 68  ? -1.483  26.696  3.247   1.00 59.17  ? 68  ARG   A CD   1 
ATOM   518  N NE   . ARG   A 1 68  ? -0.836  26.908  4.537   1.00 61.98  ? 68  ARG   A NE   1 
ATOM   519  C CZ   . ARG   A 1 68  ? -0.198  25.970  5.221   1.00 61.32  ? 68  ARG   A CZ   1 
ATOM   520  N NH1  . ARG   A 1 68  ? -0.145  24.717  4.793   1.00 59.43  ? 68  ARG   A NH1  1 
ATOM   521  N NH2  . ARG   A 1 68  ? 0.422   26.302  6.349   1.00 57.53  ? 68  ARG   A NH2  1 
ATOM   522  N N    . ASP   A 1 69  ? -6.419  28.708  4.815   1.00 57.02  ? 69  ASP   A N    1 
ATOM   523  C CA   . ASP   A 1 69  ? -7.006  29.658  5.747   1.00 60.01  ? 69  ASP   A CA   1 
ATOM   524  C C    . ASP   A 1 69  ? -8.394  29.220  6.197   1.00 60.55  ? 69  ASP   A C    1 
ATOM   525  O O    . ASP   A 1 69  ? -8.709  29.279  7.392   1.00 57.08  ? 69  ASP   A O    1 
ATOM   526  C CB   . ASP   A 1 69  ? -7.043  31.045  5.119   1.00 57.77  ? 69  ASP   A CB   1 
ATOM   527  C CG   . ASP   A 1 69  ? -5.665  31.663  5.037   1.00 61.35  ? 69  ASP   A CG   1 
ATOM   528  O OD1  . ASP   A 1 69  ? -4.844  31.376  5.928   1.00 59.64  ? 69  ASP   A OD1  1 
ATOM   529  O OD2  . ASP   A 1 69  ? -5.405  32.451  4.102   1.00 67.40  ? 69  ASP   A OD2  1 
ATOM   530  N N    . SER   A 1 70  ? -9.221  28.728  5.276   1.00 63.40  ? 70  SER   A N    1 
ATOM   531  C CA   . SER   A 1 70  ? -10.537 28.278  5.706   1.00 63.05  ? 70  SER   A CA   1 
ATOM   532  C C    . SER   A 1 70  ? -10.446 27.057  6.617   1.00 58.30  ? 70  SER   A C    1 
ATOM   533  O O    . SER   A 1 70  ? -11.380 26.812  7.381   1.00 59.58  ? 70  SER   A O    1 
ATOM   534  C CB   . SER   A 1 70  ? -11.450 28.014  4.498   1.00 58.62  ? 70  SER   A CB   1 
ATOM   535  O OG   . SER   A 1 70  ? -11.014 26.918  3.719   1.00 63.08  ? 70  SER   A OG   1 
ATOM   536  N N    . LEU   A 1 71  ? -9.357  26.280  6.547   1.00 47.44  ? 71  LEU   A N    1 
ATOM   537  C CA   . LEU   A 1 71  ? -9.160  25.171  7.479   1.00 46.43  ? 71  LEU   A CA   1 
ATOM   538  C C    . LEU   A 1 71  ? -8.637  25.636  8.834   1.00 48.97  ? 71  LEU   A C    1 
ATOM   539  O O    . LEU   A 1 71  ? -8.928  25.001  9.857   1.00 43.71  ? 71  LEU   A O    1 
ATOM   540  C CB   . LEU   A 1 71  ? -8.201  24.119  6.908   1.00 45.66  ? 71  LEU   A CB   1 
ATOM   541  C CG   . LEU   A 1 71  ? -7.782  23.022  7.917   1.00 45.02  ? 71  LEU   A CG   1 
ATOM   542  C CD1  . LEU   A 1 71  ? -8.901  22.013  8.171   1.00 42.88  ? 71  LEU   A CD1  1 
ATOM   543  C CD2  . LEU   A 1 71  ? -6.500  22.270  7.517   1.00 43.06  ? 71  LEU   A CD2  1 
ATOM   544  N N    . TYR   A 1 72  ? -7.866  26.725  8.869   1.00 57.52  ? 72  TYR   A N    1 
ATOM   545  C CA   . TYR   A 1 72  ? -7.202  27.097  10.119  1.00 57.98  ? 72  TYR   A CA   1 
ATOM   546  C C    . TYR   A 1 72  ? -8.133  27.098  11.329  1.00 56.03  ? 72  TYR   A C    1 
ATOM   547  O O    . TYR   A 1 72  ? -7.778  26.491  12.349  1.00 56.05  ? 72  TYR   A O    1 
ATOM   548  C CB   . TYR   A 1 72  ? -6.540  28.467  9.944   1.00 58.15  ? 72  TYR   A CB   1 
ATOM   549  C CG   . TYR   A 1 72  ? -5.700  28.847  11.120  1.00 55.41  ? 72  TYR   A CG   1 
ATOM   550  C CD1  . TYR   A 1 72  ? -4.415  28.352  11.259  1.00 55.90  ? 72  TYR   A CD1  1 
ATOM   551  C CD2  . TYR   A 1 72  ? -6.205  29.674  12.117  1.00 59.64  ? 72  TYR   A CD2  1 
ATOM   552  C CE1  . TYR   A 1 72  ? -3.641  28.689  12.353  1.00 57.99  ? 72  TYR   A CE1  1 
ATOM   553  C CE2  . TYR   A 1 72  ? -5.446  30.010  13.220  1.00 55.96  ? 72  TYR   A CE2  1 
ATOM   554  C CZ   . TYR   A 1 72  ? -4.163  29.519  13.327  1.00 57.87  ? 72  TYR   A CZ   1 
ATOM   555  O OH   . TYR   A 1 72  ? -3.391  29.849  14.412  1.00 64.36  ? 72  TYR   A OH   1 
ATOM   556  N N    . PRO   A 1 73  ? -9.329  27.687  11.279  1.00 52.23  ? 73  PRO   A N    1 
ATOM   557  C CA   . PRO   A 1 73  ? -10.177 27.705  12.482  1.00 48.43  ? 73  PRO   A CA   1 
ATOM   558  C C    . PRO   A 1 73  ? -10.534 26.319  13.008  1.00 51.43  ? 73  PRO   A C    1 
ATOM   559  O O    . PRO   A 1 73  ? -10.994 26.209  14.156  1.00 50.03  ? 73  PRO   A O    1 
ATOM   560  C CB   . PRO   A 1 73  ? -11.431 28.467  12.024  1.00 49.56  ? 73  PRO   A CB   1 
ATOM   561  C CG   . PRO   A 1 73  ? -11.344 28.544  10.506  1.00 50.06  ? 73  PRO   A CG   1 
ATOM   562  C CD   . PRO   A 1 73  ? -9.879  28.539  10.205  1.00 48.92  ? 73  PRO   A CD   1 
ATOM   563  N N    . TYR   A 1 74  ? -10.368 25.260  12.214  1.00 49.90  ? 74  TYR   A N    1 
ATOM   564  C CA   . TYR   A 1 74  ? -10.672 23.917  12.691  1.00 46.47  ? 74  TYR   A CA   1 
ATOM   565  C C    . TYR   A 1 74  ? -9.504  23.245  13.405  1.00 43.28  ? 74  TYR   A C    1 
ATOM   566  O O    . TYR   A 1 74  ? -9.687  22.166  13.979  1.00 44.05  ? 74  TYR   A O    1 
ATOM   567  C CB   . TYR   A 1 74  ? -11.125 23.034  11.528  1.00 42.26  ? 74  TYR   A CB   1 
ATOM   568  C CG   . TYR   A 1 74  ? -12.388 23.523  10.856  1.00 44.50  ? 74  TYR   A CG   1 
ATOM   569  C CD1  . TYR   A 1 74  ? -12.351 24.546  9.897   1.00 47.36  ? 74  TYR   A CD1  1 
ATOM   570  C CD2  . TYR   A 1 74  ? -13.622 22.954  11.156  1.00 43.51  ? 74  TYR   A CD2  1 
ATOM   571  C CE1  . TYR   A 1 74  ? -13.514 24.997  9.286   1.00 45.16  ? 74  TYR   A CE1  1 
ATOM   572  C CE2  . TYR   A 1 74  ? -14.796 23.395  10.535  1.00 43.08  ? 74  TYR   A CE2  1 
ATOM   573  C CZ   . TYR   A 1 74  ? -14.733 24.416  9.611   1.00 46.59  ? 74  TYR   A CZ   1 
ATOM   574  O OH   . TYR   A 1 74  ? -15.901 24.842  9.007   1.00 49.88  ? 74  TYR   A OH   1 
ATOM   575  N N    . LEU   A 1 75  ? -8.317  23.835  13.392  1.00 38.56  ? 75  LEU   A N    1 
ATOM   576  C CA   . LEU   A 1 75  ? -7.136  23.136  13.868  1.00 38.20  ? 75  LEU   A CA   1 
ATOM   577  C C    . LEU   A 1 75  ? -6.982  23.274  15.394  1.00 45.58  ? 75  LEU   A C    1 
ATOM   578  O O    . LEU   A 1 75  ? -7.465  24.226  16.028  1.00 40.83  ? 75  LEU   A O    1 
ATOM   579  C CB   . LEU   A 1 75  ? -5.883  23.647  13.144  1.00 39.64  ? 75  LEU   A CB   1 
ATOM   580  C CG   . LEU   A 1 75  ? -5.824  23.511  11.586  1.00 42.01  ? 75  LEU   A CG   1 
ATOM   581  C CD1  . LEU   A 1 75  ? -4.648  24.240  10.973  1.00 40.05  ? 75  LEU   A CD1  1 
ATOM   582  C CD2  . LEU   A 1 75  ? -5.812  22.050  11.078  1.00 37.90  ? 75  LEU   A CD2  1 
ATOM   583  N N    . GLU   A 1 76  ? -6.351  22.272  15.988  1.00 48.96  ? 76  GLU   A N    1 
ATOM   584  C CA   . GLU   A 1 76  ? -5.918  22.349  17.364  1.00 50.04  ? 76  GLU   A CA   1 
ATOM   585  C C    . GLU   A 1 76  ? -4.442  21.993  17.380  1.00 51.69  ? 76  GLU   A C    1 
ATOM   586  O O    . GLU   A 1 76  ? -3.939  21.312  16.477  1.00 50.36  ? 76  GLU   A O    1 
ATOM   587  C CB   . GLU   A 1 76  ? -6.747  21.423  18.280  1.00 50.05  ? 76  GLU   A CB   1 
ATOM   588  C CG   . GLU   A 1 76  ? -8.199  21.895  18.482  1.00 50.67  ? 76  GLU   A CG   1 
ATOM   589  C CD   . GLU   A 1 76  ? -9.014  20.941  19.331  1.00 48.76  ? 76  GLU   A CD   1 
ATOM   590  O OE1  . GLU   A 1 76  ? -8.436  19.937  19.804  1.00 47.35  ? 76  GLU   A OE1  1 
ATOM   591  O OE2  . GLU   A 1 76  ? -10.231 21.180  19.514  1.00 50.46  ? 76  GLU   A OE2  1 
ATOM   592  N N    . ASP   A 1 77  ? -3.732  22.549  18.350  1.00 49.84  ? 77  ASP   A N    1 
ATOM   593  C CA   . ASP   A 1 77  ? -2.317  22.246  18.547  1.00 49.63  ? 77  ASP   A CA   1 
ATOM   594  C C    . ASP   A 1 77  ? -2.246  20.958  19.371  1.00 50.61  ? 77  ASP   A C    1 
ATOM   595  O O    . ASP   A 1 77  ? -2.394  20.982  20.603  1.00 49.89  ? 77  ASP   A O    1 
ATOM   596  C CB   . ASP   A 1 77  ? -1.630  23.424  19.234  1.00 47.65  ? 77  ASP   A CB   1 
ATOM   597  C CG   . ASP   A 1 77  ? -0.119  23.384  19.122  1.00 48.29  ? 77  ASP   A CG   1 
ATOM   598  O OD1  . ASP   A 1 77  ? 0.458   22.273  19.168  1.00 46.37  ? 77  ASP   A OD1  1 
ATOM   599  O OD2  . ASP   A 1 77  ? 0.499   24.469  19.028  1.00 47.72  ? 77  ASP   A OD2  1 
ATOM   600  N N    . ILE   A 1 78  ? -2.004  19.834  18.696  1.00 49.19  ? 78  ILE   A N    1 
ATOM   601  C CA   . ILE   A 1 78  ? -2.071  18.511  19.313  1.00 45.83  ? 78  ILE   A CA   1 
ATOM   602  C C    . ILE   A 1 78  ? -0.688  18.184  19.867  1.00 47.69  ? 78  ILE   A C    1 
ATOM   603  O O    . ILE   A 1 78  ? 0.265   18.063  19.076  1.00 45.91  ? 78  ILE   A O    1 
ATOM   604  C CB   . ILE   A 1 78  ? -2.507  17.439  18.301  1.00 46.32  ? 78  ILE   A CB   1 
ATOM   605  C CG1  . ILE   A 1 78  ? -3.809  17.824  17.596  1.00 45.99  ? 78  ILE   A CG1  1 
ATOM   606  C CG2  . ILE   A 1 78  ? -2.654  16.090  18.988  1.00 46.85  ? 78  ILE   A CG2  1 
ATOM   607  C CD1  . ILE   A 1 78  ? -4.234  16.845  16.500  1.00 45.06  ? 78  ILE   A CD1  1 
ATOM   608  N N    . PRO   A 1 79  ? -0.535  18.005  21.185  1.00 35.92  ? 79  PRO   A N    1 
ATOM   609  C CA   . PRO   A 1 79  ? 0.801   17.727  21.742  1.00 37.04  ? 79  PRO   A CA   1 
ATOM   610  C C    . PRO   A 1 79  ? 1.285   16.345  21.343  1.00 36.01  ? 79  PRO   A C    1 
ATOM   611  O O    . PRO   A 1 79  ? 0.514   15.499  20.887  1.00 37.26  ? 79  PRO   A O    1 
ATOM   612  C CB   . PRO   A 1 79  ? 0.601   17.812  23.275  1.00 36.02  ? 79  PRO   A CB   1 
ATOM   613  C CG   . PRO   A 1 79  ? -0.861  17.540  23.494  1.00 35.99  ? 79  PRO   A CG   1 
ATOM   614  C CD   . PRO   A 1 79  ? -1.584  18.074  22.218  1.00 36.66  ? 79  PRO   A CD   1 
ATOM   615  N N    . ASP   A 1 80  ? 2.588   16.122  21.522  1.00 49.16  ? 80  ASP   A N    1 
ATOM   616  C CA   . ASP   A 1 80  ? 3.125   14.767  21.426  1.00 50.07  ? 80  ASP   A CA   1 
ATOM   617  C C    . ASP   A 1 80  ? 2.595   13.917  22.586  1.00 51.90  ? 80  ASP   A C    1 
ATOM   618  O O    . ASP   A 1 80  ? 2.576   14.376  23.738  1.00 50.84  ? 80  ASP   A O    1 
ATOM   619  C CB   . ASP   A 1 80  ? 4.647   14.789  21.472  1.00 49.61  ? 80  ASP   A CB   1 
ATOM   620  C CG   . ASP   A 1 80  ? 5.253   13.436  21.195  1.00 54.36  ? 80  ASP   A CG   1 
ATOM   621  O OD1  . ASP   A 1 80  ? 4.926   12.468  21.910  1.00 57.65  ? 80  ASP   A OD1  1 
ATOM   622  O OD2  . ASP   A 1 80  ? 6.059   13.335  20.251  1.00 59.10  ? 80  ASP   A OD2  1 
ATOM   623  N N    . PRO   A 1 81  ? 2.177   12.674  22.324  1.00 57.17  ? 81  PRO   A N    1 
ATOM   624  C CA   . PRO   A 1 81  ? 1.610   11.850  23.408  1.00 55.64  ? 81  PRO   A CA   1 
ATOM   625  C C    . PRO   A 1 81  ? 2.550   11.643  24.588  1.00 59.49  ? 81  PRO   A C    1 
ATOM   626  O O    . PRO   A 1 81  ? 2.082   11.272  25.676  1.00 54.31  ? 81  PRO   A O    1 
ATOM   627  C CB   . PRO   A 1 81  ? 1.281   10.526  22.711  1.00 54.93  ? 81  PRO   A CB   1 
ATOM   628  C CG   . PRO   A 1 81  ? 1.060   10.924  21.254  1.00 55.77  ? 81  PRO   A CG   1 
ATOM   629  C CD   . PRO   A 1 81  ? 2.023   12.050  20.997  1.00 53.79  ? 81  PRO   A CD   1 
ATOM   630  N N    . GLU   A 1 82  ? 3.852   11.889  24.421  1.00 68.26  ? 82  GLU   A N    1 
ATOM   631  C CA   . GLU   A 1 82  ? 4.776   11.757  25.543  1.00 68.47  ? 82  GLU   A CA   1 
ATOM   632  C C    . GLU   A 1 82  ? 4.467   12.725  26.675  1.00 64.21  ? 82  GLU   A C    1 
ATOM   633  O O    . GLU   A 1 82  ? 5.047   12.586  27.752  1.00 68.76  ? 82  GLU   A O    1 
ATOM   634  C CB   . GLU   A 1 82  ? 6.222   11.943  25.071  1.00 69.61  ? 82  GLU   A CB   1 
ATOM   635  C CG   . GLU   A 1 82  ? 6.626   13.389  24.850  1.00 71.92  ? 82  GLU   A CG   1 
ATOM   636  C CD   . GLU   A 1 82  ? 7.938   13.507  24.088  1.00 79.56  ? 82  GLU   A CD   1 
ATOM   637  O OE1  . GLU   A 1 82  ? 8.153   14.547  23.421  1.00 81.77  ? 82  GLU   A OE1  1 
ATOM   638  O OE2  . GLU   A 1 82  ? 8.756   12.552  24.161  1.00 80.15  ? 82  GLU   A OE2  1 
ATOM   639  N N    . VAL   A 1 83  ? 3.609   13.723  26.454  1.00 43.04  ? 83  VAL   A N    1 
ATOM   640  C CA   . VAL   A 1 83  ? 3.206   14.600  27.542  1.00 41.42  ? 83  VAL   A CA   1 
ATOM   641  C C    . VAL   A 1 83  ? 2.317   13.885  28.542  1.00 45.11  ? 83  VAL   A C    1 
ATOM   642  O O    . VAL   A 1 83  ? 2.047   14.449  29.604  1.00 44.58  ? 83  VAL   A O    1 
ATOM   643  C CB   . VAL   A 1 83  ? 2.470   15.880  27.084  1.00 41.39  ? 83  VAL   A CB   1 
ATOM   644  C CG1  . VAL   A 1 83  ? 3.243   16.616  25.988  1.00 39.19  ? 83  VAL   A CG1  1 
ATOM   645  C CG2  . VAL   A 1 83  ? 1.018   15.593  26.707  1.00 36.34  ? 83  VAL   A CG2  1 
ATOM   646  N N    . ASN   A 1 84  ? 1.825   12.683  28.221  1.00 48.67  ? 84  ASN   A N    1 
ATOM   647  C CA   . ASN   A 1 84  ? 1.102   11.853  29.184  1.00 50.66  ? 84  ASN   A CA   1 
ATOM   648  C C    . ASN   A 1 84  ? -0.144  12.584  29.703  1.00 50.85  ? 84  ASN   A C    1 
ATOM   649  O O    . ASN   A 1 84  ? -0.234  12.997  30.863  1.00 54.54  ? 84  ASN   A O    1 
ATOM   650  C CB   . ASN   A 1 84  ? 2.058   11.455  30.317  1.00 50.71  ? 84  ASN   A CB   1 
ATOM   651  C CG   . ASN   A 1 84  ? 1.446   10.456  31.313  1.00 52.62  ? 84  ASN   A CG   1 
ATOM   652  O OD1  . ASN   A 1 84  ? 0.315   9.998   31.158  1.00 56.84  ? 84  ASN   A OD1  1 
ATOM   653  N ND2  . ASN   A 1 84  ? 2.212   10.114  32.333  1.00 50.04  ? 84  ASN   A ND2  1 
ATOM   654  N N    . TRP   A 1 85  ? -1.087  12.786  28.778  1.00 47.05  ? 85  TRP   A N    1 
ATOM   655  C CA   . TRP   A 1 85  ? -2.253  13.640  28.988  1.00 44.47  ? 85  TRP   A CA   1 
ATOM   656  C C    . TRP   A 1 85  ? -3.543  12.903  28.641  1.00 45.78  ? 85  TRP   A C    1 
ATOM   657  O O    . TRP   A 1 85  ? -3.656  12.315  27.558  1.00 45.91  ? 85  TRP   A O    1 
ATOM   658  C CB   . TRP   A 1 85  ? -2.127  14.904  28.137  1.00 43.22  ? 85  TRP   A CB   1 
ATOM   659  C CG   . TRP   A 1 85  ? -3.288  15.849  28.209  1.00 44.75  ? 85  TRP   A CG   1 
ATOM   660  C CD1  . TRP   A 1 85  ? -4.002  16.196  29.323  1.00 46.06  ? 85  TRP   A CD1  1 
ATOM   661  C CD2  . TRP   A 1 85  ? -3.845  16.604  27.122  1.00 44.12  ? 85  TRP   A CD2  1 
ATOM   662  N NE1  . TRP   A 1 85  ? -4.980  17.110  28.990  1.00 48.18  ? 85  TRP   A NE1  1 
ATOM   663  C CE2  . TRP   A 1 85  ? -4.899  17.374  27.645  1.00 42.84  ? 85  TRP   A CE2  1 
ATOM   664  C CE3  . TRP   A 1 85  ? -3.565  16.679  25.744  1.00 44.30  ? 85  TRP   A CE3  1 
ATOM   665  C CZ2  . TRP   A 1 85  ? -5.670  18.210  26.852  1.00 46.23  ? 85  TRP   A CZ2  1 
ATOM   666  C CZ3  . TRP   A 1 85  ? -4.329  17.523  24.954  1.00 41.79  ? 85  TRP   A CZ3  1 
ATOM   667  C CH2  . TRP   A 1 85  ? -5.373  18.276  25.506  1.00 41.75  ? 85  TRP   A CH2  1 
ATOM   668  N N    . ILE   A 1 86  ? -4.513  12.956  29.551  1.00 44.25  ? 86  ILE   A N    1 
ATOM   669  C CA   . ILE   A 1 86  ? -5.893  12.527  29.321  1.00 44.85  ? 86  ILE   A CA   1 
ATOM   670  C C    . ILE   A 1 86  ? -6.753  13.786  29.265  1.00 47.43  ? 86  ILE   A C    1 
ATOM   671  O O    . ILE   A 1 86  ? -7.136  14.312  30.328  1.00 47.78  ? 86  ILE   A O    1 
ATOM   672  C CB   . ILE   A 1 86  ? -6.408  11.599  30.437  1.00 43.18  ? 86  ILE   A CB   1 
ATOM   673  C CG1  . ILE   A 1 86  ? -5.595  10.305  30.547  1.00 44.04  ? 86  ILE   A CG1  1 
ATOM   674  C CG2  . ILE   A 1 86  ? -7.893  11.295  30.253  1.00 42.29  ? 86  ILE   A CG2  1 
ATOM   675  C CD1  . ILE   A 1 86  ? -5.786  9.573   31.913  1.00 41.46  ? 86  ILE   A CD1  1 
ATOM   676  N N    . PRO   A 1 87  ? -7.098  14.295  28.078  1.00 46.69  ? 87  PRO   A N    1 
ATOM   677  C CA   . PRO   A 1 87  ? -7.872  15.549  28.025  1.00 44.82  ? 87  PRO   A CA   1 
ATOM   678  C C    . PRO   A 1 87  ? -9.159  15.507  28.829  1.00 45.25  ? 87  PRO   A C    1 
ATOM   679  O O    . PRO   A 1 87  ? -9.566  16.543  29.375  1.00 45.91  ? 87  PRO   A O    1 
ATOM   680  C CB   . PRO   A 1 87  ? -8.137  15.737  26.515  1.00 43.83  ? 87  PRO   A CB   1 
ATOM   681  C CG   . PRO   A 1 87  ? -6.971  15.087  25.848  1.00 40.89  ? 87  PRO   A CG   1 
ATOM   682  C CD   . PRO   A 1 87  ? -6.619  13.885  26.740  1.00 45.03  ? 87  PRO   A CD   1 
ATOM   683  N N    . CYS   A 1 88  ? -9.806  14.346  28.951  1.00 50.19  ? 88  CYS   A N    1 
ATOM   684  C CA   . CYS   A 1 88  ? -11.075 14.302  29.668  1.00 50.92  ? 88  CYS   A CA   1 
ATOM   685  C C    . CYS   A 1 88  ? -10.922 14.770  31.109  1.00 52.72  ? 88  CYS   A C    1 
ATOM   686  O O    . CYS   A 1 88  ? -11.796 15.471  31.631  1.00 52.44  ? 88  CYS   A O    1 
ATOM   687  C CB   . CYS   A 1 88  ? -11.654 12.888  29.661  1.00 50.83  ? 88  CYS   A CB   1 
ATOM   688  S SG   . CYS   A 1 88  ? -13.466 12.886  29.960  1.00 54.50  ? 88  CYS   A SG   1 
ATOM   689  N N    . ASN   A 1 89  ? -9.820  14.387  31.764  1.00 49.63  ? 89  ASN   A N    1 
ATOM   690  C CA   . ASN   A 1 89  ? -9.583  14.612  33.197  1.00 49.80  ? 89  ASN   A CA   1 
ATOM   691  C C    . ASN   A 1 89  ? -8.838  15.912  33.477  1.00 51.87  ? 89  ASN   A C    1 
ATOM   692  O O    . ASN   A 1 89  ? -9.085  16.564  34.498  1.00 52.79  ? 89  ASN   A O    1 
ATOM   693  C CB   . ASN   A 1 89  ? -8.791  13.447  33.798  1.00 43.40  ? 89  ASN   A CB   1 
ATOM   694  C CG   . ASN   A 1 89  ? -9.436  12.078  33.529  1.00 49.47  ? 89  ASN   A CG   1 
ATOM   695  O OD1  . ASN   A 1 89  ? -10.644 11.959  33.282  1.00 46.52  ? 89  ASN   A OD1  1 
ATOM   696  N ND2  . ASN   A 1 89  ? -8.623  11.038  33.589  1.00 50.86  ? 89  ASN   A ND2  1 
ATOM   697  N N    . ASN   A 1 90  ? -7.835  16.226  32.665  1.00 49.65  ? 90  ASN   A N    1 
ATOM   698  C CA   . ASN   A 1 90  ? -7.152  17.504  32.713  1.00 48.86  ? 90  ASN   A CA   1 
ATOM   699  C C    . ASN   A 1 90  ? -7.504  18.316  31.469  1.00 51.75  ? 90  ASN   A C    1 
ATOM   700  O O    . ASN   A 1 90  ? -6.668  18.534  30.578  1.00 51.17  ? 90  ASN   A O    1 
ATOM   701  C CB   . ASN   A 1 90  ? -5.657  17.259  32.819  1.00 45.99  ? 90  ASN   A CB   1 
ATOM   702  C CG   . ASN   A 1 90  ? -4.912  18.443  33.330  1.00 49.18  ? 90  ASN   A CG   1 
ATOM   703  O OD1  . ASN   A 1 90  ? -5.506  19.470  33.700  1.00 50.79  ? 90  ASN   A OD1  1 
ATOM   704  N ND2  . ASN   A 1 90  ? -3.590  18.313  33.377  1.00 49.82  ? 90  ASN   A ND2  1 
ATOM   705  N N    . ARG   A 1 91  ? -8.730  18.818  31.415  1.00 76.10  ? 91  ARG   A N    1 
ATOM   706  C CA   . ARG   A 1 91  ? -8.966  19.818  30.395  1.00 77.21  ? 91  ARG   A CA   1 
ATOM   707  C C    . ARG   A 1 91  ? -8.230  21.073  30.826  1.00 77.31  ? 91  ARG   A C    1 
ATOM   708  O O    . ARG   A 1 91  ? -7.849  21.227  31.988  1.00 82.01  ? 91  ARG   A O    1 
ATOM   709  C CB   . ARG   A 1 91  ? -10.457 20.097  30.212  1.00 74.16  ? 91  ARG   A CB   1 
ATOM   710  C CG   . ARG   A 1 91  ? -11.042 20.932  31.344  1.00 76.29  ? 91  ARG   A CG   1 
ATOM   711  C CD   . ARG   A 1 91  ? -12.558 20.911  31.361  1.00 77.37  ? 91  ARG   A CD   1 
ATOM   712  N NE   . ARG   A 1 91  ? -13.064 19.597  30.996  1.00 78.33  ? 91  ARG   A NE   1 
ATOM   713  C CZ   . ARG   A 1 91  ? -13.812 18.833  31.782  1.00 80.61  ? 91  ARG   A CZ   1 
ATOM   714  N NH1  . ARG   A 1 91  ? -14.171 19.224  32.994  1.00 84.59  ? 91  ARG   A NH1  1 
ATOM   715  N NH2  . ARG   A 1 91  ? -14.210 17.645  31.337  1.00 84.81  ? 91  ARG   A NH2  1 
ATOM   716  N N    . ASN   A 1 92  ? -7.988  21.961  29.883  1.00 57.34  ? 92  ASN   A N    1 
ATOM   717  C CA   . ASN   A 1 92  ? -7.305  23.214  30.176  1.00 57.64  ? 92  ASN   A CA   1 
ATOM   718  C C    . ASN   A 1 92  ? -5.815  23.055  30.433  1.00 50.99  ? 92  ASN   A C    1 
ATOM   719  O O    . ASN   A 1 92  ? -5.145  24.054  30.680  1.00 55.81  ? 92  ASN   A O    1 
ATOM   720  C CB   . ASN   A 1 92  ? -7.918  23.957  31.363  1.00 49.65  ? 92  ASN   A CB   1 
ATOM   721  C CG   . ASN   A 1 92  ? -7.576  25.416  31.337  1.00 57.84  ? 92  ASN   A CG   1 
ATOM   722  O OD1  . ASN   A 1 92  ? -7.767  26.085  30.317  1.00 58.49  ? 92  ASN   A OD1  1 
ATOM   723  N ND2  . ASN   A 1 92  ? -7.029  25.922  32.439  1.00 59.72  ? 92  ASN   A ND2  1 
ATOM   724  N N    . ARG   A 1 93  ? -5.264  21.849  30.360  1.00 42.45  ? 93  ARG   A N    1 
ATOM   725  C CA   . ARG   A 1 93  ? -3.813  21.726  30.432  1.00 42.71  ? 93  ARG   A CA   1 
ATOM   726  C C    . ARG   A 1 93  ? -3.128  22.470  29.292  1.00 43.74  ? 93  ARG   A C    1 
ATOM   727  O O    . ARG   A 1 93  ? -2.054  23.060  29.492  1.00 41.92  ? 93  ARG   A O    1 
ATOM   728  C CB   . ARG   A 1 93  ? -3.385  20.258  30.417  1.00 43.15  ? 93  ARG   A CB   1 
ATOM   729  C CG   . ARG   A 1 93  ? -1.872  20.100  30.497  1.00 39.97  ? 93  ARG   A CG   1 
ATOM   730  C CD   . ARG   A 1 93  ? -1.447  18.658  30.624  1.00 38.70  ? 93  ARG   A CD   1 
ATOM   731  N NE   . ARG   A 1 93  ? 0.009   18.583  30.600  1.00 38.51  ? 93  ARG   A NE   1 
ATOM   732  C CZ   . ARG   A 1 93  ? 0.707   17.459  30.522  1.00 40.63  ? 93  ARG   A CZ   1 
ATOM   733  N NH1  . ARG   A 1 93  ? 0.113   16.277  30.484  1.00 38.99  ? 93  ARG   A NH1  1 
ATOM   734  N NH2  . ARG   A 1 93  ? 2.037   17.520  30.506  1.00 39.57  ? 93  ARG   A NH2  1 
ATOM   735  N N    . PHE   A 1 94  ? -3.701  22.422  28.064  1.00 44.22  ? 94  PHE   A N    1 
ATOM   736  C CA   . PHE   A 1 94  ? -3.022  23.028  26.926  1.00 43.74  ? 94  PHE   A CA   1 
ATOM   737  C C    . PHE   A 1 94  ? -3.761  24.138  26.188  1.00 41.59  ? 94  PHE   A C    1 
ATOM   738  O O    . PHE   A 1 94  ? -3.100  24.862  25.435  1.00 44.67  ? 94  PHE   A O    1 
ATOM   739  C CB   . PHE   A 1 94  ? -2.645  21.947  25.906  1.00 38.72  ? 94  PHE   A CB   1 
ATOM   740  C CG   . PHE   A 1 94  ? -1.579  21.010  26.394  1.00 39.34  ? 94  PHE   A CG   1 
ATOM   741  C CD1  . PHE   A 1 94  ? -0.255  21.424  26.478  1.00 38.28  ? 94  PHE   A CD1  1 
ATOM   742  C CD2  . PHE   A 1 94  ? -1.899  19.711  26.774  1.00 38.43  ? 94  PHE   A CD2  1 
ATOM   743  C CE1  . PHE   A 1 94  ? 0.737   20.548  26.920  1.00 37.98  ? 94  PHE   A CE1  1 
ATOM   744  C CE2  . PHE   A 1 94  ? -0.922  18.836  27.201  1.00 38.69  ? 94  PHE   A CE2  1 
ATOM   745  C CZ   . PHE   A 1 94  ? 0.398   19.254  27.280  1.00 38.84  ? 94  PHE   A CZ   1 
ATOM   746  N N    . GLY   A 1 95  ? -5.062  24.342  26.408  1.00 41.02  ? 95  GLY   A N    1 
ATOM   747  C CA   . GLY   A 1 95  ? -5.755  25.469  25.803  1.00 44.69  ? 95  GLY   A CA   1 
ATOM   748  C C    . GLY   A 1 95  ? -6.432  25.199  24.462  1.00 46.83  ? 95  GLY   A C    1 
ATOM   749  O O    . GLY   A 1 95  ? -5.806  24.684  23.527  1.00 43.87  ? 95  GLY   A O    1 
ATOM   750  N N    . GLN   A 1 96  ? -7.708  25.551  24.339  1.00 46.55  ? 96  GLN   A N    1 
ATOM   751  C CA   . GLN   A 1 96  ? -8.424  25.431  23.070  1.00 50.65  ? 96  GLN   A CA   1 
ATOM   752  C C    . GLN   A 1 96  ? -8.280  24.033  22.476  1.00 49.13  ? 96  GLN   A C    1 
ATOM   753  O O    . GLN   A 1 96  ? -8.039  23.867  21.275  1.00 46.09  ? 96  GLN   A O    1 
ATOM   754  C CB   . GLN   A 1 96  ? -7.958  26.497  22.071  1.00 47.94  ? 96  GLN   A CB   1 
ATOM   755  C CG   . GLN   A 1 96  ? -8.459  27.866  22.446  1.00 52.58  ? 96  GLN   A CG   1 
ATOM   756  C CD   . GLN   A 1 96  ? -7.828  28.972  21.647  1.00 56.19  ? 96  GLN   A CD   1 
ATOM   757  O OE1  . GLN   A 1 96  ? -6.658  28.898  21.274  1.00 57.64  ? 96  GLN   A OE1  1 
ATOM   758  N NE2  . GLN   A 1 96  ? -8.573  30.048  21.450  1.00 56.62  ? 96  GLN   A NE2  1 
ATOM   759  N N    . THR   A 1 97  ? -8.464  23.007  23.329  1.00 41.64  ? 97  THR   A N    1 
ATOM   760  C CA   . THR   A 1 97  ? -8.488  21.661  22.769  1.00 42.45  ? 97  THR   A CA   1 
ATOM   761  C C    . THR   A 1 97  ? -9.832  20.953  22.949  1.00 42.03  ? 97  THR   A C    1 
ATOM   762  O O    . THR   A 1 97  ? -9.860  19.763  23.296  1.00 39.09  ? 97  THR   A O    1 
ATOM   763  C CB   . THR   A 1 97  ? -7.384  20.843  23.421  1.00 39.89  ? 97  THR   A CB   1 
ATOM   764  O OG1  . THR   A 1 97  ? -7.680  20.693  24.822  1.00 45.67  ? 97  THR   A OG1  1 
ATOM   765  C CG2  . THR   A 1 97  ? -6.083  21.598  23.290  1.00 38.34  ? 97  THR   A CG2  1 
ATOM   766  N N    . PRO   A 1 98  ? -10.957 21.600  22.604  1.00 45.90  ? 98  PRO   A N    1 
ATOM   767  C CA   . PRO   A 1 98  ? -12.262 20.951  22.829  1.00 42.36  ? 98  PRO   A CA   1 
ATOM   768  C C    . PRO   A 1 98  ? -12.458 19.650  22.059  1.00 45.40  ? 98  PRO   A C    1 
ATOM   769  O O    . PRO   A 1 98  ? -13.083 18.724  22.593  1.00 45.41  ? 98  PRO   A O    1 
ATOM   770  C CB   . PRO   A 1 98  ? -13.262 22.027  22.385  1.00 43.77  ? 98  PRO   A CB   1 
ATOM   771  C CG   . PRO   A 1 98  ? -12.514 22.853  21.414  1.00 44.93  ? 98  PRO   A CG   1 
ATOM   772  C CD   . PRO   A 1 98  ? -11.100 22.890  21.901  1.00 46.31  ? 98  PRO   A CD   1 
ATOM   773  N N    . VAL   A 1 99  ? -11.968 19.543  20.813  1.00 42.37  ? 99  VAL   A N    1 
ATOM   774  C CA   . VAL   A 1 99  ? -12.209 18.326  20.036  1.00 37.32  ? 99  VAL   A CA   1 
ATOM   775  C C    . VAL   A 1 99  ? -11.414 17.162  20.612  1.00 38.88  ? 99  VAL   A C    1 
ATOM   776  O O    . VAL   A 1 99  ? -11.933 16.046  20.776  1.00 37.64  ? 99  VAL   A O    1 
ATOM   777  C CB   . VAL   A 1 99  ? -11.892 18.560  18.548  1.00 41.91  ? 99  VAL   A CB   1 
ATOM   778  C CG1  . VAL   A 1 99  ? -11.738 17.224  17.827  1.00 34.77  ? 99  VAL   A CG1  1 
ATOM   779  C CG2  . VAL   A 1 99  ? -13.014 19.405  17.897  1.00 41.59  ? 99  VAL   A CG2  1 
ATOM   780  N N    . GLN   A 1 100 ? -10.139 17.397  20.922  1.00 41.96  ? 100 GLN   A N    1 
ATOM   781  C CA   . GLN   A 1 100 ? -9.384  16.395  21.659  1.00 43.40  ? 100 GLN   A CA   1 
ATOM   782  C C    . GLN   A 1 100 ? -10.089 16.042  22.962  1.00 42.77  ? 100 GLN   A C    1 
ATOM   783  O O    . GLN   A 1 100 ? -10.124 14.874  23.362  1.00 43.26  ? 100 GLN   A O    1 
ATOM   784  C CB   . GLN   A 1 100 ? -7.986  16.917  21.961  1.00 42.86  ? 100 GLN   A CB   1 
ATOM   785  C CG   . GLN   A 1 100 ? -7.100  17.072  20.749  1.00 43.20  ? 100 GLN   A CG   1 
ATOM   786  C CD   . GLN   A 1 100 ? -5.756  17.648  21.133  1.00 41.66  ? 100 GLN   A CD   1 
ATOM   787  O OE1  . GLN   A 1 100 ? -4.912  16.967  21.732  1.00 42.95  ? 100 GLN   A OE1  1 
ATOM   788  N NE2  . GLN   A 1 100 ? -5.553  18.925  20.807  1.00 43.69  ? 100 GLN   A NE2  1 
ATOM   789  N N    . GLU   A 1 101 ? -10.638 17.041  23.654  1.00 46.80  ? 101 GLU   A N    1 
ATOM   790  C CA   . GLU   A 1 101 ? -11.290 16.756  24.923  1.00 49.75  ? 101 GLU   A CA   1 
ATOM   791  C C    . GLU   A 1 101 ? -12.471 15.819  24.727  1.00 48.02  ? 101 GLU   A C    1 
ATOM   792  O O    . GLU   A 1 101 ? -12.629 14.832  25.458  1.00 48.79  ? 101 GLU   A O    1 
ATOM   793  C CB   . GLU   A 1 101 ? -11.741 18.053  25.587  1.00 49.50  ? 101 GLU   A CB   1 
ATOM   794  C CG   . GLU   A 1 101 ? -12.395 17.858  26.956  1.00 48.86  ? 101 GLU   A CG   1 
ATOM   795  C CD   . GLU   A 1 101 ? -13.002 19.154  27.467  1.00 54.72  ? 101 GLU   A CD   1 
ATOM   796  O OE1  . GLU   A 1 101 ? -12.401 20.222  27.193  1.00 57.01  ? 101 GLU   A OE1  1 
ATOM   797  O OE2  . GLU   A 1 101 ? -14.074 19.118  28.117  1.00 54.85  ? 101 GLU   A OE2  1 
ATOM   798  N N    . ARG   A 1 102 ? -13.304 16.106  23.732  1.00 42.35  ? 102 ARG   A N    1 
ATOM   799  C CA   . ARG   A 1 102 ? -14.490 15.286  23.520  1.00 43.85  ? 102 ARG   A CA   1 
ATOM   800  C C    . ARG   A 1 102 ? -14.111 13.888  23.031  1.00 42.42  ? 102 ARG   A C    1 
ATOM   801  O O    . ARG   A 1 102 ? -14.737 12.895  23.420  1.00 43.42  ? 102 ARG   A O    1 
ATOM   802  C CB   . ARG   A 1 102 ? -15.443 15.970  22.535  1.00 42.85  ? 102 ARG   A CB   1 
ATOM   803  C CG   . ARG   A 1 102 ? -16.700 15.145  22.257  1.00 44.59  ? 102 ARG   A CG   1 
ATOM   804  C CD   . ARG   A 1 102 ? -17.873 15.976  21.763  1.00 44.34  ? 102 ARG   A CD   1 
ATOM   805  N NE   . ARG   A 1 102 ? -19.063 15.144  21.664  1.00 43.47  ? 102 ARG   A NE   1 
ATOM   806  C CZ   . ARG   A 1 102 ? -20.087 15.387  20.860  1.00 46.12  ? 102 ARG   A CZ   1 
ATOM   807  N NH1  . ARG   A 1 102 ? -20.110 16.447  20.067  1.00 46.61  ? 102 ARG   A NH1  1 
ATOM   808  N NH2  . ARG   A 1 102 ? -21.112 14.539  20.843  1.00 48.28  ? 102 ARG   A NH2  1 
ATOM   809  N N    . LEU   A 1 103 ? -13.090 13.782  22.175  1.00 39.54  ? 103 LEU   A N    1 
ATOM   810  C CA   . LEU   A 1 103 ? -12.632 12.449  21.791  1.00 40.28  ? 103 LEU   A CA   1 
ATOM   811  C C    . LEU   A 1 103 ? -12.132 11.671  23.018  1.00 41.51  ? 103 LEU   A C    1 
ATOM   812  O O    . LEU   A 1 103 ? -12.514 10.508  23.222  1.00 40.98  ? 103 LEU   A O    1 
ATOM   813  C CB   . LEU   A 1 103 ? -11.544 12.560  20.714  1.00 37.01  ? 103 LEU   A CB   1 
ATOM   814  C CG   . LEU   A 1 103 ? -12.066 12.986  19.326  1.00 35.52  ? 103 LEU   A CG   1 
ATOM   815  C CD1  . LEU   A 1 103 ? -10.937 13.340  18.377  1.00 33.89  ? 103 LEU   A CD1  1 
ATOM   816  C CD2  . LEU   A 1 103 ? -12.961 11.909  18.745  1.00 32.65  ? 103 LEU   A CD2  1 
ATOM   817  N N    . SER   A 1 104 ? -11.322 12.314  23.868  1.00 38.77  ? 104 SER   A N    1 
ATOM   818  C CA   . SER   A 1 104 ? -10.849 11.679  25.095  1.00 41.32  ? 104 SER   A CA   1 
ATOM   819  C C    . SER   A 1 104 ? -12.012 11.178  25.934  1.00 43.48  ? 104 SER   A C    1 
ATOM   820  O O    . SER   A 1 104 ? -11.980 10.062  26.473  1.00 42.84  ? 104 SER   A O    1 
ATOM   821  C CB   . SER   A 1 104 ? -10.021 12.668  25.914  1.00 42.82  ? 104 SER   A CB   1 
ATOM   822  O OG   . SER   A 1 104 ? -9.671  12.103  27.160  1.00 42.14  ? 104 SER   A OG   1 
ATOM   823  N N    . CYS   A 1 105 ? -13.022 12.022  26.110  1.00 46.66  ? 105 CYS   A N    1 
ATOM   824  C CA   . CYS   A 1 105 ? -14.140 11.637  26.952  1.00 46.69  ? 105 CYS   A CA   1 
ATOM   825  C C    . CYS   A 1 105 ? -14.929 10.495  26.333  1.00 50.82  ? 105 CYS   A C    1 
ATOM   826  O O    . CYS   A 1 105 ? -15.386 9.594   27.049  1.00 51.09  ? 105 CYS   A O    1 
ATOM   827  C CB   . CYS   A 1 105 ? -15.005 12.860  27.224  1.00 48.07  ? 105 CYS   A CB   1 
ATOM   828  S SG   . CYS   A 1 105 ? -14.182 14.013  28.396  1.00 57.09  ? 105 CYS   A SG   1 
ATOM   829  N N    . LEU   A 1 106 ? -15.068 10.487  24.999  1.00 50.61  ? 106 LEU   A N    1 
ATOM   830  C CA   . LEU   A 1 106 ? -15.754 9.379   24.337  1.00 47.17  ? 106 LEU   A CA   1 
ATOM   831  C C    . LEU   A 1 106 ? -15.001 8.071   24.563  1.00 47.61  ? 106 LEU   A C    1 
ATOM   832  O O    . LEU   A 1 106 ? -15.606 7.019   24.813  1.00 47.68  ? 106 LEU   A O    1 
ATOM   833  C CB   . LEU   A 1 106 ? -15.897 9.662   22.831  1.00 47.59  ? 106 LEU   A CB   1 
ATOM   834  C CG   . LEU   A 1 106 ? -16.893 10.739  22.377  1.00 48.03  ? 106 LEU   A CG   1 
ATOM   835  C CD1  . LEU   A 1 106 ? -16.533 11.256  20.974  1.00 43.35  ? 106 LEU   A CD1  1 
ATOM   836  C CD2  . LEU   A 1 106 ? -18.334 10.243  22.435  1.00 45.50  ? 106 LEU   A CD2  1 
ATOM   837  N N    . ALA   A 1 107 ? -13.672 8.127   24.476  1.00 36.12  ? 107 ALA   A N    1 
ATOM   838  C CA   . ALA   A 1 107 ? -12.865 6.935   24.699  1.00 37.45  ? 107 ALA   A CA   1 
ATOM   839  C C    . ALA   A 1 107 ? -12.973 6.458   26.144  1.00 40.80  ? 107 ALA   A C    1 
ATOM   840  O O    . ALA   A 1 107 ? -13.071 5.247   26.395  1.00 40.66  ? 107 ALA   A O    1 
ATOM   841  C CB   . ALA   A 1 107 ? -11.409 7.225   24.325  1.00 33.43  ? 107 ALA   A CB   1 
ATOM   842  N N    . LYS   A 1 108 ? -13.009 7.398   27.104  1.00 49.42  ? 108 LYS   A N    1 
ATOM   843  C CA   . LYS   A 1 108 ? -12.962 7.062   28.531  1.00 47.94  ? 108 LYS   A CA   1 
ATOM   844  C C    . LYS   A 1 108 ? -14.312 6.592   29.072  1.00 46.36  ? 108 LYS   A C    1 
ATOM   845  O O    . LYS   A 1 108 ? -14.394 5.565   29.753  1.00 47.32  ? 108 LYS   A O    1 
ATOM   846  C CB   . LYS   A 1 108 ? -12.457 8.273   29.330  1.00 48.70  ? 108 LYS   A CB   1 
ATOM   847  C CG   . LYS   A 1 108 ? -12.393 8.078   30.825  1.00 45.40  ? 108 LYS   A CG   1 
ATOM   848  C CD   . LYS   A 1 108 ? -12.504 9.415   31.536  1.00 49.93  ? 108 LYS   A CD   1 
ATOM   849  C CE   . LYS   A 1 108 ? -12.751 9.280   33.064  1.00 49.14  ? 108 LYS   A CE   1 
ATOM   850  N NZ   . LYS   A 1 108 ? -12.948 10.629  33.692  1.00 49.67  ? 108 LYS   A NZ   1 
ATOM   851  N N    . ASN   A 1 109 ? -15.372 7.371   28.845  1.00 55.45  ? 109 ASN   A N    1 
ATOM   852  C CA   . ASN   A 1 109 ? -16.691 7.024   29.372  1.00 53.67  ? 109 ASN   A CA   1 
ATOM   853  C C    . ASN   A 1 109 ? -17.209 5.724   28.762  1.00 55.08  ? 109 ASN   A C    1 
ATOM   854  O O    . ASN   A 1 109 ? -18.095 5.075   29.332  1.00 59.04  ? 109 ASN   A O    1 
ATOM   855  C CB   . ASN   A 1 109 ? -17.682 8.179   29.136  1.00 53.97  ? 109 ASN   A CB   1 
ATOM   856  C CG   . ASN   A 1 109 ? -17.250 9.497   29.818  1.00 54.44  ? 109 ASN   A CG   1 
ATOM   857  O OD1  . ASN   A 1 109 ? -16.099 9.649   30.226  1.00 54.70  ? 109 ASN   A OD1  1 
ATOM   858  N ND2  . ASN   A 1 109 ? -18.178 10.460  29.915  1.00 57.60  ? 109 ASN   A ND2  1 
ATOM   859  N N    . ASN   A 1 110 ? -16.735 5.365   27.576  1.00 54.58  ? 110 ASN   A N    1 
ATOM   860  C CA   . ASN   A 1 110 ? -17.155 4.131   26.928  1.00 56.02  ? 110 ASN   A CA   1 
ATOM   861  C C    . ASN   A 1 110 ? -16.083 3.037   26.974  1.00 55.87  ? 110 ASN   A C    1 
ATOM   862  O O    . ASN   A 1 110 ? -16.271 1.980   26.365  1.00 53.93  ? 110 ASN   A O    1 
ATOM   863  C CB   . ASN   A 1 110 ? -17.572 4.419   25.478  1.00 54.22  ? 110 ASN   A CB   1 
ATOM   864  C CG   . ASN   A 1 110 ? -18.667 5.489   25.381  1.00 53.06  ? 110 ASN   A CG   1 
ATOM   865  O OD1  . ASN   A 1 110 ? -19.862 5.203   25.526  1.00 51.88  ? 110 ASN   A OD1  1 
ATOM   866  N ND2  . ASN   A 1 110 ? -18.251 6.732   25.172  1.00 50.04  ? 110 ASN   A ND2  1 
ATOM   867  N N    . SER   A 1 111 ? -14.963 3.267   27.666  1.00 50.05  ? 111 SER   A N    1 
ATOM   868  C CA   . SER   A 1 111 ? -13.913 2.253   27.855  1.00 48.92  ? 111 SER   A CA   1 
ATOM   869  C C    . SER   A 1 111 ? -13.608 1.512   26.544  1.00 50.53  ? 111 SER   A C    1 
ATOM   870  O O    . SER   A 1 111 ? -13.745 0.285   26.427  1.00 46.24  ? 111 SER   A O    1 
ATOM   871  C CB   . SER   A 1 111 ? -14.285 1.276   28.975  1.00 48.29  ? 111 SER   A CB   1 
ATOM   872  O OG   . SER   A 1 111 ? -13.274 0.292   29.163  1.00 47.84  ? 111 SER   A OG   1 
ATOM   873  N N    . ILE   A 1 112 ? -13.186 2.293   25.546  1.00 47.75  ? 112 ILE   A N    1 
ATOM   874  C CA   . ILE   A 1 112 ? -12.921 1.801   24.194  1.00 42.50  ? 112 ILE   A CA   1 
ATOM   875  C C    . ILE   A 1 112 ? -11.848 2.683   23.573  1.00 41.73  ? 112 ILE   A C    1 
ATOM   876  O O    . ILE   A 1 112 ? -11.884 3.911   23.698  1.00 43.81  ? 112 ILE   A O    1 
ATOM   877  C CB   . ILE   A 1 112 ? -14.201 1.808   23.326  1.00 46.63  ? 112 ILE   A CB   1 
ATOM   878  C CG1  . ILE   A 1 112 ? -13.966 1.172   21.946  1.00 46.83  ? 112 ILE   A CG1  1 
ATOM   879  C CG2  . ILE   A 1 112 ? -14.704 3.245   23.116  1.00 45.42  ? 112 ILE   A CG2  1 
ATOM   880  C CD1  . ILE   A 1 112 ? -15.247 0.942   21.189  1.00 42.75  ? 112 ILE   A CD1  1 
ATOM   881  N N    . TYR   A 1 113 ? -10.888 2.056   22.897  1.00 47.16  ? 113 TYR   A N    1 
ATOM   882  C CA   . TYR   A 1 113 ? -9.925  2.813   22.110  1.00 46.54  ? 113 TYR   A CA   1 
ATOM   883  C C    . TYR   A 1 113 ? -10.646 3.522   20.974  1.00 45.92  ? 113 TYR   A C    1 
ATOM   884  O O    . TYR   A 1 113 ? -11.469 2.920   20.275  1.00 48.32  ? 113 TYR   A O    1 
ATOM   885  C CB   . TYR   A 1 113 ? -8.846  1.891   21.547  1.00 44.20  ? 113 TYR   A CB   1 
ATOM   886  C CG   . TYR   A 1 113 ? -7.698  1.638   22.487  1.00 45.14  ? 113 TYR   A CG   1 
ATOM   887  C CD1  . TYR   A 1 113 ? -7.892  0.949   23.689  1.00 45.67  ? 113 TYR   A CD1  1 
ATOM   888  C CD2  . TYR   A 1 113 ? -6.415  2.066   22.174  1.00 42.22  ? 113 TYR   A CD2  1 
ATOM   889  C CE1  . TYR   A 1 113 ? -6.843  0.707   24.566  1.00 44.73  ? 113 TYR   A CE1  1 
ATOM   890  C CE2  . TYR   A 1 113 ? -5.353  1.814   23.031  1.00 43.08  ? 113 TYR   A CE2  1 
ATOM   891  C CZ   . TYR   A 1 113 ? -5.573  1.145   24.239  1.00 47.34  ? 113 TYR   A CZ   1 
ATOM   892  O OH   . TYR   A 1 113 ? -4.512  0.922   25.103  1.00 47.05  ? 113 TYR   A OH   1 
ATOM   893  N N    . VAL   A 1 114 ? -10.318 4.795   20.771  1.00 43.56  ? 114 VAL   A N    1 
ATOM   894  C CA   . VAL   A 1 114 ? -10.935 5.617   19.736  1.00 42.88  ? 114 VAL   A CA   1 
ATOM   895  C C    . VAL   A 1 114 ? -9.824  6.111   18.812  1.00 44.71  ? 114 VAL   A C    1 
ATOM   896  O O    . VAL   A 1 114 ? -8.837  6.696   19.285  1.00 43.50  ? 114 VAL   A O    1 
ATOM   897  C CB   . VAL   A 1 114 ? -11.728 6.786   20.348  1.00 45.74  ? 114 VAL   A CB   1 
ATOM   898  C CG1  . VAL   A 1 114 ? -12.235 7.736   19.272  1.00 44.29  ? 114 VAL   A CG1  1 
ATOM   899  C CG2  . VAL   A 1 114 ? -12.912 6.256   21.146  1.00 42.54  ? 114 VAL   A CG2  1 
ATOM   900  N N    . VAL   A 1 115 ? -9.966  5.839   17.505  1.00 37.22  ? 115 VAL   A N    1 
ATOM   901  C CA   . VAL   A 1 115 ? -9.087  6.365   16.459  1.00 36.07  ? 115 VAL   A CA   1 
ATOM   902  C C    . VAL   A 1 115 ? -9.898  7.360   15.638  1.00 35.96  ? 115 VAL   A C    1 
ATOM   903  O O    . VAL   A 1 115 ? -10.926 6.998   15.051  1.00 37.01  ? 115 VAL   A O    1 
ATOM   904  C CB   . VAL   A 1 115 ? -8.526  5.265   15.532  1.00 35.80  ? 115 VAL   A CB   1 
ATOM   905  C CG1  . VAL   A 1 115 ? -7.578  5.884   14.486  1.00 33.04  ? 115 VAL   A CG1  1 
ATOM   906  C CG2  . VAL   A 1 115 ? -7.805  4.153   16.301  1.00 31.89  ? 115 VAL   A CG2  1 
ATOM   907  N N    . ALA   A 1 116 ? -9.438  8.606   15.577  1.00 41.52  ? 116 ALA   A N    1 
ATOM   908  C CA   . ALA   A 1 116 ? -10.169 9.631   14.844  1.00 40.45  ? 116 ALA   A CA   1 
ATOM   909  C C    . ALA   A 1 116 ? -9.178  10.438  14.030  1.00 42.51  ? 116 ALA   A C    1 
ATOM   910  O O    . ALA   A 1 116 ? -7.968  10.374  14.256  1.00 40.40  ? 116 ALA   A O    1 
ATOM   911  C CB   . ALA   A 1 116 ? -10.977 10.554  15.766  1.00 39.89  ? 116 ALA   A CB   1 
ATOM   912  N N    . ASN   A 1 117 ? -9.701  11.145  13.028  1.00 39.54  ? 117 ASN   A N    1 
ATOM   913  C CA   . ASN   A 1 117 ? -8.890  11.995  12.174  1.00 40.24  ? 117 ASN   A CA   1 
ATOM   914  C C    . ASN   A 1 117 ? -9.328  13.447  12.336  1.00 39.56  ? 117 ASN   A C    1 
ATOM   915  O O    . ASN   A 1 117 ? -10.523 13.763  12.252  1.00 39.84  ? 117 ASN   A O    1 
ATOM   916  C CB   . ASN   A 1 117 ? -8.981  11.556  10.710  1.00 40.61  ? 117 ASN   A CB   1 
ATOM   917  C CG   . ASN   A 1 117 ? -8.149  12.412  9.824   1.00 41.31  ? 117 ASN   A CG   1 
ATOM   918  O OD1  . ASN   A 1 117 ? -8.622  13.436  9.326   1.00 43.73  ? 117 ASN   A OD1  1 
ATOM   919  N ND2  . ASN   A 1 117 ? -6.876  12.043  9.659   1.00 41.01  ? 117 ASN   A ND2  1 
ATOM   920  N N    . ILE   A 1 118 ? -8.363  14.319  12.595  1.00 39.72  ? 118 ILE   A N    1 
ATOM   921  C CA   . ILE   A 1 118 ? -8.619  15.728  12.878  1.00 43.44  ? 118 ILE   A CA   1 
ATOM   922  C C    . ILE   A 1 118 ? -7.454  16.534  12.309  1.00 44.57  ? 118 ILE   A C    1 
ATOM   923  O O    . ILE   A 1 118 ? -6.597  15.988  11.595  1.00 43.60  ? 118 ILE   A O    1 
ATOM   924  C CB   . ILE   A 1 118 ? -8.824  15.979  14.390  1.00 41.06  ? 118 ILE   A CB   1 
ATOM   925  C CG1  . ILE   A 1 118 ? -7.572  15.626  15.194  1.00 39.66  ? 118 ILE   A CG1  1 
ATOM   926  C CG2  . ILE   A 1 118 ? -10.035 15.190  14.923  1.00 37.51  ? 118 ILE   A CG2  1 
ATOM   927  C CD1  . ILE   A 1 118 ? -7.702  16.011  16.746  1.00 39.20  ? 118 ILE   A CD1  1 
ATOM   928  N N    . GLY   A 1 119 ? -7.441  17.840  12.565  1.00 41.42  ? 119 GLY   A N    1 
ATOM   929  C CA   . GLY   A 1 119 ? -6.439  18.732  12.014  1.00 43.17  ? 119 GLY   A CA   1 
ATOM   930  C C    . GLY   A 1 119 ? -5.499  19.249  13.089  1.00 41.89  ? 119 GLY   A C    1 
ATOM   931  O O    . GLY   A 1 119 ? -5.945  19.781  14.109  1.00 44.16  ? 119 GLY   A O    1 
ATOM   932  N N    . ASP   A 1 120 ? -4.198  19.086  12.842  1.00 44.04  ? 120 ASP   A N    1 
ATOM   933  C CA   . ASP   A 1 120 ? -3.154  19.601  13.720  1.00 43.19  ? 120 ASP   A CA   1 
ATOM   934  C C    . ASP   A 1 120 ? -2.598  20.910  13.169  1.00 48.43  ? 120 ASP   A C    1 
ATOM   935  O O    . ASP   A 1 120 ? -2.384  21.052  11.957  1.00 51.34  ? 120 ASP   A O    1 
ATOM   936  C CB   . ASP   A 1 120 ? -2.017  18.593  13.854  1.00 42.88  ? 120 ASP   A CB   1 
ATOM   937  C CG   . ASP   A 1 120 ? -1.070  18.910  15.000  1.00 45.03  ? 120 ASP   A CG   1 
ATOM   938  O OD1  . ASP   A 1 120 ? -1.471  19.587  15.986  1.00 45.36  ? 120 ASP   A OD1  1 
ATOM   939  O OD2  . ASP   A 1 120 ? 0.085   18.449  14.925  1.00 43.81  ? 120 ASP   A OD2  1 
ATOM   940  N N    . LYS   A 1 121 ? -2.357  21.864  14.056  1.00 47.20  ? 121 LYS   A N    1 
ATOM   941  C CA   . LYS   A 1 121 ? -1.646  23.083  13.702  1.00 46.69  ? 121 LYS   A CA   1 
ATOM   942  C C    . LYS   A 1 121 ? -0.418  23.204  14.591  1.00 46.75  ? 121 LYS   A C    1 
ATOM   943  O O    . LYS   A 1 121 ? -0.477  22.919  15.793  1.00 46.13  ? 121 LYS   A O    1 
ATOM   944  C CB   . LYS   A 1 121 ? -2.543  24.308  13.841  1.00 48.57  ? 121 LYS   A CB   1 
ATOM   945  C CG   . LYS   A 1 121 ? -2.839  24.732  15.267  1.00 48.97  ? 121 LYS   A CG   1 
ATOM   946  C CD   . LYS   A 1 121 ? -3.704  25.978  15.212  1.00 51.39  ? 121 LYS   A CD   1 
ATOM   947  C CE   . LYS   A 1 121 ? -3.983  26.590  16.566  1.00 53.55  ? 121 LYS   A CE   1 
ATOM   948  N NZ   . LYS   A 1 121 ? -5.034  27.628  16.370  1.00 51.85  ? 121 LYS   A NZ   1 
ATOM   949  N N    . LYS   A 1 122 ? 0.706   23.573  13.983  1.00 47.02  ? 122 LYS   A N    1 
ATOM   950  C CA   . LYS   A 1 122 ? 1.990   23.653  14.682  1.00 49.68  ? 122 LYS   A CA   1 
ATOM   951  C C    . LYS   A 1 122 ? 2.630   24.985  14.314  1.00 52.63  ? 122 LYS   A C    1 
ATOM   952  O O    . LYS   A 1 122 ? 3.173   25.132  13.201  1.00 52.73  ? 122 LYS   A O    1 
ATOM   953  C CB   . LYS   A 1 122 ? 2.920   22.486  14.329  1.00 48.96  ? 122 LYS   A CB   1 
ATOM   954  C CG   . LYS   A 1 122 ? 2.567   21.146  14.957  1.00 43.80  ? 122 LYS   A CG   1 
ATOM   955  C CD   . LYS   A 1 122 ? 2.765   21.219  16.493  1.00 46.02  ? 122 LYS   A CD   1 
ATOM   956  C CE   . LYS   A 1 122 ? 2.231   19.981  17.188  1.00 42.74  ? 122 LYS   A CE   1 
ATOM   957  N NZ   . LYS   A 1 122 ? 0.773   20.133  17.498  1.00 42.55  ? 122 LYS   A NZ   1 
ATOM   958  N N    . PRO   A 1 123 ? 2.553   25.988  15.189  1.00 59.50  ? 123 PRO   A N    1 
ATOM   959  C CA   . PRO   A 1 123 ? 3.178   27.278  14.873  1.00 59.48  ? 123 PRO   A CA   1 
ATOM   960  C C    . PRO   A 1 123 ? 4.681   27.144  14.691  1.00 62.24  ? 123 PRO   A C    1 
ATOM   961  O O    . PRO   A 1 123 ? 5.343   26.348  15.360  1.00 60.06  ? 123 PRO   A O    1 
ATOM   962  C CB   . PRO   A 1 123 ? 2.833   28.149  16.079  1.00 55.62  ? 123 PRO   A CB   1 
ATOM   963  C CG   . PRO   A 1 123 ? 1.558   27.545  16.603  1.00 60.81  ? 123 PRO   A CG   1 
ATOM   964  C CD   . PRO   A 1 123 ? 1.675   26.063  16.369  1.00 56.88  ? 123 PRO   A CD   1 
ATOM   965  N N    . CYS   A 1 124 ? 5.220   27.946  13.770  1.00 70.71  ? 124 CYS   A N    1 
ATOM   966  C CA   . CYS   A 1 124 ? 6.658   27.989  13.553  1.00 72.63  ? 124 CYS   A CA   1 
ATOM   967  C C    . CYS   A 1 124 ? 7.097   29.426  13.309  1.00 77.07  ? 124 CYS   A C    1 
ATOM   968  O O    . CYS   A 1 124 ? 6.319   30.283  12.879  1.00 75.37  ? 124 CYS   A O    1 
ATOM   969  C CB   . CYS   A 1 124 ? 7.104   27.086  12.390  1.00 73.08  ? 124 CYS   A CB   1 
ATOM   970  S SG   . CYS   A 1 124 ? 6.161   27.204  10.853  1.00 75.68  ? 124 CYS   A SG   1 
ATOM   971  N N    . ASP   A 1 125 ? 8.368   29.668  13.608  1.00 95.89  ? 125 ASP   A N    1 
ATOM   972  C CA   . ASP   A 1 125 ? 9.012   30.964  13.491  1.00 98.99  ? 125 ASP   A CA   1 
ATOM   973  C C    . ASP   A 1 125 ? 9.899   30.982  12.255  1.00 101.44 ? 125 ASP   A C    1 
ATOM   974  O O    . ASP   A 1 125 ? 10.211  29.944  11.666  1.00 98.56  ? 125 ASP   A O    1 
ATOM   975  C CB   . ASP   A 1 125 ? 9.846   31.256  14.750  1.00 101.76 ? 125 ASP   A CB   1 
ATOM   976  C CG   . ASP   A 1 125 ? 9.262   32.368  15.606  1.00 105.89 ? 125 ASP   A CG   1 
ATOM   977  O OD1  . ASP   A 1 125 ? 8.281   33.000  15.168  1.00 104.13 ? 125 ASP   A OD1  1 
ATOM   978  O OD2  . ASP   A 1 125 ? 9.785   32.615  16.716  1.00 111.42 ? 125 ASP   A OD2  1 
ATOM   979  N N    . THR   A 1 126 ? 10.319  32.187  11.865  1.00 121.88 ? 126 THR   A N    1 
ATOM   980  C CA   . THR   A 1 126 ? 11.317  32.279  10.809  1.00 124.15 ? 126 THR   A CA   1 
ATOM   981  C C    . THR   A 1 126 ? 12.611  31.595  11.221  1.00 125.35 ? 126 THR   A C    1 
ATOM   982  O O    . THR   A 1 126 ? 13.420  31.240  10.358  1.00 126.50 ? 126 THR   A O    1 
ATOM   983  C CB   . THR   A 1 126 ? 11.574  33.740  10.439  1.00 127.26 ? 126 THR   A CB   1 
ATOM   984  O OG1  . THR   A 1 126 ? 10.806  34.597  11.297  1.00 125.14 ? 126 THR   A OG1  1 
ATOM   985  C CG2  . THR   A 1 126 ? 11.189  33.988  8.984   1.00 120.55 ? 126 THR   A CG2  1 
ATOM   986  N N    . SER   A 1 127 ? 12.813  31.397  12.528  1.00 111.74 ? 127 SER   A N    1 
ATOM   987  C CA   . SER   A 1 127 ? 13.896  30.545  13.005  1.00 112.08 ? 127 SER   A CA   1 
ATOM   988  C C    . SER   A 1 127 ? 13.927  29.210  12.269  1.00 108.45 ? 127 SER   A C    1 
ATOM   989  O O    . SER   A 1 127 ? 15.005  28.650  12.038  1.00 106.50 ? 127 SER   A O    1 
ATOM   990  C CB   . SER   A 1 127 ? 13.749  30.322  14.516  1.00 111.61 ? 127 SER   A CB   1 
ATOM   991  O OG   . SER   A 1 127 ? 12.520  29.686  14.846  1.00 107.54 ? 127 SER   A OG   1 
ATOM   992  N N    . ASP   A 1 128 ? 12.760  28.686  11.895  1.00 99.03  ? 128 ASP   A N    1 
ATOM   993  C CA   . ASP   A 1 128 ? 12.670  27.397  11.216  1.00 95.90  ? 128 ASP   A CA   1 
ATOM   994  C C    . ASP   A 1 128 ? 12.856  27.582  9.713   1.00 98.61  ? 128 ASP   A C    1 
ATOM   995  O O    . ASP   A 1 128 ? 12.077  28.317  9.088   1.00 96.77  ? 128 ASP   A O    1 
ATOM   996  C CB   . ASP   A 1 128 ? 11.331  26.738  11.512  1.00 92.39  ? 128 ASP   A CB   1 
ATOM   997  C CG   . ASP   A 1 128 ? 11.157  25.408  10.795  1.00 91.71  ? 128 ASP   A CG   1 
ATOM   998  O OD1  . ASP   A 1 128 ? 12.128  24.932  10.165  1.00 91.21  ? 128 ASP   A OD1  1 
ATOM   999  O OD2  . ASP   A 1 128 ? 10.050  24.829  10.883  1.00 85.56  ? 128 ASP   A OD2  1 
ATOM   1000 N N    . PRO   A 1 129 ? 13.860  26.951  9.097   1.00 117.41 ? 129 PRO   A N    1 
ATOM   1001 C CA   . PRO   A 1 129 ? 14.100  27.175  7.662   1.00 117.45 ? 129 PRO   A CA   1 
ATOM   1002 C C    . PRO   A 1 129 ? 12.984  26.687  6.761   1.00 115.72 ? 129 PRO   A C    1 
ATOM   1003 O O    . PRO   A 1 129 ? 12.912  27.133  5.609   1.00 118.26 ? 129 PRO   A O    1 
ATOM   1004 C CB   . PRO   A 1 129 ? 15.397  26.401  7.392   1.00 115.68 ? 129 PRO   A CB   1 
ATOM   1005 C CG   . PRO   A 1 129 ? 15.478  25.402  8.493   1.00 119.07 ? 129 PRO   A CG   1 
ATOM   1006 C CD   . PRO   A 1 129 ? 14.865  26.060  9.694   1.00 118.35 ? 129 PRO   A CD   1 
ATOM   1007 N N    . GLN   A 1 130 ? 12.124  25.779  7.222   1.00 94.60  ? 130 GLN   A N    1 
ATOM   1008 C CA   . GLN   A 1 130 ? 11.013  25.307  6.403   1.00 96.06  ? 130 GLN   A CA   1 
ATOM   1009 C C    . GLN   A 1 130 ? 9.651   25.714  6.948   1.00 92.64  ? 130 GLN   A C    1 
ATOM   1010 O O    . GLN   A 1 130 ? 8.641   25.077  6.631   1.00 88.61  ? 130 GLN   A O    1 
ATOM   1011 C CB   . GLN   A 1 130 ? 11.063  23.794  6.225   1.00 96.15  ? 130 GLN   A CB   1 
ATOM   1012 C CG   . GLN   A 1 130 ? 12.303  23.279  5.533   1.00 97.47  ? 130 GLN   A CG   1 
ATOM   1013 C CD   . GLN   A 1 130 ? 12.258  21.776  5.386   1.00 102.06 ? 130 GLN   A CD   1 
ATOM   1014 O OE1  . GLN   A 1 130 ? 11.498  21.098  6.088   1.00 100.79 ? 130 GLN   A OE1  1 
ATOM   1015 N NE2  . GLN   A 1 130 ? 13.049  21.243  4.456   1.00 101.42 ? 130 GLN   A NE2  1 
ATOM   1016 N N    . CYS   A 1 131 ? 9.594   26.753  7.754   1.00 81.73  ? 131 CYS   A N    1 
ATOM   1017 C CA   . CYS   A 1 131 ? 8.303   27.247  8.185   1.00 77.80  ? 131 CYS   A CA   1 
ATOM   1018 C C    . CYS   A 1 131 ? 7.528   27.780  6.982   1.00 75.10  ? 131 CYS   A C    1 
ATOM   1019 O O    . CYS   A 1 131 ? 8.055   28.609  6.234   1.00 71.24  ? 131 CYS   A O    1 
ATOM   1020 C CB   . CYS   A 1 131 ? 8.475   28.340  9.231   1.00 76.03  ? 131 CYS   A CB   1 
ATOM   1021 S SG   . CYS   A 1 131 ? 6.901   28.847  9.901   1.00 77.72  ? 131 CYS   A SG   1 
ATOM   1022 N N    . PRO   A 1 132 ? 6.284   27.349  6.773   1.00 67.20  ? 132 PRO   A N    1 
ATOM   1023 C CA   . PRO   A 1 132 ? 5.519   27.866  5.640   1.00 61.76  ? 132 PRO   A CA   1 
ATOM   1024 C C    . PRO   A 1 132 ? 5.344   29.364  5.748   1.00 63.02  ? 132 PRO   A C    1 
ATOM   1025 O O    . PRO   A 1 132 ? 5.373   29.940  6.854   1.00 64.90  ? 132 PRO   A O    1 
ATOM   1026 C CB   . PRO   A 1 132 ? 4.174   27.130  5.756   1.00 58.11  ? 132 PRO   A CB   1 
ATOM   1027 C CG   . PRO   A 1 132 ? 4.483   25.888  6.533   1.00 59.05  ? 132 PRO   A CG   1 
ATOM   1028 C CD   . PRO   A 1 132 ? 5.566   26.289  7.504   1.00 62.74  ? 132 PRO   A CD   1 
ATOM   1029 N N    . PRO   A 1 133 ? 5.188   30.052  4.613   1.00 75.67  ? 133 PRO   A N    1 
ATOM   1030 C CA   . PRO   A 1 133 ? 5.100   31.521  4.643   1.00 73.73  ? 133 PRO   A CA   1 
ATOM   1031 C C    . PRO   A 1 133 ? 3.997   32.060  5.541   1.00 75.39  ? 133 PRO   A C    1 
ATOM   1032 O O    . PRO   A 1 133 ? 4.067   33.231  5.934   1.00 78.22  ? 133 PRO   A O    1 
ATOM   1033 C CB   . PRO   A 1 133 ? 4.840   31.898  3.178   1.00 72.16  ? 133 PRO   A CB   1 
ATOM   1034 C CG   . PRO   A 1 133 ? 4.896   30.630  2.397   1.00 75.88  ? 133 PRO   A CG   1 
ATOM   1035 C CD   . PRO   A 1 133 ? 5.393   29.524  3.257   1.00 71.30  ? 133 PRO   A CD   1 
ATOM   1036 N N    . ASP   A 1 134 ? 2.931   31.297  5.791   1.00 61.29  ? 134 ASP   A N    1 
ATOM   1037 C CA   . ASP   A 1 134 ? 1.836   31.792  6.610   1.00 65.71  ? 134 ASP   A CA   1 
ATOM   1038 C C    . ASP   A 1 134 ? 1.974   31.398  8.089   1.00 64.49  ? 134 ASP   A C    1 
ATOM   1039 O O    . ASP   A 1 134 ? 1.007   31.526  8.849   1.00 64.39  ? 134 ASP   A O    1 
ATOM   1040 C CB   . ASP   A 1 134 ? 0.484   31.340  6.028   1.00 58.45  ? 134 ASP   A CB   1 
ATOM   1041 C CG   . ASP   A 1 134 ? 0.327   29.833  5.984   1.00 61.00  ? 134 ASP   A CG   1 
ATOM   1042 O OD1  . ASP   A 1 134 ? 1.221   29.117  6.483   1.00 61.69  ? 134 ASP   A OD1  1 
ATOM   1043 O OD2  . ASP   A 1 134 ? -0.715  29.363  5.475   1.00 63.14  ? 134 ASP   A OD2  1 
ATOM   1044 N N    . GLY   A 1 135 ? 3.149   30.923  8.506   1.00 58.89  ? 135 GLY   A N    1 
ATOM   1045 C CA   . GLY   A 1 135 ? 3.520   30.905  9.905   1.00 58.26  ? 135 GLY   A CA   1 
ATOM   1046 C C    . GLY   A 1 135 ? 3.186   29.657  10.684  1.00 60.76  ? 135 GLY   A C    1 
ATOM   1047 O O    . GLY   A 1 135 ? 3.348   29.652  11.914  1.00 65.53  ? 135 GLY   A O    1 
ATOM   1048 N N    . ARG   A 1 136 ? 2.726   28.599  10.031  1.00 61.69  ? 136 ARG   A N    1 
ATOM   1049 C CA   . ARG   A 1 136 ? 2.415   27.391  10.776  1.00 61.33  ? 136 ARG   A CA   1 
ATOM   1050 C C    . ARG   A 1 136 ? 2.356   26.210  9.814   1.00 58.09  ? 136 ARG   A C    1 
ATOM   1051 O O    . ARG   A 1 136 ? 2.115   26.380  8.616   1.00 59.36  ? 136 ARG   A O    1 
ATOM   1052 C CB   . ARG   A 1 136 ? 1.099   27.546  11.546  1.00 54.59  ? 136 ARG   A CB   1 
ATOM   1053 C CG   . ARG   A 1 136 ? -0.141  27.352  10.709  1.00 53.64  ? 136 ARG   A CG   1 
ATOM   1054 C CD   . ARG   A 1 136 ? -0.451  28.595  9.915   1.00 54.47  ? 136 ARG   A CD   1 
ATOM   1055 N NE   . ARG   A 1 136 ? -1.717  28.456  9.205   1.00 56.54  ? 136 ARG   A NE   1 
ATOM   1056 C CZ   . ARG   A 1 136 ? -2.333  29.444  8.573   1.00 56.89  ? 136 ARG   A CZ   1 
ATOM   1057 N NH1  . ARG   A 1 136 ? -1.808  30.657  8.507   1.00 55.67  ? 136 ARG   A NH1  1 
ATOM   1058 N NH2  . ARG   A 1 136 ? -3.518  29.214  8.018   1.00 56.92  ? 136 ARG   A NH2  1 
ATOM   1059 N N    . TYR   A 1 137 ? 2.620   25.022  10.346  1.00 52.40  ? 137 TYR   A N    1 
ATOM   1060 C CA   . TYR   A 1 137 ? 2.313   23.785  9.652   1.00 51.34  ? 137 TYR   A CA   1 
ATOM   1061 C C    . TYR   A 1 137 ? 0.877   23.385  9.956   1.00 53.78  ? 137 TYR   A C    1 
ATOM   1062 O O    . TYR   A 1 137 ? 0.383   23.594  11.073  1.00 49.15  ? 137 TYR   A O    1 
ATOM   1063 C CB   . TYR   A 1 137 ? 3.255   22.657  10.086  1.00 52.11  ? 137 TYR   A CB   1 
ATOM   1064 C CG   . TYR   A 1 137 ? 4.713   22.890  9.780   1.00 54.15  ? 137 TYR   A CG   1 
ATOM   1065 C CD1  . TYR   A 1 137 ? 5.201   22.730  8.486   1.00 59.34  ? 137 TYR   A CD1  1 
ATOM   1066 C CD2  . TYR   A 1 137 ? 5.604   23.268  10.772  1.00 55.17  ? 137 TYR   A CD2  1 
ATOM   1067 C CE1  . TYR   A 1 137 ? 6.532   22.943  8.196   1.00 58.28  ? 137 TYR   A CE1  1 
ATOM   1068 C CE2  . TYR   A 1 137 ? 6.942   23.478  10.495  1.00 57.54  ? 137 TYR   A CE2  1 
ATOM   1069 C CZ   . TYR   A 1 137 ? 7.400   23.310  9.203   1.00 62.76  ? 137 TYR   A CZ   1 
ATOM   1070 O OH   . TYR   A 1 137 ? 8.728   23.520  8.906   1.00 69.78  ? 137 TYR   A OH   1 
ATOM   1071 N N    . GLN   A 1 138 ? 0.206   22.804  8.963   1.00 50.44  ? 138 GLN   A N    1 
ATOM   1072 C CA   . GLN   A 1 138 ? -1.101  22.204  9.194   1.00 50.30  ? 138 GLN   A CA   1 
ATOM   1073 C C    . GLN   A 1 138 ? -1.046  20.761  8.712   1.00 52.25  ? 138 GLN   A C    1 
ATOM   1074 O O    . GLN   A 1 138 ? -0.696  20.505  7.555   1.00 48.84  ? 138 GLN   A O    1 
ATOM   1075 C CB   . GLN   A 1 138 ? -2.209  22.987  8.483   1.00 49.12  ? 138 GLN   A CB   1 
ATOM   1076 C CG   . GLN   A 1 138 ? -1.969  24.487  8.452   1.00 49.16  ? 138 GLN   A CG   1 
ATOM   1077 C CD   . GLN   A 1 138 ? -3.180  25.277  7.981   1.00 53.43  ? 138 GLN   A CD   1 
ATOM   1078 O OE1  . GLN   A 1 138 ? -3.407  26.411  8.410   1.00 56.28  ? 138 GLN   A OE1  1 
ATOM   1079 N NE2  . GLN   A 1 138 ? -3.949  24.692  7.061   1.00 53.98  ? 138 GLN   A NE2  1 
ATOM   1080 N N    . TYR   A 1 139 ? -1.420  19.817  9.584   1.00 47.82  ? 139 TYR   A N    1 
ATOM   1081 C CA   . TYR   A 1 139 ? -1.274  18.399  9.286   1.00 46.52  ? 139 TYR   A CA   1 
ATOM   1082 C C    . TYR   A 1 139 ? -2.612  17.678  9.371   1.00 46.81  ? 139 TYR   A C    1 
ATOM   1083 O O    . TYR   A 1 139 ? -3.470  18.023  10.189  1.00 42.45  ? 139 TYR   A O    1 
ATOM   1084 C CB   . TYR   A 1 139 ? -0.297  17.723  10.229  1.00 47.10  ? 139 TYR   A CB   1 
ATOM   1085 C CG   . TYR   A 1 139 ? 1.124   18.232  10.150  1.00 49.64  ? 139 TYR   A CG   1 
ATOM   1086 C CD1  . TYR   A 1 139 ? 1.882   18.062  9.001   1.00 48.25  ? 139 TYR   A CD1  1 
ATOM   1087 C CD2  . TYR   A 1 139 ? 1.719   18.856  11.252  1.00 48.70  ? 139 TYR   A CD2  1 
ATOM   1088 C CE1  . TYR   A 1 139 ? 3.192   18.509  8.940   1.00 50.23  ? 139 TYR   A CE1  1 
ATOM   1089 C CE2  . TYR   A 1 139 ? 3.019   19.308  11.199  1.00 49.68  ? 139 TYR   A CE2  1 
ATOM   1090 C CZ   . TYR   A 1 139 ? 3.750   19.133  10.043  1.00 51.42  ? 139 TYR   A CZ   1 
ATOM   1091 O OH   . TYR   A 1 139 ? 5.046   19.583  9.991   1.00 52.28  ? 139 TYR   A OH   1 
ATOM   1092 N N    . ASN   A 1 140 ? -2.783  16.714  8.455   1.00 53.48  ? 140 ASN   A N    1 
ATOM   1093 C CA   . ASN   A 1 140 ? -3.859  15.723  8.470   1.00 50.39  ? 140 ASN   A CA   1 
ATOM   1094 C C    . ASN   A 1 140 ? -3.472  14.651  9.492   1.00 47.30  ? 140 ASN   A C    1 
ATOM   1095 O O    . ASN   A 1 140 ? -2.492  13.918  9.299   1.00 46.14  ? 140 ASN   A O    1 
ATOM   1096 C CB   . ASN   A 1 140 ? -4.025  15.169  7.050   1.00 46.21  ? 140 ASN   A CB   1 
ATOM   1097 C CG   . ASN   A 1 140 ? -5.035  14.025  6.944   1.00 47.44  ? 140 ASN   A CG   1 
ATOM   1098 O OD1  . ASN   A 1 140 ? -4.930  13.015  7.619   1.00 51.66  ? 140 ASN   A OD1  1 
ATOM   1099 N ND2  . ASN   A 1 140 ? -6.017  14.191  6.070   1.00 50.73  ? 140 ASN   A ND2  1 
ATOM   1100 N N    . THR   A 1 141 ? -4.210  14.564  10.599  1.00 42.61  ? 141 THR   A N    1 
ATOM   1101 C CA   . THR   A 1 141 ? -3.678  13.944  11.809  1.00 38.30  ? 141 THR   A CA   1 
ATOM   1102 C C    . THR   A 1 141 ? -4.625  12.881  12.323  1.00 37.86  ? 141 THR   A C    1 
ATOM   1103 O O    . THR   A 1 141 ? -5.788  13.174  12.609  1.00 39.06  ? 141 THR   A O    1 
ATOM   1104 C CB   . THR   A 1 141 ? -3.453  14.994  12.895  1.00 40.79  ? 141 THR   A CB   1 
ATOM   1105 O OG1  . THR   A 1 141 ? -2.710  16.090  12.349  1.00 38.80  ? 141 THR   A OG1  1 
ATOM   1106 C CG2  . THR   A 1 141 ? -2.678  14.382  14.072  1.00 39.17  ? 141 THR   A CG2  1 
ATOM   1107 N N    . ASP   A 1 142 ? -4.132  11.659  12.456  1.00 39.45  ? 142 ASP   A N    1 
ATOM   1108 C CA   . ASP   A 1 142 ? -4.825  10.653  13.254  1.00 44.35  ? 142 ASP   A CA   1 
ATOM   1109 C C    . ASP   A 1 142 ? -4.465  10.796  14.736  1.00 43.00  ? 142 ASP   A C    1 
ATOM   1110 O O    . ASP   A 1 142 ? -3.291  10.947  15.083  1.00 43.42  ? 142 ASP   A O    1 
ATOM   1111 C CB   . ASP   A 1 142 ? -4.452  9.257   12.766  1.00 41.87  ? 142 ASP   A CB   1 
ATOM   1112 C CG   . ASP   A 1 142 ? -4.806  9.036   11.303  1.00 43.94  ? 142 ASP   A CG   1 
ATOM   1113 O OD1  . ASP   A 1 142 ? -5.813  9.633   10.824  1.00 40.96  ? 142 ASP   A OD1  1 
ATOM   1114 O OD2  . ASP   A 1 142 ? -4.047  8.282   10.635  1.00 44.68  ? 142 ASP   A OD2  1 
ATOM   1115 N N    . VAL   A 1 143 ? -5.471  10.730  15.612  1.00 46.73  ? 143 VAL   A N    1 
ATOM   1116 C CA   . VAL   A 1 143 ? -5.241  10.674  17.059  1.00 49.83  ? 143 VAL   A CA   1 
ATOM   1117 C C    . VAL   A 1 143 ? -5.906  9.421   17.610  1.00 48.19  ? 143 VAL   A C    1 
ATOM   1118 O O    . VAL   A 1 143 ? -7.009  9.041   17.186  1.00 49.69  ? 143 VAL   A O    1 
ATOM   1119 C CB   . VAL   A 1 143 ? -5.732  11.921  17.835  1.00 45.87  ? 143 VAL   A CB   1 
ATOM   1120 C CG1  . VAL   A 1 143 ? -4.970  13.171  17.413  1.00 46.43  ? 143 VAL   A CG1  1 
ATOM   1121 C CG2  . VAL   A 1 143 ? -7.249  12.105  17.732  1.00 44.75  ? 143 VAL   A CG2  1 
ATOM   1122 N N    . VAL   A 1 144 ? -5.220  8.776   18.549  1.00 41.00  ? 144 VAL   A N    1 
ATOM   1123 C CA   . VAL   A 1 144 ? -5.730  7.596   19.237  1.00 43.78  ? 144 VAL   A CA   1 
ATOM   1124 C C    . VAL   A 1 144 ? -5.813  7.907   20.724  1.00 43.32  ? 144 VAL   A C    1 
ATOM   1125 O O    . VAL   A 1 144 ? -4.862  8.439   21.309  1.00 44.39  ? 144 VAL   A O    1 
ATOM   1126 C CB   . VAL   A 1 144 ? -4.845  6.359   19.003  1.00 42.04  ? 144 VAL   A CB   1 
ATOM   1127 C CG1  . VAL   A 1 144 ? -5.540  5.093   19.540  1.00 39.42  ? 144 VAL   A CG1  1 
ATOM   1128 C CG2  . VAL   A 1 144 ? -4.502  6.242   17.540  1.00 40.86  ? 144 VAL   A CG2  1 
ATOM   1129 N N    . PHE   A 1 145 ? -6.959  7.611   21.320  1.00 43.96  ? 145 PHE   A N    1 
ATOM   1130 C CA   . PHE   A 1 145 ? -7.142  7.690   22.759  1.00 44.78  ? 145 PHE   A CA   1 
ATOM   1131 C C    . PHE   A 1 145 ? -7.433  6.291   23.277  1.00 44.38  ? 145 PHE   A C    1 
ATOM   1132 O O    . PHE   A 1 145 ? -8.241  5.568   22.690  1.00 44.97  ? 145 PHE   A O    1 
ATOM   1133 C CB   . PHE   A 1 145 ? -8.269  8.661   23.108  1.00 45.78  ? 145 PHE   A CB   1 
ATOM   1134 C CG   . PHE   A 1 145 ? -8.042  10.065  22.583  1.00 45.98  ? 145 PHE   A CG   1 
ATOM   1135 C CD1  . PHE   A 1 145 ? -7.335  11.000  23.337  1.00 44.91  ? 145 PHE   A CD1  1 
ATOM   1136 C CD2  . PHE   A 1 145 ? -8.516  10.439  21.325  1.00 43.54  ? 145 PHE   A CD2  1 
ATOM   1137 C CE1  . PHE   A 1 145 ? -7.118  12.291  22.856  1.00 45.93  ? 145 PHE   A CE1  1 
ATOM   1138 C CE2  . PHE   A 1 145 ? -8.300  11.732  20.826  1.00 41.81  ? 145 PHE   A CE2  1 
ATOM   1139 C CZ   . PHE   A 1 145 ? -7.597  12.655  21.574  1.00 44.52  ? 145 PHE   A CZ   1 
ATOM   1140 N N    . ASP   A 1 146 ? -6.764  5.898   24.363  1.00 42.38  ? 146 ASP   A N    1 
ATOM   1141 C CA   . ASP   A 1 146 ? -6.961  4.562   24.905  1.00 42.69  ? 146 ASP   A CA   1 
ATOM   1142 C C    . ASP   A 1 146 ? -8.255  4.525   25.716  1.00 45.34  ? 146 ASP   A C    1 
ATOM   1143 O O    . ASP   A 1 146 ? -8.986  5.515   25.802  1.00 45.54  ? 146 ASP   A O    1 
ATOM   1144 C CB   . ASP   A 1 146 ? -5.735  4.129   25.712  1.00 43.34  ? 146 ASP   A CB   1 
ATOM   1145 C CG   . ASP   A 1 146 ? -5.570  4.899   27.046  1.00 43.41  ? 146 ASP   A CG   1 
ATOM   1146 O OD1  . ASP   A 1 146 ? -6.501  5.632   27.480  1.00 43.57  ? 146 ASP   A OD1  1 
ATOM   1147 O OD2  . ASP   A 1 146 ? -4.486  4.737   27.661  1.00 42.58  ? 146 ASP   A OD2  1 
ATOM   1148 N N    . SER   A 1 147 ? -8.568  3.356   26.284  1.00 46.13  ? 147 SER   A N    1 
ATOM   1149 C CA   . SER   A 1 147 ? -9.818  3.185   27.009  1.00 47.48  ? 147 SER   A CA   1 
ATOM   1150 C C    . SER   A 1 147 ? -9.891  4.031   28.274  1.00 52.07  ? 147 SER   A C    1 
ATOM   1151 O O    . SER   A 1 147 ? -10.970 4.116   28.871  1.00 52.41  ? 147 SER   A O    1 
ATOM   1152 C CB   . SER   A 1 147 ? -10.060 1.706   27.354  1.00 50.43  ? 147 SER   A CB   1 
ATOM   1153 O OG   . SER   A 1 147 ? -8.852  0.976   27.491  1.00 48.03  ? 147 SER   A OG   1 
ATOM   1154 N N    . GLN   A 1 148 ? -8.780  4.612   28.733  1.00 57.54  ? 148 GLN   A N    1 
ATOM   1155 C CA   . GLN   A 1 148 ? -8.869  5.588   29.815  1.00 58.56  ? 148 GLN   A CA   1 
ATOM   1156 C C    . GLN   A 1 148 ? -9.026  7.007   29.292  1.00 60.73  ? 148 GLN   A C    1 
ATOM   1157 O O    . GLN   A 1 148 ? -9.234  7.922   30.095  1.00 59.72  ? 148 GLN   A O    1 
ATOM   1158 C CB   . GLN   A 1 148 ? -7.639  5.543   30.739  1.00 56.48  ? 148 GLN   A CB   1 
ATOM   1159 C CG   . GLN   A 1 148 ? -7.214  4.163   31.199  1.00 57.36  ? 148 GLN   A CG   1 
ATOM   1160 C CD   . GLN   A 1 148 ? -8.366  3.316   31.699  1.00 64.92  ? 148 GLN   A CD   1 
ATOM   1161 O OE1  . GLN   A 1 148 ? -8.925  3.557   32.775  1.00 70.67  ? 148 GLN   A OE1  1 
ATOM   1162 N NE2  . GLN   A 1 148 ? -8.722  2.297   30.914  1.00 69.85  ? 148 GLN   A NE2  1 
ATOM   1163 N N    . GLY   A 1 149 ? -8.944  7.212   27.973  1.00 44.42  ? 149 GLY   A N    1 
ATOM   1164 C CA   . GLY   A 1 149 ? -8.984  8.546   27.426  1.00 42.67  ? 149 GLY   A CA   1 
ATOM   1165 C C    . GLY   A 1 149 ? -7.635  9.203   27.307  1.00 42.54  ? 149 GLY   A C    1 
ATOM   1166 O O    . GLY   A 1 149 ? -7.569  10.436  27.219  1.00 44.28  ? 149 GLY   A O    1 
ATOM   1167 N N    . LYS   A 1 150 ? -6.556  8.438   27.401  1.00 46.27  ? 150 LYS   A N    1 
ATOM   1168 C CA   . LYS   A 1 150 ? -5.228  9.004   27.244  1.00 46.60  ? 150 LYS   A CA   1 
ATOM   1169 C C    . LYS   A 1 150 ? -4.878  9.179   25.770  1.00 48.04  ? 150 LYS   A C    1 
ATOM   1170 O O    . LYS   A 1 150 ? -5.286  8.390   24.911  1.00 47.40  ? 150 LYS   A O    1 
ATOM   1171 C CB   . LYS   A 1 150 ? -4.182  8.117   27.923  1.00 47.04  ? 150 LYS   A CB   1 
ATOM   1172 C CG   . LYS   A 1 150 ? -2.829  8.775   28.008  1.00 47.23  ? 150 LYS   A CG   1 
ATOM   1173 C CD   . LYS   A 1 150 ? -1.912  8.041   28.944  1.00 53.75  ? 150 LYS   A CD   1 
ATOM   1174 C CE   . LYS   A 1 150 ? -0.478  8.622   28.920  1.00 59.31  ? 150 LYS   A CE   1 
ATOM   1175 N NZ   . LYS   A 1 150 ? 0.633   7.692   28.487  1.00 54.65  ? 150 LYS   A NZ   1 
ATOM   1176 N N    . LEU   A 1 151 ? -4.122  10.234  25.477  1.00 46.63  ? 151 LEU   A N    1 
ATOM   1177 C CA   . LEU   A 1 151 ? -3.604  10.434  24.134  1.00 46.34  ? 151 LEU   A CA   1 
ATOM   1178 C C    . LEU   A 1 151 ? -2.416  9.495   23.985  1.00 47.60  ? 151 LEU   A C    1 
ATOM   1179 O O    . LEU   A 1 151 ? -1.404  9.661   24.674  1.00 47.70  ? 151 LEU   A O    1 
ATOM   1180 C CB   . LEU   A 1 151 ? -3.199  11.891  23.902  1.00 45.26  ? 151 LEU   A CB   1 
ATOM   1181 C CG   . LEU   A 1 151 ? -2.549  12.149  22.531  1.00 47.16  ? 151 LEU   A CG   1 
ATOM   1182 C CD1  . LEU   A 1 151 ? -3.478  11.701  21.403  1.00 41.68  ? 151 LEU   A CD1  1 
ATOM   1183 C CD2  . LEU   A 1 151 ? -2.209  13.622  22.362  1.00 46.06  ? 151 LEU   A CD2  1 
ATOM   1184 N N    . VAL   A 1 152 ? -2.559  8.456   23.162  1.00 42.56  ? 152 VAL   A N    1 
ATOM   1185 C CA   . VAL   A 1 152 ? -1.500  7.462   23.025  1.00 42.60  ? 152 VAL   A CA   1 
ATOM   1186 C C    . VAL   A 1 152 ? -0.849  7.448   21.647  1.00 45.50  ? 152 VAL   A C    1 
ATOM   1187 O O    . VAL   A 1 152 ? 0.169   6.757   21.478  1.00 48.17  ? 152 VAL   A O    1 
ATOM   1188 C CB   . VAL   A 1 152 ? -1.994  6.047   23.397  1.00 42.47  ? 152 VAL   A CB   1 
ATOM   1189 C CG1  . VAL   A 1 152 ? -2.488  6.028   24.876  1.00 41.16  ? 152 VAL   A CG1  1 
ATOM   1190 C CG2  . VAL   A 1 152 ? -3.096  5.566   22.454  1.00 40.89  ? 152 VAL   A CG2  1 
ATOM   1191 N N    . ALA   A 1 153 ? -1.371  8.182   20.666  1.00 48.02  ? 153 ALA   A N    1 
ATOM   1192 C CA   . ALA   A 1 153 ? -0.702  8.220   19.369  1.00 49.41  ? 153 ALA   A CA   1 
ATOM   1193 C C    . ALA   A 1 153 ? -1.212  9.400   18.555  1.00 49.13  ? 153 ALA   A C    1 
ATOM   1194 O O    . ALA   A 1 153 ? -2.411  9.703   18.568  1.00 49.62  ? 153 ALA   A O    1 
ATOM   1195 C CB   . ALA   A 1 153 ? -0.904  6.916   18.596  1.00 42.72  ? 153 ALA   A CB   1 
ATOM   1196 N N    . ARG   A 1 154 ? -0.292  10.046  17.840  1.00 46.10  ? 154 ARG   A N    1 
ATOM   1197 C CA   . ARG   A 1 154 ? -0.604  11.149  16.932  1.00 46.73  ? 154 ARG   A CA   1 
ATOM   1198 C C    . ARG   A 1 154 ? 0.200   10.935  15.655  1.00 45.91  ? 154 ARG   A C    1 
ATOM   1199 O O    . ARG   A 1 154 ? 1.425   10.787  15.721  1.00 46.33  ? 154 ARG   A O    1 
ATOM   1200 C CB   . ARG   A 1 154 ? -0.260  12.499  17.580  1.00 47.39  ? 154 ARG   A CB   1 
ATOM   1201 C CG   . ARG   A 1 154 ? -0.562  13.718  16.714  1.00 48.00  ? 154 ARG   A CG   1 
ATOM   1202 C CD   . ARG   A 1 154 ? 0.185   14.947  17.218  1.00 49.02  ? 154 ARG   A CD   1 
ATOM   1203 N NE   . ARG   A 1 154 ? 1.604   14.858  16.897  1.00 49.46  ? 154 ARG   A NE   1 
ATOM   1204 C CZ   . ARG   A 1 154 ? 2.551   15.601  17.454  1.00 48.72  ? 154 ARG   A CZ   1 
ATOM   1205 N NH1  . ARG   A 1 154 ? 2.268   16.515  18.368  1.00 45.70  ? 154 ARG   A NH1  1 
ATOM   1206 N NH2  . ARG   A 1 154 ? 3.816   15.404  17.103  1.00 50.85  ? 154 ARG   A NH2  1 
ATOM   1207 N N    . TYR   A 1 155 ? -0.475  10.885  14.501  1.00 44.71  ? 155 TYR   A N    1 
ATOM   1208 C CA   . TYR   A 1 155 ? 0.200   10.612  13.228  1.00 44.88  ? 155 TYR   A CA   1 
ATOM   1209 C C    . TYR   A 1 155 ? -0.190  11.644  12.174  1.00 46.38  ? 155 TYR   A C    1 
ATOM   1210 O O    . TYR   A 1 155 ? -1.374  11.787  11.843  1.00 42.32  ? 155 TYR   A O    1 
ATOM   1211 C CB   . TYR   A 1 155 ? -0.112  9.201   12.711  1.00 44.95  ? 155 TYR   A CB   1 
ATOM   1212 C CG   . TYR   A 1 155 ? 0.321   9.014   11.265  1.00 45.54  ? 155 TYR   A CG   1 
ATOM   1213 C CD1  . TYR   A 1 155 ? 1.668   8.927   10.926  1.00 45.96  ? 155 TYR   A CD1  1 
ATOM   1214 C CD2  . TYR   A 1 155 ? -0.619  8.993   10.231  1.00 47.61  ? 155 TYR   A CD2  1 
ATOM   1215 C CE1  . TYR   A 1 155 ? 2.072   8.786   9.583   1.00 49.48  ? 155 TYR   A CE1  1 
ATOM   1216 C CE2  . TYR   A 1 155 ? -0.235  8.843   8.904   1.00 47.12  ? 155 TYR   A CE2  1 
ATOM   1217 C CZ   . TYR   A 1 155 ? 1.109   8.741   8.582   1.00 49.77  ? 155 TYR   A CZ   1 
ATOM   1218 O OH   . TYR   A 1 155 ? 1.483   8.608   7.252   1.00 50.55  ? 155 TYR   A OH   1 
ATOM   1219 N N    . HIS   A 1 156 ? 0.818   12.312  11.606  1.00 46.46  ? 156 HIS   A N    1 
ATOM   1220 C CA   . HIS   A 1 156 ? 0.632   13.273  10.520  1.00 47.93  ? 156 HIS   A CA   1 
ATOM   1221 C C    . HIS   A 1 156 ? 0.777   12.565  9.170   1.00 47.32  ? 156 HIS   A C    1 
ATOM   1222 O O    . HIS   A 1 156 ? 1.844   12.014  8.859   1.00 45.19  ? 156 HIS   A O    1 
ATOM   1223 C CB   . HIS   A 1 156 ? 1.652   14.408  10.633  1.00 46.11  ? 156 HIS   A CB   1 
ATOM   1224 C CG   . HIS   A 1 156 ? 1.562   15.191  11.909  1.00 48.25  ? 156 HIS   A CG   1 
ATOM   1225 N ND1  . HIS   A 1 156 ? 2.664   15.485  12.682  1.00 48.66  ? 156 HIS   A ND1  1 
ATOM   1226 C CD2  . HIS   A 1 156 ? 0.502   15.745  12.544  1.00 44.75  ? 156 HIS   A CD2  1 
ATOM   1227 C CE1  . HIS   A 1 156 ? 2.285   16.191  13.735  1.00 47.84  ? 156 HIS   A CE1  1 
ATOM   1228 N NE2  . HIS   A 1 156 ? 0.980   16.371  13.668  1.00 46.49  ? 156 HIS   A NE2  1 
ATOM   1229 N N    . LYS   A 1 157 ? -0.275  12.635  8.349   1.00 48.04  ? 157 LYS   A N    1 
ATOM   1230 C CA   . LYS   A 1 157 ? -0.327  11.918  7.075   1.00 45.66  ? 157 LYS   A CA   1 
ATOM   1231 C C    . LYS   A 1 157 ? 0.875   12.273  6.221   1.00 47.97  ? 157 LYS   A C    1 
ATOM   1232 O O    . LYS   A 1 157 ? 1.125   13.448  5.931   1.00 46.84  ? 157 LYS   A O    1 
ATOM   1233 C CB   . LYS   A 1 157 ? -1.623  12.260  6.338   1.00 45.96  ? 157 LYS   A CB   1 
ATOM   1234 C CG   . LYS   A 1 157 ? -1.846  11.475  5.036   1.00 48.58  ? 157 LYS   A CG   1 
ATOM   1235 C CD   . LYS   A 1 157 ? -3.135  11.896  4.346   1.00 47.94  ? 157 LYS   A CD   1 
ATOM   1236 C CE   . LYS   A 1 157 ? -3.422  11.023  3.126   1.00 52.05  ? 157 LYS   A CE   1 
ATOM   1237 N NZ   . LYS   A 1 157 ? -4.659  11.446  2.382   1.00 50.03  ? 157 LYS   A NZ   1 
ATOM   1238 N N    . GLN   A 1 158 ? 1.617   11.248  5.811   1.00 48.02  ? 158 GLN   A N    1 
ATOM   1239 C CA   . GLN   A 1 158 ? 2.861   11.470  5.087   1.00 47.60  ? 158 GLN   A CA   1 
ATOM   1240 C C    . GLN   A 1 158 ? 2.619   11.715  3.599   1.00 49.82  ? 158 GLN   A C    1 
ATOM   1241 O O    . GLN   A 1 158 ? 3.235   12.604  2.995   1.00 46.45  ? 158 GLN   A O    1 
ATOM   1242 C CB   . GLN   A 1 158 ? 3.783   10.269  5.282   1.00 49.30  ? 158 GLN   A CB   1 
ATOM   1243 C CG   . GLN   A 1 158 ? 5.048   10.366  4.459   1.00 52.95  ? 158 GLN   A CG   1 
ATOM   1244 C CD   . GLN   A 1 158 ? 5.956   11.476  4.960   1.00 57.59  ? 158 GLN   A CD   1 
ATOM   1245 O OE1  . GLN   A 1 158 ? 5.881   11.878  6.136   1.00 54.06  ? 158 GLN   A OE1  1 
ATOM   1246 N NE2  . GLN   A 1 158 ? 6.813   11.982  4.081   1.00 54.09  ? 158 GLN   A NE2  1 
ATOM   1247 N N    . ASN   A 1 159 ? 1.736   10.929  3.002   1.00 53.79  ? 159 ASN   A N    1 
ATOM   1248 C CA   . ASN   A 1 159 ? 1.518   10.896  1.561   1.00 51.75  ? 159 ASN   A CA   1 
ATOM   1249 C C    . ASN   A 1 159 ? 0.203   11.616  1.264   1.00 52.64  ? 159 ASN   A C    1 
ATOM   1250 O O    . ASN   A 1 159 ? -0.877  11.022  1.329   1.00 53.11  ? 159 ASN   A O    1 
ATOM   1251 C CB   . ASN   A 1 159 ? 1.509   9.452   1.061   1.00 51.70  ? 159 ASN   A CB   1 
ATOM   1252 C CG   . ASN   A 1 159 ? 2.833   8.733   1.309   1.00 53.88  ? 159 ASN   A CG   1 
ATOM   1253 O OD1  . ASN   A 1 159 ? 3.696   8.700   0.437   1.00 59.14  ? 159 ASN   A OD1  1 
ATOM   1254 N ND2  . ASN   A 1 159 ? 2.986   8.137   2.478   1.00 53.81  ? 159 ASN   A ND2  1 
ATOM   1255 N N    . LEU   A 1 160 ? 0.298   12.908  0.930   1.00 55.80  ? 160 LEU   A N    1 
ATOM   1256 C CA   . LEU   A 1 160 ? -0.890  13.707  0.644   1.00 52.73  ? 160 LEU   A CA   1 
ATOM   1257 C C    . LEU   A 1 160 ? -1.430  13.384  -0.745  1.00 56.13  ? 160 LEU   A C    1 
ATOM   1258 O O    . LEU   A 1 160 ? -0.665  13.245  -1.703  1.00 56.99  ? 160 LEU   A O    1 
ATOM   1259 C CB   . LEU   A 1 160 ? -0.581  15.200  0.773   1.00 49.39  ? 160 LEU   A CB   1 
ATOM   1260 C CG   . LEU   A 1 160 ? -0.479  15.685  2.230   1.00 53.90  ? 160 LEU   A CG   1 
ATOM   1261 C CD1  . LEU   A 1 160 ? -0.258  17.202  2.333   1.00 50.25  ? 160 LEU   A CD1  1 
ATOM   1262 C CD2  . LEU   A 1 160 ? -1.695  15.256  3.068   1.00 49.26  ? 160 LEU   A CD2  1 
ATOM   1263 N N    . PHE   A 1 161 ? -2.748  13.211  -0.835  1.00 60.68  ? 161 PHE   A N    1 
ATOM   1264 C CA   . PHE   A 1 161 ? -3.433  13.033  -2.098  1.00 58.89  ? 161 PHE   A CA   1 
ATOM   1265 C C    . PHE   A 1 161 ? -3.645  14.399  -2.752  1.00 63.06  ? 161 PHE   A C    1 
ATOM   1266 O O    . PHE   A 1 161 ? -3.581  15.445  -2.090  1.00 58.86  ? 161 PHE   A O    1 
ATOM   1267 C CB   . PHE   A 1 161 ? -4.761  12.287  -1.890  1.00 61.00  ? 161 PHE   A CB   1 
ATOM   1268 C CG   . PHE   A 1 161 ? -5.318  11.695  -3.144  1.00 61.56  ? 161 PHE   A CG   1 
ATOM   1269 C CD1  . PHE   A 1 161 ? -4.697  10.610  -3.757  1.00 65.55  ? 161 PHE   A CD1  1 
ATOM   1270 C CD2  . PHE   A 1 161 ? -6.443  12.241  -3.746  1.00 63.25  ? 161 PHE   A CD2  1 
ATOM   1271 C CE1  . PHE   A 1 161 ? -5.189  10.083  -4.967  1.00 63.64  ? 161 PHE   A CE1  1 
ATOM   1272 C CE2  . PHE   A 1 161 ? -6.936  11.719  -4.944  1.00 65.64  ? 161 PHE   A CE2  1 
ATOM   1273 C CZ   . PHE   A 1 161 ? -6.310  10.635  -5.546  1.00 63.45  ? 161 PHE   A CZ   1 
ATOM   1274 N N    . MET   A 1 162 ? -3.835  14.388  -4.078  1.00 60.00  ? 162 MET   A N    1 
ATOM   1275 C CA   . MET   A 1 162 ? -4.162  15.619  -4.786  1.00 59.71  ? 162 MET   A CA   1 
ATOM   1276 C C    . MET   A 1 162 ? -5.432  16.236  -4.202  1.00 65.55  ? 162 MET   A C    1 
ATOM   1277 O O    . MET   A 1 162 ? -6.327  15.535  -3.717  1.00 64.79  ? 162 MET   A O    1 
ATOM   1278 C CB   . MET   A 1 162 ? -4.303  15.369  -6.297  1.00 62.26  ? 162 MET   A CB   1 
ATOM   1279 C CG   . MET   A 1 162 ? -5.456  14.497  -6.737  1.00 67.93  ? 162 MET   A CG   1 
ATOM   1280 S SD   . MET   A 1 162 ? -5.693  14.435  -8.556  1.00 76.29  ? 162 MET   A SD   1 
ATOM   1281 C CE   . MET   A 1 162 ? -4.846  15.921  -9.145  1.00 66.32  ? 162 MET   A CE   1 
ATOM   1282 N N    . GLY   A 1 163 ? -5.483  17.566  -4.192  1.00 57.30  ? 163 GLY   A N    1 
ATOM   1283 C CA   . GLY   A 1 163 ? -6.591  18.247  -3.554  1.00 54.69  ? 163 GLY   A CA   1 
ATOM   1284 C C    . GLY   A 1 163 ? -6.452  18.402  -2.057  1.00 58.46  ? 163 GLY   A C    1 
ATOM   1285 O O    . GLY   A 1 163 ? -7.400  18.851  -1.397  1.00 57.03  ? 163 GLY   A O    1 
ATOM   1286 N N    . GLU   A 1 164 ? -5.309  18.022  -1.493  1.00 64.32  ? 164 GLU   A N    1 
ATOM   1287 C CA   . GLU   A 1 164 ? -5.023  18.246  -0.078  1.00 64.02  ? 164 GLU   A CA   1 
ATOM   1288 C C    . GLU   A 1 164 ? -4.082  19.426  0.131   1.00 62.97  ? 164 GLU   A C    1 
ATOM   1289 O O    . GLU   A 1 164 ? -3.144  19.341  0.930   1.00 65.33  ? 164 GLU   A O    1 
ATOM   1290 C CB   . GLU   A 1 164 ? -4.466  16.981  0.565   1.00 61.43  ? 164 GLU   A CB   1 
ATOM   1291 C CG   . GLU   A 1 164 ? -5.476  15.840  0.657   1.00 61.49  ? 164 GLU   A CG   1 
ATOM   1292 C CD   . GLU   A 1 164 ? -5.305  14.991  1.906   1.00 60.72  ? 164 GLU   A CD   1 
ATOM   1293 O OE1  . GLU   A 1 164 ? -4.447  14.079  1.890   1.00 59.99  ? 164 GLU   A OE1  1 
ATOM   1294 O OE2  . GLU   A 1 164 ? -6.031  15.234  2.899   1.00 58.90  ? 164 GLU   A OE2  1 
ATOM   1295 N N    . ASN   A 1 165 ? -4.301  20.540  -0.578  1.00 55.66  ? 165 ASN   A N    1 
ATOM   1296 C CA   . ASN   A 1 165 ? -3.416  21.697  -0.464  1.00 55.92  ? 165 ASN   A CA   1 
ATOM   1297 C C    . ASN   A 1 165 ? -3.551  22.418  0.877   1.00 58.15  ? 165 ASN   A C    1 
ATOM   1298 O O    . ASN   A 1 165 ? -2.729  23.292  1.184   1.00 56.99  ? 165 ASN   A O    1 
ATOM   1299 C CB   . ASN   A 1 165 ? -3.695  22.695  -1.590  1.00 56.69  ? 165 ASN   A CB   1 
ATOM   1300 C CG   . ASN   A 1 165 ? -5.067  23.368  -1.450  1.00 64.23  ? 165 ASN   A CG   1 
ATOM   1301 O OD1  . ASN   A 1 165 ? -6.080  22.700  -1.207  1.00 64.52  ? 165 ASN   A OD1  1 
ATOM   1302 N ND2  . ASN   A 1 165 ? -5.099  24.698  -1.584  1.00 62.61  ? 165 ASN   A ND2  1 
ATOM   1303 N N    . GLN   A 1 166 ? -4.550  22.077  1.688   1.00 62.41  ? 166 GLN   A N    1 
ATOM   1304 C CA   . GLN   A 1 166 ? -4.637  22.673  3.015   1.00 62.63  ? 166 GLN   A CA   1 
ATOM   1305 C C    . GLN   A 1 166 ? -3.612  22.105  3.990   1.00 59.91  ? 166 GLN   A C    1 
ATOM   1306 O O    . GLN   A 1 166 ? -3.442  22.681  5.070   1.00 63.20  ? 166 GLN   A O    1 
ATOM   1307 C CB   . GLN   A 1 166 ? -6.054  22.499  3.578   1.00 60.58  ? 166 GLN   A CB   1 
ATOM   1308 C CG   . GLN   A 1 166 ? -6.467  21.052  3.840   1.00 59.43  ? 166 GLN   A CG   1 
ATOM   1309 C CD   . GLN   A 1 166 ? -7.079  20.384  2.610   1.00 62.08  ? 166 GLN   A CD   1 
ATOM   1310 O OE1  . GLN   A 1 166 ? -6.598  20.560  1.489   1.00 61.90  ? 166 GLN   A OE1  1 
ATOM   1311 N NE2  . GLN   A 1 166 ? -8.141  19.619  2.817   1.00 59.99  ? 166 GLN   A NE2  1 
ATOM   1312 N N    . PHE   A 1 167 ? -2.924  21.018  3.646   1.00 51.27  ? 167 PHE   A N    1 
ATOM   1313 C CA   . PHE   A 1 167 ? -2.046  20.324  4.579   1.00 51.58  ? 167 PHE   A CA   1 
ATOM   1314 C C    . PHE   A 1 167 ? -0.582  20.419  4.172   1.00 52.61  ? 167 PHE   A C    1 
ATOM   1315 O O    . PHE   A 1 167 ? -0.246  20.621  3.005   1.00 52.51  ? 167 PHE   A O    1 
ATOM   1316 C CB   . PHE   A 1 167 ? -2.443  18.852  4.702   1.00 50.09  ? 167 PHE   A CB   1 
ATOM   1317 C CG   . PHE   A 1 167 ? -3.773  18.644  5.348   1.00 49.67  ? 167 PHE   A CG   1 
ATOM   1318 C CD1  . PHE   A 1 167 ? -3.978  19.022  6.671   1.00 49.41  ? 167 PHE   A CD1  1 
ATOM   1319 C CD2  . PHE   A 1 167 ? -4.830  18.085  4.636   1.00 52.25  ? 167 PHE   A CD2  1 
ATOM   1320 C CE1  . PHE   A 1 167 ? -5.198  18.831  7.277   1.00 48.22  ? 167 PHE   A CE1  1 
ATOM   1321 C CE2  . PHE   A 1 167 ? -6.070  17.893  5.241   1.00 50.91  ? 167 PHE   A CE2  1 
ATOM   1322 C CZ   . PHE   A 1 167 ? -6.251  18.269  6.566   1.00 50.98  ? 167 PHE   A CZ   1 
ATOM   1323 N N    . ASN   A 1 168 ? 0.298   20.268  5.154   1.00 47.26  ? 168 ASN   A N    1 
ATOM   1324 C CA   . ASN   A 1 168 ? 1.722   20.151  4.879   1.00 51.74  ? 168 ASN   A CA   1 
ATOM   1325 C C    . ASN   A 1 168 ? 2.170   18.697  5.039   1.00 53.79  ? 168 ASN   A C    1 
ATOM   1326 O O    . ASN   A 1 168 ? 1.432   17.849  5.551   1.00 49.22  ? 168 ASN   A O    1 
ATOM   1327 C CB   . ASN   A 1 168 ? 2.539   21.075  5.788   1.00 51.69  ? 168 ASN   A CB   1 
ATOM   1328 C CG   . ASN   A 1 168 ? 2.188   22.541  5.597   1.00 52.60  ? 168 ASN   A CG   1 
ATOM   1329 O OD1  . ASN   A 1 168 ? 1.441   23.117  6.393   1.00 54.88  ? 168 ASN   A OD1  1 
ATOM   1330 N ND2  . ASN   A 1 168 ? 2.732   23.157  4.550   1.00 50.71  ? 168 ASN   A ND2  1 
ATOM   1331 N N    . VAL   A 1 169 ? 3.366   18.406  4.531   1.00 65.27  ? 169 VAL   A N    1 
ATOM   1332 C CA   . VAL   A 1 169 ? 3.976   17.077  4.635   1.00 63.14  ? 169 VAL   A CA   1 
ATOM   1333 C C    . VAL   A 1 169 ? 5.016   17.094  5.755   1.00 63.50  ? 169 VAL   A C    1 
ATOM   1334 O O    . VAL   A 1 169 ? 5.838   18.018  5.815   1.00 66.08  ? 169 VAL   A O    1 
ATOM   1335 C CB   . VAL   A 1 169 ? 4.605   16.649  3.295   1.00 62.58  ? 169 VAL   A CB   1 
ATOM   1336 C CG1  . VAL   A 1 169 ? 5.099   15.212  3.364   1.00 60.34  ? 169 VAL   A CG1  1 
ATOM   1337 C CG2  . VAL   A 1 169 ? 3.604   16.804  2.178   1.00 58.05  ? 169 VAL   A CG2  1 
ATOM   1338 N N    . PRO   A 1 170 ? 5.040   16.103  6.649   1.00 58.61  ? 170 PRO   A N    1 
ATOM   1339 C CA   . PRO   A 1 170 ? 6.084   16.078  7.682   1.00 56.90  ? 170 PRO   A CA   1 
ATOM   1340 C C    . PRO   A 1 170 ? 7.478   16.038  7.069   1.00 58.80  ? 170 PRO   A C    1 
ATOM   1341 O O    . PRO   A 1 170 ? 7.705   15.419  6.031   1.00 62.72  ? 170 PRO   A O    1 
ATOM   1342 C CB   . PRO   A 1 170 ? 5.782   14.793  8.460   1.00 55.40  ? 170 PRO   A CB   1 
ATOM   1343 C CG   . PRO   A 1 170 ? 4.330   14.557  8.249   1.00 54.51  ? 170 PRO   A CG   1 
ATOM   1344 C CD   . PRO   A 1 170 ? 4.019   15.064  6.864   1.00 53.68  ? 170 PRO   A CD   1 
ATOM   1345 N N    . LYS   A 1 171 ? 8.422   16.701  7.739   1.00 76.03  ? 171 LYS   A N    1 
ATOM   1346 C CA   . LYS   A 1 171 ? 9.808   16.695  7.281   1.00 72.78  ? 171 LYS   A CA   1 
ATOM   1347 C C    . LYS   A 1 171 ? 10.313  15.270  7.076   1.00 75.53  ? 171 LYS   A C    1 
ATOM   1348 O O    . LYS   A 1 171 ? 11.021  14.983  6.102   1.00 82.73  ? 171 LYS   A O    1 
ATOM   1349 C CB   . LYS   A 1 171 ? 10.693  17.433  8.291   1.00 83.45  ? 171 LYS   A CB   1 
ATOM   1350 C CG   . LYS   A 1 171 ? 9.941   18.431  9.182   1.00 81.96  ? 171 LYS   A CG   1 
ATOM   1351 C CD   . LYS   A 1 171 ? 10.874  19.185  10.132  1.00 88.25  ? 171 LYS   A CD   1 
ATOM   1352 C CE   . LYS   A 1 171 ? 11.742  18.230  10.946  1.00 86.20  ? 171 LYS   A CE   1 
ATOM   1353 N NZ   . LYS   A 1 171 ? 10.902  17.270  11.719  1.00 81.66  ? 171 LYS   A NZ   1 
ATOM   1354 N N    . GLU   A 1 172 ? 9.964   14.365  7.988   1.00 76.06  ? 172 GLU   A N    1 
ATOM   1355 C CA   . GLU   A 1 172 ? 10.296  12.955  7.878   1.00 76.35  ? 172 GLU   A CA   1 
ATOM   1356 C C    . GLU   A 1 172 ? 9.052   12.112  8.106   1.00 74.46  ? 172 GLU   A C    1 
ATOM   1357 O O    . GLU   A 1 172 ? 8.109   12.557  8.766   1.00 74.20  ? 172 GLU   A O    1 
ATOM   1358 C CB   . GLU   A 1 172 ? 11.381  12.548  8.881   1.00 77.44  ? 172 GLU   A CB   1 
ATOM   1359 C CG   . GLU   A 1 172 ? 12.706  12.232  8.214   1.00 84.49  ? 172 GLU   A CG   1 
ATOM   1360 C CD   . GLU   A 1 172 ? 13.542  11.263  9.023   1.00 88.76  ? 172 GLU   A CD   1 
ATOM   1361 O OE1  . GLU   A 1 172 ? 13.606  11.434  10.260  1.00 90.27  ? 172 GLU   A OE1  1 
ATOM   1362 O OE2  . GLU   A 1 172 ? 14.132  10.333  8.424   1.00 93.26  ? 172 GLU   A OE2  1 
ATOM   1363 N N    . PRO   A 1 173 ? 8.999   10.913  7.527   1.00 71.70  ? 173 PRO   A N    1 
ATOM   1364 C CA   . PRO   A 1 173 ? 7.849   10.033  7.772   1.00 70.15  ? 173 PRO   A CA   1 
ATOM   1365 C C    . PRO   A 1 173 ? 7.767   9.624   9.236   1.00 70.69  ? 173 PRO   A C    1 
ATOM   1366 O O    . PRO   A 1 173 ? 8.777   9.316   9.876   1.00 71.28  ? 173 PRO   A O    1 
ATOM   1367 C CB   . PRO   A 1 173 ? 8.118   8.829   6.860   1.00 71.31  ? 173 PRO   A CB   1 
ATOM   1368 C CG   . PRO   A 1 173 ? 9.018   9.364   5.794   1.00 69.11  ? 173 PRO   A CG   1 
ATOM   1369 C CD   . PRO   A 1 173 ? 9.890   10.381  6.483   1.00 72.67  ? 173 PRO   A CD   1 
ATOM   1370 N N    . GLU   A 1 174 ? 6.544   9.603   9.757   1.00 64.72  ? 174 GLU   A N    1 
ATOM   1371 C CA   . GLU   A 1 174 ? 6.294   9.312   11.163  1.00 62.33  ? 174 GLU   A CA   1 
ATOM   1372 C C    . GLU   A 1 174 ? 5.842   7.857   11.301  1.00 61.98  ? 174 GLU   A C    1 
ATOM   1373 O O    . GLU   A 1 174 ? 4.775   7.477   10.800  1.00 60.23  ? 174 GLU   A O    1 
ATOM   1374 C CB   . GLU   A 1 174 ? 5.253   10.275  11.736  1.00 63.89  ? 174 GLU   A CB   1 
ATOM   1375 C CG   . GLU   A 1 174 ? 5.598   11.754  11.569  1.00 61.73  ? 174 GLU   A CG   1 
ATOM   1376 C CD   . GLU   A 1 174 ? 4.528   12.668  12.128  1.00 58.56  ? 174 GLU   A CD   1 
ATOM   1377 O OE1  . GLU   A 1 174 ? 3.502   12.152  12.616  1.00 60.21  ? 174 GLU   A OE1  1 
ATOM   1378 O OE2  . GLU   A 1 174 ? 4.710   13.903  12.084  1.00 58.30  ? 174 GLU   A OE2  1 
ATOM   1379 N N    . ILE   A 1 175 ? 6.677   7.039   11.945  1.00 54.95  ? 175 ILE   A N    1 
ATOM   1380 C CA   . ILE   A 1 175 ? 6.344   5.652   12.260  1.00 52.33  ? 175 ILE   A CA   1 
ATOM   1381 C C    . ILE   A 1 175 ? 5.704   5.671   13.643  1.00 53.95  ? 175 ILE   A C    1 
ATOM   1382 O O    . ILE   A 1 175 ? 6.390   5.785   14.661  1.00 51.66  ? 175 ILE   A O    1 
ATOM   1383 C CB   . ILE   A 1 175 ? 7.571   4.740   12.219  1.00 54.97  ? 175 ILE   A CB   1 
ATOM   1384 C CG1  . ILE   A 1 175 ? 8.532   5.186   11.114  1.00 56.51  ? 175 ILE   A CG1  1 
ATOM   1385 C CG2  . ILE   A 1 175 ? 7.148   3.284   12.017  1.00 58.26  ? 175 ILE   A CG2  1 
ATOM   1386 C CD1  . ILE   A 1 175 ? 7.878   5.307   9.795   1.00 52.29  ? 175 ILE   A CD1  1 
ATOM   1387 N N    . VAL   A 1 176 ? 4.381   5.553   13.679  1.00 57.74  ? 176 VAL   A N    1 
ATOM   1388 C CA   . VAL   A 1 176 ? 3.602   5.735   14.894  1.00 52.90  ? 176 VAL   A CA   1 
ATOM   1389 C C    . VAL   A 1 176 ? 2.924   4.415   15.222  1.00 56.27  ? 176 VAL   A C    1 
ATOM   1390 O O    . VAL   A 1 176 ? 2.221   3.839   14.379  1.00 55.65  ? 176 VAL   A O    1 
ATOM   1391 C CB   . VAL   A 1 176 ? 2.560   6.857   14.737  1.00 55.38  ? 176 VAL   A CB   1 
ATOM   1392 C CG1  . VAL   A 1 176 ? 1.714   6.963   15.997  1.00 52.85  ? 176 VAL   A CG1  1 
ATOM   1393 C CG2  . VAL   A 1 176 ? 3.243   8.179   14.422  1.00 53.09  ? 176 VAL   A CG2  1 
ATOM   1394 N N    . THR   A 1 177 ? 3.151   3.933   16.436  1.00 54.86  ? 177 THR   A N    1 
ATOM   1395 C CA   . THR   A 1 177 ? 2.528   2.723   16.943  1.00 55.88  ? 177 THR   A CA   1 
ATOM   1396 C C    . THR   A 1 177 ? 2.023   2.977   18.351  1.00 53.61  ? 177 THR   A C    1 
ATOM   1397 O O    . THR   A 1 177 ? 2.386   3.965   18.996  1.00 52.23  ? 177 THR   A O    1 
ATOM   1398 C CB   . THR   A 1 177 ? 3.500   1.542   16.981  1.00 56.61  ? 177 THR   A CB   1 
ATOM   1399 O OG1  . THR   A 1 177 ? 4.521   1.824   17.940  1.00 59.67  ? 177 THR   A OG1  1 
ATOM   1400 C CG2  . THR   A 1 177 ? 4.135   1.301   15.612  1.00 53.33  ? 177 THR   A CG2  1 
ATOM   1401 N N    . PHE   A 1 178 ? 1.152   2.080   18.806  1.00 56.75  ? 178 PHE   A N    1 
ATOM   1402 C CA   . PHE   A 1 178 ? 0.759   2.021   20.209  1.00 55.14  ? 178 PHE   A CA   1 
ATOM   1403 C C    . PHE   A 1 178 ? 0.522   0.561   20.563  1.00 58.54  ? 178 PHE   A C    1 
ATOM   1404 O O    . PHE   A 1 178 ? 0.049   -0.209  19.722  1.00 58.28  ? 178 PHE   A O    1 
ATOM   1405 C CB   . PHE   A 1 178 ? -0.492  2.868   20.513  1.00 51.57  ? 178 PHE   A CB   1 
ATOM   1406 C CG   . PHE   A 1 178 ? -1.687  2.546   19.637  1.00 54.95  ? 178 PHE   A CG   1 
ATOM   1407 C CD1  . PHE   A 1 178 ? -1.770  3.041   18.342  1.00 52.05  ? 178 PHE   A CD1  1 
ATOM   1408 C CD2  . PHE   A 1 178 ? -2.738  1.774   20.120  1.00 52.23  ? 178 PHE   A CD2  1 
ATOM   1409 C CE1  . PHE   A 1 178 ? -2.868  2.759   17.544  1.00 51.14  ? 178 PHE   A CE1  1 
ATOM   1410 C CE2  . PHE   A 1 178 ? -3.833  1.477   19.319  1.00 50.69  ? 178 PHE   A CE2  1 
ATOM   1411 C CZ   . PHE   A 1 178 ? -3.897  1.972   18.031  1.00 50.90  ? 178 PHE   A CZ   1 
ATOM   1412 N N    . ASN   A 1 179 ? 0.873   0.184   21.797  1.00 53.96  ? 179 ASN   A N    1 
ATOM   1413 C CA   . ASN   A 1 179 ? 0.786   -1.188  22.282  1.00 55.78  ? 179 ASN   A CA   1 
ATOM   1414 C C    . ASN   A 1 179 ? -0.408  -1.338  23.222  1.00 56.58  ? 179 ASN   A C    1 
ATOM   1415 O O    . ASN   A 1 179 ? -0.770  -0.412  23.958  1.00 53.34  ? 179 ASN   A O    1 
ATOM   1416 C CB   . ASN   A 1 179 ? 2.077   -1.604  23.004  1.00 55.06  ? 179 ASN   A CB   1 
ATOM   1417 C CG   . ASN   A 1 179 ? 2.134   -3.111  23.294  1.00 65.29  ? 179 ASN   A CG   1 
ATOM   1418 O OD1  . ASN   A 1 179 ? 1.616   -3.924  22.514  1.00 62.40  ? 179 ASN   A OD1  1 
ATOM   1419 N ND2  . ASN   A 1 179 ? 2.759   -3.490  24.425  1.00 66.50  ? 179 ASN   A ND2  1 
ATOM   1420 N N    . THR   A 1 180 ? -1.009  -2.528  23.205  1.00 63.81  ? 180 THR   A N    1 
ATOM   1421 C CA   . THR   A 1 180 ? -2.206  -2.793  23.989  1.00 62.51  ? 180 THR   A CA   1 
ATOM   1422 C C    . THR   A 1 180 ? -2.211  -4.242  24.463  1.00 64.31  ? 180 THR   A C    1 
ATOM   1423 O O    . THR   A 1 180 ? -1.450  -5.094  23.982  1.00 66.72  ? 180 THR   A O    1 
ATOM   1424 C CB   . THR   A 1 180 ? -3.482  -2.494  23.179  1.00 61.03  ? 180 THR   A CB   1 
ATOM   1425 O OG1  . THR   A 1 180 ? -3.812  -3.624  22.356  1.00 64.56  ? 180 THR   A OG1  1 
ATOM   1426 C CG2  . THR   A 1 180 ? -3.306  -1.262  22.308  1.00 59.04  ? 180 THR   A CG2  1 
ATOM   1427 N N    . THR   A 1 181 ? -3.100  -4.514  25.416  1.00 46.37  ? 181 THR   A N    1 
ATOM   1428 C CA   . THR   A 1 181 ? -3.301  -5.877  25.885  1.00 48.75  ? 181 THR   A CA   1 
ATOM   1429 C C    . THR   A 1 181 ? -3.808  -6.806  24.788  1.00 50.43  ? 181 THR   A C    1 
ATOM   1430 O O    . THR   A 1 181 ? -3.770  -8.033  24.965  1.00 51.78  ? 181 THR   A O    1 
ATOM   1431 C CB   . THR   A 1 181 ? -4.299  -5.868  27.052  1.00 50.98  ? 181 THR   A CB   1 
ATOM   1432 O OG1  . THR   A 1 181 ? -5.568  -5.361  26.584  1.00 52.82  ? 181 THR   A OG1  1 
ATOM   1433 C CG2  . THR   A 1 181 ? -3.785  -4.989  28.198  1.00 49.86  ? 181 THR   A CG2  1 
ATOM   1434 N N    . PHE   A 1 182 ? -4.294  -6.255  23.670  1.00 51.42  ? 182 PHE   A N    1 
ATOM   1435 C CA   . PHE   A 1 182 ? -4.717  -7.045  22.519  1.00 50.27  ? 182 PHE   A CA   1 
ATOM   1436 C C    . PHE   A 1 182 ? -3.874  -6.738  21.272  1.00 53.01  ? 182 PHE   A C    1 
ATOM   1437 O O    . PHE   A 1 182 ? -4.393  -6.754  20.151  1.00 51.26  ? 182 PHE   A O    1 
ATOM   1438 C CB   . PHE   A 1 182 ? -6.214  -6.849  22.237  1.00 48.56  ? 182 PHE   A CB   1 
ATOM   1439 C CG   . PHE   A 1 182 ? -6.669  -5.409  22.279  1.00 50.74  ? 182 PHE   A CG   1 
ATOM   1440 C CD1  . PHE   A 1 182 ? -6.772  -4.719  23.483  1.00 48.68  ? 182 PHE   A CD1  1 
ATOM   1441 C CD2  . PHE   A 1 182 ? -7.037  -4.752  21.097  1.00 45.88  ? 182 PHE   A CD2  1 
ATOM   1442 C CE1  . PHE   A 1 182 ? -7.200  -3.391  23.525  1.00 48.49  ? 182 PHE   A CE1  1 
ATOM   1443 C CE2  . PHE   A 1 182 ? -7.466  -3.418  21.126  1.00 44.85  ? 182 PHE   A CE2  1 
ATOM   1444 C CZ   . PHE   A 1 182 ? -7.548  -2.737  22.352  1.00 48.82  ? 182 PHE   A CZ   1 
ATOM   1445 N N    . GLY   A 1 183 ? -2.596  -6.417  21.444  1.00 55.60  ? 183 GLY   A N    1 
ATOM   1446 C CA   . GLY   A 1 183 ? -1.652  -6.422  20.342  1.00 50.06  ? 183 GLY   A CA   1 
ATOM   1447 C C    . GLY   A 1 183 ? -0.974  -5.078  20.139  1.00 52.37  ? 183 GLY   A C    1 
ATOM   1448 O O    . GLY   A 1 183 ? -1.322  -4.062  20.744  1.00 50.58  ? 183 GLY   A O    1 
ATOM   1449 N N    . SER   A 1 184 ? 0.016   -5.103  19.246  1.00 55.10  ? 184 SER   A N    1 
ATOM   1450 C CA   . SER   A 1 184 ? 0.731   -3.901  18.832  1.00 59.48  ? 184 SER   A CA   1 
ATOM   1451 C C    . SER   A 1 184 ? 0.102   -3.329  17.557  1.00 57.25  ? 184 SER   A C    1 
ATOM   1452 O O    . SER   A 1 184 ? -0.082  -4.051  16.571  1.00 58.84  ? 184 SER   A O    1 
ATOM   1453 C CB   . SER   A 1 184 ? 2.208   -4.228  18.607  1.00 57.41  ? 184 SER   A CB   1 
ATOM   1454 O OG   . SER   A 1 184 ? 2.953   -3.063  18.285  1.00 64.58  ? 184 SER   A OG   1 
ATOM   1455 N N    . PHE   A 1 185 ? -0.206  -2.029  17.562  1.00 50.64  ? 185 PHE   A N    1 
ATOM   1456 C CA   . PHE   A 1 185 ? -0.963  -1.387  16.491  1.00 49.83  ? 185 PHE   A CA   1 
ATOM   1457 C C    . PHE   A 1 185 ? -0.118  -0.338  15.775  1.00 50.81  ? 185 PHE   A C    1 
ATOM   1458 O O    . PHE   A 1 185 ? 0.592   0.444   16.419  1.00 48.45  ? 185 PHE   A O    1 
ATOM   1459 C CB   . PHE   A 1 185 ? -2.229  -0.687  17.030  1.00 48.42  ? 185 PHE   A CB   1 
ATOM   1460 C CG   . PHE   A 1 185 ? -3.380  -1.616  17.316  1.00 48.94  ? 185 PHE   A CG   1 
ATOM   1461 C CD1  . PHE   A 1 185 ? -3.332  -2.500  18.392  1.00 48.33  ? 185 PHE   A CD1  1 
ATOM   1462 C CD2  . PHE   A 1 185 ? -4.526  -1.579  16.538  1.00 45.97  ? 185 PHE   A CD2  1 
ATOM   1463 C CE1  . PHE   A 1 185 ? -4.406  -3.352  18.657  1.00 48.80  ? 185 PHE   A CE1  1 
ATOM   1464 C CE2  . PHE   A 1 185 ? -5.593  -2.425  16.799  1.00 44.54  ? 185 PHE   A CE2  1 
ATOM   1465 C CZ   . PHE   A 1 185 ? -5.531  -3.315  17.850  1.00 48.63  ? 185 PHE   A CZ   1 
ATOM   1466 N N    . GLY   A 1 186 ? -0.236  -0.303  14.443  1.00 50.00  ? 186 GLY   A N    1 
ATOM   1467 C CA   . GLY   A 1 186 ? 0.328   0.769   13.649  1.00 46.74  ? 186 GLY   A CA   1 
ATOM   1468 C C    . GLY   A 1 186 ? -0.758  1.580   12.977  1.00 46.13  ? 186 GLY   A C    1 
ATOM   1469 O O    . GLY   A 1 186 ? -1.875  1.083   12.783  1.00 46.85  ? 186 GLY   A O    1 
ATOM   1470 N N    . ILE   A 1 187 ? -0.449  2.819   12.595  1.00 50.84  ? 187 ILE   A N    1 
ATOM   1471 C CA   . ILE   A 1 187 ? -1.454  3.721   12.039  1.00 53.09  ? 187 ILE   A CA   1 
ATOM   1472 C C    . ILE   A 1 187 ? -0.897  4.448   10.812  1.00 54.66  ? 187 ILE   A C    1 
ATOM   1473 O O    . ILE   A 1 187 ? 0.252   4.908   10.816  1.00 53.10  ? 187 ILE   A O    1 
ATOM   1474 C CB   . ILE   A 1 187 ? -1.930  4.729   13.105  1.00 50.15  ? 187 ILE   A CB   1 
ATOM   1475 C CG1  . ILE   A 1 187 ? -2.997  5.661   12.528  1.00 51.84  ? 187 ILE   A CG1  1 
ATOM   1476 C CG2  . ILE   A 1 187 ? -0.750  5.519   13.661  1.00 48.96  ? 187 ILE   A CG2  1 
ATOM   1477 C CD1  . ILE   A 1 187 ? -3.973  6.168   13.573  1.00 53.54  ? 187 ILE   A CD1  1 
ATOM   1478 N N    . PHE   A 1 188 ? -1.725  4.549   9.767   1.00 49.88  ? 188 PHE   A N    1 
ATOM   1479 C CA   . PHE   A 1 188 ? -1.504  5.437   8.624   1.00 52.67  ? 188 PHE   A CA   1 
ATOM   1480 C C    . PHE   A 1 188 ? -2.863  5.742   7.997   1.00 52.86  ? 188 PHE   A C    1 
ATOM   1481 O O    . PHE   A 1 188 ? -3.895  5.231   8.439   1.00 50.30  ? 188 PHE   A O    1 
ATOM   1482 C CB   . PHE   A 1 188 ? -0.514  4.863   7.591   1.00 51.71  ? 188 PHE   A CB   1 
ATOM   1483 C CG   . PHE   A 1 188 ? -0.802  3.442   7.153   1.00 52.50  ? 188 PHE   A CG   1 
ATOM   1484 C CD1  . PHE   A 1 188 ? -1.839  3.164   6.277   1.00 55.62  ? 188 PHE   A CD1  1 
ATOM   1485 C CD2  . PHE   A 1 188 ? 0.006   2.396   7.577   1.00 51.07  ? 188 PHE   A CD2  1 
ATOM   1486 C CE1  . PHE   A 1 188 ? -2.082  1.869   5.856   1.00 54.24  ? 188 PHE   A CE1  1 
ATOM   1487 C CE2  . PHE   A 1 188 ? -0.234  1.103   7.176   1.00 50.83  ? 188 PHE   A CE2  1 
ATOM   1488 C CZ   . PHE   A 1 188 ? -1.282  0.835   6.308   1.00 54.66  ? 188 PHE   A CZ   1 
ATOM   1489 N N    . THR   A 1 189 ? -2.862  6.629   6.996   1.00 44.89  ? 189 THR   A N    1 
ATOM   1490 C CA   . THR   A 1 189 ? -4.083  7.280   6.521   1.00 44.52  ? 189 THR   A CA   1 
ATOM   1491 C C    . THR   A 1 189 ? -4.240  7.125   5.012   1.00 45.30  ? 189 THR   A C    1 
ATOM   1492 O O    . THR   A 1 189 ? -3.382  7.580   4.246   1.00 46.85  ? 189 THR   A O    1 
ATOM   1493 C CB   . THR   A 1 189 ? -4.065  8.770   6.900   1.00 43.19  ? 189 THR   A CB   1 
ATOM   1494 O OG1  . THR   A 1 189 ? -3.641  8.897   8.259   1.00 45.12  ? 189 THR   A OG1  1 
ATOM   1495 C CG2  . THR   A 1 189 ? -5.441  9.407   6.761   1.00 40.44  ? 189 THR   A CG2  1 
ATOM   1496 N N    . CYS   A 1 190 ? -5.361  6.538   4.588   1.00 49.90  ? 190 CYS   A N    1 
ATOM   1497 C CA   . CYS   A 1 190 ? -5.797  6.524   3.192   1.00 55.23  ? 190 CYS   A CA   1 
ATOM   1498 C C    . CYS   A 1 190 ? -4.669  6.267   2.191   1.00 50.33  ? 190 CYS   A C    1 
ATOM   1499 O O    . CYS   A 1 190 ? -4.124  5.154   2.109   1.00 47.67  ? 190 CYS   A O    1 
ATOM   1500 C CB   . CYS   A 1 190 ? -6.476  7.861   2.867   1.00 54.25  ? 190 CYS   A CB   1 
ATOM   1501 S SG   . CYS   A 1 190 ? -7.836  7.768   1.671   1.00 53.51  ? 190 CYS   A SG   1 
ATOM   1502 N N    . PHE   A 1 191 ? -4.277  7.324   1.471   1.00 48.48  ? 191 PHE   A N    1 
ATOM   1503 C CA   . PHE   A 1 191 ? -3.316  7.193   0.372   1.00 49.41  ? 191 PHE   A CA   1 
ATOM   1504 C C    . PHE   A 1 191 ? -2.035  6.505   0.830   1.00 53.74  ? 191 PHE   A C    1 
ATOM   1505 O O    . PHE   A 1 191 ? -1.360  5.846   0.025   1.00 51.99  ? 191 PHE   A O    1 
ATOM   1506 C CB   . PHE   A 1 191 ? -2.998  8.580   -0.207  1.00 56.61  ? 191 PHE   A CB   1 
ATOM   1507 C CG   . PHE   A 1 191 ? -2.419  8.563   -1.619  1.00 54.02  ? 191 PHE   A CG   1 
ATOM   1508 C CD1  . PHE   A 1 191 ? -2.666  7.509   -2.483  1.00 52.29  ? 191 PHE   A CD1  1 
ATOM   1509 C CD2  . PHE   A 1 191 ? -1.642  9.620   -2.065  1.00 54.29  ? 191 PHE   A CD2  1 
ATOM   1510 C CE1  . PHE   A 1 191 ? -2.146  7.498   -3.768  1.00 56.76  ? 191 PHE   A CE1  1 
ATOM   1511 C CE2  . PHE   A 1 191 ? -1.113  9.630   -3.350  1.00 59.46  ? 191 PHE   A CE2  1 
ATOM   1512 C CZ   . PHE   A 1 191 ? -1.374  8.565   -4.217  1.00 58.82  ? 191 PHE   A CZ   1 
ATOM   1513 N N    . ASP   A 1 192 ? -1.707  6.614   2.129   1.00 51.52  ? 192 ASP   A N    1 
ATOM   1514 C CA   . ASP   A 1 192 ? -0.489  6.020   2.658   1.00 48.83  ? 192 ASP   A CA   1 
ATOM   1515 C C    . ASP   A 1 192 ? -0.382  4.561   2.285   1.00 48.25  ? 192 ASP   A C    1 
ATOM   1516 O O    . ASP   A 1 192 ? 0.726   4.036   2.161   1.00 49.67  ? 192 ASP   A O    1 
ATOM   1517 C CB   . ASP   A 1 192 ? -0.463  6.121   4.182   1.00 51.16  ? 192 ASP   A CB   1 
ATOM   1518 C CG   . ASP   A 1 192 ? -0.023  7.485   4.690   1.00 52.33  ? 192 ASP   A CG   1 
ATOM   1519 O OD1  . ASP   A 1 192 ? 0.596   8.257   3.926   1.00 54.90  ? 192 ASP   A OD1  1 
ATOM   1520 O OD2  . ASP   A 1 192 ? -0.307  7.776   5.881   1.00 52.74  ? 192 ASP   A OD2  1 
ATOM   1521 N N    . ILE   A 1 193 ? -1.516  3.862   2.194   1.00 43.25  ? 193 ILE   A N    1 
ATOM   1522 C CA   . ILE   A 1 193 ? -1.472  2.419   1.972   1.00 45.99  ? 193 ILE   A CA   1 
ATOM   1523 C C    . ILE   A 1 193 ? -0.764  2.061   0.647   1.00 48.91  ? 193 ILE   A C    1 
ATOM   1524 O O    . ILE   A 1 193 ? -0.332  0.916   0.460   1.00 47.56  ? 193 ILE   A O    1 
ATOM   1525 C CB   . ILE   A 1 193 ? -2.902  1.825   2.057   1.00 44.95  ? 193 ILE   A CB   1 
ATOM   1526 C CG1  . ILE   A 1 193 ? -2.846  0.305   2.232   1.00 44.77  ? 193 ILE   A CG1  1 
ATOM   1527 C CG2  . ILE   A 1 193 ? -3.735  2.185   0.822   1.00 46.33  ? 193 ILE   A CG2  1 
ATOM   1528 C CD1  . ILE   A 1 193 ? -4.205  -0.385  2.026   1.00 43.81  ? 193 ILE   A CD1  1 
ATOM   1529 N N    . LEU   A 1 194 ? -0.611  3.009   -0.272  1.00 49.52  ? 194 LEU   A N    1 
ATOM   1530 C CA   . LEU   A 1 194 ? 0.028   2.670   -1.539  1.00 55.37  ? 194 LEU   A CA   1 
ATOM   1531 C C    . LEU   A 1 194 ? 1.542   2.859   -1.527  1.00 55.07  ? 194 LEU   A C    1 
ATOM   1532 O O    . LEU   A 1 194 ? 2.187   2.589   -2.547  1.00 53.62  ? 194 LEU   A O    1 
ATOM   1533 C CB   . LEU   A 1 194 ? -0.583  3.496   -2.676  1.00 50.33  ? 194 LEU   A CB   1 
ATOM   1534 C CG   . LEU   A 1 194 ? -1.700  2.763   -3.414  1.00 54.38  ? 194 LEU   A CG   1 
ATOM   1535 C CD1  . LEU   A 1 194 ? -2.552  3.763   -4.201  1.00 57.50  ? 194 LEU   A CD1  1 
ATOM   1536 C CD2  . LEU   A 1 194 ? -1.115  1.689   -4.353  1.00 57.32  ? 194 LEU   A CD2  1 
ATOM   1537 N N    . PHE   A 1 195 ? 2.129   3.257   -0.396  1.00 55.46  ? 195 PHE   A N    1 
ATOM   1538 C CA   . PHE   A 1 195 ? 3.536   3.637   -0.345  1.00 59.66  ? 195 PHE   A CA   1 
ATOM   1539 C C    . PHE   A 1 195 ? 4.260   2.874   0.756   1.00 55.95  ? 195 PHE   A C    1 
ATOM   1540 O O    . PHE   A 1 195 ? 3.669   2.068   1.478   1.00 54.78  ? 195 PHE   A O    1 
ATOM   1541 C CB   . PHE   A 1 195 ? 3.682   5.155   -0.164  1.00 58.65  ? 195 PHE   A CB   1 
ATOM   1542 C CG   . PHE   A 1 195 ? 3.156   5.920   -1.331  1.00 57.90  ? 195 PHE   A CG   1 
ATOM   1543 C CD1  . PHE   A 1 195 ? 3.865   5.942   -2.523  1.00 62.08  ? 195 PHE   A CD1  1 
ATOM   1544 C CD2  . PHE   A 1 195 ? 1.929   6.564   -1.270  1.00 58.42  ? 195 PHE   A CD2  1 
ATOM   1545 C CE1  . PHE   A 1 195 ? 3.373   6.613   -3.639  1.00 60.97  ? 195 PHE   A CE1  1 
ATOM   1546 C CE2  . PHE   A 1 195 ? 1.432   7.242   -2.387  1.00 62.92  ? 195 PHE   A CE2  1 
ATOM   1547 C CZ   . PHE   A 1 195 ? 2.158   7.258   -3.572  1.00 57.89  ? 195 PHE   A CZ   1 
ATOM   1548 N N    . HIS   A 1 196 ? 5.583   3.055   0.791   1.00 62.70  ? 196 HIS   A N    1 
ATOM   1549 C CA   . HIS   A 1 196 ? 6.428   2.286   1.700   1.00 66.26  ? 196 HIS   A CA   1 
ATOM   1550 C C    . HIS   A 1 196 ? 6.425   2.867   3.111   1.00 65.11  ? 196 HIS   A C    1 
ATOM   1551 O O    . HIS   A 1 196 ? 6.456   2.119   4.095   1.00 65.20  ? 196 HIS   A O    1 
ATOM   1552 C CB   . HIS   A 1 196 ? 7.856   2.220   1.158   1.00 66.71  ? 196 HIS   A CB   1 
ATOM   1553 C CG   . HIS   A 1 196 ? 8.735   1.247   1.882   1.00 67.59  ? 196 HIS   A CG   1 
ATOM   1554 N ND1  . HIS   A 1 196 ? 9.568   1.621   2.916   1.00 65.83  ? 196 HIS   A ND1  1 
ATOM   1555 C CD2  . HIS   A 1 196 ? 8.917   -0.085  1.716   1.00 67.64  ? 196 HIS   A CD2  1 
ATOM   1556 C CE1  . HIS   A 1 196 ? 10.227  0.562   3.352   1.00 65.32  ? 196 HIS   A CE1  1 
ATOM   1557 N NE2  . HIS   A 1 196 ? 9.850   -0.486  2.641   1.00 66.86  ? 196 HIS   A NE2  1 
ATOM   1558 N N    . ASP   A 1 197 ? 6.396   4.191   3.227   1.00 60.35  ? 197 ASP   A N    1 
ATOM   1559 C CA   . ASP   A 1 197 ? 6.576   4.859   4.500   1.00 60.90  ? 197 ASP   A CA   1 
ATOM   1560 C C    . ASP   A 1 197 ? 5.332   5.661   4.845   1.00 58.86  ? 197 ASP   A C    1 
ATOM   1561 O O    . ASP   A 1 197 ? 4.884   6.478   4.028   1.00 57.29  ? 197 ASP   A O    1 
ATOM   1562 C CB   . ASP   A 1 197 ? 7.800   5.775   4.453   1.00 56.07  ? 197 ASP   A CB   1 
ATOM   1563 C CG   . ASP   A 1 197 ? 9.077   5.001   4.180   1.00 61.07  ? 197 ASP   A CG   1 
ATOM   1564 O OD1  . ASP   A 1 197 ? 9.078   3.761   4.351   1.00 67.81  ? 197 ASP   A OD1  1 
ATOM   1565 O OD2  . ASP   A 1 197 ? 10.079  5.626   3.773   1.00 70.47  ? 197 ASP   A OD2  1 
ATOM   1566 N N    . PRO   A 1 198 ? 4.745   5.458   6.042   1.00 54.54  ? 198 PRO   A N    1 
ATOM   1567 C CA   . PRO   A 1 198 ? 5.191   4.524   7.079   1.00 52.63  ? 198 PRO   A CA   1 
ATOM   1568 C C    . PRO   A 1 198 ? 4.659   3.112   6.875   1.00 53.10  ? 198 PRO   A C    1 
ATOM   1569 O O    . PRO   A 1 198 ? 5.128   2.176   7.515   1.00 52.26  ? 198 PRO   A O    1 
ATOM   1570 C CB   . PRO   A 1 198 ? 4.623   5.160   8.356   1.00 51.50  ? 198 PRO   A CB   1 
ATOM   1571 C CG   . PRO   A 1 198 ? 3.314   5.779   7.900   1.00 50.75  ? 198 PRO   A CG   1 
ATOM   1572 C CD   . PRO   A 1 198 ? 3.553   6.229   6.474   1.00 51.00  ? 198 PRO   A CD   1 
ATOM   1573 N N    . ALA   A 1 199 ? 3.723   2.925   5.942   1.00 52.61  ? 199 ALA   A N    1 
ATOM   1574 C CA   . ALA   A 1 199 ? 2.877   1.730   5.936   1.00 53.79  ? 199 ALA   A CA   1 
ATOM   1575 C C    . ALA   A 1 199 ? 3.694   0.443   5.926   1.00 55.55  ? 199 ALA   A C    1 
ATOM   1576 O O    . ALA   A 1 199 ? 3.398   -0.498  6.671   1.00 54.43  ? 199 ALA   A O    1 
ATOM   1577 C CB   . ALA   A 1 199 ? 1.942   1.761   4.723   1.00 54.46  ? 199 ALA   A CB   1 
ATOM   1578 N N    . VAL   A 1 200 ? 4.697   0.356   5.051   1.00 60.39  ? 200 VAL   A N    1 
ATOM   1579 C CA   . VAL   A 1 200 ? 5.446   -0.894  4.973   1.00 61.14  ? 200 VAL   A CA   1 
ATOM   1580 C C    . VAL   A 1 200 ? 6.461   -1.000  6.108   1.00 58.99  ? 200 VAL   A C    1 
ATOM   1581 O O    . VAL   A 1 200 ? 6.740   -2.107  6.580   1.00 59.76  ? 200 VAL   A O    1 
ATOM   1582 C CB   . VAL   A 1 200 ? 6.116   -1.052  3.593   1.00 58.33  ? 200 VAL   A CB   1 
ATOM   1583 C CG1  . VAL   A 1 200 ? 6.982   -2.294  3.573   1.00 58.73  ? 200 VAL   A CG1  1 
ATOM   1584 C CG2  . VAL   A 1 200 ? 5.059   -1.150  2.491   1.00 59.31  ? 200 VAL   A CG2  1 
ATOM   1585 N N    . THR   A 1 201 ? 7.035   0.124   6.553   1.00 53.52  ? 201 THR   A N    1 
ATOM   1586 C CA   . THR   A 1 201 ? 7.960   0.096   7.690   1.00 58.11  ? 201 THR   A CA   1 
ATOM   1587 C C    . THR   A 1 201 ? 7.277   -0.433  8.953   1.00 55.84  ? 201 THR   A C    1 
ATOM   1588 O O    . THR   A 1 201 ? 7.871   -1.197  9.725   1.00 54.78  ? 201 THR   A O    1 
ATOM   1589 C CB   . THR   A 1 201 ? 8.524   1.499   7.938   1.00 57.84  ? 201 THR   A CB   1 
ATOM   1590 O OG1  . THR   A 1 201 ? 9.230   1.927   6.770   1.00 60.67  ? 201 THR   A OG1  1 
ATOM   1591 C CG2  . THR   A 1 201 ? 9.469   1.513   9.157   1.00 54.93  ? 201 THR   A CG2  1 
ATOM   1592 N N    . LEU   A 1 202 ? 6.025   -0.031  9.174   1.00 51.41  ? 202 LEU   A N    1 
ATOM   1593 C CA   . LEU   A 1 202 ? 5.280   -0.508  10.325  1.00 52.97  ? 202 LEU   A CA   1 
ATOM   1594 C C    . LEU   A 1 202 ? 5.245   -2.030  10.364  1.00 55.06  ? 202 LEU   A C    1 
ATOM   1595 O O    . LEU   A 1 202 ? 5.466   -2.634  11.419  1.00 56.08  ? 202 LEU   A O    1 
ATOM   1596 C CB   . LEU   A 1 202 ? 3.866   0.062   10.284  1.00 51.51  ? 202 LEU   A CB   1 
ATOM   1597 C CG   . LEU   A 1 202 ? 3.720   1.519   10.704  1.00 51.43  ? 202 LEU   A CG   1 
ATOM   1598 C CD1  . LEU   A 1 202 ? 2.311   1.993   10.377  1.00 47.38  ? 202 LEU   A CD1  1 
ATOM   1599 C CD2  . LEU   A 1 202 ? 4.061   1.673   12.210  1.00 49.47  ? 202 LEU   A CD2  1 
ATOM   1600 N N    . VAL   A 1 203 ? 4.985   -2.670  9.225   1.00 57.06  ? 203 VAL   A N    1 
ATOM   1601 C CA   . VAL   A 1 203 ? 4.869   -4.128  9.214   1.00 58.52  ? 203 VAL   A CA   1 
ATOM   1602 C C    . VAL   A 1 203 ? 6.244   -4.788  9.244   1.00 60.35  ? 203 VAL   A C    1 
ATOM   1603 O O    . VAL   A 1 203 ? 6.506   -5.681  10.062  1.00 62.08  ? 203 VAL   A O    1 
ATOM   1604 C CB   . VAL   A 1 203 ? 4.060   -4.588  7.989   1.00 57.86  ? 203 VAL   A CB   1 
ATOM   1605 C CG1  . VAL   A 1 203 ? 3.890   -6.112  7.996   1.00 53.35  ? 203 VAL   A CG1  1 
ATOM   1606 C CG2  . VAL   A 1 203 ? 2.717   -3.878  7.955   1.00 58.97  ? 203 VAL   A CG2  1 
ATOM   1607 N N    . LYS   A 1 204 ? 7.141   -4.350  8.357   1.00 75.80  ? 204 LYS   A N    1 
ATOM   1608 C CA   . LYS   A 1 204 ? 8.413   -5.032  8.132   1.00 75.46  ? 204 LYS   A CA   1 
ATOM   1609 C C    . LYS   A 1 204 ? 9.427   -4.759  9.244   1.00 73.59  ? 204 LYS   A C    1 
ATOM   1610 O O    . LYS   A 1 204 ? 10.203  -5.646  9.610   1.00 76.24  ? 204 LYS   A O    1 
ATOM   1611 C CB   . LYS   A 1 204 ? 8.982   -4.613  6.774   1.00 73.49  ? 204 LYS   A CB   1 
ATOM   1612 C CG   . LYS   A 1 204 ? 8.403   -5.382  5.578   1.00 79.68  ? 204 LYS   A CG   1 
ATOM   1613 C CD   . LYS   A 1 204 ? 8.029   -6.809  5.958   1.00 78.01  ? 204 LYS   A CD   1 
ATOM   1614 C CE   . LYS   A 1 204 ? 8.345   -7.794  4.844   1.00 81.28  ? 204 LYS   A CE   1 
ATOM   1615 N NZ   . LYS   A 1 204 ? 8.073   -9.199  5.260   1.00 81.40  ? 204 LYS   A NZ   1 
ATOM   1616 N N    . ASP   A 1 205 ? 9.454   -3.546  9.784   1.00 69.63  ? 205 ASP   A N    1 
ATOM   1617 C CA   . ASP   A 1 205 ? 10.459  -3.198  10.781  1.00 73.96  ? 205 ASP   A CA   1 
ATOM   1618 C C    . ASP   A 1 205 ? 9.927   -3.223  12.205  1.00 73.27  ? 205 ASP   A C    1 
ATOM   1619 O O    . ASP   A 1 205 ? 10.637  -3.654  13.119  1.00 75.13  ? 205 ASP   A O    1 
ATOM   1620 C CB   . ASP   A 1 205 ? 11.041  -1.820  10.478  1.00 74.55  ? 205 ASP   A CB   1 
ATOM   1621 C CG   . ASP   A 1 205 ? 11.957  -1.836  9.278   1.00 76.70  ? 205 ASP   A CG   1 
ATOM   1622 O OD1  . ASP   A 1 205 ? 12.115  -2.919  8.671   1.00 73.56  ? 205 ASP   A OD1  1 
ATOM   1623 O OD2  . ASP   A 1 205 ? 12.519  -0.768  8.948   1.00 77.28  ? 205 ASP   A OD2  1 
ATOM   1624 N N    . PHE   A 1 206 ? 8.692   -2.776  12.411  1.00 67.79  ? 206 PHE   A N    1 
ATOM   1625 C CA   . PHE   A 1 206 ? 8.123   -2.661  13.741  1.00 66.74  ? 206 PHE   A CA   1 
ATOM   1626 C C    . PHE   A 1 206 ? 7.148   -3.787  14.062  1.00 70.60  ? 206 PHE   A C    1 
ATOM   1627 O O    . PHE   A 1 206 ? 6.698   -3.888  15.211  1.00 69.69  ? 206 PHE   A O    1 
ATOM   1628 C CB   . PHE   A 1 206 ? 7.446   -1.292  13.895  1.00 64.93  ? 206 PHE   A CB   1 
ATOM   1629 C CG   . PHE   A 1 206 ? 8.425   -0.157  14.014  1.00 70.01  ? 206 PHE   A CG   1 
ATOM   1630 C CD1  . PHE   A 1 206 ? 9.372   0.065   13.030  1.00 68.73  ? 206 PHE   A CD1  1 
ATOM   1631 C CD2  . PHE   A 1 206 ? 8.430   0.660   15.135  1.00 75.73  ? 206 PHE   A CD2  1 
ATOM   1632 C CE1  . PHE   A 1 206 ? 10.287  1.089   13.142  1.00 70.63  ? 206 PHE   A CE1  1 
ATOM   1633 C CE2  . PHE   A 1 206 ? 9.347   1.693   15.253  1.00 74.26  ? 206 PHE   A CE2  1 
ATOM   1634 C CZ   . PHE   A 1 206 ? 10.277  1.904   14.254  1.00 70.10  ? 206 PHE   A CZ   1 
ATOM   1635 N N    . HIS   A 1 207 ? 6.841   -4.647  13.084  1.00 70.61  ? 207 HIS   A N    1 
ATOM   1636 C CA   . HIS   A 1 207 ? 6.169   -5.924  13.334  1.00 70.26  ? 207 HIS   A CA   1 
ATOM   1637 C C    . HIS   A 1 207 ? 4.818   -5.758  14.022  1.00 70.27  ? 207 HIS   A C    1 
ATOM   1638 O O    . HIS   A 1 207 ? 4.425   -6.587  14.846  1.00 68.12  ? 207 HIS   A O    1 
ATOM   1639 C CB   . HIS   A 1 207 ? 7.058   -6.851  14.167  1.00 72.11  ? 207 HIS   A CB   1 
ATOM   1640 C CG   . HIS   A 1 207 ? 8.425   -7.063  13.596  1.00 76.34  ? 207 HIS   A CG   1 
ATOM   1641 N ND1  . HIS   A 1 207 ? 8.638   -7.721  12.401  1.00 74.67  ? 207 HIS   A ND1  1 
ATOM   1642 C CD2  . HIS   A 1 207 ? 9.651   -6.740  14.073  1.00 75.57  ? 207 HIS   A CD2  1 
ATOM   1643 C CE1  . HIS   A 1 207 ? 9.936   -7.776  12.158  1.00 75.99  ? 207 HIS   A CE1  1 
ATOM   1644 N NE2  . HIS   A 1 207 ? 10.572  -7.187  13.156  1.00 80.39  ? 207 HIS   A NE2  1 
ATOM   1645 N N    . VAL   A 1 208 ? 4.084   -4.695  13.681  1.00 59.16  ? 208 VAL   A N    1 
ATOM   1646 C CA   . VAL   A 1 208 ? 2.784   -4.511  14.312  1.00 61.17  ? 208 VAL   A CA   1 
ATOM   1647 C C    . VAL   A 1 208 ? 1.858   -5.679  13.952  1.00 57.93  ? 208 VAL   A C    1 
ATOM   1648 O O    . VAL   A 1 208 ? 2.015   -6.337  12.915  1.00 59.23  ? 208 VAL   A O    1 
ATOM   1649 C CB   . VAL   A 1 208 ? 2.170   -3.150  13.939  1.00 58.42  ? 208 VAL   A CB   1 
ATOM   1650 C CG1  . VAL   A 1 208 ? 3.192   -2.047  14.160  1.00 57.00  ? 208 VAL   A CG1  1 
ATOM   1651 C CG2  . VAL   A 1 208 ? 1.714   -3.150  12.476  1.00 62.57  ? 208 VAL   A CG2  1 
ATOM   1652 N N    . ASP   A 1 209 ? 0.928   -5.983  14.858  1.00 60.48  ? 209 ASP   A N    1 
ATOM   1653 C CA   . ASP   A 1 209 ? -0.085  -6.997  14.596  1.00 57.93  ? 209 ASP   A CA   1 
ATOM   1654 C C    . ASP   A 1 209 ? -1.286  -6.432  13.851  1.00 58.04  ? 209 ASP   A C    1 
ATOM   1655 O O    . ASP   A 1 209 ? -1.905  -7.150  13.057  1.00 54.88  ? 209 ASP   A O    1 
ATOM   1656 C CB   . ASP   A 1 209 ? -0.582  -7.628  15.904  1.00 60.05  ? 209 ASP   A CB   1 
ATOM   1657 C CG   . ASP   A 1 209 ? 0.559   -8.029  16.872  1.00 64.74  ? 209 ASP   A CG   1 
ATOM   1658 O OD1  . ASP   A 1 209 ? 1.424   -8.866  16.513  1.00 63.91  ? 209 ASP   A OD1  1 
ATOM   1659 O OD2  . ASP   A 1 209 ? 0.572   -7.509  18.022  1.00 66.05  ? 209 ASP   A OD2  1 
ATOM   1660 N N    . THR   A 1 210 ? -1.638  -5.165  14.095  1.00 50.74  ? 210 THR   A N    1 
ATOM   1661 C CA   . THR   A 1 210 ? -2.875  -4.597  13.575  1.00 50.45  ? 210 THR   A CA   1 
ATOM   1662 C C    . THR   A 1 210 ? -2.652  -3.159  13.125  1.00 53.23  ? 210 THR   A C    1 
ATOM   1663 O O    . THR   A 1 210 ? -2.038  -2.362  13.847  1.00 50.15  ? 210 THR   A O    1 
ATOM   1664 C CB   . THR   A 1 210 ? -3.998  -4.644  14.622  1.00 49.11  ? 210 THR   A CB   1 
ATOM   1665 O OG1  . THR   A 1 210 ? -4.283  -6.014  14.947  1.00 50.29  ? 210 THR   A OG1  1 
ATOM   1666 C CG2  . THR   A 1 210 ? -5.263  -3.965  14.095  1.00 47.48  ? 210 THR   A CG2  1 
ATOM   1667 N N    . ILE   A 1 211 ? -3.197  -2.828  11.935  1.00 43.13  ? 211 ILE   A N    1 
ATOM   1668 C CA   . ILE   A 1 211 ? -3.211  -1.471  11.404  1.00 43.33  ? 211 ILE   A CA   1 
ATOM   1669 C C    . ILE   A 1 211 ? -4.587  -0.867  11.659  1.00 44.61  ? 211 ILE   A C    1 
ATOM   1670 O O    . ILE   A 1 211 ? -5.616  -1.541  11.487  1.00 43.70  ? 211 ILE   A O    1 
ATOM   1671 C CB   . ILE   A 1 211 ? -2.871  -1.469  9.891   1.00 46.64  ? 211 ILE   A CB   1 
ATOM   1672 C CG1  . ILE   A 1 211 ? -1.368  -1.677  9.674   1.00 45.34  ? 211 ILE   A CG1  1 
ATOM   1673 C CG2  . ILE   A 1 211 ? -3.363  -0.196  9.205   1.00 44.11  ? 211 ILE   A CG2  1 
ATOM   1674 C CD1  . ILE   A 1 211 ? -0.512  -0.603  10.345  1.00 46.59  ? 211 ILE   A CD1  1 
ATOM   1675 N N    . VAL   A 1 212 ? -4.619  0.388   12.115  1.00 44.69  ? 212 VAL   A N    1 
ATOM   1676 C CA   . VAL   A 1 212 ? -5.850  1.169   12.159  1.00 43.81  ? 212 VAL   A CA   1 
ATOM   1677 C C    . VAL   A 1 212 ? -5.763  2.213   11.056  1.00 44.65  ? 212 VAL   A C    1 
ATOM   1678 O O    . VAL   A 1 212 ? -4.714  2.843   10.870  1.00 45.17  ? 212 VAL   A O    1 
ATOM   1679 C CB   . VAL   A 1 212 ? -6.095  1.829   13.527  1.00 45.91  ? 212 VAL   A CB   1 
ATOM   1680 C CG1  . VAL   A 1 212 ? -6.488  0.759   14.566  1.00 46.86  ? 212 VAL   A CG1  1 
ATOM   1681 C CG2  . VAL   A 1 212 ? -4.878  2.617   13.966  1.00 48.05  ? 212 VAL   A CG2  1 
ATOM   1682 N N    . PHE   A 1 213 ? -6.859  2.388   10.318  1.00 44.28  ? 213 PHE   A N    1 
ATOM   1683 C CA   . PHE   A 1 213 ? -6.805  2.987   8.979   1.00 45.56  ? 213 PHE   A CA   1 
ATOM   1684 C C    . PHE   A 1 213 ? -8.016  3.871   8.729   1.00 44.63  ? 213 PHE   A C    1 
ATOM   1685 O O    . PHE   A 1 213 ? -9.026  3.432   8.162   1.00 43.90  ? 213 PHE   A O    1 
ATOM   1686 C CB   . PHE   A 1 213 ? -6.695  1.887   7.926   1.00 44.07  ? 213 PHE   A CB   1 
ATOM   1687 C CG   . PHE   A 1 213 ? -6.487  2.384   6.527   1.00 46.98  ? 213 PHE   A CG   1 
ATOM   1688 C CD1  . PHE   A 1 213 ? -5.254  2.891   6.128   1.00 48.94  ? 213 PHE   A CD1  1 
ATOM   1689 C CD2  . PHE   A 1 213 ? -7.514  2.304   5.579   1.00 45.08  ? 213 PHE   A CD2  1 
ATOM   1690 C CE1  . PHE   A 1 213 ? -5.063  3.318   4.797   1.00 48.13  ? 213 PHE   A CE1  1 
ATOM   1691 C CE2  . PHE   A 1 213 ? -7.312  2.728   4.288   1.00 46.54  ? 213 PHE   A CE2  1 
ATOM   1692 C CZ   . PHE   A 1 213 ? -6.088  3.235   3.903   1.00 43.35  ? 213 PHE   A CZ   1 
ATOM   1693 N N    . PRO   A 1 214 ? -7.964  5.123   9.177   1.00 40.75  ? 214 PRO   A N    1 
ATOM   1694 C CA   . PRO   A 1 214 ? -8.958  6.102   8.727   1.00 42.20  ? 214 PRO   A CA   1 
ATOM   1695 C C    . PRO   A 1 214 ? -8.708  6.454   7.259   1.00 39.98  ? 214 PRO   A C    1 
ATOM   1696 O O    . PRO   A 1 214 ? -7.564  6.653   6.833   1.00 37.89  ? 214 PRO   A O    1 
ATOM   1697 C CB   . PRO   A 1 214 ? -8.730  7.306   9.651   1.00 40.41  ? 214 PRO   A CB   1 
ATOM   1698 C CG   . PRO   A 1 214 ? -7.738  6.854   10.687  1.00 41.61  ? 214 PRO   A CG   1 
ATOM   1699 C CD   . PRO   A 1 214 ? -6.974  5.721   10.084  1.00 39.89  ? 214 PRO   A CD   1 
ATOM   1700 N N    . THR   A 1 215 ? -9.789  6.511   6.485   1.00 47.17  ? 215 THR   A N    1 
ATOM   1701 C CA   . THR   A 1 215 ? -9.651  6.692   5.049   1.00 51.09  ? 215 THR   A CA   1 
ATOM   1702 C C    . THR   A 1 215 ? -10.838 7.480   4.511   1.00 51.07  ? 215 THR   A C    1 
ATOM   1703 O O    . THR   A 1 215 ? -11.959 7.381   5.031   1.00 50.83  ? 215 THR   A O    1 
ATOM   1704 C CB   . THR   A 1 215 ? -9.521  5.325   4.348   1.00 49.02  ? 215 THR   A CB   1 
ATOM   1705 O OG1  . THR   A 1 215 ? -9.612  5.497   2.933   1.00 50.18  ? 215 THR   A OG1  1 
ATOM   1706 C CG2  . THR   A 1 215 ? -10.609 4.346   4.820   1.00 49.17  ? 215 THR   A CG2  1 
ATOM   1707 N N    . ALA   A 1 216 ? -10.565 8.298   3.473   1.00 43.36  ? 216 ALA   A N    1 
ATOM   1708 C CA   . ALA   A 1 216 ? -11.598 8.926   2.644   1.00 43.62  ? 216 ALA   A CA   1 
ATOM   1709 C C    . ALA   A 1 216 ? -11.275 8.542   1.197   1.00 46.87  ? 216 ALA   A C    1 
ATOM   1710 O O    . ALA   A 1 216 ? -10.853 9.375   0.395   1.00 44.31  ? 216 ALA   A O    1 
ATOM   1711 C CB   . ALA   A 1 216 ? -11.615 10.453  2.835   1.00 42.45  ? 216 ALA   A CB   1 
ATOM   1712 N N    . TRP   A 1 217 ? -11.624 7.315   0.837   1.00 49.91  ? 217 TRP   A N    1 
ATOM   1713 C CA   . TRP   A 1 217 ? -11.125 6.658   -0.359  1.00 48.47  ? 217 TRP   A CA   1 
ATOM   1714 C C    . TRP   A 1 217 ? -12.187 6.719   -1.439  1.00 47.05  ? 217 TRP   A C    1 
ATOM   1715 O O    . TRP   A 1 217 ? -13.343 6.361   -1.190  1.00 47.77  ? 217 TRP   A O    1 
ATOM   1716 C CB   . TRP   A 1 217 ? -10.785 5.206   -0.044  1.00 45.34  ? 217 TRP   A CB   1 
ATOM   1717 C CG   . TRP   A 1 217 ? -10.121 4.449   -1.111  1.00 49.76  ? 217 TRP   A CG   1 
ATOM   1718 C CD1  . TRP   A 1 217 ? -10.704 3.890   -2.228  1.00 48.89  ? 217 TRP   A CD1  1 
ATOM   1719 C CD2  . TRP   A 1 217 ? -8.733  4.121   -1.177  1.00 50.71  ? 217 TRP   A CD2  1 
ATOM   1720 N NE1  . TRP   A 1 217 ? -9.759  3.231   -2.968  1.00 47.57  ? 217 TRP   A NE1  1 
ATOM   1721 C CE2  . TRP   A 1 217 ? -8.539  3.360   -2.359  1.00 46.19  ? 217 TRP   A CE2  1 
ATOM   1722 C CE3  . TRP   A 1 217 ? -7.631  4.400   -0.355  1.00 48.49  ? 217 TRP   A CE3  1 
ATOM   1723 C CZ2  . TRP   A 1 217 ? -7.294  2.858   -2.730  1.00 45.63  ? 217 TRP   A CZ2  1 
ATOM   1724 C CZ3  . TRP   A 1 217 ? -6.392  3.910   -0.723  1.00 48.73  ? 217 TRP   A CZ3  1 
ATOM   1725 C CH2  . TRP   A 1 217 ? -6.234  3.140   -1.915  1.00 47.71  ? 217 TRP   A CH2  1 
ATOM   1726 N N    . MET   A 1 218 ? -11.785 7.154   -2.634  1.00 49.87  ? 218 MET   A N    1 
ATOM   1727 C CA   . MET   A 1 218 ? -12.648 7.201   -3.816  1.00 50.91  ? 218 MET   A CA   1 
ATOM   1728 C C    . MET   A 1 218 ? -12.326 5.981   -4.676  1.00 48.37  ? 218 MET   A C    1 
ATOM   1729 O O    . MET   A 1 218 ? -11.199 5.828   -5.160  1.00 49.48  ? 218 MET   A O    1 
ATOM   1730 C CB   . MET   A 1 218 ? -12.451 8.497   -4.601  1.00 49.62  ? 218 MET   A CB   1 
ATOM   1731 C CG   . MET   A 1 218 ? -12.879 9.742   -3.843  1.00 51.74  ? 218 MET   A CG   1 
ATOM   1732 S SD   . MET   A 1 218 ? -12.490 11.266  -4.710  1.00 59.05  ? 218 MET   A SD   1 
ATOM   1733 C CE   . MET   A 1 218 ? -10.712 11.229  -4.538  1.00 57.64  ? 218 MET   A CE   1 
ATOM   1734 N N    . ASN   A 1 219 ? -13.291 5.078   -4.795  1.00 46.98  ? 219 ASN   A N    1 
ATOM   1735 C CA   . ASN   A 1 219 ? -13.057 3.809   -5.473  1.00 45.76  ? 219 ASN   A CA   1 
ATOM   1736 C C    . ASN   A 1 219 ? -12.710 3.993   -6.945  1.00 49.60  ? 219 ASN   A C    1 
ATOM   1737 O O    . ASN   A 1 219 ? -13.398 4.703   -7.695  1.00 49.42  ? 219 ASN   A O    1 
ATOM   1738 C CB   . ASN   A 1 219 ? -14.283 2.928   -5.311  1.00 46.19  ? 219 ASN   A CB   1 
ATOM   1739 C CG   . ASN   A 1 219 ? -14.625 2.720   -3.856  1.00 46.87  ? 219 ASN   A CG   1 
ATOM   1740 O OD1  . ASN   A 1 219 ? -13.728 2.529   -3.038  1.00 48.00  ? 219 ASN   A OD1  1 
ATOM   1741 N ND2  . ASN   A 1 219 ? -15.905 2.766   -3.516  1.00 46.62  ? 219 ASN   A ND2  1 
ATOM   1742 N N    . VAL   A 1 220 ? -11.664 3.297   -7.371  1.00 49.19  ? 220 VAL   A N    1 
ATOM   1743 C CA   . VAL   A 1 220 ? -11.220 3.305   -8.751  1.00 51.21  ? 220 VAL   A CA   1 
ATOM   1744 C C    . VAL   A 1 220 ? -11.140 1.839   -9.163  1.00 52.60  ? 220 VAL   A C    1 
ATOM   1745 O O    . VAL   A 1 220 ? -10.178 1.134   -8.834  1.00 49.05  ? 220 VAL   A O    1 
ATOM   1746 C CB   . VAL   A 1 220 ? -9.881  4.024   -8.925  1.00 52.47  ? 220 VAL   A CB   1 
ATOM   1747 C CG1  . VAL   A 1 220 ? -9.498  4.098   -10.407 1.00 51.98  ? 220 VAL   A CG1  1 
ATOM   1748 C CG2  . VAL   A 1 220 ? -9.963  5.407   -8.304  1.00 50.70  ? 220 VAL   A CG2  1 
ATOM   1749 N N    . LEU   A 1 221 ? -12.180 1.360   -9.833  1.00 57.08  ? 221 LEU   A N    1 
ATOM   1750 C CA   . LEU   A 1 221 ? -12.162 0.006   -10.345 1.00 57.82  ? 221 LEU   A CA   1 
ATOM   1751 C C    . LEU   A 1 221 ? -11.214 -0.079  -11.538 1.00 53.26  ? 221 LEU   A C    1 
ATOM   1752 O O    . LEU   A 1 221 ? -10.927 0.927   -12.186 1.00 58.48  ? 221 LEU   A O    1 
ATOM   1753 C CB   . LEU   A 1 221 ? -13.574 -0.436  -10.715 1.00 54.71  ? 221 LEU   A CB   1 
ATOM   1754 C CG   . LEU   A 1 221 ? -14.338 -0.963  -9.494  1.00 57.21  ? 221 LEU   A CG   1 
ATOM   1755 C CD1  . LEU   A 1 221 ? -15.838 -1.096  -9.757  1.00 60.56  ? 221 LEU   A CD1  1 
ATOM   1756 C CD2  . LEU   A 1 221 ? -13.751 -2.289  -9.025  1.00 52.94  ? 221 LEU   A CD2  1 
ATOM   1757 N N    . PRO   A 1 222 ? -10.734 -1.275  -11.865 1.00 46.34  ? 222 PRO   A N    1 
ATOM   1758 C CA   . PRO   A 1 222 ? -11.074 -2.566  -11.254 1.00 46.39  ? 222 PRO   A CA   1 
ATOM   1759 C C    . PRO   A 1 222 ? -10.179 -3.039  -10.102 1.00 45.45  ? 222 PRO   A C    1 
ATOM   1760 O O    . PRO   A 1 222 ? -10.499 -4.058  -9.484  1.00 45.62  ? 222 PRO   A O    1 
ATOM   1761 C CB   . PRO   A 1 222 ? -10.990 -3.519  -12.445 1.00 47.67  ? 222 PRO   A CB   1 
ATOM   1762 C CG   . PRO   A 1 222 ? -9.875  -2.945  -13.283 1.00 47.78  ? 222 PRO   A CG   1 
ATOM   1763 C CD   . PRO   A 1 222 ? -10.056 -1.456  -13.175 1.00 47.26  ? 222 PRO   A CD   1 
ATOM   1764 N N    . HIS   A 1 223 ? -9.095  -2.319  -9.776  1.00 55.71  ? 223 HIS   A N    1 
ATOM   1765 C CA   . HIS   A 1 223 ? -8.122  -2.779  -8.797  1.00 55.88  ? 223 HIS   A CA   1 
ATOM   1766 C C    . HIS   A 1 223 ? -8.114  -1.974  -7.502  1.00 58.26  ? 223 HIS   A C    1 
ATOM   1767 O O    . HIS   A 1 223 ? -7.602  -2.468  -6.492  1.00 57.33  ? 223 HIS   A O    1 
ATOM   1768 C CB   . HIS   A 1 223 ? -6.705  -2.736  -9.383  1.00 54.72  ? 223 HIS   A CB   1 
ATOM   1769 C CG   . HIS   A 1 223 ? -6.548  -3.522  -10.646 1.00 59.46  ? 223 HIS   A CG   1 
ATOM   1770 N ND1  . HIS   A 1 223 ? -5.765  -3.092  -11.699 1.00 59.39  ? 223 HIS   A ND1  1 
ATOM   1771 C CD2  . HIS   A 1 223 ? -7.073  -4.713  -11.026 1.00 61.36  ? 223 HIS   A CD2  1 
ATOM   1772 C CE1  . HIS   A 1 223 ? -5.812  -3.986  -12.670 1.00 62.79  ? 223 HIS   A CE1  1 
ATOM   1773 N NE2  . HIS   A 1 223 ? -6.602  -4.976  -12.290 1.00 62.73  ? 223 HIS   A NE2  1 
ATOM   1774 N N    . LEU   A 1 224 ? -8.672  -0.766  -7.493  1.00 50.14  ? 224 LEU   A N    1 
ATOM   1775 C CA   . LEU   A 1 224 ? -8.550  0.122   -6.341  1.00 47.21  ? 224 LEU   A CA   1 
ATOM   1776 C C    . LEU   A 1 224 ? -9.923  0.520   -5.804  1.00 45.58  ? 224 LEU   A C    1 
ATOM   1777 O O    . LEU   A 1 224 ? -10.176 1.679   -5.468  1.00 44.78  ? 224 LEU   A O    1 
ATOM   1778 C CB   . LEU   A 1 224 ? -7.711  1.347   -6.703  1.00 47.11  ? 224 LEU   A CB   1 
ATOM   1779 C CG   . LEU   A 1 224 ? -6.299  0.984   -7.185  1.00 48.31  ? 224 LEU   A CG   1 
ATOM   1780 C CD1  . LEU   A 1 224 ? -5.532  2.183   -7.736  1.00 46.94  ? 224 LEU   A CD1  1 
ATOM   1781 C CD2  . LEU   A 1 224 ? -5.518  0.322   -6.035  1.00 49.54  ? 224 LEU   A CD2  1 
ATOM   1782 N N    . SER   A 1 225 ? -10.830 -0.446  -5.722  1.00 46.54  ? 225 SER   A N    1 
ATOM   1783 C CA   . SER   A 1 225 ? -11.997 -0.282  -4.872  1.00 49.35  ? 225 SER   A CA   1 
ATOM   1784 C C    . SER   A 1 225 ? -11.561 -0.400  -3.407  1.00 47.58  ? 225 SER   A C    1 
ATOM   1785 O O    . SER   A 1 225 ? -10.628 -1.140  -3.080  1.00 47.93  ? 225 SER   A O    1 
ATOM   1786 C CB   . SER   A 1 225 ? -13.047 -1.337  -5.207  1.00 49.23  ? 225 SER   A CB   1 
ATOM   1787 O OG   . SER   A 1 225 ? -14.264 -1.055  -4.543  1.00 50.93  ? 225 SER   A OG   1 
ATOM   1788 N N    . ALA   A 1 226 ? -12.202 0.363   -2.524  1.00 47.54  ? 226 ALA   A N    1 
ATOM   1789 C CA   . ALA   A 1 226 ? -11.707 0.446   -1.148  1.00 48.88  ? 226 ALA   A CA   1 
ATOM   1790 C C    . ALA   A 1 226 ? -11.570 -0.937  -0.510  1.00 49.58  ? 226 ALA   A C    1 
ATOM   1791 O O    . ALA   A 1 226 ? -10.466 -1.366  -0.150  1.00 47.76  ? 226 ALA   A O    1 
ATOM   1792 C CB   . ALA   A 1 226 ? -12.626 1.332   -0.310  1.00 48.25  ? 226 ALA   A CB   1 
ATOM   1793 N N    . VAL   A 1 227 ? -12.690 -1.655  -0.365  1.00 55.66  ? 227 VAL   A N    1 
ATOM   1794 C CA   . VAL   A 1 227 ? -12.664 -2.950  0.317   1.00 55.59  ? 227 VAL   A CA   1 
ATOM   1795 C C    . VAL   A 1 227 ? -11.706 -3.902  -0.382  1.00 57.95  ? 227 VAL   A C    1 
ATOM   1796 O O    . VAL   A 1 227 ? -10.938 -4.629  0.269   1.00 56.64  ? 227 VAL   A O    1 
ATOM   1797 C CB   . VAL   A 1 227 ? -14.082 -3.542  0.409   1.00 55.39  ? 227 VAL   A CB   1 
ATOM   1798 C CG1  . VAL   A 1 227 ? -14.978 -2.631  1.233   1.00 60.41  ? 227 VAL   A CG1  1 
ATOM   1799 C CG2  . VAL   A 1 227 ? -14.676 -3.761  -0.965  1.00 59.15  ? 227 VAL   A CG2  1 
ATOM   1800 N N    . GLU   A 1 228 ? -11.735 -3.908  -1.719  1.00 44.99  ? 228 GLU   A N    1 
ATOM   1801 C CA   . GLU   A 1 228 ? -10.918 -4.830  -2.495  1.00 47.91  ? 228 GLU   A CA   1 
ATOM   1802 C C    . GLU   A 1 228 ? -9.435  -4.639  -2.190  1.00 45.52  ? 228 GLU   A C    1 
ATOM   1803 O O    . GLU   A 1 228 ? -8.733  -5.583  -1.795  1.00 47.97  ? 228 GLU   A O    1 
ATOM   1804 C CB   . GLU   A 1 228 ? -11.224 -4.639  -3.993  1.00 46.23  ? 228 GLU   A CB   1 
ATOM   1805 C CG   . GLU   A 1 228 ? -10.197 -5.138  -4.929  1.00 47.08  ? 228 GLU   A CG   1 
ATOM   1806 C CD   . GLU   A 1 228 ? -10.376 -4.544  -6.335  1.00 50.72  ? 228 GLU   A CD   1 
ATOM   1807 O OE1  . GLU   A 1 228 ? -10.559 -3.300  -6.459  1.00 48.51  ? 228 GLU   A OE1  1 
ATOM   1808 O OE2  . GLU   A 1 228 ? -10.359 -5.337  -7.307  1.00 49.84  ? 228 GLU   A OE2  1 
ATOM   1809 N N    . PHE   A 1 229 ? -8.939  -3.416  -2.354  1.00 48.62  ? 229 PHE   A N    1 
ATOM   1810 C CA   . PHE   A 1 229 ? -7.508  -3.212  -2.167  1.00 50.44  ? 229 PHE   A CA   1 
ATOM   1811 C C    . PHE   A 1 229 ? -7.102  -3.222  -0.693  1.00 49.06  ? 229 PHE   A C    1 
ATOM   1812 O O    . PHE   A 1 229 ? -6.015  -3.710  -0.376  1.00 49.68  ? 229 PHE   A O    1 
ATOM   1813 C CB   . PHE   A 1 229 ? -7.028  -1.920  -2.851  1.00 49.53  ? 229 PHE   A CB   1 
ATOM   1814 C CG   . PHE   A 1 229 ? -5.534  -1.751  -2.781  1.00 51.11  ? 229 PHE   A CG   1 
ATOM   1815 C CD1  . PHE   A 1 229 ? -4.694  -2.600  -3.488  1.00 50.33  ? 229 PHE   A CD1  1 
ATOM   1816 C CD2  . PHE   A 1 229 ? -4.964  -0.802  -1.931  1.00 53.90  ? 229 PHE   A CD2  1 
ATOM   1817 C CE1  . PHE   A 1 229 ? -3.316  -2.475  -3.389  1.00 53.98  ? 229 PHE   A CE1  1 
ATOM   1818 C CE2  . PHE   A 1 229 ? -3.587  -0.673  -1.828  1.00 53.02  ? 229 PHE   A CE2  1 
ATOM   1819 C CZ   . PHE   A 1 229 ? -2.764  -1.506  -2.558  1.00 54.60  ? 229 PHE   A CZ   1 
ATOM   1820 N N    . HIS   A 1 230 ? -7.937  -2.723  0.224   1.00 47.46  ? 230 HIS   A N    1 
ATOM   1821 C CA   . HIS   A 1 230 ? -7.526  -2.737  1.641   1.00 48.34  ? 230 HIS   A CA   1 
ATOM   1822 C C    . HIS   A 1 230 ? -7.435  -4.158  2.178   1.00 45.50  ? 230 HIS   A C    1 
ATOM   1823 O O    . HIS   A 1 230 ? -6.411  -4.538  2.757   1.00 47.27  ? 230 HIS   A O    1 
ATOM   1824 C CB   . HIS   A 1 230 ? -8.470  -1.886  2.502   1.00 44.54  ? 230 HIS   A CB   1 
ATOM   1825 C CG   . HIS   A 1 230 ? -8.588  -0.474  2.020   1.00 46.35  ? 230 HIS   A CG   1 
ATOM   1826 N ND1  . HIS   A 1 230 ? -9.646  0.346   2.346   1.00 43.96  ? 230 HIS   A ND1  1 
ATOM   1827 C CD2  . HIS   A 1 230 ? -7.808  0.234   1.164   1.00 46.70  ? 230 HIS   A CD2  1 
ATOM   1828 C CE1  . HIS   A 1 230 ? -9.489  1.515   1.746   1.00 46.47  ? 230 HIS   A CE1  1 
ATOM   1829 N NE2  . HIS   A 1 230 ? -8.387  1.470   1.016   1.00 46.41  ? 230 HIS   A NE2  1 
ATOM   1830 N N    . SER   A 1 231 ? -8.474  -4.978  1.970   1.00 46.49  ? 231 SER   A N    1 
ATOM   1831 C CA   . SER   A 1 231 ? -8.369  -6.374  2.398   1.00 46.61  ? 231 SER   A CA   1 
ATOM   1832 C C    . SER   A 1 231 ? -7.221  -7.093  1.677   1.00 49.17  ? 231 SER   A C    1 
ATOM   1833 O O    . SER   A 1 231 ? -6.506  -7.898  2.290   1.00 48.14  ? 231 SER   A O    1 
ATOM   1834 C CB   . SER   A 1 231 ? -9.701  -7.098  2.179   1.00 47.62  ? 231 SER   A CB   1 
ATOM   1835 O OG   . SER   A 1 231 ? -9.927  -7.378  0.794   1.00 50.43  ? 231 SER   A OG   1 
ATOM   1836 N N    . ALA   A 1 232 ? -7.019  -6.829  0.366   1.00 49.14  ? 232 ALA   A N    1 
ATOM   1837 C CA   . ALA   A 1 232 ? -5.872  -7.449  -0.303  1.00 48.55  ? 232 ALA   A CA   1 
ATOM   1838 C C    . ALA   A 1 232 ? -4.556  -7.058  0.376   1.00 47.11  ? 232 ALA   A C    1 
ATOM   1839 O O    . ALA   A 1 232 ? -3.659  -7.897  0.542   1.00 47.59  ? 232 ALA   A O    1 
ATOM   1840 C CB   . ALA   A 1 232 ? -5.842  -7.071  -1.793  1.00 47.49  ? 232 ALA   A CB   1 
ATOM   1841 N N    . TRP   A 1 233 ? -4.416  -5.784  0.754   1.00 47.11  ? 233 TRP   A N    1 
ATOM   1842 C CA   . TRP   A 1 233 ? -3.198  -5.323  1.419   1.00 51.10  ? 233 TRP   A CA   1 
ATOM   1843 C C    . TRP   A 1 233 ? -3.005  -6.006  2.775   1.00 49.99  ? 233 TRP   A C    1 
ATOM   1844 O O    . TRP   A 1 233 ? -1.902  -6.454  3.109   1.00 49.20  ? 233 TRP   A O    1 
ATOM   1845 C CB   . TRP   A 1 233 ? -3.247  -3.801  1.584   1.00 48.92  ? 233 TRP   A CB   1 
ATOM   1846 C CG   . TRP   A 1 233 ? -1.911  -3.156  1.844   1.00 51.46  ? 233 TRP   A CG   1 
ATOM   1847 C CD1  . TRP   A 1 233 ? -1.068  -2.610  0.923   1.00 52.65  ? 233 TRP   A CD1  1 
ATOM   1848 C CD2  . TRP   A 1 233 ? -1.271  -2.989  3.118   1.00 52.84  ? 233 TRP   A CD2  1 
ATOM   1849 N NE1  . TRP   A 1 233 ? 0.056   -2.104  1.542   1.00 50.78  ? 233 TRP   A NE1  1 
ATOM   1850 C CE2  . TRP   A 1 233 ? -0.045  -2.325  2.888   1.00 51.52  ? 233 TRP   A CE2  1 
ATOM   1851 C CE3  . TRP   A 1 233 ? -1.615  -3.332  4.425   1.00 49.31  ? 233 TRP   A CE3  1 
ATOM   1852 C CZ2  . TRP   A 1 233 ? 0.836   -2.002  3.917   1.00 50.92  ? 233 TRP   A CZ2  1 
ATOM   1853 C CZ3  . TRP   A 1 233 ? -0.738  -3.009  5.445   1.00 52.45  ? 233 TRP   A CZ3  1 
ATOM   1854 C CH2  . TRP   A 1 233 ? 0.474   -2.352  5.185   1.00 52.45  ? 233 TRP   A CH2  1 
ATOM   1855 N N    . ALA   A 1 234 ? -4.070  -6.097  3.568   1.00 55.89  ? 234 ALA   A N    1 
ATOM   1856 C CA   . ALA   A 1 234 ? -3.959  -6.781  4.859   1.00 56.23  ? 234 ALA   A CA   1 
ATOM   1857 C C    . ALA   A 1 234 ? -3.547  -8.233  4.667   1.00 59.21  ? 234 ALA   A C    1 
ATOM   1858 O O    . ALA   A 1 234 ? -2.801  -8.791  5.484   1.00 58.53  ? 234 ALA   A O    1 
ATOM   1859 C CB   . ALA   A 1 234 ? -5.271  -6.696  5.644   1.00 53.33  ? 234 ALA   A CB   1 
ATOM   1860 N N    . MET   A 1 235 ? -4.041  -8.869  3.597   1.00 57.38  ? 235 MET   A N    1 
ATOM   1861 C CA   . MET   A 1 235 ? -3.694  -10.264 3.356   1.00 56.95  ? 235 MET   A CA   1 
ATOM   1862 C C    . MET   A 1 235 ? -2.230  -10.407 2.966   1.00 58.01  ? 235 MET   A C    1 
ATOM   1863 O O    . MET   A 1 235 ? -1.540  -11.320 3.431   1.00 56.28  ? 235 MET   A O    1 
ATOM   1864 C CB   . MET   A 1 235 ? -4.594  -10.843 2.269   1.00 57.09  ? 235 MET   A CB   1 
ATOM   1865 C CG   . MET   A 1 235 ? -4.542  -12.346 2.205   1.00 59.37  ? 235 MET   A CG   1 
ATOM   1866 S SD   . MET   A 1 235 ? -5.815  -13.010 1.123   1.00 64.56  ? 235 MET   A SD   1 
ATOM   1867 C CE   . MET   A 1 235 ? -7.274  -12.855 2.167   1.00 58.65  ? 235 MET   A CE   1 
ATOM   1868 N N    . GLY   A 1 236 ? -1.755  -9.533  2.080   1.00 55.09  ? 236 GLY   A N    1 
ATOM   1869 C CA   . GLY   A 1 236 ? -0.374  -9.617  1.638   1.00 52.19  ? 236 GLY   A CA   1 
ATOM   1870 C C    . GLY   A 1 236 ? 0.628   -9.261  2.718   1.00 52.21  ? 236 GLY   A C    1 
ATOM   1871 O O    . GLY   A 1 236 ? 1.670   -9.911  2.843   1.00 52.67  ? 236 GLY   A O    1 
ATOM   1872 N N    . MET   A 1 237 ? 0.340   -8.213  3.501   1.00 57.49  ? 237 MET   A N    1 
ATOM   1873 C CA   . MET   A 1 237 ? 1.233   -7.780  4.575   1.00 57.91  ? 237 MET   A CA   1 
ATOM   1874 C C    . MET   A 1 237 ? 1.121   -8.643  5.823   1.00 58.34  ? 237 MET   A C    1 
ATOM   1875 O O    . MET   A 1 237 ? 2.056   -8.666  6.625   1.00 57.18  ? 237 MET   A O    1 
ATOM   1876 C CB   . MET   A 1 237 ? 0.961   -6.318  4.932   1.00 61.95  ? 237 MET   A CB   1 
ATOM   1877 C CG   . MET   A 1 237 ? 1.342   -5.317  3.818   1.00 57.88  ? 237 MET   A CG   1 
ATOM   1878 S SD   . MET   A 1 237 ? 2.980   -5.649  3.120   1.00 58.40  ? 237 MET   A SD   1 
ATOM   1879 C CE   . MET   A 1 237 ? 4.076   -5.156  4.465   1.00 60.26  ? 237 MET   A CE   1 
ATOM   1880 N N    . ARG   A 1 238 ? 0.040   -9.412  5.948   1.00 67.35  ? 238 ARG   A N    1 
ATOM   1881 C CA   . ARG   A 1 238 ? -0.165  -10.343 7.054   1.00 66.18  ? 238 ARG   A CA   1 
ATOM   1882 C C    . ARG   A 1 238 ? -0.415  -9.620  8.385   1.00 70.25  ? 238 ARG   A C    1 
ATOM   1883 O O    . ARG   A 1 238 ? 0.198   -9.929  9.410   1.00 72.77  ? 238 ARG   A O    1 
ATOM   1884 C CB   . ARG   A 1 238 ? 1.021   -11.297 7.180   1.00 69.56  ? 238 ARG   A CB   1 
ATOM   1885 C CG   . ARG   A 1 238 ? 0.995   -12.491 6.264   1.00 69.76  ? 238 ARG   A CG   1 
ATOM   1886 C CD   . ARG   A 1 238 ? 2.337   -12.627 5.590   1.00 71.94  ? 238 ARG   A CD   1 
ATOM   1887 N NE   . ARG   A 1 238 ? 2.720   -14.019 5.390   1.00 80.12  ? 238 ARG   A NE   1 
ATOM   1888 C CZ   . ARG   A 1 238 ? 2.295   -14.778 4.388   1.00 85.80  ? 238 ARG   A CZ   1 
ATOM   1889 N NH1  . ARG   A 1 238 ? 1.571   -14.275 3.397   1.00 87.95  ? 238 ARG   A NH1  1 
ATOM   1890 N NH2  . ARG   A 1 238 ? 2.664   -16.056 4.340   1.00 82.57  ? 238 ARG   A NH2  1 
ATOM   1891 N N    . VAL   A 1 239 ? -1.350  -8.669  8.371   1.00 59.92  ? 239 VAL   A N    1 
ATOM   1892 C CA   . VAL   A 1 239 ? -1.792  -8.000  9.587   1.00 57.10  ? 239 VAL   A CA   1 
ATOM   1893 C C    . VAL   A 1 239 ? -3.313  -7.897  9.575   1.00 56.78  ? 239 VAL   A C    1 
ATOM   1894 O O    . VAL   A 1 239 ? -3.956  -7.935  8.520   1.00 56.63  ? 239 VAL   A O    1 
ATOM   1895 C CB   . VAL   A 1 239 ? -1.161  -6.592  9.724   1.00 55.40  ? 239 VAL   A CB   1 
ATOM   1896 C CG1  . VAL   A 1 239 ? 0.359   -6.678  9.652   1.00 54.27  ? 239 VAL   A CG1  1 
ATOM   1897 C CG2  . VAL   A 1 239 ? -1.695  -5.665  8.637   1.00 52.72  ? 239 VAL   A CG2  1 
ATOM   1898 N N    . ASN   A 1 240 ? -3.887  -7.772  10.769  1.00 54.35  ? 240 ASN   A N    1 
ATOM   1899 C CA   . ASN   A 1 240 ? -5.253  -7.283  10.892  1.00 54.83  ? 240 ASN   A CA   1 
ATOM   1900 C C    . ASN   A 1 240 ? -5.312  -5.843  10.384  1.00 54.17  ? 240 ASN   A C    1 
ATOM   1901 O O    . ASN   A 1 240 ? -4.305  -5.126  10.347  1.00 52.59  ? 240 ASN   A O    1 
ATOM   1902 C CB   . ASN   A 1 240 ? -5.743  -7.296  12.343  1.00 53.37  ? 240 ASN   A CB   1 
ATOM   1903 C CG   . ASN   A 1 240 ? -5.638  -8.656  13.009  1.00 57.50  ? 240 ASN   A CG   1 
ATOM   1904 O OD1  . ASN   A 1 240 ? -5.705  -9.699  12.365  1.00 59.94  ? 240 ASN   A OD1  1 
ATOM   1905 N ND2  . ASN   A 1 240 ? -5.501  -8.644  14.331  1.00 57.10  ? 240 ASN   A ND2  1 
ATOM   1906 N N    . PHE   A 1 241 ? -6.517  -5.407  10.024  1.00 46.30  ? 241 PHE   A N    1 
ATOM   1907 C CA   . PHE   A 1 241 ? -6.692  -4.126  9.352   1.00 45.24  ? 241 PHE   A CA   1 
ATOM   1908 C C    . PHE   A 1 241 ? -8.086  -3.600  9.647   1.00 46.53  ? 241 PHE   A C    1 
ATOM   1909 O O    . PHE   A 1 241 ? -9.079  -4.255  9.307   1.00 48.97  ? 241 PHE   A O    1 
ATOM   1910 C CB   . PHE   A 1 241 ? -6.491  -4.289  7.832   1.00 48.33  ? 241 PHE   A CB   1 
ATOM   1911 C CG   . PHE   A 1 241 ? -6.080  -3.037  7.136   1.00 43.59  ? 241 PHE   A CG   1 
ATOM   1912 C CD1  . PHE   A 1 241 ? -7.032  -2.148  6.655   1.00 44.60  ? 241 PHE   A CD1  1 
ATOM   1913 C CD2  . PHE   A 1 241 ? -4.744  -2.741  6.961   1.00 43.98  ? 241 PHE   A CD2  1 
ATOM   1914 C CE1  . PHE   A 1 241 ? -6.655  -0.984  6.002   1.00 43.41  ? 241 PHE   A CE1  1 
ATOM   1915 C CE2  . PHE   A 1 241 ? -4.357  -1.576  6.334   1.00 46.34  ? 241 PHE   A CE2  1 
ATOM   1916 C CZ   . PHE   A 1 241 ? -5.320  -0.696  5.842   1.00 44.88  ? 241 PHE   A CZ   1 
ATOM   1917 N N    . LEU   A 1 242 ? -8.169  -2.393  10.196  1.00 46.46  ? 242 LEU   A N    1 
ATOM   1918 C CA   . LEU   A 1 242 ? -9.447  -1.764  10.520  1.00 47.21  ? 242 LEU   A CA   1 
ATOM   1919 C C    . LEU   A 1 242 ? -9.578  -0.532  9.625   1.00 46.13  ? 242 LEU   A C    1 
ATOM   1920 O O    . LEU   A 1 242 ? -8.962  0.505   9.900   1.00 45.12  ? 242 LEU   A O    1 
ATOM   1921 C CB   . LEU   A 1 242 ? -9.526  -1.406  12.007  1.00 47.13  ? 242 LEU   A CB   1 
ATOM   1922 C CG   . LEU   A 1 242 ? -9.823  -2.558  12.984  1.00 48.37  ? 242 LEU   A CG   1 
ATOM   1923 C CD1  . LEU   A 1 242 ? -8.891  -3.739  12.760  1.00 46.57  ? 242 LEU   A CD1  1 
ATOM   1924 C CD2  . LEU   A 1 242 ? -9.743  -2.104  14.449  1.00 46.94  ? 242 LEU   A CD2  1 
ATOM   1925 N N    . ALA   A 1 243 ? -10.345 -0.669  8.537   1.00 44.08  ? 243 ALA   A N    1 
ATOM   1926 C CA   . ALA   A 1 243 ? -10.541 0.386   7.546   1.00 46.15  ? 243 ALA   A CA   1 
ATOM   1927 C C    . ALA   A 1 243 ? -11.867 1.080   7.819   1.00 45.73  ? 243 ALA   A C    1 
ATOM   1928 O O    . ALA   A 1 243 ? -12.929 0.450   7.759   1.00 45.92  ? 243 ALA   A O    1 
ATOM   1929 C CB   . ALA   A 1 243 ? -10.523 -0.174  6.119   1.00 44.05  ? 243 ALA   A CB   1 
ATOM   1930 N N    . SER   A 1 244 ? -11.797 2.378   8.094   1.00 44.80  ? 244 SER   A N    1 
ATOM   1931 C CA   . SER   A 1 244 ? -12.962 3.201   8.391   1.00 44.88  ? 244 SER   A CA   1 
ATOM   1932 C C    . SER   A 1 244 ? -13.063 4.274   7.307   1.00 46.44  ? 244 SER   A C    1 
ATOM   1933 O O    . SER   A 1 244 ? -12.187 5.141   7.200   1.00 45.04  ? 244 SER   A O    1 
ATOM   1934 C CB   . SER   A 1 244 ? -12.832 3.810   9.779   1.00 43.91  ? 244 SER   A CB   1 
ATOM   1935 O OG   . SER   A 1 244 ? -13.827 4.783   10.000  1.00 45.93  ? 244 SER   A OG   1 
ATOM   1936 N N    . ASN   A 1 245 ? -14.098 4.186   6.473   1.00 50.90  ? 245 ASN   A N    1 
ATOM   1937 C CA   . ASN   A 1 245 ? -14.199 4.987   5.265   1.00 53.70  ? 245 ASN   A CA   1 
ATOM   1938 C C    . ASN   A 1 245 ? -15.346 5.982   5.372   1.00 55.08  ? 245 ASN   A C    1 
ATOM   1939 O O    . ASN   A 1 245 ? -16.381 5.698   5.984   1.00 55.66  ? 245 ASN   A O    1 
ATOM   1940 C CB   . ASN   A 1 245 ? -14.410 4.087   4.035   1.00 54.79  ? 245 ASN   A CB   1 
ATOM   1941 C CG   . ASN   A 1 245 ? -13.901 4.703   2.743   1.00 54.09  ? 245 ASN   A CG   1 
ATOM   1942 O OD1  . ASN   A 1 245 ? -12.803 5.249   2.662   1.00 56.06  ? 245 ASN   A OD1  1 
ATOM   1943 N ND2  . ASN   A 1 245 ? -14.714 4.616   1.723   1.00 58.98  ? 245 ASN   A ND2  1 
ATOM   1944 N N    . ILE   A 1 246 ? -15.165 7.132   4.714   1.00 44.41  ? 246 ILE   A N    1 
ATOM   1945 C CA   . ILE   A 1 246 ? -16.247 8.090   4.533   1.00 44.28  ? 246 ILE   A CA   1 
ATOM   1946 C C    . ILE   A 1 246 ? -17.344 7.459   3.679   1.00 44.71  ? 246 ILE   A C    1 
ATOM   1947 O O    . ILE   A 1 246 ? -17.084 6.616   2.806   1.00 42.13  ? 246 ILE   A O    1 
ATOM   1948 C CB   . ILE   A 1 246 ? -15.708 9.381   3.879   1.00 46.70  ? 246 ILE   A CB   1 
ATOM   1949 C CG1  . ILE   A 1 246 ? -14.936 10.242  4.906   1.00 46.76  ? 246 ILE   A CG1  1 
ATOM   1950 C CG2  . ILE   A 1 246 ? -16.832 10.177  3.204   1.00 44.27  ? 246 ILE   A CG2  1 
ATOM   1951 C CD1  . ILE   A 1 246 ? -15.807 10.818  6.040   1.00 45.63  ? 246 ILE   A CD1  1 
ATOM   1952 N N    . HIS   A 1 247 ? -18.589 7.854   3.938   1.00 51.60  ? 247 HIS   A N    1 
ATOM   1953 C CA   . HIS   A 1 247 ? -19.720 7.454   3.103   1.00 52.67  ? 247 HIS   A CA   1 
ATOM   1954 C C    . HIS   A 1 247 ? -20.173 8.670   2.300   1.00 57.19  ? 247 HIS   A C    1 
ATOM   1955 O O    . HIS   A 1 247 ? -20.755 9.612   2.857   1.00 56.19  ? 247 HIS   A O    1 
ATOM   1956 C CB   . HIS   A 1 247 ? -20.869 6.895   3.937   1.00 53.76  ? 247 HIS   A CB   1 
ATOM   1957 C CG   . HIS   A 1 247 ? -21.942 6.258   3.110   1.00 53.87  ? 247 HIS   A CG   1 
ATOM   1958 N ND1  . HIS   A 1 247 ? -21.828 4.985   2.591   1.00 53.26  ? 247 HIS   A ND1  1 
ATOM   1959 C CD2  . HIS   A 1 247 ? -23.145 6.723   2.702   1.00 55.94  ? 247 HIS   A CD2  1 
ATOM   1960 C CE1  . HIS   A 1 247 ? -22.919 4.689   1.909   1.00 54.57  ? 247 HIS   A CE1  1 
ATOM   1961 N NE2  . HIS   A 1 247 ? -23.731 5.730   1.954   1.00 56.13  ? 247 HIS   A NE2  1 
ATOM   1962 N N    . TYR   A 1 248 ? -19.912 8.638   0.978   1.00 54.88  ? 248 TYR   A N    1 
ATOM   1963 C CA   . TYR   A 1 248 ? -20.237 9.733   0.076   1.00 56.27  ? 248 TYR   A CA   1 
ATOM   1964 C C    . TYR   A 1 248 ? -20.298 9.189   -1.345  1.00 54.33  ? 248 TYR   A C    1 
ATOM   1965 O O    . TYR   A 1 248 ? -19.374 9.405   -2.145  1.00 52.05  ? 248 TYR   A O    1 
ATOM   1966 C CB   . TYR   A 1 248 ? -19.222 10.876  0.191   1.00 57.07  ? 248 TYR   A CB   1 
ATOM   1967 C CG   . TYR   A 1 248 ? -19.859 12.229  -0.037  1.00 58.57  ? 248 TYR   A CG   1 
ATOM   1968 C CD1  . TYR   A 1 248 ? -20.583 12.846  0.972   1.00 61.74  ? 248 TYR   A CD1  1 
ATOM   1969 C CD2  . TYR   A 1 248 ? -19.772 12.874  -1.269  1.00 56.43  ? 248 TYR   A CD2  1 
ATOM   1970 C CE1  . TYR   A 1 248 ? -21.187 14.076  0.780   1.00 62.49  ? 248 TYR   A CE1  1 
ATOM   1971 C CE2  . TYR   A 1 248 ? -20.377 14.105  -1.475  1.00 57.86  ? 248 TYR   A CE2  1 
ATOM   1972 C CZ   . TYR   A 1 248 ? -21.088 14.699  -0.436  1.00 65.18  ? 248 TYR   A CZ   1 
ATOM   1973 O OH   . TYR   A 1 248 ? -21.710 15.924  -0.580  1.00 69.79  ? 248 TYR   A OH   1 
ATOM   1974 N N    . PRO   A 1 249 ? -21.372 8.463   -1.678  1.00 48.92  ? 249 PRO   A N    1 
ATOM   1975 C CA   . PRO   A 1 249 ? -21.442 7.799   -2.998  1.00 46.60  ? 249 PRO   A CA   1 
ATOM   1976 C C    . PRO   A 1 249 ? -21.182 8.728   -4.179  1.00 47.96  ? 249 PRO   A C    1 
ATOM   1977 O O    . PRO   A 1 249 ? -20.406 8.369   -5.073  1.00 46.47  ? 249 PRO   A O    1 
ATOM   1978 C CB   . PRO   A 1 249 ? -22.875 7.241   -3.024  1.00 47.07  ? 249 PRO   A CB   1 
ATOM   1979 C CG   . PRO   A 1 249 ? -23.231 7.042   -1.549  1.00 46.72  ? 249 PRO   A CG   1 
ATOM   1980 C CD   . PRO   A 1 249 ? -22.519 8.147   -0.800  1.00 46.58  ? 249 PRO   A CD   1 
ATOM   1981 N N    . SER   A 1 250 ? -21.722 9.944   -4.138  1.00 65.23  ? 250 SER   A N    1 
ATOM   1982 C CA   . SER   A 1 250 ? -21.481 10.997  -5.119  1.00 65.71  ? 250 SER   A CA   1 
ATOM   1983 C C    . SER   A 1 250 ? -20.018 11.023  -5.562  1.00 65.40  ? 250 SER   A C    1 
ATOM   1984 O O    . SER   A 1 250 ? -19.734 11.214  -6.751  1.00 65.62  ? 250 SER   A O    1 
ATOM   1985 C CB   . SER   A 1 250 ? -21.942 12.336  -4.514  1.00 73.24  ? 250 SER   A CB   1 
ATOM   1986 O OG   . SER   A 1 250 ? -21.135 13.437  -4.885  1.00 72.42  ? 250 SER   A OG   1 
ATOM   1987 N N    . LYS   A 1 251 ? -19.079 10.854  -4.626  1.00 52.76  ? 251 LYS   A N    1 
ATOM   1988 C CA   . LYS   A 1 251 ? -17.655 10.828  -4.941  1.00 51.47  ? 251 LYS   A CA   1 
ATOM   1989 C C    . LYS   A 1 251 ? -17.086 9.418   -4.911  1.00 50.81  ? 251 LYS   A C    1 
ATOM   1990 O O    . LYS   A 1 251 ? -15.871 9.245   -4.772  1.00 50.83  ? 251 LYS   A O    1 
ATOM   1991 C CB   . LYS   A 1 251 ? -16.860 11.715  -3.980  1.00 54.75  ? 251 LYS   A CB   1 
ATOM   1992 C CG   . LYS   A 1 251 ? -17.337 13.148  -3.858  1.00 57.83  ? 251 LYS   A CG   1 
ATOM   1993 C CD   . LYS   A 1 251 ? -16.230 14.013  -3.257  1.00 58.27  ? 251 LYS   A CD   1 
ATOM   1994 C CE   . LYS   A 1 251 ? -15.180 14.345  -4.332  1.00 68.71  ? 251 LYS   A CE   1 
ATOM   1995 N NZ   . LYS   A 1 251 ? -13.912 14.882  -3.745  1.00 70.50  ? 251 LYS   A NZ   1 
ATOM   1996 N N    . LYS   A 1 252 ? -17.938 8.405   -5.011  1.00 48.53  ? 252 LYS   A N    1 
ATOM   1997 C CA   . LYS   A 1 252 ? -17.487 7.018   -4.973  1.00 47.18  ? 252 LYS   A CA   1 
ATOM   1998 C C    . LYS   A 1 252 ? -16.748 6.693   -3.671  1.00 46.27  ? 252 LYS   A C    1 
ATOM   1999 O O    . LYS   A 1 252 ? -15.780 5.921   -3.660  1.00 44.92  ? 252 LYS   A O    1 
ATOM   2000 C CB   . LYS   A 1 252 ? -16.621 6.697   -6.196  1.00 46.91  ? 252 LYS   A CB   1 
ATOM   2001 C CG   . LYS   A 1 252 ? -17.427 6.676   -7.508  1.00 47.97  ? 252 LYS   A CG   1 
ATOM   2002 C CD   . LYS   A 1 252 ? -16.552 6.434   -8.685  1.00 47.86  ? 252 LYS   A CD   1 
ATOM   2003 C CE   . LYS   A 1 252 ? -17.380 6.022   -9.915  1.00 58.36  ? 252 LYS   A CE   1 
ATOM   2004 N NZ   . LYS   A 1 252 ? -18.838 6.377   -9.798  1.00 55.77  ? 252 LYS   A NZ   1 
ATOM   2005 N N    . MET   A 1 253 ? -17.182 7.304   -2.568  1.00 47.84  ? 253 MET   A N    1 
ATOM   2006 C CA   . MET   A 1 253 ? -16.636 7.010   -1.243  1.00 45.76  ? 253 MET   A CA   1 
ATOM   2007 C C    . MET   A 1 253 ? -17.571 6.014   -0.569  1.00 45.01  ? 253 MET   A C    1 
ATOM   2008 O O    . MET   A 1 253 ? -18.693 6.352   -0.181  1.00 45.98  ? 253 MET   A O    1 
ATOM   2009 C CB   . MET   A 1 253 ? -16.472 8.276   -0.417  1.00 48.03  ? 253 MET   A CB   1 
ATOM   2010 C CG   . MET   A 1 253 ? -15.247 9.070   -0.801  1.00 47.37  ? 253 MET   A CG   1 
ATOM   2011 S SD   . MET   A 1 253 ? -15.282 10.696  -0.021  1.00 56.00  ? 253 MET   A SD   1 
ATOM   2012 C CE   . MET   A 1 253 ? -13.722 11.335  -0.581  1.00 54.69  ? 253 MET   A CE   1 
ATOM   2013 N N    . THR   A 1 254 ? -17.127 4.766   -0.509  1.00 46.36  ? 254 THR   A N    1 
ATOM   2014 C CA   . THR   A 1 254 ? -17.815 3.725   0.235   1.00 49.03  ? 254 THR   A CA   1 
ATOM   2015 C C    . THR   A 1 254 ? -16.954 2.477   0.220   1.00 51.18  ? 254 THR   A C    1 
ATOM   2016 O O    . THR   A 1 254 ? -16.354 2.134   -0.804  1.00 46.30  ? 254 THR   A O    1 
ATOM   2017 C CB   . THR   A 1 254 ? -19.210 3.391   -0.319  1.00 49.65  ? 254 THR   A CB   1 
ATOM   2018 O OG1  . THR   A 1 254 ? -19.780 2.322   0.468   1.00 49.84  ? 254 THR   A OG1  1 
ATOM   2019 C CG2  . THR   A 1 254 ? -19.138 2.946   -1.803  1.00 50.04  ? 254 THR   A CG2  1 
ATOM   2020 N N    . GLY   A 1 255 ? -17.022 1.739   1.324   1.00 61.29  ? 255 GLY   A N    1 
ATOM   2021 C CA   . GLY   A 1 255 ? -16.232 0.552   1.565   1.00 58.74  ? 255 GLY   A CA   1 
ATOM   2022 C C    . GLY   A 1 255 ? -15.405 0.641   2.826   1.00 61.37  ? 255 GLY   A C    1 
ATOM   2023 O O    . GLY   A 1 255 ? -14.312 1.219   2.864   1.00 60.08  ? 255 GLY   A O    1 
ATOM   2024 N N    . SER   A 1 256 ? -15.916 -0.025  3.856   1.00 46.21  ? 256 SER   A N    1 
ATOM   2025 C CA   . SER   A 1 256 ? -15.299 -0.056  5.173   1.00 44.08  ? 256 SER   A CA   1 
ATOM   2026 C C    . SER   A 1 256 ? -15.166 -1.513  5.574   1.00 45.95  ? 256 SER   A C    1 
ATOM   2027 O O    . SER   A 1 256 ? -15.930 -2.365  5.112   1.00 45.79  ? 256 SER   A O    1 
ATOM   2028 C CB   . SER   A 1 256 ? -16.149 0.692   6.208   1.00 43.90  ? 256 SER   A CB   1 
ATOM   2029 O OG   . SER   A 1 256 ? -16.145 2.096   5.986   1.00 47.03  ? 256 SER   A OG   1 
ATOM   2030 N N    . GLY   A 1 257 ? -14.224 -1.824  6.451   1.00 48.36  ? 257 GLY   A N    1 
ATOM   2031 C CA   . GLY   A 1 257 ? -14.162 -3.217  6.840   1.00 49.35  ? 257 GLY   A CA   1 
ATOM   2032 C C    . GLY   A 1 257 ? -13.171 -3.541  7.930   1.00 48.19  ? 257 GLY   A C    1 
ATOM   2033 O O    . GLY   A 1 257 ? -12.347 -2.719  8.348   1.00 45.51  ? 257 GLY   A O    1 
ATOM   2034 N N    . ILE   A 1 258 ? -13.277 -4.785  8.374   1.00 46.47  ? 258 ILE   A N    1 
ATOM   2035 C CA   . ILE   A 1 258 ? -12.331 -5.407  9.278   1.00 48.86  ? 258 ILE   A CA   1 
ATOM   2036 C C    . ILE   A 1 258 ? -11.761 -6.605  8.536   1.00 48.65  ? 258 ILE   A C    1 
ATOM   2037 O O    . ILE   A 1 258 ? -12.513 -7.479  8.070   1.00 47.88  ? 258 ILE   A O    1 
ATOM   2038 C CB   . ILE   A 1 258 ? -12.971 -5.834  10.609  1.00 50.98  ? 258 ILE   A CB   1 
ATOM   2039 C CG1  . ILE   A 1 258 ? -13.676 -4.648  11.289  1.00 48.55  ? 258 ILE   A CG1  1 
ATOM   2040 C CG2  . ILE   A 1 258 ? -11.914 -6.417  11.523  1.00 48.68  ? 258 ILE   A CG2  1 
ATOM   2041 C CD1  . ILE   A 1 258 ? -14.841 -5.059  12.199  1.00 50.28  ? 258 ILE   A CD1  1 
ATOM   2042 N N    . TYR   A 1 259 ? -10.446 -6.611  8.378   1.00 49.30  ? 259 TYR   A N    1 
ATOM   2043 C CA   . TYR   A 1 259 ? -9.747  -7.615  7.602   1.00 52.50  ? 259 TYR   A CA   1 
ATOM   2044 C C    . TYR   A 1 259 ? -8.701  -8.292  8.477   1.00 55.81  ? 259 TYR   A C    1 
ATOM   2045 O O    . TYR   A 1 259 ? -8.101  -7.671  9.357   1.00 55.14  ? 259 TYR   A O    1 
ATOM   2046 C CB   . TYR   A 1 259 ? -9.089  -6.972  6.374   1.00 49.01  ? 259 TYR   A CB   1 
ATOM   2047 C CG   . TYR   A 1 259 ? -10.035 -6.053  5.640   1.00 48.75  ? 259 TYR   A CG   1 
ATOM   2048 C CD1  . TYR   A 1 259 ? -11.276 -6.504  5.226   1.00 48.36  ? 259 TYR   A CD1  1 
ATOM   2049 C CD2  . TYR   A 1 259 ? -9.702  -4.720  5.395   1.00 45.69  ? 259 TYR   A CD2  1 
ATOM   2050 C CE1  . TYR   A 1 259 ? -12.156 -5.670  4.565   1.00 51.45  ? 259 TYR   A CE1  1 
ATOM   2051 C CE2  . TYR   A 1 259 ? -10.581 -3.870  4.760   1.00 46.32  ? 259 TYR   A CE2  1 
ATOM   2052 C CZ   . TYR   A 1 259 ? -11.808 -4.350  4.329   1.00 49.10  ? 259 TYR   A CZ   1 
ATOM   2053 O OH   . TYR   A 1 259 ? -12.684 -3.527  3.634   1.00 49.35  ? 259 TYR   A OH   1 
ATOM   2054 N N    . ALA   A 1 260 ? -8.484  -9.569  8.224   1.00 60.38  ? 260 ALA   A N    1 
ATOM   2055 C CA   . ALA   A 1 260 ? -7.510  -10.358 8.954   1.00 57.35  ? 260 ALA   A CA   1 
ATOM   2056 C C    . ALA   A 1 260 ? -6.509  -10.928 7.953   1.00 60.53  ? 260 ALA   A C    1 
ATOM   2057 O O    . ALA   A 1 260 ? -6.752  -10.918 6.740   1.00 57.68  ? 260 ALA   A O    1 
ATOM   2058 C CB   . ALA   A 1 260 ? -8.197  -11.483 9.740   1.00 56.00  ? 260 ALA   A CB   1 
ATOM   2059 N N    . PRO   A 1 261 ? -5.359  -11.405 8.423   1.00 55.51  ? 261 PRO   A N    1 
ATOM   2060 C CA   . PRO   A 1 261 ? -4.365  -11.948 7.476   1.00 53.61  ? 261 PRO   A CA   1 
ATOM   2061 C C    . PRO   A 1 261 ? -4.909  -13.080 6.622   1.00 54.45  ? 261 PRO   A C    1 
ATOM   2062 O O    . PRO   A 1 261 ? -4.524  -13.205 5.450   1.00 55.26  ? 261 PRO   A O    1 
ATOM   2063 C CB   . PRO   A 1 261 ? -3.231  -12.413 8.396   1.00 55.63  ? 261 PRO   A CB   1 
ATOM   2064 C CG   . PRO   A 1 261 ? -3.362  -11.495 9.642   1.00 54.08  ? 261 PRO   A CG   1 
ATOM   2065 C CD   . PRO   A 1 261 ? -4.844  -11.281 9.802   1.00 51.90  ? 261 PRO   A CD   1 
ATOM   2066 N N    . ASN   A 1 262 ? -5.823  -13.891 7.160   1.00 66.96  ? 262 ASN   A N    1 
ATOM   2067 C CA   . ASN   A 1 262 ? -6.312  -15.063 6.446   1.00 67.20  ? 262 ASN   A CA   1 
ATOM   2068 C C    . ASN   A 1 262 ? -7.567  -14.793 5.621   1.00 66.64  ? 262 ASN   A C    1 
ATOM   2069 O O    . ASN   A 1 262 ? -7.901  -15.605 4.750   1.00 67.87  ? 262 ASN   A O    1 
ATOM   2070 C CB   . ASN   A 1 262 ? -6.578  -16.207 7.452   1.00 66.09  ? 262 ASN   A CB   1 
ATOM   2071 C CG   . ASN   A 1 262 ? -7.784  -15.939 8.361   1.00 73.91  ? 262 ASN   A CG   1 
ATOM   2072 O OD1  . ASN   A 1 262 ? -8.883  -15.681 7.880   1.00 70.42  ? 262 ASN   A OD1  1 
ATOM   2073 N ND2  . ASN   A 1 262 ? -7.571  -15.995 9.695   1.00 76.79  ? 262 ASN   A ND2  1 
ATOM   2074 N N    . SER   A 1 263 ? -8.263  -13.683 5.858   1.00 71.16  ? 263 SER   A N    1 
ATOM   2075 C CA   . SER   A 1 263 ? -9.504  -13.439 5.136   1.00 68.23  ? 263 SER   A CA   1 
ATOM   2076 C C    . SER   A 1 263 ? -10.114 -12.123 5.598   1.00 69.35  ? 263 SER   A C    1 
ATOM   2077 O O    . SER   A 1 263 ? -9.787  -11.611 6.672   1.00 69.75  ? 263 SER   A O    1 
ATOM   2078 C CB   . SER   A 1 263 ? -10.503 -14.578 5.345   1.00 71.90  ? 263 SER   A CB   1 
ATOM   2079 O OG   . SER   A 1 263 ? -11.835 -14.110 5.247   1.00 72.40  ? 263 SER   A OG   1 
ATOM   2080 N N    . SER   A 1 264 ? -11.022 -11.591 4.782   1.00 70.61  ? 264 SER   A N    1 
ATOM   2081 C CA   . SER   A 1 264 ? -11.879 -10.509 5.247   1.00 69.12  ? 264 SER   A CA   1 
ATOM   2082 C C    . SER   A 1 264 ? -12.845 -11.054 6.292   1.00 69.47  ? 264 SER   A C    1 
ATOM   2083 O O    . SER   A 1 264 ? -13.433 -12.127 6.111   1.00 67.93  ? 264 SER   A O    1 
ATOM   2084 C CB   . SER   A 1 264 ? -12.657 -9.888  4.082   1.00 68.04  ? 264 SER   A CB   1 
ATOM   2085 O OG   . SER   A 1 264 ? -14.048 -9.805  4.368   1.00 66.84  ? 264 SER   A OG   1 
ATOM   2086 N N    . ARG   A 1 265 ? -13.007 -10.319 7.390   1.00 57.72  ? 265 ARG   A N    1 
ATOM   2087 C CA   . ARG   A 1 265 ? -13.915 -10.738 8.447   1.00 61.51  ? 265 ARG   A CA   1 
ATOM   2088 C C    . ARG   A 1 265 ? -15.227 -9.973  8.418   1.00 61.10  ? 265 ARG   A C    1 
ATOM   2089 O O    . ARG   A 1 265 ? -16.260 -10.518 8.821   1.00 64.40  ? 265 ARG   A O    1 
ATOM   2090 C CB   . ARG   A 1 265 ? -13.246 -10.589 9.819   1.00 61.65  ? 265 ARG   A CB   1 
ATOM   2091 C CG   . ARG   A 1 265 ? -12.088 -11.560 9.990   1.00 60.74  ? 265 ARG   A CG   1 
ATOM   2092 C CD   . ARG   A 1 265 ? -12.574 -12.900 10.502  1.00 62.22  ? 265 ARG   A CD   1 
ATOM   2093 N NE   . ARG   A 1 265 ? -12.370 -12.995 11.943  1.00 70.30  ? 265 ARG   A NE   1 
ATOM   2094 C CZ   . ARG   A 1 265 ? -11.270 -13.468 12.520  1.00 73.51  ? 265 ARG   A CZ   1 
ATOM   2095 N NH1  . ARG   A 1 265 ? -10.258 -13.938 11.805  1.00 75.81  ? 265 ARG   A NH1  1 
ATOM   2096 N NH2  . ARG   A 1 265 ? -11.185 -13.482 13.851  1.00 73.96  ? 265 ARG   A NH2  1 
ATOM   2097 N N    . ALA   A 1 266 ? -15.205 -8.716  7.985   1.00 51.62  ? 266 ALA   A N    1 
ATOM   2098 C CA   . ALA   A 1 266 ? -16.439 -7.974  7.769   1.00 50.08  ? 266 ALA   A CA   1 
ATOM   2099 C C    . ALA   A 1 266 ? -16.170 -6.872  6.757   1.00 50.05  ? 266 ALA   A C    1 
ATOM   2100 O O    . ALA   A 1 266 ? -15.069 -6.318  6.703   1.00 49.79  ? 266 ALA   A O    1 
ATOM   2101 C CB   . ALA   A 1 266 ? -16.986 -7.378  9.073   1.00 53.01  ? 266 ALA   A CB   1 
ATOM   2102 N N    . PHE   A 1 267 ? -17.184 -6.548  5.963   1.00 50.02  ? 267 PHE   A N    1 
ATOM   2103 C CA   . PHE   A 1 267 ? -17.013 -5.456  5.024   1.00 51.44  ? 267 PHE   A CA   1 
ATOM   2104 C C    . PHE   A 1 267 ? -18.372 -4.853  4.699   1.00 50.91  ? 267 PHE   A C    1 
ATOM   2105 O O    . PHE   A 1 267 ? -19.418 -5.487  4.865   1.00 50.75  ? 267 PHE   A O    1 
ATOM   2106 C CB   . PHE   A 1 267 ? -16.256 -5.935  3.778   1.00 49.96  ? 267 PHE   A CB   1 
ATOM   2107 C CG   . PHE   A 1 267 ? -17.140 -6.542  2.717   1.00 54.54  ? 267 PHE   A CG   1 
ATOM   2108 C CD1  . PHE   A 1 267 ? -17.703 -5.742  1.731   1.00 52.55  ? 267 PHE   A CD1  1 
ATOM   2109 C CD2  . PHE   A 1 267 ? -17.394 -7.910  2.693   1.00 51.32  ? 267 PHE   A CD2  1 
ATOM   2110 C CE1  . PHE   A 1 267 ? -18.519 -6.276  0.770   1.00 49.83  ? 267 PHE   A CE1  1 
ATOM   2111 C CE2  . PHE   A 1 267 ? -18.212 -8.452  1.708   1.00 54.69  ? 267 PHE   A CE2  1 
ATOM   2112 C CZ   . PHE   A 1 267 ? -18.775 -7.634  0.757   1.00 51.15  ? 267 PHE   A CZ   1 
ATOM   2113 N N    . HIS   A 1 268 ? -18.333 -3.593  4.268   1.00 49.43  ? 268 HIS   A N    1 
ATOM   2114 C CA   . HIS   A 1 268 ? -19.507 -2.810  3.901   1.00 51.13  ? 268 HIS   A CA   1 
ATOM   2115 C C    . HIS   A 1 268 ? -19.219 -2.040  2.617   1.00 47.35  ? 268 HIS   A C    1 
ATOM   2116 O O    . HIS   A 1 268 ? -18.153 -1.423  2.474   1.00 46.11  ? 268 HIS   A O    1 
ATOM   2117 C CB   . HIS   A 1 268 ? -19.909 -1.828  5.029   1.00 46.25  ? 268 HIS   A CB   1 
ATOM   2118 C CG   . HIS   A 1 268 ? -21.118 -0.992  4.714   1.00 47.61  ? 268 HIS   A CG   1 
ATOM   2119 N ND1  . HIS   A 1 268 ? -22.397 -1.509  4.696   1.00 49.29  ? 268 HIS   A ND1  1 
ATOM   2120 C CD2  . HIS   A 1 268 ? -21.247 0.331   4.451   1.00 47.00  ? 268 HIS   A CD2  1 
ATOM   2121 C CE1  . HIS   A 1 268 ? -23.260 -0.548  4.417   1.00 49.10  ? 268 HIS   A CE1  1 
ATOM   2122 N NE2  . HIS   A 1 268 ? -22.589 0.580   4.265   1.00 49.72  ? 268 HIS   A NE2  1 
ATOM   2123 N N    . TYR   A 1 269 ? -20.192 -2.055  1.708   1.00 51.29  ? 269 TYR   A N    1 
ATOM   2124 C CA   . TYR   A 1 269 ? -20.138 -1.312  0.451   1.00 49.51  ? 269 TYR   A CA   1 
ATOM   2125 C C    . TYR   A 1 269 ? -21.567 -0.920  0.104   1.00 49.37  ? 269 TYR   A C    1 
ATOM   2126 O O    . TYR   A 1 269 ? -22.421 -1.799  -0.062  1.00 49.51  ? 269 TYR   A O    1 
ATOM   2127 C CB   . TYR   A 1 269 ? -19.513 -2.157  -0.674  1.00 49.59  ? 269 TYR   A CB   1 
ATOM   2128 C CG   . TYR   A 1 269 ? -19.458 -1.449  -2.037  1.00 49.68  ? 269 TYR   A CG   1 
ATOM   2129 C CD1  . TYR   A 1 269 ? -20.551 -1.451  -2.895  1.00 49.86  ? 269 TYR   A CD1  1 
ATOM   2130 C CD2  . TYR   A 1 269 ? -18.308 -0.755  -2.443  1.00 49.37  ? 269 TYR   A CD2  1 
ATOM   2131 C CE1  . TYR   A 1 269 ? -20.497 -0.788  -4.132  1.00 53.11  ? 269 TYR   A CE1  1 
ATOM   2132 C CE2  . TYR   A 1 269 ? -18.252 -0.082  -3.663  1.00 47.93  ? 269 TYR   A CE2  1 
ATOM   2133 C CZ   . TYR   A 1 269 ? -19.341 -0.104  -4.510  1.00 52.27  ? 269 TYR   A CZ   1 
ATOM   2134 O OH   . TYR   A 1 269 ? -19.272 0.555   -5.736  1.00 50.54  ? 269 TYR   A OH   1 
ATOM   2135 N N    . ASP   A 1 270 ? -21.833 0.383   -0.002  1.00 53.68  ? 270 ASP   A N    1 
ATOM   2136 C CA   . ASP   A 1 270 ? -23.202 0.858   -0.217  1.00 55.59  ? 270 ASP   A CA   1 
ATOM   2137 C C    . ASP   A 1 270 ? -23.165 2.125   -1.069  1.00 59.37  ? 270 ASP   A C    1 
ATOM   2138 O O    . ASP   A 1 270 ? -22.811 3.199   -0.568  1.00 61.10  ? 270 ASP   A O    1 
ATOM   2139 C CB   . ASP   A 1 270 ? -23.906 1.117   1.118   1.00 58.44  ? 270 ASP   A CB   1 
ATOM   2140 C CG   . ASP   A 1 270 ? -25.290 1.741   0.945   1.00 61.74  ? 270 ASP   A CG   1 
ATOM   2141 O OD1  . ASP   A 1 270 ? -25.900 1.566   -0.131  1.00 61.47  ? 270 ASP   A OD1  1 
ATOM   2142 O OD2  . ASP   A 1 270 ? -25.777 2.406   1.885   1.00 63.69  ? 270 ASP   A OD2  1 
ATOM   2143 N N    . MET   A 1 271 ? -23.554 1.998   -2.348  1.00 56.13  ? 271 MET   A N    1 
ATOM   2144 C CA   . MET   A 1 271 ? -23.689 3.120   -3.272  1.00 56.65  ? 271 MET   A CA   1 
ATOM   2145 C C    . MET   A 1 271 ? -25.104 3.685   -3.319  1.00 59.00  ? 271 MET   A C    1 
ATOM   2146 O O    . MET   A 1 271 ? -25.301 4.778   -3.864  1.00 59.97  ? 271 MET   A O    1 
ATOM   2147 C CB   . MET   A 1 271 ? -23.292 2.685   -4.693  1.00 53.45  ? 271 MET   A CB   1 
ATOM   2148 C CG   . MET   A 1 271 ? -21.804 2.691   -4.990  1.00 52.21  ? 271 MET   A CG   1 
ATOM   2149 S SD   . MET   A 1 271 ? -20.989 4.229   -4.532  1.00 55.90  ? 271 MET   A SD   1 
ATOM   2150 C CE   . MET   A 1 271 ? -20.715 4.992   -6.148  1.00 53.05  ? 271 MET   A CE   1 
ATOM   2151 N N    . LYS   A 1 272 ? -26.078 3.001   -2.719  1.00 68.18  ? 272 LYS   A N    1 
ATOM   2152 C CA   . LYS   A 1 272 ? -27.488 3.328   -2.902  1.00 71.18  ? 272 LYS   A CA   1 
ATOM   2153 C C    . LYS   A 1 272 ? -28.019 4.357   -1.905  1.00 73.43  ? 272 LYS   A C    1 
ATOM   2154 O O    . LYS   A 1 272 ? -28.768 5.256   -2.299  1.00 80.29  ? 272 LYS   A O    1 
ATOM   2155 C CB   . LYS   A 1 272 ? -28.324 2.048   -2.838  1.00 68.88  ? 272 LYS   A CB   1 
ATOM   2156 C CG   . LYS   A 1 272 ? -27.869 1.013   -3.847  1.00 69.37  ? 272 LYS   A CG   1 
ATOM   2157 C CD   . LYS   A 1 272 ? -28.686 -0.266  -3.819  1.00 72.33  ? 272 LYS   A CD   1 
ATOM   2158 C CE   . LYS   A 1 272 ? -30.096 -0.035  -3.326  1.00 79.79  ? 272 LYS   A CE   1 
ATOM   2159 N NZ   . LYS   A 1 272 ? -30.578 -1.223  -2.569  1.00 83.20  ? 272 LYS   A NZ   1 
ATOM   2160 N N    . THR   A 1 273 ? -27.681 4.237   -0.627  1.00 62.41  ? 273 THR   A N    1 
ATOM   2161 C CA   . THR   A 1 273 ? -28.207 5.096   0.431   1.00 62.74  ? 273 THR   A CA   1 
ATOM   2162 C C    . THR   A 1 273 ? -27.145 6.078   0.934   1.00 59.48  ? 273 THR   A C    1 
ATOM   2163 O O    . THR   A 1 273 ? -25.964 5.976   0.606   1.00 60.57  ? 273 THR   A O    1 
ATOM   2164 C CB   . THR   A 1 273 ? -28.720 4.230   1.582   1.00 65.03  ? 273 THR   A CB   1 
ATOM   2165 O OG1  . THR   A 1 273 ? -27.604 3.785   2.366   1.00 61.02  ? 273 THR   A OG1  1 
ATOM   2166 C CG2  . THR   A 1 273 ? -29.472 3.020   1.047   1.00 59.21  ? 273 THR   A CG2  1 
ATOM   2167 N N    . GLU   A 1 274 ? -27.551 6.985   1.824   1.00 69.98  ? 274 GLU   A N    1 
ATOM   2168 C CA   . GLU   A 1 274 ? -26.601 7.900   2.448   1.00 74.28  ? 274 GLU   A CA   1 
ATOM   2169 C C    . GLU   A 1 274 ? -26.318 7.556   3.911   1.00 72.00  ? 274 GLU   A C    1 
ATOM   2170 O O    . GLU   A 1 274 ? -25.779 8.390   4.643   1.00 72.90  ? 274 GLU   A O    1 
ATOM   2171 C CB   . GLU   A 1 274 ? -27.091 9.343   2.356   1.00 74.68  ? 274 GLU   A CB   1 
ATOM   2172 C CG   . GLU   A 1 274 ? -27.883 9.669   1.142   1.00 76.49  ? 274 GLU   A CG   1 
ATOM   2173 C CD   . GLU   A 1 274 ? -28.209 11.146  1.068   1.00 86.37  ? 274 GLU   A CD   1 
ATOM   2174 O OE1  . GLU   A 1 274 ? -27.398 11.901  0.484   1.00 89.92  ? 274 GLU   A OE1  1 
ATOM   2175 O OE2  . GLU   A 1 274 ? -29.271 11.550  1.598   1.00 89.22  ? 274 GLU   A OE2  1 
ATOM   2176 N N    . GLU   A 1 275 ? -26.661 6.348   4.351   1.00 67.04  ? 275 GLU   A N    1 
ATOM   2177 C CA   . GLU   A 1 275 ? -26.528 5.995   5.759   1.00 63.09  ? 275 GLU   A CA   1 
ATOM   2178 C C    . GLU   A 1 275 ? -25.105 5.573   6.104   1.00 60.43  ? 275 GLU   A C    1 
ATOM   2179 O O    . GLU   A 1 275 ? -24.378 5.020   5.276   1.00 61.03  ? 275 GLU   A O    1 
ATOM   2180 C CB   . GLU   A 1 275 ? -27.491 4.863   6.117   1.00 64.76  ? 275 GLU   A CB   1 
ATOM   2181 C CG   . GLU   A 1 275 ? -28.961 5.228   5.985   1.00 69.15  ? 275 GLU   A CG   1 
ATOM   2182 C CD   . GLU   A 1 275 ? -29.813 4.009   5.659   1.00 77.56  ? 275 GLU   A CD   1 
ATOM   2183 O OE1  . GLU   A 1 275 ? -30.888 4.161   5.022   1.00 81.27  ? 275 GLU   A OE1  1 
ATOM   2184 O OE2  . GLU   A 1 275 ? -29.394 2.893   6.042   1.00 78.28  ? 275 GLU   A OE2  1 
ATOM   2185 N N    . GLY   A 1 276 ? -24.711 5.839   7.352   1.00 63.28  ? 276 GLY   A N    1 
ATOM   2186 C CA   . GLY   A 1 276 ? -23.511 5.248   7.903   1.00 58.20  ? 276 GLY   A CA   1 
ATOM   2187 C C    . GLY   A 1 276 ? -23.758 3.807   8.292   1.00 58.76  ? 276 GLY   A C    1 
ATOM   2188 O O    . GLY   A 1 276 ? -24.873 3.295   8.220   1.00 63.15  ? 276 GLY   A O    1 
ATOM   2189 N N    . LYS   A 1 277 ? -22.692 3.143   8.731   1.00 54.07  ? 277 LYS   A N    1 
ATOM   2190 C CA   . LYS   A 1 277 ? -22.787 1.730   9.083   1.00 54.18  ? 277 LYS   A CA   1 
ATOM   2191 C C    . LYS   A 1 277 ? -21.652 1.377   10.031  1.00 57.81  ? 277 LYS   A C    1 
ATOM   2192 O O    . LYS   A 1 277 ? -20.492 1.707   9.752   1.00 52.69  ? 277 LYS   A O    1 
ATOM   2193 C CB   . LYS   A 1 277 ? -22.744 0.841   7.832   1.00 56.27  ? 277 LYS   A CB   1 
ATOM   2194 C CG   . LYS   A 1 277 ? -22.864 -0.652  8.122   1.00 57.83  ? 277 LYS   A CG   1 
ATOM   2195 C CD   . LYS   A 1 277 ? -24.300 -1.037  8.411   1.00 57.81  ? 277 LYS   A CD   1 
ATOM   2196 C CE   . LYS   A 1 277 ? -24.402 -2.490  8.820   1.00 59.67  ? 277 LYS   A CE   1 
ATOM   2197 N NZ   . LYS   A 1 277 ? -25.778 -2.816  9.302   1.00 67.33  ? 277 LYS   A NZ   1 
ATOM   2198 N N    . LEU   A 1 278 ? -21.999 0.744   11.165  1.00 52.37  ? 278 LEU   A N    1 
ATOM   2199 C CA   . LEU   A 1 278 ? -21.038 0.259   12.148  1.00 46.33  ? 278 LEU   A CA   1 
ATOM   2200 C C    . LEU   A 1 278 ? -20.788 -1.225  11.920  1.00 48.00  ? 278 LEU   A C    1 
ATOM   2201 O O    . LEU   A 1 278 ? -21.733 -2.029  11.873  1.00 47.33  ? 278 LEU   A O    1 
ATOM   2202 C CB   . LEU   A 1 278 ? -21.549 0.483   13.567  1.00 47.22  ? 278 LEU   A CB   1 
ATOM   2203 C CG   . LEU   A 1 278 ? -20.638 0.029   14.716  1.00 47.21  ? 278 LEU   A CG   1 
ATOM   2204 C CD1  . LEU   A 1 278 ? -19.432 0.941   14.898  1.00 46.04  ? 278 LEU   A CD1  1 
ATOM   2205 C CD2  . LEU   A 1 278 ? -21.421 -0.044  16.032  1.00 50.98  ? 278 LEU   A CD2  1 
ATOM   2206 N N    . LEU   A 1 279 ? -19.516 -1.589  11.815  1.00 49.60  ? 279 LEU   A N    1 
ATOM   2207 C CA   . LEU   A 1 279 ? -19.104 -2.970  11.621  1.00 47.38  ? 279 LEU   A CA   1 
ATOM   2208 C C    . LEU   A 1 279 ? -18.276 -3.416  12.814  1.00 48.20  ? 279 LEU   A C    1 
ATOM   2209 O O    . LEU   A 1 279 ? -17.433 -2.656  13.313  1.00 47.43  ? 279 LEU   A O    1 
ATOM   2210 C CB   . LEU   A 1 279 ? -18.281 -3.132  10.350  1.00 45.18  ? 279 LEU   A CB   1 
ATOM   2211 C CG   . LEU   A 1 279 ? -18.943 -2.850  9.007   1.00 47.54  ? 279 LEU   A CG   1 
ATOM   2212 C CD1  . LEU   A 1 279 ? -17.945 -3.226  7.900   1.00 43.87  ? 279 LEU   A CD1  1 
ATOM   2213 C CD2  . LEU   A 1 279 ? -20.247 -3.641  8.872   1.00 47.16  ? 279 LEU   A CD2  1 
ATOM   2214 N N    . LEU   A 1 280 ? -18.530 -4.646  13.265  1.00 60.23  ? 280 LEU   A N    1 
ATOM   2215 C CA   . LEU   A 1 280 ? -17.829 -5.265  14.379  1.00 60.52  ? 280 LEU   A CA   1 
ATOM   2216 C C    . LEU   A 1 280 ? -17.354 -6.655  13.989  1.00 60.49  ? 280 LEU   A C    1 
ATOM   2217 O O    . LEU   A 1 280 ? -18.030 -7.377  13.252  1.00 65.73  ? 280 LEU   A O    1 
ATOM   2218 C CB   . LEU   A 1 280 ? -18.730 -5.360  15.616  1.00 58.44  ? 280 LEU   A CB   1 
ATOM   2219 C CG   . LEU   A 1 280 ? -19.026 -4.068  16.390  1.00 62.88  ? 280 LEU   A CG   1 
ATOM   2220 C CD1  . LEU   A 1 280 ? -20.514 -3.760  16.521  1.00 63.20  ? 280 LEU   A CD1  1 
ATOM   2221 C CD2  . LEU   A 1 280 ? -18.417 -4.173  17.745  1.00 60.09  ? 280 LEU   A CD2  1 
ATOM   2222 N N    . SER   A 1 281 ? -16.198 -7.044  14.520  1.00 57.74  ? 281 SER   A N    1 
ATOM   2223 C CA   . SER   A 1 281 ? -15.702 -8.387  14.262  1.00 56.45  ? 281 SER   A CA   1 
ATOM   2224 C C    . SER   A 1 281 ? -14.610 -8.750  15.253  1.00 57.71  ? 281 SER   A C    1 
ATOM   2225 O O    . SER   A 1 281 ? -13.816 -7.894  15.664  1.00 57.04  ? 281 SER   A O    1 
ATOM   2226 C CB   . SER   A 1 281 ? -15.162 -8.534  12.839  1.00 57.71  ? 281 SER   A CB   1 
ATOM   2227 O OG   . SER   A 1 281 ? -14.588 -9.821  12.649  1.00 59.79  ? 281 SER   A OG   1 
ATOM   2228 N N    . GLN   A 1 282 ? -14.572 -10.039 15.595  1.00 73.99  ? 282 GLN   A N    1 
ATOM   2229 C CA   . GLN   A 1 282 ? -13.541 -10.602 16.460  1.00 77.88  ? 282 GLN   A CA   1 
ATOM   2230 C C    . GLN   A 1 282 ? -12.249 -10.773 15.685  1.00 76.29  ? 282 GLN   A C    1 
ATOM   2231 O O    . GLN   A 1 282 ? -12.265 -11.202 14.534  1.00 75.40  ? 282 GLN   A O    1 
ATOM   2232 C CB   . GLN   A 1 282 ? -13.989 -11.965 16.985  1.00 73.83  ? 282 GLN   A CB   1 
ATOM   2233 C CG   . GLN   A 1 282 ? -15.477 -12.049 17.056  1.00 85.38  ? 282 GLN   A CG   1 
ATOM   2234 C CD   . GLN   A 1 282 ? -16.080 -11.121 18.043  1.00 88.68  ? 282 GLN   A CD   1 
ATOM   2235 O OE1  . GLN   A 1 282 ? -17.220 -10.643 17.919  1.00 83.83  ? 282 GLN   A OE1  1 
ATOM   2236 N NE2  . GLN   A 1 282 ? -15.388 -10.942 19.093  1.00 90.27  ? 282 GLN   A NE2  1 
ATOM   2237 N N    . LEU   A 1 283 ? -11.122 -10.453 16.325  1.00 55.95  ? 283 LEU   A N    1 
ATOM   2238 C CA   . LEU   A 1 283 ? -9.814  -10.654 15.710  1.00 55.99  ? 283 LEU   A CA   1 
ATOM   2239 C C    . LEU   A 1 283 ? -8.875  -11.275 16.728  1.00 57.43  ? 283 LEU   A C    1 
ATOM   2240 O O    . LEU   A 1 283 ? -8.992  -11.016 17.919  1.00 58.39  ? 283 LEU   A O    1 
ATOM   2241 C CB   . LEU   A 1 283 ? -9.185  -9.353  15.222  1.00 52.91  ? 283 LEU   A CB   1 
ATOM   2242 C CG   . LEU   A 1 283 ? -9.982  -8.523  14.234  1.00 54.09  ? 283 LEU   A CG   1 
ATOM   2243 C CD1  . LEU   A 1 283 ? -9.123  -7.374  13.762  1.00 50.29  ? 283 LEU   A CD1  1 
ATOM   2244 C CD2  . LEU   A 1 283 ? -10.432 -9.403  13.058  1.00 55.37  ? 283 LEU   A CD2  1 
ATOM   2245 N N    . ASP   A 1 284 ? -7.923  -12.071 16.247  1.00 69.59  ? 284 ASP   A N    1 
ATOM   2246 C CA   . ASP   A 1 284 ? -6.833  -12.531 17.098  1.00 69.67  ? 284 ASP   A CA   1 
ATOM   2247 C C    . ASP   A 1 284 ? -5.849  -11.398 17.370  1.00 67.21  ? 284 ASP   A C    1 
ATOM   2248 O O    . ASP   A 1 284 ? -5.448  -10.670 16.461  1.00 67.27  ? 284 ASP   A O    1 
ATOM   2249 C CB   . ASP   A 1 284 ? -6.104  -13.702 16.444  1.00 73.31  ? 284 ASP   A CB   1 
ATOM   2250 C CG   . ASP   A 1 284 ? -6.908  -14.989 16.470  1.00 76.25  ? 284 ASP   A CG   1 
ATOM   2251 O OD1  . ASP   A 1 284 ? -7.810  -15.128 17.331  1.00 73.51  ? 284 ASP   A OD1  1 
ATOM   2252 O OD2  . ASP   A 1 284 ? -6.631  -15.862 15.619  1.00 82.96  ? 284 ASP   A OD2  1 
ATOM   2253 N N    . SER   A 1 285 ? -5.434  -11.274 18.631  1.00 63.70  ? 285 SER   A N    1 
ATOM   2254 C CA   . SER   A 1 285 ? -4.437  -10.273 18.992  1.00 61.43  ? 285 SER   A CA   1 
ATOM   2255 C C    . SER   A 1 285 ? -3.116  -10.499 18.261  1.00 61.40  ? 285 SER   A C    1 
ATOM   2256 O O    . SER   A 1 285 ? -2.451  -9.534  17.867  1.00 60.56  ? 285 SER   A O    1 
ATOM   2257 C CB   . SER   A 1 285 ? -4.215  -10.285 20.500  1.00 62.14  ? 285 SER   A CB   1 
ATOM   2258 O OG   . SER   A 1 285 ? -5.411  -9.952  21.179  1.00 63.89  ? 285 SER   A OG   1 
ATOM   2259 N N    . HIS   A 1 286 ? -2.680  -11.757 18.147  1.00 65.86  ? 286 HIS   A N    1 
ATOM   2260 C CA   . HIS   A 1 286 ? -1.456  -12.127 17.430  1.00 69.10  ? 286 HIS   A CA   1 
ATOM   2261 C C    . HIS   A 1 286 ? -1.728  -13.245 16.421  1.00 68.51  ? 286 HIS   A C    1 
ATOM   2262 O O    . HIS   A 1 286 ? -1.582  -14.432 16.757  1.00 71.04  ? 286 HIS   A O    1 
ATOM   2263 C CB   . HIS   A 1 286 ? -0.373  -12.546 18.419  1.00 68.47  ? 286 HIS   A CB   1 
ATOM   2264 C CG   . HIS   A 1 286 ? -0.086  -11.527 19.480  1.00 73.55  ? 286 HIS   A CG   1 
ATOM   2265 N ND1  . HIS   A 1 286 ? 0.806   -10.493 19.294  1.00 72.58  ? 286 HIS   A ND1  1 
ATOM   2266 C CD2  . HIS   A 1 286 ? -0.548  -11.402 20.749  1.00 69.36  ? 286 HIS   A CD2  1 
ATOM   2267 C CE1  . HIS   A 1 286 ? 0.870   -9.765  20.393  1.00 67.96  ? 286 HIS   A CE1  1 
ATOM   2268 N NE2  . HIS   A 1 286 ? 0.055   -10.293 21.289  1.00 71.07  ? 286 HIS   A NE2  1 
ATOM   2269 N N    . PRO   A 1 287 ? -2.115  -12.905 15.179  1.00 68.75  ? 287 PRO   A N    1 
ATOM   2270 C CA   . PRO   A 1 287 ? -2.446  -13.926 14.148  1.00 71.09  ? 287 PRO   A CA   1 
ATOM   2271 C C    . PRO   A 1 287 ? -1.293  -14.818 13.664  1.00 73.44  ? 287 PRO   A C    1 
ATOM   2272 O O    . PRO   A 1 287 ? -0.098  -14.484 13.760  1.00 74.05  ? 287 PRO   A O    1 
ATOM   2273 C CB   . PRO   A 1 287 ? -2.940  -13.098 12.960  1.00 64.99  ? 287 PRO   A CB   1 
ATOM   2274 C CG   . PRO   A 1 287 ? -3.071  -11.708 13.424  1.00 62.91  ? 287 PRO   A CG   1 
ATOM   2275 C CD   . PRO   A 1 287 ? -2.244  -11.539 14.674  1.00 62.91  ? 287 PRO   A CD   1 
ATOM   2276 N N    . SER   A 1 288 ? -1.648  -15.967 13.098  1.00 95.65  ? 288 SER   A N    1 
ATOM   2277 C CA   . SER   A 1 288 ? -0.571  -16.645 12.401  1.00 95.11  ? 288 SER   A CA   1 
ATOM   2278 C C    . SER   A 1 288 ? -0.501  -16.186 10.957  1.00 97.75  ? 288 SER   A C    1 
ATOM   2279 O O    . SER   A 1 288 ? -1.467  -15.700 10.365  1.00 94.92  ? 288 SER   A O    1 
ATOM   2280 C CB   . SER   A 1 288 ? -0.566  -18.210 12.454  1.00 100.41 ? 288 SER   A CB   1 
ATOM   2281 O OG   . SER   A 1 288 ? -0.963  -18.958 13.541  1.00 108.88 ? 288 SER   A OG   1 
ATOM   2282 N N    . HIS   A 1 289 ? 0.731   -16.234 10.507  1.00 124.11 ? 289 HIS   A N    1 
ATOM   2283 C CA   . HIS   A 1 289 ? 1.207   -16.185 9.162   1.00 123.43 ? 289 HIS   A CA   1 
ATOM   2284 C C    . HIS   A 1 289 ? 1.576   -17.612 8.767   1.00 125.63 ? 289 HIS   A C    1 
ATOM   2285 O O    . HIS   A 1 289 ? 2.321   -18.294 9.479   1.00 119.68 ? 289 HIS   A O    1 
ATOM   2286 C CB   . HIS   A 1 289 ? 2.398   -15.254 9.227   1.00 120.48 ? 289 HIS   A CB   1 
ATOM   2287 C CG   . HIS   A 1 289 ? 2.114   -14.040 10.068  1.00 124.01 ? 289 HIS   A CG   1 
ATOM   2288 N ND1  . HIS   A 1 289 ? 3.063   -13.425 10.856  1.00 126.11 ? 289 HIS   A ND1  1 
ATOM   2289 C CD2  . HIS   A 1 289 ? 0.969   -13.333 10.244  1.00 120.24 ? 289 HIS   A CD2  1 
ATOM   2290 C CE1  . HIS   A 1 289 ? 2.527   -12.369 11.445  1.00 120.87 ? 289 HIS   A CE1  1 
ATOM   2291 N NE2  . HIS   A 1 289 ? 1.255   -12.295 11.097  1.00 119.67 ? 289 HIS   A NE2  1 
ATOM   2292 N N    . SER   A 1 290 ? 1.016   -18.058 7.645   1.00 116.76 ? 290 SER   A N    1 
ATOM   2293 C CA   . SER   A 1 290 ? 1.493   -19.224 6.943   1.00 112.73 ? 290 SER   A CA   1 
ATOM   2294 C C    . SER   A 1 290 ? 2.904   -18.946 6.425   1.00 114.23 ? 290 SER   A C    1 
ATOM   2295 O O    . SER   A 1 290 ? 3.428   -17.829 6.536   1.00 113.88 ? 290 SER   A O    1 
ATOM   2296 C CB   . SER   A 1 290 ? 0.533   -19.549 5.801   1.00 121.99 ? 290 SER   A CB   1 
ATOM   2297 O OG   . SER   A 1 290 ? -0.055  -18.356 5.297   1.00 123.26 ? 290 SER   A OG   1 
ATOM   2298 N N    . ALA   A 1 291 ? 3.541   -19.979 5.868   1.00 85.88  ? 291 ALA   A N    1 
ATOM   2299 C CA   . ALA   A 1 291 ? 4.851   -19.762 5.267   1.00 85.24  ? 291 ALA   A CA   1 
ATOM   2300 C C    . ALA   A 1 291 ? 4.781   -18.577 4.317   1.00 84.08  ? 291 ALA   A C    1 
ATOM   2301 O O    . ALA   A 1 291 ? 3.778   -18.375 3.628   1.00 82.64  ? 291 ALA   A O    1 
ATOM   2302 C CB   . ALA   A 1 291 ? 5.317   -21.013 4.516   1.00 88.65  ? 291 ALA   A CB   1 
ATOM   2303 N N    . VAL   A 1 292 ? 5.839   -17.759 4.323   1.00 93.78  ? 292 VAL   A N    1 
ATOM   2304 C CA   . VAL   A 1 292 ? 5.892   -16.645 3.392   1.00 97.16  ? 292 VAL   A CA   1 
ATOM   2305 C C    . VAL   A 1 292 ? 5.877   -17.190 1.965   1.00 97.43  ? 292 VAL   A C    1 
ATOM   2306 O O    . VAL   A 1 292 ? 6.230   -18.346 1.696   1.00 97.39  ? 292 VAL   A O    1 
ATOM   2307 C CB   . VAL   A 1 292 ? 7.104   -15.732 3.635   1.00 98.02  ? 292 VAL   A CB   1 
ATOM   2308 C CG1  . VAL   A 1 292 ? 7.071   -14.533 2.682   1.00 94.40  ? 292 VAL   A CG1  1 
ATOM   2309 C CG2  . VAL   A 1 292 ? 7.096   -15.245 5.068   1.00 93.20  ? 292 VAL   A CG2  1 
ATOM   2310 N N    . VAL   A 1 293 ? 5.443   -16.346 1.044   1.00 82.08  ? 293 VAL   A N    1 
ATOM   2311 C CA   . VAL   A 1 293 ? 5.207   -16.736 -0.333  1.00 78.89  ? 293 VAL   A CA   1 
ATOM   2312 C C    . VAL   A 1 293 ? 6.352   -16.192 -1.180  1.00 82.43  ? 293 VAL   A C    1 
ATOM   2313 O O    . VAL   A 1 293 ? 6.822   -15.072 -0.942  1.00 79.65  ? 293 VAL   A O    1 
ATOM   2314 C CB   . VAL   A 1 293 ? 3.839   -16.220 -0.813  1.00 78.89  ? 293 VAL   A CB   1 
ATOM   2315 C CG1  . VAL   A 1 293 ? 3.620   -16.547 -2.293  1.00 76.14  ? 293 VAL   A CG1  1 
ATOM   2316 C CG2  . VAL   A 1 293 ? 2.723   -16.794 0.065   1.00 75.47  ? 293 VAL   A CG2  1 
ATOM   2317 N N    . ASN   A 1 294 ? 6.880   -17.029 -2.082  1.00 80.72  ? 294 ASN   A N    1 
ATOM   2318 C CA   . ASN   A 1 294 ? 7.752   -16.580 -3.172  1.00 79.33  ? 294 ASN   A CA   1 
ATOM   2319 C C    . ASN   A 1 294 ? 6.833   -16.291 -4.364  1.00 81.26  ? 294 ASN   A C    1 
ATOM   2320 O O    . ASN   A 1 294 ? 6.419   -17.206 -5.086  1.00 79.92  ? 294 ASN   A O    1 
ATOM   2321 C CB   . ASN   A 1 294 ? 8.811   -17.640 -3.490  1.00 80.02  ? 294 ASN   A CB   1 
ATOM   2322 C CG   . ASN   A 1 294 ? 9.935   -17.133 -4.423  1.00 83.48  ? 294 ASN   A CG   1 
ATOM   2323 O OD1  . ASN   A 1 294 ? 9.865   -16.030 -4.967  1.00 85.58  ? 294 ASN   A OD1  1 
ATOM   2324 N ND2  . ASN   A 1 294 ? 10.956  -17.970 -4.631  1.00 83.90  ? 294 ASN   A ND2  1 
ATOM   2325 N N    . TRP   A 1 295 ? 6.539   -15.006 -4.596  1.00 75.60  ? 295 TRP   A N    1 
ATOM   2326 C CA   . TRP   A 1 295 ? 5.491   -14.623 -5.543  1.00 73.86  ? 295 TRP   A CA   1 
ATOM   2327 C C    . TRP   A 1 295 ? 5.838   -14.944 -6.996  1.00 75.00  ? 295 TRP   A C    1 
ATOM   2328 O O    . TRP   A 1 295 ? 4.942   -14.932 -7.850  1.00 70.36  ? 295 TRP   A O    1 
ATOM   2329 C CB   . TRP   A 1 295 ? 5.184   -13.129 -5.412  1.00 68.69  ? 295 TRP   A CB   1 
ATOM   2330 C CG   . TRP   A 1 295 ? 4.280   -12.792 -4.275  1.00 69.99  ? 295 TRP   A CG   1 
ATOM   2331 C CD1  . TRP   A 1 295 ? 4.619   -12.119 -3.128  1.00 71.85  ? 295 TRP   A CD1  1 
ATOM   2332 C CD2  . TRP   A 1 295 ? 2.885   -13.105 -4.158  1.00 66.98  ? 295 TRP   A CD2  1 
ATOM   2333 N NE1  . TRP   A 1 295 ? 3.517   -11.998 -2.306  1.00 69.36  ? 295 TRP   A NE1  1 
ATOM   2334 C CE2  . TRP   A 1 295 ? 2.443   -12.594 -2.915  1.00 70.21  ? 295 TRP   A CE2  1 
ATOM   2335 C CE3  . TRP   A 1 295 ? 1.970   -13.770 -4.974  1.00 65.95  ? 295 TRP   A CE3  1 
ATOM   2336 C CZ2  . TRP   A 1 295 ? 1.125   -12.728 -2.482  1.00 65.75  ? 295 TRP   A CZ2  1 
ATOM   2337 C CZ3  . TRP   A 1 295 ? 0.663   -13.899 -4.541  1.00 62.48  ? 295 TRP   A CZ3  1 
ATOM   2338 C CH2  . TRP   A 1 295 ? 0.253   -13.379 -3.312  1.00 64.16  ? 295 TRP   A CH2  1 
ATOM   2339 N N    . THR   A 1 296 ? 7.104   -15.211 -7.302  1.00 79.42  ? 296 THR   A N    1 
ATOM   2340 C CA   . THR   A 1 296 ? 7.518   -15.536 -8.657  1.00 78.52  ? 296 THR   A CA   1 
ATOM   2341 C C    . THR   A 1 296 ? 7.938   -16.988 -8.823  1.00 83.20  ? 296 THR   A C    1 
ATOM   2342 O O    . THR   A 1 296 ? 8.267   -17.396 -9.944  1.00 83.17  ? 296 THR   A O    1 
ATOM   2343 C CB   . THR   A 1 296 ? 8.671   -14.626 -9.089  1.00 80.35  ? 296 THR   A CB   1 
ATOM   2344 O OG1  . THR   A 1 296 ? 8.965   -14.850 -10.476 1.00 83.10  ? 296 THR   A OG1  1 
ATOM   2345 C CG2  . THR   A 1 296 ? 9.912   -14.911 -8.257  1.00 79.68  ? 296 THR   A CG2  1 
ATOM   2346 N N    . SER   A 1 297 ? 7.913   -17.783 -7.752  1.00 88.94  ? 297 SER   A N    1 
ATOM   2347 C CA   . SER   A 1 297 ? 8.424   -19.149 -7.797  1.00 89.95  ? 297 SER   A CA   1 
ATOM   2348 C C    . SER   A 1 297 ? 7.688   -19.972 -8.858  1.00 92.23  ? 297 SER   A C    1 
ATOM   2349 O O    . SER   A 1 297 ? 8.282   -20.389 -9.867  1.00 93.11  ? 297 SER   A O    1 
ATOM   2350 C CB   . SER   A 1 297 ? 8.303   -19.794 -6.407  1.00 85.66  ? 297 SER   A CB   1 
ATOM   2351 O OG   . SER   A 1 297 ? 9.067   -20.984 -6.314  1.00 86.37  ? 297 SER   A OG   1 
ATOM   2352 N N    . TYR   A 1 298 ? 6.387   -20.200 -8.658  1.00 87.05  ? 298 TYR   A N    1 
ATOM   2353 C CA   . TYR   A 1 298 ? 5.646   -20.995 -9.627  1.00 80.19  ? 298 TYR   A CA   1 
ATOM   2354 C C    . TYR   A 1 298 ? 5.717   -20.346 -10.996 1.00 83.91  ? 298 TYR   A C    1 
ATOM   2355 O O    . TYR   A 1 298 ? 6.158   -20.975 -11.961 1.00 86.23  ? 298 TYR   A O    1 
ATOM   2356 C CB   . TYR   A 1 298 ? 4.190   -21.166 -9.184  1.00 79.32  ? 298 TYR   A CB   1 
ATOM   2357 C CG   . TYR   A 1 298 ? 3.329   -22.013 -10.107 1.00 82.52  ? 298 TYR   A CG   1 
ATOM   2358 C CD1  . TYR   A 1 298 ? 3.174   -21.689 -11.459 1.00 83.51  ? 298 TYR   A CD1  1 
ATOM   2359 C CD2  . TYR   A 1 298 ? 2.687   -23.153 -9.635  1.00 81.98  ? 298 TYR   A CD2  1 
ATOM   2360 C CE1  . TYR   A 1 298 ? 2.407   -22.466 -12.305 1.00 80.26  ? 298 TYR   A CE1  1 
ATOM   2361 C CE2  . TYR   A 1 298 ? 1.907   -23.934 -10.480 1.00 84.18  ? 298 TYR   A CE2  1 
ATOM   2362 C CZ   . TYR   A 1 298 ? 1.777   -23.582 -11.817 1.00 81.31  ? 298 TYR   A CZ   1 
ATOM   2363 O OH   . TYR   A 1 298 ? 1.014   -24.346 -12.668 1.00 77.79  ? 298 TYR   A OH   1 
ATOM   2364 N N    . ALA   A 1 299 ? 5.378   -19.056 -11.081 1.00 97.07  ? 299 ALA   A N    1 
ATOM   2365 C CA   . ALA   A 1 299 ? 5.312   -18.397 -12.383 1.00 95.26  ? 299 ALA   A CA   1 
ATOM   2366 C C    . ALA   A 1 299 ? 6.641   -18.510 -13.118 1.00 96.74  ? 299 ALA   A C    1 
ATOM   2367 O O    . ALA   A 1 299 ? 6.672   -18.661 -14.346 1.00 96.02  ? 299 ALA   A O    1 
ATOM   2368 C CB   . ALA   A 1 299 ? 4.904   -16.934 -12.220 1.00 89.97  ? 299 ALA   A CB   1 
ATOM   2369 N N    . SER   A 1 300 ? 7.752   -18.449 -12.383 1.00 82.95  ? 300 SER   A N    1 
ATOM   2370 C CA   . SER   A 1 300 ? 9.053   -18.661 -13.001 1.00 82.26  ? 300 SER   A CA   1 
ATOM   2371 C C    . SER   A 1 300 ? 9.307   -20.130 -13.313 1.00 85.03  ? 300 SER   A C    1 
ATOM   2372 O O    . SER   A 1 300 ? 10.287  -20.445 -13.999 1.00 83.42  ? 300 SER   A O    1 
ATOM   2373 C CB   . SER   A 1 300 ? 10.162  -18.112 -12.103 1.00 78.50  ? 300 SER   A CB   1 
ATOM   2374 O OG   . SER   A 1 300 ? 10.426  -16.755 -12.413 1.00 77.76  ? 300 SER   A OG   1 
ATOM   2375 N N    . SER   A 1 301 ? 8.465   -21.031 -12.810 1.00 90.37  ? 301 SER   A N    1 
ATOM   2376 C CA   . SER   A 1 301 ? 8.632   -22.455 -13.060 1.00 88.02  ? 301 SER   A CA   1 
ATOM   2377 C C    . SER   A 1 301 ? 7.883   -22.990 -14.284 1.00 94.28  ? 301 SER   A C    1 
ATOM   2378 O O    . SER   A 1 301 ? 8.103   -24.150 -14.646 1.00 96.01  ? 301 SER   A O    1 
ATOM   2379 C CB   . SER   A 1 301 ? 8.198   -23.248 -11.832 1.00 95.51  ? 301 SER   A CB   1 
ATOM   2380 O OG   . SER   A 1 301 ? 6.926   -23.831 -12.039 1.00 96.74  ? 301 SER   A OG   1 
ATOM   2381 N N    . ILE   A 1 302 ? 7.016   -22.228 -14.943 1.00 115.85 ? 302 ILE   A N    1 
ATOM   2382 C CA   . ILE   A 1 302 ? 6.319   -22.749 -16.110 1.00 118.91 ? 302 ILE   A CA   1 
ATOM   2383 C C    . ILE   A 1 302 ? 6.960   -22.175 -17.364 1.00 118.63 ? 302 ILE   A C    1 
ATOM   2384 O O    . ILE   A 1 302 ? 7.758   -21.241 -17.318 1.00 118.52 ? 302 ILE   A O    1 
ATOM   2385 C CB   . ILE   A 1 302 ? 4.769   -22.436 -16.173 1.00 117.96 ? 302 ILE   A CB   1 
ATOM   2386 C CG1  . ILE   A 1 302 ? 4.165   -21.377 -15.227 1.00 107.95 ? 302 ILE   A CG1  1 
ATOM   2387 C CG2  . ILE   A 1 302 ? 3.954   -23.721 -16.095 1.00 121.56 ? 302 ILE   A CG2  1 
ATOM   2388 C CD1  . ILE   A 1 302 ? 4.920   -20.921 -14.103 1.00 116.99 ? 302 ILE   A CD1  1 
ATOM   2389 N N    . GLU   A 1 303 ? 6.629   -22.765 -18.501 1.00 105.61 ? 303 GLU   A N    1 
ATOM   2390 C CA   . GLU   A 1 303 ? 6.734   -22.060 -19.764 1.00 110.68 ? 303 GLU   A CA   1 
ATOM   2391 C C    . GLU   A 1 303 ? 5.337   -21.563 -20.127 1.00 108.34 ? 303 GLU   A C    1 
ATOM   2392 O O    . GLU   A 1 303 ? 4.336   -21.949 -19.516 1.00 105.75 ? 303 GLU   A O    1 
ATOM   2393 C CB   . GLU   A 1 303 ? 7.368   -22.943 -20.841 1.00 109.31 ? 303 GLU   A CB   1 
ATOM   2394 C CG   . GLU   A 1 303 ? 8.892   -22.833 -20.803 1.00 113.79 ? 303 GLU   A CG   1 
ATOM   2395 C CD   . GLU   A 1 303 ? 9.620   -24.157 -20.991 1.00 123.99 ? 303 GLU   A CD   1 
ATOM   2396 O OE1  . GLU   A 1 303 ? 9.251   -24.934 -21.902 1.00 127.88 ? 303 GLU   A OE1  1 
ATOM   2397 O OE2  . GLU   A 1 303 ? 10.564  -24.418 -20.206 1.00 121.79 ? 303 GLU   A OE2  1 
ATOM   2398 N N    . ALA   A 1 304 ? 5.269   -20.705 -21.137 1.00 103.25 ? 304 ALA   A N    1 
ATOM   2399 C CA   . ALA   A 1 304 ? 4.026   -19.996 -21.414 1.00 100.70 ? 304 ALA   A CA   1 
ATOM   2400 C C    . ALA   A 1 304 ? 2.879   -20.964 -21.679 1.00 101.55 ? 304 ALA   A C    1 
ATOM   2401 O O    . ALA   A 1 304 ? 3.007   -21.897 -22.479 1.00 106.64 ? 304 ALA   A O    1 
ATOM   2402 C CB   . ALA   A 1 304 ? 4.214   -19.060 -22.608 1.00 101.67 ? 304 ALA   A CB   1 
ATOM   2403 N N    . LEU   A 1 305 ? 1.745   -20.731 -21.010 1.00 79.68  ? 305 LEU   A N    1 
ATOM   2404 C CA   . LEU   A 1 305 ? 0.586   -21.598 -21.195 1.00 79.63  ? 305 LEU   A CA   1 
ATOM   2405 C C    . LEU   A 1 305 ? -0.040  -21.414 -22.576 1.00 84.37  ? 305 LEU   A C    1 
ATOM   2406 O O    . LEU   A 1 305 ? -0.811  -22.276 -23.014 1.00 84.66  ? 305 LEU   A O    1 
ATOM   2407 C CB   . LEU   A 1 305 ? -0.465  -21.332 -20.110 1.00 78.41  ? 305 LEU   A CB   1 
ATOM   2408 C CG   . LEU   A 1 305 ? -0.097  -21.430 -18.616 1.00 75.83  ? 305 LEU   A CG   1 
ATOM   2409 C CD1  . LEU   A 1 305 ? -1.355  -21.369 -17.763 1.00 73.47  ? 305 LEU   A CD1  1 
ATOM   2410 C CD2  . LEU   A 1 305 ? 0.712   -22.684 -18.288 1.00 79.01  ? 305 LEU   A CD2  1 
ATOM   2411 N N    . SER   A 1 306 ? 0.277   -20.317 -23.266 1.00 100.91 ? 306 SER   A N    1 
ATOM   2412 C CA   . SER   A 1 306 ? -0.238  -20.039 -24.603 1.00 97.53  ? 306 SER   A CA   1 
ATOM   2413 C C    . SER   A 1 306 ? 0.800   -19.240 -25.381 1.00 98.52  ? 306 SER   A C    1 
ATOM   2414 O O    . SER   A 1 306 ? 1.661   -18.573 -24.801 1.00 100.65 ? 306 SER   A O    1 
ATOM   2415 C CB   . SER   A 1 306 ? -1.566  -19.276 -24.546 1.00 97.10  ? 306 SER   A CB   1 
ATOM   2416 O OG   . SER   A 1 306 ? -1.388  -17.986 -23.974 1.00 94.11  ? 306 SER   A OG   1 
ATOM   2417 N N    . SER   A 1 307 ? 0.713   -19.319 -26.706 1.00 125.08 ? 307 SER   A N    1 
ATOM   2418 C CA   . SER   A 1 307 ? 1.713   -18.717 -27.576 1.00 127.88 ? 307 SER   A CA   1 
ATOM   2419 C C    . SER   A 1 307 ? 1.044   -18.305 -28.878 1.00 131.45 ? 307 SER   A C    1 
ATOM   2420 O O    . SER   A 1 307 ? 0.075   -18.929 -29.320 1.00 131.19 ? 307 SER   A O    1 
ATOM   2421 C CB   . SER   A 1 307 ? 2.900   -19.654 -27.833 1.00 129.48 ? 307 SER   A CB   1 
ATOM   2422 O OG   . SER   A 1 307 ? 3.951   -19.374 -26.920 1.00 136.72 ? 307 SER   A OG   1 
ATOM   2423 N N    . GLY   A 1 308 ? 1.594   -17.268 -29.502 1.00 104.61 ? 308 GLY   A N    1 
ATOM   2424 C CA   . GLY   A 1 308 ? 0.952   -16.641 -30.646 1.00 96.02  ? 308 GLY   A CA   1 
ATOM   2425 C C    . GLY   A 1 308 ? -0.432  -16.107 -30.346 1.00 97.55  ? 308 GLY   A C    1 
ATOM   2426 O O    . GLY   A 1 308 ? -1.366  -16.334 -31.125 1.00 98.92  ? 308 GLY   A O    1 
ATOM   2427 N N    . ASN   A 1 309 ? -0.595  -15.429 -29.208 1.00 110.77 ? 309 ASN   A N    1 
ATOM   2428 C CA   . ASN   A 1 309 ? -1.874  -14.825 -28.872 1.00 105.63 ? 309 ASN   A CA   1 
ATOM   2429 C C    . ASN   A 1 309 ? -2.121  -13.587 -29.736 1.00 105.03 ? 309 ASN   A C    1 
ATOM   2430 O O    . ASN   A 1 309 ? -1.197  -12.975 -30.284 1.00 100.63 ? 309 ASN   A O    1 
ATOM   2431 C CB   . ASN   A 1 309 ? -1.943  -14.442 -27.389 1.00 106.84 ? 309 ASN   A CB   1 
ATOM   2432 C CG   . ASN   A 1 309 ? -1.527  -15.579 -26.450 1.00 111.52 ? 309 ASN   A CG   1 
ATOM   2433 O OD1  . ASN   A 1 309 ? -2.214  -16.600 -26.346 1.00 110.66 ? 309 ASN   A OD1  1 
ATOM   2434 N ND2  . ASN   A 1 309 ? -0.433  -15.373 -25.716 1.00 108.31 ? 309 ASN   A ND2  1 
ATOM   2435 N N    . LYS   A 1 310 ? -3.396  -13.217 -29.844 1.00 92.31  ? 310 LYS   A N    1 
ATOM   2436 C CA   . LYS   A 1 310 ? -3.798  -11.893 -30.316 1.00 85.56  ? 310 LYS   A CA   1 
ATOM   2437 C C    . LYS   A 1 310 ? -3.837  -10.995 -29.079 1.00 86.30  ? 310 LYS   A C    1 
ATOM   2438 O O    . LYS   A 1 310 ? -4.830  -10.932 -28.352 1.00 82.99  ? 310 LYS   A O    1 
ATOM   2439 C CB   . LYS   A 1 310 ? -5.142  -11.960 -31.035 1.00 84.70  ? 310 LYS   A CB   1 
ATOM   2440 C CG   . LYS   A 1 310 ? -5.079  -12.722 -32.352 1.00 95.26  ? 310 LYS   A CG   1 
ATOM   2441 C CD   . LYS   A 1 310 ? -6.427  -12.825 -33.076 1.00 98.08  ? 310 LYS   A CD   1 
ATOM   2442 C CE   . LYS   A 1 310 ? -7.112  -11.469 -33.224 1.00 92.55  ? 310 LYS   A CE   1 
ATOM   2443 N NZ   . LYS   A 1 310 ? -8.125  -11.484 -34.337 1.00 91.48  ? 310 LYS   A NZ   1 
ATOM   2444 N N    . GLU   A 1 311 ? -2.721  -10.328 -28.815 1.00 80.62  ? 311 GLU   A N    1 
ATOM   2445 C CA   . GLU   A 1 311 ? -2.625  -9.363  -27.738 1.00 82.14  ? 311 GLU   A CA   1 
ATOM   2446 C C    . GLU   A 1 311 ? -2.989  -7.961  -28.225 1.00 83.33  ? 311 GLU   A C    1 
ATOM   2447 O O    . GLU   A 1 311 ? -2.912  -7.646  -29.412 1.00 85.80  ? 311 GLU   A O    1 
ATOM   2448 C CB   . GLU   A 1 311 ? -1.216  -9.388  -27.133 1.00 82.05  ? 311 GLU   A CB   1 
ATOM   2449 C CG   . GLU   A 1 311 ? -0.797  -10.795 -26.688 1.00 85.91  ? 311 GLU   A CG   1 
ATOM   2450 C CD   . GLU   A 1 311 ? 0.600   -10.876 -26.095 1.00 85.08  ? 311 GLU   A CD   1 
ATOM   2451 O OE1  . GLU   A 1 311 ? 0.934   -11.952 -25.534 1.00 83.44  ? 311 GLU   A OE1  1 
ATOM   2452 O OE2  . GLU   A 1 311 ? 1.348   -9.876  -26.187 1.00 85.12  ? 311 GLU   A OE2  1 
ATOM   2453 N N    . PHE   A 1 312 ? -3.402  -7.119  -27.280 1.00 84.86  ? 312 PHE   A N    1 
ATOM   2454 C CA   . PHE   A 1 312 ? -3.820  -5.756  -27.591 1.00 83.20  ? 312 PHE   A CA   1 
ATOM   2455 C C    . PHE   A 1 312 ? -3.637  -4.893  -26.351 1.00 79.29  ? 312 PHE   A C    1 
ATOM   2456 O O    . PHE   A 1 312 ? -3.602  -5.394  -25.232 1.00 80.90  ? 312 PHE   A O    1 
ATOM   2457 C CB   . PHE   A 1 312 ? -5.277  -5.711  -28.079 1.00 77.93  ? 312 PHE   A CB   1 
ATOM   2458 C CG   . PHE   A 1 312 ? -6.288  -6.094  -27.023 1.00 77.91  ? 312 PHE   A CG   1 
ATOM   2459 C CD1  . PHE   A 1 312 ? -6.783  -5.145  -26.130 1.00 75.08  ? 312 PHE   A CD1  1 
ATOM   2460 C CD2  . PHE   A 1 312 ? -6.739  -7.402  -26.918 1.00 77.54  ? 312 PHE   A CD2  1 
ATOM   2461 C CE1  . PHE   A 1 312 ? -7.703  -5.492  -25.170 1.00 73.10  ? 312 PHE   A CE1  1 
ATOM   2462 C CE2  . PHE   A 1 312 ? -7.665  -7.758  -25.950 1.00 77.36  ? 312 PHE   A CE2  1 
ATOM   2463 C CZ   . PHE   A 1 312 ? -8.144  -6.798  -25.073 1.00 73.48  ? 312 PHE   A CZ   1 
ATOM   2464 N N    . LYS   A 1 313 ? -3.561  -3.584  -26.549 1.00 78.05  ? 313 LYS   A N    1 
ATOM   2465 C CA   . LYS   A 1 313 ? -3.399  -2.668  -25.431 1.00 78.46  ? 313 LYS   A CA   1 
ATOM   2466 C C    . LYS   A 1 313 ? -4.767  -2.220  -24.937 1.00 74.73  ? 313 LYS   A C    1 
ATOM   2467 O O    . LYS   A 1 313 ? -5.664  -1.932  -25.734 1.00 72.00  ? 313 LYS   A O    1 
ATOM   2468 C CB   . LYS   A 1 313 ? -2.577  -1.449  -25.846 1.00 76.76  ? 313 LYS   A CB   1 
ATOM   2469 C CG   . LYS   A 1 313 ? -1.148  -1.782  -26.246 1.00 81.42  ? 313 LYS   A CG   1 
ATOM   2470 C CD   . LYS   A 1 313 ? -0.439  -2.511  -25.122 1.00 83.46  ? 313 LYS   A CD   1 
ATOM   2471 C CE   . LYS   A 1 313 ? 1.074   -2.433  -25.259 1.00 82.35  ? 313 LYS   A CE   1 
ATOM   2472 N NZ   . LYS   A 1 313 ? 1.761   -3.349  -24.296 1.00 86.38  ? 313 LYS   A NZ   1 
ATOM   2473 N N    . GLY   A 1 314 ? -4.928  -2.179  -23.618 1.00 70.56  ? 314 GLY   A N    1 
ATOM   2474 C CA   . GLY   A 1 314 ? -6.154  -1.627  -23.052 1.00 67.57  ? 314 GLY   A CA   1 
ATOM   2475 C C    . GLY   A 1 314 ? -5.914  -0.941  -21.729 1.00 70.03  ? 314 GLY   A C    1 
ATOM   2476 O O    . GLY   A 1 314 ? -5.211  -1.516  -20.906 1.00 68.93  ? 314 GLY   A O    1 
ATOM   2477 N N    . THR   A 1 315 ? -6.565  0.190   -21.454 1.00 66.75  ? 315 THR   A N    1 
ATOM   2478 C CA   . THR   A 1 315 ? -6.151  1.135   -20.413 1.00 65.35  ? 315 THR   A CA   1 
ATOM   2479 C C    . THR   A 1 315 ? -6.910  0.893   -19.105 1.00 60.44  ? 315 THR   A C    1 
ATOM   2480 O O    . THR   A 1 315 ? -8.141  1.001   -19.070 1.00 59.42  ? 315 THR   A O    1 
ATOM   2481 C CB   . THR   A 1 315 ? -6.371  2.585   -20.881 1.00 66.48  ? 315 THR   A CB   1 
ATOM   2482 O OG1  . THR   A 1 315 ? -5.491  2.910   -21.966 1.00 67.54  ? 315 THR   A OG1  1 
ATOM   2483 C CG2  . THR   A 1 315 ? -6.139  3.555   -19.755 1.00 62.46  ? 315 THR   A CG2  1 
ATOM   2484 N N    . VAL   A 1 316 ? -6.153  0.602   -18.038 1.00 62.26  ? 316 VAL   A N    1 
ATOM   2485 C CA   . VAL   A 1 316 ? -6.623  0.451   -16.647 1.00 58.52  ? 316 VAL   A CA   1 
ATOM   2486 C C    . VAL   A 1 316 ? -5.995  1.568   -15.818 1.00 58.46  ? 316 VAL   A C    1 
ATOM   2487 O O    . VAL   A 1 316 ? -4.774  1.585   -15.627 1.00 59.53  ? 316 VAL   A O    1 
ATOM   2488 C CB   . VAL   A 1 316 ? -6.236  -0.917  -16.050 1.00 58.13  ? 316 VAL   A CB   1 
ATOM   2489 C CG1  . VAL   A 1 316 ? -6.751  -1.084  -14.614 1.00 54.75  ? 316 VAL   A CG1  1 
ATOM   2490 C CG2  . VAL   A 1 316 ? -6.728  -2.055  -16.939 1.00 61.05  ? 316 VAL   A CG2  1 
ATOM   2491 N N    . PHE   A 1 317 ? -6.823  2.500   -15.331 1.00 55.90  ? 317 PHE   A N    1 
ATOM   2492 C CA   . PHE   A 1 317 ? -6.396  3.607   -14.465 1.00 55.53  ? 317 PHE   A CA   1 
ATOM   2493 C C    . PHE   A 1 317 ? -5.228  4.387   -15.068 1.00 59.32  ? 317 PHE   A C    1 
ATOM   2494 O O    . PHE   A 1 317 ? -4.270  4.745   -14.382 1.00 61.83  ? 317 PHE   A O    1 
ATOM   2495 C CB   . PHE   A 1 317 ? -6.040  3.086   -13.059 1.00 54.19  ? 317 PHE   A CB   1 
ATOM   2496 C CG   . PHE   A 1 317 ? -5.990  4.157   -11.979 1.00 54.55  ? 317 PHE   A CG   1 
ATOM   2497 C CD1  . PHE   A 1 317 ? -6.621  5.374   -12.142 1.00 54.92  ? 317 PHE   A CD1  1 
ATOM   2498 C CD2  . PHE   A 1 317 ? -5.325  3.916   -10.776 1.00 56.17  ? 317 PHE   A CD2  1 
ATOM   2499 C CE1  . PHE   A 1 317 ? -6.575  6.341   -11.154 1.00 58.19  ? 317 PHE   A CE1  1 
ATOM   2500 C CE2  . PHE   A 1 317 ? -5.278  4.882   -9.774  1.00 57.85  ? 317 PHE   A CE2  1 
ATOM   2501 C CZ   . PHE   A 1 317 ? -5.907  6.097   -9.964  1.00 57.58  ? 317 PHE   A CZ   1 
ATOM   2502 N N    . PHE   A 1 318 ? -5.329  4.698   -16.364 1.00 66.20  ? 318 PHE   A N    1 
ATOM   2503 C CA   . PHE   A 1 318 ? -4.312  5.465   -17.088 1.00 64.57  ? 318 PHE   A CA   1 
ATOM   2504 C C    . PHE   A 1 318 ? -2.995  4.714   -17.234 1.00 70.67  ? 318 PHE   A C    1 
ATOM   2505 O O    . PHE   A 1 318 ? -1.980  5.294   -17.683 1.00 72.89  ? 318 PHE   A O    1 
ATOM   2506 C CB   . PHE   A 1 318 ? -4.046  6.826   -16.429 1.00 66.55  ? 318 PHE   A CB   1 
ATOM   2507 C CG   . PHE   A 1 318 ? -5.292  7.642   -16.132 1.00 68.72  ? 318 PHE   A CG   1 
ATOM   2508 C CD1  . PHE   A 1 318 ? -6.018  8.259   -17.141 1.00 65.24  ? 318 PHE   A CD1  1 
ATOM   2509 C CD2  . PHE   A 1 318 ? -5.728  7.806   -14.817 1.00 71.25  ? 318 PHE   A CD2  1 
ATOM   2510 C CE1  . PHE   A 1 318 ? -7.156  9.008   -16.855 1.00 64.80  ? 318 PHE   A CE1  1 
ATOM   2511 C CE2  . PHE   A 1 318 ? -6.860  8.557   -14.531 1.00 67.25  ? 318 PHE   A CE2  1 
ATOM   2512 C CZ   . PHE   A 1 318 ? -7.575  9.153   -15.552 1.00 68.88  ? 318 PHE   A CZ   1 
ATOM   2513 N N    . ASP   A 1 319 ? -3.005  3.423   -16.936 1.00 68.75  ? 319 ASP   A N    1 
ATOM   2514 C CA   . ASP   A 1 319 ? -1.861  2.547   -17.120 1.00 70.27  ? 319 ASP   A CA   1 
ATOM   2515 C C    . ASP   A 1 319 ? -2.214  1.671   -18.330 1.00 73.57  ? 319 ASP   A C    1 
ATOM   2516 O O    . ASP   A 1 319 ? -3.354  1.159   -18.437 1.00 69.40  ? 319 ASP   A O    1 
ATOM   2517 C CB   . ASP   A 1 319 ? -1.551  1.713   -15.850 1.00 68.14  ? 319 ASP   A CB   1 
ATOM   2518 C CG   . ASP   A 1 319 ? -1.069  2.624   -14.643 1.00 73.07  ? 319 ASP   A CG   1 
ATOM   2519 O OD1  . ASP   A 1 319 ? -0.337  3.620   -14.892 1.00 74.51  ? 319 ASP   A OD1  1 
ATOM   2520 O OD2  . ASP   A 1 319 ? -1.494  2.400   -13.462 1.00 71.13  ? 319 ASP   A OD2  1 
ATOM   2521 N N    . GLU   A 1 320 ? -1.271  1.491   -19.252 1.00 114.30 ? 320 GLU   A N    1 
ATOM   2522 C CA   . GLU   A 1 320 ? -1.619  0.733   -20.482 1.00 112.37 ? 320 GLU   A CA   1 
ATOM   2523 C C    . GLU   A 1 320 ? -1.217  -0.739  -20.319 1.00 109.76 ? 320 GLU   A C    1 
ATOM   2524 O O    . GLU   A 1 320 ? -0.016  -1.043  -20.495 1.00 110.50 ? 320 GLU   A O    1 
ATOM   2525 C CB   . GLU   A 1 320 ? -0.935  1.353   -21.698 1.00 116.38 ? 320 GLU   A CB   1 
ATOM   2526 C CG   . GLU   A 1 320 ? -1.554  0.914   -23.021 1.00 124.96 ? 320 GLU   A CG   1 
ATOM   2527 C CD   . GLU   A 1 320 ? -0.637  1.169   -24.201 1.00 123.49 ? 320 GLU   A CD   1 
ATOM   2528 O OE1  . GLU   A 1 320 ? 0.563   0.843   -24.092 1.00 119.69 ? 320 GLU   A OE1  1 
ATOM   2529 O OE2  . GLU   A 1 320 ? -1.120  1.694   -25.226 1.00 131.19 ? 320 GLU   A OE2  1 
ATOM   2530 N N    . PHE   A 1 321 ? -2.173  -1.619  -20.000 1.00 69.02  ? 321 PHE   A N    1 
ATOM   2531 C CA   . PHE   A 1 321 ? -1.816  -3.035  -19.942 1.00 68.75  ? 321 PHE   A CA   1 
ATOM   2532 C C    . PHE   A 1 321 ? -1.735  -3.725  -21.326 1.00 71.43  ? 321 PHE   A C    1 
ATOM   2533 O O    . PHE   A 1 321 ? -2.368  -3.317  -22.326 1.00 69.95  ? 321 PHE   A O    1 
ATOM   2534 C CB   . PHE   A 1 321 ? -2.779  -3.866  -19.075 1.00 66.32  ? 321 PHE   A CB   1 
ATOM   2535 C CG   . PHE   A 1 321 ? -2.683  -3.622  -17.562 1.00 66.62  ? 321 PHE   A CG   1 
ATOM   2536 C CD1  . PHE   A 1 321 ? -2.752  -2.336  -17.100 1.00 64.40  ? 321 PHE   A CD1  1 
ATOM   2537 C CD2  . PHE   A 1 321 ? -2.667  -4.672  -16.614 1.00 64.21  ? 321 PHE   A CD2  1 
ATOM   2538 C CE1  . PHE   A 1 321 ? -2.736  -2.051  -15.772 1.00 63.44  ? 321 PHE   A CE1  1 
ATOM   2539 C CE2  . PHE   A 1 321 ? -2.656  -4.386  -15.236 1.00 63.28  ? 321 PHE   A CE2  1 
ATOM   2540 C CZ   . PHE   A 1 321 ? -2.686  -3.060  -14.830 1.00 61.10  ? 321 PHE   A CZ   1 
ATOM   2541 N N    . THR   A 1 322 ? -0.957  -4.825  -21.378 1.00 73.65  ? 322 THR   A N    1 
ATOM   2542 C CA   . THR   A 1 322 ? -1.006  -5.758  -22.521 1.00 71.88  ? 322 THR   A CA   1 
ATOM   2543 C C    . THR   A 1 322 ? -2.014  -6.863  -22.197 1.00 73.06  ? 322 THR   A C    1 
ATOM   2544 O O    . THR   A 1 322 ? -1.848  -7.597  -21.210 1.00 69.39  ? 322 THR   A O    1 
ATOM   2545 C CB   . THR   A 1 322 ? 0.363   -6.372  -22.869 1.00 73.77  ? 322 THR   A CB   1 
ATOM   2546 O OG1  . THR   A 1 322 ? 1.305   -5.347  -23.216 1.00 75.61  ? 322 THR   A OG1  1 
ATOM   2547 C CG2  . THR   A 1 322 ? 0.236   -7.328  -24.103 1.00 72.48  ? 322 THR   A CG2  1 
ATOM   2548 N N    . PHE   A 1 323 ? -3.056  -6.978  -23.022 1.00 74.04  ? 323 PHE   A N    1 
ATOM   2549 C CA   . PHE   A 1 323 ? -4.169  -7.888  -22.794 1.00 75.66  ? 323 PHE   A CA   1 
ATOM   2550 C C    . PHE   A 1 323 ? -4.216  -8.996  -23.845 1.00 73.67  ? 323 PHE   A C    1 
ATOM   2551 O O    . PHE   A 1 323 ? -3.827  -8.805  -24.996 1.00 77.33  ? 323 PHE   A O    1 
ATOM   2552 C CB   . PHE   A 1 323 ? -5.522  -7.157  -22.812 1.00 74.95  ? 323 PHE   A CB   1 
ATOM   2553 C CG   . PHE   A 1 323 ? -5.793  -6.304  -21.592 1.00 72.11  ? 323 PHE   A CG   1 
ATOM   2554 C CD1  . PHE   A 1 323 ? -5.332  -5.006  -21.538 1.00 72.28  ? 323 PHE   A CD1  1 
ATOM   2555 C CD2  . PHE   A 1 323 ? -6.525  -6.788  -20.527 1.00 69.97  ? 323 PHE   A CD2  1 
ATOM   2556 C CE1  . PHE   A 1 323 ? -5.581  -4.211  -20.456 1.00 73.34  ? 323 PHE   A CE1  1 
ATOM   2557 C CE2  . PHE   A 1 323 ? -6.779  -5.994  -19.436 1.00 67.56  ? 323 PHE   A CE2  1 
ATOM   2558 C CZ   . PHE   A 1 323 ? -6.303  -4.697  -19.399 1.00 71.19  ? 323 PHE   A CZ   1 
ATOM   2559 N N    . VAL   A 1 324 ? -4.705  -10.164 -23.430 1.00 75.88  ? 324 VAL   A N    1 
ATOM   2560 C CA   . VAL   A 1 324 ? -5.173  -11.205 -24.337 1.00 76.11  ? 324 VAL   A CA   1 
ATOM   2561 C C    . VAL   A 1 324 ? -6.614  -11.524 -23.967 1.00 73.71  ? 324 VAL   A C    1 
ATOM   2562 O O    . VAL   A 1 324 ? -6.949  -11.665 -22.781 1.00 76.27  ? 324 VAL   A O    1 
ATOM   2563 C CB   . VAL   A 1 324 ? -4.297  -12.473 -24.303 1.00 76.67  ? 324 VAL   A CB   1 
ATOM   2564 C CG1  . VAL   A 1 324 ? -4.168  -13.004 -22.893 1.00 74.99  ? 324 VAL   A CG1  1 
ATOM   2565 C CG2  . VAL   A 1 324 ? -4.879  -13.538 -25.212 1.00 76.61  ? 324 VAL   A CG2  1 
ATOM   2566 N N    . LYS   A 1 325 ? -7.465  -11.597 -24.978 1.00 81.27  ? 325 LYS   A N    1 
ATOM   2567 C CA   . LYS   A 1 325 ? -8.873  -11.859 -24.753 1.00 79.30  ? 325 LYS   A CA   1 
ATOM   2568 C C    . LYS   A 1 325 ? -9.091  -13.325 -24.418 1.00 79.29  ? 325 LYS   A C    1 
ATOM   2569 O O    . LYS   A 1 325 ? -8.444  -14.210 -24.978 1.00 82.78  ? 325 LYS   A O    1 
ATOM   2570 C CB   . LYS   A 1 325 ? -9.668  -11.458 -25.987 1.00 80.49  ? 325 LYS   A CB   1 
ATOM   2571 C CG   . LYS   A 1 325 ? -11.148 -11.309 -25.769 1.00 77.90  ? 325 LYS   A CG   1 
ATOM   2572 C CD   . LYS   A 1 325 ? -11.847 -11.893 -26.966 1.00 79.64  ? 325 LYS   A CD   1 
ATOM   2573 C CE   . LYS   A 1 325 ? -13.314 -11.551 -26.954 1.00 85.48  ? 325 LYS   A CE   1 
ATOM   2574 N NZ   . LYS   A 1 325 ? -14.152 -12.781 -26.858 1.00 89.35  ? 325 LYS   A NZ   1 
ATOM   2575 N N    . LEU   A 1 326 ? -9.988  -13.579 -23.473 1.00 77.48  ? 326 LEU   A N    1 
ATOM   2576 C CA   . LEU   A 1 326 ? -10.347 -14.941 -23.115 1.00 79.12  ? 326 LEU   A CA   1 
ATOM   2577 C C    . LEU   A 1 326 ? -11.462 -15.394 -24.040 1.00 73.88  ? 326 LEU   A C    1 
ATOM   2578 O O    . LEU   A 1 326 ? -12.545 -14.802 -24.033 1.00 77.93  ? 326 LEU   A O    1 
ATOM   2579 C CB   . LEU   A 1 326 ? -10.798 -15.025 -21.657 1.00 71.96  ? 326 LEU   A CB   1 
ATOM   2580 C CG   . LEU   A 1 326 ? -9.753  -15.441 -20.634 1.00 73.89  ? 326 LEU   A CG   1 
ATOM   2581 C CD1  . LEU   A 1 326 ? -8.472  -14.635 -20.802 1.00 73.65  ? 326 LEU   A CD1  1 
ATOM   2582 C CD2  . LEU   A 1 326 ? -10.324 -15.304 -19.229 1.00 70.63  ? 326 LEU   A CD2  1 
ATOM   2583 N N    . THR   A 1 327 ? -11.212 -16.445 -24.815 1.00 77.18  ? 327 THR   A N    1 
ATOM   2584 C CA   . THR   A 1 327 ? -12.201 -16.882 -25.797 1.00 80.65  ? 327 THR   A CA   1 
ATOM   2585 C C    . THR   A 1 327 ? -12.977 -18.110 -25.334 1.00 82.33  ? 327 THR   A C    1 
ATOM   2586 O O    . THR   A 1 327 ? -14.210 -18.085 -25.285 1.00 83.72  ? 327 THR   A O    1 
ATOM   2587 C CB   . THR   A 1 327 ? -11.541 -17.156 -27.157 1.00 80.63  ? 327 THR   A CB   1 
ATOM   2588 O OG1  . THR   A 1 327 ? -10.453 -18.071 -27.003 1.00 81.67  ? 327 THR   A OG1  1 
ATOM   2589 C CG2  . THR   A 1 327 ? -11.011 -15.873 -27.749 1.00 85.12  ? 327 THR   A CG2  1 
ATOM   2590 N N    . GLY   A 1 328 ? -12.286 -19.175 -24.952 1.00 80.43  ? 328 GLY   A N    1 
ATOM   2591 C CA   . GLY   A 1 328 ? -12.985 -20.362 -24.519 1.00 85.62  ? 328 GLY   A CA   1 
ATOM   2592 C C    . GLY   A 1 328 ? -13.659 -20.159 -23.178 1.00 79.24  ? 328 GLY   A C    1 
ATOM   2593 O O    . GLY   A 1 328 ? -13.287 -19.294 -22.390 1.00 80.68  ? 328 GLY   A O    1 
ATOM   2594 N N    . VAL   A 1 329 ? -14.684 -20.981 -22.929 1.00 83.09  ? 329 VAL   A N    1 
ATOM   2595 C CA   . VAL   A 1 329 ? -15.326 -21.046 -21.620 1.00 78.11  ? 329 VAL   A CA   1 
ATOM   2596 C C    . VAL   A 1 329 ? -14.349 -21.548 -20.571 1.00 77.32  ? 329 VAL   A C    1 
ATOM   2597 O O    . VAL   A 1 329 ? -14.563 -21.347 -19.372 1.00 78.97  ? 329 VAL   A O    1 
ATOM   2598 C CB   . VAL   A 1 329 ? -16.596 -21.929 -21.703 1.00 78.28  ? 329 VAL   A CB   1 
ATOM   2599 C CG1  . VAL   A 1 329 ? -16.265 -23.403 -21.511 1.00 79.11  ? 329 VAL   A CG1  1 
ATOM   2600 C CG2  . VAL   A 1 329 ? -17.643 -21.467 -20.715 1.00 80.20  ? 329 VAL   A CG2  1 
ATOM   2601 N N    . ALA   A 1 330 ? -13.251 -22.162 -21.006 1.00 82.36  ? 330 ALA   A N    1 
ATOM   2602 C CA   . ALA   A 1 330 ? -12.149 -22.544 -20.136 1.00 80.46  ? 330 ALA   A CA   1 
ATOM   2603 C C    . ALA   A 1 330 ? -10.867 -22.415 -20.940 1.00 79.35  ? 330 ALA   A C    1 
ATOM   2604 O O    . ALA   A 1 330 ? -10.887 -22.448 -22.170 1.00 78.63  ? 330 ALA   A O    1 
ATOM   2605 C CB   . ALA   A 1 330 ? -12.310 -23.973 -19.599 1.00 77.91  ? 330 ALA   A CB   1 
ATOM   2606 N N    . GLY   A 1 331 ? -9.755  -22.223 -20.242 1.00 89.78  ? 331 GLY   A N    1 
ATOM   2607 C CA   . GLY   A 1 331 ? -8.501  -22.042 -20.957 1.00 85.05  ? 331 GLY   A CA   1 
ATOM   2608 C C    . GLY   A 1 331 ? -7.309  -21.860 -20.042 1.00 87.90  ? 331 GLY   A C    1 
ATOM   2609 O O    . GLY   A 1 331 ? -7.441  -21.651 -18.826 1.00 86.17  ? 331 GLY   A O    1 
ATOM   2610 N N    . ASN   A 1 332 ? -6.133  -21.960 -20.666 1.00 75.39  ? 332 ASN   A N    1 
ATOM   2611 C CA   . ASN   A 1 332 ? -4.842  -21.634 -20.070 1.00 77.80  ? 332 ASN   A CA   1 
ATOM   2612 C C    . ASN   A 1 332 ? -4.191  -20.563 -20.943 1.00 81.43  ? 332 ASN   A C    1 
ATOM   2613 O O    . ASN   A 1 332 ? -3.912  -20.809 -22.125 1.00 85.04  ? 332 ASN   A O    1 
ATOM   2614 C CB   . ASN   A 1 332 ? -3.931  -22.870 -19.965 1.00 78.20  ? 332 ASN   A CB   1 
ATOM   2615 C CG   . ASN   A 1 332 ? -4.552  -24.019 -19.159 1.00 79.26  ? 332 ASN   A CG   1 
ATOM   2616 O OD1  . ASN   A 1 332 ? -4.926  -23.844 -18.001 1.00 79.26  ? 332 ASN   A OD1  1 
ATOM   2617 N ND2  . ASN   A 1 332 ? -4.610  -25.215 -19.760 1.00 81.21  ? 332 ASN   A ND2  1 
ATOM   2618 N N    . TYR   A 1 333 ? -3.952  -19.381 -20.367 1.00 73.51  ? 333 TYR   A N    1 
ATOM   2619 C CA   . TYR   A 1 333 ? -3.423  -18.221 -21.082 1.00 75.88  ? 333 TYR   A CA   1 
ATOM   2620 C C    . TYR   A 1 333 ? -2.215  -17.660 -20.344 1.00 74.42  ? 333 TYR   A C    1 
ATOM   2621 O O    . TYR   A 1 333 ? -2.183  -17.641 -19.108 1.00 75.41  ? 333 TYR   A O    1 
ATOM   2622 C CB   . TYR   A 1 333 ? -4.481  -17.089 -21.226 1.00 71.73  ? 333 TYR   A CB   1 
ATOM   2623 C CG   . TYR   A 1 333 ? -5.623  -17.383 -22.178 1.00 73.67  ? 333 TYR   A CG   1 
ATOM   2624 C CD1  . TYR   A 1 333 ? -5.532  -17.061 -23.535 1.00 71.96  ? 333 TYR   A CD1  1 
ATOM   2625 C CD2  . TYR   A 1 333 ? -6.797  -17.969 -21.722 1.00 72.10  ? 333 TYR   A CD2  1 
ATOM   2626 C CE1  . TYR   A 1 333 ? -6.582  -17.320 -24.400 1.00 71.26  ? 333 TYR   A CE1  1 
ATOM   2627 C CE2  . TYR   A 1 333 ? -7.847  -18.239 -22.575 1.00 73.39  ? 333 TYR   A CE2  1 
ATOM   2628 C CZ   . TYR   A 1 333 ? -7.738  -17.913 -23.913 1.00 75.40  ? 333 TYR   A CZ   1 
ATOM   2629 O OH   . TYR   A 1 333 ? -8.797  -18.183 -24.751 1.00 74.97  ? 333 TYR   A OH   1 
ATOM   2630 N N    . THR   A 1 334 ? -1.239  -17.165 -21.105 1.00 82.03  ? 334 THR   A N    1 
ATOM   2631 C CA   . THR   A 1 334 ? -0.085  -16.450 -20.570 1.00 80.91  ? 334 THR   A CA   1 
ATOM   2632 C C    . THR   A 1 334 ? 0.050   -15.120 -21.294 1.00 81.72  ? 334 THR   A C    1 
ATOM   2633 O O    . THR   A 1 334 ? -0.137  -15.052 -22.516 1.00 84.02  ? 334 THR   A O    1 
ATOM   2634 C CB   . THR   A 1 334 ? 1.211   -17.254 -20.728 1.00 84.03  ? 334 THR   A CB   1 
ATOM   2635 O OG1  . THR   A 1 334 ? 1.148   -18.435 -19.917 1.00 81.99  ? 334 THR   A OG1  1 
ATOM   2636 C CG2  . THR   A 1 334 ? 2.411   -16.410 -20.314 1.00 81.18  ? 334 THR   A CG2  1 
ATOM   2637 N N    . VAL   A 1 335 ? 0.388   -14.071 -20.548 1.00 95.38  ? 335 VAL   A N    1 
ATOM   2638 C CA   . VAL   A 1 335 ? 0.542   -12.729 -21.106 1.00 94.51  ? 335 VAL   A CA   1 
ATOM   2639 C C    . VAL   A 1 335 ? 1.740   -12.049 -20.467 1.00 96.16  ? 335 VAL   A C    1 
ATOM   2640 O O    . VAL   A 1 335 ? 1.874   -12.044 -19.241 1.00 95.07  ? 335 VAL   A O    1 
ATOM   2641 C CB   . VAL   A 1 335 ? -0.709  -11.863 -20.869 1.00 97.93  ? 335 VAL   A CB   1 
ATOM   2642 C CG1  . VAL   A 1 335 ? -0.759  -10.720 -21.879 1.00 101.69 ? 335 VAL   A CG1  1 
ATOM   2643 C CG2  . VAL   A 1 335 ? -1.949  -12.711 -20.940 1.00 95.39  ? 335 VAL   A CG2  1 
ATOM   2644 N N    . CYS   A 1 336 ? 2.561   -11.391 -21.277 1.00 74.62  ? 336 CYS   A N    1 
ATOM   2645 C CA   . CYS   A 1 336 ? 3.784   -10.790 -20.765 1.00 79.55  ? 336 CYS   A CA   1 
ATOM   2646 C C    . CYS   A 1 336 ? 3.886   -9.332  -21.199 1.00 77.46  ? 336 CYS   A C    1 
ATOM   2647 O O    . CYS   A 1 336 ? 3.369   -8.939  -22.249 1.00 79.80  ? 336 CYS   A O    1 
ATOM   2648 C CB   . CYS   A 1 336 ? 5.031   -11.573 -21.228 1.00 78.24  ? 336 CYS   A CB   1 
ATOM   2649 S SG   . CYS   A 1 336 ? 4.995   -13.349 -20.806 1.00 81.37  ? 336 CYS   A SG   1 
ATOM   2650 N N    . GLN   A 1 337 ? 4.551   -8.536  -20.359 1.00 79.25  ? 337 GLN   A N    1 
ATOM   2651 C CA   . GLN   A 1 337 ? 4.958   -7.173  -20.685 1.00 77.21  ? 337 GLN   A CA   1 
ATOM   2652 C C    . GLN   A 1 337 ? 6.239   -6.871  -19.917 1.00 80.74  ? 337 GLN   A C    1 
ATOM   2653 O O    . GLN   A 1 337 ? 6.291   -7.054  -18.691 1.00 77.56  ? 337 GLN   A O    1 
ATOM   2654 C CB   . GLN   A 1 337 ? 3.869   -6.140  -20.354 1.00 75.46  ? 337 GLN   A CB   1 
ATOM   2655 C CG   . GLN   A 1 337 ? 4.316   -4.684  -20.541 1.00 73.40  ? 337 GLN   A CG   1 
ATOM   2656 C CD   . GLN   A 1 337 ? 3.243   -3.687  -20.131 1.00 77.90  ? 337 GLN   A CD   1 
ATOM   2657 O OE1  . GLN   A 1 337 ? 3.445   -2.849  -19.240 1.00 76.47  ? 337 GLN   A OE1  1 
ATOM   2658 N NE2  . GLN   A 1 337 ? 2.089   -3.777  -20.781 1.00 76.50  ? 337 GLN   A NE2  1 
ATOM   2659 N N    . LYS   A 1 338 ? 7.263   -6.419  -20.650 1.00 78.63  ? 338 LYS   A N    1 
ATOM   2660 C CA   . LYS   A 1 338 ? 8.608   -6.190  -20.131 1.00 81.34  ? 338 LYS   A CA   1 
ATOM   2661 C C    . LYS   A 1 338 ? 9.076   -7.376  -19.288 1.00 83.49  ? 338 LYS   A C    1 
ATOM   2662 O O    . LYS   A 1 338 ? 9.375   -8.445  -19.835 1.00 80.41  ? 338 LYS   A O    1 
ATOM   2663 C CB   . LYS   A 1 338 ? 8.659   -4.878  -19.344 1.00 82.89  ? 338 LYS   A CB   1 
ATOM   2664 C CG   . LYS   A 1 338 ? 8.196   -3.633  -20.114 1.00 81.77  ? 338 LYS   A CG   1 
ATOM   2665 C CD   . LYS   A 1 338 ? 9.041   -2.421  -19.705 1.00 87.77  ? 338 LYS   A CD   1 
ATOM   2666 C CE   . LYS   A 1 338 ? 8.178   -1.350  -19.011 1.00 86.08  ? 338 LYS   A CE   1 
ATOM   2667 N NZ   . LYS   A 1 338 ? 8.879   -0.599  -17.912 1.00 82.40  ? 338 LYS   A NZ   1 
ATOM   2668 N N    . ASP   A 1 339 ? 9.189   -7.184  -17.962 1.00 79.98  ? 339 ASP   A N    1 
ATOM   2669 C CA   . ASP   A 1 339 ? 9.724   -8.183  -17.034 1.00 75.29  ? 339 ASP   A CA   1 
ATOM   2670 C C    . ASP   A 1 339 ? 8.666   -9.079  -16.396 1.00 75.41  ? 339 ASP   A C    1 
ATOM   2671 O O    . ASP   A 1 339 ? 9.029   -9.987  -15.639 1.00 73.39  ? 339 ASP   A O    1 
ATOM   2672 C CB   . ASP   A 1 339 ? 10.504  -7.502  -15.908 1.00 79.17  ? 339 ASP   A CB   1 
ATOM   2673 C CG   . ASP   A 1 339 ? 11.831  -6.926  -16.365 1.00 83.32  ? 339 ASP   A CG   1 
ATOM   2674 O OD1  . ASP   A 1 339 ? 12.311  -7.275  -17.457 1.00 85.13  ? 339 ASP   A OD1  1 
ATOM   2675 O OD2  . ASP   A 1 339 ? 12.404  -6.116  -15.604 1.00 96.25  ? 339 ASP   A OD2  1 
ATOM   2676 N N    . LEU   A 1 340 ? 7.381   -8.837  -16.640 1.00 80.38  ? 340 LEU   A N    1 
ATOM   2677 C CA   . LEU   A 1 340 ? 6.313   -9.521  -15.919 1.00 80.00  ? 340 LEU   A CA   1 
ATOM   2678 C C    . LEU   A 1 340 ? 5.532   -10.431 -16.861 1.00 77.80  ? 340 LEU   A C    1 
ATOM   2679 O O    . LEU   A 1 340 ? 4.993   -9.968  -17.873 1.00 77.24  ? 340 LEU   A O    1 
ATOM   2680 C CB   . LEU   A 1 340 ? 5.371   -8.518  -15.251 1.00 77.50  ? 340 LEU   A CB   1 
ATOM   2681 C CG   . LEU   A 1 340 ? 4.205   -9.162  -14.492 1.00 75.33  ? 340 LEU   A CG   1 
ATOM   2682 C CD1  . LEU   A 1 340 ? 4.573   -9.381  -13.039 1.00 72.92  ? 340 LEU   A CD1  1 
ATOM   2683 C CD2  . LEU   A 1 340 ? 2.946   -8.322  -14.615 1.00 74.27  ? 340 LEU   A CD2  1 
ATOM   2684 N N    . CYS   A 1 341 ? 5.443   -11.713 -16.506 1.00 86.97  ? 341 CYS   A N    1 
ATOM   2685 C CA   . CYS   A 1 341 ? 4.571   -12.661 -17.188 1.00 88.83  ? 341 CYS   A CA   1 
ATOM   2686 C C    . CYS   A 1 341 ? 3.491   -13.129 -16.223 1.00 84.45  ? 341 CYS   A C    1 
ATOM   2687 O O    . CYS   A 1 341 ? 3.764   -13.424 -15.057 1.00 86.92  ? 341 CYS   A O    1 
ATOM   2688 C CB   . CYS   A 1 341 ? 5.335   -13.882 -17.747 1.00 88.11  ? 341 CYS   A CB   1 
ATOM   2689 S SG   . CYS   A 1 341 ? 6.308   -13.599 -19.257 1.00 94.11  ? 341 CYS   A SG   1 
ATOM   2690 N N    . CYS   A 1 342 ? 2.272   -13.213 -16.740 1.00 71.12  ? 342 CYS   A N    1 
ATOM   2691 C CA   . CYS   A 1 342 ? 1.067   -13.531 -15.998 1.00 70.46  ? 342 CYS   A CA   1 
ATOM   2692 C C    . CYS   A 1 342 ? 0.444   -14.797 -16.565 1.00 71.86  ? 342 CYS   A C    1 
ATOM   2693 O O    . CYS   A 1 342 ? 0.173   -14.871 -17.768 1.00 76.17  ? 342 CYS   A O    1 
ATOM   2694 C CB   . CYS   A 1 342 ? 0.088   -12.360 -16.099 1.00 70.18  ? 342 CYS   A CB   1 
ATOM   2695 S SG   . CYS   A 1 342 ? 0.841   -10.770 -15.652 1.00 69.80  ? 342 CYS   A SG   1 
ATOM   2696 N N    . HIS   A 1 343 ? 0.183   -15.768 -15.697 1.00 79.61  ? 343 HIS   A N    1 
ATOM   2697 C CA   . HIS   A 1 343 ? -0.405  -17.045 -16.072 1.00 81.25  ? 343 HIS   A CA   1 
ATOM   2698 C C    . HIS   A 1 343 ? -1.797  -17.158 -15.472 1.00 78.48  ? 343 HIS   A C    1 
ATOM   2699 O O    . HIS   A 1 343 ? -2.000  -16.799 -14.302 1.00 79.86  ? 343 HIS   A O    1 
ATOM   2700 C CB   . HIS   A 1 343 ? 0.466   -18.210 -15.598 1.00 83.45  ? 343 HIS   A CB   1 
ATOM   2701 C CG   . HIS   A 1 343 ? 1.918   -18.045 -15.917 1.00 87.79  ? 343 HIS   A CG   1 
ATOM   2702 N ND1  . HIS   A 1 343 ? 2.472   -18.462 -17.110 1.00 85.52  ? 343 HIS   A ND1  1 
ATOM   2703 C CD2  . HIS   A 1 343 ? 2.932   -17.507 -15.199 1.00 86.29  ? 343 HIS   A CD2  1 
ATOM   2704 C CE1  . HIS   A 1 343 ? 3.764   -18.185 -17.113 1.00 86.83  ? 343 HIS   A CE1  1 
ATOM   2705 N NE2  . HIS   A 1 343 ? 4.069   -17.607 -15.965 1.00 89.63  ? 343 HIS   A NE2  1 
ATOM   2706 N N    . LEU   A 1 344 ? -2.757  -17.613 -16.284 1.00 65.68  ? 344 LEU   A N    1 
ATOM   2707 C CA   . LEU   A 1 344 ? -4.119  -17.872 -15.838 1.00 65.53  ? 344 LEU   A CA   1 
ATOM   2708 C C    . LEU   A 1 344 ? -4.612  -19.221 -16.347 1.00 69.53  ? 344 LEU   A C    1 
ATOM   2709 O O    . LEU   A 1 344 ? -4.420  -19.567 -17.518 1.00 69.78  ? 344 LEU   A O    1 
ATOM   2710 C CB   . LEU   A 1 344 ? -5.088  -16.777 -16.310 1.00 65.84  ? 344 LEU   A CB   1 
ATOM   2711 C CG   . LEU   A 1 344 ? -6.561  -17.037 -15.974 1.00 64.69  ? 344 LEU   A CG   1 
ATOM   2712 C CD1  . LEU   A 1 344 ? -6.784  -16.906 -14.471 1.00 62.16  ? 344 LEU   A CD1  1 
ATOM   2713 C CD2  . LEU   A 1 344 ? -7.469  -16.084 -16.726 1.00 67.38  ? 344 LEU   A CD2  1 
ATOM   2714 N N    . SER   A 1 345 ? -5.248  -19.980 -15.460 1.00 75.33  ? 345 SER   A N    1 
ATOM   2715 C CA   . SER   A 1 345 ? -6.048  -21.143 -15.837 1.00 77.67  ? 345 SER   A CA   1 
ATOM   2716 C C    . SER   A 1 345 ? -7.454  -20.914 -15.302 1.00 76.62  ? 345 SER   A C    1 
ATOM   2717 O O    . SER   A 1 345 ? -7.618  -20.335 -14.235 1.00 77.07  ? 345 SER   A O    1 
ATOM   2718 C CB   . SER   A 1 345 ? -5.470  -22.445 -15.283 1.00 78.79  ? 345 SER   A CB   1 
ATOM   2719 O OG   . SER   A 1 345 ? -4.119  -22.611 -15.672 1.00 81.18  ? 345 SER   A OG   1 
ATOM   2720 N N    . TYR   A 1 346 ? -8.475  -21.281 -16.061 1.00 72.75  ? 346 TYR   A N    1 
ATOM   2721 C CA   . TYR   A 1 346 ? -9.802  -20.849 -15.640 1.00 72.51  ? 346 TYR   A CA   1 
ATOM   2722 C C    . TYR   A 1 346 ? -10.860 -21.686 -16.321 1.00 76.14  ? 346 TYR   A C    1 
ATOM   2723 O O    . TYR   A 1 346 ? -10.711 -22.093 -17.463 1.00 76.15  ? 346 TYR   A O    1 
ATOM   2724 C CB   . TYR   A 1 346 ? -10.059 -19.389 -15.962 1.00 72.98  ? 346 TYR   A CB   1 
ATOM   2725 C CG   . TYR   A 1 346 ? -10.311 -19.159 -17.449 1.00 74.41  ? 346 TYR   A CG   1 
ATOM   2726 C CD1  . TYR   A 1 346 ? -9.258  -18.917 -18.322 1.00 73.73  ? 346 TYR   A CD1  1 
ATOM   2727 C CD2  . TYR   A 1 346 ? -11.598 -19.210 -17.978 1.00 73.67  ? 346 TYR   A CD2  1 
ATOM   2728 C CE1  . TYR   A 1 346 ? -9.480  -18.702 -19.660 1.00 75.04  ? 346 TYR   A CE1  1 
ATOM   2729 C CE2  . TYR   A 1 346 ? -11.829 -19.001 -19.329 1.00 76.01  ? 346 TYR   A CE2  1 
ATOM   2730 C CZ   . TYR   A 1 346 ? -10.764 -18.750 -20.161 1.00 75.89  ? 346 TYR   A CZ   1 
ATOM   2731 O OH   . TYR   A 1 346 ? -10.974 -18.535 -21.504 1.00 78.02  ? 346 TYR   A OH   1 
ATOM   2732 N N    . LYS   A 1 347 ? -11.935 -21.922 -15.607 1.00 87.16  ? 347 LYS   A N    1 
ATOM   2733 C CA   . LYS   A 1 347 ? -13.124 -22.628 -16.075 1.00 90.11  ? 347 LYS   A CA   1 
ATOM   2734 C C    . LYS   A 1 347 ? -14.271 -21.845 -15.503 1.00 85.22  ? 347 LYS   A C    1 
ATOM   2735 O O    . LYS   A 1 347 ? -14.363 -21.755 -14.293 1.00 87.08  ? 347 LYS   A O    1 
ATOM   2736 C CB   . LYS   A 1 347 ? -12.903 -24.111 -15.698 1.00 90.43  ? 347 LYS   A CB   1 
ATOM   2737 C CG   . LYS   A 1 347 ? -13.607 -25.370 -16.193 1.00 93.26  ? 347 LYS   A CG   1 
ATOM   2738 C CD   . LYS   A 1 347 ? -14.900 -25.798 -15.584 1.00 95.95  ? 347 LYS   A CD   1 
ATOM   2739 C CE   . LYS   A 1 347 ? -14.907 -27.367 -15.821 1.00 100.20 ? 347 LYS   A CE   1 
ATOM   2740 N NZ   . LYS   A 1 347 ? -16.029 -28.165 -15.016 1.00 101.91 ? 347 LYS   A NZ   1 
ATOM   2741 N N    . MET   A 1 348 ? -15.091 -21.238 -16.378 1.00 78.06  ? 348 MET   A N    1 
ATOM   2742 C CA   . MET   A 1 348 ? -16.256 -20.429 -16.039 1.00 78.40  ? 348 MET   A CA   1 
ATOM   2743 C C    . MET   A 1 348 ? -17.464 -21.314 -15.765 1.00 80.31  ? 348 MET   A C    1 
ATOM   2744 O O    . MET   A 1 348 ? -17.587 -22.409 -16.309 1.00 82.17  ? 348 MET   A O    1 
ATOM   2745 C CB   . MET   A 1 348 ? -16.632 -19.447 -17.170 1.00 76.46  ? 348 MET   A CB   1 
ATOM   2746 C CG   . MET   A 1 348 ? -15.457 -18.741 -17.875 1.00 77.79  ? 348 MET   A CG   1 
ATOM   2747 S SD   . MET   A 1 348 ? -16.030 -17.498 -19.089 1.00 81.18  ? 348 MET   A SD   1 
ATOM   2748 C CE   . MET   A 1 348 ? -14.479 -16.986 -19.820 1.00 78.49  ? 348 MET   A CE   1 
ATOM   2749 N N    . SER   A 1 349 ? -18.378 -20.821 -14.918 1.00 82.97  ? 349 SER   A N    1 
ATOM   2750 C CA   . SER   A 1 349 ? -19.609 -21.569 -14.697 1.00 82.26  ? 349 SER   A CA   1 
ATOM   2751 C C    . SER   A 1 349 ? -20.441 -21.649 -15.974 1.00 88.48  ? 349 SER   A C    1 
ATOM   2752 O O    . SER   A 1 349 ? -21.276 -22.551 -16.114 1.00 86.63  ? 349 SER   A O    1 
ATOM   2753 C CB   . SER   A 1 349 ? -20.400 -20.921 -13.565 1.00 82.23  ? 349 SER   A CB   1 
ATOM   2754 O OG   . SER   A 1 349 ? -19.561 -20.703 -12.438 1.00 84.76  ? 349 SER   A OG   1 
ATOM   2755 N N    . GLU   A 1 350 ? -20.195 -20.749 -16.921 1.00 93.14  ? 350 GLU   A N    1 
ATOM   2756 C CA   . GLU   A 1 350 ? -20.981 -20.673 -18.137 1.00 94.95  ? 350 GLU   A CA   1 
ATOM   2757 C C    . GLU   A 1 350 ? -20.376 -19.598 -19.030 1.00 94.29  ? 350 GLU   A C    1 
ATOM   2758 O O    . GLU   A 1 350 ? -19.795 -18.626 -18.544 1.00 93.00  ? 350 GLU   A O    1 
ATOM   2759 C CB   . GLU   A 1 350 ? -22.445 -20.353 -17.817 1.00 94.85  ? 350 GLU   A CB   1 
ATOM   2760 C CG   . GLU   A 1 350 ? -22.644 -19.020 -17.125 1.00 97.53  ? 350 GLU   A CG   1 
ATOM   2761 C CD   . GLU   A 1 350 ? -23.726 -19.067 -16.063 1.00 98.99  ? 350 GLU   A CD   1 
ATOM   2762 O OE1  . GLU   A 1 350 ? -24.798 -19.645 -16.346 1.00 100.86 ? 350 GLU   A OE1  1 
ATOM   2763 O OE2  . GLU   A 1 350 ? -23.505 -18.520 -14.956 1.00 97.94  ? 350 GLU   A OE2  1 
ATOM   2764 N N    . ASN   A 1 351 ? -20.505 -19.794 -20.337 1.00 112.11 ? 351 ASN   A N    1 
ATOM   2765 C CA   . ASN   A 1 351 ? -20.132 -18.757 -21.294 1.00 111.19 ? 351 ASN   A CA   1 
ATOM   2766 C C    . ASN   A 1 351 ? -21.325 -17.830 -21.457 1.00 111.99 ? 351 ASN   A C    1 
ATOM   2767 O O    . ASN   A 1 351 ? -22.285 -18.146 -22.159 1.00 116.70 ? 351 ASN   A O    1 
ATOM   2768 C CB   . ASN   A 1 351 ? -19.691 -19.348 -22.629 1.00 115.85 ? 351 ASN   A CB   1 
ATOM   2769 C CG   . ASN   A 1 351 ? -18.372 -18.752 -23.129 1.00 119.20 ? 351 ASN   A CG   1 
ATOM   2770 O OD1  . ASN   A 1 351 ? -18.285 -17.552 -23.415 1.00 116.91 ? 351 ASN   A OD1  1 
ATOM   2771 N ND2  . ASN   A 1 351 ? -17.358 -19.595 -23.274 1.00 115.12 ? 351 ASN   A ND2  1 
ATOM   2772 N N    . ILE   A 1 352 ? -21.284 -16.698 -20.769 1.00 93.56  ? 352 ILE   A N    1 
ATOM   2773 C CA   . ILE   A 1 352 ? -22.248 -15.627 -20.988 1.00 91.83  ? 352 ILE   A CA   1 
ATOM   2774 C C    . ILE   A 1 352 ? -21.792 -14.932 -22.264 1.00 93.96  ? 352 ILE   A C    1 
ATOM   2775 O O    . ILE   A 1 352 ? -20.667 -14.412 -22.310 1.00 93.37  ? 352 ILE   A O    1 
ATOM   2776 C CB   . ILE   A 1 352 ? -22.307 -14.670 -19.786 1.00 89.52  ? 352 ILE   A CB   1 
ATOM   2777 C CG1  . ILE   A 1 352 ? -22.377 -15.466 -18.478 1.00 87.80  ? 352 ILE   A CG1  1 
ATOM   2778 C CG2  . ILE   A 1 352 ? -23.485 -13.716 -19.916 1.00 90.69  ? 352 ILE   A CG2  1 
ATOM   2779 C CD1  . ILE   A 1 352 ? -23.767 -15.931 -18.111 1.00 87.13  ? 352 ILE   A CD1  1 
ATOM   2780 N N    . PRO   A 1 353 ? -22.614 -14.908 -23.330 1.00 86.23  ? 353 PRO   A N    1 
ATOM   2781 C CA   . PRO   A 1 353 ? -22.101 -14.457 -24.633 1.00 84.66  ? 353 PRO   A CA   1 
ATOM   2782 C C    . PRO   A 1 353 ? -21.687 -12.992 -24.663 1.00 83.69  ? 353 PRO   A C    1 
ATOM   2783 O O    . PRO   A 1 353 ? -20.551 -12.688 -25.041 1.00 81.12  ? 353 PRO   A O    1 
ATOM   2784 C CB   . PRO   A 1 353 ? -23.283 -14.714 -25.581 1.00 86.60  ? 353 PRO   A CB   1 
ATOM   2785 C CG   . PRO   A 1 353 ? -24.284 -15.527 -24.787 1.00 88.75  ? 353 PRO   A CG   1 
ATOM   2786 C CD   . PRO   A 1 353 ? -24.056 -15.195 -23.367 1.00 83.74  ? 353 PRO   A CD   1 
ATOM   2787 N N    . ASN   A 1 354 ? -22.549 -12.084 -24.197 1.00 115.92 ? 354 ASN   A N    1 
ATOM   2788 C CA   . ASN   A 1 354 ? -22.268 -10.651 -24.249 1.00 114.73 ? 354 ASN   A CA   1 
ATOM   2789 C C    . ASN   A 1 354 ? -21.375 -10.173 -23.087 1.00 115.44 ? 354 ASN   A C    1 
ATOM   2790 O O    . ASN   A 1 354 ? -21.402 -8.995  -22.708 1.00 110.70 ? 354 ASN   A O    1 
ATOM   2791 C CB   . ASN   A 1 354 ? -23.577 -9.851  -24.317 1.00 115.00 ? 354 ASN   A CB   1 
ATOM   2792 C CG   . ASN   A 1 354 ? -24.344 -9.837  -22.998 1.00 124.29 ? 354 ASN   A CG   1 
ATOM   2793 O OD1  . ASN   A 1 354 ? -24.013 -10.557 -22.056 1.00 118.17 ? 354 ASN   A OD1  1 
ATOM   2794 N ND2  . ASN   A 1 354 ? -25.384 -9.010  -22.935 1.00 127.66 ? 354 ASN   A ND2  1 
ATOM   2795 N N    . GLU   A 1 355 ? -20.612 -11.070 -22.479 1.00 76.79  ? 355 GLU   A N    1 
ATOM   2796 C CA   . GLU   A 1 355 ? -19.658 -10.702 -21.448 1.00 76.02  ? 355 GLU   A CA   1 
ATOM   2797 C C    . GLU   A 1 355 ? -18.272 -11.149 -21.885 1.00 73.07  ? 355 GLU   A C    1 
ATOM   2798 O O    . GLU   A 1 355 ? -18.058 -12.336 -22.159 1.00 72.70  ? 355 GLU   A O    1 
ATOM   2799 C CB   . GLU   A 1 355 ? -20.030 -11.333 -20.109 1.00 74.64  ? 355 GLU   A CB   1 
ATOM   2800 C CG   . GLU   A 1 355 ? -19.657 -10.487 -18.921 1.00 73.88  ? 355 GLU   A CG   1 
ATOM   2801 C CD   . GLU   A 1 355 ? -20.431 -10.891 -17.676 1.00 76.31  ? 355 GLU   A CD   1 
ATOM   2802 O OE1  . GLU   A 1 355 ? -20.045 -11.905 -17.046 1.00 74.74  ? 355 GLU   A OE1  1 
ATOM   2803 O OE2  . GLU   A 1 355 ? -21.415 -10.197 -17.327 1.00 76.54  ? 355 GLU   A OE2  1 
ATOM   2804 N N    . VAL   A 1 356 ? -17.339 -10.202 -21.957 1.00 68.90  ? 356 VAL   A N    1 
ATOM   2805 C CA   . VAL   A 1 356 ? -15.969 -10.467 -22.379 1.00 68.00  ? 356 VAL   A CA   1 
ATOM   2806 C C    . VAL   A 1 356 ? -15.023 -10.294 -21.194 1.00 67.39  ? 356 VAL   A C    1 
ATOM   2807 O O    . VAL   A 1 356 ? -15.053 -9.266  -20.512 1.00 66.65  ? 356 VAL   A O    1 
ATOM   2808 C CB   . VAL   A 1 356 ? -15.547 -9.552  -23.536 1.00 69.63  ? 356 VAL   A CB   1 
ATOM   2809 C CG1  . VAL   A 1 356 ? -14.039 -9.618  -23.694 1.00 69.27  ? 356 VAL   A CG1  1 
ATOM   2810 C CG2  . VAL   A 1 356 ? -16.267 -9.960  -24.827 1.00 70.40  ? 356 VAL   A CG2  1 
ATOM   2811 N N    . TYR   A 1 357 ? -14.163 -11.283 -20.978 1.00 65.20  ? 357 TYR   A N    1 
ATOM   2812 C CA   . TYR   A 1 357 ? -13.098 -11.220 -19.991 1.00 62.83  ? 357 TYR   A CA   1 
ATOM   2813 C C    . TYR   A 1 357 ? -11.744 -11.164 -20.687 1.00 65.64  ? 357 TYR   A C    1 
ATOM   2814 O O    . TYR   A 1 357 ? -11.598 -11.556 -21.859 1.00 65.00  ? 357 TYR   A O    1 
ATOM   2815 C CB   . TYR   A 1 357 ? -13.132 -12.425 -19.046 1.00 63.24  ? 357 TYR   A CB   1 
ATOM   2816 C CG   . TYR   A 1 357 ? -14.266 -12.344 -18.068 1.00 64.97  ? 357 TYR   A CG   1 
ATOM   2817 C CD1  . TYR   A 1 357 ? -15.580 -12.461 -18.503 1.00 67.00  ? 357 TYR   A CD1  1 
ATOM   2818 C CD2  . TYR   A 1 357 ? -14.036 -12.116 -16.711 1.00 62.07  ? 357 TYR   A CD2  1 
ATOM   2819 C CE1  . TYR   A 1 357 ? -16.635 -12.371 -17.609 1.00 69.16  ? 357 TYR   A CE1  1 
ATOM   2820 C CE2  . TYR   A 1 357 ? -15.079 -12.022 -15.823 1.00 62.14  ? 357 TYR   A CE2  1 
ATOM   2821 C CZ   . TYR   A 1 357 ? -16.376 -12.153 -16.271 1.00 66.56  ? 357 TYR   A CZ   1 
ATOM   2822 O OH   . TYR   A 1 357 ? -17.423 -12.059 -15.387 1.00 69.02  ? 357 TYR   A OH   1 
ATOM   2823 N N    . ALA   A 1 358 ? -10.764 -10.608 -19.982 1.00 58.90  ? 358 ALA   A N    1 
ATOM   2824 C CA   . ALA   A 1 358 ? -9.422  -10.542 -20.538 1.00 60.57  ? 358 ALA   A CA   1 
ATOM   2825 C C    . ALA   A 1 358 ? -8.398  -10.774 -19.437 1.00 62.61  ? 358 ALA   A C    1 
ATOM   2826 O O    . ALA   A 1 358 ? -8.662  -10.544 -18.252 1.00 60.42  ? 358 ALA   A O    1 
ATOM   2827 C CB   . ALA   A 1 358 ? -9.163  -9.207  -21.249 1.00 60.13  ? 358 ALA   A CB   1 
ATOM   2828 N N    . LEU   A 1 359 ? -7.216  -11.237 -19.845 1.00 69.18  ? 359 LEU   A N    1 
ATOM   2829 C CA   . LEU   A 1 359 ? -6.072  -11.352 -18.947 1.00 67.48  ? 359 LEU   A CA   1 
ATOM   2830 C C    . LEU   A 1 359 ? -5.013  -10.346 -19.381 1.00 68.57  ? 359 LEU   A C    1 
ATOM   2831 O O    . LEU   A 1 359 ? -4.629  -10.307 -20.560 1.00 69.66  ? 359 LEU   A O    1 
ATOM   2832 C CB   . LEU   A 1 359 ? -5.501  -12.774 -18.935 1.00 66.63  ? 359 LEU   A CB   1 
ATOM   2833 C CG   . LEU   A 1 359 ? -4.072  -12.966 -18.417 1.00 66.03  ? 359 LEU   A CG   1 
ATOM   2834 C CD1  . LEU   A 1 359 ? -4.029  -12.866 -16.870 1.00 66.33  ? 359 LEU   A CD1  1 
ATOM   2835 C CD2  . LEU   A 1 359 ? -3.516  -14.306 -18.865 1.00 66.48  ? 359 LEU   A CD2  1 
ATOM   2836 N N    . GLY   A 1 360 ? -4.579  -9.517  -18.440 1.00 68.65  ? 360 GLY   A N    1 
ATOM   2837 C CA   . GLY   A 1 360 ? -3.692  -8.414  -18.743 1.00 66.55  ? 360 GLY   A CA   1 
ATOM   2838 C C    . GLY   A 1 360 ? -2.487  -8.375  -17.827 1.00 69.37  ? 360 GLY   A C    1 
ATOM   2839 O O    . GLY   A 1 360 ? -2.546  -8.758  -16.650 1.00 72.10  ? 360 GLY   A O    1 
ATOM   2840 N N    . ALA   A 1 361 ? -1.385  -7.877  -18.386 1.00 61.14  ? 361 ALA   A N    1 
ATOM   2841 C CA   . ALA   A 1 361 ? -0.119  -7.735  -17.680 1.00 62.46  ? 361 ALA   A CA   1 
ATOM   2842 C C    . ALA   A 1 361 ? 0.346   -6.288  -17.776 1.00 62.40  ? 361 ALA   A C    1 
ATOM   2843 O O    . ALA   A 1 361 ? 0.329   -5.695  -18.866 1.00 64.77  ? 361 ALA   A O    1 
ATOM   2844 C CB   . ALA   A 1 361 ? 0.953   -8.667  -18.266 1.00 61.89  ? 361 ALA   A CB   1 
ATOM   2845 N N    . PHE   A 1 362 ? 0.775   -5.728  -16.647 1.00 61.69  ? 362 PHE   A N    1 
ATOM   2846 C CA   . PHE   A 1 362 ? 1.349   -4.390  -16.621 1.00 65.41  ? 362 PHE   A CA   1 
ATOM   2847 C C    . PHE   A 1 362 ? 2.616   -4.378  -15.784 1.00 66.81  ? 362 PHE   A C    1 
ATOM   2848 O O    . PHE   A 1 362 ? 2.667   -4.975  -14.705 1.00 64.17  ? 362 PHE   A O    1 
ATOM   2849 C CB   . PHE   A 1 362 ? 0.384   -3.349  -16.054 1.00 62.67  ? 362 PHE   A CB   1 
ATOM   2850 C CG   . PHE   A 1 362 ? 0.969   -1.960  -16.010 1.00 66.73  ? 362 PHE   A CG   1 
ATOM   2851 C CD1  . PHE   A 1 362 ? 1.058   -1.196  -17.180 1.00 62.93  ? 362 PHE   A CD1  1 
ATOM   2852 C CD2  . PHE   A 1 362 ? 1.446   -1.420  -14.814 1.00 61.90  ? 362 PHE   A CD2  1 
ATOM   2853 C CE1  . PHE   A 1 362 ? 1.605   0.079   -17.154 1.00 63.27  ? 362 PHE   A CE1  1 
ATOM   2854 C CE2  . PHE   A 1 362 ? 1.999   -0.136  -14.781 1.00 62.71  ? 362 PHE   A CE2  1 
ATOM   2855 C CZ   . PHE   A 1 362 ? 2.077   0.610   -15.943 1.00 65.39  ? 362 PHE   A CZ   1 
ATOM   2856 N N    . ASP   A 1 363 ? 3.621   -3.655  -16.272 1.00 78.51  ? 363 ASP   A N    1 
ATOM   2857 C CA   . ASP   A 1 363 ? 4.914   -3.551  -15.598 1.00 77.86  ? 363 ASP   A CA   1 
ATOM   2858 C C    . ASP   A 1 363 ? 5.461   -2.161  -15.920 1.00 80.72  ? 363 ASP   A C    1 
ATOM   2859 O O    . ASP   A 1 363 ? 6.107   -1.958  -16.953 1.00 84.15  ? 363 ASP   A O    1 
ATOM   2860 C CB   . ASP   A 1 363 ? 5.848   -4.659  -16.060 1.00 79.16  ? 363 ASP   A CB   1 
ATOM   2861 C CG   . ASP   A 1 363 ? 7.259   -4.504  -15.535 1.00 82.38  ? 363 ASP   A CG   1 
ATOM   2862 O OD1  . ASP   A 1 363 ? 7.559   -3.500  -14.860 1.00 82.73  ? 363 ASP   A OD1  1 
ATOM   2863 O OD2  . ASP   A 1 363 ? 8.077   -5.404  -15.809 1.00 87.52  ? 363 ASP   A OD2  1 
ATOM   2864 N N    . GLY   A 1 364 ? 5.201   -1.212  -15.028 1.00 81.08  ? 364 GLY   A N    1 
ATOM   2865 C CA   . GLY   A 1 364 ? 5.609   0.147   -15.325 1.00 79.97  ? 364 GLY   A CA   1 
ATOM   2866 C C    . GLY   A 1 364 ? 5.213   1.104   -14.227 1.00 79.94  ? 364 GLY   A C    1 
ATOM   2867 O O    . GLY   A 1 364 ? 4.680   0.715   -13.188 1.00 78.15  ? 364 GLY   A O    1 
ATOM   2868 N N    . LEU   A 1 365 ? 5.475   2.378   -14.489 1.00 71.11  ? 365 LEU   A N    1 
ATOM   2869 C CA   . LEU   A 1 365 ? 5.318   3.451   -13.519 1.00 73.90  ? 365 LEU   A CA   1 
ATOM   2870 C C    . LEU   A 1 365 ? 3.962   4.123   -13.712 1.00 72.57  ? 365 LEU   A C    1 
ATOM   2871 O O    . LEU   A 1 365 ? 3.661   4.615   -14.806 1.00 74.07  ? 365 LEU   A O    1 
ATOM   2872 C CB   . LEU   A 1 365 ? 6.457   4.455   -13.686 1.00 71.23  ? 365 LEU   A CB   1 
ATOM   2873 C CG   . LEU   A 1 365 ? 6.505   5.705   -12.825 1.00 72.21  ? 365 LEU   A CG   1 
ATOM   2874 C CD1  . LEU   A 1 365 ? 6.543   5.336   -11.327 1.00 70.96  ? 365 LEU   A CD1  1 
ATOM   2875 C CD2  . LEU   A 1 365 ? 7.711   6.523   -13.232 1.00 74.33  ? 365 LEU   A CD2  1 
ATOM   2876 N N    . HIS   A 1 366 ? 3.139   4.111   -12.664 1.00 66.22  ? 366 HIS   A N    1 
ATOM   2877 C CA   . HIS   A 1 366 ? 1.926   4.911   -12.620 1.00 67.36  ? 366 HIS   A CA   1 
ATOM   2878 C C    . HIS   A 1 366 ? 2.282   6.354   -12.288 1.00 67.83  ? 366 HIS   A C    1 
ATOM   2879 O O    . HIS   A 1 366 ? 3.146   6.614   -11.441 1.00 72.70  ? 366 HIS   A O    1 
ATOM   2880 C CB   . HIS   A 1 366 ? 0.959   4.349   -11.569 1.00 66.34  ? 366 HIS   A CB   1 
ATOM   2881 C CG   . HIS   A 1 366 ? -0.358  5.060   -11.508 1.00 62.63  ? 366 HIS   A CG   1 
ATOM   2882 N ND1  . HIS   A 1 366 ? -1.468  4.633   -12.204 1.00 59.78  ? 366 HIS   A ND1  1 
ATOM   2883 C CD2  . HIS   A 1 366 ? -0.746  6.163   -10.824 1.00 63.74  ? 366 HIS   A CD2  1 
ATOM   2884 C CE1  . HIS   A 1 366 ? -2.480  5.447   -11.961 1.00 59.94  ? 366 HIS   A CE1  1 
ATOM   2885 N NE2  . HIS   A 1 366 ? -2.069  6.383   -11.124 1.00 62.20  ? 366 HIS   A NE2  1 
ATOM   2886 N N    . THR   A 1 367 ? 1.601   7.295   -12.954 1.00 70.29  ? 367 THR   A N    1 
ATOM   2887 C CA   . THR   A 1 367 ? 1.902   8.715   -12.815 1.00 69.41  ? 367 THR   A CA   1 
ATOM   2888 C C    . THR   A 1 367 ? 0.693   9.623   -12.614 1.00 68.55  ? 367 THR   A C    1 
ATOM   2889 O O    . THR   A 1 367 ? 0.893   10.802  -12.313 1.00 70.52  ? 367 THR   A O    1 
ATOM   2890 C CB   . THR   A 1 367 ? 2.691   9.229   -14.038 1.00 72.54  ? 367 THR   A CB   1 
ATOM   2891 O OG1  . THR   A 1 367 ? 2.012   8.881   -15.259 1.00 70.83  ? 367 THR   A OG1  1 
ATOM   2892 C CG2  . THR   A 1 367 ? 4.104   8.645   -14.049 1.00 72.56  ? 367 THR   A CG2  1 
ATOM   2893 N N    . VAL   A 1 368 ? -0.533  9.145   -12.783 1.00 69.19  ? 368 VAL   A N    1 
ATOM   2894 C CA   . VAL   A 1 368 ? -1.701  10.019  -12.721 1.00 71.40  ? 368 VAL   A CA   1 
ATOM   2895 C C    . VAL   A 1 368 ? -2.276  9.957   -11.307 1.00 69.53  ? 368 VAL   A C    1 
ATOM   2896 O O    . VAL   A 1 368 ? -2.706  8.891   -10.853 1.00 69.65  ? 368 VAL   A O    1 
ATOM   2897 C CB   . VAL   A 1 368 ? -2.750  9.625   -13.776 1.00 70.45  ? 368 VAL   A CB   1 
ATOM   2898 C CG1  . VAL   A 1 368 ? -4.135  10.038  -13.338 1.00 74.04  ? 368 VAL   A CG1  1 
ATOM   2899 C CG2  . VAL   A 1 368 ? -2.420  10.235  -15.133 1.00 71.03  ? 368 VAL   A CG2  1 
ATOM   2900 N N    . GLU   A 1 369 ? -2.320  11.111  -10.631 1.00 75.03  ? 369 GLU   A N    1 
ATOM   2901 C CA   . GLU   A 1 369 ? -2.684  11.213  -9.215  1.00 75.68  ? 369 GLU   A CA   1 
ATOM   2902 C C    . GLU   A 1 369 ? -1.922  10.183  -8.380  1.00 76.14  ? 369 GLU   A C    1 
ATOM   2903 O O    . GLU   A 1 369 ? -2.493  9.259   -7.791  1.00 77.46  ? 369 GLU   A O    1 
ATOM   2904 C CB   . GLU   A 1 369 ? -4.188  11.065  -9.004  1.00 76.65  ? 369 GLU   A CB   1 
ATOM   2905 C CG   . GLU   A 1 369 ? -5.048  11.632  -10.097 1.00 76.90  ? 369 GLU   A CG   1 
ATOM   2906 C CD   . GLU   A 1 369 ? -6.314  10.816  -10.252 1.00 81.26  ? 369 GLU   A CD   1 
ATOM   2907 O OE1  . GLU   A 1 369 ? -7.056  10.709  -9.248  1.00 82.43  ? 369 GLU   A OE1  1 
ATOM   2908 O OE2  . GLU   A 1 369 ? -6.548  10.258  -11.351 1.00 77.01  ? 369 GLU   A OE2  1 
ATOM   2909 N N    . GLY   A 1 370 ? -0.601  10.321  -8.405  1.00 63.41  ? 370 GLY   A N    1 
ATOM   2910 C CA   . GLY   A 1 370 ? 0.273   9.427   -7.681  1.00 62.36  ? 370 GLY   A CA   1 
ATOM   2911 C C    . GLY   A 1 370 ? 1.347   8.842   -8.568  1.00 67.51  ? 370 GLY   A C    1 
ATOM   2912 O O    . GLY   A 1 370 ? 1.072   8.431   -9.701  1.00 64.43  ? 370 GLY   A O    1 
ATOM   2913 N N    . ARG   A 1 371 ? 2.581   8.819   -8.072  1.00 80.55  ? 371 ARG   A N    1 
ATOM   2914 C CA   . ARG   A 1 371 ? 3.703   8.214   -8.777  1.00 83.69  ? 371 ARG   A CA   1 
ATOM   2915 C C    . ARG   A 1 371 ? 4.111   6.953   -8.027  1.00 81.06  ? 371 ARG   A C    1 
ATOM   2916 O O    . ARG   A 1 371 ? 4.500   7.025   -6.856  1.00 81.43  ? 371 ARG   A O    1 
ATOM   2917 C CB   . ARG   A 1 371 ? 4.880   9.188   -8.890  1.00 81.64  ? 371 ARG   A CB   1 
ATOM   2918 C CG   . ARG   A 1 371 ? 6.228   8.528   -9.151  1.00 87.34  ? 371 ARG   A CG   1 
ATOM   2919 C CD   . ARG   A 1 371 ? 7.014   9.298   -10.215 1.00 87.02  ? 371 ARG   A CD   1 
ATOM   2920 N NE   . ARG   A 1 371 ? 8.378   8.804   -10.380 1.00 92.07  ? 371 ARG   A NE   1 
ATOM   2921 C CZ   . ARG   A 1 371 ? 9.442   9.583   -10.533 1.00 94.61  ? 371 ARG   A CZ   1 
ATOM   2922 N NH1  . ARG   A 1 371 ? 9.338   10.902  -10.532 1.00 95.75  ? 371 ARG   A NH1  1 
ATOM   2923 N NH2  . ARG   A 1 371 ? 10.642  9.023   -10.680 1.00 96.05  ? 371 ARG   A NH2  1 
ATOM   2924 N N    . TYR   A 1 372 ? 3.985   5.795   -8.681  1.00 69.36  ? 372 TYR   A N    1 
ATOM   2925 C CA   . TYR   A 1 372 ? 4.414   4.559   -8.034  1.00 69.46  ? 372 TYR   A CA   1 
ATOM   2926 C C    . TYR   A 1 372 ? 4.575   3.459   -9.074  1.00 66.94  ? 372 TYR   A C    1 
ATOM   2927 O O    . TYR   A 1 372 ? 3.762   3.342   -9.989  1.00 67.11  ? 372 TYR   A O    1 
ATOM   2928 C CB   . TYR   A 1 372 ? 3.430   4.119   -6.932  1.00 65.07  ? 372 TYR   A CB   1 
ATOM   2929 C CG   . TYR   A 1 372 ? 1.968   4.393   -7.227  1.00 61.84  ? 372 TYR   A CG   1 
ATOM   2930 C CD1  . TYR   A 1 372 ? 1.395   5.616   -6.906  1.00 62.43  ? 372 TYR   A CD1  1 
ATOM   2931 C CD2  . TYR   A 1 372 ? 1.153   3.420   -7.793  1.00 59.37  ? 372 TYR   A CD2  1 
ATOM   2932 C CE1  . TYR   A 1 372 ? 0.049   5.879   -7.169  1.00 63.22  ? 372 TYR   A CE1  1 
ATOM   2933 C CE2  . TYR   A 1 372 ? -0.199  3.669   -8.055  1.00 57.77  ? 372 TYR   A CE2  1 
ATOM   2934 C CZ   . TYR   A 1 372 ? -0.746  4.905   -7.747  1.00 58.81  ? 372 TYR   A CZ   1 
ATOM   2935 O OH   . TYR   A 1 372 ? -2.083  5.175   -7.991  1.00 56.75  ? 372 TYR   A OH   1 
ATOM   2936 N N    . TYR   A 1 373 ? 5.608   2.640   -8.904  1.00 69.43  ? 373 TYR   A N    1 
ATOM   2937 C CA   . TYR   A 1 373 ? 5.875   1.557   -9.832  1.00 70.67  ? 373 TYR   A CA   1 
ATOM   2938 C C    . TYR   A 1 373 ? 5.011   0.347   -9.511  1.00 70.63  ? 373 TYR   A C    1 
ATOM   2939 O O    . TYR   A 1 373 ? 4.877   -0.051  -8.346  1.00 70.71  ? 373 TYR   A O    1 
ATOM   2940 C CB   . TYR   A 1 373 ? 7.343   1.162   -9.779  1.00 75.36  ? 373 TYR   A CB   1 
ATOM   2941 C CG   . TYR   A 1 373 ? 7.754   0.433   -11.016 1.00 75.20  ? 373 TYR   A CG   1 
ATOM   2942 C CD1  . TYR   A 1 373 ? 8.171   1.131   -12.144 1.00 76.04  ? 373 TYR   A CD1  1 
ATOM   2943 C CD2  . TYR   A 1 373 ? 7.696   -0.949  -11.079 1.00 76.31  ? 373 TYR   A CD2  1 
ATOM   2944 C CE1  . TYR   A 1 373 ? 8.541   0.474   -13.294 1.00 75.21  ? 373 TYR   A CE1  1 
ATOM   2945 C CE2  . TYR   A 1 373 ? 8.066   -1.624  -12.240 1.00 77.26  ? 373 TYR   A CE2  1 
ATOM   2946 C CZ   . TYR   A 1 373 ? 8.485   -0.900  -13.340 1.00 75.79  ? 373 TYR   A CZ   1 
ATOM   2947 O OH   . TYR   A 1 373 ? 8.849   -1.554  -14.490 1.00 78.49  ? 373 TYR   A OH   1 
ATOM   2948 N N    . LEU   A 1 374 ? 4.441   -0.253  -10.555 1.00 64.87  ? 374 LEU   A N    1 
ATOM   2949 C CA   . LEU   A 1 374 ? 3.462   -1.319  -10.437 1.00 64.65  ? 374 LEU   A CA   1 
ATOM   2950 C C    . LEU   A 1 374 ? 3.848   -2.520  -11.290 1.00 67.49  ? 374 LEU   A C    1 
ATOM   2951 O O    . LEU   A 1 374 ? 4.371   -2.374  -12.403 1.00 67.77  ? 374 LEU   A O    1 
ATOM   2952 C CB   . LEU   A 1 374 ? 2.069   -0.836  -10.870 1.00 62.67  ? 374 LEU   A CB   1 
ATOM   2953 C CG   . LEU   A 1 374 ? 1.405   0.274   -10.060 1.00 64.68  ? 374 LEU   A CG   1 
ATOM   2954 C CD1  . LEU   A 1 374 ? 0.157   0.791   -10.774 1.00 59.54  ? 374 LEU   A CD1  1 
ATOM   2955 C CD2  . LEU   A 1 374 ? 1.073   -0.231  -8.638  1.00 62.51  ? 374 LEU   A CD2  1 
ATOM   2956 N N    . GLN   A 1 375 ? 3.563   -3.709  -10.762 1.00 75.21  ? 375 GLN   A N    1 
ATOM   2957 C CA   . GLN   A 1 375 ? 3.531   -4.938  -11.546 1.00 73.87  ? 375 GLN   A CA   1 
ATOM   2958 C C    . GLN   A 1 375 ? 2.193   -5.614  -11.263 1.00 74.00  ? 375 GLN   A C    1 
ATOM   2959 O O    . GLN   A 1 375 ? 1.938   -6.047  -10.136 1.00 70.22  ? 375 GLN   A O    1 
ATOM   2960 C CB   . GLN   A 1 375 ? 4.705   -5.850  -11.186 1.00 73.82  ? 375 GLN   A CB   1 
ATOM   2961 C CG   . GLN   A 1 375 ? 5.972   -5.587  -11.992 1.00 78.92  ? 375 GLN   A CG   1 
ATOM   2962 C CD   . GLN   A 1 375 ? 7.091   -6.556  -11.647 1.00 79.50  ? 375 GLN   A CD   1 
ATOM   2963 O OE1  . GLN   A 1 375 ? 6.952   -7.390  -10.745 1.00 78.07  ? 375 GLN   A OE1  1 
ATOM   2964 N NE2  . GLN   A 1 375 ? 8.194   -6.478  -12.391 1.00 80.83  ? 375 GLN   A NE2  1 
ATOM   2965 N N    . ILE   A 1 376 ? 1.328   -5.704  -12.267 1.00 58.32  ? 376 ILE   A N    1 
ATOM   2966 C CA   . ILE   A 1 376 ? -0.032  -6.181  -12.048 1.00 57.16  ? 376 ILE   A CA   1 
ATOM   2967 C C    . ILE   A 1 376 ? -0.345  -7.291  -13.037 1.00 60.13  ? 376 ILE   A C    1 
ATOM   2968 O O    . ILE   A 1 376 ? -0.138  -7.129  -14.248 1.00 59.27  ? 376 ILE   A O    1 
ATOM   2969 C CB   . ILE   A 1 376 ? -1.071  -5.053  -12.175 1.00 55.27  ? 376 ILE   A CB   1 
ATOM   2970 C CG1  . ILE   A 1 376 ? -0.814  -3.953  -11.142 1.00 55.31  ? 376 ILE   A CG1  1 
ATOM   2971 C CG2  . ILE   A 1 376 ? -2.484  -5.626  -12.062 1.00 53.30  ? 376 ILE   A CG2  1 
ATOM   2972 C CD1  . ILE   A 1 376 ? -1.661  -2.719  -11.362 1.00 53.85  ? 376 ILE   A CD1  1 
ATOM   2973 N N    . CYS   A 1 377 ? -0.873  -8.403  -12.524 1.00 63.35  ? 377 CYS   A N    1 
ATOM   2974 C CA   . CYS   A 1 377 ? -1.456  -9.457  -13.348 1.00 65.68  ? 377 CYS   A CA   1 
ATOM   2975 C C    . CYS   A 1 377 ? -2.949  -9.518  -13.052 1.00 64.57  ? 377 CYS   A C    1 
ATOM   2976 O O    . CYS   A 1 377 ? -3.339  -9.680  -11.896 1.00 60.89  ? 377 CYS   A O    1 
ATOM   2977 C CB   . CYS   A 1 377 ? -0.791  -10.802 -13.071 1.00 65.15  ? 377 CYS   A CB   1 
ATOM   2978 S SG   . CYS   A 1 377 ? 0.924   -10.880 -13.607 1.00 67.50  ? 377 CYS   A SG   1 
ATOM   2979 N N    . THR   A 1 378 ? -3.791  -9.379  -14.081 1.00 63.48  ? 378 THR   A N    1 
ATOM   2980 C CA   . THR   A 1 378 ? -5.218  -9.246  -13.804 1.00 60.76  ? 378 THR   A CA   1 
ATOM   2981 C C    . THR   A 1 378 ? -6.073  -10.065 -14.757 1.00 64.61  ? 378 THR   A C    1 
ATOM   2982 O O    . THR   A 1 378 ? -5.885  -10.014 -15.974 1.00 62.98  ? 378 THR   A O    1 
ATOM   2983 C CB   . THR   A 1 378 ? -5.661  -7.775  -13.844 1.00 61.82  ? 378 THR   A CB   1 
ATOM   2984 O OG1  . THR   A 1 378 ? -7.031  -7.675  -13.423 1.00 59.09  ? 378 THR   A OG1  1 
ATOM   2985 C CG2  . THR   A 1 378 ? -5.491  -7.170  -15.231 1.00 60.11  ? 378 THR   A CG2  1 
ATOM   2986 N N    . LEU   A 1 379 ? -6.985  -10.852 -14.189 1.00 63.82  ? 379 LEU   A N    1 
ATOM   2987 C CA   . LEU   A 1 379 ? -8.155  -11.335 -14.909 1.00 61.28  ? 379 LEU   A CA   1 
ATOM   2988 C C    . LEU   A 1 379 ? -9.292  -10.356 -14.633 1.00 62.16  ? 379 LEU   A C    1 
ATOM   2989 O O    . LEU   A 1 379 ? -9.592  -10.071 -13.465 1.00 58.58  ? 379 LEU   A O    1 
ATOM   2990 C CB   . LEU   A 1 379 ? -8.525  -12.744 -14.447 1.00 58.55  ? 379 LEU   A CB   1 
ATOM   2991 C CG   . LEU   A 1 379 ? -9.986  -13.186 -14.568 1.00 60.80  ? 379 LEU   A CG   1 
ATOM   2992 C CD1  . LEU   A 1 379 ? -10.352 -13.442 -16.032 1.00 62.59  ? 379 LEU   A CD1  1 
ATOM   2993 C CD2  . LEU   A 1 379 ? -10.192 -14.453 -13.778 1.00 59.27  ? 379 LEU   A CD2  1 
ATOM   2994 N N    . LEU   A 1 380 ? -9.904  -9.803  -15.682 1.00 64.58  ? 380 LEU   A N    1 
ATOM   2995 C CA   . LEU   A 1 380 ? -10.939 -8.811  -15.398 1.00 63.94  ? 380 LEU   A CA   1 
ATOM   2996 C C    . LEU   A 1 380 ? -12.063 -8.859  -16.423 1.00 64.99  ? 380 LEU   A C    1 
ATOM   2997 O O    . LEU   A 1 380 ? -11.868 -9.233  -17.588 1.00 67.04  ? 380 LEU   A O    1 
ATOM   2998 C CB   . LEU   A 1 380 ? -10.379 -7.378  -15.310 1.00 64.38  ? 380 LEU   A CB   1 
ATOM   2999 C CG   . LEU   A 1 380 ? -9.353  -6.876  -16.329 1.00 63.15  ? 380 LEU   A CG   1 
ATOM   3000 C CD1  . LEU   A 1 380 ? -10.008 -6.678  -17.672 1.00 63.75  ? 380 LEU   A CD1  1 
ATOM   3001 C CD2  . LEU   A 1 380 ? -8.731  -5.570  -15.856 1.00 62.45  ? 380 LEU   A CD2  1 
ATOM   3002 N N    . LYS   A 1 381 ? -13.243 -8.444  -15.962 1.00 53.66  ? 381 LYS   A N    1 
ATOM   3003 C CA   . LYS   A 1 381 ? -14.409 -8.294  -16.818 1.00 55.48  ? 381 LYS   A CA   1 
ATOM   3004 C C    . LYS   A 1 381 ? -14.347 -6.945  -17.522 1.00 55.68  ? 381 LYS   A C    1 
ATOM   3005 O O    . LYS   A 1 381 ? -14.350 -5.892  -16.875 1.00 54.87  ? 381 LYS   A O    1 
ATOM   3006 C CB   . LYS   A 1 381 ? -15.692 -8.410  -16.000 1.00 55.00  ? 381 LYS   A CB   1 
ATOM   3007 C CG   . LYS   A 1 381 ? -16.948 -8.412  -16.838 1.00 57.26  ? 381 LYS   A CG   1 
ATOM   3008 C CD   . LYS   A 1 381 ? -17.954 -7.417  -16.317 1.00 58.99  ? 381 LYS   A CD   1 
ATOM   3009 C CE   . LYS   A 1 381 ? -19.240 -7.457  -17.151 1.00 59.28  ? 381 LYS   A CE   1 
ATOM   3010 N NZ   . LYS   A 1 381 ? -19.060 -6.624  -18.335 1.00 60.57  ? 381 LYS   A NZ   1 
ATOM   3011 N N    . CYS   A 1 382 ? -14.340 -6.972  -18.850 1.00 57.91  ? 382 CYS   A N    1 
ATOM   3012 C CA   . CYS   A 1 382 ? -14.297 -5.731  -19.612 1.00 58.32  ? 382 CYS   A CA   1 
ATOM   3013 C C    . CYS   A 1 382 ? -15.622 -4.987  -19.492 1.00 58.20  ? 382 CYS   A C    1 
ATOM   3014 O O    . CYS   A 1 382 ? -16.686 -5.600  -19.372 1.00 55.72  ? 382 CYS   A O    1 
ATOM   3015 C CB   . CYS   A 1 382 ? -13.948 -6.037  -21.063 1.00 60.65  ? 382 CYS   A CB   1 
ATOM   3016 S SG   . CYS   A 1 382 ? -12.454 -7.079  -21.172 1.00 60.23  ? 382 CYS   A SG   1 
ATOM   3017 N N    . LYS   A 1 383 ? -15.557 -3.658  -19.408 1.00 56.65  ? 383 LYS   A N    1 
ATOM   3018 C CA   . LYS   A 1 383 ? -16.791 -2.867  -19.162 1.00 55.23  ? 383 LYS   A CA   1 
ATOM   3019 C C    . LYS   A 1 383 ? -17.853 -3.243  -20.199 1.00 59.29  ? 383 LYS   A C    1 
ATOM   3020 O O    . LYS   A 1 383 ? -18.988 -3.549  -19.793 1.00 57.68  ? 383 LYS   A O    1 
ATOM   3021 C CB   . LYS   A 1 383 ? -16.457 -1.373  -19.169 1.00 55.60  ? 383 LYS   A CB   1 
ATOM   3022 C CG   . LYS   A 1 383 ? -17.570 -0.435  -18.745 1.00 56.93  ? 383 LYS   A CG   1 
ATOM   3023 C CD   . LYS   A 1 383 ? -17.288 0.998   -19.175 1.00 58.81  ? 383 LYS   A CD   1 
ATOM   3024 C CE   . LYS   A 1 383 ? -17.659 2.010   -18.138 1.00 64.29  ? 383 LYS   A CE   1 
ATOM   3025 N NZ   . LYS   A 1 383 ? -16.478 2.608   -17.510 1.00 74.69  ? 383 LYS   A NZ   1 
ATOM   3026 N N    . THR   A 1 384 ? -17.495 -3.205  -21.480 1.00 54.11  ? 384 THR   A N    1 
ATOM   3027 C CA   . THR   A 1 384 ? -18.426 -3.605  -22.552 1.00 55.33  ? 384 THR   A CA   1 
ATOM   3028 C C    . THR   A 1 384 ? -17.789 -4.714  -23.353 1.00 57.12  ? 384 THR   A C    1 
ATOM   3029 O O    . THR   A 1 384 ? -16.730 -5.210  -22.933 1.00 56.19  ? 384 THR   A O    1 
ATOM   3030 C CB   . THR   A 1 384 ? -18.757 -2.408  -23.448 1.00 61.11  ? 384 THR   A CB   1 
ATOM   3031 O OG1  . THR   A 1 384 ? -17.631 -2.252  -24.303 1.00 56.99  ? 384 THR   A OG1  1 
ATOM   3032 C CG2  . THR   A 1 384 ? -18.999 -1.129  -22.668 1.00 57.97  ? 384 THR   A CG2  1 
ATOM   3033 N N    . THR   A 1 385 ? -18.393 -5.070  -24.488 1.00 54.11  ? 385 THR   A N    1 
ATOM   3034 C CA   . THR   A 1 385 ? -17.840 -6.107  -25.381 1.00 56.53  ? 385 THR   A CA   1 
ATOM   3035 C C    . THR   A 1 385 ? -16.729 -5.511  -26.213 1.00 52.46  ? 385 THR   A C    1 
ATOM   3036 O O    . THR   A 1 385 ? -15.928 -6.281  -26.765 1.00 52.50  ? 385 THR   A O    1 
ATOM   3037 C CB   . THR   A 1 385 ? -18.979 -6.645  -26.236 1.00 58.38  ? 385 THR   A CB   1 
ATOM   3038 O OG1  . THR   A 1 385 ? -19.565 -5.492  -26.825 1.00 55.97  ? 385 THR   A OG1  1 
ATOM   3039 C CG2  . THR   A 1 385 ? -20.021 -7.381  -25.416 1.00 60.40  ? 385 THR   A CG2  1 
ATOM   3040 N N    . ASN   A 1 386 ? -16.667 -4.182  -26.291 1.00 55.95  ? 386 ASN   A N    1 
ATOM   3041 C CA   . ASN   A 1 386 ? -15.564 -3.511  -27.024 1.00 56.29  ? 386 ASN   A CA   1 
ATOM   3042 C C    . ASN   A 1 386 ? -14.269 -3.745  -26.256 1.00 54.96  ? 386 ASN   A C    1 
ATOM   3043 O O    . ASN   A 1 386 ? -14.193 -3.351  -25.090 1.00 56.06  ? 386 ASN   A O    1 
ATOM   3044 C CB   . ASN   A 1 386 ? -15.848 -2.033  -27.270 1.00 57.54  ? 386 ASN   A CB   1 
ATOM   3045 C CG   . ASN   A 1 386 ? -14.964 -1.407  -28.320 1.00 58.58  ? 386 ASN   A CG   1 
ATOM   3046 O OD1  . ASN   A 1 386 ? -13.796 -1.777  -28.463 1.00 57.96  ? 386 ASN   A OD1  1 
ATOM   3047 N ND2  . ASN   A 1 386 ? -15.500 -0.446  -29.056 1.00 60.51  ? 386 ASN   A ND2  1 
ATOM   3048 N N    . LEU   A 1 387 ? -13.277 -4.320  -26.922 1.00 63.92  ? 387 LEU   A N    1 
ATOM   3049 C CA   . LEU   A 1 387 ? -11.976 -4.619  -26.281 1.00 64.88  ? 387 LEU   A CA   1 
ATOM   3050 C C    . LEU   A 1 387 ? -11.298 -3.336  -25.797 1.00 63.22  ? 387 LEU   A C    1 
ATOM   3051 O O    . LEU   A 1 387 ? -10.305 -3.436  -25.061 1.00 64.87  ? 387 LEU   A O    1 
ATOM   3052 C CB   . LEU   A 1 387 ? -11.128 -5.326  -27.330 1.00 65.51  ? 387 LEU   A CB   1 
ATOM   3053 C CG   . LEU   A 1 387 ? -11.778 -6.531  -28.011 1.00 67.37  ? 387 LEU   A CG   1 
ATOM   3054 C CD1  . LEU   A 1 387 ? -10.835 -7.107  -29.049 1.00 66.49  ? 387 LEU   A CD1  1 
ATOM   3055 C CD2  . LEU   A 1 387 ? -12.155 -7.578  -26.980 1.00 62.75  ? 387 LEU   A CD2  1 
ATOM   3056 N N    . ASN   A 1 388 ? -11.803 -2.181  -26.211 1.00 54.62  ? 388 ASN   A N    1 
ATOM   3057 C CA   . ASN   A 1 388 ? -11.178 -0.896  -25.815 1.00 55.49  ? 388 ASN   A CA   1 
ATOM   3058 C C    . ASN   A 1 388 ? -11.614 -0.568  -24.384 1.00 54.79  ? 388 ASN   A C    1 
ATOM   3059 O O    . ASN   A 1 388 ? -10.986 0.307   -23.774 1.00 55.76  ? 388 ASN   A O    1 
ATOM   3060 C CB   . ASN   A 1 388 ? -11.501 0.203   -26.824 1.00 57.56  ? 388 ASN   A CB   1 
ATOM   3061 C CG   . ASN   A 1 388 ? -11.077 -0.120  -28.236 1.00 59.33  ? 388 ASN   A CG   1 
ATOM   3062 O OD1  . ASN   A 1 388 ? -9.989  -0.660  -28.456 1.00 60.47  ? 388 ASN   A OD1  1 
ATOM   3063 N ND2  . ASN   A 1 388 ? -11.912 0.220   -29.204 1.00 61.07  ? 388 ASN   A ND2  1 
ATOM   3064 N N    . THR   A 1 389 ? -12.632 -1.265  -23.874 1.00 61.56  ? 389 THR   A N    1 
ATOM   3065 C CA   . THR   A 1 389 ? -13.165 -1.023  -22.516 1.00 62.74  ? 389 THR   A CA   1 
ATOM   3066 C C    . THR   A 1 389 ? -12.583 -2.014  -21.536 1.00 61.59  ? 389 THR   A C    1 
ATOM   3067 O O    . THR   A 1 389 ? -12.942 -1.943  -20.351 1.00 63.49  ? 389 THR   A O    1 
ATOM   3068 C CB   . THR   A 1 389 ? -14.687 -1.113  -22.549 1.00 59.50  ? 389 THR   A CB   1 
ATOM   3069 O OG1  . THR   A 1 389 ? -15.012 -2.455  -22.890 1.00 59.30  ? 389 THR   A OG1  1 
ATOM   3070 C CG2  . THR   A 1 389 ? -15.281 -0.151  -23.558 1.00 60.91  ? 389 THR   A CG2  1 
ATOM   3071 N N    . CYS   A 1 390 ? -11.734 -2.922  -22.008 1.00 64.86  ? 390 CYS   A N    1 
ATOM   3072 C CA   . CYS   A 1 390 ? -11.057 -3.864  -21.085 1.00 64.12  ? 390 CYS   A CA   1 
ATOM   3073 C C    . CYS   A 1 390 ? -10.133 -3.027  -20.200 1.00 63.76  ? 390 CYS   A C    1 
ATOM   3074 O O    . CYS   A 1 390 ? -9.115  -2.536  -20.710 1.00 64.54  ? 390 CYS   A O    1 
ATOM   3075 C CB   . CYS   A 1 390 ? -10.323 -4.970  -21.838 1.00 66.69  ? 390 CYS   A CB   1 
ATOM   3076 S SG   . CYS   A 1 390 ? -11.397 -6.180  -22.652 1.00 65.26  ? 390 CYS   A SG   1 
ATOM   3077 N N    . GLY   A 1 391 ? -10.510 -2.847  -18.938 1.00 62.02  ? 391 GLY   A N    1 
ATOM   3078 C CA   . GLY   A 1 391 ? -9.716  -2.022  -18.013 1.00 62.94  ? 391 GLY   A CA   1 
ATOM   3079 C C    . GLY   A 1 391 ? -10.549 -0.920  -17.408 1.00 63.07  ? 391 GLY   A C    1 
ATOM   3080 O O    . GLY   A 1 391 ? -10.155 -0.372  -16.370 1.00 65.94  ? 391 GLY   A O    1 
ATOM   3081 N N    . ASP   A 1 392 ? -11.670 -0.612  -18.044 1.00 65.46  ? 392 ASP   A N    1 
ATOM   3082 C CA   . ASP   A 1 392 ? -12.554 0.467   -17.552 1.00 63.91  ? 392 ASP   A CA   1 
ATOM   3083 C C    . ASP   A 1 392 ? -13.306 -0.040  -16.327 1.00 66.69  ? 392 ASP   A C    1 
ATOM   3084 O O    . ASP   A 1 392 ? -13.476 -1.264  -16.199 1.00 62.10  ? 392 ASP   A O    1 
ATOM   3085 C CB   . ASP   A 1 392 ? -13.505 0.936   -18.637 1.00 65.12  ? 392 ASP   A CB   1 
ATOM   3086 C CG   . ASP   A 1 392 ? -12.873 1.659   -19.817 1.00 72.37  ? 392 ASP   A CG   1 
ATOM   3087 O OD1  . ASP   A 1 392 ? -11.636 1.816   -19.819 1.00 68.55  ? 392 ASP   A OD1  1 
ATOM   3088 O OD2  . ASP   A 1 392 ? -13.629 2.060   -20.724 1.00 73.67  ? 392 ASP   A OD2  1 
ATOM   3089 N N    . SER   A 1 393 ? -13.762 0.885   -15.487 1.00 61.31  ? 393 SER   A N    1 
ATOM   3090 C CA   . SER   A 1 393 ? -14.501 0.512   -14.262 1.00 60.56  ? 393 SER   A CA   1 
ATOM   3091 C C    . SER   A 1 393 ? -15.725 -0.330  -14.627 1.00 62.51  ? 393 SER   A C    1 
ATOM   3092 O O    . SER   A 1 393 ? -16.561 0.157   -15.404 1.00 60.91  ? 393 SER   A O    1 
ATOM   3093 C CB   . SER   A 1 393 ? -14.886 1.732   -13.477 1.00 61.58  ? 393 SER   A CB   1 
ATOM   3094 O OG   . SER   A 1 393 ? -16.172 1.589   -12.891 1.00 62.60  ? 393 SER   A OG   1 
ATOM   3095 N N    . ALA   A 1 394 ? -15.808 -1.544  -14.087 1.00 56.35  ? 394 ALA   A N    1 
ATOM   3096 C CA   . ALA   A 1 394 ? -16.992 -2.403  -14.302 1.00 53.31  ? 394 ALA   A CA   1 
ATOM   3097 C C    . ALA   A 1 394 ? -17.548 -2.773  -12.932 1.00 57.28  ? 394 ALA   A C    1 
ATOM   3098 O O    . ALA   A 1 394 ? -16.789 -3.301  -12.105 1.00 53.00  ? 394 ALA   A O    1 
ATOM   3099 C CB   . ALA   A 1 394 ? -16.606 -3.617  -15.098 1.00 53.46  ? 394 ALA   A CB   1 
ATOM   3100 N N    . GLU   A 1 395 ? -18.825 -2.502  -12.704 1.00 82.37  ? 395 GLU   A N    1 
ATOM   3101 C CA   . GLU   A 1 395 ? -19.396 -2.717  -11.358 1.00 85.48  ? 395 GLU   A CA   1 
ATOM   3102 C C    . GLU   A 1 395 ? -20.201 -4.008  -11.313 1.00 84.47  ? 395 GLU   A C    1 
ATOM   3103 O O    . GLU   A 1 395 ? -20.337 -4.567  -10.217 1.00 82.36  ? 395 GLU   A O    1 
ATOM   3104 C CB   . GLU   A 1 395 ? -20.325 -1.546  -11.056 1.00 84.12  ? 395 GLU   A CB   1 
ATOM   3105 C CG   . GLU   A 1 395 ? -19.962 -0.800  -9.777  1.00 93.09  ? 395 GLU   A CG   1 
ATOM   3106 C CD   . GLU   A 1 395 ? -20.332 0.670   -9.826  1.00 105.00 ? 395 GLU   A CD   1 
ATOM   3107 O OE1  . GLU   A 1 395 ? -21.539 0.978   -9.729  1.00 105.95 ? 395 GLU   A OE1  1 
ATOM   3108 O OE2  . GLU   A 1 395 ? -19.416 1.507   -9.965  1.00 104.25 ? 395 GLU   A OE2  1 
ATOM   3109 N N    . THR   A 1 396 ? -20.702 -4.461  -12.455 1.00 60.33  ? 396 THR   A N    1 
ATOM   3110 C CA   . THR   A 1 396 ? -21.595 -5.628  -12.438 1.00 61.03  ? 396 THR   A CA   1 
ATOM   3111 C C    . THR   A 1 396 ? -21.111 -6.690  -13.381 1.00 62.49  ? 396 THR   A C    1 
ATOM   3112 O O    . THR   A 1 396 ? -20.504 -6.326  -14.397 1.00 63.36  ? 396 THR   A O    1 
ATOM   3113 C CB   . THR   A 1 396 ? -22.993 -5.161  -12.821 1.00 62.50  ? 396 THR   A CB   1 
ATOM   3114 O OG1  . THR   A 1 396 ? -22.803 -4.327  -13.958 1.00 66.81  ? 396 THR   A OG1  1 
ATOM   3115 C CG2  . THR   A 1 396 ? -23.675 -4.391  -11.705 1.00 61.48  ? 396 THR   A CG2  1 
ATOM   3116 N N    . ALA   A 1 397 ? -21.347 -7.956  -13.046 1.00 56.82  ? 397 ALA   A N    1 
ATOM   3117 C CA   . ALA   A 1 397 ? -21.014 -9.077  -13.917 1.00 58.47  ? 397 ALA   A CA   1 
ATOM   3118 C C    . ALA   A 1 397 ? -21.983 -10.219 -13.633 1.00 60.26  ? 397 ALA   A C    1 
ATOM   3119 O O    . ALA   A 1 397 ? -22.627 -10.261 -12.582 1.00 57.86  ? 397 ALA   A O    1 
ATOM   3120 C CB   . ALA   A 1 397 ? -19.555 -9.525  -13.733 1.00 53.91  ? 397 ALA   A CB   1 
ATOM   3121 N N    . SER   A 1 398 ? -22.087 -11.146 -14.598 1.00 60.68  ? 398 SER   A N    1 
ATOM   3122 C CA   . SER   A 1 398 ? -22.943 -12.326 -14.476 1.00 59.05  ? 398 SER   A CA   1 
ATOM   3123 C C    . SER   A 1 398 ? -22.179 -13.639 -14.562 1.00 63.06  ? 398 SER   A C    1 
ATOM   3124 O O    . SER   A 1 398 ? -22.719 -14.676 -14.152 1.00 63.75  ? 398 SER   A O    1 
ATOM   3125 C CB   . SER   A 1 398 ? -24.043 -12.343 -15.557 1.00 67.13  ? 398 SER   A CB   1 
ATOM   3126 O OG   . SER   A 1 398 ? -24.737 -11.109 -15.679 1.00 69.04  ? 398 SER   A OG   1 
ATOM   3127 N N    . THR   A 1 399 ? -20.952 -13.627 -15.090 1.00 59.38  ? 399 THR   A N    1 
ATOM   3128 C CA   . THR   A 1 399 ? -20.180 -14.846 -15.298 1.00 61.62  ? 399 THR   A CA   1 
ATOM   3129 C C    . THR   A 1 399 ? -19.547 -15.271 -13.982 1.00 60.60  ? 399 THR   A C    1 
ATOM   3130 O O    . THR   A 1 399 ? -18.589 -14.643 -13.515 1.00 60.12  ? 399 THR   A O    1 
ATOM   3131 C CB   . THR   A 1 399 ? -19.095 -14.628 -16.346 1.00 59.50  ? 399 THR   A CB   1 
ATOM   3132 O OG1  . THR   A 1 399 ? -19.701 -14.278 -17.595 1.00 63.79  ? 399 THR   A OG1  1 
ATOM   3133 C CG2  . THR   A 1 399 ? -18.265 -15.904 -16.519 1.00 59.62  ? 399 THR   A CG2  1 
ATOM   3134 N N    . ARG   A 1 400 ? -20.048 -16.356 -13.409 1.00 66.44  ? 400 ARG   A N    1 
ATOM   3135 C CA   . ARG   A 1 400 ? -19.356 -16.979 -12.294 1.00 66.95  ? 400 ARG   A CA   1 
ATOM   3136 C C    . ARG   A 1 400 ? -18.275 -17.905 -12.833 1.00 67.70  ? 400 ARG   A C    1 
ATOM   3137 O O    . ARG   A 1 400 ? -18.306 -18.325 -13.993 1.00 68.06  ? 400 ARG   A O    1 
ATOM   3138 C CB   . ARG   A 1 400 ? -20.328 -17.752 -11.394 1.00 70.10  ? 400 ARG   A CB   1 
ATOM   3139 C CG   . ARG   A 1 400 ? -21.151 -16.912 -10.395 1.00 68.04  ? 400 ARG   A CG   1 
ATOM   3140 C CD   . ARG   A 1 400 ? -22.611 -17.356 -10.372 1.00 68.06  ? 400 ARG   A CD   1 
ATOM   3141 N NE   . ARG   A 1 400 ? -22.740 -18.748 -10.789 1.00 79.61  ? 400 ARG   A NE   1 
ATOM   3142 C CZ   . ARG   A 1 400 ? -23.707 -19.232 -11.561 1.00 84.61  ? 400 ARG   A CZ   1 
ATOM   3143 N NH1  . ARG   A 1 400 ? -24.522 -18.438 -12.231 1.00 81.50  ? 400 ARG   A NH1  1 
ATOM   3144 N NH2  . ARG   A 1 400 ? -23.779 -20.545 -11.761 1.00 88.00  ? 400 ARG   A NH2  1 
ATOM   3145 N N    . PHE   A 1 401 ? -17.301 -18.211 -11.979 1.00 74.88  ? 401 PHE   A N    1 
ATOM   3146 C CA   . PHE   A 1 401 ? -16.179 -19.061 -12.356 1.00 72.75  ? 401 PHE   A CA   1 
ATOM   3147 C C    . PHE   A 1 401 ? -16.178 -20.320 -11.506 1.00 75.27  ? 401 PHE   A C    1 
ATOM   3148 O O    . PHE   A 1 401 ? -16.232 -20.244 -10.275 1.00 75.36  ? 401 PHE   A O    1 
ATOM   3149 C CB   . PHE   A 1 401 ? -14.844 -18.335 -12.193 1.00 70.67  ? 401 PHE   A CB   1 
ATOM   3150 C CG   . PHE   A 1 401 ? -14.451 -17.501 -13.381 1.00 74.00  ? 401 PHE   A CG   1 
ATOM   3151 C CD1  . PHE   A 1 401 ? -15.134 -16.327 -13.685 1.00 71.60  ? 401 PHE   A CD1  1 
ATOM   3152 C CD2  . PHE   A 1 401 ? -13.400 -17.890 -14.198 1.00 71.72  ? 401 PHE   A CD2  1 
ATOM   3153 C CE1  . PHE   A 1 401 ? -14.768 -15.551 -14.773 1.00 68.11  ? 401 PHE   A CE1  1 
ATOM   3154 C CE2  . PHE   A 1 401 ? -13.034 -17.122 -15.291 1.00 70.72  ? 401 PHE   A CE2  1 
ATOM   3155 C CZ   . PHE   A 1 401 ? -13.719 -15.954 -15.579 1.00 68.44  ? 401 PHE   A CZ   1 
ATOM   3156 N N    . GLU   A 1 402 ? -16.135 -21.477 -12.170 1.00 81.38  ? 402 GLU   A N    1 
ATOM   3157 C CA   . GLU   A 1 402 ? -15.948 -22.742 -11.468 1.00 82.62  ? 402 GLU   A CA   1 
ATOM   3158 C C    . GLU   A 1 402 ? -14.545 -22.845 -10.882 1.00 81.49  ? 402 GLU   A C    1 
ATOM   3159 O O    . GLU   A 1 402 ? -14.357 -23.395 -9.793  1.00 84.81  ? 402 GLU   A O    1 
ATOM   3160 C CB   . GLU   A 1 402 ? -16.231 -23.910 -12.408 1.00 84.73  ? 402 GLU   A CB   1 
ATOM   3161 C CG   . GLU   A 1 402 ? -17.687 -24.000 -12.841 1.00 87.09  ? 402 GLU   A CG   1 
ATOM   3162 C CD   . GLU   A 1 402 ? -18.626 -24.289 -11.682 1.00 84.97  ? 402 GLU   A CD   1 
ATOM   3163 O OE1  . GLU   A 1 402 ? -18.677 -25.457 -11.238 1.00 88.11  ? 402 GLU   A OE1  1 
ATOM   3164 O OE2  . GLU   A 1 402 ? -19.310 -23.351 -11.217 1.00 85.69  ? 402 GLU   A OE2  1 
ATOM   3165 N N    . MET   A 1 403 ? -13.546 -22.331 -11.591 1.00 86.35  ? 403 MET   A N    1 
ATOM   3166 C CA   . MET   A 1 403 ? -12.187 -22.362 -11.080 1.00 84.64  ? 403 MET   A CA   1 
ATOM   3167 C C    . MET   A 1 403 ? -11.380 -21.247 -11.733 1.00 83.59  ? 403 MET   A C    1 
ATOM   3168 O O    . MET   A 1 403 ? -11.644 -20.854 -12.874 1.00 85.63  ? 403 MET   A O    1 
ATOM   3169 C CB   . MET   A 1 403 ? -11.543 -23.725 -11.355 1.00 84.90  ? 403 MET   A CB   1 
ATOM   3170 C CG   . MET   A 1 403 ? -10.032 -23.691 -11.377 1.00 86.95  ? 403 MET   A CG   1 
ATOM   3171 S SD   . MET   A 1 403 ? -9.362  -23.646 -13.039 1.00 94.43  ? 403 MET   A SD   1 
ATOM   3172 C CE   . MET   A 1 403 ? -7.602  -23.683 -12.709 1.00 91.58  ? 403 MET   A CE   1 
ATOM   3173 N N    . PHE   A 1 404 ? -10.384 -20.757 -11.006 1.00 73.65  ? 404 PHE   A N    1 
ATOM   3174 C CA   . PHE   A 1 404 ? -9.403  -19.849 -11.573 1.00 74.19  ? 404 PHE   A CA   1 
ATOM   3175 C C    . PHE   A 1 404 ? -8.081  -20.091 -10.861 1.00 73.93  ? 404 PHE   A C    1 
ATOM   3176 O O    . PHE   A 1 404 ? -8.038  -20.666 -9.771  1.00 78.05  ? 404 PHE   A O    1 
ATOM   3177 C CB   . PHE   A 1 404 ? -9.834  -18.373 -11.471 1.00 73.02  ? 404 PHE   A CB   1 
ATOM   3178 C CG   . PHE   A 1 404 ? -9.863  -17.830 -10.063 1.00 68.72  ? 404 PHE   A CG   1 
ATOM   3179 C CD1  . PHE   A 1 404 ? -8.691  -17.455 -9.415  1.00 70.21  ? 404 PHE   A CD1  1 
ATOM   3180 C CD2  . PHE   A 1 404 ? -11.067 -17.665 -9.400  1.00 70.94  ? 404 PHE   A CD2  1 
ATOM   3181 C CE1  . PHE   A 1 404 ? -8.719  -16.959 -8.122  1.00 67.50  ? 404 PHE   A CE1  1 
ATOM   3182 C CE2  . PHE   A 1 404 ? -11.097 -17.164 -8.095  1.00 68.58  ? 404 PHE   A CE2  1 
ATOM   3183 C CZ   . PHE   A 1 404 ? -9.923  -16.809 -7.468  1.00 64.48  ? 404 PHE   A CZ   1 
ATOM   3184 N N    . SER   A 1 405 ? -6.999  -19.668 -11.505 1.00 75.51  ? 405 SER   A N    1 
ATOM   3185 C CA   . SER   A 1 405 ? -5.668  -19.745 -10.908 1.00 73.47  ? 405 SER   A CA   1 
ATOM   3186 C C    . SER   A 1 405 ? -4.779  -18.740 -11.620 1.00 74.42  ? 405 SER   A C    1 
ATOM   3187 O O    . SER   A 1 405 ? -4.553  -18.869 -12.831 1.00 77.24  ? 405 SER   A O    1 
ATOM   3188 C CB   . SER   A 1 405 ? -5.098  -21.156 -11.018 1.00 73.44  ? 405 SER   A CB   1 
ATOM   3189 O OG   . SER   A 1 405 ? -3.746  -21.174 -10.596 1.00 74.61  ? 405 SER   A OG   1 
ATOM   3190 N N    . LEU   A 1 406 ? -4.278  -17.758 -10.876 1.00 64.32  ? 406 LEU   A N    1 
ATOM   3191 C CA   . LEU   A 1 406 ? -3.492  -16.655 -11.409 1.00 62.96  ? 406 LEU   A CA   1 
ATOM   3192 C C    . LEU   A 1 406 ? -2.127  -16.617 -10.730 1.00 65.38  ? 406 LEU   A C    1 
ATOM   3193 O O    . LEU   A 1 406 ? -2.020  -16.837 -9.517  1.00 69.79  ? 406 LEU   A O    1 
ATOM   3194 C CB   . LEU   A 1 406 ? -4.217  -15.317 -11.185 1.00 63.12  ? 406 LEU   A CB   1 
ATOM   3195 C CG   . LEU   A 1 406 ? -3.599  -14.059 -11.802 1.00 62.76  ? 406 LEU   A CG   1 
ATOM   3196 C CD1  . LEU   A 1 406 ? -3.667  -14.135 -13.352 1.00 58.53  ? 406 LEU   A CD1  1 
ATOM   3197 C CD2  . LEU   A 1 406 ? -4.267  -12.797 -11.272 1.00 55.26  ? 406 LEU   A CD2  1 
ATOM   3198 N N    . SER   A 1 407 ? -1.093  -16.317 -11.510 1.00 73.57  ? 407 SER   A N    1 
ATOM   3199 C CA   . SER   A 1 407 ? 0.255   -16.183 -10.966 1.00 73.95  ? 407 SER   A CA   1 
ATOM   3200 C C    . SER   A 1 407 ? 1.062   -15.274 -11.884 1.00 78.36  ? 407 SER   A C    1 
ATOM   3201 O O    . SER   A 1 407 ? 0.636   -14.945 -12.993 1.00 78.66  ? 407 SER   A O    1 
ATOM   3202 C CB   . SER   A 1 407 ? 0.927   -17.546 -10.786 1.00 76.02  ? 407 SER   A CB   1 
ATOM   3203 O OG   . SER   A 1 407 ? 0.748   -18.371 -11.926 1.00 83.23  ? 407 SER   A OG   1 
ATOM   3204 N N    . GLY   A 1 408 ? 2.222   -14.839 -11.400 1.00 79.94  ? 408 GLY   A N    1 
ATOM   3205 C CA   . GLY   A 1 408 ? 3.046   -13.944 -12.192 1.00 79.95  ? 408 GLY   A CA   1 
ATOM   3206 C C    . GLY   A 1 408 ? 4.491   -13.963 -11.757 1.00 81.51  ? 408 GLY   A C    1 
ATOM   3207 O O    . GLY   A 1 408 ? 4.810   -14.246 -10.598 1.00 81.62  ? 408 GLY   A O    1 
ATOM   3208 N N    . THR   A 1 409 ? 5.370   -13.613 -12.698 1.00 78.92  ? 409 THR   A N    1 
ATOM   3209 C CA   . THR   A 1 409 ? 6.810   -13.567 -12.438 1.00 82.69  ? 409 THR   A CA   1 
ATOM   3210 C C    . THR   A 1 409 ? 7.180   -12.212 -11.830 1.00 83.18  ? 409 THR   A C    1 
ATOM   3211 O O    . THR   A 1 409 ? 7.921   -11.409 -12.399 1.00 83.86  ? 409 THR   A O    1 
ATOM   3212 C CB   . THR   A 1 409 ? 7.594   -13.817 -13.720 1.00 87.73  ? 409 THR   A CB   1 
ATOM   3213 O OG1  . THR   A 1 409 ? 7.782   -12.566 -14.399 1.00 87.36  ? 409 THR   A OG1  1 
ATOM   3214 C CG2  . THR   A 1 409 ? 6.871   -14.801 -14.641 1.00 82.94  ? 409 THR   A CG2  1 
ATOM   3215 N N    . PHE   A 1 410 ? 6.680   -11.989 -10.621 1.00 74.15  ? 410 PHE   A N    1 
ATOM   3216 C CA   . PHE   A 1 410 ? 6.818   -10.683 -9.993  1.00 75.35  ? 410 PHE   A CA   1 
ATOM   3217 C C    . PHE   A 1 410 ? 8.265   -10.416 -9.598  1.00 76.51  ? 410 PHE   A C    1 
ATOM   3218 O O    . PHE   A 1 410 ? 8.982   -11.311 -9.136  1.00 75.92  ? 410 PHE   A O    1 
ATOM   3219 C CB   . PHE   A 1 410 ? 5.908   -10.588 -8.770  1.00 71.40  ? 410 PHE   A CB   1 
ATOM   3220 C CG   . PHE   A 1 410 ? 4.451   -10.481 -9.115  1.00 70.65  ? 410 PHE   A CG   1 
ATOM   3221 C CD1  . PHE   A 1 410 ? 3.877   -9.250  -9.388  1.00 68.46  ? 410 PHE   A CD1  1 
ATOM   3222 C CD2  . PHE   A 1 410 ? 3.656   -11.618 -9.190  1.00 72.13  ? 410 PHE   A CD2  1 
ATOM   3223 C CE1  . PHE   A 1 410 ? 2.531   -9.153  -9.714  1.00 65.22  ? 410 PHE   A CE1  1 
ATOM   3224 C CE2  . PHE   A 1 410 ? 2.311   -11.526 -9.513  1.00 67.11  ? 410 PHE   A CE2  1 
ATOM   3225 C CZ   . PHE   A 1 410 ? 1.750   -10.294 -9.772  1.00 65.56  ? 410 PHE   A CZ   1 
ATOM   3226 N N    . GLY   A 1 411 ? 8.706   -9.182  -9.831  1.00 79.97  ? 411 GLY   A N    1 
ATOM   3227 C CA   . GLY   A 1 411 ? 10.035  -8.769  -9.429  1.00 78.67  ? 411 GLY   A CA   1 
ATOM   3228 C C    . GLY   A 1 411 ? 9.993   -8.102  -8.066  1.00 80.90  ? 411 GLY   A C    1 
ATOM   3229 O O    . GLY   A 1 411 ? 10.898  -7.343  -7.703  1.00 83.16  ? 411 GLY   A O    1 
ATOM   3230 N N    . THR   A 1 412 ? 8.930   -8.366  -7.303  1.00 71.76  ? 412 THR   A N    1 
ATOM   3231 C CA   . THR   A 1 412 ? 8.795   -7.849  -5.947  1.00 70.14  ? 412 THR   A CA   1 
ATOM   3232 C C    . THR   A 1 412 ? 8.091   -8.890  -5.093  1.00 69.35  ? 412 THR   A C    1 
ATOM   3233 O O    . THR   A 1 412 ? 7.433   -9.801  -5.599  1.00 70.05  ? 412 THR   A O    1 
ATOM   3234 C CB   . THR   A 1 412 ? 8.012   -6.531  -5.908  1.00 66.44  ? 412 THR   A CB   1 
ATOM   3235 O OG1  . THR   A 1 412 ? 7.968   -6.040  -4.558  1.00 68.73  ? 412 THR   A OG1  1 
ATOM   3236 C CG2  . THR   A 1 412 ? 6.584   -6.747  -6.397  1.00 62.46  ? 412 THR   A CG2  1 
ATOM   3237 N N    . GLN   A 1 413 ? 8.303   -8.798  -3.788  1.00 72.05  ? 413 GLN   A N    1 
ATOM   3238 C CA   . GLN   A 1 413 ? 7.606   -9.665  -2.855  1.00 73.25  ? 413 GLN   A CA   1 
ATOM   3239 C C    . GLN   A 1 413 ? 6.417   -8.978  -2.194  1.00 69.24  ? 413 GLN   A C    1 
ATOM   3240 O O    . GLN   A 1 413 ? 5.670   -9.627  -1.457  1.00 72.33  ? 413 GLN   A O    1 
ATOM   3241 C CB   . GLN   A 1 413 ? 8.581   -10.198 -1.806  1.00 73.69  ? 413 GLN   A CB   1 
ATOM   3242 C CG   . GLN   A 1 413 ? 9.474   -11.325 -2.373  1.00 79.46  ? 413 GLN   A CG   1 
ATOM   3243 C CD   . GLN   A 1 413 ? 8.776   -12.681 -2.394  1.00 79.40  ? 413 GLN   A CD   1 
ATOM   3244 O OE1  . GLN   A 1 413 ? 8.771   -13.386 -3.400  1.00 74.01  ? 413 GLN   A OE1  1 
ATOM   3245 N NE2  . GLN   A 1 413 ? 8.184   -13.050 -1.260  1.00 84.09  ? 413 GLN   A NE2  1 
ATOM   3246 N N    . TYR   A 1 414 ? 6.174   -7.708  -2.501  1.00 67.14  ? 414 TYR   A N    1 
ATOM   3247 C CA   . TYR   A 1 414 ? 4.992   -6.995  -2.024  1.00 65.58  ? 414 TYR   A CA   1 
ATOM   3248 C C    . TYR   A 1 414 ? 3.913   -7.101  -3.091  1.00 67.30  ? 414 TYR   A C    1 
ATOM   3249 O O    . TYR   A 1 414 ? 3.814   -6.271  -3.998  1.00 66.18  ? 414 TYR   A O    1 
ATOM   3250 C CB   . TYR   A 1 414 ? 5.345   -5.543  -1.717  1.00 64.94  ? 414 TYR   A CB   1 
ATOM   3251 C CG   . TYR   A 1 414 ? 6.414   -5.372  -0.641  1.00 68.74  ? 414 TYR   A CG   1 
ATOM   3252 C CD1  . TYR   A 1 414 ? 6.189   -5.785  0.670   1.00 67.38  ? 414 TYR   A CD1  1 
ATOM   3253 C CD2  . TYR   A 1 414 ? 7.658   -4.824  -0.945  1.00 70.02  ? 414 TYR   A CD2  1 
ATOM   3254 C CE1  . TYR   A 1 414 ? 7.164   -5.637  1.655   1.00 67.67  ? 414 TYR   A CE1  1 
ATOM   3255 C CE2  . TYR   A 1 414 ? 8.646   -4.677  0.035   1.00 67.54  ? 414 TYR   A CE2  1 
ATOM   3256 C CZ   . TYR   A 1 414 ? 8.388   -5.089  1.334   1.00 72.52  ? 414 TYR   A CZ   1 
ATOM   3257 O OH   . TYR   A 1 414 ? 9.337   -4.954  2.334   1.00 76.27  ? 414 TYR   A OH   1 
ATOM   3258 N N    . VAL   A 1 415 ? 3.116   -8.166  -3.004  1.00 64.55  ? 415 VAL   A N    1 
ATOM   3259 C CA   . VAL   A 1 415 ? 2.035   -8.425  -3.947  1.00 65.62  ? 415 VAL   A CA   1 
ATOM   3260 C C    . VAL   A 1 415 ? 0.754   -8.684  -3.164  1.00 63.64  ? 415 VAL   A C    1 
ATOM   3261 O O    . VAL   A 1 415 ? 0.732   -9.520  -2.255  1.00 65.26  ? 415 VAL   A O    1 
ATOM   3262 C CB   . VAL   A 1 415 ? 2.375   -9.604  -4.881  1.00 67.82  ? 415 VAL   A CB   1 
ATOM   3263 C CG1  . VAL   A 1 415 ? 1.244   -9.863  -5.884  1.00 63.52  ? 415 VAL   A CG1  1 
ATOM   3264 C CG2  . VAL   A 1 415 ? 3.686   -9.331  -5.609  1.00 65.76  ? 415 VAL   A CG2  1 
ATOM   3265 N N    . PHE   A 1 416 ? -0.315  -7.985  -3.526  1.00 66.63  ? 416 PHE   A N    1 
ATOM   3266 C CA   . PHE   A 1 416 ? -1.540  -8.000  -2.740  1.00 64.00  ? 416 PHE   A CA   1 
ATOM   3267 C C    . PHE   A 1 416 ? -2.642  -8.718  -3.504  1.00 67.59  ? 416 PHE   A C    1 
ATOM   3268 O O    . PHE   A 1 416 ? -3.010  -8.292  -4.614  1.00 65.85  ? 416 PHE   A O    1 
ATOM   3269 C CB   . PHE   A 1 416 ? -1.938  -6.572  -2.394  1.00 62.98  ? 416 PHE   A CB   1 
ATOM   3270 C CG   . PHE   A 1 416 ? -0.772  -5.746  -1.901  1.00 65.30  ? 416 PHE   A CG   1 
ATOM   3271 C CD1  . PHE   A 1 416 ? -0.206  -5.998  -0.649  1.00 61.30  ? 416 PHE   A CD1  1 
ATOM   3272 C CD2  . PHE   A 1 416 ? -0.201  -4.762  -2.707  1.00 63.95  ? 416 PHE   A CD2  1 
ATOM   3273 C CE1  . PHE   A 1 416 ? 0.882   -5.261  -0.205  1.00 61.04  ? 416 PHE   A CE1  1 
ATOM   3274 C CE2  . PHE   A 1 416 ? 0.892   -4.021  -2.255  1.00 61.70  ? 416 PHE   A CE2  1 
ATOM   3275 C CZ   . PHE   A 1 416 ? 1.422   -4.268  -1.006  1.00 62.83  ? 416 PHE   A CZ   1 
ATOM   3276 N N    . PRO   A 1 417 ? -3.158  -9.832  -2.975  1.00 63.77  ? 417 PRO   A N    1 
ATOM   3277 C CA   . PRO   A 1 417 ? -4.102  -10.656 -3.751  1.00 60.69  ? 417 PRO   A CA   1 
ATOM   3278 C C    . PRO   A 1 417 ? -5.515  -10.089 -3.664  1.00 56.70  ? 417 PRO   A C    1 
ATOM   3279 O O    . PRO   A 1 417 ? -6.022  -9.818  -2.575  1.00 58.43  ? 417 PRO   A O    1 
ATOM   3280 C CB   . PRO   A 1 417 ? -4.001  -12.032 -3.079  1.00 60.15  ? 417 PRO   A CB   1 
ATOM   3281 C CG   . PRO   A 1 417 ? -3.640  -11.711 -1.659  1.00 56.61  ? 417 PRO   A CG   1 
ATOM   3282 C CD   . PRO   A 1 417 ? -2.812  -10.446 -1.676  1.00 57.73  ? 417 PRO   A CD   1 
ATOM   3283 N N    . GLU   A 1 418 ? -6.149  -9.904  -4.820  1.00 59.57  ? 418 GLU   A N    1 
ATOM   3284 C CA   . GLU   A 1 418 ? -7.472  -9.299  -4.912  1.00 56.17  ? 418 GLU   A CA   1 
ATOM   3285 C C    . GLU   A 1 418 ? -8.437  -10.250 -5.599  1.00 55.49  ? 418 GLU   A C    1 
ATOM   3286 O O    . GLU   A 1 418 ? -8.091  -10.884 -6.599  1.00 60.45  ? 418 GLU   A O    1 
ATOM   3287 C CB   . GLU   A 1 418 ? -7.445  -7.987  -5.690  1.00 51.49  ? 418 GLU   A CB   1 
ATOM   3288 C CG   . GLU   A 1 418 ? -6.441  -6.958  -5.198  1.00 49.75  ? 418 GLU   A CG   1 
ATOM   3289 C CD   . GLU   A 1 418 ? -6.624  -5.625  -5.918  1.00 53.66  ? 418 GLU   A CD   1 
ATOM   3290 O OE1  . GLU   A 1 418 ? -6.396  -5.559  -7.172  1.00 51.78  ? 418 GLU   A OE1  1 
ATOM   3291 O OE2  . GLU   A 1 418 ? -7.009  -4.661  -5.232  1.00 48.78  ? 418 GLU   A OE2  1 
ATOM   3292 N N    . VAL   A 1 419 ? -9.635  -10.369 -5.040  1.00 53.26  ? 419 VAL   A N    1 
ATOM   3293 C CA   . VAL   A 1 419 ? -10.748 -11.041 -5.697  1.00 56.61  ? 419 VAL   A CA   1 
ATOM   3294 C C    . VAL   A 1 419 ? -11.975 -10.186 -5.435  1.00 56.30  ? 419 VAL   A C    1 
ATOM   3295 O O    . VAL   A 1 419 ? -12.305 -9.921  -4.276  1.00 52.23  ? 419 VAL   A O    1 
ATOM   3296 C CB   . VAL   A 1 419 ? -10.966 -12.473 -5.184  1.00 57.63  ? 419 VAL   A CB   1 
ATOM   3297 C CG1  . VAL   A 1 419 ? -11.974 -13.187 -6.069  1.00 57.69  ? 419 VAL   A CG1  1 
ATOM   3298 C CG2  . VAL   A 1 419 ? -9.641  -13.236 -5.135  1.00 54.91  ? 419 VAL   A CG2  1 
ATOM   3299 N N    . LEU   A 1 420 ? -12.623 -9.709  -6.490  1.00 53.75  ? 420 LEU   A N    1 
ATOM   3300 C CA   . LEU   A 1 420 ? -13.805 -8.878  -6.324  1.00 50.23  ? 420 LEU   A CA   1 
ATOM   3301 C C    . LEU   A 1 420 ? -14.962 -9.483  -7.104  1.00 58.85  ? 420 LEU   A C    1 
ATOM   3302 O O    . LEU   A 1 420 ? -14.804 -9.875  -8.269  1.00 57.94  ? 420 LEU   A O    1 
ATOM   3303 C CB   . LEU   A 1 420 ? -13.526 -7.436  -6.775  1.00 49.95  ? 420 LEU   A CB   1 
ATOM   3304 C CG   . LEU   A 1 420 ? -14.631 -6.397  -6.549  1.00 52.43  ? 420 LEU   A CG   1 
ATOM   3305 C CD1  . LEU   A 1 420 ? -15.148 -6.462  -5.135  1.00 51.42  ? 420 LEU   A CD1  1 
ATOM   3306 C CD2  . LEU   A 1 420 ? -14.198 -4.968  -6.904  1.00 47.67  ? 420 LEU   A CD2  1 
ATOM   3307 N N    . LEU   A 1 421 ? -16.133 -9.535  -6.483  1.00 59.72  ? 421 LEU   A N    1 
ATOM   3308 C CA   . LEU   A 1 421 ? -17.299 -10.082 -7.158  1.00 62.10  ? 421 LEU   A CA   1 
ATOM   3309 C C    . LEU   A 1 421 ? -18.226 -8.952  -7.583  1.00 61.91  ? 421 LEU   A C    1 
ATOM   3310 O O    . LEU   A 1 421 ? -18.136 -7.822  -7.088  1.00 60.02  ? 421 LEU   A O    1 
ATOM   3311 C CB   . LEU   A 1 421 ? -18.040 -11.083 -6.266  1.00 65.00  ? 421 LEU   A CB   1 
ATOM   3312 C CG   . LEU   A 1 421 ? -17.158 -12.203 -5.691  1.00 65.95  ? 421 LEU   A CG   1 
ATOM   3313 C CD1  . LEU   A 1 421 ? -17.933 -13.064 -4.687  1.00 65.77  ? 421 LEU   A CD1  1 
ATOM   3314 C CD2  . LEU   A 1 421 ? -16.555 -13.061 -6.787  1.00 68.11  ? 421 LEU   A CD2  1 
ATOM   3315 N N    . SER   A 1 422 ? -19.112 -9.271  -8.534  1.00 62.62  ? 422 SER   A N    1 
ATOM   3316 C CA   . SER   A 1 422 ? -20.098 -8.311  -9.014  1.00 59.00  ? 422 SER   A CA   1 
ATOM   3317 C C    . SER   A 1 422 ? -20.726 -7.580  -7.834  1.00 62.20  ? 422 SER   A C    1 
ATOM   3318 O O    . SER   A 1 422 ? -20.955 -8.170  -6.769  1.00 60.89  ? 422 SER   A O    1 
ATOM   3319 C CB   . SER   A 1 422 ? -21.173 -9.036  -9.836  1.00 60.88  ? 422 SER   A CB   1 
ATOM   3320 O OG   . SER   A 1 422 ? -22.262 -8.184  -10.151 1.00 58.14  ? 422 SER   A OG   1 
ATOM   3321 N N    . GLU   A 1 423 ? -20.979 -6.283  -8.025  1.00 69.29  ? 423 GLU   A N    1 
ATOM   3322 C CA   . GLU   A 1 423 ? -21.511 -5.408  -6.989  1.00 67.05  ? 423 GLU   A CA   1 
ATOM   3323 C C    . GLU   A 1 423 ? -20.483 -5.081  -5.907  1.00 69.66  ? 423 GLU   A C    1 
ATOM   3324 O O    . GLU   A 1 423 ? -20.850 -4.647  -4.802  1.00 64.99  ? 423 GLU   A O    1 
ATOM   3325 C CB   . GLU   A 1 423 ? -22.769 -6.020  -6.366  1.00 75.90  ? 423 GLU   A CB   1 
ATOM   3326 C CG   . GLU   A 1 423 ? -24.007 -5.891  -7.246  1.00 75.43  ? 423 GLU   A CG   1 
ATOM   3327 C CD   . GLU   A 1 423 ? -24.381 -4.445  -7.519  1.00 80.65  ? 423 GLU   A CD   1 
ATOM   3328 O OE1  . GLU   A 1 423 ? -23.479 -3.573  -7.589  1.00 80.09  ? 423 GLU   A OE1  1 
ATOM   3329 O OE2  . GLU   A 1 423 ? -25.595 -4.179  -7.640  1.00 86.86  ? 423 GLU   A OE2  1 
ATOM   3330 N N    . ASN   A 1 424 ? -19.196 -5.290  -6.210  1.00 62.36  ? 424 ASN   A N    1 
ATOM   3331 C CA   . ASN   A 1 424 ? -18.095 -4.885  -5.340  1.00 59.72  ? 424 ASN   A CA   1 
ATOM   3332 C C    . ASN   A 1 424 ? -18.116 -5.680  -4.032  1.00 64.39  ? 424 ASN   A C    1 
ATOM   3333 O O    . ASN   A 1 424 ? -17.954 -5.138  -2.937  1.00 61.32  ? 424 ASN   A O    1 
ATOM   3334 C CB   . ASN   A 1 424 ? -18.135 -3.380  -5.078  1.00 57.72  ? 424 ASN   A CB   1 
ATOM   3335 C CG   . ASN   A 1 424 ? -16.754 -2.780  -4.970  1.00 60.66  ? 424 ASN   A CG   1 
ATOM   3336 O OD1  . ASN   A 1 424 ? -16.353 -1.975  -5.809  1.00 64.06  ? 424 ASN   A OD1  1 
ATOM   3337 N ND2  . ASN   A 1 424 ? -16.008 -3.177  -3.938  1.00 56.44  ? 424 ASN   A ND2  1 
ATOM   3338 N N    . GLN   A 1 425 ? -18.302 -6.989  -4.162  1.00 56.93  ? 425 GLN   A N    1 
ATOM   3339 C CA   . GLN   A 1 425 ? -18.376 -7.886  -3.024  1.00 55.82  ? 425 GLN   A CA   1 
ATOM   3340 C C    . GLN   A 1 425 ? -17.061 -8.631  -2.875  1.00 55.66  ? 425 GLN   A C    1 
ATOM   3341 O O    . GLN   A 1 425 ? -16.479 -9.087  -3.859  1.00 57.02  ? 425 GLN   A O    1 
ATOM   3342 C CB   . GLN   A 1 425 ? -19.517 -8.888  -3.191  1.00 55.38  ? 425 GLN   A CB   1 
ATOM   3343 C CG   . GLN   A 1 425 ? -20.863 -8.232  -3.386  1.00 56.03  ? 425 GLN   A CG   1 
ATOM   3344 C CD   . GLN   A 1 425 ? -21.235 -7.335  -2.228  1.00 57.64  ? 425 GLN   A CD   1 
ATOM   3345 O OE1  . GLN   A 1 425 ? -21.195 -7.751  -1.062  1.00 61.48  ? 425 GLN   A OE1  1 
ATOM   3346 N NE2  . GLN   A 1 425 ? -21.621 -6.110  -2.537  1.00 58.61  ? 425 GLN   A NE2  1 
ATOM   3347 N N    . LEU   A 1 426 ? -16.599 -8.753  -1.634  1.00 50.10  ? 426 LEU   A N    1 
ATOM   3348 C CA   . LEU   A 1 426 ? -15.421 -9.553  -1.359  1.00 48.52  ? 426 LEU   A CA   1 
ATOM   3349 C C    . LEU   A 1 426 ? -15.794 -11.028 -1.393  1.00 50.48  ? 426 LEU   A C    1 
ATOM   3350 O O    . LEU   A 1 426 ? -16.971 -11.398 -1.377  1.00 52.51  ? 426 LEU   A O    1 
ATOM   3351 C CB   . LEU   A 1 426 ? -14.812 -9.168  -0.011  1.00 46.96  ? 426 LEU   A CB   1 
ATOM   3352 C CG   . LEU   A 1 426 ? -14.233 -7.752  0.033   1.00 43.30  ? 426 LEU   A CG   1 
ATOM   3353 C CD1  . LEU   A 1 426 ? -13.401 -7.526  1.303   1.00 42.89  ? 426 LEU   A CD1  1 
ATOM   3354 C CD2  . LEU   A 1 426 ? -13.397 -7.474  -1.236  1.00 42.03  ? 426 LEU   A CD2  1 
ATOM   3355 N N    . ALA   A 1 427 ? -14.779 -11.880 -1.462  1.00 54.59  ? 427 ALA   A N    1 
ATOM   3356 C CA   . ALA   A 1 427 ? -14.987 -13.324 -1.523  1.00 59.25  ? 427 ALA   A CA   1 
ATOM   3357 C C    . ALA   A 1 427 ? -14.256 -14.025 -0.380  1.00 58.22  ? 427 ALA   A C    1 
ATOM   3358 O O    . ALA   A 1 427 ? -13.405 -14.890 -0.607  1.00 60.46  ? 427 ALA   A O    1 
ATOM   3359 C CB   . ALA   A 1 427 ? -14.533 -13.856 -2.880  1.00 60.47  ? 427 ALA   A CB   1 
ATOM   3360 N N    . PRO   A 1 428 ? -14.597 -13.708 0.868   1.00 62.94  ? 428 PRO   A N    1 
ATOM   3361 C CA   . PRO   A 1 428 ? -13.847 -14.278 2.001   1.00 61.33  ? 428 PRO   A CA   1 
ATOM   3362 C C    . PRO   A 1 428 ? -13.942 -15.797 2.028   1.00 63.31  ? 428 PRO   A C    1 
ATOM   3363 O O    . PRO   A 1 428 ? -15.028 -16.370 1.913   1.00 67.95  ? 428 PRO   A O    1 
ATOM   3364 C CB   . PRO   A 1 428 ? -14.519 -13.651 3.229   1.00 59.46  ? 428 PRO   A CB   1 
ATOM   3365 C CG   . PRO   A 1 428 ? -15.877 -13.280 2.799   1.00 58.56  ? 428 PRO   A CG   1 
ATOM   3366 C CD   . PRO   A 1 428 ? -15.736 -12.887 1.321   1.00 62.99  ? 428 PRO   A CD   1 
ATOM   3367 N N    . GLY   A 1 429 ? -12.789 -16.453 2.138   1.00 58.28  ? 429 GLY   A N    1 
ATOM   3368 C CA   . GLY   A 1 429 ? -12.757 -17.898 2.253   1.00 61.85  ? 429 GLY   A CA   1 
ATOM   3369 C C    . GLY   A 1 429 ? -13.012 -18.673 0.972   1.00 65.58  ? 429 GLY   A C    1 
ATOM   3370 O O    . GLY   A 1 429 ? -13.017 -19.913 1.012   1.00 68.43  ? 429 GLY   A O    1 
ATOM   3371 N N    . GLU   A 1 430 ? -13.209 -17.998 -0.163  1.00 69.98  ? 430 GLU   A N    1 
ATOM   3372 C CA   . GLU   A 1 430 ? -13.435 -18.680 -1.430  1.00 75.79  ? 430 GLU   A CA   1 
ATOM   3373 C C    . GLU   A 1 430 ? -12.158 -18.895 -2.223  1.00 76.83  ? 430 GLU   A C    1 
ATOM   3374 O O    . GLU   A 1 430 ? -12.203 -19.562 -3.264  1.00 80.76  ? 430 GLU   A O    1 
ATOM   3375 C CB   . GLU   A 1 430 ? -14.424 -17.901 -2.303  1.00 73.81  ? 430 GLU   A CB   1 
ATOM   3376 C CG   . GLU   A 1 430 ? -15.699 -17.512 -1.616  1.00 73.18  ? 430 GLU   A CG   1 
ATOM   3377 C CD   . GLU   A 1 430 ? -16.789 -17.104 -2.593  1.00 81.55  ? 430 GLU   A CD   1 
ATOM   3378 O OE1  . GLU   A 1 430 ? -16.709 -17.465 -3.800  1.00 82.98  ? 430 GLU   A OE1  1 
ATOM   3379 O OE2  . GLU   A 1 430 ? -17.720 -16.398 -2.151  1.00 81.12  ? 430 GLU   A OE2  1 
ATOM   3380 N N    . PHE   A 1 431 ? -11.025 -18.374 -1.754  1.00 67.36  ? 431 PHE   A N    1 
ATOM   3381 C CA   . PHE   A 1 431 ? -9.780  -18.482 -2.499  1.00 69.56  ? 431 PHE   A CA   1 
ATOM   3382 C C    . PHE   A 1 431 ? -8.622  -18.610 -1.526  1.00 69.74  ? 431 PHE   A C    1 
ATOM   3383 O O    . PHE   A 1 431 ? -8.759  -18.373 -0.327  1.00 69.33  ? 431 PHE   A O    1 
ATOM   3384 C CB   . PHE   A 1 431 ? -9.565  -17.276 -3.428  1.00 68.61  ? 431 PHE   A CB   1 
ATOM   3385 C CG   . PHE   A 1 431 ? -9.473  -15.962 -2.706  1.00 66.87  ? 431 PHE   A CG   1 
ATOM   3386 C CD1  . PHE   A 1 431 ? -10.618 -15.234 -2.408  1.00 64.12  ? 431 PHE   A CD1  1 
ATOM   3387 C CD2  . PHE   A 1 431 ? -8.244  -15.451 -2.316  1.00 65.92  ? 431 PHE   A CD2  1 
ATOM   3388 C CE1  . PHE   A 1 431 ? -10.536 -14.019 -1.727  1.00 60.72  ? 431 PHE   A CE1  1 
ATOM   3389 C CE2  . PHE   A 1 431 ? -8.159  -14.231 -1.645  1.00 61.63  ? 431 PHE   A CE2  1 
ATOM   3390 C CZ   . PHE   A 1 431 ? -9.307  -13.518 -1.353  1.00 58.60  ? 431 PHE   A CZ   1 
ATOM   3391 N N    . GLN   A 1 432 ? -7.471  -18.987 -2.069  1.00 79.87  ? 432 GLN   A N    1 
ATOM   3392 C CA   . GLN   A 1 432 ? -6.264  -19.117 -1.276  1.00 75.37  ? 432 GLN   A CA   1 
ATOM   3393 C C    . GLN   A 1 432 ? -5.064  -18.680 -2.097  1.00 80.72  ? 432 GLN   A C    1 
ATOM   3394 O O    . GLN   A 1 432 ? -5.116  -18.594 -3.329  1.00 79.59  ? 432 GLN   A O    1 
ATOM   3395 C CB   . GLN   A 1 432 ? -6.065  -20.547 -0.793  1.00 81.08  ? 432 GLN   A CB   1 
ATOM   3396 C CG   . GLN   A 1 432 ? -5.202  -20.644 0.453   1.00 82.35  ? 432 GLN   A CG   1 
ATOM   3397 C CD   . GLN   A 1 432 ? -5.057  -22.063 0.927   1.00 82.59  ? 432 GLN   A CD   1 
ATOM   3398 O OE1  . GLN   A 1 432 ? -5.926  -22.575 1.627   1.00 93.03  ? 432 GLN   A OE1  1 
ATOM   3399 N NE2  . GLN   A 1 432 ? -3.955  -22.712 0.555   1.00 87.57  ? 432 GLN   A NE2  1 
ATOM   3400 N N    . VAL   A 1 433 ? -3.980  -18.388 -1.384  1.00 74.21  ? 433 VAL   A N    1 
ATOM   3401 C CA   . VAL   A 1 433 ? -2.681  -18.120 -1.982  1.00 69.65  ? 433 VAL   A CA   1 
ATOM   3402 C C    . VAL   A 1 433 ? -1.752  -19.242 -1.557  1.00 74.44  ? 433 VAL   A C    1 
ATOM   3403 O O    . VAL   A 1 433 ? -1.679  -19.580 -0.364  1.00 72.52  ? 433 VAL   A O    1 
ATOM   3404 C CB   . VAL   A 1 433 ? -2.127  -16.748 -1.553  1.00 66.27  ? 433 VAL   A CB   1 
ATOM   3405 C CG1  . VAL   A 1 433 ? -0.679  -16.600 -1.981  1.00 66.15  ? 433 VAL   A CG1  1 
ATOM   3406 C CG2  . VAL   A 1 433 ? -2.975  -15.627 -2.108  1.00 61.94  ? 433 VAL   A CG2  1 
ATOM   3407 N N    . SER   A 1 434 ? -1.056  -19.828 -2.532  1.00 82.85  ? 434 SER   A N    1 
ATOM   3408 C CA   . SER   A 1 434 ? -0.077  -20.875 -2.284  1.00 85.58  ? 434 SER   A CA   1 
ATOM   3409 C C    . SER   A 1 434 ? 1.294   -20.248 -2.032  1.00 86.67  ? 434 SER   A C    1 
ATOM   3410 O O    . SER   A 1 434 ? 1.532   -19.073 -2.318  1.00 87.15  ? 434 SER   A O    1 
ATOM   3411 C CB   . SER   A 1 434 ? -0.020  -21.860 -3.460  1.00 84.86  ? 434 SER   A CB   1 
ATOM   3412 O OG   . SER   A 1 434 ? 0.642   -21.306 -4.583  1.00 83.56  ? 434 SER   A OG   1 
ATOM   3413 N N    . THR   A 1 435 ? 2.218   -21.052 -1.506  1.00 84.18  ? 435 THR   A N    1 
ATOM   3414 C CA   . THR   A 1 435 ? 3.532   -20.507 -1.190  1.00 84.66  ? 435 THR   A CA   1 
ATOM   3415 C C    . THR   A 1 435 ? 4.349   -20.178 -2.435  1.00 86.51  ? 435 THR   A C    1 
ATOM   3416 O O    . THR   A 1 435 ? 5.238   -19.320 -2.364  1.00 84.35  ? 435 THR   A O    1 
ATOM   3417 C CB   . THR   A 1 435 ? 4.312   -21.480 -0.314  1.00 87.62  ? 435 THR   A CB   1 
ATOM   3418 O OG1  . THR   A 1 435 ? 3.392   -22.222 0.493   1.00 86.76  ? 435 THR   A OG1  1 
ATOM   3419 C CG2  . THR   A 1 435 ? 5.278   -20.716 0.577   1.00 85.75  ? 435 THR   A CG2  1 
ATOM   3420 N N    . ASP   A 1 436 ? 4.054   -20.812 -3.573  1.00 107.93 ? 436 ASP   A N    1 
ATOM   3421 C CA   . ASP   A 1 436 ? 4.760   -20.540 -4.819  1.00 107.03 ? 436 ASP   A CA   1 
ATOM   3422 C C    . ASP   A 1 436 ? 4.099   -19.442 -5.646  1.00 104.44 ? 436 ASP   A C    1 
ATOM   3423 O O    . ASP   A 1 436 ? 4.507   -19.213 -6.789  1.00 107.20 ? 436 ASP   A O    1 
ATOM   3424 C CB   . ASP   A 1 436 ? 4.885   -21.825 -5.653  1.00 103.88 ? 436 ASP   A CB   1 
ATOM   3425 C CG   . ASP   A 1 436 ? 3.537   -22.494 -5.922  1.00 108.49 ? 436 ASP   A CG   1 
ATOM   3426 O OD1  . ASP   A 1 436 ? 2.538   -22.124 -5.268  1.00 108.07 ? 436 ASP   A OD1  1 
ATOM   3427 O OD2  . ASP   A 1 436 ? 3.475   -23.397 -6.787  1.00 109.21 ? 436 ASP   A OD2  1 
ATOM   3428 N N    . GLY   A 1 437 ? 3.108   -18.749 -5.092  1.00 83.67  ? 437 GLY   A N    1 
ATOM   3429 C CA   . GLY   A 1 437 ? 2.604   -17.523 -5.681  1.00 79.81  ? 437 GLY   A CA   1 
ATOM   3430 C C    . GLY   A 1 437 ? 1.371   -17.635 -6.551  1.00 79.81  ? 437 GLY   A C    1 
ATOM   3431 O O    . GLY   A 1 437 ? 1.176   -16.776 -7.424  1.00 80.71  ? 437 GLY   A O    1 
ATOM   3432 N N    . ARG   A 1 438 ? 0.544   -18.654 -6.360  1.00 82.61  ? 438 ARG   A N    1 
ATOM   3433 C CA   . ARG   A 1 438 ? -0.700  -18.791 -7.104  1.00 82.21  ? 438 ARG   A CA   1 
ATOM   3434 C C    . ARG   A 1 438 ? -1.854  -18.319 -6.239  1.00 81.66  ? 438 ARG   A C    1 
ATOM   3435 O O    . ARG   A 1 438 ? -1.977  -18.730 -5.080  1.00 77.07  ? 438 ARG   A O    1 
ATOM   3436 C CB   . ARG   A 1 438 ? -0.949  -20.236 -7.526  1.00 83.77  ? 438 ARG   A CB   1 
ATOM   3437 C CG   . ARG   A 1 438 ? -0.121  -20.698 -8.673  1.00 85.34  ? 438 ARG   A CG   1 
ATOM   3438 C CD   . ARG   A 1 438 ? -0.083  -22.215 -8.697  1.00 91.43  ? 438 ARG   A CD   1 
ATOM   3439 N NE   . ARG   A 1 438 ? -1.394  -22.833 -8.519  1.00 93.26  ? 438 ARG   A NE   1 
ATOM   3440 C CZ   . ARG   A 1 438 ? -1.653  -23.824 -7.674  1.00 93.40  ? 438 ARG   A CZ   1 
ATOM   3441 N NH1  . ARG   A 1 438 ? -0.718  -24.317 -6.875  1.00 90.96  ? 438 ARG   A NH1  1 
ATOM   3442 N NH2  . ARG   A 1 438 ? -2.877  -24.350 -7.648  1.00 88.99  ? 438 ARG   A NH2  1 
ATOM   3443 N N    . LEU   A 1 439 ? -2.685  -17.455 -6.802  1.00 71.45  ? 439 LEU   A N    1 
ATOM   3444 C CA   . LEU   A 1 439 ? -3.955  -17.086 -6.202  1.00 68.91  ? 439 LEU   A CA   1 
ATOM   3445 C C    . LEU   A 1 439 ? -5.022  -17.891 -6.926  1.00 73.88  ? 439 LEU   A C    1 
ATOM   3446 O O    . LEU   A 1 439 ? -5.190  -17.747 -8.146  1.00 70.66  ? 439 LEU   A O    1 
ATOM   3447 C CB   . LEU   A 1 439 ? -4.201  -15.583 -6.318  1.00 69.06  ? 439 LEU   A CB   1 
ATOM   3448 C CG   . LEU   A 1 439 ? -5.642  -15.080 -6.207  1.00 68.54  ? 439 LEU   A CG   1 
ATOM   3449 C CD1  . LEU   A 1 439 ? -6.290  -15.521 -4.897  1.00 66.89  ? 439 LEU   A CD1  1 
ATOM   3450 C CD2  . LEU   A 1 439 ? -5.701  -13.571 -6.364  1.00 64.60  ? 439 LEU   A CD2  1 
ATOM   3451 N N    . PHE   A 1 440 ? -5.716  -18.761 -6.200  1.00 73.46  ? 440 PHE   A N    1 
ATOM   3452 C CA   . PHE   A 1 440 ? -6.595  -19.706 -6.869  1.00 75.26  ? 440 PHE   A CA   1 
ATOM   3453 C C    . PHE   A 1 440 ? -7.874  -19.900 -6.067  1.00 78.33  ? 440 PHE   A C    1 
ATOM   3454 O O    . PHE   A 1 440 ? -7.965  -19.550 -4.887  1.00 72.24  ? 440 PHE   A O    1 
ATOM   3455 C CB   . PHE   A 1 440 ? -5.891  -21.054 -7.098  1.00 74.00  ? 440 PHE   A CB   1 
ATOM   3456 C CG   . PHE   A 1 440 ? -5.517  -21.779 -5.824  1.00 79.19  ? 440 PHE   A CG   1 
ATOM   3457 C CD1  . PHE   A 1 440 ? -4.437  -21.357 -5.054  1.00 77.44  ? 440 PHE   A CD1  1 
ATOM   3458 C CD2  . PHE   A 1 440 ? -6.236  -22.894 -5.405  1.00 78.13  ? 440 PHE   A CD2  1 
ATOM   3459 C CE1  . PHE   A 1 440 ? -4.083  -22.026 -3.886  1.00 80.34  ? 440 PHE   A CE1  1 
ATOM   3460 C CE2  . PHE   A 1 440 ? -5.886  -23.572 -4.239  1.00 78.14  ? 440 PHE   A CE2  1 
ATOM   3461 C CZ   . PHE   A 1 440 ? -4.810  -23.133 -3.477  1.00 80.59  ? 440 PHE   A CZ   1 
ATOM   3462 N N    . SER   A 1 441 ? -8.871  -20.462 -6.745  1.00 84.15  ? 441 SER   A N    1 
ATOM   3463 C CA   . SER   A 1 441 ? -10.211 -20.605 -6.197  1.00 83.88  ? 441 SER   A CA   1 
ATOM   3464 C C    . SER   A 1 441 ? -10.302 -21.892 -5.393  1.00 81.67  ? 441 SER   A C    1 
ATOM   3465 O O    . SER   A 1 441 ? -9.849  -22.950 -5.844  1.00 85.94  ? 441 SER   A O    1 
ATOM   3466 C CB   . SER   A 1 441 ? -11.244 -20.604 -7.323  1.00 81.68  ? 441 SER   A CB   1 
ATOM   3467 O OG   . SER   A 1 441 ? -11.155 -21.802 -8.075  1.00 85.73  ? 441 SER   A OG   1 
ATOM   3468 N N    . LEU   A 1 442 ? -10.866 -21.801 -4.198  1.00 77.25  ? 442 LEU   A N    1 
ATOM   3469 C CA   . LEU   A 1 442 ? -11.103 -23.001 -3.403  1.00 81.19  ? 442 LEU   A CA   1 
ATOM   3470 C C    . LEU   A 1 442 ? -12.393 -23.706 -3.790  1.00 81.99  ? 442 LEU   A C    1 
ATOM   3471 O O    . LEU   A 1 442 ? -12.633 -24.828 -3.341  1.00 86.22  ? 442 LEU   A O    1 
ATOM   3472 C CB   . LEU   A 1 442 ? -11.129 -22.638 -1.922  1.00 76.35  ? 442 LEU   A CB   1 
ATOM   3473 C CG   . LEU   A 1 442 ? -9.931  -23.064 -1.077  1.00 79.08  ? 442 LEU   A CG   1 
ATOM   3474 C CD1  . LEU   A 1 442 ? -8.612  -22.649 -1.712  1.00 79.59  ? 442 LEU   A CD1  1 
ATOM   3475 C CD2  . LEU   A 1 442 ? -10.086 -22.390 0.256   1.00 77.90  ? 442 LEU   A CD2  1 
ATOM   3476 N N    . LYS   A 1 443 ? -13.220 -23.074 -4.596  1.00 88.94  ? 443 LYS   A N    1 
ATOM   3477 C CA   . LYS   A 1 443 ? -14.512 -23.596 -5.009  1.00 90.36  ? 443 LYS   A CA   1 
ATOM   3478 C C    . LYS   A 1 443 ? -15.073 -22.634 -6.051  1.00 88.34  ? 443 LYS   A C    1 
ATOM   3479 O O    . LYS   A 1 443 ? -14.490 -21.569 -6.280  1.00 83.49  ? 443 LYS   A O    1 
ATOM   3480 C CB   . LYS   A 1 443 ? -15.448 -23.739 -3.802  1.00 90.20  ? 443 LYS   A CB   1 
ATOM   3481 C CG   . LYS   A 1 443 ? -15.720 -22.418 -3.078  1.00 91.30  ? 443 LYS   A CG   1 
ATOM   3482 C CD   . LYS   A 1 443 ? -17.018 -22.474 -2.287  1.00 93.42  ? 443 LYS   A CD   1 
ATOM   3483 C CE   . LYS   A 1 443 ? -16.937 -21.615 -1.038  1.00 91.20  ? 443 LYS   A CE   1 
ATOM   3484 N NZ   . LYS   A 1 443 ? -15.638 -21.805 -0.348  1.00 88.41  ? 443 LYS   A NZ   1 
ATOM   3485 N N    . PRO   A 1 444 ? -16.181 -22.967 -6.711  1.00 95.62  ? 444 PRO   A N    1 
ATOM   3486 C CA   . PRO   A 1 444 ? -16.774 -21.998 -7.636  1.00 90.48  ? 444 PRO   A CA   1 
ATOM   3487 C C    . PRO   A 1 444 ? -17.155 -20.718 -6.911  1.00 88.36  ? 444 PRO   A C    1 
ATOM   3488 O O    . PRO   A 1 444 ? -17.632 -20.743 -5.775  1.00 90.84  ? 444 PRO   A O    1 
ATOM   3489 C CB   . PRO   A 1 444 ? -17.999 -22.739 -8.178  1.00 90.71  ? 444 PRO   A CB   1 
ATOM   3490 C CG   . PRO   A 1 444 ? -18.427 -23.613 -7.065  1.00 93.36  ? 444 PRO   A CG   1 
ATOM   3491 C CD   . PRO   A 1 444 ? -17.199 -23.925 -6.215  1.00 95.60  ? 444 PRO   A CD   1 
ATOM   3492 N N    . THR   A 1 445 ? -16.928 -19.590 -7.578  1.00 75.30  ? 445 THR   A N    1 
ATOM   3493 C CA   . THR   A 1 445 ? -17.207 -18.305 -6.958  1.00 72.88  ? 445 THR   A CA   1 
ATOM   3494 C C    . THR   A 1 445 ? -18.693 -18.206 -6.624  1.00 73.27  ? 445 THR   A C    1 
ATOM   3495 O O    . THR   A 1 445 ? -19.551 -18.717 -7.349  1.00 79.30  ? 445 THR   A O    1 
ATOM   3496 C CB   . THR   A 1 445 ? -16.785 -17.158 -7.879  1.00 69.54  ? 445 THR   A CB   1 
ATOM   3497 O OG1  . THR   A 1 445 ? -17.612 -17.149 -9.047  1.00 74.43  ? 445 THR   A OG1  1 
ATOM   3498 C CG2  . THR   A 1 445 ? -15.325 -17.308 -8.299  1.00 67.39  ? 445 THR   A CG2  1 
ATOM   3499 N N    . SER   A 1 446 ? -18.993 -17.552 -5.497  1.00 80.75  ? 446 SER   A N    1 
ATOM   3500 C CA   . SER   A 1 446 ? -20.380 -17.437 -5.050  1.00 81.36  ? 446 SER   A CA   1 
ATOM   3501 C C    . SER   A 1 446 ? -21.161 -16.429 -5.880  1.00 76.49  ? 446 SER   A C    1 
ATOM   3502 O O    . SER   A 1 446 ? -22.389 -16.521 -5.967  1.00 82.00  ? 446 SER   A O    1 
ATOM   3503 C CB   . SER   A 1 446 ? -20.433 -17.054 -3.574  1.00 75.33  ? 446 SER   A CB   1 
ATOM   3504 O OG   . SER   A 1 446 ? -19.629 -15.918 -3.319  1.00 77.13  ? 446 SER   A OG   1 
ATOM   3505 N N    . GLY   A 1 447 ? -20.482 -15.458 -6.471  1.00 70.43  ? 447 GLY   A N    1 
ATOM   3506 C CA   . GLY   A 1 447 ? -21.117 -14.536 -7.382  1.00 71.20  ? 447 GLY   A CA   1 
ATOM   3507 C C    . GLY   A 1 447 ? -20.230 -14.323 -8.583  1.00 69.20  ? 447 GLY   A C    1 
ATOM   3508 O O    . GLY   A 1 447 ? -19.092 -14.805 -8.616  1.00 67.69  ? 447 GLY   A O    1 
ATOM   3509 N N    . PRO   A 1 448 ? -20.722 -13.592 -9.592  1.00 67.25  ? 448 PRO   A N    1 
ATOM   3510 C CA   . PRO   A 1 448 ? -19.916 -13.375 -10.801 1.00 68.40  ? 448 PRO   A CA   1 
ATOM   3511 C C    . PRO   A 1 448 ? -18.684 -12.537 -10.495 1.00 63.70  ? 448 PRO   A C    1 
ATOM   3512 O O    . PRO   A 1 448 ? -18.710 -11.649 -9.641  1.00 63.34  ? 448 PRO   A O    1 
ATOM   3513 C CB   . PRO   A 1 448 ? -20.879 -12.653 -11.764 1.00 67.35  ? 448 PRO   A CB   1 
ATOM   3514 C CG   . PRO   A 1 448 ? -22.254 -12.689 -11.073 1.00 67.68  ? 448 PRO   A CG   1 
ATOM   3515 C CD   . PRO   A 1 448 ? -21.957 -12.795 -9.598  1.00 63.38  ? 448 PRO   A CD   1 
ATOM   3516 N N    . VAL   A 1 449 ? -17.601 -12.819 -11.221 1.00 59.04  ? 449 VAL   A N    1 
ATOM   3517 C CA   . VAL   A 1 449 ? -16.298 -12.214 -10.951 1.00 55.60  ? 449 VAL   A CA   1 
ATOM   3518 C C    . VAL   A 1 449 ? -16.162 -10.904 -11.717 1.00 58.82  ? 449 VAL   A C    1 
ATOM   3519 O O    . VAL   A 1 449 ? -16.394 -10.853 -12.946 1.00 57.89  ? 449 VAL   A O    1 
ATOM   3520 C CB   . VAL   A 1 449 ? -15.156 -13.167 -11.335 1.00 55.69  ? 449 VAL   A CB   1 
ATOM   3521 C CG1  . VAL   A 1 449 ? -13.810 -12.540 -10.998 1.00 55.61  ? 449 VAL   A CG1  1 
ATOM   3522 C CG2  . VAL   A 1 449 ? -15.334 -14.540 -10.697 1.00 56.38  ? 449 VAL   A CG2  1 
ATOM   3523 N N    . LEU   A 1 450 ? -15.763 -9.841  -11.001 1.00 55.36  ? 450 LEU   A N    1 
ATOM   3524 C CA   . LEU   A 1 450 ? -15.320 -8.591  -11.614 1.00 57.43  ? 450 LEU   A CA   1 
ATOM   3525 C C    . LEU   A 1 450 ? -13.824 -8.638  -11.917 1.00 57.93  ? 450 LEU   A C    1 
ATOM   3526 O O    . LEU   A 1 450 ? -13.408 -8.325  -13.047 1.00 56.32  ? 450 LEU   A O    1 
ATOM   3527 C CB   . LEU   A 1 450 ? -15.632 -7.397  -10.704 1.00 52.28  ? 450 LEU   A CB   1 
ATOM   3528 C CG   . LEU   A 1 450 ? -17.095 -6.994  -10.475 1.00 55.53  ? 450 LEU   A CG   1 
ATOM   3529 C CD1  . LEU   A 1 450 ? -17.214 -5.655  -9.706  1.00 51.57  ? 450 LEU   A CD1  1 
ATOM   3530 C CD2  . LEU   A 1 450 ? -17.857 -6.929  -11.778 1.00 55.01  ? 450 LEU   A CD2  1 
ATOM   3531 N N    . THR   A 1 451 ? -13.014 -9.066  -10.942 1.00 60.87  ? 451 THR   A N    1 
ATOM   3532 C CA   . THR   A 1 451 ? -11.581 -9.201  -11.161 1.00 60.68  ? 451 THR   A CA   1 
ATOM   3533 C C    . THR   A 1 451 ? -10.964 -10.217 -10.200 1.00 62.21  ? 451 THR   A C    1 
ATOM   3534 O O    . THR   A 1 451 ? -11.454 -10.436 -9.088  1.00 65.53  ? 451 THR   A O    1 
ATOM   3535 C CB   . THR   A 1 451 ? -10.863 -7.859  -11.014 1.00 58.40  ? 451 THR   A CB   1 
ATOM   3536 O OG1  . THR   A 1 451 ? -9.509  -8.008  -11.451 1.00 60.88  ? 451 THR   A OG1  1 
ATOM   3537 C CG2  . THR   A 1 451 ? -10.864 -7.386  -9.545  1.00 57.34  ? 451 THR   A CG2  1 
ATOM   3538 N N    . VAL   A 1 452 ? -9.873  -10.824 -10.664 1.00 59.23  ? 452 VAL   A N    1 
ATOM   3539 C CA   . VAL   A 1 452 ? -8.943  -11.623 -9.870  1.00 58.83  ? 452 VAL   A CA   1 
ATOM   3540 C C    . VAL   A 1 452 ? -7.562  -11.060 -10.199 1.00 62.72  ? 452 VAL   A C    1 
ATOM   3541 O O    . VAL   A 1 452 ? -7.066  -11.241 -11.321 1.00 64.47  ? 452 VAL   A O    1 
ATOM   3542 C CB   . VAL   A 1 452 ? -9.007  -13.127 -10.203 1.00 61.93  ? 452 VAL   A CB   1 
ATOM   3543 C CG1  . VAL   A 1 452 ? -7.916  -13.884 -9.459  1.00 64.37  ? 452 VAL   A CG1  1 
ATOM   3544 C CG2  . VAL   A 1 452 ? -10.383 -13.728 -9.910  1.00 59.52  ? 452 VAL   A CG2  1 
ATOM   3545 N N    . THR   A 1 453 ? -6.952  -10.352 -9.252  1.00 57.82  ? 453 THR   A N    1 
ATOM   3546 C CA   . THR   A 1 453 ? -5.759  -9.579  -9.566  1.00 58.54  ? 453 THR   A CA   1 
ATOM   3547 C C    . THR   A 1 453 ? -4.660  -9.818  -8.546  1.00 60.46  ? 453 THR   A C    1 
ATOM   3548 O O    . THR   A 1 453 ? -4.919  -9.946  -7.340  1.00 60.06  ? 453 THR   A O    1 
ATOM   3549 C CB   . THR   A 1 453 ? -6.068  -8.086  -9.642  1.00 57.33  ? 453 THR   A CB   1 
ATOM   3550 O OG1  . THR   A 1 453 ? -6.887  -7.837  -10.794 1.00 57.19  ? 453 THR   A OG1  1 
ATOM   3551 C CG2  . THR   A 1 453 ? -4.785  -7.284  -9.762  1.00 56.08  ? 453 THR   A CG2  1 
ATOM   3552 N N    . LEU   A 1 454 ? -3.432  -9.894  -9.056  1.00 61.65  ? 454 LEU   A N    1 
ATOM   3553 C CA   . LEU   A 1 454 ? -2.210  -9.847  -8.265  1.00 64.35  ? 454 LEU   A CA   1 
ATOM   3554 C C    . LEU   A 1 454 ? -1.594  -8.474  -8.490  1.00 63.75  ? 454 LEU   A C    1 
ATOM   3555 O O    . LEU   A 1 454 ? -1.122  -8.169  -9.594  1.00 61.01  ? 454 LEU   A O    1 
ATOM   3556 C CB   . LEU   A 1 454 ? -1.248  -10.962 -8.661  1.00 63.86  ? 454 LEU   A CB   1 
ATOM   3557 C CG   . LEU   A 1 454 ? -1.652  -12.321 -8.089  1.00 66.19  ? 454 LEU   A CG   1 
ATOM   3558 C CD1  . LEU   A 1 454 ? -0.747  -13.427 -8.628  1.00 67.79  ? 454 LEU   A CD1  1 
ATOM   3559 C CD2  . LEU   A 1 454 ? -1.669  -12.284 -6.536  1.00 60.84  ? 454 LEU   A CD2  1 
ATOM   3560 N N    . PHE   A 1 455 ? -1.629  -7.651  -7.441  1.00 61.60  ? 455 PHE   A N    1 
ATOM   3561 C CA   . PHE   A 1 455 ? -1.239  -6.245  -7.474  1.00 59.85  ? 455 PHE   A CA   1 
ATOM   3562 C C    . PHE   A 1 455 ? 0.065   -6.101  -6.695  1.00 64.74  ? 455 PHE   A C    1 
ATOM   3563 O O    . PHE   A 1 455 ? 0.070   -6.206  -5.458  1.00 64.60  ? 455 PHE   A O    1 
ATOM   3564 C CB   . PHE   A 1 455 ? -2.364  -5.400  -6.878  1.00 56.77  ? 455 PHE   A CB   1 
ATOM   3565 C CG   . PHE   A 1 455 ? -2.193  -3.909  -7.025  1.00 56.06  ? 455 PHE   A CG   1 
ATOM   3566 C CD1  . PHE   A 1 455 ? -1.259  -3.218  -6.273  1.00 56.65  ? 455 PHE   A CD1  1 
ATOM   3567 C CD2  . PHE   A 1 455 ? -3.019  -3.186  -7.878  1.00 58.63  ? 455 PHE   A CD2  1 
ATOM   3568 C CE1  . PHE   A 1 455 ? -1.127  -1.850  -6.380  1.00 54.21  ? 455 PHE   A CE1  1 
ATOM   3569 C CE2  . PHE   A 1 455 ? -2.888  -1.807  -7.995  1.00 58.11  ? 455 PHE   A CE2  1 
ATOM   3570 C CZ   . PHE   A 1 455 ? -1.940  -1.140  -7.229  1.00 55.40  ? 455 PHE   A CZ   1 
ATOM   3571 N N    . GLY   A 1 456 ? 1.162   -5.838  -7.399  1.00 64.82  ? 456 GLY   A N    1 
ATOM   3572 C CA   . GLY   A 1 456 ? 2.481   -5.793  -6.789  1.00 66.82  ? 456 GLY   A CA   1 
ATOM   3573 C C    . GLY   A 1 456 ? 3.080   -4.406  -6.887  1.00 65.85  ? 456 GLY   A C    1 
ATOM   3574 O O    . GLY   A 1 456 ? 2.928   -3.723  -7.902  1.00 62.84  ? 456 GLY   A O    1 
ATOM   3575 N N    . ARG   A 1 457 ? 3.771   -4.003  -5.823  1.00 67.81  ? 457 ARG   A N    1 
ATOM   3576 C CA   . ARG   A 1 457 ? 4.389   -2.691  -5.734  1.00 67.18  ? 457 ARG   A CA   1 
ATOM   3577 C C    . ARG   A 1 457 ? 5.901   -2.844  -5.720  1.00 69.32  ? 457 ARG   A C    1 
ATOM   3578 O O    . ARG   A 1 457 ? 6.436   -3.657  -4.957  1.00 70.77  ? 457 ARG   A O    1 
ATOM   3579 C CB   . ARG   A 1 457 ? 3.911   -1.964  -4.479  1.00 60.66  ? 457 ARG   A CB   1 
ATOM   3580 C CG   . ARG   A 1 457 ? 2.538   -1.351  -4.636  1.00 58.20  ? 457 ARG   A CG   1 
ATOM   3581 C CD   . ARG   A 1 457 ? 2.598   -0.072  -5.477  1.00 58.94  ? 457 ARG   A CD   1 
ATOM   3582 N NE   . ARG   A 1 457 ? 3.151   1.034   -4.707  1.00 59.89  ? 457 ARG   A NE   1 
ATOM   3583 C CZ   . ARG   A 1 457 ? 4.282   1.665   -4.993  1.00 64.85  ? 457 ARG   A CZ   1 
ATOM   3584 N NH1  . ARG   A 1 457 ? 5.031   1.312   -6.028  1.00 63.31  ? 457 ARG   A NH1  1 
ATOM   3585 N NH2  . ARG   A 1 457 ? 4.693   2.651   -4.195  1.00 62.09  ? 457 ARG   A NH2  1 
ATOM   3586 N N    . LEU   A 1 458 ? 6.584   -2.068  -6.561  1.00 68.31  ? 458 LEU   A N    1 
ATOM   3587 C CA   . LEU   A 1 458 ? 8.044   -2.034  -6.590  1.00 70.99  ? 458 LEU   A CA   1 
ATOM   3588 C C    . LEU   A 1 458 ? 8.492   -0.672  -6.061  1.00 71.18  ? 458 LEU   A C    1 
ATOM   3589 O O    . LEU   A 1 458 ? 8.840   0.236   -6.817  1.00 70.23  ? 458 LEU   A O    1 
ATOM   3590 C CB   . LEU   A 1 458 ? 8.562   -2.290  -7.995  1.00 69.65  ? 458 LEU   A CB   1 
ATOM   3591 C CG   . LEU   A 1 458 ? 8.612   -3.742  -8.470  1.00 73.26  ? 458 LEU   A CG   1 
ATOM   3592 C CD1  . LEU   A 1 458 ? 7.226   -4.360  -8.505  1.00 72.74  ? 458 LEU   A CD1  1 
ATOM   3593 C CD2  . LEU   A 1 458 ? 9.268   -3.817  -9.845  1.00 74.53  ? 458 LEU   A CD2  1 
ATOM   3594 N N    . TYR   A 1 459 ? 8.547   -0.564  -4.731  1.00 63.47  ? 459 TYR   A N    1 
ATOM   3595 C CA   . TYR   A 1 459 ? 8.772   0.725   -4.081  1.00 64.57  ? 459 TYR   A CA   1 
ATOM   3596 C C    . TYR   A 1 459 ? 10.120  1.323   -4.464  1.00 65.46  ? 459 TYR   A C    1 
ATOM   3597 O O    . TYR   A 1 459 ? 10.259  2.549   -4.551  1.00 65.29  ? 459 TYR   A O    1 
ATOM   3598 C CB   . TYR   A 1 459 ? 8.664   0.567   -2.560  1.00 63.32  ? 459 TYR   A CB   1 
ATOM   3599 C CG   . TYR   A 1 459 ? 7.340   -0.011  -2.083  1.00 59.82  ? 459 TYR   A CG   1 
ATOM   3600 C CD1  . TYR   A 1 459 ? 6.217   0.798   -1.935  1.00 56.26  ? 459 TYR   A CD1  1 
ATOM   3601 C CD2  . TYR   A 1 459 ? 7.219   -1.365  -1.768  1.00 59.89  ? 459 TYR   A CD2  1 
ATOM   3602 C CE1  . TYR   A 1 459 ? 5.009   0.276   -1.488  1.00 55.81  ? 459 TYR   A CE1  1 
ATOM   3603 C CE2  . TYR   A 1 459 ? 6.010   -1.898  -1.320  1.00 58.59  ? 459 TYR   A CE2  1 
ATOM   3604 C CZ   . TYR   A 1 459 ? 4.909   -1.071  -1.185  1.00 56.97  ? 459 TYR   A CZ   1 
ATOM   3605 O OH   . TYR   A 1 459 ? 3.701   -1.579  -0.758  1.00 50.43  ? 459 TYR   A OH   1 
ATOM   3606 N N    . GLU   A 1 460 ? 11.124  0.477   -4.670  1.00 94.69  ? 460 GLU   A N    1 
ATOM   3607 C CA   . GLU   A 1 460 ? 12.446  0.967   -5.039  1.00 97.38  ? 460 GLU   A CA   1 
ATOM   3608 C C    . GLU   A 1 460 ? 12.416  1.775   -6.329  1.00 96.69  ? 460 GLU   A C    1 
ATOM   3609 O O    . GLU   A 1 460 ? 13.252  2.667   -6.517  1.00 97.80  ? 460 GLU   A O    1 
ATOM   3610 C CB   . GLU   A 1 460 ? 13.403  -0.215  -5.188  1.00 98.42  ? 460 GLU   A CB   1 
ATOM   3611 C CG   . GLU   A 1 460 ? 12.871  -1.297  -6.118  1.00 94.50  ? 460 GLU   A CG   1 
ATOM   3612 C CD   . GLU   A 1 460 ? 11.968  -2.295  -5.404  1.00 99.21  ? 460 GLU   A CD   1 
ATOM   3613 O OE1  . GLU   A 1 460 ? 11.560  -2.027  -4.245  1.00 102.48 ? 460 GLU   A OE1  1 
ATOM   3614 O OE2  . GLU   A 1 460 ? 11.658  -3.344  -6.006  1.00 95.89  ? 460 GLU   A OE2  1 
ATOM   3615 N N    . LYS   A 1 461 ? 11.473  1.487   -7.223  1.00 82.11  ? 461 LYS   A N    1 
ATOM   3616 C CA   . LYS   A 1 461 ? 11.469  2.085   -8.554  1.00 83.28  ? 461 LYS   A CA   1 
ATOM   3617 C C    . LYS   A 1 461 ? 10.653  3.370   -8.620  1.00 81.58  ? 461 LYS   A C    1 
ATOM   3618 O O    . LYS   A 1 461 ? 10.438  3.892   -9.714  1.00 86.57  ? 461 LYS   A O    1 
ATOM   3619 C CB   . LYS   A 1 461 ? 10.960  1.073   -9.591  1.00 77.33  ? 461 LYS   A CB   1 
ATOM   3620 C CG   . LYS   A 1 461 ? 12.062  0.283   -10.298 1.00 81.05  ? 461 LYS   A CG   1 
ATOM   3621 C CD   . LYS   A 1 461 ? 11.488  -0.890  -11.093 1.00 84.59  ? 461 LYS   A CD   1 
ATOM   3622 C CE   . LYS   A 1 461 ? 12.487  -2.033  -11.268 1.00 86.74  ? 461 LYS   A CE   1 
ATOM   3623 N NZ   . LYS   A 1 461 ? 13.063  -2.128  -12.664 1.00 88.73  ? 461 LYS   A NZ   1 
ATOM   3624 N N    . ASP   A 1 462 ? 10.191  3.883   -7.484  1.00 83.80  ? 462 ASP   A N    1 
ATOM   3625 C CA   . ASP   A 1 462 ? 9.504   5.166   -7.446  1.00 80.67  ? 462 ASP   A CA   1 
ATOM   3626 C C    . ASP   A 1 462 ? 10.526  6.289   -7.596  1.00 82.11  ? 462 ASP   A C    1 
ATOM   3627 O O    . ASP   A 1 462 ? 10.186  7.409   -7.965  1.00 83.55  ? 462 ASP   A O    1 
ATOM   3628 C CB   . ASP   A 1 462 ? 8.722   5.332   -6.137  1.00 79.06  ? 462 ASP   A CB   1 
ATOM   3629 C CG   . ASP   A 1 462 ? 7.822   4.133   -5.809  1.00 74.97  ? 462 ASP   A CG   1 
ATOM   3630 O OD1  . ASP   A 1 462 ? 7.595   3.273   -6.683  1.00 75.27  ? 462 ASP   A OD1  1 
ATOM   3631 O OD2  . ASP   A 1 462 ? 7.325   4.065   -4.659  1.00 73.37  ? 462 ASP   A OD2  1 
ATOM   3632 N N    . GLN   B 1 1   ? -3.100  8.922   -27.451 1.00 76.12  ? 1   GLN   B N    1 
ATOM   3633 C CA   . GLN   B 1 1   ? -2.940  7.644   -28.144 1.00 78.07  ? 1   GLN   B CA   1 
ATOM   3634 C C    . GLN   B 1 1   ? -2.588  7.820   -29.617 1.00 73.54  ? 1   GLN   B C    1 
ATOM   3635 O O    . GLN   B 1 1   ? -3.188  8.620   -30.333 1.00 71.31  ? 1   GLN   B O    1 
ATOM   3636 C CB   . GLN   B 1 1   ? -4.198  6.798   -28.015 1.00 75.56  ? 1   GLN   B CB   1 
ATOM   3637 C CG   . GLN   B 1 1   ? -5.309  7.183   -28.948 1.00 72.25  ? 1   GLN   B CG   1 
ATOM   3638 C CD   . GLN   B 1 1   ? -6.486  6.242   -28.802 1.00 73.76  ? 1   GLN   B CD   1 
ATOM   3639 O OE1  . GLN   B 1 1   ? -7.334  6.429   -27.921 1.00 73.05  ? 1   GLN   B OE1  1 
ATOM   3640 N NE2  . GLN   B 1 1   ? -6.552  5.229   -29.657 1.00 66.86  ? 1   GLN   B NE2  1 
ATOM   3641 N N    . ASP   B 1 2   ? -1.603  7.040   -30.054 1.00 57.46  ? 2   ASP   B N    1 
ATOM   3642 C CA   . ASP   B 1 2   ? -0.979  7.233   -31.349 1.00 62.17  ? 2   ASP   B CA   1 
ATOM   3643 C C    . ASP   B 1 2   ? -1.693  6.517   -32.493 1.00 59.94  ? 2   ASP   B C    1 
ATOM   3644 O O    . ASP   B 1 2   ? -1.484  6.894   -33.648 1.00 57.02  ? 2   ASP   B O    1 
ATOM   3645 C CB   . ASP   B 1 2   ? 0.493   6.787   -31.289 1.00 57.96  ? 2   ASP   B CB   1 
ATOM   3646 C CG   . ASP   B 1 2   ? 1.313   7.629   -30.325 1.00 69.77  ? 2   ASP   B CG   1 
ATOM   3647 O OD1  . ASP   B 1 2   ? 0.903   8.792   -30.089 1.00 71.45  ? 2   ASP   B OD1  1 
ATOM   3648 O OD2  . ASP   B 1 2   ? 2.371   7.160   -29.828 1.00 68.23  ? 2   ASP   B OD2  1 
ATOM   3649 N N    . THR   B 1 3   ? -2.534  5.523   -32.204 1.00 59.52  ? 3   THR   B N    1 
ATOM   3650 C CA   . THR   B 1 3   ? -3.230  4.761   -33.230 1.00 61.08  ? 3   THR   B CA   1 
ATOM   3651 C C    . THR   B 1 3   ? -4.641  4.420   -32.771 1.00 57.60  ? 3   THR   B C    1 
ATOM   3652 O O    . THR   B 1 3   ? -4.956  4.442   -31.582 1.00 58.07  ? 3   THR   B O    1 
ATOM   3653 C CB   . THR   B 1 3   ? -2.485  3.459   -33.593 1.00 59.52  ? 3   THR   B CB   1 
ATOM   3654 O OG1  . THR   B 1 3   ? -2.483  2.582   -32.462 1.00 64.30  ? 3   THR   B OG1  1 
ATOM   3655 C CG2  . THR   B 1 3   ? -1.046  3.747   -34.036 1.00 59.71  ? 3   THR   B CG2  1 
ATOM   3656 N N    . PHE   B 1 4   ? -5.486  4.091   -33.748 1.00 60.36  ? 4   PHE   B N    1 
ATOM   3657 C CA   . PHE   B 1 4   ? -6.861  3.688   -33.499 1.00 55.66  ? 4   PHE   B CA   1 
ATOM   3658 C C    . PHE   B 1 4   ? -7.303  2.726   -34.593 1.00 55.62  ? 4   PHE   B C    1 
ATOM   3659 O O    . PHE   B 1 4   ? -6.777  2.740   -35.708 1.00 57.37  ? 4   PHE   B O    1 
ATOM   3660 C CB   . PHE   B 1 4   ? -7.803  4.900   -33.450 1.00 54.41  ? 4   PHE   B CB   1 
ATOM   3661 C CG   . PHE   B 1 4   ? -7.881  5.669   -34.751 1.00 54.45  ? 4   PHE   B CG   1 
ATOM   3662 C CD1  . PHE   B 1 4   ? -6.825  6.473   -35.168 1.00 54.63  ? 4   PHE   B CD1  1 
ATOM   3663 C CD2  . PHE   B 1 4   ? -9.014  5.589   -35.561 1.00 53.20  ? 4   PHE   B CD2  1 
ATOM   3664 C CE1  . PHE   B 1 4   ? -6.902  7.184   -36.377 1.00 54.68  ? 4   PHE   B CE1  1 
ATOM   3665 C CE2  . PHE   B 1 4   ? -9.092  6.299   -36.749 1.00 47.17  ? 4   PHE   B CE2  1 
ATOM   3666 C CZ   . PHE   B 1 4   ? -8.037  7.098   -37.149 1.00 50.37  ? 4   PHE   B CZ   1 
ATOM   3667 N N    . ILE   B 1 5   ? -8.296  1.908   -34.267 1.00 55.68  ? 5   ILE   B N    1 
ATOM   3668 C CA   . ILE   B 1 5   ? -8.875  0.962   -35.213 1.00 52.86  ? 5   ILE   B CA   1 
ATOM   3669 C C    . ILE   B 1 5   ? -10.069 1.609   -35.897 1.00 54.11  ? 5   ILE   B C    1 
ATOM   3670 O O    . ILE   B 1 5   ? -11.063 1.943   -35.243 1.00 50.28  ? 5   ILE   B O    1 
ATOM   3671 C CB   . ILE   B 1 5   ? -9.296  -0.343  -34.531 1.00 54.95  ? 5   ILE   B CB   1 
ATOM   3672 C CG1  . ILE   B 1 5   ? -8.267  -0.773  -33.517 1.00 59.51  ? 5   ILE   B CG1  1 
ATOM   3673 C CG2  . ILE   B 1 5   ? -9.418  -1.423  -35.561 1.00 56.24  ? 5   ILE   B CG2  1 
ATOM   3674 C CD1  . ILE   B 1 5   ? -6.996  -1.159  -34.191 1.00 62.75  ? 5   ILE   B CD1  1 
ATOM   3675 N N    . ALA   B 1 6   ? -9.998  1.729   -37.224 1.00 58.83  ? 6   ALA   B N    1 
ATOM   3676 C CA   . ALA   B 1 6   ? -11.061 2.324   -38.013 1.00 54.21  ? 6   ALA   B CA   1 
ATOM   3677 C C    . ALA   B 1 6   ? -11.925 1.225   -38.616 1.00 55.10  ? 6   ALA   B C    1 
ATOM   3678 O O    . ALA   B 1 6   ? -11.470 0.096   -38.825 1.00 56.13  ? 6   ALA   B O    1 
ATOM   3679 C CB   . ALA   B 1 6   ? -10.497 3.224   -39.118 1.00 54.16  ? 6   ALA   B CB   1 
ATOM   3680 N N    . ALA   B 1 7   ? -13.207 1.531   -38.792 1.00 47.87  ? 7   ALA   B N    1 
ATOM   3681 C CA   . ALA   B 1 7   ? -14.126 0.602   -39.424 1.00 49.43  ? 7   ALA   B CA   1 
ATOM   3682 C C    . ALA   B 1 7   ? -15.002 1.340   -40.429 1.00 49.38  ? 7   ALA   B C    1 
ATOM   3683 O O    . ALA   B 1 7   ? -15.439 2.472   -40.179 1.00 47.27  ? 7   ALA   B O    1 
ATOM   3684 C CB   . ALA   B 1 7   ? -14.995 -0.122  -38.377 1.00 47.55  ? 7   ALA   B CB   1 
ATOM   3685 N N    . VAL   B 1 8   ? -15.271 0.689   -41.558 1.00 47.45  ? 8   VAL   B N    1 
ATOM   3686 C CA   . VAL   B 1 8   ? -16.236 1.172   -42.542 1.00 42.88  ? 8   VAL   B CA   1 
ATOM   3687 C C    . VAL   B 1 8   ? -17.119 0.002   -42.951 1.00 45.30  ? 8   VAL   B C    1 
ATOM   3688 O O    . VAL   B 1 8   ? -16.654 -1.145  -43.040 1.00 44.95  ? 8   VAL   B O    1 
ATOM   3689 C CB   . VAL   B 1 8   ? -15.565 1.788   -43.788 1.00 45.42  ? 8   VAL   B CB   1 
ATOM   3690 C CG1  . VAL   B 1 8   ? -14.863 3.086   -43.453 1.00 44.02  ? 8   VAL   B CG1  1 
ATOM   3691 C CG2  . VAL   B 1 8   ? -14.601 0.789   -44.437 1.00 47.45  ? 8   VAL   B CG2  1 
ATOM   3692 N N    . TYR   B 1 9   ? -18.397 0.283   -43.185 1.00 44.11  ? 9   TYR   B N    1 
ATOM   3693 C CA   . TYR   B 1 9   ? -19.338 -0.753  -43.581 1.00 46.47  ? 9   TYR   B CA   1 
ATOM   3694 C C    . TYR   B 1 9   ? -19.955 -0.422  -44.937 1.00 49.38  ? 9   TYR   B C    1 
ATOM   3695 O O    . TYR   B 1 9   ? -20.483 0.686   -45.139 1.00 47.14  ? 9   TYR   B O    1 
ATOM   3696 C CB   . TYR   B 1 9   ? -20.428 -0.935  -42.533 1.00 48.63  ? 9   TYR   B CB   1 
ATOM   3697 C CG   . TYR   B 1 9   ? -21.278 -2.137  -42.798 1.00 45.98  ? 9   TYR   B CG   1 
ATOM   3698 C CD1  . TYR   B 1 9   ? -20.713 -3.410  -42.882 1.00 47.53  ? 9   TYR   B CD1  1 
ATOM   3699 C CD2  . TYR   B 1 9   ? -22.650 -2.011  -42.955 1.00 47.47  ? 9   TYR   B CD2  1 
ATOM   3700 C CE1  . TYR   B 1 9   ? -21.500 -4.526  -43.118 1.00 48.81  ? 9   TYR   B CE1  1 
ATOM   3701 C CE2  . TYR   B 1 9   ? -23.446 -3.122  -43.203 1.00 49.25  ? 9   TYR   B CE2  1 
ATOM   3702 C CZ   . TYR   B 1 9   ? -22.867 -4.371  -43.279 1.00 50.30  ? 9   TYR   B CZ   1 
ATOM   3703 O OH   . TYR   B 1 9   ? -23.673 -5.454  -43.530 1.00 53.87  ? 9   TYR   B OH   1 
ATOM   3704 N N    . GLU   B 1 10  ? -19.882 -1.381  -45.864 1.00 44.47  ? 10  GLU   B N    1 
ATOM   3705 C CA   . GLU   B 1 10  ? -20.618 -1.300  -47.119 1.00 47.12  ? 10  GLU   B CA   1 
ATOM   3706 C C    . GLU   B 1 10  ? -21.954 -2.023  -46.925 1.00 46.40  ? 10  GLU   B C    1 
ATOM   3707 O O    . GLU   B 1 10  ? -21.990 -3.228  -46.642 1.00 47.83  ? 10  GLU   B O    1 
ATOM   3708 C CB   . GLU   B 1 10  ? -19.795 -1.887  -48.279 1.00 45.08  ? 10  GLU   B CB   1 
ATOM   3709 C CG   . GLU   B 1 10  ? -20.544 -2.112  -49.528 1.00 47.07  ? 10  GLU   B CG   1 
ATOM   3710 C CD   . GLU   B 1 10  ? -19.666 -1.939  -50.794 1.00 48.89  ? 10  GLU   B CD   1 
ATOM   3711 O OE1  . GLU   B 1 10  ? -18.780 -1.037  -50.782 1.00 46.78  ? 10  GLU   B OE1  1 
ATOM   3712 O OE2  . GLU   B 1 10  ? -19.857 -2.697  -51.780 1.00 48.23  ? 10  GLU   B OE2  1 
ATOM   3713 N N    . HIS   B 1 11  ? -23.050 -1.287  -47.070 1.00 48.88  ? 11  HIS   B N    1 
ATOM   3714 C CA   . HIS   B 1 11  ? -24.369 -1.743  -46.653 1.00 48.90  ? 11  HIS   B CA   1 
ATOM   3715 C C    . HIS   B 1 11  ? -25.225 -1.991  -47.891 1.00 51.42  ? 11  HIS   B C    1 
ATOM   3716 O O    . HIS   B 1 11  ? -25.432 -1.081  -48.699 1.00 49.67  ? 11  HIS   B O    1 
ATOM   3717 C CB   . HIS   B 1 11  ? -25.021 -0.716  -45.716 1.00 47.24  ? 11  HIS   B CB   1 
ATOM   3718 C CG   . HIS   B 1 11  ? -26.406 -1.080  -45.274 1.00 47.93  ? 11  HIS   B CG   1 
ATOM   3719 N ND1  . HIS   B 1 11  ? -26.756 -2.353  -44.864 1.00 50.64  ? 11  HIS   B ND1  1 
ATOM   3720 C CD2  . HIS   B 1 11  ? -27.532 -0.334  -45.182 1.00 47.65  ? 11  HIS   B CD2  1 
ATOM   3721 C CE1  . HIS   B 1 11  ? -28.039 -2.372  -44.547 1.00 50.28  ? 11  HIS   B CE1  1 
ATOM   3722 N NE2  . HIS   B 1 11  ? -28.532 -1.158  -44.727 1.00 49.96  ? 11  HIS   B NE2  1 
ATOM   3723 N N    . ALA   B 1 12  ? -25.689 -3.233  -48.051 1.00 56.36  ? 12  ALA   B N    1 
ATOM   3724 C CA   . ALA   B 1 12  ? -26.717 -3.578  -49.031 1.00 58.47  ? 12  ALA   B CA   1 
ATOM   3725 C C    . ALA   B 1 12  ? -28.050 -3.102  -48.466 1.00 60.92  ? 12  ALA   B C    1 
ATOM   3726 O O    . ALA   B 1 12  ? -28.724 -3.834  -47.739 1.00 62.71  ? 12  ALA   B O    1 
ATOM   3727 C CB   . ALA   B 1 12  ? -26.725 -5.080  -49.278 1.00 58.47  ? 12  ALA   B CB   1 
ATOM   3728 N N    . ALA   B 1 13  ? -28.466 -1.891  -48.831 1.00 51.48  ? 13  ALA   B N    1 
ATOM   3729 C CA   . ALA   B 1 13  ? -29.527 -1.220  -48.090 1.00 53.84  ? 13  ALA   B CA   1 
ATOM   3730 C C    . ALA   B 1 13  ? -30.913 -1.722  -48.482 1.00 56.25  ? 13  ALA   B C    1 
ATOM   3731 O O    . ALA   B 1 13  ? -31.174 -2.050  -49.638 1.00 59.77  ? 13  ALA   B O    1 
ATOM   3732 C CB   . ALA   B 1 13  ? -29.438 0.293   -48.286 1.00 51.84  ? 13  ALA   B CB   1 
ATOM   3733 N N    . ILE   B 1 14  ? -31.800 -1.800  -47.495 1.00 66.46  ? 14  ILE   B N    1 
ATOM   3734 C CA   . ILE   B 1 14  ? -33.203 -2.127  -47.739 1.00 68.20  ? 14  ILE   B CA   1 
ATOM   3735 C C    . ILE   B 1 14  ? -33.883 -0.832  -48.189 1.00 65.63  ? 14  ILE   B C    1 
ATOM   3736 O O    . ILE   B 1 14  ? -33.946 0.138   -47.430 1.00 60.83  ? 14  ILE   B O    1 
ATOM   3737 C CB   . ILE   B 1 14  ? -33.869 -2.726  -46.484 1.00 67.61  ? 14  ILE   B CB   1 
ATOM   3738 C CG1  . ILE   B 1 14  ? -33.426 -4.176  -46.255 1.00 65.00  ? 14  ILE   B CG1  1 
ATOM   3739 C CG2  . ILE   B 1 14  ? -35.387 -2.728  -46.577 1.00 67.44  ? 14  ILE   B CG2  1 
ATOM   3740 C CD1  . ILE   B 1 14  ? -31.962 -4.348  -45.965 1.00 67.59  ? 14  ILE   B CD1  1 
ATOM   3741 N N    . LEU   B 1 15  ? -34.356 -0.797  -49.452 1.00 66.69  ? 15  LEU   B N    1 
ATOM   3742 C CA   . LEU   B 1 15  ? -34.950 0.401   -50.050 1.00 66.79  ? 15  LEU   B CA   1 
ATOM   3743 C C    . LEU   B 1 15  ? -36.460 0.410   -49.863 1.00 68.61  ? 15  LEU   B C    1 
ATOM   3744 O O    . LEU   B 1 15  ? -37.114 -0.623  -50.034 1.00 70.69  ? 15  LEU   B O    1 
ATOM   3745 C CB   . LEU   B 1 15  ? -34.648 0.488   -51.546 1.00 66.80  ? 15  LEU   B CB   1 
ATOM   3746 C CG   . LEU   B 1 15  ? -33.181 0.539   -51.963 1.00 66.10  ? 15  LEU   B CG   1 
ATOM   3747 C CD1  . LEU   B 1 15  ? -33.034 0.519   -53.505 1.00 67.27  ? 15  LEU   B CD1  1 
ATOM   3748 C CD2  . LEU   B 1 15  ? -32.501 1.749   -51.330 1.00 63.14  ? 15  LEU   B CD2  1 
ATOM   3749 N N    . PRO   B 1 16  ? -37.044 1.562   -49.546 1.00 71.17  ? 16  PRO   B N    1 
ATOM   3750 C CA   . PRO   B 1 16  ? -38.499 1.615   -49.428 1.00 72.52  ? 16  PRO   B CA   1 
ATOM   3751 C C    . PRO   B 1 16  ? -39.129 1.258   -50.756 1.00 81.48  ? 16  PRO   B C    1 
ATOM   3752 O O    . PRO   B 1 16  ? -38.674 1.695   -51.819 1.00 82.51  ? 16  PRO   B O    1 
ATOM   3753 C CB   . PRO   B 1 16  ? -38.785 3.070   -49.038 1.00 75.09  ? 16  PRO   B CB   1 
ATOM   3754 C CG   . PRO   B 1 16  ? -37.531 3.816   -49.289 1.00 74.68  ? 16  PRO   B CG   1 
ATOM   3755 C CD   . PRO   B 1 16  ? -36.407 2.834   -49.172 1.00 72.81  ? 16  PRO   B CD   1 
ATOM   3756 N N    . ASN   B 1 17  ? -40.185 0.451   -50.685 1.00 98.47  ? 17  ASN   B N    1 
ATOM   3757 C CA   . ASN   B 1 17  ? -40.931 0.123   -51.885 1.00 99.89  ? 17  ASN   B CA   1 
ATOM   3758 C C    . ASN   B 1 17  ? -41.180 1.401   -52.669 1.00 100.94 ? 17  ASN   B C    1 
ATOM   3759 O O    . ASN   B 1 17  ? -41.315 2.487   -52.096 1.00 101.69 ? 17  ASN   B O    1 
ATOM   3760 C CB   . ASN   B 1 17  ? -42.255 -0.559  -51.525 1.00 101.11 ? 17  ASN   B CB   1 
ATOM   3761 C CG   . ASN   B 1 17  ? -42.143 -2.067  -51.488 1.00 105.15 ? 17  ASN   B CG   1 
ATOM   3762 O OD1  . ASN   B 1 17  ? -41.319 -2.652  -52.194 1.00 105.08 ? 17  ASN   B OD1  1 
ATOM   3763 N ND2  . ASN   B 1 17  ? -42.979 -2.710  -50.672 1.00 100.23 ? 17  ASN   B ND2  1 
ATOM   3764 N N    . ALA   B 1 18  ? -41.193 1.284   -53.990 1.00 85.35  ? 18  ALA   B N    1 
ATOM   3765 C CA   . ALA   B 1 18  ? -41.490 2.455   -54.797 1.00 88.64  ? 18  ALA   B CA   1 
ATOM   3766 C C    . ALA   B 1 18  ? -42.880 2.944   -54.423 1.00 85.71  ? 18  ALA   B C    1 
ATOM   3767 O O    . ALA   B 1 18  ? -43.861 2.204   -54.551 1.00 89.00  ? 18  ALA   B O    1 
ATOM   3768 C CB   . ALA   B 1 18  ? -41.410 2.107   -56.288 1.00 85.12  ? 18  ALA   B CB   1 
ATOM   3769 N N    . THR   B 1 19  ? -42.971 4.182   -53.942 1.00 82.95  ? 19  THR   B N    1 
ATOM   3770 C CA   . THR   B 1 19  ? -44.262 4.736   -53.569 1.00 86.26  ? 19  THR   B CA   1 
ATOM   3771 C C    . THR   B 1 19  ? -44.446 6.115   -54.175 1.00 84.81  ? 19  THR   B C    1 
ATOM   3772 O O    . THR   B 1 19  ? -43.499 6.879   -54.391 1.00 78.26  ? 19  THR   B O    1 
ATOM   3773 C CB   . THR   B 1 19  ? -44.501 4.840   -52.026 1.00 87.48  ? 19  THR   B CB   1 
ATOM   3774 O OG1  . THR   B 1 19  ? -43.581 5.769   -51.435 1.00 82.25  ? 19  THR   B OG1  1 
ATOM   3775 C CG2  . THR   B 1 19  ? -44.409 3.458   -51.330 1.00 88.53  ? 19  THR   B CG2  1 
ATOM   3776 N N    . LEU   B 1 20  ? -45.706 6.377   -54.477 1.00 104.38 ? 20  LEU   B N    1 
ATOM   3777 C CA   . LEU   B 1 20  ? -46.157 7.607   -55.094 1.00 96.91  ? 20  LEU   B CA   1 
ATOM   3778 C C    . LEU   B 1 20  ? -46.323 8.725   -54.068 1.00 97.58  ? 20  LEU   B C    1 
ATOM   3779 O O    . LEU   B 1 20  ? -45.749 9.810   -54.216 1.00 88.08  ? 20  LEU   B O    1 
ATOM   3780 C CB   . LEU   B 1 20  ? -47.462 7.266   -55.807 1.00 103.76 ? 20  LEU   B CB   1 
ATOM   3781 C CG   . LEU   B 1 20  ? -47.371 5.734   -56.036 1.00 107.52 ? 20  LEU   B CG   1 
ATOM   3782 C CD1  . LEU   B 1 20  ? -48.704 4.981   -55.988 1.00 105.61 ? 20  LEU   B CD1  1 
ATOM   3783 C CD2  . LEU   B 1 20  ? -46.616 5.384   -57.342 1.00 99.13  ? 20  LEU   B CD2  1 
ATOM   3784 N N    . THR   B 1 21  ? -47.033 8.438   -52.982 1.00 95.55  ? 21  THR   B N    1 
ATOM   3785 C CA   . THR   B 1 21  ? -47.387 9.384   -51.940 1.00 85.92  ? 21  THR   B CA   1 
ATOM   3786 C C    . THR   B 1 21  ? -46.702 9.031   -50.627 1.00 85.83  ? 21  THR   B C    1 
ATOM   3787 O O    . THR   B 1 21  ? -46.184 7.921   -50.457 1.00 90.20  ? 21  THR   B O    1 
ATOM   3788 C CB   . THR   B 1 21  ? -48.908 9.439   -51.740 1.00 87.94  ? 21  THR   B CB   1 
ATOM   3789 O OG1  . THR   B 1 21  ? -49.476 8.132   -51.908 1.00 88.38  ? 21  THR   B OG1  1 
ATOM   3790 C CG2  . THR   B 1 21  ? -49.533 10.392  -52.755 1.00 89.01  ? 21  THR   B CG2  1 
ATOM   3791 N N    . PRO   B 1 22  ? -46.638 9.978   -49.690 1.00 64.17  ? 22  PRO   B N    1 
ATOM   3792 C CA   . PRO   B 1 22  ? -45.882 9.748   -48.451 1.00 58.99  ? 22  PRO   B CA   1 
ATOM   3793 C C    . PRO   B 1 22  ? -46.453 8.608   -47.624 1.00 60.81  ? 22  PRO   B C    1 
ATOM   3794 O O    . PRO   B 1 22  ? -47.669 8.446   -47.505 1.00 61.28  ? 22  PRO   B O    1 
ATOM   3795 C CB   . PRO   B 1 22  ? -45.996 11.089  -47.717 1.00 55.72  ? 22  PRO   B CB   1 
ATOM   3796 C CG   . PRO   B 1 22  ? -46.463 12.097  -48.790 1.00 56.86  ? 22  PRO   B CG   1 
ATOM   3797 C CD   . PRO   B 1 22  ? -47.296 11.297  -49.714 1.00 58.96  ? 22  PRO   B CD   1 
ATOM   3798 N N    . VAL   B 1 23  ? -45.556 7.812   -47.040 1.00 64.90  ? 23  VAL   B N    1 
ATOM   3799 C CA   . VAL   B 1 23  ? -45.961 6.754   -46.124 1.00 63.98  ? 23  VAL   B CA   1 
ATOM   3800 C C    . VAL   B 1 23  ? -46.191 7.382   -44.755 1.00 63.93  ? 23  VAL   B C    1 
ATOM   3801 O O    . VAL   B 1 23  ? -45.808 8.537   -44.510 1.00 58.81  ? 23  VAL   B O    1 
ATOM   3802 C CB   . VAL   B 1 23  ? -44.918 5.625   -46.047 1.00 64.22  ? 23  VAL   B CB   1 
ATOM   3803 C CG1  . VAL   B 1 23  ? -44.868 4.849   -47.339 1.00 67.55  ? 23  VAL   B CG1  1 
ATOM   3804 C CG2  . VAL   B 1 23  ? -43.564 6.194   -45.728 1.00 60.74  ? 23  VAL   B CG2  1 
ATOM   3805 N N    . SER   B 1 24  ? -46.806 6.630   -43.850 1.00 62.73  ? 24  SER   B N    1 
ATOM   3806 C CA   . SER   B 1 24  ? -46.984 7.117   -42.493 1.00 63.33  ? 24  SER   B CA   1 
ATOM   3807 C C    . SER   B 1 24  ? -45.647 7.121   -41.743 1.00 61.69  ? 24  SER   B C    1 
ATOM   3808 O O    . SER   B 1 24  ? -44.637 6.572   -42.202 1.00 61.50  ? 24  SER   B O    1 
ATOM   3809 C CB   . SER   B 1 24  ? -48.007 6.262   -41.763 1.00 60.54  ? 24  SER   B CB   1 
ATOM   3810 O OG   . SER   B 1 24  ? -47.478 4.970   -41.548 1.00 65.28  ? 24  SER   B OG   1 
ATOM   3811 N N    . ARG   B 1 25  ? -45.635 7.787   -40.580 1.00 72.37  ? 25  ARG   B N    1 
ATOM   3812 C CA   . ARG   B 1 25  ? -44.431 7.772   -39.750 1.00 67.98  ? 25  ARG   B CA   1 
ATOM   3813 C C    . ARG   B 1 25  ? -44.123 6.359   -39.288 1.00 65.84  ? 25  ARG   B C    1 
ATOM   3814 O O    . ARG   B 1 25  ? -42.951 5.988   -39.153 1.00 65.42  ? 25  ARG   B O    1 
ATOM   3815 C CB   . ARG   B 1 25  ? -44.588 8.709   -38.546 1.00 65.02  ? 25  ARG   B CB   1 
ATOM   3816 C CG   . ARG   B 1 25  ? -43.268 9.313   -37.999 1.00 74.61  ? 25  ARG   B CG   1 
ATOM   3817 C CD   . ARG   B 1 25  ? -42.233 8.239   -37.598 1.00 71.96  ? 25  ARG   B CD   1 
ATOM   3818 N NE   . ARG   B 1 25  ? -41.082 8.751   -36.857 1.00 65.00  ? 25  ARG   B NE   1 
ATOM   3819 C CZ   . ARG   B 1 25  ? -39.965 9.191   -37.430 1.00 67.49  ? 25  ARG   B CZ   1 
ATOM   3820 N NH1  . ARG   B 1 25  ? -39.830 9.216   -38.740 1.00 62.39  ? 25  ARG   B NH1  1 
ATOM   3821 N NH2  . ARG   B 1 25  ? -38.951 9.601   -36.665 1.00 64.93  ? 25  ARG   B NH2  1 
ATOM   3822 N N    . GLU   B 1 26  ? -45.161 5.549   -39.082 1.00 78.43  ? 26  GLU   B N    1 
ATOM   3823 C CA   . GLU   B 1 26  ? -44.960 4.163   -38.678 1.00 82.80  ? 26  GLU   B CA   1 
ATOM   3824 C C    . GLU   B 1 26  ? -44.159 3.395   -39.721 1.00 81.70  ? 26  GLU   B C    1 
ATOM   3825 O O    . GLU   B 1 26  ? -43.157 2.746   -39.396 1.00 78.79  ? 26  GLU   B O    1 
ATOM   3826 C CB   . GLU   B 1 26  ? -46.310 3.491   -38.444 1.00 86.29  ? 26  GLU   B CB   1 
ATOM   3827 C CG   . GLU   B 1 26  ? -46.217 2.125   -37.774 1.00 92.84  ? 26  GLU   B CG   1 
ATOM   3828 C CD   . GLU   B 1 26  ? -46.580 0.971   -38.702 1.00 96.54  ? 26  GLU   B CD   1 
ATOM   3829 O OE1  . GLU   B 1 26  ? -45.770 0.022   -38.818 1.00 95.15  ? 26  GLU   B OE1  1 
ATOM   3830 O OE2  . GLU   B 1 26  ? -47.680 1.003   -39.303 1.00 97.44  ? 26  GLU   B OE2  1 
ATOM   3831 N N    . GLU   B 1 27  ? -44.590 3.459   -40.986 1.00 74.11  ? 27  GLU   B N    1 
ATOM   3832 C CA   . GLU   B 1 27  ? -43.903 2.728   -42.049 1.00 68.16  ? 27  GLU   B CA   1 
ATOM   3833 C C    . GLU   B 1 27  ? -42.478 3.228   -42.230 1.00 65.07  ? 27  GLU   B C    1 
ATOM   3834 O O    . GLU   B 1 27  ? -41.536 2.432   -42.371 1.00 62.83  ? 27  GLU   B O    1 
ATOM   3835 C CB   . GLU   B 1 27  ? -44.689 2.857   -43.356 1.00 69.40  ? 27  GLU   B CB   1 
ATOM   3836 C CG   . GLU   B 1 27  ? -46.178 3.043   -43.128 1.00 74.65  ? 27  GLU   B CG   1 
ATOM   3837 C CD   . GLU   B 1 27  ? -47.029 2.777   -44.365 1.00 80.07  ? 27  GLU   B CD   1 
ATOM   3838 O OE1  . GLU   B 1 27  ? -47.923 3.602   -44.667 1.00 80.32  ? 27  GLU   B OE1  1 
ATOM   3839 O OE2  . GLU   B 1 27  ? -46.813 1.738   -45.032 1.00 80.27  ? 27  GLU   B OE2  1 
ATOM   3840 N N    . ALA   B 1 28  ? -42.297 4.547   -42.213 1.00 52.21  ? 28  ALA   B N    1 
ATOM   3841 C CA   . ALA   B 1 28  ? -40.959 5.099   -42.358 1.00 54.24  ? 28  ALA   B CA   1 
ATOM   3842 C C    . ALA   B 1 28  ? -40.041 4.586   -41.250 1.00 55.12  ? 28  ALA   B C    1 
ATOM   3843 O O    . ALA   B 1 28  ? -38.920 4.115   -41.511 1.00 51.97  ? 28  ALA   B O    1 
ATOM   3844 C CB   . ALA   B 1 28  ? -41.032 6.630   -42.370 1.00 52.10  ? 28  ALA   B CB   1 
ATOM   3845 N N    . LEU   B 1 29  ? -40.509 4.655   -39.997 1.00 61.84  ? 29  LEU   B N    1 
ATOM   3846 C CA   . LEU   B 1 29  ? -39.681 4.184   -38.898 1.00 59.92  ? 29  LEU   B CA   1 
ATOM   3847 C C    . LEU   B 1 29  ? -39.399 2.694   -39.031 1.00 58.98  ? 29  LEU   B C    1 
ATOM   3848 O O    . LEU   B 1 29  ? -38.253 2.264   -38.887 1.00 59.00  ? 29  LEU   B O    1 
ATOM   3849 C CB   . LEU   B 1 29  ? -40.358 4.498   -37.563 1.00 62.27  ? 29  LEU   B CB   1 
ATOM   3850 C CG   . LEU   B 1 29  ? -39.589 4.181   -36.279 1.00 60.25  ? 29  LEU   B CG   1 
ATOM   3851 C CD1  . LEU   B 1 29  ? -38.200 4.790   -36.350 1.00 59.06  ? 29  LEU   B CD1  1 
ATOM   3852 C CD2  . LEU   B 1 29  ? -40.344 4.698   -35.065 1.00 56.70  ? 29  LEU   B CD2  1 
ATOM   3853 N N    . ALA   B 1 30  ? -40.405 1.902   -39.393 1.00 49.40  ? 30  ALA   B N    1 
ATOM   3854 C CA   . ALA   B 1 30  ? -40.190 0.461   -39.526 1.00 54.52  ? 30  ALA   B CA   1 
ATOM   3855 C C    . ALA   B 1 30  ? -39.101 0.141   -40.557 1.00 54.23  ? 30  ALA   B C    1 
ATOM   3856 O O    . ALA   B 1 30  ? -38.229 -0.708  -40.315 1.00 55.69  ? 30  ALA   B O    1 
ATOM   3857 C CB   . ALA   B 1 30  ? -41.504 -0.229  -39.897 1.00 54.15  ? 30  ALA   B CB   1 
ATOM   3858 N N    . LEU   B 1 31  ? -39.125 0.804   -41.713 1.00 56.38  ? 31  LEU   B N    1 
ATOM   3859 C CA   . LEU   B 1 31  ? -38.077 0.545   -42.699 1.00 55.15  ? 31  LEU   B CA   1 
ATOM   3860 C C    . LEU   B 1 31  ? -36.700 1.002   -42.200 1.00 54.78  ? 31  LEU   B C    1 
ATOM   3861 O O    . LEU   B 1 31  ? -35.682 0.307   -42.399 1.00 54.51  ? 31  LEU   B O    1 
ATOM   3862 C CB   . LEU   B 1 31  ? -38.416 1.234   -44.011 1.00 53.92  ? 31  LEU   B CB   1 
ATOM   3863 C CG   . LEU   B 1 31  ? -37.271 1.024   -44.977 1.00 55.38  ? 31  LEU   B CG   1 
ATOM   3864 C CD1  . LEU   B 1 31  ? -37.663 -0.048  -45.988 1.00 52.05  ? 31  LEU   B CD1  1 
ATOM   3865 C CD2  . LEU   B 1 31  ? -36.906 2.339   -45.588 1.00 53.89  ? 31  LEU   B CD2  1 
ATOM   3866 N N    . MET   B 1 32  ? -36.634 2.194   -41.598 1.00 52.53  ? 32  MET   B N    1 
ATOM   3867 C CA   . MET   B 1 32  ? -35.353 2.659   -41.076 1.00 51.74  ? 32  MET   B CA   1 
ATOM   3868 C C    . MET   B 1 32  ? -34.809 1.692   -40.028 1.00 54.88  ? 32  MET   B C    1 
ATOM   3869 O O    . MET   B 1 32  ? -33.593 1.501   -39.915 1.00 52.01  ? 32  MET   B O    1 
ATOM   3870 C CB   . MET   B 1 32  ? -35.484 4.071   -40.511 1.00 53.37  ? 32  MET   B CB   1 
ATOM   3871 C CG   . MET   B 1 32  ? -35.230 5.175   -41.538 1.00 53.02  ? 32  MET   B CG   1 
ATOM   3872 S SD   . MET   B 1 32  ? -35.781 6.820   -41.029 1.00 51.39  ? 32  MET   B SD   1 
ATOM   3873 C CE   . MET   B 1 32  ? -37.413 6.392   -40.375 1.00 55.00  ? 32  MET   B CE   1 
ATOM   3874 N N    . ASN   B 1 33  ? -35.697 1.073   -39.250 1.00 62.58  ? 33  ASN   B N    1 
ATOM   3875 C CA   . ASN   B 1 33  ? -35.268 0.115   -38.235 1.00 62.81  ? 33  ASN   B CA   1 
ATOM   3876 C C    . ASN   B 1 33  ? -34.798 -1.192  -38.860 1.00 65.36  ? 33  ASN   B C    1 
ATOM   3877 O O    . ASN   B 1 33  ? -33.880 -1.838  -38.333 1.00 64.42  ? 33  ASN   B O    1 
ATOM   3878 C CB   . ASN   B 1 33  ? -36.403 -0.154  -37.250 1.00 64.39  ? 33  ASN   B CB   1 
ATOM   3879 C CG   . ASN   B 1 33  ? -36.485 0.891   -36.153 1.00 66.40  ? 33  ASN   B CG   1 
ATOM   3880 O OD1  . ASN   B 1 33  ? -35.466 1.313   -35.603 1.00 63.43  ? 33  ASN   B OD1  1 
ATOM   3881 N ND2  . ASN   B 1 33  ? -37.706 1.307   -35.822 1.00 66.29  ? 33  ASN   B ND2  1 
ATOM   3882 N N    . ARG   B 1 34  ? -35.420 -1.601  -39.971 1.00 58.02  ? 34  ARG   B N    1 
ATOM   3883 C CA   . ARG   B 1 34  ? -34.908 -2.754  -40.709 1.00 59.14  ? 34  ARG   B CA   1 
ATOM   3884 C C    . ARG   B 1 34  ? -33.471 -2.519  -41.153 1.00 57.70  ? 34  ARG   B C    1 
ATOM   3885 O O    . ARG   B 1 34  ? -32.632 -3.426  -41.086 1.00 54.28  ? 34  ARG   B O    1 
ATOM   3886 C CB   . ARG   B 1 34  ? -35.792 -3.045  -41.921 1.00 61.20  ? 34  ARG   B CB   1 
ATOM   3887 C CG   . ARG   B 1 34  ? -37.163 -3.594  -41.570 1.00 64.20  ? 34  ARG   B CG   1 
ATOM   3888 C CD   . ARG   B 1 34  ? -37.926 -3.935  -42.833 1.00 64.40  ? 34  ARG   B CD   1 
ATOM   3889 N NE   . ARG   B 1 34  ? -37.191 -4.883  -43.658 1.00 66.96  ? 34  ARG   B NE   1 
ATOM   3890 C CZ   . ARG   B 1 34  ? -37.496 -5.174  -44.915 1.00 67.68  ? 34  ARG   B CZ   1 
ATOM   3891 N NH1  . ARG   B 1 34  ? -38.514 -4.596  -45.529 1.00 66.22  ? 34  ARG   B NH1  1 
ATOM   3892 N NH2  . ARG   B 1 34  ? -36.782 -6.093  -45.561 1.00 64.71  ? 34  ARG   B NH2  1 
ATOM   3893 N N    . ASN   B 1 35  ? -33.172 -1.301  -41.616 1.00 53.59  ? 35  ASN   B N    1 
ATOM   3894 C CA   . ASN   B 1 35  ? -31.792 -0.981  -41.984 1.00 50.85  ? 35  ASN   B CA   1 
ATOM   3895 C C    . ASN   B 1 35  ? -30.879 -0.882  -40.760 1.00 52.63  ? 35  ASN   B C    1 
ATOM   3896 O O    . ASN   B 1 35  ? -29.730 -1.357  -40.798 1.00 52.35  ? 35  ASN   B O    1 
ATOM   3897 C CB   . ASN   B 1 35  ? -31.755 0.318   -42.780 1.00 49.78  ? 35  ASN   B CB   1 
ATOM   3898 C CG   . ASN   B 1 35  ? -31.985 0.081   -44.282 1.00 52.37  ? 35  ASN   B CG   1 
ATOM   3899 O OD1  . ASN   B 1 35  ? -31.169 -0.557  -44.953 1.00 50.35  ? 35  ASN   B OD1  1 
ATOM   3900 N ND2  . ASN   B 1 35  ? -33.124 0.551   -44.791 1.00 49.84  ? 35  ASN   B ND2  1 
ATOM   3901 N N    . LEU   B 1 36  ? -31.367 -0.262  -39.668 1.00 43.39  ? 36  LEU   B N    1 
ATOM   3902 C CA   . LEU   B 1 36  ? -30.548 -0.115  -38.461 1.00 48.96  ? 36  LEU   B CA   1 
ATOM   3903 C C    . LEU   B 1 36  ? -30.208 -1.462  -37.830 1.00 45.38  ? 36  LEU   B C    1 
ATOM   3904 O O    . LEU   B 1 36  ? -29.180 -1.565  -37.169 1.00 44.81  ? 36  LEU   B O    1 
ATOM   3905 C CB   . LEU   B 1 36  ? -31.236 0.794   -37.422 1.00 44.09  ? 36  LEU   B CB   1 
ATOM   3906 C CG   . LEU   B 1 36  ? -31.232 2.282   -37.823 1.00 44.79  ? 36  LEU   B CG   1 
ATOM   3907 C CD1  . LEU   B 1 36  ? -32.362 3.029   -37.175 1.00 44.01  ? 36  LEU   B CD1  1 
ATOM   3908 C CD2  . LEU   B 1 36  ? -29.886 3.018   -37.593 1.00 41.18  ? 36  LEU   B CD2  1 
ATOM   3909 N N    . ASP   B 1 37  ? -31.043 -2.491  -38.018 1.00 53.88  ? 37  ASP   B N    1 
ATOM   3910 C CA   . ASP   B 1 37  ? -30.703 -3.845  -37.565 1.00 55.40  ? 37  ASP   B CA   1 
ATOM   3911 C C    . ASP   B 1 37  ? -29.419 -4.368  -38.224 1.00 56.61  ? 37  ASP   B C    1 
ATOM   3912 O O    . ASP   B 1 37  ? -28.523 -4.903  -37.548 1.00 56.64  ? 37  ASP   B O    1 
ATOM   3913 C CB   . ASP   B 1 37  ? -31.870 -4.793  -37.853 1.00 55.46  ? 37  ASP   B CB   1 
ATOM   3914 C CG   . ASP   B 1 37  ? -33.089 -4.515  -36.968 1.00 61.40  ? 37  ASP   B CG   1 
ATOM   3915 O OD1  . ASP   B 1 37  ? -32.916 -3.862  -35.910 1.00 62.64  ? 37  ASP   B OD1  1 
ATOM   3916 O OD2  . ASP   B 1 37  ? -34.210 -4.965  -37.315 1.00 60.16  ? 37  ASP   B OD2  1 
ATOM   3917 N N    . ILE   B 1 38  ? -29.329 -4.266  -39.556 1.00 48.05  ? 38  ILE   B N    1 
ATOM   3918 C CA   . ILE   B 1 38  ? -28.120 -4.702  -40.253 1.00 49.58  ? 38  ILE   B CA   1 
ATOM   3919 C C    . ILE   B 1 38  ? -26.936 -3.847  -39.824 1.00 48.42  ? 38  ILE   B C    1 
ATOM   3920 O O    . ILE   B 1 38  ? -25.834 -4.352  -39.533 1.00 48.48  ? 38  ILE   B O    1 
ATOM   3921 C CB   . ILE   B 1 38  ? -28.328 -4.642  -41.785 1.00 50.24  ? 38  ILE   B CB   1 
ATOM   3922 C CG1  . ILE   B 1 38  ? -29.378 -5.657  -42.222 1.00 50.53  ? 38  ILE   B CG1  1 
ATOM   3923 C CG2  . ILE   B 1 38  ? -27.031 -4.927  -42.516 1.00 47.02  ? 38  ILE   B CG2  1 
ATOM   3924 C CD1  . ILE   B 1 38  ? -30.281 -5.160  -43.340 1.00 49.48  ? 38  ILE   B CD1  1 
ATOM   3925 N N    . LEU   B 1 39  ? -27.148 -2.528  -39.791 1.00 45.02  ? 39  LEU   B N    1 
ATOM   3926 C CA   . LEU   B 1 39  ? -26.070 -1.640  -39.384 1.00 46.86  ? 39  LEU   B CA   1 
ATOM   3927 C C    . LEU   B 1 39  ? -25.627 -1.940  -37.960 1.00 49.68  ? 39  LEU   B C    1 
ATOM   3928 O O    . LEU   B 1 39  ? -24.446 -1.786  -37.634 1.00 51.56  ? 39  LEU   B O    1 
ATOM   3929 C CB   . LEU   B 1 39  ? -26.499 -0.177  -39.514 1.00 44.44  ? 39  LEU   B CB   1 
ATOM   3930 C CG   . LEU   B 1 39  ? -26.779 0.349   -40.926 1.00 45.32  ? 39  LEU   B CG   1 
ATOM   3931 C CD1  . LEU   B 1 39  ? -26.952 1.883   -40.915 1.00 42.65  ? 39  LEU   B CD1  1 
ATOM   3932 C CD2  . LEU   B 1 39  ? -25.682 -0.093  -41.906 1.00 41.40  ? 39  LEU   B CD2  1 
ATOM   3933 N N    . GLU   B 1 40  ? -26.556 -2.345  -37.094 1.00 52.82  ? 40  GLU   B N    1 
ATOM   3934 C CA   . GLU   B 1 40  ? -26.197 -2.684  -35.721 1.00 55.41  ? 40  GLU   B CA   1 
ATOM   3935 C C    . GLU   B 1 40  ? -25.341 -3.937  -35.672 1.00 54.48  ? 40  GLU   B C    1 
ATOM   3936 O O    . GLU   B 1 40  ? -24.410 -4.027  -34.861 1.00 53.37  ? 40  GLU   B O    1 
ATOM   3937 C CB   . GLU   B 1 40  ? -27.445 -2.869  -34.870 1.00 55.00  ? 40  GLU   B CB   1 
ATOM   3938 C CG   . GLU   B 1 40  ? -27.165 -3.722  -33.657 1.00 57.97  ? 40  GLU   B CG   1 
ATOM   3939 C CD   . GLU   B 1 40  ? -28.250 -3.628  -32.630 1.00 57.22  ? 40  GLU   B CD   1 
ATOM   3940 O OE1  . GLU   B 1 40  ? -29.229 -2.889  -32.871 1.00 60.87  ? 40  GLU   B OE1  1 
ATOM   3941 O OE2  . GLU   B 1 40  ? -28.129 -4.302  -31.587 1.00 70.30  ? 40  GLU   B OE2  1 
ATOM   3942 N N    . GLY   B 1 41  ? -25.653 -4.922  -36.521 1.00 52.58  ? 41  GLY   B N    1 
ATOM   3943 C CA   . GLY   B 1 41  ? -24.762 -6.073  -36.633 1.00 53.66  ? 41  GLY   B CA   1 
ATOM   3944 C C    . GLY   B 1 41  ? -23.346 -5.650  -36.975 1.00 53.47  ? 41  GLY   B C    1 
ATOM   3945 O O    . GLY   B 1 41  ? -22.365 -6.099  -36.356 1.00 53.48  ? 41  GLY   B O    1 
ATOM   3946 N N    . ALA   B 1 42  ? -23.228 -4.738  -37.941 1.00 53.17  ? 42  ALA   B N    1 
ATOM   3947 C CA   . ALA   B 1 42  ? -21.913 -4.250  -38.338 1.00 53.55  ? 42  ALA   B CA   1 
ATOM   3948 C C    . ALA   B 1 42  ? -21.222 -3.519  -37.192 1.00 51.92  ? 42  ALA   B C    1 
ATOM   3949 O O    . ALA   B 1 42  ? -20.040 -3.760  -36.902 1.00 53.96  ? 42  ALA   B O    1 
ATOM   3950 C CB   . ALA   B 1 42  ? -22.046 -3.343  -39.564 1.00 49.66  ? 42  ALA   B CB   1 
ATOM   3951 N N    . ILE   B 1 43  ? -21.954 -2.631  -36.519 1.00 53.08  ? 43  ILE   B N    1 
ATOM   3952 C CA   . ILE   B 1 43  ? -21.367 -1.814  -35.457 1.00 53.04  ? 43  ILE   B CA   1 
ATOM   3953 C C    . ILE   B 1 43  ? -20.881 -2.693  -34.314 1.00 53.70  ? 43  ILE   B C    1 
ATOM   3954 O O    . ILE   B 1 43  ? -19.775 -2.509  -33.787 1.00 53.44  ? 43  ILE   B O    1 
ATOM   3955 C CB   . ILE   B 1 43  ? -22.384 -0.778  -34.945 1.00 51.42  ? 43  ILE   B CB   1 
ATOM   3956 C CG1  . ILE   B 1 43  ? -22.732 0.241   -36.037 1.00 50.59  ? 43  ILE   B CG1  1 
ATOM   3957 C CG2  . ILE   B 1 43  ? -21.841 -0.100  -33.684 1.00 48.98  ? 43  ILE   B CG2  1 
ATOM   3958 C CD1  . ILE   B 1 43  ? -24.090 0.911   -35.831 1.00 46.88  ? 43  ILE   B CD1  1 
ATOM   3959 N N    . THR   B 1 44  ? -21.705 -3.660  -33.906 1.00 56.87  ? 44  THR   B N    1 
ATOM   3960 C CA   . THR   B 1 44  ? -21.295 -4.515  -32.803 1.00 57.91  ? 44  THR   B CA   1 
ATOM   3961 C C    . THR   B 1 44  ? -20.064 -5.315  -33.176 1.00 59.43  ? 44  THR   B C    1 
ATOM   3962 O O    . THR   B 1 44  ? -19.164 -5.485  -32.346 1.00 59.72  ? 44  THR   B O    1 
ATOM   3963 C CB   . THR   B 1 44  ? -22.432 -5.443  -32.361 1.00 60.89  ? 44  THR   B CB   1 
ATOM   3964 O OG1  . THR   B 1 44  ? -22.958 -6.142  -33.498 1.00 64.40  ? 44  THR   B OG1  1 
ATOM   3965 C CG2  . THR   B 1 44  ? -23.553 -4.642  -31.691 1.00 55.53  ? 44  THR   B CG2  1 
ATOM   3966 N N    . SER   B 1 45  ? -20.009 -5.829  -34.414 1.00 60.85  ? 45  SER   B N    1 
ATOM   3967 C CA   . SER   B 1 45  ? -18.844 -6.607  -34.843 1.00 58.21  ? 45  SER   B CA   1 
ATOM   3968 C C    . SER   B 1 45  ? -17.560 -5.778  -34.812 1.00 59.57  ? 45  SER   B C    1 
ATOM   3969 O O    . SER   B 1 45  ? -16.509 -6.217  -34.291 1.00 60.31  ? 45  SER   B O    1 
ATOM   3970 C CB   . SER   B 1 45  ? -19.091 -7.149  -36.241 1.00 56.03  ? 45  SER   B CB   1 
ATOM   3971 O OG   . SER   B 1 45  ? -18.244 -8.251  -36.442 1.00 58.94  ? 45  SER   B OG   1 
ATOM   3972 N N    . ALA   B 1 46  ? -17.627 -4.563  -35.366 1.00 57.44  ? 46  ALA   B N    1 
ATOM   3973 C CA   . ALA   B 1 46  ? -16.450 -3.706  -35.350 1.00 57.72  ? 46  ALA   B CA   1 
ATOM   3974 C C    . ALA   B 1 46  ? -16.031 -3.390  -33.912 1.00 57.35  ? 46  ALA   B C    1 
ATOM   3975 O O    . ALA   B 1 46  ? -14.847 -3.499  -33.568 1.00 56.96  ? 46  ALA   B O    1 
ATOM   3976 C CB   . ALA   B 1 46  ? -16.714 -2.427  -36.151 1.00 56.27  ? 46  ALA   B CB   1 
ATOM   3977 N N    . ALA   B 1 47  ? -16.992 -3.072  -33.038 1.00 56.00  ? 47  ALA   B N    1 
ATOM   3978 C CA   . ALA   B 1 47  ? -16.631 -2.794  -31.646 1.00 58.89  ? 47  ALA   B CA   1 
ATOM   3979 C C    . ALA   B 1 47  ? -15.981 -4.013  -31.003 1.00 59.47  ? 47  ALA   B C    1 
ATOM   3980 O O    . ALA   B 1 47  ? -14.973 -3.887  -30.297 1.00 57.34  ? 47  ALA   B O    1 
ATOM   3981 C CB   . ALA   B 1 47  ? -17.851 -2.353  -30.842 1.00 53.36  ? 47  ALA   B CB   1 
ATOM   3982 N N    . ASP   B 1 48  ? -16.533 -5.209  -31.261 1.00 65.43  ? 48  ASP   B N    1 
ATOM   3983 C CA   . ASP   B 1 48  ? -16.010 -6.445  -30.681 1.00 68.23  ? 48  ASP   B CA   1 
ATOM   3984 C C    . ASP   B 1 48  ? -14.576 -6.711  -31.083 1.00 66.87  ? 48  ASP   B C    1 
ATOM   3985 O O    . ASP   B 1 48  ? -13.875 -7.470  -30.400 1.00 69.75  ? 48  ASP   B O    1 
ATOM   3986 C CB   . ASP   B 1 48  ? -16.880 -7.632  -31.097 1.00 67.27  ? 48  ASP   B CB   1 
ATOM   3987 C CG   . ASP   B 1 48  ? -18.197 -7.670  -30.349 1.00 67.56  ? 48  ASP   B CG   1 
ATOM   3988 O OD1  . ASP   B 1 48  ? -18.424 -6.802  -29.474 1.00 65.40  ? 48  ASP   B OD1  1 
ATOM   3989 O OD2  . ASP   B 1 48  ? -19.011 -8.565  -30.659 1.00 74.33  ? 48  ASP   B OD2  1 
ATOM   3990 N N    . GLN   B 1 49  ? -14.134 -6.153  -32.199 1.00 64.08  ? 49  GLN   B N    1 
ATOM   3991 C CA   . GLN   B 1 49  ? -12.729 -6.269  -32.558 1.00 62.27  ? 49  GLN   B CA   1 
ATOM   3992 C C    . GLN   B 1 49  ? -11.916 -5.034  -32.182 1.00 64.73  ? 49  GLN   B C    1 
ATOM   3993 O O    . GLN   B 1 49  ? -10.810 -4.843  -32.701 1.00 66.64  ? 49  GLN   B O    1 
ATOM   3994 C CB   . GLN   B 1 49  ? -12.620 -6.583  -34.040 1.00 64.76  ? 49  GLN   B CB   1 
ATOM   3995 C CG   . GLN   B 1 49  ? -13.569 -7.674  -34.398 1.00 61.78  ? 49  GLN   B CG   1 
ATOM   3996 C CD   . GLN   B 1 49  ? -13.530 -7.982  -35.845 1.00 61.41  ? 49  GLN   B CD   1 
ATOM   3997 O OE1  . GLN   B 1 49  ? -12.556 -8.551  -36.332 1.00 62.69  ? 49  GLN   B OE1  1 
ATOM   3998 N NE2  . GLN   B 1 49  ? -14.586 -7.616  -36.558 1.00 59.83  ? 49  GLN   B NE2  1 
ATOM   3999 N N    . GLY   B 1 50  ? -12.435 -4.203  -31.280 1.00 60.08  ? 50  GLY   B N    1 
ATOM   4000 C CA   . GLY   B 1 50  ? -11.698 -3.049  -30.811 1.00 60.79  ? 50  GLY   B CA   1 
ATOM   4001 C C    . GLY   B 1 50  ? -11.727 -1.828  -31.706 1.00 62.94  ? 50  GLY   B C    1 
ATOM   4002 O O    . GLY   B 1 50  ? -10.848 -0.971  -31.591 1.00 62.45  ? 50  GLY   B O    1 
ATOM   4003 N N    . ALA   B 1 51  ? -12.694 -1.718  -32.611 1.00 64.96  ? 51  ALA   B N    1 
ATOM   4004 C CA   . ALA   B 1 51  ? -12.789 -0.513  -33.420 1.00 63.78  ? 51  ALA   B CA   1 
ATOM   4005 C C    . ALA   B 1 51  ? -13.120 0.702   -32.553 1.00 63.79  ? 51  ALA   B C    1 
ATOM   4006 O O    . ALA   B 1 51  ? -13.917 0.622   -31.614 1.00 63.08  ? 51  ALA   B O    1 
ATOM   4007 C CB   . ALA   B 1 51  ? -13.845 -0.687  -34.504 1.00 63.42  ? 51  ALA   B CB   1 
ATOM   4008 N N    . HIS   B 1 52  ? -12.525 1.846   -32.895 1.00 52.75  ? 52  HIS   B N    1 
ATOM   4009 C CA   . HIS   B 1 52  ? -12.831 3.103   -32.215 1.00 48.95  ? 52  HIS   B CA   1 
ATOM   4010 C C    . HIS   B 1 52  ? -13.934 3.888   -32.905 1.00 47.79  ? 52  HIS   B C    1 
ATOM   4011 O O    . HIS   B 1 52  ? -14.669 4.635   -32.247 1.00 45.21  ? 52  HIS   B O    1 
ATOM   4012 C CB   . HIS   B 1 52  ? -11.583 3.982   -32.141 1.00 50.21  ? 52  HIS   B CB   1 
ATOM   4013 C CG   . HIS   B 1 52  ? -10.511 3.425   -31.257 1.00 53.14  ? 52  HIS   B CG   1 
ATOM   4014 N ND1  . HIS   B 1 52  ? -9.562  2.534   -31.715 1.00 55.15  ? 52  HIS   B ND1  1 
ATOM   4015 C CD2  . HIS   B 1 52  ? -10.241 3.624   -29.945 1.00 54.64  ? 52  HIS   B CD2  1 
ATOM   4016 C CE1  . HIS   B 1 52  ? -8.753  2.212   -30.722 1.00 57.80  ? 52  HIS   B CE1  1 
ATOM   4017 N NE2  . HIS   B 1 52  ? -9.142  2.860   -29.642 1.00 57.54  ? 52  HIS   B NE2  1 
ATOM   4018 N N    . ILE   B 1 53  ? -14.064 3.740   -34.220 1.00 58.26  ? 53  ILE   B N    1 
ATOM   4019 C CA   . ILE   B 1 53  ? -15.046 4.502   -34.984 1.00 53.50  ? 53  ILE   B CA   1 
ATOM   4020 C C    . ILE   B 1 53  ? -15.437 3.667   -36.196 1.00 53.10  ? 53  ILE   B C    1 
ATOM   4021 O O    . ILE   B 1 53  ? -14.610 2.964   -36.788 1.00 54.09  ? 53  ILE   B O    1 
ATOM   4022 C CB   . ILE   B 1 53  ? -14.499 5.908   -35.354 1.00 51.55  ? 53  ILE   B CB   1 
ATOM   4023 C CG1  . ILE   B 1 53  ? -15.513 6.719   -36.163 1.00 53.95  ? 53  ILE   B CG1  1 
ATOM   4024 C CG2  . ILE   B 1 53  ? -13.150 5.839   -36.068 1.00 51.85  ? 53  ILE   B CG2  1 
ATOM   4025 C CD1  . ILE   B 1 53  ? -15.268 8.207   -36.090 1.00 50.58  ? 53  ILE   B CD1  1 
ATOM   4026 N N    . ILE   B 1 54  ? -16.718 3.703   -36.526 1.00 48.73  ? 54  ILE   B N    1 
ATOM   4027 C CA   . ILE   B 1 54  ? -17.245 2.995   -37.679 1.00 46.34  ? 54  ILE   B CA   1 
ATOM   4028 C C    . ILE   B 1 54  ? -18.092 3.979   -38.464 1.00 48.64  ? 54  ILE   B C    1 
ATOM   4029 O O    . ILE   B 1 54  ? -18.848 4.764   -37.873 1.00 47.75  ? 54  ILE   B O    1 
ATOM   4030 C CB   . ILE   B 1 54  ? -18.065 1.752   -37.291 1.00 44.97  ? 54  ILE   B CB   1 
ATOM   4031 C CG1  . ILE   B 1 54  ? -18.530 1.021   -38.549 1.00 46.08  ? 54  ILE   B CG1  1 
ATOM   4032 C CG2  . ILE   B 1 54  ? -19.258 2.126   -36.451 1.00 45.03  ? 54  ILE   B CG2  1 
ATOM   4033 C CD1  . ILE   B 1 54  ? -19.267 -0.255  -38.270 1.00 48.22  ? 54  ILE   B CD1  1 
ATOM   4034 N N    . VAL   B 1 55  ? -17.919 3.976   -39.798 1.00 45.29  ? 55  VAL   B N    1 
ATOM   4035 C CA   . VAL   B 1 55  ? -18.685 4.806   -40.718 1.00 41.71  ? 55  VAL   B CA   1 
ATOM   4036 C C    . VAL   B 1 55  ? -19.700 3.926   -41.439 1.00 44.01  ? 55  VAL   B C    1 
ATOM   4037 O O    . VAL   B 1 55  ? -19.380 2.810   -41.890 1.00 43.32  ? 55  VAL   B O    1 
ATOM   4038 C CB   . VAL   B 1 55  ? -17.768 5.503   -41.747 1.00 43.75  ? 55  VAL   B CB   1 
ATOM   4039 C CG1  . VAL   B 1 55  ? -18.566 6.494   -42.570 1.00 42.24  ? 55  VAL   B CG1  1 
ATOM   4040 C CG2  . VAL   B 1 55  ? -16.547 6.166   -41.092 1.00 40.96  ? 55  VAL   B CG2  1 
ATOM   4041 N N    . THR   B 1 56  ? -20.919 4.425   -41.572 1.00 48.07  ? 56  THR   B N    1 
ATOM   4042 C CA   . THR   B 1 56  ? -21.911 3.771   -42.401 1.00 48.15  ? 56  THR   B CA   1 
ATOM   4043 C C    . THR   B 1 56  ? -22.319 4.701   -43.555 1.00 48.76  ? 56  THR   B C    1 
ATOM   4044 O O    . THR   B 1 56  ? -22.065 5.909   -43.512 1.00 50.96  ? 56  THR   B O    1 
ATOM   4045 C CB   . THR   B 1 56  ? -23.119 3.343   -41.561 1.00 46.72  ? 56  THR   B CB   1 
ATOM   4046 O OG1  . THR   B 1 56  ? -23.725 4.493   -40.981 1.00 46.82  ? 56  THR   B OG1  1 
ATOM   4047 C CG2  . THR   B 1 56  ? -22.682 2.383   -40.492 1.00 44.87  ? 56  THR   B CG2  1 
ATOM   4048 N N    . PRO   B 1 57  ? -22.908 4.163   -44.617 1.00 41.43  ? 57  PRO   B N    1 
ATOM   4049 C CA   . PRO   B 1 57  ? -22.957 4.875   -45.901 1.00 45.29  ? 57  PRO   B CA   1 
ATOM   4050 C C    . PRO   B 1 57  ? -24.000 5.988   -45.951 1.00 43.80  ? 57  PRO   B C    1 
ATOM   4051 O O    . PRO   B 1 57  ? -24.892 6.097   -45.115 1.00 38.62  ? 57  PRO   B O    1 
ATOM   4052 C CB   . PRO   B 1 57  ? -23.302 3.770   -46.920 1.00 43.12  ? 57  PRO   B CB   1 
ATOM   4053 C CG   . PRO   B 1 57  ? -23.274 2.466   -46.150 1.00 44.03  ? 57  PRO   B CG   1 
ATOM   4054 C CD   . PRO   B 1 57  ? -23.525 2.836   -44.704 1.00 43.51  ? 57  PRO   B CD   1 
ATOM   4055 N N    . GLU   B 1 58  ? -23.880 6.817   -46.993 1.00 51.24  ? 58  GLU   B N    1 
ATOM   4056 C CA   . GLU   B 1 58  ? -24.909 7.813   -47.247 1.00 49.73  ? 58  GLU   B CA   1 
ATOM   4057 C C    . GLU   B 1 58  ? -26.206 7.127   -47.682 1.00 49.86  ? 58  GLU   B C    1 
ATOM   4058 O O    . GLU   B 1 58  ? -26.193 6.182   -48.479 1.00 49.61  ? 58  GLU   B O    1 
ATOM   4059 C CB   . GLU   B 1 58  ? -24.431 8.816   -48.301 1.00 48.80  ? 58  GLU   B CB   1 
ATOM   4060 C CG   . GLU   B 1 58  ? -25.542 9.704   -48.861 1.00 51.79  ? 58  GLU   B CG   1 
ATOM   4061 C CD   . GLU   B 1 58  ? -25.098 10.538  -50.068 1.00 54.74  ? 58  GLU   B CD   1 
ATOM   4062 O OE1  . GLU   B 1 58  ? -25.642 11.653  -50.265 1.00 52.74  ? 58  GLU   B OE1  1 
ATOM   4063 O OE2  . GLU   B 1 58  ? -24.177 10.096  -50.794 1.00 55.03  ? 58  GLU   B OE2  1 
ATOM   4064 N N    . ASP   B 1 59  ? -27.340 7.620   -47.168 1.00 47.54  ? 59  ASP   B N    1 
ATOM   4065 C CA   . ASP   B 1 59  ? -28.660 7.064   -47.462 1.00 46.33  ? 59  ASP   B CA   1 
ATOM   4066 C C    . ASP   B 1 59  ? -28.838 5.635   -46.949 1.00 49.35  ? 59  ASP   B C    1 
ATOM   4067 O O    . ASP   B 1 59  ? -29.756 4.933   -47.395 1.00 48.23  ? 59  ASP   B O    1 
ATOM   4068 C CB   . ASP   B 1 59  ? -28.947 7.090   -48.972 1.00 51.39  ? 59  ASP   B CB   1 
ATOM   4069 C CG   . ASP   B 1 59  ? -29.159 8.499   -49.514 1.00 50.96  ? 59  ASP   B CG   1 
ATOM   4070 O OD1  . ASP   B 1 59  ? -29.660 9.371   -48.759 1.00 47.78  ? 59  ASP   B OD1  1 
ATOM   4071 O OD2  . ASP   B 1 59  ? -28.828 8.726   -50.702 1.00 53.58  ? 59  ASP   B OD2  1 
ATOM   4072 N N    . ALA   B 1 60  ? -27.994 5.180   -46.010 1.00 48.43  ? 60  ALA   B N    1 
ATOM   4073 C CA   . ALA   B 1 60  ? -28.013 3.769   -45.623 1.00 48.12  ? 60  ALA   B CA   1 
ATOM   4074 C C    . ALA   B 1 60  ? -29.317 3.357   -44.953 1.00 48.45  ? 60  ALA   B C    1 
ATOM   4075 O O    . ALA   B 1 60  ? -29.660 2.167   -44.943 1.00 45.88  ? 60  ALA   B O    1 
ATOM   4076 C CB   . ALA   B 1 60  ? -26.851 3.461   -44.673 1.00 46.43  ? 60  ALA   B CB   1 
ATOM   4077 N N    . ILE   B 1 61  ? -30.068 4.306   -44.410 1.00 52.33  ? 61  ILE   B N    1 
ATOM   4078 C CA   . ILE   B 1 61  ? -31.192 3.963   -43.562 1.00 53.94  ? 61  ILE   B CA   1 
ATOM   4079 C C    . ILE   B 1 61  ? -32.534 4.169   -44.264 1.00 53.05  ? 61  ILE   B C    1 
ATOM   4080 O O    . ILE   B 1 61  ? -33.478 3.418   -43.988 1.00 51.66  ? 61  ILE   B O    1 
ATOM   4081 C CB   . ILE   B 1 61  ? -31.122 4.741   -42.222 1.00 50.48  ? 61  ILE   B CB   1 
ATOM   4082 C CG1  . ILE   B 1 61  ? -29.890 4.288   -41.443 1.00 47.24  ? 61  ILE   B CG1  1 
ATOM   4083 C CG2  . ILE   B 1 61  ? -32.332 4.496   -41.356 1.00 49.14  ? 61  ILE   B CG2  1 
ATOM   4084 C CD1  . ILE   B 1 61  ? -29.069 5.411   -40.885 1.00 47.41  ? 61  ILE   B CD1  1 
ATOM   4085 N N    . TYR   B 1 62  ? -32.627 5.082   -45.238 1.00 54.08  ? 62  TYR   B N    1 
ATOM   4086 C CA   . TYR   B 1 62  ? -33.912 5.287   -45.889 1.00 55.45  ? 62  TYR   B CA   1 
ATOM   4087 C C    . TYR   B 1 62  ? -33.891 5.326   -47.426 1.00 56.28  ? 62  TYR   B C    1 
ATOM   4088 O O    . TYR   B 1 62  ? -34.967 5.394   -48.034 1.00 55.19  ? 62  TYR   B O    1 
ATOM   4089 C CB   . TYR   B 1 62  ? -34.579 6.568   -45.341 1.00 55.03  ? 62  TYR   B CB   1 
ATOM   4090 C CG   . TYR   B 1 62  ? -33.740 7.839   -45.355 1.00 56.18  ? 62  TYR   B CG   1 
ATOM   4091 C CD1  . TYR   B 1 62  ? -32.949 8.165   -46.452 1.00 55.05  ? 62  TYR   B CD1  1 
ATOM   4092 C CD2  . TYR   B 1 62  ? -33.799 8.754   -44.297 1.00 56.27  ? 62  TYR   B CD2  1 
ATOM   4093 C CE1  . TYR   B 1 62  ? -32.206 9.329   -46.486 1.00 55.55  ? 62  TYR   B CE1  1 
ATOM   4094 C CE2  . TYR   B 1 62  ? -33.053 9.941   -44.324 1.00 52.79  ? 62  TYR   B CE2  1 
ATOM   4095 C CZ   . TYR   B 1 62  ? -32.251 10.214  -45.420 1.00 55.82  ? 62  TYR   B CZ   1 
ATOM   4096 O OH   . TYR   B 1 62  ? -31.500 11.376  -45.478 1.00 58.09  ? 62  TYR   B OH   1 
ATOM   4097 N N    . GLY   B 1 63  ? -32.732 5.229   -48.069 1.00 51.14  ? 63  GLY   B N    1 
ATOM   4098 C CA   . GLY   B 1 63  ? -32.708 5.140   -49.523 1.00 52.35  ? 63  GLY   B CA   1 
ATOM   4099 C C    . GLY   B 1 63  ? -32.625 6.490   -50.204 1.00 51.30  ? 63  GLY   B C    1 
ATOM   4100 O O    . GLY   B 1 63  ? -32.382 7.531   -49.592 1.00 53.85  ? 63  GLY   B O    1 
ATOM   4101 N N    . TRP   B 1 64  ? -32.821 6.466   -51.512 1.00 51.01  ? 64  TRP   B N    1 
ATOM   4102 C CA   . TRP   B 1 64  ? -32.622 7.658   -52.320 1.00 52.93  ? 64  TRP   B CA   1 
ATOM   4103 C C    . TRP   B 1 64  ? -33.771 7.969   -53.276 1.00 56.19  ? 64  TRP   B C    1 
ATOM   4104 O O    . TRP   B 1 64  ? -33.643 8.885   -54.097 1.00 55.45  ? 64  TRP   B O    1 
ATOM   4105 C CB   . TRP   B 1 64  ? -31.320 7.527   -53.108 1.00 51.64  ? 64  TRP   B CB   1 
ATOM   4106 C CG   . TRP   B 1 64  ? -31.233 6.221   -53.792 1.00 52.94  ? 64  TRP   B CG   1 
ATOM   4107 C CD1  . TRP   B 1 64  ? -31.812 5.885   -54.984 1.00 50.91  ? 64  TRP   B CD1  1 
ATOM   4108 C CD2  . TRP   B 1 64  ? -30.533 5.061   -53.339 1.00 51.85  ? 64  TRP   B CD2  1 
ATOM   4109 N NE1  . TRP   B 1 64  ? -31.512 4.585   -55.298 1.00 52.23  ? 64  TRP   B NE1  1 
ATOM   4110 C CE2  . TRP   B 1 64  ? -30.727 4.056   -54.306 1.00 52.94  ? 64  TRP   B CE2  1 
ATOM   4111 C CE3  . TRP   B 1 64  ? -29.764 4.774   -52.212 1.00 51.92  ? 64  TRP   B CE3  1 
ATOM   4112 C CZ2  . TRP   B 1 64  ? -30.181 2.780   -54.177 1.00 52.65  ? 64  TRP   B CZ2  1 
ATOM   4113 C CZ3  . TRP   B 1 64  ? -29.221 3.506   -52.087 1.00 51.85  ? 64  TRP   B CZ3  1 
ATOM   4114 C CH2  . TRP   B 1 64  ? -29.435 2.526   -53.063 1.00 55.23  ? 64  TRP   B CH2  1 
ATOM   4115 N N    . ASN   B 1 65  ? -34.871 7.229   -53.217 1.00 60.21  ? 65  ASN   B N    1 
ATOM   4116 C CA   . ASN   B 1 65  ? -36.000 7.451   -54.114 1.00 62.44  ? 65  ASN   B CA   1 
ATOM   4117 C C    . ASN   B 1 65  ? -37.038 8.286   -53.372 1.00 63.64  ? 65  ASN   B C    1 
ATOM   4118 O O    . ASN   B 1 65  ? -37.950 7.757   -52.736 1.00 64.08  ? 65  ASN   B O    1 
ATOM   4119 C CB   . ASN   B 1 65  ? -36.553 6.120   -54.588 1.00 64.67  ? 65  ASN   B CB   1 
ATOM   4120 C CG   . ASN   B 1 65  ? -35.581 5.397   -55.479 1.00 65.09  ? 65  ASN   B CG   1 
ATOM   4121 O OD1  . ASN   B 1 65  ? -35.222 4.250   -55.228 1.00 68.85  ? 65  ASN   B OD1  1 
ATOM   4122 N ND2  . ASN   B 1 65  ? -35.135 6.075   -56.534 1.00 69.52  ? 65  ASN   B ND2  1 
ATOM   4123 N N    . PHE   B 1 66  ? -36.902 9.610   -53.468 1.00 53.24  ? 66  PHE   B N    1 
ATOM   4124 C CA   . PHE   B 1 66  ? -37.738 10.519  -52.703 1.00 55.28  ? 66  PHE   B CA   1 
ATOM   4125 C C    . PHE   B 1 66  ? -38.075 11.776  -53.491 1.00 55.17  ? 66  PHE   B C    1 
ATOM   4126 O O    . PHE   B 1 66  ? -37.238 12.298  -54.233 1.00 59.63  ? 66  PHE   B O    1 
ATOM   4127 C CB   . PHE   B 1 66  ? -37.031 10.941  -51.410 1.00 51.65  ? 66  PHE   B CB   1 
ATOM   4128 C CG   . PHE   B 1 66  ? -37.037 9.894   -50.340 1.00 55.59  ? 66  PHE   B CG   1 
ATOM   4129 C CD1  . PHE   B 1 66  ? -38.230 9.477   -49.760 1.00 55.04  ? 66  PHE   B CD1  1 
ATOM   4130 C CD2  . PHE   B 1 66  ? -35.844 9.350   -49.875 1.00 55.26  ? 66  PHE   B CD2  1 
ATOM   4131 C CE1  . PHE   B 1 66  ? -38.227 8.531   -48.749 1.00 54.44  ? 66  PHE   B CE1  1 
ATOM   4132 C CE2  . PHE   B 1 66  ? -35.844 8.396   -48.863 1.00 51.08  ? 66  PHE   B CE2  1 
ATOM   4133 C CZ   . PHE   B 1 66  ? -37.032 7.989   -48.308 1.00 49.37  ? 66  PHE   B CZ   1 
ATOM   4134 N N    . ASN   B 1 67  ? -39.296 12.265  -53.309 1.00 52.13  ? 67  ASN   B N    1 
ATOM   4135 C CA   . ASN   B 1 67  ? -39.585 13.679  -53.453 1.00 54.30  ? 67  ASN   B CA   1 
ATOM   4136 C C    . ASN   B 1 67  ? -39.647 14.290  -52.051 1.00 57.70  ? 67  ASN   B C    1 
ATOM   4137 O O    . ASN   B 1 67  ? -39.461 13.605  -51.042 1.00 55.34  ? 67  ASN   B O    1 
ATOM   4138 C CB   . ASN   B 1 67  ? -40.877 13.896  -54.247 1.00 53.77  ? 67  ASN   B CB   1 
ATOM   4139 C CG   . ASN   B 1 67  ? -42.080 13.165  -53.648 1.00 57.56  ? 67  ASN   B CG   1 
ATOM   4140 O OD1  . ASN   B 1 67  ? -42.645 13.595  -52.640 1.00 57.69  ? 67  ASN   B OD1  1 
ATOM   4141 N ND2  . ASN   B 1 67  ? -42.507 12.084  -54.302 1.00 55.61  ? 67  ASN   B ND2  1 
ATOM   4142 N N    . ARG   B 1 68  ? -39.865 15.604  -51.980 1.00 57.68  ? 68  ARG   B N    1 
ATOM   4143 C CA   . ARG   B 1 68  ? -39.848 16.267  -50.680 1.00 58.50  ? 68  ARG   B CA   1 
ATOM   4144 C C    . ARG   B 1 68  ? -40.868 15.638  -49.736 1.00 59.89  ? 68  ARG   B C    1 
ATOM   4145 O O    . ARG   B 1 68  ? -40.556 15.295  -48.583 1.00 58.61  ? 68  ARG   B O    1 
ATOM   4146 C CB   . ARG   B 1 68  ? -40.129 17.762  -50.850 1.00 59.14  ? 68  ARG   B CB   1 
ATOM   4147 C CG   . ARG   B 1 68  ? -38.984 18.557  -51.486 1.00 57.44  ? 68  ARG   B CG   1 
ATOM   4148 C CD   . ARG   B 1 68  ? -39.261 20.067  -51.464 1.00 58.11  ? 68  ARG   B CD   1 
ATOM   4149 N NE   . ARG   B 1 68  ? -39.375 20.629  -50.114 1.00 55.70  ? 68  ARG   B NE   1 
ATOM   4150 C CZ   . ARG   B 1 68  ? -38.354 20.923  -49.312 1.00 55.91  ? 68  ARG   B CZ   1 
ATOM   4151 N NH1  . ARG   B 1 68  ? -37.104 20.663  -49.654 1.00 56.24  ? 68  ARG   B NH1  1 
ATOM   4152 N NH2  . ARG   B 1 68  ? -38.593 21.514  -48.142 1.00 56.94  ? 68  ARG   B NH2  1 
ATOM   4153 N N    . ASP   B 1 69  ? -42.095 15.455  -50.219 1.00 60.76  ? 69  ASP   B N    1 
ATOM   4154 C CA   . ASP   B 1 69  ? -43.158 15.025  -49.325 1.00 64.13  ? 69  ASP   B CA   1 
ATOM   4155 C C    . ASP   B 1 69  ? -43.007 13.565  -48.929 1.00 62.82  ? 69  ASP   B C    1 
ATOM   4156 O O    . ASP   B 1 69  ? -43.191 13.216  -47.756 1.00 65.75  ? 69  ASP   B O    1 
ATOM   4157 C CB   . ASP   B 1 69  ? -44.510 15.295  -49.968 1.00 63.30  ? 69  ASP   B CB   1 
ATOM   4158 C CG   . ASP   B 1 69  ? -44.722 16.772  -50.229 1.00 67.80  ? 69  ASP   B CG   1 
ATOM   4159 O OD1  . ASP   B 1 69  ? -44.578 17.552  -49.255 1.00 65.33  ? 69  ASP   B OD1  1 
ATOM   4160 O OD2  . ASP   B 1 69  ? -45.038 17.152  -51.381 1.00 68.68  ? 69  ASP   B OD2  1 
ATOM   4161 N N    . SER   B 1 70  ? -42.635 12.709  -49.874 1.00 62.83  ? 70  SER   B N    1 
ATOM   4162 C CA   . SER   B 1 70  ? -42.451 11.301  -49.557 1.00 63.94  ? 70  SER   B CA   1 
ATOM   4163 C C    . SER   B 1 70  ? -41.272 11.091  -48.621 1.00 63.83  ? 70  SER   B C    1 
ATOM   4164 O O    . SER   B 1 70  ? -41.226 10.087  -47.903 1.00 65.88  ? 70  SER   B O    1 
ATOM   4165 C CB   . SER   B 1 70  ? -42.253 10.494  -50.844 1.00 66.07  ? 70  SER   B CB   1 
ATOM   4166 O OG   . SER   B 1 70  ? -40.993 10.782  -51.429 1.00 63.77  ? 70  SER   B OG   1 
ATOM   4167 N N    . LEU   B 1 71  ? -40.306 12.011  -48.623 1.00 55.58  ? 71  LEU   B N    1 
ATOM   4168 C CA   . LEU   B 1 71  ? -39.211 11.928  -47.665 1.00 54.63  ? 71  LEU   B CA   1 
ATOM   4169 C C    . LEU   B 1 71  ? -39.620 12.436  -46.284 1.00 55.81  ? 71  LEU   B C    1 
ATOM   4170 O O    . LEU   B 1 71  ? -39.118 11.929  -45.269 1.00 54.35  ? 71  LEU   B O    1 
ATOM   4171 C CB   . LEU   B 1 71  ? -37.997 12.714  -48.170 1.00 54.99  ? 71  LEU   B CB   1 
ATOM   4172 C CG   . LEU   B 1 71  ? -36.883 12.940  -47.130 1.00 55.47  ? 71  LEU   B CG   1 
ATOM   4173 C CD1  . LEU   B 1 71  ? -36.015 11.696  -46.990 1.00 52.93  ? 71  LEU   B CD1  1 
ATOM   4174 C CD2  . LEU   B 1 71  ? -36.012 14.174  -47.420 1.00 51.43  ? 71  LEU   B CD2  1 
ATOM   4175 N N    . TYR   B 1 72  ? -40.540 13.405  -46.215 1.00 54.24  ? 72  TYR   B N    1 
ATOM   4176 C CA   . TYR   B 1 72  ? -40.823 14.071  -44.942 1.00 53.66  ? 72  TYR   B CA   1 
ATOM   4177 C C    . TYR   B 1 72  ? -41.064 13.127  -43.766 1.00 56.34  ? 72  TYR   B C    1 
ATOM   4178 O O    . TYR   B 1 72  ? -40.524 13.386  -42.679 1.00 55.18  ? 72  TYR   B O    1 
ATOM   4179 C CB   . TYR   B 1 72  ? -42.025 15.014  -45.074 1.00 54.34  ? 72  TYR   B CB   1 
ATOM   4180 C CG   . TYR   B 1 72  ? -42.255 15.810  -43.792 1.00 53.94  ? 72  TYR   B CG   1 
ATOM   4181 C CD1  . TYR   B 1 72  ? -41.396 16.851  -43.438 1.00 53.98  ? 72  TYR   B CD1  1 
ATOM   4182 C CD2  . TYR   B 1 72  ? -43.295 15.503  -42.931 1.00 53.18  ? 72  TYR   B CD2  1 
ATOM   4183 C CE1  . TYR   B 1 72  ? -41.576 17.572  -42.287 1.00 54.77  ? 72  TYR   B CE1  1 
ATOM   4184 C CE2  . TYR   B 1 72  ? -43.481 16.235  -41.742 1.00 56.82  ? 72  TYR   B CE2  1 
ATOM   4185 C CZ   . TYR   B 1 72  ? -42.608 17.268  -41.435 1.00 53.65  ? 72  TYR   B CZ   1 
ATOM   4186 O OH   . TYR   B 1 72  ? -42.745 18.015  -40.292 1.00 56.03  ? 72  TYR   B OH   1 
ATOM   4187 N N    . PRO   B 1 73  ? -41.869 12.068  -43.881 1.00 59.91  ? 73  PRO   B N    1 
ATOM   4188 C CA   . PRO   B 1 73  ? -42.116 11.217  -42.704 1.00 57.28  ? 73  PRO   B CA   1 
ATOM   4189 C C    . PRO   B 1 73  ? -40.871 10.549  -42.129 1.00 57.70  ? 73  PRO   B C    1 
ATOM   4190 O O    . PRO   B 1 73  ? -40.932 10.054  -40.998 1.00 56.62  ? 73  PRO   B O    1 
ATOM   4191 C CB   . PRO   B 1 73  ? -43.115 10.173  -43.226 1.00 58.98  ? 73  PRO   B CB   1 
ATOM   4192 C CG   . PRO   B 1 73  ? -43.047 10.271  -44.715 1.00 59.09  ? 73  PRO   B CG   1 
ATOM   4193 C CD   . PRO   B 1 73  ? -42.733 11.694  -45.012 1.00 57.42  ? 73  PRO   B CD   1 
ATOM   4194 N N    . TYR   B 1 74  ? -39.766 10.471  -42.872 1.00 54.68  ? 74  TYR   B N    1 
ATOM   4195 C CA   . TYR   B 1 74  ? -38.536 9.871   -42.362 1.00 52.52  ? 74  TYR   B CA   1 
ATOM   4196 C C    . TYR   B 1 74  ? -37.641 10.859  -41.621 1.00 51.36  ? 74  TYR   B C    1 
ATOM   4197 O O    . TYR   B 1 74  ? -36.626 10.447  -41.051 1.00 50.79  ? 74  TYR   B O    1 
ATOM   4198 C CB   . TYR   B 1 74  ? -37.715 9.264   -43.508 1.00 50.14  ? 74  TYR   B CB   1 
ATOM   4199 C CG   . TYR   B 1 74  ? -38.401 8.165   -44.289 1.00 54.46  ? 74  TYR   B CG   1 
ATOM   4200 C CD1  . TYR   B 1 74  ? -39.459 8.448   -45.147 1.00 54.06  ? 74  TYR   B CD1  1 
ATOM   4201 C CD2  . TYR   B 1 74  ? -37.967 6.847   -44.196 1.00 50.68  ? 74  TYR   B CD2  1 
ATOM   4202 C CE1  . TYR   B 1 74  ? -40.076 7.448   -45.860 1.00 52.30  ? 74  TYR   B CE1  1 
ATOM   4203 C CE2  . TYR   B 1 74  ? -38.579 5.842   -44.910 1.00 50.64  ? 74  TYR   B CE2  1 
ATOM   4204 C CZ   . TYR   B 1 74  ? -39.632 6.147   -45.735 1.00 50.52  ? 74  TYR   B CZ   1 
ATOM   4205 O OH   . TYR   B 1 74  ? -40.237 5.143   -46.453 1.00 53.78  ? 74  TYR   B OH   1 
ATOM   4206 N N    . LEU   B 1 75  ? -37.959 12.149  -41.647 1.00 42.56  ? 75  LEU   B N    1 
ATOM   4207 C CA   . LEU   B 1 75  ? -37.051 13.168  -41.151 1.00 40.92  ? 75  LEU   B CA   1 
ATOM   4208 C C    . LEU   B 1 75  ? -37.217 13.343  -39.641 1.00 42.59  ? 75  LEU   B C    1 
ATOM   4209 O O    . LEU   B 1 75  ? -38.292 13.107  -39.078 1.00 41.75  ? 75  LEU   B O    1 
ATOM   4210 C CB   . LEU   B 1 75  ? -37.283 14.497  -41.878 1.00 42.22  ? 75  LEU   B CB   1 
ATOM   4211 C CG   . LEU   B 1 75  ? -37.144 14.500  -43.420 1.00 42.84  ? 75  LEU   B CG   1 
ATOM   4212 C CD1  . LEU   B 1 75  ? -37.227 15.927  -43.976 1.00 42.69  ? 75  LEU   B CD1  1 
ATOM   4213 C CD2  . LEU   B 1 75  ? -35.833 13.858  -43.862 1.00 39.10  ? 75  LEU   B CD2  1 
ATOM   4214 N N    . GLU   B 1 76  ? -36.122 13.734  -38.993 1.00 50.75  ? 76  GLU   B N    1 
ATOM   4215 C CA   . GLU   B 1 76  ? -36.115 14.107  -37.589 1.00 54.57  ? 76  GLU   B CA   1 
ATOM   4216 C C    . GLU   B 1 76  ? -35.429 15.458  -37.424 1.00 54.60  ? 76  GLU   B C    1 
ATOM   4217 O O    . GLU   B 1 76  ? -34.499 15.789  -38.160 1.00 53.03  ? 76  GLU   B O    1 
ATOM   4218 C CB   . GLU   B 1 76  ? -35.402 13.040  -36.756 1.00 51.71  ? 76  GLU   B CB   1 
ATOM   4219 C CG   . GLU   B 1 76  ? -36.371 12.005  -36.220 1.00 56.86  ? 76  GLU   B CG   1 
ATOM   4220 C CD   . GLU   B 1 76  ? -35.700 10.789  -35.598 1.00 56.82  ? 76  GLU   B CD   1 
ATOM   4221 O OE1  . GLU   B 1 76  ? -34.584 10.925  -35.035 1.00 55.39  ? 76  GLU   B OE1  1 
ATOM   4222 O OE2  . GLU   B 1 76  ? -36.321 9.705   -35.638 1.00 58.33  ? 76  GLU   B OE2  1 
ATOM   4223 N N    . ASP   B 1 77  ? -35.859 16.222  -36.420 1.00 47.77  ? 77  ASP   B N    1 
ATOM   4224 C CA   . ASP   B 1 77  ? -35.258 17.530  -36.137 1.00 45.47  ? 77  ASP   B CA   1 
ATOM   4225 C C    . ASP   B 1 77  ? -33.995 17.305  -35.310 1.00 48.24  ? 77  ASP   B C    1 
ATOM   4226 O O    . ASP   B 1 77  ? -34.066 16.998  -34.112 1.00 50.04  ? 77  ASP   B O    1 
ATOM   4227 C CB   . ASP   B 1 77  ? -36.275 18.428  -35.440 1.00 46.51  ? 77  ASP   B CB   1 
ATOM   4228 C CG   . ASP   B 1 77  ? -35.834 19.893  -35.355 1.00 50.71  ? 77  ASP   B CG   1 
ATOM   4229 O OD1  . ASP   B 1 77  ? -34.613 20.171  -35.452 1.00 48.78  ? 77  ASP   B OD1  1 
ATOM   4230 O OD2  . ASP   B 1 77  ? -36.723 20.765  -35.153 1.00 46.60  ? 77  ASP   B OD2  1 
ATOM   4231 N N    . ILE   B 1 78  ? -32.839 17.389  -35.964 1.00 54.57  ? 78  ILE   B N    1 
ATOM   4232 C CA   . ILE   B 1 78  ? -31.554 17.063  -35.350 1.00 53.49  ? 78  ILE   B CA   1 
ATOM   4233 C C    . ILE   B 1 78  ? -30.942 18.350  -34.802 1.00 54.59  ? 78  ILE   B C    1 
ATOM   4234 O O    . ILE   B 1 78  ? -30.624 19.256  -35.596 1.00 53.34  ? 78  ILE   B O    1 
ATOM   4235 C CB   . ILE   B 1 78  ? -30.609 16.394  -36.357 1.00 51.80  ? 78  ILE   B CB   1 
ATOM   4236 C CG1  . ILE   B 1 78  ? -31.276 15.168  -37.001 1.00 50.47  ? 78  ILE   B CG1  1 
ATOM   4237 C CG2  . ILE   B 1 78  ? -29.292 16.024  -35.697 1.00 50.07  ? 78  ILE   B CG2  1 
ATOM   4238 C CD1  . ILE   B 1 78  ? -30.604 14.696  -38.299 1.00 48.44  ? 78  ILE   B CD1  1 
ATOM   4239 N N    . PRO   B 1 79  ? -30.732 18.465  -33.489 1.00 49.77  ? 79  PRO   B N    1 
ATOM   4240 C CA   . PRO   B 1 79  ? -30.182 19.707  -32.922 1.00 48.66  ? 79  PRO   B CA   1 
ATOM   4241 C C    . PRO   B 1 79  ? -28.709 19.894  -33.275 1.00 47.80  ? 79  PRO   B C    1 
ATOM   4242 O O    . PRO   B 1 79  ? -28.029 18.992  -33.776 1.00 45.22  ? 79  PRO   B O    1 
ATOM   4243 C CB   . PRO   B 1 79  ? -30.367 19.521  -31.406 1.00 47.98  ? 79  PRO   B CB   1 
ATOM   4244 C CG   . PRO   B 1 79  ? -30.314 18.043  -31.212 1.00 46.03  ? 79  PRO   B CG   1 
ATOM   4245 C CD   . PRO   B 1 79  ? -30.996 17.455  -32.443 1.00 50.53  ? 79  PRO   B CD   1 
ATOM   4246 N N    . ASP   B 1 80  ? -28.237 21.119  -33.048 1.00 50.35  ? 80  ASP   B N    1 
ATOM   4247 C CA   . ASP   B 1 80  ? -26.810 21.406  -33.113 1.00 49.95  ? 80  ASP   B CA   1 
ATOM   4248 C C    . ASP   B 1 80  ? -26.080 20.737  -31.945 1.00 48.97  ? 80  ASP   B C    1 
ATOM   4249 O O    . ASP   B 1 80  ? -26.558 20.778  -30.804 1.00 51.06  ? 80  ASP   B O    1 
ATOM   4250 C CB   . ASP   B 1 80  ? -26.568 22.913  -33.078 1.00 48.17  ? 80  ASP   B CB   1 
ATOM   4251 C CG   . ASP   B 1 80  ? -25.134 23.286  -33.395 1.00 51.16  ? 80  ASP   B CG   1 
ATOM   4252 O OD1  . ASP   B 1 80  ? -24.253 23.023  -32.553 1.00 54.45  ? 80  ASP   B OD1  1 
ATOM   4253 O OD2  . ASP   B 1 80  ? -24.886 23.890  -34.463 1.00 57.64  ? 80  ASP   B OD2  1 
ATOM   4254 N N    . PRO   B 1 81  ? -24.914 20.126  -32.191 1.00 49.24  ? 81  PRO   B N    1 
ATOM   4255 C CA   . PRO   B 1 81  ? -24.196 19.443  -31.097 1.00 45.60  ? 81  PRO   B CA   1 
ATOM   4256 C C    . PRO   B 1 81  ? -23.881 20.341  -29.916 1.00 47.34  ? 81  PRO   B C    1 
ATOM   4257 O O    . PRO   B 1 81  ? -23.572 19.820  -28.842 1.00 46.60  ? 81  PRO   B O    1 
ATOM   4258 C CB   . PRO   B 1 81  ? -22.916 18.938  -31.776 1.00 45.96  ? 81  PRO   B CB   1 
ATOM   4259 C CG   . PRO   B 1 81  ? -23.325 18.734  -33.229 1.00 43.68  ? 81  PRO   B CG   1 
ATOM   4260 C CD   . PRO   B 1 81  ? -24.323 19.833  -33.516 1.00 44.74  ? 81  PRO   B CD   1 
ATOM   4261 N N    . GLU   B 1 82  ? -23.966 21.665  -30.066 1.00 48.32  ? 82  GLU   B N    1 
ATOM   4262 C CA   . GLU   B 1 82  ? -23.713 22.538  -28.930 1.00 50.64  ? 82  GLU   B CA   1 
ATOM   4263 C C    . GLU   B 1 82  ? -24.706 22.315  -27.792 1.00 52.16  ? 82  GLU   B C    1 
ATOM   4264 O O    . GLU   B 1 82  ? -24.444 22.766  -26.680 1.00 54.36  ? 82  GLU   B O    1 
ATOM   4265 C CB   . GLU   B 1 82  ? -23.758 24.007  -29.364 1.00 50.18  ? 82  GLU   B CB   1 
ATOM   4266 C CG   . GLU   B 1 82  ? -25.180 24.516  -29.602 1.00 51.33  ? 82  GLU   B CG   1 
ATOM   4267 C CD   . GLU   B 1 82  ? -25.238 25.994  -29.960 1.00 55.95  ? 82  GLU   B CD   1 
ATOM   4268 O OE1  . GLU   B 1 82  ? -24.336 26.756  -29.525 1.00 58.71  ? 82  GLU   B OE1  1 
ATOM   4269 O OE2  . GLU   B 1 82  ? -26.199 26.391  -30.667 1.00 57.07  ? 82  GLU   B OE2  1 
ATOM   4270 N N    . VAL   B 1 83  ? -25.833 21.637  -28.036 1.00 51.56  ? 83  VAL   B N    1 
ATOM   4271 C CA   . VAL   B 1 83  ? -26.788 21.351  -26.968 1.00 48.35  ? 83  VAL   B CA   1 
ATOM   4272 C C    . VAL   B 1 83  ? -26.287 20.321  -25.973 1.00 50.21  ? 83  VAL   B C    1 
ATOM   4273 O O    . VAL   B 1 83  ? -26.860 20.203  -24.878 1.00 52.91  ? 83  VAL   B O    1 
ATOM   4274 C CB   . VAL   B 1 83  ? -28.136 20.855  -27.534 1.00 50.50  ? 83  VAL   B CB   1 
ATOM   4275 C CG1  . VAL   B 1 83  ? -28.701 21.871  -28.515 1.00 49.85  ? 83  VAL   B CG1  1 
ATOM   4276 C CG2  . VAL   B 1 83  ? -27.969 19.482  -28.182 1.00 47.49  ? 83  VAL   B CG2  1 
ATOM   4277 N N    . ASN   B 1 84  ? -25.230 19.583  -26.306 1.00 50.20  ? 84  ASN   B N    1 
ATOM   4278 C CA   . ASN   B 1 84  ? -24.584 18.659  -25.380 1.00 52.87  ? 84  ASN   B CA   1 
ATOM   4279 C C    . ASN   B 1 84  ? -25.571 17.602  -24.875 1.00 55.85  ? 84  ASN   B C    1 
ATOM   4280 O O    . ASN   B 1 84  ? -25.934 17.537  -23.688 1.00 53.06  ? 84  ASN   B O    1 
ATOM   4281 C CB   . ASN   B 1 84  ? -23.965 19.399  -24.196 1.00 56.59  ? 84  ASN   B CB   1 
ATOM   4282 C CG   . ASN   B 1 84  ? -22.892 18.591  -23.556 1.00 59.88  ? 84  ASN   B CG   1 
ATOM   4283 O OD1  . ASN   B 1 84  ? -23.151 17.490  -23.072 1.00 62.43  ? 84  ASN   B OD1  1 
ATOM   4284 N ND2  . ASN   B 1 84  ? -21.668 19.114  -23.555 1.00 69.62  ? 84  ASN   B ND2  1 
ATOM   4285 N N    . TRP   B 1 85  ? -25.986 16.768  -25.823 1.00 49.78  ? 85  TRP   B N    1 
ATOM   4286 C CA   . TRP   B 1 85  ? -27.092 15.840  -25.647 1.00 49.44  ? 85  TRP   B CA   1 
ATOM   4287 C C    . TRP   B 1 85  ? -26.629 14.425  -25.960 1.00 50.98  ? 85  TRP   B C    1 
ATOM   4288 O O    . TRP   B 1 85  ? -25.981 14.189  -26.991 1.00 48.97  ? 85  TRP   B O    1 
ATOM   4289 C CB   . TRP   B 1 85  ? -28.255 16.251  -26.557 1.00 47.83  ? 85  TRP   B CB   1 
ATOM   4290 C CG   . TRP   B 1 85  ? -29.469 15.371  -26.532 1.00 50.96  ? 85  TRP   B CG   1 
ATOM   4291 C CD1  . TRP   B 1 85  ? -30.072 14.825  -25.435 1.00 51.57  ? 85  TRP   B CD1  1 
ATOM   4292 C CD2  . TRP   B 1 85  ? -30.250 14.962  -27.667 1.00 51.30  ? 85  TRP   B CD2  1 
ATOM   4293 N NE1  . TRP   B 1 85  ? -31.177 14.095  -25.818 1.00 52.02  ? 85  TRP   B NE1  1 
ATOM   4294 C CE2  . TRP   B 1 85  ? -31.306 14.161  -27.179 1.00 51.41  ? 85  TRP   B CE2  1 
ATOM   4295 C CE3  . TRP   B 1 85  ? -30.157 15.195  -29.048 1.00 49.76  ? 85  TRP   B CE3  1 
ATOM   4296 C CZ2  . TRP   B 1 85  ? -32.262 13.589  -28.022 1.00 53.29  ? 85  TRP   B CZ2  1 
ATOM   4297 C CZ3  . TRP   B 1 85  ? -31.104 14.624  -29.882 1.00 49.59  ? 85  TRP   B CZ3  1 
ATOM   4298 C CH2  . TRP   B 1 85  ? -32.141 13.830  -29.368 1.00 52.20  ? 85  TRP   B CH2  1 
ATOM   4299 N N    . ILE   B 1 86  ? -26.947 13.493  -25.061 1.00 51.05  ? 86  ILE   B N    1 
ATOM   4300 C CA   . ILE   B 1 86  ? -26.786 12.060  -25.301 1.00 49.94  ? 86  ILE   B CA   1 
ATOM   4301 C C    . ILE   B 1 86  ? -28.180 11.471  -25.479 1.00 52.71  ? 86  ILE   B C    1 
ATOM   4302 O O    . ILE   B 1 86  ? -28.830 11.113  -24.479 1.00 53.34  ? 86  ILE   B O    1 
ATOM   4303 C CB   . ILE   B 1 86  ? -26.041 11.362  -24.151 1.00 50.06  ? 86  ILE   B CB   1 
ATOM   4304 C CG1  . ILE   B 1 86  ? -24.676 12.001  -23.900 1.00 49.26  ? 86  ILE   B CG1  1 
ATOM   4305 C CG2  . ILE   B 1 86  ? -25.899 9.870   -24.423 1.00 47.70  ? 86  ILE   B CG2  1 
ATOM   4306 C CD1  . ILE   B 1 86  ? -24.076 11.623  -22.529 1.00 45.68  ? 86  ILE   B CD1  1 
ATOM   4307 N N    . PRO   B 1 87  ? -28.657 11.296  -26.718 1.00 48.48  ? 87  PRO   B N    1 
ATOM   4308 C CA   . PRO   B 1 87  ? -30.043 10.830  -26.908 1.00 50.09  ? 87  PRO   B CA   1 
ATOM   4309 C C    . PRO   B 1 87  ? -30.354 9.542   -26.173 1.00 52.94  ? 87  PRO   B C    1 
ATOM   4310 O O    . PRO   B 1 87  ? -31.496 9.361   -25.716 1.00 50.36  ? 87  PRO   B O    1 
ATOM   4311 C CB   . PRO   B 1 87  ? -30.155 10.643  -28.432 1.00 47.71  ? 87  PRO   B CB   1 
ATOM   4312 C CG   . PRO   B 1 87  ? -29.152 11.599  -28.997 1.00 48.52  ? 87  PRO   B CG   1 
ATOM   4313 C CD   . PRO   B 1 87  ? -28.004 11.650  -27.990 1.00 47.57  ? 87  PRO   B CD   1 
ATOM   4314 N N    . CYS   B 1 88  ? -29.378 8.640   -26.030 1.00 63.57  ? 88  CYS   B N    1 
ATOM   4315 C CA   . CYS   B 1 88  ? -29.665 7.374   -25.367 1.00 63.69  ? 88  CYS   B CA   1 
ATOM   4316 C C    . CYS   B 1 88  ? -30.126 7.592   -23.936 1.00 64.30  ? 88  CYS   B C    1 
ATOM   4317 O O    . CYS   B 1 88  ? -30.993 6.865   -23.441 1.00 67.16  ? 88  CYS   B O    1 
ATOM   4318 C CB   . CYS   B 1 88  ? -28.454 6.447   -25.379 1.00 62.38  ? 88  CYS   B CB   1 
ATOM   4319 S SG   . CYS   B 1 88  ? -28.995 4.746   -25.005 1.00 67.76  ? 88  CYS   B SG   1 
ATOM   4320 N N    . ASN   B 1 89  ? -29.538 8.568   -23.250 1.00 60.10  ? 89  ASN   B N    1 
ATOM   4321 C CA   . ASN   B 1 89  ? -29.812 8.769   -21.831 1.00 62.53  ? 89  ASN   B CA   1 
ATOM   4322 C C    . ASN   B 1 89  ? -30.957 9.747   -21.601 1.00 64.46  ? 89  ASN   B C    1 
ATOM   4323 O O    . ASN   B 1 89  ? -31.792 9.521   -20.723 1.00 63.15  ? 89  ASN   B O    1 
ATOM   4324 C CB   . ASN   B 1 89  ? -28.550 9.247   -21.107 1.00 57.41  ? 89  ASN   B CB   1 
ATOM   4325 C CG   . ASN   B 1 89  ? -27.372 8.297   -21.297 1.00 59.44  ? 89  ASN   B CG   1 
ATOM   4326 O OD1  . ASN   B 1 89  ? -27.546 7.143   -21.672 1.00 61.33  ? 89  ASN   B OD1  1 
ATOM   4327 N ND2  . ASN   B 1 89  ? -26.166 8.783   -21.035 1.00 59.29  ? 89  ASN   B ND2  1 
ATOM   4328 N N    . ASN   B 1 90  ? -31.023 10.840  -22.359 1.00 66.54  ? 90  ASN   B N    1 
ATOM   4329 C CA   . ASN   B 1 90  ? -32.174 11.734  -22.295 1.00 64.33  ? 90  ASN   B CA   1 
ATOM   4330 C C    . ASN   B 1 90  ? -32.911 11.651  -23.631 1.00 65.62  ? 90  ASN   B C    1 
ATOM   4331 O O    . ASN   B 1 90  ? -32.794 12.528  -24.490 1.00 65.21  ? 90  ASN   B O    1 
ATOM   4332 C CB   . ASN   B 1 90  ? -31.727 13.187  -21.952 1.00 62.85  ? 90  ASN   B CB   1 
ATOM   4333 C CG   . ASN   B 1 90  ? -32.890 14.083  -21.538 1.00 67.62  ? 90  ASN   B CG   1 
ATOM   4334 O OD1  . ASN   B 1 90  ? -34.031 13.622  -21.407 1.00 66.84  ? 90  ASN   B OD1  1 
ATOM   4335 N ND2  . ASN   B 1 90  ? -32.601 15.370  -21.306 1.00 62.54  ? 90  ASN   B ND2  1 
ATOM   4336 N N    . ARG   B 1 91  ? -33.693 10.594  -23.803 1.00 78.17  ? 91  ARG   B N    1 
ATOM   4337 C CA   . ARG   B 1 91  ? -34.644 10.637  -24.896 1.00 76.62  ? 91  ARG   B CA   1 
ATOM   4338 C C    . ARG   B 1 91  ? -35.759 11.607  -24.515 1.00 80.41  ? 91  ARG   B C    1 
ATOM   4339 O O    . ARG   B 1 91  ? -35.973 11.916  -23.338 1.00 86.09  ? 91  ARG   B O    1 
ATOM   4340 C CB   . ARG   B 1 91  ? -35.186 9.241   -25.208 1.00 76.60  ? 91  ARG   B CB   1 
ATOM   4341 C CG   . ARG   B 1 91  ? -36.536 8.942   -24.573 1.00 82.66  ? 91  ARG   B CG   1 
ATOM   4342 C CD   . ARG   B 1 91  ? -36.940 7.474   -24.691 1.00 82.29  ? 91  ARG   B CD   1 
ATOM   4343 N NE   . ARG   B 1 91  ? -35.946 6.574   -24.121 1.00 80.02  ? 91  ARG   B NE   1 
ATOM   4344 C CZ   . ARG   B 1 91  ? -36.016 6.051   -22.902 1.00 88.12  ? 91  ARG   B CZ   1 
ATOM   4345 N NH1  . ARG   B 1 91  ? -37.022 6.325   -22.086 1.00 91.61  ? 91  ARG   B NH1  1 
ATOM   4346 N NH2  . ARG   B 1 91  ? -35.049 5.235   -22.487 1.00 85.59  ? 91  ARG   B NH2  1 
ATOM   4347 N N    . ASN   B 1 92  ? -36.478 12.094  -25.518 1.00 74.03  ? 92  ASN   B N    1 
ATOM   4348 C CA   . ASN   B 1 92  ? -37.568 13.051  -25.348 1.00 72.38  ? 92  ASN   B CA   1 
ATOM   4349 C C    . ASN   B 1 92  ? -37.102 14.460  -25.024 1.00 67.72  ? 92  ASN   B C    1 
ATOM   4350 O O    . ASN   B 1 92  ? -37.952 15.348  -24.906 1.00 70.34  ? 92  ASN   B O    1 
ATOM   4351 C CB   . ASN   B 1 92  ? -38.567 12.627  -24.259 1.00 72.23  ? 92  ASN   B CB   1 
ATOM   4352 C CG   . ASN   B 1 92  ? -39.039 11.198  -24.428 1.00 76.12  ? 92  ASN   B CG   1 
ATOM   4353 O OD1  . ASN   B 1 92  ? -39.282 10.483  -23.448 1.00 74.05  ? 92  ASN   B OD1  1 
ATOM   4354 N ND2  . ASN   B 1 92  ? -39.152 10.763  -25.696 1.00 81.83  ? 92  ASN   B ND2  1 
ATOM   4355 N N    . ARG   B 1 93  ? -35.793 14.710  -24.904 1.00 54.31  ? 93  ARG   B N    1 
ATOM   4356 C CA   . ARG   B 1 93  ? -35.328 16.085  -24.712 1.00 56.19  ? 93  ARG   B CA   1 
ATOM   4357 C C    . ARG   B 1 93  ? -35.746 16.965  -25.881 1.00 54.39  ? 93  ARG   B C    1 
ATOM   4358 O O    . ARG   B 1 93  ? -36.072 18.149  -25.706 1.00 52.18  ? 93  ARG   B O    1 
ATOM   4359 C CB   . ARG   B 1 93  ? -33.811 16.128  -24.526 1.00 54.45  ? 93  ARG   B CB   1 
ATOM   4360 C CG   . ARG   B 1 93  ? -33.287 17.538  -24.518 1.00 50.52  ? 93  ARG   B CG   1 
ATOM   4361 C CD   . ARG   B 1 93  ? -31.847 17.659  -24.087 1.00 48.99  ? 93  ARG   B CD   1 
ATOM   4362 N NE   . ARG   B 1 93  ? -31.411 19.026  -24.340 1.00 48.81  ? 93  ARG   B NE   1 
ATOM   4363 C CZ   . ARG   B 1 93  ? -30.169 19.469  -24.215 1.00 46.59  ? 93  ARG   B CZ   1 
ATOM   4364 N NH1  . ARG   B 1 93  ? -29.193 18.684  -23.780 1.00 45.25  ? 93  ARG   B NH1  1 
ATOM   4365 N NH2  . ARG   B 1 93  ? -29.897 20.722  -24.562 1.00 45.93  ? 93  ARG   B NH2  1 
ATOM   4366 N N    . PHE   B 1 94  ? -35.740 16.394  -27.082 1.00 56.23  ? 94  PHE   B N    1 
ATOM   4367 C CA   . PHE   B 1 94  ? -36.091 17.086  -28.309 1.00 57.79  ? 94  PHE   B CA   1 
ATOM   4368 C C    . PHE   B 1 94  ? -37.361 16.497  -28.915 1.00 60.39  ? 94  PHE   B C    1 
ATOM   4369 O O    . PHE   B 1 94  ? -37.684 16.787  -30.073 1.00 60.95  ? 94  PHE   B O    1 
ATOM   4370 C CB   . PHE   B 1 94  ? -34.916 17.056  -29.296 1.00 54.82  ? 94  PHE   B CB   1 
ATOM   4371 C CG   . PHE   B 1 94  ? -33.784 17.944  -28.880 1.00 54.24  ? 94  PHE   B CG   1 
ATOM   4372 C CD1  . PHE   B 1 94  ? -33.868 19.320  -29.059 1.00 54.05  ? 94  PHE   B CD1  1 
ATOM   4373 C CD2  . PHE   B 1 94  ? -32.654 17.417  -28.272 1.00 52.82  ? 94  PHE   B CD2  1 
ATOM   4374 C CE1  . PHE   B 1 94  ? -32.835 20.158  -28.647 1.00 53.73  ? 94  PHE   B CE1  1 
ATOM   4375 C CE2  . PHE   B 1 94  ? -31.611 18.250  -27.858 1.00 52.15  ? 94  PHE   B CE2  1 
ATOM   4376 C CZ   . PHE   B 1 94  ? -31.707 19.621  -28.035 1.00 50.64  ? 94  PHE   B CZ   1 
ATOM   4377 N N    . GLY   B 1 95  ? -38.066 15.654  -28.163 1.00 61.81  ? 95  GLY   B N    1 
ATOM   4378 C CA   . GLY   B 1 95  ? -39.316 15.066  -28.592 1.00 60.40  ? 95  GLY   B CA   1 
ATOM   4379 C C    . GLY   B 1 95  ? -39.122 13.649  -29.078 1.00 61.24  ? 95  GLY   B C    1 
ATOM   4380 O O    . GLY   B 1 95  ? -38.377 12.883  -28.456 1.00 62.50  ? 95  GLY   B O    1 
ATOM   4381 N N    . GLN   B 1 96  ? -39.781 13.293  -30.182 1.00 84.60  ? 96  GLN   B N    1 
ATOM   4382 C CA   . GLN   B 1 96  ? -39.747 11.937  -30.734 1.00 84.30  ? 96  GLN   B CA   1 
ATOM   4383 C C    . GLN   B 1 96  ? -38.602 11.817  -31.740 1.00 80.79  ? 96  GLN   B C    1 
ATOM   4384 O O    . GLN   B 1 96  ? -38.728 12.214  -32.904 1.00 81.53  ? 96  GLN   B O    1 
ATOM   4385 C CB   . GLN   B 1 96  ? -41.086 11.605  -31.374 1.00 84.85  ? 96  GLN   B CB   1 
ATOM   4386 C CG   . GLN   B 1 96  ? -42.247 11.778  -30.430 1.00 85.47  ? 96  GLN   B CG   1 
ATOM   4387 C CD   . GLN   B 1 96  ? -43.251 10.662  -30.547 1.00 89.98  ? 96  GLN   B CD   1 
ATOM   4388 O OE1  . GLN   B 1 96  ? -43.163 9.656   -29.845 1.00 94.07  ? 96  GLN   B OE1  1 
ATOM   4389 N NE2  . GLN   B 1 96  ? -44.216 10.831  -31.443 1.00 89.46  ? 96  GLN   B NE2  1 
ATOM   4390 N N    . THR   B 1 97  ? -37.488 11.239  -31.287 1.00 61.80  ? 97  THR   B N    1 
ATOM   4391 C CA   . THR   B 1 97  ? -36.269 11.096  -32.087 1.00 57.54  ? 97  THR   B CA   1 
ATOM   4392 C C    . THR   B 1 97  ? -35.777 9.649   -32.016 1.00 55.61  ? 97  THR   B C    1 
ATOM   4393 O O    . THR   B 1 97  ? -34.673 9.368   -31.531 1.00 51.22  ? 97  THR   B O    1 
ATOM   4394 C CB   . THR   B 1 97  ? -35.199 12.089  -31.631 1.00 54.20  ? 97  THR   B CB   1 
ATOM   4395 O OG1  . THR   B 1 97  ? -34.893 11.879  -30.251 1.00 56.80  ? 97  THR   B OG1  1 
ATOM   4396 C CG2  . THR   B 1 97  ? -35.713 13.522  -31.798 1.00 51.88  ? 97  THR   B CG2  1 
ATOM   4397 N N    . PRO   B 1 98  ? -36.603 8.693   -32.472 1.00 61.12  ? 98  PRO   B N    1 
ATOM   4398 C CA   . PRO   B 1 98  ? -36.204 7.273   -32.375 1.00 57.30  ? 98  PRO   B CA   1 
ATOM   4399 C C    . PRO   B 1 98  ? -34.914 6.926   -33.112 1.00 56.01  ? 98  PRO   B C    1 
ATOM   4400 O O    . PRO   B 1 98  ? -34.141 6.094   -32.617 1.00 55.72  ? 98  PRO   B O    1 
ATOM   4401 C CB   . PRO   B 1 98  ? -37.416 6.534   -32.964 1.00 58.06  ? 98  PRO   B CB   1 
ATOM   4402 C CG   . PRO   B 1 98  ? -38.174 7.574   -33.747 1.00 57.07  ? 98  PRO   B CG   1 
ATOM   4403 C CD   . PRO   B 1 98  ? -37.954 8.856   -33.041 1.00 56.48  ? 98  PRO   B CD   1 
ATOM   4404 N N    . VAL   B 1 99  ? -34.650 7.520   -34.281 1.00 53.17  ? 99  VAL   B N    1 
ATOM   4405 C CA   . VAL   B 1 99  ? -33.443 7.162   -35.032 1.00 51.54  ? 99  VAL   B CA   1 
ATOM   4406 C C    . VAL   B 1 99  ? -32.189 7.709   -34.352 1.00 51.19  ? 99  VAL   B C    1 
ATOM   4407 O O    . VAL   B 1 99  ? -31.192 6.994   -34.177 1.00 48.68  ? 99  VAL   B O    1 
ATOM   4408 C CB   . VAL   B 1 99  ? -33.535 7.657   -36.486 1.00 53.36  ? 99  VAL   B CB   1 
ATOM   4409 C CG1  . VAL   B 1 99  ? -32.167 7.503   -37.169 1.00 48.63  ? 99  VAL   B CG1  1 
ATOM   4410 C CG2  . VAL   B 1 99  ? -34.637 6.905   -37.257 1.00 49.75  ? 99  VAL   B CG2  1 
ATOM   4411 N N    . GLN   B 1 100 ? -32.204 8.997   -33.996 1.00 45.70  ? 100 GLN   B N    1 
ATOM   4412 C CA   . GLN   B 1 100 ? -31.104 9.565   -33.225 1.00 49.55  ? 100 GLN   B CA   1 
ATOM   4413 C C    . GLN   B 1 100 ? -30.904 8.811   -31.903 1.00 49.36  ? 100 GLN   B C    1 
ATOM   4414 O O    . GLN   B 1 100 ? -29.765 8.561   -31.488 1.00 47.97  ? 100 GLN   B O    1 
ATOM   4415 C CB   . GLN   B 1 100 ? -31.367 11.044  -32.951 1.00 50.23  ? 100 GLN   B CB   1 
ATOM   4416 C CG   . GLN   B 1 100 ? -31.226 11.978  -34.117 1.00 47.14  ? 100 GLN   B CG   1 
ATOM   4417 C CD   . GLN   B 1 100 ? -31.844 13.328  -33.791 1.00 49.48  ? 100 GLN   B CD   1 
ATOM   4418 O OE1  . GLN   B 1 100 ? -31.155 14.253  -33.344 1.00 47.46  ? 100 GLN   B OE1  1 
ATOM   4419 N NE2  . GLN   B 1 100 ? -33.161 13.439  -33.987 1.00 48.15  ? 100 GLN   B NE2  1 
ATOM   4420 N N    . GLU   B 1 101 ? -31.998 8.448   -31.225 1.00 56.30  ? 101 GLU   B N    1 
ATOM   4421 C CA   . GLU   B 1 101 ? -31.872 7.702   -29.976 1.00 59.33  ? 101 GLU   B CA   1 
ATOM   4422 C C    . GLU   B 1 101 ? -31.187 6.361   -30.201 1.00 59.85  ? 101 GLU   B C    1 
ATOM   4423 O O    . GLU   B 1 101 ? -30.303 5.965   -29.429 1.00 58.02  ? 101 GLU   B O    1 
ATOM   4424 C CB   . GLU   B 1 101 ? -33.244 7.494   -29.340 1.00 59.23  ? 101 GLU   B CB   1 
ATOM   4425 C CG   . GLU   B 1 101 ? -33.169 6.945   -27.927 1.00 62.08  ? 101 GLU   B CG   1 
ATOM   4426 C CD   . GLU   B 1 101 ? -34.448 6.248   -27.509 1.00 64.21  ? 101 GLU   B CD   1 
ATOM   4427 O OE1  . GLU   B 1 101 ? -35.523 6.707   -27.949 1.00 69.78  ? 101 GLU   B OE1  1 
ATOM   4428 O OE2  . GLU   B 1 101 ? -34.389 5.266   -26.736 1.00 66.82  ? 101 GLU   B OE2  1 
ATOM   4429 N N    . ARG   B 1 102 ? -31.593 5.635   -31.253 1.00 55.34  ? 102 ARG   B N    1 
ATOM   4430 C CA   . ARG   B 1 102 ? -31.024 4.311   -31.483 1.00 54.62  ? 102 ARG   B CA   1 
ATOM   4431 C C    . ARG   B 1 102 ? -29.567 4.399   -31.923 1.00 56.37  ? 102 ARG   B C    1 
ATOM   4432 O O    . ARG   B 1 102 ? -28.747 3.562   -31.529 1.00 55.37  ? 102 ARG   B O    1 
ATOM   4433 C CB   . ARG   B 1 102 ? -31.845 3.543   -32.511 1.00 56.43  ? 102 ARG   B CB   1 
ATOM   4434 C CG   . ARG   B 1 102 ? -31.321 2.148   -32.759 1.00 57.06  ? 102 ARG   B CG   1 
ATOM   4435 C CD   . ARG   B 1 102 ? -32.393 1.211   -33.290 1.00 55.00  ? 102 ARG   B CD   1 
ATOM   4436 N NE   . ARG   B 1 102 ? -31.854 -0.126  -33.521 1.00 58.56  ? 102 ARG   B NE   1 
ATOM   4437 C CZ   . ARG   B 1 102 ? -32.349 -1.007  -34.382 1.00 57.56  ? 102 ARG   B CZ   1 
ATOM   4438 N NH1  . ARG   B 1 102 ? -33.417 -0.735  -35.115 1.00 55.27  ? 102 ARG   B NH1  1 
ATOM   4439 N NH2  . ARG   B 1 102 ? -31.771 -2.200  -34.493 1.00 57.49  ? 102 ARG   B NH2  1 
ATOM   4440 N N    . LEU   B 1 103 ? -29.222 5.395   -32.752 1.00 50.60  ? 103 LEU   B N    1 
ATOM   4441 C CA   . LEU   B 1 103 ? -27.820 5.582   -33.120 1.00 47.81  ? 103 LEU   B CA   1 
ATOM   4442 C C    . LEU   B 1 103 ? -26.977 5.923   -31.880 1.00 49.39  ? 103 LEU   B C    1 
ATOM   4443 O O    . LEU   B 1 103 ? -25.902 5.336   -31.658 1.00 48.45  ? 103 LEU   B O    1 
ATOM   4444 C CB   . LEU   B 1 103 ? -27.718 6.657   -34.210 1.00 48.37  ? 103 LEU   B CB   1 
ATOM   4445 C CG   . LEU   B 1 103 ? -28.092 6.255   -35.674 1.00 49.50  ? 103 LEU   B CG   1 
ATOM   4446 C CD1  . LEU   B 1 103 ? -28.404 7.458   -36.613 1.00 40.55  ? 103 LEU   B CD1  1 
ATOM   4447 C CD2  . LEU   B 1 103 ? -27.027 5.351   -36.309 1.00 40.00  ? 103 LEU   B CD2  1 
ATOM   4448 N N    . SER   B 1 104 ? -27.475 6.835   -31.030 1.00 48.78  ? 104 SER   B N    1 
ATOM   4449 C CA   . SER   B 1 104 ? -26.782 7.158   -29.783 1.00 48.25  ? 104 SER   B CA   1 
ATOM   4450 C C    . SER   B 1 104 ? -26.521 5.893   -28.970 1.00 47.06  ? 104 SER   B C    1 
ATOM   4451 O O    . SER   B 1 104 ? -25.378 5.615   -28.588 1.00 46.08  ? 104 SER   B O    1 
ATOM   4452 C CB   . SER   B 1 104 ? -27.620 8.163   -28.981 1.00 47.53  ? 104 SER   B CB   1 
ATOM   4453 O OG   . SER   B 1 104 ? -27.005 8.551   -27.754 1.00 49.58  ? 104 SER   B OG   1 
ATOM   4454 N N    . CYS   B 1 105 ? -27.559 5.072   -28.758 1.00 54.51  ? 105 CYS   B N    1 
ATOM   4455 C CA   . CYS   B 1 105 ? -27.395 3.868   -27.941 1.00 55.35  ? 105 CYS   B CA   1 
ATOM   4456 C C    . CYS   B 1 105 ? -26.456 2.863   -28.601 1.00 58.25  ? 105 CYS   B C    1 
ATOM   4457 O O    . CYS   B 1 105 ? -25.765 2.113   -27.903 1.00 56.63  ? 105 CYS   B O    1 
ATOM   4458 C CB   . CYS   B 1 105 ? -28.747 3.207   -27.681 1.00 52.09  ? 105 CYS   B CB   1 
ATOM   4459 S SG   . CYS   B 1 105 ? -29.936 4.183   -26.738 1.00 62.23  ? 105 CYS   B SG   1 
ATOM   4460 N N    . LEU   B 1 106 ? -26.474 2.769   -29.945 1.00 53.57  ? 106 LEU   B N    1 
ATOM   4461 C CA   . LEU   B 1 106 ? -25.554 1.858   -30.627 1.00 54.10  ? 106 LEU   B CA   1 
ATOM   4462 C C    . LEU   B 1 106 ? -24.105 2.279   -30.400 1.00 52.27  ? 106 LEU   B C    1 
ATOM   4463 O O    . LEU   B 1 106 ? -23.239 1.437   -30.128 1.00 52.97  ? 106 LEU   B O    1 
ATOM   4464 C CB   . LEU   B 1 106 ? -25.878 1.765   -32.135 1.00 52.39  ? 106 LEU   B CB   1 
ATOM   4465 C CG   . LEU   B 1 106 ? -27.199 1.099   -32.579 1.00 51.31  ? 106 LEU   B CG   1 
ATOM   4466 C CD1  . LEU   B 1 106 ? -27.621 1.487   -34.036 1.00 50.16  ? 106 LEU   B CD1  1 
ATOM   4467 C CD2  . LEU   B 1 106 ? -27.131 -0.420  -32.431 1.00 48.15  ? 106 LEU   B CD2  1 
ATOM   4468 N N    . ALA   B 1 107 ? -23.824 3.577   -30.490 1.00 49.52  ? 107 ALA   B N    1 
ATOM   4469 C CA   . ALA   B 1 107 ? -22.474 4.048   -30.183 1.00 48.98  ? 107 ALA   B CA   1 
ATOM   4470 C C    . ALA   B 1 107 ? -22.141 3.848   -28.702 1.00 50.66  ? 107 ALA   B C    1 
ATOM   4471 O O    . ALA   B 1 107 ? -20.987 3.575   -28.343 1.00 51.38  ? 107 ALA   B O    1 
ATOM   4472 C CB   . ALA   B 1 107 ? -22.322 5.518   -30.576 1.00 47.33  ? 107 ALA   B CB   1 
ATOM   4473 N N    . LYS   B 1 108 ? -23.130 3.997   -27.827 1.00 53.27  ? 108 LYS   B N    1 
ATOM   4474 C CA   . LYS   B 1 108 ? -22.852 3.958   -26.389 1.00 54.42  ? 108 LYS   B CA   1 
ATOM   4475 C C    . LYS   B 1 108 ? -22.654 2.532   -25.869 1.00 55.46  ? 108 LYS   B C    1 
ATOM   4476 O O    . LYS   B 1 108 ? -21.636 2.227   -25.238 1.00 54.88  ? 108 LYS   B O    1 
ATOM   4477 C CB   . LYS   B 1 108 ? -23.985 4.651   -25.635 1.00 53.41  ? 108 LYS   B CB   1 
ATOM   4478 C CG   . LYS   B 1 108 ? -23.541 5.171   -24.291 1.00 51.09  ? 108 LYS   B CG   1 
ATOM   4479 C CD   . LYS   B 1 108 ? -24.187 4.447   -23.182 1.00 55.13  ? 108 LYS   B CD   1 
ATOM   4480 C CE   . LYS   B 1 108 ? -25.694 4.651   -23.109 1.00 55.89  ? 108 LYS   B CE   1 
ATOM   4481 N NZ   . LYS   B 1 108 ? -26.116 4.263   -21.638 1.00 53.35  ? 108 LYS   B NZ   1 
ATOM   4482 N N    . ASN   B 1 109 ? -23.617 1.643   -26.151 1.00 63.38  ? 109 ASN   B N    1 
ATOM   4483 C CA   . ASN   B 1 109 ? -23.568 0.264   -25.676 1.00 59.45  ? 109 ASN   B CA   1 
ATOM   4484 C C    . ASN   B 1 109 ? -22.361 -0.483  -26.242 1.00 63.72  ? 109 ASN   B C    1 
ATOM   4485 O O    . ASN   B 1 109 ? -21.811 -1.364  -25.575 1.00 63.84  ? 109 ASN   B O    1 
ATOM   4486 C CB   . ASN   B 1 109 ? -24.869 -0.468  -26.068 1.00 62.50  ? 109 ASN   B CB   1 
ATOM   4487 C CG   . ASN   B 1 109 ? -26.120 0.021   -25.288 1.00 63.77  ? 109 ASN   B CG   1 
ATOM   4488 O OD1  . ASN   B 1 109 ? -26.101 1.066   -24.637 1.00 63.83  ? 109 ASN   B OD1  1 
ATOM   4489 N ND2  . ASN   B 1 109 ? -27.211 -0.745  -25.373 1.00 63.91  ? 109 ASN   B ND2  1 
ATOM   4490 N N    . ASN   B 1 110 ? -21.903 -0.117  -27.445 1.00 60.55  ? 110 ASN   B N    1 
ATOM   4491 C CA   . ASN   B 1 110 ? -20.743 -0.742  -28.074 1.00 56.83  ? 110 ASN   B CA   1 
ATOM   4492 C C    . ASN   B 1 110 ? -19.486 0.118   -27.950 1.00 55.65  ? 110 ASN   B C    1 
ATOM   4493 O O    . ASN   B 1 110 ? -18.434 -0.251  -28.493 1.00 54.26  ? 110 ASN   B O    1 
ATOM   4494 C CB   . ASN   B 1 110 ? -21.037 -1.038  -29.553 1.00 56.59  ? 110 ASN   B CB   1 
ATOM   4495 C CG   . ASN   B 1 110 ? -22.234 -1.975  -29.742 1.00 59.46  ? 110 ASN   B CG   1 
ATOM   4496 O OD1  . ASN   B 1 110 ? -22.143 -3.187  -29.491 1.00 59.28  ? 110 ASN   B OD1  1 
ATOM   4497 N ND2  . ASN   B 1 110 ? -23.364 -1.413  -30.162 1.00 55.54  ? 110 ASN   B ND2  1 
ATOM   4498 N N    . SER   B 1 111 ? -19.578 1.235   -27.223 1.00 54.43  ? 111 SER   B N    1 
ATOM   4499 C CA   . SER   B 1 111 ? -18.453 2.108   -26.856 1.00 56.40  ? 111 SER   B CA   1 
ATOM   4500 C C    . SER   B 1 111 ? -17.576 2.433   -28.063 1.00 52.18  ? 111 SER   B C    1 
ATOM   4501 O O    . SER   B 1 111 ? -16.367 2.178   -28.088 1.00 50.78  ? 111 SER   B O    1 
ATOM   4502 C CB   . SER   B 1 111 ? -17.628 1.481   -25.719 1.00 55.82  ? 111 SER   B CB   1 
ATOM   4503 O OG   . SER   B 1 111 ? -16.432 2.220   -25.503 1.00 55.52  ? 111 SER   B OG   1 
ATOM   4504 N N    . ILE   B 1 112 ? -18.214 3.066   -29.048 1.00 49.64  ? 112 ILE   B N    1 
ATOM   4505 C CA   . ILE   B 1 112 ? -17.614 3.308   -30.361 1.00 50.61  ? 112 ILE   B CA   1 
ATOM   4506 C C    . ILE   B 1 112 ? -18.247 4.545   -30.995 1.00 48.44  ? 112 ILE   B C    1 
ATOM   4507 O O    . ILE   B 1 112 ? -19.457 4.768   -30.885 1.00 47.56  ? 112 ILE   B O    1 
ATOM   4508 C CB   . ILE   B 1 112 ? -17.774 2.071   -31.278 1.00 54.67  ? 112 ILE   B CB   1 
ATOM   4509 C CG1  . ILE   B 1 112 ? -16.983 2.230   -32.582 1.00 52.16  ? 112 ILE   B CG1  1 
ATOM   4510 C CG2  . ILE   B 1 112 ? -19.256 1.816   -31.609 1.00 51.76  ? 112 ILE   B CG2  1 
ATOM   4511 C CD1  . ILE   B 1 112 ? -17.000 0.990   -33.426 1.00 48.66  ? 112 ILE   B CD1  1 
ATOM   4512 N N    . TYR   B 1 113 ? -17.418 5.365   -31.642 1.00 48.73  ? 113 TYR   B N    1 
ATOM   4513 C CA   . TYR   B 1 113 ? -17.945 6.451   -32.463 1.00 49.75  ? 113 TYR   B CA   1 
ATOM   4514 C C    . TYR   B 1 113 ? -18.744 5.870   -33.629 1.00 50.37  ? 113 TYR   B C    1 
ATOM   4515 O O    . TYR   B 1 113 ? -18.312 4.917   -34.289 1.00 49.49  ? 113 TYR   B O    1 
ATOM   4516 C CB   . TYR   B 1 113 ? -16.808 7.317   -33.010 1.00 48.98  ? 113 TYR   B CB   1 
ATOM   4517 C CG   . TYR   B 1 113 ? -16.277 8.334   -32.044 1.00 49.76  ? 113 TYR   B CG   1 
ATOM   4518 C CD1  . TYR   B 1 113 ? -15.450 7.954   -30.986 1.00 51.35  ? 113 TYR   B CD1  1 
ATOM   4519 C CD2  . TYR   B 1 113 ? -16.589 9.683   -32.179 1.00 48.99  ? 113 TYR   B CD2  1 
ATOM   4520 C CE1  . TYR   B 1 113 ? -14.960 8.894   -30.087 1.00 49.12  ? 113 TYR   B CE1  1 
ATOM   4521 C CE2  . TYR   B 1 113 ? -16.092 10.636  -31.291 1.00 49.91  ? 113 TYR   B CE2  1 
ATOM   4522 C CZ   . TYR   B 1 113 ? -15.283 10.232  -30.242 1.00 51.74  ? 113 TYR   B CZ   1 
ATOM   4523 O OH   . TYR   B 1 113 ? -14.788 11.160  -29.336 1.00 55.43  ? 113 TYR   B OH   1 
ATOM   4524 N N    . VAL   B 1 114 ? -19.910 6.445   -33.884 1.00 46.96  ? 114 VAL   B N    1 
ATOM   4525 C CA   . VAL   B 1 114 ? -20.767 6.019   -34.986 1.00 45.54  ? 114 VAL   B CA   1 
ATOM   4526 C C    . VAL   B 1 114 ? -21.019 7.207   -35.908 1.00 44.35  ? 114 VAL   B C    1 
ATOM   4527 O O    . VAL   B 1 114 ? -21.493 8.260   -35.455 1.00 46.09  ? 114 VAL   B O    1 
ATOM   4528 C CB   . VAL   B 1 114 ? -22.094 5.434   -34.470 1.00 47.93  ? 114 VAL   B CB   1 
ATOM   4529 C CG1  . VAL   B 1 114 ? -23.005 5.113   -35.645 1.00 42.48  ? 114 VAL   B CG1  1 
ATOM   4530 C CG2  . VAL   B 1 114 ? -21.845 4.192   -33.570 1.00 44.35  ? 114 VAL   B CG2  1 
ATOM   4531 N N    . VAL   B 1 115 ? -20.714 7.033   -37.197 1.00 46.51  ? 115 VAL   B N    1 
ATOM   4532 C CA   . VAL   B 1 115 ? -21.022 8.018   -38.243 1.00 46.12  ? 115 VAL   B CA   1 
ATOM   4533 C C    . VAL   B 1 115 ? -22.127 7.441   -39.126 1.00 47.16  ? 115 VAL   B C    1 
ATOM   4534 O O    . VAL   B 1 115 ? -21.951 6.384   -39.748 1.00 44.69  ? 115 VAL   B O    1 
ATOM   4535 C CB   . VAL   B 1 115 ? -19.791 8.369   -39.099 1.00 45.89  ? 115 VAL   B CB   1 
ATOM   4536 C CG1  . VAL   B 1 115 ? -20.115 9.514   -40.089 1.00 43.76  ? 115 VAL   B CG1  1 
ATOM   4537 C CG2  . VAL   B 1 115 ? -18.590 8.720   -38.248 1.00 43.81  ? 115 VAL   B CG2  1 
ATOM   4538 N N    . ALA   B 1 116 ? -23.256 8.139   -39.203 1.00 47.58  ? 116 ALA   B N    1 
ATOM   4539 C CA   . ALA   B 1 116 ? -24.374 7.652   -40.001 1.00 46.65  ? 116 ALA   B CA   1 
ATOM   4540 C C    . ALA   B 1 116 ? -24.959 8.819   -40.792 1.00 47.33  ? 116 ALA   B C    1 
ATOM   4541 O O    . ALA   B 1 116 ? -24.676 9.988   -40.510 1.00 46.06  ? 116 ALA   B O    1 
ATOM   4542 C CB   . ALA   B 1 116 ? -25.435 6.952   -39.128 1.00 41.29  ? 116 ALA   B CB   1 
ATOM   4543 N N    . ASN   B 1 117 ? -25.727 8.486   -41.837 1.00 47.20  ? 117 ASN   B N    1 
ATOM   4544 C CA   . ASN   B 1 117 ? -26.390 9.465   -42.692 1.00 40.73  ? 117 ASN   B CA   1 
ATOM   4545 C C    . ASN   B 1 117 ? -27.898 9.308   -42.538 1.00 42.00  ? 117 ASN   B C    1 
ATOM   4546 O O    . ASN   B 1 117 ? -28.423 8.199   -42.674 1.00 43.19  ? 117 ASN   B O    1 
ATOM   4547 C CB   . ASN   B 1 117 ? -25.999 9.270   -44.157 1.00 45.21  ? 117 ASN   B CB   1 
ATOM   4548 C CG   . ASN   B 1 117 ? -26.653 10.284  -45.060 1.00 42.11  ? 117 ASN   B CG   1 
ATOM   4549 O OD1  . ASN   B 1 117 ? -27.743 10.054  -45.599 1.00 41.36  ? 117 ASN   B OD1  1 
ATOM   4550 N ND2  . ASN   B 1 117 ? -26.019 11.445  -45.182 1.00 40.15  ? 117 ASN   B ND2  1 
ATOM   4551 N N    . ILE   B 1 118 ? -28.586 10.405  -42.231 1.00 42.51  ? 118 ILE   B N    1 
ATOM   4552 C CA   . ILE   B 1 118 ? -30.025 10.411  -41.968 1.00 43.88  ? 118 ILE   B CA   1 
ATOM   4553 C C    . ILE   B 1 118 ? -30.578 11.734  -42.479 1.00 46.58  ? 118 ILE   B C    1 
ATOM   4554 O O    . ILE   B 1 118 ? -29.876 12.475  -43.174 1.00 48.29  ? 118 ILE   B O    1 
ATOM   4555 C CB   . ILE   B 1 118 ? -30.363 10.189  -40.478 1.00 47.01  ? 118 ILE   B CB   1 
ATOM   4556 C CG1  . ILE   B 1 118 ? -29.787 11.303  -39.594 1.00 46.05  ? 118 ILE   B CG1  1 
ATOM   4557 C CG2  . ILE   B 1 118 ? -29.884 8.820   -40.024 1.00 45.74  ? 118 ILE   B CG2  1 
ATOM   4558 C CD1  . ILE   B 1 118 ? -30.131 11.151  -38.090 1.00 44.17  ? 118 ILE   B CD1  1 
ATOM   4559 N N    . GLY   B 1 119 ? -31.858 12.001  -42.233 1.00 48.30  ? 119 GLY   B N    1 
ATOM   4560 C CA   . GLY   B 1 119 ? -32.520 13.181  -42.761 1.00 46.87  ? 119 GLY   B CA   1 
ATOM   4561 C C    . GLY   B 1 119 ? -32.894 14.180  -41.680 1.00 46.91  ? 119 GLY   B C    1 
ATOM   4562 O O    . GLY   B 1 119 ? -33.620 13.850  -40.743 1.00 48.91  ? 119 GLY   B O    1 
ATOM   4563 N N    . ASP   B 1 120 ? -32.451 15.415  -41.865 1.00 47.63  ? 120 ASP   B N    1 
ATOM   4564 C CA   . ASP   B 1 120 ? -32.776 16.492  -40.940 1.00 47.54  ? 120 ASP   B CA   1 
ATOM   4565 C C    . ASP   B 1 120 ? -33.937 17.306  -41.490 1.00 49.46  ? 120 ASP   B C    1 
ATOM   4566 O O    . ASP   B 1 120 ? -33.999 17.570  -42.691 1.00 52.14  ? 120 ASP   B O    1 
ATOM   4567 C CB   . ASP   B 1 120 ? -31.556 17.394  -40.727 1.00 50.28  ? 120 ASP   B CB   1 
ATOM   4568 C CG   . ASP   B 1 120 ? -31.699 18.340  -39.526 1.00 51.35  ? 120 ASP   B CG   1 
ATOM   4569 O OD1  . ASP   B 1 120 ? -32.582 18.129  -38.666 1.00 51.72  ? 120 ASP   B OD1  1 
ATOM   4570 O OD2  . ASP   B 1 120 ? -30.898 19.298  -39.444 1.00 50.95  ? 120 ASP   B OD2  1 
ATOM   4571 N N    . LYS   B 1 121 ? -34.863 17.689  -40.616 1.00 48.03  ? 121 LYS   B N    1 
ATOM   4572 C CA   . LYS   B 1 121 ? -35.903 18.655  -40.947 1.00 47.49  ? 121 LYS   B CA   1 
ATOM   4573 C C    . LYS   B 1 121 ? -35.805 19.823  -39.981 1.00 50.39  ? 121 LYS   B C    1 
ATOM   4574 O O    . LYS   B 1 121 ? -35.572 19.635  -38.779 1.00 53.00  ? 121 LYS   B O    1 
ATOM   4575 C CB   . LYS   B 1 121 ? -37.305 18.045  -40.912 1.00 47.72  ? 121 LYS   B CB   1 
ATOM   4576 C CG   . LYS   B 1 121 ? -37.762 17.552  -39.559 1.00 48.12  ? 121 LYS   B CG   1 
ATOM   4577 C CD   . LYS   B 1 121 ? -39.190 17.027  -39.649 1.00 48.50  ? 121 LYS   B CD   1 
ATOM   4578 C CE   . LYS   B 1 121 ? -39.809 16.943  -38.251 1.00 48.84  ? 121 LYS   B CE   1 
ATOM   4579 N NZ   . LYS   B 1 121 ? -41.111 16.211  -38.274 1.00 52.21  ? 121 LYS   B NZ   1 
ATOM   4580 N N    . LYS   B 1 122 ? -35.952 21.025  -40.529 1.00 42.07  ? 122 LYS   B N    1 
ATOM   4581 C CA   . LYS   B 1 122 ? -35.825 22.280  -39.795 1.00 45.21  ? 122 LYS   B CA   1 
ATOM   4582 C C    . LYS   B 1 122 ? -37.033 23.151  -40.137 1.00 48.25  ? 122 LYS   B C    1 
ATOM   4583 O O    . LYS   B 1 122 ? -37.058 23.781  -41.210 1.00 46.78  ? 122 LYS   B O    1 
ATOM   4584 C CB   . LYS   B 1 122 ? -34.523 22.995  -40.148 1.00 43.58  ? 122 LYS   B CB   1 
ATOM   4585 C CG   . LYS   B 1 122 ? -33.270 22.458  -39.468 1.00 43.20  ? 122 LYS   B CG   1 
ATOM   4586 C CD   . LYS   B 1 122 ? -33.272 22.824  -37.947 1.00 46.04  ? 122 LYS   B CD   1 
ATOM   4587 C CE   . LYS   B 1 122 ? -32.049 22.255  -37.244 1.00 43.34  ? 122 LYS   B CE   1 
ATOM   4588 N NZ   . LYS   B 1 122 ? -32.242 20.796  -36.992 1.00 41.43  ? 122 LYS   B NZ   1 
ATOM   4589 N N    . PRO   B 1 123 ? -38.045 23.208  -39.264 1.00 52.83  ? 123 PRO   B N    1 
ATOM   4590 C CA   . PRO   B 1 123 ? -39.225 24.045  -39.540 1.00 52.13  ? 123 PRO   B CA   1 
ATOM   4591 C C    . PRO   B 1 123 ? -38.855 25.518  -39.657 1.00 55.93  ? 123 PRO   B C    1 
ATOM   4592 O O    . PRO   B 1 123 ? -37.941 26.001  -38.984 1.00 53.97  ? 123 PRO   B O    1 
ATOM   4593 C CB   . PRO   B 1 123 ? -40.135 23.793  -38.327 1.00 54.46  ? 123 PRO   B CB   1 
ATOM   4594 C CG   . PRO   B 1 123 ? -39.639 22.527  -37.708 1.00 54.78  ? 123 PRO   B CG   1 
ATOM   4595 C CD   . PRO   B 1 123 ? -38.161 22.479  -37.988 1.00 54.97  ? 123 PRO   B CD   1 
ATOM   4596 N N    . CYS   B 1 124 ? -39.562 26.230  -40.540 1.00 61.90  ? 124 CYS   B N    1 
ATOM   4597 C CA   . CYS   B 1 124 ? -39.386 27.668  -40.706 1.00 62.16  ? 124 CYS   B CA   1 
ATOM   4598 C C    . CYS   B 1 124 ? -40.731 28.316  -41.000 1.00 64.36  ? 124 CYS   B C    1 
ATOM   4599 O O    . CYS   B 1 124 ? -41.694 27.643  -41.373 1.00 64.64  ? 124 CYS   B O    1 
ATOM   4600 C CB   . CYS   B 1 124 ? -38.390 28.002  -41.818 1.00 61.17  ? 124 CYS   B CB   1 
ATOM   4601 S SG   . CYS   B 1 124 ? -38.742 27.177  -43.374 1.00 64.42  ? 124 CYS   B SG   1 
ATOM   4602 N N    . ASP   B 1 125 ? -40.802 29.625  -40.764 1.00 74.13  ? 125 ASP   B N    1 
ATOM   4603 C CA   . ASP   B 1 125 ? -41.994 30.418  -41.043 1.00 77.47  ? 125 ASP   B CA   1 
ATOM   4604 C C    . ASP   B 1 125 ? -41.810 31.282  -42.296 1.00 77.14  ? 125 ASP   B C    1 
ATOM   4605 O O    . ASP   B 1 125 ? -40.706 31.446  -42.824 1.00 75.02  ? 125 ASP   B O    1 
ATOM   4606 C CB   . ASP   B 1 125 ? -42.351 31.291  -39.840 1.00 76.87  ? 125 ASP   B CB   1 
ATOM   4607 C CG   . ASP   B 1 125 ? -43.112 30.521  -38.772 1.00 87.17  ? 125 ASP   B CG   1 
ATOM   4608 O OD1  . ASP   B 1 125 ? -42.580 29.511  -38.241 1.00 87.10  ? 125 ASP   B OD1  1 
ATOM   4609 O OD2  . ASP   B 1 125 ? -44.263 30.917  -38.480 1.00 90.99  ? 125 ASP   B OD2  1 
ATOM   4610 N N    . THR   B 1 126 ? -42.927 31.823  -42.789 1.00 83.71  ? 126 THR   B N    1 
ATOM   4611 C CA   . THR   B 1 126 ? -42.844 32.770  -43.898 1.00 84.93  ? 126 THR   B CA   1 
ATOM   4612 C C    . THR   B 1 126 ? -42.083 34.037  -43.524 1.00 83.65  ? 126 THR   B C    1 
ATOM   4613 O O    . THR   B 1 126 ? -41.591 34.738  -44.415 1.00 90.03  ? 126 THR   B O    1 
ATOM   4614 C CB   . THR   B 1 126 ? -44.239 33.121  -44.416 1.00 89.28  ? 126 THR   B CB   1 
ATOM   4615 O OG1  . THR   B 1 126 ? -45.135 32.035  -44.145 1.00 88.09  ? 126 THR   B OG1  1 
ATOM   4616 C CG2  . THR   B 1 126 ? -44.187 33.373  -45.937 1.00 84.67  ? 126 THR   B CG2  1 
ATOM   4617 N N    . SER   B 1 127 ? -41.963 34.338  -42.229 1.00 85.81  ? 127 SER   B N    1 
ATOM   4618 C CA   . SER   B 1 127 ? -41.054 35.392  -41.788 1.00 84.27  ? 127 SER   B CA   1 
ATOM   4619 C C    . SER   B 1 127 ? -39.678 35.256  -42.436 1.00 82.45  ? 127 SER   B C    1 
ATOM   4620 O O    . SER   B 1 127 ? -39.011 36.264  -42.701 1.00 82.09  ? 127 SER   B O    1 
ATOM   4621 C CB   . SER   B 1 127 ? -40.939 35.362  -40.259 1.00 81.06  ? 127 SER   B CB   1 
ATOM   4622 O OG   . SER   B 1 127 ? -40.979 34.027  -39.774 1.00 80.79  ? 127 SER   B OG   1 
ATOM   4623 N N    . ASP   B 1 128 ? -39.245 34.022  -42.701 1.00 66.64  ? 128 ASP   B N    1 
ATOM   4624 C CA   . ASP   B 1 128 ? -37.933 33.758  -43.277 1.00 63.99  ? 128 ASP   B CA   1 
ATOM   4625 C C    . ASP   B 1 128 ? -38.015 33.892  -44.794 1.00 68.28  ? 128 ASP   B C    1 
ATOM   4626 O O    . ASP   B 1 128 ? -38.760 33.135  -45.435 1.00 66.51  ? 128 ASP   B O    1 
ATOM   4627 C CB   . ASP   B 1 128 ? -37.475 32.353  -42.874 1.00 62.54  ? 128 ASP   B CB   1 
ATOM   4628 C CG   . ASP   B 1 128 ? -36.096 31.979  -43.425 1.00 66.55  ? 128 ASP   B CG   1 
ATOM   4629 O OD1  . ASP   B 1 128 ? -35.452 32.817  -44.094 1.00 69.73  ? 128 ASP   B OD1  1 
ATOM   4630 O OD2  . ASP   B 1 128 ? -35.641 30.839  -43.168 1.00 62.93  ? 128 ASP   B OD2  1 
ATOM   4631 N N    . PRO   B 1 129 ? -37.266 34.812  -45.409 1.00 78.72  ? 129 PRO   B N    1 
ATOM   4632 C CA   . PRO   B 1 129 ? -37.399 35.012  -46.860 1.00 76.01  ? 129 PRO   B CA   1 
ATOM   4633 C C    . PRO   B 1 129 ? -36.975 33.804  -47.670 1.00 73.92  ? 129 PRO   B C    1 
ATOM   4634 O O    . PRO   B 1 129 ? -37.380 33.682  -48.830 1.00 70.69  ? 129 PRO   B O    1 
ATOM   4635 C CB   . PRO   B 1 129 ? -36.499 36.221  -47.139 1.00 76.76  ? 129 PRO   B CB   1 
ATOM   4636 C CG   . PRO   B 1 129 ? -35.531 36.260  -46.032 1.00 72.27  ? 129 PRO   B CG   1 
ATOM   4637 C CD   . PRO   B 1 129 ? -36.151 35.585  -44.835 1.00 81.24  ? 129 PRO   B CD   1 
ATOM   4638 N N    . GLN   B 1 130 ? -36.197 32.886  -47.102 1.00 79.08  ? 130 GLN   B N    1 
ATOM   4639 C CA   . GLN   B 1 130 ? -35.798 31.693  -47.836 1.00 78.86  ? 130 GLN   B CA   1 
ATOM   4640 C C    . GLN   B 1 130 ? -36.433 30.418  -47.289 1.00 75.66  ? 130 GLN   B C    1 
ATOM   4641 O O    . GLN   B 1 130 ? -35.976 29.318  -47.618 1.00 73.00  ? 130 GLN   B O    1 
ATOM   4642 C CB   . GLN   B 1 130 ? -34.275 31.570  -47.845 1.00 75.32  ? 130 GLN   B CB   1 
ATOM   4643 C CG   . GLN   B 1 130 ? -33.578 32.873  -48.184 1.00 78.68  ? 130 GLN   B CG   1 
ATOM   4644 C CD   . GLN   B 1 130 ? -32.292 33.059  -47.415 1.00 83.91  ? 130 GLN   B CD   1 
ATOM   4645 O OE1  . GLN   B 1 130 ? -32.300 33.225  -46.190 1.00 85.49  ? 130 GLN   B OE1  1 
ATOM   4646 N NE2  . GLN   B 1 130 ? -31.172 33.024  -48.126 1.00 86.45  ? 130 GLN   B NE2  1 
ATOM   4647 N N    . CYS   B 1 131 ? -37.507 30.538  -46.510 1.00 71.65  ? 131 CYS   B N    1 
ATOM   4648 C CA   . CYS   B 1 131 ? -38.243 29.353  -46.079 1.00 72.59  ? 131 CYS   B CA   1 
ATOM   4649 C C    . CYS   B 1 131 ? -38.905 28.689  -47.283 1.00 70.27  ? 131 CYS   B C    1 
ATOM   4650 O O    . CYS   B 1 131 ? -39.682 29.338  -47.986 1.00 67.30  ? 131 CYS   B O    1 
ATOM   4651 C CB   . CYS   B 1 131 ? -39.293 29.720  -45.030 1.00 69.38  ? 131 CYS   B CB   1 
ATOM   4652 S SG   . CYS   B 1 131 ? -40.174 28.304  -44.313 1.00 73.06  ? 131 CYS   B SG   1 
ATOM   4653 N N    . PRO   B 1 132 ? -38.690 27.396  -47.509 1.00 63.34  ? 132 PRO   B N    1 
ATOM   4654 C CA   . PRO   B 1 132 ? -39.312 26.745  -48.651 1.00 62.27  ? 132 PRO   B CA   1 
ATOM   4655 C C    . PRO   B 1 132 ? -40.835 26.846  -48.560 1.00 64.49  ? 132 PRO   B C    1 
ATOM   4656 O O    . PRO   B 1 132 ? -41.395 26.984  -47.461 1.00 63.61  ? 132 PRO   B O    1 
ATOM   4657 C CB   . PRO   B 1 132 ? -38.833 25.292  -48.546 1.00 57.30  ? 132 PRO   B CB   1 
ATOM   4658 C CG   . PRO   B 1 132 ? -37.565 25.378  -47.802 1.00 59.82  ? 132 PRO   B CG   1 
ATOM   4659 C CD   . PRO   B 1 132 ? -37.780 26.484  -46.790 1.00 59.61  ? 132 PRO   B CD   1 
ATOM   4660 N N    . PRO   B 1 133 ? -41.517 26.829  -49.707 1.00 82.67  ? 133 PRO   B N    1 
ATOM   4661 C CA   . PRO   B 1 133 ? -42.976 27.040  -49.678 1.00 80.57  ? 133 PRO   B CA   1 
ATOM   4662 C C    . PRO   B 1 133 ? -43.726 26.056  -48.793 1.00 82.67  ? 133 PRO   B C    1 
ATOM   4663 O O    . PRO   B 1 133 ? -44.781 26.414  -48.255 1.00 88.83  ? 133 PRO   B O    1 
ATOM   4664 C CB   . PRO   B 1 133 ? -43.388 26.916  -51.151 1.00 80.29  ? 133 PRO   B CB   1 
ATOM   4665 C CG   . PRO   B 1 133 ? -42.139 27.045  -51.951 1.00 78.50  ? 133 PRO   B CG   1 
ATOM   4666 C CD   . PRO   B 1 133 ? -40.943 26.966  -51.055 1.00 80.26  ? 133 PRO   B CD   1 
ATOM   4667 N N    . ASP   B 1 134 ? -43.226 24.834  -48.604 1.00 70.58  ? 134 ASP   B N    1 
ATOM   4668 C CA   . ASP   B 1 134 ? -43.919 23.851  -47.780 1.00 67.44  ? 134 ASP   B CA   1 
ATOM   4669 C C    . ASP   B 1 134 ? -43.465 23.850  -46.315 1.00 67.93  ? 134 ASP   B C    1 
ATOM   4670 O O    . ASP   B 1 134 ? -43.713 22.867  -45.608 1.00 69.45  ? 134 ASP   B O    1 
ATOM   4671 C CB   . ASP   B 1 134 ? -43.775 22.453  -48.377 1.00 63.90  ? 134 ASP   B CB   1 
ATOM   4672 C CG   . ASP   B 1 134 ? -42.340 22.013  -48.489 1.00 63.27  ? 134 ASP   B CG   1 
ATOM   4673 O OD1  . ASP   B 1 134 ? -41.481 22.536  -47.739 1.00 61.53  ? 134 ASP   B OD1  1 
ATOM   4674 O OD2  . ASP   B 1 134 ? -42.083 21.136  -49.346 1.00 64.00  ? 134 ASP   B OD2  1 
ATOM   4675 N N    . GLY   B 1 135 ? -42.775 24.896  -45.858 1.00 55.13  ? 135 GLY   B N    1 
ATOM   4676 C CA   . GLY   B 1 135 ? -42.658 25.170  -44.430 1.00 52.39  ? 135 GLY   B CA   1 
ATOM   4677 C C    . GLY   B 1 135 ? -41.461 24.602  -43.699 1.00 56.23  ? 135 GLY   B C    1 
ATOM   4678 O O    . GLY   B 1 135 ? -41.394 24.727  -42.463 1.00 53.27  ? 135 GLY   B O    1 
ATOM   4679 N N    . ARG   B 1 136 ? -40.491 24.022  -44.400 1.00 61.92  ? 136 ARG   B N    1 
ATOM   4680 C CA   . ARG   B 1 136 ? -39.348 23.468  -43.690 1.00 58.28  ? 136 ARG   B CA   1 
ATOM   4681 C C    . ARG   B 1 136 ? -38.182 23.304  -44.645 1.00 57.77  ? 136 ARG   B C    1 
ATOM   4682 O O    . ARG   B 1 136 ? -38.371 23.194  -45.859 1.00 59.23  ? 136 ARG   B O    1 
ATOM   4683 C CB   . ARG   B 1 136 ? -39.697 22.123  -43.055 1.00 56.26  ? 136 ARG   B CB   1 
ATOM   4684 C CG   . ARG   B 1 136 ? -39.685 20.955  -44.025 1.00 58.10  ? 136 ARG   B CG   1 
ATOM   4685 C CD   . ARG   B 1 136 ? -41.020 20.816  -44.748 1.00 59.63  ? 136 ARG   B CD   1 
ATOM   4686 N NE   . ARG   B 1 136 ? -41.075 19.581  -45.519 1.00 61.05  ? 136 ARG   B NE   1 
ATOM   4687 C CZ   . ARG   B 1 136 ? -42.125 19.177  -46.222 1.00 61.13  ? 136 ARG   B CZ   1 
ATOM   4688 N NH1  . ARG   B 1 136 ? -43.227 19.903  -46.295 1.00 61.19  ? 136 ARG   B NH1  1 
ATOM   4689 N NH2  . ARG   B 1 136 ? -42.069 18.011  -46.864 1.00 59.74  ? 136 ARG   B NH2  1 
ATOM   4690 N N    . TYR   B 1 137 ? -36.972 23.339  -44.085 1.00 50.22  ? 137 TYR   B N    1 
ATOM   4691 C CA   . TYR   B 1 137 ? -35.792 22.859  -44.786 1.00 48.56  ? 137 TYR   B CA   1 
ATOM   4692 C C    . TYR   B 1 137 ? -35.653 21.368  -44.526 1.00 49.64  ? 137 TYR   B C    1 
ATOM   4693 O O    . TYR   B 1 137 ? -35.964 20.887  -43.430 1.00 49.52  ? 137 TYR   B O    1 
ATOM   4694 C CB   . TYR   B 1 137 ? -34.522 23.580  -44.335 1.00 47.34  ? 137 TYR   B CB   1 
ATOM   4695 C CG   . TYR   B 1 137 ? -34.561 25.084  -44.482 1.00 50.61  ? 137 TYR   B CG   1 
ATOM   4696 C CD1  . TYR   B 1 137 ? -34.267 25.702  -45.700 1.00 51.63  ? 137 TYR   B CD1  1 
ATOM   4697 C CD2  . TYR   B 1 137 ? -34.887 25.891  -43.402 1.00 47.52  ? 137 TYR   B CD2  1 
ATOM   4698 C CE1  . TYR   B 1 137 ? -34.301 27.091  -45.826 1.00 53.58  ? 137 TYR   B CE1  1 
ATOM   4699 C CE2  . TYR   B 1 137 ? -34.918 27.267  -43.514 1.00 51.91  ? 137 TYR   B CE2  1 
ATOM   4700 C CZ   . TYR   B 1 137 ? -34.628 27.865  -44.725 1.00 55.49  ? 137 TYR   B CZ   1 
ATOM   4701 O OH   . TYR   B 1 137 ? -34.670 29.238  -44.808 1.00 52.95  ? 137 TYR   B OH   1 
ATOM   4702 N N    . GLN   B 1 138 ? -35.192 20.643  -45.541 1.00 49.94  ? 138 GLN   B N    1 
ATOM   4703 C CA   . GLN   B 1 138 ? -34.868 19.227  -45.429 1.00 51.50  ? 138 GLN   B CA   1 
ATOM   4704 C C    . GLN   B 1 138 ? -33.437 19.036  -45.906 1.00 51.04  ? 138 GLN   B C    1 
ATOM   4705 O O    . GLN   B 1 138 ? -33.064 19.562  -46.962 1.00 49.13  ? 138 GLN   B O    1 
ATOM   4706 C CB   . GLN   B 1 138 ? -35.840 18.360  -46.246 1.00 51.00  ? 138 GLN   B CB   1 
ATOM   4707 C CG   . GLN   B 1 138 ? -37.253 18.934  -46.348 1.00 52.88  ? 138 GLN   B CG   1 
ATOM   4708 C CD   . GLN   B 1 138 ? -38.297 17.871  -46.645 1.00 55.61  ? 138 GLN   B CD   1 
ATOM   4709 O OE1  . GLN   B 1 138 ? -39.406 17.900  -46.101 1.00 56.76  ? 138 GLN   B OE1  1 
ATOM   4710 N NE2  . GLN   B 1 138 ? -37.944 16.917  -47.504 1.00 56.41  ? 138 GLN   B NE2  1 
ATOM   4711 N N    . TYR   B 1 139 ? -32.621 18.346  -45.103 1.00 44.68  ? 139 TYR   B N    1 
ATOM   4712 C CA   . TYR   B 1 139 ? -31.194 18.199  -45.362 1.00 42.76  ? 139 TYR   B CA   1 
ATOM   4713 C C    . TYR   B 1 139 ? -30.772 16.735  -45.321 1.00 44.59  ? 139 TYR   B C    1 
ATOM   4714 O O    . TYR   B 1 139 ? -31.339 15.939  -44.565 1.00 46.28  ? 139 TYR   B O    1 
ATOM   4715 C CB   . TYR   B 1 139 ? -30.354 19.002  -44.362 1.00 43.27  ? 139 TYR   B CB   1 
ATOM   4716 C CG   . TYR   B 1 139 ? -30.593 20.497  -44.380 1.00 45.27  ? 139 TYR   B CG   1 
ATOM   4717 C CD1  . TYR   B 1 139 ? -30.263 21.264  -45.491 1.00 48.72  ? 139 TYR   B CD1  1 
ATOM   4718 C CD2  . TYR   B 1 139 ? -31.132 21.145  -43.276 1.00 47.80  ? 139 TYR   B CD2  1 
ATOM   4719 C CE1  . TYR   B 1 139 ? -30.461 22.633  -45.496 1.00 49.70  ? 139 TYR   B CE1  1 
ATOM   4720 C CE2  . TYR   B 1 139 ? -31.340 22.515  -43.271 1.00 46.01  ? 139 TYR   B CE2  1 
ATOM   4721 C CZ   . TYR   B 1 139 ? -31.004 23.251  -44.385 1.00 49.87  ? 139 TYR   B CZ   1 
ATOM   4722 O OH   . TYR   B 1 139 ? -31.212 24.612  -44.399 1.00 50.13  ? 139 TYR   B OH   1 
ATOM   4723 N N    . ASN   B 1 140 ? -29.804 16.395  -46.179 1.00 46.92  ? 140 ASN   B N    1 
ATOM   4724 C CA   . ASN   B 1 140 ? -29.049 15.137  -46.172 1.00 45.93  ? 140 ASN   B CA   1 
ATOM   4725 C C    . ASN   B 1 140 ? -27.947 15.270  -45.114 1.00 41.60  ? 140 ASN   B C    1 
ATOM   4726 O O    . ASN   B 1 140 ? -27.057 16.121  -45.241 1.00 41.40  ? 140 ASN   B O    1 
ATOM   4727 C CB   . ASN   B 1 140 ? -28.527 14.926  -47.600 1.00 43.19  ? 140 ASN   B CB   1 
ATOM   4728 C CG   . ASN   B 1 140 ? -27.640 13.697  -47.785 1.00 45.90  ? 140 ASN   B CG   1 
ATOM   4729 O OD1  . ASN   B 1 140 ? -26.721 13.440  -47.017 1.00 45.04  ? 140 ASN   B OD1  1 
ATOM   4730 N ND2  . ASN   B 1 140 ? -27.886 12.963  -48.886 1.00 47.21  ? 140 ASN   B ND2  1 
ATOM   4731 N N    . THR   B 1 141 ? -28.013 14.496  -44.029 1.00 38.35  ? 141 THR   B N    1 
ATOM   4732 C CA   . THR   B 1 141 ? -27.326 14.902  -42.797 1.00 34.57  ? 141 THR   B CA   1 
ATOM   4733 C C    . THR   B 1 141 ? -26.452 13.772  -42.266 1.00 35.33  ? 141 THR   B C    1 
ATOM   4734 O O    . THR   B 1 141 ? -26.941 12.673  -41.988 1.00 35.65  ? 141 THR   B O    1 
ATOM   4735 C CB   . THR   B 1 141 ? -28.358 15.360  -41.760 1.00 39.36  ? 141 THR   B CB   1 
ATOM   4736 O OG1  . THR   B 1 141 ? -29.153 16.418  -42.322 1.00 36.59  ? 141 THR   B OG1  1 
ATOM   4737 C CG2  . THR   B 1 141 ? -27.689 15.905  -40.433 1.00 39.08  ? 141 THR   B CG2  1 
ATOM   4738 N N    . ASP   B 1 142 ? -25.162 14.037  -42.133 1.00 41.23  ? 142 ASP   B N    1 
ATOM   4739 C CA   . ASP   B 1 142 ? -24.293 13.154  -41.373 1.00 45.75  ? 142 ASP   B CA   1 
ATOM   4740 C C    . ASP   B 1 142 ? -24.417 13.490  -39.884 1.00 47.69  ? 142 ASP   B C    1 
ATOM   4741 O O    . ASP   B 1 142 ? -24.458 14.664  -39.508 1.00 47.42  ? 142 ASP   B O    1 
ATOM   4742 C CB   . ASP   B 1 142 ? -22.840 13.313  -41.832 1.00 43.42  ? 142 ASP   B CB   1 
ATOM   4743 C CG   . ASP   B 1 142 ? -22.619 12.912  -43.303 1.00 46.54  ? 142 ASP   B CG   1 
ATOM   4744 O OD1  . ASP   B 1 142 ? -23.436 12.162  -43.881 1.00 46.56  ? 142 ASP   B OD1  1 
ATOM   4745 O OD2  . ASP   B 1 142 ? -21.600 13.352  -43.879 1.00 46.70  ? 142 ASP   B OD2  1 
ATOM   4746 N N    . VAL   B 1 143 ? -24.511 12.460  -39.043 1.00 40.87  ? 143 VAL   B N    1 
ATOM   4747 C CA   . VAL   B 1 143 ? -24.455 12.609  -37.592 1.00 42.74  ? 143 VAL   B CA   1 
ATOM   4748 C C    . VAL   B 1 143 ? -23.324 11.735  -37.071 1.00 43.35  ? 143 VAL   B C    1 
ATOM   4749 O O    . VAL   B 1 143 ? -23.091 10.630  -37.583 1.00 42.23  ? 143 VAL   B O    1 
ATOM   4750 C CB   . VAL   B 1 143 ? -25.780 12.243  -36.876 1.00 40.99  ? 143 VAL   B CB   1 
ATOM   4751 C CG1  . VAL   B 1 143 ? -26.904 13.241  -37.208 1.00 43.05  ? 143 VAL   B CG1  1 
ATOM   4752 C CG2  . VAL   B 1 143 ? -26.202 10.821  -37.201 1.00 41.42  ? 143 VAL   B CG2  1 
ATOM   4753 N N    . VAL   B 1 144 ? -22.586 12.268  -36.093 1.00 42.84  ? 144 VAL   B N    1 
ATOM   4754 C CA   . VAL   B 1 144 ? -21.554 11.523  -35.381 1.00 42.53  ? 144 VAL   B CA   1 
ATOM   4755 C C    . VAL   B 1 144 ? -21.884 11.534  -33.896 1.00 46.37  ? 144 VAL   B C    1 
ATOM   4756 O O    . VAL   B 1 144 ? -22.043 12.614  -33.294 1.00 45.81  ? 144 VAL   B O    1 
ATOM   4757 C CB   . VAL   B 1 144 ? -20.144 12.088  -35.607 1.00 44.60  ? 144 VAL   B CB   1 
ATOM   4758 C CG1  . VAL   B 1 144 ? -19.120 11.187  -34.903 1.00 42.81  ? 144 VAL   B CG1  1 
ATOM   4759 C CG2  . VAL   B 1 144 ? -19.848 12.211  -37.108 1.00 41.90  ? 144 VAL   B CG2  1 
ATOM   4760 N N    . PHE   B 1 145 ? -21.900 10.329  -33.309 1.00 44.84  ? 145 PHE   B N    1 
ATOM   4761 C CA   . PHE   B 1 145 ? -22.088 10.105  -31.876 1.00 43.81  ? 145 PHE   B CA   1 
ATOM   4762 C C    . PHE   B 1 145 ? -20.812 9.510   -31.312 1.00 45.88  ? 145 PHE   B C    1 
ATOM   4763 O O    . PHE   B 1 145 ? -20.243 8.580   -31.906 1.00 45.72  ? 145 PHE   B O    1 
ATOM   4764 C CB   . PHE   B 1 145 ? -23.260 9.153   -31.590 1.00 43.83  ? 145 PHE   B CB   1 
ATOM   4765 C CG   . PHE   B 1 145 ? -24.583 9.666   -32.078 1.00 44.85  ? 145 PHE   B CG   1 
ATOM   4766 C CD1  . PHE   B 1 145 ? -25.306 10.586  -31.331 1.00 44.39  ? 145 PHE   B CD1  1 
ATOM   4767 C CD2  . PHE   B 1 145 ? -25.080 9.268   -33.313 1.00 44.45  ? 145 PHE   B CD2  1 
ATOM   4768 C CE1  . PHE   B 1 145 ? -26.516 11.079  -31.780 1.00 44.54  ? 145 PHE   B CE1  1 
ATOM   4769 C CE2  . PHE   B 1 145 ? -26.284 9.767   -33.787 1.00 43.76  ? 145 PHE   B CE2  1 
ATOM   4770 C CZ   . PHE   B 1 145 ? -27.003 10.673  -33.022 1.00 43.69  ? 145 PHE   B CZ   1 
ATOM   4771 N N    . ASP   B 1 146 ? -20.360 10.036  -30.166 1.00 45.11  ? 146 ASP   B N    1 
ATOM   4772 C CA   . ASP   B 1 146 ? -19.116 9.538   -29.605 1.00 45.60  ? 146 ASP   B CA   1 
ATOM   4773 C C    . ASP   B 1 146 ? -19.372 8.230   -28.870 1.00 45.44  ? 146 ASP   B C    1 
ATOM   4774 O O    . ASP   B 1 146 ? -20.496 7.719   -28.816 1.00 46.27  ? 146 ASP   B O    1 
ATOM   4775 C CB   . ASP   B 1 146 ? -18.437 10.609  -28.742 1.00 46.74  ? 146 ASP   B CB   1 
ATOM   4776 C CG   . ASP   B 1 146 ? -19.209 10.967  -27.452 1.00 48.88  ? 146 ASP   B CG   1 
ATOM   4777 O OD1  . ASP   B 1 146 ? -20.100 10.201  -26.998 1.00 50.07  ? 146 ASP   B OD1  1 
ATOM   4778 O OD2  . ASP   B 1 146 ? -18.887 12.052  -26.900 1.00 44.60  ? 146 ASP   B OD2  1 
ATOM   4779 N N    . SER   B 1 147 ? -18.302 7.665   -28.327 1.00 53.57  ? 147 SER   B N    1 
ATOM   4780 C CA   . SER   B 1 147 ? -18.388 6.392   -27.630 1.00 56.86  ? 147 SER   B CA   1 
ATOM   4781 C C    . SER   B 1 147 ? -19.235 6.459   -26.363 1.00 59.16  ? 147 SER   B C    1 
ATOM   4782 O O    . SER   B 1 147 ? -19.492 5.411   -25.760 1.00 61.21  ? 147 SER   B O    1 
ATOM   4783 C CB   . SER   B 1 147 ? -16.987 5.910   -27.277 1.00 58.87  ? 147 SER   B CB   1 
ATOM   4784 O OG   . SER   B 1 147 ? -16.298 6.913   -26.556 1.00 62.22  ? 147 SER   B OG   1 
ATOM   4785 N N    . GLN   B 1 148 ? -19.590 7.649   -25.884 1.00 67.51  ? 148 GLN   B N    1 
ATOM   4786 C CA   . GLN   B 1 148 ? -20.541 7.772   -24.782 1.00 67.38  ? 148 GLN   B CA   1 
ATOM   4787 C C    . GLN   B 1 148 ? -21.979 7.927   -25.257 1.00 67.78  ? 148 GLN   B C    1 
ATOM   4788 O O    . GLN   B 1 148 ? -22.893 7.964   -24.421 1.00 64.91  ? 148 GLN   B O    1 
ATOM   4789 C CB   . GLN   B 1 148 ? -20.180 8.961   -23.887 1.00 63.86  ? 148 GLN   B CB   1 
ATOM   4790 C CG   . GLN   B 1 148 ? -19.136 8.664   -22.810 1.00 76.86  ? 148 GLN   B CG   1 
ATOM   4791 C CD   . GLN   B 1 148 ? -17.769 8.404   -23.407 1.00 79.08  ? 148 GLN   B CD   1 
ATOM   4792 O OE1  . GLN   B 1 148 ? -17.228 9.263   -24.120 1.00 80.21  ? 148 GLN   B OE1  1 
ATOM   4793 N NE2  . GLN   B 1 148 ? -17.172 7.244   -23.080 1.00 76.64  ? 148 GLN   B NE2  1 
ATOM   4794 N N    . GLY   B 1 149 ? -22.194 8.050   -26.569 1.00 46.68  ? 149 GLY   B N    1 
ATOM   4795 C CA   . GLY   B 1 149 ? -23.504 8.297   -27.118 1.00 45.29  ? 149 GLY   B CA   1 
ATOM   4796 C C    . GLY   B 1 149 ? -23.864 9.749   -27.241 1.00 43.66  ? 149 GLY   B C    1 
ATOM   4797 O O    . GLY   B 1 149 ? -25.031 10.059  -27.506 1.00 44.04  ? 149 GLY   B O    1 
ATOM   4798 N N    . LYS   B 1 150 ? -22.914 10.658  -27.066 1.00 50.38  ? 150 LYS   B N    1 
ATOM   4799 C CA   . LYS   B 1 150 ? -23.218 12.072  -27.238 1.00 52.84  ? 150 LYS   B CA   1 
ATOM   4800 C C    . LYS   B 1 150 ? -23.197 12.420  -28.721 1.00 48.96  ? 150 LYS   B C    1 
ATOM   4801 O O    . LYS   B 1 150 ? -22.410 11.858  -29.490 1.00 47.83  ? 150 LYS   B O    1 
ATOM   4802 C CB   . LYS   B 1 150 ? -22.227 12.953  -26.471 1.00 50.77  ? 150 LYS   B CB   1 
ATOM   4803 C CG   . LYS   B 1 150 ? -22.656 14.421  -26.346 1.00 50.19  ? 150 LYS   B CG   1 
ATOM   4804 C CD   . LYS   B 1 150 ? -21.546 15.277  -25.770 1.00 48.51  ? 150 LYS   B CD   1 
ATOM   4805 C CE   . LYS   B 1 150 ? -21.775 15.587  -24.236 1.00 64.48  ? 150 LYS   B CE   1 
ATOM   4806 N NZ   . LYS   B 1 150 ? -21.330 14.604  -23.167 1.00 59.45  ? 150 LYS   B NZ   1 
ATOM   4807 N N    . LEU   B 1 151 ? -24.078 13.342  -29.117 1.00 49.54  ? 151 LEU   B N    1 
ATOM   4808 C CA   . LEU   B 1 151 ? -24.115 13.846  -30.484 1.00 48.69  ? 151 LEU   B CA   1 
ATOM   4809 C C    . LEU   B 1 151 ? -23.020 14.890  -30.633 1.00 48.46  ? 151 LEU   B C    1 
ATOM   4810 O O    . LEU   B 1 151 ? -23.164 16.016  -30.150 1.00 48.47  ? 151 LEU   B O    1 
ATOM   4811 C CB   . LEU   B 1 151 ? -25.481 14.449  -30.800 1.00 47.53  ? 151 LEU   B CB   1 
ATOM   4812 C CG   . LEU   B 1 151 ? -25.492 15.427  -31.986 1.00 48.49  ? 151 LEU   B CG   1 
ATOM   4813 C CD1  . LEU   B 1 151 ? -25.417 14.652  -33.273 1.00 44.33  ? 151 LEU   B CD1  1 
ATOM   4814 C CD2  . LEU   B 1 151 ? -26.716 16.331  -31.993 1.00 46.34  ? 151 LEU   B CD2  1 
ATOM   4815 N N    . VAL   B 1 152 ? -21.953 14.556  -31.356 1.00 44.65  ? 152 VAL   B N    1 
ATOM   4816 C CA   . VAL   B 1 152 ? -20.821 15.470  -31.472 1.00 43.69  ? 152 VAL   B CA   1 
ATOM   4817 C C    . VAL   B 1 152 ? -20.714 16.102  -32.855 1.00 46.02  ? 152 VAL   B C    1 
ATOM   4818 O O    . VAL   B 1 152 ? -19.905 17.031  -33.027 1.00 45.37  ? 152 VAL   B O    1 
ATOM   4819 C CB   . VAL   B 1 152 ? -19.482 14.793  -31.094 1.00 43.46  ? 152 VAL   B CB   1 
ATOM   4820 C CG1  . VAL   B 1 152 ? -19.510 14.277  -29.640 1.00 41.82  ? 152 VAL   B CG1  1 
ATOM   4821 C CG2  . VAL   B 1 152 ? -19.126 13.653  -32.071 1.00 41.12  ? 152 VAL   B CG2  1 
ATOM   4822 N N    . ALA   B 1 153 ? -21.513 15.681  -33.834 1.00 42.79  ? 153 ALA   B N    1 
ATOM   4823 C CA   . ALA   B 1 153 ? -21.373 16.400  -35.103 1.00 43.43  ? 153 ALA   B CA   1 
ATOM   4824 C C    . ALA   B 1 153 ? -22.588 16.192  -35.999 1.00 41.15  ? 153 ALA   B C    1 
ATOM   4825 O O    . ALA   B 1 153 ? -23.154 15.100  -36.039 1.00 42.30  ? 153 ALA   B O    1 
ATOM   4826 C CB   . ALA   B 1 153 ? -20.088 15.986  -35.824 1.00 38.26  ? 153 ALA   B CB   1 
ATOM   4827 N N    . ARG   B 1 154 ? -22.983 17.254  -36.703 1.00 42.48  ? 154 ARG   B N    1 
ATOM   4828 C CA   . ARG   B 1 154 ? -24.068 17.212  -37.683 1.00 40.80  ? 154 ARG   B CA   1 
ATOM   4829 C C    . ARG   B 1 154 ? -23.656 17.992  -38.925 1.00 42.42  ? 154 ARG   B C    1 
ATOM   4830 O O    . ARG   B 1 154 ? -23.263 19.157  -38.831 1.00 37.79  ? 154 ARG   B O    1 
ATOM   4831 C CB   . ARG   B 1 154 ? -25.349 17.803  -37.075 1.00 44.31  ? 154 ARG   B CB   1 
ATOM   4832 C CG   . ARG   B 1 154 ? -26.590 17.738  -37.946 1.00 43.66  ? 154 ARG   B CG   1 
ATOM   4833 C CD   . ARG   B 1 154 ? -27.624 18.735  -37.474 1.00 41.60  ? 154 ARG   B CD   1 
ATOM   4834 N NE   . ARG   B 1 154 ? -27.222 20.112  -37.755 1.00 43.62  ? 154 ARG   B NE   1 
ATOM   4835 C CZ   . ARG   B 1 154 ? -27.744 21.185  -37.168 1.00 46.59  ? 154 ARG   B CZ   1 
ATOM   4836 N NH1  . ARG   B 1 154 ? -28.697 21.081  -36.245 1.00 44.92  ? 154 ARG   B NH1  1 
ATOM   4837 N NH2  . ARG   B 1 154 ? -27.295 22.391  -37.503 1.00 41.75  ? 154 ARG   B NH2  1 
ATOM   4838 N N    . TYR   B 1 155 ? -23.726 17.358  -40.098 1.00 42.84  ? 155 TYR   B N    1 
ATOM   4839 C CA   . TYR   B 1 155 ? -23.308 18.031  -41.321 1.00 41.04  ? 155 TYR   B CA   1 
ATOM   4840 C C    . TYR   B 1 155 ? -24.403 17.928  -42.371 1.00 42.32  ? 155 TYR   B C    1 
ATOM   4841 O O    . TYR   B 1 155 ? -24.849 16.823  -42.704 1.00 40.90  ? 155 TYR   B O    1 
ATOM   4842 C CB   . TYR   B 1 155 ? -21.991 17.465  -41.875 1.00 41.34  ? 155 TYR   B CB   1 
ATOM   4843 C CG   . TYR   B 1 155 ? -21.737 17.885  -43.323 1.00 42.57  ? 155 TYR   B CG   1 
ATOM   4844 C CD1  . TYR   B 1 155 ? -21.441 19.207  -43.645 1.00 42.76  ? 155 TYR   B CD1  1 
ATOM   4845 C CD2  . TYR   B 1 155 ? -21.823 16.964  -44.364 1.00 43.25  ? 155 TYR   B CD2  1 
ATOM   4846 C CE1  . TYR   B 1 155 ? -21.226 19.593  -44.973 1.00 45.10  ? 155 TYR   B CE1  1 
ATOM   4847 C CE2  . TYR   B 1 155 ? -21.605 17.333  -45.675 1.00 42.26  ? 155 TYR   B CE2  1 
ATOM   4848 C CZ   . TYR   B 1 155 ? -21.311 18.653  -45.980 1.00 44.48  ? 155 TYR   B CZ   1 
ATOM   4849 O OH   . TYR   B 1 155 ? -21.101 19.041  -47.291 1.00 43.89  ? 155 TYR   B OH   1 
ATOM   4850 N N    . HIS   B 1 156 ? -24.819 19.082  -42.894 1.00 42.99  ? 156 HIS   B N    1 
ATOM   4851 C CA   . HIS   B 1 156 ? -25.786 19.147  -43.984 1.00 45.82  ? 156 HIS   B CA   1 
ATOM   4852 C C    . HIS   B 1 156 ? -25.043 19.167  -45.313 1.00 45.77  ? 156 HIS   B C    1 
ATOM   4853 O O    . HIS   B 1 156 ? -24.248 20.080  -45.573 1.00 46.38  ? 156 HIS   B O    1 
ATOM   4854 C CB   . HIS   B 1 156 ? -26.660 20.387  -43.857 1.00 46.24  ? 156 HIS   B CB   1 
ATOM   4855 C CG   . HIS   B 1 156 ? -27.516 20.398  -42.632 1.00 47.26  ? 156 HIS   B CG   1 
ATOM   4856 N ND1  . HIS   B 1 156 ? -27.706 21.532  -41.871 1.00 45.98  ? 156 HIS   B ND1  1 
ATOM   4857 C CD2  . HIS   B 1 156 ? -28.241 19.417  -42.041 1.00 45.70  ? 156 HIS   B CD2  1 
ATOM   4858 C CE1  . HIS   B 1 156 ? -28.508 21.244  -40.859 1.00 49.28  ? 156 HIS   B CE1  1 
ATOM   4859 N NE2  . HIS   B 1 156 ? -28.848 19.969  -40.939 1.00 46.63  ? 156 HIS   B NE2  1 
ATOM   4860 N N    . LYS   B 1 157 ? -25.324 18.177  -46.161 1.00 45.63  ? 157 LYS   B N    1 
ATOM   4861 C CA   . LYS   B 1 157 ? -24.615 18.028  -47.430 1.00 45.77  ? 157 LYS   B CA   1 
ATOM   4862 C C    . LYS   B 1 157 ? -24.729 19.298  -48.270 1.00 47.59  ? 157 LYS   B C    1 
ATOM   4863 O O    . LYS   B 1 157 ? -25.836 19.760  -48.577 1.00 47.82  ? 157 LYS   B O    1 
ATOM   4864 C CB   . LYS   B 1 157 ? -25.171 16.827  -48.199 1.00 44.03  ? 157 LYS   B CB   1 
ATOM   4865 C CG   . LYS   B 1 157 ? -24.391 16.477  -49.450 1.00 44.05  ? 157 LYS   B CG   1 
ATOM   4866 C CD   . LYS   B 1 157 ? -25.025 15.280  -50.164 1.00 46.57  ? 157 LYS   B CD   1 
ATOM   4867 C CE   . LYS   B 1 157 ? -24.319 14.934  -51.479 1.00 44.74  ? 157 LYS   B CE   1 
ATOM   4868 N NZ   . LYS   B 1 157 ? -24.844 13.639  -52.014 1.00 45.82  ? 157 LYS   B NZ   1 
ATOM   4869 N N    . GLN   B 1 158 ? -23.575 19.846  -48.665 1.00 41.67  ? 158 GLN   B N    1 
ATOM   4870 C CA   . GLN   B 1 158 ? -23.559 21.100  -49.411 1.00 44.68  ? 158 GLN   B CA   1 
ATOM   4871 C C    . GLN   B 1 158 ? -23.801 20.891  -50.906 1.00 47.54  ? 158 GLN   B C    1 
ATOM   4872 O O    . GLN   B 1 158 ? -24.592 21.618  -51.521 1.00 47.31  ? 158 GLN   B O    1 
ATOM   4873 C CB   . GLN   B 1 158 ? -22.220 21.816  -49.209 1.00 45.70  ? 158 GLN   B CB   1 
ATOM   4874 C CG   . GLN   B 1 158 ? -22.101 23.112  -50.015 1.00 45.87  ? 158 GLN   B CG   1 
ATOM   4875 C CD   . GLN   B 1 158 ? -22.896 24.259  -49.382 1.00 52.80  ? 158 GLN   B CD   1 
ATOM   4876 O OE1  . GLN   B 1 158 ? -23.438 24.133  -48.269 1.00 50.21  ? 158 GLN   B OE1  1 
ATOM   4877 N NE2  . GLN   B 1 158 ? -22.977 25.379  -50.092 1.00 52.46  ? 158 GLN   B NE2  1 
ATOM   4878 N N    . ASN   B 1 159 ? -23.141 19.910  -51.504 1.00 45.18  ? 159 ASN   B N    1 
ATOM   4879 C CA   . ASN   B 1 159 ? -23.141 19.731  -52.949 1.00 43.59  ? 159 ASN   B CA   1 
ATOM   4880 C C    . ASN   B 1 159 ? -24.049 18.548  -53.290 1.00 44.74  ? 159 ASN   B C    1 
ATOM   4881 O O    . ASN   B 1 159 ? -23.607 17.400  -53.342 1.00 43.07  ? 159 ASN   B O    1 
ATOM   4882 C CB   . ASN   B 1 159 ? -21.723 19.522  -53.452 1.00 43.78  ? 159 ASN   B CB   1 
ATOM   4883 C CG   . ASN   B 1 159 ? -20.793 20.675  -53.094 1.00 48.36  ? 159 ASN   B CG   1 
ATOM   4884 O OD1  . ASN   B 1 159 ? -20.615 21.620  -53.878 1.00 55.53  ? 159 ASN   B OD1  1 
ATOM   4885 N ND2  . ASN   B 1 159 ? -20.170 20.590  -51.928 1.00 44.73  ? 159 ASN   B ND2  1 
ATOM   4886 N N    . LEU   B 1 160 ? -25.316 18.848  -53.576 1.00 45.88  ? 160 LEU   B N    1 
ATOM   4887 C CA   . LEU   B 1 160 ? -26.284 17.822  -53.932 1.00 45.03  ? 160 LEU   B CA   1 
ATOM   4888 C C    . LEU   B 1 160 ? -26.045 17.329  -55.358 1.00 49.96  ? 160 LEU   B C    1 
ATOM   4889 O O    . LEU   B 1 160 ? -25.770 18.108  -56.282 1.00 46.28  ? 160 LEU   B O    1 
ATOM   4890 C CB   . LEU   B 1 160 ? -27.706 18.366  -53.792 1.00 44.99  ? 160 LEU   B CB   1 
ATOM   4891 C CG   . LEU   B 1 160 ? -28.057 18.889  -52.392 1.00 47.96  ? 160 LEU   B CG   1 
ATOM   4892 C CD1  . LEU   B 1 160 ? -29.496 19.413  -52.291 1.00 46.47  ? 160 LEU   B CD1  1 
ATOM   4893 C CD2  . LEU   B 1 160 ? -27.812 17.804  -51.376 1.00 46.46  ? 160 LEU   B CD2  1 
ATOM   4894 N N    . PHE   B 1 161 ? -26.114 16.017  -55.526 1.00 58.11  ? 161 PHE   B N    1 
ATOM   4895 C CA   . PHE   B 1 161 ? -26.025 15.397  -56.830 1.00 54.13  ? 161 PHE   B CA   1 
ATOM   4896 C C    . PHE   B 1 161 ? -27.360 15.540  -57.557 1.00 59.55  ? 161 PHE   B C    1 
ATOM   4897 O O    . PHE   B 1 161 ? -28.417 15.715  -56.935 1.00 56.67  ? 161 PHE   B O    1 
ATOM   4898 C CB   . PHE   B 1 161 ? -25.655 13.924  -56.666 1.00 54.43  ? 161 PHE   B CB   1 
ATOM   4899 C CG   . PHE   B 1 161 ? -25.141 13.270  -57.912 1.00 60.05  ? 161 PHE   B CG   1 
ATOM   4900 C CD1  . PHE   B 1 161 ? -23.990 13.734  -58.542 1.00 58.60  ? 161 PHE   B CD1  1 
ATOM   4901 C CD2  . PHE   B 1 161 ? -25.816 12.187  -58.468 1.00 60.70  ? 161 PHE   B CD2  1 
ATOM   4902 C CE1  . PHE   B 1 161 ? -23.515 13.117  -59.680 1.00 56.77  ? 161 PHE   B CE1  1 
ATOM   4903 C CE2  . PHE   B 1 161 ? -25.343 11.572  -59.616 1.00 60.70  ? 161 PHE   B CE2  1 
ATOM   4904 C CZ   . PHE   B 1 161 ? -24.193 12.036  -60.216 1.00 60.13  ? 161 PHE   B CZ   1 
ATOM   4905 N N    . MET   B 1 162 ? -27.307 15.445  -58.889 1.00 61.03  ? 162 MET   B N    1 
ATOM   4906 C CA   . MET   B 1 162 ? -28.543 15.443  -59.661 1.00 62.38  ? 162 MET   B CA   1 
ATOM   4907 C C    . MET   B 1 162 ? -29.449 14.342  -59.128 1.00 63.60  ? 162 MET   B C    1 
ATOM   4908 O O    . MET   B 1 162 ? -28.978 13.302  -58.653 1.00 62.28  ? 162 MET   B O    1 
ATOM   4909 C CB   . MET   B 1 162 ? -28.260 15.252  -61.158 1.00 64.45  ? 162 MET   B CB   1 
ATOM   4910 C CG   . MET   B 1 162 ? -28.475 13.838  -61.697 1.00 69.07  ? 162 MET   B CG   1 
ATOM   4911 S SD   . MET   B 1 162 ? -28.270 13.682  -63.509 1.00 77.34  ? 162 MET   B SD   1 
ATOM   4912 C CE   . MET   B 1 162 ? -29.458 14.875  -64.176 1.00 71.54  ? 162 MET   B CE   1 
ATOM   4913 N N    . GLY   B 1 163 ? -30.750 14.616  -59.113 1.00 57.55  ? 163 GLY   B N    1 
ATOM   4914 C CA   . GLY   B 1 163 ? -31.687 13.692  -58.509 1.00 55.75  ? 163 GLY   B CA   1 
ATOM   4915 C C    . GLY   B 1 163 ? -31.819 13.758  -56.991 1.00 57.44  ? 163 GLY   B C    1 
ATOM   4916 O O    . GLY   B 1 163 ? -32.490 12.895  -56.419 1.00 56.13  ? 163 GLY   B O    1 
ATOM   4917 N N    . GLU   B 1 164 ? -31.168 14.692  -56.303 1.00 56.07  ? 164 GLU   B N    1 
ATOM   4918 C CA   . GLU   B 1 164 ? -31.440 14.846  -54.861 1.00 58.96  ? 164 GLU   B CA   1 
ATOM   4919 C C    . GLU   B 1 164 ? -32.388 16.009  -54.584 1.00 60.37  ? 164 GLU   B C    1 
ATOM   4920 O O    . GLU   B 1 164 ? -32.146 16.815  -53.680 1.00 56.44  ? 164 GLU   B O    1 
ATOM   4921 C CB   . GLU   B 1 164 ? -30.143 15.017  -54.080 1.00 54.86  ? 164 GLU   B CB   1 
ATOM   4922 C CG   . GLU   B 1 164 ? -29.203 13.846  -54.187 1.00 54.43  ? 164 GLU   B CG   1 
ATOM   4923 C CD   . GLU   B 1 164 ? -28.084 13.898  -53.176 1.00 55.78  ? 164 GLU   B CD   1 
ATOM   4924 O OE1  . GLU   B 1 164 ? -28.248 13.328  -52.078 1.00 56.17  ? 164 GLU   B OE1  1 
ATOM   4925 O OE2  . GLU   B 1 164 ? -27.044 14.530  -53.478 1.00 55.74  ? 164 GLU   B OE2  1 
ATOM   4926 N N    . ASN   B 1 165 ? -33.495 16.086  -55.328 1.00 67.97  ? 165 ASN   B N    1 
ATOM   4927 C CA   . ASN   B 1 165 ? -34.395 17.229  -55.247 1.00 70.89  ? 165 ASN   B CA   1 
ATOM   4928 C C    . ASN   B 1 165 ? -35.272 17.253  -53.987 1.00 71.08  ? 165 ASN   B C    1 
ATOM   4929 O O    . ASN   B 1 165 ? -35.964 18.250  -53.765 1.00 71.46  ? 165 ASN   B O    1 
ATOM   4930 C CB   . ASN   B 1 165 ? -35.238 17.309  -56.540 1.00 75.17  ? 165 ASN   B CB   1 
ATOM   4931 C CG   . ASN   B 1 165 ? -36.532 16.513  -56.461 1.00 81.47  ? 165 ASN   B CG   1 
ATOM   4932 O OD1  . ASN   B 1 165 ? -36.532 15.273  -56.442 1.00 79.38  ? 165 ASN   B OD1  1 
ATOM   4933 N ND2  . ASN   B 1 165 ? -37.650 17.229  -56.408 1.00 86.73  ? 165 ASN   B ND2  1 
ATOM   4934 N N    . GLN   B 1 166 ? -35.271 16.194  -53.164 1.00 56.29  ? 166 GLN   B N    1 
ATOM   4935 C CA   . GLN   B 1 166 ? -35.972 16.174  -51.872 1.00 55.03  ? 166 GLN   B CA   1 
ATOM   4936 C C    . GLN   B 1 166 ? -35.267 16.990  -50.785 1.00 52.47  ? 166 GLN   B C    1 
ATOM   4937 O O    . GLN   B 1 166 ? -35.857 17.229  -49.727 1.00 51.36  ? 166 GLN   B O    1 
ATOM   4938 C CB   . GLN   B 1 166 ? -36.145 14.728  -51.381 1.00 54.36  ? 166 GLN   B CB   1 
ATOM   4939 C CG   . GLN   B 1 166 ? -34.834 13.967  -51.036 1.00 51.91  ? 166 GLN   B CG   1 
ATOM   4940 C CD   . GLN   B 1 166 ? -34.254 13.227  -52.266 1.00 55.52  ? 166 GLN   B CD   1 
ATOM   4941 O OE1  . GLN   B 1 166 ? -34.274 13.750  -53.390 1.00 53.28  ? 166 GLN   B OE1  1 
ATOM   4942 N NE2  . GLN   B 1 166 ? -33.746 12.012  -52.052 1.00 52.79  ? 166 GLN   B NE2  1 
ATOM   4943 N N    . PHE   B 1 167 ? -34.034 17.423  -51.032 1.00 53.60  ? 167 PHE   B N    1 
ATOM   4944 C CA   . PHE   B 1 167 ? -33.172 18.102  -50.083 1.00 48.59  ? 167 PHE   B CA   1 
ATOM   4945 C C    . PHE   B 1 167 ? -32.951 19.555  -50.488 1.00 51.44  ? 167 PHE   B C    1 
ATOM   4946 O O    . PHE   B 1 167 ? -32.937 19.907  -51.672 1.00 53.48  ? 167 PHE   B O    1 
ATOM   4947 C CB   . PHE   B 1 167 ? -31.818 17.395  -50.020 1.00 46.47  ? 167 PHE   B CB   1 
ATOM   4948 C CG   . PHE   B 1 167 ? -31.881 16.041  -49.425 1.00 48.40  ? 167 PHE   B CG   1 
ATOM   4949 C CD1  . PHE   B 1 167 ? -32.488 15.850  -48.193 1.00 47.64  ? 167 PHE   B CD1  1 
ATOM   4950 C CD2  . PHE   B 1 167 ? -31.304 14.957  -50.071 1.00 48.20  ? 167 PHE   B CD2  1 
ATOM   4951 C CE1  . PHE   B 1 167 ? -32.548 14.604  -47.622 1.00 50.08  ? 167 PHE   B CE1  1 
ATOM   4952 C CE2  . PHE   B 1 167 ? -31.369 13.687  -49.510 1.00 48.96  ? 167 PHE   B CE2  1 
ATOM   4953 C CZ   . PHE   B 1 167 ? -31.992 13.520  -48.268 1.00 51.11  ? 167 PHE   B CZ   1 
ATOM   4954 N N    . ASN   B 1 168 ? -32.673 20.375  -49.485 1.00 51.43  ? 168 ASN   B N    1 
ATOM   4955 C CA   . ASN   B 1 168 ? -32.282 21.759  -49.657 1.00 51.33  ? 168 ASN   B CA   1 
ATOM   4956 C C    . ASN   B 1 168 ? -30.772 21.880  -49.492 1.00 52.98  ? 168 ASN   B C    1 
ATOM   4957 O O    . ASN   B 1 168 ? -30.098 20.983  -48.980 1.00 52.35  ? 168 ASN   B O    1 
ATOM   4958 C CB   . ASN   B 1 168 ? -32.983 22.667  -48.637 1.00 53.49  ? 168 ASN   B CB   1 
ATOM   4959 C CG   . ASN   B 1 168 ? -34.478 22.754  -48.858 1.00 54.88  ? 168 ASN   B CG   1 
ATOM   4960 O OD1  . ASN   B 1 168 ? -35.267 22.185  -48.107 1.00 56.14  ? 168 ASN   B OD1  1 
ATOM   4961 N ND2  . ASN   B 1 168 ? -34.875 23.465  -49.891 1.00 54.11  ? 168 ASN   B ND2  1 
ATOM   4962 N N    . VAL   B 1 169 ? -30.251 23.008  -49.944 1.00 54.32  ? 169 VAL   B N    1 
ATOM   4963 C CA   . VAL   B 1 169 ? -28.834 23.338  -49.835 1.00 53.04  ? 169 VAL   B CA   1 
ATOM   4964 C C    . VAL   B 1 169 ? -28.670 24.296  -48.659 1.00 51.76  ? 169 VAL   B C    1 
ATOM   4965 O O    . VAL   B 1 169 ? -29.513 25.184  -48.484 1.00 51.72  ? 169 VAL   B O    1 
ATOM   4966 C CB   . VAL   B 1 169 ? -28.321 23.964  -51.146 1.00 52.57  ? 169 VAL   B CB   1 
ATOM   4967 C CG1  . VAL   B 1 169 ? -26.843 24.242  -51.085 1.00 54.17  ? 169 VAL   B CG1  1 
ATOM   4968 C CG2  . VAL   B 1 169 ? -28.606 23.035  -52.293 1.00 49.39  ? 169 VAL   B CG2  1 
ATOM   4969 N N    . PRO   B 1 170 ? -27.683 24.100  -47.787 1.00 56.46  ? 170 PRO   B N    1 
ATOM   4970 C CA   . PRO   B 1 170 ? -27.451 25.089  -46.723 1.00 56.47  ? 170 PRO   B CA   1 
ATOM   4971 C C    . PRO   B 1 170 ? -27.115 26.441  -47.331 1.00 58.70  ? 170 PRO   B C    1 
ATOM   4972 O O    . PRO   B 1 170 ? -26.502 26.522  -48.401 1.00 59.24  ? 170 PRO   B O    1 
ATOM   4973 C CB   . PRO   B 1 170 ? -26.264 24.512  -45.943 1.00 51.75  ? 170 PRO   B CB   1 
ATOM   4974 C CG   . PRO   B 1 170 ? -26.313 23.044  -46.212 1.00 52.58  ? 170 PRO   B CG   1 
ATOM   4975 C CD   . PRO   B 1 170 ? -26.834 22.907  -47.633 1.00 54.96  ? 170 PRO   B CD   1 
ATOM   4976 N N    . LYS   B 1 171 ? -27.550 27.510  -46.653 1.00 62.48  ? 171 LYS   B N    1 
ATOM   4977 C CA   . LYS   B 1 171 ? -27.235 28.867  -47.097 1.00 63.95  ? 171 LYS   B CA   1 
ATOM   4978 C C    . LYS   B 1 171 ? -25.739 29.074  -47.266 1.00 64.95  ? 171 LYS   B C    1 
ATOM   4979 O O    . LYS   B 1 171 ? -25.301 29.769  -48.193 1.00 67.56  ? 171 LYS   B O    1 
ATOM   4980 C CB   . LYS   B 1 171 ? -27.784 29.897  -46.113 1.00 66.55  ? 171 LYS   B CB   1 
ATOM   4981 C CG   . LYS   B 1 171 ? -28.993 30.659  -46.620 1.00 74.66  ? 171 LYS   B CG   1 
ATOM   4982 C CD   . LYS   B 1 171 ? -30.263 29.872  -46.320 1.00 77.59  ? 171 LYS   B CD   1 
ATOM   4983 C CE   . LYS   B 1 171 ? -30.837 30.255  -44.958 1.00 71.78  ? 171 LYS   B CE   1 
ATOM   4984 N NZ   . LYS   B 1 171 ? -32.245 29.803  -44.807 1.00 73.72  ? 171 LYS   B NZ   1 
ATOM   4985 N N    . GLU   B 1 172 ? -24.943 28.502  -46.371 1.00 65.59  ? 172 GLU   B N    1 
ATOM   4986 C CA   . GLU   B 1 172 ? -23.493 28.571  -46.445 1.00 68.70  ? 172 GLU   B CA   1 
ATOM   4987 C C    . GLU   B 1 172 ? -22.920 27.187  -46.190 1.00 66.06  ? 172 GLU   B C    1 
ATOM   4988 O O    . GLU   B 1 172 ? -23.516 26.395  -45.450 1.00 65.07  ? 172 GLU   B O    1 
ATOM   4989 C CB   . GLU   B 1 172 ? -22.915 29.560  -45.422 1.00 65.21  ? 172 GLU   B CB   1 
ATOM   4990 C CG   . GLU   B 1 172 ? -21.940 30.550  -46.003 1.00 68.89  ? 172 GLU   B CG   1 
ATOM   4991 C CD   . GLU   B 1 172 ? -22.616 31.524  -46.964 1.00 78.30  ? 172 GLU   B CD   1 
ATOM   4992 O OE1  . GLU   B 1 172 ? -22.271 31.520  -48.176 1.00 80.05  ? 172 GLU   B OE1  1 
ATOM   4993 O OE2  . GLU   B 1 172 ? -23.502 32.284  -46.501 1.00 76.20  ? 172 GLU   B OE2  1 
ATOM   4994 N N    . PRO   B 1 173 ? -21.773 26.864  -46.791 1.00 54.82  ? 173 PRO   B N    1 
ATOM   4995 C CA   . PRO   B 1 173 ? -21.127 25.577  -46.493 1.00 52.95  ? 173 PRO   B CA   1 
ATOM   4996 C C    . PRO   B 1 173 ? -20.815 25.424  -45.004 1.00 52.14  ? 173 PRO   B C    1 
ATOM   4997 O O    . PRO   B 1 173 ? -20.279 26.329  -44.358 1.00 49.65  ? 173 PRO   B O    1 
ATOM   4998 C CB   . PRO   B 1 173 ? -19.844 25.626  -47.329 1.00 50.77  ? 173 PRO   B CB   1 
ATOM   4999 C CG   . PRO   B 1 173 ? -20.177 26.550  -48.469 1.00 54.67  ? 173 PRO   B CG   1 
ATOM   5000 C CD   . PRO   B 1 173 ? -21.098 27.587  -47.884 1.00 56.07  ? 173 PRO   B CD   1 
ATOM   5001 N N    . GLU   B 1 174 ? -21.085 24.229  -44.487 1.00 46.00  ? 174 GLU   B N    1 
ATOM   5002 C CA   . GLU   B 1 174 ? -20.924 23.917  -43.072 1.00 42.83  ? 174 GLU   B CA   1 
ATOM   5003 C C    . GLU   B 1 174 ? -19.611 23.160  -42.889 1.00 44.06  ? 174 GLU   B C    1 
ATOM   5004 O O    . GLU   B 1 174 ? -19.475 22.013  -43.338 1.00 45.33  ? 174 GLU   B O    1 
ATOM   5005 C CB   . GLU   B 1 174 ? -22.121 23.110  -42.578 1.00 39.65  ? 174 GLU   B CB   1 
ATOM   5006 C CG   . GLU   B 1 174 ? -23.446 23.825  -42.835 1.00 41.79  ? 174 GLU   B CG   1 
ATOM   5007 C CD   . GLU   B 1 174 ? -24.674 23.000  -42.449 1.00 45.37  ? 174 GLU   B CD   1 
ATOM   5008 O OE1  . GLU   B 1 174 ? -24.505 21.826  -42.046 1.00 43.81  ? 174 GLU   B OE1  1 
ATOM   5009 O OE2  . GLU   B 1 174 ? -25.811 23.536  -42.554 1.00 47.12  ? 174 GLU   B OE2  1 
ATOM   5010 N N    . ILE   B 1 175 ? -18.645 23.809  -42.236 1.00 42.76  ? 175 ILE   B N    1 
ATOM   5011 C CA   . ILE   B 1 175 ? -17.356 23.208  -41.907 1.00 42.23  ? 175 ILE   B CA   1 
ATOM   5012 C C    . ILE   B 1 175 ? -17.509 22.563  -40.534 1.00 45.51  ? 175 ILE   B C    1 
ATOM   5013 O O    . ILE   B 1 175 ? -17.514 23.248  -39.507 1.00 44.79  ? 175 ILE   B O    1 
ATOM   5014 C CB   . ILE   B 1 175 ? -16.232 24.242  -41.912 1.00 44.54  ? 175 ILE   B CB   1 
ATOM   5015 C CG1  . ILE   B 1 175 ? -16.473 25.278  -43.005 1.00 45.29  ? 175 ILE   B CG1  1 
ATOM   5016 C CG2  . ILE   B 1 175 ? -14.879 23.550  -42.048 1.00 45.25  ? 175 ILE   B CG2  1 
ATOM   5017 C CD1  . ILE   B 1 175 ? -16.520 24.675  -44.388 1.00 45.75  ? 175 ILE   B CD1  1 
ATOM   5018 N N    . VAL   B 1 176 ? -17.621 21.240  -40.519 1.00 46.36  ? 176 VAL   B N    1 
ATOM   5019 C CA   . VAL   B 1 176 ? -17.994 20.478  -39.338 1.00 47.58  ? 176 VAL   B CA   1 
ATOM   5020 C C    . VAL   B 1 176 ? -16.831 19.563  -38.974 1.00 49.04  ? 176 VAL   B C    1 
ATOM   5021 O O    . VAL   B 1 176 ? -16.356 18.791  -39.814 1.00 49.38  ? 176 VAL   B O    1 
ATOM   5022 C CB   . VAL   B 1 176 ? -19.280 19.672  -39.603 1.00 48.07  ? 176 VAL   B CB   1 
ATOM   5023 C CG1  . VAL   B 1 176 ? -19.585 18.730  -38.454 1.00 41.75  ? 176 VAL   B CG1  1 
ATOM   5024 C CG2  . VAL   B 1 176 ? -20.450 20.620  -39.905 1.00 43.82  ? 176 VAL   B CG2  1 
ATOM   5025 N N    . THR   B 1 177 ? -16.363 19.658  -37.732 1.00 50.15  ? 177 THR   B N    1 
ATOM   5026 C CA   . THR   B 1 177 ? -15.292 18.799  -37.258 1.00 49.93  ? 177 THR   B CA   1 
ATOM   5027 C C    . THR   B 1 177 ? -15.660 18.235  -35.896 1.00 52.75  ? 177 THR   B C    1 
ATOM   5028 O O    . THR   B 1 177 ? -16.585 18.708  -35.228 1.00 51.25  ? 177 THR   B O    1 
ATOM   5029 C CB   . THR   B 1 177 ? -13.961 19.549  -37.161 1.00 50.67  ? 177 THR   B CB   1 
ATOM   5030 O OG1  . THR   B 1 177 ? -14.072 20.566  -36.163 1.00 52.62  ? 177 THR   B OG1  1 
ATOM   5031 C CG2  . THR   B 1 177 ? -13.599 20.198  -38.494 1.00 50.75  ? 177 THR   B CG2  1 
ATOM   5032 N N    . PHE   B 1 178 ? -14.927 17.203  -35.495 1.00 50.32  ? 178 PHE   B N    1 
ATOM   5033 C CA   . PHE   B 1 178 ? -15.022 16.724  -34.125 1.00 49.50  ? 178 PHE   B CA   1 
ATOM   5034 C C    . PHE   B 1 178 ? -13.653 16.228  -33.681 1.00 54.07  ? 178 PHE   B C    1 
ATOM   5035 O O    . PHE   B 1 178 ? -12.876 15.725  -34.495 1.00 51.92  ? 178 PHE   B O    1 
ATOM   5036 C CB   . PHE   B 1 178 ? -16.100 15.638  -33.955 1.00 51.08  ? 178 PHE   B CB   1 
ATOM   5037 C CG   . PHE   B 1 178 ? -15.945 14.453  -34.868 1.00 51.79  ? 178 PHE   B CG   1 
ATOM   5038 C CD1  . PHE   B 1 178 ? -16.521 14.451  -36.135 1.00 48.90  ? 178 PHE   B CD1  1 
ATOM   5039 C CD2  . PHE   B 1 178 ? -15.244 13.325  -34.452 1.00 51.30  ? 178 PHE   B CD2  1 
ATOM   5040 C CE1  . PHE   B 1 178 ? -16.384 13.362  -36.971 1.00 46.46  ? 178 PHE   B CE1  1 
ATOM   5041 C CE2  . PHE   B 1 178 ? -15.103 12.233  -35.286 1.00 51.94  ? 178 PHE   B CE2  1 
ATOM   5042 C CZ   . PHE   B 1 178 ? -15.680 12.255  -36.557 1.00 48.63  ? 178 PHE   B CZ   1 
ATOM   5043 N N    . ASN   B 1 179 ? -13.346 16.428  -32.393 1.00 59.06  ? 179 ASN   B N    1 
ATOM   5044 C CA   . ASN   B 1 179 ? -12.053 16.094  -31.808 1.00 59.10  ? 179 ASN   B CA   1 
ATOM   5045 C C    . ASN   B 1 179 ? -12.157 14.847  -30.928 1.00 61.22  ? 179 ASN   B C    1 
ATOM   5046 O O    . ASN   B 1 179 ? -13.174 14.613  -30.269 1.00 58.36  ? 179 ASN   B O    1 
ATOM   5047 C CB   . ASN   B 1 179 ? -11.506 17.271  -30.991 1.00 57.59  ? 179 ASN   B CB   1 
ATOM   5048 C CG   . ASN   B 1 179 ? -9.993  17.430  -31.140 1.00 67.32  ? 179 ASN   B CG   1 
ATOM   5049 O OD1  . ASN   B 1 179 ? -9.322  16.561  -31.737 1.00 61.60  ? 179 ASN   B OD1  1 
ATOM   5050 N ND2  . ASN   B 1 179 ? -9.433  18.501  -30.542 1.00 66.03  ? 179 ASN   B ND2  1 
ATOM   5051 N N    . THR   B 1 180 ? -11.081 14.055  -30.911 1.00 53.77  ? 180 THR   B N    1 
ATOM   5052 C CA   . THR   B 1 180 ? -11.055 12.789  -30.194 1.00 51.68  ? 180 THR   B CA   1 
ATOM   5053 C C    . THR   B 1 180 ? -9.646  12.553  -29.694 1.00 52.11  ? 180 THR   B C    1 
ATOM   5054 O O    . THR   B 1 180 ? -8.684  13.165  -30.173 1.00 54.45  ? 180 THR   B O    1 
ATOM   5055 C CB   . THR   B 1 180 ? -11.485 11.605  -31.110 1.00 58.19  ? 180 THR   B CB   1 
ATOM   5056 O OG1  . THR   B 1 180 ? -10.377 11.157  -31.908 1.00 55.98  ? 180 THR   B OG1  1 
ATOM   5057 C CG2  . THR   B 1 180 ? -12.635 11.993  -32.054 1.00 49.28  ? 180 THR   B CG2  1 
ATOM   5058 N N    . THR   B 1 181 ? -9.525  11.629  -28.743 1.00 51.16  ? 181 THR   B N    1 
ATOM   5059 C CA   . THR   B 1 181 ? -8.195  11.261  -28.297 1.00 53.99  ? 181 THR   B CA   1 
ATOM   5060 C C    . THR   B 1 181 ? -7.392  10.592  -29.405 1.00 56.38  ? 181 THR   B C    1 
ATOM   5061 O O    . THR   B 1 181 ? -6.166  10.465  -29.284 1.00 57.10  ? 181 THR   B O    1 
ATOM   5062 C CB   . THR   B 1 181 ? -8.283  10.378  -27.045 1.00 57.20  ? 181 THR   B CB   1 
ATOM   5063 O OG1  . THR   B 1 181 ? -8.807  9.090   -27.391 1.00 58.38  ? 181 THR   B OG1  1 
ATOM   5064 C CG2  . THR   B 1 181 ? -9.185  11.054  -25.967 1.00 56.60  ? 181 THR   B CG2  1 
ATOM   5065 N N    . PHE   B 1 182 ? -8.035  10.188  -30.497 1.00 57.36  ? 182 PHE   B N    1 
ATOM   5066 C CA   . PHE   B 1 182 ? -7.304  9.606   -31.613 1.00 58.86  ? 182 PHE   B CA   1 
ATOM   5067 C C    . PHE   B 1 182 ? -7.385  10.489  -32.852 1.00 59.29  ? 182 PHE   B C    1 
ATOM   5068 O O    . PHE   B 1 182 ? -7.388  9.991   -33.981 1.00 59.78  ? 182 PHE   B O    1 
ATOM   5069 C CB   . PHE   B 1 182 ? -7.802  8.192   -31.906 1.00 57.12  ? 182 PHE   B CB   1 
ATOM   5070 C CG   . PHE   B 1 182 ? -9.301  8.083   -32.007 1.00 60.20  ? 182 PHE   B CG   1 
ATOM   5071 C CD1  . PHE   B 1 182 ? -10.086 7.964   -30.862 1.00 54.31  ? 182 PHE   B CD1  1 
ATOM   5072 C CD2  . PHE   B 1 182 ? -9.932  8.088   -33.261 1.00 55.86  ? 182 PHE   B CD2  1 
ATOM   5073 C CE1  . PHE   B 1 182 ? -11.471 7.854   -30.952 1.00 54.01  ? 182 PHE   B CE1  1 
ATOM   5074 C CE2  . PHE   B 1 182 ? -11.319 7.976   -33.363 1.00 52.84  ? 182 PHE   B CE2  1 
ATOM   5075 C CZ   . PHE   B 1 182 ? -12.089 7.856   -32.215 1.00 53.36  ? 182 PHE   B CZ   1 
ATOM   5076 N N    . GLY   B 1 183 ? -7.446  11.799  -32.660 1.00 60.49  ? 183 GLY   B N    1 
ATOM   5077 C CA   . GLY   B 1 183 ? -7.227  12.719  -33.756 1.00 54.79  ? 183 GLY   B CA   1 
ATOM   5078 C C    . GLY   B 1 183 ? -8.412  13.640  -33.971 1.00 55.85  ? 183 GLY   B C    1 
ATOM   5079 O O    . GLY   B 1 183 ? -9.476  13.501  -33.364 1.00 55.73  ? 183 GLY   B O    1 
ATOM   5080 N N    . SER   B 1 184 ? -8.180  14.614  -34.848 1.00 54.22  ? 184 SER   B N    1 
ATOM   5081 C CA   . SER   B 1 184 ? -9.184  15.574  -35.277 1.00 51.33  ? 184 SER   B CA   1 
ATOM   5082 C C    . SER   B 1 184 ? -9.798  15.107  -36.591 1.00 52.56  ? 184 SER   B C    1 
ATOM   5083 O O    . SER   B 1 184 ? -9.069  14.696  -37.499 1.00 52.41  ? 184 SER   B O    1 
ATOM   5084 C CB   . SER   B 1 184 ? -8.553  16.951  -35.440 1.00 51.25  ? 184 SER   B CB   1 
ATOM   5085 O OG   . SER   B 1 184 ? -9.522  17.880  -35.882 1.00 55.93  ? 184 SER   B OG   1 
ATOM   5086 N N    . PHE   B 1 185 ? -11.133 15.117  -36.671 1.00 49.48  ? 185 PHE   B N    1 
ATOM   5087 C CA   . PHE   B 1 185 ? -11.881 14.565  -37.794 1.00 49.08  ? 185 PHE   B CA   1 
ATOM   5088 C C    . PHE   B 1 185 ? -12.713 15.636  -38.491 1.00 49.66  ? 185 PHE   B C    1 
ATOM   5089 O O    . PHE   B 1 185 ? -13.304 16.504  -37.839 1.00 46.90  ? 185 PHE   B O    1 
ATOM   5090 C CB   . PHE   B 1 185 ? -12.814 13.441  -37.327 1.00 49.43  ? 185 PHE   B CB   1 
ATOM   5091 C CG   . PHE   B 1 185 ? -12.118 12.127  -37.073 1.00 52.36  ? 185 PHE   B CG   1 
ATOM   5092 C CD1  . PHE   B 1 185 ? -11.266 11.973  -35.983 1.00 50.46  ? 185 PHE   B CD1  1 
ATOM   5093 C CD2  . PHE   B 1 185 ? -12.343 11.036  -37.904 1.00 49.69  ? 185 PHE   B CD2  1 
ATOM   5094 C CE1  . PHE   B 1 185 ? -10.628 10.767  -35.745 1.00 52.02  ? 185 PHE   B CE1  1 
ATOM   5095 C CE2  . PHE   B 1 185 ? -11.710 9.821   -37.662 1.00 51.19  ? 185 PHE   B CE2  1 
ATOM   5096 C CZ   . PHE   B 1 185 ? -10.844 9.693   -36.577 1.00 55.37  ? 185 PHE   B CZ   1 
ATOM   5097 N N    . GLY   B 1 186 ? -12.760 15.565  -39.816 1.00 51.03  ? 186 GLY   B N    1 
ATOM   5098 C CA   . GLY   B 1 186 ? -13.711 16.346  -40.585 1.00 50.06  ? 186 GLY   B CA   1 
ATOM   5099 C C    . GLY   B 1 186 ? -14.691 15.434  -41.297 1.00 47.76  ? 186 GLY   B C    1 
ATOM   5100 O O    . GLY   B 1 186 ? -14.393 14.252  -41.494 1.00 49.16  ? 186 GLY   B O    1 
ATOM   5101 N N    . ILE   B 1 187 ? -15.853 15.938  -41.698 1.00 42.06  ? 187 ILE   B N    1 
ATOM   5102 C CA   . ILE   B 1 187 ? -16.870 15.085  -42.306 1.00 44.03  ? 187 ILE   B CA   1 
ATOM   5103 C C    . ILE   B 1 187 ? -17.472 15.778  -43.526 1.00 44.53  ? 187 ILE   B C    1 
ATOM   5104 O O    . ILE   B 1 187 ? -17.667 17.000  -43.520 1.00 40.24  ? 187 ILE   B O    1 
ATOM   5105 C CB   . ILE   B 1 187 ? -17.958 14.730  -41.283 1.00 42.51  ? 187 ILE   B CB   1 
ATOM   5106 C CG1  . ILE   B 1 187 ? -18.962 13.741  -41.875 1.00 43.74  ? 187 ILE   B CG1  1 
ATOM   5107 C CG2  . ILE   B 1 187 ? -18.628 15.992  -40.800 1.00 42.49  ? 187 ILE   B CG2  1 
ATOM   5108 C CD1  . ILE   B 1 187 ? -19.578 12.827  -40.814 1.00 45.86  ? 187 ILE   B CD1  1 
ATOM   5109 N N    . PHE   B 1 188 ? -17.707 15.003  -44.596 1.00 44.34  ? 188 PHE   B N    1 
ATOM   5110 C CA   . PHE   B 1 188 ? -18.528 15.449  -45.724 1.00 43.32  ? 188 PHE   B CA   1 
ATOM   5111 C C    . PHE   B 1 188 ? -19.055 14.219  -46.470 1.00 45.23  ? 188 PHE   B C    1 
ATOM   5112 O O    . PHE   B 1 188 ? -18.667 13.085  -46.181 1.00 46.45  ? 188 PHE   B O    1 
ATOM   5113 C CB   . PHE   B 1 188 ? -17.748 16.415  -46.628 1.00 42.83  ? 188 PHE   B CB   1 
ATOM   5114 C CG   . PHE   B 1 188 ? -16.460 15.854  -47.188 1.00 44.02  ? 188 PHE   B CG   1 
ATOM   5115 C CD1  . PHE   B 1 188 ? -16.482 14.955  -48.257 1.00 45.02  ? 188 PHE   B CD1  1 
ATOM   5116 C CD2  . PHE   B 1 188 ? -15.234 16.289  -46.709 1.00 43.25  ? 188 PHE   B CD2  1 
ATOM   5117 C CE1  . PHE   B 1 188 ? -15.307 14.449  -48.793 1.00 43.48  ? 188 PHE   B CE1  1 
ATOM   5118 C CE2  . PHE   B 1 188 ? -14.052 15.791  -47.233 1.00 45.51  ? 188 PHE   B CE2  1 
ATOM   5119 C CZ   . PHE   B 1 188 ? -14.091 14.868  -48.285 1.00 45.55  ? 188 PHE   B CZ   1 
ATOM   5120 N N    . THR   B 1 189 ? -19.940 14.446  -47.447 1.00 43.52  ? 189 THR   B N    1 
ATOM   5121 C CA   . THR   B 1 189 ? -20.771 13.378  -47.999 1.00 45.27  ? 189 THR   B CA   1 
ATOM   5122 C C    . THR   B 1 189 ? -20.654 13.291  -49.521 1.00 45.69  ? 189 THR   B C    1 
ATOM   5123 O O    . THR   B 1 189 ? -20.959 14.260  -50.224 1.00 45.48  ? 189 THR   B O    1 
ATOM   5124 C CB   . THR   B 1 189 ? -22.231 13.598  -47.601 1.00 42.16  ? 189 THR   B CB   1 
ATOM   5125 O OG1  . THR   B 1 189 ? -22.291 13.897  -46.216 1.00 42.82  ? 189 THR   B OG1  1 
ATOM   5126 C CG2  . THR   B 1 189 ? -23.070 12.346  -47.907 1.00 45.22  ? 189 THR   B CG2  1 
ATOM   5127 N N    . CYS   B 1 190 ? -20.267 12.114  -50.021 1.00 48.80  ? 190 CYS   B N    1 
ATOM   5128 C CA   . CYS   B 1 190 ? -20.295 11.757  -51.444 1.00 49.83  ? 190 CYS   B CA   1 
ATOM   5129 C C    . CYS   B 1 190 ? -19.818 12.866  -52.379 1.00 48.19  ? 190 CYS   B C    1 
ATOM   5130 O O    . CYS   B 1 190 ? -18.617 13.151  -52.451 1.00 48.64  ? 190 CYS   B O    1 
ATOM   5131 C CB   . CYS   B 1 190 ? -21.703 11.312  -51.868 1.00 46.74  ? 190 CYS   B CB   1 
ATOM   5132 S SG   . CYS   B 1 190 ? -21.669 10.031  -53.189 1.00 52.19  ? 190 CYS   B SG   1 
ATOM   5133 N N    . PHE   B 1 191 ? -20.763 13.491  -53.097 1.00 46.66  ? 191 PHE   B N    1 
ATOM   5134 C CA   . PHE   B 1 191 ? -20.428 14.439  -54.166 1.00 43.71  ? 191 PHE   B CA   1 
ATOM   5135 C C    . PHE   B 1 191 ? -19.515 15.557  -53.667 1.00 44.91  ? 191 PHE   B C    1 
ATOM   5136 O O    . PHE   B 1 191 ? -18.737 16.117  -54.458 1.00 41.57  ? 191 PHE   B O    1 
ATOM   5137 C CB   . PHE   B 1 191 ? -21.722 15.014  -54.764 1.00 46.05  ? 191 PHE   B CB   1 
ATOM   5138 C CG   . PHE   B 1 191 ? -21.583 15.537  -56.182 1.00 46.36  ? 191 PHE   B CG   1 
ATOM   5139 C CD1  . PHE   B 1 191 ? -20.578 15.078  -57.020 1.00 50.07  ? 191 PHE   B CD1  1 
ATOM   5140 C CD2  . PHE   B 1 191 ? -22.487 16.476  -56.682 1.00 46.25  ? 191 PHE   B CD2  1 
ATOM   5141 C CE1  . PHE   B 1 191 ? -20.469 15.566  -58.346 1.00 46.31  ? 191 PHE   B CE1  1 
ATOM   5142 C CE2  . PHE   B 1 191 ? -22.382 16.962  -57.958 1.00 44.97  ? 191 PHE   B CE2  1 
ATOM   5143 C CZ   . PHE   B 1 191 ? -21.373 16.504  -58.801 1.00 45.89  ? 191 PHE   B CZ   1 
ATOM   5144 N N    . ASP   B 1 192 ? -19.578 15.878  -52.354 1.00 41.46  ? 192 ASP   B N    1 
ATOM   5145 C CA   . ASP   B 1 192 ? -18.735 16.934  -51.779 1.00 41.30  ? 192 ASP   B CA   1 
ATOM   5146 C C    . ASP   B 1 192 ? -17.270 16.727  -52.134 1.00 39.30  ? 192 ASP   B C    1 
ATOM   5147 O O    . ASP   B 1 192 ? -16.537 17.700  -52.355 1.00 41.00  ? 192 ASP   B O    1 
ATOM   5148 C CB   . ASP   B 1 192 ? -18.871 16.994  -50.242 1.00 41.30  ? 192 ASP   B CB   1 
ATOM   5149 C CG   . ASP   B 1 192 ? -20.238 17.493  -49.770 1.00 42.67  ? 192 ASP   B CG   1 
ATOM   5150 O OD1  . ASP   B 1 192 ? -20.842 18.379  -50.429 1.00 41.02  ? 192 ASP   B OD1  1 
ATOM   5151 O OD2  . ASP   B 1 192 ? -20.706 16.994  -48.718 1.00 40.89  ? 192 ASP   B OD2  1 
ATOM   5152 N N    . ILE   B 1 193 ? -16.832 15.469  -52.236 1.00 39.64  ? 193 ILE   B N    1 
ATOM   5153 C CA   . ILE   B 1 193 ? -15.422 15.188  -52.467 1.00 41.58  ? 193 ILE   B CA   1 
ATOM   5154 C C    . ILE   B 1 193 ? -14.913 15.856  -53.748 1.00 41.41  ? 193 ILE   B C    1 
ATOM   5155 O O    . ILE   B 1 193 ? -13.710 16.123  -53.876 1.00 39.90  ? 193 ILE   B O    1 
ATOM   5156 C CB   . ILE   B 1 193 ? -15.204 13.660  -52.524 1.00 40.72  ? 193 ILE   B CB   1 
ATOM   5157 C CG1  . ILE   B 1 193 ? -13.740 13.289  -52.270 1.00 41.42  ? 193 ILE   B CG1  1 
ATOM   5158 C CG2  . ILE   B 1 193 ? -15.627 13.128  -53.901 1.00 40.45  ? 193 ILE   B CG2  1 
ATOM   5159 C CD1  . ILE   B 1 193 ? -13.544 11.789  -52.063 1.00 40.68  ? 193 ILE   B CD1  1 
ATOM   5160 N N    . LEU   B 1 194 ? -15.802 16.198  -54.677 1.00 42.79  ? 194 LEU   B N    1 
ATOM   5161 C CA   . LEU   B 1 194 ? -15.339 16.814  -55.919 1.00 43.52  ? 194 LEU   B CA   1 
ATOM   5162 C C    . LEU   B 1 194 ? -15.274 18.339  -55.855 1.00 45.52  ? 194 LEU   B C    1 
ATOM   5163 O O    . LEU   B 1 194 ? -14.949 18.966  -56.866 1.00 45.68  ? 194 LEU   B O    1 
ATOM   5164 C CB   . LEU   B 1 194 ? -16.222 16.376  -57.093 1.00 44.28  ? 194 LEU   B CB   1 
ATOM   5165 C CG   . LEU   B 1 194 ? -15.755 15.123  -57.851 1.00 44.50  ? 194 LEU   B CG   1 
ATOM   5166 C CD1  . LEU   B 1 194 ? -16.922 14.528  -58.624 1.00 47.40  ? 194 LEU   B CD1  1 
ATOM   5167 C CD2  . LEU   B 1 194 ? -14.604 15.430  -58.836 1.00 47.11  ? 194 LEU   B CD2  1 
ATOM   5168 N N    . PHE   B 1 195 ? -15.560 18.957  -54.708 1.00 52.38  ? 195 PHE   B N    1 
ATOM   5169 C CA   . PHE   B 1 195 ? -15.643 20.409  -54.639 1.00 50.71  ? 195 PHE   B CA   1 
ATOM   5170 C C    . PHE   B 1 195 ? -14.799 20.952  -53.493 1.00 53.31  ? 195 PHE   B C    1 
ATOM   5171 O O    . PHE   B 1 195 ? -14.264 20.206  -52.661 1.00 52.36  ? 195 PHE   B O    1 
ATOM   5172 C CB   . PHE   B 1 195 ? -17.105 20.851  -54.543 1.00 49.16  ? 195 PHE   B CB   1 
ATOM   5173 C CG   . PHE   B 1 195 ? -17.893 20.483  -55.772 1.00 54.02  ? 195 PHE   B CG   1 
ATOM   5174 C CD1  . PHE   B 1 195 ? -17.766 21.237  -56.934 1.00 52.96  ? 195 PHE   B CD1  1 
ATOM   5175 C CD2  . PHE   B 1 195 ? -18.692 19.349  -55.796 1.00 51.92  ? 195 PHE   B CD2  1 
ATOM   5176 C CE1  . PHE   B 1 195 ? -18.460 20.894  -58.078 1.00 54.47  ? 195 PHE   B CE1  1 
ATOM   5177 C CE2  . PHE   B 1 195 ? -19.381 18.998  -56.938 1.00 51.55  ? 195 PHE   B CE2  1 
ATOM   5178 C CZ   . PHE   B 1 195 ? -19.270 19.772  -58.081 1.00 55.06  ? 195 PHE   B CZ   1 
ATOM   5179 N N    . HIS   B 1 196 ? -14.678 22.282  -53.470 1.00 48.67  ? 196 HIS   B N    1 
ATOM   5180 C CA   . HIS   B 1 196 ? -13.761 22.937  -52.546 1.00 52.19  ? 196 HIS   B CA   1 
ATOM   5181 C C    . HIS   B 1 196 ? -14.325 23.023  -51.135 1.00 51.68  ? 196 HIS   B C    1 
ATOM   5182 O O    . HIS   B 1 196 ? -13.574 22.879  -50.165 1.00 50.98  ? 196 HIS   B O    1 
ATOM   5183 C CB   . HIS   B 1 196 ? -13.426 24.338  -53.043 1.00 52.75  ? 196 HIS   B CB   1 
ATOM   5184 C CG   . HIS   B 1 196 ? -12.320 25.000  -52.279 1.00 54.61  ? 196 HIS   B CG   1 
ATOM   5185 N ND1  . HIS   B 1 196 ? -12.535 25.691  -51.106 1.00 55.60  ? 196 HIS   B ND1  1 
ATOM   5186 C CD2  . HIS   B 1 196 ? -10.989 25.076  -52.523 1.00 53.96  ? 196 HIS   B CD2  1 
ATOM   5187 C CE1  . HIS   B 1 196 ? -11.384 26.164  -50.661 1.00 57.55  ? 196 HIS   B CE1  1 
ATOM   5188 N NE2  . HIS   B 1 196 ? -10.430 25.809  -51.506 1.00 53.23  ? 196 HIS   B NE2  1 
ATOM   5189 N N    . ASP   B 1 197 ? -15.633 23.267  -51.006 1.00 63.07  ? 197 ASP   B N    1 
ATOM   5190 C CA   . ASP   B 1 197 ? -16.286 23.547  -49.736 1.00 61.98  ? 197 ASP   B CA   1 
ATOM   5191 C C    . ASP   B 1 197 ? -17.348 22.501  -49.432 1.00 62.69  ? 197 ASP   B C    1 
ATOM   5192 O O    . ASP   B 1 197 ? -18.231 22.263  -50.270 1.00 63.32  ? 197 ASP   B O    1 
ATOM   5193 C CB   . ASP   B 1 197 ? -16.930 24.931  -49.761 1.00 61.98  ? 197 ASP   B CB   1 
ATOM   5194 C CG   . ASP   B 1 197 ? -15.910 26.034  -49.890 1.00 65.05  ? 197 ASP   B CG   1 
ATOM   5195 O OD1  . ASP   B 1 197 ? -15.141 26.239  -48.922 1.00 71.47  ? 197 ASP   B OD1  1 
ATOM   5196 O OD2  . ASP   B 1 197 ? -15.882 26.700  -50.950 1.00 70.47  ? 197 ASP   B OD2  1 
ATOM   5197 N N    . PRO   B 1 198 ? -17.299 21.848  -48.254 1.00 49.18  ? 198 PRO   B N    1 
ATOM   5198 C CA   . PRO   B 1 198 ? -16.312 22.018  -47.179 1.00 47.06  ? 198 PRO   B CA   1 
ATOM   5199 C C    . PRO   B 1 198 ? -15.039 21.213  -47.388 1.00 47.11  ? 198 PRO   B C    1 
ATOM   5200 O O    . PRO   B 1 198 ? -14.056 21.436  -46.691 1.00 47.82  ? 198 PRO   B O    1 
ATOM   5201 C CB   . PRO   B 1 198 ? -17.067 21.483  -45.960 1.00 46.91  ? 198 PRO   B CB   1 
ATOM   5202 C CG   . PRO   B 1 198 ? -17.863 20.327  -46.535 1.00 47.12  ? 198 PRO   B CG   1 
ATOM   5203 C CD   . PRO   B 1 198 ? -18.287 20.803  -47.914 1.00 46.77  ? 198 PRO   B CD   1 
ATOM   5204 N N    . ALA   B 1 199 ? -15.016 20.306  -48.365 1.00 52.74  ? 199 ALA   B N    1 
ATOM   5205 C CA   . ALA   B 1 199 ? -14.038 19.218  -48.361 1.00 51.01  ? 199 ALA   B CA   1 
ATOM   5206 C C    . ALA   B 1 199 ? -12.604 19.730  -48.295 1.00 51.83  ? 199 ALA   B C    1 
ATOM   5207 O O    . ALA   B 1 199 ? -11.795 19.216  -47.518 1.00 53.57  ? 199 ALA   B O    1 
ATOM   5208 C CB   . ALA   B 1 199 ? -14.236 18.331  -49.591 1.00 48.32  ? 199 ALA   B CB   1 
ATOM   5209 N N    . VAL   B 1 200 ? -12.254 20.713  -49.129 1.00 45.75  ? 200 VAL   B N    1 
ATOM   5210 C CA   . VAL   B 1 200 ? -10.876 21.209  -49.147 1.00 47.10  ? 200 VAL   B CA   1 
ATOM   5211 C C    . VAL   B 1 200 ? -10.632 22.188  -48.002 1.00 49.07  ? 200 VAL   B C    1 
ATOM   5212 O O    . VAL   B 1 200 ? -9.510  22.274  -47.481 1.00 48.93  ? 200 VAL   B O    1 
ATOM   5213 C CB   . VAL   B 1 200 ? -10.525 21.855  -50.506 1.00 49.10  ? 200 VAL   B CB   1 
ATOM   5214 C CG1  . VAL   B 1 200 ? -9.047  22.262  -50.551 1.00 47.42  ? 200 VAL   B CG1  1 
ATOM   5215 C CG2  . VAL   B 1 200 ? -10.834 20.923  -51.648 1.00 45.62  ? 200 VAL   B CG2  1 
ATOM   5216 N N    . THR   B 1 201 ? -11.652 22.961  -47.615 1.00 52.12  ? 201 THR   B N    1 
ATOM   5217 C CA   . THR   B 1 201 ? -11.504 23.866  -46.482 1.00 53.62  ? 201 THR   B CA   1 
ATOM   5218 C C    . THR   B 1 201 ? -11.163 23.093  -45.213 1.00 53.12  ? 201 THR   B C    1 
ATOM   5219 O O    . THR   B 1 201 ? -10.364 23.548  -44.387 1.00 50.51  ? 201 THR   B O    1 
ATOM   5220 C CB   . THR   B 1 201 ? -12.792 24.660  -46.269 1.00 56.56  ? 201 THR   B CB   1 
ATOM   5221 O OG1  . THR   B 1 201 ? -13.036 25.507  -47.397 1.00 55.49  ? 201 THR   B OG1  1 
ATOM   5222 C CG2  . THR   B 1 201 ? -12.690 25.501  -44.968 1.00 55.96  ? 201 THR   B CG2  1 
ATOM   5223 N N    . LEU   B 1 202 ? -11.787 21.928  -45.041 1.00 47.17  ? 202 LEU   B N    1 
ATOM   5224 C CA   . LEU   B 1 202 ? -11.535 21.098  -43.875 1.00 44.95  ? 202 LEU   B CA   1 
ATOM   5225 C C    . LEU   B 1 202 ? -10.050 20.782  -43.732 1.00 48.41  ? 202 LEU   B C    1 
ATOM   5226 O O    . LEU   B 1 202 ? -9.491  20.847  -42.629 1.00 48.23  ? 202 LEU   B O    1 
ATOM   5227 C CB   . LEU   B 1 202 ? -12.350 19.809  -43.988 1.00 44.22  ? 202 LEU   B CB   1 
ATOM   5228 C CG   . LEU   B 1 202 ? -13.820 19.858  -43.576 1.00 43.82  ? 202 LEU   B CG   1 
ATOM   5229 C CD1  . LEU   B 1 202 ? -14.506 18.558  -43.947 1.00 42.54  ? 202 LEU   B CD1  1 
ATOM   5230 C CD2  . LEU   B 1 202 ? -13.914 20.118  -42.058 1.00 43.54  ? 202 LEU   B CD2  1 
ATOM   5231 N N    . VAL   B 1 203 ? -9.396  20.405  -44.830 1.00 53.46  ? 203 VAL   B N    1 
ATOM   5232 C CA   . VAL   B 1 203 ? -7.991  20.019  -44.741 1.00 54.59  ? 203 VAL   B CA   1 
ATOM   5233 C C    . VAL   B 1 203 ? -7.093  21.246  -44.691 1.00 54.84  ? 203 VAL   B C    1 
ATOM   5234 O O    . VAL   B 1 203 ? -6.254  21.383  -43.792 1.00 58.10  ? 203 VAL   B O    1 
ATOM   5235 C CB   . VAL   B 1 203 ? -7.627  19.086  -45.910 1.00 52.93  ? 203 VAL   B CB   1 
ATOM   5236 C CG1  . VAL   B 1 203 ? -6.174  18.628  -45.800 1.00 51.34  ? 203 VAL   B CG1  1 
ATOM   5237 C CG2  . VAL   B 1 203 ? -8.548  17.905  -45.893 1.00 48.90  ? 203 VAL   B CG2  1 
ATOM   5238 N N    . LYS   B 1 204 ? -7.283  22.167  -45.642 1.00 61.02  ? 204 LYS   B N    1 
ATOM   5239 C CA   . LYS   B 1 204 ? -6.406  23.326  -45.785 1.00 60.05  ? 204 LYS   B CA   1 
ATOM   5240 C C    . LYS   B 1 204 ? -6.480  24.249  -44.572 1.00 64.63  ? 204 LYS   B C    1 
ATOM   5241 O O    . LYS   B 1 204 ? -5.444  24.653  -44.030 1.00 68.36  ? 204 LYS   B O    1 
ATOM   5242 C CB   . LYS   B 1 204 ? -6.768  24.084  -47.066 1.00 61.99  ? 204 LYS   B CB   1 
ATOM   5243 C CG   . LYS   B 1 204 ? -5.805  25.196  -47.469 1.00 69.11  ? 204 LYS   B CG   1 
ATOM   5244 C CD   . LYS   B 1 204 ? -6.536  26.538  -47.614 1.00 70.77  ? 204 LYS   B CD   1 
ATOM   5245 C CE   . LYS   B 1 204 ? -7.584  26.478  -48.730 1.00 66.04  ? 204 LYS   B CE   1 
ATOM   5246 N NZ   . LYS   B 1 204 ? -8.458  27.690  -48.775 1.00 67.84  ? 204 LYS   B NZ   1 
ATOM   5247 N N    . ASP   B 1 205 ? -7.692  24.605  -44.130 1.00 69.93  ? 205 ASP   B N    1 
ATOM   5248 C CA   . ASP   B 1 205 ? -7.842  25.602  -43.069 1.00 70.92  ? 205 ASP   B CA   1 
ATOM   5249 C C    . ASP   B 1 205 ? -7.871  24.998  -41.671 1.00 70.77  ? 205 ASP   B C    1 
ATOM   5250 O O    . ASP   B 1 205 ? -7.344  25.603  -40.731 1.00 70.17  ? 205 ASP   B O    1 
ATOM   5251 C CB   . ASP   B 1 205 ? -9.120  26.423  -43.267 1.00 72.39  ? 205 ASP   B CB   1 
ATOM   5252 C CG   . ASP   B 1 205 ? -9.067  27.319  -44.496 1.00 76.23  ? 205 ASP   B CG   1 
ATOM   5253 O OD1  . ASP   B 1 205 ? -7.994  27.412  -45.135 1.00 81.14  ? 205 ASP   B OD1  1 
ATOM   5254 O OD2  . ASP   B 1 205 ? -10.108 27.935  -44.820 1.00 73.47  ? 205 ASP   B OD2  1 
ATOM   5255 N N    . PHE   B 1 206 ? -8.507  23.838  -41.500 1.00 61.03  ? 206 PHE   B N    1 
ATOM   5256 C CA   . PHE   B 1 206 ? -8.708  23.276  -40.172 1.00 60.10  ? 206 PHE   B CA   1 
ATOM   5257 C C    . PHE   B 1 206 ? -7.776  22.109  -39.851 1.00 61.85  ? 206 PHE   B C    1 
ATOM   5258 O O    . PHE   B 1 206 ? -7.734  21.669  -38.693 1.00 62.52  ? 206 PHE   B O    1 
ATOM   5259 C CB   . PHE   B 1 206 ? -10.188 22.873  -40.010 1.00 58.88  ? 206 PHE   B CB   1 
ATOM   5260 C CG   . PHE   B 1 206 ? -11.131 24.060  -39.982 1.00 60.78  ? 206 PHE   B CG   1 
ATOM   5261 C CD1  . PHE   B 1 206 ? -11.375 24.799  -41.131 1.00 61.05  ? 206 PHE   B CD1  1 
ATOM   5262 C CD2  . PHE   B 1 206 ? -11.730 24.468  -38.794 1.00 63.71  ? 206 PHE   B CD2  1 
ATOM   5263 C CE1  . PHE   B 1 206 ? -12.221 25.906  -41.106 1.00 62.15  ? 206 PHE   B CE1  1 
ATOM   5264 C CE2  . PHE   B 1 206 ? -12.576 25.569  -38.756 1.00 64.52  ? 206 PHE   B CE2  1 
ATOM   5265 C CZ   . PHE   B 1 206 ? -12.824 26.293  -39.918 1.00 60.27  ? 206 PHE   B CZ   1 
ATOM   5266 N N    . HIS   B 1 207 ? -6.987  21.646  -40.821 1.00 66.81  ? 207 HIS   B N    1 
ATOM   5267 C CA   . HIS   B 1 207 ? -5.880  20.710  -40.588 1.00 67.40  ? 207 HIS   B CA   1 
ATOM   5268 C C    . HIS   B 1 207 ? -6.338  19.414  -39.925 1.00 65.71  ? 207 HIS   B C    1 
ATOM   5269 O O    . HIS   B 1 207 ? -5.592  18.800  -39.160 1.00 65.86  ? 207 HIS   B O    1 
ATOM   5270 C CB   . HIS   B 1 207 ? -4.759  21.338  -39.753 1.00 69.29  ? 207 HIS   B CB   1 
ATOM   5271 C CG   . HIS   B 1 207 ? -4.418  22.743  -40.135 1.00 73.07  ? 207 HIS   B CG   1 
ATOM   5272 N ND1  . HIS   B 1 207 ? -4.703  23.827  -39.327 1.00 72.65  ? 207 HIS   B ND1  1 
ATOM   5273 C CD2  . HIS   B 1 207 ? -3.824  23.242  -41.244 1.00 68.96  ? 207 HIS   B CD2  1 
ATOM   5274 C CE1  . HIS   B 1 207 ? -4.290  24.932  -39.922 1.00 76.49  ? 207 HIS   B CE1  1 
ATOM   5275 N NE2  . HIS   B 1 207 ? -3.757  24.605  -41.088 1.00 75.53  ? 207 HIS   B NE2  1 
ATOM   5276 N N    . VAL   B 1 208 ? -7.547  18.958  -40.254 1.00 52.30  ? 208 VAL   B N    1 
ATOM   5277 C CA   . VAL   B 1 208 ? -8.009  17.704  -39.680 1.00 52.25  ? 208 VAL   B CA   1 
ATOM   5278 C C    . VAL   B 1 208 ? -7.055  16.589  -40.108 1.00 53.08  ? 208 VAL   B C    1 
ATOM   5279 O O    . VAL   B 1 208 ? -6.424  16.651  -41.173 1.00 54.05  ? 208 VAL   B O    1 
ATOM   5280 C CB   . VAL   B 1 208 ? -9.453  17.376  -40.102 1.00 50.01  ? 208 VAL   B CB   1 
ATOM   5281 C CG1  . VAL   B 1 208 ? -10.368 18.571  -39.877 1.00 47.17  ? 208 VAL   B CG1  1 
ATOM   5282 C CG2  . VAL   B 1 208 ? -9.480  16.949  -41.547 1.00 53.16  ? 208 VAL   B CG2  1 
ATOM   5283 N N    . ASP   B 1 209 ? -6.940  15.566  -39.262 1.00 59.90  ? 209 ASP   B N    1 
ATOM   5284 C CA   . ASP   B 1 209 ? -6.144  14.383  -39.564 1.00 59.16  ? 209 ASP   B CA   1 
ATOM   5285 C C    . ASP   B 1 209 ? -6.896  13.351  -40.387 1.00 58.33  ? 209 ASP   B C    1 
ATOM   5286 O O    . ASP   B 1 209 ? -6.276  12.648  -41.188 1.00 57.78  ? 209 ASP   B O    1 
ATOM   5287 C CB   . ASP   B 1 209 ? -5.679  13.715  -38.269 1.00 61.29  ? 209 ASP   B CB   1 
ATOM   5288 C CG   . ASP   B 1 209 ? -5.017  14.684  -37.325 1.00 63.79  ? 209 ASP   B CG   1 
ATOM   5289 O OD1  . ASP   B 1 209 ? -3.892  15.113  -37.651 1.00 70.49  ? 209 ASP   B OD1  1 
ATOM   5290 O OD2  . ASP   B 1 209 ? -5.602  15.013  -36.261 1.00 66.07  ? 209 ASP   B OD2  1 
ATOM   5291 N N    . THR   B 1 210 ? -8.211  13.240  -40.204 1.00 46.28  ? 210 THR   B N    1 
ATOM   5292 C CA   . THR   B 1 210 ? -8.995  12.159  -40.774 1.00 43.40  ? 210 THR   B CA   1 
ATOM   5293 C C    . THR   B 1 210 ? -10.343 12.699  -41.215 1.00 46.02  ? 210 THR   B C    1 
ATOM   5294 O O    . THR   B 1 210 ? -10.965 13.471  -40.477 1.00 43.96  ? 210 THR   B O    1 
ATOM   5295 C CB   . THR   B 1 210 ? -9.196  11.020  -39.747 1.00 45.00  ? 210 THR   B CB   1 
ATOM   5296 O OG1  . THR   B 1 210 ? -7.927  10.436  -39.416 1.00 44.39  ? 210 THR   B OG1  1 
ATOM   5297 C CG2  . THR   B 1 210 ? -10.118 9.933   -40.286 1.00 43.91  ? 210 THR   B CG2  1 
ATOM   5298 N N    . ILE   B 1 211 ? -10.786 12.292  -42.435 1.00 45.49  ? 211 ILE   B N    1 
ATOM   5299 C CA   . ILE   B 1 211 ? -12.145 12.525  -42.932 1.00 44.90  ? 211 ILE   B CA   1 
ATOM   5300 C C    . ILE   B 1 211 ? -12.938 11.229  -42.795 1.00 45.53  ? 211 ILE   B C    1 
ATOM   5301 O O    . ILE   B 1 211 ? -12.421 10.137  -43.081 1.00 43.99  ? 211 ILE   B O    1 
ATOM   5302 C CB   . ILE   B 1 211 ? -12.186 12.991  -44.406 1.00 45.83  ? 211 ILE   B CB   1 
ATOM   5303 C CG1  . ILE   B 1 211 ? -11.557 14.381  -44.594 1.00 47.88  ? 211 ILE   B CG1  1 
ATOM   5304 C CG2  . ILE   B 1 211 ? -13.634 12.971  -44.925 1.00 40.23  ? 211 ILE   B CG2  1 
ATOM   5305 C CD1  . ILE   B 1 211 ? -12.374 15.547  -44.032 1.00 47.39  ? 211 ILE   B CD1  1 
ATOM   5306 N N    . VAL   B 1 212 ? -14.189 11.345  -42.337 1.00 47.06  ? 212 VAL   B N    1 
ATOM   5307 C CA   . VAL   B 1 212 ? -15.178 10.272  -42.380 1.00 42.66  ? 212 VAL   B CA   1 
ATOM   5308 C C    . VAL   B 1 212 ? -16.163 10.636  -43.483 1.00 48.59  ? 212 VAL   B C    1 
ATOM   5309 O O    . VAL   B 1 212 ? -16.577 11.797  -43.598 1.00 45.97  ? 212 VAL   B O    1 
ATOM   5310 C CB   . VAL   B 1 212 ? -15.888 10.064  -41.021 1.00 47.99  ? 212 VAL   B CB   1 
ATOM   5311 C CG1  . VAL   B 1 212 ? -14.950 9.315   -40.013 1.00 45.97  ? 212 VAL   B CG1  1 
ATOM   5312 C CG2  . VAL   B 1 212 ? -16.353 11.392  -40.403 1.00 45.86  ? 212 VAL   B CG2  1 
ATOM   5313 N N    . PHE   B 1 213 ? -16.534 9.645   -44.301 1.00 52.96  ? 213 PHE   B N    1 
ATOM   5314 C CA   . PHE   B 1 213 ? -17.068 9.883   -45.641 1.00 50.51  ? 213 PHE   B CA   1 
ATOM   5315 C C    . PHE   B 1 213 ? -18.194 8.905   -45.928 1.00 51.43  ? 213 PHE   B C    1 
ATOM   5316 O O    . PHE   B 1 213 ? -17.977 7.828   -46.497 1.00 52.58  ? 213 PHE   B O    1 
ATOM   5317 C CB   . PHE   B 1 213 ? -15.951 9.768   -46.682 1.00 53.13  ? 213 PHE   B CB   1 
ATOM   5318 C CG   . PHE   B 1 213 ? -16.348 10.181  -48.082 1.00 51.22  ? 213 PHE   B CG   1 
ATOM   5319 C CD1  . PHE   B 1 213 ? -16.854 11.453  -48.340 1.00 51.74  ? 213 PHE   B CD1  1 
ATOM   5320 C CD2  . PHE   B 1 213 ? -16.178 9.304   -49.145 1.00 51.63  ? 213 PHE   B CD2  1 
ATOM   5321 C CE1  . PHE   B 1 213 ? -17.205 11.835  -49.629 1.00 48.64  ? 213 PHE   B CE1  1 
ATOM   5322 C CE2  . PHE   B 1 213 ? -16.534 9.681   -50.468 1.00 51.37  ? 213 PHE   B CE2  1 
ATOM   5323 C CZ   . PHE   B 1 213 ? -17.043 10.945  -50.704 1.00 49.37  ? 213 PHE   B CZ   1 
ATOM   5324 N N    . PRO   B 1 214 ? -19.415 9.230   -45.506 1.00 40.81  ? 214 PRO   B N    1 
ATOM   5325 C CA   . PRO   B 1 214 ? -20.589 8.491   -45.998 1.00 41.12  ? 214 PRO   B CA   1 
ATOM   5326 C C    . PRO   B 1 214 ? -20.826 8.793   -47.481 1.00 42.72  ? 214 PRO   B C    1 
ATOM   5327 O O    . PRO   B 1 214 ? -20.790 9.950   -47.910 1.00 40.26  ? 214 PRO   B O    1 
ATOM   5328 C CB   . PRO   B 1 214 ? -21.738 9.010   -45.128 1.00 40.88  ? 214 PRO   B CB   1 
ATOM   5329 C CG   . PRO   B 1 214 ? -21.032 9.595   -43.842 1.00 44.84  ? 214 PRO   B CG   1 
ATOM   5330 C CD   . PRO   B 1 214 ? -19.704 10.101  -44.343 1.00 44.56  ? 214 PRO   B CD   1 
ATOM   5331 N N    . THR   B 1 215 ? -21.066 7.744   -48.271 1.00 42.31  ? 215 THR   B N    1 
ATOM   5332 C CA   . THR   B 1 215 ? -21.187 7.930   -49.719 1.00 44.54  ? 215 THR   B CA   1 
ATOM   5333 C C    . THR   B 1 215 ? -22.130 6.894   -50.309 1.00 43.01  ? 215 THR   B C    1 
ATOM   5334 O O    . THR   B 1 215 ? -22.219 5.772   -49.806 1.00 43.44  ? 215 THR   B O    1 
ATOM   5335 C CB   . THR   B 1 215 ? -19.824 7.846   -50.434 1.00 43.08  ? 215 THR   B CB   1 
ATOM   5336 O OG1  . THR   B 1 215 ? -20.029 7.886   -51.845 1.00 43.47  ? 215 THR   B OG1  1 
ATOM   5337 C CG2  . THR   B 1 215 ? -19.101 6.550   -50.099 1.00 43.65  ? 215 THR   B CG2  1 
ATOM   5338 N N    . ALA   B 1 216 ? -22.852 7.294   -51.388 1.00 42.97  ? 216 ALA   B N    1 
ATOM   5339 C CA   . ALA   B 1 216 ? -23.584 6.372   -52.265 1.00 41.06  ? 216 ALA   B CA   1 
ATOM   5340 C C    . ALA   B 1 216 ? -23.142 6.659   -53.707 1.00 45.24  ? 216 ALA   B C    1 
ATOM   5341 O O    . ALA   B 1 216 ? -23.923 7.112   -54.557 1.00 39.48  ? 216 ALA   B O    1 
ATOM   5342 C CB   . ALA   B 1 216 ? -25.081 6.543   -52.079 1.00 42.82  ? 216 ALA   B CB   1 
ATOM   5343 N N    . TRP   B 1 217 ? -21.959 6.163   -54.033 1.00 45.68  ? 217 TRP   B N    1 
ATOM   5344 C CA   . TRP   B 1 217 ? -21.192 6.599   -55.176 1.00 44.88  ? 217 TRP   B CA   1 
ATOM   5345 C C    . TRP   B 1 217 ? -21.437 5.625   -56.328 1.00 46.08  ? 217 TRP   B C    1 
ATOM   5346 O O    . TRP   B 1 217 ? -21.448 4.403   -56.125 1.00 45.26  ? 217 TRP   B O    1 
ATOM   5347 C CB   . TRP   B 1 217 ? -19.715 6.666   -54.792 1.00 40.74  ? 217 TRP   B CB   1 
ATOM   5348 C CG   . TRP   B 1 217 ? -18.819 7.257   -55.835 1.00 45.00  ? 217 TRP   B CG   1 
ATOM   5349 C CD1  . TRP   B 1 217 ? -18.312 6.620   -56.943 1.00 45.34  ? 217 TRP   B CD1  1 
ATOM   5350 C CD2  . TRP   B 1 217 ? -18.307 8.593   -55.873 1.00 45.90  ? 217 TRP   B CD2  1 
ATOM   5351 N NE1  . TRP   B 1 217 ? -17.499 7.475   -57.647 1.00 45.28  ? 217 TRP   B NE1  1 
ATOM   5352 C CE2  . TRP   B 1 217 ? -17.486 8.693   -57.018 1.00 44.45  ? 217 TRP   B CE2  1 
ATOM   5353 C CE3  . TRP   B 1 217 ? -18.452 9.715   -55.047 1.00 45.47  ? 217 TRP   B CE3  1 
ATOM   5354 C CZ2  . TRP   B 1 217 ? -16.819 9.865   -57.355 1.00 46.02  ? 217 TRP   B CZ2  1 
ATOM   5355 C CZ3  . TRP   B 1 217 ? -17.794 10.883  -55.393 1.00 45.20  ? 217 TRP   B CZ3  1 
ATOM   5356 C CH2  . TRP   B 1 217 ? -16.982 10.947  -56.529 1.00 43.75  ? 217 TRP   B CH2  1 
ATOM   5357 N N    . MET   B 1 218 ? -21.716 6.169   -57.510 1.00 46.07  ? 218 MET   B N    1 
ATOM   5358 C CA   . MET   B 1 218 ? -21.940 5.368   -58.712 1.00 48.74  ? 218 MET   B CA   1 
ATOM   5359 C C    . MET   B 1 218 ? -20.661 5.388   -59.537 1.00 48.14  ? 218 MET   B C    1 
ATOM   5360 O O    . MET   B 1 218 ? -20.296 6.422   -60.107 1.00 48.68  ? 218 MET   B O    1 
ATOM   5361 C CB   . MET   B 1 218 ? -23.136 5.909   -59.489 1.00 45.91  ? 218 MET   B CB   1 
ATOM   5362 C CG   . MET   B 1 218 ? -24.411 5.788   -58.654 1.00 49.99  ? 218 MET   B CG   1 
ATOM   5363 S SD   . MET   B 1 218 ? -25.886 6.251   -59.553 1.00 54.20  ? 218 MET   B SD   1 
ATOM   5364 C CE   . MET   B 1 218 ? -26.066 7.956   -59.065 1.00 60.37  ? 218 MET   B CE   1 
ATOM   5365 N N    . ASN   B 1 219 ? -19.978 4.247   -59.591 1.00 41.18  ? 219 ASN   B N    1 
ATOM   5366 C CA   . ASN   B 1 219 ? -18.659 4.211   -60.206 1.00 41.69  ? 219 ASN   B CA   1 
ATOM   5367 C C    . ASN   B 1 219 ? -18.744 4.581   -61.674 1.00 45.17  ? 219 ASN   B C    1 
ATOM   5368 O O    . ASN   B 1 219 ? -19.614 4.087   -62.401 1.00 42.94  ? 219 ASN   B O    1 
ATOM   5369 C CB   . ASN   B 1 219 ? -18.032 2.826   -60.058 1.00 43.08  ? 219 ASN   B CB   1 
ATOM   5370 C CG   . ASN   B 1 219 ? -17.992 2.356   -58.616 1.00 43.09  ? 219 ASN   B CG   1 
ATOM   5371 O OD1  . ASN   B 1 219 ? -17.582 3.105   -57.712 1.00 44.33  ? 219 ASN   B OD1  1 
ATOM   5372 N ND2  . ASN   B 1 219 ? -18.432 1.118   -58.386 1.00 41.49  ? 219 ASN   B ND2  1 
ATOM   5373 N N    . VAL   B 1 220 ? -17.832 5.460   -62.098 1.00 48.37  ? 220 VAL   B N    1 
ATOM   5374 C CA   . VAL   B 1 220 ? -17.661 5.875   -63.492 1.00 48.76  ? 220 VAL   B CA   1 
ATOM   5375 C C    . VAL   B 1 220 ? -16.180 5.699   -63.817 1.00 48.98  ? 220 VAL   B C    1 
ATOM   5376 O O    . VAL   B 1 220 ? -15.348 6.507   -63.394 1.00 48.93  ? 220 VAL   B O    1 
ATOM   5377 C CB   . VAL   B 1 220 ? -18.104 7.324   -63.748 1.00 48.10  ? 220 VAL   B CB   1 
ATOM   5378 C CG1  . VAL   B 1 220 ? -18.101 7.623   -65.262 1.00 46.07  ? 220 VAL   B CG1  1 
ATOM   5379 C CG2  . VAL   B 1 220 ? -19.469 7.604   -63.143 1.00 44.59  ? 220 VAL   B CG2  1 
ATOM   5380 N N    . LEU   B 1 221 ? -15.837 4.611   -64.494 1.00 49.53  ? 221 LEU   B N    1 
ATOM   5381 C CA   . LEU   B 1 221 ? -14.489 4.432   -65.012 1.00 53.86  ? 221 LEU   B CA   1 
ATOM   5382 C C    . LEU   B 1 221 ? -14.271 5.368   -66.207 1.00 51.28  ? 221 LEU   B C    1 
ATOM   5383 O O    . LEU   B 1 221 ? -15.234 5.809   -66.834 1.00 54.68  ? 221 LEU   B O    1 
ATOM   5384 C CB   . LEU   B 1 221 ? -14.269 2.972   -65.413 1.00 52.59  ? 221 LEU   B CB   1 
ATOM   5385 C CG   . LEU   B 1 221 ? -14.140 2.044   -64.192 1.00 53.24  ? 221 LEU   B CG   1 
ATOM   5386 C CD1  . LEU   B 1 221 ? -14.337 0.564   -64.552 1.00 52.37  ? 221 LEU   B CD1  1 
ATOM   5387 C CD2  . LEU   B 1 221 ? -12.796 2.266   -63.491 1.00 49.41  ? 221 LEU   B CD2  1 
ATOM   5388 N N    . PRO   B 1 222 ? -12.999 5.694   -66.545 1.00 46.00  ? 222 PRO   B N    1 
ATOM   5389 C CA   . PRO   B 1 222 ? -11.744 5.182   -65.962 1.00 49.20  ? 222 PRO   B CA   1 
ATOM   5390 C C    . PRO   B 1 222 ? -11.192 5.966   -64.747 1.00 50.21  ? 222 PRO   B C    1 
ATOM   5391 O O    . PRO   B 1 222 ? -10.205 5.523   -64.134 1.00 49.18  ? 222 PRO   B O    1 
ATOM   5392 C CB   . PRO   B 1 222 ? -10.778 5.284   -67.153 1.00 48.72  ? 222 PRO   B CB   1 
ATOM   5393 C CG   . PRO   B 1 222 ? -11.198 6.583   -67.815 1.00 47.35  ? 222 PRO   B CG   1 
ATOM   5394 C CD   . PRO   B 1 222 ? -12.724 6.593   -67.694 1.00 47.59  ? 222 PRO   B CD   1 
ATOM   5395 N N    . HIS   B 1 223 ? -11.794 7.106   -64.363 1.00 48.10  ? 223 HIS   B N    1 
ATOM   5396 C CA   . HIS   B 1 223 ? -11.240 7.978   -63.331 1.00 45.78  ? 223 HIS   B CA   1 
ATOM   5397 C C    . HIS   B 1 223 ? -12.090 8.118   -62.066 1.00 45.70  ? 223 HIS   B C    1 
ATOM   5398 O O    . HIS   B 1 223 ? -11.581 8.628   -61.058 1.00 43.31  ? 223 HIS   B O    1 
ATOM   5399 C CB   . HIS   B 1 223 ? -11.005 9.388   -63.899 1.00 46.74  ? 223 HIS   B CB   1 
ATOM   5400 C CG   . HIS   B 1 223 ? -10.070 9.438   -65.074 1.00 47.57  ? 223 HIS   B CG   1 
ATOM   5401 N ND1  . HIS   B 1 223 ? -10.194 10.376  -66.076 1.00 45.34  ? 223 HIS   B ND1  1 
ATOM   5402 C CD2  . HIS   B 1 223 ? -8.996  8.677   -65.402 1.00 48.37  ? 223 HIS   B CD2  1 
ATOM   5403 C CE1  . HIS   B 1 223 ? -9.234  10.196  -66.969 1.00 47.70  ? 223 HIS   B CE1  1 
ATOM   5404 N NE2  . HIS   B 1 223 ? -8.495  9.169   -66.584 1.00 49.55  ? 223 HIS   B NE2  1 
ATOM   5405 N N    . LEU   B 1 224 ? -13.374 7.754   -62.094 1.00 46.50  ? 224 LEU   B N    1 
ATOM   5406 C CA   . LEU   B 1 224 ? -14.274 8.054   -60.983 1.00 42.98  ? 224 LEU   B CA   1 
ATOM   5407 C C    . LEU   B 1 224 ? -14.939 6.792   -60.439 1.00 43.02  ? 224 LEU   B C    1 
ATOM   5408 O O    . LEU   B 1 224 ? -16.142 6.762   -60.157 1.00 42.25  ? 224 LEU   B O    1 
ATOM   5409 C CB   . LEU   B 1 224 ? -15.307 9.102   -61.401 1.00 41.53  ? 224 LEU   B CB   1 
ATOM   5410 C CG   . LEU   B 1 224 ? -14.647 10.480  -61.628 1.00 45.99  ? 224 LEU   B CG   1 
ATOM   5411 C CD1  . LEU   B 1 224 ? -15.569 11.523  -62.301 1.00 43.40  ? 224 LEU   B CD1  1 
ATOM   5412 C CD2  . LEU   B 1 224 ? -14.070 11.044  -60.329 1.00 43.01  ? 224 LEU   B CD2  1 
ATOM   5413 N N    . SER   B 1 225 ? -14.172 5.719   -60.304 1.00 41.74  ? 225 SER   B N    1 
ATOM   5414 C CA   . SER   B 1 225 ? -14.595 4.621   -59.454 1.00 44.56  ? 225 SER   B CA   1 
ATOM   5415 C C    . SER   B 1 225 ? -14.381 4.980   -57.969 1.00 43.75  ? 225 SER   B C    1 
ATOM   5416 O O    . SER   B 1 225 ? -13.394 5.637   -57.604 1.00 42.81  ? 225 SER   B O    1 
ATOM   5417 C CB   . SER   B 1 225 ? -13.834 3.360   -59.829 1.00 42.70  ? 225 SER   B CB   1 
ATOM   5418 O OG   . SER   B 1 225 ? -14.521 2.254   -59.301 1.00 45.06  ? 225 SER   B OG   1 
ATOM   5419 N N    . ALA   B 1 226 ? -15.303 4.534   -57.109 1.00 43.67  ? 226 ALA   B N    1 
ATOM   5420 C CA   . ALA   B 1 226 ? -15.300 4.986   -55.711 1.00 43.13  ? 226 ALA   B CA   1 
ATOM   5421 C C    . ALA   B 1 226 ? -13.944 4.764   -55.048 1.00 42.89  ? 226 ALA   B C    1 
ATOM   5422 O O    . ALA   B 1 226 ? -13.274 5.718   -54.637 1.00 44.54  ? 226 ALA   B O    1 
ATOM   5423 C CB   . ALA   B 1 226 ? -16.411 4.284   -54.922 1.00 40.74  ? 226 ALA   B CB   1 
ATOM   5424 N N    . VAL   B 1 227 ? -13.511 3.507   -54.944 1.00 42.24  ? 227 VAL   B N    1 
ATOM   5425 C CA   . VAL   B 1 227 ? -12.259 3.203   -54.251 1.00 41.07  ? 227 VAL   B CA   1 
ATOM   5426 C C    . VAL   B 1 227 ? -11.097 3.969   -54.878 1.00 45.43  ? 227 VAL   B C    1 
ATOM   5427 O O    . VAL   B 1 227 ? -10.256 4.547   -54.168 1.00 45.37  ? 227 VAL   B O    1 
ATOM   5428 C CB   . VAL   B 1 227 ? -12.018 1.684   -54.253 1.00 45.80  ? 227 VAL   B CB   1 
ATOM   5429 C CG1  . VAL   B 1 227 ? -13.046 0.990   -53.354 1.00 43.79  ? 227 VAL   B CG1  1 
ATOM   5430 C CG2  . VAL   B 1 227 ? -12.075 1.108   -55.683 1.00 46.43  ? 227 VAL   B CG2  1 
ATOM   5431 N N    . GLU   B 1 228 ? -11.060 4.014   -56.218 1.00 45.22  ? 228 GLU   B N    1 
ATOM   5432 C CA   . GLU   B 1 228 ? -9.983  4.660   -56.975 1.00 47.17  ? 228 GLU   B CA   1 
ATOM   5433 C C    . GLU   B 1 228 ? -9.844  6.142   -56.620 1.00 42.70  ? 228 GLU   B C    1 
ATOM   5434 O O    . GLU   B 1 228 ? -8.761  6.618   -56.246 1.00 44.33  ? 228 GLU   B O    1 
ATOM   5435 C CB   . GLU   B 1 228 ? -10.258 4.487   -58.481 1.00 45.03  ? 228 GLU   B CB   1 
ATOM   5436 C CG   . GLU   B 1 228 ? -9.392  5.309   -59.423 1.00 44.44  ? 228 GLU   B CG   1 
ATOM   5437 C CD   . GLU   B 1 228 ? -9.931  5.353   -60.864 1.00 50.11  ? 228 GLU   B CD   1 
ATOM   5438 O OE1  . GLU   B 1 228 ? -11.172 5.234   -61.077 1.00 48.30  ? 228 GLU   B OE1  1 
ATOM   5439 O OE2  . GLU   B 1 228 ? -9.093  5.486   -61.783 1.00 49.91  ? 228 GLU   B OE2  1 
ATOM   5440 N N    . PHE   B 1 229 ? -10.933 6.901   -56.773 1.00 43.60  ? 229 PHE   B N    1 
ATOM   5441 C CA   . PHE   B 1 229 ? -10.865 8.337   -56.536 1.00 44.36  ? 229 PHE   B CA   1 
ATOM   5442 C C    . PHE   B 1 229 ? -10.834 8.696   -55.043 1.00 46.12  ? 229 PHE   B C    1 
ATOM   5443 O O    . PHE   B 1 229 ? -10.162 9.664   -54.669 1.00 44.54  ? 229 PHE   B O    1 
ATOM   5444 C CB   . PHE   B 1 229 ? -12.028 9.049   -57.240 1.00 44.51  ? 229 PHE   B CB   1 
ATOM   5445 C CG   . PHE   B 1 229 ? -11.908 10.554  -57.204 1.00 48.90  ? 229 PHE   B CG   1 
ATOM   5446 C CD1  . PHE   B 1 229 ? -11.078 11.223  -58.101 1.00 47.19  ? 229 PHE   B CD1  1 
ATOM   5447 C CD2  . PHE   B 1 229 ? -12.579 11.294  -56.233 1.00 47.11  ? 229 PHE   B CD2  1 
ATOM   5448 C CE1  . PHE   B 1 229 ? -10.946 12.603  -58.043 1.00 45.95  ? 229 PHE   B CE1  1 
ATOM   5449 C CE2  . PHE   B 1 229 ? -12.451 12.668  -56.170 1.00 43.63  ? 229 PHE   B CE2  1 
ATOM   5450 C CZ   . PHE   B 1 229 ? -11.635 13.321  -57.085 1.00 48.21  ? 229 PHE   B CZ   1 
ATOM   5451 N N    . HIS   B 1 230 ? -11.532 7.947   -54.175 1.00 41.29  ? 230 HIS   B N    1 
ATOM   5452 C CA   . HIS   B 1 230 ? -11.509 8.280   -52.742 1.00 41.40  ? 230 HIS   B CA   1 
ATOM   5453 C C    . HIS   B 1 230 ? -10.110 8.068   -52.164 1.00 41.81  ? 230 HIS   B C    1 
ATOM   5454 O O    . HIS   B 1 230 ? -9.562  8.963   -51.507 1.00 41.54  ? 230 HIS   B O    1 
ATOM   5455 C CB   . HIS   B 1 230 ? -12.557 7.460   -51.980 1.00 39.61  ? 230 HIS   B CB   1 
ATOM   5456 C CG   . HIS   B 1 230 ? -13.955 7.615   -52.513 1.00 40.99  ? 230 HIS   B CG   1 
ATOM   5457 N ND1  . HIS   B 1 230 ? -14.954 6.688   -52.269 1.00 38.74  ? 230 HIS   B ND1  1 
ATOM   5458 C CD2  . HIS   B 1 230 ? -14.507 8.570   -53.311 1.00 40.42  ? 230 HIS   B CD2  1 
ATOM   5459 C CE1  . HIS   B 1 230 ? -16.067 7.084   -52.868 1.00 39.67  ? 230 HIS   B CE1  1 
ATOM   5460 N NE2  . HIS   B 1 230 ? -15.823 8.221   -53.508 1.00 39.27  ? 230 HIS   B NE2  1 
ATOM   5461 N N    . SER   B 1 231 ? -9.481  6.916   -52.440 1.00 43.84  ? 231 SER   B N    1 
ATOM   5462 C CA   . SER   B 1 231 ? -8.100  6.747   -51.994 1.00 43.75  ? 231 SER   B CA   1 
ATOM   5463 C C    . SER   B 1 231 ? -7.192  7.802   -52.617 1.00 46.07  ? 231 SER   B C    1 
ATOM   5464 O O    . SER   B 1 231 ? -6.323  8.360   -51.932 1.00 44.31  ? 231 SER   B O    1 
ATOM   5465 C CB   . SER   B 1 231 ? -7.602  5.343   -52.346 1.00 47.88  ? 231 SER   B CB   1 
ATOM   5466 O OG   . SER   B 1 231 ? -7.601  5.122   -53.763 1.00 47.55  ? 231 SER   B OG   1 
ATOM   5467 N N    . ALA   B 1 232 ? -7.375  8.105   -53.919 1.00 45.58  ? 232 ALA   B N    1 
ATOM   5468 C CA   . ALA   B 1 232 ? -6.531  9.136   -54.530 1.00 47.78  ? 232 ALA   B CA   1 
ATOM   5469 C C    . ALA   B 1 232 ? -6.682  10.475  -53.815 1.00 45.41  ? 232 ALA   B C    1 
ATOM   5470 O O    . ALA   B 1 232 ? -5.702  11.207  -53.630 1.00 46.08  ? 232 ALA   B O    1 
ATOM   5471 C CB   . ALA   B 1 232 ? -6.853  9.288   -56.031 1.00 45.58  ? 232 ALA   B CB   1 
ATOM   5472 N N    . TRP   B 1 233 ? -7.910  10.840  -53.456 1.00 48.96  ? 233 TRP   B N    1 
ATOM   5473 C CA   . TRP   B 1 233 ? -8.134  12.096  -52.757 1.00 46.71  ? 233 TRP   B CA   1 
ATOM   5474 C C    . TRP   B 1 233 ? -7.448  12.073  -51.394 1.00 48.48  ? 233 TRP   B C    1 
ATOM   5475 O O    . TRP   B 1 233 ? -6.795  13.046  -50.992 1.00 45.21  ? 233 TRP   B O    1 
ATOM   5476 C CB   . TRP   B 1 233 ? -9.636  12.343  -52.627 1.00 45.01  ? 233 TRP   B CB   1 
ATOM   5477 C CG   . TRP   B 1 233 ? -10.014 13.776  -52.307 1.00 49.25  ? 233 TRP   B CG   1 
ATOM   5478 C CD1  . TRP   B 1 233 ? -10.273 14.775  -53.197 1.00 46.84  ? 233 TRP   B CD1  1 
ATOM   5479 C CD2  . TRP   B 1 233 ? -10.148 14.362  -51.000 1.00 46.01  ? 233 TRP   B CD2  1 
ATOM   5480 N NE1  . TRP   B 1 233 ? -10.590 15.944  -52.532 1.00 45.92  ? 233 TRP   B NE1  1 
ATOM   5481 C CE2  . TRP   B 1 233 ? -10.513 15.720  -51.182 1.00 47.17  ? 233 TRP   B CE2  1 
ATOM   5482 C CE3  . TRP   B 1 233 ? -10.010 13.871  -49.703 1.00 48.31  ? 233 TRP   B CE3  1 
ATOM   5483 C CZ2  . TRP   B 1 233 ? -10.741 16.593  -50.108 1.00 46.89  ? 233 TRP   B CZ2  1 
ATOM   5484 C CZ3  . TRP   B 1 233 ? -10.239 14.748  -48.627 1.00 48.05  ? 233 TRP   B CZ3  1 
ATOM   5485 C CH2  . TRP   B 1 233 ? -10.599 16.093  -48.846 1.00 47.04  ? 233 TRP   B CH2  1 
ATOM   5486 N N    . ALA   B 1 234 ? -7.556  10.950  -50.685 1.00 47.81  ? 234 ALA   B N    1 
ATOM   5487 C CA   . ALA   B 1 234 ? -6.866  10.833  -49.404 1.00 48.48  ? 234 ALA   B CA   1 
ATOM   5488 C C    . ALA   B 1 234 ? -5.373  11.048  -49.586 1.00 52.56  ? 234 ALA   B C    1 
ATOM   5489 O O    . ALA   B 1 234 ? -4.725  11.696  -48.754 1.00 51.72  ? 234 ALA   B O    1 
ATOM   5490 C CB   . ALA   B 1 234 ? -7.125  9.464   -48.780 1.00 45.48  ? 234 ALA   B CB   1 
ATOM   5491 N N    . MET   B 1 235 ? -4.817  10.539  -50.694 1.00 57.91  ? 235 MET   B N    1 
ATOM   5492 C CA   . MET   B 1 235 ? -3.381  10.675  -50.934 1.00 58.88  ? 235 MET   B CA   1 
ATOM   5493 C C    . MET   B 1 235 ? -2.995  12.110  -51.287 1.00 56.29  ? 235 MET   B C    1 
ATOM   5494 O O    . MET   B 1 235 ? -1.983  12.626  -50.804 1.00 57.68  ? 235 MET   B O    1 
ATOM   5495 C CB   . MET   B 1 235 ? -2.941  9.720   -52.035 1.00 57.75  ? 235 MET   B CB   1 
ATOM   5496 C CG   . MET   B 1 235 ? -1.441  9.719   -52.212 1.00 63.81  ? 235 MET   B CG   1 
ATOM   5497 S SD   . MET   B 1 235 ? -0.831  8.228   -53.023 1.00 67.75  ? 235 MET   B SD   1 
ATOM   5498 C CE   . MET   B 1 235 ? -1.479  6.963   -51.930 1.00 65.22  ? 235 MET   B CE   1 
ATOM   5499 N N    . GLY   B 1 236 ? -3.766  12.753  -52.160 1.00 47.71  ? 236 GLY   B N    1 
ATOM   5500 C CA   . GLY   B 1 236 ? -3.448  14.116  -52.558 1.00 45.81  ? 236 GLY   B CA   1 
ATOM   5501 C C    . GLY   B 1 236 ? -3.630  15.116  -51.431 1.00 47.62  ? 236 GLY   B C    1 
ATOM   5502 O O    . GLY   B 1 236 ? -2.840  16.052  -51.287 1.00 45.61  ? 236 GLY   B O    1 
ATOM   5503 N N    . MET   B 1 237 ? -4.702  14.957  -50.647 1.00 57.27  ? 237 MET   B N    1 
ATOM   5504 C CA   . MET   B 1 237 ? -4.971  15.809  -49.497 1.00 56.44  ? 237 MET   B CA   1 
ATOM   5505 C C    . MET   B 1 237 ? -4.119  15.434  -48.290 1.00 58.64  ? 237 MET   B C    1 
ATOM   5506 O O    . MET   B 1 237 ? -3.974  16.247  -47.374 1.00 59.09  ? 237 MET   B O    1 
ATOM   5507 C CB   . MET   B 1 237 ? -6.450  15.715  -49.107 1.00 55.36  ? 237 MET   B CB   1 
ATOM   5508 C CG   . MET   B 1 237 ? -7.412  16.524  -49.956 1.00 53.83  ? 237 MET   B CG   1 
ATOM   5509 S SD   . MET   B 1 237 ? -6.594  17.827  -50.884 1.00 58.62  ? 237 MET   B SD   1 
ATOM   5510 C CE   . MET   B 1 237 ? -6.695  19.203  -49.757 1.00 55.62  ? 237 MET   B CE   1 
ATOM   5511 N N    . ARG   B 1 238 ? -3.563  14.219  -48.266 1.00 53.93  ? 238 ARG   B N    1 
ATOM   5512 C CA   . ARG   B 1 238 ? -2.659  13.779  -47.200 1.00 54.19  ? 238 ARG   B CA   1 
ATOM   5513 C C    . ARG   B 1 238 ? -3.382  13.670  -45.850 1.00 55.14  ? 238 ARG   B C    1 
ATOM   5514 O O    . ARG   B 1 238 ? -2.898  14.150  -44.823 1.00 58.41  ? 238 ARG   B O    1 
ATOM   5515 C CB   . ARG   B 1 238 ? -1.449  14.711  -47.104 1.00 54.36  ? 238 ARG   B CB   1 
ATOM   5516 C CG   . ARG   B 1 238 ? -0.428  14.505  -48.191 1.00 55.35  ? 238 ARG   B CG   1 
ATOM   5517 C CD   . ARG   B 1 238 ? 0.731   15.494  -48.108 1.00 59.47  ? 238 ARG   B CD   1 
ATOM   5518 N NE   . ARG   B 1 238 ? 0.283   16.855  -47.835 1.00 64.48  ? 238 ARG   B NE   1 
ATOM   5519 C CZ   . ARG   B 1 238 ? 0.907   17.713  -47.032 1.00 69.50  ? 238 ARG   B CZ   1 
ATOM   5520 N NH1  . ARG   B 1 238 ? 2.096   17.442  -46.512 1.00 68.89  ? 238 ARG   B NH1  1 
ATOM   5521 N NH2  . ARG   B 1 238 ? 0.347   18.895  -46.786 1.00 64.16  ? 238 ARG   B NH2  1 
ATOM   5522 N N    . VAL   B 1 239 ? -4.532  12.992  -45.845 1.00 58.71  ? 239 VAL   B N    1 
ATOM   5523 C CA   . VAL   B 1 239 ? -5.284  12.733  -44.620 1.00 55.97  ? 239 VAL   B CA   1 
ATOM   5524 C C    . VAL   B 1 239 ? -5.741  11.279  -44.617 1.00 57.68  ? 239 VAL   B C    1 
ATOM   5525 O O    . VAL   B 1 239 ? -5.868  10.642  -45.666 1.00 57.45  ? 239 VAL   B O    1 
ATOM   5526 C CB   . VAL   B 1 239 ? -6.515  13.660  -44.493 1.00 54.77  ? 239 VAL   B CB   1 
ATOM   5527 C CG1  . VAL   B 1 239 ? -6.095  15.109  -44.464 1.00 54.39  ? 239 VAL   B CG1  1 
ATOM   5528 C CG2  . VAL   B 1 239 ? -7.468  13.423  -45.649 1.00 55.64  ? 239 VAL   B CG2  1 
ATOM   5529 N N    . ASN   B 1 240 ? -6.018  10.764  -43.419 1.00 50.14  ? 240 ASN   B N    1 
ATOM   5530 C CA   . ASN   B 1 240 ? -6.760  9.513   -43.311 1.00 49.00  ? 240 ASN   B CA   1 
ATOM   5531 C C    . ASN   B 1 240 ? -8.158  9.692   -43.884 1.00 45.90  ? 240 ASN   B C    1 
ATOM   5532 O O    . ASN   B 1 240 ? -8.707  10.796  -43.901 1.00 46.81  ? 240 ASN   B O    1 
ATOM   5533 C CB   . ASN   B 1 240 ? -6.875  9.073   -41.853 1.00 50.39  ? 240 ASN   B CB   1 
ATOM   5534 C CG   . ASN   B 1 240 ? -5.570  8.575   -41.289 1.00 52.54  ? 240 ASN   B CG   1 
ATOM   5535 O OD1  . ASN   B 1 240 ? -4.703  8.118   -42.034 1.00 51.69  ? 240 ASN   B OD1  1 
ATOM   5536 N ND2  . ASN   B 1 240 ? -5.420  8.653   -39.959 1.00 49.97  ? 240 ASN   B ND2  1 
ATOM   5537 N N    . PHE   B 1 241 ? -8.763  8.581   -44.305 1.00 49.41  ? 241 PHE   B N    1 
ATOM   5538 C CA   . PHE   B 1 241 ? -10.026 8.642   -45.053 1.00 49.37  ? 241 PHE   B CA   1 
ATOM   5539 C C    . PHE   B 1 241 ? -10.810 7.352   -44.852 1.00 49.41  ? 241 PHE   B C    1 
ATOM   5540 O O    . PHE   B 1 241 ? -10.286 6.266   -45.116 1.00 51.75  ? 241 PHE   B O    1 
ATOM   5541 C CB   . PHE   B 1 241 ? -9.763  8.881   -46.550 1.00 47.03  ? 241 PHE   B CB   1 
ATOM   5542 C CG   . PHE   B 1 241 ? -10.908 9.545   -47.280 1.00 45.98  ? 241 PHE   B CG   1 
ATOM   5543 C CD1  . PHE   B 1 241 ? -11.976 8.789   -47.764 1.00 46.36  ? 241 PHE   B CD1  1 
ATOM   5544 C CD2  . PHE   B 1 241 ? -10.898 10.910  -47.529 1.00 45.90  ? 241 PHE   B CD2  1 
ATOM   5545 C CE1  . PHE   B 1 241 ? -13.030 9.387   -48.460 1.00 44.74  ? 241 PHE   B CE1  1 
ATOM   5546 C CE2  . PHE   B 1 241 ? -11.949 11.523  -48.214 1.00 45.22  ? 241 PHE   B CE2  1 
ATOM   5547 C CZ   . PHE   B 1 241 ? -13.019 10.757  -48.681 1.00 45.81  ? 241 PHE   B CZ   1 
ATOM   5548 N N    . LEU   B 1 242 ? -12.056 7.475   -44.381 1.00 42.17  ? 242 LEU   B N    1 
ATOM   5549 C CA   . LEU   B 1 242 ? -12.939 6.341   -44.091 1.00 43.02  ? 242 LEU   B CA   1 
ATOM   5550 C C    . LEU   B 1 242 ? -14.163 6.484   -44.979 1.00 44.07  ? 242 LEU   B C    1 
ATOM   5551 O O    . LEU   B 1 242 ? -15.113 7.188   -44.615 1.00 40.72  ? 242 LEU   B O    1 
ATOM   5552 C CB   . LEU   B 1 242 ? -13.327 6.313   -42.595 1.00 43.84  ? 242 LEU   B CB   1 
ATOM   5553 C CG   . LEU   B 1 242 ? -12.290 5.742   -41.611 1.00 45.73  ? 242 LEU   B CG   1 
ATOM   5554 C CD1  . LEU   B 1 242 ? -10.915 6.272   -41.978 1.00 45.93  ? 242 LEU   B CD1  1 
ATOM   5555 C CD2  . LEU   B 1 242 ? -12.607 6.013   -40.084 1.00 46.13  ? 242 LEU   B CD2  1 
ATOM   5556 N N    . ALA   B 1 243 ? -14.151 5.796   -46.130 1.00 50.39  ? 243 ALA   B N    1 
ATOM   5557 C CA   . ALA   B 1 243 ? -15.215 5.871   -47.127 1.00 45.72  ? 243 ALA   B CA   1 
ATOM   5558 C C    . ALA   B 1 243 ? -16.126 4.668   -46.941 1.00 45.63  ? 243 ALA   B C    1 
ATOM   5559 O O    . ALA   B 1 243 ? -15.677 3.522   -47.065 1.00 46.44  ? 243 ALA   B O    1 
ATOM   5560 C CB   . ALA   B 1 243 ? -14.640 5.879   -48.547 1.00 44.52  ? 243 ALA   B CB   1 
ATOM   5561 N N    . SER   B 1 244 ? -17.395 4.928   -46.636 1.00 41.02  ? 244 SER   B N    1 
ATOM   5562 C CA   . SER   B 1 244 ? -18.386 3.884   -46.391 1.00 43.41  ? 244 SER   B CA   1 
ATOM   5563 C C    . SER   B 1 244 ? -19.495 4.045   -47.420 1.00 43.61  ? 244 SER   B C    1 
ATOM   5564 O O    . SER   B 1 244 ? -20.258 5.017   -47.368 1.00 42.85  ? 244 SER   B O    1 
ATOM   5565 C CB   . SER   B 1 244 ? -18.943 3.964   -44.971 1.00 43.29  ? 244 SER   B CB   1 
ATOM   5566 O OG   . SER   B 1 244 ? -20.213 3.342   -44.940 1.00 45.19  ? 244 SER   B OG   1 
ATOM   5567 N N    . ASN   B 1 245 ? -19.600 3.076   -48.329 1.00 52.88  ? 245 ASN   B N    1 
ATOM   5568 C CA   . ASN   B 1 245 ? -20.377 3.182   -49.553 1.00 49.86  ? 245 ASN   B CA   1 
ATOM   5569 C C    . ASN   B 1 245 ? -21.588 2.257   -49.515 1.00 51.92  ? 245 ASN   B C    1 
ATOM   5570 O O    . ASN   B 1 245 ? -21.573 1.203   -48.868 1.00 54.47  ? 245 ASN   B O    1 
ATOM   5571 C CB   . ASN   B 1 245 ? -19.466 2.830   -50.745 1.00 53.17  ? 245 ASN   B CB   1 
ATOM   5572 C CG   . ASN   B 1 245 ? -20.011 3.253   -52.100 1.00 52.04  ? 245 ASN   B CG   1 
ATOM   5573 O OD1  . ASN   B 1 245 ? -21.175 3.635   -52.275 1.00 52.45  ? 245 ASN   B OD1  1 
ATOM   5574 N ND2  . ASN   B 1 245 ? -19.143 3.173   -53.084 1.00 57.42  ? 245 ASN   B ND2  1 
ATOM   5575 N N    . ILE   B 1 246 ? -22.648 2.667   -50.211 1.00 41.94  ? 246 ILE   B N    1 
ATOM   5576 C CA   . ILE   B 1 246 ? -23.763 1.764   -50.468 1.00 44.51  ? 246 ILE   B CA   1 
ATOM   5577 C C    . ILE   B 1 246 ? -23.311 0.615   -51.368 1.00 44.30  ? 246 ILE   B C    1 
ATOM   5578 O O    . ILE   B 1 246 ? -22.423 0.764   -52.222 1.00 44.38  ? 246 ILE   B O    1 
ATOM   5579 C CB   . ILE   B 1 246 ? -24.951 2.508   -51.104 1.00 44.03  ? 246 ILE   B CB   1 
ATOM   5580 C CG1  . ILE   B 1 246 ? -25.587 3.457   -50.078 1.00 42.49  ? 246 ILE   B CG1  1 
ATOM   5581 C CG2  . ILE   B 1 246 ? -25.927 1.509   -51.736 1.00 40.61  ? 246 ILE   B CG2  1 
ATOM   5582 C CD1  . ILE   B 1 246 ? -26.391 2.754   -48.954 1.00 44.68  ? 246 ILE   B CD1  1 
ATOM   5583 N N    . HIS   B 1 247 ? -23.916 -0.553  -51.155 1.00 44.02  ? 247 HIS   B N    1 
ATOM   5584 C CA   . HIS   B 1 247 ? -23.693 -1.735  -51.972 1.00 45.91  ? 247 HIS   B CA   1 
ATOM   5585 C C    . HIS   B 1 247 ? -24.956 -1.982  -52.775 1.00 47.65  ? 247 HIS   B C    1 
ATOM   5586 O O    . HIS   B 1 247 ? -25.984 -2.400  -52.215 1.00 46.15  ? 247 HIS   B O    1 
ATOM   5587 C CB   . HIS   B 1 247 ? -23.340 -2.961  -51.140 1.00 45.45  ? 247 HIS   B CB   1 
ATOM   5588 C CG   . HIS   B 1 247 ? -23.028 -4.170  -51.969 1.00 48.37  ? 247 HIS   B CG   1 
ATOM   5589 N ND1  . HIS   B 1 247 ? -21.794 -4.375  -52.553 1.00 47.77  ? 247 HIS   B ND1  1 
ATOM   5590 C CD2  . HIS   B 1 247 ? -23.800 -5.223  -52.339 1.00 52.83  ? 247 HIS   B CD2  1 
ATOM   5591 C CE1  . HIS   B 1 247 ? -21.812 -5.519  -53.218 1.00 49.08  ? 247 HIS   B CE1  1 
ATOM   5592 N NE2  . HIS   B 1 247 ? -23.015 -6.054  -53.102 1.00 51.15  ? 247 HIS   B NE2  1 
ATOM   5593 N N    . TYR   B 1 248 ? -24.860 -1.740  -54.090 1.00 50.62  ? 248 TYR   B N    1 
ATOM   5594 C CA   . TYR   B 1 248 ? -25.986 -1.845  -54.986 1.00 50.59  ? 248 TYR   B CA   1 
ATOM   5595 C C    . TYR   B 1 248 ? -25.440 -1.997  -56.403 1.00 53.81  ? 248 TYR   B C    1 
ATOM   5596 O O    . TYR   B 1 248 ? -25.530 -1.063  -57.222 1.00 50.01  ? 248 TYR   B O    1 
ATOM   5597 C CB   . TYR   B 1 248 ? -26.873 -0.613  -54.821 1.00 49.40  ? 248 TYR   B CB   1 
ATOM   5598 C CG   . TYR   B 1 248 ? -28.288 -0.853  -55.220 1.00 50.59  ? 248 TYR   B CG   1 
ATOM   5599 C CD1  . TYR   B 1 248 ? -29.180 -1.463  -54.354 1.00 49.32  ? 248 TYR   B CD1  1 
ATOM   5600 C CD2  . TYR   B 1 248 ? -28.742 -0.468  -56.463 1.00 55.39  ? 248 TYR   B CD2  1 
ATOM   5601 C CE1  . TYR   B 1 248 ? -30.509 -1.699  -54.751 1.00 51.91  ? 248 TYR   B CE1  1 
ATOM   5602 C CE2  . TYR   B 1 248 ? -30.030 -0.684  -56.851 1.00 58.02  ? 248 TYR   B CE2  1 
ATOM   5603 C CZ   . TYR   B 1 248 ? -30.907 -1.295  -56.008 1.00 56.20  ? 248 TYR   B CZ   1 
ATOM   5604 O OH   . TYR   B 1 248 ? -32.190 -1.495  -56.456 1.00 62.29  ? 248 TYR   B OH   1 
ATOM   5605 N N    . PRO   B 1 249 ? -24.883 -3.174  -56.727 1.00 55.10  ? 249 PRO   B N    1 
ATOM   5606 C CA   . PRO   B 1 249 ? -24.224 -3.343  -58.038 1.00 53.03  ? 249 PRO   B CA   1 
ATOM   5607 C C    . PRO   B 1 249 ? -25.108 -2.897  -59.183 1.00 53.75  ? 249 PRO   B C    1 
ATOM   5608 O O    . PRO   B 1 249 ? -24.625 -2.313  -60.158 1.00 51.47  ? 249 PRO   B O    1 
ATOM   5609 C CB   . PRO   B 1 249 ? -23.926 -4.850  -58.084 1.00 54.33  ? 249 PRO   B CB   1 
ATOM   5610 C CG   . PRO   B 1 249 ? -23.854 -5.254  -56.614 1.00 54.89  ? 249 PRO   B CG   1 
ATOM   5611 C CD   . PRO   B 1 249 ? -24.866 -4.405  -55.915 1.00 52.90  ? 249 PRO   B CD   1 
ATOM   5612 N N    . SER   B 1 250 ? -26.404 -3.143  -59.052 1.00 56.58  ? 250 SER   B N    1 
ATOM   5613 C CA   . SER   B 1 250 ? -27.452 -2.696  -59.953 1.00 56.84  ? 250 SER   B CA   1 
ATOM   5614 C C    . SER   B 1 250 ? -27.213 -1.279  -60.460 1.00 56.73  ? 250 SER   B C    1 
ATOM   5615 O O    . SER   B 1 250 ? -27.353 -1.010  -61.662 1.00 57.84  ? 250 SER   B O    1 
ATOM   5616 C CB   . SER   B 1 250 ? -28.783 -2.783  -59.200 1.00 61.06  ? 250 SER   B CB   1 
ATOM   5617 O OG   . SER   B 1 250 ? -29.899 -2.614  -60.038 1.00 61.74  ? 250 SER   B OG   1 
ATOM   5618 N N    . LYS   B 1 251 ? -26.855 -0.370  -59.556 1.00 52.98  ? 251 LYS   B N    1 
ATOM   5619 C CA   . LYS   B 1 251 ? -26.578 1.022   -59.882 1.00 50.77  ? 251 LYS   B CA   1 
ATOM   5620 C C    . LYS   B 1 251 ? -25.090 1.353   -59.856 1.00 51.52  ? 251 LYS   B C    1 
ATOM   5621 O O    . LYS   B 1 251 ? -24.732 2.532   -59.770 1.00 51.31  ? 251 LYS   B O    1 
ATOM   5622 C CB   . LYS   B 1 251 ? -27.335 1.952   -58.926 1.00 52.69  ? 251 LYS   B CB   1 
ATOM   5623 C CG   . LYS   B 1 251 ? -28.855 1.912   -59.077 1.00 53.80  ? 251 LYS   B CG   1 
ATOM   5624 C CD   . LYS   B 1 251 ? -29.497 2.756   -57.996 1.00 57.29  ? 251 LYS   B CD   1 
ATOM   5625 C CE   . LYS   B 1 251 ? -29.380 4.243   -58.311 1.00 58.39  ? 251 LYS   B CE   1 
ATOM   5626 N NZ   . LYS   B 1 251 ? -30.171 4.581   -59.534 1.00 63.22  ? 251 LYS   B NZ   1 
ATOM   5627 N N    . LYS   B 1 252 ? -24.214 0.349   -59.949 1.00 50.56  ? 252 LYS   B N    1 
ATOM   5628 C CA   . LYS   B 1 252 ? -22.766 0.571   -59.892 1.00 48.90  ? 252 LYS   B CA   1 
ATOM   5629 C C    . LYS   B 1 252 ? -22.356 1.226   -58.578 1.00 46.06  ? 252 LYS   B C    1 
ATOM   5630 O O    . LYS   B 1 252 ? -21.413 2.025   -58.534 1.00 44.69  ? 252 LYS   B O    1 
ATOM   5631 C CB   . LYS   B 1 252 ? -22.265 1.416   -61.076 1.00 47.42  ? 252 LYS   B CB   1 
ATOM   5632 C CG   . LYS   B 1 252 ? -22.959 1.147   -62.457 1.00 50.22  ? 252 LYS   B CG   1 
ATOM   5633 C CD   . LYS   B 1 252 ? -22.504 -0.162  -63.043 1.00 49.30  ? 252 LYS   B CD   1 
ATOM   5634 C CE   . LYS   B 1 252 ? -23.494 -0.726  -64.150 1.00 62.23  ? 252 LYS   B CE   1 
ATOM   5635 N NZ   . LYS   B 1 252 ? -24.477 -1.813  -63.726 1.00 58.81  ? 252 LYS   B NZ   1 
ATOM   5636 N N    . MET   B 1 253 ? -23.084 0.901   -57.519 1.00 47.19  ? 253 MET   B N    1 
ATOM   5637 C CA   . MET   B 1 253 ? -22.762 1.365   -56.165 1.00 45.02  ? 253 MET   B CA   1 
ATOM   5638 C C    . MET   B 1 253 ? -22.003 0.250   -55.461 1.00 44.30  ? 253 MET   B C    1 
ATOM   5639 O O    . MET   B 1 253 ? -22.575 -0.769  -55.063 1.00 45.57  ? 253 MET   B O    1 
ATOM   5640 C CB   . MET   B 1 253 ? -24.022 1.791   -55.431 1.00 44.40  ? 253 MET   B CB   1 
ATOM   5641 C CG   . MET   B 1 253 ? -24.421 3.185   -55.807 1.00 47.35  ? 253 MET   B CG   1 
ATOM   5642 S SD   . MET   B 1 253 ? -26.057 3.705   -55.238 1.00 51.56  ? 253 MET   B SD   1 
ATOM   5643 C CE   . MET   B 1 253 ? -26.617 2.276   -54.412 1.00 52.86  ? 253 MET   B CE   1 
ATOM   5644 N N    . THR   B 1 254 ? -20.695 0.431   -55.381 1.00 38.88  ? 254 THR   B N    1 
ATOM   5645 C CA   . THR   B 1 254 ? -19.818 -0.434  -54.621 1.00 39.74  ? 254 THR   B CA   1 
ATOM   5646 C C    . THR   B 1 254 ? -18.425 0.157   -54.641 1.00 43.84  ? 254 THR   B C    1 
ATOM   5647 O O    . THR   B 1 254 ? -17.945 0.615   -55.686 1.00 39.45  ? 254 THR   B O    1 
ATOM   5648 C CB   . THR   B 1 254 ? -19.761 -1.854  -55.154 1.00 41.77  ? 254 THR   B CB   1 
ATOM   5649 O OG1  . THR   B 1 254 ? -18.827 -2.587  -54.364 1.00 42.79  ? 254 THR   B OG1  1 
ATOM   5650 C CG2  . THR   B 1 254 ? -19.268 -1.879  -56.644 1.00 43.33  ? 254 THR   B CG2  1 
ATOM   5651 N N    . GLY   B 1 255 ? -17.732 -0.038  -53.525 1.00 45.52  ? 255 GLY   B N    1 
ATOM   5652 C CA   . GLY   B 1 255 ? -16.413 0.493   -53.240 1.00 45.27  ? 255 GLY   B CA   1 
ATOM   5653 C C    . GLY   B 1 255 ? -16.304 1.289   -51.959 1.00 45.86  ? 255 GLY   B C    1 
ATOM   5654 O O    . GLY   B 1 255 ? -16.618 2.485   -51.872 1.00 43.74  ? 255 GLY   B O    1 
ATOM   5655 N N    . SER   B 1 256 ? -15.753 0.604   -50.963 1.00 48.43  ? 256 SER   B N    1 
ATOM   5656 C CA   . SER   B 1 256 ? -15.581 1.165   -49.633 1.00 48.52  ? 256 SER   B CA   1 
ATOM   5657 C C    . SER   B 1 256 ? -14.136 0.959   -49.222 1.00 50.23  ? 256 SER   B C    1 
ATOM   5658 O O    . SER   B 1 256 ? -13.446 0.090   -49.751 1.00 50.22  ? 256 SER   B O    1 
ATOM   5659 C CB   . SER   B 1 256 ? -16.533 0.513   -48.617 1.00 48.58  ? 256 SER   B CB   1 
ATOM   5660 O OG   . SER   B 1 256 ? -17.881 0.841   -48.918 1.00 50.59  ? 256 SER   B OG   1 
ATOM   5661 N N    . GLY   B 1 257 ? -13.647 1.767   -48.299 1.00 49.03  ? 257 GLY   B N    1 
ATOM   5662 C CA   . GLY   B 1 257 ? -12.273 1.531   -47.912 1.00 51.35  ? 257 GLY   B CA   1 
ATOM   5663 C C    . GLY   B 1 257 ? -11.807 2.425   -46.797 1.00 48.32  ? 257 GLY   B C    1 
ATOM   5664 O O    . GLY   B 1 257 ? -12.489 3.366   -46.381 1.00 50.63  ? 257 GLY   B O    1 
ATOM   5665 N N    . ILE   B 1 258 ? -10.620 2.094   -46.317 1.00 45.31  ? 258 ILE   B N    1 
ATOM   5666 C CA   . ILE   B 1 258 ? -9.888  2.875   -45.336 1.00 47.05  ? 258 ILE   B CA   1 
ATOM   5667 C C    . ILE   B 1 258 ? -8.538  3.197   -45.952 1.00 46.27  ? 258 ILE   B C    1 
ATOM   5668 O O    . ILE   B 1 258 ? -7.765  2.280   -46.263 1.00 48.97  ? 258 ILE   B O    1 
ATOM   5669 C CB   . ILE   B 1 258 ? -9.729  2.107   -44.015 1.00 49.35  ? 258 ILE   B CB   1 
ATOM   5670 C CG1  . ILE   B 1 258 ? -11.099 1.666   -43.470 1.00 47.29  ? 258 ILE   B CG1  1 
ATOM   5671 C CG2  . ILE   B 1 258 ? -8.946  2.936   -43.009 1.00 46.73  ? 258 ILE   B CG2  1 
ATOM   5672 C CD1  . ILE   B 1 258 ? -10.998 0.590   -42.357 1.00 49.31  ? 258 ILE   B CD1  1 
ATOM   5673 N N    . TYR   B 1 259 ? -8.252  4.487   -46.113 1.00 52.36  ? 259 TYR   B N    1 
ATOM   5674 C CA   . TYR   B 1 259 ? -7.081  4.961   -46.829 1.00 54.59  ? 259 TYR   B CA   1 
ATOM   5675 C C    . TYR   B 1 259 ? -6.251  5.889   -45.952 1.00 56.75  ? 259 TYR   B C    1 
ATOM   5676 O O    . TYR   B 1 259 ? -6.775  6.593   -45.080 1.00 55.05  ? 259 TYR   B O    1 
ATOM   5677 C CB   . TYR   B 1 259 ? -7.489  5.687   -48.116 1.00 53.95  ? 259 TYR   B CB   1 
ATOM   5678 C CG   . TYR   B 1 259 ? -8.666  5.055   -48.820 1.00 52.02  ? 259 TYR   B CG   1 
ATOM   5679 C CD1  . TYR   B 1 259 ? -8.586  3.759   -49.323 1.00 52.01  ? 259 TYR   B CD1  1 
ATOM   5680 C CD2  . TYR   B 1 259 ? -9.857  5.754   -48.986 1.00 48.60  ? 259 TYR   B CD2  1 
ATOM   5681 C CE1  . TYR   B 1 259 ? -9.666  3.178   -49.981 1.00 53.64  ? 259 TYR   B CE1  1 
ATOM   5682 C CE2  . TYR   B 1 259 ? -10.939 5.184   -49.637 1.00 49.89  ? 259 TYR   B CE2  1 
ATOM   5683 C CZ   . TYR   B 1 259 ? -10.841 3.900   -50.136 1.00 52.73  ? 259 TYR   B CZ   1 
ATOM   5684 O OH   . TYR   B 1 259 ? -11.922 3.347   -50.802 1.00 51.87  ? 259 TYR   B OH   1 
ATOM   5685 N N    . ALA   B 1 260 ? -4.948  5.870   -46.185 1.00 61.75  ? 260 ALA   B N    1 
ATOM   5686 C CA   . ALA   B 1 260 ? -4.019  6.696   -45.427 1.00 63.05  ? 260 ALA   B CA   1 
ATOM   5687 C C    . ALA   B 1 260 ? -3.276  7.596   -46.404 1.00 62.45  ? 260 ALA   B C    1 
ATOM   5688 O O    . ALA   B 1 260 ? -3.365  7.411   -47.622 1.00 63.21  ? 260 ALA   B O    1 
ATOM   5689 C CB   . ALA   B 1 260 ? -3.045  5.851   -44.603 1.00 61.80  ? 260 ALA   B CB   1 
ATOM   5690 N N    . PRO   B 1 261 ? -2.570  8.605   -45.903 1.00 66.64  ? 261 PRO   B N    1 
ATOM   5691 C CA   . PRO   B 1 261 ? -1.869  9.532   -46.807 1.00 63.15  ? 261 PRO   B CA   1 
ATOM   5692 C C    . PRO   B 1 261 ? -0.866  8.854   -47.725 1.00 66.21  ? 261 PRO   B C    1 
ATOM   5693 O O    . PRO   B 1 261 ? -0.699  9.294   -48.872 1.00 63.79  ? 261 PRO   B O    1 
ATOM   5694 C CB   . PRO   B 1 261 ? -1.179  10.505  -45.835 1.00 62.54  ? 261 PRO   B CB   1 
ATOM   5695 C CG   . PRO   B 1 261 ? -1.984  10.384  -44.542 1.00 62.74  ? 261 PRO   B CG   1 
ATOM   5696 C CD   . PRO   B 1 261 ? -2.405  8.951   -44.480 1.00 59.19  ? 261 PRO   B CD   1 
ATOM   5697 N N    . ASN   B 1 262 ? -0.190  7.802   -47.256 1.00 65.71  ? 262 ASN   B N    1 
ATOM   5698 C CA   . ASN   B 1 262 ? 0.852   7.148   -48.034 1.00 66.68  ? 262 ASN   B CA   1 
ATOM   5699 C C    . ASN   B 1 262 ? 0.340   5.953   -48.819 1.00 70.59  ? 262 ASN   B C    1 
ATOM   5700 O O    . ASN   B 1 262 ? 1.059   5.445   -49.688 1.00 73.20  ? 262 ASN   B O    1 
ATOM   5701 C CB   . ASN   B 1 262 ? 2.032   6.721   -47.134 1.00 70.28  ? 262 ASN   B CB   1 
ATOM   5702 C CG   . ASN   B 1 262 ? 1.682   5.586   -46.167 1.00 72.42  ? 262 ASN   B CG   1 
ATOM   5703 O OD1  . ASN   B 1 262 ? 0.594   5.017   -46.217 1.00 72.16  ? 262 ASN   B OD1  1 
ATOM   5704 N ND2  . ASN   B 1 262 ? 2.621   5.260   -45.274 1.00 78.24  ? 262 ASN   B ND2  1 
ATOM   5705 N N    . SER   B 1 263 ? -0.874  5.487   -48.538 1.00 62.61  ? 263 SER   B N    1 
ATOM   5706 C CA   . SER   B 1 263 ? -1.350  4.297   -49.217 1.00 62.15  ? 263 SER   B CA   1 
ATOM   5707 C C    . SER   B 1 263 ? -2.768  3.981   -48.764 1.00 59.41  ? 263 SER   B C    1 
ATOM   5708 O O    . SER   B 1 263 ? -3.245  4.483   -47.743 1.00 58.99  ? 263 SER   B O    1 
ATOM   5709 C CB   . SER   B 1 263 ? -0.431  3.105   -48.947 1.00 64.90  ? 263 SER   B CB   1 
ATOM   5710 O OG   . SER   B 1 263 ? -1.168  1.901   -49.001 1.00 67.98  ? 263 SER   B OG   1 
ATOM   5711 N N    . SER   B 1 264 ? -3.451  3.184   -49.581 1.00 59.56  ? 264 SER   B N    1 
ATOM   5712 C CA   . SER   B 1 264 ? -4.699  2.546   -49.185 1.00 59.65  ? 264 SER   B CA   1 
ATOM   5713 C C    . SER   B 1 264 ? -4.408  1.451   -48.164 1.00 58.43  ? 264 SER   B C    1 
ATOM   5714 O O    . SER   B 1 264 ? -3.414  0.726   -48.273 1.00 58.82  ? 264 SER   B O    1 
ATOM   5715 C CB   . SER   B 1 264 ? -5.414  1.978   -50.417 1.00 60.58  ? 264 SER   B CB   1 
ATOM   5716 O OG   . SER   B 1 264 ? -6.331  0.948   -50.087 1.00 62.33  ? 264 SER   B OG   1 
ATOM   5717 N N    . ARG   B 1 265 ? -5.249  1.360   -47.142 1.00 63.91  ? 265 ARG   B N    1 
ATOM   5718 C CA   . ARG   B 1 265 ? -5.045  0.378   -46.087 1.00 66.66  ? 265 ARG   B CA   1 
ATOM   5719 C C    . ARG   B 1 265 ? -5.974  -0.819  -46.203 1.00 69.38  ? 265 ARG   B C    1 
ATOM   5720 O O    . ARG   B 1 265 ? -5.564  -1.946  -45.912 1.00 68.92  ? 265 ARG   B O    1 
ATOM   5721 C CB   . ARG   B 1 265 ? -5.220  1.056   -44.727 1.00 63.73  ? 265 ARG   B CB   1 
ATOM   5722 C CG   . ARG   B 1 265 ? -4.112  2.029   -44.426 1.00 62.90  ? 265 ARG   B CG   1 
ATOM   5723 C CD   . ARG   B 1 265 ? -2.782  1.291   -44.367 1.00 67.74  ? 265 ARG   B CD   1 
ATOM   5724 N NE   . ARG   B 1 265 ? -1.649  2.204   -44.321 1.00 73.10  ? 265 ARG   B NE   1 
ATOM   5725 C CZ   . ARG   B 1 265 ? -1.406  3.049   -43.324 1.00 78.00  ? 265 ARG   B CZ   1 
ATOM   5726 N NH1  . ARG   B 1 265 ? -2.224  3.152   -42.283 1.00 74.02  ? 265 ARG   B NH1  1 
ATOM   5727 N NH2  . ARG   B 1 265 ? -0.317  3.817   -43.374 1.00 80.25  ? 265 ARG   B NH2  1 
ATOM   5728 N N    . ALA   B 1 266 ? -7.206  -0.598  -46.650 1.00 64.28  ? 266 ALA   B N    1 
ATOM   5729 C CA   . ALA   B 1 266 ? -8.137  -1.682  -46.933 1.00 61.51  ? 266 ALA   B CA   1 
ATOM   5730 C C    . ALA   B 1 266 ? -9.165  -1.169  -47.930 1.00 61.50  ? 266 ALA   B C    1 
ATOM   5731 O O    . ALA   B 1 266 ? -9.496  0.018   -47.929 1.00 58.05  ? 266 ALA   B O    1 
ATOM   5732 C CB   . ALA   B 1 266 ? -8.834  -2.185  -45.662 1.00 58.77  ? 266 ALA   B CB   1 
ATOM   5733 N N    . PHE   B 1 267 ? -9.677  -2.066  -48.772 1.00 54.15  ? 267 PHE   B N    1 
ATOM   5734 C CA   . PHE   B 1 267 ? -10.723 -1.652  -49.694 1.00 50.95  ? 267 PHE   B CA   1 
ATOM   5735 C C    . PHE   B 1 267 ? -11.587 -2.852  -50.060 1.00 50.43  ? 267 PHE   B C    1 
ATOM   5736 O O    . PHE   B 1 267 ? -11.184 -4.008  -49.926 1.00 51.58  ? 267 PHE   B O    1 
ATOM   5737 C CB   . PHE   B 1 267 ? -10.138 -0.973  -50.942 1.00 51.13  ? 267 PHE   B CB   1 
ATOM   5738 C CG   . PHE   B 1 267 ? -9.511  -1.926  -51.925 1.00 52.69  ? 267 PHE   B CG   1 
ATOM   5739 C CD1  . PHE   B 1 267 ? -8.206  -2.359  -51.754 1.00 52.68  ? 267 PHE   B CD1  1 
ATOM   5740 C CD2  . PHE   B 1 267 ? -10.226 -2.380  -53.024 1.00 50.86  ? 267 PHE   B CD2  1 
ATOM   5741 C CE1  . PHE   B 1 267 ? -7.624  -3.230  -52.643 1.00 52.89  ? 267 PHE   B CE1  1 
ATOM   5742 C CE2  . PHE   B 1 267 ? -9.658  -3.258  -53.917 1.00 49.49  ? 267 PHE   B CE2  1 
ATOM   5743 C CZ   . PHE   B 1 267 ? -8.353  -3.689  -53.729 1.00 52.87  ? 267 PHE   B CZ   1 
ATOM   5744 N N    . HIS   B 1 268 ? -12.798 -2.544  -50.507 1.00 53.02  ? 268 HIS   B N    1 
ATOM   5745 C CA   . HIS   B 1 268 ? -13.785 -3.524  -50.929 1.00 54.37  ? 268 HIS   B CA   1 
ATOM   5746 C C    . HIS   B 1 268 ? -14.408 -3.062  -52.240 1.00 52.08  ? 268 HIS   B C    1 
ATOM   5747 O O    . HIS   B 1 268 ? -14.731 -1.871  -52.394 1.00 51.07  ? 268 HIS   B O    1 
ATOM   5748 C CB   . HIS   B 1 268 ? -14.881 -3.717  -49.877 1.00 49.44  ? 268 HIS   B CB   1 
ATOM   5749 C CG   . HIS   B 1 268 ? -15.809 -4.852  -50.181 1.00 50.41  ? 268 HIS   B CG   1 
ATOM   5750 N ND1  . HIS   B 1 268 ? -15.423 -6.174  -50.084 1.00 51.57  ? 268 HIS   B ND1  1 
ATOM   5751 C CD2  . HIS   B 1 268 ? -17.096 -4.863  -50.602 1.00 48.79  ? 268 HIS   B CD2  1 
ATOM   5752 C CE1  . HIS   B 1 268 ? -16.440 -6.951  -50.414 1.00 51.96  ? 268 HIS   B CE1  1 
ATOM   5753 N NE2  . HIS   B 1 268 ? -17.466 -6.181  -50.732 1.00 51.97  ? 268 HIS   B NE2  1 
ATOM   5754 N N    . TYR   B 1 269 ? -14.546 -4.007  -53.175 1.00 49.09  ? 269 TYR   B N    1 
ATOM   5755 C CA   . TYR   B 1 269 ? -15.197 -3.790  -54.469 1.00 46.21  ? 269 TYR   B CA   1 
ATOM   5756 C C    . TYR   B 1 269 ? -15.818 -5.111  -54.912 1.00 48.94  ? 269 TYR   B C    1 
ATOM   5757 O O    . TYR   B 1 269 ? -15.089 -6.081  -55.147 1.00 49.70  ? 269 TYR   B O    1 
ATOM   5758 C CB   . TYR   B 1 269 ? -14.194 -3.295  -55.513 1.00 46.50  ? 269 TYR   B CB   1 
ATOM   5759 C CG   . TYR   B 1 269 ? -14.823 -3.082  -56.872 1.00 46.43  ? 269 TYR   B CG   1 
ATOM   5760 C CD1  . TYR   B 1 269 ? -15.030 -4.149  -57.736 1.00 47.06  ? 269 TYR   B CD1  1 
ATOM   5761 C CD2  . TYR   B 1 269 ? -15.240 -1.819  -57.271 1.00 48.58  ? 269 TYR   B CD2  1 
ATOM   5762 C CE1  . TYR   B 1 269 ? -15.617 -3.954  -58.983 1.00 51.02  ? 269 TYR   B CE1  1 
ATOM   5763 C CE2  . TYR   B 1 269 ? -15.825 -1.614  -58.521 1.00 47.18  ? 269 TYR   B CE2  1 
ATOM   5764 C CZ   . TYR   B 1 269 ? -16.007 -2.686  -59.363 1.00 47.61  ? 269 TYR   B CZ   1 
ATOM   5765 O OH   . TYR   B 1 269 ? -16.595 -2.500  -60.577 1.00 52.06  ? 269 TYR   B OH   1 
ATOM   5766 N N    . ASP   B 1 270 ? -17.145 -5.150  -55.073 1.00 53.32  ? 270 ASP   B N    1 
ATOM   5767 C CA   . ASP   B 1 270 ? -17.832 -6.411  -55.363 1.00 55.14  ? 270 ASP   B CA   1 
ATOM   5768 C C    . ASP   B 1 270 ? -19.066 -6.131  -56.212 1.00 58.21  ? 270 ASP   B C    1 
ATOM   5769 O O    . ASP   B 1 270 ? -20.057 -5.592  -55.710 1.00 58.34  ? 270 ASP   B O    1 
ATOM   5770 C CB   . ASP   B 1 270 ? -18.210 -7.128  -54.067 1.00 56.82  ? 270 ASP   B CB   1 
ATOM   5771 C CG   . ASP   B 1 270 ? -19.278 -8.198  -54.264 1.00 61.14  ? 270 ASP   B CG   1 
ATOM   5772 O OD1  . ASP   B 1 270 ? -19.252 -8.905  -55.294 1.00 61.50  ? 270 ASP   B OD1  1 
ATOM   5773 O OD2  . ASP   B 1 270 ? -20.130 -8.354  -53.356 1.00 62.61  ? 270 ASP   B OD2  1 
ATOM   5774 N N    . MET   B 1 271 ? -19.014 -6.483  -57.498 1.00 54.85  ? 271 MET   B N    1 
ATOM   5775 C CA   . MET   B 1 271 ? -20.204 -6.349  -58.316 1.00 53.84  ? 271 MET   B CA   1 
ATOM   5776 C C    . MET   B 1 271 ? -21.010 -7.631  -58.413 1.00 56.00  ? 271 MET   B C    1 
ATOM   5777 O O    . MET   B 1 271 ? -22.137 -7.595  -58.915 1.00 60.05  ? 271 MET   B O    1 
ATOM   5778 C CB   . MET   B 1 271 ? -19.830 -5.848  -59.711 1.00 59.09  ? 271 MET   B CB   1 
ATOM   5779 C CG   . MET   B 1 271 ? -19.396 -4.387  -59.704 1.00 53.18  ? 271 MET   B CG   1 
ATOM   5780 S SD   . MET   B 1 271 ? -20.786 -3.234  -59.632 1.00 52.93  ? 271 MET   B SD   1 
ATOM   5781 C CE   . MET   B 1 271 ? -21.683 -3.624  -61.135 1.00 50.96  ? 271 MET   B CE   1 
ATOM   5782 N N    . LYS   B 1 272 ? -20.499 -8.749  -57.911 1.00 63.24  ? 272 LYS   B N    1 
ATOM   5783 C CA   . LYS   B 1 272 ? -21.151 -10.024 -58.177 1.00 64.85  ? 272 LYS   B CA   1 
ATOM   5784 C C    . LYS   B 1 272 ? -22.276 -10.337 -57.191 1.00 67.96  ? 272 LYS   B C    1 
ATOM   5785 O O    . LYS   B 1 272 ? -23.356 -10.752 -57.615 1.00 69.89  ? 272 LYS   B O    1 
ATOM   5786 C CB   . LYS   B 1 272 ? -20.110 -11.147 -58.161 1.00 66.65  ? 272 LYS   B CB   1 
ATOM   5787 C CG   . LYS   B 1 272 ? -18.819 -10.826 -58.926 1.00 71.29  ? 272 LYS   B CG   1 
ATOM   5788 C CD   . LYS   B 1 272 ? -18.547 -11.857 -60.024 1.00 76.99  ? 272 LYS   B CD   1 
ATOM   5789 C CE   . LYS   B 1 272 ? -17.248 -11.573 -60.774 1.00 78.91  ? 272 LYS   B CE   1 
ATOM   5790 N NZ   . LYS   B 1 272 ? -16.047 -11.887 -59.937 1.00 82.27  ? 272 LYS   B NZ   1 
ATOM   5791 N N    . THR   B 1 273 ? -22.070 -10.123 -55.883 1.00 65.34  ? 273 THR   B N    1 
ATOM   5792 C CA   . THR   B 1 273 ? -23.041 -10.495 -54.855 1.00 63.36  ? 273 THR   B CA   1 
ATOM   5793 C C    . THR   B 1 273 ? -23.767 -9.256  -54.325 1.00 65.82  ? 273 THR   B C    1 
ATOM   5794 O O    . THR   B 1 273 ? -23.516 -8.125  -54.748 1.00 58.58  ? 273 THR   B O    1 
ATOM   5795 C CB   . THR   B 1 273 ? -22.370 -11.238 -53.691 1.00 65.18  ? 273 THR   B CB   1 
ATOM   5796 O OG1  . THR   B 1 273 ? -21.762 -10.282 -52.806 1.00 65.11  ? 273 THR   B OG1  1 
ATOM   5797 C CG2  . THR   B 1 273 ? -21.323 -12.221 -54.178 1.00 64.82  ? 273 THR   B CG2  1 
ATOM   5798 N N    . GLU   B 1 274 ? -24.708 -9.494  -53.407 1.00 69.80  ? 274 GLU   B N    1 
ATOM   5799 C CA   . GLU   B 1 274 ? -25.409 -8.438  -52.684 1.00 71.62  ? 274 GLU   B CA   1 
ATOM   5800 C C    . GLU   B 1 274 ? -24.992 -8.341  -51.223 1.00 68.40  ? 274 GLU   B C    1 
ATOM   5801 O O    . GLU   B 1 274 ? -25.607 -7.585  -50.468 1.00 69.13  ? 274 GLU   B O    1 
ATOM   5802 C CB   . GLU   B 1 274 ? -26.923 -8.656  -52.744 1.00 69.39  ? 274 GLU   B CB   1 
ATOM   5803 C CG   . GLU   B 1 274 ? -27.518 -8.702  -54.110 1.00 68.98  ? 274 GLU   B CG   1 
ATOM   5804 C CD   . GLU   B 1 274 ? -29.016 -8.908  -54.047 1.00 79.25  ? 274 GLU   B CD   1 
ATOM   5805 O OE1  . GLU   B 1 274 ? -29.528 -9.194  -52.939 1.00 82.64  ? 274 GLU   B OE1  1 
ATOM   5806 O OE2  . GLU   B 1 274 ? -29.680 -8.797  -55.097 1.00 76.94  ? 274 GLU   B OE2  1 
ATOM   5807 N N    . GLU   B 1 275 ? -23.990 -9.103  -50.798 1.00 72.65  ? 275 GLU   B N    1 
ATOM   5808 C CA   . GLU   B 1 275 ? -23.542 -9.054  -49.413 1.00 69.60  ? 275 GLU   B CA   1 
ATOM   5809 C C    . GLU   B 1 275 ? -22.975 -7.678  -49.086 1.00 68.16  ? 275 GLU   B C    1 
ATOM   5810 O O    . GLU   B 1 275 ? -22.425 -6.985  -49.945 1.00 65.25  ? 275 GLU   B O    1 
ATOM   5811 C CB   . GLU   B 1 275 ? -22.473 -10.118 -49.158 1.00 68.57  ? 275 GLU   B CB   1 
ATOM   5812 C CG   . GLU   B 1 275 ? -22.953 -11.569 -49.157 1.00 75.25  ? 275 GLU   B CG   1 
ATOM   5813 C CD   . GLU   B 1 275 ? -24.440 -11.717 -48.857 1.00 81.84  ? 275 GLU   B CD   1 
ATOM   5814 O OE1  . GLU   B 1 275 ? -25.233 -11.872 -49.810 1.00 87.36  ? 275 GLU   B OE1  1 
ATOM   5815 O OE2  . GLU   B 1 275 ? -24.819 -11.683 -47.662 1.00 81.76  ? 275 GLU   B OE2  1 
ATOM   5816 N N    . GLY   B 1 276 ? -23.130 -7.276  -47.818 1.00 64.60  ? 276 GLY   B N    1 
ATOM   5817 C CA   . GLY   B 1 276 ? -22.387 -6.161  -47.273 1.00 58.20  ? 276 GLY   B CA   1 
ATOM   5818 C C    . GLY   B 1 276 ? -20.991 -6.599  -46.884 1.00 61.13  ? 276 GLY   B C    1 
ATOM   5819 O O    . GLY   B 1 276 ? -20.626 -7.769  -46.990 1.00 62.96  ? 276 GLY   B O    1 
ATOM   5820 N N    . LYS   B 1 277 ? -20.193 -5.637  -46.414 1.00 52.12  ? 277 LYS   B N    1 
ATOM   5821 C CA   . LYS   B 1 277 ? -18.810 -5.941  -46.048 1.00 50.29  ? 277 LYS   B CA   1 
ATOM   5822 C C    . LYS   B 1 277 ? -18.312 -4.918  -45.043 1.00 49.71  ? 277 LYS   B C    1 
ATOM   5823 O O    . LYS   B 1 277 ? -18.361 -3.713  -45.306 1.00 47.07  ? 277 LYS   B O    1 
ATOM   5824 C CB   . LYS   B 1 277 ? -17.896 -5.957  -47.290 1.00 51.11  ? 277 LYS   B CB   1 
ATOM   5825 C CG   . LYS   B 1 277 ? -16.449 -6.333  -46.986 1.00 50.05  ? 277 LYS   B CG   1 
ATOM   5826 C CD   . LYS   B 1 277 ? -16.353 -7.799  -46.580 1.00 52.24  ? 277 LYS   B CD   1 
ATOM   5827 C CE   . LYS   B 1 277 ? -14.911 -8.286  -46.573 1.00 52.42  ? 277 LYS   B CE   1 
ATOM   5828 N NZ   . LYS   B 1 277 ? -14.803 -9.610  -45.902 1.00 60.10  ? 277 LYS   B NZ   1 
ATOM   5829 N N    . LEU   B 1 278 ? -17.818 -5.412  -43.902 1.00 46.45  ? 278 LEU   B N    1 
ATOM   5830 C CA   . LEU   B 1 278 ? -17.233 -4.604  -42.838 1.00 45.68  ? 278 LEU   B CA   1 
ATOM   5831 C C    . LEU   B 1 278 ? -15.716 -4.625  -42.992 1.00 46.01  ? 278 LEU   B C    1 
ATOM   5832 O O    . LEU   B 1 278 ? -15.126 -5.695  -43.156 1.00 47.78  ? 278 LEU   B O    1 
ATOM   5833 C CB   . LEU   B 1 278 ? -17.634 -5.154  -41.463 1.00 47.16  ? 278 LEU   B CB   1 
ATOM   5834 C CG   . LEU   B 1 278 ? -16.997 -4.511  -40.227 1.00 47.05  ? 278 LEU   B CG   1 
ATOM   5835 C CD1  . LEU   B 1 278 ? -17.535 -3.107  -40.045 1.00 45.06  ? 278 LEU   B CD1  1 
ATOM   5836 C CD2  . LEU   B 1 278 ? -17.272 -5.371  -38.972 1.00 49.16  ? 278 LEU   B CD2  1 
ATOM   5837 N N    . LEU   B 1 279 ? -15.089 -3.452  -42.968 1.00 48.45  ? 279 LEU   B N    1 
ATOM   5838 C CA   . LEU   B 1 279 ? -13.636 -3.351  -43.028 1.00 49.48  ? 279 LEU   B CA   1 
ATOM   5839 C C    . LEU   B 1 279 ? -13.111 -2.693  -41.753 1.00 53.77  ? 279 LEU   B C    1 
ATOM   5840 O O    . LEU   B 1 279 ? -13.727 -1.756  -41.221 1.00 51.18  ? 279 LEU   B O    1 
ATOM   5841 C CB   . LEU   B 1 279 ? -13.165 -2.553  -44.250 1.00 50.88  ? 279 LEU   B CB   1 
ATOM   5842 C CG   . LEU   B 1 279 ? -13.630 -3.038  -45.630 1.00 51.82  ? 279 LEU   B CG   1 
ATOM   5843 C CD1  . LEU   B 1 279 ? -13.199 -2.051  -46.723 1.00 51.39  ? 279 LEU   B CD1  1 
ATOM   5844 C CD2  . LEU   B 1 279 ? -13.141 -4.456  -45.963 1.00 49.79  ? 279 LEU   B CD2  1 
ATOM   5845 N N    . LEU   B 1 280 ? -11.993 -3.214  -41.251 1.00 53.02  ? 280 LEU   B N    1 
ATOM   5846 C CA   . LEU   B 1 280 ? -11.303 -2.657  -40.101 1.00 54.92  ? 280 LEU   B CA   1 
ATOM   5847 C C    . LEU   B 1 280 ? -9.834  -2.483  -40.453 1.00 55.77  ? 280 LEU   B C    1 
ATOM   5848 O O    . LEU   B 1 280 ? -9.259  -3.297  -41.180 1.00 58.34  ? 280 LEU   B O    1 
ATOM   5849 C CB   . LEU   B 1 280 ? -11.434 -3.559  -38.854 1.00 52.37  ? 280 LEU   B CB   1 
ATOM   5850 C CG   . LEU   B 1 280 ? -12.538 -3.305  -37.820 1.00 52.33  ? 280 LEU   B CG   1 
ATOM   5851 C CD1  . LEU   B 1 280 ? -13.918 -3.455  -38.388 1.00 55.64  ? 280 LEU   B CD1  1 
ATOM   5852 C CD2  . LEU   B 1 280 ? -12.366 -4.286  -36.687 1.00 55.74  ? 280 LEU   B CD2  1 
ATOM   5853 N N    . SER   B 1 281 ? -9.217  -1.440  -39.900 1.00 61.50  ? 281 SER   B N    1 
ATOM   5854 C CA   . SER   B 1 281 ? -7.795  -1.229  -40.133 1.00 62.07  ? 281 SER   B CA   1 
ATOM   5855 C C    . SER   B 1 281 ? -7.246  -0.228  -39.123 1.00 60.77  ? 281 SER   B C    1 
ATOM   5856 O O    . SER   B 1 281 ? -7.961  0.664   -38.652 1.00 60.17  ? 281 SER   B O    1 
ATOM   5857 C CB   . SER   B 1 281 ? -7.522  -0.753  -41.566 1.00 61.50  ? 281 SER   B CB   1 
ATOM   5858 O OG   . SER   B 1 281 ? -6.150  -0.899  -41.877 1.00 60.87  ? 281 SER   B OG   1 
ATOM   5859 N N    . GLN   B 1 282 ? -5.984  -0.429  -38.760 1.00 68.81  ? 282 GLN   B N    1 
ATOM   5860 C CA   . GLN   B 1 282 ? -5.281  0.493   -37.889 1.00 70.90  ? 282 GLN   B CA   1 
ATOM   5861 C C    . GLN   B 1 282 ? -4.793  1.712   -38.659 1.00 69.72  ? 282 GLN   B C    1 
ATOM   5862 O O    . GLN   B 1 282 ? -4.304  1.601   -39.784 1.00 73.43  ? 282 GLN   B O    1 
ATOM   5863 C CB   . GLN   B 1 282 ? -4.106  -0.215  -37.222 1.00 71.60  ? 282 GLN   B CB   1 
ATOM   5864 C CG   . GLN   B 1 282 ? -4.482  -0.829  -35.908 1.00 69.73  ? 282 GLN   B CG   1 
ATOM   5865 C CD   . GLN   B 1 282 ? -3.996  0.006   -34.759 1.00 77.99  ? 282 GLN   B CD   1 
ATOM   5866 O OE1  . GLN   B 1 282 ? -4.778  0.698   -34.098 1.00 77.94  ? 282 GLN   B OE1  1 
ATOM   5867 N NE2  . GLN   B 1 282 ? -2.693  -0.058  -34.499 1.00 82.18  ? 282 GLN   B NE2  1 
ATOM   5868 N N    . LEU   B 1 283 ? -4.908  2.878   -38.027 1.00 62.39  ? 283 LEU   B N    1 
ATOM   5869 C CA   . LEU   B 1 283 ? -4.471  4.142   -38.599 1.00 59.64  ? 283 LEU   B CA   1 
ATOM   5870 C C    . LEU   B 1 283 ? -3.729  4.928   -37.534 1.00 61.30  ? 283 LEU   B C    1 
ATOM   5871 O O    . LEU   B 1 283 ? -3.995  4.783   -36.335 1.00 61.12  ? 283 LEU   B O    1 
ATOM   5872 C CB   . LEU   B 1 283 ? -5.641  4.988   -39.107 1.00 56.83  ? 283 LEU   B CB   1 
ATOM   5873 C CG   . LEU   B 1 283 ? -6.420  4.502   -40.326 1.00 56.71  ? 283 LEU   B CG   1 
ATOM   5874 C CD1  . LEU   B 1 283 ? -7.700  5.316   -40.441 1.00 51.57  ? 283 LEU   B CD1  1 
ATOM   5875 C CD2  . LEU   B 1 283 ? -5.559  4.597   -41.578 1.00 55.17  ? 283 LEU   B CD2  1 
ATOM   5876 N N    . ASP   B 1 284 ? -2.805  5.774   -37.981 1.00 70.56  ? 284 ASP   B N    1 
ATOM   5877 C CA   . ASP   B 1 284 ? -2.207  6.751   -37.083 1.00 69.42  ? 284 ASP   B CA   1 
ATOM   5878 C C    . ASP   B 1 284 ? -3.222  7.836   -36.733 1.00 70.56  ? 284 ASP   B C    1 
ATOM   5879 O O    . ASP   B 1 284 ? -3.985  8.298   -37.586 1.00 68.79  ? 284 ASP   B O    1 
ATOM   5880 C CB   . ASP   B 1 284 ? -0.961  7.372   -37.715 1.00 70.43  ? 284 ASP   B CB   1 
ATOM   5881 C CG   . ASP   B 1 284 ? 0.175   6.367   -37.885 1.00 78.61  ? 284 ASP   B CG   1 
ATOM   5882 O OD1  . ASP   B 1 284 ? 0.036   5.215   -37.422 1.00 83.05  ? 284 ASP   B OD1  1 
ATOM   5883 O OD2  . ASP   B 1 284 ? 1.219   6.734   -38.472 1.00 81.16  ? 284 ASP   B OD2  1 
ATOM   5884 N N    . SER   B 1 285 ? -3.256  8.218   -35.452 1.00 61.69  ? 285 SER   B N    1 
ATOM   5885 C CA   . SER   B 1 285 ? -4.115  9.325   -35.045 1.00 59.68  ? 285 SER   B CA   1 
ATOM   5886 C C    . SER   B 1 285 ? -3.713  10.598  -35.772 1.00 58.53  ? 285 SER   B C    1 
ATOM   5887 O O    . SER   B 1 285 ? -4.568  11.340  -36.264 1.00 60.76  ? 285 SER   B O    1 
ATOM   5888 C CB   . SER   B 1 285 ? -4.037  9.525   -33.529 1.00 61.60  ? 285 SER   B CB   1 
ATOM   5889 O OG   . SER   B 1 285 ? -4.185  8.292   -32.842 1.00 62.43  ? 285 SER   B OG   1 
ATOM   5890 N N    . HIS   B 1 286 ? -2.409  10.844  -35.884 1.00 69.39  ? 286 HIS   B N    1 
ATOM   5891 C CA   . HIS   B 1 286 ? -1.864  11.990  -36.607 1.00 72.64  ? 286 HIS   B CA   1 
ATOM   5892 C C    . HIS   B 1 286 ? -0.879  11.425  -37.616 1.00 73.66  ? 286 HIS   B C    1 
ATOM   5893 O O    . HIS   B 1 286 ? 0.318   11.284  -37.314 1.00 73.68  ? 286 HIS   B O    1 
ATOM   5894 C CB   . HIS   B 1 286 ? -1.196  12.992  -35.667 1.00 72.41  ? 286 HIS   B CB   1 
ATOM   5895 C CG   . HIS   B 1 286 ? -2.068  13.408  -34.528 1.00 72.58  ? 286 HIS   B CG   1 
ATOM   5896 N ND1  . HIS   B 1 286 ? -3.110  14.301  -34.679 1.00 71.85  ? 286 HIS   B ND1  1 
ATOM   5897 C CD2  . HIS   B 1 286 ? -2.066  13.043  -33.225 1.00 75.05  ? 286 HIS   B CD2  1 
ATOM   5898 C CE1  . HIS   B 1 286 ? -3.705  14.474  -33.511 1.00 76.46  ? 286 HIS   B CE1  1 
ATOM   5899 N NE2  . HIS   B 1 286 ? -3.090  13.724  -32.612 1.00 76.36  ? 286 HIS   B NE2  1 
ATOM   5900 N N    . PRO   B 1 287 ? -1.346  11.081  -38.827 1.00 77.73  ? 287 PRO   B N    1 
ATOM   5901 C CA   . PRO   B 1 287 ? -0.440  10.485  -39.818 1.00 76.80  ? 287 PRO   B CA   1 
ATOM   5902 C C    . PRO   B 1 287 ? 0.664   11.461  -40.180 1.00 80.55  ? 287 PRO   B C    1 
ATOM   5903 O O    . PRO   B 1 287 ? 0.466   12.678  -40.195 1.00 85.08  ? 287 PRO   B O    1 
ATOM   5904 C CB   . PRO   B 1 287 ? -1.348  10.194  -41.020 1.00 75.56  ? 287 PRO   B CB   1 
ATOM   5905 C CG   . PRO   B 1 287 ? -2.753  10.446  -40.557 1.00 73.53  ? 287 PRO   B CG   1 
ATOM   5906 C CD   . PRO   B 1 287 ? -2.675  11.369  -39.389 1.00 73.88  ? 287 PRO   B CD   1 
ATOM   5907 N N    . SER   B 1 288 ? 1.825   10.917  -40.534 1.00 93.49  ? 288 SER   B N    1 
ATOM   5908 C CA   . SER   B 1 288 ? 2.919   11.775  -40.954 1.00 96.91  ? 288 SER   B CA   1 
ATOM   5909 C C    . SER   B 1 288 ? 2.729   12.137  -42.422 1.00 101.57 ? 288 SER   B C    1 
ATOM   5910 O O    . SER   B 1 288 ? 2.372   11.291  -43.253 1.00 93.79  ? 288 SER   B O    1 
ATOM   5911 C CB   . SER   B 1 288 ? 4.265   11.084  -40.721 1.00 100.97 ? 288 SER   B CB   1 
ATOM   5912 O OG   . SER   B 1 288 ? 5.246   11.535  -41.633 1.00 105.28 ? 288 SER   B OG   1 
ATOM   5913 N N    . HIS   B 1 289 ? 2.992   13.406  -42.731 1.00 129.86 ? 289 HIS   B N    1 
ATOM   5914 C CA   . HIS   B 1 289 ? 2.806   13.969  -44.059 1.00 126.42 ? 289 HIS   B CA   1 
ATOM   5915 C C    . HIS   B 1 289 ? 4.146   14.113  -44.755 1.00 124.40 ? 289 HIS   B C    1 
ATOM   5916 O O    . HIS   B 1 289 ? 5.123   14.570  -44.154 1.00 122.99 ? 289 HIS   B O    1 
ATOM   5917 C CB   . HIS   B 1 289 ? 2.149   15.354  -44.008 1.00 122.37 ? 289 HIS   B CB   1 
ATOM   5918 C CG   . HIS   B 1 289 ? 0.814   15.387  -43.338 1.00 128.50 ? 289 HIS   B CG   1 
ATOM   5919 N ND1  . HIS   B 1 289 ? 0.286   16.545  -42.808 1.00 133.14 ? 289 HIS   B ND1  1 
ATOM   5920 C CD2  . HIS   B 1 289 ? -0.107  14.419  -43.120 1.00 128.43 ? 289 HIS   B CD2  1 
ATOM   5921 C CE1  . HIS   B 1 289 ? -0.900  16.288  -42.288 1.00 133.42 ? 289 HIS   B CE1  1 
ATOM   5922 N NE2  . HIS   B 1 289 ? -1.162  15.006  -42.464 1.00 132.02 ? 289 HIS   B NE2  1 
ATOM   5923 N N    . SER   B 1 290 ? 4.194   13.704  -46.019 1.00 86.51  ? 290 SER   B N    1 
ATOM   5924 C CA   . SER   B 1 290 ? 5.330   14.127  -46.813 1.00 87.93  ? 290 SER   B CA   1 
ATOM   5925 C C    . SER   B 1 290 ? 5.275   15.645  -46.990 1.00 86.29  ? 290 SER   B C    1 
ATOM   5926 O O    . SER   B 1 290 ? 4.266   16.301  -46.700 1.00 82.53  ? 290 SER   B O    1 
ATOM   5927 C CB   . SER   B 1 290 ? 5.338   13.424  -48.174 1.00 84.13  ? 290 SER   B CB   1 
ATOM   5928 O OG   . SER   B 1 290 ? 4.413   14.028  -49.067 1.00 80.88  ? 290 SER   B OG   1 
ATOM   5929 N N    . ALA   B 1 291 ? 6.389   16.211  -47.439 1.00 85.81  ? 291 ALA   B N    1 
ATOM   5930 C CA   . ALA   B 1 291 ? 6.398   17.616  -47.810 1.00 82.73  ? 291 ALA   B CA   1 
ATOM   5931 C C    . ALA   B 1 291 ? 5.291   17.878  -48.829 1.00 87.68  ? 291 ALA   B C    1 
ATOM   5932 O O    . ALA   B 1 291 ? 4.898   16.989  -49.597 1.00 87.87  ? 291 ALA   B O    1 
ATOM   5933 C CB   . ALA   B 1 291 ? 7.766   18.013  -48.365 1.00 83.03  ? 291 ALA   B CB   1 
ATOM   5934 N N    . VAL   B 1 292 ? 4.742   19.095  -48.805 1.00 78.31  ? 292 VAL   B N    1 
ATOM   5935 C CA   . VAL   B 1 292 ? 3.735   19.443  -49.797 1.00 74.90  ? 292 VAL   B CA   1 
ATOM   5936 C C    . VAL   B 1 292 ? 4.338   19.235  -51.185 1.00 71.14  ? 292 VAL   B C    1 
ATOM   5937 O O    . VAL   B 1 292 ? 5.560   19.284  -51.370 1.00 77.36  ? 292 VAL   B O    1 
ATOM   5938 C CB   . VAL   B 1 292 ? 3.255   20.891  -49.588 1.00 72.49  ? 292 VAL   B CB   1 
ATOM   5939 C CG1  . VAL   B 1 292 ? 2.563   21.429  -50.814 1.00 71.93  ? 292 VAL   B CG1  1 
ATOM   5940 C CG2  . VAL   B 1 292 ? 2.322   20.968  -48.381 1.00 76.59  ? 292 VAL   B CG2  1 
ATOM   5941 N N    . VAL   B 1 293 ? 3.476   18.970  -52.163 1.00 64.27  ? 293 VAL   B N    1 
ATOM   5942 C CA   . VAL   B 1 293 ? 3.880   18.599  -53.521 1.00 65.57  ? 293 VAL   B CA   1 
ATOM   5943 C C    . VAL   B 1 293 ? 3.623   19.782  -54.447 1.00 62.31  ? 293 VAL   B C    1 
ATOM   5944 O O    . VAL   B 1 293 ? 2.506   20.313  -54.488 1.00 65.54  ? 293 VAL   B O    1 
ATOM   5945 C CB   . VAL   B 1 293 ? 3.115   17.350  -54.006 1.00 61.79  ? 293 VAL   B CB   1 
ATOM   5946 C CG1  . VAL   B 1 293 ? 3.429   17.018  -55.487 1.00 61.06  ? 293 VAL   B CG1  1 
ATOM   5947 C CG2  . VAL   B 1 293 ? 3.426   16.171  -53.120 1.00 62.36  ? 293 VAL   B CG2  1 
ATOM   5948 N N    . ASN   B 1 294 ? 4.646   20.174  -55.211 1.00 60.12  ? 294 ASN   B N    1 
ATOM   5949 C CA   . ASN   B 1 294 ? 4.483   21.090  -56.343 1.00 59.77  ? 294 ASN   B CA   1 
ATOM   5950 C C    . ASN   B 1 294 ? 4.229   20.210  -57.559 1.00 60.15  ? 294 ASN   B C    1 
ATOM   5951 O O    . ASN   B 1 294 ? 5.135   19.523  -58.044 1.00 58.88  ? 294 ASN   B O    1 
ATOM   5952 C CB   . ASN   B 1 294 ? 5.707   21.987  -56.531 1.00 60.62  ? 294 ASN   B CB   1 
ATOM   5953 C CG   . ASN   B 1 294 ? 5.516   23.053  -57.635 1.00 60.51  ? 294 ASN   B CG   1 
ATOM   5954 O OD1  . ASN   B 1 294 ? 4.557   22.990  -58.404 1.00 59.70  ? 294 ASN   B OD1  1 
ATOM   5955 N ND2  . ASN   B 1 294 ? 6.428   24.050  -57.692 1.00 61.45  ? 294 ASN   B ND2  1 
ATOM   5956 N N    . TRP   B 1 295 ? 2.969   20.167  -58.000 1.00 68.17  ? 295 TRP   B N    1 
ATOM   5957 C CA   . TRP   B 1 295 ? 2.547   19.253  -59.056 1.00 68.51  ? 295 TRP   B CA   1 
ATOM   5958 C C    . TRP   B 1 295 ? 3.101   19.619  -60.430 1.00 64.72  ? 295 TRP   B C    1 
ATOM   5959 O O    . TRP   B 1 295 ? 3.058   18.779  -61.330 1.00 64.85  ? 295 TRP   B O    1 
ATOM   5960 C CB   . TRP   B 1 295 ? 1.017   19.180  -59.097 1.00 63.98  ? 295 TRP   B CB   1 
ATOM   5961 C CG   . TRP   B 1 295 ? 0.485   18.406  -57.940 1.00 64.77  ? 295 TRP   B CG   1 
ATOM   5962 C CD1  . TRP   B 1 295 ? -0.164  18.905  -56.845 1.00 66.13  ? 295 TRP   B CD1  1 
ATOM   5963 C CD2  . TRP   B 1 295 ? 0.593   16.991  -57.732 1.00 64.13  ? 295 TRP   B CD2  1 
ATOM   5964 N NE1  . TRP   B 1 295 ? -0.478  17.891  -55.978 1.00 63.68  ? 295 TRP   B NE1  1 
ATOM   5965 C CE2  . TRP   B 1 295 ? -0.027  16.704  -56.496 1.00 66.17  ? 295 TRP   B CE2  1 
ATOM   5966 C CE3  . TRP   B 1 295 ? 1.155   15.939  -58.470 1.00 63.42  ? 295 TRP   B CE3  1 
ATOM   5967 C CZ2  . TRP   B 1 295 ? -0.104  15.406  -55.977 1.00 64.31  ? 295 TRP   B CZ2  1 
ATOM   5968 C CZ3  . TRP   B 1 295 ? 1.077   14.650  -57.957 1.00 64.87  ? 295 TRP   B CZ3  1 
ATOM   5969 C CH2  . TRP   B 1 295 ? 0.450   14.396  -56.719 1.00 64.42  ? 295 TRP   B CH2  1 
ATOM   5970 N N    . THR   B 1 296 ? 3.623   20.828  -60.618 1.00 64.72  ? 296 THR   B N    1 
ATOM   5971 C CA   . THR   B 1 296 ? 4.131   21.251  -61.919 1.00 65.46  ? 296 THR   B CA   1 
ATOM   5972 C C    . THR   B 1 296 ? 5.652   21.370  -61.976 1.00 65.50  ? 296 THR   B C    1 
ATOM   5973 O O    . THR   B 1 296 ? 6.186   21.766  -63.021 1.00 64.03  ? 296 THR   B O    1 
ATOM   5974 C CB   . THR   B 1 296 ? 3.495   22.590  -62.322 1.00 64.15  ? 296 THR   B CB   1 
ATOM   5975 O OG1  . THR   B 1 296 ? 3.912   22.947  -63.649 1.00 64.75  ? 296 THR   B OG1  1 
ATOM   5976 C CG2  . THR   B 1 296 ? 3.902   23.682  -61.351 1.00 64.23  ? 296 THR   B CG2  1 
ATOM   5977 N N    . SER   B 1 297 ? 6.361   21.069  -60.884 1.00 72.12  ? 297 SER   B N    1 
ATOM   5978 C CA   . SER   B 1 297 ? 7.810   21.258  -60.816 1.00 71.23  ? 297 SER   B CA   1 
ATOM   5979 C C    . SER   B 1 297 ? 8.543   20.438  -61.881 1.00 74.86  ? 297 SER   B C    1 
ATOM   5980 O O    . SER   B 1 297 ? 9.104   20.988  -62.848 1.00 75.30  ? 297 SER   B O    1 
ATOM   5981 C CB   . SER   B 1 297 ? 8.299   20.884  -59.408 1.00 72.92  ? 297 SER   B CB   1 
ATOM   5982 O OG   . SER   B 1 297 ? 9.482   21.572  -59.044 1.00 73.00  ? 297 SER   B OG   1 
ATOM   5983 N N    . TYR   B 1 298 ? 8.496   19.110  -61.743 1.00 76.65  ? 298 TYR   B N    1 
ATOM   5984 C CA   . TYR   B 1 298 ? 9.203   18.248  -62.684 1.00 77.51  ? 298 TYR   B CA   1 
ATOM   5985 C C    . TYR   B 1 298 ? 8.703   18.458  -64.107 1.00 76.68  ? 298 TYR   B C    1 
ATOM   5986 O O    . TYR   B 1 298 ? 9.500   18.629  -65.035 1.00 77.29  ? 298 TYR   B O    1 
ATOM   5987 C CB   . TYR   B 1 298 ? 9.071   16.781  -62.272 1.00 76.61  ? 298 TYR   B CB   1 
ATOM   5988 C CG   . TYR   B 1 298 ? 9.835   15.833  -63.179 1.00 76.77  ? 298 TYR   B CG   1 
ATOM   5989 C CD1  . TYR   B 1 298 ? 9.239   15.288  -64.310 1.00 76.83  ? 298 TYR   B CD1  1 
ATOM   5990 C CD2  . TYR   B 1 298 ? 11.162  15.513  -62.922 1.00 75.41  ? 298 TYR   B CD2  1 
ATOM   5991 C CE1  . TYR   B 1 298 ? 9.933   14.438  -65.141 1.00 77.78  ? 298 TYR   B CE1  1 
ATOM   5992 C CE2  . TYR   B 1 298 ? 11.861  14.659  -63.743 1.00 75.87  ? 298 TYR   B CE2  1 
ATOM   5993 C CZ   . TYR   B 1 298 ? 11.242  14.123  -64.855 1.00 77.96  ? 298 TYR   B CZ   1 
ATOM   5994 O OH   . TYR   B 1 298 ? 11.926  13.268  -65.695 1.00 82.04  ? 298 TYR   B OH   1 
ATOM   5995 N N    . ALA   B 1 299 ? 7.379   18.449  -64.299 1.00 68.82  ? 299 ALA   B N    1 
ATOM   5996 C CA   . ALA   B 1 299 ? 6.830   18.543  -65.650 1.00 67.67  ? 299 ALA   B CA   1 
ATOM   5997 C C    . ALA   B 1 299 ? 7.279   19.817  -66.350 1.00 67.59  ? 299 ALA   B C    1 
ATOM   5998 O O    . ALA   B 1 299 ? 7.579   19.803  -67.549 1.00 70.68  ? 299 ALA   B O    1 
ATOM   5999 C CB   . ALA   B 1 299 ? 5.304   18.482  -65.603 1.00 67.09  ? 299 ALA   B CB   1 
ATOM   6000 N N    . SER   B 1 300 ? 7.343   20.927  -65.619 1.00 70.85  ? 300 SER   B N    1 
ATOM   6001 C CA   . SER   B 1 300 ? 7.817   22.180  -66.189 1.00 70.40  ? 300 SER   B CA   1 
ATOM   6002 C C    . SER   B 1 300 ? 9.331   22.256  -66.321 1.00 71.73  ? 300 SER   B C    1 
ATOM   6003 O O    . SER   B 1 300 ? 9.826   23.156  -67.010 1.00 70.92  ? 300 SER   B O    1 
ATOM   6004 C CB   . SER   B 1 300 ? 7.330   23.357  -65.344 1.00 70.03  ? 300 SER   B CB   1 
ATOM   6005 O OG   . SER   B 1 300 ? 5.927   23.505  -65.462 1.00 72.22  ? 300 SER   B OG   1 
ATOM   6006 N N    . SER   B 1 301 ? 10.083  21.352  -65.691 1.00 76.65  ? 301 SER   B N    1 
ATOM   6007 C CA   . SER   B 1 301 ? 11.535  21.441  -65.794 1.00 74.39  ? 301 SER   B CA   1 
ATOM   6008 C C    . SER   B 1 301 ? 12.126  20.665  -66.966 1.00 76.12  ? 301 SER   B C    1 
ATOM   6009 O O    . SER   B 1 301 ? 13.319  20.821  -67.241 1.00 78.32  ? 301 SER   B O    1 
ATOM   6010 C CB   . SER   B 1 301 ? 12.190  20.939  -64.501 1.00 77.19  ? 301 SER   B CB   1 
ATOM   6011 O OG   . SER   B 1 301 ? 12.623  19.591  -64.634 1.00 76.88  ? 301 SER   B OG   1 
ATOM   6012 N N    . ILE   B 1 302 ? 11.347  19.831  -67.650 1.00 72.01  ? 302 ILE   B N    1 
ATOM   6013 C CA   . ILE   B 1 302 ? 11.855  19.035  -68.761 1.00 74.17  ? 302 ILE   B CA   1 
ATOM   6014 C C    . ILE   B 1 302 ? 11.308  19.568  -70.089 1.00 72.30  ? 302 ILE   B C    1 
ATOM   6015 O O    . ILE   B 1 302 ? 10.360  20.354  -70.135 1.00 72.31  ? 302 ILE   B O    1 
ATOM   6016 C CB   . ILE   B 1 302 ? 11.553  17.528  -68.590 1.00 72.72  ? 302 ILE   B CB   1 
ATOM   6017 C CG1  . ILE   B 1 302 ? 10.056  17.272  -68.426 1.00 70.99  ? 302 ILE   B CG1  1 
ATOM   6018 C CG2  . ILE   B 1 302 ? 12.318  16.954  -67.401 1.00 75.66  ? 302 ILE   B CG2  1 
ATOM   6019 C CD1  . ILE   B 1 302 ? 9.715   15.799  -68.472 1.00 70.59  ? 302 ILE   B CD1  1 
ATOM   6020 N N    . GLU   B 1 303 ? 11.892  19.084  -71.180 1.00 98.02  ? 303 GLU   B N    1 
ATOM   6021 C CA   . GLU   B 1 303 ? 11.355  19.284  -72.516 1.00 101.11 ? 303 GLU   B CA   1 
ATOM   6022 C C    . GLU   B 1 303 ? 10.484  18.093  -72.913 1.00 99.73  ? 303 GLU   B C    1 
ATOM   6023 O O    . GLU   B 1 303 ? 10.422  17.076  -72.219 1.00 99.43  ? 303 GLU   B O    1 
ATOM   6024 C CB   . GLU   B 1 303 ? 12.503  19.464  -73.519 1.00 104.34 ? 303 GLU   B CB   1 
ATOM   6025 C CG   . GLU   B 1 303 ? 12.827  20.900  -73.958 1.00 105.59 ? 303 GLU   B CG   1 
ATOM   6026 C CD   . GLU   B 1 303 ? 11.596  21.730  -74.309 1.00 109.59 ? 303 GLU   B CD   1 
ATOM   6027 O OE1  . GLU   B 1 303 ? 11.738  22.968  -74.435 1.00 108.68 ? 303 GLU   B OE1  1 
ATOM   6028 O OE2  . GLU   B 1 303 ? 10.494  21.154  -74.466 1.00 106.68 ? 303 GLU   B OE2  1 
ATOM   6029 N N    . ALA   B 1 304 ? 9.778   18.241  -74.034 1.00 72.45  ? 304 ALA   B N    1 
ATOM   6030 C CA   . ALA   B 1 304 ? 8.836   17.212  -74.457 1.00 71.60  ? 304 ALA   B CA   1 
ATOM   6031 C C    . ALA   B 1 304 ? 9.579   15.898  -74.694 1.00 72.26  ? 304 ALA   B C    1 
ATOM   6032 O O    . ALA   B 1 304 ? 10.619  15.873  -75.358 1.00 75.48  ? 304 ALA   B O    1 
ATOM   6033 C CB   . ALA   B 1 304 ? 8.093   17.658  -75.718 1.00 68.60  ? 304 ALA   B CB   1 
ATOM   6034 N N    . LEU   B 1 305 ? 9.064   14.811  -74.110 1.00 83.73  ? 305 LEU   B N    1 
ATOM   6035 C CA   . LEU   B 1 305 ? 9.712   13.503  -74.209 1.00 83.37  ? 305 LEU   B CA   1 
ATOM   6036 C C    . LEU   B 1 305 ? 9.543   12.847  -75.575 1.00 85.13  ? 305 LEU   B C    1 
ATOM   6037 O O    . LEU   B 1 305 ? 10.301  11.926  -75.913 1.00 81.49  ? 305 LEU   B O    1 
ATOM   6038 C CB   . LEU   B 1 305 ? 9.166   12.570  -73.129 1.00 81.40  ? 305 LEU   B CB   1 
ATOM   6039 C CG   . LEU   B 1 305 ? 9.513   12.894  -71.674 1.00 84.82  ? 305 LEU   B CG   1 
ATOM   6040 C CD1  . LEU   B 1 305 ? 8.393   12.423  -70.782 1.00 82.85  ? 305 LEU   B CD1  1 
ATOM   6041 C CD2  . LEU   B 1 305 ? 10.819  12.236  -71.267 1.00 83.89  ? 305 LEU   B CD2  1 
ATOM   6042 N N    . SER   B 1 306 ? 8.592   13.319  -76.372 1.00 75.44  ? 306 SER   B N    1 
ATOM   6043 C CA   . SER   B 1 306 ? 8.285   12.734  -77.663 1.00 73.76  ? 306 SER   B CA   1 
ATOM   6044 C C    . SER   B 1 306 ? 7.953   13.882  -78.593 1.00 77.49  ? 306 SER   B C    1 
ATOM   6045 O O    . SER   B 1 306 ? 7.659   14.997  -78.150 1.00 77.70  ? 306 SER   B O    1 
ATOM   6046 C CB   . SER   B 1 306 ? 7.121   11.733  -77.604 1.00 73.47  ? 306 SER   B CB   1 
ATOM   6047 O OG   . SER   B 1 306 ? 5.871   12.381  -77.758 1.00 72.68  ? 306 SER   B OG   1 
ATOM   6048 N N    . SER   B 1 307 ? 8.031   13.607  -79.890 1.00 83.63  ? 307 SER   B N    1 
ATOM   6049 C CA   . SER   B 1 307 ? 8.009   14.681  -80.862 1.00 83.12  ? 307 SER   B CA   1 
ATOM   6050 C C    . SER   B 1 307 ? 7.285   14.221  -82.118 1.00 85.15  ? 307 SER   B C    1 
ATOM   6051 O O    . SER   B 1 307 ? 7.326   13.042  -82.483 1.00 85.03  ? 307 SER   B O    1 
ATOM   6052 C CB   . SER   B 1 307 ? 9.452   15.106  -81.166 1.00 80.71  ? 307 SER   B CB   1 
ATOM   6053 O OG   . SER   B 1 307 ? 9.506   16.278  -81.949 1.00 86.35  ? 307 SER   B OG   1 
ATOM   6054 N N    . GLY   B 1 308 ? 6.605   15.167  -82.765 1.00 90.76  ? 308 GLY   B N    1 
ATOM   6055 C CA   . GLY   B 1 308 ? 5.783   14.854  -83.922 1.00 85.55  ? 308 GLY   B CA   1 
ATOM   6056 C C    . GLY   B 1 308 ? 4.715   13.800  -83.697 1.00 89.39  ? 308 GLY   B C    1 
ATOM   6057 O O    . GLY   B 1 308 ? 4.567   12.895  -84.526 1.00 87.59  ? 308 GLY   B O    1 
ATOM   6058 N N    . ASN   B 1 309 ? 3.945   13.917  -82.612 1.00 87.25  ? 309 ASN   B N    1 
ATOM   6059 C CA   . ASN   B 1 309 ? 2.933   12.917  -82.295 1.00 83.54  ? 309 ASN   B CA   1 
ATOM   6060 C C    . ASN   B 1 309 ? 1.803   12.887  -83.313 1.00 82.83  ? 309 ASN   B C    1 
ATOM   6061 O O    . ASN   B 1 309 ? 1.431   13.904  -83.901 1.00 83.33  ? 309 ASN   B O    1 
ATOM   6062 C CB   . ASN   B 1 309 ? 2.308   13.182  -80.928 1.00 81.98  ? 309 ASN   B CB   1 
ATOM   6063 C CG   . ASN   B 1 309 ? 3.241   12.882  -79.802 1.00 85.26  ? 309 ASN   B CG   1 
ATOM   6064 O OD1  . ASN   B 1 309 ? 3.188   13.515  -78.743 1.00 81.61  ? 309 ASN   B OD1  1 
ATOM   6065 N ND2  . ASN   B 1 309 ? 4.116   11.903  -80.016 1.00 89.23  ? 309 ASN   B ND2  1 
ATOM   6066 N N    . LYS   B 1 310 ? 1.242   11.697  -83.498 1.00 73.17  ? 310 LYS   B N    1 
ATOM   6067 C CA   . LYS   B 1 310 ? -0.048  11.532  -84.162 1.00 73.47  ? 310 LYS   B CA   1 
ATOM   6068 C C    . LYS   B 1 310 ? -1.116  11.490  -83.071 1.00 74.05  ? 310 LYS   B C    1 
ATOM   6069 O O    . LYS   B 1 310 ? -1.375  10.438  -82.481 1.00 71.21  ? 310 LYS   B O    1 
ATOM   6070 C CB   . LYS   B 1 310 ? -0.054  10.265  -85.009 1.00 74.39  ? 310 LYS   B CB   1 
ATOM   6071 C CG   . LYS   B 1 310 ? -1.437  9.791   -85.443 1.00 79.04  ? 310 LYS   B CG   1 
ATOM   6072 C CD   . LYS   B 1 310 ? -1.943  10.511  -86.689 1.00 81.54  ? 310 LYS   B CD   1 
ATOM   6073 C CE   . LYS   B 1 310 ? -3.393  10.133  -86.960 1.00 80.48  ? 310 LYS   B CE   1 
ATOM   6074 N NZ   . LYS   B 1 310 ? -4.293  11.326  -86.978 1.00 82.52  ? 310 LYS   B NZ   1 
ATOM   6075 N N    . GLU   B 1 311 ? -1.743  12.635  -82.808 1.00 62.13  ? 311 GLU   B N    1 
ATOM   6076 C CA   . GLU   B 1 311 ? -2.762  12.777  -81.778 1.00 61.68  ? 311 GLU   B CA   1 
ATOM   6077 C C    . GLU   B 1 311 ? -4.176  12.694  -82.357 1.00 60.22  ? 311 GLU   B C    1 
ATOM   6078 O O    . GLU   B 1 311 ? -4.411  12.933  -83.544 1.00 62.39  ? 311 GLU   B O    1 
ATOM   6079 C CB   . GLU   B 1 311 ? -2.571  14.101  -81.026 1.00 59.27  ? 311 GLU   B CB   1 
ATOM   6080 C CG   . GLU   B 1 311 ? -1.148  14.304  -80.559 1.00 58.53  ? 311 GLU   B CG   1 
ATOM   6081 C CD   . GLU   B 1 311 ? -0.919  15.675  -79.985 1.00 60.46  ? 311 GLU   B CD   1 
ATOM   6082 O OE1  . GLU   B 1 311 ? -1.735  16.566  -80.300 1.00 60.20  ? 311 GLU   B OE1  1 
ATOM   6083 O OE2  . GLU   B 1 311 ? 0.106   15.881  -79.289 1.00 61.70  ? 311 GLU   B OE2  1 
ATOM   6084 N N    . PHE   B 1 312 ? -5.124  12.369  -81.474 1.00 59.48  ? 312 PHE   B N    1 
ATOM   6085 C CA   . PHE   B 1 312 ? -6.528  12.185  -81.838 1.00 52.91  ? 312 PHE   B CA   1 
ATOM   6086 C C    . PHE   B 1 312 ? -7.392  12.528  -80.622 1.00 54.29  ? 312 PHE   B C    1 
ATOM   6087 O O    . PHE   B 1 312 ? -6.918  12.551  -79.491 1.00 51.36  ? 312 PHE   B O    1 
ATOM   6088 C CB   . PHE   B 1 312 ? -6.800  10.744  -82.317 1.00 51.39  ? 312 PHE   B CB   1 
ATOM   6089 C CG   . PHE   B 1 312 ? -6.518  9.695   -81.269 1.00 56.94  ? 312 PHE   B CG   1 
ATOM   6090 C CD1  . PHE   B 1 312 ? -5.226  9.212   -81.076 1.00 57.49  ? 312 PHE   B CD1  1 
ATOM   6091 C CD2  . PHE   B 1 312 ? -7.542  9.213   -80.436 1.00 54.03  ? 312 PHE   B CD2  1 
ATOM   6092 C CE1  . PHE   B 1 312 ? -4.960  8.260   -80.086 1.00 54.73  ? 312 PHE   B CE1  1 
ATOM   6093 C CE2  . PHE   B 1 312 ? -7.281  8.260   -79.473 1.00 49.52  ? 312 PHE   B CE2  1 
ATOM   6094 C CZ   . PHE   B 1 312 ? -5.993  7.787   -79.295 1.00 51.00  ? 312 PHE   B CZ   1 
ATOM   6095 N N    . LYS   B 1 313 ? -8.661  12.825  -80.872 1.00 65.93  ? 313 LYS   B N    1 
ATOM   6096 C CA   . LYS   B 1 313 ? -9.601  13.172  -79.818 1.00 59.98  ? 313 LYS   B CA   1 
ATOM   6097 C C    . LYS   B 1 313 ? -10.333 11.928  -79.340 1.00 64.76  ? 313 LYS   B C    1 
ATOM   6098 O O    . LYS   B 1 313 ? -10.689 11.062  -80.144 1.00 63.59  ? 313 LYS   B O    1 
ATOM   6099 C CB   . LYS   B 1 313 ? -10.615 14.201  -80.308 1.00 63.35  ? 313 LYS   B CB   1 
ATOM   6100 C CG   . LYS   B 1 313 ? -10.079 15.608  -80.348 1.00 66.83  ? 313 LYS   B CG   1 
ATOM   6101 C CD   . LYS   B 1 313 ? -9.253  15.865  -79.114 1.00 66.53  ? 313 LYS   B CD   1 
ATOM   6102 C CE   . LYS   B 1 313 ? -9.232  17.339  -78.736 1.00 67.37  ? 313 LYS   B CE   1 
ATOM   6103 N NZ   . LYS   B 1 313 ? -8.695  18.193  -79.823 1.00 71.62  ? 313 LYS   B NZ   1 
ATOM   6104 N N    . GLY   B 1 314 ? -10.535 11.833  -78.030 1.00 53.05  ? 314 GLY   B N    1 
ATOM   6105 C CA   . GLY   B 1 314 ? -11.303 10.732  -77.473 1.00 53.32  ? 314 GLY   B CA   1 
ATOM   6106 C C    . GLY   B 1 314 ? -12.055 11.158  -76.227 1.00 55.28  ? 314 GLY   B C    1 
ATOM   6107 O O    . GLY   B 1 314 ? -11.625 12.054  -75.502 1.00 55.05  ? 314 GLY   B O    1 
ATOM   6108 N N    . THR   B 1 315 ? -13.198 10.522  -75.992 1.00 53.14  ? 315 THR   B N    1 
ATOM   6109 C CA   . THR   B 1 315 ? -14.158 10.954  -74.986 1.00 53.56  ? 315 THR   B CA   1 
ATOM   6110 C C    . THR   B 1 315 ? -13.957 10.142  -73.705 1.00 54.52  ? 315 THR   B C    1 
ATOM   6111 O O    . THR   B 1 315 ? -14.014 8.907   -73.736 1.00 52.37  ? 315 THR   B O    1 
ATOM   6112 C CB   . THR   B 1 315 ? -15.586 10.788  -75.504 1.00 51.90  ? 315 THR   B CB   1 
ATOM   6113 O OG1  . THR   B 1 315 ? -15.679 11.351  -76.815 1.00 60.40  ? 315 THR   B OG1  1 
ATOM   6114 C CG2  . THR   B 1 315 ? -16.568 11.508  -74.616 1.00 52.69  ? 315 THR   B CG2  1 
ATOM   6115 N N    . VAL   B 1 316 ? -13.674 10.830  -72.596 1.00 47.14  ? 316 VAL   B N    1 
ATOM   6116 C CA   . VAL   B 1 316 ? -13.622 10.229  -71.255 1.00 44.08  ? 316 VAL   B CA   1 
ATOM   6117 C C    . VAL   B 1 316 ? -14.709 10.907  -70.437 1.00 46.03  ? 316 VAL   B C    1 
ATOM   6118 O O    . VAL   B 1 316 ? -14.587 12.092  -70.102 1.00 45.47  ? 316 VAL   B O    1 
ATOM   6119 C CB   . VAL   B 1 316 ? -12.256 10.401  -70.576 1.00 44.18  ? 316 VAL   B CB   1 
ATOM   6120 C CG1  . VAL   B 1 316 ? -12.186 9.562   -69.266 1.00 44.38  ? 316 VAL   B CG1  1 
ATOM   6121 C CG2  . VAL   B 1 316 ? -11.128 10.051  -71.530 1.00 46.51  ? 316 VAL   B CG2  1 
ATOM   6122 N N    . PHE   B 1 317 ? -15.763 10.171  -70.104 1.00 47.26  ? 317 PHE   B N    1 
ATOM   6123 C CA   . PHE   B 1 317 ? -16.836 10.721  -69.290 1.00 49.24  ? 317 PHE   B CA   1 
ATOM   6124 C C    . PHE   B 1 317 ? -17.334 12.041  -69.880 1.00 51.21  ? 317 PHE   B C    1 
ATOM   6125 O O    . PHE   B 1 317 ? -17.467 13.055  -69.187 1.00 53.39  ? 317 PHE   B O    1 
ATOM   6126 C CB   . PHE   B 1 317 ? -16.379 10.899  -67.835 1.00 49.04  ? 317 PHE   B CB   1 
ATOM   6127 C CG   . PHE   B 1 317 ? -17.502 11.176  -66.860 1.00 51.05  ? 317 PHE   B CG   1 
ATOM   6128 C CD1  . PHE   B 1 317 ? -18.777 10.664  -67.074 1.00 50.42  ? 317 PHE   B CD1  1 
ATOM   6129 C CD2  . PHE   B 1 317 ? -17.276 11.939  -65.720 1.00 50.96  ? 317 PHE   B CD2  1 
ATOM   6130 C CE1  . PHE   B 1 317 ? -19.812 10.919  -66.188 1.00 52.17  ? 317 PHE   B CE1  1 
ATOM   6131 C CE2  . PHE   B 1 317 ? -18.308 12.198  -64.814 1.00 50.33  ? 317 PHE   B CE2  1 
ATOM   6132 C CZ   . PHE   B 1 317 ? -19.573 11.686  -65.040 1.00 50.63  ? 317 PHE   B CZ   1 
ATOM   6133 N N    . PHE   B 1 318 ? -17.589 12.027  -71.191 1.00 48.79  ? 318 PHE   B N    1 
ATOM   6134 C CA   . PHE   B 1 318 ? -18.112 13.162  -71.950 1.00 47.38  ? 318 PHE   B CA   1 
ATOM   6135 C C    . PHE   B 1 318 ? -17.135 14.326  -72.051 1.00 49.37  ? 318 PHE   B C    1 
ATOM   6136 O O    . PHE   B 1 318 ? -17.538 15.438  -72.415 1.00 49.71  ? 318 PHE   B O    1 
ATOM   6137 C CB   . PHE   B 1 318 ? -19.444 13.671  -71.396 1.00 47.45  ? 318 PHE   B CB   1 
ATOM   6138 C CG   . PHE   B 1 318 ? -20.436 12.587  -71.098 1.00 51.62  ? 318 PHE   B CG   1 
ATOM   6139 C CD1  . PHE   B 1 318 ? -20.470 11.988  -69.835 1.00 50.23  ? 318 PHE   B CD1  1 
ATOM   6140 C CD2  . PHE   B 1 318 ? -21.381 12.201  -72.055 1.00 50.30  ? 318 PHE   B CD2  1 
ATOM   6141 C CE1  . PHE   B 1 318 ? -21.386 10.994  -69.547 1.00 49.46  ? 318 PHE   B CE1  1 
ATOM   6142 C CE2  . PHE   B 1 318 ? -22.315 11.203  -71.770 1.00 49.39  ? 318 PHE   B CE2  1 
ATOM   6143 C CZ   . PHE   B 1 318 ? -22.312 10.603  -70.498 1.00 52.62  ? 318 PHE   B CZ   1 
ATOM   6144 N N    . ASP   B 1 319 ? -15.862 14.104  -71.746 1.00 52.39  ? 319 ASP   B N    1 
ATOM   6145 C CA   . ASP   B 1 319 ? -14.836 15.133  -71.835 1.00 53.11  ? 319 ASP   B CA   1 
ATOM   6146 C C    . ASP   B 1 319 ? -13.890 14.775  -72.978 1.00 57.24  ? 319 ASP   B C    1 
ATOM   6147 O O    . ASP   B 1 319 ? -13.466 13.621  -73.092 1.00 54.85  ? 319 ASP   B O    1 
ATOM   6148 C CB   . ASP   B 1 319 ? -14.077 15.251  -70.517 1.00 51.86  ? 319 ASP   B CB   1 
ATOM   6149 C CG   . ASP   B 1 319 ? -14.903 15.927  -69.428 1.00 55.78  ? 319 ASP   B CG   1 
ATOM   6150 O OD1  . ASP   B 1 319 ? -16.025 16.432  -69.723 1.00 54.35  ? 319 ASP   B OD1  1 
ATOM   6151 O OD2  . ASP   B 1 319 ? -14.423 15.944  -68.272 1.00 49.96  ? 319 ASP   B OD2  1 
ATOM   6152 N N    . GLU   B 1 320 ? -13.543 15.764  -73.810 1.00 67.49  ? 320 GLU   B N    1 
ATOM   6153 C CA   . GLU   B 1 320 ? -12.754 15.519  -75.020 1.00 68.13  ? 320 GLU   B CA   1 
ATOM   6154 C C    . GLU   B 1 320 ? -11.272 15.648  -74.688 1.00 66.96  ? 320 GLU   B C    1 
ATOM   6155 O O    . GLU   B 1 320 ? -10.723 16.751  -74.625 1.00 69.03  ? 320 GLU   B O    1 
ATOM   6156 C CB   . GLU   B 1 320 ? -13.152 16.495  -76.121 1.00 71.92  ? 320 GLU   B CB   1 
ATOM   6157 C CG   . GLU   B 1 320 ? -13.185 15.884  -77.509 1.00 81.54  ? 320 GLU   B CG   1 
ATOM   6158 C CD   . GLU   B 1 320 ? -14.543 15.301  -77.865 1.00 90.32  ? 320 GLU   B CD   1 
ATOM   6159 O OE1  . GLU   B 1 320 ? -15.427 16.066  -78.325 1.00 96.60  ? 320 GLU   B OE1  1 
ATOM   6160 O OE2  . GLU   B 1 320 ? -14.729 14.076  -77.677 1.00 84.62  ? 320 GLU   B OE2  1 
ATOM   6161 N N    . PHE   B 1 321 ? -10.625 14.504  -74.497 1.00 54.62  ? 321 PHE   B N    1 
ATOM   6162 C CA   . PHE   B 1 321 ? -9.197  14.412  -74.266 1.00 54.55  ? 321 PHE   B CA   1 
ATOM   6163 C C    . PHE   B 1 321 ? -8.435  14.434  -75.589 1.00 60.20  ? 321 PHE   B C    1 
ATOM   6164 O O    . PHE   B 1 321 ? -8.945  14.011  -76.641 1.00 59.63  ? 321 PHE   B O    1 
ATOM   6165 C CB   . PHE   B 1 321 ? -8.866  13.115  -73.525 1.00 53.54  ? 321 PHE   B CB   1 
ATOM   6166 C CG   . PHE   B 1 321 ? -9.042  13.182  -72.020 1.00 49.39  ? 321 PHE   B CG   1 
ATOM   6167 C CD1  . PHE   B 1 321 ? -10.284 13.436  -71.454 1.00 46.95  ? 321 PHE   B CD1  1 
ATOM   6168 C CD2  . PHE   B 1 321 ? -7.961  12.944  -71.179 1.00 46.55  ? 321 PHE   B CD2  1 
ATOM   6169 C CE1  . PHE   B 1 321 ? -10.442 13.465  -70.053 1.00 45.58  ? 321 PHE   B CE1  1 
ATOM   6170 C CE2  . PHE   B 1 321 ? -8.107  12.972  -69.796 1.00 45.25  ? 321 PHE   B CE2  1 
ATOM   6171 C CZ   . PHE   B 1 321 ? -9.351  13.238  -69.231 1.00 43.87  ? 321 PHE   B CZ   1 
ATOM   6172 N N    . THR   B 1 322 ? -7.201  14.932  -75.521 1.00 61.23  ? 322 THR   B N    1 
ATOM   6173 C CA   . THR   B 1 322 ? -6.215  14.769  -76.580 1.00 64.92  ? 322 THR   B CA   1 
ATOM   6174 C C    . THR   B 1 322 ? -5.327  13.574  -76.242 1.00 63.23  ? 322 THR   B C    1 
ATOM   6175 O O    . THR   B 1 322 ? -4.642  13.583  -75.213 1.00 60.30  ? 322 THR   B O    1 
ATOM   6176 C CB   . THR   B 1 322 ? -5.383  16.040  -76.733 1.00 67.76  ? 322 THR   B CB   1 
ATOM   6177 O OG1  . THR   B 1 322 ? -6.259  17.124  -77.060 1.00 71.86  ? 322 THR   B OG1  1 
ATOM   6178 C CG2  . THR   B 1 322 ? -4.345  15.872  -77.846 1.00 67.82  ? 322 THR   B CG2  1 
ATOM   6179 N N    . PHE   B 1 323 ? -5.335  12.558  -77.105 1.00 61.37  ? 323 PHE   B N    1 
ATOM   6180 C CA   . PHE   B 1 323 ? -4.627  11.307  -76.882 1.00 61.33  ? 323 PHE   B CA   1 
ATOM   6181 C C    . PHE   B 1 323 ? -3.501  11.113  -77.892 1.00 67.22  ? 323 PHE   B C    1 
ATOM   6182 O O    . PHE   B 1 323 ? -3.609  11.490  -79.075 1.00 67.93  ? 323 PHE   B O    1 
ATOM   6183 C CB   . PHE   B 1 323 ? -5.559  10.104  -77.005 1.00 58.59  ? 323 PHE   B CB   1 
ATOM   6184 C CG   . PHE   B 1 323 ? -6.526  9.945   -75.879 1.00 56.50  ? 323 PHE   B CG   1 
ATOM   6185 C CD1  . PHE   B 1 323 ? -6.105  9.473   -74.647 1.00 53.82  ? 323 PHE   B CD1  1 
ATOM   6186 C CD2  . PHE   B 1 323 ? -7.875  10.204  -76.071 1.00 55.44  ? 323 PHE   B CD2  1 
ATOM   6187 C CE1  . PHE   B 1 323 ? -7.008  9.300   -73.608 1.00 51.87  ? 323 PHE   B CE1  1 
ATOM   6188 C CE2  . PHE   B 1 323 ? -8.784  10.028  -75.039 1.00 53.08  ? 323 PHE   B CE2  1 
ATOM   6189 C CZ   . PHE   B 1 323 ? -8.347  9.575   -73.809 1.00 53.65  ? 323 PHE   B CZ   1 
ATOM   6190 N N    . VAL   B 1 324 ? -2.449  10.448  -77.420 1.00 64.28  ? 324 VAL   B N    1 
ATOM   6191 C CA   . VAL   B 1 324 ? -1.458  9.810   -78.275 1.00 67.44  ? 324 VAL   B CA   1 
ATOM   6192 C C    . VAL   B 1 324 ? -1.390  8.335   -77.882 1.00 64.66  ? 324 VAL   B C    1 
ATOM   6193 O O    . VAL   B 1 324 ? -1.316  8.000   -76.691 1.00 60.11  ? 324 VAL   B O    1 
ATOM   6194 C CB   . VAL   B 1 324 ? -0.080  10.491  -78.165 1.00 68.23  ? 324 VAL   B CB   1 
ATOM   6195 C CG1  . VAL   B 1 324 ? 0.476   10.401  -76.738 1.00 63.90  ? 324 VAL   B CG1  1 
ATOM   6196 C CG2  . VAL   B 1 324 ? 0.885   9.881   -79.170 1.00 67.31  ? 324 VAL   B CG2  1 
ATOM   6197 N N    . LYS   B 1 325 ? -1.448  7.457   -78.879 1.00 57.63  ? 325 LYS   B N    1 
ATOM   6198 C CA   . LYS   B 1 325 ? -1.405  6.024   -78.631 1.00 54.77  ? 325 LYS   B CA   1 
ATOM   6199 C C    . LYS   B 1 325 ? 0.023   5.605   -78.300 1.00 56.18  ? 325 LYS   B C    1 
ATOM   6200 O O    . LYS   B 1 325 ? 0.979   6.126   -78.875 1.00 61.43  ? 325 LYS   B O    1 
ATOM   6201 C CB   . LYS   B 1 325 ? -1.939  5.276   -79.854 1.00 57.91  ? 325 LYS   B CB   1 
ATOM   6202 C CG   . LYS   B 1 325 ? -1.549  3.808   -79.976 1.00 60.29  ? 325 LYS   B CG   1 
ATOM   6203 C CD   . LYS   B 1 325 ? -2.176  3.248   -81.224 1.00 58.98  ? 325 LYS   B CD   1 
ATOM   6204 C CE   . LYS   B 1 325 ? -1.287  2.242   -81.950 1.00 62.11  ? 325 LYS   B CE   1 
ATOM   6205 N NZ   . LYS   B 1 325 ? -1.432  0.850   -81.442 1.00 66.13  ? 325 LYS   B NZ   1 
ATOM   6206 N N    . LEU   B 1 326 ? 0.173   4.698   -77.336 1.00 61.36  ? 326 LEU   B N    1 
ATOM   6207 C CA   . LEU   B 1 326 ? 1.473   4.145   -76.980 1.00 60.65  ? 326 LEU   B CA   1 
ATOM   6208 C C    . LEU   B 1 326 ? 1.737   2.939   -77.875 1.00 61.47  ? 326 LEU   B C    1 
ATOM   6209 O O    . LEU   B 1 326 ? 0.930   2.003   -77.901 1.00 61.11  ? 326 LEU   B O    1 
ATOM   6210 C CB   . LEU   B 1 326 ? 1.509   3.733   -75.506 1.00 60.82  ? 326 LEU   B CB   1 
ATOM   6211 C CG   . LEU   B 1 326 ? 0.965   4.659   -74.406 1.00 59.97  ? 326 LEU   B CG   1 
ATOM   6212 C CD1  . LEU   B 1 326 ? 1.607   4.340   -73.079 1.00 60.05  ? 326 LEU   B CD1  1 
ATOM   6213 C CD2  . LEU   B 1 326 ? 1.195   6.132   -74.752 1.00 60.97  ? 326 LEU   B CD2  1 
ATOM   6214 N N    . THR   B 1 327 ? 2.852   2.962   -78.611 1.00 68.80  ? 327 THR   B N    1 
ATOM   6215 C CA   . THR   B 1 327 ? 3.161   1.911   -79.578 1.00 75.10  ? 327 THR   B CA   1 
ATOM   6216 C C    . THR   B 1 327 ? 4.152   0.886   -79.037 1.00 74.84  ? 327 THR   B C    1 
ATOM   6217 O O    . THR   B 1 327 ? 3.896   -0.321  -79.106 1.00 78.06  ? 327 THR   B O    1 
ATOM   6218 C CB   . THR   B 1 327 ? 3.708   2.503   -80.895 1.00 77.35  ? 327 THR   B CB   1 
ATOM   6219 O OG1  . THR   B 1 327 ? 4.829   3.349   -80.620 1.00 78.46  ? 327 THR   B OG1  1 
ATOM   6220 C CG2  . THR   B 1 327 ? 2.641   3.314   -81.630 1.00 72.29  ? 327 THR   B CG2  1 
ATOM   6221 N N    . GLY   B 1 328 ? 5.284   1.341   -78.514 1.00 68.74  ? 328 GLY   B N    1 
ATOM   6222 C CA   . GLY   B 1 328 ? 6.284   0.426   -78.007 1.00 68.82  ? 328 GLY   B CA   1 
ATOM   6223 C C    . GLY   B 1 328 ? 5.868   -0.259  -76.719 1.00 70.94  ? 328 GLY   B C    1 
ATOM   6224 O O    . GLY   B 1 328 ? 4.956   0.162   -76.006 1.00 69.36  ? 328 GLY   B O    1 
ATOM   6225 N N    . VAL   B 1 329 ? 6.538   -1.380  -76.440 1.00 82.05  ? 329 VAL   B N    1 
ATOM   6226 C CA   . VAL   B 1 329 ? 6.407   -2.009  -75.133 1.00 78.42  ? 329 VAL   B CA   1 
ATOM   6227 C C    . VAL   B 1 329 ? 6.970   -1.103  -74.039 1.00 79.78  ? 329 VAL   B C    1 
ATOM   6228 O O    . VAL   B 1 329 ? 6.672   -1.292  -72.852 1.00 76.18  ? 329 VAL   B O    1 
ATOM   6229 C CB   . VAL   B 1 329 ? 7.094   -3.392  -75.157 1.00 78.37  ? 329 VAL   B CB   1 
ATOM   6230 C CG1  . VAL   B 1 329 ? 8.597   -3.250  -74.968 1.00 75.56  ? 329 VAL   B CG1  1 
ATOM   6231 C CG2  . VAL   B 1 329 ? 6.475   -4.321  -74.115 1.00 81.04  ? 329 VAL   B CG2  1 
ATOM   6232 N N    . ALA   B 1 330 ? 7.781   -0.114  -74.418 1.00 73.46  ? 330 ALA   B N    1 
ATOM   6233 C CA   . ALA   B 1 330 ? 8.230   0.933   -73.512 1.00 73.95  ? 330 ALA   B CA   1 
ATOM   6234 C C    . ALA   B 1 330 ? 8.445   2.211   -74.314 1.00 72.37  ? 330 ALA   B C    1 
ATOM   6235 O O    . ALA   B 1 330 ? 8.691   2.173   -75.523 1.00 76.63  ? 330 ALA   B O    1 
ATOM   6236 C CB   . ALA   B 1 330 ? 9.505   0.532   -72.758 1.00 73.22  ? 330 ALA   B CB   1 
ATOM   6237 N N    . GLY   B 1 331 ? 8.360   3.345   -73.628 1.00 62.08  ? 331 GLY   B N    1 
ATOM   6238 C CA   . GLY   B 1 331 ? 8.474   4.623   -74.313 1.00 62.41  ? 331 GLY   B CA   1 
ATOM   6239 C C    . GLY   B 1 331 ? 8.440   5.811   -73.370 1.00 66.11  ? 331 GLY   B C    1 
ATOM   6240 O O    . GLY   B 1 331 ? 8.129   5.692   -72.174 1.00 63.68  ? 331 GLY   B O    1 
ATOM   6241 N N    . ASN   B 1 332 ? 8.798   6.965   -73.942 1.00 73.19  ? 332 ASN   B N    1 
ATOM   6242 C CA   . ASN   B 1 332 ? 8.693   8.282   -73.319 1.00 73.74  ? 332 ASN   B CA   1 
ATOM   6243 C C    . ASN   B 1 332 ? 7.825   9.162   -74.214 1.00 74.25  ? 332 ASN   B C    1 
ATOM   6244 O O    . ASN   B 1 332 ? 8.196   9.431   -75.361 1.00 72.41  ? 332 ASN   B O    1 
ATOM   6245 C CB   . ASN   B 1 332 ? 10.079  8.919   -73.131 1.00 71.71  ? 332 ASN   B CB   1 
ATOM   6246 C CG   . ASN   B 1 332 ? 10.985  8.116   -72.205 1.00 71.25  ? 332 ASN   B CG   1 
ATOM   6247 O OD1  . ASN   B 1 332 ? 10.656  7.914   -71.034 1.00 73.87  ? 332 ASN   B OD1  1 
ATOM   6248 N ND2  . ASN   B 1 332 ? 12.140  7.682   -72.713 1.00 70.69  ? 332 ASN   B ND2  1 
ATOM   6249 N N    . TYR   B 1 333 ? 6.683   9.622   -73.687 1.00 69.54  ? 333 TYR   B N    1 
ATOM   6250 C CA   . TYR   B 1 333 ? 5.699   10.377  -74.457 1.00 69.16  ? 333 TYR   B CA   1 
ATOM   6251 C C    . TYR   B 1 333 ? 5.303   11.674  -73.754 1.00 68.63  ? 333 TYR   B C    1 
ATOM   6252 O O    . TYR   B 1 333 ? 5.220   11.731  -72.526 1.00 68.62  ? 333 TYR   B O    1 
ATOM   6253 C CB   . TYR   B 1 333 ? 4.427   9.540   -74.701 1.00 65.41  ? 333 TYR   B CB   1 
ATOM   6254 C CG   . TYR   B 1 333 ? 4.552   8.510   -75.807 1.00 73.00  ? 333 TYR   B CG   1 
ATOM   6255 C CD1  . TYR   B 1 333 ? 4.314   8.848   -77.144 1.00 71.15  ? 333 TYR   B CD1  1 
ATOM   6256 C CD2  . TYR   B 1 333 ? 4.903   7.198   -75.517 1.00 70.35  ? 333 TYR   B CD2  1 
ATOM   6257 C CE1  . TYR   B 1 333 ? 4.425   7.898   -78.150 1.00 70.78  ? 333 TYR   B CE1  1 
ATOM   6258 C CE2  . TYR   B 1 333 ? 5.015   6.250   -76.514 1.00 69.91  ? 333 TYR   B CE2  1 
ATOM   6259 C CZ   . TYR   B 1 333 ? 4.778   6.598   -77.822 1.00 70.90  ? 333 TYR   B CZ   1 
ATOM   6260 O OH   . TYR   B 1 333 ? 4.906   5.620   -78.777 1.00 70.57  ? 333 TYR   B OH   1 
ATOM   6261 N N    . THR   B 1 334 ? 5.049   12.721  -74.555 1.00 63.11  ? 334 THR   B N    1 
ATOM   6262 C CA   . THR   B 1 334 ? 4.451   13.967  -74.078 1.00 60.46  ? 334 THR   B CA   1 
ATOM   6263 C C    . THR   B 1 334 ? 3.253   14.335  -74.951 1.00 63.28  ? 334 THR   B C    1 
ATOM   6264 O O    . THR   B 1 334 ? 3.337   14.280  -76.183 1.00 65.53  ? 334 THR   B O    1 
ATOM   6265 C CB   . THR   B 1 334 ? 5.450   15.139  -74.110 1.00 62.13  ? 334 THR   B CB   1 
ATOM   6266 O OG1  . THR   B 1 334 ? 6.575   14.860  -73.262 1.00 63.53  ? 334 THR   B OG1  1 
ATOM   6267 C CG2  . THR   B 1 334 ? 4.772   16.423  -73.631 1.00 62.06  ? 334 THR   B CG2  1 
ATOM   6268 N N    . VAL   B 1 335 ? 2.152   14.741  -74.307 1.00 65.92  ? 335 VAL   B N    1 
ATOM   6269 C CA   . VAL   B 1 335 ? 0.929   15.175  -74.993 1.00 67.02  ? 335 VAL   B CA   1 
ATOM   6270 C C    . VAL   B 1 335 ? 0.320   16.331  -74.202 1.00 68.39  ? 335 VAL   B C    1 
ATOM   6271 O O    . VAL   B 1 335 ? 0.329   16.319  -72.967 1.00 62.55  ? 335 VAL   B O    1 
ATOM   6272 C CB   . VAL   B 1 335 ? -0.095  14.029  -75.188 1.00 62.84  ? 335 VAL   B CB   1 
ATOM   6273 C CG1  . VAL   B 1 335 ? -0.476  13.406  -73.879 1.00 62.16  ? 335 VAL   B CG1  1 
ATOM   6274 C CG2  . VAL   B 1 335 ? -1.345  14.540  -75.911 1.00 65.03  ? 335 VAL   B CG2  1 
ATOM   6275 N N    . CYS   B 1 336 ? -0.195  17.340  -74.908 1.00 67.38  ? 336 CYS   B N    1 
ATOM   6276 C CA   . CYS   B 1 336 ? -0.664  18.572  -74.284 1.00 64.27  ? 336 CYS   B CA   1 
ATOM   6277 C C    . CYS   B 1 336 ? -2.066  18.921  -74.759 1.00 63.88  ? 336 CYS   B C    1 
ATOM   6278 O O    . CYS   B 1 336 ? -2.507  18.509  -75.830 1.00 65.34  ? 336 CYS   B O    1 
ATOM   6279 C CB   . CYS   B 1 336 ? 0.258   19.758  -74.599 1.00 66.46  ? 336 CYS   B CB   1 
ATOM   6280 S SG   . CYS   B 1 336 ? 1.990   19.466  -74.253 1.00 69.15  ? 336 CYS   B SG   1 
ATOM   6281 N N    . GLN   B 1 337 ? -2.768  19.680  -73.924 1.00 61.81  ? 337 GLN   B N    1 
ATOM   6282 C CA   . GLN   B 1 337 ? -4.009  20.329  -74.325 1.00 63.68  ? 337 GLN   B CA   1 
ATOM   6283 C C    . GLN   B 1 337 ? -4.110  21.635  -73.554 1.00 65.80  ? 337 GLN   B C    1 
ATOM   6284 O O    . GLN   B 1 337 ? -4.005  21.636  -72.320 1.00 64.54  ? 337 GLN   B O    1 
ATOM   6285 C CB   . GLN   B 1 337 ? -5.233  19.445  -74.057 1.00 61.43  ? 337 GLN   B CB   1 
ATOM   6286 C CG   . GLN   B 1 337 ? -6.544  20.017  -74.590 1.00 63.61  ? 337 GLN   B CG   1 
ATOM   6287 C CD   . GLN   B 1 337 ? -7.746  19.175  -74.201 1.00 61.88  ? 337 GLN   B CD   1 
ATOM   6288 O OE1  . GLN   B 1 337 ? -8.379  19.410  -73.155 1.00 59.32  ? 337 GLN   B OE1  1 
ATOM   6289 N NE2  . GLN   B 1 337 ? -8.071  18.184  -75.041 1.00 61.06  ? 337 GLN   B NE2  1 
ATOM   6290 N N    . LYS   B 1 338 ? -4.297  22.734  -74.285 1.00 69.66  ? 338 LYS   B N    1 
ATOM   6291 C CA   . LYS   B 1 338 ? -4.322  24.078  -73.722 1.00 71.00  ? 338 LYS   B CA   1 
ATOM   6292 C C    . LYS   B 1 338 ? -3.164  24.315  -72.754 1.00 70.59  ? 338 LYS   B C    1 
ATOM   6293 O O    . LYS   B 1 338 ? -2.007  24.376  -73.180 1.00 74.23  ? 338 LYS   B O    1 
ATOM   6294 C CB   . LYS   B 1 338 ? -5.668  24.337  -73.045 1.00 72.85  ? 338 LYS   B CB   1 
ATOM   6295 C CG   . LYS   B 1 338 ? -6.867  24.163  -73.990 1.00 72.62  ? 338 LYS   B CG   1 
ATOM   6296 C CD   . LYS   B 1 338 ? -7.950  25.208  -73.720 1.00 79.79  ? 338 LYS   B CD   1 
ATOM   6297 C CE   . LYS   B 1 338 ? -8.803  24.843  -72.505 1.00 74.13  ? 338 LYS   B CE   1 
ATOM   6298 N NZ   . LYS   B 1 338 ? -9.927  23.955  -72.924 1.00 74.56  ? 338 LYS   B NZ   1 
ATOM   6299 N N    . ASP   B 1 339 ? -3.447  24.454  -71.461 1.00 75.37  ? 339 ASP   B N    1 
ATOM   6300 C CA   . ASP   B 1 339 ? -2.415  24.808  -70.492 1.00 76.53  ? 339 ASP   B CA   1 
ATOM   6301 C C    . ASP   B 1 339 ? -1.719  23.602  -69.873 1.00 73.46  ? 339 ASP   B C    1 
ATOM   6302 O O    . ASP   B 1 339 ? -0.769  23.776  -69.099 1.00 72.26  ? 339 ASP   B O    1 
ATOM   6303 C CB   . ASP   B 1 339 ? -3.012  25.670  -69.375 1.00 76.00  ? 339 ASP   B CB   1 
ATOM   6304 C CG   . ASP   B 1 339 ? -3.503  27.009  -69.876 1.00 80.80  ? 339 ASP   B CG   1 
ATOM   6305 O OD1  . ASP   B 1 339 ? -2.852  27.579  -70.778 1.00 84.35  ? 339 ASP   B OD1  1 
ATOM   6306 O OD2  . ASP   B 1 339 ? -4.541  27.487  -69.372 1.00 80.22  ? 339 ASP   B OD2  1 
ATOM   6307 N N    . LEU   B 1 340 ? -2.151  22.392  -70.194 1.00 60.76  ? 340 LEU   B N    1 
ATOM   6308 C CA   . LEU   B 1 340 ? -1.696  21.202  -69.492 1.00 59.34  ? 340 LEU   B CA   1 
ATOM   6309 C C    . LEU   B 1 340 ? -0.842  20.343  -70.415 1.00 59.58  ? 340 LEU   B C    1 
ATOM   6310 O O    . LEU   B 1 340 ? -1.319  19.891  -71.457 1.00 60.86  ? 340 LEU   B O    1 
ATOM   6311 C CB   . LEU   B 1 340 ? -2.896  20.404  -68.987 1.00 52.53  ? 340 LEU   B CB   1 
ATOM   6312 C CG   . LEU   B 1 340 ? -2.544  19.128  -68.229 1.00 53.53  ? 340 LEU   B CG   1 
ATOM   6313 C CD1  . LEU   B 1 340 ? -2.146  19.476  -66.762 1.00 54.63  ? 340 LEU   B CD1  1 
ATOM   6314 C CD2  . LEU   B 1 340 ? -3.720  18.145  -68.287 1.00 50.83  ? 340 LEU   B CD2  1 
ATOM   6315 N N    . CYS   B 1 341 ? 0.393   20.067  -70.012 1.00 69.98  ? 341 CYS   B N    1 
ATOM   6316 C CA   . CYS   B 1 341 ? 1.217   19.090  -70.706 1.00 70.02  ? 341 CYS   B CA   1 
ATOM   6317 C C    . CYS   B 1 341 ? 1.478   17.906  -69.786 1.00 71.72  ? 341 CYS   B C    1 
ATOM   6318 O O    . CYS   B 1 341 ? 1.757   18.078  -68.593 1.00 69.97  ? 341 CYS   B O    1 
ATOM   6319 C CB   . CYS   B 1 341 ? 2.546   19.677  -71.182 1.00 72.88  ? 341 CYS   B CB   1 
ATOM   6320 S SG   . CYS   B 1 341 ? 2.455   20.693  -72.679 1.00 80.26  ? 341 CYS   B SG   1 
ATOM   6321 N N    . CYS   B 1 342 ? 1.389   16.708  -70.359 1.00 65.60  ? 342 CYS   B N    1 
ATOM   6322 C CA   . CYS   B 1 342 ? 1.491   15.445  -69.651 1.00 63.34  ? 342 CYS   B CA   1 
ATOM   6323 C C    . CYS   B 1 342 ? 2.664   14.645  -70.198 1.00 65.65  ? 342 CYS   B C    1 
ATOM   6324 O O    . CYS   B 1 342 ? 2.765   14.433  -71.415 1.00 67.25  ? 342 CYS   B O    1 
ATOM   6325 C CB   . CYS   B 1 342 ? 0.193   14.653  -69.806 1.00 59.57  ? 342 CYS   B CB   1 
ATOM   6326 S SG   . CYS   B 1 342 ? -1.287  15.568  -69.331 1.00 61.00  ? 342 CYS   B SG   1 
ATOM   6327 N N    . HIS   B 1 343 ? 3.534   14.199  -69.293 1.00 80.93  ? 343 HIS   B N    1 
ATOM   6328 C CA   . HIS   B 1 343 ? 4.698   13.382  -69.602 1.00 80.98  ? 343 HIS   B CA   1 
ATOM   6329 C C    . HIS   B 1 343 ? 4.507   11.998  -68.994 1.00 82.87  ? 343 HIS   B C    1 
ATOM   6330 O O    . HIS   B 1 343 ? 4.123   11.874  -67.822 1.00 79.86  ? 343 HIS   B O    1 
ATOM   6331 C CB   . HIS   B 1 343 ? 5.986   14.005  -69.049 1.00 83.29  ? 343 HIS   B CB   1 
ATOM   6332 C CG   . HIS   B 1 343 ? 6.165   15.456  -69.382 1.00 84.73  ? 343 HIS   B CG   1 
ATOM   6333 N ND1  . HIS   B 1 343 ? 6.012   15.954  -70.658 1.00 87.46  ? 343 HIS   B ND1  1 
ATOM   6334 C CD2  . HIS   B 1 343 ? 6.501   16.512  -68.604 1.00 86.59  ? 343 HIS   B CD2  1 
ATOM   6335 C CE1  . HIS   B 1 343 ? 6.240   17.255  -70.650 1.00 87.01  ? 343 HIS   B CE1  1 
ATOM   6336 N NE2  . HIS   B 1 343 ? 6.537   17.620  -69.416 1.00 85.41  ? 343 HIS   B NE2  1 
ATOM   6337 N N    . LEU   B 1 344 ? 4.784   10.964  -69.785 1.00 61.41  ? 344 LEU   B N    1 
ATOM   6338 C CA   . LEU   B 1 344 ? 4.730   9.588   -69.317 1.00 60.25  ? 344 LEU   B CA   1 
ATOM   6339 C C    . LEU   B 1 344 ? 5.992   8.872   -69.758 1.00 63.44  ? 344 LEU   B C    1 
ATOM   6340 O O    . LEU   B 1 344 ? 6.416   8.992   -70.912 1.00 66.16  ? 344 LEU   B O    1 
ATOM   6341 C CB   . LEU   B 1 344 ? 3.501   8.838   -69.850 1.00 58.80  ? 344 LEU   B CB   1 
ATOM   6342 C CG   . LEU   B 1 344 ? 3.498   7.346   -69.506 1.00 56.62  ? 344 LEU   B CG   1 
ATOM   6343 C CD1  . LEU   B 1 344 ? 3.207   7.188   -68.017 1.00 57.16  ? 344 LEU   B CD1  1 
ATOM   6344 C CD2  . LEU   B 1 344 ? 2.488   6.577   -70.340 1.00 56.99  ? 344 LEU   B CD2  1 
ATOM   6345 N N    . SER   B 1 345 ? 6.586   8.132   -68.842 1.00 59.19  ? 345 SER   B N    1 
ATOM   6346 C CA   . SER   B 1 345 ? 7.627   7.181   -69.173 1.00 59.46  ? 345 SER   B CA   1 
ATOM   6347 C C    . SER   B 1 345 ? 7.157   5.824   -68.668 1.00 61.62  ? 345 SER   B C    1 
ATOM   6348 O O    . SER   B 1 345 ? 6.495   5.744   -67.626 1.00 62.73  ? 345 SER   B O    1 
ATOM   6349 C CB   . SER   B 1 345 ? 8.954   7.632   -68.574 1.00 61.79  ? 345 SER   B CB   1 
ATOM   6350 O OG   . SER   B 1 345 ? 9.785   6.551   -68.238 1.00 69.08  ? 345 SER   B OG   1 
ATOM   6351 N N    . TYR   B 1 346 ? 7.393   4.769   -69.448 1.00 63.88  ? 346 TYR   B N    1 
ATOM   6352 C CA   . TYR   B 1 346 ? 6.747   3.508   -69.103 1.00 62.52  ? 346 TYR   B CA   1 
ATOM   6353 C C    . TYR   B 1 346 ? 7.470   2.327   -69.732 1.00 67.53  ? 346 TYR   B C    1 
ATOM   6354 O O    . TYR   B 1 346 ? 8.008   2.424   -70.842 1.00 67.29  ? 346 TYR   B O    1 
ATOM   6355 C CB   . TYR   B 1 346 ? 5.286   3.497   -69.567 1.00 64.60  ? 346 TYR   B CB   1 
ATOM   6356 C CG   . TYR   B 1 346 ? 5.165   3.288   -71.069 1.00 66.85  ? 346 TYR   B CG   1 
ATOM   6357 C CD1  . TYR   B 1 346 ? 5.376   4.341   -71.954 1.00 62.97  ? 346 TYR   B CD1  1 
ATOM   6358 C CD2  . TYR   B 1 346 ? 4.875   2.030   -71.599 1.00 66.52  ? 346 TYR   B CD2  1 
ATOM   6359 C CE1  . TYR   B 1 346 ? 5.284   4.148   -73.324 1.00 67.83  ? 346 TYR   B CE1  1 
ATOM   6360 C CE2  . TYR   B 1 346 ? 4.783   1.830   -72.961 1.00 65.81  ? 346 TYR   B CE2  1 
ATOM   6361 C CZ   . TYR   B 1 346 ? 4.988   2.892   -73.816 1.00 65.69  ? 346 TYR   B CZ   1 
ATOM   6362 O OH   . TYR   B 1 346 ? 4.896   2.705   -75.168 1.00 66.41  ? 346 TYR   B OH   1 
ATOM   6363 N N    . LYS   B 1 347 ? 7.464   1.210   -69.005 1.00 69.92  ? 347 LYS   B N    1 
ATOM   6364 C CA   . LYS   B 1 347 ? 7.864   -0.089  -69.531 1.00 71.71  ? 347 LYS   B CA   1 
ATOM   6365 C C    . LYS   B 1 347 ? 6.813   -1.103  -69.102 1.00 72.49  ? 347 LYS   B C    1 
ATOM   6366 O O    . LYS   B 1 347 ? 6.559   -1.258  -67.900 1.00 71.26  ? 347 LYS   B O    1 
ATOM   6367 C CB   . LYS   B 1 347 ? 9.257   -0.509  -69.046 1.00 69.35  ? 347 LYS   B CB   1 
ATOM   6368 C CG   . LYS   B 1 347 ? 9.665   -1.898  -69.540 1.00 73.39  ? 347 LYS   B CG   1 
ATOM   6369 C CD   . LYS   B 1 347 ? 10.510  -2.654  -68.517 1.00 74.66  ? 347 LYS   B CD   1 
ATOM   6370 C CE   . LYS   B 1 347 ? 11.439  -3.658  -69.213 1.00 75.76  ? 347 LYS   B CE   1 
ATOM   6371 N NZ   . LYS   B 1 347 ? 11.492  -4.991  -68.533 1.00 75.66  ? 347 LYS   B NZ   1 
ATOM   6372 N N    . MET   B 1 348 ? 6.186   -1.763  -70.078 1.00 66.91  ? 348 MET   B N    1 
ATOM   6373 C CA   . MET   B 1 348 ? 5.226   -2.824  -69.811 1.00 67.12  ? 348 MET   B CA   1 
ATOM   6374 C C    . MET   B 1 348 ? 5.936   -4.158  -69.617 1.00 70.62  ? 348 MET   B C    1 
ATOM   6375 O O    . MET   B 1 348 ? 6.997   -4.410  -70.196 1.00 73.26  ? 348 MET   B O    1 
ATOM   6376 C CB   . MET   B 1 348 ? 4.216   -2.947  -70.950 1.00 67.62  ? 348 MET   B CB   1 
ATOM   6377 C CG   . MET   B 1 348 ? 3.911   -1.648  -71.654 1.00 68.30  ? 348 MET   B CG   1 
ATOM   6378 S SD   . MET   B 1 348 ? 2.730   -1.929  -72.990 1.00 72.15  ? 348 MET   B SD   1 
ATOM   6379 C CE   . MET   B 1 348 ? 2.099   -0.263  -73.229 1.00 65.07  ? 348 MET   B CE   1 
ATOM   6380 N N    . SER   B 1 349 ? 5.333   -5.019  -68.790 1.00 72.76  ? 349 SER   B N    1 
ATOM   6381 C CA   . SER   B 1 349 ? 5.876   -6.356  -68.554 1.00 71.26  ? 349 SER   B CA   1 
ATOM   6382 C C    . SER   B 1 349 ? 5.781   -7.256  -69.772 1.00 71.34  ? 349 SER   B C    1 
ATOM   6383 O O    . SER   B 1 349 ? 6.531   -8.233  -69.867 1.00 72.25  ? 349 SER   B O    1 
ATOM   6384 C CB   . SER   B 1 349 ? 5.155   -7.023  -67.386 1.00 71.14  ? 349 SER   B CB   1 
ATOM   6385 O OG   . SER   B 1 349 ? 5.217   -6.201  -66.245 1.00 73.54  ? 349 SER   B OG   1 
ATOM   6386 N N    . GLU   B 1 350 ? 4.861   -6.966  -70.685 1.00 82.14  ? 350 GLU   B N    1 
ATOM   6387 C CA   . GLU   B 1 350 ? 4.562   -7.852  -71.794 1.00 82.18  ? 350 GLU   B CA   1 
ATOM   6388 C C    . GLU   B 1 350 ? 4.059   -7.019  -72.961 1.00 83.16  ? 350 GLU   B C    1 
ATOM   6389 O O    . GLU   B 1 350 ? 3.517   -5.925  -72.780 1.00 82.69  ? 350 GLU   B O    1 
ATOM   6390 C CB   . GLU   B 1 350 ? 3.507   -8.890  -71.404 1.00 82.58  ? 350 GLU   B CB   1 
ATOM   6391 C CG   . GLU   B 1 350 ? 4.031   -10.280 -71.148 1.00 83.30  ? 350 GLU   B CG   1 
ATOM   6392 C CD   . GLU   B 1 350 ? 2.901   -11.241 -70.864 1.00 87.12  ? 350 GLU   B CD   1 
ATOM   6393 O OE1  . GLU   B 1 350 ? 1.995   -10.861 -70.091 1.00 92.34  ? 350 GLU   B OE1  1 
ATOM   6394 O OE2  . GLU   B 1 350 ? 2.900   -12.357 -71.425 1.00 88.55  ? 350 GLU   B OE2  1 
ATOM   6395 N N    . ASN   B 1 351 ? 4.229   -7.552  -74.169 1.00 92.16  ? 351 ASN   B N    1 
ATOM   6396 C CA   . ASN   B 1 351 ? 3.637   -6.950  -75.360 1.00 93.04  ? 351 ASN   B CA   1 
ATOM   6397 C C    . ASN   B 1 351 ? 2.393   -7.771  -75.685 1.00 89.15  ? 351 ASN   B C    1 
ATOM   6398 O O    . ASN   B 1 351 ? 2.463   -8.829  -76.306 1.00 92.70  ? 351 ASN   B O    1 
ATOM   6399 C CB   . ASN   B 1 351 ? 4.634   -6.913  -76.514 1.00 91.65  ? 351 ASN   B CB   1 
ATOM   6400 C CG   . ASN   B 1 351 ? 3.957   -6.888  -77.880 1.00 95.44  ? 351 ASN   B CG   1 
ATOM   6401 O OD1  . ASN   B 1 351 ? 3.491   -7.915  -78.383 1.00 102.61 ? 351 ASN   B OD1  1 
ATOM   6402 N ND2  . ASN   B 1 351 ? 3.888   -5.704  -78.479 1.00 92.21  ? 351 ASN   B ND2  1 
ATOM   6403 N N    . ILE   B 1 352 ? 1.252   -7.318  -75.176 1.00 65.55  ? 352 ILE   B N    1 
ATOM   6404 C CA   . ILE   B 1 352 ? -0.049  -7.846  -75.579 1.00 62.99  ? 352 ILE   B CA   1 
ATOM   6405 C C    . ILE   B 1 352 ? -0.502  -7.056  -76.801 1.00 63.09  ? 352 ILE   B C    1 
ATOM   6406 O O    . ILE   B 1 352 ? -0.815  -5.856  -76.667 1.00 59.31  ? 352 ILE   B O    1 
ATOM   6407 C CB   . ILE   B 1 352 ? -1.077  -7.747  -74.447 1.00 66.48  ? 352 ILE   B CB   1 
ATOM   6408 C CG1  . ILE   B 1 352 ? -0.573  -8.495  -73.217 1.00 63.31  ? 352 ILE   B CG1  1 
ATOM   6409 C CG2  . ILE   B 1 352 ? -2.430  -8.286  -74.919 1.00 64.24  ? 352 ILE   B CG2  1 
ATOM   6410 C CD1  . ILE   B 1 352 ? -1.643  -8.768  -72.219 1.00 65.95  ? 352 ILE   B CD1  1 
ATOM   6411 N N    . PRO   B 1 353 ? -0.589  -7.682  -77.983 1.00 77.85  ? 353 PRO   B N    1 
ATOM   6412 C CA   . PRO   B 1 353 ? -0.882  -6.911  -79.204 1.00 76.58  ? 353 PRO   B CA   1 
ATOM   6413 C C    . PRO   B 1 353 ? -2.297  -6.369  -79.229 1.00 74.83  ? 353 PRO   B C    1 
ATOM   6414 O O    . PRO   B 1 353 ? -2.499  -5.196  -79.571 1.00 75.89  ? 353 PRO   B O    1 
ATOM   6415 C CB   . PRO   B 1 353 ? -0.623  -7.917  -80.340 1.00 75.77  ? 353 PRO   B CB   1 
ATOM   6416 C CG   . PRO   B 1 353 ? 0.036   -9.119  -79.683 1.00 77.74  ? 353 PRO   B CG   1 
ATOM   6417 C CD   . PRO   B 1 353 ? -0.388  -9.114  -78.256 1.00 76.63  ? 353 PRO   B CD   1 
ATOM   6418 N N    . ASN   B 1 354 ? -3.282  -7.185  -78.842 1.00 73.87  ? 354 ASN   B N    1 
ATOM   6419 C CA   . ASN   B 1 354 ? -4.695  -6.822  -78.875 1.00 73.65  ? 354 ASN   B CA   1 
ATOM   6420 C C    . ASN   B 1 354 ? -5.104  -5.910  -77.715 1.00 70.49  ? 354 ASN   B C    1 
ATOM   6421 O O    . ASN   B 1 354 ? -6.305  -5.719  -77.484 1.00 69.33  ? 354 ASN   B O    1 
ATOM   6422 C CB   . ASN   B 1 354 ? -5.549  -8.091  -78.819 1.00 75.01  ? 354 ASN   B CB   1 
ATOM   6423 C CG   . ASN   B 1 354 ? -5.417  -8.816  -77.473 1.00 81.17  ? 354 ASN   B CG   1 
ATOM   6424 O OD1  . ASN   B 1 354 ? -4.371  -9.409  -77.171 1.00 82.09  ? 354 ASN   B OD1  1 
ATOM   6425 N ND2  . ASN   B 1 354 ? -6.461  -8.736  -76.646 1.00 79.29  ? 354 ASN   B ND2  1 
ATOM   6426 N N    . GLU   B 1 355 ? -4.144  -5.309  -77.019 1.00 67.06  ? 355 GLU   B N    1 
ATOM   6427 C CA   . GLU   B 1 355 ? -4.414  -4.372  -75.935 1.00 62.97  ? 355 GLU   B CA   1 
ATOM   6428 C C    . GLU   B 1 355 ? -3.729  -3.055  -76.267 1.00 61.22  ? 355 GLU   B C    1 
ATOM   6429 O O    . GLU   B 1 355 ? -2.503  -3.015  -76.449 1.00 63.97  ? 355 GLU   B O    1 
ATOM   6430 C CB   . GLU   B 1 355 ? -3.928  -4.927  -74.598 1.00 61.29  ? 355 GLU   B CB   1 
ATOM   6431 C CG   . GLU   B 1 355 ? -4.948  -4.799  -73.478 1.00 68.31  ? 355 GLU   B CG   1 
ATOM   6432 C CD   . GLU   B 1 355 ? -4.495  -5.465  -72.180 1.00 67.23  ? 355 GLU   B CD   1 
ATOM   6433 O OE1  . GLU   B 1 355 ? -3.346  -5.224  -71.743 1.00 64.17  ? 355 GLU   B OE1  1 
ATOM   6434 O OE2  . GLU   B 1 355 ? -5.291  -6.236  -71.603 1.00 68.87  ? 355 GLU   B OE2  1 
ATOM   6435 N N    . VAL   B 1 356 ? -4.516  -1.982  -76.327 1.00 44.48  ? 356 VAL   B N    1 
ATOM   6436 C CA   . VAL   B 1 356 ? -4.044  -0.655  -76.714 1.00 44.89  ? 356 VAL   B CA   1 
ATOM   6437 C C    . VAL   B 1 356 ? -4.056  0.264   -75.496 1.00 47.97  ? 356 VAL   B C    1 
ATOM   6438 O O    . VAL   B 1 356 ? -5.047  0.317   -74.751 1.00 43.44  ? 356 VAL   B O    1 
ATOM   6439 C CB   . VAL   B 1 356 ? -4.905  -0.071  -77.845 1.00 43.57  ? 356 VAL   B CB   1 
ATOM   6440 C CG1  . VAL   B 1 356 ? -4.669  1.439   -77.980 1.00 42.20  ? 356 VAL   B CG1  1 
ATOM   6441 C CG2  . VAL   B 1 356 ? -4.610  -0.807  -79.165 1.00 45.46  ? 356 VAL   B CG2  1 
ATOM   6442 N N    . TYR   B 1 357 ? -2.943  0.961   -75.273 1.00 61.32  ? 357 TYR   B N    1 
ATOM   6443 C CA   . TYR   B 1 357 ? -2.837  1.972   -74.231 1.00 60.98  ? 357 TYR   B CA   1 
ATOM   6444 C C    . TYR   B 1 357 ? -2.637  3.352   -74.839 1.00 60.95  ? 357 TYR   B C    1 
ATOM   6445 O O    . TYR   B 1 357 ? -2.021  3.497   -75.897 1.00 64.01  ? 357 TYR   B O    1 
ATOM   6446 C CB   . TYR   B 1 357 ? -1.683  1.639   -73.279 1.00 62.84  ? 357 TYR   B CB   1 
ATOM   6447 C CG   . TYR   B 1 357 ? -2.097  0.573   -72.297 1.00 64.06  ? 357 TYR   B CG   1 
ATOM   6448 C CD1  . TYR   B 1 357 ? -1.996  -0.770  -72.626 1.00 62.82  ? 357 TYR   B CD1  1 
ATOM   6449 C CD2  . TYR   B 1 357 ? -2.648  0.911   -71.068 1.00 57.54  ? 357 TYR   B CD2  1 
ATOM   6450 C CE1  . TYR   B 1 357 ? -2.405  -1.752  -71.744 1.00 64.32  ? 357 TYR   B CE1  1 
ATOM   6451 C CE2  . TYR   B 1 357 ? -3.062  -0.063  -70.190 1.00 61.85  ? 357 TYR   B CE2  1 
ATOM   6452 C CZ   . TYR   B 1 357 ? -2.941  -1.397  -70.532 1.00 62.96  ? 357 TYR   B CZ   1 
ATOM   6453 O OH   . TYR   B 1 357 ? -3.340  -2.389  -69.659 1.00 67.54  ? 357 TYR   B OH   1 
ATOM   6454 N N    . ALA   B 1 358 ? -3.104  4.378   -74.135 1.00 54.33  ? 358 ALA   B N    1 
ATOM   6455 C CA   . ALA   B 1 358 ? -2.967  5.736   -74.636 1.00 52.45  ? 358 ALA   B CA   1 
ATOM   6456 C C    . ALA   B 1 358 ? -2.606  6.671   -73.493 1.00 53.08  ? 358 ALA   B C    1 
ATOM   6457 O O    . ALA   B 1 358 ? -2.880  6.395   -72.320 1.00 51.04  ? 358 ALA   B O    1 
ATOM   6458 C CB   . ALA   B 1 358 ? -4.244  6.214   -75.336 1.00 50.63  ? 358 ALA   B CB   1 
ATOM   6459 N N    . LEU   B 1 359 ? -1.965  7.781   -73.859 1.00 53.54  ? 359 LEU   B N    1 
ATOM   6460 C CA   . LEU   B 1 359 ? -1.675  8.878   -72.945 1.00 53.05  ? 359 LEU   B CA   1 
ATOM   6461 C C    . LEU   B 1 359 ? -2.530  10.062  -73.368 1.00 56.45  ? 359 LEU   B C    1 
ATOM   6462 O O    . LEU   B 1 359 ? -2.485  10.477  -74.539 1.00 55.07  ? 359 LEU   B O    1 
ATOM   6463 C CB   . LEU   B 1 359 ? -0.191  9.259   -72.967 1.00 54.29  ? 359 LEU   B CB   1 
ATOM   6464 C CG   . LEU   B 1 359 ? 0.158   10.555  -72.224 1.00 51.08  ? 359 LEU   B CG   1 
ATOM   6465 C CD1  . LEU   B 1 359 ? -0.274  10.444  -70.780 1.00 53.40  ? 359 LEU   B CD1  1 
ATOM   6466 C CD2  . LEU   B 1 359 ? 1.649   10.867  -72.309 1.00 52.83  ? 359 LEU   B CD2  1 
ATOM   6467 N N    . GLY   B 1 360 ? -3.307  10.590  -72.424 1.00 57.47  ? 360 GLY   B N    1 
ATOM   6468 C CA   . GLY   B 1 360 ? -4.300  11.599  -72.733 1.00 54.19  ? 360 GLY   B CA   1 
ATOM   6469 C C    . GLY   B 1 360 ? -4.211  12.780  -71.793 1.00 57.65  ? 360 GLY   B C    1 
ATOM   6470 O O    . GLY   B 1 360 ? -3.830  12.655  -70.624 1.00 56.65  ? 360 GLY   B O    1 
ATOM   6471 N N    . ALA   B 1 361 ? -4.561  13.942  -72.333 1.00 54.16  ? 361 ALA   B N    1 
ATOM   6472 C CA   . ALA   B 1 361 ? -4.583  15.187  -71.582 1.00 53.54  ? 361 ALA   B CA   1 
ATOM   6473 C C    . ALA   B 1 361 ? -5.935  15.870  -71.751 1.00 54.63  ? 361 ALA   B C    1 
ATOM   6474 O O    . ALA   B 1 361 ? -6.500  15.909  -72.856 1.00 53.86  ? 361 ALA   B O    1 
ATOM   6475 C CB   . ALA   B 1 361 ? -3.459  16.129  -72.018 1.00 58.18  ? 361 ALA   B CB   1 
ATOM   6476 N N    . PHE   B 1 362 ? -6.454  16.382  -70.640 1.00 52.60  ? 362 PHE   B N    1 
ATOM   6477 C CA   . PHE   B 1 362 ? -7.670  17.177  -70.641 1.00 53.41  ? 362 PHE   B CA   1 
ATOM   6478 C C    . PHE   B 1 362 ? -7.472  18.422  -69.782 1.00 52.93  ? 362 PHE   B C    1 
ATOM   6479 O O    . PHE   B 1 362 ? -6.835  18.368  -68.729 1.00 51.41  ? 362 PHE   B O    1 
ATOM   6480 C CB   . PHE   B 1 362 ? -8.861  16.382  -70.116 1.00 50.31  ? 362 PHE   B CB   1 
ATOM   6481 C CG   . PHE   B 1 362 ? -10.136 17.148  -70.165 1.00 51.29  ? 362 PHE   B CG   1 
ATOM   6482 C CD1  . PHE   B 1 362 ? -10.662 17.547  -71.390 1.00 52.14  ? 362 PHE   B CD1  1 
ATOM   6483 C CD2  . PHE   B 1 362 ? -10.787 17.513  -69.009 1.00 48.75  ? 362 PHE   B CD2  1 
ATOM   6484 C CE1  . PHE   B 1 362 ? -11.840 18.270  -71.452 1.00 51.50  ? 362 PHE   B CE1  1 
ATOM   6485 C CE2  . PHE   B 1 362 ? -11.958 18.234  -69.060 1.00 50.59  ? 362 PHE   B CE2  1 
ATOM   6486 C CZ   . PHE   B 1 362 ? -12.487 18.617  -70.279 1.00 52.36  ? 362 PHE   B CZ   1 
ATOM   6487 N N    . ASP   B 1 363 ? -8.004  19.545  -70.262 1.00 54.08  ? 363 ASP   B N    1 
ATOM   6488 C CA   . ASP   B 1 363 ? -7.919  20.839  -69.583 1.00 55.47  ? 363 ASP   B CA   1 
ATOM   6489 C C    . ASP   B 1 363 ? -9.181  21.610  -69.981 1.00 57.06  ? 363 ASP   B C    1 
ATOM   6490 O O    . ASP   B 1 363 ? -9.219  22.251  -71.033 1.00 56.58  ? 363 ASP   B O    1 
ATOM   6491 C CB   . ASP   B 1 363 ? -6.646  21.579  -69.972 1.00 56.80  ? 363 ASP   B CB   1 
ATOM   6492 C CG   . ASP   B 1 363 ? -6.493  22.918  -69.260 1.00 62.05  ? 363 ASP   B CG   1 
ATOM   6493 O OD1  . ASP   B 1 363 ? -7.421  23.332  -68.522 1.00 61.84  ? 363 ASP   B OD1  1 
ATOM   6494 O OD2  . ASP   B 1 363 ? -5.433  23.557  -69.439 1.00 63.74  ? 363 ASP   B OD2  1 
ATOM   6495 N N    . GLY   B 1 364 ? -10.214 21.515  -69.153 1.00 53.25  ? 364 GLY   B N    1 
ATOM   6496 C CA   . GLY   B 1 364 ? -11.464 22.153  -69.526 1.00 50.90  ? 364 GLY   B CA   1 
ATOM   6497 C C    . GLY   B 1 364 ? -12.550 21.877  -68.511 1.00 53.80  ? 364 GLY   B C    1 
ATOM   6498 O O    . GLY   B 1 364 ? -12.332 21.215  -67.491 1.00 53.38  ? 364 GLY   B O    1 
ATOM   6499 N N    . LEU   B 1 365 ? -13.748 22.350  -68.840 1.00 48.53  ? 365 LEU   B N    1 
ATOM   6500 C CA   . LEU   B 1 365 ? -14.882 22.321  -67.931 1.00 49.80  ? 365 LEU   B CA   1 
ATOM   6501 C C    . LEU   B 1 365 ? -15.725 21.076  -68.187 1.00 51.79  ? 365 LEU   B C    1 
ATOM   6502 O O    . LEU   B 1 365 ? -16.165 20.837  -69.317 1.00 48.45  ? 365 LEU   B O    1 
ATOM   6503 C CB   . LEU   B 1 365 ? -15.738 23.578  -68.084 1.00 51.03  ? 365 LEU   B CB   1 
ATOM   6504 C CG   . LEU   B 1 365 ? -16.920 23.597  -67.114 1.00 54.68  ? 365 LEU   B CG   1 
ATOM   6505 C CD1  . LEU   B 1 365 ? -16.517 24.229  -65.789 1.00 52.46  ? 365 LEU   B CD1  1 
ATOM   6506 C CD2  . LEU   B 1 365 ? -18.078 24.350  -67.736 1.00 54.81  ? 365 LEU   B CD2  1 
ATOM   6507 N N    . HIS   B 1 366 ? -15.906 20.264  -67.144 1.00 52.15  ? 366 HIS   B N    1 
ATOM   6508 C CA   . HIS   B 1 366 ? -16.880 19.191  -67.163 1.00 50.91  ? 366 HIS   B CA   1 
ATOM   6509 C C    . HIS   B 1 366 ? -18.270 19.768  -66.907 1.00 53.17  ? 366 HIS   B C    1 
ATOM   6510 O O    . HIS   B 1 366 ? -18.431 20.695  -66.106 1.00 54.65  ? 366 HIS   B O    1 
ATOM   6511 C CB   . HIS   B 1 366 ? -16.514 18.144  -66.114 1.00 47.44  ? 366 HIS   B CB   1 
ATOM   6512 C CG   . HIS   B 1 366 ? -17.387 16.938  -66.147 1.00 45.59  ? 366 HIS   B CG   1 
ATOM   6513 N ND1  . HIS   B 1 366 ? -17.036 15.783  -66.809 1.00 46.04  ? 366 HIS   B ND1  1 
ATOM   6514 C CD2  . HIS   B 1 366 ? -18.609 16.713  -65.613 1.00 48.43  ? 366 HIS   B CD2  1 
ATOM   6515 C CE1  . HIS   B 1 366 ? -18.004 14.895  -66.678 1.00 47.22  ? 366 HIS   B CE1  1 
ATOM   6516 N NE2  . HIS   B 1 366 ? -18.970 15.433  -65.955 1.00 46.31  ? 366 HIS   B NE2  1 
ATOM   6517 N N    . THR   B 1 367 ? -19.275 19.240  -67.622 1.00 49.59  ? 367 THR   B N    1 
ATOM   6518 C CA   . THR   B 1 367 ? -20.633 19.777  -67.553 1.00 50.85  ? 367 THR   B CA   1 
ATOM   6519 C C    . THR   B 1 367 ? -21.720 18.727  -67.364 1.00 49.75  ? 367 THR   B C    1 
ATOM   6520 O O    . THR   B 1 367 ? -22.858 19.107  -67.084 1.00 53.79  ? 367 THR   B O    1 
ATOM   6521 C CB   . THR   B 1 367 ? -20.979 20.578  -68.829 1.00 53.47  ? 367 THR   B CB   1 
ATOM   6522 O OG1  . THR   B 1 367 ? -20.848 19.735  -69.981 1.00 56.74  ? 367 THR   B OG1  1 
ATOM   6523 C CG2  . THR   B 1 367 ? -20.067 21.797  -69.005 1.00 54.26  ? 367 THR   B CG2  1 
ATOM   6524 N N    . VAL   B 1 368 ? -21.421 17.439  -67.498 1.00 51.01  ? 368 VAL   B N    1 
ATOM   6525 C CA   . VAL   B 1 368 ? -22.440 16.392  -67.470 1.00 53.15  ? 368 VAL   B CA   1 
ATOM   6526 C C    . VAL   B 1 368 ? -22.562 15.838  -66.053 1.00 54.95  ? 368 VAL   B C    1 
ATOM   6527 O O    . VAL   B 1 368 ? -21.572 15.378  -65.473 1.00 53.90  ? 368 VAL   B O    1 
ATOM   6528 C CB   . VAL   B 1 368 ? -22.106 15.281  -68.479 1.00 52.70  ? 368 VAL   B CB   1 
ATOM   6529 C CG1  . VAL   B 1 368 ? -23.160 14.173  -68.462 1.00 49.12  ? 368 VAL   B CG1  1 
ATOM   6530 C CG2  . VAL   B 1 368 ? -21.988 15.881  -69.847 1.00 50.15  ? 368 VAL   B CG2  1 
ATOM   6531 N N    . GLU   B 1 369 ? -23.770 15.905  -65.487 1.00 70.70  ? 369 GLU   B N    1 
ATOM   6532 C CA   . GLU   B 1 369 ? -24.027 15.545  -64.088 1.00 69.54  ? 369 GLU   B CA   1 
ATOM   6533 C C    . GLU   B 1 369 ? -22.983 16.167  -63.168 1.00 71.55  ? 369 GLU   B C    1 
ATOM   6534 O O    . GLU   B 1 369 ? -22.309 15.492  -62.383 1.00 70.87  ? 369 GLU   B O    1 
ATOM   6535 C CB   . GLU   B 1 369 ? -24.058 14.033  -63.897 1.00 71.09  ? 369 GLU   B CB   1 
ATOM   6536 C CG   . GLU   B 1 369 ? -25.086 13.315  -64.716 1.00 72.38  ? 369 GLU   B CG   1 
ATOM   6537 C CD   . GLU   B 1 369 ? -24.819 11.830  -64.739 1.00 75.80  ? 369 GLU   B CD   1 
ATOM   6538 O OE1  . GLU   B 1 369 ? -24.532 11.263  -63.655 1.00 78.17  ? 369 GLU   B OE1  1 
ATOM   6539 O OE2  . GLU   B 1 369 ? -24.854 11.243  -65.841 1.00 73.21  ? 369 GLU   B OE2  1 
ATOM   6540 N N    . GLY   B 1 370 ? -22.879 17.484  -63.262 1.00 58.76  ? 370 GLY   B N    1 
ATOM   6541 C CA   . GLY   B 1 370 ? -21.895 18.208  -62.494 1.00 55.12  ? 370 GLY   B CA   1 
ATOM   6542 C C    . GLY   B 1 370 ? -21.069 19.111  -63.383 1.00 56.68  ? 370 GLY   B C    1 
ATOM   6543 O O    . GLY   B 1 370 ? -20.645 18.718  -64.477 1.00 53.15  ? 370 GLY   B O    1 
ATOM   6544 N N    . ARG   B 1 371 ? -20.860 20.338  -62.913 1.00 59.06  ? 371 ARG   B N    1 
ATOM   6545 C CA   . ARG   B 1 371 ? -20.040 21.341  -63.578 1.00 58.95  ? 371 ARG   B CA   1 
ATOM   6546 C C    . ARG   B 1 371 ? -18.770 21.530  -62.758 1.00 58.34  ? 371 ARG   B C    1 
ATOM   6547 O O    . ARG   B 1 371 ? -18.831 22.000  -61.619 1.00 55.13  ? 371 ARG   B O    1 
ATOM   6548 C CB   . ARG   B 1 371 ? -20.807 22.660  -63.699 1.00 60.68  ? 371 ARG   B CB   1 
ATOM   6549 C CG   . ARG   B 1 371 ? -20.120 23.718  -64.518 1.00 61.99  ? 371 ARG   B CG   1 
ATOM   6550 C CD   . ARG   B 1 371 ? -20.863 25.045  -64.422 1.00 68.97  ? 371 ARG   B CD   1 
ATOM   6551 N NE   . ARG   B 1 371 ? -19.990 26.190  -64.660 1.00 73.18  ? 371 ARG   B NE   1 
ATOM   6552 C CZ   . ARG   B 1 371 ? -20.153 27.047  -65.658 1.00 72.44  ? 371 ARG   B CZ   1 
ATOM   6553 N NH1  . ARG   B 1 371 ? -21.153 26.924  -66.515 1.00 70.67  ? 371 ARG   B NH1  1 
ATOM   6554 N NH2  . ARG   B 1 371 ? -19.288 28.049  -65.802 1.00 78.09  ? 371 ARG   B NH2  1 
ATOM   6555 N N    . TYR   B 1 372 ? -17.619 21.180  -63.333 1.00 52.32  ? 372 TYR   B N    1 
ATOM   6556 C CA   . TYR   B 1 372 ? -16.386 21.374  -62.583 1.00 51.00  ? 372 TYR   B CA   1 
ATOM   6557 C C    . TYR   B 1 372 ? -15.190 21.350  -63.517 1.00 49.67  ? 372 TYR   B C    1 
ATOM   6558 O O    . TYR   B 1 372 ? -15.131 20.532  -64.435 1.00 46.03  ? 372 TYR   B O    1 
ATOM   6559 C CB   . TYR   B 1 372 ? -16.206 20.310  -61.499 1.00 47.61  ? 372 TYR   B CB   1 
ATOM   6560 C CG   . TYR   B 1 372 ? -16.618 18.877  -61.835 1.00 46.77  ? 372 TYR   B CG   1 
ATOM   6561 C CD1  . TYR   B 1 372 ? -15.696 17.946  -62.361 1.00 44.43  ? 372 TYR   B CD1  1 
ATOM   6562 C CD2  . TYR   B 1 372 ? -17.907 18.426  -61.537 1.00 45.40  ? 372 TYR   B CD2  1 
ATOM   6563 C CE1  . TYR   B 1 372 ? -16.081 16.614  -62.624 1.00 44.39  ? 372 TYR   B CE1  1 
ATOM   6564 C CE2  . TYR   B 1 372 ? -18.297 17.113  -61.793 1.00 44.65  ? 372 TYR   B CE2  1 
ATOM   6565 C CZ   . TYR   B 1 372 ? -17.391 16.209  -62.332 1.00 46.02  ? 372 TYR   B CZ   1 
ATOM   6566 O OH   . TYR   B 1 372 ? -17.830 14.910  -62.545 1.00 45.92  ? 372 TYR   B OH   1 
ATOM   6567 N N    . TYR   B 1 373 ? -14.222 22.217  -63.250 1.00 52.40  ? 373 TYR   B N    1 
ATOM   6568 C CA   . TYR   B 1 373 ? -13.065 22.309  -64.124 1.00 53.89  ? 373 TYR   B CA   1 
ATOM   6569 C C    . TYR   B 1 373 ? -12.014 21.264  -63.770 1.00 53.11  ? 373 TYR   B C    1 
ATOM   6570 O O    . TYR   B 1 373 ? -11.660 21.083  -62.605 1.00 50.95  ? 373 TYR   B O    1 
ATOM   6571 C CB   . TYR   B 1 373 ? -12.455 23.707  -64.063 1.00 56.17  ? 373 TYR   B CB   1 
ATOM   6572 C CG   . TYR   B 1 373 ? -11.677 24.021  -65.312 1.00 55.21  ? 373 TYR   B CG   1 
ATOM   6573 C CD1  . TYR   B 1 373 ? -10.375 23.562  -65.470 1.00 55.98  ? 373 TYR   B CD1  1 
ATOM   6574 C CD2  . TYR   B 1 373 ? -12.248 24.746  -66.349 1.00 56.66  ? 373 TYR   B CD2  1 
ATOM   6575 C CE1  . TYR   B 1 373 ? -9.652  23.833  -66.620 1.00 57.41  ? 373 TYR   B CE1  1 
ATOM   6576 C CE2  . TYR   B 1 373 ? -11.530 25.023  -67.515 1.00 56.22  ? 373 TYR   B CE2  1 
ATOM   6577 C CZ   . TYR   B 1 373 ? -10.233 24.561  -67.639 1.00 56.91  ? 373 TYR   B CZ   1 
ATOM   6578 O OH   . TYR   B 1 373 ? -9.505  24.816  -68.778 1.00 55.87  ? 373 TYR   B OH   1 
ATOM   6579 N N    . LEU   B 1 374 ? -11.470 20.616  -64.801 1.00 51.56  ? 374 LEU   B N    1 
ATOM   6580 C CA   . LEU   B 1 374 ? -10.535 19.516  -64.638 1.00 48.78  ? 374 LEU   B CA   1 
ATOM   6581 C C    . LEU   B 1 374 ? -9.268  19.784  -65.432 1.00 51.26  ? 374 LEU   B C    1 
ATOM   6582 O O    . LEU   B 1 374 ? -9.312  20.358  -66.533 1.00 49.92  ? 374 LEU   B O    1 
ATOM   6583 C CB   . LEU   B 1 374 ? -11.128 18.189  -65.122 1.00 46.58  ? 374 LEU   B CB   1 
ATOM   6584 C CG   . LEU   B 1 374 ? -12.488 17.775  -64.567 1.00 47.48  ? 374 LEU   B CG   1 
ATOM   6585 C CD1  . LEU   B 1 374 ? -13.044 16.567  -65.328 1.00 41.94  ? 374 LEU   B CD1  1 
ATOM   6586 C CD2  . LEU   B 1 374 ? -12.408 17.510  -63.043 1.00 45.21  ? 374 LEU   B CD2  1 
ATOM   6587 N N    . GLN   B 1 375 ? -8.141  19.356  -64.858 1.00 56.34  ? 375 GLN   B N    1 
ATOM   6588 C CA   . GLN   B 1 375 ? -6.892  19.160  -65.591 1.00 55.42  ? 375 GLN   B CA   1 
ATOM   6589 C C    . GLN   B 1 375 ? -6.437  17.736  -65.298 1.00 53.52  ? 375 GLN   B C    1 
ATOM   6590 O O    . GLN   B 1 375 ? -6.154  17.394  -64.148 1.00 51.50  ? 375 GLN   B O    1 
ATOM   6591 C CB   . GLN   B 1 375 ? -5.822  20.178  -65.203 1.00 52.71  ? 375 GLN   B CB   1 
ATOM   6592 C CG   . GLN   B 1 375 ? -5.941  21.501  -65.937 1.00 57.95  ? 375 GLN   B CG   1 
ATOM   6593 C CD   . GLN   B 1 375 ? -4.792  22.442  -65.621 1.00 60.66  ? 375 GLN   B CD   1 
ATOM   6594 O OE1  . GLN   B 1 375 ? -3.939  22.130  -64.801 1.00 59.50  ? 375 GLN   B OE1  1 
ATOM   6595 N NE2  . GLN   B 1 375 ? -4.776  23.608  -66.261 1.00 63.81  ? 375 GLN   B NE2  1 
ATOM   6596 N N    . ILE   B 1 376 ? -6.402  16.892  -66.324 1.00 49.42  ? 376 ILE   B N    1 
ATOM   6597 C CA   . ILE   B 1 376 ? -6.158  15.466  -66.141 1.00 47.29  ? 376 ILE   B CA   1 
ATOM   6598 C C    . ILE   B 1 376 ? -5.044  15.006  -67.069 1.00 49.75  ? 376 ILE   B C    1 
ATOM   6599 O O    . ILE   B 1 376 ? -5.066  15.296  -68.278 1.00 49.37  ? 376 ILE   B O    1 
ATOM   6600 C CB   . ILE   B 1 376 ? -7.426  14.632  -66.384 1.00 43.85  ? 376 ILE   B CB   1 
ATOM   6601 C CG1  . ILE   B 1 376 ? -8.540  15.077  -65.431 1.00 43.68  ? 376 ILE   B CG1  1 
ATOM   6602 C CG2  . ILE   B 1 376 ? -7.092  13.156  -66.274 1.00 42.28  ? 376 ILE   B CG2  1 
ATOM   6603 C CD1  . ILE   B 1 376 ? -9.855  14.335  -65.607 1.00 41.66  ? 376 ILE   B CD1  1 
ATOM   6604 N N    . CYS   B 1 377 ? -4.080  14.280  -66.500 1.00 54.16  ? 377 CYS   B N    1 
ATOM   6605 C CA   . CYS   B 1 377 ? -3.087  13.532  -67.263 1.00 56.16  ? 377 CYS   B CA   1 
ATOM   6606 C C    . CYS   B 1 377 ? -3.337  12.053  -67.011 1.00 57.61  ? 377 CYS   B C    1 
ATOM   6607 O O    . CYS   B 1 377 ? -3.294  11.603  -65.863 1.00 54.35  ? 377 CYS   B O    1 
ATOM   6608 C CB   . CYS   B 1 377 ? -1.666  13.903  -66.845 1.00 56.99  ? 377 CYS   B CB   1 
ATOM   6609 S SG   . CYS   B 1 377 ? -1.170  15.569  -67.289 1.00 61.03  ? 377 CYS   B SG   1 
ATOM   6610 N N    . THR   B 1 378 ? -3.585  11.285  -68.068 1.00 50.23  ? 378 THR   B N    1 
ATOM   6611 C CA   . THR   B 1 378 ? -4.002  9.912   -67.826 1.00 51.41  ? 378 THR   B CA   1 
ATOM   6612 C C    . THR   B 1 378 ? -3.311  8.950   -68.782 1.00 52.47  ? 378 THR   B C    1 
ATOM   6613 O O    . THR   B 1 378 ? -3.387  9.111   -70.005 1.00 53.26  ? 378 THR   B O    1 
ATOM   6614 C CB   . THR   B 1 378 ? -5.528  9.795   -67.937 1.00 48.08  ? 378 THR   B CB   1 
ATOM   6615 O OG1  . THR   B 1 378 ? -5.951  8.523   -67.435 1.00 48.63  ? 378 THR   B OG1  1 
ATOM   6616 C CG2  . THR   B 1 378 ? -5.988  9.965   -69.386 1.00 48.96  ? 378 THR   B CG2  1 
ATOM   6617 N N    . LEU   B 1 379 ? -2.657  7.937   -68.221 1.00 48.94  ? 379 LEU   B N    1 
ATOM   6618 C CA   . LEU   B 1 379 ? -2.321  6.736   -68.969 1.00 49.45  ? 379 LEU   B CA   1 
ATOM   6619 C C    . LEU   B 1 379 ? -3.473  5.763   -68.767 1.00 49.27  ? 379 LEU   B C    1 
ATOM   6620 O O    . LEU   B 1 379 ? -3.887  5.518   -67.625 1.00 47.06  ? 379 LEU   B O    1 
ATOM   6621 C CB   . LEU   B 1 379 ? -1.002  6.127   -68.490 1.00 48.57  ? 379 LEU   B CB   1 
ATOM   6622 C CG   . LEU   B 1 379 ? -0.863  4.611   -68.670 1.00 50.87  ? 379 LEU   B CG   1 
ATOM   6623 C CD1  . LEU   B 1 379 ? -0.859  4.266   -70.155 1.00 52.12  ? 379 LEU   B CD1  1 
ATOM   6624 C CD2  . LEU   B 1 379 ? 0.403   4.078   -68.010 1.00 51.58  ? 379 LEU   B CD2  1 
ATOM   6625 N N    . LEU   B 1 380 ? -4.042  5.268   -69.864 1.00 50.54  ? 380 LEU   B N    1 
ATOM   6626 C CA   . LEU   B 1 380 ? -5.209  4.418   -69.710 1.00 50.47  ? 380 LEU   B CA   1 
ATOM   6627 C C    . LEU   B 1 380 ? -5.235  3.317   -70.753 1.00 52.05  ? 380 LEU   B C    1 
ATOM   6628 O O    . LEU   B 1 380 ? -4.696  3.451   -71.857 1.00 53.00  ? 380 LEU   B O    1 
ATOM   6629 C CB   . LEU   B 1 380 ? -6.527  5.218   -69.770 1.00 49.93  ? 380 LEU   B CB   1 
ATOM   6630 C CG   . LEU   B 1 380 ? -6.862  6.233   -70.866 1.00 52.12  ? 380 LEU   B CG   1 
ATOM   6631 C CD1  . LEU   B 1 380 ? -7.069  5.553   -72.217 1.00 47.64  ? 380 LEU   B CD1  1 
ATOM   6632 C CD2  . LEU   B 1 380 ? -8.120  7.008   -70.484 1.00 48.15  ? 380 LEU   B CD2  1 
ATOM   6633 N N    . LYS   B 1 381 ? -5.882  2.223   -70.369 1.00 46.60  ? 381 LYS   B N    1 
ATOM   6634 C CA   . LYS   B 1 381 ? -6.147  1.108   -71.257 1.00 47.07  ? 381 LYS   B CA   1 
ATOM   6635 C C    . LYS   B 1 381 ? -7.395  1.426   -72.083 1.00 48.04  ? 381 LYS   B C    1 
ATOM   6636 O O    . LYS   B 1 381 ? -8.460  1.711   -71.522 1.00 42.64  ? 381 LYS   B O    1 
ATOM   6637 C CB   . LYS   B 1 381 ? -6.330  -0.162  -70.421 1.00 46.41  ? 381 LYS   B CB   1 
ATOM   6638 C CG   . LYS   B 1 381 ? -6.589  -1.430  -71.218 1.00 48.40  ? 381 LYS   B CG   1 
ATOM   6639 C CD   . LYS   B 1 381 ? -8.043  -1.865  -71.084 1.00 52.32  ? 381 LYS   B CD   1 
ATOM   6640 C CE   . LYS   B 1 381 ? -8.457  -2.823  -72.189 1.00 51.72  ? 381 LYS   B CE   1 
ATOM   6641 N NZ   . LYS   B 1 381 ? -7.782  -4.135  -71.985 1.00 58.00  ? 381 LYS   B NZ   1 
ATOM   6642 N N    . CYS   B 1 382 ? -7.268  1.425   -73.409 1.00 53.56  ? 382 CYS   B N    1 
ATOM   6643 C CA   . CYS   B 1 382 ? -8.441  1.642   -74.247 1.00 53.67  ? 382 CYS   B CA   1 
ATOM   6644 C C    . CYS   B 1 382 ? -9.331  0.411   -74.193 1.00 51.56  ? 382 CYS   B C    1 
ATOM   6645 O O    . CYS   B 1 382 ? -8.838  -0.719  -74.189 1.00 54.66  ? 382 CYS   B O    1 
ATOM   6646 C CB   . CYS   B 1 382 ? -8.022  1.945   -75.691 1.00 56.95  ? 382 CYS   B CB   1 
ATOM   6647 S SG   . CYS   B 1 382 ? -6.921  3.378   -75.786 1.00 64.21  ? 382 CYS   B SG   1 
ATOM   6648 N N    . LYS   B 1 383 ? -10.652 0.627   -74.171 1.00 47.49  ? 383 LYS   B N    1 
ATOM   6649 C CA   . LYS   B 1 383 ? -11.561 -0.485  -73.897 1.00 46.84  ? 383 LYS   B CA   1 
ATOM   6650 C C    . LYS   B 1 383 ? -11.337 -1.638  -74.871 1.00 51.33  ? 383 LYS   B C    1 
ATOM   6651 O O    . LYS   B 1 383 ? -11.176 -2.793  -74.452 1.00 50.66  ? 383 LYS   B O    1 
ATOM   6652 C CB   . LYS   B 1 383 ? -13.014 -0.022  -73.943 1.00 45.25  ? 383 LYS   B CB   1 
ATOM   6653 C CG   . LYS   B 1 383 ? -14.008 -1.160  -73.710 1.00 45.09  ? 383 LYS   B CG   1 
ATOM   6654 C CD   . LYS   B 1 383 ? -15.400 -0.621  -73.427 1.00 48.52  ? 383 LYS   B CD   1 
ATOM   6655 C CE   . LYS   B 1 383 ? -16.315 -0.800  -74.612 1.00 55.96  ? 383 LYS   B CE   1 
ATOM   6656 N NZ   . LYS   B 1 383 ? -17.269 0.345   -74.788 1.00 61.68  ? 383 LYS   B NZ   1 
ATOM   6657 N N    . THR   B 1 384 ? -11.331 -1.342  -76.173 1.00 48.41  ? 384 THR   B N    1 
ATOM   6658 C CA   . THR   B 1 384 ? -10.985 -2.271  -77.235 1.00 49.19  ? 384 THR   B CA   1 
ATOM   6659 C C    . THR   B 1 384 ? -9.808  -1.695  -78.036 1.00 50.40  ? 384 THR   B C    1 
ATOM   6660 O O    . THR   B 1 384 ? -9.190  -0.706  -77.639 1.00 52.10  ? 384 THR   B O    1 
ATOM   6661 C CB   . THR   B 1 384 ? -12.210 -2.559  -78.122 1.00 50.99  ? 384 THR   B CB   1 
ATOM   6662 O OG1  . THR   B 1 384 ? -12.364 -1.538  -79.123 1.00 49.51  ? 384 THR   B OG1  1 
ATOM   6663 C CG2  . THR   B 1 384 ? -13.472 -2.589  -77.250 1.00 47.32  ? 384 THR   B CG2  1 
ATOM   6664 N N    . THR   B 1 385 ? -9.482  -2.343  -79.161 1.00 50.66  ? 385 THR   B N    1 
ATOM   6665 C CA   . THR   B 1 385 ? -8.380  -1.878  -80.002 1.00 53.51  ? 385 THR   B CA   1 
ATOM   6666 C C    . THR   B 1 385 ? -8.753  -0.675  -80.855 1.00 52.88  ? 385 THR   B C    1 
ATOM   6667 O O    . THR   B 1 385 ? -7.861  0.016   -81.360 1.00 54.35  ? 385 THR   B O    1 
ATOM   6668 C CB   . THR   B 1 385 ? -7.928  -2.986  -80.934 1.00 54.26  ? 385 THR   B CB   1 
ATOM   6669 O OG1  . THR   B 1 385 ? -8.981  -3.212  -81.866 1.00 56.57  ? 385 THR   B OG1  1 
ATOM   6670 C CG2  . THR   B 1 385 ? -7.668  -4.274  -80.167 1.00 55.00  ? 385 THR   B CG2  1 
ATOM   6671 N N    . ASN   B 1 386 ? -10.043 -0.395  -80.994 1.00 51.30  ? 386 ASN   B N    1 
ATOM   6672 C CA   . ASN   B 1 386 ? -10.504 0.770   -81.730 1.00 51.52  ? 386 ASN   B CA   1 
ATOM   6673 C C    . ASN   B 1 386 ? -10.205 2.042   -80.953 1.00 53.31  ? 386 ASN   B C    1 
ATOM   6674 O O    . ASN   B 1 386 ? -10.668 2.209   -79.821 1.00 51.22  ? 386 ASN   B O    1 
ATOM   6675 C CB   . ASN   B 1 386 ? -12.002 0.650   -82.004 1.00 50.54  ? 386 ASN   B CB   1 
ATOM   6676 C CG   . ASN   B 1 386 ? -12.483 1.671   -83.022 1.00 55.51  ? 386 ASN   B CG   1 
ATOM   6677 O OD1  . ASN   B 1 386 ? -12.024 2.820   -83.023 1.00 54.47  ? 386 ASN   B OD1  1 
ATOM   6678 N ND2  . ASN   B 1 386 ? -13.373 1.249   -83.928 1.00 53.21  ? 386 ASN   B ND2  1 
ATOM   6679 N N    . LEU   B 1 387 ? -9.437  2.951   -81.554 1.00 54.84  ? 387 LEU   B N    1 
ATOM   6680 C CA   . LEU   B 1 387 ? -9.198  4.222   -80.875 1.00 56.75  ? 387 LEU   B CA   1 
ATOM   6681 C C    . LEU   B 1 387 ? -10.497 4.964   -80.573 1.00 55.97  ? 387 LEU   B C    1 
ATOM   6682 O O    . LEU   B 1 387 ? -10.474 5.917   -79.787 1.00 54.99  ? 387 LEU   B O    1 
ATOM   6683 C CB   . LEU   B 1 387 ? -8.251  5.098   -81.697 1.00 56.53  ? 387 LEU   B CB   1 
ATOM   6684 C CG   . LEU   B 1 387 ? -6.880  4.459   -81.972 1.00 57.02  ? 387 LEU   B CG   1 
ATOM   6685 C CD1  . LEU   B 1 387 ? -5.865  5.514   -82.332 1.00 58.11  ? 387 LEU   B CD1  1 
ATOM   6686 C CD2  . LEU   B 1 387 ? -6.379  3.635   -80.788 1.00 59.58  ? 387 LEU   B CD2  1 
ATOM   6687 N N    . ASN   B 1 388 ? -11.618 4.551   -81.182 1.00 55.30  ? 388 ASN   B N    1 
ATOM   6688 C CA   . ASN   B 1 388 ? -12.933 5.095   -80.861 1.00 54.63  ? 388 ASN   B CA   1 
ATOM   6689 C C    . ASN   B 1 388 ? -13.294 4.922   -79.406 1.00 53.64  ? 388 ASN   B C    1 
ATOM   6690 O O    . ASN   B 1 388 ? -14.216 5.589   -78.930 1.00 51.60  ? 388 ASN   B O    1 
ATOM   6691 C CB   . ASN   B 1 388 ? -14.033 4.346   -81.609 1.00 52.34  ? 388 ASN   B CB   1 
ATOM   6692 C CG   . ASN   B 1 388 ? -14.175 4.794   -82.983 1.00 57.66  ? 388 ASN   B CG   1 
ATOM   6693 O OD1  . ASN   B 1 388 ? -14.737 4.085   -83.834 1.00 56.46  ? 388 ASN   B OD1  1 
ATOM   6694 N ND2  . ASN   B 1 388 ? -13.649 5.988   -83.255 1.00 64.84  ? 388 ASN   B ND2  1 
ATOM   6695 N N    . THR   B 1 389 ? -12.660 3.966   -78.736 1.00 55.48  ? 389 THR   B N    1 
ATOM   6696 C CA   . THR   B 1 389 ? -13.028 3.555   -77.392 1.00 56.61  ? 389 THR   B CA   1 
ATOM   6697 C C    . THR   B 1 389 ? -11.985 3.918   -76.347 1.00 56.33  ? 389 THR   B C    1 
ATOM   6698 O O    . THR   B 1 389 ? -12.128 3.503   -75.194 1.00 57.85  ? 389 THR   B O    1 
ATOM   6699 C CB   . THR   B 1 389 ? -13.283 2.046   -77.348 1.00 54.29  ? 389 THR   B CB   1 
ATOM   6700 O OG1  . THR   B 1 389 ? -12.081 1.347   -77.703 1.00 54.55  ? 389 THR   B OG1  1 
ATOM   6701 C CG2  . THR   B 1 389 ? -14.421 1.664   -78.275 1.00 51.25  ? 389 THR   B CG2  1 
ATOM   6702 N N    . CYS   B 1 390 ? -10.941 4.669   -76.704 1.00 58.45  ? 390 CYS   B N    1 
ATOM   6703 C CA   . CYS   B 1 390 ? -10.034 5.184   -75.673 1.00 60.64  ? 390 CYS   B CA   1 
ATOM   6704 C C    . CYS   B 1 390 ? -10.779 6.218   -74.840 1.00 56.57  ? 390 CYS   B C    1 
ATOM   6705 O O    . CYS   B 1 390 ? -11.142 7.284   -75.345 1.00 55.51  ? 390 CYS   B O    1 
ATOM   6706 C CB   . CYS   B 1 390 ? -8.772  5.790   -76.282 1.00 59.24  ? 390 CYS   B CB   1 
ATOM   6707 S SG   . CYS   B 1 390 ? -7.754  4.601   -77.199 1.00 63.90  ? 390 CYS   B SG   1 
ATOM   6708 N N    . GLY   B 1 391 ? -11.003 5.911   -73.559 1.00 57.73  ? 391 GLY   B N    1 
ATOM   6709 C CA   . GLY   B 1 391 ? -11.819 6.731   -72.693 1.00 55.82  ? 391 GLY   B CA   1 
ATOM   6710 C C    . GLY   B 1 391 ? -13.085 6.056   -72.235 1.00 53.43  ? 391 GLY   B C    1 
ATOM   6711 O O    . GLY   B 1 391 ? -13.686 6.513   -71.264 1.00 54.54  ? 391 GLY   B O    1 
ATOM   6712 N N    . ASP   B 1 392 ? -13.532 5.018   -72.937 1.00 51.85  ? 392 ASP   B N    1 
ATOM   6713 C CA   . ASP   B 1 392 ? -14.653 4.211   -72.477 1.00 51.66  ? 392 ASP   B CA   1 
ATOM   6714 C C    . ASP   B 1 392 ? -14.266 3.430   -71.226 1.00 52.85  ? 392 ASP   B C    1 
ATOM   6715 O O    . ASP   B 1 392 ? -13.102 3.072   -71.024 1.00 50.63  ? 392 ASP   B O    1 
ATOM   6716 C CB   . ASP   B 1 392 ? -15.101 3.232   -73.563 1.00 50.63  ? 392 ASP   B CB   1 
ATOM   6717 C CG   . ASP   B 1 392 ? -15.794 3.927   -74.736 1.00 56.97  ? 392 ASP   B CG   1 
ATOM   6718 O OD1  . ASP   B 1 392 ? -15.956 5.159   -74.657 1.00 60.36  ? 392 ASP   B OD1  1 
ATOM   6719 O OD2  . ASP   B 1 392 ? -16.155 3.254   -75.744 1.00 58.90  ? 392 ASP   B OD2  1 
ATOM   6720 N N    . SER   B 1 393 ? -15.266 3.127   -70.404 1.00 54.61  ? 393 SER   B N    1 
ATOM   6721 C CA   . SER   B 1 393 ? -15.032 2.285   -69.238 1.00 53.21  ? 393 SER   B CA   1 
ATOM   6722 C C    . SER   B 1 393 ? -14.428 0.956   -69.670 1.00 52.65  ? 393 SER   B C    1 
ATOM   6723 O O    . SER   B 1 393 ? -14.917 0.304   -70.603 1.00 53.26  ? 393 SER   B O    1 
ATOM   6724 C CB   . SER   B 1 393 ? -16.333 2.041   -68.488 1.00 52.98  ? 393 SER   B CB   1 
ATOM   6725 O OG   . SER   B 1 393 ? -16.966 3.271   -68.228 1.00 61.05  ? 393 SER   B OG   1 
ATOM   6726 N N    . ALA   B 1 394 ? -13.344 0.577   -69.000 1.00 54.18  ? 394 ALA   B N    1 
ATOM   6727 C CA   . ALA   B 1 394 ? -12.648 -0.677  -69.240 1.00 55.55  ? 394 ALA   B CA   1 
ATOM   6728 C C    . ALA   B 1 394 ? -12.418 -1.336  -67.888 1.00 54.32  ? 394 ALA   B C    1 
ATOM   6729 O O    . ALA   B 1 394 ? -11.710 -0.782  -67.038 1.00 60.25  ? 394 ALA   B O    1 
ATOM   6730 C CB   . ALA   B 1 394 ? -11.323 -0.442  -69.964 1.00 53.48  ? 394 ALA   B CB   1 
ATOM   6731 N N    . GLU   B 1 395 ? -13.027 -2.505  -67.685 1.00 55.79  ? 395 GLU   B N    1 
ATOM   6732 C CA   . GLU   B 1 395 ? -13.000 -3.184  -66.401 1.00 58.44  ? 395 GLU   B CA   1 
ATOM   6733 C C    . GLU   B 1 395 ? -11.846 -4.161  -66.276 1.00 59.83  ? 395 GLU   B C    1 
ATOM   6734 O O    . GLU   B 1 395 ? -11.492 -4.529  -65.159 1.00 60.27  ? 395 GLU   B O    1 
ATOM   6735 C CB   . GLU   B 1 395 ? -14.306 -3.938  -66.180 1.00 58.47  ? 395 GLU   B CB   1 
ATOM   6736 C CG   . GLU   B 1 395 ? -15.516 -3.068  -66.239 1.00 59.61  ? 395 GLU   B CG   1 
ATOM   6737 C CD   . GLU   B 1 395 ? -16.510 -3.412  -65.171 1.00 71.85  ? 395 GLU   B CD   1 
ATOM   6738 O OE1  . GLU   B 1 395 ? -16.113 -3.533  -63.986 1.00 78.59  ? 395 GLU   B OE1  1 
ATOM   6739 O OE2  . GLU   B 1 395 ? -17.692 -3.604  -65.528 1.00 77.22  ? 395 GLU   B OE2  1 
ATOM   6740 N N    . THR   B 1 396 ? -11.256 -4.596  -67.383 1.00 55.76  ? 396 THR   B N    1 
ATOM   6741 C CA   . THR   B 1 396 ? -10.233 -5.629  -67.330 1.00 59.27  ? 396 THR   B CA   1 
ATOM   6742 C C    . THR   B 1 396 ? -9.105  -5.293  -68.292 1.00 60.41  ? 396 THR   B C    1 
ATOM   6743 O O    . THR   B 1 396 ? -9.309  -4.635  -69.318 1.00 60.06  ? 396 THR   B O    1 
ATOM   6744 C CB   . THR   B 1 396 ? -10.794 -6.998  -67.700 1.00 57.25  ? 396 THR   B CB   1 
ATOM   6745 O OG1  . THR   B 1 396 ? -11.333 -6.924  -69.028 1.00 58.91  ? 396 THR   B OG1  1 
ATOM   6746 C CG2  . THR   B 1 396 ? -11.886 -7.424  -66.721 1.00 58.33  ? 396 THR   B CG2  1 
ATOM   6747 N N    . ALA   B 1 397 ? -7.925  -5.814  -67.977 1.00 55.78  ? 397 ALA   B N    1 
ATOM   6748 C CA   . ALA   B 1 397 ? -6.744  -5.656  -68.809 1.00 57.00  ? 397 ALA   B CA   1 
ATOM   6749 C C    . ALA   B 1 397 ? -5.803  -6.801  -68.477 1.00 61.03  ? 397 ALA   B C    1 
ATOM   6750 O O    . ALA   B 1 397 ? -5.938  -7.465  -67.443 1.00 63.79  ? 397 ALA   B O    1 
ATOM   6751 C CB   . ALA   B 1 397 ? -6.064  -4.298  -68.590 1.00 56.71  ? 397 ALA   B CB   1 
ATOM   6752 N N    . SER   B 1 398 ? -4.843  -7.025  -69.361 1.00 55.76  ? 398 SER   B N    1 
ATOM   6753 C CA   . SER   B 1 398 ? -3.859  -8.067  -69.134 1.00 60.18  ? 398 SER   B CA   1 
ATOM   6754 C C    . SER   B 1 398 ? -2.442  -7.537  -69.018 1.00 61.47  ? 398 SER   B C    1 
ATOM   6755 O O    . SER   B 1 398 ? -1.584  -8.230  -68.454 1.00 63.48  ? 398 SER   B O    1 
ATOM   6756 C CB   . SER   B 1 398 ? -3.923  -9.101  -70.266 1.00 62.24  ? 398 SER   B CB   1 
ATOM   6757 O OG   . SER   B 1 398 ? -5.272  -9.322  -70.642 1.00 61.83  ? 398 SER   B OG   1 
ATOM   6758 N N    . THR   B 1 399 ? -2.180  -6.324  -69.497 1.00 54.86  ? 399 THR   B N    1 
ATOM   6759 C CA   . THR   B 1 399 ? -0.827  -5.794  -69.542 1.00 57.14  ? 399 THR   B CA   1 
ATOM   6760 C C    . THR   B 1 399 ? -0.464  -5.272  -68.168 1.00 57.87  ? 399 THR   B C    1 
ATOM   6761 O O    . THR   B 1 399 ? -0.993  -4.251  -67.699 1.00 55.92  ? 399 THR   B O    1 
ATOM   6762 C CB   . THR   B 1 399 ? -0.711  -4.694  -70.593 1.00 56.97  ? 399 THR   B CB   1 
ATOM   6763 O OG1  . THR   B 1 399 ? -1.070  -5.229  -71.876 1.00 60.14  ? 399 THR   B OG1  1 
ATOM   6764 C CG2  . THR   B 1 399 ? 0.703   -4.122  -70.647 1.00 60.42  ? 399 THR   B CG2  1 
ATOM   6765 N N    . ARG   B 1 400 ? 0.553   -5.921  -67.607 1.00 83.59  ? 400 ARG   B N    1 
ATOM   6766 C CA   . ARG   B 1 400 ? 1.136   -5.417  -66.351 1.00 84.35  ? 400 ARG   B CA   1 
ATOM   6767 C C    . ARG   B 1 400 ? 2.305   -4.535  -66.785 1.00 86.70  ? 400 ARG   B C    1 
ATOM   6768 O O    . ARG   B 1 400 ? 2.809   -4.729  -67.901 1.00 88.95  ? 400 ARG   B O    1 
ATOM   6769 C CB   . ARG   B 1 400 ? 1.640   -6.553  -65.464 1.00 86.95  ? 400 ARG   B CB   1 
ATOM   6770 C CG   . ARG   B 1 400 ? 0.562   -7.465  -64.900 1.00 87.27  ? 400 ARG   B CG   1 
ATOM   6771 C CD   . ARG   B 1 400 ? 1.175   -8.521  -64.000 1.00 101.85 ? 400 ARG   B CD   1 
ATOM   6772 N NE   . ARG   B 1 400 ? 0.161   -9.455  -63.501 1.00 100.70 ? 400 ARG   B NE   1 
ATOM   6773 C CZ   . ARG   B 1 400 ? 0.415   -10.545 -62.787 1.00 106.71 ? 400 ARG   B CZ   1 
ATOM   6774 N NH1  . ARG   B 1 400 ? 1.122   -10.457 -61.675 1.00 107.10 ? 400 ARG   B NH1  1 
ATOM   6775 N NH2  . ARG   B 1 400 ? -0.034  -11.719 -63.193 1.00 103.29 ? 400 ARG   B NH2  1 
ATOM   6776 N N    . PHE   B 1 401 ? 2.697   -3.590  -65.951 1.00 67.32  ? 401 PHE   B N    1 
ATOM   6777 C CA   . PHE   B 1 401 ? 3.766   -2.646  -66.279 1.00 66.91  ? 401 PHE   B CA   1 
ATOM   6778 C C    . PHE   B 1 401 ? 4.975   -2.894  -65.391 1.00 68.19  ? 401 PHE   B C    1 
ATOM   6779 O O    . PHE   B 1 401 ? 4.844   -2.937  -64.161 1.00 71.83  ? 401 PHE   B O    1 
ATOM   6780 C CB   . PHE   B 1 401 ? 3.316   -1.196  -66.106 1.00 65.38  ? 401 PHE   B CB   1 
ATOM   6781 C CG   . PHE   B 1 401 ? 2.550   -0.658  -67.275 1.00 63.95  ? 401 PHE   B CG   1 
ATOM   6782 C CD1  . PHE   B 1 401 ? 1.272   -1.116  -67.541 1.00 60.64  ? 401 PHE   B CD1  1 
ATOM   6783 C CD2  . PHE   B 1 401 ? 3.098   0.311   -68.094 1.00 63.12  ? 401 PHE   B CD2  1 
ATOM   6784 C CE1  . PHE   B 1 401 ? 0.545   -0.617  -68.588 1.00 58.55  ? 401 PHE   B CE1  1 
ATOM   6785 C CE2  . PHE   B 1 401 ? 2.377   0.817   -69.154 1.00 62.81  ? 401 PHE   B CE2  1 
ATOM   6786 C CZ   . PHE   B 1 401 ? 1.096   0.347   -69.403 1.00 61.64  ? 401 PHE   B CZ   1 
ATOM   6787 N N    . GLU   B 1 402 ? 6.156   -3.019  -66.010 1.00 79.65  ? 402 GLU   B N    1 
ATOM   6788 C CA   . GLU   B 1 402 ? 7.391   -3.111  -65.234 1.00 78.75  ? 402 GLU   B CA   1 
ATOM   6789 C C    . GLU   B 1 402 ? 7.672   -1.812  -64.488 1.00 78.47  ? 402 GLU   B C    1 
ATOM   6790 O O    . GLU   B 1 402 ? 8.157   -1.837  -63.351 1.00 79.73  ? 402 GLU   B O    1 
ATOM   6791 C CB   . GLU   B 1 402 ? 8.564   -3.483  -66.144 1.00 78.77  ? 402 GLU   B CB   1 
ATOM   6792 C CG   . GLU   B 1 402 ? 9.604   -4.425  -65.498 1.00 86.80  ? 402 GLU   B CG   1 
ATOM   6793 C CD   . GLU   B 1 402 ? 9.032   -5.770  -65.015 1.00 87.42  ? 402 GLU   B CD   1 
ATOM   6794 O OE1  . GLU   B 1 402 ? 7.813   -6.009  -65.167 1.00 82.59  ? 402 GLU   B OE1  1 
ATOM   6795 O OE2  . GLU   B 1 402 ? 9.812   -6.592  -64.478 1.00 89.03  ? 402 GLU   B OE2  1 
ATOM   6796 N N    . MET   B 1 403 ? 7.398   -0.671  -65.118 1.00 71.41  ? 403 MET   B N    1 
ATOM   6797 C CA   . MET   B 1 403 ? 7.570   0.613   -64.453 1.00 67.87  ? 403 MET   B CA   1 
ATOM   6798 C C    . MET   B 1 403 ? 6.710   1.667   -65.136 1.00 69.53  ? 403 MET   B C    1 
ATOM   6799 O O    . MET   B 1 403 ? 6.395   1.559   -66.327 1.00 69.92  ? 403 MET   B O    1 
ATOM   6800 C CB   . MET   B 1 403 ? 9.035   1.056   -64.427 1.00 66.62  ? 403 MET   B CB   1 
ATOM   6801 C CG   . MET   B 1 403 ? 9.470   1.843   -65.640 1.00 70.53  ? 403 MET   B CG   1 
ATOM   6802 S SD   . MET   B 1 403 ? 9.149   3.608   -65.456 1.00 74.18  ? 403 MET   B SD   1 
ATOM   6803 C CE   . MET   B 1 403 ? 9.819   4.204   -66.983 1.00 66.75  ? 403 MET   B CE   1 
ATOM   6804 N N    . PHE   B 1 404 ? 6.348   2.695   -64.373 1.00 63.86  ? 404 PHE   B N    1 
ATOM   6805 C CA   . PHE   B 1 404 ? 5.699   3.861   -64.952 1.00 65.21  ? 404 PHE   B CA   1 
ATOM   6806 C C    . PHE   B 1 404 ? 6.104   5.108   -64.180 1.00 63.20  ? 404 PHE   B C    1 
ATOM   6807 O O    . PHE   B 1 404 ? 6.587   5.040   -63.045 1.00 63.80  ? 404 PHE   B O    1 
ATOM   6808 C CB   . PHE   B 1 404 ? 4.170   3.721   -64.976 1.00 63.03  ? 404 PHE   B CB   1 
ATOM   6809 C CG   . PHE   B 1 404 ? 3.545   3.590   -63.619 1.00 62.18  ? 404 PHE   B CG   1 
ATOM   6810 C CD1  . PHE   B 1 404 ? 3.423   4.691   -62.784 1.00 63.55  ? 404 PHE   B CD1  1 
ATOM   6811 C CD2  . PHE   B 1 404 ? 3.063   2.368   -63.183 1.00 60.67  ? 404 PHE   B CD2  1 
ATOM   6812 C CE1  . PHE   B 1 404 ? 2.847   4.574   -61.530 1.00 61.57  ? 404 PHE   B CE1  1 
ATOM   6813 C CE2  . PHE   B 1 404 ? 2.487   2.242   -61.929 1.00 63.15  ? 404 PHE   B CE2  1 
ATOM   6814 C CZ   . PHE   B 1 404 ? 2.378   3.350   -61.103 1.00 62.67  ? 404 PHE   B CZ   1 
ATOM   6815 N N    . SER   B 1 405 ? 5.924   6.251   -64.835 1.00 60.28  ? 405 SER   B N    1 
ATOM   6816 C CA   . SER   B 1 405 ? 6.144   7.548   -64.204 1.00 61.88  ? 405 SER   B CA   1 
ATOM   6817 C C    . SER   B 1 405 ? 5.377   8.598   -64.994 1.00 59.61  ? 405 SER   B C    1 
ATOM   6818 O O    . SER   B 1 405 ? 5.654   8.805   -66.183 1.00 60.05  ? 405 SER   B O    1 
ATOM   6819 C CB   . SER   B 1 405 ? 7.626   7.880   -64.142 1.00 60.23  ? 405 SER   B CB   1 
ATOM   6820 O OG   . SER   B 1 405 ? 7.820   9.021   -63.336 1.00 63.89  ? 405 SER   B OG   1 
ATOM   6821 N N    . LEU   B 1 406 ? 4.419   9.255   -64.339 1.00 55.69  ? 406 LEU   B N    1 
ATOM   6822 C CA   . LEU   B 1 406 ? 3.520   10.212  -64.967 1.00 53.13  ? 406 LEU   B CA   1 
ATOM   6823 C C    . LEU   B 1 406 ? 3.637   11.570  -64.275 1.00 55.29  ? 406 LEU   B C    1 
ATOM   6824 O O    . LEU   B 1 406 ? 3.804   11.641  -63.051 1.00 59.49  ? 406 LEU   B O    1 
ATOM   6825 C CB   . LEU   B 1 406 ? 2.080   9.687   -64.916 1.00 51.05  ? 406 LEU   B CB   1 
ATOM   6826 C CG   . LEU   B 1 406 ? 0.969   10.678  -65.258 1.00 55.62  ? 406 LEU   B CG   1 
ATOM   6827 C CD1  . LEU   B 1 406 ? 0.863   10.832  -66.794 1.00 56.88  ? 406 LEU   B CD1  1 
ATOM   6828 C CD2  . LEU   B 1 406 ? -0.377  10.250  -64.652 1.00 54.10  ? 406 LEU   B CD2  1 
ATOM   6829 N N    . SER   B 1 407 ? 3.575   12.651  -65.058 1.00 62.67  ? 407 SER   B N    1 
ATOM   6830 C CA   . SER   B 1 407 ? 3.631   14.002  -64.498 1.00 61.43  ? 407 SER   B CA   1 
ATOM   6831 C C    . SER   B 1 407 ? 2.937   14.958  -65.458 1.00 61.25  ? 407 SER   B C    1 
ATOM   6832 O O    . SER   B 1 407 ? 2.671   14.617  -66.609 1.00 64.93  ? 407 SER   B O    1 
ATOM   6833 C CB   . SER   B 1 407 ? 5.074   14.443  -64.208 1.00 64.25  ? 407 SER   B CB   1 
ATOM   6834 O OG   . SER   B 1 407 ? 5.866   14.575  -65.378 1.00 66.93  ? 407 SER   B OG   1 
ATOM   6835 N N    . GLY   B 1 408 ? 2.644   16.165  -64.975 1.00 57.04  ? 408 GLY   B N    1 
ATOM   6836 C CA   . GLY   B 1 408 ? 1.934   17.136  -65.790 1.00 59.73  ? 408 GLY   B CA   1 
ATOM   6837 C C    . GLY   B 1 408 ? 2.185   18.547  -65.312 1.00 60.92  ? 408 GLY   B C    1 
ATOM   6838 O O    . GLY   B 1 408 ? 2.561   18.768  -64.157 1.00 62.17  ? 408 GLY   B O    1 
ATOM   6839 N N    . THR   B 1 409 ? 2.024   19.508  -66.229 1.00 56.90  ? 409 THR   B N    1 
ATOM   6840 C CA   . THR   B 1 409 ? 2.196   20.925  -65.887 1.00 55.36  ? 409 THR   B CA   1 
ATOM   6841 C C    . THR   B 1 409 ? 0.864   21.466  -65.372 1.00 57.20  ? 409 THR   B C    1 
ATOM   6842 O O    . THR   B 1 409 ? 0.182   22.270  -66.015 1.00 56.34  ? 409 THR   B O    1 
ATOM   6843 C CB   . THR   B 1 409 ? 2.715   21.725  -67.077 1.00 55.49  ? 409 THR   B CB   1 
ATOM   6844 O OG1  . THR   B 1 409 ? 1.682   21.869  -68.057 1.00 58.02  ? 409 THR   B OG1  1 
ATOM   6845 C CG2  . THR   B 1 409 ? 3.901   21.020  -67.703 1.00 56.47  ? 409 THR   B CG2  1 
ATOM   6846 N N    . PHE   B 1 410 ? 0.490   20.977  -64.187 1.00 56.69  ? 410 PHE   B N    1 
ATOM   6847 C CA   . PHE   B 1 410 ? -0.824  21.264  -63.624 1.00 55.19  ? 410 PHE   B CA   1 
ATOM   6848 C C    . PHE   B 1 410 ? -0.922  22.708  -63.164 1.00 56.16  ? 410 PHE   B C    1 
ATOM   6849 O O    . PHE   B 1 410 ? -0.009  23.242  -62.539 1.00 56.97  ? 410 PHE   B O    1 
ATOM   6850 C CB   . PHE   B 1 410 ? -1.124  20.330  -62.452 1.00 55.76  ? 410 PHE   B CB   1 
ATOM   6851 C CG   . PHE   B 1 410 ? -1.556  18.964  -62.880 1.00 52.92  ? 410 PHE   B CG   1 
ATOM   6852 C CD1  . PHE   B 1 410 ? -2.874  18.715  -63.209 1.00 50.02  ? 410 PHE   B CD1  1 
ATOM   6853 C CD2  . PHE   B 1 410 ? -0.636  17.943  -62.988 1.00 51.17  ? 410 PHE   B CD2  1 
ATOM   6854 C CE1  . PHE   B 1 410 ? -3.267  17.460  -63.630 1.00 51.64  ? 410 PHE   B CE1  1 
ATOM   6855 C CE2  . PHE   B 1 410 ? -1.021  16.688  -63.408 1.00 52.46  ? 410 PHE   B CE2  1 
ATOM   6856 C CZ   . PHE   B 1 410 ? -2.334  16.440  -63.728 1.00 50.21  ? 410 PHE   B CZ   1 
ATOM   6857 N N    . GLY   B 1 411 ? -2.041  23.335  -63.474 1.00 69.88  ? 411 GLY   B N    1 
ATOM   6858 C CA   . GLY   B 1 411 ? -2.262  24.702  -63.069 1.00 65.80  ? 411 GLY   B CA   1 
ATOM   6859 C C    . GLY   B 1 411 ? -3.001  24.751  -61.756 1.00 68.27  ? 411 GLY   B C    1 
ATOM   6860 O O    . GLY   B 1 411 ? -3.732  25.696  -61.472 1.00 69.52  ? 411 GLY   B O    1 
ATOM   6861 N N    . THR   B 1 412 ? -2.857  23.691  -60.979 1.00 61.41  ? 412 THR   B N    1 
ATOM   6862 C CA   . THR   B 1 412 ? -3.441  23.601  -59.651 1.00 56.18  ? 412 THR   B CA   1 
ATOM   6863 C C    . THR   B 1 412 ? -2.527  22.830  -58.707 1.00 61.57  ? 412 THR   B C    1 
ATOM   6864 O O    . THR   B 1 412 ? -1.717  22.020  -59.133 1.00 61.77  ? 412 THR   B O    1 
ATOM   6865 C CB   . THR   B 1 412 ? -4.793  22.886  -59.722 1.00 56.32  ? 412 THR   B CB   1 
ATOM   6866 O OG1  . THR   B 1 412 ? -5.423  22.829  -58.433 1.00 54.66  ? 412 THR   B OG1  1 
ATOM   6867 C CG2  . THR   B 1 412 ? -4.621  21.491  -60.269 1.00 58.54  ? 412 THR   B CG2  1 
ATOM   6868 N N    . GLN   B 1 413 ? -2.621  23.124  -57.423 1.00 79.66  ? 413 GLN   B N    1 
ATOM   6869 C CA   . GLN   B 1 413 ? -1.984  22.282  -56.414 1.00 76.70  ? 413 GLN   B CA   1 
ATOM   6870 C C    . GLN   B 1 413 ? -2.885  21.214  -55.836 1.00 74.75  ? 413 GLN   B C    1 
ATOM   6871 O O    . GLN   B 1 413 ? -2.438  20.546  -54.918 1.00 81.22  ? 413 GLN   B O    1 
ATOM   6872 C CB   . GLN   B 1 413 ? -1.373  23.127  -55.274 1.00 79.35  ? 413 GLN   B CB   1 
ATOM   6873 C CG   . GLN   B 1 413 ? -0.535  24.285  -55.786 1.00 87.15  ? 413 GLN   B CG   1 
ATOM   6874 C CD   . GLN   B 1 413 ? 0.977   24.068  -56.035 1.00 88.72  ? 413 GLN   B CD   1 
ATOM   6875 O OE1  . GLN   B 1 413 ? 1.450   23.734  -57.137 1.00 84.28  ? 413 GLN   B OE1  1 
ATOM   6876 N NE2  . GLN   B 1 413 ? 1.763   24.345  -54.991 1.00 92.78  ? 413 GLN   B NE2  1 
ATOM   6877 N N    . TYR   B 1 414 ? -4.144  21.129  -56.241 1.00 56.75  ? 414 TYR   B N    1 
ATOM   6878 C CA   . TYR   B 1 414 ? -5.034  20.040  -55.854 1.00 55.40  ? 414 TYR   B CA   1 
ATOM   6879 C C    . TYR   B 1 414 ? -5.099  18.998  -56.975 1.00 57.29  ? 414 TYR   B C    1 
ATOM   6880 O O    . TYR   B 1 414 ? -5.979  19.008  -57.848 1.00 54.49  ? 414 TYR   B O    1 
ATOM   6881 C CB   . TYR   B 1 414 ? -6.402  20.575  -55.504 1.00 52.79  ? 414 TYR   B CB   1 
ATOM   6882 C CG   . TYR   B 1 414 ? -6.325  21.629  -54.417 1.00 55.34  ? 414 TYR   B CG   1 
ATOM   6883 C CD1  . TYR   B 1 414 ? -5.907  21.309  -53.124 1.00 53.36  ? 414 TYR   B CD1  1 
ATOM   6884 C CD2  . TYR   B 1 414 ? -6.660  22.953  -54.681 1.00 57.01  ? 414 TYR   B CD2  1 
ATOM   6885 C CE1  . TYR   B 1 414 ? -5.844  22.299  -52.122 1.00 55.78  ? 414 TYR   B CE1  1 
ATOM   6886 C CE2  . TYR   B 1 414 ? -6.600  23.923  -53.695 1.00 55.00  ? 414 TYR   B CE2  1 
ATOM   6887 C CZ   . TYR   B 1 414 ? -6.196  23.594  -52.419 1.00 55.65  ? 414 TYR   B CZ   1 
ATOM   6888 O OH   . TYR   B 1 414 ? -6.147  24.584  -51.456 1.00 58.91  ? 414 TYR   B OH   1 
ATOM   6889 N N    . VAL   B 1 415 ? -4.168  18.047  -56.917 1.00 54.03  ? 415 VAL   B N    1 
ATOM   6890 C CA   . VAL   B 1 415 ? -4.049  16.967  -57.890 1.00 56.19  ? 415 VAL   B CA   1 
ATOM   6891 C C    . VAL   B 1 415 ? -4.047  15.635  -57.153 1.00 56.89  ? 415 VAL   B C    1 
ATOM   6892 O O    . VAL   B 1 415 ? -3.233  15.423  -56.248 1.00 53.88  ? 415 VAL   B O    1 
ATOM   6893 C CB   . VAL   B 1 415 ? -2.768  17.109  -58.727 1.00 58.06  ? 415 VAL   B CB   1 
ATOM   6894 C CG1  . VAL   B 1 415 ? -2.598  15.900  -59.602 1.00 55.13  ? 415 VAL   B CG1  1 
ATOM   6895 C CG2  . VAL   B 1 415 ? -2.818  18.424  -59.505 1.00 55.64  ? 415 VAL   B CG2  1 
ATOM   6896 N N    . PHE   B 1 416 ? -4.922  14.720  -57.577 1.00 54.28  ? 416 PHE   B N    1 
ATOM   6897 C CA   . PHE   B 1 416 ? -5.182  13.482  -56.854 1.00 51.62  ? 416 PHE   B CA   1 
ATOM   6898 C C    . PHE   B 1 416 ? -4.658  12.290  -57.643 1.00 51.82  ? 416 PHE   B C    1 
ATOM   6899 O O    . PHE   B 1 416 ? -5.140  12.023  -58.757 1.00 52.03  ? 416 PHE   B O    1 
ATOM   6900 C CB   . PHE   B 1 416 ? -6.684  13.369  -56.588 1.00 46.28  ? 416 PHE   B CB   1 
ATOM   6901 C CG   . PHE   B 1 416 ? -7.276  14.647  -56.017 1.00 47.15  ? 416 PHE   B CG   1 
ATOM   6902 C CD1  . PHE   B 1 416 ? -6.876  15.101  -54.769 1.00 48.73  ? 416 PHE   B CD1  1 
ATOM   6903 C CD2  . PHE   B 1 416 ? -8.188  15.408  -56.734 1.00 46.96  ? 416 PHE   B CD2  1 
ATOM   6904 C CE1  . PHE   B 1 416 ? -7.388  16.284  -54.228 1.00 47.78  ? 416 PHE   B CE1  1 
ATOM   6905 C CE2  . PHE   B 1 416 ? -8.706  16.579  -56.217 1.00 46.08  ? 416 PHE   B CE2  1 
ATOM   6906 C CZ   . PHE   B 1 416 ? -8.299  17.025  -54.941 1.00 47.99  ? 416 PHE   B CZ   1 
ATOM   6907 N N    . PRO   B 1 417 ? -3.664  11.569  -57.114 1.00 56.02  ? 417 PRO   B N    1 
ATOM   6908 C CA   . PRO   B 1 417 ? -3.005  10.507  -57.893 1.00 55.77  ? 417 PRO   B CA   1 
ATOM   6909 C C    . PRO   B 1 417 ? -3.792  9.204   -57.817 1.00 56.54  ? 417 PRO   B C    1 
ATOM   6910 O O    . PRO   B 1 417 ? -4.181  8.757   -56.732 1.00 53.22  ? 417 PRO   B O    1 
ATOM   6911 C CB   . PRO   B 1 417 ? -1.636  10.377  -57.222 1.00 56.68  ? 417 PRO   B CB   1 
ATOM   6912 C CG   . PRO   B 1 417 ? -1.910  10.757  -55.766 1.00 54.83  ? 417 PRO   B CG   1 
ATOM   6913 C CD   . PRO   B 1 417 ? -3.063  11.742  -55.777 1.00 54.59  ? 417 PRO   B CD   1 
ATOM   6914 N N    . GLU   B 1 418 ? -4.048  8.608   -58.983 1.00 50.38  ? 418 GLU   B N    1 
ATOM   6915 C CA   . GLU   B 1 418 ? -4.871  7.411   -59.091 1.00 48.80  ? 418 GLU   B CA   1 
ATOM   6916 C C    . GLU   B 1 418 ? -4.107  6.293   -59.782 1.00 51.76  ? 418 GLU   B C    1 
ATOM   6917 O O    . GLU   B 1 418 ? -3.503  6.498   -60.842 1.00 54.24  ? 418 GLU   B O    1 
ATOM   6918 C CB   . GLU   B 1 418 ? -6.158  7.676   -59.876 1.00 45.80  ? 418 GLU   B CB   1 
ATOM   6919 C CG   . GLU   B 1 418 ? -7.032  8.787   -59.380 1.00 45.61  ? 418 GLU   B CG   1 
ATOM   6920 C CD   . GLU   B 1 418 ? -8.290  8.939   -60.218 1.00 47.95  ? 418 GLU   B CD   1 
ATOM   6921 O OE1  . GLU   B 1 418 ? -9.390  8.722   -59.672 1.00 46.69  ? 418 GLU   B OE1  1 
ATOM   6922 O OE2  . GLU   B 1 418 ? -8.187  9.273   -61.429 1.00 51.76  ? 418 GLU   B OE2  1 
ATOM   6923 N N    . VAL   B 1 419 ? -4.206  5.091   -59.228 1.00 45.91  ? 419 VAL   B N    1 
ATOM   6924 C CA   . VAL   B 1 419 ? -3.690  3.888   -59.867 1.00 46.33  ? 419 VAL   B CA   1 
ATOM   6925 C C    . VAL   B 1 419 ? -4.765  2.821   -59.735 1.00 49.75  ? 419 VAL   B C    1 
ATOM   6926 O O    . VAL   B 1 419 ? -5.155  2.468   -58.616 1.00 44.95  ? 419 VAL   B O    1 
ATOM   6927 C CB   . VAL   B 1 419 ? -2.381  3.398   -59.221 1.00 47.28  ? 419 VAL   B CB   1 
ATOM   6928 C CG1  . VAL   B 1 419 ? -1.887  2.141   -59.904 1.00 47.14  ? 419 VAL   B CG1  1 
ATOM   6929 C CG2  . VAL   B 1 419 ? -1.318  4.511   -59.201 1.00 47.95  ? 419 VAL   B CG2  1 
ATOM   6930 N N    . LEU   B 1 420 ? -5.248  2.298   -60.861 1.00 49.65  ? 420 LEU   B N    1 
ATOM   6931 C CA   . LEU   B 1 420 ? -6.254  1.248   -60.812 1.00 43.25  ? 420 LEU   B CA   1 
ATOM   6932 C C    . LEU   B 1 420 ? -5.775  0.028   -61.580 1.00 49.57  ? 420 LEU   B C    1 
ATOM   6933 O O    . LEU   B 1 420 ? -5.225  0.142   -62.682 1.00 51.24  ? 420 LEU   B O    1 
ATOM   6934 C CB   . LEU   B 1 420 ? -7.586  1.722   -61.359 1.00 42.00  ? 420 LEU   B CB   1 
ATOM   6935 C CG   . LEU   B 1 420 ? -8.774  0.866   -60.916 1.00 44.39  ? 420 LEU   B CG   1 
ATOM   6936 C CD1  . LEU   B 1 420 ? -8.938  0.875   -59.393 1.00 43.20  ? 420 LEU   B CD1  1 
ATOM   6937 C CD2  . LEU   B 1 420 ? -10.060 1.323   -61.586 1.00 44.80  ? 420 LEU   B CD2  1 
ATOM   6938 N N    . LEU   B 1 421 ? -5.977  -1.137  -60.992 1.00 51.86  ? 421 LEU   B N    1 
ATOM   6939 C CA   . LEU   B 1 421 ? -5.608  -2.392  -61.617 1.00 54.06  ? 421 LEU   B CA   1 
ATOM   6940 C C    . LEU   B 1 421 ? -6.866  -3.088  -62.117 1.00 53.62  ? 421 LEU   B C    1 
ATOM   6941 O O    . LEU   B 1 421 ? -7.984  -2.777  -61.695 1.00 51.48  ? 421 LEU   B O    1 
ATOM   6942 C CB   . LEU   B 1 421 ? -4.852  -3.295  -60.632 1.00 55.42  ? 421 LEU   B CB   1 
ATOM   6943 C CG   . LEU   B 1 421 ? -3.573  -2.686  -60.050 1.00 55.60  ? 421 LEU   B CG   1 
ATOM   6944 C CD1  . LEU   B 1 421 ? -2.831  -3.684  -59.202 1.00 59.19  ? 421 LEU   B CD1  1 
ATOM   6945 C CD2  . LEU   B 1 421 ? -2.674  -2.199  -61.162 1.00 59.15  ? 421 LEU   B CD2  1 
ATOM   6946 N N    . SER   B 1 422 ? -6.663  -4.038  -63.031 1.00 55.57  ? 422 SER   B N    1 
ATOM   6947 C CA   . SER   B 1 422 ? -7.751  -4.849  -63.556 1.00 51.80  ? 422 SER   B CA   1 
ATOM   6948 C C    . SER   B 1 422 ? -8.659  -5.321  -62.429 1.00 55.88  ? 422 SER   B C    1 
ATOM   6949 O O    . SER   B 1 422 ? -8.202  -5.604  -61.311 1.00 56.05  ? 422 SER   B O    1 
ATOM   6950 C CB   . SER   B 1 422 ? -7.182  -6.056  -64.317 1.00 56.16  ? 422 SER   B CB   1 
ATOM   6951 O OG   . SER   B 1 422 ? -8.123  -6.584  -65.240 1.00 56.36  ? 422 SER   B OG   1 
ATOM   6952 N N    . GLU   B 1 423 ? -9.955  -5.393  -62.724 1.00 62.60  ? 423 GLU   B N    1 
ATOM   6953 C CA   . GLU   B 1 423 ? -10.985 -5.785  -61.766 1.00 65.03  ? 423 GLU   B CA   1 
ATOM   6954 C C    . GLU   B 1 423 ? -11.245 -4.721  -60.716 1.00 63.63  ? 423 GLU   B C    1 
ATOM   6955 O O    . GLU   B 1 423 ? -11.842 -5.018  -59.676 1.00 63.28  ? 423 GLU   B O    1 
ATOM   6956 C CB   . GLU   B 1 423 ? -10.646 -7.096  -61.050 1.00 66.28  ? 423 GLU   B CB   1 
ATOM   6957 C CG   . GLU   B 1 423 ? -9.740  -8.013  -61.799 1.00 71.93  ? 423 GLU   B CG   1 
ATOM   6958 C CD   . GLU   B 1 423 ? -10.509 -8.903  -62.711 1.00 74.86  ? 423 GLU   B CD   1 
ATOM   6959 O OE1  . GLU   B 1 423 ? -9.887  -9.737  -63.405 1.00 85.29  ? 423 GLU   B OE1  1 
ATOM   6960 O OE2  . GLU   B 1 423 ? -11.748 -8.771  -62.710 1.00 75.76  ? 423 GLU   B OE2  1 
ATOM   6961 N N    . ASN   B 1 424 ? -10.812 -3.484  -60.958 1.00 59.52  ? 424 ASN   B N    1 
ATOM   6962 C CA   . ASN   B 1 424 ? -11.136 -2.377  -60.072 1.00 59.68  ? 424 ASN   B CA   1 
ATOM   6963 C C    . ASN   B 1 424 ? -10.469 -2.561  -58.701 1.00 61.06  ? 424 ASN   B C    1 
ATOM   6964 O O    . ASN   B 1 424 ? -11.076 -2.346  -57.649 1.00 59.41  ? 424 ASN   B O    1 
ATOM   6965 C CB   . ASN   B 1 424 ? -12.665 -2.236  -59.972 1.00 56.21  ? 424 ASN   B CB   1 
ATOM   6966 C CG   . ASN   B 1 424 ? -13.130 -0.787  -59.994 1.00 58.15  ? 424 ASN   B CG   1 
ATOM   6967 O OD1  . ASN   B 1 424 ? -12.649 0.028   -59.199 1.00 60.96  ? 424 ASN   B OD1  1 
ATOM   6968 N ND2  . ASN   B 1 424 ? -14.019 -0.440  -60.941 1.00 54.02  ? 424 ASN   B ND2  1 
ATOM   6969 N N    . GLN   B 1 425 ? -9.199  -2.968  -58.731 1.00 56.11  ? 425 GLN   B N    1 
ATOM   6970 C CA   . GLN   B 1 425 ? -8.387  -3.221  -57.550 1.00 56.53  ? 425 GLN   B CA   1 
ATOM   6971 C C    . GLN   B 1 425 ? -7.369  -2.104  -57.368 1.00 58.32  ? 425 GLN   B C    1 
ATOM   6972 O O    . GLN   B 1 425 ? -6.793  -1.604  -58.345 1.00 56.25  ? 425 GLN   B O    1 
ATOM   6973 C CB   . GLN   B 1 425 ? -7.660  -4.566  -57.659 1.00 56.50  ? 425 GLN   B CB   1 
ATOM   6974 C CG   . GLN   B 1 425 ? -8.587  -5.723  -57.976 1.00 55.53  ? 425 GLN   B CG   1 
ATOM   6975 C CD   . GLN   B 1 425 ? -9.503  -6.045  -56.827 1.00 56.75  ? 425 GLN   B CD   1 
ATOM   6976 O OE1  . GLN   B 1 425 ? -9.041  -6.406  -55.753 1.00 59.47  ? 425 GLN   B OE1  1 
ATOM   6977 N NE2  . GLN   B 1 425 ? -10.805 -5.917  -57.041 1.00 55.10  ? 425 GLN   B NE2  1 
ATOM   6978 N N    . LEU   B 1 426 ? -7.169  -1.701  -56.114 1.00 51.07  ? 426 LEU   B N    1 
ATOM   6979 C CA   . LEU   B 1 426 ? -6.132  -0.741  -55.768 1.00 50.92  ? 426 LEU   B CA   1 
ATOM   6980 C C    . LEU   B 1 426 ? -4.765  -1.413  -55.769 1.00 52.89  ? 426 LEU   B C    1 
ATOM   6981 O O    . LEU   B 1 426 ? -4.649  -2.638  -55.721 1.00 55.23  ? 426 LEU   B O    1 
ATOM   6982 C CB   . LEU   B 1 426 ? -6.401  -0.122  -54.394 1.00 48.76  ? 426 LEU   B CB   1 
ATOM   6983 C CG   . LEU   B 1 426 ? -7.684  0.700   -54.346 1.00 47.09  ? 426 LEU   B CG   1 
ATOM   6984 C CD1  . LEU   B 1 426 ? -7.782  1.441   -53.004 1.00 45.46  ? 426 LEU   B CD1  1 
ATOM   6985 C CD2  . LEU   B 1 426 ? -7.730  1.644   -55.575 1.00 43.67  ? 426 LEU   B CD2  1 
ATOM   6986 N N    . ALA   B 1 427 ? -3.719  -0.589  -55.789 1.00 57.89  ? 427 ALA   B N    1 
ATOM   6987 C CA   . ALA   B 1 427 ? -2.335  -1.057  -55.813 1.00 56.97  ? 427 ALA   B CA   1 
ATOM   6988 C C    . ALA   B 1 427 ? -1.597  -0.488  -54.610 1.00 59.46  ? 427 ALA   B C    1 
ATOM   6989 O O    . ALA   B 1 427 ? -0.635  0.276   -54.759 1.00 59.95  ? 427 ALA   B O    1 
ATOM   6990 C CB   . ALA   B 1 427 ? -1.638  -0.658  -57.110 1.00 58.72  ? 427 ALA   B CB   1 
ATOM   6991 N N    . PRO   B 1 428 ? -2.024  -0.839  -53.398 1.00 60.26  ? 428 PRO   B N    1 
ATOM   6992 C CA   . PRO   B 1 428 ? -1.421  -0.239  -52.199 1.00 57.44  ? 428 PRO   B CA   1 
ATOM   6993 C C    . PRO   B 1 428 ? 0.058   -0.578  -52.098 1.00 62.08  ? 428 PRO   B C    1 
ATOM   6994 O O    . PRO   B 1 428 ? 0.457   -1.744  -52.166 1.00 61.78  ? 428 PRO   B O    1 
ATOM   6995 C CB   . PRO   B 1 428 ? -2.225  -0.864  -51.058 1.00 57.60  ? 428 PRO   B CB   1 
ATOM   6996 C CG   . PRO   B 1 428 ? -2.659  -2.176  -51.607 1.00 58.15  ? 428 PRO   B CG   1 
ATOM   6997 C CD   . PRO   B 1 428 ? -2.958  -1.927  -53.062 1.00 58.53  ? 428 PRO   B CD   1 
ATOM   6998 N N    . GLY   B 1 429 ? 0.875   0.459   -51.930 1.00 59.62  ? 429 GLY   B N    1 
ATOM   6999 C CA   . GLY   B 1 429 ? 2.299   0.296   -51.747 1.00 58.38  ? 429 GLY   B CA   1 
ATOM   7000 C C    . GLY   B 1 429 ? 3.109   0.018   -52.991 1.00 61.25  ? 429 GLY   B C    1 
ATOM   7001 O O    . GLY   B 1 429 ? 4.327   -0.155  -52.873 1.00 64.84  ? 429 GLY   B O    1 
ATOM   7002 N N    . GLU   B 1 430 ? 2.485   -0.014  -54.184 1.00 73.42  ? 430 GLU   B N    1 
ATOM   7003 C CA   . GLU   B 1 430 ? 3.182   -0.234  -55.450 1.00 70.64  ? 430 GLU   B CA   1 
ATOM   7004 C C    . GLU   B 1 430 ? 3.589   1.053   -56.156 1.00 72.06  ? 430 GLU   B C    1 
ATOM   7005 O O    . GLU   B 1 430 ? 4.289   0.988   -57.174 1.00 74.07  ? 430 GLU   B O    1 
ATOM   7006 C CB   . GLU   B 1 430 ? 2.311   -1.057  -56.406 1.00 69.08  ? 430 GLU   B CB   1 
ATOM   7007 C CG   . GLU   B 1 430 ? 2.205   -2.516  -56.028 1.00 75.21  ? 430 GLU   B CG   1 
ATOM   7008 C CD   . GLU   B 1 430 ? 1.115   -3.248  -56.788 1.00 76.43  ? 430 GLU   B CD   1 
ATOM   7009 O OE1  . GLU   B 1 430 ? 1.358   -3.626  -57.957 1.00 78.19  ? 430 GLU   B OE1  1 
ATOM   7010 O OE2  . GLU   B 1 430 ? 0.020   -3.453  -56.217 1.00 77.56  ? 430 GLU   B OE2  1 
ATOM   7011 N N    . PHE   B 1 431 ? 3.182   2.211   -55.643 1.00 57.91  ? 431 PHE   B N    1 
ATOM   7012 C CA   . PHE   B 1 431 ? 3.487   3.487   -56.271 1.00 57.83  ? 431 PHE   B CA   1 
ATOM   7013 C C    . PHE   B 1 431 ? 3.635   4.554   -55.197 1.00 59.78  ? 431 PHE   B C    1 
ATOM   7014 O O    . PHE   B 1 431 ? 3.144   4.409   -54.074 1.00 59.62  ? 431 PHE   B O    1 
ATOM   7015 C CB   . PHE   B 1 431 ? 2.411   3.901   -57.276 1.00 55.06  ? 431 PHE   B CB   1 
ATOM   7016 C CG   . PHE   B 1 431 ? 1.057   4.206   -56.659 1.00 53.15  ? 431 PHE   B CG   1 
ATOM   7017 C CD1  . PHE   B 1 431 ? 0.130   3.190   -56.430 1.00 51.96  ? 431 PHE   B CD1  1 
ATOM   7018 C CD2  . PHE   B 1 431 ? 0.699   5.517   -56.334 1.00 51.98  ? 431 PHE   B CD2  1 
ATOM   7019 C CE1  . PHE   B 1 431 ? -1.129  3.477   -55.894 1.00 47.76  ? 431 PHE   B CE1  1 
ATOM   7020 C CE2  . PHE   B 1 431 ? -0.548  5.811   -55.795 1.00 47.30  ? 431 PHE   B CE2  1 
ATOM   7021 C CZ   . PHE   B 1 431 ? -1.466  4.792   -55.585 1.00 47.91  ? 431 PHE   B CZ   1 
ATOM   7022 N N    . GLN   B 1 432 ? 4.326   5.632   -55.558 1.00 75.92  ? 432 GLN   B N    1 
ATOM   7023 C CA   . GLN   B 1 432 ? 4.450   6.789   -54.688 1.00 74.12  ? 432 GLN   B CA   1 
ATOM   7024 C C    . GLN   B 1 432 ? 4.431   8.057   -55.529 1.00 77.52  ? 432 GLN   B C    1 
ATOM   7025 O O    . GLN   B 1 432 ? 4.659   8.036   -56.745 1.00 76.58  ? 432 GLN   B O    1 
ATOM   7026 C CB   . GLN   B 1 432 ? 5.722   6.720   -53.825 1.00 76.92  ? 432 GLN   B CB   1 
ATOM   7027 C CG   . GLN   B 1 432 ? 5.652   7.572   -52.547 1.00 82.83  ? 432 GLN   B CG   1 
ATOM   7028 C CD   . GLN   B 1 432 ? 4.231   7.677   -51.985 1.00 81.58  ? 432 GLN   B CD   1 
ATOM   7029 O OE1  . GLN   B 1 432 ? 3.618   8.752   -51.998 1.00 77.96  ? 432 GLN   B OE1  1 
ATOM   7030 N NE2  . GLN   B 1 432 ? 3.696   6.554   -51.508 1.00 79.49  ? 432 GLN   B NE2  1 
ATOM   7031 N N    . VAL   B 1 433 ? 4.151   9.168   -54.853 1.00 72.33  ? 433 VAL   B N    1 
ATOM   7032 C CA   . VAL   B 1 433 ? 4.152   10.502  -55.441 1.00 70.68  ? 433 VAL   B CA   1 
ATOM   7033 C C    . VAL   B 1 433 ? 5.380   11.237  -54.929 1.00 70.23  ? 433 VAL   B C    1 
ATOM   7034 O O    . VAL   B 1 433 ? 5.709   11.152  -53.742 1.00 75.74  ? 433 VAL   B O    1 
ATOM   7035 C CB   . VAL   B 1 433 ? 2.870   11.282  -55.106 1.00 69.40  ? 433 VAL   B CB   1 
ATOM   7036 C CG1  . VAL   B 1 433 ? 3.099   12.784  -55.281 1.00 67.34  ? 433 VAL   B CG1  1 
ATOM   7037 C CG2  . VAL   B 1 433 ? 1.719   10.808  -55.974 1.00 65.97  ? 433 VAL   B CG2  1 
ATOM   7038 N N    . SER   B 1 434 ? 6.079   11.915  -55.831 1.00 68.90  ? 434 SER   B N    1 
ATOM   7039 C CA   . SER   B 1 434 ? 7.246   12.710  -55.483 1.00 65.38  ? 434 SER   B CA   1 
ATOM   7040 C C    . SER   B 1 434 ? 6.846   14.144  -55.117 1.00 65.48  ? 434 SER   B C    1 
ATOM   7041 O O    . SER   B 1 434 ? 5.715   14.586  -55.348 1.00 64.24  ? 434 SER   B O    1 
ATOM   7042 C CB   . SER   B 1 434 ? 8.248   12.702  -56.642 1.00 63.52  ? 434 SER   B CB   1 
ATOM   7043 O OG   . SER   B 1 434 ? 7.938   13.691  -57.610 1.00 61.21  ? 434 SER   B OG   1 
ATOM   7044 N N    . THR   B 1 435 ? 7.797   14.872  -54.521 1.00 73.76  ? 435 THR   B N    1 
ATOM   7045 C CA   . THR   B 1 435 ? 7.540   16.251  -54.125 1.00 74.19  ? 435 THR   B CA   1 
ATOM   7046 C C    . THR   B 1 435 ? 7.478   17.193  -55.322 1.00 73.94  ? 435 THR   B C    1 
ATOM   7047 O O    . THR   B 1 435 ? 6.858   18.258  -55.217 1.00 73.25  ? 435 THR   B O    1 
ATOM   7048 C CB   . THR   B 1 435 ? 8.596   16.741  -53.123 1.00 73.51  ? 435 THR   B CB   1 
ATOM   7049 O OG1  . THR   B 1 435 ? 9.911   16.560  -53.663 1.00 79.84  ? 435 THR   B OG1  1 
ATOM   7050 C CG2  . THR   B 1 435 ? 8.488   15.977  -51.818 1.00 80.91  ? 435 THR   B CG2  1 
ATOM   7051 N N    . ASP   B 1 436 ? 8.111   16.845  -56.443 1.00 65.85  ? 436 ASP   B N    1 
ATOM   7052 C CA   . ASP   B 1 436 ? 7.999   17.647  -57.658 1.00 66.18  ? 436 ASP   B CA   1 
ATOM   7053 C C    . ASP   B 1 436 ? 6.878   17.168  -58.575 1.00 66.75  ? 436 ASP   B C    1 
ATOM   7054 O O    . ASP   B 1 436 ? 6.836   17.573  -59.743 1.00 67.59  ? 436 ASP   B O    1 
ATOM   7055 C CB   . ASP   B 1 436 ? 9.325   17.700  -58.423 1.00 64.24  ? 436 ASP   B CB   1 
ATOM   7056 C CG   . ASP   B 1 436 ? 9.968   16.346  -58.594 1.00 64.87  ? 436 ASP   B CG   1 
ATOM   7057 O OD1  . ASP   B 1 436 ? 9.256   15.319  -58.652 1.00 63.43  ? 436 ASP   B OD1  1 
ATOM   7058 O OD2  . ASP   B 1 436 ? 11.210  16.313  -58.663 1.00 67.33  ? 436 ASP   B OD2  1 
ATOM   7059 N N    . GLY   B 1 437 ? 5.994   16.300  -58.085 1.00 63.08  ? 437 GLY   B N    1 
ATOM   7060 C CA   . GLY   B 1 437 ? 4.746   15.993  -58.766 1.00 63.50  ? 437 GLY   B CA   1 
ATOM   7061 C C    . GLY   B 1 437 ? 4.684   14.729  -59.599 1.00 61.22  ? 437 GLY   B C    1 
ATOM   7062 O O    . GLY   B 1 437 ? 3.684   14.525  -60.290 1.00 62.03  ? 437 GLY   B O    1 
ATOM   7063 N N    . ARG   B 1 438 ? 5.693   13.865  -59.542 1.00 57.48  ? 438 ARG   B N    1 
ATOM   7064 C CA   . ARG   B 1 438 ? 5.690   12.623  -60.304 1.00 56.60  ? 438 ARG   B CA   1 
ATOM   7065 C C    . ARG   B 1 438 ? 4.961   11.519  -59.551 1.00 58.75  ? 438 ARG   B C    1 
ATOM   7066 O O    . ARG   B 1 438 ? 5.157   11.334  -58.344 1.00 62.63  ? 438 ARG   B O    1 
ATOM   7067 C CB   . ARG   B 1 438 ? 7.119   12.171  -60.593 1.00 60.95  ? 438 ARG   B CB   1 
ATOM   7068 C CG   . ARG   B 1 438 ? 7.854   13.026  -61.594 1.00 61.11  ? 438 ARG   B CG   1 
ATOM   7069 C CD   . ARG   B 1 438 ? 9.301   12.573  -61.717 1.00 62.02  ? 438 ARG   B CD   1 
ATOM   7070 N NE   . ARG   B 1 438 ? 10.208  13.395  -60.928 1.00 59.05  ? 438 ARG   B NE   1 
ATOM   7071 C CZ   . ARG   B 1 438 ? 11.472  13.087  -60.668 1.00 60.32  ? 438 ARG   B CZ   1 
ATOM   7072 N NH1  . ARG   B 1 438 ? 12.005  11.947  -61.075 1.00 63.25  ? 438 ARG   B NH1  1 
ATOM   7073 N NH2  . ARG   B 1 438 ? 12.229  13.955  -60.006 1.00 61.42  ? 438 ARG   B NH2  1 
ATOM   7074 N N    . LEU   B 1 439 ? 4.133   10.775  -60.271 1.00 60.82  ? 439 LEU   B N    1 
ATOM   7075 C CA   . LEU   B 1 439 ? 3.435   9.610   -59.736 1.00 59.78  ? 439 LEU   B CA   1 
ATOM   7076 C C    . LEU   B 1 439 ? 4.020   8.379   -60.413 1.00 61.64  ? 439 LEU   B C    1 
ATOM   7077 O O    . LEU   B 1 439 ? 3.866   8.203   -61.627 1.00 58.47  ? 439 LEU   B O    1 
ATOM   7078 C CB   . LEU   B 1 439 ? 1.931   9.721   -59.991 1.00 56.55  ? 439 LEU   B CB   1 
ATOM   7079 C CG   . LEU   B 1 439 ? 1.164   8.409   -60.162 1.00 56.78  ? 439 LEU   B CG   1 
ATOM   7080 C CD1  . LEU   B 1 439 ? 1.202   7.591   -58.878 1.00 52.93  ? 439 LEU   B CD1  1 
ATOM   7081 C CD2  . LEU   B 1 439 ? -0.274  8.687   -60.583 1.00 54.11  ? 439 LEU   B CD2  1 
ATOM   7082 N N    . PHE   B 1 440 ? 4.689   7.520   -59.653 1.00 70.15  ? 440 PHE   B N    1 
ATOM   7083 C CA   . PHE   B 1 440 ? 5.399   6.447   -60.331 1.00 73.06  ? 440 PHE   B CA   1 
ATOM   7084 C C    . PHE   B 1 440 ? 5.398   5.178   -59.495 1.00 71.40  ? 440 PHE   B C    1 
ATOM   7085 O O    . PHE   B 1 440 ? 5.046   5.172   -58.314 1.00 69.13  ? 440 PHE   B O    1 
ATOM   7086 C CB   . PHE   B 1 440 ? 6.815   6.872   -60.690 1.00 74.34  ? 440 PHE   B CB   1 
ATOM   7087 C CG   . PHE   B 1 440 ? 7.568   7.381   -59.534 1.00 77.08  ? 440 PHE   B CG   1 
ATOM   7088 C CD1  . PHE   B 1 440 ? 7.968   6.523   -58.526 1.00 78.63  ? 440 PHE   B CD1  1 
ATOM   7089 C CD2  . PHE   B 1 440 ? 7.843   8.731   -59.418 1.00 77.77  ? 440 PHE   B CD2  1 
ATOM   7090 C CE1  . PHE   B 1 440 ? 8.639   7.002   -57.436 1.00 78.75  ? 440 PHE   B CE1  1 
ATOM   7091 C CE2  . PHE   B 1 440 ? 8.523   9.214   -58.322 1.00 80.63  ? 440 PHE   B CE2  1 
ATOM   7092 C CZ   . PHE   B 1 440 ? 8.922   8.341   -57.331 1.00 80.69  ? 440 PHE   B CZ   1 
ATOM   7093 N N    . SER   B 1 441 ? 5.794   4.094   -60.152 1.00 74.02  ? 441 SER   B N    1 
ATOM   7094 C CA   . SER   B 1 441 ? 5.734   2.750   -59.604 1.00 74.58  ? 441 SER   B CA   1 
ATOM   7095 C C    . SER   B 1 441 ? 6.977   2.465   -58.772 1.00 77.15  ? 441 SER   B C    1 
ATOM   7096 O O    . SER   B 1 441 ? 8.096   2.786   -59.187 1.00 78.46  ? 441 SER   B O    1 
ATOM   7097 C CB   . SER   B 1 441 ? 5.625   1.729   -60.736 1.00 72.13  ? 441 SER   B CB   1 
ATOM   7098 O OG   . SER   B 1 441 ? 6.816   1.732   -61.509 1.00 73.21  ? 441 SER   B OG   1 
ATOM   7099 N N    . LEU   B 1 442 ? 6.771   1.875   -57.592 1.00 79.42  ? 442 LEU   B N    1 
ATOM   7100 C CA   . LEU   B 1 442 ? 7.869   1.400   -56.755 1.00 80.31  ? 442 LEU   B CA   1 
ATOM   7101 C C    . LEU   B 1 442 ? 8.399   0.041   -57.191 1.00 80.45  ? 442 LEU   B C    1 
ATOM   7102 O O    . LEU   B 1 442 ? 9.454   -0.384  -56.710 1.00 83.19  ? 442 LEU   B O    1 
ATOM   7103 C CB   . LEU   B 1 442 ? 7.419   1.307   -55.296 1.00 77.60  ? 442 LEU   B CB   1 
ATOM   7104 C CG   . LEU   B 1 442 ? 7.187   2.622   -54.561 1.00 80.41  ? 442 LEU   B CG   1 
ATOM   7105 C CD1  . LEU   B 1 442 ? 6.323   2.406   -53.327 1.00 78.05  ? 442 LEU   B CD1  1 
ATOM   7106 C CD2  . LEU   B 1 442 ? 8.513   3.215   -54.164 1.00 82.13  ? 442 LEU   B CD2  1 
ATOM   7107 N N    . LYS   B 1 443 ? 7.701   -0.636  -58.072 1.00 79.73  ? 443 LYS   B N    1 
ATOM   7108 C CA   . LYS   B 1 443 ? 8.079   -1.957  -58.533 1.00 78.10  ? 443 LYS   B CA   1 
ATOM   7109 C C    . LYS   B 1 443 ? 7.089   -2.272  -59.633 1.00 78.53  ? 443 LYS   B C    1 
ATOM   7110 O O    . LYS   B 1 443 ? 6.128   -1.503  -59.813 1.00 78.17  ? 443 LYS   B O    1 
ATOM   7111 C CB   . LYS   B 1 443 ? 7.986   -2.987  -57.410 1.00 81.52  ? 443 LYS   B CB   1 
ATOM   7112 C CG   . LYS   B 1 443 ? 6.641   -2.971  -56.686 1.00 81.58  ? 443 LYS   B CG   1 
ATOM   7113 C CD   . LYS   B 1 443 ? 6.774   -3.655  -55.330 1.00 82.32  ? 443 LYS   B CD   1 
ATOM   7114 C CE   . LYS   B 1 443 ? 5.425   -4.004  -54.709 1.00 80.82  ? 443 LYS   B CE   1 
ATOM   7115 N NZ   . LYS   B 1 443 ? 5.539   -4.114  -53.206 1.00 85.65  ? 443 LYS   B NZ   1 
ATOM   7116 N N    . PRO   B 1 444 ? 7.274   -3.377  -60.362 1.00 68.46  ? 444 PRO   B N    1 
ATOM   7117 C CA   . PRO   B 1 444 ? 6.287   -3.792  -61.360 1.00 69.11  ? 444 PRO   B CA   1 
ATOM   7118 C C    . PRO   B 1 444 ? 4.935   -3.992  -60.681 1.00 69.39  ? 444 PRO   B C    1 
ATOM   7119 O O    . PRO   B 1 444 ? 4.848   -4.434  -59.531 1.00 69.82  ? 444 PRO   B O    1 
ATOM   7120 C CB   . PRO   B 1 444 ? 6.878   -5.102  -61.909 1.00 68.62  ? 444 PRO   B CB   1 
ATOM   7121 C CG   . PRO   B 1 444 ? 8.277   -5.042  -61.583 1.00 70.76  ? 444 PRO   B CG   1 
ATOM   7122 C CD   . PRO   B 1 444 ? 8.394   -4.312  -60.294 1.00 68.34  ? 444 PRO   B CD   1 
ATOM   7123 N N    . THR   B 1 445 ? 3.876   -3.564  -61.371 1.00 60.06  ? 445 THR   B N    1 
ATOM   7124 C CA   . THR   B 1 445 ? 2.536   -3.627  -60.803 1.00 59.45  ? 445 THR   B CA   1 
ATOM   7125 C C    . THR   B 1 445 ? 2.115   -5.070  -60.472 1.00 61.87  ? 445 THR   B C    1 
ATOM   7126 O O    . THR   B 1 445 ? 2.456   -6.031  -61.171 1.00 63.43  ? 445 THR   B O    1 
ATOM   7127 C CB   . THR   B 1 445 ? 1.546   -3.007  -61.792 1.00 59.22  ? 445 THR   B CB   1 
ATOM   7128 O OG1  . THR   B 1 445 ? 1.562   -3.789  -62.999 1.00 59.53  ? 445 THR   B OG1  1 
ATOM   7129 C CG2  . THR   B 1 445 ? 1.922   -1.553  -62.087 1.00 52.39  ? 445 THR   B CG2  1 
ATOM   7130 N N    . SER   B 1 446 ? 1.340   -5.223  -59.397 1.00 68.86  ? 446 SER   B N    1 
ATOM   7131 C CA   . SER   B 1 446 ? 0.947   -6.574  -59.005 1.00 69.80  ? 446 SER   B CA   1 
ATOM   7132 C C    . SER   B 1 446 ? -0.095  -7.173  -59.949 1.00 75.84  ? 446 SER   B C    1 
ATOM   7133 O O    . SER   B 1 446 ? -0.229  -8.402  -60.007 1.00 81.31  ? 446 SER   B O    1 
ATOM   7134 C CB   . SER   B 1 446 ? 0.442   -6.611  -57.553 1.00 75.61  ? 446 SER   B CB   1 
ATOM   7135 O OG   . SER   B 1 446 ? -0.778  -5.894  -57.382 1.00 71.78  ? 446 SER   B OG   1 
ATOM   7136 N N    . GLY   B 1 447 ? -0.874  -6.343  -60.646 1.00 64.25  ? 447 GLY   B N    1 
ATOM   7137 C CA   . GLY   B 1 447 ? -1.788  -6.808  -61.671 1.00 62.98  ? 447 GLY   B CA   1 
ATOM   7138 C C    . GLY   B 1 447 ? -1.778  -5.915  -62.903 1.00 60.81  ? 447 GLY   B C    1 
ATOM   7139 O O    . GLY   B 1 447 ? -1.095  -4.886  -62.944 1.00 59.63  ? 447 GLY   B O    1 
ATOM   7140 N N    . PRO   B 1 448 ? -2.524  -6.294  -63.939 1.00 58.46  ? 448 PRO   B N    1 
ATOM   7141 C CA   . PRO   B 1 448 ? -2.582  -5.449  -65.140 1.00 58.62  ? 448 PRO   B CA   1 
ATOM   7142 C C    . PRO   B 1 448 ? -3.191  -4.095  -64.809 1.00 54.86  ? 448 PRO   B C    1 
ATOM   7143 O O    . PRO   B 1 448 ? -4.107  -3.985  -63.988 1.00 51.74  ? 448 PRO   B O    1 
ATOM   7144 C CB   . PRO   B 1 448 ? -3.478  -6.243  -66.104 1.00 54.22  ? 448 PRO   B CB   1 
ATOM   7145 C CG   . PRO   B 1 448 ? -3.541  -7.635  -65.549 1.00 56.59  ? 448 PRO   B CG   1 
ATOM   7146 C CD   . PRO   B 1 448 ? -3.356  -7.506  -64.059 1.00 59.12  ? 448 PRO   B CD   1 
ATOM   7147 N N    . VAL   B 1 449 ? -2.680  -3.060  -65.475 1.00 53.79  ? 449 VAL   B N    1 
ATOM   7148 C CA   . VAL   B 1 449 ? -3.053  -1.678  -65.186 1.00 50.55  ? 449 VAL   B CA   1 
ATOM   7149 C C    . VAL   B 1 449 ? -4.240  -1.276  -66.050 1.00 50.99  ? 449 VAL   B C    1 
ATOM   7150 O O    . VAL   B 1 449 ? -4.232  -1.477  -67.279 1.00 49.63  ? 449 VAL   B O    1 
ATOM   7151 C CB   . VAL   B 1 449 ? -1.875  -0.723  -65.428 1.00 52.96  ? 449 VAL   B CB   1 
ATOM   7152 C CG1  . VAL   B 1 449 ? -2.396  0.716   -65.589 1.00 49.13  ? 449 VAL   B CG1  1 
ATOM   7153 C CG2  . VAL   B 1 449 ? -0.844  -0.842  -64.313 1.00 53.38  ? 449 VAL   B CG2  1 
ATOM   7154 N N    . LEU   B 1 450 ? -5.262  -0.701  -65.414 1.00 52.64  ? 450 LEU   B N    1 
ATOM   7155 C CA   . LEU   B 1 450 ? -6.347  -0.015  -66.102 1.00 49.13  ? 450 LEU   B CA   1 
ATOM   7156 C C    . LEU   B 1 450 ? -6.003  1.454   -66.344 1.00 51.96  ? 450 LEU   B C    1 
ATOM   7157 O O    . LEU   B 1 450 ? -6.179  1.962   -67.461 1.00 52.40  ? 450 LEU   B O    1 
ATOM   7158 C CB   . LEU   B 1 450 ? -7.635  -0.116  -65.277 1.00 48.52  ? 450 LEU   B CB   1 
ATOM   7159 C CG   . LEU   B 1 450 ? -8.330  -1.474  -65.252 1.00 47.21  ? 450 LEU   B CG   1 
ATOM   7160 C CD1  . LEU   B 1 450 ? -9.542  -1.405  -64.343 1.00 42.69  ? 450 LEU   B CD1  1 
ATOM   7161 C CD2  . LEU   B 1 450 ? -8.726  -1.874  -66.664 1.00 44.89  ? 450 LEU   B CD2  1 
ATOM   7162 N N    . THR   B 1 451 ? -5.525  2.151   -65.311 1.00 59.95  ? 451 THR   B N    1 
ATOM   7163 C CA   . THR   B 1 451 ? -5.127  3.542   -65.490 1.00 58.62  ? 451 THR   B CA   1 
ATOM   7164 C C    . THR   B 1 451 ? -4.118  3.973   -64.431 1.00 57.23  ? 451 THR   B C    1 
ATOM   7165 O O    . THR   B 1 451 ? -4.063  3.431   -63.322 1.00 56.24  ? 451 THR   B O    1 
ATOM   7166 C CB   . THR   B 1 451 ? -6.320  4.507   -65.468 1.00 57.27  ? 451 THR   B CB   1 
ATOM   7167 O OG1  . THR   B 1 451 ? -5.892  5.778   -65.976 1.00 61.19  ? 451 THR   B OG1  1 
ATOM   7168 C CG2  . THR   B 1 451 ? -6.857  4.695   -64.054 1.00 55.41  ? 451 THR   B CG2  1 
ATOM   7169 N N    . VAL   B 1 452 ? -3.316  4.955   -64.821 1.00 45.51  ? 452 VAL   B N    1 
ATOM   7170 C CA   . VAL   B 1 452 ? -2.448  5.725   -63.938 1.00 44.64  ? 452 VAL   B CA   1 
ATOM   7171 C C    . VAL   B 1 452 ? -2.759  7.181   -64.261 1.00 43.83  ? 452 VAL   B C    1 
ATOM   7172 O O    . VAL   B 1 452 ? -2.484  7.647   -65.376 1.00 46.70  ? 452 VAL   B O    1 
ATOM   7173 C CB   . VAL   B 1 452 ? -0.968  5.401   -64.172 1.00 43.34  ? 452 VAL   B CB   1 
ATOM   7174 C CG1  . VAL   B 1 452 ? -0.070  6.331   -63.405 1.00 44.75  ? 452 VAL   B CG1  1 
ATOM   7175 C CG2  . VAL   B 1 452 ? -0.689  3.932   -63.853 1.00 43.65  ? 452 VAL   B CG2  1 
ATOM   7176 N N    . THR   B 1 453 ? -3.411  7.873   -63.345 1.00 54.05  ? 453 THR   B N    1 
ATOM   7177 C CA   . THR   B 1 453 ? -3.961  9.180   -63.661 1.00 54.21  ? 453 THR   B CA   1 
ATOM   7178 C C    . THR   B 1 453 ? -3.617  10.199  -62.587 1.00 56.23  ? 453 THR   B C    1 
ATOM   7179 O O    . THR   B 1 453 ? -3.637  9.891   -61.386 1.00 56.31  ? 453 THR   B O    1 
ATOM   7180 C CB   . THR   B 1 453 ? -5.483  9.101   -63.830 1.00 54.36  ? 453 THR   B CB   1 
ATOM   7181 O OG1  . THR   B 1 453 ? -5.795  8.311   -64.989 1.00 55.90  ? 453 THR   B OG1  1 
ATOM   7182 C CG2  . THR   B 1 453 ? -6.085  10.502  -63.983 1.00 52.97  ? 453 THR   B CG2  1 
ATOM   7183 N N    . LEU   B 1 454 ? -3.314  11.419  -63.031 1.00 47.57  ? 454 LEU   B N    1 
ATOM   7184 C CA   . LEU   B 1 454 ? -3.244  12.600  -62.176 1.00 47.57  ? 454 LEU   B CA   1 
ATOM   7185 C C    . LEU   B 1 454 ? -4.498  13.411  -62.476 1.00 47.31  ? 454 LEU   B C    1 
ATOM   7186 O O    . LEU   B 1 454 ? -4.657  13.925  -63.588 1.00 48.45  ? 454 LEU   B O    1 
ATOM   7187 C CB   . LEU   B 1 454 ? -1.976  13.411  -62.431 1.00 49.80  ? 454 LEU   B CB   1 
ATOM   7188 C CG   . LEU   B 1 454 ? -0.672  12.738  -61.984 1.00 50.71  ? 454 LEU   B CG   1 
ATOM   7189 C CD1  . LEU   B 1 454 ? 0.533   13.413  -62.626 1.00 50.14  ? 454 LEU   B CD1  1 
ATOM   7190 C CD2  . LEU   B 1 454 ? -0.535  12.734  -60.461 1.00 49.87  ? 454 LEU   B CD2  1 
ATOM   7191 N N    . PHE   B 1 455 ? -5.404  13.473  -61.497 1.00 50.38  ? 455 PHE   B N    1 
ATOM   7192 C CA   . PHE   B 1 455 ? -6.731  14.073  -61.630 1.00 47.68  ? 455 PHE   B CA   1 
ATOM   7193 C C    . PHE   B 1 455 ? -6.722  15.368  -60.827 1.00 51.35  ? 455 PHE   B C    1 
ATOM   7194 O O    . PHE   B 1 455 ? -6.692  15.338  -59.589 1.00 49.08  ? 455 PHE   B O    1 
ATOM   7195 C CB   . PHE   B 1 455 ? -7.792  13.092  -61.119 1.00 45.64  ? 455 PHE   B CB   1 
ATOM   7196 C CG   . PHE   B 1 455 ? -9.231  13.494  -61.400 1.00 46.00  ? 455 PHE   B CG   1 
ATOM   7197 C CD1  . PHE   B 1 455 ? -9.839  14.518  -60.691 1.00 46.27  ? 455 PHE   B CD1  1 
ATOM   7198 C CD2  . PHE   B 1 455 ? -9.986  12.806  -62.338 1.00 45.03  ? 455 PHE   B CD2  1 
ATOM   7199 C CE1  . PHE   B 1 455 ? -11.168 14.869  -60.933 1.00 42.36  ? 455 PHE   B CE1  1 
ATOM   7200 C CE2  . PHE   B 1 455 ? -11.317 13.151  -62.587 1.00 44.71  ? 455 PHE   B CE2  1 
ATOM   7201 C CZ   . PHE   B 1 455 ? -11.906 14.194  -61.870 1.00 42.79  ? 455 PHE   B CZ   1 
ATOM   7202 N N    . GLY   B 1 456 ? -6.752  16.502  -61.509 1.00 50.51  ? 456 GLY   B N    1 
ATOM   7203 C CA   . GLY   B 1 456 ? -6.631  17.794  -60.858 1.00 51.58  ? 456 GLY   B CA   1 
ATOM   7204 C C    . GLY   B 1 456 ? -7.895  18.604  -61.055 1.00 53.18  ? 456 GLY   B C    1 
ATOM   7205 O O    . GLY   B 1 456 ? -8.538  18.523  -62.109 1.00 51.50  ? 456 GLY   B O    1 
ATOM   7206 N N    . ARG   B 1 457 ? -8.263  19.346  -60.017 1.00 49.62  ? 457 ARG   B N    1 
ATOM   7207 C CA   . ARG   B 1 457 ? -9.431  20.211  -60.027 1.00 51.16  ? 457 ARG   B CA   1 
ATOM   7208 C C    . ARG   B 1 457 ? -8.966  21.655  -59.905 1.00 52.45  ? 457 ARG   B C    1 
ATOM   7209 O O    . ARG   B 1 457 ? -8.153  21.978  -59.027 1.00 53.45  ? 457 ARG   B O    1 
ATOM   7210 C CB   . ARG   B 1 457 ? -10.381 19.866  -58.880 1.00 50.65  ? 457 ARG   B CB   1 
ATOM   7211 C CG   . ARG   B 1 457 ? -11.156 18.597  -59.079 1.00 46.39  ? 457 ARG   B CG   1 
ATOM   7212 C CD   . ARG   B 1 457 ? -12.461 18.864  -59.791 1.00 47.09  ? 457 ARG   B CD   1 
ATOM   7213 N NE   . ARG   B 1 457 ? -13.420 19.651  -59.017 1.00 44.04  ? 457 ARG   B NE   1 
ATOM   7214 C CZ   . ARG   B 1 457 ? -13.655 20.940  -59.223 1.00 49.00  ? 457 ARG   B CZ   1 
ATOM   7215 N NH1  . ARG   B 1 457 ? -12.958 21.635  -60.107 1.00 49.04  ? 457 ARG   B NH1  1 
ATOM   7216 N NH2  . ARG   B 1 457 ? -14.654 21.533  -58.575 1.00 48.14  ? 457 ARG   B NH2  1 
ATOM   7217 N N    . LEU   B 1 458 ? -9.495  22.523  -60.760 1.00 48.80  ? 458 LEU   B N    1 
ATOM   7218 C CA   . LEU   B 1 458 ? -9.214  23.956  -60.698 1.00 49.73  ? 458 LEU   B CA   1 
ATOM   7219 C C    . LEU   B 1 458 ? -10.501 24.619  -60.217 1.00 49.69  ? 458 LEU   B C    1 
ATOM   7220 O O    . LEU   B 1 458 ? -11.319 25.083  -61.012 1.00 50.33  ? 458 LEU   B O    1 
ATOM   7221 C CB   . LEU   B 1 458 ? -8.764  24.480  -62.058 1.00 48.11  ? 458 LEU   B CB   1 
ATOM   7222 C CG   . LEU   B 1 458 ? -7.306  24.175  -62.402 1.00 49.99  ? 458 LEU   B CG   1 
ATOM   7223 C CD1  . LEU   B 1 458 ? -7.028  22.671  -62.364 1.00 49.76  ? 458 LEU   B CD1  1 
ATOM   7224 C CD2  . LEU   B 1 458 ? -6.949  24.764  -63.764 1.00 56.31  ? 458 LEU   B CD2  1 
ATOM   7225 N N    . TYR   B 1 459 ? -10.674 24.658  -58.889 1.00 50.99  ? 459 TYR   B N    1 
ATOM   7226 C CA   . TYR   B 1 459 ? -11.968 25.022  -58.312 1.00 49.80  ? 459 TYR   B CA   1 
ATOM   7227 C C    . TYR   B 1 459 ? -12.386 26.432  -58.697 1.00 50.42  ? 459 TYR   B C    1 
ATOM   7228 O O    . TYR   B 1 459 ? -13.579 26.705  -58.876 1.00 49.45  ? 459 TYR   B O    1 
ATOM   7229 C CB   . TYR   B 1 459 ? -11.928 24.881  -56.788 1.00 49.23  ? 459 TYR   B CB   1 
ATOM   7230 C CG   . TYR   B 1 459 ? -11.604 23.482  -56.324 1.00 47.38  ? 459 TYR   B CG   1 
ATOM   7231 C CD1  . TYR   B 1 459 ? -12.601 22.518  -56.220 1.00 43.14  ? 459 TYR   B CD1  1 
ATOM   7232 C CD2  . TYR   B 1 459 ? -10.303 23.131  -55.976 1.00 46.33  ? 459 TYR   B CD2  1 
ATOM   7233 C CE1  . TYR   B 1 459 ? -12.306 21.229  -55.807 1.00 42.64  ? 459 TYR   B CE1  1 
ATOM   7234 C CE2  . TYR   B 1 459 ? -9.998  21.861  -55.550 1.00 45.46  ? 459 TYR   B CE2  1 
ATOM   7235 C CZ   . TYR   B 1 459 ? -11.001 20.907  -55.475 1.00 45.32  ? 459 TYR   B CZ   1 
ATOM   7236 O OH   . TYR   B 1 459 ? -10.698 19.634  -55.038 1.00 43.44  ? 459 TYR   B OH   1 
ATOM   7237 N N    . GLU   B 1 460 ? -11.424 27.350  -58.789 1.00 65.74  ? 460 GLU   B N    1 
ATOM   7238 C CA   . GLU   B 1 460 ? -11.735 28.727  -59.153 1.00 66.53  ? 460 GLU   B CA   1 
ATOM   7239 C C    . GLU   B 1 460 ? -12.391 28.819  -60.530 1.00 69.36  ? 460 GLU   B C    1 
ATOM   7240 O O    . GLU   B 1 460 ? -13.110 29.785  -60.813 1.00 70.44  ? 460 GLU   B O    1 
ATOM   7241 C CB   . GLU   B 1 460 ? -10.465 29.576  -59.098 1.00 66.07  ? 460 GLU   B CB   1 
ATOM   7242 C CG   . GLU   B 1 460 ? -9.591  29.460  -60.329 1.00 70.60  ? 460 GLU   B CG   1 
ATOM   7243 C CD   . GLU   B 1 460 ? -8.492  28.404  -60.193 1.00 74.46  ? 460 GLU   B CD   1 
ATOM   7244 O OE1  . GLU   B 1 460 ? -8.686  27.418  -59.434 1.00 72.32  ? 460 GLU   B OE1  1 
ATOM   7245 O OE2  . GLU   B 1 460 ? -7.441  28.560  -60.865 1.00 74.80  ? 460 GLU   B OE2  1 
ATOM   7246 N N    . LYS   B 1 461 ? -12.142 27.846  -61.406 1.00 65.54  ? 461 LYS   B N    1 
ATOM   7247 C CA   . LYS   B 1 461 ? -12.582 27.927  -62.792 1.00 62.80  ? 461 LYS   B CA   1 
ATOM   7248 C C    . LYS   B 1 461 ? -13.953 27.307  -63.024 1.00 63.17  ? 461 LYS   B C    1 
ATOM   7249 O O    . LYS   B 1 461 ? -14.391 27.226  -64.173 1.00 65.54  ? 461 LYS   B O    1 
ATOM   7250 C CB   . LYS   B 1 461 ? -11.554 27.260  -63.703 1.00 59.72  ? 461 LYS   B CB   1 
ATOM   7251 C CG   . LYS   B 1 461 ? -10.499 28.217  -64.236 1.00 63.13  ? 461 LYS   B CG   1 
ATOM   7252 C CD   . LYS   B 1 461 ? -9.333  27.465  -64.870 1.00 64.18  ? 461 LYS   B CD   1 
ATOM   7253 C CE   . LYS   B 1 461 ? -8.477  28.383  -65.701 1.00 69.70  ? 461 LYS   B CE   1 
ATOM   7254 N NZ   . LYS   B 1 461 ? -8.855  28.341  -67.143 1.00 72.62  ? 461 LYS   B NZ   1 
ATOM   7255 N N    . ASP   B 1 462 ? -14.652 26.894  -61.976 1.00 59.71  ? 462 ASP   B N    1 
ATOM   7256 C CA   . ASP   B 1 462 ? -16.006 26.399  -62.168 1.00 60.71  ? 462 ASP   B CA   1 
ATOM   7257 C C    . ASP   B 1 462 ? -16.915 27.587  -62.458 1.00 63.16  ? 462 ASP   B C    1 
ATOM   7258 O O    . ASP   B 1 462 ? -18.101 27.421  -62.723 1.00 66.72  ? 462 ASP   B O    1 
ATOM   7259 C CB   . ASP   B 1 462 ? -16.506 25.626  -60.938 1.00 60.60  ? 462 ASP   B CB   1 
ATOM   7260 C CG   . ASP   B 1 462 ? -15.507 24.580  -60.440 1.00 62.43  ? 462 ASP   B CG   1 
ATOM   7261 O OD1  . ASP   B 1 462 ? -14.572 24.257  -61.212 1.00 60.26  ? 462 ASP   B OD1  1 
ATOM   7262 O OD2  . ASP   B 1 462 ? -15.667 24.079  -59.291 1.00 56.08  ? 462 ASP   B OD2  1 
HETATM 7263 C C10  . A1EAG C 2 .   ? -11.641 13.965  -1.043  1.00 60.43  ? 501 A1EAG A C10  1 
HETATM 7264 C C13  . A1EAG C 2 .   ? -8.951  14.160  -1.442  1.00 65.13  ? 501 A1EAG A C13  1 
HETATM 7265 C C15  . A1EAG C 2 .   ? -7.447  7.669   -3.146  1.00 54.69  ? 501 A1EAG A C15  1 
HETATM 7266 C C17  . A1EAG C 2 .   ? -8.825  9.206   -1.889  1.00 52.15  ? 501 A1EAG A C17  1 
HETATM 7267 C C20  . A1EAG C 2 .   ? -6.767  6.013   -6.417  1.00 53.88  ? 501 A1EAG A C20  1 
HETATM 7268 C C21  . A1EAG C 2 .   ? -5.968  5.031   -5.466  1.00 54.40  ? 501 A1EAG A C21  1 
HETATM 7269 C C22  . A1EAG C 2 .   ? -5.986  5.813   -4.076  1.00 58.57  ? 501 A1EAG A C22  1 
HETATM 7270 C C01  . A1EAG C 2 .   ? -7.523  9.262   -1.262  1.00 61.91  ? 501 A1EAG A C01  1 
HETATM 7271 C C02  . A1EAG C 2 .   ? -7.240  10.200  0.002   1.00 59.52  ? 501 A1EAG A C02  1 
HETATM 7272 C C05  . A1EAG C 2 .   ? -8.890  12.093  -0.879  1.00 61.56  ? 501 A1EAG A C05  1 
HETATM 7273 C C06  . A1EAG C 2 .   ? -9.287  13.257  -0.314  1.00 62.08  ? 501 A1EAG A C06  1 
HETATM 7274 C C07  . A1EAG C 2 .   ? -8.081  13.647  0.685   1.00 63.82  ? 501 A1EAG A C07  1 
HETATM 7275 C C08  . A1EAG C 2 .   ? -7.781  12.476  1.300   1.00 56.77  ? 501 A1EAG A C08  1 
HETATM 7276 C C09  . A1EAG C 2 .   ? -10.722 13.219  -0.047  1.00 50.72  ? 501 A1EAG A C09  1 
HETATM 7277 C C12  . A1EAG C 2 .   ? -9.773  13.816  -2.672  1.00 63.87  ? 501 A1EAG A C12  1 
HETATM 7278 C C19  . A1EAG C 2 .   ? -7.767  6.442   -5.599  1.00 50.09  ? 501 A1EAG A C19  1 
HETATM 7279 N N03  . A1EAG C 2 .   ? -7.924  11.447  0.147   1.00 58.05  ? 501 A1EAG A N03  1 
HETATM 7280 N N16  . A1EAG C 2 .   ? -8.759  8.177   -3.071  1.00 53.28  ? 501 A1EAG A N16  1 
HETATM 7281 N N18  . A1EAG C 2 .   ? -7.020  6.691   -4.144  1.00 53.69  ? 501 A1EAG A N18  1 
HETATM 7282 O O04  . A1EAG C 2 .   ? -6.509  9.881   0.868   1.00 64.75  ? 501 A1EAG A O04  1 
HETATM 7283 O O11  . A1EAG C 2 .   ? -11.141 14.294  -2.375  1.00 68.83  ? 501 A1EAG A O11  1 
HETATM 7284 O O23  . A1EAG C 2 .   ? -5.968  7.137   -6.858  1.00 60.01  ? 501 A1EAG A O23  1 
HETATM 7285 S S14  . A1EAG C 2 .   ? -6.585  8.323   -2.008  1.00 61.08  ? 501 A1EAG A S14  1 
HETATM 7286 H H102 . A1EAG C 2 .   ? -12.527 13.349  -1.180  1.00 72.91  ? 501 A1EAG A H102 1 
HETATM 7287 H H101 . A1EAG C 2 .   ? -11.925 14.903  -0.571  1.00 72.91  ? 501 A1EAG A H101 1 
HETATM 7288 H H131 . A1EAG C 2 .   ? -9.159  15.201  -1.147  1.00 78.55  ? 501 A1EAG A H131 1 
HETATM 7289 H H132 . A1EAG C 2 .   ? -7.880  14.056  -1.682  1.00 78.55  ? 501 A1EAG A H132 1 
HETATM 7290 H H171 . A1EAG C 2 .   ? -9.687  9.770   -1.596  1.00 62.97  ? 501 A1EAG A H171 1 
HETATM 7291 H H201 . A1EAG C 2 .   ? -7.124  5.493   -7.296  1.00 65.05  ? 501 A1EAG A H201 1 
HETATM 7292 H H211 . A1EAG C 2 .   ? -4.932  4.888   -5.825  1.00 65.68  ? 501 A1EAG A H211 1 
HETATM 7293 H H212 . A1EAG C 2 .   ? -6.486  4.057   -5.379  1.00 65.68  ? 501 A1EAG A H212 1 
HETATM 7294 H H222 . A1EAG C 2 .   ? -5.046  6.352   -3.940  1.00 70.67  ? 501 A1EAG A H222 1 
HETATM 7295 H H221 . A1EAG C 2 .   ? -6.148  5.109   -3.256  1.00 70.67  ? 501 A1EAG A H221 1 
HETATM 7296 H H052 . A1EAG C 2 .   ? -8.358  12.291  -1.832  1.00 74.26  ? 501 A1EAG A H052 1 
HETATM 7297 H H051 . A1EAG C 2 .   ? -9.764  11.433  -1.050  1.00 74.26  ? 501 A1EAG A H051 1 
HETATM 7298 H H072 . A1EAG C 2 .   ? -8.410  14.388  1.413   1.00 76.97  ? 501 A1EAG A H072 1 
HETATM 7299 H H071 . A1EAG C 2 .   ? -7.222  14.016  0.125   1.00 76.97  ? 501 A1EAG A H071 1 
HETATM 7300 H H082 . A1EAG C 2 .   ? -6.777  12.489  1.679   1.00 68.52  ? 501 A1EAG A H082 1 
HETATM 7301 H H081 . A1EAG C 2 .   ? -8.479  12.267  2.087   1.00 68.52  ? 501 A1EAG A H081 1 
HETATM 7302 H H091 . A1EAG C 2 .   ? -11.021 12.194  -0.036  1.00 61.25  ? 501 A1EAG A H091 1 
HETATM 7303 H H092 . A1EAG C 2 .   ? -10.881 13.643  0.920   1.00 61.25  ? 501 A1EAG A H092 1 
HETATM 7304 H H121 . A1EAG C 2 .   ? -9.361  14.338  -3.581  1.00 77.03  ? 501 A1EAG A H121 1 
HETATM 7305 H H122 . A1EAG C 2 .   ? -9.773  12.704  -2.849  1.00 77.03  ? 501 A1EAG A H122 1 
HETATM 7306 H H192 . A1EAG C 2 .   ? -8.546  5.670   -5.504  1.00 60.50  ? 501 A1EAG A H192 1 
HETATM 7307 H H191 . A1EAG C 2 .   ? -8.198  7.382   -5.976  1.00 60.50  ? 501 A1EAG A H191 1 
HETATM 7308 H H231 . A1EAG C 2 .   ? -6.488  7.593   -7.562  1.00 72.41  ? 501 A1EAG A H231 1 
HETATM 7309 C C10  . A1EAG D 2 .   ? -28.991 10.357  -56.883 1.00 61.96  ? 501 A1EAG B C10  1 
HETATM 7310 C C13  . A1EAG D 2 .   ? -28.706 9.119   -54.275 1.00 63.33  ? 501 A1EAG B C13  1 
HETATM 7311 C C15  . A1EAG D 2 .   ? -21.174 10.656  -57.874 1.00 53.90  ? 501 A1EAG B C15  1 
HETATM 7312 C C17  . A1EAG D 2 .   ? -22.845 9.341   -56.819 1.00 46.79  ? 501 A1EAG B C17  1 
HETATM 7313 C C20  . A1EAG D 2 .   ? -19.234 10.902  -61.030 1.00 52.65  ? 501 A1EAG B C20  1 
HETATM 7314 C C21  . A1EAG D 2 .   ? -18.424 11.946  -60.172 1.00 54.84  ? 501 A1EAG B C21  1 
HETATM 7315 C C22  . A1EAG D 2 .   ? -19.357 12.108  -58.906 1.00 50.20  ? 501 A1EAG B C22  1 
HETATM 7316 C C01  . A1EAG D 2 .   ? -22.941 10.604  -56.085 1.00 55.24  ? 501 A1EAG B C01  1 
HETATM 7317 C C02  . A1EAG D 2 .   ? -24.002 10.984  -54.904 1.00 55.72  ? 501 A1EAG B C02  1 
HETATM 7318 C C05  . A1EAG D 2 .   ? -26.638 10.406  -54.067 1.00 53.52  ? 501 A1EAG B C05  1 
HETATM 7319 C C06  . A1EAG D 2 .   ? -27.553 9.778   -54.923 1.00 64.28  ? 501 A1EAG B C06  1 
HETATM 7320 C C07  . A1EAG D 2 .   ? -26.731 8.577   -55.614 1.00 64.97  ? 501 A1EAG B C07  1 
HETATM 7321 C C08  . A1EAG D 2 .   ? -25.633 9.250   -56.017 1.00 59.64  ? 501 A1EAG B C08  1 
HETATM 7322 C C09  . A1EAG D 2 .   ? -28.105 10.874  -55.724 1.00 63.89  ? 501 A1EAG B C09  1 
HETATM 7323 C C12  . A1EAG D 2 .   ? -29.758 8.669   -55.312 1.00 72.44  ? 501 A1EAG B C12  1 
HETATM 7324 C C19  . A1EAG D 2 .   ? -19.712 10.026  -60.117 1.00 47.15  ? 501 A1EAG B C19  1 
HETATM 7325 N N03  . A1EAG D 2 .   ? -25.285 10.284  -54.908 1.00 58.57  ? 501 A1EAG B N03  1 
HETATM 7326 N N16  . A1EAG D 2 .   ? -21.742 9.371   -57.924 1.00 45.10  ? 501 A1EAG B N16  1 
HETATM 7327 N N18  . A1EAG D 2 .   ? -20.119 10.988  -58.839 1.00 49.14  ? 501 A1EAG B N18  1 
HETATM 7328 O O04  . A1EAG D 2 .   ? -23.794 11.818  -54.090 1.00 49.94  ? 501 A1EAG B O04  1 
HETATM 7329 O O11  . A1EAG D 2 .   ? -29.417 8.962   -56.749 1.00 60.47  ? 501 A1EAG B O11  1 
HETATM 7330 O O23  . A1EAG D 2 .   ? -20.391 11.491  -61.657 1.00 53.24  ? 501 A1EAG B O23  1 
HETATM 7331 S S14  . A1EAG D 2 .   ? -21.929 11.519  -56.756 1.00 59.17  ? 501 A1EAG B S14  1 
HETATM 7332 H H102 . A1EAG D 2 .   ? -28.430 10.454  -57.810 1.00 74.74  ? 501 A1EAG B H102 1 
HETATM 7333 H H101 . A1EAG D 2 .   ? -29.881 10.981  -56.935 1.00 74.74  ? 501 A1EAG B H101 1 
HETATM 7334 H H131 . A1EAG D 2 .   ? -28.350 8.236   -53.721 1.00 76.39  ? 501 A1EAG B H131 1 
HETATM 7335 H H132 . A1EAG D 2 .   ? -29.176 9.826   -53.573 1.00 76.39  ? 501 A1EAG B H132 1 
HETATM 7336 H H171 . A1EAG D 2 .   ? -23.464 8.490   -56.620 1.00 56.54  ? 501 A1EAG B H171 1 
HETATM 7337 H H201 . A1EAG D 2 .   ? -18.565 10.466  -61.761 1.00 63.57  ? 501 A1EAG B H201 1 
HETATM 7338 H H211 . A1EAG D 2 .   ? -17.433 11.546  -59.888 1.00 66.20  ? 501 A1EAG B H211 1 
HETATM 7339 H H212 . A1EAG D 2 .   ? -18.315 12.906  -60.712 1.00 66.20  ? 501 A1EAG B H212 1 
HETATM 7340 H H222 . A1EAG D 2 .   ? -18.747 12.197  -58.005 1.00 60.63  ? 501 A1EAG B H222 1 
HETATM 7341 H H221 . A1EAG D 2 .   ? -19.996 12.986  -59.026 1.00 60.63  ? 501 A1EAG B H221 1 
HETATM 7342 H H052 . A1EAG D 2 .   ? -26.559 9.868   -53.100 1.00 64.61  ? 501 A1EAG B H052 1 
HETATM 7343 H H051 . A1EAG D 2 .   ? -26.911 11.468  -53.900 1.00 64.61  ? 501 A1EAG B H051 1 
HETATM 7344 H H072 . A1EAG D 2 .   ? -26.480 7.798   -54.894 1.00 78.35  ? 501 A1EAG B H072 1 
HETATM 7345 H H071 . A1EAG D 2 .   ? -27.274 8.156   -56.460 1.00 78.35  ? 501 A1EAG B H071 1 
HETATM 7346 H H082 . A1EAG D 2 .   ? -25.840 9.762   -56.936 1.00 71.96  ? 501 A1EAG B H082 1 
HETATM 7347 H H081 . A1EAG D 2 .   ? -24.815 8.566   -56.142 1.00 71.96  ? 501 A1EAG B H081 1 
HETATM 7348 H H091 . A1EAG D 2 .   ? -28.694 11.500  -55.091 1.00 77.06  ? 501 A1EAG B H091 1 
HETATM 7349 H H092 . A1EAG D 2 .   ? -27.299 11.443  -56.132 1.00 77.06  ? 501 A1EAG B H092 1 
HETATM 7350 H H121 . A1EAG D 2 .   ? -29.896 7.556   -55.207 1.00 87.32  ? 501 A1EAG B H121 1 
HETATM 7351 H H122 . A1EAG D 2 .   ? -30.728 9.189   -55.071 1.00 87.32  ? 501 A1EAG B H122 1 
HETATM 7352 H H192 . A1EAG D 2 .   ? -18.934 9.304   -59.826 1.00 56.97  ? 501 A1EAG B H192 1 
HETATM 7353 H H191 . A1EAG D 2 .   ? -20.599 9.503   -60.507 1.00 56.97  ? 501 A1EAG B H191 1 
HETATM 7354 H H231 . A1EAG D 2 .   ? -20.859 10.759  -62.119 1.00 64.28  ? 501 A1EAG B H231 1 
HETATM 7355 O O    . HOH   E 3 .   ? -13.288 28.246  7.096   1.00 50.21  ? 601 HOH   A O    1 
HETATM 7356 O O    . HOH   E 3 .   ? -8.485  15.834  3.062   1.00 41.01  ? 602 HOH   A O    1 
HETATM 7357 O O    . HOH   E 3 .   ? -14.784 4.118   -0.741  1.00 36.94  ? 603 HOH   A O    1 
HETATM 7358 O O    . HOH   E 3 .   ? -0.325  11.351  26.210  1.00 44.99  ? 604 HOH   A O    1 
HETATM 7359 O O    . HOH   E 3 .   ? -11.015 -14.796 15.945  1.00 54.48  ? 605 HOH   A O    1 
HETATM 7360 O O    . HOH   E 3 .   ? -3.946  4.632   30.109  1.00 46.26  ? 606 HOH   A O    1 
HETATM 7361 O O    . HOH   E 3 .   ? 2.053   0.140   0.695   1.00 42.42  ? 607 HOH   A O    1 
HETATM 7362 O O    . HOH   E 3 .   ? 3.878   -1.371  19.933  1.00 59.33  ? 608 HOH   A O    1 
HETATM 7363 O O    . HOH   E 3 .   ? 7.104   16.829  23.800  1.00 64.96  ? 609 HOH   A O    1 
HETATM 7364 O O    . HOH   E 3 .   ? -10.064 20.725  26.322  1.00 37.43  ? 610 HOH   A O    1 
HETATM 7365 O O    . HOH   E 3 .   ? -11.791 -0.886  2.971   1.00 40.51  ? 611 HOH   A O    1 
HETATM 7366 O O    . HOH   E 3 .   ? 2.748   5.400   11.058  1.00 41.65  ? 612 HOH   A O    1 
HETATM 7367 O O    . HOH   E 3 .   ? 1.104   13.685  32.945  1.00 62.19  ? 613 HOH   A O    1 
HETATM 7368 O O    . HOH   E 3 .   ? -0.353  23.121  2.360   1.00 47.64  ? 614 HOH   A O    1 
HETATM 7369 O O    . HOH   E 3 .   ? -9.065  17.795  1.004   1.00 46.89  ? 615 HOH   A O    1 
HETATM 7370 O O    . HOH   E 3 .   ? -23.008 13.586  3.798   1.00 51.03  ? 616 HOH   A O    1 
HETATM 7371 O O    . HOH   E 3 .   ? -7.428  -10.494 -0.455  1.00 51.05  ? 617 HOH   A O    1 
HETATM 7372 O O    . HOH   E 3 .   ? -2.423  3.142   27.032  1.00 50.27  ? 618 HOH   A O    1 
HETATM 7373 O O    . HOH   E 3 .   ? 2.991   13.143  15.320  1.00 50.13  ? 619 HOH   A O    1 
HETATM 7374 O O    . HOH   E 3 .   ? -3.623  -6.763  17.540  1.00 44.20  ? 620 HOH   A O    1 
HETATM 7375 O O    . HOH   E 3 .   ? -12.650 -3.667  -17.445 1.00 53.37  ? 621 HOH   A O    1 
HETATM 7376 O O    . HOH   E 3 .   ? -22.748 8.489   9.644   1.00 45.38  ? 622 HOH   A O    1 
HETATM 7377 O O    . HOH   E 3 .   ? -15.237 -0.232  -1.636  1.00 41.46  ? 623 HOH   A O    1 
HETATM 7378 O O    . HOH   E 3 .   ? -9.609  18.047  5.120   1.00 46.21  ? 624 HOH   A O    1 
HETATM 7379 O O    . HOH   E 3 .   ? 2.998   4.428   3.689   1.00 50.40  ? 625 HOH   A O    1 
HETATM 7380 O O    . HOH   E 3 .   ? -0.281  23.039  31.630  1.00 37.89  ? 626 HOH   A O    1 
HETATM 7381 O O    . HOH   E 3 .   ? 4.491   10.852  8.350   1.00 53.19  ? 627 HOH   A O    1 
HETATM 7382 O O    . HOH   E 3 .   ? -15.364 26.539  6.832   1.00 46.19  ? 628 HOH   A O    1 
HETATM 7383 O O    . HOH   E 3 .   ? 2.408   9.504   18.416  1.00 42.06  ? 629 HOH   A O    1 
HETATM 7384 O O    . HOH   E 3 .   ? -3.431  13.093  32.156  1.00 44.15  ? 630 HOH   A O    1 
HETATM 7385 O O    . HOH   E 3 .   ? -12.022 15.559  10.230  1.00 42.80  ? 631 HOH   A O    1 
HETATM 7386 O O    . HOH   E 3 .   ? -0.162  15.792  6.886   1.00 41.00  ? 632 HOH   A O    1 
HETATM 7387 O O    . HOH   E 3 .   ? -26.851 27.017  4.239   1.00 72.33  ? 633 HOH   A O    1 
HETATM 7388 O O    . HOH   E 3 .   ? -16.606 -10.666 5.295   1.00 45.70  ? 634 HOH   A O    1 
HETATM 7389 O O    . HOH   E 3 .   ? -3.759  -14.025 19.647  1.00 54.48  ? 635 HOH   A O    1 
HETATM 7390 O O    . HOH   E 3 .   ? -0.573  6.524   -14.646 1.00 59.86  ? 636 HOH   A O    1 
HETATM 7391 O O    . HOH   E 3 .   ? -3.921  25.015  33.094  1.00 47.29  ? 637 HOH   A O    1 
HETATM 7392 O O    . HOH   E 3 .   ? -12.501 10.617  12.525  1.00 33.79  ? 638 HOH   A O    1 
HETATM 7393 O O    . HOH   E 3 .   ? -5.315  23.990  20.280  1.00 47.30  ? 639 HOH   A O    1 
HETATM 7394 O O    . HOH   E 3 .   ? -7.161  -11.983 13.454  1.00 56.47  ? 640 HOH   A O    1 
HETATM 7395 O O    . HOH   E 3 .   ? -26.434 16.860  15.981  1.00 53.79  ? 641 HOH   A O    1 
HETATM 7396 O O    . HOH   E 3 .   ? -13.717 26.581  2.714   1.00 64.44  ? 642 HOH   A O    1 
HETATM 7397 O O    . HOH   E 3 .   ? -25.789 4.202   20.709  1.00 68.72  ? 643 HOH   A O    1 
HETATM 7398 O O    . HOH   E 3 .   ? -11.153 -11.841 1.870   1.00 45.92  ? 644 HOH   A O    1 
HETATM 7399 O O    . HOH   E 3 .   ? -0.916  22.701  22.500  1.00 50.93  ? 645 HOH   A O    1 
HETATM 7400 O O    . HOH   E 3 .   ? -9.907  23.075  25.929  1.00 43.93  ? 646 HOH   A O    1 
HETATM 7401 O O    . HOH   E 3 .   ? -14.706 2.877   -10.317 1.00 56.05  ? 647 HOH   A O    1 
HETATM 7402 O O    . HOH   E 3 .   ? -20.801 -6.395  -21.341 1.00 57.28  ? 648 HOH   A O    1 
HETATM 7403 O O    . HOH   E 3 .   ? 2.845   25.575  2.768   1.00 52.08  ? 649 HOH   A O    1 
HETATM 7404 O O    . HOH   E 3 .   ? -15.765 11.248  32.834  1.00 51.25  ? 650 HOH   A O    1 
HETATM 7405 O O    . HOH   E 3 .   ? -27.280 -0.068  2.793   1.00 59.28  ? 651 HOH   A O    1 
HETATM 7406 O O    . HOH   E 3 .   ? 1.427   3.007   -19.364 1.00 45.73  ? 652 HOH   A O    1 
HETATM 7407 O O    . HOH   E 3 .   ? -2.412  15.625  32.275  1.00 45.31  ? 653 HOH   A O    1 
HETATM 7408 O O    . HOH   E 3 .   ? -9.721  24.400  28.226  1.00 48.20  ? 654 HOH   A O    1 
HETATM 7409 O O    . HOH   E 3 .   ? -10.079 -1.650  25.797  1.00 49.89  ? 655 HOH   A O    1 
HETATM 7410 O O    . HOH   F 3 .   ? -14.080 2.205   -28.557 1.00 51.77  ? 601 HOH   B O    1 
HETATM 7411 O O    . HOH   F 3 .   ? 3.703   3.196   -44.651 1.00 64.91  ? 602 HOH   B O    1 
HETATM 7412 O O    . HOH   F 3 .   ? -0.266  8.810   -34.520 1.00 57.00  ? 603 HOH   B O    1 
HETATM 7413 O O    . HOH   F 3 .   ? -6.276  -7.105  -61.229 1.00 49.44  ? 604 HOH   B O    1 
HETATM 7414 O O    . HOH   F 3 .   ? -19.332 17.110  -72.322 1.00 48.49  ? 605 HOH   B O    1 
HETATM 7415 O O    . HOH   F 3 .   ? -43.208 16.522  -52.905 1.00 55.63  ? 606 HOH   B O    1 
HETATM 7416 O O    . HOH   F 3 .   ? -19.377 2.793   -55.518 1.00 39.16  ? 607 HOH   B O    1 
HETATM 7417 O O    . HOH   F 3 .   ? 2.588   16.388  -61.890 1.00 56.40  ? 608 HOH   B O    1 
HETATM 7418 O O    . HOH   F 3 .   ? -6.958  11.039  -36.955 1.00 52.04  ? 609 HOH   B O    1 
HETATM 7419 O O    . HOH   F 3 .   ? 4.664   24.713  -67.268 1.00 59.15  ? 610 HOH   B O    1 
HETATM 7420 O O    . HOH   F 3 .   ? -12.589 11.133  -65.880 1.00 39.31  ? 611 HOH   B O    1 
HETATM 7421 O O    . HOH   F 3 .   ? -25.032 20.854  -39.437 1.00 49.43  ? 612 HOH   B O    1 
HETATM 7422 O O    . HOH   F 3 .   ? -18.872 12.349  -24.385 1.00 50.62  ? 613 HOH   B O    1 
HETATM 7423 O O    . HOH   F 3 .   ? -12.248 18.203  -53.527 1.00 45.40  ? 614 HOH   B O    1 
HETATM 7424 O O    . HOH   F 3 .   ? 0.601   17.868  -77.738 1.00 59.67  ? 615 HOH   B O    1 
HETATM 7425 O O    . HOH   F 3 .   ? -36.619 17.258  -32.376 1.00 62.05  ? 616 HOH   B O    1 
HETATM 7426 O O    . HOH   F 3 .   ? -15.512 13.618  -29.679 1.00 54.33  ? 617 HOH   B O    1 
HETATM 7427 O O    . HOH   F 3 .   ? -10.386 3.368   -72.060 1.00 40.45  ? 618 HOH   B O    1 
HETATM 7428 O O    . HOH   F 3 .   ? -35.962 20.433  -52.357 1.00 48.74  ? 619 HOH   B O    1 
HETATM 7429 O O    . HOH   F 3 .   ? -12.451 28.703  -44.001 1.00 67.22  ? 620 HOH   B O    1 
HETATM 7430 O O    . HOH   F 3 .   ? -18.557 16.913  -69.344 1.00 43.05  ? 621 HOH   B O    1 
HETATM 7431 O O    . HOH   F 3 .   ? -40.810 14.027  -39.693 1.00 52.22  ? 622 HOH   B O    1 
HETATM 7432 O O    . HOH   F 3 .   ? -36.297 24.849  -37.283 1.00 57.78  ? 623 HOH   B O    1 
HETATM 7433 O O    . HOH   F 3 .   ? -17.981 19.571  -43.051 1.00 41.96  ? 624 HOH   B O    1 
HETATM 7434 O O    . HOH   F 3 .   ? -45.053 -4.320  -50.361 1.00 74.34  ? 625 HOH   B O    1 
HETATM 7435 O O    . HOH   F 3 .   ? -19.965 -7.136  -51.005 1.00 48.98  ? 626 HOH   B O    1 
HETATM 7436 O O    . HOH   F 3 .   ? -17.911 24.738  -58.028 1.00 63.28  ? 627 HOH   B O    1 
HETATM 7437 O O    . HOH   F 3 .   ? -42.137 3.511   -49.780 1.00 63.40  ? 628 HOH   B O    1 
HETATM 7438 O O    . HOH   F 3 .   ? -24.650 14.781  -45.313 1.00 36.36  ? 629 HOH   B O    1 
HETATM 7439 O O    . HOH   F 3 .   ? -14.338 4.037   -51.724 1.00 39.59  ? 630 HOH   B O    1 
HETATM 7440 O O    . HOH   F 3 .   ? -12.612 -7.079  -55.403 1.00 52.84  ? 631 HOH   B O    1 
HETATM 7441 O O    . HOH   F 3 .   ? -32.548 4.886   -24.430 1.00 59.82  ? 632 HOH   B O    1 
HETATM 7442 O O    . HOH   F 3 .   ? -24.257 29.448  -29.255 1.00 53.32  ? 633 HOH   B O    1 
HETATM 7443 O O    . HOH   F 3 .   ? -22.885 22.383  -46.040 1.00 44.11  ? 634 HOH   B O    1 
HETATM 7444 O O    . HOH   F 3 .   ? -0.851  -3.963  -53.692 1.00 62.01  ? 635 HOH   B O    1 
HETATM 7445 O O    . HOH   F 3 .   ? -43.073 8.112   -48.221 1.00 48.26  ? 636 HOH   B O    1 
HETATM 7446 O O    . HOH   F 3 .   ? -6.253  5.667   -56.753 1.00 39.01  ? 637 HOH   B O    1 
HETATM 7447 O O    . HOH   F 3 .   ? -7.058  -2.488  -75.466 1.00 49.46  ? 638 HOH   B O    1 
HETATM 7448 O O    . HOH   F 3 .   ? -16.700 28.828  -66.209 1.00 61.08  ? 639 HOH   B O    1 
HETATM 7449 O O    . HOH   F 3 .   ? -41.596 6.062   -48.657 1.00 53.51  ? 640 HOH   B O    1 
HETATM 7450 O O    . HOH   F 3 .   ? -4.001  2.138   -56.018 1.00 42.99  ? 641 HOH   B O    1 
HETATM 7451 O O    . HOH   F 3 .   ? -35.763 23.335  -34.898 1.00 46.50  ? 642 HOH   B O    1 
HETATM 7452 O O    . HOH   F 3 .   ? -16.807 13.831  -27.218 1.00 40.25  ? 643 HOH   B O    1 
HETATM 7453 O O    . HOH   F 3 .   ? -16.858 19.786  -50.570 1.00 40.66  ? 644 HOH   B O    1 
HETATM 7454 O O    . HOH   F 3 .   ? -11.481 1.950   -67.408 1.00 48.65  ? 645 HOH   B O    1 
HETATM 7455 O O    . HOH   F 3 .   ? -20.102 3.680   -23.452 1.00 52.93  ? 646 HOH   B O    1 
HETATM 7456 O O    . HOH   F 3 .   ? -28.399 19.070  -47.761 1.00 38.01  ? 647 HOH   B O    1 
HETATM 7457 O O    . HOH   F 3 .   ? -24.799 -6.898  -39.931 1.00 61.71  ? 648 HOH   B O    1 
HETATM 7458 O O    . HOH   F 3 .   ? -27.428 1.669   -22.269 1.00 57.16  ? 649 HOH   B O    1 
HETATM 7459 O O    . HOH   F 3 .   ? -13.395 13.087  -67.779 1.00 41.75  ? 650 HOH   B O    1 
HETATM 7460 O O    . HOH   F 3 .   ? -32.547 10.289  -50.045 1.00 42.83  ? 651 HOH   B O    1 
HETATM 7461 O O    . HOH   F 3 .   ? 5.520   17.737  -62.280 1.00 63.83  ? 652 HOH   B O    1 
HETATM 7462 O O    . HOH   F 3 .   ? -15.298 1.442   -56.325 1.00 44.80  ? 653 HOH   B O    1 
HETATM 7463 O O    . HOH   F 3 .   ? -2.636  6.274   -40.787 1.00 58.80  ? 654 HOH   B O    1 
HETATM 7464 O O    . HOH   F 3 .   ? -13.413 6.867   -26.815 1.00 56.66  ? 655 HOH   B O    1 
HETATM 7465 O O    . HOH   F 3 .   ? -37.997 15.220  -34.703 1.00 48.45  ? 656 HOH   B O    1 
HETATM 7466 O O    . HOH   F 3 .   ? -16.583 -7.803  -58.504 1.00 51.08  ? 657 HOH   B O    1 
HETATM 7467 O O    . HOH   F 3 .   ? -31.485 10.876  -53.867 1.00 49.27  ? 658 HOH   B O    1 
HETATM 7468 O O    . HOH   F 3 .   ? -29.874 16.289  -22.192 1.00 49.58  ? 659 HOH   B O    1 
HETATM 7469 O O    . HOH   F 3 .   ? -37.060 9.729   -28.757 1.00 54.80  ? 660 HOH   B O    1 
HETATM 7470 O O    . HOH   F 3 .   ? -16.534 18.834  -71.504 1.00 44.55  ? 661 HOH   B O    1 
HETATM 7471 O O    . HOH   F 3 .   ? -28.884 -0.767  -27.850 1.00 66.52  ? 662 HOH   B O    1 
HETATM 7472 O O    . HOH   F 3 .   ? -13.644 3.212   -25.942 1.00 46.13  ? 663 HOH   B O    1 
HETATM 7473 O O    . HOH   F 3 .   ? -25.122 4.186   -62.265 1.00 50.93  ? 664 HOH   B O    1 
HETATM 7474 O O    . HOH   F 3 .   ? -6.384  15.851  -31.748 1.00 59.48  ? 665 HOH   B O    1 
HETATM 7475 O O    . HOH   F 3 .   ? -19.428 -0.691  -60.612 1.00 44.02  ? 666 HOH   B O    1 
HETATM 7476 O O    . HOH   F 3 .   ? -24.988 16.405  -60.623 1.00 47.69  ? 667 HOH   B O    1 
HETATM 7477 O O    . HOH   F 3 .   ? -1.605  24.880  -66.091 1.00 57.03  ? 668 HOH   B O    1 
HETATM 7478 O O    . HOH   F 3 .   ? -14.052 8.945   -65.498 1.00 36.18  ? 669 HOH   B O    1 
HETATM 7479 O O    . HOH   F 3 .   ? -15.000 18.561  -73.599 1.00 49.97  ? 670 HOH   B O    1 
HETATM 7480 O O    . HOH   F 3 .   ? -14.141 -7.535  -58.611 1.00 56.78  ? 671 HOH   B O    1 
HETATM 7481 O O    . HOH   F 3 .   ? -13.996 13.774  -26.265 1.00 70.71  ? 672 HOH   B O    1 
HETATM 7482 O O    . HOH   F 3 .   ? -31.768 23.434  -33.762 1.00 50.72  ? 673 HOH   B O    1 
HETATM 7483 O O    . HOH   F 3 .   ? -21.460 5.260   -21.193 1.00 55.53  ? 674 HOH   B O    1 
HETATM 7484 O O    . HOH   F 3 .   ? -16.134 31.402  -65.475 1.00 66.59  ? 675 HOH   B 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   . GLN A 1   ? 1.1650 0.8303 0.7169 0.1640  -0.1850 0.1289  1   GLN A N   
2    C CA  . GLN A 1   ? 1.1957 0.8194 0.7387 0.1359  -0.1810 0.1342  1   GLN A CA  
3    C C   . GLN A 1   ? 1.1613 0.7653 0.7151 0.1525  -0.1842 0.1104  1   GLN A C   
4    O O   . GLN A 1   ? 1.1145 0.7663 0.6972 0.1700  -0.1751 0.0872  1   GLN A O   
5    C CB  . GLN A 1   ? 1.0667 0.7389 0.6305 0.0997  -0.1585 0.1382  1   GLN A CB  
6    C CG  . GLN A 1   ? 1.0557 0.7862 0.6588 0.1020  -0.1417 0.1147  1   GLN A CG  
7    C CD  . GLN A 1   ? 0.9944 0.7735 0.6181 0.0710  -0.1217 0.1198  1   GLN A CD  
8    O OE1 . GLN A 1   ? 0.9922 0.8131 0.6232 0.0677  -0.1134 0.1247  1   GLN A OE1 
9    N NE2 . GLN A 1   ? 0.9842 0.7573 0.6171 0.0487  -0.1154 0.1179  1   GLN A NE2 
10   N N   . ASP A 2   ? 1.1419 0.6731 0.6697 0.1458  -0.1970 0.1160  2   ASP A N   
11   C CA  . ASP A 2   ? 1.1432 0.6431 0.6720 0.1650  -0.2042 0.0932  2   ASP A CA  
12   C C   . ASP A 2   ? 1.1587 0.6778 0.7050 0.1424  -0.1903 0.0797  2   ASP A C   
13   O O   . ASP A 2   ? 1.1303 0.6435 0.6819 0.1595  -0.1913 0.0561  2   ASP A O   
14   C CB  . ASP A 2   ? 1.2110 0.6172 0.7015 0.1698  -0.2266 0.1035  2   ASP A CB  
15   C CG  . ASP A 2   ? 1.3159 0.6957 0.7865 0.1996  -0.2446 0.1146  2   ASP A CG  
16   O OD1 . ASP A 2   ? 1.3660 0.8010 0.8584 0.2278  -0.2423 0.1026  2   ASP A OD1 
17   O OD2 . ASP A 2   ? 1.4196 0.7242 0.8526 0.1939  -0.2614 0.1358  2   ASP A OD2 
18   N N   . THR A 3   ? 1.0458 0.5890 0.6004 0.1057  -0.1779 0.0932  3   THR A N   
19   C CA  . THR A 3   ? 1.0321 0.5958 0.6037 0.0838  -0.1672 0.0827  3   THR A CA  
20   C C   . THR A 3   ? 0.9698 0.6012 0.5681 0.0622  -0.1482 0.0903  3   THR A C   
21   O O   . THR A 3   ? 0.9129 0.5624 0.5101 0.0556  -0.1441 0.1068  3   THR A O   
22   C CB  . THR A 3   ? 1.0512 0.5536 0.6027 0.0570  -0.1777 0.0906  3   THR A CB  
23   O OG1 . THR A 3   ? 1.0350 0.5296 0.5780 0.0269  -0.1756 0.1172  3   THR A OG1 
24   C CG2 . THR A 3   ? 1.0941 0.5200 0.6158 0.0787  -0.1979 0.0840  3   THR A CG2 
25   N N   . PHE A 4   ? 1.0301 0.6966 0.6502 0.0518  -0.1374 0.0780  4   PHE A N   
26   C CA  . PHE A 4   ? 0.9764 0.7038 0.6238 0.0331  -0.1202 0.0829  4   PHE A CA  
27   C C   . PHE A 4   ? 1.0150 0.7515 0.6756 0.0115  -0.1170 0.0773  4   PHE A C   
28   O O   . PHE A 4   ? 1.0028 0.7119 0.6540 0.0167  -0.1254 0.0640  4   PHE A O   
29   C CB  . PHE A 4   ? 0.9359 0.7188 0.6039 0.0547  -0.1077 0.0714  4   PHE A CB  
30   C CG  . PHE A 4   ? 0.9395 0.7335 0.6147 0.0730  -0.1044 0.0491  4   PHE A CG  
31   C CD1 . PHE A 4   ? 0.9702 0.7364 0.6312 0.1006  -0.1136 0.0354  4   PHE A CD1 
32   C CD2 . PHE A 4   ? 0.8530 0.6861 0.5481 0.0635  -0.0915 0.0419  4   PHE A CD2 
33   C CE1 . PHE A 4   ? 0.9183 0.6980 0.5839 0.1161  -0.1077 0.0138  4   PHE A CE1 
34   C CE2 . PHE A 4   ? 0.8212 0.6632 0.5172 0.0784  -0.0870 0.0234  4   PHE A CE2 
35   C CZ  . PHE A 4   ? 0.8792 0.6964 0.5602 0.1036  -0.0939 0.0090  4   PHE A CZ  
36   N N   . ILE A 5   ? 1.0223 0.8002 0.7050 -0.0113 -0.1054 0.0860  5   ILE A N   
37   C CA  . ILE A 5   ? 1.0079 0.8037 0.7086 -0.0312 -0.1033 0.0818  5   ILE A CA  
38   C C   . ILE A 5   ? 0.9635 0.8021 0.6824 -0.0157 -0.0933 0.0679  5   ILE A C   
39   O O   . ILE A 5   ? 0.9271 0.8093 0.6644 -0.0119 -0.0797 0.0697  5   ILE A O   
40   C CB  . ILE A 5   ? 1.0122 0.8384 0.7330 -0.0600 -0.0945 0.0958  5   ILE A CB  
41   C CG1 . ILE A 5   ? 1.0579 0.8444 0.7597 -0.0807 -0.1011 0.1122  5   ILE A CG1 
42   C CG2 . ILE A 5   ? 1.0000 0.8442 0.7418 -0.0772 -0.0963 0.0894  5   ILE A CG2 
43   C CD1 . ILE A 5   ? 1.1606 0.8821 0.8341 -0.0774 -0.1185 0.1094  5   ILE A CD1 
44   N N   . ALA A 6   ? 0.8005 0.6262 0.5127 -0.0090 -0.0995 0.0542  6   ALA A N   
45   C CA  . ALA A 6   ? 0.6968 0.5584 0.4210 0.0029  -0.0895 0.0433  6   ALA A CA  
46   C C   . ALA A 6   ? 0.6611 0.5432 0.4019 -0.0151 -0.0906 0.0443  6   ALA A C   
47   O O   . ALA A 6   ? 0.7127 0.5728 0.4494 -0.0316 -0.1032 0.0456  6   ALA A O   
48   C CB  . ALA A 6   ? 0.7256 0.5640 0.4281 0.0249  -0.0936 0.0266  6   ALA A CB  
49   N N   . ALA A 7   ? 0.7009 0.6246 0.4613 -0.0118 -0.0786 0.0432  7   ALA A N   
50   C CA  . ALA A 7   ? 0.7079 0.6523 0.4847 -0.0237 -0.0814 0.0437  7   ALA A CA  
51   C C   . ALA A 7   ? 0.6746 0.6337 0.4476 -0.0091 -0.0750 0.0359  7   ALA A C   
52   O O   . ALA A 7   ? 0.6402 0.6117 0.4123 0.0049  -0.0618 0.0328  7   ALA A O   
53   C CB  . ALA A 7   ? 0.6635 0.6450 0.4729 -0.0390 -0.0736 0.0539  7   ALA A CB  
54   N N   . VAL A 8   ? 0.7071 0.6633 0.4756 -0.0131 -0.0852 0.0326  8   VAL A N   
55   C CA  . VAL A 8   ? 0.6876 0.6575 0.4511 -0.0029 -0.0797 0.0293  8   VAL A CA  
56   C C   . VAL A 8   ? 0.6824 0.6711 0.4650 -0.0131 -0.0891 0.0344  8   VAL A C   
57   O O   . VAL A 8   ? 0.6817 0.6661 0.4720 -0.0269 -0.1041 0.0350  8   VAL A O   
58   C CB  . VAL A 8   ? 0.6876 0.6299 0.4137 0.0094  -0.0835 0.0178  8   VAL A CB  
59   C CG1 . VAL A 8   ? 0.6947 0.6274 0.4090 0.0235  -0.0723 0.0107  8   VAL A CG1 
60   C CG2 . VAL A 8   ? 0.7309 0.6435 0.4390 0.0009  -0.1046 0.0120  8   VAL A CG2 
61   N N   . TYR A 9   ? 0.6136 0.6240 0.4061 -0.0064 -0.0805 0.0377  9   TYR A N   
62   C CA  . TYR A 9   ? 0.5952 0.6248 0.4078 -0.0111 -0.0901 0.0424  9   TYR A CA  
63   C C   . TYR A 9   ? 0.6098 0.6272 0.3948 -0.0004 -0.0949 0.0415  9   TYR A C   
64   O O   . TYR A 9   ? 0.5867 0.5983 0.3539 0.0097  -0.0804 0.0411  9   TYR A O   
65   C CB  . TYR A 9   ? 0.5587 0.6228 0.4098 -0.0127 -0.0773 0.0484  9   TYR A CB  
66   C CG  . TYR A 9   ? 0.5473 0.6337 0.4254 -0.0160 -0.0891 0.0514  9   TYR A CG  
67   C CD1 . TYR A 9   ? 0.5489 0.6415 0.4405 -0.0291 -0.1064 0.0498  9   TYR A CD1 
68   C CD2 . TYR A 9   ? 0.5190 0.6198 0.4102 -0.0060 -0.0839 0.0550  9   TYR A CD2 
69   C CE1 . TYR A 9   ? 0.5524 0.6713 0.4732 -0.0306 -0.1190 0.0506  9   TYR A CE1 
70   C CE2 . TYR A 9   ? 0.5398 0.6615 0.4577 -0.0053 -0.0970 0.0568  9   TYR A CE2 
71   C CZ  . TYR A 9   ? 0.5593 0.6931 0.4935 -0.0169 -0.1150 0.0540  9   TYR A CZ  
72   O OH  . TYR A 9   ? 0.5516 0.7122 0.5171 -0.0148 -0.1298 0.0540  9   TYR A OH  
73   N N   . GLU A 10  ? 0.6468 0.6592 0.4251 -0.0040 -0.1159 0.0405  10  GLU A N   
74   C CA  . GLU A 10  ? 0.6426 0.6457 0.3947 0.0051  -0.1244 0.0425  10  GLU A CA  
75   C C   . GLU A 10  ? 0.6529 0.6824 0.4379 0.0075  -0.1287 0.0514  10  GLU A C   
76   O O   . GLU A 10  ? 0.6174 0.6690 0.4361 -0.0004 -0.1422 0.0511  10  GLU A O   
77   C CB  . GLU A 10  ? 0.6584 0.6404 0.3805 0.0016  -0.1473 0.0350  10  GLU A CB  
78   C CG  . GLU A 10  ? 0.7005 0.6732 0.3910 0.0106  -0.1605 0.0385  10  GLU A CG  
79   C CD  . GLU A 10  ? 0.7635 0.7061 0.4035 0.0111  -0.1741 0.0278  10  GLU A CD  
80   O OE1 . GLU A 10  ? 0.7820 0.7044 0.3979 0.0124  -0.1628 0.0182  10  GLU A OE1 
81   O OE2 . GLU A 10  ? 0.7706 0.7105 0.3943 0.0115  -0.1970 0.0278  10  GLU A OE2 
82   N N   . HIS A 11  ? 0.6622 0.6897 0.4396 0.0181  -0.1165 0.0583  11  HIS A N   
83   C CA  . HIS A 11  ? 0.6392 0.6881 0.4504 0.0232  -0.1153 0.0658  11  HIS A CA  
84   C C   . HIS A 11  ? 0.6861 0.7211 0.4746 0.0338  -0.1311 0.0736  11  HIS A C   
85   O O   . HIS A 11  ? 0.7088 0.7171 0.4552 0.0396  -0.1241 0.0783  11  HIS A O   
86   C CB  . HIS A 11  ? 0.5949 0.6489 0.4175 0.0259  -0.0887 0.0676  11  HIS A CB  
87   C CG  . HIS A 11  ? 0.6251 0.6939 0.4777 0.0329  -0.0859 0.0735  11  HIS A CG  
88   N ND1 . HIS A 11  ? 0.6100 0.7060 0.5032 0.0333  -0.0992 0.0731  11  HIS A ND1 
89   C CD2 . HIS A 11  ? 0.6222 0.6813 0.4707 0.0400  -0.0716 0.0789  11  HIS A CD2 
90   C CE1 . HIS A 11  ? 0.6363 0.7380 0.5496 0.0429  -0.0936 0.0771  11  HIS A CE1 
91   N NE2 . HIS A 11  ? 0.6311 0.7079 0.5166 0.0463  -0.0772 0.0812  11  HIS A NE2 
92   N N   . ALA A 12  ? 0.6698 0.7242 0.4859 0.0361  -0.1526 0.0752  12  ALA A N   
93   C CA  . ALA A 12  ? 0.6965 0.7415 0.4995 0.0495  -0.1701 0.0846  12  ALA A CA  
94   C C   . ALA A 12  ? 0.7381 0.7851 0.5617 0.0593  -0.1542 0.0923  12  ALA A C   
95   O O   . ALA A 12  ? 0.6892 0.7667 0.5639 0.0615  -0.1539 0.0897  12  ALA A O   
96   C CB  . ALA A 12  ? 0.6812 0.7522 0.5136 0.0499  -0.1998 0.0812  12  ALA A CB  
97   N N   . ALA A 13  ? 0.7446 0.7603 0.5301 0.0633  -0.1386 0.1001  13  ALA A N   
98   C CA  . ALA A 13  ? 0.7490 0.7632 0.5536 0.0679  -0.1183 0.1046  13  ALA A CA  
99   C C   . ALA A 13  ? 0.7969 0.8014 0.6086 0.0835  -0.1332 0.1155  13  ALA A C   
100  O O   . ALA A 13  ? 0.8284 0.8105 0.6056 0.0917  -0.1538 0.1251  13  ALA A O   
101  C CB  . ALA A 13  ? 0.7261 0.7134 0.4924 0.0630  -0.0931 0.1073  13  ALA A CB  
102  N N   . ILE A 14  ? 0.7910 0.8109 0.6461 0.0886  -0.1231 0.1134  14  ILE A N   
103  C CA  . ILE A 14  ? 0.8025 0.8081 0.6675 0.1057  -0.1330 0.1226  14  ILE A CA  
104  C C   . ILE A 14  ? 0.8492 0.8079 0.6708 0.1055  -0.1158 0.1347  14  ILE A C   
105  O O   . ILE A 14  ? 0.8008 0.7584 0.6280 0.0958  -0.0885 0.1297  14  ILE A O   
106  C CB  . ILE A 14  ? 0.8268 0.8679 0.7563 0.1110  -0.1266 0.1121  14  ILE A CB  
107  C CG1 . ILE A 14  ? 0.7683 0.8598 0.7399 0.1044  -0.1367 0.0992  14  ILE A CG1 
108  C CG2 . ILE A 14  ? 0.7900 0.8157 0.7333 0.1323  -0.1402 0.1196  14  ILE A CG2 
109  C CD1 . ILE A 14  ? 0.7311 0.8628 0.7636 0.1067  -0.1265 0.0870  14  ILE A CD1 
110  N N   . LEU A 15  ? 0.9265 0.8468 0.7032 0.1147  -0.1317 0.1507  15  LEU A N   
111  C CA  . LEU A 15  ? 0.9878 0.8593 0.7163 0.1117  -0.1159 0.1649  15  LEU A CA  
112  C C   . LEU A 15  ? 1.0454 0.8940 0.7932 0.1251  -0.1161 0.1730  15  LEU A C   
113  O O   . LEU A 15  ? 1.1034 0.9583 0.8770 0.1439  -0.1410 0.1754  15  LEU A O   
114  C CB  . LEU A 15  ? 1.0281 0.8647 0.6895 0.1135  -0.1322 0.1800  15  LEU A CB  
115  C CG  . LEU A 15  ? 1.0011 0.8521 0.6351 0.1009  -0.1309 0.1708  15  LEU A CG  
116  C CD1 . LEU A 15  ? 1.0316 0.8463 0.5930 0.1023  -0.1446 0.1845  15  LEU A CD1 
117  C CD2 . LEU A 15  ? 0.9691 0.8305 0.6080 0.0841  -0.0963 0.1596  15  LEU A CD2 
118  N N   . PRO A 16  ? 1.0011 0.8234 0.7388 0.1161  -0.0895 0.1759  16  PRO A N   
119  C CA  . PRO A 16  ? 1.0614 0.8540 0.8149 0.1280  -0.0890 0.1828  16  PRO A CA  
120  C C   . PRO A 16  ? 1.1619 0.9049 0.8741 0.1448  -0.1143 0.2057  16  PRO A C   
121  O O   . PRO A 16  ? 1.2219 0.9330 0.8718 0.1388  -0.1179 0.2213  16  PRO A O   
122  C CB  . PRO A 16  ? 1.0492 0.8207 0.7894 0.1089  -0.0543 0.1814  16  PRO A CB  
123  C CG  . PRO A 16  ? 1.0443 0.8334 0.7572 0.0895  -0.0383 0.1760  16  PRO A CG  
124  C CD  . PRO A 16  ? 0.9882 0.8164 0.7131 0.0946  -0.0582 0.1680  16  PRO A CD  
125  N N   . ASN A 17  ? 1.2865 1.0236 1.0330 0.1674  -0.1326 0.2072  17  ASN A N   
126  C CA  . ASN A 17  ? 1.3354 1.0212 1.0463 0.1876  -0.1593 0.2299  17  ASN A CA  
127  C C   . ASN A 17  ? 1.3370 0.9545 0.9784 0.1740  -0.1426 0.2518  17  ASN A C   
128  O O   . ASN A 17  ? 1.3558 0.9627 0.9961 0.1541  -0.1098 0.2471  17  ASN A O   
129  C CB  . ASN A 17  ? 1.3514 1.0351 1.1146 0.2135  -0.1732 0.2254  17  ASN A CB  
130  C CG  . ASN A 17  ? 1.2931 1.0346 1.1111 0.2341  -0.2026 0.2119  17  ASN A CG  
131  O OD1 . ASN A 17  ? 1.3028 1.0418 1.1003 0.2486  -0.2349 0.2229  17  ASN A OD1 
132  N ND2 . ASN A 17  ? 1.1974 0.9931 1.0849 0.2344  -0.1911 0.1876  17  ASN A ND2 
133  N N   . ALA A 18  ? 1.7118 1.2857 1.2932 0.1830  -0.1652 0.2756  18  ALA A N   
134  C CA  . ALA A 18  ? 1.7796 1.2835 1.2889 0.1703  -0.1512 0.3002  18  ALA A CA  
135  C C   . ALA A 18  ? 1.8084 1.2609 1.3296 0.1780  -0.1446 0.3089  18  ALA A C   
136  O O   . ALA A 18  ? 1.8420 1.2805 1.3879 0.2066  -0.1721 0.3132  18  ALA A O   
137  C CB  . ALA A 18  ? 1.7619 1.2311 1.2015 0.1803  -0.1804 0.3243  18  ALA A CB  
138  N N   . THR A 19  ? 1.6020 1.0289 1.1104 0.1530  -0.1085 0.3090  19  THR A N   
139  C CA  . THR A 19  ? 1.6099 0.9775 1.1196 0.1548  -0.0993 0.3183  19  THR A CA  
140  C C   . THR A 19  ? 1.6736 0.9831 1.1139 0.1255  -0.0723 0.3388  19  THR A C   
141  O O   . THR A 19  ? 1.5990 0.9343 1.0167 0.0994  -0.0482 0.3336  19  THR A O   
142  C CB  . THR A 19  ? 1.5920 0.9940 1.1771 0.1522  -0.0795 0.2900  19  THR A CB  
143  O OG1 . THR A 19  ? 1.5615 0.9948 1.1507 0.1199  -0.0431 0.2750  19  THR A OG1 
144  C CG2 . THR A 19  ? 1.5278 0.9968 1.1826 0.1763  -0.1006 0.2674  19  THR A CG2 
145  N N   . LEU A 20  ? 1.9927 1.2231 1.4003 0.1300  -0.0760 0.3617  20  LEU A N   
146  C CA  . LEU A 20  ? 2.0153 1.1845 1.3546 0.0999  -0.0498 0.3839  20  LEU A CA  
147  C C   . LEU A 20  ? 2.0326 1.2169 1.4041 0.0687  -0.0077 0.3642  20  LEU A C   
148  O O   . LEU A 20  ? 2.0552 1.2402 1.3910 0.0362  0.0226  0.3672  20  LEU A O   
149  C CB  . LEU A 20  ? 2.0166 1.1241 1.3363 0.1096  -0.0662 0.4065  20  LEU A CB  
150  C CG  . LEU A 20  ? 2.1835 1.2939 1.4834 0.1351  -0.1051 0.4223  20  LEU A CG  
151  C CD1 . LEU A 20  ? 2.1697 1.2138 1.4513 0.1451  -0.1183 0.4453  20  LEU A CD1 
152  C CD2 . LEU A 20  ? 2.1693 1.3098 1.4195 0.1176  -0.1008 0.4285  20  LEU A CD2 
153  N N   . THR A 21  ? 1.8175 1.0163 1.2566 0.0780  -0.0054 0.3428  21  THR A N   
154  C CA  . THR A 21  ? 1.7608 0.9740 1.2346 0.0506  0.0306  0.3220  21  THR A CA  
155  C C   . THR A 21  ? 1.6608 0.9652 1.2074 0.0536  0.0365  0.2859  21  THR A C   
156  O O   . THR A 21  ? 1.6185 0.9654 1.2003 0.0805  0.0114  0.2759  21  THR A O   
157  C CB  . THR A 21  ? 1.7720 0.9183 1.2592 0.0561  0.0308  0.3257  21  THR A CB  
158  O OG1 . THR A 21  ? 1.7041 0.8779 1.2556 0.0900  0.0078  0.3064  21  THR A OG1 
159  C CG2 . THR A 21  ? 1.8130 0.8628 1.2272 0.0613  0.0159  0.3650  21  THR A CG2 
160  N N   . PRO A 22  ? 1.4479 0.7841 1.0185 0.0256  0.0693  0.2658  22  PRO A N   
161  C CA  . PRO A 22  ? 1.3204 0.7410 0.9524 0.0265  0.0756  0.2336  22  PRO A CA  
162  C C   . PRO A 22  ? 1.3096 0.7481 1.0029 0.0529  0.0590  0.2156  22  PRO A C   
163  O O   . PRO A 22  ? 1.3711 0.7608 1.0744 0.0606  0.0566  0.2172  22  PRO A O   
164  C CB  . PRO A 22  ? 1.2455 0.6799 0.8868 -0.0081 0.1125  0.2187  22  PRO A CB  
165  C CG  . PRO A 22  ? 1.3512 0.7287 0.9264 -0.0318 0.1279  0.2441  22  PRO A CG  
166  C CD  . PRO A 22  ? 1.4546 0.7636 0.9800 -0.0108 0.1004  0.2761  22  PRO A CD  
167  N N   . VAL A 23  ? 1.0448 0.5532 0.7789 0.0661  0.0485  0.1976  23  VAL A N   
168  C CA  . VAL A 23  ? 1.0166 0.5563 0.8122 0.0891  0.0360  0.1772  23  VAL A CA  
169  C C   . VAL A 23  ? 1.0172 0.5845 0.8555 0.0732  0.0616  0.1499  23  VAL A C   
170  O O   . VAL A 23  ? 1.0242 0.5983 0.8497 0.0450  0.0868  0.1451  23  VAL A O   
171  C CB  . VAL A 23  ? 0.9681 0.5722 0.7883 0.1052  0.0166  0.1694  23  VAL A CB  
172  C CG1 . VAL A 23  ? 1.0258 0.6044 0.8045 0.1212  -0.0114 0.1942  23  VAL A CG1 
173  C CG2 . VAL A 23  ? 0.8976 0.5601 0.7236 0.0834  0.0354  0.1551  23  VAL A CG2 
174  N N   . SER A 24  ? 1.0881 0.6743 0.9777 0.0915  0.0551  0.1303  24  SER A N   
175  C CA  . SER A 24  ? 1.0843 0.7026 1.0146 0.0785  0.0769  0.1018  24  SER A CA  
176  C C   . SER A 24  ? 1.0257 0.7215 0.9756 0.0674  0.0856  0.0860  24  SER A C   
177  O O   . SER A 24  ? 1.0264 0.7531 0.9682 0.0741  0.0724  0.0939  24  SER A O   
178  C CB  . SER A 24  ? 1.0856 0.7054 1.0635 0.1029  0.0675  0.0837  24  SER A CB  
179  O OG  . SER A 24  ? 1.0598 0.7349 1.0693 0.1249  0.0493  0.0769  24  SER A OG  
180  N N   . ARG A 25  ? 1.0881 0.8134 1.0632 0.0505  0.1068  0.0631  25  ARG A N   
181  C CA  . ARG A 25  ? 1.0069 0.8026 1.0010 0.0418  0.1138  0.0478  25  ARG A CA  
182  C C   . ARG A 25  ? 0.9779 0.8206 1.0079 0.0633  0.0980  0.0379  25  ARG A C   
183  O O   . ARG A 25  ? 0.9645 0.8542 0.9974 0.0612  0.0946  0.0366  25  ARG A O   
184  C CB  . ARG A 25  ? 1.0175 0.8335 1.0303 0.0210  0.1371  0.0251  25  ARG A CB  
185  C CG  . ARG A 25  ? 0.9957 0.8013 0.9774 -0.0061 0.1548  0.0317  25  ARG A CG  
186  C CD  . ARG A 25  ? 0.9969 0.8407 1.0021 -0.0258 0.1744  0.0069  25  ARG A CD  
187  N NE  . ARG A 25  ? 0.8756 0.7764 0.9156 -0.0152 0.1696  -0.0126 25  ARG A NE  
188  C CZ  . ARG A 25  ? 0.8890 0.8439 0.9341 -0.0208 0.1721  -0.0199 25  ARG A CZ  
189  N NH1 . ARG A 25  ? 0.8082 0.7718 0.8305 -0.0349 0.1793  -0.0124 25  ARG A NH1 
190  N NH2 . ARG A 25  ? 0.7882 0.7886 0.8607 -0.0114 0.1673  -0.0349 25  ARG A NH2 
191  N N   . GLU A 26  ? 0.9729 0.8031 1.0310 0.0839  0.0884  0.0306  26  GLU A N   
192  C CA  . GLU A 26  ? 0.9744 0.8537 1.0706 0.1033  0.0751  0.0198  26  GLU A CA  
193  C C   . GLU A 26  ? 0.9011 0.7836 0.9828 0.1168  0.0516  0.0398  26  GLU A C   
194  O O   . GLU A 26  ? 0.8595 0.7939 0.9577 0.1184  0.0451  0.0353  26  GLU A O   
195  C CB  . GLU A 26  ? 0.9574 0.8247 1.0901 0.1236  0.0720  0.0041  26  GLU A CB  
196  C CG  . GLU A 26  ? 0.9823 0.8685 1.1403 0.1124  0.0935  -0.0237 26  GLU A CG  
197  C CD  . GLU A 26  ? 1.0828 0.9215 1.2139 0.0903  0.1104  -0.0224 26  GLU A CD  
198  O OE1 . GLU A 26  ? 1.0772 0.8522 1.1769 0.0902  0.1053  -0.0020 26  GLU A OE1 
199  O OE2 . GLU A 26  ? 1.0765 0.9423 1.2172 0.0718  0.1287  -0.0418 26  GLU A OE2 
200  N N   . GLU A 27  ? 1.0512 0.8771 1.0998 0.1256  0.0379  0.0621  27  GLU A N   
201  C CA  . GLU A 27  ? 1.0199 0.8480 1.0489 0.1368  0.0142  0.0809  27  GLU A CA  
202  C C   . GLU A 27  ? 0.9842 0.8385 0.9853 0.1167  0.0204  0.0866  27  GLU A C   
203  O O   . GLU A 27  ? 0.9748 0.8653 0.9816 0.1214  0.0060  0.0880  27  GLU A O   
204  C CB  . GLU A 27  ? 1.0542 0.8117 1.0445 0.1488  -0.0014 0.1053  27  GLU A CB  
205  C CG  . GLU A 27  ? 1.1432 0.9050 1.1339 0.1739  -0.0343 0.1180  27  GLU A CG  
206  C CD  . GLU A 27  ? 1.1846 0.9871 1.1593 0.1647  -0.0424 0.1232  27  GLU A CD  
207  O OE1 . GLU A 27  ? 1.2101 0.9826 1.1306 0.1539  -0.0440 0.1422  27  GLU A OE1 
208  O OE2 . GLU A 27  ? 1.0465 0.9106 1.0622 0.1670  -0.0455 0.1071  27  GLU A OE2 
209  N N   . ALA A 28  ? 0.6878 0.5246 0.6604 0.0940  0.0417  0.0884  28  ALA A N   
210  C CA  . ALA A 28  ? 0.6576 0.5195 0.6062 0.0767  0.0492  0.0908  28  ALA A CA  
211  C C   . ALA A 28  ? 0.6154 0.5416 0.5995 0.0748  0.0509  0.0730  28  ALA A C   
212  O O   . ALA A 28  ? 0.5904 0.5410 0.5652 0.0741  0.0410  0.0771  28  ALA A O   
213  C CB  . ALA A 28  ? 0.6807 0.5221 0.6043 0.0534  0.0742  0.0906  28  ALA A CB  
214  N N   . LEU A 29  ? 0.7453 0.6969 0.7670 0.0728  0.0637  0.0531  29  LEU A N   
215  C CA  . LEU A 29  ? 0.6814 0.6914 0.7335 0.0699  0.0666  0.0374  29  LEU A CA  
216  C C   . LEU A 29  ? 0.6495 0.6857 0.7246 0.0859  0.0461  0.0388  29  LEU A C   
217  O O   . LEU A 29  ? 0.6291 0.7043 0.7117 0.0809  0.0427  0.0357  29  LEU A O   
218  C CB  . LEU A 29  ? 0.6306 0.6596 0.7142 0.0655  0.0838  0.0156  29  LEU A CB  
219  C CG  . LEU A 29  ? 0.5419 0.6284 0.6485 0.0594  0.0893  0.0010  29  LEU A CG  
220  C CD1 . LEU A 29  ? 0.5140 0.6115 0.5952 0.0425  0.0975  0.0037  29  LEU A CD1 
221  C CD2 . LEU A 29  ? 0.5328 0.6390 0.6713 0.0594  0.1026  -0.0213 29  LEU A CD2 
222  N N   . ALA A 30  ? 0.5973 0.6134 0.6863 0.1052  0.0320  0.0424  30  ALA A N   
223  C CA  . ALA A 30  ? 0.5916 0.6372 0.7074 0.1210  0.0112  0.0424  30  ALA A CA  
224  C C   . ALA A 30  ? 0.6161 0.6618 0.7023 0.1178  -0.0058 0.0582  30  ALA A C   
225  O O   . ALA A 30  ? 0.5867 0.6742 0.6913 0.1160  -0.0143 0.0539  30  ALA A O   
226  C CB  . ALA A 30  ? 0.5980 0.6166 0.7313 0.1453  -0.0031 0.0443  30  ALA A CB  
227  N N   . LEU A 31  ? 0.6371 0.6354 0.6755 0.1155  -0.0101 0.0760  31  LEU A N   
228  C CA  . LEU A 31  ? 0.6323 0.6296 0.6385 0.1124  -0.0257 0.0887  31  LEU A CA  
229  C C   . LEU A 31  ? 0.5891 0.6163 0.5881 0.0933  -0.0133 0.0818  31  LEU A C   
230  O O   . LEU A 31  ? 0.5700 0.6236 0.5726 0.0914  -0.0260 0.0811  31  LEU A O   
231  C CB  . LEU A 31  ? 0.6465 0.5867 0.5983 0.1133  -0.0309 0.1089  31  LEU A CB  
232  C CG  . LEU A 31  ? 0.6390 0.5853 0.5579 0.1078  -0.0441 0.1170  31  LEU A CG  
233  C CD1 . LEU A 31  ? 0.6773 0.6008 0.5761 0.1245  -0.0734 0.1321  31  LEU A CD1 
234  C CD2 . LEU A 31  ? 0.6318 0.5590 0.5060 0.0894  -0.0249 0.1212  31  LEU A CD2 
235  N N   . MET A 32  ? 0.6966 0.7198 0.6865 0.0793  0.0105  0.0758  32  MET A N   
236  C CA  . MET A 32  ? 0.6823 0.7336 0.6677 0.0645  0.0208  0.0685  32  MET A CA  
237  C C   . MET A 32  ? 0.6239 0.7230 0.6488 0.0642  0.0174  0.0566  32  MET A C   
238  O O   . MET A 32  ? 0.6173 0.7351 0.6359 0.0567  0.0130  0.0563  32  MET A O   
239  C CB  . MET A 32  ? 0.6370 0.6834 0.6152 0.0516  0.0454  0.0613  32  MET A CB  
240  C CG  . MET A 32  ? 0.6858 0.6936 0.6198 0.0448  0.0527  0.0725  32  MET A CG  
241  S SD  . MET A 32  ? 0.6456 0.6540 0.5773 0.0276  0.0817  0.0618  32  MET A SD  
242  C CE  . MET A 32  ? 0.6410 0.6480 0.6118 0.0321  0.0880  0.0508  32  MET A CE  
243  N N   . ASN A 33  ? 0.6307 0.7483 0.6952 0.0721  0.0195  0.0468  33  ASN A N   
244  C CA  . ASN A 33  ? 0.5586 0.7244 0.6610 0.0702  0.0193  0.0352  33  ASN A CA  
245  C C   . ASN A 33  ? 0.5653 0.7474 0.6784 0.0758  -0.0030 0.0405  33  ASN A C   
246  O O   . ASN A 33  ? 0.5073 0.7248 0.6368 0.0667  -0.0042 0.0355  33  ASN A O   
247  C CB  . ASN A 33  ? 0.5609 0.7429 0.7022 0.0783  0.0290  0.0209  33  ASN A CB  
248  C CG  . ASN A 33  ? 0.5502 0.7443 0.6941 0.0665  0.0520  0.0080  33  ASN A CG  
249  O OD1 . ASN A 33  ? 0.5229 0.7353 0.6555 0.0528  0.0589  0.0066  33  ASN A OD1 
250  N ND2 . ASN A 33  ? 0.5423 0.7248 0.7004 0.0723  0.0625  -0.0022 33  ASN A ND2 
251  N N   . ARG A 34  ? 0.6617 0.8185 0.7658 0.0900  -0.0214 0.0507  34  ARG A N   
252  C CA  . ARG A 34  ? 0.6252 0.7962 0.7346 0.0944  -0.0457 0.0559  34  ARG A CA  
253  C C   . ARG A 34  ? 0.5936 0.7611 0.6696 0.0790  -0.0490 0.0612  34  ARG A C   
254  O O   . ARG A 34  ? 0.5744 0.7697 0.6648 0.0724  -0.0601 0.0584  34  ARG A O   
255  C CB  . ARG A 34  ? 0.6499 0.7877 0.7455 0.1132  -0.0666 0.0677  34  ARG A CB  
256  C CG  . ARG A 34  ? 0.6388 0.7795 0.7717 0.1324  -0.0683 0.0616  34  ARG A CG  
257  C CD  . ARG A 34  ? 0.7418 0.8506 0.8612 0.1534  -0.0946 0.0750  34  ARG A CD  
258  N NE  . ARG A 34  ? 0.7121 0.8478 0.8408 0.1571  -0.1209 0.0771  34  ARG A NE  
259  C CZ  . ARG A 34  ? 0.8114 0.9233 0.9189 0.1723  -0.1486 0.0902  34  ARG A CZ  
260  N NH1 . ARG A 34  ? 0.7968 0.8533 0.8690 0.1854  -0.1534 0.1050  34  ARG A NH1 
261  N NH2 . ARG A 34  ? 0.7780 0.9212 0.8982 0.1732  -0.1725 0.0887  34  ARG A NH2 
262  N N   . ASN A 35  ? 0.5522 0.6854 0.5845 0.0728  -0.0392 0.0679  35  ASN A N   
263  C CA  . ASN A 35  ? 0.5208 0.6498 0.5223 0.0605  -0.0409 0.0702  35  ASN A CA  
264  C C   . ASN A 35  ? 0.5312 0.6901 0.5498 0.0467  -0.0270 0.0603  35  ASN A C   
265  O O   . ASN A 35  ? 0.4993 0.6673 0.5119 0.0376  -0.0346 0.0597  35  ASN A O   
266  C CB  . ASN A 35  ? 0.5476 0.6369 0.5007 0.0587  -0.0324 0.0779  35  ASN A CB  
267  C CG  . ASN A 35  ? 0.5906 0.6486 0.5100 0.0675  -0.0512 0.0904  35  ASN A CG  
268  O OD1 . ASN A 35  ? 0.5623 0.6231 0.4695 0.0670  -0.0700 0.0922  35  ASN A OD1 
269  N ND2 . ASN A 35  ? 0.5744 0.6003 0.4767 0.0750  -0.0473 0.0993  35  ASN A ND2 
270  N N   . LEU A 36  ? 0.5965 0.7667 0.6321 0.0445  -0.0071 0.0528  36  LEU A N   
271  C CA  . LEU A 36  ? 0.5531 0.7492 0.5995 0.0323  0.0056  0.0450  36  LEU A CA  
272  C C   . LEU A 36  ? 0.5223 0.7554 0.6029 0.0272  -0.0009 0.0405  36  LEU A C   
273  O O   . LEU A 36  ? 0.4894 0.7360 0.5676 0.0146  0.0022  0.0392  36  LEU A O   
274  C CB  . LEU A 36  ? 0.4978 0.6997 0.5541 0.0315  0.0265  0.0366  36  LEU A CB  
275  C CG  . LEU A 36  ? 0.5511 0.7230 0.5753 0.0308  0.0363  0.0393  36  LEU A CG  
276  C CD1 . LEU A 36  ? 0.5469 0.7191 0.5848 0.0316  0.0533  0.0308  36  LEU A CD1 
277  C CD2 . LEU A 36  ? 0.5277 0.7000 0.5281 0.0223  0.0399  0.0391  36  LEU A CD2 
278  N N   . ASP A 37  ? 0.5061 0.7559 0.6185 0.0364  -0.0101 0.0381  37  ASP A N   
279  C CA  . ASP A 37  ? 0.4562 0.7465 0.6039 0.0297  -0.0159 0.0329  37  ASP A CA  
280  C C   . ASP A 37  ? 0.5140 0.7992 0.6440 0.0183  -0.0315 0.0392  37  ASP A C   
281  O O   . ASP A 37  ? 0.4733 0.7780 0.6103 0.0021  -0.0276 0.0373  37  ASP A O   
282  C CB  . ASP A 37  ? 0.4358 0.7458 0.6224 0.0450  -0.0265 0.0283  37  ASP A CB  
283  C CG  . ASP A 37  ? 0.4732 0.7900 0.6831 0.0563  -0.0107 0.0186  37  ASP A CG  
284  O OD1 . ASP A 37  ? 0.4565 0.7726 0.6581 0.0490  0.0096  0.0133  37  ASP A OD1 
285  O OD2 . ASP A 37  ? 0.4843 0.8070 0.7214 0.0737  -0.0201 0.0151  37  ASP A OD2 
286  N N   . ILE A 38  ? 0.4187 0.6745 0.5225 0.0257  -0.0495 0.0469  38  ILE A N   
287  C CA  . ILE A 38  ? 0.4245 0.6707 0.5080 0.0158  -0.0659 0.0507  38  ILE A CA  
288  C C   . ILE A 38  ? 0.4463 0.6737 0.4980 0.0036  -0.0547 0.0519  38  ILE A C   
289  O O   . ILE A 38  ? 0.4368 0.6683 0.4862 -0.0109 -0.0596 0.0514  38  ILE A O   
290  C CB  . ILE A 38  ? 0.4584 0.6741 0.5128 0.0279  -0.0859 0.0577  38  ILE A CB  
291  C CG1 . ILE A 38  ? 0.4431 0.6787 0.5304 0.0416  -0.1031 0.0571  38  ILE A CG1 
292  C CG2 . ILE A 38  ? 0.4510 0.6493 0.4747 0.0179  -0.1009 0.0594  38  ILE A CG2 
293  C CD1 . ILE A 38  ? 0.5050 0.7045 0.5606 0.0588  -0.1172 0.0667  38  ILE A CD1 
294  N N   . LEU A 39  ? 0.5114 0.7159 0.5379 0.0094  -0.0407 0.0533  39  LEU A N   
295  C CA  . LEU A 39  ? 0.5477 0.7368 0.5467 0.0017  -0.0315 0.0532  39  LEU A CA  
296  C C   . LEU A 39  ? 0.5226 0.7372 0.5419 -0.0108 -0.0209 0.0499  39  LEU A C   
297  O O   . LEU A 39  ? 0.5143 0.7195 0.5177 -0.0209 -0.0233 0.0516  39  LEU A O   
298  C CB  . LEU A 39  ? 0.5863 0.7553 0.5623 0.0098  -0.0172 0.0532  39  LEU A CB  
299  C CG  . LEU A 39  ? 0.5670 0.7038 0.5088 0.0185  -0.0229 0.0581  39  LEU A CG  
300  C CD1 . LEU A 39  ? 0.5674 0.6916 0.4897 0.0204  -0.0043 0.0559  39  LEU A CD1 
301  C CD2 . LEU A 39  ? 0.5475 0.6649 0.4604 0.0161  -0.0403 0.0600  39  LEU A CD2 
302  N N   . GLU A 40  ? 0.6183 0.8635 0.6711 -0.0105 -0.0100 0.0453  40  GLU A N   
303  C CA  . GLU A 40  ? 0.5908 0.8627 0.6600 -0.0234 0.0015  0.0424  40  GLU A CA  
304  C C   . GLU A 40  ? 0.5916 0.8779 0.6740 -0.0384 -0.0092 0.0447  40  GLU A C   
305  O O   . GLU A 40  ? 0.5639 0.8514 0.6380 -0.0533 -0.0046 0.0476  40  GLU A O   
306  C CB  . GLU A 40  ? 0.5447 0.8475 0.6463 -0.0186 0.0161  0.0342  40  GLU A CB  
307  C CG  . GLU A 40  ? 0.5647 0.9074 0.6955 -0.0320 0.0240  0.0299  40  GLU A CG  
308  C CD  . GLU A 40  ? 0.5471 0.9169 0.6998 -0.0277 0.0427  0.0191  40  GLU A CD  
309  O OE1 . GLU A 40  ? 0.5632 0.9570 0.7202 -0.0402 0.0557  0.0163  40  GLU A OE1 
310  O OE2 . GLU A 40  ? 0.5409 0.9047 0.7032 -0.0122 0.0444  0.0135  40  GLU A OE2 
311  N N   . GLY A 41  ? 0.4659 0.7622 0.5682 -0.0357 -0.0244 0.0437  41  GLY A N   
312  C CA  . GLY A 41  ? 0.4611 0.7698 0.5755 -0.0523 -0.0365 0.0447  41  GLY A CA  
313  C C   . GLY A 41  ? 0.5437 0.8145 0.6186 -0.0625 -0.0441 0.0507  41  GLY A C   
314  O O   . GLY A 41  ? 0.5294 0.8025 0.6041 -0.0817 -0.0432 0.0532  41  GLY A O   
315  N N   . ALA A 42  ? 0.4900 0.7235 0.5295 -0.0497 -0.0509 0.0526  42  ALA A N   
316  C CA  . ALA A 42  ? 0.5138 0.7091 0.5147 -0.0551 -0.0573 0.0555  42  ALA A CA  
317  C C   . ALA A 42  ? 0.5212 0.7087 0.5081 -0.0607 -0.0422 0.0584  42  ALA A C   
318  O O   . ALA A 42  ? 0.5202 0.6872 0.4899 -0.0727 -0.0469 0.0619  42  ALA A O   
319  C CB  . ALA A 42  ? 0.5007 0.6634 0.4677 -0.0390 -0.0639 0.0549  42  ALA A CB  
320  N N   . ILE A 43  ? 0.5151 0.7144 0.5057 -0.0511 -0.0259 0.0570  43  ILE A N   
321  C CA  . ILE A 43  ? 0.5026 0.6961 0.4777 -0.0534 -0.0140 0.0591  43  ILE A CA  
322  C C   . ILE A 43  ? 0.5172 0.7288 0.5054 -0.0727 -0.0095 0.0636  43  ILE A C   
323  O O   . ILE A 43  ? 0.5153 0.7066 0.4809 -0.0809 -0.0099 0.0698  43  ILE A O   
324  C CB  . ILE A 43  ? 0.4592 0.6667 0.4395 -0.0406 0.0015  0.0543  43  ILE A CB  
325  C CG1 . ILE A 43  ? 0.5070 0.6916 0.4678 -0.0253 -0.0012 0.0515  43  ILE A CG1 
326  C CG2 . ILE A 43  ? 0.4377 0.6462 0.4050 -0.0429 0.0117  0.0555  43  ILE A CG2 
327  C CD1 . ILE A 43  ? 0.4413 0.6392 0.4133 -0.0155 0.0124  0.0463  43  ILE A CD1 
328  N N   . THR A 44  ? 0.4819 0.7316 0.5063 -0.0801 -0.0046 0.0606  44  THR A N   
329  C CA  . THR A 44  ? 0.4439 0.7162 0.4826 -0.1014 0.0023  0.0642  44  THR A CA  
330  C C   . THR A 44  ? 0.5162 0.7661 0.5442 -0.1194 -0.0118 0.0705  44  THR A C   
331  O O   . THR A 44  ? 0.5206 0.7574 0.5318 -0.1360 -0.0083 0.0787  44  THR A O   
332  C CB  . THR A 44  ? 0.4328 0.7556 0.5176 -0.1035 0.0105  0.0563  44  THR A CB  
333  O OG1 . THR A 44  ? 0.4822 0.8088 0.5860 -0.0925 -0.0038 0.0512  44  THR A OG1 
334  C CG2 . THR A 44  ? 0.3814 0.7252 0.4741 -0.0913 0.0285  0.0495  44  THR A CG2 
335  N N   . SER A 45  ? 0.4514 0.6918 0.4845 -0.1165 -0.0290 0.0670  45  SER A N   
336  C CA  . SER A 45  ? 0.4688 0.6844 0.4902 -0.1346 -0.0436 0.0707  45  SER A CA  
337  C C   . SER A 45  ? 0.5149 0.6784 0.4905 -0.1340 -0.0463 0.0776  45  SER A C   
338  O O   . SER A 45  ? 0.5546 0.6982 0.5177 -0.1539 -0.0483 0.0849  45  SER A O   
339  C CB  . SER A 45  ? 0.4723 0.6829 0.5000 -0.1284 -0.0638 0.0641  45  SER A CB  
340  O OG  . SER A 45  ? 0.4939 0.6811 0.5119 -0.1479 -0.0785 0.0652  45  SER A OG  
341  N N   . ALA A 46  ? 0.5241 0.6645 0.4749 -0.1112 -0.0466 0.0751  46  ALA A N   
342  C CA  . ALA A 46  ? 0.5779 0.6726 0.4890 -0.1054 -0.0501 0.0791  46  ALA A CA  
343  C C   . ALA A 46  ? 0.6409 0.7355 0.5424 -0.1136 -0.0382 0.0886  46  ALA A C   
344  O O   . ALA A 46  ? 0.6395 0.6957 0.5136 -0.1208 -0.0445 0.0962  46  ALA A O   
345  C CB  . ALA A 46  ? 0.5634 0.6460 0.4574 -0.0795 -0.0494 0.0723  46  ALA A CB  
346  N N   . ALA A 47  ? 0.6026 0.7365 0.5230 -0.1114 -0.0219 0.0882  47  ALA A N   
347  C CA  . ALA A 47  ? 0.5920 0.7293 0.5005 -0.1203 -0.0110 0.0972  47  ALA A CA  
348  C C   . ALA A 47  ? 0.5820 0.7164 0.4918 -0.1497 -0.0110 0.1073  47  ALA A C   
349  O O   . ALA A 47  ? 0.6308 0.7331 0.5104 -0.1591 -0.0127 0.1193  47  ALA A O   
350  C CB  . ALA A 47  ? 0.5113 0.6946 0.4413 -0.1141 0.0066  0.0916  47  ALA A CB  
351  N N   . ASP A 48  ? 0.7223 0.8888 0.6670 -0.1648 -0.0101 0.1028  48  ASP A N   
352  C CA  . ASP A 48  ? 0.7522 0.9206 0.7024 -0.1963 -0.0085 0.1111  48  ASP A CA  
353  C C   . ASP A 48  ? 0.8263 0.9354 0.7447 -0.2068 -0.0253 0.1187  48  ASP A C   
354  O O   . ASP A 48  ? 0.8604 0.9543 0.7684 -0.2337 -0.0231 0.1300  48  ASP A O   
355  C CB  . ASP A 48  ? 0.7292 0.9474 0.7285 -0.2088 -0.0070 0.1017  48  ASP A CB  
356  C CG  . ASP A 48  ? 0.7932 1.0262 0.8051 -0.2450 -0.0002 0.1088  48  ASP A CG  
357  O OD1 . ASP A 48  ? 0.8509 1.0556 0.8571 -0.2629 -0.0140 0.1116  48  ASP A OD1 
358  O OD2 . ASP A 48  ? 0.7873 1.0586 0.8122 -0.2573 0.0198  0.1111  48  ASP A OD2 
359  N N   . GLN A 49  ? 0.7025 0.7174 0.6051 -0.2340 -0.0563 0.1236  49  GLN A N   
360  C CA  . GLN A 49  ? 0.7285 0.6926 0.5990 -0.2398 -0.0763 0.1312  49  GLN A CA  
361  C C   . GLN A 49  ? 0.7436 0.6568 0.5708 -0.2262 -0.0885 0.1385  49  GLN A C   
362  O O   . GLN A 49  ? 0.8154 0.6837 0.6178 -0.2227 -0.1072 0.1425  49  GLN A O   
363  C CB  . GLN A 49  ? 0.7586 0.7267 0.6517 -0.2249 -0.0902 0.1245  49  GLN A CB  
364  C CG  . GLN A 49  ? 0.6828 0.6998 0.6213 -0.2369 -0.0835 0.1171  49  GLN A CG  
365  C CD  . GLN A 49  ? 0.7118 0.7334 0.6705 -0.2202 -0.0985 0.1103  49  GLN A CD  
366  O OE1 . GLN A 49  ? 0.7352 0.7211 0.6736 -0.2230 -0.1155 0.1126  49  GLN A OE1 
367  N NE2 . GLN A 49  ? 0.6569 0.7195 0.6526 -0.2032 -0.0929 0.1019  49  GLN A NE2 
368  N N   . GLY A 50  ? 0.7913 0.7097 0.6093 -0.2186 -0.0795 0.1395  50  GLY A N   
369  C CA  . GLY A 50  ? 0.8125 0.6841 0.5911 -0.2080 -0.0930 0.1466  50  GLY A CA  
370  C C   . GLY A 50  ? 0.8137 0.6743 0.5991 -0.1741 -0.1059 0.1407  50  GLY A C   
371  O O   . GLY A 50  ? 0.8535 0.6709 0.6098 -0.1643 -0.1220 0.1453  50  GLY A O   
372  N N   . ALA A 51  ? 0.7671 0.6646 0.5897 -0.1560 -0.0995 0.1303  51  ALA A N   
373  C CA  . ALA A 51  ? 0.7429 0.6329 0.5716 -0.1263 -0.1081 0.1239  51  ALA A CA  
374  C C   . ALA A 51  ? 0.7309 0.6181 0.5512 -0.1121 -0.1071 0.1242  51  ALA A C   
375  O O   . ALA A 51  ? 0.6858 0.5954 0.5095 -0.1192 -0.0943 0.1253  51  ALA A O   
376  C CB  . ALA A 51  ? 0.6740 0.6024 0.5395 -0.1139 -0.1004 0.1141  51  ALA A CB  
377  N N   . HIS A 52  ? 0.6800 0.5407 0.4908 -0.0915 -0.1208 0.1219  52  HIS A N   
378  C CA  . HIS A 52  ? 0.6550 0.5162 0.4644 -0.0752 -0.1225 0.1202  52  HIS A CA  
379  C C   . HIS A 52  ? 0.6549 0.5515 0.4967 -0.0548 -0.1126 0.1094  52  HIS A C   
380  O O   . HIS A 52  ? 0.6372 0.5489 0.4856 -0.0470 -0.1078 0.1074  52  HIS A O   
381  C CB  . HIS A 52  ? 0.6799 0.4959 0.4666 -0.0626 -0.1437 0.1219  52  HIS A CB  
382  C CG  . HIS A 52  ? 0.7313 0.5035 0.4791 -0.0818 -0.1566 0.1342  52  HIS A CG  
383  N ND1 . HIS A 52  ? 0.8093 0.5508 0.5409 -0.0934 -0.1658 0.1378  52  HIS A ND1 
384  C CD2 . HIS A 52  ? 0.7164 0.4669 0.4343 -0.0936 -0.1624 0.1443  52  HIS A CD2 
385  C CE1 . HIS A 52  ? 0.8112 0.5132 0.5047 -0.1121 -0.1762 0.1502  52  HIS A CE1 
386  N NE2 . HIS A 52  ? 0.7660 0.4720 0.4491 -0.1124 -0.1745 0.1546  52  HIS A NE2 
387  N N   . ILE A 53  ? 0.7480 0.6547 0.6068 -0.0472 -0.1105 0.1027  53  ILE A N   
388  C CA  . ILE A 53  ? 0.7182 0.6523 0.6021 -0.0297 -0.1017 0.0933  53  ILE A CA  
389  C C   . ILE A 53  ? 0.6979 0.6466 0.5954 -0.0329 -0.0971 0.0900  53  ILE A C   
390  O O   . ILE A 53  ? 0.6787 0.6078 0.5656 -0.0399 -0.1056 0.0913  53  ILE A O   
391  C CB  . ILE A 53  ? 0.7198 0.6376 0.6025 -0.0084 -0.1101 0.0863  53  ILE A CB  
392  C CG1 . ILE A 53  ? 0.6396 0.5859 0.5458 0.0060  -0.0984 0.0771  53  ILE A CG1 
393  C CG2 . ILE A 53  ? 0.7165 0.5998 0.5832 -0.0058 -0.1231 0.0846  53  ILE A CG2 
394  C CD1 . ILE A 53  ? 0.5883 0.5325 0.5010 0.0243  -0.1016 0.0698  53  ILE A CD1 
395  N N   . ILE A 54  ? 0.5840 0.5647 0.5037 -0.0280 -0.0854 0.0857  54  ILE A N   
396  C CA  . ILE A 54  ? 0.5788 0.5730 0.5115 -0.0287 -0.0835 0.0826  54  ILE A CA  
397  C C   . ILE A 54  ? 0.5492 0.5547 0.4920 -0.0122 -0.0776 0.0757  54  ILE A C   
398  O O   . ILE A 54  ? 0.5107 0.5327 0.4638 -0.0060 -0.0690 0.0740  54  ILE A O   
399  C CB  . ILE A 54  ? 0.5485 0.5707 0.4993 -0.0429 -0.0762 0.0850  54  ILE A CB  
400  C CG1 . ILE A 54  ? 0.5711 0.6060 0.5373 -0.0409 -0.0785 0.0814  54  ILE A CG1 
401  C CG2 . ILE A 54  ? 0.5095 0.5562 0.4734 -0.0406 -0.0636 0.0838  54  ILE A CG2 
402  C CD1 . ILE A 54  ? 0.5229 0.5888 0.5146 -0.0522 -0.0735 0.0814  54  ILE A CD1 
403  N N   . VAL A 55  ? 0.5482 0.5430 0.4854 -0.0067 -0.0820 0.0717  55  VAL A N   
404  C CA  . VAL A 55  ? 0.5165 0.5187 0.4578 0.0054  -0.0756 0.0660  55  VAL A CA  
405  C C   . VAL A 55  ? 0.4799 0.4955 0.4305 0.0012  -0.0760 0.0671  55  VAL A C   
406  O O   . VAL A 55  ? 0.5049 0.5168 0.4547 -0.0081 -0.0847 0.0695  55  VAL A O   
407  C CB  . VAL A 55  ? 0.4935 0.4727 0.4178 0.0155  -0.0785 0.0591  55  VAL A CB  
408  C CG1 . VAL A 55  ? 0.5082 0.4970 0.4349 0.0243  -0.0684 0.0536  55  VAL A CG1 
409  C CG2 . VAL A 55  ? 0.4971 0.4633 0.4170 0.0223  -0.0811 0.0567  55  VAL A CG2 
410  N N   . THR A 56  ? 0.4871 0.5180 0.4477 0.0075  -0.0680 0.0654  56  THR A N   
411  C CA  . THR A 56  ? 0.5436 0.5831 0.5115 0.0071  -0.0706 0.0662  56  THR A CA  
412  C C   . THR A 56  ? 0.4954 0.5224 0.4476 0.0151  -0.0682 0.0631  56  THR A C   
413  O O   . THR A 56  ? 0.5325 0.5532 0.4759 0.0211  -0.0601 0.0591  56  THR A O   
414  C CB  . THR A 56  ? 0.4968 0.5628 0.4894 0.0059  -0.0642 0.0674  56  THR A CB  
415  O OG1 . THR A 56  ? 0.4486 0.5199 0.4429 0.0120  -0.0532 0.0655  56  THR A OG1 
416  C CG2 . THR A 56  ? 0.4832 0.5617 0.4883 -0.0052 -0.0651 0.0698  56  THR A CG2 
417  N N   . PRO A 57  ? 0.5271 0.5499 0.4750 0.0146  -0.0754 0.0645  57  PRO A N   
418  C CA  . PRO A 57  ? 0.5752 0.5772 0.4968 0.0184  -0.0748 0.0622  57  PRO A CA  
419  C C   . PRO A 57  ? 0.5790 0.5854 0.5001 0.0234  -0.0624 0.0614  57  PRO A C   
420  O O   . PRO A 57  ? 0.5347 0.5591 0.4766 0.0248  -0.0571 0.0629  57  PRO A O   
421  C CB  . PRO A 57  ? 0.5279 0.5220 0.4434 0.0150  -0.0903 0.0656  57  PRO A CB  
422  C CG  . PRO A 57  ? 0.5749 0.5872 0.5166 0.0090  -0.0990 0.0679  57  PRO A CG  
423  C CD  . PRO A 57  ? 0.5484 0.5833 0.5134 0.0096  -0.0862 0.0677  57  PRO A CD  
424  N N   . GLU A 58  ? 0.6334 0.6215 0.5285 0.0246  -0.0570 0.0581  58  GLU A N   
425  C CA  . GLU A 58  ? 0.6367 0.6245 0.5258 0.0258  -0.0455 0.0578  58  GLU A CA  
426  C C   . GLU A 58  ? 0.6313 0.6142 0.5189 0.0246  -0.0549 0.0646  58  GLU A C   
427  O O   . GLU A 58  ? 0.6790 0.6514 0.5586 0.0231  -0.0704 0.0680  58  GLU A O   
428  C CB  . GLU A 58  ? 0.6850 0.6544 0.5441 0.0248  -0.0358 0.0519  58  GLU A CB  
429  C CG  . GLU A 58  ? 0.7163 0.6812 0.5629 0.0218  -0.0234 0.0522  58  GLU A CG  
430  C CD  . GLU A 58  ? 0.7701 0.7154 0.5819 0.0178  -0.0126 0.0459  58  GLU A CD  
431  O OE1 . GLU A 58  ? 0.7956 0.7232 0.5853 0.0173  -0.0196 0.0432  58  GLU A OE1 
432  O OE2 . GLU A 58  ? 0.7636 0.7111 0.5694 0.0140  0.0039  0.0427  58  GLU A OE2 
433  N N   . ASP A 59  ? 0.6417 0.6326 0.5398 0.0259  -0.0477 0.0662  59  ASP A N   
434  C CA  . ASP A 59  ? 0.6572 0.6404 0.5549 0.0269  -0.0574 0.0720  59  ASP A CA  
435  C C   . ASP A 59  ? 0.6205 0.6190 0.5456 0.0301  -0.0722 0.0739  59  ASP A C   
436  O O   . ASP A 59  ? 0.6048 0.5968 0.5326 0.0331  -0.0853 0.0777  59  ASP A O   
437  C CB  . ASP A 59  ? 0.6841 0.6345 0.5417 0.0231  -0.0645 0.0759  59  ASP A CB  
438  C CG  . ASP A 59  ? 0.7007 0.6364 0.5315 0.0176  -0.0476 0.0745  59  ASP A CG  
439  O OD1 . ASP A 59  ? 0.6827 0.6331 0.5296 0.0175  -0.0336 0.0719  59  ASP A OD1 
440  O OD2 . ASP A 59  ? 0.8012 0.7102 0.5932 0.0119  -0.0483 0.0755  59  ASP A OD2 
441  N N   . ALA A 60  ? 0.6254 0.6441 0.5716 0.0292  -0.0704 0.0710  60  ALA A N   
442  C CA  . ALA A 60  ? 0.5918 0.6272 0.5636 0.0289  -0.0822 0.0715  60  ALA A CA  
443  C C   . ALA A 60  ? 0.5513 0.6060 0.5529 0.0339  -0.0820 0.0707  60  ALA A C   
444  O O   . ALA A 60  ? 0.5127 0.5820 0.5382 0.0351  -0.0928 0.0700  60  ALA A O   
445  C CB  . ALA A 60  ? 0.5825 0.6313 0.5646 0.0238  -0.0781 0.0692  60  ALA A CB  
446  N N   . ILE A 61  ? 0.5613 0.6170 0.5637 0.0368  -0.0701 0.0695  61  ILE A N   
447  C CA  . ILE A 61  ? 0.6154 0.6896 0.6459 0.0416  -0.0671 0.0665  61  ILE A CA  
448  C C   . ILE A 61  ? 0.6207 0.6782 0.6464 0.0484  -0.0749 0.0685  61  ILE A C   
449  O O   . ILE A 61  ? 0.6097 0.6798 0.6618 0.0551  -0.0801 0.0652  61  ILE A O   
450  C CB  . ILE A 61  ? 0.5773 0.6647 0.6140 0.0396  -0.0500 0.0628  61  ILE A CB  
451  C CG1 . ILE A 61  ? 0.5345 0.6360 0.5769 0.0333  -0.0465 0.0617  61  ILE A CG1 
452  C CG2 . ILE A 61  ? 0.5422 0.6446 0.6025 0.0444  -0.0455 0.0581  61  ILE A CG2 
453  C CD1 . ILE A 61  ? 0.5684 0.6705 0.6022 0.0307  -0.0348 0.0603  61  ILE A CD1 
454  N N   . TYR A 62  ? 0.6367 0.6645 0.6285 0.0464  -0.0761 0.0733  62  TYR A N   
455  C CA  . TYR A 62  ? 0.6197 0.6243 0.6004 0.0511  -0.0852 0.0770  62  TYR A CA  
456  C C   . TYR A 62  ? 0.6842 0.6543 0.6266 0.0480  -0.0981 0.0842  62  TYR A C   
457  O O   . TYR A 62  ? 0.7276 0.6718 0.6545 0.0510  -0.1087 0.0890  62  TYR A O   
458  C CB  . TYR A 62  ? 0.6313 0.6302 0.6064 0.0495  -0.0704 0.0757  62  TYR A CB  
459  C CG  . TYR A 62  ? 0.6533 0.6494 0.6080 0.0404  -0.0535 0.0753  62  TYR A CG  
460  C CD1 . TYR A 62  ? 0.6968 0.6770 0.6221 0.0344  -0.0533 0.0780  62  TYR A CD1 
461  C CD2 . TYR A 62  ? 0.6145 0.6233 0.5796 0.0382  -0.0383 0.0708  62  TYR A CD2 
462  C CE1 . TYR A 62  ? 0.6727 0.6537 0.5845 0.0277  -0.0369 0.0751  62  TYR A CE1 
463  C CE2 . TYR A 62  ? 0.6386 0.6483 0.5910 0.0310  -0.0241 0.0690  62  TYR A CE2 
464  C CZ  . TYR A 62  ? 0.6356 0.6330 0.5634 0.0264  -0.0229 0.0706  62  TYR A CZ  
465  O OH  . TYR A 62  ? 0.6412 0.6434 0.5619 0.0207  -0.0080 0.0663  62  TYR A OH  
466  N N   . GLY A 63  ? 0.6933 0.6587 0.6167 0.0420  -0.0987 0.0850  63  GLY A N   
467  C CA  . GLY A 63  ? 0.7077 0.6391 0.5914 0.0383  -0.1121 0.0910  63  GLY A CA  
468  C C   . GLY A 63  ? 0.7277 0.6327 0.5683 0.0293  -0.0978 0.0931  63  GLY A C   
469  O O   . GLY A 63  ? 0.7051 0.6215 0.5497 0.0257  -0.0770 0.0890  63  GLY A O   
470  N N   . TRP A 64  ? 0.7875 0.6567 0.5857 0.0247  -0.1094 0.0992  64  TRP A N   
471  C CA  . TRP A 64  ? 0.8051 0.6494 0.5583 0.0134  -0.0938 0.1000  64  TRP A CA  
472  C C   . TRP A 64  ? 0.8802 0.6824 0.5914 0.0077  -0.1015 0.1092  64  TRP A C   
473  O O   . TRP A 64  ? 0.8900 0.6687 0.5584 -0.0045 -0.0879 0.1103  64  TRP A O   
474  C CB  . TRP A 64  ? 0.8071 0.6437 0.5349 0.0084  -0.0937 0.0965  64  TRP A CB  
475  C CG  . TRP A 64  ? 0.8575 0.6770 0.5738 0.0111  -0.1214 0.1014  64  TRP A CG  
476  C CD1 . TRP A 64  ? 0.8589 0.6381 0.5317 0.0071  -0.1388 0.1095  64  TRP A CD1 
477  C CD2 . TRP A 64  ? 0.8396 0.6812 0.5884 0.0172  -0.1367 0.0987  64  TRP A CD2 
478  N NE1 . TRP A 64  ? 0.8900 0.6661 0.5685 0.0118  -0.1659 0.1116  64  TRP A NE1 
479  C CE2 . TRP A 64  ? 0.8300 0.6459 0.5567 0.0173  -0.1640 0.1045  64  TRP A CE2 
480  C CE3 . TRP A 64  ? 0.7956 0.6745 0.5878 0.0210  -0.1305 0.0921  64  TRP A CE3 
481  C CZ2 . TRP A 64  ? 0.8104 0.6411 0.5622 0.0210  -0.1847 0.1030  64  TRP A CZ2 
482  C CZ3 . TRP A 64  ? 0.7729 0.6642 0.5867 0.0231  -0.1494 0.0914  64  TRP A CZ3 
483  C CH2 . TRP A 64  ? 0.8012 0.6706 0.5973 0.0231  -0.1759 0.0963  64  TRP A CH2 
484  N N   . ASN A 65  ? 0.9401 0.7313 0.6620 0.0157  -0.1223 0.1153  65  ASN A N   
485  C CA  . ASN A 65  ? 0.9811 0.7252 0.6600 0.0111  -0.1346 0.1256  65  ASN A CA  
486  C C   . ASN A 65  ? 0.9680 0.7103 0.6565 0.0099  -0.1223 0.1265  65  ASN A C   
487  O O   . ASN A 65  ? 1.0008 0.7439 0.7158 0.0211  -0.1362 0.1278  65  ASN A O   
488  C CB  . ASN A 65  ? 1.0287 0.7577 0.7129 0.0224  -0.1696 0.1313  65  ASN A CB  
489  C CG  . ASN A 65  ? 1.0575 0.7673 0.7076 0.0179  -0.1853 0.1340  65  ASN A CG  
490  O OD1 . ASN A 65  ? 1.0315 0.7556 0.7077 0.0272  -0.2073 0.1324  65  ASN A OD1 
491  N ND2 . ASN A 65  ? 1.1561 0.8330 0.7467 0.0024  -0.1738 0.1372  65  ASN A ND2 
492  N N   . PHE A 66  ? 0.9060 0.6429 0.5709 -0.0045 -0.0968 0.1252  66  PHE A N   
493  C CA  . PHE A 66  ? 0.9275 0.6672 0.6048 -0.0078 -0.0828 0.1245  66  PHE A CA  
494  C C   . PHE A 66  ? 0.9343 0.6411 0.5609 -0.0281 -0.0662 0.1293  66  PHE A C   
495  O O   . PHE A 66  ? 0.9764 0.6791 0.5727 -0.0399 -0.0520 0.1273  66  PHE A O   
496  C CB  . PHE A 66  ? 0.8992 0.6905 0.6266 -0.0039 -0.0622 0.1128  66  PHE A CB  
497  C CG  . PHE A 66  ? 0.8333 0.6566 0.6123 0.0130  -0.0736 0.1078  66  PHE A CG  
498  C CD1 . PHE A 66  ? 0.8134 0.6312 0.6121 0.0223  -0.0854 0.1091  66  PHE A CD1 
499  C CD2 . PHE A 66  ? 0.8285 0.6869 0.6358 0.0187  -0.0712 0.1010  66  PHE A CD2 
500  C CE1 . PHE A 66  ? 0.7846 0.6351 0.6318 0.0368  -0.0925 0.1024  66  PHE A CE1 
501  C CE2 . PHE A 66  ? 0.7850 0.6739 0.6380 0.0311  -0.0788 0.0962  66  PHE A CE2 
502  C CZ  . PHE A 66  ? 0.7579 0.6448 0.6315 0.0400  -0.0883 0.0963  66  PHE A CZ  
503  N N   . ASN A 67  ? 0.9927 0.6747 0.6092 -0.0329 -0.0674 0.1350  67  ASN A N   
504  C CA  . ASN A 67  ? 0.9991 0.6699 0.5907 -0.0532 -0.0429 0.1353  67  ASN A CA  
505  C C   . ASN A 67  ? 0.9622 0.6733 0.6050 -0.0496 -0.0273 0.1258  67  ASN A C   
506  O O   . ASN A 67  ? 0.9199 0.6616 0.6099 -0.0321 -0.0357 0.1200  67  ASN A O   
507  C CB  . ASN A 67  ? 1.0142 0.6236 0.5518 -0.0653 -0.0544 0.1491  67  ASN A CB  
508  C CG  . ASN A 67  ? 1.0541 0.6483 0.6130 -0.0509 -0.0769 0.1532  67  ASN A CG  
509  O OD1 . ASN A 67  ? 1.0493 0.6679 0.6470 -0.0469 -0.0677 0.1464  67  ASN A OD1 
510  N ND2 . ASN A 67  ? 1.0756 0.6290 0.6099 -0.0421 -0.1078 0.1633  67  ASN A ND2 
511  N N   . ARG A 68  ? 0.9398 0.6506 0.5720 -0.0676 -0.0044 0.1237  68  ARG A N   
512  C CA  . ARG A 68  ? 0.9400 0.6909 0.6188 -0.0663 0.0110  0.1135  68  ARG A CA  
513  C C   . ARG A 68  ? 0.9455 0.6933 0.6520 -0.0523 -0.0058 0.1143  68  ARG A C   
514  O O   . ARG A 68  ? 0.9499 0.7367 0.7035 -0.0390 -0.0051 0.1054  68  ARG A O   
515  C CB  . ARG A 68  ? 0.9319 0.6781 0.5923 -0.0903 0.0356  0.1120  68  ARG A CB  
516  C CG  . ARG A 68  ? 0.9629 0.7330 0.6170 -0.1009 0.0588  0.1041  68  ARG A CG  
517  C CD  . ARG A 68  ? 0.9431 0.7170 0.5880 -0.1251 0.0852  0.1001  68  ARG A CD  
518  N NE  . ARG A 68  ? 0.9489 0.7615 0.6447 -0.1226 0.0931  0.0907  68  ARG A NE  
519  C CZ  . ARG A 68  ? 0.9084 0.7726 0.6488 -0.1157 0.1052  0.0773  68  ARG A CZ  
520  N NH1 . ARG A 68  ? 0.8766 0.7610 0.6204 -0.1089 0.1111  0.0708  68  ARG A NH1 
521  N NH2 . ARG A 68  ? 0.8374 0.7307 0.6177 -0.1158 0.1102  0.0699  68  ARG A NH2 
522  N N   . ASP A 69  ? 0.9306 0.6296 0.6064 -0.0548 -0.0215 0.1246  69  ASP A N   
523  C CA  . ASP A 69  ? 0.9620 0.6550 0.6631 -0.0420 -0.0353 0.1232  69  ASP A CA  
524  C C   . ASP A 69  ? 0.9517 0.6625 0.6864 -0.0168 -0.0560 0.1200  69  ASP A C   
525  O O   . ASP A 69  ? 0.8831 0.6239 0.6616 -0.0039 -0.0559 0.1108  69  ASP A O   
526  C CB  . ASP A 69  ? 0.9687 0.6001 0.6260 -0.0515 -0.0475 0.1348  69  ASP A CB  
527  C CG  . ASP A 69  ? 1.0253 0.6451 0.6606 -0.0776 -0.0250 0.1356  69  ASP A CG  
528  O OD1 . ASP A 69  ? 0.9774 0.6403 0.6481 -0.0815 -0.0054 0.1246  69  ASP A OD1 
529  O OD2 . ASP A 69  ? 1.1371 0.7043 0.7197 -0.0950 -0.0279 0.1473  69  ASP A OD2 
530  N N   . SER A 70  ? 0.9994 0.6946 0.7150 -0.0108 -0.0727 0.1265  70  SER A N   
531  C CA  . SER A 70  ? 0.9752 0.6926 0.7279 0.0113  -0.0914 0.1222  70  SER A CA  
532  C C   . SER A 70  ? 0.8811 0.6567 0.6775 0.0167  -0.0765 0.1109  70  SER A C   
533  O O   . SER A 70  ? 0.8750 0.6775 0.7114 0.0327  -0.0854 0.1045  70  SER A O   
534  C CB  . SER A 70  ? 0.9386 0.6267 0.6621 0.0156  -0.1152 0.1315  70  SER A CB  
535  O OG  . SER A 70  ? 1.0011 0.6955 0.7004 0.0044  -0.1050 0.1329  70  SER A OG  
536  N N   . LEU A 71  ? 0.7394 0.5341 0.5290 0.0035  -0.0544 0.1078  71  LEU A N   
537  C CA  . LEU A 71  ? 0.6971 0.5417 0.5254 0.0083  -0.0417 0.0977  71  LEU A CA  
538  C C   . LEU A 71  ? 0.7107 0.5793 0.5708 0.0094  -0.0300 0.0895  71  LEU A C   
539  O O   . LEU A 71  ? 0.6202 0.5246 0.5158 0.0181  -0.0273 0.0819  71  LEU A O   
540  C CB  . LEU A 71  ? 0.6889 0.5448 0.5012 -0.0033 -0.0248 0.0958  71  LEU A CB  
541  C CG  . LEU A 71  ? 0.6529 0.5553 0.5024 0.0008  -0.0120 0.0856  71  LEU A CG  
542  C CD1 . LEU A 71  ? 0.6124 0.5337 0.4831 0.0135  -0.0246 0.0840  71  LEU A CD1 
543  C CD2 . LEU A 71  ? 0.6277 0.5417 0.4667 -0.0104 0.0077  0.0810  71  LEU A CD2 
544  N N   . TYR A 72  ? 0.8310 0.6784 0.6761 -0.0010 -0.0232 0.0912  72  TYR A N   
545  C CA  . TYR A 72  ? 0.8202 0.6904 0.6923 -0.0026 -0.0113 0.0826  72  TYR A CA  
546  C C   . TYR A 72  ? 0.7753 0.6686 0.6849 0.0140  -0.0190 0.0751  72  TYR A C   
547  O O   . TYR A 72  ? 0.7553 0.6836 0.6908 0.0152  -0.0089 0.0671  72  TYR A O   
548  C CB  . TYR A 72  ? 0.8414 0.6774 0.6906 -0.0152 -0.0085 0.0862  72  TYR A CB  
549  C CG  . TYR A 72  ? 0.7918 0.6491 0.6645 -0.0202 0.0040  0.0773  72  TYR A CG  
550  C CD1 . TYR A 72  ? 0.7878 0.6699 0.6662 -0.0338 0.0224  0.0726  72  TYR A CD1 
551  C CD2 . TYR A 72  ? 0.8404 0.6943 0.7313 -0.0106 -0.0035 0.0720  72  TYR A CD2 
552  C CE1 . TYR A 72  ? 0.8002 0.7023 0.7010 -0.0386 0.0309  0.0642  72  TYR A CE1 
553  C CE2 . TYR A 72  ? 0.7818 0.6534 0.6911 -0.0159 0.0064  0.0632  72  TYR A CE2 
554  C CZ  . TYR A 72  ? 0.7966 0.6918 0.7103 -0.0303 0.0226  0.0600  72  TYR A CZ  
555  O OH  . TYR A 72  ? 0.8668 0.7795 0.7990 -0.0360 0.0298  0.0514  72  TYR A OH  
556  N N   . PRO A 73  ? 0.7310 0.6078 0.6454 0.0273  -0.0364 0.0766  73  PRO A N   
557  C CA  . PRO A 73  ? 0.6615 0.5646 0.6139 0.0419  -0.0396 0.0668  73  PRO A CA  
558  C C   . PRO A 73  ? 0.6773 0.6222 0.6547 0.0461  -0.0345 0.0620  73  PRO A C   
559  O O   . PRO A 73  ? 0.6412 0.6123 0.6474 0.0534  -0.0313 0.0531  73  PRO A O   
560  C CB  . PRO A 73  ? 0.6839 0.5617 0.6373 0.0561  -0.0610 0.0693  73  PRO A CB  
561  C CG  . PRO A 73  ? 0.7164 0.5560 0.6294 0.0491  -0.0718 0.0824  73  PRO A CG  
562  C CD  . PRO A 73  ? 0.7144 0.5451 0.5994 0.0290  -0.0539 0.0861  73  PRO A CD  
563  N N   . TYR A 74  ? 0.6606 0.6100 0.6253 0.0411  -0.0337 0.0673  74  TYR A N   
564  C CA  . TYR A 74  ? 0.5990 0.5827 0.5839 0.0438  -0.0300 0.0634  74  TYR A CA  
565  C C   . TYR A 74  ? 0.5497 0.5556 0.5393 0.0355  -0.0136 0.0591  74  TYR A C   
566  O O   . TYR A 74  ? 0.5458 0.5771 0.5507 0.0373  -0.0110 0.0559  74  TYR A O   
567  C CB  . TYR A 74  ? 0.5533 0.5296 0.5230 0.0435  -0.0390 0.0699  74  TYR A CB  
568  C CG  . TYR A 74  ? 0.5878 0.5461 0.5569 0.0530  -0.0593 0.0739  74  TYR A CG  
569  C CD1 . TYR A 74  ? 0.6472 0.5650 0.5873 0.0518  -0.0699 0.0813  74  TYR A CD1 
570  C CD2 . TYR A 74  ? 0.5583 0.5392 0.5558 0.0625  -0.0691 0.0703  74  TYR A CD2 
571  C CE1 . TYR A 74  ? 0.6254 0.5248 0.5657 0.0623  -0.0924 0.0850  74  TYR A CE1 
572  C CE2 . TYR A 74  ? 0.5552 0.5233 0.5582 0.0725  -0.0900 0.0726  74  TYR A CE2 
573  C CZ  . TYR A 74  ? 0.6230 0.5497 0.5976 0.0735  -0.1029 0.0800  74  TYR A CZ  
574  O OH  . TYR A 74  ? 0.6672 0.5798 0.6482 0.0851  -0.1273 0.0823  74  TYR A OH  
575  N N   . LEU A 75  ? 0.4971 0.4935 0.4745 0.0261  -0.0039 0.0588  75  LEU A N   
576  C CA  . LEU A 75  ? 0.4836 0.5012 0.4667 0.0188  0.0089  0.0546  75  LEU A CA  
577  C C   . LEU A 75  ? 0.5622 0.6014 0.5681 0.0209  0.0130  0.0468  75  LEU A C   
578  O O   . LEU A 75  ? 0.5018 0.5351 0.5145 0.0248  0.0101  0.0436  75  LEU A O   
579  C CB  . LEU A 75  ? 0.5132 0.5162 0.4768 0.0059  0.0186  0.0563  75  LEU A CB  
580  C CG  . LEU A 75  ? 0.5616 0.5403 0.4942 -0.0001 0.0181  0.0636  75  LEU A CG  
581  C CD1 . LEU A 75  ? 0.5488 0.5118 0.4610 -0.0158 0.0301  0.0647  75  LEU A CD1 
582  C CD2 . LEU A 75  ? 0.5055 0.4981 0.4366 0.0022  0.0197  0.0628  75  LEU A CD2 
583  N N   . GLU A 76  ? 0.5940 0.6563 0.6099 0.0191  0.0184  0.0433  76  GLU A N   
584  C CA  . GLU A 76  ? 0.5972 0.6765 0.6275 0.0182  0.0220  0.0366  76  GLU A CA  
585  C C   . GLU A 76  ? 0.6140 0.7039 0.6461 0.0106  0.0289  0.0339  76  GLU A C   
586  O O   . GLU A 76  ? 0.5988 0.6895 0.6253 0.0085  0.0318  0.0359  76  GLU A O   
587  C CB  . GLU A 76  ? 0.5875 0.6847 0.6293 0.0241  0.0186  0.0347  76  GLU A CB  
588  C CG  . GLU A 76  ? 0.5942 0.6885 0.6425 0.0314  0.0139  0.0338  76  GLU A CG  
589  C CD  . GLU A 76  ? 0.5600 0.6737 0.6188 0.0336  0.0135  0.0318  76  GLU A CD  
590  O OE1 . GLU A 76  ? 0.5395 0.6635 0.5961 0.0297  0.0150  0.0324  76  GLU A OE1 
591  O OE2 . GLU A 76  ? 0.5765 0.6946 0.6461 0.0390  0.0113  0.0294  76  GLU A OE2 
592  N N   . ASP A 77  ? 0.5853 0.6826 0.6257 0.0061  0.0314  0.0282  77  ASP A N   
593  C CA  . ASP A 77  ? 0.5746 0.6872 0.6240 -0.0004 0.0359  0.0238  77  ASP A CA  
594  C C   . ASP A 77  ? 0.5773 0.7090 0.6368 0.0055  0.0307  0.0218  77  ASP A C   
595  O O   . ASP A 77  ? 0.5649 0.7027 0.6281 0.0064  0.0264  0.0188  77  ASP A O   
596  C CB  . ASP A 77  ? 0.5489 0.6594 0.6023 -0.0086 0.0381  0.0186  77  ASP A CB  
597  C CG  . ASP A 77  ? 0.5478 0.6737 0.6132 -0.0179 0.0436  0.0136  77  ASP A CG  
598  O OD1 . ASP A 77  ? 0.5127 0.6587 0.5906 -0.0144 0.0427  0.0112  77  ASP A OD1 
599  O OD2 . ASP A 77  ? 0.5435 0.6619 0.6078 -0.0288 0.0483  0.0114  77  ASP A OD2 
600  N N   . ILE A 78  ? 0.5568 0.6947 0.6174 0.0088  0.0306  0.0233  78  ILE A N   
601  C CA  . ILE A 78  ? 0.5091 0.6575 0.5745 0.0150  0.0235  0.0231  78  ILE A CA  
602  C C   . ILE A 78  ? 0.5218 0.6871 0.6030 0.0139  0.0216  0.0166  78  ILE A C   
603  O O   . ILE A 78  ? 0.4936 0.6669 0.5839 0.0124  0.0275  0.0125  78  ILE A O   
604  C CB  . ILE A 78  ? 0.5194 0.6626 0.5777 0.0200  0.0225  0.0269  78  ILE A CB  
605  C CG1 . ILE A 78  ? 0.5250 0.6525 0.5701 0.0207  0.0222  0.0329  78  ILE A CG1 
606  C CG2 . ILE A 78  ? 0.5239 0.6721 0.5840 0.0255  0.0135  0.0276  78  ILE A CG2 
607  C CD1 . ILE A 78  ? 0.5190 0.6387 0.5542 0.0241  0.0202  0.0363  78  ILE A CD1 
608  N N   . PRO A 79  ? 0.3696 0.5410 0.4542 0.0145  0.0133  0.0146  79  PRO A N   
609  C CA  . PRO A 79  ? 0.3727 0.5602 0.4744 0.0143  0.0077  0.0081  79  PRO A CA  
610  C C   . PRO A 79  ? 0.3545 0.5488 0.4648 0.0229  0.0022  0.0069  79  PRO A C   
611  O O   . PRO A 79  ? 0.3777 0.5615 0.4765 0.0280  0.0009  0.0119  79  PRO A O   
612  C CB  . PRO A 79  ? 0.3630 0.5483 0.4573 0.0128  -0.0024 0.0081  79  PRO A CB  
613  C CG  . PRO A 79  ? 0.3738 0.5451 0.4485 0.0144  -0.0019 0.0147  79  PRO A CG  
614  C CD  . PRO A 79  ? 0.3856 0.5494 0.4578 0.0145  0.0088  0.0176  79  PRO A CD  
615  N N   . ASP A 80  ? 0.5076 0.7199 0.6404 0.0247  -0.0019 -0.0010 80  ASP A N   
616  C CA  . ASP A 80  ? 0.5134 0.7316 0.6574 0.0356  -0.0112 -0.0040 80  ASP A CA  
617  C C   . ASP A 80  ? 0.5465 0.7509 0.6747 0.0401  -0.0285 0.0021  80  ASP A C   
618  O O   . ASP A 80  ? 0.5360 0.7384 0.6574 0.0352  -0.0361 0.0034  80  ASP A O   
619  C CB  . ASP A 80  ? 0.4878 0.7320 0.6652 0.0375  -0.0134 -0.0156 80  ASP A CB  
620  C CG  . ASP A 80  ? 0.5402 0.7914 0.7339 0.0514  -0.0220 -0.0213 80  ASP A CG  
621  O OD1 . ASP A 80  ? 0.5905 0.8273 0.7728 0.0595  -0.0391 -0.0164 80  ASP A OD1 
622  O OD2 . ASP A 80  ? 0.5865 0.8561 0.8030 0.0539  -0.0112 -0.0312 80  ASP A OD2 
623  N N   . PRO A 81  ? 0.6204 0.8125 0.7393 0.0481  -0.0350 0.0059  81  PRO A N   
624  C CA  . PRO A 81  ? 0.6139 0.7881 0.7121 0.0492  -0.0508 0.0134  81  PRO A CA  
625  C C   . PRO A 81  ? 0.6591 0.8371 0.7642 0.0518  -0.0688 0.0105  81  PRO A C   
626  O O   . PRO A 81  ? 0.6072 0.7680 0.6883 0.0484  -0.0808 0.0175  81  PRO A O   
627  C CB  . PRO A 81  ? 0.6116 0.7722 0.7033 0.0575  -0.0550 0.0159  81  PRO A CB  
628  C CG  . PRO A 81  ? 0.6183 0.7849 0.7158 0.0569  -0.0372 0.0129  81  PRO A CG  
629  C CD  . PRO A 81  ? 0.5782 0.7673 0.6982 0.0536  -0.0269 0.0045  81  PRO A CD  
630  N N   . GLU A 82  ? 0.7522 0.9525 0.8888 0.0566  -0.0712 0.0002  82  GLU A N   
631  C CA  . GLU A 82  ? 0.7500 0.9555 0.8961 0.0594  -0.0913 -0.0033 82  GLU A CA  
632  C C   . GLU A 82  ? 0.7042 0.9042 0.8313 0.0470  -0.0933 0.0002  82  GLU A C   
633  O O   . GLU A 82  ? 0.7635 0.9610 0.8882 0.0474  -0.1125 -0.0006 82  GLU A O   
634  C CB  . GLU A 82  ? 0.7390 0.9761 0.9298 0.0658  -0.0916 -0.0171 82  GLU A CB  
635  C CG  . GLU A 82  ? 0.7557 1.0143 0.9628 0.0537  -0.0758 -0.0232 82  GLU A CG  
636  C CD  . GLU A 82  ? 0.8258 1.1185 1.0786 0.0575  -0.0694 -0.0376 82  GLU A CD  
637  O OE1 . GLU A 82  ? 0.8452 1.1528 1.1089 0.0464  -0.0498 -0.0420 82  GLU A OE1 
638  O OE2 . GLU A 82  ? 0.8211 1.1253 1.0991 0.0714  -0.0841 -0.0449 82  GLU A OE2 
639  N N   . VAL A 83  ? 0.4415 0.6387 0.5552 0.0367  -0.0753 0.0029  83  VAL A N   
640  C CA  . VAL A 83  ? 0.4306 0.6198 0.5236 0.0260  -0.0760 0.0047  83  VAL A CA  
641  C C   . VAL A 83  ? 0.4978 0.6623 0.5540 0.0233  -0.0856 0.0137  83  VAL A C   
642  O O   . VAL A 83  ? 0.5010 0.6570 0.5359 0.0145  -0.0879 0.0142  83  VAL A O   
643  C CB  . VAL A 83  ? 0.4313 0.6213 0.5200 0.0174  -0.0553 0.0040  83  VAL A CB  
644  C CG1 . VAL A 83  ? 0.3873 0.5964 0.5053 0.0166  -0.0434 -0.0031 83  VAL A CG1 
645  C CG2 . VAL A 83  ? 0.3793 0.5545 0.4469 0.0171  -0.0450 0.0119  83  VAL A CG2 
646  N N   . ASN A 84  ? 0.5507 0.7020 0.5966 0.0290  -0.0899 0.0205  84  ASN A N   
647  C CA  . ASN A 84  ? 0.5965 0.7222 0.6060 0.0243  -0.1005 0.0297  84  ASN A CA  
648  C C   . ASN A 84  ? 0.6097 0.7287 0.5938 0.0115  -0.0851 0.0327  84  ASN A C   
649  O O   . ASN A 84  ? 0.6666 0.7775 0.6281 0.0028  -0.0888 0.0326  84  ASN A O   
650  C CB  . ASN A 84  ? 0.6029 0.7198 0.6041 0.0259  -0.1253 0.0296  84  ASN A CB  
651  C CG  . ASN A 84  ? 0.6525 0.7367 0.6100 0.0200  -0.1392 0.0406  84  ASN A CG  
652  O OD1 . ASN A 84  ? 0.7176 0.7882 0.6538 0.0139  -0.1293 0.0480  84  ASN A OD1 
653  N ND2 . ASN A 84  ? 0.6289 0.6998 0.5725 0.0206  -0.1634 0.0419  84  ASN A ND2 
654  N N   . TRP A 85  ? 0.5579 0.6819 0.5480 0.0112  -0.0677 0.0339  85  TRP A N   
655  C CA  . TRP A 85  ? 0.5286 0.6536 0.5076 0.0026  -0.0509 0.0334  85  TRP A CA  
656  C C   . TRP A 85  ? 0.5515 0.6689 0.5189 -0.0004 -0.0439 0.0403  85  TRP A C   
657  O O   . TRP A 85  ? 0.5487 0.6672 0.5284 0.0059  -0.0434 0.0428  85  TRP A O   
658  C CB  . TRP A 85  ? 0.4993 0.6402 0.5027 0.0052  -0.0375 0.0264  85  TRP A CB  
659  C CG  . TRP A 85  ? 0.5201 0.6622 0.5182 0.0001  -0.0219 0.0243  85  TRP A CG  
660  C CD1 . TRP A 85  ? 0.5453 0.6819 0.5228 -0.0080 -0.0173 0.0225  85  TRP A CD1 
661  C CD2 . TRP A 85  ? 0.5047 0.6531 0.5187 0.0035  -0.0095 0.0225  85  TRP A CD2 
662  N NE1 . TRP A 85  ? 0.5679 0.7101 0.5528 -0.0080 -0.0024 0.0183  85  TRP A NE1 
663  C CE2 . TRP A 85  ? 0.4911 0.6389 0.4977 -0.0007 0.0007  0.0191  85  TRP A CE2 
664  C CE3 . TRP A 85  ? 0.4996 0.6524 0.5314 0.0095  -0.0065 0.0232  85  TRP A CE3 
665  C CZ2 . TRP A 85  ? 0.5289 0.6797 0.5479 0.0029  0.0107  0.0167  85  TRP A CZ2 
666  C CZ3 . TRP A 85  ? 0.4656 0.6183 0.5038 0.0108  0.0036  0.0224  85  TRP A CZ3 
667  C CH2 . TRP A 85  ? 0.4672 0.6186 0.5005 0.0085  0.0106  0.0194  85  TRP A CH2 
668  N N   . ILE A 86  ? 0.5423 0.6529 0.4861 -0.0112 -0.0376 0.0422  86  ILE A N   
669  C CA  . ILE A 86  ? 0.5524 0.6622 0.4896 -0.0171 -0.0271 0.0464  86  ILE A CA  
670  C C   . ILE A 86  ? 0.5761 0.7012 0.5249 -0.0189 -0.0093 0.0388  86  ILE A C   
671  O O   . ILE A 86  ? 0.5858 0.7107 0.5188 -0.0272 -0.0023 0.0344  86  ILE A O   
672  C CB  . ILE A 86  ? 0.5489 0.6409 0.4509 -0.0302 -0.0314 0.0532  86  ILE A CB  
673  C CG1 . ILE A 86  ? 0.5719 0.6422 0.4592 -0.0275 -0.0525 0.0615  86  ILE A CG1 
674  C CG2 . ILE A 86  ? 0.5367 0.6335 0.4365 -0.0392 -0.0175 0.0556  86  ILE A CG2 
675  C CD1 . ILE A 86  ? 0.5625 0.6073 0.4055 -0.0420 -0.0609 0.0689  86  ILE A CD1 
676  N N   . PRO A 87  ? 0.5547 0.6910 0.5284 -0.0113 -0.0023 0.0365  87  PRO A N   
677  C CA  . PRO A 87  ? 0.5230 0.6708 0.5091 -0.0106 0.0114  0.0288  87  PRO A CA  
678  C C   . PRO A 87  ? 0.5297 0.6830 0.5065 -0.0196 0.0226  0.0263  87  PRO A C   
679  O O   . PRO A 87  ? 0.5350 0.6950 0.5143 -0.0204 0.0330  0.0171  87  PRO A O   
680  C CB  . PRO A 87  ? 0.5012 0.6542 0.5099 -0.0016 0.0127  0.0302  87  PRO A CB  
681  C CG  . PRO A 87  ? 0.4655 0.6121 0.4759 0.0033  0.0021  0.0346  87  PRO A CG  
682  C CD  . PRO A 87  ? 0.5280 0.6646 0.5184 -0.0020 -0.0079 0.0396  87  PRO A CD  
683  N N   . CYS A 88  ? 0.5969 0.7472 0.5627 -0.0274 0.0217  0.0330  88  CYS A N   
684  C CA  . CYS A 88  ? 0.6050 0.7648 0.5651 -0.0383 0.0354  0.0295  88  CYS A CA  
685  C C   . CYS A 88  ? 0.6374 0.7929 0.5726 -0.0475 0.0420  0.0234  88  CYS A C   
686  O O   . CYS A 88  ? 0.6279 0.7969 0.5677 -0.0513 0.0579  0.0134  88  CYS A O   
687  C CB  . CYS A 88  ? 0.6103 0.7638 0.5574 -0.0491 0.0324  0.0390  88  CYS A CB  
688  S SG  . CYS A 88  ? 0.6452 0.8219 0.6039 -0.0613 0.0521  0.0330  88  CYS A SG  
689  N N   . ASN A 89  ? 0.6134 0.7499 0.5224 -0.0507 0.0292  0.0282  89  ASN A N   
690  C CA  . ASN A 89  ? 0.6304 0.7560 0.5058 -0.0618 0.0313  0.0246  89  ASN A CA  
691  C C   . ASN A 89  ? 0.6542 0.7815 0.5352 -0.0549 0.0311  0.0144  89  ASN A C   
692  O O   . ASN A 89  ? 0.6725 0.7983 0.5350 -0.0622 0.0409  0.0055  89  ASN A O   
693  C CB  . ASN A 89  ? 0.5693 0.6693 0.4103 -0.0691 0.0131  0.0361  89  ASN A CB  
694  C CG  . ASN A 89  ? 0.6523 0.7438 0.4833 -0.0772 0.0106  0.0473  89  ASN A CG  
695  O OD1 . ASN A 89  ? 0.6069 0.7126 0.4482 -0.0837 0.0259  0.0457  89  ASN A OD1 
696  N ND2 . ASN A 89  ? 0.6843 0.7520 0.4963 -0.0769 -0.0099 0.0580  89  ASN A ND2 
697  N N   . ASN A 90  ? 0.6191 0.7465 0.5208 -0.0428 0.0195  0.0156  90  ASN A N   
698  C CA  . ASN A 90  ? 0.6048 0.7346 0.5170 -0.0370 0.0196  0.0063  90  ASN A CA  
699  C C   . ASN A 90  ? 0.6254 0.7680 0.5727 -0.0256 0.0270  0.0025  90  ASN A C   
700  O O   . ASN A 90  ? 0.6120 0.7550 0.5771 -0.0180 0.0193  0.0048  90  ASN A O   
701  C CB  . ASN A 90  ? 0.5731 0.6935 0.4810 -0.0348 0.0004  0.0102  90  ASN A CB  
702  C CG  . ASN A 90  ? 0.6141 0.7329 0.5215 -0.0352 -0.0012 0.0006  90  ASN A CG  
703  O OD1 . ASN A 90  ? 0.6347 0.7552 0.5400 -0.0370 0.0120  -0.0094 90  ASN A OD1 
704  N ND2 . ASN A 90  ? 0.6223 0.7378 0.5328 -0.0333 -0.0182 0.0023  90  ASN A ND2 
705  N N   . ARG A 91  ? 0.9272 1.0798 0.8844 -0.0248 0.0419  -0.0040 91  ARG A N   
706  C CA  . ARG A 91  ? 0.9298 1.0885 0.9154 -0.0135 0.0457  -0.0087 91  ARG A CA  
707  C C   . ARG A 91  ? 0.9348 1.0852 0.9173 -0.0122 0.0453  -0.0177 91  ARG A C   
708  O O   . ARG A 91  ? 1.0042 1.1478 0.9641 -0.0199 0.0451  -0.0228 91  ARG A O   
709  C CB  . ARG A 91  ? 0.8810 1.0535 0.8832 -0.0105 0.0589  -0.0149 91  ARG A CB  
710  C CG  . ARG A 91  ? 0.9094 1.0853 0.9038 -0.0138 0.0725  -0.0292 91  ARG A CG  
711  C CD  . ARG A 91  ? 0.9106 1.1062 0.9229 -0.0128 0.0868  -0.0366 91  ARG A CD  
712  N NE  . ARG A 91  ? 0.9193 1.1237 0.9332 -0.0192 0.0851  -0.0259 91  ARG A NE  
713  C CZ  . ARG A 91  ? 0.9493 1.1631 0.9505 -0.0324 0.0958  -0.0267 91  ARG A CZ  
714  N NH1 . ARG A 91  ? 1.0040 1.2214 0.9887 -0.0408 0.1105  -0.0384 91  ARG A NH1 
715  N NH2 . ARG A 91  ? 1.0005 1.2187 1.0032 -0.0388 0.0922  -0.0160 91  ARG A NH2 
716  N N   . ASN A 92  ? 0.6763 0.8241 0.6782 -0.0039 0.0439  -0.0193 92  ASN A N   
717  C CA  . ASN A 92  ? 0.6843 0.8215 0.6843 -0.0037 0.0431  -0.0277 92  ASN A CA  
718  C C   . ASN A 92  ? 0.6049 0.7366 0.5961 -0.0097 0.0314  -0.0244 92  ASN A C   
719  O O   . ASN A 92  ? 0.6692 0.7923 0.6590 -0.0119 0.0295  -0.0311 92  ASN A O   
720  C CB  . ASN A 92  ? 0.5884 0.7227 0.5755 -0.0064 0.0531  -0.0413 92  ASN A CB  
721  C CG  . ASN A 92  ? 0.6951 0.8160 0.6865 -0.0028 0.0535  -0.0511 92  ASN A CG  
722  O OD1 . ASN A 92  ? 0.6989 0.8148 0.7087 0.0055  0.0528  -0.0502 92  ASN A OD1 
723  N ND2 . ASN A 92  ? 0.7291 0.8402 0.7000 -0.0101 0.0529  -0.0598 92  ASN A ND2 
724  N N   . ARG A 93  ? 0.4965 0.6327 0.4839 -0.0121 0.0225  -0.0152 93  ARG A N   
725  C CA  . ARG A 93  ? 0.4997 0.6349 0.4881 -0.0151 0.0100  -0.0135 93  ARG A CA  
726  C C   . ARG A 93  ? 0.5051 0.6416 0.5154 -0.0119 0.0102  -0.0136 93  ARG A C   
727  O O   . ARG A 93  ? 0.4809 0.6165 0.4951 -0.0166 0.0046  -0.0179 93  ARG A O   
728  C CB  . ARG A 93  ? 0.5053 0.6442 0.4899 -0.0150 -0.0008 -0.0042 93  ARG A CB  
729  C CG  . ARG A 93  ? 0.4614 0.6035 0.4537 -0.0160 -0.0151 -0.0043 93  ARG A CG  
730  C CD  . ARG A 93  ? 0.4469 0.5891 0.4345 -0.0138 -0.0285 0.0033  93  ARG A CD  
731  N NE  . ARG A 93  ? 0.4365 0.5865 0.4403 -0.0123 -0.0425 0.0009  93  ARG A NE  
732  C CZ  . ARG A 93  ? 0.4604 0.6130 0.4703 -0.0071 -0.0569 0.0051  93  ARG A CZ  
733  N NH1 . ARG A 93  ? 0.4471 0.5906 0.4436 -0.0040 -0.0603 0.0132  93  ARG A NH1 
734  N NH2 . ARG A 93  ? 0.4359 0.6004 0.4672 -0.0050 -0.0689 0.0003  93  ARG A NH2 
735  N N   . PHE A 94  ? 0.5062 0.6443 0.5299 -0.0056 0.0159  -0.0088 94  PHE A N   
736  C CA  . PHE A 94  ? 0.4958 0.6321 0.5341 -0.0050 0.0167  -0.0075 94  PHE A CA  
737  C C   . PHE A 94  ? 0.4716 0.5955 0.5132 -0.0015 0.0239  -0.0090 94  PHE A C   
738  O O   . PHE A 94  ? 0.5112 0.6278 0.5582 -0.0047 0.0245  -0.0085 94  PHE A O   
739  C CB  . PHE A 94  ? 0.4261 0.5710 0.4742 -0.0016 0.0139  0.0004  94  PHE A CB  
740  C CG  . PHE A 94  ? 0.4295 0.5848 0.4804 -0.0033 0.0041  0.0009  94  PHE A CG  
741  C CD1 . PHE A 94  ? 0.4099 0.5722 0.4724 -0.0082 -0.0003 -0.0038 94  PHE A CD1 
742  C CD2 . PHE A 94  ? 0.4200 0.5773 0.4628 -0.0003 -0.0021 0.0058  94  PHE A CD2 
743  C CE1 . PHE A 94  ? 0.3997 0.5735 0.4697 -0.0075 -0.0120 -0.0045 94  PHE A CE1 
744  C CE2 . PHE A 94  ? 0.4206 0.5837 0.4659 0.0002  -0.0143 0.0064  94  PHE A CE2 
745  C CZ  . PHE A 94  ? 0.4142 0.5867 0.4748 -0.0022 -0.0200 0.0008  94  PHE A CZ  
746  N N   . GLY A 95  ? 0.4664 0.5870 0.5053 0.0042  0.0287  -0.0114 95  GLY A N   
747  C CA  . GLY A 95  ? 0.5160 0.6225 0.5594 0.0096  0.0321  -0.0141 95  GLY A CA  
748  C C   . GLY A 95  ? 0.5414 0.6454 0.5924 0.0165  0.0312  -0.0061 95  GLY A C   
749  O O   . GLY A 95  ? 0.5036 0.6083 0.5551 0.0142  0.0289  0.0017  95  GLY A O   
750  N N   . GLN A 96  ? 0.5366 0.6380 0.5940 0.0253  0.0327  -0.0089 96  GLN A N   
751  C CA  . GLN A 96  ? 0.5881 0.6843 0.6520 0.0323  0.0286  -0.0018 96  GLN A CA  
752  C C   . GLN A 96  ? 0.5649 0.6735 0.6283 0.0300  0.0266  0.0073  96  GLN A C   
753  O O   . GLN A 96  ? 0.5305 0.6303 0.5904 0.0301  0.0229  0.0149  96  GLN A O   
754  C CB  . GLN A 96  ? 0.5647 0.6351 0.6219 0.0318  0.0246  0.0017  96  GLN A CB  
755  C CG  . GLN A 96  ? 0.6289 0.6814 0.6877 0.0377  0.0237  -0.0069 96  GLN A CG  
756  C CD  . GLN A 96  ? 0.6891 0.7104 0.7355 0.0336  0.0193  -0.0031 96  GLN A CD  
757  O OE1 . GLN A 96  ? 0.7120 0.7296 0.7485 0.0217  0.0213  0.0022  96  GLN A OE1 
758  N NE2 . GLN A 96  ? 0.7018 0.7002 0.7491 0.0427  0.0137  -0.0068 96  GLN A NE2 
759  N N   . THR A 97  ? 0.4642 0.5903 0.5278 0.0274  0.0289  0.0063  97  THR A N   
760  C CA  . THR A 97  ? 0.4720 0.6061 0.5348 0.0264  0.0256  0.0144  97  THR A CA  
761  C C   . THR A 97  ? 0.4599 0.6065 0.5304 0.0289  0.0264  0.0145  97  THR A C   
762  O O   . THR A 97  ? 0.4215 0.5766 0.4872 0.0243  0.0258  0.0181  97  THR A O   
763  C CB  . THR A 97  ? 0.4402 0.5803 0.4950 0.0198  0.0244  0.0156  97  THR A CB  
764  O OG1 . THR A 97  ? 0.5129 0.6601 0.5620 0.0161  0.0273  0.0105  97  THR A OG1 
765  C CG2 . THR A 97  ? 0.4234 0.5566 0.4766 0.0163  0.0242  0.0136  97  THR A CG2 
766  N N   . PRO A 98  ? 0.5044 0.6515 0.5880 0.0361  0.0263  0.0111  98  PRO A N   
767  C CA  . PRO A 98  ? 0.4494 0.6141 0.5461 0.0371  0.0281  0.0093  98  PRO A CA  
768  C C   . PRO A 98  ? 0.4875 0.6553 0.5822 0.0342  0.0221  0.0185  98  PRO A C   
769  O O   . PRO A 98  ? 0.4821 0.6640 0.5794 0.0284  0.0250  0.0187  98  PRO A O   
770  C CB  . PRO A 98  ? 0.4613 0.6247 0.5770 0.0480  0.0257  0.0032  98  PRO A CB  
771  C CG  . PRO A 98  ? 0.4875 0.6260 0.5934 0.0518  0.0184  0.0081  98  PRO A CG  
772  C CD  . PRO A 98  ? 0.5135 0.6444 0.6017 0.0435  0.0227  0.0092  98  PRO A CD  
773  N N   . VAL A 99  ? 0.4561 0.6096 0.5441 0.0367  0.0143  0.0258  99  VAL A N   
774  C CA  . VAL A 99  ? 0.3931 0.5470 0.4776 0.0345  0.0082  0.0331  99  VAL A CA  
775  C C   . VAL A 99  ? 0.4168 0.5723 0.4881 0.0271  0.0098  0.0362  99  VAL A C   
776  O O   . VAL A 99  ? 0.3995 0.5609 0.4697 0.0223  0.0079  0.0391  99  VAL A O   
777  C CB  . VAL A 99  ? 0.4602 0.5959 0.5363 0.0385  0.0005  0.0388  99  VAL A CB  
778  C CG1 . VAL A 99  ? 0.3744 0.5066 0.4401 0.0351  -0.0045 0.0450  99  VAL A CG1 
779  C CG2 . VAL A 99  ? 0.4532 0.5853 0.5418 0.0463  -0.0067 0.0376  99  VAL A CG2 
780  N N   . GLN A 100 ? 0.4611 0.6104 0.5230 0.0258  0.0118  0.0355  100 GLN A N   
781  C CA  . GLN A 100 ? 0.4822 0.6327 0.5339 0.0207  0.0107  0.0372  100 GLN A CA  
782  C C   . GLN A 100 ? 0.4720 0.6318 0.5213 0.0143  0.0145  0.0351  100 GLN A C   
783  O O   . GLN A 100 ? 0.4822 0.6404 0.5213 0.0086  0.0111  0.0393  100 GLN A O   
784  C CB  . GLN A 100 ? 0.4778 0.6249 0.5259 0.0206  0.0116  0.0344  100 GLN A CB  
785  C CG  . GLN A 100 ? 0.4844 0.6242 0.5327 0.0235  0.0106  0.0359  100 GLN A CG  
786  C CD  . GLN A 100 ? 0.4637 0.6053 0.5138 0.0215  0.0126  0.0316  100 GLN A CD  
787  O OE1 . GLN A 100 ? 0.4784 0.6250 0.5283 0.0205  0.0087  0.0306  100 GLN A OE1 
788  N NE2 . GLN A 100 ? 0.4904 0.6268 0.5428 0.0205  0.0170  0.0291  100 GLN A NE2 
789  N N   . GLU A 101 ? 0.5183 0.6856 0.5744 0.0143  0.0218  0.0281  101 GLU A N   
790  C CA  . GLU A 101 ? 0.5543 0.7308 0.6051 0.0064  0.0285  0.0246  101 GLU A CA  
791  C C   . GLU A 101 ? 0.5273 0.7131 0.5840 0.0015  0.0292  0.0278  101 GLU A C   
792  O O   . GLU A 101 ? 0.5421 0.7274 0.5843 -0.0090 0.0302  0.0312  101 GLU A O   
793  C CB  . GLU A 101 ? 0.5460 0.7296 0.6053 0.0088  0.0379  0.0138  101 GLU A CB  
794  C CG  . GLU A 101 ? 0.5372 0.7311 0.5881 -0.0007 0.0484  0.0078  101 GLU A CG  
795  C CD  . GLU A 101 ? 0.6044 0.8068 0.6679 0.0041  0.0589  -0.0055 101 GLU A CD  
796  O OE1 . GLU A 101 ? 0.6358 0.8279 0.7025 0.0120  0.0561  -0.0092 101 GLU A OE1 
797  O OE2 . GLU A 101 ? 0.5982 0.8171 0.6689 -0.0003 0.0704  -0.0132 101 GLU A OE2 
798  N N   . ARG A 102 ? 0.4468 0.6391 0.5232 0.0079  0.0273  0.0271  102 ARG A N   
799  C CA  . ARG A 102 ? 0.4583 0.6626 0.5450 0.0024  0.0272  0.0289  102 ARG A CA  
800  C C   . ARG A 102 ? 0.4499 0.6411 0.5208 -0.0032 0.0180  0.0389  102 ARG A C   
801  O O   . ARG A 102 ? 0.4627 0.6579 0.5290 -0.0142 0.0190  0.0418  102 ARG A O   
802  C CB  . ARG A 102 ? 0.4337 0.6474 0.5469 0.0119  0.0235  0.0253  102 ARG A CB  
803  C CG  . ARG A 102 ? 0.4450 0.6748 0.5742 0.0057  0.0218  0.0261  102 ARG A CG  
804  C CD  . ARG A 102 ? 0.4246 0.6725 0.5875 0.0149  0.0199  0.0184  102 ARG A CD  
805  N NE  . ARG A 102 ? 0.4005 0.6690 0.5823 0.0064  0.0193  0.0177  102 ARG A NE  
806  C CZ  . ARG A 102 ? 0.4195 0.7021 0.6309 0.0131  0.0105  0.0144  102 ARG A CZ  
807  N NH1 . ARG A 102 ? 0.4246 0.6993 0.6472 0.0291  0.0004  0.0122  102 ARG A NH1 
808  N NH2 . ARG A 102 ? 0.4338 0.7373 0.6632 0.0026  0.0102  0.0135  102 ARG A NH2 
809  N N   . LEU A 103 ? 0.4219 0.5966 0.4837 0.0036  0.0096  0.0434  103 LEU A N   
810  C CA  . LEU A 103 ? 0.4412 0.6017 0.4875 0.0001  0.0012  0.0507  103 LEU A CA  
811  C C   . LEU A 103 ? 0.4655 0.6192 0.4924 -0.0087 0.0016  0.0533  103 LEU A C   
812  O O   . LEU A 103 ? 0.4650 0.6116 0.4805 -0.0176 -0.0024 0.0586  103 LEU A O   
813  C CB  . LEU A 103 ? 0.4060 0.5528 0.4476 0.0094  -0.0047 0.0523  103 LEU A CB  
814  C CG  . LEU A 103 ? 0.3849 0.5296 0.4351 0.0154  -0.0085 0.0526  103 LEU A CG  
815  C CD1 . LEU A 103 ? 0.3713 0.5030 0.4135 0.0221  -0.0099 0.0528  103 LEU A CD1 
816  C CD2 . LEU A 103 ? 0.3496 0.4919 0.3990 0.0109  -0.0157 0.0565  103 LEU A CD2 
817  N N   . SER A 104 ? 0.4331 0.5863 0.4536 -0.0074 0.0050  0.0500  104 SER A N   
818  C CA  . SER A 104 ? 0.4759 0.6199 0.4743 -0.0158 0.0029  0.0527  104 SER A CA  
819  C C   . SER A 104 ? 0.5042 0.6535 0.4942 -0.0303 0.0099  0.0539  104 SER A C   
820  O O   . SER A 104 ? 0.5085 0.6429 0.4762 -0.0404 0.0045  0.0607  104 SER A O   
821  C CB  . SER A 104 ? 0.4955 0.6412 0.4904 -0.0134 0.0060  0.0471  104 SER A CB  
822  O OG  . SER A 104 ? 0.4987 0.6337 0.4687 -0.0226 0.0026  0.0498  104 SER A OG  
823  N N   . CYS A 105 ? 0.5319 0.7017 0.5392 -0.0320 0.0224  0.0466  105 CYS A N   
824  C CA  . CYS A 105 ? 0.5303 0.7107 0.5331 -0.0472 0.0329  0.0453  105 CYS A CA  
825  C C   . CYS A 105 ? 0.5818 0.7614 0.5879 -0.0552 0.0283  0.0518  105 CYS A C   
826  O O   . CYS A 105 ? 0.5932 0.7673 0.5806 -0.0721 0.0313  0.0563  105 CYS A O   
827  C CB  . CYS A 105 ? 0.5312 0.7371 0.5582 -0.0444 0.0477  0.0331  105 CYS A CB  
828  S SG  . CYS A 105 ? 0.6517 0.8536 0.6637 -0.0419 0.0550  0.0247  105 CYS A SG  
829  N N   . LEU A 106 ? 0.5721 0.7534 0.5975 -0.0450 0.0202  0.0529  106 LEU A N   
830  C CA  . LEU A 106 ? 0.5292 0.7068 0.5561 -0.0526 0.0135  0.0587  106 LEU A CA  
831  C C   . LEU A 106 ? 0.5557 0.7031 0.5503 -0.0592 0.0027  0.0685  106 LEU A C   
832  O O   . LEU A 106 ? 0.5633 0.7028 0.5456 -0.0745 0.0012  0.0740  106 LEU A O   
833  C CB  . LEU A 106 ? 0.5270 0.7069 0.5744 -0.0395 0.0047  0.0579  106 LEU A CB  
834  C CG  . LEU A 106 ? 0.5125 0.7186 0.5937 -0.0328 0.0096  0.0497  106 LEU A CG  
835  C CD1 . LEU A 106 ? 0.4538 0.6509 0.5423 -0.0174 -0.0012 0.0505  106 LEU A CD1 
836  C CD2 . LEU A 106 ? 0.4668 0.6944 0.5677 -0.0451 0.0130  0.0476  106 LEU A CD2 
837  N N   . ALA A 107 ? 0.4202 0.5499 0.4022 -0.0480 -0.0056 0.0703  107 ALA A N   
838  C CA  . ALA A 107 ? 0.4560 0.5562 0.4106 -0.0504 -0.0183 0.0780  107 ALA A CA  
839  C C   . ALA A 107 ? 0.5115 0.6007 0.4380 -0.0667 -0.0159 0.0826  107 ALA A C   
840  O O   . ALA A 107 ? 0.5257 0.5910 0.4283 -0.0776 -0.0244 0.0908  107 ALA A O   
841  C CB  . ALA A 107 ? 0.4082 0.4990 0.3630 -0.0337 -0.0265 0.0761  107 ALA A CB  
842  N N   . LYS A 108 ? 0.6163 0.7196 0.5419 -0.0698 -0.0044 0.0773  108 LYS A N   
843  C CA  . LYS A 108 ? 0.6133 0.7028 0.5053 -0.0853 -0.0020 0.0812  108 LYS A CA  
844  C C   . LYS A 108 ? 0.5934 0.6905 0.4775 -0.1078 0.0110  0.0827  108 LYS A C   
845  O O   . LYS A 108 ? 0.6254 0.6975 0.4751 -0.1245 0.0063  0.0918  108 LYS A O   
846  C CB  . LYS A 108 ? 0.6194 0.7198 0.5111 -0.0806 0.0058  0.0733  108 LYS A CB  
847  C CG  . LYS A 108 ? 0.5954 0.6810 0.4486 -0.0968 0.0087  0.0760  108 LYS A CG  
848  C CD  . LYS A 108 ? 0.6441 0.7496 0.5032 -0.0961 0.0241  0.0644  108 LYS A CD  
849  C CE  . LYS A 108 ? 0.6521 0.7457 0.4695 -0.1165 0.0325  0.0650  108 LYS A CE  
850  N NZ  . LYS A 108 ? 0.6494 0.7635 0.4744 -0.1150 0.0494  0.0510  108 LYS A NZ  
851  N N   . ASN A 109 ? 0.6867 0.8181 0.6022 -0.1091 0.0275  0.0734  109 ASN A N   
852  C CA  . ASN A 109 ? 0.6589 0.8059 0.5745 -0.1310 0.0429  0.0720  109 ASN A CA  
853  C C   . ASN A 109 ? 0.6827 0.8163 0.5940 -0.1425 0.0338  0.0812  109 ASN A C   
854  O O   . ASN A 109 ? 0.7363 0.8716 0.6354 -0.1661 0.0432  0.0839  109 ASN A O   
855  C CB  . ASN A 109 ? 0.6337 0.8238 0.5930 -0.1256 0.0602  0.0576  109 ASN A CB  
856  C CG  . ASN A 109 ? 0.6354 0.8361 0.5969 -0.1156 0.0702  0.0471  109 ASN A CG  
857  O OD1 . ASN A 109 ? 0.6546 0.8327 0.5910 -0.1095 0.0617  0.0505  109 ASN A OD1 
858  N ND2 . ASN A 109 ? 0.6531 0.8884 0.6472 -0.1133 0.0871  0.0332  109 ASN A ND2 
859  N N   . ASN A 110 ? 0.6769 0.7984 0.5987 -0.1276 0.0171  0.0849  110 ASN A N   
860  C CA  . ASN A 110 ? 0.7027 0.8072 0.6185 -0.1371 0.0065  0.0927  110 ASN A CA  
861  C C   . ASN A 110 ? 0.7288 0.7868 0.6071 -0.1350 -0.0133 0.1037  110 ASN A C   
862  O O   . ASN A 110 ? 0.7138 0.7511 0.5842 -0.1401 -0.0248 0.1098  110 ASN A O   
863  C CB  . ASN A 110 ? 0.6611 0.7842 0.6147 -0.1233 0.0015  0.0876  110 ASN A CB  
864  C CG  . ASN A 110 ? 0.6179 0.7859 0.6124 -0.1228 0.0172  0.0763  110 ASN A CG  
865  O OD1 . ASN A 110 ? 0.5909 0.7797 0.6006 -0.1397 0.0260  0.0739  110 ASN A OD1 
866  N ND2 . ASN A 110 ? 0.5684 0.7512 0.5817 -0.1038 0.0204  0.0686  110 ASN A ND2 
867  N N   . SER A 111 ? 0.6681 0.7089 0.5247 -0.1267 -0.0189 0.1054  111 SER A N   
868  C CA  . SER A 111 ? 0.6796 0.6767 0.5024 -0.1232 -0.0395 0.1148  111 SER A CA  
869  C C   . SER A 111 ? 0.7017 0.6835 0.5349 -0.1102 -0.0548 0.1160  111 SER A C   
870  O O   . SER A 111 ? 0.6653 0.6153 0.4763 -0.1193 -0.0669 0.1239  111 SER A O   
871  C CB  . SER A 111 ? 0.6966 0.6634 0.4750 -0.1488 -0.0414 0.1256  111 SER A CB  
872  O OG  . SER A 111 ? 0.7173 0.6379 0.4627 -0.1435 -0.0648 0.1349  111 SER A OG  
873  N N   . ILE A 112 ? 0.6491 0.6515 0.5137 -0.0894 -0.0538 0.1076  112 ILE A N   
874  C CA  . ILE A 112 ? 0.5819 0.5748 0.4579 -0.0763 -0.0645 0.1059  112 ILE A CA  
875  C C   . ILE A 112 ? 0.5613 0.5668 0.4573 -0.0531 -0.0648 0.0980  112 ILE A C   
876  O O   . ILE A 112 ? 0.5722 0.6054 0.4870 -0.0487 -0.0529 0.0923  112 ILE A O   
877  C CB  . ILE A 112 ? 0.6212 0.6327 0.5177 -0.0844 -0.0581 0.1037  112 ILE A CB  
878  C CG1 . ILE A 112 ? 0.6280 0.6234 0.5280 -0.0734 -0.0704 0.1022  112 ILE A CG1 
879  C CG2 . ILE A 112 ? 0.5812 0.6339 0.5107 -0.0788 -0.0429 0.0953  112 ILE A CG2 
880  C CD1 . ILE A 112 ? 0.5679 0.5747 0.4817 -0.0846 -0.0690 0.1016  112 ILE A CD1 
881  N N   . TYR A 113 ? 0.6384 0.6230 0.5304 -0.0389 -0.0779 0.0969  113 TYR A N   
882  C CA  . TYR A 113 ? 0.6191 0.6175 0.5317 -0.0192 -0.0760 0.0884  113 TYR A CA  
883  C C   . TYR A 113 ? 0.5970 0.6170 0.5307 -0.0173 -0.0664 0.0837  113 TYR A C   
884  O O   . TYR A 113 ? 0.6304 0.6434 0.5620 -0.0234 -0.0695 0.0854  113 TYR A O   
885  C CB  . TYR A 113 ? 0.5998 0.5735 0.5062 -0.0050 -0.0902 0.0860  113 TYR A CB  
886  C CG  . TYR A 113 ? 0.6190 0.5796 0.5163 0.0021  -0.1011 0.0868  113 TYR A CG  
887  C CD1 . TYR A 113 ? 0.6430 0.5798 0.5126 -0.0100 -0.1108 0.0961  113 TYR A CD1 
888  C CD2 . TYR A 113 ? 0.5725 0.5436 0.4881 0.0200  -0.1026 0.0781  113 TYR A CD2 
889  C CE1 . TYR A 113 ? 0.6397 0.5613 0.4987 -0.0030 -0.1247 0.0975  113 TYR A CE1 
890  C CE2 . TYR A 113 ? 0.5881 0.5491 0.4995 0.0275  -0.1156 0.0780  113 TYR A CE2 
891  C CZ  . TYR A 113 ? 0.6605 0.5956 0.5427 0.0167  -0.1280 0.0880  113 TYR A CZ  
892  O OH  . TYR A 113 ? 0.6629 0.5856 0.5392 0.0247  -0.1443 0.0884  113 TYR A OH  
893  N N   . VAL A 114 ? 0.5532 0.5964 0.5054 -0.0090 -0.0567 0.0779  114 VAL A N   
894  C CA  . VAL A 114 ? 0.5331 0.5934 0.5027 -0.0061 -0.0496 0.0742  114 VAL A CA  
895  C C   . VAL A 114 ? 0.5541 0.6147 0.5301 0.0088  -0.0485 0.0681  114 VAL A C   
896  O O   . VAL A 114 ? 0.5348 0.6021 0.5157 0.0150  -0.0453 0.0649  114 VAL A O   
897  C CB  . VAL A 114 ? 0.5559 0.6416 0.5403 -0.0118 -0.0381 0.0728  114 VAL A CB  
898  C CG1 . VAL A 114 ? 0.5270 0.6266 0.5292 -0.0058 -0.0343 0.0689  114 VAL A CG1 
899  C CG2 . VAL A 114 ? 0.5156 0.6049 0.4959 -0.0284 -0.0361 0.0769  114 VAL A CG2 
900  N N   . VAL A 115 ? 0.4624 0.5151 0.4366 0.0128  -0.0511 0.0661  115 VAL A N   
901  C CA  . VAL A 115 ? 0.4466 0.5000 0.4240 0.0237  -0.0469 0.0599  115 VAL A CA  
902  C C   . VAL A 115 ? 0.4401 0.5029 0.4234 0.0220  -0.0424 0.0602  115 VAL A C   
903  O O   . VAL A 115 ? 0.4562 0.5139 0.4360 0.0170  -0.0481 0.0627  115 VAL A O   
904  C CB  . VAL A 115 ? 0.4543 0.4868 0.4191 0.0300  -0.0532 0.0561  115 VAL A CB  
905  C CG1 . VAL A 115 ? 0.4173 0.4535 0.3844 0.0389  -0.0448 0.0483  115 VAL A CG1 
906  C CG2 . VAL A 115 ? 0.4117 0.4296 0.3704 0.0335  -0.0620 0.0558  115 VAL A CG2 
907  N N   . ALA A 116 ? 0.5036 0.5782 0.4956 0.0259  -0.0340 0.0576  116 ALA A N   
908  C CA  . ALA A 116 ? 0.4873 0.5664 0.4832 0.0254  -0.0321 0.0585  116 ALA A CA  
909  C C   . ALA A 116 ? 0.5165 0.5917 0.5072 0.0306  -0.0252 0.0549  116 ALA A C   
910  O O   . ALA A 116 ? 0.4886 0.5660 0.4804 0.0339  -0.0195 0.0507  116 ALA A O   
911  C CB  . ALA A 116 ? 0.4690 0.5656 0.4812 0.0222  -0.0289 0.0598  116 ALA A CB  
912  N N   . ASN A 117 ? 0.4833 0.5517 0.4675 0.0304  -0.0265 0.0566  117 ASN A N   
913  C CA  . ASN A 117 ? 0.4981 0.5589 0.4717 0.0318  -0.0193 0.0546  117 ASN A CA  
914  C C   . ASN A 117 ? 0.4861 0.5504 0.4668 0.0314  -0.0181 0.0572  117 ASN A C   
915  O O   . ASN A 117 ? 0.4878 0.5521 0.4738 0.0317  -0.0266 0.0606  117 ASN A O   
916  C CB  . ASN A 117 ? 0.5177 0.5582 0.4673 0.0310  -0.0228 0.0547  117 ASN A CB  
917  C CG  . ASN A 117 ? 0.5352 0.5658 0.4688 0.0294  -0.0134 0.0530  117 ASN A CG  
918  O OD1 . ASN A 117 ? 0.5720 0.5929 0.4968 0.0272  -0.0162 0.0576  117 ASN A OD1 
919  N ND2 . ASN A 117 ? 0.5313 0.5646 0.4623 0.0302  -0.0021 0.0459  117 ASN A ND2 
920  N N   . ILE A 118 ? 0.4861 0.5540 0.4693 0.0309  -0.0084 0.0547  118 ILE A N   
921  C CA  . ILE A 118 ? 0.5311 0.5991 0.5202 0.0306  -0.0071 0.0562  118 ILE A CA  
922  C C   . ILE A 118 ? 0.5524 0.6114 0.5296 0.0266  0.0028  0.0547  118 ILE A C   
923  O O   . ILE A 118 ? 0.5456 0.6003 0.5108 0.0243  0.0091  0.0520  118 ILE A O   
924  C CB  . ILE A 118 ? 0.4875 0.5742 0.4982 0.0317  -0.0053 0.0537  118 ILE A CB  
925  C CG1 . ILE A 118 ? 0.4643 0.5620 0.4806 0.0304  0.0020  0.0493  118 ILE A CG1 
926  C CG2 . ILE A 118 ? 0.4359 0.5324 0.4571 0.0325  -0.0125 0.0550  118 ILE A CG2 
927  C CD1 . ILE A 118 ? 0.4487 0.5609 0.4797 0.0298  0.0035  0.0467  118 ILE A CD1 
928  N N   . GLY A 119 ? 0.5131 0.5679 0.4927 0.0251  0.0048  0.0556  119 GLY A N   
929  C CA  . GLY A 119 ? 0.5436 0.5869 0.5099 0.0182  0.0140  0.0552  119 GLY A CA  
930  C C   . GLY A 119 ? 0.5161 0.5755 0.4999 0.0154  0.0225  0.0498  119 GLY A C   
931  O O   . GLY A 119 ? 0.5380 0.6041 0.5359 0.0184  0.0192  0.0487  119 GLY A O   
932  N N   . ASP A 120 ? 0.5411 0.6077 0.5247 0.0095  0.0336  0.0451  120 ASP A N   
933  C CA  . ASP A 120 ? 0.5194 0.6017 0.5200 0.0051  0.0407  0.0393  120 ASP A CA  
934  C C   . ASP A 120 ? 0.5951 0.6621 0.5830 -0.0061 0.0486  0.0405  120 ASP A C   
935  O O   . ASP A 120 ? 0.6447 0.6954 0.6106 -0.0130 0.0546  0.0433  120 ASP A O   
936  C CB  . ASP A 120 ? 0.5035 0.6073 0.5185 0.0059  0.0468  0.0317  120 ASP A CB  
937  C CG  . ASP A 120 ? 0.5161 0.6404 0.5543 0.0037  0.0488  0.0253  120 ASP A CG  
938  O OD1 . ASP A 120 ? 0.5189 0.6426 0.5620 0.0038  0.0436  0.0265  120 ASP A OD1 
939  O OD2 . ASP A 120 ? 0.4900 0.6319 0.5424 0.0024  0.0551  0.0178  120 ASP A OD2 
940  N N   . LYS A 121 ? 0.5752 0.6447 0.5736 -0.0094 0.0488  0.0385  121 LYS A N   
941  C CA  . LYS A 121 ? 0.5765 0.6324 0.5651 -0.0224 0.0567  0.0388  121 LYS A CA  
942  C C   . LYS A 121 ? 0.5610 0.6420 0.5735 -0.0285 0.0634  0.0301  121 LYS A C   
943  O O   . LYS A 121 ? 0.5412 0.6390 0.5726 -0.0218 0.0570  0.0259  121 LYS A O   
944  C CB  . LYS A 121 ? 0.6135 0.6421 0.5898 -0.0215 0.0483  0.0442  121 LYS A CB  
945  C CG  . LYS A 121 ? 0.6089 0.6474 0.6044 -0.0156 0.0427  0.0393  121 LYS A CG  
946  C CD  . LYS A 121 ? 0.6537 0.6621 0.6367 -0.0134 0.0351  0.0430  121 LYS A CD  
947  C CE  . LYS A 121 ? 0.6742 0.6880 0.6724 -0.0086 0.0316  0.0362  121 LYS A CE  
948  N NZ  . LYS A 121 ? 0.6658 0.6501 0.6542 -0.0017 0.0223  0.0389  121 LYS A NZ  
949  N N   . LYS A 122 ? 0.5639 0.6479 0.5748 -0.0424 0.0761  0.0269  122 LYS A N   
950  C CA  . LYS A 122 ? 0.5793 0.6913 0.6172 -0.0495 0.0824  0.0174  122 LYS A CA  
951  C C   . LYS A 122 ? 0.6249 0.7221 0.6525 -0.0685 0.0917  0.0180  122 LYS A C   
952  O O   . LYS A 122 ? 0.6329 0.7241 0.6465 -0.0814 0.1052  0.0186  122 LYS A O   
953  C CB  . LYS A 122 ? 0.5538 0.6955 0.6109 -0.0474 0.0904  0.0091  122 LYS A CB  
954  C CG  . LYS A 122 ? 0.4780 0.6359 0.5501 -0.0300 0.0795  0.0069  122 LYS A CG  
955  C CD  . LYS A 122 ? 0.4937 0.6671 0.5876 -0.0257 0.0683  0.0032  122 LYS A CD  
956  C CE  . LYS A 122 ? 0.4479 0.6284 0.5477 -0.0106 0.0557  0.0038  122 LYS A CE  
957  N NZ  . LYS A 122 ? 0.4591 0.6183 0.5393 -0.0051 0.0477  0.0124  122 LYS A NZ  
958  N N   . PRO A 123 ? 0.7141 0.8020 0.7444 -0.0722 0.0855  0.0177  123 PRO A N   
959  C CA  . PRO A 123 ? 0.7237 0.7936 0.7425 -0.0921 0.0934  0.0185  123 PRO A CA  
960  C C   . PRO A 123 ? 0.7409 0.8419 0.7822 -0.1076 0.1080  0.0093  123 PRO A C   
961  O O   . PRO A 123 ? 0.6894 0.8283 0.7644 -0.1014 0.1068  -0.0001 123 PRO A O   
962  C CB  . PRO A 123 ? 0.6768 0.7362 0.7001 -0.0896 0.0820  0.0168  123 PRO A CB  
963  C CG  . PRO A 123 ? 0.7438 0.8007 0.7662 -0.0684 0.0694  0.0195  123 PRO A CG  
964  C CD  . PRO A 123 ? 0.6802 0.7650 0.7159 -0.0590 0.0713  0.0178  123 PRO A CD  
965  N N   . CYS A 124 ? 0.9680 0.7719 0.9467 -0.2254 0.0599  0.0249  124 CYS A N   
966  C CA  . CYS A 124 ? 0.9655 0.8127 0.9812 -0.2560 0.0569  0.0275  124 CYS A CA  
967  C C   . CYS A 124 ? 1.0387 0.8405 1.0493 -0.2880 0.0607  0.0366  124 CYS A C   
968  O O   . CYS A 124 ? 1.0462 0.7904 1.0272 -0.2826 0.0706  0.0469  124 CYS A O   
969  C CB  . CYS A 124 ? 0.9385 0.8538 0.9845 -0.2486 0.0693  0.0405  124 CYS A CB  
970  S SG  . CYS A 124 ? 0.9829 0.8847 1.0078 -0.2288 0.0913  0.0630  124 CYS A SG  
971  N N   . ASP A 125 ? 1.2576 1.0864 1.2995 -0.3218 0.0514  0.0333  125 ASP A N   
972  C CA  . ASP A 125 ? 1.3083 1.1001 1.3529 -0.3603 0.0513  0.0409  125 ASP A CA  
973  C C   . ASP A 125 ? 1.3085 1.1540 1.3917 -0.3802 0.0684  0.0638  125 ASP A C   
974  O O   . ASP A 125 ? 1.2389 1.1558 1.3500 -0.3656 0.0772  0.0687  125 ASP A O   
975  C CB  . ASP A 125 ? 1.3417 1.1282 1.3963 -0.3888 0.0262  0.0210  125 ASP A CB  
976  C CG  . ASP A 125 ? 1.4422 1.1328 1.4483 -0.3957 0.0157  0.0076  125 ASP A CG  
977  O OD1 . ASP A 125 ? 1.4523 1.0816 1.4224 -0.3798 0.0294  0.0162  125 ASP A OD1 
978  O OD2 . ASP A 125 ? 1.5187 1.1940 1.5209 -0.4158 -0.0070 -0.0119 125 ASP A OD2 
979  N N   . THR A 126 ? 1.5801 1.3881 1.6627 -0.4141 0.0741  0.0780  126 THR A N   
980  C CA  . THR A 126 ? 1.5773 1.4401 1.6998 -0.4396 0.0909  0.1004  126 THR A CA  
981  C C   . THR A 126 ? 1.5443 1.4932 1.7251 -0.4582 0.0806  0.0920  126 THR A C   
982  O O   . THR A 126 ? 1.5218 1.5413 1.7433 -0.4673 0.0971  0.1076  126 THR A O   
983  C CB  . THR A 126 ? 1.6404 1.4428 1.7522 -0.4776 0.0968  0.1180  126 THR A CB  
984  O OG1 . THR A 126 ? 1.6611 1.3672 1.7265 -0.4761 0.0819  0.1041  126 THR A OG1 
985  C CG2 . THR A 126 ? 1.5627 1.3588 1.6587 -0.4691 0.1246  0.1478  126 THR A CG2 
986  N N   . SER A 127 ? 1.3719 1.3174 1.5563 -0.4620 0.0537  0.0678  127 SER A N   
987  C CA  . SER A 127 ? 1.3300 1.3608 1.5679 -0.4696 0.0400  0.0581  127 SER A CA  
988  C C   . SER A 127 ? 1.2508 1.3580 1.5119 -0.4352 0.0558  0.0634  127 SER A C   
989  O O   . SER A 127 ? 1.1799 1.3704 1.4961 -0.4439 0.0580  0.0672  127 SER A O   
990  C CB  . SER A 127 ? 1.3378 1.3444 1.5583 -0.4647 0.0085  0.0305  127 SER A CB  
991  O OG  . SER A 127 ? 1.3125 1.2859 1.4875 -0.4214 0.0087  0.0194  127 SER A OG  
992  N N   . ASP A 128 ? 1.1538 1.2341 1.3746 -0.3959 0.0663  0.0631  128 ASP A N   
993  C CA  . ASP A 128 ? 1.0900 1.2303 1.3237 -0.3618 0.0791  0.0653  128 ASP A CA  
994  C C   . ASP A 128 ? 1.1140 1.2782 1.3546 -0.3647 0.1092  0.0893  128 ASP A C   
995  O O   . ASP A 128 ? 1.1227 1.2299 1.3244 -0.3640 0.1217  0.1027  128 ASP A O   
996  C CB  . ASP A 128 ? 1.0735 1.1749 1.2619 -0.3219 0.0744  0.0543  128 ASP A CB  
997  C CG  . ASP A 128 ? 1.0454 1.1980 1.2412 -0.2877 0.0854  0.0555  128 ASP A CG  
998  O OD1 . ASP A 128 ? 1.0031 1.2235 1.2389 -0.2914 0.0962  0.0618  128 ASP A OD1 
999  O OD2 . ASP A 128 ? 0.9880 1.1129 1.1501 -0.2572 0.0830  0.0494  128 ASP A OD2 
1000 N N   . PRO A 129 ? 1.3092 1.5558 1.5962 -0.3664 0.1220  0.0960  129 PRO A N   
1001 C CA  . PRO A 129 ? 1.3009 1.5712 1.5905 -0.3708 0.1533  0.1197  129 PRO A CA  
1002 C C   . PRO A 129 ? 1.3037 1.5480 1.5449 -0.3343 0.1678  0.1246  129 PRO A C   
1003 O O   . PRO A 129 ? 1.3434 1.5821 1.5680 -0.3390 0.1913  0.1457  129 PRO A O   
1004 C CB  . PRO A 129 ? 1.2243 1.5953 1.5758 -0.3730 0.1623  0.1203  129 PRO A CB  
1005 C CG  . PRO A 129 ? 1.2536 1.6486 1.6220 -0.3522 0.1363  0.0960  129 PRO A CG  
1006 C CD  . PRO A 129 ? 1.2785 1.6008 1.6177 -0.3644 0.1091  0.0834  129 PRO A CD  
1007 N N   . GLN A 130 ? 1.0490 1.2786 1.2667 -0.2994 0.1540  0.1073  130 GLN A N   
1008 C CA  . GLN A 130 ? 1.0907 1.2952 1.2640 -0.2670 0.1637  0.1112  130 GLN A CA  
1009 C C   . GLN A 130 ? 1.0881 1.2155 1.2164 -0.2550 0.1497  0.1062  130 GLN A C   
1010 O O   . GLN A 130 ? 1.0520 1.1642 1.1504 -0.2247 0.1489  0.1034  130 GLN A O   
1011 C CB  . GLN A 130 ? 1.0718 1.3269 1.2545 -0.2336 0.1633  0.0981  130 GLN A CB  
1012 C CG  . GLN A 130 ? 1.0489 1.3823 1.2724 -0.2361 0.1814  0.1027  130 GLN A CG  
1013 C CD  . GLN A 130 ? 1.0937 1.4645 1.3196 -0.1992 0.1795  0.0876  130 GLN A CD  
1014 O OE1 . GLN A 130 ? 1.0923 1.4366 1.3006 -0.1782 0.1596  0.0723  130 GLN A OE1 
1015 N NE2 . GLN A 130 ? 1.0595 1.4893 1.3047 -0.1904 0.2013  0.0921  130 GLN A NE2 
1016 N N   . CYS A 131 ? 0.9677 1.0468 1.0909 -0.2777 0.1386  0.1047  131 CYS A N   
1017 C CA  . CYS A 131 ? 0.9567 0.9625 1.0369 -0.2643 0.1298  0.1016  131 CYS A CA  
1018 C C   . CYS A 131 ? 0.9454 0.9170 0.9912 -0.2556 0.1464  0.1231  131 CYS A C   
1019 O O   . CYS A 131 ? 0.8977 0.8638 0.9452 -0.2788 0.1609  0.1425  131 CYS A O   
1020 C CB  . CYS A 131 ? 0.9520 0.9075 1.0293 -0.2907 0.1163  0.0948  131 CYS A CB  
1021 S SG  . CYS A 131 ? 1.0187 0.8892 1.0452 -0.2680 0.1070  0.0872  131 CYS A SG  
1022 N N   . PRO A 132 ? 0.8632 0.8118 0.8781 -0.2239 0.1438  0.1218  132 PRO A N   
1023 C CA  . PRO A 132 ? 0.8161 0.7328 0.7975 -0.2144 0.1559  0.1431  132 PRO A CA  
1024 C C   . PRO A 132 ? 0.8606 0.7102 0.8237 -0.2339 0.1576  0.1562  132 PRO A C   
1025 O O   . PRO A 132 ? 0.8957 0.7089 0.8613 -0.2456 0.1457  0.1438  132 PRO A O   
1026 C CB  . PRO A 132 ? 0.7815 0.6859 0.7406 -0.1787 0.1460  0.1349  132 PRO A CB  
1027 C CG  . PRO A 132 ? 0.7702 0.7198 0.7537 -0.1690 0.1350  0.1127  132 PRO A CG  
1028 C CD  . PRO A 132 ? 0.8050 0.7623 0.8167 -0.1961 0.1293  0.1027  132 PRO A CD  
1029 N N   . PRO A 133 ? 1.0357 0.8630 0.9765 -0.2383 0.1718  0.1814  133 PRO A N   
1030 C CA  . PRO A 133 ? 1.0406 0.7982 0.9627 -0.2584 0.1739  0.1965  133 PRO A CA  
1031 C C   . PRO A 133 ? 1.0917 0.7821 0.9906 -0.2412 0.1597  0.1860  133 PRO A C   
1032 O O   . PRO A 133 ? 1.1521 0.7807 1.0394 -0.2593 0.1575  0.1900  133 PRO A O   
1033 C CB  . PRO A 133 ? 1.0334 0.7808 0.9274 -0.2547 0.1901  0.2266  133 PRO A CB  
1034 C CG  . PRO A 133 ? 1.0568 0.8715 0.9549 -0.2352 0.1969  0.2248  133 PRO A CG  
1035 C CD  . PRO A 133 ? 0.9686 0.8380 0.9025 -0.2312 0.1880  0.1974  133 PRO A CD  
1036 N N   . ASP A 134 ? 0.9140 0.6111 0.8035 -0.2062 0.1514  0.1747  134 ASP A N   
1037 C CA  . ASP A 134 ? 0.9959 0.6355 0.8653 -0.1866 0.1415  0.1659  134 ASP A CA  
1038 C C   . ASP A 134 ? 0.9741 0.6186 0.8575 -0.1873 0.1287  0.1369  134 ASP A C   
1039 O O   . ASP A 134 ? 0.9894 0.5996 0.8574 -0.1656 0.1221  0.1261  134 ASP A O   
1040 C CB  . ASP A 134 ? 0.9094 0.5504 0.7609 -0.1491 0.1402  0.1739  134 ASP A CB  
1041 C CG  . ASP A 134 ? 0.9141 0.6213 0.7822 -0.1321 0.1355  0.1617  134 ASP A CG  
1042 O OD1 . ASP A 134 ? 0.9006 0.6503 0.7931 -0.1452 0.1333  0.1461  134 ASP A OD1 
1043 O OD2 . ASP A 134 ? 0.9423 0.6572 0.7994 -0.1052 0.1323  0.1677  134 ASP A OD2 
1044 N N   . GLY A 135 ? 0.8790 0.5677 0.7910 -0.2106 0.1254  0.1251  135 GLY A N   
1045 C CA  . GLY A 135 ? 0.8709 0.5516 0.7912 -0.2208 0.1118  0.1010  135 GLY A CA  
1046 C C   . GLY A 135 ? 0.8861 0.6067 0.8157 -0.1990 0.1018  0.0814  135 GLY A C   
1047 O O   . GLY A 135 ? 0.9511 0.6592 0.8794 -0.2039 0.0897  0.0616  135 GLY A O   
1048 N N   . ARG A 136 ? 0.8814 0.6458 0.8167 -0.1761 0.1055  0.0862  136 ARG A N   
1049 C CA  . ARG A 136 ? 0.8628 0.6609 0.8065 -0.1575 0.0956  0.0692  136 ARG A CA  
1050 C C   . ARG A 136 ? 0.7997 0.6522 0.7554 -0.1424 0.0998  0.0757  136 ARG A C   
1051 O O   . ARG A 136 ? 0.8181 0.6719 0.7653 -0.1379 0.1100  0.0929  136 ARG A O   
1052 C CB  . ARG A 136 ? 0.7992 0.5561 0.7187 -0.1336 0.0917  0.0620  136 ARG A CB  
1053 C CG  . ARG A 136 ? 0.7921 0.5460 0.7000 -0.1067 0.0978  0.0760  136 ARG A CG  
1054 C CD  . ARG A 136 ? 0.8242 0.5316 0.7139 -0.1089 0.1067  0.0946  136 ARG A CD  
1055 N NE  . ARG A 136 ? 0.8551 0.5593 0.7341 -0.0812 0.1091  0.1081  136 ARG A NE  
1056 C CZ  . ARG A 136 ? 0.8797 0.5415 0.7403 -0.0732 0.1145  0.1255  136 ARG A CZ  
1057 N NH1 . ARG A 136 ? 0.8847 0.4981 0.7326 -0.0916 0.1195  0.1326  136 ARG A NH1 
1058 N NH2 . ARG A 136 ? 0.8803 0.5469 0.7356 -0.0464 0.1133  0.1367  136 ARG A NH2 
1059 N N   . TYR A 137 ? 0.7083 0.6022 0.6805 -0.1350 0.0910  0.0616  137 TYR A N   
1060 C CA  . TYR A 137 ? 0.6801 0.6138 0.6570 -0.1154 0.0915  0.0631  137 TYR A CA  
1061 C C   . TYR A 137 ? 0.7231 0.6376 0.6828 -0.0907 0.0859  0.0613  137 TYR A C   
1062 O O   . TYR A 137 ? 0.6753 0.5644 0.6278 -0.0868 0.0797  0.0521  137 TYR A O   
1063 C CB  . TYR A 137 ? 0.6647 0.6479 0.6674 -0.1171 0.0838  0.0496  137 TYR A CB  
1064 C CG  . TYR A 137 ? 0.6704 0.6873 0.6997 -0.1396 0.0895  0.0515  137 TYR A CG  
1065 C CD1 . TYR A 137 ? 0.7237 0.7715 0.7596 -0.1405 0.1040  0.0632  137 TYR A CD1 
1066 C CD2 . TYR A 137 ? 0.6758 0.6965 0.7237 -0.1602 0.0804  0.0420  137 TYR A CD2 
1067 C CE1 . TYR A 137 ? 0.6880 0.7736 0.7528 -0.1610 0.1122  0.0666  137 TYR A CE1 
1068 C CE2 . TYR A 137 ? 0.6826 0.7416 0.7621 -0.1825 0.0849  0.0451  137 TYR A CE2 
1069 C CZ  . TYR A 137 ? 0.7335 0.8272 0.8238 -0.1825 0.1023  0.0580  137 TYR A CZ  
1070 O OH  . TYR A 137 ? 0.7955 0.9341 0.9217 -0.2045 0.1099  0.0629  137 TYR A OH  
1071 N N   . GLN A 138 ? 0.6785 0.6067 0.6313 -0.0745 0.0881  0.0702  138 GLN A N   
1072 C CA  . GLN A 138 ? 0.6809 0.6041 0.6260 -0.0530 0.0810  0.0691  138 GLN A CA  
1073 C C   . GLN A 138 ? 0.6902 0.6525 0.6426 -0.0432 0.0748  0.0642  138 GLN A C   
1074 O O   . GLN A 138 ? 0.6422 0.6226 0.5908 -0.0429 0.0796  0.0706  138 GLN A O   
1075 C CB  . GLN A 138 ? 0.6814 0.5757 0.6092 -0.0417 0.0853  0.0854  138 GLN A CB  
1076 C CG  . GLN A 138 ? 0.6993 0.5522 0.6163 -0.0534 0.0940  0.0943  138 GLN A CG  
1077 C CD  . GLN A 138 ? 0.7701 0.5894 0.6705 -0.0372 0.0962  0.1099  138 GLN A CD  
1078 O OE1 . GLN A 138 ? 0.8245 0.5993 0.7147 -0.0381 0.1004  0.1128  138 GLN A OE1 
1079 N NE2 . GLN A 138 ? 0.7717 0.6107 0.6687 -0.0218 0.0921  0.1199  138 GLN A NE2 
1080 N N   . TYR A 139 ? 0.6288 0.6003 0.5877 -0.0348 0.0646  0.0533  139 TYR A N   
1081 C CA  . TYR A 139 ? 0.6003 0.6017 0.5654 -0.0268 0.0568  0.0466  139 TYR A CA  
1082 C C   . TYR A 139 ? 0.6069 0.6044 0.5671 -0.0124 0.0478  0.0486  139 TYR A C   
1083 O O   . TYR A 139 ? 0.5576 0.5381 0.5171 -0.0087 0.0469  0.0504  139 TYR A O   
1084 C CB  . TYR A 139 ? 0.5966 0.6160 0.5769 -0.0320 0.0504  0.0327  139 TYR A CB  
1085 C CG  . TYR A 139 ? 0.6188 0.6542 0.6129 -0.0474 0.0567  0.0301  139 TYR A CG  
1086 C CD1 . TYR A 139 ? 0.5909 0.6520 0.5903 -0.0488 0.0654  0.0337  139 TYR A CD1 
1087 C CD2 . TYR A 139 ? 0.6072 0.6341 0.6092 -0.0612 0.0537  0.0238  139 TYR A CD2 
1088 C CE1 . TYR A 139 ? 0.6022 0.6855 0.6207 -0.0642 0.0726  0.0331  139 TYR A CE1 
1089 C CE2 . TYR A 139 ? 0.6071 0.6532 0.6273 -0.0782 0.0573  0.0223  139 TYR A CE2 
1090 C CZ  . TYR A 139 ? 0.6150 0.6921 0.6467 -0.0800 0.0675  0.0278  139 TYR A CZ  
1091 O OH  . TYR A 139 ? 0.6091 0.7123 0.6649 -0.0983 0.0726  0.0281  139 TYR A OH  
1092 N N   . ASN A 140 ? 0.6874 0.7010 0.6435 -0.0049 0.0420  0.0486  140 ASN A N   
1093 C CA  . ASN A 140 ? 0.6478 0.6637 0.6031 0.0048  0.0298  0.0486  140 ASN A CA  
1094 C C   . ASN A 140 ? 0.6028 0.6264 0.5680 0.0046  0.0215  0.0365  140 ASN A C   
1095 O O   . ASN A 140 ? 0.5827 0.6201 0.5503 0.0049  0.0190  0.0271  140 ASN A O   
1096 C CB  . ASN A 140 ? 0.5965 0.6210 0.5381 0.0105  0.0252  0.0512  140 ASN A CB  
1097 C CG  . ASN A 140 ? 0.6117 0.6382 0.5525 0.0169  0.0091  0.0497  140 ASN A CG  
1098 O OD1 . ASN A 140 ? 0.6617 0.6911 0.6099 0.0172  0.0010  0.0406  140 ASN A OD1 
1099 N ND2 . ASN A 140 ? 0.6572 0.6814 0.5888 0.0211  0.0030  0.0598  140 ASN A ND2 
1100 N N   . THR A 141 ? 0.5446 0.5596 0.5149 0.0053  0.0181  0.0373  141 THR A N   
1101 C CA  . THR A 141 ? 0.4878 0.5043 0.4632 0.0028  0.0130  0.0281  141 THR A CA  
1102 C C   . THR A 141 ? 0.4820 0.4973 0.4590 0.0069  0.0030  0.0301  141 THR A C   
1103 O O   . THR A 141 ? 0.4982 0.5086 0.4772 0.0088  0.0056  0.0389  141 THR A O   
1104 C CB  . THR A 141 ? 0.5244 0.5275 0.4981 -0.0033 0.0206  0.0266  141 THR A CB  
1105 O OG1 . THR A 141 ? 0.5004 0.5004 0.4734 -0.0103 0.0296  0.0273  141 THR A OG1 
1106 C CG2 . THR A 141 ? 0.5023 0.5086 0.4774 -0.0067 0.0130  0.0167  141 THR A CG2 
1107 N N   . ASP A 142 ? 0.5004 0.5204 0.4780 0.0084  -0.0077 0.0230  142 ASP A N   
1108 C CA  . ASP A 142 ? 0.5643 0.5784 0.5425 0.0086  -0.0171 0.0255  142 ASP A CA  
1109 C C   . ASP A 142 ? 0.5502 0.5583 0.5254 0.0057  -0.0153 0.0233  142 ASP A C   
1110 O O   . ASP A 142 ? 0.5546 0.5660 0.5292 0.0045  -0.0164 0.0149  142 ASP A O   
1111 C CB  . ASP A 142 ? 0.5339 0.5472 0.5098 0.0124  -0.0308 0.0191  142 ASP A CB  
1112 C CG  . ASP A 142 ? 0.5610 0.5764 0.5322 0.0155  -0.0345 0.0189  142 ASP A CG  
1113 O OD1 . ASP A 142 ? 0.5220 0.5394 0.4948 0.0134  -0.0317 0.0284  142 ASP A OD1 
1114 O OD2 . ASP A 142 ? 0.5727 0.5877 0.5371 0.0215  -0.0403 0.0090  142 ASP A OD2 
1115 N N   . VAL A 143 ? 0.6003 0.6020 0.5733 0.0043  -0.0130 0.0312  143 VAL A N   
1116 C CA  . VAL A 143 ? 0.6458 0.6391 0.6082 0.0022  -0.0124 0.0297  143 VAL A CA  
1117 C C   . VAL A 143 ? 0.6270 0.6163 0.5876 0.0009  -0.0206 0.0374  143 VAL A C   
1118 O O   . VAL A 143 ? 0.6414 0.6349 0.6116 -0.0006 -0.0207 0.0470  143 VAL A O   
1119 C CB  . VAL A 143 ? 0.6012 0.5865 0.5551 0.0021  0.0025  0.0317  143 VAL A CB  
1120 C CG1 . VAL A 143 ? 0.6100 0.5914 0.5628 0.0004  0.0089  0.0242  143 VAL A CG1 
1121 C CG2 . VAL A 143 ? 0.5829 0.5724 0.5448 0.0057  0.0121  0.0441  143 VAL A CG2 
1122 N N   . VAL A 144 ? 0.5426 0.5238 0.4916 0.0004  -0.0289 0.0344  144 VAL A N   
1123 C CA  . VAL A 144 ? 0.5831 0.5546 0.5256 -0.0022 -0.0367 0.0435  144 VAL A CA  
1124 C C   . VAL A 144 ? 0.5868 0.5502 0.5090 -0.0041 -0.0300 0.0471  144 VAL A C   
1125 O O   . VAL A 144 ? 0.6057 0.5659 0.5152 -0.0026 -0.0317 0.0379  144 VAL A O   
1126 C CB  . VAL A 144 ? 0.5643 0.5275 0.5055 0.0013  -0.0549 0.0385  144 VAL A CB  
1127 C CG1 . VAL A 144 ? 0.5388 0.4855 0.4733 -0.0034 -0.0637 0.0507  144 VAL A CG1 
1128 C CG2 . VAL A 144 ? 0.5425 0.5131 0.4968 0.0059  -0.0591 0.0302  144 VAL A CG2 
1129 N N   . PHE A 145 ? 0.5965 0.5584 0.5153 -0.0080 -0.0222 0.0607  145 PHE A N   
1130 C CA  . PHE A 145 ? 0.6184 0.5710 0.5119 -0.0093 -0.0148 0.0661  145 PHE A CA  
1131 C C   . PHE A 145 ? 0.6192 0.5614 0.5056 -0.0150 -0.0246 0.0796  145 PHE A C   
1132 O O   . PHE A 145 ? 0.6191 0.5654 0.5242 -0.0209 -0.0271 0.0899  145 PHE A O   
1133 C CB  . PHE A 145 ? 0.6282 0.5895 0.5219 -0.0076 0.0081  0.0719  145 PHE A CB  
1134 C CG  . PHE A 145 ? 0.6281 0.5921 0.5267 -0.0015 0.0173  0.0600  145 PHE A CG  
1135 C CD1 . PHE A 145 ? 0.6279 0.5774 0.5011 0.0010  0.0215  0.0478  145 PHE A CD1 
1136 C CD2 . PHE A 145 ? 0.5837 0.5613 0.5096 0.0006  0.0198  0.0615  145 PHE A CD2 
1137 C CE1 . PHE A 145 ? 0.6411 0.5866 0.5175 0.0045  0.0291  0.0378  145 PHE A CE1 
1138 C CE2 . PHE A 145 ? 0.5617 0.5371 0.4897 0.0059  0.0280  0.0530  145 PHE A CE2 
1139 C CZ  . PHE A 145 ? 0.6098 0.5678 0.5141 0.0072  0.0330  0.0414  145 PHE A CZ  
1140 N N   . ASP A 146 ? 0.6085 0.5349 0.4667 -0.0144 -0.0322 0.0802  146 ASP A N   
1141 C CA  . ASP A 146 ? 0.6217 0.5319 0.4686 -0.0197 -0.0425 0.0949  146 ASP A CA  
1142 C C   . ASP A 146 ? 0.6570 0.5707 0.4952 -0.0275 -0.0237 0.1132  146 ASP A C   
1143 O O   . ASP A 146 ? 0.6522 0.5827 0.4955 -0.0259 -0.0029 0.1129  146 ASP A O   
1144 C CB  . ASP A 146 ? 0.6446 0.5373 0.4647 -0.0143 -0.0598 0.0905  146 ASP A CB  
1145 C CG  . ASP A 146 ? 0.6590 0.5474 0.4430 -0.0132 -0.0510 0.0893  146 ASP A CG  
1146 O OD1 . ASP A 146 ? 0.6618 0.5565 0.4370 -0.0158 -0.0288 0.0935  146 ASP A OD1 
1147 O OD2 . ASP A 146 ? 0.6587 0.5370 0.4220 -0.0087 -0.0676 0.0835  146 ASP A OD2 
1148 N N   . SER A 147 ? 0.6761 0.5742 0.5026 -0.0356 -0.0301 0.1305  147 SER A N   
1149 C CA  . SER A 147 ? 0.6922 0.5977 0.5143 -0.0455 -0.0110 0.1512  147 SER A CA  
1150 C C   . SER A 147 ? 0.7618 0.6687 0.5479 -0.0399 0.0085  0.1513  147 SER A C   
1151 O O   . SER A 147 ? 0.7627 0.6826 0.5460 -0.0449 0.0309  0.1668  147 SER A O   
1152 C CB  . SER A 147 ? 0.7394 0.6228 0.5540 -0.0580 -0.0232 0.1716  147 SER A CB  
1153 O OG  . SER A 147 ? 0.7259 0.5791 0.5197 -0.0519 -0.0480 0.1658  147 SER A OG  
1154 N N   . GLN A 148 ? 0.8449 0.7389 0.6022 -0.0302 0.0005  0.1347  148 GLN A N   
1155 C CA  . GLN A 148 ? 0.8708 0.7631 0.5911 -0.0243 0.0187  0.1298  148 GLN A CA  
1156 C C   . GLN A 148 ? 0.8883 0.7952 0.6238 -0.0161 0.0334  0.1125  148 GLN A C   
1157 O O   . GLN A 148 ? 0.8868 0.7895 0.5926 -0.0097 0.0510  0.1063  148 GLN A O   
1158 C CB  . GLN A 148 ? 0.8674 0.7357 0.5428 -0.0201 0.0007  0.1212  148 GLN A CB  
1159 C CG  . GLN A 148 ? 0.8911 0.7391 0.5492 -0.0247 -0.0199 0.1367  148 GLN A CG  
1160 C CD  . GLN A 148 ? 0.9901 0.8354 0.6412 -0.0351 -0.0053 0.1639  148 GLN A CD  
1161 O OE1 . GLN A 148 ? 1.0758 0.9189 0.6903 -0.0362 0.0143  0.1739  148 GLN A OE1 
1162 N NE2 . GLN A 148 ? 1.0415 0.8860 0.7263 -0.0437 -0.0146 0.1761  148 GLN A NE2 
1163 N N   . GLY A 149 ? 0.6635 0.5839 0.4406 -0.0154 0.0269  0.1048  149 GLY A N   
1164 C CA  . GLY A 149 ? 0.6342 0.5632 0.4237 -0.0077 0.0381  0.0898  149 GLY A CA  
1165 C C   . GLY A 149 ? 0.6409 0.5570 0.4185 -0.0046 0.0233  0.0691  149 GLY A C   
1166 O O   . GLY A 149 ? 0.6652 0.5783 0.4388 0.0005  0.0335  0.0562  149 GLY A O   
1167 N N   . LYS A 150 ? 0.6933 0.6007 0.4640 -0.0075 -0.0002 0.0662  150 LYS A N   
1168 C CA  . LYS A 150 ? 0.6997 0.6031 0.4676 -0.0063 -0.0155 0.0481  150 LYS A CA  
1169 C C   . LYS A 150 ? 0.6991 0.6181 0.5081 -0.0059 -0.0206 0.0412  150 LYS A C   
1170 O O   . LYS A 150 ? 0.6794 0.6076 0.5141 -0.0063 -0.0235 0.0495  150 LYS A O   
1171 C CB  . LYS A 150 ? 0.7150 0.6087 0.4636 -0.0070 -0.0394 0.0487  150 LYS A CB  
1172 C CG  . LYS A 150 ? 0.7182 0.6130 0.4633 -0.0073 -0.0551 0.0311  150 LYS A CG  
1173 C CD  . LYS A 150 ? 0.8119 0.6982 0.5322 -0.0062 -0.0782 0.0329  150 LYS A CD  
1174 C CE  . LYS A 150 ? 0.8762 0.7728 0.6043 -0.0080 -0.0976 0.0161  150 LYS A CE  
1175 N NZ  . LYS A 150 ? 0.8027 0.7156 0.5581 -0.0024 -0.1218 0.0165  150 LYS A NZ  
1176 N N   . LEU A 151 ? 0.6797 0.5999 0.4921 -0.0062 -0.0216 0.0260  151 LEU A N   
1177 C CA  . LEU A 151 ? 0.6597 0.5949 0.5059 -0.0064 -0.0260 0.0198  151 LEU A CA  
1178 C C   . LEU A 151 ? 0.6700 0.6131 0.5257 -0.0055 -0.0481 0.0167  151 LEU A C   
1179 O O   . LEU A 151 ? 0.6757 0.6176 0.5193 -0.0073 -0.0606 0.0088  151 LEU A O   
1180 C CB  . LEU A 151 ? 0.6470 0.5791 0.4935 -0.0093 -0.0186 0.0073  151 LEU A CB  
1181 C CG  . LEU A 151 ? 0.6548 0.6034 0.5334 -0.0110 -0.0218 0.0024  151 LEU A CG  
1182 C CD1 . LEU A 151 ? 0.5749 0.5336 0.4751 -0.0063 -0.0146 0.0123  151 LEU A CD1 
1183 C CD2 . LEU A 151 ? 0.6444 0.5846 0.5209 -0.0166 -0.0137 -0.0071 151 LEU A CD2 
1184 N N   . VAL A 152 ? 0.5972 0.5470 0.4729 -0.0018 -0.0542 0.0228  152 VAL A N   
1185 C CA  . VAL A 152 ? 0.5933 0.5478 0.4774 0.0035  -0.0740 0.0201  152 VAL A CA  
1186 C C   . VAL A 152 ? 0.6138 0.5869 0.5281 0.0079  -0.0760 0.0119  152 VAL A C   
1187 O O   . VAL A 152 ? 0.6412 0.6229 0.5661 0.0154  -0.0903 0.0072  152 VAL A O   
1188 C CB  . VAL A 152 ? 0.6005 0.5388 0.4744 0.0064  -0.0831 0.0330  152 VAL A CB  
1189 C CG1 . VAL A 152 ? 0.6012 0.5225 0.4403 0.0020  -0.0804 0.0428  152 VAL A CG1 
1190 C CG2 . VAL A 152 ? 0.5762 0.5124 0.4650 0.0044  -0.0757 0.0407  152 VAL A CG2 
1191 N N   . ALA A 153 ? 0.6390 0.6193 0.5661 0.0052  -0.0619 0.0105  153 ALA A N   
1192 C CA  . ALA A 153 ? 0.6432 0.6411 0.5931 0.0093  -0.0620 0.0032  153 ALA A CA  
1193 C C   . ALA A 153 ? 0.6357 0.6386 0.5922 0.0041  -0.0456 0.0030  153 ALA A C   
1194 O O   . ALA A 153 ? 0.6474 0.6405 0.5976 0.0019  -0.0361 0.0107  153 ALA A O   
1195 C CB  . ALA A 153 ? 0.5580 0.5514 0.5138 0.0176  -0.0702 0.0053  153 ALA A CB  
1196 N N   . ARG A 154 ? 0.5871 0.6067 0.5579 0.0027  -0.0423 -0.0043 154 ARG A N   
1197 C CA  . ARG A 154 ? 0.5923 0.6147 0.5684 -0.0019 -0.0279 -0.0031 154 ARG A CA  
1198 C C   . ARG A 154 ? 0.5697 0.6126 0.5620 0.0021  -0.0268 -0.0073 154 ARG A C   
1199 O O   . ARG A 154 ? 0.5643 0.6263 0.5698 0.0028  -0.0318 -0.0141 154 ARG A O   
1200 C CB  . ARG A 154 ? 0.6045 0.6209 0.5753 -0.0122 -0.0214 -0.0065 154 ARG A CB  
1201 C CG  . ARG A 154 ? 0.6128 0.6248 0.5862 -0.0170 -0.0069 -0.0035 154 ARG A CG  
1202 C CD  . ARG A 154 ? 0.6288 0.6339 0.6000 -0.0296 -0.0041 -0.0094 154 ARG A CD  
1203 N NE  . ARG A 154 ? 0.6187 0.6502 0.6104 -0.0362 -0.0101 -0.0151 154 ARG A NE  
1204 C CZ  . ARG A 154 ? 0.6068 0.6411 0.6032 -0.0499 -0.0144 -0.0215 154 ARG A CZ  
1205 N NH1 . ARG A 154 ? 0.5850 0.5903 0.5609 -0.0584 -0.0141 -0.0252 154 ARG A NH1 
1206 N NH2 . ARG A 154 ? 0.6140 0.6816 0.6366 -0.0551 -0.0196 -0.0248 154 ARG A NH2 
1207 N N   . TYR A 155 ? 0.5553 0.5970 0.5465 0.0057  -0.0206 -0.0032 155 TYR A N   
1208 C CA  . TYR A 155 ? 0.5491 0.6079 0.5481 0.0114  -0.0177 -0.0074 155 TYR A CA  
1209 C C   . TYR A 155 ? 0.5693 0.6283 0.5647 0.0069  -0.0042 -0.0014 155 TYR A C   
1210 O O   . TYR A 155 ? 0.5257 0.5708 0.5114 0.0076  -0.0030 0.0061  155 TYR A O   
1211 C CB  . TYR A 155 ? 0.5540 0.6068 0.5471 0.0230  -0.0279 -0.0102 155 TYR A CB  
1212 C CG  . TYR A 155 ? 0.5579 0.6227 0.5496 0.0305  -0.0222 -0.0151 155 TYR A CG  
1213 C CD1 . TYR A 155 ? 0.5507 0.6403 0.5554 0.0366  -0.0175 -0.0230 155 TYR A CD1 
1214 C CD2 . TYR A 155 ? 0.5924 0.6468 0.5697 0.0315  -0.0207 -0.0111 155 TYR A CD2 
1215 C CE1 . TYR A 155 ? 0.5928 0.6948 0.5926 0.0448  -0.0085 -0.0274 155 TYR A CE1 
1216 C CE2 . TYR A 155 ? 0.5865 0.6492 0.5547 0.0388  -0.0151 -0.0160 155 TYR A CE2 
1217 C CZ  . TYR A 155 ? 0.6092 0.6949 0.5869 0.0459  -0.0073 -0.0243 155 TYR A CZ  
1218 O OH  . TYR A 155 ? 0.6203 0.7151 0.5851 0.0545  0.0016  -0.0290 155 TYR A OH  
1219 N N   . HIS A 156 ? 0.5612 0.6381 0.5660 0.0025  0.0053  -0.0033 156 HIS A N   
1220 C CA  . HIS A 156 ? 0.5819 0.6584 0.5808 -0.0020 0.0186  0.0042  156 HIS A CA  
1221 C C   . HIS A 156 ? 0.5729 0.6608 0.5641 0.0083  0.0210  0.0022  156 HIS A C   
1222 O O   . HIS A 156 ? 0.5352 0.6457 0.5360 0.0140  0.0230  -0.0057 156 HIS A O   
1223 C CB  . HIS A 156 ? 0.5509 0.6386 0.5624 -0.0157 0.0288  0.0052  156 HIS A CB  
1224 C CG  . HIS A 156 ? 0.5833 0.6540 0.5959 -0.0266 0.0257  0.0047  156 HIS A CG  
1225 N ND1 . HIS A 156 ? 0.5791 0.6629 0.6071 -0.0375 0.0220  -0.0017 156 HIS A ND1 
1226 C CD2 . HIS A 156 ? 0.5534 0.5950 0.5518 -0.0275 0.0255  0.0088  156 HIS A CD2 
1227 C CE1 . HIS A 156 ? 0.5805 0.6390 0.5984 -0.0454 0.0189  -0.0027 156 HIS A CE1 
1228 N NE2 . HIS A 156 ? 0.5781 0.6106 0.5777 -0.0383 0.0227  0.0034  156 HIS A NE2 
1229 N N   . LYS A 157 ? 0.5928 0.6664 0.5661 0.0116  0.0210  0.0092  157 LYS A N   
1230 C CA  . LYS A 157 ? 0.5668 0.6442 0.5237 0.0216  0.0202  0.0060  157 LYS A CA  
1231 C C   . LYS A 157 ? 0.5881 0.6886 0.5461 0.0218  0.0358  0.0043  157 LYS A C   
1232 O O   . LYS A 157 ? 0.5720 0.6763 0.5315 0.0114  0.0490  0.0142  157 LYS A O   
1233 C CB  . LYS A 157 ? 0.5825 0.6432 0.5206 0.0217  0.0170  0.0165  157 LYS A CB  
1234 C CG  . LYS A 157 ? 0.6244 0.6833 0.5380 0.0312  0.0117  0.0121  157 LYS A CG  
1235 C CD  . LYS A 157 ? 0.6262 0.6720 0.5235 0.0301  0.0051  0.0241  157 LYS A CD  
1236 C CE  . LYS A 157 ? 0.6898 0.7299 0.5580 0.0382  -0.0050 0.0177  157 LYS A CE  
1237 N NZ  . LYS A 157 ? 0.6724 0.7035 0.5250 0.0368  -0.0148 0.0304  157 LYS A NZ  
1238 N N   . GLN A 158 ? 0.5841 0.6991 0.5414 0.0341  0.0353  -0.0076 158 GLN A N   
1239 C CA  . GLN A 158 ? 0.5664 0.7117 0.5303 0.0363  0.0529  -0.0099 158 GLN A CA  
1240 C C   . GLN A 158 ? 0.6059 0.7486 0.5385 0.0401  0.0641  -0.0048 158 GLN A C   
1241 O O   . GLN A 158 ? 0.5571 0.7172 0.4906 0.0323  0.0828  0.0041  158 GLN A O   
1242 C CB  . GLN A 158 ? 0.5775 0.7411 0.5544 0.0523  0.0493  -0.0252 158 GLN A CB  
1243 C CG  . GLN A 158 ? 0.6081 0.8096 0.5943 0.0585  0.0696  -0.0282 158 GLN A CG  
1244 C CD  . GLN A 158 ? 0.6450 0.8774 0.6659 0.0404  0.0816  -0.0191 158 GLN A CD  
1245 O OE1 . GLN A 158 ? 0.5958 0.8222 0.6360 0.0279  0.0708  -0.0165 158 GLN A OE1 
1246 N NE2 . GLN A 158 ? 0.5879 0.8523 0.6148 0.0376  0.1038  -0.0142 158 GLN A NE2 
1247 N N   . ASN A 159 ? 0.6734 0.7937 0.5767 0.0505  0.0520  -0.0098 159 ASN A N   
1248 C CA  . ASN A 159 ? 0.6617 0.7771 0.5275 0.0574  0.0584  -0.0087 159 ASN A CA  
1249 C C   . ASN A 159 ? 0.6871 0.7786 0.5344 0.0487  0.0496  0.0062  159 ASN A C   
1250 O O   . ASN A 159 ? 0.7037 0.7741 0.5402 0.0513  0.0298  0.0039  159 ASN A O   
1251 C CB  . ASN A 159 ? 0.6723 0.7770 0.5151 0.0758  0.0480  -0.0272 159 ASN A CB  
1252 C CG  . ASN A 159 ? 0.6852 0.8145 0.5475 0.0894  0.0575  -0.0417 159 ASN A CG  
1253 O OD1 . ASN A 159 ? 0.7482 0.8990 0.5998 0.0995  0.0763  -0.0464 159 ASN A OD1 
1254 N ND2 . ASN A 159 ? 0.6756 0.8031 0.5657 0.0913  0.0448  -0.0480 159 ASN A ND2 
1255 N N   . LEU A 160 ? 0.7262 0.8219 0.5720 0.0380  0.0640  0.0228  160 LEU A N   
1256 C CA  . LEU A 160 ? 0.6996 0.7737 0.5303 0.0325  0.0566  0.0390  160 LEU A CA  
1257 C C   . LEU A 160 ? 0.7605 0.8249 0.5471 0.0412  0.0511  0.0405  160 LEU A C   
1258 O O   . LEU A 160 ? 0.7761 0.8512 0.5381 0.0467  0.0651  0.0371  160 LEU A O   
1259 C CB  . LEU A 160 ? 0.6538 0.7281 0.4948 0.0191  0.0728  0.0566  160 LEU A CB  
1260 C CG  . LEU A 160 ? 0.6995 0.7714 0.5771 0.0091  0.0715  0.0564  160 LEU A CG  
1261 C CD1 . LEU A 160 ? 0.6548 0.7168 0.5378 -0.0052 0.0850  0.0728  160 LEU A CD1 
1262 C CD2 . LEU A 160 ? 0.6436 0.6988 0.5294 0.0134  0.0519  0.0537  160 LEU A CD2 
1263 N N   . PHE A 161 ? 0.8277 0.8738 0.6042 0.0426  0.0301  0.0449  161 PHE A N   
1264 C CA  . PHE A 161 ? 0.8229 0.8576 0.5570 0.0486  0.0194  0.0484  161 PHE A CA  
1265 C C   . PHE A 161 ? 0.8826 0.9127 0.6006 0.0440  0.0294  0.0717  161 PHE A C   
1266 O O   . PHE A 161 ? 0.8212 0.8504 0.5647 0.0359  0.0394  0.0849  161 PHE A O   
1267 C CB  . PHE A 161 ? 0.8532 0.8749 0.5897 0.0497  -0.0098 0.0449  161 PHE A CB  
1268 C CG  . PHE A 161 ? 0.8794 0.8894 0.5705 0.0556  -0.0265 0.0406  161 PHE A CG  
1269 C CD1 . PHE A 161 ? 0.9421 0.9464 0.6023 0.0643  -0.0272 0.0197  161 PHE A CD1 
1270 C CD2 . PHE A 161 ? 0.9077 0.9113 0.5843 0.0541  -0.0422 0.0570  161 PHE A CD2 
1271 C CE1 . PHE A 161 ? 0.9399 0.9284 0.5496 0.0697  -0.0436 0.0135  161 PHE A CE1 
1272 C CE2 . PHE A 161 ? 0.9572 0.9495 0.5873 0.0586  -0.0605 0.0527  161 PHE A CE2 
1273 C CZ  . PHE A 161 ? 0.9445 0.9274 0.5390 0.0654  -0.0614 0.0301  161 PHE A CZ  
1274 N N   . MET A 162 ? 0.8617 0.8853 0.5327 0.0496  0.0270  0.0764  162 MET A N   
1275 C CA  . MET A 162 ? 0.8683 0.8826 0.5177 0.0467  0.0328  0.1010  162 MET A CA  
1276 C C   . MET A 162 ? 0.9379 0.9411 0.6117 0.0450  0.0151  0.1158  162 MET A C   
1277 O O   . MET A 162 ? 0.9220 0.9258 0.6138 0.0474  -0.0068 0.1080  162 MET A O   
1278 C CB  . MET A 162 ? 0.9233 0.9304 0.5120 0.0543  0.0281  0.1030  162 MET A CB  
1279 C CG  . MET A 162 ? 1.0059 1.0022 0.5729 0.0608  -0.0047 0.0949  162 MET A CG  
1280 S SD  . MET A 162 ? 1.1432 1.1261 0.6295 0.0688  -0.0129 0.1002  162 MET A SD  
1281 C CE  . MET A 162 ? 1.0235 1.0076 0.4889 0.0648  0.0211  0.1274  162 MET A CE  
1282 N N   . GLY A 163 ? 0.8357 0.8287 0.5128 0.0409  0.0263  0.1376  163 GLY A N   
1283 C CA  . GLY A 163 ? 0.7972 0.7799 0.5008 0.0428  0.0140  0.1512  163 GLY A CA  
1284 C C   . GLY A 163 ? 0.8283 0.8133 0.5797 0.0376  0.0206  0.1438  163 GLY A C   
1285 O O   . GLY A 163 ? 0.8044 0.7828 0.5798 0.0415  0.0120  0.1519  163 GLY A O   
1286 N N   . GLU A 164 ? 0.8944 0.8899 0.6595 0.0302  0.0353  0.1286  164 GLU A N   
1287 C CA  . GLU A 164 ? 0.8774 0.8733 0.6817 0.0238  0.0419  0.1217  164 GLU A CA  
1288 C C   . GLU A 164 ? 0.8659 0.8522 0.6747 0.0124  0.0633  0.1307  164 GLU A C   
1289 O O   . GLU A 164 ? 0.8852 0.8810 0.7160 0.0033  0.0732  0.1196  164 GLU A O   
1290 C CB  . GLU A 164 ? 0.8331 0.8469 0.6539 0.0233  0.0386  0.0991  164 GLU A CB  
1291 C CG  . GLU A 164 ? 0.8321 0.8489 0.6553 0.0306  0.0158  0.0904  164 GLU A CG  
1292 C CD  . GLU A 164 ? 0.8103 0.8342 0.6626 0.0286  0.0114  0.0748  164 GLU A CD  
1293 O OE1 . GLU A 164 ? 0.7991 0.8318 0.6486 0.0297  0.0130  0.0593  164 GLU A OE1 
1294 O OE2 . GLU A 164 ? 0.7805 0.8006 0.6568 0.0275  0.0069  0.0788  164 GLU A OE2 
1295 N N   . ASN A 165 ? 0.7868 0.7530 0.5749 0.0114  0.0694  0.1518  165 ASN A N   
1296 C CA  . ASN A 165 ? 0.7942 0.7462 0.5843 -0.0028 0.0891  0.1624  165 ASN A CA  
1297 C C   . ASN A 165 ? 0.8193 0.7516 0.6387 -0.0081 0.0901  0.1600  165 ASN A C   
1298 O O   . ASN A 165 ? 0.8070 0.7259 0.6324 -0.0234 0.1041  0.1644  165 ASN A O   
1299 C CB  . ASN A 165 ? 0.8232 0.7518 0.5791 -0.0019 0.0938  0.1879  165 ASN A CB  
1300 C CG  . ASN A 165 ? 0.9280 0.8292 0.6833 0.0112  0.0794  0.2022  165 ASN A CG  
1301 O OD1 . ASN A 165 ? 0.9246 0.8362 0.6905 0.0245  0.0612  0.1955  165 ASN A OD1 
1302 N ND2 . ASN A 165 ? 0.9223 0.7887 0.6677 0.0076  0.0877  0.2225  165 ASN A ND2 
1303 N N   . GLN A 166 ? 0.8684 0.7983 0.7047 0.0030  0.0763  0.1529  166 GLN A N   
1304 C CA  . GLN A 166 ? 0.8698 0.7813 0.7286 -0.0004 0.0789  0.1475  166 GLN A CA  
1305 C C   . GLN A 166 ? 0.8224 0.7516 0.7023 -0.0124 0.0828  0.1277  166 GLN A C   
1306 O O   . GLN A 166 ? 0.8657 0.7773 0.7584 -0.0188 0.0860  0.1221  166 GLN A O   
1307 C CB  . GLN A 166 ? 0.8412 0.7489 0.7117 0.0166  0.0659  0.1478  166 GLN A CB  
1308 C CG  . GLN A 166 ? 0.8119 0.7509 0.6955 0.0224  0.0526  0.1339  166 GLN A CG  
1309 C CD  . GLN A 166 ? 0.8458 0.8001 0.7128 0.0306  0.0394  0.1406  166 GLN A CD  
1310 O OE1 . GLN A 166 ? 0.8527 0.8055 0.6938 0.0279  0.0433  0.1482  166 GLN A OE1 
1311 N NE2 . GLN A 166 ? 0.8101 0.7789 0.6904 0.0394  0.0236  0.1382  166 GLN A NE2 
1312 N N   . PHE A 167 ? 0.7018 0.6629 0.5836 -0.0142 0.0819  0.1167  167 PHE A N   
1313 C CA  . PHE A 167 ? 0.6915 0.6729 0.5955 -0.0213 0.0818  0.0984  167 PHE A CA  
1314 C C   . PHE A 167 ? 0.6961 0.6980 0.6049 -0.0352 0.0954  0.0967  167 PHE A C   
1315 O O   . PHE A 167 ? 0.6986 0.7068 0.5899 -0.0369 0.1053  0.1072  167 PHE A O   
1316 C CB  . PHE A 167 ? 0.6642 0.6665 0.5726 -0.0095 0.0683  0.0853  167 PHE A CB  
1317 C CG  . PHE A 167 ? 0.6608 0.6517 0.5746 0.0005  0.0558  0.0859  167 PHE A CG  
1318 C CD1 . PHE A 167 ? 0.6568 0.6351 0.5855 -0.0018 0.0561  0.0814  167 PHE A CD1 
1319 C CD2 . PHE A 167 ? 0.6958 0.6901 0.5994 0.0116  0.0439  0.0911  167 PHE A CD2 
1320 C CE1 . PHE A 167 ? 0.6414 0.6141 0.5767 0.0080  0.0483  0.0831  167 PHE A CE1 
1321 C CE2 . PHE A 167 ? 0.6760 0.6671 0.5914 0.0194  0.0334  0.0935  167 PHE A CE2 
1322 C CZ  . PHE A 167 ? 0.6744 0.6562 0.6066 0.0182  0.0375  0.0900  167 PHE A CZ  
1323 N N   . ASN A 168 ? 0.6159 0.6308 0.5489 -0.0452 0.0959  0.0843  168 ASN A N   
1324 C CA  . ASN A 168 ? 0.6572 0.7038 0.6050 -0.0570 0.1071  0.0809  168 ASN A CA  
1325 C C   . ASN A 168 ? 0.6674 0.7484 0.6280 -0.0455 0.1003  0.0641  168 ASN A C   
1326 O O   . ASN A 168 ? 0.6121 0.6872 0.5709 -0.0327 0.0859  0.0549  168 ASN A O   
1327 C CB  . ASN A 168 ? 0.6514 0.6919 0.6205 -0.0785 0.1107  0.0800  168 ASN A CB  
1328 C CG  . ASN A 168 ? 0.6817 0.6810 0.6359 -0.0905 0.1178  0.0963  168 ASN A CG  
1329 O OD1 . ASN A 168 ? 0.7248 0.6873 0.6730 -0.0888 0.1106  0.0952  168 ASN A OD1 
1330 N ND2 . ASN A 168 ? 0.6593 0.6622 0.6054 -0.1017 0.1330  0.1120  168 ASN A ND2 
1331 N N   . VAL A 169 ? 0.7968 0.9135 0.7698 -0.0492 0.1119  0.0614  169 VAL A N   
1332 C CA  . VAL A 169 ? 0.7542 0.9038 0.7411 -0.0361 0.1075  0.0454  169 VAL A CA  
1333 C C   . VAL A 169 ? 0.7383 0.9113 0.7630 -0.0470 0.1042  0.0370  169 VAL A C   
1334 O O   . VAL A 169 ? 0.7607 0.9462 0.8038 -0.0667 0.1145  0.0442  169 VAL A O   
1335 C CB  . VAL A 169 ? 0.7417 0.9192 0.7169 -0.0278 0.1235  0.0467  169 VAL A CB  
1336 C CG1 . VAL A 169 ? 0.7015 0.9051 0.6862 -0.0088 0.1181  0.0285  169 VAL A CG1 
1337 C CG2 . VAL A 169 ? 0.7070 0.8588 0.6400 -0.0201 0.1250  0.0567  169 VAL A CG2 
1338 N N   . PRO A 170 ? 0.6702 0.8496 0.7072 -0.0364 0.0887  0.0229  170 PRO A N   
1339 C CA  . PRO A 170 ? 0.6283 0.8333 0.7002 -0.0456 0.0828  0.0154  170 PRO A CA  
1340 C C   . PRO A 170 ? 0.6261 0.8817 0.7263 -0.0492 0.0976  0.0160  170 PRO A C   
1341 O O   . PRO A 170 ? 0.6715 0.9472 0.7643 -0.0343 0.1093  0.0149  170 PRO A O   
1342 C CB  . PRO A 170 ? 0.6103 0.8121 0.6824 -0.0277 0.0643  0.0024  170 PRO A CB  
1343 C CG  . PRO A 170 ? 0.6228 0.7860 0.6624 -0.0183 0.0584  0.0051  170 PRO A CG  
1344 C CD  . PRO A 170 ? 0.6206 0.7794 0.6395 -0.0184 0.0734  0.0153  170 PRO A CD  
1345 N N   . LYS A 171 ? 0.8259 1.1037 0.9593 -0.0694 0.0970  0.0173  171 LYS A N   
1346 C CA  . LYS A 171 ? 0.7530 1.0884 0.9238 -0.0751 0.1109  0.0191  171 LYS A CA  
1347 C C   . LYS A 171 ? 0.7714 1.1431 0.9553 -0.0471 0.1094  0.0068  171 LYS A C   
1348 O O   . LYS A 171 ? 0.8458 1.2570 1.0406 -0.0382 0.1287  0.0084  171 LYS A O   
1349 C CB  . LYS A 171 ? 0.8692 1.2236 1.0781 -0.1011 0.1020  0.0195  171 LYS A CB  
1350 C CG  . LYS A 171 ? 0.8753 1.1750 1.0637 -0.1202 0.0892  0.0214  171 LYS A CG  
1351 C CD  . LYS A 171 ? 0.9387 1.2539 1.1605 -0.1483 0.0786  0.0200  171 LYS A CD  
1352 C CE  . LYS A 171 ? 0.8855 1.2466 1.1429 -0.1390 0.0615  0.0078  171 LYS A CE  
1353 N NZ  . LYS A 171 ? 0.8468 1.1783 1.0778 -0.1151 0.0432  -0.0034 171 LYS A NZ  
1354 N N   . GLU A 172 ? 0.7839 1.1409 0.9651 -0.0319 0.0877  -0.0051 172 GLU A N   
1355 C CA  . GLU A 172 ? 0.7785 1.1562 0.9661 -0.0029 0.0828  -0.0172 172 GLU A CA  
1356 C C   . GLU A 172 ? 0.7843 1.1117 0.9331 0.0138  0.0672  -0.0238 172 GLU A C   
1357 O O   . GLU A 172 ? 0.8007 1.0882 0.9305 0.0027  0.0562  -0.0202 172 GLU A O   
1358 C CB  . GLU A 172 ? 0.7639 1.1819 0.9964 -0.0010 0.0688  -0.0238 172 GLU A CB  
1359 C CG  . GLU A 172 ? 0.8176 1.3018 1.0906 0.0093  0.0853  -0.0249 172 GLU A CG  
1360 C CD  . GLU A 172 ? 0.8482 1.3668 1.1573 0.0278  0.0681  -0.0346 172 GLU A CD  
1361 O OE1 . GLU A 172 ? 0.8655 1.3773 1.1872 0.0160  0.0450  -0.0353 172 GLU A OE1 
1362 O OE2 . GLU A 172 ? 0.8903 1.4407 1.2125 0.0558  0.0774  -0.0416 172 GLU A OE2 
1363 N N   . PRO A 173 ? 0.7536 1.0811 0.8895 0.0401  0.0672  -0.0332 173 PRO A N   
1364 C CA  . PRO A 173 ? 0.7608 1.0410 0.8634 0.0530  0.0503  -0.0390 173 PRO A CA  
1365 C C   . PRO A 173 ? 0.7680 1.0359 0.8821 0.0521  0.0274  -0.0420 173 PRO A C   
1366 O O   . PRO A 173 ? 0.7545 1.0537 0.9003 0.0570  0.0206  -0.0462 173 PRO A O   
1367 C CB  . PRO A 173 ? 0.7775 1.0637 0.8681 0.0808  0.0550  -0.0505 173 PRO A CB  
1368 C CG  . PRO A 173 ? 0.7317 1.0602 0.8342 0.0805  0.0812  -0.0475 173 PRO A CG  
1369 C CD  . PRO A 173 ? 0.7497 1.1161 0.8955 0.0584  0.0853  -0.0385 173 PRO A CD  
1370 N N   . GLU A 174 ? 0.7157 0.9397 0.8037 0.0467  0.0155  -0.0389 174 GLU A N   
1371 C CA  . GLU A 174 ? 0.6905 0.8973 0.7806 0.0438  -0.0040 -0.0394 174 GLU A CA  
1372 C C   . GLU A 174 ? 0.6995 0.8819 0.7736 0.0636  -0.0185 -0.0456 174 GLU A C   
1373 O O   . GLU A 174 ? 0.6969 0.8478 0.7439 0.0665  -0.0197 -0.0447 174 GLU A O   
1374 C CB  . GLU A 174 ? 0.7260 0.9023 0.7990 0.0250  -0.0049 -0.0310 174 GLU A CB  
1375 C CG  . GLU A 174 ? 0.6914 0.8797 0.7745 0.0047  0.0084  -0.0246 174 GLU A CG  
1376 C CD  . GLU A 174 ? 0.6697 0.8223 0.7330 -0.0088 0.0080  -0.0179 174 GLU A CD  
1377 O OE1 . GLU A 174 ? 0.7059 0.8312 0.7506 -0.0027 -0.0008 -0.0172 174 GLU A OE1 
1378 O OE2 . GLU A 174 ? 0.6656 0.8171 0.7326 -0.0254 0.0170  -0.0129 174 GLU A OE2 
1379 N N   . ILE A 175 ? 0.5999 0.7965 0.6915 0.0769  -0.0306 -0.0512 175 ILE A N   
1380 C CA  . ILE A 175 ? 0.5813 0.7491 0.6580 0.0948  -0.0469 -0.0557 175 ILE A CA  
1381 C C   . ILE A 175 ? 0.6139 0.7556 0.6802 0.0832  -0.0627 -0.0483 175 ILE A C   
1382 O O   . ILE A 175 ? 0.5746 0.7317 0.6565 0.0810  -0.0729 -0.0471 175 ILE A O   
1383 C CB  . ILE A 175 ? 0.5984 0.7923 0.6977 0.1188  -0.0519 -0.0645 175 ILE A CB  
1384 C CG1 . ILE A 175 ? 0.5952 0.8352 0.7168 0.1249  -0.0307 -0.0694 175 ILE A CG1 
1385 C CG2 . ILE A 175 ? 0.6610 0.8158 0.7368 0.1403  -0.0638 -0.0710 175 ILE A CG2 
1386 C CD1 . ILE A 175 ? 0.5560 0.7805 0.6503 0.1254  -0.0148 -0.0717 175 ILE A CD1 
1387 N N   . VAL A 176 ? 0.6834 0.7876 0.7229 0.0759  -0.0648 -0.0428 176 VAL A N   
1388 C CA  . VAL A 176 ? 0.6341 0.7152 0.6607 0.0633  -0.0735 -0.0341 176 VAL A CA  
1389 C C   . VAL A 176 ? 0.6948 0.7405 0.7028 0.0718  -0.0879 -0.0316 176 VAL A C   
1390 O O   . VAL A 176 ? 0.6978 0.7236 0.6931 0.0755  -0.0874 -0.0330 176 VAL A O   
1391 C CB  . VAL A 176 ? 0.6721 0.7439 0.6881 0.0459  -0.0611 -0.0271 176 VAL A CB  
1392 C CG1 . VAL A 176 ? 0.6529 0.7016 0.6537 0.0363  -0.0672 -0.0188 176 VAL A CG1 
1393 C CG2 . VAL A 176 ? 0.6288 0.7278 0.6605 0.0358  -0.0476 -0.0283 176 VAL A CG2 
1394 N N   . THR A 177 ? 0.6812 0.7174 0.6858 0.0736  -0.1021 -0.0273 177 THR A N   
1395 C CA  . THR A 177 ? 0.7129 0.7120 0.6985 0.0784  -0.1164 -0.0213 177 THR A CA  
1396 C C   . THR A 177 ? 0.6932 0.6793 0.6643 0.0657  -0.1214 -0.0097 177 THR A C   
1397 O O   . THR A 177 ? 0.6682 0.6731 0.6433 0.0572  -0.1175 -0.0096 177 THR A O   
1398 C CB  . THR A 177 ? 0.7216 0.7166 0.7128 0.1006  -0.1312 -0.0271 177 THR A CB  
1399 O OG1 . THR A 177 ? 0.7476 0.7669 0.7526 0.1039  -0.1393 -0.0262 177 THR A OG1 
1400 C CG2 . THR A 177 ? 0.6705 0.6815 0.6744 0.1170  -0.1235 -0.0407 177 THR A CG2 
1401 N N   . PHE A 178 ? 0.7509 0.7027 0.7026 0.0633  -0.1295 0.0001  178 PHE A N   
1402 C CA  . PHE A 178 ? 0.7422 0.6782 0.6748 0.0548  -0.1352 0.0126  178 PHE A CA  
1403 C C   . PHE A 178 ? 0.8025 0.7020 0.7196 0.0613  -0.1512 0.0213  178 PHE A C   
1404 O O   . PHE A 178 ? 0.8059 0.6854 0.7230 0.0638  -0.1537 0.0199  178 PHE A O   
1405 C CB  . PHE A 178 ? 0.7010 0.6347 0.6238 0.0370  -0.1197 0.0212  178 PHE A CB  
1406 C CG  . PHE A 178 ? 0.7471 0.6687 0.6720 0.0305  -0.1135 0.0257  178 PHE A CG  
1407 C CD1 . PHE A 178 ? 0.7004 0.6371 0.6400 0.0315  -0.1049 0.0170  178 PHE A CD1 
1408 C CD2 . PHE A 178 ? 0.7252 0.6219 0.6373 0.0217  -0.1169 0.0401  178 PHE A CD2 
1409 C CE1 . PHE A 178 ? 0.6918 0.6189 0.6324 0.0250  -0.1028 0.0211  178 PHE A CE1 
1410 C CE2 . PHE A 178 ? 0.7060 0.5954 0.6243 0.0133  -0.1142 0.0446  178 PHE A CE2 
1411 C CZ  . PHE A 178 ? 0.6990 0.6038 0.6312 0.0153  -0.1085 0.0344  178 PHE A CZ  
1412 N N   . ASN A 179 ? 0.7537 0.6416 0.6550 0.0636  -0.1634 0.0303  179 ASN A N   
1413 C CA  . ASN A 179 ? 0.7955 0.6448 0.6790 0.0704  -0.1804 0.0411  179 ASN A CA  
1414 C C   . ASN A 179 ? 0.8225 0.6472 0.6801 0.0521  -0.1761 0.0605  179 ASN A C   
1415 O O   . ASN A 179 ? 0.7798 0.6193 0.6277 0.0406  -0.1645 0.0651  179 ASN A O   
1416 C CB  . ASN A 179 ? 0.7855 0.6384 0.6680 0.0882  -0.1993 0.0403  179 ASN A CB  
1417 C CG  . ASN A 179 ? 0.9357 0.7437 0.8015 0.1005  -0.2187 0.0504  179 ASN A CG  
1418 O OD1 . ASN A 179 ? 0.9093 0.6876 0.7739 0.1021  -0.2198 0.0495  179 ASN A OD1 
1419 N ND2 . ASN A 179 ? 0.9591 0.7584 0.8092 0.1090  -0.2358 0.0604  179 ASN A ND2 
1420 N N   . THR A 180 ? 0.9312 0.7167 0.7765 0.0496  -0.1850 0.0720  180 THR A N   
1421 C CA  . THR A 180 ? 0.9286 0.6928 0.7536 0.0303  -0.1792 0.0929  180 THR A CA  
1422 C C   . THR A 180 ? 0.9745 0.6903 0.7787 0.0329  -0.1979 0.1079  180 THR A C   
1423 O O   . THR A 180 ? 1.0112 0.7053 0.8185 0.0505  -0.2151 0.1002  180 THR A O   
1424 C CB  . THR A 180 ? 0.9023 0.6742 0.7425 0.0131  -0.1639 0.0943  180 THR A CB  
1425 O OG1 . THR A 180 ? 0.9564 0.6961 0.8004 0.0119  -0.1761 0.0945  180 THR A OG1 
1426 C CG2 . THR A 180 ? 0.8562 0.6677 0.7194 0.0160  -0.1500 0.0768  180 THR A CG2 
1427 N N   . THR A 181 ? 0.7608 0.4583 0.5426 0.0158  -0.1932 0.1304  181 THR A N   
1428 C CA  . THR A 181 ? 0.8153 0.4618 0.5751 0.0128  -0.2090 0.1493  181 THR A CA  
1429 C C   . THR A 181 ? 0.8426 0.4578 0.6156 0.0075  -0.2172 0.1463  181 THR A C   
1430 O O   . THR A 181 ? 0.8824 0.4466 0.6385 0.0087  -0.2346 0.1575  181 THR A O   
1431 C CB  . THR A 181 ? 0.8542 0.4935 0.5892 -0.0087 -0.1967 0.1758  181 THR A CB  
1432 O OG1 . THR A 181 ? 0.8631 0.5253 0.6185 -0.0297 -0.1758 0.1789  181 THR A OG1 
1433 C CG2 . THR A 181 ? 0.8398 0.5028 0.5519 -0.0027 -0.1904 0.1772  181 THR A CG2 
1434 N N   . PHE A 182 ? 0.8380 0.4784 0.6373 0.0013  -0.2065 0.1318  182 PHE A N   
1435 C CA  . PHE A 182 ? 0.8296 0.4418 0.6387 -0.0032 -0.2164 0.1245  182 PHE A CA  
1436 C C   . PHE A 182 ? 0.8534 0.4820 0.6789 0.0182  -0.2188 0.0958  182 PHE A C   
1437 O O   . PHE A 182 ? 0.8273 0.4560 0.6644 0.0118  -0.2179 0.0851  182 PHE A O   
1438 C CB  . PHE A 182 ? 0.7996 0.4229 0.6227 -0.0327 -0.2045 0.1360  182 PHE A CB  
1439 C CG  . PHE A 182 ? 0.8019 0.4830 0.6432 -0.0387 -0.1806 0.1338  182 PHE A CG  
1440 C CD1 . PHE A 182 ? 0.7721 0.4751 0.6025 -0.0419 -0.1654 0.1467  182 PHE A CD1 
1441 C CD2 . PHE A 182 ? 0.7229 0.4322 0.5883 -0.0405 -0.1739 0.1189  182 PHE A CD2 
1442 C CE1 . PHE A 182 ? 0.7495 0.4990 0.5938 -0.0453 -0.1433 0.1432  182 PHE A CE1 
1443 C CE2 . PHE A 182 ? 0.6885 0.4459 0.5697 -0.0440 -0.1526 0.1178  182 PHE A CE2 
1444 C CZ  . PHE A 182 ? 0.7358 0.5119 0.6070 -0.0459 -0.1370 0.1294  182 PHE A CZ  
1445 N N   . GLY A 183 ? 0.8798 0.5262 0.7066 0.0427  -0.2214 0.0839  183 GLY A N   
1446 C CA  . GLY A 183 ? 0.8023 0.4578 0.6421 0.0661  -0.2251 0.0594  183 GLY A CA  
1447 C C   . GLY A 183 ? 0.8051 0.5194 0.6654 0.0739  -0.2097 0.0463  183 GLY A C   
1448 O O   . GLY A 183 ? 0.7709 0.5162 0.6347 0.0604  -0.1963 0.0536  183 GLY A O   
1449 N N   . SER A 184 ? 0.8310 0.5584 0.7040 0.0965  -0.2114 0.0263  184 SER A N   
1450 C CA  . SER A 184 ? 0.8610 0.6428 0.7562 0.1030  -0.1969 0.0131  184 SER A CA  
1451 C C   . SER A 184 ? 0.8252 0.6214 0.7285 0.0939  -0.1829 0.0027  184 SER A C   
1452 O O   . SER A 184 ? 0.8563 0.6268 0.7525 0.1002  -0.1883 -0.0071 184 SER A O   
1453 C CB  . SER A 184 ? 0.8259 0.6214 0.7342 0.1327  -0.2044 -0.0004 184 SER A CB  
1454 O OG  . SER A 184 ? 0.8899 0.7410 0.8229 0.1358  -0.1904 -0.0105 184 SER A OG  
1455 N N   . PHE A 185 ? 0.7251 0.5591 0.6399 0.0804  -0.1662 0.0043  185 PHE A N   
1456 C CA  . PHE A 185 ? 0.7086 0.5558 0.6288 0.0697  -0.1538 -0.0007 185 PHE A CA  
1457 C C   . PHE A 185 ? 0.7016 0.5906 0.6385 0.0782  -0.1397 -0.0136 185 PHE A C   
1458 O O   . PHE A 185 ? 0.6584 0.5760 0.6067 0.0791  -0.1341 -0.0129 185 PHE A O   
1459 C CB  . PHE A 185 ? 0.6887 0.5423 0.6086 0.0462  -0.1443 0.0147  185 PHE A CB  
1460 C CG  . PHE A 185 ? 0.7106 0.5295 0.6193 0.0317  -0.1538 0.0284  185 PHE A CG  
1461 C CD1 . PHE A 185 ? 0.7173 0.5071 0.6121 0.0307  -0.1653 0.0407  185 PHE A CD1 
1462 C CD2 . PHE A 185 ? 0.6722 0.4893 0.5853 0.0173  -0.1520 0.0312  185 PHE A CD2 
1463 C CE1 . PHE A 185 ? 0.7367 0.4947 0.6229 0.0138  -0.1729 0.0558  185 PHE A CE1 
1464 C CE2 . PHE A 185 ? 0.6648 0.4545 0.5732 0.0004  -0.1613 0.0451  185 PHE A CE2 
1465 C CZ  . PHE A 185 ? 0.7309 0.4904 0.6262 -0.0023 -0.1708 0.0576  185 PHE A CZ  
1466 N N   . GLY A 186 ? 0.6907 0.5822 0.6268 0.0822  -0.1344 -0.0246 186 GLY A N   
1467 C CA  . GLY A 186 ? 0.6325 0.5621 0.5814 0.0854  -0.1181 -0.0330 186 GLY A CA  
1468 C C   . GLY A 186 ? 0.6239 0.5592 0.5697 0.0694  -0.1083 -0.0282 186 GLY A C   
1469 O O   . GLY A 186 ? 0.6449 0.5556 0.5797 0.0596  -0.1161 -0.0227 186 GLY A O   
1470 N N   . ILE A 187 ? 0.6692 0.6366 0.6257 0.0662  -0.0923 -0.0292 187 ILE A N   
1471 C CA  . ILE A 187 ? 0.6964 0.6700 0.6509 0.0530  -0.0831 -0.0224 187 ILE A CA  
1472 C C   . ILE A 187 ? 0.7088 0.7043 0.6636 0.0585  -0.0698 -0.0299 187 ILE A C   
1473 O O   . ILE A 187 ? 0.6769 0.6969 0.6439 0.0647  -0.0605 -0.0351 187 ILE A O   
1474 C CB  . ILE A 187 ? 0.6530 0.6365 0.6162 0.0396  -0.0755 -0.0102 187 ILE A CB  
1475 C CG1 . ILE A 187 ? 0.6723 0.6617 0.6357 0.0297  -0.0662 -0.0024 187 ILE A CG1 
1476 C CG2 . ILE A 187 ? 0.6262 0.6327 0.6013 0.0418  -0.0676 -0.0140 187 ILE A CG2 
1477 C CD1 . ILE A 187 ? 0.6932 0.6804 0.6605 0.0188  -0.0623 0.0106  187 ILE A CD1 
1478 N N   . PHE A 188 ? 0.6550 0.6433 0.5968 0.0549  -0.0695 -0.0289 188 PHE A N   
1479 C CA  . PHE A 188 ? 0.6860 0.6924 0.6226 0.0562  -0.0558 -0.0305 188 PHE A CA  
1480 C C   . PHE A 188 ? 0.6954 0.6921 0.6211 0.0465  -0.0601 -0.0218 188 PHE A C   
1481 O O   . PHE A 188 ? 0.6678 0.6485 0.5946 0.0387  -0.0728 -0.0156 188 PHE A O   
1482 C CB  . PHE A 188 ? 0.6766 0.6872 0.6010 0.0729  -0.0522 -0.0455 188 PHE A CB  
1483 C CG  . PHE A 188 ? 0.7045 0.6830 0.6075 0.0826  -0.0687 -0.0567 188 PHE A CG  
1484 C CD1 . PHE A 188 ? 0.7588 0.7162 0.6384 0.0774  -0.0786 -0.0571 188 PHE A CD1 
1485 C CD2 . PHE A 188 ? 0.6891 0.6569 0.5943 0.0977  -0.0757 -0.0672 188 PHE A CD2 
1486 C CE1 . PHE A 188 ? 0.7605 0.6828 0.6174 0.0842  -0.0956 -0.0691 188 PHE A CE1 
1487 C CE2 . PHE A 188 ? 0.7061 0.6366 0.5886 0.1071  -0.0913 -0.0783 188 PHE A CE2 
1488 C CZ  . PHE A 188 ? 0.7714 0.6772 0.6284 0.0992  -0.1014 -0.0801 188 PHE A CZ  
1489 N N   . THR A 189 ? 0.5931 0.6022 0.5104 0.0464  -0.0492 -0.0193 189 THR A N   
1490 C CA  . THR A 189 ? 0.5904 0.5979 0.5032 0.0378  -0.0515 -0.0073 189 THR A CA  
1491 C C   . THR A 189 ? 0.6112 0.6138 0.4961 0.0429  -0.0549 -0.0120 189 THR A C   
1492 O O   . THR A 189 ? 0.6312 0.6449 0.5040 0.0496  -0.0411 -0.0160 189 THR A O   
1493 C CB  . THR A 189 ? 0.5638 0.5867 0.4905 0.0317  -0.0354 0.0047  189 THR A CB  
1494 O OG1 . THR A 189 ? 0.5810 0.6069 0.5263 0.0284  -0.0316 0.0049  189 THR A OG1 
1495 C CG2 . THR A 189 ? 0.5287 0.5496 0.4582 0.0255  -0.0390 0.0192  189 THR A CG2 
1496 N N   . CYS A 190 ? 0.7240 0.5839 0.5879 0.0944  -0.0319 0.0194  190 CYS A N   
1497 C CA  . CYS A 190 ? 0.7999 0.6470 0.6514 0.0896  -0.0304 0.0241  190 CYS A CA  
1498 C C   . CYS A 190 ? 0.7443 0.5760 0.5921 0.0847  -0.0233 0.0205  190 CYS A C   
1499 O O   . CYS A 190 ? 0.7119 0.5407 0.5588 0.0831  -0.0219 0.0185  190 CYS A O   
1500 C CB  . CYS A 190 ? 0.7890 0.6338 0.6386 0.0933  -0.0316 0.0263  190 CYS A CB  
1501 S SG  . CYS A 190 ? 0.7853 0.6282 0.6198 0.0910  -0.0367 0.0354  190 CYS A SG  
1502 N N   . PHE A 191 ? 0.7254 0.5462 0.5703 0.0824  -0.0184 0.0189  191 PHE A N   
1503 C CA  . PHE A 191 ? 0.7436 0.5513 0.5824 0.0750  -0.0101 0.0150  191 PHE A CA  
1504 C C   . PHE A 191 ? 0.7909 0.6071 0.6439 0.0763  -0.0057 0.0057  191 PHE A C   
1505 O O   . PHE A 191 ? 0.7717 0.5823 0.6214 0.0722  0.0004  0.0015  191 PHE A O   
1506 C CB  . PHE A 191 ? 0.8415 0.6353 0.6740 0.0708  -0.0049 0.0143  191 PHE A CB  
1507 C CG  . PHE A 191 ? 0.8191 0.5968 0.6367 0.0600  0.0035  0.0134  191 PHE A CG  
1508 C CD1 . PHE A 191 ? 0.8021 0.5762 0.6086 0.0558  0.0040  0.0157  191 PHE A CD1 
1509 C CD2 . PHE A 191 ? 0.8285 0.5934 0.6409 0.0522  0.0117  0.0095  191 PHE A CD2 
1510 C CE1 . PHE A 191 ? 0.8683 0.6286 0.6596 0.0450  0.0125  0.0139  191 PHE A CE1 
1511 C CE2 . PHE A 191 ? 0.9041 0.6547 0.7004 0.0401  0.0206  0.0084  191 PHE A CE2 
1512 C CZ  . PHE A 191 ? 0.9000 0.6492 0.6858 0.0369  0.0210  0.0105  191 PHE A CZ  
1513 N N   . ASP A 192 ? 0.7527 0.5838 0.6211 0.0830  -0.0092 0.0018  192 ASP A N   
1514 C CA  . ASP A 192 ? 0.7096 0.5525 0.5930 0.0868  -0.0075 -0.0069 192 ASP A CA  
1515 C C   . ASP A 192 ? 0.7060 0.5432 0.5842 0.0893  -0.0083 -0.0062 192 ASP A C   
1516 O O   . ASP A 192 ? 0.7190 0.5613 0.6070 0.0926  -0.0045 -0.0146 192 ASP A O   
1517 C CB  . ASP A 192 ? 0.7297 0.5889 0.6251 0.0941  -0.0146 -0.0082 192 ASP A CB  
1518 C CG  . ASP A 192 ? 0.7388 0.6057 0.6439 0.0919  -0.0118 -0.0146 192 ASP A CG  
1519 O OD1 . ASP A 192 ? 0.7734 0.6340 0.6784 0.0844  -0.0035 -0.0198 192 ASP A OD1 
1520 O OD2 . ASP A 192 ? 0.7384 0.6164 0.6489 0.0964  -0.0175 -0.0149 192 ASP A OD2 
1521 N N   . ILE A 193 ? 0.6506 0.4785 0.5142 0.0884  -0.0137 0.0028  193 ILE A N   
1522 C CA  . ILE A 193 ? 0.6916 0.5089 0.5468 0.0901  -0.0150 0.0036  193 ILE A CA  
1523 C C   . ILE A 193 ? 0.7338 0.5401 0.5843 0.0860  -0.0058 -0.0029 193 ILE A C   
1524 O O   . ILE A 193 ? 0.7208 0.5180 0.5683 0.0901  -0.0049 -0.0065 193 ILE A O   
1525 C CB  . ILE A 193 ? 0.6867 0.4964 0.5247 0.0853  -0.0213 0.0138  193 ILE A CB  
1526 C CG1 . ILE A 193 ? 0.6929 0.4879 0.5202 0.0871  -0.0241 0.0150  193 ILE A CG1 
1527 C CG2 . ILE A 193 ? 0.7113 0.5136 0.5353 0.0755  -0.0186 0.0180  193 ILE A CG2 
1528 C CD1 . ILE A 193 ? 0.6908 0.4761 0.4976 0.0770  -0.0278 0.0234  193 ILE A CD1 
1529 N N   . LEU A 194 ? 0.7427 0.5479 0.5910 0.0780  0.0015  -0.0050 194 LEU A N   
1530 C CA  . LEU A 194 ? 0.8222 0.6182 0.6636 0.0721  0.0114  -0.0117 194 LEU A CA  
1531 C C   . LEU A 194 ? 0.8071 0.6174 0.6679 0.0751  0.0197  -0.0253 194 LEU A C   
1532 O O   . LEU A 194 ? 0.7910 0.5977 0.6484 0.0701  0.0297  -0.0334 194 LEU A O   
1533 C CB  . LEU A 194 ? 0.7679 0.5530 0.5914 0.0598  0.0153  -0.0065 194 LEU A CB  
1534 C CG  . LEU A 194 ? 0.8314 0.6021 0.6325 0.0540  0.0115  0.0012  194 LEU A CG  
1535 C CD1 . LEU A 194 ? 0.8785 0.6427 0.6634 0.0457  0.0099  0.0097  194 LEU A CD1 
1536 C CD2 . LEU A 194 ? 0.8754 0.6349 0.6676 0.0502  0.0195  -0.0068 194 LEU A CD2 
1537 N N   . PHE A 195 ? 0.7990 0.6279 0.6802 0.0828  0.0161  -0.0292 195 PHE A N   
1538 C CA  . PHE A 195 ? 0.8385 0.6879 0.7406 0.0836  0.0236  -0.0430 195 PHE A CA  
1539 C C   . PHE A 195 ? 0.7790 0.6460 0.7011 0.0995  0.0165  -0.0487 195 PHE A C   
1540 O O   . PHE A 195 ? 0.7689 0.6274 0.6851 0.1089  0.0060  -0.0409 195 PHE A O   
1541 C CB  . PHE A 195 ? 0.8218 0.6784 0.7281 0.0739  0.0272  -0.0440 195 PHE A CB  
1542 C CG  . PHE A 195 ? 0.8262 0.6627 0.7109 0.0595  0.0342  -0.0387 195 PHE A CG  
1543 C CD1 . PHE A 195 ? 0.8820 0.7158 0.7610 0.0488  0.0470  -0.0465 195 PHE A CD1 
1544 C CD2 . PHE A 195 ? 0.8437 0.6640 0.7121 0.0574  0.0277  -0.0259 195 PHE A CD2 
1545 C CE1 . PHE A 195 ? 0.8834 0.6955 0.7375 0.0348  0.0526  -0.0402 195 PHE A CE1 
1546 C CE2 . PHE A 195 ? 0.9150 0.7147 0.7609 0.0462  0.0321  -0.0198 195 PHE A CE2 
1547 C CZ  . PHE A 195 ? 0.8562 0.6501 0.6932 0.0344  0.0442  -0.0261 195 PHE A CZ  
1548 N N   . HIS A 196 ? 0.8487 0.7404 0.7931 0.1020  0.0224  -0.0630 196 HIS A N   
1549 C CA  . HIS A 196 ? 0.8803 0.7919 0.8452 0.1195  0.0151  -0.0700 196 HIS A CA  
1550 C C   . HIS A 196 ? 0.8565 0.7849 0.8324 0.1237  0.0046  -0.0671 196 HIS A C   
1551 O O   . HIS A 196 ? 0.8554 0.7869 0.8348 0.1384  -0.0073 -0.0638 196 HIS A O   
1552 C CB  . HIS A 196 ? 0.8697 0.8079 0.8572 0.1215  0.0253  -0.0884 196 HIS A CB  
1553 C CG  . HIS A 196 ? 0.8674 0.8251 0.8757 0.1434  0.0170  -0.0963 196 HIS A CG  
1554 N ND1 . HIS A 196 ? 0.8252 0.8175 0.8585 0.1508  0.0104  -0.1036 196 HIS A ND1 
1555 C CD2 . HIS A 196 ? 0.8727 0.8185 0.8788 0.1604  0.0134  -0.0982 196 HIS A CD2 
1556 C CE1 . HIS A 196 ? 0.8108 0.8136 0.8574 0.1730  0.0020  -0.1089 196 HIS A CE1 
1557 N NE2 . HIS A 196 ? 0.8459 0.8186 0.8759 0.1798  0.0039  -0.1057 196 HIS A NE2 
1558 N N   . ASP A 197 ? 0.7925 0.7292 0.7712 0.1106  0.0090  -0.0685 197 ASP A N   
1559 C CA  . ASP A 197 ? 0.7892 0.7449 0.7797 0.1125  0.0014  -0.0696 197 ASP A CA  
1560 C C   . ASP A 197 ? 0.7756 0.7125 0.7483 0.1048  -0.0016 -0.0579 197 ASP A C   
1561 O O   . ASP A 197 ? 0.7651 0.6860 0.7256 0.0922  0.0065  -0.0554 197 ASP A O   
1562 C CB  . ASP A 197 ? 0.7110 0.6964 0.7229 0.1035  0.0099  -0.0854 197 ASP A CB  
1563 C CG  . ASP A 197 ? 0.7576 0.7705 0.7923 0.1129  0.0127  -0.0995 197 ASP A CG  
1564 O OD1 . ASP A 197 ? 0.8441 0.8530 0.8794 0.1307  0.0047  -0.0967 197 ASP A OD1 
1565 O OD2 . ASP A 197 ? 0.8628 0.9007 0.9140 0.1025  0.0233  -0.1140 197 ASP A OD2 
1566 N N   . PRO A 198 ? 0.7214 0.6596 0.6912 0.1126  -0.0133 -0.0506 198 PRO A N   
1567 C CA  . PRO A 198 ? 0.6897 0.6420 0.6682 0.1273  -0.0247 -0.0511 198 PRO A CA  
1568 C C   . PRO A 198 ? 0.7078 0.6385 0.6714 0.1369  -0.0302 -0.0417 198 PRO A C   
1569 O O   . PRO A 198 ? 0.6944 0.6297 0.6617 0.1506  -0.0392 -0.0417 198 PRO A O   
1570 C CB  . PRO A 198 ? 0.6744 0.6328 0.6497 0.1261  -0.0324 -0.0467 198 PRO A CB  
1571 C CG  . PRO A 198 ? 0.6783 0.6142 0.6356 0.1165  -0.0281 -0.0377 198 PRO A CG  
1572 C CD  . PRO A 198 ? 0.6854 0.6110 0.6414 0.1071  -0.0160 -0.0416 198 PRO A CD  
1573 N N   . ALA A 199 ? 0.7161 0.6217 0.6613 0.1296  -0.0251 -0.0342 199 ALA A N   
1574 C CA  . ALA A 199 ? 0.7457 0.6273 0.6708 0.1339  -0.0310 -0.0235 199 ALA A CA  
1575 C C   . ALA A 199 ? 0.7686 0.6455 0.6967 0.1481  -0.0348 -0.0272 199 ALA A C   
1576 O O   . ALA A 199 ? 0.7628 0.6266 0.6788 0.1565  -0.0448 -0.0196 199 ALA A O   
1577 C CB  . ALA A 199 ? 0.7670 0.6274 0.6747 0.1225  -0.0238 -0.0180 199 ALA A CB  
1578 N N   . VAL A 200 ? 0.8224 0.7077 0.7643 0.1510  -0.0266 -0.0391 200 VAL A N   
1579 C CA  . VAL A 200 ? 0.8328 0.7122 0.7779 0.1674  -0.0300 -0.0440 200 VAL A CA  
1580 C C   . VAL A 200 ? 0.7900 0.6957 0.7556 0.1837  -0.0403 -0.0496 200 VAL A C   
1581 O O   . VAL A 200 ? 0.8052 0.6994 0.7661 0.2008  -0.0501 -0.0472 200 VAL A O   
1582 C CB  . VAL A 200 ? 0.7945 0.6749 0.7469 0.1655  -0.0166 -0.0563 200 VAL A CB  
1583 C CG1 . VAL A 200 ? 0.7984 0.6755 0.7576 0.1860  -0.0201 -0.0639 200 VAL A CG1 
1584 C CG2 . VAL A 200 ? 0.8251 0.6762 0.7523 0.1506  -0.0089 -0.0493 200 VAL A CG2 
1585 N N   . THR A 201 ? 0.7025 0.6419 0.6891 0.1787  -0.0389 -0.0572 201 THR A N   
1586 C CA  . THR A 201 ? 0.7443 0.7133 0.7502 0.1926  -0.0501 -0.0628 201 THR A CA  
1587 C C   . THR A 201 ? 0.7271 0.6804 0.7139 0.1997  -0.0656 -0.0484 201 THR A C   
1588 O O   . THR A 201 ? 0.7110 0.6694 0.7010 0.2179  -0.0784 -0.0479 201 THR A O   
1589 C CB  . THR A 201 ? 0.7219 0.7268 0.7491 0.1805  -0.0447 -0.0732 201 THR A CB  
1590 O OG1 . THR A 201 ? 0.7479 0.7668 0.7904 0.1722  -0.0297 -0.0868 201 THR A OG1 
1591 C CG2 . THR A 201 ? 0.6665 0.7067 0.7139 0.1931  -0.0574 -0.0797 201 THR A CG2 
1592 N N   . LEU A 202 ? 0.6841 0.6190 0.6502 0.1857  -0.0648 -0.0367 202 LEU A N   
1593 C CA  . LEU A 202 ? 0.7157 0.6360 0.6609 0.1885  -0.0772 -0.0234 202 LEU A CA  
1594 C C   . LEU A 202 ? 0.7587 0.6482 0.6850 0.2024  -0.0854 -0.0156 202 LEU A C   
1595 O O   . LEU A 202 ? 0.7755 0.6618 0.6935 0.2143  -0.0991 -0.0096 202 LEU A O   
1596 C CB  . LEU A 202 ? 0.7080 0.6141 0.6350 0.1709  -0.0722 -0.0141 202 LEU A CB  
1597 C CG  . LEU A 202 ? 0.6953 0.6252 0.6338 0.1600  -0.0683 -0.0189 202 LEU A CG  
1598 C CD1 . LEU A 202 ? 0.6546 0.5689 0.5768 0.1462  -0.0624 -0.0110 202 LEU A CD1 
1599 C CD2 . LEU A 202 ? 0.6629 0.6124 0.6043 0.1656  -0.0799 -0.0188 202 LEU A CD2 
1600 N N   . VAL A 203 ? 0.7958 0.6596 0.7125 0.2008  -0.0776 -0.0155 203 VAL A N   
1601 C CA  . VAL A 203 ? 0.8343 0.6609 0.7284 0.2123  -0.0843 -0.0082 203 VAL A CA  
1602 C C   . VAL A 203 ? 0.8485 0.6843 0.7602 0.2369  -0.0905 -0.0180 203 VAL A C   
1603 O O   . VAL A 203 ? 0.8798 0.6996 0.7792 0.2535  -0.1045 -0.0115 203 VAL A O   
1604 C CB  . VAL A 203 ? 0.8425 0.6377 0.7181 0.2005  -0.0736 -0.0058 203 VAL A CB  
1605 C CG1 . VAL A 203 ? 0.8096 0.5601 0.6574 0.2102  -0.0800 0.0014  203 VAL A CG1 
1606 C CG2 . VAL A 203 ? 0.8616 0.6551 0.7240 0.1784  -0.0688 0.0028  203 VAL A CG2 
1607 N N   . LYS A 204 ? 1.0259 0.8882 0.9659 0.2397  -0.0803 -0.0341 204 LYS A N   
1608 C CA  . LYS A 204 ? 1.0113 0.8850 0.9709 0.2634  -0.0833 -0.0465 204 LYS A CA  
1609 C C   . LYS A 204 ? 0.9665 0.8795 0.9499 0.2794  -0.0965 -0.0517 204 LYS A C   
1610 O O   . LYS A 204 ? 0.9989 0.9108 0.9872 0.3048  -0.1081 -0.0542 204 LYS A O   
1611 C CB  . LYS A 204 ? 0.9728 0.8655 0.9541 0.2574  -0.0657 -0.0631 204 LYS A CB  
1612 C CG  . LYS A 204 ? 1.0721 0.9242 1.0311 0.2522  -0.0555 -0.0620 204 LYS A CG  
1613 C CD  . LYS A 204 ? 1.0765 0.8811 1.0064 0.2671  -0.0668 -0.0513 204 LYS A CD  
1614 C CE  . LYS A 204 ? 1.1286 0.9071 1.0525 0.2767  -0.0586 -0.0608 204 LYS A CE  
1615 N NZ  . LYS A 204 ? 1.1576 0.8844 1.0509 0.2925  -0.0701 -0.0510 204 LYS A NZ  
1616 N N   . ASP A 205 ? 0.8999 0.8478 0.8980 0.2659  -0.0955 -0.0540 205 ASP A N   
1617 C CA  . ASP A 205 ? 0.9324 0.9231 0.9547 0.2783  -0.1073 -0.0612 205 ASP A CA  
1618 C C   . ASP A 205 ? 0.9333 0.9158 0.9350 0.2786  -0.1233 -0.0465 205 ASP A C   
1619 O O   . ASP A 205 ? 0.9501 0.9473 0.9572 0.2979  -0.1397 -0.0462 205 ASP A O   
1620 C CB  . ASP A 205 ? 0.9138 0.9518 0.9671 0.2625  -0.0956 -0.0767 205 ASP A CB  
1621 C CG  . ASP A 205 ? 0.9252 0.9844 1.0046 0.2656  -0.0821 -0.0947 205 ASP A CG  
1622 O OD1 . ASP A 205 ? 0.8945 0.9317 0.9688 0.2815  -0.0818 -0.0958 205 ASP A OD1 
1623 O OD2 . ASP A 205 ? 0.9122 1.0088 1.0154 0.2512  -0.0712 -0.1084 205 ASP A OD2 
1624 N N   . PHE A 206 ? 0.8789 0.8400 0.8568 0.2581  -0.1190 -0.0347 206 PHE A N   
1625 C CA  . PHE A 206 ? 0.8735 0.8307 0.8316 0.2542  -0.1311 -0.0225 206 PHE A CA  
1626 C C   . PHE A 206 ? 0.9528 0.8593 0.8704 0.2558  -0.1382 -0.0041 206 PHE A C   
1627 O O   . PHE A 206 ? 0.9507 0.8503 0.8471 0.2534  -0.1491 0.0071  206 PHE A O   
1628 C CB  . PHE A 206 ? 0.8439 0.8178 0.8052 0.2303  -0.1214 -0.0242 206 PHE A CB  
1629 C CG  . PHE A 206 ? 0.8811 0.9032 0.8757 0.2270  -0.1182 -0.0406 206 PHE A CG  
1630 C CD1 . PHE A 206 ? 0.8481 0.8923 0.8709 0.2298  -0.1087 -0.0559 206 PHE A CD1 
1631 C CD2 . PHE A 206 ? 0.9450 0.9909 0.9414 0.2199  -0.1242 -0.0418 206 PHE A CD2 
1632 C CE1 . PHE A 206 ? 0.8475 0.9365 0.8996 0.2237  -0.1050 -0.0717 206 PHE A CE1 
1633 C CE2 . PHE A 206 ? 0.9024 0.9913 0.9277 0.2145  -0.1210 -0.0579 206 PHE A CE2 
1634 C CZ  . PHE A 206 ? 0.8332 0.9438 0.8863 0.2157  -0.1114 -0.0727 206 PHE A CZ  
1635 N N   . HIS A 207 ? 0.9692 0.8398 0.8737 0.2582  -0.1320 -0.0015 207 HIS A N   
1636 C CA  . HIS A 207 ? 0.9950 0.8139 0.8605 0.2624  -0.1397 0.0140  207 HIS A CA  
1637 C C   . HIS A 207 ? 1.0113 0.8125 0.8461 0.2411  -0.1398 0.0286  207 HIS A C   
1638 O O   . HIS A 207 ? 1.0051 0.7756 0.8074 0.2434  -0.1509 0.0424  207 HIS A O   
1639 C CB  . HIS A 207 ? 1.0232 0.8339 0.8826 0.2892  -0.1586 0.0178  207 HIS A CB  
1640 C CG  . HIS A 207 ? 1.0580 0.8921 0.9505 0.3134  -0.1599 0.0020  207 HIS A CG  
1641 N ND1 . HIS A 207 ? 1.0429 0.8558 0.9386 0.3212  -0.1507 -0.0053 207 HIS A ND1 
1642 C CD2 . HIS A 207 ? 1.0225 0.9020 0.9466 0.3315  -0.1694 -0.0090 207 HIS A CD2 
1643 C CE1 . HIS A 207 ? 1.0375 0.8830 0.9668 0.3437  -0.1535 -0.0207 207 HIS A CE1 
1644 N NE2 . HIS A 207 ? 1.0729 0.9607 1.0209 0.3502  -0.1651 -0.0233 207 HIS A NE2 
1645 N N   . VAL A 208 ? 0.8615 0.6811 0.7051 0.2203  -0.1274 0.0254  208 VAL A N   
1646 C CA  . VAL A 208 ? 0.8989 0.7079 0.7172 0.2011  -0.1265 0.0369  208 VAL A CA  
1647 C C   . VAL A 208 ? 0.8859 0.6466 0.6685 0.1937  -0.1254 0.0489  208 VAL A C   
1648 O O   . VAL A 208 ? 0.9108 0.6482 0.6915 0.1983  -0.1204 0.0461  208 VAL A O   
1649 C CB  . VAL A 208 ? 0.8490 0.6859 0.6848 0.1836  -0.1138 0.0303  208 VAL A CB  
1650 C CG1 . VAL A 208 ? 0.8059 0.6847 0.6751 0.1894  -0.1136 0.0169  208 VAL A CG1 
1651 C CG2 . VAL A 208 ? 0.9051 0.7287 0.7437 0.1752  -0.1006 0.0270  208 VAL A CG2 
1652 N N   . ASP A 209 ? 0.9335 0.6786 0.6857 0.1814  -0.1299 0.0615  209 ASP A N   
1653 C CA  . ASP A 209 ? 0.9278 0.6296 0.6438 0.1683  -0.1275 0.0725  209 ASP A CA  
1654 C C   . ASP A 209 ? 0.9252 0.6366 0.6437 0.1459  -0.1137 0.0707  209 ASP A C   
1655 O O   . ASP A 209 ? 0.9008 0.5830 0.6014 0.1364  -0.1081 0.0739  209 ASP A O   
1656 C CB  . ASP A 209 ? 0.9743 0.6545 0.6530 0.1619  -0.1378 0.0871  209 ASP A CB  
1657 C CG  . ASP A 209 ? 1.0364 0.7126 0.7110 0.1846  -0.1546 0.0905  209 ASP A CG  
1658 O OD1 . ASP A 209 ? 1.0349 0.6858 0.7077 0.2053  -0.1616 0.0901  209 ASP A OD1 
1659 O OD2 . ASP A 209 ? 1.0460 0.7452 0.7185 0.1822  -0.1614 0.0933  209 ASP A OD2 
1660 N N   . THR A 210 ? 0.8124 0.5635 0.5518 0.1379  -0.1085 0.0652  210 THR A N   
1661 C CA  . THR A 210 ? 0.8047 0.5674 0.5450 0.1187  -0.0978 0.0646  210 THR A CA  
1662 C C   . THR A 210 ? 0.8159 0.6158 0.5908 0.1207  -0.0908 0.0531  210 THR A C   
1663 O O   . THR A 210 ? 0.7629 0.5880 0.5546 0.1278  -0.0941 0.0478  210 THR A O   
1664 C CB  . THR A 210 ? 0.7940 0.5603 0.5117 0.1022  -0.0991 0.0730  210 THR A CB  
1665 O OG1 . THR A 210 ? 0.8351 0.5606 0.5150 0.0965  -0.1044 0.0846  210 THR A OG1 
1666 C CG2 . THR A 210 ? 0.7643 0.5511 0.4888 0.0853  -0.0887 0.0702  210 THR A CG2 
1667 N N   . ILE A 211 ? 0.6851 0.4863 0.4675 0.1129  -0.0814 0.0497  211 ILE A N   
1668 C CA  . ILE A 211 ? 0.6699 0.4985 0.4779 0.1120  -0.0742 0.0409  211 ILE A CA  
1669 C C   . ILE A 211 ? 0.6823 0.5266 0.4861 0.0986  -0.0706 0.0436  211 ILE A C   
1670 O O   . ILE A 211 ? 0.6808 0.5141 0.4656 0.0866  -0.0696 0.0502  211 ILE A O   
1671 C CB  . ILE A 211 ? 0.7119 0.5312 0.5288 0.1134  -0.0669 0.0357  211 ILE A CB  
1672 C CG1 . ILE A 211 ? 0.6913 0.5089 0.5226 0.1285  -0.0684 0.0283  211 ILE A CG1 
1673 C CG2 . ILE A 211 ? 0.6686 0.5069 0.5004 0.1072  -0.0594 0.0310  211 ILE A CG2 
1674 C CD1 . ILE A 211 ? 0.6892 0.5366 0.5444 0.1356  -0.0699 0.0202  211 ILE A CD1 
1675 N N   . VAL A 212 ? 0.6686 0.5395 0.4899 0.1002  -0.0688 0.0375  212 VAL A N   
1676 C CA  . VAL A 212 ? 0.6506 0.5398 0.4743 0.0916  -0.0644 0.0369  212 VAL A CA  
1677 C C   . VAL A 212 ? 0.6534 0.5484 0.4949 0.0947  -0.0583 0.0307  212 VAL A C   
1678 O O   . VAL A 212 ? 0.6544 0.5511 0.5106 0.1023  -0.0570 0.0240  212 VAL A O   
1679 C CB  . VAL A 212 ? 0.6690 0.5804 0.4951 0.0912  -0.0663 0.0342  212 VAL A CB  
1680 C CG1 . VAL A 212 ? 0.6916 0.5958 0.4931 0.0837  -0.0716 0.0424  212 VAL A CG1 
1681 C CG2 . VAL A 212 ? 0.6874 0.6081 0.5303 0.1015  -0.0681 0.0261  212 VAL A CG2 
1682 N N   . PHE A 213 ? 0.6486 0.5466 0.4872 0.0880  -0.0550 0.0329  213 PHE A N   
1683 C CA  . PHE A 213 ? 0.6640 0.5569 0.5103 0.0895  -0.0506 0.0306  213 PHE A CA  
1684 C C   . PHE A 213 ? 0.6452 0.5546 0.4959 0.0877  -0.0492 0.0303  213 PHE A C   
1685 O O   . PHE A 213 ? 0.6378 0.5498 0.4802 0.0805  -0.0496 0.0348  213 PHE A O   
1686 C CB  . PHE A 213 ? 0.6566 0.5277 0.4902 0.0847  -0.0498 0.0346  213 PHE A CB  
1687 C CG  . PHE A 213 ? 0.6946 0.5581 0.5324 0.0850  -0.0451 0.0323  213 PHE A CG  
1688 C CD1 . PHE A 213 ? 0.7175 0.5756 0.5662 0.0913  -0.0413 0.0261  213 PHE A CD1 
1689 C CD2 . PHE A 213 ? 0.6736 0.5366 0.5026 0.0774  -0.0444 0.0362  213 PHE A CD2 
1690 C CE1 . PHE A 213 ? 0.7106 0.5595 0.5587 0.0890  -0.0361 0.0245  213 PHE A CE1 
1691 C CE2 . PHE A 213 ? 0.6953 0.5492 0.5238 0.0769  -0.0408 0.0351  213 PHE A CE2 
1692 C CZ  . PHE A 213 ? 0.6550 0.5003 0.4917 0.0822  -0.0362 0.0295  213 PHE A CZ  
1693 N N   . PRO A 214 ? 0.5877 0.5094 0.4513 0.0945  -0.0479 0.0245  214 PRO A N   
1694 C CA  . PRO A 214 ? 0.6007 0.5332 0.4697 0.0975  -0.0470 0.0235  214 PRO A CA  
1695 C C   . PRO A 214 ? 0.5789 0.4941 0.4462 0.0985  -0.0452 0.0253  214 PRO A C   
1696 O O   . PRO A 214 ? 0.5572 0.4562 0.4262 0.0997  -0.0421 0.0227  214 PRO A O   
1697 C CB  . PRO A 214 ? 0.5708 0.5131 0.4514 0.1053  -0.0457 0.0156  214 PRO A CB  
1698 C CG  . PRO A 214 ? 0.5861 0.5282 0.4666 0.1040  -0.0466 0.0130  214 PRO A CG  
1699 C CD  . PRO A 214 ? 0.5725 0.4975 0.4456 0.1003  -0.0477 0.0179  214 PRO A CD  
1700 N N   . THR A 215 ? 0.6694 0.5903 0.5326 0.0971  -0.0472 0.0294  215 THR A N   
1701 C CA  . THR A 215 ? 0.7270 0.6308 0.5834 0.0961  -0.0464 0.0326  215 THR A CA  
1702 C C   . THR A 215 ? 0.7228 0.6378 0.5800 0.1016  -0.0504 0.0350  215 THR A C   
1703 O O   . THR A 215 ? 0.7095 0.6501 0.5716 0.1025  -0.0539 0.0349  215 THR A O   
1704 C CB  . THR A 215 ? 0.7088 0.6017 0.5522 0.0855  -0.0460 0.0368  215 THR A CB  
1705 O OG1 . THR A 215 ? 0.7306 0.6109 0.5651 0.0830  -0.0456 0.0399  215 THR A OG1 
1706 C CG2 . THR A 215 ? 0.7070 0.6167 0.5446 0.0772  -0.0495 0.0400  215 THR A CG2 
1707 N N   . ALA A 216 ? 0.6331 0.5294 0.4850 0.1056  -0.0500 0.0369  216 ALA A N   
1708 C CA  . ALA A 216 ? 0.6363 0.5370 0.4841 0.1116  -0.0559 0.0414  216 ALA A CA  
1709 C C   . ALA A 216 ? 0.6899 0.5700 0.5209 0.1033  -0.0554 0.0471  216 ALA A C   
1710 O O   . ALA A 216 ? 0.6680 0.5255 0.4900 0.1062  -0.0544 0.0493  216 ALA A O   
1711 C CB  . ALA A 216 ? 0.6230 0.5147 0.4754 0.1258  -0.0567 0.0389  216 ALA A CB  
1712 N N   . TRP A 217 ? 0.7280 0.6160 0.5523 0.0922  -0.0564 0.0494  217 TRP A N   
1713 C CA  . TRP A 217 ? 0.7219 0.5901 0.5298 0.0816  -0.0537 0.0522  217 TRP A CA  
1714 C C   . TRP A 217 ? 0.7053 0.5808 0.5018 0.0796  -0.0611 0.0582  217 TRP A C   
1715 O O   . TRP A 217 ? 0.7036 0.6067 0.5048 0.0786  -0.0673 0.0592  217 TRP A O   
1716 C CB  . TRP A 217 ? 0.6834 0.5509 0.4883 0.0705  -0.0501 0.0500  217 TRP A CB  
1717 C CG  . TRP A 217 ? 0.7518 0.5975 0.5414 0.0607  -0.0454 0.0499  217 TRP A CG  
1718 C CD1 . TRP A 217 ? 0.7471 0.5901 0.5202 0.0507  -0.0476 0.0531  217 TRP A CD1 
1719 C CD2 . TRP A 217 ? 0.7704 0.5963 0.5599 0.0595  -0.0373 0.0447  217 TRP A CD2 
1720 N NE1 . TRP A 217 ? 0.7419 0.5620 0.5034 0.0434  -0.0404 0.0499  217 TRP A NE1 
1721 C CE2 . TRP A 217 ? 0.7240 0.5345 0.4964 0.0494  -0.0339 0.0445  217 TRP A CE2 
1722 C CE3 . TRP A 217 ? 0.7388 0.5616 0.5418 0.0661  -0.0327 0.0392  217 TRP A CE3 
1723 C CZ2 . TRP A 217 ? 0.7237 0.5163 0.4936 0.0472  -0.0253 0.0383  217 TRP A CZ2 
1724 C CZ3 . TRP A 217 ? 0.7472 0.5551 0.5491 0.0639  -0.0253 0.0335  217 TRP A CZ3 
1725 C CH2 . TRP A 217 ? 0.7446 0.5377 0.5306 0.0551  -0.0213 0.0327  217 TRP A CH2 
1726 N N   . MET A 218 ? 0.7537 0.6067 0.5345 0.0778  -0.0603 0.0619  218 MET A N   
1727 C CA  . MET A 218 ? 0.7709 0.6271 0.5363 0.0752  -0.0681 0.0684  218 MET A CA  
1728 C C   . MET A 218 ? 0.7476 0.5937 0.4964 0.0579  -0.0637 0.0677  218 MET A C   
1729 O O   . MET A 218 ? 0.7733 0.5940 0.5128 0.0519  -0.0548 0.0651  218 MET A O   
1730 C CB  . MET A 218 ? 0.7663 0.5999 0.5192 0.0836  -0.0707 0.0739  218 MET A CB  
1731 C CG  . MET A 218 ? 0.7870 0.6260 0.5530 0.1021  -0.0759 0.0743  218 MET A CG  
1732 S SD  . MET A 218 ? 0.8995 0.6994 0.6448 0.1109  -0.0778 0.0814  218 MET A SD  
1733 C CE  . MET A 218 ? 0.8922 0.6628 0.6349 0.0982  -0.0612 0.0747  218 MET A CE  
1734 N N   . ASN A 219 ? 0.7239 0.5910 0.4701 0.0492  -0.0689 0.0682  219 ASN A N   
1735 C CA  . ASN A 219 ? 0.7176 0.5737 0.4474 0.0320  -0.0643 0.0659  219 ASN A CA  
1736 C C   . ASN A 219 ? 0.7811 0.6160 0.4876 0.0256  -0.0633 0.0686  219 ASN A C   
1737 O O   . ASN A 219 ? 0.7798 0.6209 0.4771 0.0290  -0.0722 0.0751  219 ASN A O   
1738 C CB  . ASN A 219 ? 0.7138 0.5977 0.4435 0.0219  -0.0707 0.0657  219 ASN A CB  
1739 C CG  . ASN A 219 ? 0.7091 0.6134 0.4583 0.0256  -0.0705 0.0629  219 ASN A CG  
1740 O OD1 . ASN A 219 ? 0.7262 0.6157 0.4821 0.0287  -0.0634 0.0597  219 ASN A OD1 
1741 N ND2 . ASN A 219 ? 0.6908 0.6316 0.4491 0.0250  -0.0783 0.0636  219 ASN A ND2 
1742 N N   . VAL A 220 ? 0.7875 0.5980 0.4834 0.0162  -0.0526 0.0634  220 VAL A N   
1743 C CA  . VAL A 220 ? 0.8281 0.6178 0.4999 0.0069  -0.0487 0.0638  220 VAL A CA  
1744 C C   . VAL A 220 ? 0.8524 0.6349 0.5113 -0.0087 -0.0434 0.0574  220 VAL A C   
1745 O O   . VAL A 220 ? 0.8113 0.5784 0.4740 -0.0101 -0.0332 0.0496  220 VAL A O   
1746 C CB  . VAL A 220 ? 0.8520 0.6183 0.5234 0.0108  -0.0383 0.0612  220 VAL A CB  
1747 C CG1 . VAL A 220 ? 0.8618 0.6081 0.5051 -0.0009 -0.0337 0.0619  220 VAL A CG1 
1748 C CG2 . VAL A 220 ? 0.8241 0.5938 0.5084 0.0256  -0.0430 0.0664  220 VAL A CG2 
1749 N N   . LEU A 221 ? 0.9102 0.7045 0.5541 -0.0198 -0.0509 0.0599  221 LEU A N   
1750 C CA  . LEU A 221 ? 0.9291 0.7122 0.5557 -0.0367 -0.0458 0.0532  221 LEU A CA  
1751 C C   . LEU A 221 ? 0.8875 0.6436 0.4926 -0.0442 -0.0360 0.0486  221 LEU A C   
1752 O O   . LEU A 221 ? 0.9578 0.7086 0.5555 -0.0405 -0.0363 0.0532  221 LEU A O   
1753 C CB  . LEU A 221 ? 0.8850 0.6919 0.5016 -0.0488 -0.0568 0.0561  221 LEU A CB  
1754 C CG  . LEU A 221 ? 0.9034 0.7327 0.5374 -0.0494 -0.0608 0.0555  221 LEU A CG  
1755 C CD1 . LEU A 221 ? 0.9351 0.7999 0.5660 -0.0595 -0.0730 0.0583  221 LEU A CD1 
1756 C CD2 . LEU A 221 ? 0.8595 0.6644 0.4877 -0.0587 -0.0508 0.0478  221 LEU A CD2 
1757 N N   . PRO A 222 ? 0.8103 0.5475 0.4029 -0.0554 -0.0267 0.0391  222 PRO A N   
1758 C CA  . PRO A 222 ? 0.8119 0.5462 0.4047 -0.0626 -0.0260 0.0340  222 PRO A CA  
1759 C C   . PRO A 222 ? 0.7983 0.5195 0.4092 -0.0515 -0.0189 0.0289  222 PRO A C   
1760 O O   . PRO A 222 ? 0.8032 0.5184 0.4118 -0.0568 -0.0194 0.0266  222 PRO A O   
1761 C CB  . PRO A 222 ? 0.8446 0.5588 0.4079 -0.0804 -0.0199 0.0261  222 PRO A CB  
1762 C CG  . PRO A 222 ? 0.8535 0.5520 0.4101 -0.0769 -0.0100 0.0223  222 PRO A CG  
1763 C CD  . PRO A 222 ? 0.8372 0.5532 0.4053 -0.0658 -0.0175 0.0332  222 PRO A CD  
1764 N N   . HIS A 223 ? 0.9241 0.6411 0.5514 -0.0372 -0.0129 0.0273  223 HIS A N   
1765 C CA  . HIS A 223 ? 0.9244 0.6305 0.5682 -0.0259 -0.0068 0.0215  223 HIS A CA  
1766 C C   . HIS A 223 ? 0.9398 0.6641 0.6096 -0.0114 -0.0122 0.0271  223 HIS A C   
1767 O O   . HIS A 223 ? 0.9257 0.6450 0.6076 -0.0031 -0.0108 0.0243  223 HIS A O   
1768 C CB  . HIS A 223 ? 0.9149 0.6049 0.5593 -0.0214 0.0058  0.0116  223 HIS A CB  
1769 C CG  . HIS A 223 ? 0.9898 0.6607 0.6088 -0.0347 0.0135  0.0034  223 HIS A CG  
1770 N ND1 . HIS A 223 ? 0.9936 0.6587 0.6042 -0.0383 0.0235  -0.0027 223 HIS A ND1 
1771 C CD2 . HIS A 223 ? 1.0262 0.6813 0.6241 -0.0468 0.0136  -0.0004 223 HIS A CD2 
1772 C CE1 . HIS A 223 ? 1.0504 0.6985 0.6368 -0.0510 0.0293  -0.0105 223 HIS A CE1 
1773 N NE2 . HIS A 223 ? 1.0549 0.6955 0.6330 -0.0563 0.0233  -0.0094 223 HIS A NE2 
1774 N N   . LEU A 224 ? 0.8282 0.5718 0.5052 -0.0075 -0.0187 0.0347  224 LEU A N   
1775 C CA  . LEU A 224 ? 0.7782 0.5368 0.4789 0.0064  -0.0222 0.0381  224 LEU A CA  
1776 C C   . LEU A 224 ? 0.7473 0.5311 0.4536 0.0072  -0.0335 0.0459  224 LEU A C   
1777 O O   . LEU A 224 ? 0.7285 0.5261 0.4468 0.0170  -0.0381 0.0503  224 LEU A O   
1778 C CB  . LEU A 224 ? 0.7762 0.5312 0.4827 0.0132  -0.0174 0.0375  224 LEU A CB  
1779 C CG  . LEU A 224 ? 0.7977 0.5351 0.5027 0.0120  -0.0048 0.0275  224 LEU A CG  
1780 C CD1 . LEU A 224 ? 0.7815 0.5151 0.4869 0.0128  0.0014  0.0267  224 LEU A CD1 
1781 C CD2 . LEU A 224 ? 0.8071 0.5445 0.5306 0.0217  -0.0021 0.0212  224 LEU A CD2 
1782 N N   . SER A 225 ? 0.7604 0.5504 0.4575 -0.0037 -0.0375 0.0467  225 SER A N   
1783 C CA  . SER A 225 ? 0.7830 0.6014 0.4907 -0.0030 -0.0461 0.0512  225 SER A CA  
1784 C C   . SER A 225 ? 0.7546 0.5744 0.4787 0.0057  -0.0442 0.0498  225 SER A C   
1785 O O   . SER A 225 ? 0.7673 0.5649 0.4888 0.0066  -0.0382 0.0457  225 SER A O   
1786 C CB  . SER A 225 ? 0.7844 0.6101 0.4760 -0.0211 -0.0496 0.0512  225 SER A CB  
1787 O OG  . SER A 225 ? 0.7903 0.6512 0.4934 -0.0218 -0.0577 0.0545  225 SER A OG  
1788 N N   . ALA A 226 ? 0.7398 0.5858 0.4806 0.0137  -0.0497 0.0527  226 ALA A N   
1789 C CA  . ALA A 226 ? 0.7513 0.5992 0.5068 0.0227  -0.0479 0.0512  226 ALA A CA  
1790 C C   . ALA A 226 ? 0.7683 0.6020 0.5133 0.0135  -0.0456 0.0501  226 ALA A C   
1791 O O   . ALA A 226 ? 0.7528 0.5643 0.4976 0.0190  -0.0414 0.0473  226 ALA A O   
1792 C CB  . ALA A 226 ? 0.7268 0.6074 0.4989 0.0299  -0.0537 0.0531  226 ALA A CB  
1793 N N   . VAL A 227 ? 0.8447 0.6904 0.5796 -0.0009 -0.0488 0.0520  227 VAL A N   
1794 C CA  . VAL A 227 ? 0.8549 0.6825 0.5749 -0.0117 -0.0469 0.0522  227 VAL A CA  
1795 C C   . VAL A 227 ? 0.9040 0.6912 0.6065 -0.0140 -0.0418 0.0492  227 VAL A C   
1796 O O   . VAL A 227 ? 0.8980 0.6598 0.5944 -0.0099 -0.0397 0.0486  227 VAL A O   
1797 C CB  . VAL A 227 ? 0.8490 0.6969 0.5584 -0.0313 -0.0499 0.0539  227 VAL A CB  
1798 C CG1 . VAL A 227 ? 0.8914 0.7829 0.6211 -0.0267 -0.0540 0.0548  227 VAL A CG1 
1799 C CG2 . VAL A 227 ? 0.8999 0.7505 0.5971 -0.0438 -0.0512 0.0526  227 VAL A CG2 
1800 N N   . GLU A 228 ? 0.7452 0.5258 0.4385 -0.0197 -0.0400 0.0468  228 GLU A N   
1801 C CA  . GLU A 228 ? 0.8003 0.5441 0.4759 -0.0230 -0.0340 0.0418  228 GLU A CA  
1802 C C   . GLU A 228 ? 0.7716 0.4987 0.4594 -0.0047 -0.0294 0.0378  228 GLU A C   
1803 O O   . GLU A 228 ? 0.8144 0.5140 0.4941 -0.0010 -0.0269 0.0352  228 GLU A O   
1804 C CB  . GLU A 228 ? 0.7821 0.5277 0.4468 -0.0321 -0.0328 0.0396  228 GLU A CB  
1805 C CG  . GLU A 228 ? 0.8072 0.5217 0.4598 -0.0311 -0.0249 0.0324  228 GLU A CG  
1806 C CD  . GLU A 228 ? 0.8534 0.5751 0.4985 -0.0371 -0.0239 0.0313  228 GLU A CD  
1807 O OE1 . GLU A 228 ? 0.8133 0.5581 0.4718 -0.0297 -0.0278 0.0359  228 GLU A OE1 
1808 O OE2 . GLU A 228 ? 0.8565 0.5582 0.4792 -0.0496 -0.0196 0.0259  228 GLU A OE2 
1809 N N   . PHE A 229 ? 0.7990 0.5424 0.5058 0.0071  -0.0285 0.0371  229 PHE A N   
1810 C CA  . PHE A 229 ? 0.8214 0.5540 0.5410 0.0219  -0.0234 0.0315  229 PHE A CA  
1811 C C   . PHE A 229 ? 0.7977 0.5351 0.5311 0.0333  -0.0269 0.0331  229 PHE A C   
1812 O O   . PHE A 229 ? 0.8095 0.5315 0.5466 0.0435  -0.0245 0.0284  229 PHE A O   
1813 C CB  . PHE A 229 ? 0.8016 0.5466 0.5336 0.0274  -0.0200 0.0295  229 PHE A CB  
1814 C CG  . PHE A 229 ? 0.8195 0.5575 0.5648 0.0391  -0.0132 0.0216  229 PHE A CG  
1815 C CD1 . PHE A 229 ? 0.8193 0.5368 0.5564 0.0389  -0.0058 0.0133  229 PHE A CD1 
1816 C CD2 . PHE A 229 ? 0.8424 0.5963 0.6094 0.0502  -0.0141 0.0211  229 PHE A CD2 
1817 C CE1 . PHE A 229 ? 0.8601 0.5779 0.6130 0.0504  0.0005  0.0043  229 PHE A CE1 
1818 C CE2 . PHE A 229 ? 0.8267 0.5799 0.6079 0.0595  -0.0082 0.0125  229 PHE A CE2 
1819 C CZ  . PHE A 229 ? 0.8538 0.5912 0.6294 0.0600  -0.0010 0.0041  229 PHE A CZ  
1820 N N   . HIS A 230 ? 0.7677 0.5271 0.5083 0.0324  -0.0328 0.0390  230 HIS A N   
1821 C CA  . HIS A 230 ? 0.7742 0.5377 0.5248 0.0420  -0.0361 0.0403  230 HIS A CA  
1822 C C   . HIS A 230 ? 0.7534 0.4902 0.4850 0.0385  -0.0378 0.0422  230 HIS A C   
1823 O O   . HIS A 230 ? 0.7793 0.5024 0.5144 0.0507  -0.0386 0.0402  230 HIS A O   
1824 C CB  . HIS A 230 ? 0.7126 0.5062 0.4737 0.0410  -0.0407 0.0446  230 HIS A CB  
1825 C CG  . HIS A 230 ? 0.7235 0.5371 0.5003 0.0465  -0.0400 0.0432  230 HIS A CG  
1826 N ND1 . HIS A 230 ? 0.6819 0.5220 0.4664 0.0458  -0.0438 0.0459  230 HIS A ND1 
1827 C CD2 . HIS A 230 ? 0.7276 0.5358 0.5109 0.0520  -0.0357 0.0394  230 HIS A CD2 
1828 C CE1 . HIS A 230 ? 0.7085 0.5545 0.5025 0.0527  -0.0429 0.0446  230 HIS A CE1 
1829 N NE2 . HIS A 230 ? 0.7151 0.5413 0.5071 0.0549  -0.0377 0.0411  230 HIS A NE2 
1830 N N   . SER A 231 ? 0.7762 0.5038 0.4862 0.0218  -0.0388 0.0461  231 SER A N   
1831 C CA  . SER A 231 ? 0.7972 0.4904 0.4832 0.0169  -0.0399 0.0483  231 SER A CA  
1832 C C   . SER A 231 ? 0.8430 0.5027 0.5225 0.0264  -0.0358 0.0417  231 SER A C   
1833 O O   . SER A 231 ? 0.8418 0.4746 0.5129 0.0361  -0.0380 0.0421  231 SER A O   
1834 C CB  . SER A 231 ? 0.8194 0.5084 0.4817 -0.0067 -0.0402 0.0521  231 SER A CB  
1835 O OG  . SER A 231 ? 0.8616 0.5411 0.5133 -0.0166 -0.0361 0.0476  231 SER A OG  
1836 N N   . ALA A 232 ? 0.8415 0.5019 0.5237 0.0245  -0.0298 0.0352  232 ALA A N   
1837 C CA  . ALA A 232 ? 0.8442 0.4774 0.5231 0.0347  -0.0244 0.0266  232 ALA A CA  
1838 C C   . ALA A 232 ? 0.8156 0.4563 0.5181 0.0571  -0.0253 0.0227  232 ALA A C   
1839 O O   . ALA A 232 ? 0.8312 0.4473 0.5298 0.0699  -0.0253 0.0182  232 ALA A O   
1840 C CB  . ALA A 232 ? 0.8293 0.4672 0.5078 0.0279  -0.0170 0.0198  232 ALA A CB  
1841 N N   . TRP A 233 ? 0.7960 0.4710 0.5230 0.0626  -0.0265 0.0235  233 TRP A N   
1842 C CA  . TRP A 233 ? 0.8345 0.5222 0.5851 0.0812  -0.0275 0.0188  233 TRP A CA  
1843 C C   . TRP A 233 ? 0.8258 0.5023 0.5713 0.0905  -0.0363 0.0242  233 TRP A C   
1844 O O   . TRP A 233 ? 0.8164 0.4842 0.5689 0.1072  -0.0382 0.0193  233 TRP A O   
1845 C CB  . TRP A 233 ? 0.7877 0.5103 0.5607 0.0814  -0.0269 0.0189  233 TRP A CB  
1846 C CG  . TRP A 233 ? 0.8061 0.5451 0.6042 0.0958  -0.0247 0.0106  233 TRP A CG  
1847 C CD1 . TRP A 233 ? 0.8143 0.5613 0.6249 0.0974  -0.0161 0.0011  233 TRP A CD1 
1848 C CD2 . TRP A 233 ? 0.8143 0.5663 0.6272 0.1084  -0.0312 0.0105  233 TRP A CD2 
1849 N NE1 . TRP A 233 ? 0.7762 0.5426 0.6104 0.1095  -0.0163 -0.0058 233 TRP A NE1 
1850 C CE2 . TRP A 233 ? 0.7837 0.5539 0.6201 0.1171  -0.0262 -0.0002 233 TRP A CE2 
1851 C CE3 . TRP A 233 ? 0.7718 0.5228 0.5789 0.1117  -0.0405 0.0180  233 TRP A CE3 
1852 C CZ2 . TRP A 233 ? 0.7632 0.5526 0.6189 0.1293  -0.0312 -0.0039 233 TRP A CZ2 
1853 C CZ3 . TRP A 233 ? 0.8004 0.5680 0.6246 0.1247  -0.0458 0.0152  233 TRP A CZ3 
1854 C CH2 . TRP A 233 ? 0.7854 0.5731 0.6345 0.1336  -0.0416 0.0041  233 TRP A CH2 
1855 N N   . ALA A 234 ? 0.9044 0.5823 0.6369 0.0798  -0.0418 0.0340  234 ALA A N   
1856 C CA  . ALA A 234 ? 0.9172 0.5809 0.6385 0.0858  -0.0501 0.0406  234 ALA A CA  
1857 C C   . ALA A 234 ? 0.9781 0.5965 0.6753 0.0906  -0.0514 0.0405  234 ALA A C   
1858 O O   . ALA A 234 ? 0.9759 0.5784 0.6696 0.1060  -0.0584 0.0424  234 ALA A O   
1859 C CB  . ALA A 234 ? 0.8818 0.5546 0.5896 0.0694  -0.0537 0.0503  234 ALA A CB  
1860 N N   . MET A 235 ? 0.9688 0.5642 0.6473 0.0780  -0.0454 0.0382  235 MET A N   
1861 C CA  . MET A 235 ? 0.9883 0.5349 0.6408 0.0821  -0.0457 0.0369  235 MET A CA  
1862 C C   . MET A 235 ? 0.9974 0.5391 0.6676 0.1065  -0.0438 0.0257  235 MET A C   
1863 O O   . MET A 235 ? 0.9893 0.5001 0.6489 0.1228  -0.0493 0.0258  235 MET A O   
1864 C CB  . MET A 235 ? 1.0052 0.5307 0.6333 0.0605  -0.0390 0.0354  235 MET A CB  
1865 C CG  . MET A 235 ? 1.0650 0.5333 0.6577 0.0590  -0.0397 0.0360  235 MET A CG  
1866 S SD  . MET A 235 ? 1.1489 0.5951 0.7090 0.0272  -0.0327 0.0350  235 MET A SD  
1867 C CE  . MET A 235 ? 1.0728 0.5362 0.6194 0.0026  -0.0382 0.0488  235 MET A CE  
1868 N N   . GLY A 236 ? 0.9420 0.5134 0.6378 0.1090  -0.0359 0.0157  236 GLY A N   
1869 C CA  . GLY A 236 ? 0.8978 0.4719 0.6131 0.1297  -0.0319 0.0027  236 GLY A CA  
1870 C C   . GLY A 236 ? 0.8828 0.4787 0.6225 0.1514  -0.0400 0.0020  236 GLY A C   
1871 O O   . GLY A 236 ? 0.8905 0.4746 0.6361 0.1729  -0.0427 -0.0050 236 GLY A O   
1872 N N   . MET A 237 ? 0.9333 0.5628 0.6881 0.1468  -0.0441 0.0080  237 MET A N   
1873 C CA  . MET A 237 ? 0.9229 0.5771 0.7003 0.1645  -0.0522 0.0071  237 MET A CA  
1874 C C   . MET A 237 ? 0.9436 0.5727 0.7004 0.1729  -0.0654 0.0181  237 MET A C   
1875 O O   . MET A 237 ? 0.9205 0.5608 0.6911 0.1924  -0.0741 0.0164  237 MET A O   
1876 C CB  . MET A 237 ? 0.9532 0.6493 0.7515 0.1553  -0.0509 0.0082  237 MET A CB  
1877 C CG  . MET A 237 ? 0.8859 0.6075 0.7059 0.1499  -0.0389 -0.0028 237 MET A CG  
1878 S SD  . MET A 237 ? 0.8825 0.6118 0.7247 0.1686  -0.0327 -0.0203 237 MET A SD  
1879 C CE  . MET A 237 ? 0.8848 0.6488 0.7558 0.1871  -0.0429 -0.0238 237 MET A CE  
1880 N N   . ARG A 238 ? 1.0810 0.6749 0.8030 0.1580  -0.0672 0.0290  238 ARG A N   
1881 C CA  . ARG A 238 ? 1.0868 0.6475 0.7802 0.1620  -0.0788 0.0409  238 ARG A CA  
1882 C C   . ARG A 238 ? 1.1270 0.7158 0.8263 0.1595  -0.0869 0.0494  238 ARG A C   
1883 O O   . ARG A 238 ? 1.1619 0.7454 0.8578 0.1751  -0.0984 0.0540  238 ARG A O   
1884 C CB  . ARG A 238 ? 1.1395 0.6729 0.8307 0.1893  -0.0858 0.0367  238 ARG A CB  
1885 C CG  . ARG A 238 ? 1.1671 0.6504 0.8332 0.1905  -0.0810 0.0330  238 ARG A CG  
1886 C CD  . ARG A 238 ? 1.1833 0.6747 0.8755 0.2162  -0.0780 0.0170  238 ARG A CD  
1887 N NE  . ARG A 238 ? 1.3140 0.7497 0.9804 0.2322  -0.0814 0.0154  238 ARG A NE  
1888 C CZ  . ARG A 238 ? 1.4071 0.8034 1.0496 0.2219  -0.0722 0.0109  238 ARG A CZ  
1889 N NH1 . ARG A 238 ? 1.4288 0.8399 1.0730 0.1972  -0.0592 0.0065  238 ARG A NH1 
1890 N NH2 . ARG A 238 ? 1.3936 0.7340 1.0099 0.2383  -0.0764 0.0097  238 ARG A NH2 
1891 N N   . VAL A 239 ? 0.9840 0.6021 0.6905 0.1402  -0.0814 0.0513  239 VAL A N   
1892 C CA  . VAL A 239 ? 0.9395 0.5823 0.6478 0.1344  -0.0871 0.0583  239 VAL A CA  
1893 C C   . VAL A 239 ? 0.9412 0.5849 0.6314 0.1084  -0.0823 0.0653  239 VAL A C   
1894 O O   . VAL A 239 ? 0.9416 0.5814 0.6286 0.0955  -0.0741 0.0626  239 VAL A O   
1895 C CB  . VAL A 239 ? 0.8887 0.5805 0.6357 0.1422  -0.0854 0.0494  239 VAL A CB  
1896 C CG1 . VAL A 239 ? 0.8651 0.5634 0.6336 0.1660  -0.0892 0.0402  239 VAL A CG1 
1897 C CG2 . VAL A 239 ? 0.8424 0.5554 0.6053 0.1296  -0.0737 0.0430  239 VAL A CG2 
1898 N N   . ASN A 240 ? 0.9116 0.5635 0.5900 0.1005  -0.0875 0.0736  240 ASN A N   
1899 C CA  . ASN A 240 ? 0.9124 0.5849 0.5861 0.0782  -0.0822 0.0767  240 ASN A CA  
1900 C C   . ASN A 240 ? 0.8776 0.5940 0.5866 0.0799  -0.0760 0.0676  240 ASN A C   
1901 O O   . ASN A 240 ? 0.8433 0.5771 0.5779 0.0956  -0.0767 0.0604  240 ASN A O   
1902 C CB  . ASN A 240 ? 0.8973 0.5762 0.5546 0.0706  -0.0879 0.0850  240 ASN A CB  
1903 C CG  . ASN A 240 ? 0.9785 0.6101 0.5960 0.0689  -0.0955 0.0960  240 ASN A CG  
1904 O OD1 . ASN A 240 ? 1.0307 0.6214 0.6254 0.0651  -0.0944 0.0987  240 ASN A OD1 
1905 N ND2 . ASN A 240 ? 0.9764 0.6110 0.5821 0.0710  -0.1033 0.1027  240 ASN A ND2 
1906 N N   . PHE A 241 ? 0.7719 0.5063 0.4810 0.0631  -0.0702 0.0678  241 PHE A N   
1907 C CA  . PHE A 241 ? 0.7382 0.5056 0.4753 0.0647  -0.0647 0.0604  241 PHE A CA  
1908 C C   . PHE A 241 ? 0.7457 0.5400 0.4822 0.0496  -0.0623 0.0623  241 PHE A C   
1909 O O   . PHE A 241 ? 0.7849 0.5722 0.5035 0.0332  -0.0604 0.0660  241 PHE A O   
1910 C CB  . PHE A 241 ? 0.7806 0.5351 0.5206 0.0646  -0.0592 0.0558  241 PHE A CB  
1911 C CG  . PHE A 241 ? 0.7038 0.4816 0.4707 0.0721  -0.0548 0.0482  241 PHE A CG  
1912 C CD1 . PHE A 241 ? 0.7064 0.5068 0.4812 0.0643  -0.0516 0.0477  241 PHE A CD1 
1913 C CD2 . PHE A 241 ? 0.7035 0.4806 0.4868 0.0870  -0.0540 0.0415  241 PHE A CD2 
1914 C CE1 . PHE A 241 ? 0.6801 0.4950 0.4745 0.0708  -0.0480 0.0420  241 PHE A CE1 
1915 C CE2 . PHE A 241 ? 0.7203 0.5158 0.5247 0.0907  -0.0490 0.0348  241 PHE A CE2 
1916 C CZ  . PHE A 241 ? 0.6955 0.5064 0.5032 0.0824  -0.0460 0.0358  241 PHE A CZ  
1917 N N   . LEU A 242 ? 0.7271 0.5537 0.4845 0.0551  -0.0619 0.0581  242 LEU A N   
1918 C CA  . LEU A 242 ? 0.7249 0.5822 0.4866 0.0449  -0.0595 0.0576  242 LEU A CA  
1919 C C   . LEU A 242 ? 0.6967 0.5741 0.4821 0.0519  -0.0561 0.0512  242 LEU A C   
1920 O O   . LEU A 242 ? 0.6738 0.5630 0.4777 0.0638  -0.0559 0.0459  242 LEU A O   
1921 C CB  . LEU A 242 ? 0.7179 0.5929 0.4798 0.0457  -0.0619 0.0575  242 LEU A CB  
1922 C CG  . LEU A 242 ? 0.7490 0.6077 0.4811 0.0334  -0.0649 0.0656  242 LEU A CG  
1923 C CD1 . LEU A 242 ? 0.7471 0.5626 0.4598 0.0378  -0.0696 0.0716  242 LEU A CD1 
1924 C CD2 . LEU A 242 ? 0.7249 0.6018 0.4568 0.0351  -0.0673 0.0649  242 LEU A CD2 
1925 N N   . ALA A 243 ? 0.6712 0.5499 0.4536 0.0438  -0.0539 0.0520  243 ALA A N   
1926 C CA  . ALA A 243 ? 0.6875 0.5795 0.4863 0.0498  -0.0521 0.0482  243 ALA A CA  
1927 C C   . ALA A 243 ? 0.6679 0.5945 0.4753 0.0464  -0.0524 0.0467  243 ALA A C   
1928 O O   . ALA A 243 ? 0.6698 0.6077 0.4673 0.0326  -0.0527 0.0491  243 ALA A O   
1929 C CB  . ALA A 243 ? 0.6706 0.5436 0.4595 0.0442  -0.0506 0.0496  243 ALA A CB  
1930 N N   . SER A 244 ? 0.6442 0.5876 0.4702 0.0588  -0.0521 0.0419  244 SER A N   
1931 C CA  . SER A 244 ? 0.6301 0.6072 0.4680 0.0609  -0.0525 0.0385  244 SER A CA  
1932 C C   . SER A 244 ? 0.6460 0.6238 0.4948 0.0718  -0.0536 0.0370  244 SER A C   
1933 O O   . SER A 244 ? 0.6304 0.5944 0.4865 0.0829  -0.0524 0.0343  244 SER A O   
1934 C CB  . SER A 244 ? 0.6099 0.6021 0.4564 0.0669  -0.0514 0.0333  244 SER A CB  
1935 O OG  . SER A 244 ? 0.6203 0.6435 0.4813 0.0733  -0.0510 0.0277  244 SER A OG  
1936 N N   . ASN A 245 ? 0.6979 0.6904 0.5455 0.0675  -0.0562 0.0390  245 ASN A N   
1937 C CA  . ASN A 245 ? 0.7340 0.7214 0.5849 0.0761  -0.0589 0.0402  245 ASN A CA  
1938 C C   . ASN A 245 ? 0.7358 0.7555 0.6014 0.0869  -0.0628 0.0370  245 ASN A C   
1939 O O   . ASN A 245 ? 0.7300 0.7833 0.6016 0.0819  -0.0636 0.0341  245 ASN A O   
1940 C CB  . ASN A 245 ? 0.7564 0.7331 0.5922 0.0639  -0.0605 0.0453  245 ASN A CB  
1941 C CG  . ASN A 245 ? 0.7563 0.7113 0.5876 0.0703  -0.0616 0.0479  245 ASN A CG  
1942 O OD1 . ASN A 245 ? 0.7886 0.7204 0.6210 0.0775  -0.0581 0.0467  245 ASN A OD1 
1943 N ND2 . ASN A 245 ? 0.8173 0.7816 0.6423 0.0662  -0.0664 0.0510  245 ASN A ND2 
1944 N N   . ILE A 246 ? 0.6737 0.5144 0.4994 -0.0543 -0.0565 -0.0012 246 ILE A N   
1945 C CA  . ILE A 246 ? 0.6733 0.5143 0.4950 -0.0421 -0.0480 0.0051  246 ILE A CA  
1946 C C   . ILE A 246 ? 0.6708 0.5349 0.4933 -0.0348 -0.0560 0.0121  246 ILE A C   
1947 O O   . ILE A 246 ? 0.6359 0.5061 0.4586 -0.0378 -0.0637 0.0124  246 ILE A O   
1948 C CB  . ILE A 246 ? 0.7154 0.5307 0.5284 -0.0345 -0.0328 0.0068  246 ILE A CB  
1949 C CG1 . ILE A 246 ? 0.7232 0.5186 0.5350 -0.0436 -0.0212 -0.0026 246 ILE A CG1 
1950 C CG2 . ILE A 246 ? 0.6875 0.5027 0.4918 -0.0148 -0.0255 0.0174  246 ILE A CG2 
1951 C CD1 . ILE A 246 ? 0.7089 0.5051 0.5196 -0.0405 -0.0158 -0.0037 246 ILE A CD1 
1952 N N   . HIS A 247 ? 0.7523 0.6327 0.5754 -0.0256 -0.0538 0.0161  247 HIS A N   
1953 C CA  . HIS A 247 ? 0.7553 0.6661 0.5799 -0.0174 -0.0601 0.0210  247 HIS A CA  
1954 C C   . HIS A 247 ? 0.8165 0.7243 0.6322 0.0057  -0.0504 0.0298  247 HIS A C   
1955 O O   . HIS A 247 ? 0.8058 0.7105 0.6186 0.0178  -0.0412 0.0326  247 HIS A O   
1956 C CB  . HIS A 247 ? 0.7566 0.6971 0.5889 -0.0233 -0.0653 0.0183  247 HIS A CB  
1957 C CG  . HIS A 247 ? 0.7438 0.7231 0.5801 -0.0212 -0.0729 0.0193  247 HIS A CG  
1958 N ND1 . HIS A 247 ? 0.7325 0.7211 0.5700 -0.0363 -0.0824 0.0147  247 HIS A ND1 
1959 C CD2 . HIS A 247 ? 0.7577 0.7714 0.5964 -0.0057 -0.0721 0.0229  247 HIS A CD2 
1960 C CE1 . HIS A 247 ? 0.7345 0.7630 0.5758 -0.0335 -0.0869 0.0139  247 HIS A CE1 
1961 N NE2 . HIS A 247 ? 0.7472 0.7952 0.5902 -0.0140 -0.0817 0.0191  247 HIS A NE2 
1962 N N   . TYR A 248 ? 0.7897 0.6969 0.5986 0.0132  -0.0517 0.0347  248 TYR A N   
1963 C CA  . TYR A 248 ? 0.8143 0.7143 0.6094 0.0374  -0.0421 0.0453  248 TYR A CA  
1964 C C   . TYR A 248 ? 0.7848 0.7038 0.5756 0.0424  -0.0500 0.0490  248 TYR A C   
1965 O O   . TYR A 248 ? 0.7677 0.6615 0.5484 0.0431  -0.0451 0.0517  248 TYR A O   
1966 C CB  . TYR A 248 ? 0.8453 0.6955 0.6274 0.0403  -0.0251 0.0472  248 TYR A CB  
1967 C CG  . TYR A 248 ? 0.8754 0.7093 0.6406 0.0668  -0.0100 0.0580  248 TYR A CG  
1968 C CD1 . TYR A 248 ? 0.9153 0.7492 0.6814 0.0747  -0.0034 0.0576  248 TYR A CD1 
1969 C CD2 . TYR A 248 ? 0.8604 0.6779 0.6059 0.0859  -0.0018 0.0694  248 TYR A CD2 
1970 C CE1 . TYR A 248 ? 0.9368 0.7525 0.6849 0.1023  0.0117  0.0679  248 TYR A CE1 
1971 C CE2 . TYR A 248 ? 0.8918 0.6897 0.6171 0.1140  0.0134  0.0812  248 TYR A CE2 
1972 C CZ  . TYR A 248 ? 0.9845 0.7809 0.7112 0.1228  0.0201  0.0803  248 TYR A CZ  
1973 O OH  . TYR A 248 ? 1.0578 0.8313 0.7625 0.1536  0.0365  0.0920  248 TYR A OH  
1974 N N   . PRO A 249 ? 0.6981 0.6640 0.4964 0.0440  -0.0617 0.0477  249 PRO A N   
1975 C CA  . PRO A 249 ? 0.6622 0.6513 0.4571 0.0449  -0.0705 0.0481  249 PRO A CA  
1976 C C   . PRO A 249 ? 0.6909 0.6647 0.4666 0.0679  -0.0623 0.0599  249 PRO A C   
1977 O O   . PRO A 249 ? 0.6781 0.6405 0.4472 0.0625  -0.0639 0.0594  249 PRO A O   
1978 C CB  . PRO A 249 ? 0.6454 0.6926 0.4505 0.0465  -0.0806 0.0443  249 PRO A CB  
1979 C CG  . PRO A 249 ? 0.6361 0.6848 0.4541 0.0332  -0.0800 0.0379  249 PRO A CG  
1980 C CD  . PRO A 249 ? 0.6525 0.6540 0.4635 0.0410  -0.0667 0.0433  249 PRO A CD  
1981 N N   . SER A 250 ? 0.9161 0.8826 0.6799 0.0936  -0.0516 0.0709  250 SER A N   
1982 C CA  . SER A 250 ? 0.9390 0.8794 0.6781 0.1184  -0.0396 0.0848  250 SER A CA  
1983 C C   . SER A 250 ? 0.9533 0.8480 0.6836 0.1044  -0.0320 0.0836  250 SER A C   
1984 O O   . SER A 250 ? 0.9638 0.8522 0.6773 0.1153  -0.0291 0.0912  250 SER A O   
1985 C CB  . SER A 250 ? 1.0467 0.9626 0.7734 0.1419  -0.0239 0.0944  250 SER A CB  
1986 O OG  . SER A 250 ? 1.0643 0.9216 0.7659 0.1526  -0.0045 0.1040  250 SER A OG  
1987 N N   . LYS A 251 ? 0.7993 0.6651 0.5401 0.0812  -0.0284 0.0738  251 LYS A N   
1988 C CA  . LYS A 251 ? 0.7962 0.6268 0.5327 0.0659  -0.0216 0.0697  251 LYS A CA  
1989 C C   . LYS A 251 ? 0.7757 0.6252 0.5298 0.0424  -0.0366 0.0573  251 LYS A C   
1990 O O   . LYS A 251 ? 0.7824 0.6092 0.5398 0.0266  -0.0329 0.0502  251 LYS A O   
1991 C CB  . LYS A 251 ? 0.8533 0.6397 0.5872 0.0573  -0.0053 0.0660  251 LYS A CB  
1992 C CG  . LYS A 251 ? 0.9094 0.6650 0.6228 0.0788  0.0134  0.0768  251 LYS A CG  
1993 C CD  . LYS A 251 ? 0.9345 0.6392 0.6405 0.0647  0.0331  0.0706  251 LYS A CD  
1994 C CE  . LYS A 251 ? 1.0825 0.7566 0.7717 0.0608  0.0453  0.0735  251 LYS A CE  
1995 N NZ  . LYS A 251 ? 1.1176 0.7545 0.8067 0.0375  0.0616  0.0615  251 LYS A NZ  
1996 N N   . LYS A 252 ? 0.7294 0.6203 0.4941 0.0394  -0.0522 0.0536  252 LYS A N   
1997 C CA  . LYS A 252 ? 0.7042 0.6071 0.4813 0.0182  -0.0645 0.0421  252 LYS A CA  
1998 C C   . LYS A 252 ? 0.6950 0.5791 0.4841 0.0004  -0.0643 0.0334  252 LYS A C   
1999 O O   . LYS A 252 ? 0.6796 0.5542 0.4732 -0.0133 -0.0681 0.0259  252 LYS A O   
2000 C CB  . LYS A 252 ? 0.7064 0.6011 0.4750 0.0165  -0.0644 0.0416  252 LYS A CB  
2001 C CG  . LYS A 252 ? 0.7140 0.6374 0.4711 0.0316  -0.0688 0.0480  252 LYS A CG  
2002 C CD  . LYS A 252 ? 0.7195 0.6328 0.4662 0.0300  -0.0672 0.0476  252 LYS A CD  
2003 C CE  . LYS A 252 ? 0.8425 0.7942 0.5805 0.0397  -0.0759 0.0494  252 LYS A CE  
2004 N NZ  . LYS A 252 ? 0.7972 0.7864 0.5353 0.0556  -0.0807 0.0550  252 LYS A NZ  
2005 N N   . MET A 253 ? 0.7150 0.5947 0.5079 0.0026  -0.0595 0.0344  253 MET A N   
2006 C CA  . MET A 253 ? 0.6893 0.5573 0.4922 -0.0127 -0.0603 0.0263  253 MET A CA  
2007 C C   . MET A 253 ? 0.6676 0.5626 0.4798 -0.0211 -0.0716 0.0223  253 MET A C   
2008 O O   . MET A 253 ? 0.6729 0.5868 0.4872 -0.0141 -0.0711 0.0253  253 MET A O   
2009 C CB  . MET A 253 ? 0.7269 0.5716 0.5264 -0.0080 -0.0467 0.0277  253 MET A CB  
2010 C CG  . MET A 253 ? 0.7320 0.5444 0.5233 -0.0095 -0.0337 0.0268  253 MET A CG  
2011 S SD  . MET A 253 ? 0.8553 0.6356 0.6367 -0.0033 -0.0136 0.0284  253 MET A SD  
2012 C CE  . MET A 253 ? 0.8530 0.5992 0.6258 -0.0132 0.0015  0.0236  253 MET A CE  
2013 N N   . THR A 254 ? 0.6829 0.5795 0.4989 -0.0355 -0.0805 0.0156  254 THR A N   
2014 C CA  . THR A 254 ? 0.7100 0.6218 0.5311 -0.0477 -0.0883 0.0109  254 THR A CA  
2015 C C   . THR A 254 ? 0.7426 0.6405 0.5617 -0.0604 -0.0943 0.0049  254 THR A C   
2016 O O   . THR A 254 ? 0.6837 0.5766 0.4989 -0.0594 -0.0959 0.0036  254 THR A O   
2017 C CB  . THR A 254 ? 0.7056 0.6528 0.5280 -0.0463 -0.0930 0.0114  254 THR A CB  
2018 O OG1 . THR A 254 ? 0.7036 0.6606 0.5293 -0.0630 -0.0980 0.0052  254 THR A OG1 
2019 C CG2 . THR A 254 ? 0.7087 0.6667 0.5259 -0.0443 -0.0973 0.0106  254 THR A CG2 
2020 N N   . GLY A 255 ? 0.8721 0.7648 0.6916 -0.0711 -0.0972 0.0016  255 GLY A N   
2021 C CA  . GLY A 255 ? 0.8478 0.7223 0.6617 -0.0798 -0.1016 -0.0026 255 GLY A CA  
2022 C C   . GLY A 255 ? 0.8864 0.7452 0.7002 -0.0802 -0.1007 -0.0032 255 GLY A C   
2023 O O   . GLY A 255 ? 0.8718 0.7226 0.6886 -0.0746 -0.0984 -0.0045 255 GLY A O   
2024 N N   . SER A 256 ? 0.6968 0.5532 0.5058 -0.0882 -0.1024 -0.0033 256 SER A N   
2025 C CA  . SER A 256 ? 0.6745 0.5200 0.4804 -0.0883 -0.1026 -0.0034 256 SER A CA  
2026 C C   . SER A 256 ? 0.7091 0.5364 0.5003 -0.0944 -0.1062 -0.0031 256 SER A C   
2027 O O   . SER A 256 ? 0.7104 0.5347 0.4947 -0.1033 -0.1061 -0.0038 256 SER A O   
2028 C CB  . SER A 256 ? 0.6670 0.5243 0.4768 -0.0902 -0.0988 -0.0020 256 SER A CB  
2029 O OG  . SER A 256 ? 0.7006 0.5663 0.5198 -0.0824 -0.0931 -0.0019 256 SER A OG  
2030 N N   . GLY A 257 ? 0.7462 0.5609 0.5305 -0.0896 -0.1083 -0.0026 257 GLY A N   
2031 C CA  . GLY A 257 ? 0.7731 0.5640 0.5381 -0.0924 -0.1097 -0.0003 257 GLY A CA  
2032 C C   . GLY A 257 ? 0.7655 0.5457 0.5198 -0.0829 -0.1126 0.0020  257 GLY A C   
2033 O O   . GLY A 257 ? 0.7230 0.5188 0.4874 -0.0751 -0.1146 -0.0006 257 GLY A O   
2034 N N   . ILE A 258 ? 0.7602 0.5134 0.4919 -0.0841 -0.1118 0.0065  258 ILE A N   
2035 C CA  . ILE A 258 ? 0.8014 0.5394 0.5157 -0.0707 -0.1148 0.0108  258 ILE A CA  
2036 C C   . ILE A 258 ? 0.8141 0.5227 0.5118 -0.0632 -0.1146 0.0119  258 ILE A C   
2037 O O   . ILE A 258 ? 0.8177 0.5003 0.5011 -0.0744 -0.1090 0.0127  258 ILE A O   
2038 C CB  . ILE A 258 ? 0.8393 0.5637 0.5339 -0.0756 -0.1116 0.0174  258 ILE A CB  
2039 C CG1 . ILE A 258 ? 0.7934 0.5467 0.5044 -0.0842 -0.1104 0.0151  258 ILE A CG1 
2040 C CG2 . ILE A 258 ? 0.8210 0.5330 0.4955 -0.0572 -0.1156 0.0231  258 ILE A CG2 
2041 C CD1 . ILE A 258 ? 0.8241 0.5665 0.5196 -0.0973 -0.1042 0.0198  258 ILE A CD1 
2042 N N   . TYR A 259 ? 0.8192 0.5343 0.5198 -0.0453 -0.1198 0.0103  259 TYR A N   
2043 C CA  . TYR A 259 ? 0.8720 0.5633 0.5596 -0.0342 -0.1195 0.0102  259 TYR A CA  
2044 C C   . TYR A 259 ? 0.9242 0.6045 0.5919 -0.0112 -0.1231 0.0159  259 TYR A C   
2045 O O   . TYR A 259 ? 0.9036 0.6123 0.5791 -0.0017 -0.1288 0.0157  259 TYR A O   
2046 C CB  . TYR A 259 ? 0.8118 0.5271 0.5230 -0.0315 -0.1220 0.0017  259 TYR A CB  
2047 C CG  . TYR A 259 ? 0.7960 0.5293 0.5268 -0.0492 -0.1194 -0.0024 259 TYR A CG  
2048 C CD1 . TYR A 259 ? 0.7987 0.5170 0.5218 -0.0652 -0.1148 -0.0018 259 TYR A CD1 
2049 C CD2 . TYR A 259 ? 0.7382 0.5042 0.4934 -0.0496 -0.1206 -0.0072 259 TYR A CD2 
2050 C CE1 . TYR A 259 ? 0.8248 0.5652 0.5649 -0.0774 -0.1133 -0.0049 259 TYR A CE1 
2051 C CE2 . TYR A 259 ? 0.7374 0.5166 0.5061 -0.0613 -0.1174 -0.0088 259 TYR A CE2 
2052 C CZ  . TYR A 259 ? 0.7783 0.5474 0.5399 -0.0733 -0.1148 -0.0072 259 TYR A CZ  
2053 O OH  . TYR A 259 ? 0.7709 0.5588 0.5454 -0.0810 -0.1126 -0.0085 259 TYR A OH  
2054 N N   . ALA A 260 ? 1.0047 0.6441 0.6453 -0.0013 -0.1193 0.0205  260 ALA A N   
2055 C CA  . ALA A 260 ? 0.9797 0.6035 0.5960 0.0256  -0.1217 0.0279  260 ALA A CA  
2056 C C   . ALA A 260 ? 1.0228 0.6395 0.6377 0.0434  -0.1224 0.0239  260 ALA A C   
2057 O O   . ALA A 260 ? 0.9844 0.5968 0.6104 0.0314  -0.1191 0.0166  260 ALA A O   
2058 C CB  . ALA A 260 ? 0.9943 0.5641 0.5695 0.0247  -0.1131 0.0397  260 ALA A CB  
2059 N N   . PRO A 261 ? 0.9626 0.5821 0.5644 0.0736  -0.1270 0.0279  261 PRO A N   
2060 C CA  . PRO A 261 ? 0.9398 0.5558 0.5411 0.0930  -0.1272 0.0234  261 PRO A CA  
2061 C C   . PRO A 261 ? 0.9794 0.5349 0.5547 0.0869  -0.1160 0.0249  261 PRO A C   
2062 O O   . PRO A 261 ? 0.9859 0.5428 0.5710 0.0879  -0.1144 0.0165  261 PRO A O   
2063 C CB  . PRO A 261 ? 0.9680 0.5938 0.5521 0.1292  -0.1334 0.0302  261 PRO A CB  
2064 C CG  . PRO A 261 ? 0.9309 0.5969 0.5268 0.1240  -0.1407 0.0317  261 PRO A CG  
2065 C CD  . PRO A 261 ? 0.9134 0.5526 0.5058 0.0921  -0.1336 0.0348  261 PRO A CD  
2066 N N   . ASN A 262 ? 1.1669 0.6690 0.7084 0.0779  -0.1067 0.0340  262 ASN A N   
2067 C CA  . ASN A 262 ? 1.2009 0.6399 0.7124 0.0705  -0.0934 0.0340  262 ASN A CA  
2068 C C   . ASN A 262 ? 1.1899 0.6269 0.7152 0.0322  -0.0876 0.0246  262 ASN A C   
2069 O O   . ASN A 262 ? 1.2242 0.6216 0.7329 0.0221  -0.0776 0.0192  262 ASN A O   
2070 C CB  . ASN A 262 ? 1.2249 0.5999 0.6861 0.0810  -0.0830 0.0484  262 ASN A CB  
2071 C CG  . ASN A 262 ? 1.3280 0.6969 0.7834 0.0551  -0.0790 0.0537  262 ASN A CG  
2072 O OD1 . ASN A 262 ? 1.2789 0.6496 0.7471 0.0213  -0.0740 0.0459  262 ASN A OD1 
2073 N ND2 . ASN A 262 ? 1.3719 0.7380 0.8079 0.0721  -0.0814 0.0666  262 ASN A ND2 
2074 N N   . SER A 263 ? 1.2231 0.7033 0.7775 0.0117  -0.0932 0.0217  263 SER A N   
2075 C CA  . SER A 263 ? 1.1808 0.6645 0.7471 -0.0214 -0.0883 0.0136  263 SER A CA  
2076 C C   . SER A 263 ? 1.1679 0.7019 0.7650 -0.0353 -0.0953 0.0128  263 SER A C   
2077 O O   . SER A 263 ? 1.1655 0.7182 0.7664 -0.0245 -0.1009 0.0192  263 SER A O   
2078 C CB  . SER A 263 ? 1.2585 0.6845 0.7888 -0.0400 -0.0739 0.0157  263 SER A CB  
2079 O OG  . SER A 263 ? 1.2535 0.6993 0.7982 -0.0719 -0.0713 0.0100  263 SER A OG  
2080 N N   . SER A 264 ? 1.1699 0.7258 0.7870 -0.0583 -0.0945 0.0045  264 SER A N   
2081 C CA  . SER A 264 ? 1.1312 0.7245 0.7704 -0.0729 -0.0976 0.0045  264 SER A CA  
2082 C C   . SER A 264 ? 1.1514 0.7195 0.7687 -0.0868 -0.0901 0.0102  264 SER A C   
2083 O O   . SER A 264 ? 1.1537 0.6819 0.7456 -0.1006 -0.0798 0.0088  264 SER A O   
2084 C CB  . SER A 264 ? 1.1000 0.7229 0.7622 -0.0904 -0.0981 -0.0047 264 SER A CB  
2085 O OG  . SER A 264 ? 1.0821 0.7126 0.7450 -0.1130 -0.0936 -0.0061 264 SER A OG  
2086 N N   . ARG A 265 ? 0.9925 0.5826 0.6178 -0.0850 -0.0937 0.0156  265 ARG A N   
2087 C CA  . ARG A 265 ? 1.0539 0.6242 0.6591 -0.0983 -0.0862 0.0212  265 ARG A CA  
2088 C C   . ARG A 265 ? 1.0302 0.6347 0.6566 -0.1215 -0.0846 0.0157  265 ARG A C   
2089 O O   . ARG A 265 ? 1.0824 0.6709 0.6937 -0.1414 -0.0752 0.0157  265 ARG A O   
2090 C CB  . ARG A 265 ? 1.0599 0.6289 0.6537 -0.0794 -0.0901 0.0313  265 ARG A CB  
2091 C CG  . ARG A 265 ? 1.0702 0.6020 0.6355 -0.0542 -0.0901 0.0385  265 ARG A CG  
2092 C CD  . ARG A 265 ? 1.1246 0.5944 0.6451 -0.0597 -0.0767 0.0468  265 ARG A CD  
2093 N NE  . ARG A 265 ? 1.2374 0.6980 0.7358 -0.0464 -0.0769 0.0590  265 ARG A NE  
2094 C CZ  . ARG A 265 ? 1.2913 0.7351 0.7665 -0.0152 -0.0805 0.0688  265 ARG A CZ  
2095 N NH1 . ARG A 265 ? 1.3257 0.7579 0.7966 0.0067  -0.0834 0.0679  265 ARG A NH1 
2096 N NH2 . ARG A 265 ? 1.3047 0.7459 0.7596 -0.0041 -0.0812 0.0798  265 ARG A NH2 
2097 N N   . ALA A 266 ? 0.8837 0.5345 0.5432 -0.1187 -0.0923 0.0111  266 ALA A N   
2098 C CA  . ALA A 266 ? 0.8458 0.5315 0.5256 -0.1361 -0.0909 0.0058  266 ALA A CA  
2099 C C   . ALA A 266 ? 0.8237 0.5456 0.5323 -0.1285 -0.0977 0.0010  266 ALA A C   
2100 O O   . ALA A 266 ? 0.8155 0.5434 0.5328 -0.1114 -0.1033 0.0024  266 ALA A O   
2101 C CB  . ALA A 266 ? 0.8770 0.5779 0.5593 -0.1392 -0.0896 0.0102  266 ALA A CB  
2102 N N   . PHE A 267 ? 0.8101 0.5579 0.5324 -0.1412 -0.0964 -0.0050 267 PHE A N   
2103 C CA  . PHE A 267 ? 0.8100 0.5893 0.5553 -0.1323 -0.1013 -0.0076 267 PHE A CA  
2104 C C   . PHE A 267 ? 0.7861 0.6024 0.5458 -0.1426 -0.0998 -0.0111 267 PHE A C   
2105 O O   . PHE A 267 ? 0.7849 0.6052 0.5382 -0.1602 -0.0954 -0.0150 267 PHE A O   
2106 C CB  . PHE A 267 ? 0.7963 0.5636 0.5385 -0.1271 -0.1033 -0.0113 267 PHE A CB  
2107 C CG  . PHE A 267 ? 0.8528 0.6270 0.5922 -0.1426 -0.1008 -0.0191 267 PHE A CG  
2108 C CD1 . PHE A 267 ? 0.8095 0.6212 0.5660 -0.1424 -0.1035 -0.0225 267 PHE A CD1 
2109 C CD2 . PHE A 267 ? 0.8301 0.5726 0.5474 -0.1572 -0.0949 -0.0235 267 PHE A CD2 
2110 C CE1 . PHE A 267 ? 0.7710 0.5971 0.5254 -0.1565 -0.1023 -0.0312 267 PHE A CE1 
2111 C CE2 . PHE A 267 ? 0.8701 0.6228 0.5852 -0.1747 -0.0919 -0.0337 267 PHE A CE2 
2112 C CZ  . PHE A 267 ? 0.8034 0.6019 0.5383 -0.1744 -0.0966 -0.0381 267 PHE A CZ  
2113 N N   . HIS A 268 ? 0.7522 0.5957 0.5302 -0.1308 -0.1026 -0.0099 268 HIS A N   
2114 C CA  . HIS A 268 ? 0.7560 0.6384 0.5482 -0.1324 -0.1019 -0.0115 268 HIS A CA  
2115 C C   . HIS A 268 ? 0.6998 0.5979 0.5015 -0.1196 -0.1046 -0.0112 268 HIS A C   
2116 O O   . HIS A 268 ? 0.6877 0.5727 0.4917 -0.1066 -0.1051 -0.0078 268 HIS A O   
2117 C CB  . HIS A 268 ? 0.6870 0.5828 0.4874 -0.1272 -0.0994 -0.0075 268 HIS A CB  
2118 C CG  . HIS A 268 ? 0.6862 0.6226 0.5001 -0.1243 -0.0980 -0.0083 268 HIS A CG  
2119 N ND1 . HIS A 268 ? 0.6977 0.6617 0.5135 -0.1386 -0.0965 -0.0137 268 HIS A ND1 
2120 C CD2 . HIS A 268 ? 0.6690 0.6232 0.4937 -0.1076 -0.0968 -0.0046 268 HIS A CD2 
2121 C CE1 . HIS A 268 ? 0.6779 0.6808 0.5070 -0.1284 -0.0961 -0.0132 268 HIS A CE1 
2122 N NE2 . HIS A 268 ? 0.6875 0.6814 0.5204 -0.1083 -0.0959 -0.0067 268 HIS A NE2 
2123 N N   . TYR A 269 ? 0.7377 0.6667 0.5442 -0.1236 -0.1056 -0.0152 269 TYR A N   
2124 C CA  . TYR A 269 ? 0.7068 0.6552 0.5192 -0.1102 -0.1078 -0.0137 269 TYR A CA  
2125 C C   . TYR A 269 ? 0.6864 0.6821 0.5072 -0.1099 -0.1084 -0.0157 269 TYR A C   
2126 O O   . TYR A 269 ? 0.6819 0.6979 0.5016 -0.1271 -0.1093 -0.0243 269 TYR A O   
2127 C CB  . TYR A 269 ? 0.7150 0.6502 0.5188 -0.1144 -0.1103 -0.0187 269 TYR A CB  
2128 C CG  . TYR A 269 ? 0.7085 0.6640 0.5153 -0.1009 -0.1122 -0.0168 269 TYR A CG  
2129 C CD1 . TYR A 269 ? 0.6963 0.6926 0.5055 -0.1025 -0.1149 -0.0209 269 TYR A CD1 
2130 C CD2 . TYR A 269 ? 0.7114 0.6473 0.5173 -0.0864 -0.1105 -0.0112 269 TYR A CD2 
2131 C CE1 . TYR A 269 ? 0.7317 0.7463 0.5398 -0.0873 -0.1165 -0.0175 269 TYR A CE1 
2132 C CE2 . TYR A 269 ? 0.6888 0.6388 0.4934 -0.0737 -0.1103 -0.0079 269 TYR A CE2 
2133 C CZ  . TYR A 269 ? 0.7312 0.7192 0.5357 -0.0728 -0.1136 -0.0101 269 TYR A CZ  
2134 O OH  . TYR A 269 ? 0.7064 0.7080 0.5059 -0.0577 -0.1134 -0.0054 269 TYR A OH  
2135 N N   . ASP A 270 ? 0.7326 0.7464 0.5607 -0.0906 -0.1069 -0.0085 270 ASP A N   
2136 C CA  . ASP A 270 ? 0.7376 0.8007 0.5739 -0.0847 -0.1075 -0.0092 270 ASP A CA  
2137 C C   . ASP A 270 ? 0.7818 0.8561 0.6179 -0.0579 -0.1064 -0.0001 270 ASP A C   
2138 O O   . ASP A 270 ? 0.8104 0.8652 0.6459 -0.0425 -0.1003 0.0081  270 ASP A O   
2139 C CB  . ASP A 270 ? 0.7683 0.8408 0.6114 -0.0884 -0.1036 -0.0091 270 ASP A CB  
2140 C CG  . ASP A 270 ? 0.7883 0.9161 0.6414 -0.0778 -0.1037 -0.0096 270 ASP A CG  
2141 O OD1 . ASP A 270 ? 0.7712 0.9378 0.6265 -0.0754 -0.1084 -0.0135 270 ASP A OD1 
2142 O OD2 . ASP A 270 ? 0.8084 0.9441 0.6673 -0.0708 -0.0991 -0.0066 270 ASP A OD2 
2143 N N   . MET A 271 ? 0.7315 0.8358 0.5653 -0.0526 -0.1110 -0.0019 271 MET A N   
2144 C CA  . MET A 271 ? 0.7349 0.8537 0.5640 -0.0252 -0.1097 0.0080  271 MET A CA  
2145 C C   . MET A 271 ? 0.7439 0.9181 0.5796 -0.0100 -0.1110 0.0095  271 MET A C   
2146 O O   . MET A 271 ? 0.7556 0.9381 0.5847 0.0183  -0.1080 0.0204  271 MET A O   
2147 C CB  . MET A 271 ? 0.6956 0.8194 0.5159 -0.0249 -0.1144 0.0059  271 MET A CB  
2148 C CG  . MET A 271 ? 0.7001 0.7724 0.5113 -0.0256 -0.1107 0.0093  271 MET A CG  
2149 S SD  . MET A 271 ? 0.7626 0.7932 0.5682 -0.0047 -0.0991 0.0231  271 MET A SD  
2150 C CE  . MET A 271 ? 0.7316 0.7632 0.5207 0.0179  -0.0959 0.0330  271 MET A CE  
2151 N N   . LYS A 272 ? 0.8441 1.0550 0.6913 -0.0271 -0.1141 -0.0009 272 LYS A N   
2152 C CA  . LYS A 272 ? 0.8568 1.1346 0.7131 -0.0155 -0.1170 -0.0032 272 LYS A CA  
2153 C C   . LYS A 272 ? 0.8819 1.1642 0.7438 0.0029  -0.1104 0.0042  272 LYS A C   
2154 O O   . LYS A 272 ? 0.9567 1.2756 0.8186 0.0316  -0.1099 0.0111  272 LYS A O   
2155 C CB  . LYS A 272 ? 0.8098 1.1312 0.6762 -0.0465 -0.1221 -0.0210 272 LYS A CB  
2156 C CG  . LYS A 272 ? 0.8201 1.1365 0.6790 -0.0652 -0.1272 -0.0303 272 LYS A CG  
2157 C CD  . LYS A 272 ? 0.8429 1.1968 0.7084 -0.0993 -0.1294 -0.0500 272 LYS A CD  
2158 C CE  . LYS A 272 ? 0.9098 1.3307 0.7911 -0.0996 -0.1294 -0.0565 272 LYS A CE  
2159 N NZ  . LYS A 272 ? 0.9502 1.3751 0.8359 -0.1392 -0.1249 -0.0730 272 LYS A NZ  
2160 N N   . THR A 273 ? 0.7529 1.0004 0.6180 -0.0114 -0.1049 0.0029  273 THR A N   
2161 C CA  . THR A 273 ? 0.7539 1.0056 0.6244 0.0018  -0.0978 0.0072  273 THR A CA  
2162 C C   . THR A 273 ? 0.7372 0.9258 0.5970 0.0155  -0.0887 0.0179  273 THR A C   
2163 O O   . THR A 273 ? 0.7691 0.9125 0.6198 0.0106  -0.0882 0.0207  273 THR A O   
2164 C CB  . THR A 273 ? 0.7752 1.0395 0.6561 -0.0265 -0.0973 -0.0040 273 THR A CB  
2165 O OG1 . THR A 273 ? 0.7469 0.9510 0.6206 -0.0445 -0.0944 -0.0038 273 THR A OG1 
2166 C CG2 . THR A 273 ? 0.6831 0.9954 0.5712 -0.0507 -0.1041 -0.0179 273 THR A CG2 
2167 N N   . GLU A 274 ? 0.8703 1.0566 0.7318 0.0299  -0.0806 0.0218  274 GLU A N   
2168 C CA  . GLU A 274 ? 0.9476 1.0755 0.7991 0.0379  -0.0701 0.0285  274 GLU A CA  
2169 C C   . GLU A 274 ? 0.9241 1.0309 0.7806 0.0166  -0.0672 0.0218  274 GLU A C   
2170 O O   . GLU A 274 ? 0.9500 1.0196 0.8003 0.0228  -0.0578 0.0244  274 GLU A O   
2171 C CB  . GLU A 274 ? 0.9555 1.0828 0.7991 0.0726  -0.0598 0.0385  274 GLU A CB  
2172 C CG  . GLU A 274 ? 0.9659 1.1347 0.8057 0.0990  -0.0633 0.0453  274 GLU A CG  
2173 C CD  . GLU A 274 ? 1.1006 1.2549 0.9261 0.1371  -0.0505 0.0577  274 GLU A CD  
2174 O OE1 . GLU A 274 ? 1.1685 1.2737 0.9744 0.1513  -0.0417 0.0677  274 GLU A OE1 
2175 O OE2 . GLU A 274 ? 1.1226 1.3125 0.9548 0.1530  -0.0478 0.0573  274 GLU A OE2 
2176 N N   . GLU A 275 ? 0.8514 0.9793 0.7163 -0.0090 -0.0740 0.0128  275 GLU A N   
2177 C CA  . GLU A 275 ? 0.8063 0.9181 0.6729 -0.0272 -0.0710 0.0078  275 GLU A CA  
2178 C C   . GLU A 275 ? 0.7926 0.8530 0.6505 -0.0414 -0.0719 0.0075  275 GLU A C   
2179 O O   . GLU A 275 ? 0.8065 0.8521 0.6602 -0.0467 -0.0772 0.0078  275 GLU A O   
2180 C CB  . GLU A 275 ? 0.8114 0.9626 0.6865 -0.0494 -0.0753 -0.0012 275 GLU A CB  
2181 C CG  . GLU A 275 ? 0.8425 1.0554 0.7296 -0.0380 -0.0743 -0.0038 275 GLU A CG  
2182 C CD  . GLU A 275 ? 0.9309 1.1899 0.8262 -0.0617 -0.0799 -0.0147 275 GLU A CD  
2183 O OE1 . GLU A 275 ? 0.9541 1.2736 0.8601 -0.0522 -0.0826 -0.0184 275 GLU A OE1 
2184 O OE2 . GLU A 275 ? 0.9501 1.1846 0.8396 -0.0899 -0.0809 -0.0200 275 GLU A OE2 
2185 N N   . GLY A 276 ? 0.8375 0.8743 0.6927 -0.0466 -0.0666 0.0061  276 GLY A N   
2186 C CA  . GLY A 276 ? 0.7877 0.7878 0.6357 -0.0615 -0.0689 0.0042  276 GLY A CA  
2187 C C   . GLY A 276 ? 0.7933 0.8000 0.6393 -0.0838 -0.0746 0.0000  276 GLY A C   
2188 O O   . GLY A 276 ? 0.8363 0.8759 0.6874 -0.0917 -0.0754 -0.0032 276 GLY A O   
2189 N N   . LYS A 277 ? 0.7477 0.7222 0.5845 -0.0940 -0.0774 -0.0004 277 LYS A N   
2190 C CA  . LYS A 277 ? 0.7539 0.7223 0.5823 -0.1134 -0.0807 -0.0027 277 LYS A CA  
2191 C C   . LYS A 277 ? 0.8154 0.7495 0.6317 -0.1170 -0.0816 -0.0014 277 LYS A C   
2192 O O   . LYS A 277 ? 0.7572 0.6723 0.5726 -0.1085 -0.0839 -0.0004 277 LYS A O   
2193 C CB  . LYS A 277 ? 0.7805 0.7501 0.6072 -0.1196 -0.0858 -0.0044 277 LYS A CB  
2194 C CG  . LYS A 277 ? 0.8093 0.7647 0.6231 -0.1406 -0.0862 -0.0074 277 LYS A CG  
2195 C CD  . LYS A 277 ? 0.7971 0.7848 0.6146 -0.1560 -0.0819 -0.0127 277 LYS A CD  
2196 C CE  . LYS A 277 ? 0.8345 0.7987 0.6341 -0.1794 -0.0784 -0.0156 277 LYS A CE  
2197 N NZ  . LYS A 277 ? 0.9199 0.9156 0.7226 -0.1980 -0.0716 -0.0220 277 LYS A NZ  
2198 N N   . LEU A 278 ? 0.7511 0.6809 0.5578 -0.1289 -0.0793 -0.0016 278 LEU A N   
2199 C CA  . LEU A 278 ? 0.6892 0.5906 0.4805 -0.1310 -0.0807 0.0007  278 LEU A CA  
2200 C C   . LEU A 278 ? 0.7239 0.6015 0.4985 -0.1416 -0.0830 0.0027  278 LEU A C   
2201 O O   . LEU A 278 ? 0.7160 0.5976 0.4848 -0.1568 -0.0792 0.0013  278 LEU A O   
2202 C CB  . LEU A 278 ? 0.7003 0.6077 0.4863 -0.1357 -0.0755 0.0006  278 LEU A CB  
2203 C CG  . LEU A 278 ? 0.7143 0.5977 0.4819 -0.1359 -0.0772 0.0035  278 LEU A CG  
2204 C CD1 . LEU A 278 ? 0.6990 0.5788 0.4715 -0.1228 -0.0804 0.0010  278 LEU A CD1 
2205 C CD2 . LEU A 278 ? 0.7628 0.6531 0.5210 -0.1446 -0.0709 0.0039  278 LEU A CD2 
2206 N N   . LEU A 279 ? 0.7554 0.6079 0.5211 -0.1340 -0.0879 0.0050  279 LEU A N   
2207 C CA  . LEU A 279 ? 0.7440 0.5664 0.4900 -0.1393 -0.0891 0.0077  279 LEU A CA  
2208 C C   . LEU A 279 ? 0.7688 0.5679 0.4947 -0.1334 -0.0902 0.0130  279 LEU A C   
2209 O O   . LEU A 279 ? 0.7546 0.5615 0.4862 -0.1213 -0.0941 0.0125  279 LEU A O   
2210 C CB  . LEU A 279 ? 0.7171 0.5316 0.4678 -0.1315 -0.0941 0.0061  279 LEU A CB  
2211 C CG  . LEU A 279 ? 0.7350 0.5704 0.5010 -0.1350 -0.0942 0.0016  279 LEU A CG  
2212 C CD1 . LEU A 279 ? 0.6940 0.5144 0.4586 -0.1275 -0.0986 0.0006  279 LEU A CD1 
2213 C CD2 . LEU A 279 ? 0.7294 0.5722 0.4901 -0.1541 -0.0892 -0.0016 279 LEU A CD2 
2214 N N   . LEU A 280 ? 0.9389 0.7098 0.6396 -0.1422 -0.0858 0.0177  280 LEU A N   
2215 C CA  . LEU A 280 ? 0.9601 0.7048 0.6347 -0.1345 -0.0860 0.0252  280 LEU A CA  
2216 C C   . LEU A 280 ? 0.9827 0.6847 0.6309 -0.1328 -0.0842 0.0302  280 LEU A C   
2217 O O   . LEU A 280 ? 1.0558 0.7431 0.6986 -0.1477 -0.0780 0.0276  280 LEU A O   
2218 C CB  . LEU A 280 ? 0.9382 0.6831 0.5993 -0.1460 -0.0784 0.0283  280 LEU A CB  
2219 C CG  . LEU A 280 ? 0.9767 0.7568 0.6558 -0.1439 -0.0792 0.0245  280 LEU A CG  
2220 C CD1 . LEU A 280 ? 0.9697 0.7723 0.6591 -0.1611 -0.0709 0.0204  280 LEU A CD1 
2221 C CD2 . LEU A 280 ? 0.9514 0.7220 0.6097 -0.1352 -0.0804 0.0302  280 LEU A CD2 
2222 N N   . SER A 281 ? 0.9602 0.6432 0.5904 -0.1141 -0.0888 0.0367  281 SER A N   
2223 C CA  . SER A 281 ? 0.9692 0.6062 0.5694 -0.1079 -0.0856 0.0430  281 SER A CA  
2224 C C   . SER A 281 ? 0.9984 0.6202 0.5743 -0.0844 -0.0900 0.0524  281 SER A C   
2225 O O   . SER A 281 ? 0.9735 0.6287 0.5652 -0.0699 -0.0995 0.0501  281 SER A O   
2226 C CB  . SER A 281 ? 0.9814 0.6166 0.5946 -0.1031 -0.0894 0.0371  281 SER A CB  
2227 O OG  . SER A 281 ? 1.0341 0.6219 0.6160 -0.0937 -0.0856 0.0430  281 SER A OG  
2228 N N   . GLN A 282 ? 1.2348 0.8058 0.7707 -0.0807 -0.0822 0.0624  282 GLN A N   
2229 C CA  . GLN A 282 ? 1.3010 0.8517 0.8064 -0.0538 -0.0855 0.0738  282 GLN A CA  
2230 C C   . GLN A 282 ? 1.2779 0.8314 0.7895 -0.0297 -0.0944 0.0720  282 GLN A C   
2231 O O   . GLN A 282 ? 1.2710 0.8067 0.7869 -0.0347 -0.0913 0.0674  282 GLN A O   
2232 C CB  . GLN A 282 ? 1.2877 0.7743 0.7432 -0.0570 -0.0711 0.0864  282 GLN A CB  
2233 C CG  . GLN A 282 ? 1.4375 0.9148 0.8919 -0.0911 -0.0580 0.0829  282 GLN A CG  
2234 C CD  . GLN A 282 ? 1.4615 0.9778 0.9300 -0.1004 -0.0597 0.0816  282 GLN A CD  
2235 O OE1 . GLN A 282 ? 1.3861 0.9246 0.8746 -0.1260 -0.0543 0.0735  282 GLN A OE1 
2236 N NE2 . GLN A 282 ? 1.4839 1.0075 0.9384 -0.0797 -0.0658 0.0896  282 GLN A NE2 
2237 N N   . LEU A 283 ? 1.0116 0.5908 0.5234 -0.0038 -0.1051 0.0745  283 LEU A N   
2238 C CA  . LEU A 283 ? 1.0077 0.5952 0.5243 0.0215  -0.1135 0.0726  283 LEU A CA  
2239 C C   . LEU A 283 ? 1.0398 0.6188 0.5233 0.0538  -0.1178 0.0845  283 LEU A C   
2240 O O   . LEU A 283 ? 1.0513 0.6438 0.5233 0.0569  -0.1198 0.0897  283 LEU A O   
2241 C CB  . LEU A 283 ? 0.9330 0.5820 0.4954 0.0212  -0.1245 0.0582  283 LEU A CB  
2242 C CG  . LEU A 283 ? 0.9311 0.5966 0.5276 -0.0050 -0.1217 0.0471  283 LEU A CG  
2243 C CD1 . LEU A 283 ? 0.8540 0.5699 0.4870 -0.0006 -0.1303 0.0349  283 LEU A CD1 
2244 C CD2 . LEU A 283 ? 0.9635 0.5892 0.5511 -0.0138 -0.1140 0.0474  283 LEU A CD2 
2245 N N   . ASP A 284 ? 1.2054 0.7652 0.6734 0.0798  -0.1197 0.0884  284 ASP A N   
2246 C CA  . ASP A 284 ? 1.2132 0.7790 0.6551 0.1172  -0.1268 0.0983  284 ASP A CA  
2247 C C   . ASP A 284 ? 1.1433 0.7886 0.6218 0.1279  -0.1427 0.0861  284 ASP A C   
2248 O O   . ASP A 284 ? 1.1186 0.8010 0.6364 0.1199  -0.1478 0.0714  284 ASP A O   
2249 C CB  . ASP A 284 ? 1.2824 0.8056 0.6976 0.1443  -0.1231 0.1053  284 ASP A CB  
2250 C CG  . ASP A 284 ? 1.3651 0.8012 0.7308 0.1392  -0.1051 0.1193  284 ASP A CG  
2251 O OD1 . ASP A 284 ? 1.3467 0.7571 0.6893 0.1239  -0.0967 0.1277  284 ASP A OD1 
2252 O OD2 . ASP A 284 ? 1.4702 0.8627 0.8193 0.1492  -0.0980 0.1207  284 ASP A OD2 
2253 N N   . SER A 285 ? 1.0954 0.7665 0.5585 0.1455  -0.1496 0.0917  285 SER A N   
2254 C CA  . SER A 285 ? 1.0303 0.7794 0.5244 0.1552  -0.1640 0.0782  285 SER A CA  
2255 C C   . SER A 285 ? 1.0165 0.7934 0.5230 0.1817  -0.1720 0.0720  285 SER A C   
2256 O O   . SER A 285 ? 0.9721 0.8093 0.5194 0.1753  -0.1797 0.0542  285 SER A O   
2257 C CB  . SER A 285 ? 1.0408 0.8110 0.5093 0.1724  -0.1698 0.0861  285 SER A CB  
2258 O OG  . SER A 285 ? 1.0714 0.8234 0.5326 0.1461  -0.1622 0.0895  285 SER A OG  
2259 N N   . HIS A 286 ? 1.0994 0.8340 0.5691 0.2128  -0.1694 0.0863  286 HIS A N   
2260 C CA  . HIS A 286 ? 1.1307 0.8866 0.6080 0.2419  -0.1756 0.0818  286 HIS A CA  
2261 C C   . HIS A 286 ? 1.1556 0.8379 0.6094 0.2468  -0.1636 0.0905  286 HIS A C   
2262 O O   . HIS A 286 ? 1.2210 0.8509 0.6272 0.2759  -0.1579 0.1078  286 HIS A O   
2263 C CB  . HIS A 286 ? 1.1194 0.9094 0.5727 0.2859  -0.1864 0.0894  286 HIS A CB  
2264 C CG  . HIS A 286 ? 1.1528 1.0165 0.6251 0.2813  -0.1980 0.0796  286 HIS A CG  
2265 N ND1 . HIS A 286 ? 1.0972 1.0455 0.6150 0.2764  -0.2090 0.0574  286 HIS A ND1 
2266 C CD2 . HIS A 286 ? 1.1068 0.9722 0.5565 0.2800  -0.1992 0.0878  286 HIS A CD2 
2267 C CE1 . HIS A 286 ? 1.0201 1.0188 0.5433 0.2711  -0.2165 0.0511  286 HIS A CE1 
2268 N NE2 . HIS A 286 ? 1.0890 1.0396 0.5716 0.2741  -0.2113 0.0696  286 HIS A NE2 
2269 N N   . PRO A 287 ? 1.1512 0.8262 0.6347 0.2195  -0.1585 0.0788  287 PRO A N   
2270 C CA  . PRO A 287 ? 1.2106 0.8171 0.6733 0.2190  -0.1461 0.0838  287 PRO A CA  
2271 C C   . PRO A 287 ? 1.2490 0.8462 0.6951 0.2590  -0.1474 0.0869  287 PRO A C   
2272 O O   . PRO A 287 ? 1.2298 0.8892 0.6947 0.2847  -0.1596 0.0800  287 PRO A O   
2273 C CB  . PRO A 287 ? 1.1132 0.7372 0.6190 0.1830  -0.1443 0.0675  287 PRO A CB  
2274 C CG  . PRO A 287 ? 1.0538 0.7400 0.5967 0.1627  -0.1525 0.0568  287 PRO A CG  
2275 C CD  . PRO A 287 ? 1.0418 0.7714 0.5770 0.1886  -0.1631 0.0600  287 PRO A CD  
2276 N N   . SER A 288 ? 1.5678 1.0878 0.9787 0.2636  -0.1336 0.0957  288 SER A N   
2277 C CA  . SER A 288 ? 1.5647 1.0809 0.9683 0.2979  -0.1342 0.0945  288 SER A CA  
2278 C C   . SER A 288 ? 1.5781 1.1142 1.0216 0.2761  -0.1337 0.0766  288 SER A C   
2279 O O   . SER A 288 ? 1.5388 1.0658 1.0021 0.2361  -0.1286 0.0688  288 SER A O   
2280 C CB  . SER A 288 ? 1.6827 1.1082 1.0242 0.3270  -0.1195 0.1121  288 SER A CB  
2281 O OG  . SER A 288 ? 1.8259 1.1960 1.1149 0.3413  -0.1115 0.1321  288 SER A OG  
2282 N N   . HIS A 289 ? 1.8940 1.4699 1.3516 0.3055  -0.1407 0.0699  289 HIS A N   
2283 C CA  . HIS A 289 ? 1.8731 1.4614 1.3552 0.3028  -0.1392 0.0561  289 HIS A CA  
2284 C C   . HIS A 289 ? 1.9378 1.4595 1.3760 0.3357  -0.1284 0.0654  289 HIS A C   
2285 O O   . HIS A 289 ? 1.8747 1.3905 1.2823 0.3792  -0.1306 0.0772  289 HIS A O   
2286 C CB  . HIS A 289 ? 1.7898 1.4740 1.3140 0.3162  -0.1541 0.0428  289 HIS A CB  
2287 C CG  . HIS A 289 ? 1.8069 1.5462 1.3587 0.2930  -0.1632 0.0378  289 HIS A CG  
2288 N ND1 . HIS A 289 ? 1.8015 1.6179 1.3722 0.3106  -0.1763 0.0316  289 HIS A ND1 
2289 C CD2 . HIS A 289 ? 1.7589 1.4878 1.3218 0.2537  -0.1602 0.0368  289 HIS A CD2 
2290 C CE1 . HIS A 289 ? 1.7178 1.5650 1.3097 0.2811  -0.1801 0.0262  289 HIS A CE1 
2291 N NE2 . HIS A 289 ? 1.7219 1.5161 1.3091 0.2480  -0.1705 0.0301  289 HIS A NE2 
2292 N N   . SER A 290 ? 1.8445 1.3148 1.2772 0.3152  -0.1160 0.0601  290 SER A N   
2293 C CA  . SER A 290 ? 1.8218 1.2384 1.2232 0.3420  -0.1052 0.0622  290 SER A CA  
2294 C C   . SER A 290 ? 1.8082 1.2930 1.2392 0.3725  -0.1155 0.0513  290 SER A C   
2295 O O   . SER A 290 ? 1.7599 1.3308 1.2364 0.3663  -0.1294 0.0406  290 SER A O   
2296 C CB  . SER A 290 ? 1.9590 1.3199 1.3562 0.3053  -0.0910 0.0541  290 SER A CB  
2297 O OG  . SER A 290 ? 1.9426 1.3535 1.3870 0.2634  -0.0976 0.0408  290 SER A OG  
2298 N N   . ALA A 291 ? 1.4712 0.9171 0.8749 0.4055  -0.1071 0.0532  291 ALA A N   
2299 C CA  . ALA A 291 ? 1.4315 0.9430 0.8643 0.4331  -0.1151 0.0411  291 ALA A CA  
2300 C C   . ALA A 291 ? 1.3774 0.9504 0.8668 0.3935  -0.1208 0.0210  291 ALA A C   
2301 O O   . ALA A 291 ? 1.3685 0.9083 0.8634 0.3528  -0.1133 0.0160  291 ALA A O   
2302 C CB  . ALA A 291 ? 1.5067 0.9576 0.9040 0.4651  -0.1017 0.0429  291 ALA A CB  
2303 N N   . VAL A 292 ? 1.4560 1.1211 0.9862 0.4051  -0.1335 0.0094  292 VAL A N   
2304 C CA  . VAL A 292 ? 1.4638 1.1839 1.0437 0.3704  -0.1364 -0.0091 292 VAL A CA  
2305 C C   . VAL A 292 ? 1.4815 1.1635 1.0569 0.3655  -0.1249 -0.0172 292 VAL A C   
2306 O O   . VAL A 292 ? 1.5082 1.1424 1.0499 0.3970  -0.1167 -0.0123 292 VAL A O   
2307 C CB  . VAL A 292 ? 1.4260 1.2501 1.0481 0.3824  -0.1492 -0.0222 292 VAL A CB  
2308 C CG1 . VAL A 292 ? 1.3492 1.2198 1.0178 0.3425  -0.1488 -0.0402 292 VAL A CG1 
2309 C CG2 . VAL A 292 ? 1.3523 1.2131 0.9757 0.3867  -0.1602 -0.0156 292 VAL A CG2 
2310 N N   . VAL A 293 ? 1.2703 0.9712 0.8771 0.3264  -0.1233 -0.0294 293 VAL A N   
2311 C CA  . VAL A 293 ? 1.2431 0.9083 0.8461 0.3134  -0.1126 -0.0376 293 VAL A CA  
2312 C C   . VAL A 293 ? 1.2530 0.9869 0.8920 0.3211  -0.1154 -0.0538 293 VAL A C   
2313 O O   . VAL A 293 ? 1.1809 0.9879 0.8576 0.3107  -0.1239 -0.0617 293 VAL A O   
2314 C CB  . VAL A 293 ? 1.2504 0.8876 0.8593 0.2655  -0.1082 -0.0390 293 VAL A CB  
2315 C CG1 . VAL A 293 ? 1.2254 0.8355 0.8322 0.2509  -0.0983 -0.0495 293 VAL A CG1 
2316 C CG2 . VAL A 293 ? 1.2402 0.8135 0.8139 0.2570  -0.1043 -0.0244 293 VAL A CG2 
2317 N N   . ASN A 294 ? 1.2437 0.9544 0.8688 0.3415  -0.1071 -0.0592 294 ASN A N   
2318 C CA  . ASN A 294 ? 1.1979 0.9620 0.8543 0.3409  -0.1059 -0.0760 294 ASN A CA  
2319 C C   . ASN A 294 ? 1.2311 0.9647 0.8916 0.3005  -0.0978 -0.0824 294 ASN A C   
2320 O O   . ASN A 294 ? 1.2443 0.9161 0.8763 0.3009  -0.0874 -0.0828 294 ASN A O   
2321 C CB  . ASN A 294 ? 1.2146 0.9726 0.8531 0.3868  -0.1011 -0.0787 294 ASN A CB  
2322 C CG  . ASN A 294 ? 1.2224 1.0523 0.8971 0.3915  -0.1010 -0.0969 294 ASN A CG  
2323 O OD1 . ASN A 294 ? 1.2226 1.0971 0.9321 0.3574  -0.1022 -0.1073 294 ASN A OD1 
2324 N ND2 . ASN A 294 ? 1.2289 1.0664 0.8925 0.4348  -0.0978 -0.1004 294 ASN A ND2 
2325 N N   . TRP A 295 ? 1.1334 0.9114 0.8278 0.2662  -0.1018 -0.0883 295 TRP A N   
2326 C CA  . TRP A 295 ? 1.1196 0.8710 0.8157 0.2282  -0.0961 -0.0913 295 TRP A CA  
2327 C C   . TRP A 295 ? 1.1359 0.8820 0.8317 0.2276  -0.0871 -0.1032 295 TRP A C   
2328 O O   . TRP A 295 ? 1.0900 0.8050 0.7781 0.2013  -0.0815 -0.1054 295 TRP A O   
2329 C CB  . TRP A 295 ? 1.0268 0.8266 0.7566 0.1972  -0.1013 -0.0934 295 TRP A CB  
2330 C CG  . TRP A 295 ? 1.0495 0.8353 0.7744 0.1841  -0.1072 -0.0820 295 TRP A CG  
2331 C CD1 . TRP A 295 ? 1.0540 0.8810 0.7949 0.1881  -0.1155 -0.0793 295 TRP A CD1 
2332 C CD2 . TRP A 295 ? 1.0372 0.7676 0.7402 0.1639  -0.1046 -0.0732 295 TRP A CD2 
2333 N NE1 . TRP A 295 ? 1.0362 0.8337 0.7654 0.1728  -0.1180 -0.0683 295 TRP A NE1 
2334 C CE2 . TRP A 295 ? 1.0738 0.8134 0.7806 0.1577  -0.1113 -0.0645 295 TRP A CE2 
2335 C CE3 . TRP A 295 ? 1.0491 0.7266 0.7299 0.1491  -0.0968 -0.0736 295 TRP A CE3 
2336 C CZ2 . TRP A 295 ? 1.0367 0.7349 0.7267 0.1382  -0.1102 -0.0555 295 TRP A CZ2 
2337 C CZ3 . TRP A 295 ? 1.0231 0.6627 0.6882 0.1283  -0.0959 -0.0658 295 TRP A CZ3 
2338 C CH2 . TRP A 295 ? 1.0391 0.6894 0.7093 0.1234  -0.1024 -0.0566 295 TRP A CH2 
2339 N N   . THR A 296 ? 1.1776 0.9579 0.8820 0.2558  -0.0858 -0.1117 296 THR A N   
2340 C CA  . THR A 296 ? 1.1672 0.9451 0.8709 0.2574  -0.0767 -0.1237 296 THR A CA  
2341 C C   . THR A 296 ? 1.2537 0.9839 0.9236 0.2927  -0.0693 -0.1239 296 THR A C   
2342 O O   . THR A 296 ? 1.2578 0.9795 0.9227 0.2962  -0.0604 -0.1346 296 THR A O   
2343 C CB  . THR A 296 ? 1.1509 1.0091 0.8928 0.2588  -0.0778 -0.1364 296 THR A CB  
2344 O OG1 . THR A 296 ? 1.1870 1.0426 0.9280 0.2558  -0.0680 -0.1480 296 THR A OG1 
2345 C CG2 . THR A 296 ? 1.1244 1.0281 0.8750 0.2977  -0.0834 -0.1381 296 THR A CG2 
2346 N N   . SER A 297 ? 1.3469 1.0417 0.9905 0.3192  -0.0713 -0.1120 297 SER A N   
2347 C CA  . SER A 297 ? 1.3877 1.0347 0.9955 0.3589  -0.0629 -0.1105 297 SER A CA  
2348 C C   . SER A 297 ? 1.4514 1.0246 1.0284 0.3433  -0.0487 -0.1160 297 SER A C   
2349 O O   . SER A 297 ? 1.4634 1.0365 1.0377 0.3552  -0.0404 -0.1280 297 SER A O   
2350 C CB  . SER A 297 ? 1.3550 0.9663 0.9336 0.3858  -0.0663 -0.0936 297 SER A CB  
2351 O OG  . SER A 297 ? 1.3857 0.9637 0.9323 0.4338  -0.0591 -0.0908 297 SER A OG  
2352 N N   . TYR A 298 ? 1.4133 0.9270 0.9673 0.3150  -0.0452 -0.1092 298 TYR A N   
2353 C CA  . TYR A 298 ? 1.3587 0.8053 0.8827 0.2967  -0.0313 -0.1169 298 TYR A CA  
2354 C C   . TYR A 298 ? 1.3835 0.8708 0.9338 0.2729  -0.0303 -0.1324 298 TYR A C   
2355 O O   . TYR A 298 ? 1.4229 0.8928 0.9605 0.2836  -0.0201 -0.1441 298 TYR A O   
2356 C CB  . TYR A 298 ? 1.3733 0.7651 0.8755 0.2637  -0.0287 -0.1093 298 TYR A CB  
2357 C CG  . TYR A 298 ? 1.4471 0.7712 0.9171 0.2401  -0.0137 -0.1195 298 TYR A CG  
2358 C CD1 . TYR A 298 ? 1.4474 0.7936 0.9319 0.2166  -0.0112 -0.1352 298 TYR A CD1 
2359 C CD2 . TYR A 298 ? 1.4849 0.7225 0.9075 0.2407  -0.0008 -0.1143 298 TYR A CD2 
2360 C CE1 . TYR A 298 ? 1.4347 0.7249 0.8899 0.1941  0.0022  -0.1469 298 TYR A CE1 
2361 C CE2 . TYR A 298 ? 1.5428 0.7201 0.9356 0.2155  0.0145  -0.1267 298 TYR A CE2 
2362 C CZ  . TYR A 298 ? 1.4906 0.6977 0.9011 0.1922  0.0151  -0.1438 298 TYR A CZ  
2363 O OH  . TYR A 298 ? 1.4735 0.6271 0.8550 0.1660  0.0298  -0.1584 298 TYR A OH  
2364 N N   . ALA A 299 ? 1.5194 1.0629 1.1057 0.2436  -0.0402 -0.1325 299 ALA A N   
2365 C CA  . ALA A 299 ? 1.4789 1.0554 1.0852 0.2191  -0.0382 -0.1450 299 ALA A CA  
2366 C C   . ALA A 299 ? 1.4818 1.0943 1.0998 0.2447  -0.0338 -0.1564 299 ALA A C   
2367 O O   . ALA A 299 ? 1.4751 1.0839 1.0893 0.2353  -0.0259 -0.1686 299 ALA A O   
2368 C CB  . ALA A 299 ? 1.3822 1.0132 1.0232 0.1909  -0.0484 -0.1409 299 ALA A CB  
2369 N N   . SER A 300 ? 1.2893 0.9408 0.9216 0.2776  -0.0389 -0.1536 300 SER A N   
2370 C CA  . SER A 300 ? 1.2646 0.9533 0.9075 0.3057  -0.0341 -0.1653 300 SER A CA  
2371 C C   . SER A 300 ? 1.3340 0.9596 0.9373 0.3363  -0.0221 -0.1688 300 SER A C   
2372 O O   . SER A 300 ? 1.3048 0.9526 0.9121 0.3595  -0.0157 -0.1802 300 SER A O   
2373 C CB  . SER A 300 ? 1.1835 0.9432 0.8560 0.3308  -0.0436 -0.1632 300 SER A CB  
2374 O OG  . SER A 300 ? 1.1369 0.9675 0.8500 0.3051  -0.0481 -0.1696 300 SER A OG  
2375 N N   . SER A 301 ? 1.4410 0.9876 1.0051 0.3369  -0.0174 -0.1599 301 SER A N   
2376 C CA  . SER A 301 ? 1.4501 0.9240 0.9701 0.3644  -0.0029 -0.1628 301 SER A CA  
2377 C C   . SER A 301 ? 1.5554 0.9755 1.0514 0.3368  0.0106  -0.1759 301 SER A C   
2378 O O   . SER A 301 ? 1.6097 0.9694 1.0690 0.3582  0.0252  -0.1818 301 SER A O   
2379 C CB  . SER A 301 ? 1.5789 0.9876 1.0624 0.3820  -0.0013 -0.1464 301 SER A CB  
2380 O OG  . SER A 301 ? 1.6323 0.9619 1.0815 0.3507  0.0089  -0.1465 301 SER A OG  
2381 N N   . ILE A 302 ? 1.7742 1.3572 1.2702 0.5776  0.0007  -0.2013 302 ILE A N   
2382 C CA  . ILE A 302 ? 1.8479 1.3692 1.3011 0.5631  0.0108  -0.2138 302 ILE A CA  
2383 C C   . ILE A 302 ? 1.8233 1.3992 1.2848 0.5522  0.0362  -0.2399 302 ILE A C   
2384 O O   . ILE A 302 ? 1.7828 1.4402 1.2801 0.5471  0.0462  -0.2450 302 ILE A O   
2385 C CB  . ILE A 302 ? 1.8672 1.3328 1.2819 0.5184  0.0025  -0.1933 302 ILE A CB  
2386 C CG1 . ILE A 302 ? 1.7274 1.2186 1.1557 0.4894  -0.0095 -0.1658 302 ILE A CG1 
2387 C CG2 . ILE A 302 ? 1.9589 1.3271 1.3326 0.5263  -0.0081 -0.1899 302 ILE A CG2 
2388 C CD1 . ILE A 302 ? 1.8098 1.3576 1.2778 0.5050  -0.0169 -0.1556 302 ILE A CD1 
2389 N N   . GLU A 303 ? 1.6858 1.2156 1.1114 0.5471  0.0478  -0.2581 303 GLU A N   
2390 C CA  . GLU A 303 ? 1.7430 1.3057 1.1566 0.5188  0.0696  -0.2749 303 GLU A CA  
2391 C C   . GLU A 303 ? 1.7417 1.2601 1.1146 0.4736  0.0621  -0.2565 303 GLU A C   
2392 O O   . GLU A 303 ? 1.7340 1.1950 1.0890 0.4671  0.0431  -0.2370 303 GLU A O   
2393 C CB  . GLU A 303 ? 1.7335 1.2850 1.1348 0.5414  0.0891  -0.3101 303 GLU A CB  
2394 C CG  . GLU A 303 ? 1.7457 1.3805 1.1972 0.5730  0.1047  -0.3333 303 GLU A CG  
2395 C CD  . GLU A 303 ? 1.8769 1.4932 1.3409 0.6176  0.1089  -0.3576 303 GLU A CD  
2396 O OE1 . GLU A 303 ? 1.9547 1.5175 1.3865 0.6098  0.1167  -0.3709 303 GLU A OE1 
2397 O OE2 . GLU A 303 ? 1.8174 1.4788 1.3311 0.6521  0.1019  -0.3584 303 GLU A OE2 
2398 N N   . ALA A 304 ? 1.6733 1.2192 1.0307 0.4422  0.0770  -0.2630 304 ALA A N   
2399 C CA  . ALA A 304 ? 1.6603 1.1792 0.9867 0.4009  0.0675  -0.2432 304 ALA A CA  
2400 C C   . ALA A 304 ? 1.7123 1.1492 0.9971 0.3954  0.0549  -0.2420 304 ALA A C   
2401 O O   . ALA A 304 ? 1.7969 1.1991 1.0559 0.4066  0.0642  -0.2650 304 ALA A O   
2402 C CB  . ALA A 304 ? 1.6677 1.2205 0.9749 0.3719  0.0859  -0.2524 304 ALA A CB  
2403 N N   . LEU A 305 ? 1.4470 0.8546 0.7260 0.3761  0.0349  -0.2171 305 LEU A N   
2404 C CA  . LEU A 305 ? 1.4831 0.8175 0.7250 0.3655  0.0227  -0.2160 305 LEU A CA  
2405 C C   . LEU A 305 ? 1.5622 0.8813 0.7623 0.3368  0.0280  -0.2271 305 LEU A C   
2406 O O   . LEU A 305 ? 1.5964 0.8581 0.7620 0.3292  0.0225  -0.2355 305 LEU A O   
2407 C CB  . LEU A 305 ? 1.4708 0.7873 0.7211 0.3497  0.0018  -0.1884 305 LEU A CB  
2408 C CG  . LEU A 305 ? 1.4233 0.7500 0.7079 0.3708  -0.0076 -0.1720 305 LEU A CG  
2409 C CD1 . LEU A 305 ? 1.4055 0.7007 0.6854 0.3491  -0.0258 -0.1497 305 LEU A CD1 
2410 C CD2 . LEU A 305 ? 1.4731 0.7700 0.7591 0.4109  -0.0049 -0.1844 305 LEU A CD2 
2411 N N   . SER A 306 ? 1.7558 1.1232 0.9551 0.3193  0.0382  -0.2272 306 SER A N   
2412 C CA  . SER A 306 ? 1.7312 1.0878 0.8866 0.2921  0.0423  -0.2357 306 SER A CA  
2413 C C   . SER A 306 ? 1.7260 1.1359 0.8815 0.2882  0.0645  -0.2467 306 SER A C   
2414 O O   . SER A 306 ? 1.7233 1.1844 0.9164 0.2973  0.0728  -0.2413 306 SER A O   
2415 C CB  . SER A 306 ? 1.7333 1.0797 0.8765 0.2607  0.0218  -0.2121 306 SER A CB  
2416 O OG  . SER A 306 ? 1.6701 1.0630 0.8428 0.2528  0.0197  -0.1912 306 SER A OG  
2417 N N   . SER A 307 ? 2.0812 1.4792 1.1919 0.2721  0.0749  -0.2632 307 SER A N   
2418 C CA  . SER A 307 ? 2.1049 1.5473 1.2066 0.2659  0.0998  -0.2779 307 SER A CA  
2419 C C   . SER A 307 ? 2.1758 1.5999 1.2189 0.2328  0.0993  -0.2786 307 SER A C   
2420 O O   . SER A 307 ? 2.2000 1.5763 1.2084 0.2233  0.0855  -0.2816 307 SER A O   
2421 C CB  . SER A 307 ? 2.1170 1.5720 1.2306 0.2957  0.1232  -0.3111 307 SER A CB  
2422 O OG  . SER A 307 ? 2.1725 1.6805 1.3416 0.3190  0.1312  -0.3100 307 SER A OG  
2423 N N   . GLY A 308 ? 1.8277 1.2897 0.8574 0.2142  0.1149  -0.2766 308 GLY A N   
2424 C CA  . GLY A 308 ? 1.7434 1.1898 0.7150 0.1812  0.1112  -0.2698 308 GLY A CA  
2425 C C   . GLY A 308 ? 1.7749 1.1943 0.7374 0.1646  0.0793  -0.2398 308 GLY A C   
2426 O O   . GLY A 308 ? 1.8188 1.2039 0.7359 0.1482  0.0650  -0.2400 308 GLY A O   
2427 N N   . ASN A 309 ? 1.9218 1.3585 0.9285 0.1692  0.0673  -0.2159 309 ASN A N   
2428 C CA  . ASN A 309 ? 1.8637 1.2815 0.8682 0.1549  0.0386  -0.1887 309 ASN A CA  
2429 C C   . ASN A 309 ? 1.8681 1.2902 0.8323 0.1284  0.0363  -0.1726 309 ASN A C   
2430 O O   . ASN A 309 ? 1.8102 1.2554 0.7580 0.1195  0.0586  -0.1768 309 ASN A O   
2431 C CB  . ASN A 309 ? 1.8537 1.2892 0.9163 0.1672  0.0288  -0.1699 309 ASN A CB  
2432 C CG  . ASN A 309 ? 1.9014 1.3337 1.0021 0.1951  0.0321  -0.1827 309 ASN A CG  
2433 O OD1 . ASN A 309 ? 1.9058 1.3002 0.9988 0.2009  0.0201  -0.1893 309 ASN A OD1 
2434 N ND2 . ASN A 309 ? 1.8343 1.3054 0.9755 0.2117  0.0468  -0.1849 309 ASN A ND2 
2435 N N   . LYS A 310 ? 1.7203 1.1191 0.6678 0.1157  0.0085  -0.1538 310 LYS A N   
2436 C CA  . LYS A 310 ? 1.6440 1.0429 0.5639 0.0960  -0.0014 -0.1301 310 LYS A CA  
2437 C C   . LYS A 310 ? 1.6296 1.0478 0.6015 0.1018  -0.0074 -0.1081 310 LYS A C   
2438 O O   . LYS A 310 ? 1.5815 0.9917 0.5802 0.1058  -0.0309 -0.0947 310 LYS A O   
2439 C CB  . LYS A 310 ? 1.6563 1.0253 0.5365 0.0832  -0.0303 -0.1225 310 LYS A CB  
2440 C CG  . LYS A 310 ? 1.8161 1.1665 0.6369 0.0730  -0.0237 -0.1445 310 LYS A CG  
2441 C CD  . LYS A 310 ? 1.8732 1.1989 0.6545 0.0594  -0.0548 -0.1387 310 LYS A CD  
2442 C CE  . LYS A 310 ? 1.8080 1.1334 0.5752 0.0492  -0.0773 -0.1072 310 LYS A CE  
2443 N NZ  . LYS A 310 ? 1.8182 1.1259 0.5318 0.0340  -0.1031 -0.1041 310 LYS A NZ  
2444 N N   . GLU A 311 ? 1.5429 0.9897 0.5307 0.1012  0.0158  -0.1073 311 GLU A N   
2445 C CA  . GLU A 311 ? 1.5412 1.0074 0.5722 0.1029  0.0138  -0.0885 311 GLU A CA  
2446 C C   . GLU A 311 ? 1.5714 1.0245 0.5701 0.0828  0.0069  -0.0648 311 GLU A C   
2447 O O   . GLU A 311 ? 1.6272 1.0641 0.5687 0.0666  0.0117  -0.0638 311 GLU A O   
2448 C CB  . GLU A 311 ? 1.5141 1.0213 0.5822 0.1119  0.0417  -0.1017 311 GLU A CB  
2449 C CG  . GLU A 311 ? 1.5505 1.0664 0.6474 0.1362  0.0474  -0.1246 311 GLU A CG  
2450 C CD  . GLU A 311 ? 1.5111 1.0733 0.6482 0.1495  0.0719  -0.1390 311 GLU A CD  
2451 O OE1 . GLU A 311 ? 1.4785 1.0469 0.6450 0.1741  0.0731  -0.1540 311 GLU A OE1 
2452 O OE2 . GLU A 311 ? 1.5013 1.0928 0.6399 0.1354  0.0891  -0.1356 311 GLU A OE2 
2453 N N   . PHE A 312 ? 1.5779 1.0349 0.6115 0.0843  -0.0047 -0.0454 312 PHE A N   
2454 C CA  . PHE A 312 ? 1.5717 1.0099 0.5795 0.0693  -0.0136 -0.0212 312 PHE A CA  
2455 C C   . PHE A 312 ? 1.4998 0.9554 0.5575 0.0720  -0.0106 -0.0094 312 PHE A C   
2456 O O   . PHE A 312 ? 1.4950 0.9728 0.6059 0.0864  -0.0118 -0.0161 312 PHE A O   
2457 C CB  . PHE A 312 ? 1.5241 0.9302 0.5065 0.0692  -0.0473 -0.0076 312 PHE A CB  
2458 C CG  . PHE A 312 ? 1.5049 0.9161 0.5392 0.0840  -0.0701 -0.0048 312 PHE A CG  
2459 C CD1 . PHE A 312 ? 1.4565 0.8701 0.5260 0.0870  -0.0811 0.0128  312 PHE A CD1 
2460 C CD2 . PHE A 312 ? 1.4960 0.9078 0.5422 0.0931  -0.0786 -0.0212 312 PHE A CD2 
2461 C CE1 . PHE A 312 ? 1.4134 0.8348 0.5294 0.0982  -0.0994 0.0133  312 PHE A CE1 
2462 C CE2 . PHE A 312 ? 1.4776 0.8937 0.5682 0.1026  -0.0972 -0.0192 312 PHE A CE2 
2463 C CZ  . PHE A 312 ? 1.4141 0.8376 0.5403 0.1049  -0.1071 -0.0023 312 PHE A CZ  
2464 N N   . LYS A 313 ? 1.4958 0.9371 0.5325 0.0573  -0.0076 0.0086  313 LYS A N   
2465 C CA  . LYS A 313 ? 1.4828 0.9365 0.5619 0.0569  -0.0038 0.0188  313 LYS A CA  
2466 C C   . LYS A 313 ? 1.4369 0.8689 0.5335 0.0656  -0.0342 0.0365  313 LYS A C   
2467 O O   . LYS A 313 ? 1.4259 0.8253 0.4846 0.0639  -0.0552 0.0496  313 LYS A O   
2468 C CB  . LYS A 313 ? 1.4744 0.9199 0.5221 0.0346  0.0178  0.0277  313 LYS A CB  
2469 C CG  . LYS A 313 ? 1.5262 1.0033 0.5642 0.0235  0.0516  0.0075  313 LYS A CG  
2470 C CD  . LYS A 313 ? 1.5132 1.0416 0.6163 0.0388  0.0630  -0.0119 313 LYS A CD  
2471 C CE  . LYS A 313 ? 1.4840 1.0538 0.5912 0.0265  0.0980  -0.0303 313 LYS A CE  
2472 N NZ  . LYS A 313 ? 1.4977 1.1191 0.6652 0.0471  0.1053  -0.0509 313 LYS A NZ  
2473 N N   . GLY A 314 ? 1.3578 0.8108 0.5123 0.0755  -0.0370 0.0358  314 GLY A N   
2474 C CA  . GLY A 314 ? 1.3174 0.7556 0.4945 0.0828  -0.0619 0.0502  314 GLY A CA  
2475 C C   . GLY A 314 ? 1.3260 0.7827 0.5522 0.0834  -0.0535 0.0525  314 GLY A C   
2476 O O   . GLY A 314 ? 1.2891 0.7794 0.5505 0.0872  -0.0395 0.0391  314 GLY A O   
2477 N N   . THR A 315 ? 1.2897 0.7256 0.5211 0.0822  -0.0643 0.0680  315 THR A N   
2478 C CA  . THR A 315 ? 1.2578 0.7034 0.5218 0.0766  -0.0511 0.0706  315 THR A CA  
2479 C C   . THR A 315 ? 1.1694 0.6360 0.4912 0.0892  -0.0630 0.0663  315 THR A C   
2480 O O   . THR A 315 ? 1.1579 0.6106 0.4891 0.0991  -0.0862 0.0730  315 THR A O   
2481 C CB  . THR A 315 ? 1.2971 0.7000 0.5289 0.0673  -0.0533 0.0894  315 THR A CB  
2482 O OG1 . THR A 315 ? 1.3356 0.7193 0.5113 0.0499  -0.0362 0.0933  315 THR A OG1 
2483 C CG2 . THR A 315 ? 1.2325 0.6408 0.4999 0.0621  -0.0420 0.0904  315 THR A CG2 
2484 N N   . VAL A 316 ? 1.1680 0.6703 0.5274 0.0879  -0.0468 0.0546  316 VAL A N   
2485 C CA  . VAL A 316 ? 1.0955 0.6209 0.5070 0.0952  -0.0520 0.0496  316 VAL A CA  
2486 C C   . VAL A 316 ? 1.0853 0.6199 0.5161 0.0839  -0.0352 0.0502  316 VAL A C   
2487 O O   . VAL A 316 ? 1.0904 0.6490 0.5225 0.0745  -0.0144 0.0423  316 VAL A O   
2488 C CB  . VAL A 316 ? 1.0724 0.6299 0.5065 0.1034  -0.0488 0.0358  316 VAL A CB  
2489 C CG1 . VAL A 316 ? 1.0073 0.5850 0.4879 0.1082  -0.0541 0.0321  316 VAL A CG1 
2490 C CG2 . VAL A 316 ? 1.1217 0.6661 0.5318 0.1116  -0.0618 0.0326  316 VAL A CG2 
2491 N N   . PHE A 317 ? 1.0531 0.5705 0.5001 0.0847  -0.0440 0.0574  317 PHE A N   
2492 C CA  . PHE A 317 ? 1.0409 0.5619 0.5073 0.0733  -0.0292 0.0565  317 PHE A CA  
2493 C C   . PHE A 317 ? 1.1038 0.6132 0.5370 0.0545  -0.0074 0.0589  317 PHE A C   
2494 O O   . PHE A 317 ? 1.1216 0.6567 0.5708 0.0409  0.0126  0.0501  317 PHE A O   
2495 C CB  . PHE A 317 ? 0.9936 0.5601 0.5053 0.0737  -0.0215 0.0430  317 PHE A CB  
2496 C CG  . PHE A 317 ? 0.9875 0.5588 0.5262 0.0639  -0.0117 0.0399  317 PHE A CG  
2497 C CD1 . PHE A 317 ? 1.0075 0.5402 0.5391 0.0615  -0.0151 0.0484  317 PHE A CD1 
2498 C CD2 . PHE A 317 ? 0.9835 0.5970 0.5536 0.0581  -0.0001 0.0278  317 PHE A CD2 
2499 C CE1 . PHE A 317 ? 1.0406 0.5745 0.5959 0.0523  -0.0046 0.0431  317 PHE A CE1 
2500 C CE2 . PHE A 317 ? 0.9954 0.6144 0.5884 0.0471  0.0095  0.0227  317 PHE A CE2 
2501 C CZ  . PHE A 317 ? 1.0078 0.5861 0.5938 0.0436  0.0083  0.0294  317 PHE A CZ  
2502 N N   . PHE A 318 ? 1.2202 0.6907 0.6045 0.0515  -0.0113 0.0709  318 PHE A N   
2503 C CA  . PHE A 318 ? 1.2195 0.6713 0.5627 0.0301  0.0100  0.0748  318 PHE A CA  
2504 C C   . PHE A 318 ? 1.2825 0.7781 0.6247 0.0204  0.0313  0.0598  318 PHE A C   
2505 O O   . PHE A 318 ? 1.3198 0.8138 0.6358 -0.0013 0.0542  0.0580  318 PHE A O   
2506 C CB  . PHE A 318 ? 1.2476 0.6823 0.5986 0.0143  0.0241  0.0772  318 PHE A CB  
2507 C CG  . PHE A 318 ? 1.2858 0.6797 0.6455 0.0265  0.0052  0.0888  318 PHE A CG  
2508 C CD1 . PHE A 318 ? 1.2756 0.6113 0.5921 0.0325  -0.0104 0.1079  318 PHE A CD1 
2509 C CD2 . PHE A 318 ? 1.2934 0.7088 0.7048 0.0329  0.0028  0.0799  318 PHE A CD2 
2510 C CE1 . PHE A 318 ? 1.2770 0.5786 0.6063 0.0478  -0.0290 0.1170  318 PHE A CE1 
2511 C CE2 . PHE A 318 ? 1.2497 0.6319 0.6735 0.0456  -0.0129 0.0873  318 PHE A CE2 
2512 C CZ  . PHE A 318 ? 1.3019 0.6282 0.6869 0.0547  -0.0293 0.1055  318 PHE A CZ  
2513 N N   . ASP A 319 ? 1.2374 0.7698 0.6050 0.0361  0.0244  0.0487  319 ASP A N   
2514 C CA  . ASP A 319 ? 1.2422 0.8162 0.6117 0.0344  0.0407  0.0334  319 ASP A CA  
2515 C C   . ASP A 319 ? 1.3025 0.8575 0.6353 0.0440  0.0301  0.0354  319 ASP A C   
2516 O O   . ASP A 319 ? 1.2561 0.7915 0.5893 0.0594  0.0064  0.0415  319 ASP A O   
2517 C CB  . ASP A 319 ? 1.1807 0.8054 0.6029 0.0470  0.0403  0.0195  319 ASP A CB  
2518 C CG  . ASP A 319 ? 1.2239 0.8729 0.6797 0.0339  0.0527  0.0151  319 ASP A CG  
2519 O OD1 . ASP A 319 ? 1.2482 0.8942 0.6885 0.0117  0.0720  0.0145  319 ASP A OD1 
2520 O OD2 . ASP A 319 ? 1.1806 0.8475 0.6745 0.0431  0.0433  0.0124  319 ASP A OD2 
2521 N N   . GLU A 320 ? 1.8261 1.3899 1.1267 0.0329  0.0491  0.0278  320 GLU A N   
2522 C CA  . GLU A 320 ? 1.8248 1.3637 1.0811 0.0374  0.0408  0.0301  320 GLU A CA  
2523 C C   . GLU A 320 ? 1.7670 1.3477 1.0556 0.0566  0.0411  0.0107  320 GLU A C   
2524 O O   . GLU A 320 ? 1.7564 1.3787 1.0634 0.0545  0.0614  -0.0047 320 GLU A O   
2525 C CB  . GLU A 320 ? 1.8948 1.4271 1.1002 0.0184  0.0621  0.0268  320 GLU A CB  
2526 C CG  . GLU A 320 ? 2.0109 1.5332 1.2038 0.0382  0.0417  0.0232  320 GLU A CG  
2527 C CD  . GLU A 320 ? 1.9887 1.4923 1.2111 0.0557  0.0099  0.0353  320 GLU A CD  
2528 O OE1 . GLU A 320 ? 1.9247 1.4365 1.1866 0.0729  -0.0089 0.0339  320 GLU A OE1 
2529 O OE2 . GLU A 320 ? 2.1095 1.5874 1.2878 0.0560  0.0003  0.0382  320 GLU A OE2 
2530 N N   . PHE A 321 ? 1.2514 0.8212 0.5497 0.0756  0.0183  0.0112  321 PHE A N   
2531 C CA  . PHE A 321 ? 1.2362 0.8286 0.5476 0.0919  0.0195  -0.0054 321 PHE A CA  
2532 C C   . PHE A 321 ? 1.2915 0.8663 0.5561 0.0917  0.0219  -0.0126 321 PHE A C   
2533 O O   . PHE A 321 ? 1.2995 0.8384 0.5197 0.0822  0.0129  -0.0018 321 PHE A O   
2534 C CB  . PHE A 321 ? 1.1962 0.7850 0.5385 0.1094  -0.0020 -0.0046 321 PHE A CB  
2535 C CG  . PHE A 321 ? 1.1745 0.7901 0.5665 0.1133  -0.0020 -0.0037 321 PHE A CG  
2536 C CD1 . PHE A 321 ? 1.1431 0.7587 0.5454 0.1003  0.0014  0.0059  321 PHE A CD1 
2537 C CD2 . PHE A 321 ? 1.1277 0.7610 0.5509 0.1295  -0.0076 -0.0114 321 PHE A CD2 
2538 C CE1 . PHE A 321 ? 1.1098 0.7478 0.5528 0.1013  0.0013  0.0059  321 PHE A CE1 
2539 C CE2 . PHE A 321 ? 1.0955 0.7510 0.5579 0.1307  -0.0089 -0.0091 321 PHE A CE2 
2540 C CZ  . PHE A 321 ? 1.0629 0.7230 0.5357 0.1159  -0.0039 -0.0015 321 PHE A CZ  
2541 N N   . THR A 322 ? 1.3082 0.9081 0.5822 0.1038  0.0331  -0.0319 322 THR A N   
2542 C CA  . THR A 322 ? 1.3043 0.8868 0.5401 0.1078  0.0334  -0.0430 322 THR A CA  
2543 C C   . THR A 322 ? 1.3225 0.8848 0.5688 0.1247  0.0107  -0.0443 322 THR A C   
2544 O O   . THR A 322 ? 1.2578 0.8365 0.5423 0.1411  0.0088  -0.0511 322 THR A O   
2545 C CB  . THR A 322 ? 1.3160 0.9332 0.5538 0.1128  0.0592  -0.0660 322 THR A CB  
2546 O OG1 . THR A 322 ? 1.3357 0.9747 0.5624 0.0923  0.0827  -0.0669 322 THR A OG1 
2547 C CG2 . THR A 322 ? 1.3217 0.9161 0.5160 0.1159  0.0602  -0.0794 322 THR A CG2 
2548 N N   . PHE A 323 ? 1.3589 0.8852 0.5692 0.1194  -0.0067 -0.0378 323 PHE A N   
2549 C CA  . PHE A 323 ? 1.3842 0.8897 0.6010 0.1290  -0.0290 -0.0386 323 PHE A CA  
2550 C C   . PHE A 323 ? 1.3780 0.8641 0.5572 0.1314  -0.0286 -0.0546 323 PHE A C   
2551 O O   . PHE A 323 ? 1.4409 0.9203 0.5769 0.1212  -0.0187 -0.0591 323 PHE A O   
2552 C CB  . PHE A 323 ? 1.3837 0.8680 0.5959 0.1212  -0.0536 -0.0202 323 PHE A CB  
2553 C CG  . PHE A 323 ? 1.3287 0.8268 0.5843 0.1220  -0.0582 -0.0073 323 PHE A CG  
2554 C CD1 . PHE A 323 ? 1.3293 0.8332 0.5838 0.1121  -0.0483 0.0038  323 PHE A CD1 
2555 C CD2 . PHE A 323 ? 1.2875 0.7900 0.5812 0.1301  -0.0711 -0.0072 323 PHE A CD2 
2556 C CE1 . PHE A 323 ? 1.3269 0.8410 0.6187 0.1119  -0.0514 0.0134  323 PHE A CE1 
2557 C CE2 . PHE A 323 ? 1.2399 0.7559 0.5710 0.1295  -0.0738 0.0025  323 PHE A CE2 
2558 C CZ  . PHE A 323 ? 1.2840 0.8060 0.6150 0.1211  -0.0640 0.0122  323 PHE A CZ  
2559 N N   . VAL A 324 ? 1.4053 0.8796 0.5981 0.1430  -0.0386 -0.0637 324 VAL A N   
2560 C CA  . VAL A 324 ? 1.4294 0.8759 0.5867 0.1424  -0.0450 -0.0773 324 VAL A CA  
2561 C C   . VAL A 324 ? 1.4024 0.8294 0.5687 0.1391  -0.0711 -0.0706 324 VAL A C   
2562 O O   . VAL A 324 ? 1.4195 0.8525 0.6258 0.1456  -0.0774 -0.0651 324 VAL A O   
2563 C CB  . VAL A 324 ? 1.4357 0.8815 0.5959 0.1587  -0.0286 -0.0999 324 VAL A CB  
2564 C CG1 . VAL A 324 ? 1.3963 0.8495 0.6034 0.1756  -0.0304 -0.0988 324 VAL A CG1 
2565 C CG2 . VAL A 324 ? 1.4593 0.8707 0.5810 0.1557  -0.0355 -0.1152 324 VAL A CG2 
2566 N N   . LYS A 325 ? 1.5173 0.9244 0.6460 0.1275  -0.0861 -0.0713 325 LYS A N   
2567 C CA  . LYS A 325 ? 1.4934 0.8890 0.6309 0.1218  -0.1113 -0.0675 325 LYS A CA  
2568 C C   . LYS A 325 ? 1.4979 0.8744 0.6405 0.1264  -0.1110 -0.0849 325 LYS A C   
2569 O O   . LYS A 325 ? 1.5557 0.9166 0.6730 0.1309  -0.0975 -0.1025 325 LYS A O   
2570 C CB  . LYS A 325 ? 1.5264 0.9111 0.6209 0.1083  -0.1292 -0.0635 325 LYS A CB  
2571 C CG  . LYS A 325 ? 1.4877 0.8738 0.5982 0.1023  -0.1578 -0.0562 325 LYS A CG  
2572 C CD  . LYS A 325 ? 1.5300 0.9003 0.5957 0.0909  -0.1731 -0.0673 325 LYS A CD  
2573 C CE  . LYS A 325 ? 1.5961 0.9765 0.6755 0.0845  -0.2041 -0.0598 325 LYS A CE  
2574 N NZ  . LYS A 325 ? 1.6453 1.0193 0.7304 0.0758  -0.2138 -0.0785 325 LYS A NZ  
2575 N N   . LEU A 326 ? 1.4643 0.8402 0.6393 0.1249  -0.1244 -0.0806 326 LEU A N   
2576 C CA  . LEU A 326 ? 1.4932 0.8438 0.6690 0.1250  -0.1254 -0.0951 326 LEU A CA  
2577 C C   . LEU A 326 ? 1.4423 0.7768 0.5880 0.1081  -0.1431 -0.1048 326 LEU A C   
2578 O O   . LEU A 326 ? 1.4846 0.8344 0.6421 0.0973  -0.1633 -0.0960 326 LEU A O   
2579 C CB  . LEU A 326 ? 1.3858 0.7426 0.6059 0.1269  -0.1298 -0.0867 326 LEU A CB  
2580 C CG  . LEU A 326 ? 1.4035 0.7591 0.6448 0.1443  -0.1129 -0.0863 326 LEU A CG  
2581 C CD1 . LEU A 326 ? 1.3907 0.7721 0.6356 0.1565  -0.0971 -0.0818 326 LEU A CD1 
2582 C CD2 . LEU A 326 ? 1.3462 0.7110 0.6265 0.1418  -0.1192 -0.0752 326 LEU A CD2 
2583 N N   . THR A 327 ? 1.5059 0.8119 0.6149 0.1062  -0.1359 -0.1244 327 THR A N   
2584 C CA  . THR A 327 ? 1.5655 0.8580 0.6410 0.0879  -0.1522 -0.1363 327 THR A CA  
2585 C C   . THR A 327 ? 1.5942 0.8596 0.6744 0.0778  -0.1572 -0.1505 327 THR A C   
2586 O O   . THR A 327 ? 1.6055 0.8803 0.6952 0.0608  -0.1770 -0.1504 327 THR A O   
2587 C CB  . THR A 327 ? 1.5876 0.8657 0.6103 0.0864  -0.1419 -0.1511 327 THR A CB  
2588 O OG1 . THR A 327 ? 1.6103 0.8655 0.6273 0.1012  -0.1177 -0.1665 327 THR A OG1 
2589 C CG2 . THR A 327 ? 1.6405 0.9433 0.6502 0.0886  -0.1398 -0.1360 327 THR A CG2 
2590 N N   . GLY A 328 ? 1.5829 0.8149 0.6580 0.0880  -0.1396 -0.1627 328 GLY A N   
2591 C CA  . GLY A 328 ? 1.6613 0.8578 0.7340 0.0764  -0.1424 -0.1754 328 GLY A CA  
2592 C C   . GLY A 328 ? 1.5616 0.7708 0.6782 0.0717  -0.1501 -0.1610 328 GLY A C   
2593 O O   . GLY A 328 ? 1.5590 0.7969 0.7094 0.0841  -0.1479 -0.1428 328 GLY A O   
2594 N N   . VAL A 329 ? 1.6186 0.8060 0.7325 0.0508  -0.1579 -0.1713 329 VAL A N   
2595 C CA  . VAL A 329 ? 1.5424 0.7337 0.6917 0.0426  -0.1610 -0.1618 329 VAL A CA  
2596 C C   . VAL A 329 ? 1.5399 0.7017 0.6962 0.0627  -0.1437 -0.1545 329 VAL A C   
2597 O O   . VAL A 329 ? 1.5476 0.7188 0.7342 0.0619  -0.1437 -0.1414 329 VAL A O   
2598 C CB  . VAL A 329 ? 1.5547 0.7263 0.6933 0.0114  -0.1703 -0.1782 329 VAL A CB  
2599 C CG1 . VAL A 329 ? 1.5988 0.7019 0.7051 0.0090  -0.1555 -0.1925 329 VAL A CG1 
2600 C CG2 . VAL A 329 ? 1.5535 0.7590 0.7349 -0.0046 -0.1805 -0.1691 329 VAL A CG2 
2601 N N   . ALA A 330 ? 1.6237 0.7530 0.7528 0.0824  -0.1294 -0.1632 330 ALA A N   
2602 C CA  . ALA A 330 ? 1.6042 0.7123 0.7407 0.1086  -0.1150 -0.1561 330 ALA A CA  
2603 C C   . ALA A 330 ? 1.5930 0.7067 0.7153 0.1334  -0.1025 -0.1631 330 ALA A C   
2604 O O   . ALA A 330 ? 1.5936 0.7065 0.6877 0.1271  -0.1021 -0.1777 330 ALA A O   
2605 C CB  . ALA A 330 ? 1.6016 0.6429 0.7158 0.1052  -0.1093 -0.1647 330 ALA A CB  
2606 N N   . GLY A 331 ? 1.7146 0.8396 0.8571 0.1604  -0.0922 -0.1535 331 GLY A N   
2607 C CA  . GLY A 331 ? 1.6521 0.7921 0.7873 0.1830  -0.0784 -0.1620 331 GLY A CA  
2608 C C   . GLY A 331 ? 1.6723 0.8312 0.8363 0.2125  -0.0688 -0.1522 331 GLY A C   
2609 O O   . GLY A 331 ? 1.6387 0.8059 0.8296 0.2147  -0.0742 -0.1352 331 GLY A O   
2610 N N   . ASN A 332 ? 1.5127 0.6814 0.6704 0.2343  -0.0541 -0.1650 332 ASN A N   
2611 C CA  . ASN A 332 ? 1.5218 0.7249 0.7093 0.2627  -0.0438 -0.1602 332 ASN A CA  
2612 C C   . ASN A 332 ? 1.5487 0.8048 0.7404 0.2601  -0.0337 -0.1639 332 ASN A C   
2613 O O   . ASN A 332 ? 1.6063 0.8555 0.7694 0.2588  -0.0237 -0.1826 332 ASN A O   
2614 C CB  . ASN A 332 ? 1.5422 0.7083 0.7207 0.2947  -0.0336 -0.1756 332 ASN A CB  
2615 C CG  . ASN A 332 ? 1.5824 0.6825 0.7466 0.2964  -0.0426 -0.1715 332 ASN A CG  
2616 O OD1 . ASN A 332 ? 1.5760 0.6772 0.7584 0.2925  -0.0525 -0.1517 332 ASN A OD1 
2617 N ND2 . ASN A 332 ? 1.6389 0.6787 0.7678 0.3018  -0.0373 -0.1912 332 ASN A ND2 
2618 N N   . TYR A 333 ? 1.4211 0.7272 0.6448 0.2573  -0.0350 -0.1468 333 TYR A N   
2619 C CA  . TYR A 333 ? 1.4346 0.7878 0.6607 0.2494  -0.0256 -0.1463 333 TYR A CA  
2620 C C   . TYR A 333 ? 1.3872 0.7890 0.6512 0.2676  -0.0147 -0.1420 333 TYR A C   
2621 O O   . TYR A 333 ? 1.3873 0.7968 0.6809 0.2766  -0.0218 -0.1292 333 TYR A O   
2622 C CB  . TYR A 333 ? 1.3781 0.7446 0.6029 0.2213  -0.0392 -0.1291 333 TYR A CB  
2623 C CG  . TYR A 333 ? 1.4257 0.7599 0.6134 0.2007  -0.0509 -0.1345 333 TYR A CG  
2624 C CD1 . TYR A 333 ? 1.4149 0.7523 0.5670 0.1896  -0.0458 -0.1435 333 TYR A CD1 
2625 C CD2 . TYR A 333 ? 1.4164 0.7197 0.6033 0.1900  -0.0670 -0.1311 333 TYR A CD2 
2626 C CE1 . TYR A 333 ? 1.4261 0.7381 0.5436 0.1705  -0.0589 -0.1486 333 TYR A CE1 
2627 C CE2 . TYR A 333 ? 1.4506 0.7312 0.6068 0.1699  -0.0788 -0.1380 333 TYR A CE2 
2628 C CZ  . TYR A 333 ? 1.4857 0.7716 0.6076 0.1611  -0.0760 -0.1466 333 TYR A CZ  
2629 O OH  . TYR A 333 ? 1.4970 0.7639 0.5877 0.1409  -0.0902 -0.1537 333 TYR A OH  
2630 N N   . THR A 334 ? 1.4726 0.9097 0.7344 0.2702  0.0027  -0.1531 334 THR A N   
2631 C CA  . THR A 334 ? 1.4277 0.9210 0.7254 0.2809  0.0147  -0.1514 334 THR A CA  
2632 C C   . THR A 334 ? 1.4299 0.9562 0.7187 0.2567  0.0239  -0.1467 334 THR A C   
2633 O O   . THR A 334 ? 1.4763 0.9888 0.7272 0.2426  0.0299  -0.1551 334 THR A O   
2634 C CB  . THR A 334 ? 1.4582 0.9681 0.7665 0.3108  0.0313  -0.1742 334 THR A CB  
2635 O OG1 . THR A 334 ? 1.4411 0.9163 0.7577 0.3366  0.0212  -0.1752 334 THR A OG1 
2636 C CG2 . THR A 334 ? 1.3864 0.9652 0.7329 0.3173  0.0447  -0.1755 334 THR A CG2 
2637 N N   . VAL A 335 ? 1.5792 1.1457 0.8990 0.2508  0.0254  -0.1334 335 VAL A N   
2638 C CA  . VAL A 335 ? 1.5626 1.1549 0.8733 0.2268  0.0345  -0.1264 335 VAL A CA  
2639 C C   . VAL A 335 ? 1.5517 1.2016 0.9002 0.2312  0.0496  -0.1287 335 VAL A C   
2640 O O   . VAL A 335 ? 1.5196 1.1875 0.9050 0.2424  0.0421  -0.1213 335 VAL A O   
2641 C CB  . VAL A 335 ? 1.6148 1.1867 0.9194 0.2056  0.0162  -0.1033 335 VAL A CB  
2642 C CG1 . VAL A 335 ? 1.6718 1.2464 0.9455 0.1813  0.0232  -0.0971 335 VAL A CG1 
2643 C CG2 . VAL A 335 ? 1.6044 1.1288 0.8910 0.2060  -0.0035 -0.1007 335 VAL A CG2 
2644 N N   . CYS A 336 ? 1.2728 0.9526 0.6100 0.2184  0.0706  -0.1384 336 CYS A N   
2645 C CA  . CYS A 336 ? 1.3028 1.0435 0.6763 0.2198  0.0877  -0.1453 336 CYS A CA  
2646 C C   . CYS A 336 ? 1.2768 1.0313 0.6350 0.1871  0.0994  -0.1356 336 CYS A C   
2647 O O   . CYS A 336 ? 1.3323 1.0549 0.6448 0.1671  0.1010  -0.1303 336 CYS A O   
2648 C CB  . CYS A 336 ? 1.2709 1.0471 0.6548 0.2399  0.1080  -0.1739 336 CYS A CB  
2649 S SG  . CYS A 336 ? 1.3154 1.0648 0.7115 0.2822  0.0953  -0.1864 336 CYS A SG  
2650 N N   . GLN A 337 ? 1.2723 1.0721 0.6667 0.1813  0.1068  -0.1330 337 GLN A N   
2651 C CA  . GLN A 337 ? 1.2434 1.0626 0.6277 0.1503  0.1237  -0.1283 337 GLN A CA  
2652 C C   . GLN A 337 ? 1.2487 1.1384 0.6807 0.1530  0.1398  -0.1421 337 GLN A C   
2653 O O   . GLN A 337 ? 1.1875 1.0986 0.6607 0.1688  0.1274  -0.1385 337 GLN A O   
2654 C CB  . GLN A 337 ? 1.2381 1.0194 0.6096 0.1308  0.1080  -0.1017 337 GLN A CB  
2655 C CG  . GLN A 337 ? 1.2111 1.0056 0.5724 0.0992  0.1253  -0.0956 337 GLN A CG  
2656 C CD  . GLN A 337 ? 1.2841 1.0388 0.6369 0.0851  0.1089  -0.0705 337 GLN A CD  
2657 O OE1 . GLN A 337 ? 1.2505 1.0244 0.6306 0.0753  0.1117  -0.0651 337 GLN A OE1 
2658 N NE2 . GLN A 337 ? 1.2967 0.9974 0.6127 0.0848  0.0912  -0.0566 337 GLN A NE2 
2659 N N   . LYS A 338 ? 1.2118 1.1394 0.6365 0.1359  0.1674  -0.1585 338 LYS A N   
2660 C CA  . LYS A 338 ? 1.2051 1.2103 0.6753 0.1364  0.1864  -0.1778 338 LYS A CA  
2661 C C   . LYS A 338 ? 1.2045 1.2452 0.7225 0.1778  0.1751  -0.1914 338 LYS A C   
2662 O O   . LYS A 338 ? 1.1662 1.2079 0.6812 0.2018  0.1787  -0.2087 338 LYS A O   
2663 C CB  . LYS A 338 ? 1.2140 1.2354 0.7002 0.1099  0.1884  -0.1648 338 LYS A CB  
2664 C CG  . LYS A 338 ? 1.2308 1.2090 0.6672 0.0703  0.1984  -0.1489 338 LYS A CG  
2665 C CD  . LYS A 338 ? 1.2859 1.3083 0.7406 0.0395  0.2193  -0.1536 338 LYS A CD  
2666 C CE  . LYS A 338 ? 1.2804 1.2613 0.7289 0.0222  0.2056  -0.1283 338 LYS A CE  
2667 N NZ  . LYS A 338 ? 1.2019 1.2351 0.6939 0.0085  0.2139  -0.1347 338 LYS A NZ  
2668 N N   . ASP A 339 ? 1.1365 1.2059 0.6965 0.1864  0.1622  -0.1843 339 ASP A N   
2669 C CA  . ASP A 339 ? 1.0497 1.1562 0.6547 0.2251  0.1498  -0.1945 339 ASP A CA  
2670 C C   . ASP A 339 ? 1.0731 1.1215 0.6709 0.2501  0.1205  -0.1768 339 ASP A C   
2671 O O   . ASP A 339 ? 1.0318 1.0982 0.6585 0.2838  0.1081  -0.1821 339 ASP A O   
2672 C CB  . ASP A 339 ? 1.0603 1.2351 0.7128 0.2195  0.1514  -0.1977 339 ASP A CB  
2673 C CG  . ASP A 339 ? 1.0802 1.3316 0.7540 0.2025  0.1808  -0.2230 339 ASP A CG  
2674 O OD1 . ASP A 339 ? 1.1046 1.3655 0.7642 0.2035  0.2000  -0.2417 339 ASP A OD1 
2675 O OD2 . ASP A 339 ? 1.2154 1.5205 0.9210 0.1862  0.1857  -0.2259 339 ASP A OD2 
2676 N N   . LEU A 340 ? 1.1709 1.1518 0.7316 0.2343  0.1087  -0.1561 340 LEU A N   
2677 C CA  . LEU A 340 ? 1.1843 1.1148 0.7405 0.2503  0.0825  -0.1389 340 LEU A CA  
2678 C C   . LEU A 340 ? 1.1903 1.0592 0.7066 0.2585  0.0767  -0.1394 340 LEU A C   
2679 O O   . LEU A 340 ? 1.2057 1.0442 0.6850 0.2362  0.0825  -0.1357 340 LEU A O   
2680 C CB  . LEU A 340 ? 1.1609 1.0693 0.7143 0.2260  0.0714  -0.1161 340 LEU A CB  
2681 C CG  . LEU A 340 ? 1.1512 1.0108 0.7001 0.2376  0.0466  -0.0996 340 LEU A CG  
2682 C CD1 . LEU A 340 ? 1.0980 0.9892 0.6835 0.2532  0.0360  -0.0964 340 LEU A CD1 
2683 C CD2 . LEU A 340 ? 1.1591 0.9765 0.6863 0.2120  0.0386  -0.0812 340 LEU A CD2 
2684 N N   . CYS A 341 ? 1.3121 1.1595 0.8329 0.2895  0.0642  -0.1433 341 CYS A N   
2685 C CA  . CYS A 341 ? 1.3694 1.1524 0.8534 0.2963  0.0556  -0.1430 341 CYS A CA  
2686 C C   . CYS A 341 ? 1.3294 1.0674 0.8121 0.3015  0.0316  -0.1241 341 CYS A C   
2687 O O   . CYS A 341 ? 1.3463 1.0997 0.8565 0.3186  0.0219  -0.1188 341 CYS A O   
2688 C CB  . CYS A 341 ? 1.3606 1.1443 0.8428 0.3267  0.0642  -0.1667 341 CYS A CB  
2689 S SG  . CYS A 341 ? 1.4295 1.2489 0.8972 0.3169  0.0949  -0.1934 341 CYS A SG  
2690 N N   . CYS A 342 ? 1.1896 0.8739 0.6388 0.2857  0.0224  -0.1149 342 CYS A N   
2691 C CA  . CYS A 342 ? 1.1972 0.8386 0.6414 0.2821  0.0021  -0.0982 342 CYS A CA  
2692 C C   . CYS A 342 ? 1.2446 0.8286 0.6573 0.2915  -0.0047 -0.1051 342 CYS A C   
2693 O O   . CYS A 342 ? 1.3160 0.8801 0.6979 0.2814  0.0009  -0.1138 342 CYS A O   
2694 C CB  . CYS A 342 ? 1.1982 0.8332 0.6350 0.2516  -0.0033 -0.0826 342 CYS A CB  
2695 S SG  . CYS A 342 ? 1.1642 0.8581 0.6299 0.2355  0.0087  -0.0773 342 CYS A SG  
2696 N N   . HIS A 343 ? 1.3513 0.9057 0.7676 0.3082  -0.0167 -0.1006 343 HIS A N   
2697 C CA  . HIS A 343 ? 1.4025 0.8962 0.7885 0.3163  -0.0230 -0.1071 343 HIS A CA  
2698 C C   . HIS A 343 ? 1.3839 0.8380 0.7601 0.2977  -0.0395 -0.0912 343 HIS A C   
2699 O O   . HIS A 343 ? 1.3897 0.8570 0.7875 0.2946  -0.0475 -0.0762 343 HIS A O   
2700 C CB  . HIS A 343 ? 1.4319 0.9144 0.8246 0.3523  -0.0223 -0.1163 343 HIS A CB  
2701 C CG  . HIS A 343 ? 1.4614 0.9977 0.8767 0.3739  -0.0069 -0.1326 343 HIS A CG  
2702 N ND1 . HIS A 343 ? 1.4380 0.9733 0.8379 0.3830  0.0083  -0.1554 343 HIS A ND1 
2703 C CD2 . HIS A 343 ? 1.4092 1.0065 0.8628 0.3867  -0.0034 -0.1317 343 HIS A CD2 
2704 C CE1 . HIS A 343 ? 1.4246 1.0199 0.8546 0.4006  0.0214  -0.1683 343 HIS A CE1 
2705 N NE2 . HIS A 343 ? 1.4357 1.0706 0.8993 0.4031  0.0138  -0.1543 343 HIS A NE2 
2706 N N   . LEU A 344 ? 1.2468 0.6574 0.5912 0.2830  -0.0439 -0.0960 344 LEU A N   
2707 C CA  . LEU A 344 ? 1.2605 0.6343 0.5951 0.2639  -0.0584 -0.0857 344 LEU A CA  
2708 C C   . LEU A 344 ? 1.3433 0.6557 0.6429 0.2657  -0.0609 -0.0976 344 LEU A C   
2709 O O   . LEU A 344 ? 1.3589 0.6581 0.6341 0.2673  -0.0538 -0.1140 344 LEU A O   
2710 C CB  . LEU A 344 ? 1.2588 0.6494 0.5936 0.2354  -0.0644 -0.0784 344 LEU A CB  
2711 C CG  . LEU A 344 ? 1.2561 0.6170 0.5847 0.2144  -0.0789 -0.0719 344 LEU A CG  
2712 C CD1 . LEU A 344 ? 1.2127 0.5816 0.5677 0.2136  -0.0841 -0.0576 344 LEU A CD1 
2713 C CD2 . LEU A 344 ? 1.2860 0.6623 0.6116 0.1920  -0.0864 -0.0689 344 LEU A CD2 
2714 N N   . SER A 345 ? 1.4317 0.7045 0.7260 0.2633  -0.0699 -0.0902 345 SER A N   
2715 C CA  . SER A 345 ? 1.4940 0.7036 0.7535 0.2541  -0.0738 -0.0995 345 SER A CA  
2716 C C   . SER A 345 ? 1.4823 0.6840 0.7447 0.2232  -0.0855 -0.0886 345 SER A C   
2717 O O   . SER A 345 ? 1.4714 0.6977 0.7592 0.2188  -0.0898 -0.0731 345 SER A O   
2718 C CB  . SER A 345 ? 1.5301 0.6891 0.7744 0.2797  -0.0716 -0.1026 345 SER A CB  
2719 O OG  . SER A 345 ? 1.5529 0.7286 0.8031 0.3122  -0.0611 -0.1138 345 SER A OG  
2720 N N   . TYR A 346 ? 1.4500 0.6249 0.6891 0.2005  -0.0903 -0.0984 346 TYR A N   
2721 C CA  . TYR A 346 ? 1.4396 0.6247 0.6906 0.1708  -0.1012 -0.0905 346 TYR A CA  
2722 C C   . TYR A 346 ? 1.5093 0.6533 0.7304 0.1476  -0.1064 -0.1046 346 TYR A C   
2723 O O   . TYR A 346 ? 1.5242 0.6506 0.7185 0.1489  -0.1036 -0.1203 346 TYR A O   
2724 C CB  . TYR A 346 ? 1.4172 0.6613 0.6944 0.1614  -0.1061 -0.0836 346 TYR A CB  
2725 C CG  . TYR A 346 ? 1.4406 0.6898 0.6968 0.1530  -0.1087 -0.0958 346 TYR A CG  
2726 C CD1 . TYR A 346 ? 1.4320 0.6931 0.6764 0.1694  -0.0988 -0.1023 346 TYR A CD1 
2727 C CD2 . TYR A 346 ? 1.4360 0.6802 0.6828 0.1278  -0.1210 -0.1017 346 TYR A CD2 
2728 C CE1 . TYR A 346 ? 1.4560 0.7199 0.6752 0.1599  -0.1010 -0.1124 346 TYR A CE1 
2729 C CE2 . TYR A 346 ? 1.4717 0.7210 0.6952 0.1202  -0.1258 -0.1118 346 TYR A CE2 
2730 C CZ  . TYR A 346 ? 1.4732 0.7298 0.6804 0.1360  -0.1156 -0.1163 346 TYR A CZ  
2731 O OH  . TYR A 346 ? 1.5088 0.7686 0.6870 0.1269  -0.1198 -0.1255 346 TYR A OH  
2732 N N   . LYS A 347 ? 1.6514 0.7832 0.8771 0.1240  -0.1129 -0.1004 347 LYS A N   
2733 C CA  . LYS A 347 ? 1.7060 0.8076 0.9100 0.0948  -0.1187 -0.1139 347 LYS A CA  
2734 C C   . LYS A 347 ? 1.6192 0.7629 0.8557 0.0700  -0.1284 -0.1064 347 LYS A C   
2735 O O   . LYS A 347 ? 1.6359 0.7828 0.8899 0.0676  -0.1262 -0.0940 347 LYS A O   
2736 C CB  . LYS A 347 ? 1.7472 0.7731 0.9157 0.0981  -0.1109 -0.1197 347 LYS A CB  
2737 C CG  . LYS A 347 ? 1.8174 0.7804 0.9457 0.0763  -0.1096 -0.1377 347 LYS A CG  
2738 C CD  . LYS A 347 ? 1.8583 0.8033 0.9839 0.0390  -0.1134 -0.1390 347 LYS A CD  
2739 C CE  . LYS A 347 ? 1.9597 0.8140 1.0334 0.0322  -0.1052 -0.1538 347 LYS A CE  
2740 N NZ  . LYS A 347 ? 2.0014 0.8119 1.0588 -0.0065 -0.1034 -0.1548 347 LYS A NZ  
2741 N N   . MET A 348 ? 1.5144 0.6928 0.7589 0.0539  -0.1394 -0.1140 348 MET A N   
2742 C CA  . MET A 348 ? 1.4915 0.7167 0.7707 0.0330  -0.1507 -0.1107 348 MET A CA  
2743 C C   . MET A 348 ? 1.5255 0.7285 0.7974 0.0005  -0.1536 -0.1228 348 MET A C   
2744 O O   . MET A 348 ? 1.5770 0.7326 0.8124 -0.0101 -0.1509 -0.1373 348 MET A O   
2745 C CB  . MET A 348 ? 1.4492 0.7188 0.7372 0.0322  -0.1643 -0.1138 348 MET A CB  
2746 C CG  . MET A 348 ? 1.4649 0.7465 0.7444 0.0583  -0.1601 -0.1070 348 MET A CG  
2747 S SD  . MET A 348 ? 1.4907 0.8185 0.7752 0.0548  -0.1781 -0.1060 348 MET A SD  
2748 C CE  . MET A 348 ? 1.4647 0.7907 0.7270 0.0803  -0.1658 -0.0999 348 MET A CE  
2749 N N   . SER A 349 ? 1.5355 0.7740 0.8428 -0.0174 -0.1576 -0.1187 349 SER A N   
2750 C CA  . SER A 349 ? 1.5310 0.7587 0.8357 -0.0529 -0.1595 -0.1326 349 SER A CA  
2751 C C   . SER A 349 ? 1.6063 0.8513 0.9041 -0.0694 -0.1736 -0.1515 349 SER A C   
2752 O O   . SER A 349 ? 1.5953 0.8189 0.8773 -0.0993 -0.1739 -0.1683 349 SER A O   
2753 C CB  . SER A 349 ? 1.5012 0.7733 0.8497 -0.0679 -0.1597 -0.1267 349 SER A CB  
2754 O OG  . SER A 349 ? 1.5348 0.7970 0.8886 -0.0510 -0.1484 -0.1086 349 SER A OG  
2755 N N   . GLU A 350 ? 1.6511 0.9317 0.9560 -0.0517 -0.1852 -0.1491 350 GLU A N   
2756 C CA  . GLU A 350 ? 1.6684 0.9725 0.9668 -0.0650 -0.2022 -0.1645 350 GLU A CA  
2757 C C   . GLU A 350 ? 1.6507 0.9831 0.9489 -0.0390 -0.2116 -0.1546 350 GLU A C   
2758 O O   . GLU A 350 ? 1.6190 0.9736 0.9408 -0.0179 -0.2086 -0.1368 350 GLU A O   
2759 C CB  . GLU A 350 ? 1.6364 0.9923 0.9753 -0.0912 -0.2152 -0.1735 350 GLU A CB  
2760 C CG  . GLU A 350 ? 1.6340 1.0469 1.0249 -0.0777 -0.2207 -0.1587 350 GLU A CG  
2761 C CD  . GLU A 350 ? 1.6290 1.0724 1.0597 -0.1027 -0.2184 -0.1656 350 GLU A CD  
2762 O OE1 . GLU A 350 ? 1.6472 1.1039 1.0812 -0.1321 -0.2257 -0.1855 350 GLU A OE1 
2763 O OE2 . GLU A 350 ? 1.6020 1.0588 1.0605 -0.0948 -0.2087 -0.1528 350 GLU A OE2 
2764 N N   . ASN A 351 ? 1.8880 1.2165 1.1553 -0.0430 -0.2222 -0.1666 351 ASN A N   
2765 C CA  . ASN A 351 ? 1.8692 1.2249 1.1305 -0.0243 -0.2336 -0.1576 351 ASN A CA  
2766 C C   . ASN A 351 ? 1.8477 1.2625 1.1450 -0.0318 -0.2576 -0.1565 351 ASN A C   
2767 O O   . ASN A 351 ? 1.9041 1.3351 1.1949 -0.0509 -0.2745 -0.1722 351 ASN A O   
2768 C CB  . ASN A 351 ? 1.9564 1.2814 1.1640 -0.0248 -0.2337 -0.1705 351 ASN A CB  
2769 C CG  . ASN A 351 ? 2.0086 1.3253 1.1952 0.0020  -0.2239 -0.1581 351 ASN A CG  
2770 O OD1 . ASN A 351 ? 1.9645 1.3149 1.1628 0.0140  -0.2335 -0.1433 351 ASN A OD1 
2771 N ND2 . ASN A 351 ? 1.9828 1.2539 1.1372 0.0107  -0.2045 -0.1654 351 ASN A ND2 
2772 N N   . ILE A 352 ? 1.5898 1.0381 0.9270 -0.0166 -0.2595 -0.1392 352 ILE A N   
2773 C CA  . ILE A 352 ? 1.5381 1.0410 0.9099 -0.0146 -0.2829 -0.1355 352 ILE A CA  
2774 C C   . ILE A 352 ? 1.5766 1.0787 0.9146 0.0015  -0.2954 -0.1266 352 ILE A C   
2775 O O   . ILE A 352 ? 1.5807 1.0642 0.9029 0.0205  -0.2829 -0.1114 352 ILE A O   
2776 C CB  . ILE A 352 ? 1.4820 1.0141 0.9053 -0.0032 -0.2779 -0.1215 352 ILE A CB  
2777 C CG1 . ILE A 352 ? 1.4588 0.9770 0.9001 -0.0183 -0.2586 -0.1272 352 ILE A CG1 
2778 C CG2 . ILE A 352 ? 1.4640 1.0526 0.9291 -0.0017 -0.3023 -0.1223 352 ILE A CG2 
2779 C CD1 . ILE A 352 ? 1.4302 0.9787 0.9014 -0.0458 -0.2667 -0.1453 352 ILE A CD1 
2780 N N   . PRO A 353 ? 1.4767 0.9992 0.8003 -0.0071 -0.3199 -0.1359 353 PRO A N   
2781 C CA  . PRO A 353 ? 1.4764 0.9874 0.7527 0.0040  -0.3298 -0.1284 353 PRO A CA  
2782 C C   . PRO A 353 ? 1.4566 0.9807 0.7425 0.0285  -0.3353 -0.1037 353 PRO A C   
2783 O O   . PRO A 353 ? 1.4448 0.9409 0.6966 0.0403  -0.3214 -0.0922 353 PRO A O   
2784 C CB  . PRO A 353 ? 1.4951 1.0336 0.7616 -0.0121 -0.3589 -0.1440 353 PRO A CB  
2785 C CG  . PRO A 353 ? 1.5026 1.0612 0.8081 -0.0355 -0.3586 -0.1637 353 PRO A CG  
2786 C CD  . PRO A 353 ? 1.4225 0.9850 0.7741 -0.0274 -0.3405 -0.1532 353 PRO A CD  
2787 N N   . ASN A 354 ? 1.8353 1.4002 1.1688 0.0359  -0.3526 -0.0964 354 ASN A N   
2788 C CA  . ASN A 354 ? 1.8152 1.3874 1.1565 0.0589  -0.3597 -0.0734 354 ASN A CA  
2789 C C   . ASN A 354 ? 1.8196 1.3802 1.1866 0.0700  -0.3334 -0.0609 354 ASN A C   
2790 O O   . ASN A 354 ? 1.7466 1.3202 1.1394 0.0856  -0.3375 -0.0457 354 ASN A O   
2791 C CB  . ASN A 354 ? 1.7899 1.4091 1.1706 0.0660  -0.3914 -0.0721 354 ASN A CB  
2792 C CG  . ASN A 354 ? 1.8722 1.5279 1.3223 0.0622  -0.3873 -0.0810 354 ASN A CG  
2793 O OD1 . ASN A 354 ? 1.7938 1.4382 1.2580 0.0501  -0.3628 -0.0890 354 ASN A OD1 
2794 N ND2 . ASN A 354 ? 1.8862 1.5859 1.3786 0.0733  -0.4119 -0.0801 354 ASN A ND2 
2795 N N   . GLU A 355 ? 1.3402 0.8763 0.7011 0.0624  -0.3073 -0.0678 355 GLU A N   
2796 C CA  . GLU A 355 ? 1.3277 0.8537 0.7070 0.0724  -0.2833 -0.0569 355 GLU A CA  
2797 C C   . GLU A 355 ? 1.3177 0.8067 0.6518 0.0762  -0.2624 -0.0551 355 GLU A C   
2798 O O   . GLU A 355 ? 1.3293 0.7956 0.6374 0.0666  -0.2546 -0.0693 355 GLU A O   
2799 C CB  . GLU A 355 ? 1.2933 0.8292 0.7135 0.0621  -0.2717 -0.0662 355 GLU A CB  
2800 C CG  . GLU A 355 ? 1.2669 0.8151 0.7253 0.0725  -0.2590 -0.0542 355 GLU A CG  
2801 C CD  . GLU A 355 ? 1.2760 0.8449 0.7784 0.0597  -0.2545 -0.0638 355 GLU A CD  
2802 O OE1 . GLU A 355 ? 1.2663 0.8132 0.7601 0.0499  -0.2379 -0.0697 355 GLU A OE1 
2803 O OE2 . GLU A 355 ? 1.2528 0.8587 0.7968 0.0599  -0.2671 -0.0655 355 GLU A OE2 
2804 N N   . VAL A 356 ? 1.2699 0.7530 0.5950 0.0896  -0.2526 -0.0393 356 VAL A N   
2805 C CA  . VAL A 356 ? 1.2798 0.7368 0.5672 0.0941  -0.2315 -0.0385 356 VAL A CA  
2806 C C   . VAL A 356 ? 1.2621 0.7210 0.5773 0.1023  -0.2086 -0.0328 356 VAL A C   
2807 O O   . VAL A 356 ? 1.2368 0.7127 0.5828 0.1081  -0.2083 -0.0207 356 VAL A O   
2808 C CB  . VAL A 356 ? 1.3164 0.7655 0.5637 0.0988  -0.2365 -0.0266 356 VAL A CB  
2809 C CG1 . VAL A 356 ? 1.3259 0.7584 0.5476 0.1034  -0.2096 -0.0258 356 VAL A CG1 
2810 C CG2 . VAL A 356 ? 1.3415 0.7845 0.5486 0.0899  -0.2574 -0.0344 356 VAL A CG2 
2811 N N   . TYR A 357 ? 1.2444 0.6855 0.5473 0.1038  -0.1901 -0.0421 357 TYR A N   
2812 C CA  . TYR A 357 ? 1.2069 0.6509 0.5295 0.1134  -0.1693 -0.0378 357 TYR A CA  
2813 C C   . TYR A 357 ? 1.2559 0.6909 0.5471 0.1214  -0.1520 -0.0387 357 TYR A C   
2814 O O   . TYR A 357 ? 1.2667 0.6859 0.5171 0.1184  -0.1527 -0.0466 357 TYR A O   
2815 C CB  . TYR A 357 ? 1.2115 0.6433 0.5480 0.1120  -0.1622 -0.0473 357 TYR A CB  
2816 C CG  . TYR A 357 ? 1.2159 0.6628 0.5897 0.1025  -0.1726 -0.0457 357 TYR A CG  
2817 C CD1 . TYR A 357 ? 1.2387 0.6921 0.6149 0.0894  -0.1915 -0.0521 357 TYR A CD1 
2818 C CD2 . TYR A 357 ? 1.1637 0.6232 0.5713 0.1056  -0.1634 -0.0392 357 TYR A CD2 
2819 C CE1 . TYR A 357 ? 1.2466 0.7204 0.6608 0.0794  -0.1992 -0.0534 357 TYR A CE1 
2820 C CE2 . TYR A 357 ? 1.1482 0.6238 0.5889 0.0949  -0.1705 -0.0396 357 TYR A CE2 
2821 C CZ  . TYR A 357 ? 1.2000 0.6836 0.6455 0.0818  -0.1875 -0.0473 357 TYR A CZ  
2822 O OH  . TYR A 357 ? 1.2116 0.7172 0.6935 0.0700  -0.1927 -0.0505 357 TYR A OH  
2823 N N   . ALA A 358 ? 1.1593 0.6085 0.4699 0.1298  -0.1361 -0.0317 358 ALA A N   
2824 C CA  . ALA A 358 ? 1.1881 0.6373 0.4760 0.1363  -0.1171 -0.0349 358 ALA A CA  
2825 C C   . ALA A 358 ? 1.1996 0.6634 0.5160 0.1477  -0.1000 -0.0364 358 ALA A C   
2826 O O   . ALA A 358 ? 1.1558 0.6323 0.5076 0.1487  -0.1026 -0.0297 358 ALA A O   
2827 C CB  . ALA A 358 ? 1.1857 0.6424 0.4567 0.1313  -0.1159 -0.0230 358 ALA A CB  
2828 N N   . LEU A 359 ? 1.2879 0.7523 0.5883 0.1567  -0.0829 -0.0466 359 LEU A N   
2829 C CA  . LEU A 359 ? 1.2505 0.7364 0.5771 0.1700  -0.0672 -0.0488 359 LEU A CA  
2830 C C   . LEU A 359 ? 1.2567 0.7690 0.5796 0.1677  -0.0508 -0.0472 359 LEU A C   
2831 O O   . LEU A 359 ? 1.2837 0.7903 0.5727 0.1634  -0.0429 -0.0541 359 LEU A O   
2832 C CB  . LEU A 359 ? 1.2479 0.7175 0.5663 0.1858  -0.0601 -0.0642 359 LEU A CB  
2833 C CG  . LEU A 359 ? 1.2252 0.7208 0.5628 0.2042  -0.0431 -0.0708 359 LEU A CG  
2834 C CD1 . LEU A 359 ? 1.2108 0.7226 0.5869 0.2108  -0.0474 -0.0605 359 LEU A CD1 
2835 C CD2 . LEU A 359 ? 1.2443 0.7180 0.5636 0.2216  -0.0359 -0.0888 359 LEU A CD2 
2836 N N   . GLY A 360 ? 1.2376 0.7780 0.5927 0.1674  -0.0452 -0.0389 360 GLY A N   
2837 C CA  . GLY A 360 ? 1.2036 0.7683 0.5568 0.1596  -0.0296 -0.0363 360 GLY A CA  
2838 C C   . GLY A 360 ? 1.2152 0.8188 0.6016 0.1687  -0.0145 -0.0421 360 GLY A C   
2839 O O   . GLY A 360 ? 1.2364 0.8497 0.6533 0.1784  -0.0202 -0.0404 360 GLY A O   
2840 N N   . ALA A 361 ? 1.1055 0.7335 0.4841 0.1639  0.0050  -0.0492 361 ALA A N   
2841 C CA  . ALA A 361 ? 1.0959 0.7708 0.5063 0.1704  0.0209  -0.0576 361 ALA A CA  
2842 C C   . ALA A 361 ? 1.0881 0.7836 0.4991 0.1488  0.0344  -0.0519 361 ALA A C   
2843 O O   . ALA A 361 ? 1.1354 0.8147 0.5108 0.1328  0.0420  -0.0496 361 ALA A O   
2844 C CB  . ALA A 361 ? 1.0845 0.7775 0.4895 0.1859  0.0357  -0.0781 361 ALA A CB  
2845 N N   . PHE A 362 ? 1.0559 0.7844 0.5034 0.1468  0.0379  -0.0498 362 PHE A N   
2846 C CA  . PHE A 362 ? 1.0950 0.8446 0.5457 0.1248  0.0534  -0.0473 362 PHE A CA  
2847 C C   . PHE A 362 ? 1.0799 0.8894 0.5692 0.1290  0.0672  -0.0605 362 PHE A C   
2848 O O   . PHE A 362 ? 1.0294 0.8582 0.5504 0.1460  0.0573  -0.0621 362 PHE A O   
2849 C CB  . PHE A 362 ? 1.0668 0.7924 0.5219 0.1113  0.0423  -0.0299 362 PHE A CB  
2850 C CG  . PHE A 362 ? 1.1140 0.8529 0.5688 0.0874  0.0592  -0.0277 362 PHE A CG  
2851 C CD1 . PHE A 362 ? 1.0883 0.8015 0.5013 0.0684  0.0701  -0.0228 362 PHE A CD1 
2852 C CD2 . PHE A 362 ? 1.0285 0.8028 0.5205 0.0819  0.0649  -0.0307 362 PHE A CD2 
2853 C CE1 . PHE A 362 ? 1.0927 0.8108 0.5005 0.0437  0.0873  -0.0204 362 PHE A CE1 
2854 C CE2 . PHE A 362 ? 1.0363 0.8200 0.5262 0.0568  0.0821  -0.0305 362 PHE A CE2 
2855 C CZ  . PHE A 362 ? 1.0944 0.8479 0.5422 0.0374  0.0939  -0.0252 362 PHE A CZ  
2856 N N   . ASP A 363 ? 1.2196 1.0590 0.7044 0.1114  0.0898  -0.0697 363 ASP A N   
2857 C CA  . ASP A 363 ? 1.1766 1.0825 0.6994 0.1121  0.1047  -0.0855 363 ASP A CA  
2858 C C   . ASP A 363 ? 1.2119 1.1305 0.7244 0.0779  0.1263  -0.0862 363 ASP A C   
2859 O O   . ASP A 363 ? 1.2607 1.1873 0.7493 0.0638  0.1464  -0.0957 363 ASP A O   
2860 C CB  . ASP A 363 ? 1.1787 1.1192 0.7097 0.1336  0.1134  -0.1060 363 ASP A CB  
2861 C CG  . ASP A 363 ? 1.1803 1.1982 0.7517 0.1341  0.1297  -0.1252 363 ASP A CG  
2862 O OD1 . ASP A 363 ? 1.1695 1.2145 0.7595 0.1135  0.1360  -0.1233 363 ASP A OD1 
2863 O OD2 . ASP A 363 ? 1.2287 1.2821 0.8145 0.1557  0.1363  -0.1441 363 ASP A OD2 
2864 N N   . GLY A 364 ? 1.2114 1.1296 0.7395 0.0630  0.1234  -0.0771 364 GLY A N   
2865 C CA  . GLY A 364 ? 1.2028 1.1203 0.7156 0.0285  0.1436  -0.0762 364 GLY A CA  
2866 C C   . GLY A 364 ? 1.1978 1.1095 0.7298 0.0154  0.1384  -0.0673 364 GLY A C   
2867 O O   . GLY A 364 ? 1.1648 1.0803 0.7242 0.0322  0.1202  -0.0630 364 GLY A O   
2868 N N   . LEU A 365 ? 1.0965 0.9951 0.6101 -0.0168 0.1560  -0.0650 365 LEU A N   
2869 C CA  . LEU A 365 ? 1.1275 1.0231 0.6574 -0.0350 0.1577  -0.0612 365 LEU A CA  
2870 C C   . LEU A 365 ? 1.1460 0.9646 0.6468 -0.0372 0.1436  -0.0390 365 LEU A C   
2871 O O   . LEU A 365 ? 1.1969 0.9654 0.6520 -0.0487 0.1481  -0.0279 365 LEU A O   
2872 C CB  . LEU A 365 ? 1.0851 1.0098 0.6113 -0.0708 0.1873  -0.0740 365 LEU A CB  
2873 C CG  . LEU A 365 ? 1.0953 1.0160 0.6322 -0.0976 0.1959  -0.0742 365 LEU A CG  
2874 C CD1 . LEU A 365 ? 1.0458 1.0156 0.6346 -0.0829 0.1826  -0.0825 365 LEU A CD1 
2875 C CD2 . LEU A 365 ? 1.1157 1.0655 0.6429 -0.1353 0.2277  -0.0890 365 LEU A CD2 
2876 N N   . HIS A 366 ? 1.0596 0.8703 0.5862 -0.0249 0.1258  -0.0330 366 HIS A N   
2877 C CA  . HIS A 366 ? 1.0999 0.8487 0.6107 -0.0275 0.1142  -0.0161 366 HIS A CA  
2878 C C   . HIS A 366 ? 1.1115 0.8479 0.6180 -0.0577 0.1322  -0.0176 366 HIS A C   
2879 O O   . HIS A 366 ? 1.1472 0.9326 0.6824 -0.0718 0.1456  -0.0327 366 HIS A O   
2880 C CB  . HIS A 366 ? 1.0754 0.8268 0.6184 -0.0055 0.0919  -0.0130 366 HIS A CB  
2881 C CG  . HIS A 366 ? 1.0500 0.7456 0.5841 -0.0036 0.0785  0.0014  366 HIS A CG  
2882 N ND1 . HIS A 366 ? 1.0335 0.6889 0.5489 0.0136  0.0589  0.0141  366 HIS A ND1 
2883 C CD2 . HIS A 366 ? 1.0675 0.7433 0.6112 -0.0157 0.0816  0.0031  366 HIS A CD2 
2884 C CE1 . HIS A 366 ? 1.0480 0.6648 0.5645 0.0139  0.0496  0.0233  366 HIS A CE1 
2885 N NE2 . HIS A 366 ? 1.0680 0.6939 0.6012 -0.0030 0.0636  0.0168  366 HIS A NE2 
2886 N N   . THR A 367 ? 1.1777 0.8465 0.6466 -0.0673 0.1313  -0.0019 367 THR A N   
2887 C CA  . THR A 367 ? 1.1808 0.8214 0.6351 -0.0972 0.1496  -0.0014 367 THR A CA  
2888 C C   . THR A 367 ? 1.1953 0.7694 0.6397 -0.0928 0.1368  0.0137  367 THR A C   
2889 O O   . THR A 367 ? 1.2319 0.7794 0.6682 -0.1157 0.1515  0.0126  367 THR A O   
2890 C CB  . THR A 367 ? 1.2442 0.8629 0.6492 -0.1232 0.1714  0.0011  367 THR A CB  
2891 O OG1 . THR A 367 ? 1.2529 0.8236 0.6147 -0.1092 0.1577  0.0184  367 THR A OG1 
2892 C CG2 . THR A 367 ? 1.2129 0.9078 0.6362 -0.1352 0.1918  -0.0204 367 THR A CG2 
2893 N N   . VAL A 368 ? 1.2125 0.7589 0.6576 -0.0648 0.1109  0.0263  368 VAL A N   
2894 C CA  . VAL A 368 ? 1.2638 0.7487 0.7004 -0.0573 0.0977  0.0399  368 VAL A CA  
2895 C C   . VAL A 368 ? 1.2140 0.7254 0.7023 -0.0466 0.0896  0.0299  368 VAL A C   
2896 O O   . VAL A 368 ? 1.1936 0.7411 0.7115 -0.0265 0.0745  0.0257  368 VAL A O   
2897 C CB  . VAL A 368 ? 1.2756 0.7181 0.6833 -0.0343 0.0735  0.0580  368 VAL A CB  
2898 C CG1 . VAL A 368 ? 1.3261 0.7352 0.7518 -0.0142 0.0522  0.0658  368 VAL A CG1 
2899 C CG2 . VAL A 368 ? 1.3215 0.7115 0.6659 -0.0493 0.0816  0.0726  368 VAL A CG2 
2900 N N   . GLU A 369 ? 1.2888 0.7777 0.7845 -0.0612 0.1004  0.0258  369 GLU A N   
2901 C CA  . GLU A 369 ? 1.2724 0.7889 0.8142 -0.0582 0.0989  0.0126  369 GLU A CA  
2902 C C   . GLU A 369 ? 1.2408 0.8357 0.8166 -0.0593 0.1024  -0.0031 369 GLU A C   
2903 O O   . GLU A 369 ? 1.2385 0.8625 0.8422 -0.0397 0.0867  -0.0054 369 GLU A O   
2904 C CB  . GLU A 369 ? 1.2866 0.7794 0.8462 -0.0306 0.0749  0.0197  369 GLU A CB  
2905 C CG  . GLU A 369 ? 1.3241 0.7483 0.8494 -0.0178 0.0614  0.0388  369 GLU A CG  
2906 C CD  . GLU A 369 ? 1.3724 0.8003 0.9148 0.0126  0.0337  0.0450  369 GLU A CD  
2907 O OE1 . GLU A 369 ? 1.3666 0.8150 0.9502 0.0228  0.0268  0.0353  369 GLU A OE1 
2908 O OE2 . GLU A 369 ? 1.3326 0.7463 0.8471 0.0238  0.0199  0.0576  369 GLU A OE2 
2909 N N   . GLY A 370 ? 1.0702 0.6984 0.6406 -0.0826 0.1229  -0.0134 370 GLY A N   
2910 C CA  . GLY A 370 ? 1.0215 0.7255 0.6222 -0.0828 0.1261  -0.0283 370 GLY A CA  
2911 C C   . GLY A 370 ? 1.0822 0.8160 0.6667 -0.0875 0.1354  -0.0308 370 GLY A C   
2912 O O   . GLY A 370 ? 1.0623 0.7673 0.6183 -0.0760 0.1287  -0.0188 370 GLY A O   
2913 N N   . ARG A 371 ? 1.2210 1.0155 0.8241 -0.1047 0.1513  -0.0481 371 ARG A N   
2914 C CA  . ARG A 371 ? 1.2483 1.0858 0.8457 -0.1081 0.1620  -0.0557 371 ARG A CA  
2915 C C   . ARG A 371 ? 1.1793 1.0861 0.8143 -0.0858 0.1500  -0.0659 371 ARG A C   
2916 O O   . ARG A 371 ? 1.1581 1.1111 0.8246 -0.0914 0.1507  -0.0781 371 ARG A O   
2917 C CB  . ARG A 371 ? 1.2179 1.0759 0.8081 -0.1462 0.1906  -0.0696 371 ARG A CB  
2918 C CG  . ARG A 371 ? 1.2602 1.1932 0.8650 -0.1508 0.2032  -0.0866 371 ARG A CG  
2919 C CD  . ARG A 371 ? 1.2727 1.1914 0.8425 -0.1841 0.2306  -0.0903 371 ARG A CD  
2920 N NE  . ARG A 371 ? 1.3025 1.3029 0.8930 -0.1927 0.2465  -0.1117 371 ARG A NE  
2921 C CZ  . ARG A 371 ? 1.3256 1.3562 0.9130 -0.2315 0.2748  -0.1282 371 ARG A CZ  
2922 N NH1 . ARG A 371 ? 1.3660 1.3459 0.9263 -0.2671 0.2913  -0.1250 371 ARG A NH1 
2923 N NH2 . ARG A 371 ? 1.3074 1.4215 0.9204 -0.2347 0.2873  -0.1497 371 ARG A NH2 
2924 N N   . TYR A 372 ? 1.0322 0.9422 0.6611 -0.0600 0.1380  -0.0604 372 TYR A N   
2925 C CA  . TYR A 372 ? 1.0039 0.9717 0.6636 -0.0365 0.1265  -0.0688 372 TYR A CA  
2926 C C   . TYR A 372 ? 0.9768 0.9445 0.6220 -0.0149 0.1217  -0.0666 372 TYR A C   
2927 O O   . TYR A 372 ? 1.0074 0.9203 0.6222 -0.0079 0.1151  -0.0534 372 TYR A O   
2928 C CB  . TYR A 372 ? 0.9451 0.9040 0.6235 -0.0188 0.1053  -0.0619 372 TYR A CB  
2929 C CG  . TYR A 372 ? 0.9336 0.8231 0.5929 -0.0130 0.0934  -0.0455 372 TYR A CG  
2930 C CD1 . TYR A 372 ? 0.9537 0.8086 0.6096 -0.0310 0.0989  -0.0427 372 TYR A CD1 
2931 C CD2 . TYR A 372 ? 0.9159 0.7769 0.5630 0.0112  0.0762  -0.0346 372 TYR A CD2 
2932 C CE1 . TYR A 372 ? 0.9872 0.7841 0.6308 -0.0223 0.0866  -0.0292 372 TYR A CE1 
2933 C CE2 . TYR A 372 ? 0.9184 0.7242 0.5526 0.0167  0.0639  -0.0215 372 TYR A CE2 
2934 C CZ  . TYR A 372 ? 0.9415 0.7175 0.5756 0.0014  0.0685  -0.0188 372 TYR A CZ  
2935 O OH  . TYR A 372 ? 0.9343 0.6613 0.5608 0.0100  0.0551  -0.0075 372 TYR A OH  
2936 N N   . TYR A 373 ? 0.9801 1.0102 0.6479 -0.0029 0.1240  -0.0808 373 TYR A N   
2937 C CA  . TYR A 373 ? 0.9979 1.0322 0.6551 0.0188  0.1217  -0.0829 373 TYR A CA  
2938 C C   . TYR A 373 ? 1.0041 1.0158 0.6639 0.0516  0.0968  -0.0729 373 TYR A C   
2939 O O   . TYR A 373 ? 0.9901 1.0222 0.6745 0.0635  0.0834  -0.0725 373 TYR A O   
2940 C CB  . TYR A 373 ? 1.0224 1.1345 0.7063 0.0214  0.1343  -0.1042 373 TYR A CB  
2941 C CG  . TYR A 373 ? 1.0259 1.1389 0.6925 0.0335  0.1418  -0.1104 373 TYR A CG  
2942 C CD1 . TYR A 373 ? 1.0491 1.1522 0.6877 0.0075  0.1651  -0.1150 373 TYR A CD1 
2943 C CD2 . TYR A 373 ? 1.0359 1.1539 0.7097 0.0695  0.1267  -0.1118 373 TYR A CD2 
2944 C CE1 . TYR A 373 ? 1.0444 1.1488 0.6643 0.0165  0.1738  -0.1223 373 TYR A CE1 
2945 C CE2 . TYR A 373 ? 1.0540 1.1709 0.7107 0.0805  0.1352  -0.1200 373 TYR A CE2 
2946 C CZ  . TYR A 373 ? 1.0455 1.1581 0.6761 0.0535  0.1590  -0.1259 373 TYR A CZ  
2947 O OH  . TYR A 373 ? 1.0861 1.1988 0.6974 0.0622  0.1691  -0.1357 373 TYR A OH  
2948 N N   . LEU A 374 ? 0.9549 0.9237 0.5862 0.0640  0.0912  -0.0654 374 LEU A N   
2949 C CA  . LEU A 374 ? 0.9652 0.9001 0.5911 0.0894  0.0693  -0.0554 374 LEU A CA  
2950 C C   . LEU A 374 ? 1.0041 0.9416 0.6187 0.1114  0.0684  -0.0624 374 LEU A C   
2951 O O   . LEU A 374 ? 1.0138 0.9525 0.6086 0.1037  0.0835  -0.0693 374 LEU A O   
2952 C CB  . LEU A 374 ? 0.9706 0.8404 0.5703 0.0819  0.0598  -0.0390 374 LEU A CB  
2953 C CG  . LEU A 374 ? 0.9978 0.8524 0.6074 0.0650  0.0579  -0.0315 374 LEU A CG  
2954 C CD1 . LEU A 374 ? 0.9622 0.7554 0.5447 0.0606  0.0495  -0.0171 374 LEU A CD1 
2955 C CD2 . LEU A 374 ? 0.9539 0.8280 0.5931 0.0762  0.0446  -0.0317 374 LEU A CD2 
2956 N N   . GLN A 375 ? 1.0999 1.0340 0.7239 0.1377  0.0516  -0.0608 375 GLN A N   
2957 C CA  . GLN A 375 ? 1.0949 1.0098 0.7022 0.1604  0.0466  -0.0646 375 GLN A CA  
2958 C C   . GLN A 375 ? 1.1181 0.9807 0.7128 0.1705  0.0258  -0.0510 375 GLN A C   
2959 O O   . GLN A 375 ? 1.0633 0.9299 0.6751 0.1804  0.0133  -0.0463 375 GLN A O   
2960 C CB  . GLN A 375 ? 1.0693 1.0342 0.7014 0.1850  0.0484  -0.0796 375 GLN A CB  
2961 C CG  . GLN A 375 ? 1.1164 1.1283 0.7540 0.1800  0.0707  -0.0983 375 GLN A CG  
2962 C CD  . GLN A 375 ? 1.0964 1.1609 0.7633 0.2099  0.0702  -0.1148 375 GLN A CD  
2963 O OE1 . GLN A 375 ? 1.0746 1.1368 0.7549 0.2347  0.0519  -0.1098 375 GLN A OE1 
2964 N NE2 . GLN A 375 ? 1.0950 1.2056 0.7705 0.2085  0.0903  -0.1347 375 GLN A NE2 
2965 N N   . ILE A 376 ? 0.9458 0.7609 0.5094 0.1662  0.0220  -0.0451 376 ILE A N   
2966 C CA  . ILE A 376 ? 0.9497 0.7192 0.5031 0.1698  0.0034  -0.0337 376 ILE A CA  
2967 C C   . ILE A 376 ? 1.0077 0.7435 0.5334 0.1830  -0.0018 -0.0377 376 ILE A C   
2968 O O   . ILE A 376 ? 1.0082 0.7351 0.5089 0.1774  0.0070  -0.0425 376 ILE A O   
2969 C CB  . ILE A 376 ? 0.9369 0.6804 0.4827 0.1491  -0.0006 -0.0218 376 ILE A CB  
2970 C CG1 . ILE A 376 ? 0.9192 0.6908 0.4915 0.1353  0.0055  -0.0197 376 ILE A CG1 
2971 C CG2 . ILE A 376 ? 0.9277 0.6315 0.4660 0.1530  -0.0194 -0.0136 376 ILE A CG2 
2972 C CD1 . ILE A 376 ? 0.9121 0.6573 0.4767 0.1169  0.0046  -0.0100 376 ILE A CD1 
2973 N N   . CYS A 377 ? 1.0558 0.7695 0.5819 0.1979  -0.0154 -0.0359 377 CYS A N   
2974 C CA  . CYS A 377 ? 1.1086 0.7804 0.6065 0.2064  -0.0226 -0.0390 377 CYS A CA  
2975 C C   . CYS A 377 ? 1.1083 0.7443 0.6006 0.1962  -0.0388 -0.0281 377 CYS A C   
2976 O O   . CYS A 377 ? 1.0554 0.6925 0.5657 0.1968  -0.0465 -0.0219 377 CYS A O   
2977 C CB  . CYS A 377 ? 1.1018 0.7722 0.6015 0.2322  -0.0234 -0.0481 377 CYS A CB  
2978 S SG  . CYS A 377 ? 1.1127 0.8301 0.6220 0.2479  -0.0043 -0.0661 377 CYS A SG  
2979 N N   . THR A 378 ? 1.1123 0.7199 0.5799 0.1859  -0.0441 -0.0267 378 THR A N   
2980 C CA  . THR A 378 ? 1.0847 0.6697 0.5542 0.1747  -0.0594 -0.0181 378 THR A CA  
2981 C C   . THR A 378 ? 1.1555 0.7037 0.5958 0.1733  -0.0696 -0.0223 378 THR A C   
2982 O O   . THR A 378 ? 1.1469 0.6861 0.5600 0.1717  -0.0663 -0.0271 378 THR A O   
2983 C CB  . THR A 378 ? 1.0915 0.6870 0.5703 0.1594  -0.0601 -0.0090 378 THR A CB  
2984 O OG1 . THR A 378 ? 1.0580 0.6397 0.5473 0.1517  -0.0750 -0.0031 378 THR A OG1 
2985 C CG2 . THR A 378 ? 1.0827 0.6691 0.5321 0.1530  -0.0559 -0.0088 378 THR A CG2 
2986 N N   . LEU A 379 ? 1.1511 0.6787 0.5949 0.1718  -0.0808 -0.0218 379 LEU A N   
2987 C CA  . LEU A 379 ? 1.1352 0.6340 0.5592 0.1627  -0.0936 -0.0247 379 LEU A CA  
2988 C C   . LEU A 379 ? 1.1361 0.6459 0.5797 0.1487  -0.1048 -0.0163 379 LEU A C   
2989 O O   . LEU A 379 ? 1.0767 0.6003 0.5488 0.1453  -0.1054 -0.0114 379 LEU A O   
2990 C CB  . LEU A 379 ? 1.1130 0.5824 0.5293 0.1657  -0.0978 -0.0305 379 LEU A CB  
2991 C CG  . LEU A 379 ? 1.1504 0.5985 0.5611 0.1498  -0.1119 -0.0329 379 LEU A CG  
2992 C CD1 . LEU A 379 ? 1.1896 0.6201 0.5685 0.1449  -0.1178 -0.0416 379 LEU A CD1 
2993 C CD2 . LEU A 379 ? 1.1427 0.5615 0.5480 0.1501  -0.1121 -0.0361 379 LEU A CD2 
2994 N N   . LEU A 380 ? 1.1736 0.6783 0.6018 0.1418  -0.1138 -0.0150 380 LEU A N   
2995 C CA  . LEU A 380 ? 1.1538 0.6709 0.6046 0.1333  -0.1253 -0.0074 380 LEU A CA  
2996 C C   . LEU A 380 ? 1.1767 0.6820 0.6106 0.1268  -0.1433 -0.0095 380 LEU A C   
2997 O O   . LEU A 380 ? 1.2201 0.7090 0.6181 0.1272  -0.1454 -0.0137 380 LEU A O   
2998 C CB  . LEU A 380 ? 1.1501 0.6845 0.6115 0.1341  -0.1178 0.0022  380 LEU A CB  
2999 C CG  . LEU A 380 ? 1.1457 0.6763 0.5774 0.1361  -0.1074 0.0043  380 LEU A CG  
3000 C CD1 . LEU A 380 ? 1.1708 0.6820 0.5694 0.1323  -0.1208 0.0068  380 LEU A CD1 
3001 C CD2 . LEU A 380 ? 1.1259 0.6732 0.5736 0.1334  -0.0962 0.0123  380 LEU A CD2 
3002 N N   . LYS A 381 ? 1.0200 0.5375 0.4813 0.1207  -0.1565 -0.0077 381 LYS A N   
3003 C CA  . LYS A 381 ? 1.0456 0.5624 0.5002 0.1159  -0.1770 -0.0093 381 LYS A CA  
3004 C C   . LYS A 381 ? 1.0504 0.5689 0.4962 0.1215  -0.1833 0.0027  381 LYS A C   
3005 O O   . LYS A 381 ? 1.0272 0.5580 0.4995 0.1248  -0.1805 0.0107  381 LYS A O   
3006 C CB  . LYS A 381 ? 1.0206 0.5559 0.5132 0.1079  -0.1878 -0.0147 381 LYS A CB  
3007 C CG  . LYS A 381 ? 1.0474 0.5898 0.5383 0.1031  -0.2108 -0.0198 381 LYS A CG  
3008 C CD  . LYS A 381 ? 1.0452 0.6168 0.5794 0.1051  -0.2226 -0.0175 381 LYS A CD  
3009 C CE  . LYS A 381 ? 1.0430 0.6293 0.5800 0.1023  -0.2485 -0.0242 381 LYS A CE  
3010 N NZ  . LYS A 381 ? 1.0732 0.6479 0.5802 0.1140  -0.2618 -0.0123 381 LYS A NZ  
3011 N N   . CYS A 382 ? 0.8852 0.6402 0.6750 0.0414  -0.0359 0.0344  382 CYS A N   
3012 C CA  . CYS A 382 ? 0.9052 0.6364 0.6745 0.0408  -0.0423 0.0396  382 CYS A CA  
3013 C C   . CYS A 382 ? 0.9039 0.6269 0.6807 0.0476  -0.0608 0.0322  382 CYS A C   
3014 O O   . CYS A 382 ? 0.8642 0.6005 0.6524 0.0524  -0.0709 0.0232  382 CYS A O   
3015 C CB  . CYS A 382 ? 0.9543 0.6636 0.6865 0.0437  -0.0396 0.0458  382 CYS A CB  
3016 S SG  . CYS A 382 ? 0.9455 0.6713 0.6717 0.0442  -0.0149 0.0526  382 CYS A SG  
3017 N N   . LYS A 383 ? 0.8934 0.5954 0.6637 0.0477  -0.0641 0.0362  383 LYS A N   
3018 C CA  . LYS A 383 ? 0.8740 0.5694 0.6550 0.0605  -0.0786 0.0292  383 LYS A CA  
3019 C C   . LYS A 383 ? 0.9279 0.6252 0.6997 0.0742  -0.0954 0.0290  383 LYS A C   
3020 O O   . LYS A 383 ? 0.8899 0.6166 0.6849 0.0818  -0.1053 0.0191  383 LYS A O   
3021 C CB  . LYS A 383 ? 0.8984 0.5526 0.6615 0.0603  -0.0780 0.0354  383 LYS A CB  
3022 C CG  . LYS A 383 ? 0.9153 0.5577 0.6900 0.0781  -0.0880 0.0267  383 LYS A CG  
3023 C CD  . LYS A 383 ? 0.9704 0.5517 0.7123 0.0831  -0.0900 0.0369  383 LYS A CD  
3024 C CE  . LYS A 383 ? 1.0447 0.6028 0.7951 0.0985  -0.0917 0.0253  383 LYS A CE  
3025 N NZ  . LYS A 383 ? 1.2027 0.7072 0.9279 0.0796  -0.0796 0.0257  383 LYS A NZ  
3026 N N   . THR A 384 ? 0.8818 0.5553 0.6190 0.0748  -0.0987 0.0403  384 THR A N   
3027 C CA  . THR A 384 ? 0.9000 0.5808 0.6216 0.0819  -0.1139 0.0411  384 THR A CA  
3028 C C   . THR A 384 ? 0.9324 0.6096 0.6285 0.0690  -0.1039 0.0417  384 THR A C   
3029 O O   . THR A 384 ? 0.9198 0.5965 0.6188 0.0599  -0.0857 0.0414  384 THR A O   
3030 C CB  . THR A 384 ? 0.9898 0.6447 0.6876 0.0971  -0.1284 0.0549  384 THR A CB  
3031 O OG1 . THR A 384 ? 0.9619 0.5814 0.6220 0.0884  -0.1204 0.0695  384 THR A OG1 
3032 C CG2 . THR A 384 ? 0.9485 0.5896 0.6646 0.1137  -0.1322 0.0547  384 THR A CG2 
3033 N N   . THR A 385 ? 0.9023 0.5807 0.5730 0.0692  -0.1154 0.0418  385 THR A N   
3034 C CA  . THR A 385 ? 0.9470 0.6153 0.5857 0.0585  -0.1052 0.0391  385 THR A CA  
3035 C C   . THR A 385 ? 0.9156 0.5584 0.5194 0.0570  -0.0959 0.0534  385 THR A C   
3036 O O   . THR A 385 ? 0.9265 0.5624 0.5059 0.0506  -0.0813 0.0508  385 THR A O   
3037 C CB  . THR A 385 ? 0.9728 0.6532 0.5922 0.0531  -0.1204 0.0305  385 THR A CB  
3038 O OG1 . THR A 385 ? 0.9384 0.6320 0.5562 0.0635  -0.1427 0.0395  385 THR A OG1 
3039 C CG2 . THR A 385 ? 0.9816 0.6852 0.6283 0.0447  -0.1217 0.0143  385 THR A CG2 
3040 N N   . ASN A 386 ? 0.9667 0.5934 0.5658 0.0626  -0.1024 0.0683  386 ASN A N   
3041 C CA  . ASN A 386 ? 0.9896 0.5931 0.5560 0.0559  -0.0924 0.0840  386 ASN A CA  
3042 C C   . ASN A 386 ? 0.9657 0.5757 0.5469 0.0459  -0.0694 0.0835  386 ASN A C   
3043 O O   . ASN A 386 ? 0.9694 0.5816 0.5791 0.0445  -0.0668 0.0826  386 ASN A O   
3044 C CB  . ASN A 386 ? 1.0188 0.5938 0.5736 0.0628  -0.1053 0.1013  386 ASN A CB  
3045 C CG  . ASN A 386 ? 1.0549 0.6036 0.5673 0.0518  -0.0981 0.1206  386 ASN A CG  
3046 O OD1 . ASN A 386 ? 1.0472 0.6029 0.5522 0.0371  -0.0783 0.1215  386 ASN A OD1 
3047 N ND2 . ASN A 386 ? 1.0975 0.6195 0.5820 0.0595  -0.1139 0.1382  386 ASN A ND2 
3048 N N   . LEU A 387 ? 1.0842 0.7007 0.6439 0.0395  -0.0525 0.0847  387 LEU A N   
3049 C CA  . LEU A 387 ? 1.0847 0.7208 0.6596 0.0326  -0.0304 0.0869  387 LEU A CA  
3050 C C   . LEU A 387 ? 1.0649 0.6945 0.6428 0.0191  -0.0274 0.1011  387 LEU A C   
3051 O O   . LEU A 387 ? 1.0705 0.7258 0.6685 0.0103  -0.0124 0.1026  387 LEU A O   
3052 C CB  . LEU A 387 ? 1.0991 0.7451 0.6448 0.0321  -0.0123 0.0882  387 LEU A CB  
3053 C CG  . LEU A 387 ? 1.1317 0.7691 0.6590 0.0413  -0.0149 0.0726  387 LEU A CG  
3054 C CD1 . LEU A 387 ? 1.1352 0.7718 0.6194 0.0417  0.0012  0.0722  387 LEU A CD1 
3055 C CD2 . LEU A 387 ? 1.0589 0.7061 0.6192 0.0491  -0.0096 0.0583  387 LEU A CD2 
3056 N N   . ASN A 388 ? 0.9753 0.5702 0.5297 0.0161  -0.0409 0.1126  388 ASN A N   
3057 C CA  . ASN A 388 ? 0.9948 0.5687 0.5450 0.0000  -0.0381 0.1246  388 ASN A CA  
3058 C C   . ASN A 388 ? 0.9725 0.5488 0.5603 0.0002  -0.0400 0.1135  388 ASN A C   
3059 O O   . ASN A 388 ? 0.9900 0.5529 0.5757 -0.0183 -0.0339 0.1187  388 ASN A O   
3060 C CB  . ASN A 388 ? 1.0502 0.5746 0.5622 0.0007  -0.0526 0.1408  388 ASN A CB  
3061 C CG  . ASN A 388 ? 1.0862 0.6120 0.5561 -0.0048 -0.0493 0.1538  388 ASN A CG  
3062 O OD1 . ASN A 388 ? 1.0931 0.6488 0.5559 -0.0183 -0.0306 0.1560  388 ASN A OD1 
3063 N ND2 . ASN A 388 ? 1.1269 0.6253 0.5681 0.0064  -0.0672 0.1637  388 ASN A ND2 
3064 N N   . THR A 389 ? 1.0432 0.6350 0.6609 0.0175  -0.0485 0.0980  389 THR A N   
3065 C CA  . THR A 389 ? 1.0453 0.6417 0.6968 0.0200  -0.0517 0.0861  389 THR A CA  
3066 C C   . THR A 389 ? 1.0030 0.6475 0.6897 0.0164  -0.0399 0.0756  389 THR A C   
3067 O O   . THR A 389 ? 1.0130 0.6703 0.7292 0.0187  -0.0427 0.0643  389 THR A O   
3068 C CB  . THR A 389 ? 1.0046 0.5898 0.6662 0.0425  -0.0711 0.0782  389 THR A CB  
3069 O OG1 . THR A 389 ? 0.9890 0.6042 0.6600 0.0516  -0.0757 0.0700  389 THR A OG1 
3070 C CG2 . THR A 389 ? 1.0493 0.5876 0.6773 0.0519  -0.0841 0.0921  389 THR A CG2 
3071 N N   . CYS A 390 ? 1.0367 0.7082 0.7196 0.0135  -0.0263 0.0796  390 CYS A N   
3072 C CA  . CYS A 390 ? 1.0025 0.7179 0.7160 0.0120  -0.0133 0.0751  390 CYS A CA  
3073 C C   . CYS A 390 ? 0.9881 0.7220 0.7123 -0.0087 -0.0045 0.0806  390 CYS A C   
3074 O O   . CYS A 390 ? 1.0042 0.7400 0.7082 -0.0246 0.0044  0.0928  390 CYS A O   
3075 C CB  . CYS A 390 ? 1.0319 0.7672 0.7351 0.0195  0.0012  0.0793  390 CYS A CB  
3076 S SG  . CYS A 390 ? 1.0273 0.7398 0.7126 0.0374  -0.0062 0.0683  390 CYS A SG  
3077 N N   . GLY A 391 ? 0.9514 0.7008 0.7045 -0.0121 -0.0071 0.0711  391 GLY A N   
3078 C CA  . GLY A 391 ? 0.9561 0.7192 0.7162 -0.0358 -0.0013 0.0719  391 GLY A CA  
3079 C C   . GLY A 391 ? 0.9736 0.6940 0.7290 -0.0398 -0.0121 0.0608  391 GLY A C   
3080 O O   . GLY A 391 ? 1.0024 0.7349 0.7680 -0.0579 -0.0081 0.0541  391 GLY A O   
3081 N N   . ASP A 392 ? 1.0248 0.6980 0.7642 -0.0218 -0.0253 0.0583  392 ASP A N   
3082 C CA  . ASP A 392 ? 1.0194 0.6524 0.7566 -0.0156 -0.0348 0.0472  392 ASP A CA  
3083 C C   . ASP A 392 ? 1.0296 0.6996 0.8049 -0.0072 -0.0367 0.0302  392 ASP A C   
3084 O O   . ASP A 392 ? 0.9494 0.6621 0.7482 0.0008  -0.0364 0.0289  392 ASP A O   
3085 C CB  . ASP A 392 ? 1.0564 0.6449 0.7732 0.0086  -0.0495 0.0515  392 ASP A CB  
3086 C CG  . ASP A 392 ? 1.1793 0.7189 0.8515 -0.0013 -0.0490 0.0697  392 ASP A CG  
3087 O OD1 . ASP A 392 ? 1.1362 0.6752 0.7933 -0.0298 -0.0367 0.0773  392 ASP A OD1 
3088 O OD2 . ASP A 392 ? 1.2138 0.7199 0.8653 0.0179  -0.0615 0.0778  392 ASP A OD2 
3089 N N   . SER A 393 ? 0.9675 0.6170 0.7449 -0.0097 -0.0376 0.0169  393 SER A N   
3090 C CA  . SER A 393 ? 0.9347 0.6207 0.7456 -0.0021 -0.0390 -0.0001 393 SER A CA  
3091 C C   . SER A 393 ? 0.9484 0.6499 0.7767 0.0260  -0.0515 -0.0028 393 SER A C   
3092 O O   . SER A 393 ? 0.9445 0.6119 0.7578 0.0461  -0.0623 0.0003  393 SER A O   
3093 C CB  . SER A 393 ? 0.9623 0.6127 0.7646 -0.0048 -0.0373 -0.0165 393 SER A CB  
3094 O OG  . SER A 393 ? 0.9635 0.6266 0.7884 0.0203  -0.0444 -0.0321 393 SER A OG  
3095 N N   . ALA A 394 ? 0.8428 0.5976 0.7007 0.0253  -0.0503 -0.0069 394 ALA A N   
3096 C CA  . ALA A 394 ? 0.7913 0.5684 0.6657 0.0431  -0.0613 -0.0107 394 ALA A CA  
3097 C C   . ALA A 394 ? 0.8151 0.6390 0.7224 0.0406  -0.0598 -0.0243 394 ALA A C   
3098 O O   . ALA A 394 ? 0.7454 0.6023 0.6660 0.0248  -0.0508 -0.0217 394 ALA A O   
3099 C CB  . ALA A 394 ? 0.7918 0.5794 0.6599 0.0399  -0.0599 0.0010  394 ALA A CB  
3100 N N   . GLU A 395 ? 1.1255 0.9579 1.0463 0.0571  -0.0679 -0.0375 395 GLU A N   
3101 C CA  . GLU A 395 ? 1.1367 1.0229 1.0883 0.0507  -0.0648 -0.0492 395 GLU A CA  
3102 C C   . GLU A 395 ? 1.1036 1.0320 1.0739 0.0504  -0.0718 -0.0474 395 GLU A C   
3103 O O   . GLU A 395 ? 1.0547 1.0273 1.0473 0.0401  -0.0680 -0.0533 395 GLU A O   
3104 C CB  . GLU A 395 ? 1.1091 1.0109 1.0762 0.0622  -0.0643 -0.0690 395 GLU A CB  
3105 C CG  . GLU A 395 ? 1.2385 1.1059 1.1926 0.0643  -0.0557 -0.0843 395 GLU A CG  
3106 C CD  . GLU A 395 ? 1.4086 1.2315 1.3493 0.0949  -0.0605 -0.0927 395 GLU A CD  
3107 O OE1 . GLU A 395 ? 1.4040 1.2573 1.3645 0.1212  -0.0685 -0.0994 395 GLU A OE1 
3108 O OE2 . GLU A 395 ? 1.4350 1.1853 1.3406 0.0933  -0.0552 -0.0920 395 GLU A OE2 
3109 N N   . THR A 396 ? 0.8051 0.7227 0.7645 0.0573  -0.0817 -0.0398 396 THR A N   
3110 C CA  . THR A 396 ? 0.7953 0.7533 0.7703 0.0509  -0.0882 -0.0417 396 THR A CA  
3111 C C   . THR A 396 ? 0.8284 0.7641 0.7818 0.0413  -0.0885 -0.0303 396 THR A C   
3112 O O   . THR A 396 ? 0.8615 0.7567 0.7892 0.0462  -0.0874 -0.0222 396 THR A O   
3113 C CB  . THR A 396 ? 0.8003 0.7864 0.7879 0.0676  -0.1025 -0.0500 396 THR A CB  
3114 O OG1 . THR A 396 ? 0.8743 0.8250 0.8392 0.0845  -0.1122 -0.0431 396 THR A OG1 
3115 C CG2 . THR A 396 ? 0.7713 0.7834 0.7812 0.0809  -0.0995 -0.0642 396 THR A CG2 
3116 N N   . ALA A 397 ? 0.7466 0.7052 0.7070 0.0263  -0.0884 -0.0302 397 ALA A N   
3117 C CA  . ALA A 397 ? 0.7859 0.7151 0.7207 0.0172  -0.0868 -0.0227 397 ALA A CA  
3118 C C   . ALA A 397 ? 0.7981 0.7527 0.7387 -0.0005 -0.0924 -0.0270 397 ALA A C   
3119 O O   . ALA A 397 ? 0.7439 0.7433 0.7111 -0.0079 -0.0938 -0.0321 397 ALA A O   
3120 C CB  . ALA A 397 ? 0.7401 0.6440 0.6642 0.0145  -0.0702 -0.0115 397 ALA A CB  
3121 N N   . SER A 398 ? 0.8230 0.7478 0.7347 -0.0103 -0.0950 -0.0257 398 SER A N   
3122 C CA  . SER A 398 ? 0.8005 0.7365 0.7069 -0.0343 -0.0997 -0.0297 398 SER A CA  
3123 C C   . SER A 398 ? 0.8778 0.7628 0.7555 -0.0460 -0.0862 -0.0231 398 SER A C   
3124 O O   . SER A 398 ? 0.8883 0.7735 0.7603 -0.0690 -0.0862 -0.0240 398 SER A O   
3125 C CB  . SER A 398 ? 0.9036 0.8514 0.7956 -0.0415 -0.1171 -0.0376 398 SER A CB  
3126 O OG  . SER A 398 ? 0.9063 0.8963 0.8207 -0.0228 -0.1299 -0.0409 398 SER A OG  
3127 N N   . THR A 399 ? 0.8526 0.6932 0.7103 -0.0304 -0.0739 -0.0159 399 THR A N   
3128 C CA  . THR A 399 ? 0.9088 0.6963 0.7361 -0.0329 -0.0591 -0.0097 399 THR A CA  
3129 C C   . THR A 399 ? 0.8854 0.6843 0.7329 -0.0312 -0.0466 0.0031  399 THR A C   
3130 O O   . THR A 399 ? 0.8674 0.6837 0.7331 -0.0149 -0.0384 0.0123  399 THR A O   
3131 C CB  . THR A 399 ? 0.9037 0.6520 0.7050 -0.0135 -0.0493 -0.0063 399 THR A CB  
3132 O OG1 . THR A 399 ? 0.9690 0.7075 0.7474 -0.0168 -0.0616 -0.0165 399 THR A OG1 
3133 C CG2 . THR A 399 ? 0.9339 0.6274 0.7040 -0.0090 -0.0310 -0.0006 399 THR A CG2 
3134 N N   . ARG A 400 ? 0.9649 0.7539 0.8057 -0.0505 -0.0453 0.0052  400 ARG A N   
3135 C CA  . ARG A 400 ? 0.9683 0.7570 0.8186 -0.0473 -0.0323 0.0218  400 ARG A CA  
3136 C C   . ARG A 400 ? 1.0112 0.7340 0.8269 -0.0301 -0.0150 0.0319  400 ARG A C   
3137 O O   . ARG A 400 ? 1.0457 0.7161 0.8243 -0.0293 -0.0130 0.0225  400 ARG A O   
3138 C CB  . ARG A 400 ? 1.0016 0.8052 0.8566 -0.0758 -0.0372 0.0232  400 ARG A CB  
3139 C CG  . ARG A 400 ? 0.9345 0.8184 0.8322 -0.0871 -0.0483 0.0180  400 ARG A CG  
3140 C CD  . ARG A 400 ? 0.9286 0.8336 0.8238 -0.1194 -0.0608 0.0075  400 ARG A CD  
3141 N NE  . ARG A 400 ? 1.1112 0.9501 0.9634 -0.1403 -0.0563 0.0109  400 ARG A NE  
3142 C CZ  . ARG A 400 ? 1.1882 1.0114 1.0151 -0.1670 -0.0660 -0.0019 400 ARG A CZ  
3143 N NH1 . ARG A 400 ? 1.1300 0.9975 0.9693 -0.1692 -0.0814 -0.0171 400 ARG A NH1 
3144 N NH2 . ARG A 400 ? 1.2684 1.0234 1.0516 -0.1904 -0.0596 0.0011  400 ARG A NH2 
3145 N N   . PHE A 401 ? 1.3948 0.6334 0.8169 -0.0439 -0.2276 -0.1050 401 PHE A N   
3146 C CA  . PHE A 401 ? 1.3931 0.5737 0.7973 -0.0192 -0.2291 -0.1165 401 PHE A CA  
3147 C C   . PHE A 401 ? 1.4459 0.5638 0.8501 -0.0365 -0.2406 -0.1053 401 PHE A C   
3148 O O   . PHE A 401 ? 1.4396 0.5655 0.8581 -0.0512 -0.2379 -0.0779 401 PHE A O   
3149 C CB  . PHE A 401 ? 1.3590 0.5596 0.7666 0.0153  -0.2123 -0.1091 401 PHE A CB  
3150 C CG  . PHE A 401 ? 1.3943 0.6283 0.7891 0.0389  -0.2026 -0.1264 401 PHE A CG  
3151 C CD1 . PHE A 401 ? 1.3438 0.6334 0.7435 0.0322  -0.1978 -0.1222 401 PHE A CD1 
3152 C CD2 . PHE A 401 ? 1.3792 0.5897 0.7563 0.0678  -0.1987 -0.1468 401 PHE A CD2 
3153 C CE1 . PHE A 401 ? 1.2962 0.6123 0.6795 0.0519  -0.1899 -0.1337 401 PHE A CE1 
3154 C CE2 . PHE A 401 ? 1.3604 0.6047 0.7218 0.0858  -0.1885 -0.1609 401 PHE A CE2 
3155 C CZ  . PHE A 401 ? 1.3146 0.6091 0.6769 0.0767  -0.1844 -0.1522 401 PHE A CZ  
3156 N N   . GLU A 402 ? 1.5504 0.6046 0.9370 -0.0357 -0.2542 -0.1266 402 GLU A N   
3157 C CA  . GLU A 402 ? 1.5923 0.5716 0.9751 -0.0463 -0.2671 -0.1164 402 GLU A CA  
3158 C C   . GLU A 402 ? 1.5844 0.5419 0.9698 -0.0117 -0.2614 -0.1035 402 GLU A C   
3159 O O   . GLU A 402 ? 1.6369 0.5596 1.0261 -0.0210 -0.2677 -0.0775 402 GLU A O   
3160 C CB  . GLU A 402 ? 1.6472 0.5606 1.0114 -0.0518 -0.2837 -0.1470 402 GLU A CB  
3161 C CG  . GLU A 402 ? 1.6717 0.6023 1.0352 -0.0922 -0.2929 -0.1584 402 GLU A CG  
3162 C CD  . GLU A 402 ? 1.6414 0.5697 1.0175 -0.1382 -0.2983 -0.1296 402 GLU A CD  
3163 O OE1 . GLU A 402 ? 1.7028 0.5682 1.0767 -0.1554 -0.3086 -0.1207 402 GLU A OE1 
3164 O OE2 . GLU A 402 ? 1.6205 0.6213 1.0139 -0.1557 -0.2893 -0.1145 402 GLU A OE2 
3165 N N   . MET A 403 ? 1.6392 0.6195 1.0220 0.0274  -0.2501 -0.1209 403 MET A N   
3166 C CA  . MET A 403 ? 1.6183 0.5898 1.0078 0.0617  -0.2441 -0.1119 403 MET A CA  
3167 C C   . MET A 403 ? 1.5831 0.6172 0.9757 0.0920  -0.2245 -0.1246 403 MET A C   
3168 O O   . MET A 403 ? 1.6050 0.6630 0.9857 0.0953  -0.2197 -0.1482 403 MET A O   
3169 C CB  . MET A 403 ? 1.6466 0.5480 1.0313 0.0815  -0.2572 -0.1273 403 MET A CB  
3170 C CG  . MET A 403 ? 1.6646 0.5788 1.0602 0.1269  -0.2484 -0.1333 403 MET A CG  
3171 S SD  . MET A 403 ? 1.7524 0.6929 1.1426 0.1597  -0.2373 -0.1791 403 MET A SD  
3172 C CE  . MET A 403 ? 1.7038 0.6619 1.1139 0.2071  -0.2284 -0.1802 403 MET A CE  
3173 N N   . PHE A 404 ? 1.4436 0.5042 0.8506 0.1124  -0.2138 -0.1081 404 PHE A N   
3174 C CA  . PHE A 404 ? 1.4322 0.5443 0.8425 0.1420  -0.1951 -0.1203 404 PHE A CA  
3175 C C   . PHE A 404 ? 1.4261 0.5327 0.8503 0.1713  -0.1928 -0.1123 404 PHE A C   
3176 O O   . PHE A 404 ? 1.4861 0.5616 0.9179 0.1654  -0.2042 -0.0896 404 PHE A O   
3177 C CB  . PHE A 404 ? 1.3907 0.5744 0.8093 0.1276  -0.1793 -0.1066 404 PHE A CB  
3178 C CG  . PHE A 404 ? 1.3201 0.5316 0.7595 0.1144  -0.1751 -0.0747 404 PHE A CG  
3179 C CD1 . PHE A 404 ? 1.3261 0.5617 0.7800 0.1358  -0.1650 -0.0649 404 PHE A CD1 
3180 C CD2 . PHE A 404 ? 1.3431 0.5638 0.7884 0.0798  -0.1807 -0.0570 404 PHE A CD2 
3181 C CE1 . PHE A 404 ? 1.2765 0.5407 0.7476 0.1228  -0.1616 -0.0379 404 PHE A CE1 
3182 C CE2 . PHE A 404 ? 1.2972 0.5485 0.7602 0.0671  -0.1758 -0.0305 404 PHE A CE2 
3183 C CZ  . PHE A 404 ? 1.2345 0.5063 0.7090 0.0886  -0.1666 -0.0211 404 PHE A CZ  
3184 N N   . SER A 405 ? 1.4344 0.5739 0.8609 0.2025  -0.1785 -0.1312 405 SER A N   
3185 C CA  . SER A 405 ? 1.3989 0.5496 0.8430 0.2328  -0.1743 -0.1271 405 SER A CA  
3186 C C   . SER A 405 ? 1.3878 0.6040 0.8360 0.2523  -0.1511 -0.1431 405 SER A C   
3187 O O   . SER A 405 ? 1.4277 0.6457 0.8613 0.2661  -0.1454 -0.1733 405 SER A O   
3188 C CB  . SER A 405 ? 1.4216 0.5053 0.8635 0.2593  -0.1918 -0.1437 405 SER A CB  
3189 O OG  . SER A 405 ? 1.4230 0.5274 0.8843 0.2940  -0.1877 -0.1447 405 SER A OG  
3190 N N   . LEU A 406 ? 1.2357 0.5058 0.7023 0.2512  -0.1376 -0.1237 406 LEU A N   
3191 C CA  . LEU A 406 ? 1.1951 0.5301 0.6668 0.2617  -0.1141 -0.1331 406 LEU A CA  
3192 C C   . LEU A 406 ? 1.2074 0.5726 0.7040 0.2873  -0.1081 -0.1313 406 LEU A C   
3193 O O   . LEU A 406 ? 1.2606 0.6182 0.7728 0.2856  -0.1181 -0.1090 406 LEU A O   
3194 C CB  . LEU A 406 ? 1.1828 0.5598 0.6556 0.2327  -0.1025 -0.1131 406 LEU A CB  
3195 C CG  . LEU A 406 ? 1.1584 0.5947 0.6315 0.2358  -0.0788 -0.1188 406 LEU A CG  
3196 C CD1 . LEU A 406 ? 1.1151 0.5487 0.5603 0.2422  -0.0732 -0.1446 406 LEU A CD1 
3197 C CD2 . LEU A 406 ? 1.0503 0.5185 0.5308 0.2099  -0.0713 -0.0957 406 LEU A CD2 
3198 N N   . SER A 407 ? 1.2969 0.7017 0.7966 0.3096  -0.0916 -0.1547 407 SER A N   
3199 C CA  . SER A 407 ? 1.2788 0.7256 0.8055 0.3340  -0.0838 -0.1569 407 SER A CA  
3200 C C   . SER A 407 ? 1.3131 0.8242 0.8400 0.3399  -0.0573 -0.1761 407 SER A C   
3201 O O   . SER A 407 ? 1.3240 0.8382 0.8263 0.3298  -0.0476 -0.1888 407 SER A O   
3202 C CB  . SER A 407 ? 1.3151 0.7215 0.8518 0.3687  -0.1019 -0.1716 407 SER A CB  
3203 O OG  . SER A 407 ? 1.4259 0.7929 0.9434 0.3821  -0.1071 -0.2023 407 SER A OG  
3204 N N   . GLY A 408 ? 1.3062 0.8716 0.8598 0.3537  -0.0456 -0.1767 408 GLY A N   
3205 C CA  . GLY A 408 ? 1.2839 0.9146 0.8391 0.3548  -0.0188 -0.1929 408 GLY A CA  
3206 C C   . GLY A 408 ? 1.2743 0.9594 0.8632 0.3802  -0.0109 -0.2045 408 GLY A C   
3207 O O   . GLY A 408 ? 1.2679 0.9523 0.8811 0.3897  -0.0241 -0.1902 408 GLY A O   
3208 N N   . THR A 409 ? 1.2235 0.9619 0.8131 0.3895  0.0113  -0.2300 409 THR A N   
3209 C CA  . THR A 409 ? 1.2378 1.0420 0.8621 0.4130  0.0222  -0.2465 409 THR A CA  
3210 C C   . THR A 409 ? 1.2185 1.0823 0.8596 0.3866  0.0402  -0.2267 409 THR A C   
3211 O O   . THR A 409 ? 1.2048 1.1313 0.8501 0.3780  0.0659  -0.2383 409 THR A O   
3212 C CB  . THR A 409 ? 1.2908 1.1328 0.9097 0.4327  0.0397  -0.2856 409 THR A CB  
3213 O OG1 . THR A 409 ? 1.2723 1.1692 0.8778 0.4038  0.0690  -0.2836 409 THR A OG1 
3214 C CG2 . THR A 409 ? 1.2613 1.0408 0.8492 0.4440  0.0273  -0.3050 409 THR A CG2 
3215 N N   . PHE A 410 ? 1.1073 0.9515 0.7584 0.3728  0.0265  -0.1974 410 PHE A N   
3216 C CA  . PHE A 410 ? 1.1031 0.9927 0.7672 0.3442  0.0412  -0.1786 410 PHE A CA  
3217 C C   . PHE A 410 ? 1.0795 1.0463 0.7813 0.3581  0.0532  -0.1922 410 PHE A C   
3218 O O   . PHE A 410 ? 1.0607 1.0375 0.7866 0.3912  0.0392  -0.2035 410 PHE A O   
3219 C CB  . PHE A 410 ? 1.0647 0.9180 0.7303 0.3273  0.0231  -0.1479 410 PHE A CB  
3220 C CG  . PHE A 410 ? 1.0853 0.8805 0.7187 0.3046  0.0165  -0.1332 410 PHE A CG  
3221 C CD1 . PHE A 410 ? 1.0582 0.8635 0.6794 0.2734  0.0313  -0.1215 410 PHE A CD1 
3222 C CD2 . PHE A 410 ? 1.1315 0.8614 0.7478 0.3146  -0.0055 -0.1320 410 PHE A CD2 
3223 C CE1 . PHE A 410 ? 1.0420 0.7994 0.6367 0.2553  0.0234  -0.1095 410 PHE A CE1 
3224 C CE2 . PHE A 410 ? 1.0921 0.7760 0.6818 0.2927  -0.0119 -0.1205 410 PHE A CE2 
3225 C CZ  . PHE A 410 ? 1.0700 0.7708 0.6500 0.2645  0.0022  -0.1097 410 PHE A CZ  
3226 N N   . GLY A 411 ? 1.1033 1.1250 0.8103 0.3329  0.0786  -0.1919 411 GLY A N   
3227 C CA  . GLY A 411 ? 1.0474 1.1497 0.7918 0.3384  0.0920  -0.2043 411 GLY A CA  
3228 C C   . GLY A 411 ? 1.0630 1.1818 0.8291 0.3204  0.0860  -0.1822 411 GLY A C   
3229 O O   . GLY A 411 ? 1.0597 1.2464 0.8534 0.3099  0.1009  -0.1877 411 GLY A O   
3230 N N   . THR A 412 ? 0.9709 1.0310 0.7246 0.3143  0.0648  -0.1586 412 THR A N   
3231 C CA  . THR A 412 ? 0.9399 1.0139 0.7113 0.2985  0.0568  -0.1389 412 THR A CA  
3232 C C   . THR A 412 ? 0.9503 0.9696 0.7149 0.3133  0.0267  -0.1220 412 THR A C   
3233 O O   . THR A 412 ? 0.9870 0.9459 0.7287 0.3261  0.0136  -0.1216 412 THR A O   
3234 C CB  . THR A 412 ? 0.9000 0.9661 0.6584 0.2577  0.0706  -0.1233 412 THR A CB  
3235 O OG1 . THR A 412 ? 0.9155 1.0024 0.6936 0.2438  0.0638  -0.1096 412 THR A OG1 
3236 C CG2 . THR A 412 ? 0.8861 0.8783 0.6087 0.2484  0.0615  -0.1100 412 THR A CG2 
3237 N N   . GLN A 413 ? 0.9702 1.0132 0.7544 0.3111  0.0153  -0.1088 413 GLN A N   
3238 C CA  . GLN A 413 ? 1.0048 0.9993 0.7793 0.3180  -0.0122 -0.0875 413 GLN A CA  
3239 C C   . GLN A 413 ? 0.9665 0.9380 0.7262 0.2826  -0.0129 -0.0651 413 GLN A C   
3240 O O   . GLN A 413 ? 1.0234 0.9541 0.7705 0.2810  -0.0332 -0.0456 413 GLN A O   
3241 C CB  . GLN A 413 ? 0.9883 1.0217 0.7897 0.3425  -0.0288 -0.0856 413 GLN A CB  
3242 C CG  . GLN A 413 ? 1.0582 1.0899 0.8710 0.3872  -0.0390 -0.1051 413 GLN A CG  
3243 C CD  . GLN A 413 ? 1.0936 1.0399 0.8831 0.4071  -0.0657 -0.0937 413 GLN A CD  
3244 O OE1 . GLN A 413 ? 1.0406 0.9510 0.8205 0.4276  -0.0667 -0.1112 413 GLN A OE1 
3245 N NE2 . GLN A 413 ? 1.1672 1.0812 0.9466 0.3991  -0.0875 -0.0646 413 GLN A NE2 
3246 N N   . TYR A 414 ? 0.9326 0.9260 0.6923 0.2541  0.0086  -0.0679 414 TYR A N   
3247 C CA  . TYR A 414 ? 0.9240 0.8958 0.6718 0.2231  0.0092  -0.0517 414 TYR A CA  
3248 C C   . TYR A 414 ? 0.9746 0.8891 0.6932 0.2160  0.0107  -0.0502 414 TYR A C   
3249 O O   . TYR A 414 ? 0.9618 0.8796 0.6731 0.2035  0.0284  -0.0576 414 TYR A O   
3250 C CB  . TYR A 414 ? 0.8925 0.9160 0.6589 0.1983  0.0290  -0.0568 414 TYR A CB  
3251 C CG  . TYR A 414 ? 0.9092 0.9968 0.7059 0.2025  0.0274  -0.0608 414 TYR A CG  
3252 C CD1 . TYR A 414 ? 0.8889 0.9817 0.6893 0.2029  0.0087  -0.0464 414 TYR A CD1 
3253 C CD2 . TYR A 414 ? 0.8977 1.0445 0.7182 0.2048  0.0442  -0.0790 414 TYR A CD2 
3254 C CE1 . TYR A 414 ? 0.8634 1.0184 0.6896 0.2072  0.0052  -0.0501 414 TYR A CE1 
3255 C CE2 . TYR A 414 ? 0.8349 1.0462 0.6851 0.2085  0.0414  -0.0846 414 TYR A CE2 
3256 C CZ  . TYR A 414 ? 0.8961 1.1108 0.7485 0.2108  0.0209  -0.0701 414 TYR A CZ  
3257 O OH  . TYR A 414 ? 0.9124 1.1936 0.7920 0.2147  0.0157  -0.0750 414 TYR A OH  
3258 N N   . VAL A 415 ? 0.9637 0.8245 0.6642 0.2236  -0.0091 -0.0400 415 VAL A N   
3259 C CA  . VAL A 415 ? 1.0044 0.8113 0.6776 0.2174  -0.0116 -0.0394 415 VAL A CA  
3260 C C   . VAL A 415 ? 0.9940 0.7669 0.6570 0.1993  -0.0269 -0.0199 415 VAL A C   
3261 O O   . VAL A 415 ? 1.0184 0.7786 0.6826 0.2050  -0.0442 -0.0076 415 VAL A O   
3262 C CB  . VAL A 415 ? 1.0475 0.8211 0.7081 0.2450  -0.0194 -0.0529 415 VAL A CB  
3263 C CG1 . VAL A 415 ? 1.0203 0.7415 0.6516 0.2367  -0.0226 -0.0546 415 VAL A CG1 
3264 C CG2 . VAL A 415 ? 1.0019 0.8212 0.6755 0.2622  -0.0021 -0.0748 415 VAL A CG2 
3265 N N   . PHE A 416 ? 1.0400 0.7993 0.6922 0.1776  -0.0212 -0.0168 416 PHE A N   
3266 C CA  . PHE A 416 ? 1.0136 0.7566 0.6615 0.1568  -0.0317 -0.0015 416 PHE A CA  
3267 C C   . PHE A 416 ? 1.0847 0.7743 0.7091 0.1536  -0.0427 -0.0003 416 PHE A C   
3268 O O   . PHE A 416 ? 1.0703 0.7488 0.6830 0.1517  -0.0353 -0.0095 416 PHE A O   
3269 C CB  . PHE A 416 ? 0.9851 0.7619 0.6459 0.1351  -0.0181 -0.0012 416 PHE A CB  
3270 C CG  . PHE A 416 ? 0.9894 0.8185 0.6731 0.1365  -0.0044 -0.0076 416 PHE A CG  
3271 C CD1 . PHE A 416 ? 0.9233 0.7838 0.6221 0.1382  -0.0108 -0.0016 416 PHE A CD1 
3272 C CD2 . PHE A 416 ? 0.9645 0.8122 0.6529 0.1351  0.0140  -0.0191 416 PHE A CD2 
3273 C CE1 . PHE A 416 ? 0.8950 0.8080 0.6164 0.1386  0.0009  -0.0099 416 PHE A CE1 
3274 C CE2 . PHE A 416 ? 0.9120 0.8093 0.6230 0.1330  0.0269  -0.0263 416 PHE A CE2 
3275 C CZ  . PHE A 416 ? 0.9090 0.8404 0.6378 0.1350  0.0202  -0.0232 416 PHE A CZ  
3276 N N   . PRO A 417 ? 1.0509 0.7060 0.6660 0.1520  -0.0611 0.0111  417 PRO A N   
3277 C CA  . PRO A 417 ? 1.0368 0.6391 0.6301 0.1489  -0.0727 0.0093  417 PRO A CA  
3278 C C   . PRO A 417 ? 0.9865 0.5904 0.5773 0.1216  -0.0727 0.0150  417 PRO A C   
3279 O O   . PRO A 417 ? 0.9982 0.6230 0.5989 0.1033  -0.0745 0.0275  417 PRO A O   
3280 C CB  . PRO A 417 ? 1.0447 0.6093 0.6314 0.1555  -0.0925 0.0213  417 PRO A CB  
3281 C CG  . PRO A 417 ? 0.9820 0.5849 0.5841 0.1482  -0.0928 0.0375  417 PRO A CG  
3282 C CD  . PRO A 417 ? 0.9701 0.6313 0.5922 0.1531  -0.0731 0.0267  417 PRO A CD  
3283 N N   . GLU A 418 ? 1.0331 0.6194 0.6108 0.1197  -0.0711 0.0045  418 GLU A N   
3284 C CA  . GLU A 418 ? 0.9881 0.5802 0.5659 0.0984  -0.0719 0.0065  418 GLU A CA  
3285 C C   . GLU A 418 ? 1.0003 0.5492 0.5588 0.0921  -0.0866 0.0030  418 GLU A C   
3286 O O   . GLU A 418 ? 1.0792 0.5972 0.6205 0.1070  -0.0901 -0.0086 418 GLU A O   
3287 C CB  . GLU A 418 ? 0.9200 0.5359 0.5004 0.1003  -0.0578 -0.0018 418 GLU A CB  
3288 C CG  . GLU A 418 ? 0.8785 0.5343 0.4774 0.1046  -0.0417 -0.0016 418 GLU A CG  
3289 C CD  . GLU A 418 ? 0.9230 0.5930 0.5227 0.1014  -0.0300 -0.0061 418 GLU A CD  
3290 O OE1 . GLU A 418 ? 0.9108 0.5655 0.4910 0.1106  -0.0262 -0.0128 418 GLU A OE1 
3291 O OE2 . GLU A 418 ? 0.8468 0.5418 0.4650 0.0895  -0.0253 -0.0030 418 GLU A OE2 
3292 N N   . VAL A 419 ? 0.9703 0.5204 0.5327 0.0688  -0.0949 0.0110  419 VAL A N   
3293 C CA  . VAL A 419 ? 1.0276 0.5472 0.5759 0.0567  -0.1078 0.0060  419 VAL A CA  
3294 C C   . VAL A 419 ? 1.0071 0.5621 0.5699 0.0362  -0.1065 0.0073  419 VAL A C   
3295 O O   . VAL A 419 ? 0.9403 0.5245 0.5198 0.0205  -0.1043 0.0173  419 VAL A O   
3296 C CB  . VAL A 419 ? 1.0580 0.5353 0.5963 0.0464  -0.1232 0.0148  419 VAL A CB  
3297 C CG1 . VAL A 419 ? 1.0756 0.5183 0.5983 0.0349  -0.1360 0.0046  419 VAL A CG1 
3298 C CG2 . VAL A 419 ? 1.0357 0.4836 0.5669 0.0707  -0.1254 0.0154  419 VAL A CG2 
3299 N N   . LEU A 420 ? 0.9762 0.5330 0.5331 0.0379  -0.1081 -0.0038 420 LEU A N   
3300 C CA  . LEU A 420 ? 0.9142 0.5061 0.4880 0.0233  -0.1091 -0.0050 420 LEU A CA  
3301 C C   . LEU A 420 ? 1.0324 0.6082 0.5954 0.0118  -0.1239 -0.0134 420 LEU A C   
3302 O O   . LEU A 420 ? 1.0381 0.5846 0.5788 0.0228  -0.1293 -0.0229 420 LEU A O   
3303 C CB  . LEU A 420 ? 0.8996 0.5170 0.4813 0.0374  -0.0980 -0.0089 420 LEU A CB  
3304 C CG  . LEU A 420 ? 0.9112 0.5658 0.5153 0.0289  -0.0991 -0.0116 420 LEU A CG  
3305 C CD1 . LEU A 420 ? 0.8795 0.5664 0.5078 0.0096  -0.0978 -0.0072 420 LEU A CD1 
3306 C CD2 . LEU A 420 ? 0.8438 0.5128 0.4548 0.0438  -0.0887 -0.0127 420 LEU A CD2 
3307 N N   . LEU A 421 ? 1.0297 0.6302 0.6093 -0.0112 -0.1301 -0.0119 421 LEU A N   
3308 C CA  . LEU A 421 ? 1.0640 0.6577 0.6378 -0.0254 -0.1446 -0.0213 421 LEU A CA  
3309 C C   . LEU A 421 ? 1.0418 0.6778 0.6327 -0.0227 -0.1465 -0.0297 421 LEU A C   
3310 O O   . LEU A 421 ? 0.9995 0.6699 0.6109 -0.0152 -0.1369 -0.0273 421 LEU A O   
3311 C CB  . LEU A 421 ? 1.0995 0.6912 0.6791 -0.0566 -0.1519 -0.0148 421 LEU A CB  
3312 C CG  . LEU A 421 ? 1.1324 0.6779 0.6957 -0.0593 -0.1528 -0.0021 421 LEU A CG  
3313 C CD1 . LEU A 421 ? 1.1287 0.6742 0.6961 -0.0947 -0.1592 0.0096  421 LEU A CD1 
3314 C CD2 . LEU A 421 ? 1.1883 0.6754 0.7242 -0.0432 -0.1607 -0.0112 421 LEU A CD2 
3315 N N   . SER A 422 ? 1.0552 0.6868 0.6373 -0.0275 -0.1605 -0.0409 422 SER A N   
3316 C CA  . SER A 422 ? 0.9909 0.6620 0.5890 -0.0231 -0.1671 -0.0491 422 SER A CA  
3317 C C   . SER A 422 ? 1.0011 0.7251 0.6370 -0.0336 -0.1611 -0.0474 422 SER A C   
3318 O O   . SER A 422 ? 0.9764 0.7130 0.6242 -0.0567 -0.1577 -0.0429 422 SER A O   
3319 C CB  . SER A 422 ? 1.0180 0.6873 0.6079 -0.0366 -0.1854 -0.0618 422 SER A CB  
3320 O OG  . SER A 422 ? 0.9609 0.6764 0.5719 -0.0336 -0.1946 -0.0700 422 SER A OG  
3321 N N   . GLU A 423 ? 1.0751 0.8289 0.7286 -0.0164 -0.1600 -0.0510 423 GLU A N   
3322 C CA  . GLU A 423 ? 1.0169 0.8224 0.7085 -0.0202 -0.1536 -0.0543 423 GLU A CA  
3323 C C   . GLU A 423 ? 1.0478 0.8535 0.7456 -0.0190 -0.1356 -0.0453 423 GLU A C   
3324 O O   . GLU A 423 ? 0.9643 0.8138 0.6914 -0.0288 -0.1284 -0.0490 423 GLU A O   
3325 C CB  . GLU A 423 ? 1.1074 0.9548 0.8218 -0.0484 -0.1604 -0.0627 423 GLU A CB  
3326 C CG  . GLU A 423 ? 1.0895 0.9625 0.8142 -0.0470 -0.1783 -0.0766 423 GLU A CG  
3327 C CD  . GLU A 423 ? 1.1372 1.0411 0.8860 -0.0205 -0.1818 -0.0840 423 GLU A CD  
3328 O OE1 . GLU A 423 ? 1.1397 1.0213 0.8819 0.0017  -0.1730 -0.0764 423 GLU A OE1 
3329 O OE2 . GLU A 423 ? 1.1910 1.1422 0.9672 -0.0223 -0.1941 -0.0980 423 GLU A OE2 
3330 N N   . ASN A 424 ? 0.9784 0.7411 0.6499 -0.0073 -0.1282 -0.0356 424 ASN A N   
3331 C CA  . ASN A 424 ? 0.9428 0.7068 0.6193 -0.0026 -0.1122 -0.0281 424 ASN A CA  
3332 C C   . ASN A 424 ? 0.9942 0.7741 0.6782 -0.0258 -0.1080 -0.0220 424 ASN A C   
3333 O O   . ASN A 424 ? 0.9373 0.7512 0.6415 -0.0309 -0.0977 -0.0217 424 ASN A O   
3334 C CB  . ASN A 424 ? 0.8992 0.6926 0.6011 0.0104  -0.1049 -0.0338 424 ASN A CB  
3335 C CG  . ASN A 424 ? 0.9446 0.7209 0.6395 0.0238  -0.0907 -0.0274 424 ASN A CG  
3336 O OD1 . ASN A 424 ? 0.9966 0.7546 0.6829 0.0407  -0.0891 -0.0265 424 ASN A OD1 
3337 N ND2 . ASN A 424 ? 0.8879 0.6715 0.5853 0.0148  -0.0808 -0.0220 424 ASN A ND2 
3338 N N   . GLN A 425 ? 0.9151 0.6678 0.5803 -0.0408 -0.1168 -0.0169 425 GLN A N   
3339 C CA  . GLN A 425 ? 0.8991 0.6574 0.5644 -0.0656 -0.1157 -0.0066 425 GLN A CA  
3340 C C   . GLN A 425 ? 0.9201 0.6332 0.5616 -0.0573 -0.1133 0.0068  425 GLN A C   
3341 O O   . GLN A 425 ? 0.9597 0.6276 0.5793 -0.0415 -0.1180 0.0054  425 GLN A O   
3342 C CB  . GLN A 425 ? 0.8961 0.6507 0.5575 -0.0916 -0.1285 -0.0085 425 GLN A CB  
3343 C CG  . GLN A 425 ? 0.8783 0.6840 0.5665 -0.0988 -0.1330 -0.0240 425 GLN A CG  
3344 C CD  . GLN A 425 ? 0.8666 0.7363 0.5872 -0.1058 -0.1217 -0.0285 425 GLN A CD  
3345 O OE1 . GLN A 425 ? 0.9080 0.7969 0.6309 -0.1280 -0.1149 -0.0192 425 GLN A OE1 
3346 N NE2 . GLN A 425 ? 0.8597 0.7626 0.6045 -0.0870 -0.1206 -0.0429 425 GLN A NE2 
3347 N N   . LEU A 426 ? 0.8426 0.5721 0.4888 -0.0670 -0.1064 0.0185  426 LEU A N   
3348 C CA  . LEU A 426 ? 0.8423 0.5329 0.4684 -0.0593 -0.1071 0.0325  426 LEU A CA  
3349 C C   . LEU A 426 ? 0.8890 0.5349 0.4943 -0.0774 -0.1210 0.0427  426 LEU A C   
3350 O O   . LEU A 426 ? 0.9108 0.5654 0.5191 -0.1025 -0.1276 0.0407  426 LEU A O   
3351 C CB  . LEU A 426 ? 0.8072 0.5333 0.4439 -0.0634 -0.0973 0.0424  426 LEU A CB  
3352 C CG  . LEU A 426 ? 0.7425 0.5041 0.3987 -0.0450 -0.0835 0.0313  426 LEU A CG  
3353 C CD1 . LEU A 426 ? 0.7253 0.5166 0.3878 -0.0472 -0.0753 0.0398  426 LEU A CD1 
3354 C CD2 . LEU A 426 ? 0.7412 0.4686 0.3872 -0.0170 -0.0819 0.0242  426 LEU A CD2 
3355 N N   . ALA A 427 ? 0.9640 0.5609 0.5493 -0.0644 -0.1262 0.0523  427 ALA A N   
3356 C CA  . ALA A 427 ? 1.0489 0.5898 0.6126 -0.0784 -0.1411 0.0623  427 ALA A CA  
3357 C C   . ALA A 427 ? 1.0450 0.5687 0.5985 -0.0827 -0.1447 0.0858  427 ALA A C   
3358 O O   . ALA A 427 ? 1.0972 0.5663 0.6338 -0.0656 -0.1538 0.0918  427 ALA A O   
3359 C CB  . ALA A 427 ? 1.0880 0.5747 0.6348 -0.0553 -0.1485 0.0486  427 ALA A CB  
3360 N N   . PRO A 428 ? 1.0863 0.6561 0.6488 -0.1051 -0.1389 0.0992  428 PRO A N   
3361 C CA  . PRO A 428 ? 1.0736 0.6330 0.6237 -0.1080 -0.1431 0.1240  428 PRO A CA  
3362 C C   . PRO A 428 ? 1.1317 0.6186 0.6552 -0.1211 -0.1614 0.1426  428 PRO A C   
3363 O O   . PRO A 428 ? 1.1978 0.6690 0.7149 -0.1518 -0.1676 0.1448  428 PRO A O   
3364 C CB  . PRO A 428 ? 1.0225 0.6515 0.5852 -0.1370 -0.1331 0.1312  428 PRO A CB  
3365 C CG  . PRO A 428 ? 0.9965 0.6548 0.5738 -0.1582 -0.1293 0.1150  428 PRO A CG  
3366 C CD  . PRO A 428 ? 1.0583 0.6935 0.6417 -0.1296 -0.1298 0.0918  428 PRO A CD  
3367 N N   . GLY A 429 ? 1.0878 0.5290 0.5975 -0.0968 -0.1708 0.1545  429 GLY A N   
3368 C CA  . GLY A 429 ? 1.1672 0.5314 0.6514 -0.1054 -0.1904 0.1742  429 GLY A CA  
3369 C C   . GLY A 429 ? 1.2398 0.5372 0.7148 -0.0981 -0.2009 0.1571  429 GLY A C   
3370 O O   . GLY A 429 ? 1.3071 0.5317 0.7614 -0.1055 -0.2185 0.1711  429 GLY A O   
3371 N N   . GLU A 430 ? 1.2847 0.6017 0.7726 -0.0837 -0.1920 0.1275  430 GLU A N   
3372 C CA  . GLU A 430 ? 1.3804 0.6410 0.8581 -0.0761 -0.2016 0.1076  430 GLU A CA  
3373 C C   . GLU A 430 ? 1.4066 0.6322 0.8806 -0.0307 -0.2040 0.0926  430 GLU A C   
3374 O O   . GLU A 430 ? 1.4768 0.6518 0.9401 -0.0210 -0.2126 0.0740  430 GLU A O   
3375 C CB  . GLU A 430 ? 1.3377 0.6392 0.8276 -0.0865 -0.1929 0.0838  430 GLU A CB  
3376 C CG  . GLU A 430 ? 1.3089 0.6612 0.8102 -0.1270 -0.1883 0.0916  430 GLU A CG  
3377 C CD  . GLU A 430 ? 1.4038 0.7802 0.9146 -0.1378 -0.1872 0.0679  430 GLU A CD  
3378 O OE1 . GLU A 430 ? 1.4382 0.7759 0.9389 -0.1223 -0.1944 0.0486  430 GLU A OE1 
3379 O OE2 . GLU A 430 ? 1.3714 0.8100 0.9007 -0.1602 -0.1796 0.0670  430 GLU A OE2 
3380 N N   . PHE A 431 ? 1.2739 0.5284 0.7572 -0.0038 -0.1965 0.0979  431 PHE A N   
3381 C CA  . PHE A 431 ? 1.3078 0.5433 0.7920 0.0393  -0.1961 0.0808  431 PHE A CA  
3382 C C   . PHE A 431 ? 1.3065 0.5480 0.7952 0.0596  -0.1993 0.0991  431 PHE A C   
3383 O O   . PHE A 431 ? 1.2906 0.5621 0.7816 0.0411  -0.1987 0.1233  431 PHE A O   
3384 C CB  . PHE A 431 ? 1.2740 0.5616 0.7711 0.0558  -0.1774 0.0559  431 PHE A CB  
3385 C CG  . PHE A 431 ? 1.2209 0.5827 0.7370 0.0499  -0.1608 0.0632  431 PHE A CG  
3386 C CD1 . PHE A 431 ? 1.1699 0.5720 0.6942 0.0201  -0.1541 0.0662  431 PHE A CD1 
3387 C CD2 . PHE A 431 ? 1.1944 0.5879 0.7225 0.0743  -0.1523 0.0645  431 PHE A CD2 
3388 C CE1 . PHE A 431 ? 1.0988 0.5663 0.6420 0.0160  -0.1394 0.0695  431 PHE A CE1 
3389 C CE2 . PHE A 431 ? 1.1120 0.5715 0.6581 0.0672  -0.1373 0.0686  431 PHE A CE2 
3390 C CZ  . PHE A 431 ? 1.0599 0.5534 0.6131 0.0386  -0.1310 0.0706  431 PHE A CZ  
3391 N N   . GLN A 432 ? 1.4424 0.6600 0.9325 0.0989  -0.2030 0.0854  432 GLN A N   
3392 C CA  . GLN A 432 ? 1.3795 0.6069 0.8773 0.1246  -0.2078 0.0985  432 GLN A CA  
3393 C C   . GLN A 432 ? 1.4333 0.6876 0.9462 0.1651  -0.1968 0.0714  432 GLN A C   
3394 O O   . GLN A 432 ? 1.4224 0.6685 0.9332 0.1757  -0.1897 0.0440  432 GLN A O   
3395 C CB  . GLN A 432 ? 1.4831 0.6331 0.9646 0.1307  -0.2335 0.1180  432 GLN A CB  
3396 C CG  . GLN A 432 ? 1.4922 0.6592 0.9774 0.1431  -0.2422 0.1447  432 GLN A CG  
3397 C CD  . GLN A 432 ? 1.5274 0.6146 0.9959 0.1483  -0.2692 0.1670  432 GLN A CD  
3398 O OE1 . GLN A 432 ? 1.6711 0.7373 1.1263 0.1108  -0.2764 0.1925  432 GLN A OE1 
3399 N NE2 . GLN A 432 ? 1.5918 0.6604 1.0750 0.1899  -0.2772 0.1521  432 GLN A NE2 
3400 N N   . VAL A 433 ? 1.3333 0.6254 0.8609 0.1860  -0.1951 0.0792  433 VAL A N   
3401 C CA  . VAL A 433 ? 1.2603 0.5811 0.8049 0.2252  -0.1866 0.0557  433 VAL A CA  
3402 C C   . VAL A 433 ? 1.3343 0.6140 0.8799 0.2576  -0.2083 0.0632  433 VAL A C   
3403 O O   . VAL A 433 ? 1.3132 0.5869 0.8554 0.2514  -0.2227 0.0930  433 VAL A O   
3404 C CB  . VAL A 433 ? 1.1816 0.5890 0.7475 0.2233  -0.1659 0.0544  433 VAL A CB  
3405 C CG1 . VAL A 433 ? 1.1626 0.6030 0.7479 0.2620  -0.1590 0.0336  433 VAL A CG1 
3406 C CG2 . VAL A 433 ? 1.1155 0.5563 0.6814 0.1974  -0.1460 0.0445  433 VAL A CG2 
3407 N N   . SER A 434 ? 1.4488 0.7010 0.9982 0.2928  -0.2117 0.0360  434 SER A N   
3408 C CA  . SER A 434 ? 1.4939 0.7083 1.0494 0.3320  -0.2329 0.0365  434 SER A CA  
3409 C C   . SER A 434 ? 1.4729 0.7630 1.0573 0.3630  -0.2231 0.0266  434 SER A C   
3410 O O   . SER A 434 ? 1.4501 0.8130 1.0482 0.3555  -0.1982 0.0132  434 SER A O   
3411 C CB  . SER A 434 ? 1.5081 0.6592 1.0572 0.3553  -0.2412 0.0068  434 SER A CB  
3412 O OG  . SER A 434 ? 1.4722 0.6685 1.0341 0.3788  -0.2211 -0.0313 434 SER A OG  
3413 N N   . THR A 435 ? 1.4441 0.7156 1.0386 0.3984  -0.2441 0.0329  435 THR A N   
3414 C CA  . THR A 435 ? 1.4142 0.7632 1.0391 0.4275  -0.2371 0.0235  435 THR A CA  
3415 C C   . THR A 435 ? 1.4173 0.8073 1.0623 0.4557  -0.2174 -0.0206 435 THR A C   
3416 O O   . THR A 435 ? 1.3537 0.8271 1.0240 0.4650  -0.2005 -0.0325 435 THR A O   
3417 C CB  . THR A 435 ? 1.4574 0.7812 1.0905 0.4593  -0.2664 0.0414  435 THR A CB  
3418 O OG1 . THR A 435 ? 1.4738 0.7382 1.0843 0.4266  -0.2838 0.0780  435 THR A OG1 
3419 C CG2 . THR A 435 ? 1.3968 0.8076 1.0538 0.4709  -0.2628 0.0494  435 THR A CG2 
3420 N N   . ASP A 436 ? 1.7100 1.0473 1.3435 0.4663  -0.2181 -0.0460 436 ASP A N   
3421 C CA  . ASP A 436 ? 1.6807 1.0578 1.3283 0.4902  -0.1982 -0.0891 436 ASP A CA  
3422 C C   . ASP A 436 ? 1.6399 1.0534 1.2750 0.4556  -0.1691 -0.0997 436 ASP A C   
3423 O O   . ASP A 436 ? 1.6646 1.1056 1.3027 0.4684  -0.1514 -0.1333 436 ASP A O   
3424 C CB  . ASP A 436 ? 1.6594 0.9806 1.3069 0.5118  -0.2106 -0.1137 436 ASP A CB  
3425 C CG  . ASP A 436 ? 1.7546 0.9952 1.3723 0.4793  -0.2210 -0.1030 436 ASP A CG  
3426 O OD1 . ASP A 436 ? 1.7638 0.9818 1.3606 0.4454  -0.2244 -0.0723 436 ASP A OD1 
3427 O OD2 . ASP A 436 ? 1.7762 0.9803 1.3930 0.4868  -0.2254 -0.1265 436 ASP A OD2 
3428 N N   . GLY A 437 ? 1.3804 0.7971 1.0016 0.4131  -0.1640 -0.0723 437 GLY A N   
3429 C CA  . GLY A 437 ? 1.3188 0.7801 0.9336 0.3830  -0.1377 -0.0781 437 GLY A CA  
3430 C C   . GLY A 437 ? 1.3439 0.7581 0.9303 0.3593  -0.1363 -0.0835 437 GLY A C   
3431 O O   . GLY A 437 ? 1.3463 0.7939 0.9263 0.3465  -0.1154 -0.0976 437 GLY A O   
3432 N N   . ARG A 438 ? 1.4104 0.7491 0.9792 0.3519  -0.1583 -0.0724 438 ARG A N   
3433 C CA  . ARG A 438 ? 1.4277 0.7246 0.9712 0.3262  -0.1591 -0.0771 438 ARG A CA  
3434 C C   . ARG A 438 ? 1.4233 0.7199 0.9595 0.2847  -0.1613 -0.0454 438 ARG A C   
3435 O O   . ARG A 438 ? 1.3708 0.6485 0.9091 0.2770  -0.1761 -0.0182 438 ARG A O   
3436 C CB  . ARG A 438 ? 1.4804 0.6929 1.0095 0.3404  -0.1814 -0.0891 438 ARG A CB  
3437 C CG  . ARG A 438 ? 1.5005 0.7099 1.0321 0.3770  -0.1774 -0.1292 438 ARG A CG  
3438 C CD  . ARG A 438 ? 1.5982 0.7429 1.1329 0.3893  -0.2003 -0.1345 438 ARG A CD  
3439 N NE  . ARG A 438 ? 1.6486 0.7309 1.1639 0.3541  -0.2154 -0.1172 438 ARG A NE  
3440 C CZ  . ARG A 438 ? 1.6665 0.6981 1.1843 0.3447  -0.2364 -0.0932 438 ARG A CZ  
3441 N NH1 . ARG A 438 ? 1.6288 0.6610 1.1661 0.3689  -0.2472 -0.0808 438 ARG A NH1 
3442 N NH2 . ARG A 438 ? 1.6335 0.6143 1.1335 0.3097  -0.2469 -0.0816 438 ARG A NH2 
3443 N N   . LEU A 439 ? 1.2890 0.6095 0.8164 0.2590  -0.1471 -0.0491 439 LEU A N   
3444 C CA  . LEU A 439 ? 1.2596 0.5781 0.7803 0.2203  -0.1496 -0.0264 439 LEU A CA  
3445 C C   . LEU A 439 ? 1.3496 0.6089 0.8486 0.2060  -0.1621 -0.0351 439 LEU A C   
3446 O O   . LEU A 439 ? 1.3125 0.5717 0.8006 0.2105  -0.1553 -0.0594 439 LEU A O   
3447 C CB  . LEU A 439 ? 1.2373 0.6207 0.7659 0.2036  -0.1282 -0.0256 439 LEU A CB  
3448 C CG  . LEU A 439 ? 1.2320 0.6184 0.7538 0.1678  -0.1280 -0.0146 439 LEU A CG  
3449 C CD1 . LEU A 439 ? 1.2154 0.5870 0.7392 0.1448  -0.1411 0.0120  439 LEU A CD1 
3450 C CD2 . LEU A 439 ? 1.1588 0.6049 0.6908 0.1590  -0.1081 -0.0161 439 LEU A CD2 
3451 N N   . PHE A 440 ? 1.3635 0.5730 0.8546 0.1875  -0.1808 -0.0157 440 PHE A N   
3452 C CA  . PHE A 440 ? 1.4138 0.5601 0.8856 0.1750  -0.1950 -0.0263 440 PHE A CA  
3453 C C   . PHE A 440 ? 1.4603 0.5900 0.9259 0.1328  -0.2045 -0.0009 440 PHE A C   
3454 O O   . PHE A 440 ? 1.3714 0.5279 0.8453 0.1172  -0.2032 0.0263  440 PHE A O   
3455 C CB  . PHE A 440 ? 1.4229 0.4999 0.8888 0.2041  -0.2128 -0.0381 440 PHE A CB  
3456 C CG  . PHE A 440 ? 1.4991 0.5413 0.9686 0.2074  -0.2299 -0.0085 440 PHE A CG  
3457 C CD1 . PHE A 440 ? 1.4567 0.5418 0.9438 0.2300  -0.2252 0.0035  440 PHE A CD1 
3458 C CD2 . PHE A 440 ? 1.5126 0.4866 0.9695 0.1854  -0.2502 0.0077  440 PHE A CD2 
3459 C CE1 . PHE A 440 ? 1.5034 0.5581 0.9909 0.2344  -0.2433 0.0326  440 PHE A CE1 
3460 C CE2 . PHE A 440 ? 1.5162 0.4732 0.9795 0.1843  -0.2635 0.0375  440 PHE A CE2 
3461 C CZ  . PHE A 440 ? 1.5296 0.5256 1.0067 0.2098  -0.2610 0.0504  440 PHE A CZ  
3462 N N   . SER A 441 ? 1.5523 0.6421 1.0031 0.1129  -0.2134 -0.0123 441 SER A N   
3463 C CA  . SER A 441 ? 1.5529 0.6352 0.9989 0.0690  -0.2202 0.0058  441 SER A CA  
3464 C C   . SER A 441 ? 1.5524 0.5631 0.9875 0.0569  -0.2409 0.0272  441 SER A C   
3465 O O   . SER A 441 ? 1.6328 0.5748 1.0577 0.0762  -0.2554 0.0153  441 SER A O   
3466 C CB  . SER A 441 ? 1.5299 0.6074 0.9663 0.0518  -0.2212 -0.0176 441 SER A CB  
3467 O OG  . SER A 441 ? 1.6106 0.6155 1.0312 0.0613  -0.2365 -0.0374 441 SER A OG  
3468 N N   . LEU A 442 ? 1.4909 0.5169 0.9275 0.0252  -0.2425 0.0588  442 LEU A N   
3469 C CA  . LEU A 442 ? 1.5689 0.5256 0.9903 0.0055  -0.2624 0.0847  442 LEU A CA  
3470 C C   . LEU A 442 ? 1.5977 0.5112 1.0062 -0.0342 -0.2725 0.0802  442 LEU A C   
3471 O O   . LEU A 442 ? 1.6729 0.5307 1.0722 -0.0523 -0.2874 0.0966  442 LEU A O   
3472 C CB  . LEU A 442 ? 1.4938 0.4889 0.9182 -0.0143 -0.2595 0.1218  442 LEU A CB  
3473 C CG  . LEU A 442 ? 1.5370 0.5090 0.9586 0.0135  -0.2698 0.1440  442 LEU A CG  
3474 C CD1 . LEU A 442 ? 1.5313 0.5245 0.9681 0.0660  -0.2628 0.1197  442 LEU A CD1 
3475 C CD2 . LEU A 442 ? 1.5001 0.5343 0.9255 -0.0093 -0.2617 0.1743  442 LEU A CD2 
3476 N N   . LYS A 443 ? 1.6696 0.6252 1.0844 -0.0483 -0.2624 0.0576  443 LYS A N   
3477 C CA  . LYS A 443 ? 1.6983 0.6299 1.1052 -0.0879 -0.2705 0.0496  443 LYS A CA  
3478 C C   . LYS A 443 ? 1.6488 0.6419 1.0660 -0.0859 -0.2581 0.0203  443 LYS A C   
3479 O O   . LYS A 443 ? 1.5645 0.6144 0.9932 -0.0585 -0.2430 0.0126  443 LYS A O   
3480 C CB  . LYS A 443 ? 1.6921 0.6370 1.0982 -0.1373 -0.2723 0.0824  443 LYS A CB  
3481 C CG  . LYS A 443 ? 1.6665 0.7104 1.0920 -0.1466 -0.2532 0.0937  443 LYS A CG  
3482 C CD  . LYS A 443 ? 1.6828 0.7562 1.1105 -0.2012 -0.2522 0.1116  443 LYS A CD  
3483 C CE  . LYS A 443 ? 1.6269 0.7721 1.0661 -0.2097 -0.2384 0.1350  443 LYS A CE  
3484 N NZ  . LYS A 443 ? 1.6033 0.7226 1.0333 -0.1805 -0.2417 0.1559  443 LYS A NZ  
3485 N N   . PRO A 444 ? 1.7455 0.7291 1.1584 -0.1143 -0.2651 0.0039  444 PRO A N   
3486 C CA  . PRO A 444 ? 1.6562 0.7034 1.0783 -0.1125 -0.2556 -0.0202 444 PRO A CA  
3487 C C   . PRO A 444 ? 1.5932 0.7274 1.0366 -0.1221 -0.2399 -0.0049 444 PRO A C   
3488 O O   . PRO A 444 ? 1.6161 0.7682 1.0671 -0.1515 -0.2386 0.0196  444 PRO A O   
3489 C CB  . PRO A 444 ? 1.6700 0.6914 1.0854 -0.1493 -0.2691 -0.0350 444 PRO A CB  
3490 C CG  . PRO A 444 ? 1.7181 0.6996 1.1298 -0.1872 -0.2781 -0.0070 444 PRO A CG  
3491 C CD  . PRO A 444 ? 1.7617 0.7039 1.1668 -0.1624 -0.2785 0.0177  444 PRO A CD  
3492 N N   . THR A 445 ? 1.4073 0.5947 0.8592 -0.0972 -0.2280 -0.0199 445 THR A N   
3493 C CA  . THR A 445 ? 1.3434 0.6086 0.8170 -0.1010 -0.2136 -0.0090 445 THR A CA  
3494 C C   . THR A 445 ? 1.3310 0.6348 0.8182 -0.1422 -0.2169 -0.0070 445 THR A C   
3495 O O   . THR A 445 ? 1.4138 0.7035 0.8956 -0.1604 -0.2279 -0.0231 445 THR A O   
3496 C CB  . THR A 445 ? 1.2866 0.5918 0.7639 -0.0693 -0.2027 -0.0258 445 THR A CB  
3497 O OG1 . THR A 445 ? 1.3492 0.6591 0.8198 -0.0748 -0.2104 -0.0483 445 THR A OG1 
3498 C CG2 . THR A 445 ? 1.2742 0.5474 0.7390 -0.0311 -0.1982 -0.0314 445 THR A CG2 
3499 N N   . SER A 446 ? 1.4015 0.7589 0.9076 -0.1576 -0.2070 0.0106  446 SER A N   
3500 C CA  . SER A 446 ? 1.3878 0.7925 0.9108 -0.1972 -0.2080 0.0117  446 SER A CA  
3501 C C   . SER A 446 ? 1.3006 0.7640 0.8416 -0.1899 -0.2061 -0.0105 446 SER A C   
3502 O O   . SER A 446 ? 1.3555 0.8509 0.9092 -0.2188 -0.2120 -0.0192 446 SER A O   
3503 C CB  . SER A 446 ? 1.2921 0.7409 0.8291 -0.2150 -0.1971 0.0346  446 SER A CB  
3504 O OG  . SER A 446 ? 1.2985 0.7851 0.8470 -0.1837 -0.1835 0.0358  446 SER A OG  
3505 N N   . GLY A 447 ? 1.2178 0.6977 0.7605 -0.1528 -0.1986 -0.0188 447 GLY A N   
3506 C CA  . GLY A 447 ? 1.2093 0.7328 0.7632 -0.1414 -0.1999 -0.0372 447 GLY A CA  
3507 C C   . GLY A 447 ? 1.2014 0.6940 0.7339 -0.1055 -0.2002 -0.0486 447 GLY A C   
3508 O O   . GLY A 447 ? 1.2038 0.6497 0.7183 -0.0882 -0.1970 -0.0440 447 GLY A O   
3509 N N   . PRO A 448 ? 1.1668 0.6880 0.7005 -0.0933 -0.2043 -0.0636 448 PRO A N   
3510 C CA  . PRO A 448 ? 1.1979 0.6943 0.7067 -0.0624 -0.2038 -0.0739 448 PRO A CA  
3511 C C   . PRO A 448 ? 1.1366 0.6375 0.6462 -0.0354 -0.1870 -0.0625 448 PRO A C   
3512 O O   . PRO A 448 ? 1.1114 0.6509 0.6443 -0.0357 -0.1772 -0.0512 448 PRO A O   
3513 C CB  . PRO A 448 ? 1.1706 0.7060 0.6823 -0.0593 -0.2132 -0.0873 448 PRO A CB  
3514 C CG  . PRO A 448 ? 1.1504 0.7294 0.6919 -0.0901 -0.2205 -0.0878 448 PRO A CG  
3515 C CD  . PRO A 448 ? 1.0884 0.6723 0.6477 -0.1041 -0.2084 -0.0700 448 PRO A CD  
3516 N N   . VAL A 449 ? 1.0980 0.5625 0.5829 -0.0127 -0.1833 -0.0683 449 VAL A N   
3517 C CA  . VAL A 449 ? 1.0538 0.5200 0.5387 0.0107  -0.1671 -0.0593 449 VAL A CA  
3518 C C   . VAL A 449 ? 1.0854 0.5825 0.5671 0.0286  -0.1598 -0.0611 449 VAL A C   
3519 O O   . VAL A 449 ? 1.0824 0.5748 0.5423 0.0360  -0.1664 -0.0732 449 VAL A O   
3520 C CB  . VAL A 449 ? 1.0784 0.4960 0.5416 0.0273  -0.1659 -0.0666 449 VAL A CB  
3521 C CG1 . VAL A 449 ? 1.0722 0.5009 0.5398 0.0497  -0.1489 -0.0584 449 VAL A CG1 
3522 C CG2 . VAL A 449 ? 1.1020 0.4761 0.5642 0.0104  -0.1771 -0.0641 449 VAL A CG2 
3523 N N   . LEU A 450 ? 1.0251 0.5522 0.5263 0.0346  -0.1466 -0.0485 450 LEU A N   
3524 C CA  . LEU A 450 ? 1.0467 0.5924 0.5432 0.0523  -0.1371 -0.0463 450 LEU A CA  
3525 C C   . LEU A 450 ? 1.0641 0.5925 0.5443 0.0708  -0.1230 -0.0464 450 LEU A C   
3526 O O   . LEU A 450 ? 1.0535 0.5769 0.5093 0.0838  -0.1197 -0.0521 450 LEU A O   
3527 C CB  . LEU A 450 ? 0.9582 0.5424 0.4857 0.0488  -0.1301 -0.0359 450 LEU A CB  
3528 C CG  . LEU A 450 ? 0.9816 0.5972 0.5309 0.0358  -0.1418 -0.0383 450 LEU A CG  
3529 C CD1 . LEU A 450 ? 0.9095 0.5612 0.4888 0.0393  -0.1331 -0.0322 450 LEU A CD1 
3530 C CD2 . LEU A 450 ? 0.9820 0.5952 0.5128 0.0405  -0.1565 -0.0470 450 LEU A CD2 
3531 N N   . THR A 451 ? 1.0994 0.6217 0.5918 0.0716  -0.1153 -0.0407 451 THR A N   
3532 C CA  . THR A 451 ? 1.1037 0.6159 0.5858 0.0900  -0.1029 -0.0434 451 THR A CA  
3533 C C   . THR A 451 ? 1.1262 0.6199 0.6176 0.0908  -0.1043 -0.0401 451 THR A C   
3534 O O   . THR A 451 ? 1.1607 0.6593 0.6697 0.0754  -0.1093 -0.0292 451 THR A O   
3535 C CB  . THR A 451 ? 1.0612 0.6041 0.5535 0.0974  -0.0858 -0.0354 451 THR A CB  
3536 O OG1 . THR A 451 ? 1.0978 0.6369 0.5784 0.1141  -0.0735 -0.0414 451 THR A OG1 
3537 C CG2 . THR A 451 ? 1.0288 0.5966 0.5531 0.0878  -0.0807 -0.0235 451 THR A CG2 
3538 N N   . VAL A 452 ? 1.0991 0.5737 0.5776 0.1096  -0.1002 -0.0498 452 VAL A N   
3539 C CA  . VAL A 452 ? 1.0960 0.5558 0.5833 0.1196  -0.1003 -0.0468 452 VAL A CA  
3540 C C   . VAL A 452 ? 1.1368 0.6208 0.6256 0.1408  -0.0830 -0.0527 452 VAL A C   
3541 O O   . VAL A 452 ? 1.1675 0.6447 0.6375 0.1555  -0.0786 -0.0693 452 VAL A O   
3542 C CB  . VAL A 452 ? 1.1578 0.5654 0.6298 0.1245  -0.1157 -0.0580 452 VAL A CB  
3543 C CG1 . VAL A 452 ? 1.1912 0.5821 0.6723 0.1412  -0.1171 -0.0545 452 VAL A CG1 
3544 C CG2 . VAL A 452 ? 1.1359 0.5196 0.6060 0.0985  -0.1323 -0.0527 452 VAL A CG2 
3545 N N   . THR A 453 ? 1.0565 0.5733 0.5673 0.1406  -0.0725 -0.0410 453 THR A N   
3546 C CA  . THR A 453 ? 1.0534 0.6023 0.5684 0.1542  -0.0541 -0.0461 453 THR A CA  
3547 C C   . THR A 453 ? 1.0648 0.6310 0.6012 0.1651  -0.0504 -0.0419 453 THR A C   
3548 O O   . THR A 453 ? 1.0534 0.6231 0.6054 0.1554  -0.0573 -0.0279 453 THR A O   
3549 C CB  . THR A 453 ? 1.0256 0.6061 0.5465 0.1415  -0.0422 -0.0383 453 THR A CB  
3550 O OG1 . THR A 453 ? 1.0361 0.6032 0.5337 0.1370  -0.0459 -0.0429 453 THR A OG1 
3551 C CG2 . THR A 453 ? 0.9961 0.6103 0.5244 0.1499  -0.0224 -0.0410 453 THR A CG2 
3552 N N   . LEU A 454 ? 1.0749 0.6563 0.6113 0.1852  -0.0396 -0.0551 454 LEU A N   
3553 C CA  . LEU A 454 ? 1.0907 0.7039 0.6502 0.1978  -0.0328 -0.0543 454 LEU A CA  
3554 C C   . LEU A 454 ? 1.0644 0.7253 0.6326 0.1912  -0.0109 -0.0554 454 LEU A C   
3555 O O   . LEU A 454 ? 1.0306 0.7022 0.5853 0.1971  0.0019  -0.0680 454 LEU A O   
3556 C CB  . LEU A 454 ? 1.0894 0.6898 0.6472 0.2265  -0.0372 -0.0713 454 LEU A CB  
3557 C CG  . LEU A 454 ? 1.1366 0.6866 0.6917 0.2333  -0.0607 -0.0658 454 LEU A CG  
3558 C CD1 . LEU A 454 ? 1.1640 0.6942 0.7175 0.2657  -0.0666 -0.0867 454 LEU A CD1 
3559 C CD2 . LEU A 454 ? 1.0587 0.6200 0.6330 0.2242  -0.0688 -0.0428 454 LEU A CD2 
3560 N N   . PHE A 455 ? 1.0210 0.7096 0.6100 0.1769  -0.0067 -0.0425 455 PHE A N   
3561 C CA  . PHE A 455 ? 0.9828 0.7093 0.5821 0.1646  0.0120  -0.0412 455 PHE A CA  
3562 C C   . PHE A 455 ? 1.0210 0.7921 0.6466 0.1723  0.0206  -0.0448 455 PHE A C   
3563 O O   . PHE A 455 ? 1.0088 0.7929 0.6528 0.1689  0.0130  -0.0363 455 PHE A O   
3564 C CB  . PHE A 455 ? 0.9427 0.6664 0.5479 0.1427  0.0088  -0.0282 455 PHE A CB  
3565 C CG  . PHE A 455 ? 0.9232 0.6711 0.5358 0.1289  0.0253  -0.0266 455 PHE A CG  
3566 C CD1 . PHE A 455 ? 0.9093 0.6972 0.5462 0.1243  0.0375  -0.0281 455 PHE A CD1 
3567 C CD2 . PHE A 455 ? 0.9679 0.6962 0.5635 0.1199  0.0265  -0.0229 455 PHE A CD2 
3568 C CE1 . PHE A 455 ? 0.8709 0.6740 0.5149 0.1092  0.0517  -0.0268 455 PHE A CE1 
3569 C CE2 . PHE A 455 ? 0.9551 0.6964 0.5565 0.1073  0.0395  -0.0191 455 PHE A CE2 
3570 C CZ  . PHE A 455 ? 0.9008 0.6773 0.5269 0.1009  0.0525  -0.0214 455 PHE A CZ  
3571 N N   . GLY A 456 ? 1.0119 0.8117 0.6391 0.1810  0.0366  -0.0577 456 GLY A N   
3572 C CA  . GLY A 456 ? 1.0120 0.8607 0.6661 0.1905  0.0445  -0.0651 456 GLY A CA  
3573 C C   . GLY A 456 ? 0.9818 0.8727 0.6476 0.1719  0.0665  -0.0669 456 GLY A C   
3574 O O   . GLY A 456 ? 0.9521 0.8360 0.5994 0.1608  0.0795  -0.0678 456 GLY A O   
3575 N N   . ARG A 457 ? 0.9826 0.9162 0.6777 0.1675  0.0699  -0.0669 457 ARG A N   
3576 C CA  . ARG A 457 ? 0.9559 0.9300 0.6667 0.1469  0.0898  -0.0697 457 ARG A CA  
3577 C C   . ARG A 457 ? 0.9558 0.9887 0.6893 0.1583  0.1010  -0.0858 457 ARG A C   
3578 O O   . ARG A 457 ? 0.9606 1.0155 0.7129 0.1779  0.0890  -0.0900 457 ARG A O   
3579 C CB  . ARG A 457 ? 0.8646 0.8468 0.5934 0.1285  0.0853  -0.0607 457 ARG A CB  
3580 C CG  . ARG A 457 ? 0.8536 0.7916 0.5659 0.1122  0.0814  -0.0491 457 ARG A CG  
3581 C CD  . ARG A 457 ? 0.8670 0.8011 0.5714 0.0932  0.0995  -0.0489 457 ARG A CD  
3582 N NE  . ARG A 457 ? 0.8586 0.8278 0.5894 0.0741  0.1111  -0.0529 457 ARG A NE  
3583 C CZ  . ARG A 457 ? 0.9057 0.9109 0.6474 0.0638  0.1298  -0.0611 457 ARG A CZ  
3584 N NH1 . ARG A 457 ? 0.8866 0.9035 0.6155 0.0713  0.1406  -0.0665 457 ARG A NH1 
3585 N NH2 . ARG A 457 ? 0.8527 0.8868 0.6198 0.0442  0.1383  -0.0662 457 ARG A NH2 
3586 N N   . LEU A 458 ? 0.9346 0.9945 0.6663 0.1456  0.1234  -0.0940 458 LEU A N   
3587 C CA  . LEU A 458 ? 0.9378 1.0648 0.6948 0.1511  0.1380  -0.1115 458 LEU A CA  
3588 C C   . LEU A 458 ? 0.9207 1.0848 0.6988 0.1199  0.1539  -0.1105 458 LEU A C   
3589 O O   . LEU A 458 ? 0.9073 1.0831 0.6780 0.0976  0.1751  -0.1120 458 LEU A O   
3590 C CB  . LEU A 458 ? 0.9237 1.0604 0.6624 0.1588  0.1532  -0.1245 458 LEU A CB  
3591 C CG  . LEU A 458 ? 0.9776 1.0989 0.7071 0.1949  0.1400  -0.1366 458 LEU A CG  
3592 C CD1 . LEU A 458 ? 1.0052 1.0515 0.7071 0.2012  0.1186  -0.1224 458 LEU A CD1 
3593 C CD2 . LEU A 458 ? 0.9904 1.1368 0.7045 0.1989  0.1598  -0.1545 458 LEU A CD2 
3594 N N   . TYR A 459 ? 0.8076 0.9926 0.6116 0.1177  0.1435  -0.1088 459 TYR A N   
3595 C CA  . TYR A 459 ? 0.8060 1.0175 0.6298 0.0870  0.1551  -0.1092 459 TYR A CA  
3596 C C   . TYR A 459 ? 0.7895 1.0644 0.6335 0.0733  0.1782  -0.1249 459 TYR A C   
3597 O O   . TYR A 459 ? 0.7841 1.0646 0.6321 0.0410  0.1948  -0.1242 459 TYR A O   
3598 C CB  . TYR A 459 ? 0.7758 1.0073 0.6228 0.0901  0.1384  -0.1079 459 TYR A CB  
3599 C CG  . TYR A 459 ? 0.7560 0.9325 0.5845 0.0991  0.1170  -0.0923 459 TYR A CG  
3600 C CD1 . TYR A 459 ? 0.7281 0.8642 0.5455 0.0786  0.1167  -0.0827 459 TYR A CD1 
3601 C CD2 . TYR A 459 ? 0.7622 0.9278 0.5856 0.1277  0.0966  -0.0876 459 TYR A CD2 
3602 C CE1 . TYR A 459 ? 0.7407 0.8358 0.5439 0.0847  0.0986  -0.0704 459 TYR A CE1 
3603 C CE2 . TYR A 459 ? 0.7676 0.8851 0.5735 0.1310  0.0782  -0.0725 459 TYR A CE2 
3604 C CZ  . TYR A 459 ? 0.7604 0.8471 0.5571 0.1086  0.0802  -0.0647 459 TYR A CZ  
3605 O OH  . TYR A 459 ? 0.6957 0.7430 0.4775 0.1096  0.0637  -0.0518 459 TYR A OH  
3606 N N   . GLU A 460 ? 1.1383 1.4622 0.9972 0.0969  0.1793  -0.1401 460 GLU A N   
3607 C CA  . GLU A 460 ? 1.1411 1.5364 1.0227 0.0842  0.2021  -0.1578 460 GLU A CA  
3608 C C   . GLU A 460 ? 1.1470 1.5247 1.0021 0.0575  0.2264  -0.1540 460 GLU A C   
3609 O O   . GLU A 460 ? 1.1409 1.5645 1.0106 0.0290  0.2486  -0.1619 460 GLU A O   
3610 C CB  . GLU A 460 ? 1.1307 1.5777 1.0310 0.1209  0.1971  -0.1766 460 GLU A CB  
3611 C CG  . GLU A 460 ? 1.1075 1.5060 0.9771 0.1504  0.1884  -0.1751 460 GLU A CG  
3612 C CD  . GLU A 460 ? 1.1884 1.5323 1.0488 0.1770  0.1577  -0.1623 460 GLU A CD  
3613 O OE1 . GLU A 460 ? 1.2287 1.5654 1.0996 0.1682  0.1447  -0.1505 460 GLU A OE1 
3614 O OE2 . GLU A 460 ? 1.1644 1.4729 1.0062 0.2047  0.1471  -0.1647 460 GLU A OE2 
3615 N N   . LYS A 461 ? 0.9972 1.3102 0.8122 0.0641  0.2223  -0.1412 461 LYS A N   
3616 C CA  . LYS A 461 ? 1.0277 1.3254 0.8111 0.0431  0.2433  -0.1360 461 LYS A CA  
3617 C C   . LYS A 461 ? 1.0307 1.2745 0.7946 0.0087  0.2477  -0.1148 461 LYS A C   
3618 O O   . LYS A 461 ? 1.1142 1.3304 0.8445 -0.0087 0.2606  -0.1039 461 LYS A O   
3619 C CB  . LYS A 461 ? 0.9757 1.2382 0.7243 0.0695  0.2363  -0.1361 461 LYS A CB  
3620 C CG  . LYS A 461 ? 1.0001 1.3232 0.7564 0.0895  0.2486  -0.1605 461 LYS A CG  
3621 C CD  . LYS A 461 ? 1.0678 1.3519 0.7944 0.1212  0.2361  -0.1650 461 LYS A CD  
3622 C CE  . LYS A 461 ? 1.0691 1.4087 0.8181 0.1569  0.2362  -0.1945 461 LYS A CE  
3623 N NZ  . LYS A 461 ? 1.0900 1.4637 0.8177 0.1553  0.2593  -0.2117 461 LYS A NZ  
3624 N N   . ASP A 462 ? 1.0576 1.2857 0.8409 -0.0002 0.2364  -0.1093 462 ASP A N   
3625 C CA  . ASP A 462 ? 1.0376 1.2178 0.8098 -0.0309 0.2400  -0.0936 462 ASP A CA  
3626 C C   . ASP A 462 ? 1.0382 1.2569 0.8247 -0.0678 0.2650  -0.0988 462 ASP A C   
3627 O O   . ASP A 462 ? 1.0756 1.2529 0.8460 -0.0969 0.2736  -0.0848 462 ASP A O   
3628 C CB  . ASP A 462 ? 1.0178 1.1767 0.8093 -0.0278 0.2210  -0.0914 462 ASP A CB  
3629 C CG  . ASP A 462 ? 0.9782 1.1097 0.7606 0.0055  0.1966  -0.0873 462 ASP A CG  
3630 O OD1 . ASP A 462 ? 0.9967 1.1093 0.7538 0.0252  0.1926  -0.0843 462 ASP A OD1 
3631 O OD2 . ASP A 462 ? 0.9530 1.0821 0.7527 0.0097  0.1817  -0.0877 462 ASP A OD2 
3632 N N   . GLN B 1   ? 1.0452 1.1420 0.7051 0.0649  -0.2093 -0.0002 1   GLN B N   
3633 C CA  . GLN B 1   ? 1.0748 1.1489 0.7428 0.0970  -0.2196 0.0111  1   GLN B CA  
3634 C C   . GLN B 1   ? 0.9962 1.0870 0.7111 0.1100  -0.2020 -0.0019 1   GLN B C   
3635 O O   . GLN B 1   ? 0.9661 1.0531 0.6901 0.0949  -0.1748 -0.0124 1   GLN B O   
3636 C CB  . GLN B 1   ? 1.0801 1.0868 0.7041 0.0967  -0.2160 0.0284  1   GLN B CB  
3637 C CG  . GLN B 1   ? 1.0474 1.0255 0.6723 0.0835  -0.1866 0.0228  1   GLN B CG  
3638 C CD  . GLN B 1   ? 1.1006 1.0152 0.6868 0.0840  -0.1855 0.0394  1   GLN B CD  
3639 O OE1 . GLN B 1   ? 1.1130 1.0004 0.6621 0.0640  -0.1818 0.0480  1   GLN B OE1 
3640 N NE2 . GLN B 1   ? 1.0189 0.9080 0.6134 0.1058  -0.1873 0.0432  1   GLN B NE2 
3641 N N   . ASP B 2   ? 0.7775 0.8855 0.5204 0.1399  -0.2173 0.0004  2   ASP B N   
3642 C CA  . ASP B 2   ? 0.8130 0.9454 0.6037 0.1548  -0.2031 -0.0128 2   ASP B CA  
3643 C C   . ASP B 2   ? 0.8024 0.8881 0.5869 0.1686  -0.1887 -0.0095 2   ASP B C   
3644 O O   . ASP B 2   ? 0.7507 0.8495 0.5662 0.1748  -0.1698 -0.0219 2   ASP B O   
3645 C CB  . ASP B 2   ? 0.7323 0.9093 0.5606 0.1808  -0.2246 -0.0127 2   ASP B CB  
3646 C CG  . ASP B 2   ? 0.8575 1.0920 0.7014 0.1658  -0.2380 -0.0210 2   ASP B CG  
3647 O OD1 . ASP B 2   ? 0.8764 1.1224 0.7159 0.1355  -0.2216 -0.0337 2   ASP B OD1 
3648 O OD2 . ASP B 2   ? 0.8202 1.0899 0.6823 0.1838  -0.2640 -0.0157 2   ASP B OD2 
3649 N N   . THR B 3   ? 0.8282 0.8601 0.5730 0.1725  -0.1962 0.0061  3   THR B N   
3650 C CA  . THR B 3   ? 0.8658 0.8523 0.6028 0.1837  -0.1849 0.0079  3   THR B CA  
3651 C C   . THR B 3   ? 0.8550 0.7877 0.5460 0.1664  -0.1814 0.0189  3   THR B C   
3652 O O   . THR B 3   ? 0.8739 0.7969 0.5354 0.1533  -0.1918 0.0295  3   THR B O   
3653 C CB  . THR B 3   ? 0.8469 0.8203 0.5942 0.2179  -0.1993 0.0157  3   THR B CB  
3654 O OG1 . THR B 3   ? 0.9248 0.8757 0.6424 0.2250  -0.2214 0.0345  3   THR B OG1 
3655 C CG2 . THR B 3   ? 0.8146 0.8426 0.6115 0.2369  -0.2025 0.0062  3   THR B CG2 
3656 N N   . PHE B 4   ? 0.9032 0.8016 0.5887 0.1667  -0.1664 0.0158  4   PHE B N   
3657 C CA  . PHE B 4   ? 0.8730 0.7203 0.5214 0.1512  -0.1614 0.0248  4   PHE B CA  
3658 C C   . PHE B 4   ? 0.8854 0.6950 0.5329 0.1652  -0.1561 0.0224  4   PHE B C   
3659 O O   . PHE B 4   ? 0.8935 0.7189 0.5673 0.1804  -0.1490 0.0107  4   PHE B O   
3660 C CB  . PHE B 4   ? 0.8568 0.7117 0.4990 0.1211  -0.1414 0.0193  4   PHE B CB  
3661 C CG  . PHE B 4   ? 0.8404 0.7179 0.5104 0.1201  -0.1199 0.0039  4   PHE B CG  
3662 C CD1 . PHE B 4   ? 0.8144 0.7413 0.5199 0.1270  -0.1140 -0.0085 4   PHE B CD1 
3663 C CD2 . PHE B 4   ? 0.8366 0.6871 0.4976 0.1127  -0.1053 0.0021  4   PHE B CD2 
3664 C CE1 . PHE B 4   ? 0.8014 0.7463 0.5300 0.1279  -0.0918 -0.0213 4   PHE B CE1 
3665 C CE2 . PHE B 4   ? 0.7458 0.6177 0.4288 0.1138  -0.0859 -0.0105 4   PHE B CE2 
3666 C CZ  . PHE B 4   ? 0.7604 0.6777 0.4757 0.1219  -0.0782 -0.0215 4   PHE B CZ  
3667 N N   . ILE B 5   ? 0.9137 0.6721 0.5298 0.1589  -0.1581 0.0329  5   ILE B N   
3668 C CA  . ILE B 5   ? 0.8933 0.6109 0.5042 0.1671  -0.1529 0.0294  5   ILE B CA  
3669 C C   . ILE B 5   ? 0.9114 0.6246 0.5198 0.1450  -0.1347 0.0208  5   ILE B C   
3670 O O   . ILE B 5   ? 0.8744 0.5729 0.4633 0.1221  -0.1298 0.0281  5   ILE B O   
3671 C CB  . ILE B 5   ? 0.9480 0.6108 0.5292 0.1724  -0.1634 0.0446  5   ILE B CB  
3672 C CG1 . ILE B 5   ? 1.0041 0.6753 0.5816 0.1903  -0.1818 0.0584  5   ILE B CG1 
3673 C CG2 . ILE B 5   ? 0.9756 0.6028 0.5587 0.1879  -0.1602 0.0381  5   ILE B CG2 
3674 C CD1 . ILE B 5   ? 1.0280 0.7216 0.6345 0.2198  -0.1877 0.0528  5   ILE B CD1 
3675 N N   . ALA B 6   ? 0.9614 0.6854 0.5883 0.1532  -0.1245 0.0062  6   ALA B N   
3676 C CA  . ALA B 6   ? 0.9028 0.6278 0.5293 0.1362  -0.1082 -0.0019 6   ALA B CA  
3677 C C   . ALA B 6   ? 0.9349 0.6134 0.5454 0.1365  -0.1094 -0.0043 6   ALA B C   
3678 O O   . ALA B 6   ? 0.9584 0.6091 0.5650 0.1549  -0.1183 -0.0050 6   ALA B O   
3679 C CB  . ALA B 6   ? 0.8788 0.6462 0.5328 0.1445  -0.0948 -0.0163 6   ALA B CB  
3680 N N   . ALA B 7   ? 0.8497 0.5183 0.4509 0.1149  -0.1001 -0.0047 7   ALA B N   
3681 C CA  . ALA B 7   ? 0.8864 0.5163 0.4754 0.1109  -0.1006 -0.0098 7   ALA B CA  
3682 C C   . ALA B 7   ? 0.8764 0.5270 0.4729 0.0985  -0.0876 -0.0197 7   ALA B C   
3683 O O   . ALA B 7   ? 0.8383 0.5171 0.4406 0.0834  -0.0769 -0.0151 7   ALA B O   
3684 C CB  . ALA B 7   ? 0.8849 0.4705 0.4514 0.0956  -0.1059 0.0038  7   ALA B CB  
3685 N N   . VAL B 8   ? 0.8574 0.4932 0.4522 0.1052  -0.0880 -0.0330 8   VAL B N   
3686 C CA  . VAL B 8   ? 0.7935 0.4446 0.3911 0.0939  -0.0790 -0.0420 8   VAL B CA  
3687 C C   . VAL B 8   ? 0.8426 0.4524 0.4263 0.0863  -0.0859 -0.0493 8   VAL B C   
3688 O O   . VAL B 8   ? 0.8527 0.4271 0.4280 0.0988  -0.0940 -0.0544 8   VAL B O   
3689 C CB  . VAL B 8   ? 0.8094 0.4960 0.4204 0.1114  -0.0706 -0.0553 8   VAL B CB  
3690 C CG1 . VAL B 8   ? 0.7714 0.5015 0.3997 0.1144  -0.0598 -0.0495 8   VAL B CG1 
3691 C CG2 . VAL B 8   ? 0.8425 0.5088 0.4515 0.1356  -0.0776 -0.0667 8   VAL B CG2 
3692 N N   . TYR B 9   ? 0.8263 0.4405 0.4093 0.0656  -0.0817 -0.0497 9   TYR B N   
3693 C CA  . TYR B 9   ? 0.8710 0.4504 0.4442 0.0543  -0.0879 -0.0584 9   TYR B CA  
3694 C C   . TYR B 9   ? 0.8979 0.5032 0.4750 0.0516  -0.0851 -0.0735 9   TYR B C   
3695 O O   . TYR B 9   ? 0.8532 0.4978 0.4403 0.0434  -0.0765 -0.0685 9   TYR B O   
3696 C CB  . TYR B 9   ? 0.9074 0.4637 0.4765 0.0297  -0.0876 -0.0448 9   TYR B CB  
3697 C CG  . TYR B 9   ? 0.8902 0.4051 0.4516 0.0177  -0.0936 -0.0541 9   TYR B CG  
3698 C CD1 . TYR B 9   ? 0.9284 0.3991 0.4782 0.0301  -0.1003 -0.0621 9   TYR B CD1 
3699 C CD2 . TYR B 9   ? 0.9055 0.4252 0.4730 -0.0063 -0.0914 -0.0549 9   TYR B CD2 
3700 C CE1 . TYR B 9   ? 0.9606 0.3902 0.5038 0.0173  -0.1035 -0.0723 9   TYR B CE1 
3701 C CE2 . TYR B 9   ? 0.9416 0.4246 0.5050 -0.0196 -0.0966 -0.0655 9   TYR B CE2 
3702 C CZ  . TYR B 9   ? 0.9746 0.4113 0.5252 -0.0085 -0.1021 -0.0749 9   TYR B CZ  
3703 O OH  . TYR B 9   ? 1.0336 0.4323 0.5810 -0.0237 -0.1049 -0.0871 9   TYR B OH  
3704 N N   . GLU B 10  ? 0.8464 0.4290 0.4142 0.0591  -0.0917 -0.0917 10  GLU B N   
3705 C CA  . GLU B 10  ? 0.8746 0.4751 0.4406 0.0539  -0.0926 -0.1076 10  GLU B CA  
3706 C C   . GLU B 10  ? 0.8749 0.4499 0.4383 0.0278  -0.0991 -0.1105 10  GLU B C   
3707 O O   . GLU B 10  ? 0.9122 0.4389 0.4662 0.0239  -0.1050 -0.1163 10  GLU B O   
3708 C CB  . GLU B 10  ? 0.8556 0.4465 0.4106 0.0756  -0.0951 -0.1278 10  GLU B CB  
3709 C CG  . GLU B 10  ? 0.8813 0.4796 0.4273 0.0696  -0.0992 -0.1471 10  GLU B CG  
3710 C CD  . GLU B 10  ? 0.9022 0.5162 0.4392 0.0946  -0.0951 -0.1624 10  GLU B CD  
3711 O OE1 . GLU B 10  ? 0.8626 0.5057 0.4091 0.1124  -0.0852 -0.1537 10  GLU B OE1 
3712 O OE2 . GLU B 10  ? 0.9053 0.5014 0.4257 0.0958  -0.1007 -0.1834 10  GLU B OE2 
3713 N N   . HIS B 11  ? 0.8920 0.4994 0.4657 0.0103  -0.0965 -0.1059 11  HIS B N   
3714 C CA  . HIS B 11  ? 0.8960 0.4870 0.4749 -0.0170 -0.1003 -0.1036 11  HIS B CA  
3715 C C   . HIS B 11  ? 0.9225 0.5300 0.5013 -0.0261 -0.1081 -0.1232 11  HIS B C   
3716 O O   . HIS B 11  ? 0.8828 0.5381 0.4665 -0.0211 -0.1057 -0.1246 11  HIS B O   
3717 C CB  . HIS B 11  ? 0.8620 0.4773 0.4557 -0.0315 -0.0906 -0.0806 11  HIS B CB  
3718 C CG  . HIS B 11  ? 0.8718 0.4741 0.4751 -0.0594 -0.0920 -0.0762 11  HIS B CG  
3719 N ND1 . HIS B 11  ? 0.9251 0.4761 0.5227 -0.0716 -0.0980 -0.0823 11  HIS B ND1 
3720 C CD2 . HIS B 11  ? 0.8521 0.4859 0.4725 -0.0770 -0.0862 -0.0658 11  HIS B CD2 
3721 C CE1 . HIS B 11  ? 0.9153 0.4677 0.5273 -0.0967 -0.0964 -0.0768 11  HIS B CE1 
3722 N NE2 . HIS B 11  ? 0.8895 0.4928 0.5161 -0.1001 -0.0898 -0.0663 11  HIS B NE2 
3723 N N   . ALA B 12  ? 1.0006 0.5682 0.5728 -0.0386 -0.1169 -0.1388 12  ALA B N   
3724 C CA  . ALA B 12  ? 1.0222 0.6030 0.5963 -0.0547 -0.1263 -0.1579 12  ALA B CA  
3725 C C   . ALA B 12  ? 1.0384 0.6413 0.6348 -0.0805 -0.1246 -0.1438 12  ALA B C   
3726 O O   . ALA B 12  ? 1.0702 0.6385 0.6738 -0.1011 -0.1252 -0.1416 12  ALA B O   
3727 C CB  . ALA B 12  ? 1.0449 0.5711 0.6058 -0.0616 -0.1337 -0.1799 12  ALA B CB  
3728 N N   . ALA B 13  ? 0.8959 0.5558 0.5045 -0.0792 -0.1209 -0.1338 13  ALA B N   
3729 C CA  . ALA B 13  ? 0.9107 0.5926 0.5424 -0.0987 -0.1140 -0.1135 13  ALA B CA  
3730 C C   . ALA B 13  ? 0.9330 0.6240 0.5803 -0.1246 -0.1241 -0.1242 13  ALA B C   
3731 O O   . ALA B 13  ? 0.9734 0.6821 0.6155 -0.1251 -0.1367 -0.1458 13  ALA B O   
3732 C CB  . ALA B 13  ? 0.8639 0.6016 0.5042 -0.0864 -0.1028 -0.0967 13  ALA B CB  
3733 N N   . ILE B 14  ? 1.0602 0.7384 0.7267 -0.1469 -0.1184 -0.1095 14  ILE B N   
3734 C CA  . ILE B 14  ? 1.0695 0.7630 0.7590 -0.1736 -0.1258 -0.1160 14  ILE B CA  
3735 C C   . ILE B 14  ? 1.0073 0.7701 0.7164 -0.1725 -0.1224 -0.1022 14  ILE B C   
3736 O O   . ILE B 14  ? 0.9380 0.7158 0.6575 -0.1701 -0.1065 -0.0765 14  ILE B O   
3737 C CB  . ILE B 14  ? 1.0717 0.7216 0.7755 -0.1969 -0.1180 -0.1045 14  ILE B CB  
3738 C CG1 . ILE B 14  ? 1.0669 0.6492 0.7536 -0.2004 -0.1224 -0.1217 14  ILE B CG1 
3739 C CG2 . ILE B 14  ? 1.0494 0.7266 0.7862 -0.2246 -0.1210 -0.1040 14  ILE B CG2 
3740 C CD1 . ILE B 14  ? 1.1207 0.6690 0.7786 -0.1743 -0.1186 -0.1197 14  ILE B CD1 
3741 N N   . LEU B 15  ? 1.0057 0.8109 0.7174 -0.1727 -0.1365 -0.1191 15  LEU B N   
3742 C CA  . LEU B 15  ? 0.9786 0.8529 0.7063 -0.1672 -0.1343 -0.1064 15  LEU B CA  
3743 C C   . LEU B 15  ? 0.9807 0.8822 0.7441 -0.1941 -0.1375 -0.0995 15  LEU B C   
3744 O O   . LEU B 15  ? 1.0095 0.8946 0.7817 -0.2159 -0.1515 -0.1187 15  LEU B O   
3745 C CB  . LEU B 15  ? 0.9730 0.8829 0.6821 -0.1502 -0.1481 -0.1265 15  LEU B CB  
3746 C CG  . LEU B 15  ? 0.9815 0.8726 0.6573 -0.1214 -0.1446 -0.1348 15  LEU B CG  
3747 C CD1 . LEU B 15  ? 0.9923 0.9159 0.6477 -0.1071 -0.1586 -0.1566 15  LEU B CD1 
3748 C CD2 . LEU B 15  ? 0.9394 0.8424 0.6171 -0.1030 -0.1228 -0.1079 15  LEU B CD2 
3749 N N   . PRO B 16  ? 0.9913 0.9352 0.7777 -0.1935 -0.1238 -0.0729 16  PRO B N   
3750 C CA  . PRO B 16  ? 0.9851 0.9607 0.8096 -0.2176 -0.1264 -0.0650 16  PRO B CA  
3751 C C   . PRO B 16  ? 1.0819 1.1021 0.9118 -0.2226 -0.1505 -0.0878 16  PRO B C   
3752 O O   . PRO B 16  ? 1.0899 1.1450 0.9002 -0.2013 -0.1580 -0.0955 16  PRO B O   
3753 C CB  . PRO B 16  ? 0.9981 1.0148 0.8403 -0.2079 -0.1048 -0.0318 16  PRO B CB  
3754 C CG  . PRO B 16  ? 1.0021 1.0205 0.8149 -0.1780 -0.0947 -0.0273 16  PRO B CG  
3755 C CD  . PRO B 16  ? 1.0085 0.9687 0.7894 -0.1723 -0.1026 -0.0482 16  PRO B CD  
3756 N N   . ASN B 17  ? 1.2889 1.3074 1.1450 -0.2516 -0.1624 -0.0992 17  ASN B N   
3757 C CA  . ASN B 17  ? 1.2877 1.3542 1.1534 -0.2607 -0.1870 -0.1213 17  ASN B CA  
3758 C C   . ASN B 17  ? 1.2737 1.4164 1.1452 -0.2403 -0.1866 -0.1043 17  ASN B C   
3759 O O   . ASN B 17  ? 1.2709 1.4346 1.1582 -0.2309 -0.1656 -0.0724 17  ASN B O   
3760 C CB  . ASN B 17  ? 1.2882 1.3580 1.1956 -0.2964 -0.1944 -0.1265 17  ASN B CB  
3761 C CG  . ASN B 17  ? 1.3625 1.3731 1.2595 -0.3172 -0.2060 -0.1588 17  ASN B CG  
3762 O OD1 . ASN B 17  ? 1.3816 1.3689 1.2422 -0.3066 -0.2174 -0.1844 17  ASN B OD1 
3763 N ND2 . ASN B 17  ? 1.2983 1.2822 1.2278 -0.3467 -0.2010 -0.1577 17  ASN B ND2 
3764 N N   . ALA B 18  ? 1.0685 1.2503 0.9240 -0.2319 -0.2081 -0.1255 18  ALA B N   
3765 C CA  . ALA B 18  ? 1.0840 1.3399 0.9439 -0.2113 -0.2083 -0.1089 18  ALA B CA  
3766 C C   . ALA B 18  ? 1.0132 1.3187 0.9247 -0.2288 -0.2055 -0.0866 18  ALA B C   
3767 O O   . ALA B 18  ? 1.0410 1.3608 0.9798 -0.2563 -0.2239 -0.1018 18  ALA B O   
3768 C CB  . ALA B 18  ? 1.0373 1.3267 0.8703 -0.2026 -0.2349 -0.1377 18  ALA B CB  
3769 N N   . THR B 19  ? 0.9647 1.2955 0.8917 -0.2138 -0.1810 -0.0507 19  THR B N   
3770 C CA  . THR B 19  ? 0.9740 1.3522 0.9513 -0.2274 -0.1744 -0.0259 19  THR B CA  
3771 C C   . THR B 19  ? 0.9310 1.3776 0.9137 -0.2000 -0.1638 0.0011  19  THR B C   
3772 O O   . THR B 19  ? 0.8595 1.3022 0.8117 -0.1711 -0.1482 0.0109  19  THR B O   
3773 C CB  . THR B 19  ? 0.9959 1.3294 0.9985 -0.2437 -0.1477 -0.0027 19  THR B CB  
3774 O OG1 . THR B 19  ? 0.9447 1.2542 0.9261 -0.2210 -0.1189 0.0199  19  THR B OG1 
3775 C CG2 . THR B 19  ? 1.0336 1.2969 1.0334 -0.2710 -0.1551 -0.0259 19  THR B CG2 
3776 N N   . LEU B 20  ? 1.1437 1.6543 1.1679 -0.2099 -0.1727 0.0123  20  LEU B N   
3777 C CA  . LEU B 20  ? 1.0199 1.6044 1.0578 -0.1863 -0.1649 0.0397  20  LEU B CA  
3778 C C   . LEU B 20  ? 1.0214 1.6025 1.0838 -0.1792 -0.1259 0.0806  20  LEU B C   
3779 O O   . LEU B 20  ? 0.9030 1.4955 0.9480 -0.1502 -0.1031 0.1016  20  LEU B O   
3780 C CB  . LEU B 20  ? 1.0713 1.7251 1.1461 -0.2027 -0.1938 0.0321  20  LEU B CB  
3781 C CG  . LEU B 20  ? 1.1362 1.7520 1.1972 -0.2299 -0.2244 -0.0124 20  LEU B CG  
3782 C CD1 . LEU B 20  ? 1.0849 1.7316 1.1961 -0.2655 -0.2461 -0.0241 20  LEU B CD1 
3783 C CD2 . LEU B 20  ? 1.0443 1.6686 1.0537 -0.2122 -0.2489 -0.0427 20  LEU B CD2 
3784 N N   . THR B 21  ? 0.9911 1.5488 1.0907 -0.2060 -0.1156 0.0906  21  THR B N   
3785 C CA  . THR B 21  ? 0.8615 1.4144 0.9885 -0.2050 -0.0791 0.1280  21  THR B CA  
3786 C C   . THR B 21  ? 0.8943 1.3619 1.0050 -0.2176 -0.0590 0.1271  21  THR B C   
3787 O O   . THR B 21  ? 0.9744 1.3898 1.0630 -0.2315 -0.0752 0.0987  21  THR B O   
3788 C CB  . THR B 21  ? 0.8504 1.4525 1.0384 -0.2250 -0.0809 0.1449  21  THR B CB  
3789 O OG1 . THR B 21  ? 0.8518 1.4497 1.0565 -0.2551 -0.1125 0.1147  21  THR B OG1 
3790 C CG2 . THR B 21  ? 0.8277 1.5195 1.0347 -0.2022 -0.0843 0.1650  21  THR B CG2 
3791 N N   . PRO B 22  ? 0.6230 1.0739 0.7412 -0.2114 -0.0226 0.1580  22  PRO B N   
3792 C CA  . PRO B 22  ? 0.5911 0.9630 0.6872 -0.2200 -0.0032 0.1581  22  PRO B CA  
3793 C C   . PRO B 22  ? 0.6223 0.9507 0.7374 -0.2531 -0.0116 0.1468  22  PRO B C   
3794 O O   . PRO B 22  ? 0.6036 0.9610 0.7638 -0.2720 -0.0141 0.1552  22  PRO B O   
3795 C CB  . PRO B 22  ? 0.5442 0.9208 0.6520 -0.2091 0.0375  0.1952  22  PRO B CB  
3796 C CG  . PRO B 22  ? 0.5265 0.9828 0.6512 -0.1858 0.0399  0.2125  22  PRO B CG  
3797 C CD  . PRO B 22  ? 0.5296 1.0335 0.6771 -0.1967 0.0032  0.1946  22  PRO B CD  
3798 N N   . VAL B 23  ? 0.7088 0.9671 0.7901 -0.2594 -0.0146 0.1286  23  VAL B N   
3799 C CA  . VAL B 23  ? 0.7106 0.9164 0.8040 -0.2883 -0.0168 0.1203  23  VAL B CA  
3800 C C   . VAL B 23  ? 0.7174 0.8905 0.8211 -0.2948 0.0187  0.1505  23  VAL B C   
3801 O O   . VAL B 23  ? 0.6530 0.8349 0.7465 -0.2767 0.0434  0.1726  23  VAL B O   
3802 C CB  . VAL B 23  ? 0.7483 0.8912 0.8006 -0.2904 -0.0330 0.0905  23  VAL B CB  
3803 C CG1 . VAL B 23  ? 0.7841 0.9535 0.8292 -0.2898 -0.0673 0.0585  23  VAL B CG1 
3804 C CG2 . VAL B 23  ? 0.7294 0.8403 0.7383 -0.2670 -0.0183 0.0957  23  VAL B CG2 
3805 N N   . SER B 24  ? 0.7094 0.8420 0.8319 -0.3207 0.0233  0.1510  24  SER B N   
3806 C CA  . SER B 24  ? 0.7317 0.8196 0.8548 -0.3139 0.0566  0.1698  24  SER B CA  
3807 C C   . SER B 24  ? 0.7488 0.7737 0.8215 -0.2946 0.0664  0.1629  24  SER B C   
3808 O O   . SER B 24  ? 0.7628 0.7727 0.8014 -0.3061 0.0481  0.1517  24  SER B O   
3809 C CB  . SER B 24  ? 0.6965 0.7540 0.8498 -0.3290 0.0598  0.1630  24  SER B CB  
3810 O OG  . SER B 24  ? 0.7809 0.7863 0.9132 -0.3471 0.0436  0.1431  24  SER B OG  
3811 N N   . ARG B 25  ? 0.7411 1.0803 0.9283 -0.2574 0.0618  -0.0946 25  ARG B N   
3812 C CA  . ARG B 25  ? 0.7225 0.9992 0.8611 -0.2503 0.0711  -0.0750 25  ARG B CA  
3813 C C   . ARG B 25  ? 0.7188 0.9479 0.8348 -0.2792 0.0866  -0.0690 25  ARG B C   
3814 O O   . ARG B 25  ? 0.7473 0.9178 0.8206 -0.2738 0.0844  -0.0569 25  ARG B O   
3815 C CB  . ARG B 25  ? 0.6826 0.9700 0.8177 -0.2355 0.0854  -0.0676 25  ARG B CB  
3816 C CG  . ARG B 25  ? 0.8364 1.0722 0.9261 -0.2129 0.0823  -0.0511 25  ARG B CG  
3817 C CD  . ARG B 25  ? 0.8382 1.0090 0.8869 -0.2256 0.0891  -0.0395 25  ARG B CD  
3818 N NE  . ARG B 25  ? 0.7770 0.9053 0.7874 -0.2060 0.0881  -0.0265 25  ARG B NE  
3819 C CZ  . ARG B 25  ? 0.8220 0.9272 0.8153 -0.1881 0.0708  -0.0223 25  ARG B CZ  
3820 N NH1 . ARG B 25  ? 0.7495 0.8660 0.7548 -0.1854 0.0544  -0.0282 25  ARG B NH1 
3821 N NH2 . ARG B 25  ? 0.8112 0.8816 0.7744 -0.1730 0.0703  -0.0127 25  ARG B NH2 
3822 N N   . GLU B 26  ? 0.8609 1.1139 1.0051 -0.3099 0.1019  -0.0785 26  GLU B N   
3823 C CA  . GLU B 26  ? 0.9415 1.1434 1.0611 -0.3398 0.1176  -0.0731 26  GLU B CA  
3824 C C   . GLU B 26  ? 0.9493 1.1091 1.0459 -0.3412 0.0983  -0.0748 26  GLU B C   
3825 O O   . GLU B 26  ? 0.9500 1.0441 0.9996 -0.3409 0.1014  -0.0625 26  GLU B O   
3826 C CB  . GLU B 26  ? 0.9586 1.2001 1.1201 -0.3757 0.1368  -0.0857 26  GLU B CB  
3827 C CG  . GLU B 26  ? 1.0711 1.2540 1.2024 -0.4093 0.1599  -0.0776 26  GLU B CG  
3828 C CD  . GLU B 26  ? 1.1150 1.2911 1.2621 -0.4397 0.1524  -0.0917 26  GLU B CD  
3829 O OE1 . GLU B 26  ? 1.1363 1.2411 1.2379 -0.4470 0.1500  -0.0840 26  GLU B OE1 
3830 O OE2 . GLU B 26  ? 1.0870 1.3260 1.2892 -0.4504 0.1463  -0.1105 26  GLU B OE2 
3831 N N   . GLU B 27  ? 0.8304 1.0275 0.9578 -0.3404 0.0775  -0.0910 27  GLU B N   
3832 C CA  . GLU B 27  ? 0.7748 0.9348 0.8802 -0.3407 0.0591  -0.0945 27  GLU B CA  
3833 C C   . GLU B 27  ? 0.7634 0.8823 0.8266 -0.3096 0.0475  -0.0807 27  GLU B C   
3834 O O   . GLU B 27  ? 0.7664 0.8291 0.7916 -0.3104 0.0450  -0.0745 27  GLU B O   
3835 C CB  . GLU B 27  ? 0.7599 0.9720 0.9050 -0.3412 0.0375  -0.1155 27  GLU B CB  
3836 C CG  . GLU B 27  ? 0.7837 1.0662 0.9863 -0.3590 0.0455  -0.1313 27  GLU B CG  
3837 C CD  . GLU B 27  ? 0.8239 1.1524 1.0661 -0.3675 0.0240  -0.1560 27  GLU B CD  
3838 O OE1 . GLU B 27  ? 0.7897 1.1870 1.0750 -0.3558 0.0144  -0.1698 27  GLU B OE1 
3839 O OE2 . GLU B 27  ? 0.8420 1.1371 1.0709 -0.3841 0.0153  -0.1629 27  GLU B OE2 
3840 N N   . ALA B 28  ? 0.5894 0.7356 0.6589 -0.2821 0.0409  -0.0764 28  ALA B N   
3841 C CA  . ALA B 28  ? 0.6380 0.7499 0.6730 -0.2554 0.0318  -0.0642 28  ALA B CA  
3842 C C   . ALA B 28  ? 0.6806 0.7369 0.6769 -0.2574 0.0459  -0.0495 28  ALA B C   
3843 O O   . ALA B 28  ? 0.6663 0.6783 0.6302 -0.2496 0.0394  -0.0440 28  ALA B O   
3844 C CB  . ALA B 28  ? 0.5947 0.7418 0.6429 -0.2293 0.0252  -0.0620 28  ALA B CB  
3845 N N   . LEU B 29  ? 0.7648 0.8229 0.7621 -0.2660 0.0651  -0.0438 29  LEU B N   
3846 C CA  . LEU B 29  ? 0.7728 0.7757 0.7280 -0.2650 0.0773  -0.0303 29  LEU B CA  
3847 C C   . LEU B 29  ? 0.7871 0.7389 0.7151 -0.2843 0.0806  -0.0302 29  LEU B C   
3848 O O   . LEU B 29  ? 0.8172 0.7185 0.7060 -0.2728 0.0759  -0.0227 29  LEU B O   
3849 C CB  . LEU B 29  ? 0.7981 0.8119 0.7561 -0.2709 0.0988  -0.0249 29  LEU B CB  
3850 C CG  . LEU B 29  ? 0.8070 0.7650 0.7173 -0.2655 0.1114  -0.0107 29  LEU B CG  
3851 C CD1 . LEU B 29  ? 0.8077 0.7422 0.6940 -0.2360 0.0943  -0.0046 29  LEU B CD1 
3852 C CD2 . LEU B 29  ? 0.7543 0.7312 0.6690 -0.2674 0.1321  -0.0066 29  LEU B CD2 
3853 N N   . ALA B 30  ? 0.6541 0.6192 0.6036 -0.3127 0.0865  -0.0404 30  ALA B N   
3854 C CA  . ALA B 30  ? 0.7468 0.6571 0.6675 -0.3329 0.0897  -0.0410 30  ALA B CA  
3855 C C   . ALA B 30  ? 0.7606 0.6413 0.6585 -0.3157 0.0681  -0.0432 30  ALA B C   
3856 O O   . ALA B 30  ? 0.8144 0.6336 0.6681 -0.3127 0.0684  -0.0368 30  ALA B O   
3857 C CB  . ALA B 30  ? 0.7216 0.6585 0.6773 -0.3681 0.0971  -0.0549 30  ALA B CB  
3858 N N   . LEU B 31  ? 0.7653 0.6873 0.6895 -0.3024 0.0495  -0.0525 31  LEU B N   
3859 C CA  . LEU B 31  ? 0.7660 0.6620 0.6673 -0.2851 0.0318  -0.0543 31  LEU B CA  
3860 C C   . LEU B 31  ? 0.7810 0.6489 0.6516 -0.2578 0.0303  -0.0413 31  LEU B C   
3861 O O   . LEU B 31  ? 0.8036 0.6268 0.6407 -0.2484 0.0245  -0.0393 31  LEU B O   
3862 C CB  . LEU B 31  ? 0.7244 0.6688 0.6555 -0.2751 0.0141  -0.0658 31  LEU B CB  
3863 C CG  . LEU B 31  ? 0.7609 0.6781 0.6650 -0.2556 -0.0006 -0.0662 31  LEU B CG  
3864 C CD1 . LEU B 31  ? 0.7239 0.6284 0.6253 -0.2705 -0.0109 -0.0808 31  LEU B CD1 
3865 C CD2 . LEU B 31  ? 0.7266 0.6784 0.6425 -0.2304 -0.0104 -0.0639 31  LEU B CD2 
3866 N N   . MET B 32  ? 0.7389 0.6347 0.6223 -0.2435 0.0338  -0.0343 32  MET B N   
3867 C CA  . MET B 32  ? 0.7447 0.6175 0.6037 -0.2198 0.0314  -0.0243 32  MET B CA  
3868 C C   . MET B 32  ? 0.8171 0.6327 0.6356 -0.2227 0.0406  -0.0168 32  MET B C   
3869 O O   . MET B 32  ? 0.8003 0.5843 0.5915 -0.2044 0.0337  -0.0132 32  MET B O   
3870 C CB  . MET B 32  ? 0.7472 0.6553 0.6254 -0.2068 0.0339  -0.0193 32  MET B CB  
3871 C CG  . MET B 32  ? 0.7243 0.6673 0.6228 -0.1901 0.0207  -0.0224 32  MET B CG  
3872 S SD  . MET B 32  ? 0.6813 0.6668 0.6047 -0.1786 0.0229  -0.0194 32  MET B SD  
3873 C CE  . MET B 32  ? 0.7118 0.7217 0.6563 -0.2020 0.0374  -0.0245 32  MET B CE  
3874 N N   . ASN B 33  ? 0.9213 0.7225 0.7340 -0.2449 0.0565  -0.0149 33  ASN B N   
3875 C CA  . ASN B 33  ? 0.9606 0.6992 0.7265 -0.2478 0.0665  -0.0066 33  ASN B CA  
3876 C C   . ASN B 33  ? 1.0193 0.7086 0.7556 -0.2526 0.0595  -0.0108 33  ASN B C   
3877 O O   . ASN B 33  ? 1.0408 0.6748 0.7320 -0.2397 0.0580  -0.0050 33  ASN B O   
3878 C CB  . ASN B 33  ? 0.9816 0.7173 0.7477 -0.2723 0.0892  -0.0023 33  ASN B CB  
3879 C CG  . ASN B 33  ? 0.9993 0.7553 0.7684 -0.2598 0.0984  0.0056  33  ASN B CG  
3880 O OD1 . ASN B 33  ? 0.9763 0.7127 0.7209 -0.2348 0.0914  0.0119  33  ASN B OD1 
3881 N ND2 . ASN B 33  ? 0.9738 0.7708 0.7739 -0.2767 0.1136  0.0037  33  ASN B ND2 
3882 N N   . ARG B 34  ? 0.9131 0.6196 0.6717 -0.2691 0.0538  -0.0220 34  ARG B N   
3883 C CA  . ARG B 34  ? 0.9520 0.6129 0.6822 -0.2700 0.0440  -0.0280 34  ARG B CA  
3884 C C   . ARG B 34  ? 0.9426 0.5940 0.6556 -0.2368 0.0283  -0.0274 34  ARG B C   
3885 O O   . ARG B 34  ? 0.9310 0.5284 0.6029 -0.2263 0.0237  -0.0267 34  ARG B O   
3886 C CB  . ARG B 34  ? 0.9583 0.6476 0.7194 -0.2898 0.0369  -0.0426 34  ARG B CB  
3887 C CG  . ARG B 34  ? 0.9895 0.6823 0.7674 -0.3271 0.0521  -0.0468 34  ARG B CG  
3888 C CD  . ARG B 34  ? 0.9728 0.6931 0.7809 -0.3443 0.0403  -0.0645 34  ARG B CD  
3889 N NE  . ARG B 34  ? 1.0327 0.7046 0.8067 -0.3372 0.0260  -0.0708 34  ARG B NE  
3890 C CZ  . ARG B 34  ? 1.0320 0.7189 0.8205 -0.3419 0.0100  -0.0867 34  ARG B CZ  
3891 N NH1 . ARG B 34  ? 0.9762 0.7262 0.8135 -0.3530 0.0044  -0.0986 34  ARG B NH1 
3892 N NH2 . ARG B 34  ? 1.0238 0.6599 0.7750 -0.3338 -0.0015 -0.0921 34  ARG B NH2 
3893 N N   . ASN B 35  ? 0.8630 0.5662 0.6069 -0.2199 0.0205  -0.0281 35  ASN B N   
3894 C CA  . ASN B 35  ? 0.8328 0.5334 0.5661 -0.1907 0.0089  -0.0276 35  ASN B CA  
3895 C C   . ASN B 35  ? 0.8732 0.5461 0.5804 -0.1732 0.0116  -0.0186 35  ASN B C   
3896 O O   . ASN B 35  ? 0.8881 0.5317 0.5693 -0.1532 0.0034  -0.0198 35  ASN B O   
3897 C CB  . ASN B 35  ? 0.7874 0.5460 0.5581 -0.1805 0.0024  -0.0298 35  ASN B CB  
3898 C CG  . ASN B 35  ? 0.8118 0.5855 0.5926 -0.1830 -0.0075 -0.0404 35  ASN B CG  
3899 O OD1 . ASN B 35  ? 0.8012 0.5511 0.5609 -0.1714 -0.0150 -0.0450 35  ASN B OD1 
3900 N ND2 . ASN B 35  ? 0.7569 0.5691 0.5676 -0.1965 -0.0081 -0.0455 35  ASN B ND2 
3901 N N   . LEU B 36  ? 0.7506 0.4340 0.4640 -0.1781 0.0221  -0.0109 36  LEU B N   
3902 C CA  . LEU B 36  ? 0.8389 0.4962 0.5253 -0.1599 0.0228  -0.0035 36  LEU B CA  
3903 C C   . LEU B 36  ? 0.8347 0.4218 0.4677 -0.1586 0.0251  -0.0006 36  LEU B C   
3904 O O   . LEU B 36  ? 0.8461 0.4058 0.4506 -0.1354 0.0184  0.0017  36  LEU B O   
3905 C CB  . LEU B 36  ? 0.7655 0.4450 0.4647 -0.1652 0.0342  0.0034  36  LEU B CB  
3906 C CG  . LEU B 36  ? 0.7402 0.4793 0.4824 -0.1569 0.0288  0.0015  36  LEU B CG  
3907 C CD1 . LEU B 36  ? 0.7144 0.4818 0.4760 -0.1686 0.0411  0.0050  36  LEU B CD1 
3908 C CD2 . LEU B 36  ? 0.6930 0.4373 0.4344 -0.1305 0.0172  0.0015  36  LEU B CD2 
3909 N N   . ASP B 37  ? 0.9578 0.5137 0.5756 -0.1827 0.0337  -0.0014 37  ASP B N   
3910 C CA  . ASP B 37  ? 1.0214 0.5011 0.5823 -0.1817 0.0353  0.0013  37  ASP B CA  
3911 C C   . ASP B 37  ? 1.0511 0.5082 0.5914 -0.1549 0.0172  -0.0058 37  ASP B C   
3912 O O   . ASP B 37  ? 1.0825 0.4912 0.5783 -0.1327 0.0116  -0.0031 37  ASP B O   
3913 C CB  . ASP B 37  ? 1.0323 0.4870 0.5879 -0.2167 0.0475  -0.0005 37  ASP B CB  
3914 C CG  . ASP B 37  ? 1.0998 0.5663 0.6669 -0.2432 0.0695  0.0069  37  ASP B CG  
3915 O OD1 . ASP B 37  ? 1.1171 0.5876 0.6755 -0.2310 0.0760  0.0158  37  ASP B OD1 
3916 O OD2 . ASP B 37  ? 1.0762 0.5487 0.6609 -0.2760 0.0803  0.0027  37  ASP B OD2 
3917 N N   . ILE B 38  ? 0.9220 0.4122 0.4913 -0.1551 0.0078  -0.0157 38  ILE B N   
3918 C CA  . ILE B 38  ? 0.9513 0.4277 0.5050 -0.1288 -0.0075 -0.0236 38  ILE B CA  
3919 C C   . ILE B 38  ? 0.9241 0.4276 0.4879 -0.0988 -0.0155 -0.0227 38  ILE B C   
3920 O O   . ILE B 38  ? 0.9453 0.4180 0.4789 -0.0724 -0.0252 -0.0255 38  ILE B O   
3921 C CB  . ILE B 38  ? 0.9383 0.4491 0.5213 -0.1351 -0.0139 -0.0340 38  ILE B CB  
3922 C CG1 . ILE B 38  ? 0.9574 0.4353 0.5270 -0.1633 -0.0098 -0.0385 38  ILE B CG1 
3923 C CG2 . ILE B 38  ? 0.9029 0.4094 0.4744 -0.1058 -0.0272 -0.0422 38  ILE B CG2 
3924 C CD1 . ILE B 38  ? 0.9123 0.4423 0.5255 -0.1816 -0.0113 -0.0463 38  ILE B CD1 
3925 N N   . LEU B 39  ? 0.8470 0.4091 0.4544 -0.1018 -0.0125 -0.0201 39  LEU B N   
3926 C CA  . LEU B 39  ? 0.8562 0.4462 0.4780 -0.0774 -0.0199 -0.0205 39  LEU B CA  
3927 C C   . LEU B 39  ? 0.9184 0.4669 0.5022 -0.0629 -0.0213 -0.0154 39  LEU B C   
3928 O O   . LEU B 39  ? 0.9430 0.4937 0.5222 -0.0362 -0.0328 -0.0200 39  LEU B O   
3929 C CB  . LEU B 39  ? 0.7896 0.4399 0.4589 -0.0858 -0.0155 -0.0178 39  LEU B CB  
3930 C CG  . LEU B 39  ? 0.7742 0.4685 0.4793 -0.0938 -0.0161 -0.0226 39  LEU B CG  
3931 C CD1 . LEU B 39  ? 0.7101 0.4559 0.4544 -0.0952 -0.0137 -0.0193 39  LEU B CD1 
3932 C CD2 . LEU B 39  ? 0.7260 0.4199 0.4271 -0.0760 -0.0250 -0.0311 39  LEU B CD2 
3933 N N   . GLU B 40  ? 0.9794 0.4915 0.5360 -0.0796 -0.0094 -0.0067 40  GLU B N   
3934 C CA  . GLU B 40  ? 1.0434 0.5078 0.5539 -0.0647 -0.0097 -0.0007 40  GLU B CA  
3935 C C   . GLU B 40  ? 1.0691 0.4725 0.5283 -0.0438 -0.0203 -0.0046 40  GLU B C   
3936 O O   . GLU B 40  ? 1.0723 0.4526 0.5027 -0.0154 -0.0313 -0.0058 40  GLU B O   
3937 C CB  . GLU B 40  ? 1.0540 0.4916 0.5443 -0.0896 0.0095  0.0104  40  GLU B CB  
3938 C CG  . GLU B 40  ? 1.1389 0.5021 0.5615 -0.0768 0.0114  0.0176  40  GLU B CG  
3939 C CD  . GLU B 40  ? 1.1418 0.4863 0.5461 -0.0972 0.0326  0.0295  40  GLU B CD  
3940 O OE1 . GLU B 40  ? 1.1562 0.5511 0.6056 -0.1207 0.0449  0.0307  40  GLU B OE1 
3941 O OE2 . GLU B 40  ? 1.3499 0.6285 0.6926 -0.0884 0.0375  0.0375  40  GLU B OE2 
3942 N N   . GLY B 41  ? 1.0593 0.4342 0.5044 -0.0558 -0.0187 -0.0077 41  GLY B N   
3943 C CA  . GLY B 41  ? 1.1074 0.4263 0.5051 -0.0320 -0.0310 -0.0135 41  GLY B CA  
3944 C C   . GLY B 41  ? 1.0855 0.4419 0.5041 0.0028  -0.0491 -0.0248 41  GLY B C   
3945 O O   . GLY B 41  ? 1.1086 0.4321 0.4914 0.0342  -0.0620 -0.0285 41  GLY B O   
3946 N N   . ALA B 42  ? 1.0385 0.4657 0.5159 -0.0022 -0.0499 -0.0307 42  ALA B N   
3947 C CA  . ALA B 42  ? 1.0196 0.4904 0.5248 0.0259  -0.0632 -0.0418 42  ALA B CA  
3948 C C   . ALA B 42  ? 0.9921 0.4783 0.5022 0.0453  -0.0707 -0.0417 42  ALA B C   
3949 O O   . ALA B 42  ? 1.0227 0.5053 0.5220 0.0769  -0.0856 -0.0512 42  ALA B O   
3950 C CB  . ALA B 42  ? 0.9285 0.4671 0.4914 0.0126  -0.0585 -0.0455 42  ALA B CB  
3951 N N   . ILE B 43  ? 0.9955 0.4996 0.5216 0.0281  -0.0617 -0.0327 43  ILE B N   
3952 C CA  . ILE B 43  ? 0.9868 0.5084 0.5200 0.0447  -0.0695 -0.0337 43  ILE B CA  
3953 C C   . ILE B 43  ? 1.0370 0.4949 0.5083 0.0700  -0.0796 -0.0335 43  ILE B C   
3954 O O   . ILE B 43  ? 1.0309 0.4982 0.5014 0.0998  -0.0966 -0.0431 43  ILE B O   
3955 C CB  . ILE B 43  ? 0.9514 0.4964 0.5059 0.0216  -0.0568 -0.0238 43  ILE B CB  
3956 C CG1 . ILE B 43  ? 0.8998 0.5086 0.5139 0.0027  -0.0501 -0.0251 43  ILE B CG1 
3957 C CG2 . ILE B 43  ? 0.9217 0.4695 0.4697 0.0403  -0.0660 -0.0251 43  ILE B CG2 
3958 C CD1 . ILE B 43  ? 0.8436 0.4659 0.4718 -0.0242 -0.0349 -0.0150 43  ILE B CD1 
3959 N N   . THR B 44  ? 1.1175 0.5085 0.5348 0.0586  -0.0696 -0.0231 44  THR B N   
3960 C CA  . THR B 44  ? 1.1773 0.4975 0.5256 0.0833  -0.0779 -0.0208 44  THR B CA  
3961 C C   . THR B 44  ? 1.2087 0.5116 0.5378 0.1177  -0.0977 -0.0342 44  THR B C   
3962 O O   . THR B 44  ? 1.2294 0.5114 0.5283 0.1520  -0.1149 -0.0404 44  THR B O   
3963 C CB  . THR B 44  ? 1.2587 0.5050 0.5501 0.0609  -0.0599 -0.0061 44  THR B CB  
3964 O OG1 . THR B 44  ? 1.3038 0.5410 0.6020 0.0389  -0.0519 -0.0069 44  THR B OG1 
3965 C CG2 . THR B 44  ? 1.1808 0.4435 0.4855 0.0337  -0.0407 0.0060  44  THR B CG2 
3966 N N   . SER B 45  ? 1.2188 0.5301 0.5633 0.1115  -0.0966 -0.0400 45  SER B N   
3967 C CA  . SER B 45  ? 1.1955 0.4933 0.5229 0.1460  -0.1145 -0.0541 45  SER B CA  
3968 C C   . SER B 45  ? 1.1741 0.5402 0.5490 0.1743  -0.1313 -0.0695 45  SER B C   
3969 O O   . SER B 45  ? 1.1979 0.5467 0.5469 0.2129  -0.1509 -0.0805 45  SER B O   
3970 C CB  . SER B 45  ? 1.1619 0.4643 0.5027 0.1319  -0.1085 -0.0582 45  SER B CB  
3971 O OG  . SER B 45  ? 1.2273 0.4860 0.5261 0.1642  -0.1230 -0.0685 45  SER B OG  
3972 N N   . ALA B 46  ? 1.0978 0.5418 0.5429 0.1557  -0.1243 -0.0712 46  ALA B N   
3973 C CA  . ALA B 46  ? 1.0622 0.5732 0.5578 0.1764  -0.1375 -0.0859 46  ALA B CA  
3974 C C   . ALA B 46  ? 1.0687 0.5665 0.5438 0.1976  -0.1518 -0.0880 46  ALA B C   
3975 O O   . ALA B 46  ? 1.0583 0.5701 0.5357 0.2322  -0.1722 -0.1038 46  ALA B O   
3976 C CB  . ALA B 46  ? 0.9951 0.5809 0.5619 0.1488  -0.1248 -0.0847 46  ALA B CB  
3977 N N   . ALA B 47  ? 1.0695 0.5378 0.5203 0.1797  -0.1423 -0.0734 47  ALA B N   
3978 C CA  . ALA B 47  ? 1.1213 0.5713 0.5449 0.2017  -0.1562 -0.0753 47  ALA B CA  
3979 C C   . ALA B 47  ? 1.1746 0.5570 0.5281 0.2398  -0.1738 -0.0805 47  ALA B C   
3980 O O   . ALA B 47  ? 1.1462 0.5376 0.4950 0.2744  -0.1966 -0.0943 47  ALA B O   
3981 C CB  . ALA B 47  ? 1.0673 0.4910 0.4691 0.1767  -0.1398 -0.0577 47  ALA B CB  
3982 N N   . ASP B 48  ? 1.2917 0.6047 0.5895 0.2350  -0.1648 -0.0708 48  ASP B N   
3983 C CA  . ASP B 48  ? 1.3791 0.6140 0.5994 0.2710  -0.1801 -0.0736 48  ASP B CA  
3984 C C   . ASP B 48  ? 1.3445 0.6121 0.5842 0.3117  -0.2050 -0.0963 48  ASP B C   
3985 O O   . ASP B 48  ? 1.4165 0.6341 0.5995 0.3523  -0.2254 -0.1037 48  ASP B O   
3986 C CB  . ASP B 48  ? 1.4109 0.5690 0.5759 0.2526  -0.1639 -0.0601 48  ASP B CB  
3987 C CG  . ASP B 48  ? 1.4460 0.5509 0.5700 0.2212  -0.1416 -0.0385 48  ASP B CG  
3988 O OD1 . ASP B 48  ? 1.4093 0.5337 0.5420 0.2175  -0.1392 -0.0336 48  ASP B OD1 
3989 O OD2 . ASP B 48  ? 1.5648 0.6101 0.6494 0.1994  -0.1258 -0.0274 48  ASP B OD2 
3990 N N   . GLN B 49  ? 1.2571 0.6051 0.5725 0.3028  -0.2030 -0.1078 49  GLN B N   
3991 C CA  . GLN B 49  ? 1.2092 0.6025 0.5542 0.3403  -0.2244 -0.1313 49  GLN B CA  
3992 C C   . GLN B 49  ? 1.1903 0.6669 0.6023 0.3483  -0.2368 -0.1461 49  GLN B C   
3993 O O   . GLN B 49  ? 1.1763 0.7166 0.6392 0.3682  -0.2487 -0.1666 49  GLN B O   
3994 C CB  . GLN B 49  ? 1.2192 0.6432 0.5981 0.3301  -0.2141 -0.1365 49  GLN B CB  
3995 C CG  . GLN B 49  ? 1.2289 0.5719 0.5464 0.3149  -0.2011 -0.1218 49  GLN B CG  
3996 C CD  . GLN B 49  ? 1.2063 0.5750 0.5518 0.3052  -0.1920 -0.1273 49  GLN B CD  
3997 O OE1 . GLN B 49  ? 1.2194 0.5979 0.5647 0.3378  -0.2049 -0.1439 49  GLN B OE1 
3998 N NE2 . GLN B 49  ? 1.1746 0.5553 0.5435 0.2626  -0.1703 -0.1146 49  GLN B NE2 
3999 N N   . GLY B 50  ? 1.1309 0.6081 0.5439 0.3332  -0.2340 -0.1371 50  GLY B N   
4000 C CA  . GLY B 50  ? 1.0977 0.6444 0.5677 0.3406  -0.2478 -0.1518 50  GLY B CA  
4001 C C   . GLY B 50  ? 1.0668 0.6993 0.6252 0.3070  -0.2328 -0.1540 50  GLY B C   
4002 O O   . GLY B 50  ? 1.0193 0.7183 0.6353 0.3145  -0.2450 -0.1712 50  GLY B O   
4003 N N   . ALA B 51  ? 1.0885 0.7208 0.6588 0.2704  -0.2073 -0.1381 51  ALA B N   
4004 C CA  . ALA B 51  ? 1.0244 0.7294 0.6696 0.2396  -0.1927 -0.1381 51  ALA B CA  
4005 C C   . ALA B 51  ? 1.0117 0.7353 0.6767 0.2251  -0.1933 -0.1344 51  ALA B C   
4006 O O   . ALA B 51  ? 1.0358 0.7084 0.6527 0.2220  -0.1918 -0.1218 51  ALA B O   
4007 C CB  . ALA B 51  ? 1.0236 0.7175 0.6685 0.2068  -0.1679 -0.1218 51  ALA B CB  
4008 N N   . HIS B 52  ? 0.8245 0.6200 0.5596 0.2150  -0.1937 -0.1453 52  HIS B N   
4009 C CA  . HIS B 52  ? 0.7619 0.5774 0.5207 0.1988  -0.1936 -0.1429 52  HIS B CA  
4010 C C   . HIS B 52  ? 0.7362 0.5629 0.5167 0.1596  -0.1686 -0.1255 52  HIS B C   
4011 O O   . HIS B 52  ? 0.7094 0.5253 0.4831 0.1458  -0.1645 -0.1166 52  HIS B O   
4012 C CB  . HIS B 52  ? 0.7336 0.6176 0.5565 0.2074  -0.2086 -0.1654 52  HIS B CB  
4013 C CG  . HIS B 52  ? 0.7775 0.6577 0.5840 0.2481  -0.2380 -0.1858 52  HIS B CG  
4014 N ND1 . HIS B 52  ? 0.7966 0.6912 0.6076 0.2751  -0.2484 -0.2008 52  HIS B ND1 
4015 C CD2 . HIS B 52  ? 0.8100 0.6730 0.5929 0.2695  -0.2607 -0.1947 52  HIS B CD2 
4016 C CE1 . HIS B 52  ? 0.8385 0.7264 0.6311 0.3119  -0.2772 -0.2186 52  HIS B CE1 
4017 N NE2 . HIS B 52  ? 0.8479 0.7160 0.6223 0.3091  -0.2855 -0.2151 52  HIS B NE2 
4018 N N   . ILE B 53  ? 0.8540 0.7015 0.6581 0.1439  -0.1526 -0.1215 53  ILE B N   
4019 C CA  . ILE B 53  ? 0.7820 0.6432 0.6076 0.1101  -0.1310 -0.1069 53  ILE B CA  
4020 C C   . ILE B 53  ? 0.7844 0.6343 0.5989 0.1024  -0.1175 -0.1002 53  ILE B C   
4021 O O   . ILE B 53  ? 0.7920 0.6523 0.6108 0.1189  -0.1219 -0.1107 53  ILE B O   
4022 C CB  . ILE B 53  ? 0.7154 0.6379 0.6054 0.0955  -0.1279 -0.1142 53  ILE B CB  
4023 C CG1 . ILE B 53  ? 0.7375 0.6691 0.6435 0.0642  -0.1070 -0.0989 53  ILE B CG1 
4024 C CG2 . ILE B 53  ? 0.6880 0.6601 0.6219 0.1068  -0.1320 -0.1317 53  ILE B CG2 
4025 C CD1 . ILE B 53  ? 0.6671 0.6366 0.6182 0.0492  -0.1051 -0.1021 53  ILE B CD1 
4026 N N   . ILE B 54  ? 0.7419 0.5696 0.5401 0.0791  -0.1022 -0.0841 54  ILE B N   
4027 C CA  . ILE B 54  ? 0.7190 0.5351 0.5065 0.0688  -0.0902 -0.0781 54  ILE B CA  
4028 C C   . ILE B 54  ? 0.7294 0.5724 0.5462 0.0407  -0.0743 -0.0682 54  ILE B C   
4029 O O   . ILE B 54  ? 0.7177 0.5595 0.5371 0.0273  -0.0706 -0.0601 54  ILE B O   
4030 C CB  . ILE B 54  ? 0.7429 0.4944 0.4714 0.0703  -0.0896 -0.0698 54  ILE B CB  
4031 C CG1 . ILE B 54  ? 0.7628 0.5044 0.4835 0.0598  -0.0799 -0.0669 54  ILE B CG1 
4032 C CG2 . ILE B 54  ? 0.7579 0.4852 0.4678 0.0529  -0.0823 -0.0565 54  ILE B CG2 
4033 C CD1 . ILE B 54  ? 0.8303 0.5067 0.4951 0.0585  -0.0789 -0.0606 54  ILE B CD1 
4034 N N   . VAL B 55  ? 0.6720 0.5396 0.5092 0.0345  -0.0655 -0.0697 55  VAL B N   
4035 C CA  . VAL B 55  ? 0.6125 0.5014 0.4707 0.0117  -0.0515 -0.0608 55  VAL B CA  
4036 C C   . VAL B 55  ? 0.6612 0.5207 0.4904 0.0023  -0.0453 -0.0543 55  VAL B C   
4037 O O   . VAL B 55  ? 0.6662 0.5060 0.4738 0.0135  -0.0483 -0.0598 55  VAL B O   
4038 C CB  . VAL B 55  ? 0.6094 0.5450 0.5078 0.0111  -0.0446 -0.0670 55  VAL B CB  
4039 C CG1 . VAL B 55  ? 0.5801 0.5311 0.4935 -0.0102 -0.0313 -0.0566 55  VAL B CG1 
4040 C CG2 . VAL B 55  ? 0.5522 0.5201 0.4839 0.0210  -0.0521 -0.0781 55  VAL B CG2 
4041 N N   . THR B 56  ? 0.7130 0.5707 0.5427 -0.0174 -0.0376 -0.0442 56  THR B N   
4042 C CA  . THR B 56  ? 0.7256 0.5662 0.5379 -0.0292 -0.0323 -0.0403 56  THR B CA  
4043 C C   . THR B 56  ? 0.7144 0.5872 0.5511 -0.0412 -0.0239 -0.0368 56  THR B C   
4044 O O   . THR B 56  ? 0.7241 0.6251 0.5871 -0.0439 -0.0206 -0.0343 56  THR B O   
4045 C CB  . THR B 56  ? 0.7265 0.5344 0.5144 -0.0414 -0.0310 -0.0333 56  THR B CB  
4046 O OG1 . THR B 56  ? 0.7152 0.5422 0.5216 -0.0513 -0.0270 -0.0269 56  THR B OG1 
4047 C CG2 . THR B 56  ? 0.7276 0.4951 0.4820 -0.0279 -0.0381 -0.0355 56  THR B CG2 
4048 N N   . PRO B 57  ? 0.6275 0.4936 0.4529 -0.0472 -0.0213 -0.0371 57  PRO B N   
4049 C CA  . PRO B 57  ? 0.6625 0.5554 0.5030 -0.0510 -0.0149 -0.0359 57  PRO B CA  
4050 C C   . PRO B 57  ? 0.6338 0.5422 0.4880 -0.0647 -0.0111 -0.0279 57  PRO B C   
4051 O O   . PRO B 57  ? 0.5713 0.4719 0.4241 -0.0734 -0.0127 -0.0240 57  PRO B O   
4052 C CB  . PRO B 57  ? 0.6491 0.5232 0.4661 -0.0502 -0.0168 -0.0409 57  PRO B CB  
4053 C CG  . PRO B 57  ? 0.6822 0.5179 0.4727 -0.0459 -0.0237 -0.0451 57  PRO B CG  
4054 C CD  . PRO B 57  ? 0.6764 0.5059 0.4709 -0.0504 -0.0247 -0.0395 57  PRO B CD  
4055 N N   . GLU B 58  ? 0.7177 0.6469 0.5824 -0.0651 -0.0053 -0.0255 58  GLU B N   
4056 C CA  . GLU B 58  ? 0.6927 0.6329 0.5641 -0.0742 -0.0034 -0.0189 58  GLU B CA  
4057 C C   . GLU B 58  ? 0.7022 0.6326 0.5595 -0.0816 -0.0085 -0.0210 58  GLU B C   
4058 O O   . GLU B 58  ? 0.7081 0.6274 0.5493 -0.0792 -0.0111 -0.0268 58  GLU B O   
4059 C CB  . GLU B 58  ? 0.6733 0.6299 0.5511 -0.0714 0.0045  -0.0151 58  GLU B CB  
4060 C CG  . GLU B 58  ? 0.7104 0.6721 0.5851 -0.0760 0.0043  -0.0092 58  GLU B CG  
4061 C CD  . GLU B 58  ? 0.7479 0.7153 0.6166 -0.0718 0.0131  -0.0044 58  GLU B CD  
4062 O OE1 . GLU B 58  ? 0.7222 0.6915 0.5902 -0.0731 0.0145  0.0024  58  GLU B OE1 
4063 O OE2 . GLU B 58  ? 0.7533 0.7216 0.6160 -0.0661 0.0197  -0.0073 58  GLU B OE2 
4064 N N   . ASP B 59  ? 0.6683 0.6049 0.5332 -0.0904 -0.0102 -0.0176 59  ASP B N   
4065 C CA  . ASP B 59  ? 0.6548 0.5903 0.5151 -0.1000 -0.0150 -0.0215 59  ASP B CA  
4066 C C   . ASP B 59  ? 0.7059 0.6164 0.5527 -0.1073 -0.0172 -0.0268 59  ASP B C   
4067 O O   . ASP B 59  ? 0.6948 0.6011 0.5368 -0.1170 -0.0212 -0.0327 59  ASP B O   
4068 C CB  . ASP B 59  ? 0.7195 0.6620 0.5713 -0.0961 -0.0187 -0.0252 59  ASP B CB  
4069 C CG  . ASP B 59  ? 0.7057 0.6666 0.5639 -0.0903 -0.0171 -0.0193 59  ASP B CG  
4070 O OD1 . ASP B 59  ? 0.6572 0.6289 0.5293 -0.0928 -0.0162 -0.0146 59  ASP B OD1 
4071 O OD2 . ASP B 59  ? 0.7432 0.7042 0.5882 -0.0820 -0.0163 -0.0191 59  ASP B OD2 
4072 N N   . ALA B 60  ? 0.7033 0.5946 0.5422 -0.1027 -0.0154 -0.0255 60  ALA B N   
4073 C CA  . ALA B 60  ? 0.7181 0.5755 0.5349 -0.1067 -0.0174 -0.0298 60  ALA B CA  
4074 C C   . ALA B 60  ? 0.7253 0.5741 0.5415 -0.1251 -0.0148 -0.0292 60  ALA B C   
4075 O O   . ALA B 60  ? 0.7086 0.5284 0.5063 -0.1343 -0.0157 -0.0335 60  ALA B O   
4076 C CB  . ALA B 60  ? 0.7070 0.5447 0.5124 -0.0942 -0.0175 -0.0286 60  ALA B CB  
4077 N N   . ILE B 61  ? 0.7597 0.6327 0.5957 -0.1313 -0.0108 -0.0245 61  ILE B N   
4078 C CA  . ILE B 61  ? 0.7812 0.6494 0.6188 -0.1481 -0.0048 -0.0235 61  ILE B CA  
4079 C C   . ILE B 61  ? 0.7527 0.6510 0.6120 -0.1615 -0.0062 -0.0292 61  ILE B C   
4080 O O   . ILE B 61  ? 0.7366 0.6288 0.5973 -0.1800 -0.0020 -0.0331 61  ILE B O   
4081 C CB  . ILE B 61  ? 0.7349 0.6068 0.5764 -0.1441 0.0016  -0.0158 61  ILE B CB  
4082 C CG1 . ILE B 61  ? 0.7132 0.5517 0.5301 -0.1312 0.0004  -0.0130 61  ILE B CG1 
4083 C CG2 . ILE B 61  ? 0.7170 0.5887 0.5612 -0.1611 0.0113  -0.0143 61  ILE B CG2 
4084 C CD1 . ILE B 61  ? 0.7073 0.5600 0.5339 -0.1162 -0.0017 -0.0095 61  ILE B CD1 
4085 N N   . TYR B 62  ? 0.7507 0.6791 0.6252 -0.1528 -0.0124 -0.0311 62  TYR B N   
4086 C CA  . TYR B 62  ? 0.7513 0.7100 0.6456 -0.1618 -0.0169 -0.0384 62  TYR B CA  
4087 C C   . TYR B 62  ? 0.7597 0.7279 0.6508 -0.1539 -0.0282 -0.0455 62  TYR B C   
4088 O O   . TYR B 62  ? 0.7327 0.7257 0.6387 -0.1597 -0.0352 -0.0542 62  TYR B O   
4089 C CB  . TYR B 62  ? 0.7275 0.7192 0.6441 -0.1581 -0.0137 -0.0345 62  TYR B CB  
4090 C CG  . TYR B 62  ? 0.7412 0.7373 0.6559 -0.1395 -0.0143 -0.0262 62  TYR B CG  
4091 C CD1 . TYR B 62  ? 0.7315 0.7240 0.6361 -0.1271 -0.0198 -0.0254 62  TYR B CD1 
4092 C CD2 . TYR B 62  ? 0.7372 0.7410 0.6599 -0.1352 -0.0086 -0.0199 62  TYR B CD2 
4093 C CE1 . TYR B 62  ? 0.7373 0.7320 0.6412 -0.1140 -0.0182 -0.0180 62  TYR B CE1 
4094 C CE2 . TYR B 62  ? 0.6932 0.6981 0.6146 -0.1207 -0.0096 -0.0135 62  TYR B CE2 
4095 C CZ  . TYR B 62  ? 0.7359 0.7359 0.6489 -0.1117 -0.0138 -0.0124 62  TYR B CZ  
4096 O OH  . TYR B 62  ? 0.7655 0.7641 0.6775 -0.1010 -0.0126 -0.0060 62  TYR B OH  
4097 N N   . GLY B 63  ? 0.7070 0.6573 0.5787 -0.1406 -0.0302 -0.0434 63  GLY B N   
4098 C CA  . GLY B 63  ? 0.7245 0.6785 0.5861 -0.1326 -0.0393 -0.0502 63  GLY B CA  
4099 C C   . GLY B 63  ? 0.7030 0.6784 0.5676 -0.1174 -0.0410 -0.0452 63  GLY B C   
4100 O O   . GLY B 63  ? 0.7292 0.7137 0.6031 -0.1122 -0.0350 -0.0361 63  GLY B O   
4101 N N   . TRP B 64  ? 0.7023 0.6813 0.5546 -0.1095 -0.0498 -0.0515 64  TRP B N   
4102 C CA  . TRP B 64  ? 0.7262 0.7148 0.5699 -0.0931 -0.0505 -0.0456 64  TRP B CA  
4103 C C   . TRP B 64  ? 0.7617 0.7691 0.6042 -0.0874 -0.0645 -0.0543 64  TRP B C   
4104 O O   . TRP B 64  ? 0.7575 0.7656 0.5835 -0.0714 -0.0663 -0.0496 64  TRP B O   
4105 C CB  . TRP B 64  ? 0.7249 0.6936 0.5437 -0.0815 -0.0444 -0.0418 64  TRP B CB  
4106 C CG  . TRP B 64  ? 0.7525 0.7051 0.5540 -0.0827 -0.0508 -0.0528 64  TRP B CG  
4107 C CD1 . TRP B 64  ? 0.7325 0.6849 0.5171 -0.0771 -0.0628 -0.0629 64  TRP B CD1 
4108 C CD2 . TRP B 64  ? 0.7480 0.6785 0.5435 -0.0880 -0.0474 -0.0560 64  TRP B CD2 
4109 N NE1 . TRP B 64  ? 0.7615 0.6924 0.5307 -0.0800 -0.0666 -0.0725 64  TRP B NE1 
4110 C CE2 . TRP B 64  ? 0.7737 0.6896 0.5483 -0.0862 -0.0569 -0.0681 64  TRP B CE2 
4111 C CE3 . TRP B 64  ? 0.7503 0.6695 0.5528 -0.0918 -0.0387 -0.0507 64  TRP B CE3 
4112 C CZ2 . TRP B 64  ? 0.7842 0.6721 0.5440 -0.0884 -0.0573 -0.0744 64  TRP B CZ2 
4113 C CZ3 . TRP B 64  ? 0.7635 0.6559 0.5505 -0.0924 -0.0397 -0.0568 64  TRP B CZ3 
4114 C CH2 . TRP B 64  ? 0.8190 0.6948 0.5845 -0.0909 -0.0484 -0.0682 64  TRP B CH2 
4115 N N   . ASN B 65  ? 0.8028 0.8242 0.6608 -0.0997 -0.0746 -0.0674 65  ASN B N   
4116 C CA  . ASN B 65  ? 0.8223 0.8668 0.6834 -0.0935 -0.0913 -0.0795 65  ASN B CA  
4117 C C   . ASN B 65  ? 0.8159 0.8944 0.7078 -0.0955 -0.0928 -0.0799 65  ASN B C   
4118 O O   . ASN B 65  ? 0.8045 0.9044 0.7258 -0.1127 -0.0944 -0.0894 65  ASN B O   
4119 C CB  . ASN B 65  ? 0.8507 0.8931 0.7133 -0.1064 -0.1028 -0.0967 65  ASN B CB  
4120 C CG  . ASN B 65  ? 0.8791 0.8879 0.7061 -0.0986 -0.1034 -0.0979 65  ASN B CG  
4121 O OD1 . ASN B 65  ? 0.9359 0.9221 0.7580 -0.1110 -0.1006 -0.1022 65  ASN B OD1 
4122 N ND2 . ASN B 65  ? 0.9469 0.9494 0.7453 -0.0766 -0.1062 -0.0937 65  ASN B ND2 
4123 N N   . PHE B 66  ? 0.6856 0.7677 0.5694 -0.0777 -0.0913 -0.0699 66  PHE B N   
4124 C CA  . PHE B 66  ? 0.6939 0.8040 0.6025 -0.0753 -0.0915 -0.0690 66  PHE B CA  
4125 C C   . PHE B 66  ? 0.6963 0.8119 0.5878 -0.0501 -0.1017 -0.0669 66  PHE B C   
4126 O O   . PHE B 66  ? 0.7738 0.8611 0.6308 -0.0360 -0.0990 -0.0569 66  PHE B O   
4127 C CB  . PHE B 66  ? 0.6496 0.7477 0.5652 -0.0815 -0.0741 -0.0549 66  PHE B CB  
4128 C CG  . PHE B 66  ? 0.6937 0.7906 0.6280 -0.1040 -0.0648 -0.0571 66  PHE B CG  
4129 C CD1 . PHE B 66  ? 0.6667 0.7933 0.6312 -0.1182 -0.0662 -0.0677 66  PHE B CD1 
4130 C CD2 . PHE B 66  ? 0.7045 0.7700 0.6251 -0.1102 -0.0537 -0.0486 66  PHE B CD2 
4131 C CE1 . PHE B 66  ? 0.6583 0.7766 0.6335 -0.1396 -0.0548 -0.0676 66  PHE B CE1 
4132 C CE2 . PHE B 66  ? 0.6514 0.7082 0.5812 -0.1283 -0.0454 -0.0496 66  PHE B CE2 
4133 C CZ  . PHE B 66  ? 0.6139 0.6937 0.5682 -0.1436 -0.0451 -0.0580 66  PHE B CZ  
4134 N N   . ASN B 67  ? 0.6383 0.7895 0.5528 -0.0441 -0.1123 -0.0765 67  ASN B N   
4135 C CA  . ASN B 67  ? 0.6690 0.8226 0.5714 -0.0203 -0.1173 -0.0707 67  ASN B CA  
4136 C C   . ASN B 67  ? 0.7016 0.8641 0.6267 -0.0258 -0.1045 -0.0633 67  ASN B C   
4137 O O   . ASN B 67  ? 0.6631 0.8294 0.6102 -0.0470 -0.0922 -0.0623 67  ASN B O   
4138 C CB  . ASN B 67  ? 0.6490 0.8363 0.5579 -0.0034 -0.1403 -0.0879 67  ASN B CB  
4139 C CG  . ASN B 67  ? 0.6625 0.9016 0.6230 -0.0204 -0.1460 -0.1068 67  ASN B CG  
4140 O OD1 . ASN B 67  ? 0.6453 0.9113 0.6355 -0.0233 -0.1397 -0.1076 67  ASN B OD1 
4141 N ND2 . ASN B 67  ? 0.6295 0.8831 0.6003 -0.0314 -0.1578 -0.1233 67  ASN B ND2 
4142 N N   . ARG B 68  ? 0.7058 0.8659 0.6199 -0.0051 -0.1075 -0.0575 68  ARG B N   
4143 C CA  . ARG B 68  ? 0.7100 0.8732 0.6397 -0.0075 -0.0960 -0.0505 68  ARG B CA  
4144 C C   . ARG B 68  ? 0.6977 0.9059 0.6720 -0.0224 -0.0941 -0.0632 68  ARG B C   
4145 O O   . ARG B 68  ? 0.6775 0.8830 0.6664 -0.0393 -0.0790 -0.0582 68  ARG B O   
4146 C CB  . ARG B 68  ? 0.7280 0.8819 0.6372 0.0197  -0.1029 -0.0456 68  ARG B CB  
4147 C CG  . ARG B 68  ? 0.7392 0.8405 0.6029 0.0299  -0.0977 -0.0289 68  ARG B CG  
4148 C CD  . ARG B 68  ? 0.7611 0.8448 0.6019 0.0547  -0.1026 -0.0230 68  ARG B CD  
4149 N NE  . ARG B 68  ? 0.7219 0.8121 0.5825 0.0520  -0.0949 -0.0209 68  ARG B NE  
4150 C CZ  . ARG B 68  ? 0.7351 0.7970 0.5922 0.0398  -0.0799 -0.0091 68  ARG B CZ  
4151 N NH1 . ARG B 68  ? 0.7553 0.7855 0.5962 0.0269  -0.0693 0.0013  68  ARG B NH1 
4152 N NH2 . ARG B 68  ? 0.7419 0.8093 0.6124 0.0420  -0.0761 -0.0092 68  ARG B NH2 
4153 N N   . ASP B 69  ? 0.6873 0.9378 0.6834 -0.0165 -0.1091 -0.0804 69  ASP B N   
4154 C CA  . ASP B 69  ? 0.6986 0.9975 0.7407 -0.0302 -0.1051 -0.0932 69  ASP B CA  
4155 C C   . ASP B 69  ? 0.6753 0.9753 0.7362 -0.0632 -0.0940 -0.0966 69  ASP B C   
4156 O O   . ASP B 69  ? 0.7016 1.0123 0.7845 -0.0807 -0.0781 -0.0953 69  ASP B O   
4157 C CB  . ASP B 69  ? 0.6635 1.0130 0.7285 -0.0139 -0.1252 -0.1130 69  ASP B CB  
4158 C CG  . ASP B 69  ? 0.7297 1.0740 0.7723 0.0216  -0.1361 -0.1095 69  ASP B CG  
4159 O OD1 . ASP B 69  ? 0.7014 1.0379 0.7430 0.0273  -0.1246 -0.1002 69  ASP B OD1 
4160 O OD2 . ASP B 69  ? 0.7475 1.0920 0.7700 0.0448  -0.1565 -0.1163 69  ASP B OD2 
4161 N N   . SER B 70  ? 0.6856 0.9689 0.7327 -0.0707 -0.1014 -0.1003 70  SER B N   
4162 C CA  . SER B 70  ? 0.6985 0.9739 0.7569 -0.1007 -0.0921 -0.1036 70  SER B CA  
4163 C C   . SER B 70  ? 0.7175 0.9506 0.7571 -0.1111 -0.0727 -0.0858 70  SER B C   
4164 O O   . SER B 70  ? 0.7425 0.9685 0.7921 -0.1347 -0.0607 -0.0862 70  SER B O   
4165 C CB  . SER B 70  ? 0.7357 0.9974 0.7774 -0.1023 -0.1063 -0.1121 70  SER B CB  
4166 O OG  . SER B 70  ? 0.7364 0.9519 0.7348 -0.0888 -0.1050 -0.0978 70  SER B OG  
4167 N N   . LEU B 71  ? 0.6324 0.8354 0.6438 -0.0938 -0.0698 -0.0710 71  LEU B N   
4168 C CA  . LEU B 71  ? 0.6362 0.8053 0.6343 -0.1012 -0.0538 -0.0566 71  LEU B CA  
4169 C C   . LEU B 71  ? 0.6407 0.8240 0.6559 -0.1034 -0.0425 -0.0533 71  LEU B C   
4170 O O   . LEU B 71  ? 0.6293 0.7939 0.6418 -0.1164 -0.0292 -0.0468 71  LEU B O   
4171 C CB  . LEU B 71  ? 0.6627 0.7975 0.6290 -0.0851 -0.0541 -0.0438 71  LEU B CB  
4172 C CG  . LEU B 71  ? 0.6812 0.7880 0.6384 -0.0884 -0.0405 -0.0309 71  LEU B CG  
4173 C CD1 . LEU B 71  ? 0.6598 0.7426 0.6087 -0.1031 -0.0342 -0.0294 71  LEU B CD1 
4174 C CD2 . LEU B 71  ? 0.6443 0.7292 0.5807 -0.0722 -0.0401 -0.0200 71  LEU B CD2 
4175 N N   . TYR B 72  ? 0.6052 0.8202 0.6353 -0.0888 -0.0481 -0.0584 72  TYR B N   
4176 C CA  . TYR B 72  ? 0.5914 0.8160 0.6315 -0.0855 -0.0374 -0.0545 72  TYR B CA  
4177 C C   . TYR B 72  ? 0.6185 0.8482 0.6741 -0.1087 -0.0208 -0.0552 72  TYR B C   
4178 O O   . TYR B 72  ? 0.6146 0.8232 0.6587 -0.1084 -0.0092 -0.0456 72  TYR B O   
4179 C CB  . TYR B 72  ? 0.5796 0.8462 0.6388 -0.0671 -0.0465 -0.0645 72  TYR B CB  
4180 C CG  . TYR B 72  ? 0.5707 0.8438 0.6351 -0.0595 -0.0357 -0.0606 72  TYR B CG  
4181 C CD1 . TYR B 72  ? 0.5925 0.8293 0.6292 -0.0440 -0.0349 -0.0483 72  TYR B CD1 
4182 C CD2 . TYR B 72  ? 0.5370 0.8508 0.6330 -0.0689 -0.0254 -0.0696 72  TYR B CD2 
4183 C CE1 . TYR B 72  ? 0.6015 0.8403 0.6391 -0.0357 -0.0268 -0.0460 72  TYR B CE1 
4184 C CE2 . TYR B 72  ? 0.5817 0.8993 0.6780 -0.0598 -0.0146 -0.0662 72  TYR B CE2 
4185 C CZ  . TYR B 72  ? 0.5650 0.8433 0.6303 -0.0421 -0.0167 -0.0546 72  TYR B CZ  
4186 O OH  . TYR B 72  ? 0.5968 0.8742 0.6580 -0.0313 -0.0082 -0.0522 72  TYR B OH  
4187 N N   . PRO B 73  ? 0.6475 0.9020 0.7268 -0.1289 -0.0183 -0.0663 73  PRO B N   
4188 C CA  . PRO B 73  ? 0.6117 0.8646 0.7002 -0.1518 0.0009  -0.0651 73  PRO B CA  
4189 C C   . PRO B 73  ? 0.6460 0.8443 0.7021 -0.1606 0.0104  -0.0519 73  PRO B C   
4190 O O   . PRO B 73  ? 0.6373 0.8241 0.6899 -0.1738 0.0269  -0.0475 73  PRO B O   
4191 C CB  . PRO B 73  ? 0.6128 0.8973 0.7311 -0.1740 -0.0006 -0.0805 73  PRO B CB  
4192 C CG  . PRO B 73  ? 0.6136 0.9029 0.7287 -0.1625 -0.0227 -0.0882 73  PRO B CG  
4193 C CD  . PRO B 73  ? 0.5978 0.8860 0.6981 -0.1314 -0.0328 -0.0821 73  PRO B CD  
4194 N N   . TYR B 74  ? 0.6271 0.7920 0.6586 -0.1532 0.0009  -0.0462 74  TYR B N   
4195 C CA  . TYR B 74  ? 0.6250 0.7425 0.6280 -0.1576 0.0075  -0.0358 74  TYR B CA  
4196 C C   . TYR B 74  ? 0.6224 0.7205 0.6087 -0.1409 0.0097  -0.0251 74  TYR B C   
4197 O O   . TYR B 74  ? 0.6340 0.6970 0.5989 -0.1420 0.0140  -0.0181 74  TYR B O   
4198 C CB  . TYR B 74  ? 0.6081 0.7023 0.5947 -0.1571 -0.0027 -0.0366 74  TYR B CB  
4199 C CG  . TYR B 74  ? 0.6564 0.7597 0.6532 -0.1737 -0.0073 -0.0482 74  TYR B CG  
4200 C CD1 . TYR B 74  ? 0.6299 0.7734 0.6506 -0.1722 -0.0181 -0.0604 74  TYR B CD1 
4201 C CD2 . TYR B 74  ? 0.6252 0.6946 0.6056 -0.1893 -0.0030 -0.0482 74  TYR B CD2 
4202 C CE1 . TYR B 74  ? 0.6009 0.7536 0.6326 -0.1882 -0.0244 -0.0733 74  TYR B CE1 
4203 C CE2 . TYR B 74  ? 0.6209 0.6942 0.6090 -0.2058 -0.0081 -0.0600 74  TYR B CE2 
4204 C CZ  . TYR B 74  ? 0.5959 0.7122 0.6114 -0.2062 -0.0189 -0.0730 74  TYR B CZ  
4205 O OH  . TYR B 74  ? 0.6325 0.7536 0.6574 -0.2234 -0.0261 -0.0870 74  TYR B OH  
4206 N N   . LEU B 75  ? 0.5015 0.6196 0.4958 -0.1244 0.0051  -0.0250 75  LEU B N   
4207 C CA  . LEU B 75  ? 0.4932 0.5902 0.4715 -0.1091 0.0043  -0.0165 75  LEU B CA  
4208 C C   . LEU B 75  ? 0.5168 0.6096 0.4919 -0.1093 0.0155  -0.0135 75  LEU B C   
4209 O O   . LEU B 75  ? 0.4933 0.6102 0.4828 -0.1164 0.0245  -0.0181 75  LEU B O   
4210 C CB  . LEU B 75  ? 0.5042 0.6148 0.4853 -0.0906 -0.0060 -0.0172 75  LEU B CB  
4211 C CG  . LEU B 75  ? 0.5131 0.6247 0.4900 -0.0860 -0.0173 -0.0193 75  LEU B CG  
4212 C CD1 . LEU B 75  ? 0.5137 0.6257 0.4825 -0.0654 -0.0257 -0.0170 75  LEU B CD1 
4213 C CD2 . LEU B 75  ? 0.4819 0.5620 0.4416 -0.0919 -0.0165 -0.0139 75  LEU B CD2 
4214 N N   . GLU B 76  ? 0.6364 0.6993 0.5926 -0.1016 0.0154  -0.0067 76  GLU B N   
4215 C CA  . GLU B 76  ? 0.6913 0.7446 0.6376 -0.0964 0.0229  -0.0040 76  GLU B CA  
4216 C C   . GLU B 76  ? 0.6982 0.7397 0.6369 -0.0792 0.0147  -0.0015 76  GLU B C   
4217 O O   . GLU B 76  ? 0.6840 0.7119 0.6192 -0.0759 0.0065  0.0008  76  GLU B O   
4218 C CB  . GLU B 76  ? 0.6727 0.6941 0.5982 -0.1050 0.0295  0.0000  76  GLU B CB  
4219 C CG  . GLU B 76  ? 0.7354 0.7631 0.6620 -0.1211 0.0440  -0.0012 76  GLU B CG  
4220 C CD  . GLU B 76  ? 0.7573 0.7453 0.6564 -0.1298 0.0500  0.0034  76  GLU B CD  
4221 O OE1 . GLU B 76  ? 0.7566 0.7146 0.6334 -0.1184 0.0444  0.0071  76  GLU B OE1 
4222 O OE2 . GLU B 76  ? 0.7771 0.7629 0.6762 -0.1478 0.0600  0.0025  76  GLU B OE2 
4223 N N   . ASP B 77  ? 0.6117 0.6565 0.5467 -0.0692 0.0183  -0.0022 77  ASP B N   
4224 C CA  . ASP B 77  ? 0.5911 0.6200 0.5168 -0.0537 0.0103  -0.0011 77  ASP B CA  
4225 C C   . ASP B 77  ? 0.6428 0.6392 0.5508 -0.0541 0.0084  0.0014  77  ASP B C   
4226 O O   . ASP B 77  ? 0.6738 0.6599 0.5676 -0.0523 0.0145  0.0012  77  ASP B O   
4227 C CB  . ASP B 77  ? 0.5983 0.6435 0.5254 -0.0404 0.0133  -0.0048 77  ASP B CB  
4228 C CG  . ASP B 77  ? 0.6609 0.6880 0.5778 -0.0237 0.0033  -0.0049 77  ASP B CG  
4229 O OD1 . ASP B 77  ? 0.6488 0.6479 0.5566 -0.0250 -0.0037 -0.0021 77  ASP B OD1 
4230 O OD2 . ASP B 77  ? 0.6037 0.6449 0.5220 -0.0092 0.0027  -0.0089 77  ASP B OD2 
4231 N N   . ILE B 78  ? 0.7279 0.7093 0.6362 -0.0560 0.0005  0.0029  78  ILE B N   
4232 C CA  . ILE B 78  ? 0.7259 0.6830 0.6234 -0.0562 -0.0036 0.0027  78  ILE B CA  
4233 C C   . ILE B 78  ? 0.7458 0.6890 0.6395 -0.0458 -0.0117 0.0002  78  ILE B C   
4234 O O   . ILE B 78  ? 0.7274 0.6699 0.6295 -0.0450 -0.0164 0.0008  78  ILE B O   
4235 C CB  . ILE B 78  ? 0.7032 0.6573 0.6075 -0.0642 -0.0066 0.0036  78  ILE B CB  
4236 C CG1 . ILE B 78  ? 0.6821 0.6469 0.5886 -0.0746 -0.0003 0.0047  78  ILE B CG1 
4237 C CG2 . ILE B 78  ? 0.6904 0.6252 0.5869 -0.0618 -0.0123 0.0009  78  ILE B CG2 
4238 C CD1 . ILE B 78  ? 0.6538 0.6199 0.5669 -0.0800 -0.0032 0.0050  78  ILE B CD1 
4239 N N   . PRO B 79  ? 0.6949 0.6231 0.5730 -0.0380 -0.0136 -0.0029 79  PRO B N   
4240 C CA  . PRO B 79  ? 0.6874 0.6004 0.5613 -0.0283 -0.0232 -0.0075 79  PRO B CA  
4241 C C   . PRO B 79  ? 0.6762 0.5792 0.5608 -0.0333 -0.0328 -0.0108 79  PRO B C   
4242 O O   . PRO B 79  ? 0.6395 0.5467 0.5318 -0.0408 -0.0324 -0.0102 79  PRO B O   
4243 C CB  . PRO B 79  ? 0.6910 0.5906 0.5415 -0.0181 -0.0226 -0.0107 79  PRO B CB  
4244 C CG  . PRO B 79  ? 0.6699 0.5676 0.5113 -0.0246 -0.0158 -0.0076 79  PRO B CG  
4245 C CD  . PRO B 79  ? 0.7136 0.6335 0.5729 -0.0373 -0.0070 -0.0024 79  PRO B CD  
4246 N N   . ASP B 80  ? 0.7121 0.6025 0.5984 -0.0292 -0.0410 -0.0153 80  ASP B N   
4247 C CA  . ASP B 80  ? 0.7051 0.5881 0.6048 -0.0348 -0.0502 -0.0215 80  ASP B CA  
4248 C C   . ASP B 80  ? 0.6982 0.5739 0.5887 -0.0280 -0.0590 -0.0296 80  ASP B C   
4249 O O   . ASP B 80  ? 0.7361 0.5998 0.6040 -0.0160 -0.0615 -0.0321 80  ASP B O   
4250 C CB  . ASP B 80  ? 0.6870 0.5542 0.5892 -0.0342 -0.0566 -0.0253 80  ASP B CB  
4251 C CG  . ASP B 80  ? 0.7184 0.5832 0.6423 -0.0456 -0.0629 -0.0317 80  ASP B CG  
4252 O OD1 . ASP B 80  ? 0.7588 0.6228 0.6873 -0.0432 -0.0734 -0.0421 80  ASP B OD1 
4253 O OD2 . ASP B 80  ? 0.7970 0.6603 0.7329 -0.0566 -0.0573 -0.0272 80  ASP B OD2 
4254 N N   . PRO B 81  ? 0.6944 0.5766 0.5999 -0.0330 -0.0641 -0.0343 81  PRO B N   
4255 C CA  . PRO B 81  ? 0.6550 0.5290 0.5485 -0.0225 -0.0752 -0.0431 81  PRO B CA  
4256 C C   . PRO B 81  ? 0.6858 0.5438 0.5693 -0.0120 -0.0892 -0.0538 81  PRO B C   
4257 O O   . PRO B 81  ? 0.6874 0.5334 0.5500 0.0014  -0.0987 -0.0604 81  PRO B O   
4258 C CB  . PRO B 81  ? 0.6455 0.5353 0.5653 -0.0293 -0.0796 -0.0487 81  PRO B CB  
4259 C CG  . PRO B 81  ? 0.6074 0.5115 0.5409 -0.0424 -0.0650 -0.0381 81  PRO B CG  
4260 C CD  . PRO B 81  ? 0.6240 0.5224 0.5535 -0.0458 -0.0585 -0.0313 81  PRO B CD  
4261 N N   . GLU B 82  ? 0.6966 0.5496 0.5896 -0.0163 -0.0915 -0.0561 82  GLU B N   
4262 C CA  . GLU B 82  ? 0.7363 0.5706 0.6172 -0.0059 -0.1060 -0.0677 82  GLU B CA  
4263 C C   . GLU B 82  ? 0.7743 0.5920 0.6154 0.0119  -0.1042 -0.0656 82  GLU B C   
4264 O O   . GLU B 82  ? 0.8142 0.6141 0.6371 0.0249  -0.1176 -0.0762 82  GLU B O   
4265 C CB  . GLU B 82  ? 0.7295 0.5544 0.6226 -0.0143 -0.1071 -0.0693 82  GLU B CB  
4266 C CG  . GLU B 82  ? 0.7530 0.5701 0.6271 -0.0091 -0.0953 -0.0583 82  GLU B CG  
4267 C CD  . GLU B 82  ? 0.8167 0.6152 0.6940 -0.0135 -0.0979 -0.0599 82  GLU B CD  
4268 O OE1 . GLU B 82  ? 0.8540 0.6376 0.7391 -0.0173 -0.1112 -0.0721 82  GLU B OE1 
4269 O OE2 . GLU B 82  ? 0.8336 0.6307 0.7042 -0.0126 -0.0876 -0.0498 82  GLU B OE2 
4270 N N   . VAL B 83  ? 0.7693 0.5931 0.5968 0.0124  -0.0875 -0.0530 83  VAL B N   
4271 C CA  . VAL B 83  ? 0.7450 0.5561 0.5362 0.0270  -0.0813 -0.0503 83  VAL B CA  
4272 C C   . VAL B 83  ? 0.7825 0.5786 0.5466 0.0380  -0.0871 -0.0538 83  VAL B C   
4273 O O   . VAL B 83  ? 0.8349 0.6132 0.5623 0.0524  -0.0840 -0.0536 83  VAL B O   
4274 C CB  . VAL B 83  ? 0.7673 0.5942 0.5573 0.0214  -0.0605 -0.0373 83  VAL B CB  
4275 C CG1 . VAL B 83  ? 0.7478 0.5875 0.5589 0.0152  -0.0566 -0.0342 83  VAL B CG1 
4276 C CG2 . VAL B 83  ? 0.7232 0.5606 0.5206 0.0102  -0.0527 -0.0304 83  VAL B CG2 
4277 N N   . ASN B 84  ? 0.7762 0.5772 0.5538 0.0338  -0.0954 -0.0574 84  ASN B N   
4278 C CA  . ASN B 84  ? 0.8254 0.6083 0.5750 0.0480  -0.1054 -0.0627 84  ASN B CA  
4279 C C   . ASN B 84  ? 0.8822 0.6482 0.5917 0.0530  -0.0882 -0.0505 84  ASN B C   
4280 O O   . ASN B 84  ? 0.8691 0.6101 0.5367 0.0687  -0.0878 -0.0510 84  ASN B O   
4281 C CB  . ASN B 84  ? 0.8843 0.6490 0.6166 0.0654  -0.1261 -0.0779 84  ASN B CB  
4282 C CG  . ASN B 84  ? 0.9349 0.6884 0.6518 0.0797  -0.1438 -0.0879 84  ASN B CG  
4283 O OD1 . ASN B 84  ? 0.9865 0.7201 0.6655 0.0898  -0.1377 -0.0809 84  ASN B OD1 
4284 N ND2 . ASN B 84  ? 1.0447 0.8101 0.7905 0.0808  -0.1658 -0.1051 84  ASN B ND2 
4285 N N   . TRP B 85  ? 0.7968 0.5755 0.5191 0.0384  -0.0733 -0.0399 85  TRP B N   
4286 C CA  . TRP B 85  ? 0.8046 0.5736 0.5004 0.0344  -0.0525 -0.0274 85  TRP B CA  
4287 C C   . TRP B 85  ? 0.8315 0.5885 0.5169 0.0311  -0.0512 -0.0234 85  TRP B C   
4288 O O   . TRP B 85  ? 0.7900 0.5644 0.5062 0.0224  -0.0566 -0.0255 85  TRP B O   
4289 C CB  . TRP B 85  ? 0.7659 0.5627 0.4886 0.0186  -0.0356 -0.0196 85  TRP B CB  
4290 C CG  . TRP B 85  ? 0.8106 0.6073 0.5183 0.0095  -0.0131 -0.0088 85  TRP B CG  
4291 C CD1 . TRP B 85  ? 0.8397 0.6131 0.5066 0.0159  -0.0005 -0.0041 85  TRP B CD1 
4292 C CD2 . TRP B 85  ? 0.7976 0.6196 0.5320 -0.0090 0.0003  -0.0023 85  TRP B CD2 
4293 N NE1 . TRP B 85  ? 0.8404 0.6251 0.5110 -0.0005 0.0214  0.0049  85  TRP B NE1 
4294 C CE2 . TRP B 85  ? 0.8083 0.6238 0.5212 -0.0154 0.0206  0.0051  85  TRP B CE2 
4295 C CE3 . TRP B 85  ? 0.7566 0.6049 0.5291 -0.0208 -0.0028 -0.0025 85  TRP B CE3 
4296 C CZ2 . TRP B 85  ? 0.8178 0.6558 0.5513 -0.0341 0.0357  0.0102  85  TRP B CZ2 
4297 C CZ3 . TRP B 85  ? 0.7428 0.6107 0.5305 -0.0360 0.0108  0.0030  85  TRP B CZ3 
4298 C CH2 . TRP B 85  ? 0.7827 0.6471 0.5536 -0.0432 0.0288  0.0083  85  TRP B CH2 
4299 N N   . ILE B 86  ? 0.8592 0.5831 0.4974 0.0391  -0.0434 -0.0177 86  ILE B N   
4300 C CA  . ILE B 86  ? 0.8587 0.5618 0.4771 0.0352  -0.0379 -0.0114 86  ILE B CA  
4301 C C   . ILE B 86  ? 0.8973 0.5989 0.5065 0.0175  -0.0108 0.0017  86  ILE B C   
4302 O O   . ILE B 86  ? 0.9288 0.6025 0.4954 0.0218  0.0028  0.0081  86  ILE B O   
4303 C CB  . ILE B 86  ? 0.8927 0.5513 0.4581 0.0579  -0.0497 -0.0146 86  ILE B CB  
4304 C CG1 . ILE B 86  ? 0.8752 0.5417 0.4548 0.0762  -0.0788 -0.0312 86  ILE B CG1 
4305 C CG2 . ILE B 86  ? 0.8810 0.5108 0.4205 0.0551  -0.0440 -0.0077 86  ILE B CG2 
4306 C CD1 . ILE B 86  ? 0.8630 0.4866 0.3859 0.1044  -0.0939 -0.0370 86  ILE B CD1 
4307 N N   . PRO B 87  ? 0.8219 0.5521 0.4682 -0.0027 -0.0020 0.0052  87  PRO B N   
4308 C CA  . PRO B 87  ? 0.8401 0.5770 0.4861 -0.0213 0.0225  0.0146  87  PRO B CA  
4309 C C   . PRO B 87  ? 0.9072 0.6002 0.5040 -0.0239 0.0369  0.0230  87  PRO B C   
4310 O O   . PRO B 87  ? 0.8793 0.5706 0.4634 -0.0345 0.0592  0.0299  87  PRO B O   
4311 C CB  . PRO B 87  ? 0.7853 0.5531 0.4744 -0.0389 0.0225  0.0142  87  PRO B CB  
4312 C CG  . PRO B 87  ? 0.7785 0.5672 0.4979 -0.0301 0.0028  0.0058  87  PRO B CG  
4313 C CD  . PRO B 87  ? 0.7849 0.5458 0.4768 -0.0092 -0.0135 -0.0004 87  PRO B CD  
4314 N N   . CYS B 88  ? 1.0641 0.7201 0.6313 -0.0141 0.0257  0.0224  88  CYS B N   
4315 C CA  . CYS B 88  ? 1.1008 0.7054 0.6139 -0.0164 0.0398  0.0317  88  CYS B CA  
4316 C C   . CYS B 88  ? 1.1336 0.7099 0.5997 -0.0050 0.0512  0.0367  88  CYS B C   
4317 O O   . CYS B 88  ? 1.1901 0.7388 0.6227 -0.0171 0.0756  0.0472  88  CYS B O   
4318 C CB  . CYS B 88  ? 1.1071 0.6727 0.5905 -0.0011 0.0222  0.0288  88  CYS B CB  
4319 S SG  . CYS B 88  ? 1.2179 0.7173 0.6394 -0.0123 0.0431  0.0422  88  CYS B SG  
4320 N N   . ASN B 89  ? 1.0808 0.6612 0.5417 0.0177  0.0345  0.0288  89  ASN B N   
4321 C CA  . ASN B 89  ? 1.1400 0.6877 0.5480 0.0341  0.0418  0.0320  89  ASN B CA  
4322 C C   . ASN B 89  ? 1.1459 0.7285 0.5749 0.0264  0.0595  0.0332  89  ASN B C   
4323 O O   . ASN B 89  ? 1.1490 0.7106 0.5397 0.0253  0.0827  0.0414  89  ASN B O   
4324 C CB  . ASN B 89  ? 1.0889 0.6182 0.4743 0.0657  0.0119  0.0205  89  ASN B CB  
4325 C CG  . ASN B 89  ? 1.1311 0.6302 0.4971 0.0780  -0.0077 0.0168  89  ASN B CG  
4326 O OD1 . ASN B 89  ? 1.1694 0.6431 0.5179 0.0667  0.0036  0.0256  89  ASN B OD1 
4327 N ND2 . ASN B 89  ? 1.1267 0.6291 0.4968 0.1016  -0.0378 0.0025  89  ASN B ND2 
4328 N N   . ASN B 90  ? 1.1360 0.7698 0.6222 0.0222  0.0501  0.0251  90  ASN B N   
4329 C CA  . ASN B 90  ? 1.0883 0.7582 0.5978 0.0158  0.0663  0.0254  90  ASN B CA  
4330 C C   . ASN B 90  ? 1.0710 0.7861 0.6362 -0.0098 0.0761  0.0270  90  ASN B C   
4331 O O   . ASN B 90  ? 1.0381 0.7906 0.6490 -0.0110 0.0635  0.0202  90  ASN B O   
4332 C CB  . ASN B 90  ? 1.0607 0.7455 0.5818 0.0361  0.0463  0.0139  90  ASN B CB  
4333 C CG  . ASN B 90  ? 1.1109 0.8203 0.6381 0.0380  0.0627  0.0136  90  ASN B CG  
4334 O OD1 . ASN B 90  ? 1.0990 0.8180 0.6224 0.0249  0.0902  0.0215  90  ASN B OD1 
4335 N ND2 . ASN B 90  ? 1.0400 0.7597 0.5767 0.0546  0.0460  0.0035  90  ASN B ND2 
4336 N N   . ARG B 91  ? 1.2338 0.9433 0.7929 -0.0305 0.0987  0.0356  91  ARG B N   
4337 C CA  . ARG B 91  ? 1.1808 0.9384 0.7920 -0.0532 0.1095  0.0349  91  ARG B CA  
4338 C C   . ARG B 91  ? 1.2105 1.0056 0.8392 -0.0508 0.1236  0.0324  91  ARG B C   
4339 O O   . ARG B 91  ? 1.3000 1.0777 0.8934 -0.0370 0.1330  0.0339  91  ARG B O   
4340 C CB  . ARG B 91  ? 1.1881 0.9307 0.7918 -0.0785 0.1287  0.0425  91  ARG B CB  
4341 C CG  . ARG B 91  ? 1.2646 1.0154 0.8605 -0.0941 0.1613  0.0481  91  ARG B CG  
4342 C CD  . ARG B 91  ? 1.2757 0.9972 0.8537 -0.1204 0.1812  0.0561  91  ARG B CD  
4343 N NE  . ARG B 91  ? 1.2908 0.9419 0.8078 -0.1103 0.1748  0.0632  91  ARG B NE  
4344 C CZ  . ARG B 91  ? 1.4315 1.0303 0.8861 -0.1051 0.1920  0.0727  91  ARG B CZ  
4345 N NH1 . ARG B 91  ? 1.4753 1.0850 0.9204 -0.1104 0.2192  0.0768  91  ARG B NH1 
4346 N NH2 . ARG B 91  ? 1.4403 0.9735 0.8382 -0.0922 0.1818  0.0779  91  ARG B NH2 
4347 N N   . ASN B 92  ? 1.0950 0.9416 0.7761 -0.0618 0.1245  0.0275  92  ASN B N   
4348 C CA  . ASN B 92  ? 1.0518 0.9415 0.7568 -0.0575 0.1352  0.0228  92  ASN B CA  
4349 C C   . ASN B 92  ? 0.9927 0.8847 0.6957 -0.0313 0.1167  0.0160  92  ASN B C   
4350 O O   . ASN B 92  ? 1.0090 0.9341 0.7293 -0.0234 0.1228  0.0110  92  ASN B O   
4351 C CB  . ASN B 92  ? 1.0594 0.9457 0.7394 -0.0629 0.1660  0.0278  92  ASN B CB  
4352 C CG  . ASN B 92  ? 1.1136 0.9891 0.7896 -0.0916 0.1873  0.0351  92  ASN B CG  
4353 O OD1 . ASN B 92  ? 1.1128 0.9543 0.7463 -0.0968 0.2096  0.0432  92  ASN B OD1 
4354 N ND2 . ASN B 92  ? 1.1643 1.0640 0.8810 -0.1105 0.1804  0.0321  92  ASN B ND2 
4355 N N   . ARG B 93  ? 0.8399 0.6993 0.5243 -0.0178 0.0939  0.0142  93  ARG B N   
4356 C CA  . ARG B 93  ? 0.8621 0.7233 0.5494 0.0032  0.0750  0.0063  93  ARG B CA  
4357 C C   . ARG B 93  ? 0.8099 0.7122 0.5443 0.0000  0.0677  0.0014  93  ARG B C   
4358 O O   . ARG B 93  ? 0.7760 0.6906 0.5159 0.0150  0.0626  -0.0045 93  ARG B O   
4359 C CB  . ARG B 93  ? 0.8581 0.6838 0.5269 0.0137  0.0511  0.0031  93  ARG B CB  
4360 C CG  . ARG B 93  ? 0.8040 0.6325 0.4832 0.0294  0.0309  -0.0062 93  ARG B CG  
4361 C CD  . ARG B 93  ? 0.8010 0.5979 0.4626 0.0409  0.0079  -0.0125 93  ARG B CD  
4362 N NE  . ARG B 93  ? 0.7899 0.5934 0.4712 0.0488  -0.0099 -0.0217 93  ARG B NE  
4363 C CZ  . ARG B 93  ? 0.7668 0.5543 0.4492 0.0553  -0.0322 -0.0304 93  ARG B CZ  
4364 N NH1 . ARG B 93  ? 0.7629 0.5290 0.4272 0.0592  -0.0423 -0.0328 93  ARG B NH1 
4365 N NH2 . ARG B 93  ? 0.7498 0.5426 0.4526 0.0577  -0.0450 -0.0378 93  ARG B NH2 
4366 N N   . PHE B 94  ? 0.8175 0.7373 0.5816 -0.0176 0.0662  0.0036  94  PHE B N   
4367 C CA  . PHE B 94  ? 0.8128 0.7668 0.6163 -0.0203 0.0585  -0.0001 94  PHE B CA  
4368 C C   . PHE B 94  ? 0.8235 0.8166 0.6543 -0.0361 0.0748  0.0004  94  PHE B C   
4369 O O   . PHE B 94  ? 0.8107 0.8321 0.6729 -0.0402 0.0680  -0.0026 94  PHE B O   
4370 C CB  . PHE B 94  ? 0.7752 0.7174 0.5902 -0.0250 0.0403  0.0001  94  PHE B CB  
4371 C CG  . PHE B 94  ? 0.7808 0.6973 0.5826 -0.0104 0.0226  -0.0038 94  PHE B CG  
4372 C CD1 . PHE B 94  ? 0.7733 0.6959 0.5843 0.0012  0.0133  -0.0086 94  PHE B CD1 
4373 C CD2 . PHE B 94  ? 0.7810 0.6658 0.5602 -0.0077 0.0146  -0.0041 94  PHE B CD2 
4374 C CE1 . PHE B 94  ? 0.7812 0.6787 0.5817 0.0117  -0.0028 -0.0138 94  PHE B CE1 
4375 C CE2 . PHE B 94  ? 0.7813 0.6469 0.5533 0.0046  -0.0031 -0.0106 94  PHE B CE2 
4376 C CZ  . PHE B 94  ? 0.7562 0.6280 0.5399 0.0125  -0.0112 -0.0155 94  PHE B CZ  
4377 N N   . GLY B 95  ? 0.8453 0.8394 0.6637 -0.0457 0.0962  0.0036  95  GLY B N   
4378 C CA  . GLY B 95  ? 0.8045 0.8386 0.6519 -0.0635 0.1138  0.0020  95  GLY B CA  
4379 C C   . GLY B 95  ? 0.8199 0.8399 0.6671 -0.0878 0.1194  0.0068  95  GLY B C   
4380 O O   . GLY B 95  ? 0.8631 0.8379 0.6739 -0.0905 0.1220  0.0136  95  GLY B O   
4381 N N   . GLN B 96  ? 1.0912 1.1469 0.9761 -0.1037 0.1196  0.0024  96  GLN B N   
4382 C CA  . GLN B 96  ? 1.0904 1.1349 0.9779 -0.1283 0.1249  0.0049  96  GLN B CA  
4383 C C   . GLN B 96  ? 1.0534 1.0768 0.9393 -0.1255 0.1027  0.0057  96  GLN B C   
4384 O O   . GLN B 96  ? 1.0438 1.0950 0.9589 -0.1246 0.0899  0.0002  96  GLN B O   
4385 C CB  . GLN B 96  ? 1.0658 1.1619 0.9960 -0.1472 0.1358  -0.0030 96  GLN B CB  
4386 C CG  . GLN B 96  ? 1.0609 1.1872 0.9996 -0.1502 0.1598  -0.0054 96  GLN B CG  
4387 C CD  . GLN B 96  ? 1.1029 1.2517 1.0644 -0.1818 0.1811  -0.0085 96  GLN B CD  
4388 O OE1 . GLN B 96  ? 1.1770 1.2882 1.1090 -0.1992 0.2000  -0.0003 96  GLN B OE1 
4389 N NE2 . GLN B 96  ? 1.0593 1.2678 1.0722 -0.1894 0.1776  -0.0211 96  GLN B NE2 
4390 N N   . THR B 97  ? 0.8413 0.8155 0.6913 -0.1228 0.0987  0.0121  97  THR B N   
4391 C CA  . THR B 97  ? 0.7955 0.7491 0.6418 -0.1181 0.0795  0.0124  97  THR B CA  
4392 C C   . THR B 97  ? 0.7931 0.7068 0.6131 -0.1306 0.0837  0.0169  97  THR B C   
4393 O O   . THR B 97  ? 0.7609 0.6353 0.5498 -0.1198 0.0760  0.0201  97  THR B O   
4394 C CB  . THR B 97  ? 0.7636 0.7003 0.5956 -0.0957 0.0648  0.0125  97  THR B CB  
4395 O OG1 . THR B 97  ? 0.8204 0.7231 0.6144 -0.0874 0.0711  0.0164  97  THR B OG1 
4396 C CG2 . THR B 97  ? 0.7155 0.6853 0.5702 -0.0837 0.0600  0.0080  97  THR B CG2 
4397 N N   . PRO B 98  ? 0.8565 0.7783 0.6876 -0.1532 0.0953  0.0159  98  PRO B N   
4398 C CA  . PRO B 98  ? 0.8334 0.7096 0.6341 -0.1657 0.1003  0.0203  98  PRO B CA  
4399 C C   . PRO B 98  ? 0.8286 0.6803 0.6192 -0.1563 0.0810  0.0193  98  PRO B C   
4400 O O   . PRO B 98  ? 0.8537 0.6575 0.6060 -0.1521 0.0800  0.0236  98  PRO B O   
4401 C CB  . PRO B 98  ? 0.8267 0.7263 0.6528 -0.1935 0.1135  0.0162  98  PRO B CB  
4402 C CG  . PRO B 98  ? 0.7773 0.7390 0.6519 -0.1908 0.1071  0.0076  98  PRO B CG  
4403 C CD  . PRO B 98  ? 0.7676 0.7396 0.6389 -0.1678 0.1038  0.0094  98  PRO B CD  
4404 N N   . VAL B 99  ? 0.7723 0.6544 0.5935 -0.1515 0.0664  0.0137  99  VAL B N   
4405 C CA  . VAL B 99  ? 0.7604 0.6236 0.5742 -0.1433 0.0511  0.0121  99  VAL B CA  
4406 C C   . VAL B 99  ? 0.7684 0.6124 0.5641 -0.1214 0.0406  0.0137  99  VAL B C   
4407 O O   . VAL B 99  ? 0.7564 0.5664 0.5268 -0.1136 0.0340  0.0141  99  VAL B O   
4408 C CB  . VAL B 99  ? 0.7602 0.6593 0.6078 -0.1444 0.0409  0.0063  99  VAL B CB  
4409 C CG1 . VAL B 99  ? 0.7079 0.5914 0.5483 -0.1327 0.0273  0.0049  99  VAL B CG1 
4410 C CG2 . VAL B 99  ? 0.7038 0.6188 0.5676 -0.1654 0.0468  0.0016  99  VAL B CG2 
4411 N N   . GLN B 100 ? 0.6870 0.5530 0.4963 -0.1103 0.0373  0.0130  100 GLN B N   
4412 C CA  . GLN B 100 ? 0.7464 0.5957 0.5406 -0.0914 0.0270  0.0125  100 GLN B CA  
4413 C C   . GLN B 100 ? 0.7724 0.5795 0.5235 -0.0856 0.0322  0.0163  100 GLN B C   
4414 O O   . GLN B 100 ? 0.7705 0.5517 0.5006 -0.0710 0.0206  0.0144  100 GLN B O   
4415 C CB  . GLN B 100 ? 0.7407 0.6152 0.5525 -0.0827 0.0244  0.0108  100 GLN B CB  
4416 C CG  . GLN B 100 ? 0.6809 0.5852 0.5249 -0.0822 0.0162  0.0077  100 GLN B CG  
4417 C CD  . GLN B 100 ? 0.7002 0.6240 0.5557 -0.0750 0.0166  0.0067  100 GLN B CD  
4418 O OE1 . GLN B 100 ? 0.6775 0.5948 0.5308 -0.0632 0.0079  0.0045  100 GLN B OE1 
4419 N NE2 . GLN B 100 ? 0.6711 0.6193 0.5392 -0.0817 0.0262  0.0070  100 GLN B NE2 
4420 N N   . GLU B 101 ? 0.8675 0.6677 0.6039 -0.0960 0.0498  0.0213  101 GLU B N   
4421 C CA  . GLU B 101 ? 0.9378 0.6913 0.6253 -0.0907 0.0576  0.0268  101 GLU B CA  
4422 C C   . GLU B 101 ? 0.9677 0.6795 0.6267 -0.0921 0.0536  0.0284  101 GLU B C   
4423 O O   . GLU B 101 ? 0.9711 0.6425 0.5908 -0.0748 0.0455  0.0292  101 GLU B O   
4424 C CB  . GLU B 101 ? 0.9384 0.6942 0.6178 -0.1060 0.0819  0.0324  101 GLU B CB  
4425 C CG  . GLU B 101 ? 1.0101 0.7157 0.6331 -0.0983 0.0927  0.0396  101 GLU B CG  
4426 C CD  . GLU B 101 ? 1.0435 0.7418 0.6544 -0.1211 0.1216  0.0466  101 GLU B CD  
4427 O OE1 . GLU B 101 ? 1.0839 0.8309 0.7366 -0.1362 0.1328  0.0436  101 GLU B OE1 
4428 O OE2 . GLU B 101 ? 1.1116 0.7559 0.6712 -0.1235 0.1335  0.0546  101 GLU B OE2 
4429 N N   . ARG B 102 ? 0.9025 0.6216 0.5785 -0.1106 0.0577  0.0277  102 ARG B N   
4430 C CA  . ARG B 102 ? 0.9183 0.5932 0.5636 -0.1118 0.0545  0.0287  102 ARG B CA  
4431 C C   . ARG B 102 ? 0.9408 0.6130 0.5880 -0.0904 0.0324  0.0222  102 ARG B C   
4432 O O   . ARG B 102 ? 0.9555 0.5838 0.5644 -0.0770 0.0251  0.0223  102 ARG B O   
4433 C CB  . ARG B 102 ? 0.9325 0.6156 0.5958 -0.1373 0.0632  0.0276  102 ARG B CB  
4434 C CG  . ARG B 102 ? 0.9695 0.6012 0.5973 -0.1388 0.0601  0.0281  102 ARG B CG  
4435 C CD  . ARG B 102 ? 0.9450 0.5685 0.5762 -0.1688 0.0746  0.0286  102 ARG B CD  
4436 N NE  . ARG B 102 ? 1.0221 0.5888 0.6141 -0.1689 0.0705  0.0287  102 ARG B NE  
4437 C CZ  . ARG B 102 ? 1.0110 0.5679 0.6079 -0.1899 0.0735  0.0247  102 ARG B CZ  
4438 N NH1 . ARG B 102 ? 0.9517 0.5549 0.5933 -0.2133 0.0799  0.0195  102 ARG B NH1 
4439 N NH2 . ARG B 102 ? 1.0443 0.5418 0.5983 -0.1861 0.0686  0.0248  102 ARG B NH2 
4440 N N   . LEU B 103 ? 0.8378 0.5562 0.5285 -0.0866 0.0220  0.0161  103 LEU B N   
4441 C CA  . LEU B 103 ? 0.7986 0.5212 0.4967 -0.0679 0.0037  0.0090  103 LEU B CA  
4442 C C   . LEU B 103 ? 0.8331 0.5363 0.5071 -0.0456 -0.0064 0.0070  103 LEU B C   
4443 O O   . LEU B 103 ? 0.8362 0.5154 0.4891 -0.0281 -0.0191 0.0023  103 LEU B O   
4444 C CB  . LEU B 103 ? 0.7729 0.5456 0.5195 -0.0713 -0.0012 0.0045  103 LEU B CB  
4445 C CG  . LEU B 103 ? 0.7742 0.5646 0.5418 -0.0854 0.0015  0.0031  103 LEU B CG  
4446 C CD1 . LEU B 103 ? 0.6324 0.4682 0.4401 -0.0903 0.0009  0.0016  103 LEU B CD1 
4447 C CD2 . LEU B 103 ? 0.6630 0.4365 0.4204 -0.0764 -0.0075 -0.0020 103 LEU B CD2 
4448 N N   . SER B 104 ? 0.8222 0.5346 0.4966 -0.0440 -0.0020 0.0093  104 SER B N   
4449 C CA  . SER B 104 ? 0.8317 0.5230 0.4788 -0.0224 -0.0124 0.0064  104 SER B CA  
4450 C C   . SER B 104 ? 0.8549 0.4889 0.4444 -0.0117 -0.0121 0.0102  104 SER B C   
4451 O O   . SER B 104 ? 0.8552 0.4700 0.4257 0.0105  -0.0296 0.0033  104 SER B O   
4452 C CB  . SER B 104 ? 0.8183 0.5213 0.4662 -0.0240 -0.0037 0.0095  104 SER B CB  
4453 O OG  . SER B 104 ? 0.8607 0.5428 0.4801 -0.0022 -0.0149 0.0055  104 SER B OG  
4454 N N   . CYS B 105 ? 0.9682 0.5735 0.5295 -0.0277 0.0077  0.0204  105 CYS B N   
4455 C CA  . CYS B 105 ? 1.0215 0.5621 0.5193 -0.0189 0.0108  0.0262  105 CYS B CA  
4456 C C   . CYS B 105 ? 1.0697 0.5874 0.5563 -0.0096 -0.0027 0.0213  105 CYS B C   
4457 O O   . CYS B 105 ? 1.0829 0.5504 0.5186 0.0115  -0.0119 0.0211  105 CYS B O   
4458 C CB  . CYS B 105 ? 0.9962 0.5123 0.4708 -0.0436 0.0383  0.0382  105 CYS B CB  
4459 S SG  . CYS B 105 ? 1.1166 0.6536 0.5945 -0.0520 0.0585  0.0442  105 CYS B SG  
4460 N N   . LEU B 106 ? 0.9856 0.5357 0.5141 -0.0236 -0.0035 0.0173  106 LEU B N   
4461 C CA  . LEU B 106 ? 1.0015 0.5334 0.5208 -0.0125 -0.0164 0.0111  106 LEU B CA  
4462 C C   . LEU B 106 ? 0.9712 0.5169 0.4981 0.0177  -0.0401 -0.0006 106 LEU B C   
4463 O O   . LEU B 106 ? 1.0041 0.5131 0.4954 0.0399  -0.0529 -0.0052 106 LEU B O   
4464 C CB  . LEU B 106 ? 0.9541 0.5205 0.5161 -0.0322 -0.0124 0.0083  106 LEU B CB  
4465 C CG  . LEU B 106 ? 0.9460 0.4994 0.5039 -0.0623 0.0070  0.0157  106 LEU B CG  
4466 C CD1 . LEU B 106 ? 0.8970 0.5014 0.5076 -0.0798 0.0082  0.0109  106 LEU B CD1 
4467 C CD2 . LEU B 106 ? 0.9466 0.4326 0.4504 -0.0622 0.0095  0.0189  106 LEU B CD2 
4468 N N   . ALA B 107 ? 0.9039 0.5013 0.4765 0.0193  -0.0465 -0.0067 107 ALA B N   
4469 C CA  . ALA B 107 ? 0.8872 0.5018 0.4721 0.0449  -0.0686 -0.0198 107 ALA B CA  
4470 C C   . ALA B 107 ? 0.9401 0.5117 0.4731 0.0688  -0.0786 -0.0205 107 ALA B C   
4471 O O   . ALA B 107 ? 0.9562 0.5192 0.4767 0.0959  -0.0992 -0.0318 107 ALA B O   
4472 C CB  . ALA B 107 ? 0.8272 0.5010 0.4703 0.0374  -0.0714 -0.0255 107 ALA B CB  
4473 N N   . LYS B 108 ? 0.9919 0.5382 0.4940 0.0610  -0.0645 -0.0096 108 LYS B N   
4474 C CA  . LYS B 108 ? 1.0375 0.5432 0.4871 0.0849  -0.0734 -0.0101 108 LYS B CA  
4475 C C   . LYS B 108 ? 1.0979 0.5326 0.4767 0.1008  -0.0746 -0.0049 108 LYS B C   
4476 O O   . LYS B 108 ? 1.1091 0.5194 0.4565 0.1326  -0.0964 -0.0140 108 LYS B O   
4477 C CB  . LYS B 108 ? 1.0289 0.5327 0.4679 0.0722  -0.0556 -0.0003 108 LYS B CB  
4478 C CG  . LYS B 108 ? 1.0173 0.5019 0.4221 0.0983  -0.0694 -0.0057 108 LYS B CG  
4479 C CD  . LYS B 108 ? 1.1150 0.5350 0.4447 0.1041  -0.0551 0.0071  108 LYS B CD  
4480 C CE  . LYS B 108 ? 1.1231 0.5466 0.4537 0.0757  -0.0231 0.0214  108 LYS B CE  
4481 N NZ  . LYS B 108 ? 1.1389 0.4991 0.3892 0.0894  -0.0115 0.0315  108 LYS B NZ  
4482 N N   . ASN B 109 ? 1.2184 0.6183 0.5713 0.0790  -0.0522 0.0088  109 ASN B N   
4483 C CA  . ASN B 109 ? 1.2189 0.5414 0.4984 0.0898  -0.0495 0.0162  109 ASN B CA  
4484 C C   . ASN B 109 ? 1.2776 0.5903 0.5532 0.1132  -0.0720 0.0046  109 ASN B C   
4485 O O   . ASN B 109 ? 1.3210 0.5721 0.5323 0.1399  -0.0829 0.0045  109 ASN B O   
4486 C CB  . ASN B 109 ? 1.2708 0.5668 0.5371 0.0546  -0.0197 0.0311  109 ASN B CB  
4487 C CG  . ASN B 109 ? 1.2913 0.5849 0.5468 0.0344  0.0060  0.0435  109 ASN B CG  
4488 O OD1 . ASN B 109 ? 1.2787 0.6000 0.5464 0.0440  0.0021  0.0406  109 ASN B OD1 
4489 N ND2 . ASN B 109 ? 1.3107 0.5725 0.5449 0.0057  0.0327  0.0560  109 ASN B ND2 
4490 N N   . ASN B 110 ? 1.1957 0.5681 0.5368 0.1066  -0.0796 -0.0059 110 ASN B N   
4491 C CA  . ASN B 110 ? 1.1464 0.5207 0.4923 0.1290  -0.0994 -0.0188 110 ASN B CA  
4492 C C   . ASN B 110 ? 1.1001 0.5271 0.4872 0.1544  -0.1246 -0.0371 110 ASN B C   
4493 O O   . ASN B 110 ? 1.0718 0.5152 0.4747 0.1742  -0.1413 -0.0508 110 ASN B O   
4494 C CB  . ASN B 110 ? 1.1205 0.5224 0.5071 0.1054  -0.0892 -0.0188 110 ASN B CB  
4495 C CG  . ASN B 110 ? 1.1863 0.5371 0.5359 0.0788  -0.0666 -0.0039 110 ASN B CG  
4496 O OD1 . ASN B 110 ? 1.2270 0.5093 0.5161 0.0889  -0.0673 -0.0002 110 ASN B OD1 
4497 N ND2 . ASN B 110 ? 1.1140 0.4968 0.4993 0.0449  -0.0468 0.0038  110 ASN B ND2 
4498 N N   . SER B 111 ? 1.0700 0.5235 0.4745 0.1544  -0.1274 -0.0388 111 SER B N   
4499 C CA  . SER B 111 ? 1.0691 0.5663 0.5076 0.1769  -0.1519 -0.0570 111 SER B CA  
4500 C C   . SER B 111 ? 0.9707 0.5328 0.4792 0.1745  -0.1601 -0.0713 111 SER B C   
4501 O O   . SER B 111 ? 0.9447 0.5219 0.4629 0.2012  -0.1817 -0.0881 111 SER B O   
4502 C CB  . SER B 111 ? 1.0978 0.5471 0.4761 0.2178  -0.1754 -0.0654 111 SER B CB  
4503 O OG  . SER B 111 ? 1.0638 0.5625 0.4831 0.2398  -0.2022 -0.0872 111 SER B OG  
4504 N N   . ILE B 112 ? 0.9085 0.5113 0.4663 0.1426  -0.1420 -0.0649 112 ILE B N   
4505 C CA  . ILE B 112 ? 0.8824 0.5402 0.5002 0.1344  -0.1420 -0.0738 112 ILE B CA  
4506 C C   . ILE B 112 ? 0.8217 0.5267 0.4922 0.1041  -0.1271 -0.0685 112 ILE B C   
4507 O O   . ILE B 112 ? 0.8197 0.5097 0.4776 0.0838  -0.1105 -0.0543 112 ILE B O   
4508 C CB  . ILE B 112 ? 0.9492 0.5812 0.5468 0.1318  -0.1338 -0.0692 112 ILE B CB  
4509 C CG1 . ILE B 112 ? 0.8809 0.5673 0.5336 0.1300  -0.1352 -0.0803 112 ILE B CG1 
4510 C CG2 . ILE B 112 ? 0.9274 0.5327 0.5067 0.1013  -0.1098 -0.0507 112 ILE B CG2 
4511 C CD1 . ILE B 112 ? 0.8536 0.5126 0.4825 0.1332  -0.1308 -0.0789 112 ILE B CD1 
4512 N N   . TYR B 113 ? 0.7870 0.5488 0.5158 0.1019  -0.1328 -0.0803 113 TYR B N   
4513 C CA  . TYR B 113 ? 0.7714 0.5728 0.5462 0.0744  -0.1180 -0.0747 113 TYR B CA  
4514 C C   . TYR B 113 ? 0.7820 0.5775 0.5543 0.0560  -0.1000 -0.0634 113 TYR B C   
4515 O O   . TYR B 113 ? 0.7755 0.5644 0.5404 0.0638  -0.1012 -0.0669 113 TYR B O   
4516 C CB  . TYR B 113 ? 0.7231 0.5810 0.5570 0.0745  -0.1253 -0.0893 113 TYR B CB  
4517 C CG  . TYR B 113 ? 0.7215 0.5960 0.5732 0.0812  -0.1399 -0.1002 113 TYR B CG  
4518 C CD1 . TYR B 113 ? 0.7521 0.6144 0.5844 0.1092  -0.1623 -0.1140 113 TYR B CD1 
4519 C CD2 . TYR B 113 ? 0.6922 0.5918 0.5774 0.0614  -0.1331 -0.0979 113 TYR B CD2 
4520 C CE1 . TYR B 113 ? 0.7134 0.5911 0.5620 0.1158  -0.1782 -0.1262 113 TYR B CE1 
4521 C CE2 . TYR B 113 ? 0.6945 0.6064 0.5954 0.0667  -0.1477 -0.1094 113 TYR B CE2 
4522 C CZ  . TYR B 113 ? 0.7267 0.6289 0.6103 0.0934  -0.1706 -0.1241 113 TYR B CZ  
4523 O OH  . TYR B 113 ? 0.7648 0.6784 0.6629 0.0995  -0.1878 -0.1379 113 TYR B OH  
4524 N N   . VAL B 114 ? 0.7360 0.5343 0.5140 0.0332  -0.0848 -0.0513 114 VAL B N   
4525 C CA  . VAL B 114 ? 0.7181 0.5150 0.4970 0.0148  -0.0696 -0.0422 114 VAL B CA  
4526 C C   . VAL B 114 ? 0.6740 0.5137 0.4973 -0.0027 -0.0610 -0.0402 114 VAL B C   
4527 O O   . VAL B 114 ? 0.6888 0.5390 0.5235 -0.0101 -0.0587 -0.0367 114 VAL B O   
4528 C CB  . VAL B 114 ? 0.7747 0.5319 0.5145 0.0040  -0.0588 -0.0300 114 VAL B CB  
4529 C CG1 . VAL B 114 ? 0.7007 0.4640 0.4493 -0.0166 -0.0454 -0.0236 114 VAL B CG1 
4530 C CG2 . VAL B 114 ? 0.7651 0.4688 0.4514 0.0211  -0.0653 -0.0301 114 VAL B CG2 
4531 N N   . VAL B 115 ? 0.6879 0.5482 0.5312 -0.0076 -0.0562 -0.0421 115 VAL B N   
4532 C CA  . VAL B 115 ? 0.6614 0.5538 0.5370 -0.0235 -0.0463 -0.0383 115 VAL B CA  
4533 C C   . VAL B 115 ? 0.6829 0.5643 0.5447 -0.0363 -0.0362 -0.0303 115 VAL B C   
4534 O O   . VAL B 115 ? 0.6604 0.5294 0.5081 -0.0326 -0.0362 -0.0329 115 VAL B O   
4535 C CB  . VAL B 115 ? 0.6362 0.5626 0.5450 -0.0196 -0.0467 -0.0469 115 VAL B CB  
4536 C CG1 . VAL B 115 ? 0.5920 0.5438 0.5270 -0.0359 -0.0351 -0.0410 115 VAL B CG1 
4537 C CG2 . VAL B 115 ? 0.5992 0.5399 0.5253 -0.0061 -0.0590 -0.0589 115 VAL B CG2 
4538 N N   . ALA B 116 ? 0.6848 0.5718 0.5514 -0.0503 -0.0290 -0.0224 116 ALA B N   
4539 C CA  . ALA B 116 ? 0.6775 0.5594 0.5355 -0.0627 -0.0217 -0.0174 116 ALA B CA  
4540 C C   . ALA B 116 ? 0.6697 0.5784 0.5502 -0.0721 -0.0162 -0.0132 116 ALA B C   
4541 O O   . ALA B 116 ? 0.6430 0.5665 0.5404 -0.0709 -0.0166 -0.0123 116 ALA B O   
4542 C CB  . ALA B 116 ? 0.6275 0.4816 0.4596 -0.0692 -0.0186 -0.0129 116 ALA B CB  
4543 N N   . ASN B 117 ? 0.6676 0.5799 0.5459 -0.0802 -0.0122 -0.0116 117 ASN B N   
4544 C CA  . ASN B 117 ? 0.5741 0.5072 0.4663 -0.0862 -0.0087 -0.0079 117 ASN B CA  
4545 C C   . ASN B 117 ? 0.5912 0.5249 0.4795 -0.0959 -0.0070 -0.0058 117 ASN B C   
4546 O O   . ASN B 117 ? 0.6144 0.5358 0.4908 -0.1024 -0.0068 -0.0083 117 ASN B O   
4547 C CB  . ASN B 117 ? 0.6281 0.5688 0.5207 -0.0846 -0.0070 -0.0098 117 ASN B CB  
4548 C CG  . ASN B 117 ? 0.5815 0.5376 0.4808 -0.0876 -0.0044 -0.0055 117 ASN B CG  
4549 O OD1 . ASN B 117 ? 0.5729 0.5318 0.4668 -0.0921 -0.0061 -0.0059 117 ASN B OD1 
4550 N ND2 . ASN B 117 ? 0.5501 0.5150 0.4605 -0.0849 -0.0009 -0.0021 117 ASN B ND2 
4551 N N   . ILE B 118 ? 0.5894 0.5373 0.4885 -0.0970 -0.0057 -0.0024 118 ILE B N   
4552 C CA  . ILE B 118 ? 0.6028 0.5598 0.5047 -0.1047 -0.0034 -0.0020 118 ILE B CA  
4553 C C   . ILE B 118 ? 0.6259 0.6037 0.5402 -0.1006 -0.0046 0.0000  118 ILE B C   
4554 O O   . ILE B 118 ? 0.6466 0.6257 0.5627 -0.0945 -0.0060 0.0021  118 ILE B O   
4555 C CB  . ILE B 118 ? 0.6487 0.5942 0.5431 -0.1068 0.0007  -0.0005 118 ILE B CB  
4556 C CG1 . ILE B 118 ? 0.6359 0.5807 0.5330 -0.0968 -0.0011 0.0018  118 ILE B CG1 
4557 C CG2 . ILE B 118 ? 0.6490 0.5659 0.5230 -0.1094 0.0016  -0.0017 118 ILE B CG2 
4558 C CD1 . ILE B 118 ? 0.6209 0.5523 0.5049 -0.0959 0.0029  0.0031  118 ILE B CD1 
4559 N N   . GLY B 119 ? 0.6399 0.6336 0.5617 -0.1037 -0.0035 -0.0011 119 GLY B N   
4560 C CA  . GLY B 119 ? 0.6129 0.6250 0.5430 -0.0965 -0.0067 -0.0004 119 GLY B CA  
4561 C C   . GLY B 119 ? 0.6107 0.6269 0.5448 -0.0903 -0.0049 0.0015  119 GLY B C   
4562 O O   . GLY B 119 ? 0.6328 0.6555 0.5702 -0.0946 0.0000  -0.0003 119 GLY B O   
4563 N N   . ASP B 120 ? 0.6223 0.6332 0.5541 -0.0805 -0.0079 0.0050  120 ASP B N   
4564 C CA  . ASP B 120 ? 0.6210 0.6319 0.5533 -0.0721 -0.0079 0.0059  120 ASP B CA  
4565 C C   . ASP B 120 ? 0.6379 0.6672 0.5742 -0.0627 -0.0119 0.0041  120 ASP B C   
4566 O O   . ASP B 120 ? 0.6726 0.7034 0.6049 -0.0587 -0.0165 0.0050  120 ASP B O   
4567 C CB  . ASP B 120 ? 0.6648 0.6542 0.5914 -0.0677 -0.0098 0.0094  120 ASP B CB  
4568 C CG  . ASP B 120 ? 0.6817 0.6639 0.6053 -0.0598 -0.0110 0.0086  120 ASP B CG  
4569 O OD1 . ASP B 120 ? 0.6829 0.6754 0.6069 -0.0576 -0.0082 0.0060  120 ASP B OD1 
4570 O OD2 . ASP B 120 ? 0.6834 0.6486 0.6038 -0.0565 -0.0139 0.0101  120 ASP B OD2 
4571 N N   . LYS B 121 ? 0.6133 0.6566 0.5551 -0.0571 -0.0102 0.0010  121 LYS B N   
4572 C CA  . LYS B 121 ? 0.5996 0.6603 0.5446 -0.0429 -0.0154 -0.0021 121 LYS B CA  
4573 C C   . LYS B 121 ? 0.6440 0.6905 0.5801 -0.0305 -0.0157 -0.0007 121 LYS B C   
4574 O O   . LYS B 121 ? 0.6798 0.7197 0.6143 -0.0336 -0.0101 -0.0010 121 LYS B O   
4575 C CB  . LYS B 121 ? 0.5830 0.6826 0.5475 -0.0456 -0.0135 -0.0105 121 LYS B CB  
4576 C CG  . LYS B 121 ? 0.5817 0.6923 0.5544 -0.0528 -0.0022 -0.0128 121 LYS B CG  
4577 C CD  . LYS B 121 ? 0.5635 0.7182 0.5613 -0.0579 0.0014  -0.0223 121 LYS B CD  
4578 C CE  . LYS B 121 ? 0.5614 0.7292 0.5650 -0.0600 0.0153  -0.0243 121 LYS B CE  
4579 N NZ  . LYS B 121 ? 0.5793 0.7922 0.6123 -0.0720 0.0232  -0.0339 121 LYS B NZ  
4580 N N   . LYS B 122 ? 0.5454 0.5822 0.4709 -0.0155 -0.0229 0.0006  122 LYS B N   
4581 C CA  . LYS B 122 ? 0.5965 0.6124 0.5090 -0.0021 -0.0255 0.0014  122 LYS B CA  
4582 C C   . LYS B 122 ? 0.6308 0.6618 0.5405 0.0186  -0.0322 -0.0031 122 LYS B C   
4583 O O   . LYS B 122 ? 0.6213 0.6391 0.5171 0.0283  -0.0396 -0.0002 122 LYS B O   
4584 C CB  . LYS B 122 ? 0.5944 0.5706 0.4910 -0.0051 -0.0277 0.0083  122 LYS B CB  
4585 C CG  . LYS B 122 ? 0.5930 0.5547 0.4935 -0.0200 -0.0235 0.0097  122 LYS B CG  
4586 C CD  . LYS B 122 ? 0.6326 0.5870 0.5298 -0.0143 -0.0237 0.0053  122 LYS B CD  
4587 C CE  . LYS B 122 ? 0.6019 0.5434 0.5016 -0.0257 -0.0227 0.0047  122 LYS B CE  
4588 N NZ  . LYS B 122 ? 0.5689 0.5291 0.4760 -0.0345 -0.0167 0.0039  122 LYS B NZ  
4589 N N   . PRO B 123 ? 0.6763 0.7342 0.5966 0.0277  -0.0297 -0.0104 123 PRO B N   
4590 C CA  . PRO B 123 ? 0.6609 0.7384 0.5812 0.0511  -0.0372 -0.0171 123 PRO B CA  
4591 C C   . PRO B 123 ? 0.7334 0.7682 0.6236 0.0699  -0.0458 -0.0132 123 PRO B C   
4592 O O   . PRO B 123 ? 0.7255 0.7240 0.6010 0.0659  -0.0439 -0.0087 123 PRO B O   
4593 C CB  . PRO B 123 ? 0.6731 0.7852 0.6108 0.0544  -0.0284 -0.0254 123 PRO B CB  
4594 C CG  . PRO B 123 ? 0.6725 0.7881 0.6209 0.0294  -0.0160 -0.0226 123 PRO B CG  
4595 C CD  . PRO B 123 ? 0.6953 0.7670 0.6264 0.0180  -0.0187 -0.0132 123 PRO B CD  
4596 N N   . CYS B 124 ? 0.8119 0.8487 0.6913 0.0907  -0.0565 -0.0156 124 CYS B N   
4597 C CA  . CYS B 124 ? 0.8417 0.8333 0.6870 0.1114  -0.0651 -0.0120 124 CYS B CA  
4598 C C   . CYS B 124 ? 0.8627 0.8778 0.7049 0.1427  -0.0762 -0.0215 124 CYS B C   
4599 O O   . CYS B 124 ? 0.8403 0.9075 0.7084 0.1461  -0.0786 -0.0304 124 CYS B O   
4600 C CB  . CYS B 124 ? 0.8533 0.7985 0.6725 0.1041  -0.0673 -0.0004 124 CYS B CB  
4601 S SG  . CYS B 124 ? 0.8849 0.8541 0.7087 0.1018  -0.0718 0.0003  124 CYS B SG  
4602 N N   . ASP B 125 ? 1.0093 0.9866 0.8208 0.1659  -0.0834 -0.0212 125 ASP B N   
4603 C CA  . ASP B 125 ? 1.0505 1.0415 0.8517 0.2014  -0.0963 -0.0305 125 ASP B CA  
4604 C C   . ASP B 125 ? 1.0773 1.0184 0.8354 0.2184  -0.1087 -0.0228 125 ASP B C   
4605 O O   . ASP B 125 ? 1.0757 0.9657 0.8093 0.2019  -0.1048 -0.0094 125 ASP B O   
4606 C CB  . ASP B 125 ? 1.0489 1.0310 0.8408 0.2212  -0.0965 -0.0372 125 ASP B CB  
4607 C CG  . ASP B 125 ? 1.1444 1.1905 0.9770 0.2173  -0.0859 -0.0487 125 ASP B CG  
4608 O OD1 . ASP B 125 ? 1.1314 1.1920 0.9861 0.1877  -0.0724 -0.0453 125 ASP B OD1 
4609 O OD2 . ASP B 125 ? 1.1779 1.2600 1.0194 0.2447  -0.0903 -0.0614 125 ASP B OD2 
4610 N N   . THR B 126 ? 1.1583 1.1158 0.9064 0.2528  -0.1234 -0.0319 126 THR B N   
4611 C CA  . THR B 126 ? 1.2095 1.1112 0.9063 0.2752  -0.1362 -0.0245 126 THR B CA  
4612 C C   . THR B 126 ? 1.2360 1.0569 0.8855 0.2807  -0.1353 -0.0145 126 THR B C   
4613 O O   . THR B 126 ? 1.3539 1.1112 0.9557 0.2864  -0.1392 -0.0027 126 THR B O   
4614 C CB  . THR B 126 ? 1.2537 1.1904 0.9480 0.3159  -0.1550 -0.0387 126 THR B CB  
4615 O OG1 . THR B 126 ? 1.1892 1.2152 0.9428 0.3098  -0.1535 -0.0543 126 THR B OG1 
4616 C CG2 . THR B 126 ? 1.2211 1.1220 0.8738 0.3302  -0.1677 -0.0315 126 THR B CG2 
4617 N N   . SER B 127 ? 1.2606 1.0797 0.9199 0.2782  -0.1295 -0.0190 127 SER B N   
4618 C CA  . SER B 127 ? 1.2797 1.0220 0.9002 0.2746  -0.1275 -0.0105 127 SER B CA  
4619 C C   . SER B 127 ? 1.2774 0.9718 0.8835 0.2413  -0.1175 0.0059  127 SER B C   
4620 O O   . SER B 127 ? 1.3120 0.9325 0.8745 0.2414  -0.1180 0.0155  127 SER B O   
4621 C CB  . SER B 127 ? 1.2267 0.9840 0.8691 0.2676  -0.1207 -0.0184 127 SER B CB  
4622 O OG  . SER B 127 ? 1.1844 1.0076 0.8777 0.2441  -0.1095 -0.0226 127 SER B OG  
4623 N N   . ASP B 128 ? 1.0517 0.7867 0.6937 0.2127  -0.1076 0.0087  128 ASP B N   
4624 C CA  . ASP B 128 ? 1.0314 0.7327 0.6673 0.1809  -0.0963 0.0223  128 ASP B CA  
4625 C C   . ASP B 128 ? 1.1046 0.7819 0.7078 0.1899  -0.0998 0.0314  128 ASP B C   
4626 O O   . ASP B 128 ? 1.0615 0.7857 0.6799 0.1990  -0.1054 0.0263  128 ASP B O   
4627 C CB  . ASP B 128 ? 0.9789 0.7332 0.6640 0.1508  -0.0854 0.0200  128 ASP B CB  
4628 C CG  . ASP B 128 ? 1.0382 0.7672 0.7234 0.1190  -0.0733 0.0316  128 ASP B CG  
4629 O OD1 . ASP B 128 ? 1.1097 0.7808 0.7590 0.1166  -0.0707 0.0421  128 ASP B OD1 
4630 O OD2 . ASP B 128 ? 0.9680 0.7344 0.6886 0.0964  -0.0653 0.0300  128 ASP B OD2 
4631 N N   . PRO B 129 ? 1.2768 0.8807 0.8336 0.1869  -0.0961 0.0445  129 PRO B N   
4632 C CA  . PRO B 129 ? 1.2663 0.8400 0.7816 0.1996  -0.0990 0.0542  129 PRO B CA  
4633 C C   . PRO B 129 ? 1.2206 0.8296 0.7586 0.1779  -0.0901 0.0583  129 PRO B C   
4634 O O   . PRO B 129 ? 1.1898 0.7946 0.7015 0.1933  -0.0959 0.0616  129 PRO B O   
4635 C CB  . PRO B 129 ? 1.3235 0.8065 0.7867 0.1928  -0.0912 0.0687  129 PRO B CB  
4636 C CG  . PRO B 129 ? 1.2583 0.7366 0.7510 0.1625  -0.0804 0.0673  129 PRO B CG  
4637 C CD  . PRO B 129 ? 1.3324 0.8791 0.8753 0.1666  -0.0870 0.0512  129 PRO B CD  
4638 N N   . GLN B 130 ? 1.2596 0.9023 0.8428 0.1454  -0.0777 0.0570  130 GLN B N   
4639 C CA  . GLN B 130 ? 1.2391 0.9145 0.8429 0.1266  -0.0699 0.0595  130 GLN B CA  
4640 C C   . GLN B 130 ? 1.1555 0.9072 0.8119 0.1222  -0.0740 0.0459  130 GLN B C   
4641 O O   . GLN B 130 ? 1.1048 0.8843 0.7847 0.1021  -0.0666 0.0464  130 GLN B O   
4642 C CB  . GLN B 130 ? 1.2011 0.8502 0.8106 0.0922  -0.0510 0.0697  130 GLN B CB  
4643 C CG  . GLN B 130 ? 1.2846 0.8572 0.8478 0.0899  -0.0435 0.0824  130 GLN B CG  
4644 C CD  . GLN B 130 ? 1.3490 0.9052 0.9340 0.0581  -0.0298 0.0844  130 GLN B CD  
4645 O OE1 . GLN B 130 ? 1.3574 0.9248 0.9662 0.0555  -0.0349 0.0754  130 GLN B OE1 
4646 N NE2 . GLN B 130 ? 1.3917 0.9236 0.9695 0.0343  -0.0124 0.0951  130 GLN B NE2 
4647 N N   . CYS B 131 ? 1.0882 0.8729 0.7614 0.1412  -0.0848 0.0337  131 CYS B N   
4648 C CA  . CYS B 131 ? 1.0606 0.9165 0.7811 0.1368  -0.0870 0.0209  131 CYS B CA  
4649 C C   . CYS B 131 ? 1.0219 0.9062 0.7418 0.1461  -0.0958 0.0170  131 CYS B C   
4650 O O   . CYS B 131 ? 0.9970 0.8715 0.6887 0.1752  -0.1096 0.0145  131 CYS B O   
4651 C CB  . CYS B 131 ? 1.0045 0.8902 0.7414 0.1564  -0.0944 0.0084  131 CYS B CB  
4652 S SG  . CYS B 131 ? 1.0029 0.9736 0.7994 0.1457  -0.0916 -0.0066 131 CYS B SG  
4653 N N   . PRO B 132 ? 0.9124 0.8325 0.6618 0.1247  -0.0902 0.0144  132 PRO B N   
4654 C CA  . PRO B 132 ? 0.8906 0.8364 0.6390 0.1331  -0.1003 0.0086  132 PRO B CA  
4655 C C   . PRO B 132 ? 0.8972 0.8904 0.6627 0.1590  -0.1171 -0.0078 132 PRO B C   
4656 O O   . PRO B 132 ? 0.8675 0.8894 0.6600 0.1621  -0.1161 -0.0160 132 PRO B O   
4657 C CB  . PRO B 132 ? 0.8053 0.7829 0.5888 0.1031  -0.0905 0.0064  132 PRO B CB  
4658 C CG  . PRO B 132 ? 0.8466 0.7945 0.6317 0.0810  -0.0744 0.0168  132 PRO B CG  
4659 C CD  . PRO B 132 ? 0.8513 0.7829 0.6308 0.0930  -0.0756 0.0166  132 PRO B CD  
4660 N N   . PRO B 133 ? 1.1302 1.1321 0.8788 0.1798  -0.1329 -0.0137 133 PRO B N   
4661 C CA  . PRO B 133 ? 1.0818 1.1317 0.8478 0.2082  -0.1513 -0.0316 133 PRO B CA  
4662 C C   . PRO B 133 ? 1.0623 1.1865 0.8923 0.1923  -0.1478 -0.0477 133 PRO B C   
4663 O O   . PRO B 133 ? 1.1196 1.2839 0.9717 0.2115  -0.1555 -0.0614 133 PRO B O   
4664 C CB  . PRO B 133 ? 1.0878 1.1359 0.8268 0.2278  -0.1691 -0.0360 133 PRO B CB  
4665 C CG  . PRO B 133 ? 1.1030 1.0853 0.7944 0.2168  -0.1587 -0.0164 133 PRO B CG  
4666 C CD  . PRO B 133 ? 1.1303 1.0873 0.8321 0.1850  -0.1352 -0.0030 133 PRO B CD  
4667 N N   . ASP B 134 ? 0.8934 1.0358 0.7524 0.1585  -0.1352 -0.0467 134 ASP B N   
4668 C CA  . ASP B 134 ? 0.8139 1.0197 0.7289 0.1405  -0.1292 -0.0604 134 ASP B CA  
4669 C C   . ASP B 134 ? 0.8166 1.0173 0.7471 0.1230  -0.1102 -0.0543 134 ASP B C   
4670 O O   . ASP B 134 ? 0.8105 1.0491 0.7793 0.1005  -0.0994 -0.0605 134 ASP B O   
4671 C CB  . ASP B 134 ? 0.7551 0.9822 0.6905 0.1152  -0.1279 -0.0647 134 ASP B CB  
4672 C CG  . ASP B 134 ? 0.7704 0.9494 0.6842 0.0918  -0.1139 -0.0481 134 ASP B CG  
4673 O OD1 . ASP B 134 ? 0.7651 0.9079 0.6650 0.0859  -0.1014 -0.0353 134 ASP B OD1 
4674 O OD2 . ASP B 134 ? 0.7802 0.9596 0.6920 0.0804  -0.1167 -0.0495 134 ASP B OD2 
4675 N N   . GLY B 135 ? 0.6816 0.8326 0.5804 0.1318  -0.1057 -0.0423 135 GLY B N   
4676 C CA  . GLY B 135 ? 0.6431 0.7940 0.5534 0.1266  -0.0935 -0.0411 135 GLY B CA  
4677 C C   . GLY B 135 ? 0.6997 0.8249 0.6117 0.0972  -0.0770 -0.0303 135 GLY B C   
4678 O O   . GLY B 135 ? 0.6589 0.7856 0.5795 0.0931  -0.0676 -0.0307 135 GLY B O   
4679 N N   . ARG B 136 ? 0.6883 0.8328 0.8318 0.0463  0.0119  0.0886  136 ARG B N   
4680 C CA  . ARG B 136 ? 0.6638 0.7704 0.7802 0.0368  0.0158  0.0757  136 ARG B CA  
4681 C C   . ARG B 136 ? 0.6668 0.7676 0.7606 0.0294  0.0020  0.0663  136 ARG B C   
4682 O O   . ARG B 136 ? 0.6734 0.8031 0.7739 0.0273  -0.0119 0.0667  136 ARG B O   
4683 C CB  . ARG B 136 ? 0.6325 0.7417 0.7635 0.0237  0.0180  0.0682  136 ARG B CB  
4684 C CG  . ARG B 136 ? 0.6436 0.7767 0.7873 0.0077  0.0007  0.0571  136 ARG B CG  
4685 C CD  . ARG B 136 ? 0.6336 0.8153 0.8168 0.0062  -0.0075 0.0622  136 ARG B CD  
4686 N NE  . ARG B 136 ? 0.6403 0.8422 0.8371 -0.0114 -0.0232 0.0479  136 ARG B NE  
4687 C CZ  . ARG B 136 ? 0.6145 0.8609 0.8472 -0.0179 -0.0347 0.0462  136 ARG B CZ  
4688 N NH1 . ARG B 136 ? 0.5949 0.8745 0.8556 -0.0068 -0.0332 0.0596  136 ARG B NH1 
4689 N NH2 . ARG B 136 ? 0.5898 0.8483 0.8318 -0.0355 -0.0487 0.0294  136 ARG B NH2 
4690 N N   . TYR B 137 ? 0.5921 0.6572 0.6587 0.0268  0.0063  0.0577  137 TYR B N   
4691 C CA  . TYR B 137 ? 0.5791 0.6383 0.6278 0.0174  -0.0047 0.0456  137 TYR B CA  
4692 C C   . TYR B 137 ? 0.5914 0.6502 0.6445 0.0044  -0.0099 0.0328  137 TYR B C   
4693 O O   . TYR B 137 ? 0.5930 0.6382 0.6503 0.0036  -0.0010 0.0327  137 TYR B O   
4694 C CB  . TYR B 137 ? 0.5836 0.6087 0.6066 0.0203  0.0015  0.0414  137 TYR B CB  
4695 C CG  . TYR B 137 ? 0.6295 0.6457 0.6478 0.0320  0.0096  0.0532  137 TYR B CG  
4696 C CD1 . TYR B 137 ? 0.6404 0.6672 0.6540 0.0342  0.0050  0.0597  137 TYR B CD1 
4697 C CD2 . TYR B 137 ? 0.5981 0.5926 0.6146 0.0417  0.0235  0.0582  137 TYR B CD2 
4698 C CE1 . TYR B 137 ? 0.6709 0.6846 0.6804 0.0455  0.0146  0.0724  137 TYR B CE1 
4699 C CE2 . TYR B 137 ? 0.6594 0.6406 0.6723 0.0526  0.0324  0.0681  137 TYR B CE2 
4700 C CZ  . TYR B 137 ? 0.7028 0.6925 0.7133 0.0543  0.0282  0.0760  137 TYR B CZ  
4701 O OH  . TYR B 137 ? 0.6775 0.6492 0.6850 0.0656  0.0391  0.0876  137 TYR B OH  
4702 N N   . GLN B 138 ? 0.5917 0.6635 0.6424 -0.0047 -0.0230 0.0226  138 GLN B N   
4703 C CA  . GLN B 138 ? 0.6128 0.6789 0.6651 -0.0167 -0.0282 0.0086  138 GLN B CA  
4704 C C   . GLN B 138 ? 0.6192 0.6715 0.6486 -0.0195 -0.0338 -0.0031 138 GLN B C   
4705 O O   . GLN B 138 ? 0.5935 0.6589 0.6145 -0.0178 -0.0397 -0.0030 138 GLN B O   
4706 C CB  . GLN B 138 ? 0.5873 0.6858 0.6645 -0.0264 -0.0388 0.0040  138 GLN B CB  
4707 C CG  . GLN B 138 ? 0.5922 0.7210 0.6960 -0.0213 -0.0377 0.0172  138 GLN B CG  
4708 C CD  . GLN B 138 ? 0.6065 0.7632 0.7431 -0.0339 -0.0450 0.0107  138 GLN B CD  
4709 O OE1 . GLN B 138 ? 0.6068 0.7781 0.7719 -0.0335 -0.0377 0.0194  138 GLN B OE1 
4710 N NE2 . GLN B 138 ? 0.6149 0.7790 0.7494 -0.0459 -0.0585 -0.0058 138 GLN B NE2 
4711 N N   . TYR B 139 ? 0.5507 0.5771 0.5697 -0.0220 -0.0309 -0.0117 139 TYR B N   
4712 C CA  . TYR B 139 ? 0.5368 0.5503 0.5376 -0.0227 -0.0346 -0.0226 139 TYR B CA  
4713 C C   . TYR B 139 ? 0.5627 0.5674 0.5641 -0.0299 -0.0394 -0.0360 139 TYR B C   
4714 O O   . TYR B 139 ? 0.5846 0.5790 0.5947 -0.0326 -0.0356 -0.0349 139 TYR B O   
4715 C CB  . TYR B 139 ? 0.5565 0.5455 0.5420 -0.0152 -0.0271 -0.0206 139 TYR B CB  
4716 C CG  . TYR B 139 ? 0.5822 0.5723 0.5657 -0.0081 -0.0207 -0.0093 139 TYR B CG  
4717 C CD1 . TYR B 139 ? 0.6226 0.6253 0.6034 -0.0077 -0.0228 -0.0064 139 TYR B CD1 
4718 C CD2 . TYR B 139 ? 0.6192 0.5950 0.6018 -0.0009 -0.0109 -0.0012 139 TYR B CD2 
4719 C CE1 . TYR B 139 ? 0.6369 0.6355 0.6161 -0.0006 -0.0152 0.0052  139 TYR B CE1 
4720 C CE2 . TYR B 139 ? 0.5982 0.5705 0.5794 0.0064  -0.0038 0.0081  139 TYR B CE2 
4721 C CZ  . TYR B 139 ? 0.6439 0.6265 0.6244 0.0064  -0.0059 0.0117  139 TYR B CZ  
4722 O OH  . TYR B 139 ? 0.6501 0.6250 0.6296 0.0142  0.0027  0.0224  139 TYR B OH  
4723 N N   . ASN B 140 ? 0.5940 0.6021 0.5866 -0.0324 -0.0461 -0.0478 140 ASN B N   
4724 C CA  . ASN B 140 ? 0.5868 0.5819 0.5763 -0.0360 -0.0496 -0.0620 140 ASN B CA  
4725 C C   . ASN B 140 ? 0.5440 0.5154 0.5210 -0.0283 -0.0454 -0.0626 140 ASN B C   
4726 O O   . ASN B 140 ? 0.5438 0.5170 0.5123 -0.0243 -0.0449 -0.0634 140 ASN B O   
4727 C CB  . ASN B 140 ? 0.5479 0.5606 0.5325 -0.0397 -0.0570 -0.0737 140 ASN B CB  
4728 C CG  . ASN B 140 ? 0.5875 0.5880 0.5684 -0.0416 -0.0600 -0.0902 140 ASN B CG  
4729 O OD1 . ASN B 140 ? 0.5849 0.5659 0.5604 -0.0360 -0.0570 -0.0927 140 ASN B OD1 
4730 N ND2 . ASN B 140 ? 0.5991 0.6127 0.5821 -0.0484 -0.0668 -0.1027 140 ASN B ND2 
4731 N N   . THR B 141 ? 0.5105 0.4603 0.4865 -0.0259 -0.0421 -0.0616 141 THR B N   
4732 C CA  . THR B 141 ? 0.4735 0.4041 0.4357 -0.0164 -0.0385 -0.0580 141 THR B CA  
4733 C C   . THR B 141 ? 0.4919 0.4033 0.4470 -0.0117 -0.0412 -0.0655 141 THR B C   
4734 O O   . THR B 141 ? 0.4992 0.3971 0.4583 -0.0136 -0.0387 -0.0643 141 THR B O   
4735 C CB  . THR B 141 ? 0.5374 0.4594 0.4987 -0.0130 -0.0297 -0.0444 141 THR B CB  
4736 O OG1 . THR B 141 ? 0.4930 0.4339 0.4632 -0.0153 -0.0274 -0.0371 141 THR B OG1 
4737 C CG2 . THR B 141 ? 0.5469 0.4493 0.4886 -0.0020 -0.0268 -0.0422 141 THR B CG2 
4738 N N   . ASP B 142 ? 0.5698 0.4801 0.5166 -0.0053 -0.0458 -0.0729 142 ASP B N   
4739 C CA  . ASP B 142 ? 0.6357 0.5284 0.5741 0.0038  -0.0489 -0.0773 142 ASP B CA  
4740 C C   . ASP B 142 ? 0.6715 0.5468 0.5938 0.0134  -0.0459 -0.0679 142 ASP B C   
4741 O O   . ASP B 142 ? 0.6684 0.5484 0.5851 0.0146  -0.0447 -0.0652 142 ASP B O   
4742 C CB  . ASP B 142 ? 0.6018 0.5061 0.5420 0.0075  -0.0558 -0.0897 142 ASP B CB  
4743 C CG  . ASP B 142 ? 0.6322 0.5525 0.5835 0.0001  -0.0570 -0.0999 142 ASP B CG  
4744 O OD1 . ASP B 142 ? 0.6315 0.5496 0.5877 -0.0065 -0.0556 -0.1008 142 ASP B OD1 
4745 O OD2 . ASP B 142 ? 0.6278 0.5637 0.5831 0.0008  -0.0592 -0.1082 142 ASP B OD2 
4746 N N   . VAL B 143 ? 0.5956 0.4486 0.5085 0.0207  -0.0437 -0.0628 143 VAL B N   
4747 C CA  . VAL B 143 ? 0.6326 0.4677 0.5235 0.0330  -0.0417 -0.0545 143 VAL B CA  
4748 C C   . VAL B 143 ? 0.6481 0.4710 0.5279 0.0463  -0.0494 -0.0587 143 VAL B C   
4749 O O   . VAL B 143 ? 0.6333 0.4494 0.5221 0.0461  -0.0502 -0.0620 143 VAL B O   
4750 C CB  . VAL B 143 ? 0.6181 0.4357 0.5036 0.0324  -0.0284 -0.0389 143 VAL B CB  
4751 C CG1 . VAL B 143 ? 0.6355 0.4680 0.5324 0.0230  -0.0209 -0.0336 143 VAL B CG1 
4752 C CG2 . VAL B 143 ? 0.6244 0.4281 0.5214 0.0276  -0.0235 -0.0361 143 VAL B CG2 
4753 N N   . VAL B 144 ? 0.6484 0.4698 0.5095 0.0585  -0.0563 -0.0601 144 VAL B N   
4754 C CA  . VAL B 144 ? 0.6523 0.4640 0.4996 0.0751  -0.0653 -0.0619 144 VAL B CA  
4755 C C   . VAL B 144 ? 0.7187 0.5095 0.5338 0.0889  -0.0624 -0.0497 144 VAL B C   
4756 O O   . VAL B 144 ? 0.7145 0.5100 0.5161 0.0896  -0.0629 -0.0508 144 VAL B O   
4757 C CB  . VAL B 144 ? 0.6678 0.5033 0.5236 0.0787  -0.0801 -0.0779 144 VAL B CB  
4758 C CG1 . VAL B 144 ? 0.6511 0.4796 0.4957 0.0982  -0.0906 -0.0788 144 VAL B CG1 
4759 C CG2 . VAL B 144 ? 0.6167 0.4738 0.5016 0.0650  -0.0799 -0.0889 144 VAL B CG2 
4760 N N   . PHE B 145 ? 0.7121 0.4786 0.5130 0.1011  -0.0591 -0.0387 145 PHE B N   
4761 C CA  . PHE B 145 ? 0.7187 0.4625 0.4833 0.1182  -0.0557 -0.0247 145 PHE B CA  
4762 C C   . PHE B 145 ? 0.7508 0.4923 0.5003 0.1390  -0.0709 -0.0275 145 PHE B C   
4763 O O   . PHE B 145 ? 0.7440 0.4834 0.5098 0.1420  -0.0745 -0.0303 145 PHE B O   
4764 C CB  . PHE B 145 ? 0.7307 0.4446 0.4901 0.1165  -0.0361 -0.0050 145 PHE B CB  
4765 C CG  . PHE B 145 ? 0.7357 0.4553 0.5132 0.0975  -0.0214 -0.0013 145 PHE B CG  
4766 C CD1 . PHE B 145 ? 0.7355 0.4552 0.4958 0.0986  -0.0130 0.0052  145 PHE B CD1 
4767 C CD2 . PHE B 145 ? 0.7165 0.4439 0.5286 0.0794  -0.0172 -0.0060 145 PHE B CD2 
4768 C CE1 . PHE B 145 ? 0.7280 0.4562 0.5082 0.0832  0.0001  0.0091  145 PHE B CE1 
4769 C CE2 . PHE B 145 ? 0.6978 0.4359 0.5289 0.0632  -0.0064 -0.0030 145 PHE B CE2 
4770 C CZ  . PHE B 145 ? 0.7013 0.4405 0.5182 0.0655  0.0024  0.0053  145 PHE B CZ  
4771 N N   . ASP B 146 ? 0.7511 0.4939 0.4691 0.1546  -0.0805 -0.0275 146 ASP B N   
4772 C CA  . ASP B 146 ? 0.7605 0.5072 0.4650 0.1762  -0.0982 -0.0308 146 ASP B CA  
4773 C C   . ASP B 146 ? 0.7789 0.4903 0.4572 0.1947  -0.0895 -0.0089 146 ASP B C   
4774 O O   . ASP B 146 ? 0.8001 0.4843 0.4737 0.1885  -0.0689 0.0078  146 ASP B O   
4775 C CB  . ASP B 146 ? 0.7755 0.5416 0.4589 0.1851  -0.1153 -0.0431 146 ASP B CB  
4776 C CG  . ASP B 146 ? 0.8248 0.5701 0.4622 0.1950  -0.1074 -0.0309 146 ASP B CG  
4777 O OD1 . ASP B 146 ? 0.8572 0.5716 0.4737 0.2011  -0.0896 -0.0091 146 ASP B OD1 
4778 O OD2 . ASP B 146 ? 0.7704 0.5308 0.3935 0.1963  -0.1186 -0.0446 146 ASP B OD2 
4779 N N   . SER B 147 ? 0.8864 0.5988 0.5502 0.2180  -0.1051 -0.0083 147 SER B N   
4780 C CA  . SER B 147 ? 0.9486 0.6256 0.5862 0.2392  -0.0978 0.0141  147 SER B CA  
4781 C C   . SER B 147 ? 1.0026 0.6527 0.5924 0.2499  -0.0852 0.0346  147 SER B C   
4782 O O   . SER B 147 ? 1.0483 0.6635 0.6138 0.2660  -0.0738 0.0575  147 SER B O   
4783 C CB  . SER B 147 ? 0.9720 0.6612 0.6034 0.2652  -0.1201 0.0099  147 SER B CB  
4784 O OG  . SER B 147 ? 1.0107 0.7295 0.6238 0.2741  -0.1412 -0.0033 147 SER B OG  
4785 N N   . GLN B 148 ? 1.1094 0.7735 0.6823 0.2439  -0.0867 0.0272  148 GLN B N   
4786 C CA  . GLN B 148 ? 1.1307 0.7696 0.6599 0.2517  -0.0702 0.0458  148 GLN B CA  
4787 C C   . GLN B 148 ? 1.1335 0.7599 0.6818 0.2282  -0.0433 0.0541  148 GLN B C   
4788 O O   . GLN B 148 ? 1.1144 0.7197 0.6322 0.2328  -0.0246 0.0712  148 GLN B O   
4789 C CB  . GLN B 148 ? 1.0908 0.7489 0.5867 0.2607  -0.0854 0.0326  148 GLN B CB  
4790 C CG  . GLN B 148 ? 1.2690 0.9290 0.7224 0.2920  -0.1070 0.0343  148 GLN B CG  
4791 C CD  . GLN B 148 ? 1.2773 0.9655 0.7619 0.2971  -0.1327 0.0180  148 GLN B CD  
4792 O OE1 . GLN B 148 ? 1.2683 0.9907 0.7886 0.2807  -0.1465 -0.0073 148 GLN B OE1 
4793 N NE2 . GLN B 148 ? 1.2555 0.9299 0.7265 0.3215  -0.1387 0.0329  148 GLN B NE2 
4794 N N   . GLY B 149 ? 0.8446 0.4865 0.4424 0.2040  -0.0411 0.0421  149 GLY B N   
4795 C CA  . GLY B 149 ? 0.8203 0.4590 0.4414 0.1815  -0.0200 0.0467  149 GLY B CA  
4796 C C   . GLY B 149 ? 0.7899 0.4527 0.4164 0.1692  -0.0217 0.0330  149 GLY B C   
4797 O O   . GLY B 149 ? 0.7902 0.4516 0.4313 0.1543  -0.0037 0.0390  149 GLY B O   
4798 N N   . LYS B 150 ? 0.8705 0.5555 0.4883 0.1748  -0.0423 0.0146  150 LYS B N   
4799 C CA  . LYS B 150 ? 0.8928 0.5969 0.5181 0.1625  -0.0430 0.0007  150 LYS B CA  
4800 C C   . LYS B 150 ? 0.8196 0.5464 0.4943 0.1402  -0.0457 -0.0121 150 LYS B C   
4801 O O   . LYS B 150 ? 0.7943 0.5312 0.4919 0.1378  -0.0564 -0.0194 150 LYS B O   
4802 C CB  . LYS B 150 ? 0.8708 0.5883 0.4698 0.1748  -0.0634 -0.0160 150 LYS B CB  
4803 C CG  . LYS B 150 ? 0.8611 0.5878 0.4580 0.1654  -0.0603 -0.0284 150 LYS B CG  
4804 C CD  . LYS B 150 ? 0.8403 0.5826 0.4203 0.1732  -0.0832 -0.0503 150 LYS B CD  
4805 C CE  . LYS B 150 ? 1.0676 0.7927 0.5896 0.1928  -0.0818 -0.0475 150 LYS B CE  
4806 N NZ  . LYS B 150 ? 1.0234 0.7349 0.5007 0.2188  -0.0894 -0.0353 150 LYS B NZ  
4807 N N   . LEU B 151 ? 0.8195 0.5541 0.5088 0.1256  -0.0349 -0.0140 151 LEU B N   
4808 C CA  . LEU B 151 ? 0.7876 0.5445 0.5180 0.1062  -0.0372 -0.0248 151 LEU B CA  
4809 C C   . LEU B 151 ? 0.7765 0.5539 0.5109 0.1051  -0.0546 -0.0451 151 LEU B C   
4810 O O   . LEU B 151 ? 0.7803 0.5591 0.5024 0.1052  -0.0540 -0.0514 151 LEU B O   
4811 C CB  . LEU B 151 ? 0.7680 0.5260 0.5118 0.0939  -0.0196 -0.0171 151 LEU B CB  
4812 C CG  . LEU B 151 ? 0.7617 0.5435 0.5373 0.0780  -0.0232 -0.0286 151 LEU B CG  
4813 C CD1 . LEU B 151 ? 0.6946 0.4878 0.5018 0.0662  -0.0259 -0.0302 151 LEU B CD1 
4814 C CD2 . LEU B 151 ? 0.7320 0.5155 0.5132 0.0722  -0.0082 -0.0219 151 LEU B CD2 
4815 N N   . VAL B 152 ? 0.7161 0.5095 0.4710 0.1027  -0.0684 -0.0562 152 VAL B N   
4816 C CA  . VAL B 152 ? 0.6939 0.5087 0.4573 0.1008  -0.0844 -0.0756 152 VAL B CA  
4817 C C   . VAL B 152 ? 0.7041 0.5395 0.5047 0.0822  -0.0828 -0.0843 152 VAL B C   
4818 O O   . VAL B 152 ? 0.6866 0.5387 0.4986 0.0769  -0.0918 -0.0993 152 VAL B O   
4819 C CB  . VAL B 152 ? 0.6898 0.5130 0.4484 0.1150  -0.1028 -0.0834 152 VAL B CB  
4820 C CG1 . VAL B 152 ? 0.6901 0.4934 0.4053 0.1367  -0.1062 -0.0740 152 VAL B CG1 
4821 C CG2 . VAL B 152 ? 0.6504 0.4781 0.4340 0.1133  -0.1029 -0.0810 152 VAL B CG2 
4822 N N   . ALA B 153 ? 0.6573 0.4922 0.4765 0.0716  -0.0715 -0.0756 153 ALA B N   
4823 C CA  . ALA B 153 ? 0.6490 0.5040 0.4970 0.0562  -0.0705 -0.0832 153 ALA B CA  
4824 C C   . ALA B 153 ? 0.6159 0.4702 0.4775 0.0455  -0.0576 -0.0724 153 ALA B C   
4825 O O   . ALA B 153 ? 0.6340 0.4780 0.4950 0.0470  -0.0527 -0.0638 153 ALA B O   
4826 C CB  . ALA B 153 ? 0.5708 0.4446 0.4383 0.0553  -0.0815 -0.0954 153 ALA B CB  
4827 N N   . ARG B 154 ? 0.6246 0.4899 0.4995 0.0351  -0.0525 -0.0730 154 ARG B N   
4828 C CA  . ARG B 154 ? 0.5960 0.4680 0.4862 0.0253  -0.0434 -0.0644 154 ARG B CA  
4829 C C   . ARG B 154 ? 0.6039 0.4956 0.5124 0.0155  -0.0448 -0.0704 154 ARG B C   
4830 O O   . ARG B 154 ? 0.5443 0.4384 0.4533 0.0139  -0.0446 -0.0744 154 ARG B O   
4831 C CB  . ARG B 154 ? 0.6463 0.5084 0.5287 0.0269  -0.0319 -0.0525 154 ARG B CB  
4832 C CG  . ARG B 154 ? 0.6287 0.5012 0.5291 0.0186  -0.0237 -0.0427 154 ARG B CG  
4833 C CD  . ARG B 154 ? 0.6046 0.4735 0.5024 0.0212  -0.0128 -0.0332 154 ARG B CD  
4834 N NE  . ARG B 154 ? 0.6285 0.5014 0.5275 0.0202  -0.0134 -0.0379 154 ARG B NE  
4835 C CZ  . ARG B 154 ? 0.6715 0.5353 0.5635 0.0252  -0.0048 -0.0340 154 ARG B CZ  
4836 N NH1 . ARG B 154 ? 0.6573 0.5101 0.5394 0.0324  0.0054  -0.0253 154 ARG B NH1 
4837 N NH2 . ARG B 154 ? 0.6090 0.4730 0.5044 0.0230  -0.0048 -0.0389 154 ARG B NH2 
4838 N N   . TYR B 155 ? 0.6002 0.5048 0.5227 0.0088  -0.0455 -0.0713 155 TYR B N   
4839 C CA  . TYR B 155 ? 0.5668 0.4901 0.5024 0.0010  -0.0454 -0.0753 155 TYR B CA  
4840 C C   . TYR B 155 ? 0.5768 0.5110 0.5204 -0.0056 -0.0411 -0.0676 155 TYR B C   
4841 O O   . TYR B 155 ? 0.5574 0.4924 0.5043 -0.0076 -0.0429 -0.0682 155 TYR B O   
4842 C CB  . TYR B 155 ? 0.5645 0.4986 0.5074 0.0007  -0.0520 -0.0880 155 TYR B CB  
4843 C CG  . TYR B 155 ? 0.5698 0.5236 0.5240 -0.0074 -0.0489 -0.0900 155 TYR B CG  
4844 C CD1 . TYR B 155 ? 0.5685 0.5288 0.5274 -0.0118 -0.0438 -0.0879 155 TYR B CD1 
4845 C CD2 . TYR B 155 ? 0.5741 0.5375 0.5319 -0.0102 -0.0498 -0.0937 155 TYR B CD2 
4846 C CE1 . TYR B 155 ? 0.5905 0.5672 0.5560 -0.0179 -0.0388 -0.0868 155 TYR B CE1 
4847 C CE2 . TYR B 155 ? 0.5540 0.5354 0.5163 -0.0158 -0.0464 -0.0951 155 TYR B CE2 
4848 C CZ  . TYR B 155 ? 0.5788 0.5670 0.5441 -0.0191 -0.0404 -0.0902 155 TYR B CZ  
4849 O OH  . TYR B 155 ? 0.5656 0.5702 0.5319 -0.0235 -0.0349 -0.0887 155 TYR B OH  
4850 N N   . HIS B 156 ? 0.5813 0.5235 0.5285 -0.0087 -0.0360 -0.0607 156 HIS B N   
4851 C CA  . HIS B 156 ? 0.6096 0.5675 0.5639 -0.0132 -0.0341 -0.0531 156 HIS B CA  
4852 C C   . HIS B 156 ? 0.6023 0.5773 0.5593 -0.0177 -0.0363 -0.0590 156 HIS B C   
4853 O O   . HIS B 156 ? 0.6094 0.5864 0.5665 -0.0185 -0.0327 -0.0595 156 HIS B O   
4854 C CB  . HIS B 156 ? 0.6147 0.5720 0.5701 -0.0107 -0.0269 -0.0401 156 HIS B CB  
4855 C CG  . HIS B 156 ? 0.6335 0.5763 0.5858 -0.0054 -0.0220 -0.0337 156 HIS B CG  
4856 N ND1 . HIS B 156 ? 0.6235 0.5531 0.5703 0.0002  -0.0147 -0.0285 156 HIS B ND1 
4857 C CD2 . HIS B 156 ? 0.6149 0.5530 0.5686 -0.0046 -0.0216 -0.0315 156 HIS B CD2 
4858 C CE1 . HIS B 156 ? 0.6701 0.5893 0.6129 0.0053  -0.0098 -0.0235 156 HIS B CE1 
4859 N NE2 . HIS B 156 ? 0.6333 0.5576 0.5809 0.0021  -0.0133 -0.0241 156 HIS B NE2 
4860 N N   . LYS B 157 ? 0.5960 0.5827 0.5552 -0.0213 -0.0411 -0.0637 157 LYS B N   
4861 C CA  . LYS B 157 ? 0.5931 0.5956 0.5505 -0.0243 -0.0424 -0.0711 157 LYS B CA  
4862 C C   . LYS B 157 ? 0.6131 0.6278 0.5675 -0.0246 -0.0368 -0.0605 157 LYS B C   
4863 O O   . LYS B 157 ? 0.6135 0.6357 0.5678 -0.0236 -0.0365 -0.0489 157 LYS B O   
4864 C CB  . LYS B 157 ? 0.5676 0.5796 0.5257 -0.0281 -0.0488 -0.0786 157 LYS B CB  
4865 C CG  . LYS B 157 ? 0.5651 0.5914 0.5172 -0.0297 -0.0498 -0.0895 157 LYS B CG  
4866 C CD  . LYS B 157 ? 0.5949 0.6282 0.5466 -0.0342 -0.0571 -0.1000 157 LYS B CD  
4867 C CE  . LYS B 157 ? 0.5704 0.6182 0.5114 -0.0346 -0.0575 -0.1124 157 LYS B CE  
4868 N NZ  . LYS B 157 ? 0.5837 0.6327 0.5246 -0.0394 -0.0653 -0.1275 157 LYS B NZ  
4869 N N   . GLN B 158 ? 0.5375 0.5549 0.4910 -0.0254 -0.0315 -0.0635 158 GLN B N   
4870 C CA  . GLN B 158 ? 0.5745 0.5983 0.5247 -0.0255 -0.0230 -0.0514 158 GLN B CA  
4871 C C   . GLN B 158 ? 0.6076 0.6521 0.5468 -0.0256 -0.0235 -0.0490 158 GLN B C   
4872 O O   . GLN B 158 ? 0.6043 0.6564 0.5368 -0.0225 -0.0214 -0.0345 158 GLN B O   
4873 C CB  . GLN B 158 ? 0.5872 0.6052 0.5441 -0.0282 -0.0149 -0.0552 158 GLN B CB  
4874 C CG  . GLN B 158 ? 0.5893 0.6096 0.5438 -0.0293 -0.0027 -0.0414 158 GLN B CG  
4875 C CD  . GLN B 158 ? 0.6823 0.6859 0.6381 -0.0265 0.0021  -0.0275 158 GLN B CD  
4876 O OE1 . GLN B 158 ? 0.6527 0.6438 0.6113 -0.0241 -0.0030 -0.0297 158 GLN B OE1 
4877 N NE2 . GLN B 158 ? 0.6797 0.6813 0.6322 -0.0256 0.0133  -0.0123 158 GLN B NE2 
4878 N N   . ASN B 159 ? 0.5757 0.6296 0.5114 -0.0274 -0.0265 -0.0632 159 ASN B N   
4879 C CA  . ASN B 159 ? 0.5541 0.6273 0.4748 -0.0268 -0.0258 -0.0639 159 ASN B CA  
4880 C C   . ASN B 159 ? 0.5673 0.6492 0.4835 -0.0278 -0.0386 -0.0737 159 ASN B C   
4881 O O   . ASN B 159 ? 0.5463 0.6267 0.4635 -0.0297 -0.0428 -0.0910 159 ASN B O   
4882 C CB  . ASN B 159 ? 0.5551 0.6333 0.4750 -0.0278 -0.0177 -0.0744 159 ASN B CB  
4883 C CG  . ASN B 159 ? 0.6118 0.6830 0.5425 -0.0296 -0.0048 -0.0666 159 ASN B CG  
4884 O OD1 . ASN B 159 ? 0.7034 0.7800 0.6267 -0.0295 0.0066  -0.0540 159 ASN B OD1 
4885 N ND2 . ASN B 159 ? 0.5641 0.6232 0.5123 -0.0314 -0.0065 -0.0744 159 ASN B ND2 
4886 N N   . LEU B 160 ? 0.5792 0.6714 0.4924 -0.0265 -0.0447 -0.0632 160 LEU B N   
4887 C CA  . LEU B 160 ? 0.5644 0.6684 0.4780 -0.0296 -0.0577 -0.0729 160 LEU B CA  
4888 C C   . LEU B 160 ? 0.6272 0.7503 0.5207 -0.0294 -0.0617 -0.0840 160 LEU B C   
4889 O O   . LEU B 160 ? 0.5825 0.7180 0.4579 -0.0243 -0.0560 -0.0745 160 LEU B O   
4890 C CB  . LEU B 160 ? 0.5580 0.6725 0.4791 -0.0277 -0.0633 -0.0582 160 LEU B CB  
4891 C CG  . LEU B 160 ? 0.5961 0.6919 0.5343 -0.0265 -0.0578 -0.0473 160 LEU B CG  
4892 C CD1 . LEU B 160 ? 0.5694 0.6785 0.5179 -0.0230 -0.0619 -0.0328 160 LEU B CD1 
4893 C CD2 . LEU B 160 ? 0.5795 0.6568 0.5291 -0.0317 -0.0593 -0.0606 160 LEU B CD2 
4894 N N   . PHE B 161 ? 0.7299 0.8530 0.6251 -0.0346 -0.0700 -0.1044 161 PHE B N   
4895 C CA  . PHE B 161 ? 0.6805 0.8206 0.5555 -0.0348 -0.0757 -0.1195 161 PHE B CA  
4896 C C   . PHE B 161 ? 0.7427 0.9083 0.6116 -0.0352 -0.0894 -0.1155 161 PHE B C   
4897 O O   . PHE B 161 ? 0.6989 0.8674 0.5870 -0.0376 -0.0958 -0.1066 161 PHE B O   
4898 C CB  . PHE B 161 ? 0.6867 0.8133 0.5682 -0.0403 -0.0795 -0.1444 161 PHE B CB  
4899 C CG  . PHE B 161 ? 0.7619 0.8992 0.6205 -0.0389 -0.0806 -0.1637 161 PHE B CG  
4900 C CD1 . PHE B 161 ? 0.7481 0.8898 0.5887 -0.0319 -0.0678 -0.1620 161 PHE B CD1 
4901 C CD2 . PHE B 161 ? 0.7693 0.9122 0.6249 -0.0452 -0.0937 -0.1847 161 PHE B CD2 
4902 C CE1 . PHE B 161 ? 0.7295 0.8808 0.5466 -0.0293 -0.0669 -0.1803 161 PHE B CE1 
4903 C CE2 . PHE B 161 ? 0.7747 0.9258 0.6059 -0.0433 -0.0946 -0.2052 161 PHE B CE2 
4904 C CZ  . PHE B 161 ? 0.7730 0.9282 0.5833 -0.0344 -0.0807 -0.2025 161 PHE B CZ  
4905 N N   . MET B 162 ? 0.7636 0.9499 0.6054 -0.0318 -0.0941 -0.1230 162 MET B N   
4906 C CA  . MET B 162 ? 0.7734 0.9885 0.6081 -0.0316 -0.1110 -0.1232 162 MET B CA  
4907 C C   . MET B 162 ? 0.7802 0.9943 0.6422 -0.0436 -0.1245 -0.1402 162 MET B C   
4908 O O   . MET B 162 ? 0.7671 0.9592 0.6401 -0.0511 -0.1220 -0.1584 162 MET B O   
4909 C CB  . MET B 162 ? 0.8053 1.0412 0.6023 -0.0264 -0.1154 -0.1345 162 MET B CB  
4910 C CG  . MET B 162 ? 0.8634 1.1047 0.6564 -0.0350 -0.1293 -0.1674 162 MET B CG  
4911 S SD  . MET B 162 ? 0.9762 1.2449 0.7177 -0.0270 -0.1362 -0.1820 162 MET B SD  
4912 C CE  . MET B 162 ? 0.8952 1.2015 0.6215 -0.0164 -0.1497 -0.1562 162 MET B CE  
4913 N N   . GLY B 163 ? 0.6911 0.9275 0.5679 -0.0449 -0.1372 -0.1320 163 GLY B N   
4914 C CA  . GLY B 163 ? 0.6574 0.8939 0.5670 -0.0577 -0.1473 -0.1446 163 GLY B CA  
4915 C C   . GLY B 163 ? 0.6770 0.8879 0.6174 -0.0612 -0.1364 -0.1326 163 GLY B C   
4916 O O   . GLY B 163 ? 0.6529 0.8588 0.6208 -0.0726 -0.1409 -0.1426 163 GLY B O   
4917 N N   . GLU B 164 ? 0.6671 0.8598 0.6035 -0.0526 -0.1214 -0.1131 164 GLU B N   
4918 C CA  . GLU B 164 ? 0.7022 0.8740 0.6641 -0.0542 -0.1125 -0.1013 164 GLU B CA  
4919 C C   . GLU B 164 ? 0.7110 0.8989 0.6838 -0.0469 -0.1119 -0.0779 164 GLU B C   
4920 O O   . GLU B 164 ? 0.6662 0.8358 0.6424 -0.0408 -0.0995 -0.0619 164 GLU B O   
4921 C CB  . GLU B 164 ? 0.6636 0.8030 0.6178 -0.0503 -0.0977 -0.0986 164 GLU B CB  
4922 C CG  . GLU B 164 ? 0.6660 0.7879 0.6141 -0.0550 -0.0968 -0.1202 164 GLU B CG  
4923 C CD  . GLU B 164 ? 0.6926 0.7853 0.6413 -0.0510 -0.0847 -0.1174 164 GLU B CD  
4924 O OE1 . GLU B 164 ? 0.6994 0.7713 0.6636 -0.0539 -0.0822 -0.1177 164 GLU B OE1 
4925 O OE2 . GLU B 164 ? 0.6973 0.7892 0.6314 -0.0446 -0.0775 -0.1142 164 GLU B OE2 
4926 N N   . ASN B 165 ? 0.7934 1.0161 0.7731 -0.0469 -0.1258 -0.0769 165 ASN B N   
4927 C CA  . ASN B 165 ? 0.8208 1.0629 0.8098 -0.0366 -0.1261 -0.0539 165 ASN B CA  
4928 C C   . ASN B 165 ? 0.8136 1.0499 0.8373 -0.0394 -0.1201 -0.0449 165 ASN B C   
4929 O O   . ASN B 165 ? 0.8112 1.0593 0.8444 -0.0290 -0.1171 -0.0252 165 ASN B O   
4930 C CB  . ASN B 165 ? 0.8622 1.1483 0.8455 -0.0330 -0.1451 -0.0557 165 ASN B CB  
4931 C CG  . ASN B 165 ? 0.9209 1.2348 0.9397 -0.0440 -0.1599 -0.0669 165 ASN B CG  
4932 O OD1 . ASN B 165 ? 0.8923 1.2015 0.9224 -0.0595 -0.1657 -0.0903 165 ASN B OD1 
4933 N ND2 . ASN B 165 ? 0.9709 1.3139 1.0105 -0.0360 -0.1652 -0.0502 165 ASN B ND2 
4934 N N   . GLN B 166 ? 0.6266 0.8438 0.6684 -0.0518 -0.1166 -0.0578 166 GLN B N   
4935 C CA  . GLN B 166 ? 0.6047 0.8113 0.6751 -0.0540 -0.1067 -0.0483 166 GLN B CA  
4936 C C   . GLN B 166 ? 0.5874 0.7603 0.6459 -0.0444 -0.0891 -0.0338 166 GLN B C   
4937 O O   . GLN B 166 ? 0.5702 0.7349 0.6462 -0.0423 -0.0791 -0.0231 166 GLN B O   
4938 C CB  . GLN B 166 ? 0.5940 0.7875 0.6842 -0.0701 -0.1069 -0.0654 166 GLN B CB  
4939 C CG  . GLN B 166 ? 0.5825 0.7371 0.6528 -0.0734 -0.1001 -0.0780 166 GLN B CG  
4940 C CD  . GLN B 166 ? 0.6314 0.7931 0.6849 -0.0791 -0.1123 -0.0998 166 GLN B CD  
4941 O OE1 . GLN B 166 ? 0.5994 0.7876 0.6373 -0.0741 -0.1222 -0.1006 166 GLN B OE1 
4942 N NE2 . GLN B 166 ? 0.6047 0.7416 0.6595 -0.0880 -0.1105 -0.1170 166 GLN B NE2 
4943 N N   . PHE B 167 ? 0.6172 0.7721 0.6475 -0.0389 -0.0848 -0.0344 167 PHE B N   
4944 C CA  . PHE B 167 ? 0.5682 0.6915 0.5867 -0.0323 -0.0707 -0.0263 167 PHE B CA  
4945 C C   . PHE B 167 ? 0.6078 0.7344 0.6123 -0.0204 -0.0658 -0.0103 167 PHE B C   
4946 O O   . PHE B 167 ? 0.6308 0.7778 0.6234 -0.0169 -0.0724 -0.0077 167 PHE B O   
4947 C CB  . PHE B 167 ? 0.5543 0.6546 0.5568 -0.0367 -0.0691 -0.0413 167 PHE B CB  
4948 C CG  . PHE B 167 ? 0.5795 0.6660 0.5934 -0.0459 -0.0702 -0.0543 167 PHE B CG  
4949 C CD1 . PHE B 167 ? 0.5696 0.6418 0.5986 -0.0465 -0.0626 -0.0473 167 PHE B CD1 
4950 C CD2 . PHE B 167 ? 0.5796 0.6642 0.5876 -0.0528 -0.0769 -0.0729 167 PHE B CD2 
4951 C CE1 . PHE B 167 ? 0.6028 0.6586 0.6413 -0.0543 -0.0612 -0.0564 167 PHE B CE1 
4952 C CE2 . PHE B 167 ? 0.5914 0.6582 0.6105 -0.0606 -0.0764 -0.0838 167 PHE B CE2 
4953 C CZ  . PHE B 167 ? 0.6187 0.6703 0.6532 -0.0615 -0.0682 -0.0742 167 PHE B CZ  
4954 N N   . ASN B 168 ? 0.6161 0.7188 0.6191 -0.0142 -0.0532 -0.0004 168 ASN B N   
4955 C CA  . ASN B 168 ? 0.6216 0.7163 0.6124 -0.0045 -0.0449 0.0134  168 ASN B CA  
4956 C C   . ASN B 168 ? 0.6559 0.7266 0.6305 -0.0073 -0.0387 0.0053  168 ASN B C   
4957 O O   . ASN B 168 ? 0.6524 0.7105 0.6262 -0.0140 -0.0400 -0.0090 168 ASN B O   
4958 C CB  . ASN B 168 ? 0.6494 0.7321 0.6509 0.0041  -0.0344 0.0274  168 ASN B CB  
4959 C CG  . ASN B 168 ? 0.6507 0.7618 0.6726 0.0095  -0.0389 0.0381  168 ASN B CG  
4960 O OD1 . ASN B 168 ? 0.6590 0.7739 0.7000 0.0065  -0.0378 0.0363  168 ASN B OD1 
4961 N ND2 . ASN B 168 ? 0.6350 0.7674 0.6537 0.0180  -0.0434 0.0501  168 ASN B ND2 
4962 N N   . VAL B 169 ? 0.6783 0.7435 0.6420 -0.0018 -0.0314 0.0153  169 VAL B N   
4963 C CA  . VAL B 169 ? 0.6718 0.7178 0.6257 -0.0051 -0.0238 0.0092  169 VAL B CA  
4964 C C   . VAL B 169 ? 0.6632 0.6822 0.6214 -0.0017 -0.0131 0.0143  169 VAL B C   
4965 O O   . VAL B 169 ? 0.6622 0.6783 0.6244 0.0063  -0.0077 0.0288  169 VAL B O   
4966 C CB  . VAL B 169 ? 0.6670 0.7232 0.6070 -0.0029 -0.0202 0.0169  169 VAL B CB  
4967 C CG1 . VAL B 169 ? 0.6939 0.7346 0.6298 -0.0081 -0.0112 0.0098  169 VAL B CG1 
4968 C CG2 . VAL B 169 ? 0.6204 0.7041 0.5521 -0.0047 -0.0319 0.0103  169 VAL B CG2 
4969 N N   . PRO B 170 ? 0.7290 0.7292 0.6869 -0.0065 -0.0109 0.0018  170 PRO B N   
4970 C CA  . PRO B 170 ? 0.7373 0.7119 0.6964 -0.0038 -0.0018 0.0037  170 PRO B CA  
4971 C C   . PRO B 170 ? 0.7687 0.7356 0.7261 -0.0019 0.0088  0.0150  170 PRO B C   
4972 O O   . PRO B 170 ? 0.7735 0.7507 0.7268 -0.0052 0.0104  0.0170  170 PRO B O   
4973 C CB  . PRO B 170 ? 0.6817 0.6450 0.6397 -0.0097 -0.0052 -0.0140 170 PRO B CB  
4974 C CG  . PRO B 170 ? 0.6872 0.6654 0.6452 -0.0127 -0.0153 -0.0227 170 PRO B CG  
4975 C CD  . PRO B 170 ? 0.7101 0.7114 0.6669 -0.0131 -0.0179 -0.0155 170 PRO B CD  
4976 N N   . LYS B 171 ? 0.8226 0.7692 0.7822 0.0040  0.0179  0.0230  171 LYS B N   
4977 C CA  . LYS B 171 ? 0.8464 0.7778 0.8058 0.0058  0.0306  0.0342  171 LYS B CA  
4978 C C   . LYS B 171 ? 0.8610 0.7845 0.8224 -0.0054 0.0347  0.0234  171 LYS B C   
4979 O O   . LYS B 171 ? 0.8946 0.8170 0.8553 -0.0071 0.0442  0.0335  171 LYS B O   
4980 C CB  . LYS B 171 ? 0.8873 0.7918 0.8494 0.0130  0.0401  0.0389  171 LYS B CB  
4981 C CG  . LYS B 171 ? 0.9888 0.8956 0.9522 0.0265  0.0466  0.0610  171 LYS B CG  
4982 C CD  . LYS B 171 ? 1.0173 0.9452 0.9855 0.0339  0.0382  0.0639  171 LYS B CD  
4983 C CE  . LYS B 171 ? 0.9499 0.8566 0.9210 0.0406  0.0454  0.0607  171 LYS B CE  
4984 N NZ  . LYS B 171 ? 0.9640 0.8920 0.9449 0.0500  0.0425  0.0697  171 LYS B NZ  
4985 N N   . GLU B 172 ? 0.8695 0.7883 0.8343 -0.0123 0.0286  0.0039  172 GLU B N   
4986 C CA  . GLU B 172 ? 0.9067 0.8244 0.8791 -0.0231 0.0303  -0.0090 172 GLU B CA  
4987 C C   . GLU B 172 ? 0.8676 0.8019 0.8402 -0.0263 0.0171  -0.0254 172 GLU B C   
4988 O O   . GLU B 172 ? 0.8570 0.7915 0.8240 -0.0215 0.0082  -0.0298 172 GLU B O   
4989 C CB  . GLU B 172 ? 0.8688 0.7599 0.8491 -0.0278 0.0363  -0.0185 172 GLU B CB  
4990 C CG  . GLU B 172 ? 0.9139 0.7968 0.9068 -0.0375 0.0491  -0.0170 172 GLU B CG  
4991 C CD  . GLU B 172 ? 1.0377 0.9111 1.0263 -0.0320 0.0638  0.0072  172 GLU B CD  
4992 O OE1 . GLU B 172 ? 1.0556 0.9428 1.0431 -0.0342 0.0704  0.0180  172 GLU B OE1 
4993 O OE2 . GLU B 172 ? 1.0194 0.8716 1.0041 -0.0237 0.0693  0.0161  172 GLU B OE2 
4994 N N   . PRO B 173 ? 0.7185 0.6662 0.6983 -0.0336 0.0173  -0.0337 173 PRO B N   
4995 C CA  . PRO B 173 ? 0.6896 0.6508 0.6714 -0.0347 0.0055  -0.0499 173 PRO B CA  
4996 C C   . PRO B 173 ? 0.6830 0.6311 0.6669 -0.0336 -0.0027 -0.0637 173 PRO B C   
4997 O O   . PRO B 173 ? 0.6534 0.5884 0.6449 -0.0377 0.0005  -0.0698 173 PRO B O   
4998 C CB  . PRO B 173 ? 0.6532 0.6290 0.6469 -0.0423 0.0113  -0.0557 173 PRO B CB  
4999 C CG  . PRO B 173 ? 0.7041 0.6797 0.6933 -0.0431 0.0254  -0.0376 173 PRO B CG  
5000 C CD  . PRO B 173 ? 0.7309 0.6833 0.7164 -0.0394 0.0300  -0.0262 173 PRO B CD  
5001 N N   . GLU B 174 ? 0.6065 0.5583 0.5829 -0.0281 -0.0135 -0.0694 174 GLU B N   
5002 C CA  . GLU B 174 ? 0.5722 0.5119 0.5434 -0.0237 -0.0220 -0.0797 174 GLU B CA  
5003 C C   . GLU B 174 ? 0.5805 0.5328 0.5607 -0.0247 -0.0311 -0.0954 174 GLU B C   
5004 O O   . GLU B 174 ? 0.5929 0.5568 0.5727 -0.0220 -0.0359 -0.0976 174 GLU B O   
5005 C CB  . GLU B 174 ? 0.5386 0.4718 0.4959 -0.0159 -0.0254 -0.0726 174 GLU B CB  
5006 C CG  . GLU B 174 ? 0.5691 0.4961 0.5227 -0.0137 -0.0166 -0.0567 174 GLU B CG  
5007 C CD  . GLU B 174 ? 0.6172 0.5430 0.5638 -0.0078 -0.0183 -0.0494 174 GLU B CD  
5008 O OE1 . GLU B 174 ? 0.5984 0.5249 0.5413 -0.0061 -0.0253 -0.0556 174 GLU B OE1 
5009 O OE2 . GLU B 174 ? 0.6398 0.5640 0.5867 -0.0046 -0.0116 -0.0367 174 GLU B OE2 
5010 N N   . ILE B 175 ? 0.5614 0.5118 0.5514 -0.0283 -0.0338 -0.1074 175 ILE B N   
5011 C CA  . ILE B 175 ? 0.5456 0.5112 0.5478 -0.0278 -0.0442 -0.1233 175 ILE B CA  
5012 C C   . ILE B 175 ? 0.5964 0.5513 0.5814 -0.0168 -0.0570 -0.1290 175 ILE B C   
5013 O O   . ILE B 175 ? 0.5940 0.5360 0.5716 -0.0156 -0.0605 -0.1349 175 ILE B O   
5014 C CB  . ILE B 175 ? 0.5644 0.5378 0.5901 -0.0384 -0.0417 -0.1344 175 ILE B CB  
5015 C CG1 . ILE B 175 ? 0.5720 0.5424 0.6064 -0.0485 -0.0244 -0.1228 175 ILE B CG1 
5016 C CG2 . ILE B 175 ? 0.5576 0.5573 0.6043 -0.0386 -0.0498 -0.1484 175 ILE B CG2 
5017 C CD1 . ILE B 175 ? 0.5719 0.5588 0.6075 -0.0487 -0.0171 -0.1135 175 ILE B CD1 
5018 N N   . VAL B 176 ? 0.6086 0.5670 0.5857 -0.0081 -0.0632 -0.1274 176 VAL B N   
5019 C CA  . VAL B 176 ? 0.6358 0.5801 0.5918 0.0040  -0.0717 -0.1268 176 VAL B CA  
5020 C C   . VAL B 176 ? 0.6480 0.6053 0.6101 0.0122  -0.0847 -0.1381 176 VAL B C   
5021 O O   . VAL B 176 ? 0.6432 0.6144 0.6184 0.0124  -0.0845 -0.1399 176 VAL B O   
5022 C CB  . VAL B 176 ? 0.6505 0.5832 0.5929 0.0075  -0.0657 -0.1123 176 VAL B CB  
5023 C CG1 . VAL B 176 ? 0.5825 0.4997 0.5043 0.0201  -0.0717 -0.1096 176 VAL B CG1 
5024 C CG2 . VAL B 176 ? 0.6007 0.5247 0.5397 0.0018  -0.0541 -0.1006 176 VAL B CG2 
5025 N N   . THR B 177 ? 0.6668 0.6203 0.6185 0.0204  -0.0964 -0.1463 177 THR B N   
5026 C CA  . THR B 177 ? 0.6581 0.6250 0.6140 0.0317  -0.1108 -0.1558 177 THR B CA  
5027 C C   . THR B 177 ? 0.7108 0.6590 0.6346 0.0478  -0.1195 -0.1516 177 THR B C   
5028 O O   . THR B 177 ? 0.7065 0.6340 0.6068 0.0487  -0.1144 -0.1450 177 THR B O   
5029 C CB  . THR B 177 ? 0.6505 0.6424 0.6323 0.0260  -0.1201 -0.1738 177 THR B CB  
5030 O OG1 . THR B 177 ? 0.6826 0.6646 0.6521 0.0239  -0.1252 -0.1809 177 THR B OG1 
5031 C CG2 . THR B 177 ? 0.6357 0.6443 0.6484 0.0094  -0.1078 -0.1757 177 THR B CG2 
5032 N N   . PHE B 178 ? 0.6784 0.6334 0.6001 0.0623  -0.1313 -0.1544 178 PHE B N   
5033 C CA  . PHE B 178 ? 0.6837 0.6238 0.5732 0.0801  -0.1415 -0.1510 178 PHE B CA  
5034 C C   . PHE B 178 ? 0.7310 0.6935 0.6301 0.0937  -0.1607 -0.1627 178 PHE B C   
5035 O O   . PHE B 178 ? 0.6874 0.6701 0.6151 0.0932  -0.1622 -0.1677 178 PHE B O   
5036 C CB  . PHE B 178 ? 0.7213 0.6330 0.5865 0.0890  -0.1314 -0.1317 178 PHE B CB  
5037 C CG  . PHE B 178 ? 0.7243 0.6377 0.6058 0.0908  -0.1274 -0.1273 178 PHE B CG  
5038 C CD1 . PHE B 178 ? 0.6812 0.5961 0.5808 0.0758  -0.1142 -0.1243 178 PHE B CD1 
5039 C CD2 . PHE B 178 ? 0.7200 0.6322 0.5968 0.1090  -0.1370 -0.1263 178 PHE B CD2 
5040 C CE1 . PHE B 178 ? 0.6460 0.5609 0.5581 0.0773  -0.1107 -0.1232 178 PHE B CE1 
5041 C CE2 . PHE B 178 ? 0.7240 0.6340 0.6155 0.1113  -0.1321 -0.1238 178 PHE B CE2 
5042 C CZ  . PHE B 178 ? 0.6759 0.5869 0.5848 0.0945  -0.1188 -0.1236 178 PHE B CZ  
5043 N N   . ASN B 179 ? 0.8025 0.7639 0.6777 0.1064  -0.1756 -0.1682 179 ASN B N   
5044 C CA  . ASN B 179 ? 0.7919 0.7790 0.6746 0.1212  -0.1977 -0.1805 179 ASN B CA  
5045 C C   . ASN B 179 ? 0.8361 0.8055 0.6844 0.1474  -0.2046 -0.1665 179 ASN B C   
5046 O O   . ASN B 179 ? 0.8236 0.7609 0.6331 0.1543  -0.1961 -0.1513 179 ASN B O   
5047 C CB  . ASN B 179 ? 0.7681 0.7709 0.6493 0.1169  -0.2130 -0.2001 179 ASN B CB  
5048 C CG  . ASN B 179 ? 0.8633 0.9099 0.7847 0.1163  -0.2317 -0.2205 179 ASN B CG  
5049 O OD1 . ASN B 179 ? 0.7765 0.8415 0.7228 0.1237  -0.2338 -0.2185 179 ASN B OD1 
5050 N ND2 . ASN B 179 ? 0.8387 0.9028 0.7675 0.1085  -0.2458 -0.2414 179 ASN B ND2 
5051 N N   . THR B 180 ? 0.7294 0.7203 0.5932 0.1631  -0.2190 -0.1707 180 THR B N   
5052 C CA  . THR B 180 ? 0.7183 0.6920 0.5533 0.1902  -0.2249 -0.1555 180 THR B CA  
5053 C C   . THR B 180 ? 0.7075 0.7165 0.5559 0.2088  -0.2507 -0.1681 180 THR B C   
5054 O O   . THR B 180 ? 0.7101 0.7585 0.6002 0.1984  -0.2604 -0.1880 180 THR B O   
5055 C CB  . THR B 180 ? 0.8044 0.7573 0.6493 0.1914  -0.2075 -0.1403 180 THR B CB  
5056 O OG1 . THR B 180 ? 0.7531 0.7354 0.6385 0.1947  -0.2136 -0.1507 180 THR B OG1 
5057 C CG2 . THR B 180 ? 0.6951 0.6302 0.5472 0.1667  -0.1844 -0.1350 180 THR B CG2 
5058 N N   . THR B 181 ? 0.7112 0.7068 0.5258 0.2373  -0.2610 -0.1552 181 THR B N   
5059 C CA  . THR B 181 ? 0.7307 0.7617 0.5591 0.2592  -0.2866 -0.1648 181 THR B CA  
5060 C C   . THR B 181 ? 0.7370 0.7903 0.6150 0.2599  -0.2836 -0.1689 181 THR B C   
5061 O O   . THR B 181 ? 0.7234 0.8171 0.6290 0.2733  -0.3039 -0.1813 181 THR B O   
5062 C CB  . THR B 181 ? 0.7960 0.8047 0.5726 0.2927  -0.2973 -0.1466 181 THR B CB  
5063 O OG1 . THR B 181 ? 0.8267 0.7980 0.5933 0.3042  -0.2790 -0.1228 181 THR B OG1 
5064 C CG2 . THR B 181 ? 0.8148 0.7984 0.5372 0.2918  -0.2960 -0.1420 181 THR B CG2 
5065 N N   . PHE B 182 ? 0.7523 0.7832 0.6438 0.2459  -0.2593 -0.1605 182 PHE B N   
5066 C CA  . PHE B 182 ? 0.7497 0.8007 0.6860 0.2457  -0.2542 -0.1666 182 PHE B CA  
5067 C C   . PHE B 182 ? 0.7371 0.8053 0.7104 0.2142  -0.2397 -0.1799 182 PHE B C   
5068 O O   . PHE B 182 ? 0.7364 0.8025 0.7327 0.2078  -0.2244 -0.1794 182 PHE B O   
5069 C CB  . PHE B 182 ? 0.7457 0.7572 0.6673 0.2603  -0.2395 -0.1472 182 PHE B CB  
5070 C CG  . PHE B 182 ? 0.8111 0.7747 0.7015 0.2466  -0.2180 -0.1312 182 PHE B CG  
5071 C CD1 . PHE B 182 ? 0.7633 0.6945 0.6056 0.2571  -0.2181 -0.1146 182 PHE B CD1 
5072 C CD2 . PHE B 182 ? 0.7531 0.7064 0.6628 0.2237  -0.1973 -0.1329 182 PHE B CD2 
5073 C CE1 . PHE B 182 ? 0.7807 0.6716 0.5999 0.2440  -0.1971 -0.0998 182 PHE B CE1 
5074 C CE2 . PHE B 182 ? 0.7358 0.6503 0.6218 0.2109  -0.1791 -0.1192 182 PHE B CE2 
5075 C CZ  . PHE B 182 ? 0.7666 0.6506 0.6103 0.2205  -0.1783 -0.1026 182 PHE B CZ  
5076 N N   . GLY B 183 ? 0.7458 0.8294 0.7233 0.1951  -0.2437 -0.1918 183 GLY B N   
5077 C CA  . GLY B 183 ? 0.6525 0.7594 0.6697 0.1681  -0.2329 -0.2053 183 GLY B CA  
5078 C C   . GLY B 183 ? 0.6808 0.7616 0.6796 0.1450  -0.2171 -0.2005 183 GLY B C   
5079 O O   . GLY B 183 ? 0.7049 0.7498 0.6629 0.1488  -0.2122 -0.1867 183 GLY B O   
5080 N N   . SER B 184 ? 0.6425 0.7435 0.6742 0.1217  -0.2083 -0.2116 184 SER B N   
5081 C CA  . SER B 184 ? 0.6155 0.6966 0.6383 0.0994  -0.1919 -0.2075 184 SER B CA  
5082 C C   . SER B 184 ? 0.6333 0.7015 0.6623 0.0906  -0.1707 -0.1972 184 SER B C   
5083 O O   . SER B 184 ? 0.6142 0.7042 0.6730 0.0903  -0.1664 -0.2026 184 SER B O   
5084 C CB  . SER B 184 ? 0.5953 0.7031 0.6491 0.0798  -0.1941 -0.2246 184 SER B CB  
5085 O OG  . SER B 184 ? 0.6647 0.7509 0.7096 0.0605  -0.1772 -0.2187 184 SER B OG  
5086 N N   . PHE B 185 ? 0.6149 0.6496 0.6155 0.0848  -0.1580 -0.1831 185 PHE B N   
5087 C CA  . PHE B 185 ? 0.6147 0.6350 0.6151 0.0781  -0.1409 -0.1734 185 PHE B CA  
5088 C C   . PHE B 185 ? 0.6237 0.6383 0.6249 0.0574  -0.1266 -0.1697 185 PHE B C   
5089 O O   . PHE B 185 ? 0.5980 0.6002 0.5837 0.0521  -0.1267 -0.1670 185 PHE B O   
5090 C CB  . PHE B 185 ? 0.6409 0.6271 0.6101 0.0908  -0.1384 -0.1585 185 PHE B CB  
5091 C CG  . PHE B 185 ? 0.6778 0.6634 0.6481 0.1116  -0.1464 -0.1583 185 PHE B CG  
5092 C CD1 . PHE B 185 ? 0.6518 0.6480 0.6173 0.1298  -0.1642 -0.1622 185 PHE B CD1 
5093 C CD2 . PHE B 185 ? 0.6467 0.6197 0.6214 0.1142  -0.1366 -0.1544 185 PHE B CD2 
5094 C CE1 . PHE B 185 ? 0.6719 0.6666 0.6382 0.1518  -0.1714 -0.1599 185 PHE B CE1 
5095 C CE2 . PHE B 185 ? 0.6670 0.6350 0.6428 0.1349  -0.1424 -0.1537 185 PHE B CE2 
5096 C CZ  . PHE B 185 ? 0.7177 0.6966 0.6896 0.1547  -0.1596 -0.1552 185 PHE B CZ  
5097 N N   . GLY B 186 ? 0.6329 0.6558 0.6502 0.0474  -0.1141 -0.1693 186 GLY B N   
5098 C CA  . GLY B 186 ? 0.6248 0.6394 0.6379 0.0315  -0.1001 -0.1617 186 GLY B CA  
5099 C C   . GLY B 186 ? 0.6056 0.6038 0.6055 0.0319  -0.0916 -0.1521 186 GLY B C   
5100 O O   . GLY B 186 ? 0.6234 0.6200 0.6246 0.0416  -0.0937 -0.1546 186 GLY B O   
5101 N N   . ILE B 187 ? 0.5409 0.5273 0.5299 0.0220  -0.0824 -0.1422 187 ILE B N   
5102 C CA  . ILE B 187 ? 0.5737 0.5469 0.5523 0.0210  -0.0764 -0.1348 187 ILE B CA  
5103 C C   . ILE B 187 ? 0.5759 0.5580 0.5579 0.0079  -0.0662 -0.1306 187 ILE B C   
5104 O O   . ILE B 187 ? 0.5201 0.5054 0.5035 0.0008  -0.0621 -0.1261 187 ILE B O   
5105 C CB  . ILE B 187 ? 0.5701 0.5172 0.5280 0.0260  -0.0776 -0.1239 187 ILE B CB  
5106 C CG1 . ILE B 187 ? 0.5913 0.5261 0.5446 0.0233  -0.0721 -0.1183 187 ILE B CG1 
5107 C CG2 . ILE B 187 ? 0.5738 0.5164 0.5243 0.0201  -0.0741 -0.1169 187 ILE B CG2 
5108 C CD1 . ILE B 187 ? 0.6320 0.5404 0.5702 0.0322  -0.0730 -0.1100 187 ILE B CD1 
5109 N N   . PHE B 188 ? 0.5720 0.5580 0.5546 0.0059  -0.0624 -0.1328 188 PHE B N   
5110 C CA  . PHE B 188 ? 0.5579 0.5509 0.5370 -0.0039 -0.0550 -0.1271 188 PHE B CA  
5111 C C   . PHE B 188 ? 0.5851 0.5742 0.5591 -0.0039 -0.0553 -0.1315 188 PHE B C   
5112 O O   . PHE B 188 ? 0.6034 0.5828 0.5787 0.0034  -0.0591 -0.1390 188 PHE B O   
5113 C CB  . PHE B 188 ? 0.5414 0.5555 0.5304 -0.0099 -0.0477 -0.1293 188 PHE B CB  
5114 C CG  . PHE B 188 ? 0.5468 0.5771 0.5485 -0.0062 -0.0463 -0.1422 188 PHE B CG  
5115 C CD1 . PHE B 188 ? 0.5592 0.5951 0.5563 -0.0051 -0.0433 -0.1489 188 PHE B CD1 
5116 C CD2 . PHE B 188 ? 0.5270 0.5695 0.5469 -0.0044 -0.0475 -0.1489 188 PHE B CD2 
5117 C CE1 . PHE B 188 ? 0.5306 0.5818 0.5395 -0.0002 -0.0398 -0.1611 188 PHE B CE1 
5118 C CE2 . PHE B 188 ? 0.5439 0.6053 0.5799 -0.0002 -0.0450 -0.1605 188 PHE B CE2 
5119 C CZ  . PHE B 188 ? 0.5452 0.6102 0.5750 0.0026  -0.0400 -0.1660 188 PHE B CZ  
5120 N N   . THR B 189 ? 0.5629 0.5593 0.5312 -0.0115 -0.0519 -0.1274 189 THR B N   
5121 C CA  . THR B 189 ? 0.5885 0.5796 0.5521 -0.0141 -0.0543 -0.1318 189 THR B CA  
5122 C C   . THR B 189 ? 0.5891 0.5989 0.5479 -0.0181 -0.0517 -0.1398 189 THR B C   
5123 O O   . THR B 189 ? 0.5831 0.6082 0.5366 -0.0224 -0.0482 -0.1322 189 THR B O   
5124 C CB  . THR B 189 ? 0.5524 0.5361 0.5134 -0.0192 -0.0555 -0.1198 189 THR B CB  
5125 O OG1 . THR B 189 ? 0.5659 0.5338 0.5270 -0.0144 -0.0555 -0.1113 189 THR B OG1 
5126 C CG2 . THR B 189 ? 0.5935 0.5689 0.5557 -0.0234 -0.0588 -0.1261 189 THR B CG2 
5127 N N   . CYS B 190 ? 0.6318 0.6511 0.5714 -0.0611 -0.0601 0.0017  190 CYS B N   
5128 C CA  . CYS B 190 ? 0.6379 0.6706 0.5849 -0.0714 -0.0600 -0.0003 190 CYS B CA  
5129 C C   . CYS B 190 ? 0.6080 0.6562 0.5668 -0.0731 -0.0523 -0.0037 190 CYS B C   
5130 O O   . CYS B 190 ? 0.6110 0.6588 0.5782 -0.0699 -0.0526 -0.0172 190 CYS B O   
5131 C CB  . CYS B 190 ? 0.5965 0.6381 0.5412 -0.0813 -0.0592 0.0154  190 CYS B CB  
5132 S SG  . CYS B 190 ? 0.6673 0.7084 0.6075 -0.0946 -0.0671 0.0071  190 CYS B SG  
5133 N N   . PHE B 191 ? 0.5829 0.6465 0.5436 -0.0777 -0.0446 0.0099  191 PHE B N   
5134 C CA  . PHE B 191 ? 0.5385 0.6152 0.5069 -0.0786 -0.0352 0.0094  191 PHE B CA  
5135 C C   . PHE B 191 ? 0.5538 0.6228 0.5296 -0.0732 -0.0277 0.0021  191 PHE B C   
5136 O O   . PHE B 191 ? 0.5065 0.5812 0.4919 -0.0746 -0.0206 -0.0042 191 PHE B O   
5137 C CB  . PHE B 191 ? 0.5627 0.6576 0.5295 -0.0803 -0.0279 0.0288  191 PHE B CB  
5138 C CG  . PHE B 191 ? 0.5608 0.6709 0.5295 -0.0816 -0.0206 0.0303  191 PHE B CG  
5139 C CD1 . PHE B 191 ? 0.6085 0.7162 0.5777 -0.0841 -0.0229 0.0156  191 PHE B CD1 
5140 C CD2 . PHE B 191 ? 0.5543 0.6810 0.5221 -0.0778 -0.0102 0.0481  191 PHE B CD2 
5141 C CE1 . PHE B 191 ? 0.5575 0.6774 0.5245 -0.0832 -0.0144 0.0183  191 PHE B CE1 
5142 C CE2 . PHE B 191 ? 0.5344 0.6739 0.5003 -0.0764 -0.0028 0.0511  191 PHE B CE2 
5143 C CZ  . PHE B 191 ? 0.5479 0.6832 0.5125 -0.0795 -0.0049 0.0359  191 PHE B CZ  
5144 N N   . ASP B 192 ? 0.5169 0.5713 0.4869 -0.0678 -0.0290 0.0023  192 ASP B N   
5145 C CA  . ASP B 192 ? 0.5171 0.5608 0.4913 -0.0654 -0.0243 -0.0070 192 ASP B CA  
5146 C C   . ASP B 192 ? 0.4842 0.5337 0.4752 -0.0690 -0.0295 -0.0252 192 ASP B C   
5147 O O   . ASP B 192 ? 0.5014 0.5516 0.5047 -0.0725 -0.0217 -0.0316 192 ASP B O   
5148 C CB  . ASP B 192 ? 0.5285 0.5527 0.4882 -0.0583 -0.0299 -0.0084 192 ASP B CB  
5149 C CG  . ASP B 192 ? 0.5535 0.5704 0.4973 -0.0520 -0.0199 0.0111  192 ASP B CG  
5150 O OD1 . ASP B 192 ? 0.5303 0.5532 0.4752 -0.0518 -0.0057 0.0234  192 ASP B OD1 
5151 O OD2 . ASP B 192 ? 0.5396 0.5448 0.4692 -0.0452 -0.0248 0.0155  192 ASP B OD2 
5152 N N   . ILE B 193 ? 0.4866 0.5402 0.4793 -0.0679 -0.0409 -0.0327 193 ILE B N   
5153 C CA  . ILE B 193 ? 0.5025 0.5646 0.5125 -0.0679 -0.0455 -0.0483 193 ILE B CA  
5154 C C   . ILE B 193 ? 0.4905 0.5662 0.5167 -0.0732 -0.0323 -0.0491 193 ILE B C   
5155 O O   . ILE B 193 ? 0.4610 0.5467 0.5083 -0.0746 -0.0312 -0.0600 193 ILE B O   
5156 C CB  . ILE B 193 ? 0.4944 0.5547 0.4980 -0.0629 -0.0561 -0.0528 193 ILE B CB  
5157 C CG1 . ILE B 193 ? 0.4949 0.5639 0.5149 -0.0572 -0.0633 -0.0676 193 ILE B CG1 
5158 C CG2 . ILE B 193 ? 0.4912 0.5560 0.4897 -0.0671 -0.0505 -0.0480 193 ILE B CG2 
5159 C CD1 . ILE B 193 ? 0.4925 0.5527 0.5007 -0.0481 -0.0728 -0.0709 193 ILE B CD1 
5160 N N   . LEU B 194 ? 0.5099 0.5882 0.5279 -0.0755 -0.0217 -0.0365 194 LEU B N   
5161 C CA  . LEU B 194 ? 0.5119 0.6007 0.5409 -0.0780 -0.0075 -0.0356 194 LEU B CA  
5162 C C   . LEU B 194 ? 0.5362 0.6205 0.5730 -0.0811 0.0075  -0.0313 194 LEU B C   
5163 O O   . LEU B 194 ? 0.5335 0.6238 0.5783 -0.0826 0.0225  -0.0280 194 LEU B O   
5164 C CB  . LEU B 194 ? 0.5248 0.6196 0.5381 -0.0775 -0.0042 -0.0250 194 LEU B CB  
5165 C CG  . LEU B 194 ? 0.5284 0.6257 0.5366 -0.0761 -0.0107 -0.0333 194 LEU B CG  
5166 C CD1 . LEU B 194 ? 0.5722 0.6707 0.5582 -0.0786 -0.0146 -0.0243 194 LEU B CD1 
5167 C CD2 . LEU B 194 ? 0.5541 0.6599 0.5760 -0.0737 0.0018  -0.0394 194 LEU B CD2 
5168 N N   . PHE B 195 ? 0.6295 0.6996 0.6612 -0.0815 0.0055  -0.0310 195 PHE B N   
5169 C CA  . PHE B 195 ? 0.6126 0.6698 0.6445 -0.0842 0.0215  -0.0262 195 PHE B CA  
5170 C C   . PHE B 195 ? 0.6469 0.6913 0.6873 -0.0900 0.0157  -0.0412 195 PHE B C   
5171 O O   . PHE B 195 ? 0.6323 0.6805 0.6767 -0.0895 -0.0022 -0.0533 195 PHE B O   
5172 C CB  . PHE B 195 ? 0.6036 0.6516 0.6127 -0.0772 0.0294  -0.0073 195 PHE B CB  
5173 C CG  . PHE B 195 ? 0.6612 0.7268 0.6643 -0.0734 0.0344  0.0070  195 PHE B CG  
5174 C CD1 . PHE B 195 ? 0.6452 0.7156 0.6513 -0.0725 0.0518  0.0143  195 PHE B CD1 
5175 C CD2 . PHE B 195 ? 0.6339 0.7109 0.6279 -0.0717 0.0210  0.0123  195 PHE B CD2 
5176 C CE1 . PHE B 195 ? 0.6616 0.7494 0.6587 -0.0681 0.0541  0.0264  195 PHE B CE1 
5177 C CE2 . PHE B 195 ? 0.6254 0.7199 0.6132 -0.0707 0.0225  0.0230  195 PHE B CE2 
5178 C CZ  . PHE B 195 ? 0.6677 0.7685 0.6557 -0.0680 0.0380  0.0299  195 PHE B CZ  
5179 N N   . HIS B 196 ? 0.5934 0.6211 0.6347 -0.0953 0.0311  -0.0402 196 HIS B N   
5180 C CA  . HIS B 196 ? 0.6390 0.6540 0.6901 -0.1053 0.0261  -0.0569 196 HIS B CA  
5181 C C   . HIS B 196 ? 0.6493 0.6406 0.6737 -0.1002 0.0154  -0.0595 196 HIS B C   
5182 O O   . HIS B 196 ? 0.6396 0.6291 0.6681 -0.1048 -0.0011 -0.0763 196 HIS B O   
5183 C CB  . HIS B 196 ? 0.6487 0.6476 0.7079 -0.1150 0.0482  -0.0558 196 HIS B CB  
5184 C CG  . HIS B 196 ? 0.6699 0.6595 0.7457 -0.1308 0.0425  -0.0754 196 HIS B CG  
5185 N ND1 . HIS B 196 ? 0.7008 0.6578 0.7539 -0.1337 0.0383  -0.0830 196 HIS B ND1 
5186 C CD2 . HIS B 196 ? 0.6424 0.6524 0.7554 -0.1451 0.0396  -0.0893 196 HIS B CD2 
5187 C CE1 . HIS B 196 ? 0.7182 0.6755 0.7931 -0.1513 0.0309  -0.1024 196 HIS B CE1 
5188 N NE2 . HIS B 196 ? 0.6385 0.6306 0.7532 -0.1589 0.0317  -0.1058 196 HIS B NE2 
5189 N N   . ASP B 197 ? 0.8084 0.7830 0.8049 -0.0895 0.0250  -0.0425 197 ASP B N   
5190 C CA  . ASP B 197 ? 0.8138 0.7607 0.7804 -0.0820 0.0215  -0.0413 197 ASP B CA  
5191 C C   . ASP B 197 ? 0.8249 0.7808 0.7762 -0.0688 0.0138  -0.0277 197 ASP B C   
5192 O O   . ASP B 197 ? 0.8279 0.7984 0.7796 -0.0637 0.0227  -0.0099 197 ASP B O   
5193 C CB  . ASP B 197 ? 0.8313 0.7463 0.7775 -0.0790 0.0447  -0.0306 197 ASP B CB  
5194 C CG  . ASP B 197 ? 0.8723 0.7693 0.8301 -0.0944 0.0536  -0.0450 197 ASP B CG  
5195 O OD1 . ASP B 197 ? 0.9592 0.8415 0.9150 -0.1036 0.0403  -0.0650 197 ASP B OD1 
5196 O OD2 . ASP B 197 ? 0.9373 0.8346 0.9056 -0.0977 0.0737  -0.0362 197 ASP B OD2 
5197 N N   . PRO B 198 ? 0.6607 0.6094 0.5986 -0.0635 -0.0028 -0.0352 198 PRO B N   
5198 C CA  . PRO B 198 ? 0.6397 0.5747 0.5736 -0.0678 -0.0176 -0.0563 198 PRO B CA  
5199 C C   . PRO B 198 ? 0.6212 0.5842 0.5844 -0.0754 -0.0353 -0.0728 198 PRO B C   
5200 O O   . PRO B 198 ? 0.6291 0.5902 0.5976 -0.0815 -0.0485 -0.0911 198 PRO B O   
5201 C CB  . PRO B 198 ? 0.6538 0.5723 0.5562 -0.0532 -0.0255 -0.0506 198 PRO B CB  
5202 C CG  . PRO B 198 ? 0.6467 0.5878 0.5558 -0.0470 -0.0255 -0.0340 198 PRO B CG  
5203 C CD  . PRO B 198 ? 0.6323 0.5876 0.5573 -0.0524 -0.0086 -0.0216 198 PRO B CD  
5204 N N   . ALA B 199 ? 0.6773 0.6670 0.6596 -0.0749 -0.0357 -0.0667 199 ALA B N   
5205 C CA  . ALA B 199 ? 0.6413 0.6543 0.6425 -0.0746 -0.0527 -0.0785 199 ALA B CA  
5206 C C   . ALA B 199 ? 0.6381 0.6643 0.6667 -0.0858 -0.0595 -0.0972 199 ALA B C   
5207 O O   . ALA B 199 ? 0.6549 0.6914 0.6890 -0.0832 -0.0783 -0.1102 199 ALA B O   
5208 C CB  . ALA B 199 ? 0.5964 0.6295 0.6101 -0.0734 -0.0479 -0.0696 199 ALA B CB  
5209 N N   . VAL B 200 ? 0.5539 0.5827 0.6017 -0.0981 -0.0442 -0.0979 200 VAL B N   
5210 C CA  . VAL B 200 ? 0.5545 0.5999 0.6350 -0.1119 -0.0490 -0.1146 200 VAL B CA  
5211 C C   . VAL B 200 ? 0.5914 0.6135 0.6596 -0.1208 -0.0563 -0.1281 200 VAL B C   
5212 O O   . VAL B 200 ? 0.5770 0.6155 0.6667 -0.1302 -0.0722 -0.1457 200 VAL B O   
5213 C CB  . VAL B 200 ? 0.5674 0.6235 0.6748 -0.1224 -0.0276 -0.1096 200 VAL B CB  
5214 C CG1 . VAL B 200 ? 0.5244 0.6041 0.6732 -0.1380 -0.0319 -0.1255 200 VAL B CG1 
5215 C CG2 . VAL B 200 ? 0.5161 0.5901 0.6273 -0.1128 -0.0206 -0.0972 200 VAL B CG2 
5216 N N   . THR B 201 ? 0.6543 0.6383 0.6877 -0.1178 -0.0448 -0.1204 201 THR B N   
5217 C CA  . THR B 201 ? 0.6908 0.6438 0.7026 -0.1245 -0.0512 -0.1340 201 THR B CA  
5218 C C   . THR B 201 ? 0.6875 0.6459 0.6852 -0.1160 -0.0789 -0.1462 201 THR B C   
5219 O O   . THR B 201 ? 0.6557 0.6100 0.6537 -0.1262 -0.0947 -0.1658 201 THR B O   
5220 C CB  . THR B 201 ? 0.7565 0.6656 0.7271 -0.1162 -0.0320 -0.1200 201 THR B CB  
5221 O OG1 . THR B 201 ? 0.7416 0.6437 0.7230 -0.1229 -0.0059 -0.1088 201 THR B OG1 
5222 C CG2 . THR B 201 ? 0.7731 0.6422 0.7108 -0.1200 -0.0394 -0.1354 201 THR B CG2 
5223 N N   . LEU B 202 ? 0.6143 0.5804 0.5975 -0.0975 -0.0848 -0.1347 202 LEU B N   
5224 C CA  . LEU B 202 ? 0.5907 0.5602 0.5570 -0.0854 -0.1085 -0.1428 202 LEU B CA  
5225 C C   . LEU B 202 ? 0.6108 0.6169 0.6119 -0.0934 -0.1299 -0.1615 202 LEU B C   
5226 O O   . LEU B 202 ? 0.6129 0.6174 0.6021 -0.0926 -0.1510 -0.1769 202 LEU B O   
5227 C CB  . LEU B 202 ? 0.5838 0.5588 0.5378 -0.0670 -0.1075 -0.1256 202 LEU B CB  
5228 C CG  . LEU B 202 ? 0.6026 0.5453 0.5170 -0.0542 -0.0947 -0.1078 202 LEU B CG  
5229 C CD1 . LEU B 202 ? 0.5824 0.5371 0.4966 -0.0427 -0.0928 -0.0915 202 LEU B CD1 
5230 C CD2 . LEU B 202 ? 0.6222 0.5354 0.4967 -0.0444 -0.1062 -0.1158 202 LEU B CD2 
5231 N N   . VAL B 203 ? 0.6487 0.6903 0.6922 -0.0996 -0.1251 -0.1597 203 VAL B N   
5232 C CA  . VAL B 203 ? 0.6365 0.7198 0.7178 -0.1043 -0.1437 -0.1743 203 VAL B CA  
5233 C C   . VAL B 203 ? 0.6287 0.7185 0.7366 -0.1288 -0.1460 -0.1911 203 VAL B C   
5234 O O   . VAL B 203 ? 0.6628 0.7669 0.7776 -0.1346 -0.1692 -0.2086 203 VAL B O   
5235 C CB  . VAL B 203 ? 0.5935 0.7104 0.7073 -0.0985 -0.1359 -0.1650 203 VAL B CB  
5236 C CG1 . VAL B 203 ? 0.5440 0.7080 0.6985 -0.0993 -0.1536 -0.1773 203 VAL B CG1 
5237 C CG2 . VAL B 203 ? 0.5567 0.6606 0.6408 -0.0779 -0.1344 -0.1505 203 VAL B CG2 
5238 N N   . LYS B 204 ? 0.7063 0.7843 0.8279 -0.1440 -0.1221 -0.1858 204 LYS B N   
5239 C CA  . LYS B 204 ? 0.6822 0.7651 0.8344 -0.1703 -0.1193 -0.1999 204 LYS B CA  
5240 C C   . LYS B 204 ? 0.7630 0.8094 0.8834 -0.1808 -0.1314 -0.2163 204 LYS B C   
5241 O O   . LYS B 204 ? 0.7967 0.8609 0.9396 -0.1985 -0.1501 -0.2364 204 LYS B O   
5242 C CB  . LYS B 204 ? 0.7072 0.7765 0.8717 -0.1801 -0.0869 -0.1870 204 LYS B CB  
5243 C CG  . LYS B 204 ? 0.7818 0.8584 0.9856 -0.2082 -0.0781 -0.1981 204 LYS B CG  
5244 C CD  . LYS B 204 ? 0.8305 0.8523 1.0062 -0.2190 -0.0539 -0.1943 204 LYS B CD  
5245 C CE  . LYS B 204 ? 0.7807 0.7877 0.9407 -0.2040 -0.0252 -0.1695 204 LYS B CE  
5246 N NZ  . LYS B 204 ? 0.8335 0.7855 0.9585 -0.2071 -0.0013 -0.1622 204 LYS B NZ  
5247 N N   . ASP B 205 ? 0.8647 0.8603 0.9320 -0.1702 -0.1210 -0.2083 205 ASP B N   
5248 C CA  . ASP B 205 ? 0.9048 0.8554 0.9344 -0.1792 -0.1273 -0.2232 205 ASP B CA  
5249 C C   . ASP B 205 ? 0.9167 0.8621 0.9100 -0.1639 -0.1555 -0.2333 205 ASP B C   
5250 O O   . ASP B 205 ? 0.9189 0.8497 0.8974 -0.1761 -0.1738 -0.2547 205 ASP B O   
5251 C CB  . ASP B 205 ? 0.9562 0.8507 0.9437 -0.1734 -0.0985 -0.2085 205 ASP B CB  
5252 C CG  . ASP B 205 ? 0.9980 0.8863 1.0122 -0.1896 -0.0696 -0.2008 205 ASP B CG  
5253 O OD1 . ASP B 205 ? 1.0315 0.9551 1.0964 -0.2084 -0.0713 -0.2088 205 ASP B OD1 
5254 O OD2 . ASP B 205 ? 0.9863 0.8351 0.9703 -0.1817 -0.0439 -0.1852 205 ASP B OD2 
5255 N N   . PHE B 206 ? 0.7966 0.7503 0.7718 -0.1376 -0.1587 -0.2183 206 PHE B N   
5256 C CA  . PHE B 206 ? 0.8032 0.7442 0.7361 -0.1190 -0.1804 -0.2236 206 PHE B CA  
5257 C C   . PHE B 206 ? 0.8004 0.7916 0.7579 -0.1094 -0.2074 -0.2298 206 PHE B C   
5258 O O   . PHE B 206 ? 0.8222 0.8070 0.7463 -0.0942 -0.2286 -0.2365 206 PHE B O   
5259 C CB  . PHE B 206 ? 0.8143 0.7207 0.7020 -0.0949 -0.1629 -0.2010 206 PHE B CB  
5260 C CG  . PHE B 206 ? 0.8679 0.7210 0.7204 -0.0983 -0.1393 -0.1954 206 PHE B CG  
5261 C CD1 . PHE B 206 ? 0.8655 0.7139 0.7403 -0.1115 -0.1137 -0.1863 206 PHE B CD1 
5262 C CD2 . PHE B 206 ? 0.9402 0.7461 0.7345 -0.0865 -0.1416 -0.1989 206 PHE B CD2 
5263 C CE1 . PHE B 206 ? 0.9074 0.7057 0.7485 -0.1117 -0.0903 -0.1797 206 PHE B CE1 
5264 C CE2 . PHE B 206 ? 0.9791 0.7335 0.7387 -0.0868 -0.1178 -0.1929 206 PHE B CE2 
5265 C CZ  . PHE B 206 ? 0.9185 0.6694 0.7022 -0.0992 -0.0919 -0.1829 206 PHE B CZ  
5266 N N   . HIS B 207 ? 0.8286 0.8683 0.8414 -0.1165 -0.2066 -0.2278 207 HIS B N   
5267 C CA  . HIS B 207 ? 0.8081 0.9005 0.8522 -0.1094 -0.2313 -0.2352 207 HIS B CA  
5268 C C   . HIS B 207 ? 0.7987 0.8886 0.8096 -0.0781 -0.2412 -0.2244 207 HIS B C   
5269 O O   . HIS B 207 ? 0.7911 0.9080 0.8033 -0.0667 -0.2667 -0.2331 207 HIS B O   
5270 C CB  . HIS B 207 ? 0.8210 0.9332 0.8785 -0.1262 -0.2593 -0.2606 207 HIS B CB  
5271 C CG  . HIS B 207 ? 0.8661 0.9660 0.9444 -0.1593 -0.2496 -0.2728 207 HIS B CG  
5272 N ND1 . HIS B 207 ? 0.8906 0.9420 0.9276 -0.1719 -0.2519 -0.2853 207 HIS B ND1 
5273 C CD2 . HIS B 207 ? 0.7878 0.9126 0.9199 -0.1814 -0.2341 -0.2720 207 HIS B CD2 
5274 C CE1 . HIS B 207 ? 0.9320 0.9772 0.9971 -0.2015 -0.2390 -0.2920 207 HIS B CE1 
5275 N NE2 . HIS B 207 ? 0.8853 0.9755 1.0090 -0.2075 -0.2274 -0.2830 207 HIS B NE2 
5276 N N   . VAL B 208 ? 0.6478 0.7079 0.6313 -0.0640 -0.2206 -0.2044 208 VAL B N   
5277 C CA  . VAL B 208 ? 0.6590 0.7134 0.6128 -0.0364 -0.2267 -0.1927 208 VAL B CA  
5278 C C   . VAL B 208 ? 0.6413 0.7432 0.6323 -0.0269 -0.2368 -0.1918 208 VAL B C   
5279 O O   . VAL B 208 ? 0.6274 0.7611 0.6652 -0.0393 -0.2294 -0.1925 208 VAL B O   
5280 C CB  . VAL B 208 ? 0.6507 0.6713 0.5781 -0.0271 -0.2018 -0.1705 208 VAL B CB  
5281 C CG1 . VAL B 208 ? 0.6388 0.6171 0.5362 -0.0357 -0.1871 -0.1688 208 VAL B CG1 
5282 C CG2 . VAL B 208 ? 0.6711 0.7133 0.6356 -0.0333 -0.1849 -0.1595 208 VAL B CG2 
5283 N N   . ASP B 209 ? 0.7344 0.8393 0.7023 -0.0026 -0.2522 -0.1890 209 ASP B N   
5284 C CA  . ASP B 209 ? 0.7038 0.8465 0.6977 0.0129  -0.2596 -0.1852 209 ASP B CA  
5285 C C   . ASP B 209 ? 0.7002 0.8276 0.6885 0.0242  -0.2384 -0.1657 209 ASP B C   
5286 O O   . ASP B 209 ? 0.6734 0.8289 0.6929 0.0285  -0.2348 -0.1625 209 ASP B O   
5287 C CB  . ASP B 209 ? 0.7371 0.8871 0.7046 0.0370  -0.2847 -0.1896 209 ASP B CB  
5288 C CG  . ASP B 209 ? 0.7660 0.9276 0.7301 0.0264  -0.3096 -0.2105 209 ASP B CG  
5289 O OD1 . ASP B 209 ? 0.8206 1.0255 0.8323 0.0099  -0.3170 -0.2201 209 ASP B OD1 
5290 O OD2 . ASP B 209 ? 0.8242 0.9480 0.7380 0.0330  -0.3144 -0.2122 209 ASP B OD2 
5291 N N   . THR B 210 ? 0.5752 0.6589 0.5244 0.0288  -0.2242 -0.1528 210 THR B N   
5292 C CA  . THR B 210 ? 0.5482 0.6144 0.4864 0.0392  -0.2079 -0.1351 210 THR B CA  
5293 C C   . THR B 210 ? 0.5970 0.6318 0.5198 0.0270  -0.1872 -0.1237 210 THR B C   
5294 O O   . THR B 210 ? 0.5880 0.5984 0.4838 0.0252  -0.1864 -0.1238 210 THR B O   
5295 C CB  . THR B 210 ? 0.5870 0.6351 0.4879 0.0663  -0.2159 -0.1272 210 THR B CB  
5296 O OG1 . THR B 210 ? 0.5629 0.6443 0.4793 0.0812  -0.2344 -0.1354 210 THR B OG1 
5297 C CG2 . THR B 210 ? 0.5862 0.6091 0.4731 0.0731  -0.1977 -0.1092 210 THR B CG2 
5298 N N   . ILE B 211 ? 0.5847 0.6206 0.5232 0.0199  -0.1704 -0.1137 211 ILE B N   
5299 C CA  . ILE B 211 ? 0.5897 0.6015 0.5147 0.0115  -0.1515 -0.0994 211 ILE B CA  
5300 C C   . ILE B 211 ? 0.6122 0.6035 0.5142 0.0242  -0.1463 -0.0847 211 ILE B C   
5301 O O   . ILE B 211 ? 0.5885 0.5864 0.4963 0.0330  -0.1496 -0.0849 211 ILE B O   
5302 C CB  . ILE B 211 ? 0.5866 0.6133 0.5415 -0.0061 -0.1373 -0.0980 211 ILE B CB  
5303 C CG1 . ILE B 211 ? 0.6005 0.6411 0.5775 -0.0213 -0.1374 -0.1099 211 ILE B CG1 
5304 C CG2 . ILE B 211 ? 0.5271 0.5343 0.4674 -0.0113 -0.1205 -0.0810 211 ILE B CG2 
5305 C CD1 . ILE B 211 ? 0.6104 0.6253 0.5649 -0.0271 -0.1306 -0.1073 211 ILE B CD1 
5306 N N   . VAL B 212 ? 0.6490 0.6143 0.5249 0.0254  -0.1368 -0.0712 212 VAL B N   
5307 C CA  . VAL B 212 ? 0.6052 0.5510 0.4646 0.0304  -0.1274 -0.0548 212 VAL B CA  
5308 C C   . VAL B 212 ? 0.6748 0.6239 0.5475 0.0130  -0.1121 -0.0445 212 VAL B C   
5309 O O   . VAL B 212 ? 0.6396 0.5913 0.5156 0.0048  -0.1055 -0.0428 212 VAL B O   
5310 C CB  . VAL B 212 ? 0.6942 0.6123 0.5169 0.0459  -0.1268 -0.0444 212 VAL B CB  
5311 C CG1 . VAL B 212 ? 0.6759 0.5897 0.4810 0.0674  -0.1422 -0.0516 212 VAL B CG1 
5312 C CG2 . VAL B 212 ? 0.6748 0.5842 0.4836 0.0442  -0.1234 -0.0442 212 VAL B CG2 
5313 N N   . PHE B 213 ? 0.7288 0.6765 0.6068 0.0078  -0.1068 -0.0379 213 PHE B N   
5314 C CA  . PHE B 213 ? 0.6877 0.6478 0.5836 -0.0094 -0.0973 -0.0336 213 PHE B CA  
5315 C C   . PHE B 213 ? 0.7068 0.6537 0.5935 -0.0150 -0.0906 -0.0193 213 PHE B C   
5316 O O   . PHE B 213 ? 0.7237 0.6640 0.6100 -0.0171 -0.0921 -0.0221 213 PHE B O   
5317 C CB  . PHE B 213 ? 0.7073 0.6861 0.6252 -0.0136 -0.1008 -0.0472 213 PHE B CB  
5318 C CG  . PHE B 213 ? 0.6734 0.6658 0.6067 -0.0290 -0.0915 -0.0444 213 PHE B CG  
5319 C CD1 . PHE B 213 ? 0.6744 0.6763 0.6151 -0.0372 -0.0836 -0.0394 213 PHE B CD1 
5320 C CD2 . PHE B 213 ? 0.6773 0.6704 0.6139 -0.0334 -0.0900 -0.0470 213 PHE B CD2 
5321 C CE1 . PHE B 213 ? 0.6269 0.6422 0.5791 -0.0485 -0.0749 -0.0355 213 PHE B CE1 
5322 C CE2 . PHE B 213 ? 0.6666 0.6723 0.6129 -0.0461 -0.0824 -0.0448 213 PHE B CE2 
5323 C CZ  . PHE B 213 ? 0.6342 0.6527 0.5890 -0.0531 -0.0752 -0.0385 213 PHE B CZ  
5324 N N   . PRO B 214 ? 0.5768 0.5182 0.4555 -0.0176 -0.0825 -0.0034 214 PRO B N   
5325 C CA  . PRO B 214 ? 0.5815 0.5200 0.4609 -0.0293 -0.0758 0.0109  214 PRO B CA  
5326 C C   . PRO B 214 ? 0.5882 0.5486 0.4866 -0.0462 -0.0736 0.0096  214 PRO B C   
5327 O O   . PRO B 214 ? 0.5473 0.5255 0.4567 -0.0487 -0.0700 0.0089  214 PRO B O   
5328 C CB  . PRO B 214 ? 0.5826 0.5174 0.4535 -0.0253 -0.0665 0.0292  214 PRO B CB  
5329 C CG  . PRO B 214 ? 0.6436 0.5644 0.4958 -0.0061 -0.0702 0.0224  214 PRO B CG  
5330 C CD  . PRO B 214 ? 0.6318 0.5652 0.4961 -0.0069 -0.0799 0.0019  214 PRO B CD  
5331 N N   . THR B 215 ? 0.5843 0.5402 0.4831 -0.0573 -0.0755 0.0090  215 THR B N   
5332 C CA  . THR B 215 ? 0.6023 0.5768 0.5131 -0.0716 -0.0754 0.0055  215 THR B CA  
5333 C C   . THR B 215 ? 0.5860 0.5549 0.4934 -0.0880 -0.0766 0.0120  215 THR B C   
5334 O O   . THR B 215 ? 0.6042 0.5474 0.4990 -0.0880 -0.0779 0.0125  215 THR B O   
5335 C CB  . THR B 215 ? 0.5825 0.5578 0.4964 -0.0673 -0.0794 -0.0128 215 THR B CB  
5336 O OG1 . THR B 215 ? 0.5813 0.5697 0.5004 -0.0799 -0.0783 -0.0151 215 THR B OG1 
5337 C CG2 . THR B 215 ? 0.6032 0.5524 0.5029 -0.0591 -0.0842 -0.0217 215 THR B CG2 
5338 N N   . ALA B 216 ? 0.5740 0.5669 0.4918 -0.1024 -0.0762 0.0171  216 ALA B N   
5339 C CA  . ALA B 216 ? 0.5511 0.5430 0.4661 -0.1218 -0.0811 0.0181  216 ALA B CA  
5340 C C   . ALA B 216 ? 0.5996 0.6050 0.5144 -0.1271 -0.0843 0.0069  216 ALA B C   
5341 O O   . ALA B 216 ? 0.5153 0.5471 0.4376 -0.1381 -0.0857 0.0141  216 ALA B O   
5342 C CB  . ALA B 216 ? 0.5619 0.5754 0.4897 -0.1339 -0.0790 0.0384  216 ALA B CB  
5343 N N   . TRP B 217 ? 0.6159 0.6008 0.5191 -0.1198 -0.0857 -0.0100 217 TRP B N   
5344 C CA  . TRP B 217 ? 0.6025 0.5974 0.5052 -0.1170 -0.0846 -0.0208 217 TRP B CA  
5345 C C   . TRP B 217 ? 0.6284 0.6100 0.5126 -0.1310 -0.0904 -0.0291 217 TRP B C   
5346 O O   . TRP B 217 ? 0.6341 0.5840 0.5018 -0.1359 -0.0939 -0.0350 217 TRP B O   
5347 C CB  . TRP B 217 ? 0.5534 0.5374 0.4571 -0.0990 -0.0815 -0.0330 217 TRP B CB  
5348 C CG  . TRP B 217 ? 0.6013 0.5986 0.5099 -0.0940 -0.0767 -0.0419 217 TRP B CG  
5349 C CD1 . TRP B 217 ? 0.6142 0.6003 0.5083 -0.0947 -0.0762 -0.0527 217 TRP B CD1 
5350 C CD2 . TRP B 217 ? 0.5986 0.6193 0.5262 -0.0873 -0.0698 -0.0403 217 TRP B CD2 
5351 N NE1 . TRP B 217 ? 0.6037 0.6079 0.5088 -0.0873 -0.0684 -0.0566 217 TRP B NE1 
5352 C CE2 . TRP B 217 ? 0.5788 0.6042 0.5059 -0.0841 -0.0644 -0.0492 217 TRP B CE2 
5353 C CE3 . TRP B 217 ? 0.5835 0.6177 0.5262 -0.0836 -0.0662 -0.0326 217 TRP B CE3 
5354 C CZ2 . TRP B 217 ? 0.5861 0.6312 0.5311 -0.0790 -0.0551 -0.0494 217 TRP B CZ2 
5355 C CZ3 . TRP B 217 ? 0.5697 0.6200 0.5276 -0.0796 -0.0580 -0.0345 217 TRP B CZ3 
5356 C CH2 . TRP B 217 ? 0.5483 0.6048 0.5092 -0.0780 -0.0522 -0.0424 217 TRP B CH2 
5357 N N   . MET B 218 ? 0.6211 0.6244 0.5051 -0.1375 -0.0912 -0.0289 218 MET B N   
5358 C CA  . MET B 218 ? 0.6662 0.6577 0.5279 -0.1505 -0.0980 -0.0385 218 MET B CA  
5359 C C   . MET B 218 ? 0.6669 0.6467 0.5154 -0.1369 -0.0919 -0.0529 218 MET B C   
5360 O O   . MET B 218 ? 0.6628 0.6663 0.5205 -0.1287 -0.0852 -0.0506 218 MET B O   
5361 C CB  . MET B 218 ? 0.6174 0.6429 0.4843 -0.1650 -0.1042 -0.0277 218 MET B CB  
5362 C CG  . MET B 218 ? 0.6586 0.6985 0.5422 -0.1783 -0.1090 -0.0118 218 MET B CG  
5363 S SD  . MET B 218 ? 0.6932 0.7796 0.5864 -0.1959 -0.1187 0.0023  218 MET B SD  
5364 C CE  . MET B 218 ? 0.7499 0.8748 0.6692 -0.1770 -0.1056 0.0225  218 MET B CE  
5365 N N   . ASN B 219 ? 0.5987 0.5406 0.4254 -0.1333 -0.0920 -0.0664 219 ASN B N   
5366 C CA  . ASN B 219 ? 0.6119 0.5430 0.4291 -0.1163 -0.0834 -0.0782 219 ASN B CA  
5367 C C   . ASN B 219 ? 0.6574 0.5993 0.4595 -0.1196 -0.0822 -0.0820 219 ASN B C   
5368 O O   . ASN B 219 ? 0.6390 0.5734 0.4189 -0.1361 -0.0916 -0.0846 219 ASN B O   
5369 C CB  . ASN B 219 ? 0.6534 0.5385 0.4448 -0.1102 -0.0825 -0.0905 219 ASN B CB  
5370 C CG  . ASN B 219 ? 0.6552 0.5261 0.4559 -0.1051 -0.0835 -0.0857 219 ASN B CG  
5371 O OD1 . ASN B 219 ? 0.6548 0.5481 0.4816 -0.0935 -0.0808 -0.0790 219 ASN B OD1 
5372 N ND2 . ASN B 219 ? 0.6561 0.4873 0.4329 -0.1141 -0.0871 -0.0892 219 ASN B ND2 
5373 N N   . VAL B 220 ? 0.6878 0.6480 0.5020 -0.1043 -0.0706 -0.0820 220 VAL B N   
5374 C CA  . VAL B 220 ? 0.6953 0.6637 0.4937 -0.1012 -0.0649 -0.0847 220 VAL B CA  
5375 C C   . VAL B 220 ? 0.7035 0.6588 0.4989 -0.0812 -0.0509 -0.0939 220 VAL B C   
5376 O O   . VAL B 220 ? 0.6855 0.6618 0.5118 -0.0694 -0.0406 -0.0897 220 VAL B O   
5377 C CB  . VAL B 220 ? 0.6664 0.6748 0.4862 -0.1017 -0.0603 -0.0707 220 VAL B CB  
5378 C CG1 . VAL B 220 ? 0.6471 0.6607 0.4427 -0.0985 -0.0554 -0.0723 220 VAL B CG1 
5379 C CG2 . VAL B 220 ? 0.6116 0.6390 0.4436 -0.1168 -0.0714 -0.0580 220 VAL B CG2 
5380 N N   . LEU B 221 ? 0.7342 0.6540 0.4936 -0.0775 -0.0502 -0.1064 221 LEU B N   
5381 C CA  . LEU B 221 ? 0.7947 0.7038 0.5479 -0.0562 -0.0345 -0.1134 221 LEU B CA  
5382 C C   . LEU B 221 ? 0.7559 0.6862 0.5065 -0.0501 -0.0229 -0.1096 221 LEU B C   
5383 O O   . LEU B 221 ? 0.7993 0.7410 0.5373 -0.0620 -0.0297 -0.1051 221 LEU B O   
5384 C CB  . LEU B 221 ? 0.8105 0.6687 0.5189 -0.0524 -0.0352 -0.1274 221 LEU B CB  
5385 C CG  . LEU B 221 ? 0.8256 0.6594 0.5380 -0.0509 -0.0402 -0.1297 221 LEU B CG  
5386 C CD1 . LEU B 221 ? 0.8509 0.6261 0.5127 -0.0543 -0.0432 -0.1427 221 LEU B CD1 
5387 C CD2 . LEU B 221 ? 0.7609 0.6109 0.5054 -0.0273 -0.0285 -0.1269 221 LEU B CD2 
5388 N N   . PRO B 222 ? 0.6821 0.6203 0.4456 -0.0303 -0.0045 -0.1099 222 PRO B N   
5389 C CA  . PRO B 222 ? 0.7194 0.6509 0.4991 -0.0128 0.0047  -0.1142 222 PRO B CA  
5390 C C   . PRO B 222 ? 0.7023 0.6688 0.5366 -0.0106 0.0053  -0.1068 222 PRO B C   
5391 O O   . PRO B 222 ? 0.6837 0.6504 0.5345 0.0035  0.0092  -0.1098 222 PRO B O   
5392 C CB  . PRO B 222 ? 0.7181 0.6478 0.4851 0.0059  0.0253  -0.1159 222 PRO B CB  
5393 C CG  . PRO B 222 ? 0.6872 0.6466 0.4653 -0.0008 0.0309  -0.1059 222 PRO B CG  
5394 C CD  . PRO B 222 ? 0.6972 0.6531 0.4577 -0.0227 0.0105  -0.1045 222 PRO B CD  
5395 N N   . HIS B 223 ? 0.6573 0.6525 0.5179 -0.0232 0.0013  -0.0976 223 HIS B N   
5396 C CA  . HIS B 223 ? 0.6023 0.6275 0.5098 -0.0223 0.0027  -0.0924 223 HIS B CA  
5397 C C   . HIS B 223 ? 0.5969 0.6246 0.5150 -0.0347 -0.0131 -0.0887 223 HIS B C   
5398 O O   . HIS B 223 ? 0.5499 0.5955 0.5002 -0.0327 -0.0148 -0.0874 223 HIS B O   
5399 C CB  . HIS B 223 ? 0.5968 0.6508 0.5284 -0.0237 0.0171  -0.0842 223 HIS B CB  
5400 C CG  . HIS B 223 ? 0.6078 0.6642 0.5354 -0.0100 0.0367  -0.0850 223 HIS B CG  
5401 N ND1 . HIS B 223 ? 0.5767 0.6440 0.5019 -0.0104 0.0512  -0.0771 223 HIS B ND1 
5402 C CD2 . HIS B 223 ? 0.6213 0.6704 0.5460 0.0067  0.0463  -0.0910 223 HIS B CD2 
5403 C CE1 . HIS B 223 ? 0.6083 0.6745 0.5295 0.0048  0.0692  -0.0784 223 HIS B CE1 
5404 N NE2 . HIS B 223 ? 0.6350 0.6911 0.5565 0.0155  0.0668  -0.0867 223 HIS B NE2 
5405 N N   . LEU B 224 ? 0.6203 0.6331 0.5135 -0.0477 -0.0245 -0.0864 224 LEU B N   
5406 C CA  . LEU B 224 ? 0.5699 0.5887 0.4746 -0.0586 -0.0358 -0.0794 224 LEU B CA  
5407 C C   . LEU B 224 ? 0.5877 0.5776 0.4692 -0.0645 -0.0484 -0.0827 224 LEU B C   
5408 O O   . LEU B 224 ? 0.5803 0.5694 0.4556 -0.0784 -0.0573 -0.0759 224 LEU B O   
5409 C CB  . LEU B 224 ? 0.5444 0.5822 0.4515 -0.0696 -0.0348 -0.0681 224 LEU B CB  
5410 C CG  . LEU B 224 ? 0.5838 0.6461 0.5175 -0.0641 -0.0203 -0.0631 224 LEU B CG  
5411 C CD1 . LEU B 224 ? 0.5469 0.6248 0.4771 -0.0701 -0.0149 -0.0506 224 LEU B CD1 
5412 C CD2 . LEU B 224 ? 0.5324 0.6047 0.4973 -0.0619 -0.0211 -0.0633 224 LEU B CD2 
5413 N N   . SER B 225 ? 0.5839 0.5495 0.4527 -0.0536 -0.0478 -0.0918 225 SER B N   
5414 C CA  . SER B 225 ? 0.6345 0.5712 0.4875 -0.0561 -0.0570 -0.0934 225 SER B CA  
5415 C C   . SER B 225 ? 0.6112 0.5610 0.4900 -0.0502 -0.0612 -0.0880 225 SER B C   
5416 O O   . SER B 225 ? 0.5830 0.5557 0.4878 -0.0386 -0.0572 -0.0890 225 SER B O   
5417 C CB  . SER B 225 ? 0.6315 0.5330 0.4576 -0.0433 -0.0525 -0.1040 225 SER B CB  
5418 O OG  . SER B 225 ? 0.6816 0.5469 0.4836 -0.0508 -0.0600 -0.1052 225 SER B OG  
5419 N N   . ALA B 226 ? 0.6179 0.5529 0.4885 -0.0587 -0.0695 -0.0825 226 ALA B N   
5420 C CA  . ALA B 226 ? 0.6011 0.5475 0.4903 -0.0536 -0.0736 -0.0760 226 ALA B CA  
5421 C C   . ALA B 226 ? 0.5938 0.5423 0.4934 -0.0328 -0.0729 -0.0822 226 ALA B C   
5422 O O   . ALA B 226 ? 0.5965 0.5733 0.5224 -0.0269 -0.0728 -0.0826 226 ALA B O   
5423 C CB  . ALA B 226 ? 0.5833 0.5072 0.4576 -0.0626 -0.0796 -0.0685 226 ALA B CB  
5424 N N   . VAL B 227 ? 0.6026 0.5211 0.4814 -0.0214 -0.0723 -0.0870 227 VAL B N   
5425 C CA  . VAL B 227 ? 0.5829 0.5065 0.4712 0.0013  -0.0726 -0.0908 227 VAL B CA  
5426 C C   . VAL B 227 ? 0.6170 0.5757 0.5333 0.0093  -0.0668 -0.0960 227 VAL B C   
5427 O O   . VAL B 227 ? 0.5973 0.5853 0.5413 0.0190  -0.0707 -0.0969 227 VAL B O   
5428 C CB  . VAL B 227 ? 0.6675 0.5486 0.5242 0.0142  -0.0693 -0.0939 227 VAL B CB  
5429 C CG1 . VAL B 227 ? 0.6601 0.5087 0.4950 0.0074  -0.0741 -0.0869 227 VAL B CG1 
5430 C CG2 . VAL B 227 ? 0.6912 0.5487 0.5241 0.0089  -0.0609 -0.1008 227 VAL B CG2 
5431 N N   . GLU B 228 ? 0.6172 0.5741 0.5269 0.0043  -0.0576 -0.0994 228 GLU B N   
5432 C CA  . GLU B 228 ? 0.6236 0.6106 0.5581 0.0120  -0.0479 -0.1027 228 GLU B CA  
5433 C C   . GLU B 228 ? 0.5411 0.5680 0.5133 0.0032  -0.0496 -0.0995 228 GLU B C   
5434 O O   . GLU B 228 ? 0.5409 0.5980 0.5453 0.0120  -0.0491 -0.1018 228 GLU B O   
5435 C CB  . GLU B 228 ? 0.6091 0.5811 0.5209 0.0064  -0.0375 -0.1052 228 GLU B CB  
5436 C CG  . GLU B 228 ? 0.5841 0.5857 0.5189 0.0113  -0.0242 -0.1057 228 GLU B CG  
5437 C CD  . GLU B 228 ? 0.6697 0.6570 0.5773 0.0037  -0.0155 -0.1066 228 GLU B CD  
5438 O OE1 . GLU B 228 ? 0.6611 0.6303 0.5437 -0.0124 -0.0232 -0.1052 228 GLU B OE1 
5439 O OE2 . GLU B 228 ? 0.6631 0.6589 0.5743 0.0149  -0.0009 -0.1080 228 GLU B OE2 
5440 N N   . PHE B 229 ? 0.5533 0.5811 0.5221 -0.0147 -0.0509 -0.0942 229 PHE B N   
5441 C CA  . PHE B 229 ? 0.5432 0.6006 0.5417 -0.0230 -0.0493 -0.0911 229 PHE B CA  
5442 C C   . PHE B 229 ? 0.5587 0.6234 0.5700 -0.0221 -0.0610 -0.0907 229 PHE B C   
5443 O O   . PHE B 229 ? 0.5208 0.6105 0.5609 -0.0235 -0.0610 -0.0932 229 PHE B O   
5444 C CB  . PHE B 229 ? 0.5492 0.6048 0.5373 -0.0385 -0.0448 -0.0836 229 PHE B CB  
5445 C CG  . PHE B 229 ? 0.5880 0.6676 0.6023 -0.0454 -0.0383 -0.0798 229 PHE B CG  
5446 C CD1 . PHE B 229 ? 0.5538 0.6516 0.5875 -0.0440 -0.0246 -0.0811 229 PHE B CD1 
5447 C CD2 . PHE B 229 ? 0.5636 0.6444 0.5821 -0.0523 -0.0439 -0.0746 229 PHE B CD2 
5448 C CE1 . PHE B 229 ? 0.5249 0.6393 0.5818 -0.0516 -0.0167 -0.0776 229 PHE B CE1 
5449 C CE2 . PHE B 229 ? 0.5081 0.6035 0.5463 -0.0585 -0.0365 -0.0719 229 PHE B CE2 
5450 C CZ  . PHE B 229 ? 0.5543 0.6655 0.6121 -0.0591 -0.0229 -0.0736 229 PHE B CZ  
5451 N N   . HIS B 230 ? 0.5126 0.5543 0.5019 -0.0201 -0.0704 -0.0879 230 HIS B N   
5452 C CA  . HIS B 230 ? 0.5106 0.5565 0.5060 -0.0166 -0.0809 -0.0873 230 HIS B CA  
5453 C C   . HIS B 230 ? 0.5032 0.5677 0.5178 -0.0010 -0.0871 -0.0952 230 HIS B C   
5454 O O   . HIS B 230 ? 0.4844 0.5721 0.5218 -0.0024 -0.0930 -0.0991 230 HIS B O   
5455 C CB  . HIS B 230 ? 0.5075 0.5235 0.4738 -0.0161 -0.0868 -0.0805 230 HIS B CB  
5456 C CG  . HIS B 230 ? 0.5334 0.5382 0.4859 -0.0321 -0.0823 -0.0715 230 HIS B CG  
5457 N ND1 . HIS B 230 ? 0.5216 0.5001 0.4503 -0.0361 -0.0844 -0.0648 230 HIS B ND1 
5458 C CD2 . HIS B 230 ? 0.5188 0.5376 0.4794 -0.0448 -0.0756 -0.0670 230 HIS B CD2 
5459 C CE1 . HIS B 230 ? 0.5331 0.5151 0.4592 -0.0515 -0.0810 -0.0570 230 HIS B CE1 
5460 N NE2 . HIS B 230 ? 0.5142 0.5202 0.4577 -0.0554 -0.0757 -0.0578 230 HIS B NE2 
5461 N N   . SER B 231 ? 0.5345 0.5905 0.5408 0.0141  -0.0856 -0.0978 231 SER B N   
5462 C CA  . SER B 231 ? 0.5169 0.5990 0.5463 0.0311  -0.0907 -0.1034 231 SER B CA  
5463 C C   . SER B 231 ? 0.5195 0.6413 0.5895 0.0245  -0.0848 -0.1079 231 SER B C   
5464 O O   . SER B 231 ? 0.4766 0.6306 0.5763 0.0268  -0.0936 -0.1126 231 SER B O   
5465 C CB  . SER B 231 ? 0.5813 0.6451 0.5928 0.0509  -0.0858 -0.1036 231 SER B CB  
5466 O OG  . SER B 231 ? 0.5822 0.6370 0.5873 0.0475  -0.0710 -0.1043 231 SER B OG  
5467 N N   . ALA B 232 ? 0.5132 0.6338 0.5847 0.0154  -0.0698 -0.1062 232 ALA B N   
5468 C CA  . ALA B 232 ? 0.5164 0.6723 0.6267 0.0088  -0.0608 -0.1085 232 ALA B CA  
5469 C C   . ALA B 232 ? 0.4742 0.6458 0.6052 -0.0075 -0.0674 -0.1103 232 ALA B C   
5470 O O   . ALA B 232 ? 0.4589 0.6639 0.6280 -0.0113 -0.0685 -0.1152 232 ALA B O   
5471 C CB  . ALA B 232 ? 0.4947 0.6414 0.5958 0.0028  -0.0426 -0.1048 232 ALA B CB  
5472 N N   . TRP B 233 ? 0.5355 0.6827 0.6421 -0.0181 -0.0704 -0.1061 233 TRP B N   
5473 C CA  . TRP B 233 ? 0.5011 0.6544 0.6191 -0.0315 -0.0746 -0.1076 233 TRP B CA  
5474 C C   . TRP B 233 ? 0.5154 0.6824 0.6443 -0.0254 -0.0928 -0.1156 233 TRP B C   
5475 O O   . TRP B 233 ? 0.4577 0.6462 0.6137 -0.0347 -0.0971 -0.1227 233 TRP B O   
5476 C CB  . TRP B 233 ? 0.4997 0.6239 0.5865 -0.0393 -0.0727 -0.0991 233 TRP B CB  
5477 C CG  . TRP B 233 ? 0.5513 0.6752 0.6447 -0.0528 -0.0690 -0.0980 233 TRP B CG  
5478 C CD1 . TRP B 233 ? 0.5175 0.6432 0.6188 -0.0637 -0.0533 -0.0930 233 TRP B CD1 
5479 C CD2 . TRP B 233 ? 0.5143 0.6314 0.6025 -0.0550 -0.0800 -0.1018 233 TRP B CD2 
5480 N NE1 . TRP B 233 ? 0.5086 0.6264 0.6098 -0.0727 -0.0525 -0.0931 233 TRP B NE1 
5481 C CE2 . TRP B 233 ? 0.5294 0.6411 0.6218 -0.0680 -0.0692 -0.0994 233 TRP B CE2 
5482 C CE3 . TRP B 233 ? 0.5492 0.6610 0.6253 -0.0455 -0.0971 -0.1067 233 TRP B CE3 
5483 C CZ2 . TRP B 233 ? 0.5333 0.6317 0.6167 -0.0726 -0.0747 -0.1030 233 TRP B CZ2 
5484 C CZ3 . TRP B 233 ? 0.5526 0.6538 0.6195 -0.0499 -0.1039 -0.1104 233 TRP B CZ3 
5485 C CH2 . TRP B 233 ? 0.5414 0.6347 0.6113 -0.0638 -0.0926 -0.1092 233 TRP B CH2 
5486 N N   . ALA B 234 ? 0.5187 0.6726 0.6254 -0.0096 -0.1038 -0.1148 234 ALA B N   
5487 C CA  . ALA B 234 ? 0.5201 0.6886 0.6332 0.0002  -0.1223 -0.1216 234 ALA B CA  
5488 C C   . ALA B 234 ? 0.5419 0.7556 0.6994 0.0027  -0.1257 -0.1294 234 ALA B C   
5489 O O   . ALA B 234 ? 0.5163 0.7542 0.6944 -0.0019 -0.1399 -0.1380 234 ALA B O   
5490 C CB  . ALA B 234 ? 0.5000 0.6465 0.5815 0.0205  -0.1297 -0.1172 234 ALA B CB  
5491 N N   . MET B 235 ? 0.6004 0.8267 0.7733 0.0092  -0.1123 -0.1266 235 MET B N   
5492 C CA  . MET B 235 ? 0.5813 0.8552 0.8007 0.0135  -0.1126 -0.1312 235 MET B CA  
5493 C C   . MET B 235 ? 0.5274 0.8261 0.7852 -0.0102 -0.1065 -0.1359 235 MET B C   
5494 O O   . MET B 235 ? 0.5185 0.8573 0.8159 -0.0155 -0.1170 -0.1434 235 MET B O   
5495 C CB  . MET B 235 ? 0.5661 0.8417 0.7865 0.0297  -0.0967 -0.1254 235 MET B CB  
5496 C CG  . MET B 235 ? 0.6087 0.9373 0.8786 0.0388  -0.0960 -0.1274 235 MET B CG  
5497 S SD  . MET B 235 ? 0.6629 0.9888 0.9227 0.0702  -0.0817 -0.1200 235 MET B SD  
5498 C CE  . MET B 235 ? 0.6616 0.9470 0.8696 0.0906  -0.0972 -0.1185 235 MET B CE  
5499 N N   . GLY B 236 ? 0.4298 0.7059 0.6771 -0.0246 -0.0892 -0.1311 236 GLY B N   
5500 C CA  . GLY B 236 ? 0.3895 0.6818 0.6692 -0.0463 -0.0793 -0.1338 236 GLY B CA  
5501 C C   . GLY B 236 ? 0.4136 0.7016 0.6942 -0.0622 -0.0939 -0.1424 236 GLY B C   
5502 O O   . GLY B 236 ? 0.3668 0.6808 0.6852 -0.0783 -0.0955 -0.1501 236 GLY B O   
5503 N N   . MET B 237 ? 0.5619 0.8144 0.7995 -0.0589 -0.1033 -0.1411 237 MET B N   
5504 C CA  . MET B 237 ? 0.5589 0.7992 0.7863 -0.0700 -0.1169 -0.1492 237 MET B CA  
5505 C C   . MET B 237 ? 0.5752 0.8404 0.8125 -0.0618 -0.1428 -0.1602 237 MET B C   
5506 O O   . MET B 237 ? 0.5812 0.8454 0.8186 -0.0734 -0.1564 -0.1709 237 MET B O   
5507 C CB  . MET B 237 ? 0.5772 0.7720 0.7543 -0.0659 -0.1151 -0.1413 237 MET B CB  
5508 C CG  . MET B 237 ? 0.5698 0.7403 0.7351 -0.0776 -0.0939 -0.1319 237 MET B CG  
5509 S SD  . MET B 237 ? 0.6098 0.7999 0.8177 -0.0981 -0.0767 -0.1356 237 MET B SD  
5510 C CE  . MET B 237 ? 0.5805 0.7511 0.7817 -0.1151 -0.0842 -0.1464 237 MET B CE  
5511 N N   . ARG B 238 ? 0.5072 0.7925 0.7493 -0.0408 -0.1499 -0.1577 238 ARG B N   
5512 C CA  . ARG B 238 ? 0.4964 0.8123 0.7501 -0.0288 -0.1745 -0.1660 238 ARG B CA  
5513 C C   . ARG B 238 ? 0.5340 0.8190 0.7422 -0.0213 -0.1921 -0.1689 238 ARG B C   
5514 O O   . ARG B 238 ? 0.5690 0.8688 0.7815 -0.0254 -0.2131 -0.1807 238 ARG B O   
5515 C CB  . ARG B 238 ? 0.4649 0.8284 0.7720 -0.0469 -0.1832 -0.1781 238 ARG B CB  
5516 C CG  . ARG B 238 ? 0.4461 0.8532 0.8037 -0.0458 -0.1696 -0.1739 238 ARG B CG  
5517 C CD  . ARG B 238 ? 0.4623 0.9189 0.8786 -0.0679 -0.1769 -0.1849 238 ARG B CD  
5518 N NE  . ARG B 238 ? 0.5361 0.9672 0.9466 -0.0970 -0.1762 -0.1941 238 ARG B NE  
5519 C CZ  . ARG B 238 ? 0.5848 1.0372 1.0188 -0.1173 -0.1954 -0.2096 238 ARG B CZ  
5520 N NH1 . ARG B 238 ? 0.5444 1.0543 1.0190 -0.1145 -0.2171 -0.2172 238 ARG B NH1 
5521 N NH2 . ARG B 238 ? 0.5352 0.9507 0.9520 -0.1413 -0.1919 -0.2175 238 ARG B NH2 
5522 N N   . VAL B 239 ? 0.6081 0.8507 0.7719 -0.0097 -0.1838 -0.1579 239 VAL B N   
5523 C CA  . VAL B 239 ? 0.5992 0.8101 0.7175 0.0012  -0.1962 -0.1568 239 VAL B CA  
5524 C C   . VAL B 239 ? 0.6374 0.8278 0.7265 0.0248  -0.1924 -0.1447 239 VAL B C   
5525 O O   . VAL B 239 ? 0.6340 0.8205 0.7282 0.0276  -0.1768 -0.1370 239 VAL B O   
5526 C CB  . VAL B 239 ? 0.6069 0.7775 0.6965 -0.0137 -0.1862 -0.1539 239 VAL B CB  
5527 C CG1 . VAL B 239 ? 0.5909 0.7722 0.7034 -0.0370 -0.1879 -0.1662 239 VAL B CG1 
5528 C CG2 . VAL B 239 ? 0.6277 0.7768 0.7095 -0.0176 -0.1629 -0.1403 239 VAL B CG2 
5529 N N   . ASN B 240 ? 0.5592 0.7319 0.6138 0.0417  -0.2058 -0.1432 240 ASN B N   
5530 C CA  . ASN B 240 ? 0.5680 0.7073 0.5867 0.0604  -0.1986 -0.1301 240 ASN B CA  
5531 C C   . ASN B 240 ? 0.5480 0.6499 0.5460 0.0468  -0.1799 -0.1199 240 ASN B C   
5532 O O   . ASN B 240 ? 0.5620 0.6567 0.5600 0.0295  -0.1757 -0.1217 240 ASN B O   
5533 C CB  . ASN B 240 ? 0.6026 0.7266 0.5852 0.0806  -0.2143 -0.1289 240 ASN B CB  
5534 C CG  . ASN B 240 ? 0.6125 0.7737 0.6102 0.1006  -0.2333 -0.1352 240 ASN B CG  
5535 O OD1 . ASN B 240 ? 0.5811 0.7724 0.6106 0.1060  -0.2305 -0.1356 240 ASN B OD1 
5536 N ND2 . ASN B 240 ? 0.5884 0.7487 0.5616 0.1139  -0.2527 -0.1394 240 ASN B ND2 
5537 N N   . PHE B 241 ? 0.6073 0.6842 0.5858 0.0554  -0.1689 -0.1088 241 PHE B N   
5538 C CA  . PHE B 241 ? 0.6198 0.6700 0.5858 0.0409  -0.1521 -0.0990 241 PHE B CA  
5539 C C   . PHE B 241 ? 0.6429 0.6581 0.5763 0.0523  -0.1465 -0.0873 241 PHE B C   
5540 O O   . PHE B 241 ? 0.6747 0.6863 0.6053 0.0658  -0.1455 -0.0868 241 PHE B O   
5541 C CB  . PHE B 241 ? 0.5755 0.6423 0.5693 0.0273  -0.1400 -0.1012 241 PHE B CB  
5542 C CG  . PHE B 241 ? 0.5680 0.6214 0.5575 0.0084  -0.1266 -0.0941 241 PHE B CG  
5543 C CD1 . PHE B 241 ? 0.5885 0.6162 0.5565 0.0057  -0.1175 -0.0835 241 PHE B CD1 
5544 C CD2 . PHE B 241 ? 0.5564 0.6237 0.5639 -0.0067 -0.1229 -0.0978 241 PHE B CD2 
5545 C CE1 . PHE B 241 ? 0.5704 0.5928 0.5367 -0.0104 -0.1069 -0.0760 241 PHE B CE1 
5546 C CE2 . PHE B 241 ? 0.5530 0.6097 0.5554 -0.0204 -0.1098 -0.0892 241 PHE B CE2 
5547 C CZ  . PHE B 241 ? 0.5734 0.6110 0.5562 -0.0215 -0.1027 -0.0779 241 PHE B CZ  
5548 N N   . LEU B 242 ? 0.5683 0.5566 0.4773 0.0472  -0.1411 -0.0771 242 LEU B N   
5549 C CA  . LEU B 242 ? 0.6005 0.5540 0.4800 0.0542  -0.1344 -0.0644 242 LEU B CA  
5550 C C   . LEU B 242 ? 0.6170 0.5599 0.4975 0.0337  -0.1211 -0.0554 242 LEU B C   
5551 O O   . LEU B 242 ? 0.5783 0.5164 0.4526 0.0258  -0.1169 -0.0475 242 LEU B O   
5552 C CB  . LEU B 242 ? 0.6269 0.5617 0.4774 0.0688  -0.1398 -0.0579 242 LEU B CB  
5553 C CG  . LEU B 242 ? 0.6537 0.5916 0.4921 0.0945  -0.1534 -0.0628 242 LEU B CG  
5554 C CD1 . LEU B 242 ? 0.6317 0.6107 0.5026 0.0947  -0.1655 -0.0785 242 LEU B CD1 
5555 C CD2 . LEU B 242 ? 0.6746 0.5969 0.4811 0.1095  -0.1607 -0.0585 242 LEU B CD2 
5556 N N   . ALA B 243 ? 0.6964 0.6357 0.5826 0.0264  -0.1146 -0.0563 243 ALA B N   
5557 C CA  . ALA B 243 ? 0.6381 0.5726 0.5263 0.0062  -0.1049 -0.0497 243 ALA B CA  
5558 C C   . ALA B 243 ? 0.6560 0.5570 0.5207 0.0047  -0.0999 -0.0392 243 ALA B C   
5559 O O   . ALA B 243 ? 0.6775 0.5577 0.5292 0.0135  -0.0992 -0.0422 243 ALA B O   
5560 C CB  . ALA B 243 ? 0.6125 0.5616 0.5173 -0.0016 -0.1015 -0.0585 243 ALA B CB  
5561 N N   . SER B 244 ? 0.6013 0.4964 0.4609 -0.0060 -0.0949 -0.0262 244 SER B N   
5562 C CA  . SER B 244 ? 0.6471 0.5131 0.4892 -0.0113 -0.0889 -0.0142 244 SER B CA  
5563 C C   . SER B 244 ? 0.6427 0.5185 0.4959 -0.0360 -0.0842 -0.0080 244 SER B C   
5564 O O   . SER B 244 ? 0.6223 0.5187 0.4871 -0.0436 -0.0815 0.0009  244 SER B O   
5565 C CB  . SER B 244 ? 0.6548 0.5080 0.4821 0.0000  -0.0863 -0.0013 244 SER B CB  
5566 O OG  . SER B 244 ? 0.6864 0.5227 0.5079 -0.0131 -0.0775 0.0138  244 SER B OG  
5567 N N   . ASN B 245 ? 0.7676 0.6272 0.6145 -0.0475 -0.0834 -0.0123 245 ASN B N   
5568 C CA  . ASN B 245 ? 0.7220 0.5945 0.5781 -0.0707 -0.0830 -0.0116 245 ASN B CA  
5569 C C   . ASN B 245 ? 0.7573 0.6097 0.6055 -0.0884 -0.0800 -0.0008 245 ASN B C   
5570 O O   . ASN B 245 ? 0.8073 0.6245 0.6378 -0.0834 -0.0767 0.0016  245 ASN B O   
5571 C CB  . ASN B 245 ? 0.7665 0.6353 0.6186 -0.0711 -0.0854 -0.0280 245 ASN B CB  
5572 C CG  . ASN B 245 ? 0.7426 0.6318 0.6029 -0.0905 -0.0866 -0.0299 245 ASN B CG  
5573 O OD1 . ASN B 245 ? 0.7389 0.6453 0.6085 -0.1065 -0.0870 -0.0188 245 ASN B OD1 
5574 N ND2 . ASN B 245 ? 0.8121 0.7011 0.6685 -0.0870 -0.0868 -0.0432 245 ASN B ND2 
5575 N N   . ILE B 246 ? 0.6181 0.4947 0.4808 -0.1093 -0.0809 0.0066  246 ILE B N   
5576 C CA  . ILE B 246 ? 0.6557 0.5195 0.5161 -0.1323 -0.0807 0.0141  246 ILE B CA  
5577 C C   . ILE B 246 ? 0.6712 0.5014 0.5106 -0.1417 -0.0844 -0.0020 246 ILE B C   
5578 O O   . ILE B 246 ? 0.6739 0.5055 0.5067 -0.1356 -0.0877 -0.0171 246 ILE B O   
5579 C CB  . ILE B 246 ? 0.6279 0.5336 0.5113 -0.1519 -0.0833 0.0254  246 ILE B CB  
5580 C CG1 . ILE B 246 ? 0.5949 0.5249 0.4945 -0.1420 -0.0759 0.0448  246 ILE B CG1 
5581 C CG2 . ILE B 246 ? 0.5878 0.4848 0.4705 -0.1809 -0.0878 0.0271  246 ILE B CG2 
5582 C CD1 . ILE B 246 ? 0.6292 0.5408 0.5275 -0.1441 -0.0678 0.0615  246 ILE B CD1 
5583 N N   . HIS B 247 ? 0.6830 0.4793 0.5101 -0.1560 -0.0819 0.0015  247 HIS B N   
5584 C CA  . HIS B 247 ? 0.7289 0.4844 0.5311 -0.1685 -0.0841 -0.0131 247 HIS B CA  
5585 C C   . HIS B 247 ? 0.7439 0.5115 0.5550 -0.2037 -0.0911 -0.0104 247 HIS B C   
5586 O O   . HIS B 247 ? 0.7225 0.4869 0.5440 -0.2206 -0.0881 0.0036  247 HIS B O   
5587 C CB  . HIS B 247 ? 0.7503 0.4496 0.5271 -0.1584 -0.0750 -0.0128 247 HIS B CB  
5588 C CG  . HIS B 247 ? 0.8145 0.4636 0.5599 -0.1685 -0.0748 -0.0288 247 HIS B CG  
5589 N ND1 . HIS B 247 ? 0.8202 0.4507 0.5442 -0.1494 -0.0743 -0.0452 247 HIS B ND1 
5590 C CD2 . HIS B 247 ? 0.8882 0.5004 0.6188 -0.1963 -0.0745 -0.0312 247 HIS B CD2 
5591 C CE1 . HIS B 247 ? 0.8642 0.4438 0.5570 -0.1623 -0.0724 -0.0570 247 HIS B CE1 
5592 N NE2 . HIS B 247 ? 0.8941 0.4600 0.5895 -0.1922 -0.0733 -0.0498 247 HIS B NE2 
5593 N N   . TYR B 248 ? 0.7780 0.5605 0.5849 -0.2145 -0.1005 -0.0234 248 TYR B N   
5594 C CA  . TYR B 248 ? 0.7682 0.5707 0.5832 -0.2469 -0.1112 -0.0228 248 TYR B CA  
5595 C C   . TYR B 248 ? 0.8207 0.6130 0.6109 -0.2513 -0.1195 -0.0436 248 TYR B C   
5596 O O   . TYR B 248 ? 0.7549 0.5895 0.5557 -0.2514 -0.1262 -0.0442 248 TYR B O   
5597 C CB  . TYR B 248 ? 0.7193 0.5859 0.5719 -0.2500 -0.1137 -0.0039 248 TYR B CB  
5598 C CG  . TYR B 248 ? 0.7196 0.6120 0.5905 -0.2832 -0.1228 0.0054  248 TYR B CG  
5599 C CD1 . TYR B 248 ? 0.7011 0.5860 0.5867 -0.2984 -0.1176 0.0204  248 TYR B CD1 
5600 C CD2 . TYR B 248 ? 0.7676 0.6946 0.6423 -0.2994 -0.1366 0.0001  248 TYR B CD2 
5601 C CE1 . TYR B 248 ? 0.7161 0.6314 0.6249 -0.3321 -0.1270 0.0296  248 TYR B CE1 
5602 C CE2 . TYR B 248 ? 0.7844 0.7417 0.6786 -0.3305 -0.1477 0.0084  248 TYR B CE2 
5603 C CZ  . TYR B 248 ? 0.7561 0.7096 0.6696 -0.3480 -0.1434 0.0229  248 TYR B CZ  
5604 O OH  . TYR B 248 ? 0.8126 0.8034 0.7509 -0.3814 -0.1558 0.0313  248 TYR B OH  
5605 N N   . PRO B 249 ? 0.8688 0.6021 0.6224 -0.2533 -0.1175 -0.0602 249 PRO B N   
5606 C CA  . PRO B 249 ? 0.8584 0.5751 0.5816 -0.2518 -0.1223 -0.0807 249 PRO B CA  
5607 C C   . PRO B 249 ? 0.8530 0.6075 0.5818 -0.2766 -0.1377 -0.0831 249 PRO B C   
5608 O O   . PRO B 249 ? 0.8217 0.5933 0.5405 -0.2672 -0.1408 -0.0917 249 PRO B O   
5609 C CB  . PRO B 249 ? 0.9135 0.5552 0.5955 -0.2581 -0.1176 -0.0948 249 PRO B CB  
5610 C CG  . PRO B 249 ? 0.9246 0.5449 0.6160 -0.2459 -0.1054 -0.0810 249 PRO B CG  
5611 C CD  . PRO B 249 ? 0.8662 0.5421 0.6015 -0.2557 -0.1087 -0.0599 249 PRO B CD  
5612 N N   . SER B 250 ? 0.8774 0.6485 0.6239 -0.3071 -0.1469 -0.0739 250 SER B N   
5613 C CA  . SER B 250 ? 0.8602 0.6789 0.6206 -0.3322 -0.1638 -0.0715 250 SER B CA  
5614 C C   . SER B 250 ? 0.8347 0.7094 0.6113 -0.3126 -0.1647 -0.0649 250 SER B C   
5615 O O   . SER B 250 ? 0.8475 0.7401 0.6100 -0.3198 -0.1761 -0.0736 250 SER B O   
5616 C CB  . SER B 250 ? 0.8913 0.7396 0.6891 -0.3567 -0.1673 -0.0518 250 SER B CB  
5617 O OG  . SER B 250 ? 0.8785 0.7732 0.6942 -0.3768 -0.1811 -0.0479 250 SER B OG  
5618 N N   . LYS B 251 ? 0.7701 0.6695 0.5732 -0.2878 -0.1525 -0.0498 251 LYS B N   
5619 C CA  . LYS B 251 ? 0.7211 0.6673 0.5404 -0.2681 -0.1495 -0.0422 251 LYS B CA  
5620 C C   . LYS B 251 ? 0.7424 0.6674 0.5478 -0.2377 -0.1372 -0.0521 251 LYS B C   
5621 O O   . LYS B 251 ? 0.7228 0.6804 0.5462 -0.2193 -0.1305 -0.0439 251 LYS B O   
5622 C CB  . LYS B 251 ? 0.7166 0.7090 0.5766 -0.2637 -0.1445 -0.0174 251 LYS B CB  
5623 C CG  . LYS B 251 ? 0.7095 0.7418 0.5928 -0.2908 -0.1560 -0.0031 251 LYS B CG  
5624 C CD  . LYS B 251 ? 0.7289 0.7990 0.6490 -0.2811 -0.1463 0.0226  251 LYS B CD  
5625 C CE  . LYS B 251 ? 0.7241 0.8375 0.6568 -0.2602 -0.1413 0.0327  251 LYS B CE  
5626 N NZ  . LYS B 251 ? 0.7693 0.9267 0.7061 -0.2742 -0.1552 0.0358  251 LYS B NZ  
5627 N N   . LYS B 252 ? 0.7584 0.6299 0.5327 -0.2321 -0.1334 -0.0689 252 LYS B N   
5628 C CA  . LYS B 252 ? 0.7459 0.6011 0.5110 -0.2028 -0.1215 -0.0772 252 LYS B CA  
5629 C C   . LYS B 252 ? 0.6953 0.5661 0.4887 -0.1833 -0.1122 -0.0647 252 LYS B C   
5630 O O   . LYS B 252 ? 0.6696 0.5557 0.4729 -0.1620 -0.1049 -0.0655 252 LYS B O   
5631 C CB  . LYS B 252 ? 0.7210 0.6003 0.4804 -0.1930 -0.1205 -0.0828 252 LYS B CB  
5632 C CG  . LYS B 252 ? 0.7643 0.6454 0.4985 -0.2132 -0.1331 -0.0914 252 LYS B CG  
5633 C CD  . LYS B 252 ? 0.7874 0.6093 0.4763 -0.2178 -0.1343 -0.1118 252 LYS B CD  
5634 C CE  . LYS B 252 ? 0.9629 0.7781 0.6235 -0.2473 -0.1520 -0.1218 252 LYS B CE  
5635 N NZ  . LYS B 252 ? 0.9297 0.7190 0.5858 -0.2783 -0.1630 -0.1240 252 LYS B NZ  
5636 N N   . MET B 253 ? 0.7067 0.5737 0.5127 -0.1915 -0.1126 -0.0530 253 MET B N   
5637 C CA  . MET B 253 ? 0.6705 0.5444 0.4955 -0.1730 -0.1046 -0.0419 253 MET B CA  
5638 C C   . MET B 253 ? 0.6849 0.5092 0.4890 -0.1609 -0.0991 -0.0491 253 MET B C   
5639 O O   . MET B 253 ? 0.7156 0.5078 0.5078 -0.1736 -0.0990 -0.0468 253 MET B O   
5640 C CB  . MET B 253 ? 0.6452 0.5471 0.4947 -0.1848 -0.1057 -0.0221 253 MET B CB  
5641 C CG  . MET B 253 ? 0.6580 0.6108 0.5303 -0.1830 -0.1063 -0.0122 253 MET B CG  
5642 S SD  . MET B 253 ? 0.6883 0.6810 0.5896 -0.1971 -0.1068 0.0131  253 MET B SD  
5643 C CE  . MET B 253 ? 0.7194 0.6751 0.6140 -0.2120 -0.1065 0.0165  253 MET B CE  
5644 N N   . THR B 254 ? 0.6197 0.4382 0.4194 -0.1364 -0.0938 -0.0575 254 THR B N   
5645 C CA  . THR B 254 ? 0.6487 0.4292 0.4321 -0.1173 -0.0878 -0.0619 254 THR B CA  
5646 C C   . THR B 254 ? 0.6925 0.4892 0.4842 -0.0915 -0.0841 -0.0687 254 THR B C   
5647 O O   . THR B 254 ? 0.6311 0.4436 0.4244 -0.0903 -0.0835 -0.0769 254 THR B O   
5648 C CB  . THR B 254 ? 0.7042 0.4307 0.4521 -0.1245 -0.0860 -0.0729 254 THR B CB  
5649 O OG1 . THR B 254 ? 0.7334 0.4262 0.4663 -0.1001 -0.0783 -0.0747 254 THR B OG1 
5650 C CG2 . THR B 254 ? 0.7310 0.4539 0.4614 -0.1265 -0.0871 -0.0885 254 THR B CG2 
5651 N N   . GLY B 255 ? 0.7162 0.5042 0.5093 -0.0703 -0.0812 -0.0660 255 GLY B N   
5652 C CA  . GLY B 255 ? 0.7017 0.5100 0.5084 -0.0458 -0.0797 -0.0706 255 GLY B CA  
5653 C C   . GLY B 255 ? 0.6943 0.5272 0.5211 -0.0349 -0.0829 -0.0621 255 GLY B C   
5654 O O   . GLY B 255 ? 0.6486 0.5158 0.4976 -0.0414 -0.0853 -0.0576 255 GLY B O   
5655 N N   . SER B 256 ? 0.7375 0.5499 0.5529 -0.0154 -0.0825 -0.0607 256 SER B N   
5656 C CA  . SER B 256 ? 0.7300 0.5582 0.5555 -0.0018 -0.0868 -0.0540 256 SER B CA  
5657 C C   . SER B 256 ? 0.7488 0.5834 0.5764 0.0252  -0.0892 -0.0609 256 SER B C   
5658 O O   . SER B 256 ? 0.7589 0.5749 0.5742 0.0361  -0.0847 -0.0670 256 SER B O   
5659 C CB  . SER B 256 ? 0.7469 0.5450 0.5537 -0.0035 -0.0845 -0.0413 256 SER B CB  
5660 O OG  . SER B 256 ? 0.7687 0.5719 0.5815 -0.0284 -0.0829 -0.0328 256 SER B OG  
5661 N N   . GLY B 257 ? 0.7191 0.5814 0.5622 0.0367  -0.0966 -0.0603 257 GLY B N   
5662 C CA  . GLY B 257 ? 0.7426 0.6174 0.5911 0.0618  -0.1011 -0.0664 257 GLY B CA  
5663 C C   . GLY B 257 ? 0.6894 0.5942 0.5524 0.0719  -0.1126 -0.0669 257 GLY B C   
5664 O O   . GLY B 257 ? 0.7133 0.6282 0.5821 0.0596  -0.1156 -0.0637 257 GLY B O   
5665 N N   . ILE B 258 ? 0.6453 0.5637 0.5125 0.0957  -0.1190 -0.0711 258 ILE B N   
5666 C CA  . ILE B 258 ? 0.6508 0.6032 0.5336 0.1066  -0.1334 -0.0752 258 ILE B CA  
5667 C C   . ILE B 258 ? 0.6154 0.6099 0.5327 0.1126  -0.1371 -0.0852 258 ILE B C   
5668 O O   . ILE B 258 ? 0.6510 0.6434 0.5663 0.1314  -0.1332 -0.0852 258 ILE B O   
5669 C CB  . ILE B 258 ? 0.6954 0.6294 0.5504 0.1326  -0.1399 -0.0687 258 ILE B CB  
5670 C CG1 . ILE B 258 ? 0.6956 0.5846 0.5168 0.1269  -0.1319 -0.0563 258 ILE B CG1 
5671 C CG2 . ILE B 258 ? 0.6452 0.6164 0.5138 0.1431  -0.1582 -0.0751 258 ILE B CG2 
5672 C CD1 . ILE B 258 ? 0.7429 0.6011 0.5294 0.1550  -0.1320 -0.0468 258 ILE B CD1 
5673 N N   . TYR B 259 ? 0.6699 0.7010 0.6186 0.0974  -0.1429 -0.0926 259 TYR B N   
5674 C CA  . TYR B 259 ? 0.6708 0.7447 0.6589 0.0968  -0.1434 -0.1010 259 TYR B CA  
5675 C C   . TYR B 259 ? 0.6753 0.7910 0.6899 0.0981  -0.1609 -0.1090 259 TYR B C   
5676 O O   . TYR B 259 ? 0.6593 0.7692 0.6632 0.0902  -0.1701 -0.1104 259 TYR B O   
5677 C CB  . TYR B 259 ? 0.6560 0.7337 0.6602 0.0728  -0.1305 -0.1027 259 TYR B CB  
5678 C CG  . TYR B 259 ? 0.6557 0.6912 0.6297 0.0636  -0.1178 -0.0959 259 TYR B CG  
5679 C CD1 . TYR B 259 ? 0.6720 0.6799 0.6243 0.0761  -0.1096 -0.0935 259 TYR B CD1 
5680 C CD2 . TYR B 259 ? 0.6187 0.6422 0.5855 0.0425  -0.1143 -0.0918 259 TYR B CD2 
5681 C CE1 . TYR B 259 ? 0.7148 0.6839 0.6395 0.0641  -0.1001 -0.0892 259 TYR B CE1 
5682 C CE2 . TYR B 259 ? 0.6535 0.6453 0.5967 0.0322  -0.1052 -0.0856 259 TYR B CE2 
5683 C CZ  . TYR B 259 ? 0.7055 0.6701 0.6280 0.0411  -0.0992 -0.0854 259 TYR B CZ  
5684 O OH  . TYR B 259 ? 0.7128 0.6460 0.6122 0.0271  -0.0923 -0.0812 259 TYR B OH  
5685 N N   . ALA B 260 ? 0.7134 0.8710 0.7619 0.1082  -0.1653 -0.1143 260 ALA B N   
5686 C CA  . ALA B 260 ? 0.7040 0.9080 0.7835 0.1074  -0.1841 -0.1234 260 ALA B CA  
5687 C C   . ALA B 260 ? 0.6663 0.9112 0.7954 0.0895  -0.1779 -0.1300 260 ALA B C   
5688 O O   . ALA B 260 ? 0.6761 0.9139 0.8119 0.0847  -0.1590 -0.1263 260 ALA B O   
5689 C CB  . ALA B 260 ? 0.6804 0.9073 0.7603 0.1379  -0.1984 -0.1223 260 ALA B CB  
5690 N N   . PRO B 261 ? 0.6949 0.9800 0.8573 0.0780  -0.1927 -0.1400 261 PRO B N   
5691 C CA  . PRO B 261 ? 0.6214 0.9442 0.8338 0.0582  -0.1847 -0.1455 261 PRO B CA  
5692 C C   . PRO B 261 ? 0.6389 0.9938 0.8828 0.0732  -0.1733 -0.1407 261 PRO B C   
5693 O O   . PRO B 261 ? 0.5969 0.9611 0.8656 0.0604  -0.1551 -0.1394 261 PRO B O   
5694 C CB  . PRO B 261 ? 0.5922 0.9523 0.8317 0.0464  -0.2076 -0.1581 261 PRO B CB  
5695 C CG  . PRO B 261 ? 0.6230 0.9476 0.8134 0.0536  -0.2233 -0.1595 261 PRO B CG  
5696 C CD  . PRO B 261 ? 0.6003 0.8952 0.7534 0.0815  -0.2173 -0.1473 261 PRO B CD  
5697 N N   . ASN B 262 ? 0.6280 0.9990 0.8695 0.1024  -0.1817 -0.1369 262 ASN B N   
5698 C CA  . ASN B 262 ? 0.6190 1.0235 0.8908 0.1211  -0.1703 -0.1312 262 ASN B CA  
5699 C C   . ASN B 262 ? 0.6978 1.0545 0.9297 0.1396  -0.1495 -0.1214 262 ASN B C   
5700 O O   . ASN B 262 ? 0.7196 1.0926 0.9691 0.1543  -0.1340 -0.1163 262 ASN B O   
5701 C CB  . ASN B 262 ? 0.6385 1.0957 0.9360 0.1451  -0.1906 -0.1315 262 ASN B CB  
5702 C CG  . ASN B 262 ? 0.6930 1.1179 0.9408 0.1749  -0.2007 -0.1256 262 ASN B CG  
5703 O OD1 . ASN B 262 ? 0.7277 1.0900 0.9239 0.1775  -0.1906 -0.1207 262 ASN B OD1 
5704 N ND2 . ASN B 262 ? 0.7461 1.2160 1.0107 0.1974  -0.2208 -0.1252 262 ASN B ND2 
5705 N N   . SER B 263 ? 0.6343 0.9318 0.8129 0.1389  -0.1480 -0.1187 263 SER B N   
5706 C CA  . SER B 263 ? 0.6578 0.9069 0.7967 0.1542  -0.1303 -0.1112 263 SER B CA  
5707 C C   . SER B 263 ? 0.6601 0.8499 0.7474 0.1463  -0.1316 -0.1088 263 SER B C   
5708 O O   . SER B 263 ? 0.6583 0.8457 0.7373 0.1383  -0.1466 -0.1109 263 SER B O   
5709 C CB  . SER B 263 ? 0.6905 0.9496 0.8259 0.1911  -0.1301 -0.1049 263 SER B CB  
5710 O OG  . SER B 263 ? 0.7687 0.9648 0.8494 0.2056  -0.1199 -0.0987 263 SER B OG  
5711 N N   . SER B 264 ? 0.6892 0.8313 0.7423 0.1471  -0.1150 -0.1046 264 SER B N   
5712 C CA  . SER B 264 ? 0.7255 0.8108 0.7302 0.1439  -0.1141 -0.1001 264 SER B CA  
5713 C C   . SER B 264 ? 0.7242 0.7924 0.7036 0.1735  -0.1203 -0.0943 264 SER B C   
5714 O O   . SER B 264 ? 0.7232 0.8038 0.7080 0.1999  -0.1165 -0.0919 264 SER B O   
5715 C CB  . SER B 264 ? 0.7606 0.8028 0.7383 0.1345  -0.0960 -0.0989 264 SER B CB  
5716 O OG  . SER B 264 ? 0.8168 0.8031 0.7485 0.1379  -0.0931 -0.0938 264 SER B OG  
5717 N N   . ARG B 265 ? 0.8117 0.8531 0.7634 0.1714  -0.1288 -0.0905 265 ARG B N   
5718 C CA  . ARG B 265 ? 0.8622 0.8845 0.7859 0.2003  -0.1339 -0.0834 265 ARG B CA  
5719 C C   . ARG B 265 ? 0.9357 0.8897 0.8108 0.2040  -0.1195 -0.0755 265 ARG B C   
5720 O O   . ARG B 265 ? 0.9460 0.8758 0.7969 0.2321  -0.1139 -0.0691 265 ARG B O   
5721 C CB  . ARG B 265 ? 0.8198 0.8587 0.7431 0.2000  -0.1531 -0.0838 265 ARG B CB  
5722 C CG  . ARG B 265 ? 0.7724 0.8772 0.7404 0.2006  -0.1703 -0.0926 265 ARG B CG  
5723 C CD  . ARG B 265 ? 0.8180 0.9544 0.8013 0.2329  -0.1731 -0.0901 265 ARG B CD  
5724 N NE  . ARG B 265 ? 0.8447 1.0517 0.8809 0.2294  -0.1880 -0.0986 265 ARG B NE  
5725 C CZ  . ARG B 265 ? 0.8911 1.1314 0.9410 0.2236  -0.2108 -0.1057 265 ARG B CZ  
5726 N NH1 . ARG B 265 ? 0.8636 1.0727 0.8761 0.2227  -0.2204 -0.1048 265 ARG B NH1 
5727 N NH2 . ARG B 265 ? 0.8804 1.1862 0.9823 0.2179  -0.2239 -0.1141 265 ARG B NH2 
5728 N N   . ALA B 266 ? 0.8858 0.8091 0.7473 0.1759  -0.1128 -0.0753 266 ALA B N   
5729 C CA  . ALA B 266 ? 0.8854 0.7459 0.7060 0.1720  -0.0990 -0.0694 266 ALA B CA  
5730 C C   . ALA B 266 ? 0.8872 0.7382 0.7112 0.1373  -0.0932 -0.0730 266 ALA B C   
5731 O O   . ALA B 266 ? 0.8248 0.7076 0.6732 0.1183  -0.1004 -0.0755 266 ALA B O   
5732 C CB  . ALA B 266 ? 0.8722 0.6992 0.6615 0.1805  -0.1015 -0.0590 266 ALA B CB  
5733 N N   . PHE B 267 ? 0.8182 0.6238 0.6155 0.1296  -0.0805 -0.0733 267 PHE B N   
5734 C CA  . PHE B 267 ? 0.7802 0.5779 0.5778 0.0972  -0.0773 -0.0761 267 PHE B CA  
5735 C C   . PHE B 267 ? 0.8072 0.5435 0.5656 0.0876  -0.0673 -0.0740 267 PHE B C   
5736 O O   . PHE B 267 ? 0.8445 0.5409 0.5746 0.1069  -0.0591 -0.0728 267 PHE B O   
5737 C CB  . PHE B 267 ? 0.7637 0.5936 0.5855 0.0902  -0.0744 -0.0851 267 PHE B CB  
5738 C CG  . PHE B 267 ? 0.7989 0.6020 0.6010 0.1029  -0.0621 -0.0906 267 PHE B CG  
5739 C CD1 . PHE B 267 ? 0.7931 0.6077 0.6008 0.1342  -0.0584 -0.0909 267 PHE B CD1 
5740 C CD2 . PHE B 267 ? 0.7964 0.5632 0.5728 0.0846  -0.0543 -0.0953 267 PHE B CD2 
5741 C CE1 . PHE B 267 ? 0.8119 0.5991 0.5985 0.1492  -0.0445 -0.0947 267 PHE B CE1 
5742 C CE2 . PHE B 267 ? 0.7978 0.5334 0.5493 0.0975  -0.0421 -0.1013 267 PHE B CE2 
5743 C CZ  . PHE B 267 ? 0.8365 0.5802 0.5920 0.1309  -0.0356 -0.1006 267 PHE B CZ  
5744 N N   . HIS B 268 ? 0.8426 0.5721 0.5999 0.0571  -0.0681 -0.0731 268 HIS B N   
5745 C CA  . HIS B 268 ? 0.8875 0.5649 0.6135 0.0390  -0.0614 -0.0723 268 HIS B CA  
5746 C C   . HIS B 268 ? 0.8530 0.5410 0.5847 0.0110  -0.0628 -0.0795 268 HIS B C   
5747 O O   . HIS B 268 ? 0.8159 0.5484 0.5762 -0.0017 -0.0693 -0.0779 268 HIS B O   
5748 C CB  . HIS B 268 ? 0.8333 0.4931 0.5523 0.0287  -0.0624 -0.0596 268 HIS B CB  
5749 C CG  . HIS B 268 ? 0.8742 0.4781 0.5630 0.0100  -0.0548 -0.0582 268 HIS B CG  
5750 N ND1 . HIS B 268 ? 0.9198 0.4666 0.5729 0.0247  -0.0442 -0.0594 268 HIS B ND1 
5751 C CD2 . HIS B 268 ? 0.8560 0.4524 0.5455 -0.0233 -0.0563 -0.0558 268 HIS B CD2 
5752 C CE1 . HIS B 268 ? 0.9465 0.4491 0.5787 -0.0011 -0.0393 -0.0590 268 HIS B CE1 
5753 N NE2 . HIS B 268 ? 0.9279 0.4629 0.5838 -0.0312 -0.0476 -0.0569 268 HIS B NE2 
5754 N N   . TYR B 269 ? 0.8398 0.4844 0.5409 0.0032  -0.0563 -0.0875 269 TYR B N   
5755 C CA  . TYR B 269 ? 0.8045 0.4505 0.5009 -0.0232 -0.0587 -0.0954 269 TYR B CA  
5756 C C   . TYR B 269 ? 0.8743 0.4561 0.5290 -0.0382 -0.0541 -0.1011 269 TYR B C   
5757 O O   . TYR B 269 ? 0.9094 0.4465 0.5326 -0.0207 -0.0443 -0.1080 269 TYR B O   
5758 C CB  . TYR B 269 ? 0.7980 0.4676 0.5011 -0.0110 -0.0553 -0.1051 269 TYR B CB  
5759 C CG  . TYR B 269 ? 0.8008 0.4702 0.4930 -0.0347 -0.0576 -0.1131 269 TYR B CG  
5760 C CD1 . TYR B 269 ? 0.8408 0.4572 0.4902 -0.0429 -0.0536 -0.1238 269 TYR B CD1 
5761 C CD2 . TYR B 269 ? 0.8016 0.5212 0.5228 -0.0484 -0.0641 -0.1098 269 TYR B CD2 
5762 C CE1 . TYR B 269 ? 0.8953 0.5124 0.5309 -0.0643 -0.0582 -0.1321 269 TYR B CE1 
5763 C CE2 . TYR B 269 ? 0.7872 0.5091 0.4962 -0.0676 -0.0671 -0.1160 269 TYR B CE2 
5764 C CZ  . TYR B 269 ? 0.8235 0.4958 0.4897 -0.0755 -0.0653 -0.1275 269 TYR B CZ  
5765 O OH  . TYR B 269 ? 0.8842 0.5591 0.5346 -0.0942 -0.0706 -0.1344 269 TYR B OH  
5766 N N   . ASP B 270 ? 0.9318 0.5084 0.5859 -0.0709 -0.0606 -0.0984 270 ASP B N   
5767 C CA  . ASP B 270 ? 0.9876 0.5023 0.6050 -0.0905 -0.0576 -0.1037 270 ASP B CA  
5768 C C   . ASP B 270 ? 1.0198 0.5495 0.6423 -0.1289 -0.0690 -0.1069 270 ASP B C   
5769 O O   . ASP B 270 ? 1.0010 0.5638 0.6519 -0.1471 -0.0758 -0.0945 270 ASP B O   
5770 C CB  . ASP B 270 ? 1.0215 0.5041 0.6334 -0.0874 -0.0514 -0.0911 270 ASP B CB  
5771 C CG  . ASP B 270 ? 1.1028 0.5316 0.6888 -0.1188 -0.0498 -0.0932 270 ASP B CG  
5772 O OD1 . ASP B 270 ? 1.1324 0.5194 0.6849 -0.1308 -0.0490 -0.1087 270 ASP B OD1 
5773 O OD2 . ASP B 270 ? 1.1183 0.5443 0.7164 -0.1313 -0.0486 -0.0792 270 ASP B OD2 
5774 N N   . MET B 271 ? 0.9942 0.5016 0.5882 -0.1398 -0.0712 -0.1227 271 MET B N   
5775 C CA  . MET B 271 ? 0.9772 0.4968 0.5717 -0.1767 -0.0844 -0.1267 271 MET B CA  
5776 C C   . MET B 271 ? 1.0354 0.4943 0.5981 -0.2050 -0.0856 -0.1334 271 MET B C   
5777 O O   . MET B 271 ? 1.0801 0.5527 0.6487 -0.2399 -0.0987 -0.1349 271 MET B O   
5778 C CB  . MET B 271 ? 1.0422 0.5789 0.6240 -0.1755 -0.0890 -0.1399 271 MET B CB  
5779 C CG  . MET B 271 ? 0.9312 0.5369 0.5525 -0.1587 -0.0899 -0.1310 271 MET B CG  
5780 S SD  . MET B 271 ? 0.8916 0.5642 0.5553 -0.1853 -0.1043 -0.1163 271 MET B SD  
5781 C CE  . MET B 271 ? 0.8803 0.5422 0.5139 -0.2176 -0.1185 -0.1301 271 MET B CE  
5782 N N   . LYS B 272 ? 1.1592 0.5531 0.6904 -0.1917 -0.0722 -0.1363 272 LYS B N   
5783 C CA  . LYS B 272 ? 1.2153 0.5401 0.7086 -0.2194 -0.0712 -0.1461 272 LYS B CA  
5784 C C   . LYS B 272 ? 1.2477 0.5707 0.7637 -0.2446 -0.0719 -0.1307 272 LYS B C   
5785 O O   . LYS B 272 ? 1.2770 0.5884 0.7900 -0.2847 -0.0816 -0.1354 272 LYS B O   
5786 C CB  . LYS B 272 ? 1.2809 0.5276 0.7239 -0.1928 -0.0533 -0.1558 272 LYS B CB  
5787 C CG  . LYS B 272 ? 1.3435 0.5959 0.7693 -0.1589 -0.0474 -0.1662 272 LYS B CG  
5788 C CD  . LYS B 272 ? 1.4619 0.6388 0.8244 -0.1630 -0.0416 -0.1880 272 LYS B CD  
5789 C CE  . LYS B 272 ? 1.4903 0.6723 0.8357 -0.1264 -0.0322 -0.1960 272 LYS B CE  
5790 N NZ  . LYS B 272 ? 1.5378 0.7054 0.8826 -0.0814 -0.0133 -0.1863 272 LYS B NZ  
5791 N N   . THR B 273 ? 1.2018 0.5390 0.7417 -0.2226 -0.0622 -0.1120 273 THR B N   
5792 C CA  . THR B 273 ? 1.1737 0.5026 0.7310 -0.2409 -0.0580 -0.0952 273 THR B CA  
5793 C C   . THR B 273 ? 1.1598 0.5697 0.7715 -0.2469 -0.0668 -0.0769 273 THR B C   
5794 O O   . THR B 273 ? 1.0411 0.5095 0.6753 -0.2376 -0.0761 -0.0778 273 THR B O   
5795 C CB  . THR B 273 ? 1.2201 0.4990 0.7576 -0.2100 -0.0385 -0.0854 273 THR B CB  
5796 O OG1 . THR B 273 ? 1.1923 0.5229 0.7586 -0.1758 -0.0371 -0.0716 273 THR B OG1 
5797 C CG2 . THR B 273 ? 1.2568 0.4648 0.7414 -0.1889 -0.0271 -0.1014 273 THR B CG2 
5798 N N   . GLU B 274 ? 1.2037 0.6133 0.8350 -0.2628 -0.0619 -0.0593 274 GLU B N   
5799 C CA  . GLU B 274 ? 1.1886 0.6655 0.8672 -0.2637 -0.0651 -0.0385 274 GLU B CA  
5800 C C   . GLU B 274 ? 1.1483 0.6197 0.8309 -0.2310 -0.0507 -0.0210 274 GLU B C   
5801 O O   . GLU B 274 ? 1.1317 0.6478 0.8471 -0.2299 -0.0500 -0.0024 274 GLU B O   
5802 C CB  . GLU B 274 ? 1.1467 0.6392 0.8505 -0.3070 -0.0704 -0.0285 274 GLU B CB  
5803 C CG  . GLU B 274 ? 1.1369 0.6437 0.8404 -0.3427 -0.0882 -0.0439 274 GLU B CG  
5804 C CD  . GLU B 274 ? 1.2484 0.7789 0.9840 -0.3853 -0.0941 -0.0316 274 GLU B CD  
5805 O OE1 . GLU B 274 ? 1.2881 0.8109 1.0409 -0.3867 -0.0804 -0.0116 274 GLU B OE1 
5806 O OE2 . GLU B 274 ? 1.2062 0.7660 0.9510 -0.4152 -0.1117 -0.0409 274 GLU B OE2 
5807 N N   . GLU B 275 ? 1.2319 0.6488 0.8797 -0.2031 -0.0388 -0.0257 275 GLU B N   
5808 C CA  . GLU B 275 ? 1.1957 0.6066 0.8422 -0.1695 -0.0267 -0.0097 275 GLU B CA  
5809 C C   . GLU B 275 ? 1.1474 0.6226 0.8198 -0.1437 -0.0347 -0.0062 275 GLU B C   
5810 O O   . GLU B 275 ? 1.0972 0.6048 0.7772 -0.1403 -0.0452 -0.0193 275 GLU B O   
5811 C CB  . GLU B 275 ? 1.2197 0.5635 0.8221 -0.1411 -0.0139 -0.0163 275 GLU B CB  
5812 C CG  . GLU B 275 ? 1.3413 0.6066 0.9112 -0.1604 -0.0003 -0.0165 275 GLU B CG  
5813 C CD  . GLU B 275 ? 1.4150 0.6857 1.0089 -0.1994 0.0016  -0.0022 275 GLU B CD  
5814 O OE1 . GLU B 275 ? 1.4811 0.7550 1.0833 -0.2400 -0.0081 -0.0119 275 GLU B OE1 
5815 O OE2 . GLU B 275 ? 1.4095 0.6828 1.0142 -0.1889 0.0128  0.0193  275 GLU B OE2 
5816 N N   . GLY B 276 ? 1.0932 0.5841 0.7772 -0.1259 -0.0286 0.0120  276 GLY B N   
5817 C CA  . GLY B 276 ? 0.9927 0.5280 0.6905 -0.0961 -0.0340 0.0140  276 GLY B CA  
5818 C C   . GLY B 276 ? 1.0480 0.5559 0.7188 -0.0590 -0.0305 0.0067  276 GLY B C   
5819 O O   . GLY B 276 ? 1.1001 0.5523 0.7397 -0.0532 -0.0215 0.0023  276 GLY B O   
5820 N N   . LYS B 277 ? 0.9163 0.4643 0.5996 -0.0331 -0.0375 0.0059  277 LYS B N   
5821 C CA  . LYS B 277 ? 0.9036 0.4389 0.5682 0.0032  -0.0370 -0.0005 277 LYS B CA  
5822 C C   . LYS B 277 ? 0.8776 0.4547 0.5563 0.0276  -0.0443 0.0049  277 LYS B C   
5823 O O   . LYS B 277 ? 0.8185 0.4448 0.5249 0.0197  -0.0541 0.0011  277 LYS B O   
5824 C CB  . LYS B 277 ? 0.9122 0.4534 0.5763 0.0048  -0.0420 -0.0194 277 LYS B CB  
5825 C CG  . LYS B 277 ? 0.9069 0.4393 0.5555 0.0430  -0.0403 -0.0245 277 LYS B CG  
5826 C CD  . LYS B 277 ? 0.9708 0.4347 0.5792 0.0571  -0.0257 -0.0190 277 LYS B CD  
5827 C CE  . LYS B 277 ? 0.9819 0.4361 0.5738 0.0950  -0.0226 -0.0247 277 LYS B CE  
5828 N NZ  . LYS B 277 ? 1.1146 0.5034 0.6656 0.1159  -0.0070 -0.0151 277 LYS B NZ  
5829 N N   . LEU B 278 ? 0.8513 0.4058 0.5077 0.0578  -0.0395 0.0133  278 LEU B N   
5830 C CA  . LEU B 278 ? 0.8293 0.4162 0.4903 0.0843  -0.0480 0.0168  278 LEU B CA  
5831 C C   . LEU B 278 ? 0.8284 0.4310 0.4888 0.1119  -0.0564 0.0043  278 LEU B C   
5832 O O   . LEU B 278 ? 0.8703 0.4373 0.5080 0.1280  -0.0489 0.0028  278 LEU B O   
5833 C CB  . LEU B 278 ? 0.8680 0.4220 0.5020 0.1028  -0.0382 0.0349  278 LEU B CB  
5834 C CG  . LEU B 278 ? 0.8609 0.4387 0.4881 0.1345  -0.0474 0.0384  278 LEU B CG  
5835 C CD1 . LEU B 278 ? 0.8130 0.4346 0.4645 0.1206  -0.0560 0.0384  278 LEU B CD1 
5836 C CD2 . LEU B 278 ? 0.9149 0.4480 0.5049 0.1579  -0.0346 0.0568  278 LEU B CD2 
5837 N N   . LEU B 279 ? 0.8331 0.4885 0.5192 0.1167  -0.0706 -0.0042 279 LEU B N   
5838 C CA  . LEU B 279 ? 0.8350 0.5163 0.5285 0.1418  -0.0798 -0.0147 279 LEU B CA  
5839 C C   . LEU B 279 ? 0.8799 0.5895 0.5738 0.1652  -0.0924 -0.0121 279 LEU B C   
5840 O O   . LEU B 279 ? 0.8386 0.5660 0.5401 0.1548  -0.0976 -0.0091 279 LEU B O   
5841 C CB  . LEU B 279 ? 0.8284 0.5499 0.5550 0.1257  -0.0861 -0.0293 279 LEU B CB  
5842 C CG  . LEU B 279 ? 0.8483 0.5474 0.5734 0.1020  -0.0766 -0.0347 279 LEU B CG  
5843 C CD1 . LEU B 279 ? 0.8174 0.5607 0.5746 0.0883  -0.0826 -0.0471 279 LEU B CD1 
5844 C CD2 . LEU B 279 ? 0.8484 0.4998 0.5437 0.1178  -0.0654 -0.0357 279 LEU B CD2 
5845 N N   . LEU B 280 ? 0.8731 0.5853 0.5559 0.1980  -0.0971 -0.0129 280 LEU B N   
5846 C CA  . LEU B 280 ? 0.8870 0.6303 0.5692 0.2222  -0.1129 -0.0131 280 LEU B CA  
5847 C C   . LEU B 280 ? 0.8749 0.6624 0.5818 0.2390  -0.1252 -0.0249 280 LEU B C   
5848 O O   . LEU B 280 ? 0.9113 0.6876 0.6176 0.2488  -0.1168 -0.0263 280 LEU B O   
5849 C CB  . LEU B 280 ? 0.8820 0.5864 0.5216 0.2520  -0.1074 0.0021  280 LEU B CB  
5850 C CG  . LEU B 280 ? 0.8965 0.5786 0.5131 0.2485  -0.1031 0.0149  280 LEU B CG  
5851 C CD1 . LEU B 280 ? 0.9483 0.5996 0.5663 0.2161  -0.0862 0.0224  280 LEU B CD1 
5852 C CD2 . LEU B 280 ? 0.9661 0.6119 0.5398 0.2844  -0.0971 0.0296  280 LEU B CD2 
5853 N N   . SER B 281 ? 0.9242 0.7609 0.6518 0.2431  -0.1445 -0.0329 281 SER B N   
5854 C CA  . SER B 281 ? 0.9050 0.7915 0.6619 0.2582  -0.1576 -0.0430 281 SER B CA  
5855 C C   . SER B 281 ? 0.8698 0.8011 0.6382 0.2650  -0.1811 -0.0501 281 SER B C   
5856 O O   . SER B 281 ? 0.8640 0.7940 0.6281 0.2479  -0.1863 -0.0521 281 SER B O   
5857 C CB  . SER B 281 ? 0.8763 0.7881 0.6721 0.2343  -0.1528 -0.0537 281 SER B CB  
5858 O OG  . SER B 281 ? 0.8463 0.7986 0.6678 0.2534  -0.1591 -0.0592 281 SER B OG  
5859 N N   . GLN B 282 ? 0.9550 0.9242 0.7352 0.2916  -0.1952 -0.0532 282 GLN B N   
5860 C CA  . GLN B 282 ? 0.9601 0.9785 0.7552 0.2967  -0.2212 -0.0629 282 GLN B CA  
5861 C C   . GLN B 282 ? 0.9109 0.9799 0.7584 0.2676  -0.2300 -0.0788 282 GLN B C   
5862 O O   . GLN B 282 ? 0.9408 1.0285 0.8209 0.2603  -0.2210 -0.0818 282 GLN B O   
5863 C CB  . GLN B 282 ? 0.9612 1.0072 0.7522 0.3365  -0.2344 -0.0591 282 GLN B CB  
5864 C CG  . GLN B 282 ? 0.9670 0.9778 0.7045 0.3653  -0.2373 -0.0470 282 GLN B CG  
5865 C CD  . GLN B 282 ? 1.0592 1.1095 0.7946 0.3731  -0.2667 -0.0561 282 GLN B CD  
5866 O OE1 . GLN B 282 ? 1.0729 1.1034 0.7851 0.3601  -0.2713 -0.0588 282 GLN B OE1 
5867 N NE2 . GLN B 282 ? 1.0857 1.1927 0.8442 0.3951  -0.2873 -0.0608 282 GLN B NE2 
5868 N N   . LEU B 283 ? 0.8099 0.8980 0.6626 0.2522  -0.2466 -0.0889 283 LEU B N   
5869 C CA  . LEU B 283 ? 0.7452 0.8766 0.6442 0.2235  -0.2551 -0.1043 283 LEU B CA  
5870 C C   . LEU B 283 ? 0.7508 0.9220 0.6564 0.2275  -0.2840 -0.1166 283 LEU B C   
5871 O O   . LEU B 283 ? 0.7685 0.9209 0.6330 0.2451  -0.2953 -0.1139 283 LEU B O   
5872 C CB  . LEU B 283 ? 0.7201 0.8227 0.6164 0.1906  -0.2415 -0.1057 283 LEU B CB  
5873 C CG  . LEU B 283 ? 0.7288 0.8003 0.6258 0.1773  -0.2160 -0.0972 283 LEU B CG  
5874 C CD1 . LEU B 283 ? 0.6770 0.7204 0.5621 0.1515  -0.2065 -0.0955 283 LEU B CD1 
5875 C CD2 . LEU B 283 ? 0.6821 0.7895 0.6245 0.1686  -0.2107 -0.1035 283 LEU B CD2 
5876 N N   . ASP B 284 ? 0.8330 1.0583 0.7895 0.2102  -0.2958 -0.1304 284 ASP B N   
5877 C CA  . ASP B 284 ? 0.8034 1.0645 0.7695 0.2031  -0.3240 -0.1460 284 ASP B CA  
5878 C C   . ASP B 284 ? 0.8386 1.0629 0.7795 0.1780  -0.3222 -0.1529 284 ASP B C   
5879 O O   . ASP B 284 ? 0.8217 1.0219 0.7700 0.1543  -0.3018 -0.1509 284 ASP B O   
5880 C CB  . ASP B 284 ? 0.7715 1.1006 0.8039 0.1874  -0.3348 -0.1583 284 ASP B CB  
5881 C CG  . ASP B 284 ? 0.8511 1.2257 0.9099 0.2168  -0.3396 -0.1511 284 ASP B CG  
5882 O OD1 . ASP B 284 ? 0.9277 1.2787 0.9491 0.2507  -0.3363 -0.1377 284 ASP B OD1 
5883 O OD2 . ASP B 284 ? 0.8451 1.2767 0.9617 0.2060  -0.3431 -0.1568 284 ASP B OD2 
5884 N N   . SER B 285 ? 0.7402 0.9560 0.6478 0.1846  -0.3400 -0.1588 285 SER B N   
5885 C CA  . SER B 285 ? 0.7348 0.9155 0.6171 0.1628  -0.3376 -0.1659 285 SER B CA  
5886 C C   . SER B 285 ? 0.6958 0.9031 0.6249 0.1262  -0.3383 -0.1811 285 SER B C   
5887 O O   . SER B 285 ? 0.7351 0.9144 0.6590 0.1057  -0.3258 -0.1834 285 SER B O   
5888 C CB  . SER B 285 ? 0.7776 0.9438 0.6191 0.1745  -0.3504 -0.1682 285 SER B CB  
5889 O OG  . SER B 285 ? 0.8067 0.9546 0.6105 0.2104  -0.3490 -0.1533 285 SER B OG  
5890 N N   . HIS B 286 ? 0.7998 1.0610 0.7758 0.1179  -0.3507 -0.1896 286 HIS B N   
5891 C CA  . HIS B 286 ? 0.8148 1.1048 0.8405 0.0831  -0.3498 -0.2022 286 HIS B CA  
5892 C C   . HIS B 286 ? 0.7906 1.1344 0.8738 0.0867  -0.3474 -0.1991 286 HIS B C   
5893 O O   . HIS B 286 ? 0.7647 1.1567 0.8782 0.0913  -0.3614 -0.2011 286 HIS B O   
5894 C CB  . HIS B 286 ? 0.8073 1.1103 0.8338 0.0657  -0.3677 -0.2156 286 HIS B CB  
5895 C CG  . HIS B 286 ? 0.8476 1.0986 0.8118 0.0693  -0.3711 -0.2183 286 HIS B CG  
5896 N ND1 . HIS B 286 ? 0.8619 1.0666 0.8015 0.0518  -0.3580 -0.2220 286 HIS B ND1 
5897 C CD2 . HIS B 286 ? 0.8980 1.1354 0.8181 0.0909  -0.3846 -0.2168 286 HIS B CD2 
5898 C CE1 . HIS B 286 ? 0.9524 1.1173 0.8355 0.0628  -0.3630 -0.2228 286 HIS B CE1 
5899 N NE2 . HIS B 286 ? 0.9492 1.1327 0.8193 0.0860  -0.3790 -0.2199 286 HIS B NE2 
5900 N N   . PRO B 287 ? 0.8387 1.1771 0.9378 0.0858  -0.3296 -0.1936 287 PRO B N   
5901 C CA  . PRO B 287 ? 0.7951 1.1787 0.9443 0.0923  -0.3216 -0.1879 287 PRO B CA  
5902 C C   . PRO B 287 ? 0.8045 1.2417 1.0144 0.0660  -0.3280 -0.1993 287 PRO B C   
5903 O O   . PRO B 287 ? 0.8643 1.2887 1.0797 0.0349  -0.3258 -0.2088 287 PRO B O   
5904 C CB  . PRO B 287 ? 0.7954 1.1389 0.9367 0.0862  -0.2887 -0.1752 287 PRO B CB  
5905 C CG  . PRO B 287 ? 0.8084 1.0897 0.8957 0.0811  -0.2812 -0.1716 287 PRO B CG  
5906 C CD  . PRO B 287 ? 0.8176 1.0998 0.8896 0.0724  -0.3040 -0.1858 287 PRO B CD  
5907 N N   . SER B 288 ? 0.9351 1.4275 1.1896 0.0782  -0.3308 -0.1950 288 SER B N   
5908 C CA  . SER B 288 ? 0.9413 1.4842 1.2566 0.0524  -0.3320 -0.2009 288 SER B CA  
5909 C C   . SER B 288 ? 0.9865 1.5339 1.3388 0.0351  -0.3079 -0.2006 288 SER B C   
5910 O O   . SER B 288 ? 0.8951 1.4280 1.2403 0.0528  -0.2883 -0.1891 288 SER B O   
5911 C CB  . SER B 288 ? 0.9606 1.5645 1.3114 0.0728  -0.3438 -0.1942 288 SER B CB  
5912 O OG  . SER B 288 ? 0.9751 1.6315 1.3935 0.0555  -0.3352 -0.1937 288 SER B OG  
5913 N N   . HIS B 289 ? 1.4893 2.1275 1.3173 -0.2523 -0.2472 0.0368  289 HIS B N   
5914 C CA  . HIS B 289 ? 1.4525 2.0452 1.3058 -0.2322 -0.2245 0.0151  289 HIS B CA  
5915 C C   . HIS B 289 ? 1.4206 1.9911 1.3149 -0.2213 -0.2305 0.0096  289 HIS B C   
5916 O O   . HIS B 289 ? 1.3934 1.9875 1.2922 -0.2295 -0.2413 -0.0008 289 HIS B O   
5917 C CB  . HIS B 289 ? 1.4058 2.0023 1.2413 -0.2328 -0.1999 -0.0259 289 HIS B CB  
5918 C CG  . HIS B 289 ? 1.4861 2.1110 1.2852 -0.2427 -0.1900 -0.0297 289 HIS B CG  
5919 N ND1 . HIS B 289 ? 1.5442 2.1915 1.3232 -0.2482 -0.1742 -0.0671 289 HIS B ND1 
5920 C CD2 . HIS B 289 ? 1.4874 2.1238 1.2685 -0.2489 -0.1930 -0.0029 289 HIS B CD2 
5921 C CE1 . HIS B 289 ? 1.5475 2.2231 1.2988 -0.2568 -0.1669 -0.0648 289 HIS B CE1 
5922 N NE2 . HIS B 289 ? 1.5319 2.2018 1.2825 -0.2587 -0.1778 -0.0249 289 HIS B NE2 
5923 N N   . SER B 290 ? 0.9445 1.4733 0.8691 -0.2043 -0.2235 0.0157  290 SER B N   
5924 C CA  . SER B 290 ? 0.9568 1.4661 0.9181 -0.1952 -0.2208 0.0005  290 SER B CA  
5925 C C   . SER B 290 ? 0.9416 1.4436 0.8936 -0.1974 -0.1998 -0.0376 290 SER B C   
5926 O O   . SER B 290 ? 0.9027 1.4075 0.8257 -0.2007 -0.1860 -0.0530 290 SER B O   
5927 C CB  . SER B 290 ? 0.9117 1.3805 0.9045 -0.1782 -0.2148 0.0113  290 SER B CB  
5928 O OG  . SER B 290 ? 0.8842 1.3219 0.8671 -0.1709 -0.1898 -0.0046 290 SER B OG  
5929 N N   . ALA B 291 ? 0.9291 1.4230 0.9082 -0.1962 -0.1984 -0.0537 291 ALA B N   
5930 C CA  . ALA B 291 ? 0.8974 1.3736 0.8724 -0.1981 -0.1793 -0.0873 291 ALA B CA  
5931 C C   . ALA B 291 ? 0.9763 1.4116 0.9437 -0.1866 -0.1584 -0.0923 291 ALA B C   
5932 O O   . ALA B 291 ? 0.9820 1.3973 0.9593 -0.1760 -0.1569 -0.0723 291 ALA B O   
5933 C CB  . ALA B 291 ? 0.8921 1.3615 0.9010 -0.1994 -0.1801 -0.0992 291 ALA B CB  
5934 N N   . VAL B 292 ? 0.8672 1.2904 0.8177 -0.1886 -0.1438 -0.1196 292 VAL B N   
5935 C CA  . VAL B 292 ? 0.8389 1.2222 0.7846 -0.1770 -0.1264 -0.1250 292 VAL B CA  
5936 C C   . VAL B 292 ? 0.7946 1.1413 0.7672 -0.1699 -0.1206 -0.1176 292 VAL B C   
5937 O O   . VAL B 292 ? 0.8646 1.2150 0.8595 -0.1753 -0.1252 -0.1200 292 VAL B O   
5938 C CB  . VAL B 292 ? 0.8171 1.1892 0.7479 -0.1793 -0.1148 -0.1581 292 VAL B CB  
5939 C CG1 . VAL B 292 ? 0.8255 1.1482 0.7595 -0.1675 -0.0999 -0.1643 292 VAL B CG1 
5940 C CG2 . VAL B 292 ? 0.8658 1.2750 0.7692 -0.1836 -0.1162 -0.1669 292 VAL B CG2 
5941 N N   . VAL B 293 ? 0.7187 1.0341 0.6894 -0.1587 -0.1102 -0.1094 293 VAL B N   
5942 C CA  . VAL B 293 ? 0.7383 1.0226 0.7304 -0.1525 -0.1038 -0.1006 293 VAL B CA  
5943 C C   . VAL B 293 ? 0.7124 0.9560 0.6992 -0.1519 -0.0886 -0.1183 293 VAL B C   
5944 O O   . VAL B 293 ? 0.7648 0.9923 0.7329 -0.1461 -0.0821 -0.1255 293 VAL B O   
5945 C CB  . VAL B 293 ? 0.6920 0.9703 0.6855 -0.1420 -0.1050 -0.0766 293 VAL B CB  
5946 C CG1 . VAL B 293 ? 0.6867 0.9332 0.7000 -0.1360 -0.0961 -0.0716 293 VAL B CG1 
5947 C CG2 . VAL B 293 ? 0.6856 0.9982 0.6856 -0.1440 -0.1229 -0.0561 293 VAL B CG2 
5948 N N   . ASN B 294 ? 0.6842 0.9117 0.6884 -0.1583 -0.0839 -0.1245 294 ASN B N   
5949 C CA  . ASN B 294 ? 0.6959 0.8794 0.6955 -0.1598 -0.0708 -0.1335 294 ASN B CA  
5950 C C   . ASN B 294 ? 0.7042 0.8698 0.7113 -0.1521 -0.0647 -0.1163 294 ASN B C   
5951 O O   . ASN B 294 ? 0.6772 0.8530 0.7068 -0.1547 -0.0648 -0.1098 294 ASN B O   
5952 C CB  . ASN B 294 ? 0.7047 0.8825 0.7163 -0.1751 -0.0681 -0.1488 294 ASN B CB  
5953 C CG  . ASN B 294 ? 0.7227 0.8514 0.7249 -0.1804 -0.0566 -0.1562 294 ASN B CG  
5954 O OD1 . ASN B 294 ? 0.7262 0.8259 0.7160 -0.1712 -0.0511 -0.1477 294 ASN B OD1 
5955 N ND2 . ASN B 294 ? 0.7362 0.8552 0.7435 -0.1968 -0.0544 -0.1711 294 ASN B ND2 
5956 N N   . TRP B 295 ? 0.8188 0.9621 0.8091 -0.1418 -0.0601 -0.1103 295 TRP B N   
5957 C CA  . TRP B 295 ? 0.8265 0.9558 0.8207 -0.1341 -0.0554 -0.0942 295 TRP B CA  
5958 C C   . TRP B 295 ? 0.7866 0.8865 0.7859 -0.1413 -0.0447 -0.0961 295 TRP B C   
5959 O O   . TRP B 295 ? 0.7874 0.8824 0.7943 -0.1377 -0.0404 -0.0855 295 TRP B O   
5960 C CB  . TRP B 295 ? 0.7797 0.8968 0.7545 -0.1224 -0.0542 -0.0887 295 TRP B CB  
5961 C CG  . TRP B 295 ? 0.7792 0.9311 0.7505 -0.1177 -0.0633 -0.0811 295 TRP B CG  
5962 C CD1 . TRP B 295 ? 0.7954 0.9655 0.7518 -0.1172 -0.0666 -0.0910 295 TRP B CD1 
5963 C CD2 . TRP B 295 ? 0.7599 0.9339 0.7428 -0.1150 -0.0709 -0.0622 295 TRP B CD2 
5964 N NE1 . TRP B 295 ? 0.7537 0.9579 0.7078 -0.1167 -0.0749 -0.0775 295 TRP B NE1 
5965 C CE2 . TRP B 295 ? 0.7799 0.9841 0.7502 -0.1152 -0.0790 -0.0582 295 TRP B CE2 
5966 C CE3 . TRP B 295 ? 0.7449 0.9161 0.7485 -0.1130 -0.0722 -0.0493 295 TRP B CE3 
5967 C CZ2 . TRP B 295 ? 0.7468 0.9745 0.7223 -0.1149 -0.0900 -0.0376 295 TRP B CZ2 
5968 C CZ3 . TRP B 295 ? 0.7530 0.9455 0.7661 -0.1098 -0.0836 -0.0315 295 TRP B CZ3 
5969 C CH2 . TRP B 295 ? 0.7438 0.9623 0.7417 -0.1115 -0.0932 -0.0238 295 TRP B CH2 
5970 N N   . THR B 296 ? 0.7944 0.8756 0.7889 -0.1531 -0.0403 -0.1094 296 THR B N   
5971 C CA  . THR B 296 ? 0.8130 0.8668 0.8075 -0.1644 -0.0299 -0.1097 296 THR B CA  
5972 C C   . THR B 296 ? 0.8000 0.8729 0.8159 -0.1805 -0.0269 -0.1184 296 THR B C   
5973 O O   . THR B 296 ? 0.7873 0.8428 0.8027 -0.1942 -0.0169 -0.1200 296 THR B O   
5974 C CB  . THR B 296 ? 0.8189 0.8285 0.7901 -0.1682 -0.0276 -0.1152 296 THR B CB  
5975 O OG1 . THR B 296 ? 0.8375 0.8194 0.8033 -0.1818 -0.0184 -0.1110 296 THR B OG1 
5976 C CG2 . THR B 296 ? 0.8200 0.8302 0.7904 -0.1759 -0.0327 -0.1325 296 THR B CG2 
5977 N N   . SER B 297 ? 0.8653 0.9757 0.8993 -0.1809 -0.0356 -0.1241 297 SER B N   
5978 C CA  . SER B 297 ? 0.8385 0.9720 0.8961 -0.1960 -0.0344 -0.1348 297 SER B CA  
5979 C C   . SER B 297 ? 0.8728 1.0180 0.9538 -0.1992 -0.0256 -0.1315 297 SER B C   
5980 O O   . SER B 297 ? 0.8828 1.0146 0.9635 -0.2154 -0.0133 -0.1374 297 SER B O   
5981 C CB  . SER B 297 ? 0.8408 1.0160 0.9139 -0.1926 -0.0489 -0.1383 297 SER B CB  
5982 O OG  . SER B 297 ? 0.8312 1.0237 0.9189 -0.2090 -0.0499 -0.1534 297 SER B OG  
5983 N N   . TYR B 298 ? 0.8808 1.0501 0.9816 -0.1847 -0.0318 -0.1224 298 TYR B N   
5984 C CA  . TYR B 298 ? 0.8772 1.0618 1.0062 -0.1853 -0.0243 -0.1236 298 TYR B CA  
5985 C C   . TYR B 298 ? 0.8840 1.0361 0.9934 -0.1911 -0.0083 -0.1212 298 TYR B C   
5986 O O   . TYR B 298 ? 0.8865 1.0437 1.0064 -0.2059 0.0046  -0.1302 298 TYR B O   
5987 C CB  . TYR B 298 ? 0.8499 1.0579 1.0029 -0.1666 -0.0365 -0.1133 298 TYR B CB  
5988 C CG  . TYR B 298 ? 0.8339 1.0600 1.0230 -0.1645 -0.0302 -0.1189 298 TYR B CG  
5989 C CD1 . TYR B 298 ? 0.8432 1.0503 1.0259 -0.1601 -0.0195 -0.1152 298 TYR B CD1 
5990 C CD2 . TYR B 298 ? 0.7896 1.0544 1.0211 -0.1672 -0.0348 -0.1307 298 TYR B CD2 
5991 C CE1 . TYR B 298 ? 0.8375 1.0636 1.0544 -0.1584 -0.0126 -0.1248 298 TYR B CE1 
5992 C CE2 . TYR B 298 ? 0.7762 1.0609 1.0455 -0.1639 -0.0286 -0.1402 298 TYR B CE2 
5993 C CZ  . TYR B 298 ? 0.8118 1.0770 1.0734 -0.1596 -0.0168 -0.1383 298 TYR B CZ  
5994 O OH  . TYR B 298 ? 0.8431 1.1304 1.1436 -0.1564 -0.0093 -0.1519 298 TYR B OH  
5995 N N   . ALA B 299 ? 0.8042 0.9261 0.8847 -0.1811 -0.0091 -0.1093 299 ALA B N   
5996 C CA  . ALA B 299 ? 0.8060 0.8985 0.8667 -0.1857 0.0033  -0.1047 299 ALA B CA  
5997 C C   . ALA B 299 ? 0.8185 0.8883 0.8615 -0.2083 0.0139  -0.1111 299 ALA B C   
5998 O O   . ALA B 299 ? 0.8608 0.9247 0.8999 -0.2213 0.0268  -0.1121 299 ALA B O   
5999 C CB  . ALA B 299 ? 0.8169 0.8819 0.8501 -0.1714 -0.0018 -0.0916 299 ALA B CB  
6000 N N   . SER B 300 ? 0.8678 0.9249 0.8994 -0.2151 0.0084  -0.1158 300 SER B N   
6001 C CA  . SER B 300 ? 0.8757 0.9076 0.8915 -0.2387 0.0159  -0.1207 300 SER B CA  
6002 C C   . SER B 300 ? 0.8732 0.9372 0.9150 -0.2587 0.0239  -0.1339 300 SER B C   
6003 O O   . SER B 300 ? 0.8729 0.9194 0.9024 -0.2829 0.0329  -0.1367 300 SER B O   
6004 C CB  . SER B 300 ? 0.8863 0.8907 0.8839 -0.2383 0.0061  -0.1238 300 SER B CB  
6005 O OG  . SER B 300 ? 0.9333 0.9044 0.9063 -0.2231 0.0008  -0.1136 300 SER B OG  
6006 N N   . SER B 301 ? 0.9078 1.0184 0.9860 -0.2504 0.0199  -0.1416 301 SER B N   
6007 C CA  . SER B 301 ? 0.8575 1.0037 0.9654 -0.2685 0.0269  -0.1565 301 SER B CA  
6008 C C   . SER B 301 ? 0.8651 1.0345 0.9927 -0.2752 0.0419  -0.1618 301 SER B C   
6009 O O   . SER B 301 ? 0.8746 1.0749 1.0262 -0.2935 0.0511  -0.1762 301 SER B O   
6010 C CB  . SER B 301 ? 0.8673 1.0560 1.0094 -0.2575 0.0129  -0.1641 301 SER B CB  
6011 O OG  . SER B 301 ? 0.8386 1.0648 1.0177 -0.2437 0.0115  -0.1660 301 SER B OG  
6012 N N   . ILE B 302 ? 0.8189 0.9782 0.9390 -0.2617 0.0452  -0.1530 302 ILE B N   
6013 C CA  . ILE B 302 ? 0.8318 1.0153 0.9712 -0.2669 0.0599  -0.1615 302 ILE B CA  
6014 C C   . ILE B 302 ? 0.8329 0.9821 0.9319 -0.2846 0.0742  -0.1539 302 ILE B C   
6015 O O   . ILE B 302 ? 0.8618 0.9651 0.9206 -0.2861 0.0693  -0.1391 302 ILE B O   
6016 C CB  . ILE B 302 ? 0.7970 1.0009 0.9652 -0.2397 0.0524  -0.1605 302 ILE B CB  
6017 C CG1 . ILE B 302 ? 0.7977 0.9645 0.9350 -0.2213 0.0429  -0.1413 302 ILE B CG1 
6018 C CG2 . ILE B 302 ? 0.8066 1.0492 1.0189 -0.2261 0.0374  -0.1675 302 ILE B CG2 
6019 C CD1 . ILE B 302 ? 0.7796 0.9608 0.9416 -0.1992 0.0373  -0.1392 302 ILE B CD1 
6020 N N   . GLU B 303 ? 1.1464 1.3202 1.2576 -0.2972 0.0909  -0.1650 303 GLU B N   
6021 C CA  . GLU B 303 ? 1.2060 1.3553 1.2804 -0.3126 0.1040  -0.1576 303 GLU B CA  
6022 C C   . GLU B 303 ? 1.1884 1.3360 1.2648 -0.2899 0.1022  -0.1536 303 GLU B C   
6023 O O   . GLU B 303 ? 1.1670 1.3341 1.2768 -0.2645 0.0921  -0.1574 303 GLU B O   
6024 C CB  . GLU B 303 ? 1.2329 1.4151 1.3162 -0.3437 0.1255  -0.1743 303 GLU B CB  
6025 C CG  . GLU B 303 ? 1.2689 1.4266 1.3163 -0.3797 0.1329  -0.1674 303 GLU B CG  
6026 C CD  . GLU B 303 ? 1.3599 1.4528 1.3511 -0.3832 0.1247  -0.1417 303 GLU B CD  
6027 O OE1 . GLU B 303 ? 1.3682 1.4302 1.3309 -0.4081 0.1242  -0.1326 303 GLU B OE1 
6028 O OE2 . GLU B 303 ? 1.3346 1.4070 1.3119 -0.3613 0.1176  -0.1307 303 GLU B OE2 
6029 N N   . ALA B 304 ? 0.8642 0.9859 0.9028 -0.3005 0.1103  -0.1442 304 ALA B N   
6030 C CA  . ALA B 304 ? 0.8565 0.9720 0.8919 -0.2812 0.1080  -0.1394 304 ALA B CA  
6031 C C   . ALA B 304 ? 0.8327 0.9965 0.9163 -0.2723 0.1161  -0.1618 304 ALA B C   
6032 O O   . ALA B 304 ? 0.8561 1.0547 0.9570 -0.2916 0.1330  -0.1812 304 ALA B O   
6033 C CB  . ALA B 304 ? 0.8452 0.9298 0.8314 -0.2985 0.1158  -0.1272 304 ALA B CB  
6034 N N   . LEU B 305 ? 0.9688 1.1357 1.0768 -0.2433 0.1035  -0.1601 305 LEU B N   
6035 C CA  . LEU B 305 ? 0.9335 1.1407 1.0933 -0.2302 0.1063  -0.1808 305 LEU B CA  
6036 C C   . LEU B 305 ? 0.9546 1.1705 1.1094 -0.2375 0.1224  -0.1934 305 LEU B C   
6037 O O   . LEU B 305 ? 0.8808 1.1353 1.0802 -0.2330 0.1302  -0.2180 305 LEU B O   
6038 C CB  . LEU B 305 ? 0.9023 1.1040 1.0867 -0.1991 0.0850  -0.1712 305 LEU B CB  
6039 C CG  . LEU B 305 ? 0.9384 1.1452 1.1392 -0.1895 0.0679  -0.1638 305 LEU B CG  
6040 C CD1 . LEU B 305 ? 0.9248 1.1073 1.1158 -0.1674 0.0484  -0.1430 305 LEU B CD1 
6041 C CD2 . LEU B 305 ? 0.8914 1.1441 1.1522 -0.1831 0.0652  -0.1838 305 LEU B CD2 
6042 N N   . SER B 306 ? 0.8601 1.0430 0.9632 -0.2490 0.1269  -0.1787 306 SER B N   
6043 C CA  . SER B 306 ? 0.8410 1.0300 0.9316 -0.2572 0.1406  -0.1885 306 SER B CA  
6044 C C   . SER B 306 ? 0.9159 1.0807 0.9475 -0.2869 0.1505  -0.1752 306 SER B C   
6045 O O   . SER B 306 ? 0.9393 1.0723 0.9406 -0.2937 0.1420  -0.1549 306 SER B O   
6046 C CB  . SER B 306 ? 0.8440 1.0130 0.9345 -0.2329 0.1285  -0.1799 306 SER B CB  
6047 O OG  . SER B 306 ? 0.8659 0.9915 0.9041 -0.2351 0.1208  -0.1539 306 SER B OG  
6048 N N   . SER B 307 ? 0.9936 1.1742 1.0099 -0.3055 0.1677  -0.1875 307 SER B N   
6049 C CA  . SER B 307 ? 1.0096 1.1761 0.9726 -0.3401 0.1787  -0.1768 307 SER B CA  
6050 C C   . SER B 307 ? 1.0472 1.2103 0.9778 -0.3494 0.1865  -0.1772 307 SER B C   
6051 O O   . SER B 307 ? 1.0268 1.2178 0.9862 -0.3380 0.1932  -0.1992 307 SER B O   
6052 C CB  . SER B 307 ? 0.9595 1.1679 0.9392 -0.3682 0.1981  -0.1975 307 SER B CB  
6053 O OG  . SER B 307 ? 1.0545 1.2453 0.9810 -0.4051 0.2064  -0.1827 307 SER B OG  
6054 N N   . GLY B 308 ? 1.1502 1.2771 1.0212 -0.3699 0.1835  -0.1526 308 GLY B N   
6055 C CA  . GLY B 308 ? 1.0996 1.2184 0.9324 -0.3796 0.1869  -0.1478 308 GLY B CA  
6056 C C   . GLY B 308 ? 1.1474 1.2551 0.9940 -0.3477 0.1743  -0.1469 308 GLY B C   
6057 O O   . GLY B 308 ? 1.1162 1.2461 0.9656 -0.3497 0.1840  -0.1641 308 GLY B O   
6058 N N   . ASN B 309 ? 1.1288 1.2036 0.9825 -0.3203 0.1533  -0.1279 309 ASN B N   
6059 C CA  . ASN B 309 ? 1.0800 1.1456 0.9485 -0.2916 0.1409  -0.1258 309 ASN B CA  
6060 C C   . ASN B 309 ? 1.0927 1.1381 0.9163 -0.2991 0.1375  -0.1130 309 ASN B C   
6061 O O   . ASN B 309 ? 1.1235 1.1438 0.8987 -0.3187 0.1345  -0.0931 309 ASN B O   
6062 C CB  . ASN B 309 ? 1.0660 1.1034 0.9453 -0.2653 0.1201  -0.1069 309 ASN B CB  
6063 C CG  . ASN B 309 ? 1.0837 1.1433 1.0125 -0.2516 0.1191  -0.1195 309 ASN B CG  
6064 O OD1 . ASN B 309 ? 1.0418 1.0853 0.9736 -0.2422 0.1073  -0.1070 309 ASN B OD1 
6065 N ND2 . ASN B 309 ? 1.1073 1.2058 1.0771 -0.2501 0.1307  -0.1462 309 ASN B ND2 
6066 N N   . LYS B 310 ? 0.9612 1.0164 0.8026 -0.2832 0.1359  -0.1238 310 LYS B N   
6067 C CA  . LYS B 310 ? 0.9837 1.0177 0.7901 -0.2822 0.1270  -0.1099 310 LYS B CA  
6068 C C   . LYS B 310 ? 0.9977 1.0030 0.8129 -0.2534 0.1053  -0.0899 310 LYS B C   
6069 O O   . LYS B 310 ? 0.9470 0.9606 0.7980 -0.2316 0.1001  -0.0982 310 LYS B O   
6070 C CB  . LYS B 310 ? 0.9811 1.0436 0.8019 -0.2837 0.1382  -0.1354 310 LYS B CB  
6071 C CG  . LYS B 310 ? 1.0534 1.0978 0.8520 -0.2757 0.1264  -0.1244 310 LYS B CG  
6072 C CD  . LYS B 310 ? 1.1087 1.1427 0.8468 -0.3026 0.1278  -0.1109 310 LYS B CD  
6073 C CE  . LYS B 310 ? 1.1081 1.1229 0.8268 -0.2917 0.1121  -0.0972 310 LYS B CE  
6074 N NZ  . LYS B 310 ? 1.1610 1.1386 0.8359 -0.2946 0.0941  -0.0628 310 LYS B NZ  
6075 N N   . GLU B 311 ? 0.8685 0.8404 0.6518 -0.2542 0.0923  -0.0642 311 GLU B N   
6076 C CA  . GLU B 311 ? 0.8688 0.8169 0.6580 -0.2292 0.0730  -0.0468 311 GLU B CA  
6077 C C   . GLU B 311 ? 0.8659 0.7956 0.6264 -0.2249 0.0611  -0.0322 311 GLU B C   
6078 O O   . GLU B 311 ? 0.9069 0.8322 0.6316 -0.2439 0.0639  -0.0281 311 GLU B O   
6079 C CB  . GLU B 311 ? 0.8493 0.7740 0.6286 -0.2297 0.0651  -0.0321 311 GLU B CB  
6080 C CG  . GLU B 311 ? 0.8254 0.7693 0.6291 -0.2381 0.0767  -0.0460 311 GLU B CG  
6081 C CD  . GLU B 311 ? 0.8627 0.7819 0.6525 -0.2436 0.0699  -0.0331 311 GLU B CD  
6082 O OE1 . GLU B 311 ? 0.8825 0.7677 0.6373 -0.2471 0.0585  -0.0138 311 GLU B OE1 
6083 O OE2 . GLU B 311 ? 0.8656 0.7990 0.6797 -0.2456 0.0753  -0.0429 311 GLU B OE2 
6084 N N   . PHE B 312 ? 0.8541 0.7755 0.6304 -0.2009 0.0470  -0.0240 312 PHE B N   
6085 C CA  . PHE B 312 ? 0.7809 0.6901 0.5391 -0.1931 0.0343  -0.0119 312 PHE B CA  
6086 C C   . PHE B 312 ? 0.7988 0.6949 0.5690 -0.1703 0.0185  0.0010  312 PHE B C   
6087 O O   . PHE B 312 ? 0.7512 0.6529 0.5474 -0.1596 0.0185  -0.0024 312 PHE B O   
6088 C CB  . PHE B 312 ? 0.7493 0.6796 0.5236 -0.1905 0.0396  -0.0266 312 PHE B CB  
6089 C CG  . PHE B 312 ? 0.7987 0.7450 0.6197 -0.1728 0.0402  -0.0377 312 PHE B CG  
6090 C CD1 . PHE B 312 ? 0.7892 0.7550 0.6403 -0.1757 0.0526  -0.0563 312 PHE B CD1 
6091 C CD2 . PHE B 312 ? 0.7582 0.7008 0.5939 -0.1538 0.0270  -0.0284 312 PHE B CD2 
6092 C CE1 . PHE B 312 ? 0.7358 0.7131 0.6304 -0.1590 0.0493  -0.0634 312 PHE B CE1 
6093 C CE2 . PHE B 312 ? 0.6840 0.6387 0.5587 -0.1404 0.0254  -0.0347 312 PHE B CE2 
6094 C CZ  . PHE B 312 ? 0.6880 0.6579 0.5920 -0.1424 0.0352  -0.0510 312 PHE B CZ  
6095 N N   . LYS B 313 ? 0.9576 0.8390 0.7086 -0.1637 0.0047  0.0148  313 LYS B N   
6096 C CA  . LYS B 313 ? 0.8810 0.7548 0.6431 -0.1428 -0.0095 0.0242  313 LYS B CA  
6097 C C   . LYS B 313 ? 0.9266 0.8205 0.7133 -0.1291 -0.0118 0.0197  313 LYS B C   
6098 O O   . LYS B 313 ? 0.9101 0.8128 0.6933 -0.1345 -0.0096 0.0155  313 LYS B O   
6099 C CB  . LYS B 313 ? 0.9415 0.7906 0.6750 -0.1413 -0.0249 0.0403  313 LYS B CB  
6100 C CG  . LYS B 313 ? 1.0009 0.8226 0.7157 -0.1497 -0.0285 0.0486  313 LYS B CG  
6101 C CD  . LYS B 313 ? 0.9872 0.8139 0.7269 -0.1430 -0.0228 0.0404  313 LYS B CD  
6102 C CE  . LYS B 313 ? 1.0114 0.8078 0.7407 -0.1413 -0.0331 0.0487  313 LYS B CE  
6103 N NZ  . LYS B 313 ? 1.0850 0.8554 0.7808 -0.1646 -0.0330 0.0587  313 LYS B NZ  
6104 N N   . GLY B 314 ? 0.7678 0.6695 0.5783 -0.1136 -0.0164 0.0204  314 GLY B N   
6105 C CA  . GLY B 314 ? 0.7583 0.6777 0.5900 -0.1028 -0.0203 0.0197  314 GLY B CA  
6106 C C   . GLY B 314 ? 0.7781 0.7024 0.6200 -0.0875 -0.0297 0.0260  314 GLY B C   
6107 O O   . GLY B 314 ? 0.7767 0.6952 0.6196 -0.0837 -0.0306 0.0261  314 GLY B O   
6108 N N   . THR B 315 ? 0.7440 0.6814 0.5935 -0.0800 -0.0364 0.0296  315 THR B N   
6109 C CA  . THR B 315 ? 0.7436 0.6914 0.6001 -0.0669 -0.0449 0.0337  315 THR B CA  
6110 C C   . THR B 315 ? 0.7406 0.7101 0.6207 -0.0637 -0.0428 0.0328  315 THR B C   
6111 O O   . THR B 315 ? 0.7058 0.6855 0.5984 -0.0678 -0.0414 0.0336  315 THR B O   
6112 C CB  . THR B 315 ? 0.7224 0.6763 0.5733 -0.0626 -0.0537 0.0381  315 THR B CB  
6113 O OG1 . THR B 315 ? 0.8448 0.7784 0.6717 -0.0686 -0.0571 0.0411  315 THR B OG1 
6114 C CG2 . THR B 315 ? 0.7261 0.6918 0.5841 -0.0486 -0.0621 0.0388  315 THR B CG2 
6115 N N   . VAL B 316 ? 0.6435 0.6186 0.5291 -0.0577 -0.0435 0.0313  316 VAL B N   
6116 C CA  . VAL B 316 ? 0.5911 0.5896 0.4942 -0.0556 -0.0440 0.0328  316 VAL B CA  
6117 C C   . VAL B 316 ? 0.6103 0.6256 0.5129 -0.0461 -0.0493 0.0317  316 VAL B C   
6118 O O   . VAL B 316 ? 0.6072 0.6158 0.5047 -0.0400 -0.0504 0.0256  316 VAL B O   
6119 C CB  . VAL B 316 ? 0.5901 0.5874 0.5010 -0.0585 -0.0399 0.0294  316 VAL B CB  
6120 C CG1 . VAL B 316 ? 0.5791 0.6009 0.5063 -0.0590 -0.0428 0.0346  316 VAL B CG1 
6121 C CG2 . VAL B 316 ? 0.6243 0.6060 0.5367 -0.0668 -0.0333 0.0256  316 VAL B CG2 
6122 N N   . PHE B 317 ? 0.6159 0.6542 0.5256 -0.0455 -0.0523 0.0357  317 PHE B N   
6123 C CA  . PHE B 317 ? 0.6317 0.6946 0.5446 -0.0374 -0.0557 0.0315  317 PHE B CA  
6124 C C   . PHE B 317 ? 0.6645 0.7116 0.5696 -0.0261 -0.0604 0.0242  317 PHE B C   
6125 O O   . PHE B 317 ? 0.6895 0.7418 0.5972 -0.0172 -0.0620 0.0148  317 PHE B O   
6126 C CB  . PHE B 317 ? 0.6204 0.7039 0.5390 -0.0381 -0.0534 0.0285  317 PHE B CB  
6127 C CG  . PHE B 317 ? 0.6319 0.7518 0.5560 -0.0333 -0.0544 0.0222  317 PHE B CG  
6128 C CD1 . PHE B 317 ? 0.6152 0.7563 0.5443 -0.0333 -0.0566 0.0243  317 PHE B CD1 
6129 C CD2 . PHE B 317 ? 0.6247 0.7616 0.5499 -0.0301 -0.0526 0.0120  317 PHE B CD2 
6130 C CE1 . PHE B 317 ? 0.6216 0.8024 0.5582 -0.0299 -0.0559 0.0159  317 PHE B CE1 
6131 C CE2 . PHE B 317 ? 0.6017 0.7780 0.5328 -0.0266 -0.0517 0.0023  317 PHE B CE2 
6132 C CZ  . PHE B 317 ? 0.5955 0.7953 0.5331 -0.0266 -0.0528 0.0040  317 PHE B CZ  
6133 N N   . PHE B 318 ? 0.6440 0.6704 0.5395 -0.0270 -0.0639 0.0283  318 PHE B N   
6134 C CA  . PHE B 318 ? 0.6358 0.6423 0.5222 -0.0178 -0.0724 0.0260  318 PHE B CA  
6135 C C   . PHE B 318 ? 0.6748 0.6501 0.5509 -0.0170 -0.0725 0.0233  318 PHE B C   
6136 O O   . PHE B 318 ? 0.6872 0.6434 0.5583 -0.0081 -0.0819 0.0215  318 PHE B O   
6137 C CB  . PHE B 318 ? 0.6240 0.6553 0.5237 -0.0036 -0.0797 0.0184  318 PHE B CB  
6138 C CG  . PHE B 318 ? 0.6603 0.7288 0.5721 -0.0065 -0.0785 0.0200  318 PHE B CG  
6139 C CD1 . PHE B 318 ? 0.6279 0.7298 0.5509 -0.0110 -0.0716 0.0176  318 PHE B CD1 
6140 C CD2 . PHE B 318 ? 0.6429 0.7145 0.5538 -0.0063 -0.0854 0.0244  318 PHE B CD2 
6141 C CE1 . PHE B 318 ? 0.6036 0.7393 0.5362 -0.0171 -0.0707 0.0208  318 PHE B CE1 
6142 C CE2 . PHE B 318 ? 0.6155 0.7223 0.5385 -0.0110 -0.0843 0.0255  318 PHE B CE2 
6143 C CZ  . PHE B 318 ? 0.6423 0.7807 0.5762 -0.0170 -0.0766 0.0241  318 PHE B CZ  
6144 N N   . ASP B 319 ? 0.6155 0.6480 0.7269 -0.0210 -0.0802 -0.1765 319 ASP B N   
6145 C CA  . ASP B 319 ? 0.6473 0.6531 0.7176 -0.0308 -0.0840 -0.1576 319 ASP B CA  
6146 C C   . ASP B 319 ? 0.7076 0.7208 0.7465 -0.0374 -0.0893 -0.1426 319 ASP B C   
6147 O O   . ASP B 319 ? 0.6672 0.7067 0.7101 -0.0423 -0.0798 -0.1450 319 ASP B O   
6148 C CB  . ASP B 319 ? 0.6361 0.6358 0.6985 -0.0447 -0.0660 -0.1563 319 ASP B CB  
6149 C CG  . ASP B 319 ? 0.6855 0.6677 0.7663 -0.0385 -0.0604 -0.1692 319 ASP B CG  
6150 O OD1 . ASP B 319 ? 0.6628 0.6365 0.7659 -0.0234 -0.0708 -0.1780 319 ASP B OD1 
6151 O OD2 . ASP B 319 ? 0.6162 0.5935 0.6885 -0.0475 -0.0461 -0.1716 319 ASP B OD2 
6152 N N   . GLU B 320 ? 0.8570 0.8441 0.8632 -0.0372 -0.1020 -0.1267 320 GLU B N   
6153 C CA  . GLU B 320 ? 0.8756 0.8657 0.8475 -0.0416 -0.1054 -0.1121 320 GLU B CA  
6154 C C   . GLU B 320 ? 0.8678 0.8568 0.8197 -0.0630 -0.0890 -0.0983 320 GLU B C   
6155 O O   . GLU B 320 ? 0.9101 0.8705 0.8423 -0.0723 -0.0885 -0.0853 320 GLU B O   
6156 C CB  . GLU B 320 ? 0.9438 0.9028 0.8859 -0.0294 -0.1254 -0.1002 320 GLU B CB  
6157 C CG  . GLU B 320 ? 1.0706 1.0401 0.9873 -0.0207 -0.1363 -0.0968 320 GLU B CG  
6158 C CD  . GLU B 320 ? 1.1656 1.1544 1.1116 0.0002  -0.1556 -0.1174 320 GLU B CD  
6159 O OE1 . GLU B 320 ? 1.2533 1.2219 1.1953 0.0186  -0.1782 -0.1173 320 GLU B OE1 
6160 O OE2 . GLU B 320 ? 1.0718 1.0957 1.0476 -0.0013 -0.1486 -0.1346 320 GLU B OE2 
6161 N N   . PHE B 321 ? 0.6979 0.7187 0.6587 -0.0705 -0.0758 -0.1021 321 PHE B N   
6162 C CA  . PHE B 321 ? 0.6976 0.7278 0.6474 -0.0887 -0.0618 -0.0916 321 PHE B CA  
6163 C C   . PHE B 321 ? 0.7799 0.8090 0.6985 -0.0936 -0.0602 -0.0767 321 PHE B C   
6164 O O   . PHE B 321 ? 0.7764 0.8080 0.6813 -0.0817 -0.0681 -0.0778 321 PHE B O   
6165 C CB  . PHE B 321 ? 0.6659 0.7297 0.6388 -0.0907 -0.0491 -0.1017 321 PHE B CB  
6166 C CG  . PHE B 321 ? 0.6076 0.6700 0.5990 -0.0924 -0.0436 -0.1107 321 PHE B CG  
6167 C CD1 . PHE B 321 ? 0.5756 0.6250 0.5832 -0.0815 -0.0476 -0.1227 321 PHE B CD1 
6168 C CD2 . PHE B 321 ? 0.5670 0.6426 0.5591 -0.1037 -0.0344 -0.1082 321 PHE B CD2 
6169 C CE1 . PHE B 321 ? 0.5560 0.6018 0.5742 -0.0826 -0.0392 -0.1313 321 PHE B CE1 
6170 C CE2 . PHE B 321 ? 0.5490 0.6211 0.5491 -0.1036 -0.0303 -0.1165 321 PHE B CE2 
6171 C CZ  . PHE B 321 ? 0.5340 0.5892 0.5439 -0.0934 -0.0312 -0.1276 321 PHE B CZ  
6172 N N   . THR B 322 ? 0.7976 0.8234 0.7053 -0.1115 -0.0493 -0.0640 322 THR B N   
6173 C CA  . THR B 322 ? 0.8501 0.8824 0.7341 -0.1202 -0.0389 -0.0508 322 THR B CA  
6174 C C   . THR B 322 ? 0.8076 0.8818 0.7133 -0.1264 -0.0249 -0.0572 322 THR B C   
6175 O O   . THR B 322 ? 0.7583 0.8463 0.6864 -0.1370 -0.0191 -0.0600 322 THR B O   
6176 C CB  . THR B 322 ? 0.9012 0.9057 0.7676 -0.1376 -0.0322 -0.0338 322 THR B CB  
6177 O OG1 . THR B 322 ? 0.9751 0.9357 0.8196 -0.1288 -0.0457 -0.0268 322 THR B OG1 
6178 C CG2 . THR B 322 ? 0.9076 0.9188 0.7503 -0.1478 -0.0161 -0.0197 322 THR B CG2 
6179 N N   . PHE B 323 ? 0.7803 0.8733 0.6783 -0.1183 -0.0210 -0.0604 323 PHE B N   
6180 C CA  . PHE B 323 ? 0.7603 0.8906 0.6795 -0.1196 -0.0083 -0.0676 323 PHE B CA  
6181 C C   . PHE B 323 ? 0.8365 0.9791 0.7386 -0.1282 0.0074  -0.0578 323 PHE B C   
6182 O O   . PHE B 323 ? 0.8639 0.9879 0.7294 -0.1263 0.0078  -0.0490 323 PHE B O   
6183 C CB  . PHE B 323 ? 0.7172 0.8608 0.6480 -0.1032 -0.0131 -0.0835 323 PHE B CB  
6184 C CG  . PHE B 323 ? 0.6828 0.8236 0.6402 -0.0959 -0.0205 -0.0955 323 PHE B CG  
6185 C CD1 . PHE B 323 ? 0.6359 0.7916 0.6175 -0.0994 -0.0123 -0.0992 323 PHE B CD1 
6186 C CD2 . PHE B 323 ? 0.6746 0.7991 0.6329 -0.0839 -0.0350 -0.1039 323 PHE B CD2 
6187 C CE1 . PHE B 323 ? 0.6067 0.7566 0.6074 -0.0925 -0.0148 -0.1095 323 PHE B CE1 
6188 C CE2 . PHE B 323 ? 0.6355 0.7590 0.6221 -0.0778 -0.0372 -0.1161 323 PHE B CE2 
6189 C CZ  . PHE B 323 ? 0.6330 0.7673 0.6381 -0.0827 -0.0252 -0.1182 323 PHE B CZ  
6190 N N   . VAL B 324 ? 0.7799 0.9545 0.7079 -0.1353 0.0207  -0.0600 324 VAL B N   
6191 C CA  . VAL B 324 ? 0.8136 1.0111 0.7376 -0.1388 0.0385  -0.0571 324 VAL B CA  
6192 C C   . VAL B 324 ? 0.7591 0.9873 0.7103 -0.1276 0.0424  -0.0710 324 VAL B C   
6193 O O   . VAL B 324 ? 0.6874 0.9284 0.6681 -0.1261 0.0387  -0.0764 324 VAL B O   
6194 C CB  . VAL B 324 ? 0.8157 1.0246 0.7519 -0.1589 0.0530  -0.0461 324 VAL B CB  
6195 C CG1 . VAL B 324 ? 0.7391 0.9712 0.7175 -0.1646 0.0487  -0.0522 324 VAL B CG1 
6196 C CG2 . VAL B 324 ? 0.7980 1.0296 0.7298 -0.1619 0.0749  -0.0435 324 VAL B CG2 
6197 N N   . LYS B 325 ? 0.6718 0.9081 0.6096 -0.1188 0.0500  -0.0769 325 LYS B N   
6198 C CA  . LYS B 325 ? 0.6196 0.8796 0.5818 -0.1076 0.0556  -0.0903 325 LYS B CA  
6199 C C   . LYS B 325 ? 0.6174 0.9099 0.6074 -0.1136 0.0718  -0.0871 325 LYS B C   
6200 O O   . LYS B 325 ? 0.6830 0.9840 0.6670 -0.1252 0.0846  -0.0781 325 LYS B O   
6201 C CB  . LYS B 325 ? 0.6688 0.9246 0.6068 -0.0967 0.0573  -0.1005 325 LYS B CB  
6202 C CG  . LYS B 325 ? 0.6843 0.9637 0.6426 -0.0876 0.0703  -0.1135 325 LYS B CG  
6203 C CD  . LYS B 325 ? 0.6803 0.9509 0.6095 -0.0782 0.0688  -0.1262 325 LYS B CD  
6204 C CE  . LYS B 325 ? 0.7132 1.0039 0.6426 -0.0744 0.0894  -0.1337 325 LYS B CE  
6205 N NZ  . LYS B 325 ? 0.7482 1.0513 0.7131 -0.0638 0.0937  -0.1496 325 LYS B NZ  
6206 N N   . LEU B 326 ? 0.6665 0.9764 0.6884 -0.1055 0.0715  -0.0940 326 LEU B N   
6207 C CA  . LEU B 326 ? 0.6360 0.9796 0.6887 -0.1061 0.0833  -0.0929 326 LEU B CA  
6208 C C   . LEU B 326 ? 0.6413 0.9988 0.6953 -0.0953 0.0987  -0.1018 326 LEU B C   
6209 O O   . LEU B 326 ? 0.6406 0.9880 0.6931 -0.0824 0.0964  -0.1126 326 LEU B O   
6210 C CB  . LEU B 326 ? 0.6269 0.9779 0.7062 -0.0991 0.0739  -0.0945 326 LEU B CB  
6211 C CG  . LEU B 326 ? 0.6237 0.9559 0.6989 -0.1047 0.0574  -0.0908 326 LEU B CG  
6212 C CD1 . LEU B 326 ? 0.6113 0.9605 0.7100 -0.0999 0.0515  -0.0902 326 LEU B CD1 
6213 C CD2 . LEU B 326 ? 0.6441 0.9663 0.7060 -0.1229 0.0541  -0.0826 326 LEU B CD2 
6214 N N   . THR B 327 ? 0.7251 1.1049 0.7840 -0.1014 0.1161  -0.0989 327 THR B N   
6215 C CA  . THR B 327 ? 0.8019 1.1936 0.8580 -0.0916 0.1336  -0.1086 327 THR B CA  
6216 C C   . THR B 327 ? 0.7727 1.1979 0.8731 -0.0817 0.1435  -0.1133 327 THR B C   
6217 O O   . THR B 327 ? 0.8113 1.2357 0.9188 -0.0661 0.1477  -0.1245 327 THR B O   
6218 C CB  . THR B 327 ? 0.8400 1.2319 0.8671 -0.1023 0.1514  -0.1034 327 THR B CB  
6219 O OG1 . THR B 327 ? 0.8394 1.2522 0.8896 -0.1184 0.1604  -0.0919 327 THR B OG1 
6220 C CG2 . THR B 327 ? 0.8062 1.1599 0.7805 -0.1060 0.1407  -0.0994 327 THR B CG2 
6221 N N   . GLY B 328 ? 0.6750 1.1292 0.8076 -0.0899 0.1466  -0.1059 328 GLY B N   
6222 C CA  . GLY B 328 ? 0.6493 1.1385 0.8269 -0.0781 0.1530  -0.1101 328 GLY B CA  
6223 C C   . GLY B 328 ? 0.6734 1.1559 0.8660 -0.0626 0.1358  -0.1110 328 GLY B C   
6224 O O   . GLY B 328 ? 0.6681 1.1243 0.8429 -0.0647 0.1190  -0.1075 328 GLY B O   
6225 N N   . VAL B 329 ? 0.7964 1.3005 1.0206 -0.0453 0.1421  -0.1157 329 VAL B N   
6226 C CA  . VAL B 329 ? 0.7472 1.2465 0.9858 -0.0293 0.1274  -0.1130 329 VAL B CA  
6227 C C   . VAL B 329 ? 0.7535 1.2701 1.0078 -0.0370 0.1085  -0.1045 329 VAL B C   
6228 O O   . VAL B 329 ? 0.7130 1.2173 0.9641 -0.0270 0.0923  -0.1002 329 VAL B O   
6229 C CB  . VAL B 329 ? 0.7308 1.2478 0.9993 -0.0069 0.1387  -0.1186 329 VAL B CB  
6230 C CG1 . VAL B 329 ? 0.6634 1.2301 0.9776 -0.0053 0.1398  -0.1170 329 VAL B CG1 
6231 C CG2 . VAL B 329 ? 0.7750 1.2650 1.0392 0.0124  0.1295  -0.1159 329 VAL B CG2 
6232 N N   . ALA B 330 ? 0.6594 1.2026 0.9293 -0.0553 0.1114  -0.1028 330 ALA B N   
6233 C CA  . ALA B 330 ? 0.6565 1.2133 0.9400 -0.0679 0.0930  -0.0982 330 ALA B CA  
6234 C C   . ALA B 330 ? 0.6374 1.1966 0.9157 -0.0948 0.1021  -0.0958 330 ALA B C   
6235 O O   . ALA B 330 ? 0.6906 1.2554 0.9657 -0.1011 0.1245  -0.0970 330 ALA B O   
6236 C CB  . ALA B 330 ? 0.6154 1.2178 0.9486 -0.0567 0.0841  -0.1002 330 ALA B CB  
6237 N N   . GLY B 331 ? 0.5110 1.0625 0.7854 -0.1102 0.0857  -0.0923 331 GLY B N   
6238 C CA  . GLY B 331 ? 0.5203 1.0646 0.7864 -0.1362 0.0944  -0.0882 331 GLY B CA  
6239 C C   . GLY B 331 ? 0.5696 1.1051 0.8372 -0.1516 0.0741  -0.0869 331 GLY B C   
6240 O O   . GLY B 331 ? 0.5418 1.0710 0.8065 -0.1416 0.0520  -0.0894 331 GLY B O   
6241 N N   . ASN B 332 ? 0.6591 1.1920 0.9296 -0.1765 0.0840  -0.0831 332 ASN B N   
6242 C CA  . ASN B 332 ? 0.6729 1.1884 0.9405 -0.1959 0.0696  -0.0822 332 ASN B CA  
6243 C C   . ASN B 332 ? 0.7107 1.1782 0.9322 -0.2084 0.0802  -0.0723 332 ASN B C   
6244 O O   . ASN B 332 ? 0.6890 1.1562 0.9060 -0.2201 0.1038  -0.0657 332 ASN B O   
6245 C CB  . ASN B 332 ? 0.6146 1.1723 0.9377 -0.2163 0.0720  -0.0876 332 ASN B CB  
6246 C CG  . ASN B 332 ? 0.5756 1.1842 0.9475 -0.2018 0.0561  -0.0984 332 ASN B CG  
6247 O OD1 . ASN B 332 ? 0.6134 1.2166 0.9767 -0.1883 0.0298  -0.1029 332 ASN B OD1 
6248 N ND2 . ASN B 332 ? 0.5354 1.1929 0.9575 -0.2036 0.0722  -0.1025 332 ASN B ND2 
6249 N N   . TYR B 333 ? 0.6765 1.1029 0.8629 -0.2047 0.0635  -0.0710 333 TYR B N   
6250 C CA  . TYR B 333 ? 0.7028 1.0813 0.8438 -0.2104 0.0683  -0.0619 333 TYR B CA  
6251 C C   . TYR B 333 ? 0.7095 1.0567 0.8415 -0.2239 0.0534  -0.0614 333 TYR B C   
6252 O O   . TYR B 333 ? 0.7041 1.0553 0.8477 -0.2203 0.0343  -0.0700 333 TYR B O   
6253 C CB  . TYR B 333 ? 0.6748 1.0299 0.7807 -0.1880 0.0639  -0.0628 333 TYR B CB  
6254 C CG  . TYR B 333 ? 0.7686 1.1374 0.8676 -0.1774 0.0818  -0.0627 333 TYR B CG  
6255 C CD1 . TYR B 333 ? 0.7637 1.1111 0.8284 -0.1822 0.0965  -0.0548 333 TYR B CD1 
6256 C CD2 . TYR B 333 ? 0.7170 1.1164 0.8397 -0.1611 0.0839  -0.0706 333 TYR B CD2 
6257 C CE1 . TYR B 333 ? 0.7589 1.1176 0.8128 -0.1719 0.1126  -0.0574 333 TYR B CE1 
6258 C CE2 . TYR B 333 ? 0.7099 1.1196 0.8266 -0.1512 0.1008  -0.0730 333 TYR B CE2 
6259 C CZ  . TYR B 333 ? 0.7404 1.1309 0.8227 -0.1570 0.1150  -0.0677 333 TYR B CZ  
6260 O OH  . TYR B 333 ? 0.7356 1.1362 0.8093 -0.1463 0.1314  -0.0729 333 TYR B OH  
6261 N N   . THR B 334 ? 0.6596 0.9718 0.7666 -0.2384 0.0627  -0.0508 334 THR B N   
6262 C CA  . THR B 334 ? 0.6452 0.9163 0.7358 -0.2483 0.0504  -0.0491 334 THR B CA  
6263 C C   . THR B 334 ? 0.7137 0.9363 0.7544 -0.2399 0.0518  -0.0383 334 THR B C   
6264 O O   . THR B 334 ? 0.7525 0.9669 0.7706 -0.2409 0.0686  -0.0273 334 THR B O   
6265 C CB  . THR B 334 ? 0.6583 0.9291 0.7734 -0.2773 0.0593  -0.0464 334 THR B CB  
6266 O OG1 . THR B 334 ? 0.6422 0.9621 0.8096 -0.2852 0.0536  -0.0594 334 THR B OG1 
6267 C CG2 . THR B 334 ? 0.6800 0.9020 0.7762 -0.2863 0.0469  -0.0456 334 THR B CG2 
6268 N N   . VAL B 335 ? 0.7637 0.9544 0.7867 -0.2308 0.0339  -0.0422 335 VAL B N   
6269 C CA  . VAL B 335 ? 0.8063 0.9522 0.7880 -0.2203 0.0296  -0.0342 335 VAL B CA  
6270 C C   . VAL B 335 ? 0.8377 0.9463 0.8146 -0.2248 0.0155  -0.0368 335 VAL B C   
6271 O O   . VAL B 335 ? 0.7536 0.8724 0.7509 -0.2248 0.0043  -0.0497 335 VAL B O   
6272 C CB  . VAL B 335 ? 0.7559 0.9077 0.7242 -0.1954 0.0229  -0.0405 335 VAL B CB  
6273 C CG1 . VAL B 335 ? 0.7349 0.9024 0.7245 -0.1848 0.0108  -0.0548 335 VAL B CG1 
6274 C CG2 . VAL B 335 ? 0.8100 0.9197 0.7411 -0.1839 0.0146  -0.0345 335 VAL B CG2 
6275 N N   . CYS B 336 ? 0.8500 0.9130 0.7970 -0.2274 0.0163  -0.0246 336 CYS B N   
6276 C CA  . CYS B 336 ? 0.8255 0.8479 0.7687 -0.2331 0.0060  -0.0259 336 CYS B CA  
6277 C C   . CYS B 336 ? 0.8454 0.8265 0.7555 -0.2134 -0.0051 -0.0208 336 CYS B C   
6278 O O   . CYS B 336 ? 0.8743 0.8505 0.7579 -0.2006 -0.0034 -0.0118 336 CYS B O   
6279 C CB  . CYS B 336 ? 0.8599 0.8595 0.8057 -0.2595 0.0188  -0.0150 336 CYS B CB  
6280 S SG  . CYS B 336 ? 0.8608 0.9126 0.8540 -0.2850 0.0328  -0.0215 336 CYS B SG  
6281 N N   . GLN B 337 ? 0.8275 0.7804 0.7406 -0.2100 -0.0177 -0.0286 337 GLN B N   
6282 C CA  . GLN B 337 ? 0.8743 0.7829 0.7622 -0.1934 -0.0287 -0.0235 337 GLN B CA  
6283 C C   . GLN B 337 ? 0.9125 0.7818 0.8056 -0.2030 -0.0335 -0.0271 337 GLN B C   
6284 O O   . GLN B 337 ? 0.8846 0.7666 0.8011 -0.2077 -0.0378 -0.0443 337 GLN B O   
6285 C CB  . GLN B 337 ? 0.8388 0.7631 0.7320 -0.1680 -0.0412 -0.0367 337 GLN B CB  
6286 C CG  . GLN B 337 ? 0.8857 0.7721 0.7593 -0.1478 -0.0551 -0.0330 337 GLN B CG  
6287 C CD  . GLN B 337 ? 0.8512 0.7576 0.7423 -0.1258 -0.0657 -0.0499 337 GLN B CD  
6288 O OE1 . GLN B 337 ? 0.8141 0.7148 0.7249 -0.1204 -0.0703 -0.0640 337 GLN B OE1 
6289 N NE2 . GLN B 337 ? 0.8352 0.7644 0.7202 -0.1136 -0.0681 -0.0500 337 GLN B NE2 
6290 N N   . LYS B 338 ? 0.9868 0.8056 0.8546 -0.2050 -0.0324 -0.0109 338 LYS B N   
6291 C CA  . LYS B 338 ? 1.0181 0.7909 0.8886 -0.2156 -0.0344 -0.0123 338 LYS B CA  
6292 C C   . LYS B 338 ? 0.9962 0.7880 0.8978 -0.2431 -0.0272 -0.0249 338 LYS B C   
6293 O O   . LYS B 338 ? 1.0359 0.8399 0.9447 -0.2654 -0.0124 -0.0161 338 LYS B O   
6294 C CB  . LYS B 338 ? 1.0472 0.7999 0.9207 -0.1930 -0.0510 -0.0260 338 LYS B CB  
6295 C CG  . LYS B 338 ? 1.0576 0.7942 0.9075 -0.1645 -0.0624 -0.0165 338 LYS B CG  
6296 C CD  . LYS B 338 ? 1.1657 0.8533 1.0125 -0.1483 -0.0750 -0.0196 338 LYS B CD  
6297 C CE  . LYS B 338 ? 1.0772 0.7852 0.9544 -0.1353 -0.0827 -0.0458 338 LYS B CE  
6298 N NZ  . LYS B 338 ? 1.0728 0.8053 0.9549 -0.1085 -0.0937 -0.0508 338 LYS B NZ  
6299 N N   . ASP B 339 ? 1.0492 0.8447 0.9698 -0.2416 -0.0374 -0.0465 339 ASP B N   
6300 C CA  . ASP B 339 ? 1.0505 0.8596 0.9976 -0.2662 -0.0358 -0.0614 339 ASP B CA  
6301 C C   . ASP B 339 ? 0.9830 0.8558 0.9525 -0.2683 -0.0372 -0.0738 339 ASP B C   
6302 O O   . ASP B 339 ? 0.9532 0.8458 0.9466 -0.2873 -0.0390 -0.0871 339 ASP B O   
6303 C CB  . ASP B 339 ? 1.0542 0.8295 1.0041 -0.2638 -0.0465 -0.0801 339 ASP B CB  
6304 C CG  . ASP B 339 ? 1.1430 0.8510 1.0762 -0.2647 -0.0447 -0.0691 339 ASP B CG  
6305 O OD1 . ASP B 339 ? 1.1977 0.8828 1.1244 -0.2815 -0.0327 -0.0501 339 ASP B OD1 
6306 O OD2 . ASP B 339 ? 1.1484 0.8248 1.0749 -0.2479 -0.0537 -0.0788 339 ASP B OD2 
6307 N N   . LEU B 340 ? 0.7460 0.7792 0.7833 -0.1918 0.1232  -0.1000 340 LEU B N   
6308 C CA  . LEU B 340 ? 0.7046 0.7864 0.7638 -0.1857 0.1000  -0.1143 340 LEU B CA  
6309 C C   . LEU B 340 ? 0.6943 0.8019 0.7677 -0.1862 0.1089  -0.1135 340 LEU B C   
6310 O O   . LEU B 340 ? 0.7258 0.8185 0.7681 -0.1751 0.1158  -0.0959 340 LEU B O   
6311 C CB  . LEU B 340 ? 0.6278 0.7103 0.6577 -0.1639 0.0766  -0.1045 340 LEU B CB  
6312 C CG  . LEU B 340 ? 0.6216 0.7458 0.6665 -0.1545 0.0534  -0.1150 340 LEU B CG  
6313 C CD1 . LEU B 340 ? 0.6239 0.7645 0.6872 -0.1590 0.0383  -0.1361 340 LEU B CD1 
6314 C CD2 . LEU B 340 ? 0.5986 0.7182 0.6145 -0.1345 0.0396  -0.0986 340 LEU B CD2 
6315 N N   . CYS B 341 ? 0.7968 0.9450 0.9171 -0.1966 0.1067  -0.1341 341 CYS B N   
6316 C CA  . CYS B 341 ? 0.7807 0.9604 0.9194 -0.1931 0.1122  -0.1363 341 CYS B CA  
6317 C C   . CYS B 341 ? 0.7823 1.0042 0.9387 -0.1795 0.0819  -0.1490 341 CYS B C   
6318 O O   . CYS B 341 ? 0.7462 0.9879 0.9246 -0.1822 0.0628  -0.1657 341 CYS B O   
6319 C CB  . CYS B 341 ? 0.7958 0.9918 0.9816 -0.2150 0.1393  -0.1483 341 CYS B CB  
6320 S SG  . CYS B 341 ? 0.9154 1.0606 1.0737 -0.2268 0.1843  -0.1267 341 CYS B SG  
6321 N N   . CYS B 342 ? 0.7059 0.9378 0.8489 -0.1635 0.0775  -0.1411 342 CYS B N   
6322 C CA  . CYS B 342 ? 0.6648 0.9266 0.8155 -0.1465 0.0511  -0.1473 342 CYS B CA  
6323 C C   . CYS B 342 ? 0.6705 0.9681 0.8559 -0.1437 0.0581  -0.1572 342 CYS B C   
6324 O O   . CYS B 342 ? 0.6982 0.9851 0.8717 -0.1429 0.0793  -0.1492 342 CYS B O   
6325 C CB  . CYS B 342 ? 0.6406 0.8772 0.7454 -0.1286 0.0390  -0.1291 342 CYS B CB  
6326 S SG  . CYS B 342 ? 0.6846 0.8810 0.7521 -0.1292 0.0349  -0.1156 342 CYS B SG  
6327 N N   . HIS B 343 ? 0.8365 1.1761 1.0622 -0.1398 0.0396  -0.1750 343 HIS B N   
6328 C CA  . HIS B 343 ? 0.8096 1.1905 1.0768 -0.1335 0.0419  -0.1870 343 HIS B CA  
6329 C C   . HIS B 343 ? 0.8332 1.2259 1.0895 -0.1080 0.0141  -0.1852 343 HIS B C   
6330 O O   . HIS B 343 ? 0.7987 1.1920 1.0438 -0.0999 -0.0116 -0.1861 343 HIS B O   
6331 C CB  . HIS B 343 ? 0.8019 1.2277 1.1349 -0.1485 0.0413  -0.2114 343 HIS B CB  
6332 C CG  . HIS B 343 ? 0.8199 1.2309 1.1687 -0.1764 0.0667  -0.2149 343 HIS B CG  
6333 N ND1 . HIS B 343 ? 0.8705 1.2508 1.2017 -0.1873 0.1030  -0.2007 343 HIS B ND1 
6334 C CD2 . HIS B 343 ? 0.8305 1.2497 1.2098 -0.1952 0.0614  -0.2315 343 HIS B CD2 
6335 C CE1 . HIS B 343 ? 0.8623 1.2303 1.2132 -0.2118 0.1211  -0.2058 343 HIS B CE1 
6336 N NE2 . HIS B 343 ? 0.8237 1.2151 1.2064 -0.2182 0.0962  -0.2259 343 HIS B NE2 
6337 N N   . LEU B 344 ? 0.5593 0.9578 0.8161 -0.0947 0.0210  -0.1823 344 LEU B N   
6338 C CA  . LEU B 344 ? 0.5439 0.9505 0.7949 -0.0702 -0.0017 -0.1807 344 LEU B CA  
6339 C C   . LEU B 344 ? 0.5562 1.0020 0.8524 -0.0608 0.0048  -0.1943 344 LEU B C   
6340 O O   . LEU B 344 ? 0.5871 1.0341 0.8925 -0.0674 0.0327  -0.1961 344 LEU B O   
6341 C CB  . LEU B 344 ? 0.5576 0.9208 0.7557 -0.0595 -0.0024 -0.1620 344 LEU B CB  
6342 C CG  . LEU B 344 ? 0.5304 0.8959 0.7251 -0.0354 -0.0208 -0.1599 344 LEU B CG  
6343 C CD1 . LEU B 344 ? 0.5380 0.9067 0.7270 -0.0263 -0.0476 -0.1569 344 LEU B CD1 
6344 C CD2 . LEU B 344 ? 0.5616 0.8877 0.7159 -0.0285 -0.0166 -0.1470 344 LEU B CD2 
6345 N N   . SER B 345 ? 0.4834 0.9603 0.8055 -0.0432 -0.0201 -0.2033 345 SER B N   
6346 C CA  . SER B 345 ? 0.4625 0.9734 0.8235 -0.0262 -0.0188 -0.2140 345 SER B CA  
6347 C C   . SER B 345 ? 0.5055 0.9983 0.8376 0.0015  -0.0421 -0.2037 345 SER B C   
6348 O O   . SER B 345 ? 0.5343 1.0109 0.8384 0.0078  -0.0651 -0.1949 345 SER B O   
6349 C CB  . SER B 345 ? 0.4488 1.0198 0.8793 -0.0303 -0.0269 -0.2365 345 SER B CB  
6350 O OG  . SER B 345 ? 0.5181 1.1244 0.9821 -0.0042 -0.0440 -0.2455 345 SER B OG  
6351 N N   . TYR B 346 ? 0.5355 1.0234 0.8683 0.0177  -0.0329 -0.2034 346 TYR B N   
6352 C CA  . TYR B 346 ? 0.5399 0.9966 0.8388 0.0406  -0.0504 -0.1910 346 TYR B CA  
6353 C C   . TYR B 346 ? 0.5936 1.0595 0.9129 0.0627  -0.0445 -0.1983 346 TYR B C   
6354 O O   . TYR B 346 ? 0.5810 1.0581 0.9177 0.0577  -0.0188 -0.2079 346 TYR B O   
6355 C CB  . TYR B 346 ? 0.6040 1.0050 0.8455 0.0314  -0.0439 -0.1737 346 TYR B CB  
6356 C CG  . TYR B 346 ? 0.6437 1.0254 0.8709 0.0273  -0.0188 -0.1756 346 TYR B CG  
6357 C CD1 . TYR B 346 ? 0.5915 0.9793 0.8218 0.0076  0.0064  -0.1800 346 TYR B CD1 
6358 C CD2 . TYR B 346 ? 0.6549 1.0096 0.8631 0.0443  -0.0198 -0.1736 346 TYR B CD2 
6359 C CE1 . TYR B 346 ? 0.6670 1.0349 0.8753 0.0069  0.0295  -0.1813 346 TYR B CE1 
6360 C CE2 . TYR B 346 ? 0.6583 0.9944 0.8478 0.0426  0.0011  -0.1783 346 TYR B CE2 
6361 C CZ  . TYR B 346 ? 0.6554 0.9986 0.8421 0.0249  0.0254  -0.1816 346 TYR B CZ  
6362 O OH  . TYR B 346 ? 0.6808 1.0029 0.8397 0.0257  0.0464  -0.1855 346 TYR B OH  
6363 N N   . LYS B 347 ? 0.6283 1.0861 0.9422 0.0884  -0.0666 -0.1928 347 LYS B N   
6364 C CA  . LYS B 347 ? 0.6513 1.1012 0.9723 0.1128  -0.0632 -0.1961 347 LYS B CA  
6365 C C   . LYS B 347 ? 0.6944 1.0905 0.9693 0.1260  -0.0777 -0.1780 347 LYS B C   
6366 O O   . LYS B 347 ? 0.6845 1.0754 0.9478 0.1356  -0.1001 -0.1667 347 LYS B O   
6367 C CB  . LYS B 347 ? 0.5848 1.0874 0.9628 0.1361  -0.0750 -0.2103 347 LYS B CB  
6368 C CG  . LYS B 347 ? 0.6375 1.1283 1.0225 0.1651  -0.0716 -0.2136 347 LYS B CG  
6369 C CD  . LYS B 347 ? 0.6335 1.1528 1.0504 0.1981  -0.0988 -0.2157 347 LYS B CD  
6370 C CE  . LYS B 347 ? 0.6306 1.1646 1.0832 0.2248  -0.0878 -0.2286 347 LYS B CE  
6371 N NZ  . LYS B 347 ? 0.6413 1.1503 1.0833 0.2619  -0.1101 -0.2186 347 LYS B NZ  
6372 N N   . MET B 348 ? 0.6466 1.0014 0.8942 0.1258  -0.0641 -0.1757 348 MET B N   
6373 C CA  . MET B 348 ? 0.6785 0.9808 0.8911 0.1363  -0.0745 -0.1611 348 MET B CA  
6374 C C   . MET B 348 ? 0.7184 1.0167 0.9483 0.1684  -0.0823 -0.1641 348 MET B C   
6375 O O   . MET B 348 ? 0.7312 1.0584 0.9942 0.1814  -0.0730 -0.1805 348 MET B O   
6376 C CB  . MET B 348 ? 0.7100 0.9702 0.8889 0.1212  -0.0601 -0.1609 348 MET B CB  
6377 C CG  . MET B 348 ? 0.7185 0.9894 0.8872 0.0948  -0.0451 -0.1643 348 MET B CG  
6378 S SD  . MET B 348 ? 0.7983 1.0197 0.9232 0.0835  -0.0348 -0.1652 348 MET B SD  
6379 C CE  . MET B 348 ? 0.7120 0.9413 0.8189 0.0552  -0.0263 -0.1587 348 MET B CE  
6380 N N   . SER B 349 ? 0.7657 1.0258 0.9731 0.1820  -0.0975 -0.1470 349 SER B N   
6381 C CA  . SER B 349 ? 0.7487 0.9929 0.9660 0.2145  -0.1051 -0.1458 349 SER B CA  
6382 C C   . SER B 349 ? 0.7622 0.9730 0.9754 0.2193  -0.0894 -0.1574 349 SER B C   
6383 O O   . SER B 349 ? 0.7687 0.9763 1.0002 0.2471  -0.0904 -0.1640 349 SER B O   
6384 C CB  . SER B 349 ? 0.7709 0.9734 0.9586 0.2260  -0.1210 -0.1212 349 SER B CB  
6385 O OG  . SER B 349 ? 0.7936 1.0237 0.9769 0.2237  -0.1359 -0.1118 349 SER B OG  
6386 N N   . GLU B 350 ? 0.9163 1.1006 1.1041 0.1948  -0.0766 -0.1608 350 GLU B N   
6387 C CA  . GLU B 350 ? 0.9348 1.0787 1.1089 0.1980  -0.0655 -0.1726 350 GLU B CA  
6388 C C   . GLU B 350 ? 0.9532 1.0987 1.1077 0.1721  -0.0506 -0.1837 350 GLU B C   
6389 O O   . GLU B 350 ? 0.9462 1.1055 1.0903 0.1496  -0.0513 -0.1756 350 GLU B O   
6390 C CB  . GLU B 350 ? 0.9684 1.0501 1.1191 0.2002  -0.0747 -0.1584 350 GLU B CB  
6391 C CG  . GLU B 350 ? 0.9836 1.0366 1.1448 0.2315  -0.0788 -0.1582 350 GLU B CG  
6392 C CD  . GLU B 350 ? 1.0615 1.0476 1.2010 0.2279  -0.0833 -0.1443 350 GLU B CD  
6393 O OE1 . GLU B 350 ? 1.1360 1.1114 1.2612 0.2117  -0.0893 -0.1241 350 GLU B OE1 
6394 O OE2 . GLU B 350 ? 1.0940 1.0378 1.2326 0.2402  -0.0791 -0.1545 350 GLU B OE2 
6395 N N   . ASN B 351 ? 1.0761 1.2039 1.2215 0.1777  -0.0372 -0.2023 351 ASN B N   
6396 C CA  . ASN B 351 ? 1.1010 1.2186 1.2156 0.1574  -0.0251 -0.2124 351 ASN B CA  
6397 C C   . ASN B 351 ? 1.0811 1.1404 1.1659 0.1512  -0.0353 -0.2126 351 ASN B C   
6398 O O   . ASN B 351 ? 1.1395 1.1658 1.2170 0.1648  -0.0331 -0.2275 351 ASN B O   
6399 C CB  . ASN B 351 ? 1.0757 1.2128 1.1939 0.1675  -0.0021 -0.2340 351 ASN B CB  
6400 C CG  . ASN B 351 ? 1.1499 1.2541 1.2222 0.1573  0.0076  -0.2475 351 ASN B CG  
6401 O OD1 . ASN B 351 ? 1.2624 1.3222 1.3140 0.1653  0.0022  -0.2586 351 ASN B OD1 
6402 N ND2 . ASN B 351 ? 1.1087 1.2322 1.1627 0.1402  0.0209  -0.2467 351 ASN B ND2 
6403 N N   . ILE B 352 ? 0.7905 0.8373 0.8630 0.1311  -0.0470 -0.1966 352 ILE B N   
6404 C CA  . ILE B 352 ? 0.7809 0.7811 0.8314 0.1187  -0.0564 -0.1984 352 ILE B CA  
6405 C C   . ILE B 352 ? 0.7914 0.7945 0.8113 0.1034  -0.0510 -0.2109 352 ILE B C   
6406 O O   . ILE B 352 ? 0.7375 0.7649 0.7511 0.0877  -0.0499 -0.2001 352 ILE B O   
6407 C CB  . ILE B 352 ? 0.8270 0.8152 0.8837 0.1055  -0.0692 -0.1749 352 ILE B CB  
6408 C CG1 . ILE B 352 ? 0.7818 0.7642 0.8593 0.1240  -0.0735 -0.1599 352 ILE B CG1 
6409 C CG2 . ILE B 352 ? 0.8169 0.7623 0.8615 0.0904  -0.0783 -0.1793 352 ILE B CG2 
6410 C CD1 . ILE B 352 ? 0.8241 0.7793 0.9022 0.1144  -0.0817 -0.1378 352 ILE B CD1 
6411 N N   . PRO B 353 ? 0.9953 0.9708 0.9917 0.1087  -0.0485 -0.2331 353 PRO B N   
6412 C CA  . PRO B 353 ? 0.9911 0.9693 0.9493 0.0992  -0.0427 -0.2449 353 PRO B CA  
6413 C C   . PRO B 353 ? 0.9778 0.9446 0.9208 0.0779  -0.0593 -0.2365 353 PRO B C   
6414 O O   . PRO B 353 ? 0.9913 0.9775 0.9148 0.0675  -0.0550 -0.2302 353 PRO B O   
6415 C CB  . PRO B 353 ? 0.9994 0.9455 0.9339 0.1142  -0.0386 -0.2726 353 PRO B CB  
6416 C CG  . PRO B 353 ? 1.0177 0.9508 0.9852 0.1332  -0.0381 -0.2748 353 PRO B CG  
6417 C CD  . PRO B 353 ? 0.9914 0.9290 0.9912 0.1256  -0.0506 -0.2491 353 PRO B CD  
6418 N N   . ASN B 354 ? 0.9718 0.9077 0.9272 0.0712  -0.0770 -0.2353 354 ASN B N   
6419 C CA  . ASN B 354 ? 0.9736 0.9003 0.9244 0.0516  -0.0940 -0.2300 354 ASN B CA  
6420 C C   . ASN B 354 ? 0.9179 0.8704 0.8899 0.0391  -0.0946 -0.2024 354 ASN B C   
6421 O O   . ASN B 354 ? 0.9026 0.8490 0.8824 0.0240  -0.1073 -0.1949 354 ASN B O   
6422 C CB  . ASN B 354 ? 0.9991 0.8848 0.9660 0.0473  -0.1097 -0.2396 354 ASN B CB  
6423 C CG  . ASN B 354 ? 1.0679 0.9435 1.0729 0.0505  -0.1068 -0.2209 354 ASN B CG  
6424 O OD1 . ASN B 354 ? 1.0782 0.9502 1.0906 0.0690  -0.0968 -0.2214 354 ASN B OD1 
6425 N ND2 . ASN B 354 ? 1.0377 0.9094 1.0655 0.0345  -0.1144 -0.2031 354 ASN B ND2 
6426 N N   . GLU B 355 ? 0.8609 0.8437 0.8435 0.0454  -0.0814 -0.1895 355 GLU B N   
6427 C CA  . GLU B 355 ? 0.7962 0.8031 0.7933 0.0354  -0.0812 -0.1666 355 GLU B CA  
6428 C C   . GLU B 355 ? 0.7676 0.8076 0.7511 0.0334  -0.0682 -0.1653 355 GLU B C   
6429 O O   . GLU B 355 ? 0.7952 0.8532 0.7823 0.0444  -0.0548 -0.1723 355 GLU B O   
6430 C CB  . GLU B 355 ? 0.7650 0.7744 0.7893 0.0448  -0.0804 -0.1523 355 GLU B CB  
6431 C CG  . GLU B 355 ? 0.8517 0.8550 0.8888 0.0336  -0.0873 -0.1312 355 GLU B CG  
6432 C CD  . GLU B 355 ? 0.8343 0.8322 0.8879 0.0465  -0.0866 -0.1158 355 GLU B CD  
6433 O OE1 . GLU B 355 ? 0.7858 0.8089 0.8436 0.0601  -0.0826 -0.1146 355 GLU B OE1 
6434 O OE2 . GLU B 355 ? 0.8619 0.8301 0.9248 0.0434  -0.0899 -0.1047 355 GLU B OE2 
6435 N N   . VAL B 356 ? 0.5569 0.6044 0.5286 0.0193  -0.0710 -0.1561 356 VAL B N   
6436 C CA  . VAL B 356 ? 0.5598 0.6302 0.5157 0.0148  -0.0577 -0.1533 356 VAL B CA  
6437 C C   . VAL B 356 ? 0.5847 0.6777 0.5605 0.0066  -0.0561 -0.1355 356 VAL B C   
6438 O O   . VAL B 356 ? 0.5267 0.6130 0.5110 -0.0006 -0.0669 -0.1234 356 VAL B O   
6439 C CB  . VAL B 356 ? 0.5597 0.6162 0.4796 0.0084  -0.0621 -0.1572 356 VAL B CB  
6440 C CG1 . VAL B 356 ? 0.5413 0.6153 0.4469 0.0013  -0.0483 -0.1469 356 VAL B CG1 
6441 C CG2 . VAL B 356 ? 0.6002 0.6370 0.4902 0.0191  -0.0603 -0.1783 356 VAL B CG2 
6442 N N   . TYR B 357 ? 0.7416 0.8615 0.7269 0.0078  -0.0420 -0.1354 357 TYR B N   
6443 C CA  . TYR B 357 ? 0.7249 0.8665 0.7254 -0.0003 -0.0404 -0.1233 357 TYR B CA  
6444 C C   . TYR B 357 ? 0.7262 0.8774 0.7122 -0.0108 -0.0256 -0.1223 357 TYR B C   
6445 O O   . TYR B 357 ? 0.7693 0.9212 0.7414 -0.0087 -0.0108 -0.1313 357 TYR B O   
6446 C CB  . TYR B 357 ? 0.7299 0.8966 0.7610 0.0092  -0.0397 -0.1253 357 TYR B CB  
6447 C CG  . TYR B 357 ? 0.7468 0.8996 0.7876 0.0184  -0.0546 -0.1176 357 TYR B CG  
6448 C CD1 . TYR B 357 ? 0.7370 0.8700 0.7798 0.0312  -0.0586 -0.1241 357 TYR B CD1 
6449 C CD2 . TYR B 357 ? 0.6628 0.8168 0.7069 0.0145  -0.0626 -0.1030 357 TYR B CD2 
6450 C CE1 . TYR B 357 ? 0.7601 0.8735 0.8102 0.0392  -0.0692 -0.1145 357 TYR B CE1 
6451 C CE2 . TYR B 357 ? 0.7220 0.8582 0.7698 0.0232  -0.0721 -0.0928 357 TYR B CE2 
6452 C CZ  . TYR B 357 ? 0.7418 0.8568 0.7935 0.0351  -0.0750 -0.0976 357 TYR B CZ  
6453 O OH  . TYR B 357 ? 0.8068 0.8982 0.8614 0.0438  -0.0815 -0.0852 357 TYR B OH  
6454 N N   . ALA B 358 ? 0.6397 0.7963 0.6282 -0.0213 -0.0271 -0.1111 358 ALA B N   
6455 C CA  . ALA B 358 ? 0.6193 0.7789 0.5946 -0.0317 -0.0122 -0.1082 358 ALA B CA  
6456 C C   . ALA B 358 ? 0.6132 0.7926 0.6111 -0.0402 -0.0100 -0.1037 358 ALA B C   
6457 O O   . ALA B 358 ? 0.5808 0.7656 0.5928 -0.0379 -0.0232 -0.0993 358 ALA B O   
6458 C CB  . ALA B 358 ? 0.6157 0.7497 0.5583 -0.0355 -0.0172 -0.1001 358 ALA B CB  
6459 N N   . LEU B 359 ? 0.6159 0.8034 0.6150 -0.0498 0.0080  -0.1054 359 LEU B N   
6460 C CA  . LEU B 359 ? 0.5988 0.8002 0.6167 -0.0610 0.0112  -0.1040 359 LEU B CA  
6461 C C   . LEU B 359 ? 0.6591 0.8357 0.6502 -0.0702 0.0190  -0.0930 359 LEU B C   
6462 O O   . LEU B 359 ? 0.6546 0.8157 0.6223 -0.0722 0.0347  -0.0904 359 LEU B O   
6463 C CB  . LEU B 359 ? 0.5936 0.8247 0.6444 -0.0669 0.0270  -0.1165 359 LEU B CB  
6464 C CG  . LEU B 359 ? 0.5425 0.7850 0.6135 -0.0822 0.0324  -0.1188 359 LEU B CG  
6465 C CD1 . LEU B 359 ? 0.5675 0.8162 0.6452 -0.0784 0.0095  -0.1180 359 LEU B CD1 
6466 C CD2 . LEU B 359 ? 0.5390 0.8154 0.6528 -0.0901 0.0478  -0.1338 359 LEU B CD2 
6467 N N   . GLY B 360 ? 0.6738 0.8447 0.6650 -0.0735 0.0089  -0.0860 360 GLY B N   
6468 C CA  . GLY B 360 ? 0.6487 0.7945 0.6157 -0.0781 0.0127  -0.0745 360 GLY B CA  
6469 C C   . GLY B 360 ? 0.6881 0.8354 0.6670 -0.0881 0.0172  -0.0746 360 GLY B C   
6470 O O   . GLY B 360 ? 0.6620 0.8281 0.6625 -0.0889 0.0087  -0.0817 360 GLY B O   
6471 N N   . ALA B 361 ? 0.6575 0.7818 0.6185 -0.0944 0.0303  -0.0669 361 ALA B N   
6472 C CA  . ALA B 361 ? 0.6496 0.7665 0.6180 -0.1042 0.0366  -0.0673 361 ALA B CA  
6473 C C   . ALA B 361 ? 0.6819 0.7693 0.6244 -0.0990 0.0347  -0.0528 361 ALA B C   
6474 O O   . ALA B 361 ? 0.6877 0.7554 0.6035 -0.0926 0.0374  -0.0421 361 ALA B O   
6475 C CB  . ALA B 361 ? 0.7047 0.8205 0.6855 -0.1192 0.0598  -0.0736 361 ALA B CB  
6476 N N   . PHE B 362 ? 0.6548 0.7399 0.6040 -0.0996 0.0288  -0.0533 362 PHE B N   
6477 C CA  . PHE B 362 ? 0.6792 0.7390 0.6111 -0.0940 0.0290  -0.0413 362 PHE B CA  
6478 C C   . PHE B 362 ? 0.6747 0.7228 0.6135 -0.1028 0.0384  -0.0473 362 PHE B C   
6479 O O   . PHE B 362 ? 0.6436 0.7093 0.6005 -0.1087 0.0343  -0.0613 362 PHE B O   
6480 C CB  . PHE B 362 ? 0.6371 0.7044 0.5702 -0.0819 0.0120  -0.0351 362 PHE B CB  
6481 C CG  . PHE B 362 ? 0.6599 0.7068 0.5822 -0.0741 0.0120  -0.0235 362 PHE B CG  
6482 C CD1 . PHE B 362 ? 0.6840 0.7111 0.5858 -0.0678 0.0136  -0.0125 362 PHE B CD1 
6483 C CD2 . PHE B 362 ? 0.6251 0.6720 0.5553 -0.0709 0.0109  -0.0235 362 PHE B CD2 
6484 C CE1 . PHE B 362 ? 0.6838 0.6942 0.5786 -0.0576 0.0116  -0.0017 362 PHE B CE1 
6485 C CE2 . PHE B 362 ? 0.6555 0.6860 0.5805 -0.0618 0.0123  -0.0134 362 PHE B CE2 
6486 C CZ  . PHE B 362 ? 0.6888 0.7022 0.5987 -0.0549 0.0116  -0.0025 362 PHE B CZ  
6487 N N   . ASP B 363 ? 0.7057 0.7216 0.6277 -0.1022 0.0498  -0.0375 363 ASP B N   
6488 C CA  . ASP B 363 ? 0.7290 0.7242 0.6545 -0.1100 0.0606  -0.0431 363 ASP B CA  
6489 C C   . ASP B 363 ? 0.7674 0.7299 0.6708 -0.0974 0.0637  -0.0265 363 ASP B C   
6490 O O   . ASP B 363 ? 0.7772 0.7113 0.6612 -0.0962 0.0759  -0.0144 363 ASP B O   
6491 C CB  . ASP B 363 ? 0.7451 0.7316 0.6814 -0.1285 0.0799  -0.0515 363 ASP B CB  
6492 C CG  . ASP B 363 ? 0.8171 0.7793 0.7610 -0.1393 0.0908  -0.0608 363 ASP B CG  
6493 O OD1 . ASP B 363 ? 0.8220 0.7707 0.7568 -0.1299 0.0846  -0.0597 363 ASP B OD1 
6494 O OD2 . ASP B 363 ? 0.8347 0.7910 0.7961 -0.1578 0.1070  -0.0706 363 ASP B OD2 
6495 N N   . GLY B 364 ? 0.7169 0.6837 0.6228 -0.0860 0.0533  -0.0248 364 GLY B N   
6496 C CA  . GLY B 364 ? 0.6998 0.6424 0.5917 -0.0710 0.0540  -0.0097 364 GLY B CA  
6497 C C   . GLY B 364 ? 0.7284 0.6845 0.6314 -0.0592 0.0447  -0.0098 364 GLY B C   
6498 O O   . GLY B 364 ? 0.7111 0.6907 0.6262 -0.0625 0.0392  -0.0201 364 GLY B O   
6499 N N   . LEU B 365 ? 0.6679 0.6096 0.5663 -0.0435 0.0435  0.0032  365 LEU B N   
6500 C CA  . LEU B 365 ? 0.6761 0.6275 0.5885 -0.0311 0.0405  0.0045  365 LEU B CA  
6501 C C   . LEU B 365 ? 0.6852 0.6681 0.6147 -0.0228 0.0247  0.0118  365 LEU B C   
6502 O O   . LEU B 365 ? 0.6436 0.6272 0.5700 -0.0157 0.0143  0.0214  365 LEU B O   
6503 C CB  . LEU B 365 ? 0.7042 0.6248 0.6101 -0.0171 0.0488  0.0131  365 LEU B CB  
6504 C CG  . LEU B 365 ? 0.7402 0.6728 0.6644 -0.0030 0.0496  0.0136  365 LEU B CG  
6505 C CD1 . LEU B 365 ? 0.7182 0.6380 0.6371 -0.0085 0.0634  -0.0017 365 LEU B CD1 
6506 C CD2 . LEU B 365 ? 0.7462 0.6630 0.6732 0.0175  0.0489  0.0276  365 LEU B CD2 
6507 N N   . HIS B 366 ? 0.6762 0.6833 0.6220 -0.0242 0.0229  0.0065  366 HIS B N   
6508 C CA  . HIS B 366 ? 0.6437 0.6773 0.6134 -0.0174 0.0124  0.0133  366 HIS B CA  
6509 C C   . HIS B 366 ? 0.6663 0.7001 0.6539 -0.0020 0.0163  0.0211  366 HIS B C   
6510 O O   . HIS B 366 ? 0.6921 0.7106 0.6739 0.0030  0.0303  0.0183  366 HIS B O   
6511 C CB  . HIS B 366 ? 0.5906 0.6439 0.5679 -0.0241 0.0132  0.0075  366 HIS B CB  
6512 C CG  . HIS B 366 ? 0.5502 0.6273 0.5548 -0.0210 0.0053  0.0144  366 HIS B CG  
6513 N ND1 . HIS B 366 ? 0.5499 0.6390 0.5604 -0.0273 -0.0076 0.0136  366 HIS B ND1 
6514 C CD2 . HIS B 366 ? 0.5727 0.6630 0.6043 -0.0132 0.0100  0.0214  366 HIS B CD2 
6515 C CE1 . HIS B 366 ? 0.5490 0.6556 0.5895 -0.0250 -0.0116 0.0192  366 HIS B CE1 
6516 N NE2 . HIS B 366 ? 0.5312 0.6409 0.5873 -0.0170 -0.0004 0.0246  366 HIS B NE2 
6517 N N   . THR B 367 ? 0.6069 0.6588 0.6185 0.0063  0.0030  0.0291  367 THR B N   
6518 C CA  . THR B 367 ? 0.6123 0.6704 0.6493 0.0228  0.0041  0.0364  367 THR B CA  
6519 C C   . THR B 367 ? 0.5710 0.6654 0.6541 0.0253  -0.0029 0.0395  367 THR B C   
6520 O O   . THR B 367 ? 0.6079 0.7144 0.7217 0.0383  0.0016  0.0441  367 THR B O   
6521 C CB  . THR B 367 ? 0.6549 0.6966 0.6801 0.0359  -0.0076 0.0439  367 THR B CB  
6522 O OG1 . THR B 367 ? 0.6937 0.7466 0.7156 0.0327  -0.0286 0.0446  367 THR B OG1 
6523 C CG2 . THR B 367 ? 0.6926 0.6923 0.6766 0.0343  0.0049  0.0437  367 THR B CG2 
6524 N N   . VAL B 368 ? 0.5779 0.6895 0.6708 0.0132  -0.0121 0.0367  368 VAL B N   
6525 C CA  . VAL B 368 ? 0.5782 0.7216 0.7196 0.0124  -0.0193 0.0388  368 VAL B CA  
6526 C C   . VAL B 368 ? 0.5932 0.7452 0.7493 0.0069  0.0020  0.0406  368 VAL B C   
6527 O O   . VAL B 368 ? 0.5925 0.7338 0.7216 -0.0026 0.0088  0.0377  368 VAL B O   
6528 C CB  . VAL B 368 ? 0.5692 0.7209 0.7124 0.0031  -0.0413 0.0341  368 VAL B CB  
6529 C CG1 . VAL B 368 ? 0.4949 0.6775 0.6941 -0.0008 -0.0494 0.0338  368 VAL B CG1 
6530 C CG2 . VAL B 368 ? 0.5492 0.6887 0.6676 0.0115  -0.0601 0.0334  368 VAL B CG2 
6531 N N   . GLU B 369 ? 0.7724 0.9437 0.9702 0.0145  0.0135  0.0460  369 GLU B N   
6532 C CA  . GLU B 369 ? 0.7531 0.9290 0.9601 0.0129  0.0397  0.0504  369 GLU B CA  
6533 C C   . GLU B 369 ? 0.8065 0.9540 0.9581 0.0135  0.0547  0.0464  369 GLU B C   
6534 O O   . GLU B 369 ? 0.8074 0.9485 0.9369 0.0064  0.0628  0.0463  369 GLU B O   
6535 C CB  . GLU B 369 ? 0.7602 0.9499 0.9909 -0.0006 0.0395  0.0535  369 GLU B CB  
6536 C CG  . GLU B 369 ? 0.7466 0.9655 1.0382 -0.0045 0.0242  0.0537  369 GLU B CG  
6537 C CD  . GLU B 369 ? 0.7843 1.0061 1.0898 -0.0203 0.0201  0.0538  369 GLU B CD  
6538 O OE1 . GLU B 369 ? 0.8216 1.0335 1.1151 -0.0249 0.0421  0.0610  369 GLU B OE1 
6539 O OE2 . GLU B 369 ? 0.7428 0.9730 1.0657 -0.0267 -0.0054 0.0464  369 GLU B OE2 
6540 N N   . GLY B 370 ? 0.6578 0.7871 0.7877 0.0232  0.0572  0.0425  370 GLY B N   
6541 C CA  . GLY B 370 ? 0.6372 0.7389 0.7184 0.0227  0.0679  0.0345  370 GLY B CA  
6542 C C   . GLY B 370 ? 0.6738 0.7524 0.7273 0.0205  0.0555  0.0281  370 GLY B C   
6543 O O   . GLY B 370 ? 0.6284 0.7095 0.6816 0.0135  0.0376  0.0288  370 GLY B O   
6544 N N   . ARG B 371 ? 0.7206 0.7736 0.7499 0.0268  0.0673  0.0216  371 ARG B N   
6545 C CA  . ARG B 371 ? 0.7379 0.7617 0.7401 0.0234  0.0623  0.0157  371 ARG B CA  
6546 C C   . ARG B 371 ? 0.7468 0.7546 0.7152 0.0118  0.0676  0.0012  371 ARG B C   
6547 O O   . ARG B 371 ? 0.7143 0.7118 0.6684 0.0168  0.0813  -0.0071 371 ARG B O   
6548 C CB  . ARG B 371 ? 0.7660 0.7687 0.7710 0.0395  0.0713  0.0182  371 ARG B CB  
6549 C CG  . ARG B 371 ? 0.8028 0.7701 0.7826 0.0372  0.0686  0.0165  371 ARG B CG  
6550 C CD  . ARG B 371 ? 0.9003 0.8403 0.8800 0.0552  0.0806  0.0186  371 ARG B CD  
6551 N NE  . ARG B 371 ? 0.9789 0.8738 0.9278 0.0492  0.0873  0.0123  371 ARG B NE  
6552 C CZ  . ARG B 371 ? 0.9820 0.8477 0.9226 0.0583  0.0859  0.0226  371 ARG B CZ  
6553 N NH1 . ARG B 371 ? 0.9493 0.8281 0.9075 0.0762  0.0742  0.0384  371 ARG B NH1 
6554 N NH2 . ARG B 371 ? 1.0770 0.8986 0.9914 0.0495  0.0960  0.0169  371 ARG B NH2 
6555 N N   . TYR B 372 ? 0.6749 0.6819 0.6311 -0.0026 0.0563  -0.0036 372 TYR B N   
6556 C CA  . TYR B 372 ? 0.6695 0.6670 0.6014 -0.0135 0.0582  -0.0196 372 TYR B CA  
6557 C C   . TYR B 372 ? 0.6557 0.6494 0.5823 -0.0283 0.0490  -0.0242 372 TYR B C   
6558 O O   . TYR B 372 ? 0.6012 0.6098 0.5378 -0.0312 0.0389  -0.0159 372 TYR B O   
6559 C CB  . TYR B 372 ? 0.6214 0.6393 0.5483 -0.0136 0.0572  -0.0223 372 TYR B CB  
6560 C CG  . TYR B 372 ? 0.5950 0.6392 0.5427 -0.0135 0.0496  -0.0092 372 TYR B CG  
6561 C CD1 . TYR B 372 ? 0.5611 0.6175 0.5095 -0.0237 0.0360  -0.0106 372 TYR B CD1 
6562 C CD2 . TYR B 372 ? 0.5662 0.6230 0.5357 -0.0035 0.0578  0.0032  372 TYR B CD2 
6563 C CE1 . TYR B 372 ? 0.5479 0.6233 0.5153 -0.0238 0.0296  -0.0003 372 TYR B CE1 
6564 C CE2 . TYR B 372 ? 0.5418 0.6199 0.5348 -0.0059 0.0520  0.0135  372 TYR B CE2 
6565 C CZ  . TYR B 372 ? 0.5579 0.6428 0.5480 -0.0159 0.0375  0.0115  372 TYR B CZ  
6566 O OH  . TYR B 372 ? 0.5432 0.6442 0.5572 -0.0182 0.0328  0.0206  372 TYR B OH  
6567 N N   . TYR B 373 ? 0.7013 0.6758 0.6138 -0.0381 0.0535  -0.0391 373 TYR B N   
6568 C CA  . TYR B 373 ? 0.7214 0.6923 0.6339 -0.0533 0.0500  -0.0437 373 TYR B CA  
6569 C C   . TYR B 373 ? 0.7010 0.6997 0.6171 -0.0626 0.0393  -0.0534 373 TYR B C   
6570 O O   . TYR B 373 ? 0.6728 0.6806 0.5823 -0.0624 0.0360  -0.0658 373 TYR B O   
6571 C CB  . TYR B 373 ? 0.7638 0.7020 0.6684 -0.0625 0.0612  -0.0560 373 TYR B CB  
6572 C CG  . TYR B 373 ? 0.7550 0.6809 0.6617 -0.0749 0.0654  -0.0520 373 TYR B CG  
6573 C CD1 . TYR B 373 ? 0.7557 0.6997 0.6717 -0.0912 0.0618  -0.0630 373 TYR B CD1 
6574 C CD2 . TYR B 373 ? 0.7860 0.6825 0.6844 -0.0683 0.0740  -0.0360 373 TYR B CD2 
6575 C CE1 . TYR B 373 ? 0.7768 0.7098 0.6949 -0.1025 0.0705  -0.0585 373 TYR B CE1 
6576 C CE2 . TYR B 373 ? 0.7873 0.6684 0.6803 -0.0782 0.0814  -0.0297 373 TYR B CE2 
6577 C CZ  . TYR B 373 ? 0.7863 0.6860 0.6898 -0.0962 0.0815  -0.0411 373 TYR B CZ  
6578 O OH  . TYR B 373 ? 0.7796 0.6648 0.6783 -0.1061 0.0935  -0.0345 373 TYR B OH  
6579 N N   . LEU B 374 ? 0.6748 0.6855 0.5987 -0.0692 0.0336  -0.0483 374 LEU B N   
6580 C CA  . LEU B 374 ? 0.6281 0.6661 0.5591 -0.0748 0.0231  -0.0552 374 LEU B CA  
6581 C C   . LEU B 374 ? 0.6568 0.6954 0.5954 -0.0896 0.0261  -0.0637 374 LEU B C   
6582 O O   . LEU B 374 ? 0.6471 0.6671 0.5823 -0.0932 0.0355  -0.0558 374 LEU B O   
6583 C CB  . LEU B 374 ? 0.5923 0.6479 0.5298 -0.0669 0.0142  -0.0416 374 LEU B CB  
6584 C CG  . LEU B 374 ? 0.6019 0.6602 0.5418 -0.0541 0.0139  -0.0302 374 LEU B CG  
6585 C CD1 . LEU B 374 ? 0.5226 0.5949 0.4759 -0.0505 0.0050  -0.0188 374 LEU B CD1 
6586 C CD2 . LEU B 374 ? 0.5738 0.6390 0.5050 -0.0495 0.0147  -0.0365 374 LEU B CD2 
6587 N N   . GLN B 375 ? 0.7103 0.7711 0.6592 -0.0967 0.0189  -0.0791 375 GLN B N   
6588 C CA  . GLN B 375 ? 0.6884 0.7633 0.6540 -0.1088 0.0205  -0.0868 375 GLN B CA  
6589 C C   . GLN B 375 ? 0.6511 0.7578 0.6249 -0.1023 0.0057  -0.0890 375 GLN B C   
6590 O O   . GLN B 375 ? 0.6205 0.7423 0.5941 -0.0976 -0.0058 -0.0987 375 GLN B O   
6591 C CB  . GLN B 375 ? 0.6495 0.7226 0.6305 -0.1251 0.0263  -0.1071 375 GLN B CB  
6592 C CG  . GLN B 375 ? 0.7289 0.7664 0.7067 -0.1354 0.0462  -0.1031 375 GLN B CG  
6593 C CD  . GLN B 375 ? 0.7557 0.7918 0.7573 -0.1556 0.0535  -0.1250 375 GLN B CD  
6594 O OE1 . GLN B 375 ? 0.7246 0.7904 0.7459 -0.1607 0.0403  -0.1453 375 GLN B OE1 
6595 N NE2 . GLN B 375 ? 0.8077 0.8083 0.8087 -0.1668 0.0741  -0.1213 375 GLN B NE2 
6596 N N   . ILE B 376 ? 0.5959 0.7095 0.5726 -0.0997 0.0055  -0.0797 376 ILE B N   
6597 C CA  . ILE B 376 ? 0.5593 0.6957 0.5418 -0.0910 -0.0073 -0.0790 376 ILE B CA  
6598 C C   . ILE B 376 ? 0.5797 0.7322 0.5785 -0.0965 -0.0042 -0.0854 376 ILE B C   
6599 O O   . ILE B 376 ? 0.5807 0.7206 0.5744 -0.1011 0.0079  -0.0796 376 ILE B O   
6600 C CB  . ILE B 376 ? 0.5223 0.6503 0.4936 -0.0795 -0.0120 -0.0622 376 ILE B CB  
6601 C CG1 . ILE B 376 ? 0.5280 0.6435 0.4882 -0.0733 -0.0113 -0.0557 376 ILE B CG1 
6602 C CG2 . ILE B 376 ? 0.4942 0.6396 0.4727 -0.0718 -0.0230 -0.0618 376 ILE B CG2 
6603 C CD1 . ILE B 376 ? 0.5042 0.6151 0.4636 -0.0641 -0.0139 -0.0401 376 ILE B CD1 
6604 N N   . CYS B 377 ? 0.6207 0.8005 0.6368 -0.0937 -0.0145 -0.0967 377 CYS B N   
6605 C CA  . CYS B 377 ? 0.6332 0.8330 0.6679 -0.0937 -0.0129 -0.1025 377 CYS B CA  
6606 C C   . CYS B 377 ? 0.6504 0.8576 0.6809 -0.0779 -0.0270 -0.0964 377 CYS B C   
6607 O O   . CYS B 377 ? 0.6064 0.8228 0.6359 -0.0688 -0.0406 -0.0980 377 CYS B O   
6608 C CB  . CYS B 377 ? 0.6231 0.8521 0.6903 -0.1023 -0.0137 -0.1224 377 CYS B CB  
6609 S SG  . CYS B 377 ? 0.6726 0.8915 0.7547 -0.1252 0.0074  -0.1314 377 CYS B SG  
6610 N N   . THR B 378 ? 0.5612 0.7610 0.5862 -0.0736 -0.0236 -0.0896 378 THR B N   
6611 C CA  . THR B 378 ? 0.5781 0.7765 0.5989 -0.0601 -0.0357 -0.0829 378 THR B CA  
6612 C C   . THR B 378 ? 0.5859 0.7920 0.6158 -0.0549 -0.0340 -0.0883 378 THR B C   
6613 O O   . THR B 378 ? 0.6020 0.7982 0.6234 -0.0592 -0.0235 -0.0882 378 THR B O   
6614 C CB  . THR B 378 ? 0.5503 0.7241 0.5524 -0.0580 -0.0372 -0.0681 378 THR B CB  
6615 O OG1 . THR B 378 ? 0.5582 0.7288 0.5609 -0.0473 -0.0471 -0.0614 378 THR B OG1 
6616 C CG2 . THR B 378 ? 0.5700 0.7289 0.5613 -0.0619 -0.0302 -0.0649 378 THR B CG2 
6617 N N   . LEU B 379 ? 0.5315 0.7530 0.5750 -0.0433 -0.0443 -0.0928 379 LEU B N   
6618 C CA  . LEU B 379 ? 0.5366 0.7574 0.5847 -0.0336 -0.0450 -0.0955 379 LEU B CA  
6619 C C   . LEU B 379 ? 0.5476 0.7434 0.5809 -0.0262 -0.0540 -0.0831 379 LEU B C   
6620 O O   . LEU B 379 ? 0.5221 0.7139 0.5520 -0.0207 -0.0622 -0.0745 379 LEU B O   
6621 C CB  . LEU B 379 ? 0.5074 0.7567 0.5814 -0.0226 -0.0514 -0.1066 379 LEU B CB  
6622 C CG  . LEU B 379 ? 0.5382 0.7803 0.6144 -0.0057 -0.0582 -0.1057 379 LEU B CG  
6623 C CD1 . LEU B 379 ? 0.5596 0.7903 0.6304 -0.0076 -0.0460 -0.1112 379 LEU B CD1 
6624 C CD2 . LEU B 379 ? 0.5284 0.8001 0.6311 0.0091  -0.0675 -0.1150 379 LEU B CD2 
6625 N N   . LEU B 380 ? 0.5730 0.7507 0.5966 -0.0269 -0.0515 -0.0824 380 LEU B N   
6626 C CA  . LEU B 380 ? 0.5818 0.7367 0.5993 -0.0238 -0.0595 -0.0726 380 LEU B CA  
6627 C C   . LEU B 380 ? 0.6070 0.7477 0.6229 -0.0186 -0.0619 -0.0797 380 LEU B C   
6628 O O   . LEU B 380 ? 0.6205 0.7639 0.6294 -0.0190 -0.0553 -0.0904 380 LEU B O   
6629 C CB  . LEU B 380 ? 0.5824 0.7252 0.5895 -0.0336 -0.0587 -0.0630 380 LEU B CB  
6630 C CG  . LEU B 380 ? 0.6164 0.7548 0.6092 -0.0418 -0.0527 -0.0652 380 LEU B CG  
6631 C CD1 . LEU B 380 ? 0.5675 0.6931 0.5495 -0.0393 -0.0561 -0.0722 380 LEU B CD1 
6632 C CD2 . LEU B 380 ? 0.5700 0.7005 0.5592 -0.0470 -0.0539 -0.0540 380 LEU B CD2 
6633 N N   . LYS B 381 ? 0.5423 0.6650 0.5635 -0.0138 -0.0696 -0.0737 381 LYS B N   
6634 C CA  . LYS B 381 ? 0.5550 0.6576 0.5759 -0.0104 -0.0741 -0.0814 381 LYS B CA  
6635 C C   . LYS B 381 ? 0.5744 0.6643 0.5866 -0.0209 -0.0787 -0.0819 381 LYS B C   
6636 O O   . LYS B 381 ? 0.5047 0.5913 0.5242 -0.0279 -0.0816 -0.0705 381 LYS B O   
6637 C CB  . LYS B 381 ? 0.5482 0.6332 0.5818 -0.0022 -0.0791 -0.0739 381 LYS B CB  
6638 C CG  . LYS B 381 ? 0.5809 0.6398 0.6183 0.0009  -0.0841 -0.0835 381 LYS B CG  
6639 C CD  . LYS B 381 ? 0.6341 0.6713 0.6824 -0.0098 -0.0893 -0.0759 381 LYS B CD  
6640 C CE  . LYS B 381 ? 0.6334 0.6469 0.6848 -0.0120 -0.0973 -0.0920 381 LYS B CE  
6641 N NZ  . LYS B 381 ? 0.7179 0.7094 0.7764 0.0006  -0.0962 -0.0955 381 LYS B NZ  
6642 N N   . CYS B 382 ? 0.6755 0.7608 0.5987 -0.1010 0.0141  -0.1275 382 CYS B N   
6643 C CA  . CYS B 382 ? 0.6851 0.7593 0.5949 -0.1046 0.0228  -0.1178 382 CYS B CA  
6644 C C   . CYS B 382 ? 0.6735 0.7290 0.5566 -0.1035 0.0109  -0.1115 382 CYS B C   
6645 O O   . CYS B 382 ? 0.7190 0.7651 0.5926 -0.0961 -0.0004 -0.1142 382 CYS B O   
6646 C CB  . CYS B 382 ? 0.7223 0.8019 0.6394 -0.1001 0.0360  -0.1155 382 CYS B CB  
6647 S SG  . CYS B 382 ? 0.7945 0.8956 0.7495 -0.1059 0.0515  -0.1186 382 CYS B SG  
6648 N N   . LYS B 383 ? 0.6266 0.6766 0.5010 -0.1109 0.0129  -0.1028 383 LYS B N   
6649 C CA  . LYS B 383 ? 0.6295 0.6647 0.4856 -0.1151 0.0012  -0.0950 383 LYS B CA  
6650 C C   . LYS B 383 ? 0.6968 0.7139 0.5397 -0.1088 -0.0091 -0.0966 383 LYS B C   
6651 O O   . LYS B 383 ? 0.6984 0.6977 0.5288 -0.1073 -0.0229 -0.0960 383 LYS B O   
6652 C CB  . LYS B 383 ? 0.6070 0.6474 0.4650 -0.1238 0.0064  -0.0852 383 LYS B CB  
6653 C CG  . LYS B 383 ? 0.6124 0.6417 0.4593 -0.1323 -0.0050 -0.0749 383 LYS B CG  
6654 C CD  . LYS B 383 ? 0.6467 0.6924 0.5044 -0.1409 0.0023  -0.0649 383 LYS B CD  
6655 C CE  . LYS B 383 ? 0.7394 0.7844 0.6022 -0.1443 -0.0037 -0.0597 383 LYS B CE  
6656 N NZ  . LYS B 383 ? 0.7985 0.8658 0.6795 -0.1438 0.0070  -0.0551 383 LYS B NZ  
6657 N N   . THR B 384 ? 0.6601 0.6778 0.5016 -0.1038 -0.0031 -0.0987 384 THR B N   
6658 C CA  . THR B 384 ? 0.6812 0.6822 0.5058 -0.0937 -0.0106 -0.1048 384 THR B CA  
6659 C C   . THR B 384 ? 0.6890 0.7053 0.5208 -0.0813 0.0042  -0.1121 384 THR B C   
6660 O O   . THR B 384 ? 0.6960 0.7334 0.5503 -0.0834 0.0169  -0.1120 384 THR B O   
6661 C CB  . THR B 384 ? 0.7133 0.7013 0.5228 -0.0988 -0.0186 -0.0999 384 THR B CB  
6662 O OG1 . THR B 384 ? 0.6903 0.6911 0.4999 -0.0954 -0.0061 -0.0976 384 THR B OG1 
6663 C CG2 . THR B 384 ? 0.6634 0.6534 0.4813 -0.1151 -0.0247 -0.0884 384 THR B CG2 
6664 N N   . THR B 385 ? 0.7022 0.7076 0.5150 -0.0686 0.0026  -0.1190 385 THR B N   
6665 C CA  . THR B 385 ? 0.7304 0.7542 0.5485 -0.0560 0.0204  -0.1240 385 THR B CA  
6666 C C   . THR B 385 ? 0.7189 0.7543 0.5360 -0.0602 0.0371  -0.1141 385 THR B C   
6667 O O   . THR B 385 ? 0.7269 0.7823 0.5560 -0.0554 0.0565  -0.1126 385 THR B O   
6668 C CB  . THR B 385 ? 0.7539 0.7618 0.5460 -0.0373 0.0150  -0.1360 385 THR B CB  
6669 O OG1 . THR B 385 ? 0.8008 0.7876 0.5610 -0.0384 0.0069  -0.1347 385 THR B OG1 
6670 C CG2 . THR B 385 ? 0.7713 0.7578 0.5605 -0.0313 -0.0049 -0.1445 385 THR B CG2 
6671 N N   . ASN B 386 ? 0.7061 0.7309 0.5123 -0.0695 0.0300  -0.1057 386 ASN B N   
6672 C CA  . ASN B 386 ? 0.7070 0.7390 0.5115 -0.0721 0.0426  -0.0942 386 ASN B CA  
6673 C C   . ASN B 386 ? 0.7130 0.7615 0.5509 -0.0818 0.0565  -0.0875 386 ASN B C   
6674 O O   . ASN B 386 ? 0.6810 0.7302 0.5349 -0.0911 0.0499  -0.0876 386 ASN B O   
6675 C CB  . ASN B 386 ? 0.7039 0.7231 0.4932 -0.0777 0.0272  -0.0880 386 ASN B CB  
6676 C CG  . ASN B 386 ? 0.7694 0.7917 0.5479 -0.0748 0.0360  -0.0760 386 ASN B CG  
6677 O OD1 . ASN B 386 ? 0.7474 0.7804 0.5418 -0.0762 0.0543  -0.0674 386 ASN B OD1 
6678 N ND2 . ASN B 386 ? 0.7535 0.7641 0.5041 -0.0708 0.0211  -0.0751 386 ASN B ND2 
6679 N N   . LEU B 387 ? 0.7254 0.7858 0.5726 -0.0799 0.0762  -0.0816 387 LEU B N   
6680 C CA  . LEU B 387 ? 0.7358 0.8052 0.6154 -0.0909 0.0870  -0.0761 387 LEU B CA  
6681 C C   . LEU B 387 ? 0.7295 0.7880 0.6091 -0.0972 0.0817  -0.0680 387 LEU B C   
6682 O O   . LEU B 387 ? 0.7086 0.7685 0.6123 -0.1050 0.0863  -0.0676 387 LEU B O   
6683 C CB  . LEU B 387 ? 0.7252 0.8063 0.6163 -0.0909 0.1096  -0.0671 387 LEU B CB  
6684 C CG  . LEU B 387 ? 0.7215 0.8232 0.6216 -0.0834 0.1189  -0.0750 387 LEU B CG  
6685 C CD1 . LEU B 387 ? 0.7188 0.8399 0.6492 -0.0906 0.1427  -0.0649 387 LEU B CD1 
6686 C CD2 . LEU B 387 ? 0.7453 0.8546 0.6638 -0.0831 0.1040  -0.0912 387 LEU B CD2 
6687 N N   . ASN B 388 ? 0.7326 0.7812 0.5874 -0.0928 0.0711  -0.0630 388 ASN B N   
6688 C CA  . ASN B 388 ? 0.7238 0.7685 0.5835 -0.0962 0.0642  -0.0562 388 ASN B CA  
6689 C C   . ASN B 388 ? 0.7035 0.7533 0.5813 -0.1035 0.0576  -0.0637 388 ASN B C   
6690 O O   . ASN B 388 ? 0.6732 0.7251 0.5624 -0.1053 0.0574  -0.0596 388 ASN B O   
6691 C CB  . ASN B 388 ? 0.7047 0.7439 0.5403 -0.0920 0.0481  -0.0529 388 ASN B CB  
6692 C CG  . ASN B 388 ? 0.7816 0.8147 0.5943 -0.0834 0.0516  -0.0425 388 ASN B CG  
6693 O OD1 . ASN B 388 ? 0.7776 0.8046 0.5631 -0.0778 0.0375  -0.0430 388 ASN B OD1 
6694 N ND2 . ASN B 388 ? 0.8703 0.9024 0.6911 -0.0824 0.0696  -0.0322 388 ASN B ND2 
6695 N N   . THR B 389 ? 0.7263 0.7781 0.6035 -0.1055 0.0514  -0.0739 389 THR B N   
6696 C CA  . THR B 389 ? 0.7372 0.7921 0.6214 -0.1115 0.0437  -0.0788 389 THR B CA  
6697 C C   . THR B 389 ? 0.7267 0.7873 0.6261 -0.1139 0.0481  -0.0882 389 THR B C   
6698 O O   . THR B 389 ? 0.7458 0.8082 0.6440 -0.1170 0.0413  -0.0926 389 THR B O   
6699 C CB  . THR B 389 ? 0.7161 0.7633 0.5835 -0.1123 0.0281  -0.0807 389 THR B CB  
6700 O OG1 . THR B 389 ? 0.7236 0.7657 0.5832 -0.1055 0.0265  -0.0886 389 THR B OG1 
6701 C CG2 . THR B 389 ? 0.6833 0.7253 0.5387 -0.1126 0.0188  -0.0735 389 THR B CG2 
6702 N N   . CYS B 390 ? 0.7474 0.8121 0.6612 -0.1133 0.0586  -0.0907 390 CYS B N   
6703 C CA  . CYS B 390 ? 0.7661 0.8379 0.7001 -0.1178 0.0597  -0.1009 390 CYS B CA  
6704 C C   . CYS B 390 ? 0.7140 0.7809 0.6546 -0.1217 0.0619  -0.1028 390 CYS B C   
6705 O O   . CYS B 390 ? 0.7000 0.7599 0.6491 -0.1221 0.0712  -0.0969 390 CYS B O   
6706 C CB  . CYS B 390 ? 0.7380 0.8187 0.6941 -0.1195 0.0707  -0.1017 390 CYS B CB  
6707 S SG  . CYS B 390 ? 0.7951 0.8874 0.7454 -0.1100 0.0717  -0.1029 390 CYS B SG  
6708 N N   . GLY B 391 ? 0.7302 0.7991 0.6642 -0.1226 0.0537  -0.1108 391 GLY B N   
6709 C CA  . GLY B 391 ? 0.7072 0.7729 0.6408 -0.1224 0.0566  -0.1149 391 GLY B CA  
6710 C C   . GLY B 391 ? 0.6810 0.7515 0.5976 -0.1203 0.0544  -0.1083 391 GLY B C   
6711 O O   . GLY B 391 ? 0.6955 0.7688 0.6081 -0.1181 0.0575  -0.1134 391 GLY B O   
6712 N N   . ASP B 392 ? 0.6634 0.7354 0.5712 -0.1210 0.0495  -0.0974 392 ASP B N   
6713 C CA  . ASP B 392 ? 0.6624 0.7408 0.5595 -0.1234 0.0459  -0.0892 392 ASP B CA  
6714 C C   . ASP B 392 ? 0.6826 0.7613 0.5641 -0.1259 0.0393  -0.0929 392 ASP B C   
6715 O O   . ASP B 392 ? 0.6580 0.7307 0.5352 -0.1248 0.0318  -0.1002 392 ASP B O   
6716 C CB  . ASP B 392 ? 0.6522 0.7270 0.5446 -0.1259 0.0378  -0.0789 392 ASP B CB  
6717 C CG  . ASP B 392 ? 0.7287 0.8055 0.6305 -0.1224 0.0418  -0.0723 392 ASP B CG  
6718 O OD1 . ASP B 392 ? 0.7668 0.8461 0.6805 -0.1177 0.0518  -0.0738 392 ASP B OD1 
6719 O OD2 . ASP B 392 ? 0.7568 0.8295 0.6518 -0.1232 0.0331  -0.0661 392 ASP B OD2 
6720 N N   . SER B 393 ? 0.7047 0.7924 0.5779 -0.1285 0.0423  -0.0859 393 SER B N   
6721 C CA  . SER B 393 ? 0.6947 0.7806 0.5464 -0.1310 0.0365  -0.0841 393 SER B CA  
6722 C C   . SER B 393 ? 0.6957 0.7661 0.5389 -0.1344 0.0216  -0.0785 393 SER B C   
6723 O O   . SER B 393 ? 0.7035 0.7681 0.5519 -0.1389 0.0170  -0.0699 393 SER B O   
6724 C CB  . SER B 393 ? 0.6887 0.7897 0.5344 -0.1352 0.0455  -0.0719 393 SER B CB  
6725 O OG  . SER B 393 ? 0.7826 0.8983 0.6385 -0.1281 0.0600  -0.0786 393 SER B OG  
6726 N N   . ALA B 394 ? 0.7221 0.7844 0.5520 -0.1304 0.0121  -0.0851 394 ALA B N   
6727 C CA  . ALA B 394 ? 0.7482 0.7935 0.5690 -0.1292 -0.0031 -0.0817 394 ALA B CA  
6728 C C   . ALA B 394 ? 0.7433 0.7822 0.5385 -0.1285 -0.0115 -0.0764 394 ALA B C   
6729 O O   . ALA B 394 ? 0.8184 0.8642 0.6067 -0.1225 -0.0137 -0.0872 394 ALA B O   
6730 C CB  . ALA B 394 ? 0.7173 0.7621 0.5528 -0.1206 -0.0076 -0.0953 394 ALA B CB  
6731 N N   . GLU B 395 ? 0.7719 0.7960 0.5519 -0.1355 -0.0175 -0.0593 395 GLU B N   
6732 C CA  . GLU B 395 ? 0.8182 0.8335 0.5686 -0.1362 -0.0235 -0.0479 395 GLU B CA  
6733 C C   . GLU B 395 ? 0.8477 0.8398 0.5857 -0.1270 -0.0443 -0.0489 395 GLU B C   
6734 O O   . GLU B 395 ? 0.8645 0.8499 0.5757 -0.1229 -0.0525 -0.0428 395 GLU B O   
6735 C CB  . GLU B 395 ? 0.8225 0.8334 0.5655 -0.1511 -0.0177 -0.0245 395 GLU B CB  
6736 C CG  . GLU B 395 ? 0.8220 0.8614 0.5814 -0.1581 0.0026  -0.0219 395 GLU B CG  
6737 C CD  . GLU B 395 ? 0.9789 1.0292 0.7219 -0.1678 0.0147  -0.0011 395 GLU B CD  
6738 O OE1 . GLU B 395 ? 1.0765 1.1233 0.7861 -0.1625 0.0146  0.0025  395 GLU B OE1 
6739 O OE2 . GLU B 395 ? 1.0355 1.0992 0.7991 -0.1809 0.0237  0.0127  395 GLU B OE2 
6740 N N   . THR B 396 ? 0.7948 0.7746 0.5492 -0.1215 -0.0531 -0.0564 396 THR B N   
6741 C CA  . THR B 396 ? 0.8499 0.8067 0.5954 -0.1097 -0.0729 -0.0572 396 THR B CA  
6742 C C   . THR B 396 ? 0.8524 0.8197 0.6234 -0.0961 -0.0751 -0.0772 396 THR B C   
6743 O O   . THR B 396 ? 0.8370 0.8171 0.6280 -0.0987 -0.0627 -0.0851 396 THR B O   
6744 C CB  . THR B 396 ? 0.8402 0.7607 0.5742 -0.1159 -0.0833 -0.0417 396 THR B CB  
6745 O OG1 . THR B 396 ? 0.8554 0.7750 0.6079 -0.1213 -0.0777 -0.0473 396 THR B OG1 
6746 C CG2 . THR B 396 ? 0.8641 0.7760 0.5762 -0.1320 -0.0795 -0.0173 396 THR B CG2 
6747 N N   . ALA B 397 ? 0.7957 0.7579 0.5659 -0.0807 -0.0909 -0.0832 397 ALA B N   
6748 C CA  . ALA B 397 ? 0.7971 0.7738 0.5948 -0.0659 -0.0925 -0.1005 397 ALA B CA  
6749 C C   . ALA B 397 ? 0.8566 0.8149 0.6472 -0.0477 -0.1143 -0.1004 397 ALA B C   
6750 O O   . ALA B 397 ? 0.9075 0.8451 0.6712 -0.0471 -0.1286 -0.0874 397 ALA B O   
6751 C CB  . ALA B 397 ? 0.7720 0.7871 0.5958 -0.0663 -0.0840 -0.1147 397 ALA B CB  
6752 N N   . SER B 398 ? 0.7794 0.7460 0.5933 -0.0312 -0.1158 -0.1140 398 SER B N   
6753 C CA  . SER B 398 ? 0.8403 0.7929 0.6535 -0.0090 -0.1363 -0.1166 398 SER B CA  
6754 C C   . SER B 398 ? 0.8300 0.8254 0.6803 0.0064  -0.1395 -0.1323 398 SER B C   
6755 O O   . SER B 398 ? 0.8558 0.8482 0.7080 0.0253  -0.1602 -0.1333 398 SER B O   
6756 C CB  . SER B 398 ? 0.8789 0.7994 0.6865 0.0028  -0.1386 -0.1202 398 SER B CB  
6757 O OG  . SER B 398 ? 0.8912 0.7821 0.6761 -0.0162 -0.1329 -0.1094 398 SER B OG  
6758 N N   . THR B 399 ? 0.7224 0.7577 0.6045 -0.0019 -0.1211 -0.1429 399 THR B N   
6759 C CA  . THR B 399 ? 0.7210 0.8017 0.6484 0.0091  -0.1220 -0.1573 399 THR B CA  
6760 C C   . THR B 399 ? 0.7240 0.8216 0.6533 0.0042  -0.1386 -0.1584 399 THR B C   
6761 O O   . THR B 399 ? 0.6983 0.8036 0.6227 -0.0147 -0.1311 -0.1585 399 THR B O   
6762 C CB  . THR B 399 ? 0.6971 0.8100 0.6574 -0.0009 -0.0954 -0.1649 399 THR B CB  
6763 O OG1 . THR B 399 ? 0.7468 0.8420 0.6962 0.0061  -0.0818 -0.1644 399 THR B OG1 
6764 C CG2 . THR B 399 ? 0.7052 0.8698 0.7205 0.0065  -0.0944 -0.1776 399 THR B CG2 
6765 N N   . ARG B 400 ? 1.0465 1.1484 0.9812 0.0232  -0.1627 -0.1606 400 ARG B N   
6766 C CA  . ARG B 400 ? 1.0435 1.1721 0.9893 0.0213  -0.1805 -0.1670 400 ARG B CA  
6767 C C   . ARG B 400 ? 1.0325 1.2174 1.0441 0.0216  -0.1749 -0.1843 400 ARG B C   
6768 O O   . ARG B 400 ? 1.0430 1.2472 1.0894 0.0298  -0.1589 -0.1891 400 ARG B O   
6769 C CB  . ARG B 400 ? 1.0862 1.2022 1.0152 0.0425  -0.2118 -0.1622 400 ARG B CB  
6770 C CG  . ARG B 400 ? 1.1253 1.1955 0.9949 0.0452  -0.2290 -0.1441 400 ARG B CG  
6771 C CD  . ARG B 400 ? 1.2888 1.3854 1.1956 0.0720  -0.2523 -0.1539 400 ARG B CD  
6772 N NE  . ARG B 400 ? 1.2388 1.3929 1.1943 0.0644  -0.2538 -0.1726 400 ARG B NE  
6773 C CZ  . ARG B 400 ? 1.2970 1.4836 1.2738 0.0730  -0.2807 -0.1822 400 ARG B CZ  
6774 N NH1 . ARG B 400 ? 1.2602 1.5026 1.3066 0.0761  -0.2808 -0.1993 400 ARG B NH1 
6775 N NH2 . ARG B 400 ? 1.2774 1.4417 1.2055 0.0779  -0.3074 -0.1735 400 ARG B NH2 
6776 N N   . PHE B 401 ? 0.8477 0.8674 0.8426 0.1614  -0.0004 -0.0417 401 PHE B N   
6777 C CA  . PHE B 401 ? 0.8165 0.8780 0.8477 0.1619  -0.0019 -0.0388 401 PHE B CA  
6778 C C   . PHE B 401 ? 0.8137 0.9030 0.8743 0.1766  -0.0127 -0.0260 401 PHE B C   
6779 O O   . PHE B 401 ? 0.8606 0.9533 0.9154 0.1749  -0.0290 -0.0198 401 PHE B O   
6780 C CB  . PHE B 401 ? 0.7900 0.8697 0.8245 0.1412  -0.0114 -0.0434 401 PHE B CB  
6781 C CG  . PHE B 401 ? 0.7793 0.8494 0.8010 0.1294  0.0007  -0.0520 401 PHE B CG  
6782 C CD1 . PHE B 401 ? 0.7607 0.7971 0.7463 0.1226  0.0056  -0.0591 401 PHE B CD1 
6783 C CD2 . PHE B 401 ? 0.7516 0.8488 0.7980 0.1247  0.0069  -0.0515 401 PHE B CD2 
6784 C CE1 . PHE B 401 ? 0.7394 0.7721 0.7131 0.1117  0.0150  -0.0652 401 PHE B CE1 
6785 C CE2 . PHE B 401 ? 0.7537 0.8450 0.7877 0.1144  0.0173  -0.0562 401 PHE B CE2 
6786 C CZ  . PHE B 401 ? 0.7614 0.8219 0.7587 0.1082  0.0208  -0.0628 401 PHE B CZ  
6787 N N   . GLU B 402 ? 0.9401 1.0533 1.0328 0.1904  -0.0038 -0.0217 402 GLU B N   
6788 C CA  . GLU B 402 ? 0.9053 1.0546 1.0322 0.2037  -0.0149 -0.0086 402 GLU B CA  
6789 C C   . GLU B 402 ? 0.8827 1.0710 1.0278 0.1874  -0.0332 -0.0086 402 GLU B C   
6790 O O   . GLU B 402 ? 0.8870 1.0991 1.0434 0.1906  -0.0504 0.0003  402 GLU B O   
6791 C CB  . GLU B 402 ? 0.8884 1.0566 1.0480 0.2216  0.0007  -0.0050 402 GLU B CB  
6792 C CG  . GLU B 402 ? 0.9765 1.1600 1.1615 0.2463  -0.0032 0.0109  402 GLU B CG  
6793 C CD  . GLU B 402 ? 1.0076 1.1477 1.1664 0.2599  -0.0006 0.0170  402 GLU B CD  
6794 O OE1 . GLU B 402 ? 0.9735 1.0712 1.0933 0.2489  0.0041  0.0073  402 GLU B OE1 
6795 O OE2 . GLU B 402 ? 1.0181 1.1674 1.1972 0.2817  -0.0030 0.0328  402 GLU B OE2 
6796 N N   . MET B 403 ? 0.7893 0.9856 0.9384 0.1698  -0.0293 -0.0183 403 MET B N   
6797 C CA  . MET B 403 ? 0.7282 0.9556 0.8947 0.1520  -0.0441 -0.0212 403 MET B CA  
6798 C C   . MET B 403 ? 0.7570 0.9718 0.9131 0.1323  -0.0370 -0.0318 403 MET B C   
6799 O O   . MET B 403 ? 0.7703 0.9686 0.9179 0.1338  -0.0202 -0.0344 403 MET B O   
6800 C CB  . MET B 403 ? 0.6799 0.9573 0.8938 0.1568  -0.0476 -0.0152 403 MET B CB  
6801 C CG  . MET B 403 ? 0.7164 1.0089 0.9545 0.1510  -0.0325 -0.0188 403 MET B CG  
6802 S SD  . MET B 403 ? 0.7533 1.0612 1.0038 0.1221  -0.0393 -0.0281 403 MET B SD  
6803 C CE  . MET B 403 ? 0.6437 0.9688 0.9237 0.1217  -0.0184 -0.0262 403 MET B CE  
6804 N N   . PHE B 404 ? 0.6815 0.9059 0.8392 0.1140  -0.0495 -0.0376 404 PHE B N   
6805 C CA  . PHE B 404 ? 0.7004 0.9187 0.8584 0.0961  -0.0431 -0.0453 404 PHE B CA  
6806 C C   . PHE B 404 ? 0.6563 0.9039 0.8412 0.0795  -0.0549 -0.0504 404 PHE B C   
6807 O O   . PHE B 404 ? 0.6544 0.9229 0.8469 0.0787  -0.0706 -0.0507 404 PHE B O   
6808 C CB  . PHE B 404 ? 0.6997 0.8781 0.8170 0.0887  -0.0409 -0.0511 404 PHE B CB  
6809 C CG  . PHE B 404 ? 0.6991 0.8678 0.7955 0.0826  -0.0564 -0.0550 404 PHE B CG  
6810 C CD1 . PHE B 404 ? 0.7082 0.8916 0.8149 0.0657  -0.0671 -0.0624 404 PHE B CD1 
6811 C CD2 . PHE B 404 ? 0.6984 0.8424 0.7643 0.0929  -0.0589 -0.0516 404 PHE B CD2 
6812 C CE1 . PHE B 404 ? 0.6925 0.8692 0.7778 0.0594  -0.0804 -0.0670 404 PHE B CE1 
6813 C CE2 . PHE B 404 ? 0.7391 0.8759 0.7843 0.0870  -0.0724 -0.0537 404 PHE B CE2 
6814 C CZ  . PHE B 404 ? 0.7243 0.8789 0.7782 0.0702  -0.0833 -0.0617 404 PHE B CZ  
6815 N N   . SER B 405 ? 0.6133 0.8633 0.8136 0.0658  -0.0464 -0.0542 405 SER B N   
6816 C CA  . SER B 405 ? 0.6183 0.8886 0.8441 0.0470  -0.0539 -0.0619 405 SER B CA  
6817 C C   . SER B 405 ? 0.5946 0.8478 0.8226 0.0340  -0.0415 -0.0643 405 SER B C   
6818 O O   . SER B 405 ? 0.5945 0.8512 0.8360 0.0374  -0.0269 -0.0569 405 SER B O   
6819 C CB  . SER B 405 ? 0.5681 0.8824 0.8379 0.0475  -0.0569 -0.0590 405 SER B CB  
6820 O OG  . SER B 405 ? 0.6008 0.9341 0.8926 0.0276  -0.0662 -0.0695 405 SER B OG  
6821 N N   . LEU B 406 ? 0.5548 0.7909 0.7702 0.0200  -0.0465 -0.0736 406 LEU B N   
6822 C CA  . LEU B 406 ? 0.5288 0.7455 0.7447 0.0092  -0.0353 -0.0744 406 LEU B CA  
6823 C C   . LEU B 406 ? 0.5432 0.7700 0.7876 -0.0101 -0.0387 -0.0850 406 LEU B C   
6824 O O   . LEU B 406 ? 0.5932 0.8299 0.8374 -0.0176 -0.0524 -0.0966 406 LEU B O   
6825 C CB  . LEU B 406 ? 0.5280 0.7101 0.7016 0.0115  -0.0351 -0.0761 406 LEU B CB  
6826 C CG  . LEU B 406 ? 0.5927 0.7554 0.7652 0.0003  -0.0270 -0.0775 406 LEU B CG  
6827 C CD1 . LEU B 406 ? 0.6077 0.7686 0.7849 0.0055  -0.0111 -0.0642 406 LEU B CD1 
6828 C CD2 . LEU B 406 ? 0.5950 0.7305 0.7302 -0.0011 -0.0321 -0.0838 406 LEU B CD2 
6829 N N   . SER B 407 ? 0.6289 0.8538 0.8985 -0.0186 -0.0256 -0.0812 407 SER B N   
6830 C CA  . SER B 407 ? 0.6019 0.8307 0.9016 -0.0377 -0.0252 -0.0919 407 SER B CA  
6831 C C   . SER B 407 ? 0.6019 0.8117 0.9136 -0.0425 -0.0084 -0.0834 407 SER B C   
6832 O O   . SER B 407 ? 0.6542 0.8575 0.9553 -0.0319 0.0018  -0.0681 407 SER B O   
6833 C CB  . SER B 407 ? 0.6117 0.8770 0.9523 -0.0453 -0.0290 -0.0960 407 SER B CB  
6834 O OG  . SER B 407 ? 0.6320 0.9128 0.9984 -0.0399 -0.0164 -0.0817 407 SER B OG  
6835 N N   . GLY B 408 ? 0.5437 0.7454 0.8781 -0.0588 -0.0052 -0.0932 408 GLY B N   
6836 C CA  . GLY B 408 ? 0.5794 0.7618 0.9283 -0.0626 0.0108  -0.0833 408 GLY B CA  
6837 C C   . GLY B 408 ? 0.5808 0.7624 0.9714 -0.0815 0.0168  -0.0941 408 GLY B C   
6838 O O   . GLY B 408 ? 0.5910 0.7814 0.9897 -0.0936 0.0068  -0.1144 408 GLY B O   
6839 N N   . THR B 409 ? 0.5238 0.6960 0.9419 -0.0844 0.0338  -0.0800 409 THR B N   
6840 C CA  . THR B 409 ? 0.4923 0.6574 0.9539 -0.1024 0.0435  -0.0888 409 THR B CA  
6841 C C   . THR B 409 ? 0.5293 0.6624 0.9818 -0.1064 0.0470  -0.0973 409 THR B C   
6842 O O   . THR B 409 ? 0.5195 0.6326 0.9884 -0.1056 0.0621  -0.0838 409 THR B O   
6843 C CB  . THR B 409 ? 0.4797 0.6496 0.9790 -0.1037 0.0614  -0.0677 409 THR B CB  
6844 O OG1 . THR B 409 ? 0.5223 0.6725 1.0098 -0.0929 0.0730  -0.0457 409 THR B OG1 
6845 C CG2 . THR B 409 ? 0.4804 0.6827 0.9827 -0.0964 0.0591  -0.0575 409 THR B CG2 
6846 N N   . PHE B 410 ? 0.5328 0.6629 0.9584 -0.1095 0.0329  -0.1186 410 PHE B N   
6847 C CA  . PHE B 410 ? 0.5283 0.6305 0.9383 -0.1113 0.0349  -0.1280 410 PHE B CA  
6848 C C   . PHE B 410 ? 0.5322 0.6186 0.9831 -0.1285 0.0475  -0.1421 410 PHE B C   
6849 O O   . PHE B 410 ? 0.5291 0.6286 1.0070 -0.1447 0.0458  -0.1599 410 PHE B O   
6850 C CB  . PHE B 410 ? 0.5476 0.6534 0.9174 -0.1109 0.0172  -0.1467 410 PHE B CB  
6851 C CG  . PHE B 410 ? 0.5262 0.6329 0.8518 -0.0930 0.0089  -0.1329 410 PHE B CG  
6852 C CD1 . PHE B 410 ? 0.5051 0.5899 0.8057 -0.0842 0.0130  -0.1245 410 PHE B CD1 
6853 C CD2 . PHE B 410 ? 0.5007 0.6307 0.8129 -0.0850 -0.0019 -0.1282 410 PHE B CD2 
6854 C CE1 . PHE B 410 ? 0.5385 0.6236 0.8000 -0.0698 0.0064  -0.1136 410 PHE B CE1 
6855 C CE2 . PHE B 410 ? 0.5307 0.6580 0.8045 -0.0691 -0.0073 -0.1167 410 PHE B CE2 
6856 C CZ  . PHE B 410 ? 0.5186 0.6229 0.7663 -0.0625 -0.0032 -0.1104 410 PHE B CZ  
6857 N N   . GLY B 411 ? 0.7130 0.7719 1.1700 -0.1253 0.0605  -0.1345 411 GLY B N   
6858 C CA  . GLY B 411 ? 0.6550 0.6930 1.1520 -0.1397 0.0753  -0.1473 411 GLY B CA  
6859 C C   . GLY B 411 ? 0.6966 0.7214 1.1761 -0.1480 0.0701  -0.1761 411 GLY B C   
6860 O O   . GLY B 411 ? 0.7138 0.7130 1.2146 -0.1539 0.0840  -0.1847 411 GLY B O   
6861 N N   . THR B 412 ? 0.6172 0.6593 1.0567 -0.1471 0.0510  -0.1895 412 THR B N   
6862 C CA  . THR B 412 ? 0.5606 0.5964 0.9776 -0.1559 0.0439  -0.2174 412 THR B CA  
6863 C C   . THR B 412 ? 0.6262 0.6925 1.0208 -0.1635 0.0236  -0.2351 412 THR B C   
6864 O O   . THR B 412 ? 0.6241 0.7138 1.0090 -0.1554 0.0129  -0.2215 412 THR B O   
6865 C CB  . THR B 412 ? 0.5806 0.6010 0.9584 -0.1409 0.0419  -0.2080 412 THR B CB  
6866 O OG1 . THR B 412 ? 0.5689 0.5830 0.9248 -0.1495 0.0370  -0.2345 412 THR B OG1 
6867 C CG2 . THR B 412 ? 0.6158 0.6526 0.9559 -0.1250 0.0279  -0.1890 412 THR B CG2 
6868 N N   . GLN B 413 ? 0.8566 0.9248 1.2454 -0.1792 0.0191  -0.2653 413 GLN B N   
6869 C CA  . GLN B 413 ? 0.8187 0.9177 1.1779 -0.1845 -0.0021 -0.2802 413 GLN B CA  
6870 C C   . GLN B 413 ? 0.8127 0.9080 1.1194 -0.1742 -0.0132 -0.2798 413 GLN B C   
6871 O O   . GLN B 413 ? 0.8951 1.0149 1.1762 -0.1785 -0.0302 -0.2911 413 GLN B O   
6872 C CB  . GLN B 413 ? 0.8407 0.9538 1.2204 -0.2103 -0.0037 -0.3147 413 GLN B CB  
6873 C CG  . GLN B 413 ? 0.9208 1.0341 1.3564 -0.2238 0.0097  -0.3178 413 GLN B CG  
6874 C CD  . GLN B 413 ? 0.9212 1.0730 1.3768 -0.2284 -0.0010 -0.3124 413 GLN B CD  
6875 O OE1 . GLN B 413 ? 0.8594 1.0171 1.3259 -0.2147 0.0009  -0.2849 413 GLN B OE1 
6876 N NE2 . GLN B 413 ? 0.9604 1.1409 1.4240 -0.2496 -0.0112 -0.3405 413 GLN B NE2 
6877 N N   . TYR B 414 ? 0.5989 0.6660 0.8914 -0.1629 -0.0037 -0.2692 414 TYR B N   
6878 C CA  . TYR B 414 ? 0.5995 0.6621 0.8434 -0.1522 -0.0129 -0.2651 414 TYR B CA  
6879 C C   . TYR B 414 ? 0.6296 0.6920 0.8553 -0.1316 -0.0166 -0.2346 414 TYR B C   
6880 O O   . TYR B 414 ? 0.6009 0.6436 0.8258 -0.1207 -0.0065 -0.2179 414 TYR B O   
6881 C CB  . TYR B 414 ? 0.5769 0.6122 0.8167 -0.1544 -0.0003 -0.2754 414 TYR B CB  
6882 C CG  . TYR B 414 ? 0.6033 0.6372 0.8621 -0.1755 0.0059  -0.3085 414 TYR B CG  
6883 C CD1 . TYR B 414 ? 0.5788 0.6350 0.8135 -0.1886 -0.0081 -0.3323 414 TYR B CD1 
6884 C CD2 . TYR B 414 ? 0.6180 0.6288 0.9192 -0.1827 0.0264  -0.3162 414 TYR B CD2 
6885 C CE1 . TYR B 414 ? 0.6070 0.6629 0.8494 -0.2019 -0.0007 -0.3529 414 TYR B CE1 
6886 C CE2 . TYR B 414 ? 0.5893 0.5971 0.9034 -0.1985 0.0342  -0.3427 414 TYR B CE2 
6887 C CZ  . TYR B 414 ? 0.6008 0.6321 0.8816 -0.2060 0.0207  -0.3581 414 TYR B CZ  
6888 O OH  . TYR B 414 ? 0.6400 0.6701 0.9280 -0.2176 0.0295  -0.3778 414 TYR B OH  
6889 N N   . VAL B 415 ? 0.5855 0.6719 0.7954 -0.1263 -0.0316 -0.2280 415 VAL B N   
6890 C CA  . VAL B 415 ? 0.6182 0.7066 0.8104 -0.1079 -0.0353 -0.2029 415 VAL B CA  
6891 C C   . VAL B 415 ? 0.6381 0.7363 0.7872 -0.1013 -0.0516 -0.2030 415 VAL B C   
6892 O O   . VAL B 415 ? 0.5932 0.7152 0.7387 -0.1079 -0.0644 -0.2138 415 VAL B O   
6893 C CB  . VAL B 415 ? 0.6252 0.7329 0.8480 -0.1053 -0.0344 -0.1911 415 VAL B CB  
6894 C CG1 . VAL B 415 ? 0.5941 0.7054 0.7952 -0.0868 -0.0383 -0.1692 415 VAL B CG1 
6895 C CG2 . VAL B 415 ? 0.5842 0.6800 0.8499 -0.1115 -0.0167 -0.1875 415 VAL B CG2 
6896 N N   . PHE B 416 ? 0.6209 0.7026 0.7387 -0.0884 -0.0510 -0.1897 416 PHE B N   
6897 C CA  . PHE B 416 ? 0.6008 0.6838 0.6765 -0.0825 -0.0633 -0.1890 416 PHE B CA  
6898 C C   . PHE B 416 ? 0.6063 0.6936 0.6691 -0.0660 -0.0677 -0.1692 416 PHE B C   
6899 O O   . PHE B 416 ? 0.6149 0.6873 0.6748 -0.0565 -0.0589 -0.1554 416 PHE B O   
6900 C CB  . PHE B 416 ? 0.5498 0.6086 0.6001 -0.0831 -0.0577 -0.1925 416 PHE B CB  
6901 C CG  . PHE B 416 ? 0.5571 0.6081 0.6261 -0.0975 -0.0486 -0.2114 416 PHE B CG  
6902 C CD1 . PHE B 416 ? 0.5719 0.6372 0.6423 -0.1120 -0.0549 -0.2333 416 PHE B CD1 
6903 C CD2 . PHE B 416 ? 0.5554 0.5866 0.6424 -0.0965 -0.0335 -0.2075 416 PHE B CD2 
6904 C CE1 . PHE B 416 ? 0.5568 0.6132 0.6455 -0.1260 -0.0446 -0.2539 416 PHE B CE1 
6905 C CE2 . PHE B 416 ? 0.5404 0.5623 0.6482 -0.1083 -0.0233 -0.2247 416 PHE B CE2 
6906 C CZ  . PHE B 416 ? 0.5606 0.5935 0.6693 -0.1236 -0.0281 -0.2497 416 PHE B CZ  
6907 N N   . PRO B 417 ? 0.6545 0.7634 0.7106 -0.0621 -0.0806 -0.1674 417 PRO B N   
6908 C CA  . PRO B 417 ? 0.6515 0.7651 0.7025 -0.0456 -0.0827 -0.1495 417 PRO B CA  
6909 C C   . PRO B 417 ? 0.6815 0.7752 0.6916 -0.0348 -0.0850 -0.1411 417 PRO B C   
6910 O O   . PRO B 417 ? 0.6486 0.7408 0.6328 -0.0380 -0.0934 -0.1466 417 PRO B O   
6911 C CB  . PRO B 417 ? 0.6470 0.7944 0.7123 -0.0465 -0.0956 -0.1516 417 PRO B CB  
6912 C CG  . PRO B 417 ? 0.6245 0.7810 0.6776 -0.0611 -0.1053 -0.1692 417 PRO B CG  
6913 C CD  . PRO B 417 ? 0.6287 0.7616 0.6838 -0.0729 -0.0936 -0.1819 417 PRO B CD  
6914 N N   . GLU B 418 ? 0.6105 0.6891 0.6144 -0.0234 -0.0764 -0.1283 418 GLU B N   
6915 C CA  . GLU B 418 ? 0.6101 0.6663 0.5780 -0.0149 -0.0756 -0.1215 418 GLU B CA  
6916 C C   . GLU B 418 ? 0.6484 0.7057 0.6126 0.0009  -0.0750 -0.1086 418 GLU B C   
6917 O O   . GLU B 418 ? 0.6702 0.7351 0.6556 0.0063  -0.0678 -0.1026 418 GLU B O   
6918 C CB  . GLU B 418 ? 0.5822 0.6162 0.5417 -0.0176 -0.0641 -0.1210 418 GLU B CB  
6919 C CG  . GLU B 418 ? 0.5789 0.6085 0.5455 -0.0308 -0.0610 -0.1323 418 GLU B CG  
6920 C CD  . GLU B 418 ? 0.6167 0.6286 0.5766 -0.0310 -0.0504 -0.1282 418 GLU B CD  
6921 O OE1 . GLU B 418 ? 0.6125 0.6110 0.5505 -0.0353 -0.0503 -0.1333 418 GLU B OE1 
6922 O OE2 . GLU B 418 ? 0.6588 0.6728 0.6353 -0.0269 -0.0421 -0.1191 418 GLU B OE2 
6923 N N   . VAL B 419 ? 0.5866 0.6342 0.5237 0.0087  -0.0808 -0.1038 419 VAL B N   
6924 C CA  . VAL B 419 ? 0.5964 0.6371 0.5267 0.0246  -0.0776 -0.0924 419 VAL B CA  
6925 C C   . VAL B 419 ? 0.6622 0.6723 0.5559 0.0271  -0.0747 -0.0904 419 VAL B C   
6926 O O   . VAL B 419 ? 0.6097 0.6149 0.4832 0.0238  -0.0826 -0.0913 419 VAL B O   
6927 C CB  . VAL B 419 ? 0.5969 0.6607 0.5390 0.0344  -0.0880 -0.0854 419 VAL B CB  
6928 C CG1 . VAL B 419 ? 0.6001 0.6534 0.5378 0.0524  -0.0820 -0.0739 419 VAL B CG1 
6929 C CG2 . VAL B 419 ? 0.5813 0.6795 0.5613 0.0288  -0.0921 -0.0894 419 VAL B CG2 
6930 N N   . LEU B 420 ? 0.6705 0.6613 0.5548 0.0315  -0.0633 -0.0880 420 LEU B N   
6931 C CA  . LEU B 420 ? 0.6101 0.5715 0.4616 0.0322  -0.0594 -0.0874 420 LEU B CA  
6932 C C   . LEU B 420 ? 0.6967 0.6441 0.5426 0.0462  -0.0516 -0.0809 420 LEU B C   
6933 O O   . LEU B 420 ? 0.7102 0.6650 0.5718 0.0517  -0.0436 -0.0801 420 LEU B O   
6934 C CB  . LEU B 420 ? 0.6019 0.5512 0.4429 0.0208  -0.0523 -0.0941 420 LEU B CB  
6935 C CG  . LEU B 420 ? 0.6517 0.5752 0.4599 0.0163  -0.0510 -0.0959 420 LEU B CG  
6936 C CD1 . LEU B 420 ? 0.6399 0.5648 0.4366 0.0116  -0.0612 -0.0968 420 LEU B CD1 
6937 C CD2 . LEU B 420 ? 0.6614 0.5781 0.4628 0.0058  -0.0440 -0.1016 420 LEU B CD2 
6938 N N   . LEU B 421 ? 0.7398 0.6666 0.5639 0.0519  -0.0527 -0.0763 421 LEU B N   
6939 C CA  . LEU B 421 ? 0.7763 0.6836 0.5943 0.0652  -0.0435 -0.0714 421 LEU B CA  
6940 C C   . LEU B 421 ? 0.7906 0.6661 0.5808 0.0582  -0.0335 -0.0776 421 LEU B C   
6941 O O   . LEU B 421 ? 0.7711 0.6397 0.5450 0.0450  -0.0361 -0.0826 421 LEU B O   
6942 C CB  . LEU B 421 ? 0.7945 0.6996 0.6115 0.0785  -0.0502 -0.0593 421 LEU B CB  
6943 C CG  . LEU B 421 ? 0.7752 0.7171 0.6201 0.0850  -0.0620 -0.0526 421 LEU B CG  
6944 C CD1 . LEU B 421 ? 0.8207 0.7627 0.6653 0.1004  -0.0681 -0.0376 421 LEU B CD1 
6945 C CD2 . LEU B 421 ? 0.8042 0.7652 0.6781 0.0907  -0.0553 -0.0546 421 LEU B CD2 
6946 N N   . SER B 422 ? 0.8227 0.6800 0.6088 0.0665  -0.0213 -0.0786 422 SER B N   
6947 C CA  . SER B 422 ? 0.7935 0.6206 0.5540 0.0593  -0.0109 -0.0863 422 SER B CA  
6948 C C   . SER B 422 ? 0.8595 0.6666 0.5973 0.0520  -0.0160 -0.0839 422 SER B C   
6949 O O   . SER B 422 ? 0.8615 0.6686 0.5996 0.0590  -0.0241 -0.0734 422 SER B O   
6950 C CB  . SER B 422 ? 0.8561 0.6621 0.6157 0.0718  0.0027  -0.0872 422 SER B CB  
6951 O OG  . SER B 422 ? 0.8723 0.6574 0.6119 0.0620  0.0147  -0.0995 422 SER B OG  
6952 N N   . GLU B 423 ? 0.9558 0.7490 0.6739 0.0376  -0.0113 -0.0928 423 GLU B N   
6953 C CA  . GLU B 423 ? 0.9999 0.7750 0.6958 0.0279  -0.0140 -0.0919 423 GLU B CA  
6954 C C   . GLU B 423 ? 0.9737 0.7708 0.6730 0.0208  -0.0266 -0.0896 423 GLU B C   
6955 O O   . GLU B 423 ? 0.9782 0.7651 0.6609 0.0153  -0.0304 -0.0863 423 GLU B O   
6956 C CB  . GLU B 423 ? 1.0287 0.7758 0.7140 0.0379  -0.0114 -0.0820 423 GLU B CB  
6957 C CG  . GLU B 423 ? 1.1024 0.8341 0.7964 0.0528  -0.0009 -0.0803 423 GLU B CG  
6958 C CD  . GLU B 423 ? 1.1550 0.8565 0.8328 0.0453  0.0142  -0.0923 423 GLU B CD  
6959 O OE1 . GLU B 423 ? 1.2912 0.9754 0.9742 0.0559  0.0261  -0.0945 423 GLU B OE1 
6960 O OE2 . GLU B 423 ? 1.1739 0.8699 0.8346 0.0282  0.0147  -0.1003 423 GLU B OE2 
6961 N N   . ASN B 424 ? 0.9047 0.7312 0.6254 0.0201  -0.0320 -0.0919 424 ASN B N   
6962 C CA  . ASN B 424 ? 0.8986 0.7446 0.6243 0.0113  -0.0415 -0.0938 424 ASN B CA  
6963 C C   . ASN B 424 ? 0.9148 0.7669 0.6383 0.0168  -0.0520 -0.0856 424 ASN B C   
6964 O O   . ASN B 424 ? 0.8977 0.7513 0.6082 0.0083  -0.0574 -0.0867 424 ASN B O   
6965 C CB  . ASN B 424 ? 0.8637 0.7001 0.5720 -0.0036 -0.0382 -0.1009 424 ASN B CB  
6966 C CG  . ASN B 424 ? 0.8756 0.7344 0.5995 -0.0127 -0.0409 -0.1073 424 ASN B CG  
6967 O OD1 . ASN B 424 ? 0.9013 0.7772 0.6376 -0.0130 -0.0484 -0.1077 424 ASN B OD1 
6968 N ND2 . ASN B 424 ? 0.8222 0.6827 0.5475 -0.0198 -0.0343 -0.1121 424 ASN B ND2 
6969 N N   . GLN B 425 ? 0.8455 0.7042 0.5823 0.0312  -0.0546 -0.0770 425 GLN B N   
6970 C CA  . GLN B 425 ? 0.8467 0.7170 0.5842 0.0389  -0.0655 -0.0664 425 GLN B CA  
6971 C C   . GLN B 425 ? 0.8478 0.7550 0.6130 0.0400  -0.0750 -0.0681 425 GLN B C   
6972 O O   . GLN B 425 ? 0.8102 0.7288 0.5983 0.0434  -0.0709 -0.0713 425 GLN B O   
6973 C CB  . GLN B 425 ? 0.8527 0.7054 0.5885 0.0560  -0.0614 -0.0532 425 GLN B CB  
6974 C CG  . GLN B 425 ? 0.8617 0.6744 0.5737 0.0543  -0.0494 -0.0532 425 GLN B CG  
6975 C CD  . GLN B 425 ? 0.8899 0.6903 0.5759 0.0451  -0.0531 -0.0492 425 GLN B CD  
6976 O OE1 . GLN B 425 ? 0.9241 0.7304 0.6050 0.0518  -0.0614 -0.0357 425 GLN B OE1 
6977 N NE2 . GLN B 425 ? 0.8792 0.6655 0.5489 0.0298  -0.0470 -0.0598 425 GLN B NE2 
6978 N N   . LEU B 426 ? 0.7504 0.6773 0.5127 0.0356  -0.0873 -0.0666 426 LEU B N   
6979 C CA  . LEU B 426 ? 0.7278 0.6913 0.5156 0.0352  -0.0976 -0.0689 426 LEU B CA  
6980 C C   . LEU B 426 ? 0.7428 0.7204 0.5465 0.0528  -0.1024 -0.0547 426 LEU B C   
6981 O O   . LEU B 426 ? 0.7827 0.7413 0.5746 0.0655  -0.0995 -0.0417 426 LEU B O   
6982 C CB  . LEU B 426 ? 0.6978 0.6799 0.4748 0.0229  -0.1088 -0.0745 426 LEU B CB  
6983 C CG  . LEU B 426 ? 0.6833 0.6556 0.4505 0.0060  -0.1033 -0.0898 426 LEU B CG  
6984 C CD1 . LEU B 426 ? 0.6574 0.6522 0.4178 -0.0066 -0.1133 -0.0987 426 LEU B CD1 
6985 C CD2 . LEU B 426 ? 0.6308 0.6045 0.4240 0.0027  -0.0946 -0.0988 426 LEU B CD2 
6986 N N   . ALA B 427 ? 0.7848 0.7967 0.6179 0.0533  -0.1094 -0.0570 427 ALA B N   
6987 C CA  . ALA B 427 ? 0.7587 0.7922 0.6137 0.0697  -0.1147 -0.0441 427 ALA B CA  
6988 C C   . ALA B 427 ? 0.7734 0.8482 0.6377 0.0648  -0.1322 -0.0431 427 ALA B C   
6989 O O   . ALA B 427 ? 0.7584 0.8663 0.6533 0.0635  -0.1374 -0.0469 427 ALA B O   
6990 C CB  . ALA B 427 ? 0.7681 0.8092 0.6537 0.0751  -0.1056 -0.0473 427 ALA B CB  
6991 N N   . PRO B 428 ? 0.7919 0.8680 0.6299 0.0609  -0.1415 -0.0385 428 PRO B N   
6992 C CA  . PRO B 428 ? 0.7405 0.8594 0.5827 0.0530  -0.1588 -0.0403 428 PRO B CA  
6993 C C   . PRO B 428 ? 0.7783 0.9329 0.6474 0.0684  -0.1688 -0.0253 428 PRO B C   
6994 O O   . PRO B 428 ? 0.7782 0.9237 0.6456 0.0880  -0.1677 -0.0050 428 PRO B O   
6995 C CB  . PRO B 428 ? 0.7590 0.8669 0.5627 0.0495  -0.1640 -0.0335 428 PRO B CB  
6996 C CG  . PRO B 428 ? 0.7848 0.8509 0.5736 0.0646  -0.1523 -0.0183 428 PRO B CG  
6997 C CD  . PRO B 428 ? 0.7932 0.8340 0.5968 0.0647  -0.1365 -0.0291 428 PRO B CD  
6998 N N   . GLY B 429 ? 0.7243 0.9201 0.6207 0.0592  -0.1779 -0.0356 429 GLY B N   
6999 C CA  . GLY B 429 ? 0.6847 0.9234 0.6101 0.0709  -0.1893 -0.0232 429 GLY B CA  
7000 C C   . GLY B 429 ? 0.7110 0.9470 0.6692 0.0872  -0.1788 -0.0160 429 GLY B C   
7001 O O   . GLY B 429 ? 0.7347 1.0083 0.7205 0.0985  -0.1874 -0.0046 429 GLY B O   
7002 N N   . GLU B 430 ? 0.8789 1.0752 0.8355 0.0884  -0.1605 -0.0225 430 GLU B N   
7003 C CA  . GLU B 430 ? 0.8354 1.0282 0.8203 0.1022  -0.1481 -0.0181 430 GLU B CA  
7004 C C   . GLU B 430 ? 0.8363 1.0493 0.8522 0.0895  -0.1441 -0.0330 430 GLU B C   
7005 O O   . GLU B 430 ? 0.8515 1.0692 0.8936 0.0996  -0.1344 -0.0294 430 GLU B O   
7006 C CB  . GLU B 430 ? 0.8399 0.9809 0.8041 0.1103  -0.1298 -0.0167 430 GLU B CB  
7007 C CG  . GLU B 430 ? 0.9318 1.0496 0.8762 0.1281  -0.1287 0.0012  430 GLU B CG  
7008 C CD  . GLU B 430 ? 0.9736 1.0382 0.8920 0.1297  -0.1115 -0.0021 430 GLU B CD  
7009 O OE1 . GLU B 430 ? 0.9973 1.0461 0.9276 0.1396  -0.0967 -0.0031 430 GLU B OE1 
7010 O OE2 . GLU B 430 ? 1.0069 1.0473 0.8929 0.1202  -0.1125 -0.0045 430 GLU B OE2 
7011 N N   . PHE B 431 ? 0.6538 0.8781 0.6684 0.0677  -0.1501 -0.0494 431 PHE B N   
7012 C CA  . PHE B 431 ? 0.6377 0.8769 0.6825 0.0542  -0.1449 -0.0631 431 PHE B CA  
7013 C C   . PHE B 431 ? 0.6494 0.9203 0.7015 0.0336  -0.1584 -0.0776 431 PHE B C   
7014 O O   . PHE B 431 ? 0.6557 0.9284 0.6812 0.0269  -0.1691 -0.0805 431 PHE B O   
7015 C CB  . PHE B 431 ? 0.6190 0.8195 0.6536 0.0473  -0.1280 -0.0718 431 PHE B CB  
7016 C CG  . PHE B 431 ? 0.6135 0.7893 0.6165 0.0331  -0.1286 -0.0828 431 PHE B CG  
7017 C CD1 . PHE B 431 ? 0.6214 0.7654 0.5875 0.0397  -0.1266 -0.0766 431 PHE B CD1 
7018 C CD2 . PHE B 431 ? 0.5931 0.7763 0.6055 0.0129  -0.1294 -0.0997 431 PHE B CD2 
7019 C CE1 . PHE B 431 ? 0.5842 0.7074 0.5230 0.0265  -0.1260 -0.0866 431 PHE B CE1 
7020 C CE2 . PHE B 431 ? 0.5500 0.7111 0.5359 0.0010  -0.1281 -0.1102 431 PHE B CE2 
7021 C CZ  . PHE B 431 ? 0.5796 0.7122 0.5286 0.0078  -0.1266 -0.1034 431 PHE B CZ  
7022 N N   . GLN B 432 ? 0.8335 1.1294 0.9219 0.0227  -0.1569 -0.0873 432 GLN B N   
7023 C CA  . GLN B 432 ? 0.7980 1.1205 0.8975 0.0001  -0.1664 -0.1056 432 GLN B CA  
7024 C C   . GLN B 432 ? 0.8331 1.1499 0.9626 -0.0139 -0.1532 -0.1186 432 GLN B C   
7025 O O   . GLN B 432 ? 0.8187 1.1248 0.9662 -0.0049 -0.1400 -0.1106 432 GLN B O   
7026 C CB  . GLN B 432 ? 0.8085 1.1861 0.9279 -0.0001 -0.1848 -0.1023 432 GLN B CB  
7027 C CG  . GLN B 432 ? 0.8761 1.2808 0.9904 -0.0237 -0.1984 -0.1220 432 GLN B CG  
7028 C CD  . GLN B 432 ? 0.8857 1.2548 0.9594 -0.0337 -0.1950 -0.1333 432 GLN B CD  
7029 O OE1 . GLN B 432 ? 0.8433 1.1979 0.9210 -0.0524 -0.1870 -0.1537 432 GLN B OE1 
7030 N NE2 . GLN B 432 ? 0.8766 1.2305 0.9130 -0.0208 -0.1998 -0.1193 432 GLN B NE2 
7031 N N   . VAL B 433 ? 0.7632 1.0874 0.8978 -0.0362 -0.1561 -0.1389 433 VAL B N   
7032 C CA  . VAL B 433 ? 0.7331 1.0532 0.8994 -0.0521 -0.1442 -0.1523 433 VAL B CA  
7033 C C   . VAL B 433 ? 0.6993 1.0669 0.9022 -0.0661 -0.1541 -0.1626 433 VAL B C   
7034 O O   . VAL B 433 ? 0.7618 1.1600 0.9561 -0.0740 -0.1707 -0.1706 433 VAL B O   
7035 C CB  . VAL B 433 ? 0.7329 1.0217 0.8821 -0.0676 -0.1368 -0.1693 433 VAL B CB  
7036 C CG1 . VAL B 433 ? 0.6923 0.9867 0.8797 -0.0878 -0.1282 -0.1864 433 VAL B CG1 
7037 C CG2 . VAL B 433 ? 0.7123 0.9565 0.8377 -0.0557 -0.1233 -0.1588 433 VAL B CG2 
7038 N N   . SER B 434 ? 0.6657 1.0428 0.9093 -0.0692 -0.1441 -0.1615 434 SER B N   
7039 C CA  . SER B 434 ? 0.5928 1.0143 0.8769 -0.0848 -0.1509 -0.1724 434 SER B CA  
7040 C C   . SER B 434 ? 0.5918 1.0047 0.8916 -0.1120 -0.1444 -0.1977 434 SER B C   
7041 O O   . SER B 434 ? 0.5947 0.9661 0.8802 -0.1161 -0.1319 -0.2038 434 SER B O   
7042 C CB  . SER B 434 ? 0.5513 0.9884 0.8738 -0.0750 -0.1419 -0.1578 434 SER B CB  
7043 O OG  . SER B 434 ? 0.5229 0.9349 0.8679 -0.0837 -0.1225 -0.1610 434 SER B OG  
7044 N N   . THR B 435 ? 0.6723 1.1265 1.0037 -0.1310 -0.1528 -0.2132 435 THR B N   
7045 C CA  . THR B 435 ? 0.6736 1.1210 1.0242 -0.1585 -0.1457 -0.2400 435 THR B CA  
7046 C C   . THR B 435 ? 0.6673 1.0879 1.0541 -0.1628 -0.1232 -0.2373 435 THR B C   
7047 O O   . THR B 435 ? 0.6637 1.0587 1.0606 -0.1801 -0.1113 -0.2549 435 THR B O   
7048 C CB  . THR B 435 ? 0.6391 1.1407 1.0131 -0.1800 -0.1614 -0.2596 435 THR B CB  
7049 O OG1 . THR B 435 ? 0.6937 1.2351 1.1049 -0.1742 -0.1653 -0.2462 435 THR B OG1 
7050 C CG2 . THR B 435 ? 0.7374 1.2648 1.0719 -0.1792 -0.1832 -0.2642 435 THR B CG2 
7051 N N   . ASP B 436 ? 0.5561 0.9826 0.9634 -0.1475 -0.1163 -0.2154 436 ASP B N   
7052 C CA  . ASP B 436 ? 0.5587 0.9598 0.9959 -0.1492 -0.0943 -0.2081 436 ASP B CA  
7053 C C   . ASP B 436 ? 0.5909 0.9465 0.9989 -0.1301 -0.0816 -0.1903 436 ASP B C   
7054 O O   . ASP B 436 ? 0.6003 0.9395 1.0281 -0.1259 -0.0646 -0.1771 436 ASP B O   
7055 C CB  . ASP B 436 ? 0.5088 0.9441 0.9880 -0.1465 -0.0911 -0.1957 436 ASP B CB  
7056 C CG  . ASP B 436 ? 0.5125 0.9740 0.9781 -0.1229 -0.1024 -0.1765 436 ASP B CG  
7057 O OD1 . ASP B 436 ? 0.5155 0.9548 0.9397 -0.1035 -0.1054 -0.1651 436 ASP B OD1 
7058 O OD2 . ASP B 436 ? 0.5182 1.0232 1.0170 -0.1241 -0.1076 -0.1730 436 ASP B OD2 
7059 N N   . GLY B 437 ? 0.5657 0.9034 0.9274 -0.1192 -0.0897 -0.1888 437 GLY B N   
7060 C CA  . GLY B 437 ? 0.5952 0.8893 0.9282 -0.1065 -0.0783 -0.1777 437 GLY B CA  
7061 C C   . GLY B 437 ? 0.5766 0.8638 0.8858 -0.0817 -0.0775 -0.1549 437 GLY B C   
7062 O O   . GLY B 437 ? 0.6048 0.8589 0.8931 -0.0729 -0.0673 -0.1459 437 GLY B O   
7063 N N   . ARG B 438 ? 0.5180 0.8358 0.8300 -0.0704 -0.0877 -0.1460 438 ARG B N   
7064 C CA  . ARG B 438 ? 0.5165 0.8264 0.8076 -0.0468 -0.0854 -0.1266 438 ARG B CA  
7065 C C   . ARG B 438 ? 0.5640 0.8589 0.8092 -0.0367 -0.0964 -0.1257 438 ARG B C   
7066 O O   . ARG B 438 ? 0.6102 0.9237 0.8459 -0.0421 -0.1122 -0.1343 438 ARG B O   
7067 C CB  . ARG B 438 ? 0.5495 0.8982 0.8680 -0.0372 -0.0892 -0.1166 438 ARG B CB  
7068 C CG  . ARG B 438 ? 0.5328 0.8949 0.8944 -0.0430 -0.0752 -0.1122 438 ARG B CG  
7069 C CD  . ARG B 438 ? 0.5199 0.9259 0.9107 -0.0344 -0.0803 -0.1041 438 ARG B CD  
7070 N NE  . ARG B 438 ? 0.4572 0.9024 0.8841 -0.0533 -0.0901 -0.1171 438 ARG B NE  
7071 C CZ  . ARG B 438 ? 0.4485 0.9407 0.9026 -0.0498 -0.0998 -0.1135 438 ARG B CZ  
7072 N NH1 . ARG B 438 ? 0.4828 0.9875 0.9329 -0.0262 -0.1007 -0.0968 438 ARG B NH1 
7073 N NH2 . ARG B 438 ? 0.4389 0.9673 0.9274 -0.0706 -0.1078 -0.1274 438 ARG B NH2 
7074 N N   . LEU B 439 ? 0.5090 0.8651 0.9367 -0.0322 -0.2245 -0.2299 439 LEU B N   
7075 C CA  . LEU B 439 ? 0.5303 0.8559 0.8853 -0.0072 -0.2369 -0.2188 439 LEU B CA  
7076 C C   . LEU B 439 ? 0.5368 0.8903 0.9151 0.0042  -0.2310 -0.2180 439 LEU B C   
7077 O O   . LEU B 439 ? 0.4867 0.8545 0.8803 -0.0084 -0.1978 -0.2048 439 LEU B O   
7078 C CB  . LEU B 439 ? 0.5259 0.8099 0.8128 -0.0125 -0.2122 -0.1925 439 LEU B CB  
7079 C CG  . LEU B 439 ? 0.5547 0.8178 0.7851 0.0040  -0.2034 -0.1760 439 LEU B CG  
7080 C CD1 . LEU B 439 ? 0.5302 0.7666 0.7145 0.0317  -0.2354 -0.1837 439 LEU B CD1 
7081 C CD2 . LEU B 439 ? 0.5477 0.7799 0.7282 -0.0057 -0.1765 -0.1535 439 LEU B CD2 
7082 N N   . PHE B 440 ? 0.6419 1.0021 1.0212 0.0292  -0.2627 -0.2320 440 PHE B N   
7083 C CA  . PHE B 440 ? 0.6565 1.0476 1.0718 0.0390  -0.2562 -0.2343 440 PHE B CA  
7084 C C   . PHE B 440 ? 0.6581 1.0276 1.0271 0.0727  -0.2819 -0.2341 440 PHE B C   
7085 O O   . PHE B 440 ? 0.6589 0.9939 0.9738 0.0898  -0.3090 -0.2354 440 PHE B O   
7086 C CB  . PHE B 440 ? 0.6214 1.0683 1.1349 0.0293  -0.2619 -0.2582 440 PHE B CB  
7087 C CG  . PHE B 440 ? 0.6454 1.1010 1.1821 0.0385  -0.3023 -0.2828 440 PHE B CG  
7088 C CD1 . PHE B 440 ? 0.6803 1.1218 1.1857 0.0703  -0.3350 -0.2884 440 PHE B CD1 
7089 C CD2 . PHE B 440 ? 0.6416 1.1019 1.2115 0.0159  -0.2979 -0.2929 440 PHE B CD2 
7090 C CE1 . PHE B 440 ? 0.6831 1.1191 1.1901 0.0791  -0.3636 -0.3046 440 PHE B CE1 
7091 C CE2 . PHE B 440 ? 0.6778 1.1333 1.2526 0.0241  -0.3266 -0.3109 440 PHE B CE2 
7092 C CZ  . PHE B 440 ? 0.6928 1.1377 1.2355 0.0558  -0.3600 -0.3171 440 PHE B CZ  
7093 N N   . SER B 441 ? 0.6784 1.0662 1.0678 0.0826  -0.2705 -0.2317 441 SER B N   
7094 C CA  . SER B 441 ? 0.7079 1.0717 1.0540 0.1141  -0.2849 -0.2270 441 SER B CA  
7095 C C   . SER B 441 ? 0.7192 1.1079 1.1041 0.1393  -0.3274 -0.2492 441 SER B C   
7096 O O   . SER B 441 ? 0.6898 1.1314 1.1601 0.1318  -0.3328 -0.2688 441 SER B O   
7097 C CB  . SER B 441 ? 0.6706 1.0437 1.0261 0.1126  -0.2516 -0.2165 441 SER B CB  
7098 O OG  . SER B 441 ? 0.6369 1.0653 1.0795 0.1055  -0.2463 -0.2321 441 SER B OG  
7099 N N   . LEU B 442 ? 0.7819 1.1320 1.1037 0.1700  -0.3572 -0.2467 442 LEU B N   
7100 C CA  . LEU B 442 ? 0.7824 1.1456 1.1235 0.1998  -0.3961 -0.2627 442 LEU B CA  
7101 C C   . LEU B 442 ? 0.7716 1.1494 1.1357 0.2231  -0.3936 -0.2610 442 LEU B C   
7102 O O   . LEU B 442 ? 0.7946 1.1834 1.1827 0.2429  -0.4144 -0.2715 442 LEU B O   
7103 C CB  . LEU B 442 ? 0.7969 1.1027 1.0486 0.2237  -0.4226 -0.2563 442 LEU B CB  
7104 C CG  . LEU B 442 ? 0.8437 1.1350 1.0763 0.2070  -0.4320 -0.2631 442 LEU B CG  
7105 C CD1 . LEU B 442 ? 0.8706 1.0956 0.9993 0.2276  -0.4449 -0.2505 442 LEU B CD1 
7106 C CD2 . LEU B 442 ? 0.8332 1.1602 1.1272 0.2054  -0.4527 -0.2863 442 LEU B CD2 
7107 N N   . LYS B 443 ? 0.7743 1.1363 1.1187 0.2149  -0.3547 -0.2430 443 LYS B N   
7108 C CA  . LYS B 443 ? 0.7474 1.1138 1.1064 0.2341  -0.3436 -0.2393 443 LYS B CA  
7109 C C   . LYS B 443 ? 0.7660 1.1158 1.1020 0.2108  -0.2936 -0.2214 443 LYS B C   
7110 O O   . LYS B 443 ? 0.7790 1.1103 1.0809 0.1866  -0.2758 -0.2114 443 LYS B O   
7111 C CB  . LYS B 443 ? 0.8288 1.1476 1.1211 0.2760  -0.3697 -0.2308 443 LYS B CB  
7112 C CG  . LYS B 443 ? 0.8877 1.1364 1.0755 0.2781  -0.3627 -0.2105 443 LYS B CG  
7113 C CD  . LYS B 443 ? 0.9336 1.1375 1.0569 0.3212  -0.3981 -0.2060 443 LYS B CD  
7114 C CE  . LYS B 443 ? 0.9759 1.1021 0.9928 0.3269  -0.3808 -0.1830 443 LYS B CE  
7115 N NZ  . LYS B 443 ? 1.0748 1.1578 1.0217 0.3630  -0.4210 -0.1814 443 LYS B NZ  
7116 N N   . PRO B 444 ? 0.6307 0.9864 0.9839 0.2182  -0.2713 -0.2183 444 PRO B N   
7117 C CA  . PRO B 444 ? 0.6541 0.9922 0.9796 0.1986  -0.2261 -0.2038 444 PRO B CA  
7118 C C   . PRO B 444 ? 0.7105 0.9838 0.9420 0.2034  -0.2208 -0.1853 444 PRO B C   
7119 O O   . PRO B 444 ? 0.7463 0.9789 0.9276 0.2315  -0.2448 -0.1805 444 PRO B O   
7120 C CB  . PRO B 444 ? 0.6338 0.9832 0.9901 0.2154  -0.2129 -0.2075 444 PRO B CB  
7121 C CG  . PRO B 444 ? 0.6241 1.0159 1.0488 0.2327  -0.2442 -0.2259 444 PRO B CG  
7122 C CD  . PRO B 444 ? 0.6058 0.9850 1.0057 0.2460  -0.2872 -0.2296 444 PRO B CD  
7123 N N   . THR B 445 ? 0.6033 0.8676 0.8110 0.1757  -0.1898 -0.1755 445 THR B N   
7124 C CA  . THR B 445 ? 0.6412 0.8490 0.7688 0.1758  -0.1812 -0.1602 445 THR B CA  
7125 C C   . THR B 445 ? 0.7031 0.8644 0.7834 0.1992  -0.1702 -0.1515 445 THR B C   
7126 O O   . THR B 445 ? 0.7097 0.8834 0.8170 0.2040  -0.1525 -0.1547 445 THR B O   
7127 C CB  . THR B 445 ? 0.6370 0.8528 0.7601 0.1429  -0.1489 -0.1534 445 THR B CB  
7128 O OG1 . THR B 445 ? 0.6252 0.8621 0.7744 0.1344  -0.1184 -0.1550 445 THR B OG1 
7129 C CG2 . THR B 445 ? 0.5239 0.7776 0.6889 0.1207  -0.1566 -0.1592 445 THR B CG2 
7130 N N   . SER B 446 ? 0.8349 0.9386 0.8429 0.2134  -0.1773 -0.1407 446 SER B N   
7131 C CA  . SER B 446 ? 0.8797 0.9321 0.8403 0.2364  -0.1642 -0.1314 446 SER B CA  
7132 C C   . SER B 446 ? 0.9633 1.0044 0.9138 0.2165  -0.1200 -0.1268 446 SER B C   
7133 O O   . SER B 446 ? 1.0473 1.0598 0.9824 0.2305  -0.1017 -0.1237 446 SER B O   
7134 C CB  . SER B 446 ? 1.0008 0.9896 0.8824 0.2588  -0.1814 -0.1206 446 SER B CB  
7135 O OG  . SER B 446 ? 0.9750 0.9382 0.8141 0.2380  -0.1667 -0.1136 446 SER B OG  
7136 N N   . GLY B 447 ? 0.8080 0.8684 0.7647 0.1854  -0.1028 -0.1267 447 GLY B N   
7137 C CA  . GLY B 447 ? 0.7914 0.8537 0.7477 0.1651  -0.0649 -0.1265 447 GLY B CA  
7138 C C   . GLY B 447 ? 0.7300 0.8483 0.7323 0.1353  -0.0547 -0.1323 447 GLY B C   
7139 O O   . GLY B 447 ? 0.6926 0.8450 0.7279 0.1286  -0.0738 -0.1354 447 GLY B O   
7140 N N   . PRO B 448 ? 0.6960 0.8242 0.7009 0.1174  -0.0237 -0.1345 448 PRO B N   
7141 C CA  . PRO B 448 ? 0.6705 0.8476 0.7092 0.0912  -0.0130 -0.1377 448 PRO B CA  
7142 C C   . PRO B 448 ? 0.6296 0.8043 0.6505 0.0783  -0.0236 -0.1295 448 PRO B C   
7143 O O   . PRO B 448 ? 0.6189 0.7531 0.5940 0.0817  -0.0255 -0.1227 448 PRO B O   
7144 C CB  . PRO B 448 ? 0.6176 0.7952 0.6472 0.0788  0.0196  -0.1423 448 PRO B CB  
7145 C CG  . PRO B 448 ? 0.6682 0.8049 0.6772 0.0984  0.0281  -0.1446 448 PRO B CG  
7146 C CD  . PRO B 448 ? 0.7254 0.8193 0.7014 0.1205  0.0033  -0.1352 448 PRO B CD  
7147 N N   . VAL B 449 ? 0.5896 0.8062 0.6479 0.0630  -0.0273 -0.1304 449 VAL B N   
7148 C CA  . VAL B 449 ? 0.5513 0.7680 0.6015 0.0513  -0.0380 -0.1232 449 VAL B CA  
7149 C C   . VAL B 449 ? 0.5605 0.7831 0.5937 0.0320  -0.0162 -0.1170 449 VAL B C   
7150 O O   . VAL B 449 ? 0.5265 0.7804 0.5790 0.0206  0.0029  -0.1199 449 VAL B O   
7151 C CB  . VAL B 449 ? 0.5519 0.8071 0.6534 0.0446  -0.0512 -0.1273 449 VAL B CB  
7152 C CG1 . VAL B 449 ? 0.5028 0.7630 0.6010 0.0264  -0.0506 -0.1190 449 VAL B CG1 
7153 C CG2 . VAL B 449 ? 0.5550 0.8030 0.6702 0.0646  -0.0812 -0.1347 449 VAL B CG2 
7154 N N   . LEU B 450 ? 0.6034 0.7968 0.6000 0.0296  -0.0196 -0.1094 450 LEU B N   
7155 C CA  . LEU B 450 ? 0.5600 0.7618 0.5451 0.0131  -0.0055 -0.1027 450 LEU B CA  
7156 C C   . LEU B 450 ? 0.5817 0.8044 0.5882 0.0014  -0.0135 -0.0958 450 LEU B C   
7157 O O   . LEU B 450 ? 0.5733 0.8245 0.5931 -0.0120 -0.0001 -0.0912 450 LEU B O   
7158 C CB  . LEU B 450 ? 0.5813 0.7408 0.5215 0.0165  -0.0030 -0.0990 450 LEU B CB  
7159 C CG  . LEU B 450 ? 0.5793 0.7168 0.4975 0.0224  0.0142  -0.1055 450 LEU B CG  
7160 C CD1 . LEU B 450 ? 0.5500 0.6441 0.4280 0.0245  0.0182  -0.1019 450 LEU B CD1 
7161 C CD2 . LEU B 450 ? 0.5325 0.7056 0.4676 0.0096  0.0345  -0.1116 450 LEU B CD2 
7162 N N   . THR B 451 ? 0.6877 0.8945 0.6956 0.0068  -0.0344 -0.0951 451 THR B N   
7163 C CA  . THR B 451 ? 0.6567 0.8807 0.6899 -0.0050 -0.0401 -0.0906 451 THR B CA  
7164 C C   . THR B 451 ? 0.6353 0.8529 0.6861 0.0028  -0.0657 -0.0982 451 THR B C   
7165 O O   . THR B 451 ? 0.6407 0.8295 0.6666 0.0190  -0.0823 -0.1032 451 THR B O   
7166 C CB  . THR B 451 ? 0.6535 0.8614 0.6610 -0.0141 -0.0343 -0.0794 451 THR B CB  
7167 O OG1 . THR B 451 ? 0.6867 0.9148 0.7234 -0.0271 -0.0326 -0.0735 451 THR B OG1 
7168 C CG2 . THR B 451 ? 0.6562 0.8208 0.6285 -0.0049 -0.0490 -0.0799 451 THR B CG2 
7169 N N   . VAL B 452 ? 0.4637 0.7083 0.5572 -0.0087 -0.0676 -0.0997 452 VAL B N   
7170 C CA  . VAL B 452 ? 0.4444 0.6889 0.5627 -0.0071 -0.0909 -0.1091 452 VAL B CA  
7171 C C   . VAL B 452 ? 0.4298 0.6764 0.5592 -0.0252 -0.0821 -0.1010 452 VAL B C   
7172 O O   . VAL B 452 ? 0.4469 0.7204 0.6071 -0.0393 -0.0628 -0.0954 452 VAL B O   
7173 C CB  . VAL B 452 ? 0.3970 0.6776 0.5721 -0.0042 -0.0989 -0.1231 452 VAL B CB  
7174 C CG1 . VAL B 452 ? 0.4004 0.6888 0.6112 -0.0060 -0.1221 -0.1359 452 VAL B CG1 
7175 C CG2 . VAL B 452 ? 0.4068 0.6821 0.5697 0.0164  -0.1070 -0.1295 452 VAL B CG2 
7176 N N   . THR B 453 ? 0.5797 0.7943 0.6796 -0.0242 -0.0927 -0.0987 453 THR B N   
7177 C CA  . THR B 453 ? 0.5828 0.7920 0.6852 -0.0394 -0.0809 -0.0883 453 THR B CA  
7178 C C   . THR B 453 ? 0.6109 0.8035 0.7221 -0.0416 -0.1002 -0.0980 453 THR B C   
7179 O O   . THR B 453 ? 0.6291 0.7974 0.7132 -0.0284 -0.1223 -0.1078 453 THR B O   
7180 C CB  . THR B 453 ? 0.6088 0.7939 0.6628 -0.0386 -0.0671 -0.0737 453 THR B CB  
7181 O OG1 . THR B 453 ? 0.6221 0.8282 0.6735 -0.0397 -0.0481 -0.0668 453 THR B OG1 
7182 C CG2 . THR B 453 ? 0.5945 0.7689 0.6491 -0.0505 -0.0580 -0.0626 453 THR B CG2 
7183 N N   . LEU B 454 ? 0.4857 0.6892 0.6325 -0.0579 -0.0904 -0.0954 454 LEU B N   
7184 C CA  . LEU B 454 ? 0.4895 0.6740 0.6439 -0.0643 -0.1017 -0.1029 454 LEU B CA  
7185 C C   . LEU B 454 ? 0.5041 0.6640 0.6297 -0.0712 -0.0828 -0.0840 454 LEU B C   
7186 O O   . LEU B 454 ? 0.5088 0.6815 0.6507 -0.0820 -0.0595 -0.0690 454 LEU B O   
7187 C CB  . LEU B 454 ? 0.4861 0.6985 0.7076 -0.0784 -0.1018 -0.1155 454 LEU B CB  
7188 C CG  . LEU B 454 ? 0.4759 0.7158 0.7350 -0.0705 -0.1253 -0.1386 454 LEU B CG  
7189 C CD1 . LEU B 454 ? 0.4313 0.7071 0.7668 -0.0875 -0.1152 -0.1493 454 LEU B CD1 
7190 C CD2 . LEU B 454 ? 0.4793 0.6982 0.7172 -0.0575 -0.1603 -0.1573 454 LEU B CD2 
7191 N N   . PHE B 455 ? 0.5701 0.6937 0.6505 -0.0632 -0.0923 -0.0842 455 PHE B N   
7192 C CA  . PHE B 455 ? 0.5544 0.6528 0.6042 -0.0658 -0.0767 -0.0681 455 PHE B CA  
7193 C C   . PHE B 455 ? 0.6064 0.6807 0.6640 -0.0732 -0.0826 -0.0749 455 PHE B C   
7194 O O   . PHE B 455 ? 0.5930 0.6434 0.6286 -0.0662 -0.1022 -0.0897 455 PHE B O   
7195 C CB  . PHE B 455 ? 0.5545 0.6291 0.5505 -0.0518 -0.0790 -0.0654 455 PHE B CB  
7196 C CG  . PHE B 455 ? 0.5739 0.6302 0.5436 -0.0529 -0.0617 -0.0499 455 PHE B CG  
7197 C CD1 . PHE B 455 ? 0.5915 0.6171 0.5495 -0.0555 -0.0615 -0.0494 455 PHE B CD1 
7198 C CD2 . PHE B 455 ? 0.5605 0.6316 0.5188 -0.0504 -0.0467 -0.0383 455 PHE B CD2 
7199 C CE1 . PHE B 455 ? 0.5533 0.5642 0.4919 -0.0548 -0.0463 -0.0362 455 PHE B CE1 
7200 C CE2 . PHE B 455 ? 0.5669 0.6258 0.5059 -0.0498 -0.0337 -0.0266 455 PHE B CE2 
7201 C CZ  . PHE B 455 ? 0.5556 0.5844 0.4860 -0.0515 -0.0335 -0.0250 455 PHE B CZ  
7202 N N   . GLY B 456 ? 0.5853 0.6628 0.6709 -0.0865 -0.0649 -0.0643 456 GLY B N   
7203 C CA  . GLY B 456 ? 0.6007 0.6566 0.7027 -0.0959 -0.0670 -0.0720 456 GLY B CA  
7204 C C   . GLY B 456 ? 0.6374 0.6661 0.7171 -0.0971 -0.0488 -0.0535 456 GLY B C   
7205 O O   . GLY B 456 ? 0.6154 0.6533 0.6880 -0.0957 -0.0304 -0.0321 456 GLY B O   
7206 N N   . ARG B 457 ? 0.6075 0.6031 0.6745 -0.0980 -0.0555 -0.0630 457 ARG B N   
7207 C CA  . ARG B 457 ? 0.6424 0.6089 0.6926 -0.0982 -0.0396 -0.0485 457 ARG B CA  
7208 C C   . ARG B 457 ? 0.6507 0.6037 0.7385 -0.1125 -0.0315 -0.0531 457 ARG B C   
7209 O O   . ARG B 457 ? 0.6593 0.6071 0.7645 -0.1189 -0.0471 -0.0772 457 ARG B O   
7210 C CB  . ARG B 457 ? 0.6632 0.5967 0.6646 -0.0872 -0.0492 -0.0562 457 ARG B CB  
7211 C CG  . ARG B 457 ? 0.6196 0.5587 0.5843 -0.0743 -0.0485 -0.0483 457 ARG B CG  
7212 C CD  . ARG B 457 ? 0.6332 0.5680 0.5880 -0.0712 -0.0285 -0.0274 457 ARG B CD  
7213 N NE  . ARG B 457 ? 0.6128 0.5103 0.5504 -0.0696 -0.0227 -0.0283 457 ARG B NE  
7214 C CZ  . ARG B 457 ? 0.6728 0.5573 0.6315 -0.0758 -0.0106 -0.0198 457 ARG B CZ  
7215 N NH1 . ARG B 457 ? 0.6552 0.5571 0.6509 -0.0847 -0.0025 -0.0098 457 ARG B NH1 
7216 N NH2 . ARG B 457 ? 0.6783 0.5300 0.6206 -0.0724 -0.0034 -0.0201 457 ARG B NH2 
7217 N N   . LEU B 458 ? 0.6029 0.5488 0.7024 -0.1167 -0.0075 -0.0309 458 LEU B N   
7218 C CA  . LEU B 458 ? 0.6102 0.5357 0.7436 -0.1298 0.0061  -0.0318 458 LEU B CA  
7219 C C   . LEU B 458 ? 0.6316 0.5192 0.7373 -0.1233 0.0138  -0.0235 458 LEU B C   
7220 O O   . LEU B 458 ? 0.6436 0.5240 0.7448 -0.1185 0.0332  0.0019  458 LEU B O   
7221 C CB  . LEU B 458 ? 0.5730 0.5144 0.7404 -0.1381 0.0309  -0.0108 458 LEU B CB  
7222 C CG  . LEU B 458 ? 0.5718 0.5457 0.7820 -0.1497 0.0281  -0.0244 458 LEU B CG  
7223 C CD1 . LEU B 458 ? 0.5646 0.5699 0.7564 -0.1399 0.0077  -0.0332 458 LEU B CD1 
7224 C CD2 . LEU B 458 ? 0.6397 0.6220 0.8779 -0.1580 0.0587  -0.0013 458 LEU B CD2 
7225 N N   . TYR B 459 ? 0.6628 0.5258 0.7488 -0.1218 -0.0019 -0.0459 459 TYR B N   
7226 C CA  . TYR B 459 ? 0.6702 0.4982 0.7239 -0.1135 0.0043  -0.0411 459 TYR B CA  
7227 C C   . TYR B 459 ? 0.6779 0.4819 0.7559 -0.1192 0.0279  -0.0265 459 TYR B C   
7228 O O   . TYR B 459 ? 0.6771 0.4643 0.7376 -0.1094 0.0404  -0.0095 459 TYR B O   
7229 C CB  . TYR B 459 ? 0.6804 0.4831 0.7070 -0.1121 -0.0149 -0.0697 459 TYR B CB  
7230 C CG  . TYR B 459 ? 0.6621 0.4807 0.6572 -0.1028 -0.0374 -0.0817 459 TYR B CG  
7231 C CD1 . TYR B 459 ? 0.6250 0.4379 0.5762 -0.0888 -0.0364 -0.0729 459 TYR B CD1 
7232 C CD2 . TYR B 459 ? 0.6366 0.4750 0.6485 -0.1074 -0.0588 -0.1027 459 TYR B CD2 
7233 C CE1 . TYR B 459 ? 0.6255 0.4477 0.5469 -0.0796 -0.0537 -0.0822 459 TYR B CE1 
7234 C CE2 . TYR B 459 ? 0.6317 0.4817 0.6138 -0.0961 -0.0793 -0.1119 459 TYR B CE2 
7235 C CZ  . TYR B 459 ? 0.6491 0.4887 0.5841 -0.0822 -0.0755 -0.1004 459 TYR B CZ  
7236 O OH  . TYR B 459 ? 0.6337 0.4793 0.5375 -0.0702 -0.0930 -0.1084 459 TYR B OH  
7237 N N   . GLU B 460 ? 0.8587 0.6597 0.9796 -0.1348 0.0349  -0.0343 460 GLU B N   
7238 C CA  . GLU B 460 ? 0.8696 0.6427 1.0155 -0.1406 0.0603  -0.0200 460 GLU B CA  
7239 C C   . GLU B 460 ? 0.9036 0.6853 1.0464 -0.1306 0.0810  0.0179  460 GLU B C   
7240 O O   . GLU B 460 ? 0.9250 0.6795 1.0719 -0.1264 0.1006  0.0362  460 GLU B O   
7241 C CB  . GLU B 460 ? 0.8469 0.6186 1.0447 -0.1611 0.0665  -0.0366 460 GLU B CB  
7242 C CG  . GLU B 460 ? 0.8834 0.6852 1.1139 -0.1682 0.0795  -0.0215 460 GLU B CG  
7243 C CD  . GLU B 460 ? 0.9151 0.7573 1.1567 -0.1727 0.0566  -0.0428 460 GLU B CD  
7244 O OE1 . GLU B 460 ? 0.8964 0.7478 1.1037 -0.1627 0.0302  -0.0576 460 GLU B OE1 
7245 O OE2 . GLU B 460 ? 0.8979 0.7612 1.1830 -0.1854 0.0671  -0.0437 460 GLU B OE2 
7246 N N   . LYS B 461 ? 0.8456 0.6642 0.9805 -0.1255 0.0767  0.0296  461 LYS B N   
7247 C CA  . LYS B 461 ? 0.8084 0.6388 0.9391 -0.1165 0.0946  0.0636  461 LYS B CA  
7248 C C   . LYS B 461 ? 0.8239 0.6603 0.9158 -0.0968 0.0896  0.0783  461 LYS B C   
7249 O O   . LYS B 461 ? 0.8519 0.7034 0.9347 -0.0863 0.0992  0.1044  461 LYS B O   
7250 C CB  . LYS B 461 ? 0.7525 0.6198 0.8969 -0.1225 0.0955  0.0672  461 LYS B CB  
7251 C CG  . LYS B 461 ? 0.7834 0.6437 0.9714 -0.1386 0.1175  0.0716  461 LYS B CG  
7252 C CD  . LYS B 461 ? 0.7776 0.6758 0.9849 -0.1471 0.1163  0.0660  461 LYS B CD  
7253 C CE  . LYS B 461 ? 0.8372 0.7279 1.0834 -0.1610 0.1463  0.0781  461 LYS B CE  
7254 N NZ  . LYS B 461 ? 0.8799 0.7766 1.1025 -0.1501 0.1675  0.1145  461 LYS B NZ  
7255 N N   . ASP B 462 ? 0.7916 0.6163 0.8609 -0.0912 0.0757  0.0617  462 ASP B N   
7256 C CA  . ASP B 462 ? 0.8119 0.6416 0.8531 -0.0741 0.0743  0.0733  462 ASP B CA  
7257 C C   . ASP B 462 ? 0.8492 0.6525 0.8980 -0.0656 0.0918  0.0935  462 ASP B C   
7258 O O   . ASP B 462 ? 0.8978 0.7054 0.9320 -0.0501 0.0927  0.1052  462 ASP B O   
7259 C CB  . ASP B 462 ? 0.8225 0.6425 0.8373 -0.0711 0.0594  0.0497  462 ASP B CB  
7260 C CG  . ASP B 462 ? 0.8429 0.6798 0.8493 -0.0781 0.0412  0.0282  462 ASP B CG  
7261 O OD1 . ASP B 462 ? 0.8007 0.6658 0.8231 -0.0836 0.0396  0.0327  462 ASP B OD1 
7262 O OD2 . ASP B 462 ? 0.7759 0.5966 0.7584 -0.0768 0.0295  0.0076  462 ASP B OD2 
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