data_9H8U
# 
_entry.id   9H8U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9H8U         pdb_00009h8u 10.2210/pdb9h8u/pdb 
WWPDB D_1292142855 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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                        9H8U 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gwen.tjallinks@iusspavia.it 
_pdbx_contact_author.name_first         Gwen 
_pdbx_contact_author.name_last          Tjallinks 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5174-913X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tjallinks, G.' 1 0000-0002-5174-913X 
'Mattevi, A.'   2 0000-0002-9523-7128 
# 
_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            'Acs Chem.Biol.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1554-8937 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                646 
_citation.page_last                 655 
_citation.title                     
;Structural and Mechanistic Characterization of the Flavin-Dependent Monooxygenase and Oxidase Involved in Sorbicillinoid Biosynthesis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acschembio.4c00783 
_citation.pdbx_database_id_PubMed   40052414 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tjallinks, G.'   1 ? 
primary 'Angeleri, N.'    2 ? 
primary 'Nguyen, Q.T.'    3 ? 
primary 'Mannucci, B.'    4 ? 
primary 'Arentshorst, M.' 5 ? 
primary 'Visser, J.'      6 ? 
primary 'Ram, A.F.J.'     7 ? 
primary 'Fraaije, M.W.'   8 ? 
primary 'Mattevi, A.'     9 ? 
# 
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 'FAD-linked oxidoreductase sorD' 50444.559 2 1.1.1.- ? ? ? 
2 branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1 ?       ? ? ? 
3 branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1 ?       ? ? ? 
4 branched    man 
;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1 ?       ? ? ? 
5 branched    man 
'alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   3 
?       ? ? ? 
6 non-polymer man 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   2 ?       ? ? ? 
7 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   4 ?       ? ? ? 
8 non-polymer syn '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' 232.275   2 ?       ? ? ? 
9 water       nat water 18.015    9 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sorbicillinoid biosynthetic cluster protein D' 
# 
_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       
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMNETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVTHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQPTDEALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMNETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVTHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQPTDEALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_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 
6 'FLAVIN-ADENINE DINUCLEOTIDE'                                         FAD   
7 2-acetamido-2-deoxy-beta-D-glucopyranose                              NAG   
8 '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' A1ITD 
9 water                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLN n 
1 3   ALA n 
1 4   ALA n 
1 5   SER n 
1 6   ALA n 
1 7   PHE n 
1 8   ALA n 
1 9   THR n 
1 10  CYS n 
1 11  LEU n 
1 12  LEU n 
1 13  ALA n 
1 14  SER n 
1 15  VAL n 
1 16  GLY n 
1 17  GLY n 
1 18  ASN n 
1 19  SER n 
1 20  SER n 
1 21  ALA n 
1 22  VAL n 
1 23  ALA n 
1 24  PHE n 
1 25  PRO n 
1 26  ASN n 
1 27  GLN n 
1 28  ALA n 
1 29  ASN n 
1 30  TYR n 
1 31  SER n 
1 32  THR n 
1 33  LEU n 
1 34  VAL n 
1 35  ALA n 
1 36  PRO n 
1 37  TYR n 
1 38  ASN n 
1 39  PHE n 
1 40  ASP n 
1 41  LEU n 
1 42  LEU n 
1 43  THR n 
1 44  THR n 
1 45  PRO n 
1 46  SER n 
1 47  ALA n 
1 48  ILE n 
1 49  VAL n 
1 50  TRP n 
1 51  PRO n 
1 52  GLN n 
1 53  ASP n 
1 54  THR n 
1 55  GLN n 
1 56  GLN n 
1 57  VAL n 
1 58  ALA n 
1 59  ALA n 
1 60  ALA n 
1 61  VAL n 
1 62  LYS n 
1 63  CYS n 
1 64  ALA n 
1 65  VAL n 
1 66  ASP n 
1 67  SER n 
1 68  ASP n 
1 69  ILE n 
1 70  LYS n 
1 71  VAL n 
1 72  GLN n 
1 73  PRO n 
1 74  LYS n 
1 75  SER n 
1 76  GLY n 
1 77  GLY n 
1 78  HIS n 
1 79  ASN n 
1 80  TYR n 
1 81  GLY n 
1 82  ASN n 
1 83  TYR n 
1 84  GLY n 
1 85  SER n 
1 86  THR n 
1 87  THR n 
1 88  GLY n 
1 89  GLU n 
1 90  LEU n 
1 91  SER n 
1 92  VAL n 
1 93  ASN n 
1 94  LEU n 
1 95  ASP n 
1 96  ASN n 
1 97  LEU n 
1 98  GLN n 
1 99  HIS n 
1 100 PHE n 
1 101 SER n 
1 102 MET n 
1 103 ASN n 
1 104 GLU n 
1 105 THR n 
1 106 SER n 
1 107 TRP n 
1 108 THR n 
1 109 ALA n 
1 110 ARG n 
1 111 LEU n 
1 112 GLY n 
1 113 PRO n 
1 114 GLY n 
1 115 ASN n 
1 116 ARG n 
1 117 LEU n 
1 118 GLY n 
1 119 ARG n 
1 120 VAL n 
1 121 THR n 
1 122 GLU n 
1 123 LEU n 
1 124 MET n 
1 125 TYR n 
1 126 ASN n 
1 127 ASN n 
1 128 GLY n 
1 129 GLY n 
1 130 ARG n 
1 131 HIS n 
1 132 VAL n 
1 133 PRO n 
1 134 HIS n 
1 135 GLY n 
1 136 THR n 
1 137 THR n 
1 138 PHE n 
1 139 THR n 
1 140 VAL n 
1 141 GLY n 
1 142 LEU n 
1 143 GLY n 
1 144 GLY n 
1 145 HIS n 
1 146 ALA n 
1 147 THR n 
1 148 VAL n 
1 149 GLY n 
1 150 GLY n 
1 151 ALA n 
1 152 GLY n 
1 153 ALA n 
1 154 ALA n 
1 155 SER n 
1 156 ARG n 
1 157 MET n 
1 158 HIS n 
1 159 GLY n 
1 160 LEU n 
1 161 LEU n 
1 162 LEU n 
1 163 ASP n 
1 164 TYR n 
1 165 VAL n 
1 166 GLU n 
1 167 GLU n 
1 168 VAL n 
1 169 GLU n 
1 170 VAL n 
1 171 VAL n 
1 172 LEU n 
1 173 ALA n 
1 174 ASN n 
1 175 SER n 
1 176 SER n 
1 177 ILE n 
1 178 VAL n 
1 179 ARG n 
1 180 ALA n 
1 181 SER n 
1 182 LYS n 
1 183 SER n 
1 184 HIS n 
1 185 ASN n 
1 186 GLU n 
1 187 ASP n 
1 188 LEU n 
1 189 PHE n 
1 190 PHE n 
1 191 ALA n 
1 192 VAL n 
1 193 ARG n 
1 194 GLY n 
1 195 ALA n 
1 196 ALA n 
1 197 SER n 
1 198 SER n 
1 199 VAL n 
1 200 GLY n 
1 201 ILE n 
1 202 VAL n 
1 203 THR n 
1 204 ASP n 
1 205 PHE n 
1 206 SER n 
1 207 ILE n 
1 208 ARG n 
1 209 THR n 
1 210 GLU n 
1 211 PRO n 
1 212 VAL n 
1 213 PRO n 
1 214 VAL n 
1 215 SER n 
1 216 SER n 
1 217 VAL n 
1 218 THR n 
1 219 TYR n 
1 220 SER n 
1 221 TYR n 
1 222 ILE n 
1 223 TRP n 
1 224 GLU n 
1 225 GLY n 
1 226 THR n 
1 227 ASP n 
1 228 PRO n 
1 229 ALA n 
1 230 ALA n 
1 231 ARG n 
1 232 ALA n 
1 233 GLU n 
1 234 VAL n 
1 235 PHE n 
1 236 LEU n 
1 237 THR n 
1 238 TRP n 
1 239 GLN n 
1 240 SER n 
1 241 LEU n 
1 242 LEU n 
1 243 ALA n 
1 244 GLY n 
1 245 GLY n 
1 246 SER n 
1 247 LEU n 
1 248 PRO n 
1 249 GLN n 
1 250 HIS n 
1 251 MET n 
1 252 ALA n 
1 253 TYR n 
1 254 ASP n 
1 255 LEU n 
1 256 VAL n 
1 257 ALA n 
1 258 THR n 
1 259 ALA n 
1 260 ASN n 
1 261 SER n 
1 262 MET n 
1 263 ILE n 
1 264 LEU n 
1 265 GLY n 
1 266 GLY n 
1 267 ALA n 
1 268 TYR n 
1 269 PHE n 
1 270 GLY n 
1 271 SER n 
1 272 GLN n 
1 273 GLU n 
1 274 ASP n 
1 275 PHE n 
1 276 GLU n 
1 277 ALA n 
1 278 PHE n 
1 279 ASN n 
1 280 LEU n 
1 281 SER n 
1 282 SER n 
1 283 HIS n 
1 284 PHE n 
1 285 LYS n 
1 286 VAL n 
1 287 ALA n 
1 288 PRO n 
1 289 ASP n 
1 290 VAL n 
1 291 THR n 
1 292 HIS n 
1 293 ILE n 
1 294 LYS n 
1 295 THR n 
1 296 TYR n 
1 297 THR n 
1 298 ASN n 
1 299 PHE n 
1 300 PHE n 
1 301 ASP n 
1 302 PHE n 
1 303 SER n 
1 304 ALA n 
1 305 ALA n 
1 306 ALA n 
1 307 SER n 
1 308 ALA n 
1 309 GLN n 
1 310 THR n 
1 311 LYS n 
1 312 ALA n 
1 313 ALA n 
1 314 GLY n 
1 315 ILE n 
1 316 ALA n 
1 317 SER n 
1 318 PRO n 
1 319 SER n 
1 320 HIS n 
1 321 PHE n 
1 322 TYR n 
1 323 ALA n 
1 324 LYS n 
1 325 SER n 
1 326 LEU n 
1 327 VAL n 
1 328 PHE n 
1 329 ASN n 
1 330 GLN n 
1 331 GLN n 
1 332 THR n 
1 333 LEU n 
1 334 ILE n 
1 335 PRO n 
1 336 ASP n 
1 337 ASP n 
1 338 ALA n 
1 339 ALA n 
1 340 GLU n 
1 341 GLU n 
1 342 VAL n 
1 343 PHE n 
1 344 LYS n 
1 345 TYR n 
1 346 LEU n 
1 347 ALA n 
1 348 THR n 
1 349 THR n 
1 350 LYS n 
1 351 ASN n 
1 352 GLY n 
1 353 THR n 
1 354 ASP n 
1 355 LEU n 
1 356 TYR n 
1 357 ALA n 
1 358 VAL n 
1 359 THR n 
1 360 PHE n 
1 361 ALA n 
1 362 ALA n 
1 363 LEU n 
1 364 GLY n 
1 365 GLY n 
1 366 ALA n 
1 367 VAL n 
1 368 ARG n 
1 369 ASP n 
1 370 VAL n 
1 371 SER n 
1 372 ALA n 
1 373 SER n 
1 374 GLU n 
1 375 THR n 
1 376 ALA n 
1 377 PHE n 
1 378 TYR n 
1 379 HIS n 
1 380 ARG n 
1 381 ASP n 
1 382 ALA n 
1 383 SER n 
1 384 TYR n 
1 385 PHE n 
1 386 MET n 
1 387 PHE n 
1 388 SER n 
1 389 PHE n 
1 390 GLY n 
1 391 ARG n 
1 392 THR n 
1 393 SER n 
1 394 GLY n 
1 395 ASP n 
1 396 LEU n 
1 397 THR n 
1 398 ASP n 
1 399 THR n 
1 400 THR n 
1 401 VAL n 
1 402 GLN n 
1 403 PHE n 
1 404 LEU n 
1 405 ASP n 
1 406 GLY n 
1 407 LEU n 
1 408 SER n 
1 409 GLU n 
1 410 VAL n 
1 411 LEU n 
1 412 THR n 
1 413 SER n 
1 414 GLY n 
1 415 GLN n 
1 416 PRO n 
1 417 ASP n 
1 418 ALA n 
1 419 TYR n 
1 420 TYR n 
1 421 GLY n 
1 422 GLN n 
1 423 TYR n 
1 424 VAL n 
1 425 GLY n 
1 426 ASN n 
1 427 VAL n 
1 428 ASP n 
1 429 PRO n 
1 430 ARG n 
1 431 GLN n 
1 432 PRO n 
1 433 THR n 
1 434 ASP n 
1 435 GLU n 
1 436 ALA n 
1 437 LEU n 
1 438 THR n 
1 439 GLY n 
1 440 TYR n 
1 441 TYR n 
1 442 GLY n 
1 443 LYS n 
1 444 ASN n 
1 445 LEU n 
1 446 HIS n 
1 447 ARG n 
1 448 LEU n 
1 449 GLN n 
1 450 GLN n 
1 451 ILE n 
1 452 LYS n 
1 453 SER n 
1 454 ALA n 
1 455 VAL n 
1 456 ASP n 
1 457 PRO n 
1 458 ASN n 
1 459 ASP n 
1 460 VAL n 
1 461 PHE n 
1 462 HIS n 
1 463 ASN n 
1 464 GLN n 
1 465 GLN n 
1 466 SER n 
1 467 ILE n 
1 468 PRO n 
1 469 PRO n 
1 470 LEU n 
1 471 SER 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                   471 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'sorD, Pc21g05110' 
_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      'Penicillium rubens Wisconsin 54-1255' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     500485 
_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      'Aspergillus niger' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     5061 
_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_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1  2 DManpa1-3DManpa1-3DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                    
'Glycam Condensed Sequence' GMML       1.0   
2  2 'WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2-2/a4-b1_b4-c1_c3-d1_d3-e1'             WURCS PDB2Glycan 
1.1.0 
3  2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}' LINUCS PDB-CARE   ? 
4  3 'DManpa1-3[DManpa1-6]DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                
'Glycam Condensed Sequence' GMML       1.0   
5  3 'WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2-2/a4-b1_b4-c1_c3-d1_c6-e1'             WURCS PDB2Glycan 
1.1.0 
6  3 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}' LINUCS PDB-CARE   ? 
7  4 DManpa1-3DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                             
'Glycam Condensed Sequence' GMML       1.0   
8  4 'WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2/a4-b1_b4-c1_c3-d1'                     WURCS PDB2Glycan 
1.1.0 
9  4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][b-D-Manp]{}}}}'                    LINUCS PDB-CARE   ? 
10 5 DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                      
'Glycam Condensed Sequence' GMML       1.0   
11 5 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2/a4-b1_b4-c1'                             WURCS PDB2Glycan 
1.1.0 
12 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{}}}'                                       LINUCS PDB-CARE   ? 
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  2 3 MAN C1 O1 2 NAG O4 HO4 sing ? 
3  2 4 MAN C1 O1 3 MAN O3 HO3 sing ? 
4  2 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
5  3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  3 3 MAN C1 O1 2 NAG O4 HO4 sing ? 
7  3 4 MAN C1 O1 3 MAN O3 HO3 sing ? 
8  3 5 MAN C1 O1 3 MAN O6 HO6 sing ? 
9  4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
10 4 3 MAN C1 O1 2 NAG O4 HO4 sing ? 
11 4 4 MAN C1 O1 3 MAN O3 HO3 sing ? 
12 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
13 5 3 MAN C1 O1 2 NAG O4 HO4 sing ? 
# 
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 
A1ITD non-polymer                   . '(2~{Z})-1-[3,5-dimethyl-2,4-bis(oxidanyl)phenyl]hexa-2,4-dien-1-one' ? 'C14 H16 O3'        
232.275 
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 
FAD   non-polymer                   . 'FLAVIN-ADENINE DINUCLEOTIDE'                                         ? 'C27 H33 N9 O15 P2' 
785.550 
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 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose                                                 
'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'         180.156 
MET   'L-peptide linking'           y METHIONINE                                                            ? 'C5 H11 N O2 S'     
149.211 
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose                              
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'       221.208 
PHE   'L-peptide linking'           y PHENYLALANINE                                                         ? 'C9 H11 N O2'       
165.189 
PRO   'L-peptide linking'           y PROLINE                                                               ? 'C5 H9 N O2'        
115.130 
SER   'L-peptide linking'           y SERINE                                                                ? 'C3 H7 N O3'        
105.093 
THR   'L-peptide linking'           y THREONINE                                                             ? 'C4 H9 N O3'        
119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN                                                            ? 'C11 H12 N2 O2'     
204.225 
TYR   'L-peptide linking'           y TYROSINE                                                              ? 'C9 H11 N O3'       
181.189 
VAL   'L-peptide linking'           y VALINE                                                                ? 'C5 H11 N O2'       
117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  TRP 50  50  50  TRP TRP A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  CYS 63  63  63  CYS CYS A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 MET 124 124 124 MET MET A . n 
A 1 125 TYR 125 125 125 TYR TYR A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ASN 185 185 185 ASN ASN A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ASP 204 204 204 ASP ASP A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 TRP 223 223 223 TRP TRP A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 LEU 241 241 241 LEU LEU 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 GLY 244 244 244 GLY GLY A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 GLN 249 249 249 GLN GLN A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 MET 251 251 251 MET MET A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLY 265 265 265 GLY GLY A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 ASN 279 279 279 ASN ASN 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 SER 282 282 282 SER SER A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 LYS 294 294 294 LYS LYS A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 GLN 309 309 309 GLN GLN A . n 
A 1 310 THR 310 310 310 THR THR A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 HIS 320 320 320 HIS HIS A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 LYS 324 324 324 LYS LYS A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 GLU 341 341 341 GLU GLU A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 TYR 345 345 345 TYR TYR A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 THR 348 348 348 THR THR A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 ASN 351 351 351 ASN ASN A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 TYR 356 356 356 TYR TYR A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 ALA 366 366 366 ALA ALA A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 ASP 369 369 369 ASP ASP A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 THR 375 375 375 THR THR A . n 
A 1 376 ALA 376 376 376 ALA ALA A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 TYR 378 378 378 TYR TYR A . n 
A 1 379 HIS 379 379 379 HIS HIS A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 TYR 384 384 384 TYR TYR A . n 
A 1 385 PHE 385 385 385 PHE PHE A . n 
A 1 386 MET 386 386 386 MET MET A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 PHE 389 389 389 PHE PHE A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 THR 392 392 392 THR THR A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 LEU 396 396 396 LEU LEU A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 THR 400 400 400 THR THR A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 GLN 402 402 402 GLN GLN A . n 
A 1 403 PHE 403 403 403 PHE PHE A . n 
A 1 404 LEU 404 404 404 LEU LEU A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 LEU 407 407 407 LEU LEU A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 VAL 410 410 410 VAL VAL A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 GLY 414 414 414 GLY GLY A . n 
A 1 415 GLN 415 415 415 GLN GLN A . n 
A 1 416 PRO 416 416 416 PRO PRO A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 ALA 418 418 418 ALA ALA A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 TYR 420 420 420 TYR TYR A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 GLN 422 422 422 GLN GLN A . n 
A 1 423 TYR 423 423 423 TYR TYR A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 ASN 426 426 426 ASN ASN A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 PRO 429 429 429 PRO PRO A . n 
A 1 430 ARG 430 430 430 ARG ARG A . n 
A 1 431 GLN 431 431 431 GLN GLN A . n 
A 1 432 PRO 432 432 432 PRO PRO A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 GLU 435 435 435 GLU GLU A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 TYR 441 441 441 TYR TYR A . n 
A 1 442 GLY 442 442 442 GLY GLY A . n 
A 1 443 LYS 443 443 443 LYS LYS A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 HIS 446 446 446 HIS HIS A . n 
A 1 447 ARG 447 447 447 ARG ARG A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 GLN 449 449 449 GLN GLN A . n 
A 1 450 GLN 450 450 450 GLN GLN A . n 
A 1 451 ILE 451 451 451 ILE ILE A . n 
A 1 452 LYS 452 452 452 LYS LYS A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 ASP 456 456 456 ASP ASP A . n 
A 1 457 PRO 457 457 457 PRO PRO A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 ASP 459 459 459 ASP ASP A . n 
A 1 460 VAL 460 460 460 VAL VAL A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 HIS 462 462 462 HIS HIS A . n 
A 1 463 ASN 463 463 463 ASN ASN A . n 
A 1 464 GLN 464 464 464 GLN GLN A . n 
A 1 465 GLN 465 465 465 GLN GLN A . n 
A 1 466 SER 466 466 466 SER SER A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 PRO 468 468 468 PRO PRO A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 SER 471 471 471 SER SER A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLN 2   2   ?   ?   ?   B . n 
B 1 3   ALA 3   3   ?   ?   ?   B . n 
B 1 4   ALA 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   ALA 8   8   8   ALA ALA B . n 
B 1 9   THR 9   9   9   THR THR B . n 
B 1 10  CYS 10  10  10  CYS CYS B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  VAL 15  15  15  VAL VAL B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  SER 20  20  20  SER SER B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  VAL 22  22  22  VAL VAL B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  ASN 29  29  29  ASN ASN B . n 
B 1 30  TYR 30  30  30  TYR TYR B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  PRO 36  36  36  PRO PRO B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  PHE 39  39  39  PHE PHE B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  ILE 48  48  48  ILE ILE B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  TRP 50  50  50  TRP TRP B . n 
B 1 51  PRO 51  51  51  PRO PRO B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  GLN 56  56  56  GLN GLN B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  VAL 61  61  61  VAL VAL B . n 
B 1 62  LYS 62  62  62  LYS LYS B . n 
B 1 63  CYS 63  63  63  CYS CYS B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  GLN 72  72  72  GLN GLN B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  HIS 78  78  78  HIS HIS B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  TYR 80  80  80  TYR TYR B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  SER 91  91  91  SER SER B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  ASN 93  93  93  ASN ASN B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  HIS 99  99  99  HIS HIS B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 MET 102 102 102 MET MET B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 THR 105 105 105 THR THR B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 TRP 107 107 107 TRP TRP B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 ARG 110 110 110 ARG ARG B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 ARG 119 119 119 ARG ARG B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 THR 121 121 121 THR THR B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 MET 124 124 124 MET MET B . n 
B 1 125 TYR 125 125 125 TYR TYR B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 ASN 127 127 127 ASN ASN B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 ARG 130 130 130 ARG ARG B . n 
B 1 131 HIS 131 131 131 HIS HIS B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 HIS 134 134 134 HIS HIS B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 THR 139 139 139 THR THR B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 HIS 145 145 145 HIS HIS B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 HIS 158 158 158 HIS HIS B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 GLU 169 169 169 GLU GLU B . n 
B 1 170 VAL 170 170 170 VAL VAL B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 ASN 174 174 174 ASN ASN B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 LYS 182 182 182 LYS LYS B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 HIS 184 184 184 HIS HIS B . n 
B 1 185 ASN 185 185 185 ASN ASN B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 PHE 190 190 190 PHE PHE B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 VAL 192 192 192 VAL VAL B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 ASP 204 204 204 ASP ASP B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 SER 206 206 206 SER SER B . n 
B 1 207 ILE 207 207 207 ILE ILE B . n 
B 1 208 ARG 208 208 208 ARG ARG B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 PRO 211 211 211 PRO PRO B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 PRO 213 213 213 PRO PRO B . n 
B 1 214 VAL 214 214 214 VAL VAL B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 THR 218 218 218 THR THR B . n 
B 1 219 TYR 219 219 219 TYR TYR B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 TYR 221 221 221 TYR TYR B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 TRP 223 223 223 TRP TRP B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 ALA 229 229 229 ALA ALA B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ARG 231 231 231 ARG ARG B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 GLU 233 233 233 GLU GLU B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 THR 237 237 237 THR THR B . n 
B 1 238 TRP 238 238 238 TRP TRP B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 LEU 241 241 241 LEU LEU 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 GLY 244 244 244 GLY GLY B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 LEU 247 247 247 LEU LEU B . n 
B 1 248 PRO 248 248 248 PRO PRO B . n 
B 1 249 GLN 249 249 249 GLN GLN B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 MET 251 251 251 MET MET B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 TYR 253 253 253 TYR TYR B . n 
B 1 254 ASP 254 254 254 ASP ASP B . n 
B 1 255 LEU 255 255 255 LEU LEU B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 THR 258 258 258 THR THR B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 ASN 260 260 260 ASN ASN B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLY 265 265 265 GLY GLY B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 ALA 267 267 267 ALA ALA B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 PHE 269 269 269 PHE PHE B . n 
B 1 270 GLY 270 270 270 GLY GLY B . n 
B 1 271 SER 271 271 271 SER SER B . n 
B 1 272 GLN 272 272 272 GLN GLN B . n 
B 1 273 GLU 273 273 273 GLU GLU B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 PHE 275 275 275 PHE PHE B . n 
B 1 276 GLU 276 276 276 GLU GLU B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 PHE 278 278 278 PHE PHE B . n 
B 1 279 ASN 279 279 279 ASN ASN 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 SER 282 282 282 SER SER B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 PHE 284 284 284 PHE PHE B . n 
B 1 285 LYS 285 285 285 LYS LYS B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 VAL 290 290 290 VAL VAL B . n 
B 1 291 THR 291 291 291 THR THR B . n 
B 1 292 HIS 292 292 292 HIS HIS B . n 
B 1 293 ILE 293 293 293 ILE ILE B . n 
B 1 294 LYS 294 294 294 LYS LYS B . n 
B 1 295 THR 295 295 295 THR THR B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 THR 297 297 297 THR THR B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 PHE 299 299 299 PHE PHE B . n 
B 1 300 PHE 300 300 300 PHE PHE B . n 
B 1 301 ASP 301 301 301 ASP ASP B . n 
B 1 302 PHE 302 302 302 PHE PHE B . n 
B 1 303 SER 303 303 303 SER SER B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 ALA 306 306 306 ALA ALA B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 GLN 309 309 309 GLN GLN B . n 
B 1 310 THR 310 310 310 THR THR B . n 
B 1 311 LYS 311 311 311 LYS LYS B . n 
B 1 312 ALA 312 312 312 ALA ALA B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 GLY 314 314 314 GLY GLY B . n 
B 1 315 ILE 315 315 315 ILE ILE B . n 
B 1 316 ALA 316 316 316 ALA ALA B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 PRO 318 318 318 PRO PRO B . n 
B 1 319 SER 319 319 319 SER SER B . n 
B 1 320 HIS 320 320 320 HIS HIS B . n 
B 1 321 PHE 321 321 321 PHE PHE B . n 
B 1 322 TYR 322 322 322 TYR TYR B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 LYS 324 324 324 LYS LYS B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 LEU 326 326 326 LEU LEU B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 PHE 328 328 328 PHE PHE B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 GLN 330 330 330 GLN GLN B . n 
B 1 331 GLN 331 331 331 GLN GLN B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 ILE 334 334 334 ILE ILE B . n 
B 1 335 PRO 335 335 335 PRO PRO B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 ASP 337 337 337 ASP ASP B . n 
B 1 338 ALA 338 338 338 ALA ALA B . n 
B 1 339 ALA 339 339 339 ALA ALA B . n 
B 1 340 GLU 340 340 340 GLU GLU B . n 
B 1 341 GLU 341 341 341 GLU GLU B . n 
B 1 342 VAL 342 342 342 VAL VAL B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 TYR 345 345 345 TYR TYR B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 THR 348 348 348 THR THR B . n 
B 1 349 THR 349 349 349 THR THR B . n 
B 1 350 LYS 350 350 350 LYS LYS B . n 
B 1 351 ASN 351 351 351 ASN ASN B . n 
B 1 352 GLY 352 352 352 GLY GLY B . n 
B 1 353 THR 353 353 353 THR THR B . n 
B 1 354 ASP 354 354 354 ASP ASP B . n 
B 1 355 LEU 355 355 355 LEU LEU B . n 
B 1 356 TYR 356 356 356 TYR TYR B . n 
B 1 357 ALA 357 357 357 ALA ALA B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 THR 359 359 359 THR THR B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 ALA 361 361 361 ALA ALA B . n 
B 1 362 ALA 362 362 362 ALA ALA B . n 
B 1 363 LEU 363 363 363 LEU LEU B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 GLY 365 365 365 GLY GLY B . n 
B 1 366 ALA 366 366 366 ALA ALA B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 ASP 369 369 369 ASP ASP B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 SER 371 371 371 SER SER B . n 
B 1 372 ALA 372 372 372 ALA ALA B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 GLU 374 374 374 GLU GLU B . n 
B 1 375 THR 375 375 375 THR THR B . n 
B 1 376 ALA 376 376 376 ALA ALA B . n 
B 1 377 PHE 377 377 377 PHE PHE B . n 
B 1 378 TYR 378 378 378 TYR TYR B . n 
B 1 379 HIS 379 379 379 HIS HIS B . n 
B 1 380 ARG 380 380 380 ARG ARG B . n 
B 1 381 ASP 381 381 381 ASP ASP B . n 
B 1 382 ALA 382 382 382 ALA ALA B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 TYR 384 384 384 TYR TYR B . n 
B 1 385 PHE 385 385 385 PHE PHE B . n 
B 1 386 MET 386 386 386 MET MET B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 SER 388 388 388 SER SER B . n 
B 1 389 PHE 389 389 389 PHE PHE B . n 
B 1 390 GLY 390 390 390 GLY GLY B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 THR 392 392 392 THR THR B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 ASP 395 395 395 ASP ASP B . n 
B 1 396 LEU 396 396 396 LEU LEU B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 ASP 398 398 398 ASP ASP B . n 
B 1 399 THR 399 399 399 THR THR B . n 
B 1 400 THR 400 400 400 THR THR B . n 
B 1 401 VAL 401 401 401 VAL VAL B . n 
B 1 402 GLN 402 402 402 GLN GLN B . n 
B 1 403 PHE 403 403 403 PHE PHE B . n 
B 1 404 LEU 404 404 404 LEU LEU B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 LEU 407 407 407 LEU LEU B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 GLU 409 409 409 GLU GLU B . n 
B 1 410 VAL 410 410 410 VAL VAL B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 THR 412 412 412 THR THR B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 GLY 414 414 414 GLY GLY B . n 
B 1 415 GLN 415 415 415 GLN GLN B . n 
B 1 416 PRO 416 416 416 PRO PRO B . n 
B 1 417 ASP 417 417 417 ASP ASP B . n 
B 1 418 ALA 418 418 418 ALA ALA B . n 
B 1 419 TYR 419 419 419 TYR TYR B . n 
B 1 420 TYR 420 420 420 TYR TYR B . n 
B 1 421 GLY 421 421 421 GLY GLY B . n 
B 1 422 GLN 422 422 422 GLN GLN B . n 
B 1 423 TYR 423 423 423 TYR TYR B . n 
B 1 424 VAL 424 424 424 VAL VAL B . n 
B 1 425 GLY 425 425 425 GLY GLY B . n 
B 1 426 ASN 426 426 426 ASN ASN B . n 
B 1 427 VAL 427 427 427 VAL VAL B . n 
B 1 428 ASP 428 428 428 ASP ASP B . n 
B 1 429 PRO 429 429 429 PRO PRO B . n 
B 1 430 ARG 430 430 430 ARG ARG B . n 
B 1 431 GLN 431 431 431 GLN GLN B . n 
B 1 432 PRO 432 432 432 PRO PRO B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 GLU 435 435 435 GLU GLU B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 GLY 439 439 439 GLY GLY B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 TYR 441 441 441 TYR TYR B . n 
B 1 442 GLY 442 442 442 GLY GLY B . n 
B 1 443 LYS 443 443 443 LYS LYS B . n 
B 1 444 ASN 444 444 444 ASN ASN B . n 
B 1 445 LEU 445 445 445 LEU LEU B . n 
B 1 446 HIS 446 446 446 HIS HIS B . n 
B 1 447 ARG 447 447 447 ARG ARG B . n 
B 1 448 LEU 448 448 448 LEU LEU B . n 
B 1 449 GLN 449 449 449 GLN GLN B . n 
B 1 450 GLN 450 450 450 GLN GLN B . n 
B 1 451 ILE 451 451 451 ILE ILE B . n 
B 1 452 LYS 452 452 452 LYS LYS B . n 
B 1 453 SER 453 453 453 SER SER B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 VAL 455 455 455 VAL VAL B . n 
B 1 456 ASP 456 456 456 ASP ASP B . n 
B 1 457 PRO 457 457 457 PRO PRO B . n 
B 1 458 ASN 458 458 458 ASN ASN B . n 
B 1 459 ASP 459 459 459 ASP ASP B . n 
B 1 460 VAL 460 460 460 VAL VAL B . n 
B 1 461 PHE 461 461 461 PHE PHE B . n 
B 1 462 HIS 462 462 462 HIS HIS B . n 
B 1 463 ASN 463 463 463 ASN ASN B . n 
B 1 464 GLN 464 464 464 GLN GLN B . n 
B 1 465 GLN 465 465 465 GLN GLN B . n 
B 1 466 SER 466 466 466 SER SER B . n 
B 1 467 ILE 467 467 467 ILE ILE B . n 
B 1 468 PRO 468 468 468 PRO PRO B . n 
B 1 469 PRO 469 469 469 PRO PRO B . n 
B 1 470 LEU 470 470 470 LEU LEU B . n 
B 1 471 SER 471 471 471 SER SER B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 NAG 1 C NAG 1 C NAG 1 n 
C 2 NAG 2 C NAG 2 C NAG 2 n 
C 2 MAN 3 C MAN 3 C MAN 3 n 
C 2 MAN 4 C MAN 4 C MAN 4 n 
C 2 MAN 5 C MAN 5 C MAN 5 n 
D 3 NAG 1 D NAG 1 D NAG 1 n 
D 3 NAG 2 D NAG 2 D NAG 2 n 
D 3 MAN 3 D MAN 3 D MAN 3 n 
D 3 MAN 4 D MAN 4 D MAN 4 n 
D 3 MAN 5 D MAN 5 D MAN 5 n 
E 4 NAG 1 E NAG 1 E NAG 1 n 
E 4 NAG 2 E NAG 2 E NAG 2 n 
E 4 MAN 3 E MAN 3 E MAN 3 n 
E 4 MAN 4 E MAN 4 E MAN 4 n 
F 5 NAG 1 F NAG 1 F NAG 1 n 
F 5 NAG 2 F NAG 2 F NAG 2 n 
F 5 MAN 3 F MAN 3 F MAN 3 n 
G 5 NAG 1 G NAG 1 G NAG 1 n 
G 5 NAG 2 G NAG 2 G NAG 2 n 
G 5 MAN 3 G MAN 3 G MAN 3 n 
H 5 NAG 1 H NAG 1 H NAG 1 n 
H 5 NAG 2 H NAG 2 H NAG 2 n 
H 5 MAN 3 H MAN 3 H MAN 3 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ITD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ITD 
_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 
I 6 FAD   1 501 472 FAD   FAD A . 
J 7 NAG   1 502 480 NAG   NAG A . 
K 8 A1ITD 1 503 483 A1ITD DRG A . 
L 7 NAG   1 504 488 NAG   NAG A . 
M 6 FAD   1 501 472 FAD   FAD B . 
N 8 A1ITD 1 502 473 A1ITD DRG B . 
O 7 NAG   1 503 483 NAG   NAG B . 
P 7 NAG   1 504 484 NAG   NAG B . 
Q 9 HOH   1 601 81  HOH   HOH A . 
Q 9 HOH   2 602 30  HOH   HOH A . 
Q 9 HOH   3 603 14  HOH   HOH A . 
Q 9 HOH   4 604 26  HOH   HOH A . 
Q 9 HOH   5 605 85  HOH   HOH A . 
Q 9 HOH   6 606 1   HOH   HOH A . 
Q 9 HOH   7 607 47  HOH   HOH A . 
Q 9 HOH   8 608 75  HOH   HOH A . 
R 9 HOH   1 601 11  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU   104 ? CG  ? A GLU   104 CG  
2  1 Y 1 A GLU   104 ? CD  ? A GLU   104 CD  
3  1 Y 1 A GLU   104 ? OE1 ? A GLU   104 OE1 
4  1 Y 1 A GLU   104 ? OE2 ? A GLU   104 OE2 
5  1 Y 1 A GLU   233 ? CG  ? A GLU   233 CG  
6  1 Y 1 A GLU   233 ? CD  ? A GLU   233 CD  
7  1 Y 1 A GLU   233 ? OE1 ? A GLU   233 OE1 
8  1 Y 1 A GLU   233 ? OE2 ? A GLU   233 OE2 
9  1 Y 1 A GLN   249 ? CG  ? A GLN   249 CG  
10 1 Y 1 A GLN   249 ? CD  ? A GLN   249 CD  
11 1 Y 1 A GLN   249 ? OE1 ? A GLN   249 OE1 
12 1 Y 1 A GLN   249 ? NE2 ? A GLN   249 NE2 
13 1 Y 1 A LYS   285 ? CG  ? A LYS   285 CG  
14 1 Y 1 A LYS   285 ? CD  ? A LYS   285 CD  
15 1 Y 1 A LYS   285 ? CE  ? A LYS   285 CE  
16 1 Y 1 A LYS   285 ? NZ  ? A LYS   285 NZ  
17 1 Y 1 A LYS   344 ? CG  ? A LYS   344 CG  
18 1 Y 1 A LYS   344 ? CD  ? A LYS   344 CD  
19 1 Y 1 A LYS   344 ? CE  ? A LYS   344 CE  
20 1 Y 1 A LYS   344 ? NZ  ? A LYS   344 NZ  
21 1 Y 1 A LYS   350 ? CG  ? A LYS   350 CG  
22 1 Y 1 A LYS   350 ? CD  ? A LYS   350 CD  
23 1 Y 1 A LYS   350 ? CE  ? A LYS   350 CE  
24 1 Y 1 A LYS   350 ? NZ  ? A LYS   350 NZ  
25 1 Y 1 A ARG   368 ? CG  ? A ARG   368 CG  
26 1 Y 1 A ARG   368 ? CD  ? A ARG   368 CD  
27 1 Y 1 A ARG   368 ? NE  ? A ARG   368 NE  
28 1 Y 1 A ARG   368 ? CZ  ? A ARG   368 CZ  
29 1 Y 1 A ARG   368 ? NH1 ? A ARG   368 NH1 
30 1 Y 1 A ARG   368 ? NH2 ? A ARG   368 NH2 
31 1 Y 1 A LYS   443 ? CG  ? A LYS   443 CG  
32 1 Y 1 A LYS   443 ? CD  ? A LYS   443 CD  
33 1 Y 1 A LYS   443 ? CE  ? A LYS   443 CE  
34 1 Y 1 A LYS   443 ? NZ  ? A LYS   443 NZ  
35 1 Y 1 B ARG   156 ? CG  ? B ARG   156 CG  
36 1 Y 1 B ARG   156 ? CD  ? B ARG   156 CD  
37 1 Y 1 B ARG   156 ? NE  ? B ARG   156 NE  
38 1 Y 1 B ARG   156 ? CZ  ? B ARG   156 CZ  
39 1 Y 1 B ARG   156 ? NH1 ? B ARG   156 NH1 
40 1 Y 1 B ARG   156 ? NH2 ? B ARG   156 NH2 
41 1 Y 1 B LYS   285 ? CG  ? B LYS   285 CG  
42 1 Y 1 B LYS   285 ? CD  ? B LYS   285 CD  
43 1 Y 1 B LYS   285 ? CE  ? B LYS   285 CE  
44 1 Y 1 B LYS   285 ? NZ  ? B LYS   285 NZ  
45 1 Y 1 B LYS   344 ? CG  ? B LYS   344 CG  
46 1 Y 1 B LYS   344 ? CD  ? B LYS   344 CD  
47 1 Y 1 B LYS   344 ? CE  ? B LYS   344 CE  
48 1 Y 1 B LYS   344 ? NZ  ? B LYS   344 NZ  
49 1 Y 1 B LYS   350 ? CG  ? B LYS   350 CG  
50 1 Y 1 B LYS   350 ? CD  ? B LYS   350 CD  
51 1 Y 1 B LYS   350 ? CE  ? B LYS   350 CE  
52 1 Y 1 B LYS   350 ? NZ  ? B LYS   350 NZ  
53 1 Y 1 B ARG   380 ? CG  ? B ARG   380 CG  
54 1 Y 1 B ARG   380 ? CD  ? B ARG   380 CD  
55 1 Y 1 B ARG   380 ? NE  ? B ARG   380 NE  
56 1 Y 1 B ARG   380 ? CZ  ? B ARG   380 CZ  
57 1 Y 1 B ARG   380 ? NH1 ? B ARG   380 NH1 
58 1 Y 1 B ARG   380 ? NH2 ? B ARG   380 NH2 
59 1 Y 1 B ARG   391 ? CG  ? B ARG   391 CG  
60 1 Y 1 B ARG   391 ? CD  ? B ARG   391 CD  
61 1 Y 1 B ARG   391 ? NE  ? B ARG   391 NE  
62 1 Y 1 B ARG   391 ? CZ  ? B ARG   391 CZ  
63 1 Y 1 B ARG   391 ? NH1 ? B ARG   391 NH1 
64 1 Y 1 B ARG   391 ? NH2 ? B ARG   391 NH2 
65 1 Y 1 B LYS   443 ? CG  ? B LYS   443 CG  
66 1 Y 1 B LYS   443 ? CD  ? B LYS   443 CD  
67 1 Y 1 B LYS   443 ? CE  ? B LYS   443 CE  
68 1 Y 1 B LYS   443 ? NZ  ? B LYS   443 NZ  
69 1 N 1 A A1ITD 503 ? C4  ? K A1ITD 1   C4  
70 1 N 1 A A1ITD 503 ? C1  ? K A1ITD 1   C1  
71 1 N 1 A A1ITD 503 ? C2  ? K A1ITD 1   C2  
72 1 N 1 A A1ITD 503 ? C3  ? K A1ITD 1   C3  
73 1 N 1 B A1ITD 502 ? C2  ? N A1ITD 1   C2  
74 1 N 1 B A1ITD 502 ? C3  ? N A1ITD 1   C3  
# 
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_4459 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20_4459 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .         4 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H8U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.565 
_cell.length_a_esd                 ? 
_cell.length_b                     90.565 
_cell.length_b_esd                 ? 
_cell.length_c                     290.432 
_cell.length_c_esd                 ? 
_cell.volume                       2382128.848 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9H8U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9H8U 
_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             2.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.33 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_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    '0.1 M NaAcetate pH 4.6, 20% w/v PEG1000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-03 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.965459 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965459 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H8U 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.00 
_reflns.d_resolution_low                               290.43 
_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                                     24425 
_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                           96.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.176 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       247786 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.167 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.00 
_reflns_shell.d_res_low                                     3.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           15607 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3287 
_reflns_shell.percent_possible_obs                          83.9 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.7 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.2 
_reflns_shell.pdbx_Rrim_I_all                               1.451 
_reflns_shell.pdbx_Rpim_I_all                               0.631 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.467 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.300 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               77.50 
_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                                 9H8U 
_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                            3.00 
_refine.ls_d_res_low                             76.85 
_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                     24347 
_refine.ls_number_reflns_R_free                  1232 
_refine.ls_number_reflns_R_work                  23115 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.63 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2101 
_refine.ls_R_factor_R_free                       0.2859 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2061 
_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                          1.35 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 32.5209 
_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                            0.5453 
_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                       3.00 
_refine_hist.d_res_low                        76.85 
_refine_hist.number_atoms_solvent             9 
_refine_hist.number_atoms_total               7491 
_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        7002 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         480 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0118  ? 7668  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.3291  ? 10502 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0679  ? 1254  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0095  ? 1321  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.0182 ? 1219  ? f_dihedral_angle_d ? ? 
# 
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' 3.00 3.12  . . 97  2099 80.00  . . . . 0.3586 . . . . . . . . . . . 0.4371 
'X-RAY DIFFRACTION' 3.12 3.26  . . 145 2330 90.79  . . . . 0.3237 . . . . . . . . . . . 0.4080 
'X-RAY DIFFRACTION' 3.26 3.43  . . 153 2558 99.49  . . . . 0.2843 . . . . . . . . . . . 0.3608 
'X-RAY DIFFRACTION' 3.43 3.65  . . 120 2633 99.96  . . . . 0.2413 . . . . . . . . . . . 0.3694 
'X-RAY DIFFRACTION' 3.65 3.93  . . 143 2629 99.96  . . . . 0.2241 . . . . . . . . . . . 0.3519 
'X-RAY DIFFRACTION' 3.93 4.33  . . 152 2622 100.00 . . . . 0.1860 . . . . . . . . . . . 0.2766 
'X-RAY DIFFRACTION' 4.33 4.95  . . 140 2660 100.00 . . . . 0.1543 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 4.95 6.24  . . 140 2709 99.96  . . . . 0.1856 . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 6.24 76.85 . . 142 2875 99.05  . . . . 0.1791 . . . . . . . . . . . 0.2210 
# 
_struct.entry_id                     9H8U 
_struct.title                        'FAD-dependent oxidase sorD with sorbicillin bound' 
_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        9H8U 
_struct_keywords.text            'Flavin, FAD, natural product, oxidase, sorbicillinoids, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
K N N 8 ? 
L N N 7 ? 
M N N 6 ? 
N N N 8 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 9 ? 
R N N 9 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SORD_PENRW 
_struct_ref.pdbx_db_accession          B6HNK6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQAASAFATCLLASVGGNSSAVAFPNQANYSTLVAPYNFDLLTTPSAIVWPQDTQQVAAAVKCAVDSDIKVQPKSGGHNY
GNYGSTTGELSVNLDNLQHFSMDETSWTARLGPGNRLGRVTELMYNNGGRHVPHGTTFTVGLGGHATVGGAGAASRMHGL
LLDYVEEVEVVLANSSIVRASKSHNEDLFFAVRGAASSVGIVTDFSIRTEPVPVSSVTYSYIWEGTDPAARAEVFLTWQS
LLAGGSLPQHMAYDLVATANSMILGGAYFGSQEDFEAFNLSSHFKVAPDVAHIKTYTNFFDFSAAASAQTKAAGIASPSH
FYAKSLVFNQQTLIPDDAAEEVFKYLATTKNGTDLYAVTFAALGGAVRDVSASETAFYHRDASYFMFSFGRTSGDLTDTT
VQFLDGLSEVLTSGQPDAYYGQYVGNVDPRQSTDKALTGYYGKNLHRLQQIKSAVDPNDVFHNQQSIPPLS
;
_struct_ref.pdbx_align_begin           1 
# 
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 9H8U A 1 ? 471 ? B6HNK6 1 ? 471 ? 1 471 
2 1 9H8U B 1 ? 471 ? B6HNK6 1 ? 471 ? 1 471 
# 
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 9H8U ASN A 103 ? UNP B6HNK6 ASP 103 conflict 103 1 
1 9H8U THR A 291 ? UNP B6HNK6 ALA 291 conflict 291 2 
1 9H8U PRO A 432 ? UNP B6HNK6 SER 432 conflict 432 3 
1 9H8U GLU A 435 ? UNP B6HNK6 LYS 435 conflict 435 4 
2 9H8U ASN B 103 ? UNP B6HNK6 ASP 103 conflict 103 5 
2 9H8U THR B 291 ? UNP B6HNK6 ALA 291 conflict 291 6 
2 9H8U PRO B 432 ? UNP B6HNK6 SER 432 conflict 432 7 
2 9H8U GLU B 435 ? UNP B6HNK6 LYS 435 conflict 435 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10200 ? 
1 MORE         66    ? 
1 'SSA (A^2)'  35830 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_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 5   ? VAL A 15  ? SER A 5   VAL A 15  1 ? 11 
HELX_P HELX_P2  AA2 ASN A 18  ? SER A 20  ? ASN A 18  SER A 20  5 ? 3  
HELX_P HELX_P3  AA3 ASN A 29  ? VAL A 34  ? ASN A 29  VAL A 34  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 53  ? SER A 67  ? ASP A 53  SER A 67  1 ? 15 
HELX_P HELX_P5  AA5 ASN A 82  ? THR A 86  ? ASN A 82  THR A 86  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 116 ? ASN A 127 ? ARG A 116 ASN A 127 1 ? 12 
HELX_P HELX_P7  AA7 ALA A 154 ? GLY A 159 ? ALA A 154 GLY A 159 1 ? 6  
HELX_P HELX_P8  AA8 LEU A 160 ? ASP A 163 ? LEU A 160 ASP A 163 5 ? 4  
HELX_P HELX_P9  AA9 ASN A 185 ? ALA A 196 ? ASN A 185 ALA A 196 1 ? 12 
HELX_P HELX_P10 AB1 SER A 197 ? VAL A 199 ? SER A 197 VAL A 199 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 227 ? GLY A 245 ? ASP A 227 GLY A 245 1 ? 19 
HELX_P HELX_P12 AB3 SER A 271 ? PHE A 278 ? SER A 271 PHE A 278 1 ? 8  
HELX_P HELX_P13 AB4 ASN A 298 ? GLY A 314 ? ASN A 298 GLY A 314 1 ? 17 
HELX_P HELX_P14 AB5 ASN A 329 ? LEU A 333 ? ASN A 329 LEU A 333 5 ? 5  
HELX_P HELX_P15 AB6 PRO A 335 ? THR A 349 ? PRO A 335 THR A 349 1 ? 15 
HELX_P HELX_P16 AB7 GLY A 364 ? VAL A 370 ? GLY A 364 VAL A 370 5 ? 7  
HELX_P HELX_P17 AB8 THR A 397 ? SER A 413 ? THR A 397 SER A 413 1 ? 17 
HELX_P HELX_P18 AB9 PRO A 432 ? GLY A 442 ? PRO A 432 GLY A 442 1 ? 11 
HELX_P HELX_P19 AC1 ASN A 444 ? ASP A 456 ? ASN A 444 ASP A 456 1 ? 13 
HELX_P HELX_P20 AC2 ALA B 6   ? VAL B 15  ? ALA B 6   VAL B 15  1 ? 10 
HELX_P HELX_P21 AC3 ASN B 18  ? SER B 20  ? ASN B 18  SER B 20  5 ? 3  
HELX_P HELX_P22 AC4 ASN B 29  ? ALA B 35  ? ASN B 29  ALA B 35  1 ? 7  
HELX_P HELX_P23 AC5 ASP B 53  ? SER B 67  ? ASP B 53  SER B 67  1 ? 15 
HELX_P HELX_P24 AC6 ASN B 82  ? THR B 86  ? ASN B 82  THR B 86  5 ? 5  
HELX_P HELX_P25 AC7 ARG B 116 ? ASN B 127 ? ARG B 116 ASN B 127 1 ? 12 
HELX_P HELX_P26 AC8 ALA B 154 ? GLY B 159 ? ALA B 154 GLY B 159 1 ? 6  
HELX_P HELX_P27 AC9 LEU B 160 ? ASP B 163 ? LEU B 160 ASP B 163 5 ? 4  
HELX_P HELX_P28 AD1 ASN B 185 ? GLY B 200 ? ASN B 185 GLY B 200 1 ? 16 
HELX_P HELX_P29 AD2 ASP B 227 ? GLY B 244 ? ASP B 227 GLY B 244 1 ? 18 
HELX_P HELX_P30 AD3 SER B 271 ? ASN B 279 ? SER B 271 ASN B 279 1 ? 9  
HELX_P HELX_P31 AD4 LEU B 280 ? PHE B 284 ? LEU B 280 PHE B 284 5 ? 5  
HELX_P HELX_P32 AD5 ASN B 298 ? GLY B 314 ? ASN B 298 GLY B 314 1 ? 17 
HELX_P HELX_P33 AD6 PRO B 335 ? THR B 349 ? PRO B 335 THR B 349 1 ? 15 
HELX_P HELX_P34 AD7 THR B 397 ? SER B 413 ? THR B 397 SER B 413 1 ? 17 
HELX_P HELX_P35 AD8 PRO B 432 ? TYR B 441 ? PRO B 432 TYR B 441 1 ? 10 
HELX_P HELX_P36 AD9 ASN B 444 ? ASP B 456 ? ASN B 444 ASP B 456 1 ? 13 
# 
_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 10  SG  ? ? ? 1_555 A CYS 63 SG ? ? A CYS 10  A CYS 63  1_555 ? ? ? ? ? ? ? 2.093 ? ?               
disulf2  disulf ?    ? B CYS 10  SG  ? ? ? 1_555 B CYS 63 SG ? ? B CYS 10  B CYS 63  1_555 ? ? ? ? ? ? ? 2.077 ? ?               
covale1  covale one  ? A ASN 18  ND2 ? ? ? 1_555 C NAG .  C1 ? ? A ASN 18  C NAG 1   1_555 ? ? ? ? ? ? ? 1.438 ? N-Glycosylation 
covale2  covale one  ? A ASN 29  ND2 ? ? ? 1_555 J NAG .  C1 ? ? A ASN 29  A NAG 502 1_555 ? ? ? ? ? ? ? 1.463 ? N-Glycosylation 
covale3  covale one  ? A ASN 174 ND2 ? ? ? 1_555 D NAG .  C1 ? ? A ASN 174 D NAG 1   1_555 ? ? ? ? ? ? ? 1.417 ? N-Glycosylation 
covale4  covale one  ? A ASN 279 ND2 ? ? ? 1_555 L NAG .  C1 ? ? A ASN 279 A NAG 504 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale5  covale one  ? A ASN 351 ND2 ? ? ? 1_555 E NAG .  C1 ? ? A ASN 351 E NAG 1   1_555 ? ? ? ? ? ? ? 1.462 ? N-Glycosylation 
covale6  covale one  ? B ASN 18  ND2 ? ? ? 1_555 F NAG .  C1 ? ? B ASN 18  F NAG 1   1_555 ? ? ? ? ? ? ? 1.428 ? N-Glycosylation 
covale7  covale one  ? B ASN 29  ND2 ? ? ? 1_555 P NAG .  C1 ? ? B ASN 29  B NAG 504 1_555 ? ? ? ? ? ? ? 1.463 ? N-Glycosylation 
covale8  covale one  ? B ASN 174 ND2 ? ? ? 1_555 G NAG .  C1 ? ? B ASN 174 G NAG 1   1_555 ? ? ? ? ? ? ? 1.471 ? N-Glycosylation 
covale9  covale one  ? B ASN 279 ND2 ? ? ? 1_555 O NAG .  C1 ? ? B ASN 279 B NAG 503 1_555 ? ? ? ? ? ? ? 1.459 ? N-Glycosylation 
covale10 covale one  ? B ASN 351 ND2 ? ? ? 1_555 H NAG .  C1 ? ? B ASN 351 H NAG 1   1_555 ? ? ? ? ? ? ? 1.460 ? N-Glycosylation 
covale11 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .  C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.460 ? ?               
covale12 covale both ? C NAG .   O4  ? ? ? 1_555 C MAN .  C1 ? ? C NAG 2   C MAN 3   1_555 ? ? ? ? ? ? ? 1.447 ? ?               
covale13 covale both ? C MAN .   O3  ? ? ? 1_555 C MAN .  C1 ? ? C MAN 3   C MAN 4   1_555 ? ? ? ? ? ? ? 1.463 ? ?               
covale14 covale both ? C MAN .   O3  ? ? ? 1_555 C MAN .  C1 ? ? C MAN 4   C MAN 5   1_555 ? ? ? ? ? ? ? 1.468 ? ?               
covale15 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .  C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.437 ? ?               
covale16 covale both ? D NAG .   O4  ? ? ? 1_555 D MAN .  C1 ? ? D NAG 2   D MAN 3   1_555 ? ? ? ? ? ? ? 1.442 ? ?               
covale17 covale both ? D MAN .   O3  ? ? ? 1_555 D MAN .  C1 ? ? D MAN 3   D MAN 4   1_555 ? ? ? ? ? ? ? 1.444 ? ?               
covale18 covale both ? D MAN .   O6  ? ? ? 1_555 D MAN .  C1 ? ? D MAN 3   D MAN 5   1_555 ? ? ? ? ? ? ? 1.442 ? ?               
covale19 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .  C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.456 ? ?               
covale20 covale both ? E NAG .   O4  ? ? ? 1_555 E MAN .  C1 ? ? E NAG 2   E MAN 3   1_555 ? ? ? ? ? ? ? 1.446 ? ?               
covale21 covale both ? E MAN .   O3  ? ? ? 1_555 E MAN .  C1 ? ? E MAN 3   E MAN 4   1_555 ? ? ? ? ? ? ? 1.469 ? ?               
covale22 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .  C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.441 ? ?               
covale23 covale both ? F NAG .   O4  ? ? ? 1_555 F MAN .  C1 ? ? F NAG 2   F MAN 3   1_555 ? ? ? ? ? ? ? 1.485 ? ?               
covale24 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .  C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.444 ? ?               
covale25 covale both ? G NAG .   O4  ? ? ? 1_555 G MAN .  C1 ? ? G NAG 2   G MAN 3   1_555 ? ? ? ? ? ? ? 1.456 ? ?               
covale26 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .  C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.449 ? ?               
covale27 covale both ? H NAG .   O4  ? ? ? 1_555 H MAN .  C1 ? ? H NAG 2   H MAN 3   1_555 ? ? ? ? ? ? ? 1.440 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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  NAG C .  ? ASN A 18  ? NAG C 1   ? 1_555 ASN A 18  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .  ? ASN A 174 ? NAG D 1   ? 1_555 ASN A 174 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .  ? ASN A 351 ? NAG E 1   ? 1_555 ASN A 351 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .  ? ASN B 18  ? NAG F 1   ? 1_555 ASN B 18  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G .  ? ASN B 174 ? NAG G 1   ? 1_555 ASN B 174 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG H .  ? ASN B 351 ? NAG H 1   ? 1_555 ASN B 351 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG J .  ? ASN A 29  ? NAG A 502 ? 1_555 ASN A 29  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG L .  ? ASN A 279 ? NAG A 504 ? 1_555 ASN A 279 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG O .  ? ASN B 279 ? NAG B 503 ? 1_555 ASN B 279 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG P .  ? ASN B 29  ? NAG B 504 ? 1_555 ASN B 29  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 CYS A 10 ? CYS A 63  ? CYS A 10  ? 1_555 CYS A 63  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS B 10 ? CYS B 63  ? CYS B 10  ? 1_555 CYS B 63  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 4 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 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 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 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 VAL A 22  ? ALA A 23  ? VAL A 22  ALA A 23  
AA1 2 ALA A 47  ? VAL A 49  ? ALA A 47  VAL A 49  
AA1 3 GLU A 89  ? ASN A 93  ? GLU A 89  ASN A 93  
AA1 4 LYS A 70  ? LYS A 74  ? LYS A 70  LYS A 74  
AA2 1 PHE A 100 ? SER A 101 ? PHE A 100 SER A 101 
AA2 2 THR A 108 ? LEU A 111 ? THR A 108 LEU A 111 
AA2 3 ILE A 201 ? ARG A 208 ? ILE A 201 ARG A 208 
AA2 4 VAL A 165 ? VAL A 171 ? VAL A 165 VAL A 171 
AA2 5 ILE A 177 ? SER A 181 ? ILE A 177 SER A 181 
AA3 1 ARG A 130 ? HIS A 131 ? ARG A 130 HIS A 131 
AA3 2 GLU A 210 ? PRO A 211 ? GLU A 210 PRO A 211 
AA4 1 VAL A 290 ? TYR A 296 ? VAL A 290 TYR A 296 
AA4 2 SER A 216 ? GLU A 224 ? SER A 216 GLU A 224 
AA4 3 SER A 261 ? PHE A 269 ? SER A 261 PHE A 269 
AA4 4 ASP A 254 ? ALA A 257 ? ASP A 254 ALA A 257 
AA4 5 LEU A 355 ? ALA A 362 ? LEU A 355 ALA A 362 
AA4 6 TYR A 384 ? ARG A 391 ? TYR A 384 ARG A 391 
AA4 7 PHE A 321 ? PHE A 328 ? PHE A 321 PHE A 328 
AA5 1 VAL B 22  ? ALA B 23  ? VAL B 22  ALA B 23  
AA5 2 ALA B 47  ? VAL B 49  ? ALA B 47  VAL B 49  
AA5 3 LEU B 90  ? ASN B 93  ? LEU B 90  ASN B 93  
AA5 4 VAL B 71  ? LYS B 74  ? VAL B 71  LYS B 74  
AA6 1 MET B 102 ? ASN B 103 ? MET B 102 ASN B 103 
AA6 2 THR B 108 ? LEU B 111 ? THR B 108 LEU B 111 
AA6 3 ILE B 201 ? ARG B 208 ? ILE B 201 ARG B 208 
AA6 4 VAL B 165 ? VAL B 171 ? VAL B 165 VAL B 171 
AA6 5 ILE B 177 ? ALA B 180 ? ILE B 177 ALA B 180 
AA7 1 ARG B 130 ? HIS B 131 ? ARG B 130 HIS B 131 
AA7 2 GLU B 210 ? PRO B 211 ? GLU B 210 PRO B 211 
AA8 1 SER B 216 ? VAL B 217 ? SER B 216 VAL B 217 
AA8 2 THR B 295 ? TYR B 296 ? THR B 295 TYR B 296 
AA9 1 SER B 220 ? ILE B 222 ? SER B 220 ILE B 222 
AA9 2 VAL B 290 ? HIS B 292 ? VAL B 290 HIS B 292 
AB1 1 SER B 261 ? ILE B 263 ? SER B 261 ILE B 263 
AB1 2 ASP B 254 ? THR B 258 ? ASP B 254 THR B 258 
AB1 3 LEU B 355 ? ALA B 362 ? LEU B 355 ALA B 362 
AB1 4 TYR B 384 ? ARG B 391 ? TYR B 384 ARG B 391 
AB1 5 PHE B 321 ? PHE B 328 ? PHE B 321 PHE B 328 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 23  ? N ALA A 23  O ILE A 48  ? O ILE A 48  
AA1 2 3 N VAL A 49  ? N VAL A 49  O ASN A 93  ? O ASN A 93  
AA1 3 4 O LEU A 90  ? O LEU A 90  N LYS A 70  ? N LYS A 70  
AA2 1 2 N SER A 101 ? N SER A 101 O ARG A 110 ? O ARG A 110 
AA2 2 3 N LEU A 111 ? N LEU A 111 O PHE A 205 ? O PHE A 205 
AA2 3 4 O SER A 206 ? O SER A 206 N GLU A 167 ? N GLU A 167 
AA2 4 5 N VAL A 170 ? N VAL A 170 O VAL A 178 ? O VAL A 178 
AA3 1 2 N HIS A 131 ? N HIS A 131 O GLU A 210 ? O GLU A 210 
AA4 1 2 O TYR A 296 ? O TYR A 296 N SER A 216 ? N SER A 216 
AA4 2 3 N TYR A 221 ? N TYR A 221 O LEU A 264 ? O LEU A 264 
AA4 3 4 O GLY A 265 ? O GLY A 265 N ASP A 254 ? N ASP A 254 
AA4 4 5 N ALA A 257 ? N ALA A 257 O VAL A 358 ? O VAL A 358 
AA4 5 6 N ALA A 361 ? N ALA A 361 O PHE A 385 ? O PHE A 385 
AA4 6 7 O GLY A 390 ? O GLY A 390 N TYR A 322 ? N TYR A 322 
AA5 1 2 N ALA B 23  ? N ALA B 23  O ILE B 48  ? O ILE B 48  
AA5 2 3 N VAL B 49  ? N VAL B 49  O SER B 91  ? O SER B 91  
AA5 3 4 O LEU B 90  ? O LEU B 90  N GLN B 72  ? N GLN B 72  
AA6 1 2 N ASN B 103 ? N ASN B 103 O THR B 108 ? O THR B 108 
AA6 2 3 N ALA B 109 ? N ALA B 109 O ILE B 207 ? O ILE B 207 
AA6 3 4 O SER B 206 ? O SER B 206 N GLU B 166 ? N GLU B 166 
AA6 4 5 N VAL B 170 ? N VAL B 170 O VAL B 178 ? O VAL B 178 
AA7 1 2 N HIS B 131 ? N HIS B 131 O GLU B 210 ? O GLU B 210 
AA8 1 2 N SER B 216 ? N SER B 216 O TYR B 296 ? O TYR B 296 
AA9 1 2 N SER B 220 ? N SER B 220 O HIS B 292 ? O HIS B 292 
AB1 1 2 O ILE B 263 ? O ILE B 263 N VAL B 256 ? N VAL B 256 
AB1 2 3 N LEU B 255 ? N LEU B 255 O PHE B 360 ? O PHE B 360 
AB1 3 4 N ALA B 357 ? N ALA B 357 O PHE B 389 ? O PHE B 389 
AB1 4 5 O SER B 388 ? O SER B 388 N LYS B 324 ? N LYS B 324 
# 
_pdbx_entry_details.entry_id                   9H8U 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 ND1 A HIS 78  ? ? C8M A FAD 501 ? ? 1.44 
2 1 ND1 B HIS 78  ? ? C8M B FAD 501 ? ? 1.45 
3 1 O3  E MAN 3   ? ? O5  E MAN 4   ? ? 1.88 
4 1 O   B LYS 344 ? ? OG1 B THR 348 ? ? 1.91 
5 1 NZ  B LYS 70  ? ? O   B ASP 459 ? ? 2.06 
6 1 NH2 B ARG 231 ? ? O   B THR 258 ? ? 2.15 
# 
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 18  ? ? -42.16  98.56   
2  1 VAL A 22  ? ? -170.60 146.92  
3  1 LEU A 41  ? ? -92.30  55.79   
4  1 ASP A 68  ? ? 39.36   56.41   
5  1 SER A 75  ? ? -99.99  -74.61  
6  1 THR A 86  ? ? -21.49  123.17  
7  1 ALA A 195 ? ? -146.80 26.50   
8  1 TYR A 253 ? ? -159.53 84.65   
9  1 THR A 258 ? ? -103.62 -163.35 
10 1 HIS A 283 ? ? -45.87  -12.34  
11 1 THR A 297 ? ? -94.42  -67.52  
12 1 ASN A 298 ? ? -37.85  110.74  
13 1 LEU A 333 ? ? -44.06  159.93  
14 1 LEU A 363 ? ? -157.23 41.78   
15 1 ASP A 369 ? ? -67.64  4.79    
16 1 HIS A 379 ? ? -82.95  45.12   
17 1 SER A 413 ? ? -69.77  6.37    
18 1 GLN A 415 ? ? -170.32 43.51   
19 1 ASN A 426 ? ? -110.92 65.92   
20 1 PRO A 429 ? ? -79.00  20.98   
21 1 ASP A 456 ? ? -165.35 80.18   
22 1 ASP A 459 ? ? -104.03 52.66   
23 1 ASN B 18  ? ? -61.47  99.23   
24 1 ALA B 35  ? ? 62.65   60.71   
25 1 ASP B 40  ? ? -102.44 -61.95  
26 1 LEU B 41  ? ? -56.29  56.21   
27 1 LEU B 42  ? ? -57.45  179.80  
28 1 SER B 75  ? ? -124.51 -96.14  
29 1 THR B 86  ? ? -32.76  137.55  
30 1 LEU B 97  ? ? -112.14 73.90   
31 1 ASN B 127 ? ? -96.37  53.85   
32 1 HIS B 145 ? ? -119.33 -78.31  
33 1 ALA B 146 ? ? -45.06  -12.82  
34 1 GLU B 166 ? ? -95.71  -66.67  
35 1 HIS B 184 ? ? 179.78  136.25  
36 1 ASN B 185 ? ? 27.03   46.52   
37 1 ALA B 195 ? ? -151.58 47.86   
38 1 MET B 251 ? ? -174.37 119.52  
39 1 TYR B 253 ? ? -152.11 87.89   
40 1 LEU B 255 ? ? -166.83 113.28  
41 1 THR B 258 ? ? -123.33 -166.20 
42 1 ASN B 260 ? ? -162.15 71.10   
43 1 SER B 261 ? ? 171.06  151.27  
44 1 LYS B 285 ? ? -79.09  -83.88  
45 1 ILE B 293 ? ? -156.58 88.89   
46 1 ALA B 316 ? ? -92.48  37.40   
47 1 GLN B 330 ? ? -39.48  -35.48  
48 1 LEU B 333 ? ? -40.83  108.07  
49 1 ALA B 339 ? ? -37.02  -39.52  
50 1 LYS B 350 ? ? -57.57  88.00   
51 1 LEU B 363 ? ? -137.62 -138.80 
52 1 ARG B 368 ? ? -105.66 44.88   
53 1 ASP B 381 ? ? -90.63  52.83   
54 1 ASP B 395 ? ? -49.63  151.44  
55 1 VAL B 410 ? ? -49.15  -19.97  
56 1 PRO B 416 ? ? -49.82  -13.61  
57 1 ASP B 456 ? ? -170.28 51.99   
58 1 GLN B 464 ? ? -34.61  -21.28  
59 1 GLN B 465 ? ? -144.79 31.98   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A GLN 2 ? A GLN 2 
3 1 Y 1 A ALA 3 ? A ALA 3 
4 1 Y 1 A ALA 4 ? A ALA 4 
5 1 Y 1 B MET 1 ? B MET 1 
6 1 Y 1 B GLN 2 ? B GLN 2 
7 1 Y 1 B ALA 3 ? B ALA 3 
8 1 Y 1 B ALA 4 ? B ALA 4 
# 
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 
A1ITD C4     C N N 1   
A1ITD C14    C Y N 2   
A1ITD C5     C N N 3   
A1ITD C6     C N N 4   
A1ITD C11    C Y N 5   
A1ITD C7     C Y N 6   
A1ITD C8     C Y N 7   
A1ITD C9     C Y N 8   
A1ITD C10    C N N 9   
A1ITD C12    C Y N 10  
A1ITD C13    C N N 11  
A1ITD O1     O N N 12  
A1ITD O2     O N N 13  
A1ITD O3     O N N 14  
A1ITD H1     H N N 15  
A1ITD H3     H N N 16  
A1ITD H4     H N N 17  
A1ITD H5     H N N 18  
A1ITD H6     H N N 19  
A1ITD H7     H N N 20  
A1ITD H8     H N N 21  
A1ITD H9     H N N 22  
A1ITD H10    H N N 23  
A1ITD H11    H N N 24  
A1ITD H12    H N N 25  
A1ITD C1     C N N 26  
A1ITD C2     C N N 27  
A1ITD C3     C N N 28  
A1ITD H2     H N N 29  
A1ITD H13    H N N 30  
A1ITD H14    H N N 31  
A1ITD H15    H N N 32  
A1ITD H16    H N N 33  
ALA   N      N N N 34  
ALA   CA     C N S 35  
ALA   C      C N N 36  
ALA   O      O N N 37  
ALA   CB     C N N 38  
ALA   OXT    O N N 39  
ALA   H      H N N 40  
ALA   H2     H N N 41  
ALA   HA     H N N 42  
ALA   HB1    H N N 43  
ALA   HB2    H N N 44  
ALA   HB3    H N N 45  
ALA   HXT    H N N 46  
ARG   N      N N N 47  
ARG   CA     C N S 48  
ARG   C      C N N 49  
ARG   O      O N N 50  
ARG   CB     C N N 51  
ARG   CG     C N N 52  
ARG   CD     C N N 53  
ARG   NE     N N N 54  
ARG   CZ     C N N 55  
ARG   NH1    N N N 56  
ARG   NH2    N N N 57  
ARG   OXT    O N N 58  
ARG   H      H N N 59  
ARG   H2     H N N 60  
ARG   HA     H N N 61  
ARG   HB2    H N N 62  
ARG   HB3    H N N 63  
ARG   HG2    H N N 64  
ARG   HG3    H N N 65  
ARG   HD2    H N N 66  
ARG   HD3    H N N 67  
ARG   HE     H N N 68  
ARG   HH11   H N N 69  
ARG   HH12   H N N 70  
ARG   HH21   H N N 71  
ARG   HH22   H N N 72  
ARG   HXT    H N N 73  
ASN   N      N N N 74  
ASN   CA     C N S 75  
ASN   C      C N N 76  
ASN   O      O N N 77  
ASN   CB     C N N 78  
ASN   CG     C N N 79  
ASN   OD1    O N N 80  
ASN   ND2    N N N 81  
ASN   OXT    O N N 82  
ASN   H      H N N 83  
ASN   H2     H N N 84  
ASN   HA     H N N 85  
ASN   HB2    H N N 86  
ASN   HB3    H N N 87  
ASN   HD21   H N N 88  
ASN   HD22   H N N 89  
ASN   HXT    H N N 90  
ASP   N      N N N 91  
ASP   CA     C N S 92  
ASP   C      C N N 93  
ASP   O      O N N 94  
ASP   CB     C N N 95  
ASP   CG     C N N 96  
ASP   OD1    O N N 97  
ASP   OD2    O N N 98  
ASP   OXT    O N N 99  
ASP   H      H N N 100 
ASP   H2     H N N 101 
ASP   HA     H N N 102 
ASP   HB2    H N N 103 
ASP   HB3    H N N 104 
ASP   HD2    H N N 105 
ASP   HXT    H N N 106 
CYS   N      N N N 107 
CYS   CA     C N R 108 
CYS   C      C N N 109 
CYS   O      O N N 110 
CYS   CB     C N N 111 
CYS   SG     S N N 112 
CYS   OXT    O N N 113 
CYS   H      H N N 114 
CYS   H2     H N N 115 
CYS   HA     H N N 116 
CYS   HB2    H N N 117 
CYS   HB3    H N N 118 
CYS   HG     H N N 119 
CYS   HXT    H N N 120 
FAD   PA     P N R 121 
FAD   O1A    O N N 122 
FAD   O2A    O N N 123 
FAD   O5B    O N N 124 
FAD   C5B    C N N 125 
FAD   C4B    C N R 126 
FAD   O4B    O N N 127 
FAD   C3B    C N S 128 
FAD   O3B    O N N 129 
FAD   C2B    C N R 130 
FAD   O2B    O N N 131 
FAD   C1B    C N R 132 
FAD   N9A    N Y N 133 
FAD   C8A    C Y N 134 
FAD   N7A    N Y N 135 
FAD   C5A    C Y N 136 
FAD   C6A    C Y N 137 
FAD   N6A    N N N 138 
FAD   N1A    N Y N 139 
FAD   C2A    C Y N 140 
FAD   N3A    N Y N 141 
FAD   C4A    C Y N 142 
FAD   N1     N N N 143 
FAD   C2     C N N 144 
FAD   O2     O N N 145 
FAD   N3     N N N 146 
FAD   C4     C N N 147 
FAD   O4     O N N 148 
FAD   C4X    C N N 149 
FAD   N5     N N N 150 
FAD   C5X    C Y N 151 
FAD   C6     C Y N 152 
FAD   C7     C Y N 153 
FAD   C7M    C N N 154 
FAD   C8     C Y N 155 
FAD   C8M    C N N 156 
FAD   C9     C Y N 157 
FAD   C9A    C Y N 158 
FAD   N10    N N N 159 
FAD   C10    C N N 160 
FAD   "C1'"  C N N 161 
FAD   "C2'"  C N S 162 
FAD   "O2'"  O N N 163 
FAD   "C3'"  C N S 164 
FAD   "O3'"  O N N 165 
FAD   "C4'"  C N R 166 
FAD   "O4'"  O N N 167 
FAD   "C5'"  C N N 168 
FAD   "O5'"  O N N 169 
FAD   P      P N R 170 
FAD   O1P    O N N 171 
FAD   O2P    O N N 172 
FAD   O3P    O N N 173 
FAD   HOA2   H N N 174 
FAD   H51A   H N N 175 
FAD   H52A   H N N 176 
FAD   H4B    H N N 177 
FAD   H3B    H N N 178 
FAD   HO3A   H N N 179 
FAD   H2B    H N N 180 
FAD   HO2A   H N N 181 
FAD   H1B    H N N 182 
FAD   H8A    H N N 183 
FAD   H61A   H N N 184 
FAD   H62A   H N N 185 
FAD   H2A    H N N 186 
FAD   HN3    H N N 187 
FAD   H6     H N N 188 
FAD   HM71   H N N 189 
FAD   HM72   H N N 190 
FAD   HM73   H N N 191 
FAD   HM81   H N N 192 
FAD   HM82   H N N 193 
FAD   HM83   H N N 194 
FAD   H9     H N N 195 
FAD   "H1'1" H N N 196 
FAD   "H1'2" H N N 197 
FAD   "H2'"  H N N 198 
FAD   "HO2'" H N N 199 
FAD   "H3'"  H N N 200 
FAD   "HO3'" H N N 201 
FAD   "H4'"  H N N 202 
FAD   "HO4'" H N N 203 
FAD   "H5'1" H N N 204 
FAD   "H5'2" H N N 205 
FAD   HOP2   H N N 206 
GLN   N      N N N 207 
GLN   CA     C N S 208 
GLN   C      C N N 209 
GLN   O      O N N 210 
GLN   CB     C N N 211 
GLN   CG     C N N 212 
GLN   CD     C N N 213 
GLN   OE1    O N N 214 
GLN   NE2    N N N 215 
GLN   OXT    O N N 216 
GLN   H      H N N 217 
GLN   H2     H N N 218 
GLN   HA     H N N 219 
GLN   HB2    H N N 220 
GLN   HB3    H N N 221 
GLN   HG2    H N N 222 
GLN   HG3    H N N 223 
GLN   HE21   H N N 224 
GLN   HE22   H N N 225 
GLN   HXT    H N N 226 
GLU   N      N N N 227 
GLU   CA     C N S 228 
GLU   C      C N N 229 
GLU   O      O N N 230 
GLU   CB     C N N 231 
GLU   CG     C N N 232 
GLU   CD     C N N 233 
GLU   OE1    O N N 234 
GLU   OE2    O N N 235 
GLU   OXT    O N N 236 
GLU   H      H N N 237 
GLU   H2     H N N 238 
GLU   HA     H N N 239 
GLU   HB2    H N N 240 
GLU   HB3    H N N 241 
GLU   HG2    H N N 242 
GLU   HG3    H N N 243 
GLU   HE2    H N N 244 
GLU   HXT    H N N 245 
GLY   N      N N N 246 
GLY   CA     C N N 247 
GLY   C      C N N 248 
GLY   O      O N N 249 
GLY   OXT    O N N 250 
GLY   H      H N N 251 
GLY   H2     H N N 252 
GLY   HA2    H N N 253 
GLY   HA3    H N N 254 
GLY   HXT    H N N 255 
HIS   N      N N N 256 
HIS   CA     C N S 257 
HIS   C      C N N 258 
HIS   O      O N N 259 
HIS   CB     C N N 260 
HIS   CG     C Y N 261 
HIS   ND1    N Y N 262 
HIS   CD2    C Y N 263 
HIS   CE1    C Y N 264 
HIS   NE2    N Y N 265 
HIS   OXT    O N N 266 
HIS   H      H N N 267 
HIS   H2     H N N 268 
HIS   HA     H N N 269 
HIS   HB2    H N N 270 
HIS   HB3    H N N 271 
HIS   HD1    H N N 272 
HIS   HD2    H N N 273 
HIS   HE1    H N N 274 
HIS   HE2    H N N 275 
HIS   HXT    H N N 276 
HOH   O      O N N 277 
HOH   H1     H N N 278 
HOH   H2     H N N 279 
ILE   N      N N N 280 
ILE   CA     C N S 281 
ILE   C      C N N 282 
ILE   O      O N N 283 
ILE   CB     C N S 284 
ILE   CG1    C N N 285 
ILE   CG2    C N N 286 
ILE   CD1    C N N 287 
ILE   OXT    O N N 288 
ILE   H      H N N 289 
ILE   H2     H N N 290 
ILE   HA     H N N 291 
ILE   HB     H N N 292 
ILE   HG12   H N N 293 
ILE   HG13   H N N 294 
ILE   HG21   H N N 295 
ILE   HG22   H N N 296 
ILE   HG23   H N N 297 
ILE   HD11   H N N 298 
ILE   HD12   H N N 299 
ILE   HD13   H N N 300 
ILE   HXT    H N N 301 
LEU   N      N N N 302 
LEU   CA     C N S 303 
LEU   C      C N N 304 
LEU   O      O N N 305 
LEU   CB     C N N 306 
LEU   CG     C N N 307 
LEU   CD1    C N N 308 
LEU   CD2    C N N 309 
LEU   OXT    O N N 310 
LEU   H      H N N 311 
LEU   H2     H N N 312 
LEU   HA     H N N 313 
LEU   HB2    H N N 314 
LEU   HB3    H N N 315 
LEU   HG     H N N 316 
LEU   HD11   H N N 317 
LEU   HD12   H N N 318 
LEU   HD13   H N N 319 
LEU   HD21   H N N 320 
LEU   HD22   H N N 321 
LEU   HD23   H N N 322 
LEU   HXT    H N N 323 
LYS   N      N N N 324 
LYS   CA     C N S 325 
LYS   C      C N N 326 
LYS   O      O N N 327 
LYS   CB     C N N 328 
LYS   CG     C N N 329 
LYS   CD     C N N 330 
LYS   CE     C N N 331 
LYS   NZ     N N N 332 
LYS   OXT    O N N 333 
LYS   H      H N N 334 
LYS   H2     H N N 335 
LYS   HA     H N N 336 
LYS   HB2    H N N 337 
LYS   HB3    H N N 338 
LYS   HG2    H N N 339 
LYS   HG3    H N N 340 
LYS   HD2    H N N 341 
LYS   HD3    H N N 342 
LYS   HE2    H N N 343 
LYS   HE3    H N N 344 
LYS   HZ1    H N N 345 
LYS   HZ2    H N N 346 
LYS   HZ3    H N N 347 
LYS   HXT    H N N 348 
MAN   C1     C N S 349 
MAN   C2     C N S 350 
MAN   C3     C N S 351 
MAN   C4     C N S 352 
MAN   C5     C N R 353 
MAN   C6     C N N 354 
MAN   O1     O N N 355 
MAN   O2     O N N 356 
MAN   O3     O N N 357 
MAN   O4     O N N 358 
MAN   O5     O N N 359 
MAN   O6     O N N 360 
MAN   H1     H N N 361 
MAN   H2     H N N 362 
MAN   H3     H N N 363 
MAN   H4     H N N 364 
MAN   H5     H N N 365 
MAN   H61    H N N 366 
MAN   H62    H N N 367 
MAN   HO1    H N N 368 
MAN   HO2    H N N 369 
MAN   HO3    H N N 370 
MAN   HO4    H N N 371 
MAN   HO6    H N N 372 
MET   N      N N N 373 
MET   CA     C N S 374 
MET   C      C N N 375 
MET   O      O N N 376 
MET   CB     C N N 377 
MET   CG     C N N 378 
MET   SD     S N N 379 
MET   CE     C N N 380 
MET   OXT    O N N 381 
MET   H      H N N 382 
MET   H2     H N N 383 
MET   HA     H N N 384 
MET   HB2    H N N 385 
MET   HB3    H N N 386 
MET   HG2    H N N 387 
MET   HG3    H N N 388 
MET   HE1    H N N 389 
MET   HE2    H N N 390 
MET   HE3    H N N 391 
MET   HXT    H N N 392 
NAG   C1     C N R 393 
NAG   C2     C N R 394 
NAG   C3     C N R 395 
NAG   C4     C N S 396 
NAG   C5     C N R 397 
NAG   C6     C N N 398 
NAG   C7     C N N 399 
NAG   C8     C N N 400 
NAG   N2     N N N 401 
NAG   O1     O N N 402 
NAG   O3     O N N 403 
NAG   O4     O N N 404 
NAG   O5     O N N 405 
NAG   O6     O N N 406 
NAG   O7     O N N 407 
NAG   H1     H N N 408 
NAG   H2     H N N 409 
NAG   H3     H N N 410 
NAG   H4     H N N 411 
NAG   H5     H N N 412 
NAG   H61    H N N 413 
NAG   H62    H N N 414 
NAG   H81    H N N 415 
NAG   H82    H N N 416 
NAG   H83    H N N 417 
NAG   HN2    H N N 418 
NAG   HO1    H N N 419 
NAG   HO3    H N N 420 
NAG   HO4    H N N 421 
NAG   HO6    H N N 422 
PHE   N      N N N 423 
PHE   CA     C N S 424 
PHE   C      C N N 425 
PHE   O      O N N 426 
PHE   CB     C N N 427 
PHE   CG     C Y N 428 
PHE   CD1    C Y N 429 
PHE   CD2    C Y N 430 
PHE   CE1    C Y N 431 
PHE   CE2    C Y N 432 
PHE   CZ     C Y N 433 
PHE   OXT    O N N 434 
PHE   H      H N N 435 
PHE   H2     H N N 436 
PHE   HA     H N N 437 
PHE   HB2    H N N 438 
PHE   HB3    H N N 439 
PHE   HD1    H N N 440 
PHE   HD2    H N N 441 
PHE   HE1    H N N 442 
PHE   HE2    H N N 443 
PHE   HZ     H N N 444 
PHE   HXT    H N N 445 
PRO   N      N N N 446 
PRO   CA     C N S 447 
PRO   C      C N N 448 
PRO   O      O N N 449 
PRO   CB     C N N 450 
PRO   CG     C N N 451 
PRO   CD     C N N 452 
PRO   OXT    O N N 453 
PRO   H      H N N 454 
PRO   HA     H N N 455 
PRO   HB2    H N N 456 
PRO   HB3    H N N 457 
PRO   HG2    H N N 458 
PRO   HG3    H N N 459 
PRO   HD2    H N N 460 
PRO   HD3    H N N 461 
PRO   HXT    H N N 462 
SER   N      N N N 463 
SER   CA     C N S 464 
SER   C      C N N 465 
SER   O      O N N 466 
SER   CB     C N N 467 
SER   OG     O N N 468 
SER   OXT    O N N 469 
SER   H      H N N 470 
SER   H2     H N N 471 
SER   HA     H N N 472 
SER   HB2    H N N 473 
SER   HB3    H N N 474 
SER   HG     H N N 475 
SER   HXT    H N N 476 
THR   N      N N N 477 
THR   CA     C N S 478 
THR   C      C N N 479 
THR   O      O N N 480 
THR   CB     C N R 481 
THR   OG1    O N N 482 
THR   CG2    C N N 483 
THR   OXT    O N N 484 
THR   H      H N N 485 
THR   H2     H N N 486 
THR   HA     H N N 487 
THR   HB     H N N 488 
THR   HG1    H N N 489 
THR   HG21   H N N 490 
THR   HG22   H N N 491 
THR   HG23   H N N 492 
THR   HXT    H N N 493 
TRP   N      N N N 494 
TRP   CA     C N S 495 
TRP   C      C N N 496 
TRP   O      O N N 497 
TRP   CB     C N N 498 
TRP   CG     C Y N 499 
TRP   CD1    C Y N 500 
TRP   CD2    C Y N 501 
TRP   NE1    N Y N 502 
TRP   CE2    C Y N 503 
TRP   CE3    C Y N 504 
TRP   CZ2    C Y N 505 
TRP   CZ3    C Y N 506 
TRP   CH2    C Y N 507 
TRP   OXT    O N N 508 
TRP   H      H N N 509 
TRP   H2     H N N 510 
TRP   HA     H N N 511 
TRP   HB2    H N N 512 
TRP   HB3    H N N 513 
TRP   HD1    H N N 514 
TRP   HE1    H N N 515 
TRP   HE3    H N N 516 
TRP   HZ2    H N N 517 
TRP   HZ3    H N N 518 
TRP   HH2    H N N 519 
TRP   HXT    H N N 520 
TYR   N      N N N 521 
TYR   CA     C N S 522 
TYR   C      C N N 523 
TYR   O      O N N 524 
TYR   CB     C N N 525 
TYR   CG     C Y N 526 
TYR   CD1    C Y N 527 
TYR   CD2    C Y N 528 
TYR   CE1    C Y N 529 
TYR   CE2    C Y N 530 
TYR   CZ     C Y N 531 
TYR   OH     O N N 532 
TYR   OXT    O N N 533 
TYR   H      H N N 534 
TYR   H2     H N N 535 
TYR   HA     H N N 536 
TYR   HB2    H N N 537 
TYR   HB3    H N N 538 
TYR   HD1    H N N 539 
TYR   HD2    H N N 540 
TYR   HE1    H N N 541 
TYR   HE2    H N N 542 
TYR   HH     H N N 543 
TYR   HXT    H N N 544 
VAL   N      N N N 545 
VAL   CA     C N S 546 
VAL   C      C N N 547 
VAL   O      O N N 548 
VAL   CB     C N N 549 
VAL   CG1    C N N 550 
VAL   CG2    C N N 551 
VAL   OXT    O N N 552 
VAL   H      H N N 553 
VAL   H2     H N N 554 
VAL   HA     H N N 555 
VAL   HB     H N N 556 
VAL   HG11   H N N 557 
VAL   HG12   H N N 558 
VAL   HG13   H N N 559 
VAL   HG21   H N N 560 
VAL   HG22   H N N 561 
VAL   HG23   H N N 562 
VAL   HXT    H N N 563 
# 
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 
A1ITD O1    C6     doub N N 1   
A1ITD C10   C9     sing N N 2   
A1ITD C8    C9     doub Y N 3   
A1ITD C8    C7     sing Y N 4   
A1ITD C6    C7     sing N N 5   
A1ITD C6    C5     sing N N 6   
A1ITD C9    C11    sing Y N 7   
A1ITD C4    C5     doub N E 8   
A1ITD C7    C14    doub Y N 9   
A1ITD C11   O2     sing N N 10  
A1ITD C11   C12    doub Y N 11  
A1ITD C14   C12    sing Y N 12  
A1ITD C14   O3     sing N N 13  
A1ITD C12   C13    sing N N 14  
A1ITD C4    H1     sing N N 15  
A1ITD C5    H3     sing N N 16  
A1ITD C8    H4     sing N N 17  
A1ITD C10   H5     sing N N 18  
A1ITD C10   H6     sing N N 19  
A1ITD C10   H7     sing N N 20  
A1ITD C13   H8     sing N N 21  
A1ITD C13   H9     sing N N 22  
A1ITD C13   H10    sing N N 23  
A1ITD O2    H11    sing N N 24  
A1ITD O3    H12    sing N N 25  
A1ITD C4    C1     sing N N 26  
A1ITD C1    C2     doub N N 27  
A1ITD C2    C3     sing N N 28  
A1ITD C1    H2     sing N N 29  
A1ITD C2    H13    sing N N 30  
A1ITD C3    H14    sing N N 31  
A1ITD C3    H15    sing N N 32  
A1ITD C3    H16    sing N N 33  
ALA   N     CA     sing N N 34  
ALA   N     H      sing N N 35  
ALA   N     H2     sing N N 36  
ALA   CA    C      sing N N 37  
ALA   CA    CB     sing N N 38  
ALA   CA    HA     sing N N 39  
ALA   C     O      doub N N 40  
ALA   C     OXT    sing N N 41  
ALA   CB    HB1    sing N N 42  
ALA   CB    HB2    sing N N 43  
ALA   CB    HB3    sing N N 44  
ALA   OXT   HXT    sing N N 45  
ARG   N     CA     sing N N 46  
ARG   N     H      sing N N 47  
ARG   N     H2     sing N N 48  
ARG   CA    C      sing N N 49  
ARG   CA    CB     sing N N 50  
ARG   CA    HA     sing N N 51  
ARG   C     O      doub N N 52  
ARG   C     OXT    sing N N 53  
ARG   CB    CG     sing N N 54  
ARG   CB    HB2    sing N N 55  
ARG   CB    HB3    sing N N 56  
ARG   CG    CD     sing N N 57  
ARG   CG    HG2    sing N N 58  
ARG   CG    HG3    sing N N 59  
ARG   CD    NE     sing N N 60  
ARG   CD    HD2    sing N N 61  
ARG   CD    HD3    sing N N 62  
ARG   NE    CZ     sing N N 63  
ARG   NE    HE     sing N N 64  
ARG   CZ    NH1    sing N N 65  
ARG   CZ    NH2    doub N N 66  
ARG   NH1   HH11   sing N N 67  
ARG   NH1   HH12   sing N N 68  
ARG   NH2   HH21   sing N N 69  
ARG   NH2   HH22   sing N N 70  
ARG   OXT   HXT    sing N N 71  
ASN   N     CA     sing N N 72  
ASN   N     H      sing N N 73  
ASN   N     H2     sing N N 74  
ASN   CA    C      sing N N 75  
ASN   CA    CB     sing N N 76  
ASN   CA    HA     sing N N 77  
ASN   C     O      doub N N 78  
ASN   C     OXT    sing N N 79  
ASN   CB    CG     sing N N 80  
ASN   CB    HB2    sing N N 81  
ASN   CB    HB3    sing N N 82  
ASN   CG    OD1    doub N N 83  
ASN   CG    ND2    sing N N 84  
ASN   ND2   HD21   sing N N 85  
ASN   ND2   HD22   sing N N 86  
ASN   OXT   HXT    sing N N 87  
ASP   N     CA     sing N N 88  
ASP   N     H      sing N N 89  
ASP   N     H2     sing N N 90  
ASP   CA    C      sing N N 91  
ASP   CA    CB     sing N N 92  
ASP   CA    HA     sing N N 93  
ASP   C     O      doub N N 94  
ASP   C     OXT    sing N N 95  
ASP   CB    CG     sing N N 96  
ASP   CB    HB2    sing N N 97  
ASP   CB    HB3    sing N N 98  
ASP   CG    OD1    doub N N 99  
ASP   CG    OD2    sing N N 100 
ASP   OD2   HD2    sing N N 101 
ASP   OXT   HXT    sing N N 102 
CYS   N     CA     sing N N 103 
CYS   N     H      sing N N 104 
CYS   N     H2     sing N N 105 
CYS   CA    C      sing N N 106 
CYS   CA    CB     sing N N 107 
CYS   CA    HA     sing N N 108 
CYS   C     O      doub N N 109 
CYS   C     OXT    sing N N 110 
CYS   CB    SG     sing N N 111 
CYS   CB    HB2    sing N N 112 
CYS   CB    HB3    sing N N 113 
CYS   SG    HG     sing N N 114 
CYS   OXT   HXT    sing N N 115 
FAD   PA    O1A    doub N N 116 
FAD   PA    O2A    sing N N 117 
FAD   PA    O5B    sing N N 118 
FAD   PA    O3P    sing N N 119 
FAD   O2A   HOA2   sing N N 120 
FAD   O5B   C5B    sing N N 121 
FAD   C5B   C4B    sing N N 122 
FAD   C5B   H51A   sing N N 123 
FAD   C5B   H52A   sing N N 124 
FAD   C4B   O4B    sing N N 125 
FAD   C4B   C3B    sing N N 126 
FAD   C4B   H4B    sing N N 127 
FAD   O4B   C1B    sing N N 128 
FAD   C3B   O3B    sing N N 129 
FAD   C3B   C2B    sing N N 130 
FAD   C3B   H3B    sing N N 131 
FAD   O3B   HO3A   sing N N 132 
FAD   C2B   O2B    sing N N 133 
FAD   C2B   C1B    sing N N 134 
FAD   C2B   H2B    sing N N 135 
FAD   O2B   HO2A   sing N N 136 
FAD   C1B   N9A    sing N N 137 
FAD   C1B   H1B    sing N N 138 
FAD   N9A   C8A    sing Y N 139 
FAD   N9A   C4A    sing Y N 140 
FAD   C8A   N7A    doub Y N 141 
FAD   C8A   H8A    sing N N 142 
FAD   N7A   C5A    sing Y N 143 
FAD   C5A   C6A    sing Y N 144 
FAD   C5A   C4A    doub Y N 145 
FAD   C6A   N6A    sing N N 146 
FAD   C6A   N1A    doub Y N 147 
FAD   N6A   H61A   sing N N 148 
FAD   N6A   H62A   sing N N 149 
FAD   N1A   C2A    sing Y N 150 
FAD   C2A   N3A    doub Y N 151 
FAD   C2A   H2A    sing N N 152 
FAD   N3A   C4A    sing Y N 153 
FAD   N1    C2     sing N N 154 
FAD   N1    C10    doub N N 155 
FAD   C2    O2     doub N N 156 
FAD   C2    N3     sing N N 157 
FAD   N3    C4     sing N N 158 
FAD   N3    HN3    sing N N 159 
FAD   C4    O4     doub N N 160 
FAD   C4    C4X    sing N N 161 
FAD   C4X   N5     doub N N 162 
FAD   C4X   C10    sing N N 163 
FAD   N5    C5X    sing N N 164 
FAD   C5X   C6     doub Y N 165 
FAD   C5X   C9A    sing Y N 166 
FAD   C6    C7     sing Y N 167 
FAD   C6    H6     sing N N 168 
FAD   C7    C7M    sing N N 169 
FAD   C7    C8     doub Y N 170 
FAD   C7M   HM71   sing N N 171 
FAD   C7M   HM72   sing N N 172 
FAD   C7M   HM73   sing N N 173 
FAD   C8    C8M    sing N N 174 
FAD   C8    C9     sing Y N 175 
FAD   C8M   HM81   sing N N 176 
FAD   C8M   HM82   sing N N 177 
FAD   C8M   HM83   sing N N 178 
FAD   C9    C9A    doub Y N 179 
FAD   C9    H9     sing N N 180 
FAD   C9A   N10    sing N N 181 
FAD   N10   C10    sing N N 182 
FAD   N10   "C1'"  sing N N 183 
FAD   "C1'" "C2'"  sing N N 184 
FAD   "C1'" "H1'1" sing N N 185 
FAD   "C1'" "H1'2" sing N N 186 
FAD   "C2'" "O2'"  sing N N 187 
FAD   "C2'" "C3'"  sing N N 188 
FAD   "C2'" "H2'"  sing N N 189 
FAD   "O2'" "HO2'" sing N N 190 
FAD   "C3'" "O3'"  sing N N 191 
FAD   "C3'" "C4'"  sing N N 192 
FAD   "C3'" "H3'"  sing N N 193 
FAD   "O3'" "HO3'" sing N N 194 
FAD   "C4'" "O4'"  sing N N 195 
FAD   "C4'" "C5'"  sing N N 196 
FAD   "C4'" "H4'"  sing N N 197 
FAD   "O4'" "HO4'" sing N N 198 
FAD   "C5'" "O5'"  sing N N 199 
FAD   "C5'" "H5'1" sing N N 200 
FAD   "C5'" "H5'2" sing N N 201 
FAD   "O5'" P      sing N N 202 
FAD   P     O1P    doub N N 203 
FAD   P     O2P    sing N N 204 
FAD   P     O3P    sing N N 205 
FAD   O2P   HOP2   sing N N 206 
GLN   N     CA     sing N N 207 
GLN   N     H      sing N N 208 
GLN   N     H2     sing N N 209 
GLN   CA    C      sing N N 210 
GLN   CA    CB     sing N N 211 
GLN   CA    HA     sing N N 212 
GLN   C     O      doub N N 213 
GLN   C     OXT    sing N N 214 
GLN   CB    CG     sing N N 215 
GLN   CB    HB2    sing N N 216 
GLN   CB    HB3    sing N N 217 
GLN   CG    CD     sing N N 218 
GLN   CG    HG2    sing N N 219 
GLN   CG    HG3    sing N N 220 
GLN   CD    OE1    doub N N 221 
GLN   CD    NE2    sing N N 222 
GLN   NE2   HE21   sing N N 223 
GLN   NE2   HE22   sing N N 224 
GLN   OXT   HXT    sing N N 225 
GLU   N     CA     sing N N 226 
GLU   N     H      sing N N 227 
GLU   N     H2     sing N N 228 
GLU   CA    C      sing N N 229 
GLU   CA    CB     sing N N 230 
GLU   CA    HA     sing N N 231 
GLU   C     O      doub N N 232 
GLU   C     OXT    sing N N 233 
GLU   CB    CG     sing N N 234 
GLU   CB    HB2    sing N N 235 
GLU   CB    HB3    sing N N 236 
GLU   CG    CD     sing N N 237 
GLU   CG    HG2    sing N N 238 
GLU   CG    HG3    sing N N 239 
GLU   CD    OE1    doub N N 240 
GLU   CD    OE2    sing N N 241 
GLU   OE2   HE2    sing N N 242 
GLU   OXT   HXT    sing N N 243 
GLY   N     CA     sing N N 244 
GLY   N     H      sing N N 245 
GLY   N     H2     sing N N 246 
GLY   CA    C      sing N N 247 
GLY   CA    HA2    sing N N 248 
GLY   CA    HA3    sing N N 249 
GLY   C     O      doub N N 250 
GLY   C     OXT    sing N N 251 
GLY   OXT   HXT    sing N N 252 
HIS   N     CA     sing N N 253 
HIS   N     H      sing N N 254 
HIS   N     H2     sing N N 255 
HIS   CA    C      sing N N 256 
HIS   CA    CB     sing N N 257 
HIS   CA    HA     sing N N 258 
HIS   C     O      doub N N 259 
HIS   C     OXT    sing N N 260 
HIS   CB    CG     sing N N 261 
HIS   CB    HB2    sing N N 262 
HIS   CB    HB3    sing N N 263 
HIS   CG    ND1    sing Y N 264 
HIS   CG    CD2    doub Y N 265 
HIS   ND1   CE1    doub Y N 266 
HIS   ND1   HD1    sing N N 267 
HIS   CD2   NE2    sing Y N 268 
HIS   CD2   HD2    sing N N 269 
HIS   CE1   NE2    sing Y N 270 
HIS   CE1   HE1    sing N N 271 
HIS   NE2   HE2    sing N N 272 
HIS   OXT   HXT    sing N N 273 
HOH   O     H1     sing N N 274 
HOH   O     H2     sing N N 275 
ILE   N     CA     sing N N 276 
ILE   N     H      sing N N 277 
ILE   N     H2     sing N N 278 
ILE   CA    C      sing N N 279 
ILE   CA    CB     sing N N 280 
ILE   CA    HA     sing N N 281 
ILE   C     O      doub N N 282 
ILE   C     OXT    sing N N 283 
ILE   CB    CG1    sing N N 284 
ILE   CB    CG2    sing N N 285 
ILE   CB    HB     sing N N 286 
ILE   CG1   CD1    sing N N 287 
ILE   CG1   HG12   sing N N 288 
ILE   CG1   HG13   sing N N 289 
ILE   CG2   HG21   sing N N 290 
ILE   CG2   HG22   sing N N 291 
ILE   CG2   HG23   sing N N 292 
ILE   CD1   HD11   sing N N 293 
ILE   CD1   HD12   sing N N 294 
ILE   CD1   HD13   sing N N 295 
ILE   OXT   HXT    sing N N 296 
LEU   N     CA     sing N N 297 
LEU   N     H      sing N N 298 
LEU   N     H2     sing N N 299 
LEU   CA    C      sing N N 300 
LEU   CA    CB     sing N N 301 
LEU   CA    HA     sing N N 302 
LEU   C     O      doub N N 303 
LEU   C     OXT    sing N N 304 
LEU   CB    CG     sing N N 305 
LEU   CB    HB2    sing N N 306 
LEU   CB    HB3    sing N N 307 
LEU   CG    CD1    sing N N 308 
LEU   CG    CD2    sing N N 309 
LEU   CG    HG     sing N N 310 
LEU   CD1   HD11   sing N N 311 
LEU   CD1   HD12   sing N N 312 
LEU   CD1   HD13   sing N N 313 
LEU   CD2   HD21   sing N N 314 
LEU   CD2   HD22   sing N N 315 
LEU   CD2   HD23   sing N N 316 
LEU   OXT   HXT    sing N N 317 
LYS   N     CA     sing N N 318 
LYS   N     H      sing N N 319 
LYS   N     H2     sing N N 320 
LYS   CA    C      sing N N 321 
LYS   CA    CB     sing N N 322 
LYS   CA    HA     sing N N 323 
LYS   C     O      doub N N 324 
LYS   C     OXT    sing N N 325 
LYS   CB    CG     sing N N 326 
LYS   CB    HB2    sing N N 327 
LYS   CB    HB3    sing N N 328 
LYS   CG    CD     sing N N 329 
LYS   CG    HG2    sing N N 330 
LYS   CG    HG3    sing N N 331 
LYS   CD    CE     sing N N 332 
LYS   CD    HD2    sing N N 333 
LYS   CD    HD3    sing N N 334 
LYS   CE    NZ     sing N N 335 
LYS   CE    HE2    sing N N 336 
LYS   CE    HE3    sing N N 337 
LYS   NZ    HZ1    sing N N 338 
LYS   NZ    HZ2    sing N N 339 
LYS   NZ    HZ3    sing N N 340 
LYS   OXT   HXT    sing N N 341 
MAN   C1    C2     sing N N 342 
MAN   C1    O1     sing N N 343 
MAN   C1    O5     sing N N 344 
MAN   C1    H1     sing N N 345 
MAN   C2    C3     sing N N 346 
MAN   C2    O2     sing N N 347 
MAN   C2    H2     sing N N 348 
MAN   C3    C4     sing N N 349 
MAN   C3    O3     sing N N 350 
MAN   C3    H3     sing N N 351 
MAN   C4    C5     sing N N 352 
MAN   C4    O4     sing N N 353 
MAN   C4    H4     sing N N 354 
MAN   C5    C6     sing N N 355 
MAN   C5    O5     sing N N 356 
MAN   C5    H5     sing N N 357 
MAN   C6    O6     sing N N 358 
MAN   C6    H61    sing N N 359 
MAN   C6    H62    sing N N 360 
MAN   O1    HO1    sing N N 361 
MAN   O2    HO2    sing N N 362 
MAN   O3    HO3    sing N N 363 
MAN   O4    HO4    sing N N 364 
MAN   O6    HO6    sing N N 365 
MET   N     CA     sing N N 366 
MET   N     H      sing N N 367 
MET   N     H2     sing N N 368 
MET   CA    C      sing N N 369 
MET   CA    CB     sing N N 370 
MET   CA    HA     sing N N 371 
MET   C     O      doub N N 372 
MET   C     OXT    sing N N 373 
MET   CB    CG     sing N N 374 
MET   CB    HB2    sing N N 375 
MET   CB    HB3    sing N N 376 
MET   CG    SD     sing N N 377 
MET   CG    HG2    sing N N 378 
MET   CG    HG3    sing N N 379 
MET   SD    CE     sing N N 380 
MET   CE    HE1    sing N N 381 
MET   CE    HE2    sing N N 382 
MET   CE    HE3    sing N N 383 
MET   OXT   HXT    sing N N 384 
NAG   C1    C2     sing N N 385 
NAG   C1    O1     sing N N 386 
NAG   C1    O5     sing N N 387 
NAG   C1    H1     sing N N 388 
NAG   C2    C3     sing N N 389 
NAG   C2    N2     sing N N 390 
NAG   C2    H2     sing N N 391 
NAG   C3    C4     sing N N 392 
NAG   C3    O3     sing N N 393 
NAG   C3    H3     sing N N 394 
NAG   C4    C5     sing N N 395 
NAG   C4    O4     sing N N 396 
NAG   C4    H4     sing N N 397 
NAG   C5    C6     sing N N 398 
NAG   C5    O5     sing N N 399 
NAG   C5    H5     sing N N 400 
NAG   C6    O6     sing N N 401 
NAG   C6    H61    sing N N 402 
NAG   C6    H62    sing N N 403 
NAG   C7    C8     sing N N 404 
NAG   C7    N2     sing N N 405 
NAG   C7    O7     doub N N 406 
NAG   C8    H81    sing N N 407 
NAG   C8    H82    sing N N 408 
NAG   C8    H83    sing N N 409 
NAG   N2    HN2    sing N N 410 
NAG   O1    HO1    sing N N 411 
NAG   O3    HO3    sing N N 412 
NAG   O4    HO4    sing N N 413 
NAG   O6    HO6    sing N N 414 
PHE   N     CA     sing N N 415 
PHE   N     H      sing N N 416 
PHE   N     H2     sing N N 417 
PHE   CA    C      sing N N 418 
PHE   CA    CB     sing N N 419 
PHE   CA    HA     sing N N 420 
PHE   C     O      doub N N 421 
PHE   C     OXT    sing N N 422 
PHE   CB    CG     sing N N 423 
PHE   CB    HB2    sing N N 424 
PHE   CB    HB3    sing N N 425 
PHE   CG    CD1    doub Y N 426 
PHE   CG    CD2    sing Y N 427 
PHE   CD1   CE1    sing Y N 428 
PHE   CD1   HD1    sing N N 429 
PHE   CD2   CE2    doub Y N 430 
PHE   CD2   HD2    sing N N 431 
PHE   CE1   CZ     doub Y N 432 
PHE   CE1   HE1    sing N N 433 
PHE   CE2   CZ     sing Y N 434 
PHE   CE2   HE2    sing N N 435 
PHE   CZ    HZ     sing N N 436 
PHE   OXT   HXT    sing N N 437 
PRO   N     CA     sing N N 438 
PRO   N     CD     sing N N 439 
PRO   N     H      sing N N 440 
PRO   CA    C      sing N N 441 
PRO   CA    CB     sing N N 442 
PRO   CA    HA     sing N N 443 
PRO   C     O      doub N N 444 
PRO   C     OXT    sing N N 445 
PRO   CB    CG     sing N N 446 
PRO   CB    HB2    sing N N 447 
PRO   CB    HB3    sing N N 448 
PRO   CG    CD     sing N N 449 
PRO   CG    HG2    sing N N 450 
PRO   CG    HG3    sing N N 451 
PRO   CD    HD2    sing N N 452 
PRO   CD    HD3    sing N N 453 
PRO   OXT   HXT    sing N N 454 
SER   N     CA     sing N N 455 
SER   N     H      sing N N 456 
SER   N     H2     sing N N 457 
SER   CA    C      sing N N 458 
SER   CA    CB     sing N N 459 
SER   CA    HA     sing N N 460 
SER   C     O      doub N N 461 
SER   C     OXT    sing N N 462 
SER   CB    OG     sing N N 463 
SER   CB    HB2    sing N N 464 
SER   CB    HB3    sing N N 465 
SER   OG    HG     sing N N 466 
SER   OXT   HXT    sing N N 467 
THR   N     CA     sing N N 468 
THR   N     H      sing N N 469 
THR   N     H2     sing N N 470 
THR   CA    C      sing N N 471 
THR   CA    CB     sing N N 472 
THR   CA    HA     sing N N 473 
THR   C     O      doub N N 474 
THR   C     OXT    sing N N 475 
THR   CB    OG1    sing N N 476 
THR   CB    CG2    sing N N 477 
THR   CB    HB     sing N N 478 
THR   OG1   HG1    sing N N 479 
THR   CG2   HG21   sing N N 480 
THR   CG2   HG22   sing N N 481 
THR   CG2   HG23   sing N N 482 
THR   OXT   HXT    sing N N 483 
TRP   N     CA     sing N N 484 
TRP   N     H      sing N N 485 
TRP   N     H2     sing N N 486 
TRP   CA    C      sing N N 487 
TRP   CA    CB     sing N N 488 
TRP   CA    HA     sing N N 489 
TRP   C     O      doub N N 490 
TRP   C     OXT    sing N N 491 
TRP   CB    CG     sing N N 492 
TRP   CB    HB2    sing N N 493 
TRP   CB    HB3    sing N N 494 
TRP   CG    CD1    doub Y N 495 
TRP   CG    CD2    sing Y N 496 
TRP   CD1   NE1    sing Y N 497 
TRP   CD1   HD1    sing N N 498 
TRP   CD2   CE2    doub Y N 499 
TRP   CD2   CE3    sing Y N 500 
TRP   NE1   CE2    sing Y N 501 
TRP   NE1   HE1    sing N N 502 
TRP   CE2   CZ2    sing Y N 503 
TRP   CE3   CZ3    doub Y N 504 
TRP   CE3   HE3    sing N N 505 
TRP   CZ2   CH2    doub Y N 506 
TRP   CZ2   HZ2    sing N N 507 
TRP   CZ3   CH2    sing Y N 508 
TRP   CZ3   HZ3    sing N N 509 
TRP   CH2   HH2    sing N N 510 
TRP   OXT   HXT    sing N N 511 
TYR   N     CA     sing N N 512 
TYR   N     H      sing N N 513 
TYR   N     H2     sing N N 514 
TYR   CA    C      sing N N 515 
TYR   CA    CB     sing N N 516 
TYR   CA    HA     sing N N 517 
TYR   C     O      doub N N 518 
TYR   C     OXT    sing N N 519 
TYR   CB    CG     sing N N 520 
TYR   CB    HB2    sing N N 521 
TYR   CB    HB3    sing N N 522 
TYR   CG    CD1    doub Y N 523 
TYR   CG    CD2    sing Y N 524 
TYR   CD1   CE1    sing Y N 525 
TYR   CD1   HD1    sing N N 526 
TYR   CD2   CE2    doub Y N 527 
TYR   CD2   HD2    sing N N 528 
TYR   CE1   CZ     doub Y N 529 
TYR   CE1   HE1    sing N N 530 
TYR   CE2   CZ     sing Y N 531 
TYR   CE2   HE2    sing N N 532 
TYR   CZ    OH     sing N N 533 
TYR   OH    HH     sing N N 534 
TYR   OXT   HXT    sing N N 535 
VAL   N     CA     sing N N 536 
VAL   N     H      sing N N 537 
VAL   N     H2     sing N N 538 
VAL   CA    C      sing N N 539 
VAL   CA    CB     sing N N 540 
VAL   CA    HA     sing N N 541 
VAL   C     O      doub N N 542 
VAL   C     OXT    sing N N 543 
VAL   CB    CG1    sing N N 544 
VAL   CB    CG2    sing N N 545 
VAL   CB    HB     sing N N 546 
VAL   CG1   HG11   sing N N 547 
VAL   CG1   HG12   sing N N 548 
VAL   CG1   HG13   sing N N 549 
VAL   CG2   HG21   sing N N 550 
VAL   CG2   HG22   sing N N 551 
VAL   CG2   HG23   sing N N 552 
VAL   OXT   HXT    sing N N 553 
# 
_pdbx_audit_support.funding_organization   'European Cooperation in Science and Technology (COST) action' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'COZYME (CA21162)' 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 MAN 3 n 
2 MAN 4 n 
2 MAN 5 n 
3 NAG 1 n 
3 NAG 2 n 
3 MAN 3 n 
3 MAN 4 n 
3 MAN 5 n 
4 NAG 1 n 
4 NAG 2 n 
4 MAN 3 n 
4 MAN 4 n 
5 NAG 1 n 
5 NAG 2 n 
5 MAN 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H8U 
_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]   0.011042 
_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]   0.011042 
_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]   0.003443 
_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 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER   A 1 5   ? 15.25752  16.97210  40.83477  1.000 77.63198  ? 5   SER   A N     1 
ATOM   2    C CA    . SER   A 1 5   ? 13.88378  16.92285  40.32070  1.000 79.65091  ? 5   SER   A CA    1 
ATOM   3    C C     . SER   A 1 5   ? 13.70319  17.68583  38.98198  1.000 81.17302  ? 5   SER   A C     1 
ATOM   4    O O     . SER   A 1 5   ? 13.22387  17.08381  38.01092  1.000 79.93830  ? 5   SER   A O     1 
ATOM   5    C CB    . SER   A 1 5   ? 12.88058  17.44594  41.36632  1.000 83.40849  ? 5   SER   A CB    1 
ATOM   6    O OG    . SER   A 1 5   ? 12.62000  16.49992  42.40060  1.000 88.80620  ? 5   SER   A OG    1 
ATOM   7    N N     . ALA   A 1 6   ? 14.05032  18.98406  38.90534  1.000 80.02090  ? 6   ALA   A N     1 
ATOM   8    C CA    . ALA   A 1 6   ? 14.12886  19.63374  37.59184  1.000 70.91436  ? 6   ALA   A CA    1 
ATOM   9    C C     . ALA   A 1 6   ? 14.90816  18.75836  36.63852  1.000 68.94975  ? 6   ALA   A C     1 
ATOM   10   O O     . ALA   A 1 6   ? 14.50306  18.52966  35.49511  1.000 61.83854  ? 6   ALA   A O     1 
ATOM   11   C CB    . ALA   A 1 6   ? 14.81591  20.99535  37.69146  1.000 63.31312  ? 6   ALA   A CB    1 
ATOM   12   N N     . PHE   A 1 7   ? 16.04079  18.25756  37.14113  1.000 75.01247  ? 7   PHE   A N     1 
ATOM   13   C CA    . PHE   A 1 7   ? 16.92293  17.31652  36.46502  1.000 65.71027  ? 7   PHE   A CA    1 
ATOM   14   C C     . PHE   A 1 7   ? 16.25967  15.94952  36.35382  1.000 68.37242  ? 7   PHE   A C     1 
ATOM   15   O O     . PHE   A 1 7   ? 16.12098  15.40377  35.25669  1.000 78.36866  ? 7   PHE   A O     1 
ATOM   16   C CB    . PHE   A 1 7   ? 18.22639  17.29457  37.27492  1.000 71.16566  ? 7   PHE   A CB    1 
ATOM   17   C CG    . PHE   A 1 7   ? 19.22958  16.21510  36.93592  1.000 67.74325  ? 7   PHE   A CG    1 
ATOM   18   C CD1   . PHE   A 1 7   ? 20.18438  16.40886  35.95515  1.000 66.68543  ? 7   PHE   A CD1   1 
ATOM   19   C CD2   . PHE   A 1 7   ? 19.29721  15.05381  37.69608  1.000 72.89970  ? 7   PHE   A CD2   1 
ATOM   20   C CE1   . PHE   A 1 7   ? 21.14096  15.43774  35.69705  1.000 65.54960  ? 7   PHE   A CE1   1 
ATOM   21   C CE2   . PHE   A 1 7   ? 20.25499  14.08001  37.44059  1.000 67.40225  ? 7   PHE   A CE2   1 
ATOM   22   C CZ    . PHE   A 1 7   ? 21.17622  14.27709  36.44007  1.000 64.89312  ? 7   PHE   A CZ    1 
ATOM   23   N N     . ALA   A 1 8   ? 15.75727  15.41218  37.45837  1.000 64.81165  ? 8   ALA   A N     1 
ATOM   24   C CA    . ALA   A 1 8   ? 15.08017  14.11833  37.37460  1.000 67.50782  ? 8   ALA   A CA    1 
ATOM   25   C C     . ALA   A 1 8   ? 13.89503  14.10036  36.39795  1.000 67.90269  ? 8   ALA   A C     1 
ATOM   26   O O     . ALA   A 1 8   ? 13.47645  13.02368  35.97865  1.000 66.52514  ? 8   ALA   A O     1 
ATOM   27   C CB    . ALA   A 1 8   ? 14.60578  13.68180  38.76276  1.000 67.56728  ? 8   ALA   A CB    1 
ATOM   28   N N     . THR   A 1 9   ? 13.32507  15.24661  36.03741  1.000 70.32086  ? 9   THR   A N     1 
ATOM   29   C CA    . THR   A 1 9   ? 12.11523  15.22861  35.22405  1.000 71.46178  ? 9   THR   A CA    1 
ATOM   30   C C     . THR   A 1 9   ? 12.36121  15.25956  33.73272  1.000 74.44461  ? 9   THR   A C     1 
ATOM   31   O O     . THR   A 1 9   ? 11.53707  14.73171  32.96577  1.000 76.52098  ? 9   THR   A O     1 
ATOM   32   C CB    . THR   A 1 9   ? 11.20429  16.39831  35.55569  1.000 66.32178  ? 9   THR   A CB    1 
ATOM   33   O OG1   . THR   A 1 9   ? 10.67938  16.19465  36.86520  1.000 74.31514  ? 9   THR   A OG1   1 
ATOM   34   C CG2   . THR   A 1 9   ? 10.06935  16.49571  34.52386  1.000 64.01201  ? 9   THR   A CG2   1 
ATOM   35   N N     . CYS   A 1 10  ? 13.42773  15.93062  33.29823  1.000 70.65573  ? 10  CYS   A N     1 
ATOM   36   C CA    . CYS   A 1 10  ? 13.80388  15.84131  31.90555  1.000 72.24041  ? 10  CYS   A CA    1 
ATOM   37   C C     . CYS   A 1 10  ? 14.66897  14.62037  31.62660  1.000 67.74291  ? 10  CYS   A C     1 
ATOM   38   O O     . CYS   A 1 10  ? 14.74172  14.18188  30.46739  1.000 65.26516  ? 10  CYS   A O     1 
ATOM   39   C CB    . CYS   A 1 10  ? 14.55193  17.09847  31.46245  1.000 75.28866  ? 10  CYS   A CB    1 
ATOM   40   S SG    . CYS   A 1 10  ? 16.25022  17.10164  32.07449  1.000 95.67319  ? 10  CYS   A SG    1 
ATOM   41   N N     . LEU   A 1 11  ? 15.32340  14.06987  32.64827  1.000 63.76361  ? 11  LEU   A N     1 
ATOM   42   C CA    . LEU   A 1 11  ? 16.09691  12.84696  32.44273  1.000 61.70536  ? 11  LEU   A CA    1 
ATOM   43   C C     . LEU   A 1 11  ? 15.14510  11.67327  32.20609  1.000 62.97184  ? 11  LEU   A C     1 
ATOM   44   O O     . LEU   A 1 11  ? 15.47508  10.73006  31.47746  1.000 64.11346  ? 11  LEU   A O     1 
ATOM   45   C CB    . LEU   A 1 11  ? 17.02487  12.62745  33.64010  1.000 56.44772  ? 11  LEU   A CB    1 
ATOM   46   C CG    . LEU   A 1 11  ? 18.47714  12.16897  33.53130  1.000 53.76668  ? 11  LEU   A CG    1 
ATOM   47   C CD1   . LEU   A 1 11  ? 19.18477  13.02214  32.54966  1.000 55.75172  ? 11  LEU   A CD1   1 
ATOM   48   C CD2   . LEU   A 1 11  ? 19.14050  12.42768  34.83150  1.000 60.14061  ? 11  LEU   A CD2   1 
ATOM   49   N N     . LEU   A 1 12  ? 13.94548  11.73258  32.78978  1.000 60.14523  ? 12  LEU   A N     1 
ATOM   50   C CA    . LEU   A 1 12  ? 12.85624  10.86992  32.33504  1.000 58.73755  ? 12  LEU   A CA    1 
ATOM   51   C C     . LEU   A 1 12  ? 12.49254  11.16975  30.88839  1.000 62.44173  ? 12  LEU   A C     1 
ATOM   52   O O     . LEU   A 1 12  ? 12.08796  10.27588  30.13891  1.000 60.58804  ? 12  LEU   A O     1 
ATOM   53   C CB    . LEU   A 1 12  ? 11.62691  11.06667  33.21221  1.000 61.22376  ? 12  LEU   A CB    1 
ATOM   54   C CG    . LEU   A 1 12  ? 10.56016  10.01548  32.93000  1.000 60.70859  ? 12  LEU   A CG    1 
ATOM   55   C CD1   . LEU   A 1 12  ? 10.21260  9.30194   34.21125  1.000 58.51601  ? 12  LEU   A CD1   1 
ATOM   56   C CD2   . LEU   A 1 12  ? 9.31845   10.64142  32.22794  1.000 62.19095  ? 12  LEU   A CD2   1 
ATOM   57   N N     . ALA   A 1 13  ? 12.58701  12.44177  30.49552  1.000 62.57284  ? 13  ALA   A N     1 
ATOM   58   C CA    . ALA   A 1 13  ? 12.19321  12.85241  29.15614  1.000 56.97577  ? 13  ALA   A CA    1 
ATOM   59   C C     . ALA   A 1 13  ? 13.24479  12.46268  28.12356  1.000 58.37868  ? 13  ALA   A C     1 
ATOM   60   O O     . ALA   A 1 13  ? 12.91732  12.20033  26.95966  1.000 56.66844  ? 13  ALA   A O     1 
ATOM   61   C CB    . ALA   A 1 13  ? 11.95552  14.36159  29.14457  1.000 56.52950  ? 13  ALA   A CB    1 
ATOM   62   N N     . SER   A 1 14  ? 14.51443  12.44399  28.52326  1.000 60.43348  ? 14  SER   A N     1 
ATOM   63   C CA    . SER   A 1 14  ? 15.56168  12.00835  27.61385  1.000 54.78763  ? 14  SER   A CA    1 
ATOM   64   C C     . SER   A 1 14  ? 15.33753  10.56804  27.17644  1.000 55.04335  ? 14  SER   A C     1 
ATOM   65   O O     . SER   A 1 14  ? 15.60596  10.21109  26.02248  1.000 56.01047  ? 14  SER   A O     1 
ATOM   66   C CB    . SER   A 1 14  ? 16.92034  12.18891  28.28480  1.000 46.52349  ? 14  SER   A CB    1 
ATOM   67   O OG    . SER   A 1 14  ? 16.96813  11.34236  29.42153  1.000 49.93442  ? 14  SER   A OG    1 
ATOM   68   N N     . VAL   A 1 15  ? 14.82693  9.73505   28.07269  1.000 57.61051  ? 15  VAL   A N     1 
ATOM   69   C CA    . VAL   A 1 15  ? 14.58897  8.33585   27.75712  1.000 55.97140  ? 15  VAL   A CA    1 
ATOM   70   C C     . VAL   A 1 15  ? 13.09067  8.15496   27.51470  1.000 59.15482  ? 15  VAL   A C     1 
ATOM   71   O O     . VAL   A 1 15  ? 12.51163  7.11983   27.88450  1.000 60.77389  ? 15  VAL   A O     1 
ATOM   72   C CB    . VAL   A 1 15  ? 15.11450  7.41433   28.87969  1.000 52.40550  ? 15  VAL   A CB    1 
ATOM   73   C CG1   . VAL   A 1 15  ? 16.58769  7.68434   29.15388  1.000 53.15257  ? 15  VAL   A CG1   1 
ATOM   74   C CG2   . VAL   A 1 15  ? 14.34836  7.62383   30.13331  1.000 57.15312  ? 15  VAL   A CG2   1 
ATOM   75   N N     . GLY   A 1 16  ? 12.45612  9.19084   26.93599  1.000 57.15701  ? 16  GLY   A N     1 
ATOM   76   C CA    . GLY   A 1 16  ? 11.08447  9.18508   26.44277  1.000 53.28705  ? 16  GLY   A CA    1 
ATOM   77   C C     . GLY   A 1 16  ? 10.04861  8.57613   27.36090  1.000 57.55956  ? 16  GLY   A C     1 
ATOM   78   O O     . GLY   A 1 16  ? 9.16200   7.85390   26.90164  1.000 65.97466  ? 16  GLY   A O     1 
ATOM   79   N N     . GLY   A 1 17  ? 10.14119  8.85688   28.65715  1.000 55.50436  ? 17  GLY   A N     1 
ATOM   80   C CA    . GLY   A 1 17  ? 9.19185   8.30362   29.59271  1.000 54.59169  ? 17  GLY   A CA    1 
ATOM   81   C C     . GLY   A 1 17  ? 9.72133   7.08230   30.30891  1.000 58.81986  ? 17  GLY   A C     1 
ATOM   82   O O     . GLY   A 1 17  ? 9.66564   7.02068   31.53967  1.000 65.67615  ? 17  GLY   A O     1 
ATOM   83   N N     . ASN   A 1 18  ? 10.25312  6.11462   29.55415  1.000 58.48939  ? 18  ASN   A N     1 
ATOM   84   C CA    . ASN   A 1 18  ? 10.57371  4.79484   30.09011  1.000 59.49425  ? 18  ASN   A CA    1 
ATOM   85   C C     . ASN   A 1 18  ? 11.21952  4.93136   31.46723  1.000 62.95295  ? 18  ASN   A C     1 
ATOM   86   O O     . ASN   A 1 18  ? 12.41263  5.22500   31.56799  1.000 63.13675  ? 18  ASN   A O     1 
ATOM   87   C CB    . ASN   A 1 18  ? 11.46494  4.01803   29.10800  1.000 57.30997  ? 18  ASN   A CB    1 
ATOM   88   C CG    . ASN   A 1 18  ? 11.87600  2.65108   29.62419  1.000 58.14546  ? 18  ASN   A CG    1 
ATOM   89   O OD1   . ASN   A 1 18  ? 11.63967  2.30898   30.77478  1.000 60.26732  ? 18  ASN   A OD1   1 
ATOM   90   N ND2   . ASN   A 1 18  ? 12.53455  1.88808   28.78316  1.000 57.39429  ? 18  ASN   A ND2   1 
ATOM   91   N N     . SER   A 1 19  ? 10.42363  4.75473   32.53943  1.000 64.71278  ? 19  SER   A N     1 
ATOM   92   C CA    . SER   A 1 19  ? 10.93975  4.91045   33.89607  1.000 62.52075  ? 19  SER   A CA    1 
ATOM   93   C C     . SER   A 1 19  ? 11.97308  3.84992   34.23443  1.000 62.79512  ? 19  SER   A C     1 
ATOM   94   O O     . SER   A 1 19  ? 12.70426  4.00391   35.21890  1.000 63.62729  ? 19  SER   A O     1 
ATOM   95   C CB    . SER   A 1 19  ? 9.81342   4.83221   34.92343  1.000 71.87486  ? 19  SER   A CB    1 
ATOM   96   O OG    . SER   A 1 19  ? 9.41777   3.48218   35.16702  1.000 76.59156  ? 19  SER   A OG    1 
ATOM   97   N N     . SER   A 1 20  ? 12.01898  2.77397   33.45973  1.000 58.00313  ? 20  SER   A N     1 
ATOM   98   C CA    . SER   A 1 20  ? 12.99373  1.71752   33.68702  1.000 65.80575  ? 20  SER   A CA    1 
ATOM   99   C C     . SER   A 1 20  ? 14.32747  2.00385   33.00742  1.000 61.55796  ? 20  SER   A C     1 
ATOM   100  O O     . SER   A 1 20  ? 15.28471  1.24533   33.19123  1.000 59.27993  ? 20  SER   A O     1 
ATOM   101  C CB    . SER   A 1 20  ? 12.41257  0.38467   33.21217  1.000 70.45363  ? 20  SER   A CB    1 
ATOM   102  O OG    . SER   A 1 20  ? 11.20414  0.10579   33.90668  1.000 68.29623  ? 20  SER   A OG    1 
ATOM   103  N N     . ALA   A 1 21  ? 14.41353  3.08992   32.24400  1.000 60.80322  ? 21  ALA   A N     1 
ATOM   104  C CA    . ALA   A 1 21  ? 15.66937  3.52939   31.65763  1.000 56.80072  ? 21  ALA   A CA    1 
ATOM   105  C C     . ALA   A 1 21  ? 16.23974  4.76320   32.34898  1.000 53.70393  ? 21  ALA   A C     1 
ATOM   106  O O     . ALA   A 1 21  ? 16.85877  5.59822   31.69041  1.000 56.02141  ? 21  ALA   A O     1 
ATOM   107  C CB    . ALA   A 1 21  ? 15.48327  3.79728   30.16691  1.000 54.75104  ? 21  ALA   A CB    1 
ATOM   108  N N     . VAL   A 1 22  ? 16.05156  4.89669   33.66213  1.000 54.69276  ? 22  VAL   A N     1 
ATOM   109  C CA    . VAL   A 1 22  ? 16.58103  6.02406   34.43232  1.000 55.37140  ? 22  VAL   A CA    1 
ATOM   110  C C     . VAL   A 1 22  ? 16.36978  5.71090   35.89485  1.000 52.60448  ? 22  VAL   A C     1 
ATOM   111  O O     . VAL   A 1 22  ? 15.38225  5.06878   36.24856  1.000 55.58619  ? 22  VAL   A O     1 
ATOM   112  C CB    . VAL   A 1 22  ? 15.92576  7.35552   34.06694  1.000 56.57206  ? 22  VAL   A CB    1 
ATOM   113  C CG1   . VAL   A 1 22  ? 14.46203  7.31359   34.42172  1.000 58.50829  ? 22  VAL   A CG1   1 
ATOM   114  C CG2   . VAL   A 1 22  ? 16.61429  8.50441   34.80325  1.000 51.64562  ? 22  VAL   A CG2   1 
ATOM   115  N N     . ALA   A 1 23  ? 17.28596  6.16422   36.75473  1.000 52.62078  ? 23  ALA   A N     1 
ATOM   116  C CA    . ALA   A 1 23  ? 17.29383  5.66474   38.12001  1.000 59.45756  ? 23  ALA   A CA    1 
ATOM   117  C C     . ALA   A 1 23  ? 18.10934  6.59465   39.00805  1.000 61.66768  ? 23  ALA   A C     1 
ATOM   118  O O     . ALA   A 1 23  ? 19.13688  7.13013   38.58420  1.000 56.81312  ? 23  ALA   A O     1 
ATOM   119  C CB    . ALA   A 1 23  ? 17.84081  4.23162   38.16856  1.000 56.82980  ? 23  ALA   A CB    1 
ATOM   120  N N     . PHE   A 1 24  ? 17.65523  6.75851   40.24566  1.000 64.73440  ? 24  PHE   A N     1 
ATOM   121  C CA    . PHE   A 1 24  ? 18.15913  7.78626   41.13870  1.000 61.08132  ? 24  PHE   A CA    1 
ATOM   122  C C     . PHE   A 1 24  ? 18.54486  7.22608   42.48655  1.000 64.76244  ? 24  PHE   A C     1 
ATOM   123  O O     . PHE   A 1 24  ? 17.98701  6.22365   42.93710  1.000 63.73453  ? 24  PHE   A O     1 
ATOM   124  C CB    . PHE   A 1 24  ? 17.10919  8.86850   41.33240  1.000 63.36685  ? 24  PHE   A CB    1 
ATOM   125  C CG    . PHE   A 1 24  ? 16.75897  9.50474   40.09339  1.000 56.70028  ? 24  PHE   A CG    1 
ATOM   126  C CD1   . PHE   A 1 24  ? 15.86331  8.91044   39.25463  1.000 59.06913  ? 24  PHE   A CD1   1 
ATOM   127  C CD2   . PHE   A 1 24  ? 17.34216  10.68407  39.74310  1.000 60.63184  ? 24  PHE   A CD2   1 
ATOM   128  C CE1   . PHE   A 1 24  ? 15.54256  9.47046   38.07933  1.000 59.45981  ? 24  PHE   A CE1   1 
ATOM   129  C CE2   . PHE   A 1 24  ? 17.02617  11.26733  38.57449  1.000 66.26502  ? 24  PHE   A CE2   1 
ATOM   130  C CZ    . PHE   A 1 24  ? 16.11284  10.65523  37.73590  1.000 66.30592  ? 24  PHE   A CZ    1 
ATOM   131  N N     . PRO   A 1 25  ? 19.44976  7.91100   43.18865  1.000 66.01782  ? 25  PRO   A N     1 
ATOM   132  C CA    . PRO   A 1 25  ? 20.16214  7.30397   44.31933  1.000 60.63292  ? 25  PRO   A CA    1 
ATOM   133  C C     . PRO   A 1 25  ? 19.30407  7.03725   45.52469  1.000 64.41131  ? 25  PRO   A C     1 
ATOM   134  O O     . PRO   A 1 25  ? 19.83473  6.53897   46.52418  1.000 66.71688  ? 25  PRO   A O     1 
ATOM   135  C CB    . PRO   A 1 25  ? 21.24492  8.35062   44.65080  1.000 63.00336  ? 25  PRO   A CB    1 
ATOM   136  C CG    . PRO   A 1 25  ? 21.10982  9.42772   43.57376  1.000 63.03425  ? 25  PRO   A CG    1 
ATOM   137  C CD    . PRO   A 1 25  ? 19.73639  9.34451   43.05086  1.000 65.09891  ? 25  PRO   A CD    1 
ATOM   138  N N     . ASN   A 1 26  ? 18.01247  7.37156   45.47764  1.000 69.40812  ? 26  ASN   A N     1 
ATOM   139  C CA    . ASN   A 1 26  ? 17.14023  7.12150   46.62085  1.000 72.69338  ? 26  ASN   A CA    1 
ATOM   140  C C     . ASN   A 1 26  ? 16.59129  5.69592   46.63950  1.000 76.07373  ? 26  ASN   A C     1 
ATOM   141  O O     . ASN   A 1 26  ? 16.33938  5.14721   47.71839  1.000 81.37067  ? 26  ASN   A O     1 
ATOM   142  C CB    . ASN   A 1 26  ? 16.01105  8.15215   46.64174  1.000 74.83462  ? 26  ASN   A CB    1 
ATOM   143  C CG    . ASN   A 1 26  ? 15.23352  8.21139   45.33261  1.000 83.68866  ? 26  ASN   A CG    1 
ATOM   144  O OD1   . ASN   A 1 26  ? 14.35857  7.37590   45.04132  1.000 79.73771  ? 26  ASN   A OD1   1 
ATOM   145  N ND2   . ASN   A 1 26  ? 15.55582  9.21660   44.52887  1.000 99.07866  ? 26  ASN   A ND2   1 
ATOM   146  N N     . GLN   A 1 27  ? 16.42625  5.08273   45.47066  1.000 75.18926  ? 27  GLN   A N     1 
ATOM   147  C CA    . GLN   A 1 27  ? 15.95539  3.71047   45.34802  1.000 76.07139  ? 27  GLN   A CA    1 
ATOM   148  C C     . GLN   A 1 27  ? 16.92004  2.73048   46.04450  1.000 78.29521  ? 27  GLN   A C     1 
ATOM   149  O O     . GLN   A 1 27  ? 18.03740  3.07233   46.44177  1.000 72.67486  ? 27  GLN   A O     1 
ATOM   150  C CB    . GLN   A 1 27  ? 15.84118  3.34359   43.87573  1.000 74.57022  ? 27  GLN   A CB    1 
ATOM   151  C CG    . GLN   A 1 27  ? 15.26438  4.45713   43.01392  1.000 77.49244  ? 27  GLN   A CG    1 
ATOM   152  C CD    . GLN   A 1 27  ? 15.47729  4.20039   41.52322  1.000 85.16097  ? 27  GLN   A CD    1 
ATOM   153  O OE1   . GLN   A 1 27  ? 16.05541  3.17682   41.13187  1.000 84.06265  ? 27  GLN   A OE1   1 
ATOM   154  N NE2   . GLN   A 1 27  ? 15.06462  5.15825   40.68958  1.000 76.63249  ? 27  GLN   A NE2   1 
ATOM   155  N N     . ALA   A 1 28  ? 16.48533  1.47440   46.14907  1.000 75.39912  ? 28  ALA   A N     1 
ATOM   156  C CA    . ALA   A 1 28  ? 17.26927  0.46446   46.84818  1.000 73.49807  ? 28  ALA   A CA    1 
ATOM   157  C C     . ALA   A 1 28  ? 18.17186  -0.36651  45.94960  1.000 76.86014  ? 28  ALA   A C     1 
ATOM   158  O O     . ALA   A 1 28  ? 19.19637  -0.86583  46.43502  1.000 81.22240  ? 28  ALA   A O     1 
ATOM   159  C CB    . ALA   A 1 28  ? 16.35624  -0.49479  47.60449  1.000 74.46985  ? 28  ALA   A CB    1 
ATOM   160  N N     . ASN   A 1 29  ? 17.80630  -0.57174  44.66737  1.000 75.67347  ? 29  ASN   A N     1 
ATOM   161  C CA    . ASN   A 1 29  ? 18.69948  -1.29316  43.75407  1.000 71.82312  ? 29  ASN   A CA    1 
ATOM   162  C C     . ASN   A 1 29  ? 19.85504  -0.41824  43.29948  1.000 72.86254  ? 29  ASN   A C     1 
ATOM   163  O O     . ASN   A 1 29  ? 20.78634  -0.91954  42.65166  1.000 67.52639  ? 29  ASN   A O     1 
ATOM   164  C CB    . ASN   A 1 29  ? 17.96588  -1.87236  42.50921  1.000 66.08288  ? 29  ASN   A CB    1 
ATOM   165  C CG    . ASN   A 1 29  ? 16.88247  -0.93087  41.90375  1.000 77.64825  ? 29  ASN   A CG    1 
ATOM   166  O OD1   . ASN   A 1 29  ? 16.88718  0.28451   42.13053  1.000 74.48808  ? 29  ASN   A OD1   1 
ATOM   167  N ND2   . ASN   A 1 29  ? 15.92525  -1.53848  41.14873  1.000 83.94863  ? 29  ASN   A ND2   1 
ATOM   168  N N     . TYR   A 1 30  ? 19.81829  0.87197   43.64280  1.000 71.52967  ? 30  TYR   A N     1 
ATOM   169  C CA    . TYR   A 1 30  ? 20.81980  1.79786   43.13620  1.000 63.81093  ? 30  TYR   A CA    1 
ATOM   170  C C     . TYR   A 1 30  ? 22.22673  1.28367   43.39637  1.000 65.96431  ? 30  TYR   A C     1 
ATOM   171  O O     . TYR   A 1 30  ? 23.07919  1.31932   42.50383  1.000 70.12079  ? 30  TYR   A O     1 
ATOM   172  C CB    . TYR   A 1 30  ? 20.61814  3.16119   43.76284  1.000 61.91173  ? 30  TYR   A CB    1 
ATOM   173  C CG    . TYR   A 1 30  ? 21.20528  4.26135   42.94851  1.000 55.22517  ? 30  TYR   A CG    1 
ATOM   174  C CD1   . TYR   A 1 30  ? 20.56619  4.71364   41.80669  1.000 60.20760  ? 30  TYR   A CD1   1 
ATOM   175  C CD2   . TYR   A 1 30  ? 22.40090  4.84000   43.30497  1.000 52.89311  ? 30  TYR   A CD2   1 
ATOM   176  C CE1   . TYR   A 1 30  ? 21.09992  5.74445   41.04933  1.000 58.45835  ? 30  TYR   A CE1   1 
ATOM   177  C CE2   . TYR   A 1 30  ? 22.94468  5.86544   42.55871  1.000 56.69205  ? 30  TYR   A CE2   1 
ATOM   178  C CZ    . TYR   A 1 30  ? 22.28830  6.31995   41.43030  1.000 56.48704  ? 30  TYR   A CZ    1 
ATOM   179  O OH    . TYR   A 1 30  ? 22.82981  7.34628   40.68433  1.000 54.50579  ? 30  TYR   A OH    1 
ATOM   180  N N     . SER   A 1 31  ? 22.49215  0.81737   44.62642  1.000 71.73173  ? 31  SER   A N     1 
ATOM   181  C CA    . SER   A 1 31  ? 23.80276  0.25062   44.95262  1.000 68.84562  ? 31  SER   A CA    1 
ATOM   182  C C     . SER   A 1 31  ? 24.21787  -0.76205  43.89896  1.000 65.65524  ? 31  SER   A C     1 
ATOM   183  O O     . SER   A 1 31  ? 25.36228  -0.75845  43.44164  1.000 67.41692  ? 31  SER   A O     1 
ATOM   184  C CB    . SER   A 1 31  ? 23.77331  -0.41568  46.34144  1.000 82.99781  ? 31  SER   A CB    1 
ATOM   185  O OG    . SER   A 1 31  ? 22.67441  -1.32443  46.48962  1.000 79.82746  ? 31  SER   A OG    1 
ATOM   186  N N     . THR   A 1 32  ? 23.27157  -1.60075  43.47344  1.000 64.85657  ? 32  THR   A N     1 
ATOM   187  C CA    . THR   A 1 32  ? 23.50146  -2.73646  42.59528  1.000 65.28197  ? 32  THR   A CA    1 
ATOM   188  C C     . THR   A 1 32  ? 23.51458  -2.37526  41.10452  1.000 65.21874  ? 32  THR   A C     1 
ATOM   189  O O     . THR   A 1 32  ? 24.26451  -2.99842  40.33614  1.000 67.96709  ? 32  THR   A O     1 
ATOM   190  C CB    . THR   A 1 32  ? 22.43091  -3.80266  42.89465  1.000 69.05459  ? 32  THR   A CB    1 
ATOM   191  O OG1   . THR   A 1 32  ? 22.27918  -3.93993  44.31838  1.000 74.94639  ? 32  THR   A OG1   1 
ATOM   192  C CG2   . THR   A 1 32  ? 22.78724  -5.14882  42.27727  1.000 59.47784  ? 32  THR   A CG2   1 
ATOM   193  N N     . LEU   A 1 33  ? 22.70898  -1.39077  40.68218  1.000 58.80642  ? 33  LEU   A N     1 
ATOM   194  C CA    . LEU   A 1 33  ? 22.76561  -0.88201  39.31207  1.000 51.96710  ? 33  LEU   A CA    1 
ATOM   195  C C     . LEU   A 1 33  ? 24.10840  -0.19314  39.03084  1.000 54.09590  ? 33  LEU   A C     1 
ATOM   196  O O     . LEU   A 1 33  ? 24.69442  -0.35990  37.95752  1.000 57.75102  ? 33  LEU   A O     1 
ATOM   197  C CB    . LEU   A 1 33  ? 21.60459  0.08887   39.10309  1.000 52.05658  ? 33  LEU   A CB    1 
ATOM   198  C CG    . LEU   A 1 33  ? 20.16485  -0.45400  39.05868  1.000 48.06151  ? 33  LEU   A CG    1 
ATOM   199  C CD1   . LEU   A 1 33  ? 19.09674  0.63844   39.02800  1.000 45.86214  ? 33  LEU   A CD1   1 
ATOM   200  C CD2   . LEU   A 1 33  ? 19.96589  -1.35383  37.89438  1.000 36.28572  ? 33  LEU   A CD2   1 
ATOM   201  N N     . VAL   A 1 34  ? 24.62218  0.58464   39.98483  1.000 54.65295  ? 34  VAL   A N     1 
ATOM   202  C CA    . VAL   A 1 34  ? 25.86695  1.29670   39.74996  1.000 53.69718  ? 34  VAL   A CA    1 
ATOM   203  C C     . VAL   A 1 34  ? 26.98638  0.32633   39.45241  1.000 54.55631  ? 34  VAL   A C     1 
ATOM   204  O O     . VAL   A 1 34  ? 28.02848  0.71335   38.91195  1.000 63.21163  ? 34  VAL   A O     1 
ATOM   205  C CB    . VAL   A 1 34  ? 26.23681  2.18048   40.94866  1.000 48.51953  ? 34  VAL   A CB    1 
ATOM   206  C CG1   . VAL   A 1 34  ? 27.68913  2.65110   40.84785  1.000 48.00476  ? 34  VAL   A CG1   1 
ATOM   207  C CG2   . VAL   A 1 34  ? 25.29172  3.36283   41.00672  1.000 49.87936  ? 34  VAL   A CG2   1 
ATOM   208  N N     . ALA   A 1 35  ? 26.80259  -0.92673  39.83941  1.000 48.18040  ? 35  ALA   A N     1 
ATOM   209  C CA    . ALA   A 1 35  ? 27.64291  -2.03982  39.41361  1.000 48.09197  ? 35  ALA   A CA    1 
ATOM   210  C C     . ALA   A 1 35  ? 29.12883  -1.67912  39.46723  1.000 52.66190  ? 35  ALA   A C     1 
ATOM   211  O O     . ALA   A 1 35  ? 29.79554  -1.60621  38.41742  1.000 54.19848  ? 35  ALA   A O     1 
ATOM   212  C CB    . ALA   A 1 35  ? 27.24564  -2.50913  38.02254  1.000 52.62619  ? 35  ALA   A CB    1 
ATOM   213  N N     . PRO   A 1 36  ? 29.68771  -1.45632  40.65127  1.000 51.59156  ? 36  PRO   A N     1 
ATOM   214  C CA    . PRO   A 1 36  ? 31.10032  -1.09919  40.75458  1.000 55.07922  ? 36  PRO   A CA    1 
ATOM   215  C C     . PRO   A 1 36  ? 31.98380  -2.26927  40.38115  1.000 55.25331  ? 36  PRO   A C     1 
ATOM   216  O O     . PRO   A 1 36  ? 31.68770  -3.41709  40.72112  1.000 61.06521  ? 36  PRO   A O     1 
ATOM   217  C CB    . PRO   A 1 36  ? 31.26584  -0.76751  42.23217  1.000 55.03630  ? 36  PRO   A CB    1 
ATOM   218  C CG    . PRO   A 1 36  ? 30.34483  -1.74850  42.84407  1.000 55.79402  ? 36  PRO   A CG    1 
ATOM   219  C CD    . PRO   A 1 36  ? 29.11556  -1.71738  41.98009  1.000 51.48262  ? 36  PRO   A CD    1 
ATOM   220  N N     . TYR   A 1 37  ? 33.08814  -1.96446  39.68833  1.000 53.26693  ? 37  TYR   A N     1 
ATOM   221  C CA    . TYR   A 1 37  ? 34.07644  -2.97451  39.32311  1.000 55.73295  ? 37  TYR   A CA    1 
ATOM   222  C C     . TYR   A 1 37  ? 35.14263  -3.09044  40.39577  1.000 64.63178  ? 37  TYR   A C     1 
ATOM   223  O O     . TYR   A 1 37  ? 35.56414  -4.20222  40.74334  1.000 66.38846  ? 37  TYR   A O     1 
ATOM   224  C CB    . TYR   A 1 37  ? 34.76416  -2.65359  37.99033  1.000 54.07711  ? 37  TYR   A CB    1 
ATOM   225  C CG    . TYR   A 1 37  ? 35.66546  -3.78589  37.52437  1.000 53.09440  ? 37  TYR   A CG    1 
ATOM   226  C CD1   . TYR   A 1 37  ? 35.19269  -4.79628  36.68583  1.000 48.97846  ? 37  TYR   A CD1   1 
ATOM   227  C CD2   . TYR   A 1 37  ? 36.97927  -3.88176  37.98333  1.000 55.34532  ? 37  TYR   A CD2   1 
ATOM   228  C CE1   . TYR   A 1 37  ? 36.01896  -5.83896  36.27402  1.000 45.56625  ? 37  TYR   A CE1   1 
ATOM   229  C CE2   . TYR   A 1 37  ? 37.80337  -4.93087  37.58176  1.000 55.42093  ? 37  TYR   A CE2   1 
ATOM   230  C CZ    . TYR   A 1 37  ? 37.30999  -5.90173  36.72785  1.000 48.15770  ? 37  TYR   A CZ    1 
ATOM   231  O OH    . TYR   A 1 37  ? 38.14230  -6.92219  36.33360  1.000 57.01636  ? 37  TYR   A OH    1 
ATOM   232  N N     . ASN   A 1 38  ? 35.58749  -1.95719  40.91391  1.000 60.78697  ? 38  ASN   A N     1 
ATOM   233  C CA    . ASN   A 1 38  ? 36.44369  -1.96845  42.08174  1.000 57.91753  ? 38  ASN   A CA    1 
ATOM   234  C C     . ASN   A 1 38  ? 35.55506  -1.83999  43.30152  1.000 67.80513  ? 38  ASN   A C     1 
ATOM   235  O O     . ASN   A 1 38  ? 34.77958  -0.87653  43.41111  1.000 69.23488  ? 38  ASN   A O     1 
ATOM   236  C CB    . ASN   A 1 38  ? 37.47207  -0.86111  42.02828  1.000 61.54600  ? 38  ASN   A CB    1 
ATOM   237  C CG    . ASN   A 1 38  ? 38.50756  -1.03134  43.05729  1.000 63.73904  ? 38  ASN   A CG    1 
ATOM   238  O OD1   . ASN   A 1 38  ? 38.27009  -0.76793  44.23895  1.000 68.33804  ? 38  ASN   A OD1   1 
ATOM   239  N ND2   . ASN   A 1 38  ? 39.65096  -1.55506  42.65278  1.000 61.92382  ? 38  ASN   A ND2   1 
ATOM   240  N N     . PHE   A 1 39  ? 35.65431  -2.83086  44.19709  1.000 70.54838  ? 39  PHE   A N     1 
ATOM   241  C CA    . PHE   A 1 39  ? 34.76168  -2.94603  45.34050  1.000 68.04762  ? 39  PHE   A CA    1 
ATOM   242  C C     . PHE   A 1 39  ? 35.08011  -1.98692  46.47154  1.000 69.23065  ? 39  PHE   A C     1 
ATOM   243  O O     . PHE   A 1 39  ? 34.24519  -1.82346  47.36664  1.000 72.54046  ? 39  PHE   A O     1 
ATOM   244  C CB    . PHE   A 1 39  ? 34.78364  -4.36428  45.85694  1.000 67.62982  ? 39  PHE   A CB    1 
ATOM   245  C CG    . PHE   A 1 39  ? 33.82551  -5.22479  45.16565  1.000 67.68951  ? 39  PHE   A CG    1 
ATOM   246  C CD1   . PHE   A 1 39  ? 32.58914  -4.70100  44.78549  1.000 68.53904  ? 39  PHE   A CD1   1 
ATOM   247  C CD2   . PHE   A 1 39  ? 34.12319  -6.54438  44.89442  1.000 63.62660  ? 39  PHE   A CD2   1 
ATOM   248  C CE1   . PHE   A 1 39  ? 31.66855  -5.48138  44.14548  1.000 71.00494  ? 39  PHE   A CE1   1 
ATOM   249  C CE2   . PHE   A 1 39  ? 33.20306  -7.33688  44.24850  1.000 64.48823  ? 39  PHE   A CE2   1 
ATOM   250  C CZ    . PHE   A 1 39  ? 31.97272  -6.80672  43.87214  1.000 64.07753  ? 39  PHE   A CZ    1 
ATOM   251  N N     . ASP   A 1 40  ? 36.24084  -1.34172  46.43551  1.000 67.54251  ? 40  ASP   A N     1 
ATOM   252  C CA    . ASP   A 1 40  ? 36.66884  -0.39277  47.45297  1.000 71.24353  ? 40  ASP   A CA    1 
ATOM   253  C C     . ASP   A 1 40  ? 36.29037  1.04670   47.11017  1.000 72.79623  ? 40  ASP   A C     1 
ATOM   254  O O     . ASP   A 1 40  ? 35.88001  1.81221   47.99174  1.000 74.89355  ? 40  ASP   A O     1 
ATOM   255  C CB    . ASP   A 1 40  ? 38.17053  -0.53543  47.63754  1.000 72.00831  ? 40  ASP   A CB    1 
ATOM   256  C CG    . ASP   A 1 40  ? 38.54574  -1.95516  47.98836  1.000 83.83345  ? 40  ASP   A CG    1 
ATOM   257  O OD1   . ASP   A 1 40  ? 37.98529  -2.45376  48.99995  1.000 84.36235  ? 40  ASP   A OD1   1 
ATOM   258  O OD2   . ASP   A 1 40  ? 39.34715  -2.58368  47.24506  1.000 81.06586  ? 40  ASP   A OD2   1 
ATOM   259  N N     . LEU   A 1 41  ? 36.36953  1.42429   45.84136  1.000 64.47670  ? 41  LEU   A N     1 
ATOM   260  C CA    . LEU   A 1 41  ? 36.12879  2.80847   45.44982  1.000 60.99951  ? 41  LEU   A CA    1 
ATOM   261  C C     . LEU   A 1 41  ? 34.66185  3.01682   45.07725  1.000 64.32836  ? 41  LEU   A C     1 
ATOM   262  O O     . LEU   A 1 41  ? 34.31291  3.47255   43.99283  1.000 62.84513  ? 41  LEU   A O     1 
ATOM   263  C CB    . LEU   A 1 41  ? 37.06262  3.17958   44.31301  1.000 60.96870  ? 41  LEU   A CB    1 
ATOM   264  C CG    . LEU   A 1 41  ? 38.49508  3.20213   44.82299  1.000 64.42582  ? 41  LEU   A CG    1 
ATOM   265  C CD1   . LEU   A 1 41  ? 39.55400  2.88244   43.73646  1.000 60.12384  ? 41  LEU   A CD1   1 
ATOM   266  C CD2   . LEU   A 1 41  ? 38.70271  4.58038   45.43606  1.000 63.11673  ? 41  LEU   A CD2   1 
ATOM   267  N N     . LEU   A 1 42  ? 33.78203  2.67625   46.01109  1.000 67.04356  ? 42  LEU   A N     1 
ATOM   268  C CA    . LEU   A 1 42  ? 32.36367  2.78804   45.71705  1.000 62.82923  ? 42  LEU   A CA    1 
ATOM   269  C C     . LEU   A 1 42  ? 31.99716  4.24172   45.45049  1.000 56.62726  ? 42  LEU   A C     1 
ATOM   270  O O     . LEU   A 1 42  ? 32.55489  5.16147   46.05126  1.000 62.55415  ? 42  LEU   A O     1 
ATOM   271  C CB    . LEU   A 1 42  ? 31.52206  2.21805   46.86106  1.000 66.66292  ? 42  LEU   A CB    1 
ATOM   272  C CG    . LEU   A 1 42  ? 31.89523  0.77931   47.27736  1.000 69.74152  ? 42  LEU   A CG    1 
ATOM   273  C CD1   . LEU   A 1 42  ? 30.72365  0.09505   47.98251  1.000 73.65995  ? 42  LEU   A CD1   1 
ATOM   274  C CD2   . LEU   A 1 42  ? 32.46940  -0.08634  46.13687  1.000 58.84342  ? 42  LEU   A CD2   1 
ATOM   275  N N     . THR   A 1 43  ? 31.04921  4.44188   44.53078  1.000 58.69400  ? 43  THR   A N     1 
ATOM   276  C CA    . THR   A 1 43  ? 30.65883  5.76424   44.02306  1.000 58.45489  ? 43  THR   A CA    1 
ATOM   277  C C     . THR   A 1 43  ? 29.13513  5.89711   44.01120  1.000 50.70486  ? 43  THR   A C     1 
ATOM   278  O O     . THR   A 1 43  ? 28.42549  4.91697   43.78223  1.000 53.87795  ? 43  THR   A O     1 
ATOM   279  C CB    . THR   A 1 43  ? 31.18438  5.97804   42.58055  1.000 63.20471  ? 43  THR   A CB    1 
ATOM   280  O OG1   . THR   A 1 43  ? 30.65940  4.94838   41.72371  1.000 68.35866  ? 43  THR   A OG1   1 
ATOM   281  C CG2   . THR   A 1 43  ? 32.72033  5.92248   42.52698  1.000 58.01866  ? 43  THR   A CG2   1 
ATOM   282  N N     . THR   A 1 44  ? 28.61993  7.10173   44.24132  1.000 53.07341  ? 44  THR   A N     1 
ATOM   283  C CA    . THR   A 1 44  ? 27.18706  7.36808   44.04363  1.000 56.24053  ? 44  THR   A CA    1 
ATOM   284  C C     . THR   A 1 44  ? 26.96507  8.44136   42.97557  1.000 56.10236  ? 44  THR   A C     1 
ATOM   285  O O     . THR   A 1 44  ? 27.16549  9.64905   43.22899  1.000 52.25449  ? 44  THR   A O     1 
ATOM   286  C CB    . THR   A 1 44  ? 26.46657  7.74218   45.34825  1.000 54.41607  ? 44  THR   A CB    1 
ATOM   287  O OG1   . THR   A 1 44  ? 26.63348  6.69176   46.31129  1.000 60.27103  ? 44  THR   A OG1   1 
ATOM   288  C CG2   . THR   A 1 44  ? 24.94649  7.92996   45.11940  1.000 57.00758  ? 44  THR   A CG2   1 
ATOM   289  N N     . PRO   A 1 45  ? 26.58211  8.03600   41.76274  1.000 53.36389  ? 45  PRO   A N     1 
ATOM   290  C CA    . PRO   A 1 45  ? 26.22112  9.00156   40.73103  1.000 52.73486  ? 45  PRO   A CA    1 
ATOM   291  C C     . PRO   A 1 45  ? 24.99586  9.78429   41.14704  1.000 52.56498  ? 45  PRO   A C     1 
ATOM   292  O O     . PRO   A 1 45  ? 24.19421  9.34469   41.96334  1.000 52.85020  ? 45  PRO   A O     1 
ATOM   293  C CB    . PRO   A 1 45  ? 25.90830  8.12397   39.50995  1.000 52.20623  ? 45  PRO   A CB    1 
ATOM   294  C CG    . PRO   A 1 45  ? 26.60031  6.83889   39.76883  1.000 53.66487  ? 45  PRO   A CG    1 
ATOM   295  C CD    . PRO   A 1 45  ? 26.56919  6.65451   41.25604  1.000 55.71038  ? 45  PRO   A CD    1 
ATOM   296  N N     . SER   A 1 46  ? 24.85830  10.95701  40.54787  1.000 51.19960  ? 46  SER   A N     1 
ATOM   297  C CA    . SER   A 1 46  ? 23.67985  11.77280  40.76425  1.000 53.76778  ? 46  SER   A CA    1 
ATOM   298  C C     . SER   A 1 46  ? 22.42946  11.11233  40.17888  1.000 52.35577  ? 46  SER   A C     1 
ATOM   299  O O     . SER   A 1 46  ? 21.33938  11.23994  40.75122  1.000 58.65554  ? 46  SER   A O     1 
ATOM   300  C CB    . SER   A 1 46  ? 23.93510  13.15525  40.16843  1.000 61.44861  ? 46  SER   A CB    1 
ATOM   301  O OG    . SER   A 1 46  ? 25.00334  13.78952  40.86792  1.000 65.49171  ? 46  SER   A OG    1 
ATOM   302  N N     . ALA   A 1 47  ? 22.57827  10.40544  39.06015  1.000 48.31499  ? 47  ALA   A N     1 
ATOM   303  C CA    . ALA   A 1 47  ? 21.54219  9.59514   38.42703  1.000 48.74372  ? 47  ALA   A CA    1 
ATOM   304  C C     . ALA   A 1 47  ? 22.24568  8.59645   37.51794  1.000 47.20733  ? 47  ALA   A C     1 
ATOM   305  O O     . ALA   A 1 47  ? 23.47133  8.59683   37.40408  1.000 46.26622  ? 47  ALA   A O     1 
ATOM   306  C CB    . ALA   A 1 47  ? 20.52954  10.43103  37.63143  1.000 39.33830  ? 47  ALA   A CB    1 
ATOM   307  N N     . ILE   A 1 48  ? 21.45418  7.71887   36.90822  1.000 44.36227  ? 48  ILE   A N     1 
ATOM   308  C CA    . ILE   A 1 48  ? 21.90860  6.77074   35.90126  1.000 38.14755  ? 48  ILE   A CA    1 
ATOM   309  C C     . ILE   A 1 48  ? 20.81576  6.67433   34.86611  1.000 46.84545  ? 48  ILE   A C     1 
ATOM   310  O O     . ILE   A 1 48  ? 19.64204  6.49152   35.19725  1.000 55.08787  ? 48  ILE   A O     1 
ATOM   311  C CB    . ILE   A 1 48  ? 22.20097  5.35038   36.42639  1.000 45.12831  ? 48  ILE   A CB    1 
ATOM   312  C CG1   . ILE   A 1 48  ? 23.14334  5.33418   37.61122  1.000 46.18886  ? 48  ILE   A CG1   1 
ATOM   313  C CG2   . ILE   A 1 48  ? 22.77119  4.46618   35.31415  1.000 50.82700  ? 48  ILE   A CG2   1 
ATOM   314  C CD1   . ILE   A 1 48  ? 23.32181  3.95494   38.19110  1.000 45.03137  ? 48  ILE   A CD1   1 
ATOM   315  N N     . VAL   A 1 49  ? 21.20776  6.74862   33.61536  1.000 48.47157  ? 49  VAL   A N     1 
ATOM   316  C CA    . VAL   A 1 49  ? 20.27887  6.74799   32.50458  1.000 45.85088  ? 49  VAL   A CA    1 
ATOM   317  C C     . VAL   A 1 49  ? 20.79155  5.76253   31.45944  1.000 51.83102  ? 49  VAL   A C     1 
ATOM   318  O O     . VAL   A 1 49  ? 22.00326  5.63562   31.23120  1.000 49.59436  ? 49  VAL   A O     1 
ATOM   319  C CB    . VAL   A 1 49  ? 20.12492  8.18901   31.97988  1.000 45.75559  ? 49  VAL   A CB    1 
ATOM   320  C CG1   . VAL   A 1 49  ? 21.48933  8.76844   31.66044  1.000 43.99945  ? 49  VAL   A CG1   1 
ATOM   321  C CG2   . VAL   A 1 49  ? 19.24687  8.20371   30.75048  1.000 52.39837  ? 49  VAL   A CG2   1 
ATOM   322  N N     . TRP   A 1 50  ? 19.86638  4.99820   30.88177  1.000 51.11380  ? 50  TRP   A N     1 
ATOM   323  C CA    . TRP   A 1 50  ? 20.17040  4.03497   29.82697  1.000 50.87147  ? 50  TRP   A CA    1 
ATOM   324  C C     . TRP   A 1 50  ? 19.61148  4.58006   28.52652  1.000 46.80773  ? 50  TRP   A C     1 
ATOM   325  O O     . TRP   A 1 50  ? 18.51276  4.20237   28.12126  1.000 53.05537  ? 50  TRP   A O     1 
ATOM   326  C CB    . TRP   A 1 50  ? 19.58241  2.65543   30.13859  1.000 48.20560  ? 50  TRP   A CB    1 
ATOM   327  C CG    . TRP   A 1 50  ? 20.27798  1.91618   31.21621  1.000 49.10903  ? 50  TRP   A CG    1 
ATOM   328  C CD1   . TRP   A 1 50  ? 21.14729  0.86459   31.05854  1.000 50.88809  ? 50  TRP   A CD1   1 
ATOM   329  C CD2   . TRP   A 1 50  ? 20.18268  2.14685   32.61878  1.000 53.62761  ? 50  TRP   A CD2   1 
ATOM   330  N NE1   . TRP   A 1 50  ? 21.58604  0.41710   32.28915  1.000 47.45323  ? 50  TRP   A NE1   1 
ATOM   331  C CE2   . TRP   A 1 50  ? 21.01592  1.19930   33.25989  1.000 50.12286  ? 50  TRP   A CE2   1 
ATOM   332  C CE3   . TRP   A 1 50  ? 19.48339  3.06866   33.40271  1.000 53.52958  ? 50  TRP   A CE3   1 
ATOM   333  C CZ2   . TRP   A 1 50  ? 21.17326  1.16115   34.64497  1.000 47.66968  ? 50  TRP   A CZ2   1 
ATOM   334  C CZ3   . TRP   A 1 50  ? 19.63986  3.02104   34.79096  1.000 50.66375  ? 50  TRP   A CZ3   1 
ATOM   335  C CH2   . TRP   A 1 50  ? 20.47982  2.07648   35.38990  1.000 46.33427  ? 50  TRP   A CH2   1 
ATOM   336  N N     . PRO   A 1 51  ? 20.32655  5.44426   27.82080  1.000 47.74564  ? 51  PRO   A N     1 
ATOM   337  C CA    . PRO   A 1 51  ? 19.81959  5.91136   26.52240  1.000 49.55974  ? 51  PRO   A CA    1 
ATOM   338  C C     . PRO   A 1 51  ? 19.71254  4.75682   25.53781  1.000 55.12632  ? 51  PRO   A C     1 
ATOM   339  O O     . PRO   A 1 51  ? 20.36890  3.70134   25.66983  1.000 52.43662  ? 51  PRO   A O     1 
ATOM   340  C CB    . PRO   A 1 51  ? 20.84451  6.95083   26.06600  1.000 44.17483  ? 51  PRO   A CB    1 
ATOM   341  C CG    . PRO   A 1 51  ? 22.05721  6.68375   26.90250  1.000 52.12120  ? 51  PRO   A CG    1 
ATOM   342  C CD    . PRO   A 1 51  ? 21.61476  6.05172   28.18643  1.000 51.33483  ? 51  PRO   A CD    1 
ATOM   343  N N     . GLN   A 1 52  ? 18.80179  4.97133   24.57653  1.000 50.99295  ? 52  GLN   A N     1 
ATOM   344  C CA    . GLN   A 1 52  ? 18.39142  4.04532   23.52895  1.000 55.40023  ? 52  GLN   A CA    1 
ATOM   345  C C     . GLN   A 1 52  ? 19.23720  4.19106   22.27502  1.000 55.52566  ? 52  GLN   A C     1 
ATOM   346  O O     . GLN   A 1 52  ? 19.68576  3.19379   21.69690  1.000 53.90894  ? 52  GLN   A O     1 
ATOM   347  C CB    . GLN   A 1 52  ? 16.92678  4.28393   23.15271  1.000 55.21266  ? 52  GLN   A CB    1 
ATOM   348  C CG    . GLN   A 1 52  ? 16.27912  3.15101   22.34942  1.000 59.76931  ? 52  GLN   A CG    1 
ATOM   349  C CD    . GLN   A 1 52  ? 16.02119  1.92153   23.20493  1.000 76.23428  ? 52  GLN   A CD    1 
ATOM   350  O OE1   . GLN   A 1 52  ? 15.06443  1.88847   23.97164  1.000 83.20965  ? 52  GLN   A OE1   1 
ATOM   351  N NE2   . GLN   A 1 52  ? 16.87859  0.90717   23.08252  1.000 74.97866  ? 52  GLN   A NE2   1 
ATOM   352  N N     . ASP   A 1 53  ? 19.47448  5.43470   21.87293  1.000 54.41564  ? 53  ASP   A N     1 
ATOM   353  C CA    . ASP   A 1 53  ? 20.09718  5.79675   20.61324  1.000 51.37029  ? 53  ASP   A CA    1 
ATOM   354  C C     . ASP   A 1 53  ? 20.98064  7.03408   20.85920  1.000 50.65520  ? 53  ASP   A C     1 
ATOM   355  O O     . ASP   A 1 53  ? 21.25014  7.40116   22.00592  1.000 49.42775  ? 53  ASP   A O     1 
ATOM   356  C CB    . ASP   A 1 53  ? 19.00199  6.02442   19.56055  1.000 61.30509  ? 53  ASP   A CB    1 
ATOM   357  C CG    . ASP   A 1 53  ? 18.07541  7.22460   19.89634  1.000 64.82343  ? 53  ASP   A CG    1 
ATOM   358  O OD1   . ASP   A 1 53  ? 18.61839  8.30112   20.20203  1.000 71.52341  ? 53  ASP   A OD1   1 
ATOM   359  O OD2   . ASP   A 1 53  ? 16.81959  7.12475   19.83264  1.000 61.89096  ? 53  ASP   A OD2   1 
ATOM   360  N N     . THR   A 1 54  ? 21.41506  7.71398   19.78855  1.000 53.13317  ? 54  THR   A N     1 
ATOM   361  C CA    . THR   A 1 54  ? 22.28053  8.87725   19.95834  1.000 49.95219  ? 54  THR   A CA    1 
ATOM   362  C C     . THR   A 1 54  ? 21.50492  10.12307  20.39791  1.000 51.32482  ? 54  THR   A C     1 
ATOM   363  O O     . THR   A 1 54  ? 21.95114  10.84305  21.29555  1.000 54.75762  ? 54  THR   A O     1 
ATOM   364  C CB    . THR   A 1 54  ? 23.10896  9.15645   18.68137  1.000 46.75446  ? 54  THR   A CB    1 
ATOM   365  O OG1   . THR   A 1 54  ? 23.96700  8.03805   18.40445  1.000 40.24211  ? 54  THR   A OG1   1 
ATOM   366  C CG2   . THR   A 1 54  ? 23.96300  10.40701  18.84019  1.000 46.92553  ? 54  THR   A CG2   1 
ATOM   367  N N     . GLN   A 1 55  ? 20.33208  10.40675  19.82838  1.000 56.66741  ? 55  GLN   A N     1 
ATOM   368  C CA    . GLN   A 1 55  ? 19.63040  11.61593  20.28444  1.000 61.04316  ? 55  GLN   A CA    1 
ATOM   369  C C     . GLN   A 1 55  ? 19.34329  11.54834  21.77640  1.000 55.08314  ? 55  GLN   A C     1 
ATOM   370  O O     . GLN   A 1 55  ? 19.27505  12.58459  22.44370  1.000 60.17664  ? 55  GLN   A O     1 
ATOM   371  C CB    . GLN   A 1 55  ? 18.31433  11.82863  19.53633  1.000 62.20557  ? 55  GLN   A CB    1 
ATOM   372  C CG    . GLN   A 1 55  ? 17.29814  10.76137  19.83301  1.000 68.08932  ? 55  GLN   A CG    1 
ATOM   373  C CD    . GLN   A 1 55  ? 16.02033  10.92363  19.05449  1.000 84.29121  ? 55  GLN   A CD    1 
ATOM   374  O OE1   . GLN   A 1 55  ? 16.00292  11.59253  18.01804  1.000 95.79741  ? 55  GLN   A OE1   1 
ATOM   375  N NE2   . GLN   A 1 55  ? 14.94878  10.29080  19.52494  1.000 91.11990  ? 55  GLN   A NE2   1 
ATOM   376  N N     . GLN   A 1 56  ? 19.19137  10.34498  22.31754  1.000 51.06409  ? 56  GLN   A N     1 
ATOM   377  C CA    . GLN   A 1 56  ? 18.91276  10.21775  23.73156  1.000 48.19651  ? 56  GLN   A CA    1 
ATOM   378  C C     . GLN   A 1 56  ? 20.15978  10.47641  24.57313  1.000 54.54189  ? 56  GLN   A C     1 
ATOM   379  O O     . GLN   A 1 56  ? 20.06160  10.99570  25.69153  1.000 53.45077  ? 56  GLN   A O     1 
ATOM   380  C CB    . GLN   A 1 56  ? 18.33886  8.83938   23.99336  1.000 51.35681  ? 56  GLN   A CB    1 
ATOM   381  C CG    . GLN   A 1 56  ? 16.96158  8.61928   23.39985  1.000 53.67447  ? 56  GLN   A CG    1 
ATOM   382  C CD    . GLN   A 1 56  ? 16.21049  7.48585   24.08818  1.000 59.17460  ? 56  GLN   A CD    1 
ATOM   383  O OE1   . GLN   A 1 56  ? 16.77987  6.73558   24.89616  1.000 57.56370  ? 56  GLN   A OE1   1 
ATOM   384  N NE2   . GLN   A 1 56  ? 14.91595  7.39046   23.81233  1.000 55.19076  ? 56  GLN   A NE2   1 
ATOM   385  N N     . VAL   A 1 57  ? 21.34254  10.12008  24.06800  1.000 54.96047  ? 57  VAL   A N     1 
ATOM   386  C CA    . VAL   A 1 57  ? 22.55268  10.52172  24.76715  1.000 50.75923  ? 57  VAL   A CA    1 
ATOM   387  C C     . VAL   A 1 57  ? 22.69186  12.03785  24.69682  1.000 53.68880  ? 57  VAL   A C     1 
ATOM   388  O O     . VAL   A 1 57  ? 23.02157  12.69060  25.69760  1.000 56.30805  ? 57  VAL   A O     1 
ATOM   389  C CB    . VAL   A 1 57  ? 23.79401  9.81223   24.19264  1.000 48.26796  ? 57  VAL   A CB    1 
ATOM   390  C CG1   . VAL   A 1 57  ? 25.08746  10.46065  24.74782  1.000 45.11780  ? 57  VAL   A CG1   1 
ATOM   391  C CG2   . VAL   A 1 57  ? 23.73958  8.31724   24.43485  1.000 43.46019  ? 57  VAL   A CG2   1 
ATOM   392  N N     . ALA   A 1 58  ? 22.43571  12.62782  23.51969  1.000 49.28512  ? 58  ALA   A N     1 
ATOM   393  C CA    . ALA   A 1 58  ? 22.52143  14.07692  23.40821  1.000 48.24933  ? 58  ALA   A CA    1 
ATOM   394  C C     . ALA   A 1 58  ? 21.60070  14.72438  24.41913  1.000 53.60190  ? 58  ALA   A C     1 
ATOM   395  O O     . ALA   A 1 58  ? 22.02726  15.56395  25.22069  1.000 51.37092  ? 58  ALA   A O     1 
ATOM   396  C CB    . ALA   A 1 58  ? 22.16951  14.53204  21.99143  1.000 46.82906  ? 58  ALA   A CB    1 
ATOM   397  N N     . ALA   A 1 59  ? 20.33788  14.28957  24.42519  1.000 54.25895  ? 59  ALA   A N     1 
ATOM   398  C CA    . ALA   A 1 59  ? 19.34124  14.79742  25.36450  1.000 51.27837  ? 59  ALA   A CA    1 
ATOM   399  C C     . ALA   A 1 59  ? 19.79565  14.66782  26.80815  1.000 51.00712  ? 59  ALA   A C     1 
ATOM   400  O O     . ALA   A 1 59  ? 19.82288  15.65646  27.55210  1.000 52.70069  ? 59  ALA   A O     1 
ATOM   401  C CB    . ALA   A 1 59  ? 18.04208  14.03983  25.18188  1.000 50.78127  ? 59  ALA   A CB    1 
ATOM   402  N N     . ALA   A 1 60  ? 20.11958  13.44370  27.23742  1.000 50.98859  ? 60  ALA   A N     1 
ATOM   403  C CA    . ALA   A 1 60  ? 20.56037  13.25644  28.61588  1.000 53.00903  ? 60  ALA   A CA    1 
ATOM   404  C C     . ALA   A 1 60  ? 21.68560  14.22749  28.97777  1.000 55.17947  ? 60  ALA   A C     1 
ATOM   405  O O     . ALA   A 1 60  ? 21.67773  14.82329  30.06031  1.000 55.38457  ? 60  ALA   A O     1 
ATOM   406  C CB    . ALA   A 1 60  ? 20.98976  11.80221  28.84523  1.000 45.19466  ? 60  ALA   A CB    1 
ATOM   407  N N     . VAL   A 1 61  ? 22.64382  14.43900  28.07311  1.000 53.04298  ? 61  VAL   A N     1 
ATOM   408  C CA    . VAL   A 1 61  ? 23.78824  15.26705  28.43860  1.000 52.75288  ? 61  VAL   A CA    1 
ATOM   409  C C     . VAL   A 1 61  ? 23.32951  16.68969  28.74689  1.000 54.10675  ? 61  VAL   A C     1 
ATOM   410  O O     . VAL   A 1 61  ? 23.73577  17.27739  29.75357  1.000 57.30725  ? 61  VAL   A O     1 
ATOM   411  C CB    . VAL   A 1 61  ? 24.86682  15.23108  27.34196  1.000 51.71363  ? 61  VAL   A CB    1 
ATOM   412  C CG1   . VAL   A 1 61  ? 25.94298  16.23994  27.65499  1.000 47.67339  ? 61  VAL   A CG1   1 
ATOM   413  C CG2   . VAL   A 1 61  ? 25.46306  13.83423  27.22587  1.000 46.94299  ? 61  VAL   A CG2   1 
ATOM   414  N N     . LYS   A 1 62  ? 22.46094  17.26024  27.89589  1.000 54.11428  ? 62  LYS   A N     1 
ATOM   415  C CA    . LYS   A 1 62  ? 21.88638  18.56712  28.20791  1.000 52.79333  ? 62  LYS   A CA    1 
ATOM   416  C C     . LYS   A 1 62  ? 21.22583  18.55230  29.58436  1.000 56.66836  ? 62  LYS   A C     1 
ATOM   417  O O     . LYS   A 1 62  ? 21.45966  19.46167  30.39486  1.000 57.80085  ? 62  LYS   A O     1 
ATOM   418  C CB    . LYS   A 1 62  ? 20.88429  19.01985  27.14119  1.000 47.96348  ? 62  LYS   A CB    1 
ATOM   419  C CG    . LYS   A 1 62  ? 20.66376  20.52123  27.19457  1.000 47.70872  ? 62  LYS   A CG    1 
ATOM   420  C CD    . LYS   A 1 62  ? 20.17130  21.06982  25.87964  1.000 59.89487  ? 62  LYS   A CD    1 
ATOM   421  C CE    . LYS   A 1 62  ? 20.17459  22.61589  25.81611  1.000 76.72726  ? 62  LYS   A CE    1 
ATOM   422  N NZ    . LYS   A 1 62  ? 19.10827  23.35879  26.56872  1.000 77.00357  ? 62  LYS   A NZ    1 
ATOM   423  N N     . CYS   A 1 63  ? 20.43841  17.50821  29.89288  1.000 52.03226  ? 63  CYS   A N     1 
ATOM   424  C CA    . CYS   A 1 63  ? 19.83920  17.43561  31.22020  1.000 50.09284  ? 63  CYS   A CA    1 
ATOM   425  C C     . CYS   A 1 63  ? 20.85189  17.71510  32.32325  1.000 56.21562  ? 63  CYS   A C     1 
ATOM   426  O O     . CYS   A 1 63  ? 20.56562  18.48615  33.24091  1.000 60.74840  ? 63  CYS   A O     1 
ATOM   427  C CB    . CYS   A 1 63  ? 19.14104  16.09363  31.44802  1.000 53.76693  ? 63  CYS   A CB    1 
ATOM   428  S SG    . CYS   A 1 63  ? 17.45190  16.03572  30.73302  1.000 74.40608  ? 63  CYS   A SG    1 
ATOM   429  N N     . ALA   A 1 64  ? 22.06024  17.13421  32.24171  1.000 53.48509  ? 64  ALA   A N     1 
ATOM   430  C CA    . ALA   A 1 64  ? 23.06243  17.40819  33.27250  1.000 53.20579  ? 64  ALA   A CA    1 
ATOM   431  C C     . ALA   A 1 64  ? 23.61001  18.82806  33.16445  1.000 55.62900  ? 64  ALA   A C     1 
ATOM   432  O O     . ALA   A 1 64  ? 23.92133  19.46030  34.18332  1.000 55.95793  ? 64  ALA   A O     1 
ATOM   433  C CB    . ALA   A 1 64  ? 24.20793  16.39753  33.19387  1.000 54.81814  ? 64  ALA   A CB    1 
ATOM   434  N N     . VAL   A 1 65  ? 23.73220  19.34908  31.94698  1.000 52.92386  ? 65  VAL   A N     1 
ATOM   435  C CA    . VAL   A 1 65  ? 24.31980  20.67060  31.77358  1.000 56.01434  ? 65  VAL   A CA    1 
ATOM   436  C C     . VAL   A 1 65  ? 23.37114  21.73049  32.29319  1.000 56.88368  ? 65  VAL   A C     1 
ATOM   437  O O     . VAL   A 1 65  ? 23.79488  22.74241  32.86976  1.000 60.15126  ? 65  VAL   A O     1 
ATOM   438  C CB    . VAL   A 1 65  ? 24.66997  20.91611  30.29331  1.000 53.23382  ? 65  VAL   A CB    1 
ATOM   439  C CG1   . VAL   A 1 65  ? 24.82838  22.40941  30.03349  1.000 52.82177  ? 65  VAL   A CG1   1 
ATOM   440  C CG2   . VAL   A 1 65  ? 25.91026  20.12565  29.88235  1.000 45.76227  ? 65  VAL   A CG2   1 
ATOM   441  N N     . ASP   A 1 66  ? 22.07064  21.52096  32.08013  1.000 55.80036  ? 66  ASP   A N     1 
ATOM   442  C CA    . ASP   A 1 66  ? 21.06971  22.48732  32.52237  1.000 62.17953  ? 66  ASP   A CA    1 
ATOM   443  C C     . ASP   A 1 66  ? 21.09698  22.68282  34.03957  1.000 65.08294  ? 66  ASP   A C     1 
ATOM   444  O O     . ASP   A 1 66  ? 20.78363  23.78219  34.51914  1.000 71.39169  ? 66  ASP   A O     1 
ATOM   445  C CB    . ASP   A 1 66  ? 19.67353  22.05944  32.04153  1.000 65.86342  ? 66  ASP   A CB    1 
ATOM   446  C CG    . ASP   A 1 66  ? 19.48677  22.18947  30.50784  1.000 71.16872  ? 66  ASP   A CG    1 
ATOM   447  O OD1   . ASP   A 1 66  ? 20.44911  22.60219  29.80438  1.000 73.49795  ? 66  ASP   A OD1   1 
ATOM   448  O OD2   . ASP   A 1 66  ? 18.37312  21.87389  30.00111  1.000 68.42436  ? 66  ASP   A OD2   1 
ATOM   449  N N     . SER   A 1 67  ? 21.51272  21.64938  34.80018  1.000 62.88511  ? 67  SER   A N     1 
ATOM   450  C CA    . SER   A 1 67  ? 21.55156  21.63372  36.27204  1.000 59.70928  ? 67  SER   A CA    1 
ATOM   451  C C     . SER   A 1 67  ? 22.98220  21.52432  36.80306  1.000 62.83079  ? 67  SER   A C     1 
ATOM   452  O O     . SER   A 1 67  ? 23.23276  20.89188  37.83974  1.000 60.70159  ? 67  SER   A O     1 
ATOM   453  C CB    . SER   A 1 67  ? 20.70403  20.49535  36.84472  1.000 56.04474  ? 67  SER   A CB    1 
ATOM   454  O OG    . SER   A 1 67  ? 19.50984  20.27281  36.10557  1.000 58.96403  ? 67  SER   A OG    1 
ATOM   455  N N     . ASP   A 1 68  ? 23.92381  22.14111  36.08460  1.000 63.44959  ? 68  ASP   A N     1 
ATOM   456  C CA    . ASP   A 1 68  ? 25.34794  22.23550  36.43980  1.000 54.77709  ? 68  ASP   A CA    1 
ATOM   457  C C     . ASP   A 1 68  ? 25.87032  20.91876  37.05365  1.000 53.38950  ? 68  ASP   A C     1 
ATOM   458  O O     . ASP   A 1 68  ? 26.38520  20.87915  38.16498  1.000 51.41067  ? 68  ASP   A O     1 
ATOM   459  C CB    . ASP   A 1 68  ? 25.59643  23.44125  37.36765  1.000 63.57750  ? 68  ASP   A CB    1 
ATOM   460  C CG    . ASP   A 1 68  ? 25.37954  24.83803  36.66328  1.000 81.04307  ? 68  ASP   A CG    1 
ATOM   461  O OD1   . ASP   A 1 68  ? 25.31256  24.92643  35.40078  1.000 84.12161  ? 68  ASP   A OD1   1 
ATOM   462  O OD2   . ASP   A 1 68  ? 25.34488  25.87507  37.38259  1.000 82.43071  ? 68  ASP   A OD2   1 
ATOM   463  N N     . ILE   A 1 69  ? 25.71270  19.81545  36.29949  1.000 59.80576  ? 69  ILE   A N     1 
ATOM   464  C CA    . ILE   A 1 69  ? 26.21235  18.49493  36.69751  1.000 53.92315  ? 69  ILE   A CA    1 
ATOM   465  C C     . ILE   A 1 69  ? 27.12076  17.96154  35.59198  1.000 57.74984  ? 69  ILE   A C     1 
ATOM   466  O O     . ILE   A 1 69  ? 26.87709  18.18218  34.39891  1.000 55.21069  ? 69  ILE   A O     1 
ATOM   467  C CB    . ILE   A 1 69  ? 25.09082  17.47375  36.97394  1.000 57.92513  ? 69  ILE   A CB    1 
ATOM   468  C CG1   . ILE   A 1 69  ? 24.25761  17.86400  38.18881  1.000 57.17811  ? 69  ILE   A CG1   1 
ATOM   469  C CG2   . ILE   A 1 69  ? 25.70640  16.16501  37.35537  1.000 59.39061  ? 69  ILE   A CG2   1 
ATOM   470  C CD1   . ILE   A 1 69  ? 22.97101  17.11877  38.25116  1.000 59.21062  ? 69  ILE   A CD1   1 
ATOM   471  N N     . LYS   A 1 70  ? 28.17501  17.25018  35.99982  1.000 55.56338  ? 70  LYS   A N     1 
ATOM   472  C CA    . LYS   A 1 70  ? 29.17479  16.71645  35.08467  1.000 49.14129  ? 70  LYS   A CA    1 
ATOM   473  C C     . LYS   A 1 70  ? 28.83732  15.28063  34.72004  1.000 53.04967  ? 70  LYS   A C     1 
ATOM   474  O O     . LYS   A 1 70  ? 27.99985  14.62847  35.35075  1.000 58.79437  ? 70  LYS   A O     1 
ATOM   475  C CB    . LYS   A 1 70  ? 30.55668  16.79686  35.71245  1.000 47.70431  ? 70  LYS   A CB    1 
ATOM   476  C CG    . LYS   A 1 70  ? 30.97363  18.21566  35.86379  1.000 50.75489  ? 70  LYS   A CG    1 
ATOM   477  C CD    . LYS   A 1 70  ? 32.34163  18.34462  36.46488  1.000 51.84598  ? 70  LYS   A CD    1 
ATOM   478  C CE    . LYS   A 1 70  ? 32.63731  19.82079  36.64419  1.000 54.28427  ? 70  LYS   A CE    1 
ATOM   479  N NZ    . LYS   A 1 70  ? 32.39418  20.59553  35.39591  1.000 44.80843  ? 70  LYS   A NZ    1 
ATOM   480  N N     . VAL   A 1 71  ? 29.50718  14.76960  33.69060  1.000 49.98388  ? 71  VAL   A N     1 
ATOM   481  C CA    . VAL   A 1 71  ? 29.02666  13.56993  33.00397  1.000 49.61412  ? 71  VAL   A CA    1 
ATOM   482  C C     . VAL   A 1 71  ? 30.18232  12.60034  32.75726  1.000 47.86888  ? 71  VAL   A C     1 
ATOM   483  O O     . VAL   A 1 71  ? 31.30876  13.01544  32.44163  1.000 48.08832  ? 71  VAL   A O     1 
ATOM   484  C CB    . VAL   A 1 71  ? 28.30929  13.93732  31.68464  1.000 39.95486  ? 71  VAL   A CB    1 
ATOM   485  C CG1   . VAL   A 1 71  ? 27.87160  12.69309  30.99219  1.000 40.02412  ? 71  VAL   A CG1   1 
ATOM   486  C CG2   . VAL   A 1 71  ? 27.11759  14.84299  31.94018  1.000 37.57584  ? 71  VAL   A CG2   1 
ATOM   487  N N     . GLN   A 1 72  ? 29.89388  11.29353  32.88882  1.000 39.93460  ? 72  GLN   A N     1 
ATOM   488  C CA    . GLN   A 1 72  ? 30.83372  10.27356  32.47790  1.000 37.80717  ? 72  GLN   A CA    1 
ATOM   489  C C     . GLN   A 1 72  ? 30.02092  9.13155   31.87457  1.000 41.29924  ? 72  GLN   A C     1 
ATOM   490  O O     . GLN   A 1 72  ? 29.08317  8.63581   32.50855  1.000 44.18720  ? 72  GLN   A O     1 
ATOM   491  C CB    . GLN   A 1 72  ? 31.70245  9.77550   33.63535  1.000 39.05023  ? 72  GLN   A CB    1 
ATOM   492  C CG    . GLN   A 1 72  ? 32.90383  10.69098  33.90874  1.000 42.13828  ? 72  GLN   A CG    1 
ATOM   493  C CD    . GLN   A 1 72  ? 33.97593  10.59271  32.82817  1.000 43.26133  ? 72  GLN   A CD    1 
ATOM   494  O OE1   . GLN   A 1 72  ? 34.89461  9.75700   32.89983  1.000 40.35386  ? 72  GLN   A OE1   1 
ATOM   495  N NE2   . GLN   A 1 72  ? 33.82864  11.41589  31.79140  1.000 36.62868  ? 72  GLN   A NE2   1 
ATOM   496  N N     . PRO   A 1 73  ? 30.32276  8.69944   30.65760  1.000 43.11651  ? 73  PRO   A N     1 
ATOM   497  C CA    . PRO   A 1 73  ? 29.64868  7.51344   30.12148  1.000 45.46730  ? 73  PRO   A CA    1 
ATOM   498  C C     . PRO   A 1 73  ? 30.23007  6.23586   30.70830  1.000 43.58484  ? 73  PRO   A C     1 
ATOM   499  O O     . PRO   A 1 73  ? 31.39600  6.16985   31.10273  1.000 45.03228  ? 73  PRO   A O     1 
ATOM   500  C CB    . PRO   A 1 73  ? 29.93296  7.60643   28.62099  1.000 40.77655  ? 73  PRO   A CB    1 
ATOM   501  C CG    . PRO   A 1 73  ? 31.31435  8.15347   28.61164  1.000 41.71159  ? 73  PRO   A CG    1 
ATOM   502  C CD    . PRO   A 1 73  ? 31.33051  9.21140   29.71007  1.000 40.01807  ? 73  PRO   A CD    1 
ATOM   503  N N     . LYS   A 1 74  ? 29.38893  5.21103   30.76078  1.000 41.47299  ? 74  LYS   A N     1 
ATOM   504  C CA    . LYS   A 1 74  ? 29.79186  3.88427   31.21131  1.000 42.51544  ? 74  LYS   A CA    1 
ATOM   505  C C     . LYS   A 1 74  ? 29.39771  2.93800   30.09774  1.000 41.93823  ? 74  LYS   A C     1 
ATOM   506  O O     . LYS   A 1 74  ? 28.22328  2.89493   29.72713  1.000 46.31494  ? 74  LYS   A O     1 
ATOM   507  C CB    . LYS   A 1 74  ? 29.11431  3.48099   32.52745  1.000 39.20323  ? 74  LYS   A CB    1 
ATOM   508  C CG    . LYS   A 1 74  ? 29.59547  2.16288   33.11573  1.000 41.68499  ? 74  LYS   A CG    1 
ATOM   509  C CD    . LYS   A 1 74  ? 29.31429  2.08442   34.62619  1.000 48.61897  ? 74  LYS   A CD    1 
ATOM   510  C CE    . LYS   A 1 74  ? 27.96598  1.47548   34.98673  1.000 52.87553  ? 74  LYS   A CE    1 
ATOM   511  N NZ    . LYS   A 1 74  ? 28.09761  -0.00597  34.87423  1.000 52.80388  ? 74  LYS   A NZ    1 
ATOM   512  N N     . SER   A 1 75  ? 30.36665  2.21856   29.53612  1.000 37.98309  ? 75  SER   A N     1 
ATOM   513  C CA    . SER   A 1 75  ? 30.01867  1.22711   28.53826  1.000 38.66332  ? 75  SER   A CA    1 
ATOM   514  C C     . SER   A 1 75  ? 30.00253  -0.14835  29.17679  1.000 41.78028  ? 75  SER   A C     1 
ATOM   515  O O     . SER   A 1 75  ? 28.93679  -0.71023  29.47932  1.000 44.04961  ? 75  SER   A O     1 
ATOM   516  C CB    . SER   A 1 75  ? 31.01083  1.26400   27.37823  1.000 45.75415  ? 75  SER   A CB    1 
ATOM   517  O OG    . SER   A 1 75  ? 30.93415  2.48323   26.65036  1.000 46.74704  ? 75  SER   A OG    1 
ATOM   518  N N     . GLY   A 1 76  ? 31.21048  -0.65049  29.42989  1.000 42.28245  ? 76  GLY   A N     1 
ATOM   519  C CA    . GLY   A 1 76  ? 31.47238  -2.00907  29.82903  1.000 44.21326  ? 76  GLY   A CA    1 
ATOM   520  C C     . GLY   A 1 76  ? 31.77036  -2.16588  31.30267  1.000 51.45134  ? 76  GLY   A C     1 
ATOM   521  O O     . GLY   A 1 76  ? 31.58714  -3.26264  31.84099  1.000 58.69582  ? 76  GLY   A O     1 
ATOM   522  N N     . GLY   A 1 77  ? 32.23909  -1.09312  31.95994  1.000 46.90755  ? 77  GLY   A N     1 
ATOM   523  C CA    . GLY   A 1 77  ? 32.34986  -1.03636  33.40400  1.000 45.03067  ? 77  GLY   A CA    1 
ATOM   524  C C     . GLY   A 1 77  ? 33.73580  -1.24191  34.00825  1.000 50.72859  ? 77  GLY   A C     1 
ATOM   525  O O     . GLY   A 1 77  ? 33.87211  -1.12938  35.23614  1.000 53.16552  ? 77  GLY   A O     1 
ATOM   526  N N     . HIS   A 1 78  ? 34.77479  -1.49897  33.20044  1.000 53.26084  ? 78  HIS   A N     1 
ATOM   527  C CA    . HIS   A 1 78  ? 36.06563  -1.97650  33.70817  1.000 49.11784  ? 78  HIS   A CA    1 
ATOM   528  C C     . HIS   A 1 78  ? 37.00774  -0.90791  34.19763  1.000 48.88274  ? 78  HIS   A C     1 
ATOM   529  O O     . HIS   A 1 78  ? 38.19318  -1.22841  34.39570  1.000 54.12336  ? 78  HIS   A O     1 
ATOM   530  C CB    . HIS   A 1 78  ? 36.81924  -2.73068  32.63683  1.000 53.27302  ? 78  HIS   A CB    1 
ATOM   531  C CG    . HIS   A 1 78  ? 36.70147  -4.20131  32.76516  1.000 52.54939  ? 78  HIS   A CG    1 
ATOM   532  N ND1   . HIS   A 1 78  ? 37.70021  -4.97923  33.32415  1.000 55.33144  ? 78  HIS   A ND1   1 
ATOM   533  C CD2   . HIS   A 1 78  ? 35.70250  -5.03854  32.39101  1.000 44.14934  ? 78  HIS   A CD2   1 
ATOM   534  C CE1   . HIS   A 1 78  ? 37.29633  -6.23872  33.29860  1.000 56.45223  ? 78  HIS   A CE1   1 
ATOM   535  N NE2   . HIS   A 1 78  ? 36.09957  -6.30091  32.73529  1.000 50.03921  ? 78  HIS   A NE2   1 
ATOM   536  N N     . ASN   A 1 79  ? 36.57498  0.32876   34.35627  1.000 46.01063  ? 79  ASN   A N     1 
ATOM   537  C CA    . ASN   A 1 79  ? 37.48469  1.33825   34.86372  1.000 50.58452  ? 79  ASN   A CA    1 
ATOM   538  C C     . ASN   A 1 79  ? 37.80287  1.09295   36.34040  1.000 50.00099  ? 79  ASN   A C     1 
ATOM   539  O O     . ASN   A 1 79  ? 36.88687  1.14035   37.17030  1.000 53.54986  ? 79  ASN   A O     1 
ATOM   540  C CB    . ASN   A 1 79  ? 36.84813  2.69373   34.67736  1.000 50.93629  ? 79  ASN   A CB    1 
ATOM   541  C CG    . ASN   A 1 79  ? 37.76482  3.78326   35.08430  1.000 52.40653  ? 79  ASN   A CG    1 
ATOM   542  O OD1   . ASN   A 1 79  ? 37.54041  4.44892   36.09302  1.000 44.17770  ? 79  ASN   A OD1   1 
ATOM   543  N ND2   . ASN   A 1 79  ? 38.83395  3.97171   34.30598  1.000 59.26373  ? 79  ASN   A ND2   1 
ATOM   544  N N     . TYR   A 1 80  ? 39.09619  0.87748   36.68036  1.000 45.29082  ? 80  TYR   A N     1 
ATOM   545  C CA    . TYR   A 1 80  ? 39.50860  0.60660   38.07279  1.000 48.01114  ? 80  TYR   A CA    1 
ATOM   546  C C     . TYR   A 1 80  ? 39.17559  1.75419   39.04750  1.000 53.16771  ? 80  TYR   A C     1 
ATOM   547  O O     . TYR   A 1 80  ? 39.05743  1.53263   40.26614  1.000 49.91725  ? 80  TYR   A O     1 
ATOM   548  C CB    . TYR   A 1 80  ? 41.00996  0.31192   38.15448  1.000 47.33601  ? 80  TYR   A CB    1 
ATOM   549  C CG    . TYR   A 1 80  ? 41.47696  -0.94469  37.48738  1.000 51.05963  ? 80  TYR   A CG    1 
ATOM   550  C CD1   . TYR   A 1 80  ? 40.58948  -1.96920  37.15354  1.000 57.02655  ? 80  TYR   A CD1   1 
ATOM   551  C CD2   . TYR   A 1 80  ? 42.80169  -1.09070  37.13418  1.000 52.53072  ? 80  TYR   A CD2   1 
ATOM   552  C CE1   . TYR   A 1 80  ? 41.03628  -3.13335  36.52405  1.000 54.29830  ? 80  TYR   A CE1   1 
ATOM   553  C CE2   . TYR   A 1 80  ? 43.24638  -2.23817  36.49503  1.000 58.40415  ? 80  TYR   A CE2   1 
ATOM   554  C CZ    . TYR   A 1 80  ? 42.36143  -3.24624  36.19582  1.000 56.73143  ? 80  TYR   A CZ    1 
ATOM   555  O OH    . TYR   A 1 80  ? 42.80205  -4.37671  35.57256  1.000 63.69936  ? 80  TYR   A OH    1 
ATOM   556  N N     . GLY   A 1 81  ? 39.06221  2.98892   38.56003  1.000 55.12887  ? 81  GLY   A N     1 
ATOM   557  C CA    . GLY   A 1 81  ? 38.58073  4.02295   39.45007  1.000 51.73423  ? 81  GLY   A CA    1 
ATOM   558  C C     . GLY   A 1 81  ? 37.07686  4.07273   39.58447  1.000 50.22196  ? 81  GLY   A C     1 
ATOM   559  O O     . GLY   A 1 81  ? 36.56863  4.80832   40.44082  1.000 51.20425  ? 81  GLY   A O     1 
ATOM   560  N N     . ASN   A 1 82  ? 36.36513  3.28831   38.76449  1.000 45.45059  ? 82  ASN   A N     1 
ATOM   561  C CA    . ASN   A 1 82  ? 34.91191  3.36863   38.62594  1.000 48.55176  ? 82  ASN   A CA    1 
ATOM   562  C C     . ASN   A 1 82  ? 34.46769  4.72030   38.07778  1.000 50.24961  ? 82  ASN   A C     1 
ATOM   563  O O     . ASN   A 1 82  ? 33.36809  5.19258   38.36818  1.000 49.36259  ? 82  ASN   A O     1 
ATOM   564  C CB    . ASN   A 1 82  ? 34.19732  3.06257   39.94439  1.000 46.57612  ? 82  ASN   A CB    1 
ATOM   565  C CG    . ASN   A 1 82  ? 34.27462  1.57995   40.31886  1.000 57.23736  ? 82  ASN   A CG    1 
ATOM   566  O OD1   . ASN   A 1 82  ? 34.67233  0.73910   39.49471  1.000 60.53138  ? 82  ASN   A OD1   1 
ATOM   567  N ND2   . ASN   A 1 82  ? 33.86715  1.24849   41.54781  1.000 56.63928  ? 82  ASN   A ND2   1 
ATOM   568  N N     . TYR   A 1 83  ? 35.29950  5.34803   37.24601  1.000 48.95320  ? 83  TYR   A N     1 
ATOM   569  C CA    . TYR   A 1 83  ? 34.98676  6.70783   36.83149  1.000 44.60249  ? 83  TYR   A CA    1 
ATOM   570  C C     . TYR   A 1 83  ? 33.73514  6.73919   36.00136  1.000 46.12918  ? 83  TYR   A C     1 
ATOM   571  O O     . TYR   A 1 83  ? 33.13220  7.80140   35.85113  1.000 43.77297  ? 83  TYR   A O     1 
ATOM   572  C CB    . TYR   A 1 83  ? 36.10310  7.31388   36.00387  1.000 47.38422  ? 83  TYR   A CB    1 
ATOM   573  C CG    . TYR   A 1 83  ? 37.43678  7.45177   36.70154  1.000 53.07387  ? 83  TYR   A CG    1 
ATOM   574  C CD1   . TYR   A 1 83  ? 37.52672  7.62284   38.07963  1.000 49.69343  ? 83  TYR   A CD1   1 
ATOM   575  C CD2   . TYR   A 1 83  ? 38.61611  7.45800   35.96159  1.000 59.04333  ? 83  TYR   A CD2   1 
ATOM   576  C CE1   . TYR   A 1 83  ? 38.73496  7.73836   38.68907  1.000 48.36152  ? 83  TYR   A CE1   1 
ATOM   577  C CE2   . TYR   A 1 83  ? 39.83671  7.59423   36.56896  1.000 57.42453  ? 83  TYR   A CE2   1 
ATOM   578  C CZ    . TYR   A 1 83  ? 39.88390  7.73661   37.93183  1.000 53.51787  ? 83  TYR   A CZ    1 
ATOM   579  O OH    . TYR   A 1 83  ? 41.09681  7.86968   38.53927  1.000 61.16001  ? 83  TYR   A OH    1 
ATOM   580  N N     . GLY   A 1 84  ? 33.34937  5.60076   35.42130  1.000 50.85954  ? 84  GLY   A N     1 
ATOM   581  C CA    . GLY   A 1 84  ? 32.11306  5.58666   34.66985  1.000 50.18494  ? 84  GLY   A CA    1 
ATOM   582  C C     . GLY   A 1 84  ? 30.95990  6.00501   35.54943  1.000 51.03048  ? 84  GLY   A C     1 
ATOM   583  O O     . GLY   A 1 84  ? 29.92935  6.46509   35.05701  1.000 46.36425  ? 84  GLY   A O     1 
ATOM   584  N N     . SER   A 1 85  ? 31.13720  5.86590   36.87149  1.000 58.26043  ? 85  SER   A N     1 
ATOM   585  C CA    . SER   A 1 85  ? 30.12431  6.14469   37.88325  1.000 56.75748  ? 85  SER   A CA    1 
ATOM   586  C C     . SER   A 1 85  ? 30.57235  7.25276   38.85585  1.000 53.33652  ? 85  SER   A C     1 
ATOM   587  O O     . SER   A 1 85  ? 29.99503  7.41573   39.93014  1.000 50.35573  ? 85  SER   A O     1 
ATOM   588  C CB    . SER   A 1 85  ? 29.76404  4.83484   38.61266  1.000 54.50248  ? 85  SER   A CB    1 
ATOM   589  O OG    . SER   A 1 85  ? 29.43086  3.79760   37.67009  1.000 56.85197  ? 85  SER   A OG    1 
ATOM   590  N N     . THR   A 1 86  ? 31.58537  8.03104   38.48280  1.000 52.47750  ? 86  THR   A N     1 
ATOM   591  C CA    . THR   A 1 86  ? 31.93330  9.25147   39.20265  1.000 54.01573  ? 86  THR   A CA    1 
ATOM   592  C C     . THR   A 1 86  ? 30.80404  9.83016   40.04146  1.000 54.96922  ? 86  THR   A C     1 
ATOM   593  O O     . THR   A 1 86  ? 29.72196  10.11756  39.51475  1.000 56.13641  ? 86  THR   A O     1 
ATOM   594  C CB    . THR   A 1 86  ? 32.45137  10.27642  38.19463  1.000 45.73096  ? 86  THR   A CB    1 
ATOM   595  O OG1   . THR   A 1 86  ? 33.73462  9.82066   37.72449  1.000 44.83254  ? 86  THR   A OG1   1 
ATOM   596  C CG2   . THR   A 1 86  ? 32.52550  11.67528  38.78836  1.000 41.29324  ? 86  THR   A CG2   1 
ATOM   597  N N     . THR   A 1 87  ? 31.06254  9.99464   41.34292  1.000 53.37173  ? 87  THR   A N     1 
ATOM   598  C CA    . THR   A 1 87  ? 30.02693  10.40063  42.28419  1.000 54.98875  ? 87  THR   A CA    1 
ATOM   599  C C     . THR   A 1 87  ? 29.50634  11.79544  42.00523  1.000 50.33549  ? 87  THR   A C     1 
ATOM   600  O O     . THR   A 1 87  ? 30.28292  12.73767  41.83355  1.000 55.59447  ? 87  THR   A O     1 
ATOM   601  C CB    . THR   A 1 87  ? 30.54220  10.38394  43.71541  1.000 56.89406  ? 87  THR   A CB    1 
ATOM   602  O OG1   . THR   A 1 87  ? 31.04245  9.07850   44.06819  1.000 56.21098  ? 87  THR   A OG1   1 
ATOM   603  C CG2   . THR   A 1 87  ? 29.39137  10.81011  44.62636  1.000 48.06695  ? 87  THR   A CG2   1 
ATOM   604  N N     . GLY   A 1 88  ? 28.18976  11.94976  42.05095  1.000 48.81713  ? 88  GLY   A N     1 
ATOM   605  C CA    . GLY   A 1 88  ? 27.63807  13.27327  41.82730  1.000 54.55768  ? 88  GLY   A CA    1 
ATOM   606  C C     . GLY   A 1 88  ? 27.81279  13.76397  40.41126  1.000 55.66403  ? 88  GLY   A C     1 
ATOM   607  O O     . GLY   A 1 88  ? 27.86294  14.97224  40.16875  1.000 59.91859  ? 88  GLY   A O     1 
ATOM   608  N N     . GLU   A 1 89  ? 27.92163  12.84632  39.46247  1.000 55.18457  ? 89  GLU   A N     1 
ATOM   609  C CA    . GLU   A 1 89  ? 27.95649  13.16273  38.04705  1.000 51.67527  ? 89  GLU   A CA    1 
ATOM   610  C C     . GLU   A 1 89  ? 26.83992  12.38173  37.38186  1.000 51.74552  ? 89  GLU   A C     1 
ATOM   611  O O     . GLU   A 1 89  ? 26.29990  11.44750  37.96589  1.000 54.17267  ? 89  GLU   A O     1 
ATOM   612  C CB    . GLU   A 1 89  ? 29.29679  12.78817  37.43626  1.000 48.88528  ? 89  GLU   A CB    1 
ATOM   613  C CG    . GLU   A 1 89  ? 30.39520  13.61975  38.01482  1.000 51.73453  ? 89  GLU   A CG    1 
ATOM   614  C CD    . GLU   A 1 89  ? 31.52725  13.80631  37.06511  1.000 51.89974  ? 89  GLU   A CD    1 
ATOM   615  O OE1   . GLU   A 1 89  ? 31.34395  13.41765  35.90427  1.000 54.95021  ? 89  GLU   A OE1   1 
ATOM   616  O OE2   . GLU   A 1 89  ? 32.56476  14.38553  37.44012  1.000 51.81626  ? 89  GLU   A OE2   1 
ATOM   617  N N     . LEU   A 1 90  ? 26.47611  12.74941  36.16237  1.000 48.08132  ? 90  LEU   A N     1 
ATOM   618  C CA    . LEU   A 1 90  ? 25.56066  11.90381  35.40956  1.000 43.63164  ? 90  LEU   A CA    1 
ATOM   619  C C     . LEU   A 1 90  ? 26.32495  10.66558  34.90473  1.000 47.76272  ? 90  LEU   A C     1 
ATOM   620  O O     . LEU   A 1 90  ? 27.44163  10.79456  34.37580  1.000 47.47774  ? 90  LEU   A O     1 
ATOM   621  C CB    . LEU   A 1 90  ? 24.93753  12.71198  34.27119  1.000 45.77874  ? 90  LEU   A CB    1 
ATOM   622  C CG    . LEU   A 1 90  ? 23.89233  11.89983  33.50598  1.000 46.02845  ? 90  LEU   A CG    1 
ATOM   623  C CD1   . LEU   A 1 90  ? 22.92666  11.30456  34.50774  1.000 44.98357  ? 90  LEU   A CD1   1 
ATOM   624  C CD2   . LEU   A 1 90  ? 23.17172  12.71252  32.44367  1.000 40.46873  ? 90  LEU   A CD2   1 
ATOM   625  N N     . SER   A 1 91  ? 25.75769  9.45475   35.11836  1.000 43.74835  ? 91  SER   A N     1 
ATOM   626  C CA    . SER   A 1 91  ? 26.32921  8.19340   34.60462  1.000 37.02285  ? 91  SER   A CA    1 
ATOM   627  C C     . SER   A 1 91  ? 25.50671  7.67540   33.41923  1.000 44.84272  ? 91  SER   A C     1 
ATOM   628  O O     . SER   A 1 91  ? 24.42613  7.10282   33.59421  1.000 43.71579  ? 91  SER   A O     1 
ATOM   629  C CB    . SER   A 1 91  ? 26.40324  7.13816   35.69058  1.000 40.39077  ? 91  SER   A CB    1 
ATOM   630  O OG    . SER   A 1 91  ? 27.09671  5.99197   35.23620  1.000 43.38959  ? 91  SER   A OG    1 
ATOM   631  N N     . VAL   A 1 92  ? 26.04075  7.84987   32.20990  1.000 51.24566  ? 92  VAL   A N     1 
ATOM   632  C CA    . VAL   A 1 92  ? 25.32868  7.52341   30.97653  1.000 47.05231  ? 92  VAL   A CA    1 
ATOM   633  C C     . VAL   A 1 92  ? 25.70560  6.10340   30.59146  1.000 43.24229  ? 92  VAL   A C     1 
ATOM   634  O O     . VAL   A 1 92  ? 26.75691  5.87383   29.99284  1.000 43.77202  ? 92  VAL   A O     1 
ATOM   635  C CB    . VAL   A 1 92  ? 25.64741  8.49526   29.84361  1.000 40.73436  ? 92  VAL   A CB    1 
ATOM   636  C CG1   . VAL   A 1 92  ? 25.10126  7.93939   28.58612  1.000 43.96009  ? 92  VAL   A CG1   1 
ATOM   637  C CG2   . VAL   A 1 92  ? 24.97956  9.81834   30.09242  1.000 39.69882  ? 92  VAL   A CG2   1 
ATOM   638  N N     . ASN   A 1 93  ? 24.81503  5.15999   30.90002  1.000 46.09338  ? 93  ASN   A N     1 
ATOM   639  C CA    . ASN   A 1 93  ? 25.05796  3.74492   30.66203  1.000 43.10864  ? 93  ASN   A CA    1 
ATOM   640  C C     . ASN   A 1 93  ? 24.63513  3.37912   29.25118  1.000 45.37845  ? 93  ASN   A C     1 
ATOM   641  O O     . ASN   A 1 93  ? 23.45771  3.49073   28.87671  1.000 49.83731  ? 93  ASN   A O     1 
ATOM   642  C CB    . ASN   A 1 93  ? 24.32395  2.88193   31.65763  1.000 44.48094  ? 93  ASN   A CB    1 
ATOM   643  C CG    . ASN   A 1 93  ? 24.80596  1.48764   31.62264  1.000 46.19143  ? 93  ASN   A CG    1 
ATOM   644  O OD1   . ASN   A 1 93  ? 24.75788  0.82851   30.57491  1.000 47.93665  ? 93  ASN   A OD1   1 
ATOM   645  N ND2   . ASN   A 1 93  ? 25.32024  1.00989   32.76452  1.000 45.86915  ? 93  ASN   A ND2   1 
ATOM   646  N N     . LEU   A 1 94  ? 25.60072  2.92804   28.47484  1.000 39.67061  ? 94  LEU   A N     1 
ATOM   647  C CA    . LEU   A 1 94  ? 25.41954  2.76625   27.04857  1.000 44.18354  ? 94  LEU   A CA    1 
ATOM   648  C C     . LEU   A 1 94  ? 25.03455  1.34235   26.69046  1.000 42.84616  ? 94  LEU   A C     1 
ATOM   649  O O     . LEU   A 1 94  ? 25.26912  0.91255   25.56094  1.000 38.59765  ? 94  LEU   A O     1 
ATOM   650  C CB    . LEU   A 1 94  ? 26.71047  3.17508   26.35168  1.000 43.97684  ? 94  LEU   A CB    1 
ATOM   651  C CG    . LEU   A 1 94  ? 27.14748  4.59196   26.73316  1.000 37.68217  ? 94  LEU   A CG    1 
ATOM   652  C CD1   . LEU   A 1 94  ? 28.50253  4.96935   26.18574  1.000 38.55727  ? 94  LEU   A CD1   1 
ATOM   653  C CD2   . LEU   A 1 94  ? 26.11426  5.55101   26.24777  1.000 40.84225  ? 94  LEU   A CD2   1 
ATOM   654  N N     . ASP   A 1 95  ? 24.48105  0.59220   27.65153  1.000 48.91386  ? 95  ASP   A N     1 
ATOM   655  C CA    . ASP   A 1 95  ? 24.31085  -0.82973  27.42703  1.000 47.49242  ? 95  ASP   A CA    1 
ATOM   656  C C     . ASP   A 1 95  ? 23.34519  -1.08742  26.26896  1.000 43.53397  ? 95  ASP   A C     1 
ATOM   657  O O     . ASP   A 1 95  ? 23.40832  -2.14385  25.63834  1.000 41.28234  ? 95  ASP   A O     1 
ATOM   658  C CB    . ASP   A 1 95  ? 23.86526  -1.52474  28.71953  1.000 43.03374  ? 95  ASP   A CB    1 
ATOM   659  C CG    . ASP   A 1 95  ? 23.96042  -3.05796  28.61582  1.000 69.25487  ? 95  ASP   A CG    1 
ATOM   660  O OD1   . ASP   A 1 95  ? 25.04137  -3.53957  28.19658  1.000 77.18008  ? 95  ASP   A OD1   1 
ATOM   661  O OD2   . ASP   A 1 95  ? 22.96852  -3.78660  28.91745  1.000 70.28608  ? 95  ASP   A OD2   1 
ATOM   662  N N     . ASN   A 1 96  ? 22.52589  -0.11193  25.90038  1.000 40.80937  ? 96  ASN   A N     1 
ATOM   663  C CA    . ASN   A 1 96  ? 21.61111  -0.36534  24.80376  1.000 41.10963  ? 96  ASN   A CA    1 
ATOM   664  C C     . ASN   A 1 96  ? 22.22455  -0.07558  23.44163  1.000 43.62939  ? 96  ASN   A C     1 
ATOM   665  O O     . ASN   A 1 96  ? 21.77234  -0.63115  22.43212  1.000 47.95636  ? 96  ASN   A O     1 
ATOM   666  C CB    . ASN   A 1 96  ? 20.34805  0.45518   24.98684  1.000 48.24974  ? 96  ASN   A CB    1 
ATOM   667  C CG    . ASN   A 1 96  ? 19.51939  -0.06435  26.11120  1.000 55.99422  ? 96  ASN   A CG    1 
ATOM   668  O OD1   . ASN   A 1 96  ? 19.15156  -1.24328  26.15133  1.000 50.76766  ? 96  ASN   A OD1   1 
ATOM   669  N ND2   . ASN   A 1 96  ? 19.20895  0.81602   27.04641  1.000 60.64612  ? 96  ASN   A ND2   1 
ATOM   670  N N     . LEU   A 1 97  ? 23.25030  0.76455   23.38523  1.000 46.91929  ? 97  LEU   A N     1 
ATOM   671  C CA    . LEU   A 1 97  ? 23.91722  1.06947   22.12269  1.000 47.53864  ? 97  LEU   A CA    1 
ATOM   672  C C     . LEU   A 1 97  ? 24.85281  -0.09360  21.82523  1.000 46.36659  ? 97  LEU   A C     1 
ATOM   673  O O     . LEU   A 1 97  ? 26.05348  -0.05811  22.11192  1.000 43.29941  ? 97  LEU   A O     1 
ATOM   674  C CB    . LEU   A 1 97  ? 24.68110  2.37540   22.20099  1.000 48.11546  ? 97  LEU   A CB    1 
ATOM   675  C CG    . LEU   A 1 97  ? 23.90691  3.67545   22.16153  1.000 45.61213  ? 97  LEU   A CG    1 
ATOM   676  C CD1   . LEU   A 1 97  ? 22.98109  3.79194   23.34803  1.000 45.42284  ? 97  LEU   A CD1   1 
ATOM   677  C CD2   . LEU   A 1 97  ? 24.91952  4.76979   22.18456  1.000 48.75793  ? 97  LEU   A CD2   1 
ATOM   678  N N     . GLN   A 1 98  ? 24.27299  -1.15327  21.26576  1.000 48.48888  ? 98  GLN   A N     1 
ATOM   679  C CA    . GLN   A 1 98  ? 24.98699  -2.39378  21.01098  1.000 48.37390  ? 98  GLN   A CA    1 
ATOM   680  C C     . GLN   A 1 98  ? 24.81104  -2.81771  19.57055  1.000 51.99655  ? 98  GLN   A C     1 
ATOM   681  O O     . GLN   A 1 98  ? 24.70249  -4.02017  19.28943  1.000 52.13099  ? 98  GLN   A O     1 
ATOM   682  C CB    . GLN   A 1 98  ? 24.53442  -3.52373  21.93608  1.000 40.65159  ? 98  GLN   A CB    1 
ATOM   683  C CG    . GLN   A 1 98  ? 25.05472  -3.49807  23.36951  1.000 45.74584  ? 98  GLN   A CG    1 
ATOM   684  C CD    . GLN   A 1 98  ? 24.97445  -4.87718  24.05422  1.000 62.31420  ? 98  GLN   A CD    1 
ATOM   685  O OE1   . GLN   A 1 98  ? 25.76666  -5.79290  23.77005  1.000 60.44804  ? 98  GLN   A OE1   1 
ATOM   686  N NE2   . GLN   A 1 98  ? 24.04108  -5.00975  24.99452  1.000 74.90222  ? 98  GLN   A NE2   1 
ATOM   687  N N     . HIS   A 1 99  ? 24.78438  -1.85076  18.63768  1.000 50.68581  ? 99  HIS   A N     1 
ATOM   688  C CA    . HIS   A 1 99  ? 24.55527  -2.14722  17.22413  1.000 60.72662  ? 99  HIS   A CA    1 
ATOM   689  C C     . HIS   A 1 99  ? 25.81468  -2.69009  16.53814  1.000 63.24310  ? 99  HIS   A C     1 
ATOM   690  O O     . HIS   A 1 99  ? 26.95417  -2.34844  16.90590  1.000 58.86691  ? 99  HIS   A O     1 
ATOM   691  C CB    . HIS   A 1 99  ? 24.03254  -0.90080  16.47692  1.000 66.26868  ? 99  HIS   A CB    1 
ATOM   692  C CG    . HIS   A 1 99  ? 24.07710  -1.02105  14.97807  1.000 75.55724  ? 99  HIS   A CG    1 
ATOM   693  N ND1   . HIS   A 1 99  ? 25.02728  -0.37465  14.20734  1.000 72.12374  ? 99  HIS   A ND1   1 
ATOM   694  C CD2   . HIS   A 1 99  ? 23.33641  -1.76500  14.11469  1.000 72.13641  ? 99  HIS   A CD2   1 
ATOM   695  C CE1   . HIS   A 1 99  ? 24.85346  -0.69167  12.93455  1.000 65.52043  ? 99  HIS   A CE1   1 
ATOM   696  N NE2   . HIS   A 1 99  ? 23.83740  -1.53679  12.84837  1.000 66.62627  ? 99  HIS   A NE2   1 
ATOM   697  N N     . PHE   A 1 100 ? 25.59847  -3.55510  15.53476  1.000 60.00655  ? 100 PHE   A N     1 
ATOM   698  C CA    . PHE   A 1 100 ? 26.68970  -4.19704  14.79995  1.000 58.35103  ? 100 PHE   A CA    1 
ATOM   699  C C     . PHE   A 1 100 ? 26.27256  -4.44970  13.36206  1.000 58.38255  ? 100 PHE   A C     1 
ATOM   700  O O     . PHE   A 1 100 ? 25.41822  -5.29718  13.10282  1.000 62.26766  ? 100 PHE   A O     1 
ATOM   701  C CB    . PHE   A 1 100 ? 27.09655  -5.52513  15.44143  1.000 59.78092  ? 100 PHE   A CB    1 
ATOM   702  C CG    . PHE   A 1 100 ? 28.12214  -6.26680  14.64751  1.000 53.89939  ? 100 PHE   A CG    1 
ATOM   703  C CD1   . PHE   A 1 100 ? 27.74312  -7.09287  13.61034  1.000 50.76193  ? 100 PHE   A CD1   1 
ATOM   704  C CD2   . PHE   A 1 100 ? 29.46398  -6.10238  14.90824  1.000 52.57747  ? 100 PHE   A CD2   1 
ATOM   705  C CE1   . PHE   A 1 100 ? 28.68161  -7.75327  12.84926  1.000 50.53715  ? 100 PHE   A CE1   1 
ATOM   706  C CE2   . PHE   A 1 100 ? 30.40245  -6.76738  14.14854  1.000 53.59951  ? 100 PHE   A CE2   1 
ATOM   707  C CZ    . PHE   A 1 100 ? 30.00184  -7.59218  13.11411  1.000 53.60862  ? 100 PHE   A CZ    1 
ATOM   708  N N     . SER   A 1 101 ? 26.93505  -3.78850  12.42913  1.000 58.51029  ? 101 SER   A N     1 
ATOM   709  C CA    . SER   A 1 101 ? 26.77913  -4.09265  11.01841  1.000 56.22374  ? 101 SER   A CA    1 
ATOM   710  C C     . SER   A 1 101 ? 28.15561  -4.31316  10.39373  1.000 59.41803  ? 101 SER   A C     1 
ATOM   711  O O     . SER   A 1 101 ? 29.16761  -3.79248  10.87661  1.000 56.42776  ? 101 SER   A O     1 
ATOM   712  C CB    . SER   A 1 101 ? 26.04761  -2.97064  10.29505  1.000 58.33088  ? 101 SER   A CB    1 
ATOM   713  O OG    . SER   A 1 101 ? 26.93681  -1.91901  9.95634   1.000 55.54070  ? 101 SER   A OG    1 
ATOM   714  N N     . MET   A 1 102 ? 28.19067  -5.09446  9.31226   1.000 61.00584  ? 102 MET   A N     1 
ATOM   715  C CA    . MET   A 1 102 ? 29.42975  -5.34276  8.59560   1.000 56.44153  ? 102 MET   A CA    1 
ATOM   716  C C     . MET   A 1 102 ? 29.25429  -5.02096  7.11334   1.000 63.56208  ? 102 MET   A C     1 
ATOM   717  O O     . MET   A 1 102 ? 28.17198  -5.22955  6.55452   1.000 65.56659  ? 102 MET   A O     1 
ATOM   718  C CB    . MET   A 1 102 ? 29.86747  -6.78703  8.78697   1.000 56.56852  ? 102 MET   A CB    1 
ATOM   719  C CG    . MET   A 1 102 ? 31.10459  -7.07098  8.01868   1.000 58.78663  ? 102 MET   A CG    1 
ATOM   720  S SD    . MET   A 1 102 ? 32.60581  -6.28056  8.66835   1.000 60.48474  ? 102 MET   A SD    1 
ATOM   721  C CE    . MET   A 1 102 ? 33.25999  -7.63419  9.64872   1.000 54.47512  ? 102 MET   A CE    1 
ATOM   722  N N     . ASN   A 1 103 ? 30.32108  -4.46810  6.48788   1.000 64.61834  ? 103 ASN   A N     1 
ATOM   723  C CA    . ASN   A 1 103 ? 30.40978  -4.21608  5.03604   1.000 61.62830  ? 103 ASN   A CA    1 
ATOM   724  C C     . ASN   A 1 103 ? 31.24456  -5.32467  4.38631   1.000 67.77172  ? 103 ASN   A C     1 
ATOM   725  O O     . ASN   A 1 103 ? 32.47273  -5.34482  4.54226   1.000 66.44774  ? 103 ASN   A O     1 
ATOM   726  C CB    . ASN   A 1 103 ? 31.06823  -2.86890  4.74355   1.000 58.68642  ? 103 ASN   A CB    1 
ATOM   727  C CG    . ASN   A 1 103 ? 30.92269  -2.43677  3.28182   1.000 66.74937  ? 103 ASN   A CG    1 
ATOM   728  O OD1   . ASN   A 1 103 ? 31.81889  -1.78732  2.70288   1.000 70.89736  ? 103 ASN   A OD1   1 
ATOM   729  N ND2   . ASN   A 1 103 ? 29.75702  -2.71807  2.70403   1.000 70.46163  ? 103 ASN   A ND2   1 
ATOM   730  N N     . GLU   A 1 104 ? 30.58977  -6.21077  3.60926   1.000 67.29188  ? 104 GLU   A N     1 
ATOM   731  C CA    . GLU   A 1 104 ? 31.29835  -7.32622  2.97351   1.000 64.37442  ? 104 GLU   A CA    1 
ATOM   732  C C     . GLU   A 1 104 ? 32.36099  -6.82111  1.98891   1.000 68.09078  ? 104 GLU   A C     1 
ATOM   733  O O     . GLU   A 1 104 ? 33.30021  -7.55845  1.66259   1.000 69.30152  ? 104 GLU   A O     1 
ATOM   734  C CB    . GLU   A 1 104 ? 30.26868  -8.26873  2.30057   1.000 57.53449  ? 104 GLU   A CB    1 
ATOM   735  N N     . THR   A 1 105 ? 32.26081  -5.56042  1.55497   1.000 63.68756  ? 105 THR   A N     1 
ATOM   736  C CA    . THR   A 1 105 ? 33.20422  -5.00811  0.58670   1.000 61.62012  ? 105 THR   A CA    1 
ATOM   737  C C     . THR   A 1 105 ? 34.46108  -4.41274  1.21557   1.000 64.11420  ? 105 THR   A C     1 
ATOM   738  O O     . THR   A 1 105 ? 35.57973  -4.82324  0.89766   1.000 55.78259  ? 105 THR   A O     1 
ATOM   739  C CB    . THR   A 1 105 ? 32.50675  -3.93922  -0.24089  1.000 68.99517  ? 105 THR   A CB    1 
ATOM   740  O OG1   . THR   A 1 105 ? 31.28843  -4.47750  -0.78884  1.000 64.27622  ? 105 THR   A OG1   1 
ATOM   741  C CG2   . THR   A 1 105 ? 33.46990  -3.40837  -1.31743  1.000 61.07581  ? 105 THR   A CG2   1 
ATOM   742  N N     . SER   A 1 106 ? 34.30265  -3.37673  2.04977   1.000 64.47578  ? 106 SER   A N     1 
ATOM   743  C CA    . SER   A 1 106 ? 35.47685  -2.80847  2.71140   1.000 55.65161  ? 106 SER   A CA    1 
ATOM   744  C C     . SER   A 1 106 ? 35.96338  -3.68867  3.85426   1.000 61.11210  ? 106 SER   A C     1 
ATOM   745  O O     . SER   A 1 106 ? 37.15222  -3.66933  4.18290   1.000 61.00144  ? 106 SER   A O     1 
ATOM   746  C CB    . SER   A 1 106 ? 35.17895  -1.40663  3.23057   1.000 59.31998  ? 106 SER   A CB    1 
ATOM   747  O OG    . SER   A 1 106 ? 34.01737  -1.35107  4.04943   1.000 58.92279  ? 106 SER   A OG    1 
ATOM   748  N N     . TRP   A 1 107 ? 35.05701  -4.47985  4.45180   1.000 62.18401  ? 107 TRP   A N     1 
ATOM   749  C CA    . TRP   A 1 107 ? 35.26989  -5.17172  5.71886   1.000 62.41770  ? 107 TRP   A CA    1 
ATOM   750  C C     . TRP   A 1 107 ? 35.34723  -4.18933  6.88624   1.000 60.43218  ? 107 TRP   A C     1 
ATOM   751  O O     . TRP   A 1 107 ? 36.04453  -4.43030  7.87075   1.000 58.53452  ? 107 TRP   A O     1 
ATOM   752  C CB    . TRP   A 1 107 ? 36.51227  -6.07826  5.68569   1.000 62.80782  ? 107 TRP   A CB    1 
ATOM   753  C CG    . TRP   A 1 107 ? 36.36410  -7.30336  4.79375   1.000 60.67439  ? 107 TRP   A CG    1 
ATOM   754  C CD1   . TRP   A 1 107 ? 37.21235  -7.68642  3.81714   1.000 57.03008  ? 107 TRP   A CD1   1 
ATOM   755  C CD2   . TRP   A 1 107 ? 35.29969  -8.27736  4.80366   1.000 63.21209  ? 107 TRP   A CD2   1 
ATOM   756  N NE1   . TRP   A 1 107 ? 36.75471  -8.82621  3.20986   1.000 64.14323  ? 107 TRP   A NE1   1 
ATOM   757  C CE2   . TRP   A 1 107 ? 35.58634  -9.21284  3.80122   1.000 61.19157  ? 107 TRP   A CE2   1 
ATOM   758  C CE3   . TRP   A 1 107 ? 34.13824  -8.44652  5.56504   1.000 64.94529  ? 107 TRP   A CE3   1 
ATOM   759  C CZ2   . TRP   A 1 107 ? 34.76597  -10.29958 3.53719   1.000 64.87026  ? 107 TRP   A CZ2   1 
ATOM   760  C CZ3   . TRP   A 1 107 ? 33.31600  -9.53301  5.29692   1.000 63.51687  ? 107 TRP   A CZ3   1 
ATOM   761  C CH2   . TRP   A 1 107 ? 33.63647  -10.44236 4.29424   1.000 65.61847  ? 107 TRP   A CH2   1 
ATOM   762  N N     . THR   A 1 108 ? 34.63392  -3.07746  6.78920   1.000 61.85961  ? 108 THR   A N     1 
ATOM   763  C CA    . THR   A 1 108 ? 34.57844  -2.07974  7.84458   1.000 53.37985  ? 108 THR   A CA    1 
ATOM   764  C C     . THR   A 1 108 ? 33.25773  -2.29851  8.57090   1.000 58.40217  ? 108 THR   A C     1 
ATOM   765  O O     . THR   A 1 108 ? 32.18267  -2.05024  8.00919   1.000 57.99734  ? 108 THR   A O     1 
ATOM   766  C CB    . THR   A 1 108 ? 34.66792  -0.66797  7.26984   1.000 53.51159  ? 108 THR   A CB    1 
ATOM   767  O OG1   . THR   A 1 108 ? 35.89809  -0.50154  6.55308   1.000 58.76245  ? 108 THR   A OG1   1 
ATOM   768  C CG2   . THR   A 1 108 ? 34.60765  0.36866   8.38770   1.000 57.81862  ? 108 THR   A CG2   1 
ATOM   769  N N     . ALA   A 1 109 ? 33.34116  -2.79539  9.80649   1.000 61.24779  ? 109 ALA   A N     1 
ATOM   770  C CA    . ALA   A 1 109 ? 32.18619  -3.00486  10.67382  1.000 56.03018  ? 109 ALA   A CA    1 
ATOM   771  C C     . ALA   A 1 109 ? 31.86171  -1.72291  11.42964  1.000 52.16504  ? 109 ALA   A C     1 
ATOM   772  O O     . ALA   A 1 109 ? 32.68791  -0.81476  11.54715  1.000 50.27389  ? 109 ALA   A O     1 
ATOM   773  C CB    . ALA   A 1 109 ? 32.43825  -4.14840  11.66428  1.000 54.30634  ? 109 ALA   A CB    1 
ATOM   774  N N     . ARG   A 1 110 ? 30.63933  -1.66920  11.95423  1.000 55.32413  ? 110 ARG   A N     1 
ATOM   775  C CA    . ARG   A 1 110 ? 30.06795  -0.45621  12.55457  1.000 58.87088  ? 110 ARG   A CA    1 
ATOM   776  C C     . ARG   A 1 110 ? 29.38769  -0.87729  13.86493  1.000 63.40062  ? 110 ARG   A C     1 
ATOM   777  O O     . ARG   A 1 110 ? 28.30579  -1.48170  13.84556  1.000 64.42244  ? 110 ARG   A O     1 
ATOM   778  C CB    . ARG   A 1 110 ? 29.11205  0.20667   11.55493  1.000 55.23192  ? 110 ARG   A CB    1 
ATOM   779  C CG    . ARG   A 1 110 ? 28.43943  1.51226   11.88672  1.000 60.09160  ? 110 ARG   A CG    1 
ATOM   780  C CD    . ARG   A 1 110 ? 27.14225  1.56834   11.04726  1.000 72.90916  ? 110 ARG   A CD    1 
ATOM   781  N NE    . ARG   A 1 110 ? 26.05205  2.35130   11.62519  1.000 79.81031  ? 110 ARG   A NE    1 
ATOM   782  C CZ    . ARG   A 1 110 ? 26.10328  3.65400   11.86755  1.000 101.97866 ? 110 ARG   A CZ    1 
ATOM   783  N NH1   . ARG   A 1 110 ? 27.15082  4.38638   11.50953  1.000 118.28866 ? 110 ARG   A NH1   1 
ATOM   784  N NH2   . ARG   A 1 110 ? 25.06561  4.23883   12.46157  1.000 104.21866 ? 110 ARG   A NH2   1 
ATOM   785  N N     . LEU   A 1 111 ? 30.04139  -0.58858  15.00735  1.000 58.05905  ? 111 LEU   A N     1 
ATOM   786  C CA    . LEU   A 1 111 ? 29.60002  -1.06722  16.31422  1.000 57.64017  ? 111 LEU   A CA    1 
ATOM   787  C C     . LEU   A 1 111 ? 29.26990  0.08659   17.25307  1.000 56.19258  ? 111 LEU   A C     1 
ATOM   788  O O     . LEU   A 1 111 ? 29.83765  1.17988   17.16398  1.000 54.19629  ? 111 LEU   A O     1 
ATOM   789  C CB    . LEU   A 1 111 ? 30.66143  -1.92572  16.99948  1.000 55.28235  ? 111 LEU   A CB    1 
ATOM   790  C CG    . LEU   A 1 111 ? 31.30062  -2.94141  16.08786  1.000 49.93835  ? 111 LEU   A CG    1 
ATOM   791  C CD1   . LEU   A 1 111 ? 32.51425  -2.27078  15.57680  1.000 50.14552  ? 111 LEU   A CD1   1 
ATOM   792  C CD2   . LEU   A 1 111 ? 31.64519  -4.23710  16.81816  1.000 51.44357  ? 111 LEU   A CD2   1 
ATOM   793  N N     . GLY   A 1 112 ? 28.37207  -0.20204  18.19260  1.000 56.70501  ? 112 GLY   A N     1 
ATOM   794  C CA    . GLY   A 1 112 ? 28.04665  0.71586   19.26179  1.000 52.79225  ? 112 GLY   A CA    1 
ATOM   795  C C     . GLY   A 1 112 ? 28.89285  0.45952   20.49326  1.000 49.80567  ? 112 GLY   A C     1 
ATOM   796  O O     . GLY   A 1 112 ? 29.49778  -0.60939  20.65501  1.000 48.51057  ? 112 GLY   A O     1 
ATOM   797  N N     . PRO   A 1 113 ? 28.94290  1.44758   21.39408  1.000 46.74176  ? 113 PRO   A N     1 
ATOM   798  C CA    . PRO   A 1 113 ? 29.92257  1.38874   22.48537  1.000 42.40062  ? 113 PRO   A CA    1 
ATOM   799  C C     . PRO   A 1 113 ? 29.60309  0.34602   23.53488  1.000 43.08708  ? 113 PRO   A C     1 
ATOM   800  O O     . PRO   A 1 113 ? 30.50932  -0.09433  24.25820  1.000 40.82176  ? 113 PRO   A O     1 
ATOM   801  C CB    . PRO   A 1 113 ? 29.86242  2.80524   23.05721  1.000 42.60173  ? 113 PRO   A CB    1 
ATOM   802  C CG    . PRO   A 1 113 ? 28.52263  3.28859   22.65395  1.000 39.46822  ? 113 PRO   A CG    1 
ATOM   803  C CD    . PRO   A 1 113 ? 28.31998  2.77309   21.31082  1.000 42.05928  ? 113 PRO   A CD    1 
ATOM   804  N N     . GLY   A 1 114 ? 28.33571  -0.05437  23.65044  1.000 47.47181  ? 114 GLY   A N     1 
ATOM   805  C CA    . GLY   A 1 114 ? 27.93518  -1.03666  24.64389  1.000 47.46061  ? 114 GLY   A CA    1 
ATOM   806  C C     . GLY   A 1 114 ? 28.26372  -2.46447  24.27018  1.000 45.72796  ? 114 GLY   A C     1 
ATOM   807  O O     . GLY   A 1 114 ? 28.04605  -3.36211  25.08531  1.000 49.33563  ? 114 GLY   A O     1 
ATOM   808  N N     . ASN   A 1 115 ? 28.76020  -2.69691  23.05993  1.000 43.36717  ? 115 ASN   A N     1 
ATOM   809  C CA    . ASN   A 1 115 ? 29.26525  -4.01135  22.71180  1.000 44.53239  ? 115 ASN   A CA    1 
ATOM   810  C C     . ASN   A 1 115 ? 30.43937  -4.39737  23.59708  1.000 45.96978  ? 115 ASN   A C     1 
ATOM   811  O O     . ASN   A 1 115 ? 31.41033  -3.64676  23.70908  1.000 46.95344  ? 115 ASN   A O     1 
ATOM   812  C CB    . ASN   A 1 115 ? 29.71694  -4.02514  21.26761  1.000 41.82246  ? 115 ASN   A CB    1 
ATOM   813  C CG    . ASN   A 1 115 ? 28.60342  -4.18432  20.33530  1.000 40.92774  ? 115 ASN   A CG    1 
ATOM   814  O OD1   . ASN   A 1 115 ? 28.05516  -5.26402  20.24370  1.000 45.34383  ? 115 ASN   A OD1   1 
ATOM   815  N ND2   . ASN   A 1 115 ? 28.26735  -3.13694  19.59446  1.000 43.64286  ? 115 ASN   A ND2   1 
ATOM   816  N N     . ARG   A 1 116 ? 30.36350  -5.57315  24.21773  1.000 44.78208  ? 116 ARG   A N     1 
ATOM   817  C CA    . ARG   A 1 116 ? 31.48400  -6.05235  25.01216  1.000 43.61579  ? 116 ARG   A CA    1 
ATOM   818  C C     . ARG   A 1 116 ? 32.40776  -6.87786  24.12812  1.000 43.51330  ? 116 ARG   A C     1 
ATOM   819  O O     . ARG   A 1 116 ? 31.97438  -7.45635  23.13158  1.000 41.40744  ? 116 ARG   A O     1 
ATOM   820  C CB    . ARG   A 1 116 ? 30.99373  -6.87960  26.19862  1.000 45.16092  ? 116 ARG   A CB    1 
ATOM   821  C CG    . ARG   A 1 116 ? 29.84168  -6.25224  27.00399  1.000 47.56564  ? 116 ARG   A CG    1 
ATOM   822  C CD    . ARG   A 1 116 ? 30.29517  -5.03287  27.79760  1.000 49.03474  ? 116 ARG   A CD    1 
ATOM   823  N NE    . ARG   A 1 116 ? 29.39716  -4.61458  28.88115  1.000 50.32517  ? 116 ARG   A NE    1 
ATOM   824  C CZ    . ARG   A 1 116 ? 28.18525  -4.10892  28.69782  1.000 49.02153  ? 116 ARG   A CZ    1 
ATOM   825  N NH1   . ARG   A 1 116 ? 27.62971  -4.08095  27.50221  1.000 53.03126  ? 116 ARG   A NH1   1 
ATOM   826  N NH2   . ARG   A 1 116 ? 27.52805  -3.58889  29.73571  1.000 51.19158  ? 116 ARG   A NH2   1 
ATOM   827  N N     . LEU   A 1 117 ? 33.69934  -6.90276  24.47418  1.000 45.75732  ? 117 LEU   A N     1 
ATOM   828  C CA    . LEU   A 1 117 ? 34.69376  -7.51033  23.58601  1.000 40.35945  ? 117 LEU   A CA    1 
ATOM   829  C C     . LEU   A 1 117 ? 34.30268  -8.91179  23.15391  1.000 41.60181  ? 117 LEU   A C     1 
ATOM   830  O O     . LEU   A 1 117 ? 34.55294  -9.30338  22.01497  1.000 39.93533  ? 117 LEU   A O     1 
ATOM   831  C CB    . LEU   A 1 117 ? 36.06645  -7.52564  24.24240  1.000 43.98903  ? 117 LEU   A CB    1 
ATOM   832  C CG    . LEU   A 1 117 ? 36.65448  -6.13119  24.18271  1.000 48.58814  ? 117 LEU   A CG    1 
ATOM   833  C CD1   . LEU   A 1 117 ? 38.08512  -6.07940  24.64542  1.000 44.92926  ? 117 LEU   A CD1   1 
ATOM   834  C CD2   . LEU   A 1 117 ? 36.58611  -5.79882  22.73054  1.000 46.69866  ? 117 LEU   A CD2   1 
ATOM   835  N N     . GLY   A 1 118 ? 33.66096  -9.67424  24.04518  1.000 48.82595  ? 118 GLY   A N     1 
ATOM   836  C CA    . GLY   A 1 118 ? 33.20350  -11.00806 23.68178  1.000 42.75284  ? 118 GLY   A CA    1 
ATOM   837  C C     . GLY   A 1 118 ? 32.25701  -10.99552 22.49891  1.000 44.62275  ? 118 GLY   A C     1 
ATOM   838  O O     . GLY   A 1 118 ? 32.35731  -11.83538 21.60180  1.000 45.85241  ? 118 GLY   A O     1 
ATOM   839  N N     . ARG   A 1 119 ? 31.33124  -10.03261 22.47240  1.000 45.83534  ? 119 ARG   A N     1 
ATOM   840  C CA    . ARG   A 1 119 ? 30.37810  -9.98632  21.37335  1.000 44.76948  ? 119 ARG   A CA    1 
ATOM   841  C C     . ARG   A 1 119 ? 30.97969  -9.33711  20.13497  1.000 46.09804  ? 119 ARG   A C     1 
ATOM   842  O O     . ARG   A 1 119 ? 30.57366  -9.64934  19.01707  1.000 46.79922  ? 119 ARG   A O     1 
ATOM   843  C CB    . ARG   A 1 119 ? 29.12531  -9.24184  21.78993  1.000 41.34849  ? 119 ARG   A CB    1 
ATOM   844  C CG    . ARG   A 1 119 ? 28.12608  -9.08240  20.70341  1.000 40.92780  ? 119 ARG   A CG    1 
ATOM   845  C CD    . ARG   A 1 119 ? 27.26381  -8.00310  21.16516  1.000 54.37461  ? 119 ARG   A CD    1 
ATOM   846  N NE    . ARG   A 1 119 ? 26.39960  -7.45469  20.14123  1.000 50.82927  ? 119 ARG   A NE    1 
ATOM   847  C CZ    . ARG   A 1 119 ? 25.36600  -8.09567  19.63265  1.000 58.36080  ? 119 ARG   A CZ    1 
ATOM   848  N NH1   . ARG   A 1 119 ? 25.04339  -9.31612  20.03456  1.000 73.24595  ? 119 ARG   A NH1   1 
ATOM   849  N NH2   . ARG   A 1 119 ? 24.60307  -7.47319  18.74797  1.000 56.27723  ? 119 ARG   A NH2   1 
ATOM   850  N N     . VAL   A 1 120 ? 31.95774  -8.45477  20.29014  1.000 45.47858  ? 120 VAL   A N     1 
ATOM   851  C CA    . VAL   A 1 120 ? 32.62223  -7.96531  19.09816  1.000 40.92106  ? 120 VAL   A CA    1 
ATOM   852  C C     . VAL   A 1 120 ? 33.30741  -9.13237  18.40818  1.000 41.75098  ? 120 VAL   A C     1 
ATOM   853  O O     . VAL   A 1 120 ? 33.19039  -9.31623  17.19802  1.000 43.21717  ? 120 VAL   A O     1 
ATOM   854  C CB    . VAL   A 1 120 ? 33.61977  -6.84379  19.43517  1.000 42.55445  ? 120 VAL   A CB    1 
ATOM   855  C CG1   . VAL   A 1 120 ? 34.21061  -6.27159  18.14015  1.000 40.79137  ? 120 VAL   A CG1   1 
ATOM   856  C CG2   . VAL   A 1 120 ? 33.00591  -5.76916  20.33153  1.000 44.94134  ? 120 VAL   A CG2   1 
ATOM   857  N N     . THR   A 1 121 ? 34.01672  -9.96032  19.17531  1.000 45.79713  ? 121 THR   A N     1 
ATOM   858  C CA    . THR   A 1 121 ? 34.73787  -11.09082 18.58121  1.000 50.42304  ? 121 THR   A CA    1 
ATOM   859  C C     . THR   A 1 121 ? 33.78645  -12.10815 17.93666  1.000 57.45926  ? 121 THR   A C     1 
ATOM   860  O O     . THR   A 1 121 ? 33.99380  -12.51470 16.78328  1.000 58.54499  ? 121 THR   A O     1 
ATOM   861  C CB    . THR   A 1 121 ? 35.62685  -11.76663 19.62940  1.000 48.13285  ? 121 THR   A CB    1 
ATOM   862  O OG1   . THR   A 1 121 ? 36.61430  -10.83607 20.10677  1.000 45.85345  ? 121 THR   A OG1   1 
ATOM   863  C CG2   . THR   A 1 121 ? 36.29126  -13.00181 19.05333  1.000 49.61307  ? 121 THR   A CG2   1 
ATOM   864  N N     . GLU   A 1 122 ? 32.73477  -12.54012 18.65106  1.000 53.25071  ? 122 GLU   A N     1 
ATOM   865  C CA    . GLU   A 1 122 ? 31.81170  -13.49347 18.03801  1.000 56.24154  ? 122 GLU   A CA    1 
ATOM   866  C C     . GLU   A 1 122 ? 31.23217  -12.94545 16.72725  1.000 55.16459  ? 122 GLU   A C     1 
ATOM   867  O O     . GLU   A 1 122 ? 31.02484  -13.69467 15.76906  1.000 62.05665  ? 122 GLU   A O     1 
ATOM   868  C CB    . GLU   A 1 122 ? 30.68083  -13.86320 19.00736  1.000 63.41541  ? 122 GLU   A CB    1 
ATOM   869  C CG    . GLU   A 1 122 ? 30.05870  -15.24514 18.72282  1.000 70.82034  ? 122 GLU   A CG    1 
ATOM   870  C CD    . GLU   A 1 122 ? 28.54440  -15.31543 18.96431  1.000 86.51340  ? 122 GLU   A CD    1 
ATOM   871  O OE1   . GLU   A 1 122 ? 27.92170  -14.28404 19.29173  1.000 88.48538  ? 122 GLU   A OE1   1 
ATOM   872  O OE2   . GLU   A 1 122 ? 27.95856  -16.40626 18.78226  1.000 98.87342  ? 122 GLU   A OE2   1 
ATOM   873  N N     . LEU   A 1 123 ? 30.95926  -11.64724 16.65666  1.000 49.02354  ? 123 LEU   A N     1 
ATOM   874  C CA    . LEU   A 1 123 ? 30.25692  -11.14318 15.48049  1.000 50.33980  ? 123 LEU   A CA    1 
ATOM   875  C C     . LEU   A 1 123 ? 31.19037  -10.90336 14.30124  1.000 50.54532  ? 123 LEU   A C     1 
ATOM   876  O O     . LEU   A 1 123 ? 30.81791  -11.16187 13.14612  1.000 53.86085  ? 123 LEU   A O     1 
ATOM   877  C CB    . LEU   A 1 123 ? 29.49447  -9.86320  15.81796  1.000 47.26697  ? 123 LEU   A CB    1 
ATOM   878  C CG    . LEU   A 1 123 ? 28.36006  -10.18020 16.76900  1.000 48.24279  ? 123 LEU   A CG    1 
ATOM   879  C CD1   . LEU   A 1 123 ? 27.60175  -8.93463  17.11818  1.000 52.87844  ? 123 LEU   A CD1   1 
ATOM   880  C CD2   . LEU   A 1 123 ? 27.45648  -11.20435 16.13686  1.000 50.37164  ? 123 LEU   A CD2   1 
ATOM   881  N N     . MET   A 1 124 ? 32.38055  -10.37269 14.56159  1.000 46.76919  ? 124 MET   A N     1 
ATOM   882  C CA    . MET   A 1 124 ? 33.33279  -10.17104 13.48105  1.000 49.09917  ? 124 MET   A CA    1 
ATOM   883  C C     . MET   A 1 124 ? 33.84200  -11.50026 12.93388  1.000 53.73485  ? 124 MET   A C     1 
ATOM   884  O O     . MET   A 1 124 ? 34.32031  -11.55676 11.79160  1.000 50.47874  ? 124 MET   A O     1 
ATOM   885  C CB    . MET   A 1 124 ? 34.50241  -9.32416  13.96080  1.000 46.47026  ? 124 MET   A CB    1 
ATOM   886  C CG    . MET   A 1 124 ? 34.21394  -7.87837  14.08879  1.000 43.72759  ? 124 MET   A CG    1 
ATOM   887  S SD    . MET   A 1 124 ? 35.76332  -7.05887  14.48265  1.000 56.56215  ? 124 MET   A SD    1 
ATOM   888  C CE    . MET   A 1 124 ? 35.13391  -5.46554  14.98754  1.000 52.41370  ? 124 MET   A CE    1 
ATOM   889  N N     . TYR   A 1 125 ? 33.79067  -12.55825 13.73971  1.000 55.83988  ? 125 TYR   A N     1 
ATOM   890  C CA    . TYR   A 1 125 ? 34.13567  -13.87267 13.23267  1.000 54.36786  ? 125 TYR   A CA    1 
ATOM   891  C C     . TYR   A 1 125 ? 33.01996  -14.39724 12.34679  1.000 55.69992  ? 125 TYR   A C     1 
ATOM   892  O O     . TYR   A 1 125 ? 33.23365  -14.69566 11.16830  1.000 61.77970  ? 125 TYR   A O     1 
ATOM   893  C CB    . TYR   A 1 125 ? 34.39501  -14.81804 14.39910  1.000 57.86986  ? 125 TYR   A CB    1 
ATOM   894  C CG    . TYR   A 1 125 ? 34.91965  -16.15491 13.97675  1.000 61.51584  ? 125 TYR   A CG    1 
ATOM   895  C CD1   . TYR   A 1 125 ? 36.26810  -16.33259 13.76565  1.000 64.44341  ? 125 TYR   A CD1   1 
ATOM   896  C CD2   . TYR   A 1 125 ? 34.06924  -17.24131 13.79574  1.000 63.21763  ? 125 TYR   A CD2   1 
ATOM   897  C CE1   . TYR   A 1 125 ? 36.76801  -17.53117 13.38705  1.000 70.85677  ? 125 TYR   A CE1   1 
ATOM   898  C CE2   . TYR   A 1 125 ? 34.56234  -18.46076 13.40023  1.000 68.76315  ? 125 TYR   A CE2   1 
ATOM   899  C CZ    . TYR   A 1 125 ? 35.92859  -18.59435 13.19758  1.000 73.47627  ? 125 TYR   A CZ    1 
ATOM   900  O OH    . TYR   A 1 125 ? 36.50228  -19.78037 12.80072  1.000 79.57822  ? 125 TYR   A OH    1 
ATOM   901  N N     . ASN   A 1 126 ? 31.80426  -14.47511 12.89303  1.000 53.74203  ? 126 ASN   A N     1 
ATOM   902  C CA    . ASN   A 1 126 ? 30.68491  -15.04154 12.15054  1.000 56.04688  ? 126 ASN   A CA    1 
ATOM   903  C C     . ASN   A 1 126 ? 30.39202  -14.26252 10.87284  1.000 58.98021  ? 126 ASN   A C     1 
ATOM   904  O O     . ASN   A 1 126 ? 30.00806  -14.85859 9.86284   1.000 58.46052  ? 126 ASN   A O     1 
ATOM   905  C CB    . ASN   A 1 126 ? 29.45163  -15.10747 13.04663  1.000 58.15139  ? 126 ASN   A CB    1 
ATOM   906  C CG    . ASN   A 1 126 ? 29.66394  -16.00384 14.25206  1.000 64.93926  ? 126 ASN   A CG    1 
ATOM   907  O OD1   . ASN   A 1 126 ? 30.70585  -16.66887 14.37795  1.000 51.11796  ? 126 ASN   A OD1   1 
ATOM   908  N ND2   . ASN   A 1 126 ? 28.67894  -16.02157 15.15720  1.000 75.23052  ? 126 ASN   A ND2   1 
ATOM   909  N N     . ASN   A 1 127 ? 30.56085  -12.93490 10.89039  1.000 59.86983  ? 127 ASN   A N     1 
ATOM   910  C CA    . ASN   A 1 127 ? 30.27255  -12.12687 9.70303   1.000 54.33059  ? 127 ASN   A CA    1 
ATOM   911  C C     . ASN   A 1 127 ? 31.54340  -11.89128 8.88055   1.000 57.01984  ? 127 ASN   A C     1 
ATOM   912  O O     . ASN   A 1 127 ? 32.02267  -10.76427 8.70057   1.000 53.47729  ? 127 ASN   A O     1 
ATOM   913  C CB    . ASN   A 1 127 ? 29.58113  -10.82255 10.08355  1.000 49.24073  ? 127 ASN   A CB    1 
ATOM   914  C CG    . ASN   A 1 127 ? 28.22793  -11.06009 10.74126  1.000 56.28134  ? 127 ASN   A CG    1 
ATOM   915  O OD1   . ASN   A 1 127 ? 27.16476  -10.74632 10.17408  1.000 61.20653  ? 127 ASN   A OD1   1 
ATOM   916  N ND2   . ASN   A 1 127 ? 28.25870  -11.60730 11.94812  1.000 49.62110  ? 127 ASN   A ND2   1 
ATOM   917  N N     . GLY   A 1 128 ? 32.07792  -13.00621 8.36684   1.000 56.30020  ? 128 GLY   A N     1 
ATOM   918  C CA    . GLY   A 1 128 ? 33.10078  -12.99457 7.33918   1.000 55.44893  ? 128 GLY   A CA    1 
ATOM   919  C C     . GLY   A 1 128 ? 34.49685  -13.33377 7.81746   1.000 54.36698  ? 128 GLY   A C     1 
ATOM   920  O O     . GLY   A 1 128 ? 35.47764  -12.87314 7.22602   1.000 59.70709  ? 128 GLY   A O     1 
ATOM   921  N N     . GLY   A 1 129 ? 34.61641  -14.12557 8.87615   1.000 49.97777  ? 129 GLY   A N     1 
ATOM   922  C CA    . GLY   A 1 129 ? 35.92477  -14.49262 9.38486   1.000 51.98159  ? 129 GLY   A CA    1 
ATOM   923  C C     . GLY   A 1 129 ? 36.88613  -13.33504 9.56910   1.000 56.92260  ? 129 GLY   A C     1 
ATOM   924  O O     . GLY   A 1 129 ? 38.02548  -13.37682 9.09631   1.000 53.81741  ? 129 GLY   A O     1 
ATOM   925  N N     . ARG   A 1 130 ? 36.43276  -12.29085 10.26812  1.000 61.32953  ? 130 ARG   A N     1 
ATOM   926  C CA    . ARG   A 1 130 ? 37.21302  -11.10078 10.57656  1.000 57.70303  ? 130 ARG   A CA    1 
ATOM   927  C C     . ARG   A 1 130 ? 37.46919  -11.02501 12.07624  1.000 58.45244  ? 130 ARG   A C     1 
ATOM   928  O O     . ARG   A 1 130 ? 36.72240  -11.57658 12.88234  1.000 60.00807  ? 130 ARG   A O     1 
ATOM   929  C CB    . ARG   A 1 130 ? 36.49207  -9.82679  10.12566  1.000 50.43848  ? 130 ARG   A CB    1 
ATOM   930  C CG    . ARG   A 1 130 ? 35.79448  -9.92718  8.80445   1.000 54.60875  ? 130 ARG   A CG    1 
ATOM   931  C CD    . ARG   A 1 130 ? 36.79491  -10.20749 7.70168   1.000 59.74168  ? 130 ARG   A CD    1 
ATOM   932  N NE    . ARG   A 1 130 ? 37.68995  -9.07453  7.48430   1.000 62.60540  ? 130 ARG   A NE    1 
ATOM   933  C CZ    . ARG   A 1 130 ? 38.80216  -9.13636  6.76702   1.000 59.83026  ? 130 ARG   A CZ    1 
ATOM   934  N NH1   . ARG   A 1 130 ? 39.15261  -10.24431 6.13653   1.000 67.57634  ? 130 ARG   A NH1   1 
ATOM   935  N NH2   . ARG   A 1 130 ? 39.59108  -8.07171  6.69749   1.000 54.64922  ? 130 ARG   A NH2   1 
ATOM   936  N N     . HIS   A 1 131 ? 38.54454  -10.33230 12.44251  1.000 56.59353  ? 131 HIS   A N     1 
ATOM   937  C CA    . HIS   A 1 131 ? 38.78240  -9.95660  13.82673  1.000 52.96550  ? 131 HIS   A CA    1 
ATOM   938  C C     . HIS   A 1 131 ? 39.50309  -8.62557  13.79319  1.000 54.27555  ? 131 HIS   A C     1 
ATOM   939  O O     . HIS   A 1 131 ? 39.83625  -8.11006  12.72601  1.000 52.31353  ? 131 HIS   A O     1 
ATOM   940  C CB    . HIS   A 1 131 ? 39.65400  -10.96773 14.56206  1.000 59.08559  ? 131 HIS   A CB    1 
ATOM   941  C CG    . HIS   A 1 131 ? 41.11123  -10.79907 14.25852  1.000 61.34586  ? 131 HIS   A CG    1 
ATOM   942  N ND1   . HIS   A 1 131 ? 42.05091  -10.45688 15.21737  1.000 58.33342  ? 131 HIS   A ND1   1 
ATOM   943  C CD2   . HIS   A 1 131 ? 41.78254  -10.87740 13.08338  1.000 57.29814  ? 131 HIS   A CD2   1 
ATOM   944  C CE1   . HIS   A 1 131 ? 43.23918  -10.34904 14.64261  1.000 57.35129  ? 131 HIS   A CE1   1 
ATOM   945  N NE2   . HIS   A 1 131 ? 43.10405  -10.60236 13.34918  1.000 58.74258  ? 131 HIS   A NE2   1 
ATOM   946  N N     . VAL   A 1 132 ? 39.78890  -8.09043  14.97002  1.000 57.96875  ? 132 VAL   A N     1 
ATOM   947  C CA    . VAL   A 1 132 ? 40.58053  -6.86653  15.06193  1.000 57.81002  ? 132 VAL   A CA    1 
ATOM   948  C C     . VAL   A 1 132 ? 41.41152  -6.90952  16.33554  1.000 59.50360  ? 132 VAL   A C     1 
ATOM   949  O O     . VAL   A 1 132 ? 41.03112  -7.60882  17.29889  1.000 59.55830  ? 132 VAL   A O     1 
ATOM   950  C CB    . VAL   A 1 132 ? 39.69459  -5.60475  14.97953  1.000 51.40016  ? 132 VAL   A CB    1 
ATOM   951  C CG1   . VAL   A 1 132 ? 38.60727  -5.62281  16.01313  1.000 41.64070  ? 132 VAL   A CG1   1 
ATOM   952  C CG2   . VAL   A 1 132 ? 40.55784  -4.39404  15.19197  1.000 48.27761  ? 132 VAL   A CG2   1 
ATOM   953  N N     . PRO   A 1 133 ? 42.57241  -6.24944  16.37272  1.000 57.21315  ? 133 PRO   A N     1 
ATOM   954  C CA    . PRO   A 1 133 ? 43.40110  -6.31285  17.58859  1.000 59.35181  ? 133 PRO   A CA    1 
ATOM   955  C C     . PRO   A 1 133 ? 42.66399  -5.66813  18.75452  1.000 50.31174  ? 133 PRO   A C     1 
ATOM   956  O O     . PRO   A 1 133 ? 42.09044  -4.58542  18.61554  1.000 48.35000  ? 133 PRO   A O     1 
ATOM   957  C CB    . PRO   A 1 133 ? 44.67161  -5.53391  17.19665  1.000 55.09735  ? 133 PRO   A CB    1 
ATOM   958  C CG    . PRO   A 1 133 ? 44.32896  -4.79507  15.96650  1.000 51.89032  ? 133 PRO   A CG    1 
ATOM   959  C CD    . PRO   A 1 133 ? 43.28423  -5.59574  15.26426  1.000 50.39060  ? 133 PRO   A CD    1 
ATOM   960  N N     . HIS   A 1 134 ? 42.66161  -6.35109  19.89871  1.000 51.26799  ? 134 HIS   A N     1 
ATOM   961  C CA    . HIS   A 1 134 ? 42.00722  -5.79833  21.09115  1.000 54.03408  ? 134 HIS   A CA    1 
ATOM   962  C C     . HIS   A 1 134 ? 42.46433  -6.54703  22.35994  1.000 55.10310  ? 134 HIS   A C     1 
ATOM   963  O O     . HIS   A 1 134 ? 43.39121  -7.36261  22.32706  1.000 62.58683  ? 134 HIS   A O     1 
ATOM   964  C CB    . HIS   A 1 134 ? 40.49299  -5.80490  20.86694  1.000 50.80408  ? 134 HIS   A CB    1 
ATOM   965  C CG    . HIS   A 1 134 ? 39.87815  -7.16027  20.76374  1.000 46.91723  ? 134 HIS   A CG    1 
ATOM   966  N ND1   . HIS   A 1 134 ? 40.03913  -8.13144  21.72678  1.000 52.61580  ? 134 HIS   A ND1   1 
ATOM   967  C CD2   . HIS   A 1 134 ? 39.12377  -7.71458  19.79178  1.000 49.84106  ? 134 HIS   A CD2   1 
ATOM   968  C CE1   . HIS   A 1 134 ? 39.37400  -9.21591  21.36685  1.000 57.21061  ? 134 HIS   A CE1   1 
ATOM   969  N NE2   . HIS   A 1 134 ? 38.81568  -8.98968  20.19230  1.000 59.23214  ? 134 HIS   A NE2   1 
ATOM   970  N N     . GLY   A 1 135 ? 41.84499  -6.24119  23.50080  1.000 51.52540  ? 135 GLY   A N     1 
ATOM   971  C CA    . GLY   A 1 135 ? 42.22863  -6.90915  24.73049  1.000 58.59879  ? 135 GLY   A CA    1 
ATOM   972  C C     . GLY   A 1 135 ? 41.62526  -8.30372  24.84521  1.000 53.56433  ? 135 GLY   A C     1 
ATOM   973  O O     . GLY   A 1 135 ? 40.72827  -8.69028  24.09313  1.000 46.77158  ? 135 GLY   A O     1 
ATOM   974  N N     . THR   A 1 136 ? 42.11052  -9.06023  25.82695  1.000 51.55536  ? 136 THR   A N     1 
ATOM   975  C CA    . THR   A 1 136 ? 41.66230  -10.43815 25.98878  1.000 58.80026  ? 136 THR   A CA    1 
ATOM   976  C C     . THR   A 1 136 ? 40.39076  -10.60588 26.82319  1.000 57.59635  ? 136 THR   A C     1 
ATOM   977  O O     . THR   A 1 136 ? 39.67477  -11.59908 26.64859  1.000 60.47702  ? 136 THR   A O     1 
ATOM   978  C CB    . THR   A 1 136 ? 42.79538  -11.26809 26.58126  1.000 58.84560  ? 136 THR   A CB    1 
ATOM   979  O OG1   . THR   A 1 136 ? 43.36871  -10.56557 27.69913  1.000 72.00704  ? 136 THR   A OG1   1 
ATOM   980  C CG2   . THR   A 1 136 ? 43.83453  -11.49006 25.52065  1.000 58.20296  ? 136 THR   A CG2   1 
ATOM   981  N N     . THR   A 1 137 ? 40.05925  -9.66712  27.69132  1.000 54.38554  ? 137 THR   A N     1 
ATOM   982  C CA    . THR   A 1 137 ? 38.94355  -9.88394  28.59507  1.000 55.12891  ? 137 THR   A CA    1 
ATOM   983  C C     . THR   A 1 137 ? 37.62090  -9.60288  27.88695  1.000 51.73823  ? 137 THR   A C     1 
ATOM   984  O O     . THR   A 1 137 ? 37.33554  -8.46422  27.50967  1.000 53.10264  ? 137 THR   A O     1 
ATOM   985  C CB    . THR   A 1 137 ? 39.13070  -9.01798  29.83438  1.000 60.90328  ? 137 THR   A CB    1 
ATOM   986  O OG1   . THR   A 1 137 ? 40.32868  -9.44875  30.50668  1.000 66.65525  ? 137 THR   A OG1   1 
ATOM   987  C CG2   . THR   A 1 137 ? 37.91493  -9.10749  30.78240  1.000 49.95289  ? 137 THR   A CG2   1 
ATOM   988  N N     . PHE   A 1 138 ? 36.80617  -10.64654 27.72218  1.000 51.21287  ? 138 PHE   A N     1 
ATOM   989  C CA    . PHE   A 1 138 ? 35.52244  -10.54504 27.03436  1.000 49.26852  ? 138 PHE   A CA    1 
ATOM   990  C C     . PHE   A 1 138 ? 34.51127  -9.62638  27.72884  1.000 46.28341  ? 138 PHE   A C     1 
ATOM   991  O O     . PHE   A 1 138 ? 33.48338  -9.29667  27.11390  1.000 46.53653  ? 138 PHE   A O     1 
ATOM   992  C CB    . PHE   A 1 138 ? 34.86825  -11.92290 26.93712  1.000 49.07675  ? 138 PHE   A CB    1 
ATOM   993  C CG    . PHE   A 1 138 ? 35.19952  -12.67720 25.70616  1.000 45.43037  ? 138 PHE   A CG    1 
ATOM   994  C CD1   . PHE   A 1 138 ? 36.31296  -12.36243 24.96154  1.000 54.85252  ? 138 PHE   A CD1   1 
ATOM   995  C CD2   . PHE   A 1 138 ? 34.42411  -13.74797 25.31884  1.000 47.04381  ? 138 PHE   A CD2   1 
ATOM   996  C CE1   . PHE   A 1 138 ? 36.63630  -13.10885 23.81473  1.000 57.05304  ? 138 PHE   A CE1   1 
ATOM   997  C CE2   . PHE   A 1 138 ? 34.73093  -14.48686 24.18886  1.000 50.84696  ? 138 PHE   A CE2   1 
ATOM   998  C CZ    . PHE   A 1 138 ? 35.83631  -14.16192 23.43058  1.000 51.05488  ? 138 PHE   A CZ    1 
ATOM   999  N N     . THR   A 1 139 ? 34.69898  -9.27529  29.00320  1.000 39.62690  ? 139 THR   A N     1 
ATOM   1000 C CA    . THR   A 1 139 ? 33.74467  -8.35067  29.62566  1.000 43.45107  ? 139 THR   A CA    1 
ATOM   1001 C C     . THR   A 1 139 ? 34.11582  -6.87910  29.49040  1.000 50.18194  ? 139 THR   A C     1 
ATOM   1002 O O     . THR   A 1 139 ? 33.30255  -6.01414  29.85646  1.000 47.77836  ? 139 THR   A O     1 
ATOM   1003 C CB    . THR   A 1 139 ? 33.51107  -8.70904  31.08519  1.000 36.17782  ? 139 THR   A CB    1 
ATOM   1004 O OG1   . THR   A 1 139 ? 34.75248  -8.88297  31.77207  1.000 48.24644  ? 139 THR   A OG1   1 
ATOM   1005 C CG2   . THR   A 1 139 ? 32.69685  -9.89223  31.15885  1.000 38.78880  ? 139 THR   A CG2   1 
ATOM   1006 N N     . VAL   A 1 140 ? 35.29044  -6.57922  28.92597  1.000 48.00701  ? 140 VAL   A N     1 
ATOM   1007 C CA    . VAL   A 1 140 ? 35.64289  -5.21273  28.58992  1.000 45.02604  ? 140 VAL   A CA    1 
ATOM   1008 C C     . VAL   A 1 140 ? 34.64806  -4.65218  27.58854  1.000 45.79451  ? 140 VAL   A C     1 
ATOM   1009 O O     . VAL   A 1 140 ? 34.46390  -5.20461  26.49810  1.000 48.50109  ? 140 VAL   A O     1 
ATOM   1010 C CB    . VAL   A 1 140 ? 37.06211  -5.18247  28.02815  1.000 47.25112  ? 140 VAL   A CB    1 
ATOM   1011 C CG1   . VAL   A 1 140 ? 37.37565  -3.80671  27.56354  1.000 46.27227  ? 140 VAL   A CG1   1 
ATOM   1012 C CG2   . VAL   A 1 140 ? 38.04611  -5.64779  29.08546  1.000 51.20267  ? 140 VAL   A CG2   1 
ATOM   1013 N N     . GLY   A 1 141 ? 34.00580  -3.54475  27.94673  1.000 42.27194  ? 141 GLY   A N     1 
ATOM   1014 C CA    . GLY   A 1 141 ? 33.15464  -2.85685  26.99671  1.000 45.40150  ? 141 GLY   A CA    1 
ATOM   1015 C C     . GLY   A 1 141 ? 33.97420  -2.16102  25.92865  1.000 46.68698  ? 141 GLY   A C     1 
ATOM   1016 O O     . GLY   A 1 141 ? 35.11978  -1.78664  26.15411  1.000 53.61930  ? 141 GLY   A O     1 
ATOM   1017 N N     . LEU   A 1 142 ? 33.38949  -2.00453  24.73219  1.000 46.19913  ? 142 LEU   A N     1 
ATOM   1018 C CA    . LEU   A 1 142 ? 34.12503  -1.38387  23.62007  1.000 44.56459  ? 142 LEU   A CA    1 
ATOM   1019 C C     . LEU   A 1 142 ? 34.25306  0.13383   23.79473  1.000 44.67401  ? 142 LEU   A C     1 
ATOM   1020 O O     . LEU   A 1 142 ? 35.32226  0.69938   23.54700  1.000 41.12099  ? 142 LEU   A O     1 
ATOM   1021 C CB    . LEU   A 1 142 ? 33.44938  -1.73563  22.28828  1.000 42.33746  ? 142 LEU   A CB    1 
ATOM   1022 C CG    . LEU   A 1 142 ? 33.94538  -1.04911  21.00804  1.000 44.34589  ? 142 LEU   A CG    1 
ATOM   1023 C CD1   . LEU   A 1 142 ? 35.36256  -1.47382  20.61550  1.000 37.72726  ? 142 LEU   A CD1   1 
ATOM   1024 C CD2   . LEU   A 1 142 ? 32.92996  -1.28560  19.84595  1.000 46.41794  ? 142 LEU   A CD2   1 
ATOM   1025 N N     . GLY   A 1 143 ? 33.18430  0.79969   24.25266  1.000 45.42319  ? 143 GLY   A N     1 
ATOM   1026 C CA    . GLY   A 1 143 ? 33.20929  2.24972   24.39477  1.000 41.42209  ? 143 GLY   A CA    1 
ATOM   1027 C C     . GLY   A 1 143 ? 34.45643  2.79085   25.07687  1.000 42.33635  ? 143 GLY   A C     1 
ATOM   1028 O O     . GLY   A 1 143 ? 35.06492  3.75793   24.61083  1.000 41.34466  ? 143 GLY   A O     1 
ATOM   1029 N N     . GLY   A 1 144 ? 34.84347  2.19249   26.20492  1.000 45.95124  ? 144 GLY   A N     1 
ATOM   1030 C CA    . GLY   A 1 144 ? 35.99396  2.61407   26.98777  1.000 49.21737  ? 144 GLY   A CA    1 
ATOM   1031 C C     . GLY   A 1 144 ? 37.33422  2.00738   26.61655  1.000 44.87961  ? 144 GLY   A C     1 
ATOM   1032 O O     . GLY   A 1 144 ? 38.35815  2.33302   27.23903  1.000 43.25296  ? 144 GLY   A O     1 
ATOM   1033 N N     . HIS   A 1 145 ? 37.35072  1.14715   25.59406  1.000 42.10847  ? 145 HIS   A N     1 
ATOM   1034 C CA    . HIS   A 1 145 ? 38.50893  0.35108   25.18609  1.000 46.11688  ? 145 HIS   A CA    1 
ATOM   1035 C C     . HIS   A 1 145 ? 39.11989  0.87577   23.89123  1.000 48.51557  ? 145 HIS   A C     1 
ATOM   1036 O O     . HIS   A 1 145 ? 40.31281  1.18851   23.83612  1.000 47.70196  ? 145 HIS   A O     1 
ATOM   1037 C CB    . HIS   A 1 145 ? 38.06400  -1.11749  25.05233  1.000 42.87808  ? 145 HIS   A CB    1 
ATOM   1038 C CG    . HIS   A 1 145 ? 39.17010  -2.09700  24.79518  1.000 45.14543  ? 145 HIS   A CG    1 
ATOM   1039 N ND1   . HIS   A 1 145 ? 40.11946  -2.41502  25.74274  1.000 55.89515  ? 145 HIS   A ND1   1 
ATOM   1040 C CD2   . HIS   A 1 145 ? 39.41059  -2.91918  23.74062  1.000 47.55385  ? 145 HIS   A CD2   1 
ATOM   1041 C CE1   . HIS   A 1 145 ? 40.93491  -3.34394  25.26075  1.000 58.03835  ? 145 HIS   A CE1   1 
ATOM   1042 N NE2   . HIS   A 1 145 ? 40.51954  -3.67463  24.05010  1.000 48.44352  ? 145 HIS   A NE2   1 
ATOM   1043 N N     . ALA   A 1 146 ? 38.31252  0.98432   22.83613  1.000 45.51396  ? 146 ALA   A N     1 
ATOM   1044 C CA    . ALA   A 1 146 ? 38.76938  1.64277   21.62721  1.000 41.01706  ? 146 ALA   A CA    1 
ATOM   1045 C C     . ALA   A 1 146 ? 39.20881  3.06163   21.92405  1.000 46.47390  ? 146 ALA   A C     1 
ATOM   1046 O O     . ALA   A 1 146 ? 40.09396  3.59298   21.25286  1.000 48.83928  ? 146 ALA   A O     1 
ATOM   1047 C CB    . ALA   A 1 146 ? 37.65879  1.63200   20.59131  1.000 43.79796  ? 146 ALA   A CB    1 
ATOM   1048 N N     . THR   A 1 147 ? 38.65624  3.67624   22.95092  1.000 46.17523  ? 147 THR   A N     1 
ATOM   1049 C CA    . THR   A 1 147 ? 39.04803  5.04710   23.21918  1.000 45.30409  ? 147 THR   A CA    1 
ATOM   1050 C C     . THR   A 1 147 ? 40.28549  5.20432   24.11657  1.000 41.65960  ? 147 THR   A C     1 
ATOM   1051 O O     . THR   A 1 147 ? 40.78914  6.32864   24.22101  1.000 39.93539  ? 147 THR   A O     1 
ATOM   1052 C CB    . THR   A 1 147 ? 37.85123  5.80601   23.82410  1.000 48.00812  ? 147 THR   A CB    1 
ATOM   1053 O OG1   . THR   A 1 147 ? 37.31261  5.07469   24.93411  1.000 46.44385  ? 147 THR   A OG1   1 
ATOM   1054 C CG2   . THR   A 1 147 ? 36.74636  6.00057   22.78624  1.000 35.94409  ? 147 THR   A CG2   1 
ATOM   1055 N N     . VAL   A 1 148 ? 40.80250  4.15383   24.77343  1.000 44.43146  ? 148 VAL   A N     1 
ATOM   1056 C CA    . VAL   A 1 148 ? 42.01356  4.34721   25.60333  1.000 46.39931  ? 148 VAL   A CA    1 
ATOM   1057 C C     . VAL   A 1 148 ? 43.22428  3.78595   24.87401  1.000 48.70249  ? 148 VAL   A C     1 
ATOM   1058 O O     . VAL   A 1 148 ? 44.34077  4.29168   24.99581  1.000 49.83897  ? 148 VAL   A O     1 
ATOM   1059 C CB    . VAL   A 1 148 ? 41.90006  3.69998   26.99200  1.000 43.19235  ? 148 VAL   A CB    1 
ATOM   1060 C CG1   . VAL   A 1 148 ? 40.82552  4.36936   27.76600  1.000 46.90042  ? 148 VAL   A CG1   1 
ATOM   1061 C CG2   . VAL   A 1 148 ? 41.63851  2.21178   26.88690  1.000 47.63892  ? 148 VAL   A CG2   1 
ATOM   1062 N N     . GLY   A 1 149 ? 43.00634  2.74466   24.09723  1.000 51.11658  ? 149 GLY   A N     1 
ATOM   1063 C CA    . GLY   A 1 149 ? 44.03138  2.20113   23.24299  1.000 46.12006  ? 149 GLY   A CA    1 
ATOM   1064 C C     . GLY   A 1 149 ? 43.62691  0.82730   22.75590  1.000 46.31131  ? 149 GLY   A C     1 
ATOM   1065 O O     . GLY   A 1 149 ? 43.29509  0.64965   21.58034  1.000 46.88630  ? 149 GLY   A O     1 
ATOM   1066 N N     . GLY   A 1 150 ? 43.68328  -0.15685  23.65623  1.000 53.70645  ? 150 GLY   A N     1 
ATOM   1067 C CA    . GLY   A 1 150 ? 43.23653  -1.51867  23.40127  1.000 56.08318  ? 150 GLY   A CA    1 
ATOM   1068 C C     . GLY   A 1 150 ? 44.26825  -2.47891  22.83480  1.000 52.73005  ? 150 GLY   A C     1 
ATOM   1069 O O     . GLY   A 1 150 ? 44.29968  -2.70405  21.62279  1.000 44.87815  ? 150 GLY   A O     1 
ATOM   1070 N N     . ALA   A 1 151 ? 45.07852  -3.08103  23.70308  1.000 59.51264  ? 151 ALA   A N     1 
ATOM   1071 C CA    . ALA   A 1 151 ? 46.16344  -3.96852  23.30806  1.000 59.06853  ? 151 ALA   A CA    1 
ATOM   1072 C C     . ALA   A 1 151 ? 45.84028  -5.42762  23.62311  1.000 59.30597  ? 151 ALA   A C     1 
ATOM   1073 O O     . ALA   A 1 151 ? 45.06682  -5.73531  24.53286  1.000 64.79031  ? 151 ALA   A O     1 
ATOM   1074 C CB    . ALA   A 1 151 ? 47.45817  -3.55946  24.01279  1.000 55.90908  ? 151 ALA   A CB    1 
ATOM   1075 N N     . GLY   A 1 152 ? 46.44347  -6.33725  22.87917  1.000 49.51975  ? 152 GLY   A N     1 
ATOM   1076 C CA    . GLY   A 1 152 ? 46.12539  -7.72928  23.10771  1.000 55.69309  ? 152 GLY   A CA    1 
ATOM   1077 C C     . GLY   A 1 152 ? 46.92610  -8.64823  22.22540  1.000 57.32290  ? 152 GLY   A C     1 
ATOM   1078 O O     . GLY   A 1 152 ? 47.98064  -8.27826  21.70756  1.000 61.19769  ? 152 GLY   A O     1 
ATOM   1079 N N     . ALA   A 1 153 ? 46.39840  -9.85967  22.05536  1.000 62.50563  ? 153 ALA   A N     1 
ATOM   1080 C CA    . ALA   A 1 153 ? 47.15592  -10.91425 21.39043  1.000 63.62876  ? 153 ALA   A CA    1 
ATOM   1081 C C     . ALA   A 1 153 ? 47.69513  -10.44124 20.04260  1.000 66.85541  ? 153 ALA   A C     1 
ATOM   1082 O O     . ALA   A 1 153 ? 48.88225  -10.63370 19.72450  1.000 69.09778  ? 153 ALA   A O     1 
ATOM   1083 C CB    . ALA   A 1 153 ? 46.27109  -12.15841 21.23243  1.000 58.64159  ? 153 ALA   A CB    1 
ATOM   1084 N N     . ALA   A 1 154 ? 46.84068  -9.78316  19.25073  1.000 57.34270  ? 154 ALA   A N     1 
ATOM   1085 C CA    . ALA   A 1 154 ? 47.18069  -9.44815  17.88456  1.000 56.66575  ? 154 ALA   A CA    1 
ATOM   1086 C C     . ALA   A 1 154 ? 47.83591  -8.08247  17.75847  1.000 62.69517  ? 154 ALA   A C     1 
ATOM   1087 O O     . ALA   A 1 154 ? 47.86368  -7.52318  16.66142  1.000 66.56491  ? 154 ALA   A O     1 
ATOM   1088 C CB    . ALA   A 1 154 ? 45.93305  -9.52488  17.01124  1.000 54.86803  ? 154 ALA   A CB    1 
ATOM   1089 N N     . SER   A 1 155 ? 48.37833  -7.53192  18.84329  1.000 64.70131  ? 155 SER   A N     1 
ATOM   1090 C CA    . SER   A 1 155 ? 48.81031  -6.13678  18.79913  1.000 61.44390  ? 155 SER   A CA    1 
ATOM   1091 C C     . SER   A 1 155 ? 50.18290  -5.98424  18.16245  1.000 68.96065  ? 155 SER   A C     1 
ATOM   1092 O O     . SER   A 1 155 ? 50.35549  -5.16439  17.25402  1.000 67.29743  ? 155 SER   A O     1 
ATOM   1093 C CB    . SER   A 1 155 ? 48.79852  -5.53066  20.19053  1.000 56.76558  ? 155 SER   A CB    1 
ATOM   1094 O OG    . SER   A 1 155 ? 47.45749  -5.30684  20.59157  1.000 60.41499  ? 155 SER   A OG    1 
ATOM   1095 N N     . ARG   A 1 156 ? 51.17927  -6.75818  18.61637  1.000 73.87282  ? 156 ARG   A N     1 
ATOM   1096 C CA    . ARG   A 1 156 ? 52.47480  -6.71876  17.93967  1.000 67.83499  ? 156 ARG   A CA    1 
ATOM   1097 C C     . ARG   A 1 156 ? 52.30390  -6.98803  16.44925  1.000 63.15632  ? 156 ARG   A C     1 
ATOM   1098 O O     . ARG   A 1 156 ? 53.02632  -6.42379  15.62361  1.000 61.96506  ? 156 ARG   A O     1 
ATOM   1099 C CB    . ARG   A 1 156 ? 53.43503  -7.71898  18.59123  1.000 71.42840  ? 156 ARG   A CB    1 
ATOM   1100 C CG    . ARG   A 1 156 ? 53.91981  -7.29438  19.98772  1.000 73.99283  ? 156 ARG   A CG    1 
ATOM   1101 C CD    . ARG   A 1 156 ? 54.58935  -8.45688  20.69235  1.000 78.05629  ? 156 ARG   A CD    1 
ATOM   1102 N NE    . ARG   A 1 156 ? 55.66738  -9.00341  19.87763  1.000 81.38028  ? 156 ARG   A NE    1 
ATOM   1103 C CZ    . ARG   A 1 156 ? 56.80277  -8.37281  19.62350  1.000 77.33144  ? 156 ARG   A CZ    1 
ATOM   1104 N NH1   . ARG   A 1 156 ? 57.07239  -7.19650  20.16496  1.000 74.93536  ? 156 ARG   A NH1   1 
ATOM   1105 N NH2   . ARG   A 1 156 ? 57.68531  -8.93726  18.80480  1.000 85.97966  ? 156 ARG   A NH2   1 
ATOM   1106 N N     . MET   A 1 157 ? 51.29400  -7.78294  16.09051  1.000 62.81011  ? 157 MET   A N     1 
ATOM   1107 C CA    . MET   A 1 157 ? 51.03112  -8.11742  14.69580  1.000 70.92701  ? 157 MET   A CA    1 
ATOM   1108 C C     . MET   A 1 157 ? 50.34990  -6.97983  13.95026  1.000 64.68828  ? 157 MET   A C     1 
ATOM   1109 O O     . MET   A 1 157 ? 50.66228  -6.72224  12.78579  1.000 67.38121  ? 157 MET   A O     1 
ATOM   1110 C CB    . MET   A 1 157 ? 50.17108  -9.38366  14.63673  1.000 78.02075  ? 157 MET   A CB    1 
ATOM   1111 C CG    . MET   A 1 157 ? 49.79122  -9.85458  13.23516  1.000 81.36763  ? 157 MET   A CG    1 
ATOM   1112 S SD    . MET   A 1 157 ? 49.09549  -11.52107 13.26023  1.000 80.63079  ? 157 MET   A SD    1 
ATOM   1113 C CE    . MET   A 1 157 ? 48.57076  -11.72875 11.55422  1.000 89.71129  ? 157 MET   A CE    1 
ATOM   1114 N N     . HIS   A 1 158 ? 49.42077  -6.29261  14.59426  1.000 62.56562  ? 158 HIS   A N     1 
ATOM   1115 C CA    . HIS   A 1 158 ? 48.53879  -5.34983  13.92047  1.000 60.85706  ? 158 HIS   A CA    1 
ATOM   1116 C C     . HIS   A 1 158 ? 48.41781  -3.99001  14.60135  1.000 62.12633  ? 158 HIS   A C     1 
ATOM   1117 O O     . HIS   A 1 158 ? 47.99327  -3.03748  13.94591  1.000 69.18497  ? 158 HIS   A O     1 
ATOM   1118 C CB    . HIS   A 1 158 ? 47.12659  -5.92729  13.81135  1.000 61.48716  ? 158 HIS   A CB    1 
ATOM   1119 C CG    . HIS   A 1 158 ? 46.96224  -6.98646  12.77402  1.000 62.92942  ? 158 HIS   A CG    1 
ATOM   1120 N ND1   . HIS   A 1 158 ? 47.55621  -6.91857  11.53752  1.000 67.27881  ? 158 HIS   A ND1   1 
ATOM   1121 C CD2   . HIS   A 1 158 ? 46.22845  -8.12490  12.77785  1.000 68.09982  ? 158 HIS   A CD2   1 
ATOM   1122 C CE1   . HIS   A 1 158 ? 47.20935  -7.98160  10.82929  1.000 71.38198  ? 158 HIS   A CE1   1 
ATOM   1123 N NE2   . HIS   A 1 158 ? 46.40072  -8.72718  11.55877  1.000 66.80463  ? 158 HIS   A NE2   1 
ATOM   1124 N N     . GLY   A 1 159 ? 48.71679  -3.86294  15.87779  1.000 57.62223  ? 159 GLY   A N     1 
ATOM   1125 C CA    . GLY   A 1 159 ? 48.60258  -2.57818  16.53683  1.000 56.56815  ? 159 GLY   A CA    1 
ATOM   1126 C C     . GLY   A 1 159 ? 47.47371  -2.52461  17.55476  1.000 61.75040  ? 159 GLY   A C     1 
ATOM   1127 O O     . GLY   A 1 159 ? 46.89803  -3.54093  17.96909  1.000 61.61990  ? 159 GLY   A O     1 
ATOM   1128 N N     . LEU   A 1 160 ? 47.17825  -1.29568  17.97431  1.000 53.88919  ? 160 LEU   A N     1 
ATOM   1129 C CA    . LEU   A 1 160 ? 46.05804  -1.01856  18.86470  1.000 48.47830  ? 160 LEU   A CA    1 
ATOM   1130 C C     . LEU   A 1 160 ? 44.72333  -1.07884  18.11282  1.000 50.26112  ? 160 LEU   A C     1 
ATOM   1131 O O     . LEU   A 1 160 ? 44.63841  -0.80829  16.90793  1.000 54.31835  ? 160 LEU   A O     1 
ATOM   1132 C CB    . LEU   A 1 160 ? 46.24151  0.35504   19.51098  1.000 49.00800  ? 160 LEU   A CB    1 
ATOM   1133 C CG    . LEU   A 1 160 ? 47.60737  0.48728   20.20887  1.000 52.16255  ? 160 LEU   A CG    1 
ATOM   1134 C CD1   . LEU   A 1 160 ? 47.81491  1.81833   20.95007  1.000 45.57557  ? 160 LEU   A CD1   1 
ATOM   1135 C CD2   . LEU   A 1 160 ? 47.82909  -0.70346  21.14613  1.000 55.67173  ? 160 LEU   A CD2   1 
ATOM   1136 N N     . LEU   A 1 161 ? 43.67579  -1.48480  18.83513  1.000 46.77444  ? 161 LEU   A N     1 
ATOM   1137 C CA    . LEU   A 1 161 ? 42.33449  -1.37974  18.28308  1.000 41.96785  ? 161 LEU   A CA    1 
ATOM   1138 C C     . LEU   A 1 161 ? 42.09600  0.01212   17.70896  1.000 44.03556  ? 161 LEU   A C     1 
ATOM   1139 O O     . LEU   A 1 161 ? 41.50474  0.14978   16.62865  1.000 42.01037  ? 161 LEU   A O     1 
ATOM   1140 C CB    . LEU   A 1 161 ? 41.29279  -1.71928  19.34895  1.000 41.00055  ? 161 LEU   A CB    1 
ATOM   1141 C CG    . LEU   A 1 161 ? 39.88290  -1.18643  19.02766  1.000 41.74341  ? 161 LEU   A CG    1 
ATOM   1142 C CD1   . LEU   A 1 161 ? 39.30220  -1.74349  17.76036  1.000 39.63352  ? 161 LEU   A CD1   1 
ATOM   1143 C CD2   . LEU   A 1 161 ? 38.88169  -1.34548  20.16274  1.000 43.33697  ? 161 LEU   A CD2   1 
ATOM   1144 N N     . LEU   A 1 162 ? 42.57922  1.05895   18.39232  1.000 41.81233  ? 162 LEU   A N     1 
ATOM   1145 C CA    . LEU   A 1 162 ? 42.26274  2.39511   17.90868  1.000 42.90709  ? 162 LEU   A CA    1 
ATOM   1146 C C     . LEU   A 1 162 ? 42.97170  2.72267   16.60679  1.000 50.17666  ? 162 LEU   A C     1 
ATOM   1147 O O     . LEU   A 1 162 ? 42.55960  3.67314   15.92266  1.000 55.70905  ? 162 LEU   A O     1 
ATOM   1148 C CB    . LEU   A 1 162 ? 42.57404  3.46878   18.94862  1.000 42.63489  ? 162 LEU   A CB    1 
ATOM   1149 C CG    . LEU   A 1 162 ? 43.91775  3.59653   19.65449  1.000 47.96941  ? 162 LEU   A CG    1 
ATOM   1150 C CD1   . LEU   A 1 162 ? 44.93323  4.15901   18.69590  1.000 49.37075  ? 162 LEU   A CD1   1 
ATOM   1151 C CD2   . LEU   A 1 162 ? 43.76332  4.46804   20.88354  1.000 44.46989  ? 162 LEU   A CD2   1 
ATOM   1152 N N     . ASP   A 1 163 ? 43.99368  1.95146   16.22400  1.000 47.61835  ? 163 ASP   A N     1 
ATOM   1153 C CA    . ASP   A 1 163 ? 44.54144  2.12166   14.88511  1.000 43.22496  ? 163 ASP   A CA    1 
ATOM   1154 C C     . ASP   A 1 163 ? 43.56100  1.72230   13.79778  1.000 50.65339  ? 163 ASP   A C     1 
ATOM   1155 O O     . ASP   A 1 163 ? 43.63405  2.26076   12.68549  1.000 59.41141  ? 163 ASP   A O     1 
ATOM   1156 C CB    . ASP   A 1 163 ? 45.84132  1.36774   14.77007  1.000 42.71843  ? 163 ASP   A CB    1 
ATOM   1157 C CG    . ASP   A 1 163 ? 46.96201  2.04265   15.57916  1.000 56.58359  ? 163 ASP   A CG    1 
ATOM   1158 O OD1   . ASP   A 1 163 ? 47.12422  3.28406   15.43243  1.000 58.73379  ? 163 ASP   A OD1   1 
ATOM   1159 O OD2   . ASP   A 1 163 ? 47.66469  1.36420   16.37072  1.000 57.60827  ? 163 ASP   A OD2   1 
ATOM   1160 N N     . TYR   A 1 164 ? 42.60693  0.84885   14.09971  1.000 47.63283  ? 164 TYR   A N     1 
ATOM   1161 C CA    . TYR   A 1 164 ? 41.63050  0.39761   13.12303  1.000 49.13129  ? 164 TYR   A CA    1 
ATOM   1162 C C     . TYR   A 1 164 ? 40.33347  1.18682   13.19977  1.000 55.68344  ? 164 TYR   A C     1 
ATOM   1163 O O     . TYR   A 1 164 ? 39.38444  0.89758   12.45076  1.000 54.28555  ? 164 TYR   A O     1 
ATOM   1164 C CB    . TYR   A 1 164 ? 41.37146  -1.10216  13.30631  1.000 47.44494  ? 164 TYR   A CB    1 
ATOM   1165 C CG    . TYR   A 1 164 ? 42.56552  -1.92198  12.84908  1.000 53.79033  ? 164 TYR   A CG    1 
ATOM   1166 C CD1   . TYR   A 1 164 ? 43.76063  -1.91995  13.58464  1.000 52.59671  ? 164 TYR   A CD1   1 
ATOM   1167 C CD2   . TYR   A 1 164 ? 42.52536  -2.64878  11.66066  1.000 52.86788  ? 164 TYR   A CD2   1 
ATOM   1168 C CE1   . TYR   A 1 164 ? 44.85705  -2.63756  13.16332  1.000 55.13699  ? 164 TYR   A CE1   1 
ATOM   1169 C CE2   . TYR   A 1 164 ? 43.62274  -3.36836  11.22760  1.000 54.16116  ? 164 TYR   A CE2   1 
ATOM   1170 C CZ    . TYR   A 1 164 ? 44.79186  -3.36550  11.98061  1.000 58.40275  ? 164 TYR   A CZ    1 
ATOM   1171 O OH    . TYR   A 1 164 ? 45.91162  -4.08735  11.57963  1.000 62.46824  ? 164 TYR   A OH    1 
ATOM   1172 N N     . VAL   A 1 165 ? 40.26814  2.17128   14.09538  1.000 55.22315  ? 165 VAL   A N     1 
ATOM   1173 C CA    . VAL   A 1 165 ? 39.12297  3.06619   14.15628  1.000 49.99507  ? 165 VAL   A CA    1 
ATOM   1174 C C     . VAL   A 1 165 ? 39.30828  4.09905   13.05465  1.000 59.04236  ? 165 VAL   A C     1 
ATOM   1175 O O     . VAL   A 1 165 ? 40.34386  4.78156   12.99691  1.000 59.95763  ? 165 VAL   A O     1 
ATOM   1176 C CB    . VAL   A 1 165 ? 39.00127  3.73464   15.52853  1.000 47.37634  ? 165 VAL   A CB    1 
ATOM   1177 C CG1   . VAL   A 1 165 ? 37.84441  4.70357   15.49263  1.000 52.98782  ? 165 VAL   A CG1   1 
ATOM   1178 C CG2   . VAL   A 1 165 ? 38.76893  2.71003   16.58867  1.000 44.12829  ? 165 VAL   A CG2   1 
ATOM   1179 N N     . GLU   A 1 166 ? 38.31414  4.19162   12.16855  1.000 58.46100  ? 166 GLU   A N     1 
ATOM   1180 C CA    . GLU   A 1 166 ? 38.35802  5.00810   10.97113  1.000 56.29888  ? 166 GLU   A CA    1 
ATOM   1181 C C     . GLU   A 1 166 ? 37.49417  6.25651   11.06254  1.000 56.81329  ? 166 GLU   A C     1 
ATOM   1182 O O     . GLU   A 1 166 ? 37.85945  7.29072   10.48430  1.000 57.12350  ? 166 GLU   A O     1 
ATOM   1183 C CB    . GLU   A 1 166 ? 37.88772  4.15988   9.78255   1.000 61.73951  ? 166 GLU   A CB    1 
ATOM   1184 C CG    . GLU   A 1 166 ? 38.06813  4.73653   8.40979   1.000 70.57688  ? 166 GLU   A CG    1 
ATOM   1185 C CD    . GLU   A 1 166 ? 37.40173  3.82089   7.40839   1.000 91.42307  ? 166 GLU   A CD    1 
ATOM   1186 O OE1   . GLU   A 1 166 ? 38.02403  2.79651   7.03249   1.000 86.49487  ? 166 GLU   A OE1   1 
ATOM   1187 O OE2   . GLU   A 1 166 ? 36.21959  4.08161   7.05559   1.000 104.05794 ? 166 GLU   A OE2   1 
ATOM   1188 N N     . GLU   A 1 167 ? 36.36638  6.16826   11.77693  1.000 51.46696  ? 167 GLU   A N     1 
ATOM   1189 C CA    . GLU   A 1 167 ? 35.41099  7.24360   12.01693  1.000 50.92041  ? 167 GLU   A CA    1 
ATOM   1190 C C     . GLU   A 1 167 ? 34.66203  6.94316   13.31851  1.000 55.53390  ? 167 GLU   A C     1 
ATOM   1191 O O     . GLU   A 1 167 ? 34.46875  5.77025   13.66141  1.000 54.11148  ? 167 GLU   A O     1 
ATOM   1192 C CB    . GLU   A 1 167 ? 34.44282  7.35676   10.83763  1.000 51.76705  ? 167 GLU   A CB    1 
ATOM   1193 C CG    . GLU   A 1 167 ? 33.60607  8.62035   10.74642  1.000 58.06164  ? 167 GLU   A CG    1 
ATOM   1194 C CD    . GLU   A 1 167 ? 32.54076  8.51877   9.65702   1.000 71.34172  ? 167 GLU   A CD    1 
ATOM   1195 O OE1   . GLU   A 1 167 ? 32.36984  7.39524   9.11057   1.000 76.74915  ? 167 GLU   A OE1   1 
ATOM   1196 O OE2   . GLU   A 1 167 ? 31.87318  9.54353   9.34723   1.000 73.56208  ? 167 GLU   A OE2   1 
ATOM   1197 N N     . VAL   A 1 168 ? 34.24899  8.01058   14.05390  1.000 53.11892  ? 168 VAL   A N     1 
ATOM   1198 C CA    . VAL   A 1 168 ? 33.40597  7.90246   15.25268  1.000 44.49960  ? 168 VAL   A CA    1 
ATOM   1199 C C     . VAL   A 1 168 ? 32.23818  8.87303   15.20241  1.000 44.09847  ? 168 VAL   A C     1 
ATOM   1200 O O     . VAL   A 1 168 ? 32.30641  9.92316   14.56424  1.000 50.11455  ? 168 VAL   A O     1 
ATOM   1201 C CB    . VAL   A 1 168 ? 34.17366  8.17140   16.55268  1.000 44.01179  ? 168 VAL   A CB    1 
ATOM   1202 C CG1   . VAL   A 1 168 ? 34.98596  6.97113   16.90555  1.000 45.61891  ? 168 VAL   A CG1   1 
ATOM   1203 C CG2   . VAL   A 1 168 ? 35.03190  9.44256   16.42720  1.000 45.71423  ? 168 VAL   A CG2   1 
ATOM   1204 N N     . GLU   A 1 169 ? 31.17641  8.55181   15.93206  1.000 44.02173  ? 169 GLU   A N     1 
ATOM   1205 C CA    . GLU   A 1 169 ? 30.08440  9.49706   16.13697  1.000 48.17065  ? 169 GLU   A CA    1 
ATOM   1206 C C     . GLU   A 1 169 ? 30.20657  10.02294  17.56502  1.000 44.55470  ? 169 GLU   A C     1 
ATOM   1207 O O     . GLU   A 1 169 ? 30.18263  9.24799   18.52466  1.000 40.98997  ? 169 GLU   A O     1 
ATOM   1208 C CB    . GLU   A 1 169 ? 28.72014  8.86597   15.88319  1.000 43.42743  ? 169 GLU   A CB    1 
ATOM   1209 C CG    . GLU   A 1 169 ? 27.59979  9.88606   16.02006  1.000 47.78636  ? 169 GLU   A CG    1 
ATOM   1210 C CD    . GLU   A 1 169 ? 26.20425  9.33310   15.65933  1.000 61.10177  ? 169 GLU   A CD    1 
ATOM   1211 O OE1   . GLU   A 1 169 ? 25.60930  8.59749   16.47835  1.000 57.58499  ? 169 GLU   A OE1   1 
ATOM   1212 O OE2   . GLU   A 1 169 ? 25.71490  9.60407   14.52869  1.000 67.17701  ? 169 GLU   A OE2   1 
ATOM   1213 N N     . VAL   A 1 170 ? 30.39505  11.32626  17.71342  1.000 44.85359  ? 170 VAL   A N     1 
ATOM   1214 C CA    . VAL   A 1 170 ? 30.69327  11.88692  19.02016  1.000 45.63791  ? 170 VAL   A CA    1 
ATOM   1215 C C     . VAL   A 1 170 ? 29.56185  12.81252  19.43516  1.000 50.08885  ? 170 VAL   A C     1 
ATOM   1216 O O     . VAL   A 1 170 ? 29.13351  13.67704  18.65394  1.000 50.21155  ? 170 VAL   A O     1 
ATOM   1217 C CB    . VAL   A 1 170 ? 32.03316  12.62845  19.01641  1.000 47.75054  ? 170 VAL   A CB    1 
ATOM   1218 C CG1   . VAL   A 1 170 ? 32.26044  13.24682  20.38682  1.000 48.74579  ? 170 VAL   A CG1   1 
ATOM   1219 C CG2   . VAL   A 1 170 ? 33.14198  11.65532  18.67569  1.000 47.61270  ? 170 VAL   A CG2   1 
ATOM   1220 N N     . VAL   A 1 171 ? 29.06634  12.62133  20.65560  1.000 41.73935  ? 171 VAL   A N     1 
ATOM   1221 C CA    . VAL   A 1 171 ? 28.13103  13.55742  21.25036  1.000 43.46393  ? 171 VAL   A CA    1 
ATOM   1222 C C     . VAL   A 1 171 ? 28.93411  14.46403  22.14407  1.000 43.61147  ? 171 VAL   A C     1 
ATOM   1223 O O     . VAL   A 1 171 ? 29.65624  13.97325  23.01122  1.000 43.74947  ? 171 VAL   A O     1 
ATOM   1224 C CB    . VAL   A 1 171 ? 27.04884  12.85135  22.06841  1.000 46.14318  ? 171 VAL   A CB    1 
ATOM   1225 C CG1   . VAL   A 1 171 ? 26.38754  13.88341  22.91814  1.000 42.18542  ? 171 VAL   A CG1   1 
ATOM   1226 C CG2   . VAL   A 1 171 ? 26.04450  12.12135  21.16304  1.000 45.87372  ? 171 VAL   A CG2   1 
ATOM   1227 N N     . LEU   A 1 172 ? 28.81157  15.77635  21.94410  1.000 46.15083  ? 172 LEU   A N     1 
ATOM   1228 C CA    . LEU   A 1 172 ? 29.70857  16.75473  22.55876  1.000 49.77566  ? 172 LEU   A CA    1 
ATOM   1229 C C     . LEU   A 1 172 ? 29.08845  17.35413  23.81106  1.000 48.14109  ? 172 LEU   A C     1 
ATOM   1230 O O     . LEU   A 1 172 ? 27.91553  17.12200  24.11663  1.000 46.09656  ? 172 LEU   A O     1 
ATOM   1231 C CB    . LEU   A 1 172 ? 30.06427  17.87125  21.56508  1.000 50.71862  ? 172 LEU   A CB    1 
ATOM   1232 C CG    . LEU   A 1 172 ? 30.84593  17.46819  20.31784  1.000 48.27949  ? 172 LEU   A CG    1 
ATOM   1233 C CD1   . LEU   A 1 172 ? 31.01010  18.66544  19.43593  1.000 46.69603  ? 172 LEU   A CD1   1 
ATOM   1234 C CD2   . LEU   A 1 172 ? 32.18803  16.86748  20.68998  1.000 45.40581  ? 172 LEU   A CD2   1 
ATOM   1235 N N     . ALA   A 1 173 ? 29.89068  18.15130  24.53624  1.000 47.58367  ? 173 ALA   A N     1 
ATOM   1236 C CA    . ALA   A 1 173 ? 29.37802  18.79762  25.75057  1.000 44.13716  ? 173 ALA   A CA    1 
ATOM   1237 C C     . ALA   A 1 173 ? 28.15800  19.67654  25.47095  1.000 46.18471  ? 173 ALA   A C     1 
ATOM   1238 O O     . ALA   A 1 173 ? 27.15644  19.60983  26.18224  1.000 51.73924  ? 173 ALA   A O     1 
ATOM   1239 C CB    . ALA   A 1 173 ? 30.47344  19.62469  26.40813  1.000 52.10562  ? 173 ALA   A CB    1 
ATOM   1240 N N     . ASN   A 1 174 ? 28.20615  20.50157  24.44986  1.000 48.12504  ? 174 ASN   A N     1 
ATOM   1241 C CA    . ASN   A 1 174 ? 27.02197  21.28662  24.13721  1.000 48.25078  ? 174 ASN   A CA    1 
ATOM   1242 C C     . ASN   A 1 174 ? 25.93434  20.48661  23.42005  1.000 52.25454  ? 174 ASN   A C     1 
ATOM   1243 O O     . ASN   A 1 174 ? 25.05764  21.09959  22.78421  1.000 59.87424  ? 174 ASN   A O     1 
ATOM   1244 C CB    . ASN   A 1 174 ? 27.40697  22.48714  23.28666  1.000 55.63268  ? 174 ASN   A CB    1 
ATOM   1245 C CG    . ASN   A 1 174 ? 28.11376  22.08495  22.04004  1.000 56.39986  ? 174 ASN   A CG    1 
ATOM   1246 O OD1   . ASN   A 1 174 ? 28.27486  20.89859  21.74335  1.000 55.21808  ? 174 ASN   A OD1   1 
ATOM   1247 N ND2   . ASN   A 1 174 ? 28.56583  23.05750  21.31284  1.000 54.14870  ? 174 ASN   A ND2   1 
ATOM   1248 N N     . SER   A 1 175 ? 25.98002  19.15279  23.45827  1.000 50.94577  ? 175 SER   A N     1 
ATOM   1249 C CA    . SER   A 1 175 ? 24.96031  18.24807  22.90063  1.000 50.83209  ? 175 SER   A CA    1 
ATOM   1250 C C     . SER   A 1 175 ? 24.91770  18.14567  21.37619  1.000 49.64747  ? 175 SER   A C     1 
ATOM   1251 O O     . SER   A 1 175 ? 24.01367  17.49016  20.83837  1.000 45.33995  ? 175 SER   A O     1 
ATOM   1252 C CB    . SER   A 1 175 ? 23.56734  18.61007  23.39532  1.000 47.37968  ? 175 SER   A CB    1 
ATOM   1253 O OG    . SER   A 1 175 ? 23.53621  18.36044  24.78291  1.000 60.55598  ? 175 SER   A OG    1 
ATOM   1254 N N     . SER   A 1 176 ? 25.86966  18.74359  20.66213  1.000 51.38776  ? 176 SER   A N     1 
ATOM   1255 C CA    . SER   A 1 176 ? 25.95102  18.53518  19.22881  1.000 47.10265  ? 176 SER   A CA    1 
ATOM   1256 C C     . SER   A 1 176 ? 26.38726  17.11289  18.93573  1.000 51.73113  ? 176 SER   A C     1 
ATOM   1257 O O     . SER   A 1 176 ? 27.07091  16.46011  19.73251  1.000 55.18601  ? 176 SER   A O     1 
ATOM   1258 C CB    . SER   A 1 176 ? 26.93871  19.49911  18.60676  1.000 54.41849  ? 176 SER   A CB    1 
ATOM   1259 O OG    . SER   A 1 176 ? 26.46688  20.83283  18.71926  1.000 70.61065  ? 176 SER   A OG    1 
ATOM   1260 N N     . ILE   A 1 177 ? 25.98216  16.62269  17.78314  1.000 52.10242  ? 177 ILE   A N     1 
ATOM   1261 C CA    . ILE   A 1 177 ? 26.38029  15.29572  17.34530  1.000 48.67520  ? 177 ILE   A CA    1 
ATOM   1262 C C     . ILE   A 1 177 ? 27.26312  15.48742  16.12787  1.000 46.56451  ? 177 ILE   A C     1 
ATOM   1263 O O     . ILE   A 1 177 ? 26.82918  15.99401  15.08917  1.000 48.77712  ? 177 ILE   A O     1 
ATOM   1264 C CB    . ILE   A 1 177 ? 25.17150  14.41439  17.04726  1.000 38.52817  ? 177 ILE   A CB    1 
ATOM   1265 C CG1   . ILE   A 1 177 ? 24.53881  14.01659  18.36758  1.000 42.96480  ? 177 ILE   A CG1   1 
ATOM   1266 C CG2   . ILE   A 1 177 ? 25.61346  13.25027  16.24602  1.000 40.18020  ? 177 ILE   A CG2   1 
ATOM   1267 C CD1   . ILE   A 1 177 ? 23.00993  13.91105  18.33354  1.000 42.37297  ? 177 ILE   A CD1   1 
ATOM   1268 N N     . VAL   A 1 178 ? 28.51556  15.13522  16.25702  1.000 45.28020  ? 178 VAL   A N     1 
ATOM   1269 C CA    . VAL   A 1 178 ? 29.44039  15.35310  15.17256  1.000 44.84611  ? 178 VAL   A CA    1 
ATOM   1270 C C     . VAL   A 1 178 ? 30.02449  13.99835  14.79017  1.000 51.54114  ? 178 VAL   A C     1 
ATOM   1271 O O     . VAL   A 1 178 ? 29.92353  13.00975  15.53876  1.000 51.90633  ? 178 VAL   A O     1 
ATOM   1272 C CB    . VAL   A 1 178 ? 30.53124  16.36288  15.58126  1.000 46.91949  ? 178 VAL   A CB    1 
ATOM   1273 C CG1   . VAL   A 1 178 ? 29.87328  17.59546  16.19343  1.000 49.53487  ? 178 VAL   A CG1   1 
ATOM   1274 C CG2   . VAL   A 1 178 ? 31.49182  15.73597  16.58102  1.000 48.77843  ? 178 VAL   A CG2   1 
ATOM   1275 N N     . ARG   A 1 179 ? 30.59646  13.93592  13.59144  1.000 47.44047  ? 179 ARG   A N     1 
ATOM   1276 C CA    . ARG   A 1 179 ? 31.46855  12.81527  13.29310  1.000 48.51806  ? 179 ARG   A CA    1 
ATOM   1277 C C     . ARG   A 1 179 ? 32.91083  13.30949  13.28596  1.000 48.96388  ? 179 ARG   A C     1 
ATOM   1278 O O     . ARG   A 1 179 ? 33.18897  14.51757  13.25020  1.000 46.19277  ? 179 ARG   A O     1 
ATOM   1279 C CB    . ARG   A 1 179 ? 31.09839  12.13874  11.96908  1.000 50.82019  ? 179 ARG   A CB    1 
ATOM   1280 C CG    . ARG   A 1 179 ? 29.61460  11.76421  11.84210  1.000 49.02863  ? 179 ARG   A CG    1 
ATOM   1281 C CD    . ARG   A 1 179 ? 29.36777  10.95414  10.57633  1.000 52.91073  ? 179 ARG   A CD    1 
ATOM   1282 N NE    . ARG   A 1 179 ? 29.68327  9.53596   10.69286  1.000 58.14547  ? 179 ARG   A NE    1 
ATOM   1283 C CZ    . ARG   A 1 179 ? 28.92316  8.68563   11.37401  1.000 69.74583  ? 179 ARG   A CZ    1 
ATOM   1284 N NH1   . ARG   A 1 179 ? 27.76696  9.07223   11.90697  1.000 72.55512  ? 179 ARG   A NH1   1 
ATOM   1285 N NH2   . ARG   A 1 179 ? 29.29128  7.40581   11.46364  1.000 67.82722  ? 179 ARG   A NH2   1 
ATOM   1286 N N     . ALA   A 1 180 ? 33.82868  12.35559  13.37595  1.000 47.58501  ? 180 ALA   A N     1 
ATOM   1287 C CA    . ALA   A 1 180 ? 35.24530  12.65869  13.41974  1.000 48.76658  ? 180 ALA   A CA    1 
ATOM   1288 C C     . ALA   A 1 180 ? 36.00042  11.54557  12.71688  1.000 54.00776  ? 180 ALA   A C     1 
ATOM   1289 O O     . ALA   A 1 180 ? 35.61269  10.37250  12.76800  1.000 52.79580  ? 180 ALA   A O     1 
ATOM   1290 C CB    . ALA   A 1 180 ? 35.74906  12.81994  14.85089  1.000 46.93026  ? 180 ALA   A CB    1 
ATOM   1291 N N     . SER   A 1 181 ? 37.09149  11.92452  12.07578  1.000 51.66198  ? 181 SER   A N     1 
ATOM   1292 C CA    . SER   A 1 181 ? 37.88862  11.00503  11.28313  1.000 51.74837  ? 181 SER   A CA    1 
ATOM   1293 C C     . SER   A 1 181 ? 39.17239  11.72750  10.97129  1.000 53.95450  ? 181 SER   A C     1 
ATOM   1294 O O     . SER   A 1 181 ? 39.32803  12.89914  11.31349  1.000 57.82287  ? 181 SER   A O     1 
ATOM   1295 C CB    . SER   A 1 181 ? 37.17492  10.62714  10.00478  1.000 56.48525  ? 181 SER   A CB    1 
ATOM   1296 O OG    . SER   A 1 181 ? 36.90509  11.82500  9.29504   1.000 59.88152  ? 181 SER   A OG    1 
ATOM   1297 N N     . LYS   A 1 182 ? 40.07841  11.04613  10.27481  1.000 59.62546  ? 182 LYS   A N     1 
ATOM   1298 C CA    . LYS   A 1 182 ? 41.34867  11.69613  9.96384   1.000 64.65356  ? 182 LYS   A CA    1 
ATOM   1299 C C     . LYS   A 1 182 ? 41.17683  12.86870  8.97969   1.000 65.91961  ? 182 LYS   A C     1 
ATOM   1300 O O     . LYS   A 1 182 ? 42.08951  13.70428  8.88628   1.000 66.07869  ? 182 LYS   A O     1 
ATOM   1301 C CB    . LYS   A 1 182 ? 42.35810  10.65541  9.45178   1.000 61.69453  ? 182 LYS   A CB    1 
ATOM   1302 C CG    . LYS   A 1 182 ? 42.62079  9.56397   10.48103  1.000 65.20679  ? 182 LYS   A CG    1 
ATOM   1303 C CD    . LYS   A 1 182 ? 43.64519  8.51106   10.07056  1.000 69.26882  ? 182 LYS   A CD    1 
ATOM   1304 C CE    . LYS   A 1 182 ? 45.05213  9.07757   10.11484  1.000 83.72104  ? 182 LYS   A CE    1 
ATOM   1305 N NZ    . LYS   A 1 182 ? 46.05547  8.07868   9.67467   1.000 93.10197  ? 182 LYS   A NZ    1 
ATOM   1306 N N     . SER   A 1 183 ? 40.00749  12.99191  8.31928   1.000 58.76727  ? 183 SER   A N     1 
ATOM   1307 C CA    . SER   A 1 183 ? 39.72110  14.04336  7.33889   1.000 63.15585  ? 183 SER   A CA    1 
ATOM   1308 C C     . SER   A 1 183 ? 38.73105  15.11349  7.81182   1.000 66.21821  ? 183 SER   A C     1 
ATOM   1309 O O     . SER   A 1 183 ? 38.52782  16.10285  7.09808   1.000 73.28853  ? 183 SER   A O     1 
ATOM   1310 C CB    . SER   A 1 183 ? 39.17260  13.41617  6.03708   1.000 63.80942  ? 183 SER   A CB    1 
ATOM   1311 O OG    . SER   A 1 183 ? 37.86109  12.85370  6.15915   1.000 63.37211  ? 183 SER   A OG    1 
ATOM   1312 N N     . HIS   A 1 184 ? 38.10594  14.95114  8.97088   1.000 62.56156  ? 184 HIS   A N     1 
ATOM   1313 C CA    . HIS   A 1 184 ? 36.95170  15.77110  9.31490   1.000 58.63625  ? 184 HIS   A CA    1 
ATOM   1314 C C     . HIS   A 1 184 ? 36.85494  15.89475  10.82109  1.000 63.81379  ? 184 HIS   A C     1 
ATOM   1315 O O     . HIS   A 1 184 ? 36.39561  14.95613  11.47194  1.000 66.24700  ? 184 HIS   A O     1 
ATOM   1316 C CB    . HIS   A 1 184 ? 35.68755  15.15563  8.76313   1.000 56.64242  ? 184 HIS   A CB    1 
ATOM   1317 C CG    . HIS   A 1 184 ? 34.46544  15.88859  9.17226   1.000 63.69600  ? 184 HIS   A CG    1 
ATOM   1318 N ND1   . HIS   A 1 184 ? 34.34388  17.25393  9.02757   1.000 75.56161  ? 184 HIS   A ND1   1 
ATOM   1319 C CD2   . HIS   A 1 184 ? 33.32632  15.46630  9.76776   1.000 62.49183  ? 184 HIS   A CD2   1 
ATOM   1320 C CE1   . HIS   A 1 184 ? 33.17265  17.64250  9.50249   1.000 75.65271  ? 184 HIS   A CE1   1 
ATOM   1321 N NE2   . HIS   A 1 184 ? 32.53740  16.57739  9.96232   1.000 69.25998  ? 184 HIS   A NE2   1 
ATOM   1322 N N     . ASN   A 1 185 ? 37.21892  17.05148  11.36627  1.000 64.54175  ? 185 ASN   A N     1 
ATOM   1323 C CA    . ASN   A 1 185 ? 37.40216  17.20317  12.81078  1.000 58.59059  ? 185 ASN   A CA    1 
ATOM   1324 C C     . ASN   A 1 185 ? 38.61411  16.40620  13.27220  1.000 55.77635  ? 185 ASN   A C     1 
ATOM   1325 O O     . ASN   A 1 185 ? 38.54635  15.62163  14.21128  1.000 56.60920  ? 185 ASN   A O     1 
ATOM   1326 C CB    . ASN   A 1 185 ? 36.15004  16.79454  13.58396  1.000 51.24546  ? 185 ASN   A CB    1 
ATOM   1327 C CG    . ASN   A 1 185 ? 34.96003  17.68506  13.28736  1.000 56.98157  ? 185 ASN   A CG    1 
ATOM   1328 O OD1   . ASN   A 1 185 ? 35.03887  18.90997  13.38980  1.000 53.95656  ? 185 ASN   A OD1   1 
ATOM   1329 N ND2   . ASN   A 1 185 ? 33.84248  17.06837  12.92646  1.000 60.31642  ? 185 ASN   A ND2   1 
ATOM   1330 N N     . GLU   A 1 186 ? 39.73569  16.62616  12.59440  1.000 59.58191  ? 186 GLU   A N     1 
ATOM   1331 C CA    . GLU   A 1 186 ? 40.95902  15.88136  12.88117  1.000 61.60470  ? 186 GLU   A CA    1 
ATOM   1332 C C     . GLU   A 1 186 ? 41.29506  15.95387  14.36235  1.000 60.11833  ? 186 GLU   A C     1 
ATOM   1333 O O     . GLU   A 1 186 ? 41.65513  14.94836  14.97608  1.000 56.95831  ? 186 GLU   A O     1 
ATOM   1334 C CB    . GLU   A 1 186 ? 42.15491  16.43781  12.08698  1.000 75.74551  ? 186 GLU   A CB    1 
ATOM   1335 C CG    . GLU   A 1 186 ? 42.03932  16.51067  10.56421  1.000 77.82866  ? 186 GLU   A CG    1 
ATOM   1336 C CD    . GLU   A 1 186 ? 41.05892  17.60858  10.10395  1.000 84.83866  ? 186 GLU   A CD    1 
ATOM   1337 O OE1   . GLU   A 1 186 ? 40.53272  18.34854  10.97689  1.000 83.93866  ? 186 GLU   A OE1   1 
ATOM   1338 O OE2   . GLU   A 1 186 ? 40.78396  17.71563  8.88246   1.000 89.52866  ? 186 GLU   A OE2   1 
ATOM   1339 N N     . ASP   A 1 187 ? 41.22283  17.15365  14.94327  1.000 64.84544  ? 187 ASP   A N     1 
ATOM   1340 C CA    . ASP   A 1 187 ? 41.69385  17.33512  16.31223  1.000 62.97664  ? 187 ASP   A CA    1 
ATOM   1341 C C     . ASP   A 1 187 ? 40.84063  16.54282  17.28997  1.000 58.77439  ? 187 ASP   A C     1 
ATOM   1342 O O     . ASP   A 1 187 ? 41.36707  15.83591  18.15577  1.000 57.36225  ? 187 ASP   A O     1 
ATOM   1343 C CB    . ASP   A 1 187 ? 41.69026  18.81384  16.69874  1.000 73.46711  ? 187 ASP   A CB    1 
ATOM   1344 C CG    . ASP   A 1 187 ? 42.47433  19.67124  15.73099  1.000 82.18766  ? 187 ASP   A CG    1 
ATOM   1345 O OD1   . ASP   A 1 187 ? 43.11464  19.10959  14.81011  1.000 75.47904  ? 187 ASP   A OD1   1 
ATOM   1346 O OD2   . ASP   A 1 187 ? 42.42186  20.91609  15.88474  1.000 96.72327  ? 187 ASP   A OD2   1 
ATOM   1347 N N     . LEU   A 1 188 ? 39.51398  16.68164  17.19297  1.000 56.22275  ? 188 LEU   A N     1 
ATOM   1348 C CA    . LEU   A 1 188 ? 38.62746  15.88220  18.02861  1.000 48.84475  ? 188 LEU   A CA    1 
ATOM   1349 C C     . LEU   A 1 188 ? 38.99638  14.42095  17.90655  1.000 50.08170  ? 188 LEU   A C     1 
ATOM   1350 O O     . LEU   A 1 188 ? 39.25500  13.74328  18.90773  1.000 53.00975  ? 188 LEU   A O     1 
ATOM   1351 C CB    . LEU   A 1 188 ? 37.17074  16.09680  17.62255  1.000 51.92172  ? 188 LEU   A CB    1 
ATOM   1352 C CG    . LEU   A 1 188 ? 36.07407  15.24400  18.25525  1.000 46.24187  ? 188 LEU   A CG    1 
ATOM   1353 C CD1   . LEU   A 1 188 ? 36.29737  15.24301  19.73172  1.000 53.28058  ? 188 LEU   A CD1   1 
ATOM   1354 C CD2   . LEU   A 1 188 ? 34.73689  15.86403  17.94270  1.000 41.99976  ? 188 LEU   A CD2   1 
ATOM   1355 N N     . PHE   A 1 189 ? 39.07057  13.93684  16.66115  1.000 51.44210  ? 189 PHE   A N     1 
ATOM   1356 C CA    . PHE   A 1 189 ? 39.40034  12.54258  16.37217  1.000 51.99348  ? 189 PHE   A CA    1 
ATOM   1357 C C     . PHE   A 1 189 ? 40.76594  12.14463  16.93518  1.000 52.70754  ? 189 PHE   A C     1 
ATOM   1358 O O     . PHE   A 1 189 ? 40.97677  10.97494  17.28272  1.000 54.41387  ? 189 PHE   A O     1 
ATOM   1359 C CB    . PHE   A 1 189 ? 39.35905  12.31464  14.86319  1.000 50.15195  ? 189 PHE   A CB    1 
ATOM   1360 C CG    . PHE   A 1 189 ? 39.42057  10.88788  14.46577  1.000 52.03534  ? 189 PHE   A CG    1 
ATOM   1361 C CD1   . PHE   A 1 189 ? 38.34711  10.05583  14.71556  1.000 51.82465  ? 189 PHE   A CD1   1 
ATOM   1362 C CD2   . PHE   A 1 189 ? 40.54836  10.37110  13.82959  1.000 57.68971  ? 189 PHE   A CD2   1 
ATOM   1363 C CE1   . PHE   A 1 189 ? 38.37077  8.73541   14.33679  1.000 52.34444  ? 189 PHE   A CE1   1 
ATOM   1364 C CE2   . PHE   A 1 189 ? 40.58276  9.03783   13.44036  1.000 57.53393  ? 189 PHE   A CE2   1 
ATOM   1365 C CZ    . PHE   A 1 189 ? 39.48677  8.21807   13.70496  1.000 55.72532  ? 189 PHE   A CZ    1 
ATOM   1366 N N     . PHE   A 1 190 ? 41.69980  13.09580  17.03716  1.000 52.84629  ? 190 PHE   A N     1 
ATOM   1367 C CA    . PHE   A 1 190 ? 42.94715  12.84206  17.75381  1.000 50.53603  ? 190 PHE   A CA    1 
ATOM   1368 C C     . PHE   A 1 190 ? 42.67477  12.50243  19.21693  1.000 49.91116  ? 190 PHE   A C     1 
ATOM   1369 O O     . PHE   A 1 190 ? 43.24673  11.54823  19.75550  1.000 48.37723  ? 190 PHE   A O     1 
ATOM   1370 C CB    . PHE   A 1 190 ? 43.88374  14.04635  17.61403  1.000 50.60198  ? 190 PHE   A CB    1 
ATOM   1371 C CG    . PHE   A 1 190 ? 45.07706  14.05107  18.56481  1.000 53.33986  ? 190 PHE   A CG    1 
ATOM   1372 C CD1   . PHE   A 1 190 ? 45.00152  14.65093  19.82012  1.000 51.59834  ? 190 PHE   A CD1   1 
ATOM   1373 C CD2   . PHE   A 1 190 ? 46.28698  13.49317  18.18474  1.000 55.88731  ? 190 PHE   A CD2   1 
ATOM   1374 C CE1   . PHE   A 1 190 ? 46.10440  14.66719  20.68319  1.000 49.60909  ? 190 PHE   A CE1   1 
ATOM   1375 C CE2   . PHE   A 1 190 ? 47.38009  13.51725  19.04511  1.000 56.58350  ? 190 PHE   A CE2   1 
ATOM   1376 C CZ    . PHE   A 1 190 ? 47.28123  14.09951  20.29741  1.000 49.10252  ? 190 PHE   A CZ    1 
ATOM   1377 N N     . ALA   A 1 191 ? 41.78075  13.25713  19.87322  1.000 49.75923  ? 191 ALA   A N     1 
ATOM   1378 C CA    . ALA   A 1 191 ? 41.55106  13.06326  21.30582  1.000 48.26693  ? 191 ALA   A CA    1 
ATOM   1379 C C     . ALA   A 1 191 ? 40.66236  11.84895  21.57792  1.000 52.57982  ? 191 ALA   A C     1 
ATOM   1380 O O     . ALA   A 1 191 ? 40.85083  11.12106  22.56867  1.000 50.37703  ? 191 ALA   A O     1 
ATOM   1381 C CB    . ALA   A 1 191 ? 40.93480  14.32011  21.90480  1.000 39.15871  ? 191 ALA   A CB    1 
ATOM   1382 N N     . VAL   A 1 192 ? 39.69113  11.60474  20.70864  1.000 49.27890  ? 192 VAL   A N     1 
ATOM   1383 C CA    . VAL   A 1 192 ? 38.86298  10.43985  20.91624  1.000 45.30872  ? 192 VAL   A CA    1 
ATOM   1384 C C     . VAL   A 1 192 ? 39.70949  9.16186   20.85153  1.000 48.27787  ? 192 VAL   A C     1 
ATOM   1385 O O     . VAL   A 1 192 ? 39.37522  8.15715   21.48943  1.000 47.19084  ? 192 VAL   A O     1 
ATOM   1386 C CB    . VAL   A 1 192 ? 37.72789  10.46950  19.88517  1.000 42.50972  ? 192 VAL   A CB    1 
ATOM   1387 C CG1   . VAL   A 1 192 ? 36.97884  9.17883   19.88274  1.000 44.05781  ? 192 VAL   A CG1   1 
ATOM   1388 C CG2   . VAL   A 1 192 ? 36.82742  11.64623  20.14620  1.000 42.38930  ? 192 VAL   A CG2   1 
ATOM   1389 N N     . ARG   A 1 193 ? 40.82809  9.17190   20.11740  1.000 49.52261  ? 193 ARG   A N     1 
ATOM   1390 C CA    . ARG   A 1 193 ? 41.67294  7.96527   20.01050  1.000 47.62596  ? 193 ARG   A CA    1 
ATOM   1391 C C     . ARG   A 1 193 ? 42.79434  8.01571   21.04602  1.000 52.20701  ? 193 ARG   A C     1 
ATOM   1392 O O     . ARG   A 1 193 ? 43.98546  8.08207   20.72391  1.000 56.48853  ? 193 ARG   A O     1 
ATOM   1393 C CB    . ARG   A 1 193 ? 42.23538  7.79878   18.60005  1.000 46.96013  ? 193 ARG   A CB    1 
ATOM   1394 C CG    . ARG   A 1 193 ? 41.16805  7.46521   17.59232  1.000 51.89142  ? 193 ARG   A CG    1 
ATOM   1395 C CD    . ARG   A 1 193 ? 41.59093  7.06497   16.17404  1.000 53.58380  ? 193 ARG   A CD    1 
ATOM   1396 N NE    . ARG   A 1 193 ? 42.38986  8.05983   15.47878  1.000 59.18057  ? 193 ARG   A NE    1 
ATOM   1397 C CZ    . ARG   A 1 193 ? 43.34181  7.77579   14.59730  1.000 68.72268  ? 193 ARG   A CZ    1 
ATOM   1398 N NH1   . ARG   A 1 193 ? 43.46167  6.55565   14.06864  1.000 59.13950  ? 193 ARG   A NH1   1 
ATOM   1399 N NH2   . ARG   A 1 193 ? 44.15517  8.75389   14.18669  1.000 67.99866  ? 193 ARG   A NH2   1 
ATOM   1400 N N     . GLY   A 1 194 ? 42.37671  7.99246   22.31530  1.000 47.79551  ? 194 GLY   A N     1 
ATOM   1401 C CA    . GLY   A 1 194 ? 43.26581  7.78982   23.44401  1.000 43.75705  ? 194 GLY   A CA    1 
ATOM   1402 C C     . GLY   A 1 194 ? 42.72778  8.45456   24.68999  1.000 48.75462  ? 194 GLY   A C     1 
ATOM   1403 O O     . GLY   A 1 194 ? 43.12788  8.11278   25.82327  1.000 45.90015  ? 194 GLY   A O     1 
ATOM   1404 N N     . ALA   A 1 195 ? 41.80061  9.40789   24.47397  1.000 47.21360  ? 195 ALA   A N     1 
ATOM   1405 C CA    . ALA   A 1 195 ? 41.31260  10.25105  25.55447  1.000 46.10147  ? 195 ALA   A CA    1 
ATOM   1406 C C     . ALA   A 1 195 ? 39.83962  10.65031  25.39120  1.000 51.28752  ? 195 ALA   A C     1 
ATOM   1407 O O     . ALA   A 1 195 ? 39.40354  11.67281  25.95532  1.000 50.95554  ? 195 ALA   A O     1 
ATOM   1408 C CB    . ALA   A 1 195 ? 42.18892  11.49046  25.69206  1.000 42.25598  ? 195 ALA   A CB    1 
ATOM   1409 N N     . ALA   A 1 196 ? 39.04611  9.82614   24.68646  1.000 50.24765  ? 196 ALA   A N     1 
ATOM   1410 C CA    . ALA   A 1 196 ? 37.63642  10.15772  24.45889  1.000 46.42359  ? 196 ALA   A CA    1 
ATOM   1411 C C     . ALA   A 1 196 ? 36.89426  10.47098  25.75975  1.000 48.82742  ? 196 ALA   A C     1 
ATOM   1412 O O     . ALA   A 1 196 ? 35.95942  11.28089  25.75554  1.000 48.18042  ? 196 ALA   A O     1 
ATOM   1413 C CB    . ALA   A 1 196 ? 36.92582  9.03447   23.69414  1.000 41.37236  ? 196 ALA   A CB    1 
ATOM   1414 N N     . SER   A 1 197 ? 37.30563  9.87980   26.89024  1.000 50.49630  ? 197 SER   A N     1 
ATOM   1415 C CA    . SER   A 1 197 ? 36.51855  10.07537  28.10777  1.000 46.81646  ? 197 SER   A CA    1 
ATOM   1416 C C     . SER   A 1 197 ? 36.39489  11.54422  28.46733  1.000 49.96037  ? 197 SER   A C     1 
ATOM   1417 O O     . SER   A 1 197 ? 35.42389  11.92424  29.12894  1.000 49.01995  ? 197 SER   A O     1 
ATOM   1418 C CB    . SER   A 1 197 ? 37.12114  9.34393   29.30217  1.000 44.91351  ? 197 SER   A CB    1 
ATOM   1419 O OG    . SER   A 1 197 ? 38.45456  9.77363   29.51054  1.000 52.39387  ? 197 SER   A OG    1 
ATOM   1420 N N     . SER   A 1 198 ? 37.35027  12.37577  28.05330  1.000 51.36169  ? 198 SER   A N     1 
ATOM   1421 C CA    . SER   A 1 198 ? 37.38523  13.74773  28.54830  1.000 51.69796  ? 198 SER   A CA    1 
ATOM   1422 C C     . SER   A 1 198 ? 36.78536  14.77162  27.57604  1.000 52.60720  ? 198 SER   A C     1 
ATOM   1423 O O     . SER   A 1 198 ? 36.57339  15.91934  27.99314  1.000 50.88305  ? 198 SER   A O     1 
ATOM   1424 C CB    . SER   A 1 198 ? 38.83210  14.12278  28.92411  1.000 50.23787  ? 198 SER   A CB    1 
ATOM   1425 O OG    . SER   A 1 198 ? 39.36425  13.18779  29.86529  1.000 48.45398  ? 198 SER   A OG    1 
ATOM   1426 N N     . VAL   A 1 199 ? 36.43654  14.38120  26.33624  1.000 48.99611  ? 199 VAL   A N     1 
ATOM   1427 C CA    . VAL   A 1 199 ? 35.95679  15.33954  25.34112  1.000 48.04261  ? 199 VAL   A CA    1 
ATOM   1428 C C     . VAL   A 1 199 ? 34.54118  15.05504  24.81525  1.000 49.02174  ? 199 VAL   A C     1 
ATOM   1429 O O     . VAL   A 1 199 ? 33.92496  15.96110  24.21225  1.000 51.03557  ? 199 VAL   A O     1 
ATOM   1430 C CB    . VAL   A 1 199 ? 36.94173  15.45140  24.15314  1.000 47.49329  ? 199 VAL   A CB    1 
ATOM   1431 C CG1   . VAL   A 1 199 ? 38.32755  15.91462  24.63039  1.000 42.76336  ? 199 VAL   A CG1   1 
ATOM   1432 C CG2   . VAL   A 1 199 ? 37.03193  14.17520  23.38815  1.000 46.34321  ? 199 VAL   A CG2   1 
ATOM   1433 N N     . GLY   A 1 200 ? 33.98840  13.86060  25.00461  1.000 43.28338  ? 200 GLY   A N     1 
ATOM   1434 C CA    . GLY   A 1 200 ? 32.70416  13.53222  24.39948  1.000 36.62536  ? 200 GLY   A CA    1 
ATOM   1435 C C     . GLY   A 1 200 ? 32.34190  12.08450  24.65885  1.000 41.90000  ? 200 GLY   A C     1 
ATOM   1436 O O     . GLY   A 1 200 ? 33.09530  11.32863  25.27551  1.000 44.53189  ? 200 GLY   A O     1 
ATOM   1437 N N     . ILE   A 1 201 ? 31.14329  11.72036  24.20932  1.000 44.97479  ? 201 ILE   A N     1 
ATOM   1438 C CA    . ILE   A 1 201 ? 30.63072  10.35352  24.29018  1.000 38.42652  ? 201 ILE   A CA    1 
ATOM   1439 C C     . ILE   A 1 201 ? 30.59461  9.78006   22.88142  1.000 43.12147  ? 201 ILE   A C     1 
ATOM   1440 O O     . ILE   A 1 201 ? 29.90629  10.31332  21.99311  1.000 43.97111  ? 201 ILE   A O     1 
ATOM   1441 C CB    . ILE   A 1 201 ? 29.23863  10.28780  24.93841  1.000 40.61362  ? 201 ILE   A CB    1 
ATOM   1442 C CG1   . ILE   A 1 201 ? 29.24461  11.01494  26.27259  1.000 41.79321  ? 201 ILE   A CG1   1 
ATOM   1443 C CG2   . ILE   A 1 201 ? 28.80505  8.86807   25.14455  1.000 41.92948  ? 201 ILE   A CG2   1 
ATOM   1444 C CD1   . ILE   A 1 201 ? 28.07546  10.67464  27.07455  1.000 37.67183  ? 201 ILE   A CD1   1 
ATOM   1445 N N     . VAL   A 1 202 ? 31.36272  8.71583   22.67088  1.000 39.50532  ? 202 VAL   A N     1 
ATOM   1446 C CA    . VAL   A 1 202 ? 31.45048  8.07372   21.36792  1.000 38.26471  ? 202 VAL   A CA    1 
ATOM   1447 C C     . VAL   A 1 202 ? 30.24080  7.14990   21.27004  1.000 42.60152  ? 202 VAL   A C     1 
ATOM   1448 O O     . VAL   A 1 202 ? 30.16190  6.15765   21.99804  1.000 45.41108  ? 202 VAL   A O     1 
ATOM   1449 C CB    . VAL   A 1 202 ? 32.76995  7.30437   21.21666  1.000 34.28450  ? 202 VAL   A CB    1 
ATOM   1450 C CG1   . VAL   A 1 202 ? 32.74805  6.46496   20.00791  1.000 35.45018  ? 202 VAL   A CG1   1 
ATOM   1451 C CG2   . VAL   A 1 202 ? 33.94570  8.25303   21.14938  1.000 38.52032  ? 202 VAL   A CG2   1 
ATOM   1452 N N     . THR   A 1 203 ? 29.28799  7.45917   20.38782  1.000 38.52254  ? 203 THR   A N     1 
ATOM   1453 C CA    . THR   A 1 203 ? 28.09663  6.63580   20.29038  1.000 37.92507  ? 203 THR   A CA    1 
ATOM   1454 C C     . THR   A 1 203 ? 28.04625  5.72353   19.07741  1.000 44.64621  ? 203 THR   A C     1 
ATOM   1455 O O     . THR   A 1 203 ? 27.01735  5.05986   18.86665  1.000 48.84113  ? 203 THR   A O     1 
ATOM   1456 C CB    . THR   A 1 203 ? 26.85771  7.50402   20.26970  1.000 39.75131  ? 203 THR   A CB    1 
ATOM   1457 O OG1   . THR   A 1 203 ? 26.77516  8.11116   18.98805  1.000 43.51984  ? 203 THR   A OG1   1 
ATOM   1458 C CG2   . THR   A 1 203 ? 26.95025  8.58367   21.34071  1.000 43.07101  ? 203 THR   A CG2   1 
ATOM   1459 N N     . ASP   A 1 204 ? 29.09352  5.68225   18.25545  1.000 47.13429  ? 204 ASP   A N     1 
ATOM   1460 C CA    . ASP   A 1 204 ? 29.19423  4.63240   17.25019  1.000 44.68438  ? 204 ASP   A CA    1 
ATOM   1461 C C     . ASP   A 1 204 ? 30.59748  4.65287   16.70022  1.000 46.26859  ? 204 ASP   A C     1 
ATOM   1462 O O     . ASP   A 1 204 ? 31.24482  5.69810   16.68878  1.000 46.05948  ? 204 ASP   A O     1 
ATOM   1463 C CB    . ASP   A 1 204 ? 28.19036  4.82662   16.12469  1.000 57.99043  ? 204 ASP   A CB    1 
ATOM   1464 C CG    . ASP   A 1 204 ? 27.64672  3.49080   15.57469  1.000 73.28433  ? 204 ASP   A CG    1 
ATOM   1465 O OD1   . ASP   A 1 204 ? 26.93592  2.76211   16.34389  1.000 78.93157  ? 204 ASP   A OD1   1 
ATOM   1466 O OD2   . ASP   A 1 204 ? 27.92045  3.18508   14.38244  1.000 70.46123  ? 204 ASP   A OD2   1 
ATOM   1467 N N     . PHE   A 1 205 ? 31.04019  3.49393   16.20766  1.000 54.15372  ? 205 PHE   A N     1 
ATOM   1468 C CA    . PHE   A 1 205 ? 32.42822  3.24438   15.80206  1.000 49.54801  ? 205 PHE   A CA    1 
ATOM   1469 C C     . PHE   A 1 205 ? 32.47506  2.65650   14.39625  1.000 56.04416  ? 205 PHE   A C     1 
ATOM   1470 O O     . PHE   A 1 205 ? 31.86890  1.60427   14.15483  1.000 54.78778  ? 205 PHE   A O     1 
ATOM   1471 C CB    . PHE   A 1 205 ? 33.07720  2.24277   16.74639  1.000 44.00488  ? 205 PHE   A CB    1 
ATOM   1472 C CG    . PHE   A 1 205 ? 33.43918  2.79018   18.07335  1.000 41.52917  ? 205 PHE   A CG    1 
ATOM   1473 C CD1   . PHE   A 1 205 ? 34.65705  3.41847   18.25964  1.000 43.13567  ? 205 PHE   A CD1   1 
ATOM   1474 C CD2   . PHE   A 1 205 ? 32.60365  2.63133   19.15534  1.000 47.26515  ? 205 PHE   A CD2   1 
ATOM   1475 C CE1   . PHE   A 1 205 ? 35.03283  3.90154   19.49408  1.000 42.65690  ? 205 PHE   A CE1   1 
ATOM   1476 C CE2   . PHE   A 1 205 ? 32.97425  3.11818   20.40790  1.000 47.19812  ? 205 PHE   A CE2   1 
ATOM   1477 C CZ    . PHE   A 1 205 ? 34.19314  3.74956   20.57044  1.000 45.93603  ? 205 PHE   A CZ    1 
ATOM   1478 N N     . SER   A 1 206 ? 33.22094  3.29479   13.48261  1.000 56.89172  ? 206 SER   A N     1 
ATOM   1479 C CA    . SER   A 1 206 ? 33.63125  2.65499   12.23251  1.000 49.78319  ? 206 SER   A CA    1 
ATOM   1480 C C     . SER   A 1 206 ? 34.98792  2.03062   12.47080  1.000 54.72024  ? 206 SER   A C     1 
ATOM   1481 O O     . SER   A 1 206 ? 35.96642  2.73982   12.72400  1.000 58.60813  ? 206 SER   A O     1 
ATOM   1482 C CB    . SER   A 1 206 ? 33.72460  3.63985   11.07429  1.000 54.84881  ? 206 SER   A CB    1 
ATOM   1483 O OG    . SER   A 1 206 ? 32.45998  4.18264   10.77400  1.000 68.03788  ? 206 SER   A OG    1 
ATOM   1484 N N     . ILE   A 1 207 ? 35.05559  0.71153   12.40714  1.000 57.18142  ? 207 ILE   A N     1 
ATOM   1485 C CA    . ILE   A 1 207 ? 36.30657  0.03180   12.68482  1.000 53.67403  ? 207 ILE   A CA    1 
ATOM   1486 C C     . ILE   A 1 207 ? 36.62061  -0.88751  11.51517  1.000 53.98214  ? 207 ILE   A C     1 
ATOM   1487 O O     . ILE   A 1 207 ? 35.81775  -1.76885  11.18202  1.000 50.75112  ? 207 ILE   A O     1 
ATOM   1488 C CB    . ILE   A 1 207 ? 36.24358  -0.74569  14.00312  1.000 52.21654  ? 207 ILE   A CB    1 
ATOM   1489 C CG1   . ILE   A 1 207 ? 35.95523  0.22763   15.14857  1.000 46.20692  ? 207 ILE   A CG1   1 
ATOM   1490 C CG2   . ILE   A 1 207 ? 37.56790  -1.41359  14.26287  1.000 50.12653  ? 207 ILE   A CG2   1 
ATOM   1491 C CD1   . ILE   A 1 207 ? 35.83297  -0.42344  16.47963  1.000 41.04576  ? 207 ILE   A CD1   1 
ATOM   1492 N N     . ARG   A 1 208 ? 37.76460  -0.64801  10.87255  1.000 56.18420  ? 208 ARG   A N     1 
ATOM   1493 C CA    . ARG   A 1 208 ? 38.34028  -1.59130  9.92659   1.000 57.04523  ? 208 ARG   A CA    1 
ATOM   1494 C C     . ARG   A 1 208 ? 38.66118  -2.92523  10.59402  1.000 56.81378  ? 208 ARG   A C     1 
ATOM   1495 O O     . ARG   A 1 208 ? 38.95808  -2.99603  11.78742  1.000 53.71629  ? 208 ARG   A O     1 
ATOM   1496 C CB    . ARG   A 1 208 ? 39.61968  -1.00972  9.33310   1.000 57.23928  ? 208 ARG   A CB    1 
ATOM   1497 C CG    . ARG   A 1 208 ? 39.38830  -0.01414  8.25803   1.000 64.44703  ? 208 ARG   A CG    1 
ATOM   1498 C CD    . ARG   A 1 208 ? 40.70363  0.41822   7.69149   1.000 64.74192  ? 208 ARG   A CD    1 
ATOM   1499 N NE    . ARG   A 1 208 ? 41.44400  1.22316   8.65249   1.000 61.63096  ? 208 ARG   A NE    1 
ATOM   1500 C CZ    . ARG   A 1 208 ? 42.61480  0.88867   9.18032   1.000 67.00466  ? 208 ARG   A CZ    1 
ATOM   1501 N NH1   . ARG   A 1 208 ? 43.20013  -0.28305  8.90254   1.000 57.60507  ? 208 ARG   A NH1   1 
ATOM   1502 N NH2   . ARG   A 1 208 ? 43.22463  1.75885   9.99454   1.000 63.49791  ? 208 ARG   A NH2   1 
ATOM   1503 N N     . THR   A 1 209 ? 38.65131  -3.99553  9.79900   1.000 58.70489  ? 209 THR   A N     1 
ATOM   1504 C CA    . THR   A 1 209 ? 39.01975  -5.30219  10.32080  1.000 60.34702  ? 209 THR   A CA    1 
ATOM   1505 C C     . THR   A 1 209 ? 40.10349  -5.95384  9.45715   1.000 58.63450  ? 209 THR   A C     1 
ATOM   1506 O O     . THR   A 1 209 ? 40.36482  -5.56231  8.32024   1.000 53.57550  ? 209 THR   A O     1 
ATOM   1507 C CB    . THR   A 1 209 ? 37.80387  -6.24447  10.42345  1.000 56.86208  ? 209 THR   A CB    1 
ATOM   1508 O OG1   . THR   A 1 209 ? 37.36398  -6.62563  9.11896   1.000 57.89261  ? 209 THR   A OG1   1 
ATOM   1509 C CG2   . THR   A 1 209 ? 36.65823  -5.52187  11.11886  1.000 53.41138  ? 209 THR   A CG2   1 
ATOM   1510 N N     . GLU   A 1 210 ? 40.72927  -6.95566  10.04608  1.000 61.09197  ? 210 GLU   A N     1 
ATOM   1511 C CA    . GLU   A 1 210 ? 41.66134  -7.86129  9.41493   1.000 59.74526  ? 210 GLU   A CA    1 
ATOM   1512 C C     . GLU   A 1 210 ? 40.97516  -9.21427  9.23184   1.000 64.12273  ? 210 GLU   A C     1 
ATOM   1513 O O     . GLU   A 1 210 ? 39.93504  -9.47805  9.84779   1.000 66.83161  ? 210 GLU   A O     1 
ATOM   1514 C CB    . GLU   A 1 210 ? 42.90149  -8.03033  10.29828  1.000 58.35042  ? 210 GLU   A CB    1 
ATOM   1515 C CG    . GLU   A 1 210 ? 43.68400  -6.76664  10.43618  1.000 61.66646  ? 210 GLU   A CG    1 
ATOM   1516 C CD    . GLU   A 1 210 ? 44.28925  -6.34432  9.13261   1.000 70.87455  ? 210 GLU   A CD    1 
ATOM   1517 O OE1   . GLU   A 1 210 ? 44.34571  -7.20555  8.23049   1.000 78.88801  ? 210 GLU   A OE1   1 
ATOM   1518 O OE2   . GLU   A 1 210 ? 44.71775  -5.16862  9.00608   1.000 71.45385  ? 210 GLU   A OE2   1 
ATOM   1519 N N     . PRO   A 1 211 ? 41.51530  -10.09371 8.39442   1.000 64.22849  ? 211 PRO   A N     1 
ATOM   1520 C CA    . PRO   A 1 211 ? 41.02291  -11.47726 8.36233   1.000 61.64944  ? 211 PRO   A CA    1 
ATOM   1521 C C     . PRO   A 1 211 ? 41.69155  -12.31555 9.44470   1.000 61.16179  ? 211 PRO   A C     1 
ATOM   1522 O O     . PRO   A 1 211 ? 42.83272  -12.06523 9.84655   1.000 59.23005  ? 211 PRO   A O     1 
ATOM   1523 C CB    . PRO   A 1 211 ? 41.40482  -11.95162 6.96074   1.000 54.35865  ? 211 PRO   A CB    1 
ATOM   1524 C CG    . PRO   A 1 211 ? 42.62239  -11.13162 6.63824   1.000 56.70649  ? 211 PRO   A CG    1 
ATOM   1525 C CD    . PRO   A 1 211 ? 42.51340  -9.82385  7.34475   1.000 58.30209  ? 211 PRO   A CD    1 
ATOM   1526 N N     . VAL   A 1 212 ? 40.95102  -13.29612 9.95975   1.000 61.49852  ? 212 VAL   A N     1 
ATOM   1527 C CA    . VAL   A 1 212 ? 41.39213  -13.93769 11.19944  1.000 62.42394  ? 212 VAL   A CA    1 
ATOM   1528 C C     . VAL   A 1 212 ? 42.62408  -14.75462 10.85041  1.000 63.27113  ? 212 VAL   A C     1 
ATOM   1529 O O     . VAL   A 1 212 ? 42.77993  -15.12323 9.68518   1.000 75.89356  ? 212 VAL   A O     1 
ATOM   1530 C CB    . VAL   A 1 212 ? 40.31263  -14.83820 11.80368  1.000 56.98341  ? 212 VAL   A CB    1 
ATOM   1531 C CG1   . VAL   A 1 212 ? 39.05034  -14.05642 12.00996  1.000 59.88142  ? 212 VAL   A CG1   1 
ATOM   1532 C CG2   . VAL   A 1 212 ? 40.09667  -16.02690 10.93400  1.000 59.87861  ? 212 VAL   A CG2   1 
ATOM   1533 N N     . PRO   A 1 213 ? 43.51077  -15.06634 11.79380  1.000 58.08604  ? 213 PRO   A N     1 
ATOM   1534 C CA    . PRO   A 1 213 ? 44.60998  -15.98058 11.48955  1.000 65.71436  ? 213 PRO   A CA    1 
ATOM   1535 C C     . PRO   A 1 213 ? 44.10767  -17.41185 11.37585  1.000 73.95730  ? 213 PRO   A C     1 
ATOM   1536 O O     . PRO   A 1 213 ? 43.20364  -17.84625 12.09918  1.000 75.74605  ? 213 PRO   A O     1 
ATOM   1537 C CB    . PRO   A 1 213 ? 45.53809  -15.83561 12.69634  1.000 66.42555  ? 213 PRO   A CB    1 
ATOM   1538 C CG    . PRO   A 1 213 ? 45.15123  -14.58636 13.28791  1.000 67.70047  ? 213 PRO   A CG    1 
ATOM   1539 C CD    . PRO   A 1 213 ? 43.67026  -14.51639 13.13784  1.000 61.24210  ? 213 PRO   A CD    1 
ATOM   1540 N N     . VAL   A 1 214 ? 44.73430  -18.16430 10.47396  1.000 75.67391  ? 214 VAL   A N     1 
ATOM   1541 C CA    . VAL   A 1 214 ? 44.27530  -19.52393 10.22262  1.000 79.42923  ? 214 VAL   A CA    1 
ATOM   1542 C C     . VAL   A 1 214 ? 44.66232  -20.45608 11.37319  1.000 77.30777  ? 214 VAL   A C     1 
ATOM   1543 O O     . VAL   A 1 214 ? 43.92270  -21.40133 11.69566  1.000 68.34209  ? 214 VAL   A O     1 
ATOM   1544 C CB    . VAL   A 1 214 ? 44.86104  -19.98994 8.87895   1.000 82.58964  ? 214 VAL   A CB    1 
ATOM   1545 C CG1   . VAL   A 1 214 ? 44.21129  -21.29484 8.40496   1.000 83.03738  ? 214 VAL   A CG1   1 
ATOM   1546 C CG2   . VAL   A 1 214 ? 44.74329  -18.86281 7.85485   1.000 75.87292  ? 214 VAL   A CG2   1 
ATOM   1547 N N     . SER   A 1 215 ? 45.81264  -20.19162 12.00101  1.000 79.14520  ? 215 SER   A N     1 
ATOM   1548 C CA    . SER   A 1 215 ? 46.40897  -21.04042 13.02727  1.000 78.01058  ? 215 SER   A CA    1 
ATOM   1549 C C     . SER   A 1 215 ? 46.88714  -20.13748 14.15114  1.000 76.77771  ? 215 SER   A C     1 
ATOM   1550 O O     . SER   A 1 215 ? 47.90795  -19.45708 14.02219  1.000 80.83832  ? 215 SER   A O     1 
ATOM   1551 C CB    . SER   A 1 215 ? 47.58185  -21.85164 12.46158  1.000 80.15761  ? 215 SER   A CB    1 
ATOM   1552 O OG    . SER   A 1 215 ? 48.30795  -22.53307 13.47937  1.000 83.51942  ? 215 SER   A OG    1 
ATOM   1553 N N     . SER   A 1 216 ? 46.16704  -20.12501 15.24969  1.000 72.02227  ? 216 SER   A N     1 
ATOM   1554 C CA    . SER   A 1 216 ? 46.64805  -19.44391 16.43516  1.000 75.38346  ? 216 SER   A CA    1 
ATOM   1555 C C     . SER   A 1 216 ? 47.18002  -20.50233 17.39532  1.000 75.68078  ? 216 SER   A C     1 
ATOM   1556 O O     . SER   A 1 216 ? 46.50241  -21.50370 17.65893  1.000 77.36527  ? 216 SER   A O     1 
ATOM   1557 C CB    . SER   A 1 216 ? 45.52889  -18.60656 17.05519  1.000 75.27189  ? 216 SER   A CB    1 
ATOM   1558 O OG    . SER   A 1 216 ? 44.76264  -17.99062 16.02573  1.000 76.30912  ? 216 SER   A OG    1 
ATOM   1559 N N     . VAL   A 1 217 ? 48.39906  -20.29061 17.88334  1.000 72.03914  ? 217 VAL   A N     1 
ATOM   1560 C CA    . VAL   A 1 217 ? 49.11582  -21.22064 18.75610  1.000 69.20043  ? 217 VAL   A CA    1 
ATOM   1561 C C     . VAL   A 1 217 ? 49.35425  -20.54918 20.10257  1.000 74.37971  ? 217 VAL   A C     1 
ATOM   1562 O O     . VAL   A 1 217 ? 50.19615  -19.64680 20.20403  1.000 80.28056  ? 217 VAL   A O     1 
ATOM   1563 C CB    . VAL   A 1 217 ? 50.45553  -21.65355 18.13580  1.000 71.07979  ? 217 VAL   A CB    1 
ATOM   1564 C CG1   . VAL   A 1 217 ? 51.28798  -22.43758 19.12135  1.000 72.19694  ? 217 VAL   A CG1   1 
ATOM   1565 C CG2   . VAL   A 1 217 ? 50.21479  -22.46668 16.88286  1.000 79.40481  ? 217 VAL   A CG2   1 
ATOM   1566 N N     . THR   A 1 218 ? 48.64788  -21.00139 21.13976  1.000 73.52348  ? 218 THR   A N     1 
ATOM   1567 C CA    . THR   A 1 218 ? 48.89502  -20.57180 22.51167  1.000 73.20516  ? 218 THR   A CA    1 
ATOM   1568 C C     . THR   A 1 218 ? 50.08987  -21.33385 23.09890  1.000 73.19669  ? 218 THR   A C     1 
ATOM   1569 O O     . THR   A 1 218 ? 50.45183  -22.41145 22.63054  1.000 74.99727  ? 218 THR   A O     1 
ATOM   1570 C CB    . THR   A 1 218 ? 47.66235  -20.82565 23.36408  1.000 75.84956  ? 218 THR   A CB    1 
ATOM   1571 O OG1   . THR   A 1 218 ? 47.47867  -22.23954 23.46515  1.000 83.60938  ? 218 THR   A OG1   1 
ATOM   1572 C CG2   . THR   A 1 218 ? 46.42476  -20.25769 22.67894  1.000 67.58538  ? 218 THR   A CG2   1 
ATOM   1573 N N     . TYR   A 1 219 ? 50.71768  -20.76569 24.12458  1.000 73.21148  ? 219 TYR   A N     1 
ATOM   1574 C CA    . TYR   A 1 219 ? 51.88361  -21.42766 24.69709  1.000 74.99298  ? 219 TYR   A CA    1 
ATOM   1575 C C     . TYR   A 1 219 ? 52.12789  -20.87954 26.08332  1.000 77.39253  ? 219 TYR   A C     1 
ATOM   1576 O O     . TYR   A 1 219 ? 51.98737  -19.67621 26.31605  1.000 77.45179  ? 219 TYR   A O     1 
ATOM   1577 C CB    . TYR   A 1 219 ? 53.15800  -21.25832 23.85776  1.000 80.10108  ? 219 TYR   A CB    1 
ATOM   1578 C CG    . TYR   A 1 219 ? 53.71630  -19.86086 23.81769  1.000 78.13102  ? 219 TYR   A CG    1 
ATOM   1579 C CD1   . TYR   A 1 219 ? 54.50077  -19.36992 24.85300  1.000 80.66972  ? 219 TYR   A CD1   1 
ATOM   1580 C CD2   . TYR   A 1 219 ? 53.50029  -19.05091 22.71772  1.000 73.36142  ? 219 TYR   A CD2   1 
ATOM   1581 C CE1   . TYR   A 1 219 ? 55.00676  -18.09736 24.80284  1.000 79.42359  ? 219 TYR   A CE1   1 
ATOM   1582 C CE2   . TYR   A 1 219 ? 54.00528  -17.80808 22.65544  1.000 75.28645  ? 219 TYR   A CE2   1 
ATOM   1583 C CZ    . TYR   A 1 219 ? 54.75445  -17.32718 23.68752  1.000 76.35852  ? 219 TYR   A CZ    1 
ATOM   1584 O OH    . TYR   A 1 219 ? 55.24647  -16.06014 23.57177  1.000 76.97606  ? 219 TYR   A OH    1 
ATOM   1585 N N     . SER   A 1 220 ? 52.52649  -21.76726 26.98838  1.000 84.73733  ? 220 SER   A N     1 
ATOM   1586 C CA    . SER   A 1 220 ? 52.53107  -21.43622 28.40914  1.000 86.01176  ? 220 SER   A CA    1 
ATOM   1587 C C     . SER   A 1 220 ? 53.62063  -22.27351 29.08287  1.000 85.86791  ? 220 SER   A C     1 
ATOM   1588 O O     . SER   A 1 220 ? 53.42187  -23.43478 29.44622  1.000 92.32460  ? 220 SER   A O     1 
ATOM   1589 C CB    . SER   A 1 220 ? 51.16026  -21.66659 29.02997  1.000 81.54229  ? 220 SER   A CB    1 
ATOM   1590 O OG    . SER   A 1 220 ? 51.02508  -20.92114 30.22440  1.000 87.64469  ? 220 SER   A OG    1 
ATOM   1591 N N     . TYR   A 1 221 ? 54.77131  -21.66639 29.23483  1.000 80.68437  ? 221 TYR   A N     1 
ATOM   1592 C CA    . TYR   A 1 221 ? 55.86261  -22.26884 29.95350  1.000 83.21925  ? 221 TYR   A CA    1 
ATOM   1593 C C     . TYR   A 1 221 ? 55.77061  -21.80229 31.40984  1.000 88.97658  ? 221 TYR   A C     1 
ATOM   1594 O O     . TYR   A 1 221 ? 55.34005  -20.67796 31.67199  1.000 92.83694  ? 221 TYR   A O     1 
ATOM   1595 C CB    . TYR   A 1 221 ? 57.15467  -21.83353 29.28555  1.000 84.47446  ? 221 TYR   A CB    1 
ATOM   1596 C CG    . TYR   A 1 221 ? 57.20421  -22.23956 27.82038  1.000 87.90263  ? 221 TYR   A CG    1 
ATOM   1597 C CD1   . TYR   A 1 221 ? 56.98711  -23.55962 27.44501  1.000 93.50361  ? 221 TYR   A CD1   1 
ATOM   1598 C CD2   . TYR   A 1 221 ? 57.52266  -21.31726 26.81612  1.000 87.66209  ? 221 TYR   A CD2   1 
ATOM   1599 C CE1   . TYR   A 1 221 ? 57.04583  -23.95181 26.10848  1.000 91.53614  ? 221 TYR   A CE1   1 
ATOM   1600 C CE2   . TYR   A 1 221 ? 57.59371  -21.69634 25.48197  1.000 90.65643  ? 221 TYR   A CE2   1 
ATOM   1601 C CZ    . TYR   A 1 221 ? 57.35464  -23.01940 25.13736  1.000 92.37212  ? 221 TYR   A CZ    1 
ATOM   1602 O OH    . TYR   A 1 221 ? 57.41765  -23.41953 23.82731  1.000 90.86121  ? 221 TYR   A OH    1 
ATOM   1603 N N     . ILE   A 1 222 ? 56.13001  -22.66268 32.36421  1.000 89.55738  ? 222 ILE   A N     1 
ATOM   1604 C CA    . ILE   A 1 222 ? 56.08126  -22.25611 33.76886  1.000 90.36934  ? 222 ILE   A CA    1 
ATOM   1605 C C     . ILE   A 1 222 ? 57.35474  -22.59907 34.52570  1.000 92.26113  ? 222 ILE   A C     1 
ATOM   1606 O O     . ILE   A 1 222 ? 58.04351  -23.57529 34.22517  1.000 96.73436  ? 222 ILE   A O     1 
ATOM   1607 C CB    . ILE   A 1 222 ? 54.89345  -22.85625 34.53278  1.000 91.25489  ? 222 ILE   A CB    1 
ATOM   1608 C CG1   . ILE   A 1 222 ? 53.58943  -22.55802 33.80624  1.000 85.85071  ? 222 ILE   A CG1   1 
ATOM   1609 C CG2   . ILE   A 1 222 ? 54.87950  -22.35562 35.97811  1.000 86.59895  ? 222 ILE   A CG2   1 
ATOM   1610 C CD1   . ILE   A 1 222 ? 52.40491  -23.03464 34.58398  1.000 90.47669  ? 222 ILE   A CD1   1 
ATOM   1611 N N     . TRP   A 1 223 ? 57.64196  -21.77609 35.53334  1.000 88.98844  ? 223 TRP   A N     1 
ATOM   1612 C CA    . TRP   A 1 223 ? 58.68897  -22.02392 36.51485  1.000 92.96073  ? 223 TRP   A CA    1 
ATOM   1613 C C     . TRP   A 1 223 ? 58.07480  -21.80272 37.88804  1.000 98.29716  ? 223 TRP   A C     1 
ATOM   1614 O O     . TRP   A 1 223 ? 57.77980  -20.65880 38.25099  1.000 99.00394  ? 223 TRP   A O     1 
ATOM   1615 C CB    . TRP   A 1 223 ? 59.89207  -21.09267 36.32748  1.000 92.86447  ? 223 TRP   A CB    1 
ATOM   1616 C CG    . TRP   A 1 223 ? 60.75570  -21.38613 35.14391  1.000 99.35714  ? 223 TRP   A CG    1 
ATOM   1617 C CD1   . TRP   A 1 223 ? 61.78871  -22.28001 35.08023  1.000 102.18424 ? 223 TRP   A CD1   1 
ATOM   1618 C CD2   . TRP   A 1 223 ? 60.69356  -20.75090 33.85948  1.000 96.90759  ? 223 TRP   A CD2   1 
ATOM   1619 N NE1   . TRP   A 1 223 ? 62.35719  -22.25390 33.82787  1.000 104.77549 ? 223 TRP   A NE1   1 
ATOM   1620 C CE2   . TRP   A 1 223 ? 61.70218  -21.32461 33.06108  1.000 100.87523 ? 223 TRP   A CE2   1 
ATOM   1621 C CE3   . TRP   A 1 223 ? 59.87088  -19.76968 33.30323  1.000 90.49860  ? 223 TRP   A CE3   1 
ATOM   1622 C CZ2   . TRP   A 1 223 ? 61.91083  -20.94385 31.74135  1.000 99.73660  ? 223 TRP   A CZ2   1 
ATOM   1623 C CZ3   . TRP   A 1 223 ? 60.07625  -19.39810 31.99945  1.000 90.55626  ? 223 TRP   A CZ3   1 
ATOM   1624 C CH2   . TRP   A 1 223 ? 61.08738  -19.97865 31.23342  1.000 98.81769  ? 223 TRP   A CH2   1 
ATOM   1625 N N     . GLU   A 1 224 ? 57.87041  -22.88482 38.64620  1.000 99.12657  ? 224 GLU   A N     1 
ATOM   1626 C CA    . GLU   A 1 224 ? 57.54623  -22.71080 40.05337  1.000 95.02593  ? 224 GLU   A CA    1 
ATOM   1627 C C     . GLU   A 1 224 ? 58.82601  -22.52148 40.86315  1.000 100.31382 ? 224 GLU   A C     1 
ATOM   1628 O O     . GLU   A 1 224 ? 59.93428  -22.85618 40.42410  1.000 103.46619 ? 224 GLU   A O     1 
ATOM   1629 C CB    . GLU   A 1 224 ? 56.74318  -23.88622 40.61763  1.000 95.31172  ? 224 GLU   A CB    1 
ATOM   1630 C CG    . GLU   A 1 224 ? 55.26493  -23.95811 40.19987  1.000 101.82146 ? 224 GLU   A CG    1 
ATOM   1631 C CD    . GLU   A 1 224 ? 54.99591  -24.95024 39.06839  1.000 106.10974 ? 224 GLU   A CD    1 
ATOM   1632 O OE1   . GLU   A 1 224 ? 55.86023  -25.82914 38.83105  1.000 98.02356  ? 224 GLU   A OE1   1 
ATOM   1633 O OE2   . GLU   A 1 224 ? 53.92303  -24.84876 38.41846  1.000 105.62353 ? 224 GLU   A OE2   1 
ATOM   1634 N N     . GLY   A 1 225 ? 58.66394  -21.96655 42.05623  1.000 101.89694 ? 225 GLY   A N     1 
ATOM   1635 C CA    . GLY   A 1 225 ? 59.81515  -21.67430 42.88845  1.000 102.77056 ? 225 GLY   A CA    1 
ATOM   1636 C C     . GLY   A 1 225 ? 59.83222  -20.22813 43.33496  1.000 103.44203 ? 225 GLY   A C     1 
ATOM   1637 O O     . GLY   A 1 225 ? 59.79863  -19.29998 42.51388  1.000 103.14083 ? 225 GLY   A O     1 
ATOM   1638 N N     . THR   A 1 226 ? 59.88490  -20.03002 44.65336  1.000 96.24606  ? 226 THR   A N     1 
ATOM   1639 C CA    . THR   A 1 226 ? 59.87582  -18.69854 45.24237  1.000 96.97358  ? 226 THR   A CA    1 
ATOM   1640 C C     . THR   A 1 226 ? 61.28934  -18.12782 45.44960  1.000 95.92597  ? 226 THR   A C     1 
ATOM   1641 O O     . THR   A 1 226 ? 61.48598  -17.27930 46.32747  1.000 88.72077  ? 226 THR   A O     1 
ATOM   1642 C CB    . THR   A 1 226 ? 59.07646  -18.73532 46.54638  1.000 96.74510  ? 226 THR   A CB    1 
ATOM   1643 O OG1   . THR   A 1 226 ? 59.74504  -19.56543 47.50489  1.000 108.32919 ? 226 THR   A OG1   1 
ATOM   1644 C CG2   . THR   A 1 226 ? 57.69157  -19.31666 46.28492  1.000 86.96952  ? 226 THR   A CG2   1 
ATOM   1645 N N     . ASP   A 1 227 ? 62.26721  -18.54379 44.62629  1.000 98.10532  ? 227 ASP   A N     1 
ATOM   1646 C CA    . ASP   A 1 227 ? 63.64596  -18.07653 44.75921  1.000 99.90331  ? 227 ASP   A CA    1 
ATOM   1647 C C     . ASP   A 1 227 ? 63.91015  -16.84923 43.88821  1.000 100.87802 ? 227 ASP   A C     1 
ATOM   1648 O O     . ASP   A 1 227 ? 64.07202  -16.99649 42.66170  1.000 99.52735  ? 227 ASP   A O     1 
ATOM   1649 C CB    . ASP   A 1 227 ? 64.63122  -19.17602 44.39193  1.000 98.11923  ? 227 ASP   A CB    1 
ATOM   1650 C CG    . ASP   A 1 227 ? 66.07972  -18.72507 44.52338  1.000 99.39996  ? 227 ASP   A CG    1 
ATOM   1651 O OD1   . ASP   A 1 227 ? 66.33796  -17.77196 45.29276  1.000 100.15692 ? 227 ASP   A OD1   1 
ATOM   1652 O OD2   . ASP   A 1 227 ? 66.94754  -19.27489 43.81192  1.000 94.01485  ? 227 ASP   A OD2   1 
ATOM   1653 N N     . PRO   A 1 228 ? 64.00161  -15.63039 44.46781  1.000 96.85613  ? 228 PRO   A N     1 
ATOM   1654 C CA    . PRO   A 1 228 ? 64.31952  -14.43845 43.67041  1.000 100.89491 ? 228 PRO   A CA    1 
ATOM   1655 C C     . PRO   A 1 228 ? 65.32506  -14.64012 42.54171  1.000 102.80728 ? 228 PRO   A C     1 
ATOM   1656 O O     . PRO   A 1 228 ? 65.03900  -14.28428 41.38805  1.000 104.12008 ? 228 PRO   A O     1 
ATOM   1657 C CB    . PRO   A 1 228 ? 64.86047  -13.47804 44.73524  1.000 98.44468  ? 228 PRO   A CB    1 
ATOM   1658 C CG    . PRO   A 1 228 ? 64.01647  -13.81523 45.96934  1.000 96.16157  ? 228 PRO   A CG    1 
ATOM   1659 C CD    . PRO   A 1 228 ? 63.50219  -15.24797 45.80253  1.000 88.88141  ? 228 PRO   A CD    1 
ATOM   1660 N N     . ALA   A 1 229 ? 66.49640  -15.21112 42.85536  1.000 100.08478 ? 229 ALA   A N     1 
ATOM   1661 C CA    . ALA   A 1 229 ? 67.57486  -15.30867 41.86731  1.000 103.89840 ? 229 ALA   A CA    1 
ATOM   1662 C C     . ALA   A 1 229 ? 67.13733  -16.06740 40.62087  1.000 105.36053 ? 229 ALA   A C     1 
ATOM   1663 O O     . ALA   A 1 229 ? 67.50014  -15.69610 39.49696  1.000 100.93055 ? 229 ALA   A O     1 
ATOM   1664 C CB    . ALA   A 1 229 ? 68.79280  -15.99082 42.48248  1.000 111.00851 ? 229 ALA   A CB    1 
ATOM   1665 N N     . ALA   A 1 230 ? 66.39311  -17.16192 40.80329  1.000 108.00794 ? 230 ALA   A N     1 
ATOM   1666 C CA    . ALA   A 1 230 ? 65.92213  -17.93383 39.65683  1.000 106.19214 ? 230 ALA   A CA    1 
ATOM   1667 C C     . ALA   A 1 230 ? 64.90484  -17.13596 38.85047  1.000 107.30842 ? 230 ALA   A C     1 
ATOM   1668 O O     . ALA   A 1 230 ? 64.91864  -17.16107 37.60912  1.000 106.52072 ? 230 ALA   A O     1 
ATOM   1669 C CB    . ALA   A 1 230 ? 65.32250  -19.25872 40.13464  1.000 98.19091  ? 230 ALA   A CB    1 
ATOM   1670 N N     . ARG   A 1 231 ? 64.03327  -16.40165 39.55522  1.000 104.48181 ? 231 ARG   A N     1 
ATOM   1671 C CA    . ARG   A 1 231 ? 62.98094  -15.62094 38.91928  1.000 99.25734  ? 231 ARG   A CA    1 
ATOM   1672 C C     . ARG   A 1 231 ? 63.55719  -14.44825 38.13794  1.000 99.79274  ? 231 ARG   A C     1 
ATOM   1673 O O     . ARG   A 1 231 ? 63.15725  -14.20152 36.99216  1.000 97.84927  ? 231 ARG   A O     1 
ATOM   1674 C CB    . ARG   A 1 231 ? 62.01475  -15.13194 39.98804  1.000 96.65182  ? 231 ARG   A CB    1 
ATOM   1675 C CG    . ARG   A 1 231 ? 61.36450  -16.27161 40.71902  1.000 94.84510  ? 231 ARG   A CG    1 
ATOM   1676 C CD    . ARG   A 1 231 ? 60.81592  -15.81743 42.05328  1.000 97.99001  ? 231 ARG   A CD    1 
ATOM   1677 N NE    . ARG   A 1 231 ? 59.52399  -15.14514 41.98434  1.000 94.20542  ? 231 ARG   A NE    1 
ATOM   1678 C CZ    . ARG   A 1 231 ? 58.40078  -15.75479 41.63899  1.000 92.70088  ? 231 ARG   A CZ    1 
ATOM   1679 N NH1   . ARG   A 1 231 ? 58.39360  -17.02777 41.26705  1.000 89.39670  ? 231 ARG   A NH1   1 
ATOM   1680 N NH2   . ARG   A 1 231 ? 57.25569  -15.08445 41.70222  1.000 92.43515  ? 231 ARG   A NH2   1 
ATOM   1681 N N     . ALA   A 1 232 ? 64.49924  -13.71541 38.73794  1.000 93.29678  ? 232 ALA   A N     1 
ATOM   1682 C CA    . ALA   A 1 232 ? 65.15551  -12.64201 38.00365  1.000 95.22802  ? 232 ALA   A CA    1 
ATOM   1683 C C     . ALA   A 1 232 ? 65.91633  -13.16225 36.78465  1.000 99.80541  ? 232 ALA   A C     1 
ATOM   1684 O O     . ALA   A 1 232 ? 66.10592  -12.41499 35.81519  1.000 100.72665 ? 232 ALA   A O     1 
ATOM   1685 C CB    . ALA   A 1 232 ? 66.08606  -11.86651 38.92614  1.000 96.99111  ? 232 ALA   A CB    1 
ATOM   1686 N N     . GLU   A 1 233 ? 66.37008  -14.42715 36.81144  1.000 98.81928  ? 233 GLU   A N     1 
ATOM   1687 C CA    . GLU   A 1 233 ? 67.00283  -15.00620 35.62578  1.000 95.19439  ? 233 GLU   A CA    1 
ATOM   1688 C C     . GLU   A 1 233 ? 65.97895  -15.20173 34.52170  1.000 96.44244  ? 233 GLU   A C     1 
ATOM   1689 O O     . GLU   A 1 233 ? 66.23379  -14.87870 33.35616  1.000 95.32789  ? 233 GLU   A O     1 
ATOM   1690 C CB    . GLU   A 1 233 ? 67.68412  -16.33314 35.96054  1.000 93.58243  ? 233 GLU   A CB    1 
ATOM   1691 N N     . VAL   A 1 234 ? 64.79720  -15.69518 34.87778  1.000 100.66645 ? 234 VAL   A N     1 
ATOM   1692 C CA    . VAL   A 1 234 ? 63.72187  -15.81514 33.89975  1.000 100.33605 ? 234 VAL   A CA    1 
ATOM   1693 C C     . VAL   A 1 234 ? 63.41141  -14.45217 33.28890  1.000 100.54808 ? 234 VAL   A C     1 
ATOM   1694 O O     . VAL   A 1 234 ? 63.46979  -14.27356 32.06575  1.000 93.68944  ? 234 VAL   A O     1 
ATOM   1695 C CB    . VAL   A 1 234 ? 62.48074  -16.43392 34.55331  1.000 92.33826  ? 234 VAL   A CB    1 
ATOM   1696 C CG1   . VAL   A 1 234 ? 61.48357  -16.73314 33.49410  1.000 92.37728  ? 234 VAL   A CG1   1 
ATOM   1697 C CG2   . VAL   A 1 234 ? 62.87397  -17.66486 35.32755  1.000 93.19953  ? 234 VAL   A CG2   1 
ATOM   1698 N N     . PHE   A 1 235 ? 63.08817  -13.46681 34.14029  1.000 97.53601  ? 235 PHE   A N     1 
ATOM   1699 C CA    . PHE   A 1 235 ? 62.75748  -12.12858 33.65900  1.000 89.91920  ? 235 PHE   A CA    1 
ATOM   1700 C C     . PHE   A 1 235 ? 63.84178  -11.57041 32.76090  1.000 94.08634  ? 235 PHE   A C     1 
ATOM   1701 O O     . PHE   A 1 235 ? 63.57107  -11.11860 31.64197  1.000 94.51444  ? 235 PHE   A O     1 
ATOM   1702 C CB    . PHE   A 1 235 ? 62.54972  -11.15022 34.80231  1.000 89.34645  ? 235 PHE   A CB    1 
ATOM   1703 C CG    . PHE   A 1 235 ? 62.49386  -9.71112  34.33578  1.000 98.33563  ? 235 PHE   A CG    1 
ATOM   1704 C CD1   . PHE   A 1 235 ? 63.65371  -8.95135  34.20789  1.000 101.11977 ? 235 PHE   A CD1   1 
ATOM   1705 C CD2   . PHE   A 1 235 ? 61.29075  -9.12335  33.98821  1.000 102.09866 ? 235 PHE   A CD2   1 
ATOM   1706 C CE1   . PHE   A 1 235 ? 63.60454  -7.62171  33.76367  1.000 100.89711 ? 235 PHE   A CE1   1 
ATOM   1707 C CE2   . PHE   A 1 235 ? 61.23944  -7.79987  33.54638  1.000 106.87866 ? 235 PHE   A CE2   1 
ATOM   1708 C CZ    . PHE   A 1 235 ? 62.40130  -7.05088  33.43649  1.000 101.99866 ? 235 PHE   A CZ    1 
ATOM   1709 N N     . LEU   A 1 236 ? 65.06668  -11.49550 33.28293  1.000 96.26927  ? 236 LEU   A N     1 
ATOM   1710 C CA    . LEU   A 1 236 ? 66.15067  -10.91156 32.50415  1.000 96.69339  ? 236 LEU   A CA    1 
ATOM   1711 C C     . LEU   A 1 236 ? 66.27824  -11.59939 31.15565  1.000 93.79972  ? 236 LEU   A C     1 
ATOM   1712 O O     . LEU   A 1 236 ? 66.49898  -10.93492 30.13373  1.000 88.07828  ? 236 LEU   A O     1 
ATOM   1713 C CB    . LEU   A 1 236 ? 67.45085  -10.99149 33.28599  1.000 95.09511  ? 236 LEU   A CB    1 
ATOM   1714 C CG    . LEU   A 1 236 ? 67.51694  -9.83220  34.26435  1.000 102.32662 ? 236 LEU   A CG    1 
ATOM   1715 C CD1   . LEU   A 1 236 ? 68.53930  -10.11895 35.35156  1.000 109.46065 ? 236 LEU   A CD1   1 
ATOM   1716 C CD2   . LEU   A 1 236 ? 67.83719  -8.55608  33.49865  1.000 97.67670  ? 236 LEU   A CD2   1 
ATOM   1717 N N     . THR   A 1 237 ? 66.12799  -12.93007 31.13583  1.000 92.48805  ? 237 THR   A N     1 
ATOM   1718 C CA    . THR   A 1 237 ? 66.05939  -13.66993 29.87736  1.000 93.12034  ? 237 THR   A CA    1 
ATOM   1719 C C     . THR   A 1 237 ? 64.97072  -13.10306 28.97624  1.000 94.41410  ? 237 THR   A C     1 
ATOM   1720 O O     . THR   A 1 237 ? 65.23061  -12.68161 27.84125  1.000 91.02432  ? 237 THR   A O     1 
ATOM   1721 C CB    . THR   A 1 237 ? 65.78817  -15.15782 30.14638  1.000 100.49567 ? 237 THR   A CB    1 
ATOM   1722 O OG1   . THR   A 1 237 ? 66.67670  -15.65258 31.15740  1.000 104.17866 ? 237 THR   A OG1   1 
ATOM   1723 C CG2   . THR   A 1 237 ? 65.97187  -15.98614 28.86174  1.000 99.31474  ? 237 THR   A CG2   1 
ATOM   1724 N N     . TRP   A 1 238 ? 63.73713  -13.07717 29.48395  1.000 93.12855  ? 238 TRP   A N     1 
ATOM   1725 C CA    . TRP   A 1 238 ? 62.60275  -12.61661 28.69583  1.000 85.33901  ? 238 TRP   A CA    1 
ATOM   1726 C C     . TRP   A 1 238 ? 62.81890  -11.19833 28.20129  1.000 85.49742  ? 238 TRP   A C     1 
ATOM   1727 O O     . TRP   A 1 238 ? 62.75151  -10.93679 26.99540  1.000 84.43631  ? 238 TRP   A O     1 
ATOM   1728 C CB    . TRP   A 1 238 ? 61.35549  -12.73889 29.55009  1.000 86.29766  ? 238 TRP   A CB    1 
ATOM   1729 C CG    . TRP   A 1 238 ? 60.09826  -12.26606 28.97636  1.000 86.06520  ? 238 TRP   A CG    1 
ATOM   1730 C CD1   . TRP   A 1 238 ? 59.16118  -13.01247 28.31583  1.000 80.27035  ? 238 TRP   A CD1   1 
ATOM   1731 C CD2   . TRP   A 1 238 ? 59.54994  -10.96530 29.11507  1.000 87.52153  ? 238 TRP   A CD2   1 
ATOM   1732 N NE1   . TRP   A 1 238 ? 58.08350  -12.23472 27.99340  1.000 76.32109  ? 238 TRP   A NE1   1 
ATOM   1733 C CE2   . TRP   A 1 238 ? 58.29626  -10.97135 28.48063  1.000 82.95880  ? 238 TRP   A CE2   1 
ATOM   1734 C CE3   . TRP   A 1 238 ? 60.00826  -9.77915  29.69594  1.000 86.91606  ? 238 TRP   A CE3   1 
ATOM   1735 C CZ2   . TRP   A 1 238 ? 57.49969  -9.83594  28.41034  1.000 78.99542  ? 238 TRP   A CZ2   1 
ATOM   1736 C CZ3   . TRP   A 1 238 ? 59.21337  -8.66054  29.62563  1.000 80.90531  ? 238 TRP   A CZ3   1 
ATOM   1737 C CH2   . TRP   A 1 238 ? 57.97872  -8.69347  28.98656  1.000 75.22314  ? 238 TRP   A CH2   1 
ATOM   1738 N N     . GLN   A 1 239 ? 63.13603  -10.27836 29.11470  1.000 83.45191  ? 239 GLN   A N     1 
ATOM   1739 C CA    . GLN   A 1 239 ? 63.44793  -8.90984  28.70630  1.000 85.83246  ? 239 GLN   A CA    1 
ATOM   1740 C C     . GLN   A 1 239 ? 64.58793  -8.84980  27.69609  1.000 86.24432  ? 239 GLN   A C     1 
ATOM   1741 O O     . GLN   A 1 239 ? 64.59003  -8.00005  26.79609  1.000 79.38072  ? 239 GLN   A O     1 
ATOM   1742 C CB    . GLN   A 1 239 ? 63.82194  -8.06767  29.90892  1.000 88.12699  ? 239 GLN   A CB    1 
ATOM   1743 C CG    . GLN   A 1 239 ? 64.32095  -6.71729  29.48854  1.000 84.39444  ? 239 GLN   A CG    1 
ATOM   1744 C CD    . GLN   A 1 239 ? 64.77434  -5.92378  30.66275  1.000 94.20965  ? 239 GLN   A CD    1 
ATOM   1745 O OE1   . GLN   A 1 239 ? 64.25642  -4.83980  30.93583  1.000 94.19290  ? 239 GLN   A OE1   1 
ATOM   1746 N NE2   . GLN   A 1 239 ? 65.77187  -6.44794  31.37034  1.000 100.91876 ? 239 GLN   A NE2   1 
ATOM   1747 N N     . SER   A 1 240 ? 65.60133  -9.69056  27.86198  1.000 90.08666  ? 240 SER   A N     1 
ATOM   1748 C CA    . SER   A 1 240 ? 66.73954  -9.56412  26.96982  1.000 88.40596  ? 240 SER   A CA    1 
ATOM   1749 C C     . SER   A 1 240 ? 66.43420  -10.16158 25.60073  1.000 88.17580  ? 240 SER   A C     1 
ATOM   1750 O O     . SER   A 1 240 ? 66.83856  -9.59572  24.57832  1.000 86.35665  ? 240 SER   A O     1 
ATOM   1751 C CB    . SER   A 1 240 ? 67.96706  -10.21250 27.57808  1.000 91.48707  ? 240 SER   A CB    1 
ATOM   1752 O OG    . SER   A 1 240 ? 69.07018  -10.00215 26.71564  1.000 99.72311  ? 240 SER   A OG    1 
ATOM   1753 N N     . LEU   A 1 241 ? 65.74224  -11.31258 25.56366  1.000 90.29070  ? 241 LEU   A N     1 
ATOM   1754 C CA    . LEU   A 1 241 ? 65.21568  -11.83924 24.30286  1.000 95.80014  ? 241 LEU   A CA    1 
ATOM   1755 C C     . LEU   A 1 241 ? 64.40051  -10.80079 23.55430  1.000 94.07514  ? 241 LEU   A C     1 
ATOM   1756 O O     . LEU   A 1 241 ? 64.63402  -10.54717 22.36164  1.000 92.64070  ? 241 LEU   A O     1 
ATOM   1757 C CB    . LEU   A 1 241 ? 64.34356  -13.08350 24.54293  1.000 98.97659  ? 241 LEU   A CB    1 
ATOM   1758 C CG    . LEU   A 1 241 ? 64.89394  -14.48458 24.29191  1.000 100.46543 ? 241 LEU   A CG    1 
ATOM   1759 C CD1   . LEU   A 1 241 ? 63.91695  -15.54303 24.78139  1.000 99.46808  ? 241 LEU   A CD1   1 
ATOM   1760 C CD2   . LEU   A 1 241 ? 65.12662  -14.62792 22.77050  1.000 98.49866  ? 241 LEU   A CD2   1 
ATOM   1761 N N     . LEU   A 1 242 ? 63.39322  -10.23828 24.23314  1.000 89.76931  ? 242 LEU   A N     1 
ATOM   1762 C CA    . LEU   A 1 242 ? 62.51698  -9.24343  23.62627  1.000 85.19502  ? 242 LEU   A CA    1 
ATOM   1763 C C     . LEU   A 1 242 ? 63.32559  -8.10112  23.03195  1.000 82.24335  ? 242 LEU   A C     1 
ATOM   1764 O O     . LEU   A 1 242 ? 63.22663  -7.82530  21.83632  1.000 81.31891  ? 242 LEU   A O     1 
ATOM   1765 C CB    . LEU   A 1 242 ? 61.51768  -8.74810  24.67260  1.000 84.02405  ? 242 LEU   A CB    1 
ATOM   1766 C CG    . LEU   A 1 242 ? 60.41725  -7.74006  24.32505  1.000 77.64037  ? 242 LEU   A CG    1 
ATOM   1767 C CD1   . LEU   A 1 242 ? 59.66431  -8.16110  23.07673  1.000 78.47838  ? 242 LEU   A CD1   1 
ATOM   1768 C CD2   . LEU   A 1 242 ? 59.44333  -7.58555  25.51328  1.000 72.65092  ? 242 LEU   A CD2   1 
ATOM   1769 N N     . ALA   A 1 243 ? 64.16707  -7.45481  23.85083  1.000 84.61683  ? 243 ALA   A N     1 
ATOM   1770 C CA    . ALA   A 1 243 ? 65.08666  -6.43416  23.36001  1.000 83.08889  ? 243 ALA   A CA    1 
ATOM   1771 C C     . ALA   A 1 243 ? 66.03300  -6.96388  22.28990  1.000 80.76863  ? 243 ALA   A C     1 
ATOM   1772 O O     . ALA   A 1 243 ? 66.69193  -6.16575  21.61389  1.000 73.81567  ? 243 ALA   A O     1 
ATOM   1773 C CB    . ALA   A 1 243 ? 65.89203  -5.84070  24.52326  1.000 83.35532  ? 243 ALA   A CB    1 
ATOM   1774 N N     . GLY   A 1 244 ? 66.12565  -8.27908  22.12409  1.000 87.43057  ? 244 GLY   A N     1 
ATOM   1775 C CA    . GLY   A 1 244 ? 66.89200  -8.82757  21.02560  1.000 89.25998  ? 244 GLY   A CA    1 
ATOM   1776 C C     . GLY   A 1 244 ? 66.35172  -8.37270  19.68951  1.000 88.85044  ? 244 GLY   A C     1 
ATOM   1777 O O     . GLY   A 1 244 ? 67.03373  -7.66406  18.94890  1.000 84.78395  ? 244 GLY   A O     1 
ATOM   1778 N N     . GLY   A 1 245 ? 65.09636  -8.71669  19.40698  1.000 96.15930  ? 245 GLY   A N     1 
ATOM   1779 C CA    . GLY   A 1 245 ? 64.56661  -8.69665  18.06100  1.000 97.63647  ? 245 GLY   A CA    1 
ATOM   1780 C C     . GLY   A 1 245 ? 64.65998  -10.04091 17.37686  1.000 101.13587 ? 245 GLY   A C     1 
ATOM   1781 O O     . GLY   A 1 245 ? 64.15902  -10.19886 16.25158  1.000 97.55929  ? 245 GLY   A O     1 
ATOM   1782 N N     . SER   A 1 246 ? 65.31183  -11.00592 18.02340  1.000 97.69827  ? 246 SER   A N     1 
ATOM   1783 C CA    . SER   A 1 246 ? 65.22330  -12.39963 17.62637  1.000 101.73620 ? 246 SER   A CA    1 
ATOM   1784 C C     . SER   A 1 246 ? 63.79012  -12.90305 17.59300  1.000 110.97058 ? 246 SER   A C     1 
ATOM   1785 O O     . SER   A 1 246 ? 63.51156  -13.91880 16.94300  1.000 111.92968 ? 246 SER   A O     1 
ATOM   1786 C CB    . SER   A 1 246 ? 66.03031  -13.23145 18.60825  1.000 102.68875 ? 246 SER   A CB    1 
ATOM   1787 O OG    . SER   A 1 246 ? 65.67775  -12.86241 19.93763  1.000 107.53489 ? 246 SER   A OG    1 
ATOM   1788 N N     . LEU   A 1 247 ? 62.88057  -12.23313 18.30075  1.000 110.59866 ? 247 LEU   A N     1 
ATOM   1789 C CA    . LEU   A 1 247 ? 61.51520  -12.69935 18.39136  1.000 103.43183 ? 247 LEU   A CA    1 
ATOM   1790 C C     . LEU   A 1 247 ? 60.76751  -12.40113 17.10082  1.000 99.39713  ? 247 LEU   A C     1 
ATOM   1791 O O     . LEU   A 1 247 ? 61.10022  -11.45470 16.38520  1.000 98.13662  ? 247 LEU   A O     1 
ATOM   1792 C CB    . LEU   A 1 247 ? 60.80585  -12.02406 19.54967  1.000 99.50293  ? 247 LEU   A CB    1 
ATOM   1793 C CG    . LEU   A 1 247 ? 61.34326  -12.53713 20.86536  1.000 102.57866 ? 247 LEU   A CG    1 
ATOM   1794 C CD1   . LEU   A 1 247 ? 60.64087  -11.83083 21.98743  1.000 103.65866 ? 247 LEU   A CD1   1 
ATOM   1795 C CD2   . LEU   A 1 247 ? 61.14542  -14.04132 20.92871  1.000 106.50634 ? 247 LEU   A CD2   1 
ATOM   1796 N N     . PRO   A 1 248 ? 59.75105  -13.19033 16.78510  1.000 97.09481  ? 248 PRO   A N     1 
ATOM   1797 C CA    . PRO   A 1 248 ? 58.89704  -12.86287 15.64048  1.000 99.02985  ? 248 PRO   A CA    1 
ATOM   1798 C C     . PRO   A 1 248 ? 57.97668  -11.69216 15.96351  1.000 101.41498 ? 248 PRO   A C     1 
ATOM   1799 O O     . PRO   A 1 248 ? 57.53834  -11.51530 17.10474  1.000 93.78329  ? 248 PRO   A O     1 
ATOM   1800 C CB    . PRO   A 1 248 ? 58.09598  -14.15184 15.41113  1.000 99.23746  ? 248 PRO   A CB    1 
ATOM   1801 C CG    . PRO   A 1 248 ? 58.79757  -15.21012 16.23893  1.000 103.00448 ? 248 PRO   A CG    1 
ATOM   1802 C CD    . PRO   A 1 248 ? 59.40616  -14.48359 17.38934  1.000 100.45623 ? 248 PRO   A CD    1 
ATOM   1803 N N     . GLN   A 1 249 ? 57.67854  -10.88734 14.93306  1.000 108.35810 ? 249 GLN   A N     1 
ATOM   1804 C CA    . GLN   A 1 249 ? 56.78222  -9.74546  15.11650  1.000 112.19866 ? 249 GLN   A CA    1 
ATOM   1805 C C     . GLN   A 1 249 ? 55.34148  -10.19159 15.36293  1.000 99.12866  ? 249 GLN   A C     1 
ATOM   1806 O O     . GLN   A 1 249 ? 54.66611  -9.65610  16.24590  1.000 94.16866  ? 249 GLN   A O     1 
ATOM   1807 C CB    . GLN   A 1 249 ? 56.85251  -8.80407  13.90686  1.000 124.34866 ? 249 GLN   A CB    1 
ATOM   1808 N N     . HIS   A 1 250 ? 54.85147  -11.16828 14.60526  1.000 98.84769  ? 250 HIS   A N     1 
ATOM   1809 C CA    . HIS   A 1 250 ? 53.48180  -11.64801 14.77986  1.000 101.50866 ? 250 HIS   A CA    1 
ATOM   1810 C C     . HIS   A 1 250 ? 53.41429  -12.73282 15.85132  1.000 94.72866  ? 250 HIS   A C     1 
ATOM   1811 O O     . HIS   A 1 250 ? 52.93679  -13.84748 15.62524  1.000 93.11870  ? 250 HIS   A O     1 
ATOM   1812 C CB    . HIS   A 1 250 ? 52.91879  -12.15831 13.45858  1.000 111.00866 ? 250 HIS   A CB    1 
ATOM   1813 C CG    . HIS   A 1 250 ? 52.90733  -11.13031 12.37405  1.000 109.25866 ? 250 HIS   A CG    1 
ATOM   1814 N ND1   . HIS   A 1 250 ? 52.37016  -11.37002 11.12666  1.000 108.13043 ? 250 HIS   A ND1   1 
ATOM   1815 C CD2   . HIS   A 1 250 ? 53.36936  -9.85555  12.34976  1.000 109.75866 ? 250 HIS   A CD2   1 
ATOM   1816 C CE1   . HIS   A 1 250 ? 52.49847  -10.28499 10.38120  1.000 110.54163 ? 250 HIS   A CE1   1 
ATOM   1817 N NE2   . HIS   A 1 250 ? 53.10603  -9.35352  11.09760  1.000 108.73674 ? 250 HIS   A NE2   1 
ATOM   1818 N N     . MET   A 1 251 ? 53.90262  -12.39090 17.03654  1.000 91.84629  ? 251 MET   A N     1 
ATOM   1819 C CA    . MET   A 1 251 ? 53.89053  -13.33412 18.14340  1.000 84.84113  ? 251 MET   A CA    1 
ATOM   1820 C C     . MET   A 1 251 ? 53.67163  -12.54968 19.42490  1.000 81.79372  ? 251 MET   A C     1 
ATOM   1821 O O     . MET   A 1 251 ? 54.47669  -11.67816 19.74974  1.000 81.77156  ? 251 MET   A O     1 
ATOM   1822 C CB    . MET   A 1 251 ? 55.20096  -14.12789 18.20582  1.000 86.04339  ? 251 MET   A CB    1 
ATOM   1823 C CG    . MET   A 1 251 ? 55.20784  -15.15533 19.31977  1.000 86.88311  ? 251 MET   A CG    1 
ATOM   1824 S SD    . MET   A 1 251 ? 56.80331  -15.41114 20.10810  1.000 90.24649  ? 251 MET   A SD    1 
ATOM   1825 C CE    . MET   A 1 251 ? 57.44528  -16.78009 19.14729  1.000 102.69293 ? 251 MET   A CE    1 
ATOM   1826 N N     . ALA   A 1 252 ? 52.58335  -12.83763 20.13666  1.000 80.30004  ? 252 ALA   A N     1 
ATOM   1827 C CA    . ALA   A 1 252 ? 52.33943  -12.18364 21.41530  1.000 79.43901  ? 252 ALA   A CA    1 
ATOM   1828 C C     . ALA   A 1 252 ? 53.20420  -12.82649 22.47370  1.000 74.57063  ? 252 ALA   A C     1 
ATOM   1829 O O     . ALA   A 1 252 ? 53.59337  -13.98611 22.35329  1.000 73.60494  ? 252 ALA   A O     1 
ATOM   1830 C CB    . ALA   A 1 252 ? 50.87278  -12.28262 21.81598  1.000 79.36934  ? 252 ALA   A CB    1 
ATOM   1831 N N     . TYR   A 1 253 ? 53.47853  -12.07766 23.53951  1.000 78.92683  ? 253 TYR   A N     1 
ATOM   1832 C CA    . TYR   A 1 253 ? 54.63110  -12.43842 24.37230  1.000 80.54141  ? 253 TYR   A CA    1 
ATOM   1833 C C     . TYR   A 1 253 ? 54.48171  -11.81217 25.76865  1.000 76.43636  ? 253 TYR   A C     1 
ATOM   1834 O O     . TYR   A 1 253 ? 55.01838  -10.73913 26.03802  1.000 75.72452  ? 253 TYR   A O     1 
ATOM   1835 C CB    . TYR   A 1 253 ? 55.89049  -11.98946 23.65292  1.000 75.77083  ? 253 TYR   A CB    1 
ATOM   1836 C CG    . TYR   A 1 253 ? 57.21555  -12.39836 24.23173  1.000 81.67495  ? 253 TYR   A CG    1 
ATOM   1837 C CD1   . TYR   A 1 253 ? 57.63399  -13.71936 24.21257  1.000 87.33239  ? 253 TYR   A CD1   1 
ATOM   1838 C CD2   . TYR   A 1 253 ? 58.08274  -11.45179 24.73658  1.000 86.53921  ? 253 TYR   A CD2   1 
ATOM   1839 C CE1   . TYR   A 1 253 ? 58.86831  -14.08261 24.72645  1.000 89.31501  ? 253 TYR   A CE1   1 
ATOM   1840 C CE2   . TYR   A 1 253 ? 59.31047  -11.80661 25.24382  1.000 86.82243  ? 253 TYR   A CE2   1 
ATOM   1841 C CZ    . TYR   A 1 253 ? 59.69629  -13.11422 25.23530  1.000 86.20854  ? 253 TYR   A CZ    1 
ATOM   1842 O OH    . TYR   A 1 253 ? 60.92733  -13.42361 25.74645  1.000 94.91461  ? 253 TYR   A OH    1 
ATOM   1843 N N     . ASP   A 1 254 ? 53.75449  -12.50051 26.63984  1.000 73.36359  ? 254 ASP   A N     1 
ATOM   1844 C CA    . ASP   A 1 254 ? 53.47362  -12.02990 27.99019  1.000 70.72222  ? 254 ASP   A CA    1 
ATOM   1845 C C     . ASP   A 1 254 ? 54.40294  -12.71106 28.98214  1.000 72.25197  ? 254 ASP   A C     1 
ATOM   1846 O O     . ASP   A 1 254 ? 55.11950  -13.65262 28.65743  1.000 71.00260  ? 254 ASP   A O     1 
ATOM   1847 C CB    . ASP   A 1 254 ? 52.01381  -12.31952 28.36859  1.000 78.13205  ? 254 ASP   A CB    1 
ATOM   1848 C CG    . ASP   A 1 254 ? 50.99518  -11.56826 27.48041  1.000 91.48214  ? 254 ASP   A CG    1 
ATOM   1849 O OD1   . ASP   A 1 254 ? 50.65267  -10.39993 27.80171  1.000 92.79866  ? 254 ASP   A OD1   1 
ATOM   1850 O OD2   . ASP   A 1 254 ? 50.52553  -12.14395 26.46181  1.000 85.62110  ? 254 ASP   A OD2   1 
ATOM   1851 N N     . LEU   A 1 255 ? 54.37246  -12.23045 30.21842  1.000 73.47571  ? 255 LEU   A N     1 
ATOM   1852 C CA    . LEU   A 1 255 ? 55.16070  -12.83874 31.28347  1.000 72.52481  ? 255 LEU   A CA    1 
ATOM   1853 C C     . LEU   A 1 255 ? 54.52009  -12.41537 32.59467  1.000 70.91471  ? 255 LEU   A C     1 
ATOM   1854 O O     . LEU   A 1 255 ? 54.60213  -11.24094 32.96262  1.000 73.83399  ? 255 LEU   A O     1 
ATOM   1855 C CB    . LEU   A 1 255 ? 56.63252  -12.41249 31.19439  1.000 76.03963  ? 255 LEU   A CB    1 
ATOM   1856 C CG    . LEU   A 1 255 ? 57.55805  -12.76531 32.37957  1.000 80.48457  ? 255 LEU   A CG    1 
ATOM   1857 C CD1   . LEU   A 1 255 ? 57.42235  -14.23709 32.79535  1.000 79.81954  ? 255 LEU   A CD1   1 
ATOM   1858 C CD2   . LEU   A 1 255 ? 59.00133  -12.46308 32.03427  1.000 72.68774  ? 255 LEU   A CD2   1 
ATOM   1859 N N     . VAL   A 1 256 ? 53.85342  -13.34366 33.27268  1.000 70.59458  ? 256 VAL   A N     1 
ATOM   1860 C CA    . VAL   A 1 256 ? 53.11720  -13.04127 34.50194  1.000 75.86575  ? 256 VAL   A CA    1 
ATOM   1861 C C     . VAL   A 1 256 ? 53.80672  -13.70445 35.68032  1.000 78.79319  ? 256 VAL   A C     1 
ATOM   1862 O O     . VAL   A 1 256 ? 54.08248  -14.90823 35.64847  1.000 85.44691  ? 256 VAL   A O     1 
ATOM   1863 C CB    . VAL   A 1 256 ? 51.64654  -13.49208 34.43099  1.000 78.58866  ? 256 VAL   A CB    1 
ATOM   1864 C CG1   . VAL   A 1 256 ? 50.89568  -13.03943 35.67907  1.000 74.78866  ? 256 VAL   A CG1   1 
ATOM   1865 C CG2   . VAL   A 1 256 ? 50.98671  -12.93574 33.18694  1.000 82.42866  ? 256 VAL   A CG2   1 
ATOM   1866 N N     . ALA   A 1 257 ? 54.04660  -12.93161 36.72838  1.000 79.84844  ? 257 ALA   A N     1 
ATOM   1867 C CA    . ALA   A 1 257 ? 54.69132  -13.42272 37.93893  1.000 82.39255  ? 257 ALA   A CA    1 
ATOM   1868 C C     . ALA   A 1 257 ? 53.70897  -13.31596 39.10246  1.000 85.19894  ? 257 ALA   A C     1 
ATOM   1869 O O     . ALA   A 1 257 ? 53.14970  -12.24373 39.36442  1.000 84.14290  ? 257 ALA   A O     1 
ATOM   1870 C CB    . ALA   A 1 257 ? 55.98173  -12.65373 38.23199  1.000 79.24717  ? 257 ALA   A CB    1 
ATOM   1871 N N     . THR   A 1 258 ? 53.49033  -14.43254 39.78127  1.000 89.67393  ? 258 THR   A N     1 
ATOM   1872 C CA    . THR   A 1 258 ? 52.60604  -14.49619 40.92095  1.000 91.23160  ? 258 THR   A CA    1 
ATOM   1873 C C     . THR   A 1 258 ? 53.46176  -14.54151 42.17254  1.000 94.89297  ? 258 THR   A C     1 
ATOM   1874 O O     . THR   A 1 258 ? 54.66573  -14.26070 42.12951  1.000 98.08866  ? 258 THR   A O     1 
ATOM   1875 C CB    . THR   A 1 258 ? 51.73470  -15.73797 40.82069  1.000 97.73681  ? 258 THR   A CB    1 
ATOM   1876 O OG1   . THR   A 1 258 ? 52.57598  -16.87973 41.01601  1.000 106.80866 ? 258 THR   A OG1   1 
ATOM   1877 C CG2   . THR   A 1 258 ? 51.14130  -15.84892 39.43138  1.000 105.63866 ? 258 THR   A CG2   1 
ATOM   1878 N N     . ALA   A 1 259 ? 52.86201  -14.94110 43.28861  1.000 96.66565  ? 259 ALA   A N     1 
ATOM   1879 C CA    . ALA   A 1 259 ? 53.67018  -15.24964 44.46068  1.000 95.36646  ? 259 ALA   A CA    1 
ATOM   1880 C C     . ALA   A 1 259 ? 54.74868  -16.28024 44.13039  1.000 94.33376  ? 259 ALA   A C     1 
ATOM   1881 O O     . ALA   A 1 259 ? 55.94528  -16.03654 44.32714  1.000 94.59336  ? 259 ALA   A O     1 
ATOM   1882 C CB    . ALA   A 1 259 ? 52.77105  -15.75091 45.58994  1.000 92.90832  ? 259 ALA   A CB    1 
ATOM   1883 N N     . ASN   A 1 260 ? 54.34218  -17.41210 43.55628  1.000 92.85507  ? 260 ASN   A N     1 
ATOM   1884 C CA    . ASN   A 1 260 ? 55.15129  -18.62056 43.52189  1.000 90.24194  ? 260 ASN   A CA    1 
ATOM   1885 C C     . ASN   A 1 260 ? 55.41930  -19.16440 42.12152  1.000 95.13576  ? 260 ASN   A C     1 
ATOM   1886 O O     . ASN   A 1 260 ? 55.83673  -20.32342 41.99754  1.000 99.81425  ? 260 ASN   A O     1 
ATOM   1887 C CB    . ASN   A 1 260 ? 54.44722  -19.68377 44.34491  1.000 89.46730  ? 260 ASN   A CB    1 
ATOM   1888 C CG    . ASN   A 1 260 ? 53.16749  -20.11572 43.69318  1.000 91.35514  ? 260 ASN   A CG    1 
ATOM   1889 O OD1   . ASN   A 1 260 ? 52.74217  -19.51240 42.71095  1.000 86.47387  ? 260 ASN   A OD1   1 
ATOM   1890 N ND2   . ASN   A 1 260 ? 52.51048  -21.12421 44.25717  1.000 98.72841  ? 260 ASN   A ND2   1 
ATOM   1891 N N     . SER   A 1 261 ? 55.18069  -18.39364 41.06238  1.000 96.10424  ? 261 SER   A N     1 
ATOM   1892 C CA    . SER   A 1 261 ? 55.43883  -18.92214 39.72539  1.000 93.87076  ? 261 SER   A CA    1 
ATOM   1893 C C     . SER   A 1 261 ? 55.76195  -17.79502 38.75360  1.000 90.93264  ? 261 SER   A C     1 
ATOM   1894 O O     . SER   A 1 261 ? 55.44871  -16.62309 38.98793  1.000 90.71669  ? 261 SER   A O     1 
ATOM   1895 C CB    . SER   A 1 261 ? 54.25773  -19.75314 39.20018  1.000 87.50711  ? 261 SER   A CB    1 
ATOM   1896 O OG    . SER   A 1 261 ? 53.02017  -19.07554 39.36939  1.000 88.77106  ? 261 SER   A OG    1 
ATOM   1897 N N     . MET   A 1 262 ? 56.41967  -18.18031 37.66332  1.000 85.66103  ? 262 MET   A N     1 
ATOM   1898 C CA    . MET   A 1 262 ? 56.69894  -17.32859 36.51620  1.000 87.22135  ? 262 MET   A CA    1 
ATOM   1899 C C     . MET   A 1 262 ? 56.07810  -17.98600 35.29044  1.000 94.44178  ? 262 MET   A C     1 
ATOM   1900 O O     . MET   A 1 262 ? 56.31483  -19.17544 35.04006  1.000 97.39325  ? 262 MET   A O     1 
ATOM   1901 C CB    . MET   A 1 262 ? 58.20222  -17.17410 36.30837  1.000 87.44682  ? 262 MET   A CB    1 
ATOM   1902 C CG    . MET   A 1 262 ? 58.94457  -16.63286 37.50067  1.000 97.13976  ? 262 MET   A CG    1 
ATOM   1903 S SD    . MET   A 1 262 ? 58.81159  -14.85305 37.66998  1.000 105.83493 ? 262 MET   A SD    1 
ATOM   1904 C CE    . MET   A 1 262 ? 59.91899  -14.40994 36.31482  1.000 91.91120  ? 262 MET   A CE    1 
ATOM   1905 N N     . ILE   A 1 263 ? 55.29486  -17.22838 34.51934  1.000 87.76292  ? 263 ILE   A N     1 
ATOM   1906 C CA    . ILE   A 1 263 ? 54.48232  -17.79085 33.44288  1.000 83.51093  ? 263 ILE   A CA    1 
ATOM   1907 C C     . ILE   A 1 263 ? 54.82163  -17.03329 32.16299  1.000 84.55437  ? 263 ILE   A C     1 
ATOM   1908 O O     . ILE   A 1 263 ? 54.15679  -16.05267 31.81839  1.000 84.41874  ? 263 ILE   A O     1 
ATOM   1909 C CB    . ILE   A 1 263 ? 52.98717  -17.70649 33.74147  1.000 78.42317  ? 263 ILE   A CB    1 
ATOM   1910 C CG1   . ILE   A 1 263 ? 52.73209  -18.05155 35.19744  1.000 75.11839  ? 263 ILE   A CG1   1 
ATOM   1911 C CG2   . ILE   A 1 263 ? 52.24269  -18.67395 32.85882  1.000 79.17165  ? 263 ILE   A CG2   1 
ATOM   1912 C CD1   . ILE   A 1 263 ? 51.29578  -17.91522 35.58624  1.000 82.81664  ? 263 ILE   A CD1   1 
ATOM   1913 N N     . LEU   A 1 264 ? 55.85177  -17.48565 31.44498  1.000 84.93529  ? 264 LEU   A N     1 
ATOM   1914 C CA    . LEU   A 1 264 ? 56.02605  -17.05272 30.06553  1.000 80.09514  ? 264 LEU   A CA    1 
ATOM   1915 C C     . LEU   A 1 264 ? 54.89223  -17.63216 29.21863  1.000 84.04128  ? 264 LEU   A C     1 
ATOM   1916 O O     . LEU   A 1 264 ? 54.71736  -18.85176 29.15363  1.000 83.80006  ? 264 LEU   A O     1 
ATOM   1917 C CB    . LEU   A 1 264 ? 57.37820  -17.48562 29.50531  1.000 78.29738  ? 264 LEU   A CB    1 
ATOM   1918 C CG    . LEU   A 1 264 ? 57.45925  -17.25334 27.97969  1.000 80.36657  ? 264 LEU   A CG    1 
ATOM   1919 C CD1   . LEU   A 1 264 ? 57.05867  -15.85175 27.64566  1.000 80.56442  ? 264 LEU   A CD1   1 
ATOM   1920 C CD2   . LEU   A 1 264 ? 58.82620  -17.52897 27.38375  1.000 84.05104  ? 264 LEU   A CD2   1 
ATOM   1921 N N     . GLY   A 1 265 ? 54.10917  -16.75402 28.58206  1.000 84.86815  ? 265 GLY   A N     1 
ATOM   1922 C CA    . GLY   A 1 265 ? 53.00648  -17.16712 27.74052  1.000 82.42669  ? 265 GLY   A CA    1 
ATOM   1923 C C     . GLY   A 1 265 ? 52.81460  -16.20062 26.58613  1.000 81.77751  ? 265 GLY   A C     1 
ATOM   1924 O O     . GLY   A 1 265 ? 53.47780  -15.16573 26.49974  1.000 81.33062  ? 265 GLY   A O     1 
ATOM   1925 N N     . GLY   A 1 266 ? 51.89260  -16.55375 25.70381  1.000 79.09343  ? 266 GLY   A N     1 
ATOM   1926 C CA    . GLY   A 1 266 ? 51.69847  -15.78905 24.49226  1.000 79.13022  ? 266 GLY   A CA    1 
ATOM   1927 C C     . GLY   A 1 266 ? 51.07027  -16.64682 23.40923  1.000 80.79859  ? 266 GLY   A C     1 
ATOM   1928 O O     . GLY   A 1 266 ? 50.66036  -17.78610 23.64101  1.000 77.65153  ? 266 GLY   A O     1 
ATOM   1929 N N     . ALA   A 1 267 ? 50.99703  -16.05517 22.21778  1.000 76.82212  ? 267 ALA   A N     1 
ATOM   1930 C CA    . ALA   A 1 267 ? 50.36828  -16.67526 21.06675  1.000 67.04151  ? 267 ALA   A CA    1 
ATOM   1931 C C     . ALA   A 1 267 ? 51.22682  -16.38790 19.85200  1.000 71.78141  ? 267 ALA   A C     1 
ATOM   1932 O O     . ALA   A 1 267 ? 51.70220  -15.26644 19.68423  1.000 77.56847  ? 267 ALA   A O     1 
ATOM   1933 C CB    . ALA   A 1 267 ? 48.94905  -16.13932 20.86802  1.000 61.51028  ? 267 ALA   A CB    1 
ATOM   1934 N N     . TYR   A 1 268 ? 51.45037  -17.40673 19.02536  1.000 70.56459  ? 268 TYR   A N     1 
ATOM   1935 C CA    . TYR   A 1 268 ? 52.12477  -17.25754 17.73851  1.000 77.05780  ? 268 TYR   A CA    1 
ATOM   1936 C C     . TYR   A 1 268 ? 51.14459  -17.56442 16.60281  1.000 78.51976  ? 268 TYR   A C     1 
ATOM   1937 O O     . TYR   A 1 268 ? 50.38686  -18.53665 16.67188  1.000 77.09085  ? 268 TYR   A O     1 
ATOM   1938 C CB    . TYR   A 1 268 ? 53.35284  -18.17305 17.67763  1.000 83.46487  ? 268 TYR   A CB    1 
ATOM   1939 C CG    . TYR   A 1 268 ? 53.99206  -18.28088 16.30974  1.000 87.29406  ? 268 TYR   A CG    1 
ATOM   1940 C CD1   . TYR   A 1 268 ? 53.46357  -19.14864 15.34886  1.000 88.18762  ? 268 TYR   A CD1   1 
ATOM   1941 C CD2   . TYR   A 1 268 ? 55.14719  -17.57531 15.99674  1.000 83.44556  ? 268 TYR   A CD2   1 
ATOM   1942 C CE1   . TYR   A 1 268 ? 54.02929  -19.27356 14.10946  1.000 87.28007  ? 268 TYR   A CE1   1 
ATOM   1943 C CE2   . TYR   A 1 268 ? 55.73158  -17.70389 14.75726  1.000 87.07320  ? 268 TYR   A CE2   1 
ATOM   1944 C CZ    . TYR   A 1 268 ? 55.16355  -18.55748 13.81694  1.000 87.77762  ? 268 TYR   A CZ    1 
ATOM   1945 O OH    . TYR   A 1 268 ? 55.71143  -18.70684 12.56836  1.000 86.50854  ? 268 TYR   A OH    1 
ATOM   1946 N N     . PHE   A 1 269 ? 51.15540  -16.73975 15.55480  1.000 82.76354  ? 269 PHE   A N     1 
ATOM   1947 C CA    . PHE   A 1 269 ? 50.24125  -16.90130 14.42371  1.000 84.91714  ? 269 PHE   A CA    1 
ATOM   1948 C C     . PHE   A 1 269 ? 51.04233  -17.43486 13.24377  1.000 90.31705  ? 269 PHE   A C     1 
ATOM   1949 O O     . PHE   A 1 269 ? 51.91222  -16.74009 12.69777  1.000 91.90499  ? 269 PHE   A O     1 
ATOM   1950 C CB    . PHE   A 1 269 ? 49.51261  -15.59208 14.10420  1.000 83.96186  ? 269 PHE   A CB    1 
ATOM   1951 C CG    . PHE   A 1 269 ? 48.77431  -15.02471 15.29117  1.000 81.25875  ? 269 PHE   A CG    1 
ATOM   1952 C CD1   . PHE   A 1 269 ? 47.54584  -15.53991 15.67519  1.000 78.20030  ? 269 PHE   A CD1   1 
ATOM   1953 C CD2   . PHE   A 1 269 ? 49.35863  -14.05154 16.08861  1.000 80.13185  ? 269 PHE   A CD2   1 
ATOM   1954 C CE1   . PHE   A 1 269 ? 46.88611  -15.04177 16.79580  1.000 70.82782  ? 269 PHE   A CE1   1 
ATOM   1955 C CE2   . PHE   A 1 269 ? 48.70431  -13.56897 17.21187  1.000 67.07286  ? 269 PHE   A CE2   1 
ATOM   1956 C CZ    . PHE   A 1 269 ? 47.46921  -14.06416 17.55579  1.000 59.04061  ? 269 PHE   A CZ    1 
ATOM   1957 N N     . GLY   A 1 270 ? 50.73446  -18.67365 12.86609  1.000 89.71777  ? 270 GLY   A N     1 
ATOM   1958 C CA    . GLY   A 1 270 ? 51.59018  -19.52389 12.07228  1.000 89.60725  ? 270 GLY   A CA    1 
ATOM   1959 C C     . GLY   A 1 270 ? 51.48665  -20.93352 12.61422  1.000 94.44235  ? 270 GLY   A C     1 
ATOM   1960 O O     . GLY   A 1 270 ? 50.85002  -21.14675 13.65033  1.000 92.49827  ? 270 GLY   A O     1 
ATOM   1961 N N     . SER   A 1 271 ? 52.10901  -21.90046 11.94348  1.000 103.31113 ? 271 SER   A N     1 
ATOM   1962 C CA    . SER   A 1 271 ? 51.91119  -23.30334 12.29660  1.000 103.49931 ? 271 SER   A CA    1 
ATOM   1963 C C     . SER   A 1 271 ? 52.61934  -23.64882 13.60495  1.000 101.59190 ? 271 SER   A C     1 
ATOM   1964 O O     . SER   A 1 271 ? 53.71780  -23.15321 13.88750  1.000 97.91552  ? 271 SER   A O     1 
ATOM   1965 C CB    . SER   A 1 271 ? 52.41903  -24.20122 11.17067  1.000 102.29160 ? 271 SER   A CB    1 
ATOM   1966 O OG    . SER   A 1 271 ? 53.76393  -23.88060 10.85310  1.000 103.09358 ? 271 SER   A OG    1 
ATOM   1967 N N     . GLN   A 1 272 ? 51.96648  -24.50209 14.41249  1.000 97.36435  ? 272 GLN   A N     1 
ATOM   1968 C CA    . GLN   A 1 272 ? 52.58721  -25.03026 15.62590  1.000 94.24430  ? 272 GLN   A CA    1 
ATOM   1969 C C     . GLN   A 1 272 ? 53.99384  -25.54729 15.39329  1.000 102.30124 ? 272 GLN   A C     1 
ATOM   1970 O O     . GLN   A 1 272 ? 54.82707  -25.52636 16.31103  1.000 98.52479  ? 272 GLN   A O     1 
ATOM   1971 C CB    . GLN   A 1 272 ? 51.74841  -26.15455 16.20446  1.000 91.16314  ? 272 GLN   A CB    1 
ATOM   1972 C CG    . GLN   A 1 272 ? 52.43915  -26.78985 17.37737  1.000 90.02431  ? 272 GLN   A CG    1 
ATOM   1973 C CD    . GLN   A 1 272 ? 51.54334  -27.74106 18.11816  1.000 94.71728  ? 272 GLN   A CD    1 
ATOM   1974 O OE1   . GLN   A 1 272 ? 50.72856  -27.32597 18.94275  1.000 90.05419  ? 272 GLN   A OE1   1 
ATOM   1975 N NE2   . GLN   A 1 272 ? 51.65067  -29.02843 17.79485  1.000 98.97885  ? 272 GLN   A NE2   1 
ATOM   1976 N N     . GLU   A 1 273 ? 54.25946  -26.06251 14.19077  1.000 107.16341 ? 273 GLU   A N     1 
ATOM   1977 C CA    . GLU   A 1 273 ? 55.61015  -26.45081 13.81209  1.000 101.76495 ? 273 GLU   A CA    1 
ATOM   1978 C C     . GLU   A 1 273 ? 56.57813  -25.30388 14.05470  1.000 103.50774 ? 273 GLU   A C     1 
ATOM   1979 O O     . GLU   A 1 273 ? 57.47235  -25.37550 14.91222  1.000 98.76307  ? 273 GLU   A O     1 
ATOM   1980 C CB    . GLU   A 1 273 ? 55.61777  -26.87381 12.33952  1.000 95.33685  ? 273 GLU   A CB    1 
ATOM   1981 C CG    . GLU   A 1 273 ? 55.20949  -28.31863 12.14642  1.000 106.42395 ? 273 GLU   A CG    1 
ATOM   1982 C CD    . GLU   A 1 273 ? 54.04122  -28.71857 13.06313  1.000 123.51770 ? 273 GLU   A CD    1 
ATOM   1983 O OE1   . GLU   A 1 273 ? 52.96715  -28.08062 12.96933  1.000 131.41866 ? 273 GLU   A OE1   1 
ATOM   1984 O OE2   . GLU   A 1 273 ? 54.19642  -29.65146 13.89433  1.000 119.99945 ? 273 GLU   A OE2   1 
ATOM   1985 N N     . ASP   A 1 274 ? 56.36486  -24.20522 13.32863  1.000 100.52553 ? 274 ASP   A N     1 
ATOM   1986 C CA    . ASP   A 1 274 ? 57.33185  -23.11953 13.33378  1.000 99.30012  ? 274 ASP   A CA    1 
ATOM   1987 C C     . ASP   A 1 274 ? 57.51638  -22.54067 14.73216  1.000 97.71018  ? 274 ASP   A C     1 
ATOM   1988 O O     . ASP   A 1 274 ? 58.61534  -22.09144 15.08300  1.000 100.30211 ? 274 ASP   A O     1 
ATOM   1989 C CB    . ASP   A 1 274 ? 56.89511  -22.03284 12.35284  1.000 97.25613  ? 274 ASP   A CB    1 
ATOM   1990 C CG    . ASP   A 1 274 ? 56.75977  -22.54123 10.92737  1.000 97.83679  ? 274 ASP   A CG    1 
ATOM   1991 O OD1   . ASP   A 1 274 ? 56.51989  -23.75583 10.72988  1.000 104.38541 ? 274 ASP   A OD1   1 
ATOM   1992 O OD2   . ASP   A 1 274 ? 56.94072  -21.73133 9.99768   1.000 99.92209  ? 274 ASP   A OD2   1 
ATOM   1993 N N     . PHE   A 1 275 ? 56.46398  -22.52217 15.54317  1.000 88.70258  ? 275 PHE   A N     1 
ATOM   1994 C CA    . PHE   A 1 275 ? 56.65800  -22.02690 16.89270  1.000 93.32170  ? 275 PHE   A CA    1 
ATOM   1995 C C     . PHE   A 1 275 ? 57.69746  -22.86528 17.61398  1.000 100.59287 ? 275 PHE   A C     1 
ATOM   1996 O O     . PHE   A 1 275 ? 58.71166  -22.35206 18.10847  1.000 100.56101 ? 275 PHE   A O     1 
ATOM   1997 C CB    . PHE   A 1 275 ? 55.35322  -22.03423 17.67249  1.000 90.33758  ? 275 PHE   A CB    1 
ATOM   1998 C CG    . PHE   A 1 275 ? 55.53186  -21.62676 19.09684  1.000 85.37917  ? 275 PHE   A CG    1 
ATOM   1999 C CD1   . PHE   A 1 275 ? 55.72483  -20.29707 19.42935  1.000 84.99894  ? 275 PHE   A CD1   1 
ATOM   2000 C CD2   . PHE   A 1 275 ? 55.55673  -22.58019 20.10705  1.000 87.70223  ? 275 PHE   A CD2   1 
ATOM   2001 C CE1   . PHE   A 1 275 ? 55.90759  -19.91954 20.75449  1.000 91.84684  ? 275 PHE   A CE1   1 
ATOM   2002 C CE2   . PHE   A 1 275 ? 55.73929  -22.21706 21.43486  1.000 87.54750  ? 275 PHE   A CE2   1 
ATOM   2003 C CZ    . PHE   A 1 275 ? 55.91458  -20.89097 21.76084  1.000 90.18200  ? 275 PHE   A CZ    1 
ATOM   2004 N N     . GLU   A 1 276 ? 57.44233  -24.17409 17.69522  1.000 102.06608 ? 276 GLU   A N     1 
ATOM   2005 C CA    . GLU   A 1 276 ? 58.35388  -25.06562 18.39749  1.000 101.50972 ? 276 GLU   A CA    1 
ATOM   2006 C C     . GLU   A 1 276 ? 59.74400  -24.99041 17.78467  1.000 103.15802 ? 276 GLU   A C     1 
ATOM   2007 O O     . GLU   A 1 276 ? 60.75332  -25.00473 18.50562  1.000 101.43294 ? 276 GLU   A O     1 
ATOM   2008 C CB    . GLU   A 1 276 ? 57.79055  -26.48626 18.36754  1.000 99.40287  ? 276 GLU   A CB    1 
ATOM   2009 C CG    . GLU   A 1 276 ? 56.79125  -26.73526 19.49061  1.000 99.43974  ? 276 GLU   A CG    1 
ATOM   2010 C CD    . GLU   A 1 276 ? 55.74954  -27.77320 19.12060  1.000 103.44768 ? 276 GLU   A CD    1 
ATOM   2011 O OE1   . GLU   A 1 276 ? 55.81742  -28.29712 17.98443  1.000 99.56692  ? 276 GLU   A OE1   1 
ATOM   2012 O OE2   . GLU   A 1 276 ? 54.87065  -28.06323 19.96783  1.000 102.47216 ? 276 GLU   A OE2   1 
ATOM   2013 N N     . ALA   A 1 277 ? 59.80547  -24.84891 16.45168  1.000 102.32978 ? 277 ALA   A N     1 
ATOM   2014 C CA    . ALA   A 1 277 ? 61.07151  -24.65260 15.74964  1.000 101.73887 ? 277 ALA   A CA    1 
ATOM   2015 C C     . ALA   A 1 277 ? 61.81036  -23.39834 16.21519  1.000 104.65544 ? 277 ALA   A C     1 
ATOM   2016 O O     . ALA   A 1 277 ? 63.03658  -23.31808 16.06413  1.000 100.89631 ? 277 ALA   A O     1 
ATOM   2017 C CB    . ALA   A 1 277 ? 60.82843  -24.60536 14.23699  1.000 92.23037  ? 277 ALA   A CB    1 
ATOM   2018 N N     . PHE   A 1 278 ? 61.10717  -22.42396 16.79528  1.000 105.41951 ? 278 PHE   A N     1 
ATOM   2019 C CA    . PHE   A 1 278 ? 61.82103  -21.35500 17.47566  1.000 110.16695 ? 278 PHE   A CA    1 
ATOM   2020 C C     . PHE   A 1 278 ? 62.39705  -21.81595 18.81011  1.000 113.78798 ? 278 PHE   A C     1 
ATOM   2021 O O     . PHE   A 1 278 ? 63.26740  -21.13215 19.36449  1.000 113.46904 ? 278 PHE   A O     1 
ATOM   2022 C CB    . PHE   A 1 278 ? 60.88795  -20.16315 17.66499  1.000 108.76496 ? 278 PHE   A CB    1 
ATOM   2023 C CG    . PHE   A 1 278 ? 61.60803  -18.87355 17.91061  1.000 119.32498 ? 278 PHE   A CG    1 
ATOM   2024 C CD1   . PHE   A 1 278 ? 62.22582  -18.20611 16.85893  1.000 122.43924 ? 278 PHE   A CD1   1 
ATOM   2025 C CD2   . PHE   A 1 278 ? 61.64616  -18.30581 19.17853  1.000 118.39105 ? 278 PHE   A CD2   1 
ATOM   2026 C CE1   . PHE   A 1 278 ? 62.88775  -17.00036 17.06133  1.000 119.40184 ? 278 PHE   A CE1   1 
ATOM   2027 C CE2   . PHE   A 1 278 ? 62.30662  -17.09482 19.39132  1.000 118.90866 ? 278 PHE   A CE2   1 
ATOM   2028 C CZ    . PHE   A 1 278 ? 62.92737  -16.44177 18.32844  1.000 120.82866 ? 278 PHE   A CZ    1 
ATOM   2029 N N     . ASN   A 1 279 ? 61.94044  -22.96679 19.31445  1.000 111.66482 ? 279 ASN   A N     1 
ATOM   2030 C CA    . ASN   A 1 279 ? 62.42505  -23.57924 20.54955  1.000 112.39312 ? 279 ASN   A CA    1 
ATOM   2031 C C     . ASN   A 1 279 ? 62.48575  -22.52384 21.65096  1.000 112.67557 ? 279 ASN   A C     1 
ATOM   2032 O O     . ASN   A 1 279 ? 63.45850  -22.39592 22.39467  1.000 111.12995 ? 279 ASN   A O     1 
ATOM   2033 C CB    . ASN   A 1 279 ? 63.76679  -24.29281 20.31509  1.000 119.04133 ? 279 ASN   A CB    1 
ATOM   2034 C CG    . ASN   A 1 279 ? 64.06802  -25.34120 21.37618  1.000 130.22924 ? 279 ASN   A CG    1 
ATOM   2035 O OD1   . ASN   A 1 279 ? 63.36885  -25.41397 22.38635  1.000 130.28547 ? 279 ASN   A OD1   1 
ATOM   2036 N ND2   . ASN   A 1 279 ? 65.05959  -26.20631 21.11976  1.000 135.46114 ? 279 ASN   A ND2   1 
ATOM   2037 N N     . LEU   A 1 280 ? 61.38794  -21.76569 21.73900  1.000 112.43781 ? 280 LEU   A N     1 
ATOM   2038 C CA    . LEU   A 1 280 ? 61.37941  -20.54003 22.52725  1.000 115.06559 ? 280 LEU   A CA    1 
ATOM   2039 C C     . LEU   A 1 280 ? 61.98626  -20.74600 23.91031  1.000 113.63730 ? 280 LEU   A C     1 
ATOM   2040 O O     . LEU   A 1 280 ? 62.73576  -19.89284 24.40098  1.000 114.73908 ? 280 LEU   A O     1 
ATOM   2041 C CB    . LEU   A 1 280 ? 59.95191  -20.01438 22.62642  1.000 121.05866 ? 280 LEU   A CB    1 
ATOM   2042 C CG    . LEU   A 1 280 ? 59.83471  -18.67677 23.34829  1.000 125.66866 ? 280 LEU   A CG    1 
ATOM   2043 C CD1   . LEU   A 1 280 ? 60.66497  -17.58103 22.66274  1.000 120.70866 ? 280 LEU   A CD1   1 
ATOM   2044 C CD2   . LEU   A 1 280 ? 58.37458  -18.31238 23.42678  1.000 125.43866 ? 280 LEU   A CD2   1 
ATOM   2045 N N     . SER   A 1 281 ? 61.70045  -21.88501 24.54647  1.000 111.15047 ? 281 SER   A N     1 
ATOM   2046 C CA    . SER   A 1 281 ? 62.20355  -22.10123 25.89978  1.000 107.41103 ? 281 SER   A CA    1 
ATOM   2047 C C     . SER   A 1 281 ? 63.69715  -22.41038 25.93008  1.000 105.77481 ? 281 SER   A C     1 
ATOM   2048 O O     . SER   A 1 281 ? 64.32582  -22.27713 26.98733  1.000 104.17404 ? 281 SER   A O     1 
ATOM   2049 C CB    . SER   A 1 281 ? 61.39317  -23.21116 26.58254  1.000 102.42622 ? 281 SER   A CB    1 
ATOM   2050 O OG    . SER   A 1 281 ? 61.07012  -24.23367 25.65561  1.000 108.84474 ? 281 SER   A OG    1 
ATOM   2051 N N     . SER   A 1 282 ? 64.29757  -22.78636 24.79775  1.000 108.03526 ? 282 SER   A N     1 
ATOM   2052 C CA    . SER   A 1 282 ? 65.74156  -23.00141 24.78648  1.000 110.65733 ? 282 SER   A CA    1 
ATOM   2053 C C     . SER   A 1 282 ? 66.47452  -21.78947 25.35049  1.000 110.04549 ? 282 SER   A C     1 
ATOM   2054 O O     . SER   A 1 282 ? 67.21518  -21.90059 26.33268  1.000 109.79337 ? 282 SER   A O     1 
ATOM   2055 C CB    . SER   A 1 282 ? 66.22589  -23.29578 23.36722  1.000 109.09457 ? 282 SER   A CB    1 
ATOM   2056 O OG    . SER   A 1 282 ? 66.46903  -22.08890 22.67495  1.000 101.23451 ? 282 SER   A OG    1 
ATOM   2057 N N     . HIS   A 1 283 ? 66.24626  -20.61483 24.76022  1.000 112.08916 ? 283 HIS   A N     1 
ATOM   2058 C CA    . HIS   A 1 283 ? 66.92290  -19.37044 25.12465  1.000 110.24811 ? 283 HIS   A CA    1 
ATOM   2059 C C     . HIS   A 1 283 ? 67.00365  -19.10383 26.62643  1.000 106.63489 ? 283 HIS   A C     1 
ATOM   2060 O O     . HIS   A 1 283 ? 67.72061  -18.18755 27.03477  1.000 101.96549 ? 283 HIS   A O     1 
ATOM   2061 C CB    . HIS   A 1 283 ? 66.21744  -18.18373 24.47801  1.000 101.68405 ? 283 HIS   A CB    1 
ATOM   2062 C CG    . HIS   A 1 283 ? 66.05444  -18.31339 23.00068  1.000 103.64127 ? 283 HIS   A CG    1 
ATOM   2063 N ND1   . HIS   A 1 283 ? 66.99809  -17.86063 22.10445  1.000 104.52711 ? 283 HIS   A ND1   1 
ATOM   2064 C CD2   . HIS   A 1 283 ? 65.03976  -18.81688 22.25785  1.000 106.25722 ? 283 HIS   A CD2   1 
ATOM   2065 C CE1   . HIS   A 1 283 ? 66.57924  -18.09417 20.87195  1.000 103.97610 ? 283 HIS   A CE1   1 
ATOM   2066 N NE2   . HIS   A 1 283 ? 65.39224  -18.67185 20.93676  1.000 105.38763 ? 283 HIS   A NE2   1 
ATOM   2067 N N     . PHE   A 1 284 ? 66.25648  -19.85941 27.44398  1.000 105.79423 ? 284 PHE   A N     1 
ATOM   2068 C CA    . PHE   A 1 284 ? 66.24856  -19.68365 28.89631  1.000 110.72119 ? 284 PHE   A CA    1 
ATOM   2069 C C     . PHE   A 1 284 ? 67.23738  -20.62112 29.57374  1.000 117.04621 ? 284 PHE   A C     1 
ATOM   2070 O O     . PHE   A 1 284 ? 67.40501  -21.77320 29.15440  1.000 111.33088 ? 284 PHE   A O     1 
ATOM   2071 C CB    . PHE   A 1 284 ? 64.86042  -19.93764 29.48361  1.000 110.34799 ? 284 PHE   A CB    1 
ATOM   2072 C CG    . PHE   A 1 284 ? 63.88672  -18.84250 29.22019  1.000 109.90937 ? 284 PHE   A CG    1 
ATOM   2073 C CD1   . PHE   A 1 284 ? 63.46010  -18.57751 27.92761  1.000 105.32896 ? 284 PHE   A CD1   1 
ATOM   2074 C CD2   . PHE   A 1 284 ? 63.41189  -18.05769 30.26492  1.000 108.47635 ? 284 PHE   A CD2   1 
ATOM   2075 C CE1   . PHE   A 1 284 ? 62.56795  -17.56825 27.68081  1.000 103.09866 ? 284 PHE   A CE1   1 
ATOM   2076 C CE2   . PHE   A 1 284 ? 62.51700  -17.03997 30.02862  1.000 105.84866 ? 284 PHE   A CE2   1 
ATOM   2077 C CZ    . PHE   A 1 284 ? 62.09324  -16.79190 28.73366  1.000 108.40866 ? 284 PHE   A CZ    1 
ATOM   2078 N N     . LYS   A 1 285 ? 67.85309  -20.12407 30.65680  1.000 119.79968 ? 285 LYS   A N     1 
ATOM   2079 C CA    . LYS   A 1 285 ? 68.93515  -20.84972 31.32124  1.000 120.12412 ? 285 LYS   A CA    1 
ATOM   2080 C C     . LYS   A 1 285 ? 68.42408  -22.14215 31.93641  1.000 116.10336 ? 285 LYS   A C     1 
ATOM   2081 O O     . LYS   A 1 285 ? 68.87402  -23.23639 31.58713  1.000 123.29866 ? 285 LYS   A O     1 
ATOM   2082 C CB    . LYS   A 1 285 ? 69.58751  -19.97008 32.39116  1.000 117.04761 ? 285 LYS   A CB    1 
ATOM   2083 N N     . VAL   A 1 286 ? 67.49568  -22.03647 32.84093  1.000 109.38010 ? 286 VAL   A N     1 
ATOM   2084 C CA    . VAL   A 1 286 ? 66.83921  -23.20406 33.40660  1.000 104.94279 ? 286 VAL   A CA    1 
ATOM   2085 C C     . VAL   A 1 286 ? 65.66552  -23.57561 32.51631  1.000 110.07454 ? 286 VAL   A C     1 
ATOM   2086 O O     . VAL   A 1 286 ? 65.04293  -22.70267 31.89603  1.000 113.49794 ? 286 VAL   A O     1 
ATOM   2087 C CB    . VAL   A 1 286 ? 66.37632  -22.91290 34.83882  1.000 102.15847 ? 286 VAL   A CB    1 
ATOM   2088 C CG1   . VAL   A 1 286 ? 65.62422  -24.10102 35.39811  1.000 105.53174 ? 286 VAL   A CG1   1 
ATOM   2089 C CG2   . VAL   A 1 286 ? 67.56797  -22.51933 35.68587  1.000 109.08995 ? 286 VAL   A CG2   1 
ATOM   2090 N N     . ALA   A 1 287 ? 65.35299  -24.87383 32.44371  1.000 107.87822 ? 287 ALA   A N     1 
ATOM   2091 C CA    . ALA   A 1 287 ? 64.17852  -25.24641 31.67047  1.000 106.99186 ? 287 ALA   A CA    1 
ATOM   2092 C C     . ALA   A 1 287 ? 62.91884  -25.09346 32.51811  1.000 103.80593 ? 287 ALA   A C     1 
ATOM   2093 O O     . ALA   A 1 287 ? 62.97106  -25.16851 33.74897  1.000 103.42815 ? 287 ALA   A O     1 
ATOM   2094 C CB    . ALA   A 1 287 ? 64.28573  -26.67960 31.16195  1.000 106.69852 ? 287 ALA   A CB    1 
ATOM   2095 N N     . PRO   A 1 288 ? 61.78010  -24.86214 31.88145  1.000 103.32800 ? 288 PRO   A N     1 
ATOM   2096 C CA    . PRO   A 1 288 ? 60.53341  -24.70073 32.63237  1.000 101.09961 ? 288 PRO   A CA    1 
ATOM   2097 C C     . PRO   A 1 288 ? 59.96107  -26.03737 33.10298  1.000 100.13537 ? 288 PRO   A C     1 
ATOM   2098 O O     . PRO   A 1 288 ? 60.22528  -27.10057 32.53459  1.000 99.14349  ? 288 PRO   A O     1 
ATOM   2099 C CB    . PRO   A 1 288 ? 59.60971  -24.01119 31.62063  1.000 94.61866  ? 288 PRO   A CB    1 
ATOM   2100 C CG    . PRO   A 1 288 ? 60.12446  -24.46758 30.27309  1.000 97.05280  ? 288 PRO   A CG    1 
ATOM   2101 C CD    . PRO   A 1 288 ? 61.60409  -24.68139 30.42617  1.000 100.57476 ? 288 PRO   A CD    1 
ATOM   2102 N N     . ASP   A 1 289 ? 59.18510  -25.95782 34.18725  1.000 95.43689  ? 289 ASP   A N     1 
ATOM   2103 C CA    . ASP   A 1 289 ? 58.49380  -27.12455 34.73626  1.000 92.56143  ? 289 ASP   A CA    1 
ATOM   2104 C C     . ASP   A 1 289 ? 57.44683  -27.66680 33.78030  1.000 98.12246  ? 289 ASP   A C     1 
ATOM   2105 O O     . ASP   A 1 289 ? 57.45248  -28.85205 33.42012  1.000 97.61393  ? 289 ASP   A O     1 
ATOM   2106 C CB    . ASP   A 1 289 ? 57.80747  -26.77048 36.04639  1.000 90.46195  ? 289 ASP   A CB    1 
ATOM   2107 C CG    . ASP   A 1 289 ? 58.73683  -26.15821 37.03024  1.000 98.79493  ? 289 ASP   A CG    1 
ATOM   2108 O OD1   . ASP   A 1 289 ? 59.93717  -25.98739 36.67990  1.000 101.18363 ? 289 ASP   A OD1   1 
ATOM   2109 O OD2   . ASP   A 1 289 ? 58.26098  -25.83971 38.14559  1.000 92.84682  ? 289 ASP   A OD2   1 
ATOM   2110 N N     . VAL   A 1 290 ? 56.50306  -26.81752 33.39755  1.000 100.43223 ? 290 VAL   A N     1 
ATOM   2111 C CA    . VAL   A 1 290 ? 55.32226  -27.26104 32.68116  1.000 93.94849  ? 290 VAL   A CA    1 
ATOM   2112 C C     . VAL   A 1 290 ? 55.29754  -26.57649 31.32045  1.000 88.56041  ? 290 VAL   A C     1 
ATOM   2113 O O     . VAL   A 1 290 ? 55.87452  -25.50031 31.13045  1.000 89.43831  ? 290 VAL   A O     1 
ATOM   2114 C CB    . VAL   A 1 290 ? 54.05939  -26.94909 33.50448  1.000 86.63571  ? 290 VAL   A CB    1 
ATOM   2115 C CG1   . VAL   A 1 290 ? 52.84542  -27.54945 32.84655  1.000 90.91704  ? 290 VAL   A CG1   1 
ATOM   2116 C CG2   . VAL   A 1 290 ? 54.22962  -27.43299 34.92796  1.000 89.18293  ? 290 VAL   A CG2   1 
ATOM   2117 N N     . THR   A 1 291 ? 54.63522  -27.22846 30.36860  1.000 86.65214  ? 291 THR   A N     1 
ATOM   2118 C CA    . THR   A 1 291 ? 54.62973  -26.84061 28.95511  1.000 89.98237  ? 291 THR   A CA    1 
ATOM   2119 C C     . THR   A 1 291 ? 53.24606  -27.13579 28.37540  1.000 96.54212  ? 291 THR   A C     1 
ATOM   2120 O O     . THR   A 1 291 ? 52.92164  -28.28578 28.03984  1.000 97.08486  ? 291 THR   A O     1 
ATOM   2121 C CB    . THR   A 1 291 ? 55.72442  -27.56256 28.14563  1.000 101.42640 ? 291 THR   A CB    1 
ATOM   2122 O OG1   . THR   A 1 291 ? 55.80671  -26.99758 26.82383  1.000 103.11816 ? 291 THR   A OG1   1 
ATOM   2123 C CG2   . THR   A 1 291 ? 55.48976  -29.13158 28.03652  1.000 97.47314  ? 291 THR   A CG2   1 
ATOM   2124 N N     . HIS   A 1 292 ? 52.43092  -26.10258 28.25489  1.000 92.03610  ? 292 HIS   A N     1 
ATOM   2125 C CA    . HIS   A 1 292 ? 51.14695  -26.21209 27.58942  1.000 91.44930  ? 292 HIS   A CA    1 
ATOM   2126 C C     . HIS   A 1 292 ? 51.30666  -25.51595 26.24967  1.000 87.46274  ? 292 HIS   A C     1 
ATOM   2127 O O     . HIS   A 1 292 ? 51.71853  -24.35382 26.20259  1.000 89.77309  ? 292 HIS   A O     1 
ATOM   2128 C CB    . HIS   A 1 292 ? 50.03513  -25.59126 28.43708  1.000 95.30866  ? 292 HIS   A CB    1 
ATOM   2129 C CG    . HIS   A 1 292 ? 49.66317  -26.40105 29.65090  1.000 107.64866 ? 292 HIS   A CG    1 
ATOM   2130 N ND1   . HIS   A 1 292 ? 50.05374  -27.71317 29.82713  1.000 111.53397 ? 292 HIS   A ND1   1 
ATOM   2131 C CD2   . HIS   A 1 292 ? 48.94010  -26.07644 30.75195  1.000 108.18970 ? 292 HIS   A CD2   1 
ATOM   2132 C CE1   . HIS   A 1 292 ? 49.58239  -28.16262 30.97802  1.000 113.73944 ? 292 HIS   A CE1   1 
ATOM   2133 N NE2   . HIS   A 1 292 ? 48.90412  -27.18825 31.55882  1.000 111.59929 ? 292 HIS   A NE2   1 
ATOM   2134 N N     . ILE   A 1 293 ? 51.07776  -26.25108 25.16609  1.000 86.47838  ? 293 ILE   A N     1 
ATOM   2135 C CA    . ILE   A 1 293 ? 51.07398  -25.69261 23.81826  1.000 84.16671  ? 293 ILE   A CA    1 
ATOM   2136 C C     . ILE   A 1 293 ? 49.83158  -26.23034 23.11653  1.000 84.54048  ? 293 ILE   A C     1 
ATOM   2137 O O     . ILE   A 1 293 ? 49.64485  -27.45105 23.03668  1.000 89.11213  ? 293 ILE   A O     1 
ATOM   2138 C CB    . ILE   A 1 293 ? 52.34980  -26.04468 23.03494  1.000 78.93294  ? 293 ILE   A CB    1 
ATOM   2139 C CG1   . ILE   A 1 293 ? 53.53051  -25.23260 23.54646  1.000 79.42321  ? 293 ILE   A CG1   1 
ATOM   2140 C CG2   . ILE   A 1 293 ? 52.17902  -25.82217 21.52209  1.000 73.95352  ? 293 ILE   A CG2   1 
ATOM   2141 C CD1   . ILE   A 1 293 ? 54.77657  -25.47354 22.76049  1.000 86.86173  ? 293 ILE   A CD1   1 
ATOM   2142 N N     . LYS   A 1 294 ? 48.97733  -25.32447 22.61971  1.000 77.54356  ? 294 LYS   A N     1 
ATOM   2143 C CA    . LYS   A 1 294 ? 47.71919  -25.67227 21.96458  1.000 79.74747  ? 294 LYS   A CA    1 
ATOM   2144 C C     . LYS   A 1 294 ? 47.60341  -24.86607 20.67822  1.000 79.55278  ? 294 LYS   A C     1 
ATOM   2145 O O     . LYS   A 1 294 ? 48.12297  -23.74929 20.57816  1.000 78.39639  ? 294 LYS   A O     1 
ATOM   2146 C CB    . LYS   A 1 294 ? 46.50803  -25.38409 22.88529  1.000 78.60639  ? 294 LYS   A CB    1 
ATOM   2147 C CG    . LYS   A 1 294 ? 45.20971  -26.16430 22.62370  1.000 73.85866  ? 294 LYS   A CG    1 
ATOM   2148 C CD    . LYS   A 1 294 ? 44.28124  -25.98763 23.84408  1.000 84.06866  ? 294 LYS   A CD    1 
ATOM   2149 C CE    . LYS   A 1 294 ? 43.09194  -26.96051 23.92664  1.000 96.05629  ? 294 LYS   A CE    1 
ATOM   2150 N NZ    . LYS   A 1 294 ? 41.98223  -26.81107 22.94066  1.000 99.43866  ? 294 LYS   A NZ    1 
ATOM   2151 N N     . THR   A 1 295 ? 46.92583  -25.43251 19.68379  1.000 71.57378  ? 295 THR   A N     1 
ATOM   2152 C CA    . THR   A 1 295 ? 46.83877  -24.77448 18.39119  1.000 70.16932  ? 295 THR   A CA    1 
ATOM   2153 C C     . THR   A 1 295 ? 45.37967  -24.75274 17.99213  1.000 71.96039  ? 295 THR   A C     1 
ATOM   2154 O O     . THR   A 1 295 ? 44.75778  -25.80912 17.84786  1.000 65.95705  ? 295 THR   A O     1 
ATOM   2155 C CB    . THR   A 1 295 ? 47.71136  -25.47266 17.33906  1.000 74.08008  ? 295 THR   A CB    1 
ATOM   2156 O OG1   . THR   A 1 295 ? 49.08676  -25.26026 17.66943  1.000 78.82233  ? 295 THR   A OG1   1 
ATOM   2157 C CG2   . THR   A 1 295 ? 47.48235  -24.89559 15.93018  1.000 69.12290  ? 295 THR   A CG2   1 
ATOM   2158 N N     . TYR   A 1 296 ? 44.83635  -23.54505 17.85226  1.000 76.70314  ? 296 TYR   A N     1 
ATOM   2159 C CA    . TYR   A 1 296 ? 43.45682  -23.30774 17.46100  1.000 73.57657  ? 296 TYR   A CA    1 
ATOM   2160 C C     . TYR   A 1 296 ? 43.41266  -22.82406 16.02059  1.000 71.69477  ? 296 TYR   A C     1 
ATOM   2161 O O     . TYR   A 1 296 ? 44.23253  -21.99100 15.60534  1.000 72.65335  ? 296 TYR   A O     1 
ATOM   2162 C CB    . TYR   A 1 296 ? 42.80795  -22.24242 18.34975  1.000 76.88919  ? 296 TYR   A CB    1 
ATOM   2163 C CG    . TYR   A 1 296 ? 42.77759  -22.50426 19.84892  1.000 71.98029  ? 296 TYR   A CG    1 
ATOM   2164 C CD1   . TYR   A 1 296 ? 43.86450  -22.16048 20.66029  1.000 73.82386  ? 296 TYR   A CD1   1 
ATOM   2165 C CD2   . TYR   A 1 296 ? 41.63194  -22.99939 20.46688  1.000 66.73538  ? 296 TYR   A CD2   1 
ATOM   2166 C CE1   . TYR   A 1 296 ? 43.83055  -22.36389 22.04163  1.000 73.23936  ? 296 TYR   A CE1   1 
ATOM   2167 C CE2   . TYR   A 1 296 ? 41.58548  -23.20036 21.84676  1.000 73.52561  ? 296 TYR   A CE2   1 
ATOM   2168 C CZ    . TYR   A 1 296 ? 42.68538  -22.88577 22.62798  1.000 76.13260  ? 296 TYR   A CZ    1 
ATOM   2169 O OH    . TYR   A 1 296 ? 42.62974  -23.09278 23.99007  1.000 76.68799  ? 296 TYR   A OH    1 
ATOM   2170 N N     . THR   A 1 297 ? 42.43763  -23.32062 15.27072  1.000 70.74906  ? 297 THR   A N     1 
ATOM   2171 C CA    . THR   A 1 297 ? 42.14301  -22.74973 13.95099  1.000 76.27980  ? 297 THR   A CA    1 
ATOM   2172 C C     . THR   A 1 297 ? 41.03242  -21.71180 14.07288  1.000 80.43622  ? 297 THR   A C     1 
ATOM   2173 O O     . THR   A 1 297 ? 41.26151  -20.51237 13.87255  1.000 85.25413  ? 297 THR   A O     1 
ATOM   2174 C CB    . THR   A 1 297 ? 41.78525  -23.86527 12.98952  1.000 70.02257  ? 297 THR   A CB    1 
ATOM   2175 O OG1   . THR   A 1 297 ? 40.80745  -24.69038 13.62573  1.000 70.22767  ? 297 THR   A OG1   1 
ATOM   2176 C CG2   . THR   A 1 297 ? 43.04730  -24.67688 12.70428  1.000 63.30731  ? 297 THR   A CG2   1 
ATOM   2177 N N     . ASN   A 1 298 ? 39.82000  -22.17237 14.39885  1.000 80.55528  ? 298 ASN   A N     1 
ATOM   2178 C CA    . ASN   A 1 298 ? 38.75452  -21.30431 14.90518  1.000 77.45467  ? 298 ASN   A CA    1 
ATOM   2179 C C     . ASN   A 1 298 ? 39.33738  -20.23754 15.83627  1.000 76.97109  ? 298 ASN   A C     1 
ATOM   2180 O O     . ASN   A 1 298 ? 39.81558  -20.54410 16.93305  1.000 70.39393  ? 298 ASN   A O     1 
ATOM   2181 C CB    . ASN   A 1 298 ? 37.68035  -22.15004 15.61015  1.000 73.06473  ? 298 ASN   A CB    1 
ATOM   2182 C CG    . ASN   A 1 298 ? 36.40500  -21.35651 15.91218  1.000 81.26127  ? 298 ASN   A CG    1 
ATOM   2183 O OD1   . ASN   A 1 298 ? 36.47783  -20.19377 16.29739  1.000 76.79728  ? 298 ASN   A OD1   1 
ATOM   2184 N ND2   . ASN   A 1 298 ? 35.22737  -21.98275 15.70577  1.000 89.38003  ? 298 ASN   A ND2   1 
ATOM   2185 N N     . PHE   A 1 299 ? 39.31808  -18.98711 15.38754  1.000 79.23026  ? 299 PHE   A N     1 
ATOM   2186 C CA    . PHE   A 1 299 ? 39.98376  -17.89963 16.08017  1.000 72.35931  ? 299 PHE   A CA    1 
ATOM   2187 C C     . PHE   A 1 299 ? 39.16720  -17.38521 17.26357  1.000 71.10477  ? 299 PHE   A C     1 
ATOM   2188 O O     . PHE   A 1 299 ? 39.75392  -16.95519 18.27157  1.000 70.27942  ? 299 PHE   A O     1 
ATOM   2189 C CB    . PHE   A 1 299 ? 40.23829  -16.77394 15.08389  1.000 67.76360  ? 299 PHE   A CB    1 
ATOM   2190 C CG    . PHE   A 1 299 ? 40.80762  -15.55338 15.67690  1.000 64.34147  ? 299 PHE   A CG    1 
ATOM   2191 C CD1   . PHE   A 1 299 ? 42.16308  -15.45080 15.84666  1.000 64.04121  ? 299 PHE   A CD1   1 
ATOM   2192 C CD2   . PHE   A 1 299 ? 39.99832  -14.51202 16.07338  1.000 62.18431  ? 299 PHE   A CD2   1 
ATOM   2193 C CE1   . PHE   A 1 299 ? 42.70432  -14.33867 16.37020  1.000 62.37853  ? 299 PHE   A CE1   1 
ATOM   2194 C CE2   . PHE   A 1 299 ? 40.54619  -13.39464 16.61737  1.000 58.11963  ? 299 PHE   A CE2   1 
ATOM   2195 C CZ    . PHE   A 1 299 ? 41.90051  -13.30634 16.76393  1.000 57.20081  ? 299 PHE   A CZ    1 
ATOM   2196 N N     . PHE   A 1 300 ? 37.83562  -17.44628 17.16610  1.000 69.51557  ? 300 PHE   A N     1 
ATOM   2197 C CA    . PHE   A 1 300 ? 36.97355  -17.09545 18.29215  1.000 63.08448  ? 300 PHE   A CA    1 
ATOM   2198 C C     . PHE   A 1 300 ? 37.20343  -18.02234 19.46658  1.000 63.44948  ? 300 PHE   A C     1 
ATOM   2199 O O     . PHE   A 1 300 ? 37.01060  -17.61182 20.61035  1.000 67.31369  ? 300 PHE   A O     1 
ATOM   2200 C CB    . PHE   A 1 300 ? 35.50751  -17.14025 17.86803  1.000 59.33848  ? 300 PHE   A CB    1 
ATOM   2201 C CG    . PHE   A 1 300 ? 34.50196  -17.04973 19.01326  1.000 59.39662  ? 300 PHE   A CG    1 
ATOM   2202 C CD1   . PHE   A 1 300 ? 34.26065  -15.84639 19.67706  1.000 65.34948  ? 300 PHE   A CD1   1 
ATOM   2203 C CD2   . PHE   A 1 300 ? 33.73823  -18.14960 19.37509  1.000 63.08062  ? 300 PHE   A CD2   1 
ATOM   2204 C CE1   . PHE   A 1 300 ? 33.30591  -15.74494 20.69567  1.000 58.80866  ? 300 PHE   A CE1   1 
ATOM   2205 C CE2   . PHE   A 1 300 ? 32.78097  -18.05461 20.39629  1.000 71.43583  ? 300 PHE   A CE2   1 
ATOM   2206 C CZ    . PHE   A 1 300 ? 32.57204  -16.84263 21.05314  1.000 68.54620  ? 300 PHE   A CZ    1 
ATOM   2207 N N     . ASP   A 1 301 ? 37.58693  -19.27993 19.20773  1.000 68.52560  ? 301 ASP   A N     1 
ATOM   2208 C CA    . ASP   A 1 301 ? 37.89236  -20.21507 20.30320  1.000 72.00871  ? 301 ASP   A CA    1 
ATOM   2209 C C     . ASP   A 1 301 ? 39.23175  -19.87029 20.95086  1.000 66.63807  ? 301 ASP   A C     1 
ATOM   2210 O O     . ASP   A 1 301 ? 39.42129  -20.03952 22.16113  1.000 62.80055  ? 301 ASP   A O     1 
ATOM   2211 C CB    . ASP   A 1 301 ? 37.93259  -21.67685 19.81226  1.000 75.97980  ? 301 ASP   A CB    1 
ATOM   2212 C CG    . ASP   A 1 301 ? 36.59230  -22.19347 19.23927  1.000 78.14348  ? 301 ASP   A CG    1 
ATOM   2213 O OD1   . ASP   A 1 301 ? 35.57051  -21.46583 19.19564  1.000 74.56136  ? 301 ASP   A OD1   1 
ATOM   2214 O OD2   . ASP   A 1 301 ? 36.58869  -23.37069 18.79753  1.000 84.77263  ? 301 ASP   A OD2   1 
ATOM   2215 N N     . PHE   A 1 302 ? 40.19440  -19.43419 20.14754  1.000 65.56240  ? 302 PHE   A N     1 
ATOM   2216 C CA    . PHE   A 1 302 ? 41.42298  -18.94179 20.72734  1.000 63.80396  ? 302 PHE   A CA    1 
ATOM   2217 C C     . PHE   A 1 302 ? 41.11147  -17.78006 21.66032  1.000 65.37679  ? 302 PHE   A C     1 
ATOM   2218 O O     . PHE   A 1 302 ? 41.50619  -17.77894 22.83506  1.000 63.01566  ? 302 PHE   A O     1 
ATOM   2219 C CB    . PHE   A 1 302 ? 42.37107  -18.54349 19.59996  1.000 64.54727  ? 302 PHE   A CB    1 
ATOM   2220 C CG    . PHE   A 1 302 ? 43.40841  -17.55924 20.00598  1.000 67.98460  ? 302 PHE   A CG    1 
ATOM   2221 C CD1   . PHE   A 1 302 ? 44.49657  -17.95663 20.75517  1.000 68.98478  ? 302 PHE   A CD1   1 
ATOM   2222 C CD2   . PHE   A 1 302 ? 43.30464  -16.23207 19.63739  1.000 68.32595  ? 302 PHE   A CD2   1 
ATOM   2223 C CE1   . PHE   A 1 302 ? 45.47229  -17.05519 21.13008  1.000 66.93028  ? 302 PHE   A CE1   1 
ATOM   2224 C CE2   . PHE   A 1 302 ? 44.28581  -15.32303 20.01357  1.000 69.86973  ? 302 PHE   A CE2   1 
ATOM   2225 C CZ    . PHE   A 1 302 ? 45.37449  -15.74334 20.76349  1.000 63.51505  ? 302 PHE   A CZ    1 
ATOM   2226 N N     . SER   A 1 303 ? 40.29751  -16.83720 21.17482  1.000 63.45620  ? 303 SER   A N     1 
ATOM   2227 C CA    . SER   A 1 303 ? 39.98052  -15.62571 21.92251  1.000 59.62616  ? 303 SER   A CA    1 
ATOM   2228 C C     . SER   A 1 303 ? 39.19941  -15.91867 23.19964  1.000 63.42138  ? 303 SER   A C     1 
ATOM   2229 O O     . SER   A 1 303 ? 39.53546  -15.39762 24.27061  1.000 65.70745  ? 303 SER   A O     1 
ATOM   2230 C CB    . SER   A 1 303 ? 39.19528  -14.67653 21.02727  1.000 60.97334  ? 303 SER   A CB    1 
ATOM   2231 O OG    . SER   A 1 303 ? 39.67384  -14.75900 19.69207  1.000 70.43659  ? 303 SER   A OG    1 
ATOM   2232 N N     . ALA   A 1 304 ? 38.13303  -16.72318 23.10209  1.000 64.41219  ? 304 ALA   A N     1 
ATOM   2233 C CA    . ALA   A 1 304 ? 37.30297  -17.01377 24.27044  1.000 61.99701  ? 304 ALA   A CA    1 
ATOM   2234 C C     . ALA   A 1 304 ? 38.05656  -17.84926 25.29301  1.000 61.41233  ? 304 ALA   A C     1 
ATOM   2235 O O     . ALA   A 1 304 ? 37.79867  -17.73554 26.50082  1.000 56.73178  ? 304 ALA   A O     1 
ATOM   2236 C CB    . ALA   A 1 304 ? 36.02311  -17.72758 23.83896  1.000 61.27730  ? 304 ALA   A CB    1 
ATOM   2237 N N     . ALA   A 1 305 ? 38.96848  -18.70321 24.80775  1.000 64.66391  ? 305 ALA   A N     1 
ATOM   2238 C CA    . ALA   A 1 305 ? 39.86145  -19.46256 25.67557  1.000 64.89143  ? 305 ALA   A CA    1 
ATOM   2239 C C     . ALA   A 1 305 ? 40.70712  -18.52591 26.52831  1.000 61.92033  ? 305 ALA   A C     1 
ATOM   2240 O O     . ALA   A 1 305 ? 40.72275  -18.63216 27.76463  1.000 59.13368  ? 305 ALA   A O     1 
ATOM   2241 C CB    . ALA   A 1 305 ? 40.74649  -20.38509 24.82950  1.000 57.22476  ? 305 ALA   A CB    1 
ATOM   2242 N N     . ALA   A 1 306 ? 41.38785  -17.57235 25.88100  1.000 57.05067  ? 306 ALA   A N     1 
ATOM   2243 C CA    . ALA   A 1 306 ? 42.24360  -16.66435 26.62309  1.000 55.79820  ? 306 ALA   A CA    1 
ATOM   2244 C C     . ALA   A 1 306 ? 41.44326  -15.70275 27.51397  1.000 59.63533  ? 306 ALA   A C     1 
ATOM   2245 O O     . ALA   A 1 306 ? 41.90963  -15.34798 28.60545  1.000 57.15257  ? 306 ALA   A O     1 
ATOM   2246 C CB    . ALA   A 1 306 ? 43.14562  -15.91980 25.64743  1.000 56.86967  ? 306 ALA   A CB    1 
ATOM   2247 N N     . SER   A 1 307 ? 40.24468  -15.27824 27.08910  1.000 62.19064  ? 307 SER   A N     1 
ATOM   2248 C CA    . SER   A 1 307 ? 39.38377  -14.52378 27.99763  1.000 59.92144  ? 307 SER   A CA    1 
ATOM   2249 C C     . SER   A 1 307 ? 39.02834  -15.35477 29.20695  1.000 61.75841  ? 307 SER   A C     1 
ATOM   2250 O O     . SER   A 1 307 ? 39.01024  -14.85380 30.34115  1.000 64.61800  ? 307 SER   A O     1 
ATOM   2251 C CB    . SER   A 1 307 ? 38.09024  -14.07043 27.30607  1.000 56.44102  ? 307 SER   A CB    1 
ATOM   2252 O OG    . SER   A 1 307 ? 37.18617  -13.49223 28.24817  1.000 50.96510  ? 307 SER   A OG    1 
ATOM   2253 N N     . ALA   A 1 308 ? 38.70165  -16.62414 28.97435  1.000 66.07037  ? 308 ALA   A N     1 
ATOM   2254 C CA    . ALA   A 1 308 ? 38.41171  -17.51725 30.08274  1.000 65.31629  ? 308 ALA   A CA    1 
ATOM   2255 C C     . ALA   A 1 308 ? 39.61518  -17.63456 31.00095  1.000 64.00216  ? 308 ALA   A C     1 
ATOM   2256 O O     . ALA   A 1 308 ? 39.46712  -17.59770 32.22648  1.000 61.91329  ? 308 ALA   A O     1 
ATOM   2257 C CB    . ALA   A 1 308 ? 37.99063  -18.88037 29.54571  1.000 59.20819  ? 308 ALA   A CB    1 
ATOM   2258 N N     . GLN   A 1 309 ? 40.82047  -17.69651 30.42126  1.000 64.02950  ? 309 GLN   A N     1 
ATOM   2259 C CA    . GLN   A 1 309 ? 42.02551  -17.94197 31.20913  1.000 64.62524  ? 309 GLN   A CA    1 
ATOM   2260 C C     . GLN   A 1 309 ? 42.32970  -16.82547 32.20906  1.000 67.80862  ? 309 GLN   A C     1 
ATOM   2261 O O     . GLN   A 1 309 ? 42.64529  -17.09941 33.37079  1.000 72.17977  ? 309 GLN   A O     1 
ATOM   2262 C CB    . GLN   A 1 309 ? 43.22521  -18.15456 30.30618  1.000 66.12866  ? 309 GLN   A CB    1 
ATOM   2263 C CG    . GLN   A 1 309 ? 44.46621  -17.90124 31.10209  1.000 76.25546  ? 309 GLN   A CG    1 
ATOM   2264 C CD    . GLN   A 1 309 ? 45.62868  -18.61094 30.53315  1.000 91.80667  ? 309 GLN   A CD    1 
ATOM   2265 O OE1   . GLN   A 1 309 ? 45.49796  -19.30770 29.51650  1.000 89.69202  ? 309 GLN   A OE1   1 
ATOM   2266 N NE2   . GLN   A 1 309 ? 46.78948  -18.46045 31.17540  1.000 91.98668  ? 309 GLN   A NE2   1 
ATOM   2267 N N     . THR   A 1 310 ? 42.30836  -15.56842 31.77413  1.000 64.33084  ? 310 THR   A N     1 
ATOM   2268 C CA    . THR   A 1 310 ? 42.48266  -14.48660 32.73417  1.000 63.11474  ? 310 THR   A CA    1 
ATOM   2269 C C     . THR   A 1 310 ? 41.37023  -14.47163 33.78456  1.000 62.00990  ? 310 THR   A C     1 
ATOM   2270 O O     . THR   A 1 310 ? 41.63608  -14.17878 34.95620  1.000 67.07299  ? 310 THR   A O     1 
ATOM   2271 C CB    . THR   A 1 310 ? 42.56321  -13.15226 31.99765  1.000 68.04075  ? 310 THR   A CB    1 
ATOM   2272 O OG1   . THR   A 1 310 ? 41.26470  -12.80108 31.46259  1.000 66.10655  ? 310 THR   A OG1   1 
ATOM   2273 C CG2   . THR   A 1 310 ? 43.58380  -13.27225 30.88822  1.000 65.12031  ? 310 THR   A CG2   1 
ATOM   2274 N N     . LYS   A 1 311 ? 40.13201  -14.79342 33.40871  1.000 60.16370  ? 311 LYS   A N     1 
ATOM   2275 C CA    . LYS   A 1 311 ? 39.06131  -14.77792 34.40042  1.000 68.56421  ? 311 LYS   A CA    1 
ATOM   2276 C C     . LYS   A 1 311 ? 39.34029  -15.78814 35.50111  1.000 69.47665  ? 311 LYS   A C     1 
ATOM   2277 O O     . LYS   A 1 311 ? 39.30182  -15.45487 36.69368  1.000 74.34165  ? 311 LYS   A O     1 
ATOM   2278 C CB    . LYS   A 1 311 ? 37.70183  -15.04138 33.72950  1.000 68.42068  ? 311 LYS   A CB    1 
ATOM   2279 C CG    . LYS   A 1 311 ? 36.54561  -14.29091 34.38991  1.000 65.34866  ? 311 LYS   A CG    1 
ATOM   2280 C CD    . LYS   A 1 311 ? 35.13745  -14.85923 34.11705  1.000 80.58310  ? 311 LYS   A CD    1 
ATOM   2281 C CE    . LYS   A 1 311 ? 34.74962  -16.09162 34.94036  1.000 78.41242  ? 311 LYS   A CE    1 
ATOM   2282 N NZ    . LYS   A 1 311 ? 33.24982  -16.28463 34.84518  1.000 69.11967  ? 311 LYS   A NZ    1 
ATOM   2283 N N     . ALA   A 1 312 ? 39.68436  -17.02016 35.10468  1.000 65.89130  ? 312 ALA   A N     1 
ATOM   2284 C CA    . ALA   A 1 312 ? 39.98427  -18.10308 36.04390  1.000 56.02003  ? 312 ALA   A CA    1 
ATOM   2285 C C     . ALA   A 1 312 ? 41.19432  -17.82338 36.91187  1.000 60.70697  ? 312 ALA   A C     1 
ATOM   2286 O O     . ALA   A 1 312 ? 41.29270  -18.37715 38.00798  1.000 69.97352  ? 312 ALA   A O     1 
ATOM   2287 C CB    . ALA   A 1 312 ? 40.24184  -19.39416 35.29464  1.000 59.51421  ? 312 ALA   A CB    1 
ATOM   2288 N N     . ALA   A 1 313 ? 42.15645  -17.04263 36.42600  1.000 62.09126  ? 313 ALA   A N     1 
ATOM   2289 C CA    . ALA   A 1 313 ? 43.27953  -16.67391 37.28284  1.000 64.55569  ? 313 ALA   A CA    1 
ATOM   2290 C C     . ALA   A 1 313 ? 42.83017  -15.83477 38.46900  1.000 68.55539  ? 313 ALA   A C     1 
ATOM   2291 O O     . ALA   A 1 313 ? 43.52103  -15.82876 39.49531  1.000 72.68905  ? 313 ALA   A O     1 
ATOM   2292 C CB    . ALA   A 1 313 ? 44.34560  -15.92473 36.47959  1.000 67.46286  ? 313 ALA   A CB    1 
ATOM   2293 N N     . GLY   A 1 314 ? 41.68857  -15.14961 38.35506  1.000 64.48220  ? 314 GLY   A N     1 
ATOM   2294 C CA    . GLY   A 1 314 ? 41.18908  -14.30969 39.42632  1.000 70.70403  ? 314 GLY   A CA    1 
ATOM   2295 C C     . GLY   A 1 314 ? 41.61140  -12.86050 39.34835  1.000 71.74384  ? 314 GLY   A C     1 
ATOM   2296 O O     . GLY   A 1 314 ? 41.47790  -12.12315 40.33932  1.000 69.38445  ? 314 GLY   A O     1 
ATOM   2297 N N     . ILE   A 1 315 ? 42.10962  -12.42511 38.19842  1.000 70.65400  ? 315 ILE   A N     1 
ATOM   2298 C CA    . ILE   A 1 315 ? 42.55304  -11.05341 38.02387  1.000 78.74648  ? 315 ILE   A CA    1 
ATOM   2299 C C     . ILE   A 1 315 ? 41.63796  -10.27010 37.07637  1.000 75.86993  ? 315 ILE   A C     1 
ATOM   2300 O O     . ILE   A 1 315 ? 41.97795  -9.14271  36.68619  1.000 71.21303  ? 315 ILE   A O     1 
ATOM   2301 C CB    . ILE   A 1 315 ? 44.02029  -11.02428 37.56606  1.000 79.78866  ? 315 ILE   A CB    1 
ATOM   2302 C CG1   . ILE   A 1 315 ? 44.23249  -11.83966 36.29270  1.000 79.96866  ? 315 ILE   A CG1   1 
ATOM   2303 C CG2   . ILE   A 1 315 ? 44.89071  -11.62231 38.63764  1.000 83.91866  ? 315 ILE   A CG2   1 
ATOM   2304 C CD1   . ILE   A 1 315 ? 45.67881  -11.84969 35.83511  1.000 75.91866  ? 315 ILE   A CD1   1 
ATOM   2305 N N     . ALA   A 1 316 ? 40.44389  -10.81692 36.75021  1.000 68.03282  ? 316 ALA   A N     1 
ATOM   2306 C CA    . ALA   A 1 316 ? 39.55672  -10.22904 35.74977  1.000 62.23925  ? 316 ALA   A CA    1 
ATOM   2307 C C     . ALA   A 1 316 ? 38.11515  -10.01601 36.20988  1.000 61.29023  ? 316 ALA   A C     1 
ATOM   2308 O O     . ALA   A 1 316 ? 37.26829  -9.61879  35.39447  1.000 63.36918  ? 316 ALA   A O     1 
ATOM   2309 C CB    . ALA   A 1 316 ? 39.53262  -11.09748 34.49058  1.000 65.70271  ? 316 ALA   A CB    1 
ATOM   2310 N N     . SER   A 1 317 ? 37.80648  -10.26452 37.45072  1.000 59.26687  ? 317 SER   A N     1 
ATOM   2311 C CA    . SER   A 1 317 ? 36.43845  -10.14877 37.92816  1.000 54.04521  ? 317 SER   A CA    1 
ATOM   2312 C C     . SER   A 1 317 ? 36.32308  -8.95366  38.85903  1.000 58.55743  ? 317 SER   A C     1 
ATOM   2313 O O     . SER   A 1 317 ? 37.30549  -8.61742  39.52399  1.000 67.88215  ? 317 SER   A O     1 
ATOM   2314 C CB    . SER   A 1 317 ? 36.06912  -11.41073 38.70625  1.000 54.90242  ? 317 SER   A CB    1 
ATOM   2315 O OG    . SER   A 1 317 ? 36.34330  -12.53582 37.90249  1.000 60.20011  ? 317 SER   A OG    1 
ATOM   2316 N N     . PRO   A 1 318 ? 35.16426  -8.29636  38.96414  1.000 56.08602  ? 318 PRO   A N     1 
ATOM   2317 C CA    . PRO   A 1 318 ? 35.01123  -7.29482  40.02653  1.000 57.14797  ? 318 PRO   A CA    1 
ATOM   2318 C C     . PRO   A 1 318 ? 35.45552  -7.89345  41.35299  1.000 60.43756  ? 318 PRO   A C     1 
ATOM   2319 O O     . PRO   A 1 318 ? 35.21644  -9.07514  41.62770  1.000 60.98283  ? 318 PRO   A O     1 
ATOM   2320 C CB    . PRO   A 1 318 ? 33.51609  -6.96955  40.01547  1.000 50.00312  ? 318 PRO   A CB    1 
ATOM   2321 C CG    . PRO   A 1 318 ? 33.07200  -7.31558  38.69370  1.000 46.24252  ? 318 PRO   A CG    1 
ATOM   2322 C CD    . PRO   A 1 318 ? 33.93715  -8.42560  38.16783  1.000 54.77281  ? 318 PRO   A CD    1 
ATOM   2323 N N     . SER   A 1 319 ? 36.15939  -7.09318  42.15202  1.000 62.33665  ? 319 SER   A N     1 
ATOM   2324 C CA    . SER   A 1 319 ? 36.76284  -7.59510  43.38311  1.000 64.35952  ? 319 SER   A CA    1 
ATOM   2325 C C     . SER   A 1 319 ? 37.21120  -6.41731  44.23522  1.000 63.28912  ? 319 SER   A C     1 
ATOM   2326 O O     . SER   A 1 319 ? 36.98578  -5.25026  43.89872  1.000 63.24013  ? 319 SER   A O     1 
ATOM   2327 C CB    . SER   A 1 319 ? 37.92881  -8.53531  43.07828  1.000 59.97779  ? 319 SER   A CB    1 
ATOM   2328 O OG    . SER   A 1 319 ? 39.00442  -7.83205  42.48881  1.000 63.74609  ? 319 SER   A OG    1 
ATOM   2329 N N     . HIS   A 1 320 ? 37.81525  -6.74104  45.36973  1.000 64.69994  ? 320 HIS   A N     1 
ATOM   2330 C CA    . HIS   A 1 320 ? 38.57603  -5.76092  46.13049  1.000 69.51839  ? 320 HIS   A CA    1 
ATOM   2331 C C     . HIS   A 1 320 ? 40.01997  -5.83364  45.63946  1.000 68.45115  ? 320 HIS   A C     1 
ATOM   2332 O O     . HIS   A 1 320 ? 40.63362  -6.91001  45.64110  1.000 64.84625  ? 320 HIS   A O     1 
ATOM   2333 C CB    . HIS   A 1 320 ? 38.46584  -6.00102  47.64419  1.000 71.41009  ? 320 HIS   A CB    1 
ATOM   2334 C CG    . HIS   A 1 320 ? 37.07171  -5.85695  48.19921  1.000 71.52356  ? 320 HIS   A CG    1 
ATOM   2335 N ND1   . HIS   A 1 320 ? 36.62110  -4.68700  48.77692  1.000 68.96675  ? 320 HIS   A ND1   1 
ATOM   2336 C CD2   . HIS   A 1 320 ? 36.04631  -6.73991  48.30418  1.000 69.88884  ? 320 HIS   A CD2   1 
ATOM   2337 C CE1   . HIS   A 1 320 ? 35.37159  -4.84166  49.18137  1.000 65.39167  ? 320 HIS   A CE1   1 
ATOM   2338 N NE2   . HIS   A 1 320 ? 34.99999  -6.08024  48.91238  1.000 64.33614  ? 320 HIS   A NE2   1 
ATOM   2339 N N     . PHE   A 1 321 ? 40.54371  -4.71089  45.16458  1.000 65.67049  ? 321 PHE   A N     1 
ATOM   2340 C CA    . PHE   A 1 321 ? 41.87170  -4.75879  44.56916  1.000 64.80353  ? 321 PHE   A CA    1 
ATOM   2341 C C     . PHE   A 1 321 ? 42.42199  -3.34390  44.43684  1.000 62.47909  ? 321 PHE   A C     1 
ATOM   2342 O O     . PHE   A 1 321 ? 41.73052  -2.35228  44.69500  1.000 58.32674  ? 321 PHE   A O     1 
ATOM   2343 C CB    . PHE   A 1 321 ? 41.83951  -5.46590  43.20256  1.000 68.74453  ? 321 PHE   A CB    1 
ATOM   2344 C CG    . PHE   A 1 321 ? 41.18136  -4.64639  42.09608  1.000 68.22365  ? 321 PHE   A CG    1 
ATOM   2345 C CD1   . PHE   A 1 321 ? 39.79942  -4.58746  41.98148  1.000 66.21237  ? 321 PHE   A CD1   1 
ATOM   2346 C CD2   . PHE   A 1 321 ? 41.95352  -3.91374  41.19064  1.000 63.48196  ? 321 PHE   A CD2   1 
ATOM   2347 C CE1   . PHE   A 1 321 ? 39.20519  -3.83526  40.98609  1.000 63.04186  ? 321 PHE   A CE1   1 
ATOM   2348 C CE2   . PHE   A 1 321 ? 41.36855  -3.15343  40.20042  1.000 57.93937  ? 321 PHE   A CE2   1 
ATOM   2349 C CZ    . PHE   A 1 321 ? 39.99502  -3.11168  40.09803  1.000 61.31124  ? 321 PHE   A CZ    1 
ATOM   2350 N N     . TYR   A 1 322 ? 43.69588  -3.27164  44.05229  1.000 55.93862  ? 322 TYR   A N     1 
ATOM   2351 C CA    . TYR   A 1 322 ? 44.30825  -2.04211  43.58682  1.000 58.40887  ? 322 TYR   A CA    1 
ATOM   2352 C C     . TYR   A 1 322 ? 45.40502  -2.48791  42.63169  1.000 63.23203  ? 322 TYR   A C     1 
ATOM   2353 O O     . TYR   A 1 322 ? 45.90898  -3.60697  42.74879  1.000 63.60165  ? 322 TYR   A O     1 
ATOM   2354 C CB    . TYR   A 1 322 ? 44.81102  -1.19031  44.76940  1.000 66.57014  ? 322 TYR   A CB    1 
ATOM   2355 C CG    . TYR   A 1 322 ? 45.81361  -0.09049  44.46135  1.000 68.40077  ? 322 TYR   A CG    1 
ATOM   2356 C CD1   . TYR   A 1 322 ? 45.41165  1.07806   43.83180  1.000 69.69131  ? 322 TYR   A CD1   1 
ATOM   2357 C CD2   . TYR   A 1 322 ? 47.15840  -0.22051  44.79559  1.000 71.73272  ? 322 TYR   A CD2   1 
ATOM   2358 C CE1   . TYR   A 1 322 ? 46.31864  2.09729   43.53394  1.000 70.98765  ? 322 TYR   A CE1   1 
ATOM   2359 C CE2   . TYR   A 1 322 ? 48.07972  0.79328   44.50053  1.000 73.36062  ? 322 TYR   A CE2   1 
ATOM   2360 C CZ    . TYR   A 1 322 ? 47.64430  1.95805   43.86940  1.000 73.17139  ? 322 TYR   A CZ    1 
ATOM   2361 O OH    . TYR   A 1 322 ? 48.52229  2.98003   43.56054  1.000 66.07356  ? 322 TYR   A OH    1 
ATOM   2362 N N     . ALA   A 1 323 ? 45.71344  -1.64387  41.64415  1.000 64.96693  ? 323 ALA   A N     1 
ATOM   2363 C CA    . ALA   A 1 323 ? 46.63181  -1.98869  40.56472  1.000 70.33774  ? 323 ALA   A CA    1 
ATOM   2364 C C     . ALA   A 1 323 ? 47.25297  -0.71217  40.01210  1.000 72.70405  ? 323 ALA   A C     1 
ATOM   2365 O O     . ALA   A 1 323 ? 46.66188  0.36977   40.08083  1.000 69.04079  ? 323 ALA   A O     1 
ATOM   2366 C CB    . ALA   A 1 323 ? 45.93350  -2.75873  39.43286  1.000 63.52310  ? 323 ALA   A CB    1 
ATOM   2367 N N     . LYS   A 1 324 ? 48.45224  -0.85001  39.45214  1.000 68.82761  ? 324 LYS   A N     1 
ATOM   2368 C CA    . LYS   A 1 324 ? 49.15915  0.27806   38.85701  1.000 66.36824  ? 324 LYS   A CA    1 
ATOM   2369 C C     . LYS   A 1 324 ? 49.77325  -0.17155  37.55036  1.000 70.90160  ? 324 LYS   A C     1 
ATOM   2370 O O     . LYS   A 1 324 ? 49.82174  -1.36634  37.22775  1.000 69.56669  ? 324 LYS   A O     1 
ATOM   2371 C CB    . LYS   A 1 324 ? 50.26672  0.81634   39.76342  1.000 70.92639  ? 324 LYS   A CB    1 
ATOM   2372 C CG    . LYS   A 1 324 ? 49.86850  0.99590   41.20581  1.000 72.34632  ? 324 LYS   A CG    1 
ATOM   2373 C CD    . LYS   A 1 324 ? 51.09741  1.28859   42.04088  1.000 72.72212  ? 324 LYS   A CD    1 
ATOM   2374 C CE    . LYS   A 1 324 ? 51.67075  2.62012   41.71734  1.000 67.67456  ? 324 LYS   A CE    1 
ATOM   2375 N NZ    . LYS   A 1 324 ? 50.78049  3.61132   42.31472  1.000 66.75102  ? 324 LYS   A NZ    1 
ATOM   2376 N N     . SER   A 1 325 ? 50.26282  0.80077   36.79761  1.000 71.30676  ? 325 SER   A N     1 
ATOM   2377 C CA    . SER   A 1 325 ? 50.87847  0.48330   35.51972  1.000 74.71663  ? 325 SER   A CA    1 
ATOM   2378 C C     . SER   A 1 325 ? 52.22648  1.18390   35.41652  1.000 70.55996  ? 325 SER   A C     1 
ATOM   2379 O O     . SER   A 1 325 ? 52.58085  2.03791   36.24879  1.000 67.96872  ? 325 SER   A O     1 
ATOM   2380 C CB    . SER   A 1 325 ? 49.95083  0.82743   34.31615  1.000 73.90177  ? 325 SER   A CB    1 
ATOM   2381 O OG    . SER   A 1 325 ? 49.31770  2.10462   34.37552  1.000 72.99850  ? 325 SER   A OG    1 
ATOM   2382 N N     . LEU   A 1 326 ? 52.97589  0.74998   34.40254  1.000 61.06008  ? 326 LEU   A N     1 
ATOM   2383 C CA    . LEU   A 1 326 ? 54.24878  1.31542   34.01222  1.000 60.09971  ? 326 LEU   A CA    1 
ATOM   2384 C C     . LEU   A 1 326 ? 54.54948  0.92620   32.57784  1.000 65.22231  ? 326 LEU   A C     1 
ATOM   2385 O O     . LEU   A 1 326 ? 54.26046  -0.19746  32.16064  1.000 66.36315  ? 326 LEU   A O     1 
ATOM   2386 C CB    . LEU   A 1 326 ? 55.37619  0.81254   34.89806  1.000 68.23050  ? 326 LEU   A CB    1 
ATOM   2387 C CG    . LEU   A 1 326 ? 55.46032  1.28308   36.33653  1.000 76.98929  ? 326 LEU   A CG    1 
ATOM   2388 C CD1   . LEU   A 1 326 ? 56.66578  0.54969   36.90898  1.000 78.95817  ? 326 LEU   A CD1   1 
ATOM   2389 C CD2   . LEU   A 1 326 ? 55.60269  2.81401   36.44345  1.000 66.11805  ? 326 LEU   A CD2   1 
ATOM   2390 N N     . VAL   A 1 327 ? 55.17375  1.84855   31.84746  1.000 63.69119  ? 327 VAL   A N     1 
ATOM   2391 C CA    . VAL   A 1 327 ? 55.69349  1.59899   30.51175  1.000 62.39597  ? 327 VAL   A CA    1 
ATOM   2392 C C     . VAL   A 1 327 ? 57.20965  1.55975   30.59184  1.000 69.32812  ? 327 VAL   A C     1 
ATOM   2393 O O     . VAL   A 1 327 ? 57.81295  2.44342   31.20857  1.000 77.20581  ? 327 VAL   A O     1 
ATOM   2394 C CB    . VAL   A 1 327 ? 55.26102  2.69592   29.53345  1.000 63.67572  ? 327 VAL   A CB    1 
ATOM   2395 C CG1   . VAL   A 1 327 ? 55.91101  2.47338   28.21313  1.000 64.57816  ? 327 VAL   A CG1   1 
ATOM   2396 C CG2   . VAL   A 1 327 ? 53.76409  2.73208   29.38986  1.000 70.66955  ? 327 VAL   A CG2   1 
ATOM   2397 N N     . PHE   A 1 328 ? 57.82997  0.55342   29.95791  1.000 70.75384  ? 328 PHE   A N     1 
ATOM   2398 C CA    . PHE   A 1 328 ? 59.28520  0.47577   29.80332  1.000 70.69881  ? 328 PHE   A CA    1 
ATOM   2399 C C     . PHE   A 1 328 ? 59.62976  0.34294   28.32002  1.000 73.91022  ? 328 PHE   A C     1 
ATOM   2400 O O     . PHE   A 1 328 ? 59.08588  -0.51949  27.61687  1.000 68.54139  ? 328 PHE   A O     1 
ATOM   2401 C CB    . PHE   A 1 328 ? 59.90241  -0.71052  30.58133  1.000 68.87412  ? 328 PHE   A CB    1 
ATOM   2402 C CG    . PHE   A 1 328 ? 59.76158  -0.60919  32.07173  1.000 70.89842  ? 328 PHE   A CG    1 
ATOM   2403 C CD1   . PHE   A 1 328 ? 60.65244  0.14542   32.81733  1.000 76.38936  ? 328 PHE   A CD1   1 
ATOM   2404 C CD2   . PHE   A 1 328 ? 58.73978  -1.28013  32.73608  1.000 69.49581  ? 328 PHE   A CD2   1 
ATOM   2405 C CE1   . PHE   A 1 328 ? 60.52016  0.26248   34.20859  1.000 81.09523  ? 328 PHE   A CE1   1 
ATOM   2406 C CE2   . PHE   A 1 328 ? 58.60933  -1.17657  34.12411  1.000 77.72283  ? 328 PHE   A CE2   1 
ATOM   2407 C CZ    . PHE   A 1 328 ? 59.50118  -0.40180  34.86102  1.000 79.84300  ? 328 PHE   A CZ    1 
ATOM   2408 N N     . ASN   A 1 329 ? 60.55417  1.17377   27.85564  1.000 78.76434  ? 329 ASN   A N     1 
ATOM   2409 C CA    . ASN   A 1 329 ? 61.03986  1.15235   26.48256  1.000 79.20539  ? 329 ASN   A CA    1 
ATOM   2410 C C     . ASN   A 1 329 ? 62.55180  0.87620   26.48281  1.000 84.07625  ? 329 ASN   A C     1 
ATOM   2411 O O     . ASN   A 1 329 ? 63.13988  0.54327   27.51762  1.000 85.71188  ? 329 ASN   A O     1 
ATOM   2412 C CB    . ASN   A 1 329 ? 60.66678  2.46593   25.80912  1.000 78.97177  ? 329 ASN   A CB    1 
ATOM   2413 C CG    . ASN   A 1 329 ? 61.43421  3.61913   26.37693  1.000 84.32667  ? 329 ASN   A CG    1 
ATOM   2414 O OD1   . ASN   A 1 329 ? 62.54335  3.90434   25.93566  1.000 91.39287  ? 329 ASN   A OD1   1 
ATOM   2415 N ND2   . ASN   A 1 329 ? 60.86590  4.28119   27.38015  1.000 77.33170  ? 329 ASN   A ND2   1 
ATOM   2416 N N     . GLN   A 1 330 ? 63.18853  1.00782   25.31553  1.000 86.91164  ? 330 GLN   A N     1 
ATOM   2417 C CA    . GLN   A 1 330 ? 64.60359  0.64693   25.19804  1.000 87.63991  ? 330 GLN   A CA    1 
ATOM   2418 C C     . GLN   A 1 330 ? 65.46917  1.40366   26.20901  1.000 88.16492  ? 330 GLN   A C     1 
ATOM   2419 O O     . GLN   A 1 330 ? 66.17995  0.79489   27.01564  1.000 85.27912  ? 330 GLN   A O     1 
ATOM   2420 C CB    . GLN   A 1 330 ? 65.09872  0.90716   23.77356  1.000 94.15349  ? 330 GLN   A CB    1 
ATOM   2421 C CG    . GLN   A 1 330 ? 66.38626  0.16989   23.42988  1.000 93.30712  ? 330 GLN   A CG    1 
ATOM   2422 C CD    . GLN   A 1 330 ? 66.14611  -1.26338  22.99682  1.000 101.30395 ? 330 GLN   A CD    1 
ATOM   2423 O OE1   . GLN   A 1 330 ? 65.69010  -1.51327  21.87909  1.000 107.66943 ? 330 GLN   A OE1   1 
ATOM   2424 N NE2   . GLN   A 1 330 ? 66.45185  -2.21199  23.87641  1.000 101.99107 ? 330 GLN   A NE2   1 
ATOM   2425 N N     . GLN   A 1 331 ? 65.42138  2.74217   26.17433  1.000 86.41642  ? 331 GLN   A N     1 
ATOM   2426 C CA    . GLN   A 1 331 ? 66.18652  3.55700   27.11206  1.000 84.58856  ? 331 GLN   A CA    1 
ATOM   2427 C C     . GLN   A 1 331 ? 65.94563  3.17992   28.56745  1.000 88.67666  ? 331 GLN   A C     1 
ATOM   2428 O O     . GLN   A 1 331 ? 66.80501  3.43934   29.42053  1.000 96.77654  ? 331 GLN   A O     1 
ATOM   2429 C CB    . GLN   A 1 331 ? 65.84072  5.03136   26.93630  1.000 82.60798  ? 331 GLN   A CB    1 
ATOM   2430 C CG    . GLN   A 1 331 ? 66.37478  5.63037   25.67088  1.000 93.89636  ? 331 GLN   A CG    1 
ATOM   2431 C CD    . GLN   A 1 331 ? 65.64715  5.14233   24.43459  1.000 99.22967  ? 331 GLN   A CD    1 
ATOM   2432 O OE1   . GLN   A 1 331 ? 64.50197  5.53348   24.18089  1.000 106.25188 ? 331 GLN   A OE1   1 
ATOM   2433 N NE2   . GLN   A 1 331 ? 66.32292  4.31844   23.63221  1.000 93.78554  ? 331 GLN   A NE2   1 
ATOM   2434 N N     . THR   A 1 332 ? 64.79626  2.59084   28.88348  1.000 81.83091  ? 332 THR   A N     1 
ATOM   2435 C CA    . THR   A 1 332 ? 64.35833  2.46990   30.26764  1.000 82.17279  ? 332 THR   A CA    1 
ATOM   2436 C C     . THR   A 1 332 ? 64.27318  1.04180   30.78280  1.000 83.24832  ? 332 THR   A C     1 
ATOM   2437 O O     . THR   A 1 332 ? 63.82211  0.84067   31.91863  1.000 87.29295  ? 332 THR   A O     1 
ATOM   2438 C CB    . THR   A 1 332 ? 63.01824  3.16553   30.44005  1.000 84.94480  ? 332 THR   A CB    1 
ATOM   2439 O OG1   . THR   A 1 332 ? 62.08876  2.66397   29.46945  1.000 79.57835  ? 332 THR   A OG1   1 
ATOM   2440 C CG2   . THR   A 1 332 ? 63.20215  4.64334   30.25574  1.000 89.03642  ? 332 THR   A CG2   1 
ATOM   2441 N N     . LEU   A 1 333 ? 64.72240  0.05479   29.99613  1.000 80.50549  ? 333 LEU   A N     1 
ATOM   2442 C CA    . LEU   A 1 333 ? 64.73067  -1.35254  30.39653  1.000 81.54511  ? 333 LEU   A CA    1 
ATOM   2443 C C     . LEU   A 1 333 ? 65.23205  -1.52812  31.82303  1.000 83.84941  ? 333 LEU   A C     1 
ATOM   2444 O O     . LEU   A 1 333 ? 65.91445  -0.65321  32.36148  1.000 88.60244  ? 333 LEU   A O     1 
ATOM   2445 C CB    . LEU   A 1 333 ? 65.60712  -2.16729  29.44232  1.000 80.76318  ? 333 LEU   A CB    1 
ATOM   2446 C CG    . LEU   A 1 333 ? 65.03876  -2.27774  28.02857  1.000 84.27217  ? 333 LEU   A CG    1 
ATOM   2447 C CD1   . LEU   A 1 333 ? 65.92475  -3.06637  27.04990  1.000 82.66869  ? 333 LEU   A CD1   1 
ATOM   2448 C CD2   . LEU   A 1 333 ? 63.65957  -2.90973  28.15007  1.000 87.98119  ? 333 LEU   A CD2   1 
ATOM   2449 N N     . ILE   A 1 334 ? 64.92328  -2.64860  32.45343  1.000 89.24637  ? 334 ILE   A N     1 
ATOM   2450 C CA    . ILE   A 1 334 ? 65.32872  -2.79670  33.84324  1.000 95.98265  ? 334 ILE   A CA    1 
ATOM   2451 C C     . ILE   A 1 334 ? 66.72934  -3.40294  33.91487  1.000 103.08300 ? 334 ILE   A C     1 
ATOM   2452 O O     . ILE   A 1 334 ? 67.02315  -4.39315  33.22635  1.000 103.64202 ? 334 ILE   A O     1 
ATOM   2453 C CB    . ILE   A 1 334 ? 64.30137  -3.61911  34.62335  1.000 92.25025  ? 334 ILE   A CB    1 
ATOM   2454 C CG1   . ILE   A 1 334 ? 63.05763  -2.77523  34.77870  1.000 88.06991  ? 334 ILE   A CG1   1 
ATOM   2455 C CG2   . ILE   A 1 334 ? 64.80597  -3.89318  35.99867  1.000 97.48818  ? 334 ILE   A CG2   1 
ATOM   2456 C CD1   . ILE   A 1 334 ? 61.83444  -3.55040  34.98700  1.000 88.03398  ? 334 ILE   A CD1   1 
ATOM   2457 N N     . PRO   A 1 335 ? 67.63218  -2.82467  34.71293  1.000 104.93003 ? 335 PRO   A N     1 
ATOM   2458 C CA    . PRO   A 1 335 ? 68.99214  -3.37432  34.85163  1.000 105.67150 ? 335 PRO   A CA    1 
ATOM   2459 C C     . PRO   A 1 335 ? 69.01087  -4.82679  35.32724  1.000 112.49606 ? 335 PRO   A C     1 
ATOM   2460 O O     . PRO   A 1 335 ? 68.00130  -5.39594  35.76025  1.000 112.97803 ? 335 PRO   A O     1 
ATOM   2461 C CB    . PRO   A 1 335 ? 69.61915  -2.43839  35.89156  1.000 113.00620 ? 335 PRO   A CB    1 
ATOM   2462 C CG    . PRO   A 1 335 ? 68.94663  -1.12088  35.63265  1.000 108.10073 ? 335 PRO   A CG    1 
ATOM   2463 C CD    . PRO   A 1 335 ? 67.51491  -1.48198  35.32080  1.000 106.18276 ? 335 PRO   A CD    1 
ATOM   2464 N N     . ASP   A 1 336 ? 70.20179  -5.43538  35.24580  1.000 115.95704 ? 336 ASP   A N     1 
ATOM   2465 C CA    . ASP   A 1 336 ? 70.41175  -6.74346  35.87103  1.000 112.55366 ? 336 ASP   A CA    1 
ATOM   2466 C C     . ASP   A 1 336 ? 70.29851  -6.65000  37.38352  1.000 113.97806 ? 336 ASP   A C     1 
ATOM   2467 O O     . ASP   A 1 336 ? 69.61147  -7.46201  38.01071  1.000 113.40298 ? 336 ASP   A O     1 
ATOM   2468 C CB    . ASP   A 1 336 ? 71.77375  -7.32863  35.48511  1.000 116.21211 ? 336 ASP   A CB    1 
ATOM   2469 C CG    . ASP   A 1 336 ? 71.79868  -7.86805  34.06802  1.000 121.19747 ? 336 ASP   A CG    1 
ATOM   2470 O OD1   . ASP   A 1 336 ? 71.10513  -8.88017  33.80801  1.000 115.49625 ? 336 ASP   A OD1   1 
ATOM   2471 O OD2   . ASP   A 1 336 ? 72.52927  -7.29931  33.22320  1.000 126.63209 ? 336 ASP   A OD2   1 
ATOM   2472 N N     . ASP   A 1 337 ? 70.98275  -5.68095  37.99577  1.000 115.48121 ? 337 ASP   A N     1 
ATOM   2473 C CA    . ASP   A 1 337 ? 70.84656  -5.51255  39.44039  1.000 120.33593 ? 337 ASP   A CA    1 
ATOM   2474 C C     . ASP   A 1 337 ? 69.39682  -5.23267  39.80651  1.000 121.35308 ? 337 ASP   A C     1 
ATOM   2475 O O     . ASP   A 1 337 ? 68.81277  -5.90928  40.66703  1.000 117.58777 ? 337 ASP   A O     1 
ATOM   2476 C CB    . ASP   A 1 337 ? 71.76229  -4.38660  39.94216  1.000 129.08866 ? 337 ASP   A CB    1 
ATOM   2477 C CG    . ASP   A 1 337 ? 71.39046  -3.90094  41.35340  1.000 141.02866 ? 337 ASP   A CG    1 
ATOM   2478 O OD1   . ASP   A 1 337 ? 71.36176  -4.72386  42.29792  1.000 146.44866 ? 337 ASP   A OD1   1 
ATOM   2479 O OD2   . ASP   A 1 337 ? 71.17317  -2.68178  41.53021  1.000 147.10866 ? 337 ASP   A OD2   1 
ATOM   2480 N N     . ALA   A 1 338 ? 68.79399  -4.24809  39.13215  1.000 119.71941 ? 338 ALA   A N     1 
ATOM   2481 C CA    . ALA   A 1 338 ? 67.43894  -3.81950  39.46487  1.000 114.17643 ? 338 ALA   A CA    1 
ATOM   2482 C C     . ALA   A 1 338 ? 66.48484  -5.00669  39.51106  1.000 109.05345 ? 338 ALA   A C     1 
ATOM   2483 O O     . ALA   A 1 338 ? 65.71564  -5.16603  40.46562  1.000 108.41902 ? 338 ALA   A O     1 
ATOM   2484 C CB    . ALA   A 1 338 ? 66.97020  -2.76220  38.46019  1.000 108.63617 ? 338 ALA   A CB    1 
ATOM   2485 N N     . ALA   A 1 339 ? 66.54359  -5.87130  38.49692  1.000 108.29922 ? 339 ALA   A N     1 
ATOM   2486 C CA    . ALA   A 1 339 ? 65.73642  -7.08859  38.51231  1.000 109.02303 ? 339 ALA   A CA    1 
ATOM   2487 C C     . ALA   A 1 339 ? 65.84645  -7.80996  39.85083  1.000 111.59768 ? 339 ALA   A C     1 
ATOM   2488 O O     . ALA   A 1 339 ? 64.83960  -8.08987  40.51540  1.000 108.55175 ? 339 ALA   A O     1 
ATOM   2489 C CB    . ALA   A 1 339 ? 66.17190  -8.00470  37.36594  1.000 103.30448 ? 339 ALA   A CB    1 
ATOM   2490 N N     . GLU   A 1 340 ? 67.08084  -8.09357  40.27048  1.000 112.80709 ? 340 GLU   A N     1 
ATOM   2491 C CA    . GLU   A 1 340 ? 67.31782  -8.87969  41.47682  1.000 103.94339 ? 340 GLU   A CA    1 
ATOM   2492 C C     . GLU   A 1 340 ? 66.70613  -8.19238  42.68541  1.000 107.54082 ? 340 GLU   A C     1 
ATOM   2493 O O     . GLU   A 1 340 ? 66.06943  -8.83047  43.53310  1.000 107.02084 ? 340 GLU   A O     1 
ATOM   2494 C CB    . GLU   A 1 340 ? 68.81708  -9.03903  41.67052  1.000 104.10933 ? 340 GLU   A CB    1 
ATOM   2495 C CG    . GLU   A 1 340 ? 69.54595  -9.50426  40.40717  1.000 110.01699 ? 340 GLU   A CG    1 
ATOM   2496 C CD    . GLU   A 1 340 ? 69.53866  -11.00478 40.16296  1.000 108.48877 ? 340 GLU   A CD    1 
ATOM   2497 O OE1   . GLU   A 1 340 ? 68.92230  -11.75983 40.95047  1.000 106.74191 ? 340 GLU   A OE1   1 
ATOM   2498 O OE2   . GLU   A 1 340 ? 70.18336  -11.41942 39.17184  1.000 101.44056 ? 340 GLU   A OE2   1 
ATOM   2499 N N     . GLU   A 1 341 ? 66.92491  -6.87823  42.78246  1.000 113.26271 ? 341 GLU   A N     1 
ATOM   2500 C CA    . GLU   A 1 341 ? 66.33124  -6.07170  43.83947  1.000 115.77104 ? 341 GLU   A CA    1 
ATOM   2501 C C     . GLU   A 1 341 ? 64.81316  -6.16133  43.81032  1.000 111.64482 ? 341 GLU   A C     1 
ATOM   2502 O O     . GLU   A 1 341 ? 64.15698  -6.15643  44.86240  1.000 107.92172 ? 341 GLU   A O     1 
ATOM   2503 C CB    . GLU   A 1 341 ? 66.78567  -4.61882  43.67793  1.000 115.02237 ? 341 GLU   A CB    1 
ATOM   2504 C CG    . GLU   A 1 341 ? 68.09979  -4.31716  44.34865  1.000 121.24828 ? 341 GLU   A CG    1 
ATOM   2505 C CD    . GLU   A 1 341 ? 67.94879  -4.16338  45.85069  1.000 128.91629 ? 341 GLU   A CD    1 
ATOM   2506 O OE1   . GLU   A 1 341 ? 67.39680  -3.11812  46.26567  1.000 133.08547 ? 341 GLU   A OE1   1 
ATOM   2507 O OE2   . GLU   A 1 341 ? 68.35499  -5.08098  46.60745  1.000 120.18912 ? 341 GLU   A OE2   1 
ATOM   2508 N N     . VAL   A 1 342 ? 64.24272  -6.23325  42.60801  1.000 111.11161 ? 342 VAL   A N     1 
ATOM   2509 C CA    . VAL   A 1 342 ? 62.80461  -6.32181  42.40508  1.000 109.13309 ? 342 VAL   A CA    1 
ATOM   2510 C C     . VAL   A 1 342 ? 62.25685  -7.57856  43.05645  1.000 108.28039 ? 342 VAL   A C     1 
ATOM   2511 O O     . VAL   A 1 342 ? 61.47627  -7.51257  44.01662  1.000 105.27589 ? 342 VAL   A O     1 
ATOM   2512 C CB    . VAL   A 1 342 ? 62.45641  -6.32583  40.91175  1.000 108.14103 ? 342 VAL   A CB    1 
ATOM   2513 C CG1   . VAL   A 1 342 ? 61.02700  -6.80232  40.74835  1.000 98.70552  ? 342 VAL   A CG1   1 
ATOM   2514 C CG2   . VAL   A 1 342 ? 62.68064  -4.94292  40.30526  1.000 104.60882 ? 342 VAL   A CG2   1 
ATOM   2515 N N     . PHE   A 1 343 ? 62.65729  -8.73522  42.51233  1.000 104.09221 ? 343 PHE   A N     1 
ATOM   2516 C CA    . PHE   A 1 343 ? 62.13006  -10.00700 42.98807  1.000 106.73007 ? 343 PHE   A CA    1 
ATOM   2517 C C     . PHE   A 1 343 ? 62.48693  -10.22775 44.45881  1.000 105.00713 ? 343 PHE   A C     1 
ATOM   2518 O O     . PHE   A 1 343 ? 61.68101  -10.76172 45.23811  1.000 96.68459  ? 343 PHE   A O     1 
ATOM   2519 C CB    . PHE   A 1 343 ? 62.65080  -11.13109 42.09879  1.000 109.48866 ? 343 PHE   A CB    1 
ATOM   2520 C CG    . PHE   A 1 343 ? 61.98294  -11.18653 40.73113  1.000 111.23921 ? 343 PHE   A CG    1 
ATOM   2521 C CD1   . PHE   A 1 343 ? 60.73047  -11.78671 40.56329  1.000 104.74916 ? 343 PHE   A CD1   1 
ATOM   2522 C CD2   . PHE   A 1 343 ? 62.62050  -10.65130 39.60957  1.000 107.69594 ? 343 PHE   A CD2   1 
ATOM   2523 C CE1   . PHE   A 1 343 ? 60.11887  -11.83781 39.30578  1.000 94.89846  ? 343 PHE   A CE1   1 
ATOM   2524 C CE2   . PHE   A 1 343 ? 62.02143  -10.70491 38.35200  1.000 100.20866 ? 343 PHE   A CE2   1 
ATOM   2525 C CZ    . PHE   A 1 343 ? 60.77543  -11.29776 38.19970  1.000 101.80866 ? 343 PHE   A CZ    1 
ATOM   2526 N N     . LYS   A 1 344 ? 63.68928  -9.80083  44.85476  1.000 104.41840 ? 344 LYS   A N     1 
ATOM   2527 C CA    . LYS   A 1 344 ? 63.97879  -9.60872  46.26644  1.000 100.51619 ? 344 LYS   A CA    1 
ATOM   2528 C C     . LYS   A 1 344 ? 62.84785  -8.83527  46.94467  1.000 98.90140  ? 344 LYS   A C     1 
ATOM   2529 O O     . LYS   A 1 344 ? 62.26358  -9.30683  47.92118  1.000 99.49315  ? 344 LYS   A O     1 
ATOM   2530 C CB    . LYS   A 1 344 ? 65.33109  -8.90742  46.43557  1.000 100.30866 ? 344 LYS   A CB    1 
ATOM   2531 N N     . TYR   A 1 345 ? 62.49119  -7.66085  46.41944  1.000 100.05237 ? 345 TYR   A N     1 
ATOM   2532 C CA    . TYR   A 1 345 ? 61.38158  -6.91438  47.00813  1.000 98.04562  ? 345 TYR   A CA    1 
ATOM   2533 C C     . TYR   A 1 345 ? 60.14116  -7.78925  47.13035  1.000 98.18067  ? 345 TYR   A C     1 
ATOM   2534 O O     . TYR   A 1 345 ? 59.48150  -7.82058  48.17890  1.000 94.61247  ? 345 TYR   A O     1 
ATOM   2535 C CB    . TYR   A 1 345 ? 61.04993  -5.68116  46.17160  1.000 97.19309  ? 345 TYR   A CB    1 
ATOM   2536 C CG    . TYR   A 1 345 ? 59.91927  -4.83655  46.73741  1.000 94.36008  ? 345 TYR   A CG    1 
ATOM   2537 C CD1   . TYR   A 1 345 ? 58.62075  -5.32367  46.79376  1.000 98.19712  ? 345 TYR   A CD1   1 
ATOM   2538 C CD2   . TYR   A 1 345 ? 60.13370  -3.53368  47.13493  1.000 89.24122  ? 345 TYR   A CD2   1 
ATOM   2539 C CE1   . TYR   A 1 345 ? 57.59330  -4.56274  47.29393  1.000 95.95121  ? 345 TYR   A CE1   1 
ATOM   2540 C CE2   . TYR   A 1 345 ? 59.11200  -2.76008  47.61958  1.000 88.22226  ? 345 TYR   A CE2   1 
ATOM   2541 C CZ    . TYR   A 1 345 ? 57.84068  -3.27892  47.69879  1.000 90.98983  ? 345 TYR   A CZ    1 
ATOM   2542 O OH    . TYR   A 1 345 ? 56.79694  -2.52355  48.18103  1.000 92.72132  ? 345 TYR   A OH    1 
ATOM   2543 N N     . LEU   A 1 346 ? 59.78295  -8.47438  46.04388  1.000 96.55690  ? 346 LEU   A N     1 
ATOM   2544 C CA    . LEU   A 1 346 ? 58.50003  -9.17006  46.00458  1.000 102.93483 ? 346 LEU   A CA    1 
ATOM   2545 C C     . LEU   A 1 346 ? 58.42027  -10.25701 47.05855  1.000 100.33099 ? 346 LEU   A C     1 
ATOM   2546 O O     . LEU   A 1 346 ? 57.37466  -10.44666 47.69813  1.000 97.47631  ? 346 LEU   A O     1 
ATOM   2547 C CB    . LEU   A 1 346 ? 58.25559  -9.75882  44.61957  1.000 101.52545 ? 346 LEU   A CB    1 
ATOM   2548 C CG    . LEU   A 1 346 ? 57.56042  -8.81581  43.64879  1.000 94.64039  ? 346 LEU   A CG    1 
ATOM   2549 C CD1   . LEU   A 1 346 ? 57.60352  -9.45052  42.31246  1.000 87.28560  ? 346 LEU   A CD1   1 
ATOM   2550 C CD2   . LEU   A 1 346 ? 56.11600  -8.60094  44.07823  1.000 91.54154  ? 346 LEU   A CD2   1 
ATOM   2551 N N     . ALA   A 1 347 ? 59.51701  -10.98253 47.24706  1.000 99.34650  ? 347 ALA   A N     1 
ATOM   2552 C CA    . ALA   A 1 347 ? 59.51043  -12.10101 48.17335  1.000 103.99794 ? 347 ALA   A CA    1 
ATOM   2553 C C     . ALA   A 1 347 ? 59.33409  -11.65370 49.62569  1.000 105.26359 ? 347 ALA   A C     1 
ATOM   2554 O O     . ALA   A 1 347 ? 58.80310  -12.41506 50.44576  1.000 103.56663 ? 347 ALA   A O     1 
ATOM   2555 C CB    . ALA   A 1 347 ? 60.80001  -12.90639 48.00564  1.000 102.35993 ? 347 ALA   A CB    1 
ATOM   2556 N N     . THR   A 1 348 ? 59.73440  -10.42949 49.96677  1.000 104.13866 ? 348 THR   A N     1 
ATOM   2557 C CA    . THR   A 1 348 ? 59.94819  -10.08736 51.36576  1.000 108.11975 ? 348 THR   A CA    1 
ATOM   2558 C C     . THR   A 1 348 ? 59.13547  -8.91580  51.88716  1.000 103.91089 ? 348 THR   A C     1 
ATOM   2559 O O     . THR   A 1 348 ? 59.24225  -8.61334  53.08311  1.000 104.92273 ? 348 THR   A O     1 
ATOM   2560 C CB    . THR   A 1 348 ? 61.43596  -9.80593  51.61685  1.000 115.41866 ? 348 THR   A CB    1 
ATOM   2561 O OG1   . THR   A 1 348 ? 61.90342  -8.79289  50.71084  1.000 107.97744 ? 348 THR   A OG1   1 
ATOM   2562 C CG2   . THR   A 1 348 ? 62.24507  -11.09399 51.44977  1.000 118.73866 ? 348 THR   A CG2   1 
ATOM   2563 N N     . THR   A 1 349 ? 58.34077  -8.24632  51.05106  1.000 98.45470  ? 349 THR   A N     1 
ATOM   2564 C CA    . THR   A 1 349 ? 57.43472  -7.21144  51.52852  1.000 94.38435  ? 349 THR   A CA    1 
ATOM   2565 C C     . THR   A 1 349 ? 56.10006  -7.84550  51.88355  1.000 91.38703  ? 349 THR   A C     1 
ATOM   2566 O O     . THR   A 1 349 ? 55.53276  -8.59607  51.07943  1.000 94.20948  ? 349 THR   A O     1 
ATOM   2567 C CB    . THR   A 1 349 ? 57.21557  -6.11820  50.48219  1.000 93.56071  ? 349 THR   A CB    1 
ATOM   2568 O OG1   . THR   A 1 349 ? 58.46413  -5.72494  49.90563  1.000 86.47542  ? 349 THR   A OG1   1 
ATOM   2569 C CG2   . THR   A 1 349 ? 56.54958  -4.91026  51.11731  1.000 91.78176  ? 349 THR   A CG2   1 
ATOM   2570 N N     . LYS   A 1 350 ? 55.60526  -7.55966  53.08225  1.000 81.84035  ? 350 LYS   A N     1 
ATOM   2571 C CA    . LYS   A 1 350 ? 54.22400  -7.89339  53.35703  1.000 84.09078  ? 350 LYS   A CA    1 
ATOM   2572 C C     . LYS   A 1 350 ? 53.37422  -7.19323  52.31435  1.000 97.16234  ? 350 LYS   A C     1 
ATOM   2573 O O     . LYS   A 1 350 ? 53.49635  -5.98030  52.10419  1.000 91.41546  ? 350 LYS   A O     1 
ATOM   2574 C CB    . LYS   A 1 350 ? 53.81054  -7.47154  54.76179  1.000 88.50866  ? 350 LYS   A CB    1 
ATOM   2575 N N     . ASN   A 1 351 ? 52.54269  -7.97295  51.63012  1.000 99.70255  ? 351 ASN   A N     1 
ATOM   2576 C CA    . ASN   A 1 351 ? 51.72753  -7.47038  50.53594  1.000 92.54906  ? 351 ASN   A CA    1 
ATOM   2577 C C     . ASN   A 1 351 ? 50.23772  -7.35550  50.85644  1.000 88.36204  ? 351 ASN   A C     1 
ATOM   2578 O O     . ASN   A 1 351 ? 49.57371  -6.48202  50.29841  1.000 89.79835  ? 351 ASN   A O     1 
ATOM   2579 C CB    . ASN   A 1 351 ? 51.94667  -8.33440  49.28551  1.000 91.16921  ? 351 ASN   A CB    1 
ATOM   2580 C CG    . ASN   A 1 351 ? 51.50670  -9.77880  49.46924  1.000 91.95514  ? 351 ASN   A CG    1 
ATOM   2581 O OD1   . ASN   A 1 351 ? 50.45677  -10.04480 50.06191  1.000 98.15529  ? 351 ASN   A OD1   1 
ATOM   2582 N ND2   . ASN   A 1 351 ? 52.28603  -10.71860 48.92272  1.000 90.65552  ? 351 ASN   A ND2   1 
ATOM   2583 N N     . GLY   A 1 352 ? 49.68693  -8.19335  51.73665  1.000 80.11393  ? 352 GLY   A N     1 
ATOM   2584 C CA    . GLY   A 1 352 ? 48.30446  -8.02467  52.12474  1.000 79.35241  ? 352 GLY   A CA    1 
ATOM   2585 C C     . GLY   A 1 352 ? 47.29850  -8.59468  51.15788  1.000 85.70158  ? 352 GLY   A C     1 
ATOM   2586 O O     . GLY   A 1 352 ? 46.11417  -8.24507  51.22661  1.000 85.71474  ? 352 GLY   A O     1 
ATOM   2587 N N     . THR   A 1 353 ? 47.72567  -9.49675  50.27803  1.000 86.90479  ? 353 THR   A N     1 
ATOM   2588 C CA    . THR   A 1 353 ? 46.92185  -9.96133  49.15294  1.000 87.64083  ? 353 THR   A CA    1 
ATOM   2589 C C     . THR   A 1 353 ? 46.54320  -11.41890 49.33829  1.000 88.91303  ? 353 THR   A C     1 
ATOM   2590 O O     . THR   A 1 353 ? 47.36264  -12.21397 49.80303  1.000 89.97904  ? 353 THR   A O     1 
ATOM   2591 C CB    . THR   A 1 353 ? 47.69262  -9.85006  47.84007  1.000 84.91197  ? 353 THR   A CB    1 
ATOM   2592 O OG1   . THR   A 1 353 ? 48.64013  -10.92096 47.76705  1.000 82.97387  ? 353 THR   A OG1   1 
ATOM   2593 C CG2   . THR   A 1 353 ? 48.43734  -8.53405  47.75495  1.000 86.35379  ? 353 THR   A CG2   1 
ATOM   2594 N N     . ASP   A 1 354 ? 45.31416  -11.76959 48.93838  1.000 86.63641  ? 354 ASP   A N     1 
ATOM   2595 C CA    . ASP   A 1 354 ? 44.98906  -13.17920 48.76184  1.000 84.38535  ? 354 ASP   A CA    1 
ATOM   2596 C C     . ASP   A 1 354 ? 45.40871  -13.68089 47.39420  1.000 83.82154  ? 354 ASP   A C     1 
ATOM   2597 O O     . ASP   A 1 354 ? 45.35354  -14.89142 47.14861  1.000 84.03159  ? 354 ASP   A O     1 
ATOM   2598 C CB    . ASP   A 1 354 ? 43.49172  -13.45340 48.95390  1.000 87.59492  ? 354 ASP   A CB    1 
ATOM   2599 C CG    . ASP   A 1 354 ? 42.64721  -12.93783 47.80234  1.000 93.92362  ? 354 ASP   A CG    1 
ATOM   2600 O OD1   . ASP   A 1 354 ? 43.16046  -12.09438 47.02678  1.000 96.30866  ? 354 ASP   A OD1   1 
ATOM   2601 O OD2   . ASP   A 1 354 ? 41.46899  -13.37845 47.66838  1.000 92.53637  ? 354 ASP   A OD2   1 
ATOM   2602 N N     . LEU   A 1 355 ? 45.77218  -12.77104 46.49162  1.000 86.76909  ? 355 LEU   A N     1 
ATOM   2603 C CA    . LEU   A 1 355 ? 46.36522  -13.10359 45.20270  1.000 92.71807  ? 355 LEU   A CA    1 
ATOM   2604 C C     . LEU   A 1 355 ? 46.93706  -11.84658 44.57175  1.000 87.89586  ? 355 LEU   A C     1 
ATOM   2605 O O     . LEU   A 1 355 ? 46.29955  -10.78371 44.58865  1.000 88.54866  ? 355 LEU   A O     1 
ATOM   2606 C CB    . LEU   A 1 355 ? 45.37141  -13.75044 44.22554  1.000 87.53248  ? 355 LEU   A CB    1 
ATOM   2607 C CG    . LEU   A 1 355 ? 46.09538  -13.96855 42.88241  1.000 88.20866  ? 355 LEU   A CG    1 
ATOM   2608 C CD1   . LEU   A 1 355 ? 47.24154  -14.98648 43.00114  1.000 87.05642  ? 355 LEU   A CD1   1 
ATOM   2609 C CD2   . LEU   A 1 355 ? 45.12131  -14.36530 41.79107  1.000 83.94866  ? 355 LEU   A CD2   1 
ATOM   2610 N N     . TYR   A 1 356 ? 48.13341  -11.98057 44.01327  1.000 79.17655  ? 356 TYR   A N     1 
ATOM   2611 C CA    . TYR   A 1 356 ? 48.75928  -10.90163 43.27994  1.000 80.34355  ? 356 TYR   A CA    1 
ATOM   2612 C C     . TYR   A 1 356 ? 49.38365  -11.48595 42.01549  1.000 86.74352  ? 356 TYR   A C     1 
ATOM   2613 O O     . TYR   A 1 356 ? 49.69386  -12.68652 41.94450  1.000 83.86262  ? 356 TYR   A O     1 
ATOM   2614 C CB    . TYR   A 1 356 ? 49.78360  -10.13048 44.16213  1.000 81.11039  ? 356 TYR   A CB    1 
ATOM   2615 C CG    . TYR   A 1 356 ? 51.20885  -10.68996 44.20192  1.000 90.58214  ? 356 TYR   A CG    1 
ATOM   2616 C CD1   . TYR   A 1 356 ? 52.08020  -10.51486 43.13093  1.000 88.61711  ? 356 TYR   A CD1   1 
ATOM   2617 C CD2   . TYR   A 1 356 ? 51.69408  -11.36383 45.31990  1.000 93.92282  ? 356 TYR   A CD2   1 
ATOM   2618 C CE1   . TYR   A 1 356 ? 53.36788  -11.01189 43.15711  1.000 88.01379  ? 356 TYR   A CE1   1 
ATOM   2619 C CE2   . TYR   A 1 356 ? 52.99424  -11.87142 45.34991  1.000 91.76913  ? 356 TYR   A CE2   1 
ATOM   2620 C CZ    . TYR   A 1 356 ? 53.82257  -11.68471 44.26169  1.000 91.07438  ? 356 TYR   A CZ    1 
ATOM   2621 O OH    . TYR   A 1 356 ? 55.11142  -12.16846 44.25805  1.000 92.91223  ? 356 TYR   A OH    1 
ATOM   2622 N N     . ALA   A 1 357 ? 49.51256  -10.62147 41.00226  1.000 86.25298  ? 357 ALA   A N     1 
ATOM   2623 C CA    . ALA   A 1 357 ? 50.20663  -10.92209 39.75757  1.000 82.71165  ? 357 ALA   A CA    1 
ATOM   2624 C C     . ALA   A 1 357 ? 50.88964  -9.65505  39.24083  1.000 76.54833  ? 357 ALA   A C     1 
ATOM   2625 O O     . ALA   A 1 357 ? 50.48890  -8.52980  39.56850  1.000 76.10306  ? 357 ALA   A O     1 
ATOM   2626 C CB    . ALA   A 1 357 ? 49.24365  -11.49514 38.70842  1.000 73.40572  ? 357 ALA   A CB    1 
ATOM   2627 N N     . VAL   A 1 358 ? 51.93271  -9.85187  38.42650  1.000 69.45303  ? 358 VAL   A N     1 
ATOM   2628 C CA    . VAL   A 1 358 ? 52.64966  -8.75872  37.76272  1.000 72.91851  ? 358 VAL   A CA    1 
ATOM   2629 C C     . VAL   A 1 358 ? 52.90125  -9.12132  36.29251  1.000 72.56820  ? 358 VAL   A C     1 
ATOM   2630 O O     . VAL   A 1 358 ? 53.72757  -9.99606  35.99183  1.000 66.77007  ? 358 VAL   A O     1 
ATOM   2631 C CB    . VAL   A 1 358 ? 53.96832  -8.42803  38.46497  1.000 68.84273  ? 358 VAL   A CB    1 
ATOM   2632 C CG1   . VAL   A 1 358 ? 54.68849  -7.33216  37.69585  1.000 73.54510  ? 358 VAL   A CG1   1 
ATOM   2633 C CG2   . VAL   A 1 358 ? 53.70355  -8.00160  39.88504  1.000 65.44279  ? 358 VAL   A CG2   1 
ATOM   2634 N N     . THR   A 1 359 ? 52.23527  -8.42169  35.37736  1.000 67.40486  ? 359 THR   A N     1 
ATOM   2635 C CA    . THR   A 1 359 ? 52.21920  -8.84382  33.98692  1.000 66.04164  ? 359 THR   A CA    1 
ATOM   2636 C C     . THR   A 1 359 ? 53.11760  -7.93055  33.14720  1.000 63.35124  ? 359 THR   A C     1 
ATOM   2637 O O     . THR   A 1 359 ? 53.18259  -6.71475  33.36601  1.000 62.09901  ? 359 THR   A O     1 
ATOM   2638 C CB    . THR   A 1 359 ? 50.77733  -8.86462  33.47009  1.000 64.47014  ? 359 THR   A CB    1 
ATOM   2639 O OG1   . THR   A 1 359 ? 49.90898  -9.33410  34.51441  1.000 61.13451  ? 359 THR   A OG1   1 
ATOM   2640 C CG2   . THR   A 1 359 ? 50.65903  -9.82293  32.30224  1.000 62.05267  ? 359 THR   A CG2   1 
ATOM   2641 N N     . PHE   A 1 360 ? 53.85358  -8.54072  32.22597  1.000 58.96019  ? 360 PHE   A N     1 
ATOM   2642 C CA    . PHE   A 1 360 ? 54.83391  -7.87853  31.36584  1.000 67.61218  ? 360 PHE   A CA    1 
ATOM   2643 C C     . PHE   A 1 360 ? 54.40189  -8.16207  29.93270  1.000 69.07197  ? 360 PHE   A C     1 
ATOM   2644 O O     . PHE   A 1 360 ? 54.81495  -9.15380  29.32371  1.000 70.98828  ? 360 PHE   A O     1 
ATOM   2645 C CB    . PHE   A 1 360 ? 56.31965  -8.38130  31.63776  1.000 73.04634  ? 360 PHE   A CB    1 
ATOM   2646 C CG    . PHE   A 1 360 ? 56.83929  -8.03377  33.01593  1.000 74.66707  ? 360 PHE   A CG    1 
ATOM   2647 C CD1   . PHE   A 1 360 ? 57.45143  -6.80835  33.24875  1.000 78.50602  ? 360 PHE   A CD1   1 
ATOM   2648 C CD2   . PHE   A 1 360 ? 56.70213  -8.90904  34.07942  1.000 73.62347  ? 360 PHE   A CD2   1 
ATOM   2649 C CE1   . PHE   A 1 360 ? 57.91517  -6.46103  34.51817  1.000 78.91521  ? 360 PHE   A CE1   1 
ATOM   2650 C CE2   . PHE   A 1 360 ? 57.16347  -8.55714  35.34805  1.000 70.89939  ? 360 PHE   A CE2   1 
ATOM   2651 C CZ    . PHE   A 1 360 ? 57.76808  -7.33493  35.56152  1.000 70.83935  ? 360 PHE   A CZ    1 
ATOM   2652 N N     . ALA   A 1 361 ? 53.54806  -7.30751  29.38608  1.000 65.41608  ? 361 ALA   A N     1 
ATOM   2653 C CA    . ALA   A 1 361 ? 53.01367  -7.54121  28.05661  1.000 63.27654  ? 361 ALA   A CA    1 
ATOM   2654 C C     . ALA   A 1 361 ? 53.90233  -6.85442  27.03783  1.000 61.63786  ? 361 ALA   A C     1 
ATOM   2655 O O     . ALA   A 1 361 ? 54.19235  -5.66209  27.14774  1.000 62.81202  ? 361 ALA   A O     1 
ATOM   2656 C CB    . ALA   A 1 361 ? 51.57599  -7.03995  27.95290  1.000 67.93777  ? 361 ALA   A CB    1 
ATOM   2657 N N     . ALA   A 1 362 ? 54.34988  -7.61262  26.06135  1.000 58.07497  ? 362 ALA   A N     1 
ATOM   2658 C CA    . ALA   A 1 362 ? 55.24347  -7.05822  25.06953  1.000 61.73168  ? 362 ALA   A CA    1 
ATOM   2659 C C     . ALA   A 1 362 ? 54.43683  -6.28335  24.06253  1.000 69.45997  ? 362 ALA   A C     1 
ATOM   2660 O O     . ALA   A 1 362 ? 53.28626  -6.62007  23.77295  1.000 70.39871  ? 362 ALA   A O     1 
ATOM   2661 C CB    . ALA   A 1 362 ? 56.00942  -8.15616  24.35220  1.000 71.32665  ? 362 ALA   A CB    1 
ATOM   2662 N N     . LEU   A 1 363 ? 55.07254  -5.28607  23.46136  1.000 69.74933  ? 363 LEU   A N     1 
ATOM   2663 C CA    . LEU   A 1 363 ? 54.24660  -4.24200  22.90403  1.000 63.30999  ? 363 LEU   A CA    1 
ATOM   2664 C C     . LEU   A 1 363 ? 54.98408  -3.49044  21.80429  1.000 67.83106  ? 363 LEU   A C     1 
ATOM   2665 O O     . LEU   A 1 363 ? 54.89872  -2.25353  21.71550  1.000 72.49319  ? 363 LEU   A O     1 
ATOM   2666 C CB    . LEU   A 1 363 ? 53.82205  -3.32982  24.05153  1.000 59.36432  ? 363 LEU   A CB    1 
ATOM   2667 C CG    . LEU   A 1 363 ? 52.94526  -2.16872  23.68983  1.000 52.62851  ? 363 LEU   A CG    1 
ATOM   2668 C CD1   . LEU   A 1 363 ? 51.68782  -2.77083  23.16295  1.000 56.41866  ? 363 LEU   A CD1   1 
ATOM   2669 C CD2   . LEU   A 1 363 ? 52.71115  -1.41091  24.93687  1.000 62.30704  ? 363 LEU   A CD2   1 
ATOM   2670 N N     . GLY   A 1 364 ? 55.70510  -4.21952  20.94928  1.000 63.63705  ? 364 GLY   A N     1 
ATOM   2671 C CA    . GLY   A 1 364 ? 56.42305  -3.52878  19.88884  1.000 61.81391  ? 364 GLY   A CA    1 
ATOM   2672 C C     . GLY   A 1 364 ? 55.75031  -3.69933  18.55121  1.000 59.63035  ? 364 GLY   A C     1 
ATOM   2673 O O     . GLY   A 1 364 ? 54.55111  -3.47690  18.42045  1.000 64.41407  ? 364 GLY   A O     1 
ATOM   2674 N N     . GLY   A 1 365 ? 56.51022  -4.08800  17.54725  1.000 61.74327  ? 365 GLY   A N     1 
ATOM   2675 C CA    . GLY   A 1 365 ? 55.90262  -4.49460  16.29014  1.000 61.86519  ? 365 GLY   A CA    1 
ATOM   2676 C C     . GLY   A 1 365 ? 55.04101  -3.40905  15.68018  1.000 66.23706  ? 365 GLY   A C     1 
ATOM   2677 O O     . GLY   A 1 365 ? 55.41326  -2.22676  15.62138  1.000 67.00801  ? 365 GLY   A O     1 
ATOM   2678 N N     . ALA   A 1 366 ? 53.86051  -3.82969  15.21765  1.000 64.38132  ? 366 ALA   A N     1 
ATOM   2679 C CA    . ALA   A 1 366 ? 52.92581  -2.93337  14.55089  1.000 59.71429  ? 366 ALA   A CA    1 
ATOM   2680 C C     . ALA   A 1 366 ? 52.49200  -1.75974  15.42263  1.000 62.06380  ? 366 ALA   A C     1 
ATOM   2681 O O     . ALA   A 1 366 ? 52.03216  -0.75392  14.88414  1.000 71.58523  ? 366 ALA   A O     1 
ATOM   2682 C CB    . ALA   A 1 366 ? 51.70184  -3.71136  14.08209  1.000 52.62630  ? 366 ALA   A CB    1 
ATOM   2683 N N     . VAL   A 1 367 ? 52.61141  -1.84279  16.74602  1.000 56.66211  ? 367 VAL   A N     1 
ATOM   2684 C CA    . VAL   A 1 367 ? 52.23772  -0.68762  17.55753  1.000 60.90754  ? 367 VAL   A CA    1 
ATOM   2685 C C     . VAL   A 1 367 ? 53.12593  0.51351   17.23389  1.000 70.30289  ? 367 VAL   A C     1 
ATOM   2686 O O     . VAL   A 1 367 ? 52.66700  1.66696   17.26787  1.000 63.82170  ? 367 VAL   A O     1 
ATOM   2687 C CB    . VAL   A 1 367 ? 52.29916  -1.02037  19.05364  1.000 60.66751  ? 367 VAL   A CB    1 
ATOM   2688 C CG1   . VAL   A 1 367 ? 52.02534  0.25730   19.85915  1.000 57.51958  ? 367 VAL   A CG1   1 
ATOM   2689 C CG2   . VAL   A 1 367 ? 51.33183  -2.12911  19.38822  1.000 57.38239  ? 367 VAL   A CG2   1 
ATOM   2690 N N     . ARG   A 1 368 ? 54.42330  0.26264   16.95378  1.000 73.36638  ? 368 ARG   A N     1 
ATOM   2691 C CA    . ARG   A 1 368 ? 55.37408  1.32328   16.63984  1.000 66.82428  ? 368 ARG   A CA    1 
ATOM   2692 C C     . ARG   A 1 368 ? 55.07070  1.96412   15.29621  1.000 65.42799  ? 368 ARG   A C     1 
ATOM   2693 O O     . ARG   A 1 368 ? 55.54947  3.07356   15.02656  1.000 61.69773  ? 368 ARG   A O     1 
ATOM   2694 C CB    . ARG   A 1 368 ? 56.80929  0.78279   16.66204  1.000 72.44866  ? 368 ARG   A CB    1 
ATOM   2695 N N     . ASP   A 1 369 ? 54.24750  1.31293   14.46472  1.000 61.78543  ? 369 ASP   A N     1 
ATOM   2696 C CA    . ASP   A 1 369 ? 53.96814  1.80154   13.10744  1.000 68.63177  ? 369 ASP   A CA    1 
ATOM   2697 C C     . ASP   A 1 369 ? 53.17332  3.10874   13.05565  1.000 72.42395  ? 369 ASP   A C     1 
ATOM   2698 O O     . ASP   A 1 369 ? 52.79427  3.51658   11.94553  1.000 68.56968  ? 369 ASP   A O     1 
ATOM   2699 C CB    . ASP   A 1 369 ? 53.18685  0.77852   12.27010  1.000 72.54361  ? 369 ASP   A CB    1 
ATOM   2700 C CG    . ASP   A 1 369 ? 53.95865  -0.52080  11.99998  1.000 95.72882  ? 369 ASP   A CG    1 
ATOM   2701 O OD1   . ASP   A 1 369 ? 55.17371  -0.58754  12.31087  1.000 114.80866 ? 369 ASP   A OD1   1 
ATOM   2702 O OD2   . ASP   A 1 369 ? 53.33940  -1.49083  11.46384  1.000 94.61618  ? 369 ASP   A OD2   1 
ATOM   2703 N N     . VAL   A 1 370 ? 52.87187  3.76305   14.17049  1.000 71.81030  ? 370 VAL   A N     1 
ATOM   2704 C CA    . VAL   A 1 370 ? 52.03385  4.95404   14.14545  1.000 62.22506  ? 370 VAL   A CA    1 
ATOM   2705 C C     . VAL   A 1 370 ? 52.68507  5.99806   15.03756  1.000 59.47591  ? 370 VAL   A C     1 
ATOM   2706 O O     . VAL   A 1 370 ? 53.28674  5.67593   16.07020  1.000 59.90671  ? 370 VAL   A O     1 
ATOM   2707 C CB    . VAL   A 1 370 ? 50.57748  4.65301   14.58163  1.000 58.56391  ? 370 VAL   A CB    1 
ATOM   2708 C CG1   . VAL   A 1 370 ? 49.75029  5.89791   14.54497  1.000 62.21858  ? 370 VAL   A CG1   1 
ATOM   2709 C CG2   . VAL   A 1 370 ? 49.94548  3.59709   13.69350  1.000 53.60153  ? 370 VAL   A CG2   1 
ATOM   2710 N N     . SER   A 1 371 ? 52.59082  7.24776   14.61369  1.000 63.06547  ? 371 SER   A N     1 
ATOM   2711 C CA    . SER   A 1 371 ? 53.31194  8.33108   15.25893  1.000 61.01593  ? 371 SER   A CA    1 
ATOM   2712 C C     . SER   A 1 371 ? 52.89456  8.47685   16.71848  1.000 65.44665  ? 371 SER   A C     1 
ATOM   2713 O O     . SER   A 1 371 ? 51.72744  8.28548   17.08028  1.000 67.41777  ? 371 SER   A O     1 
ATOM   2714 C CB    . SER   A 1 371 ? 53.04380  9.61749   14.49169  1.000 67.14981  ? 371 SER   A CB    1 
ATOM   2715 O OG    . SER   A 1 371 ? 53.39407  10.74701  15.24703  1.000 75.13849  ? 371 SER   A OG    1 
ATOM   2716 N N     . ALA   A 1 372 ? 53.85942  8.83258   17.57048  1.000 64.80379  ? 372 ALA   A N     1 
ATOM   2717 C CA    . ALA   A 1 372 ? 53.51631  9.09103   18.96978  1.000 66.14624  ? 372 ALA   A CA    1 
ATOM   2718 C C     . ALA   A 1 372 ? 52.46121  10.19569  19.11148  1.000 67.31793  ? 372 ALA   A C     1 
ATOM   2719 O O     . ALA   A 1 372 ? 51.69462  10.21171  20.08126  1.000 68.68772  ? 372 ALA   A O     1 
ATOM   2720 C CB    . ALA   A 1 372 ? 54.77118  9.45401   19.75040  1.000 67.50529  ? 372 ALA   A CB    1 
ATOM   2721 N N     . SER   A 1 373 ? 52.39505  11.10925  18.14778  1.000 65.97785  ? 373 SER   A N     1 
ATOM   2722 C CA    . SER   A 1 373 ? 51.54726  12.29078  18.19936  1.000 66.18511  ? 373 SER   A CA    1 
ATOM   2723 C C     . SER   A 1 373 ? 50.38288  12.22200  17.21798  1.000 66.30104  ? 373 SER   A C     1 
ATOM   2724 O O     . SER   A 1 373 ? 49.68039  13.23308  17.02583  1.000 69.23456  ? 373 SER   A O     1 
ATOM   2725 C CB    . SER   A 1 373 ? 52.38127  13.52842  17.89098  1.000 74.96370  ? 373 SER   A CB    1 
ATOM   2726 O OG    . SER   A 1 373 ? 52.92340  13.40394  16.57798  1.000 72.91409  ? 373 SER   A OG    1 
ATOM   2727 N N     . GLU   A 1 374 ? 50.18113  11.07082  16.56750  1.000 63.28576  ? 374 GLU   A N     1 
ATOM   2728 C CA    . GLU   A 1 374 ? 49.11190  10.92304  15.59228  1.000 64.72189  ? 374 GLU   A CA    1 
ATOM   2729 C C     . GLU   A 1 374 ? 47.79215  10.51661  16.22266  1.000 67.71150  ? 374 GLU   A C     1 
ATOM   2730 O O     . GLU   A 1 374 ? 46.71909  10.76789  15.63575  1.000 65.85458  ? 374 GLU   A O     1 
ATOM   2731 C CB    . GLU   A 1 374 ? 49.49192  9.88481   14.55568  1.000 66.67324  ? 374 GLU   A CB    1 
ATOM   2732 C CG    . GLU   A 1 374 ? 48.73796  10.05911  13.26545  1.000 79.72151  ? 374 GLU   A CG    1 
ATOM   2733 C CD    . GLU   A 1 374 ? 49.06079  8.93776   12.34356  1.000 90.69664  ? 374 GLU   A CD    1 
ATOM   2734 O OE1   . GLU   A 1 374 ? 50.28807  8.67426   12.21475  1.000 80.79640  ? 374 GLU   A OE1   1 
ATOM   2735 O OE2   . GLU   A 1 374 ? 48.11177  8.32006   11.78064  1.000 87.46866  ? 374 GLU   A OE2   1 
ATOM   2736 N N     . THR   A 1 375 ? 47.87543  9.86145   17.38308  1.000 64.69151  ? 375 THR   A N     1 
ATOM   2737 C CA    . THR   A 1 375 ? 46.79888  9.51575   18.31070  1.000 58.72865  ? 375 THR   A CA    1 
ATOM   2738 C C     . THR   A 1 375 ? 47.04127  10.18234  19.66084  1.000 61.39007  ? 375 THR   A C     1 
ATOM   2739 O O     . THR   A 1 375 ? 48.15315  10.63990  19.96648  1.000 64.35592  ? 375 THR   A O     1 
ATOM   2740 C CB    . THR   A 1 375 ? 46.70622  7.99442   18.50652  1.000 59.42786  ? 375 THR   A CB    1 
ATOM   2741 O OG1   . THR   A 1 375 ? 48.02050  7.45050   18.78160  1.000 65.67956  ? 375 THR   A OG1   1 
ATOM   2742 C CG2   . THR   A 1 375 ? 46.06272  7.32576   17.27273  1.000 57.59065  ? 375 THR   A CG2   1 
ATOM   2743 N N     . ALA   A 1 376 ? 46.00540  10.24380  20.50344  1.000 56.47199  ? 376 ALA   A N     1 
ATOM   2744 C CA    . ALA   A 1 376 ? 46.26523  10.68455  21.87147  1.000 53.38995  ? 376 ALA   A CA    1 
ATOM   2745 C C     . ALA   A 1 376 ? 47.14223  9.68445   22.62913  1.000 56.80098  ? 376 ALA   A C     1 
ATOM   2746 O O     . ALA   A 1 376 ? 47.82836  10.07259  23.57878  1.000 58.00107  ? 376 ALA   A O     1 
ATOM   2747 C CB    . ALA   A 1 376 ? 44.95276  10.94413  22.61730  1.000 50.32181  ? 376 ALA   A CB    1 
ATOM   2748 N N     . PHE   A 1 377 ? 47.16536  8.41149   22.20987  1.000 61.00050  ? 377 PHE   A N     1 
ATOM   2749 C CA    . PHE   A 1 377 ? 48.04798  7.40664   22.81443  1.000 56.95284  ? 377 PHE   A CA    1 
ATOM   2750 C C     . PHE   A 1 377 ? 49.49967  7.76274   22.54048  1.000 59.66887  ? 377 PHE   A C     1 
ATOM   2751 O O     . PHE   A 1 377 ? 49.91844  7.87334   21.37930  1.000 63.30040  ? 377 PHE   A O     1 
ATOM   2752 C CB    . PHE   A 1 377 ? 47.73599  6.01704   22.26871  1.000 55.83735  ? 377 PHE   A CB    1 
ATOM   2753 C CG    . PHE   A 1 377 ? 48.56111  4.92391   22.88929  1.000 55.85787  ? 377 PHE   A CG    1 
ATOM   2754 C CD1   . PHE   A 1 377 ? 48.30838  4.49626   24.17966  1.000 52.30632  ? 377 PHE   A CD1   1 
ATOM   2755 C CD2   . PHE   A 1 377 ? 49.59340  4.33691   22.18863  1.000 56.07172  ? 377 PHE   A CD2   1 
ATOM   2756 C CE1   . PHE   A 1 377 ? 49.07226  3.50894   24.74324  1.000 50.16768  ? 377 PHE   A CE1   1 
ATOM   2757 C CE2   . PHE   A 1 377 ? 50.34724  3.35313   22.75440  1.000 53.84580  ? 377 PHE   A CE2   1 
ATOM   2758 C CZ    . PHE   A 1 377 ? 50.09380  2.94036   24.02520  1.000 50.71621  ? 377 PHE   A CZ    1 
ATOM   2759 N N     . TYR   A 1 378 ? 50.27805  7.91009   23.60596  1.000 57.89094  ? 378 TYR   A N     1 
ATOM   2760 C CA    . TYR   A 1 378 ? 51.60487  8.50113   23.48376  1.000 62.58333  ? 378 TYR   A CA    1 
ATOM   2761 C C     . TYR   A 1 378 ? 52.73219  7.46629   23.41140  1.000 65.26238  ? 378 TYR   A C     1 
ATOM   2762 O O     . TYR   A 1 378 ? 53.73155  7.70205   22.71734  1.000 65.45830  ? 378 TYR   A O     1 
ATOM   2763 C CB    . TYR   A 1 378 ? 51.82119  9.47293   24.65048  1.000 63.76395  ? 378 TYR   A CB    1 
ATOM   2764 C CG    . TYR   A 1 378 ? 53.18994  10.03813  24.72050  1.000 69.08092  ? 378 TYR   A CG    1 
ATOM   2765 C CD1   . TYR   A 1 378 ? 53.66537  10.86278  23.71332  1.000 67.76887  ? 378 TYR   A CD1   1 
ATOM   2766 C CD2   . TYR   A 1 378 ? 54.00966  9.76705   25.79811  1.000 70.60678  ? 378 TYR   A CD2   1 
ATOM   2767 C CE1   . TYR   A 1 378 ? 54.93837  11.37961  23.76007  1.000 66.13177  ? 378 TYR   A CE1   1 
ATOM   2768 C CE2   . TYR   A 1 378 ? 55.27656  10.28945  25.86214  1.000 73.03706  ? 378 TYR   A CE2   1 
ATOM   2769 C CZ    . TYR   A 1 378 ? 55.73659  11.09757  24.83348  1.000 76.71026  ? 378 TYR   A CZ    1 
ATOM   2770 O OH    . TYR   A 1 378 ? 57.00430  11.62875  24.88277  1.000 90.60560  ? 378 TYR   A OH    1 
ATOM   2771 N N     . HIS   A 1 379 ? 52.55015  6.29189   24.02444  1.000 66.68655  ? 379 HIS   A N     1 
ATOM   2772 C CA    . HIS   A 1 379 ? 53.58423  5.28006   24.26010  1.000 64.47314  ? 379 HIS   A CA    1 
ATOM   2773 C C     . HIS   A 1 379 ? 53.83919  4.35965   23.06061  1.000 68.09127  ? 379 HIS   A C     1 
ATOM   2774 O O     . HIS   A 1 379 ? 53.94740  3.15144   23.26454  1.000 67.29289  ? 379 HIS   A O     1 
ATOM   2775 C CB    . HIS   A 1 379 ? 53.19113  4.44577   25.47244  1.000 57.98160  ? 379 HIS   A CB    1 
ATOM   2776 C CG    . HIS   A 1 379 ? 52.67543  5.26231   26.60969  1.000 64.58532  ? 379 HIS   A CG    1 
ATOM   2777 N ND1   . HIS   A 1 379 ? 53.19610  6.49774   26.93194  1.000 67.76398  ? 379 HIS   A ND1   1 
ATOM   2778 C CD2   . HIS   A 1 379 ? 51.71086  5.01015   27.52450  1.000 63.55199  ? 379 HIS   A CD2   1 
ATOM   2779 C CE1   . HIS   A 1 379 ? 52.55775  6.98347   27.98018  1.000 66.11641  ? 379 HIS   A CE1   1 
ATOM   2780 N NE2   . HIS   A 1 379 ? 51.65737  6.09558   28.36456  1.000 66.16366  ? 379 HIS   A NE2   1 
ATOM   2781 N N     . ARG   A 1 380 ? 53.95212  4.88206   21.82403  1.000 66.69564  ? 380 ARG   A N     1 
ATOM   2782 C CA    . ARG   A 1 380 ? 54.10820  3.99859   20.66095  1.000 67.69991  ? 380 ARG   A CA    1 
ATOM   2783 C C     . ARG   A 1 380 ? 55.42991  3.23910   20.70223  1.000 73.19375  ? 380 ARG   A C     1 
ATOM   2784 O O     . ARG   A 1 380 ? 55.50149  2.07947   20.26939  1.000 72.32927  ? 380 ARG   A O     1 
ATOM   2785 C CB    . ARG   A 1 380 ? 54.00948  4.79736   19.36031  1.000 63.95374  ? 380 ARG   A CB    1 
ATOM   2786 C CG    . ARG   A 1 380 ? 52.66166  5.36677   19.11302  1.000 59.70789  ? 380 ARG   A CG    1 
ATOM   2787 C CD    . ARG   A 1 380 ? 51.69687  4.27724   18.78291  1.000 60.69068  ? 380 ARG   A CD    1 
ATOM   2788 N NE    . ARG   A 1 380 ? 50.40489  4.82706   18.38821  1.000 62.71736  ? 380 ARG   A NE    1 
ATOM   2789 C CZ    . ARG   A 1 380 ? 49.41458  4.09837   17.88562  1.000 58.56482  ? 380 ARG   A CZ    1 
ATOM   2790 N NH1   . ARG   A 1 380 ? 49.50442  2.78001   17.79066  1.000 58.70717  ? 380 ARG   A NH1   1 
ATOM   2791 N NH2   . ARG   A 1 380 ? 48.32010  4.70583   17.44486  1.000 52.73574  ? 380 ARG   A NH2   1 
ATOM   2792 N N     . ASP   A 1 381 ? 56.48799  3.89207   21.19347  1.000 74.69837  ? 381 ASP   A N     1 
ATOM   2793 C CA    . ASP   A 1 381 ? 57.84277  3.35291   21.23197  1.000 75.97214  ? 381 ASP   A CA    1 
ATOM   2794 C C     . ASP   A 1 381 ? 58.08948  2.47624   22.44596  1.000 80.02908  ? 381 ASP   A C     1 
ATOM   2795 O O     . ASP   A 1 381 ? 59.24315  2.10404   22.70039  1.000 82.20150  ? 381 ASP   A O     1 
ATOM   2796 C CB    . ASP   A 1 381 ? 58.86579  4.48828   21.22356  1.000 80.28291  ? 381 ASP   A CB    1 
ATOM   2797 C CG    . ASP   A 1 381 ? 58.83094  5.31033   22.50508  1.000 91.92832  ? 381 ASP   A CG    1 
ATOM   2798 O OD1   . ASP   A 1 381 ? 57.81798  5.23600   23.23663  1.000 89.91866  ? 381 ASP   A OD1   1 
ATOM   2799 O OD2   . ASP   A 1 381 ? 59.82244  6.01907   22.79670  1.000 102.45866 ? 381 ASP   A OD2   1 
ATOM   2800 N N     . ALA   A 1 382 ? 57.04150  2.17349   23.21005  1.000 80.87315  ? 382 ALA   A N     1 
ATOM   2801 C CA    . ALA   A 1 382 ? 57.17004  1.31232   24.37316  1.000 76.84774  ? 382 ALA   A CA    1 
ATOM   2802 C C     . ALA   A 1 382 ? 57.58103  -0.09342  23.95361  1.000 80.72763  ? 382 ALA   A C     1 
ATOM   2803 O O     . ALA   A 1 382 ? 57.12833  -0.61901  22.92692  1.000 77.35991  ? 382 ALA   A O     1 
ATOM   2804 C CB    . ALA   A 1 382 ? 55.84915  1.26692   25.14181  1.000 68.67866  ? 382 ALA   A CB    1 
ATOM   2805 N N     . SER   A 1 383 ? 58.44829  -0.69784  24.76487  1.000 80.52531  ? 383 SER   A N     1 
ATOM   2806 C CA    . SER   A 1 383 ? 58.90252  -2.06469  24.55550  1.000 73.78222  ? 383 SER   A CA    1 
ATOM   2807 C C     . SER   A 1 383 ? 58.00302  -3.09594  25.25149  1.000 74.00814  ? 383 SER   A C     1 
ATOM   2808 O O     . SER   A 1 383 ? 57.64673  -4.10769  24.62892  1.000 70.39339  ? 383 SER   A O     1 
ATOM   2809 C CB    . SER   A 1 383 ? 60.35087  -2.18613  25.02257  1.000 74.85586  ? 383 SER   A CB    1 
ATOM   2810 O OG    . SER   A 1 383 ? 61.17560  -1.32075  24.25777  1.000 78.37430  ? 383 SER   A OG    1 
ATOM   2811 N N     . TYR   A 1 384 ? 57.61545  -2.85657  26.51652  1.000 73.25987  ? 384 TYR   A N     1 
ATOM   2812 C CA    . TYR   A 1 384 ? 56.63773  -3.70325  27.19362  1.000 70.47839  ? 384 TYR   A CA    1 
ATOM   2813 C C     . TYR   A 1 384 ? 55.89161  -2.92891  28.27667  1.000 66.87121  ? 384 TYR   A C     1 
ATOM   2814 O O     . TYR   A 1 384 ? 56.41067  -1.97942  28.85281  1.000 66.88745  ? 384 TYR   A O     1 
ATOM   2815 C CB    . TYR   A 1 384 ? 57.29978  -4.95798  27.79168  1.000 70.84234  ? 384 TYR   A CB    1 
ATOM   2816 C CG    . TYR   A 1 384 ? 58.27930  -4.72101  28.92766  1.000 70.90687  ? 384 TYR   A CG    1 
ATOM   2817 C CD1   . TYR   A 1 384 ? 57.84476  -4.57351  30.24300  1.000 72.42374  ? 384 TYR   A CD1   1 
ATOM   2818 C CD2   . TYR   A 1 384 ? 59.65338  -4.66303  28.68385  1.000 75.74039  ? 384 TYR   A CD2   1 
ATOM   2819 C CE1   . TYR   A 1 384 ? 58.75443  -4.36055  31.29623  1.000 77.94589  ? 384 TYR   A CE1   1 
ATOM   2820 C CE2   . TYR   A 1 384 ? 60.57955  -4.45238  29.72660  1.000 77.72698  ? 384 TYR   A CE2   1 
ATOM   2821 C CZ    . TYR   A 1 384 ? 60.11945  -4.30477  31.03407  1.000 85.90182  ? 384 TYR   A CZ    1 
ATOM   2822 O OH    . TYR   A 1 384 ? 61.00861  -4.10064  32.08274  1.000 93.80971  ? 384 TYR   A OH    1 
ATOM   2823 N N     . PHE   A 1 385 ? 54.66352  -3.36811  28.55675  1.000 66.99325  ? 385 PHE   A N     1 
ATOM   2824 C CA    . PHE   A 1 385 ? 53.89078  -2.83858  29.66897  1.000 61.64335  ? 385 PHE   A CA    1 
ATOM   2825 C C     . PHE   A 1 385 ? 54.16211  -3.60352  30.94463  1.000 63.22021  ? 385 PHE   A C     1 
ATOM   2826 O O     . PHE   A 1 385 ? 54.54254  -4.77629  30.92828  1.000 65.87504  ? 385 PHE   A O     1 
ATOM   2827 C CB    . PHE   A 1 385 ? 52.39697  -2.92382  29.40766  1.000 67.06162  ? 385 PHE   A CB    1 
ATOM   2828 C CG    . PHE   A 1 385 ? 51.85921  -1.81043  28.59697  1.000 69.86232  ? 385 PHE   A CG    1 
ATOM   2829 C CD1   . PHE   A 1 385 ? 52.44715  -0.55529  28.63540  1.000 69.60678  ? 385 PHE   A CD1   1 
ATOM   2830 C CD2   . PHE   A 1 385 ? 50.71592  -1.99004  27.85450  1.000 67.63836  ? 385 PHE   A CD2   1 
ATOM   2831 C CE1   . PHE   A 1 385 ? 51.92974  0.47581   27.88973  1.000 66.61105  ? 385 PHE   A CE1   1 
ATOM   2832 C CE2   . PHE   A 1 385 ? 50.18794  -0.96670  27.11997  1.000 65.81605  ? 385 PHE   A CE2   1 
ATOM   2833 C CZ    . PHE   A 1 385 ? 50.79451  0.27295   27.13810  1.000 67.00606  ? 385 PHE   A CZ    1 
ATOM   2834 N N     . MET   A 1 386 ? 53.89511  -2.94251  32.06666  1.000 55.78414  ? 386 MET   A N     1 
ATOM   2835 C CA    . MET   A 1 386 ? 53.88500  -3.62158  33.35353  1.000 57.45859  ? 386 MET   A CA    1 
ATOM   2836 C C     . MET   A 1 386 ? 52.60739  -3.25264  34.09058  1.000 63.61007  ? 386 MET   A C     1 
ATOM   2837 O O     . MET   A 1 386 ? 52.43667  -2.10447  34.50673  1.000 66.87682  ? 386 MET   A O     1 
ATOM   2838 C CB    . MET   A 1 386 ? 55.12689  -3.27637  34.16252  1.000 58.73055  ? 386 MET   A CB    1 
ATOM   2839 C CG    . MET   A 1 386 ? 55.25687  -4.02846  35.46979  1.000 64.19566  ? 386 MET   A CG    1 
ATOM   2840 S SD    . MET   A 1 386 ? 54.01909  -3.50261  36.72000  1.000 73.60913  ? 386 MET   A SD    1 
ATOM   2841 C CE    . MET   A 1 386 ? 54.37570  -1.75266  36.95953  1.000 74.49923  ? 386 MET   A CE    1 
ATOM   2842 N N     . PHE   A 1 387 ? 51.72762  -4.23177  34.26341  1.000 63.53765  ? 387 PHE   A N     1 
ATOM   2843 C CA    . PHE   A 1 387 ? 50.54205  -4.11285  35.08815  1.000 63.69025  ? 387 PHE   A CA    1 
ATOM   2844 C C     . PHE   A 1 387 ? 50.76117  -4.87728  36.37475  1.000 70.38773  ? 387 PHE   A C     1 
ATOM   2845 O O     . PHE   A 1 387 ? 51.14070  -6.05586  36.34158  1.000 71.94319  ? 387 PHE   A O     1 
ATOM   2846 C CB    . PHE   A 1 387 ? 49.31197  -4.66703  34.37377  1.000 73.16135  ? 387 PHE   A CB    1 
ATOM   2847 C CG    . PHE   A 1 387 ? 49.09803  -4.06315  33.04893  1.000 74.73921  ? 387 PHE   A CG    1 
ATOM   2848 C CD1   . PHE   A 1 387 ? 48.63046  -2.76719  32.93650  1.000 71.28047  ? 387 PHE   A CD1   1 
ATOM   2849 C CD2   . PHE   A 1 387 ? 49.42633  -4.75797  31.91695  1.000 73.58586  ? 387 PHE   A CD2   1 
ATOM   2850 C CE1   . PHE   A 1 387 ? 48.47456  -2.19807  31.72392  1.000 72.21677  ? 387 PHE   A CE1   1 
ATOM   2851 C CE2   . PHE   A 1 387 ? 49.27004  -4.19065  30.69313  1.000 73.67967  ? 387 PHE   A CE2   1 
ATOM   2852 C CZ    . PHE   A 1 387 ? 48.79723  -2.90667  30.59254  1.000 74.61473  ? 387 PHE   A CZ    1 
ATOM   2853 N N     . SER   A 1 388 ? 50.52349  -4.20646  37.50058  1.000 70.65096  ? 388 SER   A N     1 
ATOM   2854 C CA    . SER   A 1 388 ? 50.58166  -4.83316  38.81360  1.000 70.95255  ? 388 SER   A CA    1 
ATOM   2855 C C     . SER   A 1 388 ? 49.19887  -4.76926  39.44666  1.000 71.20415  ? 388 SER   A C     1 
ATOM   2856 O O     . SER   A 1 388 ? 48.54676  -3.71393  39.42629  1.000 64.94471  ? 388 SER   A O     1 
ATOM   2857 C CB    . SER   A 1 388 ? 51.65000  -4.18671  39.72359  1.000 78.51752  ? 388 SER   A CB    1 
ATOM   2858 O OG    . SER   A 1 388 ? 51.66152  -2.75754  39.78063  1.000 79.80291  ? 388 SER   A OG    1 
ATOM   2859 N N     . PHE   A 1 389 ? 48.76339  -5.91124  39.99731  1.000 72.17183  ? 389 PHE   A N     1 
ATOM   2860 C CA    . PHE   A 1 389 ? 47.40787  -6.12813  40.50494  1.000 71.84889  ? 389 PHE   A CA    1 
ATOM   2861 C C     . PHE   A 1 389 ? 47.44247  -6.80772  41.86811  1.000 73.88267  ? 389 PHE   A C     1 
ATOM   2862 O O     . PHE   A 1 389 ? 48.05484  -7.86966  42.01718  1.000 75.76880  ? 389 PHE   A O     1 
ATOM   2863 C CB    . PHE   A 1 389 ? 46.59870  -6.97610  39.51378  1.000 67.60052  ? 389 PHE   A CB    1 
ATOM   2864 C CG    . PHE   A 1 389 ? 45.18852  -7.24610  39.94772  1.000 65.64065  ? 389 PHE   A CG    1 
ATOM   2865 C CD1   . PHE   A 1 389 ? 44.18775  -6.35047  39.66421  1.000 62.87853  ? 389 PHE   A CD1   1 
ATOM   2866 C CD2   . PHE   A 1 389 ? 44.85368  -8.44875  40.55355  1.000 69.12818  ? 389 PHE   A CD2   1 
ATOM   2867 C CE1   . PHE   A 1 389 ? 42.89713  -6.60978  40.03695  1.000 67.07601  ? 389 PHE   A CE1   1 
ATOM   2868 C CE2   . PHE   A 1 389 ? 43.56229  -8.72045  40.91934  1.000 66.96067  ? 389 PHE   A CE2   1 
ATOM   2869 C CZ    . PHE   A 1 389 ? 42.58107  -7.79575  40.66410  1.000 69.42461  ? 389 PHE   A CZ    1 
ATOM   2870 N N     . GLY   A 1 390 ? 46.77279  -6.20894  42.85192  1.000 68.00950  ? 390 GLY   A N     1 
ATOM   2871 C CA    . GLY   A 1 390 ? 46.71777  -6.80595  44.16542  1.000 62.21599  ? 390 GLY   A CA    1 
ATOM   2872 C C     . GLY   A 1 390 ? 45.29190  -7.01804  44.61871  1.000 71.93682  ? 390 GLY   A C     1 
ATOM   2873 O O     . GLY   A 1 390 ? 44.60444  -6.06652  44.99925  1.000 66.59950  ? 390 GLY   A O     1 
ATOM   2874 N N     . ARG   A 1 391 ? 44.81832  -8.25762  44.55810  1.000 79.35527  ? 391 ARG   A N     1 
ATOM   2875 C CA    . ARG   A 1 391 ? 43.51978  -8.57652  45.11345  1.000 80.02600  ? 391 ARG   A CA    1 
ATOM   2876 C C     . ARG   A 1 391 ? 43.66106  -8.82896  46.59890  1.000 81.31607  ? 391 ARG   A C     1 
ATOM   2877 O O     . ARG   A 1 391 ? 44.69369  -9.30409  47.07155  1.000 83.74039  ? 391 ARG   A O     1 
ATOM   2878 C CB    . ARG   A 1 391 ? 42.89723  -9.80888  44.45061  1.000 79.49347  ? 391 ARG   A CB    1 
ATOM   2879 C CG    . ARG   A 1 391 ? 41.44378  -10.01973 44.86291  1.000 79.60955  ? 391 ARG   A CG    1 
ATOM   2880 C CD    . ARG   A 1 391 ? 40.84837  -11.17127 44.12626  1.000 75.78306  ? 391 ARG   A CD    1 
ATOM   2881 N NE    . ARG   A 1 391 ? 41.70704  -12.33023 44.32117  1.000 88.72859  ? 391 ARG   A NE    1 
ATOM   2882 C CZ    . ARG   A 1 391 ? 41.42484  -13.56471 43.93022  1.000 89.00477  ? 391 ARG   A CZ    1 
ATOM   2883 N NH1   . ARG   A 1 391 ? 40.24356  -13.87763 43.41498  1.000 93.87749  ? 391 ARG   A NH1   1 
ATOM   2884 N NH2   . ARG   A 1 391 ? 42.34806  -14.51066 44.06791  1.000 78.20094  ? 391 ARG   A NH2   1 
ATOM   2885 N N     . THR   A 1 392 ? 42.61286  -8.49749  47.33934  1.000 78.89918  ? 392 THR   A N     1 
ATOM   2886 C CA    . THR   A 1 392 ? 42.58219  -8.78963  48.76385  1.000 83.27384  ? 392 THR   A CA    1 
ATOM   2887 C C     . THR   A 1 392 ? 41.24523  -9.42670  49.05981  1.000 82.32280  ? 392 THR   A C     1 
ATOM   2888 O O     . THR   A 1 392 ? 40.21960  -8.96780  48.55393  1.000 82.39600  ? 392 THR   A O     1 
ATOM   2889 C CB    . THR   A 1 392 ? 42.80057  -7.53146  49.62842  1.000 86.00816  ? 392 THR   A CB    1 
ATOM   2890 O OG1   . THR   A 1 392 ? 41.63052  -6.70015  49.61238  1.000 76.50796  ? 392 THR   A OG1   1 
ATOM   2891 C CG2   . THR   A 1 392 ? 44.00757  -6.73161  49.11152  1.000 91.00866  ? 392 THR   A CG2   1 
ATOM   2892 N N     . SER   A 1 393 ? 41.26265  -10.50293 49.84732  1.000 91.13876  ? 393 SER   A N     1 
ATOM   2893 C CA    . SER   A 1 393 ? 39.99865  -11.11985 50.22713  1.000 88.90338  ? 393 SER   A CA    1 
ATOM   2894 C C     . SER   A 1 393 ? 39.23409  -10.21870 51.17977  1.000 82.61644  ? 393 SER   A C     1 
ATOM   2895 O O     . SER   A 1 393 ? 37.99803  -10.22879 51.18237  1.000 89.46195  ? 393 SER   A O     1 
ATOM   2896 C CB    . SER   A 1 393 ? 40.22156  -12.50156 50.84216  1.000 86.33426  ? 393 SER   A CB    1 
ATOM   2897 O OG    . SER   A 1 393 ? 41.02666  -12.43506 52.00362  1.000 89.15895  ? 393 SER   A OG    1 
ATOM   2898 N N     . GLY   A 1 394 ? 39.93395  -9.42743  51.97519  1.000 69.03593  ? 394 GLY   A N     1 
ATOM   2899 C CA    . GLY   A 1 394 ? 39.26923  -8.43288  52.77046  1.000 81.72933  ? 394 GLY   A CA    1 
ATOM   2900 C C     . GLY   A 1 394 ? 39.03979  -7.18226  51.95560  1.000 82.44923  ? 394 GLY   A C     1 
ATOM   2901 O O     . GLY   A 1 394 ? 39.17280  -7.16626  50.73135  1.000 81.66424  ? 394 GLY   A O     1 
ATOM   2902 N N     . ASP   A 1 395 ? 38.68977  -6.10864  52.66084  1.000 82.50761  ? 395 ASP   A N     1 
ATOM   2903 C CA    . ASP   A 1 395 ? 38.81061  -4.78909  52.07357  1.000 71.48226  ? 395 ASP   A CA    1 
ATOM   2904 C C     . ASP   A 1 395 ? 40.26759  -4.48041  51.78238  1.000 81.91434  ? 395 ASP   A C     1 
ATOM   2905 O O     . ASP   A 1 395 ? 41.18658  -5.01558  52.41259  1.000 87.06848  ? 395 ASP   A O     1 
ATOM   2906 C CB    . ASP   A 1 395 ? 38.25243  -3.72194  52.99526  1.000 67.93329  ? 395 ASP   A CB    1 
ATOM   2907 C CG    . ASP   A 1 395 ? 36.75279  -3.57383  52.87607  1.000 80.47846  ? 395 ASP   A CG    1 
ATOM   2908 O OD1   . ASP   A 1 395 ? 36.09595  -4.35863  52.15030  1.000 83.06954  ? 395 ASP   A OD1   1 
ATOM   2909 O OD2   . ASP   A 1 395 ? 36.22728  -2.63121  53.48999  1.000 83.48589  ? 395 ASP   A OD2   1 
ATOM   2910 N N     . LEU   A 1 396 ? 40.47090  -3.60216  50.80656  1.000 85.11240  ? 396 LEU   A N     1 
ATOM   2911 C CA    . LEU   A 1 396 ? 41.80087  -3.06863  50.54556  1.000 85.41843  ? 396 LEU   A CA    1 
ATOM   2912 C C     . LEU   A 1 396 ? 42.29855  -2.29867  51.76501  1.000 86.80159  ? 396 LEU   A C     1 
ATOM   2913 O O     . LEU   A 1 396 ? 41.57464  -1.46794  52.32734  1.000 86.90567  ? 396 LEU   A O     1 
ATOM   2914 C CB    . LEU   A 1 396 ? 41.76270  -2.16213  49.31514  1.000 75.70765  ? 396 LEU   A CB    1 
ATOM   2915 C CG    . LEU   A 1 396 ? 43.13841  -1.67799  48.86928  1.000 73.96929  ? 396 LEU   A CG    1 
ATOM   2916 C CD1   . LEU   A 1 396 ? 43.84713  -2.73840  48.03567  1.000 64.20664  ? 396 LEU   A CD1   1 
ATOM   2917 C CD2   . LEU   A 1 396 ? 43.02516  -0.35110  48.13779  1.000 73.23830  ? 396 LEU   A CD2   1 
ATOM   2918 N N     . THR   A 1 397 ? 43.53246  -2.57843  52.18364  1.000 86.37213  ? 397 THR   A N     1 
ATOM   2919 C CA    . THR   A 1 397 ? 44.15431  -1.82321  53.26089  1.000 90.62998  ? 397 THR   A CA    1 
ATOM   2920 C C     . THR   A 1 397 ? 45.42063  -1.13794  52.77189  1.000 88.90993  ? 397 THR   A C     1 
ATOM   2921 O O     . THR   A 1 397 ? 46.01300  -1.52230  51.75432  1.000 85.22035  ? 397 THR   A O     1 
ATOM   2922 C CB    . THR   A 1 397 ? 44.48042  -2.71637  54.44942  1.000 85.82645  ? 397 THR   A CB    1 
ATOM   2923 O OG1   . THR   A 1 397 ? 45.48972  -3.65531  54.06808  1.000 85.85785  ? 397 THR   A OG1   1 
ATOM   2924 C CG2   . THR   A 1 397 ? 43.22925  -3.44971  54.87294  1.000 92.51516  ? 397 THR   A CG2   1 
ATOM   2925 N N     . ASP   A 1 398 ? 45.83302  -0.10756  53.51681  1.000 87.26030  ? 398 ASP   A N     1 
ATOM   2926 C CA    . ASP   A 1 398 ? 46.98255  0.67364   53.08898  1.000 87.47375  ? 398 ASP   A CA    1 
ATOM   2927 C C     . ASP   A 1 398 ? 48.24976  -0.17936  52.98951  1.000 81.85830  ? 398 ASP   A C     1 
ATOM   2928 O O     . ASP   A 1 398 ? 49.24434  0.26930   52.40072  1.000 79.82933  ? 398 ASP   A O     1 
ATOM   2929 C CB    . ASP   A 1 398 ? 47.16743  1.85938   54.03983  1.000 90.61120  ? 398 ASP   A CB    1 
ATOM   2930 C CG    . ASP   A 1 398 ? 47.89022  3.03577   53.37491  1.000 102.95793 ? 398 ASP   A CG    1 
ATOM   2931 O OD1   . ASP   A 1 398 ? 47.25440  3.70115   52.51666  1.000 101.29697 ? 398 ASP   A OD1   1 
ATOM   2932 O OD2   . ASP   A 1 398 ? 49.07815  3.29763   53.69572  1.000 111.09347 ? 398 ASP   A OD2   1 
ATOM   2933 N N     . THR   A 1 399 ? 48.23129  -1.39215  53.54406  1.000 74.86187  ? 399 THR   A N     1 
ATOM   2934 C CA    . THR   A 1 399 ? 49.30589  -2.34997  53.30651  1.000 79.55421  ? 399 THR   A CA    1 
ATOM   2935 C C     . THR   A 1 399 ? 49.47951  -2.59841  51.82254  1.000 83.65930  ? 399 THR   A C     1 
ATOM   2936 O O     . THR   A 1 399 ? 50.57531  -2.45153  51.26233  1.000 82.62884  ? 399 THR   A O     1 
ATOM   2937 C CB    . THR   A 1 399 ? 48.98694  -3.67204  54.02423  1.000 83.63229  ? 399 THR   A CB    1 
ATOM   2938 O OG1   . THR   A 1 399 ? 48.64931  -3.41675  55.39548  1.000 82.33444  ? 399 THR   A OG1   1 
ATOM   2939 C CG2   . THR   A 1 399 ? 50.13778  -4.71615  53.90760  1.000 77.03199  ? 399 THR   A CG2   1 
ATOM   2940 N N     . THR   A 1 400 ? 48.38544  -2.97454  51.17124  1.000 85.61492  ? 400 THR   A N     1 
ATOM   2941 C CA    . THR   A 1 400 ? 48.44484  -3.46223  49.80448  1.000 84.42834  ? 400 THR   A CA    1 
ATOM   2942 C C     . THR   A 1 400 ? 48.88945  -2.35856  48.85056  1.000 84.91912  ? 400 THR   A C     1 
ATOM   2943 O O     . THR   A 1 400 ? 49.67533  -2.61055  47.92596  1.000 82.12287  ? 400 THR   A O     1 
ATOM   2944 C CB    . THR   A 1 400 ? 47.07096  -4.02356  49.46056  1.000 84.23370  ? 400 THR   A CB    1 
ATOM   2945 O OG1   . THR   A 1 400 ? 46.59323  -4.76338  50.59864  1.000 85.07436  ? 400 THR   A OG1   1 
ATOM   2946 C CG2   . THR   A 1 400 ? 47.16009  -4.95224  48.27754  1.000 80.12858  ? 400 THR   A CG2   1 
ATOM   2947 N N     . VAL   A 1 401 ? 48.42479  -1.12220  49.09692  1.000 82.61453  ? 401 VAL   A N     1 
ATOM   2948 C CA    . VAL   A 1 401 ? 48.87125  0.05581   48.34253  1.000 83.34465  ? 401 VAL   A CA    1 
ATOM   2949 C C     . VAL   A 1 401 ? 50.39093  0.16696   48.35478  1.000 85.68159  ? 401 VAL   A C     1 
ATOM   2950 O O     . VAL   A 1 401 ? 51.04702  0.29273   47.31040  1.000 83.82788  ? 401 VAL   A O     1 
ATOM   2951 C CB    . VAL   A 1 401 ? 48.24402  1.33490   48.92728  1.000 78.70873  ? 401 VAL   A CB    1 
ATOM   2952 C CG1   . VAL   A 1 401 ? 48.79680  2.55757   48.22093  1.000 75.30437  ? 401 VAL   A CG1   1 
ATOM   2953 C CG2   . VAL   A 1 401 ? 46.73423  1.30368   48.83480  1.000 78.58242  ? 401 VAL   A CG2   1 
ATOM   2954 N N     . GLN   A 1 402 ? 50.96389  0.19128   49.55351  1.000 87.91935  ? 402 GLN   A N     1 
ATOM   2955 C CA    . GLN   A 1 402 ? 52.39926  0.37063   49.68209  1.000 89.43912  ? 402 GLN   A CA    1 
ATOM   2956 C C     . GLN   A 1 402 ? 53.14478  -0.77274  49.00657  1.000 88.51445  ? 402 GLN   A C     1 
ATOM   2957 O O     . GLN   A 1 402 ? 54.19199  -0.56010  48.37523  1.000 87.78335  ? 402 GLN   A O     1 
ATOM   2958 C CB    . GLN   A 1 402 ? 52.75394  0.49436   51.15862  1.000 94.18801  ? 402 GLN   A CB    1 
ATOM   2959 C CG    . GLN   A 1 402 ? 52.22248  1.79310   51.78409  1.000 95.49866  ? 402 GLN   A CG    1 
ATOM   2960 C CD    . GLN   A 1 402 ? 52.66829  3.02534   51.01178  1.000 103.97866 ? 402 GLN   A CD    1 
ATOM   2961 O OE1   . GLN   A 1 402 ? 53.83122  3.13161   50.61872  1.000 109.42866 ? 402 GLN   A OE1   1 
ATOM   2962 N NE2   . GLN   A 1 402 ? 51.75421  3.96258   50.80043  1.000 107.54866 ? 402 GLN   A NE2   1 
ATOM   2963 N N     . PHE   A 1 403 ? 52.60069  -1.99020  49.08997  1.000 85.30350  ? 403 PHE   A N     1 
ATOM   2964 C CA    . PHE   A 1 403 ? 53.19723  -3.09537  48.34898  1.000 89.05751  ? 403 PHE   A CA    1 
ATOM   2965 C C     . PHE   A 1 403 ? 53.33279  -2.73694  46.86386  1.000 91.71531  ? 403 PHE   A C     1 
ATOM   2966 O O     . PHE   A 1 403 ? 54.43422  -2.79135  46.29414  1.000 90.62032  ? 403 PHE   A O     1 
ATOM   2967 C CB    . PHE   A 1 403 ? 52.36567  -4.37063  48.52382  1.000 88.41627  ? 403 PHE   A CB    1 
ATOM   2968 C CG    . PHE   A 1 403 ? 52.89154  -5.53620  47.73103  1.000 86.26133  ? 403 PHE   A CG    1 
ATOM   2969 C CD1   . PHE   A 1 403 ? 54.24462  -5.85693  47.75377  1.000 87.04031  ? 403 PHE   A CD1   1 
ATOM   2970 C CD2   . PHE   A 1 403 ? 52.05105  -6.26371  46.90700  1.000 82.95606  ? 403 PHE   A CD2   1 
ATOM   2971 C CE1   . PHE   A 1 403 ? 54.74702  -6.92874  47.01051  1.000 88.53732  ? 403 PHE   A CE1   1 
ATOM   2972 C CE2   . PHE   A 1 403 ? 52.54465  -7.33171  46.15519  1.000 85.98589  ? 403 PHE   A CE2   1 
ATOM   2973 C CZ    . PHE   A 1 403 ? 53.90024  -7.66086  46.20737  1.000 87.04422  ? 403 PHE   A CZ    1 
ATOM   2974 N N     . LEU   A 1 404 ? 52.21524  -2.32829  46.23196  1.000 88.14913  ? 404 LEU   A N     1 
ATOM   2975 C CA    . LEU   A 1 404 ? 52.21769  -1.98003  44.81141  1.000 82.33687  ? 404 LEU   A CA    1 
ATOM   2976 C C     . LEU   A 1 404 ? 52.95254  -0.67573  44.53967  1.000 82.39362  ? 404 LEU   A C     1 
ATOM   2977 O O     . LEU   A 1 404 ? 53.67996  -0.56929  43.54312  1.000 81.72149  ? 404 LEU   A O     1 
ATOM   2978 C CB    . LEU   A 1 404 ? 50.78296  -1.89270  44.29287  1.000 81.15443  ? 404 LEU   A CB    1 
ATOM   2979 C CG    . LEU   A 1 404 ? 50.14797  -3.25495  44.02585  1.000 80.54118  ? 404 LEU   A CG    1 
ATOM   2980 C CD1   . LEU   A 1 404 ? 48.64847  -3.13092  43.77737  1.000 76.25866  ? 404 LEU   A CD1   1 
ATOM   2981 C CD2   . LEU   A 1 404 ? 50.87023  -3.93581  42.86787  1.000 67.19795  ? 404 LEU   A CD2   1 
ATOM   2982 N N     . ASP   A 1 405 ? 52.73576  0.34269   45.37804  1.000 81.96218  ? 405 ASP   A N     1 
ATOM   2983 C CA    . ASP   A 1 405 ? 53.51614  1.56924   45.26235  1.000 80.45112  ? 405 ASP   A CA    1 
ATOM   2984 C C     . ASP   A 1 405 ? 54.99759  1.26698   45.26144  1.000 85.37120  ? 405 ASP   A C     1 
ATOM   2985 O O     . ASP   A 1 405 ? 55.73166  1.70253   44.36950  1.000 85.80275  ? 405 ASP   A O     1 
ATOM   2986 C CB    . ASP   A 1 405 ? 53.16466  2.51933   46.39956  1.000 79.63217  ? 405 ASP   A CB    1 
ATOM   2987 C CG    . ASP   A 1 405 ? 52.09351  3.49301   46.01401  1.000 78.85589  ? 405 ASP   A CG    1 
ATOM   2988 O OD1   . ASP   A 1 405 ? 51.66036  3.44389   44.85581  1.000 84.38947  ? 405 ASP   A OD1   1 
ATOM   2989 O OD2   . ASP   A 1 405 ? 51.63564  4.27329   46.86610  1.000 77.64638  ? 405 ASP   A OD2   1 
ATOM   2990 N N     . GLY   A 1 406 ? 55.45262  0.50777   46.25895  1.000 84.44191  ? 406 GLY   A N     1 
ATOM   2991 C CA    . GLY   A 1 406 ? 56.86070  0.16673   46.32993  1.000 87.18681  ? 406 GLY   A CA    1 
ATOM   2992 C C     . GLY   A 1 406 ? 57.31936  -0.63679  45.13994  1.000 83.39642  ? 406 GLY   A C     1 
ATOM   2993 O O     . GLY   A 1 406 ? 58.46212  -0.50324  44.69447  1.000 86.18152  ? 406 GLY   A O     1 
ATOM   2994 N N     . LEU   A 1 407 ? 56.43130  -1.47413  44.61416  1.000 83.77992  ? 407 LEU   A N     1 
ATOM   2995 C CA    . LEU   A 1 407 ? 56.73638  -2.29463  43.44911  1.000 89.97347  ? 407 LEU   A CA    1 
ATOM   2996 C C     . LEU   A 1 407 ? 57.03593  -1.46078  42.20415  1.000 89.79402  ? 407 LEU   A C     1 
ATOM   2997 O O     . LEU   A 1 407 ? 57.88607  -1.83554  41.38056  1.000 82.16548  ? 407 LEU   A O     1 
ATOM   2998 C CB    . LEU   A 1 407 ? 55.57286  -3.24202  43.20172  1.000 86.47854  ? 407 LEU   A CB    1 
ATOM   2999 C CG    . LEU   A 1 407 ? 55.73723  -4.02095  41.91430  1.000 93.11580  ? 407 LEU   A CG    1 
ATOM   3000 C CD1   . LEU   A 1 407 ? 57.14173  -4.61926  41.76906  1.000 88.63069  ? 407 LEU   A CD1   1 
ATOM   3001 C CD2   . LEU   A 1 407 ? 54.66645  -5.09300  41.96945  1.000 94.01866  ? 407 LEU   A CD2   1 
ATOM   3002 N N     . SER   A 1 408 ? 56.31375  -0.35216  42.02413  1.000 93.13723  ? 408 SER   A N     1 
ATOM   3003 C CA    . SER   A 1 408 ? 56.65524  0.58182   40.95718  1.000 92.28754  ? 408 SER   A CA    1 
ATOM   3004 C C     . SER   A 1 408 ? 57.98335  1.27416   41.27748  1.000 91.51834  ? 408 SER   A C     1 
ATOM   3005 O O     . SER   A 1 408 ? 58.88187  1.35721   40.42303  1.000 85.04345  ? 408 SER   A O     1 
ATOM   3006 C CB    . SER   A 1 408 ? 55.49911  1.59912   40.75070  1.000 86.90797  ? 408 SER   A CB    1 
ATOM   3007 O OG    . SER   A 1 408 ? 54.32718  1.05839   40.10497  1.000 72.65866  ? 408 SER   A OG    1 
ATOM   3008 N N     . GLU   A 1 409 ? 58.15334  1.70607   42.53978  1.000 93.91681  ? 409 GLU   A N     1 
ATOM   3009 C CA    . GLU   A 1 409 ? 59.36247  2.43772   42.93454  1.000 95.27593  ? 409 GLU   A CA    1 
ATOM   3010 C C     . GLU   A 1 409 ? 60.60823  1.61228   42.66253  1.000 96.68199  ? 409 GLU   A C     1 
ATOM   3011 O O     . GLU   A 1 409 ? 61.60234  2.12535   42.13081  1.000 96.01874  ? 409 GLU   A O     1 
ATOM   3012 C CB    . GLU   A 1 409 ? 59.28713  2.82642   44.41752  1.000 92.01361  ? 409 GLU   A CB    1 
ATOM   3013 C CG    . GLU   A 1 409 ? 58.15168  3.84566   44.70610  1.000 106.03863 ? 409 GLU   A CG    1 
ATOM   3014 C CD    . GLU   A 1 409 ? 57.94024  4.13614   46.19212  1.000 109.54041 ? 409 GLU   A CD    1 
ATOM   3015 O OE1   . GLU   A 1 409 ? 58.88774  3.87315   46.97232  1.000 110.99777 ? 409 GLU   A OE1   1 
ATOM   3016 O OE2   . GLU   A 1 409 ? 56.82026  4.57777   46.57927  1.000 96.88744  ? 409 GLU   A OE2   1 
ATOM   3017 N N     . VAL   A 1 410 ? 60.55548  0.32299   42.99207  1.000 91.86115  ? 410 VAL   A N     1 
ATOM   3018 C CA    . VAL   A 1 410 ? 61.70004  -0.55125  42.79457  1.000 88.41222  ? 410 VAL   A CA    1 
ATOM   3019 C C     . VAL   A 1 410 ? 61.89734  -0.88125  41.32138  1.000 92.90631  ? 410 VAL   A C     1 
ATOM   3020 O O     . VAL   A 1 410 ? 63.03300  -1.00668  40.85296  1.000 96.27906  ? 410 VAL   A O     1 
ATOM   3021 C CB    . VAL   A 1 410 ? 61.51398  -1.81962  43.63327  1.000 92.29549  ? 410 VAL   A CB    1 
ATOM   3022 C CG1   . VAL   A 1 410 ? 60.33156  -2.57456  43.10771  1.000 96.16901  ? 410 VAL   A CG1   1 
ATOM   3023 C CG2   . VAL   A 1 410 ? 62.76616  -2.68550  43.54928  1.000 100.61528 ? 410 VAL   A CG2   1 
ATOM   3024 N N     . LEU   A 1 411 ? 60.80544  -1.04700  40.57246  1.000 92.19957  ? 411 LEU   A N     1 
ATOM   3025 C CA    . LEU   A 1 411 ? 60.92187  -1.46462  39.17654  1.000 93.90404  ? 411 LEU   A CA    1 
ATOM   3026 C C     . LEU   A 1 411 ? 61.66273  -0.42699  38.34479  1.000 95.12831  ? 411 LEU   A C     1 
ATOM   3027 O O     . LEU   A 1 411 ? 62.41974  -0.77410  37.43045  1.000 94.45254  ? 411 LEU   A O     1 
ATOM   3028 C CB    . LEU   A 1 411 ? 59.53485  -1.71611  38.60807  1.000 95.74420  ? 411 LEU   A CB    1 
ATOM   3029 C CG    . LEU   A 1 411 ? 59.10466  -3.16143  38.75454  1.000 91.00738  ? 411 LEU   A CG    1 
ATOM   3030 C CD1   . LEU   A 1 411 ? 57.60034  -3.26391  38.78746  1.000 86.50914  ? 411 LEU   A CD1   1 
ATOM   3031 C CD2   . LEU   A 1 411 ? 59.66299  -3.89712  37.56012  1.000 83.41272  ? 411 LEU   A CD2   1 
ATOM   3032 N N     . THR   A 1 412 ? 61.44519  0.85256   38.64849  1.000 95.84707  ? 412 THR   A N     1 
ATOM   3033 C CA    . THR   A 1 412 ? 62.12424  1.95394   37.98582  1.000 95.58510  ? 412 THR   A CA    1 
ATOM   3034 C C     . THR   A 1 412 ? 63.45105  2.33552   38.62814  1.000 99.50494  ? 412 THR   A C     1 
ATOM   3035 O O     . THR   A 1 412 ? 64.23724  3.04374   37.98894  1.000 99.66866  ? 412 THR   A O     1 
ATOM   3036 C CB    . THR   A 1 412 ? 61.21434  3.19522   37.94589  1.000 94.84725  ? 412 THR   A CB    1 
ATOM   3037 O OG1   . THR   A 1 412 ? 60.46044  3.29507   39.16654  1.000 91.22640  ? 412 THR   A OG1   1 
ATOM   3038 C CG2   . THR   A 1 412 ? 60.27423  3.12141   36.77413  1.000 90.40866  ? 412 THR   A CG2   1 
ATOM   3039 N N     . SER   A 1 413 ? 63.72782  1.87560   39.85787  1.000 99.43447  ? 413 SER   A N     1 
ATOM   3040 C CA    . SER   A 1 413 ? 64.84269  2.37747   40.66459  1.000 95.77453  ? 413 SER   A CA    1 
ATOM   3041 C C     . SER   A 1 413 ? 66.17438  1.94246   40.07110  1.000 95.27839  ? 413 SER   A C     1 
ATOM   3042 O O     . SER   A 1 413 ? 67.23991  2.14128   40.65682  1.000 90.19449  ? 413 SER   A O     1 
ATOM   3043 C CB    . SER   A 1 413 ? 64.71251  1.91276   42.11586  1.000 89.90351  ? 413 SER   A CB    1 
ATOM   3044 O OG    . SER   A 1 413 ? 64.88453  0.51981   42.19413  1.000 88.70158  ? 413 SER   A OG    1 
ATOM   3045 N N     . GLY   A 1 414 ? 66.10748  1.32569   38.90013  1.000 100.63031 ? 414 GLY   A N     1 
ATOM   3046 C CA    . GLY   A 1 414 ? 67.26384  1.27128   38.04598  1.000 100.09178 ? 414 GLY   A CA    1 
ATOM   3047 C C     . GLY   A 1 414 ? 67.49824  2.50697   37.18879  1.000 98.28326  ? 414 GLY   A C     1 
ATOM   3048 O O     . GLY   A 1 414 ? 68.46938  2.50459   36.42965  1.000 97.09401  ? 414 GLY   A O     1 
ATOM   3049 N N     . GLN   A 1 415 ? 66.63247  3.55365   37.25262  1.000 93.14528  ? 415 GLN   A N     1 
ATOM   3050 C CA    . GLN   A 1 415 ? 66.79151  4.81814   36.52586  1.000 90.07137  ? 415 GLN   A CA    1 
ATOM   3051 C C     . GLN   A 1 415 ? 65.76686  5.81566   37.03275  1.000 95.58169  ? 415 GLN   A C     1 
ATOM   3052 O O     . GLN   A 1 415 ? 65.16594  6.52916   36.22521  1.000 99.33756  ? 415 GLN   A O     1 
ATOM   3053 C CB    . GLN   A 1 415 ? 66.58506  4.67647   35.01586  1.000 88.30844  ? 415 GLN   A CB    1 
ATOM   3054 C CG    . GLN   A 1 415 ? 67.85155  4.40428   34.22738  1.000 95.50736  ? 415 GLN   A CG    1 
ATOM   3055 C CD    . GLN   A 1 415 ? 67.59916  3.99636   32.77212  1.000 92.61823  ? 415 GLN   A CD    1 
ATOM   3056 O OE1   . GLN   A 1 415 ? 67.17545  4.81855   31.95440  1.000 92.99973  ? 415 GLN   A OE1   1 
ATOM   3057 N NE2   . GLN   A 1 415 ? 67.80383  2.71556   32.46438  1.000 82.76866  ? 415 GLN   A NE2   1 
ATOM   3058 N N     . PRO   A 1 416 ? 65.55721  5.91471   38.34639  1.000 96.10332  ? 416 PRO   A N     1 
ATOM   3059 C CA    . PRO   A 1 416 ? 64.27534  6.44904   38.85637  1.000 102.66683 ? 416 PRO   A CA    1 
ATOM   3060 C C     . PRO   A 1 416 ? 63.86032  7.86035   38.39768  1.000 100.76841 ? 416 PRO   A C     1 
ATOM   3061 O O     . PRO   A 1 416 ? 62.67621  8.17198   38.53655  1.000 97.42112  ? 416 PRO   A O     1 
ATOM   3062 C CB    . PRO   A 1 416 ? 64.46140  6.38112   40.38320  1.000 103.24866 ? 416 PRO   A CB    1 
ATOM   3063 C CG    . PRO   A 1 416 ? 65.95195  6.34263   40.58796  1.000 101.03789 ? 416 PRO   A CG    1 
ATOM   3064 C CD    . PRO   A 1 416 ? 66.44220  5.49846   39.44620  1.000 94.73169  ? 416 PRO   A CD    1 
ATOM   3065 N N     . ASP   A 1 417 ? 64.74559  8.72227   37.87426  1.000 98.45414  ? 417 ASP   A N     1 
ATOM   3066 C CA    . ASP   A 1 417 ? 64.32779  10.08414  37.50672  1.000 102.70946 ? 417 ASP   A CA    1 
ATOM   3067 C C     . ASP   A 1 417 ? 64.00819  10.27480  36.01448  1.000 107.72181 ? 417 ASP   A C     1 
ATOM   3068 O O     . ASP   A 1 417 ? 63.82605  11.42742  35.58218  1.000 104.84412 ? 417 ASP   A O     1 
ATOM   3069 C CB    . ASP   A 1 417 ? 65.36451  11.14383  37.94900  1.000 106.17304 ? 417 ASP   A CB    1 
ATOM   3070 C CG    . ASP   A 1 417 ? 65.52904  11.25195  39.48451  1.000 116.15834 ? 417 ASP   A CG    1 
ATOM   3071 O OD1   . ASP   A 1 417 ? 64.80543  10.56531  40.23934  1.000 115.45310 ? 417 ASP   A OD1   1 
ATOM   3072 O OD2   . ASP   A 1 417 ? 66.39163  12.05241  39.94443  1.000 116.41680 ? 417 ASP   A OD2   1 
ATOM   3073 N N     . ALA   A 1 418 ? 63.87695  9.18615   35.23419  1.000 108.68204 ? 418 ALA   A N     1 
ATOM   3074 C CA    . ALA   A 1 418 ? 63.53243  9.21624   33.81049  1.000 99.21742  ? 418 ALA   A CA    1 
ATOM   3075 C C     . ALA   A 1 418 ? 62.01162  9.18664   33.62786  1.000 95.15034  ? 418 ALA   A C     1 
ATOM   3076 O O     . ALA   A 1 418 ? 61.24984  9.20118   34.59846  1.000 93.84609  ? 418 ALA   A O     1 
ATOM   3077 C CB    . ALA   A 1 418 ? 64.18898  8.05085   33.07094  1.000 91.34083  ? 418 ALA   A CB    1 
ATOM   3078 N N     . TYR   A 1 419 ? 61.54370  9.11727   32.37789  1.000 96.65593  ? 419 TYR   A N     1 
ATOM   3079 C CA    . TYR   A 1 419 ? 60.10763  9.13690   32.09471  1.000 93.98210  ? 419 TYR   A CA    1 
ATOM   3080 C C     . TYR   A 1 419 ? 59.53773  7.72847   31.97134  1.000 91.05229  ? 419 TYR   A C     1 
ATOM   3081 O O     . TYR   A 1 419 ? 59.91884  6.96433   31.06682  1.000 87.14589  ? 419 TYR   A O     1 
ATOM   3082 C CB    . TYR   A 1 419 ? 59.76459  9.91337   30.81921  1.000 91.50368  ? 419 TYR   A CB    1 
ATOM   3083 C CG    . TYR   A 1 419 ? 58.26903  9.81807   30.52939  1.000 82.40593  ? 419 TYR   A CG    1 
ATOM   3084 C CD1   . TYR   A 1 419 ? 57.33446  10.31877  31.43276  1.000 76.42738  ? 419 TYR   A CD1   1 
ATOM   3085 C CD2   . TYR   A 1 419 ? 57.79355  9.18719   29.39004  1.000 79.43113  ? 419 TYR   A CD2   1 
ATOM   3086 C CE1   . TYR   A 1 419 ? 55.99062  10.21067  31.20444  1.000 68.70587  ? 419 TYR   A CE1   1 
ATOM   3087 C CE2   . TYR   A 1 419 ? 56.43486  9.08373   29.15166  1.000 76.25511  ? 419 TYR   A CE2   1 
ATOM   3088 C CZ    . TYR   A 1 419 ? 55.54277  9.60108   30.06554  1.000 71.61355  ? 419 TYR   A CZ    1 
ATOM   3089 O OH    . TYR   A 1 419 ? 54.18829  9.51358   29.85016  1.000 73.74334  ? 419 TYR   A OH    1 
ATOM   3090 N N     . TYR   A 1 420 ? 58.55878  7.42842   32.82692  1.000 89.83329  ? 420 TYR   A N     1 
ATOM   3091 C CA    . TYR   A 1 420 ? 57.81197  6.18143   32.77029  1.000 85.61042  ? 420 TYR   A CA    1 
ATOM   3092 C C     . TYR   A 1 420 ? 56.32418  6.47688   32.57010  1.000 80.68912  ? 420 TYR   A C     1 
ATOM   3093 O O     . TYR   A 1 420 ? 55.71524  7.23973   33.33631  1.000 78.42040  ? 420 TYR   A O     1 
ATOM   3094 C CB    . TYR   A 1 420 ? 58.09667  5.36409   34.02975  1.000 80.89092  ? 420 TYR   A CB    1 
ATOM   3095 C CG    . TYR   A 1 420 ? 59.54548  4.96750   34.04178  1.000 81.28882  ? 420 TYR   A CG    1 
ATOM   3096 C CD1   . TYR   A 1 420 ? 60.02307  4.04628   33.12029  1.000 77.86735  ? 420 TYR   A CD1   1 
ATOM   3097 C CD2   . TYR   A 1 420 ? 60.45009  5.53796   34.93444  1.000 83.70790  ? 420 TYR   A CD2   1 
ATOM   3098 C CE1   . TYR   A 1 420 ? 61.35602  3.67624   33.08747  1.000 83.82889  ? 420 TYR   A CE1   1 
ATOM   3099 C CE2   . TYR   A 1 420 ? 61.79859  5.16402   34.91907  1.000 91.22009  ? 420 TYR   A CE2   1 
ATOM   3100 C CZ    . TYR   A 1 420 ? 62.24688  4.22772   33.98289  1.000 91.63175  ? 420 TYR   A CZ    1 
ATOM   3101 O OH    . TYR   A 1 420 ? 63.57102  3.82319   33.91682  1.000 87.59076  ? 420 TYR   A OH    1 
ATOM   3102 N N     . GLY   A 1 421 ? 55.74954  5.89484   31.52053  1.000 73.59732  ? 421 GLY   A N     1 
ATOM   3103 C CA    . GLY   A 1 421 ? 54.34360  6.10274   31.26406  1.000 71.96343  ? 421 GLY   A CA    1 
ATOM   3104 C C     . GLY   A 1 421 ? 53.44439  5.17607   32.04421  1.000 65.18969  ? 421 GLY   A C     1 
ATOM   3105 O O     . GLY   A 1 421 ? 53.87152  4.24338   32.72834  1.000 64.47875  ? 421 GLY   A O     1 
ATOM   3106 N N     . GLN   A 1 422 ? 52.16119  5.45340   31.92736  1.000 63.68465  ? 422 GLN   A N     1 
ATOM   3107 C CA    . GLN   A 1 422 ? 51.12064  4.60960   32.47882  1.000 64.63222  ? 422 GLN   A CA    1 
ATOM   3108 C C     . GLN   A 1 422 ? 50.06004  4.40635   31.40411  1.000 64.63781  ? 422 GLN   A C     1 
ATOM   3109 O O     . GLN   A 1 422 ? 49.77215  5.31520   30.61672  1.000 66.24572  ? 422 GLN   A O     1 
ATOM   3110 C CB    . GLN   A 1 422 ? 50.50702  5.24006   33.74272  1.000 67.20499  ? 422 GLN   A CB    1 
ATOM   3111 C CG    . GLN   A 1 422 ? 51.52657  5.51960   34.85183  1.000 63.74961  ? 422 GLN   A CG    1 
ATOM   3112 C CD    . GLN   A 1 422 ? 50.87537  5.91456   36.16572  1.000 67.75667  ? 422 GLN   A CD    1 
ATOM   3113 O OE1   . GLN   A 1 422 ? 51.02793  7.03317   36.67383  1.000 69.05206  ? 422 GLN   A OE1   1 
ATOM   3114 N NE2   . GLN   A 1 422 ? 50.16145  4.95112   36.75071  1.000 78.87185  ? 422 GLN   A NE2   1 
ATOM   3115 N N     . TYR   A 1 423 ? 49.48474  3.21655   31.36293  1.000 59.88220  ? 423 TYR   A N     1 
ATOM   3116 C CA    . TYR   A 1 423 ? 48.36900  2.97588   30.45951  1.000 60.72677  ? 423 TYR   A CA    1 
ATOM   3117 C C     . TYR   A 1 423 ? 47.07567  3.56040   31.03682  1.000 62.88523  ? 423 TYR   A C     1 
ATOM   3118 O O     . TYR   A 1 423 ? 46.77177  3.36669   32.21585  1.000 69.37866  ? 423 TYR   A O     1 
ATOM   3119 C CB    . TYR   A 1 423 ? 48.26183  1.48472   30.23605  1.000 57.59792  ? 423 TYR   A CB    1 
ATOM   3120 C CG    . TYR   A 1 423 ? 47.28052  1.11243   29.21174  1.000 59.55237  ? 423 TYR   A CG    1 
ATOM   3121 C CD1   . TYR   A 1 423 ? 47.07943  1.89360   28.09446  1.000 54.73313  ? 423 TYR   A CD1   1 
ATOM   3122 C CD2   . TYR   A 1 423 ? 46.52817  -0.03957  29.36777  1.000 67.31413  ? 423 TYR   A CD2   1 
ATOM   3123 C CE1   . TYR   A 1 423 ? 46.13508  1.52823   27.14492  1.000 54.23250  ? 423 TYR   A CE1   1 
ATOM   3124 C CE2   . TYR   A 1 423 ? 45.59203  -0.41672  28.43939  1.000 64.29895  ? 423 TYR   A CE2   1 
ATOM   3125 C CZ    . TYR   A 1 423 ? 45.38986  0.36469   27.32973  1.000 58.16692  ? 423 TYR   A CZ    1 
ATOM   3126 O OH    . TYR   A 1 423 ? 44.43835  -0.05461  26.42919  1.000 57.69502  ? 423 TYR   A OH    1 
ATOM   3127 N N     . VAL   A 1 424 ? 46.31969  4.31414   30.23527  1.000 58.11696  ? 424 VAL   A N     1 
ATOM   3128 C CA    . VAL   A 1 424 ? 45.16199  4.97568   30.83584  1.000 56.96490  ? 424 VAL   A CA    1 
ATOM   3129 C C     . VAL   A 1 424 ? 43.96063  4.05096   30.86471  1.000 56.90750  ? 424 VAL   A C     1 
ATOM   3130 O O     . VAL   A 1 424 ? 42.90603  4.43569   31.39462  1.000 55.07044  ? 424 VAL   A O     1 
ATOM   3131 C CB    . VAL   A 1 424 ? 44.79227  6.31239   30.14796  1.000 57.41418  ? 424 VAL   A CB    1 
ATOM   3132 C CG1   . VAL   A 1 424 ? 44.01769  6.10001   28.85003  1.000 56.77996  ? 424 VAL   A CG1   1 
ATOM   3133 C CG2   . VAL   A 1 424 ? 44.07759  7.27384   31.12117  1.000 47.61177  ? 424 VAL   A CG2   1 
ATOM   3134 N N     . GLY   A 1 425 ? 44.09296  2.84076   30.31968  1.000 54.22323  ? 425 GLY   A N     1 
ATOM   3135 C CA    . GLY   A 1 425 ? 43.10857  1.80184   30.56403  1.000 56.25922  ? 425 GLY   A CA    1 
ATOM   3136 C C     . GLY   A 1 425 ? 43.21726  1.17831   31.94303  1.000 59.92170  ? 425 GLY   A C     1 
ATOM   3137 O O     . GLY   A 1 425 ? 42.24093  0.61254   32.44553  1.000 71.92070  ? 425 GLY   A O     1 
ATOM   3138 N N     . ASN   A 1 426 ? 44.38102  1.26941   32.56520  1.000 58.40508  ? 426 ASN   A N     1 
ATOM   3139 C CA    . ASN   A 1 426 ? 44.62522  0.73443   33.89732  1.000 64.58198  ? 426 ASN   A CA    1 
ATOM   3140 C C     . ASN   A 1 426 ? 44.80887  1.92229   34.84434  1.000 66.71689  ? 426 ASN   A C     1 
ATOM   3141 O O     . ASN   A 1 426 ? 45.90642  2.18195   35.37818  1.000 66.44213  ? 426 ASN   A O     1 
ATOM   3142 C CB    . ASN   A 1 426 ? 45.87220  -0.23396  33.84546  1.000 68.74797  ? 426 ASN   A CB    1 
ATOM   3143 C CG    . ASN   A 1 426 ? 46.07866  -1.03588  35.12624  1.000 73.40632  ? 426 ASN   A CG    1 
ATOM   3144 O OD1   . ASN   A 1 426 ? 46.07759  -0.49227  36.22890  1.000 73.72240  ? 426 ASN   A OD1   1 
ATOM   3145 N ND2   . ASN   A 1 426 ? 46.26764  -2.33981  34.97990  1.000 76.03921  ? 426 ASN   A ND2   1 
ATOM   3146 N N     . VAL   A 1 427 ? 43.71989  2.68752   35.02423  1.000 61.04418  ? 427 VAL   A N     1 
ATOM   3147 C CA    . VAL   A 1 427 ? 43.83068  3.88978   35.84405  1.000 57.73118  ? 427 VAL   A CA    1 
ATOM   3148 C C     . VAL   A 1 427 ? 44.26379  3.51376   37.24884  1.000 58.38069  ? 427 VAL   A C     1 
ATOM   3149 O O     . VAL   A 1 427 ? 44.09630  2.37894   37.72023  1.000 59.96073  ? 427 VAL   A O     1 
ATOM   3150 C CB    . VAL   A 1 427 ? 42.55552  4.74605   35.91584  1.000 55.09028  ? 427 VAL   A CB    1 
ATOM   3151 C CG1   . VAL   A 1 427 ? 42.32206  5.44902   34.61172  1.000 57.93304  ? 427 VAL   A CG1   1 
ATOM   3152 C CG2   . VAL   A 1 427 ? 41.36756  3.90729   36.29642  1.000 56.43523  ? 427 VAL   A CG2   1 
ATOM   3153 N N     . ASP   A 1 428 ? 44.79123  4.51476   37.94051  1.000 61.13048  ? 428 ASP   A N     1 
ATOM   3154 C CA    . ASP   A 1 428 ? 45.46001  4.33320   39.21916  1.000 61.23754  ? 428 ASP   A CA    1 
ATOM   3155 C C     . ASP   A 1 428 ? 45.01924  5.52581   40.04262  1.000 54.46431  ? 428 ASP   A C     1 
ATOM   3156 O O     . ASP   A 1 428 ? 45.66874  6.57296   40.04118  1.000 59.69979  ? 428 ASP   A O     1 
ATOM   3157 C CB    . ASP   A 1 428 ? 46.97846  4.29065   39.02003  1.000 65.17982  ? 428 ASP   A CB    1 
ATOM   3158 C CG    . ASP   A 1 428 ? 47.76934  4.23049   40.32211  1.000 67.98066  ? 428 ASP   A CG    1 
ATOM   3159 O OD1   . ASP   A 1 428 ? 47.18094  4.30530   41.43502  1.000 64.20361  ? 428 ASP   A OD1   1 
ATOM   3160 O OD2   . ASP   A 1 428 ? 49.00920  4.05808   40.20246  1.000 68.88299  ? 428 ASP   A OD2   1 
ATOM   3161 N N     . PRO   A 1 429 ? 43.88941  5.44131   40.68027  1.000 49.60484  ? 429 PRO   A N     1 
ATOM   3162 C CA    . PRO   A 1 429 ? 43.36124  6.64307   41.34069  1.000 59.37116  ? 429 PRO   A CA    1 
ATOM   3163 C C     . PRO   A 1 429 ? 44.02614  6.94834   42.68117  1.000 65.13686  ? 429 PRO   A C     1 
ATOM   3164 O O     . PRO   A 1 429 ? 43.44986  7.66720   43.50389  1.000 63.30860  ? 429 PRO   A O     1 
ATOM   3165 C CB    . PRO   A 1 429 ? 41.86290  6.32581   41.49272  1.000 56.87286  ? 429 PRO   A CB    1 
ATOM   3166 C CG    . PRO   A 1 429 ? 41.82334  4.81380   41.60699  1.000 58.58224  ? 429 PRO   A CG    1 
ATOM   3167 C CD    . PRO   A 1 429 ? 42.97721  4.28487   40.77367  1.000 56.46165  ? 429 PRO   A CD    1 
ATOM   3168 N N     . ARG   A 1 430 ? 45.22921  6.42309   42.91683  1.000 68.58462  ? 430 ARG   A N     1 
ATOM   3169 C CA    . ARG   A 1 430 ? 45.93901  6.55253   44.19175  1.000 69.09132  ? 430 ARG   A CA    1 
ATOM   3170 C C     . ARG   A 1 430 ? 47.26170  7.30053   44.02678  1.000 72.03261  ? 430 ARG   A C     1 
ATOM   3171 O O     . ARG   A 1 430 ? 48.29112  6.94866   44.62521  1.000 74.10684  ? 430 ARG   A O     1 
ATOM   3172 C CB    . ARG   A 1 430 ? 46.15284  5.18146   44.84380  1.000 67.87150  ? 430 ARG   A CB    1 
ATOM   3173 C CG    . ARG   A 1 430 ? 44.84606  4.46267   45.17355  1.000 62.44962  ? 430 ARG   A CG    1 
ATOM   3174 C CD    . ARG   A 1 430 ? 45.02120  3.21349   46.02043  1.000 65.30375  ? 430 ARG   A CD    1 
ATOM   3175 N NE    . ARG   A 1 430 ? 43.75180  2.53430   46.25220  1.000 67.59451  ? 430 ARG   A NE    1 
ATOM   3176 C CZ    . ARG   A 1 430 ? 42.79277  3.01896   47.03357  1.000 67.25481  ? 430 ARG   A CZ    1 
ATOM   3177 N NH1   . ARG   A 1 430 ? 42.89904  4.21643   47.60158  1.000 60.18293  ? 430 ARG   A NH1   1 
ATOM   3178 N NH2   . ARG   A 1 430 ? 41.69425  2.29587   47.23402  1.000 72.43408  ? 430 ARG   A NH2   1 
ATOM   3179 N N     . GLN   A 1 431 ? 47.22482  8.38244   43.24749  1.000 68.32294  ? 431 GLN   A N     1 
ATOM   3180 C CA    . GLN   A 1 431 ? 48.42759  9.06619   42.81438  1.000 67.02192  ? 431 GLN   A CA    1 
ATOM   3181 C C     . GLN   A 1 431 ? 48.04682  10.50036  42.46865  1.000 66.67485  ? 431 GLN   A C     1 
ATOM   3182 O O     . GLN   A 1 431 ? 46.89158  10.75844  42.10258  1.000 63.03819  ? 431 GLN   A O     1 
ATOM   3183 C CB    . GLN   A 1 431 ? 49.09915  8.31305   41.63417  1.000 61.24725  ? 431 GLN   A CB    1 
ATOM   3184 C CG    . GLN   A 1 431 ? 48.41604  8.34586   40.27361  1.000 63.66960  ? 431 GLN   A CG    1 
ATOM   3185 C CD    . GLN   A 1 431 ? 49.29062  7.76427   39.11806  1.000 66.21638  ? 431 GLN   A CD    1 
ATOM   3186 O OE1   . GLN   A 1 431 ? 48.75801  7.19666   38.16572  1.000 64.30908  ? 431 GLN   A OE1   1 
ATOM   3187 N NE2   . GLN   A 1 431 ? 50.61775  7.93259   39.19534  1.000 67.44687  ? 431 GLN   A NE2   1 
ATOM   3188 N N     . PRO   A 1 432 ? 48.96872  11.46242  42.65777  1.000 77.37250  ? 432 PRO   A N     1 
ATOM   3189 C CA    . PRO   A 1 432 ? 48.61621  12.88003  42.45069  1.000 72.82539  ? 432 PRO   A CA    1 
ATOM   3190 C C     . PRO   A 1 432 ? 48.10592  13.14504  41.04115  1.000 67.52478  ? 432 PRO   A C     1 
ATOM   3191 O O     . PRO   A 1 432 ? 48.69590  12.69590  40.04722  1.000 63.72399  ? 432 PRO   A O     1 
ATOM   3192 C CB    . PRO   A 1 432 ? 49.92918  13.63691  42.70684  1.000 68.45663  ? 432 PRO   A CB    1 
ATOM   3193 C CG    . PRO   A 1 432 ? 50.75287  12.73862  43.57460  1.000 76.41667  ? 432 PRO   A CG    1 
ATOM   3194 C CD    . PRO   A 1 432 ? 50.32675  11.30090  43.23360  1.000 79.99514  ? 432 PRO   A CD    1 
ATOM   3195 N N     . THR   A 1 433 ? 46.99505  13.89149  40.96633  1.000 60.50727  ? 433 THR   A N     1 
ATOM   3196 C CA    . THR   A 1 433 ? 46.36324  14.13129  39.67411  1.000 59.49388  ? 433 THR   A CA    1 
ATOM   3197 C C     . THR   A 1 433 ? 47.37123  14.60202  38.63599  1.000 58.59672  ? 433 THR   A C     1 
ATOM   3198 O O     . THR   A 1 433 ? 47.26529  14.24747  37.45727  1.000 56.39231  ? 433 THR   A O     1 
ATOM   3199 C CB    . THR   A 1 433 ? 45.20651  15.12088  39.84674  1.000 63.93734  ? 433 THR   A CB    1 
ATOM   3200 O OG1   . THR   A 1 433 ? 44.21010  14.56741  40.72577  1.000 67.09446  ? 433 THR   A OG1   1 
ATOM   3201 C CG2   . THR   A 1 433 ? 44.57200  15.45083  38.52223  1.000 65.59790  ? 433 THR   A CG2   1 
ATOM   3202 N N     . ASP   A 1 434 ? 48.38567  15.35789  39.06619  1.000 61.66074  ? 434 ASP   A N     1 
ATOM   3203 C CA    . ASP   A 1 434 ? 49.40797  15.85622  38.14738  1.000 58.82184  ? 434 ASP   A CA    1 
ATOM   3204 C C     . ASP   A 1 434 ? 50.31266  14.74015  37.64428  1.000 57.76198  ? 434 ASP   A C     1 
ATOM   3205 O O     . ASP   A 1 434 ? 50.74539  14.75465  36.48638  1.000 55.88716  ? 434 ASP   A O     1 
ATOM   3206 C CB    . ASP   A 1 434 ? 50.22984  16.95746  38.83821  1.000 64.10492  ? 434 ASP   A CB    1 
ATOM   3207 C CG    . ASP   A 1 434 ? 51.34613  16.40033  39.75423  1.000 68.13921  ? 434 ASP   A CG    1 
ATOM   3208 O OD1   . ASP   A 1 434 ? 51.01138  15.69893  40.74375  1.000 70.97501  ? 434 ASP   A OD1   1 
ATOM   3209 O OD2   . ASP   A 1 434 ? 52.55683  16.66966  39.51347  1.000 62.74745  ? 434 ASP   A OD2   1 
ATOM   3210 N N     . GLU   A 1 435 ? 50.62040  13.77407  38.50712  1.000 63.22229  ? 435 GLU   A N     1 
ATOM   3211 C CA    . GLU   A 1 435 ? 51.51760  12.68120  38.13807  1.000 63.53049  ? 435 GLU   A CA    1 
ATOM   3212 C C     . GLU   A 1 435 ? 50.85374  11.76889  37.12014  1.000 61.59451  ? 435 GLU   A C     1 
ATOM   3213 O O     . GLU   A 1 435 ? 51.50937  11.25687  36.20063  1.000 56.17669  ? 435 GLU   A O     1 
ATOM   3214 C CB    . GLU   A 1 435 ? 51.87856  11.90627  39.39801  1.000 66.75138  ? 435 GLU   A CB    1 
ATOM   3215 C CG    . GLU   A 1 435 ? 52.89677  10.79519  39.27966  1.000 68.88806  ? 435 GLU   A CG    1 
ATOM   3216 C CD    . GLU   A 1 435 ? 53.17039  10.10260  40.65953  1.000 91.27653  ? 435 GLU   A CD    1 
ATOM   3217 O OE1   . GLU   A 1 435 ? 52.51707  10.47257  41.69429  1.000 89.31794  ? 435 GLU   A OE1   1 
ATOM   3218 O OE2   . GLU   A 1 435 ? 54.02451  9.16564   40.69311  1.000 116.40658 ? 435 GLU   A OE2   1 
ATOM   3219 N N     . ALA   A 1 436 ? 49.53791  11.58226  37.28721  1.000 63.26092  ? 436 ALA   A N     1 
ATOM   3220 C CA    . ALA   A 1 436 ? 48.71885  10.73402  36.42730  1.000 59.44838  ? 436 ALA   A CA    1 
ATOM   3221 C C     . ALA   A 1 436 ? 48.69800  11.23366  34.98008  1.000 60.22959  ? 436 ALA   A C     1 
ATOM   3222 O O     . ALA   A 1 436 ? 49.08199  10.50985  34.04321  1.000 55.98994  ? 436 ALA   A O     1 
ATOM   3223 C CB    . ALA   A 1 436 ? 47.30401  10.67845  37.00024  1.000 58.11886  ? 436 ALA   A CB    1 
ATOM   3224 N N     . LEU   A 1 437 ? 48.23283  12.47490  34.77511  1.000 56.46333  ? 437 LEU   A N     1 
ATOM   3225 C CA    . LEU   A 1 437 ? 48.07842  12.99078  33.41452  1.000 55.54907  ? 437 LEU   A CA    1 
ATOM   3226 C C     . LEU   A 1 437 ? 49.39066  12.92186  32.64870  1.000 56.75893  ? 437 LEU   A C     1 
ATOM   3227 O O     . LEU   A 1 437 ? 49.40436  12.82766  31.41373  1.000 58.48912  ? 437 LEU   A O     1 
ATOM   3228 C CB    . LEU   A 1 437 ? 47.57226  14.42858  33.46363  1.000 52.13704  ? 437 LEU   A CB    1 
ATOM   3229 C CG    . LEU   A 1 437 ? 46.18388  14.60725  34.08363  1.000 53.43652  ? 437 LEU   A CG    1 
ATOM   3230 C CD1   . LEU   A 1 437 ? 45.90773  16.06577  34.20957  1.000 54.55844  ? 437 LEU   A CD1   1 
ATOM   3231 C CD2   . LEU   A 1 437 ? 45.12606  13.95944  33.24090  1.000 56.71521  ? 437 LEU   A CD2   1 
ATOM   3232 N N     . THR   A 1 438 ? 50.49890  12.95903  33.37744  1.000 61.60331  ? 438 THR   A N     1 
ATOM   3233 C CA    . THR   A 1 438 ? 51.81883  12.89957  32.77167  1.000 59.43789  ? 438 THR   A CA    1 
ATOM   3234 C C     . THR   A 1 438 ? 52.13391  11.50673  32.26231  1.000 56.90344  ? 438 THR   A C     1 
ATOM   3235 O O     . THR   A 1 438 ? 52.58294  11.33852  31.12517  1.000 53.67273  ? 438 THR   A O     1 
ATOM   3236 C CB    . THR   A 1 438 ? 52.84526  13.32694  33.79566  1.000 55.59014  ? 438 THR   A CB    1 
ATOM   3237 O OG1   . THR   A 1 438 ? 52.55842  14.67290  34.18340  1.000 55.47126  ? 438 THR   A OG1   1 
ATOM   3238 C CG2   . THR   A 1 438 ? 54.18164  13.23138  33.20077  1.000 53.74207  ? 438 THR   A CG2   1 
ATOM   3239 N N     . GLY   A 1 439 ? 51.92936  10.50062  33.11211  1.000 65.82194  ? 439 GLY   A N     1 
ATOM   3240 C CA    . GLY   A 1 439 ? 52.10059  9.12243   32.68060  1.000 69.36537  ? 439 GLY   A CA    1 
ATOM   3241 C C     . GLY   A 1 439 ? 51.10762  8.71937   31.60557  1.000 65.51378  ? 439 GLY   A C     1 
ATOM   3242 O O     . GLY   A 1 439 ? 51.48945  8.13497   30.58492  1.000 64.25475  ? 439 GLY   A O     1 
ATOM   3243 N N     . TYR   A 1 440 ? 49.81908  9.02596   31.81889  1.000 63.03252  ? 440 TYR   A N     1 
ATOM   3244 C CA    . TYR   A 1 440 ? 48.79326  8.67931   30.84035  1.000 59.70063  ? 440 TYR   A CA    1 
ATOM   3245 C C     . TYR   A 1 440 ? 49.11561  9.25458   29.47352  1.000 57.52831  ? 440 TYR   A C     1 
ATOM   3246 O O     . TYR   A 1 440 ? 49.20069  8.53506   28.46928  1.000 59.95621  ? 440 TYR   A O     1 
ATOM   3247 C CB    . TYR   A 1 440 ? 47.43231  9.20469   31.28161  1.000 54.39534  ? 440 TYR   A CB    1 
ATOM   3248 C CG    . TYR   A 1 440 ? 46.91915  8.59834   32.53317  1.000 54.25974  ? 440 TYR   A CG    1 
ATOM   3249 C CD1   . TYR   A 1 440 ? 47.46442  7.43107   33.04227  1.000 56.58678  ? 440 TYR   A CD1   1 
ATOM   3250 C CD2   . TYR   A 1 440 ? 45.87487  9.18433   33.21065  1.000 56.13515  ? 440 TYR   A CD2   1 
ATOM   3251 C CE1   . TYR   A 1 440 ? 46.98242  6.87500   34.22756  1.000 60.87181  ? 440 TYR   A CE1   1 
ATOM   3252 C CE2   . TYR   A 1 440 ? 45.38808  8.64785   34.38630  1.000 54.33931  ? 440 TYR   A CE2   1 
ATOM   3253 C CZ    . TYR   A 1 440 ? 45.93115  7.49818   34.89776  1.000 55.11100  ? 440 TYR   A CZ    1 
ATOM   3254 O OH    . TYR   A 1 440 ? 45.39927  6.99918   36.07587  1.000 49.49957  ? 440 TYR   A OH    1 
ATOM   3255 N N     . TYR   A 1 441 ? 49.25471  10.56490  29.40957  1.000 56.38465  ? 441 TYR   A N     1 
ATOM   3256 C CA    . TYR   A 1 441 ? 49.25348  11.24794  28.13391  1.000 55.69309  ? 441 TYR   A CA    1 
ATOM   3257 C C     . TYR   A 1 441 ? 50.63097  11.72365  27.71046  1.000 62.91114  ? 441 TYR   A C     1 
ATOM   3258 O O     . TYR   A 1 441 ? 50.84914  11.96552  26.52075  1.000 65.09577  ? 441 TYR   A O     1 
ATOM   3259 C CB    . TYR   A 1 441 ? 48.28593  12.41951  28.22805  1.000 48.78784  ? 441 TYR   A CB    1 
ATOM   3260 C CG    . TYR   A 1 441 ? 46.92701  11.88494  28.55805  1.000 50.24306  ? 441 TYR   A CG    1 
ATOM   3261 C CD1   . TYR   A 1 441 ? 46.38638  10.83011  27.84641  1.000 51.00702  ? 441 TYR   A CD1   1 
ATOM   3262 C CD2   . TYR   A 1 441 ? 46.22416  12.35804  29.66075  1.000 52.45377  ? 441 TYR   A CD2   1 
ATOM   3263 C CE1   . TYR   A 1 441 ? 45.11616  10.30451  28.17548  1.000 49.87340  ? 441 TYR   A CE1   1 
ATOM   3264 C CE2   . TYR   A 1 441 ? 44.96968  11.84661  29.99678  1.000 53.05917  ? 441 TYR   A CE2   1 
ATOM   3265 C CZ    . TYR   A 1 441 ? 44.42356  10.81559  29.25008  1.000 51.48394  ? 441 TYR   A CZ    1 
ATOM   3266 O OH    . TYR   A 1 441 ? 43.19913  10.29196  29.59522  1.000 55.57613  ? 441 TYR   A OH    1 
ATOM   3267 N N     . GLY   A 1 442 ? 51.57863  11.81542  28.64389  1.000 63.50271  ? 442 GLY   A N     1 
ATOM   3268 C CA    . GLY   A 1 442 ? 52.89735  12.25981  28.25698  1.000 60.96815  ? 442 GLY   A CA    1 
ATOM   3269 C C     . GLY   A 1 442 ? 52.80972  13.54993  27.48953  1.000 61.74636  ? 442 GLY   A C     1 
ATOM   3270 O O     . GLY   A 1 442 ? 52.03313  14.44765  27.82564  1.000 62.11507  ? 442 GLY   A O     1 
ATOM   3271 N N     . LYS   A 1 443 ? 53.58652  13.64582  26.41478  1.000 64.72816  ? 443 LYS   A N     1 
ATOM   3272 C CA    . LYS   A 1 443 ? 53.73103  14.95104  25.79347  1.000 68.51713  ? 443 LYS   A CA    1 
ATOM   3273 C C     . LYS   A 1 443 ? 52.46186  15.38929  25.07187  1.000 66.01421  ? 443 LYS   A C     1 
ATOM   3274 O O     . LYS   A 1 443 ? 52.25122  16.59889  24.91367  1.000 70.61630  ? 443 LYS   A O     1 
ATOM   3275 C CB    . LYS   A 1 443 ? 54.93455  14.96527  24.84934  1.000 75.89866  ? 443 LYS   A CB    1 
ATOM   3276 N N     . ASN   A 1 444 ? 51.59623  14.44714  24.66536  1.000 63.06052  ? 444 ASN   A N     1 
ATOM   3277 C CA    . ASN   A 1 444 ? 50.29687  14.81383  24.09748  1.000 60.91514  ? 444 ASN   A CA    1 
ATOM   3278 C C     . ASN   A 1 444 ? 49.41535  15.57419  25.08779  1.000 59.60761  ? 444 ASN   A C     1 
ATOM   3279 O O     . ASN   A 1 444 ? 48.38178  16.11589  24.68779  1.000 55.71624  ? 444 ASN   A O     1 
ATOM   3280 C CB    . ASN   A 1 444 ? 49.52462  13.57478  23.61849  1.000 58.38481  ? 444 ASN   A CB    1 
ATOM   3281 C CG    . ASN   A 1 444 ? 50.06930  12.97939  22.32724  1.000 60.10115  ? 444 ASN   A CG    1 
ATOM   3282 O OD1   . ASN   A 1 444 ? 50.79153  13.63590  21.57365  1.000 63.44538  ? 444 ASN   A OD1   1 
ATOM   3283 N ND2   . ASN   A 1 444 ? 49.75226  11.70344  22.08974  1.000 56.08798  ? 444 ASN   A ND2   1 
ATOM   3284 N N     . LEU   A 1 445 ? 49.78622  15.62830  26.36324  1.000 54.78022  ? 445 LEU   A N     1 
ATOM   3285 C CA    . LEU   A 1 445 ? 48.88861  16.21929  27.33539  1.000 52.56262  ? 445 LEU   A CA    1 
ATOM   3286 C C     . LEU   A 1 445 ? 48.54906  17.64606  26.96870  1.000 55.41908  ? 445 LEU   A C     1 
ATOM   3287 O O     . LEU   A 1 445 ? 47.44086  18.11291  27.23358  1.000 56.66529  ? 445 LEU   A O     1 
ATOM   3288 C CB    . LEU   A 1 445 ? 49.50520  16.15160  28.72325  1.000 59.42962  ? 445 LEU   A CB    1 
ATOM   3289 C CG    . LEU   A 1 445 ? 48.81448  16.97405  29.80956  1.000 58.05004  ? 445 LEU   A CG    1 
ATOM   3290 C CD1   . LEU   A 1 445 ? 47.33992  16.65222  29.86407  1.000 56.15863  ? 445 LEU   A CD1   1 
ATOM   3291 C CD2   . LEU   A 1 445 ? 49.48289  16.67152  31.14088  1.000 58.54191  ? 445 LEU   A CD2   1 
ATOM   3292 N N     . HIS   A 1 446 ? 49.48681  18.36678  26.36873  1.000 63.67248  ? 446 HIS   A N     1 
ATOM   3293 C CA    . HIS   A 1 446 ? 49.19648  19.76531  26.10511  1.000 68.43022  ? 446 HIS   A CA    1 
ATOM   3294 C C     . HIS   A 1 446 ? 48.28970  19.93279  24.89775  1.000 65.73483  ? 446 HIS   A C     1 
ATOM   3295 O O     . HIS   A 1 446 ? 47.30503  20.66878  24.96323  1.000 67.36023  ? 446 HIS   A O     1 
ATOM   3296 C CB    . HIS   A 1 446 ? 50.46803  20.57193  25.92141  1.000 82.75567  ? 446 HIS   A CB    1 
ATOM   3297 C CG    . HIS   A 1 446 ? 50.19725  21.96851  25.46540  1.000 100.48615 ? 446 HIS   A CG    1 
ATOM   3298 N ND1   . HIS   A 1 446 ? 50.17241  22.31926  24.12811  1.000 105.60866 ? 446 HIS   A ND1   1 
ATOM   3299 C CD2   . HIS   A 1 446 ? 49.87064  23.08966  26.15552  1.000 107.90371 ? 446 HIS   A CD2   1 
ATOM   3300 C CE1   . HIS   A 1 446 ? 49.87909  23.60514  24.01482  1.000 104.18736 ? 446 HIS   A CE1   1 
ATOM   3301 N NE2   . HIS   A 1 446 ? 49.68768  24.09617  25.22962  1.000 113.42866 ? 446 HIS   A NE2   1 
ATOM   3302 N N     . ARG   A 1 447 ? 48.57495  19.26217  23.78451  1.000 61.63732  ? 447 ARG   A N     1 
ATOM   3303 C CA    . ARG   A 1 447 ? 47.60264  19.32568  22.69379  1.000 61.39216  ? 447 ARG   A CA    1 
ATOM   3304 C C     . ARG   A 1 447 ? 46.20752  18.97052  23.18551  1.000 60.84114  ? 447 ARG   A C     1 
ATOM   3305 O O     . ARG   A 1 447 ? 45.21375  19.55683  22.74668  1.000 62.99253  ? 447 ARG   A O     1 
ATOM   3306 C CB    . ARG   A 1 447 ? 47.99638  18.40410  21.53655  1.000 53.35872  ? 447 ARG   A CB    1 
ATOM   3307 C CG    . ARG   A 1 447 ? 46.92043  18.35924  20.48083  1.000 51.78580  ? 447 ARG   A CG    1 
ATOM   3308 C CD    . ARG   A 1 447 ? 47.36599  17.71257  19.20362  1.000 55.35802  ? 447 ARG   A CD    1 
ATOM   3309 N NE    . ARG   A 1 447 ? 46.35330  17.88431  18.16187  1.000 59.92240  ? 447 ARG   A NE    1 
ATOM   3310 C CZ    . ARG   A 1 447 ? 46.31387  17.21536  17.01250  1.000 65.41266  ? 447 ARG   A CZ    1 
ATOM   3311 N NH1   . ARG   A 1 447 ? 47.23306  16.29579  16.70250  1.000 63.47820  ? 447 ARG   A NH1   1 
ATOM   3312 N NH2   . ARG   A 1 447 ? 45.34400  17.49203  16.14019  1.000 63.70675  ? 447 ARG   A NH2   1 
ATOM   3313 N N     . LEU   A 1 448 ? 46.12140  18.02299  24.12801  1.000 61.68517  ? 448 LEU   A N     1 
ATOM   3314 C CA    . LEU   A 1 448 ? 44.83489  17.60089  24.67860  1.000 57.81668  ? 448 LEU   A CA    1 
ATOM   3315 C C     . LEU   A 1 448 ? 44.16749  18.72469  25.48095  1.000 57.90029  ? 448 LEU   A C     1 
ATOM   3316 O O     . LEU   A 1 448 ? 42.94297  18.89236  25.43643  1.000 55.47114  ? 448 LEU   A O     1 
ATOM   3317 C CB    . LEU   A 1 448 ? 45.02538  16.34647  25.53458  1.000 55.84608  ? 448 LEU   A CB    1 
ATOM   3318 C CG    . LEU   A 1 448 ? 45.42553  15.08415  24.75670  1.000 54.51427  ? 448 LEU   A CG    1 
ATOM   3319 C CD1   . LEU   A 1 448 ? 45.99098  13.99692  25.66330  1.000 51.56862  ? 448 LEU   A CD1   1 
ATOM   3320 C CD2   . LEU   A 1 448 ? 44.25301  14.55088  23.97308  1.000 52.61905  ? 448 LEU   A CD2   1 
ATOM   3321 N N     . GLN   A 1 449 ? 44.93756  19.52372  26.21457  1.000 58.40294  ? 449 GLN   A N     1 
ATOM   3322 C CA    . GLN   A 1 449 ? 44.31948  20.69411  26.82049  1.000 58.54270  ? 449 GLN   A CA    1 
ATOM   3323 C C     . GLN   A 1 449 ? 43.85591  21.67397  25.74247  1.000 59.49162  ? 449 GLN   A C     1 
ATOM   3324 O O     . GLN   A 1 449 ? 42.83247  22.34525  25.90781  1.000 59.09390  ? 449 GLN   A O     1 
ATOM   3325 C CB    . GLN   A 1 449 ? 45.27739  21.34154  27.80290  1.000 56.22012  ? 449 GLN   A CB    1 
ATOM   3326 C CG    . GLN   A 1 449 ? 45.73033  20.34341  28.81562  1.000 57.91137  ? 449 GLN   A CG    1 
ATOM   3327 C CD    . GLN   A 1 449 ? 46.56091  20.94265  29.91543  1.000 67.31674  ? 449 GLN   A CD    1 
ATOM   3328 O OE1   . GLN   A 1 449 ? 47.73630  20.58883  30.08213  1.000 66.97915  ? 449 GLN   A OE1   1 
ATOM   3329 N NE2   . GLN   A 1 449 ? 45.96205  21.85553  30.68148  1.000 70.80533  ? 449 GLN   A NE2   1 
ATOM   3330 N N     . GLN   A 1 450 ? 44.57833  21.75376  24.61581  1.000 60.65150  ? 450 GLN   A N     1 
ATOM   3331 C CA    . GLN   A 1 450 ? 44.12059  22.60638  23.52435  1.000 62.90234  ? 450 GLN   A CA    1 
ATOM   3332 C C     . GLN   A 1 450 ? 42.75380  22.16067  23.02642  1.000 57.12415  ? 450 GLN   A C     1 
ATOM   3333 O O     . GLN   A 1 450 ? 41.84180  22.97710  22.86470  1.000 57.83113  ? 450 GLN   A O     1 
ATOM   3334 C CB    . GLN   A 1 450 ? 45.12713  22.63576  22.36750  1.000 66.95693  ? 450 GLN   A CB    1 
ATOM   3335 C CG    . GLN   A 1 450 ? 46.28823  23.62237  22.54695  1.000 85.86680  ? 450 GLN   A CG    1 
ATOM   3336 C CD    . GLN   A 1 450 ? 47.18566  23.73471  21.30148  1.000 105.23218 ? 450 GLN   A CD    1 
ATOM   3337 O OE1   . GLN   A 1 450 ? 46.90097  23.14281  20.25562  1.000 109.54866 ? 450 GLN   A OE1   1 
ATOM   3338 N NE2   . GLN   A 1 450 ? 48.25989  24.51897  21.41078  1.000 110.22866 ? 450 GLN   A NE2   1 
ATOM   3339 N N     . ILE   A 1 451 ? 42.58571  20.86351  22.78676  1.000 57.83526  ? 451 ILE   A N     1 
ATOM   3340 C CA    . ILE   A 1 451 ? 41.30789  20.36796  22.27590  1.000 60.30977  ? 451 ILE   A CA    1 
ATOM   3341 C C     . ILE   A 1 451 ? 40.23314  20.42269  23.36634  1.000 52.94347  ? 451 ILE   A C     1 
ATOM   3342 O O     . ILE   A 1 451 ? 39.11610  20.91010  23.13781  1.000 48.59581  ? 451 ILE   A O     1 
ATOM   3343 C CB    . ILE   A 1 451 ? 41.47215  18.94796  21.70097  1.000 56.76762  ? 451 ILE   A CB    1 
ATOM   3344 C CG1   . ILE   A 1 451 ? 42.60153  18.89262  20.67446  1.000 55.96854  ? 451 ILE   A CG1   1 
ATOM   3345 C CG2   . ILE   A 1 451 ? 40.18483  18.49964  21.07145  1.000 49.87960  ? 451 ILE   A CG2   1 
ATOM   3346 C CD1   . ILE   A 1 451 ? 43.21194  17.50853  20.49659  1.000 57.94351  ? 451 ILE   A CD1   1 
ATOM   3347 N N     . LYS   A 1 452 ? 40.54866  19.91152  24.55953  1.000 44.35868  ? 452 LYS   A N     1 
ATOM   3348 C CA    . LYS   A 1 452 ? 39.58965  19.94331  25.64825  1.000 45.99729  ? 452 LYS   A CA    1 
ATOM   3349 C C     . LYS   A 1 452 ? 38.93647  21.30573  25.69715  1.000 53.31507  ? 452 LYS   A C     1 
ATOM   3350 O O     . LYS   A 1 452 ? 37.71407  21.43953  25.56458  1.000 50.98907  ? 452 LYS   A O     1 
ATOM   3351 C CB    . LYS   A 1 452 ? 40.27497  19.65973  26.98875  1.000 48.64855  ? 452 LYS   A CB    1 
ATOM   3352 C CG    . LYS   A 1 452 ? 39.36215  19.86887  28.21550  1.000 49.04317  ? 452 LYS   A CG    1 
ATOM   3353 C CD    . LYS   A 1 452 ? 38.33495  18.75703  28.31909  1.000 46.17912  ? 452 LYS   A CD    1 
ATOM   3354 C CE    . LYS   A 1 452 ? 37.36802  18.94184  29.45368  1.000 51.05770  ? 452 LYS   A CE    1 
ATOM   3355 N NZ    . LYS   A 1 452 ? 36.55050  17.72275  29.70681  1.000 52.71339  ? 452 LYS   A NZ    1 
ATOM   3356 N N     . SER   A 1 453 ? 39.78326  22.32562  25.87214  1.000 56.99164  ? 453 SER   A N     1 
ATOM   3357 C CA    . SER   A 1 453 ? 39.32619  23.70550  25.97478  1.000 56.57935  ? 453 SER   A CA    1 
ATOM   3358 C C     . SER   A 1 453 ? 38.37608  24.08720  24.85295  1.000 52.04443  ? 453 SER   A C     1 
ATOM   3359 O O     . SER   A 1 453 ? 37.45747  24.86669  25.08148  1.000 54.22990  ? 453 SER   A O     1 
ATOM   3360 C CB    . SER   A 1 453 ? 40.51984  24.65082  26.00302  1.000 58.65102  ? 453 SER   A CB    1 
ATOM   3361 O OG    . SER   A 1 453 ? 41.01550  24.78852  27.33102  1.000 73.02593  ? 453 SER   A OG    1 
ATOM   3362 N N     . ALA   A 1 454 ? 38.55351  23.53202  23.65471  1.000 50.97041  ? 454 ALA   A N     1 
ATOM   3363 C CA    . ALA   A 1 454 ? 37.82014  24.00090  22.49067  1.000 47.08505  ? 454 ALA   A CA    1 
ATOM   3364 C C     . ALA   A 1 454 ? 36.52874  23.24291  22.18342  1.000 53.90551  ? 454 ALA   A C     1 
ATOM   3365 O O     . ALA   A 1 454 ? 35.68316  23.79431  21.47166  1.000 53.99578  ? 454 ALA   A O     1 
ATOM   3366 C CB    . ALA   A 1 454 ? 38.71754  23.94997  21.25706  1.000 51.02747  ? 454 ALA   A CB    1 
ATOM   3367 N N     . VAL   A 1 455 ? 36.35340  22.00151  22.65853  1.000 55.36241  ? 455 VAL   A N     1 
ATOM   3368 C CA    . VAL   A 1 455 ? 35.10195  21.25898  22.50814  1.000 49.01742  ? 455 VAL   A CA    1 
ATOM   3369 C C     . VAL   A 1 455 ? 34.42365  20.95839  23.83338  1.000 49.62912  ? 455 VAL   A C     1 
ATOM   3370 O O     . VAL   A 1 455 ? 33.40958  20.23837  23.85673  1.000 53.62036  ? 455 VAL   A O     1 
ATOM   3371 C CB    . VAL   A 1 455 ? 35.29706  19.95273  21.71644  1.000 49.50459  ? 455 VAL   A CB    1 
ATOM   3372 C CG1   . VAL   A 1 455 ? 35.78283  20.24087  20.30237  1.000 54.83317  ? 455 VAL   A CG1   1 
ATOM   3373 C CG2   . VAL   A 1 455 ? 36.25544  19.04158  22.47022  1.000 44.99751  ? 455 VAL   A CG2   1 
ATOM   3374 N N     . ASP   A 1 456 ? 34.94894  21.45554  24.92743  1.000 51.11541  ? 456 ASP   A N     1 
ATOM   3375 C CA    . ASP   A 1 456 ? 34.31867  21.30167  26.22875  1.000 57.83761  ? 456 ASP   A CA    1 
ATOM   3376 C C     . ASP   A 1 456 ? 35.01762  22.30698  27.13497  1.000 56.30971  ? 456 ASP   A C     1 
ATOM   3377 O O     . ASP   A 1 456 ? 35.97976  21.96969  27.84113  1.000 52.48323  ? 456 ASP   A O     1 
ATOM   3378 C CB    . ASP   A 1 456 ? 34.44178  19.86891  26.77010  1.000 54.47637  ? 456 ASP   A CB    1 
ATOM   3379 C CG    . ASP   A 1 456 ? 33.67259  19.67067  28.06486  1.000 54.21344  ? 456 ASP   A CG    1 
ATOM   3380 O OD1   . ASP   A 1 456 ? 32.72673  20.47196  28.31830  1.000 51.46983  ? 456 ASP   A OD1   1 
ATOM   3381 O OD2   . ASP   A 1 456 ? 34.06553  18.77700  28.86116  1.000 53.75497  ? 456 ASP   A OD2   1 
ATOM   3382 N N     . PRO   A 1 457 ? 34.62660  23.57355  27.05881  1.000 54.45318  ? 457 PRO   A N     1 
ATOM   3383 C CA    . PRO   A 1 457 ? 35.32684  24.58005  27.84919  1.000 52.70441  ? 457 PRO   A CA    1 
ATOM   3384 C C     . PRO   A 1 457 ? 34.99027  24.48813  29.30798  1.000 51.61287  ? 457 PRO   A C     1 
ATOM   3385 O O     . PRO   A 1 457 ? 35.89018  24.63312  30.14237  1.000 48.88622  ? 457 PRO   A O     1 
ATOM   3386 C CB    . PRO   A 1 457 ? 34.86994  25.89674  27.22292  1.000 52.53082  ? 457 PRO   A CB    1 
ATOM   3387 C CG    . PRO   A 1 457 ? 33.70753  25.58589  26.45076  1.000 53.60483  ? 457 PRO   A CG    1 
ATOM   3388 C CD    . PRO   A 1 457 ? 33.66496  24.15583  26.12195  1.000 52.90365  ? 457 PRO   A CD    1 
ATOM   3389 N N     . ASN   A 1 458 ? 33.72963  24.23126  29.64911  1.000 52.81922  ? 458 ASN   A N     1 
ATOM   3390 C CA    . ASN   A 1 458 ? 33.45335  23.83889  31.02787  1.000 56.92344  ? 458 ASN   A CA    1 
ATOM   3391 C C     . ASN   A 1 458 ? 33.89872  22.40078  31.17893  1.000 58.40368  ? 458 ASN   A C     1 
ATOM   3392 O O     . ASN   A 1 458 ? 34.41340  21.79246  30.24373  1.000 64.31508  ? 458 ASN   A O     1 
ATOM   3393 C CB    . ASN   A 1 458 ? 31.99222  24.05193  31.34267  1.000 51.53043  ? 458 ASN   A CB    1 
ATOM   3394 C CG    . ASN   A 1 458 ? 31.48282  25.28357  30.64102  1.000 60.02516  ? 458 ASN   A CG    1 
ATOM   3395 O OD1   . ASN   A 1 458 ? 30.64959  25.18710  29.72922  1.000 54.07574  ? 458 ASN   A OD1   1 
ATOM   3396 N ND2   . ASN   A 1 458 ? 32.05583  26.45158  30.99301  1.000 51.56286  ? 458 ASN   A ND2   1 
ATOM   3397 N N     . ASP   A 1 459 ? 33.78041  21.82847  32.34631  1.000 53.41881  ? 459 ASP   A N     1 
ATOM   3398 C CA    . ASP   A 1 459 ? 34.35259  20.49541  32.33245  1.000 52.05384  ? 459 ASP   A CA    1 
ATOM   3399 C C     . ASP   A 1 459 ? 33.22393  19.48544  32.28031  1.000 55.43550  ? 459 ASP   A C     1 
ATOM   3400 O O     . ASP   A 1 459 ? 33.18005  18.57561  33.11121  1.000 62.36152  ? 459 ASP   A O     1 
ATOM   3401 C CB    . ASP   A 1 459 ? 35.23369  20.19983  33.54925  1.000 55.16131  ? 459 ASP   A CB    1 
ATOM   3402 C CG    . ASP   A 1 459 ? 36.45901  19.31099  33.21144  1.000 63.72264  ? 459 ASP   A CG    1 
ATOM   3403 O OD1   . ASP   A 1 459 ? 36.59325  18.80694  32.06621  1.000 66.08116  ? 459 ASP   A OD1   1 
ATOM   3404 O OD2   . ASP   A 1 459 ? 37.21881  18.96350  34.13933  1.000 64.20333  ? 459 ASP   A OD2   1 
ATOM   3405 N N     . VAL   A 1 460 ? 32.29998  19.60488  31.33157  1.000 48.72134  ? 460 VAL   A N     1 
ATOM   3406 C CA    . VAL   A 1 460 ? 31.11855  18.75451  31.42802  1.000 46.01919  ? 460 VAL   A CA    1 
ATOM   3407 C C     . VAL   A 1 460 ? 31.50451  17.27413  31.53561  1.000 48.85322  ? 460 VAL   A C     1 
ATOM   3408 O O     . VAL   A 1 460 ? 30.89917  16.51116  32.29856  1.000 50.16268  ? 460 VAL   A O     1 
ATOM   3409 C CB    . VAL   A 1 460 ? 30.19064  19.03148  30.24946  1.000 43.38613  ? 460 VAL   A CB    1 
ATOM   3410 C CG1   . VAL   A 1 460 ? 28.97368  18.18126  30.37141  1.000 47.30835  ? 460 VAL   A CG1   1 
ATOM   3411 C CG2   . VAL   A 1 460 ? 29.85104  20.48012  30.26032  1.000 46.63494  ? 460 VAL   A CG2   1 
ATOM   3412 N N     . PHE   A 1 461 ? 32.54422  16.85416  30.81555  1.000 47.61900  ? 461 PHE   A N     1 
ATOM   3413 C CA    . PHE   A 1 461 ? 33.01459  15.47463  30.81295  1.000 44.87779  ? 461 PHE   A CA    1 
ATOM   3414 C C     . PHE   A 1 461 ? 34.23914  15.37989  31.69824  1.000 46.36072  ? 461 PHE   A C     1 
ATOM   3415 O O     . PHE   A 1 461 ? 35.35535  15.66433  31.25745  1.000 50.69234  ? 461 PHE   A O     1 
ATOM   3416 C CB    . PHE   A 1 461 ? 33.34681  15.06033  29.39371  1.000 47.20211  ? 461 PHE   A CB    1 
ATOM   3417 C CG    . PHE   A 1 461 ? 32.17981  15.06480  28.50599  1.000 45.17721  ? 461 PHE   A CG    1 
ATOM   3418 C CD1   . PHE   A 1 461 ? 31.06588  14.31778  28.82180  1.000 45.64859  ? 461 PHE   A CD1   1 
ATOM   3419 C CD2   . PHE   A 1 461 ? 32.16555  15.85957  27.38120  1.000 45.49288  ? 461 PHE   A CD2   1 
ATOM   3420 C CE1   . PHE   A 1 461 ? 29.97594  14.31487  28.00050  1.000 45.70729  ? 461 PHE   A CE1   1 
ATOM   3421 C CE2   . PHE   A 1 461 ? 31.08456  15.88000  26.55213  1.000 46.95689  ? 461 PHE   A CE2   1 
ATOM   3422 C CZ    . PHE   A 1 461 ? 29.97387  15.10791  26.86390  1.000 46.37616  ? 461 PHE   A CZ    1 
ATOM   3423 N N     . HIS   A 1 462 ? 34.04263  14.92809  32.92742  1.000 46.64369  ? 462 HIS   A N     1 
ATOM   3424 C CA    . HIS   A 1 462 ? 35.00812  15.12720  34.00694  1.000 51.81581  ? 462 HIS   A CA    1 
ATOM   3425 C C     . HIS   A 1 462 ? 35.17224  13.86581  34.85199  1.000 50.59356  ? 462 HIS   A C     1 
ATOM   3426 O O     . HIS   A 1 462 ? 34.20641  13.14600  35.11610  1.000 48.41553  ? 462 HIS   A O     1 
ATOM   3427 C CB    . HIS   A 1 462 ? 34.56446  16.28780  34.93638  1.000 53.67386  ? 462 HIS   A CB    1 
ATOM   3428 C CG    . HIS   A 1 462 ? 35.43887  16.46242  36.13035  1.000 51.34724  ? 462 HIS   A CG    1 
ATOM   3429 N ND1   . HIS   A 1 462 ? 36.66210  17.08288  36.06141  1.000 54.75366  ? 462 HIS   A ND1   1 
ATOM   3430 C CD2   . HIS   A 1 462 ? 35.30057  16.04402  37.40656  1.000 50.97652  ? 462 HIS   A CD2   1 
ATOM   3431 C CE1   . HIS   A 1 462 ? 37.23803  17.05058  37.24927  1.000 55.24067  ? 462 HIS   A CE1   1 
ATOM   3432 N NE2   . HIS   A 1 462 ? 36.43240  16.42751  38.08421  1.000 49.81389  ? 462 HIS   A NE2   1 
ATOM   3433 N N     . ASN   A 1 463 ? 36.39134  13.61034  35.30538  1.000 50.77194  ? 463 ASN   A N     1 
ATOM   3434 C CA    . ASN   A 1 463 ? 36.57362  12.57788  36.30809  1.000 52.13417  ? 463 ASN   A CA    1 
ATOM   3435 C C     . ASN   A 1 463 ? 37.83079  12.92547  37.09624  1.000 55.74429  ? 463 ASN   A C     1 
ATOM   3436 O O     . ASN   A 1 463 ? 38.35144  14.03933  36.99087  1.000 53.35769  ? 463 ASN   A O     1 
ATOM   3437 C CB    . ASN   A 1 463 ? 36.57534  11.18824  35.65607  1.000 50.31113  ? 463 ASN   A CB    1 
ATOM   3438 C CG    . ASN   A 1 463 ? 37.74950  10.97341  34.75268  1.000 57.74650  ? 463 ASN   A CG    1 
ATOM   3439 O OD1   . ASN   A 1 463 ? 38.85627  10.71520  35.22493  1.000 64.42326  ? 463 ASN   A OD1   1 
ATOM   3440 N ND2   . ASN   A 1 463 ? 37.51957  11.03079  33.44038  1.000 57.88183  ? 463 ASN   A ND2   1 
ATOM   3441 N N     . GLN   A 1 464 ? 38.30425  11.98606  37.91594  1.000 56.17156  ? 464 GLN   A N     1 
ATOM   3442 C CA    . GLN   A 1 464 ? 39.42519  12.30599  38.79525  1.000 56.05545  ? 464 GLN   A CA    1 
ATOM   3443 C C     . GLN   A 1 464 ? 40.68595  12.67986  38.02756  1.000 56.86009  ? 464 GLN   A C     1 
ATOM   3444 O O     . GLN   A 1 464 ? 41.47745  13.50441  38.49198  1.000 63.99957  ? 464 GLN   A O     1 
ATOM   3445 C CB    . GLN   A 1 464 ? 39.70441  11.14077  39.72442  1.000 53.82230  ? 464 GLN   A CB    1 
ATOM   3446 C CG    . GLN   A 1 464 ? 40.81775  11.39292  40.67952  1.000 55.66139  ? 464 GLN   A CG    1 
ATOM   3447 C CD    . GLN   A 1 464 ? 40.85837  10.33943  41.72897  1.000 59.95880  ? 464 GLN   A CD    1 
ATOM   3448 O OE1   . GLN   A 1 464 ? 39.87685  10.16249  42.44914  1.000 71.57255  ? 464 GLN   A OE1   1 
ATOM   3449 N NE2   . GLN   A 1 464 ? 41.95191  9.59138   41.79931  1.000 58.72650  ? 464 GLN   A NE2   1 
ATOM   3450 N N     . GLN   A 1 465 ? 40.89007  12.10404  36.86255  1.000 52.74803  ? 465 GLN   A N     1 
ATOM   3451 C CA    . GLN   A 1 465 ? 42.11182  12.30524  36.10773  1.000 55.95810  ? 465 GLN   A CA    1 
ATOM   3452 C C     . GLN   A 1 465 ? 41.77330  12.61427  34.64496  1.000 58.16528  ? 465 GLN   A C     1 
ATOM   3453 O O     . GLN   A 1 465 ? 42.46263  12.18275  33.68601  1.000 52.29041  ? 465 GLN   A O     1 
ATOM   3454 C CB    . GLN   A 1 465 ? 43.00041  11.07564  36.27718  1.000 54.91105  ? 465 GLN   A CB    1 
ATOM   3455 C CG    . GLN   A 1 465 ? 43.33954  10.87550  37.74688  1.000 53.32820  ? 465 GLN   A CG    1 
ATOM   3456 C CD    . GLN   A 1 465 ? 43.76901  9.46767   38.05877  1.000 57.08259  ? 465 GLN   A CD    1 
ATOM   3457 O OE1   . GLN   A 1 465 ? 43.56850  8.57000   37.24927  1.000 57.86566  ? 465 GLN   A OE1   1 
ATOM   3458 N NE2   . GLN   A 1 465 ? 44.38711  9.26396   39.23012  1.000 59.21631  ? 465 GLN   A NE2   1 
ATOM   3459 N N     . SER   A 1 466 ? 40.68361  13.35504  34.46929  1.000 55.95573  ? 466 SER   A N     1 
ATOM   3460 C CA    . SER   A 1 466 ? 40.29089  13.79941  33.15149  1.000 51.66306  ? 466 SER   A CA    1 
ATOM   3461 C C     . SER   A 1 466 ? 41.23983  14.90375  32.73193  1.000 51.17734  ? 466 SER   A C     1 
ATOM   3462 O O     . SER   A 1 466 ? 42.03384  15.40385  33.52101  1.000 50.65655  ? 466 SER   A O     1 
ATOM   3463 C CB    . SER   A 1 466 ? 38.85766  14.28507  33.14934  1.000 47.98442  ? 466 SER   A CB    1 
ATOM   3464 O OG    . SER   A 1 466 ? 38.80206  15.60702  33.63396  1.000 49.74816  ? 466 SER   A OG    1 
ATOM   3465 N N     . ILE   A 1 467 ? 41.17186  15.28474  31.47051  1.000 56.21499  ? 467 ILE   A N     1 
ATOM   3466 C CA    . ILE   A 1 467 ? 42.06972  16.29180  30.92257  1.000 52.77287  ? 467 ILE   A CA    1 
ATOM   3467 C C     . ILE   A 1 467 ? 41.43168  17.65440  31.15369  1.000 54.49999  ? 467 ILE   A C     1 
ATOM   3468 O O     . ILE   A 1 467 ? 40.30080  17.87672  30.68788  1.000 57.74799  ? 467 ILE   A O     1 
ATOM   3469 C CB    . ILE   A 1 467 ? 42.34333  16.04417  29.44377  1.000 48.05741  ? 467 ILE   A CB    1 
ATOM   3470 C CG1   . ILE   A 1 467 ? 43.24309  14.80105  29.36404  1.000 47.93678  ? 467 ILE   A CG1   1 
ATOM   3471 C CG2   . ILE   A 1 467 ? 42.97029  17.30493  28.85545  1.000 46.61252  ? 467 ILE   A CG2   1 
ATOM   3472 C CD1   . ILE   A 1 467 ? 43.02162  13.92743  28.19726  1.000 43.61743  ? 467 ILE   A CD1   1 
ATOM   3473 N N     . PRO   A 1 468 ? 42.08935  18.56629  31.86884  1.000 54.45288  ? 468 PRO   A N     1 
ATOM   3474 C CA    . PRO   A 1 468 ? 41.44500  19.81599  32.25682  1.000 58.11185  ? 468 PRO   A CA    1 
ATOM   3475 C C     . PRO   A 1 468 ? 41.83073  20.92277  31.29609  1.000 59.86888  ? 468 PRO   A C     1 
ATOM   3476 O O     . PRO   A 1 468 ? 42.95019  20.92537  30.75355  1.000 61.71011  ? 468 PRO   A O     1 
ATOM   3477 C CB    . PRO   A 1 468 ? 42.04072  20.07361  33.63646  1.000 60.33687  ? 468 PRO   A CB    1 
ATOM   3478 C CG    . PRO   A 1 468 ? 43.47863  19.64843  33.42408  1.000 54.02904  ? 468 PRO   A CG    1 
ATOM   3479 C CD    . PRO   A 1 468 ? 43.44064  18.47462  32.43798  1.000 49.85456  ? 468 PRO   A CD    1 
ATOM   3480 N N     . PRO   A 1 469 ? 40.96438  21.90315  31.09641  1.000 58.57762  ? 469 PRO   A N     1 
ATOM   3481 C CA    . PRO   A 1 469 ? 41.19671  22.89059  30.03075  1.000 63.85848  ? 469 PRO   A CA    1 
ATOM   3482 C C     . PRO   A 1 469 ? 42.12579  24.03807  30.43811  1.000 67.41679  ? 469 PRO   A C     1 
ATOM   3483 O O     . PRO   A 1 469 ? 42.33888  24.33040  31.61847  1.000 75.69094  ? 469 PRO   A O     1 
ATOM   3484 C CB    . PRO   A 1 469 ? 39.78123  23.37473  29.69553  1.000 57.95387  ? 469 PRO   A CB    1 
ATOM   3485 C CG    . PRO   A 1 469 ? 39.01365  23.17357  30.97967  1.000 60.62003  ? 469 PRO   A CG    1 
ATOM   3486 C CD    . PRO   A 1 469 ? 39.68377  22.08401  31.79203  1.000 51.08091  ? 469 PRO   A CD    1 
ATOM   3487 N N     . LEU   A 1 470 ? 42.68977  24.68051  29.41218  1.000 64.48801  ? 470 LEU   A N     1 
ATOM   3488 C CA    . LEU   A 1 470 ? 43.82362  25.58145  29.58614  1.000 75.81182  ? 470 LEU   A CA    1 
ATOM   3489 C C     . LEU   A 1 470 ? 43.49414  26.77029  30.49916  1.000 94.91013  ? 470 LEU   A C     1 
ATOM   3490 O O     . LEU   A 1 470 ? 42.33080  27.06977  30.80877  1.000 93.78633  ? 470 LEU   A O     1 
ATOM   3491 C CB    . LEU   A 1 470 ? 44.31220  26.08161  28.22134  1.000 64.93975  ? 470 LEU   A CB    1 
ATOM   3492 C CG    . LEU   A 1 470 ? 45.00895  24.99562  27.39640  1.000 66.92913  ? 470 LEU   A CG    1 
ATOM   3493 C CD1   . LEU   A 1 470 ? 45.28332  25.37547  25.94993  1.000 59.45916  ? 470 LEU   A CD1   1 
ATOM   3494 C CD2   . LEU   A 1 470 ? 46.31794  24.63594  28.07560  1.000 73.11778  ? 470 LEU   A CD2   1 
ATOM   3495 N N     . SER   A 1 471 ? 44.55456  27.45020  30.93910  1.000 107.01663 ? 471 SER   A N     1 
ATOM   3496 C CA    . SER   A 1 471 ? 44.43344  28.71700  31.66641  1.000 105.97000 ? 471 SER   A CA    1 
ATOM   3497 C C     . SER   A 1 471 ? 45.33164  29.82945  31.10816  1.000 115.10625 ? 471 SER   A C     1 
ATOM   3498 O O     . SER   A 1 471 ? 46.56663  29.74500  31.17501  1.000 122.39104 ? 471 SER   A O     1 
ATOM   3499 C CB    . SER   A 1 471 ? 44.74163  28.48537  33.13112  1.000 104.36739 ? 471 SER   A CB    1 
ATOM   3500 O OG    . SER   A 1 471 ? 43.70854  27.68465  33.66751  1.000 96.76499  ? 471 SER   A OG    1 
ATOM   3501 O OXT   . SER   A 1 471 ? 44.83296  30.83534  30.58482  1.000 115.91881 ? 471 SER   A OXT   1 
ATOM   3502 N N     . SER   B 1 5   ? 101.23293 28.85369  32.15005  1.000 64.10019  ? 5   SER   B N     1 
ATOM   3503 C CA    . SER   B 1 5   ? 102.60564 28.46916  32.49625  1.000 75.93430  ? 5   SER   B CA    1 
ATOM   3504 C C     . SER   B 1 5   ? 102.73423 26.97574  32.60577  1.000 80.75761  ? 5   SER   B C     1 
ATOM   3505 O O     . SER   B 1 5   ? 103.42497 26.34230  31.80360  1.000 86.11866  ? 5   SER   B O     1 
ATOM   3506 C CB    . SER   B 1 5   ? 103.06464 29.08498  33.81427  1.000 84.80860  ? 5   SER   B CB    1 
ATOM   3507 O OG    . SER   B 1 5   ? 104.17485 28.35750  34.35037  1.000 82.41351  ? 5   SER   B OG    1 
ATOM   3508 N N     . ALA   B 1 6   ? 102.11380 26.40274  33.63732  1.000 77.87660  ? 6   ALA   B N     1 
ATOM   3509 C CA    . ALA   B 1 6   ? 101.93390 24.95632  33.63255  1.000 78.96691  ? 6   ALA   B CA    1 
ATOM   3510 C C     . ALA   B 1 6   ? 101.15246 24.54750  32.39179  1.000 75.79854  ? 6   ALA   B C     1 
ATOM   3511 O O     . ALA   B 1 6   ? 101.65488 23.81792  31.52615  1.000 71.06337  ? 6   ALA   B O     1 
ATOM   3512 C CB    . ALA   B 1 6   ? 101.21670 24.50715  34.91050  1.000 80.39108  ? 6   ALA   B CB    1 
ATOM   3513 N N     . PHE   B 1 7   ? 99.93826  25.09795  32.26443  1.000 75.04399  ? 7   PHE   B N     1 
ATOM   3514 C CA    . PHE   B 1 7   ? 99.06985  24.86594  31.11526  1.000 67.70703  ? 7   PHE   B CA    1 
ATOM   3515 C C     . PHE   B 1 7   ? 99.81376  25.17516  29.80340  1.000 65.97892  ? 7   PHE   B C     1 
ATOM   3516 O O     . PHE   B 1 7   ? 99.89181  24.32594  28.90640  1.000 62.22934  ? 7   PHE   B O     1 
ATOM   3517 C CB    . PHE   B 1 7   ? 97.77913  25.69725  31.34354  1.000 60.87371  ? 7   PHE   B CB    1 
ATOM   3518 C CG    . PHE   B 1 7   ? 96.73654  25.65641  30.23292  1.000 61.05503  ? 7   PHE   B CG    1 
ATOM   3519 C CD1   . PHE   B 1 7   ? 96.03777  24.49377  29.93270  1.000 62.18555  ? 7   PHE   B CD1   1 
ATOM   3520 C CD2   . PHE   B 1 7   ? 96.39827  26.81877  29.54050  1.000 61.01571  ? 7   PHE   B CD2   1 
ATOM   3521 C CE1   . PHE   B 1 7   ? 95.06025  24.47992  28.91453  1.000 60.54921  ? 7   PHE   B CE1   1 
ATOM   3522 C CE2   . PHE   B 1 7   ? 95.42518  26.81096  28.53473  1.000 59.13435  ? 7   PHE   B CE2   1 
ATOM   3523 C CZ    . PHE   B 1 7   ? 94.75587  25.63692  28.22334  1.000 57.58407  ? 7   PHE   B CZ    1 
ATOM   3524 N N     . ALA   B 1 8   ? 100.46010 26.33856  29.70088  1.000 65.68211  ? 8   ALA   B N     1 
ATOM   3525 C CA    . ALA   B 1 8   ? 101.11197 26.64789  28.42385  1.000 69.88124  ? 8   ALA   B CA    1 
ATOM   3526 C C     . ALA   B 1 8   ? 102.24635 25.66723  28.10300  1.000 70.97824  ? 8   ALA   B C     1 
ATOM   3527 O O     . ALA   B 1 8   ? 102.45266 25.30645  26.93883  1.000 62.84615  ? 8   ALA   B O     1 
ATOM   3528 C CB    . ALA   B 1 8   ? 101.62627 28.08653  28.41146  1.000 64.79059  ? 8   ALA   B CB    1 
ATOM   3529 N N     . THR   B 1 9   ? 103.00060 25.22950  29.11332  1.000 71.93054  ? 9   THR   B N     1 
ATOM   3530 C CA    . THR   B 1 9   ? 104.09029 24.30314  28.83752  1.000 67.33119  ? 9   THR   B CA    1 
ATOM   3531 C C     . THR   B 1 9   ? 103.55911 22.95309  28.37026  1.000 69.73321  ? 9   THR   B C     1 
ATOM   3532 O O     . THR   B 1 9   ? 103.91111 22.48678  27.27672  1.000 69.29584  ? 9   THR   B O     1 
ATOM   3533 C CB    . THR   B 1 9   ? 104.99489 24.16144  30.06264  1.000 64.47171  ? 9   THR   B CB    1 
ATOM   3534 O OG1   . THR   B 1 9   ? 105.87903 25.28925  30.12979  1.000 64.15589  ? 9   THR   B OG1   1 
ATOM   3535 C CG2   . THR   B 1 9   ? 105.81843 22.91161  29.96920  1.000 61.91259  ? 9   THR   B CG2   1 
ATOM   3536 N N     . CYS   B 1 10  ? 102.69033 22.31994  29.17583  1.000 73.17157  ? 10  CYS   B N     1 
ATOM   3537 C CA    . CYS   B 1 10  ? 102.01796 21.08009  28.75830  1.000 71.88339  ? 10  CYS   B CA    1 
ATOM   3538 C C     . CYS   B 1 10  ? 101.50360 21.17508  27.33204  1.000 70.22672  ? 10  CYS   B C     1 
ATOM   3539 O O     . CYS   B 1 10  ? 101.55478 20.19486  26.58096  1.000 70.03624  ? 10  CYS   B O     1 
ATOM   3540 C CB    . CYS   B 1 10  ? 100.83361 20.75526  29.67243  1.000 76.59866  ? 10  CYS   B CB    1 
ATOM   3541 S SG    . CYS   B 1 10  ? 99.81561  19.30808  29.15221  1.000 107.31160 ? 10  CYS   B SG    1 
ATOM   3542 N N     . LEU   B 1 11  ? 100.94921 22.32879  26.96613  1.000 71.03403  ? 11  LEU   B N     1 
ATOM   3543 C CA    . LEU   B 1 11  ? 100.23207 22.46878  25.70649  1.000 68.23845  ? 11  LEU   B CA    1 
ATOM   3544 C C     . LEU   B 1 11  ? 101.18202 22.56698  24.52827  1.000 65.42656  ? 11  LEU   B C     1 
ATOM   3545 O O     . LEU   B 1 11  ? 100.86261 22.09652  23.42986  1.000 65.77191  ? 11  LEU   B O     1 
ATOM   3546 C CB    . LEU   B 1 11  ? 99.31610  23.69183  25.78856  1.000 68.20080  ? 11  LEU   B CB    1 
ATOM   3547 C CG    . LEU   B 1 11  ? 97.98986  23.61581  25.06795  1.000 66.84235  ? 11  LEU   B CG    1 
ATOM   3548 C CD1   . LEU   B 1 11  ? 97.07272  22.66781  25.81102  1.000 63.58866  ? 11  LEU   B CD1   1 
ATOM   3549 C CD2   . LEU   B 1 11  ? 97.43811  25.02964  25.03727  1.000 69.13866  ? 11  LEU   B CD2   1 
ATOM   3550 N N     . LEU   B 1 12  ? 102.35420 23.16509  24.73445  1.000 67.12127  ? 12  LEU   B N     1 
ATOM   3551 C CA    . LEU   B 1 12  ? 103.39508 23.06690  23.72035  1.000 65.61418  ? 12  LEU   B CA    1 
ATOM   3552 C C     . LEU   B 1 12  ? 103.84296 21.62548  23.57642  1.000 62.92380  ? 12  LEU   B C     1 
ATOM   3553 O O     . LEU   B 1 12  ? 104.01435 21.13887  22.46090  1.000 65.46322  ? 12  LEU   B O     1 
ATOM   3554 C CB    . LEU   B 1 12  ? 104.55235 23.99346  24.07074  1.000 62.10099  ? 12  LEU   B CB    1 
ATOM   3555 C CG    . LEU   B 1 12  ? 105.65165 24.24245  23.05413  1.000 56.22435  ? 12  LEU   B CG    1 
ATOM   3556 C CD1   . LEU   B 1 12  ? 105.04193 24.54042  21.71700  1.000 66.79257  ? 12  LEU   B CD1   1 
ATOM   3557 C CD2   . LEU   B 1 12  ? 106.37257 25.47271  23.51948  1.000 56.27123  ? 12  LEU   B CD2   1 
ATOM   3558 N N     . ALA   B 1 13  ? 103.95882 20.90019  24.69424  1.000 61.52134  ? 13  ALA   B N     1 
ATOM   3559 C CA    . ALA   B 1 13  ? 104.18524 19.45116  24.62512  1.000 59.72077  ? 13  ALA   B CA    1 
ATOM   3560 C C     . ALA   B 1 13  ? 103.15835 18.75157  23.74946  1.000 63.11478  ? 13  ALA   B C     1 
ATOM   3561 O O     . ALA   B 1 13  ? 103.51931 17.90364  22.92597  1.000 64.09038  ? 13  ALA   B O     1 
ATOM   3562 C CB    . ALA   B 1 13  ? 104.14702 18.82249  26.01144  1.000 65.12863  ? 13  ALA   B CB    1 
ATOM   3563 N N     . SER   B 1 14  ? 101.86937 19.04801  23.94426  1.000 66.95100  ? 14  SER   B N     1 
ATOM   3564 C CA    . SER   B 1 14  ? 100.84706 18.26490  23.25928  1.000 62.17604  ? 14  SER   B CA    1 
ATOM   3565 C C     . SER   B 1 14  ? 101.00291 18.35193  21.74940  1.000 65.26224  ? 14  SER   B C     1 
ATOM   3566 O O     . SER   B 1 14  ? 100.70405 17.37710  21.04708  1.000 70.41925  ? 14  SER   B O     1 
ATOM   3567 C CB    . SER   B 1 14  ? 99.43896  18.71064  23.67072  1.000 62.77171  ? 14  SER   B CB    1 
ATOM   3568 O OG    . SER   B 1 14  ? 98.93713  19.71248  22.79948  1.000 63.87775  ? 14  SER   B OG    1 
ATOM   3569 N N     . VAL   B 1 15  ? 101.46298 19.49229  21.23396  1.000 58.92471  ? 15  VAL   B N     1 
ATOM   3570 C CA    . VAL   B 1 15  ? 101.74753 19.62734  19.80394  1.000 63.89543  ? 15  VAL   B CA    1 
ATOM   3571 C C     . VAL   B 1 15  ? 103.21843 19.36131  19.49584  1.000 63.97166  ? 15  VAL   B C     1 
ATOM   3572 O O     . VAL   B 1 15  ? 103.71343 19.77654  18.44455  1.000 66.89655  ? 15  VAL   B O     1 
ATOM   3573 C CB    . VAL   B 1 15  ? 101.32128 20.99273  19.24389  1.000 66.04436  ? 15  VAL   B CB    1 
ATOM   3574 C CG1   . VAL   B 1 15  ? 99.80559  21.08920  19.15449  1.000 65.76602  ? 15  VAL   B CG1   1 
ATOM   3575 C CG2   . VAL   B 1 15  ? 101.95257 22.13139  20.06370  1.000 63.79322  ? 15  VAL   B CG2   1 
ATOM   3576 N N     . GLY   B 1 16  ? 103.92676 18.69604  20.39857  1.000 59.43615  ? 16  GLY   B N     1 
ATOM   3577 C CA    . GLY   B 1 16  ? 105.31605 18.35866  20.11736  1.000 61.04136  ? 16  GLY   B CA    1 
ATOM   3578 C C     . GLY   B 1 16  ? 106.17523 19.55570  19.78976  1.000 59.17424  ? 16  GLY   B C     1 
ATOM   3579 O O     . GLY   B 1 16  ? 106.94357 19.52741  18.82190  1.000 65.82474  ? 16  GLY   B O     1 
ATOM   3580 N N     . GLY   B 1 17  ? 106.04631 20.62395  20.56978  1.000 61.21012  ? 17  GLY   B N     1 
ATOM   3581 C CA    . GLY   B 1 17  ? 106.92795 21.76237  20.48127  1.000 64.78350  ? 17  GLY   B CA    1 
ATOM   3582 C C     . GLY   B 1 17  ? 106.70813 22.66706  19.29481  1.000 69.06787  ? 17  GLY   B C     1 
ATOM   3583 O O     . GLY   B 1 17  ? 107.35273 23.73264  19.22971  1.000 71.23820  ? 17  GLY   B O     1 
ATOM   3584 N N     . ASN   B 1 18  ? 105.84167 22.28935  18.34458  1.000 61.48710  ? 18  ASN   B N     1 
ATOM   3585 C CA    . ASN   B 1 18  ? 105.53403 23.24746  17.29500  1.000 65.04217  ? 18  ASN   B CA    1 
ATOM   3586 C C     . ASN   B 1 18  ? 104.90065 24.47459  17.92162  1.000 69.91686  ? 18  ASN   B C     1 
ATOM   3587 O O     . ASN   B 1 18  ? 103.70299 24.46030  18.23415  1.000 66.66670  ? 18  ASN   B O     1 
ATOM   3588 C CB    . ASN   B 1 18  ? 104.61353 22.67427  16.23852  1.000 64.57342  ? 18  ASN   B CB    1 
ATOM   3589 C CG    . ASN   B 1 18  ? 104.48146 23.59445  15.06383  1.000 66.14484  ? 18  ASN   B CG    1 
ATOM   3590 O OD1   . ASN   B 1 18  ? 104.93956 24.74705  15.09787  1.000 67.73682  ? 18  ASN   B OD1   1 
ATOM   3591 N ND2   . ASN   B 1 18  ? 103.83008 23.11500  14.02787  1.000 67.14681  ? 18  ASN   B ND2   1 
ATOM   3592 N N     . SER   B 1 19  ? 105.70136 25.52879  18.12740  1.000 66.88262  ? 19  SER   B N     1 
ATOM   3593 C CA    . SER   B 1 19  ? 105.16543 26.67315  18.83575  1.000 64.43441  ? 19  SER   B CA    1 
ATOM   3594 C C     . SER   B 1 19  ? 104.22980 27.48841  17.95814  1.000 70.67617  ? 19  SER   B C     1 
ATOM   3595 O O     . SER   B 1 19  ? 103.61414 28.43483  18.46857  1.000 76.59907  ? 19  SER   B O     1 
ATOM   3596 C CB    . SER   B 1 19  ? 106.29068 27.55431  19.38513  1.000 68.91728  ? 19  SER   B CB    1 
ATOM   3597 O OG    . SER   B 1 19  ? 106.97924 28.24513  18.35354  1.000 79.85047  ? 19  SER   B OG    1 
ATOM   3598 N N     . SER   B 1 20  ? 104.08078 27.13750  16.67915  1.000 62.32327  ? 20  SER   B N     1 
ATOM   3599 C CA    . SER   B 1 20  ? 103.04635 27.72993  15.84470  1.000 63.42223  ? 20  SER   B CA    1 
ATOM   3600 C C     . SER   B 1 20  ? 101.80398 26.85634  15.75602  1.000 65.09167  ? 20  SER   B C     1 
ATOM   3601 O O     . SER   B 1 20  ? 100.95660 27.07312  14.88428  1.000 69.13121  ? 20  SER   B O     1 
ATOM   3602 C CB    . SER   B 1 20  ? 103.60180 28.04307  14.46503  1.000 68.62672  ? 20  SER   B CB    1 
ATOM   3603 O OG    . SER   B 1 20  ? 104.60158 29.04199  14.56481  1.000 78.35663  ? 20  SER   B OG    1 
ATOM   3604 N N     . ALA   B 1 21  ? 101.68622 25.87876  16.65401  1.000 66.96441  ? 21  ALA   B N     1 
ATOM   3605 C CA    . ALA   B 1 21  ? 100.46953 25.11703  16.89890  1.000 65.44048  ? 21  ALA   B CA    1 
ATOM   3606 C C     . ALA   B 1 21  ? 99.88229  25.43103  18.27871  1.000 65.40402  ? 21  ALA   B C     1 
ATOM   3607 O O     . ALA   B 1 21  ? 99.10113  24.64586  18.82929  1.000 63.77446  ? 21  ALA   B O     1 
ATOM   3608 C CB    . ALA   B 1 21  ? 100.76156 23.62301  16.75271  1.000 62.32753  ? 21  ALA   B CB    1 
ATOM   3609 N N     . VAL   B 1 22  ? 100.26019 26.56225  18.85743  1.000 62.87571  ? 22  VAL   B N     1 
ATOM   3610 C CA    . VAL   B 1 22  ? 99.71245  27.01328  20.12524  1.000 61.11519  ? 22  VAL   B CA    1 
ATOM   3611 C C     . VAL   B 1 22  ? 99.63443  28.52907  20.07368  1.000 68.13627  ? 22  VAL   B C     1 
ATOM   3612 O O     . VAL   B 1 22  ? 100.59474 29.19690  19.66711  1.000 65.21834  ? 22  VAL   B O     1 
ATOM   3613 C CB    . VAL   B 1 22  ? 100.56809 26.56006  21.31544  1.000 63.90896  ? 22  VAL   B CB    1 
ATOM   3614 C CG1   . VAL   B 1 22  ? 100.74375 25.07557  21.28670  1.000 62.12866  ? 22  VAL   B CG1   1 
ATOM   3615 C CG2   . VAL   B 1 22  ? 101.91297 27.25657  21.28022  1.000 74.03175  ? 22  VAL   B CG2   1 
ATOM   3616 N N     . ALA   B 1 23  ? 98.48049  29.06360  20.47340  1.000 72.14603  ? 23  ALA   B N     1 
ATOM   3617 C CA    . ALA   B 1 23  ? 98.17671  30.49023  20.46406  1.000 74.29140  ? 23  ALA   B CA    1 
ATOM   3618 C C     . ALA   B 1 23  ? 97.62350  30.91204  21.81940  1.000 75.56047  ? 23  ALA   B C     1 
ATOM   3619 O O     . ALA   B 1 23  ? 96.61113  30.36716  22.27680  1.000 75.16620  ? 23  ALA   B O     1 
ATOM   3620 C CB    . ALA   B 1 23  ? 97.14974  30.82624  19.37426  1.000 67.14975  ? 23  ALA   B CB    1 
ATOM   3621 N N     . PHE   B 1 24  ? 98.26017  31.89162  22.45274  1.000 73.74195  ? 24  PHE   B N     1 
ATOM   3622 C CA    . PHE   B 1 24  ? 97.68513  32.37269  23.70181  1.000 72.69315  ? 24  PHE   B CA    1 
ATOM   3623 C C     . PHE   B 1 24  ? 97.17994  33.79560  23.56288  1.000 78.70385  ? 24  PHE   B C     1 
ATOM   3624 O O     . PHE   B 1 24  ? 97.68767  34.56075  22.73082  1.000 80.51122  ? 24  PHE   B O     1 
ATOM   3625 C CB    . PHE   B 1 24  ? 98.72933  32.29699  24.80149  1.000 69.39786  ? 24  PHE   B CB    1 
ATOM   3626 C CG    . PHE   B 1 24  ? 99.17044  30.93399  25.08612  1.000 68.91095  ? 24  PHE   B CG    1 
ATOM   3627 C CD1   . PHE   B 1 24  ? 98.35752  30.08908  25.81184  1.000 66.63732  ? 24  PHE   B CD1   1 
ATOM   3628 C CD2   . PHE   B 1 24  ? 100.34551 30.45358  24.55464  1.000 73.23168  ? 24  PHE   B CD2   1 
ATOM   3629 C CE1   . PHE   B 1 24  ? 98.75252  28.80699  26.07013  1.000 66.36516  ? 24  PHE   B CE1   1 
ATOM   3630 C CE2   . PHE   B 1 24  ? 100.74203 29.16502  24.79640  1.000 73.44503  ? 24  PHE   B CE2   1 
ATOM   3631 C CZ    . PHE   B 1 24  ? 99.95155  28.34062  25.55541  1.000 70.47027  ? 24  PHE   B CZ    1 
ATOM   3632 N N     . PRO   B 1 25  ? 96.18819  34.19796  24.36936  1.000 81.43010  ? 25  PRO   B N     1 
ATOM   3633 C CA    . PRO   B 1 25  ? 95.65989  35.58095  24.26696  1.000 75.83179  ? 25  PRO   B CA    1 
ATOM   3634 C C     . PRO   B 1 25  ? 96.68209  36.71665  24.28757  1.000 75.67276  ? 25  PRO   B C     1 
ATOM   3635 O O     . PRO   B 1 25  ? 96.38404  37.79933  23.76442  1.000 76.86220  ? 25  PRO   B O     1 
ATOM   3636 C CB    . PRO   B 1 25  ? 94.70567  35.67497  25.47552  1.000 75.12087  ? 25  PRO   B CB    1 
ATOM   3637 C CG    . PRO   B 1 25  ? 94.48160  34.28467  25.94992  1.000 70.66348  ? 25  PRO   B CG    1 
ATOM   3638 C CD    . PRO   B 1 25  ? 95.58825  33.41599  25.46663  1.000 76.36085  ? 25  PRO   B CD    1 
ATOM   3639 N N     . ASN   B 1 26  ? 97.88594  36.53351  24.83707  1.000 71.25430  ? 26  ASN   B N     1 
ATOM   3640 C CA    . ASN   B 1 26  ? 98.83155  37.65039  24.80650  1.000 82.40392  ? 26  ASN   B CA    1 
ATOM   3641 C C     . ASN   B 1 26  ? 99.38594  37.99133  23.41217  1.000 89.17919  ? 26  ASN   B C     1 
ATOM   3642 O O     . ASN   B 1 26  ? 99.90047  39.10076  23.25199  1.000 86.68286  ? 26  ASN   B O     1 
ATOM   3643 C CB    . ASN   B 1 26  ? 99.96402  37.40430  25.80867  1.000 80.29999  ? 26  ASN   B CB    1 
ATOM   3644 C CG    . ASN   B 1 26  ? 100.70331 36.13346  25.54376  1.000 89.34742  ? 26  ASN   B CG    1 
ATOM   3645 O OD1   . ASN   B 1 26  ? 100.19789 35.29522  24.79933  1.000 94.43866  ? 26  ASN   B OD1   1 
ATOM   3646 N ND2   . ASN   B 1 26  ? 101.91523 35.99685  26.07499  1.000 101.34203 ? 26  ASN   B ND2   1 
ATOM   3647 N N     . GLN   B 1 27  ? 99.24405  37.10437  22.40286  1.000 89.35879  ? 27  GLN   B N     1 
ATOM   3648 C CA    . GLN   B 1 27  ? 99.80806  37.27458  21.05364  1.000 75.10409  ? 27  GLN   B CA    1 
ATOM   3649 C C     . GLN   B 1 27  ? 98.97417  38.20950  20.19611  1.000 82.59488  ? 27  GLN   B C     1 
ATOM   3650 O O     . GLN   B 1 27  ? 97.75612  38.30038  20.34185  1.000 90.03256  ? 27  GLN   B O     1 
ATOM   3651 C CB    . GLN   B 1 27  ? 99.86737  35.95007  20.29986  1.000 77.62764  ? 27  GLN   B CB    1 
ATOM   3652 C CG    . GLN   B 1 27  ? 100.52828 34.81038  21.01802  1.000 83.14831  ? 27  GLN   B CG    1 
ATOM   3653 C CD    . GLN   B 1 27  ? 100.40392 33.52348  20.23668  1.000 85.97867  ? 27  GLN   B CD    1 
ATOM   3654 O OE1   . GLN   B 1 27  ? 99.84106  33.51097  19.13296  1.000 90.82889  ? 27  GLN   B OE1   1 
ATOM   3655 N NE2   . GLN   B 1 27  ? 100.86992 32.42248  20.82546  1.000 79.07026  ? 27  GLN   B NE2   1 
ATOM   3656 N N     . ALA   B 1 28  ? 99.63545  38.85497  19.23197  1.000 85.26305  ? 28  ALA   B N     1 
ATOM   3657 C CA    . ALA   B 1 28  ? 98.90735  39.72771  18.30887  1.000 89.71285  ? 28  ALA   B CA    1 
ATOM   3658 C C     . ALA   B 1 28  ? 98.19617  38.94246  17.20335  1.000 86.97868  ? 28  ALA   B C     1 
ATOM   3659 O O     . ALA   B 1 28  ? 97.17618  39.39358  16.66567  1.000 78.77916  ? 28  ALA   B O     1 
ATOM   3660 C CB    . ALA   B 1 28  ? 99.87025  40.74299  17.71016  1.000 88.50406  ? 28  ALA   B CB    1 
ATOM   3661 N N     . ASN   B 1 29  ? 98.72383  37.77743  16.84768  1.000 91.93096  ? 29  ASN   B N     1 
ATOM   3662 C CA    . ASN   B 1 29  ? 97.97325  36.90060  15.97098  1.000 87.02188  ? 29  ASN   B CA    1 
ATOM   3663 C C     . ASN   B 1 29  ? 96.56807  36.63631  16.54555  1.000 83.29661  ? 29  ASN   B C     1 
ATOM   3664 O O     . ASN   B 1 29  ? 95.57517  36.72507  15.80780  1.000 77.99415  ? 29  ASN   B O     1 
ATOM   3665 C CB    . ASN   B 1 29  ? 98.83343  35.63866  15.69389  1.000 92.84820  ? 29  ASN   B CB    1 
ATOM   3666 C CG    . ASN   B 1 29  ? 100.14489 36.00670  14.92633  1.000 114.86757 ? 29  ASN   B CG    1 
ATOM   3667 O OD1   . ASN   B 1 29  ? 100.23836 37.15072  14.49842  1.000 122.16866 ? 29  ASN   B OD1   1 
ATOM   3668 N ND2   . ASN   B 1 29  ? 101.13371 35.09484  14.73436  1.000 127.71624 ? 29  ASN   B ND2   1 
ATOM   3669 N N     . TYR   B 1 30  ? 96.45444  36.47686  17.87101  1.000 82.09462  ? 30  TYR   B N     1 
ATOM   3670 C CA    . TYR   B 1 30  ? 95.30466  35.81716  18.49561  1.000 75.14775  ? 30  TYR   B CA    1 
ATOM   3671 C C     . TYR   B 1 30  ? 93.92184  36.14317  17.96337  1.000 70.72210  ? 30  TYR   B C     1 
ATOM   3672 O O     . TYR   B 1 30  ? 93.15831  35.23867  17.62348  1.000 70.78551  ? 30  TYR   B O     1 
ATOM   3673 C CB    . TYR   B 1 30  ? 95.29553  36.05798  19.99312  1.000 76.02723  ? 30  TYR   B CB    1 
ATOM   3674 C CG    . TYR   B 1 30  ? 94.66903  34.90500  20.74374  1.000 71.81053  ? 30  TYR   B CG    1 
ATOM   3675 C CD1   . TYR   B 1 30  ? 95.25712  33.64985  20.78637  1.000 69.32920  ? 30  TYR   B CD1   1 
ATOM   3676 C CD2   . TYR   B 1 30  ? 93.46198  35.08746  21.39997  1.000 71.26934  ? 30  TYR   B CD2   1 
ATOM   3677 C CE1   . TYR   B 1 30  ? 94.63739  32.61134  21.47278  1.000 74.33825  ? 30  TYR   B CE1   1 
ATOM   3678 C CE2   . TYR   B 1 30  ? 92.84941  34.08206  22.08308  1.000 74.83215  ? 30  TYR   B CE2   1 
ATOM   3679 C CZ    . TYR   B 1 30  ? 93.43178  32.84155  22.12582  1.000 74.20737  ? 30  TYR   B CZ    1 
ATOM   3680 O OH    . TYR   B 1 30  ? 92.79352  31.84027  22.81955  1.000 63.76777  ? 30  TYR   B OH    1 
ATOM   3681 N N     . SER   B 1 31  ? 93.54142  37.41776  18.00528  1.000 76.15822  ? 31  SER   B N     1 
ATOM   3682 C CA    . SER   B 1 31  ? 92.18348  37.82179  17.69219  1.000 72.57240  ? 31  SER   B CA    1 
ATOM   3683 C C     . SER   B 1 31  ? 91.72015  37.16324  16.40337  1.000 74.42353  ? 31  SER   B C     1 
ATOM   3684 O O     . SER   B 1 31  ? 90.57397  36.69074  16.29742  1.000 70.54750  ? 31  SER   B O     1 
ATOM   3685 C CB    . SER   B 1 31  ? 92.11291  39.34104  17.58008  1.000 67.60893  ? 31  SER   B CB    1 
ATOM   3686 O OG    . SER   B 1 31  ? 93.01892  39.74063  16.56497  1.000 80.00618  ? 31  SER   B OG    1 
ATOM   3687 N N     . THR   B 1 32  ? 92.64183  37.07590  15.43377  1.000 74.24279  ? 32  THR   B N     1 
ATOM   3688 C CA    . THR   B 1 32  ? 92.28944  36.58848  14.10876  1.000 71.38762  ? 32  THR   B CA    1 
ATOM   3689 C C     . THR   B 1 32  ? 92.28975  35.06028  14.01875  1.000 67.52460  ? 32  THR   B C     1 
ATOM   3690 O O     . THR   B 1 32  ? 91.42928  34.48778  13.33488  1.000 68.13807  ? 32  THR   B O     1 
ATOM   3691 C CB    . THR   B 1 32  ? 93.23385  37.19371  13.08210  1.000 69.00441  ? 32  THR   B CB    1 
ATOM   3692 O OG1   . THR   B 1 32  ? 93.32221  38.60503  13.31931  1.000 65.52922  ? 32  THR   B OG1   1 
ATOM   3693 C CG2   . THR   B 1 32  ? 92.68523  36.95531  11.68304  1.000 70.41082  ? 32  THR   B CG2   1 
ATOM   3694 N N     . LEU   B 1 33  ? 93.24138  34.39432  14.68197  1.000 64.96630  ? 33  LEU   B N     1 
ATOM   3695 C CA    . LEU   B 1 33  ? 93.21965  32.94025  14.79899  1.000 64.52257  ? 33  LEU   B CA    1 
ATOM   3696 C C     . LEU   B 1 33  ? 91.87286  32.44908  15.31883  1.000 69.52435  ? 33  LEU   B C     1 
ATOM   3697 O O     . LEU   B 1 33  ? 91.36536  31.39496  14.90364  1.000 71.90048  ? 33  LEU   B O     1 
ATOM   3698 C CB    . LEU   B 1 33  ? 94.34169  32.49788  15.73719  1.000 64.95907  ? 33  LEU   B CB    1 
ATOM   3699 C CG    . LEU   B 1 33  ? 95.74717  32.94139  15.32588  1.000 65.62040  ? 33  LEU   B CG    1 
ATOM   3700 C CD1   . LEU   B 1 33  ? 96.79661  32.70094  16.40863  1.000 66.36128  ? 33  LEU   B CD1   1 
ATOM   3701 C CD2   . LEU   B 1 33  ? 96.16491  32.22323  14.06256  1.000 72.96556  ? 33  LEU   B CD2   1 
ATOM   3702 N N     . VAL   B 1 34  ? 91.27506  33.19805  16.23609  1.000 65.52651  ? 34  VAL   B N     1 
ATOM   3703 C CA    . VAL   B 1 34  ? 90.00257  32.76363  16.77324  1.000 63.23821  ? 34  VAL   B CA    1 
ATOM   3704 C C     . VAL   B 1 34  ? 88.95794  32.75732  15.67359  1.000 68.01440  ? 34  VAL   B C     1 
ATOM   3705 O O     . VAL   B 1 34  ? 88.05110  31.91194  15.66162  1.000 75.36056  ? 34  VAL   B O     1 
ATOM   3706 C CB    . VAL   B 1 34  ? 89.59139  33.67393  17.92453  1.000 62.24703  ? 34  VAL   B CB    1 
ATOM   3707 C CG1   . VAL   B 1 34  ? 88.33637  33.12819  18.54856  1.000 65.90730  ? 34  VAL   B CG1   1 
ATOM   3708 C CG2   . VAL   B 1 34  ? 90.73483  33.81494  18.89023  1.000 69.66621  ? 34  VAL   B CG2   1 
ATOM   3709 N N     . ALA   B 1 35  ? 89.05170  33.70960  14.74731  1.000 63.29794  ? 35  ALA   B N     1 
ATOM   3710 C CA    . ALA   B 1 35  ? 88.36590  33.59315  13.46335  1.000 64.77517  ? 35  ALA   B CA    1 
ATOM   3711 C C     . ALA   B 1 35  ? 86.86246  33.54601  13.65607  1.000 69.83310  ? 35  ALA   B C     1 
ATOM   3712 O O     . ALA   B 1 35  ? 86.20432  32.57654  13.24840  1.000 72.78928  ? 35  ALA   B O     1 
ATOM   3713 C CB    . ALA   B 1 35  ? 88.82210  32.33946  12.71974  1.000 66.80586  ? 35  ALA   B CB    1 
ATOM   3714 N N     . PRO   B 1 36  ? 86.29676  34.60263  14.23608  1.000 63.20312  ? 36  PRO   B N     1 
ATOM   3715 C CA    . PRO   B 1 36  ? 84.90168  34.56629  14.71062  1.000 66.02331  ? 36  PRO   B CA    1 
ATOM   3716 C C     . PRO   B 1 36  ? 83.86682  34.56619  13.58872  1.000 63.57947  ? 36  PRO   B C     1 
ATOM   3717 O O     . PRO   B 1 36  ? 83.94176  35.36086  12.65109  1.000 67.56405  ? 36  PRO   B O     1 
ATOM   3718 C CB    . PRO   B 1 36  ? 84.81117  35.82977  15.56725  1.000 66.04770  ? 36  PRO   B CB    1 
ATOM   3719 C CG    . PRO   B 1 36  ? 85.90894  36.72266  15.02993  1.000 59.62475  ? 36  PRO   B CG    1 
ATOM   3720 C CD    . PRO   B 1 36  ? 87.01221  35.79605  14.70154  1.000 56.96877  ? 36  PRO   B CD    1 
ATOM   3721 N N     . TYR   B 1 37  ? 82.88763  33.66407  13.69305  1.000 59.50304  ? 37  TYR   B N     1 
ATOM   3722 C CA    . TYR   B 1 37  ? 81.89289  33.59778  12.62791  1.000 62.69484  ? 37  TYR   B CA    1 
ATOM   3723 C C     . TYR   B 1 37  ? 80.78078  34.61694  12.83663  1.000 68.74871  ? 37  TYR   B C     1 
ATOM   3724 O O     . TYR   B 1 37  ? 80.31971  35.25237  11.88434  1.000 71.12575  ? 37  TYR   B O     1 
ATOM   3725 C CB    . TYR   B 1 37  ? 81.27932  32.20332  12.50977  1.000 64.15720  ? 37  TYR   B CB    1 
ATOM   3726 C CG    . TYR   B 1 37  ? 80.38363  32.12355  11.30451  1.000 63.31236  ? 37  TYR   B CG    1 
ATOM   3727 C CD1   . TYR   B 1 37  ? 79.06021  32.55321  11.37209  1.000 70.90162  ? 37  TYR   B CD1   1 
ATOM   3728 C CD2   . TYR   B 1 37  ? 80.85628  31.65686  10.09184  1.000 63.19029  ? 37  TYR   B CD2   1 
ATOM   3729 C CE1   . TYR   B 1 37  ? 78.23224  32.51467  10.25141  1.000 77.27215  ? 37  TYR   B CE1   1 
ATOM   3730 C CE2   . TYR   B 1 37  ? 80.03839  31.60692  8.96903   1.000 68.32447  ? 37  TYR   B CE2   1 
ATOM   3731 C CZ    . TYR   B 1 37  ? 78.72762  32.03563  9.05120   1.000 69.86743  ? 37  TYR   B CZ    1 
ATOM   3732 O OH    . TYR   B 1 37  ? 77.90793  31.98677  7.94737   1.000 59.08878  ? 37  TYR   B OH    1 
ATOM   3733 N N     . ASN   B 1 38  ? 80.31763  34.75536  14.05787  1.000 73.64872  ? 38  ASN   B N     1 
ATOM   3734 C CA    . ASN   B 1 38  ? 79.42931  35.83954  14.41314  1.000 69.97619  ? 38  ASN   B CA    1 
ATOM   3735 C C     . ASN   B 1 38  ? 80.30389  36.97672  14.91504  1.000 70.57968  ? 38  ASN   B C     1 
ATOM   3736 O O     . ASN   B 1 38  ? 81.25347  36.74441  15.67270  1.000 69.82326  ? 38  ASN   B O     1 
ATOM   3737 C CB    . ASN   B 1 38  ? 78.45171  35.38307  15.48743  1.000 66.24558  ? 38  ASN   B CB    1 
ATOM   3738 C CG    . ASN   B 1 38  ? 77.42827  36.39976  15.77678  1.000 69.93362  ? 38  ASN   B CG    1 
ATOM   3739 O OD1   . ASN   B 1 38  ? 77.72440  37.50695  16.25716  1.000 69.38395  ? 38  ASN   B OD1   1 
ATOM   3740 N ND2   . ASN   B 1 38  ? 76.19109  36.05114  15.47505  1.000 70.24355  ? 38  ASN   B ND2   1 
ATOM   3741 N N     . PHE   B 1 39  ? 80.01369  38.19667  14.46968  1.000 70.63452  ? 39  PHE   B N     1 
ATOM   3742 C CA    . PHE   B 1 39  ? 80.87438  39.31345  14.85179  1.000 75.90321  ? 39  PHE   B CA    1 
ATOM   3743 C C     . PHE   B 1 39  ? 80.44144  40.02427  16.12556  1.000 72.49563  ? 39  PHE   B C     1 
ATOM   3744 O O     . PHE   B 1 39  ? 81.14046  40.93884  16.57535  1.000 66.38743  ? 39  PHE   B O     1 
ATOM   3745 C CB    . PHE   B 1 39  ? 80.98774  40.31750  13.71449  1.000 74.23322  ? 39  PHE   B CB    1 
ATOM   3746 C CG    . PHE   B 1 39  ? 81.83183  39.83466  12.59857  1.000 76.52472  ? 39  PHE   B CG    1 
ATOM   3747 C CD1   . PHE   B 1 39  ? 82.62652  38.70496  12.76701  1.000 74.35736  ? 39  PHE   B CD1   1 
ATOM   3748 C CD2   . PHE   B 1 39  ? 81.87550  40.51431  11.40226  1.000 74.15736  ? 39  PHE   B CD2   1 
ATOM   3749 C CE1   . PHE   B 1 39  ? 83.42587  38.25242  11.74946  1.000 73.94586  ? 39  PHE   B CE1   1 
ATOM   3750 C CE2   . PHE   B 1 39  ? 82.67958  40.06611  10.37867  1.000 76.77344  ? 39  PHE   B CE2   1 
ATOM   3751 C CZ    . PHE   B 1 39  ? 83.45478  38.93656  10.55060  1.000 75.47723  ? 39  PHE   B CZ    1 
ATOM   3752 N N     . ASP   B 1 40  ? 79.33502  39.62153  16.73150  1.000 70.22802  ? 40  ASP   B N     1 
ATOM   3753 C CA    . ASP   B 1 40  ? 78.89511  40.24279  17.96361  1.000 71.02569  ? 40  ASP   B CA    1 
ATOM   3754 C C     . ASP   B 1 40  ? 79.21911  39.37254  19.16314  1.000 74.05673  ? 40  ASP   B C     1 
ATOM   3755 O O     . ASP   B 1 40  ? 80.01252  39.78077  20.02360  1.000 77.97076  ? 40  ASP   B O     1 
ATOM   3756 C CB    . ASP   B 1 40  ? 77.41246  40.52029  17.86180  1.000 78.14641  ? 40  ASP   B CB    1 
ATOM   3757 C CG    . ASP   B 1 40  ? 77.09819  41.32321  16.64247  1.000 74.33971  ? 40  ASP   B CG    1 
ATOM   3758 O OD1   . ASP   B 1 40  ? 77.56968  42.49290  16.56866  1.000 72.54658  ? 40  ASP   B OD1   1 
ATOM   3759 O OD2   . ASP   B 1 40  ? 76.44836  40.74349  15.74139  1.000 68.48315  ? 40  ASP   B OD2   1 
ATOM   3760 N N     . LEU   B 1 41  ? 78.64971  38.17009  19.21537  1.000 67.08577  ? 41  LEU   B N     1 
ATOM   3761 C CA    . LEU   B 1 41  ? 79.15149  37.17243  20.14585  1.000 68.65322  ? 41  LEU   B CA    1 
ATOM   3762 C C     . LEU   B 1 41  ? 80.64548  36.88025  19.96162  1.000 69.58175  ? 41  LEU   B C     1 
ATOM   3763 O O     . LEU   B 1 41  ? 81.03594  35.72952  19.78173  1.000 70.44135  ? 41  LEU   B O     1 
ATOM   3764 C CB    . LEU   B 1 41  ? 78.33811  35.89058  19.99316  1.000 65.13628  ? 41  LEU   B CB    1 
ATOM   3765 C CG    . LEU   B 1 41  ? 76.87473  36.22499  20.20439  1.000 73.00352  ? 41  LEU   B CG    1 
ATOM   3766 C CD1   . LEU   B 1 41  ? 75.97950  35.36438  19.32361  1.000 84.02866  ? 41  LEU   B CD1   1 
ATOM   3767 C CD2   . LEU   B 1 41  ? 76.48799  36.09520  21.66196  1.000 82.79700  ? 41  LEU   B CD2   1 
ATOM   3768 N N     . LEU   B 1 42  ? 81.51176  37.88699  20.03469  1.000 65.11792  ? 42  LEU   B N     1 
ATOM   3769 C CA    . LEU   B 1 42  ? 82.94059  37.58921  20.02149  1.000 65.36428  ? 42  LEU   B CA    1 
ATOM   3770 C C     . LEU   B 1 42  ? 83.24801  36.64062  21.19016  1.000 74.16351  ? 42  LEU   B C     1 
ATOM   3771 O O     . LEU   B 1 42  ? 82.33072  36.26349  21.93018  1.000 81.00851  ? 42  LEU   B O     1 
ATOM   3772 C CB    . LEU   B 1 42  ? 83.76234  38.87137  20.10948  1.000 71.55283  ? 42  LEU   B CB    1 
ATOM   3773 C CG    . LEU   B 1 42  ? 83.66626  39.76354  18.85120  1.000 75.26280  ? 42  LEU   B CG    1 
ATOM   3774 C CD1   . LEU   B 1 42  ? 84.75598  40.85133  18.83404  1.000 64.25448  ? 42  LEU   B CD1   1 
ATOM   3775 C CD2   . LEU   B 1 42  ? 83.56807  38.97063  17.51749  1.000 63.91934  ? 42  LEU   B CD2   1 
ATOM   3776 N N     . THR   B 1 43  ? 84.51237  36.23940  21.35381  1.000 74.35858  ? 43  THR   B N     1 
ATOM   3777 C CA    . THR   B 1 43  ? 84.90001  35.30033  22.41204  1.000 75.26268  ? 43  THR   B CA    1 
ATOM   3778 C C     . THR   B 1 43  ? 86.42232  35.29728  22.50031  1.000 72.29481  ? 43  THR   B C     1 
ATOM   3779 O O     . THR   B 1 43  ? 87.10605  35.61125  21.52084  1.000 76.31289  ? 43  THR   B O     1 
ATOM   3780 C CB    . THR   B 1 43  ? 84.42906  33.84260  22.15048  1.000 73.22007  ? 43  THR   B CB    1 
ATOM   3781 O OG1   . THR   B 1 43  ? 85.00609  33.34272  20.93566  1.000 74.55734  ? 43  THR   B OG1   1 
ATOM   3782 C CG2   . THR   B 1 43  ? 82.88275  33.70026  22.06516  1.000 65.29939  ? 43  THR   B CG2   1 
ATOM   3783 N N     . THR   B 1 44  ? 86.94807  34.92288  23.67163  1.000 72.82545  ? 44  THR   B N     1 
ATOM   3784 C CA    . THR   B 1 44  ? 88.38304  34.68534  23.89145  1.000 75.07839  ? 44  THR   B CA    1 
ATOM   3785 C C     . THR   B 1 44  ? 88.62678  33.34518  24.57808  1.000 72.15964  ? 44  THR   B C     1 
ATOM   3786 O O     . THR   B 1 44  ? 88.39045  33.22133  25.79168  1.000 70.42946  ? 44  THR   B O     1 
ATOM   3787 C CB    . THR   B 1 44  ? 89.03239  35.77819  24.73838  1.000 72.32247  ? 44  THR   B CB    1 
ATOM   3788 O OG1   . THR   B 1 44  ? 88.87894  37.06076  24.11976  1.000 79.20252  ? 44  THR   B OG1   1 
ATOM   3789 C CG2   . THR   B 1 44  ? 90.50855  35.45920  24.97498  1.000 62.14433  ? 44  THR   B CG2   1 
ATOM   3790 N N     . PRO   B 1 45  ? 89.11981  32.33807  23.86125  1.000 66.83569  ? 45  PRO   B N     1 
ATOM   3791 C CA    . PRO   B 1 45  ? 89.49761  31.08025  24.51316  1.000 66.43923  ? 45  PRO   B CA    1 
ATOM   3792 C C     . PRO   B 1 45  ? 90.84677  31.20467  25.20574  1.000 65.67926  ? 45  PRO   B C     1 
ATOM   3793 O O     . PRO   B 1 45  ? 91.67898  32.04652  24.84909  1.000 66.83166  ? 45  PRO   B O     1 
ATOM   3794 C CB    . PRO   B 1 45  ? 89.55223  30.08958  23.34817  1.000 66.80290  ? 45  PRO   B CB    1 
ATOM   3795 C CG    . PRO   B 1 45  ? 89.85084  30.93752  22.15303  1.000 65.32098  ? 45  PRO   B CG    1 
ATOM   3796 C CD    . PRO   B 1 45  ? 89.36534  32.31671  22.41041  1.000 62.48151  ? 45  PRO   B CD    1 
ATOM   3797 N N     . SER   B 1 46  ? 91.05470  30.38168  26.23918  1.000 62.22126  ? 46  SER   B N     1 
ATOM   3798 C CA    . SER   B 1 46  ? 92.26607  30.64799  27.01593  1.000 72.54989  ? 46  SER   B CA    1 
ATOM   3799 C C     . SER   B 1 46  ? 93.51472  30.06117  26.35259  1.000 68.35818  ? 46  SER   B C     1 
ATOM   3800 O O     . SER   B 1 46  ? 94.64107  30.35794  26.78983  1.000 67.23101  ? 46  SER   B O     1 
ATOM   3801 C CB    . SER   B 1 46  ? 92.10007  30.20786  28.49710  1.000 69.80947  ? 46  SER   B CB    1 
ATOM   3802 O OG    . SER   B 1 46  ? 91.77309  28.84641  28.65978  1.000 69.86866  ? 46  SER   B OG    1 
ATOM   3803 N N     . ALA   B 1 47  ? 93.33010  29.30973  25.26603  1.000 63.74585  ? 47  ALA   B N     1 
ATOM   3804 C CA    . ALA   B 1 47  ? 94.36928  28.96852  24.30175  1.000 63.52617  ? 47  ALA   B CA    1 
ATOM   3805 C C     . ALA   B 1 47  ? 93.70426  28.32207  23.09738  1.000 62.97517  ? 47  ALA   B C     1 
ATOM   3806 O O     . ALA   B 1 47  ? 92.59302  27.78957  23.20047  1.000 59.69711  ? 47  ALA   B O     1 
ATOM   3807 C CB    . ALA   B 1 47  ? 95.41826  28.02408  24.89441  1.000 63.56206  ? 47  ALA   B CB    1 
ATOM   3808 N N     . ILE   B 1 48  ? 94.38012  28.39921  21.95088  1.000 63.39263  ? 48  ILE   B N     1 
ATOM   3809 C CA    . ILE   B 1 48  ? 94.04080  27.58988  20.78743  1.000 60.95966  ? 48  ILE   B CA    1 
ATOM   3810 C C     . ILE   B 1 48  ? 95.19292  26.62661  20.56108  1.000 59.42798  ? 48  ILE   B C     1 
ATOM   3811 O O     . ILE   B 1 48  ? 96.36373  26.99294  20.68278  1.000 61.04662  ? 48  ILE   B O     1 
ATOM   3812 C CB    . ILE   B 1 48  ? 93.74639  28.42365  19.52172  1.000 57.20865  ? 48  ILE   B CB    1 
ATOM   3813 C CG1   . ILE   B 1 48  ? 92.72824  29.51982  19.81906  1.000 58.18223  ? 48  ILE   B CG1   1 
ATOM   3814 C CG2   . ILE   B 1 48  ? 93.22635  27.52446  18.40452  1.000 54.34590  ? 48  ILE   B CG2   1 
ATOM   3815 C CD1   . ILE   B 1 48  ? 92.53072  30.47147  18.70074  1.000 59.44035  ? 48  ILE   B CD1   1 
ATOM   3816 N N     . VAL   B 1 49  ? 94.85941  25.38532  20.26952  1.000 62.33641  ? 49  VAL   B N     1 
ATOM   3817 C CA    . VAL   B 1 49  ? 95.85528  24.36197  20.00974  1.000 64.14960  ? 49  VAL   B CA    1 
ATOM   3818 C C     . VAL   B 1 49  ? 95.52866  23.73358  18.66457  1.000 62.86098  ? 49  VAL   B C     1 
ATOM   3819 O O     . VAL   B 1 49  ? 94.35537  23.50220  18.35097  1.000 60.71211  ? 49  VAL   B O     1 
ATOM   3820 C CB    . VAL   B 1 49  ? 95.88170  23.30043  21.12987  1.000 66.70073  ? 49  VAL   B CB    1 
ATOM   3821 C CG1   . VAL   B 1 49  ? 94.58927  22.48564  21.12352  1.000 62.82111  ? 49  VAL   B CG1   1 
ATOM   3822 C CG2   . VAL   B 1 49  ? 97.09978  22.41372  21.00193  1.000 68.05396  ? 49  VAL   B CG2   1 
ATOM   3823 N N     . TRP   B 1 50  ? 96.56637  23.47518  17.86692  1.000 64.17160  ? 50  TRP   B N     1 
ATOM   3824 C CA    . TRP   B 1 50  ? 96.42706  22.95210  16.51150  1.000 63.44190  ? 50  TRP   B CA    1 
ATOM   3825 C C     . TRP   B 1 50  ? 97.03822  21.55426  16.42651  1.000 65.55346  ? 50  TRP   B C     1 
ATOM   3826 O O     . TRP   B 1 50  ? 98.17736  21.41225  15.97622  1.000 71.36835  ? 50  TRP   B O     1 
ATOM   3827 C CB    . TRP   B 1 50  ? 97.09306  23.90189  15.50784  1.000 55.49253  ? 50  TRP   B CB    1 
ATOM   3828 C CG    . TRP   B 1 50  ? 96.25388  25.05874  15.06679  1.000 54.79316  ? 50  TRP   B CG    1 
ATOM   3829 C CD1   . TRP   B 1 50  ? 95.32791  25.07148  14.04977  1.000 57.42060  ? 50  TRP   B CD1   1 
ATOM   3830 C CD2   . TRP   B 1 50  ? 96.27365  26.37707  15.59439  1.000 54.63355  ? 50  TRP   B CD2   1 
ATOM   3831 N NE1   . TRP   B 1 50  ? 94.76055  26.31851  13.93041  1.000 48.28767  ? 50  TRP   B NE1   1 
ATOM   3832 C CE2   . TRP   B 1 50  ? 95.32707  27.13957  14.86776  1.000 54.44825  ? 50  TRP   B CE2   1 
ATOM   3833 C CE3   . TRP   B 1 50  ? 96.98514  26.99295  16.61844  1.000 58.94103  ? 50  TRP   B CE3   1 
ATOM   3834 C CZ2   . TRP   B 1 50  ? 95.08031  28.48380  15.14407  1.000 55.46577  ? 50  TRP   B CZ2   1 
ATOM   3835 C CZ3   . TRP   B 1 50  ? 96.73660  28.33063  16.88893  1.000 59.32957  ? 50  TRP   B CZ3   1 
ATOM   3836 C CH2   . TRP   B 1 50  ? 95.79430  29.05946  16.15206  1.000 51.56467  ? 50  TRP   B CH2   1 
ATOM   3837 N N     . PRO   B 1 51  ? 96.34296  20.50106  16.84886  1.000 65.40101  ? 51  PRO   B N     1 
ATOM   3838 C CA    . PRO   B 1 51  ? 96.95720  19.17154  16.80860  1.000 66.10670  ? 51  PRO   B CA    1 
ATOM   3839 C C     . PRO   B 1 51  ? 97.02494  18.62306  15.39162  1.000 73.29708  ? 51  PRO   B C     1 
ATOM   3840 O O     . PRO   B 1 51  ? 96.20628  18.96715  14.52721  1.000 73.83973  ? 51  PRO   B O     1 
ATOM   3841 C CB    . PRO   B 1 51  ? 96.03435  18.32712  17.69213  1.000 62.77553  ? 51  PRO   B CB    1 
ATOM   3842 C CG    . PRO   B 1 51  ? 94.74171  18.97190  17.56897  1.000 66.78541  ? 51  PRO   B CG    1 
ATOM   3843 C CD    . PRO   B 1 51  ? 95.02284  20.45652  17.49400  1.000 66.79077  ? 51  PRO   B CD    1 
ATOM   3844 N N     . GLN   B 1 52  ? 98.03848  17.76755  15.16592  1.000 72.79721  ? 52  GLN   B N     1 
ATOM   3845 C CA    . GLN   B 1 52  ? 98.28915  17.10547  13.88439  1.000 75.29609  ? 52  GLN   B CA    1 
ATOM   3846 C C     . GLN   B 1 52  ? 97.47321  15.83413  13.70402  1.000 69.78870  ? 52  GLN   B C     1 
ATOM   3847 O O     . GLN   B 1 52  ? 97.01545  15.55746  12.59072  1.000 70.25383  ? 52  GLN   B O     1 
ATOM   3848 C CB    . GLN   B 1 52  ? 99.77486  16.74536  13.71726  1.000 79.75882  ? 52  GLN   B CB    1 
ATOM   3849 C CG    . GLN   B 1 52  ? 100.72500 17.91832  13.54930  1.000 85.19616  ? 52  GLN   B CG    1 
ATOM   3850 C CD    . GLN   B 1 52  ? 100.69262 18.50292  12.14563  1.000 93.37389  ? 52  GLN   B CD    1 
ATOM   3851 O OE1   . GLN   B 1 52  ? 100.49149 17.78608  11.16320  1.000 95.04098  ? 52  GLN   B OE1   1 
ATOM   3852 N NE2   . GLN   B 1 52  ? 100.90147 19.81623  12.04823  1.000 91.66866  ? 52  GLN   B NE2   1 
ATOM   3853 N N     . ASP   B 1 53  ? 97.28717  15.05984  14.77670  1.000 65.72768  ? 53  ASP   B N     1 
ATOM   3854 C CA    . ASP   B 1 53  ? 96.60364  13.76764  14.72592  1.000 68.66642  ? 53  ASP   B CA    1 
ATOM   3855 C C     . ASP   B 1 53  ? 95.94750  13.44962  16.07176  1.000 67.24758  ? 53  ASP   B C     1 
ATOM   3856 O O     . ASP   B 1 53  ? 96.08694  14.18572  17.05772  1.000 65.19913  ? 53  ASP   B O     1 
ATOM   3857 C CB    . ASP   B 1 53  ? 97.58127  12.65211  14.37540  1.000 73.47054  ? 53  ASP   B CB    1 
ATOM   3858 C CG    . ASP   B 1 53  ? 98.65413  12.49403  15.43756  1.000 76.29628  ? 53  ASP   B CG    1 
ATOM   3859 O OD1   . ASP   B 1 53  ? 99.43628  13.45764  15.57502  1.000 74.62665  ? 53  ASP   B OD1   1 
ATOM   3860 O OD2   . ASP   B 1 53  ? 98.68737  11.45838  16.16079  1.000 75.54634  ? 53  ASP   B OD2   1 
ATOM   3861 N N     . THR   B 1 54  ? 95.28124  12.28945  16.11463  1.000 64.33387  ? 54  THR   B N     1 
ATOM   3862 C CA    . THR   B 1 54  ? 94.52033  11.86930  17.29024  1.000 60.40201  ? 54  THR   B CA    1 
ATOM   3863 C C     . THR   B 1 54  ? 95.35683  11.92733  18.57159  1.000 64.30354  ? 54  THR   B C     1 
ATOM   3864 O O     . THR   B 1 54  ? 94.92280  12.48138  19.59066  1.000 61.16721  ? 54  THR   B O     1 
ATOM   3865 C CB    . THR   B 1 54  ? 93.98711  10.45863  17.06522  1.000 55.76031  ? 54  THR   B CB    1 
ATOM   3866 O OG1   . THR   B 1 54  ? 92.98668  10.51403  16.06274  1.000 58.09168  ? 54  THR   B OG1   1 
ATOM   3867 C CG2   . THR   B 1 54  ? 93.36976  9.89202   18.33261  1.000 57.77004  ? 54  THR   B CG2   1 
ATOM   3868 N N     . GLN   B 1 55  ? 96.54840  11.33540  18.54660  1.000 65.95975  ? 55  GLN   B N     1 
ATOM   3869 C CA    . GLN   B 1 55  ? 97.38003  11.32950  19.73963  1.000 65.54850  ? 55  GLN   B CA    1 
ATOM   3870 C C     . GLN   B 1 55  ? 97.51792  12.72970  20.31400  1.000 58.16901  ? 55  GLN   B C     1 
ATOM   3871 O O     . GLN   B 1 55  ? 97.59445  12.90458  21.53472  1.000 56.28435  ? 55  GLN   B O     1 
ATOM   3872 C CB    . GLN   B 1 55  ? 98.74955  10.71908  19.41125  1.000 74.27605  ? 55  GLN   B CB    1 
ATOM   3873 C CG    . GLN   B 1 55  ? 99.82230  10.83348  20.51948  1.000 81.86225  ? 55  GLN   B CG    1 
ATOM   3874 C CD    . GLN   B 1 55  ? 100.93440 11.88183  20.22244  1.000 87.05590  ? 55  GLN   B CD    1 
ATOM   3875 O OE1   . GLN   B 1 55  ? 101.78705 11.67334  19.33545  1.000 84.18339  ? 55  GLN   B OE1   1 
ATOM   3876 N NE2   . GLN   B 1 55  ? 100.94486 12.98736  20.99034  1.000 74.00236  ? 55  GLN   B NE2   1 
ATOM   3877 N N     . GLN   B 1 56  ? 97.50794  13.73837  19.45064  1.000 58.44325  ? 56  GLN   B N     1 
ATOM   3878 C CA    . GLN   B 1 56  ? 97.69100  15.10989  19.90069  1.000 63.26128  ? 56  GLN   B CA    1 
ATOM   3879 C C     . GLN   B 1 56  ? 96.38662  15.76708  20.37307  1.000 61.88225  ? 56  GLN   B C     1 
ATOM   3880 O O     . GLN   B 1 56  ? 96.41209  16.58929  21.29286  1.000 61.23539  ? 56  GLN   B O     1 
ATOM   3881 C CB    . GLN   B 1 56  ? 98.34075  15.91156  18.77908  1.000 64.80499  ? 56  GLN   B CB    1 
ATOM   3882 C CG    . GLN   B 1 56  ? 99.82754  15.65458  18.60987  1.000 63.19225  ? 56  GLN   B CG    1 
ATOM   3883 C CD    . GLN   B 1 56  ? 100.47276 16.63514  17.63265  1.000 69.96985  ? 56  GLN   B CD    1 
ATOM   3884 O OE1   . GLN   B 1 56  ? 99.78486  17.25759  16.81025  1.000 68.95887  ? 56  GLN   B OE1   1 
ATOM   3885 N NE2   . GLN   B 1 56  ? 101.79920 16.75438  17.69871  1.000 70.23188  ? 56  GLN   B NE2   1 
ATOM   3886 N N     . VAL   B 1 57  ? 95.24039  15.45199  19.77226  1.000 59.66963  ? 57  VAL   B N     1 
ATOM   3887 C CA    . VAL   B 1 57  ? 93.98250  15.80111  20.42291  1.000 52.92007  ? 57  VAL   B CA    1 
ATOM   3888 C C     . VAL   B 1 57  ? 93.97645  15.26358  21.84283  1.000 55.10404  ? 57  VAL   B C     1 
ATOM   3889 O O     . VAL   B 1 57  ? 93.89948  16.02010  22.81628  1.000 55.92268  ? 57  VAL   B O     1 
ATOM   3890 C CB    . VAL   B 1 57  ? 92.78553  15.25750  19.63629  1.000 53.12343  ? 57  VAL   B CB    1 
ATOM   3891 C CG1   . VAL   B 1 57  ? 91.55052  15.30974  20.52224  1.000 57.16207  ? 57  VAL   B CG1   1 
ATOM   3892 C CG2   . VAL   B 1 57  ? 92.59290  16.07112  18.38397  1.000 56.63312  ? 57  VAL   B CG2   1 
ATOM   3893 N N     . ALA   B 1 58  ? 94.06944  13.93557  21.97986  1.000 60.06296  ? 58  ALA   B N     1 
ATOM   3894 C CA    . ALA   B 1 58  ? 93.97141  13.31432  23.30160  1.000 56.96383  ? 58  ALA   B CA    1 
ATOM   3895 C C     . ALA   B 1 58  ? 94.92542  13.95210  24.29255  1.000 59.91337  ? 58  ALA   B C     1 
ATOM   3896 O O     . ALA   B 1 58  ? 94.55908  14.18730  25.45197  1.000 61.48703  ? 58  ALA   B O     1 
ATOM   3897 C CB    . ALA   B 1 58  ? 94.24864  11.82070  23.21708  1.000 54.38418  ? 58  ALA   B CB    1 
ATOM   3898 N N     . ALA   B 1 59  ? 96.16257  14.23072  23.85335  1.000 58.42666  ? 59  ALA   B N     1 
ATOM   3899 C CA    . ALA   B 1 59  ? 97.11147  14.90942  24.72227  1.000 54.02571  ? 59  ALA   B CA    1 
ATOM   3900 C C     . ALA   B 1 59  ? 96.72143  16.35884  24.93662  1.000 58.33054  ? 59  ALA   B C     1 
ATOM   3901 O O     . ALA   B 1 59  ? 96.96786  16.91967  26.00777  1.000 59.51719  ? 59  ALA   B O     1 
ATOM   3902 C CB    . ALA   B 1 59  ? 98.50845  14.84051  24.13114  1.000 59.22944  ? 59  ALA   B CB    1 
ATOM   3903 N N     . ALA   B 1 60  ? 96.12291  16.98828  23.93108  1.000 60.55994  ? 60  ALA   B N     1 
ATOM   3904 C CA    . ALA   B 1 60  ? 95.65970  18.35442  24.12033  1.000 61.41363  ? 60  ALA   B CA    1 
ATOM   3905 C C     . ALA   B 1 60  ? 94.56717  18.41085  25.17342  1.000 59.12452  ? 60  ALA   B C     1 
ATOM   3906 O O     . ALA   B 1 60  ? 94.55785  19.32106  26.01313  1.000 57.06661  ? 60  ALA   B O     1 
ATOM   3907 C CB    . ALA   B 1 60  ? 95.16348  18.94039  22.79599  1.000 60.48423  ? 60  ALA   B CB    1 
ATOM   3908 N N     . VAL   B 1 61  ? 93.65237  17.42919  25.16013  1.000 57.75645  ? 61  VAL   B N     1 
ATOM   3909 C CA    . VAL   B 1 61  ? 92.50223  17.47558  26.06536  1.000 58.60575  ? 61  VAL   B CA    1 
ATOM   3910 C C     . VAL   B 1 61  ? 92.96476  17.35936  27.50651  1.000 58.72490  ? 61  VAL   B C     1 
ATOM   3911 O O     . VAL   B 1 61  ? 92.52168  18.11711  28.37522  1.000 61.81840  ? 61  VAL   B O     1 
ATOM   3912 C CB    . VAL   B 1 61  ? 91.46662  16.38723  25.72392  1.000 53.54331  ? 61  VAL   B CB    1 
ATOM   3913 C CG1   . VAL   B 1 61  ? 90.67338  16.03437  26.94475  1.000 55.17847  ? 61  VAL   B CG1   1 
ATOM   3914 C CG2   . VAL   B 1 61  ? 90.52358  16.88004  24.70942  1.000 51.40979  ? 61  VAL   B CG2   1 
ATOM   3915 N N     . LYS   B 1 62  ? 93.86106  16.41261  27.78651  1.000 50.04205  ? 62  LYS   B N     1 
ATOM   3916 C CA    . LYS   B 1 62  ? 94.36454  16.30983  29.14781  1.000 56.88988  ? 62  LYS   B CA    1 
ATOM   3917 C C     . LYS   B 1 62  ? 95.04625  17.59792  29.61387  1.000 60.90616  ? 62  LYS   B C     1 
ATOM   3918 O O     . LYS   B 1 62  ? 95.00408  17.90835  30.81164  1.000 59.26835  ? 62  LYS   B O     1 
ATOM   3919 C CB    . LYS   B 1 62  ? 95.31428  15.12095  29.27981  1.000 59.39555  ? 62  LYS   B CB    1 
ATOM   3920 C CG    . LYS   B 1 62  ? 95.63891  14.68401  30.70498  1.000 53.32419  ? 62  LYS   B CG    1 
ATOM   3921 C CD    . LYS   B 1 62  ? 95.94291  13.18628  30.72353  1.000 64.13161  ? 62  LYS   B CD    1 
ATOM   3922 C CE    . LYS   B 1 62  ? 95.88967  12.59574  32.11444  1.000 76.93943  ? 62  LYS   B CE    1 
ATOM   3923 N NZ    . LYS   B 1 62  ? 96.69850  13.38189  33.11500  1.000 69.44491  ? 62  LYS   B NZ    1 
ATOM   3924 N N     . CYS   B 1 63  ? 95.68433  18.36430  28.71254  1.000 62.93861  ? 63  CYS   B N     1 
ATOM   3925 C CA    . CYS   B 1 63  ? 96.32460  19.60038  29.17258  1.000 62.05562  ? 63  CYS   B CA    1 
ATOM   3926 C C     . CYS   B 1 63  ? 95.30588  20.51508  29.80918  1.000 62.96024  ? 63  CYS   B C     1 
ATOM   3927 O O     . CYS   B 1 63  ? 95.54836  21.09220  30.87583  1.000 60.92040  ? 63  CYS   B O     1 
ATOM   3928 C CB    . CYS   B 1 63  ? 97.04093  20.35388  28.03989  1.000 65.32958  ? 63  CYS   B CB    1 
ATOM   3929 S SG    . CYS   B 1 63  ? 98.67475  19.79280  27.48580  1.000 83.66583  ? 63  CYS   B SG    1 
ATOM   3930 N N     . ALA   B 1 64  ? 94.17782  20.70175  29.12271  1.000 64.99276  ? 64  ALA   B N     1 
ATOM   3931 C CA    . ALA   B 1 64  ? 93.04890  21.42017  29.68885  1.000 59.30298  ? 64  ALA   B CA    1 
ATOM   3932 C C     . ALA   B 1 64  ? 92.60121  20.76243  30.99137  1.000 62.26385  ? 64  ALA   B C     1 
ATOM   3933 O O     . ALA   B 1 64  ? 92.60884  21.39325  32.05624  1.000 66.47437  ? 64  ALA   B O     1 
ATOM   3934 C CB    . ALA   B 1 64  ? 91.92258  21.47355  28.66169  1.000 55.09181  ? 64  ALA   B CB    1 
ATOM   3935 N N     . VAL   B 1 65  ? 92.26322  19.47120  30.93512  1.000 57.69687  ? 65  VAL   B N     1 
ATOM   3936 C CA    . VAL   B 1 65  ? 91.75023  18.76781  32.11375  1.000 57.79119  ? 65  VAL   B CA    1 
ATOM   3937 C C     . VAL   B 1 65  ? 92.66482  18.93087  33.32443  1.000 58.27228  ? 65  VAL   B C     1 
ATOM   3938 O O     . VAL   B 1 65  ? 92.19616  19.07559  34.45849  1.000 61.80139  ? 65  VAL   B O     1 
ATOM   3939 C CB    . VAL   B 1 65  ? 91.51452  17.28118  31.79541  1.000 56.95879  ? 65  VAL   B CB    1 
ATOM   3940 C CG1   . VAL   B 1 65  ? 91.56515  16.49463  33.05583  1.000 56.72512  ? 65  VAL   B CG1   1 
ATOM   3941 C CG2   . VAL   B 1 65  ? 90.15699  17.06340  31.07805  1.000 56.47982  ? 65  VAL   B CG2   1 
ATOM   3942 N N     . ASP   B 1 66  ? 93.97426  18.90003  33.12248  1.000 61.40171  ? 66  ASP   B N     1 
ATOM   3943 C CA    . ASP   B 1 66  ? 94.87487  18.93239  34.27390  1.000 66.37282  ? 66  ASP   B CA    1 
ATOM   3944 C C     . ASP   B 1 66  ? 94.98150  20.31739  34.90734  1.000 67.30080  ? 66  ASP   B C     1 
ATOM   3945 O O     . ASP   B 1 66  ? 95.47390  20.42588  36.03914  1.000 72.28349  ? 66  ASP   B O     1 
ATOM   3946 C CB    . ASP   B 1 66  ? 96.27542  18.43141  33.87373  1.000 71.41509  ? 66  ASP   B CB    1 
ATOM   3947 C CG    . ASP   B 1 66  ? 96.34189  16.90311  33.73841  1.000 75.19096  ? 66  ASP   B CG    1 
ATOM   3948 O OD1   . ASP   B 1 66  ? 95.55252  16.18191  34.41638  1.000 70.98826  ? 66  ASP   B OD1   1 
ATOM   3949 O OD2   . ASP   B 1 66  ? 97.18124  16.43110  32.93305  1.000 79.58299  ? 66  ASP   B OD2   1 
ATOM   3950 N N     . SER   B 1 67  ? 94.54330  21.37523  34.20545  1.000 68.78553  ? 67  SER   B N     1 
ATOM   3951 C CA    . SER   B 1 67  ? 94.47286  22.74408  34.72118  1.000 63.64472  ? 67  SER   B CA    1 
ATOM   3952 C C     . SER   B 1 67  ? 93.03808  23.20405  34.96560  1.000 66.87778  ? 67  SER   B C     1 
ATOM   3953 O O     . SER   B 1 67  ? 92.75012  24.39700  34.88950  1.000 71.15319  ? 67  SER   B O     1 
ATOM   3954 C CB    . SER   B 1 67  ? 95.14589  23.71387  33.75755  1.000 62.50204  ? 67  SER   B CB    1 
ATOM   3955 O OG    . SER   B 1 67  ? 96.51043  23.87315  34.05867  1.000 69.68896  ? 67  SER   B OG    1 
ATOM   3956 N N     . ASP   B 1 68  ? 92.11619  22.27698  35.22570  1.000 66.44509  ? 68  ASP   B N     1 
ATOM   3957 C CA    . ASP   B 1 68  ? 90.71765  22.61033  35.46921  1.000 64.14173  ? 68  ASP   B CA    1 
ATOM   3958 C C     . ASP   B 1 68  ? 90.19342  23.62454  34.44401  1.000 69.97185  ? 68  ASP   B C     1 
ATOM   3959 O O     . ASP   B 1 68  ? 89.49788  24.58557  34.79511  1.000 76.98666  ? 68  ASP   B O     1 
ATOM   3960 C CB    . ASP   B 1 68  ? 90.52278  23.12571  36.89525  1.000 70.44529  ? 68  ASP   B CB    1 
ATOM   3961 C CG    . ASP   B 1 68  ? 90.96426  22.10724  37.96785  1.000 88.85558  ? 68  ASP   B CG    1 
ATOM   3962 O OD1   . ASP   B 1 68  ? 90.31950  21.02686  38.13114  1.000 81.26750  ? 68  ASP   B OD1   1 
ATOM   3963 O OD2   . ASP   B 1 68  ? 91.97424  22.40819  38.66354  1.000 99.79150  ? 68  ASP   B OD2   1 
ATOM   3964 N N     . ILE   B 1 69  ? 90.54336  23.42134  33.16482  1.000 63.83167  ? 69  ILE   B N     1 
ATOM   3965 C CA    . ILE   B 1 69  ? 90.02001  24.19513  32.04217  1.000 56.94684  ? 69  ILE   B CA    1 
ATOM   3966 C C     . ILE   B 1 69  ? 89.12142  23.29746  31.20020  1.000 59.03131  ? 69  ILE   B C     1 
ATOM   3967 O O     . ILE   B 1 69  ? 89.22024  22.06402  31.24327  1.000 61.00347  ? 69  ILE   B O     1 
ATOM   3968 C CB    . ILE   B 1 69  ? 91.14256  24.83584  31.19541  1.000 57.55925  ? 69  ILE   B CB    1 
ATOM   3969 C CG1   . ILE   B 1 69  ? 91.60424  26.11191  31.90075  1.000 58.87632  ? 69  ILE   B CG1   1 
ATOM   3970 C CG2   . ILE   B 1 69  ? 90.69986  25.06228  29.74657  1.000 57.39201  ? 69  ILE   B CG2   1 
ATOM   3971 C CD1   . ILE   B 1 69  ? 92.83731  26.74843  31.35506  1.000 61.20920  ? 69  ILE   B CD1   1 
ATOM   3972 N N     . LYS   B 1 70  ? 88.18131  23.91680  30.48530  1.000 62.68277  ? 70  LYS   B N     1 
ATOM   3973 C CA    . LYS   B 1 70  ? 87.21383  23.18794  29.66782  1.000 63.68978  ? 70  LYS   B CA    1 
ATOM   3974 C C     . LYS   B 1 70  ? 87.51544  23.33835  28.19071  1.000 62.72624  ? 70  LYS   B C     1 
ATOM   3975 O O     . LYS   B 1 70  ? 88.23097  24.24670  27.76241  1.000 66.11436  ? 70  LYS   B O     1 
ATOM   3976 C CB    . LYS   B 1 70  ? 85.77092  23.62853  29.92859  1.000 65.42018  ? 70  LYS   B CB    1 
ATOM   3977 C CG    . LYS   B 1 70  ? 85.15297  23.05363  31.19931  1.000 74.62654  ? 70  LYS   B CG    1 
ATOM   3978 C CD    . LYS   B 1 70  ? 83.90034  23.80410  31.66996  1.000 75.58503  ? 70  LYS   B CD    1 
ATOM   3979 C CE    . LYS   B 1 70  ? 83.44773  23.31152  33.04025  1.000 73.84319  ? 70  LYS   B CE    1 
ATOM   3980 N NZ    . LYS   B 1 70  ? 83.14170  21.83218  33.01164  1.000 68.73951  ? 70  LYS   B NZ    1 
ATOM   3981 N N     . VAL   B 1 71  ? 86.92058  22.45545  27.40846  1.000 60.95013  ? 71  VAL   B N     1 
ATOM   3982 C CA    . VAL   B 1 71  ? 87.38458  22.20647  26.05285  1.000 64.41639  ? 71  VAL   B CA    1 
ATOM   3983 C C     . VAL   B 1 71  ? 86.21763  22.26025  25.06261  1.000 65.96271  ? 71  VAL   B C     1 
ATOM   3984 O O     . VAL   B 1 71  ? 85.11095  21.78057  25.34809  1.000 61.89405  ? 71  VAL   B O     1 
ATOM   3985 C CB    . VAL   B 1 71  ? 88.11140  20.84416  26.00230  1.000 60.03659  ? 71  VAL   B CB    1 
ATOM   3986 C CG1   . VAL   B 1 71  ? 88.37269  20.41168  24.58009  1.000 64.18961  ? 71  VAL   B CG1   1 
ATOM   3987 C CG2   . VAL   B 1 71  ? 89.36180  20.91870  26.78351  1.000 57.33981  ? 71  VAL   B CG2   1 
ATOM   3988 N N     . GLN   B 1 72  ? 86.47270  22.86249  23.89210  1.000 58.73787  ? 72  GLN   B N     1 
ATOM   3989 C CA    . GLN   B 1 72  ? 85.58517  22.73207  22.73748  1.000 61.25368  ? 72  GLN   B CA    1 
ATOM   3990 C C     . GLN   B 1 72  ? 86.47469  22.58906  21.50176  1.000 62.33755  ? 72  GLN   B C     1 
ATOM   3991 O O     . GLN   B 1 72  ? 87.42123  23.39044  21.32620  1.000 61.59422  ? 72  GLN   B O     1 
ATOM   3992 C CB    . GLN   B 1 72  ? 84.61930  23.92766  22.57693  1.000 62.25885  ? 72  GLN   B CB    1 
ATOM   3993 C CG    . GLN   B 1 72  ? 83.30294  23.85301  23.36542  1.000 62.00124  ? 72  GLN   B CG    1 
ATOM   3994 C CD    . GLN   B 1 72  ? 82.38548  22.70328  22.93559  1.000 60.08314  ? 72  GLN   B CD    1 
ATOM   3995 O OE1   . GLN   B 1 72  ? 81.46469  22.88872  22.13841  1.000 60.10428  ? 72  GLN   B OE1   1 
ATOM   3996 N NE2   . GLN   B 1 72  ? 82.62789  21.51966  23.48164  1.000 59.87221  ? 72  GLN   B NE2   1 
ATOM   3997 N N     . PRO   B 1 73  ? 86.23343  21.59341  20.64368  1.000 59.59803  ? 73  PRO   B N     1 
ATOM   3998 C CA    . PRO   B 1 73  ? 86.92029  21.54850  19.35469  1.000 56.61663  ? 73  PRO   B CA    1 
ATOM   3999 C C     . PRO   B 1 73  ? 86.28100  22.49471  18.36023  1.000 61.27577  ? 73  PRO   B C     1 
ATOM   4000 O O     . PRO   B 1 73  ? 85.06927  22.72480  18.37435  1.000 59.15199  ? 73  PRO   B O     1 
ATOM   4001 C CB    . PRO   B 1 73  ? 86.72387  20.09540  18.91592  1.000 56.22129  ? 73  PRO   B CB    1 
ATOM   4002 C CG    . PRO   B 1 73  ? 85.41806  19.76843  19.44218  1.000 58.04037  ? 73  PRO   B CG    1 
ATOM   4003 C CD    . PRO   B 1 73  ? 85.39222  20.39762  20.81945  1.000 60.23545  ? 73  PRO   B CD    1 
ATOM   4004 N N     . LYS   B 1 74  ? 87.12430  23.06883  17.50315  1.000 64.50868  ? 74  LYS   B N     1 
ATOM   4005 C CA    . LYS   B 1 74  ? 86.66373  23.82839  16.34702  1.000 57.66979  ? 74  LYS   B CA    1 
ATOM   4006 C C     . LYS   B 1 74  ? 86.96134  23.00524  15.09364  1.000 57.58118  ? 74  LYS   B C     1 
ATOM   4007 O O     . LYS   B 1 74  ? 87.99048  22.31889  15.02541  1.000 58.83697  ? 74  LYS   B O     1 
ATOM   4008 C CB    . LYS   B 1 74  ? 87.33401  25.20739  16.28514  1.000 51.95266  ? 74  LYS   B CB    1 
ATOM   4009 C CG    . LYS   B 1 74  ? 86.69657  26.12099  15.26900  1.000 56.79972  ? 74  LYS   B CG    1 
ATOM   4010 C CD    . LYS   B 1 74  ? 86.76230  27.55474  15.74060  1.000 60.14592  ? 74  LYS   B CD    1 
ATOM   4011 C CE    . LYS   B 1 74  ? 88.18138  28.07785  15.78692  1.000 69.39260  ? 74  LYS   B CE    1 
ATOM   4012 N NZ    . LYS   B 1 74  ? 88.49416  28.85620  14.55373  1.000 71.46866  ? 74  LYS   B NZ    1 
ATOM   4013 N N     . SER   B 1 75  ? 86.03065  23.02121  14.13275  1.000 50.33168  ? 75  SER   B N     1 
ATOM   4014 C CA    . SER   B 1 75  ? 86.23896  22.38131  12.84769  1.000 46.10784  ? 75  SER   B CA    1 
ATOM   4015 C C     . SER   B 1 75  ? 86.01622  23.43996  11.77035  1.000 54.47361  ? 75  SER   B C     1 
ATOM   4016 O O     . SER   B 1 75  ? 86.93899  24.19891  11.46346  1.000 61.82248  ? 75  SER   B O     1 
ATOM   4017 C CB    . SER   B 1 75  ? 85.34157  21.15568  12.66753  1.000 57.54093  ? 75  SER   B CB    1 
ATOM   4018 O OG    . SER   B 1 75  ? 85.84141  20.04790  13.39428  1.000 59.14683  ? 75  SER   B OG    1 
ATOM   4019 N N     . GLY   B 1 76  ? 84.82031  23.52209  11.18353  1.000 57.88593  ? 76  GLY   B N     1 
ATOM   4020 C CA    . GLY   B 1 76  ? 84.57499  24.53994  10.16173  1.000 57.55031  ? 76  GLY   B CA    1 
ATOM   4021 C C     . GLY   B 1 76  ? 84.47887  25.94751  10.72933  1.000 60.23221  ? 76  GLY   B C     1 
ATOM   4022 O O     . GLY   B 1 76  ? 84.99555  26.90679  10.14128  1.000 61.97350  ? 76  GLY   B O     1 
ATOM   4023 N N     . GLY   B 1 77  ? 83.81651  26.09311  11.87353  1.000 58.05072  ? 77  GLY   B N     1 
ATOM   4024 C CA    . GLY   B 1 77  ? 83.64222  27.38486  12.49850  1.000 59.72310  ? 77  GLY   B CA    1 
ATOM   4025 C C     . GLY   B 1 77  ? 82.25517  27.96893  12.35658  1.000 56.66454  ? 77  GLY   B C     1 
ATOM   4026 O O     . GLY   B 1 77  ? 82.03146  29.09493  12.80794  1.000 53.53128  ? 77  GLY   B O     1 
ATOM   4027 N N     . HIS   B 1 78  ? 81.30537  27.23698  11.77518  1.000 58.31662  ? 78  HIS   B N     1 
ATOM   4028 C CA    . HIS   B 1 78  ? 80.00413  27.81324  11.45151  1.000 66.24476  ? 78  HIS   B CA    1 
ATOM   4029 C C     . HIS   B 1 78  ? 79.00977  27.87671  12.60531  1.000 72.39501  ? 78  HIS   B C     1 
ATOM   4030 O O     . HIS   B 1 78  ? 77.78827  27.90829  12.38662  1.000 73.61420  ? 78  HIS   B O     1 
ATOM   4031 C CB    . HIS   B 1 78  ? 79.35866  27.05032  10.29690  1.000 65.14081  ? 78  HIS   B CB    1 
ATOM   4032 C CG    . HIS   B 1 78  ? 79.46616  27.75990  8.99020   1.000 66.21527  ? 78  HIS   B CG    1 
ATOM   4033 N ND1   . HIS   B 1 78  ? 78.45015  28.56495  8.49523   1.000 71.75611  ? 78  HIS   B ND1   1 
ATOM   4034 C CD2   . HIS   B 1 78  ? 80.47332  27.79885  8.08509   1.000 67.12857  ? 78  HIS   B CD2   1 
ATOM   4035 C CE1   . HIS   B 1 78  ? 78.85436  29.06443  7.33505   1.000 75.76758  ? 78  HIS   B CE1   1 
ATOM   4036 N NE2   . HIS   B 1 78  ? 80.06810  28.61245  7.06390   1.000 69.01907  ? 78  HIS   B NE2   1 
ATOM   4037 N N     . ASN   B 1 79  ? 79.49616  27.92675  13.83489  1.000 68.72526  ? 79  ASN   B N     1 
ATOM   4038 C CA    . ASN   B 1 79  ? 78.58613  27.95290  14.95996  1.000 68.92786  ? 79  ASN   B CA    1 
ATOM   4039 C C     . ASN   B 1 79  ? 78.19513  29.38546  15.23821  1.000 68.51256  ? 79  ASN   B C     1 
ATOM   4040 O O     . ASN   B 1 79  ? 79.05746  30.23040  15.50298  1.000 63.44781  ? 79  ASN   B O     1 
ATOM   4041 C CB    . ASN   B 1 79  ? 79.19242  27.34160  16.20133  1.000 71.91481  ? 79  ASN   B CB    1 
ATOM   4042 C CG    . ASN   B 1 79  ? 78.20324  27.28227  17.27708  1.000 70.52317  ? 79  ASN   B CG    1 
ATOM   4043 O OD1   . ASN   B 1 79  ? 78.15133  28.18460  18.12168  1.000 67.33532  ? 79  ASN   B OD1   1 
ATOM   4044 N ND2   . ASN   B 1 79  ? 77.35107  26.25695  17.24186  1.000 70.20141  ? 79  ASN   B ND2   1 
ATOM   4045 N N     . TYR   B 1 80  ? 76.89332  29.65198  15.17488  1.000 71.74494  ? 80  TYR   B N     1 
ATOM   4046 C CA    . TYR   B 1 80  ? 76.44241  31.03411  15.20399  1.000 69.61176  ? 80  TYR   B CA    1 
ATOM   4047 C C     . TYR   B 1 80  ? 76.73489  31.69111  16.51160  1.000 64.65595  ? 80  TYR   B C     1 
ATOM   4048 O O     . TYR   B 1 80  ? 76.70335  32.92650  16.59153  1.000 64.11759  ? 80  TYR   B O     1 
ATOM   4049 C CB    . TYR   B 1 80  ? 74.97266  31.09300  14.91752  1.000 70.86361  ? 80  TYR   B CB    1 
ATOM   4050 C CG    . TYR   B 1 80  ? 74.65222  30.64298  13.53709  1.000 74.52489  ? 80  TYR   B CG    1 
ATOM   4051 C CD1   . TYR   B 1 80  ? 74.62405  29.29313  13.20571  1.000 78.21080  ? 80  TYR   B CD1   1 
ATOM   4052 C CD2   . TYR   B 1 80  ? 74.26752  31.55418  12.59555  1.000 71.24307  ? 80  TYR   B CD2   1 
ATOM   4053 C CE1   . TYR   B 1 80  ? 74.29095  28.89647  11.94295  1.000 75.83559  ? 80  TYR   B CE1   1 
ATOM   4054 C CE2   . TYR   B 1 80  ? 73.93026  31.17710  11.35049  1.000 78.43392  ? 80  TYR   B CE2   1 
ATOM   4055 C CZ    . TYR   B 1 80  ? 73.93238  29.85561  11.01778  1.000 79.52120  ? 80  TYR   B CZ    1 
ATOM   4056 O OH    . TYR   B 1 80  ? 73.56288  29.51980  9.73779   1.000 82.87309  ? 80  TYR   B OH    1 
ATOM   4057 N N     . GLY   B 1 81  ? 77.00949  30.89114  17.52472  1.000 65.19837  ? 81  GLY   B N     1 
ATOM   4058 C CA    . GLY   B 1 81  ? 77.45617  31.43428  18.78036  1.000 68.68914  ? 81  GLY   B CA    1 
ATOM   4059 C C     . GLY   B 1 81  ? 78.93327  31.60406  18.86313  1.000 66.86023  ? 81  GLY   B C     1 
ATOM   4060 O O     . GLY   B 1 81  ? 79.40675  32.34137  19.72094  1.000 64.56835  ? 81  GLY   B O     1 
ATOM   4061 N N     . ASN   B 1 82  ? 79.67365  30.97320  17.94880  1.000 67.09593  ? 82  ASN   B N     1 
ATOM   4062 C CA    . ASN   B 1 82  ? 81.12685  30.83029  18.06560  1.000 68.66711  ? 82  ASN   B CA    1 
ATOM   4063 C C     . ASN   B 1 82  ? 81.50272  29.90408  19.22365  1.000 64.26641  ? 82  ASN   B C     1 
ATOM   4064 O O     . ASN   B 1 82  ? 82.43233  30.18074  19.98712  1.000 62.30190  ? 82  ASN   B O     1 
ATOM   4065 C CB    . ASN   B 1 82  ? 81.86502  32.18178  18.18483  1.000 65.31706  ? 82  ASN   B CB    1 
ATOM   4066 C CG    . ASN   B 1 82  ? 81.61596  33.11667  16.99435  1.000 67.36023  ? 82  ASN   B CG    1 
ATOM   4067 O OD1   . ASN   B 1 82  ? 81.14306  32.68923  15.93880  1.000 72.73583  ? 82  ASN   B OD1   1 
ATOM   4068 N ND2   . ASN   B 1 82  ? 82.00418  34.38188  17.14261  1.000 61.95981  ? 82  ASN   B ND2   1 
ATOM   4069 N N     . TYR   B 1 83  ? 80.81117  28.76504  19.30767  1.000 64.92250  ? 83  TYR   B N     1 
ATOM   4070 C CA    . TYR   B 1 83  ? 81.01068  27.83951  20.41997  1.000 66.23795  ? 83  TYR   B CA    1 
ATOM   4071 C C     . TYR   B 1 83  ? 82.34103  27.09101  20.35138  1.000 67.43494  ? 83  TYR   B C     1 
ATOM   4072 O O     . TYR   B 1 83  ? 82.83885  26.64133  21.39242  1.000 69.84728  ? 83  TYR   B O     1 
ATOM   4073 C CB    . TYR   B 1 83  ? 79.85822  26.83556  20.48559  1.000 65.51822  ? 83  TYR   B CB    1 
ATOM   4074 C CG    . TYR   B 1 83  ? 78.59111  27.40123  21.08623  1.000 71.25962  ? 83  TYR   B CG    1 
ATOM   4075 C CD1   . TYR   B 1 83  ? 78.58467  28.65232  21.71087  1.000 68.15599  ? 83  TYR   B CD1   1 
ATOM   4076 C CD2   . TYR   B 1 83  ? 77.38319  26.69217  21.00540  1.000 71.14602  ? 83  TYR   B CD2   1 
ATOM   4077 C CE1   . TYR   B 1 83  ? 77.41916  29.17388  22.25811  1.000 67.34678  ? 83  TYR   B CE1   1 
ATOM   4078 C CE2   . TYR   B 1 83  ? 76.21315  27.20949  21.53836  1.000 70.26151  ? 83  TYR   B CE2   1 
ATOM   4079 C CZ    . TYR   B 1 83  ? 76.23633  28.45058  22.16760  1.000 72.23899  ? 83  TYR   B CZ    1 
ATOM   4080 O OH    . TYR   B 1 83  ? 75.07314  28.96845  22.70508  1.000 71.76520  ? 83  TYR   B OH    1 
ATOM   4081 N N     . GLY   B 1 84  ? 82.92457  26.91763  19.15820  1.000 64.38910  ? 84  GLY   B N     1 
ATOM   4082 C CA    . GLY   B 1 84  ? 84.23609  26.28025  19.08809  1.000 60.65842  ? 84  GLY   B CA    1 
ATOM   4083 C C     . GLY   B 1 84  ? 85.34496  27.10011  19.72719  1.000 63.03089  ? 84  GLY   B C     1 
ATOM   4084 O O     . GLY   B 1 84  ? 86.39972  26.54786  20.08370  1.000 61.90089  ? 84  GLY   B O     1 
ATOM   4085 N N     . SER   B 1 85  ? 85.12887  28.40869  19.88434  1.000 61.29761  ? 85  SER   B N     1 
ATOM   4086 C CA    . SER   B 1 85  ? 86.08414  29.30361  20.51776  1.000 61.83285  ? 85  SER   B CA    1 
ATOM   4087 C C     . SER   B 1 85  ? 85.53570  29.89561  21.81119  1.000 65.00096  ? 85  SER   B C     1 
ATOM   4088 O O     . SER   B 1 85  ? 85.89735  31.00880  22.16717  1.000 73.41830  ? 85  SER   B O     1 
ATOM   4089 C CB    . SER   B 1 85  ? 86.49284  30.42145  19.55266  1.000 63.98322  ? 85  SER   B CB    1 
ATOM   4090 O OG    . SER   B 1 85  ? 87.54004  30.03378  18.67207  1.000 70.63998  ? 85  SER   B OG    1 
ATOM   4091 N N     . THR   B 1 86  ? 84.64319  29.17452  22.51346  1.000 63.95280  ? 86  THR   B N     1 
ATOM   4092 C CA    . THR   B 1 86  ? 84.18002  29.54220  23.86636  1.000 62.13710  ? 86  THR   B CA    1 
ATOM   4093 C C     . THR   B 1 86  ? 85.22993  30.24036  24.71572  1.000 63.96740  ? 86  THR   B C     1 
ATOM   4094 O O     . THR   B 1 86  ? 86.38528  29.80973  24.79858  1.000 68.16149  ? 86  THR   B O     1 
ATOM   4095 C CB    . THR   B 1 86  ? 83.69120  28.31542  24.65510  1.000 58.60830  ? 86  THR   B CB    1 
ATOM   4096 O OG1   . THR   B 1 86  ? 82.42798  27.82657  24.15112  1.000 62.86188  ? 86  THR   B OG1   1 
ATOM   4097 C CG2   . THR   B 1 86  ? 83.68190  28.62197  26.14793  1.000 49.66040  ? 86  THR   B CG2   1 
ATOM   4098 N N     . THR   B 1 87  ? 84.79760  31.27359  25.41759  1.000 61.01699  ? 87  THR   B N     1 
ATOM   4099 C CA    . THR   B 1 87  ? 85.73122  32.10619  26.14724  1.000 64.80632  ? 87  THR   B CA    1 
ATOM   4100 C C     . THR   B 1 87  ? 86.28804  31.36438  27.36052  1.000 66.70343  ? 87  THR   B C     1 
ATOM   4101 O O     . THR   B 1 87  ? 85.55213  30.70312  28.10019  1.000 66.60042  ? 87  THR   B O     1 
ATOM   4102 C CB    . THR   B 1 87  ? 85.03198  33.38760  26.57709  1.000 71.30906  ? 87  THR   B CB    1 
ATOM   4103 O OG1   . THR   B 1 87  ? 84.29288  33.91617  25.46259  1.000 70.11486  ? 87  THR   B OG1   1 
ATOM   4104 C CG2   . THR   B 1 87  ? 86.06052  34.41938  27.09249  1.000 66.24476  ? 87  THR   B CG2   1 
ATOM   4105 N N     . GLY   B 1 88  ? 87.61186  31.47531  27.55532  1.000 65.60123  ? 88  GLY   B N     1 
ATOM   4106 C CA    . GLY   B 1 88  ? 88.33207  30.83045  28.64287  1.000 65.06566  ? 88  GLY   B CA    1 
ATOM   4107 C C     . GLY   B 1 88  ? 88.50352  29.33256  28.50990  1.000 67.96081  ? 88  GLY   B C     1 
ATOM   4108 O O     . GLY   B 1 88  ? 89.22210  28.72996  29.32625  1.000 66.41729  ? 88  GLY   B O     1 
ATOM   4109 N N     . GLU   B 1 89  ? 87.84955  28.71355  27.53867  1.000 65.56876  ? 89  GLU   B N     1 
ATOM   4110 C CA    . GLU   B 1 89  ? 88.01087  27.30724  27.25557  1.000 61.53464  ? 89  GLU   B CA    1 
ATOM   4111 C C     . GLU   B 1 89  ? 89.17111  27.09889  26.27436  1.000 63.63468  ? 89  GLU   B C     1 
ATOM   4112 O O     . GLU   B 1 89  ? 89.66882  28.03431  25.63132  1.000 61.88425  ? 89  GLU   B O     1 
ATOM   4113 C CB    . GLU   B 1 89  ? 86.68624  26.74517  26.71462  1.000 60.68178  ? 89  GLU   B CB    1 
ATOM   4114 C CG    . GLU   B 1 89  ? 85.56027  26.60004  27.77689  1.000 66.48611  ? 89  GLU   B CG    1 
ATOM   4115 C CD    . GLU   B 1 89  ? 84.35955  25.71617  27.32099  1.000 69.20029  ? 89  GLU   B CD    1 
ATOM   4116 O OE1   . GLU   B 1 89  ? 84.42336  25.10798  26.22974  1.000 69.74419  ? 89  GLU   B OE1   1 
ATOM   4117 O OE2   . GLU   B 1 89  ? 83.37812  25.55800  28.09100  1.000 65.75615  ? 89  GLU   B OE2   1 
ATOM   4118 N N     . LEU   B 1 90  ? 89.63459  25.85577  26.20389  1.000 61.68349  ? 90  LEU   B N     1 
ATOM   4119 C CA    . LEU   B 1 90  ? 90.59201  25.44279  25.19522  1.000 60.08018  ? 90  LEU   B CA    1 
ATOM   4120 C C     . LEU   B 1 90  ? 89.89369  25.25717  23.84624  1.000 63.38299  ? 90  LEU   B C     1 
ATOM   4121 O O     . LEU   B 1 90  ? 88.86710  24.57443  23.75520  1.000 64.16536  ? 90  LEU   B O     1 
ATOM   4122 C CB    . LEU   B 1 90  ? 91.27558  24.14846  25.63570  1.000 59.69027  ? 90  LEU   B CB    1 
ATOM   4123 C CG    . LEU   B 1 90  ? 92.26707  23.55704  24.63937  1.000 60.14448  ? 90  LEU   B CG    1 
ATOM   4124 C CD1   . LEU   B 1 90  ? 93.27022  24.62138  24.20387  1.000 59.44066  ? 90  LEU   B CD1   1 
ATOM   4125 C CD2   . LEU   B 1 90  ? 92.95364  22.34775  25.26489  1.000 57.61081  ? 90  LEU   B CD2   1 
ATOM   4126 N N     . SER   B 1 91  ? 90.43982  25.88638  22.79784  1.000 59.28609  ? 91  SER   B N     1 
ATOM   4127 C CA    . SER   B 1 91  ? 89.93669  25.74017  21.43642  1.000 55.25487  ? 91  SER   B CA    1 
ATOM   4128 C C     . SER   B 1 91  ? 90.86081  24.74638  20.76089  1.000 63.05265  ? 91  SER   B C     1 
ATOM   4129 O O     . SER   B 1 91  ? 92.05019  25.03052  20.59334  1.000 63.95760  ? 91  SER   B O     1 
ATOM   4130 C CB    . SER   B 1 91  ? 89.92424  27.07368  20.69844  1.000 59.68628  ? 91  SER   B CB    1 
ATOM   4131 O OG    . SER   B 1 91  ? 89.00880  27.06334  19.62754  1.000 60.68120  ? 91  SER   B OG    1 
ATOM   4132 N N     . VAL   B 1 92  ? 90.32569  23.57231  20.41682  1.000 65.88093  ? 92  VAL   B N     1 
ATOM   4133 C CA    . VAL   B 1 92  ? 91.08767  22.49536  19.77534  1.000 57.46917  ? 92  VAL   B CA    1 
ATOM   4134 C C     . VAL   B 1 92  ? 90.78220  22.56563  18.28701  1.000 60.53223  ? 92  VAL   B C     1 
ATOM   4135 O O     . VAL   B 1 92  ? 89.88650  21.88916  17.76553  1.000 61.76571  ? 92  VAL   B O     1 
ATOM   4136 C CB    . VAL   B 1 92  ? 90.75350  21.13504  20.35797  1.000 59.67238  ? 92  VAL   B CB    1 
ATOM   4137 C CG1   . VAL   B 1 92  ? 91.40002  20.03646  19.52199  1.000 61.91744  ? 92  VAL   B CG1   1 
ATOM   4138 C CG2   . VAL   B 1 92  ? 91.24344  21.08401  21.77847  1.000 61.44226  ? 92  VAL   B CG2   1 
ATOM   4139 N N     . ASN   B 1 93  ? 91.55107  23.39379  17.59895  1.000 60.17015  ? 93  ASN   B N     1 
ATOM   4140 C CA    . ASN   B 1 93  ? 91.36445  23.59663  16.17713  1.000 55.42677  ? 93  ASN   B CA    1 
ATOM   4141 C C     . ASN   B 1 93  ? 91.83290  22.36282  15.43848  1.000 60.83703  ? 93  ASN   B C     1 
ATOM   4142 O O     . ASN   B 1 93  ? 92.99308  21.94401  15.55784  1.000 63.60695  ? 93  ASN   B O     1 
ATOM   4143 C CB    . ASN   B 1 93  ? 92.12566  24.82535  15.73447  1.000 55.58394  ? 93  ASN   B CB    1 
ATOM   4144 C CG    . ASN   B 1 93  ? 91.64869  25.33825  14.43799  1.000 63.19769  ? 93  ASN   B CG    1 
ATOM   4145 O OD1   . ASN   B 1 93  ? 91.58107  24.60015  13.45480  1.000 66.83447  ? 93  ASN   B OD1   1 
ATOM   4146 N ND2   . ASN   B 1 93  ? 91.23055  26.60945  14.42975  1.000 65.65535  ? 93  ASN   B ND2   1 
ATOM   4147 N N     . LEU   B 1 94  ? 90.92111  21.75265  14.69594  1.000 61.95712  ? 94  LEU   B N     1 
ATOM   4148 C CA    . LEU   B 1 94  ? 91.22196  20.49701  14.02300  1.000 67.32783  ? 94  LEU   B CA    1 
ATOM   4149 C C     . LEU   B 1 94  ? 91.67079  20.70228  12.57325  1.000 66.50064  ? 94  LEU   B C     1 
ATOM   4150 O O     . LEU   B 1 94  ? 91.57955  19.78425  11.74673  1.000 62.44271  ? 94  LEU   B O     1 
ATOM   4151 C CB    . LEU   B 1 94  ? 90.01091  19.57468  14.11664  1.000 62.96426  ? 94  LEU   B CB    1 
ATOM   4152 C CG    . LEU   B 1 94  ? 89.68353  19.27263  15.57245  1.000 59.19256  ? 94  LEU   B CG    1 
ATOM   4153 C CD1   . LEU   B 1 94  ? 88.41244  18.42682  15.68456  1.000 59.66131  ? 94  LEU   B CD1   1 
ATOM   4154 C CD2   . LEU   B 1 94  ? 90.88639  18.59340  16.21179  1.000 59.71041  ? 94  LEU   B CD2   1 
ATOM   4155 N N     . ASP   B 1 95  ? 92.21029  21.88322  12.26060  1.000 68.85218  ? 95  ASP   B N     1 
ATOM   4156 C CA    . ASP   B 1 95  ? 92.46575  22.20908  10.86325  1.000 69.80803  ? 95  ASP   B CA    1 
ATOM   4157 C C     . ASP   B 1 95  ? 93.37474  21.16801  10.20312  1.000 70.15905  ? 95  ASP   B C     1 
ATOM   4158 O O     . ASP   B 1 95  ? 93.24340  20.89900  9.00349   1.000 72.05088  ? 95  ASP   B O     1 
ATOM   4159 C CB    . ASP   B 1 95  ? 93.06783  23.61025  10.76052  1.000 73.45578  ? 95  ASP   B CB    1 
ATOM   4160 C CG    . ASP   B 1 95  ? 92.80592  24.24743  9.40269   1.000 89.41016  ? 95  ASP   B CG    1 
ATOM   4161 O OD1   . ASP   B 1 95  ? 91.63237  24.60036  9.15661   1.000 97.51794  ? 95  ASP   B OD1   1 
ATOM   4162 O OD2   . ASP   B 1 95  ? 93.74096  24.37211  8.57828   1.000 89.31695  ? 95  ASP   B OD2   1 
ATOM   4163 N N     . ASN   B 1 96  ? 94.25797  20.53228  10.97401  1.000 70.37782  ? 96  ASN   B N     1 
ATOM   4164 C CA    . ASN   B 1 96  ? 95.24207  19.61771  10.41403  1.000 66.63783  ? 96  ASN   B CA    1 
ATOM   4165 C C     . ASN   B 1 96  ? 94.75044  18.17494  10.31330  1.000 71.09835  ? 96  ASN   B C     1 
ATOM   4166 O O     . ASN   B 1 96  ? 95.56400  17.26852  10.05479  1.000 76.66703  ? 96  ASN   B O     1 
ATOM   4167 C CB    . ASN   B 1 96  ? 96.53330  19.65561  11.23062  1.000 72.00423  ? 96  ASN   B CB    1 
ATOM   4168 C CG    . ASN   B 1 96  ? 97.19473  21.00399  11.19629  1.000 75.61140  ? 96  ASN   B CG    1 
ATOM   4169 O OD1   . ASN   B 1 96  ? 97.23387  21.65696  10.15135  1.000 73.53026  ? 96  ASN   B OD1   1 
ATOM   4170 N ND2   . ASN   B 1 96  ? 97.80475  21.38994  12.31141  1.000 77.43180  ? 96  ASN   B ND2   1 
ATOM   4171 N N     . LEU   B 1 97  ? 93.46092  17.93448  10.51834  1.000 66.56154  ? 97  LEU   B N     1 
ATOM   4172 C CA    . LEU   B 1 97  ? 92.90763  16.58785  10.42408  1.000 60.25816  ? 97  LEU   B CA    1 
ATOM   4173 C C     . LEU   B 1 97  ? 91.99201  16.53889  9.21138   1.000 59.16456  ? 97  LEU   B C     1 
ATOM   4174 O O     . LEU   B 1 97  ? 90.77454  16.56718  9.33079   1.000 62.37320  ? 97  LEU   B O     1 
ATOM   4175 C CB    . LEU   B 1 97  ? 92.15824  16.24343  11.68007  1.000 57.12156  ? 97  LEU   B CB    1 
ATOM   4176 C CG    . LEU   B 1 97  ? 92.98967  15.87555  12.89107  1.000 61.63563  ? 97  LEU   B CG    1 
ATOM   4177 C CD1   . LEU   B 1 97  ? 93.61220  17.12233  13.48904  1.000 70.84462  ? 97  LEU   B CD1   1 
ATOM   4178 C CD2   . LEU   B 1 97  ? 92.09569  15.23239  13.92296  1.000 64.62835  ? 97  LEU   B CD2   1 
ATOM   4179 N N     . GLN   B 1 98  ? 92.59711  16.52003  8.02520   1.000 60.91517  ? 98  GLN   B N     1 
ATOM   4180 C CA    . GLN   B 1 98  ? 91.85925  16.47198  6.76762   1.000 62.80639  ? 98  GLN   B CA    1 
ATOM   4181 C C     . GLN   B 1 98  ? 92.19894  15.22137  5.97845   1.000 60.22746  ? 98  GLN   B C     1 
ATOM   4182 O O     . GLN   B 1 98  ? 92.32217  15.25009  4.74776   1.000 58.10428  ? 98  GLN   B O     1 
ATOM   4183 C CB    . GLN   B 1 98  ? 92.09488  17.73014  5.93410   1.000 57.21884  ? 98  GLN   B CB    1 
ATOM   4184 C CG    . GLN   B 1 98  ? 91.94031  19.01972  6.72267   1.000 53.52949  ? 98  GLN   B CG    1 
ATOM   4185 C CD    . GLN   B 1 98  ? 91.78226  20.25343  5.85631   1.000 59.79176  ? 98  GLN   B CD    1 
ATOM   4186 O OE1   . GLN   B 1 98  ? 91.31256  20.17890  4.71314   1.000 57.87986  ? 98  GLN   B OE1   1 
ATOM   4187 N NE2   . GLN   B 1 98  ? 92.11279  21.41389  6.42373   1.000 69.86505  ? 98  GLN   B NE2   1 
ATOM   4188 N N     . HIS   B 1 99  ? 92.33723  14.10849  6.69484   1.000 56.71005  ? 99  HIS   B N     1 
ATOM   4189 C CA    . HIS   B 1 99  ? 92.68114  12.85728  6.05122   1.000 63.77440  ? 99  HIS   B CA    1 
ATOM   4190 C C     . HIS   B 1 99  ? 91.51789  12.34658  5.21484   1.000 68.98516  ? 99  HIS   B C     1 
ATOM   4191 O O     . HIS   B 1 99  ? 90.35503  12.43811  5.61164   1.000 70.58241  ? 99  HIS   B O     1 
ATOM   4192 C CB    . HIS   B 1 99  ? 93.06604  11.80815  7.07820   1.000 70.80679  ? 99  HIS   B CB    1 
ATOM   4193 C CG    . HIS   B 1 99  ? 93.14650  10.44573  6.49037   1.000 79.42571  ? 99  HIS   B CG    1 
ATOM   4194 N ND1   . HIS   B 1 99  ? 93.79499  10.20699  5.29719   1.000 81.73503  ? 99  HIS   B ND1   1 
ATOM   4195 C CD2   . HIS   B 1 99  ? 92.62256  9.26171   6.88361   1.000 86.69512  ? 99  HIS   B CD2   1 
ATOM   4196 C CE1   . HIS   B 1 99  ? 93.68935  8.92631   4.99207   1.000 87.44080  ? 99  HIS   B CE1   1 
ATOM   4197 N NE2   . HIS   B 1 99  ? 92.98260  8.32960   5.93787   1.000 92.35394  ? 99  HIS   B NE2   1 
ATOM   4198 N N     . PHE   B 1 100 ? 91.84505  11.80246  4.04751   1.000 70.89902  ? 100 PHE   B N     1 
ATOM   4199 C CA    . PHE   B 1 100 ? 90.84542  11.25575  3.15189   1.000 74.13805  ? 100 PHE   B CA    1 
ATOM   4200 C C     . PHE   B 1 100 ? 91.38982  9.98678   2.53184   1.000 78.41474  ? 100 PHE   B C     1 
ATOM   4201 O O     . PHE   B 1 100 ? 92.59625  9.87040   2.29135   1.000 81.00325  ? 100 PHE   B O     1 
ATOM   4202 C CB    . PHE   B 1 100 ? 90.46411  12.24438  2.05123   1.000 72.70960  ? 100 PHE   B CB    1 
ATOM   4203 C CG    . PHE   B 1 100 ? 89.29625  11.80724  1.21514   1.000 74.72792  ? 100 PHE   B CG    1 
ATOM   4204 C CD1   . PHE   B 1 100 ? 89.46566  10.91537  0.16762   1.000 76.41687  ? 100 PHE   B CD1   1 
ATOM   4205 C CD2   . PHE   B 1 100 ? 88.02812  12.31129  1.46076   1.000 78.91430  ? 100 PHE   B CD2   1 
ATOM   4206 C CE1   . PHE   B 1 100 ? 88.38364  10.51211  -0.60587  1.000 80.34063  ? 100 PHE   B CE1   1 
ATOM   4207 C CE2   . PHE   B 1 100 ? 86.94308  11.93090  0.69411   1.000 78.92482  ? 100 PHE   B CE2   1 
ATOM   4208 C CZ    . PHE   B 1 100 ? 87.11889  11.02469  -0.34234  1.000 84.51795  ? 100 PHE   B CZ    1 
ATOM   4209 N N     . SER   B 1 101 ? 90.48025  9.04939   2.27875   1.000 79.36879  ? 101 SER   B N     1 
ATOM   4210 C CA    . SER   B 1 101 ? 90.72037  7.78777   1.58968   1.000 78.72837  ? 101 SER   B CA    1 
ATOM   4211 C C     . SER   B 1 101 ? 89.37036  7.16435   1.27721   1.000 83.62644  ? 101 SER   B C     1 
ATOM   4212 O O     . SER   B 1 101 ? 88.40885  7.33067   2.04015   1.000 84.98195  ? 101 SER   B O     1 
ATOM   4213 C CB    . SER   B 1 101 ? 91.57390  6.84679   2.43934   1.000 76.98726  ? 101 SER   B CB    1 
ATOM   4214 O OG    . SER   B 1 101 ? 91.04289  6.76602   3.74176   1.000 78.91378  ? 101 SER   B OG    1 
ATOM   4215 N N     . MET   B 1 102 ? 89.29440  6.46801   0.14513   1.000 85.12318  ? 102 MET   B N     1 
ATOM   4216 C CA    . MET   B 1 102 ? 88.04837  5.85968   -0.31201  1.000 88.29721  ? 102 MET   B CA    1 
ATOM   4217 C C     . MET   B 1 102 ? 88.31264  4.39357   -0.62544  1.000 91.68662  ? 102 MET   B C     1 
ATOM   4218 O O     . MET   B 1 102 ? 89.15947  4.09520   -1.47209  1.000 95.57244  ? 102 MET   B O     1 
ATOM   4219 C CB    . MET   B 1 102 ? 87.51254  6.58676   -1.54520  1.000 90.94173  ? 102 MET   B CB    1 
ATOM   4220 C CG    . MET   B 1 102 ? 86.36171  5.85843   -2.13177  1.000 91.11578  ? 102 MET   B CG    1 
ATOM   4221 S SD    . MET   B 1 102 ? 84.84565  6.25796   -1.25513  1.000 94.38214  ? 102 MET   B SD    1 
ATOM   4222 C CE    . MET   B 1 102 ? 84.69145  8.01813   -1.61651  1.000 88.46103  ? 102 MET   B CE    1 
ATOM   4223 N N     . ASN   B 1 103 ? 87.61813  3.48266   0.06082   1.000 92.53198  ? 103 ASN   B N     1 
ATOM   4224 C CA    . ASN   B 1 103 ? 87.68148  2.06944   -0.30842  1.000 90.75891  ? 103 ASN   B CA    1 
ATOM   4225 C C     . ASN   B 1 103 ? 86.77276  1.84302   -1.51658  1.000 92.46368  ? 103 ASN   B C     1 
ATOM   4226 O O     . ASN   B 1 103 ? 85.54899  1.97842   -1.41063  1.000 88.82293  ? 103 ASN   B O     1 
ATOM   4227 C CB    . ASN   B 1 103 ? 87.30823  1.15893   0.86692   1.000 82.74963  ? 103 ASN   B CB    1 
ATOM   4228 C CG    . ASN   B 1 103 ? 87.34904  -0.32847  0.48707   1.000 83.29281  ? 103 ASN   B CG    1 
ATOM   4229 O OD1   . ASN   B 1 103 ? 88.13577  -0.74873  -0.36681  1.000 89.72551  ? 103 ASN   B OD1   1 
ATOM   4230 N ND2   . ASN   B 1 103 ? 86.50519  -1.12394  1.12962   1.000 78.40896  ? 103 ASN   B ND2   1 
ATOM   4231 N N     . GLU   B 1 104 ? 87.38335  1.51267   -2.66692  1.000 93.46068  ? 104 GLU   B N     1 
ATOM   4232 C CA    . GLU   B 1 104 ? 86.61494  1.27268   -3.89183  1.000 96.67238  ? 104 GLU   B CA    1 
ATOM   4233 C C     . GLU   B 1 104 ? 85.58363  0.16567   -3.70561  1.000 95.07432  ? 104 GLU   B C     1 
ATOM   4234 O O     . GLU   B 1 104 ? 84.43517  0.27939   -4.15450  1.000 95.05041  ? 104 GLU   B O     1 
ATOM   4235 C CB    . GLU   B 1 104 ? 87.55486  0.92847   -5.05992  1.000 92.60724  ? 104 GLU   B CB    1 
ATOM   4236 C CG    . GLU   B 1 104 ? 88.73034  1.88142   -5.24862  1.000 97.60219  ? 104 GLU   B CG    1 
ATOM   4237 C CD    . GLU   B 1 104 ? 88.29313  3.27035   -5.74602  1.000 107.15327 ? 104 GLU   B CD    1 
ATOM   4238 O OE1   . GLU   B 1 104 ? 88.10396  3.43300   -6.97813  1.000 105.58859 ? 104 GLU   B OE1   1 
ATOM   4239 O OE2   . GLU   B 1 104 ? 88.06615  4.17751   -4.91657  1.000 110.61226 ? 104 GLU   B OE2   1 
ATOM   4240 N N     . THR   B 1 105 ? 85.98988  -0.91100  -3.03789  1.000 92.23642  ? 105 THR   B N     1 
ATOM   4241 C CA    . THR   B 1 105 ? 85.12366  -2.05167  -2.77177  1.000 87.52456  ? 105 THR   B CA    1 
ATOM   4242 C C     . THR   B 1 105 ? 83.81632  -1.63787  -2.09136  1.000 88.55074  ? 105 THR   B C     1 
ATOM   4243 O O     . THR   B 1 105 ? 82.71955  -1.89082  -2.60745  1.000 86.58152  ? 105 THR   B O     1 
ATOM   4244 C CB    . THR   B 1 105 ? 85.89417  -3.03596  -1.90276  1.000 86.49758  ? 105 THR   B CB    1 
ATOM   4245 O OG1   . THR   B 1 105 ? 87.04690  -3.45423  -2.62609  1.000 89.95748  ? 105 THR   B OG1   1 
ATOM   4246 C CG2   . THR   B 1 105 ? 85.06422  -4.24693  -1.60127  1.000 83.68770  ? 105 THR   B CG2   1 
ATOM   4247 N N     . SER   B 1 106 ? 83.91454  -1.01389  -0.91839  1.000 87.09942  ? 106 SER   B N     1 
ATOM   4248 C CA    . SER   B 1 106 ? 82.72868  -0.66113  -0.14677  1.000 87.43297  ? 106 SER   B CA    1 
ATOM   4249 C C     . SER   B 1 106 ? 82.17623  0.72600   -0.46722  1.000 87.81939  ? 106 SER   B C     1 
ATOM   4250 O O     . SER   B 1 106 ? 81.06623  1.04743   -0.02906  1.000 82.96474  ? 106 SER   B O     1 
ATOM   4251 C CB    . SER   B 1 106 ? 83.02869  -0.72746  1.35506   1.000 86.54602  ? 106 SER   B CB    1 
ATOM   4252 O OG    . SER   B 1 106 ? 83.98163  0.24711   1.73773   1.000 89.11349  ? 106 SER   B OG    1 
ATOM   4253 N N     . TRP   B 1 107 ? 82.91850  1.55695   -1.19104  1.000 89.56380  ? 107 TRP   B N     1 
ATOM   4254 C CA    . TRP   B 1 107 ? 82.56046  2.96691   -1.34375  1.000 90.91146  ? 107 TRP   B CA    1 
ATOM   4255 C C     . TRP   B 1 107 ? 82.19327  3.57820   0.00951   1.000 89.35507  ? 107 TRP   B C     1 
ATOM   4256 O O     . TRP   B 1 107 ? 81.24160  4.35454   0.14414   1.000 88.09408  ? 107 TRP   B O     1 
ATOM   4257 C CB    . TRP   B 1 107 ? 81.43208  3.14352   -2.36537  1.000 94.11424  ? 107 TRP   B CB    1 
ATOM   4258 C CG    . TRP   B 1 107 ? 81.72102  2.53178   -3.71676  1.000 94.89959  ? 107 TRP   B CG    1 
ATOM   4259 C CD1   . TRP   B 1 107 ? 81.06087  1.49043   -4.29703  1.000 96.13361  ? 107 TRP   B CD1   1 
ATOM   4260 C CD2   . TRP   B 1 107 ? 82.76822  2.89998   -4.62983  1.000 99.50558  ? 107 TRP   B CD2   1 
ATOM   4261 N NE1   . TRP   B 1 107 ? 81.61201  1.19692   -5.52073  1.000 98.18229  ? 107 TRP   B NE1   1 
ATOM   4262 C CE2   . TRP   B 1 107 ? 82.66342  2.04682   -5.74736  1.000 105.02471 ? 107 TRP   B CE2   1 
ATOM   4263 C CE3   . TRP   B 1 107 ? 83.77793  3.87209   -4.61555  1.000 97.72650  ? 107 TRP   B CE3   1 
ATOM   4264 C CZ2   . TRP   B 1 107 ? 83.53092  2.13555   -6.83993  1.000 109.78833 ? 107 TRP   B CZ2   1 
ATOM   4265 C CZ3   . TRP   B 1 107 ? 84.63939  3.95696   -5.70301  1.000 98.07866  ? 107 TRP   B CZ3   1 
ATOM   4266 C CH2   . TRP   B 1 107 ? 84.50945  3.09437   -6.79672  1.000 104.68317 ? 107 TRP   B CH2   1 
ATOM   4267 N N     . THR   B 1 108 ? 82.94365  3.19334   1.03311   1.000 89.37598  ? 108 THR   B N     1 
ATOM   4268 C CA    . THR   B 1 108 ? 82.92336  3.88381   2.31180   1.000 85.82916  ? 108 THR   B CA    1 
ATOM   4269 C C     . THR   B 1 108 ? 84.18883  4.71884   2.41887   1.000 87.67252  ? 108 THR   B C     1 
ATOM   4270 O O     . THR   B 1 108 ? 85.27882  4.23276   2.09475   1.000 91.47693  ? 108 THR   B O     1 
ATOM   4271 C CB    . THR   B 1 108 ? 82.83744  2.90470   3.47618   1.000 83.86033  ? 108 THR   B CB    1 
ATOM   4272 O OG1   . THR   B 1 108 ? 81.59758  2.19246   3.40815   1.000 88.04509  ? 108 THR   B OG1   1 
ATOM   4273 C CG2   . THR   B 1 108 ? 82.86723  3.67924   4.75525   1.000 89.89097  ? 108 THR   B CG2   1 
ATOM   4274 N N     . ALA   B 1 109 ? 84.04017  5.97564   2.84673   1.000 87.57878  ? 109 ALA   B N     1 
ATOM   4275 C CA    . ALA   B 1 109 ? 85.14637  6.92289   2.95029   1.000 81.81033  ? 109 ALA   B CA    1 
ATOM   4276 C C     . ALA   B 1 109 ? 85.50129  7.16489   4.41298   1.000 79.31419  ? 109 ALA   B C     1 
ATOM   4277 O O     . ALA   B 1 109 ? 84.63812  7.10495   5.29827   1.000 81.59841  ? 109 ALA   B O     1 
ATOM   4278 C CB    . ALA   B 1 109 ? 84.79968  8.25030   2.26748   1.000 79.08551  ? 109 ALA   B CB    1 
ATOM   4279 N N     . ARG   B 1 110 ? 86.78029  7.44109   4.65780   1.000 70.25772  ? 110 ARG   B N     1 
ATOM   4280 C CA    . ARG   B 1 110 ? 87.29993  7.66023   6.00386   1.000 70.30550  ? 110 ARG   B CA    1 
ATOM   4281 C C     . ARG   B 1 110 ? 87.94998  9.03455   6.05189   1.000 70.63739  ? 110 ARG   B C     1 
ATOM   4282 O O     . ARG   B 1 110 ? 89.04747  9.23732   5.52844   1.000 78.07770  ? 110 ARG   B O     1 
ATOM   4283 C CB    . ARG   B 1 110 ? 88.29003  6.55898   6.37441   1.000 77.39220  ? 110 ARG   B CB    1 
ATOM   4284 C CG    . ARG   B 1 110 ? 88.83040  6.59167   7.77591   1.000 78.46973  ? 110 ARG   B CG    1 
ATOM   4285 C CD    . ARG   B 1 110 ? 90.07135  5.73042   7.82997   1.000 91.25611  ? 110 ARG   B CD    1 
ATOM   4286 N NE    . ARG   B 1 110 ? 91.20332  6.47348   8.38767   1.000 109.47727 ? 110 ARG   B NE    1 
ATOM   4287 C CZ    . ARG   B 1 110 ? 92.42382  5.97799   8.56905   1.000 121.71866 ? 110 ARG   B CZ    1 
ATOM   4288 N NH1   . ARG   B 1 110 ? 92.72453  4.73134   8.22050   1.000 123.17188 ? 110 ARG   B NH1   1 
ATOM   4289 N NH2   . ARG   B 1 110 ? 93.36429  6.75067   9.11718   1.000 120.89866 ? 110 ARG   B NH2   1 
ATOM   4290 N N     . LEU   B 1 111 ? 87.28172  9.97475   6.68406   1.000 65.39444  ? 111 LEU   B N     1 
ATOM   4291 C CA    . LEU   B 1 111 ? 87.69741  11.36057  6.66785   1.000 69.26008  ? 111 LEU   B CA    1 
ATOM   4292 C C     . LEU   B 1 111 ? 88.10810  11.81962  8.05916   1.000 69.90417  ? 111 LEU   B C     1 
ATOM   4293 O O     . LEU   B 1 111 ? 87.84619  11.15737  9.06912   1.000 73.79698  ? 111 LEU   B O     1 
ATOM   4294 C CB    . LEU   B 1 111 ? 86.56948  12.24768  6.12691   1.000 67.98348  ? 111 LEU   B CB    1 
ATOM   4295 C CG    . LEU   B 1 111 ? 86.20500  11.92385  4.68027   1.000 63.97068  ? 111 LEU   B CG    1 
ATOM   4296 C CD1   . LEU   B 1 111 ? 85.28558  10.73855  4.60261   1.000 64.46261  ? 111 LEU   B CD1   1 
ATOM   4297 C CD2   . LEU   B 1 111 ? 85.58850  13.14688  4.00901   1.000 61.16419  ? 111 LEU   B CD2   1 
ATOM   4298 N N     . GLY   B 1 112 ? 88.75767  12.97055  8.09942   1.000 63.29042  ? 112 GLY   B N     1 
ATOM   4299 C CA    . GLY   B 1 112 ? 89.02870  13.62493  9.34795   1.000 60.90609  ? 112 GLY   B CA    1 
ATOM   4300 C C     . GLY   B 1 112 ? 88.10950  14.81329  9.49039   1.000 62.24705  ? 112 GLY   B C     1 
ATOM   4301 O O     . GLY   B 1 112 ? 87.55829  15.31212  8.50083   1.000 61.58647  ? 112 GLY   B O     1 
ATOM   4302 N N     . PRO   B 1 113 ? 87.92785  15.29523  10.72750  1.000 59.82043  ? 113 PRO   B N     1 
ATOM   4303 C CA    . PRO   B 1 113 ? 86.95245  16.37682  10.95671  1.000 59.67652  ? 113 PRO   B CA    1 
ATOM   4304 C C     . PRO   B 1 113 ? 87.27673  17.68098  10.25414  1.000 60.91535  ? 113 PRO   B C     1 
ATOM   4305 O O     . PRO   B 1 113 ? 86.34263  18.41229  9.91143   1.000 66.87096  ? 113 PRO   B O     1 
ATOM   4306 C CB    . PRO   B 1 113 ? 86.95996  16.53577  12.47812  1.000 58.83495  ? 113 PRO   B CB    1 
ATOM   4307 C CG    . PRO   B 1 113 ? 88.26884  15.96341  12.89835  1.000 61.51017  ? 113 PRO   B CG    1 
ATOM   4308 C CD    . PRO   B 1 113 ? 88.48986  14.80020  11.98974  1.000 58.81582  ? 113 PRO   B CD    1 
ATOM   4309 N N     . GLY   B 1 114 ? 88.54847  17.98737  9.98853   1.000 57.01566  ? 114 GLY   B N     1 
ATOM   4310 C CA    . GLY   B 1 114 ? 88.89070  19.27136  9.39057   1.000 58.05738  ? 114 GLY   B CA    1 
ATOM   4311 C C     . GLY   B 1 114 ? 88.30739  19.51565  8.01072   1.000 59.30462  ? 114 GLY   B C     1 
ATOM   4312 O O     . GLY   B 1 114 ? 88.18059  20.67706  7.59299   1.000 61.07570  ? 114 GLY   B O     1 
ATOM   4313 N N     . ASN   B 1 115 ? 87.94440  18.45273  7.29495   1.000 58.22165  ? 115 ASN   B N     1 
ATOM   4314 C CA    . ASN   B 1 115 ? 87.50015  18.54131  5.90126   1.000 59.40107  ? 115 ASN   B CA    1 
ATOM   4315 C C     . ASN   B 1 115 ? 86.27209  19.42953  5.73934   1.000 62.80671  ? 115 ASN   B C     1 
ATOM   4316 O O     . ASN   B 1 115 ? 85.20443  19.05740  6.22186   1.000 72.38869  ? 115 ASN   B O     1 
ATOM   4317 C CB    . ASN   B 1 115 ? 87.17185  17.13621  5.43081   1.000 55.44700  ? 115 ASN   B CB    1 
ATOM   4318 C CG    . ASN   B 1 115 ? 88.35712  16.43405  4.86029   1.000 60.48993  ? 115 ASN   B CG    1 
ATOM   4319 O OD1   . ASN   B 1 115 ? 88.83253  16.83392  3.80653   1.000 68.08516  ? 115 ASN   B OD1   1 
ATOM   4320 N ND2   . ASN   B 1 115 ? 88.82506  15.36731  5.51082   1.000 56.70124  ? 115 ASN   B ND2   1 
ATOM   4321 N N     . ARG   B 1 116 ? 86.37758  20.57320  5.03620   1.000 55.36681  ? 116 ARG   B N     1 
ATOM   4322 C CA    . ARG   B 1 116 ? 85.12679  21.30148  4.80044   1.000 55.47007  ? 116 ARG   B CA    1 
ATOM   4323 C C     . ARG   B 1 116 ? 84.25583  20.57606  3.78940   1.000 58.40528  ? 116 ARG   B C     1 
ATOM   4324 O O     . ARG   B 1 116 ? 84.72032  19.71718  3.04464   1.000 63.25115  ? 116 ARG   B O     1 
ATOM   4325 C CB    . ARG   B 1 116 ? 85.34039  22.71180  4.28201   1.000 60.18701  ? 116 ARG   B CB    1 
ATOM   4326 C CG    . ARG   B 1 116 ? 86.43450  23.45774  4.94411   1.000 59.89566  ? 116 ARG   B CG    1 
ATOM   4327 C CD    . ARG   B 1 116 ? 86.33101  23.43592  6.41767   1.000 56.58532  ? 116 ARG   B CD    1 
ATOM   4328 N NE    . ARG   B 1 116 ? 86.84630  24.68472  6.96316   1.000 60.42431  ? 116 ARG   B NE    1 
ATOM   4329 C CZ    . ARG   B 1 116 ? 87.89899  24.78073  7.76803   1.000 61.07699  ? 116 ARG   B CZ    1 
ATOM   4330 N NH1   . ARG   B 1 116 ? 88.62840  23.71852  8.09066   1.000 53.87992  ? 116 ARG   B NH1   1 
ATOM   4331 N NH2   . ARG   B 1 116 ? 88.22832  25.97290  8.25966   1.000 61.67289  ? 116 ARG   B NH2   1 
ATOM   4332 N N     . LEU   B 1 117 ? 82.97696  20.95456  3.74217   1.000 64.81125  ? 117 LEU   B N     1 
ATOM   4333 C CA    . LEU   B 1 117 ? 82.04054  20.24559  2.87477   1.000 63.10430  ? 117 LEU   B CA    1 
ATOM   4334 C C     . LEU   B 1 117 ? 82.49860  20.28310  1.42380   1.000 67.61369  ? 117 LEU   B C     1 
ATOM   4335 O O     . LEU   B 1 117 ? 82.52542  19.24173  0.74703   1.000 66.52270  ? 117 LEU   B O     1 
ATOM   4336 C CB    . LEU   B 1 117 ? 80.62465  20.80572  3.01993   1.000 61.55091  ? 117 LEU   B CB    1 
ATOM   4337 C CG    . LEU   B 1 117 ? 80.06222  20.39826  4.38155   1.000 69.89414  ? 117 LEU   B CG    1 
ATOM   4338 C CD1   . LEU   B 1 117 ? 78.58534  20.79176  4.55501   1.000 66.74910  ? 117 LEU   B CD1   1 
ATOM   4339 C CD2   . LEU   B 1 117 ? 80.30010  18.88811  4.57995   1.000 67.19784  ? 117 LEU   B CD2   1 
ATOM   4340 N N     . GLY   B 1 118 ? 82.89504  21.46886  0.93036   1.000 62.41929  ? 118 GLY   B N     1 
ATOM   4341 C CA    . GLY   B 1 118 ? 83.50737  21.53537  -0.38163  1.000 65.43013  ? 118 GLY   B CA    1 
ATOM   4342 C C     . GLY   B 1 118 ? 84.52853  20.44083  -0.68024  1.000 70.00375  ? 118 GLY   B C     1 
ATOM   4343 O O     . GLY   B 1 118 ? 84.31009  19.56989  -1.53665  1.000 68.24941  ? 118 GLY   B O     1 
ATOM   4344 N N     . ARG   B 1 119 ? 85.66027  20.47224  0.02218   1.000 64.81889  ? 119 ARG   B N     1 
ATOM   4345 C CA    . ARG   B 1 119 ? 86.64326  19.42531  -0.17773  1.000 61.71776  ? 119 ARG   B CA    1 
ATOM   4346 C C     . ARG   B 1 119 ? 86.01795  18.03722  -0.08272  1.000 63.87527  ? 119 ARG   B C     1 
ATOM   4347 O O     . ARG   B 1 119 ? 86.44234  17.12777  -0.80036  1.000 68.22268  ? 119 ARG   B O     1 
ATOM   4348 C CB    . ARG   B 1 119 ? 87.77520  19.59606  0.83092   1.000 66.37408  ? 119 ARG   B CB    1 
ATOM   4349 C CG    . ARG   B 1 119 ? 88.79922  18.48407  0.86696   1.000 65.19702  ? 119 ARG   B CG    1 
ATOM   4350 C CD    . ARG   B 1 119 ? 89.91232  18.84634  1.82482   1.000 60.07037  ? 119 ARG   B CD    1 
ATOM   4351 N NE    . ARG   B 1 119 ? 90.73410  17.69831  2.18258   1.000 64.64924  ? 119 ARG   B NE    1 
ATOM   4352 C CZ    . ARG   B 1 119 ? 91.63081  17.13674  1.38469   1.000 64.10347  ? 119 ARG   B CZ    1 
ATOM   4353 N NH1   . ARG   B 1 119 ? 91.84353  17.59497  0.16503   1.000 67.49207  ? 119 ARG   B NH1   1 
ATOM   4354 N NH2   . ARG   B 1 119 ? 92.33099  16.09105  1.82620   1.000 58.10766  ? 119 ARG   B NH2   1 
ATOM   4355 N N     . VAL   B 1 120 ? 85.00111  17.84500  0.76602   1.000 62.37642  ? 120 VAL   B N     1 
ATOM   4356 C CA    . VAL   B 1 120 ? 84.42748  16.50184  0.90731   1.000 66.38505  ? 120 VAL   B CA    1 
ATOM   4357 C C     . VAL   B 1 120 ? 83.66310  16.12172  -0.35140  1.000 66.78687  ? 120 VAL   B C     1 
ATOM   4358 O O     . VAL   B 1 120 ? 83.85005  15.02759  -0.89816  1.000 63.64573  ? 120 VAL   B O     1 
ATOM   4359 C CB    . VAL   B 1 120 ? 83.52369  16.37022  2.15285   1.000 64.42376  ? 120 VAL   B CB    1 
ATOM   4360 C CG1   . VAL   B 1 120 ? 82.82907  15.02977  2.10007   1.000 58.91831  ? 120 VAL   B CG1   1 
ATOM   4361 C CG2   . VAL   B 1 120 ? 84.31219  16.44208  3.46287   1.000 61.05716  ? 120 VAL   B CG2   1 
ATOM   4362 N N     . THR   B 1 121 ? 82.77982  17.01696  -0.81321  1.000 64.53397  ? 121 THR   B N     1 
ATOM   4363 C CA    . THR   B 1 121 ? 82.04284  16.82012  -2.06374  1.000 68.67092  ? 121 THR   B CA    1 
ATOM   4364 C C     . THR   B 1 121 ? 82.96110  16.36850  -3.20100  1.000 75.21910  ? 121 THR   B C     1 
ATOM   4365 O O     . THR   B 1 121 ? 82.79007  15.28645  -3.78066  1.000 73.32522  ? 121 THR   B O     1 
ATOM   4366 C CB    . THR   B 1 121 ? 81.36800  18.11669  -2.47151  1.000 64.09375  ? 121 THR   B CB    1 
ATOM   4367 O OG1   . THR   B 1 121 ? 80.61983  18.62179  -1.36947  1.000 64.63427  ? 121 THR   B OG1   1 
ATOM   4368 C CG2   . THR   B 1 121 ? 80.44834  17.84650  -3.63020  1.000 68.15674  ? 121 THR   B CG2   1 
ATOM   4369 N N     . GLU   B 1 122 ? 83.90394  17.25058  -3.55997  1.000 73.69397  ? 122 GLU   B N     1 
ATOM   4370 C CA    . GLU   B 1 122 ? 84.95495  17.00820  -4.54538  1.000 70.21433  ? 122 GLU   B CA    1 
ATOM   4371 C C     . GLU   B 1 122 ? 85.65704  15.66233  -4.36723  1.000 73.78159  ? 122 GLU   B C     1 
ATOM   4372 O O     . GLU   B 1 122 ? 85.58744  14.79686  -5.24658  1.000 79.48881  ? 122 GLU   B O     1 
ATOM   4373 C CB    . GLU   B 1 122 ? 85.95878  18.15082  -4.44528  1.000 74.82221  ? 122 GLU   B CB    1 
ATOM   4374 C CG    . GLU   B 1 122 ? 87.19625  18.06599  -5.30277  1.000 81.36381  ? 122 GLU   B CG    1 
ATOM   4375 C CD    . GLU   B 1 122 ? 88.14982  19.20494  -4.98733  1.000 89.31191  ? 122 GLU   B CD    1 
ATOM   4376 O OE1   . GLU   B 1 122 ? 88.86473  19.11448  -3.95539  1.000 81.80522  ? 122 GLU   B OE1   1 
ATOM   4377 O OE2   . GLU   B 1 122 ? 88.14108  20.20808  -5.74327  1.000 87.43602  ? 122 GLU   B OE2   1 
ATOM   4378 N N     . LEU   B 1 123 ? 86.39037  15.48105  -3.26172  1.000 72.01621  ? 123 LEU   B N     1 
ATOM   4379 C CA    . LEU   B 1 123 ? 87.13971  14.23374  -3.07175  1.000 74.18294  ? 123 LEU   B CA    1 
ATOM   4380 C C     . LEU   B 1 123 ? 86.27789  12.97754  -3.23924  1.000 74.40557  ? 123 LEU   B C     1 
ATOM   4381 O O     . LEU   B 1 123 ? 86.80749  11.91237  -3.58905  1.000 72.89339  ? 123 LEU   B O     1 
ATOM   4382 C CB    . LEU   B 1 123 ? 87.78330  14.20243  -1.69182  1.000 72.33134  ? 123 LEU   B CB    1 
ATOM   4383 C CG    . LEU   B 1 123 ? 88.92338  15.18925  -1.53541  1.000 69.10102  ? 123 LEU   B CG    1 
ATOM   4384 C CD1   . LEU   B 1 123 ? 89.49567  15.11049  -0.13424  1.000 66.46368  ? 123 LEU   B CD1   1 
ATOM   4385 C CD2   . LEU   B 1 123 ? 89.97015  14.92326  -2.59010  1.000 72.47253  ? 123 LEU   B CD2   1 
ATOM   4386 N N     . MET   B 1 124 ? 84.97105  13.06839  -2.98908  1.000 73.26028  ? 124 MET   B N     1 
ATOM   4387 C CA    . MET   B 1 124 ? 84.12706  11.89199  -3.15422  1.000 73.74155  ? 124 MET   B CA    1 
ATOM   4388 C C     . MET   B 1 124 ? 83.81416  11.64467  -4.62233  1.000 74.88118  ? 124 MET   B C     1 
ATOM   4389 O O     . MET   B 1 124 ? 84.07802  10.55624  -5.13765  1.000 77.02493  ? 124 MET   B O     1 
ATOM   4390 C CB    . MET   B 1 124 ? 82.85955  12.04876  -2.32636  1.000 76.38235  ? 124 MET   B CB    1 
ATOM   4391 C CG    . MET   B 1 124 ? 83.11283  11.79377  -0.84287  1.000 79.76852  ? 124 MET   B CG    1 
ATOM   4392 S SD    . MET   B 1 124 ? 81.59362  11.73849  0.12644   1.000 80.66157  ? 124 MET   B SD    1 
ATOM   4393 C CE    . MET   B 1 124 ? 82.20363  11.22510  1.72723   1.000 72.51384  ? 124 MET   B CE    1 
ATOM   4394 N N     . TYR   B 1 125 ? 83.26953  12.65360  -5.31014  1.000 75.76950  ? 125 TYR   B N     1 
ATOM   4395 C CA    . TYR   B 1 125 ? 83.09391  12.60494  -6.76434  1.000 75.86799  ? 125 TYR   B CA    1 
ATOM   4396 C C     . TYR   B 1 125 ? 84.34448  12.05854  -7.45795  1.000 77.24902  ? 125 TYR   B C     1 
ATOM   4397 O O     . TYR   B 1 125 ? 84.29347  11.04285  -8.16459  1.000 80.13415  ? 125 TYR   B O     1 
ATOM   4398 C CB    . TYR   B 1 125 ? 82.75970  14.01755  -7.25623  1.000 70.45549  ? 125 TYR   B CB    1 
ATOM   4399 C CG    . TYR   B 1 125 ? 82.33445  14.22256  -8.69801  1.000 73.63003  ? 125 TYR   B CG    1 
ATOM   4400 C CD1   . TYR   B 1 125 ? 80.98922  14.21274  -9.06268  1.000 78.70476  ? 125 TYR   B CD1   1 
ATOM   4401 C CD2   . TYR   B 1 125 ? 83.27047  14.51581  -9.68379  1.000 79.54328  ? 125 TYR   B CD2   1 
ATOM   4402 C CE1   . TYR   B 1 125 ? 80.58178  14.44781  -10.39247 1.000 79.52544  ? 125 TYR   B CE1   1 
ATOM   4403 C CE2   . TYR   B 1 125 ? 82.87576  14.74755  -11.01611 1.000 86.42082  ? 125 TYR   B CE2   1 
ATOM   4404 C CZ    . TYR   B 1 125 ? 81.53503  14.70889  -11.36548 1.000 81.71853  ? 125 TYR   B CZ    1 
ATOM   4405 O OH    . TYR   B 1 125 ? 81.18588  14.93420  -12.68584 1.000 80.80545  ? 125 TYR   B OH    1 
ATOM   4406 N N     . ASN   B 1 126 ? 85.48828  12.70850  -7.23500  1.000 75.71021  ? 126 ASN   B N     1 
ATOM   4407 C CA    . ASN   B 1 126 ? 86.70855  12.34220  -7.95274  1.000 75.36568  ? 126 ASN   B CA    1 
ATOM   4408 C C     . ASN   B 1 126 ? 87.13567  10.90526  -7.70432  1.000 73.15027  ? 126 ASN   B C     1 
ATOM   4409 O O     . ASN   B 1 126 ? 87.66271  10.27555  -8.61745  1.000 80.85007  ? 126 ASN   B O     1 
ATOM   4410 C CB    . ASN   B 1 126 ? 87.86144  13.29113  -7.60755  1.000 75.33232  ? 126 ASN   B CB    1 
ATOM   4411 C CG    . ASN   B 1 126 ? 87.71612  14.67365  -8.25726  1.000 71.61103  ? 126 ASN   B CG    1 
ATOM   4412 O OD1   . ASN   B 1 126 ? 86.81224  14.92797  -9.06630  1.000 68.82630  ? 126 ASN   B OD1   1 
ATOM   4413 N ND2   . ASN   B 1 126 ? 88.63373  15.56582  -7.91496  1.000 72.96469  ? 126 ASN   B ND2   1 
ATOM   4414 N N     . ASN   B 1 127 ? 86.94918  10.36859  -6.50372  1.000 76.12982  ? 127 ASN   B N     1 
ATOM   4415 C CA    . ASN   B 1 127 ? 87.37327  8.98828   -6.21954  1.000 81.18384  ? 127 ASN   B CA    1 
ATOM   4416 C C     . ASN   B 1 127 ? 86.22244  7.99106   -6.36829  1.000 83.82080  ? 127 ASN   B C     1 
ATOM   4417 O O     . ASN   B 1 127 ? 85.93520  7.19720   -5.47795  1.000 90.26532  ? 127 ASN   B O     1 
ATOM   4418 C CB    . ASN   B 1 127 ? 88.01049  8.90459   -4.84022  1.000 78.46183  ? 127 ASN   B CB    1 
ATOM   4419 C CG    . ASN   B 1 127 ? 89.33456  9.61334   -4.79095  1.000 77.67591  ? 127 ASN   B CG    1 
ATOM   4420 O OD1   . ASN   B 1 127 ? 89.41857  10.81219  -5.05417  1.000 75.00149  ? 127 ASN   B OD1   1 
ATOM   4421 N ND2   . ASN   B 1 127 ? 90.38773  8.87449   -4.46660  1.000 81.34540  ? 127 ASN   B ND2   1 
ATOM   4422 N N     . GLY   B 1 128 ? 85.57515  8.01775   -7.53375  1.000 81.65467  ? 128 GLY   B N     1 
ATOM   4423 C CA    . GLY   B 1 128 ? 84.51317  7.07596   -7.81340  1.000 81.93740  ? 128 GLY   B CA    1 
ATOM   4424 C C     . GLY   B 1 128 ? 83.11752  7.66576   -7.91649  1.000 81.57291  ? 128 GLY   B C     1 
ATOM   4425 O O     . GLY   B 1 128 ? 82.13520  6.97113   -7.64107  1.000 90.39909  ? 128 GLY   B O     1 
ATOM   4426 N N     . GLY   B 1 129 ? 82.99354  8.92440   -8.31902  1.000 72.65117  ? 129 GLY   B N     1 
ATOM   4427 C CA    . GLY   B 1 129 ? 81.67144  9.48542   -8.53141  1.000 77.12729  ? 129 GLY   B CA    1 
ATOM   4428 C C     . GLY   B 1 129 ? 80.66404  9.21050   -7.43205  1.000 80.06937  ? 129 GLY   B C     1 
ATOM   4429 O O     . GLY   B 1 129 ? 79.52768  8.79743   -7.69956  1.000 77.21271  ? 129 GLY   B O     1 
ATOM   4430 N N     . ARG   B 1 130 ? 81.08328  9.44814   -6.18557  1.000 77.52180  ? 130 ARG   B N     1 
ATOM   4431 C CA    . ARG   B 1 130 ? 80.28849  9.25704   -4.97975  1.000 79.39366  ? 130 ARG   B CA    1 
ATOM   4432 C C     . ARG   B 1 130 ? 79.90640  10.61023  -4.38843  1.000 77.74373  ? 130 ARG   B C     1 
ATOM   4433 O O     . ARG   B 1 130 ? 80.54104  11.63154  -4.66305  1.000 73.64101  ? 130 ARG   B O     1 
ATOM   4434 C CB    . ARG   B 1 130 ? 81.05078  8.46740   -3.90127  1.000 80.87763  ? 130 ARG   B CB    1 
ATOM   4435 C CG    . ARG   B 1 130 ? 81.83176  7.22760   -4.33363  1.000 83.00572  ? 130 ARG   B CG    1 
ATOM   4436 C CD    . ARG   B 1 130 ? 80.99953  6.16494   -5.03352  1.000 89.28931  ? 130 ARG   B CD    1 
ATOM   4437 N NE    . ARG   B 1 130 ? 79.88915  5.62777   -4.25385  1.000 88.59182  ? 130 ARG   B NE    1 
ATOM   4438 C CZ    . ARG   B 1 130 ? 79.20728  4.54504   -4.60286  1.000 88.93370  ? 130 ARG   B CZ    1 
ATOM   4439 N NH1   . ARG   B 1 130 ? 79.54379  3.83275   -5.66823  1.000 90.41779  ? 130 ARG   B NH1   1 
ATOM   4440 N NH2   . ARG   B 1 130 ? 78.17167  4.16158   -3.86138  1.000 87.46554  ? 130 ARG   B NH2   1 
ATOM   4441 N N     . HIS   B 1 131 ? 78.87238  10.59524  -3.54774  1.000 76.58681  ? 131 HIS   B N     1 
ATOM   4442 C CA    . HIS   B 1 131 ? 78.50093  11.75254  -2.74758  1.000 72.64553  ? 131 HIS   B CA    1 
ATOM   4443 C C     . HIS   B 1 131 ? 77.87770  11.26434  -1.45611  1.000 72.26021  ? 131 HIS   B C     1 
ATOM   4444 O O     . HIS   B 1 131 ? 77.86749  10.06706  -1.16458  1.000 76.28982  ? 131 HIS   B O     1 
ATOM   4445 C CB    . HIS   B 1 131 ? 77.53833  12.68169  -3.48230  1.000 73.67380  ? 131 HIS   B CB    1 
ATOM   4446 C CG    . HIS   B 1 131 ? 76.13086  12.18230  -3.54576  1.000 78.46916  ? 131 HIS   B CG    1 
ATOM   4447 N ND1   . HIS   B 1 131 ? 75.05188  12.95988  -3.17425  1.000 76.05043  ? 131 HIS   B ND1   1 
ATOM   4448 C CD2   . HIS   B 1 131 ? 75.61825  11.00506  -3.98159  1.000 80.54736  ? 131 HIS   B CD2   1 
ATOM   4449 C CE1   . HIS   B 1 131 ? 73.93581  12.27869  -3.36999  1.000 79.26405  ? 131 HIS   B CE1   1 
ATOM   4450 N NE2   . HIS   B 1 131 ? 74.25124  11.08953  -3.85876  1.000 83.80513  ? 131 HIS   B NE2   1 
ATOM   4451 N N     . VAL   B 1 132 ? 77.35361  12.19817  -0.67757  1.000 68.69089  ? 132 VAL   B N     1 
ATOM   4452 C CA    . VAL   B 1 132 ? 76.72573  11.85026  0.58956   1.000 71.82127  ? 132 VAL   B CA    1 
ATOM   4453 C C     . VAL   B 1 132 ? 75.95222  13.06161  1.08972   1.000 77.19002  ? 132 VAL   B C     1 
ATOM   4454 O O     . VAL   B 1 132 ? 76.52414  14.15504  1.24138   1.000 78.05016  ? 132 VAL   B O     1 
ATOM   4455 C CB    . VAL   B 1 132 ? 77.75473  11.37545  1.62022   1.000 68.83904  ? 132 VAL   B CB    1 
ATOM   4456 C CG1   . VAL   B 1 132 ? 78.80753  12.40909  1.78088   1.000 68.94253  ? 132 VAL   B CG1   1 
ATOM   4457 C CG2   . VAL   B 1 132 ? 77.06775  11.17794  2.93687   1.000 71.95682  ? 132 VAL   B CG2   1 
ATOM   4458 N N     . PRO   B 1 133 ? 74.65920  12.90196  1.35974   1.000 78.36840  ? 133 PRO   B N     1 
ATOM   4459 C CA    . PRO   B 1 133 ? 73.80362  14.05353  1.68939   1.000 79.62169  ? 133 PRO   B CA    1 
ATOM   4460 C C     . PRO   B 1 133 ? 74.43670  14.99932  2.69357   1.000 74.26425  ? 133 PRO   B C     1 
ATOM   4461 O O     . PRO   B 1 133 ? 74.98007  14.57702  3.71540   1.000 76.12668  ? 133 PRO   B O     1 
ATOM   4462 C CB    . PRO   B 1 133 ? 72.54892  13.39253  2.27240   1.000 83.15846  ? 133 PRO   B CB    1 
ATOM   4463 C CG    . PRO   B 1 133 ? 72.97745  11.94168  2.59842   1.000 77.67156  ? 133 PRO   B CG    1 
ATOM   4464 C CD    . PRO   B 1 133 ? 73.96241  11.61654  1.53748   1.000 71.40883  ? 133 PRO   B CD    1 
ATOM   4465 N N     . HIS   B 1 134 ? 74.33558  16.29101  2.41862   1.000 72.90525  ? 134 HIS   B N     1 
ATOM   4466 C CA    . HIS   B 1 134 ? 74.88808  17.25071  3.36274   1.000 71.86498  ? 134 HIS   B CA    1 
ATOM   4467 C C     . HIS   B 1 134 ? 74.48691  18.65438  2.94216   1.000 72.04207  ? 134 HIS   B C     1 
ATOM   4468 O O     . HIS   B 1 134 ? 73.98263  18.88531  1.83361   1.000 72.68508  ? 134 HIS   B O     1 
ATOM   4469 C CB    . HIS   B 1 134 ? 76.40799  17.13002  3.46317   1.000 68.29943  ? 134 HIS   B CB    1 
ATOM   4470 C CG    . HIS   B 1 134 ? 77.10432  17.42167  2.17799   1.000 73.48765  ? 134 HIS   B CG    1 
ATOM   4471 N ND1   . HIS   B 1 134 ? 77.13909  18.68316  1.62179   1.000 74.34406  ? 134 HIS   B ND1   1 
ATOM   4472 C CD2   . HIS   B 1 134 ? 77.73874  16.60442  1.30300   1.000 75.48760  ? 134 HIS   B CD2   1 
ATOM   4473 C CE1   . HIS   B 1 134 ? 77.78348  18.63456  0.46851   1.000 73.05726  ? 134 HIS   B CE1   1 
ATOM   4474 N NE2   . HIS   B 1 134 ? 78.15698  17.38426  0.25006   1.000 74.65842  ? 134 HIS   B NE2   1 
ATOM   4475 N N     . GLY   B 1 135 ? 74.72648  19.58021  3.87263   1.000 70.30633  ? 135 GLY   B N     1 
ATOM   4476 C CA    . GLY   B 1 135 ? 74.46902  20.99770  3.76839   1.000 71.85154  ? 135 GLY   B CA    1 
ATOM   4477 C C     . GLY   B 1 135 ? 75.01513  21.55623  2.48417   1.000 73.96827  ? 135 GLY   B C     1 
ATOM   4478 O O     . GLY   B 1 135 ? 76.00481  21.03032  1.95663   1.000 70.87550  ? 135 GLY   B O     1 
ATOM   4479 N N     . THR   B 1 136 ? 74.38051  22.58851  1.94809   1.000 79.20252  ? 136 THR   B N     1 
ATOM   4480 C CA    . THR   B 1 136 ? 74.85098  23.10871  0.67096   1.000 81.91365  ? 136 THR   B CA    1 
ATOM   4481 C C     . THR   B 1 136 ? 76.11349  23.95425  0.80355   1.000 76.09375  ? 136 THR   B C     1 
ATOM   4482 O O     . THR   B 1 136 ? 76.93986  23.95007  -0.11658  1.000 77.46062  ? 136 THR   B O     1 
ATOM   4483 C CB    . THR   B 1 136 ? 73.73560  23.88618  -0.02637  1.000 72.88140  ? 136 THR   B CB    1 
ATOM   4484 O OG1   . THR   B 1 136 ? 73.26722  24.93499  0.83485   1.000 71.68274  ? 136 THR   B OG1   1 
ATOM   4485 C CG2   . THR   B 1 136 ? 72.62390  22.92852  -0.36655  1.000 72.57322  ? 136 THR   B CG2   1 
ATOM   4486 N N     . THR   B 1 137 ? 76.32333  24.63369  1.93324   1.000 67.74634  ? 137 THR   B N     1 
ATOM   4487 C CA    . THR   B 1 137 ? 77.43346  25.57793  2.02167   1.000 66.99986  ? 137 THR   B CA    1 
ATOM   4488 C C     . THR   B 1 137 ? 78.76432  24.86219  2.22098   1.000 66.12495  ? 137 THR   B C     1 
ATOM   4489 O O     . THR   B 1 137 ? 78.90800  24.05195  3.13429   1.000 70.78239  ? 137 THR   B O     1 
ATOM   4490 C CB    . THR   B 1 137 ? 77.19428  26.53181  3.16982   1.000 64.94888  ? 137 THR   B CB    1 
ATOM   4491 O OG1   . THR   B 1 137 ? 75.94432  27.16775  2.94418   1.000 67.82520  ? 137 THR   B OG1   1 
ATOM   4492 C CG2   . THR   B 1 137 ? 78.27369  27.57651  3.15563   1.000 61.77351  ? 137 THR   B CG2   1 
ATOM   4493 N N     . PHE   B 1 138 ? 79.76292  25.21028  1.39778   1.000 66.48461  ? 138 PHE   B N     1 
ATOM   4494 C CA    . PHE   B 1 138 ? 80.99629  24.42013  1.29622   1.000 64.30372  ? 138 PHE   B CA    1 
ATOM   4495 C C     . PHE   B 1 138 ? 82.00128  24.71872  2.39839   1.000 65.07538  ? 138 PHE   B C     1 
ATOM   4496 O O     . PHE   B 1 138 ? 82.90381  23.89682  2.62709   1.000 64.97692  ? 138 PHE   B O     1 
ATOM   4497 C CB    . PHE   B 1 138 ? 81.65662  24.67623  -0.05634  1.000 62.67781  ? 138 PHE   B CB    1 
ATOM   4498 C CG    . PHE   B 1 138 ? 81.34576  23.63817  -1.10267  1.000 66.35694  ? 138 PHE   B CG    1 
ATOM   4499 C CD1   . PHE   B 1 138 ? 80.34700  22.71068  -0.91815  1.000 70.95643  ? 138 PHE   B CD1   1 
ATOM   4500 C CD2   . PHE   B 1 138 ? 82.01256  23.64829  -2.32006  1.000 70.15467  ? 138 PHE   B CD2   1 
ATOM   4501 C CE1   . PHE   B 1 138 ? 80.05823  21.77714  -1.91301  1.000 71.02712  ? 138 PHE   B CE1   1 
ATOM   4502 C CE2   . PHE   B 1 138 ? 81.72617  22.72282  -3.31530  1.000 65.13270  ? 138 PHE   B CE2   1 
ATOM   4503 C CZ    . PHE   B 1 138 ? 80.74952  21.79017  -3.10877  1.000 64.80509  ? 138 PHE   B CZ    1 
ATOM   4504 N N     . THR   B 1 139 ? 81.87753  25.88388  3.05697   1.000 59.76934  ? 139 THR   B N     1 
ATOM   4505 C CA    . THR   B 1 139 ? 82.75605  26.31683  4.13634   1.000 56.57509  ? 139 THR   B CA    1 
ATOM   4506 C C     . THR   B 1 139 ? 82.43881  25.65793  5.46777   1.000 60.25652  ? 139 THR   B C     1 
ATOM   4507 O O     . THR   B 1 139 ? 83.19207  25.82767  6.43687   1.000 55.77325  ? 139 THR   B O     1 
ATOM   4508 C CB    . THR   B 1 139 ? 82.65012  27.82160  4.29294   1.000 53.14379  ? 139 THR   B CB    1 
ATOM   4509 O OG1   . THR   B 1 139 ? 81.27273  28.17963  4.21205   1.000 58.45839  ? 139 THR   B OG1   1 
ATOM   4510 C CG2   . THR   B 1 139 ? 83.43036  28.51911  3.23005   1.000 51.15141  ? 139 THR   B CG2   1 
ATOM   4511 N N     . VAL   B 1 140 ? 81.32824  24.92844  5.54361   1.000 65.12639  ? 140 VAL   B N     1 
ATOM   4512 C CA    . VAL   B 1 140 ? 80.99656  24.16615  6.73624   1.000 65.06492  ? 140 VAL   B CA    1 
ATOM   4513 C C     . VAL   B 1 140 ? 81.95047  22.99332  6.88954   1.000 63.00573  ? 140 VAL   B C     1 
ATOM   4514 O O     . VAL   B 1 140 ? 82.26587  22.28994  5.92428   1.000 58.98379  ? 140 VAL   B O     1 
ATOM   4515 C CB    . VAL   B 1 140 ? 79.53736  23.70065  6.67011   1.000 63.36077  ? 140 VAL   B CB    1 
ATOM   4516 C CG1   . VAL   B 1 140 ? 79.36632  22.40831  7.47123   1.000 58.03675  ? 140 VAL   B CG1   1 
ATOM   4517 C CG2   . VAL   B 1 140 ? 78.62344  24.82684  7.16892   1.000 62.51821  ? 140 VAL   B CG2   1 
ATOM   4518 N N     . GLY   B 1 141 ? 82.41988  22.78556  8.11680   1.000 60.33868  ? 141 GLY   B N     1 
ATOM   4519 C CA    . GLY   B 1 141 ? 83.32047  21.68753  8.40684   1.000 57.88773  ? 141 GLY   B CA    1 
ATOM   4520 C C     . GLY   B 1 141 ? 82.56653  20.42954  8.79303   1.000 60.80103  ? 141 GLY   B C     1 
ATOM   4521 O O     . GLY   B 1 141 ? 81.58784  20.47904  9.53235   1.000 69.93189  ? 141 GLY   B O     1 
ATOM   4522 N N     . LEU   B 1 142 ? 83.04368  19.30076  8.27464   1.000 57.48238  ? 142 LEU   B N     1 
ATOM   4523 C CA    . LEU   B 1 142 ? 82.50908  17.99239  8.63993   1.000 57.89499  ? 142 LEU   B CA    1 
ATOM   4524 C C     . LEU   B 1 142 ? 82.44735  17.80983  10.15684  1.000 63.05217  ? 142 LEU   B C     1 
ATOM   4525 O O     . LEU   B 1 142 ? 81.49166  17.22709  10.68518  1.000 64.27348  ? 142 LEU   B O     1 
ATOM   4526 C CB    . LEU   B 1 142 ? 83.37430  16.90331  8.01657   1.000 54.32968  ? 142 LEU   B CB    1 
ATOM   4527 C CG    . LEU   B 1 142 ? 82.92460  15.46544  8.14371   1.000 50.96814  ? 142 LEU   B CG    1 
ATOM   4528 C CD1   . LEU   B 1 142 ? 81.78691  15.30520  7.20453   1.000 51.92592  ? 142 LEU   B CD1   1 
ATOM   4529 C CD2   . LEU   B 1 142 ? 84.06068  14.54436  7.76624   1.000 57.98805  ? 142 LEU   B CD2   1 
ATOM   4530 N N     . GLY   B 1 143 ? 83.45200  18.30804  10.87564  1.000 58.83514  ? 143 GLY   B N     1 
ATOM   4531 C CA    . GLY   B 1 143 ? 83.52844  18.10556  12.30754  1.000 60.60212  ? 143 GLY   B CA    1 
ATOM   4532 C C     . GLY   B 1 143 ? 82.25658  18.39582  13.09004  1.000 64.59492  ? 143 GLY   B C     1 
ATOM   4533 O O     . GLY   B 1 143 ? 81.63884  17.47694  13.64621  1.000 62.64274  ? 143 GLY   B O     1 
ATOM   4534 N N     . GLY   B 1 144 ? 81.88235  19.67495  13.17472  1.000 66.03016  ? 144 GLY   B N     1 
ATOM   4535 C CA    . GLY   B 1 144 ? 80.62261  20.08214  13.77533  1.000 68.87559  ? 144 GLY   B CA    1 
ATOM   4536 C C     . GLY   B 1 144 ? 79.46634  20.11019  12.78688  1.000 68.18452  ? 144 GLY   B C     1 
ATOM   4537 O O     . GLY   B 1 144 ? 78.58014  20.96133  12.89141  1.000 68.83063  ? 144 GLY   B O     1 
ATOM   4538 N N     . HIS   B 1 145 ? 79.47147  19.19051  11.81703  1.000 64.63067  ? 145 HIS   B N     1 
ATOM   4539 C CA    . HIS   B 1 145 ? 78.37131  19.04648  10.86702  1.000 66.01546  ? 145 HIS   B CA    1 
ATOM   4540 C C     . HIS   B 1 145 ? 77.79033  17.64876  11.01195  1.000 67.42080  ? 145 HIS   B C     1 
ATOM   4541 O O     . HIS   B 1 145 ? 76.77176  17.48971  11.67483  1.000 67.70455  ? 145 HIS   B O     1 
ATOM   4542 C CB    . HIS   B 1 145 ? 78.82982  19.33378  9.42665   1.000 65.88164  ? 145 HIS   B CB    1 
ATOM   4543 C CG    . HIS   B 1 145 ? 77.70605  19.42547  8.42790   1.000 68.84094  ? 145 HIS   B CG    1 
ATOM   4544 N ND1   . HIS   B 1 145 ? 76.89023  20.53555  8.31971   1.000 69.37840  ? 145 HIS   B ND1   1 
ATOM   4545 C CD2   . HIS   B 1 145 ? 77.27422  18.55230  7.48546   1.000 68.69910  ? 145 HIS   B CD2   1 
ATOM   4546 C CE1   . HIS   B 1 145 ? 75.99825  20.33776  7.36680   1.000 66.24055  ? 145 HIS   B CE1   1 
ATOM   4547 N NE2   . HIS   B 1 145 ? 76.21569  19.14502  6.84029   1.000 71.29643  ? 145 HIS   B NE2   1 
ATOM   4548 N N     . ALA   B 1 146 ? 78.43637  16.62726  10.45321  1.000 68.11120  ? 146 ALA   B N     1 
ATOM   4549 C CA    . ALA   B 1 146 ? 78.06762  15.23625  10.69095  1.000 69.07448  ? 146 ALA   B CA    1 
ATOM   4550 C C     . ALA   B 1 146 ? 77.79773  14.91068  12.17315  1.000 72.16718  ? 146 ALA   B C     1 
ATOM   4551 O O     . ALA   B 1 146 ? 77.22444  13.85804  12.48361  1.000 67.79133  ? 146 ALA   B O     1 
ATOM   4552 C CB    . ALA   B 1 146 ? 79.15988  14.32001  10.12660  1.000 58.94116  ? 146 ALA   B CB    1 
ATOM   4553 N N     . THR   B 1 147 ? 78.16219  15.79555  13.10232  1.000 70.61827  ? 147 THR   B N     1 
ATOM   4554 C CA    . THR   B 1 147 ? 77.77570  15.56747  14.48593  1.000 70.02280  ? 147 THR   B CA    1 
ATOM   4555 C C     . THR   B 1 147 ? 76.47343  16.26192  14.88484  1.000 73.32618  ? 147 THR   B C     1 
ATOM   4556 O O     . THR   B 1 147 ? 75.75782  15.72938  15.73903  1.000 73.71138  ? 147 THR   B O     1 
ATOM   4557 C CB    . THR   B 1 147 ? 78.88132  16.02602  15.43372  1.000 70.19701  ? 147 THR   B CB    1 
ATOM   4558 O OG1   . THR   B 1 147 ? 79.10879  17.42898  15.26244  1.000 72.50866  ? 147 THR   B OG1   1 
ATOM   4559 C CG2   . THR   B 1 147 ? 80.13636  15.28578  15.09149  1.000 63.98866  ? 147 THR   B CG2   1 
ATOM   4560 N N     . VAL   B 1 148 ? 76.12880  17.41284  14.29686  1.000 72.14778  ? 148 VAL   B N     1 
ATOM   4561 C CA    . VAL   B 1 148 ? 74.81652  17.99799  14.58114  1.000 69.63598  ? 148 VAL   B CA    1 
ATOM   4562 C C     . VAL   B 1 148 ? 73.70474  17.40890  13.70106  1.000 69.83223  ? 148 VAL   B C     1 
ATOM   4563 O O     . VAL   B 1 148 ? 72.53505  17.53245  14.05182  1.000 79.82878  ? 148 VAL   B O     1 
ATOM   4564 C CB    . VAL   B 1 148 ? 74.82107  19.53255  14.46139  1.000 73.35575  ? 148 VAL   B CB    1 
ATOM   4565 C CG1   . VAL   B 1 148 ? 75.70899  20.20748  15.55672  1.000 67.61013  ? 148 VAL   B CG1   1 
ATOM   4566 C CG2   . VAL   B 1 148 ? 75.21484  19.93951  13.05678  1.000 75.79866  ? 148 VAL   B CG2   1 
ATOM   4567 N N     . GLY   B 1 149 ? 74.03103  16.76395  12.58085  1.000 70.27010  ? 149 GLY   B N     1 
ATOM   4568 C CA    . GLY   B 1 149 ? 73.02996  16.13997  11.71630  1.000 68.68395  ? 149 GLY   B CA    1 
ATOM   4569 C C     . GLY   B 1 149 ? 73.29774  16.26074  10.21784  1.000 73.62357  ? 149 GLY   B C     1 
ATOM   4570 O O     . GLY   B 1 149 ? 73.57463  15.26252  9.53331   1.000 69.89969  ? 149 GLY   B O     1 
ATOM   4571 N N     . GLY   B 1 150 ? 73.18966  17.48549  9.68937   1.000 73.81686  ? 150 GLY   B N     1 
ATOM   4572 C CA    . GLY   B 1 150 ? 73.66296  17.78788  8.34966   1.000 70.18586  ? 150 GLY   B CA    1 
ATOM   4573 C C     . GLY   B 1 150 ? 72.72407  17.45690  7.21373   1.000 70.63450  ? 150 GLY   B C     1 
ATOM   4574 O O     . GLY   B 1 150 ? 72.72541  16.33090  6.69550   1.000 68.38311  ? 150 GLY   B O     1 
ATOM   4575 N N     . ALA   B 1 151 ? 71.95487  18.46276  6.79145   1.000 67.99610  ? 151 ALA   B N     1 
ATOM   4576 C CA    . ALA   B 1 151 ? 70.87676  18.29446  5.83141   1.000 69.09656  ? 151 ALA   B CA    1 
ATOM   4577 C C     . ALA   B 1 151 ? 71.02922  19.27512  4.68422   1.000 78.31488  ? 151 ALA   B C     1 
ATOM   4578 O O     . ALA   B 1 151 ? 71.28643  20.46369  4.89550   1.000 80.41321  ? 151 ALA   B O     1 
ATOM   4579 C CB    . ALA   B 1 151 ? 69.52625  18.50777  6.48613   1.000 67.30502  ? 151 ALA   B CB    1 
ATOM   4580 N N     . GLY   B 1 152 ? 70.85307  18.77427  3.47948   1.000 82.20777  ? 152 GLY   B N     1 
ATOM   4581 C CA    . GLY   B 1 152 ? 70.87921  19.61075  2.29613   1.000 80.75216  ? 152 GLY   B CA    1 
ATOM   4582 C C     . GLY   B 1 152 ? 70.12800  18.91810  1.18602   1.000 87.37550  ? 152 GLY   B C     1 
ATOM   4583 O O     . GLY   B 1 152 ? 69.22948  18.11326  1.44125   1.000 85.59878  ? 152 GLY   B O     1 
ATOM   4584 N N     . ALA   B 1 153 ? 70.54475  19.19711  -0.04735  1.000 88.98197  ? 153 ALA   B N     1 
ATOM   4585 C CA    . ALA   B 1 153 ? 69.77076  18.84005  -1.23051  1.000 78.38331  ? 153 ALA   B CA    1 
ATOM   4586 C C     . ALA   B 1 153 ? 69.25853  17.38930  -1.21913  1.000 82.41132  ? 153 ALA   B C     1 
ATOM   4587 O O     . ALA   B 1 153 ? 68.06842  17.14287  -1.44521  1.000 82.31240  ? 153 ALA   B O     1 
ATOM   4588 C CB    . ALA   B 1 153 ? 70.61851  19.12482  -2.47258  1.000 71.69535  ? 153 ALA   B CB    1 
ATOM   4589 N N     . ALA   B 1 154 ? 70.13234  16.40517  -0.96679  1.000 79.56204  ? 154 ALA   B N     1 
ATOM   4590 C CA    . ALA   B 1 154 ? 69.77266  14.99979  -1.18845  1.000 87.49017  ? 154 ALA   B CA    1 
ATOM   4591 C C     . ALA   B 1 154 ? 69.19223  14.30822  0.05415   1.000 92.16274  ? 154 ALA   B C     1 
ATOM   4592 O O     . ALA   B 1 154 ? 69.07876  13.06471  0.07038   1.000 87.88563  ? 154 ALA   B O     1 
ATOM   4593 C CB    . ALA   B 1 154 ? 70.98004  14.22108  -1.70233  1.000 85.51928  ? 154 ALA   B CB    1 
ATOM   4594 N N     . SER   B 1 155 ? 68.79825  15.07552  1.08074   1.000 93.65133  ? 155 SER   B N     1 
ATOM   4595 C CA    . SER   B 1 155 ? 68.35058  14.46551  2.33569   1.000 92.87301  ? 155 SER   B CA    1 
ATOM   4596 C C     . SER   B 1 155 ? 66.97928  13.78239  2.18520   1.000 95.04259  ? 155 SER   B C     1 
ATOM   4597 O O     . SER   B 1 155 ? 66.82934  12.60252  2.53909   1.000 92.86926  ? 155 SER   B O     1 
ATOM   4598 C CB    . SER   B 1 155 ? 68.36780  15.50116  3.46792   1.000 84.46007  ? 155 SER   B CB    1 
ATOM   4599 O OG    . SER   B 1 155 ? 69.69065  15.96281  3.75459   1.000 82.05087  ? 155 SER   B OG    1 
ATOM   4600 N N     . ARG   B 1 156 ? 65.96484  14.48935  1.63567   1.000 97.13927  ? 156 ARG   B N     1 
ATOM   4601 C CA    . ARG   B 1 156 ? 64.64450  13.87737  1.41421   1.000 92.00107  ? 156 ARG   B CA    1 
ATOM   4602 C C     . ARG   B 1 156 ? 64.68955  12.71466  0.41391   1.000 91.20174  ? 156 ARG   B C     1 
ATOM   4603 O O     . ARG   B 1 156 ? 63.65593  12.09162  0.14489   1.000 96.44622  ? 156 ARG   B O     1 
ATOM   4604 C CB    . ARG   B 1 156 ? 63.62030  14.93971  0.96472   1.000 79.07866  ? 156 ARG   B CB    1 
ATOM   4605 N N     . MET   B 1 157 ? 65.85722  12.41354  -0.13789  1.000 88.67150  ? 157 MET   B N     1 
ATOM   4606 C CA    . MET   B 1 157 ? 66.05397  11.29346  -1.03969  1.000 100.21040 ? 157 MET   B CA    1 
ATOM   4607 C C     . MET   B 1 157 ? 67.05247  10.27660  -0.51956  1.000 100.23206 ? 157 MET   B C     1 
ATOM   4608 O O     . MET   B 1 157 ? 67.03360  9.12196   -0.96391  1.000 102.36866 ? 157 MET   B O     1 
ATOM   4609 C CB    . MET   B 1 157 ? 66.53535  11.77507  -2.42531  1.000 103.63383 ? 157 MET   B CB    1 
ATOM   4610 C CG    . MET   B 1 157 ? 67.37395  10.72340  -3.18679  1.000 104.34866 ? 157 MET   B CG    1 
ATOM   4611 S SD    . MET   B 1 157 ? 67.94302  11.25246  -4.81465  1.000 126.75866 ? 157 MET   B SD    1 
ATOM   4612 C CE    . MET   B 1 157 ? 68.12939  9.70720   -5.71425  1.000 109.53866 ? 157 MET   B CE    1 
ATOM   4613 N N     . HIS   B 1 158 ? 67.94568  10.66742  0.36863   1.000 90.75534  ? 158 HIS   B N     1 
ATOM   4614 C CA    . HIS   B 1 158 ? 68.94040  9.73622   0.86761   1.000 86.96283  ? 158 HIS   B CA    1 
ATOM   4615 C C     . HIS   B 1 158 ? 69.08238  9.75475   2.37618   1.000 84.70609  ? 158 HIS   B C     1 
ATOM   4616 O O     . HIS   B 1 158 ? 69.52958  8.75029   2.93355   1.000 83.38507  ? 158 HIS   B O     1 
ATOM   4617 C CB    . HIS   B 1 158 ? 70.30094  10.00999  0.21225   1.000 85.35182  ? 158 HIS   B CB    1 
ATOM   4618 C CG    . HIS   B 1 158 ? 70.51058  9.31337   -1.10111  1.000 91.05690  ? 158 HIS   B CG    1 
ATOM   4619 N ND1   . HIS   B 1 158 ? 70.10057  8.01901   -1.33371  1.000 94.23474  ? 158 HIS   B ND1   1 
ATOM   4620 C CD2   . HIS   B 1 158 ? 71.07849  9.73570   -2.25742  1.000 97.62523  ? 158 HIS   B CD2   1 
ATOM   4621 C CE1   . HIS   B 1 158 ? 70.42609  7.66550   -2.56615  1.000 97.27697  ? 158 HIS   B CE1   1 
ATOM   4622 N NE2   . HIS   B 1 158 ? 71.01661  8.69204   -3.15069  1.000 96.67261  ? 158 HIS   B NE2   1 
ATOM   4623 N N     . GLY   B 1 159 ? 68.69290  10.83522  3.04691   1.000 83.96529  ? 159 GLY   B N     1 
ATOM   4624 C CA    . GLY   B 1 159 ? 68.73774  10.93516  4.49158   1.000 80.91853  ? 159 GLY   B CA    1 
ATOM   4625 C C     . GLY   B 1 159 ? 69.67046  12.03615  4.96568   1.000 81.82724  ? 159 GLY   B C     1 
ATOM   4626 O O     . GLY   B 1 159 ? 70.26603  12.77298  4.18232   1.000 84.68833  ? 159 GLY   B O     1 
ATOM   4627 N N     . LEU   B 1 160 ? 69.78916  12.13647  6.28570   1.000 77.88090  ? 160 LEU   B N     1 
ATOM   4628 C CA    . LEU   B 1 160 ? 70.78974  13.03695  6.83714   1.000 76.77557  ? 160 LEU   B CA    1 
ATOM   4629 C C     . LEU   B 1 160 ? 72.20162  12.51200  6.59060   1.000 77.55209  ? 160 LEU   B C     1 
ATOM   4630 O O     . LEU   B 1 160 ? 72.42277  11.32441  6.31135   1.000 76.85361  ? 160 LEU   B O     1 
ATOM   4631 C CB    . LEU   B 1 160 ? 70.57737  13.25009  8.32963   1.000 74.79775  ? 160 LEU   B CB    1 
ATOM   4632 C CG    . LEU   B 1 160 ? 69.26757  13.96989  8.62934   1.000 81.19696  ? 160 LEU   B CG    1 
ATOM   4633 C CD1   . LEU   B 1 160 ? 69.36112  14.70536  9.97045   1.000 75.95866  ? 160 LEU   B CD1   1 
ATOM   4634 C CD2   . LEU   B 1 160 ? 68.90622  14.91699  7.48458   1.000 77.71866  ? 160 LEU   B CD2   1 
ATOM   4635 N N     . LEU   B 1 161 ? 73.16841  13.42920  6.67776   1.000 79.65827  ? 161 LEU   B N     1 
ATOM   4636 C CA    . LEU   B 1 161 ? 74.56981  13.01964  6.65386   1.000 79.58905  ? 161 LEU   B CA    1 
ATOM   4637 C C     . LEU   B 1 161 ? 74.81814  11.87789  7.63647   1.000 77.02019  ? 161 LEU   B C     1 
ATOM   4638 O O     . LEU   B 1 161 ? 75.33976  10.81627  7.25960   1.000 70.65836  ? 161 LEU   B O     1 
ATOM   4639 C CB    . LEU   B 1 161 ? 75.47945  14.21397  6.95652   1.000 70.17635  ? 161 LEU   B CB    1 
ATOM   4640 C CG    . LEU   B 1 161 ? 76.95698  13.86654  7.17978   1.000 64.24000  ? 161 LEU   B CG    1 
ATOM   4641 C CD1   . LEU   B 1 161 ? 77.46997  12.90562  6.13781   1.000 56.11909  ? 161 LEU   B CD1   1 
ATOM   4642 C CD2   . LEU   B 1 161 ? 77.83414  15.13204  7.24413   1.000 66.13415  ? 161 LEU   B CD2   1 
ATOM   4643 N N     . LEU   B 1 162 ? 74.40843  12.06939  8.90428   1.000 74.37549  ? 162 LEU   B N     1 
ATOM   4644 C CA    . LEU   B 1 162 ? 74.74762  11.12671  9.96048   1.000 72.00618  ? 162 LEU   B CA    1 
ATOM   4645 C C     . LEU   B 1 162 ? 74.08701  9.77187   9.77031   1.000 72.77008  ? 162 LEU   B C     1 
ATOM   4646 O O     . LEU   B 1 162 ? 74.44829  8.81584   10.47274  1.000 76.37697  ? 162 LEU   B O     1 
ATOM   4647 C CB    . LEU   B 1 162 ? 74.39039  11.70702  11.33358  1.000 65.99094  ? 162 LEU   B CB    1 
ATOM   4648 C CG    . LEU   B 1 162 ? 73.00840  12.26311  11.64052  1.000 66.46050  ? 162 LEU   B CG    1 
ATOM   4649 C CD1   . LEU   B 1 162 ? 71.98627  11.16893  11.53820  1.000 72.54676  ? 162 LEU   B CD1   1 
ATOM   4650 C CD2   . LEU   B 1 162 ? 72.98081  12.93564  13.00808  1.000 67.61648  ? 162 LEU   B CD2   1 
ATOM   4651 N N     . ASP   B 1 163 ? 73.14657  9.66161   8.84604   1.000 70.09757  ? 163 ASP   B N     1 
ATOM   4652 C CA    . ASP   B 1 163 ? 72.57435  8.36658   8.54090   1.000 71.46279  ? 163 ASP   B CA    1 
ATOM   4653 C C     . ASP   B 1 163 ? 73.51643  7.55123   7.65443   1.000 72.39484  ? 163 ASP   B C     1 
ATOM   4654 O O     . ASP   B 1 163 ? 73.18937  6.42262   7.27485   1.000 71.48945  ? 163 ASP   B O     1 
ATOM   4655 C CB    . ASP   B 1 163 ? 71.18105  8.56171   7.91545   1.000 70.19240  ? 163 ASP   B CB    1 
ATOM   4656 C CG    . ASP   B 1 163 ? 70.18217  9.37211   8.84200   1.000 86.93352  ? 163 ASP   B CG    1 
ATOM   4657 O OD1   . ASP   B 1 163 ? 69.90327  9.02578   10.02877  1.000 83.82118  ? 163 ASP   B OD1   1 
ATOM   4658 O OD2   . ASP   B 1 163 ? 69.66483  10.40939  8.36649   1.000 93.60866  ? 163 ASP   B OD2   1 
ATOM   4659 N N     . TYR   B 1 164 ? 74.70240  8.08619   7.34758   1.000 72.96160  ? 164 TYR   B N     1 
ATOM   4660 C CA    . TYR   B 1 164 ? 75.71504  7.35673   6.59808   1.000 76.12742  ? 164 TYR   B CA    1 
ATOM   4661 C C     . TYR   B 1 164 ? 77.01162  7.15354   7.36656   1.000 76.50060  ? 164 TYR   B C     1 
ATOM   4662 O O     . TYR   B 1 164 ? 77.78954  6.25075   7.01293   1.000 74.10836  ? 164 TYR   B O     1 
ATOM   4663 C CB    . TYR   B 1 164 ? 76.01144  8.07993   5.27584   1.000 74.29727  ? 164 TYR   B CB    1 
ATOM   4664 C CG    . TYR   B 1 164 ? 74.89442  7.87714   4.29350   1.000 72.52590  ? 164 TYR   B CG    1 
ATOM   4665 C CD1   . TYR   B 1 164 ? 73.73680  8.63362   4.39039   1.000 72.12513  ? 164 TYR   B CD1   1 
ATOM   4666 C CD2   . TYR   B 1 164 ? 74.97838  6.92911   3.28875   1.000 72.58705  ? 164 TYR   B CD2   1 
ATOM   4667 C CE1   . TYR   B 1 164 ? 72.70107  8.46120   3.51841   1.000 72.70972  ? 164 TYR   B CE1   1 
ATOM   4668 C CE2   . TYR   B 1 164 ? 73.93589  6.74669   2.39900   1.000 77.59894  ? 164 TYR   B CE2   1 
ATOM   4669 C CZ    . TYR   B 1 164 ? 72.79327  7.51739   2.51841   1.000 80.04156  ? 164 TYR   B CZ    1 
ATOM   4670 O OH    . TYR   B 1 164 ? 71.72975  7.35041   1.63903   1.000 87.20356  ? 164 TYR   B OH    1 
ATOM   4671 N N     . VAL   B 1 165 ? 77.25964  7.95483   8.40978   1.000 76.59029  ? 165 VAL   B N     1 
ATOM   4672 C CA    . VAL   B 1 165 ? 78.37036  7.70048   9.31830   1.000 75.15485  ? 165 VAL   B CA    1 
ATOM   4673 C C     . VAL   B 1 165 ? 78.24156  6.31344   9.90330   1.000 77.00481  ? 165 VAL   B C     1 
ATOM   4674 O O     . VAL   B 1 165 ? 77.27606  5.98834   10.60251  1.000 73.76786  ? 165 VAL   B O     1 
ATOM   4675 C CB    . VAL   B 1 165 ? 78.41958  8.71582   10.45169  1.000 70.05456  ? 165 VAL   B CB    1 
ATOM   4676 C CG1   . VAL   B 1 165 ? 79.52853  8.31201   11.37058  1.000 71.47667  ? 165 VAL   B CG1   1 
ATOM   4677 C CG2   . VAL   B 1 165 ? 78.69425  10.07158  9.94101   1.000 68.64529  ? 165 VAL   B CG2   1 
ATOM   4678 N N     . GLU   B 1 166 ? 79.26420  5.51564   9.69140   1.000 77.01039  ? 166 GLU   B N     1 
ATOM   4679 C CA    . GLU   B 1 166 ? 79.24975  4.11809   10.11120  1.000 77.07377  ? 166 GLU   B CA    1 
ATOM   4680 C C     . GLU   B 1 166 ? 79.94032  4.04210   11.47101  1.000 82.57731  ? 166 GLU   B C     1 
ATOM   4681 O O     . GLU   B 1 166 ? 79.29826  3.80237   12.50016  1.000 83.08144  ? 166 GLU   B O     1 
ATOM   4682 C CB    . GLU   B 1 166 ? 79.92747  3.28812   9.03224   1.000 75.35543  ? 166 GLU   B CB    1 
ATOM   4683 C CG    . GLU   B 1 166 ? 79.93202  1.80254   9.19445   1.000 85.10569  ? 166 GLU   B CG    1 
ATOM   4684 C CD    . GLU   B 1 166 ? 80.55355  1.17638   7.96689   1.000 101.21515 ? 166 GLU   B CD    1 
ATOM   4685 O OE1   . GLU   B 1 166 ? 79.93238  1.26795   6.88962   1.000 103.77866 ? 166 GLU   B OE1   1 
ATOM   4686 O OE2   . GLU   B 1 166 ? 81.68309  0.64222   8.05843   1.000 112.96256 ? 166 GLU   B OE2   1 
ATOM   4687 N N     . GLU   B 1 167 ? 81.24175  4.31991   11.48917  1.000 81.11464  ? 167 GLU   B N     1 
ATOM   4688 C CA    . GLU   B 1 167 ? 82.09210  4.20347   12.65978  1.000 73.15377  ? 167 GLU   B CA    1 
ATOM   4689 C C     . GLU   B 1 167 ? 82.66208  5.57694   13.00731  1.000 73.85282  ? 167 GLU   B C     1 
ATOM   4690 O O     . GLU   B 1 167 ? 82.61902  6.49811   12.19002  1.000 75.72110  ? 167 GLU   B O     1 
ATOM   4691 C CB    . GLU   B 1 167 ? 83.20531  3.21306   12.36598  1.000 70.61528  ? 167 GLU   B CB    1 
ATOM   4692 C CG    . GLU   B 1 167 ? 83.90797  2.68052   13.55979  1.000 75.29038  ? 167 GLU   B CG    1 
ATOM   4693 C CD    . GLU   B 1 167 ? 84.95331  1.66599   13.16323  1.000 87.81094  ? 167 GLU   B CD    1 
ATOM   4694 O OE1   . GLU   B 1 167 ? 85.37547  1.66842   11.97705  1.000 88.40361  ? 167 GLU   B OE1   1 
ATOM   4695 O OE2   . GLU   B 1 167 ? 85.33639  0.85253   14.03299  1.000 92.03853  ? 167 GLU   B OE2   1 
ATOM   4696 N N     . VAL   B 1 168 ? 83.20460  5.72712   14.22566  1.000 71.83500  ? 168 VAL   B N     1 
ATOM   4697 C CA    . VAL   B 1 168 ? 83.91471  6.94936   14.60358  1.000 68.02780  ? 168 VAL   B CA    1 
ATOM   4698 C C     . VAL   B 1 168 ? 85.08664  6.65443   15.52288  1.000 70.85508  ? 168 VAL   B C     1 
ATOM   4699 O O     . VAL   B 1 168 ? 85.11608  5.64871   16.23002  1.000 74.28544  ? 168 VAL   B O     1 
ATOM   4700 C CB    . VAL   B 1 168 ? 83.03074  7.99167   15.30611  1.000 67.34341  ? 168 VAL   B CB    1 
ATOM   4701 C CG1   . VAL   B 1 168 ? 82.25421  8.77443   14.28340  1.000 63.64065  ? 168 VAL   B CG1   1 
ATOM   4702 C CG2   . VAL   B 1 168 ? 82.12553  7.31892   16.32880  1.000 73.11428  ? 168 VAL   B CG2   1 
ATOM   4703 N N     . GLU   B 1 169 ? 86.04877  7.57959   15.52015  1.000 71.59709  ? 169 GLU   B N     1 
ATOM   4704 C CA    . GLU   B 1 169 ? 87.12775  7.64525   16.50430  1.000 67.11039  ? 169 GLU   B CA    1 
ATOM   4705 C C     . GLU   B 1 169 ? 86.93473  8.87980   17.37231  1.000 64.05291  ? 169 GLU   B C     1 
ATOM   4706 O O     . GLU   B 1 169 ? 86.73538  9.98330   16.84796  1.000 66.71724  ? 169 GLU   B O     1 
ATOM   4707 C CB    . GLU   B 1 169 ? 88.49386  7.70834   15.83817  1.000 68.42729  ? 169 GLU   B CB    1 
ATOM   4708 C CG    . GLU   B 1 169 ? 89.62980  7.78329   16.82440  1.000 72.68363  ? 169 GLU   B CG    1 
ATOM   4709 C CD    . GLU   B 1 169 ? 90.98871  7.70577   16.14452  1.000 83.84936  ? 169 GLU   B CD    1 
ATOM   4710 O OE1   . GLU   B 1 169 ? 91.22073  8.47255   15.17330  1.000 80.94594  ? 169 GLU   B OE1   1 
ATOM   4711 O OE2   . GLU   B 1 169 ? 91.82021  6.86564   16.56676  1.000 86.78250  ? 169 GLU   B OE2   1 
ATOM   4712 N N     . VAL   B 1 170 ? 86.99894  8.70158   18.68711  1.000 57.45172  ? 170 VAL   B N     1 
ATOM   4713 C CA    . VAL   B 1 170 ? 86.56635  9.73111   19.61674  1.000 55.52155  ? 170 VAL   B CA    1 
ATOM   4714 C C     . VAL   B 1 170 ? 87.57730  9.86027   20.74491  1.000 60.49765  ? 170 VAL   B C     1 
ATOM   4715 O O     . VAL   B 1 170 ? 88.05650  8.86181   21.30185  1.000 57.97806  ? 170 VAL   B O     1 
ATOM   4716 C CB    . VAL   B 1 170 ? 85.16095  9.42573   20.18060  1.000 57.99995  ? 170 VAL   B CB    1 
ATOM   4717 C CG1   . VAL   B 1 170 ? 84.62277  10.61393  21.00193  1.000 58.76484  ? 170 VAL   B CG1   1 
ATOM   4718 C CG2   . VAL   B 1 170 ? 84.22809  9.09435   19.05028  1.000 60.89472  ? 170 VAL   B CG2   1 
ATOM   4719 N N     . VAL   B 1 171 ? 87.90197  11.10125  21.07029  1.000 57.59349  ? 171 VAL   B N     1 
ATOM   4720 C CA    . VAL   B 1 171 ? 88.70754  11.41199  22.23391  1.000 60.43001  ? 171 VAL   B CA    1 
ATOM   4721 C C     . VAL   B 1 171 ? 87.72729  11.75236  23.35635  1.000 61.12604  ? 171 VAL   B C     1 
ATOM   4722 O O     . VAL   B 1 171 ? 87.05955  12.78068  23.31503  1.000 61.20352  ? 171 VAL   B O     1 
ATOM   4723 C CB    . VAL   B 1 171 ? 89.68789  12.55738  21.93464  1.000 57.18426  ? 171 VAL   B CB    1 
ATOM   4724 C CG1   . VAL   B 1 171 ? 90.30586  13.07751  23.18893  1.000 55.56936  ? 171 VAL   B CG1   1 
ATOM   4725 C CG2   . VAL   B 1 171 ? 90.76893  12.08420  20.98122  1.000 49.77578  ? 171 VAL   B CG2   1 
ATOM   4726 N N     . LEU   B 1 172 ? 87.57367  10.84135  24.31669  1.000 64.58953  ? 172 LEU   B N     1 
ATOM   4727 C CA    . LEU   B 1 172 ? 86.75969  11.03286  25.51105  1.000 62.20807  ? 172 LEU   B CA    1 
ATOM   4728 C C     . LEU   B 1 172 ? 87.45482  11.98343  26.47480  1.000 64.53321  ? 172 LEU   B C     1 
ATOM   4729 O O     . LEU   B 1 172 ? 88.68106  12.07094  26.50814  1.000 64.54537  ? 172 LEU   B O     1 
ATOM   4730 C CB    . LEU   B 1 172 ? 86.51787  9.68819   26.19789  1.000 61.17118  ? 172 LEU   B CB    1 
ATOM   4731 C CG    . LEU   B 1 172 ? 85.87512  8.58894   25.36268  1.000 66.24209  ? 172 LEU   B CG    1 
ATOM   4732 C CD1   . LEU   B 1 172 ? 85.99131  7.19963   26.00995  1.000 65.32831  ? 172 LEU   B CD1   1 
ATOM   4733 C CD2   . LEU   B 1 172 ? 84.41880  8.99003   25.24063  1.000 69.48947  ? 172 LEU   B CD2   1 
ATOM   4734 N N     . ALA   B 1 173 ? 86.66043  12.66593  27.30677  1.000 68.07883  ? 173 ALA   B N     1 
ATOM   4735 C CA    . ALA   B 1 173 ? 87.21133  13.71715  28.16440  1.000 65.20177  ? 173 ALA   B CA    1 
ATOM   4736 C C     . ALA   B 1 173 ? 88.26270  13.23991  29.17252  1.000 64.22975  ? 173 ALA   B C     1 
ATOM   4737 O O     . ALA   B 1 173 ? 88.88085  14.10796  29.80304  1.000 65.19026  ? 173 ALA   B O     1 
ATOM   4738 C CB    . ALA   B 1 173 ? 86.09929  14.42608  28.92817  1.000 69.97768  ? 173 ALA   B CB    1 
ATOM   4739 N N     . ASN   B 1 174 ? 88.44775  11.91143  29.37575  1.000 60.46357  ? 174 ASN   B N     1 
ATOM   4740 C CA    . ASN   B 1 174 ? 89.55714  11.35111  30.16475  1.000 62.35770  ? 174 ASN   B CA    1 
ATOM   4741 C C     . ASN   B 1 174 ? 90.76211  11.02477  29.29566  1.000 62.37921  ? 174 ASN   B C     1 
ATOM   4742 O O     . ASN   B 1 174 ? 91.63907  10.26916  29.71755  1.000 64.23553  ? 174 ASN   B O     1 
ATOM   4743 C CB    . ASN   B 1 174 ? 89.12423  10.11128  30.99375  1.000 65.94687  ? 174 ASN   B CB    1 
ATOM   4744 C CG    . ASN   B 1 174 ? 88.60322  8.90995   30.15238  1.000 64.43338  ? 174 ASN   B CG    1 
ATOM   4745 O OD1   . ASN   B 1 174 ? 88.62476  8.94776   28.93341  1.000 72.39902  ? 174 ASN   B OD1   1 
ATOM   4746 N ND2   . ASN   B 1 174 ? 88.09039  7.86648   30.83254  1.000 64.98003  ? 174 ASN   B ND2   1 
ATOM   4747 N N     . SER   B 1 175 ? 90.78368  11.57465  28.08023  1.000 62.48440  ? 175 SER   B N     1 
ATOM   4748 C CA    . SER   B 1 175 ? 91.79969  11.43675  27.03939  1.000 59.18674  ? 175 SER   B CA    1 
ATOM   4749 C C     . SER   B 1 175 ? 91.94142  10.01690  26.49796  1.000 57.90989  ? 175 SER   B C     1 
ATOM   4750 O O     . SER   B 1 175 ? 92.79970  9.77508   25.63088  1.000 59.00066  ? 175 SER   B O     1 
ATOM   4751 C CB    . SER   B 1 175 ? 93.15170  11.98284  27.51171  1.000 57.52286  ? 175 SER   B CB    1 
ATOM   4752 O OG    . SER   B 1 175 ? 93.00609  13.34132  27.90384  1.000 62.44831  ? 175 SER   B OG    1 
ATOM   4753 N N     . SER   B 1 176 ? 91.10326  9.07374   26.92059  1.000 57.72875  ? 176 SER   B N     1 
ATOM   4754 C CA    . SER   B 1 176 ? 91.07878  7.77467   26.25673  1.000 61.81031  ? 176 SER   B CA    1 
ATOM   4755 C C     . SER   B 1 176 ? 90.54269  7.92170   24.83307  1.000 60.38086  ? 176 SER   B C     1 
ATOM   4756 O O     . SER   B 1 176 ? 89.70427  8.77791   24.55245  1.000 63.05348  ? 176 SER   B O     1 
ATOM   4757 C CB    . SER   B 1 176 ? 90.23480  6.76665   27.04393  1.000 66.46814  ? 176 SER   B CB    1 
ATOM   4758 O OG    . SER   B 1 176 ? 90.84872  6.38194   28.27183  1.000 71.07421  ? 176 SER   B OG    1 
ATOM   4759 N N     . ILE   B 1 177 ? 91.06547  7.10547   23.91702  1.000 63.55735  ? 177 ILE   B N     1 
ATOM   4760 C CA    . ILE   B 1 177 ? 90.69203  7.13951   22.50103  1.000 60.41900  ? 177 ILE   B CA    1 
ATOM   4761 C C     . ILE   B 1 177 ? 89.91915  5.87681   22.18244  1.000 63.50317  ? 177 ILE   B C     1 
ATOM   4762 O O     . ILE   B 1 177 ? 90.47804  4.77575   22.22357  1.000 59.15946  ? 177 ILE   B O     1 
ATOM   4763 C CB    . ILE   B 1 177 ? 91.90832  7.24417   21.57521  1.000 50.31358  ? 177 ILE   B CB    1 
ATOM   4764 C CG1   . ILE   B 1 177 ? 92.76134  8.43394   21.95046  1.000 55.03476  ? 177 ILE   B CG1   1 
ATOM   4765 C CG2   . ILE   B 1 177 ? 91.47550  7.33629   20.14848  1.000 53.23412  ? 177 ILE   B CG2   1 
ATOM   4766 C CD1   . ILE   B 1 177 ? 94.09531  8.37573   21.30463  1.000 61.86598  ? 177 ILE   B CD1   1 
ATOM   4767 N N     . VAL   B 1 178 ? 88.64840  6.03352   21.83474  1.000 67.70780  ? 178 VAL   B N     1 
ATOM   4768 C CA    . VAL   B 1 178 ? 87.76120  4.89961   21.63060  1.000 64.15374  ? 178 VAL   B CA    1 
ATOM   4769 C C     . VAL   B 1 178 ? 87.06221  5.08152   20.29570  1.000 65.25525  ? 178 VAL   B C     1 
ATOM   4770 O O     . VAL   B 1 178 ? 86.91530  6.20315   19.79755  1.000 61.28773  ? 178 VAL   B O     1 
ATOM   4771 C CB    . VAL   B 1 178 ? 86.73854  4.74842   22.78574  1.000 69.19743  ? 178 VAL   B CB    1 
ATOM   4772 C CG1   . VAL   B 1 178 ? 87.42022  4.37385   24.10720  1.000 67.30610  ? 178 VAL   B CG1   1 
ATOM   4773 C CG2   . VAL   B 1 178 ? 85.98084  6.04215   22.98482  1.000 70.98301  ? 178 VAL   B CG2   1 
ATOM   4774 N N     . ARG   B 1 179 ? 86.67326  3.95511   19.70274  1.000 72.17606  ? 179 ARG   B N     1 
ATOM   4775 C CA    . ARG   B 1 179 ? 85.85881  3.88687   18.49903  1.000 72.80889  ? 179 ARG   B CA    1 
ATOM   4776 C C     . ARG   B 1 179 ? 84.40725  3.62131   18.88797  1.000 74.94962  ? 179 ARG   B C     1 
ATOM   4777 O O     . ARG   B 1 179 ? 84.12051  3.20347   20.01243  1.000 75.63151  ? 179 ARG   B O     1 
ATOM   4778 C CB    . ARG   B 1 179 ? 86.38466  2.78939   17.57401  1.000 72.48096  ? 179 ARG   B CB    1 
ATOM   4779 C CG    . ARG   B 1 179 ? 87.86743  2.92578   17.35171  1.000 67.16002  ? 179 ARG   B CG    1 
ATOM   4780 C CD    . ARG   B 1 179 ? 88.34901  2.18804   16.12293  1.000 79.90880  ? 179 ARG   B CD    1 
ATOM   4781 N NE    . ARG   B 1 179 ? 87.79585  2.72988   14.88471  1.000 93.70301  ? 179 ARG   B NE    1 
ATOM   4782 C CZ    . ARG   B 1 179 ? 88.12043  3.90688   14.35967  1.000 90.61795  ? 179 ARG   B CZ    1 
ATOM   4783 N NH1   . ARG   B 1 179 ? 89.01202  4.69943   14.93893  1.000 88.35461  ? 179 ARG   B NH1   1 
ATOM   4784 N NH2   . ARG   B 1 179 ? 87.54248  4.29462   13.21852  1.000 88.30241  ? 179 ARG   B NH2   1 
ATOM   4785 N N     . ALA   B 1 180 ? 83.48736  3.88206   17.95194  1.000 74.02021  ? 180 ALA   B N     1 
ATOM   4786 C CA    . ALA   B 1 180 ? 82.06210  3.71317   18.22840  1.000 75.98232  ? 180 ALA   B CA    1 
ATOM   4787 C C     . ALA   B 1 180 ? 81.29424  3.42873   16.94600  1.000 79.77964  ? 180 ALA   B C     1 
ATOM   4788 O O     . ALA   B 1 180 ? 81.72208  3.80642   15.85064  1.000 81.38561  ? 180 ALA   B O     1 
ATOM   4789 C CB    . ALA   B 1 180 ? 81.45822  4.93537   18.92276  1.000 71.88526  ? 180 ALA   B CB    1 
ATOM   4790 N N     . SER   B 1 181 ? 80.14218  2.79194   17.10365  1.000 80.50680  ? 181 SER   B N     1 
ATOM   4791 C CA    . SER   B 1 181 ? 79.35453  2.34956   15.97118  1.000 83.01939  ? 181 SER   B CA    1 
ATOM   4792 C C     . SER   B 1 181 ? 77.98192  1.92811   16.47672  1.000 89.18680  ? 181 SER   B C     1 
ATOM   4793 O O     . SER   B 1 181 ? 77.63354  2.15424   17.64042  1.000 89.75203  ? 181 SER   B O     1 
ATOM   4794 C CB    . SER   B 1 181 ? 80.06447  1.19871   15.24967  1.000 78.97241  ? 181 SER   B CB    1 
ATOM   4795 O OG    . SER   B 1 181 ? 80.15918  0.09493   16.11210  1.000 77.71877  ? 181 SER   B OG    1 
ATOM   4796 N N     . LYS   B 1 182 ? 77.18924  1.32171   15.58514  1.000 89.69935  ? 182 LYS   B N     1 
ATOM   4797 C CA    . LYS   B 1 182 ? 75.90897  0.77242   16.00410  1.000 90.45114  ? 182 LYS   B CA    1 
ATOM   4798 C C     . LYS   B 1 182 ? 76.10649  -0.43756  16.90676  1.000 96.77035  ? 182 LYS   B C     1 
ATOM   4799 O O     . LYS   B 1 182 ? 75.30443  -0.67442  17.81955  1.000 100.29032 ? 182 LYS   B O     1 
ATOM   4800 C CB    . LYS   B 1 182 ? 75.06761  0.42270   14.77414  1.000 98.28945  ? 182 LYS   B CB    1 
ATOM   4801 C CG    . LYS   B 1 182 ? 74.27157  1.62202   14.19180  1.000 104.41866 ? 182 LYS   B CG    1 
ATOM   4802 C CD    . LYS   B 1 182 ? 73.31680  1.21519   13.04686  1.000 102.19508 ? 182 LYS   B CD    1 
ATOM   4803 C CE    . LYS   B 1 182 ? 72.31572  2.32514   12.69741  1.000 93.82188  ? 182 LYS   B CE    1 
ATOM   4804 N NZ    . LYS   B 1 182 ? 72.94297  3.57293   12.18997  1.000 88.31229  ? 182 LYS   B NZ    1 
ATOM   4805 N N     . SER   B 1 183 ? 77.19335  -1.17882  16.71022  1.000 95.02692  ? 183 SER   B N     1 
ATOM   4806 C CA    . SER   B 1 183 ? 77.44052  -2.39213  17.47895  1.000 91.56496  ? 183 SER   B CA    1 
ATOM   4807 C C     . SER   B 1 183 ? 78.70779  -2.28860  18.32529  1.000 88.59974  ? 183 SER   B C     1 
ATOM   4808 O O     . SER   B 1 183 ? 79.52888  -3.21492  18.33359  1.000 87.29846  ? 183 SER   B O     1 
ATOM   4809 C CB    . SER   B 1 183 ? 77.53283  -3.58123  16.52117  1.000 95.59780  ? 183 SER   B CB    1 
ATOM   4810 O OG    . SER   B 1 183 ? 78.58054  -3.38804  15.57729  1.000 89.78074  ? 183 SER   B OG    1 
ATOM   4811 N N     . HIS   B 1 184 ? 78.88133  -1.16809  19.03609  1.000 88.22437  ? 184 HIS   B N     1 
ATOM   4812 C CA    . HIS   B 1 184 ? 80.08315  -0.88810  19.82330  1.000 85.18786  ? 184 HIS   B CA    1 
ATOM   4813 C C     . HIS   B 1 184 ? 79.92957  0.47997   20.49172  1.000 80.97802  ? 184 HIS   B C     1 
ATOM   4814 O O     . HIS   B 1 184 ? 79.46275  1.43387   19.85993  1.000 82.23079  ? 184 HIS   B O     1 
ATOM   4815 C CB    . HIS   B 1 184 ? 81.33147  -0.95096  18.92479  1.000 85.29087  ? 184 HIS   B CB    1 
ATOM   4816 C CG    . HIS   B 1 184 ? 82.63862  -0.71548  19.63543  1.000 88.09889  ? 184 HIS   B CG    1 
ATOM   4817 N ND1   . HIS   B 1 184 ? 83.07306  -1.50071  20.68366  1.000 88.04173  ? 184 HIS   B ND1   1 
ATOM   4818 C CD2   . HIS   B 1 184 ? 83.62474  0.19323   19.41916  1.000 86.97472  ? 184 HIS   B CD2   1 
ATOM   4819 C CE1   . HIS   B 1 184 ? 84.25502  -1.07548  21.09679  1.000 83.90995  ? 184 HIS   B CE1   1 
ATOM   4820 N NE2   . HIS   B 1 184 ? 84.61070  -0.04479  20.34934  1.000 87.44144  ? 184 HIS   B NE2   1 
ATOM   4821 N N     . ASN   B 1 185 ? 80.29807  0.57582   21.77133  1.000 72.44267  ? 185 ASN   B N     1 
ATOM   4822 C CA    . ASN   B 1 185 ? 80.02365  1.73515   22.62075  1.000 82.31660  ? 185 ASN   B CA    1 
ATOM   4823 C C     . ASN   B 1 185 ? 78.77508  2.48385   22.15924  1.000 87.64798  ? 185 ASN   B C     1 
ATOM   4824 O O     . ASN   B 1 185 ? 78.77524  3.71920   22.06178  1.000 84.81630  ? 185 ASN   B O     1 
ATOM   4825 C CB    . ASN   B 1 185 ? 81.21744  2.69591   22.65383  1.000 85.98598  ? 185 ASN   B CB    1 
ATOM   4826 C CG    . ASN   B 1 185 ? 82.55257  1.98863   22.89461  1.000 83.27985  ? 185 ASN   B CG    1 
ATOM   4827 O OD1   . ASN   B 1 185 ? 82.60366  0.77465   23.05295  1.000 87.65509  ? 185 ASN   B OD1   1 
ATOM   4828 N ND2   . ASN   B 1 185 ? 83.63370  2.75513   22.90836  1.000 79.48591  ? 185 ASN   B ND2   1 
ATOM   4829 N N     . GLU   B 1 186 ? 77.69857  1.73183   21.88625  1.000 88.10978  ? 186 GLU   B N     1 
ATOM   4830 C CA    . GLU   B 1 186 ? 76.55070  2.29907   21.18579  1.000 83.24051  ? 186 GLU   B CA    1 
ATOM   4831 C C     . GLU   B 1 186 ? 75.98966  3.50409   21.93171  1.000 79.75476  ? 186 GLU   B C     1 
ATOM   4832 O O     . GLU   B 1 186 ? 75.65630  4.51960   21.31715  1.000 73.50224  ? 186 GLU   B O     1 
ATOM   4833 C CB    . GLU   B 1 186 ? 75.47239  1.24038   20.98097  1.000 81.47471  ? 186 GLU   B CB    1 
ATOM   4834 C CG    . GLU   B 1 186 ? 75.98377  -0.03395  20.38656  1.000 87.71864  ? 186 GLU   B CG    1 
ATOM   4835 C CD    . GLU   B 1 186 ? 76.24276  -1.09920  21.44088  1.000 100.11799 ? 186 GLU   B CD    1 
ATOM   4836 O OE1   . GLU   B 1 186 ? 76.78299  -0.78820  22.53839  1.000 98.42169  ? 186 GLU   B OE1   1 
ATOM   4837 O OE2   . GLU   B 1 186 ? 75.92030  -2.27362  21.14727  1.000 103.39509 ? 186 GLU   B OE2   1 
ATOM   4838 N N     . ASP   B 1 187 ? 75.89459  3.42255   23.25760  1.000 81.53370  ? 187 ASP   B N     1 
ATOM   4839 C CA    . ASP   B 1 187 ? 75.44236  4.58000   24.01579  1.000 85.20076  ? 187 ASP   B CA    1 
ATOM   4840 C C     . ASP   B 1 187 ? 76.22022  5.84176   23.60347  1.000 91.00170  ? 187 ASP   B C     1 
ATOM   4841 O O     . ASP   B 1 187 ? 75.68266  6.96295   23.64891  1.000 87.32179  ? 187 ASP   B O     1 
ATOM   4842 C CB    . ASP   B 1 187 ? 75.58892  4.30739   25.52960  1.000 92.65088  ? 187 ASP   B CB    1 
ATOM   4843 C CG    . ASP   B 1 187 ? 74.54499  3.29246   26.08252  1.000 96.79190  ? 187 ASP   B CG    1 
ATOM   4844 O OD1   . ASP   B 1 187 ? 74.73313  2.05455   25.89574  1.000 92.09549  ? 187 ASP   B OD1   1 
ATOM   4845 O OD2   . ASP   B 1 187 ? 73.54620  3.72616   26.71093  1.000 93.49234  ? 187 ASP   B OD2   1 
ATOM   4846 N N     . LEU   B 1 188 ? 77.48125  5.68441   23.17876  1.000 88.81276  ? 188 LEU   B N     1 
ATOM   4847 C CA    . LEU   B 1 188 ? 78.26432  6.83368   22.71708  1.000 82.43222  ? 188 LEU   B CA    1 
ATOM   4848 C C     . LEU   B 1 188 ? 77.87669  7.21687   21.30012  1.000 78.57286  ? 188 LEU   B C     1 
ATOM   4849 O O     . LEU   B 1 188 ? 77.45859  8.34938   21.04482  1.000 76.60421  ? 188 LEU   B O     1 
ATOM   4850 C CB    . LEU   B 1 188 ? 79.76324  6.52303   22.80173  1.000 82.45965  ? 188 LEU   B CB    1 
ATOM   4851 C CG    . LEU   B 1 188 ? 80.71162  7.64978   22.39068  1.000 80.72421  ? 188 LEU   B CG    1 
ATOM   4852 C CD1   . LEU   B 1 188 ? 80.38958  8.94861   23.13363  1.000 70.30387  ? 188 LEU   B CD1   1 
ATOM   4853 C CD2   . LEU   B 1 188 ? 82.14621  7.18420   22.65985  1.000 77.79246  ? 188 LEU   B CD2   1 
ATOM   4854 N N     . PHE   B 1 189 ? 77.98562  6.26508   20.37272  1.000 78.37329  ? 189 PHE   B N     1 
ATOM   4855 C CA    . PHE   B 1 189 ? 77.62003  6.49579   18.98280  1.000 72.57601  ? 189 PHE   B CA    1 
ATOM   4856 C C     . PHE   B 1 189 ? 76.33307  7.30946   18.84634  1.000 76.24714  ? 189 PHE   B C     1 
ATOM   4857 O O     . PHE   B 1 189 ? 76.25444  8.23970   18.04047  1.000 79.49705  ? 189 PHE   B O     1 
ATOM   4858 C CB    . PHE   B 1 189 ? 77.46911  5.15429   18.28846  1.000 72.90290  ? 189 PHE   B CB    1 
ATOM   4859 C CG    . PHE   B 1 189 ? 77.43518  5.26587   16.83027  1.000 75.03538  ? 189 PHE   B CG    1 
ATOM   4860 C CD1   . PHE   B 1 189 ? 78.41457  5.96214   16.16224  1.000 76.47478  ? 189 PHE   B CD1   1 
ATOM   4861 C CD2   . PHE   B 1 189 ? 76.40180  4.71044   16.11382  1.000 79.30531  ? 189 PHE   B CD2   1 
ATOM   4862 C CE1   . PHE   B 1 189 ? 78.38378  6.07709   14.79880  1.000 77.91712  ? 189 PHE   B CE1   1 
ATOM   4863 C CE2   . PHE   B 1 189 ? 76.36763  4.82259   14.74870  1.000 81.36990  ? 189 PHE   B CE2   1 
ATOM   4864 C CZ    . PHE   B 1 189 ? 77.35727  5.50893   14.08924  1.000 77.99655  ? 189 PHE   B CZ    1 
ATOM   4865 N N     . PHE   B 1 190 ? 75.31554  6.96390   19.63536  1.000 80.81240  ? 190 PHE   B N     1 
ATOM   4866 C CA    . PHE   B 1 190 ? 74.08867  7.75969   19.70231  1.000 74.27171  ? 190 PHE   B CA    1 
ATOM   4867 C C     . PHE   B 1 190 ? 74.37746  9.25331   19.91820  1.000 74.16287  ? 190 PHE   B C     1 
ATOM   4868 O O     . PHE   B 1 190 ? 73.89669  10.09898  19.15619  1.000 73.31963  ? 190 PHE   B O     1 
ATOM   4869 C CB    . PHE   B 1 190 ? 73.18589  7.17011   20.79627  1.000 76.06798  ? 190 PHE   B CB    1 
ATOM   4870 C CG    . PHE   B 1 190 ? 71.96636  8.00340   21.14008  1.000 80.54714  ? 190 PHE   B CG    1 
ATOM   4871 C CD1   . PHE   B 1 190 ? 72.06120  9.10114   22.01850  1.000 75.79917  ? 190 PHE   B CD1   1 
ATOM   4872 C CD2   . PHE   B 1 190 ? 70.72388  7.68980   20.58930  1.000 77.48684  ? 190 PHE   B CD2   1 
ATOM   4873 C CE1   . PHE   B 1 190 ? 70.94807  9.86603   22.34518  1.000 70.64459  ? 190 PHE   B CE1   1 
ATOM   4874 C CE2   . PHE   B 1 190 ? 69.61685  8.45023   20.90874  1.000 76.60427  ? 190 PHE   B CE2   1 
ATOM   4875 C CZ    . PHE   B 1 190 ? 69.73548  9.54454   21.79016  1.000 75.91018  ? 190 PHE   B CZ    1 
ATOM   4876 N N     . ALA   B 1 191 ? 75.17145  9.60077   20.94592  1.000 73.63463  ? 191 ALA   B N     1 
ATOM   4877 C CA    . ALA   B 1 191 ? 75.38804  11.01782  21.28167  1.000 75.02501  ? 191 ALA   B CA    1 
ATOM   4878 C C     . ALA   B 1 191 ? 76.29364  11.73682  20.27383  1.000 74.44432  ? 191 ALA   B C     1 
ATOM   4879 O O     . ALA   B 1 191 ? 76.19123  12.96490  20.09015  1.000 66.48176  ? 191 ALA   B O     1 
ATOM   4880 C CB    . ALA   B 1 191 ? 75.98912  11.13172  22.68486  1.000 70.86226  ? 191 ALA   B CB    1 
ATOM   4881 N N     . VAL   B 1 192 ? 77.20795  10.98772  19.65024  1.000 76.96097  ? 192 VAL   B N     1 
ATOM   4882 C CA    . VAL   B 1 192 ? 78.08878  11.52554  18.61884  1.000 72.33982  ? 192 VAL   B CA    1 
ATOM   4883 C C     . VAL   B 1 192 ? 77.26907  12.02230  17.43729  1.000 72.88026  ? 192 VAL   B C     1 
ATOM   4884 O O     . VAL   B 1 192 ? 77.56419  13.07639  16.85294  1.000 74.92838  ? 192 VAL   B O     1 
ATOM   4885 C CB    . VAL   B 1 192 ? 79.09870  10.43884  18.19902  1.000 71.62791  ? 192 VAL   B CB    1 
ATOM   4886 C CG1   . VAL   B 1 192 ? 79.58291  10.66345  16.78971  1.000 70.40859  ? 192 VAL   B CG1   1 
ATOM   4887 C CG2   . VAL   B 1 192 ? 80.25878  10.37662  19.18645  1.000 70.19517  ? 192 VAL   B CG2   1 
ATOM   4888 N N     . ARG   B 1 193 ? 76.22275  11.27201  17.08086  1.000 70.38488  ? 193 ARG   B N     1 
ATOM   4889 C CA    . ARG   B 1 193 ? 75.29717  11.54753  15.98548  1.000 62.71087  ? 193 ARG   B CA    1 
ATOM   4890 C C     . ARG   B 1 193 ? 74.14382  12.46672  16.40938  1.000 64.22750  ? 193 ARG   B C     1 
ATOM   4891 O O     . ARG   B 1 193 ? 72.97534  12.17984  16.16944  1.000 68.28690  ? 193 ARG   B O     1 
ATOM   4892 C CB    . ARG   B 1 193 ? 74.77987  10.21839  15.46304  1.000 54.27602  ? 193 ARG   B CB    1 
ATOM   4893 C CG    . ARG   B 1 193 ? 75.87775  9.31683   15.03661  1.000 59.48297  ? 193 ARG   B CG    1 
ATOM   4894 C CD    . ARG   B 1 193 ? 75.43419  8.29013   13.98799  1.000 71.93718  ? 193 ARG   B CD    1 
ATOM   4895 N NE    . ARG   B 1 193 ? 74.38276  7.41007   14.48608  1.000 79.80622  ? 193 ARG   B NE    1 
ATOM   4896 C CZ    . ARG   B 1 193 ? 73.87526  6.37745   13.82342  1.000 79.30748  ? 193 ARG   B CZ    1 
ATOM   4897 N NH1   . ARG   B 1 193 ? 74.32305  6.03285   12.62469  1.000 76.09679  ? 193 ARG   B NH1   1 
ATOM   4898 N NH2   . ARG   B 1 193 ? 72.92767  5.64376   14.39931  1.000 80.75381  ? 193 ARG   B NH2   1 
ATOM   4899 N N     . GLY   B 1 194 ? 74.45719  13.58870  17.04492  1.000 57.43004  ? 194 GLY   B N     1 
ATOM   4900 C CA    . GLY   B 1 194 ? 73.41469  14.48778  17.46512  1.000 56.19511  ? 194 GLY   B CA    1 
ATOM   4901 C C     . GLY   B 1 194 ? 73.97479  15.58307  18.32577  1.000 66.96160  ? 194 GLY   B C     1 
ATOM   4902 O O     . GLY   B 1 194 ? 73.61654  16.74830  18.17844  1.000 72.26498  ? 194 GLY   B O     1 
ATOM   4903 N N     . ALA   B 1 195 ? 74.87448  15.23690  19.23482  1.000 71.90850  ? 195 ALA   B N     1 
ATOM   4904 C CA    . ALA   B 1 195 ? 75.44070  16.23511  20.12844  1.000 75.98197  ? 195 ALA   B CA    1 
ATOM   4905 C C     . ALA   B 1 195 ? 76.84710  15.79275  20.52959  1.000 74.68627  ? 195 ALA   B C     1 
ATOM   4906 O O     . ALA   B 1 195 ? 77.22748  15.79851  21.70583  1.000 75.62314  ? 195 ALA   B O     1 
ATOM   4907 C CB    . ALA   B 1 195 ? 74.53883  16.46688  21.33891  1.000 72.41177  ? 195 ALA   B CB    1 
ATOM   4908 N N     . ALA   B 1 196 ? 77.62969  15.40032  19.53165  1.000 69.57792  ? 196 ALA   B N     1 
ATOM   4909 C CA    . ALA   B 1 196 ? 79.05904  15.25128  19.72605  1.000 68.16600  ? 196 ALA   B CA    1 
ATOM   4910 C C     . ALA   B 1 196 ? 79.61197  16.44897  20.50097  1.000 63.67212  ? 196 ALA   B C     1 
ATOM   4911 O O     . ALA   B 1 196 ? 80.42887  16.28608  21.40974  1.000 59.33190  ? 196 ALA   B O     1 
ATOM   4912 C CB    . ALA   B 1 196 ? 79.75089  15.09130  18.37002  1.000 70.12786  ? 196 ALA   B CB    1 
ATOM   4913 N N     . SER   B 1 197 ? 79.13832  17.65243  20.19783  1.000 64.91042  ? 197 SER   B N     1 
ATOM   4914 C CA    . SER   B 1 197 ? 79.67802  18.85681  20.82832  1.000 69.00926  ? 197 SER   B CA    1 
ATOM   4915 C C     . SER   B 1 197 ? 79.83261  18.66432  22.32899  1.000 68.27500  ? 197 SER   B C     1 
ATOM   4916 O O     . SER   B 1 197 ? 80.65760  19.32621  22.97777  1.000 60.08543  ? 197 SER   B O     1 
ATOM   4917 C CB    . SER   B 1 197 ? 78.78945  20.08075  20.54704  1.000 71.55556  ? 197 SER   B CB    1 
ATOM   4918 O OG    . SER   B 1 197 ? 77.41955  19.76230  20.64161  1.000 75.97471  ? 197 SER   B OG    1 
ATOM   4919 N N     . SER   B 1 198 ? 79.04540  17.73689  22.87283  1.000 74.58880  ? 198 SER   B N     1 
ATOM   4920 C CA    . SER   B 1 198 ? 78.86411  17.62167  24.30948  1.000 75.74090  ? 198 SER   B CA    1 
ATOM   4921 C C     . SER   B 1 198 ? 79.63593  16.47197  24.93083  1.000 74.19494  ? 198 SER   B C     1 
ATOM   4922 O O     . SER   B 1 198 ? 79.98643  16.56543  26.11252  1.000 75.65709  ? 198 SER   B O     1 
ATOM   4923 C CB    . SER   B 1 198 ? 77.37287  17.49092  24.65157  1.000 70.49479  ? 198 SER   B CB    1 
ATOM   4924 O OG    . SER   B 1 198 ? 76.75983  18.76819  24.76369  1.000 64.35767  ? 198 SER   B OG    1 
ATOM   4925 N N     . VAL   B 1 199 ? 79.97436  15.42853  24.16985  1.000 70.70379  ? 199 VAL   B N     1 
ATOM   4926 C CA    . VAL   B 1 199 ? 80.46360  14.19027  24.77207  1.000 68.40104  ? 199 VAL   B CA    1 
ATOM   4927 C C     . VAL   B 1 199 ? 81.88383  13.77588  24.36154  1.000 67.49413  ? 199 VAL   B C     1 
ATOM   4928 O O     . VAL   B 1 199 ? 82.48271  12.93262  25.04505  1.000 67.51399  ? 199 VAL   B O     1 
ATOM   4929 C CB    . VAL   B 1 199 ? 79.47386  13.05245  24.49581  1.000 69.20334  ? 199 VAL   B CB    1 
ATOM   4930 C CG1   . VAL   B 1 199 ? 78.15880  13.46219  25.06372  1.000 71.53495  ? 199 VAL   B CG1   1 
ATOM   4931 C CG2   . VAL   B 1 199 ? 79.33958  12.82013  23.00496  1.000 68.43119  ? 199 VAL   B CG2   1 
ATOM   4932 N N     . GLY   B 1 200 ? 82.46520  14.31917  23.30042  1.000 76.30826  ? 200 GLY   B N     1 
ATOM   4933 C CA    . GLY   B 1 200 ? 83.82838  13.95884  22.93255  1.000 71.75359  ? 200 GLY   B CA    1 
ATOM   4934 C C     . GLY   B 1 200 ? 84.29188  14.73515  21.71219  1.000 73.95807  ? 200 GLY   B C     1 
ATOM   4935 O O     . GLY   B 1 200 ? 83.52690  15.49156  21.10345  1.000 83.47866  ? 200 GLY   B O     1 
ATOM   4936 N N     . ILE   B 1 201 ? 85.56864  14.54733  21.35959  1.000 69.81115  ? 201 ILE   B N     1 
ATOM   4937 C CA    . ILE   B 1 201 ? 86.12386  15.05305  20.10376  1.000 62.88073  ? 201 ILE   B CA    1 
ATOM   4938 C C     . ILE   B 1 201 ? 86.26617  13.89476  19.12879  1.000 59.82696  ? 201 ILE   B C     1 
ATOM   4939 O O     . ILE   B 1 201 ? 86.99546  12.93164  19.39647  1.000 59.82825  ? 201 ILE   B O     1 
ATOM   4940 C CB    . ILE   B 1 201 ? 87.47757  15.73039  20.30999  1.000 54.96726  ? 201 ILE   B CB    1 
ATOM   4941 C CG1   . ILE   B 1 201 ? 87.28772  16.94297  21.19702  1.000 60.29071  ? 201 ILE   B CG1   1 
ATOM   4942 C CG2   . ILE   B 1 201 ? 88.06808  16.06355  18.96876  1.000 53.59607  ? 201 ILE   B CG2   1 
ATOM   4943 C CD1   . ILE   B 1 201 ? 88.56349  17.66173  21.55861  1.000 65.05710  ? 201 ILE   B CD1   1 
ATOM   4944 N N     . VAL   B 1 202 ? 85.59688  13.98594  17.99362  1.000 54.66322  ? 202 VAL   B N     1 
ATOM   4945 C CA    . VAL   B 1 202 ? 85.73375  12.97546  16.96177  1.000 56.00527  ? 202 VAL   B CA    1 
ATOM   4946 C C     . VAL   B 1 202 ? 86.93348  13.34195  16.11128  1.000 59.20930  ? 202 VAL   B C     1 
ATOM   4947 O O     . VAL   B 1 202 ? 87.08053  14.49489  15.69051  1.000 59.81345  ? 202 VAL   B O     1 
ATOM   4948 C CB    . VAL   B 1 202 ? 84.47044  12.88175  16.10517  1.000 52.49604  ? 202 VAL   B CB    1 
ATOM   4949 C CG1   . VAL   B 1 202 ? 84.49710  11.60275  15.34476  1.000 55.12701  ? 202 VAL   B CG1   1 
ATOM   4950 C CG2   . VAL   B 1 202 ? 83.24115  13.03063  16.96379  1.000 51.96355  ? 202 VAL   B CG2   1 
ATOM   4951 N N     . THR   B 1 203 ? 87.79121  12.36223  15.85046  1.000 58.92436  ? 203 THR   B N     1 
ATOM   4952 C CA    . THR   B 1 203 ? 89.04326  12.59937  15.14354  1.000 57.62040  ? 203 THR   B CA    1 
ATOM   4953 C C     . THR   B 1 203 ? 89.14078  11.77596  13.85538  1.000 64.40966  ? 203 THR   B C     1 
ATOM   4954 O O     . THR   B 1 203 ? 90.18239  11.80479  13.18643  1.000 64.52107  ? 203 THR   B O     1 
ATOM   4955 C CB    . THR   B 1 203 ? 90.21326  12.31573  16.08907  1.000 55.94872  ? 203 THR   B CB    1 
ATOM   4956 O OG1   . THR   B 1 203 ? 90.21237  10.92741  16.42419  1.000 58.86851  ? 203 THR   B OG1   1 
ATOM   4957 C CG2   . THR   B 1 203 ? 90.07865  13.12174  17.39454  1.000 47.35619  ? 203 THR   B CG2   1 
ATOM   4958 N N     . ASP   B 1 204 ? 88.06566  11.06753  13.48331  1.000 66.15608  ? 204 ASP   B N     1 
ATOM   4959 C CA    . ASP   B 1 204 ? 87.98501  10.22920  12.29406  1.000 63.47505  ? 204 ASP   B CA    1 
ATOM   4960 C C     . ASP   B 1 204 ? 86.53717  9.82220   12.07942  1.000 70.19413  ? 204 ASP   B C     1 
ATOM   4961 O O     . ASP   B 1 204 ? 85.85468  9.43295   13.03421  1.000 70.81435  ? 204 ASP   B O     1 
ATOM   4962 C CB    . ASP   B 1 204 ? 88.85150  8.98016   12.44228  1.000 71.50657  ? 204 ASP   B CB    1 
ATOM   4963 C CG    . ASP   B 1 204 ? 88.93182  8.14823   11.15717  1.000 87.94181  ? 204 ASP   B CG    1 
ATOM   4964 O OD1   . ASP   B 1 204 ? 89.65003  8.57985   10.21133  1.000 86.76174  ? 204 ASP   B OD1   1 
ATOM   4965 O OD2   . ASP   B 1 204 ? 88.31208  7.04618   11.11142  1.000 89.86388  ? 204 ASP   B OD2   1 
ATOM   4966 N N     . PHE   B 1 205 ? 86.07958  9.88993   10.82836  1.000 72.21412  ? 205 PHE   B N     1 
ATOM   4967 C CA    . PHE   B 1 205 ? 84.75203  9.43617   10.43137  1.000 69.07895  ? 205 PHE   B CA    1 
ATOM   4968 C C     . PHE   B 1 205 ? 84.87603  8.28296   9.44143   1.000 71.29339  ? 205 PHE   B C     1 
ATOM   4969 O O     . PHE   B 1 205 ? 85.85330  8.19893   8.69907   1.000 75.13747  ? 205 PHE   B O     1 
ATOM   4970 C CB    . PHE   B 1 205 ? 83.96992  10.56218  9.76560   1.000 64.53693  ? 205 PHE   B CB    1 
ATOM   4971 C CG    . PHE   B 1 205 ? 83.47612  11.61383  10.71029  1.000 63.61049  ? 205 PHE   B CG    1 
ATOM   4972 C CD1   . PHE   B 1 205 ? 84.25628  12.73448  10.99371  1.000 65.50104  ? 205 PHE   B CD1   1 
ATOM   4973 C CD2   . PHE   B 1 205 ? 82.23089  11.50293  11.31149  1.000 58.78195  ? 205 PHE   B CD2   1 
ATOM   4974 C CE1   . PHE   B 1 205 ? 83.79304  13.74059  11.87053  1.000 63.65096  ? 205 PHE   B CE1   1 
ATOM   4975 C CE2   . PHE   B 1 205 ? 81.76905  12.49501  12.18834  1.000 62.47352  ? 205 PHE   B CE2   1 
ATOM   4976 C CZ    . PHE   B 1 205 ? 82.55446  13.61661  12.46846  1.000 59.34492  ? 205 PHE   B CZ    1 
ATOM   4977 N N     . SER   B 1 206 ? 83.87464  7.40756   9.40371   1.000 71.05263  ? 206 SER   B N     1 
ATOM   4978 C CA    . SER   B 1 206 ? 83.78618  6.35284   8.38702   1.000 72.76182  ? 206 SER   B CA    1 
ATOM   4979 C C     . SER   B 1 206 ? 82.42775  6.52915   7.75015   1.000 74.64987  ? 206 SER   B C     1 
ATOM   4980 O O     . SER   B 1 206 ? 81.43543  6.00714   8.25546   1.000 84.86621  ? 206 SER   B O     1 
ATOM   4981 C CB    . SER   B 1 206 ? 83.91452  4.93337   8.96096   1.000 74.32211  ? 206 SER   B CB    1 
ATOM   4982 O OG    . SER   B 1 206 ? 85.22580  4.63044   9.39330   1.000 80.61881  ? 206 SER   B OG    1 
ATOM   4983 N N     . ILE   B 1 207 ? 82.35782  7.24991   6.65271   1.000 74.88033  ? 207 ILE   B N     1 
ATOM   4984 C CA    . ILE   B 1 207 ? 81.07090  7.51550   6.03357   1.000 79.38024  ? 207 ILE   B CA    1 
ATOM   4985 C C     . ILE   B 1 207 ? 80.90732  6.64100   4.79624   1.000 82.25112  ? 207 ILE   B C     1 
ATOM   4986 O O     . ILE   B 1 207 ? 81.80387  6.58129   3.94469   1.000 84.95811  ? 207 ILE   B O     1 
ATOM   4987 C CB    . ILE   B 1 207 ? 80.93341  9.00095   5.68998   1.000 73.96102  ? 207 ILE   B CB    1 
ATOM   4988 C CG1   . ILE   B 1 207 ? 81.42618  9.83393   6.85434   1.000 70.84207  ? 207 ILE   B CG1   1 
ATOM   4989 C CG2   . ILE   B 1 207 ? 79.49696  9.33042   5.49621   1.000 73.64368  ? 207 ILE   B CG2   1 
ATOM   4990 C CD1   . ILE   B 1 207 ? 81.10947  11.29326  6.70094   1.000 65.88001  ? 207 ILE   B CD1   1 
ATOM   4991 N N     . ARG   B 1 208 ? 79.77337  5.94727   4.70517   1.000 83.03891  ? 208 ARG   B N     1 
ATOM   4992 C CA    . ARG   B 1 208 ? 79.38442  5.30771   3.45401   1.000 83.94176  ? 208 ARG   B CA    1 
ATOM   4993 C C     . ARG   B 1 208 ? 78.98359  6.35828   2.43871   1.000 80.72453  ? 208 ARG   B C     1 
ATOM   4994 O O     . ARG   B 1 208 ? 78.56890  7.46781   2.79069   1.000 78.21093  ? 208 ARG   B O     1 
ATOM   4995 C CB    . ARG   B 1 208 ? 78.20184  4.37807   3.66840   1.000 84.93287  ? 208 ARG   B CB    1 
ATOM   4996 C CG    . ARG   B 1 208 ? 78.53953  3.00059   4.11279   1.000 84.98497  ? 208 ARG   B CG    1 
ATOM   4997 C CD    . ARG   B 1 208 ? 77.24753  2.24255   4.34659   1.000 82.19938  ? 208 ARG   B CD    1 
ATOM   4998 N NE    . ARG   B 1 208 ? 76.41646  2.96296   5.30731   1.000 82.75524  ? 208 ARG   B NE    1 
ATOM   4999 C CZ    . ARG   B 1 208 ? 75.27805  3.57761   5.00549   1.000 79.89640  ? 208 ARG   B CZ    1 
ATOM   5000 N NH1   . ARG   B 1 208 ? 74.72780  3.46749   3.80261   1.000 78.21011  ? 208 ARG   B NH1   1 
ATOM   5001 N NH2   . ARG   B 1 208 ? 74.66698  4.30955   5.93643   1.000 70.41969  ? 208 ARG   B NH2   1 
ATOM   5002 N N     . THR   B 1 209 ? 79.06163  5.99266   1.16616   1.000 83.29958  ? 209 THR   B N     1 
ATOM   5003 C CA    . THR   B 1 209 ? 78.65280  6.91359   0.11757   1.000 85.50358  ? 209 THR   B CA    1 
ATOM   5004 C C     . THR   B 1 209 ? 77.67638  6.24458   -0.83766  1.000 82.05493  ? 209 THR   B C     1 
ATOM   5005 O O     . THR   B 1 209 ? 77.69035  5.02484   -1.03599  1.000 79.15909  ? 209 THR   B O     1 
ATOM   5006 C CB    . THR   B 1 209 ? 79.86771  7.48628   -0.67486  1.000 89.01913  ? 209 THR   B CB    1 
ATOM   5007 O OG1   . THR   B 1 209 ? 80.66930  6.42630   -1.21364  1.000 87.63892  ? 209 THR   B OG1   1 
ATOM   5008 C CG2   . THR   B 1 209 ? 80.73231  8.35194   0.23631   1.000 83.00866  ? 209 THR   B CG2   1 
ATOM   5009 N N     . GLU   B 1 210 ? 76.80197  7.04978   -1.37238  1.000 83.25643  ? 210 GLU   B N     1 
ATOM   5010 C CA    . GLU   B 1 210 ? 76.01883  6.68672   -2.53780  1.000 89.45804  ? 210 GLU   B CA    1 
ATOM   5011 C C     . GLU   B 1 210 ? 76.79280  7.03321   -3.79612  1.000 86.44572  ? 210 GLU   B C     1 
ATOM   5012 O O     . GLU   B 1 210 ? 77.75654  7.80344   -3.75890  1.000 83.67444  ? 210 GLU   B O     1 
ATOM   5013 C CB    . GLU   B 1 210 ? 74.68362  7.42829   -2.53132  1.000 88.60560  ? 210 GLU   B CB    1 
ATOM   5014 C CG    . GLU   B 1 210 ? 73.79792  7.14689   -1.33676  1.000 88.35866  ? 210 GLU   B CG    1 
ATOM   5015 C CD    . GLU   B 1 210 ? 73.07614  5.81471   -1.44914  1.000 98.26384  ? 210 GLU   B CD    1 
ATOM   5016 O OE1   . GLU   B 1 210 ? 73.14146  5.18195   -2.52973  1.000 100.87000 ? 210 GLU   B OE1   1 
ATOM   5017 O OE2   . GLU   B 1 210 ? 72.43080  5.40356   -0.45975  1.000 98.75116  ? 210 GLU   B OE2   1 
ATOM   5018 N N     . PRO   B 1 211 ? 76.40281  6.47898   -4.92806  1.000 84.15858  ? 211 PRO   B N     1 
ATOM   5019 C CA    . PRO   B 1 211 ? 76.88753  7.00630   -6.19829  1.000 83.63431  ? 211 PRO   B CA    1 
ATOM   5020 C C     . PRO   B 1 211 ? 76.11328  8.26661   -6.54746  1.000 84.68321  ? 211 PRO   B C     1 
ATOM   5021 O O     . PRO   B 1 211 ? 75.02074  8.52215   -6.03305  1.000 79.38566  ? 211 PRO   B O     1 
ATOM   5022 C CB    . PRO   B 1 211 ? 76.59079  5.87688   -7.18113  1.000 80.45061  ? 211 PRO   B CB    1 
ATOM   5023 C CG    . PRO   B 1 211 ? 75.36345  5.27171   -6.61709  1.000 83.88843  ? 211 PRO   B CG    1 
ATOM   5024 C CD    . PRO   B 1 211 ? 75.45179  5.37593   -5.11613  1.000 80.01390  ? 211 PRO   B CD    1 
ATOM   5025 N N     . VAL   B 1 212 ? 76.71320  9.06388   -7.42548  1.000 89.33463  ? 212 VAL   B N     1 
ATOM   5026 C CA    . VAL   B 1 212 ? 76.22414  10.40501  -7.74659  1.000 89.14626  ? 212 VAL   B CA    1 
ATOM   5027 C C     . VAL   B 1 212 ? 75.03056  10.30174  -8.68966  1.000 88.80099  ? 212 VAL   B C     1 
ATOM   5028 O O     . VAL   B 1 212 ? 74.99036  9.37592   -9.51396  1.000 87.35212  ? 212 VAL   B O     1 
ATOM   5029 C CB    . VAL   B 1 212 ? 77.34657  11.25396  -8.36029  1.000 84.72866  ? 212 VAL   B CB    1 
ATOM   5030 C CG1   . VAL   B 1 212 ? 78.39999  11.59007  -7.32401  1.000 81.92080  ? 212 VAL   B CG1   1 
ATOM   5031 C CG2   . VAL   B 1 212 ? 78.00454  10.47047  -9.45574  1.000 88.47866  ? 212 VAL   B CG2   1 
ATOM   5032 N N     . PRO   B 1 213 ? 74.04647  11.20916  -8.61391  1.000 92.72547  ? 213 PRO   B N     1 
ATOM   5033 C CA    . PRO   B 1 213 ? 72.90217  11.13363  -9.52769  1.000 91.84066  ? 213 PRO   B CA    1 
ATOM   5034 C C     . PRO   B 1 213 ? 73.29121  11.64233  -10.89887 1.000 93.60126  ? 213 PRO   B C     1 
ATOM   5035 O O     . PRO   B 1 213 ? 73.98652  12.65570  -11.03691 1.000 92.34376  ? 213 PRO   B O     1 
ATOM   5036 C CB    . PRO   B 1 213 ? 71.85939  12.05515  -8.88092  1.000 91.58237  ? 213 PRO   B CB    1 
ATOM   5037 C CG    . PRO   B 1 213 ? 72.64647  13.06109  -8.16482  1.000 86.94988  ? 213 PRO   B CG    1 
ATOM   5038 C CD    . PRO   B 1 213 ? 73.99766  12.43759  -7.80254  1.000 93.20152  ? 213 PRO   B CD    1 
ATOM   5039 N N     . VAL   B 1 214 ? 72.81119  10.93068  -11.92095 1.000 96.36233  ? 214 VAL   B N     1 
ATOM   5040 C CA    . VAL   B 1 214 ? 73.23265  11.21119  -13.28684 1.000 93.78368  ? 214 VAL   B CA    1 
ATOM   5041 C C     . VAL   B 1 214 ? 72.67940  12.52044  -13.80411 1.000 89.85508  ? 214 VAL   B C     1 
ATOM   5042 O O     . VAL   B 1 214 ? 73.22404  13.07607  -14.76488 1.000 83.79615  ? 214 VAL   B O     1 
ATOM   5043 C CB    . VAL   B 1 214 ? 72.80253  10.07743  -14.22106 1.000 96.56913  ? 214 VAL   B CB    1 
ATOM   5044 C CG1   . VAL   B 1 214 ? 73.50442  10.22467  -15.57351 1.000 100.91214 ? 214 VAL   B CG1   1 
ATOM   5045 C CG2   . VAL   B 1 214 ? 73.08793  8.73941   -13.55465 1.000 100.13360 ? 214 VAL   B CG2   1 
ATOM   5046 N N     . SER   B 1 215 ? 71.60922  13.02412  -13.19647 1.000 88.43306  ? 215 SER   B N     1 
ATOM   5047 C CA    . SER   B 1 215 ? 71.02958  14.28671  -13.62236 1.000 88.85701  ? 215 SER   B CA    1 
ATOM   5048 C C     . SER   B 1 215 ? 70.48134  15.02114  -12.41311 1.000 92.08202  ? 215 SER   B C     1 
ATOM   5049 O O     . SER   B 1 215 ? 69.64094  14.49461  -11.67638 1.000 95.53418  ? 215 SER   B O     1 
ATOM   5050 C CB    . SER   B 1 215 ? 69.93489  14.05933  -14.65706 1.000 95.43116  ? 215 SER   B CB    1 
ATOM   5051 O OG    . SER   B 1 215 ? 69.36893  15.29271  -15.05789 1.000 101.51092 ? 215 SER   B OG    1 
ATOM   5052 N N     . SER   B 1 216 ? 70.95310  16.23944  -12.22673 1.000 85.42767  ? 216 SER   B N     1 
ATOM   5053 C CA    . SER   B 1 216 ? 70.46145  17.12267  -11.19263 1.000 85.63635  ? 216 SER   B CA    1 
ATOM   5054 C C     . SER   B 1 216 ? 69.85149  18.33224  -11.88057 1.000 85.75198  ? 216 SER   B C     1 
ATOM   5055 O O     . SER   B 1 216 ? 70.36450  18.79188  -12.90158 1.000 90.22111  ? 216 SER   B O     1 
ATOM   5056 C CB    . SER   B 1 216 ? 71.60116  17.54401  -10.26453 1.000 86.27305  ? 216 SER   B CB    1 
ATOM   5057 O OG    . SER   B 1 216 ? 72.27889  16.41133  -9.75792  1.000 90.04654  ? 216 SER   B OG    1 
ATOM   5058 N N     . VAL   B 1 217 ? 68.76840  18.85903  -11.32081 1.000 83.08257  ? 217 VAL   B N     1 
ATOM   5059 C CA    . VAL   B 1 217 ? 68.00798  19.89584  -12.00865 1.000 84.72585  ? 217 VAL   B CA    1 
ATOM   5060 C C     . VAL   B 1 217 ? 67.69866  21.06528  -11.08948 1.000 86.07591  ? 217 VAL   B C     1 
ATOM   5061 O O     . VAL   B 1 217 ? 66.55573  21.22577  -10.64335 1.000 92.05774  ? 217 VAL   B O     1 
ATOM   5062 C CB    . VAL   B 1 217 ? 66.70099  19.32374  -12.59271 1.000 86.38135  ? 217 VAL   B CB    1 
ATOM   5063 C CG1   . VAL   B 1 217 ? 66.00050  20.38044  -13.43814 1.000 86.99642  ? 217 VAL   B CG1   1 
ATOM   5064 C CG2   . VAL   B 1 217 ? 66.98280  18.05200  -13.38803 1.000 90.15458  ? 217 VAL   B CG2   1 
ATOM   5065 N N     . THR   B 1 218 ? 68.68837  21.90885  -10.82039 1.000 80.24844  ? 218 THR   B N     1 
ATOM   5066 C CA    . THR   B 1 218 ? 68.40543  23.10336  -10.03477 1.000 83.10541  ? 218 THR   B CA    1 
ATOM   5067 C C     . THR   B 1 218 ? 67.27618  23.91104  -10.66564 1.000 80.65552  ? 218 THR   B C     1 
ATOM   5068 O O     . THR   B 1 218 ? 67.00744  23.82215  -11.86827 1.000 81.17302  ? 218 THR   B O     1 
ATOM   5069 C CB    . THR   B 1 218 ? 69.64922  23.96868  -9.90988  1.000 81.79586  ? 218 THR   B CB    1 
ATOM   5070 O OG1   . THR   B 1 218 ? 70.18754  24.16771  -11.21626 1.000 89.71590  ? 218 THR   B OG1   1 
ATOM   5071 C CG2   . THR   B 1 218 ? 70.68728  23.30962  -9.02841  1.000 79.15658  ? 218 THR   B CG2   1 
ATOM   5072 N N     . TYR   B 1 219 ? 66.60044  24.69998  -9.83581  1.000 77.73894  ? 219 TYR   B N     1 
ATOM   5073 C CA    . TYR   B 1 219 ? 65.46143  25.47055  -10.30990 1.000 81.33977  ? 219 TYR   B CA    1 
ATOM   5074 C C     . TYR   B 1 219 ? 65.19981  26.61733  -9.34927  1.000 79.93514  ? 219 TYR   B C     1 
ATOM   5075 O O     . TYR   B 1 219 ? 65.69505  26.63424  -8.22416  1.000 84.38121  ? 219 TYR   B O     1 
ATOM   5076 C CB    . TYR   B 1 219 ? 64.22165  24.58550  -10.46432 1.000 84.85127  ? 219 TYR   B CB    1 
ATOM   5077 C CG    . TYR   B 1 219 ? 63.58763  24.11590  -9.17502  1.000 87.80039  ? 219 TYR   B CG    1 
ATOM   5078 C CD1   . TYR   B 1 219 ? 62.85532  24.99278  -8.36312  1.000 92.00996  ? 219 TYR   B CD1   1 
ATOM   5079 C CD2   . TYR   B 1 219 ? 63.70273  22.79912  -8.76989  1.000 87.82411  ? 219 TYR   B CD2   1 
ATOM   5080 C CE1   . TYR   B 1 219 ? 62.26537  24.56475  -7.18747  1.000 90.75427  ? 219 TYR   B CE1   1 
ATOM   5081 C CE2   . TYR   B 1 219 ? 63.11009  22.36093  -7.59209  1.000 93.42887  ? 219 TYR   B CE2   1 
ATOM   5082 C CZ    . TYR   B 1 219 ? 62.39652  23.24805  -6.80900  1.000 92.80035  ? 219 TYR   B CZ    1 
ATOM   5083 O OH    . TYR   B 1 219 ? 61.81471  22.82220  -5.64051  1.000 98.26229  ? 219 TYR   B OH    1 
ATOM   5084 N N     . SER   B 1 220 ? 64.37884  27.56479  -9.79741  1.000 81.63259  ? 220 SER   B N     1 
ATOM   5085 C CA    . SER   B 1 220 ? 64.04943  28.72403  -8.97666  1.000 85.95912  ? 220 SER   B CA    1 
ATOM   5086 C C     . SER   B 1 220 ? 62.88689  29.49073  -9.58582  1.000 86.99057  ? 220 SER   B C     1 
ATOM   5087 O O     . SER   B 1 220 ? 62.76323  29.57291  -10.81450 1.000 92.14775  ? 220 SER   B O     1 
ATOM   5088 C CB    . SER   B 1 220 ? 65.25793  29.65305  -8.81117  1.000 88.84932  ? 220 SER   B CB    1 
ATOM   5089 O OG    . SER   B 1 220 ? 64.84317  30.95355  -8.42541  1.000 85.13748  ? 220 SER   B OG    1 
ATOM   5090 N N     . TYR   B 1 221 ? 62.06102  30.06284  -8.71190  1.000 82.75662  ? 221 TYR   B N     1 
ATOM   5091 C CA    . TYR   B 1 221 ? 60.86552  30.82738  -9.04206  1.000 86.36340  ? 221 TYR   B CA    1 
ATOM   5092 C C     . TYR   B 1 221 ? 60.83521  32.00687  -8.09000  1.000 90.10070  ? 221 TYR   B C     1 
ATOM   5093 O O     . TYR   B 1 221 ? 60.97765  31.82189  -6.87422  1.000 94.14879  ? 221 TYR   B O     1 
ATOM   5094 C CB    . TYR   B 1 221 ? 59.59723  29.96717  -8.87487  1.000 88.07683  ? 221 TYR   B CB    1 
ATOM   5095 C CG    . TYR   B 1 221 ? 59.53175  28.80288  -9.83316  1.000 85.94674  ? 221 TYR   B CG    1 
ATOM   5096 C CD1   . TYR   B 1 221 ? 58.94636  28.92804  -11.09882 1.000 90.67442  ? 221 TYR   B CD1   1 
ATOM   5097 C CD2   . TYR   B 1 221 ? 60.16675  27.59843  -9.50196  1.000 91.27903  ? 221 TYR   B CD2   1 
ATOM   5098 C CE1   . TYR   B 1 221 ? 58.92655  27.83869  -11.98181 1.000 103.85285 ? 221 TYR   B CE1   1 
ATOM   5099 C CE2   . TYR   B 1 221 ? 60.17287  26.51561  -10.36169 1.000 98.83372  ? 221 TYR   B CE2   1 
ATOM   5100 C CZ    . TYR   B 1 221 ? 59.55785  26.62765  -11.60332 1.000 103.86138 ? 221 TYR   B CZ    1 
ATOM   5101 O OH    . TYR   B 1 221 ? 59.58850  25.50598  -12.42142 1.000 100.65746 ? 221 TYR   B OH    1 
ATOM   5102 N N     . ILE   B 1 222 ? 60.65369  33.21581  -8.61193  1.000 89.24405  ? 222 ILE   B N     1 
ATOM   5103 C CA    . ILE   B 1 222 ? 60.83283  34.40826  -7.79536  1.000 88.82862  ? 222 ILE   B CA    1 
ATOM   5104 C C     . ILE   B 1 222 ? 59.58907  35.27446  -7.88266  1.000 91.16694  ? 222 ILE   B C     1 
ATOM   5105 O O     . ILE   B 1 222 ? 59.01357  35.44839  -8.95818  1.000 92.40651  ? 222 ILE   B O     1 
ATOM   5106 C CB    . ILE   B 1 222 ? 62.06755  35.19797  -8.23006  1.000 82.97895  ? 222 ILE   B CB    1 
ATOM   5107 C CG1   . ILE   B 1 222 ? 63.29852  34.32613  -8.00031  1.000 86.45011  ? 222 ILE   B CG1   1 
ATOM   5108 C CG2   . ILE   B 1 222 ? 62.14341  36.45280  -7.39285  1.000 88.82918  ? 222 ILE   B CG2   1 
ATOM   5109 C CD1   . ILE   B 1 222 ? 64.57120  34.82897  -8.62659  1.000 92.38057  ? 222 ILE   B CD1   1 
ATOM   5110 N N     . TRP   B 1 223 ? 59.18003  35.82334  -6.74753  1.000 92.11740  ? 223 TRP   B N     1 
ATOM   5111 C CA    . TRP   B 1 223 ? 57.99283  36.66109  -6.65239  1.000 94.02503  ? 223 TRP   B CA    1 
ATOM   5112 C C     . TRP   B 1 223 ? 58.42767  38.00493  -6.09953  1.000 94.18048  ? 223 TRP   B C     1 
ATOM   5113 O O     . TRP   B 1 223 ? 58.33270  38.26172  -4.89534  1.000 97.10769  ? 223 TRP   B O     1 
ATOM   5114 C CB    . TRP   B 1 223 ? 56.98888  36.06801  -5.79839  1.000 98.21598  ? 223 TRP   B CB    1 
ATOM   5115 C CG    . TRP   B 1 223 ? 56.11342  35.10983  -6.45044  1.000 94.41653  ? 223 TRP   B CG    1 
ATOM   5116 C CD1   . TRP   B 1 223 ? 54.92815  35.38675  -7.04477  1.000 92.21064  ? 223 TRP   B CD1   1 
ATOM   5117 C CD2   . TRP   B 1 223 ? 56.27538  33.68841  -6.49285  1.000 96.77542  ? 223 TRP   B CD2   1 
ATOM   5118 N NE1   . TRP   B 1 223 ? 54.36117  34.23041  -7.50235  1.000 97.50511  ? 223 TRP   B NE1   1 
ATOM   5119 C CE2   . TRP   B 1 223 ? 55.16348  33.16971  -7.17471  1.000 98.87483  ? 223 TRP   B CE2   1 
ATOM   5120 C CE3   . TRP   B 1 223 ? 57.25997  32.80326  -6.03476  1.000 96.99651  ? 223 TRP   B CE3   1 
ATOM   5121 C CZ2   . TRP   B 1 223 ? 55.00214  31.79884  -7.41972  1.000 98.30377  ? 223 TRP   B CZ2   1 
ATOM   5122 C CZ3   . TRP   B 1 223 ? 57.09975  31.43942  -6.27894  1.000 100.18204 ? 223 TRP   B CZ3   1 
ATOM   5123 C CH2   . TRP   B 1 223 ? 55.97841  30.95432  -6.96679  1.000 99.30709  ? 223 TRP   B CH2   1 
ATOM   5124 N N     . GLU   B 1 224 ? 58.90176  38.86598  -6.98162  1.000 88.25095  ? 224 GLU   B N     1 
ATOM   5125 C CA    . GLU   B 1 224 ? 59.25900  40.18200  -6.49652  1.000 95.05612  ? 224 GLU   B CA    1 
ATOM   5126 C C     . GLU   B 1 224 ? 58.00779  40.90272  -6.01335  1.000 93.18710  ? 224 GLU   B C     1 
ATOM   5127 O O     . GLU   B 1 224 ? 56.89271  40.60717  -6.45301  1.000 91.93608  ? 224 GLU   B O     1 
ATOM   5128 C CB    . GLU   B 1 224 ? 59.97922  40.95949  -7.58023  1.000 96.63210  ? 224 GLU   B CB    1 
ATOM   5129 C CG    . GLU   B 1 224 ? 61.24853  40.24603  -7.95371  1.000 94.49899  ? 224 GLU   B CG    1 
ATOM   5130 C CD    . GLU   B 1 224 ? 61.98316  40.92265  -9.07186  1.000 110.19352 ? 224 GLU   B CD    1 
ATOM   5131 O OE1   . GLU   B 1 224 ? 62.53589  42.01536  -8.81299  1.000 110.76460 ? 224 GLU   B OE1   1 
ATOM   5132 O OE2   . GLU   B 1 224 ? 61.99614  40.38616  -10.20620 1.000 118.18011 ? 224 GLU   B OE2   1 
ATOM   5133 N N     . GLY   B 1 225 ? 58.19597  41.81772  -5.05654  1.000 91.39201  ? 225 GLY   B N     1 
ATOM   5134 C CA    . GLY   B 1 225 ? 57.06186  42.49083  -4.44692  1.000 94.85504  ? 225 GLY   B CA    1 
ATOM   5135 C C     . GLY   B 1 225 ? 56.90842  42.40145  -2.93719  1.000 92.98265  ? 225 GLY   B C     1 
ATOM   5136 O O     . GLY   B 1 225 ? 57.16538  41.37209  -2.29540  1.000 89.53819  ? 225 GLY   B O     1 
ATOM   5137 N N     . THR   B 1 226 ? 56.43022  43.49830  -2.37201  1.000 92.02979  ? 226 THR   B N     1 
ATOM   5138 C CA    . THR   B 1 226 ? 56.37115  43.67754  -0.93763  1.000 90.33997  ? 226 THR   B CA    1 
ATOM   5139 C C     . THR   B 1 226 ? 54.97151  43.53020  -0.38815  1.000 93.12549  ? 226 THR   B C     1 
ATOM   5140 O O     . THR   B 1 226 ? 54.75842  43.79292  0.79847   1.000 91.11294  ? 226 THR   B O     1 
ATOM   5141 C CB    . THR   B 1 226 ? 56.88506  45.06189  -0.57108  1.000 92.82914  ? 226 THR   B CB    1 
ATOM   5142 O OG1   . THR   B 1 226 ? 55.96307  46.03285  -1.07050  1.000 92.21580  ? 226 THR   B OG1   1 
ATOM   5143 C CG2   . THR   B 1 226 ? 58.24550  45.30852  -1.19574  1.000 92.92685  ? 226 THR   B CG2   1 
ATOM   5144 N N     . ASP   B 1 227 ? 54.01207  43.15290  -1.20319  1.000 93.43328  ? 227 ASP   B N     1 
ATOM   5145 C CA    . ASP   B 1 227 ? 52.68559  43.04438  -0.64516  1.000 100.81662 ? 227 ASP   B CA    1 
ATOM   5146 C C     . ASP   B 1 227 ? 52.62037  41.87103  0.32496   1.000 106.49491 ? 227 ASP   B C     1 
ATOM   5147 O O     . ASP   B 1 227 ? 52.79064  40.71433  -0.10248  1.000 101.40053 ? 227 ASP   B O     1 
ATOM   5148 C CB    . ASP   B 1 227 ? 51.63795  42.88846  -1.71041  1.000 101.31794 ? 227 ASP   B CB    1 
ATOM   5149 C CG    . ASP   B 1 227 ? 50.27584  42.84340  -1.10950  1.000 103.73869 ? 227 ASP   B CG    1 
ATOM   5150 O OD1   . ASP   B 1 227 ? 49.87970  43.87321  -0.51354  1.000 101.22137 ? 227 ASP   B OD1   1 
ATOM   5151 O OD2   . ASP   B 1 227 ? 49.65534  41.75626  -1.15795  1.000 98.20672  ? 227 ASP   B OD2   1 
ATOM   5152 N N     . PRO   B 1 228 ? 52.36842  42.11702  1.62531   1.000 104.67857 ? 228 PRO   B N     1 
ATOM   5153 C CA    . PRO   B 1 228 ? 52.40331  41.01259  2.60523   1.000 102.42345 ? 228 PRO   B CA    1 
ATOM   5154 C C     . PRO   B 1 228 ? 51.34873  39.94878  2.35647   1.000 105.51855 ? 228 PRO   B C     1 
ATOM   5155 O O     . PRO   B 1 228 ? 51.64232  38.74836  2.44674   1.000 106.82911 ? 228 PRO   B O     1 
ATOM   5156 C CB    . PRO   B 1 228 ? 52.18292  41.71922  3.95372   1.000 97.29432  ? 228 PRO   B CB    1 
ATOM   5157 C CG    . PRO   B 1 228 ? 52.48063  43.16431  3.70492   1.000 93.79891  ? 228 PRO   B CG    1 
ATOM   5158 C CD    . PRO   B 1 228 ? 52.17290  43.43335  2.26118   1.000 96.67029  ? 228 PRO   B CD    1 
ATOM   5159 N N     . ALA   B 1 229 ? 50.11608  40.34470  2.05319   1.000 103.74582 ? 229 ALA   B N     1 
ATOM   5160 C CA    . ALA   B 1 229 ? 49.13588  39.33250  1.69209   1.000 107.25013 ? 229 ALA   B CA    1 
ATOM   5161 C C     . ALA   B 1 229 ? 49.59783  38.55842  0.47000   1.000 104.13371 ? 229 ALA   B C     1 
ATOM   5162 O O     . ALA   B 1 229 ? 49.51037  37.32556  0.43634   1.000 102.03105 ? 229 ALA   B O     1 
ATOM   5163 C CB    . ALA   B 1 229 ? 47.77659  39.97507  1.44100   1.000 113.82899 ? 229 ALA   B CB    1 
ATOM   5164 N N     . ALA   B 1 230 ? 50.10179  39.27516  -0.54046  1.000 105.05148 ? 230 ALA   B N     1 
ATOM   5165 C CA    . ALA   B 1 230 ? 50.57548  38.63562  -1.76161  1.000 104.21756 ? 230 ALA   B CA    1 
ATOM   5166 C C     . ALA   B 1 230 ? 51.62122  37.58152  -1.45093  1.000 110.05675 ? 230 ALA   B C     1 
ATOM   5167 O O     . ALA   B 1 230 ? 51.60929  36.48490  -2.02952  1.000 108.52509 ? 230 ALA   B O     1 
ATOM   5168 C CB    . ALA   B 1 230 ? 51.14960  39.69394  -2.70078  1.000 97.87216  ? 230 ALA   B CB    1 
ATOM   5169 N N     . ARG   B 1 231 ? 52.53685  37.90596  -0.53363  1.000 110.50416 ? 231 ARG   B N     1 
ATOM   5170 C CA    . ARG   B 1 231 ? 53.58548  36.97809  -0.11934  1.000 103.92120 ? 231 ARG   B CA    1 
ATOM   5171 C C     . ARG   B 1 231 ? 52.99458  35.83783  0.70202   1.000 104.63974 ? 231 ARG   B C     1 
ATOM   5172 O O     . ARG   B 1 231 ? 53.17596  34.65651  0.37600   1.000 104.31054 ? 231 ARG   B O     1 
ATOM   5173 C CB    . ARG   B 1 231 ? 54.63380  37.75370  0.67526   1.000 96.20239  ? 231 ARG   B CB    1 
ATOM   5174 C CG    . ARG   B 1 231 ? 55.29778  38.81150  -0.15999  1.000 94.19593  ? 231 ARG   B CG    1 
ATOM   5175 C CD    . ARG   B 1 231 ? 55.69491  39.99692  0.67400   1.000 97.56787  ? 231 ARG   B CD    1 
ATOM   5176 N NE    . ARG   B 1 231 ? 56.78362  39.75807  1.61582   1.000 98.63874  ? 231 ARG   B NE    1 
ATOM   5177 C CZ    . ARG   B 1 231 ? 58.05074  39.59403  1.25715   1.000 96.66866  ? 231 ARG   B CZ    1 
ATOM   5178 N NH1   . ARG   B 1 231 ? 58.39637  39.44893  -0.01481  1.000 94.37866  ? 231 ARG   B NH1   1 
ATOM   5179 N NH2   . ARG   B 1 231 ? 58.99758  39.61126  2.19151   1.000 97.01866  ? 231 ARG   B NH2   1 
ATOM   5180 N N     . ALA   B 1 232 ? 52.25093  36.18988  1.75838   1.000 103.52766 ? 232 ALA   B N     1 
ATOM   5181 C CA    . ALA   B 1 232 ? 51.58316  35.20299  2.59914   1.000 104.17989 ? 232 ALA   B CA    1 
ATOM   5182 C C     . ALA   B 1 232 ? 50.83733  34.17273  1.76254   1.000 106.30793 ? 232 ALA   B C     1 
ATOM   5183 O O     . ALA   B 1 232 ? 50.89708  32.96924  2.03100   1.000 100.73711 ? 232 ALA   B O     1 
ATOM   5184 C CB    . ALA   B 1 232 ? 50.62476  35.91279  3.55414   1.000 105.44925 ? 232 ALA   B CB    1 
ATOM   5185 N N     . GLU   B 1 233 ? 50.09933  34.63836  0.75649   1.000 112.64511 ? 233 GLU   B N     1 
ATOM   5186 C CA    . GLU   B 1 233 ? 49.51424  33.72532  -0.21267  1.000 113.73737 ? 233 GLU   B CA    1 
ATOM   5187 C C     . GLU   B 1 233 ? 50.58897  32.77425  -0.72283  1.000 113.43535 ? 233 GLU   B C     1 
ATOM   5188 O O     . GLU   B 1 233 ? 50.43703  31.54965  -0.65936  1.000 114.76309 ? 233 GLU   B O     1 
ATOM   5189 C CB    . GLU   B 1 233 ? 48.87786  34.53274  -1.35034  1.000 112.28296 ? 233 GLU   B CB    1 
ATOM   5190 C CG    . GLU   B 1 233 ? 48.50182  33.77496  -2.63250  1.000 124.33294 ? 233 GLU   B CG    1 
ATOM   5191 C CD    . GLU   B 1 233 ? 47.66010  32.51641  -2.40165  1.000 125.85270 ? 233 GLU   B CD    1 
ATOM   5192 O OE1   . GLU   B 1 233 ? 46.77578  32.52710  -1.51038  1.000 123.64308 ? 233 GLU   B OE1   1 
ATOM   5193 O OE2   . GLU   B 1 233 ? 47.86097  31.52545  -3.14006  1.000 120.70759 ? 233 GLU   B OE2   1 
ATOM   5194 N N     . VAL   B 1 234 ? 51.71489  33.33238  -1.17698  1.000 109.32012 ? 234 VAL   B N     1 
ATOM   5195 C CA    . VAL   B 1 234 ? 52.81503  32.52242  -1.69580  1.000 113.79281 ? 234 VAL   B CA    1 
ATOM   5196 C C     . VAL   B 1 234 ? 53.10623  31.37101  -0.75214  1.000 122.52866 ? 234 VAL   B C     1 
ATOM   5197 O O     . VAL   B 1 234 ? 53.10499  30.19263  -1.13964  1.000 127.80866 ? 234 VAL   B O     1 
ATOM   5198 C CB    . VAL   B 1 234 ? 54.07031  33.38693  -1.88851  1.000 115.15866 ? 234 VAL   B CB    1 
ATOM   5199 C CG1   . VAL   B 1 234 ? 55.23069  32.52614  -2.37292  1.000 123.21866 ? 234 VAL   B CG1   1 
ATOM   5200 C CG2   . VAL   B 1 234 ? 53.77818  34.52741  -2.83390  1.000 114.23866 ? 234 VAL   B CG2   1 
ATOM   5201 N N     . PHE   B 1 235 ? 53.35639  31.71884  0.51205   1.000 123.14866 ? 235 PHE   B N     1 
ATOM   5202 C CA    . PHE   B 1 235 ? 53.81027  30.75511  1.50857   1.000 116.31143 ? 235 PHE   B CA    1 
ATOM   5203 C C     . PHE   B 1 235 ? 52.73235  29.73060  1.85021   1.000 114.21398 ? 235 PHE   B C     1 
ATOM   5204 O O     . PHE   B 1 235 ? 53.00076  28.52342  1.89235   1.000 111.87152 ? 235 PHE   B O     1 
ATOM   5205 C CB    . PHE   B 1 235 ? 54.24822  31.49947  2.76289   1.000 110.34718 ? 235 PHE   B CB    1 
ATOM   5206 C CG    . PHE   B 1 235 ? 54.31187  30.63114  3.95113   1.000 113.29233 ? 235 PHE   B CG    1 
ATOM   5207 C CD1   . PHE   B 1 235 ? 55.01288  29.43687  3.90540   1.000 109.48866 ? 235 PHE   B CD1   1 
ATOM   5208 C CD2   . PHE   B 1 235 ? 53.62699  30.96950  5.09680   1.000 112.90509 ? 235 PHE   B CD2   1 
ATOM   5209 C CE1   . PHE   B 1 235 ? 55.05335  28.61680  4.98648   1.000 106.73866 ? 235 PHE   B CE1   1 
ATOM   5210 C CE2   . PHE   B 1 235 ? 53.66497  30.15059  6.18405   1.000 111.98026 ? 235 PHE   B CE2   1 
ATOM   5211 C CZ    . PHE   B 1 235 ? 54.38138  28.97209  6.13380   1.000 108.31905 ? 235 PHE   B CZ    1 
ATOM   5212 N N     . LEU   B 1 236 ? 51.51286  30.20171  2.14540   1.000 118.19853 ? 236 LEU   B N     1 
ATOM   5213 C CA    . LEU   B 1 236 ? 50.44984  29.29739  2.57372   1.000 116.24411 ? 236 LEU   B CA    1 
ATOM   5214 C C     . LEU   B 1 236 ? 50.12214  28.29906  1.47326   1.000 113.03850 ? 236 LEU   B C     1 
ATOM   5215 O O     . LEU   B 1 236 ? 49.67992  27.17750  1.76176   1.000 108.67803 ? 236 LEU   B O     1 
ATOM   5216 C CB    . LEU   B 1 236 ? 49.21088  30.10124  2.99697   1.000 114.41727 ? 236 LEU   B CB    1 
ATOM   5217 C CG    . LEU   B 1 236 ? 49.37909  31.02170  4.22960   1.000 115.70866 ? 236 LEU   B CG    1 
ATOM   5218 C CD1   . LEU   B 1 236 ? 48.15720  31.88717  4.48784   1.000 110.28432 ? 236 LEU   B CD1   1 
ATOM   5219 C CD2   . LEU   B 1 236 ? 49.73894  30.25009  5.49192   1.000 120.50866 ? 236 LEU   B CD2   1 
ATOM   5220 N N     . THR   B 1 237 ? 50.35518  28.68947  0.21441   1.000 112.02629 ? 237 THR   B N     1 
ATOM   5221 C CA    . THR   B 1 237 ? 50.32729  27.74375  -0.89323  1.000 112.74503 ? 237 THR   B CA    1 
ATOM   5222 C C     . THR   B 1 237 ? 51.50662  26.80450  -0.81559  1.000 110.03809 ? 237 THR   B C     1 
ATOM   5223 O O     . THR   B 1 237 ? 51.41173  25.63846  -1.21799  1.000 111.14483 ? 237 THR   B O     1 
ATOM   5224 C CB    . THR   B 1 237 ? 50.38674  28.48194  -2.22180  1.000 112.15587 ? 237 THR   B CB    1 
ATOM   5225 O OG1   . THR   B 1 237 ? 49.63064  29.68850  -2.11959  1.000 112.64369 ? 237 THR   B OG1   1 
ATOM   5226 C CG2   . THR   B 1 237 ? 49.79057  27.61667  -3.32085  1.000 112.29128 ? 237 THR   B CG2   1 
ATOM   5227 N N     . TRP   B 1 238 ? 52.62516  27.32796  -0.32944  1.000 109.06269 ? 238 TRP   B N     1 
ATOM   5228 C CA    . TRP   B 1 238 ? 53.84625  26.55366  -0.21068  1.000 111.94186 ? 238 TRP   B CA    1 
ATOM   5229 C C     . TRP   B 1 238 ? 53.72651  25.53660  0.92429   1.000 109.72712 ? 238 TRP   B C     1 
ATOM   5230 O O     . TRP   B 1 238 ? 54.02431  24.34559  0.74415   1.000 103.48553 ? 238 TRP   B O     1 
ATOM   5231 C CB    . TRP   B 1 238 ? 55.00550  27.53717  -0.00008  1.000 112.24293 ? 238 TRP   B CB    1 
ATOM   5232 C CG    . TRP   B 1 238 ? 56.35391  26.93254  0.10607   1.000 115.58677 ? 238 TRP   B CG    1 
ATOM   5233 C CD1   . TRP   B 1 238 ? 57.24348  26.71407  -0.90730  1.000 107.54866 ? 238 TRP   B CD1   1 
ATOM   5234 C CD2   . TRP   B 1 238 ? 56.97275  26.44425  1.29862   1.000 122.42866 ? 238 TRP   B CD2   1 
ATOM   5235 N NE1   . TRP   B 1 238 ? 58.38072  26.12585  -0.41803  1.000 105.31866 ? 238 TRP   B NE1   1 
ATOM   5236 C CE2   . TRP   B 1 238 ? 58.24002  25.94957  0.93622   1.000 119.16866 ? 238 TRP   B CE2   1 
ATOM   5237 C CE3   . TRP   B 1 238 ? 56.57925  26.38035  2.64148   1.000 126.59866 ? 238 TRP   B CE3   1 
ATOM   5238 C CZ2   . TRP   B 1 238 ? 59.12037  25.39135  1.87113   1.000 125.48866 ? 238 TRP   B CZ2   1 
ATOM   5239 C CZ3   . TRP   B 1 238 ? 57.45554  25.82857  3.56668   1.000 123.63866 ? 238 TRP   B CZ3   1 
ATOM   5240 C CH2   . TRP   B 1 238 ? 58.70602  25.33633  3.17457   1.000 125.59866 ? 238 TRP   B CH2   1 
ATOM   5241 N N     . GLN   B 1 239 ? 53.25856  25.99481  2.09530   1.000 109.66568 ? 239 GLN   B N     1 
ATOM   5242 C CA    . GLN   B 1 239 ? 52.94026  25.09902  3.20578   1.000 108.79809 ? 239 GLN   B CA    1 
ATOM   5243 C C     . GLN   B 1 239 ? 51.93509  24.03935  2.76904   1.000 109.02120 ? 239 GLN   B C     1 
ATOM   5244 O O     . GLN   B 1 239 ? 52.13010  22.83940  2.99055   1.000 107.26563 ? 239 GLN   B O     1 
ATOM   5245 C CB    . GLN   B 1 239 ? 52.40093  25.91861  4.39099   1.000 107.58988 ? 239 GLN   B CB    1 
ATOM   5246 C CG    . GLN   B 1 239 ? 52.31743  25.18044  5.74911   1.000 106.72128 ? 239 GLN   B CG    1 
ATOM   5247 C CD    . GLN   B 1 239 ? 51.69151  26.03201  6.87892   1.000 110.01104 ? 239 GLN   B CD    1 
ATOM   5248 O OE1   . GLN   B 1 239 ? 52.34235  26.35154  7.88670   1.000 97.83760  ? 239 GLN   B OE1   1 
ATOM   5249 N NE2   . GLN   B 1 239 ? 50.42023  26.38580  6.71023   1.000 120.52777 ? 239 GLN   B NE2   1 
ATOM   5250 N N     . SER   B 1 240 ? 50.86547  24.47071  2.10310   1.000 111.58834 ? 240 SER   B N     1 
ATOM   5251 C CA    . SER   B 1 240 ? 49.82550  23.54173  1.68267   1.000 111.09473 ? 240 SER   B CA    1 
ATOM   5252 C C     . SER   B 1 240 ? 50.30872  22.59543  0.58205   1.000 112.65289 ? 240 SER   B C     1 
ATOM   5253 O O     . SER   B 1 240 ? 49.86052  21.44440  0.50729   1.000 108.16794 ? 240 SER   B O     1 
ATOM   5254 C CB    . SER   B 1 240 ? 48.60606  24.33830  1.22757   1.000 111.26882 ? 240 SER   B CB    1 
ATOM   5255 O OG    . SER   B 1 240 ? 47.41114  23.59439  1.39682   1.000 123.20289 ? 240 SER   B OG    1 
ATOM   5256 N N     . LEU   B 1 241 ? 51.21999  23.05203  -0.27428  1.000 117.79039 ? 241 LEU   B N     1 
ATOM   5257 C CA    . LEU   B 1 241 ? 51.69787  22.19938  -1.35530  1.000 117.76323 ? 241 LEU   B CA    1 
ATOM   5258 C C     . LEU   B 1 241 ? 52.55413  21.05322  -0.82919  1.000 119.44139 ? 241 LEU   B C     1 
ATOM   5259 O O     . LEU   B 1 241 ? 52.51239  19.93985  -1.37602  1.000 122.18111 ? 241 LEU   B O     1 
ATOM   5260 C CB    . LEU   B 1 241 ? 52.47635  23.03572  -2.36085  1.000 117.43152 ? 241 LEU   B CB    1 
ATOM   5261 C CG    . LEU   B 1 241 ? 52.35793  22.53881  -3.79247  1.000 135.04866 ? 241 LEU   B CG    1 
ATOM   5262 C CD1   . LEU   B 1 241 ? 53.10918  23.50474  -4.68739  1.000 152.77866 ? 241 LEU   B CD1   1 
ATOM   5263 C CD2   . LEU   B 1 241 ? 52.88290  21.10131  -3.93025  1.000 132.08866 ? 241 LEU   B CD2   1 
ATOM   5264 N N     . LEU   B 1 242 ? 53.34048  21.30927  0.22738   1.000 112.11779 ? 242 LEU   B N     1 
ATOM   5265 C CA    . LEU   B 1 242 ? 54.20631  20.27258  0.79635   1.000 118.13131 ? 242 LEU   B CA    1 
ATOM   5266 C C     . LEU   B 1 242 ? 53.39219  19.20645  1.52467   1.000 116.61654 ? 242 LEU   B C     1 
ATOM   5267 O O     . LEU   B 1 242 ? 53.54598  18.00097  1.26149   1.000 114.24356 ? 242 LEU   B O     1 
ATOM   5268 C CB    . LEU   B 1 242 ? 55.23650  20.90452  1.74511   1.000 114.96866 ? 242 LEU   B CB    1 
ATOM   5269 C CG    . LEU   B 1 242 ? 56.15688  20.03743  2.63476   1.000 104.96432 ? 242 LEU   B CG    1 
ATOM   5270 C CD1   . LEU   B 1 242 ? 57.08649  19.09422  1.84834   1.000 99.88639  ? 242 LEU   B CD1   1 
ATOM   5271 C CD2   . LEU   B 1 242 ? 56.95669  20.93057  3.60291   1.000 96.01292  ? 242 LEU   B CD2   1 
ATOM   5272 N N     . ALA   B 1 243 ? 52.51383  19.64505  2.44386   1.000 110.02443 ? 243 ALA   B N     1 
ATOM   5273 C CA    . ALA   B 1 243 ? 51.68460  18.73808  3.22579   1.000 111.26897 ? 243 ALA   B CA    1 
ATOM   5274 C C     . ALA   B 1 243 ? 50.80595  17.82778  2.35676   1.000 119.74132 ? 243 ALA   B C     1 
ATOM   5275 O O     . ALA   B 1 243 ? 50.42355  16.74072  2.80802   1.000 120.61089 ? 243 ALA   B O     1 
ATOM   5276 C CB    . ALA   B 1 243 ? 50.83230  19.54709  4.21432   1.000 101.73426 ? 243 ALA   B CB    1 
ATOM   5277 N N     . GLY   B 1 244 ? 50.48585  18.22380  1.12395   1.000 119.32826 ? 244 GLY   B N     1 
ATOM   5278 C CA    . GLY   B 1 244 ? 49.70132  17.36575  0.25670   1.000 109.32388 ? 244 GLY   B CA    1 
ATOM   5279 C C     . GLY   B 1 244 ? 50.29143  15.98471  0.03818   1.000 107.36689 ? 244 GLY   B C     1 
ATOM   5280 O O     . GLY   B 1 244 ? 49.58717  15.06207  -0.38435  1.000 108.06436 ? 244 GLY   B O     1 
ATOM   5281 N N     . GLY   B 1 245 ? 51.57583  15.81148  0.33514   1.000 108.39055 ? 245 GLY   B N     1 
ATOM   5282 C CA    . GLY   B 1 245 ? 52.19540  14.54415  0.00404   1.000 115.51754 ? 245 GLY   B CA    1 
ATOM   5283 C C     . GLY   B 1 245 ? 52.21591  14.29727  -1.48210  1.000 114.03869 ? 245 GLY   B C     1 
ATOM   5284 O O     . GLY   B 1 245 ? 52.39901  13.15751  -1.92929  1.000 109.37716 ? 245 GLY   B O     1 
ATOM   5285 N N     . SER   B 1 246 ? 52.01752  15.36569  -2.25108  1.000 114.60981 ? 246 SER   B N     1 
ATOM   5286 C CA    . SER   B 1 246 ? 51.98916  15.33705  -3.70223  1.000 117.18349 ? 246 SER   B CA    1 
ATOM   5287 C C     . SER   B 1 246 ? 53.38450  15.26452  -4.30922  1.000 127.44253 ? 246 SER   B C     1 
ATOM   5288 O O     . SER   B 1 246 ? 53.58018  14.62877  -5.35679  1.000 120.13984 ? 246 SER   B O     1 
ATOM   5289 C CB    . SER   B 1 246 ? 51.25391  16.59019  -4.19092  1.000 116.70557 ? 246 SER   B CB    1 
ATOM   5290 O OG    . SER   B 1 246 ? 51.61375  17.72812  -3.40471  1.000 112.56838 ? 246 SER   B OG    1 
ATOM   5291 N N     . LEU   B 1 247 ? 54.35874  15.88717  -3.64279  1.000 128.96944 ? 247 LEU   B N     1 
ATOM   5292 C CA    . LEU   B 1 247 ? 55.66846  16.15403  -4.20236  1.000 121.47310 ? 247 LEU   B CA    1 
ATOM   5293 C C     . LEU   B 1 247 ? 56.45133  14.85148  -4.34700  1.000 124.63859 ? 247 LEU   B C     1 
ATOM   5294 O O     . LEU   B 1 247 ? 56.14833  13.85792  -3.68539  1.000 126.63616 ? 247 LEU   B O     1 
ATOM   5295 C CB    . LEU   B 1 247 ? 56.40600  17.11198  -3.27949  1.000 118.95654 ? 247 LEU   B CB    1 
ATOM   5296 C CG    . LEU   B 1 247 ? 55.67797  18.44678  -3.07813  1.000 121.45866 ? 247 LEU   B CG    1 
ATOM   5297 C CD1   . LEU   B 1 247 ? 56.35046  19.29571  -2.02449  1.000 118.27866 ? 247 LEU   B CD1   1 
ATOM   5298 C CD2   . LEU   B 1 247 ? 55.57096  19.22034  -4.37602  1.000 133.22866 ? 247 LEU   B CD2   1 
ATOM   5299 N N     . PRO   B 1 248 ? 57.46583  14.82906  -5.20862  1.000 127.19161 ? 248 PRO   B N     1 
ATOM   5300 C CA    . PRO   B 1 248 ? 58.32443  13.63586  -5.32067  1.000 128.92361 ? 248 PRO   B CA    1 
ATOM   5301 C C     . PRO   B 1 248 ? 59.18385  13.42230  -4.07381  1.000 125.88086 ? 248 PRO   B C     1 
ATOM   5302 O O     . PRO   B 1 248 ? 59.33335  14.28592  -3.20049  1.000 117.61136 ? 248 PRO   B O     1 
ATOM   5303 C CB    . PRO   B 1 248 ? 59.18914  13.91875  -6.55300  1.000 119.23574 ? 248 PRO   B CB    1 
ATOM   5304 C CG    . PRO   B 1 248 ? 58.47042  15.03680  -7.26887  1.000 125.63518 ? 248 PRO   B CG    1 
ATOM   5305 C CD    . PRO   B 1 248 ? 57.81167  15.84962  -6.21122  1.000 121.39272 ? 248 PRO   B CD    1 
ATOM   5306 N N     . GLN   B 1 249 ? 59.75550  12.22357  -3.98878  1.000 126.00158 ? 249 GLN   B N     1 
ATOM   5307 C CA    . GLN   B 1 249 ? 60.66280  11.95007  -2.88446  1.000 124.54740 ? 249 GLN   B CA    1 
ATOM   5308 C C     . GLN   B 1 249 ? 62.01957  12.57397  -3.15156  1.000 119.07746 ? 249 GLN   B C     1 
ATOM   5309 O O     . GLN   B 1 249 ? 62.59481  13.22716  -2.26899  1.000 109.40326 ? 249 GLN   B O     1 
ATOM   5310 C CB    . GLN   B 1 249 ? 60.80718  10.44531  -2.66857  1.000 124.19011 ? 249 GLN   B CB    1 
ATOM   5311 C CG    . GLN   B 1 249 ? 59.55178  9.78932   -2.11568  1.000 127.66125 ? 249 GLN   B CG    1 
ATOM   5312 C CD    . GLN   B 1 249 ? 59.31558  10.09948  -0.64277  1.000 119.94123 ? 249 GLN   B CD    1 
ATOM   5313 O OE1   . GLN   B 1 249 ? 58.35692  10.79204  -0.29395  1.000 118.59674 ? 249 GLN   B OE1   1 
ATOM   5314 N NE2   . GLN   B 1 249 ? 60.19608  9.60327   0.22098   1.000 110.54804 ? 249 GLN   B NE2   1 
ATOM   5315 N N     . HIS   B 1 250 ? 62.49774  12.42573  -4.39180  1.000 124.31804 ? 250 HIS   B N     1 
ATOM   5316 C CA    . HIS   B 1 250 ? 63.83671  12.85952  -4.79485  1.000 122.71944 ? 250 HIS   B CA    1 
ATOM   5317 C C     . HIS   B 1 250 ? 63.77533  14.28447  -5.33964  1.000 112.93820 ? 250 HIS   B C     1 
ATOM   5318 O O     . HIS   B 1 250 ? 63.92864  14.52570  -6.54000  1.000 104.53523 ? 250 HIS   B O     1 
ATOM   5319 C CB    . HIS   B 1 250 ? 64.41476  11.92387  -5.85022  1.000 113.70680 ? 250 HIS   B CB    1 
ATOM   5320 C CG    . HIS   B 1 250 ? 64.25939  10.47601  -5.52295  1.000 122.14461 ? 250 HIS   B CG    1 
ATOM   5321 N ND1   . HIS   B 1 250 ? 63.87875  10.03056  -4.27328  1.000 126.41739 ? 250 HIS   B ND1   1 
ATOM   5322 C CD2   . HIS   B 1 250 ? 64.50619  9.36739   -6.25951  1.000 125.99602 ? 250 HIS   B CD2   1 
ATOM   5323 C CE1   . HIS   B 1 250 ? 63.84279  8.70976   -4.27260  1.000 124.94379 ? 250 HIS   B CE1   1 
ATOM   5324 N NE2   . HIS   B 1 250 ? 64.22935  8.28220   -5.46271  1.000 127.82370 ? 250 HIS   B NE2   1 
ATOM   5325 N N     . MET   B 1 251 ? 63.55849  15.23566  -4.42768  1.000 100.05661 ? 251 MET   B N     1 
ATOM   5326 C CA    . MET   B 1 251 ? 63.42406  16.61777  -4.86002  1.000 97.98241  ? 251 MET   B CA    1 
ATOM   5327 C C     . MET   B 1 251 ? 63.32401  17.52487  -3.64495  1.000 93.51045  ? 251 MET   B C     1 
ATOM   5328 O O     . MET   B 1 251 ? 62.40527  17.36918  -2.83886  1.000 95.84205  ? 251 MET   B O     1 
ATOM   5329 C CB    . MET   B 1 251 ? 62.18661  16.76658  -5.75619  1.000 108.71828 ? 251 MET   B CB    1 
ATOM   5330 C CG    . MET   B 1 251 ? 62.09921  18.07436  -6.55440  1.000 113.01866 ? 251 MET   B CG    1 
ATOM   5331 S SD    . MET   B 1 251 ? 60.85821  19.27227  -5.99703  1.000 124.43866 ? 251 MET   B SD    1 
ATOM   5332 C CE    . MET   B 1 251 ? 59.54683  19.05266  -7.19821  1.000 120.93212 ? 251 MET   B CE    1 
ATOM   5333 N N     . ALA   B 1 252 ? 64.25776  18.45653  -3.49021  1.000 89.53468  ? 252 ALA   B N     1 
ATOM   5334 C CA    . ALA   B 1 252 ? 64.21523  19.39083  -2.37577  1.000 87.68366  ? 252 ALA   B CA    1 
ATOM   5335 C C     . ALA   B 1 252 ? 63.34431  20.57679  -2.73238  1.000 86.55870  ? 252 ALA   B C     1 
ATOM   5336 O O     . ALA   B 1 252 ? 63.06616  20.84377  -3.90077  1.000 93.09465  ? 252 ALA   B O     1 
ATOM   5337 C CB    . ALA   B 1 252 ? 65.61119  19.87411  -1.98354  1.000 88.71068  ? 252 ALA   B CB    1 
ATOM   5338 N N     . TYR   B 1 253 ? 62.93463  21.30901  -1.70917  1.000 82.26039  ? 253 TYR   B N     1 
ATOM   5339 C CA    . TYR   B 1 253 ? 61.82395  22.24139  -1.87144  1.000 85.71044  ? 253 TYR   B CA    1 
ATOM   5340 C C     . TYR   B 1 253 ? 62.04878  23.35726  -0.85300  1.000 91.75160  ? 253 TYR   B C     1 
ATOM   5341 O O     . TYR   B 1 253 ? 61.60157  23.27660  0.28848   1.000 97.93364  ? 253 TYR   B O     1 
ATOM   5342 C CB    . TYR   B 1 253 ? 60.50567  21.49567  -1.68528  1.000 86.18160  ? 253 TYR   B CB    1 
ATOM   5343 C CG    . TYR   B 1 253 ? 59.17795  22.25995  -1.68031  1.000 98.87891  ? 253 TYR   B CG    1 
ATOM   5344 C CD1   . TYR   B 1 253 ? 58.58867  22.67596  -0.48946  1.000 101.00821 ? 253 TYR   B CD1   1 
ATOM   5345 C CD2   . TYR   B 1 253 ? 58.47579  22.49328  -2.85979  1.000 106.50587 ? 253 TYR   B CD2   1 
ATOM   5346 C CE1   . TYR   B 1 253 ? 57.35560  23.32876  -0.47245  1.000 106.11076 ? 253 TYR   B CE1   1 
ATOM   5347 C CE2   . TYR   B 1 253 ? 57.24051  23.15466  -2.84632  1.000 109.87902 ? 253 TYR   B CE2   1 
ATOM   5348 C CZ    . TYR   B 1 253 ? 56.68666  23.57356  -1.64743  1.000 108.70974 ? 253 TYR   B CZ    1 
ATOM   5349 O OH    . TYR   B 1 253 ? 55.45973  24.22457  -1.61170  1.000 106.90948 ? 253 TYR   B OH    1 
ATOM   5350 N N     . ASP   B 1 254 ? 62.79692  24.36573  -1.25822  1.000 89.19864  ? 254 ASP   B N     1 
ATOM   5351 C CA    . ASP   B 1 254 ? 63.05283  25.47094  -0.35791  1.000 89.90693  ? 254 ASP   B CA    1 
ATOM   5352 C C     . ASP   B 1 254 ? 62.00342  26.54638  -0.57894  1.000 87.35520  ? 254 ASP   B C     1 
ATOM   5353 O O     . ASP   B 1 254 ? 61.13060  26.43965  -1.43807  1.000 90.82194  ? 254 ASP   B O     1 
ATOM   5354 C CB    . ASP   B 1 254 ? 64.46267  26.03268  -0.56069  1.000 96.64244  ? 254 ASP   B CB    1 
ATOM   5355 C CG    . ASP   B 1 254 ? 65.54153  24.95312  -0.49229  1.000 100.79410 ? 254 ASP   B CG    1 
ATOM   5356 O OD1   . ASP   B 1 254 ? 65.73848  24.37663  0.60173   1.000 104.71866 ? 254 ASP   B OD1   1 
ATOM   5357 O OD2   . ASP   B 1 254 ? 66.20204  24.69105  -1.52531  1.000 104.51582 ? 254 ASP   B OD2   1 
ATOM   5358 N N     . LEU   B 1 255 ? 62.08007  27.59346  0.22219   1.000 83.01586  ? 255 LEU   B N     1 
ATOM   5359 C CA    . LEU   B 1 255 ? 61.33609  28.79510  -0.06312  1.000 82.69564  ? 255 LEU   B CA    1 
ATOM   5360 C C     . LEU   B 1 255 ? 61.88707  29.87783  0.83067   1.000 80.92371  ? 255 LEU   B C     1 
ATOM   5361 O O     . LEU   B 1 255 ? 61.75993  29.80771  2.04365   1.000 84.65726  ? 255 LEU   B O     1 
ATOM   5362 C CB    . LEU   B 1 255 ? 59.83985  28.63600  0.18707   1.000 92.29385  ? 255 LEU   B CB    1 
ATOM   5363 C CG    . LEU   B 1 255 ? 59.04883  29.88642  -0.20993  1.000 95.68941  ? 255 LEU   B CG    1 
ATOM   5364 C CD1   . LEU   B 1 255 ? 58.80211  29.89256  -1.72614  1.000 95.31698  ? 255 LEU   B CD1   1 
ATOM   5365 C CD2   . LEU   B 1 255 ? 57.74592  30.05967  0.56849   1.000 101.84985 ? 255 LEU   B CD2   1 
ATOM   5366 N N     . VAL   B 1 256 ? 62.51832  30.86986  0.24855   1.000 82.41200  ? 256 VAL   B N     1 
ATOM   5367 C CA    . VAL   B 1 256 ? 63.11953  31.92626  1.03886   1.000 79.06361  ? 256 VAL   B CA    1 
ATOM   5368 C C     . VAL   B 1 256 ? 62.28502  33.18093  0.84686   1.000 81.18874  ? 256 VAL   B C     1 
ATOM   5369 O O     . VAL   B 1 256 ? 61.57588  33.32638  -0.15839  1.000 86.11291  ? 256 VAL   B O     1 
ATOM   5370 C CB    . VAL   B 1 256 ? 64.58828  32.13753  0.63649   1.000 74.74533  ? 256 VAL   B CB    1 
ATOM   5371 C CG1   . VAL   B 1 256 ? 65.23361  33.07617  1.62079   1.000 73.00574  ? 256 VAL   B CG1   1 
ATOM   5372 C CG2   . VAL   B 1 256 ? 65.32254  30.79183  0.55067   1.000 72.53361  ? 256 VAL   B CG2   1 
ATOM   5373 N N     . ALA   B 1 257 ? 62.36075  34.09022  1.82122   1.000 75.83696  ? 257 ALA   B N     1 
ATOM   5374 C CA    . ALA   B 1 257 ? 61.54931  35.30440  1.80739   1.000 72.39307  ? 257 ALA   B CA    1 
ATOM   5375 C C     . ALA   B 1 257 ? 62.37602  36.48795  2.26667   1.000 77.63800  ? 257 ALA   B C     1 
ATOM   5376 O O     . ALA   B 1 257 ? 62.88430  36.48776  3.38964   1.000 78.54624  ? 257 ALA   B O     1 
ATOM   5377 C CB    . ALA   B 1 257 ? 60.34087  35.14765  2.71447   1.000 73.18909  ? 257 ALA   B CB    1 
ATOM   5378 N N     . THR   B 1 258 ? 62.47322  37.51279  1.44057   1.000 79.47339  ? 258 THR   B N     1 
ATOM   5379 C CA    . THR   B 1 258 ? 63.18638  38.70085  1.86586   1.000 78.95213  ? 258 THR   B CA    1 
ATOM   5380 C C     . THR   B 1 258 ? 62.27447  39.92117  1.76575   1.000 80.54513  ? 258 THR   B C     1 
ATOM   5381 O O     . THR   B 1 258 ? 61.05796  39.81610  1.61164   1.000 83.01390  ? 258 THR   B O     1 
ATOM   5382 C CB    . THR   B 1 258 ? 64.44818  38.87996  1.03856   1.000 82.40309  ? 258 THR   B CB    1 
ATOM   5383 O OG1   . THR   B 1 258 ? 64.10369  39.53273  -0.18542  1.000 97.71311  ? 258 THR   B OG1   1 
ATOM   5384 C CG2   . THR   B 1 258 ? 65.01370  37.52786  0.69580   1.000 82.24866  ? 258 THR   B CG2   1 
ATOM   5385 N N     . ALA   B 1 259 ? 62.89049  41.09185  1.85160   1.000 81.11574  ? 259 ALA   B N     1 
ATOM   5386 C CA    . ALA   B 1 259 ? 62.13692  42.33313  1.92299   1.000 86.66789  ? 259 ALA   B CA    1 
ATOM   5387 C C     . ALA   B 1 259 ? 61.27574  42.57942  0.68751   1.000 89.06716  ? 259 ALA   B C     1 
ATOM   5388 O O     . ALA   B 1 259 ? 60.34457  43.38796  0.76023   1.000 89.38736  ? 259 ALA   B O     1 
ATOM   5389 C CB    . ALA   B 1 259 ? 63.10244  43.49681  2.15211   1.000 88.37097  ? 259 ALA   B CB    1 
ATOM   5390 N N     . ASN   B 1 260 ? 61.56506  41.91660  -0.43824  1.000 89.85978  ? 260 ASN   B N     1 
ATOM   5391 C CA    . ASN   B 1 260 ? 60.70473  41.97150  -1.62249  1.000 92.61296  ? 260 ASN   B CA    1 
ATOM   5392 C C     . ASN   B 1 260 ? 61.00189  40.82262  -2.58420  1.000 89.87966  ? 260 ASN   B C     1 
ATOM   5393 O O     . ASN   B 1 260 ? 61.57017  41.03450  -3.66023  1.000 88.78940  ? 260 ASN   B O     1 
ATOM   5394 C CB    . ASN   B 1 260 ? 60.84280  43.31315  -2.35802  1.000 92.61698  ? 260 ASN   B CB    1 
ATOM   5395 C CG    . ASN   B 1 260 ? 62.27670  43.77213  -2.48083  1.000 92.88259  ? 260 ASN   B CG    1 
ATOM   5396 O OD1   . ASN   B 1 260 ? 63.15477  43.00622  -2.88346  1.000 96.52054  ? 260 ASN   B OD1   1 
ATOM   5397 N ND2   . ASN   B 1 260 ? 62.52296  45.02813  -2.13539  1.000 91.49546  ? 260 ASN   B ND2   1 
ATOM   5398 N N     . SER   B 1 261 ? 60.62743  39.60284  -2.19763  1.000 88.84069  ? 261 SER   B N     1 
ATOM   5399 C CA    . SER   B 1 261 ? 60.73373  38.43230  -3.06383  1.000 91.17275  ? 261 SER   B CA    1 
ATOM   5400 C C     . SER   B 1 261 ? 60.43749  37.17055  -2.26363  1.000 89.63311  ? 261 SER   B C     1 
ATOM   5401 O O     . SER   B 1 261 ? 60.67082  37.11883  -1.04990  1.000 88.67738  ? 261 SER   B O     1 
ATOM   5402 C CB    . SER   B 1 261 ? 62.11875  38.32079  -3.71311  1.000 91.47815  ? 261 SER   B CB    1 
ATOM   5403 O OG    . SER   B 1 261 ? 63.14146  38.23038  -2.73945  1.000 93.66458  ? 261 SER   B OG    1 
ATOM   5404 N N     . MET   B 1 262 ? 59.92138  36.15176  -2.94443  1.000 84.99277  ? 262 MET   B N     1 
ATOM   5405 C CA    . MET   B 1 262 ? 59.58308  34.86380  -2.34154  1.000 89.72531  ? 262 MET   B CA    1 
ATOM   5406 C C     . MET   B 1 262 ? 60.19275  33.80891  -3.24920  1.000 92.50373  ? 262 MET   B C     1 
ATOM   5407 O O     . MET   B 1 262 ? 59.51141  33.23171  -4.10504  1.000 97.27911  ? 262 MET   B O     1 
ATOM   5408 C CB    . MET   B 1 262 ? 58.07574  34.67371  -2.19629  1.000 93.26126  ? 262 MET   B CB    1 
ATOM   5409 C CG    . MET   B 1 262 ? 57.35668  35.82471  -1.55335  1.000 96.76235  ? 262 MET   B CG    1 
ATOM   5410 S SD    . MET   B 1 262 ? 57.73233  35.90046  0.20856   1.000 91.31406  ? 262 MET   B SD    1 
ATOM   5411 C CE    . MET   B 1 262 ? 56.97694  34.35020  0.72326   1.000 99.23325  ? 262 MET   B CE    1 
ATOM   5412 N N     . ILE   B 1 263 ? 61.47319  33.54630  -3.06061  1.000 83.04268  ? 263 ILE   B N     1 
ATOM   5413 C CA    . ILE   B 1 263 ? 62.18354  32.65142  -3.95771  1.000 87.81872  ? 263 ILE   B CA    1 
ATOM   5414 C C     . ILE   B 1 263 ? 61.84219  31.21376  -3.57113  1.000 88.52599  ? 263 ILE   B C     1 
ATOM   5415 O O     . ILE   B 1 263 ? 61.93756  30.84109  -2.39901  1.000 91.18696  ? 263 ILE   B O     1 
ATOM   5416 C CB    . ILE   B 1 263 ? 63.69224  32.92275  -3.89543  1.000 91.43886  ? 263 ILE   B CB    1 
ATOM   5417 C CG1   . ILE   B 1 263 ? 63.96763  34.35253  -4.34743  1.000 91.41866  ? 263 ILE   B CG1   1 
ATOM   5418 C CG2   . ILE   B 1 263 ? 64.47465  31.93224  -4.75481  1.000 96.37955  ? 263 ILE   B CG2   1 
ATOM   5419 C CD1   . ILE   B 1 263 ? 65.40953  34.77032  -4.18130  1.000 97.53339  ? 263 ILE   B CD1   1 
ATOM   5420 N N     . LEU   B 1 264 ? 61.40549  30.41830  -4.54806  1.000 83.86873  ? 264 LEU   B N     1 
ATOM   5421 C CA    . LEU   B 1 264 ? 61.08027  29.00575  -4.34914  1.000 80.91424  ? 264 LEU   B CA    1 
ATOM   5422 C C     . LEU   B 1 264 ? 62.22178  28.15937  -4.89238  1.000 85.24108  ? 264 LEU   B C     1 
ATOM   5423 O O     . LEU   B 1 264 ? 62.22072  27.75944  -6.05864  1.000 87.56778  ? 264 LEU   B O     1 
ATOM   5424 C CB    . LEU   B 1 264 ? 59.77329  28.65256  -5.03740  1.000 83.29769  ? 264 LEU   B CB    1 
ATOM   5425 C CG    . LEU   B 1 264 ? 59.18275  27.27051  -4.78899  1.000 87.85318  ? 264 LEU   B CG    1 
ATOM   5426 C CD1   . LEU   B 1 264 ? 57.73364  27.31949  -5.19349  1.000 97.29118  ? 264 LEU   B CD1   1 
ATOM   5427 C CD2   . LEU   B 1 264 ? 59.90258  26.18169  -5.58019  1.000 85.90696  ? 264 LEU   B CD2   1 
ATOM   5428 N N     . GLY   B 1 265 ? 63.18979  27.85209  -4.03379  1.000 87.27809  ? 265 GLY   B N     1 
ATOM   5429 C CA    . GLY   B 1 265 ? 64.34619  27.09823  -4.46605  1.000 89.06309  ? 265 GLY   B CA    1 
ATOM   5430 C C     . GLY   B 1 265 ? 64.13738  25.59309  -4.42378  1.000 86.90048  ? 265 GLY   B C     1 
ATOM   5431 O O     . GLY   B 1 265 ? 63.16406  25.08134  -3.87651  1.000 85.00755  ? 265 GLY   B O     1 
ATOM   5432 N N     . GLY   B 1 266 ? 65.08415  24.88393  -5.01543  1.000 85.74496  ? 266 GLY   B N     1 
ATOM   5433 C CA    . GLY   B 1 266 ? 65.10520  23.44217  -4.90627  1.000 82.29037  ? 266 GLY   B CA    1 
ATOM   5434 C C     . GLY   B 1 266 ? 65.99572  22.83359  -5.96504  1.000 84.76988  ? 266 GLY   B C     1 
ATOM   5435 O O     . GLY   B 1 266 ? 66.56999  23.52235  -6.80793  1.000 84.06821  ? 266 GLY   B O     1 
ATOM   5436 N N     . ALA   B 1 267 ? 66.10770  21.51329  -5.88075  1.000 82.64499  ? 267 ALA   B N     1 
ATOM   5437 C CA    . ALA   B 1 267 ? 66.76193  20.67626  -6.86866  1.000 84.72296  ? 267 ALA   B CA    1 
ATOM   5438 C C     . ALA   B 1 267 ? 65.80820  19.53558  -7.22138  1.000 90.74714  ? 267 ALA   B C     1 
ATOM   5439 O O     . ALA   B 1 267 ? 64.73015  19.40230  -6.63657  1.000 91.14646  ? 267 ALA   B O     1 
ATOM   5440 C CB    . ALA   B 1 267 ? 68.10648  20.14101  -6.34544  1.000 76.57753  ? 267 ALA   B CB    1 
ATOM   5441 N N     . TYR   B 1 268 ? 66.20757  18.71013  -8.19020  1.000 90.55950  ? 268 TYR   B N     1 
ATOM   5442 C CA    . TYR   B 1 268 ? 65.43925  17.54781  -8.61671  1.000 93.28200  ? 268 TYR   B CA    1 
ATOM   5443 C C     . TYR   B 1 268 ? 66.38137  16.53148  -9.24484  1.000 93.25360  ? 268 TYR   B C     1 
ATOM   5444 O O     . TYR   B 1 268 ? 67.22531  16.88231  -10.07341 1.000 94.74551  ? 268 TYR   B O     1 
ATOM   5445 C CB    . TYR   B 1 268 ? 64.33352  17.92924  -9.61533  1.000 98.05536  ? 268 TYR   B CB    1 
ATOM   5446 C CG    . TYR   B 1 268 ? 63.59692  16.73664  -10.18567 1.000 100.90352 ? 268 TYR   B CG    1 
ATOM   5447 C CD1   . TYR   B 1 268 ? 64.07150  16.07069  -11.31444 1.000 102.34713 ? 268 TYR   B CD1   1 
ATOM   5448 C CD2   . TYR   B 1 268 ? 62.45098  16.25406  -9.57672  1.000 104.64970 ? 268 TYR   B CD2   1 
ATOM   5449 C CE1   . TYR   B 1 268 ? 63.42163  14.98204  -11.82596 1.000 100.32059 ? 268 TYR   B CE1   1 
ATOM   5450 C CE2   . TYR   B 1 268 ? 61.79295  15.15560  -10.08595 1.000 108.01517 ? 268 TYR   B CE2   1 
ATOM   5451 C CZ    . TYR   B 1 268 ? 62.28825  14.52925  -11.21028 1.000 104.00473 ? 268 TYR   B CZ    1 
ATOM   5452 O OH    . TYR   B 1 268 ? 61.64225  13.43698  -11.71732 1.000 107.59913 ? 268 TYR   B OH    1 
ATOM   5453 N N     . PHE   B 1 269 ? 66.22816  15.27013  -8.87348  1.000 94.39608  ? 269 PHE   B N     1 
ATOM   5454 C CA    . PHE   B 1 269 ? 67.15245  14.23483  -9.31327  1.000 98.38519  ? 269 PHE   B CA    1 
ATOM   5455 C C     . PHE   B 1 269 ? 66.45634  13.34057  -10.32113 1.000 102.11050 ? 269 PHE   B C     1 
ATOM   5456 O O     . PHE   B 1 269 ? 65.61496  12.51445  -9.95344  1.000 105.17047 ? 269 PHE   B O     1 
ATOM   5457 C CB    . PHE   B 1 269 ? 67.68783  13.47479  -8.11122  1.000 103.50210 ? 269 PHE   B CB    1 
ATOM   5458 C CG    . PHE   B 1 269 ? 68.46088  14.35506  -7.19848  1.000 98.86678  ? 269 PHE   B CG    1 
ATOM   5459 C CD1   . PHE   B 1 269 ? 69.79359  14.61644  -7.44629  1.000 96.37743  ? 269 PHE   B CD1   1 
ATOM   5460 C CD2   . PHE   B 1 269 ? 67.83138  15.01730  -6.16092  1.000 101.24356 ? 269 PHE   B CD2   1 
ATOM   5461 C CE1   . PHE   B 1 269 ? 70.50399  15.47941  -6.63454  1.000 96.58504  ? 269 PHE   B CE1   1 
ATOM   5462 C CE2   . PHE   B 1 269 ? 68.53371  15.87935  -5.33773  1.000 95.80393  ? 269 PHE   B CE2   1 
ATOM   5463 C CZ    . PHE   B 1 269 ? 69.86975  16.11285  -5.57414  1.000 96.32901  ? 269 PHE   B CZ    1 
ATOM   5464 N N     . GLY   B 1 270 ? 66.83282  13.51268  -11.58551 1.000 100.81000 ? 270 GLY   B N     1 
ATOM   5465 C CA    . GLY   B 1 270 ? 66.18573  12.97334  -12.75729 1.000 105.28714 ? 270 GLY   B CA    1 
ATOM   5466 C C     . GLY   B 1 270 ? 66.33316  13.94721  -13.91266 1.000 109.44031 ? 270 GLY   B C     1 
ATOM   5467 O O     . GLY   B 1 270 ? 67.16722  14.85082  -13.87403 1.000 111.30866 ? 270 GLY   B O     1 
ATOM   5468 N N     . SER   B 1 271 ? 65.50066  13.78125  -14.94005 1.000 113.35120 ? 271 SER   B N     1 
ATOM   5469 C CA    . SER   B 1 271 ? 65.61449  14.56948  -16.16040 1.000 116.83089 ? 271 SER   B CA    1 
ATOM   5470 C C     . SER   B 1 271 ? 64.76256  15.83742  -16.09383 1.000 115.12207 ? 271 SER   B C     1 
ATOM   5471 O O     . SER   B 1 271 ? 63.79765  15.93606  -15.33020 1.000 113.85316 ? 271 SER   B O     1 
ATOM   5472 C CB    . SER   B 1 271 ? 65.22005  13.73532  -17.38479 1.000 122.65507 ? 271 SER   B CB    1 
ATOM   5473 O OG    . SER   B 1 271 ? 63.81390  13.63965  -17.53631 1.000 126.22866 ? 271 SER   B OG    1 
ATOM   5474 N N     . GLN   B 1 272 ? 65.13455  16.81368  -16.92813 1.000 113.38875 ? 272 GLN   B N     1 
ATOM   5475 C CA    . GLN   B 1 272 ? 64.48246  18.11870  -16.87428 1.000 114.94634 ? 272 GLN   B CA    1 
ATOM   5476 C C     . GLN   B 1 272 ? 63.03292  18.05125  -17.33969 1.000 123.17224 ? 272 GLN   B C     1 
ATOM   5477 O O     . GLN   B 1 272 ? 62.15613  18.65896  -16.71364 1.000 123.00843 ? 272 GLN   B O     1 
ATOM   5478 C CB    . GLN   B 1 272 ? 65.26988  19.13134  -17.70202 1.000 110.11117 ? 272 GLN   B CB    1 
ATOM   5479 C CG    . GLN   B 1 272 ? 64.73976  20.55370  -17.62806 1.000 107.01994 ? 272 GLN   B CG    1 
ATOM   5480 C CD    . GLN   B 1 272 ? 65.45050  21.47599  -18.60329 1.000 106.43960 ? 272 GLN   B CD    1 
ATOM   5481 O OE1   . GLN   B 1 272 ? 66.68133  21.50368  -18.65220 1.000 98.36999  ? 272 GLN   B OE1   1 
ATOM   5482 N NE2   . GLN   B 1 272 ? 64.68170  22.22521  -19.39372 1.000 104.66784 ? 272 GLN   B NE2   1 
ATOM   5483 N N     . GLU   B 1 273 ? 62.75887  17.33531  -18.44065 1.000 125.47361 ? 273 GLU   B N     1 
ATOM   5484 C CA    . GLU   B 1 273 ? 61.39247  17.20242  -18.94908 1.000 127.47654 ? 273 GLU   B CA    1 
ATOM   5485 C C     . GLU   B 1 273 ? 60.43135  16.97541  -17.79416 1.000 129.02346 ? 273 GLU   B C     1 
ATOM   5486 O O     . GLU   B 1 273 ? 59.34605  17.57009  -17.72462 1.000 126.98548 ? 273 GLU   B O     1 
ATOM   5487 C CB    . GLU   B 1 273 ? 61.27725  16.03588  -19.94261 1.000 121.11264 ? 273 GLU   B CB    1 
ATOM   5488 C CG    . GLU   B 1 273 ? 61.93014  16.24234  -21.29785 1.000 124.15833 ? 273 GLU   B CG    1 
ATOM   5489 C CD    . GLU   B 1 273 ? 63.43268  16.05934  -21.24105 1.000 129.59429 ? 273 GLU   B CD    1 
ATOM   5490 O OE1   . GLU   B 1 273 ? 63.96989  16.05144  -20.11077 1.000 126.45987 ? 273 GLU   B OE1   1 
ATOM   5491 O OE2   . GLU   B 1 273 ? 64.07533  15.92082  -22.31195 1.000 127.71177 ? 273 GLU   B OE2   1 
ATOM   5492 N N     . ASP   B 1 274 ? 60.85378  16.12114  -16.86777 1.000 125.53367 ? 274 ASP   B N     1 
ATOM   5493 C CA    . ASP   B 1 274 ? 59.96956  15.66501  -15.81046 1.000 125.69920 ? 274 ASP   B CA    1 
ATOM   5494 C C     . ASP   B 1 274 ? 59.67100  16.78795  -14.83299 1.000 125.16121 ? 274 ASP   B C     1 
ATOM   5495 O O     . ASP   B 1 274 ? 58.50562  17.06412  -14.52683 1.000 126.85177 ? 274 ASP   B O     1 
ATOM   5496 C CB    . ASP   B 1 274 ? 60.62479  14.48051  -15.11933 1.000 121.96844 ? 274 ASP   B CB    1 
ATOM   5497 C CG    . ASP   B 1 274 ? 61.17713  13.49258  -16.11069 1.000 119.29169 ? 274 ASP   B CG    1 
ATOM   5498 O OD1   . ASP   B 1 274 ? 60.72879  13.50829  -17.27451 1.000 120.03991 ? 274 ASP   B OD1   1 
ATOM   5499 O OD2   . ASP   B 1 274 ? 62.08784  12.73607  -15.74393 1.000 120.89326 ? 274 ASP   B OD2   1 
ATOM   5500 N N     . PHE   B 1 275 ? 60.71478  17.46242  -14.34223 1.000 120.46349 ? 275 PHE   B N     1 
ATOM   5501 C CA    . PHE   B 1 275 ? 60.48092  18.52573  -13.37512 1.000 121.79073 ? 275 PHE   B CA    1 
ATOM   5502 C C     . PHE   B 1 275 ? 59.54372  19.58911  -13.94509 1.000 128.70866 ? 275 PHE   B C     1 
ATOM   5503 O O     . PHE   B 1 275 ? 58.66904  20.10782  -13.23522 1.000 126.09208 ? 275 PHE   B O     1 
ATOM   5504 C CB    . PHE   B 1 275 ? 61.79786  19.16262  -12.92361 1.000 107.97023 ? 275 PHE   B CB    1 
ATOM   5505 C CG    . PHE   B 1 275 ? 61.58573  20.43745  -12.20514 1.000 100.54418 ? 275 PHE   B CG    1 
ATOM   5506 C CD1   . PHE   B 1 275 ? 61.30613  20.43800  -10.86036 1.000 105.33130 ? 275 PHE   B CD1   1 
ATOM   5507 C CD2   . PHE   B 1 275 ? 61.56476  21.63779  -12.89112 1.000 104.94364 ? 275 PHE   B CD2   1 
ATOM   5508 C CE1   . PHE   B 1 275 ? 61.05460  21.62288  -10.19052 1.000 111.71866 ? 275 PHE   B CE1   1 
ATOM   5509 C CE2   . PHE   B 1 275 ? 61.30916  22.82591  -12.22869 1.000 105.74576 ? 275 PHE   B CE2   1 
ATOM   5510 C CZ    . PHE   B 1 275 ? 61.05614  22.81888  -10.87740 1.000 104.03869 ? 275 PHE   B CZ    1 
ATOM   5511 N N     . GLU   B 1 276 ? 59.72304  19.93989  -15.22090 1.000 138.59866 ? 276 GLU   B N     1 
ATOM   5512 C CA    . GLU   B 1 276 ? 58.75465  20.79527  -15.89984 1.000 129.67592 ? 276 GLU   B CA    1 
ATOM   5513 C C     . GLU   B 1 276 ? 57.42636  20.06723  -16.04818 1.000 131.69328 ? 276 GLU   B C     1 
ATOM   5514 O O     . GLU   B 1 276 ? 56.35888  20.61687  -15.73535 1.000 122.41379 ? 276 GLU   B O     1 
ATOM   5515 C CB    . GLU   B 1 276 ? 59.30239  21.20553  -17.26288 1.000 123.20111 ? 276 GLU   B CB    1 
ATOM   5516 C CG    . GLU   B 1 276 ? 60.33270  22.29924  -17.20370 1.000 118.11888 ? 276 GLU   B CG    1 
ATOM   5517 C CD    . GLU   B 1 276 ? 60.97852  22.53507  -18.55121 1.000 123.16517 ? 276 GLU   B CD    1 
ATOM   5518 O OE1   . GLU   B 1 276 ? 61.68280  21.61756  -19.03468 1.000 126.67823 ? 276 GLU   B OE1   1 
ATOM   5519 O OE2   . GLU   B 1 276 ? 60.78754  23.62910  -19.12651 1.000 114.23160 ? 276 GLU   B OE2   1 
ATOM   5520 N N     . ALA   B 1 277 ? 57.48585  18.81422  -16.51980 1.000 132.15654 ? 277 ALA   B N     1 
ATOM   5521 C CA    . ALA   B 1 277 ? 56.31389  17.95234  -16.52363 1.000 128.91178 ? 277 ALA   B CA    1 
ATOM   5522 C C     . ALA   B 1 277 ? 55.51578  18.18078  -15.25203 1.000 132.54714 ? 277 ALA   B C     1 
ATOM   5523 O O     . ALA   B 1 277 ? 54.34955  18.57548  -15.29943 1.000 136.58114 ? 277 ALA   B O     1 
ATOM   5524 C CB    . ALA   B 1 277 ? 56.72717  16.48271  -16.66963 1.000 119.23146 ? 277 ALA   B CB    1 
ATOM   5525 N N     . PHE   B 1 278 ? 56.15913  18.02658  -14.09922 1.000 133.65432 ? 278 PHE   B N     1 
ATOM   5526 C CA    . PHE   B 1 278 ? 55.43417  18.20731  -12.84766 1.000 140.62748 ? 278 PHE   B CA    1 
ATOM   5527 C C     . PHE   B 1 278 ? 54.81796  19.60293  -12.73958 1.000 139.77360 ? 278 PHE   B C     1 
ATOM   5528 O O     . PHE   B 1 278 ? 53.83833  19.78739  -12.00838 1.000 139.86371 ? 278 PHE   B O     1 
ATOM   5529 C CB    . PHE   B 1 278 ? 56.35720  17.93168  -11.66992 1.000 142.12325 ? 278 PHE   B CB    1 
ATOM   5530 C CG    . PHE   B 1 278 ? 55.63883  17.69489  -10.38960 1.000 149.74688 ? 278 PHE   B CG    1 
ATOM   5531 C CD1   . PHE   B 1 278 ? 55.22681  18.75914  -9.60718  1.000 161.54866 ? 278 PHE   B CD1   1 
ATOM   5532 C CD2   . PHE   B 1 278 ? 55.37292  16.41022  -9.96390  1.000 154.05308 ? 278 PHE   B CD2   1 
ATOM   5533 C CE1   . PHE   B 1 278 ? 54.56178  18.54356  -8.41859  1.000 171.14866 ? 278 PHE   B CE1   1 
ATOM   5534 C CE2   . PHE   B 1 278 ? 54.70874  16.18427  -8.77231  1.000 160.33866 ? 278 PHE   B CE2   1 
ATOM   5535 C CZ    . PHE   B 1 278 ? 54.30275  17.25203  -7.99759  1.000 170.40866 ? 278 PHE   B CZ    1 
ATOM   5536 N N     . ASN   B 1 279 ? 55.35361  20.59067  -13.46235 1.000 136.35438 ? 279 ASN   B N     1 
ATOM   5537 C CA    . ASN   B 1 279 ? 54.76889  21.93221  -13.44810 1.000 136.91170 ? 279 ASN   B CA    1 
ATOM   5538 C C     . ASN   B 1 279 ? 54.63840  22.45594  -12.02153 1.000 128.56352 ? 279 ASN   B C     1 
ATOM   5539 O O     . ASN   B 1 279 ? 53.58372  22.92846  -11.59981 1.000 126.63741 ? 279 ASN   B O     1 
ATOM   5540 C CB    . ASN   B 1 279 ? 53.41783  21.93870  -14.17782 1.000 139.63410 ? 279 ASN   B CB    1 
ATOM   5541 C CG    . ASN   B 1 279 ? 53.25069  23.13873  -15.10445 1.000 140.40866 ? 279 ASN   B CG    1 
ATOM   5542 O OD1   . ASN   B 1 279 ? 53.81274  24.20387  -14.84432 1.000 155.48866 ? 279 ASN   B OD1   1 
ATOM   5543 N ND2   . ASN   B 1 279 ? 52.49970  22.96388  -16.20902 1.000 143.04866 ? 279 ASN   B ND2   1 
ATOM   5544 N N     . LEU   B 1 280 ? 55.73532  22.36492  -11.27256 1.000 126.25447 ? 280 LEU   B N     1 
ATOM   5545 C CA    . LEU   B 1 280 ? 55.71535  22.86401  -9.90548  1.000 131.60895 ? 280 LEU   B CA    1 
ATOM   5546 C C     . LEU   B 1 280 ? 54.99947  24.20436  -9.83604  1.000 127.93151 ? 280 LEU   B C     1 
ATOM   5547 O O     . LEU   B 1 280 ? 54.17390  24.44239  -8.94352  1.000 127.14758 ? 280 LEU   B O     1 
ATOM   5548 C CB    . LEU   B 1 280 ? 57.14101  22.99390  -9.36926  1.000 132.20276 ? 280 LEU   B CB    1 
ATOM   5549 C CG    . LEU   B 1 280 ? 57.30754  23.26987  -7.87186  1.000 138.39866 ? 280 LEU   B CG    1 
ATOM   5550 C CD1   . LEU   B 1 280 ? 56.79617  22.09344  -7.04055  1.000 137.76866 ? 280 LEU   B CD1   1 
ATOM   5551 C CD2   . LEU   B 1 280 ? 58.75832  23.62416  -7.53646  1.000 144.48866 ? 280 LEU   B CD2   1 
ATOM   5552 N N     . SER   B 1 281 ? 55.27863  25.08213  -10.79685 1.000 127.50720 ? 281 SER   B N     1 
ATOM   5553 C CA    . SER   B 1 281 ? 54.71348  26.42354  -10.74947 1.000 124.27369 ? 281 SER   B CA    1 
ATOM   5554 C C     . SER   B 1 281 ? 53.19136  26.38104  -10.77399 1.000 123.13291 ? 281 SER   B C     1 
ATOM   5555 O O     . SER   B 1 281 ? 52.53104  27.15997  -10.07602 1.000 117.06803 ? 281 SER   B O     1 
ATOM   5556 C CB    . SER   B 1 281 ? 55.25838  27.23718  -11.91512 1.000 118.57898 ? 281 SER   B CB    1 
ATOM   5557 O OG    . SER   B 1 281 ? 55.18992  26.43602  -13.07750 1.000 127.48267 ? 281 SER   B OG    1 
ATOM   5558 N N     . SER   B 1 282 ? 52.61335  25.45242  -11.54407 1.000 126.45137 ? 282 SER   B N     1 
ATOM   5559 C CA    . SER   B 1 282 ? 51.16731  25.46912  -11.76453 1.000 127.79382 ? 282 SER   B CA    1 
ATOM   5560 C C     . SER   B 1 282 ? 50.39601  25.59349  -10.45234 1.000 122.23739 ? 282 SER   B C     1 
ATOM   5561 O O     . SER   B 1 282 ? 49.52507  26.45757  -10.31059 1.000 121.09044 ? 282 SER   B O     1 
ATOM   5562 C CB    . SER   B 1 282 ? 50.72707  24.21223  -12.52051 1.000 127.21647 ? 282 SER   B CB    1 
ATOM   5563 O OG    . SER   B 1 282 ? 50.55893  23.11910  -11.64037 1.000 119.43176 ? 282 SER   B OG    1 
ATOM   5564 N N     . HIS   B 1 283 ? 50.71710  24.75553  -9.47307  1.000 118.30288 ? 283 HIS   B N     1 
ATOM   5565 C CA    . HIS   B 1 283 ? 49.87269  24.66557  -8.29365  1.000 115.40695 ? 283 HIS   B CA    1 
ATOM   5566 C C     . HIS   B 1 283 ? 49.67441  25.99954  -7.58914  1.000 113.44278 ? 283 HIS   B C     1 
ATOM   5567 O O     . HIS   B 1 283 ? 48.82694  26.07024  -6.69434  1.000 111.82183 ? 283 HIS   B O     1 
ATOM   5568 C CB    . HIS   B 1 283 ? 50.47814  23.66681  -7.32857  1.000 118.61961 ? 283 HIS   B CB    1 
ATOM   5569 C CG    . HIS   B 1 283 ? 50.70075  22.32408  -7.93912  1.000 125.50740 ? 283 HIS   B CG    1 
ATOM   5570 N ND1   . HIS   B 1 283 ? 51.72145  22.08013  -8.83325  1.000 132.46466 ? 283 HIS   B ND1   1 
ATOM   5571 C CD2   . HIS   B 1 283 ? 50.05547  21.14624  -7.77417  1.000 124.24988 ? 283 HIS   B CD2   1 
ATOM   5572 C CE1   . HIS   B 1 283 ? 51.68499  20.81349  -9.20702  1.000 131.67027 ? 283 HIS   B CE1   1 
ATOM   5573 N NE2   . HIS   B 1 283 ? 50.68636  20.22342  -8.57454  1.000 130.42113 ? 283 HIS   B NE2   1 
ATOM   5574 N N     . PHE   B 1 284 ? 50.43136  27.03715  -7.95263  1.000 113.47003 ? 284 PHE   B N     1 
ATOM   5575 C CA    . PHE   B 1 284 ? 50.39372  28.33160  -7.27478  1.000 118.59825 ? 284 PHE   B CA    1 
ATOM   5576 C C     . PHE   B 1 284 ? 49.33915  29.25067  -7.91395  1.000 112.00266 ? 284 PHE   B C     1 
ATOM   5577 O O     . PHE   B 1 284 ? 48.92591  29.04434  -9.05555  1.000 114.22509 ? 284 PHE   B O     1 
ATOM   5578 C CB    . PHE   B 1 284 ? 51.77206  29.02852  -7.30005  1.000 123.00095 ? 284 PHE   B CB    1 
ATOM   5579 C CG    . PHE   B 1 284 ? 52.68752  28.70060  -6.10363  1.000 124.60563 ? 284 PHE   B CG    1 
ATOM   5580 C CD1   . PHE   B 1 284 ? 53.21632  27.42196  -5.93788  1.000 119.15613 ? 284 PHE   B CD1   1 
ATOM   5581 C CD2   . PHE   B 1 284 ? 53.01050  29.68510  -5.15026  1.000 117.31461 ? 284 PHE   B CD2   1 
ATOM   5582 C CE1   . PHE   B 1 284 ? 54.04196  27.12971  -4.85948  1.000 115.01331 ? 284 PHE   B CE1   1 
ATOM   5583 C CE2   . PHE   B 1 284 ? 53.83153  29.39697  -4.06186  1.000 110.52421 ? 284 PHE   B CE2   1 
ATOM   5584 C CZ    . PHE   B 1 284 ? 54.34773  28.12206  -3.91937  1.000 116.66630 ? 284 PHE   B CZ    1 
ATOM   5585 N N     . LYS   B 1 285 ? 48.91815  30.27515  -7.15452  1.000 108.73616 ? 285 LYS   B N     1 
ATOM   5586 C CA    . LYS   B 1 285 ? 47.88103  31.20966  -7.58891  1.000 111.30960 ? 285 LYS   B CA    1 
ATOM   5587 C C     . LYS   B 1 285 ? 48.42977  32.26054  -8.55571  1.000 105.22798 ? 285 LYS   B C     1 
ATOM   5588 O O     . LYS   B 1 285 ? 48.30837  32.10445  -9.77410  1.000 108.62946 ? 285 LYS   B O     1 
ATOM   5589 C CB    . LYS   B 1 285 ? 47.20547  31.89599  -6.38771  1.000 111.57674 ? 285 LYS   B CB    1 
ATOM   5590 N N     . VAL   B 1 286 ? 49.02097  33.33989  -8.04601  1.000 103.03303 ? 286 VAL   B N     1 
ATOM   5591 C CA    . VAL   B 1 286 ? 49.74126  34.29159  -8.89422  1.000 93.69912  ? 286 VAL   B CA    1 
ATOM   5592 C C     . VAL   B 1 286 ? 50.98624  33.60099  -9.44420  1.000 94.81817  ? 286 VAL   B C     1 
ATOM   5593 O O     . VAL   B 1 286 ? 51.77800  33.04332  -8.68261  1.000 100.46093 ? 286 VAL   B O     1 
ATOM   5594 C CB    . VAL   B 1 286 ? 50.11118  35.55666  -8.10734  1.000 84.84440  ? 286 VAL   B CB    1 
ATOM   5595 C CG1   . VAL   B 1 286 ? 51.13240  36.39964  -8.86916  1.000 79.21002  ? 286 VAL   B CG1   1 
ATOM   5596 C CG2   . VAL   B 1 286 ? 48.86066  36.34997  -7.77567  1.000 76.59309  ? 286 VAL   B CG2   1 
ATOM   5597 N N     . ALA   B 1 287 ? 51.16944  33.63349  -10.76409 1.000 96.39421  ? 287 ALA   B N     1 
ATOM   5598 C CA    . ALA   B 1 287 ? 52.33970  32.99516  -11.35186 1.000 91.07718  ? 287 ALA   B CA    1 
ATOM   5599 C C     . ALA   B 1 287 ? 53.59361  33.84925  -11.12914 1.000 91.10191  ? 287 ALA   B C     1 
ATOM   5600 O O     . ALA   B 1 287 ? 53.50955  35.06319  -10.89442 1.000 81.34184  ? 287 ALA   B O     1 
ATOM   5601 C CB    . ALA   B 1 287 ? 52.12850  32.72874  -12.83967 1.000 86.16525  ? 287 ALA   B CB    1 
ATOM   5602 N N     . PRO   B 1 288 ? 54.78602  33.22358  -11.21797 1.000 92.94440  ? 288 PRO   B N     1 
ATOM   5603 C CA    . PRO   B 1 288 ? 56.00080  33.86277  -10.69529 1.000 94.36622  ? 288 PRO   B CA    1 
ATOM   5604 C C     . PRO   B 1 288 ? 56.66449  34.83339  -11.67571 1.000 95.49098  ? 288 PRO   B C     1 
ATOM   5605 O O     . PRO   B 1 288 ? 56.88971  34.49230  -12.84780 1.000 95.36451  ? 288 PRO   B O     1 
ATOM   5606 C CB    . PRO   B 1 288 ? 56.90130  32.65261  -10.39402 1.000 91.14738  ? 288 PRO   B CB    1 
ATOM   5607 C CG    . PRO   B 1 288 ? 56.54393  31.67237  -11.51557 1.000 89.18406  ? 288 PRO   B CG    1 
ATOM   5608 C CD    . PRO   B 1 288 ? 55.06473  31.89419  -11.80795 1.000 89.58674  ? 288 PRO   B CD    1 
ATOM   5609 N N     . ASP   B 1 289 ? 57.01096  36.03604  -11.19547 1.000 90.50723  ? 289 ASP   B N     1 
ATOM   5610 C CA    . ASP   B 1 289 ? 57.66566  37.03778  -12.03893 1.000 95.16569  ? 289 ASP   B CA    1 
ATOM   5611 C C     . ASP   B 1 289 ? 58.83134  36.49178  -12.87078 1.000 103.59567 ? 289 ASP   B C     1 
ATOM   5612 O O     . ASP   B 1 289 ? 59.12589  37.04553  -13.94238 1.000 109.15229 ? 289 ASP   B O     1 
ATOM   5613 C CB    . ASP   B 1 289 ? 58.17377  38.19832  -11.17643 1.000 98.42625  ? 289 ASP   B CB    1 
ATOM   5614 C CG    . ASP   B 1 289 ? 57.05378  39.06895  -10.65309 1.000 101.91702 ? 289 ASP   B CG    1 
ATOM   5615 O OD1   . ASP   B 1 289 ? 56.35608  39.72001  -11.47192 1.000 102.20519 ? 289 ASP   B OD1   1 
ATOM   5616 O OD2   . ASP   B 1 289 ? 56.87093  39.08116  -9.41371  1.000 101.80758 ? 289 ASP   B OD2   1 
ATOM   5617 N N     . VAL   B 1 290 ? 59.50934  35.42011  -12.40653 1.000 99.81480  ? 290 VAL   B N     1 
ATOM   5618 C CA    . VAL   B 1 290 ? 60.76747  34.94482  -13.00010 1.000 96.52320  ? 290 VAL   B CA    1 
ATOM   5619 C C     . VAL   B 1 290 ? 60.95996  33.44270  -12.73425 1.000 95.04382  ? 290 VAL   B C     1 
ATOM   5620 O O     . VAL   B 1 290 ? 60.31509  32.85976  -11.85934 1.000 95.97505  ? 290 VAL   B O     1 
ATOM   5621 C CB    . VAL   B 1 290 ? 61.96186  35.76849  -12.44331 1.000 97.21924  ? 290 VAL   B CB    1 
ATOM   5622 C CG1   . VAL   B 1 290 ? 63.30424  35.23863  -12.95020 1.000 104.96621 ? 290 VAL   B CG1   1 
ATOM   5623 C CG2   . VAL   B 1 290 ? 61.79865  37.26652  -12.74154 1.000 98.10350  ? 290 VAL   B CG2   1 
ATOM   5624 N N     . THR   B 1 291 ? 61.88251  32.81834  -13.48398 1.000 98.35910  ? 291 THR   B N     1 
ATOM   5625 C CA    . THR   B 1 291 ? 62.11499  31.37095  -13.45234 1.000 95.11740  ? 291 THR   B CA    1 
ATOM   5626 C C     . THR   B 1 291 ? 63.49517  31.02500  -13.99944 1.000 97.54666  ? 291 THR   B C     1 
ATOM   5627 O O     . THR   B 1 291 ? 63.95038  31.62411  -14.97542 1.000 106.05723 ? 291 THR   B O     1 
ATOM   5628 C CB    . THR   B 1 291 ? 61.07932  30.60490  -14.29586 1.000 99.03875  ? 291 THR   B CB    1 
ATOM   5629 O OG1   . THR   B 1 291 ? 59.75399  30.88026  -13.81768 1.000 97.80461  ? 291 THR   B OG1   1 
ATOM   5630 C CG2   . THR   B 1 291 ? 61.37379  29.07454  -14.27993 1.000 97.99293  ? 291 THR   B CG2   1 
ATOM   5631 N N     . HIS   B 1 292 ? 64.13495  30.03186  -13.40236 1.000 91.72341  ? 292 HIS   B N     1 
ATOM   5632 C CA    . HIS   B 1 292 ? 65.35604  29.46530  -13.96049 1.000 92.07593  ? 292 HIS   B CA    1 
ATOM   5633 C C     . HIS   B 1 292 ? 65.30694  27.96502  -13.73421 1.000 87.92365  ? 292 HIS   B C     1 
ATOM   5634 O O     . HIS   B 1 292 ? 64.65530  27.49586  -12.79822 1.000 92.97866  ? 292 HIS   B O     1 
ATOM   5635 C CB    . HIS   B 1 292 ? 66.64078  30.06080  -13.33772 1.000 99.69489  ? 292 HIS   B CB    1 
ATOM   5636 C CG    . HIS   B 1 292 ? 66.59574  31.54651  -13.09526 1.000 117.31866 ? 292 HIS   B CG    1 
ATOM   5637 N ND1   . HIS   B 1 292 ? 67.07660  32.46557  -14.00771 1.000 125.33866 ? 292 HIS   B ND1   1 
ATOM   5638 C CD2   . HIS   B 1 292 ? 66.14886  32.27279  -12.04038 1.000 124.97866 ? 292 HIS   B CD2   1 
ATOM   5639 C CE1   . HIS   B 1 292 ? 66.93165  33.68912  -13.52421 1.000 120.53866 ? 292 HIS   B CE1   1 
ATOM   5640 N NE2   . HIS   B 1 292 ? 66.36528  33.60086  -12.33396 1.000 124.58866 ? 292 HIS   B NE2   1 
ATOM   5641 N N     . ILE   B 1 293 ? 65.95857  27.21354  -14.61220 1.000 83.47165  ? 293 ILE   B N     1 
ATOM   5642 C CA    . ILE   B 1 293 ? 66.01566  25.75755  -14.51423 1.000 86.17487  ? 293 ILE   B CA    1 
ATOM   5643 C C     . ILE   B 1 293 ? 67.23704  25.22774  -15.24930 1.000 91.59611  ? 293 ILE   B C     1 
ATOM   5644 O O     . ILE   B 1 293 ? 67.15789  24.88621  -16.43573 1.000 97.28910  ? 293 ILE   B O     1 
ATOM   5645 C CB    . ILE   B 1 293 ? 64.75746  25.08075  -15.08482 1.000 84.86011  ? 293 ILE   B CB    1 
ATOM   5646 C CG1   . ILE   B 1 293 ? 63.49246  25.44663  -14.31283 1.000 86.63527  ? 293 ILE   B CG1   1 
ATOM   5647 C CG2   . ILE   B 1 293 ? 64.97317  23.58467  -15.18487 1.000 88.69696  ? 293 ILE   B CG2   1 
ATOM   5648 C CD1   . ILE   B 1 293 ? 62.24332  24.97775  -15.00638 1.000 91.06796  ? 293 ILE   B CD1   1 
ATOM   5649 N N     . LYS   B 1 294 ? 68.36385  25.12888  -14.56098 1.000 91.43621  ? 294 LYS   B N     1 
ATOM   5650 C CA    . LYS   B 1 294 ? 69.59731  24.68017  -15.18539 1.000 88.29539  ? 294 LYS   B CA    1 
ATOM   5651 C C     . LYS   B 1 294 ? 69.79317  23.21329  -14.84226 1.000 89.35709  ? 294 LYS   B C     1 
ATOM   5652 O O     . LYS   B 1 294 ? 69.42313  22.76075  -13.75442 1.000 93.41067  ? 294 LYS   B O     1 
ATOM   5653 C CB    . LYS   B 1 294 ? 70.79173  25.51330  -14.71585 1.000 83.32364  ? 294 LYS   B CB    1 
ATOM   5654 C CG    . LYS   B 1 294 ? 72.16109  25.13010  -15.29446 1.000 89.25866  ? 294 LYS   B CG    1 
ATOM   5655 C CD    . LYS   B 1 294 ? 72.23778  25.30154  -16.81451 1.000 100.48866 ? 294 LYS   B CD    1 
ATOM   5656 C CE    . LYS   B 1 294 ? 73.65576  25.08658  -17.32935 1.000 115.27866 ? 294 LYS   B CE    1 
ATOM   5657 N NZ    . LYS   B 1 294 ? 73.74697  25.03095  -18.81317 1.000 124.39866 ? 294 LYS   B NZ    1 
ATOM   5658 N N     . THR   B 1 295 ? 70.36115  22.46863  -15.76417 1.000 86.30288  ? 295 THR   B N     1 
ATOM   5659 C CA    . THR   B 1 295 ? 70.51050  21.04219  -15.57354 1.000 81.58166  ? 295 THR   B CA    1 
ATOM   5660 C C     . THR   B 1 295 ? 71.98569  20.69396  -15.51716 1.000 81.44502  ? 295 THR   B C     1 
ATOM   5661 O O     . THR   B 1 295 ? 72.72065  20.92762  -16.48091 1.000 83.79935  ? 295 THR   B O     1 
ATOM   5662 C CB    . THR   B 1 295 ? 69.80384  20.28771  -16.69123 1.000 89.34113  ? 295 THR   B CB    1 
ATOM   5663 O OG1   . THR   B 1 295 ? 68.38798  20.38583  -16.48919 1.000 89.25592  ? 295 THR   B OG1   1 
ATOM   5664 C CG2   . THR   B 1 295 ? 70.23741  18.83665  -16.67757 1.000 87.86277  ? 295 THR   B CG2   1 
ATOM   5665 N N     . TYR   B 1 296 ? 72.40902  20.14692  -14.38524 1.000 83.75219  ? 296 TYR   B N     1 
ATOM   5666 C CA    . TYR   B 1 296 ? 73.78164  19.70985  -14.15576 1.000 83.97785  ? 296 TYR   B CA    1 
ATOM   5667 C C     . TYR   B 1 296 ? 73.85362  18.19576  -14.27886 1.000 81.57691  ? 296 TYR   B C     1 
ATOM   5668 O O     . TYR   B 1 296 ? 73.25146  17.47094  -13.47472 1.000 82.10904  ? 296 TYR   B O     1 
ATOM   5669 C CB    . TYR   B 1 296 ? 74.25274  20.14112  -12.77128 1.000 79.53523  ? 296 TYR   B CB    1 
ATOM   5670 C CG    . TYR   B 1 296 ? 74.34917  21.62697  -12.62486 1.000 75.80912  ? 296 TYR   B CG    1 
ATOM   5671 C CD1   . TYR   B 1 296 ? 73.20815  22.41208  -12.66091 1.000 79.30068  ? 296 TYR   B CD1   1 
ATOM   5672 C CD2   . TYR   B 1 296 ? 75.56081  22.23916  -12.37187 1.000 68.16792  ? 296 TYR   B CD2   1 
ATOM   5673 C CE1   . TYR   B 1 296 ? 73.28072  23.77227  -12.52759 1.000 81.15186  ? 296 TYR   B CE1   1 
ATOM   5674 C CE2   . TYR   B 1 296 ? 75.64250  23.59647  -12.22034 1.000 69.56996  ? 296 TYR   B CE2   1 
ATOM   5675 C CZ    . TYR   B 1 296 ? 74.50247  24.36697  -12.29907 1.000 75.94684  ? 296 TYR   B CZ    1 
ATOM   5676 O OH    . TYR   B 1 296 ? 74.57795  25.73912  -12.14385 1.000 78.99718  ? 296 TYR   B OH    1 
ATOM   5677 N N     . THR   B 1 297 ? 74.57403  17.71606  -15.28345 1.000 79.49970  ? 297 THR   B N     1 
ATOM   5678 C CA    . THR   B 1 297 ? 74.95440  16.31316  -15.28869 1.000 82.61625  ? 297 THR   B CA    1 
ATOM   5679 C C     . THR   B 1 297 ? 76.05334  16.06917  -14.25887 1.000 94.55093  ? 297 THR   B C     1 
ATOM   5680 O O     . THR   B 1 297 ? 75.90941  15.21952  -13.36173 1.000 94.42525  ? 297 THR   B O     1 
ATOM   5681 C CB    . THR   B 1 297 ? 75.45338  15.92754  -16.66665 1.000 81.67032  ? 297 THR   B CB    1 
ATOM   5682 O OG1   . THR   B 1 297 ? 76.86523  16.19728  -16.73931 1.000 83.97801  ? 297 THR   B OG1   1 
ATOM   5683 C CG2   . THR   B 1 297 ? 74.76184  16.79652  -17.67766 1.000 75.90003  ? 297 THR   B CG2   1 
ATOM   5684 N N     . ASN   B 1 298 ? 77.15795  16.82457  -14.38243 1.000 91.97634  ? 298 ASN   B N     1 
ATOM   5685 C CA    . ASN   B 1 298 ? 78.20955  16.86170  -13.37336 1.000 83.20350  ? 298 ASN   B CA    1 
ATOM   5686 C C     . ASN   B 1 298 ? 77.61150  17.32969  -12.04851 1.000 83.58149  ? 298 ASN   B C     1 
ATOM   5687 O O     . ASN   B 1 298 ? 77.00816  18.40966  -11.97625 1.000 79.20271  ? 298 ASN   B O     1 
ATOM   5688 C CB    . ASN   B 1 298 ? 79.34488  17.78435  -13.83155 1.000 77.98480  ? 298 ASN   B CB    1 
ATOM   5689 C CG    . ASN   B 1 298 ? 80.55814  17.75770  -12.90456 1.000 80.52299  ? 298 ASN   B CG    1 
ATOM   5690 O OD1   . ASN   B 1 298 ? 80.41355  17.81438  -11.67934 1.000 82.57804  ? 298 ASN   B OD1   1 
ATOM   5691 N ND2   . ASN   B 1 298 ? 81.75905  17.68842  -13.48406 1.000 75.36084  ? 298 ASN   B ND2   1 
ATOM   5692 N N     . PHE   B 1 299 ? 77.73788  16.47526  -11.01950 1.000 87.52062  ? 299 PHE   B N     1 
ATOM   5693 C CA    . PHE   B 1 299 ? 77.14271  16.72274  -9.70441  1.000 88.95904  ? 299 PHE   B CA    1 
ATOM   5694 C C     . PHE   B 1 299 ? 77.95567  17.74146  -8.90628  1.000 82.31028  ? 299 PHE   B C     1 
ATOM   5695 O O     . PHE   B 1 299 ? 77.38512  18.65601  -8.28995  1.000 77.17943  ? 299 PHE   B O     1 
ATOM   5696 C CB    . PHE   B 1 299 ? 76.97477  15.37812  -8.95367  1.000 86.40799  ? 299 PHE   B CB    1 
ATOM   5697 C CG    . PHE   B 1 299 ? 76.44740  15.51866  -7.55443  1.000 82.97895  ? 299 PHE   B CG    1 
ATOM   5698 C CD1   . PHE   B 1 299 ? 75.16344  15.98351  -7.32766  1.000 89.94803  ? 299 PHE   B CD1   1 
ATOM   5699 C CD2   . PHE   B 1 299 ? 77.20885  15.13848  -6.47547  1.000 78.02668  ? 299 PHE   B CD2   1 
ATOM   5700 C CE1   . PHE   B 1 299 ? 74.67525  16.13359  -6.04082  1.000 86.91503  ? 299 PHE   B CE1   1 
ATOM   5701 C CE2   . PHE   B 1 299 ? 76.72523  15.27206  -5.18810  1.000 84.66864  ? 299 PHE   B CE2   1 
ATOM   5702 C CZ    . PHE   B 1 299 ? 75.45530  15.76740  -4.96815  1.000 86.09335  ? 299 PHE   B CZ    1 
ATOM   5703 N N     . PHE   B 1 300 ? 79.28928  17.61275  -8.93788  1.000 78.81494  ? 300 PHE   B N     1 
ATOM   5704 C CA    . PHE   B 1 300 ? 80.14305  18.54986  -8.22340  1.000 74.81455  ? 300 PHE   B CA    1 
ATOM   5705 C C     . PHE   B 1 300 ? 79.88683  19.97560  -8.68796  1.000 75.20992  ? 300 PHE   B C     1 
ATOM   5706 O O     . PHE   B 1 300 ? 79.77058  20.90127  -7.86805  1.000 74.05981  ? 300 PHE   B O     1 
ATOM   5707 C CB    . PHE   B 1 300 ? 81.61042  18.19533  -8.43743  1.000 67.97847  ? 300 PHE   B CB    1 
ATOM   5708 C CG    . PHE   B 1 300 ? 82.54826  19.17599  -7.82106  1.000 67.30593  ? 300 PHE   B CG    1 
ATOM   5709 C CD1   . PHE   B 1 300 ? 82.78215  19.17179  -6.46359  1.000 70.92436  ? 300 PHE   B CD1   1 
ATOM   5710 C CD2   . PHE   B 1 300 ? 83.12585  20.17071  -8.58982  1.000 71.06283  ? 300 PHE   B CD2   1 
ATOM   5711 C CE1   . PHE   B 1 300 ? 83.63635  20.09759  -5.88521  1.000 72.52730  ? 300 PHE   B CE1   1 
ATOM   5712 C CE2   . PHE   B 1 300 ? 83.96835  21.10228  -8.01875  1.000 70.93364  ? 300 PHE   B CE2   1 
ATOM   5713 C CZ    . PHE   B 1 300 ? 84.22726  21.06300  -6.66448  1.000 70.23015  ? 300 PHE   B CZ    1 
ATOM   5714 N N     . ASP   B 1 301 ? 79.81188  20.17450  -10.00502 1.000 71.65060  ? 301 ASP   B N     1 
ATOM   5715 C CA    . ASP   B 1 301 ? 79.43851  21.48101  -10.53752 1.000 73.68683  ? 301 ASP   B CA    1 
ATOM   5716 C C     . ASP   B 1 301 ? 78.11674  21.93146  -9.93229  1.000 75.40195  ? 301 ASP   B C     1 
ATOM   5717 O O     . ASP   B 1 301 ? 77.94055  23.10967  -9.59586  1.000 72.47155  ? 301 ASP   B O     1 
ATOM   5718 C CB    . ASP   B 1 301 ? 79.33779  21.41134  -12.06621 1.000 72.31208  ? 301 ASP   B CB    1 
ATOM   5719 C CG    . ASP   B 1 301 ? 80.68702  21.11285  -12.74541 1.000 81.06035  ? 301 ASP   B CG    1 
ATOM   5720 O OD1   . ASP   B 1 301 ? 81.76046  21.27586  -12.10514 1.000 79.60806  ? 301 ASP   B OD1   1 
ATOM   5721 O OD2   . ASP   B 1 301 ? 80.66143  20.65107  -13.91780 1.000 82.18805  ? 301 ASP   B OD2   1 
ATOM   5722 N N     . PHE   B 1 302 ? 77.18546  20.97934  -9.75787  1.000 79.90735  ? 302 PHE   B N     1 
ATOM   5723 C CA    . PHE   B 1 302 ? 75.88808  21.27789  -9.16194  1.000 75.34153  ? 302 PHE   B CA    1 
ATOM   5724 C C     . PHE   B 1 302 ? 76.02137  21.69387  -7.70175  1.000 70.29870  ? 302 PHE   B C     1 
ATOM   5725 O O     . PHE   B 1 302 ? 75.43751  22.69778  -7.27287  1.000 60.23865  ? 302 PHE   B O     1 
ATOM   5726 C CB    . PHE   B 1 302 ? 74.95961  20.07203  -9.26856  1.000 76.23129  ? 302 PHE   B CB    1 
ATOM   5727 C CG    . PHE   B 1 302 ? 73.85782  20.10646  -8.25840  1.000 81.72493  ? 302 PHE   B CG    1 
ATOM   5728 C CD1   . PHE   B 1 302 ? 72.73896  20.91417  -8.46273  1.000 79.33828  ? 302 PHE   B CD1   1 
ATOM   5729 C CD2   . PHE   B 1 302 ? 73.93760  19.35990  -7.09663  1.000 81.78248  ? 302 PHE   B CD2   1 
ATOM   5730 C CE1   . PHE   B 1 302 ? 71.73000  20.97090  -7.52066  1.000 81.77411  ? 302 PHE   B CE1   1 
ATOM   5731 C CE2   . PHE   B 1 302 ? 72.92576  19.41026  -6.15358  1.000 83.74115  ? 302 PHE   B CE2   1 
ATOM   5732 C CZ    . PHE   B 1 302 ? 71.81937  20.21693  -6.36444  1.000 84.21546  ? 302 PHE   B CZ    1 
ATOM   5733 N N     . SER   B 1 303 ? 76.74426  20.90305  -6.90507  1.000 73.67229  ? 303 SER   B N     1 
ATOM   5734 C CA    . SER   B 1 303 ? 76.96514  21.30875  -5.52541  1.000 72.94978  ? 303 SER   B CA    1 
ATOM   5735 C C     . SER   B 1 303 ? 77.68985  22.64095  -5.46249  1.000 72.06347  ? 303 SER   B C     1 
ATOM   5736 O O     . SER   B 1 303 ? 77.41325  23.46734  -4.58381  1.000 70.01218  ? 303 SER   B O     1 
ATOM   5737 C CB    . SER   B 1 303 ? 77.74435  20.23215  -4.76187  1.000 72.52250  ? 303 SER   B CB    1 
ATOM   5738 O OG    . SER   B 1 303 ? 76.89203  19.15030  -4.40867  1.000 76.79447  ? 303 SER   B OG    1 
ATOM   5739 N N     . ALA   B 1 304 ? 78.60997  22.88095  -6.40259  1.000 69.90988  ? 304 ALA   B N     1 
ATOM   5740 C CA    . ALA   B 1 304 ? 79.50315  24.01675  -6.24900  1.000 66.11351  ? 304 ALA   B CA    1 
ATOM   5741 C C     . ALA   B 1 304 ? 78.82095  25.31283  -6.64271  1.000 64.03695  ? 304 ALA   B C     1 
ATOM   5742 O O     . ALA   B 1 304 ? 79.12388  26.38057  -6.08531  1.000 62.03131  ? 304 ALA   B O     1 
ATOM   5743 C CB    . ALA   B 1 304 ? 80.77924  23.78611  -7.05329  1.000 63.60755  ? 304 ALA   B CB    1 
ATOM   5744 N N     . ALA   B 1 305 ? 77.88686  25.24635  -7.57750  1.000 61.41501  ? 305 ALA   B N     1 
ATOM   5745 C CA    . ALA   B 1 305 ? 77.09866  26.43569  -7.83122  1.000 62.40161  ? 305 ALA   B CA    1 
ATOM   5746 C C     . ALA   B 1 305 ? 76.18602  26.71085  -6.64788  1.000 67.38574  ? 305 ALA   B C     1 
ATOM   5747 O O     . ALA   B 1 305 ? 76.10738  27.84699  -6.16456  1.000 69.03866  ? 305 ALA   B O     1 
ATOM   5748 C CB    . ALA   B 1 305 ? 76.31026  26.27768  -9.12651  1.000 67.49046  ? 305 ALA   B CB    1 
ATOM   5749 N N     . ALA   B 1 306 ? 75.54607  25.65921  -6.12055  1.000 66.04886  ? 306 ALA   B N     1 
ATOM   5750 C CA    . ALA   B 1 306 ? 74.62870  25.80467  -4.99358  1.000 61.09985  ? 306 ALA   B CA    1 
ATOM   5751 C C     . ALA   B 1 306 ? 75.29671  26.49443  -3.79677  1.000 63.63441  ? 306 ALA   B C     1 
ATOM   5752 O O     . ALA   B 1 306 ? 74.83719  27.54139  -3.32278  1.000 66.08315  ? 306 ALA   B O     1 
ATOM   5753 C CB    . ALA   B 1 306 ? 74.08437  24.43049  -4.61023  1.000 60.01866  ? 306 ALA   B CB    1 
ATOM   5754 N N     . SER   B 1 307 ? 76.36646  25.89691  -3.27060  1.000 62.65463  ? 307 SER   B N     1 
ATOM   5755 C CA    . SER   B 1 307 ? 77.17391  26.56856  -2.25380  1.000 68.06831  ? 307 SER   B CA    1 
ATOM   5756 C C     . SER   B 1 307 ? 77.43411  28.01854  -2.60501  1.000 66.33143  ? 307 SER   B C     1 
ATOM   5757 O O     . SER   B 1 307 ? 77.17788  28.93251  -1.80965  1.000 60.35460  ? 307 SER   B O     1 
ATOM   5758 C CB    . SER   B 1 307 ? 78.52140  25.85910  -2.08922  1.000 70.50304  ? 307 SER   B CB    1 
ATOM   5759 O OG    . SER   B 1 307 ? 79.27320  26.49320  -1.06021  1.000 74.35789  ? 307 SER   B OG    1 
ATOM   5760 N N     . ALA   B 1 308 ? 78.03812  28.22286  -3.77452  1.000 70.55563  ? 308 ALA   B N     1 
ATOM   5761 C CA    . ALA   B 1 308 ? 78.41400  29.54904  -4.21068  1.000 67.11472  ? 308 ALA   B CA    1 
ATOM   5762 C C     . ALA   B 1 308 ? 77.21260  30.47341  -4.25317  1.000 66.92175  ? 308 ALA   B C     1 
ATOM   5763 O O     . ALA   B 1 308 ? 77.34816  31.67966  -3.99612  1.000 66.67158  ? 308 ALA   B O     1 
ATOM   5764 C CB    . ALA   B 1 308 ? 79.09193  29.44755  -5.57013  1.000 62.44075  ? 308 ALA   B CB    1 
ATOM   5765 N N     . GLN   B 1 309 ? 76.02112  29.94068  -4.54069  1.000 62.89784  ? 309 GLN   B N     1 
ATOM   5766 C CA    . GLN   B 1 309 ? 74.87985  30.84187  -4.57644  1.000 64.03147  ? 309 GLN   B CA    1 
ATOM   5767 C C     . GLN   B 1 309 ? 74.54878  31.33043  -3.17199  1.000 68.90251  ? 309 GLN   B C     1 
ATOM   5768 O O     . GLN   B 1 309 ? 74.40970  32.53663  -2.95737  1.000 69.91715  ? 309 GLN   B O     1 
ATOM   5769 C CB    . GLN   B 1 309 ? 73.65446  30.20506  -5.22938  1.000 63.76361  ? 309 GLN   B CB    1 
ATOM   5770 C CG    . GLN   B 1 309 ? 73.76610  29.98959  -6.75757  1.000 65.05335  ? 309 GLN   B CG    1 
ATOM   5771 C CD    . GLN   B 1 309 ? 73.69842  31.26370  -7.60346  1.000 73.38881  ? 309 GLN   B CD    1 
ATOM   5772 O OE1   . GLN   B 1 309 ? 73.68817  32.38598  -7.08318  1.000 74.30866  ? 309 GLN   B OE1   1 
ATOM   5773 N NE2   . GLN   B 1 309 ? 73.57937  31.08150  -8.92014  1.000 68.73866  ? 309 GLN   B NE2   1 
ATOM   5774 N N     . THR   B 1 310 ? 74.46845  30.42547  -2.19119  1.000 70.17871  ? 310 THR   B N     1 
ATOM   5775 C CA    . THR   B 1 310 ? 74.18214  30.88183  -0.83491  1.000 67.12143  ? 310 THR   B CA    1 
ATOM   5776 C C     . THR   B 1 310 ? 75.15221  31.98164  -0.41486  1.000 64.75029  ? 310 THR   B C     1 
ATOM   5777 O O     . THR   B 1 310 ? 74.73885  32.95176  0.22211   1.000 67.52847  ? 310 THR   B O     1 
ATOM   5778 C CB    . THR   B 1 310 ? 74.22514  29.71650  0.16745   1.000 70.76078  ? 310 THR   B CB    1 
ATOM   5779 O OG1   . THR   B 1 310 ? 75.58721  29.34708  0.43204   1.000 74.11204  ? 310 THR   B OG1   1 
ATOM   5780 C CG2   . THR   B 1 310 ? 73.46600  28.50323  -0.37827  1.000 60.99540  ? 310 THR   B CG2   1 
ATOM   5781 N N     . LYS   B 1 311 ? 76.43661  31.87088  -0.79225  1.000 64.80847  ? 311 LYS   B N     1 
ATOM   5782 C CA    . LYS   B 1 311 ? 77.39740  32.91307  -0.42152  1.000 70.32400  ? 311 LYS   B CA    1 
ATOM   5783 C C     . LYS   B 1 311 ? 76.96720  34.26804  -0.98173  1.000 69.23213  ? 311 LYS   B C     1 
ATOM   5784 O O     . LYS   B 1 311 ? 76.98844  35.28367  -0.27444  1.000 67.94006  ? 311 LYS   B O     1 
ATOM   5785 C CB    . LYS   B 1 311 ? 78.82360  32.58777  -0.90623  1.000 63.54152  ? 311 LYS   B CB    1 
ATOM   5786 C CG    . LYS   B 1 311 ? 79.46025  31.31554  -0.35724  1.000 66.21182  ? 311 LYS   B CG    1 
ATOM   5787 C CD    . LYS   B 1 311 ? 79.05233  31.03266  1.09126   1.000 70.10553  ? 311 LYS   B CD    1 
ATOM   5788 C CE    . LYS   B 1 311 ? 80.09653  30.27045  1.92525   1.000 65.42866  ? 311 LYS   B CE    1 
ATOM   5789 N NZ    . LYS   B 1 311 ? 81.19937  31.07247  2.51444   1.000 66.10866  ? 311 LYS   B NZ    1 
ATOM   5790 N N     . ALA   B 1 312 ? 76.59275  34.30631  -2.26388  1.000 67.39774  ? 312 ALA   B N     1 
ATOM   5791 C CA    . ALA   B 1 312 ? 76.18950  35.56698  -2.87342  1.000 64.86688  ? 312 ALA   B CA    1 
ATOM   5792 C C     . ALA   B 1 312 ? 74.87801  36.04593  -2.32563  1.000 63.53289  ? 312 ALA   B C     1 
ATOM   5793 O O     . ALA   B 1 312 ? 74.58211  37.24171  -2.43791  1.000 61.08025  ? 312 ALA   B O     1 
ATOM   5794 C CB    . ALA   B 1 312 ? 76.07131  35.43821  -4.39128  1.000 66.80947  ? 312 ALA   B CB    1 
ATOM   5795 N N     . ALA   B 1 313 ? 74.07741  35.10837  -1.78999  1.000 70.07770  ? 313 ALA   B N     1 
ATOM   5796 C CA    . ALA   B 1 313 ? 72.85353  35.44041  -1.05972  1.000 68.97124  ? 313 ALA   B CA    1 
ATOM   5797 C C     . ALA   B 1 313 ? 73.12339  36.50431  -0.00652  1.000 67.71032  ? 313 ALA   B C     1 
ATOM   5798 O O     . ALA   B 1 313 ? 72.32719  37.43801  0.16452   1.000 67.70199  ? 313 ALA   B O     1 
ATOM   5799 C CB    . ALA   B 1 313 ? 72.27236  34.18020  -0.41712  1.000 62.32329  ? 313 ALA   B CB    1 
ATOM   5800 N N     . GLY   B 1 314 ? 74.26771  36.39803  0.67043   1.000 64.24045  ? 314 GLY   B N     1 
ATOM   5801 C CA    . GLY   B 1 314 ? 74.69282  37.34264  1.67571   1.000 64.56053  ? 314 GLY   B CA    1 
ATOM   5802 C C     . GLY   B 1 314 ? 74.60332  36.80021  3.07544   1.000 66.92590  ? 314 GLY   B C     1 
ATOM   5803 O O     . GLY   B 1 314 ? 75.11975  37.43366  4.00124   1.000 68.97452  ? 314 GLY   B O     1 
ATOM   5804 N N     . ILE   B 1 315 ? 73.97551  35.63283  3.23691   1.000 69.37120  ? 315 ILE   B N     1 
ATOM   5805 C CA    . ILE   B 1 315 ? 73.74419  35.04425  4.54603   1.000 66.08315  ? 315 ILE   B CA    1 
ATOM   5806 C C     . ILE   B 1 315 ? 74.95284  34.24400  5.01073   1.000 67.63872  ? 315 ILE   B C     1 
ATOM   5807 O O     . ILE   B 1 315 ? 75.27659  34.22367  6.20355   1.000 69.11053  ? 315 ILE   B O     1 
ATOM   5808 C CB    . ILE   B 1 315 ? 72.48629  34.16653  4.51282   1.000 65.40226  ? 315 ILE   B CB    1 
ATOM   5809 C CG1   . ILE   B 1 315 ? 72.73692  32.89831  3.68917   1.000 65.14029  ? 315 ILE   B CG1   1 
ATOM   5810 C CG2   . ILE   B 1 315 ? 71.31825  34.93722  3.93798   1.000 63.89389  ? 315 ILE   B CG2   1 
ATOM   5811 C CD1   . ILE   B 1 315 ? 71.51499  32.03018  3.58025   1.000 66.01541  ? 315 ILE   B CD1   1 
ATOM   5812 N N     . ALA   B 1 316 ? 75.61661  33.54625  4.09917   1.000 66.77082  ? 316 ALA   B N     1 
ATOM   5813 C CA    . ALA   B 1 316 ? 76.44896  32.43260  4.52977   1.000 61.62881  ? 316 ALA   B CA    1 
ATOM   5814 C C     . ALA   B 1 316 ? 77.88644  32.84277  4.77543   1.000 64.45196  ? 316 ALA   B C     1 
ATOM   5815 O O     . ALA   B 1 316 ? 78.78967  32.05483  4.49875   1.000 61.58179  ? 316 ALA   B O     1 
ATOM   5816 C CB    . ALA   B 1 316 ? 76.36036  31.30364  3.50782   1.000 56.01165  ? 316 ALA   B CB    1 
ATOM   5817 N N     . SER   B 1 317 ? 78.12825  34.04223  5.32505   1.000 67.00923  ? 317 SER   B N     1 
ATOM   5818 C CA    . SER   B 1 317 ? 79.45155  34.62057  5.55467   1.000 63.32040  ? 317 SER   B CA    1 
ATOM   5819 C C     . SER   B 1 317 ? 79.59278  35.08979  6.99510   1.000 63.95183  ? 317 SER   B C     1 
ATOM   5820 O O     . SER   B 1 317 ? 78.59575  35.39137  7.65137   1.000 68.27821  ? 317 SER   B O     1 
ATOM   5821 C CB    . SER   B 1 317 ? 79.69428  35.82818  4.63773   1.000 70.88464  ? 317 SER   B CB    1 
ATOM   5822 O OG    . SER   B 1 317 ? 79.47821  35.52321  3.26639   1.000 84.36661  ? 317 SER   B OG    1 
ATOM   5823 N N     . PRO   B 1 318 ? 80.81435  35.16557  7.51437   1.000 61.75046  ? 318 PRO   B N     1 
ATOM   5824 C CA    . PRO   B 1 318 ? 81.01860  35.83792  8.80287   1.000 66.22278  ? 318 PRO   B CA    1 
ATOM   5825 C C     . PRO   B 1 318 ? 80.53419  37.27356  8.77657   1.000 68.85828  ? 318 PRO   B C     1 
ATOM   5826 O O     . PRO   B 1 318 ? 80.64040  37.97226  7.77044   1.000 72.72788  ? 318 PRO   B O     1 
ATOM   5827 C CB    . PRO   B 1 318 ? 82.52895  35.76546  8.99979   1.000 58.43241  ? 318 PRO   B CB    1 
ATOM   5828 C CG    . PRO   B 1 318 ? 82.86512  34.49337  8.34744   1.000 58.59719  ? 318 PRO   B CG    1 
ATOM   5829 C CD    . PRO   B 1 318 ? 81.96531  34.32803  7.16568   1.000 57.36647  ? 318 PRO   B CD    1 
ATOM   5830 N N     . SER   B 1 319 ? 79.98937  37.72012  9.90105   1.000 72.35296  ? 319 SER   B N     1 
ATOM   5831 C CA    . SER   B 1 319 ? 79.29991  39.00203  9.86078   1.000 74.77858  ? 319 SER   B CA    1 
ATOM   5832 C C     . SER   B 1 319 ? 78.74372  39.35482  11.23741  1.000 75.78322  ? 319 SER   B C     1 
ATOM   5833 O O     . SER   B 1 319 ? 78.73747  38.54525  12.17073  1.000 70.83934  ? 319 SER   B O     1 
ATOM   5834 C CB    . SER   B 1 319 ? 78.15785  38.98629  8.84214   1.000 70.76798  ? 319 SER   B CB    1 
ATOM   5835 O OG    . SER   B 1 319 ? 77.36256  37.82411  9.00206   1.000 66.79790  ? 319 SER   B OG    1 
ATOM   5836 N N     . HIS   B 1 320 ? 78.29131  40.60271  11.34221  1.000 78.87950  ? 320 HIS   B N     1 
ATOM   5837 C CA    . HIS   B 1 320 ? 77.40674  41.02488  12.41300  1.000 70.65597  ? 320 HIS   B CA    1 
ATOM   5838 C C     . HIS   B 1 320 ? 76.00445  40.54105  12.04830  1.000 73.28351  ? 320 HIS   B C     1 
ATOM   5839 O O     . HIS   B 1 320 ? 75.48311  40.90564  10.99241  1.000 78.48431  ? 320 HIS   B O     1 
ATOM   5840 C CB    . HIS   B 1 320 ? 77.42569  42.54483  12.54007  1.000 64.90622  ? 320 HIS   B CB    1 
ATOM   5841 C CG    . HIS   B 1 320 ? 78.74625  43.11379  12.96043  1.000 73.47280  ? 320 HIS   B CG    1 
ATOM   5842 N ND1   . HIS   B 1 320 ? 79.22791  43.02567  14.24963  1.000 77.64297  ? 320 HIS   B ND1   1 
ATOM   5843 C CD2   . HIS   B 1 320 ? 79.66286  43.83861  12.27227  1.000 77.74293  ? 320 HIS   B CD2   1 
ATOM   5844 C CE1   . HIS   B 1 320 ? 80.39881  43.63939  14.33034  1.000 77.38044  ? 320 HIS   B CE1   1 
ATOM   5845 N NE2   . HIS   B 1 320 ? 80.68373  44.14682  13.14507  1.000 75.37414  ? 320 HIS   B NE2   1 
ATOM   5846 N N     . PHE   B 1 321 ? 75.39606  39.71536  12.89317  1.000 74.03265  ? 321 PHE   B N     1 
ATOM   5847 C CA    . PHE   B 1 321 ? 74.10696  39.12074  12.55456  1.000 71.98864  ? 321 PHE   B CA    1 
ATOM   5848 C C     . PHE   B 1 321 ? 73.51223  38.47560  13.80663  1.000 74.74447  ? 321 PHE   B C     1 
ATOM   5849 O O     . PHE   B 1 321 ? 74.17405  38.36512  14.84598  1.000 76.33041  ? 321 PHE   B O     1 
ATOM   5850 C CB    . PHE   B 1 321 ? 74.26283  38.08298  11.44788  1.000 70.98851  ? 321 PHE   B CB    1 
ATOM   5851 C CG    . PHE   B 1 321 ? 74.85866  36.77727  11.92670  1.000 73.16188  ? 321 PHE   B CG    1 
ATOM   5852 C CD1   . PHE   B 1 321 ? 76.23647  36.60979  12.01367  1.000 69.94061  ? 321 PHE   B CD1   1 
ATOM   5853 C CD2   . PHE   B 1 321 ? 74.03087  35.70551  12.26208  1.000 68.70825  ? 321 PHE   B CD2   1 
ATOM   5854 C CE1   . PHE   B 1 321 ? 76.77639  35.40494  12.46373  1.000 69.06656  ? 321 PHE   B CE1   1 
ATOM   5855 C CE2   . PHE   B 1 321 ? 74.56302  34.51644  12.69015  1.000 67.51904  ? 321 PHE   B CE2   1 
ATOM   5856 C CZ    . PHE   B 1 321 ? 75.93971  34.36060  12.79718  1.000 69.30951  ? 321 PHE   B CZ    1 
ATOM   5857 N N     . TYR   B 1 322 ? 72.25428  38.03308  13.68547  1.000 69.45968  ? 322 TYR   B N     1 
ATOM   5858 C CA    . TYR   B 1 322 ? 71.57233  37.25195  14.71362  1.000 74.71988  ? 322 TYR   B CA    1 
ATOM   5859 C C     . TYR   B 1 322 ? 70.59765  36.35547  13.97732  1.000 70.69161  ? 322 TYR   B C     1 
ATOM   5860 O O     . TYR   B 1 322 ? 70.18378  36.68548  12.87075  1.000 73.38983  ? 322 TYR   B O     1 
ATOM   5861 C CB    . TYR   B 1 322 ? 70.86043  38.13548  15.76486  1.000 80.90836  ? 322 TYR   B CB    1 
ATOM   5862 C CG    . TYR   B 1 322 ? 70.10376  37.35795  16.84531  1.000 85.97474  ? 322 TYR   B CG    1 
ATOM   5863 C CD1   . TYR   B 1 322 ? 70.69039  36.25880  17.46787  1.000 92.35866  ? 322 TYR   B CD1   1 
ATOM   5864 C CD2   . TYR   B 1 322 ? 68.84174  37.75875  17.29225  1.000 89.74443  ? 322 TYR   B CD2   1 
ATOM   5865 C CE1   . TYR   B 1 322 ? 70.02444  35.54649  18.46267  1.000 96.83866  ? 322 TYR   B CE1   1 
ATOM   5866 C CE2   . TYR   B 1 322 ? 68.16458  37.04641  18.30208  1.000 91.00669  ? 322 TYR   B CE2   1 
ATOM   5867 C CZ    . TYR   B 1 322 ? 68.76886  35.94012  18.88183  1.000 91.21866  ? 322 TYR   B CZ    1 
ATOM   5868 O OH    . TYR   B 1 322 ? 68.12956  35.22126  19.87753  1.000 92.31231  ? 322 TYR   B OH    1 
ATOM   5869 N N     . ALA   B 1 323 ? 70.25498  35.21160  14.56810  1.000 70.60361  ? 323 ALA   B N     1 
ATOM   5870 C CA    . ALA   B 1 323 ? 69.57801  34.20517  13.76311  1.000 69.86817  ? 323 ALA   B CA    1 
ATOM   5871 C C     . ALA   B 1 323 ? 69.11465  33.06343  14.64525  1.000 72.98322  ? 323 ALA   B C     1 
ATOM   5872 O O     . ALA   B 1 323 ? 69.74415  32.75584  15.66282  1.000 74.12283  ? 323 ALA   B O     1 
ATOM   5873 C CB    . ALA   B 1 323 ? 70.49322  33.67305  12.65666  1.000 71.49578  ? 323 ALA   B CB    1 
ATOM   5874 N N     . LYS   B 1 324 ? 68.02213  32.42822  14.21844  1.000 66.47148  ? 324 LYS   B N     1 
ATOM   5875 C CA    . LYS   B 1 324 ? 67.21784  31.56427  15.06807  1.000 68.98204  ? 324 LYS   B CA    1 
ATOM   5876 C C     . LYS   B 1 324 ? 66.52750  30.54949  14.18219  1.000 74.29344  ? 324 LYS   B C     1 
ATOM   5877 O O     . LYS   B 1 324 ? 66.56304  30.64223  12.95256  1.000 77.93893  ? 324 LYS   B O     1 
ATOM   5878 C CB    . LYS   B 1 324 ? 66.17572  32.35664  15.87692  1.000 76.99913  ? 324 LYS   B CB    1 
ATOM   5879 C CG    . LYS   B 1 324 ? 66.72738  33.61526  16.60452  1.000 86.24964  ? 324 LYS   B CG    1 
ATOM   5880 C CD    . LYS   B 1 324 ? 65.62890  34.55281  17.09459  1.000 82.46070  ? 324 LYS   B CD    1 
ATOM   5881 C CE    . LYS   B 1 324 ? 64.91558  34.01955  18.29663  1.000 81.56396  ? 324 LYS   B CE    1 
ATOM   5882 N NZ    . LYS   B 1 324 ? 65.67367  34.37999  19.50569  1.000 82.13205  ? 324 LYS   B NZ    1 
ATOM   5883 N N     . SER   B 1 325 ? 65.89227  29.57352  14.81461  1.000 71.98437  ? 325 SER   B N     1 
ATOM   5884 C CA    . SER   B 1 325 ? 65.26033  28.50137  14.06868  1.000 74.76666  ? 325 SER   B CA    1 
ATOM   5885 C C     . SER   B 1 325 ? 64.00955  28.06063  14.81818  1.000 77.46105  ? 325 SER   B C     1 
ATOM   5886 O O     . SER   B 1 325 ? 63.72584  28.52910  15.93319  1.000 71.52449  ? 325 SER   B O     1 
ATOM   5887 C CB    . SER   B 1 325 ? 66.23321  27.32157  13.81441  1.000 72.19426  ? 325 SER   B CB    1 
ATOM   5888 O OG    . SER   B 1 325 ? 66.81508  26.81596  15.01375  1.000 72.56151  ? 325 SER   B OG    1 
ATOM   5889 N N     . LEU   B 1 326 ? 63.25250  27.17130  14.16074  1.000 73.43166  ? 326 LEU   B N     1 
ATOM   5890 C CA    . LEU   B 1 326 ? 62.00041  26.58647  14.62259  1.000 75.27522  ? 326 LEU   B CA    1 
ATOM   5891 C C     . LEU   B 1 326 ? 61.70936  25.39795  13.71612  1.000 77.31101  ? 326 LEU   B C     1 
ATOM   5892 O O     . LEU   B 1 326 ? 61.93107  25.48366  12.51135  1.000 78.65334  ? 326 LEU   B O     1 
ATOM   5893 C CB    . LEU   B 1 326 ? 60.83978  27.60361  14.57848  1.000 80.81730  ? 326 LEU   B CB    1 
ATOM   5894 C CG    . LEU   B 1 326 ? 60.87480  28.85702  15.49269  1.000 84.32629  ? 326 LEU   B CG    1 
ATOM   5895 C CD1   . LEU   B 1 326 ? 59.86125  29.97152  15.15173  1.000 83.16769  ? 326 LEU   B CD1   1 
ATOM   5896 C CD2   . LEU   B 1 326 ? 60.68631  28.43374  16.93905  1.000 83.67594  ? 326 LEU   B CD2   1 
ATOM   5897 N N     . VAL   B 1 327 ? 61.24868  24.28591  14.28142  1.000 83.36697  ? 327 VAL   B N     1 
ATOM   5898 C CA    . VAL   B 1 327 ? 60.83253  23.14650  13.46459  1.000 87.59626  ? 327 VAL   B CA    1 
ATOM   5899 C C     . VAL   B 1 327 ? 59.30970  23.13466  13.41518  1.000 93.47268  ? 327 VAL   B C     1 
ATOM   5900 O O     . VAL   B 1 327 ? 58.63962  23.63142  14.33033  1.000 99.63546  ? 327 VAL   B O     1 
ATOM   5901 C CB    . VAL   B 1 327 ? 61.34126  21.78545  13.98911  1.000 93.72163  ? 327 VAL   B CB    1 
ATOM   5902 C CG1   . VAL   B 1 327 ? 60.90721  20.64717  13.02837  1.000 91.32867  ? 327 VAL   B CG1   1 
ATOM   5903 C CG2   . VAL   B 1 327 ? 62.82812  21.80171  14.23864  1.000 84.12532  ? 327 VAL   B CG2   1 
ATOM   5904 N N     . PHE   B 1 328 ? 58.75685  22.54207  12.35239  1.000 89.53221  ? 328 PHE   B N     1 
ATOM   5905 C CA    . PHE   B 1 328 ? 57.32072  22.51347  12.11150  1.000 84.43652  ? 328 PHE   B CA    1 
ATOM   5906 C C     . PHE   B 1 328 ? 56.97355  21.18336  11.47971  1.000 93.16695  ? 328 PHE   B C     1 
ATOM   5907 O O     . PHE   B 1 328 ? 57.83592  20.48315  10.93914  1.000 96.34866  ? 328 PHE   B O     1 
ATOM   5908 C CB    . PHE   B 1 328 ? 56.85594  23.67431  11.21879  1.000 75.44172  ? 328 PHE   B CB    1 
ATOM   5909 C CG    . PHE   B 1 328 ? 56.91213  25.01134  11.89056  1.000 75.33652  ? 328 PHE   B CG    1 
ATOM   5910 C CD1   . PHE   B 1 328 ? 58.10519  25.66761  12.04921  1.000 77.42547  ? 328 PHE   B CD1   1 
ATOM   5911 C CD2   . PHE   B 1 328 ? 55.76008  25.63106  12.33370  1.000 92.72037  ? 328 PHE   B CD2   1 
ATOM   5912 C CE1   . PHE   B 1 328 ? 58.16784  26.90363  12.68216  1.000 86.32132  ? 328 PHE   B CE1   1 
ATOM   5913 C CE2   . PHE   B 1 328 ? 55.80087  26.88041  12.96288  1.000 97.25670  ? 328 PHE   B CE2   1 
ATOM   5914 C CZ    . PHE   B 1 328 ? 57.00874  27.51705  13.13154  1.000 94.38080  ? 328 PHE   B CZ    1 
ATOM   5915 N N     . ASN   B 1 329 ? 55.68122  20.87372  11.50452  1.000 103.36152 ? 329 ASN   B N     1 
ATOM   5916 C CA    . ASN   B 1 329 ? 55.17473  19.51317  11.37142  1.000 104.72025 ? 329 ASN   B CA    1 
ATOM   5917 C C     . ASN   B 1 329 ? 53.65628  19.57667  11.20133  1.000 105.73060 ? 329 ASN   B C     1 
ATOM   5918 O O     . ASN   B 1 329 ? 53.02970  20.60062  11.51887  1.000 100.83392 ? 329 ASN   B O     1 
ATOM   5919 C CB    . ASN   B 1 329 ? 55.56417  18.70582  12.60175  1.000 102.04770 ? 329 ASN   B CB    1 
ATOM   5920 C CG    . ASN   B 1 329 ? 55.39094  19.51196  13.87924  1.000 97.36911  ? 329 ASN   B CG    1 
ATOM   5921 O OD1   . ASN   B 1 329 ? 54.30019  20.01355  14.16866  1.000 95.82846  ? 329 ASN   B OD1   1 
ATOM   5922 N ND2   . ASN   B 1 329 ? 56.47620  19.69209  14.61671  1.000 94.52194  ? 329 ASN   B ND2   1 
ATOM   5923 N N     . GLN   B 1 330 ? 53.07828  18.47366  10.69424  1.000 107.40016 ? 330 GLN   B N     1 
ATOM   5924 C CA    . GLN   B 1 330 ? 51.65423  18.40104  10.35287  1.000 101.65951 ? 330 GLN   B CA    1 
ATOM   5925 C C     . GLN   B 1 330 ? 50.81655  19.13098  11.39973  1.000 106.77021 ? 330 GLN   B C     1 
ATOM   5926 O O     . GLN   B 1 330 ? 49.81917  19.77505  11.05973  1.000 115.92866 ? 330 GLN   B O     1 
ATOM   5927 C CB    . GLN   B 1 330 ? 51.16197  16.95218  10.24891  1.000 88.26861  ? 330 GLN   B CB    1 
ATOM   5928 C CG    . GLN   B 1 330 ? 51.78517  16.10943  9.16262   1.000 91.58651  ? 330 GLN   B CG    1 
ATOM   5929 C CD    . GLN   B 1 330 ? 53.27243  15.88509  9.40840   1.000 104.84578 ? 330 GLN   B CD    1 
ATOM   5930 O OE1   . GLN   B 1 330 ? 53.80100  16.24846  10.46588  1.000 103.51441 ? 330 GLN   B OE1   1 
ATOM   5931 N NE2   . GLN   B 1 330 ? 53.95138  15.27983  8.44209   1.000 105.51405 ? 330 GLN   B NE2   1 
ATOM   5932 N N     . GLN   B 1 331 ? 51.23769  19.05789  12.67500  1.000 104.04631 ? 331 GLN   B N     1 
ATOM   5933 C CA    . GLN   B 1 331 ? 50.41264  19.50276  13.79798  1.000 106.59294 ? 331 GLN   B CA    1 
ATOM   5934 C C     . GLN   B 1 331 ? 50.54335  21.00188  14.10473  1.000 115.71919 ? 331 GLN   B C     1 
ATOM   5935 O O     . GLN   B 1 331 ? 49.58091  21.60076  14.61012  1.000 117.49220 ? 331 GLN   B O     1 
ATOM   5936 C CB    . GLN   B 1 331 ? 50.74127  18.68488  15.05765  1.000 106.41866 ? 331 GLN   B CB    1 
ATOM   5937 C CG    . GLN   B 1 331 ? 50.09429  17.28590  15.17037  1.000 108.08866 ? 331 GLN   B CG    1 
ATOM   5938 C CD    . GLN   B 1 331 ? 50.56099  16.29301  14.11199  1.000 104.30500 ? 331 GLN   B CD    1 
ATOM   5939 O OE1   . GLN   B 1 331 ? 51.72704  15.89744  14.08038  1.000 101.69635 ? 331 GLN   B OE1   1 
ATOM   5940 N NE2   . GLN   B 1 331 ? 49.63797  15.86497  13.25930  1.000 104.88029 ? 331 GLN   B NE2   1 
ATOM   5941 N N     . THR   B 1 332 ? 51.70011  21.63788  13.84323  1.000 110.14242 ? 332 THR   B N     1 
ATOM   5942 C CA    . THR   B 1 332 ? 51.79512  23.08859  14.02651  1.000 106.30982 ? 332 THR   B CA    1 
ATOM   5943 C C     . THR   B 1 332 ? 51.91707  23.84020  12.69825  1.000 100.45474 ? 332 THR   B C     1 
ATOM   5944 O O     . THR   B 1 332 ? 52.25590  25.02706  12.70279  1.000 97.75875  ? 332 THR   B O     1 
ATOM   5945 C CB    . THR   B 1 332 ? 52.93886  23.48194  14.98163  1.000 97.08019  ? 332 THR   B CB    1 
ATOM   5946 O OG1   . THR   B 1 332 ? 54.19356  23.43961  14.31513  1.000 96.43859  ? 332 THR   B OG1   1 
ATOM   5947 C CG2   . THR   B 1 332 ? 53.01661  22.55226  16.15139  1.000 102.37544 ? 332 THR   B CG2   1 
ATOM   5948 N N     . LEU   B 1 333 ? 51.61948  23.17305  11.57319  1.000 102.29057 ? 333 LEU   B N     1 
ATOM   5949 C CA    . LEU   B 1 333 ? 51.55043  23.76708  10.23365  1.000 102.12356 ? 333 LEU   B CA    1 
ATOM   5950 C C     . LEU   B 1 333 ? 50.87416  25.14034  10.28630  1.000 108.80711 ? 333 LEU   B C     1 
ATOM   5951 O O     . LEU   B 1 333 ? 49.65566  25.19903  10.46870  1.000 115.51702 ? 333 LEU   B O     1 
ATOM   5952 C CB    . LEU   B 1 333 ? 50.79835  22.81284  9.28781   1.000 88.13069  ? 333 LEU   B CB    1 
ATOM   5953 C CG    . LEU   B 1 333 ? 51.56811  21.55289  8.87571   1.000 84.13461  ? 333 LEU   B CG    1 
ATOM   5954 C CD1   . LEU   B 1 333 ? 50.76493  20.46798  8.15424   1.000 85.14852  ? 333 LEU   B CD1   1 
ATOM   5955 C CD2   . LEU   B 1 333 ? 52.67583  21.99266  8.00459   1.000 92.68070  ? 333 LEU   B CD2   1 
ATOM   5956 N N     . ILE   B 1 334 ? 51.62998  26.23345  10.11046  1.000 109.19693 ? 334 ILE   B N     1 
ATOM   5957 C CA    . ILE   B 1 334 ? 51.15332  27.54049  10.60732  1.000 119.20866 ? 334 ILE   B CA    1 
ATOM   5958 C C     . ILE   B 1 334 ? 49.79586  27.88387  10.01203  1.000 129.59866 ? 334 ILE   B C     1 
ATOM   5959 O O     . ILE   B 1 334 ? 49.52400  27.56746  8.82627   1.000 124.08237 ? 334 ILE   B O     1 
ATOM   5960 C CB    . ILE   B 1 334 ? 52.15688  28.68129  10.35545  1.000 117.56866 ? 334 ILE   B CB    1 
ATOM   5961 C CG1   . ILE   B 1 334 ? 53.25246  28.70330  11.42527  1.000 112.04704 ? 334 ILE   B CG1   1 
ATOM   5962 C CG2   . ILE   B 1 334 ? 51.44312  30.02654  10.37399  1.000 122.79866 ? 334 ILE   B CG2   1 
ATOM   5963 C CD1   . ILE   B 1 334 ? 54.37978  29.67822  11.15178  1.000 99.32866  ? 334 ILE   B CD1   1 
ATOM   5964 N N     . PRO   B 1 335 ? 48.92063  28.54189  10.76724  1.000 126.55866 ? 335 PRO   B N     1 
ATOM   5965 C CA    . PRO   B 1 335 ? 47.56467  28.78961  10.28734  1.000 123.84131 ? 335 PRO   B CA    1 
ATOM   5966 C C     . PRO   B 1 335 ? 47.53447  29.97936  9.34401   1.000 120.12096 ? 335 PRO   B C     1 
ATOM   5967 O O     . PRO   B 1 335 ? 48.46481  30.78529  9.25735   1.000 113.54594 ? 335 PRO   B O     1 
ATOM   5968 C CB    . PRO   B 1 335 ? 46.77264  29.08104  11.57174  1.000 121.22851 ? 335 PRO   B CB    1 
ATOM   5969 C CG    . PRO   B 1 335 ? 47.77123  28.99696  12.72486  1.000 122.30866 ? 335 PRO   B CG    1 
ATOM   5970 C CD    . PRO   B 1 335 ? 49.14145  29.02082  12.13879  1.000 123.38866 ? 335 PRO   B CD    1 
ATOM   5971 N N     . ASP   B 1 336 ? 46.42094  30.07260  8.62552   1.000 123.24816 ? 336 ASP   B N     1 
ATOM   5972 C CA    . ASP   B 1 336 ? 46.29008  31.12554  7.63138   1.000 117.70325 ? 336 ASP   B CA    1 
ATOM   5973 C C     . ASP   B 1 336 ? 46.15556  32.48600  8.31396   1.000 113.68503 ? 336 ASP   B C     1 
ATOM   5974 O O     . ASP   B 1 336 ? 46.70347  33.48942  7.83426   1.000 110.79440 ? 336 ASP   B O     1 
ATOM   5975 C CB    . ASP   B 1 336 ? 45.09112  30.82899  6.72474   1.000 112.67224 ? 336 ASP   B CB    1 
ATOM   5976 C CG    . ASP   B 1 336 ? 45.31190  29.59892  5.84377   1.000 117.98617 ? 336 ASP   B CG    1 
ATOM   5977 O OD1   . ASP   B 1 336 ? 46.47009  29.13377  5.73455   1.000 120.92479 ? 336 ASP   B OD1   1 
ATOM   5978 O OD2   . ASP   B 1 336 ? 44.33373  29.11787  5.23125   1.000 124.00710 ? 336 ASP   B OD2   1 
ATOM   5979 N N     . ASP   B 1 337 ? 45.45805  32.52612  9.45892   1.000 115.44830 ? 337 ASP   B N     1 
ATOM   5980 C CA    . ASP   B 1 337 ? 45.22210  33.79326  10.15708  1.000 120.12527 ? 337 ASP   B CA    1 
ATOM   5981 C C     . ASP   B 1 337 ? 46.53453  34.45277  10.58103  1.000 118.40462 ? 337 ASP   B C     1 
ATOM   5982 O O     . ASP   B 1 337 ? 46.77256  35.63390  10.29383  1.000 111.81091 ? 337 ASP   B O     1 
ATOM   5983 C CB    . ASP   B 1 337 ? 44.29450  33.58607  11.37149  1.000 117.53964 ? 337 ASP   B CB    1 
ATOM   5984 C CG    . ASP   B 1 337 ? 44.89418  32.67318  12.45532  1.000 122.87433 ? 337 ASP   B CG    1 
ATOM   5985 O OD1   . ASP   B 1 337 ? 44.80558  31.43101  12.31975  1.000 124.26915 ? 337 ASP   B OD1   1 
ATOM   5986 O OD2   . ASP   B 1 337 ? 45.45227  33.19638  13.44879  1.000 120.77672 ? 337 ASP   B OD2   1 
ATOM   5987 N N     . ALA   B 1 338 ? 47.39765  33.70033  11.27846  1.000 120.34978 ? 338 ALA   B N     1 
ATOM   5988 C CA    . ALA   B 1 338 ? 48.67191  34.23652  11.74639  1.000 111.37132 ? 338 ALA   B CA    1 
ATOM   5989 C C     . ALA   B 1 338 ? 49.64410  34.45652  10.58780  1.000 117.02656 ? 338 ALA   B C     1 
ATOM   5990 O O     . ALA   B 1 338 ? 50.25662  35.52563  10.48882  1.000 114.61351 ? 338 ALA   B O     1 
ATOM   5991 C CB    . ALA   B 1 338 ? 49.27526  33.30311  12.79966  1.000 109.59003 ? 338 ALA   B CB    1 
ATOM   5992 N N     . ALA   B 1 339 ? 49.79212  33.46142  9.69219   1.000 118.60643 ? 339 ALA   B N     1 
ATOM   5993 C CA    . ALA   B 1 339 ? 50.66393  33.55880  8.51686   1.000 110.74859 ? 339 ALA   B CA    1 
ATOM   5994 C C     . ALA   B 1 339 ? 50.64236  34.95993  7.91384   1.000 110.61778 ? 339 ALA   B C     1 
ATOM   5995 O O     . ALA   B 1 339 ? 51.67688  35.48872  7.49079   1.000 108.26071 ? 339 ALA   B O     1 
ATOM   5996 C CB    . ALA   B 1 339 ? 50.25842  32.53287  7.45451   1.000 106.37693 ? 339 ALA   B CB    1 
ATOM   5997 N N     . GLU   B 1 340 ? 49.45857  35.56817  7.88435   1.000 109.69243 ? 340 GLU   B N     1 
ATOM   5998 C CA    . GLU   B 1 340 ? 49.32603  36.95498  7.45459   1.000 115.40079 ? 340 GLU   B CA    1 
ATOM   5999 C C     . GLU   B 1 340 ? 50.06390  37.91388  8.38585   1.000 110.48845 ? 340 GLU   B C     1 
ATOM   6000 O O     . GLU   B 1 340 ? 50.83120  38.78107  7.93577   1.000 102.72780 ? 340 GLU   B O     1 
ATOM   6001 C CB    . GLU   B 1 340 ? 47.84328  37.31465  7.40081   1.000 123.10926 ? 340 GLU   B CB    1 
ATOM   6002 C CG    . GLU   B 1 340 ? 47.22053  37.04596  6.06909   1.000 128.50220 ? 340 GLU   B CG    1 
ATOM   6003 C CD    . GLU   B 1 340 ? 47.69110  38.03848  5.03631   1.000 134.00866 ? 340 GLU   B CD    1 
ATOM   6004 O OE1   . GLU   B 1 340 ? 48.32366  39.04393  5.43839   1.000 142.82866 ? 340 GLU   B OE1   1 
ATOM   6005 O OE2   . GLU   B 1 340 ? 47.42508  37.82029  3.83344   1.000 137.38866 ? 340 GLU   B OE2   1 
ATOM   6006 N N     . GLU   B 1 341 ? 49.79071  37.80803  9.69494   1.000 110.10989 ? 341 GLU   B N     1 
ATOM   6007 C CA    . GLU   B 1 341 ? 50.40133  38.71545  10.66587  1.000 109.10706 ? 341 GLU   B CA    1 
ATOM   6008 C C     . GLU   B 1 341 ? 51.91482  38.69964  10.52611  1.000 106.07679 ? 341 GLU   B C     1 
ATOM   6009 O O     . GLU   B 1 341 ? 52.57493  39.73743  10.64117  1.000 105.36130 ? 341 GLU   B O     1 
ATOM   6010 C CB    . GLU   B 1 341 ? 50.00623  38.33032  12.09780  1.000 108.39795 ? 341 GLU   B CB    1 
ATOM   6011 C CG    . GLU   B 1 341 ? 48.51208  38.19677  12.39475  1.000 107.47618 ? 341 GLU   B CG    1 
ATOM   6012 C CD    . GLU   B 1 341 ? 47.70151  39.36687  11.90950  1.000 99.82332  ? 341 GLU   B CD    1 
ATOM   6013 O OE1   . GLU   B 1 341 ? 47.97706  40.51388  12.32891  1.000 94.78539  ? 341 GLU   B OE1   1 
ATOM   6014 O OE2   . GLU   B 1 341 ? 46.78007  39.12289  11.10576  1.000 96.23189  ? 341 GLU   B OE2   1 
ATOM   6015 N N     . VAL   B 1 342 ? 52.47567  37.51691  10.30011  1.000 104.15510 ? 342 VAL   B N     1 
ATOM   6016 C CA    . VAL   B 1 342 ? 53.87467  37.31399  9.95000   1.000 102.08624 ? 342 VAL   B CA    1 
ATOM   6017 C C     . VAL   B 1 342 ? 54.35569  38.39798  8.99027   1.000 101.03135 ? 342 VAL   B C     1 
ATOM   6018 O O     . VAL   B 1 342 ? 55.20302  39.24177  9.32012   1.000 87.81405  ? 342 VAL   B O     1 
ATOM   6019 C CB    . VAL   B 1 342 ? 54.03341  35.92330  9.30308   1.000 105.67133 ? 342 VAL   B CB    1 
ATOM   6020 C CG1   . VAL   B 1 342 ? 55.44793  35.71259  8.80173   1.000 99.35866  ? 342 VAL   B CG1   1 
ATOM   6021 C CG2   . VAL   B 1 342 ? 53.55485  34.81759  10.24944  1.000 107.59380 ? 342 VAL   B CG2   1 
ATOM   6022 N N     . PHE   B 1 343 ? 53.80405  38.35945  7.77530   1.000 104.46409 ? 343 PHE   B N     1 
ATOM   6023 C CA    . PHE   B 1 343 ? 54.30613  39.17133  6.68035   1.000 98.48103  ? 343 PHE   B CA    1 
ATOM   6024 C C     . PHE   B 1 343 ? 53.96412  40.64228  6.89841   1.000 95.49936  ? 343 PHE   B C     1 
ATOM   6025 O O     . PHE   B 1 343 ? 54.74733  41.52976  6.53385   1.000 92.83350  ? 343 PHE   B O     1 
ATOM   6026 C CB    . PHE   B 1 343 ? 53.70919  38.63880  5.38940   1.000 99.09263  ? 343 PHE   B CB    1 
ATOM   6027 C CG    . PHE   B 1 343 ? 54.15863  37.23803  5.03428   1.000 98.20313  ? 343 PHE   B CG    1 
ATOM   6028 C CD1   . PHE   B 1 343 ? 55.36873  37.00816  4.40253   1.000 94.46726  ? 343 PHE   B CD1   1 
ATOM   6029 C CD2   . PHE   B 1 343 ? 53.34716  36.14908  5.32192   1.000 100.10179 ? 343 PHE   B CD2   1 
ATOM   6030 C CE1   . PHE   B 1 343 ? 55.75153  35.71777  4.06531   1.000 91.77256  ? 343 PHE   B CE1   1 
ATOM   6031 C CE2   . PHE   B 1 343 ? 53.72456  34.86029  4.99062   1.000 100.39044 ? 343 PHE   B CE2   1 
ATOM   6032 C CZ    . PHE   B 1 343 ? 54.92166  34.64071  4.35950   1.000 95.48106  ? 343 PHE   B CZ    1 
ATOM   6033 N N     . LYS   B 1 344 ? 52.79650  40.90109  7.49681   1.000 93.87314  ? 344 LYS   B N     1 
ATOM   6034 C CA    . LYS   B 1 344 ? 52.49079  42.23427  8.00030   1.000 99.21845  ? 344 LYS   B CA    1 
ATOM   6035 C C     . LYS   B 1 344 ? 53.52970  42.70541  9.02429   1.000 97.31130  ? 344 LYS   B C     1 
ATOM   6036 O O     . LYS   B 1 344 ? 53.85793  43.89734  9.08213   1.000 91.77300  ? 344 LYS   B O     1 
ATOM   6037 C CB    . LYS   B 1 344 ? 51.08543  42.24509  8.60757   1.000 99.88866  ? 344 LYS   B CB    1 
ATOM   6038 N N     . TYR   B 1 345 ? 54.04035  41.77838  9.85080   1.000 104.19320 ? 345 TYR   B N     1 
ATOM   6039 C CA    . TYR   B 1 345 ? 55.08960  42.06874  10.83795  1.000 97.42309  ? 345 TYR   B CA    1 
ATOM   6040 C C     . TYR   B 1 345 ? 56.43907  42.30210  10.17324  1.000 94.42965  ? 345 TYR   B C     1 
ATOM   6041 O O     . TYR   B 1 345 ? 57.18845  43.20679  10.56973  1.000 84.01590  ? 345 TYR   B O     1 
ATOM   6042 C CB    . TYR   B 1 345 ? 55.17936  40.90542  11.83901  1.000 98.05560  ? 345 TYR   B CB    1 
ATOM   6043 C CG    . TYR   B 1 345 ? 56.33933  40.95774  12.81212  1.000 96.22329  ? 345 TYR   B CG    1 
ATOM   6044 C CD1   . TYR   B 1 345 ? 57.59056  40.47067  12.44992  1.000 99.34172  ? 345 TYR   B CD1   1 
ATOM   6045 C CD2   . TYR   B 1 345 ? 56.18900  41.48015  14.08244  1.000 98.67342  ? 345 TYR   B CD2   1 
ATOM   6046 C CE1   . TYR   B 1 345 ? 58.65662  40.51346  13.31619  1.000 96.76050  ? 345 TYR   B CE1   1 
ATOM   6047 C CE2   . TYR   B 1 345 ? 57.25036  41.52535  14.95570  1.000 96.69043  ? 345 TYR   B CE2   1 
ATOM   6048 C CZ    . TYR   B 1 345 ? 58.47735  41.04125  14.56585  1.000 94.77497  ? 345 TYR   B CZ    1 
ATOM   6049 O OH    . TYR   B 1 345 ? 59.52119  41.09089  15.44959  1.000 98.56382  ? 345 TYR   B OH    1 
ATOM   6050 N N     . LEU   B 1 346 ? 56.78523  41.43399  9.20538   1.000 94.12866  ? 346 LEU   B N     1 
ATOM   6051 C CA    . LEU   B 1 346 ? 57.98267  41.61601  8.38763   1.000 90.69281  ? 346 LEU   B CA    1 
ATOM   6052 C C     . LEU   B 1 346 ? 57.99324  42.97472  7.71959   1.000 94.07165  ? 346 LEU   B C     1 
ATOM   6053 O O     . LEU   B 1 346 ? 58.99361  43.70577  7.78245   1.000 91.79186  ? 346 LEU   B O     1 
ATOM   6054 C CB    . LEU   B 1 346 ? 58.04765  40.53717  7.32231   1.000 82.50287  ? 346 LEU   B CB    1 
ATOM   6055 C CG    . LEU   B 1 346 ? 58.39016  39.22291  7.97240   1.000 81.43464  ? 346 LEU   B CG    1 
ATOM   6056 C CD1   . LEU   B 1 346 ? 58.23137  38.06728  6.99673   1.000 76.11006  ? 346 LEU   B CD1   1 
ATOM   6057 C CD2   . LEU   B 1 346 ? 59.79563  39.34850  8.53659   1.000 79.61865  ? 346 LEU   B CD2   1 
ATOM   6058 N N     . ALA   B 1 347 ? 56.88154  43.30100  7.05762   1.000 95.26155  ? 347 ALA   B N     1 
ATOM   6059 C CA    . ALA   B 1 347 ? 56.61566  44.53074  6.33440   1.000 97.42942  ? 347 ALA   B CA    1 
ATOM   6060 C C     . ALA   B 1 347 ? 56.53099  45.77920  7.22248   1.000 97.79603  ? 347 ALA   B C     1 
ATOM   6061 O O     . ALA   B 1 347 ? 56.66465  46.89431  6.70146   1.000 97.52578  ? 347 ALA   B O     1 
ATOM   6062 C CB    . ALA   B 1 347 ? 55.30817  44.34837  5.55550   1.000 89.79199  ? 347 ALA   B CB    1 
ATOM   6063 N N     . THR   B 1 348 ? 56.32203  45.63924  8.53033   1.000 98.02047  ? 348 THR   B N     1 
ATOM   6064 C CA    . THR   B 1 348 ? 55.97559  46.75913  9.40040   1.000 99.02484  ? 348 THR   B CA    1 
ATOM   6065 C C     . THR   B 1 348 ? 56.92212  46.98134  10.59145  1.000 98.94440  ? 348 THR   B C     1 
ATOM   6066 O O     . THR   B 1 348 ? 57.07362  48.12681  11.03505  1.000 96.87473  ? 348 THR   B O     1 
ATOM   6067 C CB    . THR   B 1 348 ? 54.51070  46.58868  9.87610   1.000 100.91866 ? 348 THR   B CB    1 
ATOM   6068 O OG1   . THR   B 1 348 ? 54.30325  45.25221  10.35341  1.000 104.07866 ? 348 THR   B OG1   1 
ATOM   6069 C CG2   . THR   B 1 348 ? 53.52658  46.84476  8.74501   1.000 100.29866 ? 348 THR   B CG2   1 
ATOM   6070 N N     . THR   B 1 349 ? 57.62733  45.94320  11.06178  1.000 97.62458  ? 349 THR   B N     1 
ATOM   6071 C CA    . THR   B 1 349 ? 58.48517  46.03776  12.23874  1.000 88.68653  ? 349 THR   B CA    1 
ATOM   6072 C C     . THR   B 1 349 ? 59.84826  46.61859  11.88658  1.000 92.58004  ? 349 THR   B C     1 
ATOM   6073 O O     . THR   B 1 349 ? 60.51074  46.12556  10.96499  1.000 96.72212  ? 349 THR   B O     1 
ATOM   6074 C CB    . THR   B 1 349 ? 58.69736  44.64993  12.81652  1.000 92.97979  ? 349 THR   B CB    1 
ATOM   6075 O OG1   . THR   B 1 349 ? 57.45339  43.93821  12.85206  1.000 90.80967  ? 349 THR   B OG1   1 
ATOM   6076 C CG2   . THR   B 1 349 ? 59.24748  44.78302  14.20602  1.000 92.19314  ? 349 THR   B CG2   1 
ATOM   6077 N N     . LYS   B 1 350 ? 60.28706  47.64371  12.64160  1.000 94.07101  ? 350 LYS   B N     1 
ATOM   6078 C CA    . LYS   B 1 350 ? 61.59639  48.27468  12.40863  1.000 95.97332  ? 350 LYS   B CA    1 
ATOM   6079 C C     . LYS   B 1 350 ? 62.69237  47.22601  12.51047  1.000 97.04811  ? 350 LYS   B C     1 
ATOM   6080 O O     . LYS   B 1 350 ? 63.25816  47.02113  13.58793  1.000 93.83629  ? 350 LYS   B O     1 
ATOM   6081 C CB    . LYS   B 1 350 ? 61.88972  49.41425  13.39615  1.000 76.55866  ? 350 LYS   B CB    1 
ATOM   6082 N N     . ASN   B 1 351 ? 63.00397  46.55603  11.39766  1.000 100.71338 ? 351 ASN   B N     1 
ATOM   6083 C CA    . ASN   B 1 351 ? 63.82358  45.35213  11.47595  1.000 98.09918  ? 351 ASN   B CA    1 
ATOM   6084 C C     . ASN   B 1 351 ? 65.29017  45.63952  11.84594  1.000 93.71038  ? 351 ASN   B C     1 
ATOM   6085 O O     . ASN   B 1 351 ? 66.00714  44.70791  12.24882  1.000 87.96491  ? 351 ASN   B O     1 
ATOM   6086 C CB    . ASN   B 1 351 ? 63.63369  44.51658  10.16586  1.000 96.73746  ? 351 ASN   B CB    1 
ATOM   6087 C CG    . ASN   B 1 351 ? 64.11114  45.21274  8.87787   1.000 95.37340  ? 351 ASN   B CG    1 
ATOM   6088 O OD1   . ASN   B 1 351 ? 65.22361  45.75571  8.82721   1.000 93.29336  ? 351 ASN   B OD1   1 
ATOM   6089 N ND2   . ASN   B 1 351 ? 63.28762  45.14908  7.81430   1.000 93.11171  ? 351 ASN   B ND2   1 
ATOM   6090 N N     . GLY   B 1 352 ? 65.72736  46.90903  11.81869  1.000 89.18523  ? 352 GLY   B N     1 
ATOM   6091 C CA    . GLY   B 1 352 ? 67.08629  47.25439  12.18554  1.000 85.21393  ? 352 GLY   B CA    1 
ATOM   6092 C C     . GLY   B 1 352 ? 68.17382  46.54930  11.40749  1.000 90.93340  ? 352 GLY   B C     1 
ATOM   6093 O O     . GLY   B 1 352 ? 69.35024  46.69429  11.75690  1.000 91.76599  ? 352 GLY   B O     1 
ATOM   6094 N N     . THR   B 1 353 ? 67.82068  45.79949  10.36063  1.000 90.80932  ? 353 THR   B N     1 
ATOM   6095 C CA    . THR   B 1 353 ? 68.78519  45.07088  9.54691   1.000 87.74960  ? 353 THR   B CA    1 
ATOM   6096 C C     . THR   B 1 353 ? 69.30352  45.93585  8.39212   1.000 88.17529  ? 353 THR   B C     1 
ATOM   6097 O O     . THR   B 1 353 ? 68.90914  47.09348  8.20986   1.000 90.85950  ? 353 THR   B O     1 
ATOM   6098 C CB    . THR   B 1 353 ? 68.15022  43.80430  8.96465   1.000 84.12082  ? 353 THR   B CB    1 
ATOM   6099 O OG1   . THR   B 1 353 ? 67.16576  44.16179  7.98865   1.000 80.80922  ? 353 THR   B OG1   1 
ATOM   6100 C CG2   . THR   B 1 353 ? 67.47770  43.02540  10.03744  1.000 82.83684  ? 353 THR   B CG2   1 
ATOM   6101 N N     . ASP   B 1 354 ? 70.22727  45.35212  7.61113   1.000 86.96361  ? 354 ASP   B N     1 
ATOM   6102 C CA    . ASP   B 1 354 ? 70.42262  45.70997  6.20790   1.000 87.84144  ? 354 ASP   B CA    1 
ATOM   6103 C C     . ASP   B 1 354 ? 70.11051  44.55407  5.26827   1.000 83.05055  ? 354 ASP   B C     1 
ATOM   6104 O O     . ASP   B 1 354 ? 70.10636  44.74075  4.04585   1.000 86.94937  ? 354 ASP   B O     1 
ATOM   6105 C CB    . ASP   B 1 354 ? 71.85933  46.22963  5.96645   1.000 88.08274  ? 354 ASP   B CB    1 
ATOM   6106 C CG    . ASP   B 1 354 ? 72.89720  45.12341  5.83994   1.000 85.64507  ? 354 ASP   B CG    1 
ATOM   6107 O OD1   . ASP   B 1 354 ? 72.55021  43.91248  5.87589   1.000 84.04267  ? 354 ASP   B OD1   1 
ATOM   6108 O OD2   . ASP   B 1 354 ? 74.09353  45.49038  5.70869   1.000 87.95474  ? 354 ASP   B OD2   1 
ATOM   6109 N N     . LEU   B 1 355 ? 69.83365  43.37373  5.80490   1.000 80.33372  ? 355 LEU   B N     1 
ATOM   6110 C CA    . LEU   B 1 355 ? 69.45522  42.22188  5.00226   1.000 77.73615  ? 355 LEU   B CA    1 
ATOM   6111 C C     . LEU   B 1 355 ? 68.81187  41.19610  5.92352   1.000 81.65880  ? 355 LEU   B C     1 
ATOM   6112 O O     . LEU   B 1 355 ? 69.34161  40.93176  7.00994   1.000 84.98783  ? 355 LEU   B O     1 
ATOM   6113 C CB    . LEU   B 1 355 ? 70.67767  41.65354  4.30601   1.000 77.59029  ? 355 LEU   B CB    1 
ATOM   6114 C CG    . LEU   B 1 355 ? 70.54868  40.34300  3.55567   1.000 83.22020  ? 355 LEU   B CG    1 
ATOM   6115 C CD1   . LEU   B 1 355 ? 69.56452  40.45592  2.40788   1.000 93.88567  ? 355 LEU   B CD1   1 
ATOM   6116 C CD2   . LEU   B 1 355 ? 71.95119  40.02608  3.05621   1.000 76.93326  ? 355 LEU   B CD2   1 
ATOM   6117 N N     . TYR   B 1 356 ? 67.66235  40.65486  5.52138   1.000 75.18366  ? 356 TYR   B N     1 
ATOM   6118 C CA    . TYR   B 1 356 ? 66.95896  39.68017  6.33993   1.000 68.78085  ? 356 TYR   B CA    1 
ATOM   6119 C C     . TYR   B 1 356 ? 66.40197  38.62483  5.40982   1.000 73.78543  ? 356 TYR   B C     1 
ATOM   6120 O O     . TYR   B 1 356 ? 66.15677  38.88774  4.23006   1.000 82.87595  ? 356 TYR   B O     1 
ATOM   6121 C CB    . TYR   B 1 356 ? 65.83157  40.30581  7.21623   1.000 75.69313  ? 356 TYR   B CB    1 
ATOM   6122 C CG    . TYR   B 1 356 ? 64.45840  40.62358  6.57614   1.000 78.69572  ? 356 TYR   B CG    1 
ATOM   6123 C CD1   . TYR   B 1 356 ? 63.57150  39.59725  6.22953   1.000 74.63591  ? 356 TYR   B CD1   1 
ATOM   6124 C CD2   . TYR   B 1 356 ? 64.02169  41.94849  6.40527   1.000 77.70864  ? 356 TYR   B CD2   1 
ATOM   6125 C CE1   . TYR   B 1 356 ? 62.33393  39.87478  5.66635   1.000 80.32364  ? 356 TYR   B CE1   1 
ATOM   6126 C CE2   . TYR   B 1 356 ? 62.78246  42.23659  5.85153   1.000 76.91805  ? 356 TYR   B CE2   1 
ATOM   6127 C CZ    . TYR   B 1 356 ? 61.94090  41.19070  5.48208   1.000 83.38078  ? 356 TYR   B CZ    1 
ATOM   6128 O OH    . TYR   B 1 356 ? 60.70120  41.43189  4.92753   1.000 80.72879  ? 356 TYR   B OH    1 
ATOM   6129 N N     . ALA   B 1 357 ? 66.20186  37.42262  5.94912   1.000 63.37353  ? 357 ALA   B N     1 
ATOM   6130 C CA    . ALA   B 1 357 ? 65.80196  36.28957  5.12903   1.000 65.92085  ? 357 ALA   B CA    1 
ATOM   6131 C C     . ALA   B 1 357 ? 65.27106  35.17344  6.00561   1.000 71.34704  ? 357 ALA   B C     1 
ATOM   6132 O O     . ALA   B 1 357 ? 65.70669  35.00373  7.14624   1.000 70.04407  ? 357 ALA   B O     1 
ATOM   6133 C CB    . ALA   B 1 357 ? 66.96591  35.74562  4.30499   1.000 63.94964  ? 357 ALA   B CB    1 
ATOM   6134 N N     . VAL   B 1 358 ? 64.37647  34.36895  5.43837   1.000 72.91828  ? 358 VAL   B N     1 
ATOM   6135 C CA    . VAL   B 1 358 ? 63.59386  33.47337  6.27245   1.000 70.64757  ? 358 VAL   B CA    1 
ATOM   6136 C C     . VAL   B 1 358 ? 63.36075  32.17034  5.53731   1.000 69.10492  ? 358 VAL   B C     1 
ATOM   6137 O O     . VAL   B 1 358 ? 62.38945  32.02643  4.79528   1.000 71.75822  ? 358 VAL   B O     1 
ATOM   6138 C CB    . VAL   B 1 358 ? 62.27008  34.13584  6.67754   1.000 72.55549  ? 358 VAL   B CB    1 
ATOM   6139 C CG1   . VAL   B 1 358 ? 61.73975  33.47419  7.90834   1.000 73.52765  ? 358 VAL   B CG1   1 
ATOM   6140 C CG2   . VAL   B 1 358 ? 62.44964  35.65189  6.89188   1.000 72.40824  ? 358 VAL   B CG2   1 
ATOM   6141 N N     . THR   B 1 359 ? 64.23322  31.20541  5.77168   1.000 70.02410  ? 359 THR   B N     1 
ATOM   6142 C CA    . THR   B 1 359 ? 64.36485  30.04029  4.90387   1.000 77.90640  ? 359 THR   B CA    1 
ATOM   6143 C C     . THR   B 1 359 ? 63.48633  28.91246  5.44737   1.000 79.86182  ? 359 THR   B C     1 
ATOM   6144 O O     . THR   B 1 359 ? 63.75919  28.37433  6.52252   1.000 86.27293  ? 359 THR   B O     1 
ATOM   6145 C CB    . THR   B 1 359 ? 65.83590  29.60798  4.83266   1.000 80.09914  ? 359 THR   B CB    1 
ATOM   6146 O OG1   . THR   B 1 359 ? 66.68152  30.76313  4.71091   1.000 80.15716  ? 359 THR   B OG1   1 
ATOM   6147 C CG2   . THR   B 1 359 ? 66.07593  28.68719  3.62482   1.000 74.33551  ? 359 THR   B CG2   1 
ATOM   6148 N N     . PHE   B 1 360 ? 62.42877  28.56629  4.71936   1.000 78.42660  ? 360 PHE   B N     1 
ATOM   6149 C CA    . PHE   B 1 360 ? 61.69121  27.32356  4.94625   1.000 79.95717  ? 360 PHE   B CA    1 
ATOM   6150 C C     . PHE   B 1 360 ? 62.29973  26.23463  4.07216   1.000 85.53384  ? 360 PHE   B C     1 
ATOM   6151 O O     . PHE   B 1 360 ? 62.53665  26.45156  2.88126   1.000 91.74241  ? 360 PHE   B O     1 
ATOM   6152 C CB    . PHE   B 1 360 ? 60.19749  27.50036  4.63022   1.000 86.30915  ? 360 PHE   B CB    1 
ATOM   6153 C CG    . PHE   B 1 360 ? 59.54852  28.67577  5.33998   1.000 91.39556  ? 360 PHE   B CG    1 
ATOM   6154 C CD1   . PHE   B 1 360 ? 58.97787  28.53005  6.59533   1.000 92.85728  ? 360 PHE   B CD1   1 
ATOM   6155 C CD2   . PHE   B 1 360 ? 59.54570  29.93390  4.77270   1.000 92.91504  ? 360 PHE   B CD2   1 
ATOM   6156 C CE1   . PHE   B 1 360 ? 58.40304  29.61620  7.24891   1.000 95.27775  ? 360 PHE   B CE1   1 
ATOM   6157 C CE2   . PHE   B 1 360 ? 58.97429  31.02575  5.42945   1.000 87.20319  ? 360 PHE   B CE2   1 
ATOM   6158 C CZ    . PHE   B 1 360 ? 58.40492  30.86654  6.65988   1.000 90.03828  ? 360 PHE   B CZ    1 
ATOM   6159 N N     . ALA   B 1 361 ? 62.57529  25.07378  4.65510   1.000 88.18277  ? 361 ALA   B N     1 
ATOM   6160 C CA    . ALA   B 1 361 ? 63.16822  23.98956  3.87722   1.000 89.41842  ? 361 ALA   B CA    1 
ATOM   6161 C C     . ALA   B 1 361 ? 62.53034  22.66367  4.24898   1.000 84.75917  ? 361 ALA   B C     1 
ATOM   6162 O O     . ALA   B 1 361 ? 62.43967  22.32945  5.43269   1.000 88.47389  ? 361 ALA   B O     1 
ATOM   6163 C CB    . ALA   B 1 361 ? 64.68038  23.91530  4.09458   1.000 86.66393  ? 361 ALA   B CB    1 
ATOM   6164 N N     . ALA   B 1 362 ? 62.11308  21.90692  3.23856   1.000 76.97192  ? 362 ALA   B N     1 
ATOM   6165 C CA    . ALA   B 1 362 ? 61.41803  20.64678  3.46669   1.000 84.67207  ? 362 ALA   B CA    1 
ATOM   6166 C C     . ALA   B 1 362 ? 62.29397  19.67514  4.24407   1.000 89.72076  ? 362 ALA   B C     1 
ATOM   6167 O O     . ALA   B 1 362 ? 63.50270  19.85812  4.35925   1.000 89.39756  ? 362 ALA   B O     1 
ATOM   6168 C CB    . ALA   B 1 362 ? 61.01163  20.00207  2.14339   1.000 82.00616  ? 362 ALA   B CB    1 
ATOM   6169 N N     . LEU   B 1 363 ? 61.65604  18.62580  4.78009   1.000 92.95612  ? 363 LEU   B N     1 
ATOM   6170 C CA    . LEU   B 1 363 ? 62.37531  17.48661  5.34792   1.000 88.03284  ? 363 LEU   B CA    1 
ATOM   6171 C C     . LEU   B 1 363 ? 61.69638  16.18167  4.92663   1.000 85.54726  ? 363 LEU   B C     1 
ATOM   6172 O O     . LEU   B 1 363 ? 61.30937  16.02696  3.75954   1.000 86.50905  ? 363 LEU   B O     1 
ATOM   6173 C CB    . LEU   B 1 363 ? 62.46560  17.59668  6.87135   1.000 89.84380  ? 363 LEU   B CB    1 
ATOM   6174 C CG    . LEU   B 1 363 ? 63.68465  18.38707  7.35819   1.000 87.14657  ? 363 LEU   B CG    1 
ATOM   6175 C CD1   . LEU   B 1 363 ? 63.46962  19.85594  7.11298   1.000 85.16854  ? 363 LEU   B CD1   1 
ATOM   6176 C CD2   . LEU   B 1 363 ? 63.96471  18.14917  8.80459   1.000 94.68199  ? 363 LEU   B CD2   1 
ATOM   6177 N N     . GLY   B 1 364 ? 61.58469  15.23144  5.85474   1.000 83.62797  ? 364 GLY   B N     1 
ATOM   6178 C CA    . GLY   B 1 364 ? 60.92220  13.96477  5.53970   1.000 86.76492  ? 364 GLY   B CA    1 
ATOM   6179 C C     . GLY   B 1 364 ? 61.58890  13.18603  4.41404   1.000 77.23586  ? 364 GLY   B C     1 
ATOM   6180 O O     . GLY   B 1 364 ? 62.81035  13.07614  4.33991   1.000 87.65316  ? 364 GLY   B O     1 
ATOM   6181 N N     . GLY   B 1 365 ? 60.78352  12.59817  3.54794   1.000 66.74743  ? 365 GLY   B N     1 
ATOM   6182 C CA    . GLY   B 1 365 ? 61.30647  11.85990  2.41049   1.000 81.76844  ? 365 GLY   B CA    1 
ATOM   6183 C C     . GLY   B 1 365 ? 62.02308  10.57500  2.78614   1.000 91.81473  ? 365 GLY   B C     1 
ATOM   6184 O O     . GLY   B 1 365 ? 61.51490  9.46705   2.55013   1.000 91.64174  ? 365 GLY   B O     1 
ATOM   6185 N N     . ALA   B 1 366 ? 63.22944  10.72341  3.34824   1.000 90.87884  ? 366 ALA   B N     1 
ATOM   6186 C CA    . ALA   B 1 366 ? 63.96864  9.62961   3.96659   1.000 87.58103  ? 366 ALA   B CA    1 
ATOM   6187 C C     . ALA   B 1 366 ? 64.48504  9.97705   5.35060   1.000 85.13275  ? 366 ALA   B C     1 
ATOM   6188 O O     . ALA   B 1 366 ? 64.80474  9.06136   6.12078   1.000 85.07426  ? 366 ALA   B O     1 
ATOM   6189 C CB    . ALA   B 1 366 ? 65.14830  9.18734   3.08815   1.000 85.27914  ? 366 ALA   B CB    1 
ATOM   6190 N N     . VAL   B 1 367 ? 64.55861  11.25742  5.70038   1.000 83.86228  ? 367 VAL   B N     1 
ATOM   6191 C CA    . VAL   B 1 367 ? 64.79113  11.71876  7.06366   1.000 87.84114  ? 367 VAL   B CA    1 
ATOM   6192 C C     . VAL   B 1 367 ? 63.94493  10.94441  8.06834   1.000 99.80167  ? 367 VAL   B C     1 
ATOM   6193 O O     . VAL   B 1 367 ? 64.29876  10.81691  9.25223   1.000 105.48788 ? 367 VAL   B O     1 
ATOM   6194 C CB    . VAL   B 1 367 ? 64.50067  13.22023  7.15273   1.000 79.95761  ? 367 VAL   B CB    1 
ATOM   6195 C CG1   . VAL   B 1 367 ? 64.61412  13.69690  8.57624   1.000 83.88174  ? 367 VAL   B CG1   1 
ATOM   6196 C CG2   . VAL   B 1 367 ? 65.47585  13.92684  6.30025   1.000 86.29330  ? 367 VAL   B CG2   1 
ATOM   6197 N N     . ARG   B 1 368 ? 62.81302  10.43733  7.60493   1.000 100.86731 ? 368 ARG   B N     1 
ATOM   6198 C CA    . ARG   B 1 368 ? 61.93044  9.61209   8.42283   1.000 99.74739  ? 368 ARG   B CA    1 
ATOM   6199 C C     . ARG   B 1 368 ? 62.03511  8.13659   8.01516   1.000 97.88889  ? 368 ARG   B C     1 
ATOM   6200 O O     . ARG   B 1 368 ? 61.03022  7.46173   7.82583   1.000 107.20207 ? 368 ARG   B O     1 
ATOM   6201 C CB    . ARG   B 1 368 ? 60.50129  10.13179  8.30154   1.000 103.44961 ? 368 ARG   B CB    1 
ATOM   6202 C CG    . ARG   B 1 368 ? 60.24246  11.53182  8.89873   1.000 101.66264 ? 368 ARG   B CG    1 
ATOM   6203 C CD    . ARG   B 1 368 ? 58.76823  11.87981  8.71575   1.000 102.82844 ? 368 ARG   B CD    1 
ATOM   6204 N NE    . ARG   B 1 368 ? 58.39080  13.21191  9.16632   1.000 99.33505  ? 368 ARG   B NE    1 
ATOM   6205 C CZ    . ARG   B 1 368 ? 57.18608  13.73349  8.96748   1.000 109.44855 ? 368 ARG   B CZ    1 
ATOM   6206 N NH1   . ARG   B 1 368 ? 56.24332  13.06631  8.32391   1.000 112.88758 ? 368 ARG   B NH1   1 
ATOM   6207 N NH2   . ARG   B 1 368 ? 56.91884  14.95636  9.41965   1.000 111.73324 ? 368 ARG   B NH2   1 
ATOM   6208 N N     . ASP   B 1 369 ? 63.25982  7.62667   7.81555   1.000 96.38881  ? 369 ASP   B N     1 
ATOM   6209 C CA    . ASP   B 1 369 ? 63.54660  6.19069   7.87895   1.000 97.21678  ? 369 ASP   B CA    1 
ATOM   6210 C C     . ASP   B 1 369 ? 64.34781  5.84959   9.13973   1.000 96.69204  ? 369 ASP   B C     1 
ATOM   6211 O O     . ASP   B 1 369 ? 64.88560  4.74361   9.26558   1.000 89.97336  ? 369 ASP   B O     1 
ATOM   6212 C CB    . ASP   B 1 369 ? 64.29245  5.69738   6.63193   1.000 94.87821  ? 369 ASP   B CB    1 
ATOM   6213 C CG    . ASP   B 1 369 ? 63.57445  6.03289   5.32064   1.000 107.81276 ? 369 ASP   B CG    1 
ATOM   6214 O OD1   . ASP   B 1 369 ? 62.61530  6.84213   5.35732   1.000 111.75704 ? 369 ASP   B OD1   1 
ATOM   6215 O OD2   . ASP   B 1 369 ? 63.93190  5.45976   4.26035   1.000 107.93121 ? 369 ASP   B OD2   1 
ATOM   6216 N N     . VAL   B 1 370 ? 64.42726  6.79542   10.07436  1.000 95.05978  ? 370 VAL   B N     1 
ATOM   6217 C CA    . VAL   B 1 370 ? 65.29161  6.71315   11.24202  1.000 91.81648  ? 370 VAL   B CA    1 
ATOM   6218 C C     . VAL   B 1 370 ? 64.52557  7.29872   12.42052  1.000 90.80355  ? 370 VAL   B C     1 
ATOM   6219 O O     . VAL   B 1 370 ? 64.15090  8.48084   12.39900  1.000 82.38656  ? 370 VAL   B O     1 
ATOM   6220 C CB    . VAL   B 1 370 ? 66.63039  7.44958   11.00610  1.000 93.56200  ? 370 VAL   B CB    1 
ATOM   6221 C CG1   . VAL   B 1 370 ? 67.45604  7.55239   12.28282  1.000 86.33292  ? 370 VAL   B CG1   1 
ATOM   6222 C CG2   . VAL   B 1 370 ? 67.41903  6.73126   9.92780   1.000 91.80292  ? 370 VAL   B CG2   1 
ATOM   6223 N N     . SER   B 1 371 ? 64.26422  6.45523   13.42210  1.000 87.40984  ? 371 SER   B N     1 
ATOM   6224 C CA    . SER   B 1 371 ? 63.49882  6.84373   14.60141  1.000 81.76585  ? 371 SER   B CA    1 
ATOM   6225 C C     . SER   B 1 371 ? 64.19638  7.94528   15.39615  1.000 83.04592  ? 371 SER   B C     1 
ATOM   6226 O O     . SER   B 1 371 ? 65.41508  7.93531   15.56249  1.000 88.30252  ? 371 SER   B O     1 
ATOM   6227 C CB    . SER   B 1 371 ? 63.29509  5.61143   15.48306  1.000 89.56647  ? 371 SER   B CB    1 
ATOM   6228 O OG    . SER   B 1 371 ? 62.85893  5.95725   16.78534  1.000 94.75025  ? 371 SER   B OG    1 
ATOM   6229 N N     . ALA   B 1 372 ? 63.41562  8.88927   15.92548  1.000 80.34280  ? 372 ALA   B N     1 
ATOM   6230 C CA    . ALA   B 1 372 ? 64.00641  9.98034   16.69708  1.000 84.97704  ? 372 ALA   B CA    1 
ATOM   6231 C C     . ALA   B 1 372 ? 64.82353  9.49541   17.88415  1.000 90.14220  ? 372 ALA   B C     1 
ATOM   6232 O O     . ALA   B 1 372 ? 65.58383  10.28187  18.45640  1.000 92.10277  ? 372 ALA   B O     1 
ATOM   6233 C CB    . ALA   B 1 372 ? 62.94056  10.93531  17.23475  1.000 88.23790  ? 372 ALA   B CB    1 
ATOM   6234 N N     . SER   B 1 373 ? 64.65216  8.24478   18.30103  1.000 92.43675  ? 373 SER   B N     1 
ATOM   6235 C CA    . SER   B 1 373 ? 65.38526  7.68037   19.42772  1.000 94.17701  ? 373 SER   B CA    1 
ATOM   6236 C C     . SER   B 1 373 ? 66.65358  6.94685   19.00082  1.000 94.38082  ? 373 SER   B C     1 
ATOM   6237 O O     . SER   B 1 373 ? 67.44327  6.54059   19.86517  1.000 97.48866  ? 373 SER   B O     1 
ATOM   6238 C CB    . SER   B 1 373 ? 64.48254  6.72154   20.22353  1.000 98.21313  ? 373 SER   B CB    1 
ATOM   6239 O OG    . SER   B 1 373 ? 63.92445  5.71698   19.38122  1.000 93.66388  ? 373 SER   B OG    1 
ATOM   6240 N N     . GLU   B 1 374 ? 66.86806  6.79162   17.69540  1.000 85.23592  ? 374 GLU   B N     1 
ATOM   6241 C CA    . GLU   B 1 374 ? 67.96608  6.03432   17.12112  1.000 85.86689  ? 374 GLU   B CA    1 
ATOM   6242 C C     . GLU   B 1 374 ? 69.20939  6.88167   16.84801  1.000 84.74529  ? 374 GLU   B C     1 
ATOM   6243 O O     . GLU   B 1 374 ? 70.27758  6.32028   16.56879  1.000 86.41095  ? 374 GLU   B O     1 
ATOM   6244 C CB    . GLU   B 1 374 ? 67.45079  5.38785   15.83812  1.000 88.74524  ? 374 GLU   B CB    1 
ATOM   6245 C CG    . GLU   B 1 374 ? 68.19076  4.21214   15.29747  1.000 88.20205  ? 374 GLU   B CG    1 
ATOM   6246 C CD    . GLU   B 1 374 ? 67.30803  3.45619   14.32544  1.000 96.73259  ? 374 GLU   B CD    1 
ATOM   6247 O OE1   . GLU   B 1 374 ? 66.08958  3.76219   14.25435  1.000 87.20738  ? 374 GLU   B OE1   1 
ATOM   6248 O OE2   . GLU   B 1 374 ? 67.83104  2.56740   13.62850  1.000 104.16397 ? 374 GLU   B OE2   1 
ATOM   6249 N N     . THR   B 1 375 ? 69.08609  8.20592   16.89785  1.000 80.46526  ? 375 THR   B N     1 
ATOM   6250 C CA    . THR   B 1 375 ? 70.19946  9.13898   16.81325  1.000 73.61313  ? 375 THR   B CA    1 
ATOM   6251 C C     . THR   B 1 375 ? 69.94484  10.22986  17.82176  1.000 71.82504  ? 375 THR   B C     1 
ATOM   6252 O O     . THR   B 1 375 ? 68.83477  10.38895  18.32111  1.000 75.27471  ? 375 THR   B O     1 
ATOM   6253 C CB    . THR   B 1 375 ? 70.34657  9.79392   15.43712  1.000 77.50611  ? 375 THR   B CB    1 
ATOM   6254 O OG1   . THR   B 1 375 ? 69.16157  10.55347  15.12771  1.000 81.66054  ? 375 THR   B OG1   1 
ATOM   6255 C CG2   . THR   B 1 375 ? 70.59263  8.73204   14.36077  1.000 74.01704  ? 375 THR   B CG2   1 
ATOM   6256 N N     . ALA   B 1 376 ? 70.96919  11.01014  18.10151  1.000 70.17406  ? 376 ALA   B N     1 
ATOM   6257 C CA    . ALA   B 1 376 ? 70.75814  12.08216  19.06380  1.000 72.63268  ? 376 ALA   B CA    1 
ATOM   6258 C C     . ALA   B 1 376 ? 69.89437  13.15106  18.41244  1.000 79.75359  ? 376 ALA   B C     1 
ATOM   6259 O O     . ALA   B 1 376 ? 69.51447  14.14210  19.04771  1.000 80.93402  ? 376 ALA   B O     1 
ATOM   6260 C CB    . ALA   B 1 376 ? 72.08703  12.65672  19.54969  1.000 72.45127  ? 376 ALA   B CB    1 
ATOM   6261 N N     . PHE   B 1 377 ? 69.54668  12.92674  17.14344  1.000 85.53134  ? 377 PHE   B N     1 
ATOM   6262 C CA    . PHE   B 1 377 ? 68.72293  13.84216  16.35769  1.000 86.83972  ? 377 PHE   B CA    1 
ATOM   6263 C C     . PHE   B 1 377 ? 67.25251  13.49423  16.55753  1.000 84.58435  ? 377 PHE   B C     1 
ATOM   6264 O O     . PHE   B 1 377 ? 66.77069  12.47156  16.04556  1.000 82.49106  ? 377 PHE   B O     1 
ATOM   6265 C CB    . PHE   B 1 377 ? 69.10882  13.76673  14.88398  1.000 85.60892  ? 377 PHE   B CB    1 
ATOM   6266 C CG    . PHE   B 1 377 ? 68.35737  14.72358  14.03172  1.000 86.45816  ? 377 PHE   B CG    1 
ATOM   6267 C CD1   . PHE   B 1 377 ? 68.31312  16.07012  14.36793  1.000 83.16764  ? 377 PHE   B CD1   1 
ATOM   6268 C CD2   . PHE   B 1 377 ? 67.70838  14.29612  12.88878  1.000 78.70361  ? 377 PHE   B CD2   1 
ATOM   6269 C CE1   . PHE   B 1 377 ? 67.60689  16.97552  13.57637  1.000 78.46233  ? 377 PHE   B CE1   1 
ATOM   6270 C CE2   . PHE   B 1 377 ? 67.01444  15.20120  12.09763  1.000 78.47697  ? 377 PHE   B CE2   1 
ATOM   6271 C CZ    . PHE   B 1 377 ? 66.96489  16.53813  12.44032  1.000 77.14330  ? 377 PHE   B CZ    1 
ATOM   6272 N N     . TYR   B 1 378 ? 66.53181  14.35994  17.27202  1.000 82.09668  ? 378 TYR   B N     1 
ATOM   6273 C CA    . TYR   B 1 378 ? 65.18368  14.02079  17.70589  1.000 92.50869  ? 378 TYR   B CA    1 
ATOM   6274 C C     . TYR   B 1 378 ? 64.09181  14.61320  16.83018  1.000 93.00791  ? 378 TYR   B C     1 
ATOM   6275 O O     . TYR   B 1 378 ? 62.99434  14.05016  16.77358  1.000 100.38308 ? 378 TYR   B O     1 
ATOM   6276 C CB    . TYR   B 1 378 ? 64.95094  14.45019  19.17204  1.000 97.67866  ? 378 TYR   B CB    1 
ATOM   6277 C CG    . TYR   B 1 378 ? 63.48474  14.63926  19.59585  1.000 101.01866 ? 378 TYR   B CG    1 
ATOM   6278 C CD1   . TYR   B 1 378 ? 62.58011  13.56641  19.60840  1.000 102.61024 ? 378 TYR   B CD1   1 
ATOM   6279 C CD2   . TYR   B 1 378 ? 63.01501  15.88293  20.01961  1.000 95.51866  ? 378 TYR   B CD2   1 
ATOM   6280 C CE1   . TYR   B 1 378 ? 61.23439  13.73868  20.01354  1.000 104.89865 ? 378 TYR   B CE1   1 
ATOM   6281 C CE2   . TYR   B 1 378 ? 61.68069  16.05959  20.42286  1.000 100.56172 ? 378 TYR   B CE2   1 
ATOM   6282 C CZ    . TYR   B 1 378 ? 60.79785  14.99084  20.42302  1.000 107.26845 ? 378 TYR   B CZ    1 
ATOM   6283 O OH    . TYR   B 1 378 ? 59.49091  15.20619  20.83140  1.000 101.68994 ? 378 TYR   B OH    1 
ATOM   6284 N N     . HIS   B 1 379 ? 64.35030  15.72314  16.13992  1.000 83.10480  ? 379 HIS   B N     1 
ATOM   6285 C CA    . HIS   B 1 379 ? 63.35234  16.35138  15.26893  1.000 75.43689  ? 379 HIS   B CA    1 
ATOM   6286 C C     . HIS   B 1 379 ? 63.33074  15.67904  13.90001  1.000 80.27527  ? 379 HIS   B C     1 
ATOM   6287 O O     . HIS   B 1 379 ? 63.44292  16.32462  12.86725  1.000 82.49852  ? 379 HIS   B O     1 
ATOM   6288 C CB    . HIS   B 1 379 ? 63.65341  17.82812  15.12945  1.000 80.42346  ? 379 HIS   B CB    1 
ATOM   6289 C CG    . HIS   B 1 379 ? 63.71314  18.55794  16.42617  1.000 92.11744  ? 379 HIS   B CG    1 
ATOM   6290 N ND1   . HIS   B 1 379 ? 64.72809  18.34608  17.32463  1.000 93.18783  ? 379 HIS   B ND1   1 
ATOM   6291 C CD2   . HIS   B 1 379 ? 62.93655  19.54109  16.95440  1.000 98.14607  ? 379 HIS   B CD2   1 
ATOM   6292 C CE1   . HIS   B 1 379 ? 64.55566  19.12777  18.37722  1.000 92.68828  ? 379 HIS   B CE1   1 
ATOM   6293 N NE2   . HIS   B 1 379 ? 63.48141  19.87129  18.17594  1.000 93.10593  ? 379 HIS   B NE2   1 
ATOM   6294 N N     . ARG   B 1 380 ? 63.18022  14.34984  13.90398  1.000 81.25731  ? 380 ARG   B N     1 
ATOM   6295 C CA    . ARG   B 1 380 ? 63.16483  13.58220  12.67142  1.000 85.23494  ? 380 ARG   B CA    1 
ATOM   6296 C C     . ARG   B 1 380 ? 61.77577  13.45985  12.03465  1.000 93.95927  ? 380 ARG   B C     1 
ATOM   6297 O O     . ARG   B 1 380 ? 61.69166  13.20479  10.82757  1.000 97.10950  ? 380 ARG   B O     1 
ATOM   6298 C CB    . ARG   B 1 380 ? 63.76372  12.18182  12.90192  1.000 82.15994  ? 380 ARG   B CB    1 
ATOM   6299 N N     . ASP   B 1 381 ? 60.68635  13.62198  12.79316  1.000 103.82685 ? 381 ASP   B N     1 
ATOM   6300 C CA    . ASP   B 1 381 ? 59.33342  13.74161  12.21250  1.000 102.50807 ? 381 ASP   B CA    1 
ATOM   6301 C C     . ASP   B 1 381 ? 59.00781  15.20252  11.94603  1.000 102.81974 ? 381 ASP   B C     1 
ATOM   6302 O O     . ASP   B 1 381 ? 57.99293  15.74341  12.40741  1.000 97.08409  ? 381 ASP   B O     1 
ATOM   6303 C CB    . ASP   B 1 381 ? 58.26160  13.12809  13.11426  1.000 106.60811 ? 381 ASP   B CB    1 
ATOM   6304 C CG    . ASP   B 1 381 ? 58.53042  13.35819  14.60752  1.000 116.33724 ? 381 ASP   B CG    1 
ATOM   6305 O OD1   . ASP   B 1 381 ? 59.33410  14.25234  14.94944  1.000 115.23053 ? 381 ASP   B OD1   1 
ATOM   6306 O OD2   . ASP   B 1 381 ? 57.91943  12.64647  15.44521  1.000 118.85751 ? 381 ASP   B OD2   1 
ATOM   6307 N N     . ALA   B 1 382 ? 59.89084  15.87984  11.22885  1.000 103.60220 ? 382 ALA   B N     1 
ATOM   6308 C CA    . ALA   B 1 382 ? 59.65787  17.26549  10.85056  1.000 107.40866 ? 382 ALA   B CA    1 
ATOM   6309 C C     . ALA   B 1 382 ? 59.21920  17.32475  9.39207   1.000 115.50866 ? 382 ALA   B C     1 
ATOM   6310 O O     . ALA   B 1 382 ? 59.59505  16.47614  8.56638   1.000 102.73698 ? 382 ALA   B O     1 
ATOM   6311 C CB    . ALA   B 1 382 ? 60.89767  18.13872  11.07834  1.000 102.57866 ? 382 ALA   B CB    1 
ATOM   6312 N N     . SER   B 1 383 ? 58.37843  18.32265  9.11105   1.000 114.74866 ? 383 SER   B N     1 
ATOM   6313 C CA    . SER   B 1 383 ? 57.93370  18.65485  7.76966   1.000 106.19654 ? 383 SER   B CA    1 
ATOM   6314 C C     . SER   B 1 383 ? 58.80245  19.73651  7.14586   1.000 94.32586  ? 383 SER   B C     1 
ATOM   6315 O O     . SER   B 1 383 ? 59.10718  19.66589  5.95419   1.000 91.61225  ? 383 SER   B O     1 
ATOM   6316 C CB    . SER   B 1 383 ? 56.46790  19.08831  7.81469   1.000 105.14610 ? 383 SER   B CB    1 
ATOM   6317 O OG    . SER   B 1 383 ? 55.67113  18.00226  8.26391   1.000 108.76834 ? 383 SER   B OG    1 
ATOM   6318 N N     . TYR   B 1 384 ? 59.24600  20.71405  7.93281   1.000 88.98936  ? 384 TYR   B N     1 
ATOM   6319 C CA    . TYR   B 1 384 ? 60.13736  21.73021  7.39575   1.000 90.40315  ? 384 TYR   B CA    1 
ATOM   6320 C C     . TYR   B 1 384 ? 60.76500  22.51971  8.53840   1.000 90.51867  ? 384 TYR   B C     1 
ATOM   6321 O O     . TYR   B 1 384 ? 60.19710  22.59462  9.62709   1.000 96.55866  ? 384 TYR   B O     1 
ATOM   6322 C CB    . TYR   B 1 384 ? 59.38923  22.65918  6.42620   1.000 95.15850  ? 384 TYR   B CB    1 
ATOM   6323 C CG    . TYR   B 1 384 ? 58.28515  23.55040  7.00562   1.000 95.30819  ? 384 TYR   B CG    1 
ATOM   6324 C CD1   . TYR   B 1 384 ? 58.59333  24.71695  7.70128   1.000 92.79014  ? 384 TYR   B CD1   1 
ATOM   6325 C CD2   . TYR   B 1 384 ? 56.93085  23.27531  6.78019   1.000 98.04958  ? 384 TYR   B CD2   1 
ATOM   6326 C CE1   . TYR   B 1 384 ? 57.58262  25.56335  8.22217   1.000 95.11125  ? 384 TYR   B CE1   1 
ATOM   6327 C CE2   . TYR   B 1 384 ? 55.90985  24.12110  7.28948   1.000 97.00308  ? 384 TYR   B CE2   1 
ATOM   6328 C CZ    . TYR   B 1 384 ? 56.24419  25.26589  8.01294   1.000 98.96238  ? 384 TYR   B CZ    1 
ATOM   6329 O OH    . TYR   B 1 384 ? 55.26514  26.11657  8.52634   1.000 96.21895  ? 384 TYR   B OH    1 
ATOM   6330 N N     . PHE   B 1 385 ? 61.95123  23.08511  8.29471   1.000 87.29142  ? 385 PHE   B N     1 
ATOM   6331 C CA    . PHE   B 1 385 ? 62.57399  23.99551  9.24610   1.000 85.40961  ? 385 PHE   B CA    1 
ATOM   6332 C C     . PHE   B 1 385 ? 62.24223  25.43028  8.90737   1.000 81.13658  ? 385 PHE   B C     1 
ATOM   6333 O O     . PHE   B 1 385 ? 61.70201  25.74361  7.84334   1.000 85.00990  ? 385 PHE   B O     1 
ATOM   6334 C CB    . PHE   B 1 385 ? 64.10789  23.91061  9.26108   1.000 90.43720  ? 385 PHE   B CB    1 
ATOM   6335 C CG    . PHE   B 1 385 ? 64.67188  22.59715  9.67770   1.000 97.20173  ? 385 PHE   B CG    1 
ATOM   6336 C CD1   . PHE   B 1 385 ? 64.22206  21.93646  10.80912  1.000 98.13088  ? 385 PHE   B CD1   1 
ATOM   6337 C CD2   . PHE   B 1 385 ? 65.69007  22.02771  8.93148   1.000 99.96773  ? 385 PHE   B CD2   1 
ATOM   6338 C CE1   . PHE   B 1 385 ? 64.77177  20.71415  11.17709  1.000 97.24649  ? 385 PHE   B CE1   1 
ATOM   6339 C CE2   . PHE   B 1 385 ? 66.23593  20.81938  9.29052   1.000 98.35866  ? 385 PHE   B CE2   1 
ATOM   6340 C CZ    . PHE   B 1 385 ? 65.77898  20.15922  10.41763  1.000 94.73866  ? 385 PHE   B CZ    1 
ATOM   6341 N N     . MET   B 1 386 ? 62.66573  26.31638  9.80096   1.000 77.75952  ? 386 MET   B N     1 
ATOM   6342 C CA    . MET   B 1 386 ? 62.66725  27.75967  9.57102   1.000 75.56076  ? 386 MET   B CA    1 
ATOM   6343 C C     . MET   B 1 386 ? 63.96865  28.31507  10.12619  1.000 78.09905  ? 386 MET   B C     1 
ATOM   6344 O O     . MET   B 1 386 ? 64.26122  28.15946  11.31882  1.000 80.46663  ? 386 MET   B O     1 
ATOM   6345 C CB    . MET   B 1 386 ? 61.45451  28.44258  10.22255  1.000 62.86584  ? 386 MET   B CB    1 
ATOM   6346 C CG    . MET   B 1 386 ? 61.33716  29.94491  10.00422  1.000 65.81093  ? 386 MET   B CG    1 
ATOM   6347 S SD    . MET   B 1 386 ? 62.56712  31.00115  10.86753  1.000 76.65966  ? 386 MET   B SD    1 
ATOM   6348 C CE    . MET   B 1 386 ? 61.77302  31.33545  12.44954  1.000 71.63820  ? 386 MET   B CE    1 
ATOM   6349 N N     . PHE   B 1 387 ? 64.74867  28.96966  9.28146   1.000 75.87539  ? 387 PHE   B N     1 
ATOM   6350 C CA    . PHE   B 1 387 ? 65.93152  29.68616  9.73692   1.000 77.83608  ? 387 PHE   B CA    1 
ATOM   6351 C C     . PHE   B 1 387 ? 65.72384  31.17103  9.47934   1.000 72.97095  ? 387 PHE   B C     1 
ATOM   6352 O O     . PHE   B 1 387 ? 65.45340  31.57686  8.34525   1.000 80.10324  ? 387 PHE   B O     1 
ATOM   6353 C CB    . PHE   B 1 387 ? 67.16555  29.16322  9.01340   1.000 77.87779  ? 387 PHE   B CB    1 
ATOM   6354 C CG    . PHE   B 1 387 ? 67.30787  27.69651  9.09809   1.000 73.09685  ? 387 PHE   B CG    1 
ATOM   6355 C CD1   . PHE   B 1 387 ? 66.69482  26.88839  8.15979   1.000 74.85976  ? 387 PHE   B CD1   1 
ATOM   6356 C CD2   . PHE   B 1 387 ? 68.02148  27.11393  10.12760  1.000 76.20051  ? 387 PHE   B CD2   1 
ATOM   6357 C CE1   . PHE   B 1 387 ? 66.80444  25.50336  8.22988   1.000 81.15235  ? 387 PHE   B CE1   1 
ATOM   6358 C CE2   . PHE   B 1 387 ? 68.13677  25.73260  10.20745  1.000 83.86994  ? 387 PHE   B CE2   1 
ATOM   6359 C CZ    . PHE   B 1 387 ? 67.52165  24.91941  9.25115   1.000 81.20172  ? 387 PHE   B CZ    1 
ATOM   6360 N N     . SER   B 1 388 ? 65.83087  31.98192  10.50894  1.000 65.56840  ? 388 SER   B N     1 
ATOM   6361 C CA    . SER   B 1 388 ? 65.65852  33.42065  10.33021  1.000 73.80497  ? 388 SER   B CA    1 
ATOM   6362 C C     . SER   B 1 388 ? 67.02384  34.08097  10.48230  1.000 75.21270  ? 388 SER   B C     1 
ATOM   6363 O O     . SER   B 1 388 ? 67.58531  34.12690  11.58549  1.000 78.85509  ? 388 SER   B O     1 
ATOM   6364 C CB    . SER   B 1 388 ? 64.65171  34.01519  11.31711  1.000 83.12002  ? 388 SER   B CB    1 
ATOM   6365 O OG    . SER   B 1 388 ? 65.06280  33.93361  12.68100  1.000 86.39495  ? 388 SER   B OG    1 
ATOM   6366 N N     . PHE   B 1 389 ? 67.56222  34.58610  9.38894   1.000 65.59148  ? 389 PHE   B N     1 
ATOM   6367 C CA    . PHE   B 1 389 ? 68.82096  35.30153  9.45005   1.000 63.27712  ? 389 PHE   B CA    1 
ATOM   6368 C C     . PHE   B 1 389 ? 68.51521  36.80029  9.44376   1.000 63.43280  ? 389 PHE   B C     1 
ATOM   6369 O O     . PHE   B 1 389 ? 67.55407  37.23090  8.81357   1.000 68.98557  ? 389 PHE   B O     1 
ATOM   6370 C CB    . PHE   B 1 389 ? 69.72592  34.87027  8.28231   1.000 60.49920  ? 389 PHE   B CB    1 
ATOM   6371 C CG    . PHE   B 1 389 ? 71.12151  35.45194  8.33351   1.000 68.37465  ? 389 PHE   B CG    1 
ATOM   6372 C CD1   . PHE   B 1 389 ? 72.12841  34.81732  9.04855   1.000 69.43967  ? 389 PHE   B CD1   1 
ATOM   6373 C CD2   . PHE   B 1 389 ? 71.42539  36.64473  7.68110   1.000 72.28223  ? 389 PHE   B CD2   1 
ATOM   6374 C CE1   . PHE   B 1 389 ? 73.41400  35.35901  9.10718   1.000 66.81341  ? 389 PHE   B CE1   1 
ATOM   6375 C CE2   . PHE   B 1 389 ? 72.70226  37.19794  7.74298   1.000 70.48810  ? 389 PHE   B CE2   1 
ATOM   6376 C CZ    . PHE   B 1 389 ? 73.69931  36.54067  8.45534   1.000 67.56965  ? 389 PHE   B CZ    1 
ATOM   6377 N N     . GLY   B 1 390 ? 69.29466  37.58973  10.18489  1.000 62.86015  ? 390 GLY   B N     1 
ATOM   6378 C CA    . GLY   B 1 390 ? 69.15925  39.03418  10.15422  1.000 59.23890  ? 390 GLY   B CA    1 
ATOM   6379 C C     . GLY   B 1 390 ? 70.47225  39.77921  10.28875  1.000 68.87934  ? 390 GLY   B C     1 
ATOM   6380 O O     . GLY   B 1 390 ? 70.96528  39.91635  11.40861  1.000 72.99107  ? 390 GLY   B O     1 
ATOM   6381 N N     . ARG   B 1 391 ? 71.04586  40.27369  9.18154   1.000 74.80787  ? 391 ARG   B N     1 
ATOM   6382 C CA    . ARG   B 1 391 ? 72.37973  40.87561  9.16606   1.000 76.93616  ? 391 ARG   B CA    1 
ATOM   6383 C C     . ARG   B 1 391 ? 72.30151  42.38958  9.41354   1.000 70.42921  ? 391 ARG   B C     1 
ATOM   6384 O O     . ARG   B 1 391 ? 71.24882  43.01331  9.28523   1.000 70.86419  ? 391 ARG   B O     1 
ATOM   6385 C CB    . ARG   B 1 391 ? 73.10458  40.55814  7.83930   1.000 65.69745  ? 391 ARG   B CB    1 
ATOM   6386 N N     . THR   B 1 392 ? 73.43841  42.97856  9.77864   1.000 64.61902  ? 392 THR   B N     1 
ATOM   6387 C CA    . THR   B 1 392 ? 73.42993  44.34212  10.29562  1.000 76.71941  ? 392 THR   B CA    1 
ATOM   6388 C C     . THR   B 1 392 ? 74.72614  45.04336  9.90613   1.000 74.71272  ? 392 THR   B C     1 
ATOM   6389 O O     . THR   B 1 392 ? 75.81057  44.49198  10.11061  1.000 76.61247  ? 392 THR   B O     1 
ATOM   6390 C CB    . THR   B 1 392 ? 73.26275  44.32843  11.83030  1.000 80.61526  ? 392 THR   B CB    1 
ATOM   6391 O OG1   . THR   B 1 392 ? 73.19694  45.66485  12.34005  1.000 90.53278  ? 392 THR   B OG1   1 
ATOM   6392 C CG2   . THR   B 1 392 ? 74.45946  43.67581  12.47475  1.000 75.79000  ? 392 THR   B CG2   1 
ATOM   6393 N N     . SER   B 1 393 ? 74.61434  46.25173  9.35132   1.000 71.54790  ? 393 SER   B N     1 
ATOM   6394 C CA    . SER   B 1 393 ? 75.78520  47.08275  9.04055   1.000 76.32268  ? 393 SER   B CA    1 
ATOM   6395 C C     . SER   B 1 393 ? 76.41052  47.59285  10.32923  1.000 83.94519  ? 393 SER   B C     1 
ATOM   6396 O O     . SER   B 1 393 ? 75.98151  48.61109  10.88101  1.000 92.56494  ? 393 SER   B O     1 
ATOM   6397 C CB    . SER   B 1 393 ? 75.39745  48.25653  8.14951   1.000 84.46223  ? 393 SER   B CB    1 
ATOM   6398 O OG    . SER   B 1 393 ? 76.37926  49.28964  8.21607   1.000 77.70449  ? 393 SER   B OG    1 
ATOM   6399 N N     . GLY   B 1 394 ? 77.45813  46.92848  10.79321  1.000 83.77917  ? 394 GLY   B N     1 
ATOM   6400 C CA    . GLY   B 1 394 ? 77.97477  47.23335  12.11052  1.000 80.17465  ? 394 GLY   B CA    1 
ATOM   6401 C C     . GLY   B 1 394 ? 77.22322  46.49310  13.21359  1.000 79.94025  ? 394 GLY   B C     1 
ATOM   6402 O O     . GLY   B 1 394 ? 76.29771  45.68451  12.96564  1.000 70.37823  ? 394 GLY   B O     1 
ATOM   6403 N N     . ASP   B 1 395 ? 77.61656  46.79843  14.45789  1.000 81.66974  ? 395 ASP   B N     1 
ATOM   6404 C CA    . ASP   B 1 395 ? 77.24799  45.95643  15.58910  1.000 77.53132  ? 395 ASP   B CA    1 
ATOM   6405 C C     . ASP   B 1 395 ? 75.76121  45.66178  15.58774  1.000 77.57511  ? 395 ASP   B C     1 
ATOM   6406 O O     . ASP   B 1 395 ? 74.94055  46.44782  15.10532  1.000 79.59624  ? 395 ASP   B O     1 
ATOM   6407 C CB    . ASP   B 1 395 ? 77.59366  46.59875  16.91639  1.000 78.53689  ? 395 ASP   B CB    1 
ATOM   6408 C CG    . ASP   B 1 395 ? 79.01791  47.01171  17.00521  1.000 80.11779  ? 395 ASP   B CG    1 
ATOM   6409 O OD1   . ASP   B 1 395 ? 79.76683  46.73002  16.05597  1.000 82.51930  ? 395 ASP   B OD1   1 
ATOM   6410 O OD2   . ASP   B 1 395 ? 79.39153  47.60836  18.03862  1.000 85.00308  ? 395 ASP   B OD2   1 
ATOM   6411 N N     . LEU   B 1 396 ? 75.43128  44.50958  16.14838  1.000 79.05455  ? 396 LEU   B N     1 
ATOM   6412 C CA    . LEU   B 1 396 ? 74.04701  44.13399  16.34571  1.000 76.79348  ? 396 LEU   B CA    1 
ATOM   6413 C C     . LEU   B 1 396 ? 73.45210  44.98772  17.45670  1.000 82.89359  ? 396 LEU   B C     1 
ATOM   6414 O O     . LEU   B 1 396 ? 74.15238  45.42644  18.37681  1.000 87.04932  ? 396 LEU   B O     1 
ATOM   6415 C CB    . LEU   B 1 396 ? 73.97007  42.65347  16.68588  1.000 60.62362  ? 396 LEU   B CB    1 
ATOM   6416 C CG    . LEU   B 1 396 ? 72.60719  42.07487  16.94511  1.000 71.37197  ? 396 LEU   B CG    1 
ATOM   6417 C CD1   . LEU   B 1 396 ? 71.74721  42.04075  15.68662  1.000 77.38956  ? 396 LEU   B CD1   1 
ATOM   6418 C CD2   . LEU   B 1 396 ? 72.83019  40.68919  17.46124  1.000 76.00838  ? 396 LEU   B CD2   1 
ATOM   6419 N N     . THR   B 1 397 ? 72.16666  45.27960  17.34493  1.000 80.52153  ? 397 THR   B N     1 
ATOM   6420 C CA    . THR   B 1 397 ? 71.49100  46.01685  18.39518  1.000 79.21788  ? 397 THR   B CA    1 
ATOM   6421 C C     . THR   B 1 397 ? 70.25800  45.25552  18.82343  1.000 84.15270  ? 397 THR   B C     1 
ATOM   6422 O O     . THR   B 1 397 ? 69.80463  44.32006  18.15137  1.000 84.56048  ? 397 THR   B O     1 
ATOM   6423 C CB    . THR   B 1 397 ? 71.12044  47.46368  17.98804  1.000 81.87002  ? 397 THR   B CB    1 
ATOM   6424 O OG1   . THR   B 1 397 ? 70.15059  47.45280  16.93365  1.000 88.78113  ? 397 THR   B OG1   1 
ATOM   6425 C CG2   . THR   B 1 397 ? 72.33955  48.28468  17.60629  1.000 75.22934  ? 397 THR   B CG2   1 
ATOM   6426 N N     . ASP   B 1 398 ? 69.76424  45.65078  19.99541  1.000 91.30370  ? 398 ASP   B N     1 
ATOM   6427 C CA    . ASP   B 1 398 ? 68.54162  45.07877  20.54708  1.000 99.82664  ? 398 ASP   B CA    1 
ATOM   6428 C C     . ASP   B 1 398 ? 67.43382  45.07159  19.48363  1.000 94.43086  ? 398 ASP   B C     1 
ATOM   6429 O O     . ASP   B 1 398 ? 66.73636  44.06041  19.30165  1.000 89.25618  ? 398 ASP   B O     1 
ATOM   6430 C CB    . ASP   B 1 398 ? 68.17501  45.89285  21.81531  1.000 109.26454 ? 398 ASP   B CB    1 
ATOM   6431 C CG    . ASP   B 1 398 ? 66.95407  45.34687  22.57568  1.000 113.23126 ? 398 ASP   B CG    1 
ATOM   6432 O OD1   . ASP   B 1 398 ? 67.03593  44.21651  23.11442  1.000 112.58866 ? 398 ASP   B OD1   1 
ATOM   6433 O OD2   . ASP   B 1 398 ? 65.92149  46.06288  22.64879  1.000 111.57866 ? 398 ASP   B OD2   1 
ATOM   6434 N N     . THR   B 1 399 ? 67.32861  46.17867  18.71957  1.000 93.60767  ? 399 THR   B N     1 
ATOM   6435 C CA    . THR   B 1 399 ? 66.33489  46.37097  17.65525  1.000 89.95187  ? 399 THR   B CA    1 
ATOM   6436 C C     . THR   B 1 399 ? 66.19353  45.12319  16.79436  1.000 90.44640  ? 399 THR   B C     1 
ATOM   6437 O O     . THR   B 1 399 ? 65.07551  44.68391  16.48171  1.000 83.20895  ? 399 THR   B O     1 
ATOM   6438 C CB    . THR   B 1 399 ? 66.73623  47.57247  16.77175  1.000 87.23704  ? 399 THR   B CB    1 
ATOM   6439 O OG1   . THR   B 1 399 ? 67.07952  48.70573  17.57615  1.000 82.56969  ? 399 THR   B OG1   1 
ATOM   6440 C CG2   . THR   B 1 399 ? 65.58996  47.99713  15.84106  1.000 93.59869  ? 399 THR   B CG2   1 
ATOM   6441 N N     . THR   B 1 400 ? 67.34965  44.56234  16.40345  1.000 94.39191  ? 400 THR   B N     1 
ATOM   6442 C CA    . THR   B 1 400 ? 67.43532  43.40874  15.51139  1.000 94.22573  ? 400 THR   B CA    1 
ATOM   6443 C C     . THR   B 1 400 ? 67.20622  42.10004  16.26851  1.000 94.22619  ? 400 THR   B C     1 
ATOM   6444 O O     . THR   B 1 400 ? 66.49884  41.20896  15.77408  1.000 91.95148  ? 400 THR   B O     1 
ATOM   6445 C CB    . THR   B 1 400 ? 68.80090  43.39388  14.82221  1.000 87.29746  ? 400 THR   B CB    1 
ATOM   6446 O OG1   . THR   B 1 400 ? 69.07553  44.68741  14.26844  1.000 87.04320  ? 400 THR   B OG1   1 
ATOM   6447 C CG2   . THR   B 1 400 ? 68.79185  42.39336  13.68992  1.000 83.70247  ? 400 THR   B CG2   1 
ATOM   6448 N N     . VAL   B 1 401 ? 67.80720  41.97154  17.46021  1.000 92.17769  ? 401 VAL   B N     1 
ATOM   6449 C CA    . VAL   B 1 401 ? 67.48038  40.86316  18.35947  1.000 93.60121  ? 401 VAL   B CA    1 
ATOM   6450 C C     . VAL   B 1 401 ? 65.97371  40.75219  18.50177  1.000 93.90282  ? 401 VAL   B C     1 
ATOM   6451 O O     . VAL   B 1 401 ? 65.35708  39.72132  18.19137  1.000 89.36542  ? 401 VAL   B O     1 
ATOM   6452 C CB    . VAL   B 1 401 ? 68.12606  41.07445  19.74055  1.000 91.32151  ? 401 VAL   B CB    1 
ATOM   6453 C CG1   . VAL   B 1 401 ? 67.81586  39.89614  20.67458  1.000 90.74567  ? 401 VAL   B CG1   1 
ATOM   6454 C CG2   . VAL   B 1 401 ? 69.59837  41.31897  19.62039  1.000 84.13055  ? 401 VAL   B CG2   1 
ATOM   6455 N N     . GLN   B 1 402 ? 65.37225  41.83495  18.99581  1.000 94.86338  ? 402 GLN   B N     1 
ATOM   6456 C CA    . GLN   B 1 402 ? 63.94255  41.85185  19.24787  1.000 94.97473  ? 402 GLN   B CA    1 
ATOM   6457 C C     . GLN   B 1 402 ? 63.16678  41.51806  17.98247  1.000 96.72835  ? 402 GLN   B C     1 
ATOM   6458 O O     . GLN   B 1 402 ? 62.13854  40.83658  18.05157  1.000 100.03064 ? 402 GLN   B O     1 
ATOM   6459 C CB    . GLN   B 1 402 ? 63.53566  43.22308  19.78990  1.000 95.71521  ? 402 GLN   B CB    1 
ATOM   6460 C CG    . GLN   B 1 402 ? 64.21944  43.66291  21.11595  1.000 96.96252  ? 402 GLN   B CG    1 
ATOM   6461 C CD    . GLN   B 1 402 ? 63.74618  42.92179  22.37552  1.000 98.12450  ? 402 GLN   B CD    1 
ATOM   6462 O OE1   . GLN   B 1 402 ? 62.54633  42.73547  22.59329  1.000 99.01613  ? 402 GLN   B OE1   1 
ATOM   6463 N NE2   . GLN   B 1 402 ? 64.70160  42.54887  23.23812  1.000 93.77353  ? 402 GLN   B NE2   1 
ATOM   6464 N N     . PHE   B 1 403 ? 63.65429  41.97716  16.82233  1.000 92.64096  ? 403 PHE   B N     1 
ATOM   6465 C CA    . PHE   B 1 403 ? 62.91673  41.79018  15.57919  1.000 95.59355  ? 403 PHE   B CA    1 
ATOM   6466 C C     . PHE   B 1 403 ? 62.73003  40.30563  15.28853  1.000 98.39075  ? 403 PHE   B C     1 
ATOM   6467 O O     . PHE   B 1 403 ? 61.62805  39.85180  14.94272  1.000 97.26432  ? 403 PHE   B O     1 
ATOM   6468 C CB    . PHE   B 1 403 ? 63.65314  42.49649  14.43008  1.000 100.02404 ? 403 PHE   B CB    1 
ATOM   6469 C CG    . PHE   B 1 403 ? 63.06771  42.23731  13.04428  1.000 99.44881  ? 403 PHE   B CG    1 
ATOM   6470 C CD1   . PHE   B 1 403 ? 61.94173  42.90314  12.60171  1.000 97.30248  ? 403 PHE   B CD1   1 
ATOM   6471 C CD2   . PHE   B 1 403 ? 63.66429  41.33270  12.18664  1.000 94.99010  ? 403 PHE   B CD2   1 
ATOM   6472 C CE1   . PHE   B 1 403 ? 61.42523  42.66520  11.33390  1.000 98.83567  ? 403 PHE   B CE1   1 
ATOM   6473 C CE2   . PHE   B 1 403 ? 63.14758  41.09285  10.93298  1.000 91.58712  ? 403 PHE   B CE2   1 
ATOM   6474 C CZ    . PHE   B 1 403 ? 62.02829  41.76160  10.50600  1.000 96.18866  ? 403 PHE   B CZ    1 
ATOM   6475 N N     . LEU   B 1 404 ? 63.79719  39.52684  15.44695  1.000 97.34538  ? 404 LEU   B N     1 
ATOM   6476 C CA    . LEU   B 1 404 ? 63.70723  38.10254  15.15257  1.000 101.80280 ? 404 LEU   B CA    1 
ATOM   6477 C C     . LEU   B 1 404 ? 62.98950  37.34570  16.24078  1.000 101.69864 ? 404 LEU   B C     1 
ATOM   6478 O O     . LEU   B 1 404 ? 62.37269  36.30550  15.95972  1.000 100.77248 ? 404 LEU   B O     1 
ATOM   6479 C CB    . LEU   B 1 404 ? 65.09830  37.51109  14.94525  1.000 104.63866 ? 404 LEU   B CB    1 
ATOM   6480 C CG    . LEU   B 1 404 ? 65.69570  37.85729  13.59291  1.000 102.39866 ? 404 LEU   B CG    1 
ATOM   6481 C CD1   . LEU   B 1 404 ? 67.16186  37.51815  13.60142  1.000 107.00866 ? 404 LEU   B CD1   1 
ATOM   6482 C CD2   . LEU   B 1 404 ? 64.93228  37.05801  12.54074  1.000 93.04866  ? 404 LEU   B CD2   1 
ATOM   6483 N N     . ASP   B 1 405 ? 63.09502  37.83677  17.47992  1.000 101.19789 ? 405 ASP   B N     1 
ATOM   6484 C CA    . ASP   B 1 405 ? 62.30966  37.28748  18.57666  1.000 96.55357  ? 405 ASP   B CA    1 
ATOM   6485 C C     . ASP   B 1 405 ? 60.83115  37.50284  18.31407  1.000 98.59823  ? 405 ASP   B C     1 
ATOM   6486 O O     . ASP   B 1 405 ? 60.05333  36.54498  18.21294  1.000 98.77404  ? 405 ASP   B O     1 
ATOM   6487 C CB    . ASP   B 1 405 ? 62.73759  37.95190  19.87732  1.000 95.38969  ? 405 ASP   B CB    1 
ATOM   6488 C CG    . ASP   B 1 405 ? 64.05120  37.42397  20.36698  1.000 100.66646 ? 405 ASP   B CG    1 
ATOM   6489 O OD1   . ASP   B 1 405 ? 64.11467  36.23853  20.77479  1.000 97.36326  ? 405 ASP   B OD1   1 
ATOM   6490 O OD2   . ASP   B 1 405 ? 65.03552  38.19325  20.30433  1.000 101.07973 ? 405 ASP   B OD2   1 
ATOM   6491 N N     . GLY   B 1 406 ? 60.44195  38.77061  18.14483  1.000 94.84846  ? 406 GLY   B N     1 
ATOM   6492 C CA    . GLY   B 1 406 ? 59.09107  39.07666  17.70475  1.000 99.22892  ? 406 GLY   B CA    1 
ATOM   6493 C C     . GLY   B 1 406 ? 58.65736  38.23975  16.51749  1.000 105.52281 ? 406 GLY   B C     1 
ATOM   6494 O O     . GLY   B 1 406 ? 57.59787  37.60593  16.54014  1.000 108.88763 ? 406 GLY   B O     1 
ATOM   6495 N N     . LEU   B 1 407 ? 59.46380  38.22622  15.45588  1.000 101.08884 ? 407 LEU   B N     1 
ATOM   6496 C CA    . LEU   B 1 407 ? 59.15364  37.33382  14.34977  1.000 99.76942  ? 407 LEU   B CA    1 
ATOM   6497 C C     . LEU   B 1 407 ? 58.93509  35.91499  14.86073  1.000 99.30922  ? 407 LEU   B C     1 
ATOM   6498 O O     . LEU   B 1 407 ? 57.91768  35.28167  14.56048  1.000 99.29047  ? 407 LEU   B O     1 
ATOM   6499 C CB    . LEU   B 1 407 ? 60.27695  37.36454  13.31500  1.000 101.28265 ? 407 LEU   B CB    1 
ATOM   6500 C CG    . LEU   B 1 407 ? 60.16717  36.25786  12.26082  1.000 94.71959  ? 407 LEU   B CG    1 
ATOM   6501 C CD1   . LEU   B 1 407 ? 58.82104  36.26619  11.53864  1.000 85.88837  ? 407 LEU   B CD1   1 
ATOM   6502 C CD2   . LEU   B 1 407 ? 61.30922  36.36001  11.29295  1.000 96.17372  ? 407 LEU   B CD2   1 
ATOM   6503 N N     . SER   B 1 408 ? 59.87953  35.41085  15.65957  1.000 99.10980  ? 408 SER   B N     1 
ATOM   6504 C CA    . SER   B 1 408 ? 59.76466  34.05588  16.18531  1.000 100.43690 ? 408 SER   B CA    1 
ATOM   6505 C C     . SER   B 1 408 ? 58.38784  33.82066  16.78351  1.000 104.25114 ? 408 SER   B C     1 
ATOM   6506 O O     . SER   B 1 408 ? 57.72712  32.82041  16.47056  1.000 108.65834 ? 408 SER   B O     1 
ATOM   6507 C CB    . SER   B 1 408 ? 60.86151  33.80459  17.21804  1.000 99.80966  ? 408 SER   B CB    1 
ATOM   6508 O OG    . SER   B 1 408 ? 62.14069  34.00206  16.63123  1.000 99.46709  ? 408 SER   B OG    1 
ATOM   6509 N N     . GLU   B 1 409 ? 57.92912  34.75355  17.62889  1.000 105.70416 ? 409 GLU   B N     1 
ATOM   6510 C CA    . GLU   B 1 409 ? 56.57433  34.67572  18.17377  1.000 105.13308 ? 409 GLU   B CA    1 
ATOM   6511 C C     . GLU   B 1 409 ? 55.53730  34.67747  17.05274  1.000 104.04213 ? 409 GLU   B C     1 
ATOM   6512 O O     . GLU   B 1 409 ? 54.85401  33.67212  16.80888  1.000 104.06118 ? 409 GLU   B O     1 
ATOM   6513 C CB    . GLU   B 1 409 ? 56.32151  35.82426  19.17105  1.000 102.76393 ? 409 GLU   B CB    1 
ATOM   6514 C CG    . GLU   B 1 409 ? 57.38674  35.95305  20.29566  1.000 114.23085 ? 409 GLU   B CG    1 
ATOM   6515 C CD    . GLU   B 1 409 ? 57.36988  37.30214  21.05398  1.000 125.65688 ? 409 GLU   B CD    1 
ATOM   6516 O OE1   . GLU   B 1 409 ? 56.35369  38.02911  20.94477  1.000 129.77299 ? 409 GLU   B OE1   1 
ATOM   6517 O OE2   . GLU   B 1 409 ? 58.36860  37.63105  21.76244  1.000 122.03856 ? 409 GLU   B OE2   1 
ATOM   6518 N N     . VAL   B 1 410 ? 55.44744  35.78443  16.31740  1.000 103.36901 ? 410 VAL   B N     1 
ATOM   6519 C CA    . VAL   B 1 410 ? 54.39314  35.98764  15.32524  1.000 101.31246 ? 410 VAL   B CA    1 
ATOM   6520 C C     . VAL   B 1 410 ? 54.24448  34.78318  14.38607  1.000 100.22321 ? 410 VAL   B C     1 
ATOM   6521 O O     . VAL   B 1 410 ? 53.18929  34.60237  13.76688  1.000 101.16309 ? 410 VAL   B O     1 
ATOM   6522 C CB    . VAL   B 1 410 ? 54.65727  37.31091  14.57319  1.000 103.51102 ? 410 VAL   B CB    1 
ATOM   6523 C CG1   . VAL   B 1 410 ? 55.64407  37.11981  13.42757  1.000 105.46269 ? 410 VAL   B CG1   1 
ATOM   6524 C CG2   . VAL   B 1 410 ? 53.34876  37.95376  14.12062  1.000 103.59280 ? 410 VAL   B CG2   1 
ATOM   6525 N N     . LEU   B 1 411 ? 55.27976  33.93948  14.29447  1.000 103.82603 ? 411 LEU   B N     1 
ATOM   6526 C CA    . LEU   B 1 411 ? 55.19204  32.64780  13.61008  1.000 107.68759 ? 411 LEU   B CA    1 
ATOM   6527 C C     . LEU   B 1 411 ? 54.43331  31.63267  14.43834  1.000 107.10999 ? 411 LEU   B C     1 
ATOM   6528 O O     . LEU   B 1 411 ? 53.69803  30.78645  13.90366  1.000 108.34404 ? 411 LEU   B O     1 
ATOM   6529 C CB    . LEU   B 1 411 ? 56.58992  32.10089  13.34401  1.000 106.26064 ? 411 LEU   B CB    1 
ATOM   6530 C CG    . LEU   B 1 411 ? 57.39016  32.86846  12.31739  1.000 103.68866 ? 411 LEU   B CG    1 
ATOM   6531 C CD1   . LEU   B 1 411 ? 58.85314  32.60532  12.54446  1.000 106.57866 ? 411 LEU   B CD1   1 
ATOM   6532 C CD2   . LEU   B 1 411 ? 56.94087  32.37284  10.95224  1.000 107.27866 ? 411 LEU   B CD2   1 
ATOM   6533 N N     . THR   B 1 412 ? 54.64168  31.70337  15.74241  1.000 103.99604 ? 412 THR   B N     1 
ATOM   6534 C CA    . THR   B 1 412 ? 54.09959  30.74119  16.66863  1.000 107.99091 ? 412 THR   B CA    1 
ATOM   6535 C C     . THR   B 1 412 ? 52.66120  31.04786  17.07923  1.000 114.41709 ? 412 THR   B C     1 
ATOM   6536 O O     . THR   B 1 412 ? 51.97874  30.13292  17.55851  1.000 135.52866 ? 412 THR   B O     1 
ATOM   6537 C CB    . THR   B 1 412 ? 55.03986  30.67454  17.86655  1.000 103.49048 ? 412 THR   B CB    1 
ATOM   6538 O OG1   . THR   B 1 412 ? 55.05992  31.93869  18.53032  1.000 97.07491  ? 412 THR   B OG1   1 
ATOM   6539 C CG2   . THR   B 1 412 ? 56.42903  30.40940  17.35628  1.000 99.63850  ? 412 THR   B CG2   1 
ATOM   6540 N N     . SER   B 1 413 ? 52.15083  32.27829  16.84500  1.000 112.14489 ? 413 SER   B N     1 
ATOM   6541 C CA    . SER   B 1 413 ? 50.77844  32.63566  17.23382  1.000 103.87497 ? 413 SER   B CA    1 
ATOM   6542 C C     . SER   B 1 413 ? 49.74919  31.61055  16.76288  1.000 106.80777 ? 413 SER   B C     1 
ATOM   6543 O O     . SER   B 1 413 ? 48.67144  31.51994  17.36471  1.000 102.53004 ? 413 SER   B O     1 
ATOM   6544 C CB    . SER   B 1 413 ? 50.35774  34.01461  16.70107  1.000 97.58140  ? 413 SER   B CB    1 
ATOM   6545 O OG    . SER   B 1 413 ? 50.91274  34.30769  15.42669  1.000 108.64434 ? 413 SER   B OG    1 
ATOM   6546 N N     . GLY   B 1 414 ? 50.04544  30.87190  15.68565  1.000 106.61841 ? 414 GLY   B N     1 
ATOM   6547 C CA    . GLY   B 1 414 ? 49.32771  29.65363  15.33756  1.000 105.03825 ? 414 GLY   B CA    1 
ATOM   6548 C C     . GLY   B 1 414 ? 48.84776  28.85746  16.53952  1.000 105.53468 ? 414 GLY   B C     1 
ATOM   6549 O O     . GLY   B 1 414 ? 47.65242  28.85445  16.83484  1.000 107.68186 ? 414 GLY   B O     1 
ATOM   6550 N N     . GLN   B 1 415 ? 49.76957  28.17524  17.23429  1.000 108.79042 ? 415 GLN   B N     1 
ATOM   6551 C CA    . GLN   B 1 415 ? 49.50977  27.50712  18.51463  1.000 101.11391 ? 415 GLN   B CA    1 
ATOM   6552 C C     . GLN   B 1 415 ? 50.58616  27.93019  19.50011  1.000 105.82588 ? 415 GLN   B C     1 
ATOM   6553 O O     . GLN   B 1 415 ? 51.50972  27.15385  19.79481  1.000 105.18439 ? 415 GLN   B O     1 
ATOM   6554 C CB    . GLN   B 1 415 ? 49.54334  25.99201  18.37537  1.000 94.65098  ? 415 GLN   B CB    1 
ATOM   6555 C CG    . GLN   B 1 415 ? 48.46730  25.45457  17.56121  1.000 96.39179  ? 415 GLN   B CG    1 
ATOM   6556 C CD    . GLN   B 1 415 ? 48.90916  24.20625  16.92416  1.000 94.09575  ? 415 GLN   B CD    1 
ATOM   6557 O OE1   . GLN   B 1 415 ? 49.44344  23.33795  17.58744  1.000 92.57672  ? 415 GLN   B OE1   1 
ATOM   6558 N NE2   . GLN   B 1 415 ? 48.69232  24.09041  15.62550  1.000 96.08940  ? 415 GLN   B NE2   1 
ATOM   6559 N N     . PRO   B 1 416 ? 50.48809  29.14363  20.05522  1.000 108.28653 ? 416 PRO   B N     1 
ATOM   6560 C CA    . PRO   B 1 416 ? 51.64771  29.74332  20.73566  1.000 109.34705 ? 416 PRO   B CA    1 
ATOM   6561 C C     . PRO   B 1 416 ? 52.33614  28.84976  21.75182  1.000 116.30016 ? 416 PRO   B C     1 
ATOM   6562 O O     . PRO   B 1 416 ? 53.44960  29.16512  22.17836  1.000 116.88679 ? 416 PRO   B O     1 
ATOM   6563 C CB    . PRO   B 1 416 ? 51.05384  30.98183  21.42361  1.000 101.97062 ? 416 PRO   B CB    1 
ATOM   6564 C CG    . PRO   B 1 416 ? 49.62224  30.74052  21.49872  1.000 103.42382 ? 416 PRO   B CG    1 
ATOM   6565 C CD    . PRO   B 1 416 ? 49.26606  29.93231  20.27772  1.000 105.67141 ? 416 PRO   B CD    1 
ATOM   6566 N N     . ASP   B 1 417 ? 51.70449  27.74341  22.14928  1.000 120.73279 ? 417 ASP   B N     1 
ATOM   6567 C CA    . ASP   B 1 417 ? 52.23232  26.90637  23.22142  1.000 119.95411 ? 417 ASP   B CA    1 
ATOM   6568 C C     . ASP   B 1 417 ? 52.59654  25.48364  22.79096  1.000 110.26905 ? 417 ASP   B C     1 
ATOM   6569 O O     . ASP   B 1 417 ? 53.01195  24.69313  23.64177  1.000 110.56194 ? 417 ASP   B O     1 
ATOM   6570 C CB    . ASP   B 1 417 ? 51.23704  26.84425  24.40483  1.000 118.76976 ? 417 ASP   B CB    1 
ATOM   6571 C CG    . ASP   B 1 417 ? 50.76723  28.24262  24.89798  1.000 122.79637 ? 417 ASP   B CG    1 
ATOM   6572 O OD1   . ASP   B 1 417 ? 51.59139  29.05890  25.40272  1.000 116.26129 ? 417 ASP   B OD1   1 
ATOM   6573 O OD2   . ASP   B 1 417 ? 49.54454  28.51045  24.78255  1.000 121.86565 ? 417 ASP   B OD2   1 
ATOM   6574 N N     . ALA   B 1 418 ? 52.48206  25.12881  21.51431  1.000 104.46724 ? 418 ALA   B N     1 
ATOM   6575 C CA    . ALA   B 1 418 ? 52.84382  23.77583  21.11004  1.000 111.06076 ? 418 ALA   B CA    1 
ATOM   6576 C C     . ALA   B 1 418 ? 54.37386  23.58613  21.17487  1.000 116.62251 ? 418 ALA   B C     1 
ATOM   6577 O O     . ALA   B 1 418 ? 55.13135  24.54134  21.38234  1.000 108.32342 ? 418 ALA   B O     1 
ATOM   6578 C CB    . ALA   B 1 418 ? 52.28496  23.48793  19.71528  1.000 108.46063 ? 418 ALA   B CB    1 
ATOM   6579 N N     . TYR   B 1 419 ? 54.83789  22.32872  21.01539  1.000 121.23609 ? 419 TYR   B N     1 
ATOM   6580 C CA    . TYR   B 1 419 ? 56.27978  22.03280  21.00418  1.000 113.91309 ? 419 TYR   B CA    1 
ATOM   6581 C C     . TYR   B 1 419 ? 56.88280  22.42455  19.66196  1.000 113.10674 ? 419 TYR   B C     1 
ATOM   6582 O O     . TYR   B 1 419 ? 56.62858  21.78011  18.62804  1.000 102.06459 ? 419 TYR   B O     1 
ATOM   6583 C CB    . TYR   B 1 419 ? 56.59886  20.56487  21.30167  1.000 120.20132 ? 419 TYR   B CB    1 
ATOM   6584 C CG    . TYR   B 1 419 ? 58.10650  20.28610  21.20806  1.000 115.51866 ? 419 TYR   B CG    1 
ATOM   6585 C CD1   . TYR   B 1 419 ? 59.02027  21.14069  21.82288  1.000 103.44382 ? 419 TYR   B CD1   1 
ATOM   6586 C CD2   . TYR   B 1 419 ? 58.61542  19.19403  20.48810  1.000 108.13057 ? 419 TYR   B CD2   1 
ATOM   6587 C CE1   . TYR   B 1 419 ? 60.39387  20.92586  21.73723  1.000 98.32866  ? 419 TYR   B CE1   1 
ATOM   6588 C CE2   . TYR   B 1 419 ? 60.00320  18.96856  20.40005  1.000 102.86866 ? 419 TYR   B CE2   1 
ATOM   6589 C CZ    . TYR   B 1 419 ? 60.88712  19.84726  21.03444  1.000 103.34866 ? 419 TYR   B CZ    1 
ATOM   6590 O OH    . TYR   B 1 419 ? 62.26519  19.67539  20.98714  1.000 92.13285  ? 419 TYR   B OH    1 
ATOM   6591 N N     . TYR   B 1 420 ? 57.71691  23.46259  19.70487  1.000 113.99656 ? 420 TYR   B N     1 
ATOM   6592 C CA    . TYR   B 1 420 ? 58.37771  24.04698  18.54507  1.000 113.63667 ? 420 TYR   B CA    1 
ATOM   6593 C C     . TYR   B 1 420 ? 59.86511  23.71564  18.67886  1.000 110.11141 ? 420 TYR   B C     1 
ATOM   6594 O O     . TYR   B 1 420 ? 60.54511  24.22579  19.58055  1.000 95.90051  ? 420 TYR   B O     1 
ATOM   6595 C CB    . TYR   B 1 420 ? 58.13252  25.56187  18.50944  1.000 107.09264 ? 420 TYR   B CB    1 
ATOM   6596 C CG    . TYR   B 1 420 ? 56.79669  26.02425  17.92120  1.000 104.52773 ? 420 TYR   B CG    1 
ATOM   6597 C CD1   . TYR   B 1 420 ? 56.35910  25.57409  16.68002  1.000 105.22299 ? 420 TYR   B CD1   1 
ATOM   6598 C CD2   . TYR   B 1 420 ? 55.99624  26.95390  18.59053  1.000 98.19911  ? 420 TYR   B CD2   1 
ATOM   6599 C CE1   . TYR   B 1 420 ? 55.14628  26.01256  16.13432  1.000 106.79508 ? 420 TYR   B CE1   1 
ATOM   6600 C CE2   . TYR   B 1 420 ? 54.78771  27.39671  18.05200  1.000 101.71491 ? 420 TYR   B CE2   1 
ATOM   6601 C CZ    . TYR   B 1 420 ? 54.36847  26.92615  16.82023  1.000 106.83435 ? 420 TYR   B CZ    1 
ATOM   6602 O OH    . TYR   B 1 420 ? 53.17704  27.36009  16.26067  1.000 105.32642 ? 420 TYR   B OH    1 
ATOM   6603 N N     . GLY   B 1 421 ? 60.36486  22.83651  17.80979  1.000 107.11381 ? 421 GLY   B N     1 
ATOM   6604 C CA    . GLY   B 1 421 ? 61.77828  22.44877  17.88224  1.000 105.16866 ? 421 GLY   B CA    1 
ATOM   6605 C C     . GLY   B 1 421 ? 62.71581  23.49883  17.28180  1.000 97.44866  ? 421 GLY   B C     1 
ATOM   6606 O O     . GLY   B 1 421 ? 62.39762  24.15195  16.28969  1.000 108.90866 ? 421 GLY   B O     1 
ATOM   6607 N N     . GLN   B 1 422 ? 63.88739  23.66123  17.90362  1.000 84.12503  ? 422 GLN   B N     1 
ATOM   6608 C CA    . GLN   B 1 422 ? 65.02768  24.33789  17.30143  1.000 78.29051  ? 422 GLN   B CA    1 
ATOM   6609 C C     . GLN   B 1 422 ? 65.98402  23.31254  16.67297  1.000 86.77209  ? 422 GLN   B C     1 
ATOM   6610 O O     . GLN   B 1 422 ? 65.92757  22.11178  16.97421  1.000 87.08469  ? 422 GLN   B O     1 
ATOM   6611 C CB    . GLN   B 1 422 ? 65.74745  25.18592  18.35729  1.000 74.16009  ? 422 GLN   B CB    1 
ATOM   6612 C CG    . GLN   B 1 422 ? 64.99760  26.45787  18.77399  1.000 77.70749  ? 422 GLN   B CG    1 
ATOM   6613 C CD    . GLN   B 1 422 ? 65.86852  27.54769  19.44093  1.000 77.98567  ? 422 GLN   B CD    1 
ATOM   6614 O OE1   . GLN   B 1 422 ? 65.88359  27.63635  20.66595  1.000 77.97043  ? 422 GLN   B OE1   1 
ATOM   6615 N NE2   . GLN   B 1 422 ? 66.52903  28.40794  18.64384  1.000 88.97433  ? 422 GLN   B NE2   1 
ATOM   6616 N N     . TYR   B 1 423 ? 66.84544  23.79593  15.75025  1.000 86.70295  ? 423 TYR   B N     1 
ATOM   6617 C CA    . TYR   B 1 423 ? 67.85486  22.97166  15.06843  1.000 80.68124  ? 423 TYR   B CA    1 
ATOM   6618 C C     . TYR   B 1 423 ? 69.23878  23.23642  15.63364  1.000 77.75374  ? 423 TYR   B C     1 
ATOM   6619 O O     . TYR   B 1 423 ? 69.68354  24.38969  15.66860  1.000 74.31263  ? 423 TYR   B O     1 
ATOM   6620 C CB    . TYR   B 1 423 ? 67.89397  23.22502  13.55975  1.000 80.37123  ? 423 TYR   B CB    1 
ATOM   6621 C CG    . TYR   B 1 423 ? 68.93507  22.37381  12.84035  1.000 79.60918  ? 423 TYR   B CG    1 
ATOM   6622 C CD1   . TYR   B 1 423 ? 69.03773  21.01666  13.08912  1.000 80.68831  ? 423 TYR   B CD1   1 
ATOM   6623 C CD2   . TYR   B 1 423 ? 69.84182  22.94138  11.94029  1.000 82.46947  ? 423 TYR   B CD2   1 
ATOM   6624 C CE1   . TYR   B 1 423 ? 69.98465  20.22962  12.44213  1.000 82.86674  ? 423 TYR   B CE1   1 
ATOM   6625 C CE2   . TYR   B 1 423 ? 70.80417  22.16376  11.29038  1.000 79.69431  ? 423 TYR   B CE2   1 
ATOM   6626 C CZ    . TYR   B 1 423 ? 70.86756  20.79933  11.54459  1.000 80.88107  ? 423 TYR   B CZ    1 
ATOM   6627 O OH    . TYR   B 1 423 ? 71.80048  19.98719  10.91562  1.000 74.62963  ? 423 TYR   B OH    1 
ATOM   6628 N N     . VAL   B 1 424 ? 69.94229  22.16395  16.02465  1.000 78.61979  ? 424 VAL   B N     1 
ATOM   6629 C CA    . VAL   B 1 424 ? 71.17806  22.35248  16.80524  1.000 77.57533  ? 424 VAL   B CA    1 
ATOM   6630 C C     . VAL   B 1 424 ? 72.30472  22.89422  15.92916  1.000 85.11976  ? 424 VAL   B C     1 
ATOM   6631 O O     . VAL   B 1 424 ? 73.21523  23.56542  16.44904  1.000 80.82039  ? 424 VAL   B O     1 
ATOM   6632 C CB    . VAL   B 1 424 ? 71.58933  21.04904  17.51341  1.000 72.31922  ? 424 VAL   B CB    1 
ATOM   6633 C CG1   . VAL   B 1 424 ? 71.87867  19.94229  16.51903  1.000 74.30776  ? 424 VAL   B CG1   1 
ATOM   6634 C CG2   . VAL   B 1 424 ? 72.76225  21.30340  18.42769  1.000 70.29223  ? 424 VAL   B CG2   1 
ATOM   6635 N N     . GLY   B 1 425 ? 72.27213  22.59956  14.60467  1.000 82.59808  ? 425 GLY   B N     1 
ATOM   6636 C CA    . GLY   B 1 425 ? 73.23669  23.16507  13.66984  1.000 70.45665  ? 425 GLY   B CA    1 
ATOM   6637 C C     . GLY   B 1 425 ? 73.08851  24.67106  13.51295  1.000 75.53175  ? 425 GLY   B C     1 
ATOM   6638 O O     . GLY   B 1 425 ? 74.04110  25.35614  13.11911  1.000 80.18927  ? 425 GLY   B O     1 
ATOM   6639 N N     . ASN   B 1 426 ? 71.91605  25.20800  13.81915  1.000 74.41922  ? 426 ASN   B N     1 
ATOM   6640 C CA    . ASN   B 1 426 ? 71.68840  26.65518  13.88531  1.000 76.91642  ? 426 ASN   B CA    1 
ATOM   6641 C C     . ASN   B 1 426 ? 71.46061  27.03266  15.34710  1.000 75.32371  ? 426 ASN   B C     1 
ATOM   6642 O O     . ASN   B 1 426 ? 70.32173  27.10736  15.80963  1.000 80.85825  ? 426 ASN   B O     1 
ATOM   6643 C CB    . ASN   B 1 426 ? 70.49070  27.06442  13.00421  1.000 78.00866  ? 426 ASN   B CB    1 
ATOM   6644 C CG    . ASN   B 1 426 ? 70.34375  28.58740  12.87921  1.000 83.33866  ? 426 ASN   B CG    1 
ATOM   6645 O OD1   . ASN   B 1 426 ? 70.13395  29.29886  13.87474  1.000 81.64866  ? 426 ASN   B OD1   1 
ATOM   6646 N ND2   . ASN   B 1 426 ? 70.46897  29.09149  11.65623  1.000 87.33086  ? 426 ASN   B ND2   1 
ATOM   6647 N N     . VAL   B 1 427 ? 72.54522  27.29439  16.08255  1.000 70.62074  ? 427 VAL   B N     1 
ATOM   6648 C CA    . VAL   B 1 427 ? 72.38508  27.53973  17.51932  1.000 72.76224  ? 427 VAL   B CA    1 
ATOM   6649 C C     . VAL   B 1 427 ? 71.90508  28.96785  17.75708  1.000 78.43479  ? 427 VAL   B C     1 
ATOM   6650 O O     . VAL   B 1 427 ? 71.96804  29.82171  16.87104  1.000 81.37765  ? 427 VAL   B O     1 
ATOM   6651 C CB    . VAL   B 1 427 ? 73.67762  27.24282  18.30720  1.000 70.06911  ? 427 VAL   B CB    1 
ATOM   6652 C CG1   . VAL   B 1 427 ? 74.14958  25.81118  18.03982  1.000 73.69815  ? 427 VAL   B CG1   1 
ATOM   6653 C CG2   . VAL   B 1 427 ? 74.74325  28.30154  18.03328  1.000 69.01089  ? 427 VAL   B CG2   1 
ATOM   6654 N N     . ASP   B 1 428 ? 71.40607  29.21809  18.96939  1.000 78.94358  ? 428 ASP   B N     1 
ATOM   6655 C CA    . ASP   B 1 428 ? 70.78596  30.49381  19.31804  1.000 72.91876  ? 428 ASP   B CA    1 
ATOM   6656 C C     . ASP   B 1 428 ? 71.20997  30.86887  20.73169  1.000 68.72287  ? 428 ASP   B C     1 
ATOM   6657 O O     . ASP   B 1 428 ? 70.65989  30.36652  21.72791  1.000 70.96905  ? 428 ASP   B O     1 
ATOM   6658 C CB    . ASP   B 1 428 ? 69.25968  30.41994  19.18314  1.000 75.72914  ? 428 ASP   B CB    1 
ATOM   6659 C CG    . ASP   B 1 428 ? 68.53870  31.71814  19.58019  1.000 77.26509  ? 428 ASP   B CG    1 
ATOM   6660 O OD1   . ASP   B 1 428 ? 69.12552  32.66825  20.18639  1.000 74.74443  ? 428 ASP   B OD1   1 
ATOM   6661 O OD2   . ASP   B 1 428 ? 67.37134  31.81294  19.15529  1.000 70.26570  ? 428 ASP   B OD2   1 
ATOM   6662 N N     . PRO   B 1 429 ? 72.16982  31.75999  20.85694  1.000 67.32281  ? 429 PRO   B N     1 
ATOM   6663 C CA    . PRO   B 1 429 ? 72.70744  32.10616  22.17577  1.000 76.92481  ? 429 PRO   B CA    1 
ATOM   6664 C C     . PRO   B 1 429 ? 72.15239  33.36519  22.82765  1.000 81.06651  ? 429 PRO   B C     1 
ATOM   6665 O O     . PRO   B 1 429 ? 72.82700  33.94587  23.69473  1.000 78.28997  ? 429 PRO   B O     1 
ATOM   6666 C CB    . PRO   B 1 429 ? 74.19898  32.28385  21.86907  1.000 76.65688  ? 429 PRO   B CB    1 
ATOM   6667 C CG    . PRO   B 1 429 ? 74.22226  32.86575  20.47309  1.000 70.40935  ? 429 PRO   B CG    1 
ATOM   6668 C CD    . PRO   B 1 429 ? 72.90579  32.43811  19.78735  1.000 73.74892  ? 429 PRO   B CD    1 
ATOM   6669 N N     . ARG   B 1 430 ? 70.96424  33.81630  22.43473  1.000 79.02025  ? 430 ARG   B N     1 
ATOM   6670 C CA    . ARG   B 1 430 ? 70.37336  34.99884  23.04976  1.000 81.91173  ? 430 ARG   B CA    1 
ATOM   6671 C C     . ARG   B 1 430 ? 69.05389  34.68510  23.74233  1.000 88.20546  ? 430 ARG   B C     1 
ATOM   6672 O O     . ARG   B 1 430 ? 68.35210  35.61193  24.19489  1.000 80.71702  ? 430 ARG   B O     1 
ATOM   6673 C CB    . ARG   B 1 430 ? 70.21634  36.12406  22.02232  1.000 76.15121  ? 430 ARG   B CB    1 
ATOM   6674 C CG    . ARG   B 1 430 ? 71.55733  36.62570  21.57495  1.000 72.92402  ? 430 ARG   B CG    1 
ATOM   6675 C CD    . ARG   B 1 430 ? 71.48117  37.86785  20.72155  1.000 73.35098  ? 430 ARG   B CD    1 
ATOM   6676 N NE    . ARG   B 1 430 ? 72.71213  38.05166  19.96116  1.000 71.35762  ? 430 ARG   B NE    1 
ATOM   6677 C CZ    . ARG   B 1 430 ? 73.72884  38.81075  20.35646  1.000 71.64618  ? 430 ARG   B CZ    1 
ATOM   6678 N NH1   . ARG   B 1 430 ? 73.64114  39.59890  21.42436  1.000 55.89799  ? 430 ARG   B NH1   1 
ATOM   6679 N NH2   . ARG   B 1 430 ? 74.86433  38.78300  19.66363  1.000 77.04285  ? 430 ARG   B NH2   1 
ATOM   6680 N N     . GLN   B 1 431 ? 68.72605  33.38114  23.86716  1.000 88.35577  ? 431 GLN   B N     1 
ATOM   6681 C CA    . GLN   B 1 431 ? 67.65565  32.79933  24.65686  1.000 90.70021  ? 431 GLN   B CA    1 
ATOM   6682 C C     . GLN   B 1 431 ? 68.21787  32.10759  25.90931  1.000 93.37421  ? 431 GLN   B C     1 
ATOM   6683 O O     . GLN   B 1 431 ? 69.37647  31.66818  25.90274  1.000 92.08912  ? 431 GLN   B O     1 
ATOM   6684 C CB    . GLN   B 1 431 ? 66.88710  31.76999  23.86272  1.000 77.36219  ? 431 GLN   B CB    1 
ATOM   6685 C CG    . GLN   B 1 431 ? 67.74760  30.64882  23.51480  1.000 74.49782  ? 431 GLN   B CG    1 
ATOM   6686 C CD    . GLN   B 1 431 ? 66.98121  29.60253  22.81362  1.000 79.82863  ? 431 GLN   B CD    1 
ATOM   6687 O OE1   . GLN   B 1 431 ? 67.41168  28.46426  22.73746  1.000 91.58161  ? 431 GLN   B OE1   1 
ATOM   6688 N NE2   . GLN   B 1 431 ? 65.80149  29.95123  22.34296  1.000 79.91291  ? 431 GLN   B NE2   1 
ATOM   6689 N N     . PRO   B 1 432 ? 67.41884  31.99194  26.98614  1.000 92.53254  ? 432 PRO   B N     1 
ATOM   6690 C CA    . PRO   B 1 432 ? 67.87529  31.25100  28.17695  1.000 89.24364  ? 432 PRO   B CA    1 
ATOM   6691 C C     . PRO   B 1 432 ? 68.15062  29.77590  27.89926  1.000 93.85687  ? 432 PRO   B C     1 
ATOM   6692 O O     . PRO   B 1 432 ? 67.52973  29.13255  27.02957  1.000 85.55296  ? 432 PRO   B O     1 
ATOM   6693 C CB    . PRO   B 1 432 ? 66.71371  31.40544  29.17338  1.000 79.94289  ? 432 PRO   B CB    1 
ATOM   6694 C CG    . PRO   B 1 432 ? 66.18621  32.77135  28.85583  1.000 81.52945  ? 432 PRO   B CG    1 
ATOM   6695 C CD    . PRO   B 1 432 ? 66.30472  32.91300  27.31138  1.000 84.97147  ? 432 PRO   B CD    1 
ATOM   6696 N N     . THR   B 1 433 ? 69.07384  29.24044  28.71065  1.000 85.51074  ? 433 THR   B N     1 
ATOM   6697 C CA    . THR   B 1 433 ? 69.67244  27.94031  28.43559  1.000 83.48154  ? 433 THR   B CA    1 
ATOM   6698 C C     . THR   B 1 433 ? 68.65623  26.80537  28.52982  1.000 84.18276  ? 433 THR   B C     1 
ATOM   6699 O O     . THR   B 1 433 ? 68.59930  25.93977  27.64541  1.000 83.37973  ? 433 THR   B O     1 
ATOM   6700 C CB    . THR   B 1 433 ? 70.82824  27.69744  29.39348  1.000 81.95433  ? 433 THR   B CB    1 
ATOM   6701 O OG1   . THR   B 1 433 ? 71.62202  28.88676  29.49386  1.000 75.13206  ? 433 THR   B OG1   1 
ATOM   6702 C CG2   . THR   B 1 433 ? 71.66248  26.54190  28.89801  1.000 77.58501  ? 433 THR   B CG2   1 
ATOM   6703 N N     . ASP   B 1 434 ? 67.88449  26.75894  29.62321  1.000 85.39637  ? 434 ASP   B N     1 
ATOM   6704 C CA    . ASP   B 1 434 ? 66.80865  25.77553  29.72364  1.000 90.32002  ? 434 ASP   B CA    1 
ATOM   6705 C C     . ASP   B 1 434 ? 65.99098  25.75423  28.44273  1.000 88.42545  ? 434 ASP   B C     1 
ATOM   6706 O O     . ASP   B 1 434 ? 65.60619  24.67979  27.95901  1.000 81.46204  ? 434 ASP   B O     1 
ATOM   6707 C CB    . ASP   B 1 434 ? 65.88459  26.08488  30.91517  1.000 88.44419  ? 434 ASP   B CB    1 
ATOM   6708 C CG    . ASP   B 1 434 ? 65.46284  27.54125  30.97138  1.000 90.37692  ? 434 ASP   B CG    1 
ATOM   6709 O OD1   . ASP   B 1 434 ? 66.36797  28.40007  31.02138  1.000 95.73866  ? 434 ASP   B OD1   1 
ATOM   6710 O OD2   . ASP   B 1 434 ? 64.23671  27.82755  31.02761  1.000 84.83765  ? 434 ASP   B OD2   1 
ATOM   6711 N N     . GLU   B 1 435 ? 65.71300  26.95137  27.89689  1.000 85.89556  ? 435 GLU   B N     1 
ATOM   6712 C CA    . GLU   B 1 435 ? 64.95483  27.08290  26.66177  1.000 85.54617  ? 435 GLU   B CA    1 
ATOM   6713 C C     . GLU   B 1 435 ? 65.64378  26.36045  25.52126  1.000 87.15171  ? 435 GLU   B C     1 
ATOM   6714 O O     . GLU   B 1 435 ? 65.02730  25.56462  24.78658  1.000 81.91264  ? 435 GLU   B O     1 
ATOM   6715 C CB    . GLU   B 1 435 ? 64.78311  28.55960  26.30236  1.000 84.16373  ? 435 GLU   B CB    1 
ATOM   6716 C CG    . GLU   B 1 435 ? 64.05124  29.40241  27.35240  1.000 98.48083  ? 435 GLU   B CG    1 
ATOM   6717 C CD    . GLU   B 1 435 ? 63.70637  30.90774  26.93238  1.000 108.36108 ? 435 GLU   B CD    1 
ATOM   6718 O OE1   . GLU   B 1 435 ? 64.16456  31.42230  25.85046  1.000 95.97000  ? 435 GLU   B OE1   1 
ATOM   6719 O OE2   . GLU   B 1 435 ? 62.95797  31.56252  27.74106  1.000 115.44291 ? 435 GLU   B OE2   1 
ATOM   6720 N N     . ALA   B 1 436 ? 66.92912  26.65508  25.33689  1.000 84.53649  ? 436 ALA   B N     1 
ATOM   6721 C CA    . ALA   B 1 436 ? 67.67512  26.01497  24.26380  1.000 80.11924  ? 436 ALA   B CA    1 
ATOM   6722 C C     . ALA   B 1 436 ? 67.53093  24.49031  24.34322  1.000 81.31219  ? 436 ALA   B C     1 
ATOM   6723 O O     . ALA   B 1 436 ? 66.87607  23.86541  23.49386  1.000 76.61179  ? 436 ALA   B O     1 
ATOM   6724 C CB    . ALA   B 1 436 ? 69.13469  26.48324  24.32277  1.000 71.94658  ? 436 ALA   B CB    1 
ATOM   6725 N N     . LEU   B 1 437 ? 68.04532  23.89455  25.42521  1.000 78.83042  ? 437 LEU   B N     1 
ATOM   6726 C CA    . LEU   B 1 437 ? 68.25531  22.44662  25.49702  1.000 75.40791  ? 437 LEU   B CA    1 
ATOM   6727 C C     . LEU   B 1 437 ? 67.04071  21.67980  25.01776  1.000 76.96230  ? 437 LEU   B C     1 
ATOM   6728 O O     . LEU   B 1 437 ? 67.13786  20.74454  24.20913  1.000 74.73137  ? 437 LEU   B O     1 
ATOM   6729 C CB    . LEU   B 1 437 ? 68.59779  22.08942  26.93314  1.000 77.38832  ? 437 LEU   B CB    1 
ATOM   6730 C CG    . LEU   B 1 437 ? 69.94019  22.78389  27.14689  1.000 79.87866  ? 437 LEU   B CG    1 
ATOM   6731 C CD1   . LEU   B 1 437 ? 70.23619  23.05799  28.59132  1.000 80.58866  ? 437 LEU   B CD1   1 
ATOM   6732 C CD2   . LEU   B 1 437 ? 71.03205  21.93884  26.52269  1.000 96.90866  ? 437 LEU   B CD2   1 
ATOM   6733 N N     . THR   B 1 438 ? 65.88673  22.07924  25.52604  1.000 84.92822  ? 438 THR   B N     1 
ATOM   6734 C CA    . THR   B 1 438 ? 64.61238  21.48460  25.15696  1.000 90.61211  ? 438 THR   B CA    1 
ATOM   6735 C C     . THR   B 1 438 ? 64.32995  21.64436  23.66225  1.000 88.43504  ? 438 THR   B C     1 
ATOM   6736 O O     . THR   B 1 438 ? 63.79663  20.72488  23.01412  1.000 85.83385  ? 438 THR   B O     1 
ATOM   6737 C CB    . THR   B 1 438 ? 63.54938  22.14964  26.01183  1.000 81.21100  ? 438 THR   B CB    1 
ATOM   6738 O OG1   . THR   B 1 438 ? 63.72735  23.56193  25.87531  1.000 77.58735  ? 438 THR   B OG1   1 
ATOM   6739 C CG2   . THR   B 1 438 ? 63.78243  21.78901  27.48255  1.000 75.35197  ? 438 THR   B CG2   1 
ATOM   6740 N N     . GLY   B 1 439 ? 64.69817  22.80093  23.09836  1.000 77.39102  ? 439 GLY   B N     1 
ATOM   6741 C CA    . GLY   B 1 439 ? 64.59768  22.97930  21.65914  1.000 81.73733  ? 439 GLY   B CA    1 
ATOM   6742 C C     . GLY   B 1 439 ? 65.48686  22.02881  20.86880  1.000 84.34817  ? 439 GLY   B C     1 
ATOM   6743 O O     . GLY   B 1 439 ? 64.99860  21.28303  20.00732  1.000 82.30702  ? 439 GLY   B O     1 
ATOM   6744 N N     . TYR   B 1 440 ? 66.80499  22.03893  21.15363  1.000 80.32400  ? 440 TYR   B N     1 
ATOM   6745 C CA    . TYR   B 1 440 ? 67.76734  21.28344  20.34731  1.000 75.23884  ? 440 TYR   B CA    1 
ATOM   6746 C C     . TYR   B 1 440 ? 67.50608  19.78532  20.43180  1.000 79.86630  ? 440 TYR   B C     1 
ATOM   6747 O O     . TYR   B 1 440 ? 67.34609  19.10415  19.40499  1.000 77.93328  ? 440 TYR   B O     1 
ATOM   6748 C CB    . TYR   B 1 440 ? 69.21549  21.57383  20.78170  1.000 67.20766  ? 440 TYR   B CB    1 
ATOM   6749 C CG    . TYR   B 1 440 ? 69.61674  23.00470  20.74666  1.000 62.41473  ? 440 TYR   B CG    1 
ATOM   6750 C CD1   . TYR   B 1 440 ? 69.02316  23.87600  19.85736  1.000 67.57152  ? 440 TYR   B CD1   1 
ATOM   6751 C CD2   . TYR   B 1 440 ? 70.59361  23.49296  21.59812  1.000 64.43748  ? 440 TYR   B CD2   1 
ATOM   6752 C CE1   . TYR   B 1 440 ? 69.37360  25.19702  19.81982  1.000 67.29067  ? 440 TYR   B CE1   1 
ATOM   6753 C CE2   . TYR   B 1 440 ? 70.96140  24.82943  21.57444  1.000 62.91483  ? 440 TYR   B CE2   1 
ATOM   6754 C CZ    . TYR   B 1 440 ? 70.34319  25.66788  20.67577  1.000 67.75349  ? 440 TYR   B CZ    1 
ATOM   6755 O OH    . TYR   B 1 440 ? 70.67188  26.99370  20.62975  1.000 73.87214  ? 440 TYR   B OH    1 
ATOM   6756 N N     . TYR   B 1 441 ? 67.51957  19.23853  21.64139  1.000 78.22103  ? 441 TYR   B N     1 
ATOM   6757 C CA    . TYR   B 1 441 ? 67.50493  17.78954  21.76184  1.000 79.00027  ? 441 TYR   B CA    1 
ATOM   6758 C C     . TYR   B 1 441 ? 66.12799  17.25079  22.08103  1.000 83.25121  ? 441 TYR   B C     1 
ATOM   6759 O O     . TYR   B 1 441 ? 65.75158  16.19569  21.53343  1.000 81.95401  ? 441 TYR   B O     1 
ATOM   6760 C CB    . TYR   B 1 441 ? 68.52895  17.35856  22.81554  1.000 75.37599  ? 441 TYR   B CB    1 
ATOM   6761 C CG    . TYR   B 1 441 ? 69.89199  17.92153  22.50039  1.000 70.71361  ? 441 TYR   B CG    1 
ATOM   6762 C CD1   . TYR   B 1 441 ? 70.63504  17.41992  21.43559  1.000 65.70099  ? 441 TYR   B CD1   1 
ATOM   6763 C CD2   . TYR   B 1 441 ? 70.38512  19.03918  23.18783  1.000 72.18574  ? 441 TYR   B CD2   1 
ATOM   6764 C CE1   . TYR   B 1 441 ? 71.87231  17.96836  21.10851  1.000 71.86024  ? 441 TYR   B CE1   1 
ATOM   6765 C CE2   . TYR   B 1 441 ? 71.61738  19.59689  22.86763  1.000 73.20007  ? 441 TYR   B CE2   1 
ATOM   6766 C CZ    . TYR   B 1 441 ? 72.36282  19.05666  21.82698  1.000 74.52522  ? 441 TYR   B CZ    1 
ATOM   6767 O OH    . TYR   B 1 441 ? 73.59328  19.60488  21.51304  1.000 71.55708  ? 441 TYR   B OH    1 
ATOM   6768 N N     . GLY   B 1 442 ? 65.36454  17.98879  22.90801  1.000 79.31931  ? 442 GLY   B N     1 
ATOM   6769 C CA    . GLY   B 1 442 ? 64.04023  17.58259  23.35201  1.000 87.73819  ? 442 GLY   B CA    1 
ATOM   6770 C C     . GLY   B 1 442 ? 63.92927  16.22849  24.05537  1.000 92.86166  ? 442 GLY   B C     1 
ATOM   6771 O O     . GLY   B 1 442 ? 64.45681  16.05341  25.16410  1.000 89.24205  ? 442 GLY   B O     1 
ATOM   6772 N N     . LYS   B 1 443 ? 63.23618  15.26506  23.41811  1.000 92.75844  ? 443 LYS   B N     1 
ATOM   6773 C CA    . LYS   B 1 443 ? 62.96085  13.97021  24.04542  1.000 92.85655  ? 443 LYS   B CA    1 
ATOM   6774 C C     . LYS   B 1 443 ? 64.22337  13.35651  24.63251  1.000 95.46731  ? 443 LYS   B C     1 
ATOM   6775 O O     . LYS   B 1 443 ? 64.21232  12.81456  25.74762  1.000 93.08962  ? 443 LYS   B O     1 
ATOM   6776 C CB    . LYS   B 1 443 ? 62.33668  13.01366  23.02195  1.000 96.80866  ? 443 LYS   B CB    1 
ATOM   6777 N N     . ASN   B 1 444 ? 65.32733  13.45551  23.90311  1.000 96.11552  ? 444 ASN   B N     1 
ATOM   6778 C CA    . ASN   B 1 444 ? 66.55255  12.76112  24.25591  1.000 90.41112  ? 444 ASN   B CA    1 
ATOM   6779 C C     . ASN   B 1 444 ? 67.37907  13.51308  25.28229  1.000 85.33663  ? 444 ASN   B C     1 
ATOM   6780 O O     . ASN   B 1 444 ? 68.26271  12.90501  25.88517  1.000 90.46924  ? 444 ASN   B O     1 
ATOM   6781 C CB    . ASN   B 1 444 ? 67.33636  12.51608  22.97543  1.000 82.22976  ? 444 ASN   B CB    1 
ATOM   6782 C CG    . ASN   B 1 444 ? 66.45954  11.88724  21.91333  1.000 90.03336  ? 444 ASN   B CG    1 
ATOM   6783 O OD1   . ASN   B 1 444 ? 65.35914  11.39114  22.21795  1.000 90.69585  ? 444 ASN   B OD1   1 
ATOM   6784 N ND2   . ASN   B 1 444 ? 66.90722  11.93191  20.66292  1.000 85.95700  ? 444 ASN   B ND2   1 
ATOM   6785 N N     . LEU   B 1 445 ? 67.08851  14.80039  25.50673  1.000 80.06239  ? 445 LEU   B N     1 
ATOM   6786 C CA    . LEU   B 1 445 ? 67.76731  15.58518  26.53342  1.000 76.47001  ? 445 LEU   B CA    1 
ATOM   6787 C C     . LEU   B 1 445 ? 68.06988  14.75580  27.76744  1.000 88.49109  ? 445 LEU   B C     1 
ATOM   6788 O O     . LEU   B 1 445 ? 69.16654  14.83665  28.32619  1.000 87.30827  ? 445 LEU   B O     1 
ATOM   6789 C CB    . LEU   B 1 445 ? 66.91067  16.78724  26.92097  1.000 77.80354  ? 445 LEU   B CB    1 
ATOM   6790 C CG    . LEU   B 1 445 ? 67.49521  17.78743  27.92737  1.000 88.49338  ? 445 LEU   B CG    1 
ATOM   6791 C CD1   . LEU   B 1 445 ? 68.80392  18.46097  27.44030  1.000 81.75866  ? 445 LEU   B CD1   1 
ATOM   6792 C CD2   . LEU   B 1 445 ? 66.43805  18.82444  28.29286  1.000 89.01835  ? 445 LEU   B CD2   1 
ATOM   6793 N N     . HIS   B 1 446 ? 67.10410  13.94821  28.21596  1.000 96.96815  ? 446 HIS   B N     1 
ATOM   6794 C CA    . HIS   B 1 446 ? 67.37126  13.06100  29.34174  1.000 91.93866  ? 446 HIS   B CA    1 
ATOM   6795 C C     . HIS   B 1 446 ? 68.40780  12.00517  28.98365  1.000 90.84906  ? 446 HIS   B C     1 
ATOM   6796 O O     . HIS   B 1 446 ? 69.47606  11.94280  29.60797  1.000 87.46797  ? 446 HIS   B O     1 
ATOM   6797 C CB    . HIS   B 1 446 ? 66.09486  12.39624  29.84433  1.000 106.97866 ? 446 HIS   B CB    1 
ATOM   6798 C CG    . HIS   B 1 446 ? 66.36979  11.38265  30.90451  1.000 112.17866 ? 446 HIS   B CG    1 
ATOM   6799 N ND1   . HIS   B 1 446 ? 66.47992  11.71579  32.23779  1.000 107.07372 ? 446 HIS   B ND1   1 
ATOM   6800 C CD2   . HIS   B 1 446 ? 66.60671  10.05021  30.82538  1.000 105.95866 ? 446 HIS   B CD2   1 
ATOM   6801 C CE1   . HIS   B 1 446 ? 66.76321  10.63158  32.93669  1.000 100.08804 ? 446 HIS   B CE1   1 
ATOM   6802 N NE2   . HIS   B 1 446 ? 66.84171  9.60647   32.10434  1.000 104.49866 ? 446 HIS   B NE2   1 
ATOM   6803 N N     . ARG   B 1 447 ? 68.11642  11.16311  27.97610  1.000 85.24280  ? 447 ARG   B N     1 
ATOM   6804 C CA    . ARG   B 1 447 ? 69.04324  10.07153  27.66685  1.000 87.94953  ? 447 ARG   B CA    1 
ATOM   6805 C C     . ARG   B 1 447 ? 70.45352  10.57000  27.37131  1.000 84.82126  ? 447 ARG   B C     1 
ATOM   6806 O O     . ARG   B 1 447 ? 71.44260  9.93789   27.75933  1.000 85.93141  ? 447 ARG   B O     1 
ATOM   6807 C CB    . ARG   B 1 447 ? 68.56524  9.23662   26.48921  1.000 78.79275  ? 447 ARG   B CB    1 
ATOM   6808 C CG    . ARG   B 1 447 ? 69.53292  8.09787   26.29136  1.000 63.64039  ? 447 ARG   B CG    1 
ATOM   6809 C CD    . ARG   B 1 447 ? 69.35762  7.36140   24.99793  1.000 73.17521  ? 447 ARG   B CD    1 
ATOM   6810 N NE    . ARG   B 1 447 ? 70.33568  6.28097   24.88437  1.000 81.05590  ? 447 ARG   B NE    1 
ATOM   6811 C CZ    . ARG   B 1 447 ? 70.38962  5.41586   23.87805  1.000 82.88710  ? 447 ARG   B CZ    1 
ATOM   6812 N NH1   . ARG   B 1 447 ? 69.51594  5.46186   22.88133  1.000 85.11891  ? 447 ARG   B NH1   1 
ATOM   6813 N NH2   . ARG   B 1 447 ? 71.30785  4.44734   23.89980  1.000 82.51046  ? 447 ARG   B NH2   1 
ATOM   6814 N N     . LEU   B 1 448 ? 70.57807  11.67085  26.64893  1.000 81.91847  ? 448 LEU   B N     1 
ATOM   6815 C CA    . LEU   B 1 448 ? 71.90311  12.23440  26.50218  1.000 79.58154  ? 448 LEU   B CA    1 
ATOM   6816 C C     . LEU   B 1 448 ? 72.47870  12.58112  27.86816  1.000 79.26737  ? 448 LEU   B C     1 
ATOM   6817 O O     . LEU   B 1 448 ? 73.63773  12.26094  28.15302  1.000 82.17016  ? 448 LEU   B O     1 
ATOM   6818 C CB    . LEU   B 1 448 ? 71.87249  13.46432  25.59543  1.000 84.16918  ? 448 LEU   B CB    1 
ATOM   6819 C CG    . LEU   B 1 448 ? 71.55064  13.16015  24.11990  1.000 78.94577  ? 448 LEU   B CG    1 
ATOM   6820 C CD1   . LEU   B 1 448 ? 71.22736  14.44747  23.33897  1.000 66.90412  ? 448 LEU   B CD1   1 
ATOM   6821 C CD2   . LEU   B 1 448 ? 72.60486  12.29281  23.44354  1.000 78.02970  ? 448 LEU   B CD2   1 
ATOM   6822 N N     . GLN   B 1 449 ? 71.67033  13.19032  28.74986  1.000 81.80238  ? 449 GLN   B N     1 
ATOM   6823 C CA    . GLN   B 1 449 ? 72.17445  13.56538  30.07828  1.000 85.03324  ? 449 GLN   B CA    1 
ATOM   6824 C C     . GLN   B 1 449 ? 72.67780  12.35790  30.87348  1.000 82.20840  ? 449 GLN   B C     1 
ATOM   6825 O O     . GLN   B 1 449 ? 73.52512  12.51620  31.76682  1.000 72.85696  ? 449 GLN   B O     1 
ATOM   6826 C CB    . GLN   B 1 449 ? 71.10359  14.32066  30.87283  1.000 79.94572  ? 449 GLN   B CB    1 
ATOM   6827 C CG    . GLN   B 1 449 ? 70.96107  15.79132  30.51144  1.000 82.53527  ? 449 GLN   B CG    1 
ATOM   6828 C CD    . GLN   B 1 449 ? 70.40473  16.63567  31.65183  1.000 83.63621  ? 449 GLN   B CD    1 
ATOM   6829 O OE1   . GLN   B 1 449 ? 69.33060  17.23551  31.53279  1.000 82.57286  ? 449 GLN   B OE1   1 
ATOM   6830 N NE2   . GLN   B 1 449 ? 71.13274  16.68681  32.76044  1.000 83.49117  ? 449 GLN   B NE2   1 
ATOM   6831 N N     . GLN   B 1 450 ? 72.15088  11.15807  30.58836  1.000 82.39807  ? 450 GLN   B N     1 
ATOM   6832 C CA    . GLN   B 1 450 ? 72.78677  9.92814   31.06454  1.000 82.91056  ? 450 GLN   B CA    1 
ATOM   6833 C C     . GLN   B 1 450 ? 74.16846  9.78091   30.46233  1.000 81.67875  ? 450 GLN   B C     1 
ATOM   6834 O O     . GLN   B 1 450 ? 75.18541  9.78350   31.16927  1.000 78.12686  ? 450 GLN   B O     1 
ATOM   6835 C CB    . GLN   B 1 450 ? 71.97065  8.68591   30.69103  1.000 82.59998  ? 450 GLN   B CB    1 
ATOM   6836 C CG    . GLN   B 1 450 ? 70.66881  8.46425   31.41868  1.000 90.41713  ? 450 GLN   B CG    1 
ATOM   6837 C CD    . GLN   B 1 450 ? 70.00883  7.18186   30.94835  1.000 95.11658  ? 450 GLN   B CD    1 
ATOM   6838 O OE1   . GLN   B 1 450 ? 70.61552  6.41377   30.18795  1.000 91.78839  ? 450 GLN   B OE1   1 
ATOM   6839 N NE2   . GLN   B 1 450 ? 68.76100  6.95092   31.37466  1.000 93.67803  ? 450 GLN   B NE2   1 
ATOM   6840 N N     . ILE   B 1 451 ? 74.20827  9.61616   29.13977  1.000 82.57843  ? 451 ILE   B N     1 
ATOM   6841 C CA    . ILE   B 1 451 ? 75.45459  9.29789   28.46154  1.000 78.72358  ? 451 ILE   B CA    1 
ATOM   6842 C C     . ILE   B 1 451 ? 76.52148  10.34308  28.77537  1.000 74.05414  ? 451 ILE   B C     1 
ATOM   6843 O O     . ILE   B 1 451 ? 77.69843  10.00953  28.96031  1.000 68.88798  ? 451 ILE   B O     1 
ATOM   6844 C CB    . ILE   B 1 451 ? 75.18561  9.15349   26.95848  1.000 72.51040  ? 451 ILE   B CB    1 
ATOM   6845 C CG1   . ILE   B 1 451 ? 74.21616  8.00160   26.75056  1.000 77.09078  ? 451 ILE   B CG1   1 
ATOM   6846 C CG2   . ILE   B 1 451 ? 76.44574  8.79364   26.25326  1.000 76.62770  ? 451 ILE   B CG2   1 
ATOM   6847 C CD1   . ILE   B 1 451 ? 73.50532  8.02706   25.44583  1.000 77.70707  ? 451 ILE   B CD1   1 
ATOM   6848 N N     . LYS   B 1 452 ? 76.11614  11.61550  28.88192  1.000 70.56193  ? 452 LYS   B N     1 
ATOM   6849 C CA    . LYS   B 1 452 ? 77.03952  12.67863  29.26698  1.000 69.00209  ? 452 LYS   B CA    1 
ATOM   6850 C C     . LYS   B 1 452 ? 77.65040  12.42930  30.63965  1.000 75.29802  ? 452 LYS   B C     1 
ATOM   6851 O O     . LYS   B 1 452 ? 78.80836  12.78249  30.88862  1.000 76.55871  ? 452 LYS   B O     1 
ATOM   6852 C CB    . LYS   B 1 452 ? 76.31618  14.02513  29.23466  1.000 69.03477  ? 452 LYS   B CB    1 
ATOM   6853 C CG    . LYS   B 1 452 ? 77.03108  15.16827  29.93011  1.000 72.65065  ? 452 LYS   B CG    1 
ATOM   6854 C CD    . LYS   B 1 452 ? 78.20132  15.73787  29.17049  1.000 69.38275  ? 452 LYS   B CD    1 
ATOM   6855 C CE    . LYS   B 1 452 ? 78.87710  16.78766  30.03731  1.000 69.87537  ? 452 LYS   B CE    1 
ATOM   6856 N NZ    . LYS   B 1 452 ? 79.53134  17.81921  29.21795  1.000 73.12261  ? 452 LYS   B NZ    1 
ATOM   6857 N N     . SER   B 1 453 ? 76.88838  11.84389  31.55447  1.000 84.56575  ? 453 SER   B N     1 
ATOM   6858 C CA    . SER   B 1 453 ? 77.42054  11.62537  32.89031  1.000 81.56605  ? 453 SER   B CA    1 
ATOM   6859 C C     . SER   B 1 453 ? 78.26774  10.35814  32.94677  1.000 75.59494  ? 453 SER   B C     1 
ATOM   6860 O O     . SER   B 1 453 ? 79.11018  10.23128  33.84621  1.000 74.69399  ? 453 SER   B O     1 
ATOM   6861 C CB    . SER   B 1 453 ? 76.27120  11.57891  33.92019  1.000 82.06879  ? 453 SER   B CB    1 
ATOM   6862 O OG    . SER   B 1 453 ? 75.57307  12.82677  34.00951  1.000 76.37552  ? 453 SER   B OG    1 
ATOM   6863 N N     . ALA   B 1 454 ? 78.07832  9.43557   31.99263  1.000 74.89889  ? 454 ALA   B N     1 
ATOM   6864 C CA    . ALA   B 1 454 ? 78.91377  8.23521   31.92755  1.000 74.51933  ? 454 ALA   B CA    1 
ATOM   6865 C C     . ALA   B 1 454 ? 80.28087  8.53594   31.32965  1.000 78.68914  ? 454 ALA   B C     1 
ATOM   6866 O O     . ALA   B 1 454 ? 81.29263  7.99605   31.78554  1.000 84.36429  ? 454 ALA   B O     1 
ATOM   6867 C CB    . ALA   B 1 454 ? 78.23176  7.13645   31.10790  1.000 69.22136  ? 454 ALA   B CB    1 
ATOM   6868 N N     . VAL   B 1 455 ? 80.33574  9.38425   30.31036  1.000 74.20141  ? 455 VAL   B N     1 
ATOM   6869 C CA    . VAL   B 1 455 ? 81.56865  9.58062   29.57631  1.000 66.62170  ? 455 VAL   B CA    1 
ATOM   6870 C C     . VAL   B 1 455 ? 81.99571  11.04495  29.58002  1.000 70.20484  ? 455 VAL   B C     1 
ATOM   6871 O O     . VAL   B 1 455 ? 82.72498  11.48044  28.69542  1.000 82.78996  ? 455 VAL   B O     1 
ATOM   6872 C CB    . VAL   B 1 455 ? 81.43924  9.01649   28.15118  1.000 66.12283  ? 455 VAL   B CB    1 
ATOM   6873 C CG1   . VAL   B 1 455 ? 81.00678  7.56857   28.19528  1.000 68.74882  ? 455 VAL   B CG1   1 
ATOM   6874 C CG2   . VAL   B 1 455 ? 80.40828  9.78497   27.39306  1.000 66.45587  ? 455 VAL   B CG2   1 
ATOM   6875 N N     . ASP   B 1 456 ? 81.54879  11.82851  30.56914  1.000 67.42619  ? 456 ASP   B N     1 
ATOM   6876 C CA    . ASP   B 1 456 ? 82.14953  13.13995  30.85079  1.000 69.27078  ? 456 ASP   B CA    1 
ATOM   6877 C C     . ASP   B 1 456 ? 81.60181  13.69393  32.17084  1.000 72.44450  ? 456 ASP   B C     1 
ATOM   6878 O O     . ASP   B 1 456 ? 81.11446  14.82758  32.21959  1.000 74.43229  ? 456 ASP   B O     1 
ATOM   6879 C CB    . ASP   B 1 456 ? 81.90046  14.13346  29.70307  1.000 71.18116  ? 456 ASP   B CB    1 
ATOM   6880 C CG    . ASP   B 1 456 ? 82.64171  15.48106  29.90445  1.000 77.39013  ? 456 ASP   B CG    1 
ATOM   6881 O OD1   . ASP   B 1 456 ? 83.36175  15.61800  30.92279  1.000 79.80420  ? 456 ASP   B OD1   1 
ATOM   6882 O OD2   . ASP   B 1 456 ? 82.49669  16.40837  29.05671  1.000 73.89077  ? 456 ASP   B OD2   1 
ATOM   6883 N N     . PRO   B 1 457 ? 81.65439  12.92016  33.25400  1.000 73.47010  ? 457 PRO   B N     1 
ATOM   6884 C CA    . PRO   B 1 457 ? 81.13358  13.38864  34.54090  1.000 70.71525  ? 457 PRO   B CA    1 
ATOM   6885 C C     . PRO   B 1 457 ? 81.50354  14.80383  34.91801  1.000 67.75018  ? 457 PRO   B C     1 
ATOM   6886 O O     . PRO   B 1 457 ? 80.67785  15.54975  35.45846  1.000 67.41814  ? 457 PRO   B O     1 
ATOM   6887 C CB    . PRO   B 1 457 ? 81.75633  12.39225  35.52445  1.000 74.28626  ? 457 PRO   B CB    1 
ATOM   6888 C CG    . PRO   B 1 457 ? 81.82741  11.12997  34.75026  1.000 75.33710  ? 457 PRO   B CG    1 
ATOM   6889 C CD    . PRO   B 1 457 ? 81.95933  11.48126  33.29126  1.000 75.95551  ? 457 PRO   B CD    1 
ATOM   6890 N N     . ASN   B 1 458 ? 82.74237  15.18589  34.67713  1.000 67.46902  ? 458 ASN   B N     1 
ATOM   6891 C CA    . ASN   B 1 458 ? 83.16859  16.50441  35.11533  1.000 76.99194  ? 458 ASN   B CA    1 
ATOM   6892 C C     . ASN   B 1 458 ? 82.88431  17.58942  34.08900  1.000 75.97575  ? 458 ASN   B C     1 
ATOM   6893 O O     . ASN   B 1 458 ? 83.39260  18.70539  34.24552  1.000 70.09562  ? 458 ASN   B O     1 
ATOM   6894 C CB    . ASN   B 1 458 ? 84.65469  16.49965  35.46283  1.000 79.45339  ? 458 ASN   B CB    1 
ATOM   6895 C CG    . ASN   B 1 458 ? 84.98425  15.50495  36.54590  1.000 82.02542  ? 458 ASN   B CG    1 
ATOM   6896 O OD1   . ASN   B 1 458 ? 84.33564  15.47047  37.59832  1.000 81.15586  ? 458 ASN   B OD1   1 
ATOM   6897 N ND2   . ASN   B 1 458 ? 85.97883  14.65938  36.27998  1.000 82.75789  ? 458 ASN   B ND2   1 
ATOM   6898 N N     . ASP   B 1 459 ? 82.07942  17.27891  33.06149  1.000 76.16001  ? 459 ASP   B N     1 
ATOM   6899 C CA    . ASP   B 1 459 ? 81.66562  18.22531  32.01423  1.000 74.56554  ? 459 ASP   B CA    1 
ATOM   6900 C C     . ASP   B 1 459 ? 82.89671  18.99368  31.51407  1.000 76.56429  ? 459 ASP   B C     1 
ATOM   6901 O O     . ASP   B 1 459 ? 83.06973  20.19217  31.76769  1.000 75.51793  ? 459 ASP   B O     1 
ATOM   6902 C CB    . ASP   B 1 459 ? 80.54803  19.13069  32.57048  1.000 72.88951  ? 459 ASP   B CB    1 
ATOM   6903 C CG    . ASP   B 1 459 ? 80.04363  20.21456  31.57888  1.000 79.46545  ? 459 ASP   B CG    1 
ATOM   6904 O OD1   . ASP   B 1 459 ? 79.44164  19.93149  30.49548  1.000 77.94087  ? 459 ASP   B OD1   1 
ATOM   6905 O OD2   . ASP   B 1 459 ? 80.25295  21.39650  31.92741  1.000 80.74124  ? 459 ASP   B OD2   1 
ATOM   6906 N N     . VAL   B 1 460 ? 83.79081  18.22765  30.85671  1.000 70.01274  ? 460 VAL   B N     1 
ATOM   6907 C CA    . VAL   B 1 460 ? 85.00331  18.79726  30.26358  1.000 73.92805  ? 460 VAL   B CA    1 
ATOM   6908 C C     . VAL   B 1 460 ? 84.65479  19.53979  28.98233  1.000 73.82571  ? 460 VAL   B C     1 
ATOM   6909 O O     . VAL   B 1 460 ? 85.16306  20.64439  28.72013  1.000 70.59576  ? 460 VAL   B O     1 
ATOM   6910 C CB    . VAL   B 1 460 ? 86.05812  17.70370  29.97585  1.000 78.48558  ? 460 VAL   B CB    1 
ATOM   6911 C CG1   . VAL   B 1 460 ? 87.30906  18.30727  29.33155  1.000 76.73866  ? 460 VAL   B CG1   1 
ATOM   6912 C CG2   . VAL   B 1 460 ? 86.40973  16.88915  31.21314  1.000 78.10866  ? 460 VAL   B CG2   1 
ATOM   6913 N N     . PHE   B 1 461 ? 83.78135  18.92209  28.17923  1.000 72.00451  ? 461 PHE   B N     1 
ATOM   6914 C CA    . PHE   B 1 461 ? 83.31068  19.45100  26.90552  1.000 71.78348  ? 461 PHE   B CA    1 
ATOM   6915 C C     . PHE   B 1 461 ? 82.03675  20.24577  27.17366  1.000 71.85569  ? 461 PHE   B C     1 
ATOM   6916 O O     . PHE   B 1 461 ? 80.92389  19.71856  27.15456  1.000 74.90456  ? 461 PHE   B O     1 
ATOM   6917 C CB    . PHE   B 1 461 ? 83.07552  18.31880  25.92253  1.000 69.67924  ? 461 PHE   B CB    1 
ATOM   6918 C CG    . PHE   B 1 461 ? 84.27267  17.45138  25.72408  1.000 72.13340  ? 461 PHE   B CG    1 
ATOM   6919 C CD1   . PHE   B 1 461 ? 85.52642  18.01673  25.51365  1.000 68.23754  ? 461 PHE   B CD1   1 
ATOM   6920 C CD2   . PHE   B 1 461 ? 84.14148  16.07088  25.70240  1.000 68.85226  ? 461 PHE   B CD2   1 
ATOM   6921 C CE1   . PHE   B 1 461 ? 86.62667  17.21704  25.31762  1.000 67.29189  ? 461 PHE   B CE1   1 
ATOM   6922 C CE2   . PHE   B 1 461 ? 85.23138  15.26918  25.50468  1.000 68.13723  ? 461 PHE   B CE2   1 
ATOM   6923 C CZ    . PHE   B 1 461 ? 86.47893  15.83377  25.31162  1.000 68.48548  ? 461 PHE   B CZ    1 
ATOM   6924 N N     . HIS   B 1 462 ? 82.21549  21.53170  27.42053  1.000 69.08320  ? 462 HIS   B N     1 
ATOM   6925 C CA    . HIS   B 1 462 ? 81.14078  22.42062  27.79284  1.000 67.10831  ? 462 HIS   B CA    1 
ATOM   6926 C C     . HIS   B 1 462 ? 81.09204  23.60416  26.84915  1.000 70.40747  ? 462 HIS   B C     1 
ATOM   6927 O O     . HIS   B 1 462 ? 82.13644  24.15751  26.47932  1.000 63.24551  ? 462 HIS   B O     1 
ATOM   6928 C CB    . HIS   B 1 462 ? 81.34123  22.89017  29.20568  1.000 69.13700  ? 462 HIS   B CB    1 
ATOM   6929 C CG    . HIS   B 1 462 ? 80.28883  23.83112  29.67989  1.000 75.17766  ? 462 HIS   B CG    1 
ATOM   6930 N ND1   . HIS   B 1 462 ? 79.03186  23.40668  30.05684  1.000 77.08610  ? 462 HIS   B ND1   1 
ATOM   6931 C CD2   . HIS   B 1 462 ? 80.32043  25.17144  29.88841  1.000 76.51896  ? 462 HIS   B CD2   1 
ATOM   6932 C CE1   . HIS   B 1 462 ? 78.32520  24.45453  30.44999  1.000 88.85886  ? 462 HIS   B CE1   1 
ATOM   6933 N NE2   . HIS   B 1 462 ? 79.08479  25.53611  30.36173  1.000 81.39830  ? 462 HIS   B NE2   1 
ATOM   6934 N N     . ASN   B 1 463 ? 79.86651  23.96867  26.45163  1.000 77.04206  ? 463 ASN   B N     1 
ATOM   6935 C CA    . ASN   B 1 463 ? 79.55934  25.23981  25.79627  1.000 75.98187  ? 463 ASN   B CA    1 
ATOM   6936 C C     . ASN   B 1 463 ? 78.28903  25.81061  26.43186  1.000 78.01823  ? 463 ASN   B C     1 
ATOM   6937 O O     . ASN   B 1 463 ? 77.47273  25.06599  27.00162  1.000 71.13816  ? 463 ASN   B O     1 
ATOM   6938 C CB    . ASN   B 1 463 ? 79.34863  25.07561  24.28444  1.000 65.50744  ? 463 ASN   B CB    1 
ATOM   6939 C CG    . ASN   B 1 463 ? 78.19669  24.14679  23.96212  1.000 64.91851  ? 463 ASN   B CG    1 
ATOM   6940 O OD1   . ASN   B 1 463 ? 77.10441  24.35708  24.46881  1.000 68.03833  ? 463 ASN   B OD1   1 
ATOM   6941 N ND2   . ASN   B 1 463 ? 78.41066  23.16192  23.08672  1.000 64.51029  ? 463 ASN   B ND2   1 
ATOM   6942 N N     . GLN   B 1 464 ? 78.10642  27.13156  26.29053  1.000 75.99267  ? 464 GLN   B N     1 
ATOM   6943 C CA    . GLN   B 1 464 ? 76.94468  27.84849  26.81361  1.000 68.53190  ? 464 GLN   B CA    1 
ATOM   6944 C C     . GLN   B 1 464 ? 75.60851  27.10022  26.80340  1.000 67.64755  ? 464 GLN   B C     1 
ATOM   6945 O O     . GLN   B 1 464 ? 74.69338  27.48564  27.53033  1.000 69.34311  ? 464 GLN   B O     1 
ATOM   6946 C CB    . GLN   B 1 464 ? 76.73408  29.15629  26.05645  1.000 68.00579  ? 464 GLN   B CB    1 
ATOM   6947 C CG    . GLN   B 1 464 ? 75.67296  30.01555  26.73364  1.000 75.13952  ? 464 GLN   B CG    1 
ATOM   6948 C CD    . GLN   B 1 464 ? 75.00041  31.05518  25.84359  1.000 69.34034  ? 464 GLN   B CD    1 
ATOM   6949 O OE1   . GLN   B 1 464 ? 75.60060  32.07882  25.47887  1.000 65.29940  ? 464 GLN   B OE1   1 
ATOM   6950 N NE2   . GLN   B 1 464 ? 73.73817  30.79333  25.49578  1.000 63.93959  ? 464 GLN   B NE2   1 
ATOM   6951 N N     . GLN   B 1 465 ? 75.45539  26.06160  25.96391  1.000 63.56814  ? 465 GLN   B N     1 
ATOM   6952 C CA    . GLN   B 1 465 ? 74.17577  25.36662  25.83990  1.000 64.21204  ? 465 GLN   B CA    1 
ATOM   6953 C C     . GLN   B 1 465 ? 74.37193  23.88418  25.60263  1.000 67.88219  ? 465 GLN   B C     1 
ATOM   6954 O O     . GLN   B 1 465 ? 73.56651  23.24916  24.90406  1.000 60.15342  ? 465 GLN   B O     1 
ATOM   6955 C CB    . GLN   B 1 465 ? 73.33502  25.94265  24.71318  1.000 65.34853  ? 465 GLN   B CB    1 
ATOM   6956 C CG    . GLN   B 1 465 ? 73.11668  27.44313  24.85713  1.000 72.09195  ? 465 GLN   B CG    1 
ATOM   6957 C CD    . GLN   B 1 465 ? 72.40833  28.01819  23.66325  1.000 73.52483  ? 465 GLN   B CD    1 
ATOM   6958 O OE1   . GLN   B 1 465 ? 72.37126  27.39265  22.58484  1.000 69.59371  ? 465 GLN   B OE1   1 
ATOM   6959 N NE2   . GLN   B 1 465 ? 71.80950  29.20054  23.84286  1.000 76.09843  ? 465 GLN   B NE2   1 
ATOM   6960 N N     . SER   B 1 466 ? 75.45318  23.33613  26.16907  1.000 71.36612  ? 466 SER   B N     1 
ATOM   6961 C CA    . SER   B 1 466 ? 75.80214  21.93316  26.04986  1.000 69.30504  ? 466 SER   B CA    1 
ATOM   6962 C C     . SER   B 1 466 ? 74.95903  21.09457  27.00697  1.000 69.01714  ? 466 SER   B C     1 
ATOM   6963 O O     . SER   B 1 466 ? 74.50069  21.58045  28.05127  1.000 67.89017  ? 466 SER   B O     1 
ATOM   6964 C CB    . SER   B 1 466 ? 77.30920  21.75576  26.32288  1.000 68.76708  ? 466 SER   B CB    1 
ATOM   6965 O OG    . SER   B 1 466 ? 77.66093  21.90113  27.69959  1.000 70.82293  ? 466 SER   B OG    1 
ATOM   6966 N N     . ILE   B 1 467 ? 74.72919  19.83430  26.63538  1.000 67.87568  ? 467 ILE   B N     1 
ATOM   6967 C CA    . ILE   B 1 467 ? 74.07604  18.86273  27.51918  1.000 68.14854  ? 467 ILE   B CA    1 
ATOM   6968 C C     . ILE   B 1 467 ? 74.77646  18.82197  28.87116  1.000 74.66030  ? 467 ILE   B C     1 
ATOM   6969 O O     . ILE   B 1 467 ? 76.01861  18.76458  28.90808  1.000 72.60353  ? 467 ILE   B O     1 
ATOM   6970 C CB    . ILE   B 1 467 ? 74.06712  17.46404  26.89622  1.000 64.60872  ? 467 ILE   B CB    1 
ATOM   6971 C CG1   . ILE   B 1 467 ? 72.96926  17.36597  25.84674  1.000 66.92587  ? 467 ILE   B CG1   1 
ATOM   6972 C CG2   . ILE   B 1 467 ? 73.94887  16.40702  27.96988  1.000 64.39486  ? 467 ILE   B CG2   1 
ATOM   6973 C CD1   . ILE   B 1 467 ? 73.33876  16.51486  24.68737  1.000 64.73931  ? 467 ILE   B CD1   1 
ATOM   6974 N N     . PRO   B 1 468 ? 74.05274  18.86552  30.00026  1.000 82.29469  ? 468 PRO   B N     1 
ATOM   6975 C CA    . PRO   B 1 468 ? 74.71538  18.70223  31.29900  1.000 81.26289  ? 468 PRO   B CA    1 
ATOM   6976 C C     . PRO   B 1 468 ? 74.49410  17.30718  31.85521  1.000 80.94757  ? 468 PRO   B C     1 
ATOM   6977 O O     . PRO   B 1 468 ? 73.59219  16.57033  31.41836  1.000 79.94148  ? 468 PRO   B O     1 
ATOM   6978 C CB    . PRO   B 1 468 ? 74.04502  19.77116  32.18802  1.000 73.70751  ? 468 PRO   B CB    1 
ATOM   6979 C CG    . PRO   B 1 468 ? 72.88914  20.32920  31.37718  1.000 70.06404  ? 468 PRO   B CG    1 
ATOM   6980 C CD    . PRO   B 1 468 ? 72.68846  19.37662  30.20894  1.000 72.69287  ? 468 PRO   B CD    1 
ATOM   6981 N N     . PRO   B 1 469 ? 75.31524  16.90705  32.81652  1.000 78.73811  ? 469 PRO   B N     1 
ATOM   6982 C CA    . PRO   B 1 469 ? 75.04455  15.68594  33.57466  1.000 81.12894  ? 469 PRO   B CA    1 
ATOM   6983 C C     . PRO   B 1 469 ? 73.97583  15.87190  34.65792  1.000 85.26536  ? 469 PRO   B C     1 
ATOM   6984 O O     . PRO   B 1 469 ? 73.67842  16.98844  35.10736  1.000 83.67143  ? 469 PRO   B O     1 
ATOM   6985 C CB    . PRO   B 1 469 ? 76.41613  15.38607  34.17719  1.000 84.72565  ? 469 PRO   B CB    1 
ATOM   6986 C CG    . PRO   B 1 469 ? 76.96450  16.78305  34.47192  1.000 77.59996  ? 469 PRO   B CG    1 
ATOM   6987 C CD    . PRO   B 1 469 ? 76.51913  17.61438  33.29508  1.000 72.42581  ? 469 PRO   B CD    1 
ATOM   6988 N N     . LEU   B 1 470 ? 73.44367  14.72619  35.10702  1.000 79.42010  ? 470 LEU   B N     1 
ATOM   6989 C CA    . LEU   B 1 470 ? 72.25241  14.61895  35.94529  1.000 78.00922  ? 470 LEU   B CA    1 
ATOM   6990 C C     . LEU   B 1 470 ? 72.48561  15.03790  37.40852  1.000 88.81535  ? 470 LEU   B C     1 
ATOM   6991 O O     . LEU   B 1 470 ? 73.62582  15.16674  37.87669  1.000 86.23476  ? 470 LEU   B O     1 
ATOM   6992 C CB    . LEU   B 1 470 ? 71.75206  13.18531  35.89855  1.000 66.46692  ? 470 LEU   B CB    1 
ATOM   6993 C CG    . LEU   B 1 470 ? 71.03803  12.91622  34.59468  1.000 74.23602  ? 470 LEU   B CG    1 
ATOM   6994 C CD1   . LEU   B 1 470 ? 70.93519  11.41979  34.27093  1.000 72.35840  ? 470 LEU   B CD1   1 
ATOM   6995 C CD2   . LEU   B 1 470 ? 69.65537  13.57222  34.70007  1.000 74.53545  ? 470 LEU   B CD2   1 
ATOM   6996 N N     . SER   B 1 471 ? 71.36468  15.21179  38.14609  1.000 96.86536  ? 471 SER   B N     1 
ATOM   6997 C CA    . SER   B 1 471 ? 71.33895  15.77129  39.53801  1.000 101.54151 ? 471 SER   B CA    1 
ATOM   6998 C C     . SER   B 1 471 ? 70.45359  15.08548  40.65776  1.000 93.69976  ? 471 SER   B C     1 
ATOM   6999 O O     . SER   B 1 471 ? 69.27304  15.38014  40.92747  1.000 81.40211  ? 471 SER   B O     1 
ATOM   7000 C CB    . SER   B 1 471 ? 70.93063  17.25199  39.44884  1.000 100.10484 ? 471 SER   B CB    1 
ATOM   7001 O OG    . SER   B 1 471 ? 71.92234  18.02042  38.77469  1.000 92.90634  ? 471 SER   B OG    1 
ATOM   7002 O OXT   . SER   B 1 471 ? 70.92518  14.23048  41.41208  1.000 91.18647  ? 471 SER   B OXT   1 
HETATM 7003 C C1    . NAG   C 2 .   ? 12.99938  0.58805   29.18360  1.000 64.01484  ? 1   NAG   C C1    1 
HETATM 7004 C C2    . NAG   C 2 .   ? 12.76637  -0.12898  27.91830  1.000 67.31139  ? 1   NAG   C C2    1 
HETATM 7005 C C3    . NAG   C 2 .   ? 13.18962  -1.57473  28.06343  1.000 69.51776  ? 1   NAG   C C3    1 
HETATM 7006 C C4    . NAG   C 2 .   ? 14.67207  -1.64304  28.41318  1.000 68.97648  ? 1   NAG   C C4    1 
HETATM 7007 C C5    . NAG   C 2 .   ? 14.97935  -0.82346  29.65901  1.000 66.63543  ? 1   NAG   C C5    1 
HETATM 7008 C C6    . NAG   C 2 .   ? 16.46731  -0.61231  29.82897  1.000 64.88903  ? 1   NAG   C C6    1 
HETATM 7009 C C7    . NAG   C 2 .   ? 10.93959  0.59643   26.43889  1.000 80.89700  ? 1   NAG   C C7    1 
HETATM 7010 C C8    . NAG   C 2 .   ? 12.00534  1.11640   25.52886  1.000 79.96698  ? 1   NAG   C C8    1 
HETATM 7011 N N2    . NAG   C 2 .   ? 11.36281  -0.00429  27.55917  1.000 76.25411  ? 1   NAG   C N2    1 
HETATM 7012 O O3    . NAG   C 2 .   ? 12.96681  -2.23079  26.82487  1.000 74.77990  ? 1   NAG   C O3    1 
HETATM 7013 O O4    . NAG   C 2 .   ? 15.09869  -2.98870  28.61684  1.000 76.97811  ? 1   NAG   C O4    1 
HETATM 7014 O O5    . NAG   C 2 .   ? 14.40099  0.48944   29.55239  1.000 65.67492  ? 1   NAG   C O5    1 
HETATM 7015 O O6    . NAG   C 2 .   ? 16.89972  0.60716   29.23648  1.000 59.16592  ? 1   NAG   C O6    1 
HETATM 7016 O O7    . NAG   C 2 .   ? 9.74388   0.72510   26.18085  1.000 90.63108  ? 1   NAG   C O7    1 
HETATM 7017 C C1    . NAG   C 2 .   ? 16.44730  -3.22250  28.10743  1.000 74.50059  ? 2   NAG   C C1    1 
HETATM 7018 C C2    . NAG   C 2 .   ? 17.09909  -4.21923  29.07116  1.000 70.79375  ? 2   NAG   C C2    1 
HETATM 7019 C C3    . NAG   C 2 .   ? 18.01206  -5.17965  28.31635  1.000 79.20855  ? 2   NAG   C C3    1 
HETATM 7020 C C4    . NAG   C 2 .   ? 17.17661  -6.02965  27.37006  1.000 85.21818  ? 2   NAG   C C4    1 
HETATM 7021 C C5    . NAG   C 2 .   ? 16.34568  -5.13733  26.44155  1.000 83.53879  ? 2   NAG   C C5    1 
HETATM 7022 C C6    . NAG   C 2 .   ? 14.85676  -5.37795  26.56363  1.000 83.22475  ? 2   NAG   C C6    1 
HETATM 7023 C C7    . NAG   C 2 .   ? 17.34962  -3.28218  31.32092  1.000 72.79992  ? 2   NAG   C C7    1 
HETATM 7024 C C8    . NAG   C 2 .   ? 15.99460  -3.86154  31.61189  1.000 68.66563  ? 2   NAG   C C8    1 
HETATM 7025 N N2    . NAG   C 2 .   ? 17.83113  -3.49471  30.09344  1.000 70.14089  ? 2   NAG   C N2    1 
HETATM 7026 O O3    . NAG   C 2 .   ? 18.66874  -6.01081  29.26586  1.000 86.81728  ? 2   NAG   C O3    1 
HETATM 7027 O O4    . NAG   C 2 .   ? 17.94661  -6.91132  26.55336  1.000 87.05669  ? 2   NAG   C O4    1 
HETATM 7028 O O5    . NAG   C 2 .   ? 16.56707  -3.73751  26.68492  1.000 77.38153  ? 2   NAG   C O5    1 
HETATM 7029 O O6    . NAG   C 2 .   ? 14.57750  -6.47709  27.42181  1.000 90.41089  ? 2   NAG   C O6    1 
HETATM 7030 O O7    . NAG   C 2 .   ? 17.98045  -2.64826  32.16072  1.000 73.90755  ? 2   NAG   C O7    1 
HETATM 7031 C C1    . MAN   C 2 .   ? 19.15562  -7.52550  27.05951  1.000 98.05899  ? 3   MAN   C C1    1 
HETATM 7032 C C2    . MAN   C 2 .   ? 19.78883  -8.32217  25.79882  1.000 114.77816 ? 3   MAN   C C2    1 
HETATM 7033 C C3    . MAN   C 2 .   ? 19.45960  -9.82943  25.72887  1.000 125.28763 ? 3   MAN   C C3    1 
HETATM 7034 C C4    . MAN   C 2 .   ? 19.41966  -10.39000 27.15431  1.000 120.17297 ? 3   MAN   C C4    1 
HETATM 7035 C C5    . MAN   C 2 .   ? 18.37183  -9.61968  27.95856  1.000 108.78823 ? 3   MAN   C C5    1 
HETATM 7036 C C6    . MAN   C 2 .   ? 18.04015  -10.26430 29.29590  1.000 103.09102 ? 3   MAN   C C6    1 
HETATM 7037 O O2    . MAN   C 2 .   ? 21.20794  -8.24301  25.77793  1.000 126.87150 ? 3   MAN   C O2    1 
HETATM 7038 O O3    . MAN   C 2 .   ? 20.45854  -10.53623 24.93316  1.000 134.58073 ? 3   MAN   C O3    1 
HETATM 7039 O O4    . MAN   C 2 .   ? 19.11230  -11.76526 27.14429  1.000 120.91694 ? 3   MAN   C O4    1 
HETATM 7040 O O5    . MAN   C 2 .   ? 18.92419  -8.31978  28.21202  1.000 102.35657 ? 3   MAN   C O5    1 
HETATM 7041 O O6    . MAN   C 2 .   ? 19.18763  -10.16828 30.13936  1.000 113.26782 ? 3   MAN   C O6    1 
HETATM 7042 C C1    . MAN   C 2 .   ? 20.07855  -11.27569 23.72990  1.000 137.43250 ? 4   MAN   C C1    1 
HETATM 7043 C C2    . MAN   C 2 .   ? 21.36546  -11.98275 23.35016  1.000 136.61200 ? 4   MAN   C C2    1 
HETATM 7044 C C3    . MAN   C 2 .   ? 22.30793  -10.80033 23.20329  1.000 141.27745 ? 4   MAN   C C3    1 
HETATM 7045 C C4    . MAN   C 2 .   ? 21.99295  -10.05704 21.88378  1.000 137.56866 ? 4   MAN   C C4    1 
HETATM 7046 C C5    . MAN   C 2 .   ? 20.53298  -9.49358  22.01184  1.000 136.19417 ? 4   MAN   C C5    1 
HETATM 7047 C C6    . MAN   C 2 .   ? 19.92055  -9.02794  20.70127  1.000 127.85784 ? 4   MAN   C C6    1 
HETATM 7048 O O2    . MAN   C 2 .   ? 21.28119  -12.62305 22.05375  1.000 127.04536 ? 4   MAN   C O2    1 
HETATM 7049 O O3    . MAN   C 2 .   ? 23.71391  -11.04342 23.48122  1.000 142.19866 ? 4   MAN   C O3    1 
HETATM 7050 O O4    . MAN   C 2 .   ? 22.93030  -8.98848  21.66883  1.000 130.86866 ? 4   MAN   C O4    1 
HETATM 7051 O O5    . MAN   C 2 .   ? 19.60014  -10.48768 22.62798  1.000 134.18641 ? 4   MAN   C O5    1 
HETATM 7052 O O6    . MAN   C 2 .   ? 19.38797  -7.72318  20.92757  1.000 113.21311 ? 4   MAN   C O6    1 
HETATM 7053 C C1    . MAN   C 2 .   ? 23.97469  -10.39251 24.77106  1.000 148.01866 ? 5   MAN   C C1    1 
HETATM 7054 C C2    . MAN   C 2 .   ? 25.21684  -9.40129  24.64086  1.000 158.50866 ? 5   MAN   C C2    1 
HETATM 7055 C C3    . MAN   C 2 .   ? 26.08992  -9.40920  25.93748  1.000 146.26866 ? 5   MAN   C C3    1 
HETATM 7056 C C4    . MAN   C 2 .   ? 25.20727  -9.48591  27.20902  1.000 148.22282 ? 5   MAN   C C4    1 
HETATM 7057 C C5    . MAN   C 2 .   ? 24.50537  -10.87748 27.24059  1.000 150.07314 ? 5   MAN   C C5    1 
HETATM 7058 C C6    . MAN   C 2 .   ? 23.27293  -10.95849 28.17914  1.000 143.79363 ? 5   MAN   C C6    1 
HETATM 7059 O O2    . MAN   C 2 .   ? 24.79552  -8.03567  24.41864  1.000 162.06866 ? 5   MAN   C O2    1 
HETATM 7060 O O3    . MAN   C 2 .   ? 27.03929  -8.33110  25.99387  1.000 113.76866 ? 5   MAN   C O3    1 
HETATM 7061 O O4    . MAN   C 2 .   ? 25.98776  -9.28955  28.41583  1.000 138.52591 ? 5   MAN   C O4    1 
HETATM 7062 O O5    . MAN   C 2 .   ? 24.14436  -11.37111 25.85077  1.000 147.20901 ? 5   MAN   C O5    1 
HETATM 7063 O O6    . MAN   C 2 .   ? 23.69736  -11.38343 29.50094  1.000 136.42024 ? 5   MAN   C O6    1 
HETATM 7064 C C1    . NAG   D 3 .   ? 29.26169  22.70214  20.13021  1.000 56.13890  ? 1   NAG   D C1    1 
HETATM 7065 C C2    . NAG   D 3 .   ? 28.92606  23.82252  19.20273  1.000 64.32557  ? 1   NAG   D C2    1 
HETATM 7066 C C3    . NAG   D 3 .   ? 29.73481  23.73714  17.91006  1.000 64.48456  ? 1   NAG   D C3    1 
HETATM 7067 C C4    . NAG   D 3 .   ? 31.20671  23.41710  18.17500  1.000 66.36317  ? 1   NAG   D C4    1 
HETATM 7068 C C5    . NAG   D 3 .   ? 31.34553  22.31626  19.21227  1.000 53.82960  ? 1   NAG   D C5    1 
HETATM 7069 C C6    . NAG   D 3 .   ? 32.75603  22.17845  19.69773  1.000 55.51364  ? 1   NAG   D C6    1 
HETATM 7070 C C7    . NAG   D 3 .   ? 26.61159  24.61470  19.42681  1.000 69.01213  ? 1   NAG   D C7    1 
HETATM 7071 C C8    . NAG   D 3 .   ? 27.16134  25.73228  20.27266  1.000 62.20111  ? 1   NAG   D C8    1 
HETATM 7072 N N2    . NAG   D 3 .   ? 27.50211  23.75241  18.93185  1.000 65.46758  ? 1   NAG   D N2    1 
HETATM 7073 O O3    . NAG   D 3 .   ? 29.62653  25.00583  17.27262  1.000 63.22646  ? 1   NAG   D O3    1 
HETATM 7074 O O4    . NAG   D 3 .   ? 31.85758  22.95043  16.99551  1.000 75.52708  ? 1   NAG   D O4    1 
HETATM 7075 O O5    . NAG   D 3 .   ? 30.58895  22.67866  20.36118  1.000 56.49325  ? 1   NAG   D O5    1 
HETATM 7076 O O6    . NAG   D 3 .   ? 33.08331  23.32662  20.46540  1.000 58.94184  ? 1   NAG   D O6    1 
HETATM 7077 O O7    . NAG   D 3 .   ? 25.41535  24.48870  19.21066  1.000 81.68858  ? 1   NAG   D O7    1 
HETATM 7078 C C1    . NAG   D 3 .   ? 32.98503  23.71441  16.53635  1.000 73.56668  ? 2   NAG   D C1    1 
HETATM 7079 C C2    . NAG   D 3 .   ? 33.66230  22.93014  15.41397  1.000 72.16585  ? 2   NAG   D C2    1 
HETATM 7080 C C3    . NAG   D 3 .   ? 34.76771  23.75351  14.76208  1.000 79.21098  ? 2   NAG   D C3    1 
HETATM 7081 C C4    . NAG   D 3 .   ? 34.30704  25.17196  14.44394  1.000 89.51427  ? 2   NAG   D C4    1 
HETATM 7082 C C5    . NAG   D 3 .   ? 33.51261  25.79762  15.59108  1.000 82.18219  ? 2   NAG   D C5    1 
HETATM 7083 C C6    . NAG   D 3 .   ? 32.76270  27.02459  15.15103  1.000 80.79008  ? 2   NAG   D C6    1 
HETATM 7084 C C7    . NAG   D 3 .   ? 33.48803  20.53600  15.99113  1.000 63.08325  ? 2   NAG   D C7    1 
HETATM 7085 C C8    . NAG   D 3 .   ? 34.21443  19.34703  16.53155  1.000 66.80499  ? 2   NAG   D C8    1 
HETATM 7086 N N2    . NAG   D 3 .   ? 34.19771  21.67185  15.91047  1.000 68.63205  ? 2   NAG   D N2    1 
HETATM 7087 O O3    . NAG   D 3 .   ? 35.14705  23.10370  13.55320  1.000 85.13713  ? 2   NAG   D O3    1 
HETATM 7088 O O4    . NAG   D 3 .   ? 35.45357  25.98946  14.23170  1.000 92.00268  ? 2   NAG   D O4    1 
HETATM 7089 O O5    . NAG   D 3 .   ? 32.50385  24.89588  16.05061  1.000 78.59177  ? 2   NAG   D O5    1 
HETATM 7090 O O6    . NAG   D 3 .   ? 31.62858  26.62502  14.39402  1.000 69.44012  ? 2   NAG   D O6    1 
HETATM 7091 O O7    . NAG   D 3 .   ? 32.31268  20.47344  15.66298  1.000 59.43347  ? 2   NAG   D O7    1 
HETATM 7092 C C1    . MAN   D 3 .   ? 35.64961  26.34860  12.84846  1.000 103.80548 ? 3   MAN   D C1    1 
HETATM 7093 C C2    . MAN   D 3 .   ? 36.59276  27.54073  12.91700  1.000 114.73103 ? 3   MAN   D C2    1 
HETATM 7094 C C3    . MAN   D 3 .   ? 36.19008  28.64175  11.87639  1.000 127.23286 ? 3   MAN   D C3    1 
HETATM 7095 C C4    . MAN   D 3 .   ? 35.67751  28.05029  10.55002  1.000 116.94978 ? 3   MAN   D C4    1 
HETATM 7096 C C5    . MAN   D 3 .   ? 34.53123  27.06074  10.79604  1.000 108.98077 ? 3   MAN   D C5    1 
HETATM 7097 C C6    . MAN   D 3 .   ? 34.70052  25.79540  9.99137   1.000 107.82726 ? 3   MAN   D C6    1 
HETATM 7098 O O2    . MAN   D 3 .   ? 37.95613  27.13847  12.69171  1.000 112.02714 ? 3   MAN   D O2    1 
HETATM 7099 O O3    . MAN   D 3 .   ? 37.26613  29.54336  11.61666  1.000 139.83866 ? 3   MAN   D O3    1 
HETATM 7100 O O4    . MAN   D 3 .   ? 35.26281  29.10429  9.64393   1.000 115.64428 ? 3   MAN   D O4    1 
HETATM 7101 O O5    . MAN   D 3 .   ? 34.44016  26.68465  12.20429  1.000 103.43003 ? 3   MAN   D O5    1 
HETATM 7102 O O6    . MAN   D 3 .   ? 36.06879  25.69732  9.56067   1.000 112.40866 ? 3   MAN   D O6    1 
HETATM 7103 C C1    . MAN   D 3 .   ? 36.93021  30.89426  11.99941  1.000 139.48095 ? 4   MAN   D C1    1 
HETATM 7104 C C2    . MAN   D 3 .   ? 38.01623  31.79784  11.35810  1.000 143.30181 ? 4   MAN   D C2    1 
HETATM 7105 C C3    . MAN   D 3 .   ? 38.81933  32.54512  12.47556  1.000 144.85799 ? 4   MAN   D C3    1 
HETATM 7106 C C4    . MAN   D 3 .   ? 37.89694  33.28400  13.47744  1.000 147.43958 ? 4   MAN   D C4    1 
HETATM 7107 C C5    . MAN   D 3 .   ? 36.69691  32.36087  13.93834  1.000 148.16365 ? 4   MAN   D C5    1 
HETATM 7108 C C6    . MAN   D 3 .   ? 35.28388  32.85497  13.52207  1.000 141.34247 ? 4   MAN   D C6    1 
HETATM 7109 O O2    . MAN   D 3 .   ? 37.46217  32.75626  10.40361  1.000 141.62344 ? 4   MAN   D O2    1 
HETATM 7110 O O3    . MAN   D 3 .   ? 39.81378  33.43331  11.95207  1.000 142.23322 ? 4   MAN   D O3    1 
HETATM 7111 O O4    . MAN   D 3 .   ? 38.67363  33.73262  14.60882  1.000 139.60546 ? 4   MAN   D O4    1 
HETATM 7112 O O5    . MAN   D 3 .   ? 36.85744  31.01826  13.41854  1.000 145.02866 ? 4   MAN   D O5    1 
HETATM 7113 O O6    . MAN   D 3 .   ? 34.34676  31.74895  13.56158  1.000 126.30803 ? 4   MAN   D O6    1 
HETATM 7114 C C1    . MAN   D 3 .   ? 36.55443  24.34249  9.65559   1.000 117.95762 ? 5   MAN   D C1    1 
HETATM 7115 C C2    . MAN   D 3 .   ? 37.99588  24.07920  10.27458  1.000 119.68960 ? 5   MAN   D C2    1 
HETATM 7116 C C3    . MAN   D 3 .   ? 39.09334  24.66315  9.34468   1.000 116.82528 ? 5   MAN   D C3    1 
HETATM 7117 C C4    . MAN   D 3 .   ? 38.93035  24.13114  7.86746   1.000 113.34509 ? 5   MAN   D C4    1 
HETATM 7118 C C5    . MAN   D 3 .   ? 37.46718  24.25216  7.26611   1.000 110.09726 ? 5   MAN   D C5    1 
HETATM 7119 C C6    . MAN   D 3 .   ? 37.39590  23.50921  5.92293   1.000 100.96811 ? 5   MAN   D C6    1 
HETATM 7120 O O2    . MAN   D 3 .   ? 38.28071  22.61389  10.47236  1.000 109.10580 ? 5   MAN   D O2    1 
HETATM 7121 O O3    . MAN   D 3 .   ? 40.51220  24.50311  9.81622   1.000 106.13507 ? 5   MAN   D O3    1 
HETATM 7122 O O4    . MAN   D 3 .   ? 39.94924  24.82955  7.04147   1.000 112.94139 ? 5   MAN   D O4    1 
HETATM 7123 O O5    . MAN   D 3 .   ? 36.48283  23.67990  8.27048   1.000 116.81052 ? 5   MAN   D O5    1 
HETATM 7124 O O6    . MAN   D 3 .   ? 36.17279  22.79212  5.81077   1.000 95.63659  ? 5   MAN   D O6    1 
HETATM 7125 H H1    . MAN   D 3 .   ? 35.85898  23.89521  10.38256  1.000 141.54914 ? 5   MAN   D H1    1 
HETATM 7126 H H2    . MAN   D 3 .   ? 38.05985  24.57907  11.25011  1.000 143.62752 ? 5   MAN   D H2    1 
HETATM 7127 H H3    . MAN   D 3 .   ? 38.95263  25.74899  9.35796   1.000 140.19034 ? 5   MAN   D H3    1 
HETATM 7128 H H4    . MAN   D 3 .   ? 39.05524  23.03535  7.88329   1.000 136.01411 ? 5   MAN   D H4    1 
HETATM 7129 H H5    . MAN   D 3 .   ? 37.16352  25.29352  7.09594   1.000 132.11671 ? 5   MAN   D H5    1 
HETATM 7130 H H61   . MAN   D 3 .   ? 38.25916  22.82799  5.86890   1.000 121.16174 ? 5   MAN   D H61   1 
HETATM 7131 H H62   . MAN   D 3 .   ? 37.49050  24.25624  5.11969   1.000 121.16174 ? 5   MAN   D H62   1 
HETATM 7132 H HO2   . MAN   D 3 .   ? 39.26439  22.49802  10.43863  1.000 130.92697 ? 5   MAN   D HO2   1 
HETATM 7133 H HO3   . MAN   D 3 .   ? 40.97070  23.89314  9.23328   1.000 127.36209 ? 5   MAN   D HO3   1 
HETATM 7134 H HO4   . MAN   D 3 .   ? 39.61230  25.75423  6.89911   1.000 135.52967 ? 5   MAN   D HO4   1 
HETATM 7135 H HO6   . MAN   D 3 .   ? 35.52378  23.26571  6.35980   1.000 114.76391 ? 5   MAN   D HO6   1 
HETATM 7136 C C1    . NAG   E 4 .   ? 52.00354  -12.15001 49.01319  1.000 101.15791 ? 1   NAG   E C1    1 
HETATM 7137 C C2    . NAG   E 4 .   ? 51.71879  -12.59606 50.45039  1.000 109.08866 ? 1   NAG   E C2    1 
HETATM 7138 C C3    . NAG   E 4 .   ? 51.43542  -14.09856 50.51763  1.000 102.82866 ? 1   NAG   E C3    1 
HETATM 7139 C C4    . NAG   E 4 .   ? 50.41286  -14.52747 49.47125  1.000 104.21866 ? 1   NAG   E C4    1 
HETATM 7140 C C5    . NAG   E 4 .   ? 50.75658  -13.97917 48.07924  1.000 99.10675  ? 1   NAG   E C5    1 
HETATM 7141 C C6    . NAG   E 4 .   ? 49.63404  -14.16240 47.08533  1.000 95.60778  ? 1   NAG   E C6    1 
HETATM 7142 C C7    . NAG   E 4 .   ? 52.68975  -11.47909 52.42436  1.000 106.57722 ? 1   NAG   E C7    1 
HETATM 7143 C C8    . NAG   E 4 .   ? 51.29422  -11.00115 52.73129  1.000 95.77276  ? 1   NAG   E C8    1 
HETATM 7144 N N2    . NAG   E 4 .   ? 52.82745  -12.23314 51.32465  1.000 111.38866 ? 1   NAG   E N2    1 
HETATM 7145 O O3    . NAG   E 4 .   ? 50.86836  -14.38397 51.79100  1.000 104.52694 ? 1   NAG   E O3    1 
HETATM 7146 O O4    . NAG   E 4 .   ? 50.26056  -15.94994 49.50243  1.000 106.31844 ? 1   NAG   E O4    1 
HETATM 7147 O O5    . NAG   E 4 .   ? 50.94499  -12.56185 48.16443  1.000 95.96437  ? 1   NAG   E O5    1 
HETATM 7148 O O6    . NAG   E 4 .   ? 48.57733  -13.25177 47.36748  1.000 91.47854  ? 1   NAG   E O6    1 
HETATM 7149 O O7    . NAG   E 4 .   ? 53.65191  -11.17821 53.12796  1.000 104.60837 ? 1   NAG   E O7    1 
HETATM 7150 C C1    . NAG   E 4 .   ? 48.89435  -16.28904 49.13091  1.000 102.55865 ? 2   NAG   E C1    1 
HETATM 7151 C C2    . NAG   E 4 .   ? 48.54261  -17.78796 49.28004  1.000 96.81350  ? 2   NAG   E C2    1 
HETATM 7152 C C3    . NAG   E 4 .   ? 47.03264  -17.97040 49.42763  1.000 102.31801 ? 2   NAG   E C3    1 
HETATM 7153 C C4    . NAG   E 4 .   ? 46.51638  -17.34816 50.71826  1.000 98.02430  ? 2   NAG   E C4    1 
HETATM 7154 C C5    . NAG   E 4 .   ? 47.13560  -15.97814 50.99943  1.000 94.76905  ? 2   NAG   E C5    1 
HETATM 7155 C C6    . NAG   E 4 .   ? 47.94244  -15.91530 52.26843  1.000 102.18759 ? 2   NAG   E C6    1 
HETATM 7156 C C7    . NAG   E 4 .   ? 50.31230  -18.57521 47.72957  1.000 111.58397 ? 2   NAG   E C7    1 
HETATM 7157 C C8    . NAG   E 4 .   ? 50.59647  -19.38096 46.48817  1.000 105.32698 ? 2   NAG   E C8    1 
HETATM 7158 N N2    . NAG   E 4 .   ? 49.02947  -18.53141 48.11951  1.000 105.95355 ? 2   NAG   E N2    1 
HETATM 7159 O O3    . NAG   E 4 .   ? 46.70581  -19.35791 49.42079  1.000 102.20175 ? 2   NAG   E O3    1 
HETATM 7160 O O4    . NAG   E 4 .   ? 45.14159  -17.00914 50.58791  1.000 97.67746  ? 2   NAG   E O4    1 
HETATM 7161 O O5    . NAG   E 4 .   ? 47.93871  -15.44384 49.93255  1.000 107.22144 ? 2   NAG   E O5    1 
HETATM 7162 O O6    . NAG   E 4 .   ? 47.07588  -15.56636 53.33852  1.000 107.09738 ? 2   NAG   E O6    1 
HETATM 7163 O O7    . NAG   E 4 .   ? 51.19166  -17.96417 48.32458  1.000 115.59825 ? 2   NAG   E O7    1 
HETATM 7164 C C1    . MAN   E 4 .   ? 44.09681  -18.00632 50.52431  1.000 103.67291 ? 3   MAN   E C1    1 
HETATM 7165 C C2    . MAN   E 4 .   ? 43.11284  -17.44227 51.57521  1.000 105.39749 ? 3   MAN   E C2    1 
HETATM 7166 C C3    . MAN   E 4 .   ? 42.16301  -18.49397 51.99985  1.000 103.66131 ? 3   MAN   E C3    1 
HETATM 7167 C C4    . MAN   E 4 .   ? 42.03386  -19.48578 50.86794  1.000 107.89486 ? 3   MAN   E C4    1 
HETATM 7168 C C5    . MAN   E 4 .   ? 43.32808  -20.26403 50.58778  1.000 103.69579 ? 3   MAN   E C5    1 
HETATM 7169 C C6    . MAN   E 4 .   ? 43.29916  -20.77469 49.11146  1.000 100.73744 ? 3   MAN   E C6    1 
HETATM 7170 O O2    . MAN   E 4 .   ? 42.28387  -16.41842 50.98724  1.000 99.48368  ? 3   MAN   E O2    1 
HETATM 7171 O O3    . MAN   E 4 .   ? 40.85798  -17.89791 52.16886  1.000 107.86866 ? 3   MAN   E O3    1 
HETATM 7172 O O4    . MAN   E 4 .   ? 40.96829  -20.37680 51.14301  1.000 109.49528 ? 3   MAN   E O4    1 
HETATM 7173 O O5    . MAN   E 4 .   ? 44.44014  -19.36269 50.80539  1.000 102.62101 ? 3   MAN   E O5    1 
HETATM 7174 O O6    . MAN   E 4 .   ? 44.53846  -21.36034 48.68996  1.000 100.15407 ? 3   MAN   E O6    1 
HETATM 7175 C C1    . MAN   E 4 .   ? 40.18599  -18.11937 53.45595  1.000 111.70324 ? 4   MAN   E C1    1 
HETATM 7176 C C2    . MAN   E 4 .   ? 39.49551  -16.85279 54.25812  1.000 111.77257 ? 4   MAN   E C2    1 
HETATM 7177 C C3    . MAN   E 4 .   ? 38.33641  -16.17471 53.41681  1.000 114.87763 ? 4   MAN   E C3    1 
HETATM 7178 C C4    . MAN   E 4 .   ? 37.11697  -17.15020 53.44672  1.000 116.05994 ? 4   MAN   E C4    1 
HETATM 7179 C C5    . MAN   E 4 .   ? 37.68678  -18.59497 53.13623  1.000 115.16034 ? 4   MAN   E C5    1 
HETATM 7180 C C6    . MAN   E 4 .   ? 36.85299  -19.46530 52.18565  1.000 116.08958 ? 4   MAN   E C6    1 
HETATM 7181 O O1    . MAN   E 4 .   ? 41.07811  -18.75617 54.46204  1.000 119.19211 ? 4   MAN   E O1    1 
HETATM 7182 O O2    . MAN   E 4 .   ? 40.49133  -15.83096 54.65512  1.000 108.89543 ? 4   MAN   E O2    1 
HETATM 7183 O O3    . MAN   E 4 .   ? 38.76866  -15.78462 52.05143  1.000 114.96925 ? 4   MAN   E O3    1 
HETATM 7184 O O4    . MAN   E 4 .   ? 36.36597  -17.09300 54.76967  1.000 101.59859 ? 4   MAN   E O4    1 
HETATM 7185 O O5    . MAN   E 4 .   ? 39.12035  -18.53616 52.49661  1.000 109.85279 ? 4   MAN   E O5    1 
HETATM 7186 O O6    . MAN   E 4 .   ? 37.15503  -19.07821 50.78234  1.000 106.70930 ? 4   MAN   E O6    1 
HETATM 7187 H H1    . MAN   E 4 .   ? 39.70967  -19.14184 53.63175  1.000 134.04389 ? 4   MAN   E H1    1 
HETATM 7188 H H2    . MAN   E 4 .   ? 39.01937  -17.23777 55.16954  1.000 134.12708 ? 4   MAN   E H2    1 
HETATM 7189 H H3    . MAN   E 4 .   ? 38.02608  -15.21143 53.83494  1.000 137.85315 ? 4   MAN   E H3    1 
HETATM 7190 H H4    . MAN   E 4 .   ? 36.39447  -16.87431 52.66028  1.000 139.27192 ? 4   MAN   E H4    1 
HETATM 7191 H H5    . MAN   E 4 .   ? 37.72316  -19.08048 54.12038  1.000 138.19241 ? 4   MAN   E H5    1 
HETATM 7192 H H61   . MAN   E 4 .   ? 35.78867  -19.31350 52.42313  1.000 139.30750 ? 4   MAN   E H61   1 
HETATM 7193 H H62   . MAN   E 4 .   ? 37.10506  -20.52045 52.37354  1.000 139.30750 ? 4   MAN   E H62   1 
HETATM 7194 H HO1   . MAN   E 4 .   ? 41.39693  -17.98712 55.07184  1.000 143.03053 ? 4   MAN   E HO1   1 
HETATM 7195 H HO2   . MAN   E 4 .   ? 41.25043  -15.84136 54.02823  1.000 130.67452 ? 4   MAN   E HO2   1 
HETATM 7196 H HO3   . MAN   E 4 .   ? 38.73439  -16.59201 51.53914  1.000 137.96309 ? 4   MAN   E HO3   1 
HETATM 7197 H HO4   . MAN   E 4 .   ? 36.98348  -17.44353 55.46820  1.000 121.91831 ? 4   MAN   E HO4   1 
HETATM 7198 H HO6   . MAN   E 4 .   ? 37.92589  -18.47683 50.79127  1.000 128.05116 ? 4   MAN   E HO6   1 
HETATM 7199 C C1    . NAG   F 5 .   ? 103.65577 23.84602  12.81391  1.000 73.15967  ? 1   NAG   F C1    1 
HETATM 7200 C C2    . NAG   F 5 .   ? 103.61360 22.84302  11.68827  1.000 76.86653  ? 1   NAG   F C2    1 
HETATM 7201 C C3    . NAG   F 5 .   ? 102.91274 23.42513  10.47118  1.000 78.62974  ? 1   NAG   F C3    1 
HETATM 7202 C C4    . NAG   F 5 .   ? 101.45920 23.79033  10.73994  1.000 82.60012  ? 1   NAG   F C4    1 
HETATM 7203 C C5    . NAG   F 5 .   ? 101.29825 24.34846  12.15256  1.000 74.34738  ? 1   NAG   F C5    1 
HETATM 7204 C C6    . NAG   F 5 .   ? 100.72413 23.33881  13.11734  1.000 72.78076  ? 1   NAG   F C6    1 
HETATM 7205 C C7    . NAG   F 5 .   ? 105.66230 21.45939  11.89162  1.000 85.65298  ? 1   NAG   F C7    1 
HETATM 7206 C C8    . NAG   F 5 .   ? 107.08444 21.30578  11.42876  1.000 84.23185  ? 1   NAG   F C8    1 
HETATM 7207 N N2    . NAG   F 5 .   ? 104.98772 22.48775  11.35783  1.000 80.32020  ? 1   NAG   F N2    1 
HETATM 7208 O O3    . NAG   F 5 .   ? 102.96899 22.47963  9.41625   1.000 81.83261  ? 1   NAG   F O3    1 
HETATM 7209 O O4    . NAG   F 5 .   ? 101.07491 24.77760  9.78159   1.000 87.51527  ? 1   NAG   F O4    1 
HETATM 7210 O O5    . NAG   F 5 .   ? 102.55246 24.78948  12.69453  1.000 76.76206  ? 1   NAG   F O5    1 
HETATM 7211 O O6    . NAG   F 5 .   ? 99.30958  23.42404  13.06056  1.000 70.27807  ? 1   NAG   F O6    1 
HETATM 7212 O O7    . NAG   F 5 .   ? 105.16005 20.70186  12.71771  1.000 90.00833  ? 1   NAG   F O7    1 
HETATM 7213 C C1    . NAG   F 5 .   ? 100.03673 24.44927  8.83703   1.000 83.79123  ? 2   NAG   F C1    1 
HETATM 7214 C C2    . NAG   F 5 .   ? 99.35636  25.79732  8.48823   1.000 84.39211  ? 2   NAG   F C2    1 
HETATM 7215 C C3    . NAG   F 5 .   ? 98.52682  25.76462  7.17321   1.000 97.31055  ? 2   NAG   F C3    1 
HETATM 7216 C C4    . NAG   F 5 .   ? 99.01194  24.75762  6.13129   1.000 102.06917 ? 2   NAG   F C4    1 
HETATM 7217 C C5    . NAG   F 5 .   ? 99.48556  23.49155  6.82176   1.000 94.15918  ? 2   NAG   F C5    1 
HETATM 7218 C C6    . NAG   F 5 .   ? 100.05423 22.47150  5.87511   1.000 94.66793  ? 2   NAG   F C6    1 
HETATM 7219 C C7    . NAG   F 5 .   ? 98.93772  27.03443  10.58613  1.000 92.91582  ? 2   NAG   F C7    1 
HETATM 7220 C C8    . NAG   F 5 .   ? 97.92685  27.36192  11.64957  1.000 76.75866  ? 2   NAG   F C8    1 
HETATM 7221 N N2    . NAG   F 5 .   ? 98.51639  26.23228  9.59693   1.000 86.75459  ? 2   NAG   F N2    1 
HETATM 7222 O O3    . NAG   F 5 .   ? 98.58192  27.06988  6.60254   1.000 102.78315 ? 2   NAG   F O3    1 
HETATM 7223 O O4    . NAG   F 5 .   ? 97.94801  24.37394  5.25785   1.000 101.76255 ? 2   NAG   F O4    1 
HETATM 7224 O O5    . NAG   F 5 .   ? 100.53592 23.85439  7.71366   1.000 83.26561  ? 2   NAG   F O5    1 
HETATM 7225 O O6    . NAG   F 5 .   ? 101.45535 22.39756  6.08912   1.000 103.01597 ? 2   NAG   F O6    1 
HETATM 7226 O O7    . NAG   F 5 .   ? 100.08800 27.46647  10.63039  1.000 99.18262  ? 2   NAG   F O7    1 
HETATM 7227 C C1    . MAN   F 5 .   ? 97.56184  25.01932  3.97777   1.000 102.42142 ? 3   MAN   F C1    1 
HETATM 7228 C C2    . MAN   F 5 .   ? 98.14545  24.16246  2.73683   1.000 104.19644 ? 3   MAN   F C2    1 
HETATM 7229 C C3    . MAN   F 5 .   ? 97.44433  24.60880  1.43745   1.000 113.83359 ? 3   MAN   F C3    1 
HETATM 7230 C C4    . MAN   F 5 .   ? 96.53661  25.88487  1.70720   1.000 119.49573 ? 3   MAN   F C4    1 
HETATM 7231 C C5    . MAN   F 5 .   ? 97.31470  27.00722  2.51078   1.000 110.47229 ? 3   MAN   F C5    1 
HETATM 7232 C C6    . MAN   F 5 .   ? 96.44245  28.25970  2.81048   1.000 103.99577 ? 3   MAN   F C6    1 
HETATM 7233 O O2    . MAN   F 5 .   ? 97.88984  22.76032  2.83309   1.000 109.30963 ? 3   MAN   F O2    1 
HETATM 7234 O O3    . MAN   F 5 .   ? 96.71823  23.51272  0.75935   1.000 114.45445 ? 3   MAN   F O3    1 
HETATM 7235 O O4    . MAN   F 5 .   ? 95.96447  26.43085  0.48537   1.000 121.83138 ? 3   MAN   F O4    1 
HETATM 7236 O O5    . MAN   F 5 .   ? 97.91406  26.43786  3.78227   1.000 106.84974 ? 3   MAN   F O5    1 
HETATM 7237 O O6    . MAN   F 5 .   ? 95.77578  28.67431  1.60107   1.000 88.24313  ? 3   MAN   F O6    1 
HETATM 7238 C C1    . NAG   G 5 .   ? 87.49466  6.67239   30.21384  1.000 71.47949  ? 1   NAG   G C1    1 
HETATM 7239 C C2    . NAG   G 5 .   ? 87.88156  5.36117   30.86974  1.000 75.78383  ? 1   NAG   G C2    1 
HETATM 7240 C C3    . NAG   G 5 .   ? 87.19536  4.18580   30.19896  1.000 77.51794  ? 1   NAG   G C3    1 
HETATM 7241 C C4    . NAG   G 5 .   ? 85.69926  4.41556   30.04910  1.000 80.43012  ? 1   NAG   G C4    1 
HETATM 7242 C C5    . NAG   G 5 .   ? 85.44241  5.78075   29.43006  1.000 80.99567  ? 1   NAG   G C5    1 
HETATM 7243 C C6    . NAG   G 5 .   ? 83.96993  6.13422   29.38402  1.000 85.24130  ? 1   NAG   G C6    1 
HETATM 7244 C C7    . NAG   G 5 .   ? 90.10303  5.45991   31.88574  1.000 74.03389  ? 1   NAG   G C7    1 
HETATM 7245 C C8    . NAG   G 5 .   ? 89.41981  5.98985   33.11039  1.000 69.57582  ? 1   NAG   G C8    1 
HETATM 7246 N N2    . NAG   G 5 .   ? 89.32064  5.19248   30.84193  1.000 79.00453  ? 1   NAG   G N2    1 
HETATM 7247 O O3    . NAG   G 5 .   ? 87.43100  3.02061   30.97806  1.000 83.99429  ? 1   NAG   G O3    1 
HETATM 7248 O O4    . NAG   G 5 .   ? 85.15670  3.42741   29.17629  1.000 91.79761  ? 1   NAG   G O4    1 
HETATM 7249 O O5    . NAG   G 5 .   ? 86.09817  6.79448   30.20094  1.000 78.00535  ? 1   NAG   G O5    1 
HETATM 7250 O O6    . NAG   G 5 .   ? 83.55460  6.84640   30.54286  1.000 69.87472  ? 1   NAG   G O6    1 
HETATM 7251 O O7    . NAG   G 5 .   ? 91.30753  5.31609   31.82556  1.000 76.05182  ? 1   NAG   G O7    1 
HETATM 7252 C C1    . NAG   G 5 .   ? 83.98407  2.78472   29.72021  1.000 95.55386  ? 2   NAG   G C1    1 
HETATM 7253 C C2    . NAG   G 5 .   ? 83.24586  2.26950   28.50762  1.000 95.16703  ? 2   NAG   G C2    1 
HETATM 7254 C C3    . NAG   G 5 .   ? 82.00489  1.48182   28.91376  1.000 106.89910 ? 2   NAG   G C3    1 
HETATM 7255 C C4    . NAG   G 5 .   ? 82.30512  0.47420   30.02499  1.000 117.05946 ? 2   NAG   G C4    1 
HETATM 7256 C C5    . NAG   G 5 .   ? 83.21155  1.06938   31.10971  1.000 111.21238 ? 2   NAG   G C5    1 
HETATM 7257 C C6    . NAG   G 5 .   ? 83.77225  0.01556   32.02991  1.000 116.80090 ? 2   NAG   G C6    1 
HETATM 7258 C C7    . NAG   G 5 .   ? 83.34029  3.45260   26.38488  1.000 93.35732  ? 2   NAG   G C7    1 
HETATM 7259 C C8    . NAG   G 5 .   ? 82.90774  4.65506   25.60089  1.000 91.47866  ? 2   NAG   G C8    1 
HETATM 7260 N N2    . NAG   G 5 .   ? 82.89213  3.37521   27.63638  1.000 92.47219  ? 2   NAG   G N2    1 
HETATM 7261 O O3    . NAG   G 5 .   ? 81.52709  0.80863   27.75191  1.000 101.85652 ? 2   NAG   G O3    1 
HETATM 7262 O O4    . NAG   G 5 .   ? 81.08792  0.09122   30.66741  1.000 121.29587 ? 2   NAG   G O4    1 
HETATM 7263 O O5    . NAG   G 5 .   ? 84.34306  1.72273   30.52359  1.000 105.60832 ? 2   NAG   G O5    1 
HETATM 7264 O O6    . NAG   G 5 .   ? 84.01852  -1.18417  31.30732  1.000 124.03465 ? 2   NAG   G O6    1 
HETATM 7265 O O7    . NAG   G 5 .   ? 84.06585  2.58772   25.90939  1.000 89.86826  ? 2   NAG   G O7    1 
HETATM 7266 C C1    . MAN   G 5 .   ? 80.68464  -1.30163  30.53471  1.000 119.78891 ? 3   MAN   G C1    1 
HETATM 7267 C C2    . MAN   G 5 .   ? 80.37926  -1.85018  31.97866  1.000 118.22404 ? 3   MAN   G C2    1 
HETATM 7268 C C3    . MAN   G 5 .   ? 80.97733  -3.24990  32.15647  1.000 120.27413 ? 3   MAN   G C3    1 
HETATM 7269 C C4    . MAN   G 5 .   ? 80.71600  -4.14472  30.88292  1.000 127.93357 ? 3   MAN   G C4    1 
HETATM 7270 C C5    . MAN   G 5 .   ? 81.23415  -3.44533  29.56065  1.000 126.17696 ? 3   MAN   G C5    1 
HETATM 7271 C C6    . MAN   G 5 .   ? 80.26198  -3.43042  28.30201  1.000 121.28511 ? 3   MAN   G C6    1 
HETATM 7272 O O2    . MAN   G 5 .   ? 78.97635  -1.99209  32.19718  1.000 120.74287 ? 3   MAN   G O2    1 
HETATM 7273 O O3    . MAN   G 5 .   ? 80.55971  -3.88809  33.41216  1.000 114.12305 ? 3   MAN   G O3    1 
HETATM 7274 O O4    . MAN   G 5 .   ? 81.39102  -5.38631  31.04264  1.000 127.31338 ? 3   MAN   G O4    1 
HETATM 7275 O O5    . MAN   G 5 .   ? 81.66194  -2.09310  29.86226  1.000 120.81866 ? 3   MAN   G O5    1 
HETATM 7276 O O6    . MAN   G 5 .   ? 78.86930  -3.32122  28.69337  1.000 117.13342 ? 3   MAN   G O6    1 
HETATM 7277 C C1    . NAG   H 5 .   ? 63.71657  45.77603  6.56701   1.000 97.85984  ? 1   NAG   H C1    1 
HETATM 7278 C C2    . NAG   H 5 .   ? 64.20241  47.20368  6.84313   1.000 95.01080  ? 1   NAG   H C2    1 
HETATM 7279 C C3    . NAG   H 5 .   ? 64.81938  47.83085  5.59934   1.000 92.75388  ? 1   NAG   H C3    1 
HETATM 7280 C C4    . NAG   H 5 .   ? 65.86355  46.92764  4.95618   1.000 86.53709  ? 1   NAG   H C4    1 
HETATM 7281 C C5    . NAG   H 5 .   ? 65.25903  45.55180  4.70330   1.000 91.08614  ? 1   NAG   H C5    1 
HETATM 7282 C C6    . NAG   H 5 .   ? 66.27297  44.54861  4.21445   1.000 92.54219  ? 1   NAG   H C6    1 
HETATM 7283 C C7    . NAG   H 5 .   ? 63.05996  48.66145  8.47349   1.000 99.05900  ? 1   NAG   H C7    1 
HETATM 7284 C C8    . NAG   H 5 .   ? 64.29416  48.55801  9.32057   1.000 97.56965  ? 1   NAG   H C8    1 
HETATM 7285 N N2    . NAG   H 5 .   ? 63.07891  47.99886  7.31295   1.000 95.52477  ? 1   NAG   H N2    1 
HETATM 7286 O O3    . NAG   H 5 .   ? 65.40432  49.07301  5.96361   1.000 99.58124  ? 1   NAG   H O3    1 
HETATM 7287 O O4    . NAG   H 5 .   ? 66.26326  47.49815  3.71155   1.000 86.59390  ? 1   NAG   H O4    1 
HETATM 7288 O O5    . NAG   H 5 .   ? 64.75297  45.02031  5.93327   1.000 100.26562 ? 1   NAG   H O5    1 
HETATM 7289 O O6    . NAG   H 5 .   ? 66.58607  43.61981  5.24412   1.000 96.48866  ? 1   NAG   H O6    1 
HETATM 7290 O O7    . NAG   H 5 .   ? 62.07481  49.28534  8.83857   1.000 98.44579  ? 1   NAG   H O7    1 
HETATM 7291 C C1    . NAG   H 5 .   ? 67.69957  47.65964  3.60796   1.000 88.26543  ? 2   NAG   H C1    1 
HETATM 7292 C C2    . NAG   H 5 .   ? 68.15191  47.67249  2.13539   1.000 84.70149  ? 2   NAG   H C2    1 
HETATM 7293 C C3    . NAG   H 5 .   ? 69.63623  47.99799  2.02433   1.000 92.33919  ? 2   NAG   H C3    1 
HETATM 7294 C C4    . NAG   H 5 .   ? 70.03527  49.20041  2.87068   1.000 97.02113  ? 2   NAG   H C4    1 
HETATM 7295 C C5    . NAG   H 5 .   ? 69.46198  49.07661  4.28131   1.000 94.79662  ? 2   NAG   H C5    1 
HETATM 7296 C C6    . NAG   H 5 .   ? 69.68566  50.30403  5.12859   1.000 97.70034  ? 2   NAG   H C6    1 
HETATM 7297 C C7    . NAG   H 5 .   ? 66.68662  46.06906  1.00848   1.000 86.26759  ? 2   NAG   H C7    1 
HETATM 7298 C C8    . NAG   H 5 .   ? 66.56816  44.70043  0.40726   1.000 90.30665  ? 2   NAG   H C8    1 
HETATM 7299 N N2    . NAG   H 5 .   ? 67.88074  46.39144  1.50923   1.000 78.08755  ? 2   NAG   H N2    1 
HETATM 7300 O O3    . NAG   H 5 .   ? 69.94571  48.24810  0.65844   1.000 101.72603 ? 2   NAG   H O3    1 
HETATM 7301 O O4    . NAG   H 5 .   ? 71.45508  49.16542  2.97920   1.000 106.16866 ? 2   NAG   H O4    1 
HETATM 7302 O O5    . NAG   H 5 .   ? 68.04528  48.88016  4.21837   1.000 91.46322  ? 2   NAG   H O5    1 
HETATM 7303 O O6    . NAG   H 5 .   ? 68.49179  51.06594  5.23652   1.000 91.93940  ? 2   NAG   H O6    1 
HETATM 7304 O O7    . NAG   H 5 .   ? 65.74127  46.84202  1.04865   1.000 90.76477  ? 2   NAG   H O7    1 
HETATM 7305 C C1    . MAN   H 5 .   ? 72.17476  50.35468  2.60223   1.000 115.03866 ? 3   MAN   H C1    1 
HETATM 7306 C C2    . MAN   H 5 .   ? 72.86442  50.12621  1.26567   1.000 113.59286 ? 3   MAN   H C2    1 
HETATM 7307 C C3    . MAN   H 5 .   ? 73.90054  51.27045  1.12310   1.000 119.70994 ? 3   MAN   H C3    1 
HETATM 7308 C C4    . MAN   H 5 .   ? 75.03722  51.07951  2.13826   1.000 115.82663 ? 3   MAN   H C4    1 
HETATM 7309 C C5    . MAN   H 5 .   ? 74.52186  50.21425  3.25515   1.000 119.41397 ? 3   MAN   H C5    1 
HETATM 7310 C C6    . MAN   H 5 .   ? 75.43368  50.28543  4.44588   1.000 110.56883 ? 3   MAN   H C6    1 
HETATM 7311 O O2    . MAN   H 5 .   ? 71.95627  50.14198  0.13906   1.000 112.51414 ? 3   MAN   H O2    1 
HETATM 7312 O O3    . MAN   H 5 .   ? 73.30897  52.56457  1.34866   1.000 115.69046 ? 3   MAN   H O3    1 
HETATM 7313 O O4    . MAN   H 5 .   ? 76.14735  50.44173  1.55423   1.000 109.73576 ? 3   MAN   H O4    1 
HETATM 7314 O O5    . MAN   H 5 .   ? 73.17451  50.70064  3.58365   1.000 124.54819 ? 3   MAN   H O5    1 
HETATM 7315 O O6    . MAN   H 5 .   ? 76.67907  50.76570  3.94134   1.000 106.54776 ? 3   MAN   H O6    1 
HETATM 7316 P PA    . FAD   I 6 .   ? 34.28351  1.79058   31.46462  1.000 49.55532  ? 501 FAD   A PA    1 
HETATM 7317 O O1A   . FAD   I 6 .   ? 34.47389  1.93534   32.92004  1.000 52.33241  ? 501 FAD   A O1A   1 
HETATM 7318 O O2A   . FAD   I 6 .   ? 32.85588  1.75393   30.92269  1.000 43.07124  ? 501 FAD   A O2A   1 
HETATM 7319 O O5B   . FAD   I 6 .   ? 34.94743  2.98438   30.75097  1.000 43.81941  ? 501 FAD   A O5B   1 
HETATM 7320 C C5B   . FAD   I 6 .   ? 36.28189  3.42296   31.07974  1.000 43.99301  ? 501 FAD   A C5B   1 
HETATM 7321 C C4B   . FAD   I 6 .   ? 36.41468  4.90036   30.80981  1.000 47.14279  ? 501 FAD   A C4B   1 
HETATM 7322 O O4B   . FAD   I 6 .   ? 36.05830  5.16086   29.43521  1.000 45.22810  ? 501 FAD   A O4B   1 
HETATM 7323 C C3B   . FAD   I 6 .   ? 35.54914  5.83384   31.65822  1.000 44.06233  ? 501 FAD   A C3B   1 
HETATM 7324 O O3B   . FAD   I 6 .   ? 36.21776  7.07524   31.85330  1.000 48.41723  ? 501 FAD   A O3B   1 
HETATM 7325 C C2B   . FAD   I 6 .   ? 34.34033  6.07787   30.76251  1.000 42.02935  ? 501 FAD   A C2B   1 
HETATM 7326 O O2B   . FAD   I 6 .   ? 33.71425  7.33631   30.98487  1.000 38.75766  ? 501 FAD   A O2B   1 
HETATM 7327 C C1B   . FAD   I 6 .   ? 35.00489  6.10413   29.38952  1.000 46.61277  ? 501 FAD   A C1B   1 
HETATM 7328 N N9A   . FAD   I 6 .   ? 34.07995  5.71401   28.34288  1.000 45.46915  ? 501 FAD   A N9A   1 
HETATM 7329 C C8A   . FAD   I 6 .   ? 33.27863  4.60677   28.34900  1.000 46.43473  ? 501 FAD   A C8A   1 
HETATM 7330 N N7A   . FAD   I 6 .   ? 32.50648  4.49884   27.29927  1.000 47.30767  ? 501 FAD   A N7A   1 
HETATM 7331 C C5A   . FAD   I 6 .   ? 32.80534  5.63135   26.56252  1.000 41.92134  ? 501 FAD   A C5A   1 
HETATM 7332 C C6A   . FAD   I 6 .   ? 32.31520  6.11351   25.33651  1.000 43.92096  ? 501 FAD   A C6A   1 
HETATM 7333 N N6A   . FAD   I 6 .   ? 31.37919  5.48208   24.61340  1.000 41.03284  ? 501 FAD   A N6A   1 
HETATM 7334 N N1A   . FAD   I 6 .   ? 32.82446  7.28577   24.87487  1.000 42.76355  ? 501 FAD   A N1A   1 
HETATM 7335 C C2A   . FAD   I 6 .   ? 33.74982  7.91229   25.60548  1.000 40.13086  ? 501 FAD   A C2A   1 
HETATM 7336 N N3A   . FAD   I 6 .   ? 34.27572  7.55123   26.77752  1.000 42.74416  ? 501 FAD   A N3A   1 
HETATM 7337 C C4A   . FAD   I 6 .   ? 33.76568  6.39431   27.19851  1.000 39.81084  ? 501 FAD   A C4A   1 
HETATM 7338 N N1    . FAD   I 6 .   ? 43.04934  -3.10091  28.27316  1.000 71.84827  ? 501 FAD   A N1    1 
HETATM 7339 C C2    . FAD   I 6 .   ? 43.88960  -3.47748  27.26221  1.000 72.14303  ? 501 FAD   A C2    1 
HETATM 7340 O O2    . FAD   I 6 .   ? 44.32699  -2.64698  26.44728  1.000 62.82256  ? 501 FAD   A O2    1 
HETATM 7341 N N3    . FAD   I 6 .   ? 44.26657  -4.81815  27.14213  1.000 68.70554  ? 501 FAD   A N3    1 
HETATM 7342 C C4    . FAD   I 6 .   ? 43.86325  -5.84602  27.95809  1.000 71.73572  ? 501 FAD   A C4    1 
HETATM 7343 O O4    . FAD   I 6 .   ? 44.26124  -6.99384  27.75877  1.000 76.86945  ? 501 FAD   A O4    1 
HETATM 7344 C C4X   . FAD   I 6 .   ? 42.97195  -5.42693  29.02144  1.000 72.07797  ? 501 FAD   A C4X   1 
HETATM 7345 N N5    . FAD   I 6 .   ? 42.54649  -6.33221  29.84627  1.000 71.80086  ? 501 FAD   A N5    1 
HETATM 7346 C C5X   . FAD   I 6 .   ? 41.69992  -5.93020  30.85594  1.000 64.73221  ? 501 FAD   A C5X   1 
HETATM 7347 C C6    . FAD   I 6 .   ? 41.22007  -6.88029  31.74485  1.000 61.15729  ? 501 FAD   A C6    1 
HETATM 7348 C C7    . FAD   I 6 .   ? 40.35100  -6.51779  32.76767  1.000 54.66048  ? 501 FAD   A C7    1 
HETATM 7349 C C7M   . FAD   I 6 .   ? 39.85540  -7.57015  33.71780  1.000 52.95049  ? 501 FAD   A C7M   1 
HETATM 7350 C C8    . FAD   I 6 .   ? 39.95001  -5.17922  32.90185  1.000 55.78925  ? 501 FAD   A C8    1 
HETATM 7351 C C8M   . FAD   I 6 .   ? 38.97414  -4.75476  33.96420  1.000 56.99427  ? 501 FAD   A C8M   1 
HETATM 7352 C C9    . FAD   I 6 .   ? 40.41970  -4.23092  32.01111  1.000 58.57781  ? 501 FAD   A C9    1 
HETATM 7353 C C9A   . FAD   I 6 .   ? 41.28913  -4.59858  31.00002  1.000 59.90274  ? 501 FAD   A C9A   1 
HETATM 7354 N N10   . FAD   I 6 .   ? 41.73912  -3.65879  30.06462  1.000 59.84504  ? 501 FAD   A N10   1 
HETATM 7355 C C10   . FAD   I 6 .   ? 42.62332  -4.02571  29.09419  1.000 69.12841  ? 501 FAD   A C10   1 
HETATM 7356 C "C1'" . FAD   I 6 .   ? 41.45685  -2.23561  30.26293  1.000 54.37314  ? 501 FAD   A "C1'" 1 
HETATM 7357 C "C2'" . FAD   I 6 .   ? 40.39643  -1.62601  29.37440  1.000 53.16966  ? 501 FAD   A "C2'" 1 
HETATM 7358 O "O2'" . FAD   I 6 .   ? 40.93291  -1.51250  28.06061  1.000 56.75839  ? 501 FAD   A "O2'" 1 
HETATM 7359 C "C3'" . FAD   I 6 .   ? 40.10958  -0.22351  29.91650  1.000 50.90047  ? 501 FAD   A "C3'" 1 
HETATM 7360 O "O3'" . FAD   I 6 .   ? 40.04015  -0.35911  31.33153  1.000 58.06873  ? 501 FAD   A "O3'" 1 
HETATM 7361 C "C4'" . FAD   I 6 .   ? 38.82847  0.47605   29.49190  1.000 44.71525  ? 501 FAD   A "C4'" 1 
HETATM 7362 O "O4'" . FAD   I 6 .   ? 38.79719  1.73576   30.16441  1.000 46.82359  ? 501 FAD   A "O4'" 1 
HETATM 7363 C "C5'" . FAD   I 6 .   ? 37.64002  -0.37872  29.86775  1.000 46.36925  ? 501 FAD   A "C5'" 1 
HETATM 7364 O "O5'" . FAD   I 6 .   ? 36.52036  -0.03784  29.02640  1.000 45.48495  ? 501 FAD   A "O5'" 1 
HETATM 7365 P P     . FAD   I 6 .   ? 35.04706  -0.23295  29.53099  1.000 58.66698  ? 501 FAD   A P     1 
HETATM 7366 O O1P   . FAD   I 6 .   ? 34.75709  -1.60745  29.69733  1.000 46.79612  ? 501 FAD   A O1P   1 
HETATM 7367 O O2P   . FAD   I 6 .   ? 33.99121  0.43298   28.65611  1.000 46.54644  ? 501 FAD   A O2P   1 
HETATM 7368 O O3P   . FAD   I 6 .   ? 35.06449  0.50412   30.94434  1.000 47.57351  ? 501 FAD   A O3P   1 
HETATM 7369 C C1    . NAG   J 7 .   ? 14.76027  -0.99414  40.45041  1.000 90.21916  ? 502 NAG   A C1    1 
HETATM 7370 C C2    . NAG   J 7 .   ? 14.06031  -2.10161  39.67990  1.000 100.70320 ? 502 NAG   A C2    1 
HETATM 7371 C C3    . NAG   J 7 .   ? 12.88522  -1.53218  38.88628  1.000 107.24604 ? 502 NAG   A C3    1 
HETATM 7372 C C4    . NAG   J 7 .   ? 11.92662  -0.81611  39.82929  1.000 106.40548 ? 502 NAG   A C4    1 
HETATM 7373 C C5    . NAG   J 7 .   ? 12.68341  0.26408   40.60505  1.000 105.82915 ? 502 NAG   A C5    1 
HETATM 7374 C C6    . NAG   J 7 .   ? 11.82826  0.93151   41.65702  1.000 108.08144 ? 502 NAG   A C6    1 
HETATM 7375 C C7    . NAG   J 7 .   ? 14.96594  -4.10020  38.55538  1.000 101.89638 ? 502 NAG   A C7    1 
HETATM 7376 C C8    . NAG   J 7 .   ? 13.82272  -4.85871  39.16360  1.000 100.05541 ? 502 NAG   A C8    1 
HETATM 7377 N N2    . NAG   J 7 .   ? 15.01477  -2.79012  38.82445  1.000 102.09258 ? 502 NAG   A N2    1 
HETATM 7378 O O3    . NAG   J 7 .   ? 12.17052  -2.54530  38.19072  1.000 107.63687 ? 502 NAG   A O3    1 
HETATM 7379 O O4    . NAG   J 7 .   ? 10.80873  -0.28030  39.11990  1.000 114.99866 ? 502 NAG   A O4    1 
HETATM 7380 O O5    . NAG   J 7 .   ? 13.80830  -0.31616  41.29266  1.000 95.28866  ? 502 NAG   A O5    1 
HETATM 7381 O O6    . NAG   J 7 .   ? 12.57361  1.25249   42.82507  1.000 99.51754  ? 502 NAG   A O6    1 
HETATM 7382 O O7    . NAG   J 7 .   ? 15.82342  -4.65271  37.87020  1.000 104.27494 ? 502 NAG   A O7    1 
HETATM 7383 C C14   . A1ITD K 8 .   ? 45.85046  -4.75159  30.78474  1.000 89.83866  ? 503 A1ITD A C14   1 
HETATM 7384 C C5    . A1ITD K 8 .   ? 47.59348  -7.64429  28.94932  1.000 111.93866 ? 503 A1ITD A C5    1 
HETATM 7385 C C6    . A1ITD K 8 .   ? 47.14541  -6.28711  29.23009  1.000 115.46866 ? 503 A1ITD A C6    1 
HETATM 7386 C C11   . A1ITD K 8 .   ? 45.14504  -5.51403  32.96172  1.000 92.44866  ? 503 A1ITD A C11   1 
HETATM 7387 C C7    . A1ITD K 8 .   ? 46.44648  -6.00094  30.52115  1.000 112.58866 ? 503 A1ITD A C7    1 
HETATM 7388 C C8    . A1ITD K 8 .   ? 46.36085  -6.98845  31.52060  1.000 112.95866 ? 503 A1ITD A C8    1 
HETATM 7389 C C9    . A1ITD K 8 .   ? 45.72714  -6.76698  32.73122  1.000 105.85866 ? 503 A1ITD A C9    1 
HETATM 7390 C C10   . A1ITD K 8 .   ? 45.65806  -7.84897  33.77494  1.000 99.82866  ? 503 A1ITD A C10   1 
HETATM 7391 C C12   . A1ITD K 8 .   ? 45.19683  -4.49246  31.99577  1.000 79.09866  ? 503 A1ITD A C12   1 
HETATM 7392 C C13   . A1ITD K 8 .   ? 44.57051  -3.15140  32.27340  1.000 73.77866  ? 503 A1ITD A C13   1 
HETATM 7393 O O1    . A1ITD K 8 .   ? 47.35941  -5.37472  28.40415  1.000 86.11866  ? 503 A1ITD A O1    1 
HETATM 7394 O O2    . A1ITD K 8 .   ? 44.51980  -5.24700  34.11561  1.000 86.97866  ? 503 A1ITD A O2    1 
HETATM 7395 O O3    . A1ITD K 8 .   ? 45.89265  -3.75578  29.86595  1.000 77.18866  ? 503 A1ITD A O3    1 
HETATM 7396 C C1    . NAG   L 7 .   ? 65.35750  -27.25300 22.07887  1.000 149.28045 ? 504 NAG   A C1    1 
HETATM 7397 C C2    . NAG   L 7 .   ? 66.06465  -28.48690 21.47800  1.000 162.02866 ? 504 NAG   A C2    1 
HETATM 7398 C C3    . NAG   L 7 .   ? 67.47166  -28.69177 22.06901  1.000 168.82866 ? 504 NAG   A C3    1 
HETATM 7399 C C4    . NAG   L 7 .   ? 67.46381  -28.69350 23.59672  1.000 166.43860 ? 504 NAG   A C4    1 
HETATM 7400 C C5    . NAG   L 7 .   ? 66.40470  -27.74725 24.15140  1.000 155.98824 ? 504 NAG   A C5    1 
HETATM 7401 C C6    . NAG   L 7 .   ? 66.81955  -27.02584 25.41730  1.000 147.71042 ? 504 NAG   A C6    1 
HETATM 7402 C C7    . NAG   L 7 .   ? 65.04416  -30.55489 20.64881  1.000 160.79335 ? 504 NAG   A C7    1 
HETATM 7403 C C8    . NAG   L 7 .   ? 65.76270  -30.27529 19.36828  1.000 151.15211 ? 504 NAG   A C8    1 
HETATM 7404 N N2    . NAG   L 7 .   ? 65.25761  -29.68427 21.63832  1.000 159.17588 ? 504 NAG   A N2    1 
HETATM 7405 O O3    . NAG   L 7 .   ? 68.37017  -27.71905 21.54118  1.000 168.18866 ? 504 NAG   A O3    1 
HETATM 7406 O O4    . NAG   L 7 .   ? 67.19158  -30.01563 24.04951  1.000 173.17866 ? 504 NAG   A O4    1 
HETATM 7407 O O5    . NAG   L 7 .   ? 66.10938  -26.74942 23.17008  1.000 153.95866 ? 504 NAG   A O5    1 
HETATM 7408 O O6    . NAG   L 7 .   ? 67.93164  -26.15797 25.24349  1.000 126.65606 ? 504 NAG   A O6    1 
HETATM 7409 O O7    . NAG   L 7 .   ? 64.34205  -31.55611 20.80107  1.000 164.32748 ? 504 NAG   A O7    1 
HETATM 7410 P PA    . FAD   M 6 .   ? 82.11005  24.57492  14.48916  1.000 69.15542  ? 501 FAD   B PA    1 
HETATM 7411 O O1A   . FAD   M 6 .   ? 81.73875  25.84006  15.19700  1.000 60.40992  ? 501 FAD   B O1A   1 
HETATM 7412 O O2A   . FAD   M 6 .   ? 83.61704  24.25081  14.49579  1.000 65.01567  ? 501 FAD   B O2A   1 
HETATM 7413 O O5B   . FAD   M 6 .   ? 81.41679  23.32632  15.18648  1.000 65.40574  ? 501 FAD   B O5B   1 
HETATM 7414 C C5B   . FAD   M 6 .   ? 80.04375  23.37999  15.63001  1.000 66.95833  ? 501 FAD   B C5B   1 
HETATM 7415 C C4B   . FAD   M 6 .   ? 79.92384  22.77639  17.00750  1.000 66.25897  ? 501 FAD   B C4B   1 
HETATM 7416 O O4B   . FAD   M 6 .   ? 80.35271  21.39498  16.98087  1.000 56.79295  ? 501 FAD   B O4B   1 
HETATM 7417 C C3B   . FAD   M 6 .   ? 80.77338  23.47357  18.06081  1.000 64.70597  ? 501 FAD   B C3B   1 
HETATM 7418 O O3B   . FAD   M 6 .   ? 80.10075  23.61283  19.30937  1.000 69.78934  ? 501 FAD   B O3B   1 
HETATM 7419 C C2B   . FAD   M 6 .   ? 82.02658  22.60050  18.10458  1.000 62.92192  ? 501 FAD   B C2B   1 
HETATM 7420 O O2B   . FAD   M 6 .   ? 82.57289  22.51588  19.40703  1.000 73.18459  ? 501 FAD   B O2B   1 
HETATM 7421 C C1B   . FAD   M 6 .   ? 81.47634  21.21431  17.80832  1.000 57.91863  ? 501 FAD   B C1B   1 
HETATM 7422 N N9A   . FAD   M 6 .   ? 82.44986  20.39040  17.09844  1.000 66.72647  ? 501 FAD   B N9A   1 
HETATM 7423 C C8A   . FAD   M 6 .   ? 83.19961  20.78236  16.01956  1.000 64.41286  ? 501 FAD   B C8A   1 
HETATM 7424 N N7A   . FAD   M 6 .   ? 84.00801  19.85659  15.55992  1.000 63.58395  ? 501 FAD   B N7A   1 
HETATM 7425 C C5A   . FAD   M 6 .   ? 83.78756  18.77931  16.40578  1.000 63.56682  ? 501 FAD   B C5A   1 
HETATM 7426 C C6A   . FAD   M 6 .   ? 84.34401  17.48286  16.45733  1.000 59.91142  ? 501 FAD   B C6A   1 
HETATM 7427 N N6A   . FAD   M 6 .   ? 85.27464  17.03732  15.60897  1.000 57.31025  ? 501 FAD   B N6A   1 
HETATM 7428 N N1A   . FAD   M 6 .   ? 83.90720  16.64831  17.42933  1.000 61.01277  ? 501 FAD   B N1A   1 
HETATM 7429 C C2A   . FAD   M 6 .   ? 82.98031  17.09153  18.28477  1.000 61.77983  ? 501 FAD   B C2A   1 
HETATM 7430 N N3A   . FAD   M 6 .   ? 82.38771  18.29099  18.33844  1.000 60.83592  ? 501 FAD   B N3A   1 
HETATM 7431 C C4A   . FAD   M 6 .   ? 82.83740  19.09659  17.36705  1.000 64.93292  ? 501 FAD   B C4A   1 
HETATM 7432 N N1    . FAD   M 6 .   ? 73.54128  22.49228  8.46779   1.000 71.16186  ? 501 FAD   B N1    1 
HETATM 7433 C C2    . FAD   M 6 .   ? 72.80813  21.57907  7.77026   1.000 76.45180  ? 501 FAD   B C2    1 
HETATM 7434 O O2    . FAD   M 6 .   ? 72.44979  20.51330  8.29197   1.000 74.69855  ? 501 FAD   B O2    1 
HETATM 7435 N N3    . FAD   M 6 .   ? 72.45462  21.85173  6.44692   1.000 82.47565  ? 501 FAD   B N3    1 
HETATM 7436 C C4    . FAD   M 6 .   ? 72.78218  23.00173  5.73121   1.000 78.79383  ? 501 FAD   B C4    1 
HETATM 7437 O O4    . FAD   M 6 .   ? 72.41793  23.13106  4.56040   1.000 75.94636  ? 501 FAD   B O4    1 
HETATM 7438 C C4X   . FAD   M 6 .   ? 73.56448  23.95782  6.50071   1.000 75.90422  ? 501 FAD   B C4X   1 
HETATM 7439 N N5    . FAD   M 6 .   ? 73.92225  25.06665  5.91998   1.000 72.91851  ? 501 FAD   B N5    1 
HETATM 7440 C C5X   . FAD   M 6 .   ? 74.66992  25.97321  6.65551   1.000 71.45115  ? 501 FAD   B C5X   1 
HETATM 7441 C C6    . FAD   M 6 .   ? 75.06649  27.15884  6.04267   1.000 72.34849  ? 501 FAD   B C6    1 
HETATM 7442 C C7    . FAD   M 6 .   ? 75.81923  28.10955  6.72542   1.000 65.03382  ? 501 FAD   B C7    1 
HETATM 7443 C C7M   . FAD   M 6 .   ? 76.21758  29.38022  6.02503   1.000 62.05482  ? 501 FAD   B C7M   1 
HETATM 7444 C C8    . FAD   M 6 .   ? 76.19630  27.87192  8.05605   1.000 70.41292  ? 501 FAD   B C8    1 
HETATM 7445 C C8M   . FAD   M 6 .   ? 77.06617  28.87112  8.79797   1.000 70.64047  ? 501 FAD   B C8M   1 
HETATM 7446 C C9    . FAD   M 6 .   ? 75.80347  26.68028  8.67485   1.000 70.60030  ? 501 FAD   B C9    1 
HETATM 7447 C C9A   . FAD   M 6 .   ? 75.04356  25.73107  7.98867   1.000 71.12711  ? 501 FAD   B C9A   1 
HETATM 7448 N N10   . FAD   M 6 .   ? 74.67903  24.48412  8.55460   1.000 71.75705  ? 501 FAD   B N10   1 
HETATM 7449 C C10   . FAD   M 6 .   ? 73.89561  23.60801  7.85902   1.000 73.15593  ? 501 FAD   B C10   1 
HETATM 7450 C "C1'" . FAD   M 6 .   ? 74.84889  24.21803  9.98582   1.000 67.48917  ? 501 FAD   B "C1'" 1 
HETATM 7451 C "C2'" . FAD   M 6 .   ? 76.13967  23.57713  10.42854  1.000 63.85611  ? 501 FAD   B "C2'" 1 
HETATM 7452 O "O2'" . FAD   M 6 .   ? 76.03782  22.15623  10.39906  1.000 59.17564  ? 501 FAD   B "O2'" 1 
HETATM 7453 C "C3'" . FAD   M 6 .   ? 76.30166  23.91608  11.90229  1.000 65.13012  ? 501 FAD   B "C3'" 1 
HETATM 7454 O "O3'" . FAD   M 6 .   ? 76.25842  25.33245  12.04984  1.000 66.35982  ? 501 FAD   B "O3'" 1 
HETATM 7455 C "C4'" . FAD   M 6 .   ? 77.53925  23.30383  12.53145  1.000 66.53048  ? 501 FAD   B "C4'" 1 
HETATM 7456 O "O4'" . FAD   M 6 .   ? 77.35927  23.21963  13.94641  1.000 71.50326  ? 501 FAD   B "O4'" 1 
HETATM 7457 C "C5'" . FAD   M 6 .   ? 78.78881  24.06021  12.14216  1.000 65.40046  ? 501 FAD   B "C5'" 1 
HETATM 7458 O "O5'" . FAD   M 6 .   ? 79.80848  23.10846  11.78456  1.000 62.71062  ? 501 FAD   B "O5'" 1 
HETATM 7459 P P     . FAD   M 6 .   ? 81.33262  23.48829  11.82723  1.000 61.89023  ? 501 FAD   B P     1 
HETATM 7460 O O1P   . FAD   M 6 .   ? 81.62605  24.07712  10.50830  1.000 64.05902  ? 501 FAD   B O1P   1 
HETATM 7461 O O2P   . FAD   M 6 .   ? 82.01967  22.17313  12.21515  1.000 60.76096  ? 501 FAD   B O2P   1 
HETATM 7462 O O3P   . FAD   M 6 .   ? 81.57424  24.60751  12.98812  1.000 63.31581  ? 501 FAD   B O3P   1 
HETATM 7463 C C4    . A1ITD N 8 .   ? 68.60813  22.62671  4.59478   1.000 90.03841  ? 502 A1ITD B C4    1 
HETATM 7464 C C14   . A1ITD N 8 .   ? 70.90546  25.59034  7.88511   1.000 82.54768  ? 502 A1ITD B C14   1 
HETATM 7465 C C5    . A1ITD N 8 .   ? 69.21735  23.81385  4.92816   1.000 93.22302  ? 502 A1ITD B C5    1 
HETATM 7466 C C6    . A1ITD N 8 .   ? 69.71857  24.07466  6.27115   1.000 87.18428  ? 502 A1ITD B C6    1 
HETATM 7467 C C11   . A1ITD N 8 .   ? 71.06500  27.96330  7.47391   1.000 85.67835  ? 502 A1ITD B C11   1 
HETATM 7468 C C7    . A1ITD N 8 .   ? 70.21480  25.42066  6.66775   1.000 82.43323  ? 502 A1ITD B C7    1 
HETATM 7469 C C8    . A1ITD N 8 .   ? 69.96047  26.56146  5.87890   1.000 84.18925  ? 502 A1ITD B C8    1 
HETATM 7470 C C9    . A1ITD N 8 .   ? 70.37193  27.82832  6.26083   1.000 87.48268  ? 502 A1ITD B C9    1 
HETATM 7471 C C10   . A1ITD N 8 .   ? 70.08327  29.02607  5.39519   1.000 75.88029  ? 502 A1ITD B C10   1 
HETATM 7472 C C12   . A1ITD N 8 .   ? 71.34046  26.85714  8.30047   1.000 81.19612  ? 502 A1ITD B C12   1 
HETATM 7473 C C13   . A1ITD N 8 .   ? 72.07485  27.04259  9.60376   1.000 70.22214  ? 502 A1ITD B C13   1 
HETATM 7474 O O1    . A1ITD N 8 .   ? 69.63013  23.18928  7.13418   1.000 84.43667  ? 502 A1ITD B O1    1 
HETATM 7475 O O2    . A1ITD N 8 .   ? 71.50390  29.14315  7.92524   1.000 76.97288  ? 502 A1ITD B O2    1 
HETATM 7476 O O3    . A1ITD N 8 .   ? 71.17213  24.52968  8.69186   1.000 80.19705  ? 502 A1ITD B O3    1 
HETATM 7477 C C1    . A1ITD N 8 .   ? 68.07871  22.26340  3.34152   1.000 89.38055  ? 502 A1ITD B C1    1 
HETATM 7478 C C1    . NAG   O 7 .   ? 52.29146  24.02031  -17.19420 1.000 143.79883 ? 503 NAG   B C1    1 
HETATM 7479 C C2    . NAG   O 7 .   ? 52.42308  23.53195  -18.65110 1.000 145.11866 ? 503 NAG   B C2    1 
HETATM 7480 C C3    . NAG   O 7 .   ? 52.33775  24.72796  -19.60137 1.000 142.03863 ? 503 NAG   B C3    1 
HETATM 7481 C C4    . NAG   O 7 .   ? 51.02922  25.47137  -19.37704 1.000 141.99308 ? 503 NAG   B C4    1 
HETATM 7482 C C5    . NAG   O 7 .   ? 50.93381  25.90704  -17.91917 1.000 140.68557 ? 503 NAG   B C5    1 
HETATM 7483 C C6    . NAG   O 7 .   ? 49.62758  26.59574  -17.60567 1.000 138.36700 ? 503 NAG   B C6    1 
HETATM 7484 C C7    . NAG   O 7 .   ? 54.86565  23.32475  -18.63621 1.000 142.85874 ? 503 NAG   B C7    1 
HETATM 7485 C C8    . NAG   O 7 .   ? 56.04122  22.42735  -18.90050 1.000 138.53071 ? 503 NAG   B C8    1 
HETATM 7486 N N2    . NAG   O 7 .   ? 53.66002  22.79516  -18.86122 1.000 151.80866 ? 503 NAG   B N2    1 
HETATM 7487 O O3    . NAG   O 7 .   ? 52.43457  24.31506  -20.95969 1.000 141.83514 ? 503 NAG   B O3    1 
HETATM 7488 O O4    . NAG   O 7 .   ? 50.94877  26.62274  -20.21000 1.000 137.16583 ? 503 NAG   B O4    1 
HETATM 7489 O O5    . NAG   O 7 .   ? 51.04444  24.76992  -17.04124 1.000 142.42933 ? 503 NAG   B O5    1 
HETATM 7490 O O6    . NAG   O 7 .   ? 49.32593  27.57027  -18.59780 1.000 129.76000 ? 503 NAG   B O6    1 
HETATM 7491 O O7    . NAG   O 7 .   ? 55.00247  24.48651  -18.28749 1.000 142.45760 ? 503 NAG   B O7    1 
HETATM 7492 C C1    . NAG   P 7 .   ? 101.41625 33.68815  15.02199  1.000 137.49866 ? 504 NAG   B C1    1 
HETATM 7493 C C2    . NAG   P 7 .   ? 102.07622 32.88641  13.85702  1.000 130.86866 ? 504 NAG   B C2    1 
HETATM 7494 C C3    . NAG   P 7 .   ? 103.43912 32.35605  14.27559  1.000 127.36634 ? 504 NAG   B C3    1 
HETATM 7495 C C4    . NAG   P 7 .   ? 104.25207 33.43290  14.96260  1.000 133.69807 ? 504 NAG   B C4    1 
HETATM 7496 C C5    . NAG   P 7 .   ? 103.60837 33.71114  16.31443  1.000 145.66348 ? 504 NAG   B C5    1 
HETATM 7497 C C6    . NAG   P 7 .   ? 103.81045 35.13336  16.78958  1.000 137.22457 ? 504 NAG   B C6    1 
HETATM 7498 C C7    . NAG   P 7 .   ? 100.09866 31.93427  12.75687  1.000 127.71866 ? 504 NAG   B C7    1 
HETATM 7499 C C8    . NAG   P 7 .   ? 99.36147  30.66591  12.42002  1.000 130.16866 ? 504 NAG   B C8    1 
HETATM 7500 N N2    . NAG   P 7 .   ? 101.22967 31.78063  13.44582  1.000 129.50866 ? 504 NAG   B N2    1 
HETATM 7501 O O3    . NAG   P 7 .   ? 104.15823 31.83254  13.16888  1.000 124.08022 ? 504 NAG   B O3    1 
HETATM 7502 O O4    . NAG   P 7 .   ? 105.58891 32.95590  15.09652  1.000 118.90955 ? 504 NAG   B O4    1 
HETATM 7503 O O5    . NAG   P 7 .   ? 102.18175 33.47156  16.28374  1.000 162.69866 ? 504 NAG   B O5    1 
HETATM 7504 O O6    . NAG   P 7 .   ? 103.15293 36.07766  15.95413  1.000 130.55597 ? 504 NAG   B O6    1 
HETATM 7505 O O7    . NAG   P 7 .   ? 99.71703  33.03192  12.37523  1.000 114.01027 ? 504 NAG   B O7    1 
HETATM 7506 O O     . HOH   Q 9 .   ? 18.46218  -0.08688  21.56747  1.000 46.33205  ? 601 HOH   A O     1 
HETATM 7507 O O     . HOH   Q 9 .   ? 35.26353  -15.13081 29.46916  1.000 43.09474  ? 602 HOH   A O     1 
HETATM 7508 O O     . HOH   Q 9 .   ? 70.12698  -30.41083 23.18724  1.000 102.27659 ? 603 HOH   A O     1 
HETATM 7509 O O     . HOH   Q 9 .   ? 46.10846  4.77243   12.92172  1.000 49.85797  ? 604 HOH   A O     1 
HETATM 7510 O O     . HOH   Q 9 .   ? 43.73304  -17.76792 42.02631  1.000 53.50814  ? 605 HOH   A O     1 
HETATM 7511 O O     . HOH   Q 9 .   ? 59.49391  -21.35919 12.00391  1.000 68.29051  ? 606 HOH   A O     1 
HETATM 7512 O O     . HOH   Q 9 .   ? 66.84151  -22.29450 19.37811  1.000 81.70538  ? 607 HOH   A O     1 
HETATM 7513 O O     . HOH   Q 9 .   ? 5.61991   1.88365   36.74548  1.000 59.78436  ? 608 HOH   A O     1 
HETATM 7514 O O     . HOH   R 9 .   ? 50.71364  41.03914  12.69911  1.000 80.09461  ? 601 HOH   B O     1 
# 
