data_9DX6
# 
_entry.id   9DX6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DX6         pdb_00009dx6 10.2210/pdb9dx6/pdb 
WWPDB D_1000289023 ?            ?                   
# 
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 2024-11-13 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_citation_author.identifier_ORCID' 
13 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DX6 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tham@wehi.edu.au 
_pdbx_contact_author.name_first         Wai-Hong 
_pdbx_contact_author.name_last          Tham 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7950-8699 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dietrich, M.H.' 1 0000-0002-2780-4389 
'Tham, W.H.'     2 0000-0001-7950-8699 
'Jung, N.C.'     3 ?                   
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10556 
_citation.page_last                 10556 
_citation.title                     
'Potent AMA1-specific human monoclonal antibody against Plasmodium vivax Pre-erythrocytic and Blood Stages.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-53848-4 
_citation.pdbx_database_id_PubMed   39632799 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Winnicki, A.C.'            1  ?                   
primary 'Dietrich, M.H.'            2  0000-0002-2780-4389 
primary 'Yeoh, L.M.'                3  0000-0001-7872-762X 
primary 'Carias, L.L.'              4  ?                   
primary 'Roobsoong, W.'             5  0000-0002-1789-0439 
primary 'Drago, C.L.'               6  ?                   
primary 'Malachin, A.N.'            7  ?                   
primary 'Redinger, K.R.'            8  0009-0008-5073-0809 
primary 'Feufack-Donfack, L.B.'     9  ?                   
primary 'Baldor, L.'                10 ?                   
primary 'Jung, N.C.'                11 ?                   
primary 'McLaine, O.S.'             12 ?                   
primary 'Skomorovska-Prokvolit, Y.' 13 ?                   
primary 'Orban, A.'                 14 ?                   
primary 'Opi, D.H.'                 15 0000-0002-4589-4365 
primary 'Kirtley, P.'               16 ?                   
primary 'Nielson, K.'               17 0009-0000-8429-4840 
primary 'Aleshnick, M.'             18 ?                   
primary 'Zanghi, G.'                19 ?                   
primary 'Rezakhani, N.'             20 ?                   
primary 'Vaughan, A.M.'             21 0000-0001-5815-756X 
primary 'Wilder, B.K.'              22 0000-0002-5577-7787 
primary 'Sattabongkot, J.'          23 ?                   
primary 'Tham, W.H.'                24 0000-0001-7950-8699 
primary 'Popovici, J.'              25 0000-0002-3135-1175 
primary 'Beeson, J.G.'              26 ?                   
primary 'Bosch, J.'                 27 0000-0002-2624-4105 
primary 'King, C.L.'                28 0000-0003-3873-7860 
# 
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 'Apical merozoite protein 1' 54376.090 1   ? 'S178N, N226D, N441Q' ? ? 
2 polymer man '826827 Fab Heavy chain'     24953.760 1   ? ?                     ? ? 
3 polymer man '826827 Fab Light chain'     23569.205 1   ? ?                     ? ? 
4 water   nat water                        18.015    259 ? ?                     ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;HHHHHHGRNQKPSRLTRSANNVLLEKGPTVERSTRMSNPWKAFMEKYDIERTHSSGVRVDLGEDAEVENAKYRIPAGRCP
VFGKGIVIENSAVSFLKPVATGDQRLKDGGFAFPNANDHISPMTLENLKARYKDNVEMMKLNDIALCRTHAASFVMAGDQ
NSNYRHPAVYDEKEKTCHMLYLSAQENMGPRYCSPDAQNRDAVFCFKPDKDESFENLVYLSKNVRNDWDKKCPRKNLGNA
KFGLWVDGNCEEIPYVKEVEAKDLRECNRIVFEASASDQPTQYEEEMTDYQKIQQGFRQNNREMIKSAFLPVGAFNSDNF
KSKGRGFNWANFDSVKKKCYIFNTKPTCLINDKNFIATTALSHPREVDLEFPCSIYKDEIEREIKKQSRNMNLYSVDGER
IVLPRIFISNDKESIKCPCEPEHISQSTCNFYVCNCVEKRAEIKENNQVVIKEEFRDYYENGEEKSNKQGS
;
;HHHHHHGRNQKPSRLTRSANNVLLEKGPTVERSTRMSNPWKAFMEKYDIERTHSSGVRVDLGEDAEVENAKYRIPAGRCP
VFGKGIVIENSAVSFLKPVATGDQRLKDGGFAFPNANDHISPMTLENLKARYKDNVEMMKLNDIALCRTHAASFVMAGDQ
NSNYRHPAVYDEKEKTCHMLYLSAQENMGPRYCSPDAQNRDAVFCFKPDKDESFENLVYLSKNVRNDWDKKCPRKNLGNA
KFGLWVDGNCEEIPYVKEVEAKDLRECNRIVFEASASDQPTQYEEEMTDYQKIQQGFRQNNREMIKSAFLPVGAFNSDNF
KSKGRGFNWANFDSVKKKCYIFNTKPTCLINDKNFIATTALSHPREVDLEFPCSIYKDEIEREIKKQSRNMNLYSVDGER
IVLPRIFISNDKESIKCPCEPEHISQSTCNFYVCNCVEKRAEIKENNQVVIKEEFRDYYENGEEKSNKQGS
;
A ? 
2 'polypeptide(L)' no no 
;QLQLQESGPGLVKPSETLSLTCTVSGGSVSSPGYYWSWIRQPPGQGLEWIGDIYYRGSSNQNPSLKSRVTTSVDTATNQF
SLRLSSVTAADTAVYFCARSRGEGYCSFGTCYTLFYYFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLV
KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
;QLQLQESGPGLVKPSETLSLTCTVSGGSVSSPGYYWSWIRQPPGQGLEWIGDIYYRGSSNQNPSLKSRVTTSVDTATNQF
SLRLSSVTAADTAVYFCARSRGEGYCSFGTCYTLFYYFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLV
KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
;
B ? 
3 'polypeptide(L)' no no 
;EIVMTQSPATLSLSPGERATLSCRASQSISKTLAWYQQKPGQAPRLLIYSASTRASGVPARFSGSGSGTEFSLTISSLQS
EDFAVYYCQQYNEWPPRPTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGN
SQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;EIVMTQSPATLSLSPGERATLSCRASQSISKTLAWYQQKPGQAPRLLIYSASTRASGVPARFSGSGSGTEFSLTISSLQS
EDFAVYYCQQYNEWPPRPTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGN
SQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
C ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   GLY n 
1 8   ARG n 
1 9   ASN n 
1 10  GLN n 
1 11  LYS n 
1 12  PRO n 
1 13  SER n 
1 14  ARG n 
1 15  LEU n 
1 16  THR n 
1 17  ARG n 
1 18  SER n 
1 19  ALA n 
1 20  ASN n 
1 21  ASN n 
1 22  VAL n 
1 23  LEU n 
1 24  LEU n 
1 25  GLU n 
1 26  LYS n 
1 27  GLY n 
1 28  PRO n 
1 29  THR n 
1 30  VAL n 
1 31  GLU n 
1 32  ARG n 
1 33  SER n 
1 34  THR n 
1 35  ARG n 
1 36  MET n 
1 37  SER n 
1 38  ASN n 
1 39  PRO n 
1 40  TRP n 
1 41  LYS n 
1 42  ALA n 
1 43  PHE n 
1 44  MET n 
1 45  GLU n 
1 46  LYS n 
1 47  TYR n 
1 48  ASP n 
1 49  ILE n 
1 50  GLU n 
1 51  ARG n 
1 52  THR n 
1 53  HIS n 
1 54  SER n 
1 55  SER n 
1 56  GLY n 
1 57  VAL n 
1 58  ARG n 
1 59  VAL n 
1 60  ASP n 
1 61  LEU n 
1 62  GLY n 
1 63  GLU n 
1 64  ASP n 
1 65  ALA n 
1 66  GLU n 
1 67  VAL n 
1 68  GLU n 
1 69  ASN n 
1 70  ALA n 
1 71  LYS n 
1 72  TYR n 
1 73  ARG n 
1 74  ILE n 
1 75  PRO n 
1 76  ALA n 
1 77  GLY n 
1 78  ARG n 
1 79  CYS n 
1 80  PRO n 
1 81  VAL n 
1 82  PHE n 
1 83  GLY n 
1 84  LYS n 
1 85  GLY n 
1 86  ILE n 
1 87  VAL n 
1 88  ILE n 
1 89  GLU n 
1 90  ASN n 
1 91  SER n 
1 92  ALA n 
1 93  VAL n 
1 94  SER n 
1 95  PHE n 
1 96  LEU n 
1 97  LYS n 
1 98  PRO n 
1 99  VAL n 
1 100 ALA n 
1 101 THR n 
1 102 GLY n 
1 103 ASP n 
1 104 GLN n 
1 105 ARG n 
1 106 LEU n 
1 107 LYS n 
1 108 ASP n 
1 109 GLY n 
1 110 GLY n 
1 111 PHE n 
1 112 ALA n 
1 113 PHE n 
1 114 PRO n 
1 115 ASN n 
1 116 ALA n 
1 117 ASN n 
1 118 ASP n 
1 119 HIS n 
1 120 ILE n 
1 121 SER n 
1 122 PRO n 
1 123 MET n 
1 124 THR n 
1 125 LEU n 
1 126 GLU n 
1 127 ASN n 
1 128 LEU n 
1 129 LYS n 
1 130 ALA n 
1 131 ARG n 
1 132 TYR n 
1 133 LYS n 
1 134 ASP n 
1 135 ASN n 
1 136 VAL n 
1 137 GLU n 
1 138 MET n 
1 139 MET n 
1 140 LYS n 
1 141 LEU n 
1 142 ASN n 
1 143 ASP n 
1 144 ILE n 
1 145 ALA n 
1 146 LEU n 
1 147 CYS n 
1 148 ARG n 
1 149 THR n 
1 150 HIS n 
1 151 ALA n 
1 152 ALA n 
1 153 SER n 
1 154 PHE n 
1 155 VAL n 
1 156 MET n 
1 157 ALA n 
1 158 GLY n 
1 159 ASP n 
1 160 GLN n 
1 161 ASN n 
1 162 SER n 
1 163 ASN n 
1 164 TYR n 
1 165 ARG n 
1 166 HIS n 
1 167 PRO n 
1 168 ALA n 
1 169 VAL n 
1 170 TYR n 
1 171 ASP n 
1 172 GLU n 
1 173 LYS n 
1 174 GLU n 
1 175 LYS n 
1 176 THR n 
1 177 CYS n 
1 178 HIS n 
1 179 MET n 
1 180 LEU n 
1 181 TYR n 
1 182 LEU n 
1 183 SER n 
1 184 ALA n 
1 185 GLN n 
1 186 GLU n 
1 187 ASN n 
1 188 MET n 
1 189 GLY n 
1 190 PRO n 
1 191 ARG n 
1 192 TYR n 
1 193 CYS n 
1 194 SER n 
1 195 PRO n 
1 196 ASP n 
1 197 ALA n 
1 198 GLN n 
1 199 ASN n 
1 200 ARG n 
1 201 ASP n 
1 202 ALA n 
1 203 VAL n 
1 204 PHE n 
1 205 CYS n 
1 206 PHE n 
1 207 LYS n 
1 208 PRO n 
1 209 ASP n 
1 210 LYS n 
1 211 ASP n 
1 212 GLU n 
1 213 SER n 
1 214 PHE n 
1 215 GLU n 
1 216 ASN n 
1 217 LEU n 
1 218 VAL n 
1 219 TYR n 
1 220 LEU n 
1 221 SER n 
1 222 LYS n 
1 223 ASN n 
1 224 VAL n 
1 225 ARG n 
1 226 ASN n 
1 227 ASP n 
1 228 TRP n 
1 229 ASP n 
1 230 LYS n 
1 231 LYS n 
1 232 CYS n 
1 233 PRO n 
1 234 ARG n 
1 235 LYS n 
1 236 ASN n 
1 237 LEU n 
1 238 GLY n 
1 239 ASN n 
1 240 ALA n 
1 241 LYS n 
1 242 PHE n 
1 243 GLY n 
1 244 LEU n 
1 245 TRP n 
1 246 VAL n 
1 247 ASP n 
1 248 GLY n 
1 249 ASN n 
1 250 CYS n 
1 251 GLU n 
1 252 GLU n 
1 253 ILE n 
1 254 PRO n 
1 255 TYR n 
1 256 VAL n 
1 257 LYS n 
1 258 GLU n 
1 259 VAL n 
1 260 GLU n 
1 261 ALA n 
1 262 LYS n 
1 263 ASP n 
1 264 LEU n 
1 265 ARG n 
1 266 GLU n 
1 267 CYS n 
1 268 ASN n 
1 269 ARG n 
1 270 ILE n 
1 271 VAL n 
1 272 PHE n 
1 273 GLU n 
1 274 ALA n 
1 275 SER n 
1 276 ALA n 
1 277 SER n 
1 278 ASP n 
1 279 GLN n 
1 280 PRO n 
1 281 THR n 
1 282 GLN n 
1 283 TYR n 
1 284 GLU n 
1 285 GLU n 
1 286 GLU n 
1 287 MET n 
1 288 THR n 
1 289 ASP n 
1 290 TYR n 
1 291 GLN n 
1 292 LYS n 
1 293 ILE n 
1 294 GLN n 
1 295 GLN n 
1 296 GLY n 
1 297 PHE n 
1 298 ARG n 
1 299 GLN n 
1 300 ASN n 
1 301 ASN n 
1 302 ARG n 
1 303 GLU n 
1 304 MET n 
1 305 ILE n 
1 306 LYS n 
1 307 SER n 
1 308 ALA n 
1 309 PHE n 
1 310 LEU n 
1 311 PRO n 
1 312 VAL n 
1 313 GLY n 
1 314 ALA n 
1 315 PHE n 
1 316 ASN n 
1 317 SER n 
1 318 ASP n 
1 319 ASN n 
1 320 PHE n 
1 321 LYS n 
1 322 SER n 
1 323 LYS n 
1 324 GLY n 
1 325 ARG n 
1 326 GLY n 
1 327 PHE n 
1 328 ASN n 
1 329 TRP n 
1 330 ALA n 
1 331 ASN n 
1 332 PHE n 
1 333 ASP n 
1 334 SER n 
1 335 VAL n 
1 336 LYS n 
1 337 LYS n 
1 338 LYS n 
1 339 CYS n 
1 340 TYR n 
1 341 ILE n 
1 342 PHE n 
1 343 ASN n 
1 344 THR n 
1 345 LYS n 
1 346 PRO n 
1 347 THR n 
1 348 CYS n 
1 349 LEU n 
1 350 ILE n 
1 351 ASN n 
1 352 ASP n 
1 353 LYS n 
1 354 ASN n 
1 355 PHE n 
1 356 ILE n 
1 357 ALA n 
1 358 THR n 
1 359 THR n 
1 360 ALA n 
1 361 LEU n 
1 362 SER n 
1 363 HIS n 
1 364 PRO n 
1 365 ARG n 
1 366 GLU n 
1 367 VAL n 
1 368 ASP n 
1 369 LEU n 
1 370 GLU n 
1 371 PHE n 
1 372 PRO n 
1 373 CYS n 
1 374 SER n 
1 375 ILE n 
1 376 TYR n 
1 377 LYS n 
1 378 ASP n 
1 379 GLU n 
1 380 ILE n 
1 381 GLU n 
1 382 ARG n 
1 383 GLU n 
1 384 ILE n 
1 385 LYS n 
1 386 LYS n 
1 387 GLN n 
1 388 SER n 
1 389 ARG n 
1 390 ASN n 
1 391 MET n 
1 392 ASN n 
1 393 LEU n 
1 394 TYR n 
1 395 SER n 
1 396 VAL n 
1 397 ASP n 
1 398 GLY n 
1 399 GLU n 
1 400 ARG n 
1 401 ILE n 
1 402 VAL n 
1 403 LEU n 
1 404 PRO n 
1 405 ARG n 
1 406 ILE n 
1 407 PHE n 
1 408 ILE n 
1 409 SER n 
1 410 ASN n 
1 411 ASP n 
1 412 LYS n 
1 413 GLU n 
1 414 SER n 
1 415 ILE n 
1 416 LYS n 
1 417 CYS n 
1 418 PRO n 
1 419 CYS n 
1 420 GLU n 
1 421 PRO n 
1 422 GLU n 
1 423 HIS n 
1 424 ILE n 
1 425 SER n 
1 426 GLN n 
1 427 SER n 
1 428 THR n 
1 429 CYS n 
1 430 ASN n 
1 431 PHE n 
1 432 TYR n 
1 433 VAL n 
1 434 CYS n 
1 435 ASN n 
1 436 CYS n 
1 437 VAL n 
1 438 GLU n 
1 439 LYS n 
1 440 ARG n 
1 441 ALA n 
1 442 GLU n 
1 443 ILE n 
1 444 LYS n 
1 445 GLU n 
1 446 ASN n 
1 447 ASN n 
1 448 GLN n 
1 449 VAL n 
1 450 VAL n 
1 451 ILE n 
1 452 LYS n 
1 453 GLU n 
1 454 GLU n 
1 455 PHE n 
1 456 ARG n 
1 457 ASP n 
1 458 TYR n 
1 459 TYR n 
1 460 GLU n 
1 461 ASN n 
1 462 GLY n 
1 463 GLU n 
1 464 GLU n 
1 465 LYS n 
1 466 SER n 
1 467 ASN n 
1 468 LYS n 
1 469 GLN n 
1 470 GLY n 
1 471 SER n 
2 1   GLN n 
2 2   LEU n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   PRO n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  LYS n 
2 14  PRO n 
2 15  SER n 
2 16  GLU n 
2 17  THR n 
2 18  LEU n 
2 19  SER n 
2 20  LEU n 
2 21  THR n 
2 22  CYS n 
2 23  THR n 
2 24  VAL n 
2 25  SER n 
2 26  GLY n 
2 27  GLY n 
2 28  SER n 
2 29  VAL n 
2 30  SER n 
2 31  SER n 
2 32  PRO n 
2 33  GLY n 
2 34  TYR n 
2 35  TYR n 
2 36  TRP n 
2 37  SER n 
2 38  TRP n 
2 39  ILE n 
2 40  ARG n 
2 41  GLN n 
2 42  PRO n 
2 43  PRO n 
2 44  GLY n 
2 45  GLN n 
2 46  GLY n 
2 47  LEU n 
2 48  GLU n 
2 49  TRP n 
2 50  ILE n 
2 51  GLY n 
2 52  ASP n 
2 53  ILE n 
2 54  TYR n 
2 55  TYR n 
2 56  ARG n 
2 57  GLY n 
2 58  SER n 
2 59  SER n 
2 60  ASN n 
2 61  GLN n 
2 62  ASN n 
2 63  PRO n 
2 64  SER n 
2 65  LEU n 
2 66  LYS n 
2 67  SER n 
2 68  ARG n 
2 69  VAL n 
2 70  THR n 
2 71  THR n 
2 72  SER n 
2 73  VAL n 
2 74  ASP n 
2 75  THR n 
2 76  ALA n 
2 77  THR n 
2 78  ASN n 
2 79  GLN n 
2 80  PHE n 
2 81  SER n 
2 82  LEU n 
2 83  ARG n 
2 84  LEU n 
2 85  SER n 
2 86  SER n 
2 87  VAL n 
2 88  THR n 
2 89  ALA n 
2 90  ALA n 
2 91  ASP n 
2 92  THR n 
2 93  ALA n 
2 94  VAL n 
2 95  TYR n 
2 96  PHE n 
2 97  CYS n 
2 98  ALA n 
2 99  ARG n 
2 100 SER n 
2 101 ARG n 
2 102 GLY n 
2 103 GLU n 
2 104 GLY n 
2 105 TYR n 
2 106 CYS n 
2 107 SER n 
2 108 PHE n 
2 109 GLY n 
2 110 THR n 
2 111 CYS n 
2 112 TYR n 
2 113 THR n 
2 114 LEU n 
2 115 PHE n 
2 116 TYR n 
2 117 TYR n 
2 118 PHE n 
2 119 ASP n 
2 120 TYR n 
2 121 TRP n 
2 122 GLY n 
2 123 GLN n 
2 124 GLY n 
2 125 THR n 
2 126 LEU n 
2 127 VAL n 
2 128 THR n 
2 129 VAL n 
2 130 SER n 
2 131 SER n 
2 132 ALA n 
2 133 SER n 
2 134 THR n 
2 135 LYS n 
2 136 GLY n 
2 137 PRO n 
2 138 SER n 
2 139 VAL n 
2 140 PHE n 
2 141 PRO n 
2 142 LEU n 
2 143 ALA n 
2 144 PRO n 
2 145 SER n 
2 146 SER n 
2 147 LYS n 
2 148 SER n 
2 149 THR n 
2 150 SER n 
2 151 GLY n 
2 152 GLY n 
2 153 THR n 
2 154 ALA n 
2 155 ALA n 
2 156 LEU n 
2 157 GLY n 
2 158 CYS n 
2 159 LEU n 
2 160 VAL n 
2 161 LYS n 
2 162 ASP n 
2 163 TYR n 
2 164 PHE n 
2 165 PRO n 
2 166 GLU n 
2 167 PRO n 
2 168 VAL n 
2 169 THR n 
2 170 VAL n 
2 171 SER n 
2 172 TRP n 
2 173 ASN n 
2 174 SER n 
2 175 GLY n 
2 176 ALA n 
2 177 LEU n 
2 178 THR n 
2 179 SER n 
2 180 GLY n 
2 181 VAL n 
2 182 HIS n 
2 183 THR n 
2 184 PHE n 
2 185 PRO n 
2 186 ALA n 
2 187 VAL n 
2 188 LEU n 
2 189 GLN n 
2 190 SER n 
2 191 SER n 
2 192 GLY n 
2 193 LEU n 
2 194 TYR n 
2 195 SER n 
2 196 LEU n 
2 197 SER n 
2 198 SER n 
2 199 VAL n 
2 200 VAL n 
2 201 THR n 
2 202 VAL n 
2 203 PRO n 
2 204 SER n 
2 205 SER n 
2 206 SER n 
2 207 LEU n 
2 208 GLY n 
2 209 THR n 
2 210 GLN n 
2 211 THR n 
2 212 TYR n 
2 213 ILE n 
2 214 CYS n 
2 215 ASN n 
2 216 VAL n 
2 217 ASN n 
2 218 HIS n 
2 219 LYS n 
2 220 PRO n 
2 221 SER n 
2 222 ASN n 
2 223 THR n 
2 224 LYS n 
2 225 VAL n 
2 226 ASP n 
2 227 LYS n 
2 228 ARG n 
2 229 VAL n 
2 230 GLU n 
2 231 PRO n 
2 232 LYS n 
2 233 SER n 
2 234 CYS n 
3 1   GLU n 
3 2   ILE n 
3 3   VAL n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   ALA n 
3 10  THR n 
3 11  LEU n 
3 12  SER n 
3 13  LEU n 
3 14  SER n 
3 15  PRO n 
3 16  GLY n 
3 17  GLU n 
3 18  ARG n 
3 19  ALA n 
3 20  THR n 
3 21  LEU n 
3 22  SER n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  ILE n 
3 30  SER n 
3 31  LYS n 
3 32  THR n 
3 33  LEU n 
3 34  ALA n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  GLN n 
3 43  ALA n 
3 44  PRO n 
3 45  ARG n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  SER n 
3 51  ALA n 
3 52  SER n 
3 53  THR n 
3 54  ARG n 
3 55  ALA n 
3 56  SER n 
3 57  GLY n 
3 58  VAL n 
3 59  PRO n 
3 60  ALA n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  GLU n 
3 71  PHE n 
3 72  SER n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  SER n 
3 81  GLU n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  VAL n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  TYR n 
3 92  ASN n 
3 93  GLU n 
3 94  TRP n 
3 95  PRO n 
3 96  PRO n 
3 97  ARG n 
3 98  PRO n 
3 99  THR n 
3 100 PHE n 
3 101 GLY n 
3 102 GLY n 
3 103 GLY n 
3 104 THR n 
3 105 LYS n 
3 106 VAL n 
3 107 GLU n 
3 108 ILE n 
3 109 LYS n 
3 110 ARG n 
3 111 THR n 
3 112 VAL n 
3 113 ALA n 
3 114 ALA n 
3 115 PRO n 
3 116 SER n 
3 117 VAL n 
3 118 PHE n 
3 119 ILE n 
3 120 PHE n 
3 121 PRO n 
3 122 PRO n 
3 123 SER n 
3 124 ASP n 
3 125 GLU n 
3 126 GLN n 
3 127 LEU n 
3 128 LYS n 
3 129 SER n 
3 130 GLY n 
3 131 THR n 
3 132 ALA n 
3 133 SER n 
3 134 VAL n 
3 135 VAL n 
3 136 CYS n 
3 137 LEU n 
3 138 LEU n 
3 139 ASN n 
3 140 ASN n 
3 141 PHE n 
3 142 TYR n 
3 143 PRO n 
3 144 ARG n 
3 145 GLU n 
3 146 ALA n 
3 147 LYS n 
3 148 VAL n 
3 149 GLN n 
3 150 TRP n 
3 151 LYS n 
3 152 VAL n 
3 153 ASP n 
3 154 ASN n 
3 155 ALA n 
3 156 LEU n 
3 157 GLN n 
3 158 SER n 
3 159 GLY n 
3 160 ASN n 
3 161 SER n 
3 162 GLN n 
3 163 GLU n 
3 164 SER n 
3 165 VAL n 
3 166 THR n 
3 167 GLU n 
3 168 GLN n 
3 169 ASP n 
3 170 SER n 
3 171 LYS n 
3 172 ASP n 
3 173 SER n 
3 174 THR n 
3 175 TYR n 
3 176 SER n 
3 177 LEU n 
3 178 SER n 
3 179 SER n 
3 180 THR n 
3 181 LEU n 
3 182 THR n 
3 183 LEU n 
3 184 SER n 
3 185 LYS n 
3 186 ALA n 
3 187 ASP n 
3 188 TYR n 
3 189 GLU n 
3 190 LYS n 
3 191 HIS n 
3 192 LYS n 
3 193 VAL n 
3 194 TYR n 
3 195 ALA n 
3 196 CYS n 
3 197 GLU n 
3 198 VAL n 
3 199 THR n 
3 200 HIS n 
3 201 GLN n 
3 202 GLY n 
3 203 LEU n 
3 204 SER n 
3 205 SER n 
3 206 PRO n 
3 207 VAL n 
3 208 THR n 
3 209 LYS n 
3 210 SER n 
3 211 PHE n 
3 212 ASN n 
3 213 ARG n 
3 214 GLY n 
3 215 GLU n 
3 216 CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 471 'malaria parasite P. vivax' ? ama1 ? ? ? ? ? ? 'Plasmodium vivax' 5855 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 234 ?                           ? ?    ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 216 ?                           ? ?    ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   16  ?   ?   ?   A . n 
A 1 2   HIS 2   17  ?   ?   ?   A . n 
A 1 3   HIS 3   18  ?   ?   ?   A . n 
A 1 4   HIS 4   19  ?   ?   ?   A . n 
A 1 5   HIS 5   20  ?   ?   ?   A . n 
A 1 6   HIS 6   21  ?   ?   ?   A . n 
A 1 7   GLY 7   22  ?   ?   ?   A . n 
A 1 8   ARG 8   23  ?   ?   ?   A . n 
A 1 9   ASN 9   24  ?   ?   ?   A . n 
A 1 10  GLN 10  25  ?   ?   ?   A . n 
A 1 11  LYS 11  26  ?   ?   ?   A . n 
A 1 12  PRO 12  27  ?   ?   ?   A . n 
A 1 13  SER 13  28  ?   ?   ?   A . n 
A 1 14  ARG 14  29  ?   ?   ?   A . n 
A 1 15  LEU 15  30  ?   ?   ?   A . n 
A 1 16  THR 16  31  ?   ?   ?   A . n 
A 1 17  ARG 17  32  ?   ?   ?   A . n 
A 1 18  SER 18  33  ?   ?   ?   A . n 
A 1 19  ALA 19  34  ?   ?   ?   A . n 
A 1 20  ASN 20  35  ?   ?   ?   A . n 
A 1 21  ASN 21  36  ?   ?   ?   A . n 
A 1 22  VAL 22  37  ?   ?   ?   A . n 
A 1 23  LEU 23  38  ?   ?   ?   A . n 
A 1 24  LEU 24  39  ?   ?   ?   A . n 
A 1 25  GLU 25  40  ?   ?   ?   A . n 
A 1 26  LYS 26  41  ?   ?   ?   A . n 
A 1 27  GLY 27  42  ?   ?   ?   A . n 
A 1 28  PRO 28  43  ?   ?   ?   A . n 
A 1 29  THR 29  44  ?   ?   ?   A . n 
A 1 30  VAL 30  45  ?   ?   ?   A . n 
A 1 31  GLU 31  46  46  GLU GLU A . n 
A 1 32  ARG 32  47  47  ARG ARG A . n 
A 1 33  SER 33  48  48  SER SER A . n 
A 1 34  THR 34  49  49  THR THR A . n 
A 1 35  ARG 35  50  50  ARG ARG A . n 
A 1 36  MET 36  51  51  MET MET A . n 
A 1 37  SER 37  52  52  SER SER A . n 
A 1 38  ASN 38  53  53  ASN ASN A . n 
A 1 39  PRO 39  54  54  PRO PRO A . n 
A 1 40  TRP 40  55  55  TRP TRP A . n 
A 1 41  LYS 41  56  56  LYS LYS A . n 
A 1 42  ALA 42  57  57  ALA ALA A . n 
A 1 43  PHE 43  58  58  PHE PHE A . n 
A 1 44  MET 44  59  59  MET MET A . n 
A 1 45  GLU 45  60  60  GLU GLU A . n 
A 1 46  LYS 46  61  61  LYS LYS A . n 
A 1 47  TYR 47  62  62  TYR TYR A . n 
A 1 48  ASP 48  63  63  ASP ASP A . n 
A 1 49  ILE 49  64  64  ILE ILE A . n 
A 1 50  GLU 50  65  65  GLU GLU A . n 
A 1 51  ARG 51  66  66  ARG ARG A . n 
A 1 52  THR 52  67  67  THR THR A . n 
A 1 53  HIS 53  68  68  HIS HIS A . n 
A 1 54  SER 54  69  69  SER SER A . n 
A 1 55  SER 55  70  70  SER SER A . n 
A 1 56  GLY 56  71  71  GLY GLY A . n 
A 1 57  VAL 57  72  72  VAL VAL A . n 
A 1 58  ARG 58  73  73  ARG ARG A . n 
A 1 59  VAL 59  74  74  VAL VAL A . n 
A 1 60  ASP 60  75  75  ASP ASP A . n 
A 1 61  LEU 61  76  76  LEU LEU A . n 
A 1 62  GLY 62  77  77  GLY GLY A . n 
A 1 63  GLU 63  78  78  GLU GLU A . n 
A 1 64  ASP 64  79  79  ASP ASP A . n 
A 1 65  ALA 65  80  80  ALA ALA A . n 
A 1 66  GLU 66  81  81  GLU GLU A . n 
A 1 67  VAL 67  82  82  VAL VAL A . n 
A 1 68  GLU 68  83  83  GLU GLU A . n 
A 1 69  ASN 69  84  84  ASN ASN A . n 
A 1 70  ALA 70  85  85  ALA ALA A . n 
A 1 71  LYS 71  86  86  LYS LYS A . n 
A 1 72  TYR 72  87  87  TYR TYR A . n 
A 1 73  ARG 73  88  88  ARG ARG A . n 
A 1 74  ILE 74  89  89  ILE ILE A . n 
A 1 75  PRO 75  90  90  PRO PRO A . n 
A 1 76  ALA 76  91  91  ALA ALA A . n 
A 1 77  GLY 77  92  92  GLY GLY A . n 
A 1 78  ARG 78  93  93  ARG ARG A . n 
A 1 79  CYS 79  94  94  CYS CYS A . n 
A 1 80  PRO 80  95  95  PRO PRO A . n 
A 1 81  VAL 81  96  96  VAL VAL A . n 
A 1 82  PHE 82  97  97  PHE PHE A . n 
A 1 83  GLY 83  98  98  GLY GLY A . n 
A 1 84  LYS 84  99  99  LYS LYS A . n 
A 1 85  GLY 85  100 100 GLY GLY A . n 
A 1 86  ILE 86  101 101 ILE ILE A . n 
A 1 87  VAL 87  102 102 VAL VAL A . n 
A 1 88  ILE 88  103 103 ILE ILE A . n 
A 1 89  GLU 89  104 104 GLU GLU A . n 
A 1 90  ASN 90  105 105 ASN ASN A . n 
A 1 91  SER 91  106 106 SER SER A . n 
A 1 92  ALA 92  107 107 ALA ALA A . n 
A 1 93  VAL 93  108 108 VAL VAL A . n 
A 1 94  SER 94  109 109 SER SER A . n 
A 1 95  PHE 95  110 110 PHE PHE A . n 
A 1 96  LEU 96  111 111 LEU LEU A . n 
A 1 97  LYS 97  112 112 LYS LYS A . n 
A 1 98  PRO 98  113 113 PRO PRO A . n 
A 1 99  VAL 99  114 114 VAL VAL A . n 
A 1 100 ALA 100 115 115 ALA ALA A . n 
A 1 101 THR 101 116 116 THR THR A . n 
A 1 102 GLY 102 117 117 GLY GLY A . n 
A 1 103 ASP 103 118 118 ASP ASP A . n 
A 1 104 GLN 104 119 119 GLN GLN A . n 
A 1 105 ARG 105 120 120 ARG ARG A . n 
A 1 106 LEU 106 121 121 LEU LEU A . n 
A 1 107 LYS 107 122 122 LYS LYS A . n 
A 1 108 ASP 108 123 123 ASP ASP A . n 
A 1 109 GLY 109 124 124 GLY GLY A . n 
A 1 110 GLY 110 125 125 GLY GLY A . n 
A 1 111 PHE 111 126 126 PHE PHE A . n 
A 1 112 ALA 112 127 127 ALA ALA A . n 
A 1 113 PHE 113 128 128 PHE PHE A . n 
A 1 114 PRO 114 129 129 PRO PRO A . n 
A 1 115 ASN 115 130 130 ASN ASN A . n 
A 1 116 ALA 116 131 131 ALA ALA A . n 
A 1 117 ASN 117 132 132 ASN ASN A . n 
A 1 118 ASP 118 133 133 ASP ASP A . n 
A 1 119 HIS 119 134 134 HIS HIS A . n 
A 1 120 ILE 120 135 135 ILE ILE A . n 
A 1 121 SER 121 136 136 SER SER A . n 
A 1 122 PRO 122 137 137 PRO PRO A . n 
A 1 123 MET 123 138 138 MET MET A . n 
A 1 124 THR 124 139 139 THR THR A . n 
A 1 125 LEU 125 140 140 LEU LEU A . n 
A 1 126 GLU 126 141 141 GLU GLU A . n 
A 1 127 ASN 127 142 142 ASN ASN A . n 
A 1 128 LEU 128 143 143 LEU LEU A . n 
A 1 129 LYS 129 144 144 LYS LYS A . n 
A 1 130 ALA 130 145 145 ALA ALA A . n 
A 1 131 ARG 131 146 146 ARG ARG A . n 
A 1 132 TYR 132 147 147 TYR TYR A . n 
A 1 133 LYS 133 148 148 LYS LYS A . n 
A 1 134 ASP 134 149 149 ASP ASP A . n 
A 1 135 ASN 135 150 150 ASN ASN A . n 
A 1 136 VAL 136 151 151 VAL VAL A . n 
A 1 137 GLU 137 152 152 GLU GLU A . n 
A 1 138 MET 138 153 153 MET MET A . n 
A 1 139 MET 139 154 154 MET MET A . n 
A 1 140 LYS 140 155 155 LYS LYS A . n 
A 1 141 LEU 141 156 156 LEU LEU A . n 
A 1 142 ASN 142 157 157 ASN ASN A . n 
A 1 143 ASP 143 158 158 ASP ASP A . n 
A 1 144 ILE 144 159 159 ILE ILE A . n 
A 1 145 ALA 145 160 160 ALA ALA A . n 
A 1 146 LEU 146 161 161 LEU LEU A . n 
A 1 147 CYS 147 162 162 CYS CYS A . n 
A 1 148 ARG 148 163 163 ARG ARG A . n 
A 1 149 THR 149 164 164 THR THR A . n 
A 1 150 HIS 150 165 165 HIS HIS A . n 
A 1 151 ALA 151 166 166 ALA ALA A . n 
A 1 152 ALA 152 167 167 ALA ALA A . n 
A 1 153 SER 153 168 168 SER SER A . n 
A 1 154 PHE 154 169 169 PHE PHE A . n 
A 1 155 VAL 155 170 170 VAL VAL A . n 
A 1 156 MET 156 171 171 MET MET A . n 
A 1 157 ALA 157 172 172 ALA ALA A . n 
A 1 158 GLY 158 173 173 GLY GLY A . n 
A 1 159 ASP 159 174 174 ASP ASP A . n 
A 1 160 GLN 160 175 175 GLN GLN A . n 
A 1 161 ASN 161 176 176 ASN ASN A . n 
A 1 162 SER 162 177 177 SER SER A . n 
A 1 163 ASN 163 178 178 ASN ASN A . n 
A 1 164 TYR 164 179 179 TYR TYR A . n 
A 1 165 ARG 165 180 180 ARG ARG A . n 
A 1 166 HIS 166 181 181 HIS HIS A . n 
A 1 167 PRO 167 182 182 PRO PRO A . n 
A 1 168 ALA 168 183 183 ALA ALA A . n 
A 1 169 VAL 169 184 184 VAL VAL A . n 
A 1 170 TYR 170 185 185 TYR TYR A . n 
A 1 171 ASP 171 186 186 ASP ASP A . n 
A 1 172 GLU 172 187 187 GLU GLU A . n 
A 1 173 LYS 173 188 188 LYS LYS A . n 
A 1 174 GLU 174 189 189 GLU GLU A . n 
A 1 175 LYS 175 190 190 LYS LYS A . n 
A 1 176 THR 176 191 191 THR THR A . n 
A 1 177 CYS 177 192 192 CYS CYS A . n 
A 1 178 HIS 178 193 193 HIS HIS A . n 
A 1 179 MET 179 194 194 MET MET A . n 
A 1 180 LEU 180 195 195 LEU LEU A . n 
A 1 181 TYR 181 196 196 TYR TYR A . n 
A 1 182 LEU 182 197 197 LEU LEU A . n 
A 1 183 SER 183 198 198 SER SER A . n 
A 1 184 ALA 184 199 199 ALA ALA A . n 
A 1 185 GLN 185 200 200 GLN GLN A . n 
A 1 186 GLU 186 201 201 GLU GLU A . n 
A 1 187 ASN 187 202 202 ASN ASN A . n 
A 1 188 MET 188 203 203 MET MET A . n 
A 1 189 GLY 189 204 204 GLY GLY A . n 
A 1 190 PRO 190 205 205 PRO PRO A . n 
A 1 191 ARG 191 206 206 ARG ARG A . n 
A 1 192 TYR 192 207 207 TYR TYR A . n 
A 1 193 CYS 193 208 208 CYS CYS A . n 
A 1 194 SER 194 209 209 SER SER A . n 
A 1 195 PRO 195 210 210 PRO PRO A . n 
A 1 196 ASP 196 211 ?   ?   ?   A . n 
A 1 197 ALA 197 212 ?   ?   ?   A . n 
A 1 198 GLN 198 213 ?   ?   ?   A . n 
A 1 199 ASN 199 214 ?   ?   ?   A . n 
A 1 200 ARG 200 215 ?   ?   ?   A . n 
A 1 201 ASP 201 216 216 ASP ASP A . n 
A 1 202 ALA 202 217 217 ALA ALA A . n 
A 1 203 VAL 203 218 218 VAL VAL A . n 
A 1 204 PHE 204 219 219 PHE PHE A . n 
A 1 205 CYS 205 220 220 CYS CYS A . n 
A 1 206 PHE 206 221 221 PHE PHE A . n 
A 1 207 LYS 207 222 222 LYS LYS A . n 
A 1 208 PRO 208 223 223 PRO PRO A . n 
A 1 209 ASP 209 224 224 ASP ASP A . n 
A 1 210 LYS 210 225 225 LYS LYS A . n 
A 1 211 ASP 211 226 226 ASP ASP A . n 
A 1 212 GLU 212 227 227 GLU GLU A . n 
A 1 213 SER 213 228 228 SER SER A . n 
A 1 214 PHE 214 229 229 PHE PHE A . n 
A 1 215 GLU 215 230 230 GLU GLU A . n 
A 1 216 ASN 216 231 231 ASN ASN A . n 
A 1 217 LEU 217 232 232 LEU LEU A . n 
A 1 218 VAL 218 233 233 VAL VAL A . n 
A 1 219 TYR 219 234 234 TYR TYR A . n 
A 1 220 LEU 220 235 235 LEU LEU A . n 
A 1 221 SER 221 236 236 SER SER A . n 
A 1 222 LYS 222 237 237 LYS LYS A . n 
A 1 223 ASN 223 238 238 ASN ASN A . n 
A 1 224 VAL 224 239 239 VAL VAL A . n 
A 1 225 ARG 225 240 240 ARG ARG A . n 
A 1 226 ASN 226 241 241 ASN ASN A . n 
A 1 227 ASP 227 242 242 ASP ASP A . n 
A 1 228 TRP 228 243 243 TRP TRP A . n 
A 1 229 ASP 229 244 244 ASP ASP A . n 
A 1 230 LYS 230 245 245 LYS LYS A . n 
A 1 231 LYS 231 246 246 LYS LYS A . n 
A 1 232 CYS 232 247 247 CYS CYS A . n 
A 1 233 PRO 233 248 248 PRO PRO A . n 
A 1 234 ARG 234 249 249 ARG ARG A . n 
A 1 235 LYS 235 250 250 LYS LYS A . n 
A 1 236 ASN 236 251 251 ASN ASN A . n 
A 1 237 LEU 237 252 252 LEU LEU A . n 
A 1 238 GLY 238 253 253 GLY GLY A . n 
A 1 239 ASN 239 254 254 ASN ASN A . n 
A 1 240 ALA 240 255 255 ALA ALA A . n 
A 1 241 LYS 241 256 256 LYS LYS A . n 
A 1 242 PHE 242 257 257 PHE PHE A . n 
A 1 243 GLY 243 258 258 GLY GLY A . n 
A 1 244 LEU 244 259 259 LEU LEU A . n 
A 1 245 TRP 245 260 260 TRP TRP A . n 
A 1 246 VAL 246 261 261 VAL VAL A . n 
A 1 247 ASP 247 262 262 ASP ASP A . n 
A 1 248 GLY 248 263 263 GLY GLY A . n 
A 1 249 ASN 249 264 264 ASN ASN A . n 
A 1 250 CYS 250 265 265 CYS CYS A . n 
A 1 251 GLU 251 266 266 GLU GLU A . n 
A 1 252 GLU 252 267 267 GLU GLU A . n 
A 1 253 ILE 253 268 268 ILE ILE A . n 
A 1 254 PRO 254 269 269 PRO PRO A . n 
A 1 255 TYR 255 270 270 TYR TYR A . n 
A 1 256 VAL 256 271 271 VAL VAL A . n 
A 1 257 LYS 257 272 272 LYS LYS A . n 
A 1 258 GLU 258 273 273 GLU GLU A . n 
A 1 259 VAL 259 274 274 VAL VAL A . n 
A 1 260 GLU 260 275 275 GLU GLU A . n 
A 1 261 ALA 261 276 276 ALA ALA A . n 
A 1 262 LYS 262 277 277 LYS LYS A . n 
A 1 263 ASP 263 278 278 ASP ASP A . n 
A 1 264 LEU 264 279 279 LEU LEU A . n 
A 1 265 ARG 265 280 280 ARG ARG A . n 
A 1 266 GLU 266 281 281 GLU GLU A . n 
A 1 267 CYS 267 282 282 CYS CYS A . n 
A 1 268 ASN 268 283 283 ASN ASN A . n 
A 1 269 ARG 269 284 284 ARG ARG A . n 
A 1 270 ILE 270 285 285 ILE ILE A . n 
A 1 271 VAL 271 286 286 VAL VAL A . n 
A 1 272 PHE 272 287 287 PHE PHE A . n 
A 1 273 GLU 273 288 288 GLU GLU A . n 
A 1 274 ALA 274 289 289 ALA ALA A . n 
A 1 275 SER 275 290 290 SER SER A . n 
A 1 276 ALA 276 291 291 ALA ALA A . n 
A 1 277 SER 277 292 292 SER SER A . n 
A 1 278 ASP 278 293 293 ASP ASP A . n 
A 1 279 GLN 279 294 294 GLN GLN A . n 
A 1 280 PRO 280 295 295 PRO PRO A . n 
A 1 281 THR 281 296 ?   ?   ?   A . n 
A 1 282 GLN 282 297 ?   ?   ?   A . n 
A 1 283 TYR 283 298 ?   ?   ?   A . n 
A 1 284 GLU 284 299 ?   ?   ?   A . n 
A 1 285 GLU 285 300 ?   ?   ?   A . n 
A 1 286 GLU 286 301 ?   ?   ?   A . n 
A 1 287 MET 287 302 ?   ?   ?   A . n 
A 1 288 THR 288 303 ?   ?   ?   A . n 
A 1 289 ASP 289 304 304 ASP ASP A . n 
A 1 290 TYR 290 305 305 TYR TYR A . n 
A 1 291 GLN 291 306 306 GLN GLN A . n 
A 1 292 LYS 292 307 307 LYS LYS A . n 
A 1 293 ILE 293 308 308 ILE ILE A . n 
A 1 294 GLN 294 309 309 GLN GLN A . n 
A 1 295 GLN 295 310 310 GLN GLN A . n 
A 1 296 GLY 296 311 311 GLY GLY A . n 
A 1 297 PHE 297 312 312 PHE PHE A . n 
A 1 298 ARG 298 313 313 ARG ARG A . n 
A 1 299 GLN 299 314 314 GLN GLN A . n 
A 1 300 ASN 300 315 315 ASN ASN A . n 
A 1 301 ASN 301 316 316 ASN ASN A . n 
A 1 302 ARG 302 317 317 ARG ARG A . n 
A 1 303 GLU 303 318 318 GLU GLU A . n 
A 1 304 MET 304 319 319 MET MET A . n 
A 1 305 ILE 305 320 320 ILE ILE A . n 
A 1 306 LYS 306 321 321 LYS LYS A . n 
A 1 307 SER 307 322 322 SER SER A . n 
A 1 308 ALA 308 323 323 ALA ALA A . n 
A 1 309 PHE 309 324 324 PHE PHE A . n 
A 1 310 LEU 310 325 325 LEU LEU A . n 
A 1 311 PRO 311 326 326 PRO PRO A . n 
A 1 312 VAL 312 327 327 VAL VAL A . n 
A 1 313 GLY 313 328 ?   ?   ?   A . n 
A 1 314 ALA 314 329 ?   ?   ?   A . n 
A 1 315 PHE 315 330 ?   ?   ?   A . n 
A 1 316 ASN 316 331 ?   ?   ?   A . n 
A 1 317 SER 317 332 ?   ?   ?   A . n 
A 1 318 ASP 318 333 ?   ?   ?   A . n 
A 1 319 ASN 319 334 ?   ?   ?   A . n 
A 1 320 PHE 320 335 335 PHE PHE A . n 
A 1 321 LYS 321 336 336 LYS LYS A . n 
A 1 322 SER 322 337 337 SER SER A . n 
A 1 323 LYS 323 338 338 LYS LYS A . n 
A 1 324 GLY 324 339 339 GLY GLY A . n 
A 1 325 ARG 325 340 340 ARG ARG A . n 
A 1 326 GLY 326 341 341 GLY GLY A . n 
A 1 327 PHE 327 342 342 PHE PHE A . n 
A 1 328 ASN 328 343 343 ASN ASN A . n 
A 1 329 TRP 329 344 344 TRP TRP A . n 
A 1 330 ALA 330 345 345 ALA ALA A . n 
A 1 331 ASN 331 346 346 ASN ASN A . n 
A 1 332 PHE 332 347 347 PHE PHE A . n 
A 1 333 ASP 333 348 348 ASP ASP A . n 
A 1 334 SER 334 349 349 SER SER A . n 
A 1 335 VAL 335 350 350 VAL VAL A . n 
A 1 336 LYS 336 351 351 LYS LYS A . n 
A 1 337 LYS 337 352 352 LYS LYS A . n 
A 1 338 LYS 338 353 353 LYS LYS A . n 
A 1 339 CYS 339 354 354 CYS CYS A . n 
A 1 340 TYR 340 355 355 TYR TYR A . n 
A 1 341 ILE 341 356 356 ILE ILE A . n 
A 1 342 PHE 342 357 357 PHE PHE A . n 
A 1 343 ASN 343 358 358 ASN ASN A . n 
A 1 344 THR 344 359 359 THR THR A . n 
A 1 345 LYS 345 360 360 LYS LYS A . n 
A 1 346 PRO 346 361 361 PRO PRO A . n 
A 1 347 THR 347 362 362 THR THR A . n 
A 1 348 CYS 348 363 363 CYS CYS A . n 
A 1 349 LEU 349 364 364 LEU LEU A . n 
A 1 350 ILE 350 365 365 ILE ILE A . n 
A 1 351 ASN 351 366 366 ASN ASN A . n 
A 1 352 ASP 352 367 367 ASP ASP A . n 
A 1 353 LYS 353 368 368 LYS LYS A . n 
A 1 354 ASN 354 369 369 ASN ASN A . n 
A 1 355 PHE 355 370 370 PHE PHE A . n 
A 1 356 ILE 356 371 371 ILE ILE A . n 
A 1 357 ALA 357 372 372 ALA ALA A . n 
A 1 358 THR 358 373 373 THR THR A . n 
A 1 359 THR 359 374 374 THR THR A . n 
A 1 360 ALA 360 375 375 ALA ALA A . n 
A 1 361 LEU 361 376 376 LEU LEU A . n 
A 1 362 SER 362 377 377 SER SER A . n 
A 1 363 HIS 363 378 378 HIS HIS A . n 
A 1 364 PRO 364 379 379 PRO PRO A . n 
A 1 365 ARG 365 380 380 ARG ARG A . n 
A 1 366 GLU 366 381 381 GLU GLU A . n 
A 1 367 VAL 367 382 382 VAL VAL A . n 
A 1 368 ASP 368 383 383 ASP ASP A . n 
A 1 369 LEU 369 384 384 LEU LEU A . n 
A 1 370 GLU 370 385 385 GLU GLU A . n 
A 1 371 PHE 371 386 386 PHE PHE A . n 
A 1 372 PRO 372 387 387 PRO PRO A . n 
A 1 373 CYS 373 388 388 CYS CYS A . n 
A 1 374 SER 374 389 389 SER SER A . n 
A 1 375 ILE 375 390 390 ILE ILE A . n 
A 1 376 TYR 376 391 391 TYR TYR A . n 
A 1 377 LYS 377 392 392 LYS LYS A . n 
A 1 378 ASP 378 393 393 ASP ASP A . n 
A 1 379 GLU 379 394 394 GLU GLU A . n 
A 1 380 ILE 380 395 395 ILE ILE A . n 
A 1 381 GLU 381 396 396 GLU GLU A . n 
A 1 382 ARG 382 397 397 ARG ARG A . n 
A 1 383 GLU 383 398 398 GLU GLU A . n 
A 1 384 ILE 384 399 399 ILE ILE A . n 
A 1 385 LYS 385 400 400 LYS LYS A . n 
A 1 386 LYS 386 401 401 LYS LYS A . n 
A 1 387 GLN 387 402 ?   ?   ?   A . n 
A 1 388 SER 388 403 ?   ?   ?   A . n 
A 1 389 ARG 389 404 ?   ?   ?   A . n 
A 1 390 ASN 390 405 ?   ?   ?   A . n 
A 1 391 MET 391 406 ?   ?   ?   A . n 
A 1 392 ASN 392 407 ?   ?   ?   A . n 
A 1 393 LEU 393 408 ?   ?   ?   A . n 
A 1 394 TYR 394 409 ?   ?   ?   A . n 
A 1 395 SER 395 410 ?   ?   ?   A . n 
A 1 396 VAL 396 411 ?   ?   ?   A . n 
A 1 397 ASP 397 412 ?   ?   ?   A . n 
A 1 398 GLY 398 413 ?   ?   ?   A . n 
A 1 399 GLU 399 414 ?   ?   ?   A . n 
A 1 400 ARG 400 415 ?   ?   ?   A . n 
A 1 401 ILE 401 416 416 ILE ILE A . n 
A 1 402 VAL 402 417 417 VAL VAL A . n 
A 1 403 LEU 403 418 418 LEU LEU A . n 
A 1 404 PRO 404 419 419 PRO PRO A . n 
A 1 405 ARG 405 420 420 ARG ARG A . n 
A 1 406 ILE 406 421 421 ILE ILE A . n 
A 1 407 PHE 407 422 422 PHE PHE A . n 
A 1 408 ILE 408 423 423 ILE ILE A . n 
A 1 409 SER 409 424 424 SER SER A . n 
A 1 410 ASN 410 425 425 ASN ASN A . n 
A 1 411 ASP 411 426 426 ASP ASP A . n 
A 1 412 LYS 412 427 427 LYS LYS A . n 
A 1 413 GLU 413 428 428 GLU GLU A . n 
A 1 414 SER 414 429 429 SER SER A . n 
A 1 415 ILE 415 430 430 ILE ILE A . n 
A 1 416 LYS 416 431 431 LYS LYS A . n 
A 1 417 CYS 417 432 432 CYS CYS A . n 
A 1 418 PRO 418 433 433 PRO PRO A . n 
A 1 419 CYS 419 434 434 CYS CYS A . n 
A 1 420 GLU 420 435 435 GLU GLU A . n 
A 1 421 PRO 421 436 436 PRO PRO A . n 
A 1 422 GLU 422 437 437 GLU GLU A . n 
A 1 423 HIS 423 438 438 HIS HIS A . n 
A 1 424 ILE 424 439 439 ILE ILE A . n 
A 1 425 SER 425 440 440 SER SER A . n 
A 1 426 GLN 426 441 441 GLN GLN A . n 
A 1 427 SER 427 442 442 SER SER A . n 
A 1 428 THR 428 443 443 THR THR A . n 
A 1 429 CYS 429 444 444 CYS CYS A . n 
A 1 430 ASN 430 445 445 ASN ASN A . n 
A 1 431 PHE 431 446 446 PHE PHE A . n 
A 1 432 TYR 432 447 447 TYR TYR A . n 
A 1 433 VAL 433 448 448 VAL VAL A . n 
A 1 434 CYS 434 449 449 CYS CYS A . n 
A 1 435 ASN 435 450 450 ASN ASN A . n 
A 1 436 CYS 436 451 451 CYS CYS A . n 
A 1 437 VAL 437 452 452 VAL VAL A . n 
A 1 438 GLU 438 453 453 GLU GLU A . n 
A 1 439 LYS 439 454 454 LYS LYS A . n 
A 1 440 ARG 440 455 455 ARG ARG A . n 
A 1 441 ALA 441 456 456 ALA ALA A . n 
A 1 442 GLU 442 457 457 GLU GLU A . n 
A 1 443 ILE 443 458 458 ILE ILE A . n 
A 1 444 LYS 444 459 459 LYS LYS A . n 
A 1 445 GLU 445 460 460 GLU GLU A . n 
A 1 446 ASN 446 461 461 ASN ASN A . n 
A 1 447 ASN 447 462 462 ASN ASN A . n 
A 1 448 GLN 448 463 463 GLN GLN A . n 
A 1 449 VAL 449 464 464 VAL VAL A . n 
A 1 450 VAL 450 465 465 VAL VAL A . n 
A 1 451 ILE 451 466 466 ILE ILE A . n 
A 1 452 LYS 452 467 467 LYS LYS A . n 
A 1 453 GLU 453 468 468 GLU GLU A . n 
A 1 454 GLU 454 469 469 GLU GLU A . n 
A 1 455 PHE 455 470 470 PHE PHE A . n 
A 1 456 ARG 456 471 471 ARG ARG A . n 
A 1 457 ASP 457 472 472 ASP ASP A . n 
A 1 458 TYR 458 473 473 TYR TYR A . n 
A 1 459 TYR 459 474 474 TYR TYR A . n 
A 1 460 GLU 460 475 ?   ?   ?   A . n 
A 1 461 ASN 461 476 ?   ?   ?   A . n 
A 1 462 GLY 462 477 ?   ?   ?   A . n 
A 1 463 GLU 463 478 ?   ?   ?   A . n 
A 1 464 GLU 464 479 ?   ?   ?   A . n 
A 1 465 LYS 465 480 ?   ?   ?   A . n 
A 1 466 SER 466 481 ?   ?   ?   A . n 
A 1 467 ASN 467 482 ?   ?   ?   A . n 
A 1 468 LYS 468 483 ?   ?   ?   A . n 
A 1 469 GLN 469 484 ?   ?   ?   A . n 
A 1 470 GLY 470 485 ?   ?   ?   A . n 
A 1 471 SER 471 486 ?   ?   ?   A . n 
B 2 1   GLN 1   1   1   GLN GLN B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PRO 9   9   9   PRO PRO B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  LYS 13  13  13  LYS LYS B . n 
B 2 14  PRO 14  14  14  PRO PRO B . n 
B 2 15  SER 15  15  15  SER SER B . n 
B 2 16  GLU 16  16  16  GLU GLU B . n 
B 2 17  THR 17  17  17  THR THR B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  SER 19  19  19  SER SER B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  THR 21  21  21  THR THR B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  THR 23  23  23  THR THR B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  GLY 27  27  27  GLY GLY B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  VAL 29  29  29  VAL VAL B . n 
B 2 30  SER 30  30  30  SER SER B . n 
B 2 31  SER 31  31  31  SER SER B . n 
B 2 32  PRO 32  32  32  PRO PRO B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  TYR 35  35  35  TYR TYR B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  SER 37  37  37  SER SER B . n 
B 2 38  TRP 38  38  38  TRP TRP B . n 
B 2 39  ILE 39  39  39  ILE ILE B . n 
B 2 40  ARG 40  40  40  ARG ARG B . n 
B 2 41  GLN 41  41  41  GLN GLN B . n 
B 2 42  PRO 42  42  42  PRO PRO B . n 
B 2 43  PRO 43  43  43  PRO PRO B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  GLN 45  45  45  GLN GLN B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  LEU 47  47  47  LEU LEU B . n 
B 2 48  GLU 48  48  48  GLU GLU B . n 
B 2 49  TRP 49  49  49  TRP TRP B . n 
B 2 50  ILE 50  50  50  ILE ILE B . n 
B 2 51  GLY 51  51  51  GLY GLY B . n 
B 2 52  ASP 52  52  52  ASP ASP B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  TYR 55  55  55  TYR TYR B . n 
B 2 56  ARG 56  56  56  ARG ARG B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  SER 58  58  58  SER SER B . n 
B 2 59  SER 59  59  59  SER SER B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  GLN 61  61  61  GLN GLN B . n 
B 2 62  ASN 62  62  62  ASN ASN B . n 
B 2 63  PRO 63  63  63  PRO PRO B . n 
B 2 64  SER 64  64  64  SER SER B . n 
B 2 65  LEU 65  65  65  LEU LEU B . n 
B 2 66  LYS 66  66  66  LYS LYS B . n 
B 2 67  SER 67  67  67  SER SER B . n 
B 2 68  ARG 68  68  68  ARG ARG B . n 
B 2 69  VAL 69  69  69  VAL VAL B . n 
B 2 70  THR 70  70  70  THR THR B . n 
B 2 71  THR 71  71  71  THR THR B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  VAL 73  73  73  VAL VAL B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  THR 75  75  75  THR THR B . n 
B 2 76  ALA 76  76  76  ALA ALA B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  ASN 78  78  78  ASN ASN B . n 
B 2 79  GLN 79  79  79  GLN GLN B . n 
B 2 80  PHE 80  80  80  PHE PHE B . n 
B 2 81  SER 81  81  81  SER SER B . n 
B 2 82  LEU 82  82  82  LEU LEU B . n 
B 2 83  ARG 83  83  83  ARG ARG B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  SER 85  85  85  SER SER B . n 
B 2 86  SER 86  86  86  SER SER B . n 
B 2 87  VAL 87  87  87  VAL VAL B . n 
B 2 88  THR 88  88  88  THR THR B . n 
B 2 89  ALA 89  89  89  ALA ALA B . n 
B 2 90  ALA 90  90  90  ALA ALA B . n 
B 2 91  ASP 91  91  91  ASP ASP B . n 
B 2 92  THR 92  92  92  THR THR B . n 
B 2 93  ALA 93  93  93  ALA ALA B . n 
B 2 94  VAL 94  94  94  VAL VAL B . n 
B 2 95  TYR 95  95  95  TYR TYR B . n 
B 2 96  PHE 96  96  96  PHE PHE B . n 
B 2 97  CYS 97  97  97  CYS CYS B . n 
B 2 98  ALA 98  98  98  ALA ALA B . n 
B 2 99  ARG 99  99  99  ARG ARG B . n 
B 2 100 SER 100 100 100 SER SER B . n 
B 2 101 ARG 101 101 101 ARG ARG B . n 
B 2 102 GLY 102 102 102 GLY GLY B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 CYS 106 106 106 CYS CYS B . n 
B 2 107 SER 107 107 107 SER SER B . n 
B 2 108 PHE 108 108 108 PHE PHE B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 THR 110 110 110 THR THR B . n 
B 2 111 CYS 111 111 111 CYS CYS B . n 
B 2 112 TYR 112 112 112 TYR TYR B . n 
B 2 113 THR 113 113 113 THR THR B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 PHE 115 115 115 PHE PHE B . n 
B 2 116 TYR 116 116 116 TYR TYR B . n 
B 2 117 TYR 117 117 117 TYR TYR B . n 
B 2 118 PHE 118 118 118 PHE PHE B . n 
B 2 119 ASP 119 119 119 ASP ASP B . n 
B 2 120 TYR 120 120 120 TYR TYR B . n 
B 2 121 TRP 121 121 121 TRP TRP B . n 
B 2 122 GLY 122 122 122 GLY GLY B . n 
B 2 123 GLN 123 123 123 GLN GLN B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 THR 125 125 125 THR THR B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 THR 128 128 128 THR THR B . n 
B 2 129 VAL 129 129 129 VAL VAL B . n 
B 2 130 SER 130 130 130 SER SER B . n 
B 2 131 SER 131 131 131 SER SER B . n 
B 2 132 ALA 132 132 132 ALA ALA B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 THR 134 134 134 THR THR B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 PRO 137 137 137 PRO PRO B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 VAL 139 139 139 VAL VAL B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 PRO 141 141 141 PRO PRO B . n 
B 2 142 LEU 142 142 142 LEU LEU B . n 
B 2 143 ALA 143 143 143 ALA ALA B . n 
B 2 144 PRO 144 144 144 PRO PRO B . n 
B 2 145 SER 145 145 145 SER SER B . n 
B 2 146 SER 146 146 146 SER SER B . n 
B 2 147 LYS 147 147 147 LYS LYS B . n 
B 2 148 SER 148 148 148 SER SER B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 SER 150 150 150 SER SER B . n 
B 2 151 GLY 151 151 151 GLY GLY B . n 
B 2 152 GLY 152 152 152 GLY GLY B . n 
B 2 153 THR 153 153 153 THR THR B . n 
B 2 154 ALA 154 154 154 ALA ALA B . n 
B 2 155 ALA 155 155 155 ALA ALA B . n 
B 2 156 LEU 156 156 156 LEU LEU B . n 
B 2 157 GLY 157 157 157 GLY GLY B . n 
B 2 158 CYS 158 158 158 CYS CYS B . n 
B 2 159 LEU 159 159 159 LEU LEU B . n 
B 2 160 VAL 160 160 160 VAL VAL B . n 
B 2 161 LYS 161 161 161 LYS LYS B . n 
B 2 162 ASP 162 162 162 ASP ASP B . n 
B 2 163 TYR 163 163 163 TYR TYR B . n 
B 2 164 PHE 164 164 164 PHE PHE B . n 
B 2 165 PRO 165 165 165 PRO PRO B . n 
B 2 166 GLU 166 166 166 GLU GLU B . n 
B 2 167 PRO 167 167 167 PRO PRO B . n 
B 2 168 VAL 168 168 168 VAL VAL B . n 
B 2 169 THR 169 169 169 THR THR B . n 
B 2 170 VAL 170 170 170 VAL VAL B . n 
B 2 171 SER 171 171 171 SER SER B . n 
B 2 172 TRP 172 172 172 TRP TRP B . n 
B 2 173 ASN 173 173 173 ASN ASN B . n 
B 2 174 SER 174 174 174 SER SER B . n 
B 2 175 GLY 175 175 175 GLY GLY B . n 
B 2 176 ALA 176 176 176 ALA ALA B . n 
B 2 177 LEU 177 177 177 LEU LEU B . n 
B 2 178 THR 178 178 178 THR THR B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 GLY 180 180 180 GLY GLY B . n 
B 2 181 VAL 181 181 181 VAL VAL B . n 
B 2 182 HIS 182 182 182 HIS HIS B . n 
B 2 183 THR 183 183 183 THR THR B . n 
B 2 184 PHE 184 184 184 PHE PHE B . n 
B 2 185 PRO 185 185 185 PRO PRO B . n 
B 2 186 ALA 186 186 186 ALA ALA B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 GLN 189 189 189 GLN GLN B . n 
B 2 190 SER 190 190 190 SER SER B . n 
B 2 191 SER 191 191 191 SER SER B . n 
B 2 192 GLY 192 192 192 GLY GLY B . n 
B 2 193 LEU 193 193 193 LEU LEU B . n 
B 2 194 TYR 194 194 194 TYR TYR B . n 
B 2 195 SER 195 195 195 SER SER B . n 
B 2 196 LEU 196 196 196 LEU LEU B . n 
B 2 197 SER 197 197 197 SER SER B . n 
B 2 198 SER 198 198 198 SER SER B . n 
B 2 199 VAL 199 199 199 VAL VAL B . n 
B 2 200 VAL 200 200 200 VAL VAL B . n 
B 2 201 THR 201 201 201 THR THR B . n 
B 2 202 VAL 202 202 202 VAL VAL B . n 
B 2 203 PRO 203 203 203 PRO PRO B . n 
B 2 204 SER 204 204 204 SER SER B . n 
B 2 205 SER 205 205 205 SER SER B . n 
B 2 206 SER 206 206 206 SER SER B . n 
B 2 207 LEU 207 207 207 LEU LEU B . n 
B 2 208 GLY 208 208 208 GLY GLY B . n 
B 2 209 THR 209 209 209 THR THR B . n 
B 2 210 GLN 210 210 210 GLN GLN B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 TYR 212 212 212 TYR TYR B . n 
B 2 213 ILE 213 213 213 ILE ILE B . n 
B 2 214 CYS 214 214 214 CYS CYS B . n 
B 2 215 ASN 215 215 215 ASN ASN B . n 
B 2 216 VAL 216 216 216 VAL VAL B . n 
B 2 217 ASN 217 217 217 ASN ASN B . n 
B 2 218 HIS 218 218 218 HIS HIS B . n 
B 2 219 LYS 219 219 219 LYS LYS B . n 
B 2 220 PRO 220 220 220 PRO PRO B . n 
B 2 221 SER 221 221 221 SER SER B . n 
B 2 222 ASN 222 222 222 ASN ASN B . n 
B 2 223 THR 223 223 223 THR THR B . n 
B 2 224 LYS 224 224 224 LYS LYS B . n 
B 2 225 VAL 225 225 225 VAL VAL B . n 
B 2 226 ASP 226 226 226 ASP ASP B . n 
B 2 227 LYS 227 227 227 LYS LYS B . n 
B 2 228 ARG 228 228 228 ARG ARG B . n 
B 2 229 VAL 229 229 229 VAL VAL B . n 
B 2 230 GLU 230 230 230 GLU GLU B . n 
B 2 231 PRO 231 231 231 PRO PRO B . n 
B 2 232 LYS 232 232 ?   ?   ?   B . n 
B 2 233 SER 233 233 ?   ?   ?   B . n 
B 2 234 CYS 234 234 ?   ?   ?   B . n 
C 3 1   GLU 1   1   1   GLU GLU C . n 
C 3 2   ILE 2   2   2   ILE ILE C . n 
C 3 3   VAL 3   3   3   VAL VAL C . n 
C 3 4   MET 4   4   4   MET MET C . n 
C 3 5   THR 5   5   5   THR THR C . n 
C 3 6   GLN 6   6   6   GLN GLN C . n 
C 3 7   SER 7   7   7   SER SER C . n 
C 3 8   PRO 8   8   8   PRO PRO C . n 
C 3 9   ALA 9   9   9   ALA ALA C . n 
C 3 10  THR 10  10  10  THR THR C . n 
C 3 11  LEU 11  11  11  LEU LEU C . n 
C 3 12  SER 12  12  12  SER SER C . n 
C 3 13  LEU 13  13  13  LEU LEU C . n 
C 3 14  SER 14  14  14  SER SER C . n 
C 3 15  PRO 15  15  15  PRO PRO C . n 
C 3 16  GLY 16  16  16  GLY GLY C . n 
C 3 17  GLU 17  17  17  GLU GLU C . n 
C 3 18  ARG 18  18  18  ARG ARG C . n 
C 3 19  ALA 19  19  19  ALA ALA C . n 
C 3 20  THR 20  20  20  THR THR C . n 
C 3 21  LEU 21  21  21  LEU LEU C . n 
C 3 22  SER 22  22  22  SER SER C . n 
C 3 23  CYS 23  23  23  CYS CYS C . n 
C 3 24  ARG 24  24  24  ARG ARG C . n 
C 3 25  ALA 25  25  25  ALA ALA C . n 
C 3 26  SER 26  26  26  SER SER C . n 
C 3 27  GLN 27  27  27  GLN GLN C . n 
C 3 28  SER 28  28  28  SER SER C . n 
C 3 29  ILE 29  29  29  ILE ILE C . n 
C 3 30  SER 30  30  30  SER SER C . n 
C 3 31  LYS 31  31  31  LYS LYS C . n 
C 3 32  THR 32  32  32  THR THR C . n 
C 3 33  LEU 33  33  33  LEU LEU C . n 
C 3 34  ALA 34  34  34  ALA ALA C . n 
C 3 35  TRP 35  35  35  TRP TRP C . n 
C 3 36  TYR 36  36  36  TYR TYR C . n 
C 3 37  GLN 37  37  37  GLN GLN C . n 
C 3 38  GLN 38  38  38  GLN GLN C . n 
C 3 39  LYS 39  39  39  LYS LYS C . n 
C 3 40  PRO 40  40  40  PRO PRO C . n 
C 3 41  GLY 41  41  41  GLY GLY C . n 
C 3 42  GLN 42  42  42  GLN GLN C . n 
C 3 43  ALA 43  43  43  ALA ALA C . n 
C 3 44  PRO 44  44  44  PRO PRO C . n 
C 3 45  ARG 45  45  45  ARG ARG C . n 
C 3 46  LEU 46  46  46  LEU LEU C . n 
C 3 47  LEU 47  47  47  LEU LEU C . n 
C 3 48  ILE 48  48  48  ILE ILE C . n 
C 3 49  TYR 49  49  49  TYR TYR C . n 
C 3 50  SER 50  50  50  SER SER C . n 
C 3 51  ALA 51  51  51  ALA ALA C . n 
C 3 52  SER 52  52  52  SER SER C . n 
C 3 53  THR 53  53  53  THR THR C . n 
C 3 54  ARG 54  54  54  ARG ARG C . n 
C 3 55  ALA 55  55  55  ALA ALA C . n 
C 3 56  SER 56  56  56  SER SER C . n 
C 3 57  GLY 57  57  57  GLY GLY C . n 
C 3 58  VAL 58  58  58  VAL VAL C . n 
C 3 59  PRO 59  59  59  PRO PRO C . n 
C 3 60  ALA 60  60  60  ALA ALA C . n 
C 3 61  ARG 61  61  61  ARG ARG C . n 
C 3 62  PHE 62  62  62  PHE PHE C . n 
C 3 63  SER 63  63  63  SER SER C . n 
C 3 64  GLY 64  64  64  GLY GLY C . n 
C 3 65  SER 65  65  65  SER SER C . n 
C 3 66  GLY 66  66  66  GLY GLY C . n 
C 3 67  SER 67  67  67  SER SER C . n 
C 3 68  GLY 68  68  68  GLY GLY C . n 
C 3 69  THR 69  69  69  THR THR C . n 
C 3 70  GLU 70  70  70  GLU GLU C . n 
C 3 71  PHE 71  71  71  PHE PHE C . n 
C 3 72  SER 72  72  72  SER SER C . n 
C 3 73  LEU 73  73  73  LEU LEU C . n 
C 3 74  THR 74  74  74  THR THR C . n 
C 3 75  ILE 75  75  75  ILE ILE C . n 
C 3 76  SER 76  76  76  SER SER C . n 
C 3 77  SER 77  77  77  SER SER C . n 
C 3 78  LEU 78  78  78  LEU LEU C . n 
C 3 79  GLN 79  79  79  GLN GLN C . n 
C 3 80  SER 80  80  80  SER SER C . n 
C 3 81  GLU 81  81  81  GLU GLU C . n 
C 3 82  ASP 82  82  82  ASP ASP C . n 
C 3 83  PHE 83  83  83  PHE PHE C . n 
C 3 84  ALA 84  84  84  ALA ALA C . n 
C 3 85  VAL 85  85  85  VAL VAL C . n 
C 3 86  TYR 86  86  86  TYR TYR C . n 
C 3 87  TYR 87  87  87  TYR TYR C . n 
C 3 88  CYS 88  88  88  CYS CYS C . n 
C 3 89  GLN 89  89  89  GLN GLN C . n 
C 3 90  GLN 90  90  90  GLN GLN C . n 
C 3 91  TYR 91  91  91  TYR TYR C . n 
C 3 92  ASN 92  92  92  ASN ASN C . n 
C 3 93  GLU 93  93  93  GLU GLU C . n 
C 3 94  TRP 94  94  94  TRP TRP C . n 
C 3 95  PRO 95  95  95  PRO PRO C . n 
C 3 96  PRO 96  96  96  PRO PRO C . n 
C 3 97  ARG 97  97  97  ARG ARG C . n 
C 3 98  PRO 98  98  98  PRO PRO C . n 
C 3 99  THR 99  99  99  THR THR C . n 
C 3 100 PHE 100 100 100 PHE PHE C . n 
C 3 101 GLY 101 101 101 GLY GLY C . n 
C 3 102 GLY 102 102 102 GLY GLY C . n 
C 3 103 GLY 103 103 103 GLY GLY C . n 
C 3 104 THR 104 104 104 THR THR C . n 
C 3 105 LYS 105 105 105 LYS LYS C . n 
C 3 106 VAL 106 106 106 VAL VAL C . n 
C 3 107 GLU 107 107 107 GLU GLU C . n 
C 3 108 ILE 108 108 108 ILE ILE C . n 
C 3 109 LYS 109 109 109 LYS LYS C . n 
C 3 110 ARG 110 110 110 ARG ARG C . n 
C 3 111 THR 111 111 111 THR THR C . n 
C 3 112 VAL 112 112 112 VAL VAL C . n 
C 3 113 ALA 113 113 113 ALA ALA C . n 
C 3 114 ALA 114 114 114 ALA ALA C . n 
C 3 115 PRO 115 115 115 PRO PRO C . n 
C 3 116 SER 116 116 116 SER SER C . n 
C 3 117 VAL 117 117 117 VAL VAL C . n 
C 3 118 PHE 118 118 118 PHE PHE C . n 
C 3 119 ILE 119 119 119 ILE ILE C . n 
C 3 120 PHE 120 120 120 PHE PHE C . n 
C 3 121 PRO 121 121 121 PRO PRO C . n 
C 3 122 PRO 122 122 122 PRO PRO C . n 
C 3 123 SER 123 123 123 SER SER C . n 
C 3 124 ASP 124 124 124 ASP ASP C . n 
C 3 125 GLU 125 125 125 GLU GLU C . n 
C 3 126 GLN 126 126 126 GLN GLN C . n 
C 3 127 LEU 127 127 127 LEU LEU C . n 
C 3 128 LYS 128 128 128 LYS LYS C . n 
C 3 129 SER 129 129 129 SER SER C . n 
C 3 130 GLY 130 130 130 GLY GLY C . n 
C 3 131 THR 131 131 131 THR THR C . n 
C 3 132 ALA 132 132 132 ALA ALA C . n 
C 3 133 SER 133 133 133 SER SER C . n 
C 3 134 VAL 134 134 134 VAL VAL C . n 
C 3 135 VAL 135 135 135 VAL VAL C . n 
C 3 136 CYS 136 136 136 CYS CYS C . n 
C 3 137 LEU 137 137 137 LEU LEU C . n 
C 3 138 LEU 138 138 138 LEU LEU C . n 
C 3 139 ASN 139 139 139 ASN ASN C . n 
C 3 140 ASN 140 140 140 ASN ASN C . n 
C 3 141 PHE 141 141 141 PHE PHE C . n 
C 3 142 TYR 142 142 142 TYR TYR C . n 
C 3 143 PRO 143 143 143 PRO PRO C . n 
C 3 144 ARG 144 144 144 ARG ARG C . n 
C 3 145 GLU 145 145 145 GLU GLU C . n 
C 3 146 ALA 146 146 146 ALA ALA C . n 
C 3 147 LYS 147 147 147 LYS LYS C . n 
C 3 148 VAL 148 148 148 VAL VAL C . n 
C 3 149 GLN 149 149 149 GLN GLN C . n 
C 3 150 TRP 150 150 150 TRP TRP C . n 
C 3 151 LYS 151 151 151 LYS LYS C . n 
C 3 152 VAL 152 152 152 VAL VAL C . n 
C 3 153 ASP 153 153 153 ASP ASP C . n 
C 3 154 ASN 154 154 154 ASN ASN C . n 
C 3 155 ALA 155 155 155 ALA ALA C . n 
C 3 156 LEU 156 156 156 LEU LEU C . n 
C 3 157 GLN 157 157 157 GLN GLN C . n 
C 3 158 SER 158 158 158 SER SER C . n 
C 3 159 GLY 159 159 159 GLY GLY C . n 
C 3 160 ASN 160 160 160 ASN ASN C . n 
C 3 161 SER 161 161 161 SER SER C . n 
C 3 162 GLN 162 162 162 GLN GLN C . n 
C 3 163 GLU 163 163 163 GLU GLU C . n 
C 3 164 SER 164 164 164 SER SER C . n 
C 3 165 VAL 165 165 165 VAL VAL C . n 
C 3 166 THR 166 166 166 THR THR C . n 
C 3 167 GLU 167 167 167 GLU GLU C . n 
C 3 168 GLN 168 168 168 GLN GLN C . n 
C 3 169 ASP 169 169 169 ASP ASP C . n 
C 3 170 SER 170 170 170 SER SER C . n 
C 3 171 LYS 171 171 171 LYS LYS C . n 
C 3 172 ASP 172 172 172 ASP ASP C . n 
C 3 173 SER 173 173 173 SER SER C . n 
C 3 174 THR 174 174 174 THR THR C . n 
C 3 175 TYR 175 175 175 TYR TYR C . n 
C 3 176 SER 176 176 176 SER SER C . n 
C 3 177 LEU 177 177 177 LEU LEU C . n 
C 3 178 SER 178 178 178 SER SER C . n 
C 3 179 SER 179 179 179 SER SER C . n 
C 3 180 THR 180 180 180 THR THR C . n 
C 3 181 LEU 181 181 181 LEU LEU C . n 
C 3 182 THR 182 182 182 THR THR C . n 
C 3 183 LEU 183 183 183 LEU LEU C . n 
C 3 184 SER 184 184 184 SER SER C . n 
C 3 185 LYS 185 185 185 LYS LYS C . n 
C 3 186 ALA 186 186 186 ALA ALA C . n 
C 3 187 ASP 187 187 187 ASP ASP C . n 
C 3 188 TYR 188 188 188 TYR TYR C . n 
C 3 189 GLU 189 189 189 GLU GLU C . n 
C 3 190 LYS 190 190 190 LYS LYS C . n 
C 3 191 HIS 191 191 191 HIS HIS C . n 
C 3 192 LYS 192 192 192 LYS LYS C . n 
C 3 193 VAL 193 193 193 VAL VAL C . n 
C 3 194 TYR 194 194 194 TYR TYR C . n 
C 3 195 ALA 195 195 195 ALA ALA C . n 
C 3 196 CYS 196 196 196 CYS CYS C . n 
C 3 197 GLU 197 197 197 GLU GLU C . n 
C 3 198 VAL 198 198 198 VAL VAL C . n 
C 3 199 THR 199 199 199 THR THR C . n 
C 3 200 HIS 200 200 200 HIS HIS C . n 
C 3 201 GLN 201 201 201 GLN GLN C . n 
C 3 202 GLY 202 202 202 GLY GLY C . n 
C 3 203 LEU 203 203 203 LEU LEU C . n 
C 3 204 SER 204 204 204 SER SER C . n 
C 3 205 SER 205 205 205 SER SER C . n 
C 3 206 PRO 206 206 206 PRO PRO C . n 
C 3 207 VAL 207 207 207 VAL VAL C . n 
C 3 208 THR 208 208 208 THR THR C . n 
C 3 209 LYS 209 209 209 LYS LYS C . n 
C 3 210 SER 210 210 210 SER SER C . n 
C 3 211 PHE 211 211 211 PHE PHE C . n 
C 3 212 ASN 212 212 212 ASN ASN C . n 
C 3 213 ARG 213 213 213 ARG ARG C . n 
C 3 214 GLY 214 214 214 GLY GLY C . n 
C 3 215 GLU 215 215 ?   ?   ?   C . n 
C 3 216 CYS 216 216 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 HOH 1   501 232 HOH HOH A . 
D 4 HOH 2   502 15  HOH HOH A . 
D 4 HOH 3   503 174 HOH HOH A . 
D 4 HOH 4   504 26  HOH HOH A . 
D 4 HOH 5   505 70  HOH HOH A . 
D 4 HOH 6   506 110 HOH HOH A . 
D 4 HOH 7   507 149 HOH HOH A . 
D 4 HOH 8   508 32  HOH HOH A . 
D 4 HOH 9   509 49  HOH HOH A . 
D 4 HOH 10  510 119 HOH HOH A . 
D 4 HOH 11  511 9   HOH HOH A . 
D 4 HOH 12  512 73  HOH HOH A . 
D 4 HOH 13  513 179 HOH HOH A . 
D 4 HOH 14  514 124 HOH HOH A . 
D 4 HOH 15  515 82  HOH HOH A . 
D 4 HOH 16  516 41  HOH HOH A . 
D 4 HOH 17  517 66  HOH HOH A . 
D 4 HOH 18  518 108 HOH HOH A . 
D 4 HOH 19  519 227 HOH HOH A . 
D 4 HOH 20  520 39  HOH HOH A . 
D 4 HOH 21  521 187 HOH HOH A . 
D 4 HOH 22  522 72  HOH HOH A . 
D 4 HOH 23  523 157 HOH HOH A . 
D 4 HOH 24  524 11  HOH HOH A . 
D 4 HOH 25  525 29  HOH HOH A . 
D 4 HOH 26  526 23  HOH HOH A . 
D 4 HOH 27  527 181 HOH HOH A . 
D 4 HOH 28  528 189 HOH HOH A . 
D 4 HOH 29  529 80  HOH HOH A . 
D 4 HOH 30  530 55  HOH HOH A . 
D 4 HOH 31  531 3   HOH HOH A . 
D 4 HOH 32  532 107 HOH HOH A . 
D 4 HOH 33  533 69  HOH HOH A . 
D 4 HOH 34  534 17  HOH HOH A . 
D 4 HOH 35  535 97  HOH HOH A . 
D 4 HOH 36  536 77  HOH HOH A . 
D 4 HOH 37  537 21  HOH HOH A . 
D 4 HOH 38  538 123 HOH HOH A . 
D 4 HOH 39  539 7   HOH HOH A . 
D 4 HOH 40  540 24  HOH HOH A . 
D 4 HOH 41  541 155 HOH HOH A . 
D 4 HOH 42  542 139 HOH HOH A . 
D 4 HOH 43  543 87  HOH HOH A . 
D 4 HOH 44  544 22  HOH HOH A . 
D 4 HOH 45  545 228 HOH HOH A . 
D 4 HOH 46  546 84  HOH HOH A . 
D 4 HOH 47  547 30  HOH HOH A . 
D 4 HOH 48  548 183 HOH HOH A . 
D 4 HOH 49  549 6   HOH HOH A . 
D 4 HOH 50  550 132 HOH HOH A . 
D 4 HOH 51  551 37  HOH HOH A . 
D 4 HOH 52  552 81  HOH HOH A . 
D 4 HOH 53  553 231 HOH HOH A . 
D 4 HOH 54  554 16  HOH HOH A . 
D 4 HOH 55  555 241 HOH HOH A . 
D 4 HOH 56  556 198 HOH HOH A . 
D 4 HOH 57  557 140 HOH HOH A . 
D 4 HOH 58  558 35  HOH HOH A . 
D 4 HOH 59  559 75  HOH HOH A . 
D 4 HOH 60  560 191 HOH HOH A . 
D 4 HOH 61  561 13  HOH HOH A . 
D 4 HOH 62  562 216 HOH HOH A . 
D 4 HOH 63  563 103 HOH HOH A . 
D 4 HOH 64  564 133 HOH HOH A . 
D 4 HOH 65  565 146 HOH HOH A . 
D 4 HOH 66  566 51  HOH HOH A . 
D 4 HOH 67  567 236 HOH HOH A . 
D 4 HOH 68  568 78  HOH HOH A . 
D 4 HOH 69  569 52  HOH HOH A . 
D 4 HOH 70  570 61  HOH HOH A . 
D 4 HOH 71  571 89  HOH HOH A . 
D 4 HOH 72  572 42  HOH HOH A . 
D 4 HOH 73  573 19  HOH HOH A . 
D 4 HOH 74  574 36  HOH HOH A . 
D 4 HOH 75  575 95  HOH HOH A . 
D 4 HOH 76  576 63  HOH HOH A . 
D 4 HOH 77  577 152 HOH HOH A . 
D 4 HOH 78  578 34  HOH HOH A . 
D 4 HOH 79  579 224 HOH HOH A . 
D 4 HOH 80  580 85  HOH HOH A . 
D 4 HOH 81  581 120 HOH HOH A . 
D 4 HOH 82  582 56  HOH HOH A . 
D 4 HOH 83  583 226 HOH HOH A . 
D 4 HOH 84  584 194 HOH HOH A . 
D 4 HOH 85  585 234 HOH HOH A . 
D 4 HOH 86  586 127 HOH HOH A . 
D 4 HOH 87  587 96  HOH HOH A . 
D 4 HOH 88  588 151 HOH HOH A . 
D 4 HOH 89  589 197 HOH HOH A . 
D 4 HOH 90  590 58  HOH HOH A . 
D 4 HOH 91  591 158 HOH HOH A . 
D 4 HOH 92  592 53  HOH HOH A . 
D 4 HOH 93  593 106 HOH HOH A . 
D 4 HOH 94  594 240 HOH HOH A . 
D 4 HOH 95  595 182 HOH HOH A . 
D 4 HOH 96  596 160 HOH HOH A . 
D 4 HOH 97  597 222 HOH HOH A . 
D 4 HOH 98  598 104 HOH HOH A . 
D 4 HOH 99  599 65  HOH HOH A . 
D 4 HOH 100 600 134 HOH HOH A . 
D 4 HOH 101 601 200 HOH HOH A . 
D 4 HOH 102 602 71  HOH HOH A . 
D 4 HOH 103 603 184 HOH HOH A . 
D 4 HOH 104 604 233 HOH HOH A . 
D 4 HOH 105 605 212 HOH HOH A . 
D 4 HOH 106 606 239 HOH HOH A . 
D 4 HOH 107 607 130 HOH HOH A . 
D 4 HOH 108 608 195 HOH HOH A . 
D 4 HOH 109 609 112 HOH HOH A . 
D 4 HOH 110 610 223 HOH HOH A . 
D 4 HOH 111 611 116 HOH HOH A . 
D 4 HOH 112 612 117 HOH HOH A . 
D 4 HOH 113 613 211 HOH HOH A . 
D 4 HOH 114 614 230 HOH HOH A . 
D 4 HOH 115 615 50  HOH HOH A . 
D 4 HOH 116 616 64  HOH HOH A . 
D 4 HOH 117 617 225 HOH HOH A . 
D 4 HOH 118 618 238 HOH HOH A . 
D 4 HOH 119 619 242 HOH HOH A . 
D 4 HOH 120 620 196 HOH HOH A . 
D 4 HOH 121 621 153 HOH HOH A . 
D 4 HOH 122 622 254 HOH HOH A . 
D 4 HOH 123 623 40  HOH HOH A . 
D 4 HOH 124 624 199 HOH HOH A . 
D 4 HOH 125 625 229 HOH HOH A . 
D 4 HOH 126 626 205 HOH HOH A . 
D 4 HOH 127 627 43  HOH HOH A . 
D 4 HOH 128 628 143 HOH HOH A . 
D 4 HOH 129 629 237 HOH HOH A . 
D 4 HOH 130 630 245 HOH HOH A . 
E 4 HOH 1   301 118 HOH HOH B . 
E 4 HOH 2   302 128 HOH HOH B . 
E 4 HOH 3   303 68  HOH HOH B . 
E 4 HOH 4   304 46  HOH HOH B . 
E 4 HOH 5   305 91  HOH HOH B . 
E 4 HOH 6   306 186 HOH HOH B . 
E 4 HOH 7   307 159 HOH HOH B . 
E 4 HOH 8   308 62  HOH HOH B . 
E 4 HOH 9   309 190 HOH HOH B . 
E 4 HOH 10  310 25  HOH HOH B . 
E 4 HOH 11  311 27  HOH HOH B . 
E 4 HOH 12  312 243 HOH HOH B . 
E 4 HOH 13  313 206 HOH HOH B . 
E 4 HOH 14  314 92  HOH HOH B . 
E 4 HOH 15  315 215 HOH HOH B . 
E 4 HOH 16  316 59  HOH HOH B . 
E 4 HOH 17  317 18  HOH HOH B . 
E 4 HOH 18  318 169 HOH HOH B . 
E 4 HOH 19  319 145 HOH HOH B . 
E 4 HOH 20  320 121 HOH HOH B . 
E 4 HOH 21  321 14  HOH HOH B . 
E 4 HOH 22  322 47  HOH HOH B . 
E 4 HOH 23  323 20  HOH HOH B . 
E 4 HOH 24  324 109 HOH HOH B . 
E 4 HOH 25  325 10  HOH HOH B . 
E 4 HOH 26  326 12  HOH HOH B . 
E 4 HOH 27  327 144 HOH HOH B . 
E 4 HOH 28  328 246 HOH HOH B . 
E 4 HOH 29  329 122 HOH HOH B . 
E 4 HOH 30  330 86  HOH HOH B . 
E 4 HOH 31  331 94  HOH HOH B . 
E 4 HOH 32  332 126 HOH HOH B . 
E 4 HOH 33  333 67  HOH HOH B . 
E 4 HOH 34  334 204 HOH HOH B . 
E 4 HOH 35  335 57  HOH HOH B . 
E 4 HOH 36  336 114 HOH HOH B . 
E 4 HOH 37  337 154 HOH HOH B . 
E 4 HOH 38  338 164 HOH HOH B . 
E 4 HOH 39  339 251 HOH HOH B . 
E 4 HOH 40  340 88  HOH HOH B . 
E 4 HOH 41  341 203 HOH HOH B . 
E 4 HOH 42  342 249 HOH HOH B . 
E 4 HOH 43  343 163 HOH HOH B . 
E 4 HOH 44  344 185 HOH HOH B . 
E 4 HOH 45  345 235 HOH HOH B . 
E 4 HOH 46  346 137 HOH HOH B . 
E 4 HOH 47  347 177 HOH HOH B . 
E 4 HOH 48  348 220 HOH HOH B . 
E 4 HOH 49  349 99  HOH HOH B . 
E 4 HOH 50  350 175 HOH HOH B . 
E 4 HOH 51  351 247 HOH HOH B . 
E 4 HOH 52  352 31  HOH HOH B . 
E 4 HOH 53  353 176 HOH HOH B . 
E 4 HOH 54  354 250 HOH HOH B . 
E 4 HOH 55  355 244 HOH HOH B . 
E 4 HOH 56  356 210 HOH HOH B . 
E 4 HOH 57  357 213 HOH HOH B . 
E 4 HOH 58  358 165 HOH HOH B . 
E 4 HOH 59  359 248 HOH HOH B . 
E 4 HOH 60  360 150 HOH HOH B . 
F 4 HOH 1   301 83  HOH HOH C . 
F 4 HOH 2   302 172 HOH HOH C . 
F 4 HOH 3   303 125 HOH HOH C . 
F 4 HOH 4   304 138 HOH HOH C . 
F 4 HOH 5   305 129 HOH HOH C . 
F 4 HOH 6   306 48  HOH HOH C . 
F 4 HOH 7   307 1   HOH HOH C . 
F 4 HOH 8   308 111 HOH HOH C . 
F 4 HOH 9   309 171 HOH HOH C . 
F 4 HOH 10  310 170 HOH HOH C . 
F 4 HOH 11  311 60  HOH HOH C . 
F 4 HOH 12  312 2   HOH HOH C . 
F 4 HOH 13  313 28  HOH HOH C . 
F 4 HOH 14  314 4   HOH HOH C . 
F 4 HOH 15  315 253 HOH HOH C . 
F 4 HOH 16  316 93  HOH HOH C . 
F 4 HOH 17  317 79  HOH HOH C . 
F 4 HOH 18  318 44  HOH HOH C . 
F 4 HOH 19  319 259 HOH HOH C . 
F 4 HOH 20  320 135 HOH HOH C . 
F 4 HOH 21  321 105 HOH HOH C . 
F 4 HOH 22  322 90  HOH HOH C . 
F 4 HOH 23  323 192 HOH HOH C . 
F 4 HOH 24  324 218 HOH HOH C . 
F 4 HOH 25  325 131 HOH HOH C . 
F 4 HOH 26  326 201 HOH HOH C . 
F 4 HOH 27  327 166 HOH HOH C . 
F 4 HOH 28  328 76  HOH HOH C . 
F 4 HOH 29  329 258 HOH HOH C . 
F 4 HOH 30  330 167 HOH HOH C . 
F 4 HOH 31  331 161 HOH HOH C . 
F 4 HOH 32  332 113 HOH HOH C . 
F 4 HOH 33  333 156 HOH HOH C . 
F 4 HOH 34  334 188 HOH HOH C . 
F 4 HOH 35  335 101 HOH HOH C . 
F 4 HOH 36  336 102 HOH HOH C . 
F 4 HOH 37  337 8   HOH HOH C . 
F 4 HOH 38  338 98  HOH HOH C . 
F 4 HOH 39  339 74  HOH HOH C . 
F 4 HOH 40  340 45  HOH HOH C . 
F 4 HOH 41  341 33  HOH HOH C . 
F 4 HOH 42  342 5   HOH HOH C . 
F 4 HOH 43  343 217 HOH HOH C . 
F 4 HOH 44  344 136 HOH HOH C . 
F 4 HOH 45  345 115 HOH HOH C . 
F 4 HOH 46  346 214 HOH HOH C . 
F 4 HOH 47  347 193 HOH HOH C . 
F 4 HOH 48  348 142 HOH HOH C . 
F 4 HOH 49  349 141 HOH HOH C . 
F 4 HOH 50  350 257 HOH HOH C . 
F 4 HOH 51  351 38  HOH HOH C . 
F 4 HOH 52  352 100 HOH HOH C . 
F 4 HOH 53  353 208 HOH HOH C . 
F 4 HOH 54  354 148 HOH HOH C . 
F 4 HOH 55  355 162 HOH HOH C . 
F 4 HOH 56  356 219 HOH HOH C . 
F 4 HOH 57  357 256 HOH HOH C . 
F 4 HOH 58  358 178 HOH HOH C . 
F 4 HOH 59  359 54  HOH HOH C . 
F 4 HOH 60  360 202 HOH HOH C . 
F 4 HOH 61  361 255 HOH HOH C . 
F 4 HOH 62  362 209 HOH HOH C . 
F 4 HOH 63  363 180 HOH HOH C . 
F 4 HOH 64  364 147 HOH HOH C . 
F 4 HOH 65  365 207 HOH HOH C . 
F 4 HOH 66  366 221 HOH HOH C . 
F 4 HOH 67  367 173 HOH HOH C . 
F 4 HOH 68  368 252 HOH HOH C . 
F 4 HOH 69  369 168 HOH HOH C . 
# 
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 46  ? CG  ? A GLU 31  CG  
2   1 Y 1 A GLU 46  ? CD  ? A GLU 31  CD  
3   1 Y 1 A GLU 46  ? OE1 ? A GLU 31  OE1 
4   1 Y 1 A GLU 46  ? OE2 ? A GLU 31  OE2 
5   1 Y 1 A ARG 50  ? CG  ? A ARG 35  CG  
6   1 Y 1 A ARG 50  ? CD  ? A ARG 35  CD  
7   1 Y 1 A ARG 50  ? NE  ? A ARG 35  NE  
8   1 Y 1 A ARG 50  ? CZ  ? A ARG 35  CZ  
9   1 Y 1 A ARG 50  ? NH1 ? A ARG 35  NH1 
10  1 Y 1 A ARG 50  ? NH2 ? A ARG 35  NH2 
11  1 Y 1 A LYS 56  ? CG  ? A LYS 41  CG  
12  1 Y 1 A LYS 56  ? CD  ? A LYS 41  CD  
13  1 Y 1 A LYS 56  ? CE  ? A LYS 41  CE  
14  1 Y 1 A LYS 56  ? NZ  ? A LYS 41  NZ  
15  1 Y 1 A LYS 86  ? CE  ? A LYS 71  CE  
16  1 Y 1 A LYS 86  ? NZ  ? A LYS 71  NZ  
17  1 Y 1 A LYS 112 ? CD  ? A LYS 97  CD  
18  1 Y 1 A LYS 112 ? CE  ? A LYS 97  CE  
19  1 Y 1 A LYS 112 ? NZ  ? A LYS 97  NZ  
20  1 Y 1 A LYS 148 ? CE  ? A LYS 133 CE  
21  1 Y 1 A LYS 148 ? NZ  ? A LYS 133 NZ  
22  1 Y 1 A ARG 206 ? CG  ? A ARG 191 CG  
23  1 Y 1 A ARG 206 ? CD  ? A ARG 191 CD  
24  1 Y 1 A ARG 206 ? NE  ? A ARG 191 NE  
25  1 Y 1 A ARG 206 ? CZ  ? A ARG 191 CZ  
26  1 Y 1 A ARG 206 ? NH1 ? A ARG 191 NH1 
27  1 Y 1 A ARG 206 ? NH2 ? A ARG 191 NH2 
28  1 Y 1 A LYS 245 ? CE  ? A LYS 230 CE  
29  1 Y 1 A LYS 245 ? NZ  ? A LYS 230 NZ  
30  1 Y 1 A TYR 270 ? CG  ? A TYR 255 CG  
31  1 Y 1 A TYR 270 ? CD1 ? A TYR 255 CD1 
32  1 Y 1 A TYR 270 ? CD2 ? A TYR 255 CD2 
33  1 Y 1 A TYR 270 ? CE1 ? A TYR 255 CE1 
34  1 Y 1 A TYR 270 ? CE2 ? A TYR 255 CE2 
35  1 Y 1 A TYR 270 ? CZ  ? A TYR 255 CZ  
36  1 Y 1 A TYR 270 ? OH  ? A TYR 255 OH  
37  1 Y 1 A GLN 306 ? CG  ? A GLN 291 CG  
38  1 Y 1 A GLN 306 ? CD  ? A GLN 291 CD  
39  1 Y 1 A GLN 306 ? OE1 ? A GLN 291 OE1 
40  1 Y 1 A GLN 306 ? NE2 ? A GLN 291 NE2 
41  1 Y 1 A LYS 307 ? CG  ? A LYS 292 CG  
42  1 Y 1 A LYS 307 ? CD  ? A LYS 292 CD  
43  1 Y 1 A LYS 307 ? CE  ? A LYS 292 CE  
44  1 Y 1 A LYS 307 ? NZ  ? A LYS 292 NZ  
45  1 Y 1 A VAL 327 ? CG1 ? A VAL 312 CG1 
46  1 Y 1 A VAL 327 ? CG2 ? A VAL 312 CG2 
47  1 Y 1 A LYS 338 ? CE  ? A LYS 323 CE  
48  1 Y 1 A LYS 338 ? NZ  ? A LYS 323 NZ  
49  1 Y 1 A LYS 392 ? CD  ? A LYS 377 CD  
50  1 Y 1 A LYS 392 ? CE  ? A LYS 377 CE  
51  1 Y 1 A LYS 392 ? NZ  ? A LYS 377 NZ  
52  1 Y 1 A GLU 396 ? CD  ? A GLU 381 CD  
53  1 Y 1 A GLU 396 ? OE1 ? A GLU 381 OE1 
54  1 Y 1 A GLU 396 ? OE2 ? A GLU 381 OE2 
55  1 Y 1 A ARG 397 ? CG  ? A ARG 382 CG  
56  1 Y 1 A ARG 397 ? CD  ? A ARG 382 CD  
57  1 Y 1 A ARG 397 ? NE  ? A ARG 382 NE  
58  1 Y 1 A ARG 397 ? CZ  ? A ARG 382 CZ  
59  1 Y 1 A ARG 397 ? NH1 ? A ARG 382 NH1 
60  1 Y 1 A ARG 397 ? NH2 ? A ARG 382 NH2 
61  1 Y 1 A ILE 399 ? CG1 ? A ILE 384 CG1 
62  1 Y 1 A ILE 399 ? CG2 ? A ILE 384 CG2 
63  1 Y 1 A ILE 399 ? CD1 ? A ILE 384 CD1 
64  1 Y 1 A LYS 400 ? CE  ? A LYS 385 CE  
65  1 Y 1 A LYS 400 ? NZ  ? A LYS 385 NZ  
66  1 Y 1 A LYS 401 ? CG  ? A LYS 386 CG  
67  1 Y 1 A LYS 401 ? CD  ? A LYS 386 CD  
68  1 Y 1 A LYS 401 ? CE  ? A LYS 386 CE  
69  1 Y 1 A LYS 401 ? NZ  ? A LYS 386 NZ  
70  1 Y 1 A ILE 416 ? CG1 ? A ILE 401 CG1 
71  1 Y 1 A ILE 416 ? CG2 ? A ILE 401 CG2 
72  1 Y 1 A ILE 416 ? CD1 ? A ILE 401 CD1 
73  1 Y 1 A GLU 428 ? CG  ? A GLU 413 CG  
74  1 Y 1 A GLU 428 ? CD  ? A GLU 413 CD  
75  1 Y 1 A GLU 428 ? OE1 ? A GLU 413 OE1 
76  1 Y 1 A GLU 428 ? OE2 ? A GLU 413 OE2 
77  1 Y 1 A LYS 431 ? CE  ? A LYS 416 CE  
78  1 Y 1 A LYS 431 ? NZ  ? A LYS 416 NZ  
79  1 Y 1 A GLU 435 ? CD  ? A GLU 420 CD  
80  1 Y 1 A GLU 435 ? OE1 ? A GLU 420 OE1 
81  1 Y 1 A GLU 435 ? OE2 ? A GLU 420 OE2 
82  1 Y 1 A GLU 437 ? CD  ? A GLU 422 CD  
83  1 Y 1 A GLU 437 ? OE1 ? A GLU 422 OE1 
84  1 Y 1 A GLU 437 ? OE2 ? A GLU 422 OE2 
85  1 Y 1 A GLU 457 ? CG  ? A GLU 442 CG  
86  1 Y 1 A GLU 457 ? CD  ? A GLU 442 CD  
87  1 Y 1 A GLU 457 ? OE1 ? A GLU 442 OE1 
88  1 Y 1 A GLU 457 ? OE2 ? A GLU 442 OE2 
89  1 Y 1 A LYS 459 ? CG  ? A LYS 444 CG  
90  1 Y 1 A LYS 459 ? CD  ? A LYS 444 CD  
91  1 Y 1 A LYS 459 ? CE  ? A LYS 444 CE  
92  1 Y 1 A LYS 459 ? NZ  ? A LYS 444 NZ  
93  1 Y 1 A ASN 461 ? CG  ? A ASN 446 CG  
94  1 Y 1 A ASN 461 ? OD1 ? A ASN 446 OD1 
95  1 Y 1 A ASN 461 ? ND2 ? A ASN 446 ND2 
96  1 Y 1 A GLU 468 ? CG  ? A GLU 453 CG  
97  1 Y 1 A GLU 468 ? CD  ? A GLU 453 CD  
98  1 Y 1 A GLU 468 ? OE1 ? A GLU 453 OE1 
99  1 Y 1 A GLU 468 ? OE2 ? A GLU 453 OE2 
100 1 Y 1 A ARG 471 ? CG  ? A ARG 456 CG  
101 1 Y 1 A ARG 471 ? CD  ? A ARG 456 CD  
102 1 Y 1 A ARG 471 ? NE  ? A ARG 456 NE  
103 1 Y 1 A ARG 471 ? CZ  ? A ARG 456 CZ  
104 1 Y 1 A ARG 471 ? NH1 ? A ARG 456 NH1 
105 1 Y 1 A ARG 471 ? NH2 ? A ARG 456 NH2 
106 1 Y 1 A ASP 472 ? CG  ? A ASP 457 CG  
107 1 Y 1 A ASP 472 ? OD1 ? A ASP 457 OD1 
108 1 Y 1 A ASP 472 ? OD2 ? A ASP 457 OD2 
109 1 Y 1 A TYR 473 ? CG  ? A TYR 458 CG  
110 1 Y 1 A TYR 473 ? CD1 ? A TYR 458 CD1 
111 1 Y 1 A TYR 473 ? CD2 ? A TYR 458 CD2 
112 1 Y 1 A TYR 473 ? CE1 ? A TYR 458 CE1 
113 1 Y 1 A TYR 473 ? CE2 ? A TYR 458 CE2 
114 1 Y 1 A TYR 473 ? CZ  ? A TYR 458 CZ  
115 1 Y 1 A TYR 473 ? OH  ? A TYR 458 OH  
116 1 Y 1 A TYR 474 ? CG  ? A TYR 459 CG  
117 1 Y 1 A TYR 474 ? CD1 ? A TYR 459 CD1 
118 1 Y 1 A TYR 474 ? CD2 ? A TYR 459 CD2 
119 1 Y 1 A TYR 474 ? CE1 ? A TYR 459 CE1 
120 1 Y 1 A TYR 474 ? CE2 ? A TYR 459 CE2 
121 1 Y 1 A TYR 474 ? CZ  ? A TYR 459 CZ  
122 1 Y 1 A TYR 474 ? OH  ? A TYR 459 OH  
123 1 Y 1 B GLN 1   ? CG  ? B GLN 1   CG  
124 1 Y 1 B GLN 1   ? CD  ? B GLN 1   CD  
125 1 Y 1 B GLN 1   ? OE1 ? B GLN 1   OE1 
126 1 Y 1 B GLN 1   ? NE2 ? B GLN 1   NE2 
127 1 Y 1 B ARG 83  ? NE  ? B ARG 83  NE  
128 1 Y 1 B ARG 83  ? CZ  ? B ARG 83  CZ  
129 1 Y 1 B ARG 83  ? NH1 ? B ARG 83  NH1 
130 1 Y 1 B ARG 83  ? NH2 ? B ARG 83  NH2 
131 1 Y 1 B GLN 123 ? CG  ? B GLN 123 CG  
132 1 Y 1 B GLN 123 ? CD  ? B GLN 123 CD  
133 1 Y 1 B GLN 123 ? OE1 ? B GLN 123 OE1 
134 1 Y 1 B GLN 123 ? NE2 ? B GLN 123 NE2 
135 1 Y 1 B LYS 147 ? CG  ? B LYS 147 CG  
136 1 Y 1 B LYS 147 ? CD  ? B LYS 147 CD  
137 1 Y 1 B LYS 147 ? CE  ? B LYS 147 CE  
138 1 Y 1 B LYS 147 ? NZ  ? B LYS 147 NZ  
139 1 Y 1 B LYS 224 ? CE  ? B LYS 224 CE  
140 1 Y 1 B LYS 224 ? NZ  ? B LYS 224 NZ  
141 1 Y 1 C ASP 124 ? CG  ? C ASP 124 CG  
142 1 Y 1 C ASP 124 ? OD1 ? C ASP 124 OD1 
143 1 Y 1 C ASP 124 ? OD2 ? C ASP 124 OD2 
144 1 Y 1 C LYS 128 ? CD  ? C LYS 128 CD  
145 1 Y 1 C LYS 128 ? CE  ? C LYS 128 CE  
146 1 Y 1 C LYS 128 ? NZ  ? C LYS 128 NZ  
147 1 Y 1 C LYS 147 ? CG  ? C LYS 147 CG  
148 1 Y 1 C LYS 147 ? CD  ? C LYS 147 CD  
149 1 Y 1 C LYS 147 ? CE  ? C LYS 147 CE  
150 1 Y 1 C LYS 147 ? NZ  ? C LYS 147 NZ  
151 1 Y 1 C GLN 149 ? CG  ? C GLN 149 CG  
152 1 Y 1 C GLN 149 ? CD  ? C GLN 149 CD  
153 1 Y 1 C GLN 149 ? OE1 ? C GLN 149 OE1 
154 1 Y 1 C GLN 149 ? NE2 ? C GLN 149 NE2 
155 1 Y 1 C LYS 151 ? CG  ? C LYS 151 CG  
156 1 Y 1 C LYS 151 ? CD  ? C LYS 151 CD  
157 1 Y 1 C LYS 151 ? CE  ? C LYS 151 CE  
158 1 Y 1 C LYS 151 ? NZ  ? C LYS 151 NZ  
159 1 Y 1 C LEU 156 ? CG  ? C LEU 156 CG  
160 1 Y 1 C LEU 156 ? CD1 ? C LEU 156 CD1 
161 1 Y 1 C LEU 156 ? CD2 ? C LEU 156 CD2 
162 1 Y 1 C SER 170 ? OG  ? C SER 170 OG  
163 1 Y 1 C LYS 171 ? CG  ? C LYS 171 CG  
164 1 Y 1 C LYS 171 ? CD  ? C LYS 171 CD  
165 1 Y 1 C LYS 171 ? CE  ? C LYS 171 CE  
166 1 Y 1 C LYS 171 ? NZ  ? C LYS 171 NZ  
167 1 Y 1 C LYS 185 ? CG  ? C LYS 185 CG  
168 1 Y 1 C LYS 185 ? CD  ? C LYS 185 CD  
169 1 Y 1 C LYS 185 ? CE  ? C LYS 185 CE  
170 1 Y 1 C LYS 185 ? NZ  ? C LYS 185 NZ  
171 1 Y 1 C LYS 190 ? CG  ? C LYS 190 CG  
172 1 Y 1 C LYS 190 ? CD  ? C LYS 190 CD  
173 1 Y 1 C LYS 190 ? CE  ? C LYS 190 CE  
174 1 Y 1 C LYS 190 ? NZ  ? C LYS 190 NZ  
175 1 Y 1 C LYS 192 ? CG  ? C LYS 192 CG  
176 1 Y 1 C LYS 192 ? CD  ? C LYS 192 CD  
177 1 Y 1 C LYS 192 ? CE  ? C LYS 192 CE  
178 1 Y 1 C LYS 192 ? NZ  ? C LYS 192 NZ  
179 1 Y 1 C LYS 209 ? CE  ? C LYS 209 CE  
180 1 Y 1 C LYS 209 ? NZ  ? C LYS 209 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DX6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     187.237 
_cell.length_a_esd                 ? 
_cell.length_b                     54.461 
_cell.length_b_esd                 ? 
_cell.length_c                     104.130 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9DX6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DX6 
_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             2.56 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.94 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '22% PEG Smear Broad, 0.1 M Tris pH 8.5, 0.3 M Glycyl-glycyl-glycine' 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-18 
_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   0.953724563122 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.953724563122 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DX6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               47.76 
_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                                     41378 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.53 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.18 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.166 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.40 2.54 ? ? ? ? ? ? 6614 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.176 ? ? 1 1 0.642              ? ? ? ? 1.0859999999999999  ? ? ? ? ? ? 
? ? ? 
2.54 2.72 ? ? ? ? ? ? 6229 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.8   ? ? 2 1 0.792              ? ? ? ? 0.743               ? ? ? ? ? ? 
? ? ? 
2.72 2.93 ? ? ? ? ? ? 5785 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.531 ? ? 3 1 0.9                ? ? ? ? 0.493               ? ? ? ? ? ? 
? ? ? 
2.93 3.21 ? ? ? ? ? ? 5377 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.331 ? ? 4 1 0.9540000000000001 ? ? ? ? 0.306               ? ? ? ? ? ? 
? ? ? 
3.21 3.59 ? ? ? ? ? ? 4881 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.184 ? ? 5 1 0.985              ? ? ? ? 0.17                ? ? ? ? ? ? 
? ? ? 
3.59 4.14 ? ? ? ? ? ? 4284 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.115 ? ? 6 1 0.9940000000000001 ? ? ? ? 0.107               ? ? ? ? ? ? 
? ? ? 
4.14 5.06 ? ? ? ? ? ? 3652 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.079 ? ? 7 1 0.997              ? ? ? ? 0.07400000000000001 ? ? ? ? ? ? 
? ? ? 
5.06 7.12 ? ? ? ? ? ? 2877 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.086 ? ? 8 1 0.996              ? ? ? ? 0.079               ? ? ? ? ? ? 
? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DX6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             47.76 
_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                     41218 
_refine.ls_number_reflns_R_free                  2060 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1936 
_refine.ls_R_factor_R_free                       0.2350 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1915 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.09 
_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                            0.30 
_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.pdbx_number_atoms_protein        6395 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               6654 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        47.76 
# 
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' ? 0.004 ? 6543 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.668 ? 8894 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.854 ? 901  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045 ? 983  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1162 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.46  . . 136 2579 100.00 . . . . 0.2973 . . . . . . . . . . . 0.3550 
'X-RAY DIFFRACTION' 2.46 2.52  . . 137 2589 100.00 . . . . 0.2768 . . . . . . . . . . . 0.3117 
'X-RAY DIFFRACTION' 2.52 2.59  . . 136 2598 100.00 . . . . 0.2525 . . . . . . . . . . . 0.3043 
'X-RAY DIFFRACTION' 2.59 2.66  . . 135 2564 100.00 . . . . 0.2355 . . . . . . . . . . . 0.2871 
'X-RAY DIFFRACTION' 2.66 2.75  . . 137 2609 100.00 . . . . 0.2270 . . . . . . . . . . . 0.3210 
'X-RAY DIFFRACTION' 2.75 2.85  . . 136 2592 100.00 . . . . 0.2251 . . . . . . . . . . . 0.2857 
'X-RAY DIFFRACTION' 2.85 2.96  . . 137 2597 100.00 . . . . 0.2067 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 2.96 3.09  . . 136 2594 100.00 . . . . 0.1946 . . . . . . . . . . . 0.2587 
'X-RAY DIFFRACTION' 3.09 3.26  . . 137 2607 100.00 . . . . 0.1876 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 3.26 3.46  . . 137 2601 100.00 . . . . 0.1789 . . . . . . . . . . . 0.2220 
'X-RAY DIFFRACTION' 3.46 3.73  . . 137 2600 100.00 . . . . 0.1753 . . . . . . . . . . . 0.2147 
'X-RAY DIFFRACTION' 3.73 4.10  . . 138 2612 100.00 . . . . 0.1645 . . . . . . . . . . . 0.1979 
'X-RAY DIFFRACTION' 4.10 4.70  . . 139 2641 100.00 . . . . 0.1597 . . . . . . . . . . . 0.1935 
'X-RAY DIFFRACTION' 4.70 5.92  . . 139 2644 100.00 . . . . 0.1827 . . . . . . . . . . . 0.2216 
'X-RAY DIFFRACTION' 5.92 47.76 . . 143 2731 100.00 . . . . 0.1950 . . . . . . . . . . . 0.2334 
# 
_struct.entry_id                     9DX6 
_struct.title                        'Crystal structure of Plasmodium vivax (Palo Alto) PvAMA1 in complex with human Fab 826827' 
_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        9DX6 
_struct_keywords.text            'inhibitory antibody, complex, Plasmodium vivax, cell invasion' 
_struct_keywords.pdbx_keywords   'CELL INVASION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP B9TXF7_PLAVI B9TXF7 ? 1 
;GRNQKPSRLTRSANNVLLEKGPTVERSTRMSNPWKAFMEKYDIERTHSSGVRVDLGEDAEVENAKYRIPAGRCPVFGKGI
VIENSAVSFLKPVATGDQRLKDGGFAFPNANDHISPMTLENLKARYKDNVEMMKLNDIALCRTHAASFVMAGDQNSSYRH
PAVYDEKEKTCHMLYLSAQENMGPRYCSPDAQNRDAVFCFKPDKNESFENLVYLSKNVRNDWDKKCPRKNLGNAKFGLWV
DGNCEEIPYVKEVEAKDLRECNRIVFEASASDQPTQYEEEMTDYQKIQQGFRQNNREMIKSAFLPVGAFNSDNFKSKGRG
FNWANFDSVKKKCYIFNTKPTCLINDKNFIATTALSHPREVDLEFPCSIYKDEIEREIKKQSRNMNLYSVDGERIVLPRI
FISNDKESIKCPCEPEHISNSTCNFYVCNCVEKRAEIKENNQVVIKEEFRDYYENGEEKSNKQ
;
22 
2 PDB 9DX6         9DX6   ? 2 ? 1  
3 PDB 9DX6         9DX6   ? 3 ? 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 9DX6 A 7 ? 469 ? B9TXF7 22 ? 484 ? 22 484 
2 2 9DX6 B 1 ? 234 ? 9DX6   1  ? 234 ? 1  234 
3 3 9DX6 C 1 ? 216 ? 9DX6   1  ? 216 ? 1  216 
# 
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 9DX6 HIS A 1   ? UNP B9TXF7 ?   ?   'expression tag'      16  1  
1 9DX6 HIS A 2   ? UNP B9TXF7 ?   ?   'expression tag'      17  2  
1 9DX6 HIS A 3   ? UNP B9TXF7 ?   ?   'expression tag'      18  3  
1 9DX6 HIS A 4   ? UNP B9TXF7 ?   ?   'expression tag'      19  4  
1 9DX6 HIS A 5   ? UNP B9TXF7 ?   ?   'expression tag'      20  5  
1 9DX6 HIS A 6   ? UNP B9TXF7 ?   ?   'expression tag'      21  6  
1 9DX6 ASN A 163 ? UNP B9TXF7 SER 178 'engineered mutation' 178 7  
1 9DX6 ASP A 211 ? UNP B9TXF7 ASN 226 'engineered mutation' 226 8  
1 9DX6 GLN A 426 ? UNP B9TXF7 ASN 441 'engineered mutation' 441 9  
1 9DX6 GLY A 470 ? UNP B9TXF7 ?   ?   'expression tag'      485 10 
1 9DX6 SER A 471 ? UNP B9TXF7 ?   ?   'expression tag'      486 11 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 6630  ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  34090 ? 
# 
_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 
# 
_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 ALA A 42  ? TYR A 47  ? ALA A 57  TYR A 62  5 ? 6  
HELX_P HELX_P2  AA2 ASP A 48  ? HIS A 53  ? ASP A 63  HIS A 68  1 ? 6  
HELX_P HELX_P3  AA3 ARG A 105 ? GLY A 109 ? ARG A 120 GLY A 124 5 ? 5  
HELX_P HELX_P4  AA4 LEU A 125 ? TYR A 132 ? LEU A 140 TYR A 147 1 ? 8  
HELX_P HELX_P5  AA5 GLU A 137 ? LEU A 141 ? GLU A 152 LEU A 156 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 142 ? PHE A 154 ? ASN A 157 PHE A 169 1 ? 13 
HELX_P HELX_P7  AA7 PRO A 190 ? SER A 194 ? PRO A 205 SER A 209 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 211 ? GLU A 215 ? ASP A 226 GLU A 230 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 227 ? CYS A 232 ? ASP A 242 CYS A 247 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 263 ? ALA A 274 ? ASP A 278 ALA A 289 1 ? 12 
HELX_P HELX_P11 AB2 TYR A 290 ? GLN A 299 ? TYR A 305 GLN A 314 1 ? 10 
HELX_P HELX_P12 AB3 ASN A 301 ? SER A 307 ? ASN A 316 SER A 322 1 ? 7  
HELX_P HELX_P13 AB4 SER A 374 ? LYS A 385 ? SER A 389 LYS A 400 1 ? 12 
HELX_P HELX_P14 AB5 GLU A 445 ? ASN A 447 ? GLU A 460 ASN A 462 5 ? 3  
HELX_P HELX_P15 AB6 LYS A 452 ? ASP A 457 ? LYS A 467 ASP A 472 1 ? 6  
HELX_P HELX_P16 AB7 LEU B 65  ? SER B 67  ? LEU B 65  SER B 67  5 ? 3  
HELX_P HELX_P17 AB8 THR B 88  ? THR B 92  ? THR B 88  THR B 92  5 ? 5  
HELX_P HELX_P18 AB9 SER B 145 ? LYS B 147 ? SER B 145 LYS B 147 5 ? 3  
HELX_P HELX_P19 AC1 SER B 174 ? ALA B 176 ? SER B 174 ALA B 176 5 ? 3  
HELX_P HELX_P20 AC2 SER B 205 ? GLN B 210 ? SER B 205 GLN B 210 5 ? 6  
HELX_P HELX_P21 AC3 LYS B 219 ? ASN B 222 ? LYS B 219 ASN B 222 5 ? 4  
HELX_P HELX_P22 AC4 GLN C 79  ? PHE C 83  ? GLN C 79  PHE C 83  5 ? 5  
HELX_P HELX_P23 AC5 SER C 123 ? SER C 129 ? SER C 123 SER C 129 1 ? 7  
HELX_P HELX_P24 AC6 LYS C 185 ? HIS C 191 ? LYS C 185 HIS C 191 1 ? 7  
# 
_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 79  SG ? ? ? 1_555 A CYS 232 SG ? ? A CYS 94  A CYS 247 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf2  disulf ? ? A CYS 147 SG ? ? ? 1_555 A CYS 177 SG ? ? A CYS 162 A CYS 192 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf3  disulf ? ? A CYS 193 SG ? ? ? 1_555 A CYS 205 SG ? ? A CYS 208 A CYS 220 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf4  disulf ? ? A CYS 250 SG ? ? ? 1_555 A CYS 348 SG ? ? A CYS 265 A CYS 363 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf5  disulf ? ? A CYS 267 SG ? ? ? 1_555 A CYS 339 SG ? ? A CYS 282 A CYS 354 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf6  disulf ? ? A CYS 373 SG ? ? ? 1_555 A CYS 429 SG ? ? A CYS 388 A CYS 444 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf7  disulf ? ? A CYS 417 SG ? ? ? 1_555 A CYS 434 SG ? ? A CYS 432 A CYS 449 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf8  disulf ? ? A CYS 419 SG ? ? ? 1_555 A CYS 436 SG ? ? A CYS 434 A CYS 451 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf9  disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 97  SG ? ? B CYS 22  B CYS 97  1_555 ? ? ? ? ? ? ? 2.054 ? ? 
disulf10 disulf ? ? B CYS 106 SG ? ? ? 1_555 B CYS 111 SG ? ? B CYS 106 B CYS 111 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf11 disulf ? ? B CYS 158 SG ? ? ? 1_555 B CYS 214 SG ? ? B CYS 158 B CYS 214 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf12 disulf ? ? C CYS 23  SG ? ? ? 1_555 C CYS 88  SG ? ? C CYS 23  C CYS 88  1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf13 disulf ? ? C CYS 136 SG ? ? ? 1_555 C CYS 196 SG ? ? C CYS 136 C CYS 196 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 79  ? CYS A 232 ? CYS A 94  ? 1_555 CYS A 247 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 147 ? CYS A 177 ? CYS A 162 ? 1_555 CYS A 192 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 193 ? CYS A 205 ? CYS A 208 ? 1_555 CYS A 220 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 250 ? CYS A 348 ? CYS A 265 ? 1_555 CYS A 363 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 267 ? CYS A 339 ? CYS A 282 ? 1_555 CYS A 354 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 373 ? CYS A 429 ? CYS A 388 ? 1_555 CYS A 444 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 417 ? CYS A 434 ? CYS A 432 ? 1_555 CYS A 449 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS A 419 ? CYS A 436 ? CYS A 434 ? 1_555 CYS A 451 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS B 22  ? CYS B 97  ? CYS B 22  ? 1_555 CYS B 97  ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS B 106 ? CYS B 111 ? CYS B 106 ? 1_555 CYS B 111 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS B 158 ? CYS B 214 ? CYS B 158 ? 1_555 CYS B 214 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS C 23  ? CYS C 88  ? CYS C 23  ? 1_555 CYS C 88  ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS C 136 ? CYS C 196 ? CYS C 136 ? 1_555 CYS C 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 121 A . ? SER 136 A PRO 122 A ? PRO 137 A 1 -11.45 
2 PHE 164 B . ? PHE 164 B PRO 165 B ? PRO 165 B 1 -6.26  
3 GLU 166 B . ? GLU 166 B PRO 167 B ? PRO 167 B 1 0.91   
4 SER 7   C . ? SER 7   C PRO 8   C ? PRO 8   C 1 -9.67  
5 TRP 94  C . ? TRP 94  C PRO 95  C ? PRO 95  C 1 0.53   
6 TYR 142 C . ? TYR 142 C PRO 143 C ? PRO 143 C 1 5.86   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 3 ? 
AB5 ? 4 ? 
AB6 ? 6 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
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 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? 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 GLU A 63  ? VAL A 67  ? GLU A 78  VAL A 82  
AA1 2 ALA A 70  ? ILE A 74  ? ALA A 85  ILE A 89  
AA2 1 VAL A 81  ? PHE A 82  ? VAL A 96  PHE A 97  
AA2 2 LEU A 217 ? LEU A 220 ? LEU A 232 LEU A 235 
AA2 3 ALA A 168 ? ASP A 171 ? ALA A 183 ASP A 186 
AA2 4 THR A 176 ? MET A 179 ? THR A 191 MET A 194 
AA2 5 MET A 123 ? THR A 124 ? MET A 138 THR A 139 
AA3 1 GLY A 85  ? ILE A 88  ? GLY A 100 ILE A 103 
AA3 2 PHE A 206 ? ASP A 209 ? PHE A 221 ASP A 224 
AA4 1 VAL A 155 ? MET A 156 ? VAL A 170 MET A 171 
AA4 2 ALA B 93  ? SER B 107 ? ALA B 93  SER B 107 
AA4 3 TYR B 34  ? GLN B 41  ? TYR B 34  GLN B 41  
AA4 4 GLU B 48  ? ILE B 53  ? GLU B 48  ILE B 53  
AA5 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA5 2 THR B 125 ? VAL B 129 ? THR B 125 VAL B 129 
AA5 3 ALA B 93  ? SER B 107 ? ALA B 93  SER B 107 
AA5 4 THR B 110 ? TRP B 121 ? THR B 110 TRP B 121 
AA6 1 CYS A 250 ? GLU A 251 ? CYS A 265 GLU A 266 
AA6 2 ASN A 236 ? TRP A 245 ? ASN A 251 TRP A 260 
AA6 3 CYS A 348 ? THR A 359 ? CYS A 363 THR A 374 
AA6 4 TRP A 329 ? ASP A 333 ? TRP A 344 ASP A 348 
AA6 5 LYS A 338 ? PHE A 342 ? LYS A 353 PHE A 357 
AA6 6 LYS A 257 ? GLU A 260 ? LYS A 272 GLU A 275 
AA7 1 CYS A 250 ? GLU A 251 ? CYS A 265 GLU A 266 
AA7 2 ASN A 236 ? TRP A 245 ? ASN A 251 TRP A 260 
AA7 3 VAL A 367 ? ASP A 368 ? VAL A 382 ASP A 383 
AA8 1 ILE A 408 ? SER A 409 ? ILE A 423 SER A 424 
AA8 2 TYR A 432 ? VAL A 433 ? TYR A 447 VAL A 448 
AA8 3 GLU A 422 ? HIS A 423 ? GLU A 437 HIS A 438 
AA9 1 ALA A 441 ? ILE A 443 ? ALA A 456 ILE A 458 
AA9 2 VAL A 449 ? ILE A 451 ? VAL A 464 ILE A 466 
AB1 1 GLN B 3   ? GLU B 6   ? GLN B 3   GLU B 6   
AB1 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AB1 3 GLN B 79  ? LEU B 84  ? GLN B 79  LEU B 84  
AB1 4 VAL B 69  ? ASP B 74  ? VAL B 69  ASP B 74  
AB2 1 SER B 138 ? LEU B 142 ? SER B 138 LEU B 142 
AB2 2 THR B 153 ? TYR B 163 ? THR B 153 TYR B 163 
AB2 3 TYR B 194 ? PRO B 203 ? TYR B 194 PRO B 203 
AB2 4 VAL B 181 ? THR B 183 ? VAL B 181 THR B 183 
AB3 1 THR B 149 ? SER B 150 ? THR B 149 SER B 150 
AB3 2 THR B 153 ? TYR B 163 ? THR B 153 TYR B 163 
AB3 3 TYR B 194 ? PRO B 203 ? TYR B 194 PRO B 203 
AB3 4 VAL B 187 ? LEU B 188 ? VAL B 187 LEU B 188 
AB4 1 THR B 169 ? TRP B 172 ? THR B 169 TRP B 172 
AB4 2 ILE B 213 ? HIS B 218 ? ILE B 213 HIS B 218 
AB4 3 THR B 223 ? ARG B 228 ? THR B 223 ARG B 228 
AB5 1 MET C 4   ? SER C 7   ? MET C 4   SER C 7   
AB5 2 ALA C 19  ? ALA C 25  ? ALA C 19  ALA C 25  
AB5 3 GLU C 70  ? ILE C 75  ? GLU C 70  ILE C 75  
AB5 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AB6 1 THR C 10  ? LEU C 13  ? THR C 10  LEU C 13  
AB6 2 THR C 104 ? ILE C 108 ? THR C 104 ILE C 108 
AB6 3 ALA C 84  ? GLN C 90  ? ALA C 84  GLN C 90  
AB6 4 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AB6 5 ARG C 45  ? TYR C 49  ? ARG C 45  TYR C 49  
AB6 6 THR C 53  ? ARG C 54  ? THR C 53  ARG C 54  
AB7 1 THR C 10  ? LEU C 13  ? THR C 10  LEU C 13  
AB7 2 THR C 104 ? ILE C 108 ? THR C 104 ILE C 108 
AB7 3 ALA C 84  ? GLN C 90  ? ALA C 84  GLN C 90  
AB7 4 THR C 99  ? PHE C 100 ? THR C 99  PHE C 100 
AB8 1 SER C 116 ? PHE C 120 ? SER C 116 PHE C 120 
AB8 2 THR C 131 ? PHE C 141 ? THR C 131 PHE C 141 
AB8 3 TYR C 175 ? SER C 184 ? TYR C 175 SER C 184 
AB8 4 SER C 161 ? VAL C 165 ? SER C 161 VAL C 165 
AB9 1 ALA C 155 ? LEU C 156 ? ALA C 155 LEU C 156 
AB9 2 LYS C 147 ? VAL C 152 ? LYS C 147 VAL C 152 
AB9 3 VAL C 193 ? THR C 199 ? VAL C 193 THR C 199 
AB9 4 VAL C 207 ? ASN C 212 ? VAL C 207 ASN C 212 
# 
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 65  ? N ALA A 80  O TYR A 72  ? O TYR A 87  
AA2 1 2 N VAL A 81  ? N VAL A 96  O TYR A 219 ? O TYR A 234 
AA2 2 3 O LEU A 220 ? O LEU A 235 N ALA A 168 ? N ALA A 183 
AA2 3 4 N ASP A 171 ? N ASP A 186 O THR A 176 ? O THR A 191 
AA2 4 5 O CYS A 177 ? O CYS A 192 N MET A 123 ? N MET A 138 
AA3 1 2 N VAL A 87  ? N VAL A 102 O LYS A 207 ? O LYS A 222 
AA4 1 2 N VAL A 155 ? N VAL A 170 O CYS B 106 ? O CYS B 106 
AA4 2 3 O SER B 100 ? O SER B 100 N TYR B 35  ? N TYR B 35  
AA4 3 4 N TRP B 38  ? N TRP B 38  O ILE B 50  ? O ILE B 50  
AA5 1 2 N GLY B 10  ? N GLY B 10  O THR B 128 ? O THR B 128 
AA5 2 3 O VAL B 127 ? O VAL B 127 N ALA B 93  ? N ALA B 93  
AA5 3 4 N GLU B 103 ? N GLU B 103 O LEU B 114 ? O LEU B 114 
AA6 1 2 O GLU A 251 ? O GLU A 266 N LEU A 244 ? N LEU A 259 
AA6 2 3 N LYS A 241 ? N LYS A 256 O ILE A 350 ? O ILE A 365 
AA6 3 4 O ILE A 356 ? O ILE A 371 N PHE A 332 ? N PHE A 347 
AA6 4 5 N ASN A 331 ? N ASN A 346 O TYR A 340 ? O TYR A 355 
AA6 5 6 O CYS A 339 ? O CYS A 354 N VAL A 259 ? N VAL A 274 
AA7 1 2 O GLU A 251 ? O GLU A 266 N LEU A 244 ? N LEU A 259 
AA7 2 3 N ASN A 236 ? N ASN A 251 O ASP A 368 ? O ASP A 383 
AA8 1 2 N SER A 409 ? N SER A 424 O TYR A 432 ? O TYR A 447 
AA8 2 3 O VAL A 433 ? O VAL A 448 N GLU A 422 ? N GLU A 437 
AA9 1 2 N GLU A 442 ? N GLU A 457 O VAL A 450 ? O VAL A 465 
AB1 1 2 N GLN B 3   ? N GLN B 3   O SER B 25  ? O SER B 25  
AB1 2 3 N LEU B 18  ? N LEU B 18  O LEU B 84  ? O LEU B 84  
AB1 3 4 O GLN B 79  ? O GLN B 79  N ASP B 74  ? N ASP B 74  
AB2 1 2 N PHE B 140 ? N PHE B 140 O LEU B 159 ? O LEU B 159 
AB2 2 3 N ALA B 154 ? N ALA B 154 O VAL B 202 ? O VAL B 202 
AB2 3 4 O VAL B 199 ? O VAL B 199 N HIS B 182 ? N HIS B 182 
AB3 1 2 N SER B 150 ? N SER B 150 O THR B 153 ? O THR B 153 
AB3 2 3 N ALA B 154 ? N ALA B 154 O VAL B 202 ? O VAL B 202 
AB3 3 4 O SER B 195 ? O SER B 195 N VAL B 187 ? N VAL B 187 
AB4 1 2 N THR B 169 ? N THR B 169 O ASN B 217 ? O ASN B 217 
AB4 2 3 N VAL B 216 ? N VAL B 216 O VAL B 225 ? O VAL B 225 
AB5 1 2 N THR C 5   ? N THR C 5   O ARG C 24  ? O ARG C 24  
AB5 2 3 N LEU C 21  ? N LEU C 21  O LEU C 73  ? O LEU C 73  
AB5 3 4 O THR C 74  ? O THR C 74  N SER C 63  ? N SER C 63  
AB6 1 2 N LEU C 11  ? N LEU C 11  O GLU C 107 ? O GLU C 107 
AB6 2 3 O VAL C 106 ? O VAL C 106 N ALA C 84  ? N ALA C 84  
AB6 3 4 O VAL C 85  ? O VAL C 85  N GLN C 38  ? N GLN C 38  
AB6 4 5 N TRP C 35  ? N TRP C 35  O LEU C 47  ? O LEU C 47  
AB6 5 6 N TYR C 49  ? N TYR C 49  O THR C 53  ? O THR C 53  
AB7 1 2 N LEU C 11  ? N LEU C 11  O GLU C 107 ? O GLU C 107 
AB7 2 3 O VAL C 106 ? O VAL C 106 N ALA C 84  ? N ALA C 84  
AB7 3 4 N GLN C 90  ? N GLN C 90  O THR C 99  ? O THR C 99  
AB8 1 2 N PHE C 120 ? N PHE C 120 O VAL C 135 ? O VAL C 135 
AB8 2 3 N LEU C 138 ? N LEU C 138 O LEU C 177 ? O LEU C 177 
AB8 3 4 O THR C 180 ? O THR C 180 N GLN C 162 ? N GLN C 162 
AB9 1 2 O ALA C 155 ? O ALA C 155 N VAL C 152 ? N VAL C 152 
AB9 2 3 N GLN C 149 ? N GLN C 149 O GLU C 197 ? O GLU C 197 
AB9 3 4 N VAL C 198 ? N VAL C 198 O VAL C 207 ? O VAL C 207 
# 
_pdbx_entry_details.entry_id                   9DX6 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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 O   B HOH 338 ? ? O  B HOH 352 ? ? 2.12 
2 1 O   B HOH 342 ? ? O  B HOH 354 ? ? 2.13 
3 1 OE2 A GLU 141 ? ? O  A HOH 501 ? ? 2.14 
4 1 O   B HOH 350 ? ? O  B HOH 353 ? ? 2.18 
5 1 NH2 A ARG 47  ? ? O  A ILE 430 ? ? 2.19 
6 1 O   C HIS 191 ? ? NE C ARG 213 ? ? 2.19 
# 
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 VAL A 72  ? ? -104.09 -63.03  
2  1 LEU A 76  ? ? -142.48 49.80   
3  1 ASP A 118 ? ? -90.15  37.63   
4  1 ASN A 130 ? ? -87.19  47.50   
5  1 ILE A 135 ? ? -106.52 -75.89  
6  1 LYS A 225 ? ? -106.66 65.82   
7  1 ASP A 242 ? ? -99.57  33.70   
8  1 ARG A 249 ? ? -146.16 -68.56  
9  1 CYS A 434 ? ? -130.47 -151.26 
10 1 CYS A 451 ? ? -102.76 63.86   
11 1 LYS A 459 ? ? -79.97  -164.80 
12 1 SER B 15  ? ? 77.16   -10.78  
13 1 GLN B 45  ? ? -125.37 -167.60 
14 1 TYR B 116 ? ? -153.99 80.01   
15 1 ASP B 162 ? ? 64.44   65.92   
16 1 SER C 30  ? ? 52.78   -113.94 
17 1 ALA C 51  ? ? 70.94   -37.86  
18 1 TYR C 91  ? ? -148.04 50.73   
19 1 ASN C 154 ? ? 55.02   8.07    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS 16  ? A HIS 1   
2  1 Y 1 A HIS 17  ? A HIS 2   
3  1 Y 1 A HIS 18  ? A HIS 3   
4  1 Y 1 A HIS 19  ? A HIS 4   
5  1 Y 1 A HIS 20  ? A HIS 5   
6  1 Y 1 A HIS 21  ? A HIS 6   
7  1 Y 1 A GLY 22  ? A GLY 7   
8  1 Y 1 A ARG 23  ? A ARG 8   
9  1 Y 1 A ASN 24  ? A ASN 9   
10 1 Y 1 A GLN 25  ? A GLN 10  
11 1 Y 1 A LYS 26  ? A LYS 11  
12 1 Y 1 A PRO 27  ? A PRO 12  
13 1 Y 1 A SER 28  ? A SER 13  
14 1 Y 1 A ARG 29  ? A ARG 14  
15 1 Y 1 A LEU 30  ? A LEU 15  
16 1 Y 1 A THR 31  ? A THR 16  
17 1 Y 1 A ARG 32  ? A ARG 17  
18 1 Y 1 A SER 33  ? A SER 18  
19 1 Y 1 A ALA 34  ? A ALA 19  
20 1 Y 1 A ASN 35  ? A ASN 20  
21 1 Y 1 A ASN 36  ? A ASN 21  
22 1 Y 1 A VAL 37  ? A VAL 22  
23 1 Y 1 A LEU 38  ? A LEU 23  
24 1 Y 1 A LEU 39  ? A LEU 24  
25 1 Y 1 A GLU 40  ? A GLU 25  
26 1 Y 1 A LYS 41  ? A LYS 26  
27 1 Y 1 A GLY 42  ? A GLY 27  
28 1 Y 1 A PRO 43  ? A PRO 28  
29 1 Y 1 A THR 44  ? A THR 29  
30 1 Y 1 A VAL 45  ? A VAL 30  
31 1 Y 1 A ASP 211 ? A ASP 196 
32 1 Y 1 A ALA 212 ? A ALA 197 
33 1 Y 1 A GLN 213 ? A GLN 198 
34 1 Y 1 A ASN 214 ? A ASN 199 
35 1 Y 1 A ARG 215 ? A ARG 200 
36 1 Y 1 A THR 296 ? A THR 281 
37 1 Y 1 A GLN 297 ? A GLN 282 
38 1 Y 1 A TYR 298 ? A TYR 283 
39 1 Y 1 A GLU 299 ? A GLU 284 
40 1 Y 1 A GLU 300 ? A GLU 285 
41 1 Y 1 A GLU 301 ? A GLU 286 
42 1 Y 1 A MET 302 ? A MET 287 
43 1 Y 1 A THR 303 ? A THR 288 
44 1 Y 1 A GLY 328 ? A GLY 313 
45 1 Y 1 A ALA 329 ? A ALA 314 
46 1 Y 1 A PHE 330 ? A PHE 315 
47 1 Y 1 A ASN 331 ? A ASN 316 
48 1 Y 1 A SER 332 ? A SER 317 
49 1 Y 1 A ASP 333 ? A ASP 318 
50 1 Y 1 A ASN 334 ? A ASN 319 
51 1 Y 1 A GLN 402 ? A GLN 387 
52 1 Y 1 A SER 403 ? A SER 388 
53 1 Y 1 A ARG 404 ? A ARG 389 
54 1 Y 1 A ASN 405 ? A ASN 390 
55 1 Y 1 A MET 406 ? A MET 391 
56 1 Y 1 A ASN 407 ? A ASN 392 
57 1 Y 1 A LEU 408 ? A LEU 393 
58 1 Y 1 A TYR 409 ? A TYR 394 
59 1 Y 1 A SER 410 ? A SER 395 
60 1 Y 1 A VAL 411 ? A VAL 396 
61 1 Y 1 A ASP 412 ? A ASP 397 
62 1 Y 1 A GLY 413 ? A GLY 398 
63 1 Y 1 A GLU 414 ? A GLU 399 
64 1 Y 1 A ARG 415 ? A ARG 400 
65 1 Y 1 A GLU 475 ? A GLU 460 
66 1 Y 1 A ASN 476 ? A ASN 461 
67 1 Y 1 A GLY 477 ? A GLY 462 
68 1 Y 1 A GLU 478 ? A GLU 463 
69 1 Y 1 A GLU 479 ? A GLU 464 
70 1 Y 1 A LYS 480 ? A LYS 465 
71 1 Y 1 A SER 481 ? A SER 466 
72 1 Y 1 A ASN 482 ? A ASN 467 
73 1 Y 1 A LYS 483 ? A LYS 468 
74 1 Y 1 A GLN 484 ? A GLN 469 
75 1 Y 1 A GLY 485 ? A GLY 470 
76 1 Y 1 A SER 486 ? A SER 471 
77 1 Y 1 B LYS 232 ? B LYS 232 
78 1 Y 1 B SER 233 ? B SER 233 
79 1 Y 1 B CYS 234 ? B CYS 234 
80 1 Y 1 C GLU 215 ? C GLU 215 
81 1 Y 1 C CYS 216 ? C CYS 216 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 'R01 AI143694' 1 
'Department of Veterans Affairs (VA, United States)'                                              'United States' BX001350       2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 5NQR ? 
2 ? 'experimental model' PDB 6FG1 ? 
# 
_atom_sites.entry_id                    9DX6 
_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]   0.005341 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000675 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018362 
_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]   0.009680 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLU A 1 31  ? -9.141  -5.601 0.813   1.00 75.41  ? 46  GLU A N   1 
ATOM   2    C CA  . GLU A 1 31  ? -8.263  -4.439 0.717   1.00 72.73  ? 46  GLU A CA  1 
ATOM   3    C C   . GLU A 1 31  ? -8.667  -3.356 1.714   1.00 68.19  ? 46  GLU A C   1 
ATOM   4    O O   . GLU A 1 31  ? -9.520  -3.574 2.576   1.00 72.74  ? 46  GLU A O   1 
ATOM   5    C CB  . GLU A 1 31  ? -8.274  -3.873 -0.705  1.00 69.08  ? 46  GLU A CB  1 
ATOM   6    N N   . ARG A 1 32  ? -8.039  -2.190 1.589   1.00 70.89  ? 47  ARG A N   1 
ATOM   7    C CA  . ARG A 1 32  ? -8.332  -1.080 2.484   1.00 66.87  ? 47  ARG A CA  1 
ATOM   8    C C   . ARG A 1 32  ? -9.750  -0.582 2.264   1.00 67.39  ? 47  ARG A C   1 
ATOM   9    O O   . ARG A 1 32  ? -10.217 -0.478 1.128   1.00 64.18  ? 47  ARG A O   1 
ATOM   10   C CB  . ARG A 1 32  ? -7.355  0.069  2.250   1.00 60.07  ? 47  ARG A CB  1 
ATOM   11   C CG  . ARG A 1 32  ? -6.043  -0.081 2.971   1.00 71.24  ? 47  ARG A CG  1 
ATOM   12   C CD  . ARG A 1 32  ? -6.106  0.272  4.447   1.00 62.28  ? 47  ARG A CD  1 
ATOM   13   N NE  . ARG A 1 32  ? -4.863  -0.150 5.079   1.00 65.17  ? 47  ARG A NE  1 
ATOM   14   C CZ  . ARG A 1 32  ? -4.771  -1.096 6.001   1.00 59.76  ? 47  ARG A CZ  1 
ATOM   15   N NH1 . ARG A 1 32  ? -5.847  -1.620 6.561   1.00 63.52  ? 47  ARG A NH1 1 
ATOM   16   N NH2 . ARG A 1 32  ? -3.569  -1.521 6.376   1.00 65.15  ? 47  ARG A NH2 1 
ATOM   17   N N   . SER A 1 33  ? -10.434 -0.273 3.361   1.00 71.96  ? 48  SER A N   1 
ATOM   18   C CA  . SER A 1 33  ? -11.680 0.467  3.261   1.00 62.13  ? 48  SER A CA  1 
ATOM   19   C C   . SER A 1 33  ? -11.423 1.837  2.642   1.00 59.07  ? 48  SER A C   1 
ATOM   20   O O   . SER A 1 33  ? -10.325 2.397  2.736   1.00 62.71  ? 48  SER A O   1 
ATOM   21   C CB  . SER A 1 33  ? -12.325 0.625  4.638   1.00 56.79  ? 48  SER A CB  1 
ATOM   22   O OG  . SER A 1 33  ? -13.396 1.551  4.592   1.00 57.21  ? 48  SER A OG  1 
ATOM   23   N N   . THR A 1 34  ? -12.441 2.362  1.970   1.00 57.51  ? 49  THR A N   1 
ATOM   24   C CA  . THR A 1 34  ? -12.432 3.746  1.531   1.00 61.06  ? 49  THR A CA  1 
ATOM   25   C C   . THR A 1 34  ? -13.165 4.650  2.510   1.00 56.58  ? 49  THR A C   1 
ATOM   26   O O   . THR A 1 34  ? -13.057 5.877  2.407   1.00 56.84  ? 49  THR A O   1 
ATOM   27   C CB  . THR A 1 34  ? -13.051 3.862  0.128   1.00 61.14  ? 49  THR A CB  1 
ATOM   28   O OG1 . THR A 1 34  ? -12.552 5.038  -0.524  1.00 64.19  ? 49  THR A OG1 1 
ATOM   29   C CG2 . THR A 1 34  ? -14.569 3.924  0.205   1.00 53.65  ? 49  THR A CG2 1 
ATOM   30   N N   . ARG A 1 35  ? -13.885 4.065  3.463   1.00 54.49  ? 50  ARG A N   1 
ATOM   31   C CA  . ARG A 1 35  ? -14.552 4.825  4.507   1.00 57.23  ? 50  ARG A CA  1 
ATOM   32   C C   . ARG A 1 35  ? -13.554 5.266  5.569   1.00 57.50  ? 50  ARG A C   1 
ATOM   33   O O   . ARG A 1 35  ? -12.637 4.524  5.934   1.00 57.76  ? 50  ARG A O   1 
ATOM   34   C CB  . ARG A 1 35  ? -15.657 3.986  5.150   1.00 59.03  ? 50  ARG A CB  1 
ATOM   35   N N   . MET A 1 36  ? -13.738 6.484  6.064   1.00 60.31  ? 51  MET A N   1 
ATOM   36   C CA  . MET A 1 36  ? -12.938 6.983  7.170   1.00 59.11  ? 51  MET A CA  1 
ATOM   37   C C   . MET A 1 36  ? -13.460 6.429  8.489   1.00 59.82  ? 51  MET A C   1 
ATOM   38   O O   . MET A 1 36  ? -14.660 6.194  8.659   1.00 62.08  ? 51  MET A O   1 
ATOM   39   C CB  . MET A 1 36  ? -12.963 8.510  7.194   1.00 54.60  ? 51  MET A CB  1 
ATOM   40   C CG  . MET A 1 36  ? -12.605 9.129  5.863   1.00 59.44  ? 51  MET A CG  1 
ATOM   41   S SD  . MET A 1 36  ? -10.881 9.641  5.784   1.00 67.28  ? 51  MET A SD  1 
ATOM   42   C CE  . MET A 1 36  ? -11.013 11.350 6.308   1.00 62.95  ? 51  MET A CE  1 
ATOM   43   N N   . SER A 1 37  ? -12.543 6.211  9.428   1.00 60.23  ? 52  SER A N   1 
ATOM   44   C CA  . SER A 1 37  ? -12.907 5.666  10.729  1.00 64.47  ? 52  SER A CA  1 
ATOM   45   C C   . SER A 1 37  ? -12.060 6.316  11.812  1.00 59.28  ? 52  SER A C   1 
ATOM   46   O O   . SER A 1 37  ? -10.840 6.432  11.667  1.00 60.02  ? 52  SER A O   1 
ATOM   47   C CB  . SER A 1 37  ? -12.737 4.143  10.759  1.00 56.97  ? 52  SER A CB  1 
ATOM   48   O OG  . SER A 1 37  ? -11.487 3.763  10.214  1.00 64.48  ? 52  SER A OG  1 
ATOM   49   N N   . ASN A 1 38  ? -12.715 6.756  12.882  1.00 57.07  ? 53  ASN A N   1 
ATOM   50   C CA  . ASN A 1 38  ? -12.031 7.284  14.061  1.00 49.40  ? 53  ASN A CA  1 
ATOM   51   C C   . ASN A 1 38  ? -12.398 6.420  15.252  1.00 45.59  ? 53  ASN A C   1 
ATOM   52   O O   . ASN A 1 38  ? -13.509 6.547  15.797  1.00 43.02  ? 53  ASN A O   1 
ATOM   53   C CB  . ASN A 1 38  ? -12.403 8.741  14.325  1.00 46.41  ? 53  ASN A CB  1 
ATOM   54   C CG  . ASN A 1 38  ? -11.517 9.381  15.379  1.00 51.70  ? 53  ASN A CG  1 
ATOM   55   O OD1 . ASN A 1 38  ? -10.757 8.693  16.062  1.00 50.86  ? 53  ASN A OD1 1 
ATOM   56   N ND2 . ASN A 1 38  ? -11.604 10.701 15.512  1.00 46.84  ? 53  ASN A ND2 1 
ATOM   57   N N   . PRO A 1 39  ? -11.507 5.530  15.699  1.00 50.05  ? 54  PRO A N   1 
ATOM   58   C CA  . PRO A 1 39  ? -11.804 4.729  16.896  1.00 49.77  ? 54  PRO A CA  1 
ATOM   59   C C   . PRO A 1 39  ? -11.878 5.546  18.178  1.00 40.46  ? 54  PRO A C   1 
ATOM   60   O O   . PRO A 1 39  ? -12.269 4.992  19.211  1.00 41.78  ? 54  PRO A O   1 
ATOM   61   C CB  . PRO A 1 39  ? -10.643 3.726  16.939  1.00 50.31  ? 54  PRO A CB  1 
ATOM   62   C CG  . PRO A 1 39  ? -9.531  4.413  16.216  1.00 48.91  ? 54  PRO A CG  1 
ATOM   63   C CD  . PRO A 1 39  ? -10.187 5.213  15.130  1.00 48.30  ? 54  PRO A CD  1 
ATOM   64   N N   . TRP A 1 40  ? -11.532 6.834  18.144  1.00 42.49  ? 55  TRP A N   1 
ATOM   65   C CA  . TRP A 1 40  ? -11.542 7.691  19.323  1.00 43.93  ? 55  TRP A CA  1 
ATOM   66   C C   . TRP A 1 40  ? -12.855 8.441  19.520  1.00 46.29  ? 55  TRP A C   1 
ATOM   67   O O   . TRP A 1 40  ? -12.984 9.164  20.515  1.00 42.19  ? 55  TRP A O   1 
ATOM   68   C CB  . TRP A 1 40  ? -10.402 8.716  19.245  1.00 40.57  ? 55  TRP A CB  1 
ATOM   69   C CG  . TRP A 1 40  ? -9.026  8.153  19.456  1.00 43.05  ? 55  TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 40  ? -8.110  7.833  18.491  1.00 43.16  ? 55  TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 40  ? -8.402  7.861  20.712  1.00 39.36  ? 55  TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 40  ? -6.956  7.357  19.072  1.00 45.01  ? 55  TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 40  ? -7.112  7.360  20.434  1.00 44.02  ? 55  TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 40  ? -8.811  7.970  22.046  1.00 40.97  ? 55  TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 40  ? -6.228  6.969  21.442  1.00 38.99  ? 55  TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 40  ? -7.936  7.580  23.044  1.00 37.94  ? 55  TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 40  ? -6.658  7.085  22.737  1.00 41.35  ? 55  TRP A CH2 1 
ATOM   78   N N   . LYS A 1 41  ? -13.824 8.279  18.612  1.00 43.27  ? 56  LYS A N   1 
ATOM   79   C CA  . LYS A 1 41  ? -14.977 9.179  18.562  1.00 40.29  ? 56  LYS A CA  1 
ATOM   80   C C   . LYS A 1 41  ? -15.724 9.222  19.892  1.00 40.89  ? 56  LYS A C   1 
ATOM   81   O O   . LYS A 1 41  ? -15.977 10.302 20.439  1.00 46.68  ? 56  LYS A O   1 
ATOM   82   C CB  . LYS A 1 41  ? -15.919 8.758  17.430  1.00 46.99  ? 56  LYS A CB  1 
ATOM   83   N N   . ALA A 1 42  ? -16.093 8.057  20.426  1.00 38.34  ? 57  ALA A N   1 
ATOM   84   C CA  . ALA A 1 42  ? -16.809 8.029  21.699  1.00 43.06  ? 57  ALA A CA  1 
ATOM   85   C C   . ALA A 1 42  ? -15.919 8.521  22.833  1.00 44.24  ? 57  ALA A C   1 
ATOM   86   O O   . ALA A 1 42  ? -16.305 9.411  23.600  1.00 40.98  ? 57  ALA A O   1 
ATOM   87   C CB  . ALA A 1 42  ? -17.318 6.615  21.989  1.00 27.00  ? 57  ALA A CB  1 
ATOM   88   N N   . PHE A 1 43  ? -14.717 7.946  22.939  1.00 43.81  ? 58  PHE A N   1 
ATOM   89   C CA  . PHE A 1 43  ? -13.765 8.311  23.982  1.00 36.87  ? 58  PHE A CA  1 
ATOM   90   C C   . PHE A 1 43  ? -13.540 9.816  24.042  1.00 39.20  ? 58  PHE A C   1 
ATOM   91   O O   . PHE A 1 43  ? -13.469 10.396 25.132  1.00 41.42  ? 58  PHE A O   1 
ATOM   92   C CB  . PHE A 1 43  ? -12.447 7.570  23.728  1.00 33.94  ? 58  PHE A CB  1 
ATOM   93   C CG  . PHE A 1 43  ? -11.395 7.785  24.780  1.00 36.93  ? 58  PHE A CG  1 
ATOM   94   C CD1 . PHE A 1 43  ? -10.632 8.946  24.798  1.00 32.15  ? 58  PHE A CD1 1 
ATOM   95   C CD2 . PHE A 1 43  ? -11.138 6.804  25.726  1.00 35.48  ? 58  PHE A CD2 1 
ATOM   96   C CE1 . PHE A 1 43  ? -9.661  9.132  25.751  1.00 35.58  ? 58  PHE A CE1 1 
ATOM   97   C CE2 . PHE A 1 43  ? -10.160 6.983  26.681  1.00 32.04  ? 58  PHE A CE2 1 
ATOM   98   C CZ  . PHE A 1 43  ? -9.421  8.149  26.696  1.00 37.71  ? 58  PHE A CZ  1 
ATOM   99   N N   . MET A 1 44  ? -13.424 10.465 22.884  1.00 37.27  ? 59  MET A N   1 
ATOM   100  C CA  . MET A 1 44  ? -13.077 11.880 22.812  1.00 39.46  ? 59  MET A CA  1 
ATOM   101  C C   . MET A 1 44  ? -14.273 12.810 22.949  1.00 37.46  ? 59  MET A C   1 
ATOM   102  O O   . MET A 1 44  ? -14.090 14.031 22.918  1.00 37.77  ? 59  MET A O   1 
ATOM   103  C CB  . MET A 1 44  ? -12.353 12.183 21.496  1.00 33.11  ? 59  MET A CB  1 
ATOM   104  C CG  . MET A 1 44  ? -10.949 11.625 21.434  1.00 39.41  ? 59  MET A CG  1 
ATOM   105  S SD  . MET A 1 44  ? -9.988  12.012 22.915  1.00 40.39  ? 59  MET A SD  1 
ATOM   106  C CE  . MET A 1 44  ? -9.327  13.615 22.490  1.00 36.94  ? 59  MET A CE  1 
ATOM   107  N N   . GLU A 1 45  ? -15.483 12.272 23.116  1.00 40.58  ? 60  GLU A N   1 
ATOM   108  C CA  . GLU A 1 45  ? -16.665 13.129 23.174  1.00 46.97  ? 60  GLU A CA  1 
ATOM   109  C C   . GLU A 1 45  ? -16.611 14.076 24.368  1.00 43.13  ? 60  GLU A C   1 
ATOM   110  O O   . GLU A 1 45  ? -17.002 15.244 24.260  1.00 41.60  ? 60  GLU A O   1 
ATOM   111  C CB  . GLU A 1 45  ? -17.932 12.275 23.221  1.00 47.18  ? 60  GLU A CB  1 
ATOM   112  C CG  . GLU A 1 45  ? -18.935 12.601 22.129  1.00 59.86  ? 60  GLU A CG  1 
ATOM   113  C CD  . GLU A 1 45  ? -20.111 11.640 22.104  1.00 66.75  ? 60  GLU A CD  1 
ATOM   114  O OE1 . GLU A 1 45  ? -21.017 11.776 22.956  1.00 72.69  ? 60  GLU A OE1 1 
ATOM   115  O OE2 . GLU A 1 45  ? -20.125 10.748 21.229  1.00 67.15  ? 60  GLU A OE2 1 
ATOM   116  N N   . LYS A 1 46  ? -16.110 13.599 25.510  1.00 39.98  ? 61  LYS A N   1 
ATOM   117  C CA  . LYS A 1 46  ? -16.131 14.410 26.721  1.00 40.90  ? 61  LYS A CA  1 
ATOM   118  C C   . LYS A 1 46  ? -15.121 15.548 26.693  1.00 41.52  ? 61  LYS A C   1 
ATOM   119  O O   . LYS A 1 46  ? -15.199 16.441 27.543  1.00 34.75  ? 61  LYS A O   1 
ATOM   120  C CB  . LYS A 1 46  ? -15.893 13.534 27.952  1.00 38.68  ? 61  LYS A CB  1 
ATOM   121  C CG  . LYS A 1 46  ? -14.499 12.973 28.082  1.00 36.06  ? 61  LYS A CG  1 
ATOM   122  C CD  . LYS A 1 46  ? -14.302 12.372 29.469  1.00 37.61  ? 61  LYS A CD  1 
ATOM   123  C CE  . LYS A 1 46  ? -15.245 11.206 29.718  1.00 36.18  ? 61  LYS A CE  1 
ATOM   124  N NZ  . LYS A 1 46  ? -15.061 10.116 28.727  1.00 48.09  ? 61  LYS A NZ  1 
ATOM   125  N N   . TYR A 1 47  ? -14.187 15.549 25.747  1.00 41.40  ? 62  TYR A N   1 
ATOM   126  C CA  . TYR A 1 47  ? -13.240 16.645 25.624  1.00 39.31  ? 62  TYR A CA  1 
ATOM   127  C C   . TYR A 1 47  ? -13.659 17.651 24.568  1.00 38.76  ? 62  TYR A C   1 
ATOM   128  O O   . TYR A 1 47  ? -12.934 18.624 24.332  1.00 37.87  ? 62  TYR A O   1 
ATOM   129  C CB  . TYR A 1 47  ? -11.836 16.097 25.348  1.00 37.97  ? 62  TYR A CB  1 
ATOM   130  C CG  . TYR A 1 47  ? -11.413 15.151 26.441  1.00 37.68  ? 62  TYR A CG  1 
ATOM   131  C CD1 . TYR A 1 47  ? -11.075 15.634 27.704  1.00 35.21  ? 62  TYR A CD1 1 
ATOM   132  C CD2 . TYR A 1 47  ? -11.411 13.774 26.238  1.00 35.31  ? 62  TYR A CD2 1 
ATOM   133  C CE1 . TYR A 1 47  ? -10.713 14.775 28.727  1.00 33.37  ? 62  TYR A CE1 1 
ATOM   134  C CE2 . TYR A 1 47  ? -11.053 12.902 27.258  1.00 33.40  ? 62  TYR A CE2 1 
ATOM   135  C CZ  . TYR A 1 47  ? -10.704 13.409 28.499  1.00 37.65  ? 62  TYR A CZ  1 
ATOM   136  O OH  . TYR A 1 47  ? -10.342 12.551 29.517  1.00 36.54  ? 62  TYR A OH  1 
ATOM   137  N N   . ASP A 1 48  ? -14.825 17.445 23.949  1.00 38.18  ? 63  ASP A N   1 
ATOM   138  C CA  . ASP A 1 48  ? -15.447 18.425 23.058  1.00 37.98  ? 63  ASP A CA  1 
ATOM   139  C C   . ASP A 1 48  ? -16.240 19.399 23.921  1.00 37.34  ? 63  ASP A C   1 
ATOM   140  O O   . ASP A 1 48  ? -17.468 19.343 24.021  1.00 39.00  ? 63  ASP A O   1 
ATOM   141  C CB  . ASP A 1 48  ? -16.337 17.733 22.034  1.00 41.76  ? 63  ASP A CB  1 
ATOM   142  C CG  . ASP A 1 48  ? -16.925 18.699 21.014  1.00 44.24  ? 63  ASP A CG  1 
ATOM   143  O OD1 . ASP A 1 48  ? -16.791 19.934 21.181  1.00 41.69  ? 63  ASP A OD1 1 
ATOM   144  O OD2 . ASP A 1 48  ? -17.536 18.209 20.041  1.00 44.02  ? 63  ASP A OD2 1 
ATOM   145  N N   . ILE A 1 49  ? -15.511 20.328 24.539  1.00 35.77  ? 64  ILE A N   1 
ATOM   146  C CA  . ILE A 1 49  ? -16.095 21.207 25.546  1.00 36.36  ? 64  ILE A CA  1 
ATOM   147  C C   . ILE A 1 49  ? -17.182 22.097 24.953  1.00 38.25  ? 64  ILE A C   1 
ATOM   148  O O   . ILE A 1 49  ? -18.178 22.403 25.623  1.00 37.90  ? 64  ILE A O   1 
ATOM   149  C CB  . ILE A 1 49  ? -14.967 22.011 26.220  1.00 37.83  ? 64  ILE A CB  1 
ATOM   150  C CG1 . ILE A 1 49  ? -14.182 21.075 27.147  1.00 37.80  ? 64  ILE A CG1 1 
ATOM   151  C CG2 . ILE A 1 49  ? -15.520 23.207 26.993  1.00 32.73  ? 64  ILE A CG2 1 
ATOM   152  C CD1 . ILE A 1 49  ? -12.705 21.304 27.150  1.00 42.50  ? 64  ILE A CD1 1 
ATOM   153  N N   . GLU A 1 50  ? -17.035 22.500 23.689  1.00 42.78  ? 65  GLU A N   1 
ATOM   154  C CA  . GLU A 1 50  ? -18.088 23.276 23.041  1.00 43.38  ? 65  GLU A CA  1 
ATOM   155  C C   . GLU A 1 50  ? -19.406 22.510 23.019  1.00 41.61  ? 65  GLU A C   1 
ATOM   156  O O   . GLU A 1 50  ? -20.471 23.082 23.283  1.00 46.44  ? 65  GLU A O   1 
ATOM   157  C CB  . GLU A 1 50  ? -17.671 23.655 21.622  1.00 46.42  ? 65  GLU A CB  1 
ATOM   158  C CG  . GLU A 1 50  ? -18.259 24.969 21.143  1.00 53.22  ? 65  GLU A CG  1 
ATOM   159  C CD  . GLU A 1 50  ? -17.991 25.235 19.670  1.00 57.03  ? 65  GLU A CD  1 
ATOM   160  O OE1 . GLU A 1 50  ? -16.821 25.119 19.245  1.00 54.18  ? 65  GLU A OE1 1 
ATOM   161  O OE2 . GLU A 1 50  ? -18.949 25.579 18.945  1.00 60.58  ? 65  GLU A OE2 1 
ATOM   162  N N   . ARG A 1 51  ? -19.356 21.215 22.721  1.00 37.52  ? 66  ARG A N   1 
ATOM   163  C CA  . ARG A 1 51  ? -20.576 20.426 22.623  1.00 44.72  ? 66  ARG A CA  1 
ATOM   164  C C   . ARG A 1 51  ? -21.027 19.851 23.962  1.00 43.70  ? 66  ARG A C   1 
ATOM   165  O O   . ARG A 1 51  ? -22.234 19.748 24.204  1.00 41.19  ? 66  ARG A O   1 
ATOM   166  C CB  . ARG A 1 51  ? -20.386 19.290 21.612  1.00 43.49  ? 66  ARG A CB  1 
ATOM   167  C CG  . ARG A 1 51  ? -21.642 18.484 21.320  1.00 49.11  ? 66  ARG A CG  1 
ATOM   168  C CD  . ARG A 1 51  ? -21.433 17.565 20.121  1.00 60.21  ? 66  ARG A CD  1 
ATOM   169  N NE  . ARG A 1 51  ? -21.372 16.161 20.507  1.00 64.03  ? 66  ARG A NE  1 
ATOM   170  C CZ  . ARG A 1 51  ? -22.303 15.261 20.219  1.00 74.84  ? 66  ARG A CZ  1 
ATOM   171  N NH1 . ARG A 1 51  ? -23.383 15.580 19.524  1.00 76.46  ? 66  ARG A NH1 1 
ATOM   172  N NH2 . ARG A 1 51  ? -22.147 14.008 20.640  1.00 79.03  ? 66  ARG A NH2 1 
ATOM   173  N N   . THR A 1 52  ? -20.098 19.477 24.841  1.00 40.43  ? 67  THR A N   1 
ATOM   174  C CA  . THR A 1 52  ? -20.504 18.820 26.076  1.00 44.86  ? 67  THR A CA  1 
ATOM   175  C C   . THR A 1 52  ? -20.717 19.808 27.220  1.00 38.45  ? 67  THR A C   1 
ATOM   176  O O   . THR A 1 52  ? -21.619 19.610 28.041  1.00 39.38  ? 67  THR A O   1 
ATOM   177  C CB  . THR A 1 52  ? -19.477 17.749 26.477  1.00 43.91  ? 67  THR A CB  1 
ATOM   178  O OG1 . THR A 1 52  ? -19.971 17.010 27.602  1.00 44.22  ? 67  THR A OG1 1 
ATOM   179  C CG2 . THR A 1 52  ? -18.134 18.368 26.843  1.00 41.47  ? 67  THR A CG2 1 
ATOM   180  N N   . HIS A 1 53  ? -19.919 20.876 27.286  1.00 41.40  ? 68  HIS A N   1 
ATOM   181  C CA  . HIS A 1 53  ? -20.046 21.884 28.334  1.00 39.57  ? 68  HIS A CA  1 
ATOM   182  C C   . HIS A 1 53  ? -20.902 23.060 27.875  1.00 37.36  ? 68  HIS A C   1 
ATOM   183  O O   . HIS A 1 53  ? -21.843 23.449 28.573  1.00 32.13  ? 68  HIS A O   1 
ATOM   184  C CB  . HIS A 1 53  ? -18.656 22.359 28.769  1.00 34.83  ? 68  HIS A CB  1 
ATOM   185  C CG  . HIS A 1 53  ? -18.668 23.290 29.944  1.00 34.89  ? 68  HIS A CG  1 
ATOM   186  N ND1 . HIS A 1 53  ? -19.062 22.899 31.207  1.00 34.13  ? 68  HIS A ND1 1 
ATOM   187  C CD2 . HIS A 1 53  ? -18.316 24.594 30.047  1.00 32.80  ? 68  HIS A CD2 1 
ATOM   188  C CE1 . HIS A 1 53  ? -18.955 23.922 32.036  1.00 34.03  ? 68  HIS A CE1 1 
ATOM   189  N NE2 . HIS A 1 53  ? -18.509 24.964 31.356  1.00 39.39  ? 68  HIS A NE2 1 
ATOM   190  N N   . SER A 1 54  ? -20.575 23.632 26.710  1.00 38.07  ? 69  SER A N   1 
ATOM   191  C CA  . SER A 1 54  ? -21.402 24.597 25.982  1.00 39.67  ? 69  SER A CA  1 
ATOM   192  C C   . SER A 1 54  ? -21.524 25.949 26.677  1.00 38.53  ? 69  SER A C   1 
ATOM   193  O O   . SER A 1 54  ? -22.477 26.687 26.418  1.00 38.80  ? 69  SER A O   1 
ATOM   194  C CB  . SER A 1 54  ? -22.801 24.033 25.710  1.00 32.04  ? 69  SER A CB  1 
ATOM   195  O OG  . SER A 1 54  ? -22.723 22.671 25.332  1.00 46.19  ? 69  SER A OG  1 
ATOM   196  N N   . SER A 1 55  ? -20.588 26.304 27.553  1.00 36.30  ? 70  SER A N   1 
ATOM   197  C CA  . SER A 1 55  ? -20.617 27.607 28.204  1.00 34.16  ? 70  SER A CA  1 
ATOM   198  C C   . SER A 1 55  ? -19.200 27.964 28.632  1.00 35.10  ? 70  SER A C   1 
ATOM   199  O O   . SER A 1 55  ? -18.261 27.186 28.449  1.00 34.84  ? 70  SER A O   1 
ATOM   200  C CB  . SER A 1 55  ? -21.585 27.619 29.393  1.00 35.67  ? 70  SER A CB  1 
ATOM   201  O OG  . SER A 1 55  ? -21.954 28.946 29.742  1.00 37.32  ? 70  SER A OG  1 
ATOM   202  N N   . GLY A 1 56  ? -19.053 29.158 29.201  1.00 35.33  ? 71  GLY A N   1 
ATOM   203  C CA  . GLY A 1 56  ? -17.751 29.581 29.675  1.00 34.29  ? 71  GLY A CA  1 
ATOM   204  C C   . GLY A 1 56  ? -17.219 28.663 30.757  1.00 37.08  ? 71  GLY A C   1 
ATOM   205  O O   . GLY A 1 56  ? -17.971 28.031 31.502  1.00 35.67  ? 71  GLY A O   1 
ATOM   206  N N   . VAL A 1 57  ? -15.893 28.581 30.827  1.00 40.37  ? 72  VAL A N   1 
ATOM   207  C CA  . VAL A 1 57  ? -15.219 27.757 31.820  1.00 37.29  ? 72  VAL A CA  1 
ATOM   208  C C   . VAL A 1 57  ? -14.661 28.661 32.910  1.00 35.72  ? 72  VAL A C   1 
ATOM   209  O O   . VAL A 1 57  ? -15.071 28.567 34.071  1.00 33.62  ? 72  VAL A O   1 
ATOM   210  C CB  . VAL A 1 57  ? -14.109 26.901 31.179  1.00 42.06  ? 72  VAL A CB  1 
ATOM   211  C CG1 . VAL A 1 57  ? -13.278 26.207 32.262  1.00 35.44  ? 72  VAL A CG1 1 
ATOM   212  C CG2 . VAL A 1 57  ? -14.714 25.886 30.215  1.00 31.05  ? 72  VAL A CG2 1 
ATOM   213  N N   . ARG A 1 58  ? -13.726 29.546 32.548  1.00 34.16  ? 73  ARG A N   1 
ATOM   214  C CA  . ARG A 1 58  ? -13.153 30.458 33.535  1.00 37.63  ? 73  ARG A CA  1 
ATOM   215  C C   . ARG A 1 58  ? -14.235 31.336 34.153  1.00 39.76  ? 73  ARG A C   1 
ATOM   216  O O   . ARG A 1 58  ? -14.380 31.399 35.381  1.00 36.55  ? 73  ARG A O   1 
ATOM   217  C CB  . ARG A 1 58  ? -12.060 31.316 32.895  1.00 38.49  ? 73  ARG A CB  1 
ATOM   218  C CG  . ARG A 1 58  ? -11.122 31.958 33.908  1.00 41.16  ? 73  ARG A CG  1 
ATOM   219  C CD  . ARG A 1 58  ? -10.167 32.943 33.254  1.00 39.40  ? 73  ARG A CD  1 
ATOM   220  N NE  . ARG A 1 58  ? -10.814 34.226 33.015  1.00 49.00  ? 73  ARG A NE  1 
ATOM   221  C CZ  . ARG A 1 58  ? -10.624 35.311 33.753  1.00 52.01  ? 73  ARG A CZ  1 
ATOM   222  N NH1 . ARG A 1 58  ? -9.781  35.314 34.775  1.00 41.26  ? 73  ARG A NH1 1 
ATOM   223  N NH2 . ARG A 1 58  ? -11.295 36.420 33.458  1.00 54.29  ? 73  ARG A NH2 1 
ATOM   224  N N   . VAL A 1 59  ? -15.009 32.019 33.315  1.00 38.15  ? 74  VAL A N   1 
ATOM   225  C CA  . VAL A 1 59  ? -16.218 32.709 33.741  1.00 35.49  ? 74  VAL A CA  1 
ATOM   226  C C   . VAL A 1 59  ? -17.383 32.062 33.012  1.00 36.54  ? 74  VAL A C   1 
ATOM   227  O O   . VAL A 1 59  ? -17.408 32.031 31.775  1.00 39.38  ? 74  VAL A O   1 
ATOM   228  C CB  . VAL A 1 59  ? -16.164 34.217 33.456  1.00 39.77  ? 74  VAL A CB  1 
ATOM   229  C CG1 . VAL A 1 59  ? -17.497 34.860 33.807  1.00 36.75  ? 74  VAL A CG1 1 
ATOM   230  C CG2 . VAL A 1 59  ? -15.027 34.872 34.228  1.00 37.24  ? 74  VAL A CG2 1 
ATOM   231  N N   . ASP A 1 60  ? -18.336 31.537 33.773  1.00 34.67  ? 75  ASP A N   1 
ATOM   232  C CA  . ASP A 1 60  ? -19.522 30.885 33.228  1.00 35.53  ? 75  ASP A CA  1 
ATOM   233  C C   . ASP A 1 60  ? -20.715 31.789 33.505  1.00 38.31  ? 75  ASP A C   1 
ATOM   234  O O   . ASP A 1 60  ? -21.175 31.884 34.649  1.00 38.81  ? 75  ASP A O   1 
ATOM   235  C CB  . ASP A 1 60  ? -19.715 29.501 33.845  1.00 31.28  ? 75  ASP A CB  1 
ATOM   236  C CG  . ASP A 1 60  ? -20.875 28.737 33.229  1.00 37.59  ? 75  ASP A CG  1 
ATOM   237  O OD1 . ASP A 1 60  ? -21.613 29.311 32.398  1.00 36.20  ? 75  ASP A OD1 1 
ATOM   238  O OD2 . ASP A 1 60  ? -21.054 27.550 33.586  1.00 40.75  ? 75  ASP A OD2 1 
ATOM   239  N N   . LEU A 1 61  ? -21.207 32.455 32.462  1.00 34.12  ? 76  LEU A N   1 
ATOM   240  C CA  . LEU A 1 61  ? -22.409 33.281 32.543  1.00 36.34  ? 76  LEU A CA  1 
ATOM   241  C C   . LEU A 1 61  ? -23.206 33.131 31.252  1.00 42.23  ? 76  LEU A C   1 
ATOM   242  O O   . LEU A 1 61  ? -23.611 34.108 30.622  1.00 42.77  ? 76  LEU A O   1 
ATOM   243  C CB  . LEU A 1 61  ? -22.060 34.745 32.806  1.00 39.84  ? 76  LEU A CB  1 
ATOM   244  C CG  . LEU A 1 61  ? -21.445 35.080 34.167  1.00 41.23  ? 76  LEU A CG  1 
ATOM   245  C CD1 . LEU A 1 61  ? -20.870 36.492 34.171  1.00 34.96  ? 76  LEU A CD1 1 
ATOM   246  C CD2 . LEU A 1 61  ? -22.456 34.893 35.293  1.00 33.63  ? 76  LEU A CD2 1 
ATOM   247  N N   . GLY A 1 62  ? -23.437 31.884 30.849  1.00 37.83  ? 77  GLY A N   1 
ATOM   248  C CA  . GLY A 1 62  ? -23.981 31.570 29.546  1.00 40.40  ? 77  GLY A CA  1 
ATOM   249  C C   . GLY A 1 62  ? -25.486 31.569 29.410  1.00 45.01  ? 77  GLY A C   1 
ATOM   250  O O   . GLY A 1 62  ? -25.985 31.319 28.309  1.00 45.01  ? 77  GLY A O   1 
ATOM   251  N N   . GLU A 1 63  ? -26.234 31.829 30.481  1.00 41.63  ? 78  GLU A N   1 
ATOM   252  C CA  . GLU A 1 63  ? -27.685 31.876 30.414  1.00 36.65  ? 78  GLU A CA  1 
ATOM   253  C C   . GLU A 1 63  ? -28.193 33.184 31.001  1.00 39.75  ? 78  GLU A C   1 
ATOM   254  O O   . GLU A 1 63  ? -27.594 33.754 31.917  1.00 40.31  ? 78  GLU A O   1 
ATOM   255  C CB  . GLU A 1 63  ? -28.333 30.697 31.154  1.00 41.46  ? 78  GLU A CB  1 
ATOM   256  C CG  . GLU A 1 63  ? -28.923 29.636 30.235  1.00 38.28  ? 78  GLU A CG  1 
ATOM   257  C CD  . GLU A 1 63  ? -29.498 28.457 30.996  1.00 44.68  ? 78  GLU A CD  1 
ATOM   258  O OE1 . GLU A 1 63  ? -30.216 28.682 31.998  1.00 47.98  ? 78  GLU A OE1 1 
ATOM   259  O OE2 . GLU A 1 63  ? -29.228 27.303 30.596  1.00 40.63  ? 78  GLU A OE2 1 
ATOM   260  N N   . ASP A 1 64  ? -29.308 33.653 30.456  1.00 40.22  ? 79  ASP A N   1 
ATOM   261  C CA  . ASP A 1 64  ? -29.985 34.840 30.950  1.00 41.29  ? 79  ASP A CA  1 
ATOM   262  C C   . ASP A 1 64  ? -31.196 34.437 31.775  1.00 39.29  ? 79  ASP A C   1 
ATOM   263  O O   . ASP A 1 64  ? -31.794 33.380 31.561  1.00 42.07  ? 79  ASP A O   1 
ATOM   264  C CB  . ASP A 1 64  ? -30.420 35.743 29.797  1.00 40.74  ? 79  ASP A CB  1 
ATOM   265  C CG  . ASP A 1 64  ? -29.256 36.186 28.939  1.00 43.86  ? 79  ASP A CG  1 
ATOM   266  O OD1 . ASP A 1 64  ? -28.414 36.965 29.429  1.00 48.83  ? 79  ASP A OD1 1 
ATOM   267  O OD2 . ASP A 1 64  ? -29.179 35.746 27.776  1.00 50.82  ? 79  ASP A OD2 1 
ATOM   268  N N   . ALA A 1 65  ? -31.545 35.287 32.734  1.00 39.10  ? 80  ALA A N   1 
ATOM   269  C CA  . ALA A 1 65  ? -32.695 35.033 33.585  1.00 38.99  ? 80  ALA A CA  1 
ATOM   270  C C   . ALA A 1 65  ? -33.274 36.363 34.027  1.00 42.38  ? 80  ALA A C   1 
ATOM   271  O O   . ALA A 1 65  ? -32.532 37.298 34.339  1.00 42.12  ? 80  ALA A O   1 
ATOM   272  C CB  . ALA A 1 65  ? -32.323 34.186 34.807  1.00 44.34  ? 80  ALA A CB  1 
ATOM   273  N N   . GLU A 1 66  ? -34.598 36.445 34.034  1.00 42.76  ? 81  GLU A N   1 
ATOM   274  C CA  . GLU A 1 66  ? -35.304 37.590 34.585  1.00 47.87  ? 81  GLU A CA  1 
ATOM   275  C C   . GLU A 1 66  ? -35.945 37.185 35.905  1.00 45.89  ? 81  GLU A C   1 
ATOM   276  O O   . GLU A 1 66  ? -36.558 36.117 36.004  1.00 45.47  ? 81  GLU A O   1 
ATOM   277  C CB  . GLU A 1 66  ? -36.354 38.121 33.608  1.00 45.43  ? 81  GLU A CB  1 
ATOM   278  C CG  . GLU A 1 66  ? -36.175 39.597 33.296  1.00 58.07  ? 81  GLU A CG  1 
ATOM   279  C CD  . GLU A 1 66  ? -37.182 40.116 32.292  1.00 70.03  ? 81  GLU A CD  1 
ATOM   280  O OE1 . GLU A 1 66  ? -36.787 40.317 31.121  1.00 72.86  ? 81  GLU A OE1 1 
ATOM   281  O OE2 . GLU A 1 66  ? -38.358 40.324 32.673  1.00 63.55  ? 81  GLU A OE2 1 
ATOM   282  N N   . VAL A 1 67  ? -35.774 38.022 36.921  1.00 45.24  ? 82  VAL A N   1 
ATOM   283  C CA  . VAL A 1 67  ? -36.364 37.805 38.235  1.00 48.75  ? 82  VAL A CA  1 
ATOM   284  C C   . VAL A 1 67  ? -36.999 39.122 38.647  1.00 45.93  ? 82  VAL A C   1 
ATOM   285  O O   . VAL A 1 67  ? -36.289 40.102 38.905  1.00 42.98  ? 82  VAL A O   1 
ATOM   286  C CB  . VAL A 1 67  ? -35.331 37.347 39.275  1.00 51.49  ? 82  VAL A CB  1 
ATOM   287  C CG1 . VAL A 1 67  ? -35.916 37.429 40.678  1.00 51.17  ? 82  VAL A CG1 1 
ATOM   288  C CG2 . VAL A 1 67  ? -34.853 35.942 38.972  1.00 45.41  ? 82  VAL A CG2 1 
ATOM   289  N N   . GLU A 1 68  ? -38.330 39.154 38.690  1.00 52.68  ? 83  GLU A N   1 
ATOM   290  C CA  . GLU A 1 68  ? -39.078 40.337 39.105  1.00 49.69  ? 83  GLU A CA  1 
ATOM   291  C C   . GLU A 1 68  ? -38.649 41.562 38.303  1.00 50.66  ? 83  GLU A C   1 
ATOM   292  O O   . GLU A 1 68  ? -38.339 42.623 38.850  1.00 48.91  ? 83  GLU A O   1 
ATOM   293  C CB  . GLU A 1 68  ? -38.924 40.575 40.609  1.00 48.69  ? 83  GLU A CB  1 
ATOM   294  C CG  . GLU A 1 68  ? -39.765 39.633 41.462  1.00 53.54  ? 83  GLU A CG  1 
ATOM   295  C CD  . GLU A 1 68  ? -39.435 39.721 42.941  1.00 52.04  ? 83  GLU A CD  1 
ATOM   296  O OE1 . GLU A 1 68  ? -38.389 39.185 43.362  1.00 52.81  ? 83  GLU A OE1 1 
ATOM   297  O OE2 . GLU A 1 68  ? -40.224 40.333 43.685  1.00 56.76  ? 83  GLU A OE2 1 
ATOM   298  N N   . ASN A 1 69  ? -38.603 41.389 36.981  1.00 51.90  ? 84  ASN A N   1 
ATOM   299  C CA  . ASN A 1 69  ? -38.338 42.436 35.994  1.00 55.13  ? 84  ASN A CA  1 
ATOM   300  C C   . ASN A 1 69  ? -36.905 42.952 36.024  1.00 54.08  ? 84  ASN A C   1 
ATOM   301  O O   . ASN A 1 69  ? -36.618 43.988 35.409  1.00 57.90  ? 84  ASN A O   1 
ATOM   302  C CB  . ASN A 1 69  ? -39.308 43.616 36.149  1.00 56.27  ? 84  ASN A CB  1 
ATOM   303  C CG  . ASN A 1 69  ? -40.757 43.197 35.993  1.00 60.61  ? 84  ASN A CG  1 
ATOM   304  O OD1 . ASN A 1 69  ? -41.049 42.049 35.654  1.00 63.45  ? 84  ASN A OD1 1 
ATOM   305  N ND2 . ASN A 1 69  ? -41.675 44.120 36.262  1.00 66.26  ? 84  ASN A ND2 1 
ATOM   306  N N   . ALA A 1 70  ? -35.996 42.273 36.716  1.00 51.29  ? 85  ALA A N   1 
ATOM   307  C CA  . ALA A 1 70  ? -34.574 42.571 36.649  1.00 44.59  ? 85  ALA A CA  1 
ATOM   308  C C   . ALA A 1 70  ? -33.867 41.462 35.883  1.00 43.35  ? 85  ALA A C   1 
ATOM   309  O O   . ALA A 1 70  ? -34.284 40.299 35.916  1.00 45.66  ? 85  ALA A O   1 
ATOM   310  C CB  . ALA A 1 70  ? -33.964 42.720 38.045  1.00 41.55  ? 85  ALA A CB  1 
ATOM   311  N N   . LYS A 1 71  ? -32.800 41.828 35.184  1.00 40.62  ? 86  LYS A N   1 
ATOM   312  C CA  . LYS A 1 71  ? -32.094 40.906 34.305  1.00 43.47  ? 86  LYS A CA  1 
ATOM   313  C C   . LYS A 1 71  ? -30.823 40.400 34.974  1.00 40.83  ? 86  LYS A C   1 
ATOM   314  O O   . LYS A 1 71  ? -30.042 41.184 35.529  1.00 40.19  ? 86  LYS A O   1 
ATOM   315  C CB  . LYS A 1 71  ? -31.774 41.575 32.968  1.00 42.82  ? 86  LYS A CB  1 
ATOM   316  C CG  . LYS A 1 71  ? -33.007 41.751 32.084  1.00 52.72  ? 86  LYS A CG  1 
ATOM   317  C CD  . LYS A 1 71  ? -32.672 42.490 30.801  1.00 60.49  ? 86  LYS A CD  1 
ATOM   318  N N   . TYR A 1 72  ? -30.621 39.088 34.917  1.00 38.12  ? 87  TYR A N   1 
ATOM   319  C CA  . TYR A 1 72  ? -29.462 38.450 35.514  1.00 35.16  ? 87  TYR A CA  1 
ATOM   320  C C   . TYR A 1 72  ? -28.774 37.569 34.481  1.00 36.51  ? 87  TYR A C   1 
ATOM   321  O O   . TYR A 1 72  ? -29.378 37.136 33.498  1.00 40.16  ? 87  TYR A O   1 
ATOM   322  C CB  . TYR A 1 72  ? -29.860 37.621 36.744  1.00 34.94  ? 87  TYR A CB  1 
ATOM   323  C CG  . TYR A 1 72  ? -30.541 38.435 37.826  1.00 35.76  ? 87  TYR A CG  1 
ATOM   324  C CD1 . TYR A 1 72  ? -31.904 38.721 37.756  1.00 41.16  ? 87  TYR A CD1 1 
ATOM   325  C CD2 . TYR A 1 72  ? -29.821 38.929 38.907  1.00 31.83  ? 87  TYR A CD2 1 
ATOM   326  C CE1 . TYR A 1 72  ? -32.532 39.468 38.736  1.00 42.19  ? 87  TYR A CE1 1 
ATOM   327  C CE2 . TYR A 1 72  ? -30.440 39.681 39.896  1.00 36.58  ? 87  TYR A CE2 1 
ATOM   328  C CZ  . TYR A 1 72  ? -31.795 39.947 39.804  1.00 41.22  ? 87  TYR A CZ  1 
ATOM   329  O OH  . TYR A 1 72  ? -32.419 40.691 40.780  1.00 41.08  ? 87  TYR A OH  1 
ATOM   330  N N   . ARG A 1 73  ? -27.488 37.327 34.709  1.00 42.00  ? 88  ARG A N   1 
ATOM   331  C CA  . ARG A 1 73  ? -26.714 36.340 33.971  1.00 41.41  ? 88  ARG A CA  1 
ATOM   332  C C   . ARG A 1 73  ? -26.224 35.300 34.965  1.00 40.98  ? 88  ARG A C   1 
ATOM   333  O O   . ARG A 1 73  ? -25.771 35.647 36.061  1.00 42.51  ? 88  ARG A O   1 
ATOM   334  C CB  . ARG A 1 73  ? -25.526 36.977 33.234  1.00 44.11  ? 88  ARG A CB  1 
ATOM   335  C CG  . ARG A 1 73  ? -25.924 38.007 32.186  1.00 52.52  ? 88  ARG A CG  1 
ATOM   336  C CD  . ARG A 1 73  ? -25.304 37.706 30.827  1.00 55.89  ? 88  ARG A CD  1 
ATOM   337  N NE  . ARG A 1 73  ? -23.857 37.527 30.897  1.00 62.27  ? 88  ARG A NE  1 
ATOM   338  C CZ  . ARG A 1 73  ? -23.107 37.086 29.894  1.00 58.50  ? 88  ARG A CZ  1 
ATOM   339  N NH1 . ARG A 1 73  ? -23.633 36.785 28.718  1.00 61.75  ? 88  ARG A NH1 1 
ATOM   340  N NH2 . ARG A 1 73  ? -21.796 36.945 30.074  1.00 53.87  ? 88  ARG A NH2 1 
ATOM   341  N N   . ILE A 1 74  ? -26.328 34.027 34.592  1.00 39.93  ? 89  ILE A N   1 
ATOM   342  C CA  . ILE A 1 74  ? -26.056 32.939 35.531  1.00 40.12  ? 89  ILE A CA  1 
ATOM   343  C C   . ILE A 1 74  ? -25.308 31.828 34.821  1.00 43.44  ? 89  ILE A C   1 
ATOM   344  O O   . ILE A 1 74  ? -25.417 31.643 33.597  1.00 35.93  ? 89  ILE A O   1 
ATOM   345  C CB  . ILE A 1 74  ? -27.354 32.381 36.147  1.00 46.02  ? 89  ILE A CB  1 
ATOM   346  C CG1 . ILE A 1 74  ? -28.336 31.987 35.045  1.00 40.62  ? 89  ILE A CG1 1 
ATOM   347  C CG2 . ILE A 1 74  ? -27.979 33.399 37.106  1.00 45.10  ? 89  ILE A CG2 1 
ATOM   348  C CD1 . ILE A 1 74  ? -29.374 31.006 35.511  1.00 44.03  ? 89  ILE A CD1 1 
ATOM   349  N N   . PRO A 1 75  ? -24.526 31.056 35.578  1.00 36.12  ? 90  PRO A N   1 
ATOM   350  C CA  . PRO A 1 75  ? -23.748 29.972 34.969  1.00 33.29  ? 90  PRO A CA  1 
ATOM   351  C C   . PRO A 1 75  ? -24.652 28.899 34.389  1.00 37.51  ? 90  PRO A C   1 
ATOM   352  O O   . PRO A 1 75  ? -25.724 28.597 34.923  1.00 37.52  ? 90  PRO A O   1 
ATOM   353  C CB  . PRO A 1 75  ? -22.916 29.425 36.136  1.00 37.02  ? 90  PRO A CB  1 
ATOM   354  C CG  . PRO A 1 75  ? -22.931 30.501 37.175  1.00 36.59  ? 90  PRO A CG  1 
ATOM   355  C CD  . PRO A 1 75  ? -24.244 31.202 37.016  1.00 34.20  ? 90  PRO A CD  1 
ATOM   356  N N   . ALA A 1 76  ? -24.197 28.310 33.282  1.00 34.58  ? 91  ALA A N   1 
ATOM   357  C CA  . ALA A 1 76  ? -25.009 27.346 32.555  1.00 35.93  ? 91  ALA A CA  1 
ATOM   358  C C   . ALA A 1 76  ? -24.226 26.181 31.964  1.00 34.99  ? 91  ALA A C   1 
ATOM   359  O O   . ALA A 1 76  ? -24.835 25.328 31.309  1.00 31.77  ? 91  ALA A O   1 
ATOM   360  C CB  . ALA A 1 76  ? -25.785 28.055 31.430  1.00 36.38  ? 91  ALA A CB  1 
ATOM   361  N N   . GLY A 1 77  ? -22.912 26.109 32.170  1.00 35.75  ? 92  GLY A N   1 
ATOM   362  C CA  . GLY A 1 77  ? -22.151 25.001 31.619  1.00 34.03  ? 92  GLY A CA  1 
ATOM   363  C C   . GLY A 1 77  ? -22.625 23.670 32.176  1.00 34.32  ? 92  GLY A C   1 
ATOM   364  O O   . GLY A 1 77  ? -22.989 23.558 33.349  1.00 37.23  ? 92  GLY A O   1 
ATOM   365  N N   . ARG A 1 78  ? -22.617 22.652 31.323  1.00 32.52  ? 93  ARG A N   1 
ATOM   366  C CA  . ARG A 1 78  ? -23.160 21.348 31.684  1.00 38.13  ? 93  ARG A CA  1 
ATOM   367  C C   . ARG A 1 78  ? -22.125 20.420 32.316  1.00 40.32  ? 93  ARG A C   1 
ATOM   368  O O   . ARG A 1 78  ? -22.475 19.309 32.732  1.00 34.57  ? 93  ARG A O   1 
ATOM   369  C CB  . ARG A 1 78  ? -23.784 20.691 30.450  1.00 35.24  ? 93  ARG A CB  1 
ATOM   370  C CG  . ARG A 1 78  ? -24.699 21.635 29.668  1.00 41.41  ? 93  ARG A CG  1 
ATOM   371  C CD  . ARG A 1 78  ? -25.829 20.889 28.990  1.00 44.07  ? 93  ARG A CD  1 
ATOM   372  N NE  . ARG A 1 78  ? -26.442 19.941 29.911  1.00 56.45  ? 93  ARG A NE  1 
ATOM   373  C CZ  . ARG A 1 78  ? -27.585 20.143 30.554  1.00 60.97  ? 93  ARG A CZ  1 
ATOM   374  N NH1 . ARG A 1 78  ? -28.301 21.244 30.367  1.00 60.90  ? 93  ARG A NH1 1 
ATOM   375  N NH2 . ARG A 1 78  ? -28.021 19.217 31.407  1.00 51.15  ? 93  ARG A NH2 1 
ATOM   376  N N   . CYS A 1 79  ? -20.875 20.846 32.406  1.00 34.23  ? 94  CYS A N   1 
ATOM   377  C CA  . CYS A 1 79  ? -19.861 20.041 33.055  1.00 34.82  ? 94  CYS A CA  1 
ATOM   378  C C   . CYS A 1 79  ? -19.365 20.730 34.320  1.00 34.90  ? 94  CYS A C   1 
ATOM   379  O O   . CYS A 1 79  ? -19.391 21.961 34.419  1.00 34.66  ? 94  CYS A O   1 
ATOM   380  C CB  . CYS A 1 79  ? -18.676 19.786 32.116  1.00 36.02  ? 94  CYS A CB  1 
ATOM   381  S SG  . CYS A 1 79  ? -19.047 18.614 30.791  1.00 42.15  ? 94  CYS A SG  1 
ATOM   382  N N   . PRO A 1 80  ? -18.924 19.969 35.311  1.00 36.24  ? 95  PRO A N   1 
ATOM   383  C CA  . PRO A 1 80  ? -18.334 20.580 36.502  1.00 34.49  ? 95  PRO A CA  1 
ATOM   384  C C   . PRO A 1 80  ? -16.922 21.066 36.216  1.00 35.40  ? 95  PRO A C   1 
ATOM   385  O O   . PRO A 1 80  ? -16.246 20.597 35.299  1.00 38.75  ? 95  PRO A O   1 
ATOM   386  C CB  . PRO A 1 80  ? -18.332 19.437 37.521  1.00 31.34  ? 95  PRO A CB  1 
ATOM   387  C CG  . PRO A 1 80  ? -18.227 18.201 36.697  1.00 30.59  ? 95  PRO A CG  1 
ATOM   388  C CD  . PRO A 1 80  ? -18.904 18.495 35.372  1.00 35.90  ? 95  PRO A CD  1 
ATOM   389  N N   . VAL A 1 81  ? -16.483 22.031 37.019  1.00 30.84  ? 96  VAL A N   1 
ATOM   390  C CA  . VAL A 1 81  ? -15.144 22.602 36.891  1.00 34.68  ? 96  VAL A CA  1 
ATOM   391  C C   . VAL A 1 81  ? -14.391 22.277 38.175  1.00 31.95  ? 96  VAL A C   1 
ATOM   392  O O   . VAL A 1 81  ? -14.581 22.935 39.204  1.00 32.66  ? 96  VAL A O   1 
ATOM   393  C CB  . VAL A 1 81  ? -15.174 24.112 36.630  1.00 33.77  ? 96  VAL A CB  1 
ATOM   394  C CG1 . VAL A 1 81  ? -13.762 24.629 36.401  1.00 33.39  ? 96  VAL A CG1 1 
ATOM   395  C CG2 . VAL A 1 81  ? -16.062 24.424 35.438  1.00 30.84  ? 96  VAL A CG2 1 
ATOM   396  N N   . PHE A 1 82  ? -13.528 21.267 38.118  1.00 32.52  ? 97  PHE A N   1 
ATOM   397  C CA  . PHE A 1 82  ? -12.809 20.827 39.304  1.00 30.41  ? 97  PHE A CA  1 
ATOM   398  C C   . PHE A 1 82  ? -11.697 21.807 39.647  1.00 36.52  ? 97  PHE A C   1 
ATOM   399  O O   . PHE A 1 82  ? -10.892 22.177 38.787  1.00 36.54  ? 97  PHE A O   1 
ATOM   400  C CB  . PHE A 1 82  ? -12.231 19.431 39.081  1.00 33.76  ? 97  PHE A CB  1 
ATOM   401  C CG  . PHE A 1 82  ? -13.273 18.382 38.842  1.00 33.40  ? 97  PHE A CG  1 
ATOM   402  C CD1 . PHE A 1 82  ? -13.873 17.731 39.910  1.00 31.95  ? 97  PHE A CD1 1 
ATOM   403  C CD2 . PHE A 1 82  ? -13.666 18.056 37.549  1.00 30.73  ? 97  PHE A CD2 1 
ATOM   404  C CE1 . PHE A 1 82  ? -14.846 16.766 39.694  1.00 33.89  ? 97  PHE A CE1 1 
ATOM   405  C CE2 . PHE A 1 82  ? -14.636 17.094 37.323  1.00 32.06  ? 97  PHE A CE2 1 
ATOM   406  C CZ  . PHE A 1 82  ? -15.228 16.445 38.396  1.00 32.76  ? 97  PHE A CZ  1 
ATOM   407  N N   . GLY A 1 83  ? -11.651 22.224 40.910  1.00 33.15  ? 98  GLY A N   1 
ATOM   408  C CA  . GLY A 1 83  ? -10.585 23.072 41.392  1.00 31.34  ? 98  GLY A CA  1 
ATOM   409  C C   . GLY A 1 83  ? -10.782 24.555 41.187  1.00 33.86  ? 98  GLY A C   1 
ATOM   410  O O   . GLY A 1 83  ? -9.833  25.321 41.394  1.00 34.19  ? 98  GLY A O   1 
ATOM   411  N N   . LYS A 1 84  ? -11.973 24.990 40.787  1.00 31.25  ? 99  LYS A N   1 
ATOM   412  C CA  . LYS A 1 84  ? -12.244 26.406 40.594  1.00 32.91  ? 99  LYS A CA  1 
ATOM   413  C C   . LYS A 1 84  ? -12.846 27.019 41.850  1.00 34.18  ? 99  LYS A C   1 
ATOM   414  O O   . LYS A 1 84  ? -13.738 26.443 42.479  1.00 34.80  ? 99  LYS A O   1 
ATOM   415  C CB  . LYS A 1 84  ? -13.196 26.625 39.417  1.00 31.83  ? 99  LYS A CB  1 
ATOM   416  C CG  . LYS A 1 84  ? -13.747 28.047 39.313  1.00 26.74  ? 99  LYS A CG  1 
ATOM   417  C CD  . LYS A 1 84  ? -14.693 28.174 38.127  1.00 34.04  ? 99  LYS A CD  1 
ATOM   418  C CE  . LYS A 1 84  ? -15.650 29.342 38.281  1.00 29.34  ? 99  LYS A CE  1 
ATOM   419  N NZ  . LYS A 1 84  ? -16.192 29.748 36.955  1.00 36.26  ? 99  LYS A NZ  1 
ATOM   420  N N   . GLY A 1 85  ? -12.354 28.196 42.204  1.00 32.97  ? 100 GLY A N   1 
ATOM   421  C CA  . GLY A 1 85  ? -13.008 29.010 43.202  1.00 33.73  ? 100 GLY A CA  1 
ATOM   422  C C   . GLY A 1 85  ? -12.884 30.465 42.817  1.00 35.43  ? 100 GLY A C   1 
ATOM   423  O O   . GLY A 1 85  ? -12.441 30.783 41.707  1.00 33.82  ? 100 GLY A O   1 
ATOM   424  N N   . ILE A 1 86  ? -13.265 31.362 43.718  1.00 33.37  ? 101 ILE A N   1 
ATOM   425  C CA  . ILE A 1 86  ? -13.109 32.793 43.500  1.00 36.53  ? 101 ILE A CA  1 
ATOM   426  C C   . ILE A 1 86  ? -12.113 33.319 44.523  1.00 36.29  ? 101 ILE A C   1 
ATOM   427  O O   . ILE A 1 86  ? -12.329 33.204 45.737  1.00 32.27  ? 101 ILE A O   1 
ATOM   428  C CB  . ILE A 1 86  ? -14.452 33.532 43.582  1.00 34.46  ? 101 ILE A CB  1 
ATOM   429  C CG1 . ILE A 1 86  ? -15.422 32.957 42.546  1.00 33.73  ? 101 ILE A CG1 1 
ATOM   430  C CG2 . ILE A 1 86  ? -14.244 35.025 43.344  1.00 35.46  ? 101 ILE A CG2 1 
ATOM   431  C CD1 . ILE A 1 86  ? -16.821 33.518 42.647  1.00 37.36  ? 101 ILE A CD1 1 
ATOM   432  N N   . VAL A 1 87  ? -11.008 33.868 44.031  1.00 37.63  ? 102 VAL A N   1 
ATOM   433  C CA  . VAL A 1 87  ? -10.033 34.540 44.879  1.00 37.63  ? 102 VAL A CA  1 
ATOM   434  C C   . VAL A 1 87  ? -10.482 35.984 45.038  1.00 32.84  ? 102 VAL A C   1 
ATOM   435  O O   . VAL A 1 87  ? -10.694 36.684 44.042  1.00 32.68  ? 102 VAL A O   1 
ATOM   436  C CB  . VAL A 1 87  ? -8.619  34.465 44.282  1.00 35.01  ? 102 VAL A CB  1 
ATOM   437  C CG1 . VAL A 1 87  ? -7.682  35.428 45.016  1.00 33.05  ? 102 VAL A CG1 1 
ATOM   438  C CG2 . VAL A 1 87  ? -8.092  33.041 44.354  1.00 34.04  ? 102 VAL A CG2 1 
ATOM   439  N N   . ILE A 1 88  ? -10.659 36.420 46.282  1.00 29.17  ? 103 ILE A N   1 
ATOM   440  C CA  . ILE A 1 88  ? -10.912 37.824 46.587  1.00 36.61  ? 103 ILE A CA  1 
ATOM   441  C C   . ILE A 1 88  ? -9.574  38.468 46.924  1.00 39.65  ? 103 ILE A C   1 
ATOM   442  O O   . ILE A 1 88  ? -8.926  38.094 47.910  1.00 39.51  ? 103 ILE A O   1 
ATOM   443  C CB  . ILE A 1 88  ? -11.918 37.989 47.737  1.00 42.30  ? 103 ILE A CB  1 
ATOM   444  C CG1 . ILE A 1 88  ? -13.239 37.286 47.405  1.00 36.23  ? 103 ILE A CG1 1 
ATOM   445  C CG2 . ILE A 1 88  ? -12.164 39.471 48.017  1.00 36.56  ? 103 ILE A CG2 1 
ATOM   446  C CD1 . ILE A 1 88  ? -13.862 36.604 48.582  1.00 33.86  ? 103 ILE A CD1 1 
ATOM   447  N N   . GLU A 1 89  ? -9.151  39.422 46.101  1.00 40.61  ? 104 GLU A N   1 
ATOM   448  C CA  . GLU A 1 89  ? -7.867  40.066 46.324  1.00 45.43  ? 104 GLU A CA  1 
ATOM   449  C C   . GLU A 1 89  ? -7.917  40.924 47.581  1.00 45.99  ? 104 GLU A C   1 
ATOM   450  O O   . GLU A 1 89  ? -8.969  41.445 47.964  1.00 44.93  ? 104 GLU A O   1 
ATOM   451  C CB  . GLU A 1 89  ? -7.476  40.916 45.117  1.00 46.85  ? 104 GLU A CB  1 
ATOM   452  C CG  . GLU A 1 89  ? -7.558  40.165 43.800  1.00 53.80  ? 104 GLU A CG  1 
ATOM   453  C CD  . GLU A 1 89  ? -6.258  40.205 43.029  1.00 64.22  ? 104 GLU A CD  1 
ATOM   454  O OE1 . GLU A 1 89  ? -5.938  41.276 42.467  1.00 66.17  ? 104 GLU A OE1 1 
ATOM   455  O OE2 . GLU A 1 89  ? -5.558  39.169 42.989  1.00 67.14  ? 104 GLU A OE2 1 
ATOM   456  N N   . ASN A 1 90  ? -6.760  41.053 48.230  1.00 38.26  ? 105 ASN A N   1 
ATOM   457  C CA  . ASN A 1 90  ? -6.636  41.833 49.461  1.00 45.40  ? 105 ASN A CA  1 
ATOM   458  C C   . ASN A 1 90  ? -7.623  41.348 50.521  1.00 42.77  ? 105 ASN A C   1 
ATOM   459  O O   . ASN A 1 90  ? -8.188  42.137 51.282  1.00 47.69  ? 105 ASN A O   1 
ATOM   460  C CB  . ASN A 1 90  ? -6.809  43.329 49.186  1.00 50.23  ? 105 ASN A CB  1 
ATOM   461  C CG  . ASN A 1 90  ? -5.863  43.835 48.110  1.00 55.30  ? 105 ASN A CG  1 
ATOM   462  O OD1 . ASN A 1 90  ? -4.647  43.664 48.203  1.00 50.24  ? 105 ASN A OD1 1 
ATOM   463  N ND2 . ASN A 1 90  ? -6.422  44.448 47.073  1.00 58.85  ? 105 ASN A ND2 1 
ATOM   464  N N   . SER A 1 91  ? -7.831  40.035 50.574  1.00 37.65  ? 106 SER A N   1 
ATOM   465  C CA  . SER A 1 91  ? -8.733  39.448 51.552  1.00 43.69  ? 106 SER A CA  1 
ATOM   466  C C   . SER A 1 91  ? -8.292  38.024 51.851  1.00 35.32  ? 106 SER A C   1 
ATOM   467  O O   . SER A 1 91  ? -7.978  37.261 50.935  1.00 40.32  ? 106 SER A O   1 
ATOM   468  C CB  . SER A 1 91  ? -10.185 39.453 51.054  1.00 39.42  ? 106 SER A CB  1 
ATOM   469  O OG  . SER A 1 91  ? -10.999 38.651 51.891  1.00 41.09  ? 106 SER A OG  1 
ATOM   470  N N   . ALA A 1 92  ? -8.274  37.675 53.134  1.00 32.65  ? 107 ALA A N   1 
ATOM   471  C CA  . ALA A 1 92  ? -8.038  36.305 53.566  1.00 40.53  ? 107 ALA A CA  1 
ATOM   472  C C   . ALA A 1 92  ? -9.326  35.498 53.703  1.00 36.98  ? 107 ALA A C   1 
ATOM   473  O O   . ALA A 1 92  ? -9.266  34.300 54.003  1.00 32.34  ? 107 ALA A O   1 
ATOM   474  C CB  . ALA A 1 92  ? -7.279  36.301 54.897  1.00 35.78  ? 107 ALA A CB  1 
ATOM   475  N N   . VAL A 1 93  ? -10.479 36.119 53.483  1.00 35.58  ? 108 VAL A N   1 
ATOM   476  C CA  . VAL A 1 93  ? -11.758 35.446 53.668  1.00 36.40  ? 108 VAL A CA  1 
ATOM   477  C C   . VAL A 1 93  ? -12.026 34.541 52.477  1.00 34.97  ? 108 VAL A C   1 
ATOM   478  O O   . VAL A 1 93  ? -11.829 34.935 51.322  1.00 36.82  ? 108 VAL A O   1 
ATOM   479  C CB  . VAL A 1 93  ? -12.889 36.474 53.856  1.00 37.80  ? 108 VAL A CB  1 
ATOM   480  C CG1 . VAL A 1 93  ? -14.234 35.769 54.024  1.00 30.04  ? 108 VAL A CG1 1 
ATOM   481  C CG2 . VAL A 1 93  ? -12.596 37.378 55.047  1.00 28.64  ? 108 VAL A CG2 1 
ATOM   482  N N   . SER A 1 94  ? -12.469 33.319 52.761  1.00 29.82  ? 109 SER A N   1 
ATOM   483  C CA  . SER A 1 94  ? -12.807 32.368 51.714  1.00 32.20  ? 109 SER A CA  1 
ATOM   484  C C   . SER A 1 94  ? -14.118 32.749 51.037  1.00 36.03  ? 109 SER A C   1 
ATOM   485  O O   . SER A 1 94  ? -15.087 33.140 51.695  1.00 37.26  ? 109 SER A O   1 
ATOM   486  C CB  . SER A 1 94  ? -12.910 30.962 52.304  1.00 32.91  ? 109 SER A CB  1 
ATOM   487  O OG  . SER A 1 94  ? -13.851 30.185 51.592  1.00 35.76  ? 109 SER A OG  1 
ATOM   488  N N   . PHE A 1 95  ? -14.150 32.626 49.706  1.00 36.01  ? 110 PHE A N   1 
ATOM   489  C CA  . PHE A 1 95  ? -15.362 32.928 48.951  1.00 32.41  ? 110 PHE A CA  1 
ATOM   490  C C   . PHE A 1 95  ? -16.520 31.993 49.290  1.00 33.38  ? 110 PHE A C   1 
ATOM   491  O O   . PHE A 1 95  ? -17.651 32.253 48.859  1.00 32.69  ? 110 PHE A O   1 
ATOM   492  C CB  . PHE A 1 95  ? -15.065 32.878 47.448  1.00 33.73  ? 110 PHE A CB  1 
ATOM   493  C CG  . PHE A 1 95  ? -15.256 31.518 46.832  1.00 34.82  ? 110 PHE A CG  1 
ATOM   494  C CD1 . PHE A 1 95  ? -14.347 30.499 47.075  1.00 34.65  ? 110 PHE A CD1 1 
ATOM   495  C CD2 . PHE A 1 95  ? -16.347 31.259 46.011  1.00 30.82  ? 110 PHE A CD2 1 
ATOM   496  C CE1 . PHE A 1 95  ? -14.524 29.244 46.507  1.00 36.93  ? 110 PHE A CE1 1 
ATOM   497  C CE2 . PHE A 1 95  ? -16.529 30.013 45.437  1.00 31.05  ? 110 PHE A CE2 1 
ATOM   498  C CZ  . PHE A 1 95  ? -15.619 29.001 45.684  1.00 29.99  ? 110 PHE A CZ  1 
ATOM   499  N N   . LEU A 1 96  ? -16.274 30.923 50.043  1.00 32.02  ? 111 LEU A N   1 
ATOM   500  C CA  . LEU A 1 96  ? -17.348 30.064 50.522  1.00 34.27  ? 111 LEU A CA  1 
ATOM   501  C C   . LEU A 1 96  ? -17.976 30.568 51.819  1.00 30.51  ? 111 LEU A C   1 
ATOM   502  O O   . LEU A 1 96  ? -18.972 29.995 52.268  1.00 27.02  ? 111 LEU A O   1 
ATOM   503  C CB  . LEU A 1 96  ? -16.834 28.629 50.711  1.00 30.84  ? 111 LEU A CB  1 
ATOM   504  C CG  . LEU A 1 96  ? -16.486 27.848 49.438  1.00 32.24  ? 111 LEU A CG  1 
ATOM   505  C CD1 . LEU A 1 96  ? -16.099 26.409 49.756  1.00 26.77  ? 111 LEU A CD1 1 
ATOM   506  C CD2 . LEU A 1 96  ? -17.638 27.879 48.447  1.00 35.74  ? 111 LEU A CD2 1 
ATOM   507  N N   . LYS A 1 97  ? -17.413 31.605 52.437  1.00 33.34  ? 112 LYS A N   1 
ATOM   508  C CA  . LYS A 1 97  ? -18.096 32.268 53.536  1.00 34.07  ? 112 LYS A CA  1 
ATOM   509  C C   . LYS A 1 97  ? -19.343 32.970 53.006  1.00 35.81  ? 112 LYS A C   1 
ATOM   510  O O   . LYS A 1 97  ? -19.367 33.416 51.854  1.00 33.58  ? 112 LYS A O   1 
ATOM   511  C CB  . LYS A 1 97  ? -17.178 33.287 54.214  1.00 33.53  ? 112 LYS A CB  1 
ATOM   512  C CG  . LYS A 1 97  ? -16.529 32.794 55.497  1.00 42.48  ? 112 LYS A CG  1 
ATOM   513  N N   . PRO A 1 98  ? -20.395 33.072 53.818  1.00 37.61  ? 113 PRO A N   1 
ATOM   514  C CA  . PRO A 1 98  ? -21.621 33.729 53.349  1.00 33.95  ? 113 PRO A CA  1 
ATOM   515  C C   . PRO A 1 98  ? -21.370 35.184 52.988  1.00 32.23  ? 113 PRO A C   1 
ATOM   516  O O   . PRO A 1 98  ? -20.426 35.811 53.473  1.00 32.24  ? 113 PRO A O   1 
ATOM   517  C CB  . PRO A 1 98  ? -22.572 33.606 54.547  1.00 36.00  ? 113 PRO A CB  1 
ATOM   518  C CG  . PRO A 1 98  ? -22.039 32.459 55.342  1.00 34.42  ? 113 PRO A CG  1 
ATOM   519  C CD  . PRO A 1 98  ? -20.549 32.522 55.176  1.00 36.03  ? 113 PRO A CD  1 
ATOM   520  N N   . VAL A 1 99  ? -22.221 35.714 52.104  1.00 33.70  ? 114 VAL A N   1 
ATOM   521  C CA  . VAL A 1 99  ? -22.118 37.123 51.745  1.00 32.51  ? 114 VAL A CA  1 
ATOM   522  C C   . VAL A 1 99  ? -22.219 37.969 53.013  1.00 34.41  ? 114 VAL A C   1 
ATOM   523  O O   . VAL A 1 99  ? -22.907 37.610 53.976  1.00 34.15  ? 114 VAL A O   1 
ATOM   524  C CB  . VAL A 1 99  ? -23.199 37.527 50.728  1.00 32.45  ? 114 VAL A CB  1 
ATOM   525  C CG1 . VAL A 1 99  ? -22.946 36.869 49.395  1.00 29.94  ? 114 VAL A CG1 1 
ATOM   526  C CG2 . VAL A 1 99  ? -24.587 37.163 51.242  1.00 33.69  ? 114 VAL A CG2 1 
ATOM   527  N N   . ALA A 1 100 ? -21.514 39.096 53.020  1.00 33.45  ? 115 ALA A N   1 
ATOM   528  C CA  . ALA A 1 100 ? -21.462 39.980 54.179  1.00 33.32  ? 115 ALA A CA  1 
ATOM   529  C C   . ALA A 1 100 ? -22.479 41.099 53.989  1.00 36.88  ? 115 ALA A C   1 
ATOM   530  O O   . ALA A 1 100 ? -22.310 41.962 53.122  1.00 39.31  ? 115 ALA A O   1 
ATOM   531  C CB  . ALA A 1 100 ? -20.055 40.539 54.374  1.00 33.70  ? 115 ALA A CB  1 
ATOM   532  N N   . THR A 1 101 ? -23.537 41.074 54.791  1.00 36.56  ? 116 THR A N   1 
ATOM   533  C CA  . THR A 1 101 ? -24.555 42.111 54.782  1.00 34.90  ? 116 THR A CA  1 
ATOM   534  C C   . THR A 1 101 ? -24.620 42.767 56.156  1.00 41.42  ? 116 THR A C   1 
ATOM   535  O O   . THR A 1 101 ? -23.957 42.340 57.105  1.00 41.86  ? 116 THR A O   1 
ATOM   536  C CB  . THR A 1 101 ? -25.928 41.546 54.396  1.00 33.30  ? 116 THR A CB  1 
ATOM   537  O OG1 . THR A 1 101 ? -26.303 40.516 55.318  1.00 36.84  ? 116 THR A OG1 1 
ATOM   538  C CG2 . THR A 1 101 ? -25.892 40.976 52.983  1.00 33.60  ? 116 THR A CG2 1 
ATOM   539  N N   . GLY A 1 102 ? -25.434 43.814 56.258  1.00 35.83  ? 117 GLY A N   1 
ATOM   540  C CA  . GLY A 1 102 ? -25.571 44.530 57.508  1.00 38.27  ? 117 GLY A CA  1 
ATOM   541  C C   . GLY A 1 102 ? -24.426 45.482 57.796  1.00 44.60  ? 117 GLY A C   1 
ATOM   542  O O   . GLY A 1 102 ? -23.942 46.173 56.895  1.00 41.86  ? 117 GLY A O   1 
ATOM   543  N N   . ASP A 1 103 ? -23.976 45.518 59.050  1.00 49.11  ? 118 ASP A N   1 
ATOM   544  C CA  . ASP A 1 103 ? -22.956 46.469 59.494  1.00 47.67  ? 118 ASP A CA  1 
ATOM   545  C C   . ASP A 1 103 ? -21.537 45.938 59.346  1.00 50.51  ? 118 ASP A C   1 
ATOM   546  O O   . ASP A 1 103 ? -20.684 46.190 60.198  1.00 64.23  ? 118 ASP A O   1 
ATOM   547  C CB  . ASP A 1 103 ? -23.223 46.870 60.940  1.00 45.75  ? 118 ASP A CB  1 
ATOM   548  C CG  . ASP A 1 103 ? -22.546 48.173 61.313  1.00 49.14  ? 118 ASP A CG  1 
ATOM   549  O OD1 . ASP A 1 103 ? -23.029 49.248 60.891  1.00 48.91  ? 118 ASP A OD1 1 
ATOM   550  O OD2 . ASP A 1 103 ? -21.518 48.105 62.018  1.00 44.03  ? 118 ASP A OD2 1 
ATOM   551  N N   . GLN A 1 104 ? -21.244 45.200 58.288  1.00 48.89  ? 119 GLN A N   1 
ATOM   552  C CA  . GLN A 1 104 ? -19.884 44.780 57.998  1.00 52.16  ? 119 GLN A CA  1 
ATOM   553  C C   . GLN A 1 104 ? -19.564 45.167 56.564  1.00 56.26  ? 119 GLN A C   1 
ATOM   554  O O   . GLN A 1 104 ? -20.463 45.427 55.761  1.00 54.53  ? 119 GLN A O   1 
ATOM   555  C CB  . GLN A 1 104 ? -19.696 43.276 58.207  1.00 47.70  ? 119 GLN A CB  1 
ATOM   556  C CG  . GLN A 1 104 ? -20.819 42.459 57.640  1.00 45.67  ? 119 GLN A CG  1 
ATOM   557  C CD  . GLN A 1 104 ? -20.896 41.084 58.252  1.00 45.91  ? 119 GLN A CD  1 
ATOM   558  O OE1 . GLN A 1 104 ? -19.984 40.657 58.960  1.00 52.64  ? 119 GLN A OE1 1 
ATOM   559  N NE2 . GLN A 1 104 ? -21.994 40.384 57.994  1.00 38.62  ? 119 GLN A NE2 1 
ATOM   560  N N   . ARG A 1 105 ? -18.276 45.228 56.251  1.00 55.59  ? 120 ARG A N   1 
ATOM   561  C CA  . ARG A 1 105 ? -17.889 45.584 54.897  1.00 54.23  ? 120 ARG A CA  1 
ATOM   562  C C   . ARG A 1 105 ? -17.964 44.359 53.987  1.00 49.84  ? 120 ARG A C   1 
ATOM   563  O O   . ARG A 1 105 ? -17.962 43.211 54.439  1.00 48.08  ? 120 ARG A O   1 
ATOM   564  C CB  . ARG A 1 105 ? -16.492 46.207 54.877  1.00 48.57  ? 120 ARG A CB  1 
ATOM   565  C CG  . ARG A 1 105 ? -15.419 45.372 55.522  1.00 52.67  ? 120 ARG A CG  1 
ATOM   566  C CD  . ARG A 1 105 ? -14.151 46.182 55.740  1.00 57.96  ? 120 ARG A CD  1 
ATOM   567  N NE  . ARG A 1 105 ? -13.125 45.392 56.410  1.00 59.70  ? 120 ARG A NE  1 
ATOM   568  C CZ  . ARG A 1 105 ? -11.853 45.341 56.040  1.00 65.25  ? 120 ARG A CZ  1 
ATOM   569  N NH1 . ARG A 1 105 ? -11.399 46.055 55.022  1.00 62.64  ? 120 ARG A NH1 1 
ATOM   570  N NH2 . ARG A 1 105 ? -11.015 44.551 56.707  1.00 68.05  ? 120 ARG A NH2 1 
ATOM   571  N N   . LEU A 1 106 ? -18.065 44.627 52.684  1.00 52.18  ? 121 LEU A N   1 
ATOM   572  C CA  . LEU A 1 106 ? -18.238 43.551 51.714  1.00 45.57  ? 121 LEU A CA  1 
ATOM   573  C C   . LEU A 1 106 ? -17.095 42.547 51.795  1.00 44.66  ? 121 LEU A C   1 
ATOM   574  O O   . LEU A 1 106 ? -17.311 41.334 51.692  1.00 42.51  ? 121 LEU A O   1 
ATOM   575  C CB  . LEU A 1 106 ? -18.335 44.142 50.311  1.00 45.93  ? 121 LEU A CB  1 
ATOM   576  C CG  . LEU A 1 106 ? -19.318 43.510 49.330  1.00 50.49  ? 121 LEU A CG  1 
ATOM   577  C CD1 . LEU A 1 106 ? -19.500 44.412 48.121  1.00 49.02  ? 121 LEU A CD1 1 
ATOM   578  C CD2 . LEU A 1 106 ? -18.876 42.123 48.908  1.00 48.55  ? 121 LEU A CD2 1 
ATOM   579  N N   . LYS A 1 107 ? -15.872 43.036 52.002  1.00 51.08  ? 122 LYS A N   1 
ATOM   580  C CA  . LYS A 1 107 ? -14.695 42.178 52.023  1.00 47.77  ? 122 LYS A CA  1 
ATOM   581  C C   . LYS A 1 107 ? -14.671 41.219 53.207  1.00 43.86  ? 122 LYS A C   1 
ATOM   582  O O   . LYS A 1 107 ? -13.880 40.268 53.192  1.00 39.97  ? 122 LYS A O   1 
ATOM   583  C CB  . LYS A 1 107 ? -13.434 43.042 52.023  1.00 45.55  ? 122 LYS A CB  1 
ATOM   584  C CG  . LYS A 1 107 ? -12.339 42.534 51.111  1.00 54.24  ? 122 LYS A CG  1 
ATOM   585  C CD  . LYS A 1 107 ? -11.217 43.550 50.980  1.00 54.48  ? 122 LYS A CD  1 
ATOM   586  C CE  . LYS A 1 107 ? -10.769 44.044 52.342  1.00 55.07  ? 122 LYS A CE  1 
ATOM   587  N NZ  . LYS A 1 107 ? -9.381  44.579 52.290  1.00 62.42  ? 122 LYS A NZ  1 
ATOM   588  N N   . ASP A 1 108 ? -15.513 41.434 54.219  1.00 38.78  ? 123 ASP A N   1 
ATOM   589  C CA  . ASP A 1 108 ? -15.571 40.533 55.366  1.00 37.98  ? 123 ASP A CA  1 
ATOM   590  C C   . ASP A 1 108 ? -16.280 39.216 55.069  1.00 42.54  ? 123 ASP A C   1 
ATOM   591  O O   . ASP A 1 108 ? -16.273 38.324 55.924  1.00 38.37  ? 123 ASP A O   1 
ATOM   592  C CB  . ASP A 1 108 ? -16.278 41.213 56.538  1.00 45.07  ? 123 ASP A CB  1 
ATOM   593  C CG  . ASP A 1 108 ? -15.503 42.395 57.083  1.00 50.09  ? 123 ASP A CG  1 
ATOM   594  O OD1 . ASP A 1 108 ? -14.295 42.509 56.788  1.00 49.65  ? 123 ASP A OD1 1 
ATOM   595  O OD2 . ASP A 1 108 ? -16.110 43.214 57.809  1.00 56.08  ? 123 ASP A OD2 1 
ATOM   596  N N   . GLY A 1 109 ? -16.901 39.074 53.899  1.00 36.71  ? 124 GLY A N   1 
ATOM   597  C CA  . GLY A 1 109 ? -17.623 37.861 53.585  1.00 34.42  ? 124 GLY A CA  1 
ATOM   598  C C   . GLY A 1 109 ? -17.245 37.285 52.240  1.00 35.23  ? 124 GLY A C   1 
ATOM   599  O O   . GLY A 1 109 ? -16.297 37.750 51.602  1.00 32.48  ? 124 GLY A O   1 
ATOM   600  N N   . GLY A 1 110 ? -17.978 36.268 51.800  1.00 33.77  ? 125 GLY A N   1 
ATOM   601  C CA  . GLY A 1 110 ? -17.714 35.663 50.514  1.00 32.95  ? 125 GLY A CA  1 
ATOM   602  C C   . GLY A 1 110 ? -18.895 35.733 49.570  1.00 31.37  ? 125 GLY A C   1 
ATOM   603  O O   . GLY A 1 110 ? -19.592 36.749 49.508  1.00 29.63  ? 125 GLY A O   1 
ATOM   604  N N   . PHE A 1 111 ? -19.137 34.649 48.835  1.00 34.70  ? 126 PHE A N   1 
ATOM   605  C CA  . PHE A 1 111 ? -20.170 34.611 47.809  1.00 36.24  ? 126 PHE A CA  1 
ATOM   606  C C   . PHE A 1 111 ? -21.320 33.671 48.151  1.00 38.15  ? 126 PHE A C   1 
ATOM   607  O O   . PHE A 1 111 ? -22.299 33.608 47.398  1.00 34.37  ? 126 PHE A O   1 
ATOM   608  C CB  . PHE A 1 111 ? -19.548 34.200 46.468  1.00 32.49  ? 126 PHE A CB  1 
ATOM   609  C CG  . PHE A 1 111 ? -18.780 35.300 45.786  1.00 32.79  ? 126 PHE A CG  1 
ATOM   610  C CD1 . PHE A 1 111 ? -17.609 35.801 46.342  1.00 34.57  ? 126 PHE A CD1 1 
ATOM   611  C CD2 . PHE A 1 111 ? -19.221 35.828 44.580  1.00 34.46  ? 126 PHE A CD2 1 
ATOM   612  C CE1 . PHE A 1 111 ? -16.892 36.812 45.712  1.00 34.56  ? 126 PHE A CE1 1 
ATOM   613  C CE2 . PHE A 1 111 ? -18.508 36.843 43.942  1.00 38.31  ? 126 PHE A CE2 1 
ATOM   614  C CZ  . PHE A 1 111 ? -17.340 37.336 44.510  1.00 32.08  ? 126 PHE A CZ  1 
ATOM   615  N N   . ALA A 1 112 ? -21.237 32.951 49.267  1.00 36.21  ? 127 ALA A N   1 
ATOM   616  C CA  . ALA A 1 112 ? -22.168 31.870 49.540  1.00 34.72  ? 127 ALA A CA  1 
ATOM   617  C C   . ALA A 1 112 ? -23.472 32.390 50.139  1.00 35.12  ? 127 ALA A C   1 
ATOM   618  O O   . ALA A 1 112 ? -23.559 33.515 50.642  1.00 34.36  ? 127 ALA A O   1 
ATOM   619  C CB  . ALA A 1 112 ? -21.537 30.848 50.484  1.00 32.95  ? 127 ALA A CB  1 
ATOM   620  N N   . PHE A 1 113 ? -24.495 31.548 50.068  1.00 32.87  ? 128 PHE A N   1 
ATOM   621  C CA  . PHE A 1 113 ? -25.746 31.828 50.752  1.00 35.96  ? 128 PHE A CA  1 
ATOM   622  C C   . PHE A 1 113 ? -25.474 32.125 52.226  1.00 35.54  ? 128 PHE A C   1 
ATOM   623  O O   . PHE A 1 113 ? -24.624 31.465 52.842  1.00 34.88  ? 128 PHE A O   1 
ATOM   624  C CB  . PHE A 1 113 ? -26.692 30.627 50.643  1.00 28.86  ? 128 PHE A CB  1 
ATOM   625  C CG  . PHE A 1 113 ? -27.748 30.768 49.588  1.00 33.26  ? 128 PHE A CG  1 
ATOM   626  C CD1 . PHE A 1 113 ? -27.404 30.784 48.242  1.00 33.13  ? 128 PHE A CD1 1 
ATOM   627  C CD2 . PHE A 1 113 ? -29.086 30.870 49.940  1.00 27.80  ? 128 PHE A CD2 1 
ATOM   628  C CE1 . PHE A 1 113 ? -28.371 30.897 47.264  1.00 31.73  ? 128 PHE A CE1 1 
ATOM   629  C CE2 . PHE A 1 113 ? -30.064 30.991 48.966  1.00 36.10  ? 128 PHE A CE2 1 
ATOM   630  C CZ  . PHE A 1 113 ? -29.702 31.008 47.622  1.00 33.52  ? 128 PHE A CZ  1 
ATOM   631  N N   . PRO A 1 114 ? -26.152 33.106 52.819  1.00 35.58  ? 129 PRO A N   1 
ATOM   632  C CA  . PRO A 1 114 ? -26.135 33.218 54.280  1.00 35.22  ? 129 PRO A CA  1 
ATOM   633  C C   . PRO A 1 114 ? -26.601 31.903 54.888  1.00 37.82  ? 129 PRO A C   1 
ATOM   634  O O   . PRO A 1 114 ? -27.549 31.279 54.404  1.00 32.61  ? 129 PRO A O   1 
ATOM   635  C CB  . PRO A 1 114 ? -27.107 34.369 54.573  1.00 31.19  ? 129 PRO A CB  1 
ATOM   636  C CG  . PRO A 1 114 ? -27.813 34.657 53.300  1.00 29.14  ? 129 PRO A CG  1 
ATOM   637  C CD  . PRO A 1 114 ? -26.965 34.156 52.180  1.00 33.61  ? 129 PRO A CD  1 
ATOM   638  N N   . ASN A 1 115 ? -25.899 31.455 55.926  1.00 37.48  ? 130 ASN A N   1 
ATOM   639  C CA  . ASN A 1 115 ? -26.154 30.129 56.493  1.00 35.47  ? 130 ASN A CA  1 
ATOM   640  C C   . ASN A 1 115 ? -27.254 30.167 57.551  1.00 34.97  ? 130 ASN A C   1 
ATOM   641  O O   . ASN A 1 115 ? -27.110 29.606 58.633  1.00 39.46  ? 130 ASN A O   1 
ATOM   642  C CB  . ASN A 1 115 ? -24.866 29.543 57.067  1.00 35.86  ? 130 ASN A CB  1 
ATOM   643  C CG  . ASN A 1 115 ? -24.191 30.468 58.062  1.00 38.55  ? 130 ASN A CG  1 
ATOM   644  O OD1 . ASN A 1 115 ? -24.789 31.429 58.542  1.00 49.24  ? 130 ASN A OD1 1 
ATOM   645  N ND2 . ASN A 1 115 ? -22.934 30.181 58.377  1.00 46.49  ? 130 ASN A ND2 1 
ATOM   646  N N   . ALA A 1 116 ? -28.370 30.822 57.240  1.00 33.95  ? 131 ALA A N   1 
ATOM   647  C CA  . ALA A 1 116 ? -29.416 31.013 58.236  1.00 36.52  ? 131 ALA A CA  1 
ATOM   648  C C   . ALA A 1 116 ? -30.334 29.805 58.374  1.00 33.96  ? 131 ALA A C   1 
ATOM   649  O O   . ALA A 1 116 ? -30.966 29.641 59.424  1.00 33.94  ? 131 ALA A O   1 
ATOM   650  C CB  . ALA A 1 116 ? -30.244 32.251 57.900  1.00 32.73  ? 131 ALA A CB  1 
ATOM   651  N N   . ASN A 1 117 ? -30.415 28.954 57.356  1.00 32.89  ? 132 ASN A N   1 
ATOM   652  C CA  . ASN A 1 117 ? -31.372 27.854 57.334  1.00 33.48  ? 132 ASN A CA  1 
ATOM   653  C C   . ASN A 1 117 ? -30.641 26.566 56.974  1.00 31.56  ? 132 ASN A C   1 
ATOM   654  O O   . ASN A 1 117 ? -30.144 26.420 55.851  1.00 34.19  ? 132 ASN A O   1 
ATOM   655  C CB  . ASN A 1 117 ? -32.511 28.140 56.348  1.00 31.53  ? 132 ASN A CB  1 
ATOM   656  C CG  . ASN A 1 117 ? -33.715 27.232 56.562  1.00 37.73  ? 132 ASN A CG  1 
ATOM   657  O OD1 . ASN A 1 117 ? -33.571 26.024 56.780  1.00 38.65  ? 132 ASN A OD1 1 
ATOM   658  N ND2 . ASN A 1 117 ? -34.915 27.813 56.506  1.00 29.31  ? 132 ASN A ND2 1 
ATOM   659  N N   . ASP A 1 118 ? -30.610 25.623 57.921  1.00 38.18  ? 133 ASP A N   1 
ATOM   660  C CA  . ASP A 1 118 ? -29.938 24.339 57.731  1.00 39.94  ? 133 ASP A CA  1 
ATOM   661  C C   . ASP A 1 118 ? -30.491 23.545 56.556  1.00 38.33  ? 133 ASP A C   1 
ATOM   662  O O   . ASP A 1 118 ? -29.810 22.640 56.064  1.00 40.81  ? 133 ASP A O   1 
ATOM   663  C CB  . ASP A 1 118 ? -30.071 23.493 58.998  1.00 40.33  ? 133 ASP A CB  1 
ATOM   664  C CG  . ASP A 1 118 ? -29.045 23.844 60.036  1.00 48.71  ? 133 ASP A CG  1 
ATOM   665  O OD1 . ASP A 1 118 ? -28.006 24.428 59.662  1.00 53.07  ? 133 ASP A OD1 1 
ATOM   666  O OD2 . ASP A 1 118 ? -29.290 23.554 61.230  1.00 62.50  ? 133 ASP A OD2 1 
ATOM   667  N N   . HIS A 1 119 ? -31.715 23.833 56.112  1.00 37.13  ? 134 HIS A N   1 
ATOM   668  C CA  . HIS A 1 119 ? -32.294 23.099 54.995  1.00 36.31  ? 134 HIS A CA  1 
ATOM   669  C C   . HIS A 1 119 ? -31.870 23.642 53.639  1.00 37.29  ? 134 HIS A C   1 
ATOM   670  O O   . HIS A 1 119 ? -32.138 22.994 52.622  1.00 40.25  ? 134 HIS A O   1 
ATOM   671  C CB  . HIS A 1 119 ? -33.820 23.114 55.085  1.00 40.46  ? 134 HIS A CB  1 
ATOM   672  C CG  . HIS A 1 119 ? -34.360 22.391 56.278  1.00 49.22  ? 134 HIS A CG  1 
ATOM   673  N ND1 . HIS A 1 119 ? -34.124 21.052 56.505  1.00 51.78  ? 134 HIS A ND1 1 
ATOM   674  C CD2 . HIS A 1 119 ? -35.130 22.818 57.307  1.00 47.38  ? 134 HIS A CD2 1 
ATOM   675  C CE1 . HIS A 1 119 ? -34.722 20.686 57.625  1.00 51.50  ? 134 HIS A CE1 1 
ATOM   676  N NE2 . HIS A 1 119 ? -35.340 21.738 58.130  1.00 52.66  ? 134 HIS A NE2 1 
ATOM   677  N N   . ILE A 1 120 ? -31.215 24.800 53.594  1.00 32.21  ? 135 ILE A N   1 
ATOM   678  C CA  . ILE A 1 120 ? -30.842 25.397 52.320  1.00 35.66  ? 135 ILE A CA  1 
ATOM   679  C C   . ILE A 1 120 ? -29.340 25.248 52.095  1.00 38.35  ? 135 ILE A C   1 
ATOM   680  O O   . ILE A 1 120 ? -28.900 24.401 51.311  1.00 36.75  ? 135 ILE A O   1 
ATOM   681  C CB  . ILE A 1 120 ? -31.274 26.871 52.258  1.00 36.01  ? 135 ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 120 ? -32.753 27.000 52.642  1.00 33.37  ? 135 ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 120 ? -31.019 27.442 50.870  1.00 33.91  ? 135 ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 120 ? -33.276 28.426 52.600  1.00 28.29  ? 135 ILE A CD1 1 
ATOM   685  N N   . SER A 1 121 ? -28.544 26.058 52.782  1.00 36.25  ? 136 SER A N   1 
ATOM   686  C CA  . SER A 1 121 ? -27.116 26.098 52.537  1.00 32.63  ? 136 SER A CA  1 
ATOM   687  C C   . SER A 1 121 ? -26.400 26.459 53.828  1.00 34.10  ? 136 SER A C   1 
ATOM   688  O O   . SER A 1 121 ? -26.937 27.222 54.641  1.00 33.92  ? 136 SER A O   1 
ATOM   689  C CB  . SER A 1 121 ? -26.768 27.115 51.437  1.00 28.66  ? 136 SER A CB  1 
ATOM   690  O OG  . SER A 1 121 ? -25.412 27.008 51.032  1.00 27.36  ? 136 SER A OG  1 
ATOM   691  N N   . PRO A 1 122 ? -25.211 25.898 54.066  1.00 30.76  ? 137 PRO A N   1 
ATOM   692  C CA  . PRO A 1 122 ? -24.604 24.780 53.327  1.00 30.55  ? 137 PRO A CA  1 
ATOM   693  C C   . PRO A 1 122 ? -25.139 23.456 53.858  1.00 29.55  ? 137 PRO A C   1 
ATOM   694  O O   . PRO A 1 122 ? -25.743 23.428 54.925  1.00 30.99  ? 137 PRO A O   1 
ATOM   695  C CB  . PRO A 1 122 ? -23.104 24.958 53.598  1.00 30.61  ? 137 PRO A CB  1 
ATOM   696  C CG  . PRO A 1 122 ? -23.060 25.594 54.970  1.00 31.39  ? 137 PRO A CG  1 
ATOM   697  C CD  . PRO A 1 122 ? -24.263 26.513 55.015  1.00 31.27  ? 137 PRO A CD  1 
ATOM   698  N N   . MET A 1 123 ? -24.931 22.343 53.159  1.00 30.01  ? 138 MET A N   1 
ATOM   699  C CA  . MET A 1 123 ? -25.426 21.057 53.627  1.00 28.48  ? 138 MET A CA  1 
ATOM   700  C C   . MET A 1 123 ? -24.363 19.986 53.422  1.00 34.75  ? 138 MET A C   1 
ATOM   701  O O   . MET A 1 123 ? -23.731 19.915 52.362  1.00 32.44  ? 138 MET A O   1 
ATOM   702  C CB  . MET A 1 123 ? -26.717 20.665 52.901  1.00 35.44  ? 138 MET A CB  1 
ATOM   703  C CG  . MET A 1 123 ? -27.426 19.477 53.532  1.00 45.47  ? 138 MET A CG  1 
ATOM   704  S SD  . MET A 1 123 ? -29.094 19.288 52.895  1.00 49.02  ? 138 MET A SD  1 
ATOM   705  C CE  . MET A 1 123 ? -29.750 20.891 53.329  1.00 34.13  ? 138 MET A CE  1 
ATOM   706  N N   . THR A 1 124 ? -24.158 19.164 54.445  1.00 31.91  ? 139 THR A N   1 
ATOM   707  C CA  . THR A 1 124 ? -23.222 18.062 54.313  1.00 32.83  ? 139 THR A CA  1 
ATOM   708  C C   . THR A 1 124 ? -23.842 16.947 53.480  1.00 33.88  ? 139 THR A C   1 
ATOM   709  O O   . THR A 1 124 ? -25.064 16.854 53.331  1.00 33.81  ? 139 THR A O   1 
ATOM   710  C CB  . THR A 1 124 ? -22.815 17.525 55.685  1.00 37.63  ? 139 THR A CB  1 
ATOM   711  O OG1 . THR A 1 124 ? -23.957 16.950 56.327  1.00 41.75  ? 139 THR A OG1 1 
ATOM   712  C CG2 . THR A 1 124 ? -22.261 18.646 56.564  1.00 27.36  ? 139 THR A CG2 1 
ATOM   713  N N   . LEU A 1 125 ? -22.974 16.101 52.914  1.00 38.93  ? 140 LEU A N   1 
ATOM   714  C CA  . LEU A 1 125 ? -23.450 14.924 52.189  1.00 37.80  ? 140 LEU A CA  1 
ATOM   715  C C   . LEU A 1 125 ? -24.391 14.091 53.050  1.00 39.44  ? 140 LEU A C   1 
ATOM   716  O O   . LEU A 1 125 ? -25.437 13.632 52.578  1.00 35.40  ? 140 LEU A O   1 
ATOM   717  C CB  . LEU A 1 125 ? -22.267 14.071 51.728  1.00 38.41  ? 140 LEU A CB  1 
ATOM   718  C CG  . LEU A 1 125 ? -22.635 12.802 50.947  1.00 35.97  ? 140 LEU A CG  1 
ATOM   719  C CD1 . LEU A 1 125 ? -23.371 13.145 49.662  1.00 35.48  ? 140 LEU A CD1 1 
ATOM   720  C CD2 . LEU A 1 125 ? -21.403 11.969 50.649  1.00 40.22  ? 140 LEU A CD2 1 
ATOM   721  N N   . GLU A 1 126 ? -24.036 13.899 54.324  1.00 36.45  ? 141 GLU A N   1 
ATOM   722  C CA  . GLU A 1 126 ? -24.861 13.095 55.218  1.00 41.17  ? 141 GLU A CA  1 
ATOM   723  C C   . GLU A 1 126 ? -26.271 13.668 55.339  1.00 40.04  ? 141 GLU A C   1 
ATOM   724  O O   . GLU A 1 126 ? -27.260 12.926 55.275  1.00 38.00  ? 141 GLU A O   1 
ATOM   725  C CB  . GLU A 1 126 ? -24.185 13.003 56.586  1.00 36.32  ? 141 GLU A CB  1 
ATOM   726  C CG  . GLU A 1 126 ? -25.064 12.484 57.701  1.00 50.41  ? 141 GLU A CG  1 
ATOM   727  C CD  . GLU A 1 126 ? -24.347 12.477 59.042  1.00 59.57  ? 141 GLU A CD  1 
ATOM   728  O OE1 . GLU A 1 126 ? -23.237 11.909 59.116  1.00 54.99  ? 141 GLU A OE1 1 
ATOM   729  O OE2 . GLU A 1 126 ? -24.887 13.051 60.015  1.00 65.01  ? 141 GLU A OE2 1 
ATOM   730  N N   . ASN A 1 127 ? -26.388 14.987 55.489  1.00 33.23  ? 142 ASN A N   1 
ATOM   731  C CA  . ASN A 1 127 ? -27.710 15.594 55.595  1.00 40.79  ? 142 ASN A CA  1 
ATOM   732  C C   . ASN A 1 127 ? -28.426 15.616 54.248  1.00 42.47  ? 142 ASN A C   1 
ATOM   733  O O   . ASN A 1 127 ? -29.648 15.429 54.188  1.00 41.89  ? 142 ASN A O   1 
ATOM   734  C CB  . ASN A 1 127 ? -27.591 16.998 56.178  1.00 38.86  ? 142 ASN A CB  1 
ATOM   735  C CG  . ASN A 1 127 ? -27.192 16.981 57.642  1.00 42.34  ? 142 ASN A CG  1 
ATOM   736  O OD1 . ASN A 1 127 ? -26.306 17.721 58.063  1.00 45.39  ? 142 ASN A OD1 1 
ATOM   737  N ND2 . ASN A 1 127 ? -27.841 16.123 58.423  1.00 41.12  ? 142 ASN A ND2 1 
ATOM   738  N N   . LEU A 1 128 ? -27.687 15.850 53.161  1.00 38.60  ? 143 LEU A N   1 
ATOM   739  C CA  . LEU A 1 128 ? -28.245 15.680 51.822  1.00 40.36  ? 143 LEU A CA  1 
ATOM   740  C C   . LEU A 1 128 ? -28.859 14.293 51.661  1.00 39.47  ? 143 LEU A C   1 
ATOM   741  O O   . LEU A 1 128 ? -29.988 14.150 51.176  1.00 40.16  ? 143 LEU A O   1 
ATOM   742  C CB  . LEU A 1 128 ? -27.153 15.909 50.772  1.00 33.50  ? 143 LEU A CB  1 
ATOM   743  C CG  . LEU A 1 128 ? -26.755 17.336 50.381  1.00 37.55  ? 143 LEU A CG  1 
ATOM   744  C CD1 . LEU A 1 128 ? -25.649 17.297 49.344  1.00 37.64  ? 143 LEU A CD1 1 
ATOM   745  C CD2 . LEU A 1 128 ? -27.945 18.110 49.827  1.00 34.50  ? 143 LEU A CD2 1 
ATOM   746  N N   . LYS A 1 129 ? -28.122 13.258 52.075  1.00 36.67  ? 144 LYS A N   1 
ATOM   747  C CA  . LYS A 1 129 ? -28.616 11.889 51.963  1.00 40.01  ? 144 LYS A CA  1 
ATOM   748  C C   . LYS A 1 129 ? -29.873 11.678 52.800  1.00 42.28  ? 144 LYS A C   1 
ATOM   749  O O   . LYS A 1 129 ? -30.842 11.071 52.333  1.00 42.13  ? 144 LYS A O   1 
ATOM   750  C CB  . LYS A 1 129 ? -27.526 10.899 52.382  1.00 39.43  ? 144 LYS A CB  1 
ATOM   751  C CG  . LYS A 1 129 ? -26.357 10.793 51.418  1.00 39.70  ? 144 LYS A CG  1 
ATOM   752  C CD  . LYS A 1 129 ? -26.779 10.169 50.103  1.00 42.82  ? 144 LYS A CD  1 
ATOM   753  C CE  . LYS A 1 129 ? -25.567 9.798  49.253  1.00 43.33  ? 144 LYS A CE  1 
ATOM   754  N NZ  . LYS A 1 129 ? -25.942 8.930  48.097  1.00 41.21  ? 144 LYS A NZ  1 
ATOM   755  N N   . ALA A 1 130 ? -29.876 12.167 54.041  1.00 41.59  ? 145 ALA A N   1 
ATOM   756  C CA  . ALA A 1 130 ? -31.058 12.024 54.886  1.00 47.03  ? 145 ALA A CA  1 
ATOM   757  C C   . ALA A 1 130 ? -32.250 12.768 54.292  1.00 46.29  ? 145 ALA A C   1 
ATOM   758  O O   . ALA A 1 130 ? -33.352 12.217 54.184  1.00 49.12  ? 145 ALA A O   1 
ATOM   759  C CB  . ALA A 1 130 ? -30.755 12.526 56.300  1.00 35.88  ? 145 ALA A CB  1 
ATOM   760  N N   . ARG A 1 131 ? -32.034 14.021 53.882  1.00 40.72  ? 146 ARG A N   1 
ATOM   761  C CA  . ARG A 1 131 ? -33.117 14.860 53.384  1.00 37.54  ? 146 ARG A CA  1 
ATOM   762  C C   . ARG A 1 131 ? -33.854 14.203 52.224  1.00 41.81  ? 146 ARG A C   1 
ATOM   763  O O   . ARG A 1 131 ? -35.084 14.290 52.127  1.00 41.66  ? 146 ARG A O   1 
ATOM   764  C CB  . ARG A 1 131 ? -32.554 16.222 52.968  1.00 41.56  ? 146 ARG A CB  1 
ATOM   765  C CG  . ARG A 1 131 ? -33.269 16.883 51.810  1.00 40.57  ? 146 ARG A CG  1 
ATOM   766  C CD  . ARG A 1 131 ? -34.524 17.582 52.293  1.00 51.69  ? 146 ARG A CD  1 
ATOM   767  N NE  . ARG A 1 131 ? -34.233 18.943 52.722  1.00 55.09  ? 146 ARG A NE  1 
ATOM   768  C CZ  . ARG A 1 131 ? -34.256 19.999 51.922  1.00 50.08  ? 146 ARG A CZ  1 
ATOM   769  N NH1 . ARG A 1 131 ? -34.584 19.891 50.643  1.00 44.61  ? 146 ARG A NH1 1 
ATOM   770  N NH2 . ARG A 1 131 ? -33.937 21.191 52.416  1.00 48.76  ? 146 ARG A NH2 1 
ATOM   771  N N   . TYR A 1 132 ? -33.122 13.535 51.333  1.00 43.31  ? 147 TYR A N   1 
ATOM   772  C CA  . TYR A 1 132 ? -33.716 12.908 50.161  1.00 43.66  ? 147 TYR A CA  1 
ATOM   773  C C   . TYR A 1 132 ? -33.693 11.389 50.248  1.00 49.54  ? 147 TYR A C   1 
ATOM   774  O O   . TYR A 1 132 ? -33.708 10.716 49.213  1.00 50.88  ? 147 TYR A O   1 
ATOM   775  C CB  . TYR A 1 132 ? -33.008 13.366 48.884  1.00 45.74  ? 147 TYR A CB  1 
ATOM   776  C CG  . TYR A 1 132 ? -32.959 14.864 48.690  1.00 44.88  ? 147 TYR A CG  1 
ATOM   777  C CD1 . TYR A 1 132 ? -34.095 15.571 48.308  1.00 39.10  ? 147 TYR A CD1 1 
ATOM   778  C CD2 . TYR A 1 132 ? -31.771 15.567 48.871  1.00 38.26  ? 147 TYR A CD2 1 
ATOM   779  C CE1 . TYR A 1 132 ? -34.053 16.939 48.124  1.00 41.04  ? 147 TYR A CE1 1 
ATOM   780  C CE2 . TYR A 1 132 ? -31.715 16.936 48.690  1.00 40.17  ? 147 TYR A CE2 1 
ATOM   781  C CZ  . TYR A 1 132 ? -32.859 17.617 48.318  1.00 43.80  ? 147 TYR A CZ  1 
ATOM   782  O OH  . TYR A 1 132 ? -32.806 18.980 48.135  1.00 39.57  ? 147 TYR A OH  1 
ATOM   783  N N   . LYS A 1 133 ? -33.656 10.833 51.462  1.00 53.20  ? 148 LYS A N   1 
ATOM   784  C CA  . LYS A 1 133 ? -33.567 9.383  51.605  1.00 52.87  ? 148 LYS A CA  1 
ATOM   785  C C   . LYS A 1 133 ? -34.761 8.678  50.973  1.00 57.98  ? 148 LYS A C   1 
ATOM   786  O O   . LYS A 1 133 ? -34.636 7.535  50.520  1.00 59.26  ? 148 LYS A O   1 
ATOM   787  C CB  . LYS A 1 133 ? -33.438 9.009  53.085  1.00 51.58  ? 148 LYS A CB  1 
ATOM   788  C CG  . LYS A 1 133 ? -34.735 9.091  53.881  1.00 62.83  ? 148 LYS A CG  1 
ATOM   789  C CD  . LYS A 1 133 ? -34.547 8.575  55.305  1.00 59.23  ? 148 LYS A CD  1 
ATOM   790  N N   . ASP A 1 134 ? -35.910 9.346  50.903  1.00 56.28  ? 149 ASP A N   1 
ATOM   791  C CA  . ASP A 1 134 ? -37.131 8.728  50.412  1.00 59.50  ? 149 ASP A CA  1 
ATOM   792  C C   . ASP A 1 134 ? -37.368 8.954  48.922  1.00 63.10  ? 149 ASP A C   1 
ATOM   793  O O   . ASP A 1 134 ? -38.427 8.569  48.414  1.00 76.02  ? 149 ASP A O   1 
ATOM   794  C CB  . ASP A 1 134 ? -38.329 9.236  51.217  1.00 64.56  ? 149 ASP A CB  1 
ATOM   795  C CG  . ASP A 1 134 ? -38.255 8.838  52.683  1.00 76.78  ? 149 ASP A CG  1 
ATOM   796  O OD1 . ASP A 1 134 ? -37.880 7.677  52.971  1.00 73.74  ? 149 ASP A OD1 1 
ATOM   797  O OD2 . ASP A 1 134 ? -38.571 9.687  53.548  1.00 81.19  ? 149 ASP A OD2 1 
ATOM   798  N N   . ASN A 1 135 ? -36.417 9.556  48.210  1.00 57.39  ? 150 ASN A N   1 
ATOM   799  C CA  . ASN A 1 135 ? -36.528 9.758  46.770  1.00 54.64  ? 150 ASN A CA  1 
ATOM   800  C C   . ASN A 1 135 ? -35.571 8.803  46.072  1.00 54.99  ? 150 ASN A C   1 
ATOM   801  O O   . ASN A 1 135 ? -34.351 8.909  46.237  1.00 56.61  ? 150 ASN A O   1 
ATOM   802  C CB  . ASN A 1 135 ? -36.232 11.207 46.385  1.00 54.96  ? 150 ASN A CB  1 
ATOM   803  C CG  . ASN A 1 135 ? -36.516 11.492 44.916  1.00 51.94  ? 150 ASN A CG  1 
ATOM   804  O OD1 . ASN A 1 135 ? -36.011 10.810 44.020  1.00 54.86  ? 150 ASN A OD1 1 
ATOM   805  N ND2 . ASN A 1 135 ? -37.329 12.510 44.667  1.00 54.88  ? 150 ASN A ND2 1 
ATOM   806  N N   . VAL A 1 136 ? -36.131 7.885  45.281  1.00 55.02  ? 151 VAL A N   1 
ATOM   807  C CA  . VAL A 1 136 ? -35.332 6.818  44.688  1.00 58.62  ? 151 VAL A CA  1 
ATOM   808  C C   . VAL A 1 136 ? -34.392 7.370  43.624  1.00 58.18  ? 151 VAL A C   1 
ATOM   809  O O   . VAL A 1 136 ? -33.243 6.929  43.505  1.00 56.55  ? 151 VAL A O   1 
ATOM   810  C CB  . VAL A 1 136 ? -36.255 5.726  44.117  1.00 61.43  ? 151 VAL A CB  1 
ATOM   811  C CG1 . VAL A 1 136 ? -35.506 4.404  43.992  1.00 63.19  ? 151 VAL A CG1 1 
ATOM   812  C CG2 . VAL A 1 136 ? -37.491 5.577  44.987  1.00 58.92  ? 151 VAL A CG2 1 
ATOM   813  N N   . GLU A 1 137 ? -34.864 8.329  42.825  1.00 57.60  ? 152 GLU A N   1 
ATOM   814  C CA  . GLU A 1 137 ? -34.011 8.917  41.798  1.00 57.92  ? 152 GLU A CA  1 
ATOM   815  C C   . GLU A 1 137 ? -32.892 9.742  42.423  1.00 53.04  ? 152 GLU A C   1 
ATOM   816  O O   . GLU A 1 137 ? -31.728 9.630  42.023  1.00 53.73  ? 152 GLU A O   1 
ATOM   817  C CB  . GLU A 1 137 ? -34.850 9.769  40.844  1.00 62.74  ? 152 GLU A CB  1 
ATOM   818  C CG  . GLU A 1 137 ? -34.612 9.490  39.359  1.00 66.42  ? 152 GLU A CG  1 
ATOM   819  C CD  . GLU A 1 137 ? -34.766 8.023  38.991  1.00 67.77  ? 152 GLU A CD  1 
ATOM   820  O OE1 . GLU A 1 137 ? -34.059 7.568  38.065  1.00 74.99  ? 152 GLU A OE1 1 
ATOM   821  O OE2 . GLU A 1 137 ? -35.595 7.328  39.619  1.00 68.35  ? 152 GLU A OE2 1 
ATOM   822  N N   . MET A 1 138 ? -33.230 10.579 43.407  1.00 49.30  ? 153 MET A N   1 
ATOM   823  C CA  . MET A 1 138 ? -32.206 11.332 44.125  1.00 50.44  ? 153 MET A CA  1 
ATOM   824  C C   . MET A 1 138 ? -31.127 10.410 44.680  1.00 48.70  ? 153 MET A C   1 
ATOM   825  O O   . MET A 1 138 ? -29.931 10.707 44.575  1.00 46.62  ? 153 MET A O   1 
ATOM   826  C CB  . MET A 1 138 ? -32.842 12.141 45.258  1.00 49.20  ? 153 MET A CB  1 
ATOM   827  C CG  . MET A 1 138 ? -33.694 13.319 44.812  1.00 43.60  ? 153 MET A CG  1 
ATOM   828  S SD  . MET A 1 138 ? -32.755 14.606 43.978  1.00 50.56  ? 153 MET A SD  1 
ATOM   829  C CE  . MET A 1 138 ? -32.158 15.565 45.368  1.00 41.71  ? 153 MET A CE  1 
ATOM   830  N N   . MET A 1 139 ? -31.529 9.276  45.263  1.00 52.57  ? 154 MET A N   1 
ATOM   831  C CA  . MET A 1 139 ? -30.575 8.351  45.873  1.00 51.57  ? 154 MET A CA  1 
ATOM   832  C C   . MET A 1 139 ? -29.714 7.620  44.852  1.00 47.93  ? 154 MET A C   1 
ATOM   833  O O   . MET A 1 139 ? -28.744 6.966  45.248  1.00 46.31  ? 154 MET A O   1 
ATOM   834  C CB  . MET A 1 139 ? -31.309 7.331  46.745  1.00 45.44  ? 154 MET A CB  1 
ATOM   835  C CG  . MET A 1 139 ? -31.835 7.904  48.052  1.00 51.44  ? 154 MET A CG  1 
ATOM   836  S SD  . MET A 1 139 ? -30.682 9.072  48.797  1.00 53.51  ? 154 MET A SD  1 
ATOM   837  C CE  . MET A 1 139 ? -30.293 8.260  50.343  1.00 53.68  ? 154 MET A CE  1 
ATOM   838  N N   . LYS A 1 140 ? -30.043 7.701  43.564  1.00 47.56  ? 155 LYS A N   1 
ATOM   839  C CA  . LYS A 1 140 ? -29.201 7.125  42.524  1.00 49.44  ? 155 LYS A CA  1 
ATOM   840  C C   . LYS A 1 140 ? -28.113 8.077  42.047  1.00 50.29  ? 155 LYS A C   1 
ATOM   841  O O   . LYS A 1 140 ? -27.250 7.665  41.265  1.00 51.21  ? 155 LYS A O   1 
ATOM   842  C CB  . LYS A 1 140 ? -30.051 6.694  41.321  1.00 53.07  ? 155 LYS A CB  1 
ATOM   843  C CG  . LYS A 1 140 ? -30.886 5.448  41.547  1.00 56.13  ? 155 LYS A CG  1 
ATOM   844  C CD  . LYS A 1 140 ? -32.187 5.526  40.770  1.00 60.28  ? 155 LYS A CD  1 
ATOM   845  C CE  . LYS A 1 140 ? -31.929 5.539  39.271  1.00 71.15  ? 155 LYS A CE  1 
ATOM   846  N NZ  . LYS A 1 140 ? -32.706 4.490  38.544  1.00 73.21  ? 155 LYS A NZ  1 
ATOM   847  N N   . LEU A 1 141 ? -28.131 9.330  42.493  1.00 44.38  ? 156 LEU A N   1 
ATOM   848  C CA  . LEU A 1 141 ? -27.163 10.311 42.032  1.00 40.90  ? 156 LEU A CA  1 
ATOM   849  C C   . LEU A 1 141 ? -25.852 10.165 42.792  1.00 41.69  ? 156 LEU A C   1 
ATOM   850  O O   . LEU A 1 141 ? -25.832 9.798  43.971  1.00 40.55  ? 156 LEU A O   1 
ATOM   851  C CB  . LEU A 1 141 ? -27.709 11.729 42.213  1.00 39.36  ? 156 LEU A CB  1 
ATOM   852  C CG  . LEU A 1 141 ? -29.038 12.053 41.528  1.00 39.64  ? 156 LEU A CG  1 
ATOM   853  C CD1 . LEU A 1 141 ? -29.569 13.396 41.996  1.00 37.96  ? 156 LEU A CD1 1 
ATOM   854  C CD2 . LEU A 1 141 ? -28.892 12.029 40.016  1.00 39.06  ? 156 LEU A CD2 1 
ATOM   855  N N   . ASN A 1 142 ? -24.748 10.453 42.103  1.00 35.82  ? 157 ASN A N   1 
ATOM   856  C CA  . ASN A 1 142 ? -23.473 10.539 42.793  1.00 37.49  ? 157 ASN A CA  1 
ATOM   857  C C   . ASN A 1 142 ? -23.426 11.825 43.622  1.00 38.79  ? 157 ASN A C   1 
ATOM   858  O O   . ASN A 1 142 ? -24.257 12.724 43.468  1.00 35.33  ? 157 ASN A O   1 
ATOM   859  C CB  . ASN A 1 142 ? -22.306 10.445 41.801  1.00 33.43  ? 157 ASN A CB  1 
ATOM   860  C CG  . ASN A 1 142 ? -22.334 11.532 40.728  1.00 40.53  ? 157 ASN A CG  1 
ATOM   861  O OD1 . ASN A 1 142 ? -22.481 12.720 41.024  1.00 38.35  ? 157 ASN A OD1 1 
ATOM   862  N ND2 . ASN A 1 142 ? -22.175 11.122 39.470  1.00 33.14  ? 157 ASN A ND2 1 
ATOM   863  N N   . ASP A 1 143 ? -22.442 11.894 44.525  1.00 42.68  ? 158 ASP A N   1 
ATOM   864  C CA  . ASP A 1 143 ? -22.405 12.968 45.517  1.00 39.85  ? 158 ASP A CA  1 
ATOM   865  C C   . ASP A 1 143 ? -22.449 14.341 44.858  1.00 38.90  ? 158 ASP A C   1 
ATOM   866  O O   . ASP A 1 143 ? -23.207 15.223 45.279  1.00 36.69  ? 158 ASP A O   1 
ATOM   867  C CB  . ASP A 1 143 ? -21.152 12.842 46.385  1.00 42.54  ? 158 ASP A CB  1 
ATOM   868  C CG  . ASP A 1 143 ? -21.072 11.516 47.112  1.00 42.80  ? 158 ASP A CG  1 
ATOM   869  O OD1 . ASP A 1 143 ? -22.122 10.853 47.262  1.00 40.52  ? 158 ASP A OD1 1 
ATOM   870  O OD2 . ASP A 1 143 ? -19.957 11.143 47.539  1.00 42.93  ? 158 ASP A OD2 1 
ATOM   871  N N   . ILE A 1 144 ? -21.637 14.540 43.820  1.00 36.46  ? 159 ILE A N   1 
ATOM   872  C CA  . ILE A 1 144 ? -21.572 15.843 43.164  1.00 38.33  ? 159 ILE A CA  1 
ATOM   873  C C   . ILE A 1 144 ? -22.921 16.188 42.542  1.00 37.53  ? 159 ILE A C   1 
ATOM   874  O O   . ILE A 1 144 ? -23.441 17.299 42.713  1.00 30.42  ? 159 ILE A O   1 
ATOM   875  C CB  . ILE A 1 144 ? -20.436 15.854 42.125  1.00 35.40  ? 159 ILE A CB  1 
ATOM   876  C CG1 . ILE A 1 144 ? -19.085 16.032 42.822  1.00 29.38  ? 159 ILE A CG1 1 
ATOM   877  C CG2 . ILE A 1 144 ? -20.664 16.921 41.064  1.00 28.23  ? 159 ILE A CG2 1 
ATOM   878  C CD1 . ILE A 1 144 ? -17.897 15.710 41.934  1.00 33.36  ? 159 ILE A CD1 1 
ATOM   879  N N   . ALA A 1 145 ? -23.515 15.230 41.826  1.00 35.66  ? 160 ALA A N   1 
ATOM   880  C CA  . ALA A 1 145 ? -24.808 15.471 41.195  1.00 36.88  ? 160 ALA A CA  1 
ATOM   881  C C   . ALA A 1 145 ? -25.910 15.657 42.229  1.00 39.18  ? 160 ALA A C   1 
ATOM   882  O O   . ALA A 1 145 ? -26.876 16.391 41.979  1.00 36.45  ? 160 ALA A O   1 
ATOM   883  C CB  . ALA A 1 145 ? -25.151 14.325 40.243  1.00 34.26  ? 160 ALA A CB  1 
ATOM   884  N N   . LEU A 1 146 ? -25.785 15.012 43.392  1.00 34.08  ? 161 LEU A N   1 
ATOM   885  C CA  . LEU A 1 146 ? -26.758 15.232 44.455  1.00 34.02  ? 161 LEU A CA  1 
ATOM   886  C C   . LEU A 1 146 ? -26.694 16.668 44.960  1.00 37.31  ? 161 LEU A C   1 
ATOM   887  O O   . LEU A 1 146 ? -27.731 17.315 45.142  1.00 38.31  ? 161 LEU A O   1 
ATOM   888  C CB  . LEU A 1 146 ? -26.529 14.241 45.597  1.00 32.21  ? 161 LEU A CB  1 
ATOM   889  C CG  . LEU A 1 146 ? -27.512 14.320 46.769  1.00 35.84  ? 161 LEU A CG  1 
ATOM   890  C CD1 . LEU A 1 146 ? -28.927 14.083 46.288  1.00 36.89  ? 161 LEU A CD1 1 
ATOM   891  C CD2 . LEU A 1 146 ? -27.147 13.322 47.856  1.00 38.38  ? 161 LEU A CD2 1 
ATOM   892  N N   . CYS A 1 147 ? -25.483 17.190 45.169  1.00 36.01  ? 162 CYS A N   1 
ATOM   893  C CA  . CYS A 1 147 ? -25.338 18.575 45.610  1.00 37.05  ? 162 CYS A CA  1 
ATOM   894  C C   . CYS A 1 147 ? -25.860 19.544 44.556  1.00 32.18  ? 162 CYS A C   1 
ATOM   895  O O   . CYS A 1 147 ? -26.591 20.489 44.875  1.00 34.63  ? 162 CYS A O   1 
ATOM   896  C CB  . CYS A 1 147 ? -23.871 18.870 45.937  1.00 31.96  ? 162 CYS A CB  1 
ATOM   897  S SG  . CYS A 1 147 ? -23.425 20.636 45.935  1.00 32.41  ? 162 CYS A SG  1 
ATOM   898  N N   . ARG A 1 148 ? -25.489 19.328 43.291  1.00 29.61  ? 163 ARG A N   1 
ATOM   899  C CA  . ARG A 1 148 ? -25.989 20.180 42.216  1.00 35.24  ? 163 ARG A CA  1 
ATOM   900  C C   . ARG A 1 148 ? -27.512 20.176 42.187  1.00 38.18  ? 163 ARG A C   1 
ATOM   901  O O   . ARG A 1 148 ? -28.147 21.235 42.116  1.00 32.72  ? 163 ARG A O   1 
ATOM   902  C CB  . ARG A 1 148 ? -25.435 19.720 40.866  1.00 33.31  ? 163 ARG A CB  1 
ATOM   903  C CG  . ARG A 1 148 ? -25.482 20.794 39.777  1.00 39.46  ? 163 ARG A CG  1 
ATOM   904  C CD  . ARG A 1 148 ? -26.804 20.833 38.993  1.00 30.69  ? 163 ARG A CD  1 
ATOM   905  N NE  . ARG A 1 148 ? -27.431 19.526 38.840  1.00 35.94  ? 163 ARG A NE  1 
ATOM   906  C CZ  . ARG A 1 148 ? -28.630 19.331 38.302  1.00 39.24  ? 163 ARG A CZ  1 
ATOM   907  N NH1 . ARG A 1 148 ? -29.363 20.342 37.864  1.00 33.88  ? 163 ARG A NH1 1 
ATOM   908  N NH2 . ARG A 1 148 ? -29.102 18.092 38.195  1.00 38.16  ? 163 ARG A NH2 1 
ATOM   909  N N   . THR A 1 149 ? -28.112 18.985 42.258  1.00 35.51  ? 164 THR A N   1 
ATOM   910  C CA  . THR A 1 149 ? -29.563 18.874 42.174  1.00 36.78  ? 164 THR A CA  1 
ATOM   911  C C   . THR A 1 149 ? -30.237 19.548 43.363  1.00 34.68  ? 164 THR A C   1 
ATOM   912  O O   . THR A 1 149 ? -31.281 20.192 43.208  1.00 36.64  ? 164 THR A O   1 
ATOM   913  C CB  . THR A 1 149 ? -29.972 17.403 42.076  1.00 36.70  ? 164 THR A CB  1 
ATOM   914  O OG1 . THR A 1 149 ? -29.474 16.854 40.846  1.00 39.63  ? 164 THR A OG1 1 
ATOM   915  C CG2 . THR A 1 149 ? -31.481 17.268 42.104  1.00 38.15  ? 164 THR A CG2 1 
ATOM   916  N N   . HIS A 1 150 ? -29.648 19.433 44.552  1.00 34.61  ? 165 HIS A N   1 
ATOM   917  C CA  . HIS A 1 150 ? -30.199 20.123 45.714  1.00 34.86  ? 165 HIS A CA  1 
ATOM   918  C C   . HIS A 1 150 ? -30.147 21.632 45.520  1.00 34.05  ? 165 HIS A C   1 
ATOM   919  O O   . HIS A 1 150 ? -31.160 22.324 45.665  1.00 35.70  ? 165 HIS A O   1 
ATOM   920  C CB  . HIS A 1 150 ? -29.437 19.712 46.974  1.00 33.85  ? 165 HIS A CB  1 
ATOM   921  C CG  . HIS A 1 150 ? -29.692 20.597 48.154  1.00 34.83  ? 165 HIS A CG  1 
ATOM   922  N ND1 . HIS A 1 150 ? -30.780 20.434 48.985  1.00 32.24  ? 165 HIS A ND1 1 
ATOM   923  C CD2 . HIS A 1 150 ? -28.990 21.641 48.655  1.00 29.83  ? 165 HIS A CD2 1 
ATOM   924  C CE1 . HIS A 1 150 ? -30.741 21.343 49.942  1.00 35.96  ? 165 HIS A CE1 1 
ATOM   925  N NE2 . HIS A 1 150 ? -29.666 22.090 49.764  1.00 34.47  ? 165 HIS A NE2 1 
ATOM   926  N N   . ALA A 1 151 ? -28.967 22.154 45.170  1.00 34.83  ? 166 ALA A N   1 
ATOM   927  C CA  . ALA A 1 151 ? -28.801 23.592 44.982  1.00 35.69  ? 166 ALA A CA  1 
ATOM   928  C C   . ALA A 1 151 ? -29.683 24.113 43.854  1.00 33.98  ? 166 ALA A C   1 
ATOM   929  O O   . ALA A 1 151 ? -30.359 25.137 44.002  1.00 31.83  ? 166 ALA A O   1 
ATOM   930  C CB  . ALA A 1 151 ? -27.335 23.913 44.698  1.00 35.38  ? 166 ALA A CB  1 
ATOM   931  N N   . ALA A 1 152 ? -29.682 23.426 42.711  1.00 30.34  ? 167 ALA A N   1 
ATOM   932  C CA  . ALA A 1 152 ? -30.381 23.938 41.539  1.00 36.09  ? 167 ALA A CA  1 
ATOM   933  C C   . ALA A 1 152 ? -31.894 23.788 41.636  1.00 34.23  ? 167 ALA A C   1 
ATOM   934  O O   . ALA A 1 152 ? -32.617 24.472 40.906  1.00 33.41  ? 167 ALA A O   1 
ATOM   935  C CB  . ALA A 1 152 ? -29.871 23.241 40.274  1.00 32.75  ? 167 ALA A CB  1 
ATOM   936  N N   . SER A 1 153 ? -32.391 22.920 42.516  1.00 31.73  ? 168 SER A N   1 
ATOM   937  C CA  . SER A 1 153 ? -33.826 22.702 42.609  1.00 38.06  ? 168 SER A CA  1 
ATOM   938  C C   . SER A 1 153 ? -34.544 23.824 43.345  1.00 39.83  ? 168 SER A C   1 
ATOM   939  O O   . SER A 1 153 ? -35.773 23.916 43.257  1.00 37.82  ? 168 SER A O   1 
ATOM   940  C CB  . SER A 1 153 ? -34.111 21.371 43.307  1.00 38.88  ? 168 SER A CB  1 
ATOM   941  O OG  . SER A 1 153 ? -33.898 20.285 42.419  1.00 41.95  ? 168 SER A OG  1 
ATOM   942  N N   . PHE A 1 154 ? -33.813 24.669 44.064  1.00 36.68  ? 169 PHE A N   1 
ATOM   943  C CA  . PHE A 1 154 ? -34.447 25.712 44.856  1.00 36.40  ? 169 PHE A CA  1 
ATOM   944  C C   . PHE A 1 154 ? -34.963 26.821 43.952  1.00 40.86  ? 169 PHE A C   1 
ATOM   945  O O   . PHE A 1 154 ? -34.208 27.398 43.160  1.00 38.17  ? 169 PHE A O   1 
ATOM   946  C CB  . PHE A 1 154 ? -33.472 26.271 45.890  1.00 34.34  ? 169 PHE A CB  1 
ATOM   947  C CG  . PHE A 1 154 ? -33.393 25.455 47.140  1.00 36.88  ? 169 PHE A CG  1 
ATOM   948  C CD1 . PHE A 1 154 ? -34.454 25.431 48.032  1.00 34.92  ? 169 PHE A CD1 1 
ATOM   949  C CD2 . PHE A 1 154 ? -32.265 24.707 47.426  1.00 35.16  ? 169 PHE A CD2 1 
ATOM   950  C CE1 . PHE A 1 154 ? -34.388 24.677 49.192  1.00 35.47  ? 169 PHE A CE1 1 
ATOM   951  C CE2 . PHE A 1 154 ? -32.193 23.950 48.587  1.00 34.77  ? 169 PHE A CE2 1 
ATOM   952  C CZ  . PHE A 1 154 ? -33.254 23.935 49.470  1.00 33.52  ? 169 PHE A CZ  1 
ATOM   953  N N   . VAL A 1 155 ? -36.254 27.096 44.068  1.00 37.86  ? 170 VAL A N   1 
ATOM   954  C CA  . VAL A 1 155 ? -36.904 28.246 43.458  1.00 35.23  ? 170 VAL A CA  1 
ATOM   955  C C   . VAL A 1 155 ? -37.095 29.301 44.537  1.00 34.26  ? 170 VAL A C   1 
ATOM   956  O O   . VAL A 1 155 ? -37.356 28.969 45.701  1.00 37.34  ? 170 VAL A O   1 
ATOM   957  C CB  . VAL A 1 155 ? -38.256 27.833 42.839  1.00 43.57  ? 170 VAL A CB  1 
ATOM   958  C CG1 . VAL A 1 155 ? -39.012 29.036 42.373  1.00 43.88  ? 170 VAL A CG1 1 
ATOM   959  C CG2 . VAL A 1 155 ? -38.049 26.860 41.689  1.00 39.61  ? 170 VAL A CG2 1 
ATOM   960  N N   . MET A 1 156 ? -36.950 30.569 44.169  1.00 36.99  ? 171 MET A N   1 
ATOM   961  C CA  . MET A 1 156 ? -37.302 31.639 45.091  1.00 45.16  ? 171 MET A CA  1 
ATOM   962  C C   . MET A 1 156 ? -38.809 31.855 45.075  1.00 41.69  ? 171 MET A C   1 
ATOM   963  O O   . MET A 1 156 ? -39.442 31.838 44.015  1.00 43.09  ? 171 MET A O   1 
ATOM   964  C CB  . MET A 1 156 ? -36.576 32.940 44.743  1.00 44.26  ? 171 MET A CB  1 
ATOM   965  C CG  . MET A 1 156 ? -36.776 34.034 45.791  1.00 45.80  ? 171 MET A CG  1 
ATOM   966  S SD  . MET A 1 156 ? -36.139 35.648 45.303  1.00 47.71  ? 171 MET A SD  1 
ATOM   967  C CE  . MET A 1 156 ? -37.362 36.171 44.106  1.00 49.45  ? 171 MET A CE  1 
ATOM   968  N N   . ALA A 1 157 ? -39.380 32.059 46.268  1.00 45.02  ? 172 ALA A N   1 
ATOM   969  C CA  . ALA A 1 157 ? -40.833 32.089 46.424  1.00 47.37  ? 172 ALA A CA  1 
ATOM   970  C C   . ALA A 1 157 ? -41.500 33.082 45.481  1.00 54.24  ? 172 ALA A C   1 
ATOM   971  O O   . ALA A 1 157 ? -42.687 32.936 45.164  1.00 56.75  ? 172 ALA A O   1 
ATOM   972  C CB  . ALA A 1 157 ? -41.198 32.409 47.873  1.00 39.19  ? 172 ALA A CB  1 
ATOM   973  N N   . GLY A 1 158 ? -40.760 34.081 45.009  1.00 55.97  ? 173 GLY A N   1 
ATOM   974  C CA  . GLY A 1 158 ? -41.289 35.079 44.105  1.00 61.59  ? 173 GLY A CA  1 
ATOM   975  C C   . GLY A 1 158 ? -40.897 34.945 42.647  1.00 63.16  ? 173 GLY A C   1 
ATOM   976  O O   . GLY A 1 158 ? -41.209 35.846 41.860  1.00 68.13  ? 173 GLY A O   1 
ATOM   977  N N   . ASP A 1 159 ? -40.224 33.862 42.250  1.00 62.88  ? 174 ASP A N   1 
ATOM   978  C CA  . ASP A 1 159 ? -39.845 33.693 40.849  1.00 62.48  ? 174 ASP A CA  1 
ATOM   979  C C   . ASP A 1 159 ? -40.186 32.300 40.332  1.00 60.06  ? 174 ASP A C   1 
ATOM   980  O O   . ASP A 1 159 ? -39.526 31.794 39.421  1.00 66.16  ? 174 ASP A O   1 
ATOM   981  C CB  . ASP A 1 159 ? -38.361 34.031 40.619  1.00 54.68  ? 174 ASP A CB  1 
ATOM   982  C CG  . ASP A 1 159 ? -37.373 32.984 41.189  1.00 64.15  ? 174 ASP A CG  1 
ATOM   983  O OD1 . ASP A 1 159 ? -37.567 31.754 41.074  1.00 62.75  ? 174 ASP A OD1 1 
ATOM   984  O OD2 . ASP A 1 159 ? -36.330 33.425 41.727  1.00 72.16  ? 174 ASP A OD2 1 
ATOM   985  N N   . GLN A 1 160 ? -41.260 31.700 40.848  1.00 58.45  ? 175 GLN A N   1 
ATOM   986  C CA  . GLN A 1 160 ? -41.547 30.293 40.573  1.00 60.56  ? 175 GLN A CA  1 
ATOM   987  C C   . GLN A 1 160 ? -41.576 29.958 39.084  1.00 63.06  ? 175 GLN A C   1 
ATOM   988  O O   . GLN A 1 160 ? -41.514 28.776 38.726  1.00 67.89  ? 175 GLN A O   1 
ATOM   989  C CB  . GLN A 1 160 ? -42.858 29.906 41.260  1.00 65.21  ? 175 GLN A CB  1 
ATOM   990  C CG  . GLN A 1 160 ? -42.739 29.947 42.781  1.00 64.35  ? 175 GLN A CG  1 
ATOM   991  C CD  . GLN A 1 160 ? -44.041 29.652 43.495  1.00 83.16  ? 175 GLN A CD  1 
ATOM   992  O OE1 . GLN A 1 160 ? -45.125 29.815 42.930  1.00 91.83  ? 175 GLN A OE1 1 
ATOM   993  N NE2 . GLN A 1 160 ? -43.942 29.231 44.756  1.00 66.69  ? 175 GLN A NE2 1 
ATOM   994  N N   . ASN A 1 161 ? -41.622 30.966 38.209  1.00 59.39  ? 176 ASN A N   1 
ATOM   995  C CA  . ASN A 1 161 ? -41.566 30.763 36.766  1.00 58.65  ? 176 ASN A CA  1 
ATOM   996  C C   . ASN A 1 161 ? -40.248 31.232 36.151  1.00 63.38  ? 176 ASN A C   1 
ATOM   997  O O   . ASN A 1 161 ? -40.171 31.405 34.929  1.00 62.96  ? 176 ASN A O   1 
ATOM   998  C CB  . ASN A 1 161 ? -42.735 31.475 36.086  1.00 55.98  ? 176 ASN A CB  1 
ATOM   999  C CG  . ASN A 1 161 ? -44.080 31.073 36.660  1.00 64.78  ? 176 ASN A CG  1 
ATOM   1000 O OD1 . ASN A 1 161 ? -44.701 30.113 36.201  1.00 57.16  ? 176 ASN A OD1 1 
ATOM   1001 N ND2 . ASN A 1 161 ? -44.542 31.812 37.665  1.00 67.02  ? 176 ASN A ND2 1 
ATOM   1002 N N   . SER A 1 162 ? -39.210 31.438 36.957  1.00 51.81  ? 177 SER A N   1 
ATOM   1003 C CA  . SER A 1 162 ? -37.973 32.031 36.469  1.00 52.44  ? 177 SER A CA  1 
ATOM   1004 C C   . SER A 1 162 ? -36.949 30.970 36.093  1.00 47.26  ? 177 SER A C   1 
ATOM   1005 O O   . SER A 1 162 ? -36.945 29.858 36.627  1.00 47.82  ? 177 SER A O   1 
ATOM   1006 C CB  . SER A 1 162 ? -37.359 32.965 37.509  1.00 51.63  ? 177 SER A CB  1 
ATOM   1007 O OG  . SER A 1 162 ? -36.118 33.469 37.052  1.00 44.66  ? 177 SER A OG  1 
ATOM   1008 N N   . ASN A 1 163 ? -36.067 31.341 35.166  1.00 45.91  ? 178 ASN A N   1 
ATOM   1009 C CA  . ASN A 1 163 ? -34.940 30.508 34.770  1.00 46.10  ? 178 ASN A CA  1 
ATOM   1010 C C   . ASN A 1 163 ? -33.761 30.617 35.731  1.00 43.83  ? 178 ASN A C   1 
ATOM   1011 O O   . ASN A 1 163 ? -32.781 29.879 35.577  1.00 47.09  ? 178 ASN A O   1 
ATOM   1012 C CB  . ASN A 1 163 ? -34.492 30.890 33.358  1.00 39.07  ? 178 ASN A CB  1 
ATOM   1013 C CG  . ASN A 1 163 ? -33.525 29.892 32.767  1.00 50.97  ? 178 ASN A CG  1 
ATOM   1014 O OD1 . ASN A 1 163 ? -33.786 28.687 32.768  1.00 56.25  ? 178 ASN A OD1 1 
ATOM   1015 N ND2 . ASN A 1 163 ? -32.388 30.383 32.274  1.00 42.79  ? 178 ASN A ND2 1 
ATOM   1016 N N   . TYR A 1 164 ? -33.835 31.510 36.713  1.00 44.29  ? 179 TYR A N   1 
ATOM   1017 C CA  . TYR A 1 164 ? -32.730 31.741 37.633  1.00 38.29  ? 179 TYR A CA  1 
ATOM   1018 C C   . TYR A 1 164 ? -32.646 30.593 38.632  1.00 39.57  ? 179 TYR A C   1 
ATOM   1019 O O   . TYR A 1 164 ? -33.581 30.367 39.407  1.00 38.79  ? 179 TYR A O   1 
ATOM   1020 C CB  . TYR A 1 164 ? -32.918 33.078 38.350  1.00 34.91  ? 179 TYR A CB  1 
ATOM   1021 C CG  . TYR A 1 164 ? -31.731 33.549 39.165  1.00 35.57  ? 179 TYR A CG  1 
ATOM   1022 C CD1 . TYR A 1 164 ? -31.335 32.876 40.314  1.00 29.62  ? 179 TYR A CD1 1 
ATOM   1023 C CD2 . TYR A 1 164 ? -31.015 34.679 38.792  1.00 34.17  ? 179 TYR A CD2 1 
ATOM   1024 C CE1 . TYR A 1 164 ? -30.259 33.302 41.056  1.00 32.79  ? 179 TYR A CE1 1 
ATOM   1025 C CE2 . TYR A 1 164 ? -29.933 35.114 39.531  1.00 36.31  ? 179 TYR A CE2 1 
ATOM   1026 C CZ  . TYR A 1 164 ? -29.562 34.419 40.662  1.00 35.92  ? 179 TYR A CZ  1 
ATOM   1027 O OH  . TYR A 1 164 ? -28.488 34.842 41.403  1.00 39.61  ? 179 TYR A OH  1 
ATOM   1028 N N   . ARG A 1 165 ? -31.524 29.875 38.612  1.00 35.88  ? 180 ARG A N   1 
ATOM   1029 C CA  . ARG A 1 165 ? -31.201 28.874 39.618  1.00 34.21  ? 180 ARG A CA  1 
ATOM   1030 C C   . ARG A 1 165 ? -29.736 29.039 40.005  1.00 38.07  ? 180 ARG A C   1 
ATOM   1031 O O   . ARG A 1 165 ? -28.890 29.372 39.168  1.00 34.94  ? 180 ARG A O   1 
ATOM   1032 C CB  . ARG A 1 165 ? -31.471 27.445 39.120  1.00 35.15  ? 180 ARG A CB  1 
ATOM   1033 C CG  . ARG A 1 165 ? -32.890 27.196 38.618  1.00 34.93  ? 180 ARG A CG  1 
ATOM   1034 C CD  . ARG A 1 165 ? -33.904 27.229 39.756  1.00 33.18  ? 180 ARG A CD  1 
ATOM   1035 N NE  . ARG A 1 165 ? -35.251 26.953 39.277  1.00 32.41  ? 180 ARG A NE  1 
ATOM   1036 C CZ  . ARG A 1 165 ? -35.799 25.747 39.237  1.00 36.75  ? 180 ARG A CZ  1 
ATOM   1037 N NH1 . ARG A 1 165 ? -35.156 24.678 39.679  1.00 33.24  ? 180 ARG A NH1 1 
ATOM   1038 N NH2 . ARG A 1 165 ? -37.025 25.608 38.739  1.00 38.23  ? 180 ARG A NH2 1 
ATOM   1039 N N   . HIS A 1 166 ? -29.441 28.794 41.275  1.00 34.46  ? 181 HIS A N   1 
ATOM   1040 C CA  . HIS A 1 166 ? -28.132 29.180 41.784  1.00 35.08  ? 181 HIS A CA  1 
ATOM   1041 C C   . HIS A 1 166 ? -27.079 28.123 41.457  1.00 34.91  ? 181 HIS A C   1 
ATOM   1042 O O   . HIS A 1 166 ? -27.368 26.924 41.478  1.00 37.38  ? 181 HIS A O   1 
ATOM   1043 C CB  . HIS A 1 166 ? -28.188 29.398 43.292  1.00 33.09  ? 181 HIS A CB  1 
ATOM   1044 C CG  . HIS A 1 166 ? -29.144 30.470 43.705  1.00 35.31  ? 181 HIS A CG  1 
ATOM   1045 N ND1 . HIS A 1 166 ? -30.483 30.227 43.924  1.00 33.60  ? 181 HIS A ND1 1 
ATOM   1046 C CD2 . HIS A 1 166 ? -28.960 31.793 43.920  1.00 34.35  ? 181 HIS A CD2 1 
ATOM   1047 C CE1 . HIS A 1 166 ? -31.081 31.355 44.266  1.00 34.98  ? 181 HIS A CE1 1 
ATOM   1048 N NE2 . HIS A 1 166 ? -30.179 32.320 44.271  1.00 36.83  ? 181 HIS A NE2 1 
ATOM   1049 N N   . PRO A 1 167 ? -25.856 28.542 41.156  1.00 33.04  ? 182 PRO A N   1 
ATOM   1050 C CA  . PRO A 1 167 ? -24.746 27.593 41.086  1.00 34.42  ? 182 PRO A CA  1 
ATOM   1051 C C   . PRO A 1 167 ? -24.302 27.173 42.479  1.00 36.92  ? 182 PRO A C   1 
ATOM   1052 O O   . PRO A 1 167 ? -24.651 27.787 43.491  1.00 33.51  ? 182 PRO A O   1 
ATOM   1053 C CB  . PRO A 1 167 ? -23.651 28.386 40.369  1.00 35.01  ? 182 PRO A CB  1 
ATOM   1054 C CG  . PRO A 1 167 ? -23.924 29.803 40.755  1.00 32.47  ? 182 PRO A CG  1 
ATOM   1055 C CD  . PRO A 1 167 ? -25.421 29.929 40.920  1.00 32.76  ? 182 PRO A CD  1 
ATOM   1056 N N   . ALA A 1 168 ? -23.517 26.099 42.515  1.00 33.78  ? 183 ALA A N   1 
ATOM   1057 C CA  . ALA A 1 168 ? -23.088 25.518 43.777  1.00 32.70  ? 183 ALA A CA  1 
ATOM   1058 C C   . ALA A 1 168 ? -21.614 25.151 43.711  1.00 32.61  ? 183 ALA A C   1 
ATOM   1059 O O   . ALA A 1 168 ? -21.037 24.972 42.635  1.00 30.92  ? 183 ALA A O   1 
ATOM   1060 C CB  . ALA A 1 168 ? -23.906 24.275 44.141  1.00 28.51  ? 183 ALA A CB  1 
ATOM   1061 N N   . VAL A 1 169 ? -21.011 25.053 44.891  1.00 32.59  ? 184 VAL A N   1 
ATOM   1062 C CA  . VAL A 1 169 ? -19.668 24.523 45.061  1.00 33.31  ? 184 VAL A CA  1 
ATOM   1063 C C   . VAL A 1 169 ? -19.770 23.331 45.998  1.00 34.08  ? 184 VAL A C   1 
ATOM   1064 O O   . VAL A 1 169 ? -20.214 23.470 47.145  1.00 31.83  ? 184 VAL A O   1 
ATOM   1065 C CB  . VAL A 1 169 ? -18.691 25.572 45.617  1.00 32.30  ? 184 VAL A CB  1 
ATOM   1066 C CG1 . VAL A 1 169 ? -17.334 24.930 45.892  1.00 31.02  ? 184 VAL A CG1 1 
ATOM   1067 C CG2 . VAL A 1 169 ? -18.550 26.745 44.649  1.00 30.17  ? 184 VAL A CG2 1 
ATOM   1068 N N   . TYR A 1 170 ? -19.379 22.162 45.510  1.00 33.03  ? 185 TYR A N   1 
ATOM   1069 C CA  . TYR A 1 170 ? -19.309 20.972 46.344  1.00 34.01  ? 185 TYR A CA  1 
ATOM   1070 C C   . TYR A 1 170 ? -17.867 20.748 46.777  1.00 36.81  ? 185 TYR A C   1 
ATOM   1071 O O   . TYR A 1 170 ? -16.958 20.703 45.940  1.00 32.83  ? 185 TYR A O   1 
ATOM   1072 C CB  . TYR A 1 170 ? -19.840 19.742 45.615  1.00 29.39  ? 185 TYR A CB  1 
ATOM   1073 C CG  . TYR A 1 170 ? -19.780 18.511 46.475  1.00 39.48  ? 185 TYR A CG  1 
ATOM   1074 C CD1 . TYR A 1 170 ? -20.584 18.397 47.605  1.00 36.75  ? 185 TYR A CD1 1 
ATOM   1075 C CD2 . TYR A 1 170 ? -18.894 17.474 46.181  1.00 36.48  ? 185 TYR A CD2 1 
ATOM   1076 C CE1 . TYR A 1 170 ? -20.522 17.277 48.406  1.00 38.83  ? 185 TYR A CE1 1 
ATOM   1077 C CE2 . TYR A 1 170 ? -18.829 16.348 46.974  1.00 36.53  ? 185 TYR A CE2 1 
ATOM   1078 C CZ  . TYR A 1 170 ? -19.644 16.256 48.084  1.00 36.36  ? 185 TYR A CZ  1 
ATOM   1079 O OH  . TYR A 1 170 ? -19.585 15.141 48.884  1.00 41.18  ? 185 TYR A OH  1 
ATOM   1080 N N   . ASP A 1 171 ? -17.664 20.628 48.086  1.00 37.38  ? 186 ASP A N   1 
ATOM   1081 C CA  . ASP A 1 171 ? -16.348 20.436 48.681  1.00 34.24  ? 186 ASP A CA  1 
ATOM   1082 C C   . ASP A 1 171 ? -16.151 18.941 48.893  1.00 36.69  ? 186 ASP A C   1 
ATOM   1083 O O   . ASP A 1 171 ? -16.756 18.356 49.794  1.00 36.46  ? 186 ASP A O   1 
ATOM   1084 C CB  . ASP A 1 171 ? -16.250 21.204 49.998  1.00 37.74  ? 186 ASP A CB  1 
ATOM   1085 C CG  . ASP A 1 171 ? -14.845 21.224 50.573  1.00 39.03  ? 186 ASP A CG  1 
ATOM   1086 O OD1 . ASP A 1 171 ? -14.068 20.276 50.328  1.00 38.42  ? 186 ASP A OD1 1 
ATOM   1087 O OD2 . ASP A 1 171 ? -14.524 22.197 51.290  1.00 39.99  ? 186 ASP A OD2 1 
ATOM   1088 N N   . GLU A 1 172 ? -15.292 18.327 48.073  1.00 37.48  ? 187 GLU A N   1 
ATOM   1089 C CA  . GLU A 1 172 ? -15.131 16.876 48.130  1.00 36.69  ? 187 GLU A CA  1 
ATOM   1090 C C   . GLU A 1 172 ? -14.391 16.432 49.383  1.00 36.32  ? 187 GLU A C   1 
ATOM   1091 O O   . GLU A 1 172 ? -14.607 15.314 49.860  1.00 36.90  ? 187 GLU A O   1 
ATOM   1092 C CB  . GLU A 1 172 ? -14.402 16.370 46.883  1.00 31.60  ? 187 GLU A CB  1 
ATOM   1093 C CG  . GLU A 1 172 ? -15.336 16.040 45.729  1.00 40.27  ? 187 GLU A CG  1 
ATOM   1094 C CD  . GLU A 1 172 ? -14.672 15.219 44.645  1.00 45.43  ? 187 GLU A CD  1 
ATOM   1095 O OE1 . GLU A 1 172 ? -13.467 15.426 44.393  1.00 48.15  ? 187 GLU A OE1 1 
ATOM   1096 O OE2 . GLU A 1 172 ? -15.357 14.360 44.048  1.00 48.77  ? 187 GLU A OE2 1 
ATOM   1097 N N   . LYS A 1 173 ? -13.513 17.276 49.926  1.00 39.08  ? 188 LYS A N   1 
ATOM   1098 C CA  . LYS A 1 173 ? -12.821 16.908 51.156  1.00 38.09  ? 188 LYS A CA  1 
ATOM   1099 C C   . LYS A 1 173 ? -13.764 16.991 52.350  1.00 39.42  ? 188 LYS A C   1 
ATOM   1100 O O   . LYS A 1 173 ? -13.841 16.059 53.159  1.00 37.07  ? 188 LYS A O   1 
ATOM   1101 C CB  . LYS A 1 173 ? -11.597 17.802 51.367  1.00 39.68  ? 188 LYS A CB  1 
ATOM   1102 C CG  . LYS A 1 173 ? -10.994 17.706 52.765  1.00 42.73  ? 188 LYS A CG  1 
ATOM   1103 C CD  . LYS A 1 173 ? -9.587  18.283 52.817  1.00 39.68  ? 188 LYS A CD  1 
ATOM   1104 C CE  . LYS A 1 173 ? -9.367  19.084 54.100  1.00 50.64  ? 188 LYS A CE  1 
ATOM   1105 N NZ  . LYS A 1 173 ? -7.915  19.298 54.414  1.00 51.98  ? 188 LYS A NZ  1 
ATOM   1106 N N   . GLU A 1 174 ? -14.496 18.096 52.470  1.00 38.61  ? 189 GLU A N   1 
ATOM   1107 C CA  . GLU A 1 174 ? -15.431 18.292 53.568  1.00 36.71  ? 189 GLU A CA  1 
ATOM   1108 C C   . GLU A 1 174 ? -16.807 17.695 53.303  1.00 37.64  ? 189 GLU A C   1 
ATOM   1109 O O   . GLU A 1 174 ? -17.653 17.722 54.202  1.00 38.52  ? 189 GLU A O   1 
ATOM   1110 C CB  . GLU A 1 174 ? -15.570 19.784 53.880  1.00 36.95  ? 189 GLU A CB  1 
ATOM   1111 C CG  . GLU A 1 174 ? -14.238 20.461 54.095  1.00 39.97  ? 189 GLU A CG  1 
ATOM   1112 C CD  . GLU A 1 174 ? -13.567 19.992 55.371  1.00 46.89  ? 189 GLU A CD  1 
ATOM   1113 O OE1 . GLU A 1 174 ? -14.287 19.577 56.305  1.00 46.59  ? 189 GLU A OE1 1 
ATOM   1114 O OE2 . GLU A 1 174 ? -12.321 20.022 55.435  1.00 52.42  ? 189 GLU A OE2 1 
ATOM   1115 N N   . LYS A 1 175 ? -17.046 17.153 52.106  1.00 37.28  ? 190 LYS A N   1 
ATOM   1116 C CA  . LYS A 1 175 ? -18.339 16.562 51.751  1.00 38.43  ? 190 LYS A CA  1 
ATOM   1117 C C   . LYS A 1 175 ? -19.478 17.542 52.027  1.00 35.67  ? 190 LYS A C   1 
ATOM   1118 O O   . LYS A 1 175 ? -20.480 17.211 52.662  1.00 41.21  ? 190 LYS A O   1 
ATOM   1119 C CB  . LYS A 1 175 ? -18.561 15.245 52.496  1.00 40.15  ? 190 LYS A CB  1 
ATOM   1120 C CG  . LYS A 1 175 ? -17.542 14.174 52.181  1.00 38.03  ? 190 LYS A CG  1 
ATOM   1121 C CD  . LYS A 1 175 ? -18.207 12.816 52.073  1.00 46.62  ? 190 LYS A CD  1 
ATOM   1122 C CE  . LYS A 1 175 ? -17.179 11.705 52.062  1.00 52.85  ? 190 LYS A CE  1 
ATOM   1123 N NZ  . LYS A 1 175 ? -16.028 12.038 52.950  1.00 59.91  ? 190 LYS A NZ  1 
ATOM   1124 N N   . THR A 1 176 ? -19.308 18.776 51.560  1.00 37.03  ? 191 THR A N   1 
ATOM   1125 C CA  . THR A 1 176 ? -20.236 19.848 51.885  1.00 37.03  ? 191 THR A CA  1 
ATOM   1126 C C   . THR A 1 176 ? -20.611 20.623 50.630  1.00 34.66  ? 191 THR A C   1 
ATOM   1127 O O   . THR A 1 176 ? -19.759 20.919 49.786  1.00 35.05  ? 191 THR A O   1 
ATOM   1128 C CB  . THR A 1 176 ? -19.642 20.781 52.939  1.00 36.51  ? 191 THR A CB  1 
ATOM   1129 O OG1 . THR A 1 176 ? -19.396 20.026 54.131  1.00 34.87  ? 191 THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 176 ? -20.611 21.924 53.265  1.00 26.98  ? 191 THR A CG2 1 
ATOM   1131 N N   . CYS A 1 177 ? -21.899 20.934 50.522  1.00 36.05  ? 192 CYS A N   1 
ATOM   1132 C CA  . CYS A 1 177 ? -22.498 21.592 49.368  1.00 33.05  ? 192 CYS A CA  1 
ATOM   1133 C C   . CYS A 1 177 ? -22.809 23.034 49.742  1.00 33.64  ? 192 CYS A C   1 
ATOM   1134 O O   . CYS A 1 177 ? -23.605 23.281 50.655  1.00 34.26  ? 192 CYS A O   1 
ATOM   1135 C CB  . CYS A 1 177 ? -23.771 20.853 48.944  1.00 32.37  ? 192 CYS A CB  1 
ATOM   1136 S SG  . CYS A 1 177 ? -24.546 21.440 47.431  1.00 34.49  ? 192 CYS A SG  1 
ATOM   1137 N N   . HIS A 1 178 ? -22.179 23.977 49.050  1.00 36.37  ? 193 HIS A N   1 
ATOM   1138 C CA  . HIS A 1 178 ? -22.378 25.400 49.291  1.00 33.99  ? 193 HIS A CA  1 
ATOM   1139 C C   . HIS A 1 178 ? -23.144 26.011 48.129  1.00 36.36  ? 193 HIS A C   1 
ATOM   1140 O O   . HIS A 1 178 ? -22.764 25.837 46.965  1.00 37.49  ? 193 HIS A O   1 
ATOM   1141 C CB  . HIS A 1 178 ? -21.041 26.126 49.457  1.00 34.10  ? 193 HIS A CB  1 
ATOM   1142 C CG  . HIS A 1 178 ? -20.157 25.528 50.503  1.00 36.47  ? 193 HIS A CG  1 
ATOM   1143 N ND1 . HIS A 1 178 ? -20.094 26.015 51.791  1.00 31.93  ? 193 HIS A ND1 1 
ATOM   1144 C CD2 . HIS A 1 178 ? -19.304 24.478 50.454  1.00 35.30  ? 193 HIS A CD2 1 
ATOM   1145 C CE1 . HIS A 1 178 ? -19.233 25.295 52.489  1.00 36.10  ? 193 HIS A CE1 1 
ATOM   1146 N NE2 . HIS A 1 178 ? -18.740 24.356 51.701  1.00 38.76  ? 193 HIS A NE2 1 
ATOM   1147 N N   . MET A 1 179 ? -24.209 26.731 48.444  1.00 33.77  ? 194 MET A N   1 
ATOM   1148 C CA  . MET A 1 179 ? -24.939 27.473 47.431  1.00 38.32  ? 194 MET A CA  1 
ATOM   1149 C C   . MET A 1 179 ? -24.373 28.886 47.334  1.00 38.15  ? 194 MET A C   1 
ATOM   1150 O O   . MET A 1 179 ? -24.071 29.514 48.353  1.00 33.21  ? 194 MET A O   1 
ATOM   1151 C CB  . MET A 1 179 ? -26.427 27.521 47.768  1.00 30.53  ? 194 MET A CB  1 
ATOM   1152 C CG  . MET A 1 179 ? -27.242 26.440 47.108  1.00 34.42  ? 194 MET A CG  1 
ATOM   1153 S SD  . MET A 1 179 ? -28.808 26.147 47.948  1.00 35.95  ? 194 MET A SD  1 
ATOM   1154 C CE  . MET A 1 179 ? -29.854 27.247 47.008  1.00 35.01  ? 194 MET A CE  1 
ATOM   1155 N N   . LEU A 1 180 ? -24.228 29.380 46.107  1.00 33.26  ? 195 LEU A N   1 
ATOM   1156 C CA  . LEU A 1 180 ? -23.682 30.711 45.877  1.00 35.56  ? 195 LEU A CA  1 
ATOM   1157 C C   . LEU A 1 180 ? -24.824 31.711 45.749  1.00 37.97  ? 195 LEU A C   1 
ATOM   1158 O O   . LEU A 1 180 ? -25.705 31.552 44.897  1.00 36.99  ? 195 LEU A O   1 
ATOM   1159 C CB  . LEU A 1 180 ? -22.792 30.733 44.637  1.00 35.70  ? 195 LEU A CB  1 
ATOM   1160 C CG  . LEU A 1 180 ? -21.568 29.814 44.709  1.00 37.16  ? 195 LEU A CG  1 
ATOM   1161 C CD1 . LEU A 1 180 ? -20.751 29.899 43.427  1.00 31.13  ? 195 LEU A CD1 1 
ATOM   1162 C CD2 . LEU A 1 180 ? -20.716 30.147 45.936  1.00 35.41  ? 195 LEU A CD2 1 
ATOM   1163 N N   . TYR A 1 181 ? -24.806 32.740 46.600  1.00 34.47  ? 196 TYR A N   1 
ATOM   1164 C CA  . TYR A 1 181 ? -25.903 33.702 46.632  1.00 34.94  ? 196 TYR A CA  1 
ATOM   1165 C C   . TYR A 1 181 ? -25.873 34.638 45.428  1.00 36.29  ? 196 TYR A C   1 
ATOM   1166 O O   . TYR A 1 181 ? -26.928 35.082 44.965  1.00 32.06  ? 196 TYR A O   1 
ATOM   1167 C CB  . TYR A 1 181 ? -25.849 34.496 47.940  1.00 33.64  ? 196 TYR A CB  1 
ATOM   1168 C CG  . TYR A 1 181 ? -27.129 35.218 48.290  1.00 35.36  ? 196 TYR A CG  1 
ATOM   1169 C CD1 . TYR A 1 181 ? -28.290 34.510 48.596  1.00 33.00  ? 196 TYR A CD1 1 
ATOM   1170 C CD2 . TYR A 1 181 ? -27.170 36.611 48.341  1.00 30.49  ? 196 TYR A CD2 1 
ATOM   1171 C CE1 . TYR A 1 181 ? -29.465 35.172 48.921  1.00 32.89  ? 196 TYR A CE1 1 
ATOM   1172 C CE2 . TYR A 1 181 ? -28.339 37.280 48.661  1.00 30.69  ? 196 TYR A CE2 1 
ATOM   1173 C CZ  . TYR A 1 181 ? -29.484 36.557 48.950  1.00 34.69  ? 196 TYR A CZ  1 
ATOM   1174 O OH  . TYR A 1 181 ? -30.647 37.224 49.277  1.00 33.94  ? 196 TYR A OH  1 
ATOM   1175 N N   . LEU A 1 182 ? -24.690 34.961 44.913  1.00 33.73  ? 197 LEU A N   1 
ATOM   1176 C CA  . LEU A 1 182 ? -24.577 35.787 43.722  1.00 40.45  ? 197 LEU A CA  1 
ATOM   1177 C C   . LEU A 1 182 ? -23.723 35.062 42.692  1.00 39.41  ? 197 LEU A C   1 
ATOM   1178 O O   . LEU A 1 182 ? -22.888 34.220 43.033  1.00 36.25  ? 197 LEU A O   1 
ATOM   1179 C CB  . LEU A 1 182 ? -23.997 37.177 44.040  1.00 38.83  ? 197 LEU A CB  1 
ATOM   1180 C CG  . LEU A 1 182 ? -22.540 37.310 44.475  1.00 39.59  ? 197 LEU A CG  1 
ATOM   1181 C CD1 . LEU A 1 182 ? -22.080 38.763 44.304  1.00 37.49  ? 197 LEU A CD1 1 
ATOM   1182 C CD2 . LEU A 1 182 ? -22.360 36.850 45.903  1.00 37.00  ? 197 LEU A CD2 1 
ATOM   1183 N N   . SER A 1 183 ? -23.960 35.383 41.422  1.00 38.28  ? 198 SER A N   1 
ATOM   1184 C CA  . SER A 1 183 ? -23.391 34.631 40.316  1.00 38.05  ? 198 SER A CA  1 
ATOM   1185 C C   . SER A 1 183 ? -22.112 35.239 39.757  1.00 38.18  ? 198 SER A C   1 
ATOM   1186 O O   . SER A 1 183 ? -21.418 34.567 38.986  1.00 34.40  ? 198 SER A O   1 
ATOM   1187 C CB  . SER A 1 183 ? -24.425 34.499 39.197  1.00 38.29  ? 198 SER A CB  1 
ATOM   1188 O OG  . SER A 1 183 ? -25.347 33.467 39.507  1.00 47.13  ? 198 SER A OG  1 
ATOM   1189 N N   . ALA A 1 184 ? -21.791 36.480 40.115  1.00 35.70  ? 199 ALA A N   1 
ATOM   1190 C CA  . ALA A 1 184 ? -20.587 37.121 39.610  1.00 36.99  ? 199 ALA A CA  1 
ATOM   1191 C C   . ALA A 1 184 ? -19.356 36.271 39.904  1.00 39.27  ? 199 ALA A C   1 
ATOM   1192 O O   . ALA A 1 184 ? -19.247 35.647 40.963  1.00 35.20  ? 199 ALA A O   1 
ATOM   1193 C CB  . ALA A 1 184 ? -20.432 38.510 40.231  1.00 32.95  ? 199 ALA A CB  1 
ATOM   1194 N N   . GLN A 1 185 ? -18.433 36.234 38.943  1.00 35.29  ? 200 GLN A N   1 
ATOM   1195 C CA  . GLN A 1 185 ? -17.184 35.509 39.111  1.00 40.24  ? 200 GLN A CA  1 
ATOM   1196 C C   . GLN A 1 185 ? -15.940 36.371 38.978  1.00 38.63  ? 200 GLN A C   1 
ATOM   1197 O O   . GLN A 1 185 ? -14.873 35.949 39.438  1.00 40.11  ? 200 GLN A O   1 
ATOM   1198 C CB  . GLN A 1 185 ? -17.086 34.357 38.097  1.00 34.35  ? 200 GLN A CB  1 
ATOM   1199 C CG  . GLN A 1 185 ? -18.014 33.200 38.397  1.00 30.40  ? 200 GLN A CG  1 
ATOM   1200 C CD  . GLN A 1 185 ? -18.557 32.563 37.136  1.00 36.07  ? 200 GLN A CD  1 
ATOM   1201 O OE1 . GLN A 1 185 ? -17.867 31.776 36.485  1.00 31.95  ? 200 GLN A OE1 1 
ATOM   1202 N NE2 . GLN A 1 185 ? -19.794 32.909 36.775  1.00 30.03  ? 200 GLN A NE2 1 
ATOM   1203 N N   . GLU A 1 186 ? -16.032 37.550 38.369  1.00 40.55  ? 201 GLU A N   1 
ATOM   1204 C CA  . GLU A 1 186 ? -14.849 38.379 38.192  1.00 43.68  ? 201 GLU A CA  1 
ATOM   1205 C C   . GLU A 1 186 ? -15.209 39.849 38.312  1.00 42.51  ? 201 GLU A C   1 
ATOM   1206 O O   . GLU A 1 186 ? -16.156 40.316 37.673  1.00 42.67  ? 201 GLU A O   1 
ATOM   1207 C CB  . GLU A 1 186 ? -14.187 38.125 36.841  1.00 42.62  ? 201 GLU A CB  1 
ATOM   1208 C CG  . GLU A 1 186 ? -13.017 39.053 36.585  1.00 47.19  ? 201 GLU A CG  1 
ATOM   1209 C CD  . GLU A 1 186 ? -12.289 38.729 35.300  1.00 52.61  ? 201 GLU A CD  1 
ATOM   1210 O OE1 . GLU A 1 186 ? -12.724 39.210 34.230  1.00 55.16  ? 201 GLU A OE1 1 
ATOM   1211 O OE2 . GLU A 1 186 ? -11.282 37.990 35.361  1.00 52.91  ? 201 GLU A OE2 1 
ATOM   1212 N N   . ASN A 1 187 ? -14.445 40.564 39.137  1.00 40.78  ? 202 ASN A N   1 
ATOM   1213 C CA  . ASN A 1 187 ? -14.453 42.028 39.184  1.00 46.89  ? 202 ASN A CA  1 
ATOM   1214 C C   . ASN A 1 187 ? -12.984 42.442 39.282  1.00 48.92  ? 202 ASN A C   1 
ATOM   1215 O O   . ASN A 1 187 ? -12.441 42.601 40.381  1.00 45.26  ? 202 ASN A O   1 
ATOM   1216 C CB  . ASN A 1 187 ? -15.284 42.562 40.344  1.00 45.80  ? 202 ASN A CB  1 
ATOM   1217 C CG  . ASN A 1 187 ? -15.226 44.072 40.453  1.00 46.04  ? 202 ASN A CG  1 
ATOM   1218 O OD1 . ASN A 1 187 ? -15.372 44.780 39.458  1.00 50.93  ? 202 ASN A OD1 1 
ATOM   1219 N ND2 . ASN A 1 187 ? -15.010 44.572 41.662  1.00 46.75  ? 202 ASN A ND2 1 
ATOM   1220 N N   . MET A 1 188 ? -12.338 42.573 38.120  1.00 47.55  ? 203 MET A N   1 
ATOM   1221 C CA  . MET A 1 188 ? -10.937 42.973 38.029  1.00 57.36  ? 203 MET A CA  1 
ATOM   1222 C C   . MET A 1 188 ? -10.746 44.166 37.101  1.00 60.09  ? 203 MET A C   1 
ATOM   1223 O O   . MET A 1 188 ? -9.605  44.580 36.872  1.00 63.29  ? 203 MET A O   1 
ATOM   1224 C CB  . MET A 1 188 ? -10.062 41.810 37.541  1.00 49.32  ? 203 MET A CB  1 
ATOM   1225 C CG  . MET A 1 188 ? -9.764  40.732 38.570  1.00 53.93  ? 203 MET A CG  1 
ATOM   1226 S SD  . MET A 1 188 ? -9.132  41.362 40.135  1.00 63.33  ? 203 MET A SD  1 
ATOM   1227 C CE  . MET A 1 188 ? -7.519  41.965 39.652  1.00 66.21  ? 203 MET A CE  1 
ATOM   1228 N N   . GLY A 1 189 ? -11.828 44.729 36.574  1.00 62.82  ? 204 GLY A N   1 
ATOM   1229 C CA  . GLY A 1 189 ? -11.756 45.717 35.526  1.00 67.92  ? 204 GLY A CA  1 
ATOM   1230 C C   . GLY A 1 189 ? -11.715 47.157 35.997  1.00 73.66  ? 204 GLY A C   1 
ATOM   1231 O O   . GLY A 1 189 ? -10.790 47.906 35.659  1.00 77.12  ? 204 GLY A O   1 
ATOM   1232 N N   . PRO A 1 190 ? -12.743 47.587 36.768  1.00 78.41  ? 205 PRO A N   1 
ATOM   1233 C CA  . PRO A 1 190 ? -12.811 48.988 37.212  1.00 75.39  ? 205 PRO A CA  1 
ATOM   1234 C C   . PRO A 1 190 ? -11.492 49.527 37.739  1.00 80.06  ? 205 PRO A C   1 
ATOM   1235 O O   . PRO A 1 190 ? -10.725 48.793 38.372  1.00 78.77  ? 205 PRO A O   1 
ATOM   1236 C CB  . PRO A 1 190 ? -13.867 48.941 38.321  1.00 74.80  ? 205 PRO A CB  1 
ATOM   1237 C CG  . PRO A 1 190 ? -14.791 47.858 37.896  1.00 74.29  ? 205 PRO A CG  1 
ATOM   1238 C CD  . PRO A 1 190 ? -13.932 46.823 37.199  1.00 73.67  ? 205 PRO A CD  1 
ATOM   1239 N N   . ARG A 1 191 ? -11.219 50.809 37.474  1.00 79.00  ? 206 ARG A N   1 
ATOM   1240 C CA  . ARG A 1 191 ? -9.947  51.402 37.872  1.00 78.44  ? 206 ARG A CA  1 
ATOM   1241 C C   . ARG A 1 191 ? -9.688  51.262 39.366  1.00 79.06  ? 206 ARG A C   1 
ATOM   1242 O O   . ARG A 1 191 ? -8.524  51.281 39.785  1.00 80.04  ? 206 ARG A O   1 
ATOM   1243 C CB  . ARG A 1 191 ? -9.902  52.877 37.469  1.00 70.31  ? 206 ARG A CB  1 
ATOM   1244 N N   . TYR A 1 192 ? -10.738 51.104 40.177  1.00 80.31  ? 207 TYR A N   1 
ATOM   1245 C CA  . TYR A 1 192 ? -10.521 50.862 41.597  1.00 80.58  ? 207 TYR A CA  1 
ATOM   1246 C C   . TYR A 1 192 ? -9.967  49.469 41.877  1.00 75.26  ? 207 TYR A C   1 
ATOM   1247 O O   . TYR A 1 192 ? -9.527  49.214 43.002  1.00 75.87  ? 207 TYR A O   1 
ATOM   1248 C CB  . TYR A 1 192 ? -11.811 51.096 42.406  1.00 80.16  ? 207 TYR A CB  1 
ATOM   1249 C CG  . TYR A 1 192 ? -13.039 50.279 42.022  1.00 80.77  ? 207 TYR A CG  1 
ATOM   1250 C CD1 . TYR A 1 192 ? -13.099 48.915 42.275  1.00 79.54  ? 207 TYR A CD1 1 
ATOM   1251 C CD2 . TYR A 1 192 ? -14.174 50.891 41.497  1.00 81.77  ? 207 TYR A CD2 1 
ATOM   1252 C CE1 . TYR A 1 192 ? -14.229 48.169 41.966  1.00 78.23  ? 207 TYR A CE1 1 
ATOM   1253 C CE2 . TYR A 1 192 ? -15.313 50.153 41.186  1.00 77.82  ? 207 TYR A CE2 1 
ATOM   1254 C CZ  . TYR A 1 192 ? -15.331 48.790 41.421  1.00 74.64  ? 207 TYR A CZ  1 
ATOM   1255 O OH  . TYR A 1 192 ? -16.448 48.043 41.115  1.00 70.30  ? 207 TYR A OH  1 
ATOM   1256 N N   . CYS A 1 193 ? -9.967  48.572 40.894  1.00 72.69  ? 208 CYS A N   1 
ATOM   1257 C CA  . CYS A 1 193 ? -9.367  47.255 41.050  1.00 76.33  ? 208 CYS A CA  1 
ATOM   1258 C C   . CYS A 1 193 ? -7.907  47.215 40.620  1.00 80.02  ? 208 CYS A C   1 
ATOM   1259 O O   . CYS A 1 193 ? -7.301  46.137 40.630  1.00 81.10  ? 208 CYS A O   1 
ATOM   1260 C CB  . CYS A 1 193 ? -10.167 46.214 40.264  1.00 60.28  ? 208 CYS A CB  1 
ATOM   1261 S SG  . CYS A 1 193 ? -11.579 45.599 41.178  1.00 64.10  ? 208 CYS A SG  1 
ATOM   1262 N N   . SER A 1 194 ? -7.330  48.360 40.248  1.00 81.30  ? 209 SER A N   1 
ATOM   1263 C CA  . SER A 1 194 ? -5.945  48.474 39.821  1.00 87.46  ? 209 SER A CA  1 
ATOM   1264 C C   . SER A 1 194 ? -5.114  49.196 40.877  1.00 87.68  ? 209 SER A C   1 
ATOM   1265 O O   . SER A 1 194 ? -5.602  50.147 41.501  1.00 88.68  ? 209 SER A O   1 
ATOM   1266 C CB  . SER A 1 194 ? -5.843  49.227 38.487  1.00 87.83  ? 209 SER A CB  1 
ATOM   1267 O OG  . SER A 1 194 ? -6.067  50.615 38.666  1.00 90.86  ? 209 SER A OG  1 
ATOM   1268 N N   . PRO A 1 195 ? -3.859  48.764 41.105  1.00 83.32  ? 210 PRO A N   1 
ATOM   1269 C CA  . PRO A 1 195 ? -2.937  49.289 42.123  1.00 86.15  ? 210 PRO A CA  1 
ATOM   1270 C C   . PRO A 1 195 ? -2.881  50.813 42.190  1.00 84.26  ? 210 PRO A C   1 
ATOM   1271 O O   . PRO A 1 195 ? -2.921  51.358 43.293  1.00 83.62  ? 210 PRO A O   1 
ATOM   1272 C CB  . PRO A 1 195 ? -1.589  48.724 41.681  1.00 84.54  ? 210 PRO A CB  1 
ATOM   1273 C CG  . PRO A 1 195 ? -1.937  47.425 41.054  1.00 84.74  ? 210 PRO A CG  1 
ATOM   1274 C CD  . PRO A 1 195 ? -3.256  47.648 40.353  1.00 81.09  ? 210 PRO A CD  1 
ATOM   1275 N N   . ASP A 1 201 ? -7.636  47.771 47.726  1.00 63.73  ? 216 ASP A N   1 
ATOM   1276 C CA  . ASP A 1 201 ? -7.176  47.248 49.010  1.00 69.93  ? 216 ASP A CA  1 
ATOM   1277 C C   . ASP A 1 201 ? -8.304  47.245 50.037  1.00 76.00  ? 216 ASP A C   1 
ATOM   1278 O O   . ASP A 1 201 ? -8.338  46.399 50.931  1.00 76.77  ? 216 ASP A O   1 
ATOM   1279 C CB  . ASP A 1 201 ? -5.990  48.063 49.530  1.00 68.24  ? 216 ASP A CB  1 
ATOM   1280 C CG  . ASP A 1 201 ? -4.657  47.535 49.028  1.00 73.17  ? 216 ASP A CG  1 
ATOM   1281 O OD1 . ASP A 1 201 ? -4.135  46.571 49.628  1.00 69.15  ? 216 ASP A OD1 1 
ATOM   1282 O OD2 . ASP A 1 201 ? -4.133  48.082 48.031  1.00 73.23  ? 216 ASP A OD2 1 
ATOM   1283 N N   . ALA A 1 202 ? -9.221  48.207 49.911  1.00 73.01  ? 217 ALA A N   1 
ATOM   1284 C CA  . ALA A 1 202 ? -10.437 48.244 50.716  1.00 72.71  ? 217 ALA A CA  1 
ATOM   1285 C C   . ALA A 1 202 ? -11.676 48.093 49.844  1.00 69.76  ? 217 ALA A C   1 
ATOM   1286 O O   . ALA A 1 202 ? -12.786 48.429 50.275  1.00 66.05  ? 217 ALA A O   1 
ATOM   1287 C CB  . ALA A 1 202 ? -10.511 49.534 51.534  1.00 70.31  ? 217 ALA A CB  1 
ATOM   1288 N N   . VAL A 1 203 ? -11.499 47.598 48.624  1.00 67.66  ? 218 VAL A N   1 
ATOM   1289 C CA  . VAL A 1 203 ? -12.576 47.420 47.664  1.00 66.37  ? 218 VAL A CA  1 
ATOM   1290 C C   . VAL A 1 203 ? -12.659 45.942 47.305  1.00 60.76  ? 218 VAL A C   1 
ATOM   1291 O O   . VAL A 1 203 ? -11.670 45.206 47.394  1.00 67.45  ? 218 VAL A O   1 
ATOM   1292 C CB  . VAL A 1 203 ? -12.346 48.296 46.413  1.00 63.29  ? 218 VAL A CB  1 
ATOM   1293 C CG1 . VAL A 1 203 ? -10.932 48.102 45.889  1.00 60.57  ? 218 VAL A CG1 1 
ATOM   1294 C CG2 . VAL A 1 203 ? -13.383 48.010 45.355  1.00 66.40  ? 218 VAL A CG2 1 
ATOM   1295 N N   . PHE A 1 204 ? -13.855 45.503 46.920  1.00 57.34  ? 219 PHE A N   1 
ATOM   1296 C CA  . PHE A 1 204 ? -14.108 44.107 46.571  1.00 50.75  ? 219 PHE A CA  1 
ATOM   1297 C C   . PHE A 1 204 ? -13.671 43.842 45.135  1.00 48.69  ? 219 PHE A C   1 
ATOM   1298 O O   . PHE A 1 204 ? -14.417 44.099 44.187  1.00 47.08  ? 219 PHE A O   1 
ATOM   1299 C CB  . PHE A 1 204 ? -15.584 43.781 46.748  1.00 56.14  ? 219 PHE A CB  1 
ATOM   1300 C CG  . PHE A 1 204 ? -15.847 42.360 47.133  1.00 52.16  ? 219 PHE A CG  1 
ATOM   1301 C CD1 . PHE A 1 204 ? -15.315 41.837 48.301  1.00 47.26  ? 219 PHE A CD1 1 
ATOM   1302 C CD2 . PHE A 1 204 ? -16.617 41.544 46.323  1.00 44.04  ? 219 PHE A CD2 1 
ATOM   1303 C CE1 . PHE A 1 204 ? -15.560 40.530 48.664  1.00 46.50  ? 219 PHE A CE1 1 
ATOM   1304 C CE2 . PHE A 1 204 ? -16.866 40.237 46.681  1.00 48.28  ? 219 PHE A CE2 1 
ATOM   1305 C CZ  . PHE A 1 204 ? -16.333 39.729 47.854  1.00 48.88  ? 219 PHE A CZ  1 
ATOM   1306 N N   . CYS A 1 205 ? -12.464 43.303 44.969  1.00 48.37  ? 220 CYS A N   1 
ATOM   1307 C CA  . CYS A 1 205 ? -11.963 42.854 43.677  1.00 46.61  ? 220 CYS A CA  1 
ATOM   1308 C C   . CYS A 1 205 ? -11.702 41.358 43.750  1.00 42.58  ? 220 CYS A C   1 
ATOM   1309 O O   . CYS A 1 205 ? -11.127 40.871 44.728  1.00 45.33  ? 220 CYS A O   1 
ATOM   1310 C CB  . CYS A 1 205 ? -10.678 43.594 43.278  1.00 49.62  ? 220 CYS A CB  1 
ATOM   1311 S SG  . CYS A 1 205 ? -10.886 45.384 43.083  1.00 55.81  ? 220 CYS A SG  1 
ATOM   1312 N N   . PHE A 1 206 ? -12.123 40.630 42.716  1.00 39.57  ? 221 PHE A N   1 
ATOM   1313 C CA  . PHE A 1 206 ? -12.034 39.178 42.749  1.00 37.58  ? 221 PHE A CA  1 
ATOM   1314 C C   . PHE A 1 206 ? -11.911 38.624 41.337  1.00 42.67  ? 221 PHE A C   1 
ATOM   1315 O O   . PHE A 1 206 ? -12.215 39.300 40.350  1.00 42.52  ? 221 PHE A O   1 
ATOM   1316 C CB  . PHE A 1 206 ? -13.246 38.564 43.460  1.00 36.68  ? 221 PHE A CB  1 
ATOM   1317 C CG  . PHE A 1 206 ? -14.567 38.983 42.887  1.00 34.97  ? 221 PHE A CG  1 
ATOM   1318 C CD1 . PHE A 1 206 ? -15.211 40.114 43.354  1.00 38.30  ? 221 PHE A CD1 1 
ATOM   1319 C CD2 . PHE A 1 206 ? -15.180 38.231 41.896  1.00 36.41  ? 221 PHE A CD2 1 
ATOM   1320 C CE1 . PHE A 1 206 ? -16.439 40.495 42.840  1.00 39.54  ? 221 PHE A CE1 1 
ATOM   1321 C CE2 . PHE A 1 206 ? -16.411 38.610 41.375  1.00 36.35  ? 221 PHE A CE2 1 
ATOM   1322 C CZ  . PHE A 1 206 ? -17.038 39.742 41.848  1.00 36.02  ? 221 PHE A CZ  1 
ATOM   1323 N N   . LYS A 1 207 ? -11.467 37.369 41.257  1.00 38.03  ? 222 LYS A N   1 
ATOM   1324 C CA  . LYS A 1 207 ? -11.245 36.701 39.984  1.00 41.55  ? 222 LYS A CA  1 
ATOM   1325 C C   . LYS A 1 207 ? -11.417 35.202 40.169  1.00 40.30  ? 222 LYS A C   1 
ATOM   1326 O O   . LYS A 1 207 ? -11.166 34.680 41.262  1.00 34.09  ? 222 LYS A O   1 
ATOM   1327 C CB  . LYS A 1 207 ? -9.845  37.006 39.428  1.00 37.16  ? 222 LYS A CB  1 
ATOM   1328 C CG  . LYS A 1 207 ? -8.709  36.332 40.188  1.00 44.57  ? 222 LYS A CG  1 
ATOM   1329 C CD  . LYS A 1 207 ? -7.406  37.113 40.057  1.00 58.52  ? 222 LYS A CD  1 
ATOM   1330 C CE  . LYS A 1 207 ? -6.193  36.247 40.393  1.00 58.94  ? 222 LYS A CE  1 
ATOM   1331 N NZ  . LYS A 1 207 ? -5.468  35.797 39.164  1.00 64.31  ? 222 LYS A NZ  1 
ATOM   1332 N N   . PRO A 1 208 ? -11.846 34.486 39.130  1.00 40.92  ? 223 PRO A N   1 
ATOM   1333 C CA  . PRO A 1 208 ? -11.795 33.022 39.183  1.00 36.48  ? 223 PRO A CA  1 
ATOM   1334 C C   . PRO A 1 208 ? -10.356 32.542 39.130  1.00 39.85  ? 223 PRO A C   1 
ATOM   1335 O O   . PRO A 1 208 ? -9.496  33.148 38.485  1.00 41.34  ? 223 PRO A O   1 
ATOM   1336 C CB  . PRO A 1 208 ? -12.570 32.596 37.933  1.00 35.94  ? 223 PRO A CB  1 
ATOM   1337 C CG  . PRO A 1 208 ? -12.338 33.717 36.971  1.00 40.56  ? 223 PRO A CG  1 
ATOM   1338 C CD  . PRO A 1 208 ? -12.270 34.978 37.808  1.00 35.91  ? 223 PRO A CD  1 
ATOM   1339 N N   . ASP A 1 209 ? -10.092 31.440 39.826  1.00 39.40  ? 224 ASP A N   1 
ATOM   1340 C CA  . ASP A 1 209 ? -8.743  30.898 39.857  1.00 40.24  ? 224 ASP A CA  1 
ATOM   1341 C C   . ASP A 1 209 ? -8.783  29.467 40.367  1.00 37.98  ? 224 ASP A C   1 
ATOM   1342 O O   . ASP A 1 209 ? -9.770  29.021 40.958  1.00 37.95  ? 224 ASP A O   1 
ATOM   1343 C CB  . ASP A 1 209 ? -7.816  31.749 40.733  1.00 39.48  ? 224 ASP A CB  1 
ATOM   1344 C CG  . ASP A 1 209 ? -6.387  31.747 40.235  1.00 43.36  ? 224 ASP A CG  1 
ATOM   1345 O OD1 . ASP A 1 209 ? -6.041  30.850 39.439  1.00 41.64  ? 224 ASP A OD1 1 
ATOM   1346 O OD2 . ASP A 1 209 ? -5.610  32.637 40.641  1.00 48.01  ? 224 ASP A OD2 1 
ATOM   1347 N N   . LYS A 1 210 ? -7.694  28.752 40.116  1.00 41.66  ? 225 LYS A N   1 
ATOM   1348 C CA  . LYS A 1 210 ? -7.459  27.449 40.718  1.00 41.88  ? 225 LYS A CA  1 
ATOM   1349 C C   . LYS A 1 210 ? -6.374  27.599 41.781  1.00 40.30  ? 225 LYS A C   1 
ATOM   1350 O O   . LYS A 1 210 ? -5.260  27.095 41.653  1.00 44.91  ? 225 LYS A O   1 
ATOM   1351 C CB  . LYS A 1 210 ? -7.087  26.414 39.645  1.00 36.40  ? 225 LYS A CB  1 
ATOM   1352 C CG  . LYS A 1 210 ? -8.183  26.190 38.599  1.00 39.39  ? 225 LYS A CG  1 
ATOM   1353 C CD  . LYS A 1 210 ? -8.260  24.732 38.146  1.00 34.47  ? 225 LYS A CD  1 
ATOM   1354 C CE  . LYS A 1 210 ? -9.316  24.550 37.064  1.00 35.75  ? 225 LYS A CE  1 
ATOM   1355 N NZ  . LYS A 1 210 ? -9.322  23.177 36.472  1.00 30.75  ? 225 LYS A NZ  1 
ATOM   1356 N N   . ASP A 1 211 ? -6.710  28.347 42.829  1.00 47.36  ? 226 ASP A N   1 
ATOM   1357 C CA  . ASP A 1 211 ? -5.868  28.406 44.015  1.00 43.23  ? 226 ASP A CA  1 
ATOM   1358 C C   . ASP A 1 211 ? -5.731  27.017 44.626  1.00 46.25  ? 226 ASP A C   1 
ATOM   1359 O O   . ASP A 1 211 ? -6.629  26.176 44.521  1.00 42.25  ? 226 ASP A O   1 
ATOM   1360 C CB  . ASP A 1 211 ? -6.469  29.374 45.040  1.00 38.56  ? 226 ASP A CB  1 
ATOM   1361 C CG  . ASP A 1 211 ? -5.484  29.770 46.125  1.00 46.26  ? 226 ASP A CG  1 
ATOM   1362 O OD1 . ASP A 1 211 ? -4.756  30.771 45.931  1.00 52.23  ? 226 ASP A OD1 1 
ATOM   1363 O OD2 . ASP A 1 211 ? -5.441  29.080 47.171  1.00 40.11  ? 226 ASP A OD2 1 
ATOM   1364 N N   . GLU A 1 212 ? -4.588  26.778 45.274  1.00 47.42  ? 227 GLU A N   1 
ATOM   1365 C CA  . GLU A 1 212 ? -4.372  25.484 45.913  1.00 45.88  ? 227 GLU A CA  1 
ATOM   1366 C C   . GLU A 1 212 ? -5.414  25.207 46.987  1.00 39.61  ? 227 GLU A C   1 
ATOM   1367 O O   . GLU A 1 212 ? -5.743  24.043 47.240  1.00 42.64  ? 227 GLU A O   1 
ATOM   1368 C CB  . GLU A 1 212 ? -2.967  25.416 46.505  1.00 47.83  ? 227 GLU A CB  1 
ATOM   1369 C CG  . GLU A 1 212 ? -1.907  25.039 45.497  1.00 55.20  ? 227 GLU A CG  1 
ATOM   1370 C CD  . GLU A 1 212 ? -0.630  25.831 45.671  1.00 71.34  ? 227 GLU A CD  1 
ATOM   1371 O OE1 . GLU A 1 212 ? -0.299  26.628 44.763  1.00 68.76  ? 227 GLU A OE1 1 
ATOM   1372 O OE2 . GLU A 1 212 ? 0.032   25.660 46.722  1.00 71.72  ? 227 GLU A OE2 1 
ATOM   1373 N N   . SER A 1 213 ? -5.955  26.257 47.616  1.00 39.32  ? 228 SER A N   1 
ATOM   1374 C CA  . SER A 1 213 ? -7.026  26.069 48.593  1.00 42.29  ? 228 SER A CA  1 
ATOM   1375 C C   . SER A 1 213 ? -8.259  25.429 47.966  1.00 37.98  ? 228 SER A C   1 
ATOM   1376 O O   . SER A 1 213 ? -9.028  24.759 48.663  1.00 36.00  ? 228 SER A O   1 
ATOM   1377 C CB  . SER A 1 213 ? -7.410  27.407 49.229  1.00 39.74  ? 228 SER A CB  1 
ATOM   1378 O OG  . SER A 1 213 ? -6.323  27.964 49.941  1.00 56.84  ? 228 SER A OG  1 
ATOM   1379 N N   . PHE A 1 214 ? -8.461  25.618 46.664  1.00 36.83  ? 229 PHE A N   1 
ATOM   1380 C CA  . PHE A 1 214 ? -9.662  25.164 45.974  1.00 34.86  ? 229 PHE A CA  1 
ATOM   1381 C C   . PHE A 1 214 ? -9.523  23.761 45.392  1.00 38.38  ? 229 PHE A C   1 
ATOM   1382 O O   . PHE A 1 214 ? -10.407 23.330 44.641  1.00 37.17  ? 229 PHE A O   1 
ATOM   1383 C CB  . PHE A 1 214 ? -10.027 26.136 44.842  1.00 33.26  ? 229 PHE A CB  1 
ATOM   1384 C CG  . PHE A 1 214 ? -10.090 27.589 45.256  1.00 35.21  ? 229 PHE A CG  1 
ATOM   1385 C CD1 . PHE A 1 214 ? -10.369 27.960 46.567  1.00 30.51  ? 229 PHE A CD1 1 
ATOM   1386 C CD2 . PHE A 1 214 ? -9.879  28.588 44.313  1.00 35.43  ? 229 PHE A CD2 1 
ATOM   1387 C CE1 . PHE A 1 214 ? -10.430 29.302 46.928  1.00 30.93  ? 229 PHE A CE1 1 
ATOM   1388 C CE2 . PHE A 1 214 ? -9.945  29.935 44.664  1.00 35.49  ? 229 PHE A CE2 1 
ATOM   1389 C CZ  . PHE A 1 214 ? -10.215 30.292 45.973  1.00 33.69  ? 229 PHE A CZ  1 
ATOM   1390 N N   . GLU A 1 215 ? -8.441  23.045 45.715  1.00 33.62  ? 230 GLU A N   1 
ATOM   1391 C CA  . GLU A 1 215 ? -8.117  21.816 44.991  1.00 39.35  ? 230 GLU A CA  1 
ATOM   1392 C C   . GLU A 1 215 ? -9.264  20.808 45.016  1.00 42.22  ? 230 GLU A C   1 
ATOM   1393 O O   . GLU A 1 215 ? -9.525  20.129 44.015  1.00 36.49  ? 230 GLU A O   1 
ATOM   1394 C CB  . GLU A 1 215 ? -6.848  21.186 45.566  1.00 36.89  ? 230 GLU A CB  1 
ATOM   1395 C CG  . GLU A 1 215 ? -6.049  20.386 44.543  1.00 52.53  ? 230 GLU A CG  1 
ATOM   1396 C CD  . GLU A 1 215 ? -5.041  19.432 45.176  1.00 55.17  ? 230 GLU A CD  1 
ATOM   1397 O OE1 . GLU A 1 215 ? -4.305  19.857 46.092  1.00 50.91  ? 230 GLU A OE1 1 
ATOM   1398 O OE2 . GLU A 1 215 ? -4.978  18.259 44.744  1.00 55.98  ? 230 GLU A OE2 1 
ATOM   1399 N N   . ASN A 1 216 ? -9.956  20.690 46.148  1.00 33.69  ? 231 ASN A N   1 
ATOM   1400 C CA  . ASN A 1 216 ? -11.017 19.703 46.287  1.00 33.72  ? 231 ASN A CA  1 
ATOM   1401 C C   . ASN A 1 216 ? -12.390 20.246 45.918  1.00 36.01  ? 231 ASN A C   1 
ATOM   1402 O O   . ASN A 1 216 ? -13.377 19.513 46.040  1.00 36.52  ? 231 ASN A O   1 
ATOM   1403 C CB  . ASN A 1 216 ? -11.052 19.158 47.718  1.00 33.26  ? 231 ASN A CB  1 
ATOM   1404 C CG  . ASN A 1 216 ? -9.674  18.787 48.226  1.00 38.05  ? 231 ASN A CG  1 
ATOM   1405 O OD1 . ASN A 1 216 ? -8.984  17.979 47.611  1.00 36.33  ? 231 ASN A OD1 1 
ATOM   1406 N ND2 . ASN A 1 216 ? -9.259  19.387 49.342  1.00 36.43  ? 231 ASN A ND2 1 
ATOM   1407 N N   . LEU A 1 217 ? -12.478 21.498 45.470  1.00 34.30  ? 232 LEU A N   1 
ATOM   1408 C CA  . LEU A 1 217 ? -13.760 22.125 45.183  1.00 33.75  ? 232 LEU A CA  1 
ATOM   1409 C C   . LEU A 1 217 ? -14.217 21.807 43.764  1.00 34.49  ? 232 LEU A C   1 
ATOM   1410 O O   . LEU A 1 217 ? -13.407 21.653 42.845  1.00 35.05  ? 232 LEU A O   1 
ATOM   1411 C CB  . LEU A 1 217 ? -13.679 23.642 45.377  1.00 30.39  ? 232 LEU A CB  1 
ATOM   1412 C CG  . LEU A 1 217 ? -13.228 24.141 46.754  1.00 38.25  ? 232 LEU A CG  1 
ATOM   1413 C CD1 . LEU A 1 217 ? -13.344 25.660 46.831  1.00 27.66  ? 232 LEU A CD1 1 
ATOM   1414 C CD2 . LEU A 1 217 ? -14.020 23.471 47.880  1.00 34.34  ? 232 LEU A CD2 1 
ATOM   1415 N N   . VAL A 1 218 ? -15.533 21.705 43.600  1.00 32.70  ? 233 VAL A N   1 
ATOM   1416 C CA  . VAL A 1 218 ? -16.168 21.442 42.312  1.00 33.58  ? 233 VAL A CA  1 
ATOM   1417 C C   . VAL A 1 218 ? -17.160 22.564 42.039  1.00 38.44  ? 233 VAL A C   1 
ATOM   1418 O O   . VAL A 1 218 ? -18.130 22.737 42.789  1.00 34.16  ? 233 VAL A O   1 
ATOM   1419 C CB  . VAL A 1 218 ? -16.871 20.078 42.300  1.00 29.94  ? 233 VAL A CB  1 
ATOM   1420 C CG1 . VAL A 1 218 ? -17.287 19.708 40.884  1.00 29.15  ? 233 VAL A CG1 1 
ATOM   1421 C CG2 . VAL A 1 218 ? -15.960 19.019 42.906  1.00 30.56  ? 233 VAL A CG2 1 
ATOM   1422 N N   . TYR A 1 219 ? -16.922 23.327 40.973  1.00 31.22  ? 234 TYR A N   1 
ATOM   1423 C CA  . TYR A 1 219 ? -17.799 24.439 40.621  1.00 35.24  ? 234 TYR A CA  1 
ATOM   1424 C C   . TYR A 1 219 ? -18.918 23.930 39.714  1.00 36.55  ? 234 TYR A C   1 
ATOM   1425 O O   . TYR A 1 219 ? -18.653 23.363 38.647  1.00 33.71  ? 234 TYR A O   1 
ATOM   1426 C CB  . TYR A 1 219 ? -17.017 25.568 39.949  1.00 34.29  ? 234 TYR A CB  1 
ATOM   1427 C CG  . TYR A 1 219 ? -17.875 26.770 39.648  1.00 36.43  ? 234 TYR A CG  1 
ATOM   1428 C CD1 . TYR A 1 219 ? -18.168 27.703 40.637  1.00 33.38  ? 234 TYR A CD1 1 
ATOM   1429 C CD2 . TYR A 1 219 ? -18.413 26.962 38.379  1.00 34.86  ? 234 TYR A CD2 1 
ATOM   1430 C CE1 . TYR A 1 219 ? -18.957 28.804 40.367  1.00 34.59  ? 234 TYR A CE1 1 
ATOM   1431 C CE2 . TYR A 1 219 ? -19.203 28.057 38.098  1.00 35.29  ? 234 TYR A CE2 1 
ATOM   1432 C CZ  . TYR A 1 219 ? -19.474 28.974 39.094  1.00 37.59  ? 234 TYR A CZ  1 
ATOM   1433 O OH  . TYR A 1 219 ? -20.266 30.063 38.811  1.00 34.08  ? 234 TYR A OH  1 
ATOM   1434 N N   . LEU A 1 220 ? -20.165 24.147 40.135  1.00 32.81  ? 235 LEU A N   1 
ATOM   1435 C CA  . LEU A 1 220 ? -21.328 23.489 39.545  1.00 34.27  ? 235 LEU A CA  1 
ATOM   1436 C C   . LEU A 1 220 ? -22.371 24.526 39.156  1.00 34.51  ? 235 LEU A C   1 
ATOM   1437 O O   . LEU A 1 220 ? -22.943 25.188 40.029  1.00 33.88  ? 235 LEU A O   1 
ATOM   1438 C CB  . LEU A 1 220 ? -21.927 22.483 40.527  1.00 29.11  ? 235 LEU A CB  1 
ATOM   1439 C CG  . LEU A 1 220 ? -21.002 21.336 40.932  1.00 35.13  ? 235 LEU A CG  1 
ATOM   1440 C CD1 . LEU A 1 220 ? -21.468 20.729 42.243  1.00 29.85  ? 235 LEU A CD1 1 
ATOM   1441 C CD2 . LEU A 1 220 ? -20.953 20.288 39.831  1.00 28.10  ? 235 LEU A CD2 1 
ATOM   1442 N N   . SER A 1 221 ? -22.635 24.665 37.856  1.00 34.08  ? 236 SER A N   1 
ATOM   1443 C CA  . SER A 1 221 ? -23.763 25.493 37.449  1.00 40.05  ? 236 SER A CA  1 
ATOM   1444 C C   . SER A 1 221 ? -25.043 24.692 37.628  1.00 33.45  ? 236 SER A C   1 
ATOM   1445 O O   . SER A 1 221 ? -25.017 23.512 37.977  1.00 33.72  ? 236 SER A O   1 
ATOM   1446 C CB  . SER A 1 221 ? -23.633 25.962 36.000  1.00 33.34  ? 236 SER A CB  1 
ATOM   1447 O OG  . SER A 1 221 ? -24.039 24.947 35.095  1.00 36.82  ? 236 SER A OG  1 
ATOM   1448 N N   . LYS A 1 222 ? -26.177 25.338 37.365  1.00 35.27  ? 237 LYS A N   1 
ATOM   1449 C CA  . LYS A 1 222 ? -27.472 24.682 37.496  1.00 36.51  ? 237 LYS A CA  1 
ATOM   1450 C C   . LYS A 1 222 ? -27.674 23.548 36.490  1.00 37.01  ? 237 LYS A C   1 
ATOM   1451 O O   . LYS A 1 222 ? -28.550 22.701 36.700  1.00 35.97  ? 237 LYS A O   1 
ATOM   1452 C CB  . LYS A 1 222 ? -28.578 25.722 37.327  1.00 39.82  ? 237 LYS A CB  1 
ATOM   1453 C CG  . LYS A 1 222 ? -28.665 26.255 35.907  1.00 37.40  ? 237 LYS A CG  1 
ATOM   1454 C CD  . LYS A 1 222 ? -29.460 27.539 35.843  1.00 43.74  ? 237 LYS A CD  1 
ATOM   1455 C CE  . LYS A 1 222 ? -30.835 27.310 35.244  1.00 50.81  ? 237 LYS A CE  1 
ATOM   1456 N NZ  . LYS A 1 222 ? -30.739 26.713 33.874  1.00 48.75  ? 237 LYS A NZ  1 
ATOM   1457 N N   . ASN A 1 223 ? -26.892 23.507 35.411  1.00 36.93  ? 238 ASN A N   1 
ATOM   1458 C CA  . ASN A 1 223 ? -27.134 22.597 34.299  1.00 35.18  ? 238 ASN A CA  1 
ATOM   1459 C C   . ASN A 1 223 ? -26.189 21.399 34.262  1.00 38.42  ? 238 ASN A C   1 
ATOM   1460 O O   . ASN A 1 223 ? -26.234 20.632 33.295  1.00 41.43  ? 238 ASN A O   1 
ATOM   1461 C CB  . ASN A 1 223 ? -27.027 23.348 32.970  1.00 39.17  ? 238 ASN A CB  1 
ATOM   1462 C CG  . ASN A 1 223 ? -28.085 24.414 32.813  1.00 39.81  ? 238 ASN A CG  1 
ATOM   1463 O OD1 . ASN A 1 223 ? -29.200 24.282 33.318  1.00 41.51  ? 238 ASN A OD1 1 
ATOM   1464 N ND2 . ASN A 1 223 ? -27.747 25.474 32.086  1.00 37.75  ? 238 ASN A ND2 1 
ATOM   1465 N N   . VAL A 1 224 ? -25.335 21.219 35.273  1.00 34.88  ? 239 VAL A N   1 
ATOM   1466 C CA  . VAL A 1 224 ? -24.315 20.177 35.197  1.00 35.83  ? 239 VAL A CA  1 
ATOM   1467 C C   . VAL A 1 224 ? -24.980 18.814 35.101  1.00 35.61  ? 239 VAL A C   1 
ATOM   1468 O O   . VAL A 1 224 ? -25.913 18.509 35.853  1.00 36.99  ? 239 VAL A O   1 
ATOM   1469 C CB  . VAL A 1 224 ? -23.372 20.258 36.406  1.00 36.94  ? 239 VAL A CB  1 
ATOM   1470 C CG1 . VAL A 1 224 ? -22.562 18.970 36.538  1.00 31.18  ? 239 VAL A CG1 1 
ATOM   1471 C CG2 . VAL A 1 224 ? -22.457 21.460 36.272  1.00 37.25  ? 239 VAL A CG2 1 
ATOM   1472 N N   . ARG A 1 225 ? -24.510 17.994 34.159  1.00 35.41  ? 240 ARG A N   1 
ATOM   1473 C CA  . ARG A 1 225 ? -25.099 16.680 33.930  1.00 36.56  ? 240 ARG A CA  1 
ATOM   1474 C C   . ARG A 1 225 ? -24.911 15.778 35.139  1.00 37.45  ? 240 ARG A C   1 
ATOM   1475 O O   . ARG A 1 225 ? -23.832 15.736 35.740  1.00 39.17  ? 240 ARG A O   1 
ATOM   1476 C CB  . ARG A 1 225 ? -24.468 16.005 32.708  1.00 40.32  ? 240 ARG A CB  1 
ATOM   1477 C CG  . ARG A 1 225 ? -24.126 16.932 31.575  1.00 42.32  ? 240 ARG A CG  1 
ATOM   1478 C CD  . ARG A 1 225 ? -23.164 16.280 30.596  1.00 40.53  ? 240 ARG A CD  1 
ATOM   1479 N NE  . ARG A 1 225 ? -23.183 16.993 29.326  1.00 45.98  ? 240 ARG A NE  1 
ATOM   1480 C CZ  . ARG A 1 225 ? -24.124 16.850 28.402  1.00 49.53  ? 240 ARG A CZ  1 
ATOM   1481 N NH1 . ARG A 1 225 ? -25.081 15.943 28.522  1.00 52.02  ? 240 ARG A NH1 1 
ATOM   1482 N NH2 . ARG A 1 225 ? -24.108 17.640 27.333  1.00 46.25  ? 240 ARG A NH2 1 
ATOM   1483 N N   . ASN A 1 226 ? -25.968 15.033 35.480  1.00 37.32  ? 241 ASN A N   1 
ATOM   1484 C CA  . ASN A 1 226 ? -25.854 14.049 36.553  1.00 38.09  ? 241 ASN A CA  1 
ATOM   1485 C C   . ASN A 1 226 ? -24.878 12.939 36.191  1.00 37.77  ? 241 ASN A C   1 
ATOM   1486 O O   . ASN A 1 226 ? -24.290 12.318 37.084  1.00 39.60  ? 241 ASN A O   1 
ATOM   1487 C CB  . ASN A 1 226 ? -27.222 13.458 36.887  1.00 36.69  ? 241 ASN A CB  1 
ATOM   1488 C CG  . ASN A 1 226 ? -28.177 14.486 37.443  1.00 39.13  ? 241 ASN A CG  1 
ATOM   1489 O OD1 . ASN A 1 226 ? -27.757 15.485 38.026  1.00 42.97  ? 241 ASN A OD1 1 
ATOM   1490 N ND2 . ASN A 1 226 ? -29.471 14.246 37.276  1.00 36.04  ? 241 ASN A ND2 1 
ATOM   1491 N N   . ASP A 1 227 ? -24.692 12.672 34.896  1.00 37.11  ? 242 ASP A N   1 
ATOM   1492 C CA  . ASP A 1 227 ? -23.719 11.688 34.437  1.00 37.62  ? 242 ASP A CA  1 
ATOM   1493 C C   . ASP A 1 227 ? -22.422 12.343 33.969  1.00 39.30  ? 242 ASP A C   1 
ATOM   1494 O O   . ASP A 1 227 ? -21.766 11.844 33.044  1.00 40.22  ? 242 ASP A O   1 
ATOM   1495 C CB  . ASP A 1 227 ? -24.320 10.804 33.340  1.00 34.17  ? 242 ASP A CB  1 
ATOM   1496 C CG  . ASP A 1 227 ? -24.765 11.589 32.117  1.00 42.64  ? 242 ASP A CG  1 
ATOM   1497 O OD1 . ASP A 1 227 ? -24.794 12.838 32.172  1.00 39.68  ? 242 ASP A OD1 1 
ATOM   1498 O OD2 . ASP A 1 227 ? -25.100 10.947 31.096  1.00 43.71  ? 242 ASP A OD2 1 
ATOM   1499 N N   . TRP A 1 228 ? -22.040 13.453 34.614  1.00 36.33  ? 243 TRP A N   1 
ATOM   1500 C CA  . TRP A 1 228 ? -20.791 14.143 34.300  1.00 35.32  ? 243 TRP A CA  1 
ATOM   1501 C C   . TRP A 1 228 ? -19.593 13.200 34.307  1.00 36.29  ? 243 TRP A C   1 
ATOM   1502 O O   . TRP A 1 228 ? -18.634 13.415 33.557  1.00 37.53  ? 243 TRP A O   1 
ATOM   1503 C CB  . TRP A 1 228 ? -20.558 15.277 35.308  1.00 36.12  ? 243 TRP A CB  1 
ATOM   1504 C CG  . TRP A 1 228 ? -20.504 14.765 36.718  1.00 33.21  ? 243 TRP A CG  1 
ATOM   1505 C CD1 . TRP A 1 228 ? -21.545 14.673 37.592  1.00 30.68  ? 243 TRP A CD1 1 
ATOM   1506 C CD2 . TRP A 1 228 ? -19.360 14.230 37.397  1.00 29.43  ? 243 TRP A CD2 1 
ATOM   1507 N NE1 . TRP A 1 228 ? -21.120 14.123 38.779  1.00 33.66  ? 243 TRP A NE1 1 
ATOM   1508 C CE2 . TRP A 1 228 ? -19.784 13.837 38.683  1.00 31.29  ? 243 TRP A CE2 1 
ATOM   1509 C CE3 . TRP A 1 228 ? -18.017 14.048 37.044  1.00 32.21  ? 243 TRP A CE3 1 
ATOM   1510 C CZ2 . TRP A 1 228 ? -18.915 13.275 39.619  1.00 32.81  ? 243 TRP A CZ2 1 
ATOM   1511 C CZ3 . TRP A 1 228 ? -17.154 13.479 37.971  1.00 33.22  ? 243 TRP A CZ3 1 
ATOM   1512 C CH2 . TRP A 1 228 ? -17.608 13.105 39.246  1.00 33.97  ? 243 TRP A CH2 1 
ATOM   1513 N N   . ASP A 1 229 ? -19.616 12.165 35.156  1.00 33.84  ? 244 ASP A N   1 
ATOM   1514 C CA  . ASP A 1 229 ? -18.477 11.254 35.236  1.00 39.84  ? 244 ASP A CA  1 
ATOM   1515 C C   . ASP A 1 229 ? -18.276 10.487 33.933  1.00 41.26  ? 244 ASP A C   1 
ATOM   1516 O O   . ASP A 1 229 ? -17.136 10.200 33.554  1.00 36.11  ? 244 ASP A O   1 
ATOM   1517 C CB  . ASP A 1 229 ? -18.648 10.297 36.422  1.00 35.48  ? 244 ASP A CB  1 
ATOM   1518 C CG  . ASP A 1 229 ? -19.990 9.584  36.419  1.00 42.17  ? 244 ASP A CG  1 
ATOM   1519 O OD1 . ASP A 1 229 ? -21.023 10.232 36.140  1.00 45.89  ? 244 ASP A OD1 1 
ATOM   1520 O OD2 . ASP A 1 229 ? -20.020 8.375  36.718  1.00 50.98  ? 244 ASP A OD2 1 
ATOM   1521 N N   . LYS A 1 230 ? -19.361 10.172 33.219  1.00 41.89  ? 245 LYS A N   1 
ATOM   1522 C CA  . LYS A 1 230 ? -19.216 9.546  31.910  1.00 41.95  ? 245 LYS A CA  1 
ATOM   1523 C C   . LYS A 1 230 ? -19.005 10.568 30.799  1.00 41.25  ? 245 LYS A C   1 
ATOM   1524 O O   . LYS A 1 230 ? -18.368 10.252 29.789  1.00 42.36  ? 245 LYS A O   1 
ATOM   1525 C CB  . LYS A 1 230 ? -20.442 8.685  31.586  1.00 40.31  ? 245 LYS A CB  1 
ATOM   1526 C CG  . LYS A 1 230 ? -21.100 8.019  32.781  1.00 47.13  ? 245 LYS A CG  1 
ATOM   1527 C CD  . LYS A 1 230 ? -20.298 6.824  33.267  1.00 54.60  ? 245 LYS A CD  1 
ATOM   1528 N N   . LYS A 1 231 ? -19.504 11.795 30.965  1.00 39.60  ? 246 LYS A N   1 
ATOM   1529 C CA  . LYS A 1 231 ? -19.639 12.717 29.845  1.00 37.78  ? 246 LYS A CA  1 
ATOM   1530 C C   . LYS A 1 231 ? -18.720 13.931 29.895  1.00 38.19  ? 246 LYS A C   1 
ATOM   1531 O O   . LYS A 1 231 ? -18.666 14.680 28.910  1.00 35.26  ? 246 LYS A O   1 
ATOM   1532 C CB  . LYS A 1 231 ? -21.094 13.200 29.745  1.00 40.16  ? 246 LYS A CB  1 
ATOM   1533 C CG  . LYS A 1 231 ? -21.885 12.525 28.644  1.00 44.43  ? 246 LYS A CG  1 
ATOM   1534 C CD  . LYS A 1 231 ? -22.556 11.268 29.138  1.00 44.99  ? 246 LYS A CD  1 
ATOM   1535 C CE  . LYS A 1 231 ? -23.635 10.801 28.169  1.00 54.33  ? 246 LYS A CE  1 
ATOM   1536 N NZ  . LYS A 1 231 ? -24.706 10.016 28.867  1.00 58.03  ? 246 LYS A NZ  1 
ATOM   1537 N N   . CYS A 1 232 ? -17.994 14.148 30.982  1.00 41.02  ? 247 CYS A N   1 
ATOM   1538 C CA  . CYS A 1 232 ? -17.254 15.382 31.188  1.00 34.68  ? 247 CYS A CA  1 
ATOM   1539 C C   . CYS A 1 232 ? -15.823 15.074 31.592  1.00 37.31  ? 247 CYS A C   1 
ATOM   1540 O O   . CYS A 1 232 ? -15.534 13.978 32.087  1.00 35.17  ? 247 CYS A O   1 
ATOM   1541 C CB  . CYS A 1 232 ? -17.938 16.232 32.270  1.00 35.70  ? 247 CYS A CB  1 
ATOM   1542 S SG  . CYS A 1 232 ? -19.555 16.907 31.784  1.00 40.03  ? 247 CYS A SG  1 
ATOM   1543 N N   . PRO A 1 233 ? -14.899 16.020 31.401  1.00 33.97  ? 248 PRO A N   1 
ATOM   1544 C CA  . PRO A 1 233 ? -13.525 15.807 31.865  1.00 31.33  ? 248 PRO A CA  1 
ATOM   1545 C C   . PRO A 1 233 ? -13.441 15.832 33.380  1.00 34.39  ? 248 PRO A C   1 
ATOM   1546 O O   . PRO A 1 233 ? -14.205 16.523 34.057  1.00 36.31  ? 248 PRO A O   1 
ATOM   1547 C CB  . PRO A 1 233 ? -12.748 16.983 31.254  1.00 31.45  ? 248 PRO A CB  1 
ATOM   1548 C CG  . PRO A 1 233 ? -13.661 17.567 30.199  1.00 33.97  ? 248 PRO A CG  1 
ATOM   1549 C CD  . PRO A 1 233 ? -15.043 17.311 30.705  1.00 32.81  ? 248 PRO A CD  1 
ATOM   1550 N N   . ARG A 1 234 ? -12.508 15.045 33.911  1.00 32.58  ? 249 ARG A N   1 
ATOM   1551 C CA  . ARG A 1 234 ? -12.143 15.151 35.318  1.00 36.26  ? 249 ARG A CA  1 
ATOM   1552 C C   . ARG A 1 234 ? -10.658 14.853 35.504  1.00 40.44  ? 249 ARG A C   1 
ATOM   1553 O O   . ARG A 1 234 ? -9.874  15.746 35.842  1.00 35.48  ? 249 ARG A O   1 
ATOM   1554 C CB  . ARG A 1 234 ? -12.966 14.207 36.199  1.00 29.23  ? 249 ARG A CB  1 
ATOM   1555 C CG  . ARG A 1 234 ? -12.469 14.257 37.637  1.00 33.45  ? 249 ARG A CG  1 
ATOM   1556 C CD  . ARG A 1 234 ? -13.264 13.446 38.638  1.00 35.97  ? 249 ARG A CD  1 
ATOM   1557 N NE  . ARG A 1 234 ? -12.625 13.553 39.945  1.00 35.52  ? 249 ARG A NE  1 
ATOM   1558 C CZ  . ARG A 1 234 ? -13.262 13.770 41.088  1.00 41.24  ? 249 ARG A CZ  1 
ATOM   1559 N NH1 . ARG A 1 234 ? -14.583 13.827 41.145  1.00 36.73  ? 249 ARG A NH1 1 
ATOM   1560 N NH2 . ARG A 1 234 ? -12.554 13.926 42.205  1.00 37.85  ? 249 ARG A NH2 1 
ATOM   1561 N N   . LYS A 1 235 ? -10.263 13.602 35.292  1.00 33.07  ? 250 LYS A N   1 
ATOM   1562 C CA  . LYS A 1 235 ? -8.879  13.211 35.501  1.00 36.21  ? 250 LYS A CA  1 
ATOM   1563 C C   . LYS A 1 235 ? -8.028  13.599 34.299  1.00 35.71  ? 250 LYS A C   1 
ATOM   1564 O O   . LYS A 1 235 ? -8.482  13.545 33.152  1.00 37.94  ? 250 LYS A O   1 
ATOM   1565 C CB  . LYS A 1 235 ? -8.786  11.705 35.752  1.00 40.16  ? 250 LYS A CB  1 
ATOM   1566 C CG  . LYS A 1 235 ? -9.543  11.239 36.995  1.00 38.39  ? 250 LYS A CG  1 
ATOM   1567 C CD  . LYS A 1 235 ? -8.661  10.400 37.904  1.00 42.04  ? 250 LYS A CD  1 
ATOM   1568 C CE  . LYS A 1 235 ? -9.460  9.759  39.029  1.00 40.56  ? 250 LYS A CE  1 
ATOM   1569 N NZ  . LYS A 1 235 ? -10.069 8.463  38.626  1.00 46.22  ? 250 LYS A NZ  1 
ATOM   1570 N N   . ASN A 1 236 ? -6.795  14.011 34.568  1.00 38.48  ? 251 ASN A N   1 
ATOM   1571 C CA  . ASN A 1 236 ? -5.844  14.263 33.499  1.00 38.74  ? 251 ASN A CA  1 
ATOM   1572 C C   . ASN A 1 236 ? -5.314  12.938 32.967  1.00 38.67  ? 251 ASN A C   1 
ATOM   1573 O O   . ASN A 1 236 ? -5.263  11.938 33.685  1.00 32.51  ? 251 ASN A O   1 
ATOM   1574 C CB  . ASN A 1 236 ? -4.699  15.143 33.996  1.00 34.65  ? 251 ASN A CB  1 
ATOM   1575 C CG  . ASN A 1 236 ? -5.194  16.420 34.642  1.00 42.25  ? 251 ASN A CG  1 
ATOM   1576 O OD1 . ASN A 1 236 ? -5.606  17.355 33.956  1.00 40.86  ? 251 ASN A OD1 1 
ATOM   1577 N ND2 . ASN A 1 236 ? -5.168  16.462 35.971  1.00 35.42  ? 251 ASN A ND2 1 
ATOM   1578 N N   . LEU A 1 237 ? -4.926  12.938 31.691  1.00 38.38  ? 252 LEU A N   1 
ATOM   1579 C CA  . LEU A 1 237 ? -4.619  11.710 30.963  1.00 35.60  ? 252 LEU A CA  1 
ATOM   1580 C C   . LEU A 1 237 ? -3.105  11.528 30.883  1.00 41.98  ? 252 LEU A C   1 
ATOM   1581 O O   . LEU A 1 237 ? -2.419  12.248 30.147  1.00 34.66  ? 252 LEU A O   1 
ATOM   1582 C CB  . LEU A 1 237 ? -5.254  11.744 29.576  1.00 37.42  ? 252 LEU A CB  1 
ATOM   1583 C CG  . LEU A 1 237 ? -6.775  11.936 29.599  1.00 41.37  ? 252 LEU A CG  1 
ATOM   1584 C CD1 . LEU A 1 237 ? -7.377  11.790 28.207  1.00 35.49  ? 252 LEU A CD1 1 
ATOM   1585 C CD2 . LEU A 1 237 ? -7.432  10.969 30.580  1.00 40.10  ? 252 LEU A CD2 1 
ATOM   1586 N N   . GLY A 1 238 ? -2.589  10.551 31.636  1.00 38.13  ? 253 GLY A N   1 
ATOM   1587 C CA  . GLY A 1 238 ? -1.169  10.289 31.635  1.00 39.01  ? 253 GLY A CA  1 
ATOM   1588 C C   . GLY A 1 238 ? -0.711  9.504  30.417  1.00 41.41  ? 253 GLY A C   1 
ATOM   1589 O O   . GLY A 1 238 ? -1.489  8.810  29.761  1.00 42.14  ? 253 GLY A O   1 
ATOM   1590 N N   . ASN A 1 239 ? 0.589   9.623  30.126  1.00 41.08  ? 254 ASN A N   1 
ATOM   1591 C CA  . ASN A 1 239 ? 1.203   8.980  28.963  1.00 41.58  ? 254 ASN A CA  1 
ATOM   1592 C C   . ASN A 1 239 ? 0.433   9.314  27.691  1.00 41.11  ? 254 ASN A C   1 
ATOM   1593 O O   . ASN A 1 239 ? 0.234   8.472  26.811  1.00 41.64  ? 254 ASN A O   1 
ATOM   1594 C CB  . ASN A 1 239 ? 1.309   7.471  29.163  1.00 36.70  ? 254 ASN A CB  1 
ATOM   1595 C CG  . ASN A 1 239 ? 2.158   7.112  30.359  1.00 41.00  ? 254 ASN A CG  1 
ATOM   1596 O OD1 . ASN A 1 239 ? 3.349   7.418  30.398  1.00 46.47  ? 254 ASN A OD1 1 
ATOM   1597 N ND2 . ASN A 1 239 ? 1.549   6.469  31.349  1.00 44.20  ? 254 ASN A ND2 1 
ATOM   1598 N N   . ALA A 1 240 ? -0.011  10.563 27.600  1.00 38.24  ? 255 ALA A N   1 
ATOM   1599 C CA  . ALA A 1 240 ? -0.946  10.948 26.559  1.00 36.54  ? 255 ALA A CA  1 
ATOM   1600 C C   . ALA A 1 240 ? -0.805  12.433 26.284  1.00 38.60  ? 255 ALA A C   1 
ATOM   1601 O O   . ALA A 1 240 ? -0.481  13.222 27.176  1.00 36.83  ? 255 ALA A O   1 
ATOM   1602 C CB  . ALA A 1 240 ? -2.389  10.614 26.954  1.00 35.43  ? 255 ALA A CB  1 
ATOM   1603 N N   . LYS A 1 241 ? -1.033  12.796 25.028  1.00 40.04  ? 256 LYS A N   1 
ATOM   1604 C CA  . LYS A 1 241 ? -1.191  14.186 24.639  1.00 39.88  ? 256 LYS A CA  1 
ATOM   1605 C C   . LYS A 1 241 ? -2.331  14.256 23.636  1.00 39.02  ? 256 LYS A C   1 
ATOM   1606 O O   . LYS A 1 241 ? -2.598  13.294 22.911  1.00 40.22  ? 256 LYS A O   1 
ATOM   1607 C CB  . LYS A 1 241 ? 0.107   14.772 24.059  1.00 37.40  ? 256 LYS A CB  1 
ATOM   1608 C CG  . LYS A 1 241 ? 0.524   14.172 22.743  1.00 40.57  ? 256 LYS A CG  1 
ATOM   1609 C CD  . LYS A 1 241 ? 1.512   15.063 22.023  1.00 43.83  ? 256 LYS A CD  1 
ATOM   1610 C CE  . LYS A 1 241 ? 2.935   14.797 22.471  1.00 41.14  ? 256 LYS A CE  1 
ATOM   1611 N NZ  . LYS A 1 241 ? 3.923   15.553 21.644  1.00 41.75  ? 256 LYS A NZ  1 
ATOM   1612 N N   . PHE A 1 242 ? -3.031  15.383 23.632  1.00 39.18  ? 257 PHE A N   1 
ATOM   1613 C CA  . PHE A 1 242 ? -4.137  15.553 22.703  1.00 38.83  ? 257 PHE A CA  1 
ATOM   1614 C C   . PHE A 1 242 ? -3.601  15.671 21.282  1.00 37.92  ? 257 PHE A C   1 
ATOM   1615 O O   . PHE A 1 242 ? -2.552  16.278 21.047  1.00 40.90  ? 257 PHE A O   1 
ATOM   1616 C CB  . PHE A 1 242 ? -4.958  16.790 23.068  1.00 36.96  ? 257 PHE A CB  1 
ATOM   1617 C CG  . PHE A 1 242 ? -5.858  16.598 24.261  1.00 38.83  ? 257 PHE A CG  1 
ATOM   1618 C CD1 . PHE A 1 242 ? -6.794  15.571 24.288  1.00 37.29  ? 257 PHE A CD1 1 
ATOM   1619 C CD2 . PHE A 1 242 ? -5.775  17.453 25.350  1.00 36.89  ? 257 PHE A CD2 1 
ATOM   1620 C CE1 . PHE A 1 242 ? -7.622  15.393 25.376  1.00 31.35  ? 257 PHE A CE1 1 
ATOM   1621 C CE2 . PHE A 1 242 ? -6.602  17.285 26.445  1.00 36.59  ? 257 PHE A CE2 1 
ATOM   1622 C CZ  . PHE A 1 242 ? -7.527  16.252 26.459  1.00 34.31  ? 257 PHE A CZ  1 
ATOM   1623 N N   . GLY A 1 243 ? -4.318  15.072 20.332  1.00 34.66  ? 258 GLY A N   1 
ATOM   1624 C CA  . GLY A 1 243 ? -3.939  15.136 18.938  1.00 42.28  ? 258 GLY A CA  1 
ATOM   1625 C C   . GLY A 1 243 ? -5.156  15.315 18.054  1.00 42.18  ? 258 GLY A C   1 
ATOM   1626 O O   . GLY A 1 243 ? -6.286  15.417 18.535  1.00 43.44  ? 258 GLY A O   1 
ATOM   1627 N N   . LEU A 1 244 ? -4.902  15.357 16.749  1.00 42.74  ? 259 LEU A N   1 
ATOM   1628 C CA  . LEU A 1 244 ? -5.950  15.421 15.739  1.00 43.20  ? 259 LEU A CA  1 
ATOM   1629 C C   . LEU A 1 244 ? -5.880  14.167 14.882  1.00 39.76  ? 259 LEU A C   1 
ATOM   1630 O O   . LEU A 1 244 ? -4.809  13.813 14.378  1.00 41.67  ? 259 LEU A O   1 
ATOM   1631 C CB  . LEU A 1 244 ? -5.811  16.673 14.868  1.00 39.37  ? 259 LEU A CB  1 
ATOM   1632 C CG  . LEU A 1 244 ? -6.004  18.022 15.566  1.00 41.60  ? 259 LEU A CG  1 
ATOM   1633 C CD1 . LEU A 1 244 ? -5.447  19.148 14.710  1.00 44.74  ? 259 LEU A CD1 1 
ATOM   1634 C CD2 . LEU A 1 244 ? -7.476  18.263 15.899  1.00 36.44  ? 259 LEU A CD2 1 
ATOM   1635 N N   . TRP A 1 245 ? -7.013  13.488 14.739  1.00 43.51  ? 260 TRP A N   1 
ATOM   1636 C CA  . TRP A 1 245 ? -7.094  12.283 13.923  1.00 46.46  ? 260 TRP A CA  1 
ATOM   1637 C C   . TRP A 1 245 ? -7.114  12.669 12.451  1.00 48.51  ? 260 TRP A C   1 
ATOM   1638 O O   . TRP A 1 245 ? -8.006  13.402 12.007  1.00 47.66  ? 260 TRP A O   1 
ATOM   1639 C CB  . TRP A 1 245 ? -8.337  11.476 14.285  1.00 41.22  ? 260 TRP A CB  1 
ATOM   1640 C CG  . TRP A 1 245 ? -8.358  10.088 13.715  1.00 47.60  ? 260 TRP A CG  1 
ATOM   1641 C CD1 . TRP A 1 245 ? -9.102  9.648  12.661  1.00 47.62  ? 260 TRP A CD1 1 
ATOM   1642 C CD2 . TRP A 1 245 ? -7.609  8.955  14.177  1.00 48.76  ? 260 TRP A CD2 1 
ATOM   1643 N NE1 . TRP A 1 245 ? -8.864  8.314  12.435  1.00 51.35  ? 260 TRP A NE1 1 
ATOM   1644 C CE2 . TRP A 1 245 ? -7.950  7.864  13.352  1.00 51.39  ? 260 TRP A CE2 1 
ATOM   1645 C CE3 . TRP A 1 245 ? -6.681  8.759  15.204  1.00 46.83  ? 260 TRP A CE3 1 
ATOM   1646 C CZ2 . TRP A 1 245 ? -7.401  6.593  13.527  1.00 49.08  ? 260 TRP A CZ2 1 
ATOM   1647 C CZ3 . TRP A 1 245 ? -6.136  7.495  15.375  1.00 48.17  ? 260 TRP A CZ3 1 
ATOM   1648 C CH2 . TRP A 1 245 ? -6.498  6.430  14.541  1.00 47.86  ? 260 TRP A CH2 1 
ATOM   1649 N N   . VAL A 1 246 ? -6.131  12.182 11.697  1.00 45.33  ? 261 VAL A N   1 
ATOM   1650 C CA  . VAL A 1 246 ? -5.988  12.496 10.276  1.00 45.98  ? 261 VAL A CA  1 
ATOM   1651 C C   . VAL A 1 246 ? -5.891  11.165 9.535   1.00 45.44  ? 261 VAL A C   1 
ATOM   1652 O O   . VAL A 1 246 ? -4.800  10.609 9.369   1.00 45.05  ? 261 VAL A O   1 
ATOM   1653 C CB  . VAL A 1 246 ? -4.770  13.378 9.986   1.00 47.23  ? 261 VAL A CB  1 
ATOM   1654 C CG1 . VAL A 1 246 ? -4.765  13.795 8.523   1.00 43.67  ? 261 VAL A CG1 1 
ATOM   1655 C CG2 . VAL A 1 246 ? -4.758  14.593 10.911  1.00 38.76  ? 261 VAL A CG2 1 
ATOM   1656 N N   . ASP A 1 247 ? -7.036  10.647 9.092   1.00 50.48  ? 262 ASP A N   1 
ATOM   1657 C CA  . ASP A 1 247 ? -7.121  9.468  8.228   1.00 55.81  ? 262 ASP A CA  1 
ATOM   1658 C C   . ASP A 1 247 ? -6.241  8.323  8.741   1.00 52.35  ? 262 ASP A C   1 
ATOM   1659 O O   . ASP A 1 247 ? -5.250  7.931  8.123   1.00 52.08  ? 262 ASP A O   1 
ATOM   1660 C CB  . ASP A 1 247 ? -6.756  9.825  6.784   1.00 52.06  ? 262 ASP A CB  1 
ATOM   1661 C CG  . ASP A 1 247 ? -7.237  8.786  5.787   1.00 55.96  ? 262 ASP A CG  1 
ATOM   1662 O OD1 . ASP A 1 247 ? -8.135  7.990  6.143   1.00 54.86  ? 262 ASP A OD1 1 
ATOM   1663 O OD2 . ASP A 1 247 ? -6.704  8.753  4.657   1.00 56.37  ? 262 ASP A OD2 1 
ATOM   1664 N N   . GLY A 1 248 ? -6.627  7.808  9.905   1.00 47.20  ? 263 GLY A N   1 
ATOM   1665 C CA  . GLY A 1 248 ? -6.051  6.581  10.415  1.00 47.47  ? 263 GLY A CA  1 
ATOM   1666 C C   . GLY A 1 248 ? -4.861  6.720  11.339  1.00 48.78  ? 263 GLY A C   1 
ATOM   1667 O O   . GLY A 1 248 ? -4.235  5.702  11.663  1.00 46.33  ? 263 GLY A O   1 
ATOM   1668 N N   . ASN A 1 249 ? -4.521  7.932  11.774  1.00 45.84  ? 264 ASN A N   1 
ATOM   1669 C CA  . ASN A 1 249 ? -3.455  8.105  12.749  1.00 41.94  ? 264 ASN A CA  1 
ATOM   1670 C C   . ASN A 1 249 ? -3.658  9.417  13.494  1.00 46.56  ? 264 ASN A C   1 
ATOM   1671 O O   . ASN A 1 249 ? -4.150  10.400 12.929  1.00 42.60  ? 264 ASN A O   1 
ATOM   1672 C CB  . ASN A 1 249 ? -2.068  8.075  12.095  1.00 42.29  ? 264 ASN A CB  1 
ATOM   1673 C CG  . ASN A 1 249 ? -0.941  8.054  13.121  1.00 48.85  ? 264 ASN A CG  1 
ATOM   1674 O OD1 . ASN A 1 249 ? -0.951  7.241  14.046  1.00 49.89  ? 264 ASN A OD1 1 
ATOM   1675 N ND2 . ASN A 1 249 ? 0.026   8.958  12.971  1.00 42.53  ? 264 ASN A ND2 1 
ATOM   1676 N N   . CYS A 1 250 ? -3.270  9.418  14.771  1.00 43.05  ? 265 CYS A N   1 
ATOM   1677 C CA  . CYS A 1 250 ? -3.352  10.605 15.613  1.00 42.41  ? 265 CYS A CA  1 
ATOM   1678 C C   . CYS A 1 250 ? -2.105  11.460 15.417  1.00 39.73  ? 265 CYS A C   1 
ATOM   1679 O O   . CYS A 1 250 ? -0.980  10.966 15.532  1.00 43.30  ? 265 CYS A O   1 
ATOM   1680 C CB  . CYS A 1 250 ? -3.513  10.219 17.090  1.00 43.09  ? 265 CYS A CB  1 
ATOM   1681 S SG  . CYS A 1 250 ? -4.145  11.577 18.169  1.00 47.93  ? 265 CYS A SG  1 
ATOM   1682 N N   . GLU A 1 251 ? -2.307  12.741 15.125  1.00 39.52  ? 266 GLU A N   1 
ATOM   1683 C CA  . GLU A 1 251 ? -1.229  13.623 14.710  1.00 41.55  ? 266 GLU A CA  1 
ATOM   1684 C C   . GLU A 1 251 ? -1.138  14.828 15.635  1.00 38.98  ? 266 GLU A C   1 
ATOM   1685 O O   . GLU A 1 251 ? -2.101  15.188 16.319  1.00 46.59  ? 266 GLU A O   1 
ATOM   1686 C CB  . GLU A 1 251 ? -1.431  14.093 13.260  1.00 46.05  ? 266 GLU A CB  1 
ATOM   1687 C CG  . GLU A 1 251 ? -1.689  12.952 12.276  1.00 41.05  ? 266 GLU A CG  1 
ATOM   1688 C CD  . GLU A 1 251 ? -0.408  12.236 11.885  1.00 43.79  ? 266 GLU A CD  1 
ATOM   1689 O OE1 . GLU A 1 251 ? 0.680   12.784 12.165  1.00 42.80  ? 266 GLU A OE1 1 
ATOM   1690 O OE2 . GLU A 1 251 ? -0.484  11.126 11.314  1.00 45.60  ? 266 GLU A OE2 1 
ATOM   1691 N N   . GLU A 1 252 ? 0.038   15.453 15.639  1.00 39.89  ? 267 GLU A N   1 
ATOM   1692 C CA  . GLU A 1 252 ? 0.271   16.622 16.475  1.00 41.31  ? 267 GLU A CA  1 
ATOM   1693 C C   . GLU A 1 252 ? -0.621  17.779 16.045  1.00 45.57  ? 267 GLU A C   1 
ATOM   1694 O O   . GLU A 1 252 ? -0.950  17.937 14.867  1.00 49.89  ? 267 GLU A O   1 
ATOM   1695 C CB  . GLU A 1 252 ? 1.736   17.054 16.401  1.00 38.84  ? 267 GLU A CB  1 
ATOM   1696 C CG  . GLU A 1 252 ? 2.720   16.057 16.988  1.00 41.41  ? 267 GLU A CG  1 
ATOM   1697 C CD  . GLU A 1 252 ? 2.792   16.114 18.505  1.00 50.16  ? 267 GLU A CD  1 
ATOM   1698 O OE1 . GLU A 1 252 ? 2.296   17.099 19.095  1.00 46.76  ? 267 GLU A OE1 1 
ATOM   1699 O OE2 . GLU A 1 252 ? 3.355   15.174 19.109  1.00 55.19  ? 267 GLU A OE2 1 
ATOM   1700 N N   . ILE A 1 253 ? -1.012  18.592 17.020  1.00 45.99  ? 268 ILE A N   1 
ATOM   1701 C CA  . ILE A 1 253 ? -1.755  19.820 16.757  1.00 45.93  ? 268 ILE A CA  1 
ATOM   1702 C C   . ILE A 1 253 ? -0.746  20.874 16.320  1.00 46.59  ? 268 ILE A C   1 
ATOM   1703 O O   . ILE A 1 253 ? 0.099   21.288 17.124  1.00 51.46  ? 268 ILE A O   1 
ATOM   1704 C CB  . ILE A 1 253 ? -2.551  20.266 17.993  1.00 49.07  ? 268 ILE A CB  1 
ATOM   1705 C CG1 . ILE A 1 253 ? -3.623  19.229 18.324  1.00 44.42  ? 268 ILE A CG1 1 
ATOM   1706 C CG2 . ILE A 1 253 ? -3.196  21.624 17.759  1.00 48.71  ? 268 ILE A CG2 1 
ATOM   1707 C CD1 . ILE A 1 253 ? -3.855  19.055 19.799  1.00 39.34  ? 268 ILE A CD1 1 
ATOM   1708 N N   . PRO A 1 254 ? -0.784  21.326 15.063  1.00 50.08  ? 269 PRO A N   1 
ATOM   1709 C CA  . PRO A 1 254 ? 0.292   22.214 14.584  1.00 51.45  ? 269 PRO A CA  1 
ATOM   1710 C C   . PRO A 1 254 ? 0.308   23.587 15.240  1.00 52.70  ? 269 PRO A C   1 
ATOM   1711 O O   . PRO A 1 254 ? 1.391   24.106 15.543  1.00 50.07  ? 269 PRO A O   1 
ATOM   1712 C CB  . PRO A 1 254 ? 0.025   22.304 13.072  1.00 46.94  ? 269 PRO A CB  1 
ATOM   1713 C CG  . PRO A 1 254 ? -1.392  21.881 12.893  1.00 48.30  ? 269 PRO A CG  1 
ATOM   1714 C CD  . PRO A 1 254 ? -1.690  20.904 13.982  1.00 50.05  ? 269 PRO A CD  1 
ATOM   1715 N N   . TYR A 1 255 ? -0.851  24.201 15.466  1.00 52.54  ? 270 TYR A N   1 
ATOM   1716 C CA  . TYR A 1 255 ? -0.925  25.543 16.038  1.00 48.03  ? 270 TYR A CA  1 
ATOM   1717 C C   . TYR A 1 255 ? -1.212  25.431 17.533  1.00 47.44  ? 270 TYR A C   1 
ATOM   1718 O O   . TYR A 1 255 ? -2.340  25.131 17.935  1.00 48.42  ? 270 TYR A O   1 
ATOM   1719 C CB  . TYR A 1 255 ? -1.993  26.375 15.331  1.00 48.55  ? 270 TYR A CB  1 
ATOM   1720 N N   . VAL A 1 256 ? -0.185  25.670 18.353  1.00 48.46  ? 271 VAL A N   1 
ATOM   1721 C CA  . VAL A 1 256 ? -0.302  25.661 19.806  1.00 47.03  ? 271 VAL A CA  1 
ATOM   1722 C C   . VAL A 1 256 ? 0.523   26.816 20.363  1.00 50.58  ? 271 VAL A C   1 
ATOM   1723 O O   . VAL A 1 256 ? 1.426   27.337 19.707  1.00 54.64  ? 271 VAL A O   1 
ATOM   1724 C CB  . VAL A 1 256 ? 0.170   24.326 20.431  1.00 48.17  ? 271 VAL A CB  1 
ATOM   1725 C CG1 . VAL A 1 256 ? -0.676  23.156 19.937  1.00 38.26  ? 271 VAL A CG1 1 
ATOM   1726 C CG2 . VAL A 1 256 ? 1.651   24.098 20.137  1.00 45.05  ? 271 VAL A CG2 1 
ATOM   1727 N N   . LYS A 1 257 ? 0.204   27.213 21.594  1.00 52.30  ? 272 LYS A N   1 
ATOM   1728 C CA  . LYS A 1 257 ? 0.933   28.262 22.300  1.00 49.30  ? 272 LYS A CA  1 
ATOM   1729 C C   . LYS A 1 257 ? 1.696   27.629 23.455  1.00 52.01  ? 272 LYS A C   1 
ATOM   1730 O O   . LYS A 1 257 ? 1.096   26.952 24.299  1.00 45.41  ? 272 LYS A O   1 
ATOM   1731 C CB  . LYS A 1 257 ? -0.013  29.348 22.812  1.00 50.10  ? 272 LYS A CB  1 
ATOM   1732 C CG  . LYS A 1 257 ? 0.690   30.508 23.506  1.00 55.27  ? 272 LYS A CG  1 
ATOM   1733 C CD  . LYS A 1 257 ? -0.315  31.509 24.075  1.00 65.56  ? 272 LYS A CD  1 
ATOM   1734 C CE  . LYS A 1 257 ? 0.260   32.919 24.147  1.00 64.56  ? 272 LYS A CE  1 
ATOM   1735 N NZ  . LYS A 1 257 ? -0.686  33.931 23.590  1.00 64.64  ? 272 LYS A NZ  1 
ATOM   1736 N N   . GLU A 1 258 ? 3.010   27.846 23.488  1.00 50.11  ? 273 GLU A N   1 
ATOM   1737 C CA  . GLU A 1 258 ? 3.870   27.248 24.500  1.00 47.10  ? 273 GLU A CA  1 
ATOM   1738 C C   . GLU A 1 258 ? 4.013   28.186 25.689  1.00 50.91  ? 273 GLU A C   1 
ATOM   1739 O O   . GLU A 1 258 ? 4.257   29.386 25.518  1.00 49.59  ? 273 GLU A O   1 
ATOM   1740 C CB  . GLU A 1 258 ? 5.252   26.926 23.929  1.00 49.48  ? 273 GLU A CB  1 
ATOM   1741 C CG  . GLU A 1 258 ? 6.173   26.252 24.931  1.00 47.77  ? 273 GLU A CG  1 
ATOM   1742 C CD  . GLU A 1 258 ? 7.599   26.134 24.435  1.00 53.31  ? 273 GLU A CD  1 
ATOM   1743 O OE1 . GLU A 1 258 ? 7.788   25.954 23.214  1.00 53.36  ? 273 GLU A OE1 1 
ATOM   1744 O OE2 . GLU A 1 258 ? 8.530   26.221 25.267  1.00 54.01  ? 273 GLU A OE2 1 
ATOM   1745 N N   . VAL A 1 259 ? 3.858   27.635 26.890  1.00 47.21  ? 274 VAL A N   1 
ATOM   1746 C CA  . VAL A 1 259 ? 3.998   28.386 28.131  1.00 46.19  ? 274 VAL A CA  1 
ATOM   1747 C C   . VAL A 1 259 ? 4.823   27.553 29.101  1.00 47.58  ? 274 VAL A C   1 
ATOM   1748 O O   . VAL A 1 259 ? 4.667   26.329 29.170  1.00 47.49  ? 274 VAL A O   1 
ATOM   1749 C CB  . VAL A 1 259 ? 2.625   28.739 28.750  1.00 50.25  ? 274 VAL A CB  1 
ATOM   1750 C CG1 . VAL A 1 259 ? 2.787   29.708 29.925  1.00 40.55  ? 274 VAL A CG1 1 
ATOM   1751 C CG2 . VAL A 1 259 ? 1.688   29.323 27.700  1.00 46.43  ? 274 VAL A CG2 1 
ATOM   1752 N N   . GLU A 1 260 ? 5.705   28.214 29.846  1.00 46.54  ? 275 GLU A N   1 
ATOM   1753 C CA  . GLU A 1 260 ? 6.428   27.529 30.907  1.00 51.02  ? 275 GLU A CA  1 
ATOM   1754 C C   . GLU A 1 260 ? 5.447   27.049 31.967  1.00 47.86  ? 275 GLU A C   1 
ATOM   1755 O O   . GLU A 1 260 ? 4.479   27.738 32.294  1.00 47.99  ? 275 GLU A O   1 
ATOM   1756 C CB  . GLU A 1 260 ? 7.468   28.457 31.539  1.00 50.98  ? 275 GLU A CB  1 
ATOM   1757 C CG  . GLU A 1 260 ? 8.848   28.392 30.902  1.00 61.17  ? 275 GLU A CG  1 
ATOM   1758 C CD  . GLU A 1 260 ? 9.604   29.708 31.019  1.00 78.37  ? 275 GLU A CD  1 
ATOM   1759 O OE1 . GLU A 1 260 ? 8.943   30.769 31.050  1.00 74.13  ? 275 GLU A OE1 1 
ATOM   1760 O OE2 . GLU A 1 260 ? 10.856  29.686 31.082  1.00 76.69  ? 275 GLU A OE2 1 
ATOM   1761 N N   . ALA A 1 261 ? 5.693   25.852 32.493  1.00 44.73  ? 276 ALA A N   1 
ATOM   1762 C CA  . ALA A 1 261 ? 4.885   25.308 33.578  1.00 47.29  ? 276 ALA A CA  1 
ATOM   1763 C C   . ALA A 1 261 ? 5.725   24.302 34.346  1.00 46.96  ? 276 ALA A C   1 
ATOM   1764 O O   . ALA A 1 261 ? 6.256   23.359 33.753  1.00 47.00  ? 276 ALA A O   1 
ATOM   1765 C CB  . ALA A 1 261 ? 3.605   24.647 33.054  1.00 44.61  ? 276 ALA A CB  1 
ATOM   1766 N N   . LYS A 1 262 ? 5.837   24.502 35.662  1.00 44.02  ? 277 LYS A N   1 
ATOM   1767 C CA  . LYS A 1 262 ? 6.707   23.649 36.463  1.00 40.91  ? 277 LYS A CA  1 
ATOM   1768 C C   . LYS A 1 262 ? 6.122   22.255 36.661  1.00 50.27  ? 277 LYS A C   1 
ATOM   1769 O O   . LYS A 1 262 ? 6.879   21.288 36.805  1.00 53.63  ? 277 LYS A O   1 
ATOM   1770 C CB  . LYS A 1 262 ? 6.985   24.300 37.820  1.00 49.86  ? 277 LYS A CB  1 
ATOM   1771 C CG  . LYS A 1 262 ? 5.757   24.461 38.703  1.00 53.95  ? 277 LYS A CG  1 
ATOM   1772 C CD  . LYS A 1 262 ? 5.978   25.477 39.811  1.00 53.05  ? 277 LYS A CD  1 
ATOM   1773 C CE  . LYS A 1 262 ? 5.287   25.024 41.090  1.00 58.68  ? 277 LYS A CE  1 
ATOM   1774 N NZ  . LYS A 1 262 ? 4.567   26.142 41.765  1.00 64.28  ? 277 LYS A NZ  1 
ATOM   1775 N N   . ASP A 1 263 ? 4.797   22.125 36.679  1.00 44.10  ? 278 ASP A N   1 
ATOM   1776 C CA  . ASP A 1 263 ? 4.167   20.834 36.918  1.00 38.94  ? 278 ASP A CA  1 
ATOM   1777 C C   . ASP A 1 263 ? 2.780   20.836 36.284  1.00 41.53  ? 278 ASP A C   1 
ATOM   1778 O O   . ASP A 1 263 ? 2.342   21.830 35.700  1.00 41.85  ? 278 ASP A O   1 
ATOM   1779 C CB  . ASP A 1 263 ? 4.106   20.512 38.415  1.00 46.50  ? 278 ASP A CB  1 
ATOM   1780 C CG  . ASP A 1 263 ? 3.453   21.617 39.236  1.00 48.43  ? 278 ASP A CG  1 
ATOM   1781 O OD1 . ASP A 1 263 ? 2.596   22.357 38.701  1.00 49.03  ? 278 ASP A OD1 1 
ATOM   1782 O OD2 . ASP A 1 263 ? 3.791   21.739 40.431  1.00 54.15  ? 278 ASP A OD2 1 
ATOM   1783 N N   . LEU A 1 264 ? 2.086   19.702 36.417  1.00 40.73  ? 279 LEU A N   1 
ATOM   1784 C CA  . LEU A 1 264 ? 0.751   19.575 35.841  1.00 41.78  ? 279 LEU A CA  1 
ATOM   1785 C C   . LEU A 1 264 ? -0.207  20.603 36.426  1.00 44.47  ? 279 LEU A C   1 
ATOM   1786 O O   . LEU A 1 264 ? -0.993  21.217 35.694  1.00 40.23  ? 279 LEU A O   1 
ATOM   1787 C CB  . LEU A 1 264 ? 0.214   18.164 36.067  1.00 40.38  ? 279 LEU A CB  1 
ATOM   1788 C CG  . LEU A 1 264 ? -1.270  17.991 35.743  1.00 43.17  ? 279 LEU A CG  1 
ATOM   1789 C CD1 . LEU A 1 264 ? -1.507  18.162 34.251  1.00 33.59  ? 279 LEU A CD1 1 
ATOM   1790 C CD2 . LEU A 1 264 ? -1.764  16.643 36.218  1.00 38.68  ? 279 LEU A CD2 1 
ATOM   1791 N N   . ARG A 1 265 ? -0.153  20.801 37.746  1.00 42.85  ? 280 ARG A N   1 
ATOM   1792 C CA  . ARG A 1 265 ? -1.009  21.788 38.398  1.00 44.74  ? 280 ARG A CA  1 
ATOM   1793 C C   . ARG A 1 265 ? -0.874  23.160 37.746  1.00 43.23  ? 280 ARG A C   1 
ATOM   1794 O O   . ARG A 1 265 ? -1.876  23.814 37.435  1.00 40.66  ? 280 ARG A O   1 
ATOM   1795 C CB  . ARG A 1 265 ? -0.669  21.868 39.888  1.00 44.26  ? 280 ARG A CB  1 
ATOM   1796 C CG  . ARG A 1 265 ? -1.825  22.331 40.754  1.00 46.40  ? 280 ARG A CG  1 
ATOM   1797 C CD  . ARG A 1 265 ? -1.357  23.307 41.813  1.00 51.43  ? 280 ARG A CD  1 
ATOM   1798 N NE  . ARG A 1 265 ? -0.091  22.904 42.414  1.00 57.04  ? 280 ARG A NE  1 
ATOM   1799 C CZ  . ARG A 1 265 ? 0.016   22.246 43.560  1.00 56.84  ? 280 ARG A CZ  1 
ATOM   1800 N NH1 . ARG A 1 265 ? -1.054  21.882 44.249  1.00 55.16  ? 280 ARG A NH1 1 
ATOM   1801 N NH2 . ARG A 1 265 ? 1.225   21.941 44.023  1.00 52.46  ? 280 ARG A NH2 1 
ATOM   1802 N N   . GLU A 1 266 ? 0.362   23.609 37.527  1.00 42.01  ? 281 GLU A N   1 
ATOM   1803 C CA  . GLU A 1 266 ? 0.567   24.919 36.920  1.00 42.14  ? 281 GLU A CA  1 
ATOM   1804 C C   . GLU A 1 266 ? 0.050   24.947 35.487  1.00 42.35  ? 281 GLU A C   1 
ATOM   1805 O O   . GLU A 1 266 ? -0.560  25.935 35.058  1.00 42.75  ? 281 GLU A O   1 
ATOM   1806 C CB  . GLU A 1 266 ? 2.048   25.292 36.976  1.00 44.29  ? 281 GLU A CB  1 
ATOM   1807 C CG  . GLU A 1 266 ? 2.416   26.512 36.160  1.00 48.28  ? 281 GLU A CG  1 
ATOM   1808 C CD  . GLU A 1 266 ? 3.577   27.292 36.757  1.00 58.54  ? 281 GLU A CD  1 
ATOM   1809 O OE1 . GLU A 1 266 ? 4.697   27.210 36.202  1.00 59.75  ? 281 GLU A OE1 1 
ATOM   1810 O OE2 . GLU A 1 266 ? 3.369   27.998 37.767  1.00 62.46  ? 281 GLU A OE2 1 
ATOM   1811 N N   . CYS A 1 267 ? 0.273   23.869 34.734  1.00 41.38  ? 282 CYS A N   1 
ATOM   1812 C CA  . CYS A 1 267 ? -0.264  23.793 33.380  1.00 40.98  ? 282 CYS A CA  1 
ATOM   1813 C C   . CYS A 1 267 ? -1.788  23.815 33.389  1.00 38.63  ? 282 CYS A C   1 
ATOM   1814 O O   . CYS A 1 267 ? -2.415  24.489 32.563  1.00 39.36  ? 282 CYS A O   1 
ATOM   1815 C CB  . CYS A 1 267 ? 0.253   22.533 32.692  1.00 37.58  ? 282 CYS A CB  1 
ATOM   1816 S SG  . CYS A 1 267 ? -0.229  22.378 30.981  1.00 44.29  ? 282 CYS A SG  1 
ATOM   1817 N N   . ASN A 1 268 ? -2.401  23.085 34.321  1.00 38.08  ? 283 ASN A N   1 
ATOM   1818 C CA  . ASN A 1 268 ? -3.854  23.084 34.424  1.00 36.61  ? 283 ASN A CA  1 
ATOM   1819 C C   . ASN A 1 268 ? -4.381  24.462 34.815  1.00 40.89  ? 283 ASN A C   1 
ATOM   1820 O O   . ASN A 1 268 ? -5.457  24.876 34.363  1.00 38.86  ? 283 ASN A O   1 
ATOM   1821 C CB  . ASN A 1 268 ? -4.293  22.020 35.428  1.00 39.02  ? 283 ASN A CB  1 
ATOM   1822 C CG  . ASN A 1 268 ? -5.782  22.028 35.675  1.00 36.29  ? 283 ASN A CG  1 
ATOM   1823 O OD1 . ASN A 1 268 ? -6.250  22.618 36.644  1.00 37.02  ? 283 ASN A OD1 1 
ATOM   1824 N ND2 . ASN A 1 268 ? -6.537  21.359 34.807  1.00 33.69  ? 283 ASN A ND2 1 
ATOM   1825 N N   . ARG A 1 269 ? -3.632  25.192 35.646  1.00 37.21  ? 284 ARG A N   1 
ATOM   1826 C CA  . ARG A 1 269 ? -4.049  26.541 36.019  1.00 41.21  ? 284 ARG A CA  1 
ATOM   1827 C C   . ARG A 1 269 ? -3.879  27.512 34.856  1.00 40.49  ? 284 ARG A C   1 
ATOM   1828 O O   . ARG A 1 269 ? -4.728  28.386 34.640  1.00 39.98  ? 284 ARG A O   1 
ATOM   1829 C CB  . ARG A 1 269 ? -3.263  27.027 37.242  1.00 40.59  ? 284 ARG A CB  1 
ATOM   1830 C CG  . ARG A 1 269 ? -4.021  28.046 38.085  1.00 46.28  ? 284 ARG A CG  1 
ATOM   1831 C CD  . ARG A 1 269 ? -3.108  29.038 38.798  1.00 41.39  ? 284 ARG A CD  1 
ATOM   1832 N NE  . ARG A 1 269 ? -2.684  28.566 40.112  1.00 55.03  ? 284 ARG A NE  1 
ATOM   1833 C CZ  . ARG A 1 269 ? -2.785  29.269 41.234  1.00 56.48  ? 284 ARG A CZ  1 
ATOM   1834 N NH1 . ARG A 1 269 ? -3.347  30.469 41.252  1.00 51.04  ? 284 ARG A NH1 1 
ATOM   1835 N NH2 . ARG A 1 269 ? -2.314  28.754 42.368  1.00 49.64  ? 284 ARG A NH2 1 
ATOM   1836 N N   . ILE A 1 270 ? -2.789  27.376 34.096  1.00 41.49  ? 285 ILE A N   1 
ATOM   1837 C CA  . ILE A 1 270 ? -2.556  28.260 32.957  1.00 39.53  ? 285 ILE A CA  1 
ATOM   1838 C C   . ILE A 1 270 ? -3.689  28.134 31.951  1.00 38.43  ? 285 ILE A C   1 
ATOM   1839 O O   . ILE A 1 270 ? -4.247  29.135 31.486  1.00 39.76  ? 285 ILE A O   1 
ATOM   1840 C CB  . ILE A 1 270 ? -1.197  27.955 32.301  1.00 40.56  ? 285 ILE A CB  1 
ATOM   1841 C CG1 . ILE A 1 270 ? -0.055  28.533 33.136  1.00 43.77  ? 285 ILE A CG1 1 
ATOM   1842 C CG2 . ILE A 1 270 ? -1.154  28.501 30.874  1.00 35.62  ? 285 ILE A CG2 1 
ATOM   1843 C CD1 . ILE A 1 270 ? 1.228   27.751 33.006  1.00 45.68  ? 285 ILE A CD1 1 
ATOM   1844 N N   . VAL A 1 271 ? -4.047  26.897 31.598  1.00 39.57  ? 286 VAL A N   1 
ATOM   1845 C CA  . VAL A 1 271 ? -5.091  26.695 30.606  1.00 36.61  ? 286 VAL A CA  1 
ATOM   1846 C C   . VAL A 1 271 ? -6.456  27.084 31.162  1.00 39.47  ? 286 VAL A C   1 
ATOM   1847 O O   . VAL A 1 271 ? -7.359  27.441 30.393  1.00 35.17  ? 286 VAL A O   1 
ATOM   1848 C CB  . VAL A 1 271 ? -5.062  25.238 30.095  1.00 34.57  ? 286 VAL A CB  1 
ATOM   1849 C CG1 . VAL A 1 271 ? -5.582  24.267 31.161  1.00 32.80  ? 286 VAL A CG1 1 
ATOM   1850 C CG2 . VAL A 1 271 ? -5.847  25.107 28.795  1.00 35.93  ? 286 VAL A CG2 1 
ATOM   1851 N N   . PHE A 1 272 ? -6.630  27.051 32.488  1.00 38.28  ? 287 PHE A N   1 
ATOM   1852 C CA  . PHE A 1 272 ? -7.859  27.584 33.066  1.00 40.67  ? 287 PHE A CA  1 
ATOM   1853 C C   . PHE A 1 272 ? -7.910  29.099 32.929  1.00 37.89  ? 287 PHE A C   1 
ATOM   1854 O O   . PHE A 1 272 ? -8.977  29.669 32.678  1.00 39.64  ? 287 PHE A O   1 
ATOM   1855 C CB  . PHE A 1 272 ? -7.988  27.179 34.534  1.00 39.14  ? 287 PHE A CB  1 
ATOM   1856 C CG  . PHE A 1 272 ? -9.164  27.809 35.226  1.00 37.16  ? 287 PHE A CG  1 
ATOM   1857 C CD1 . PHE A 1 272 ? -10.433 27.267 35.089  1.00 35.43  ? 287 PHE A CD1 1 
ATOM   1858 C CD2 . PHE A 1 272 ? -9.005  28.953 35.999  1.00 35.32  ? 287 PHE A CD2 1 
ATOM   1859 C CE1 . PHE A 1 272 ? -11.530 27.844 35.718  1.00 34.67  ? 287 PHE A CE1 1 
ATOM   1860 C CE2 . PHE A 1 272 ? -10.093 29.536 36.630  1.00 38.93  ? 287 PHE A CE2 1 
ATOM   1861 C CZ  . PHE A 1 272 ? -11.361 28.978 36.488  1.00 36.47  ? 287 PHE A CZ  1 
ATOM   1862 N N   . GLU A 1 273 ? -6.768  29.767 33.084  1.00 37.18  ? 288 GLU A N   1 
ATOM   1863 C CA  . GLU A 1 273 ? -6.747  31.216 32.922  1.00 43.51  ? 288 GLU A CA  1 
ATOM   1864 C C   . GLU A 1 273 ? -7.036  31.624 31.482  1.00 42.18  ? 288 GLU A C   1 
ATOM   1865 O O   . GLU A 1 273 ? -7.570  32.712 31.245  1.00 42.50  ? 288 GLU A O   1 
ATOM   1866 C CB  . GLU A 1 273 ? -5.398  31.774 33.376  1.00 42.50  ? 288 GLU A CB  1 
ATOM   1867 C CG  . GLU A 1 273 ? -5.206  31.778 34.890  1.00 56.00  ? 288 GLU A CG  1 
ATOM   1868 C CD  . GLU A 1 273 ? -5.070  33.177 35.465  1.00 75.72  ? 288 GLU A CD  1 
ATOM   1869 O OE1 . GLU A 1 273 ? -4.606  33.300 36.624  1.00 73.24  ? 288 GLU A OE1 1 
ATOM   1870 O OE2 . GLU A 1 273 ? -5.422  34.149 34.755  1.00 77.20  ? 288 GLU A OE2 1 
ATOM   1871 N N   . ALA A 1 274 ? -6.709  30.765 30.519  1.00 38.18  ? 289 ALA A N   1 
ATOM   1872 C CA  . ALA A 1 274 ? -6.899  31.059 29.105  1.00 42.31  ? 289 ALA A CA  1 
ATOM   1873 C C   . ALA A 1 274 ? -8.202  30.510 28.539  1.00 40.24  ? 289 ALA A C   1 
ATOM   1874 O O   . ALA A 1 274 ? -8.483  30.732 27.357  1.00 38.06  ? 289 ALA A O   1 
ATOM   1875 C CB  . ALA A 1 274 ? -5.724  30.499 28.295  1.00 38.76  ? 289 ALA A CB  1 
ATOM   1876 N N   . SER A 1 275 ? -9.004  29.813 29.343  1.00 36.94  ? 290 SER A N   1 
ATOM   1877 C CA  . SER A 1 275 ? -10.111 29.026 28.815  1.00 40.95  ? 290 SER A CA  1 
ATOM   1878 C C   . SER A 1 275 ? -11.268 29.915 28.370  1.00 39.70  ? 290 SER A C   1 
ATOM   1879 O O   . SER A 1 275 ? -11.238 31.140 28.502  1.00 44.42  ? 290 SER A O   1 
ATOM   1880 C CB  . SER A 1 275 ? -10.598 28.022 29.855  1.00 38.76  ? 290 SER A CB  1 
ATOM   1881 O OG  . SER A 1 275 ? -11.201 28.672 30.959  1.00 36.57  ? 290 SER A OG  1 
ATOM   1882 N N   . ALA A 1 276 ? -12.308 29.267 27.839  1.00 42.65  ? 291 ALA A N   1 
ATOM   1883 C CA  . ALA A 1 276 ? -13.512 29.963 27.406  1.00 43.33  ? 291 ALA A CA  1 
ATOM   1884 C C   . ALA A 1 276 ? -14.083 30.795 28.544  1.00 45.49  ? 291 ALA A C   1 
ATOM   1885 O O   . ALA A 1 276 ? -14.168 30.336 29.687  1.00 45.97  ? 291 ALA A O   1 
ATOM   1886 C CB  . ALA A 1 276 ? -14.557 28.956 26.913  1.00 36.61  ? 291 ALA A CB  1 
ATOM   1887 N N   . SER A 1 277 ? -14.472 32.029 28.223  1.00 41.40  ? 292 SER A N   1 
ATOM   1888 C CA  . SER A 1 277 ? -14.974 32.962 29.218  1.00 42.77  ? 292 SER A CA  1 
ATOM   1889 C C   . SER A 1 277 ? -16.193 33.693 28.677  1.00 46.22  ? 292 SER A C   1 
ATOM   1890 O O   . SER A 1 277 ? -16.242 34.043 27.495  1.00 44.92  ? 292 SER A O   1 
ATOM   1891 C CB  . SER A 1 277 ? -13.890 33.968 29.622  1.00 42.52  ? 292 SER A CB  1 
ATOM   1892 O OG  . SER A 1 277 ? -14.362 34.846 30.625  1.00 47.38  ? 292 SER A OG  1 
ATOM   1893 N N   . ASP A 1 278 ? -17.178 33.913 29.549  1.00 45.85  ? 293 ASP A N   1 
ATOM   1894 C CA  . ASP A 1 278 ? -18.365 34.687 29.217  1.00 44.10  ? 293 ASP A CA  1 
ATOM   1895 C C   . ASP A 1 278 ? -18.324 36.097 29.790  1.00 43.69  ? 293 ASP A C   1 
ATOM   1896 O O   . ASP A 1 278 ? -19.325 36.814 29.710  1.00 45.76  ? 293 ASP A O   1 
ATOM   1897 C CB  . ASP A 1 278 ? -19.629 33.978 29.711  1.00 42.05  ? 293 ASP A CB  1 
ATOM   1898 C CG  . ASP A 1 278 ? -19.770 32.577 29.160  1.00 40.95  ? 293 ASP A CG  1 
ATOM   1899 O OD1 . ASP A 1 278 ? -19.170 32.294 28.103  1.00 44.80  ? 293 ASP A OD1 1 
ATOM   1900 O OD2 . ASP A 1 278 ? -20.491 31.761 29.780  1.00 40.11  ? 293 ASP A OD2 1 
ATOM   1901 N N   . GLN A 1 279 ? -17.200 36.504 30.367  1.00 46.97  ? 294 GLN A N   1 
ATOM   1902 C CA  . GLN A 1 279 ? -17.139 37.786 31.062  1.00 52.60  ? 294 GLN A CA  1 
ATOM   1903 C C   . GLN A 1 279 ? -17.203 38.937 30.063  1.00 59.51  ? 294 GLN A C   1 
ATOM   1904 O O   . GLN A 1 279 ? -16.465 38.932 29.069  1.00 59.20  ? 294 GLN A O   1 
ATOM   1905 C CB  . GLN A 1 279 ? -15.864 37.875 31.898  1.00 50.81  ? 294 GLN A CB  1 
ATOM   1906 C CG  . GLN A 1 279 ? -15.746 39.147 32.724  1.00 50.82  ? 294 GLN A CG  1 
ATOM   1907 C CD  . GLN A 1 279 ? -16.614 39.114 33.972  1.00 51.54  ? 294 GLN A CD  1 
ATOM   1908 O OE1 . GLN A 1 279 ? -17.235 38.099 34.287  1.00 51.42  ? 294 GLN A OE1 1 
ATOM   1909 N NE2 . GLN A 1 279 ? -16.663 40.230 34.687  1.00 53.58  ? 294 GLN A NE2 1 
ATOM   1910 N N   . PRO A 1 280 ? -18.063 39.943 30.291  1.00 62.37  ? 295 PRO A N   1 
ATOM   1911 C CA  . PRO A 1 280 ? -18.252 41.092 29.392  1.00 66.84  ? 295 PRO A CA  1 
ATOM   1912 C C   . PRO A 1 280 ? -16.994 41.947 29.240  1.00 62.82  ? 295 PRO A C   1 
ATOM   1913 O O   . PRO A 1 280 ? -16.490 42.452 30.243  1.00 71.72  ? 295 PRO A O   1 
ATOM   1914 C CB  . PRO A 1 280 ? -19.373 41.891 30.070  1.00 63.50  ? 295 PRO A CB  1 
ATOM   1915 C CG  . PRO A 1 280 ? -20.052 40.910 30.988  1.00 65.04  ? 295 PRO A CG  1 
ATOM   1916 C CD  . PRO A 1 280 ? -18.959 40.004 31.458  1.00 57.94  ? 295 PRO A CD  1 
ATOM   1917 N N   . ASP A 1 289 ? -21.702 51.914 40.303  1.00 69.77  ? 304 ASP A N   1 
ATOM   1918 C CA  . ASP A 1 289 ? -20.862 52.509 41.339  1.00 68.24  ? 304 ASP A CA  1 
ATOM   1919 C C   . ASP A 1 289 ? -20.634 51.538 42.496  1.00 63.45  ? 304 ASP A C   1 
ATOM   1920 O O   . ASP A 1 289 ? -21.567 50.885 42.969  1.00 60.96  ? 304 ASP A O   1 
ATOM   1921 C CB  . ASP A 1 289 ? -21.486 53.807 41.858  1.00 68.51  ? 304 ASP A CB  1 
ATOM   1922 C CG  . ASP A 1 289 ? -20.672 54.442 42.971  1.00 73.63  ? 304 ASP A CG  1 
ATOM   1923 O OD1 . ASP A 1 289 ? -19.427 54.303 42.963  1.00 76.34  ? 304 ASP A OD1 1 
ATOM   1924 O OD2 . ASP A 1 289 ? -21.279 55.080 43.858  1.00 73.99  ? 304 ASP A OD2 1 
ATOM   1925 N N   . TYR A 1 290 ? -19.381 51.449 42.948  1.00 64.63  ? 305 TYR A N   1 
ATOM   1926 C CA  . TYR A 1 290 ? -19.057 50.546 44.047  1.00 61.92  ? 305 TYR A CA  1 
ATOM   1927 C C   . TYR A 1 290 ? -19.781 50.948 45.327  1.00 57.81  ? 305 TYR A C   1 
ATOM   1928 O O   . TYR A 1 290 ? -20.228 50.086 46.094  1.00 56.92  ? 305 TYR A O   1 
ATOM   1929 C CB  . TYR A 1 290 ? -17.545 50.513 44.275  1.00 55.88  ? 305 TYR A CB  1 
ATOM   1930 C CG  . TYR A 1 290 ? -17.135 49.605 45.411  1.00 62.80  ? 305 TYR A CG  1 
ATOM   1931 C CD1 . TYR A 1 290 ? -17.251 48.224 45.297  1.00 63.23  ? 305 TYR A CD1 1 
ATOM   1932 C CD2 . TYR A 1 290 ? -16.655 50.127 46.607  1.00 55.66  ? 305 TYR A CD2 1 
ATOM   1933 C CE1 . TYR A 1 290 ? -16.888 47.386 46.339  1.00 65.05  ? 305 TYR A CE1 1 
ATOM   1934 C CE2 . TYR A 1 290 ? -16.289 49.299 47.652  1.00 60.33  ? 305 TYR A CE2 1 
ATOM   1935 C CZ  . TYR A 1 290 ? -16.409 47.928 47.513  1.00 65.31  ? 305 TYR A CZ  1 
ATOM   1936 O OH  . TYR A 1 290 ? -16.048 47.094 48.550  1.00 67.58  ? 305 TYR A OH  1 
ATOM   1937 N N   . GLN A 1 291 ? -19.907 52.255 45.574  1.00 56.31  ? 306 GLN A N   1 
ATOM   1938 C CA  . GLN A 1 291 ? -20.547 52.719 46.801  1.00 53.75  ? 306 GLN A CA  1 
ATOM   1939 C C   . GLN A 1 291 ? -22.020 52.324 46.843  1.00 54.42  ? 306 GLN A C   1 
ATOM   1940 O O   . GLN A 1 291 ? -22.540 51.958 47.905  1.00 55.26  ? 306 GLN A O   1 
ATOM   1941 C CB  . GLN A 1 291 ? -20.389 54.232 46.936  1.00 49.53  ? 306 GLN A CB  1 
ATOM   1942 N N   . LYS A 1 292 ? -22.709 52.390 45.703  1.00 49.84  ? 307 LYS A N   1 
ATOM   1943 C CA  . LYS A 1 292 ? -24.086 51.914 45.662  1.00 54.48  ? 307 LYS A CA  1 
ATOM   1944 C C   . LYS A 1 292 ? -24.155 50.403 45.840  1.00 53.90  ? 307 LYS A C   1 
ATOM   1945 O O   . LYS A 1 292 ? -25.103 49.892 46.449  1.00 53.06  ? 307 LYS A O   1 
ATOM   1946 C CB  . LYS A 1 292 ? -24.751 52.329 44.350  1.00 58.73  ? 307 LYS A CB  1 
ATOM   1947 N N   . ILE A 1 293 ? -23.163 49.674 45.327  1.00 48.19  ? 308 ILE A N   1 
ATOM   1948 C CA  . ILE A 1 293 ? -23.119 48.234 45.557  1.00 46.89  ? 308 ILE A CA  1 
ATOM   1949 C C   . ILE A 1 293 ? -22.913 47.941 47.039  1.00 46.70  ? 308 ILE A C   1 
ATOM   1950 O O   . ILE A 1 293 ? -23.572 47.062 47.610  1.00 42.78  ? 308 ILE A O   1 
ATOM   1951 C CB  . ILE A 1 293 ? -22.029 47.583 44.686  1.00 49.56  ? 308 ILE A CB  1 
ATOM   1952 C CG1 . ILE A 1 293 ? -22.542 47.376 43.260  1.00 55.88  ? 308 ILE A CG1 1 
ATOM   1953 C CG2 . ILE A 1 293 ? -21.579 46.249 45.276  1.00 47.10  ? 308 ILE A CG2 1 
ATOM   1954 C CD1 . ILE A 1 293 ? -21.487 46.827 42.314  1.00 48.67  ? 308 ILE A CD1 1 
ATOM   1955 N N   . GLN A 1 294 ? -22.008 48.677 47.691  1.00 44.89  ? 309 GLN A N   1 
ATOM   1956 C CA  . GLN A 1 294 ? -21.784 48.463 49.118  1.00 48.67  ? 309 GLN A CA  1 
ATOM   1957 C C   . GLN A 1 294 ? -23.010 48.830 49.949  1.00 48.45  ? 309 GLN A C   1 
ATOM   1958 O O   . GLN A 1 294 ? -23.255 48.215 50.995  1.00 44.33  ? 309 GLN A O   1 
ATOM   1959 C CB  . GLN A 1 294 ? -20.567 49.257 49.594  1.00 43.73  ? 309 GLN A CB  1 
ATOM   1960 C CG  . GLN A 1 294 ? -19.346 48.396 49.921  1.00 55.93  ? 309 GLN A CG  1 
ATOM   1961 C CD  . GLN A 1 294 ? -19.439 47.693 51.283  1.00 64.13  ? 309 GLN A CD  1 
ATOM   1962 O OE1 . GLN A 1 294 ? -20.527 47.318 51.741  1.00 57.64  ? 309 GLN A OE1 1 
ATOM   1963 N NE2 . GLN A 1 294 ? -18.288 47.502 51.930  1.00 55.85  ? 309 GLN A NE2 1 
ATOM   1964 N N   . GLN A 1 295 ? -23.788 49.821 49.511  1.00 48.63  ? 310 GLN A N   1 
ATOM   1965 C CA  . GLN A 1 295 ? -24.996 50.165 50.251  1.00 48.34  ? 310 GLN A CA  1 
ATOM   1966 C C   . GLN A 1 295 ? -26.033 49.060 50.132  1.00 47.77  ? 310 GLN A C   1 
ATOM   1967 O O   . GLN A 1 295 ? -26.760 48.779 51.093  1.00 47.14  ? 310 GLN A O   1 
ATOM   1968 C CB  . GLN A 1 295 ? -25.567 51.495 49.757  1.00 53.27  ? 310 GLN A CB  1 
ATOM   1969 C CG  . GLN A 1 295 ? -25.176 52.695 50.611  1.00 58.89  ? 310 GLN A CG  1 
ATOM   1970 C CD  . GLN A 1 295 ? -25.143 52.377 52.098  1.00 61.79  ? 310 GLN A CD  1 
ATOM   1971 O OE1 . GLN A 1 295 ? -26.184 52.169 52.723  1.00 65.56  ? 310 GLN A OE1 1 
ATOM   1972 N NE2 . GLN A 1 295 ? -23.942 52.341 52.672  1.00 55.93  ? 310 GLN A NE2 1 
ATOM   1973 N N   . GLY A 1 296 ? -26.108 48.418 48.964  1.00 44.29  ? 311 GLY A N   1 
ATOM   1974 C CA  . GLY A 1 296 ? -27.027 47.305 48.799  1.00 41.15  ? 311 GLY A CA  1 
ATOM   1975 C C   . GLY A 1 296 ? -26.693 46.135 49.702  1.00 39.10  ? 311 GLY A C   1 
ATOM   1976 O O   . GLY A 1 296 ? -27.585 45.516 50.286  1.00 36.46  ? 311 GLY A O   1 
ATOM   1977 N N   . PHE A 1 297 ? -25.402 45.814 49.830  1.00 42.01  ? 312 PHE A N   1 
ATOM   1978 C CA  . PHE A 1 297 ? -24.998 44.758 50.753  1.00 39.66  ? 312 PHE A CA  1 
ATOM   1979 C C   . PHE A 1 297 ? -25.299 45.148 52.197  1.00 42.32  ? 312 PHE A C   1 
ATOM   1980 O O   . PHE A 1 297 ? -25.829 44.338 52.965  1.00 37.56  ? 312 PHE A O   1 
ATOM   1981 C CB  . PHE A 1 297 ? -23.513 44.441 50.574  1.00 38.53  ? 312 PHE A CB  1 
ATOM   1982 C CG  . PHE A 1 297 ? -23.219 43.503 49.426  1.00 45.60  ? 312 PHE A CG  1 
ATOM   1983 C CD1 . PHE A 1 297 ? -23.369 43.921 48.110  1.00 43.43  ? 312 PHE A CD1 1 
ATOM   1984 C CD2 . PHE A 1 297 ? -22.776 42.208 49.664  1.00 41.32  ? 312 PHE A CD2 1 
ATOM   1985 C CE1 . PHE A 1 297 ? -23.089 43.065 47.049  1.00 39.33  ? 312 PHE A CE1 1 
ATOM   1986 C CE2 . PHE A 1 297 ? -22.494 41.346 48.609  1.00 40.08  ? 312 PHE A CE2 1 
ATOM   1987 C CZ  . PHE A 1 297 ? -22.651 41.777 47.299  1.00 38.49  ? 312 PHE A CZ  1 
ATOM   1988 N N   . ARG A 1 298 ? -24.985 46.389 52.580  1.00 42.45  ? 313 ARG A N   1 
ATOM   1989 C CA  . ARG A 1 298 ? -25.287 46.845 53.933  1.00 43.49  ? 313 ARG A CA  1 
ATOM   1990 C C   . ARG A 1 298 ? -26.783 46.800 54.208  1.00 46.83  ? 313 ARG A C   1 
ATOM   1991 O O   . ARG A 1 298 ? -27.214 46.438 55.310  1.00 45.88  ? 313 ARG A O   1 
ATOM   1992 C CB  . ARG A 1 298 ? -24.746 48.258 54.147  1.00 46.67  ? 313 ARG A CB  1 
ATOM   1993 C CG  . ARG A 1 298 ? -23.263 48.268 54.464  1.00 53.31  ? 313 ARG A CG  1 
ATOM   1994 C CD  . ARG A 1 298 ? -22.803 49.587 55.068  1.00 56.82  ? 313 ARG A CD  1 
ATOM   1995 N NE  . ARG A 1 298 ? -21.348 49.727 55.101  1.00 65.43  ? 313 ARG A NE  1 
ATOM   1996 C CZ  . ARG A 1 298 ? -20.506 48.888 55.698  1.00 67.15  ? 313 ARG A CZ  1 
ATOM   1997 N NH1 . ARG A 1 298 ? -20.935 47.837 56.381  1.00 66.89  ? 313 ARG A NH1 1 
ATOM   1998 N NH2 . ARG A 1 298 ? -19.197 49.121 55.623  1.00 64.65  ? 313 ARG A NH2 1 
ATOM   1999 N N   . GLN A 1 299 ? -27.589 47.154 53.215  1.00 41.53  ? 314 GLN A N   1 
ATOM   2000 C CA  . GLN A 1 299 ? -29.036 47.147 53.355  1.00 44.05  ? 314 GLN A CA  1 
ATOM   2001 C C   . GLN A 1 299 ? -29.647 45.773 53.123  1.00 39.56  ? 314 GLN A C   1 
ATOM   2002 O O   . GLN A 1 299 ? -30.871 45.638 53.233  1.00 42.71  ? 314 GLN A O   1 
ATOM   2003 C CB  . GLN A 1 299 ? -29.649 48.159 52.384  1.00 41.90  ? 314 GLN A CB  1 
ATOM   2004 C CG  . GLN A 1 299 ? -29.476 49.606 52.828  1.00 49.35  ? 314 GLN A CG  1 
ATOM   2005 C CD  . GLN A 1 299 ? -29.919 50.597 51.771  1.00 60.96  ? 314 GLN A CD  1 
ATOM   2006 O OE1 . GLN A 1 299 ? -29.857 51.810 51.977  1.00 70.35  ? 314 GLN A OE1 1 
ATOM   2007 N NE2 . GLN A 1 299 ? -30.366 50.085 50.626  1.00 65.49  ? 314 GLN A NE2 1 
ATOM   2008 N N   . ASN A 1 300 ? -28.832 44.763 52.812  1.00 36.62  ? 315 ASN A N   1 
ATOM   2009 C CA  . ASN A 1 300 ? -29.315 43.426 52.475  1.00 39.54  ? 315 ASN A CA  1 
ATOM   2010 C C   . ASN A 1 300 ? -30.403 43.506 51.401  1.00 42.39  ? 315 ASN A C   1 
ATOM   2011 O O   . ASN A 1 300 ? -31.517 43.001 51.556  1.00 39.34  ? 315 ASN A O   1 
ATOM   2012 C CB  . ASN A 1 300 ? -29.808 42.687 53.725  1.00 35.37  ? 315 ASN A CB  1 
ATOM   2013 C CG  . ASN A 1 300 ? -30.118 41.221 53.453  1.00 40.96  ? 315 ASN A CG  1 
ATOM   2014 O OD1 . ASN A 1 300 ? -29.728 40.679 52.418  1.00 38.01  ? 315 ASN A OD1 1 
ATOM   2015 N ND2 . ASN A 1 300 ? -30.831 40.578 54.376  1.00 35.56  ? 315 ASN A ND2 1 
ATOM   2016 N N   . ASN A 1 301 ? -30.071 44.177 50.305  1.00 40.40  ? 316 ASN A N   1 
ATOM   2017 C CA  . ASN A 1 301 ? -31.000 44.364 49.200  1.00 40.75  ? 316 ASN A CA  1 
ATOM   2018 C C   . ASN A 1 301 ? -30.790 43.232 48.203  1.00 43.00  ? 316 ASN A C   1 
ATOM   2019 O O   . ASN A 1 301 ? -29.731 43.142 47.572  1.00 40.81  ? 316 ASN A O   1 
ATOM   2020 C CB  . ASN A 1 301 ? -30.790 45.728 48.548  1.00 43.53  ? 316 ASN A CB  1 
ATOM   2021 C CG  . ASN A 1 301 ? -31.764 45.987 47.415  1.00 47.20  ? 316 ASN A CG  1 
ATOM   2022 O OD1 . ASN A 1 301 ? -31.579 45.505 46.296  1.00 44.58  ? 316 ASN A OD1 1 
ATOM   2023 N ND2 . ASN A 1 301 ? -32.805 46.761 47.699  1.00 51.04  ? 316 ASN A ND2 1 
ATOM   2024 N N   . ARG A 1 302 ? -31.805 42.380 48.051  1.00 39.64  ? 317 ARG A N   1 
ATOM   2025 C CA  . ARG A 1 302 ? -31.654 41.175 47.240  1.00 41.66  ? 317 ARG A CA  1 
ATOM   2026 C C   . ARG A 1 302 ? -31.250 41.507 45.809  1.00 41.92  ? 317 ARG A C   1 
ATOM   2027 O O   . ARG A 1 302 ? -30.296 40.933 45.272  1.00 41.45  ? 317 ARG A O   1 
ATOM   2028 C CB  . ARG A 1 302 ? -32.951 40.367 47.257  1.00 35.65  ? 317 ARG A CB  1 
ATOM   2029 C CG  . ARG A 1 302 ? -32.732 38.898 46.977  1.00 35.64  ? 317 ARG A CG  1 
ATOM   2030 C CD  . ARG A 1 302 ? -33.978 38.224 46.442  1.00 36.97  ? 317 ARG A CD  1 
ATOM   2031 N NE  . ARG A 1 302 ? -34.424 38.802 45.182  1.00 38.97  ? 317 ARG A NE  1 
ATOM   2032 C CZ  . ARG A 1 302 ? -35.672 39.176 44.931  1.00 45.93  ? 317 ARG A CZ  1 
ATOM   2033 N NH1 . ARG A 1 302 ? -36.621 39.080 45.849  1.00 41.62  ? 317 ARG A NH1 1 
ATOM   2034 N NH2 . ARG A 1 302 ? -35.975 39.655 43.727  1.00 44.98  ? 317 ARG A NH2 1 
ATOM   2035 N N   . GLU A 1 303 ? -31.970 42.431 45.172  1.00 44.36  ? 318 GLU A N   1 
ATOM   2036 C CA  . GLU A 1 303 ? -31.683 42.755 43.779  1.00 43.27  ? 318 GLU A CA  1 
ATOM   2037 C C   . GLU A 1 303 ? -30.278 43.322 43.615  1.00 45.36  ? 318 GLU A C   1 
ATOM   2038 O O   . GLU A 1 303 ? -29.559 42.962 42.676  1.00 41.71  ? 318 GLU A O   1 
ATOM   2039 C CB  . GLU A 1 303 ? -32.720 43.742 43.252  1.00 42.97  ? 318 GLU A CB  1 
ATOM   2040 C CG  . GLU A 1 303 ? -34.101 43.148 43.069  1.00 53.38  ? 318 GLU A CG  1 
ATOM   2041 C CD  . GLU A 1 303 ? -34.954 43.965 42.120  1.00 53.95  ? 318 GLU A CD  1 
ATOM   2042 O OE1 . GLU A 1 303 ? -35.166 45.163 42.407  1.00 59.45  ? 318 GLU A OE1 1 
ATOM   2043 O OE2 . GLU A 1 303 ? -35.412 43.410 41.093  1.00 48.21  ? 318 GLU A OE2 1 
ATOM   2044 N N   . MET A 1 304 ? -29.873 44.219 44.511  1.00 43.07  ? 319 MET A N   1 
ATOM   2045 C CA  . MET A 1 304 ? -28.571 44.852 44.358  1.00 40.73  ? 319 MET A CA  1 
ATOM   2046 C C   . MET A 1 304 ? -27.441 43.859 44.607  1.00 39.89  ? 319 MET A C   1 
ATOM   2047 O O   . MET A 1 304 ? -26.425 43.878 43.902  1.00 38.15  ? 319 MET A O   1 
ATOM   2048 C CB  . MET A 1 304 ? -28.467 46.049 45.299  1.00 46.31  ? 319 MET A CB  1 
ATOM   2049 C CG  . MET A 1 304 ? -29.211 47.281 44.790  1.00 56.69  ? 319 MET A CG  1 
ATOM   2050 S SD  . MET A 1 304 ? -28.577 48.839 45.445  1.00 76.72  ? 319 MET A SD  1 
ATOM   2051 C CE  . MET A 1 304 ? -29.889 49.289 46.576  1.00 54.71  ? 319 MET A CE  1 
ATOM   2052 N N   . ILE A 1 305 ? -27.601 42.979 45.596  1.00 39.20  ? 320 ILE A N   1 
ATOM   2053 C CA  . ILE A 1 305 ? -26.559 41.997 45.882  1.00 42.34  ? 320 ILE A CA  1 
ATOM   2054 C C   . ILE A 1 305 ? -26.408 41.025 44.716  1.00 43.16  ? 320 ILE A C   1 
ATOM   2055 O O   . ILE A 1 305 ? -25.309 40.836 44.183  1.00 35.30  ? 320 ILE A O   1 
ATOM   2056 C CB  . ILE A 1 305 ? -26.859 41.254 47.195  1.00 36.97  ? 320 ILE A CB  1 
ATOM   2057 C CG1 . ILE A 1 305 ? -26.771 42.214 48.382  1.00 39.05  ? 320 ILE A CG1 1 
ATOM   2058 C CG2 . ILE A 1 305 ? -25.889 40.081 47.382  1.00 32.31  ? 320 ILE A CG2 1 
ATOM   2059 C CD1 . ILE A 1 305 ? -27.264 41.610 49.686  1.00 35.72  ? 320 ILE A CD1 1 
ATOM   2060 N N   . LYS A 1 306 ? -27.512 40.404 44.296  1.00 40.33  ? 321 LYS A N   1 
ATOM   2061 C CA  . LYS A 1 306 ? -27.432 39.349 43.291  1.00 46.12  ? 321 LYS A CA  1 
ATOM   2062 C C   . LYS A 1 306 ? -27.078 39.868 41.903  1.00 43.80  ? 321 LYS A C   1 
ATOM   2063 O O   . LYS A 1 306 ? -26.602 39.088 41.072  1.00 44.64  ? 321 LYS A O   1 
ATOM   2064 C CB  . LYS A 1 306 ? -28.748 38.577 43.227  1.00 37.01  ? 321 LYS A CB  1 
ATOM   2065 C CG  . LYS A 1 306 ? -29.125 37.917 44.525  1.00 37.58  ? 321 LYS A CG  1 
ATOM   2066 C CD  . LYS A 1 306 ? -30.202 36.868 44.317  1.00 38.35  ? 321 LYS A CD  1 
ATOM   2067 C CE  . LYS A 1 306 ? -29.906 35.627 45.141  1.00 35.17  ? 321 LYS A CE  1 
ATOM   2068 N NZ  . LYS A 1 306 ? -31.078 35.186 45.922  1.00 42.83  ? 321 LYS A NZ  1 
ATOM   2069 N N   . SER A 1 307 ? -27.296 41.148 41.625  1.00 115.07 ? 322 SER A N   1 
ATOM   2070 C CA  . SER A 1 307 ? -26.912 41.720 40.344  1.00 49.09  ? 322 SER A CA  1 
ATOM   2071 C C   . SER A 1 307 ? -25.562 42.422 40.398  1.00 44.75  ? 322 SER A C   1 
ATOM   2072 O O   . SER A 1 307 ? -25.110 42.949 39.374  1.00 37.97  ? 322 SER A O   1 
ATOM   2073 C CB  . SER A 1 307 ? -27.989 42.695 39.855  1.00 43.15  ? 322 SER A CB  1 
ATOM   2074 O OG  . SER A 1 307 ? -28.060 43.836 40.692  1.00 48.82  ? 322 SER A OG  1 
ATOM   2075 N N   . ALA A 1 308 ? -24.911 42.434 41.562  1.00 46.39  ? 323 ALA A N   1 
ATOM   2076 C CA  . ALA A 1 308 ? -23.657 43.159 41.727  1.00 43.37  ? 323 ALA A CA  1 
ATOM   2077 C C   . ALA A 1 308 ? -22.583 42.611 40.800  1.00 41.52  ? 323 ALA A C   1 
ATOM   2078 O O   . ALA A 1 308 ? -22.511 41.404 40.547  1.00 40.22  ? 323 ALA A O   1 
ATOM   2079 C CB  . ALA A 1 308 ? -23.180 43.075 43.178  1.00 40.68  ? 323 ALA A CB  1 
ATOM   2080 N N   . PHE A 1 309 ? -21.747 43.519 40.293  1.00 46.40  ? 324 PHE A N   1 
ATOM   2081 C CA  . PHE A 1 309 ? -20.579 43.189 39.476  1.00 47.92  ? 324 PHE A CA  1 
ATOM   2082 C C   . PHE A 1 309 ? -20.955 42.461 38.197  1.00 45.56  ? 324 PHE A C   1 
ATOM   2083 O O   . PHE A 1 309 ? -20.135 41.735 37.628  1.00 55.36  ? 324 PHE A O   1 
ATOM   2084 C CB  . PHE A 1 309 ? -19.562 42.375 40.283  1.00 38.51  ? 324 PHE A CB  1 
ATOM   2085 C CG  . PHE A 1 309 ? -19.296 42.944 41.635  1.00 39.84  ? 324 PHE A CG  1 
ATOM   2086 C CD1 . PHE A 1 309 ? -18.643 44.159 41.769  1.00 39.86  ? 324 PHE A CD1 1 
ATOM   2087 C CD2 . PHE A 1 309 ? -19.735 42.291 42.772  1.00 39.93  ? 324 PHE A CD2 1 
ATOM   2088 C CE1 . PHE A 1 309 ? -18.403 44.701 43.017  1.00 45.04  ? 324 PHE A CE1 1 
ATOM   2089 C CE2 . PHE A 1 309 ? -19.510 42.828 44.024  1.00 44.78  ? 324 PHE A CE2 1 
ATOM   2090 C CZ  . PHE A 1 309 ? -18.839 44.036 44.149  1.00 46.83  ? 324 PHE A CZ  1 
ATOM   2091 N N   . LEU A 1 310 ? -22.193 42.638 37.748  1.00 47.95  ? 325 LEU A N   1 
ATOM   2092 C CA  . LEU A 1 310 ? -22.643 42.126 36.461  1.00 55.10  ? 325 LEU A CA  1 
ATOM   2093 C C   . LEU A 1 310 ? -23.162 43.297 35.640  1.00 64.44  ? 325 LEU A C   1 
ATOM   2094 O O   . LEU A 1 310 ? -24.080 44.003 36.093  1.00 59.76  ? 325 LEU A O   1 
ATOM   2095 C CB  . LEU A 1 310 ? -23.731 41.068 36.633  1.00 52.39  ? 325 LEU A CB  1 
ATOM   2096 C CG  . LEU A 1 310 ? -23.263 39.719 37.184  1.00 52.39  ? 325 LEU A CG  1 
ATOM   2097 C CD1 . LEU A 1 310 ? -24.447 38.791 37.407  1.00 47.70  ? 325 LEU A CD1 1 
ATOM   2098 C CD2 . LEU A 1 310 ? -22.243 39.086 36.257  1.00 48.00  ? 325 LEU A CD2 1 
ATOM   2099 N N   . PRO A 1 311 ? -22.606 43.562 34.461  1.00 72.72  ? 326 PRO A N   1 
ATOM   2100 C CA  . PRO A 1 311 ? -23.158 44.630 33.618  1.00 69.05  ? 326 PRO A CA  1 
ATOM   2101 C C   . PRO A 1 311 ? -24.288 44.119 32.740  1.00 74.95  ? 326 PRO A C   1 
ATOM   2102 O O   . PRO A 1 311 ? -24.111 43.158 31.983  1.00 78.55  ? 326 PRO A O   1 
ATOM   2103 C CB  . PRO A 1 311 ? -21.947 45.085 32.794  1.00 67.45  ? 326 PRO A CB  1 
ATOM   2104 C CG  . PRO A 1 311 ? -21.067 43.862 32.706  1.00 69.27  ? 326 PRO A CG  1 
ATOM   2105 C CD  . PRO A 1 311 ? -21.415 42.935 33.859  1.00 66.04  ? 326 PRO A CD  1 
ATOM   2106 N N   . VAL A 1 312 ? -25.457 44.743 32.844  1.00 76.45  ? 327 VAL A N   1 
ATOM   2107 C CA  . VAL A 1 312 ? -26.614 44.321 32.066  1.00 75.97  ? 327 VAL A CA  1 
ATOM   2108 C C   . VAL A 1 312 ? -26.529 44.891 30.656  1.00 74.93  ? 327 VAL A C   1 
ATOM   2109 O O   . VAL A 1 312 ? -27.534 45.317 30.089  1.00 78.88  ? 327 VAL A O   1 
ATOM   2110 C CB  . VAL A 1 312 ? -27.929 44.739 32.749  1.00 74.46  ? 327 VAL A CB  1 
ATOM   2111 N N   . PHE A 1 320 ? -19.532 38.693 25.471  1.00 56.90  ? 335 PHE A N   1 
ATOM   2112 C CA  . PHE A 1 320 ? -20.808 37.994 25.470  1.00 56.57  ? 335 PHE A CA  1 
ATOM   2113 C C   . PHE A 1 320 ? -20.604 36.518 25.834  1.00 56.66  ? 335 PHE A C   1 
ATOM   2114 O O   . PHE A 1 320 ? -19.914 36.211 26.807  1.00 55.94  ? 335 PHE A O   1 
ATOM   2115 C CB  . PHE A 1 320 ? -21.499 38.146 24.111  1.00 61.28  ? 335 PHE A CB  1 
ATOM   2116 C CG  . PHE A 1 320 ? -23.000 38.072 24.179  1.00 59.42  ? 335 PHE A CG  1 
ATOM   2117 C CD1 . PHE A 1 320 ? -23.753 38.006 23.018  1.00 55.03  ? 335 PHE A CD1 1 
ATOM   2118 C CD2 . PHE A 1 320 ? -23.655 38.051 25.403  1.00 61.40  ? 335 PHE A CD2 1 
ATOM   2119 C CE1 . PHE A 1 320 ? -25.136 37.933 23.069  1.00 61.57  ? 335 PHE A CE1 1 
ATOM   2120 C CE2 . PHE A 1 320 ? -25.040 37.977 25.466  1.00 66.00  ? 335 PHE A CE2 1 
ATOM   2121 C CZ  . PHE A 1 320 ? -25.782 37.916 24.294  1.00 65.85  ? 335 PHE A CZ  1 
ATOM   2122 N N   . LYS A 1 321 ? -21.190 35.603 25.064  1.00 48.08  ? 336 LYS A N   1 
ATOM   2123 C CA  . LYS A 1 321 ? -21.257 34.193 25.436  1.00 50.02  ? 336 LYS A CA  1 
ATOM   2124 C C   . LYS A 1 321 ? -20.266 33.370 24.619  1.00 50.33  ? 336 LYS A C   1 
ATOM   2125 O O   . LYS A 1 321 ? -20.372 33.298 23.390  1.00 45.93  ? 336 LYS A O   1 
ATOM   2126 C CB  . LYS A 1 321 ? -22.678 33.659 25.261  1.00 45.63  ? 336 LYS A CB  1 
ATOM   2127 C CG  . LYS A 1 321 ? -23.652 34.235 26.273  1.00 47.85  ? 336 LYS A CG  1 
ATOM   2128 C CD  . LYS A 1 321 ? -25.071 33.761 26.023  1.00 52.35  ? 336 LYS A CD  1 
ATOM   2129 C CE  . LYS A 1 321 ? -26.024 34.373 27.034  1.00 49.52  ? 336 LYS A CE  1 
ATOM   2130 N NZ  . LYS A 1 321 ? -26.940 35.345 26.397  1.00 51.70  ? 336 LYS A NZ  1 
ATOM   2131 N N   . SER A 1 322 ? -19.322 32.728 25.314  1.00 48.82  ? 337 SER A N   1 
ATOM   2132 C CA  . SER A 1 322 ? -18.323 31.901 24.644  1.00 44.72  ? 337 SER A CA  1 
ATOM   2133 C C   . SER A 1 322 ? -18.925 30.617 24.093  1.00 44.15  ? 337 SER A C   1 
ATOM   2134 O O   . SER A 1 322 ? -18.414 30.070 23.109  1.00 45.14  ? 337 SER A O   1 
ATOM   2135 C CB  . SER A 1 322 ? -17.190 31.558 25.611  1.00 44.12  ? 337 SER A CB  1 
ATOM   2136 O OG  . SER A 1 322 ? -17.642 30.647 26.605  1.00 38.77  ? 337 SER A OG  1 
ATOM   2137 N N   . LYS A 1 323 ? -19.988 30.114 24.724  1.00 44.45  ? 338 LYS A N   1 
ATOM   2138 C CA  . LYS A 1 323 ? -20.611 28.836 24.368  1.00 44.97  ? 338 LYS A CA  1 
ATOM   2139 C C   . LYS A 1 323 ? -19.610 27.678 24.390  1.00 45.55  ? 338 LYS A C   1 
ATOM   2140 O O   . LYS A 1 323 ? -19.815 26.654 23.725  1.00 45.52  ? 338 LYS A O   1 
ATOM   2141 C CB  . LYS A 1 323 ? -21.311 28.920 23.008  1.00 44.68  ? 338 LYS A CB  1 
ATOM   2142 C CG  . LYS A 1 323 ? -22.633 29.666 23.053  1.00 44.86  ? 338 LYS A CG  1 
ATOM   2143 C CD  . LYS A 1 323 ? -22.787 30.587 21.858  1.00 52.23  ? 338 LYS A CD  1 
ATOM   2144 N N   . GLY A 1 324 ? -18.525 27.821 25.157  1.00 37.81  ? 339 GLY A N   1 
ATOM   2145 C CA  . GLY A 1 324 ? -17.529 26.783 25.295  1.00 37.37  ? 339 GLY A CA  1 
ATOM   2146 C C   . GLY A 1 324 ? -16.303 26.938 24.421  1.00 41.24  ? 339 GLY A C   1 
ATOM   2147 O O   . GLY A 1 324 ? -15.367 26.142 24.559  1.00 38.18  ? 339 GLY A O   1 
ATOM   2148 N N   . ARG A 1 325 ? -16.269 27.933 23.539  1.00 42.40  ? 340 ARG A N   1 
ATOM   2149 C CA  . ARG A 1 325 ? -15.139 28.111 22.638  1.00 44.46  ? 340 ARG A CA  1 
ATOM   2150 C C   . ARG A 1 325 ? -14.026 28.883 23.335  1.00 46.23  ? 340 ARG A C   1 
ATOM   2151 O O   . ARG A 1 325 ? -14.260 29.961 23.890  1.00 45.88  ? 340 ARG A O   1 
ATOM   2152 C CB  . ARG A 1 325 ? -15.577 28.845 21.370  1.00 47.51  ? 340 ARG A CB  1 
ATOM   2153 C CG  . ARG A 1 325 ? -16.723 28.172 20.632  1.00 50.98  ? 340 ARG A CG  1 
ATOM   2154 C CD  . ARG A 1 325 ? -17.180 28.970 19.413  1.00 57.54  ? 340 ARG A CD  1 
ATOM   2155 N NE  . ARG A 1 325 ? -17.742 30.267 19.778  1.00 63.45  ? 340 ARG A NE  1 
ATOM   2156 C CZ  . ARG A 1 325 ? -18.991 30.642 19.532  1.00 67.49  ? 340 ARG A CZ  1 
ATOM   2157 N NH1 . ARG A 1 325 ? -19.844 29.844 18.909  1.00 67.55  ? 340 ARG A NH1 1 
ATOM   2158 N NH2 . ARG A 1 325 ? -19.395 31.849 19.921  1.00 64.91  ? 340 ARG A NH2 1 
ATOM   2159 N N   . GLY A 1 326 ? -12.819 28.332 23.304  1.00 42.39  ? 341 GLY A N   1 
ATOM   2160 C CA  . GLY A 1 326 ? -11.681 29.006 23.893  1.00 41.71  ? 341 GLY A CA  1 
ATOM   2161 C C   . GLY A 1 326 ? -10.487 28.083 23.985  1.00 41.13  ? 341 GLY A C   1 
ATOM   2162 O O   . GLY A 1 326 ? -10.504 26.946 23.502  1.00 40.69  ? 341 GLY A O   1 
ATOM   2163 N N   . PHE A 1 327 ? -9.437  28.601 24.622  1.00 41.44  ? 342 PHE A N   1 
ATOM   2164 C CA  . PHE A 1 327 ? -8.218  27.833 24.865  1.00 39.13  ? 342 PHE A CA  1 
ATOM   2165 C C   . PHE A 1 327 ? -8.473  26.910 26.052  1.00 40.50  ? 342 PHE A C   1 
ATOM   2166 O O   . PHE A 1 327 ? -8.038  27.149 27.181  1.00 40.07  ? 342 PHE A O   1 
ATOM   2167 C CB  . PHE A 1 327 ? -7.035  28.762 25.104  1.00 40.19  ? 342 PHE A CB  1 
ATOM   2168 C CG  . PHE A 1 327 ? -6.480  29.357 23.845  1.00 46.36  ? 342 PHE A CG  1 
ATOM   2169 C CD1 . PHE A 1 327 ? -7.070  30.476 23.274  1.00 43.71  ? 342 PHE A CD1 1 
ATOM   2170 C CD2 . PHE A 1 327 ? -5.385  28.785 23.217  1.00 46.11  ? 342 PHE A CD2 1 
ATOM   2171 C CE1 . PHE A 1 327 ? -6.573  31.020 22.112  1.00 39.40  ? 342 PHE A CE1 1 
ATOM   2172 C CE2 . PHE A 1 327 ? -4.882  29.323 22.055  1.00 44.58  ? 342 PHE A CE2 1 
ATOM   2173 C CZ  . PHE A 1 327 ? -5.476  30.444 21.500  1.00 46.69  ? 342 PHE A CZ  1 
ATOM   2174 N N   . ASN A 1 328 ? -9.197  25.824 25.778  1.00 37.18  ? 343 ASN A N   1 
ATOM   2175 C CA  . ASN A 1 328 ? -9.693  24.943 26.825  1.00 36.78  ? 343 ASN A CA  1 
ATOM   2176 C C   . ASN A 1 328 ? -8.781  23.757 27.114  1.00 40.32  ? 343 ASN A C   1 
ATOM   2177 O O   . ASN A 1 328 ? -8.931  23.125 28.167  1.00 37.15  ? 343 ASN A O   1 
ATOM   2178 C CB  . ASN A 1 328 ? -11.083 24.419 26.453  1.00 37.11  ? 343 ASN A CB  1 
ATOM   2179 C CG  . ASN A 1 328 ? -12.085 25.533 26.207  1.00 41.56  ? 343 ASN A CG  1 
ATOM   2180 O OD1 . ASN A 1 328 ? -12.154 26.502 26.966  1.00 41.43  ? 343 ASN A OD1 1 
ATOM   2181 N ND2 . ASN A 1 328 ? -12.877 25.393 25.149  1.00 35.71  ? 343 ASN A ND2 1 
ATOM   2182 N N   . TRP A 1 329 ? -7.853  23.432 26.217  1.00 36.94  ? 344 TRP A N   1 
ATOM   2183 C CA  . TRP A 1 329 ? -7.068  22.211 26.317  1.00 36.99  ? 344 TRP A CA  1 
ATOM   2184 C C   . TRP A 1 329 ? -5.580  22.534 26.381  1.00 44.51  ? 344 TRP A C   1 
ATOM   2185 O O   . TRP A 1 329 ? -5.134  23.581 25.899  1.00 44.37  ? 344 TRP A O   1 
ATOM   2186 C CB  . TRP A 1 329 ? -7.336  21.279 25.128  1.00 36.34  ? 344 TRP A CB  1 
ATOM   2187 C CG  . TRP A 1 329 ? -8.789  21.030 24.822  1.00 35.75  ? 344 TRP A CG  1 
ATOM   2188 C CD1 . TRP A 1 329 ? -9.535  19.958 25.217  1.00 36.26  ? 344 TRP A CD1 1 
ATOM   2189 C CD2 . TRP A 1 329 ? -9.663  21.860 24.041  1.00 41.97  ? 344 TRP A CD2 1 
ATOM   2190 N NE1 . TRP A 1 329 ? -10.822 20.072 24.741  1.00 35.31  ? 344 TRP A NE1 1 
ATOM   2191 C CE2 . TRP A 1 329 ? -10.927 21.231 24.018  1.00 39.16  ? 344 TRP A CE2 1 
ATOM   2192 C CE3 . TRP A 1 329 ? -9.502  23.079 23.370  1.00 38.82  ? 344 TRP A CE3 1 
ATOM   2193 C CZ2 . TRP A 1 329 ? -12.024 21.775 23.344  1.00 34.50  ? 344 TRP A CZ2 1 
ATOM   2194 C CZ3 . TRP A 1 329 ? -10.596 23.618 22.699  1.00 38.92  ? 344 TRP A CZ3 1 
ATOM   2195 C CH2 . TRP A 1 329 ? -11.839 22.964 22.692  1.00 36.50  ? 344 TRP A CH2 1 
ATOM   2196 N N   . ALA A 1 330 ? -4.810  21.619 26.972  1.00 38.41  ? 345 ALA A N   1 
ATOM   2197 C CA  . ALA A 1 330 ? -3.367  21.790 27.062  1.00 36.15  ? 345 ALA A CA  1 
ATOM   2198 C C   . ALA A 1 330 ? -2.681  20.434 27.137  1.00 39.03  ? 345 ALA A C   1 
ATOM   2199 O O   . ALA A 1 330 ? -3.190  19.505 27.771  1.00 36.85  ? 345 ALA A O   1 
ATOM   2200 C CB  . ALA A 1 330 ? -2.964  22.631 28.279  1.00 35.97  ? 345 ALA A CB  1 
ATOM   2201 N N   . ASN A 1 331 ? -1.525  20.338 26.486  1.00 38.23  ? 346 ASN A N   1 
ATOM   2202 C CA  . ASN A 1 331 ? -0.629  19.197 26.606  1.00 36.85  ? 346 ASN A CA  1 
ATOM   2203 C C   . ASN A 1 331 ? 0.558   19.608 27.466  1.00 38.69  ? 346 ASN A C   1 
ATOM   2204 O O   . ASN A 1 331 ? 1.219   20.611 27.176  1.00 39.50  ? 346 ASN A O   1 
ATOM   2205 C CB  . ASN A 1 331 ? -0.141  18.731 25.232  1.00 36.32  ? 346 ASN A CB  1 
ATOM   2206 C CG  . ASN A 1 331 ? -1.229  18.066 24.419  1.00 40.27  ? 346 ASN A CG  1 
ATOM   2207 O OD1 . ASN A 1 331 ? -2.138  17.442 24.968  1.00 42.58  ? 346 ASN A OD1 1 
ATOM   2208 N ND2 . ASN A 1 331 ? -1.144  18.193 23.099  1.00 38.17  ? 346 ASN A ND2 1 
ATOM   2209 N N   . PHE A 1 332 ? 0.826   18.844 28.522  1.00 39.28  ? 347 PHE A N   1 
ATOM   2210 C CA  . PHE A 1 332 ? 1.905   19.161 29.448  1.00 41.48  ? 347 PHE A CA  1 
ATOM   2211 C C   . PHE A 1 332 ? 3.082   18.222 29.219  1.00 38.09  ? 347 PHE A C   1 
ATOM   2212 O O   . PHE A 1 332 ? 2.967   17.013 29.443  1.00 39.02  ? 347 PHE A O   1 
ATOM   2213 C CB  . PHE A 1 332 ? 1.440   19.067 30.900  1.00 37.25  ? 347 PHE A CB  1 
ATOM   2214 C CG  . PHE A 1 332 ? 2.537   19.314 31.887  1.00 38.40  ? 347 PHE A CG  1 
ATOM   2215 C CD1 . PHE A 1 332 ? 3.203   20.528 31.908  1.00 39.36  ? 347 PHE A CD1 1 
ATOM   2216 C CD2 . PHE A 1 332 ? 2.928   18.325 32.771  1.00 38.79  ? 347 PHE A CD2 1 
ATOM   2217 C CE1 . PHE A 1 332 ? 4.226   20.757 32.813  1.00 43.44  ? 347 PHE A CE1 1 
ATOM   2218 C CE2 . PHE A 1 332 ? 3.951   18.548 33.677  1.00 39.22  ? 347 PHE A CE2 1 
ATOM   2219 C CZ  . PHE A 1 332 ? 4.601   19.763 33.696  1.00 38.34  ? 347 PHE A CZ  1 
ATOM   2220 N N   . ASP A 1 333 ? 4.210   18.781 28.784  1.00 39.19  ? 348 ASP A N   1 
ATOM   2221 C CA  . ASP A 1 333 ? 5.464   18.034 28.725  1.00 42.65  ? 348 ASP A CA  1 
ATOM   2222 C C   . ASP A 1 333 ? 6.056   17.977 30.131  1.00 44.32  ? 348 ASP A C   1 
ATOM   2223 O O   . ASP A 1 333 ? 6.482   18.999 30.676  1.00 43.07  ? 348 ASP A O   1 
ATOM   2224 C CB  . ASP A 1 333 ? 6.433   18.683 27.741  1.00 46.11  ? 348 ASP A CB  1 
ATOM   2225 C CG  . ASP A 1 333 ? 7.625   17.792 27.415  1.00 49.12  ? 348 ASP A CG  1 
ATOM   2226 O OD1 . ASP A 1 333 ? 8.186   17.162 28.341  1.00 48.25  ? 348 ASP A OD1 1 
ATOM   2227 O OD2 . ASP A 1 333 ? 8.007   17.728 26.226  1.00 47.57  ? 348 ASP A OD2 1 
ATOM   2228 N N   . SER A 1 334 ? 6.087   16.783 30.720  1.00 43.80  ? 349 SER A N   1 
ATOM   2229 C CA  . SER A 1 334 ? 6.578   16.638 32.082  1.00 47.49  ? 349 SER A CA  1 
ATOM   2230 C C   . SER A 1 334 ? 8.101   16.654 32.164  1.00 50.43  ? 349 SER A C   1 
ATOM   2231 O O   . SER A 1 334 ? 8.646   16.871 33.251  1.00 44.87  ? 349 SER A O   1 
ATOM   2232 C CB  . SER A 1 334 ? 6.024   15.352 32.700  1.00 41.62  ? 349 SER A CB  1 
ATOM   2233 O OG  . SER A 1 334 ? 6.629   14.211 32.120  1.00 56.46  ? 349 SER A OG  1 
ATOM   2234 N N   . VAL A 1 335 ? 8.792   16.444 31.047  1.00 51.87  ? 350 VAL A N   1 
ATOM   2235 C CA  . VAL A 1 335 ? 10.251  16.497 31.022  1.00 49.01  ? 350 VAL A CA  1 
ATOM   2236 C C   . VAL A 1 335 ? 10.746  17.911 30.766  1.00 52.30  ? 350 VAL A C   1 
ATOM   2237 O O   . VAL A 1 335 ? 11.538  18.454 31.542  1.00 54.45  ? 350 VAL A O   1 
ATOM   2238 C CB  . VAL A 1 335 ? 10.808  15.507 29.979  1.00 49.10  ? 350 VAL A CB  1 
ATOM   2239 C CG1 . VAL A 1 335 ? 12.304  15.732 29.786  1.00 44.70  ? 350 VAL A CG1 1 
ATOM   2240 C CG2 . VAL A 1 335 ? 10.530  14.072 30.406  1.00 47.93  ? 350 VAL A CG2 1 
ATOM   2241 N N   . LYS A 1 336 ? 10.277  18.533 29.688  1.00 49.50  ? 351 LYS A N   1 
ATOM   2242 C CA  . LYS A 1 336 ? 10.716  19.872 29.326  1.00 50.39  ? 351 LYS A CA  1 
ATOM   2243 C C   . LYS A 1 336 ? 9.993   20.963 30.103  1.00 49.04  ? 351 LYS A C   1 
ATOM   2244 O O   . LYS A 1 336 ? 10.341  22.140 29.953  1.00 48.51  ? 351 LYS A O   1 
ATOM   2245 C CB  . LYS A 1 336 ? 10.545  20.088 27.817  1.00 51.94  ? 351 LYS A CB  1 
ATOM   2246 C CG  . LYS A 1 336 ? 11.435  19.179 26.975  1.00 52.18  ? 351 LYS A CG  1 
ATOM   2247 C CD  . LYS A 1 336 ? 10.831  18.864 25.614  1.00 58.24  ? 351 LYS A CD  1 
ATOM   2248 C CE  . LYS A 1 336 ? 11.193  17.449 25.146  1.00 61.72  ? 351 LYS A CE  1 
ATOM   2249 N NZ  . LYS A 1 336 ? 10.087  16.460 25.385  1.00 53.61  ? 351 LYS A NZ  1 
ATOM   2250 N N   . LYS A 1 337 ? 9.018   20.600 30.937  1.00 54.37  ? 352 LYS A N   1 
ATOM   2251 C CA  . LYS A 1 337 ? 8.264   21.552 31.759  1.00 51.16  ? 352 LYS A CA  1 
ATOM   2252 C C   . LYS A 1 337 ? 7.598   22.620 30.890  1.00 49.00  ? 352 LYS A C   1 
ATOM   2253 O O   . LYS A 1 337 ? 7.730   23.823 31.125  1.00 43.86  ? 352 LYS A O   1 
ATOM   2254 C CB  . LYS A 1 337 ? 9.154   22.186 32.833  1.00 48.75  ? 352 LYS A CB  1 
ATOM   2255 C CG  . LYS A 1 337 ? 9.978   21.194 33.649  1.00 50.04  ? 352 LYS A CG  1 
ATOM   2256 C CD  . LYS A 1 337 ? 9.172   19.974 34.067  1.00 51.15  ? 352 LYS A CD  1 
ATOM   2257 C CE  . LYS A 1 337 ? 9.863   19.227 35.194  1.00 50.81  ? 352 LYS A CE  1 
ATOM   2258 N NZ  . LYS A 1 337 ? 9.219   17.915 35.482  1.00 51.66  ? 352 LYS A NZ  1 
ATOM   2259 N N   . LYS A 1 338 ? 6.871   22.163 29.874  1.00 50.02  ? 353 LYS A N   1 
ATOM   2260 C CA  . LYS A 1 338 ? 6.173   23.040 28.949  1.00 45.96  ? 353 LYS A CA  1 
ATOM   2261 C C   . LYS A 1 338 ? 4.690   22.701 28.931  1.00 44.61  ? 353 LYS A C   1 
ATOM   2262 O O   . LYS A 1 338 ? 4.297   21.536 29.043  1.00 45.64  ? 353 LYS A O   1 
ATOM   2263 C CB  . LYS A 1 338 ? 6.742   22.932 27.526  1.00 49.23  ? 353 LYS A CB  1 
ATOM   2264 C CG  . LYS A 1 338 ? 8.203   23.327 27.402  1.00 52.45  ? 353 LYS A CG  1 
ATOM   2265 C CD  . LYS A 1 338 ? 8.486   24.639 28.108  1.00 55.07  ? 353 LYS A CD  1 
ATOM   2266 C CE  . LYS A 1 338 ? 9.975   24.961 28.100  1.00 50.46  ? 353 LYS A CE  1 
ATOM   2267 N NZ  . LYS A 1 338 ? 10.218  26.335 27.578  1.00 59.83  ? 353 LYS A NZ  1 
ATOM   2268 N N   . CYS A 1 339 ? 3.875   23.741 28.778  1.00 45.23  ? 354 CYS A N   1 
ATOM   2269 C CA  . CYS A 1 339 ? 2.422   23.638 28.740  1.00 41.75  ? 354 CYS A CA  1 
ATOM   2270 C C   . CYS A 1 339 ? 1.967   24.191 27.394  1.00 46.73  ? 354 CYS A C   1 
ATOM   2271 O O   . CYS A 1 339 ? 2.125   25.388 27.128  1.00 46.96  ? 354 CYS A O   1 
ATOM   2272 C CB  . CYS A 1 339 ? 1.804   24.405 29.913  1.00 46.50  ? 354 CYS A CB  1 
ATOM   2273 S SG  . CYS A 1 339 ? 0.015   24.232 30.159  1.00 49.29  ? 354 CYS A SG  1 
ATOM   2274 N N   . TYR A 1 340 ? 1.426   23.322 26.539  1.00 39.28  ? 355 TYR A N   1 
ATOM   2275 C CA  . TYR A 1 340 ? 1.019   23.695 25.185  1.00 39.16  ? 355 TYR A CA  1 
ATOM   2276 C C   . TYR A 1 340 ? -0.502  23.810 25.141  1.00 41.49  ? 355 TYR A C   1 
ATOM   2277 O O   . TYR A 1 340 ? -1.208  22.801 25.070  1.00 40.46  ? 355 TYR A O   1 
ATOM   2278 C CB  . TYR A 1 340 ? 1.515   22.674 24.166  1.00 40.68  ? 355 TYR A CB  1 
ATOM   2279 C CG  . TYR A 1 340 ? 3.007   22.432 24.179  1.00 47.90  ? 355 TYR A CG  1 
ATOM   2280 C CD1 . TYR A 1 340 ? 3.873   23.259 23.473  1.00 47.06  ? 355 TYR A CD1 1 
ATOM   2281 C CD2 . TYR A 1 340 ? 3.549   21.361 24.878  1.00 46.49  ? 355 TYR A CD2 1 
ATOM   2282 C CE1 . TYR A 1 340 ? 5.235   23.031 23.471  1.00 47.47  ? 355 TYR A CE1 1 
ATOM   2283 C CE2 . TYR A 1 340 ? 4.913   21.125 24.885  1.00 46.76  ? 355 TYR A CE2 1 
ATOM   2284 C CZ  . TYR A 1 340 ? 5.751   21.961 24.179  1.00 51.21  ? 355 TYR A CZ  1 
ATOM   2285 O OH  . TYR A 1 340 ? 7.111   21.728 24.182  1.00 46.81  ? 355 TYR A OH  1 
ATOM   2286 N N   . ILE A 1 341 ? -1.007  25.039 25.154  1.00 42.76  ? 356 ILE A N   1 
ATOM   2287 C CA  . ILE A 1 341 ? -2.444  25.289 25.151  1.00 46.85  ? 356 ILE A CA  1 
ATOM   2288 C C   . ILE A 1 341 ? -2.908  25.553 23.723  1.00 43.44  ? 356 ILE A C   1 
ATOM   2289 O O   . ILE A 1 341 ? -2.150  26.037 22.876  1.00 46.81  ? 356 ILE A O   1 
ATOM   2290 C CB  . ILE A 1 341 ? -2.813  26.457 26.093  1.00 42.63  ? 356 ILE A CB  1 
ATOM   2291 C CG1 . ILE A 1 341 ? -2.442  27.804 25.473  1.00 46.91  ? 356 ILE A CG1 1 
ATOM   2292 C CG2 . ILE A 1 341 ? -2.118  26.300 27.436  1.00 41.94  ? 356 ILE A CG2 1 
ATOM   2293 C CD1 . ILE A 1 341 ? -2.851  28.995 26.322  1.00 46.20  ? 356 ILE A CD1 1 
ATOM   2294 N N   . PHE A 1 342 ? -4.166  25.214 23.449  1.00 42.39  ? 357 PHE A N   1 
ATOM   2295 C CA  . PHE A 1 342 ? -4.742  25.402 22.125  1.00 45.86  ? 357 PHE A CA  1 
ATOM   2296 C C   . PHE A 1 342 ? -6.252  25.541 22.253  1.00 44.12  ? 357 PHE A C   1 
ATOM   2297 O O   . PHE A 1 342 ? -6.850  25.150 23.260  1.00 42.57  ? 357 PHE A O   1 
ATOM   2298 C CB  . PHE A 1 342 ? -4.388  24.253 21.164  1.00 39.57  ? 357 PHE A CB  1 
ATOM   2299 C CG  . PHE A 1 342 ? -4.657  22.882 21.717  1.00 42.48  ? 357 PHE A CG  1 
ATOM   2300 C CD1 . PHE A 1 342 ? -3.767  22.284 22.601  1.00 39.64  ? 357 PHE A CD1 1 
ATOM   2301 C CD2 . PHE A 1 342 ? -5.799  22.184 21.343  1.00 40.22  ? 357 PHE A CD2 1 
ATOM   2302 C CE1 . PHE A 1 342 ? -4.014  21.016 23.111  1.00 40.29  ? 357 PHE A CE1 1 
ATOM   2303 C CE2 . PHE A 1 342 ? -6.055  20.916 21.846  1.00 42.61  ? 357 PHE A CE2 1 
ATOM   2304 C CZ  . PHE A 1 342 ? -5.159  20.328 22.732  1.00 39.26  ? 357 PHE A CZ  1 
ATOM   2305 N N   . ASN A 1 343 ? -6.862  26.116 21.217  1.00 42.67  ? 358 ASN A N   1 
ATOM   2306 C CA  . ASN A 1 343 ? -8.291  26.401 21.203  1.00 42.55  ? 358 ASN A CA  1 
ATOM   2307 C C   . ASN A 1 343 ? -9.050  25.527 20.215  1.00 45.52  ? 358 ASN A C   1 
ATOM   2308 O O   . ASN A 1 343 ? -10.224 25.796 19.937  1.00 52.02  ? 358 ASN A O   1 
ATOM   2309 C CB  . ASN A 1 343 ? -8.533  27.878 20.882  1.00 45.69  ? 358 ASN A CB  1 
ATOM   2310 C CG  . ASN A 1 343 ? -8.067  28.256 19.488  1.00 51.03  ? 358 ASN A CG  1 
ATOM   2311 O OD1 . ASN A 1 343 ? -7.214  27.587 18.898  1.00 50.40  ? 358 ASN A OD1 1 
ATOM   2312 N ND2 . ASN A 1 343 ? -8.620  29.338 18.957  1.00 45.72  ? 358 ASN A ND2 1 
ATOM   2313 N N   . THR A 1 344 ? -8.415  24.493 19.681  1.00 44.28  ? 359 THR A N   1 
ATOM   2314 C CA  . THR A 1 344 ? -9.060  23.574 18.756  1.00 48.80  ? 359 THR A CA  1 
ATOM   2315 C C   . THR A 1 344 ? -9.465  22.316 19.512  1.00 45.32  ? 359 THR A C   1 
ATOM   2316 O O   . THR A 1 344 ? -8.671  21.773 20.288  1.00 43.48  ? 359 THR A O   1 
ATOM   2317 C CB  . THR A 1 344 ? -8.121  23.225 17.598  1.00 51.49  ? 359 THR A CB  1 
ATOM   2318 O OG1 . THR A 1 344 ? -7.942  24.380 16.769  1.00 55.46  ? 359 THR A OG1 1 
ATOM   2319 C CG2 . THR A 1 344 ? -8.693  22.080 16.752  1.00 48.34  ? 359 THR A CG2 1 
ATOM   2320 N N   . LYS A 1 345 ? -10.696 21.869 19.298  1.00 42.20  ? 360 LYS A N   1 
ATOM   2321 C CA  . LYS A 1 345 ? -11.144 20.611 19.870  1.00 42.14  ? 360 LYS A CA  1 
ATOM   2322 C C   . LYS A 1 345 ? -10.192 19.486 19.463  1.00 42.95  ? 360 LYS A C   1 
ATOM   2323 O O   . LYS A 1 345 ? -9.864  19.358 18.276  1.00 44.65  ? 360 LYS A O   1 
ATOM   2324 C CB  . LYS A 1 345 ? -12.562 20.286 19.399  1.00 38.86  ? 360 LYS A CB  1 
ATOM   2325 C CG  . LYS A 1 345 ? -13.101 18.967 19.922  1.00 45.37  ? 360 LYS A CG  1 
ATOM   2326 C CD  . LYS A 1 345 ? -13.814 18.167 18.842  1.00 41.11  ? 360 LYS A CD  1 
ATOM   2327 C CE  . LYS A 1 345 ? -14.772 19.020 18.037  1.00 48.20  ? 360 LYS A CE  1 
ATOM   2328 N NZ  . LYS A 1 345 ? -15.294 18.276 16.853  1.00 52.38  ? 360 LYS A NZ  1 
ATOM   2329 N N   . PRO A 1 346 ? -9.717  18.673 20.401  1.00 44.17  ? 361 PRO A N   1 
ATOM   2330 C CA  . PRO A 1 346 ? -8.931  17.498 20.023  1.00 37.76  ? 361 PRO A CA  1 
ATOM   2331 C C   . PRO A 1 346 ? -9.854  16.342 19.686  1.00 42.78  ? 361 PRO A C   1 
ATOM   2332 O O   . PRO A 1 346 ? -10.983 16.256 20.175  1.00 40.66  ? 361 PRO A O   1 
ATOM   2333 C CB  . PRO A 1 346 ? -8.112  17.208 21.284  1.00 40.04  ? 361 PRO A CB  1 
ATOM   2334 C CG  . PRO A 1 346 ? -9.036  17.638 22.406  1.00 38.58  ? 361 PRO A CG  1 
ATOM   2335 C CD  . PRO A 1 346 ? -9.857  18.800 21.863  1.00 38.79  ? 361 PRO A CD  1 
ATOM   2336 N N   . THR A 1 347 ? -9.363  15.450 18.825  1.00 39.11  ? 362 THR A N   1 
ATOM   2337 C CA  . THR A 1 347 ? -10.164 14.321 18.370  1.00 40.63  ? 362 THR A CA  1 
ATOM   2338 C C   . THR A 1 347 ? -9.491  12.975 18.611  1.00 40.60  ? 362 THR A C   1 
ATOM   2339 O O   . THR A 1 347 ? -10.041 11.941 18.206  1.00 40.00  ? 362 THR A O   1 
ATOM   2340 C CB  . THR A 1 347 ? -10.518 14.477 16.882  1.00 43.70  ? 362 THR A CB  1 
ATOM   2341 O OG1 . THR A 1 347 ? -9.326  14.611 16.099  1.00 38.98  ? 362 THR A OG1 1 
ATOM   2342 C CG2 . THR A 1 347 ? -11.408 15.703 16.672  1.00 37.58  ? 362 THR A CG2 1 
ATOM   2343 N N   . CYS A 1 348 ? -8.337  12.950 19.276  1.00 41.87  ? 363 CYS A N   1 
ATOM   2344 C CA  . CYS A 1 348 ? -7.661  11.697 19.603  1.00 41.46  ? 363 CYS A CA  1 
ATOM   2345 C C   . CYS A 1 348 ? -6.529  11.991 20.578  1.00 41.41  ? 363 CYS A C   1 
ATOM   2346 O O   . CYS A 1 348 ? -6.212  13.149 20.865  1.00 40.50  ? 363 CYS A O   1 
ATOM   2347 C CB  . CYS A 1 348 ? -7.116  11.002 18.351  1.00 41.47  ? 363 CYS A CB  1 
ATOM   2348 S SG  . CYS A 1 348 ? -5.971  12.017 17.386  1.00 44.44  ? 363 CYS A SG  1 
ATOM   2349 N N   . LEU A 1 349 ? -5.903  10.918 21.060  1.00 41.14  ? 364 LEU A N   1 
ATOM   2350 C CA  . LEU A 1 349 ? -4.754  10.991 21.950  1.00 36.41  ? 364 LEU A CA  1 
ATOM   2351 C C   . LEU A 1 349 ? -3.539  10.363 21.282  1.00 40.40  ? 364 LEU A C   1 
ATOM   2352 O O   . LEU A 1 349 ? -3.648  9.313  20.642  1.00 37.34  ? 364 LEU A O   1 
ATOM   2353 C CB  . LEU A 1 349 ? -5.017  10.261 23.269  1.00 37.57  ? 364 LEU A CB  1 
ATOM   2354 C CG  . LEU A 1 349 ? -6.179  10.664 24.174  1.00 37.14  ? 364 LEU A CG  1 
ATOM   2355 C CD1 . LEU A 1 349 ? -6.226  9.721  25.364  1.00 38.27  ? 364 LEU A CD1 1 
ATOM   2356 C CD2 . LEU A 1 349 ? -6.044  12.104 24.638  1.00 35.40  ? 364 LEU A CD2 1 
ATOM   2357 N N   . ILE A 1 350 ? -2.381  11.008 21.438  1.00 42.24  ? 365 ILE A N   1 
ATOM   2358 C CA  . ILE A 1 350 ? -1.096  10.403 21.108  1.00 41.21  ? 365 ILE A CA  1 
ATOM   2359 C C   . ILE A 1 350 ? -0.520  9.781  22.371  1.00 44.20  ? 365 ILE A C   1 
ATOM   2360 O O   . ILE A 1 350 ? -0.556  10.388 23.449  1.00 43.54  ? 365 ILE A O   1 
ATOM   2361 C CB  . ILE A 1 350 ? -0.125  11.439 20.512  1.00 45.60  ? 365 ILE A CB  1 
ATOM   2362 C CG1 . ILE A 1 350 ? -0.713  12.089 19.259  1.00 41.13  ? 365 ILE A CG1 1 
ATOM   2363 C CG2 . ILE A 1 350 ? 1.213   10.798 20.190  1.00 40.03  ? 365 ILE A CG2 1 
ATOM   2364 C CD1 . ILE A 1 350 ? -0.206  13.505 19.031  1.00 35.40  ? 365 ILE A CD1 1 
ATOM   2365 N N   . ASN A 1 351 ? 0.014   8.565  22.240  1.00 42.97  ? 366 ASN A N   1 
ATOM   2366 C CA  . ASN A 1 351 ? 0.639   7.854  23.351  1.00 34.22  ? 366 ASN A CA  1 
ATOM   2367 C C   . ASN A 1 351 ? 2.076   8.346  23.513  1.00 39.16  ? 366 ASN A C   1 
ATOM   2368 O O   . ASN A 1 351 ? 2.939   8.043  22.685  1.00 42.85  ? 366 ASN A O   1 
ATOM   2369 C CB  . ASN A 1 351 ? 0.582   6.352  23.094  1.00 38.75  ? 366 ASN A CB  1 
ATOM   2370 C CG  . ASN A 1 351 ? 1.020   5.527  24.292  1.00 44.50  ? 366 ASN A CG  1 
ATOM   2371 O OD1 . ASN A 1 351 ? 1.376   4.357  24.148  1.00 41.12  ? 366 ASN A OD1 1 
ATOM   2372 N ND2 . ASN A 1 351 ? 0.987   6.127  25.480  1.00 44.98  ? 366 ASN A ND2 1 
ATOM   2373 N N   . ASP A 1 352 ? 2.340   9.109  24.576  1.00 39.05  ? 367 ASP A N   1 
ATOM   2374 C CA  . ASP A 1 352 ? 3.670   9.666  24.823  1.00 41.72  ? 367 ASP A CA  1 
ATOM   2375 C C   . ASP A 1 352 ? 3.956   9.677  26.319  1.00 44.42  ? 367 ASP A C   1 
ATOM   2376 O O   . ASP A 1 352 ? 3.284   10.384 27.077  1.00 38.89  ? 367 ASP A O   1 
ATOM   2377 C CB  . ASP A 1 352 ? 3.789   11.082 24.252  1.00 40.13  ? 367 ASP A CB  1 
ATOM   2378 C CG  . ASP A 1 352 ? 5.231   11.555 24.158  1.00 43.81  ? 367 ASP A CG  1 
ATOM   2379 O OD1 . ASP A 1 352 ? 6.006   11.334 25.116  1.00 43.73  ? 367 ASP A OD1 1 
ATOM   2380 O OD2 . ASP A 1 352 ? 5.586   12.164 23.126  1.00 44.39  ? 367 ASP A OD2 1 
ATOM   2381 N N   . LYS A 1 353 ? 4.990   8.936  26.732  1.00 42.55  ? 368 LYS A N   1 
ATOM   2382 C CA  . LYS A 1 353 ? 5.293   8.792  28.154  1.00 43.97  ? 368 LYS A CA  1 
ATOM   2383 C C   . LYS A 1 353 ? 5.727   10.102 28.808  1.00 41.78  ? 368 LYS A C   1 
ATOM   2384 O O   . LYS A 1 353 ? 5.732   10.190 30.040  1.00 46.76  ? 368 LYS A O   1 
ATOM   2385 C CB  . LYS A 1 353 ? 6.378   7.728  28.365  1.00 42.12  ? 368 LYS A CB  1 
ATOM   2386 C CG  . LYS A 1 353 ? 7.749   8.072  27.779  1.00 52.66  ? 368 LYS A CG  1 
ATOM   2387 C CD  . LYS A 1 353 ? 8.687   6.861  27.795  1.00 52.85  ? 368 LYS A CD  1 
ATOM   2388 C CE  . LYS A 1 353 ? 8.142   5.721  26.937  1.00 53.60  ? 368 LYS A CE  1 
ATOM   2389 N NZ  . LYS A 1 353 ? 9.090   4.576  26.821  1.00 57.83  ? 368 LYS A NZ  1 
ATOM   2390 N N   . ASN A 1 354 ? 6.086   11.118 28.031  1.00 37.94  ? 369 ASN A N   1 
ATOM   2391 C CA  . ASN A 1 354 ? 6.542   12.383 28.591  1.00 44.42  ? 369 ASN A CA  1 
ATOM   2392 C C   . ASN A 1 354 ? 5.425   13.404 28.776  1.00 49.24  ? 369 ASN A C   1 
ATOM   2393 O O   . ASN A 1 354 ? 5.698   14.517 29.246  1.00 44.30  ? 369 ASN A O   1 
ATOM   2394 C CB  . ASN A 1 354 ? 7.626   12.998 27.701  1.00 45.39  ? 369 ASN A CB  1 
ATOM   2395 C CG  . ASN A 1 354 ? 8.817   12.084 27.514  1.00 53.25  ? 369 ASN A CG  1 
ATOM   2396 O OD1 . ASN A 1 354 ? 9.189   11.338 28.420  1.00 46.90  ? 369 ASN A OD1 1 
ATOM   2397 N ND2 . ASN A 1 354 ? 9.433   12.149 26.338  1.00 55.60  ? 369 ASN A ND2 1 
ATOM   2398 N N   . PHE A 1 355 ? 4.186   13.067 28.421  1.00 37.57  ? 370 PHE A N   1 
ATOM   2399 C CA  . PHE A 1 355 ? 3.139   14.065 28.294  1.00 38.72  ? 370 PHE A CA  1 
ATOM   2400 C C   . PHE A 1 355 ? 1.926   13.713 29.141  1.00 39.06  ? 370 PHE A C   1 
ATOM   2401 O O   . PHE A 1 355 ? 1.604   12.540 29.356  1.00 38.18  ? 370 PHE A O   1 
ATOM   2402 C CB  . PHE A 1 355 ? 2.714   14.226 26.833  1.00 37.57  ? 370 PHE A CB  1 
ATOM   2403 C CG  . PHE A 1 355 ? 3.505   15.258 26.088  1.00 39.51  ? 370 PHE A CG  1 
ATOM   2404 C CD1 . PHE A 1 355 ? 4.687   14.914 25.452  1.00 38.94  ? 370 PHE A CD1 1 
ATOM   2405 C CD2 . PHE A 1 355 ? 3.068   16.575 26.026  1.00 42.62  ? 370 PHE A CD2 1 
ATOM   2406 C CE1 . PHE A 1 355 ? 5.419   15.862 24.761  1.00 41.96  ? 370 PHE A CE1 1 
ATOM   2407 C CE2 . PHE A 1 355 ? 3.797   17.531 25.338  1.00 45.49  ? 370 PHE A CE2 1 
ATOM   2408 C CZ  . PHE A 1 355 ? 4.976   17.174 24.705  1.00 42.95  ? 370 PHE A CZ  1 
ATOM   2409 N N   . ILE A 1 356 ? 1.254   14.755 29.620  1.00 37.02  ? 371 ILE A N   1 
ATOM   2410 C CA  . ILE A 1 356 ? -0.050  14.634 30.259  1.00 38.44  ? 371 ILE A CA  1 
ATOM   2411 C C   . ILE A 1 356 ? -0.998  15.603 29.568  1.00 40.37  ? 371 ILE A C   1 
ATOM   2412 O O   . ILE A 1 356 ? -0.640  16.760 29.311  1.00 37.42  ? 371 ILE A O   1 
ATOM   2413 C CB  . ILE A 1 356 ? 0.019   14.916 31.776  1.00 36.08  ? 371 ILE A CB  1 
ATOM   2414 C CG1 . ILE A 1 356 ? 1.094   14.044 32.437  1.00 32.74  ? 371 ILE A CG1 1 
ATOM   2415 C CG2 . ILE A 1 356 ? -1.325  14.661 32.417  1.00 32.72  ? 371 ILE A CG2 1 
ATOM   2416 C CD1 . ILE A 1 356 ? 1.144   14.159 33.936  1.00 27.00  ? 371 ILE A CD1 1 
ATOM   2417 N N   . ALA A 1 357 ? -2.197  15.125 29.245  1.00 34.13  ? 372 ALA A N   1 
ATOM   2418 C CA  . ALA A 1 357 ? -3.222  15.940 28.608  1.00 37.48  ? 372 ALA A CA  1 
ATOM   2419 C C   . ALA A 1 357 ? -4.196  16.448 29.664  1.00 37.09  ? 372 ALA A C   1 
ATOM   2420 O O   . ALA A 1 357 ? -4.767  15.658 30.422  1.00 36.11  ? 372 ALA A O   1 
ATOM   2421 C CB  . ALA A 1 357 ? -3.965  15.147 27.532  1.00 36.34  ? 372 ALA A CB  1 
ATOM   2422 N N   . THR A 1 358 ? -4.374  17.766 29.714  1.00 34.39  ? 373 THR A N   1 
ATOM   2423 C CA  . THR A 1 358 ? -5.237  18.406 30.691  1.00 35.45  ? 373 THR A CA  1 
ATOM   2424 C C   . THR A 1 358 ? -6.194  19.365 29.995  1.00 38.02  ? 373 THR A C   1 
ATOM   2425 O O   . THR A 1 358 ? -5.915  19.871 28.904  1.00 40.41  ? 373 THR A O   1 
ATOM   2426 C CB  . THR A 1 358 ? -4.412  19.157 31.749  1.00 40.24  ? 373 THR A CB  1 
ATOM   2427 O OG1 . THR A 1 358 ? -5.275  19.616 32.796  1.00 39.41  ? 373 THR A OG1 1 
ATOM   2428 C CG2 . THR A 1 358 ? -3.677  20.340 31.137  1.00 32.42  ? 373 THR A CG2 1 
ATOM   2429 N N   . THR A 1 359 ? -7.341  19.593 30.625  1.00 36.31  ? 374 THR A N   1 
ATOM   2430 C CA  . THR A 1 359 ? -8.266  20.628 30.192  1.00 38.92  ? 374 THR A CA  1 
ATOM   2431 C C   . THR A 1 359 ? -8.529  21.586 31.345  1.00 36.81  ? 374 THR A C   1 
ATOM   2432 O O   . THR A 1 359 ? -8.291  21.270 32.517  1.00 34.25  ? 374 THR A O   1 
ATOM   2433 C CB  . THR A 1 359 ? -9.605  20.054 29.698  1.00 40.88  ? 374 THR A CB  1 
ATOM   2434 O OG1 . THR A 1 359 ? -10.472 19.837 30.820  1.00 35.07  ? 374 THR A OG1 1 
ATOM   2435 C CG2 . THR A 1 359 ? -9.400  18.741 28.930  1.00 34.79  ? 374 THR A CG2 1 
ATOM   2436 N N   . ALA A 1 360 ? -9.039  22.767 30.989  1.00 36.58  ? 375 ALA A N   1 
ATOM   2437 C CA  . ALA A 1 360 ? -9.373  23.766 31.996  1.00 37.07  ? 375 ALA A CA  1 
ATOM   2438 C C   . ALA A 1 360 ? -10.372 23.234 33.013  1.00 34.06  ? 375 ALA A C   1 
ATOM   2439 O O   . ALA A 1 360 ? -10.344 23.644 34.177  1.00 35.32  ? 375 ALA A O   1 
ATOM   2440 C CB  . ALA A 1 360 ? -9.928  25.015 31.325  1.00 32.71  ? 375 ALA A CB  1 
ATOM   2441 N N   . LEU A 1 361 ? -11.248 22.319 32.597  1.00 33.58  ? 376 LEU A N   1 
ATOM   2442 C CA  . LEU A 1 361 ? -12.253 21.745 33.484  1.00 35.80  ? 376 LEU A CA  1 
ATOM   2443 C C   . LEU A 1 361 ? -11.705 20.639 34.381  1.00 37.21  ? 376 LEU A C   1 
ATOM   2444 O O   . LEU A 1 361 ? -12.350 20.287 35.378  1.00 39.18  ? 376 LEU A O   1 
ATOM   2445 C CB  . LEU A 1 361 ? -13.407 21.187 32.650  1.00 36.40  ? 376 LEU A CB  1 
ATOM   2446 C CG  . LEU A 1 361 ? -14.255 22.201 31.883  1.00 41.17  ? 376 LEU A CG  1 
ATOM   2447 C CD1 . LEU A 1 361 ? -13.779 22.293 30.454  1.00 41.16  ? 376 LEU A CD1 1 
ATOM   2448 C CD2 . LEU A 1 361 ? -15.715 21.800 31.922  1.00 36.19  ? 376 LEU A CD2 1 
ATOM   2449 N N   . SER A 1 362 ? -10.545 20.082 34.051  1.00 38.77  ? 377 SER A N   1 
ATOM   2450 C CA  . SER A 1 362 ? -10.068 18.871 34.693  1.00 34.67  ? 377 SER A CA  1 
ATOM   2451 C C   . SER A 1 362 ? -9.541  19.165 36.093  1.00 33.56  ? 377 SER A C   1 
ATOM   2452 O O   . SER A 1 362 ? -9.197  20.301 36.433  1.00 33.60  ? 377 SER A O   1 
ATOM   2453 C CB  . SER A 1 362 ? -8.972  18.216 33.847  1.00 36.72  ? 377 SER A CB  1 
ATOM   2454 O OG  . SER A 1 362 ? -9.400  18.015 32.509  1.00 37.60  ? 377 SER A OG  1 
ATOM   2455 N N   . HIS A 1 363 ? -9.473  18.109 36.900  1.00 34.78  ? 378 HIS A N   1 
ATOM   2456 C CA  . HIS A 1 363 ? -8.904  18.219 38.234  1.00 35.98  ? 378 HIS A CA  1 
ATOM   2457 C C   . HIS A 1 363 ? -7.476  18.756 38.157  1.00 36.40  ? 378 HIS A C   1 
ATOM   2458 O O   . HIS A 1 363 ? -6.754  18.469 37.195  1.00 33.18  ? 378 HIS A O   1 
ATOM   2459 C CB  . HIS A 1 363 ? -8.913  16.863 38.937  1.00 33.19  ? 378 HIS A CB  1 
ATOM   2460 C CG  . HIS A 1 363 ? -8.637  16.947 40.406  1.00 41.78  ? 378 HIS A CG  1 
ATOM   2461 N ND1 . HIS A 1 363 ? -7.363  17.094 40.914  1.00 37.92  ? 378 HIS A ND1 1 
ATOM   2462 C CD2 . HIS A 1 363 ? -9.468  16.923 41.474  1.00 34.29  ? 378 HIS A CD2 1 
ATOM   2463 C CE1 . HIS A 1 363 ? -7.422  17.148 42.231  1.00 38.76  ? 378 HIS A CE1 1 
ATOM   2464 N NE2 . HIS A 1 363 ? -8.686  17.041 42.596  1.00 39.01  ? 378 HIS A NE2 1 
ATOM   2465 N N   . PRO A 1 364 ? -7.045  19.554 39.137  1.00 34.88  ? 379 PRO A N   1 
ATOM   2466 C CA  . PRO A 1 364 ? -5.685  20.111 39.079  1.00 39.90  ? 379 PRO A CA  1 
ATOM   2467 C C   . PRO A 1 364 ? -4.579  19.068 39.037  1.00 38.64  ? 379 PRO A C   1 
ATOM   2468 O O   . PRO A 1 364 ? -3.545  19.316 38.404  1.00 42.87  ? 379 PRO A O   1 
ATOM   2469 C CB  . PRO A 1 364 ? -5.612  20.960 40.352  1.00 40.94  ? 379 PRO A CB  1 
ATOM   2470 C CG  . PRO A 1 364 ? -7.025  21.389 40.577  1.00 39.66  ? 379 PRO A CG  1 
ATOM   2471 C CD  . PRO A 1 364 ? -7.860  20.202 40.179  1.00 32.87  ? 379 PRO A CD  1 
ATOM   2472 N N   . ARG A 1 365 ? -4.747  17.910 39.674  1.00 35.19  ? 380 ARG A N   1 
ATOM   2473 C CA  . ARG A 1 365 ? -3.617  16.987 39.782  1.00 42.15  ? 380 ARG A CA  1 
ATOM   2474 C C   . ARG A 1 365 ? -3.948  15.515 39.585  1.00 36.51  ? 380 ARG A C   1 
ATOM   2475 O O   . ARG A 1 365 ? -3.018  14.732 39.375  1.00 41.99  ? 380 ARG A O   1 
ATOM   2476 C CB  . ARG A 1 365 ? -2.927  17.158 41.140  1.00 42.83  ? 380 ARG A CB  1 
ATOM   2477 C CG  . ARG A 1 365 ? -1.931  18.303 41.157  1.00 45.28  ? 380 ARG A CG  1 
ATOM   2478 C CD  . ARG A 1 365 ? -0.998  18.203 42.338  1.00 49.83  ? 380 ARG A CD  1 
ATOM   2479 N NE  . ARG A 1 365 ? -1.713  18.295 43.603  1.00 51.01  ? 380 ARG A NE  1 
ATOM   2480 C CZ  . ARG A 1 365 ? -1.146  18.634 44.751  1.00 54.98  ? 380 ARG A CZ  1 
ATOM   2481 N NH1 . ARG A 1 365 ? 0.144   18.928 44.822  1.00 51.69  ? 380 ARG A NH1 1 
ATOM   2482 N NH2 . ARG A 1 365 ? -1.889  18.678 45.854  1.00 46.23  ? 380 ARG A NH2 1 
ATOM   2483 N N   . GLU A 1 366 ? -5.207  15.095 39.645  1.00 40.70  ? 381 GLU A N   1 
ATOM   2484 C CA  . GLU A 1 366 ? -5.532  13.696 39.404  1.00 37.28  ? 381 GLU A CA  1 
ATOM   2485 C C   . GLU A 1 366 ? -5.081  13.274 38.008  1.00 41.09  ? 381 GLU A C   1 
ATOM   2486 O O   . GLU A 1 366 ? -5.357  13.954 37.015  1.00 35.60  ? 381 GLU A O   1 
ATOM   2487 C CB  . GLU A 1 366 ? -7.035  13.474 39.573  1.00 38.14  ? 381 GLU A CB  1 
ATOM   2488 C CG  . GLU A 1 366 ? -7.511  13.537 41.014  1.00 36.53  ? 381 GLU A CG  1 
ATOM   2489 C CD  . GLU A 1 366 ? -9.023  13.428 41.131  1.00 44.99  ? 381 GLU A CD  1 
ATOM   2490 O OE1 . GLU A 1 366 ? -9.687  13.182 40.100  1.00 42.60  ? 381 GLU A OE1 1 
ATOM   2491 O OE2 . GLU A 1 366 ? -9.548  13.586 42.256  1.00 48.69  ? 381 GLU A OE2 1 
ATOM   2492 N N   . VAL A 1 367 ? -4.369  12.154 37.935  1.00 37.32  ? 382 VAL A N   1 
ATOM   2493 C CA  . VAL A 1 367 ? -3.863  11.633 36.673  1.00 39.70  ? 382 VAL A CA  1 
ATOM   2494 C C   . VAL A 1 367 ? -4.286  10.180 36.541  1.00 40.83  ? 382 VAL A C   1 
ATOM   2495 O O   . VAL A 1 367 ? -4.030  9.370  37.439  1.00 41.58  ? 382 VAL A O   1 
ATOM   2496 C CB  . VAL A 1 367 ? -2.330  11.748 36.567  1.00 39.85  ? 382 VAL A CB  1 
ATOM   2497 C CG1 . VAL A 1 367 ? -1.835  11.016 35.334  1.00 39.03  ? 382 VAL A CG1 1 
ATOM   2498 C CG2 . VAL A 1 367 ? -1.908  13.194 36.509  1.00 37.80  ? 382 VAL A CG2 1 
ATOM   2499 N N   . ASP A 1 368 ? -4.930  9.852  35.426  1.00 36.86  ? 383 ASP A N   1 
ATOM   2500 C CA  . ASP A 1 368 ? -5.182  8.468  35.055  1.00 40.96  ? 383 ASP A CA  1 
ATOM   2501 C C   . ASP A 1 368 ? -4.057  8.030  34.123  1.00 42.97  ? 383 ASP A C   1 
ATOM   2502 O O   . ASP A 1 368 ? -3.909  8.575  33.022  1.00 43.95  ? 383 ASP A O   1 
ATOM   2503 C CB  . ASP A 1 368 ? -6.551  8.326  34.392  1.00 43.85  ? 383 ASP A CB  1 
ATOM   2504 C CG  . ASP A 1 368 ? -6.795  6.935  33.837  1.00 49.90  ? 383 ASP A CG  1 
ATOM   2505 O OD1 . ASP A 1 368 ? -6.075  5.989  34.230  1.00 52.45  ? 383 ASP A OD1 1 
ATOM   2506 O OD2 . ASP A 1 368 ? -7.727  6.787  33.021  1.00 58.54  ? 383 ASP A OD2 1 
ATOM   2507 N N   . LEU A 1 369 ? -3.261  7.055  34.568  1.00 43.59  ? 384 LEU A N   1 
ATOM   2508 C CA  . LEU A 1 369 ? -2.024  6.699  33.883  1.00 46.59  ? 384 LEU A CA  1 
ATOM   2509 C C   . LEU A 1 369 ? -2.199  5.637  32.806  1.00 49.03  ? 384 LEU A C   1 
ATOM   2510 O O   . LEU A 1 369 ? -1.301  5.470  31.970  1.00 45.94  ? 384 LEU A O   1 
ATOM   2511 C CB  . LEU A 1 369 ? -0.985  6.218  34.899  1.00 37.72  ? 384 LEU A CB  1 
ATOM   2512 C CG  . LEU A 1 369 ? -0.213  7.363  35.544  1.00 49.64  ? 384 LEU A CG  1 
ATOM   2513 C CD1 . LEU A 1 369 ? 0.747   6.844  36.596  1.00 42.60  ? 384 LEU A CD1 1 
ATOM   2514 C CD2 . LEU A 1 369 ? 0.518   8.156  34.471  1.00 45.72  ? 384 LEU A CD2 1 
ATOM   2515 N N   . GLU A 1 370 ? -3.324  4.930  32.789  1.00 45.21  ? 385 GLU A N   1 
ATOM   2516 C CA  . GLU A 1 370 ? -3.496  3.768  31.920  1.00 47.60  ? 385 GLU A CA  1 
ATOM   2517 C C   . GLU A 1 370 ? -4.018  4.220  30.562  1.00 49.83  ? 385 GLU A C   1 
ATOM   2518 O O   . GLU A 1 370 ? -5.223  4.407  30.377  1.00 56.42  ? 385 GLU A O   1 
ATOM   2519 C CB  . GLU A 1 370 ? -4.434  2.753  32.564  1.00 52.26  ? 385 GLU A CB  1 
ATOM   2520 C CG  . GLU A 1 370 ? -3.748  1.733  33.480  1.00 57.24  ? 385 GLU A CG  1 
ATOM   2521 C CD  . GLU A 1 370 ? -2.359  1.299  33.004  1.00 67.95  ? 385 GLU A CD  1 
ATOM   2522 O OE1 . GLU A 1 370 ? -1.452  1.186  33.862  1.00 69.85  ? 385 GLU A OE1 1 
ATOM   2523 O OE2 . GLU A 1 370 ? -2.177  1.030  31.795  1.00 66.59  ? 385 GLU A OE2 1 
ATOM   2524 N N   . PHE A 1 371 ? -3.108  4.386  29.609  1.00 48.61  ? 386 PHE A N   1 
ATOM   2525 C CA  . PHE A 1 371 ? -3.506  4.665  28.238  1.00 47.25  ? 386 PHE A CA  1 
ATOM   2526 C C   . PHE A 1 371 ? -4.301  3.483  27.684  1.00 48.04  ? 386 PHE A C   1 
ATOM   2527 O O   . PHE A 1 371 ? -3.974  2.326  27.975  1.00 45.03  ? 386 PHE A O   1 
ATOM   2528 C CB  . PHE A 1 371 ? -2.272  4.925  27.369  1.00 47.16  ? 386 PHE A CB  1 
ATOM   2529 C CG  . PHE A 1 371 ? -2.575  5.588  26.056  1.00 40.88  ? 386 PHE A CG  1 
ATOM   2530 C CD1 . PHE A 1 371 ? -2.931  4.834  24.947  1.00 41.53  ? 386 PHE A CD1 1 
ATOM   2531 C CD2 . PHE A 1 371 ? -2.489  6.963  25.926  1.00 39.90  ? 386 PHE A CD2 1 
ATOM   2532 C CE1 . PHE A 1 371 ? -3.211  5.444  23.734  1.00 44.17  ? 386 PHE A CE1 1 
ATOM   2533 C CE2 . PHE A 1 371 ? -2.769  7.583  24.715  1.00 42.83  ? 386 PHE A CE2 1 
ATOM   2534 C CZ  . PHE A 1 371 ? -3.130  6.822  23.617  1.00 39.09  ? 386 PHE A CZ  1 
ATOM   2535 N N   . PRO A 1 372 ? -5.358  3.731  26.900  1.00 43.93  ? 387 PRO A N   1 
ATOM   2536 C CA  . PRO A 1 372 ? -6.125  2.617  26.325  1.00 45.30  ? 387 PRO A CA  1 
ATOM   2537 C C   . PRO A 1 372 ? -5.382  1.947  25.180  1.00 45.70  ? 387 PRO A C   1 
ATOM   2538 O O   . PRO A 1 372 ? -5.631  2.249  24.009  1.00 44.55  ? 387 PRO A O   1 
ATOM   2539 C CB  . PRO A 1 372 ? -7.417  3.288  25.844  1.00 41.40  ? 387 PRO A CB  1 
ATOM   2540 C CG  . PRO A 1 372 ? -7.047  4.712  25.624  1.00 43.37  ? 387 PRO A CG  1 
ATOM   2541 C CD  . PRO A 1 372 ? -5.944  5.044  26.579  1.00 41.66  ? 387 PRO A CD  1 
ATOM   2542 N N   . CYS A 1 373 ? -4.479  1.020  25.515  1.00 44.78  ? 388 CYS A N   1 
ATOM   2543 C CA  . CYS A 1 373 ? -3.562  0.465  24.521  1.00 48.80  ? 388 CYS A CA  1 
ATOM   2544 C C   . CYS A 1 373 ? -4.276  -0.411 23.498  1.00 47.39  ? 388 CYS A C   1 
ATOM   2545 O O   . CYS A 1 373 ? -3.790  -0.561 22.372  1.00 46.79  ? 388 CYS A O   1 
ATOM   2546 C CB  . CYS A 1 373 ? -2.457  -0.337 25.214  1.00 49.52  ? 388 CYS A CB  1 
ATOM   2547 S SG  . CYS A 1 373 ? -1.300  0.652  26.215  1.00 48.83  ? 388 CYS A SG  1 
ATOM   2548 N N   . SER A 1 374 ? -5.416  -0.991 23.861  1.00 49.59  ? 389 SER A N   1 
ATOM   2549 C CA  . SER A 1 374 ? -6.129  -1.919 22.992  1.00 48.26  ? 389 SER A CA  1 
ATOM   2550 C C   . SER A 1 374 ? -7.084  -1.232 22.025  1.00 48.73  ? 389 SER A C   1 
ATOM   2551 O O   . SER A 1 374 ? -7.770  -1.927 21.268  1.00 51.41  ? 389 SER A O   1 
ATOM   2552 C CB  . SER A 1 374 ? -6.915  -2.929 23.836  1.00 43.16  ? 389 SER A CB  1 
ATOM   2553 O OG  . SER A 1 374 ? -6.064  -3.945 24.332  1.00 52.92  ? 389 SER A OG  1 
ATOM   2554 N N   . ILE A 1 375 ? -7.144  0.103  22.026  1.00 49.19  ? 390 ILE A N   1 
ATOM   2555 C CA  . ILE A 1 375 ? -8.190  0.800  21.279  1.00 50.16  ? 390 ILE A CA  1 
ATOM   2556 C C   . ILE A 1 375 ? -8.083  0.502  19.788  1.00 49.00  ? 390 ILE A C   1 
ATOM   2557 O O   . ILE A 1 375 ? -9.093  0.259  19.118  1.00 48.74  ? 390 ILE A O   1 
ATOM   2558 C CB  . ILE A 1 375 ? -8.146  2.315  21.572  1.00 46.53  ? 390 ILE A CB  1 
ATOM   2559 C CG1 . ILE A 1 375 ? -9.385  3.010  21.007  1.00 44.12  ? 390 ILE A CG1 1 
ATOM   2560 C CG2 . ILE A 1 375 ? -6.860  2.962  21.040  1.00 41.63  ? 390 ILE A CG2 1 
ATOM   2561 C CD1 . ILE A 1 375 ? -9.491  4.464  21.410  1.00 46.38  ? 390 ILE A CD1 1 
ATOM   2562 N N   . TYR A 1 376 ? -6.860  0.483  19.253  1.00 46.90  ? 391 TYR A N   1 
ATOM   2563 C CA  . TYR A 1 376 ? -6.681  0.262  17.823  1.00 45.13  ? 391 TYR A CA  1 
ATOM   2564 C C   . TYR A 1 376 ? -6.908  -1.198 17.459  1.00 46.01  ? 391 TYR A C   1 
ATOM   2565 O O   . TYR A 1 376 ? -7.600  -1.502 16.482  1.00 52.61  ? 391 TYR A O   1 
ATOM   2566 C CB  . TYR A 1 376 ? -5.287  0.721  17.401  1.00 43.29  ? 391 TYR A CB  1 
ATOM   2567 C CG  . TYR A 1 376 ? -5.071  2.198  17.618  1.00 46.14  ? 391 TYR A CG  1 
ATOM   2568 C CD1 . TYR A 1 376 ? -5.997  3.124  17.156  1.00 41.49  ? 391 TYR A CD1 1 
ATOM   2569 C CD2 . TYR A 1 376 ? -3.951  2.671  18.301  1.00 45.72  ? 391 TYR A CD2 1 
ATOM   2570 C CE1 . TYR A 1 376 ? -5.812  4.481  17.351  1.00 42.57  ? 391 TYR A CE1 1 
ATOM   2571 C CE2 . TYR A 1 376 ? -3.756  4.031  18.504  1.00 42.27  ? 391 TYR A CE2 1 
ATOM   2572 C CZ  . TYR A 1 376 ? -4.694  4.930  18.024  1.00 41.80  ? 391 TYR A CZ  1 
ATOM   2573 O OH  . TYR A 1 376 ? -4.525  6.282  18.209  1.00 41.86  ? 391 TYR A OH  1 
ATOM   2574 N N   . LYS A 1 377 ? -6.350  -2.117 18.250  1.00 50.92  ? 392 LYS A N   1 
ATOM   2575 C CA  . LYS A 1 377 ? -6.499  -3.541 17.964  1.00 50.97  ? 392 LYS A CA  1 
ATOM   2576 C C   . LYS A 1 377 ? -7.960  -3.972 18.044  1.00 55.36  ? 392 LYS A C   1 
ATOM   2577 O O   . LYS A 1 377 ? -8.449  -4.705 17.175  1.00 60.40  ? 392 LYS A O   1 
ATOM   2578 C CB  . LYS A 1 377 ? -5.639  -4.358 18.928  1.00 45.42  ? 392 LYS A CB  1 
ATOM   2579 C CG  . LYS A 1 377 ? -5.356  -5.769 18.456  1.00 46.04  ? 392 LYS A CG  1 
ATOM   2580 N N   . ASP A 1 378 ? -8.675  -3.527 19.084  1.00 49.32  ? 393 ASP A N   1 
ATOM   2581 C CA  . ASP A 1 378 ? -10.091 -3.868 19.214  1.00 53.27  ? 393 ASP A CA  1 
ATOM   2582 C C   . ASP A 1 378 ? -10.900 -3.343 18.035  1.00 56.52  ? 393 ASP A C   1 
ATOM   2583 O O   . ASP A 1 378 ? -11.792 -4.033 17.528  1.00 57.33  ? 393 ASP A O   1 
ATOM   2584 C CB  . ASP A 1 378 ? -10.666 -3.307 20.518  1.00 51.33  ? 393 ASP A CB  1 
ATOM   2585 C CG  . ASP A 1 378 ? -10.091 -3.971 21.753  1.00 52.89  ? 393 ASP A CG  1 
ATOM   2586 O OD1 . ASP A 1 378 ? -9.329  -4.951 21.613  1.00 51.51  ? 393 ASP A OD1 1 
ATOM   2587 O OD2 . ASP A 1 378 ? -10.410 -3.506 22.870  1.00 51.69  ? 393 ASP A OD2 1 
ATOM   2588 N N   . GLU A 1 379 ? -10.613 -2.118 17.593  1.00 56.57  ? 394 GLU A N   1 
ATOM   2589 C CA  . GLU A 1 379 ? -11.408 -1.521 16.527  1.00 61.95  ? 394 GLU A CA  1 
ATOM   2590 C C   . GLU A 1 379 ? -11.105 -2.166 15.183  1.00 63.99  ? 394 GLU A C   1 
ATOM   2591 O O   . GLU A 1 379 ? -12.017 -2.395 14.380  1.00 68.02  ? 394 GLU A O   1 
ATOM   2592 C CB  . GLU A 1 379 ? -11.165 -0.015 16.464  1.00 55.11  ? 394 GLU A CB  1 
ATOM   2593 C CG  . GLU A 1 379 ? -12.281 0.753  15.775  1.00 63.30  ? 394 GLU A CG  1 
ATOM   2594 C CD  . GLU A 1 379 ? -13.580 0.745  16.564  1.00 72.87  ? 394 GLU A CD  1 
ATOM   2595 O OE1 . GLU A 1 379 ? -13.554 0.405  17.769  1.00 71.04  ? 394 GLU A OE1 1 
ATOM   2596 O OE2 . GLU A 1 379 ? -14.631 1.079  15.973  1.00 78.30  ? 394 GLU A OE2 1 
ATOM   2597 N N   . ILE A 1 380 ? -9.831  -2.459 14.919  1.00 60.29  ? 395 ILE A N   1 
ATOM   2598 C CA  . ILE A 1 380 ? -9.471  -3.157 13.688  1.00 62.20  ? 395 ILE A CA  1 
ATOM   2599 C C   . ILE A 1 380 ? -10.221 -4.480 13.590  1.00 67.53  ? 395 ILE A C   1 
ATOM   2600 O O   . ILE A 1 380 ? -10.723 -4.848 12.520  1.00 69.90  ? 395 ILE A O   1 
ATOM   2601 C CB  . ILE A 1 380 ? -7.944  -3.350 13.617  1.00 54.89  ? 395 ILE A CB  1 
ATOM   2602 C CG1 . ILE A 1 380 ? -7.267  -2.027 13.247  1.00 49.75  ? 395 ILE A CG1 1 
ATOM   2603 C CG2 . ILE A 1 380 ? -7.573  -4.444 12.627  1.00 55.16  ? 395 ILE A CG2 1 
ATOM   2604 C CD1 . ILE A 1 380 ? -5.880  -1.854 13.840  1.00 46.63  ? 395 ILE A CD1 1 
ATOM   2605 N N   . GLU A 1 381 ? -10.334 -5.204 14.707  1.00 64.04  ? 396 GLU A N   1 
ATOM   2606 C CA  . GLU A 1 381 ? -11.152 -6.413 14.714  1.00 69.85  ? 396 GLU A CA  1 
ATOM   2607 C C   . GLU A 1 381 ? -12.636 -6.091 14.570  1.00 75.47  ? 396 GLU A C   1 
ATOM   2608 O O   . GLU A 1 381 ? -13.375 -6.859 13.942  1.00 75.13  ? 396 GLU A O   1 
ATOM   2609 C CB  . GLU A 1 381 ? -10.904 -7.215 15.992  1.00 60.23  ? 396 GLU A CB  1 
ATOM   2610 C CG  . GLU A 1 381 ? -9.550  -7.906 16.033  1.00 63.84  ? 396 GLU A CG  1 
ATOM   2611 N N   . ARG A 1 382 ? -13.091 -4.970 15.136  1.00 72.15  ? 397 ARG A N   1 
ATOM   2612 C CA  . ARG A 1 382 ? -14.497 -4.600 15.005  1.00 73.67  ? 397 ARG A CA  1 
ATOM   2613 C C   . ARG A 1 382 ? -14.843 -4.251 13.563  1.00 81.80  ? 397 ARG A C   1 
ATOM   2614 O O   . ARG A 1 382 ? -15.930 -4.591 13.080  1.00 87.27  ? 397 ARG A O   1 
ATOM   2615 C CB  . ARG A 1 382 ? -14.826 -3.431 15.936  1.00 68.47  ? 397 ARG A CB  1 
ATOM   2616 N N   . GLU A 1 383 ? -13.929 -3.582 12.855  1.00 79.97  ? 398 GLU A N   1 
ATOM   2617 C CA  . GLU A 1 383 ? -14.182 -3.192 11.473  1.00 80.15  ? 398 GLU A CA  1 
ATOM   2618 C C   . GLU A 1 383 ? -13.962 -4.331 10.490  1.00 83.16  ? 398 GLU A C   1 
ATOM   2619 O O   . GLU A 1 383 ? -14.448 -4.250 9.356   1.00 87.83  ? 398 GLU A O   1 
ATOM   2620 C CB  . GLU A 1 383 ? -13.293 -2.013 11.079  1.00 72.15  ? 398 GLU A CB  1 
ATOM   2621 C CG  . GLU A 1 383 ? -13.517 -0.747 11.887  1.00 74.84  ? 398 GLU A CG  1 
ATOM   2622 C CD  . GLU A 1 383 ? -14.924 -0.204 11.750  1.00 83.22  ? 398 GLU A CD  1 
ATOM   2623 O OE1 . GLU A 1 383 ? -15.493 -0.300 10.643  1.00 87.92  ? 398 GLU A OE1 1 
ATOM   2624 O OE2 . GLU A 1 383 ? -15.453 0.332  12.747  1.00 87.86  ? 398 GLU A OE2 1 
ATOM   2625 N N   . ILE A 1 384 ? -13.233 -5.379 10.888  1.00 81.04  ? 399 ILE A N   1 
ATOM   2626 C CA  . ILE A 1 384 ? -13.085 -6.544 10.021  1.00 84.94  ? 399 ILE A CA  1 
ATOM   2627 C C   . ILE A 1 384 ? -14.431 -7.215 9.804   1.00 86.69  ? 399 ILE A C   1 
ATOM   2628 O O   . ILE A 1 384 ? -14.684 -7.793 8.739   1.00 93.54  ? 399 ILE A O   1 
ATOM   2629 C CB  . ILE A 1 384 ? -12.052 -7.529 10.604  1.00 78.90  ? 399 ILE A CB  1 
ATOM   2630 N N   . LYS A 1 385 ? -15.323 -7.138 10.794  1.00 84.32  ? 400 LYS A N   1 
ATOM   2631 C CA  . LYS A 1 385 ? -16.675 -7.662 10.645  1.00 87.42  ? 400 LYS A CA  1 
ATOM   2632 C C   . LYS A 1 385 ? -17.532 -6.824 9.704   1.00 91.19  ? 400 LYS A C   1 
ATOM   2633 O O   . LYS A 1 385 ? -18.710 -7.151 9.515   1.00 92.10  ? 400 LYS A O   1 
ATOM   2634 C CB  . LYS A 1 385 ? -17.350 -7.765 12.013  1.00 83.83  ? 400 LYS A CB  1 
ATOM   2635 C CG  . LYS A 1 385 ? -17.843 -9.164 12.363  1.00 84.84  ? 400 LYS A CG  1 
ATOM   2636 C CD  . LYS A 1 385 ? -18.357 -9.909 11.140  1.00 79.28  ? 400 LYS A CD  1 
ATOM   2637 N N   . LYS A 1 386 ? -16.983 -5.760 9.123   1.00 90.30  ? 401 LYS A N   1 
ATOM   2638 C CA  . LYS A 1 386 ? -17.682 -4.980 8.109   1.00 86.85  ? 401 LYS A CA  1 
ATOM   2639 C C   . LYS A 1 386 ? -17.052 -5.224 6.741   1.00 82.19  ? 401 LYS A C   1 
ATOM   2640 O O   . LYS A 1 386 ? -16.220 -6.122 6.582   1.00 80.37  ? 401 LYS A O   1 
ATOM   2641 C CB  . LYS A 1 386 ? -17.655 -3.489 8.452   1.00 84.03  ? 401 LYS A CB  1 
ATOM   2642 N N   . ILE A 1 401 ? -11.947 -9.268 3.657   1.00 80.64  ? 416 ILE A N   1 
ATOM   2643 C CA  . ILE A 1 401 ? -10.641 -8.670 3.411   1.00 79.74  ? 416 ILE A CA  1 
ATOM   2644 C C   . ILE A 1 401 ? -10.741 -7.150 3.427   1.00 75.40  ? 416 ILE A C   1 
ATOM   2645 O O   . ILE A 1 401 ? -9.849  -6.456 2.936   1.00 78.12  ? 416 ILE A O   1 
ATOM   2646 C CB  . ILE A 1 401 ? -10.039 -9.162 2.079   1.00 75.18  ? 416 ILE A CB  1 
ATOM   2647 N N   . VAL A 1 402 ? -11.832 -6.633 3.990   1.00 72.50  ? 417 VAL A N   1 
ATOM   2648 C CA  . VAL A 1 402 ? -12.025 -5.189 4.120   1.00 77.38  ? 417 VAL A CA  1 
ATOM   2649 C C   . VAL A 1 402 ? -11.297 -4.747 5.387   1.00 72.15  ? 417 VAL A C   1 
ATOM   2650 O O   . VAL A 1 402 ? -11.786 -4.949 6.500   1.00 71.97  ? 417 VAL A O   1 
ATOM   2651 C CB  . VAL A 1 402 ? -13.506 -4.807 4.157   1.00 74.42  ? 417 VAL A CB  1 
ATOM   2652 C CG1 . VAL A 1 402 ? -13.680 -3.340 3.775   1.00 72.30  ? 417 VAL A CG1 1 
ATOM   2653 C CG2 . VAL A 1 402 ? -14.302 -5.705 3.231   1.00 68.41  ? 417 VAL A CG2 1 
ATOM   2654 N N   . LEU A 1 403 ? -10.123 -4.144 5.220   1.00 70.69  ? 418 LEU A N   1 
ATOM   2655 C CA  . LEU A 1 403 ? -9.357  -3.705 6.381   1.00 71.11  ? 418 LEU A CA  1 
ATOM   2656 C C   . LEU A 1 403 ? -9.602  -2.224 6.654   1.00 64.00  ? 418 LEU A C   1 
ATOM   2657 O O   . LEU A 1 403 ? -9.610  -1.413 5.721   1.00 64.43  ? 418 LEU A O   1 
ATOM   2658 C CB  . LEU A 1 403 ? -7.860  -3.943 6.175   1.00 65.66  ? 418 LEU A CB  1 
ATOM   2659 C CG  . LEU A 1 403 ? -7.243  -5.330 6.405   1.00 68.93  ? 418 LEU A CG  1 
ATOM   2660 C CD1 . LEU A 1 403 ? -8.169  -6.476 5.996   1.00 72.15  ? 418 LEU A CD1 1 
ATOM   2661 C CD2 . LEU A 1 403 ? -5.904  -5.437 5.684   1.00 63.80  ? 418 LEU A CD2 1 
ATOM   2662 N N   . PRO A 1 404 ? -9.794  -1.846 7.915   1.00 63.16  ? 419 PRO A N   1 
ATOM   2663 C CA  . PRO A 1 404 ? -10.184 -0.465 8.223   1.00 60.52  ? 419 PRO A CA  1 
ATOM   2664 C C   . PRO A 1 404 ? -9.063  0.533  7.979   1.00 55.40  ? 419 PRO A C   1 
ATOM   2665 O O   . PRO A 1 404 ? -7.877  0.200  7.928   1.00 56.66  ? 419 PRO A O   1 
ATOM   2666 C CB  . PRO A 1 404 ? -10.546 -0.521 9.709   1.00 60.21  ? 419 PRO A CB  1 
ATOM   2667 C CG  . PRO A 1 404 ? -9.768  -1.684 10.239  1.00 63.05  ? 419 PRO A CG  1 
ATOM   2668 C CD  . PRO A 1 404 ? -9.718  -2.687 9.124   1.00 60.62  ? 419 PRO A CD  1 
ATOM   2669 N N   . ARG A 1 405 ? -9.471  1.795  7.842   1.00 53.25  ? 420 ARG A N   1 
ATOM   2670 C CA  . ARG A 1 405 ? -8.535  2.903  7.668   1.00 54.52  ? 420 ARG A CA  1 
ATOM   2671 C C   . ARG A 1 405 ? -7.980  3.297  9.039   1.00 55.38  ? 420 ARG A C   1 
ATOM   2672 O O   . ARG A 1 405 ? -8.322  4.324  9.630   1.00 53.91  ? 420 ARG A O   1 
ATOM   2673 C CB  . ARG A 1 405 ? -9.217  4.069  6.967   1.00 57.37  ? 420 ARG A CB  1 
ATOM   2674 C CG  . ARG A 1 405 ? -9.386  3.865  5.469   1.00 55.20  ? 420 ARG A CG  1 
ATOM   2675 C CD  . ARG A 1 405 ? -9.780  5.157  4.762   1.00 54.93  ? 420 ARG A CD  1 
ATOM   2676 N NE  . ARG A 1 405 ? -8.616  5.930  4.340   1.00 52.15  ? 420 ARG A NE  1 
ATOM   2677 C CZ  . ARG A 1 405 ? -7.768  5.557  3.391   1.00 52.22  ? 420 ARG A CZ  1 
ATOM   2678 N NH1 . ARG A 1 405 ? -7.940  4.436  2.707   1.00 54.32  ? 420 ARG A NH1 1 
ATOM   2679 N NH2 . ARG A 1 405 ? -6.719  6.328  3.120   1.00 53.61  ? 420 ARG A NH2 1 
ATOM   2680 N N   . ILE A 1 406 ? -7.118  2.425  9.555   1.00 47.90  ? 421 ILE A N   1 
ATOM   2681 C CA  . ILE A 1 406 ? -6.417  2.639  10.815  1.00 47.53  ? 421 ILE A CA  1 
ATOM   2682 C C   . ILE A 1 406 ? -4.992  2.150  10.612  1.00 45.76  ? 421 ILE A C   1 
ATOM   2683 O O   . ILE A 1 406 ? -4.777  0.966  10.332  1.00 48.81  ? 421 ILE A O   1 
ATOM   2684 C CB  . ILE A 1 406 ? -7.079  1.903  11.998  1.00 48.58  ? 421 ILE A CB  1 
ATOM   2685 C CG1 . ILE A 1 406 ? -8.482  2.455  12.262  1.00 49.31  ? 421 ILE A CG1 1 
ATOM   2686 C CG2 . ILE A 1 406 ? -6.221  2.027  13.253  1.00 45.45  ? 421 ILE A CG2 1 
ATOM   2687 C CD1 . ILE A 1 406 ? -9.388  1.506  13.002  1.00 50.66  ? 421 ILE A CD1 1 
ATOM   2688 N N   . PHE A 1 407 ? -4.021  3.055  10.738  1.00 43.36  ? 422 PHE A N   1 
ATOM   2689 C CA  . PHE A 1 407 ? -2.630  2.760  10.423  1.00 43.01  ? 422 PHE A CA  1 
ATOM   2690 C C   . PHE A 1 407 ? -1.730  2.797  11.655  1.00 49.15  ? 422 PHE A C   1 
ATOM   2691 O O   . PHE A 1 407 ? -0.518  3.012  11.536  1.00 49.18  ? 422 PHE A O   1 
ATOM   2692 C CB  . PHE A 1 407 ? -2.137  3.728  9.349   1.00 46.24  ? 422 PHE A CB  1 
ATOM   2693 C CG  . PHE A 1 407 ? -3.043  3.799  8.154   1.00 51.67  ? 422 PHE A CG  1 
ATOM   2694 C CD1 . PHE A 1 407 ? -3.137  2.729  7.277   1.00 56.18  ? 422 PHE A CD1 1 
ATOM   2695 C CD2 . PHE A 1 407 ? -3.820  4.921  7.917   1.00 52.21  ? 422 PHE A CD2 1 
ATOM   2696 C CE1 . PHE A 1 407 ? -3.974  2.782  6.178   1.00 48.59  ? 422 PHE A CE1 1 
ATOM   2697 C CE2 . PHE A 1 407 ? -4.663  4.975  6.818   1.00 53.39  ? 422 PHE A CE2 1 
ATOM   2698 C CZ  . PHE A 1 407 ? -4.736  3.903  5.949   1.00 48.44  ? 422 PHE A CZ  1 
ATOM   2699 N N   . ILE A 1 408 ? -2.305  2.585  12.835  1.00 47.29  ? 423 ILE A N   1 
ATOM   2700 C CA  . ILE A 1 408 ? -1.567  2.509  14.089  1.00 41.17  ? 423 ILE A CA  1 
ATOM   2701 C C   . ILE A 1 408 ? -2.165  1.374  14.905  1.00 44.92  ? 423 ILE A C   1 
ATOM   2702 O O   . ILE A 1 408 ? -3.389  1.211  14.954  1.00 43.80  ? 423 ILE A O   1 
ATOM   2703 C CB  . ILE A 1 408 ? -1.625  3.840  14.867  1.00 45.40  ? 423 ILE A CB  1 
ATOM   2704 C CG1 . ILE A 1 408 ? -0.964  3.701  16.241  1.00 44.78  ? 423 ILE A CG1 1 
ATOM   2705 C CG2 . ILE A 1 408 ? -3.063  4.318  15.022  1.00 41.28  ? 423 ILE A CG2 1 
ATOM   2706 C CD1 . ILE A 1 408 ? -0.590  5.043  16.870  1.00 35.77  ? 423 ILE A CD1 1 
ATOM   2707 N N   . SER A 1 409 ? -1.302  0.576  15.526  1.00 44.26  ? 424 SER A N   1 
ATOM   2708 C CA  . SER A 1 409 ? -1.740  -0.506 16.400  1.00 47.10  ? 424 SER A CA  1 
ATOM   2709 C C   . SER A 1 409 ? -0.533  -0.990 17.187  1.00 47.86  ? 424 SER A C   1 
ATOM   2710 O O   . SER A 1 409 ? 0.614   -0.719 16.816  1.00 47.82  ? 424 SER A O   1 
ATOM   2711 C CB  . SER A 1 409 ? -2.367  -1.660 15.606  1.00 44.78  ? 424 SER A CB  1 
ATOM   2712 O OG  . SER A 1 409 ? -2.761  -2.717 16.460  1.00 42.34  ? 424 SER A OG  1 
ATOM   2713 N N   . ASN A 1 410 ? -0.800  -1.697 18.289  1.00 48.35  ? 425 ASN A N   1 
ATOM   2714 C CA  . ASN A 1 410 ? 0.293   -2.379 18.972  1.00 50.63  ? 425 ASN A CA  1 
ATOM   2715 C C   . ASN A 1 410 ? 0.594   -3.730 18.342  1.00 51.16  ? 425 ASN A C   1 
ATOM   2716 O O   . ASN A 1 410 ? 1.685   -4.271 18.555  1.00 56.75  ? 425 ASN A O   1 
ATOM   2717 C CB  . ASN A 1 410 ? -0.002  -2.548 20.467  1.00 46.11  ? 425 ASN A CB  1 
ATOM   2718 C CG  . ASN A 1 410 ? -1.394  -3.068 20.741  1.00 47.57  ? 425 ASN A CG  1 
ATOM   2719 O OD1 . ASN A 1 410 ? -2.129  -3.441 19.825  1.00 49.86  ? 425 ASN A OD1 1 
ATOM   2720 N ND2 . ASN A 1 410 ? -1.766  -3.097 22.016  1.00 42.77  ? 425 ASN A ND2 1 
ATOM   2721 N N   . ASP A 1 411 ? -0.343  -4.273 17.566  1.00 55.65  ? 426 ASP A N   1 
ATOM   2722 C CA  . ASP A 1 411 ? -0.111  -5.458 16.746  1.00 55.21  ? 426 ASP A CA  1 
ATOM   2723 C C   . ASP A 1 411 ? 0.382   -4.992 15.379  1.00 55.05  ? 426 ASP A C   1 
ATOM   2724 O O   . ASP A 1 411 ? -0.389  -4.430 14.593  1.00 53.32  ? 426 ASP A O   1 
ATOM   2725 C CB  . ASP A 1 411 ? -1.391  -6.286 16.633  1.00 55.00  ? 426 ASP A CB  1 
ATOM   2726 C CG  . ASP A 1 411 ? -1.240  -7.503 15.724  1.00 62.83  ? 426 ASP A CG  1 
ATOM   2727 O OD1 . ASP A 1 411 ? -0.127  -7.762 15.209  1.00 63.69  ? 426 ASP A OD1 1 
ATOM   2728 O OD2 . ASP A 1 411 ? -2.256  -8.209 15.530  1.00 62.70  ? 426 ASP A OD2 1 
ATOM   2729 N N   . LYS A 1 412 ? 1.670   -5.230 15.104  1.00 60.58  ? 427 LYS A N   1 
ATOM   2730 C CA  . LYS A 1 412 ? 2.279   -4.826 13.838  1.00 58.62  ? 427 LYS A CA  1 
ATOM   2731 C C   . LYS A 1 412 ? 1.513   -5.388 12.648  1.00 56.88  ? 427 LYS A C   1 
ATOM   2732 O O   . LYS A 1 412 ? 1.067   -4.645 11.767  1.00 60.52  ? 427 LYS A O   1 
ATOM   2733 C CB  . LYS A 1 412 ? 3.738   -5.289 13.784  1.00 51.78  ? 427 LYS A CB  1 
ATOM   2734 C CG  . LYS A 1 412 ? 4.742   -4.263 14.252  1.00 58.04  ? 427 LYS A CG  1 
ATOM   2735 C CD  . LYS A 1 412 ? 6.177   -4.686 13.944  1.00 56.48  ? 427 LYS A CD  1 
ATOM   2736 C CE  . LYS A 1 412 ? 6.484   -6.094 14.431  1.00 53.40  ? 427 LYS A CE  1 
ATOM   2737 N NZ  . LYS A 1 412 ? 6.258   -6.244 15.897  1.00 58.16  ? 427 LYS A NZ  1 
ATOM   2738 N N   . GLU A 1 413 ? 1.346   -6.712 12.617  1.00 58.23  ? 428 GLU A N   1 
ATOM   2739 C CA  . GLU A 1 413 ? 0.768   -7.376 11.453  1.00 65.79  ? 428 GLU A CA  1 
ATOM   2740 C C   . GLU A 1 413 ? -0.676  -6.965 11.193  1.00 59.78  ? 428 GLU A C   1 
ATOM   2741 O O   . GLU A 1 413 ? -1.138  -7.066 10.052  1.00 62.70  ? 428 GLU A O   1 
ATOM   2742 C CB  . GLU A 1 413 ? 0.854   -8.895 11.622  1.00 62.88  ? 428 GLU A CB  1 
ATOM   2743 N N   . SER A 1 414 ? -1.398  -6.498 12.214  1.00 59.32  ? 429 SER A N   1 
ATOM   2744 C CA  . SER A 1 414 ? -2.799  -6.138 12.023  1.00 59.46  ? 429 SER A CA  1 
ATOM   2745 C C   . SER A 1 414 ? -2.973  -4.950 11.084  1.00 59.15  ? 429 SER A C   1 
ATOM   2746 O O   . SER A 1 414 ? -4.081  -4.729 10.583  1.00 65.64  ? 429 SER A O   1 
ATOM   2747 C CB  . SER A 1 414 ? -3.456  -5.838 13.373  1.00 54.41  ? 429 SER A CB  1 
ATOM   2748 O OG  . SER A 1 414 ? -2.798  -4.776 14.045  1.00 60.22  ? 429 SER A OG  1 
ATOM   2749 N N   . ILE A 1 415 ? -1.914  -4.187 10.830  1.00 53.78  ? 430 ILE A N   1 
ATOM   2750 C CA  . ILE A 1 415 ? -2.004  -3.016 9.961   1.00 60.57  ? 430 ILE A CA  1 
ATOM   2751 C C   . ILE A 1 415 ? -1.794  -3.388 8.501   1.00 63.78  ? 430 ILE A C   1 
ATOM   2752 O O   . ILE A 1 415 ? -2.594  -3.017 7.640   1.00 64.90  ? 430 ILE A O   1 
ATOM   2753 C CB  . ILE A 1 415 ? -0.995  -1.940 10.411  1.00 55.49  ? 430 ILE A CB  1 
ATOM   2754 C CG1 . ILE A 1 415 ? -1.098  -1.695 11.920  1.00 58.88  ? 430 ILE A CG1 1 
ATOM   2755 C CG2 . ILE A 1 415 ? -1.215  -0.658 9.635   1.00 53.90  ? 430 ILE A CG2 1 
ATOM   2756 C CD1 . ILE A 1 415 ? 0.186   -1.152 12.529  1.00 48.83  ? 430 ILE A CD1 1 
ATOM   2757 N N   . LYS A 1 416 ? -0.713  -4.120 8.218   1.00 64.04  ? 431 LYS A N   1 
ATOM   2758 C CA  . LYS A 1 416 ? -0.292  -4.504 6.871   1.00 54.96  ? 431 LYS A CA  1 
ATOM   2759 C C   . LYS A 1 416 ? 0.183   -3.298 6.071   1.00 54.01  ? 431 LYS A C   1 
ATOM   2760 O O   . LYS A 1 416 ? -0.353  -3.018 4.996   1.00 60.40  ? 431 LYS A O   1 
ATOM   2761 C CB  . LYS A 1 416 ? -1.415  -5.233 6.121   1.00 62.03  ? 431 LYS A CB  1 
ATOM   2762 C CG  . LYS A 1 416 ? -1.977  -6.424 6.866   1.00 59.65  ? 431 LYS A CG  1 
ATOM   2763 C CD  . LYS A 1 416 ? -1.010  -7.591 6.832   1.00 62.33  ? 431 LYS A CD  1 
ATOM   2764 N N   . CYS A 1 417 ? 1.187   -2.588 6.589   1.00 56.11  ? 432 CYS A N   1 
ATOM   2765 C CA  . CYS A 1 417 ? 1.927   -1.620 5.792   1.00 60.19  ? 432 CYS A CA  1 
ATOM   2766 C C   . CYS A 1 417 ? 2.328   -2.203 4.442   1.00 62.70  ? 432 CYS A C   1 
ATOM   2767 O O   . CYS A 1 417 ? 2.721   -3.376 4.361   1.00 61.80  ? 432 CYS A O   1 
ATOM   2768 C CB  . CYS A 1 417 ? 3.207   -1.178 6.499   1.00 51.93  ? 432 CYS A CB  1 
ATOM   2769 S SG  . CYS A 1 417 ? 3.260   0.426  7.246   1.00 64.35  ? 432 CYS A SG  1 
ATOM   2770 N N   . PRO A 1 418 ? 2.281   -1.406 3.372   1.00 64.98  ? 433 PRO A N   1 
ATOM   2771 C CA  . PRO A 1 418 ? 3.114   -1.704 2.200   1.00 64.55  ? 433 PRO A CA  1 
ATOM   2772 C C   . PRO A 1 418 ? 4.595   -1.647 2.515   1.00 65.26  ? 433 PRO A C   1 
ATOM   2773 O O   . PRO A 1 418 ? 5.405   -2.046 1.669   1.00 71.78  ? 433 PRO A O   1 
ATOM   2774 C CB  . PRO A 1 418 ? 2.711   -0.620 1.188   1.00 66.94  ? 433 PRO A CB  1 
ATOM   2775 C CG  . PRO A 1 418 ? 1.357   -0.162 1.625   1.00 68.77  ? 433 PRO A CG  1 
ATOM   2776 C CD  . PRO A 1 418 ? 1.383   -0.267 3.137   1.00 63.06  ? 433 PRO A CD  1 
ATOM   2777 N N   . CYS A 1 419 ? 4.970   -1.165 3.700   1.00 59.15  ? 434 CYS A N   1 
ATOM   2778 C CA  . CYS A 1 419 ? 6.363   -1.149 4.122   1.00 58.22  ? 434 CYS A CA  1 
ATOM   2779 C C   . CYS A 1 419 ? 6.501   -1.740 5.519   1.00 61.23  ? 434 CYS A C   1 
ATOM   2780 O O   . CYS A 1 419 ? 5.718   -2.608 5.917   1.00 65.75  ? 434 CYS A O   1 
ATOM   2781 C CB  . CYS A 1 419 ? 6.930   0.272  4.085   1.00 59.23  ? 434 CYS A CB  1 
ATOM   2782 S SG  . CYS A 1 419 ? 6.104   1.453  5.162   1.00 79.37  ? 434 CYS A SG  1 
ATOM   2783 N N   . GLU A 1 420 ? 7.496   -1.298 6.255   1.00 55.64  ? 435 GLU A N   1 
ATOM   2784 C CA  . GLU A 1 420 ? 7.652   -1.791 7.616   1.00 60.83  ? 435 GLU A CA  1 
ATOM   2785 C C   . GLU A 1 420 ? 7.111   -0.758 8.592   1.00 59.50  ? 435 GLU A C   1 
ATOM   2786 O O   . GLU A 1 420 ? 7.510   0.412  8.518   1.00 53.07  ? 435 GLU A O   1 
ATOM   2787 C CB  . GLU A 1 420 ? 9.120   -2.078 7.917   1.00 49.92  ? 435 GLU A CB  1 
ATOM   2788 C CG  . GLU A 1 420 ? 9.555   -3.497 7.592   1.00 54.55  ? 435 GLU A CG  1 
ATOM   2789 N N   . PRO A 1 421 ? 6.203   -1.125 9.497   1.00 53.30  ? 436 PRO A N   1 
ATOM   2790 C CA  . PRO A 1 421 ? 5.713   -0.149 10.477  1.00 51.33  ? 436 PRO A CA  1 
ATOM   2791 C C   . PRO A 1 421 ? 6.841   0.371  11.354  1.00 50.38  ? 436 PRO A C   1 
ATOM   2792 O O   . PRO A 1 421 ? 7.824   -0.323 11.623  1.00 53.28  ? 436 PRO A O   1 
ATOM   2793 C CB  . PRO A 1 421 ? 4.694   -0.949 11.295  1.00 52.74  ? 436 PRO A CB  1 
ATOM   2794 C CG  . PRO A 1 421 ? 4.277   -2.068 10.387  1.00 54.72  ? 436 PRO A CG  1 
ATOM   2795 C CD  . PRO A 1 421 ? 5.514   -2.421 9.614   1.00 47.70  ? 436 PRO A CD  1 
ATOM   2796 N N   . GLU A 1 422 ? 6.692   1.615  11.798  1.00 46.31  ? 437 GLU A N   1 
ATOM   2797 C CA  . GLU A 1 422 ? 7.679   2.263  12.648  1.00 43.28  ? 437 GLU A CA  1 
ATOM   2798 C C   . GLU A 1 422 ? 7.159   2.334  14.078  1.00 47.11  ? 437 GLU A C   1 
ATOM   2799 O O   . GLU A 1 422 ? 6.053   2.831  14.320  1.00 46.93  ? 437 GLU A O   1 
ATOM   2800 C CB  . GLU A 1 422 ? 8.012   3.661  12.130  1.00 43.71  ? 437 GLU A CB  1 
ATOM   2801 C CG  . GLU A 1 422 ? 9.253   4.272  12.766  1.00 54.62  ? 437 GLU A CG  1 
ATOM   2802 N N   . HIS A 1 423 ? 7.955   1.824  15.011  1.00 42.58  ? 438 HIS A N   1 
ATOM   2803 C CA  . HIS A 1 423 ? 7.618   1.870  16.426  1.00 41.71  ? 438 HIS A CA  1 
ATOM   2804 C C   . HIS A 1 423 ? 7.750   3.293  16.959  1.00 45.80  ? 438 HIS A C   1 
ATOM   2805 O O   . HIS A 1 423 ? 8.684   4.018  16.605  1.00 44.23  ? 438 HIS A O   1 
ATOM   2806 C CB  . HIS A 1 423 ? 8.545   0.924  17.191  1.00 44.65  ? 438 HIS A CB  1 
ATOM   2807 C CG  . HIS A 1 423 ? 8.390   0.975  18.679  1.00 44.95  ? 438 HIS A CG  1 
ATOM   2808 N ND1 . HIS A 1 423 ? 9.306   1.599  19.497  1.00 44.33  ? 438 HIS A ND1 1 
ATOM   2809 C CD2 . HIS A 1 423 ? 7.452   0.444  19.498  1.00 40.76  ? 438 HIS A CD2 1 
ATOM   2810 C CE1 . HIS A 1 423 ? 8.925   1.472  20.755  1.00 38.38  ? 438 HIS A CE1 1 
ATOM   2811 N NE2 . HIS A 1 423 ? 7.805   0.774  20.783  1.00 45.17  ? 438 HIS A NE2 1 
ATOM   2812 N N   . ILE A 1 424 ? 6.803   3.698  17.805  1.00 41.27  ? 439 ILE A N   1 
ATOM   2813 C CA  . ILE A 1 424 ? 6.859   5.003  18.462  1.00 44.08  ? 439 ILE A CA  1 
ATOM   2814 C C   . ILE A 1 424 ? 7.685   4.852  19.730  1.00 44.36  ? 439 ILE A C   1 
ATOM   2815 O O   . ILE A 1 424 ? 7.297   4.116  20.643  1.00 42.47  ? 439 ILE A O   1 
ATOM   2816 C CB  . ILE A 1 424 ? 5.457   5.540  18.790  1.00 46.27  ? 439 ILE A CB  1 
ATOM   2817 C CG1 . ILE A 1 424 ? 4.439   5.098  17.741  1.00 48.17  ? 439 ILE A CG1 1 
ATOM   2818 C CG2 . ILE A 1 424 ? 5.482   7.062  18.896  1.00 40.97  ? 439 ILE A CG2 1 
ATOM   2819 C CD1 . ILE A 1 424 ? 4.556   5.851  16.464  1.00 46.99  ? 439 ILE A CD1 1 
ATOM   2820 N N   . SER A 1 425 ? 8.820   5.556  19.791  1.00 45.63  ? 440 SER A N   1 
ATOM   2821 C CA  . SER A 1 425 ? 9.749   5.358  20.900  1.00 50.62  ? 440 SER A CA  1 
ATOM   2822 C C   . SER A 1 425 ? 9.134   5.747  22.239  1.00 46.60  ? 440 SER A C   1 
ATOM   2823 O O   . SER A 1 425 ? 9.410   5.103  23.255  1.00 49.24  ? 440 SER A O   1 
ATOM   2824 C CB  . SER A 1 425 ? 11.039  6.143  20.658  1.00 53.59  ? 440 SER A CB  1 
ATOM   2825 O OG  . SER A 1 425 ? 10.775  7.359  19.981  1.00 70.23  ? 440 SER A OG  1 
ATOM   2826 N N   . GLN A 1 426 ? 8.297   6.778  22.271  1.00 48.09  ? 441 GLN A N   1 
ATOM   2827 C CA  . GLN A 1 426 ? 7.699   7.196  23.530  1.00 47.87  ? 441 GLN A CA  1 
ATOM   2828 C C   . GLN A 1 426 ? 6.334   6.564  23.776  1.00 46.15  ? 441 GLN A C   1 
ATOM   2829 O O   . GLN A 1 426 ? 5.680   6.897  24.770  1.00 43.35  ? 441 GLN A O   1 
ATOM   2830 C CB  . GLN A 1 426 ? 7.604   8.725  23.584  1.00 42.48  ? 441 GLN A CB  1 
ATOM   2831 C CG  . GLN A 1 426 ? 8.890   9.471  23.169  1.00 49.74  ? 441 GLN A CG  1 
ATOM   2832 C CD  . GLN A 1 426 ? 10.123  9.205  24.048  1.00 61.92  ? 441 GLN A CD  1 
ATOM   2833 O OE1 . GLN A 1 426 ? 10.266  8.155  24.683  1.00 64.13  ? 441 GLN A OE1 1 
ATOM   2834 N NE2 . GLN A 1 426 ? 11.030  10.175 24.071  1.00 66.26  ? 441 GLN A NE2 1 
ATOM   2835 N N   . SER A 1 427 ? 5.904   5.654  22.906  1.00 44.79  ? 442 SER A N   1 
ATOM   2836 C CA  . SER A 1 427 ? 4.671   4.905  23.116  1.00 43.55  ? 442 SER A CA  1 
ATOM   2837 C C   . SER A 1 427 ? 4.841   3.921  24.270  1.00 41.69  ? 442 SER A C   1 
ATOM   2838 O O   . SER A 1 427 ? 5.640   2.985  24.182  1.00 44.68  ? 442 SER A O   1 
ATOM   2839 C CB  . SER A 1 427 ? 4.295   4.158  21.837  1.00 40.36  ? 442 SER A CB  1 
ATOM   2840 O OG  . SER A 1 427 ? 3.146   3.346  22.019  1.00 47.56  ? 442 SER A OG  1 
ATOM   2841 N N   . THR A 1 428 ? 4.083   4.116  25.349  1.00 37.91  ? 443 THR A N   1 
ATOM   2842 C CA  . THR A 1 428 ? 4.076   3.112  26.405  1.00 37.62  ? 443 THR A CA  1 
ATOM   2843 C C   . THR A 1 428 ? 3.405   1.821  25.956  1.00 43.94  ? 443 THR A C   1 
ATOM   2844 O O   . THR A 1 428 ? 3.694   0.759  26.518  1.00 47.04  ? 443 THR A O   1 
ATOM   2845 C CB  . THR A 1 428 ? 3.377   3.645  27.657  1.00 37.75  ? 443 THR A CB  1 
ATOM   2846 O OG1 . THR A 1 428 ? 1.986   3.847  27.383  1.00 42.28  ? 443 THR A OG1 1 
ATOM   2847 C CG2 . THR A 1 428 ? 4.002   4.958  28.105  1.00 38.89  ? 443 THR A CG2 1 
ATOM   2848 N N   . CYS A 1 429 ? 2.524   1.888  24.958  1.00 40.19  ? 444 CYS A N   1 
ATOM   2849 C CA  . CYS A 1 429 ? 1.844   0.717  24.425  1.00 42.07  ? 444 CYS A CA  1 
ATOM   2850 C C   . CYS A 1 429 ? 2.659   -0.015 23.367  1.00 40.31  ? 444 CYS A C   1 
ATOM   2851 O O   . CYS A 1 429 ? 2.219   -1.074 22.903  1.00 37.46  ? 444 CYS A O   1 
ATOM   2852 C CB  . CYS A 1 429 ? 0.496   1.125  23.825  1.00 45.19  ? 444 CYS A CB  1 
ATOM   2853 S SG  . CYS A 1 429 ? -0.575  2.051  24.937  1.00 45.64  ? 444 CYS A SG  1 
ATOM   2854 N N   . ASN A 1 430 ? 3.824   0.517  22.986  1.00 34.71  ? 445 ASN A N   1 
ATOM   2855 C CA  . ASN A 1 430 ? 4.632   -0.007 21.881  1.00 40.24  ? 445 ASN A CA  1 
ATOM   2856 C C   . ASN A 1 430 ? 3.855   0.032  20.564  1.00 44.32  ? 445 ASN A C   1 
ATOM   2857 O O   . ASN A 1 430 ? 3.781   -0.953 19.822  1.00 41.02  ? 445 ASN A O   1 
ATOM   2858 C CB  . ASN A 1 430 ? 5.150   -1.417 22.186  1.00 38.02  ? 445 ASN A CB  1 
ATOM   2859 C CG  . ASN A 1 430 ? 6.092   -1.442 23.376  1.00 42.89  ? 445 ASN A CG  1 
ATOM   2860 O OD1 . ASN A 1 430 ? 5.794   -2.042 24.410  1.00 41.86  ? 445 ASN A OD1 1 
ATOM   2861 N ND2 . ASN A 1 430 ? 7.224   -0.756 23.246  1.00 34.57  ? 445 ASN A ND2 1 
ATOM   2862 N N   . PHE A 1 431 ? 3.277   1.195  20.272  1.00 36.99  ? 446 PHE A N   1 
ATOM   2863 C CA  . PHE A 1 431 ? 2.510   1.361  19.046  1.00 41.49  ? 446 PHE A CA  1 
ATOM   2864 C C   . PHE A 1 431 ? 3.428   1.400  17.830  1.00 41.00  ? 446 PHE A C   1 
ATOM   2865 O O   . PHE A 1 431 ? 4.528   1.958  17.875  1.00 37.77  ? 446 PHE A O   1 
ATOM   2866 C CB  . PHE A 1 431 ? 1.676   2.641  19.106  1.00 35.97  ? 446 PHE A CB  1 
ATOM   2867 C CG  . PHE A 1 431 ? 0.389   2.489  19.863  1.00 39.52  ? 446 PHE A CG  1 
ATOM   2868 C CD1 . PHE A 1 431 ? -0.270  1.271  19.899  1.00 37.88  ? 446 PHE A CD1 1 
ATOM   2869 C CD2 . PHE A 1 431 ? -0.162  3.566  20.538  1.00 35.34  ? 446 PHE A CD2 1 
ATOM   2870 C CE1 . PHE A 1 431 ? -1.451  1.129  20.597  1.00 43.00  ? 446 PHE A CE1 1 
ATOM   2871 C CE2 . PHE A 1 431 ? -1.346  3.429  21.237  1.00 41.65  ? 446 PHE A CE2 1 
ATOM   2872 C CZ  . PHE A 1 431 ? -1.991  2.209  21.267  1.00 41.47  ? 446 PHE A CZ  1 
ATOM   2873 N N   . TYR A 1 432 ? 2.969   0.796  16.742  1.00 39.70  ? 447 TYR A N   1 
ATOM   2874 C CA  . TYR A 1 432 ? 3.609   0.909  15.440  1.00 45.81  ? 447 TYR A CA  1 
ATOM   2875 C C   . TYR A 1 432 ? 2.686   1.684  14.509  1.00 46.69  ? 447 TYR A C   1 
ATOM   2876 O O   . TYR A 1 432 ? 1.465   1.506  14.554  1.00 48.73  ? 447 TYR A O   1 
ATOM   2877 C CB  . TYR A 1 432 ? 3.913   -0.472 14.855  1.00 44.36  ? 447 TYR A CB  1 
ATOM   2878 C CG  . TYR A 1 432 ? 5.115   -1.143 15.473  1.00 47.55  ? 447 TYR A CG  1 
ATOM   2879 C CD1 . TYR A 1 432 ? 5.016   -1.790 16.702  1.00 41.06  ? 447 TYR A CD1 1 
ATOM   2880 C CD2 . TYR A 1 432 ? 6.351   -1.131 14.830  1.00 49.33  ? 447 TYR A CD2 1 
ATOM   2881 C CE1 . TYR A 1 432 ? 6.112   -2.406 17.275  1.00 45.44  ? 447 TYR A CE1 1 
ATOM   2882 C CE2 . TYR A 1 432 ? 7.456   -1.747 15.393  1.00 51.19  ? 447 TYR A CE2 1 
ATOM   2883 C CZ  . TYR A 1 432 ? 7.331   -2.382 16.616  1.00 51.90  ? 447 TYR A CZ  1 
ATOM   2884 O OH  . TYR A 1 432 ? 8.430   -2.992 17.182  1.00 49.11  ? 447 TYR A OH  1 
ATOM   2885 N N   . VAL A 1 433 ? 3.261   2.543  13.668  1.00 49.33  ? 448 VAL A N   1 
ATOM   2886 C CA  . VAL A 1 433 ? 2.482   3.427  12.805  1.00 50.50  ? 448 VAL A CA  1 
ATOM   2887 C C   . VAL A 1 433 ? 2.888   3.206  11.352  1.00 51.79  ? 448 VAL A C   1 
ATOM   2888 O O   . VAL A 1 433 ? 4.081   3.159  11.029  1.00 48.17  ? 448 VAL A O   1 
ATOM   2889 C CB  . VAL A 1 433 ? 2.646   4.907  13.199  1.00 49.04  ? 448 VAL A CB  1 
ATOM   2890 C CG1 . VAL A 1 433 ? 4.099   5.336  13.095  1.00 47.59  ? 448 VAL A CG1 1 
ATOM   2891 C CG2 . VAL A 1 433 ? 1.759   5.787  12.328  1.00 51.09  ? 448 VAL A CG2 1 
ATOM   2892 N N   . CYS A 1 434 ? 1.889   3.084  10.480  1.00 51.73  ? 449 CYS A N   1 
ATOM   2893 C CA  . CYS A 1 434 ? 2.097   2.829  9.057   1.00 47.57  ? 449 CYS A CA  1 
ATOM   2894 C C   . CYS A 1 434 ? 2.001   4.157  8.315   1.00 51.50  ? 449 CYS A C   1 
ATOM   2895 O O   . CYS A 1 434 ? 0.899   4.637  8.040   1.00 52.33  ? 449 CYS A O   1 
ATOM   2896 C CB  . CYS A 1 434 ? 1.059   1.845  8.531   1.00 51.70  ? 449 CYS A CB  1 
ATOM   2897 S SG  . CYS A 1 434 ? 1.454   1.266  6.869   1.00 63.27  ? 449 CYS A SG  1 
ATOM   2898 N N   . ASN A 1 435 ? 3.147   4.751  7.980   1.00 50.91  ? 450 ASN A N   1 
ATOM   2899 C CA  . ASN A 1 435 ? 3.142   6.044  7.301   1.00 57.83  ? 450 ASN A CA  1 
ATOM   2900 C C   . ASN A 1 435 ? 3.287   5.947  5.786   1.00 59.39  ? 450 ASN A C   1 
ATOM   2901 O O   . ASN A 1 435 ? 3.283   6.985  5.117   1.00 62.89  ? 450 ASN A O   1 
ATOM   2902 C CB  . ASN A 1 435 ? 4.242   6.963  7.848   1.00 52.78  ? 450 ASN A CB  1 
ATOM   2903 C CG  . ASN A 1 435 ? 4.294   6.983  9.359   1.00 58.69  ? 450 ASN A CG  1 
ATOM   2904 O OD1 . ASN A 1 435 ? 5.077   6.260  9.972   1.00 61.20  ? 450 ASN A OD1 1 
ATOM   2905 N ND2 . ASN A 1 435 ? 3.444   7.801  9.970   1.00 59.69  ? 450 ASN A ND2 1 
ATOM   2906 N N   . CYS A 1 436 ? 3.402   4.747  5.224   1.00 60.90  ? 451 CYS A N   1 
ATOM   2907 C CA  . CYS A 1 436 ? 3.623   4.600  3.784   1.00 64.43  ? 451 CYS A CA  1 
ATOM   2908 C C   . CYS A 1 436 ? 2.319   4.197  3.094   1.00 63.63  ? 451 CYS A C   1 
ATOM   2909 O O   . CYS A 1 436 ? 2.181   3.123  2.509   1.00 66.48  ? 451 CYS A O   1 
ATOM   2910 C CB  . CYS A 1 436 ? 4.737   3.593  3.521   1.00 57.75  ? 451 CYS A CB  1 
ATOM   2911 S SG  . CYS A 1 436 ? 4.410   1.945  4.166   1.00 67.61  ? 451 CYS A SG  1 
ATOM   2912 N N   . VAL A 1 437 ? 1.343   5.102  3.166   1.00 54.83  ? 452 VAL A N   1 
ATOM   2913 C CA  . VAL A 1 437 ? 0.012   4.834  2.641   1.00 57.25  ? 452 VAL A CA  1 
ATOM   2914 C C   . VAL A 1 437 ? -0.561  6.132  2.094   1.00 55.93  ? 452 VAL A C   1 
ATOM   2915 O O   . VAL A 1 437 ? -0.099  7.227  2.421   1.00 53.91  ? 452 VAL A O   1 
ATOM   2916 C CB  . VAL A 1 437 ? -0.915  4.221  3.722   1.00 60.03  ? 452 VAL A CB  1 
ATOM   2917 C CG1 . VAL A 1 437 ? -1.552  5.313  4.576   1.00 56.93  ? 452 VAL A CG1 1 
ATOM   2918 C CG2 . VAL A 1 437 ? -1.974  3.327  3.082   1.00 62.73  ? 452 VAL A CG2 1 
ATOM   2919 N N   . GLU A 1 438 ? -1.565  6.000  1.228   1.00 54.37  ? 453 GLU A N   1 
ATOM   2920 C CA  . GLU A 1 438 ? -2.269  7.170  0.722   1.00 57.65  ? 453 GLU A CA  1 
ATOM   2921 C C   . GLU A 1 438 ? -3.100  7.795  1.835   1.00 56.72  ? 453 GLU A C   1 
ATOM   2922 O O   . GLU A 1 438 ? -3.916  7.122  2.473   1.00 52.51  ? 453 GLU A O   1 
ATOM   2923 C CB  . GLU A 1 438 ? -3.169  6.797  -0.457  1.00 54.31  ? 453 GLU A CB  1 
ATOM   2924 C CG  . GLU A 1 438 ? -4.129  7.915  -0.863  1.00 60.83  ? 453 GLU A CG  1 
ATOM   2925 C CD  . GLU A 1 438 ? -5.214  7.458  -1.820  1.00 65.77  ? 453 GLU A CD  1 
ATOM   2926 O OE1 . GLU A 1 438 ? -6.157  6.768  -1.368  1.00 64.77  ? 453 GLU A OE1 1 
ATOM   2927 O OE2 . GLU A 1 438 ? -5.128  7.802  -3.021  1.00 64.22  ? 453 GLU A OE2 1 
ATOM   2928 N N   . LYS A 1 439 ? -2.888  9.084  2.069   1.00 51.89  ? 454 LYS A N   1 
ATOM   2929 C CA  . LYS A 1 439 ? -3.651  9.841  3.047   1.00 59.01  ? 454 LYS A CA  1 
ATOM   2930 C C   . LYS A 1 439 ? -4.684  10.693 2.323   1.00 60.77  ? 454 LYS A C   1 
ATOM   2931 O O   . LYS A 1 439 ? -4.370  11.334 1.316   1.00 58.66  ? 454 LYS A O   1 
ATOM   2932 C CB  . LYS A 1 439 ? -2.723  10.702 3.906   1.00 58.61  ? 454 LYS A CB  1 
ATOM   2933 C CG  . LYS A 1 439 ? -2.895  10.448 5.391   1.00 58.03  ? 454 LYS A CG  1 
ATOM   2934 C CD  . LYS A 1 439 ? -1.934  9.384  5.910   1.00 58.54  ? 454 LYS A CD  1 
ATOM   2935 C CE  . LYS A 1 439 ? -2.353  8.947  7.308   1.00 54.75  ? 454 LYS A CE  1 
ATOM   2936 N NZ  . LYS A 1 439 ? -1.540  7.840  7.863   1.00 55.14  ? 454 LYS A NZ  1 
ATOM   2937 N N   . ARG A 1 440 ? -5.920  10.672 2.821   1.00 60.83  ? 455 ARG A N   1 
ATOM   2938 C CA  . ARG A 1 440 ? -7.031  11.370 2.186   1.00 61.95  ? 455 ARG A CA  1 
ATOM   2939 C C   . ARG A 1 440 ? -7.524  12.559 3.000   1.00 62.62  ? 455 ARG A C   1 
ATOM   2940 O O   . ARG A 1 440 ? -8.604  13.086 2.718   1.00 62.54  ? 455 ARG A O   1 
ATOM   2941 C CB  . ARG A 1 440 ? -8.185  10.400 1.922   1.00 62.03  ? 455 ARG A CB  1 
ATOM   2942 C CG  . ARG A 1 440 ? -7.739  9.032  1.429   1.00 62.84  ? 455 ARG A CG  1 
ATOM   2943 C CD  . ARG A 1 440 ? -8.919  8.110  1.154   1.00 60.00  ? 455 ARG A CD  1 
ATOM   2944 N NE  . ARG A 1 440 ? -8.786  7.449  -0.140  1.00 65.52  ? 455 ARG A NE  1 
ATOM   2945 C CZ  . ARG A 1 440 ? -9.779  6.854  -0.786  1.00 63.70  ? 455 ARG A CZ  1 
ATOM   2946 N NH1 . ARG A 1 440 ? -11.000 6.799  -0.278  1.00 58.58  ? 455 ARG A NH1 1 
ATOM   2947 N NH2 . ARG A 1 440 ? -9.540  6.298  -1.971  1.00 64.47  ? 455 ARG A NH2 1 
ATOM   2948 N N   . ALA A 1 441 ? -6.760  12.992 3.999   1.00 60.17  ? 456 ALA A N   1 
ATOM   2949 C CA  . ALA A 1 441 ? -7.113  14.162 4.787   1.00 60.49  ? 456 ALA A CA  1 
ATOM   2950 C C   . ALA A 1 441 ? -5.833  14.836 5.252   1.00 57.79  ? 456 ALA A C   1 
ATOM   2951 O O   . ALA A 1 441 ? -4.760  14.227 5.277   1.00 62.27  ? 456 ALA A O   1 
ATOM   2952 C CB  . ALA A 1 441 ? -8.004  13.795 5.982   1.00 58.57  ? 456 ALA A CB  1 
ATOM   2953 N N   . GLU A 1 442 ? -5.955  16.110 5.615   1.00 57.25  ? 457 GLU A N   1 
ATOM   2954 C CA  . GLU A 1 442 ? -4.804  16.899 6.028   1.00 56.32  ? 457 GLU A CA  1 
ATOM   2955 C C   . GLU A 1 442 ? -5.266  17.988 6.985   1.00 59.95  ? 457 GLU A C   1 
ATOM   2956 O O   . GLU A 1 442 ? -6.462  18.252 7.134   1.00 57.20  ? 457 GLU A O   1 
ATOM   2957 C CB  . GLU A 1 442 ? -4.082  17.502 4.818   1.00 61.60  ? 457 GLU A CB  1 
ATOM   2958 N N   . ILE A 1 443 ? -4.295  18.624 7.634   1.00 61.14  ? 458 ILE A N   1 
ATOM   2959 C CA  . ILE A 1 443 ? -4.550  19.691 8.593   1.00 65.14  ? 458 ILE A CA  1 
ATOM   2960 C C   . ILE A 1 443 ? -4.290  21.025 7.903   1.00 67.19  ? 458 ILE A C   1 
ATOM   2961 O O   . ILE A 1 443 ? -3.146  21.351 7.567   1.00 64.14  ? 458 ILE A O   1 
ATOM   2962 C CB  . ILE A 1 443 ? -3.687  19.542 9.854   1.00 61.15  ? 458 ILE A CB  1 
ATOM   2963 C CG1 . ILE A 1 443 ? -3.828  18.138 10.444  1.00 55.04  ? 458 ILE A CG1 1 
ATOM   2964 C CG2 . ILE A 1 443 ? -4.062  20.599 10.880  1.00 54.39  ? 458 ILE A CG2 1 
ATOM   2965 C CD1 . ILE A 1 443 ? -3.134  17.971 11.786  1.00 47.84  ? 458 ILE A CD1 1 
ATOM   2966 N N   . LYS A 1 444 ? -5.351  21.802 7.697   1.00 63.71  ? 459 LYS A N   1 
ATOM   2967 C CA  . LYS A 1 444 ? -5.228  23.158 7.179   1.00 66.46  ? 459 LYS A CA  1 
ATOM   2968 C C   . LYS A 1 444 ? -4.829  24.088 8.326   1.00 71.01  ? 459 LYS A C   1 
ATOM   2969 O O   . LYS A 1 444 ? -4.399  23.644 9.394   1.00 71.20  ? 459 LYS A O   1 
ATOM   2970 C CB  . LYS A 1 444 ? -6.529  23.585 6.503   1.00 60.45  ? 459 LYS A CB  1 
ATOM   2971 N N   . GLU A 1 445 ? -4.970  25.395 8.123   1.00 71.18  ? 460 GLU A N   1 
ATOM   2972 C CA  . GLU A 1 445 ? -4.593  26.341 9.161   1.00 68.01  ? 460 GLU A CA  1 
ATOM   2973 C C   . GLU A 1 445 ? -5.637  26.366 10.272  1.00 69.70  ? 460 GLU A C   1 
ATOM   2974 O O   . GLU A 1 445 ? -6.773  25.910 10.110  1.00 67.09  ? 460 GLU A O   1 
ATOM   2975 C CB  . GLU A 1 445 ? -4.409  27.745 8.586   1.00 73.00  ? 460 GLU A CB  1 
ATOM   2976 C CG  . GLU A 1 445 ? -3.035  27.988 7.988   1.00 78.02  ? 460 GLU A CG  1 
ATOM   2977 C CD  . GLU A 1 445 ? -3.065  28.030 6.475   1.00 87.07  ? 460 GLU A CD  1 
ATOM   2978 O OE1 . GLU A 1 445 ? -3.668  27.118 5.867   1.00 83.48  ? 460 GLU A OE1 1 
ATOM   2979 O OE2 . GLU A 1 445 ? -2.484  28.972 5.895   1.00 92.46  ? 460 GLU A OE2 1 
ATOM   2980 N N   . ASN A 1 446 ? -5.227  26.917 11.417  1.00 68.39  ? 461 ASN A N   1 
ATOM   2981 C CA  . ASN A 1 446 ? -6.037  26.930 12.633  1.00 62.79  ? 461 ASN A CA  1 
ATOM   2982 C C   . ASN A 1 446 ? -6.429  25.517 13.059  1.00 59.64  ? 461 ASN A C   1 
ATOM   2983 O O   . ASN A 1 446 ? -7.512  25.305 13.607  1.00 61.26  ? 461 ASN A O   1 
ATOM   2984 C CB  . ASN A 1 446 ? -7.282  27.809 12.469  1.00 70.76  ? 461 ASN A CB  1 
ATOM   2985 N N   . ASN A 1 447 ? -5.547  24.547 12.790  1.00 61.86  ? 462 ASN A N   1 
ATOM   2986 C CA  . ASN A 1 447 ? -5.698  23.163 13.252  1.00 57.99  ? 462 ASN A CA  1 
ATOM   2987 C C   . ASN A 1 447 ? -6.949  22.504 12.677  1.00 55.13  ? 462 ASN A C   1 
ATOM   2988 O O   . ASN A 1 447 ? -7.601  21.687 13.332  1.00 55.39  ? 462 ASN A O   1 
ATOM   2989 C CB  . ASN A 1 447 ? -5.706  23.086 14.781  1.00 47.49  ? 462 ASN A CB  1 
ATOM   2990 C CG  . ASN A 1 447 ? -4.504  23.755 15.404  1.00 48.84  ? 462 ASN A CG  1 
ATOM   2991 O OD1 . ASN A 1 447 ? -3.363  23.445 15.068  1.00 52.03  ? 462 ASN A OD1 1 
ATOM   2992 N ND2 . ASN A 1 447 ? -4.751  24.674 16.329  1.00 53.12  ? 462 ASN A ND2 1 
ATOM   2993 N N   . GLN A 1 448 ? -7.286  22.845 11.440  1.00 59.40  ? 463 GLN A N   1 
ATOM   2994 C CA  . GLN A 1 448 ? -8.511  22.368 10.810  1.00 63.42  ? 463 GLN A CA  1 
ATOM   2995 C C   . GLN A 1 448 ? -8.194  21.128 9.980   1.00 62.78  ? 463 GLN A C   1 
ATOM   2996 O O   . GLN A 1 448 ? -7.452  21.204 8.996   1.00 63.67  ? 463 GLN A O   1 
ATOM   2997 C CB  . GLN A 1 448 ? -9.139  23.470 9.962   1.00 61.60  ? 463 GLN A CB  1 
ATOM   2998 C CG  . GLN A 1 448 ? -9.784  24.580 10.786  1.00 62.48  ? 463 GLN A CG  1 
ATOM   2999 C CD  . GLN A 1 448 ? -10.520 24.058 12.015  1.00 63.93  ? 463 GLN A CD  1 
ATOM   3000 O OE1 . GLN A 1 448 ? -9.939  23.923 13.096  1.00 61.97  ? 463 GLN A OE1 1 
ATOM   3001 N NE2 . GLN A 1 448 ? -11.806 23.759 11.852  1.00 65.11  ? 463 GLN A NE2 1 
ATOM   3002 N N   . VAL A 1 449 ? -8.758  19.991 10.380  1.00 57.07  ? 464 VAL A N   1 
ATOM   3003 C CA  . VAL A 1 449 ? -8.561  18.731 9.670   1.00 58.17  ? 464 VAL A CA  1 
ATOM   3004 C C   . VAL A 1 449 ? -9.558  18.679 8.519   1.00 56.85  ? 464 VAL A C   1 
ATOM   3005 O O   . VAL A 1 449 ? -10.768 18.593 8.738   1.00 54.93  ? 464 VAL A O   1 
ATOM   3006 C CB  . VAL A 1 449 ? -8.728  17.525 10.602  1.00 58.95  ? 464 VAL A CB  1 
ATOM   3007 C CG1 . VAL A 1 449 ? -8.547  16.224 9.824   1.00 56.04  ? 464 VAL A CG1 1 
ATOM   3008 C CG2 . VAL A 1 449 ? -7.745  17.607 11.766  1.00 53.87  ? 464 VAL A CG2 1 
ATOM   3009 N N   . VAL A 1 450 ? -9.051  18.719 7.289   1.00 60.07  ? 465 VAL A N   1 
ATOM   3010 C CA  . VAL A 1 450 ? -9.896  18.797 6.106   1.00 61.26  ? 465 VAL A CA  1 
ATOM   3011 C C   . VAL A 1 450 ? -9.541  17.665 5.155   1.00 65.70  ? 465 VAL A C   1 
ATOM   3012 O O   . VAL A 1 450 ? -8.382  17.249 5.056   1.00 67.77  ? 465 VAL A O   1 
ATOM   3013 C CB  . VAL A 1 450 ? -9.759  20.161 5.397   1.00 62.26  ? 465 VAL A CB  1 
ATOM   3014 C CG1 . VAL A 1 450 ? -10.446 21.246 6.207   1.00 60.09  ? 465 VAL A CG1 1 
ATOM   3015 C CG2 . VAL A 1 450 ? -8.290  20.498 5.165   1.00 56.24  ? 465 VAL A CG2 1 
ATOM   3016 N N   . ILE A 1 451 ? -10.559 17.163 4.454   1.00 66.07  ? 466 ILE A N   1 
ATOM   3017 C CA  . ILE A 1 451 ? -10.347 16.161 3.417   1.00 66.80  ? 466 ILE A CA  1 
ATOM   3018 C C   . ILE A 1 451 ? -9.581  16.793 2.264   1.00 66.15  ? 466 ILE A C   1 
ATOM   3019 O O   . ILE A 1 451 ? -9.888  17.914 1.838   1.00 64.81  ? 466 ILE A O   1 
ATOM   3020 C CB  . ILE A 1 451 ? -11.691 15.583 2.948   1.00 61.74  ? 466 ILE A CB  1 
ATOM   3021 C CG1 . ILE A 1 451 ? -12.320 14.739 4.057   1.00 61.53  ? 466 ILE A CG1 1 
ATOM   3022 C CG2 . ILE A 1 451 ? -11.515 14.767 1.675   1.00 66.73  ? 466 ILE A CG2 1 
ATOM   3023 C CD1 . ILE A 1 451 ? -13.672 14.168 3.698   1.00 67.34  ? 466 ILE A CD1 1 
ATOM   3024 N N   . LYS A 1 452 ? -8.568  16.086 1.763   1.00 70.44  ? 467 LYS A N   1 
ATOM   3025 C CA  . LYS A 1 452 ? -7.783  16.603 0.650   1.00 74.11  ? 467 LYS A CA  1 
ATOM   3026 C C   . LYS A 1 452 ? -8.669  16.842 -0.568  1.00 74.50  ? 467 LYS A C   1 
ATOM   3027 O O   . LYS A 1 452 ? -9.745  16.250 -0.710  1.00 72.08  ? 467 LYS A O   1 
ATOM   3028 C CB  . LYS A 1 452 ? -6.649  15.641 0.302   1.00 68.37  ? 467 LYS A CB  1 
ATOM   3029 C CG  . LYS A 1 452 ? -5.623  15.500 1.410   1.00 65.03  ? 467 LYS A CG  1 
ATOM   3030 C CD  . LYS A 1 452 ? -4.736  14.300 1.179   1.00 63.78  ? 467 LYS A CD  1 
ATOM   3031 C CE  . LYS A 1 452 ? -3.262  14.643 1.263   1.00 66.80  ? 467 LYS A CE  1 
ATOM   3032 N NZ  . LYS A 1 452 ? -2.535  13.653 2.105   1.00 66.91  ? 467 LYS A NZ  1 
ATOM   3033 N N   . GLU A 1 453 ? -8.203  17.732 -1.448  1.00 72.76  ? 468 GLU A N   1 
ATOM   3034 C CA  . GLU A 1 453 ? -9.027  18.179 -2.568  1.00 80.80  ? 468 GLU A CA  1 
ATOM   3035 C C   . GLU A 1 453 ? -9.389  17.024 -3.495  1.00 83.03  ? 468 GLU A C   1 
ATOM   3036 O O   . GLU A 1 453 ? -10.514 16.959 -4.007  1.00 79.53  ? 468 GLU A O   1 
ATOM   3037 C CB  . GLU A 1 453 ? -8.301  19.279 -3.340  1.00 82.35  ? 468 GLU A CB  1 
ATOM   3038 N N   . GLU A 1 454 ? -8.452  16.095 -3.709  1.00 79.23  ? 469 GLU A N   1 
ATOM   3039 C CA  . GLU A 1 454 ? -8.673  14.986 -4.631  1.00 72.23  ? 469 GLU A CA  1 
ATOM   3040 C C   . GLU A 1 454 ? -9.862  14.121 -4.235  1.00 74.58  ? 469 GLU A C   1 
ATOM   3041 O O   . GLU A 1 454 ? -10.434 13.441 -5.095  1.00 78.97  ? 469 GLU A O   1 
ATOM   3042 C CB  . GLU A 1 454 ? -7.413  14.123 -4.710  1.00 74.01  ? 469 GLU A CB  1 
ATOM   3043 C CG  . GLU A 1 454 ? -6.173  14.884 -5.152  1.00 79.92  ? 469 GLU A CG  1 
ATOM   3044 C CD  . GLU A 1 454 ? -4.937  14.013 -5.169  1.00 90.20  ? 469 GLU A CD  1 
ATOM   3045 O OE1 . GLU A 1 454 ? -3.816  14.567 -5.148  1.00 93.29  ? 469 GLU A OE1 1 
ATOM   3046 O OE2 . GLU A 1 454 ? -5.088  12.772 -5.200  1.00 91.58  ? 469 GLU A OE2 1 
ATOM   3047 N N   . PHE A 1 455 ? -10.244 14.126 -2.959  1.00 77.44  ? 470 PHE A N   1 
ATOM   3048 C CA  . PHE A 1 455 ? -11.339 13.303 -2.469  1.00 77.70  ? 470 PHE A CA  1 
ATOM   3049 C C   . PHE A 1 455 ? -12.483 14.123 -1.894  1.00 80.96  ? 470 PHE A C   1 
ATOM   3050 O O   . PHE A 1 455 ? -13.458 13.536 -1.409  1.00 83.11  ? 470 PHE A O   1 
ATOM   3051 C CB  . PHE A 1 455 ? -10.842 12.315 -1.398  1.00 74.22  ? 470 PHE A CB  1 
ATOM   3052 C CG  . PHE A 1 455 ? -9.598  11.560 -1.788  1.00 70.84  ? 470 PHE A CG  1 
ATOM   3053 C CD1 . PHE A 1 455 ? -8.344  12.136 -1.645  1.00 68.54  ? 470 PHE A CD1 1 
ATOM   3054 C CD2 . PHE A 1 455 ? -9.684  10.272 -2.291  1.00 69.38  ? 470 PHE A CD2 1 
ATOM   3055 C CE1 . PHE A 1 455 ? -7.203  11.444 -2.006  1.00 69.87  ? 470 PHE A CE1 1 
ATOM   3056 C CE2 . PHE A 1 455 ? -8.546  9.575  -2.650  1.00 65.63  ? 470 PHE A CE2 1 
ATOM   3057 C CZ  . PHE A 1 455 ? -7.305  10.162 -2.508  1.00 67.06  ? 470 PHE A CZ  1 
ATOM   3058 N N   . ARG A 1 456 ? -12.390 15.456 -1.926  1.00 82.95  ? 471 ARG A N   1 
ATOM   3059 C CA  . ARG A 1 456 ? -13.430 16.295 -1.335  1.00 83.05  ? 471 ARG A CA  1 
ATOM   3060 C C   . ARG A 1 456 ? -14.779 16.045 -1.996  1.00 85.93  ? 471 ARG A C   1 
ATOM   3061 O O   . ARG A 1 456 ? -15.787 15.828 -1.314  1.00 87.29  ? 471 ARG A O   1 
ATOM   3062 C CB  . ARG A 1 456 ? -13.039 17.771 -1.442  1.00 78.35  ? 471 ARG A CB  1 
ATOM   3063 N N   . ASP A 1 457 ? -14.815 16.068 -3.333  1.00 88.21  ? 472 ASP A N   1 
ATOM   3064 C CA  . ASP A 1 457 ? -16.056 15.777 -4.044  1.00 90.23  ? 472 ASP A CA  1 
ATOM   3065 C C   . ASP A 1 457 ? -16.503 14.341 -3.800  1.00 91.63  ? 472 ASP A C   1 
ATOM   3066 O O   . ASP A 1 457 ? -17.700 14.075 -3.631  1.00 88.17  ? 472 ASP A O   1 
ATOM   3067 C CB  . ASP A 1 457 ? -15.881 16.040 -5.541  1.00 89.05  ? 472 ASP A CB  1 
ATOM   3068 N N   . TYR A 1 458 ? -15.552 13.404 -3.760  1.00 90.25  ? 473 TYR A N   1 
ATOM   3069 C CA  . TYR A 1 458 ? -15.868 12.001 -3.520  1.00 86.59  ? 473 TYR A CA  1 
ATOM   3070 C C   . TYR A 1 458 ? -16.393 11.742 -2.113  1.00 90.81  ? 473 TYR A C   1 
ATOM   3071 O O   . TYR A 1 458 ? -16.879 10.638 -1.847  1.00 92.67  ? 473 TYR A O   1 
ATOM   3072 C CB  . TYR A 1 458 ? -14.633 11.135 -3.780  1.00 77.68  ? 473 TYR A CB  1 
ATOM   3073 N N   . TYR A 1 459 ? -16.311 12.719 -1.215  1.00 89.93  ? 474 TYR A N   1 
ATOM   3074 C CA  . TYR A 1 459 ? -16.809 12.549 0.145   1.00 90.94  ? 474 TYR A CA  1 
ATOM   3075 C C   . TYR A 1 459 ? -17.697 13.721 0.550   1.00 91.55  ? 474 TYR A C   1 
ATOM   3076 O O   . TYR A 1 459 ? -18.190 13.777 1.677   1.00 88.61  ? 474 TYR A O   1 
ATOM   3077 C CB  . TYR A 1 459 ? -15.646 12.402 1.131   1.00 85.01  ? 474 TYR A CB  1 
ATOM   3078 N N   . GLN B 2 1   ? -34.515 57.487 52.328  1.00 67.70  ? 1   GLN B N   1 
ATOM   3079 C CA  . GLN B 2 1   ? -35.324 58.331 53.201  1.00 70.76  ? 1   GLN B CA  1 
ATOM   3080 C C   . GLN B 2 1   ? -36.603 57.619 53.644  1.00 60.00  ? 1   GLN B C   1 
ATOM   3081 O O   . GLN B 2 1   ? -37.650 58.249 53.789  1.00 64.69  ? 1   GLN B O   1 
ATOM   3082 C CB  . GLN B 2 1   ? -35.680 59.642 52.492  1.00 61.40  ? 1   GLN B CB  1 
ATOM   3083 N N   . LEU B 2 2   ? -36.512 56.308 53.862  1.00 56.12  ? 2   LEU B N   1 
ATOM   3084 C CA  . LEU B 2 2   ? -37.708 55.498 54.066  1.00 59.50  ? 2   LEU B CA  1 
ATOM   3085 C C   . LEU B 2 2   ? -38.404 55.842 55.378  1.00 56.73  ? 2   LEU B C   1 
ATOM   3086 O O   . LEU B 2 2   ? -37.794 55.801 56.452  1.00 57.43  ? 2   LEU B O   1 
ATOM   3087 C CB  . LEU B 2 2   ? -37.361 54.011 54.042  1.00 54.11  ? 2   LEU B CB  1 
ATOM   3088 C CG  . LEU B 2 2   ? -38.613 53.129 54.051  1.00 48.33  ? 2   LEU B CG  1 
ATOM   3089 C CD1 . LEU B 2 2   ? -39.389 53.294 52.750  1.00 47.81  ? 2   LEU B CD1 1 
ATOM   3090 C CD2 . LEU B 2 2   ? -38.267 51.671 54.298  1.00 46.14  ? 2   LEU B CD2 1 
ATOM   3091 N N   . GLN B 2 3   ? -39.692 56.160 55.287  1.00 48.99  ? 3   GLN B N   1 
ATOM   3092 C CA  . GLN B 2 3   ? -40.519 56.416 56.455  1.00 53.91  ? 3   GLN B CA  1 
ATOM   3093 C C   . GLN B 2 3   ? -41.904 55.834 56.222  1.00 49.70  ? 3   GLN B C   1 
ATOM   3094 O O   . GLN B 2 3   ? -42.433 55.892 55.109  1.00 50.31  ? 3   GLN B O   1 
ATOM   3095 C CB  . GLN B 2 3   ? -40.611 57.916 56.762  1.00 56.32  ? 3   GLN B CB  1 
ATOM   3096 C CG  . GLN B 2 3   ? -39.465 58.420 57.631  1.00 60.63  ? 3   GLN B CG  1 
ATOM   3097 C CD  . GLN B 2 3   ? -39.580 59.895 57.963  1.00 71.20  ? 3   GLN B CD  1 
ATOM   3098 O OE1 . GLN B 2 3   ? -39.387 60.753 57.102  1.00 77.62  ? 3   GLN B OE1 1 
ATOM   3099 N NE2 . GLN B 2 3   ? -39.888 60.198 59.220  1.00 74.21  ? 3   GLN B NE2 1 
ATOM   3100 N N   . LEU B 2 4   ? -42.478 55.266 57.280  1.00 46.61  ? 4   LEU B N   1 
ATOM   3101 C CA  . LEU B 2 4   ? -43.805 54.669 57.261  1.00 45.03  ? 4   LEU B CA  1 
ATOM   3102 C C   . LEU B 2 4   ? -44.699 55.444 58.212  1.00 43.71  ? 4   LEU B C   1 
ATOM   3103 O O   . LEU B 2 4   ? -44.282 55.782 59.324  1.00 43.21  ? 4   LEU B O   1 
ATOM   3104 C CB  . LEU B 2 4   ? -43.764 53.199 57.691  1.00 43.10  ? 4   LEU B CB  1 
ATOM   3105 C CG  . LEU B 2 4   ? -43.103 52.167 56.783  1.00 44.33  ? 4   LEU B CG  1 
ATOM   3106 C CD1 . LEU B 2 4   ? -41.606 52.128 57.035  1.00 43.87  ? 4   LEU B CD1 1 
ATOM   3107 C CD2 . LEU B 2 4   ? -43.720 50.797 57.027  1.00 41.21  ? 4   LEU B CD2 1 
ATOM   3108 N N   . GLN B 2 5   ? -45.932 55.715 57.785  1.00 49.90  ? 5   GLN B N   1 
ATOM   3109 C CA  . GLN B 2 5   ? -46.876 56.495 58.583  1.00 51.15  ? 5   GLN B CA  1 
ATOM   3110 C C   . GLN B 2 5   ? -48.211 55.768 58.650  1.00 46.95  ? 5   GLN B C   1 
ATOM   3111 O O   . GLN B 2 5   ? -48.916 55.659 57.639  1.00 44.14  ? 5   GLN B O   1 
ATOM   3112 C CB  . GLN B 2 5   ? -47.056 57.900 58.009  1.00 52.21  ? 5   GLN B CB  1 
ATOM   3113 C CG  . GLN B 2 5   ? -47.250 58.969 59.070  1.00 65.31  ? 5   GLN B CG  1 
ATOM   3114 C CD  . GLN B 2 5   ? -46.632 60.297 58.680  1.00 76.66  ? 5   GLN B CD  1 
ATOM   3115 O OE1 . GLN B 2 5   ? -46.497 60.609 57.495  1.00 80.59  ? 5   GLN B OE1 1 
ATOM   3116 N NE2 . GLN B 2 5   ? -46.249 61.086 59.677  1.00 78.84  ? 5   GLN B NE2 1 
ATOM   3117 N N   . GLU B 2 6   ? -48.556 55.279 59.839  1.00 41.79  ? 6   GLU B N   1 
ATOM   3118 C CA  . GLU B 2 6   ? -49.883 54.734 60.074  1.00 42.39  ? 6   GLU B CA  1 
ATOM   3119 C C   . GLU B 2 6   ? -50.920 55.855 60.114  1.00 41.14  ? 6   GLU B C   1 
ATOM   3120 O O   . GLU B 2 6   ? -50.621 56.999 60.465  1.00 43.08  ? 6   GLU B O   1 
ATOM   3121 C CB  . GLU B 2 6   ? -49.913 53.954 61.391  1.00 43.51  ? 6   GLU B CB  1 
ATOM   3122 C CG  . GLU B 2 6   ? -48.951 52.775 61.460  1.00 44.38  ? 6   GLU B CG  1 
ATOM   3123 C CD  . GLU B 2 6   ? -47.628 53.131 62.125  1.00 43.54  ? 6   GLU B CD  1 
ATOM   3124 O OE1 . GLU B 2 6   ? -47.228 54.318 62.093  1.00 43.06  ? 6   GLU B OE1 1 
ATOM   3125 O OE2 . GLU B 2 6   ? -46.981 52.217 62.676  1.00 44.21  ? 6   GLU B OE2 1 
ATOM   3126 N N   . SER B 2 7   ? -52.151 55.521 59.744  1.00 40.50  ? 7   SER B N   1 
ATOM   3127 C CA  . SER B 2 7   ? -53.241 56.457 59.947  1.00 44.37  ? 7   SER B CA  1 
ATOM   3128 C C   . SER B 2 7   ? -53.468 56.675 61.450  1.00 50.64  ? 7   SER B C   1 
ATOM   3129 O O   . SER B 2 7   ? -52.931 55.957 62.302  1.00 46.54  ? 7   SER B O   1 
ATOM   3130 C CB  . SER B 2 7   ? -54.498 55.961 59.231  1.00 42.19  ? 7   SER B CB  1 
ATOM   3131 O OG  . SER B 2 7   ? -54.943 54.731 59.762  1.00 40.05  ? 7   SER B OG  1 
ATOM   3132 N N   . GLY B 2 8   ? -54.261 57.699 61.772  1.00 47.85  ? 8   GLY B N   1 
ATOM   3133 C CA  . GLY B 2 8   ? -54.348 58.219 63.121  1.00 43.11  ? 8   GLY B CA  1 
ATOM   3134 C C   . GLY B 2 8   ? -55.015 57.296 64.125  1.00 48.76  ? 8   GLY B C   1 
ATOM   3135 O O   . GLY B 2 8   ? -55.744 56.364 63.772  1.00 50.16  ? 8   GLY B O   1 
ATOM   3136 N N   . PRO B 2 9   ? -54.776 57.556 65.408  1.00 50.66  ? 9   PRO B N   1 
ATOM   3137 C CA  . PRO B 2 9   ? -55.367 56.728 66.464  1.00 50.52  ? 9   PRO B CA  1 
ATOM   3138 C C   . PRO B 2 9   ? -56.828 57.071 66.692  1.00 51.95  ? 9   PRO B C   1 
ATOM   3139 O O   . PRO B 2 9   ? -57.268 58.200 66.459  1.00 52.87  ? 9   PRO B O   1 
ATOM   3140 C CB  . PRO B 2 9   ? -54.524 57.085 67.693  1.00 43.29  ? 9   PRO B CB  1 
ATOM   3141 C CG  . PRO B 2 9   ? -54.142 58.517 67.452  1.00 42.94  ? 9   PRO B CG  1 
ATOM   3142 C CD  . PRO B 2 9   ? -53.955 58.653 65.956  1.00 47.25  ? 9   PRO B CD  1 
ATOM   3143 N N   . GLY B 2 10  ? -57.580 56.081 67.162  1.00 51.40  ? 10  GLY B N   1 
ATOM   3144 C CA  . GLY B 2 10  ? -58.989 56.307 67.423  1.00 51.17  ? 10  GLY B CA  1 
ATOM   3145 C C   . GLY B 2 10  ? -59.712 55.086 67.947  1.00 45.77  ? 10  GLY B C   1 
ATOM   3146 O O   . GLY B 2 10  ? -59.106 54.138 68.447  1.00 47.62  ? 10  GLY B O   1 
ATOM   3147 N N   . LEU B 2 11  ? -61.032 55.135 67.818  1.00 49.55  ? 11  LEU B N   1 
ATOM   3148 C CA  . LEU B 2 11  ? -61.941 54.146 68.369  1.00 44.65  ? 11  LEU B CA  1 
ATOM   3149 C C   . LEU B 2 11  ? -62.445 53.203 67.283  1.00 45.64  ? 11  LEU B C   1 
ATOM   3150 O O   . LEU B 2 11  ? -62.553 53.571 66.112  1.00 46.85  ? 11  LEU B O   1 
ATOM   3151 C CB  . LEU B 2 11  ? -63.139 54.833 69.027  1.00 46.66  ? 11  LEU B CB  1 
ATOM   3152 C CG  . LEU B 2 11  ? -62.922 55.646 70.298  1.00 49.46  ? 11  LEU B CG  1 
ATOM   3153 C CD1 . LEU B 2 11  ? -64.043 56.662 70.473  1.00 47.20  ? 11  LEU B CD1 1 
ATOM   3154 C CD2 . LEU B 2 11  ? -62.850 54.715 71.494  1.00 47.71  ? 11  LEU B CD2 1 
ATOM   3155 N N   . VAL B 2 12  ? -62.759 51.975 67.688  1.00 43.98  ? 12  VAL B N   1 
ATOM   3156 C CA  . VAL B 2 12  ? -63.541 51.048 66.879  1.00 40.74  ? 12  VAL B CA  1 
ATOM   3157 C C   . VAL B 2 12  ? -64.583 50.417 67.789  1.00 40.42  ? 12  VAL B C   1 
ATOM   3158 O O   . VAL B 2 12  ? -64.261 49.983 68.901  1.00 38.79  ? 12  VAL B O   1 
ATOM   3159 C CB  . VAL B 2 12  ? -62.675 49.958 66.218  1.00 41.27  ? 12  VAL B CB  1 
ATOM   3160 C CG1 . VAL B 2 12  ? -63.539 49.079 65.318  1.00 39.72  ? 12  VAL B CG1 1 
ATOM   3161 C CG2 . VAL B 2 12  ? -61.541 50.576 65.424  1.00 40.58  ? 12  VAL B CG2 1 
ATOM   3162 N N   . LYS B 2 13  ? -65.818 50.377 67.329  1.00 43.28  ? 13  LYS B N   1 
ATOM   3163 C CA  . LYS B 2 13  ? -66.861 49.793 68.154  1.00 46.26  ? 13  LYS B CA  1 
ATOM   3164 C C   . LYS B 2 13  ? -66.760 48.268 68.140  1.00 43.35  ? 13  LYS B C   1 
ATOM   3165 O O   . LYS B 2 13  ? -66.358 47.672 67.135  1.00 39.71  ? 13  LYS B O   1 
ATOM   3166 C CB  . LYS B 2 13  ? -68.239 50.233 67.664  1.00 45.13  ? 13  LYS B CB  1 
ATOM   3167 C CG  . LYS B 2 13  ? -68.780 51.506 68.332  1.00 47.24  ? 13  LYS B CG  1 
ATOM   3168 C CD  . LYS B 2 13  ? -67.760 52.642 68.346  1.00 55.00  ? 13  LYS B CD  1 
ATOM   3169 C CE  . LYS B 2 13  ? -68.430 53.992 68.570  1.00 52.70  ? 13  LYS B CE  1 
ATOM   3170 N NZ  . LYS B 2 13  ? -67.776 55.085 67.794  1.00 60.48  ? 13  LYS B NZ  1 
ATOM   3171 N N   . PRO B 2 14  ? -67.100 47.618 69.252  1.00 42.28  ? 14  PRO B N   1 
ATOM   3172 C CA  . PRO B 2 14  ? -67.065 46.150 69.290  1.00 40.94  ? 14  PRO B CA  1 
ATOM   3173 C C   . PRO B 2 14  ? -67.875 45.533 68.157  1.00 41.18  ? 14  PRO B C   1 
ATOM   3174 O O   . PRO B 2 14  ? -68.937 46.034 67.782  1.00 40.02  ? 14  PRO B O   1 
ATOM   3175 C CB  . PRO B 2 14  ? -67.668 45.822 70.660  1.00 38.09  ? 14  PRO B CB  1 
ATOM   3176 C CG  . PRO B 2 14  ? -67.367 47.020 71.494  1.00 47.46  ? 14  PRO B CG  1 
ATOM   3177 C CD  . PRO B 2 14  ? -67.421 48.205 70.565  1.00 43.24  ? 14  PRO B CD  1 
ATOM   3178 N N   . SER B 2 15  ? -67.343 44.445 67.600  1.00 41.25  ? 15  SER B N   1 
ATOM   3179 C CA  . SER B 2 15  ? -67.875 43.648 66.498  1.00 38.19  ? 15  SER B CA  1 
ATOM   3180 C C   . SER B 2 15  ? -67.660 44.310 65.136  1.00 37.87  ? 15  SER B C   1 
ATOM   3181 O O   . SER B 2 15  ? -67.881 43.657 64.112  1.00 38.07  ? 15  SER B O   1 
ATOM   3182 C CB  . SER B 2 15  ? -69.372 43.317 66.654  1.00 42.10  ? 15  SER B CB  1 
ATOM   3183 O OG  . SER B 2 15  ? -70.176 44.360 66.128  1.00 40.26  ? 15  SER B OG  1 
ATOM   3184 N N   . GLU B 2 16  ? -67.243 45.572 65.079  1.00 38.13  ? 16  GLU B N   1 
ATOM   3185 C CA  . GLU B 2 16  ? -67.043 46.244 63.808  1.00 40.38  ? 16  GLU B CA  1 
ATOM   3186 C C   . GLU B 2 16  ? -65.633 45.966 63.292  1.00 40.27  ? 16  GLU B C   1 
ATOM   3187 O O   . GLU B 2 16  ? -64.834 45.271 63.928  1.00 37.32  ? 16  GLU B O   1 
ATOM   3188 C CB  . GLU B 2 16  ? -67.312 47.742 63.946  1.00 39.62  ? 16  GLU B CB  1 
ATOM   3189 C CG  . GLU B 2 16  ? -68.586 48.063 64.713  1.00 40.61  ? 16  GLU B CG  1 
ATOM   3190 C CD  . GLU B 2 16  ? -69.270 49.322 64.216  1.00 42.94  ? 16  GLU B CD  1 
ATOM   3191 O OE1 . GLU B 2 16  ? -68.565 50.289 63.843  1.00 41.38  ? 16  GLU B OE1 1 
ATOM   3192 O OE2 . GLU B 2 16  ? -70.520 49.343 64.205  1.00 50.04  ? 16  GLU B OE2 1 
ATOM   3193 N N   . THR B 2 17  ? -65.323 46.524 62.123  1.00 35.06  ? 17  THR B N   1 
ATOM   3194 C CA  . THR B 2 17  ? -64.076 46.246 61.424  1.00 35.81  ? 17  THR B CA  1 
ATOM   3195 C C   . THR B 2 17  ? -63.080 47.375 61.660  1.00 33.41  ? 17  THR B C   1 
ATOM   3196 O O   . THR B 2 17  ? -63.381 48.542 61.394  1.00 35.90  ? 17  THR B O   1 
ATOM   3197 C CB  . THR B 2 17  ? -64.324 46.062 59.928  1.00 35.83  ? 17  THR B CB  1 
ATOM   3198 O OG1 . THR B 2 17  ? -65.132 44.897 59.722  1.00 41.46  ? 17  THR B OG1 1 
ATOM   3199 C CG2 . THR B 2 17  ? -63.003 45.898 59.186  1.00 35.10  ? 17  THR B CG2 1 
ATOM   3200 N N   . LEU B 2 18  ? -61.899 47.022 62.158  1.00 40.67  ? 18  LEU B N   1 
ATOM   3201 C CA  . LEU B 2 18  ? -60.803 47.969 62.267  1.00 41.32  ? 18  LEU B CA  1 
ATOM   3202 C C   . LEU B 2 18  ? -60.163 48.170 60.898  1.00 40.58  ? 18  LEU B C   1 
ATOM   3203 O O   . LEU B 2 18  ? -59.946 47.211 60.151  1.00 41.33  ? 18  LEU B O   1 
ATOM   3204 C CB  . LEU B 2 18  ? -59.763 47.469 63.271  1.00 36.91  ? 18  LEU B CB  1 
ATOM   3205 C CG  . LEU B 2 18  ? -58.385 48.119 63.147  1.00 39.41  ? 18  LEU B CG  1 
ATOM   3206 C CD1 . LEU B 2 18  ? -58.444 49.567 63.590  1.00 43.32  ? 18  LEU B CD1 1 
ATOM   3207 C CD2 . LEU B 2 18  ? -57.344 47.353 63.936  1.00 42.09  ? 18  LEU B CD2 1 
ATOM   3208 N N   . SER B 2 19  ? -59.868 49.428 60.572  1.00 36.30  ? 19  SER B N   1 
ATOM   3209 C CA  . SER B 2 19  ? -59.337 49.808 59.267  1.00 38.24  ? 19  SER B CA  1 
ATOM   3210 C C   . SER B 2 19  ? -58.120 50.704 59.462  1.00 41.31  ? 19  SER B C   1 
ATOM   3211 O O   . SER B 2 19  ? -58.211 51.742 60.127  1.00 37.17  ? 19  SER B O   1 
ATOM   3212 C CB  . SER B 2 19  ? -60.411 50.524 58.443  1.00 34.84  ? 19  SER B CB  1 
ATOM   3213 O OG  . SER B 2 19  ? -60.193 50.372 57.059  1.00 46.17  ? 19  SER B OG  1 
ATOM   3214 N N   . LEU B 2 20  ? -56.986 50.311 58.881  1.00 38.10  ? 20  LEU B N   1 
ATOM   3215 C CA  . LEU B 2 20  ? -55.754 51.079 59.001  1.00 36.95  ? 20  LEU B CA  1 
ATOM   3216 C C   . LEU B 2 20  ? -55.053 51.164 57.655  1.00 37.70  ? 20  LEU B C   1 
ATOM   3217 O O   . LEU B 2 20  ? -55.122 50.241 56.838  1.00 38.67  ? 20  LEU B O   1 
ATOM   3218 C CB  . LEU B 2 20  ? -54.799 50.463 60.028  1.00 35.83  ? 20  LEU B CB  1 
ATOM   3219 C CG  . LEU B 2 20  ? -55.317 50.396 61.465  1.00 44.89  ? 20  LEU B CG  1 
ATOM   3220 C CD1 . LEU B 2 20  ? -54.422 49.491 62.281  1.00 42.87  ? 20  LEU B CD1 1 
ATOM   3221 C CD2 . LEU B 2 20  ? -55.417 51.786 62.095  1.00 39.51  ? 20  LEU B CD2 1 
ATOM   3222 N N   . THR B 2 21  ? -54.358 52.277 57.443  1.00 38.98  ? 21  THR B N   1 
ATOM   3223 C CA  . THR B 2 21  ? -53.542 52.475 56.255  1.00 41.55  ? 21  THR B CA  1 
ATOM   3224 C C   . THR B 2 21  ? -52.151 52.931 56.672  1.00 38.62  ? 21  THR B C   1 
ATOM   3225 O O   . THR B 2 21  ? -51.987 53.666 57.650  1.00 36.49  ? 21  THR B O   1 
ATOM   3226 C CB  . THR B 2 21  ? -54.179 53.499 55.298  1.00 38.91  ? 21  THR B CB  1 
ATOM   3227 O OG1 . THR B 2 21  ? -55.472 53.030 54.904  1.00 41.32  ? 21  THR B OG1 1 
ATOM   3228 C CG2 . THR B 2 21  ? -53.328 53.695 54.043  1.00 36.78  ? 21  THR B CG2 1 
ATOM   3229 N N   . CYS B 2 22  ? -51.149 52.462 55.931  1.00 39.54  ? 22  CYS B N   1 
ATOM   3230 C CA  . CYS B 2 22  ? -49.764 52.878 56.098  1.00 40.48  ? 22  CYS B CA  1 
ATOM   3231 C C   . CYS B 2 22  ? -49.311 53.562 54.817  1.00 40.90  ? 22  CYS B C   1 
ATOM   3232 O O   . CYS B 2 22  ? -49.499 53.020 53.722  1.00 39.98  ? 22  CYS B O   1 
ATOM   3233 C CB  . CYS B 2 22  ? -48.869 51.678 56.420  1.00 38.75  ? 22  CYS B CB  1 
ATOM   3234 S SG  . CYS B 2 22  ? -47.148 52.073 56.825  1.00 47.11  ? 22  CYS B SG  1 
ATOM   3235 N N   . THR B 2 23  ? -48.722 54.748 54.949  1.00 41.74  ? 23  THR B N   1 
ATOM   3236 C CA  . THR B 2 23  ? -48.272 55.529 53.802  1.00 45.45  ? 23  THR B CA  1 
ATOM   3237 C C   . THR B 2 23  ? -46.749 55.524 53.761  1.00 48.60  ? 23  THR B C   1 
ATOM   3238 O O   . THR B 2 23  ? -46.093 56.044 54.672  1.00 46.26  ? 23  THR B O   1 
ATOM   3239 C CB  . THR B 2 23  ? -48.805 56.962 53.859  1.00 45.54  ? 23  THR B CB  1 
ATOM   3240 O OG1 . THR B 2 23  ? -50.240 56.940 53.884  1.00 45.02  ? 23  THR B OG1 1 
ATOM   3241 C CG2 . THR B 2 23  ? -48.334 57.742 52.638  1.00 42.44  ? 23  THR B CG2 1 
ATOM   3242 N N   . VAL B 2 24  ? -46.194 54.943 52.707  1.00 47.02  ? 24  VAL B N   1 
ATOM   3243 C CA  . VAL B 2 24  ? -44.751 54.791 52.578  1.00 53.00  ? 24  VAL B CA  1 
ATOM   3244 C C   . VAL B 2 24  ? -44.193 55.979 51.807  1.00 51.65  ? 24  VAL B C   1 
ATOM   3245 O O   . VAL B 2 24  ? -44.675 56.311 50.718  1.00 47.93  ? 24  VAL B O   1 
ATOM   3246 C CB  . VAL B 2 24  ? -44.400 53.465 51.883  1.00 48.10  ? 24  VAL B CB  1 
ATOM   3247 C CG1 . VAL B 2 24  ? -42.898 53.344 51.703  1.00 47.20  ? 24  VAL B CG1 1 
ATOM   3248 C CG2 . VAL B 2 24  ? -44.949 52.291 52.684  1.00 44.34  ? 24  VAL B CG2 1 
ATOM   3249 N N   . SER B 2 25  ? -43.183 56.625 52.378  1.00 54.06  ? 25  SER B N   1 
ATOM   3250 C CA  . SER B 2 25  ? -42.460 57.701 51.723  1.00 54.79  ? 25  SER B CA  1 
ATOM   3251 C C   . SER B 2 25  ? -40.972 57.375 51.757  1.00 55.81  ? 25  SER B C   1 
ATOM   3252 O O   . SER B 2 25  ? -40.506 56.605 52.600  1.00 50.20  ? 25  SER B O   1 
ATOM   3253 C CB  . SER B 2 25  ? -42.741 59.055 52.394  1.00 49.09  ? 25  SER B CB  1 
ATOM   3254 O OG  . SER B 2 25  ? -42.150 59.120 53.683  1.00 59.78  ? 25  SER B OG  1 
ATOM   3255 N N   . GLY B 2 26  ? -40.229 57.966 50.822  1.00 59.02  ? 26  GLY B N   1 
ATOM   3256 C CA  . GLY B 2 26  ? -38.811 57.671 50.706  1.00 54.16  ? 26  GLY B CA  1 
ATOM   3257 C C   . GLY B 2 26  ? -38.517 56.270 50.223  1.00 58.42  ? 26  GLY B C   1 
ATOM   3258 O O   . GLY B 2 26  ? -37.505 55.681 50.618  1.00 57.07  ? 26  GLY B O   1 
ATOM   3259 N N   . GLY B 2 27  ? -39.377 55.721 49.379  1.00 51.17  ? 27  GLY B N   1 
ATOM   3260 C CA  . GLY B 2 27  ? -39.269 54.351 48.924  1.00 45.59  ? 27  GLY B CA  1 
ATOM   3261 C C   . GLY B 2 27  ? -40.573 53.889 48.324  1.00 49.44  ? 27  GLY B C   1 
ATOM   3262 O O   . GLY B 2 27  ? -41.619 54.523 48.468  1.00 59.06  ? 27  GLY B O   1 
ATOM   3263 N N   . SER B 2 28  ? -40.511 52.755 47.637  1.00 50.80  ? 28  SER B N   1 
ATOM   3264 C CA  . SER B 2 28  ? -41.653 52.223 46.908  1.00 47.18  ? 28  SER B CA  1 
ATOM   3265 C C   . SER B 2 28  ? -42.112 50.905 47.517  1.00 50.39  ? 28  SER B C   1 
ATOM   3266 O O   . SER B 2 28  ? -41.289 50.075 47.918  1.00 47.76  ? 28  SER B O   1 
ATOM   3267 C CB  . SER B 2 28  ? -41.308 52.017 45.430  1.00 46.88  ? 28  SER B CB  1 
ATOM   3268 O OG  . SER B 2 28  ? -42.286 51.220 44.775  1.00 50.17  ? 28  SER B OG  1 
ATOM   3269 N N   . VAL B 2 29  ? -43.433 50.718 47.586  1.00 44.34  ? 29  VAL B N   1 
ATOM   3270 C CA  . VAL B 2 29  ? -43.983 49.430 47.985  1.00 43.84  ? 29  VAL B CA  1 
ATOM   3271 C C   . VAL B 2 29  ? -43.823 48.388 46.897  1.00 47.33  ? 29  VAL B C   1 
ATOM   3272 O O   . VAL B 2 29  ? -44.124 47.212 47.128  1.00 47.93  ? 29  VAL B O   1 
ATOM   3273 C CB  . VAL B 2 29  ? -45.476 49.543 48.360  1.00 50.67  ? 29  VAL B CB  1 
ATOM   3274 C CG1 . VAL B 2 29  ? -45.692 50.667 49.370  1.00 46.51  ? 29  VAL B CG1 1 
ATOM   3275 C CG2 . VAL B 2 29  ? -46.325 49.751 47.111  1.00 45.72  ? 29  VAL B CG2 1 
ATOM   3276 N N   . SER B 2 30  ? -43.381 48.801 45.709  1.00 48.76  ? 30  SER B N   1 
ATOM   3277 C CA  . SER B 2 30  ? -43.035 47.877 44.633  1.00 51.57  ? 30  SER B CA  1 
ATOM   3278 C C   . SER B 2 30  ? -41.530 47.618 44.665  1.00 47.63  ? 30  SER B C   1 
ATOM   3279 O O   . SER B 2 30  ? -40.775 48.024 43.783  1.00 60.87  ? 30  SER B O   1 
ATOM   3280 C CB  . SER B 2 30  ? -43.476 48.442 43.284  1.00 49.31  ? 30  SER B CB  1 
ATOM   3281 O OG  . SER B 2 30  ? -44.886 48.544 43.197  1.00 56.79  ? 30  SER B OG  1 
ATOM   3282 N N   . SER B 2 31  ? -41.096 46.935 45.719  1.00 50.65  ? 31  SER B N   1 
ATOM   3283 C CA  . SER B 2 31  ? -39.672 46.690 45.946  1.00 50.07  ? 31  SER B CA  1 
ATOM   3284 C C   . SER B 2 31  ? -39.444 45.208 46.214  1.00 51.72  ? 31  SER B C   1 
ATOM   3285 O O   . SER B 2 31  ? -39.723 44.723 47.327  1.00 49.56  ? 31  SER B O   1 
ATOM   3286 C CB  . SER B 2 31  ? -39.147 47.542 47.095  1.00 56.46  ? 31  SER B CB  1 
ATOM   3287 O OG  . SER B 2 31  ? -37.762 47.812 46.926  1.00 64.45  ? 31  SER B OG  1 
ATOM   3288 N N   . PRO B 2 32  ? -38.963 44.460 45.222  1.00 51.59  ? 32  PRO B N   1 
ATOM   3289 C CA  . PRO B 2 32  ? -38.699 43.031 45.422  1.00 49.28  ? 32  PRO B CA  1 
ATOM   3290 C C   . PRO B 2 32  ? -37.832 42.772 46.646  1.00 43.99  ? 32  PRO B C   1 
ATOM   3291 O O   . PRO B 2 32  ? -36.923 43.541 46.966  1.00 44.35  ? 32  PRO B O   1 
ATOM   3292 C CB  . PRO B 2 32  ? -37.983 42.617 44.132  1.00 47.91  ? 32  PRO B CB  1 
ATOM   3293 C CG  . PRO B 2 32  ? -38.035 43.813 43.212  1.00 51.31  ? 32  PRO B CG  1 
ATOM   3294 C CD  . PRO B 2 32  ? -38.915 44.844 43.805  1.00 54.28  ? 32  PRO B CD  1 
ATOM   3295 N N   . GLY B 2 33  ? -38.122 41.668 47.330  1.00 39.65  ? 33  GLY B N   1 
ATOM   3296 C CA  . GLY B 2 33  ? -37.441 41.318 48.553  1.00 39.77  ? 33  GLY B CA  1 
ATOM   3297 C C   . GLY B 2 33  ? -38.068 41.878 49.808  1.00 40.67  ? 33  GLY B C   1 
ATOM   3298 O O   . GLY B 2 33  ? -37.639 41.509 50.911  1.00 37.34  ? 33  GLY B O   1 
ATOM   3299 N N   . TYR B 2 34  ? -39.076 42.742 49.680  1.00 41.89  ? 34  TYR B N   1 
ATOM   3300 C CA  . TYR B 2 34  ? -39.691 43.401 50.823  1.00 36.99  ? 34  TYR B CA  1 
ATOM   3301 C C   . TYR B 2 34  ? -41.197 43.185 50.815  1.00 37.49  ? 34  TYR B C   1 
ATOM   3302 O O   . TYR B 2 34  ? -41.862 43.423 49.804  1.00 39.92  ? 34  TYR B O   1 
ATOM   3303 C CB  . TYR B 2 34  ? -39.373 44.897 50.828  1.00 36.72  ? 34  TYR B CB  1 
ATOM   3304 C CG  . TYR B 2 34  ? -37.897 45.181 50.906  1.00 38.37  ? 34  TYR B CG  1 
ATOM   3305 C CD1 . TYR B 2 34  ? -37.217 45.089 52.113  1.00 37.62  ? 34  TYR B CD1 1 
ATOM   3306 C CD2 . TYR B 2 34  ? -37.174 45.521 49.768  1.00 39.88  ? 34  TYR B CD2 1 
ATOM   3307 C CE1 . TYR B 2 34  ? -35.859 45.342 52.186  1.00 40.65  ? 34  TYR B CE1 1 
ATOM   3308 C CE2 . TYR B 2 34  ? -35.814 45.778 49.833  1.00 39.71  ? 34  TYR B CE2 1 
ATOM   3309 C CZ  . TYR B 2 34  ? -35.164 45.687 51.042  1.00 40.00  ? 34  TYR B CZ  1 
ATOM   3310 O OH  . TYR B 2 34  ? -33.814 45.940 51.114  1.00 46.68  ? 34  TYR B OH  1 
ATOM   3311 N N   . TYR B 2 35  ? -41.721 42.729 51.945  1.00 34.04  ? 35  TYR B N   1 
ATOM   3312 C CA  . TYR B 2 35  ? -43.149 42.645 52.196  1.00 34.99  ? 35  TYR B CA  1 
ATOM   3313 C C   . TYR B 2 35  ? -43.530 43.701 53.224  1.00 38.74  ? 35  TYR B C   1 
ATOM   3314 O O   . TYR B 2 35  ? -42.701 44.160 54.014  1.00 42.77  ? 35  TYR B O   1 
ATOM   3315 C CB  . TYR B 2 35  ? -43.549 41.249 52.695  1.00 33.96  ? 35  TYR B CB  1 
ATOM   3316 C CG  . TYR B 2 35  ? -43.171 40.118 51.757  1.00 34.33  ? 35  TYR B CG  1 
ATOM   3317 C CD1 . TYR B 2 35  ? -41.838 39.759 51.559  1.00 35.19  ? 35  TYR B CD1 1 
ATOM   3318 C CD2 . TYR B 2 35  ? -44.146 39.402 51.075  1.00 35.16  ? 35  TYR B CD2 1 
ATOM   3319 C CE1 . TYR B 2 35  ? -41.491 38.731 50.699  1.00 38.18  ? 35  TYR B CE1 1 
ATOM   3320 C CE2 . TYR B 2 35  ? -43.809 38.369 50.216  1.00 34.64  ? 35  TYR B CE2 1 
ATOM   3321 C CZ  . TYR B 2 35  ? -42.484 38.038 50.034  1.00 38.52  ? 35  TYR B CZ  1 
ATOM   3322 O OH  . TYR B 2 35  ? -42.146 37.010 49.184  1.00 48.15  ? 35  TYR B OH  1 
ATOM   3323 N N   . TRP B 2 36  ? -44.798 44.091 53.206  1.00 39.29  ? 36  TRP B N   1 
ATOM   3324 C CA  . TRP B 2 36  ? -45.303 45.143 54.079  1.00 34.59  ? 36  TRP B CA  1 
ATOM   3325 C C   . TRP B 2 36  ? -46.323 44.535 55.024  1.00 32.78  ? 36  TRP B C   1 
ATOM   3326 O O   . TRP B 2 36  ? -47.344 43.997 54.583  1.00 34.10  ? 36  TRP B O   1 
ATOM   3327 C CB  . TRP B 2 36  ? -45.904 46.276 53.251  1.00 35.28  ? 36  TRP B CB  1 
ATOM   3328 C CG  . TRP B 2 36  ? -44.915 46.733 52.247  1.00 39.36  ? 36  TRP B CG  1 
ATOM   3329 C CD1 . TRP B 2 36  ? -44.755 46.259 50.975  1.00 37.82  ? 36  TRP B CD1 1 
ATOM   3330 C CD2 . TRP B 2 36  ? -43.886 47.702 52.447  1.00 34.86  ? 36  TRP B CD2 1 
ATOM   3331 N NE1 . TRP B 2 36  ? -43.709 46.900 50.360  1.00 39.17  ? 36  TRP B NE1 1 
ATOM   3332 C CE2 . TRP B 2 36  ? -43.157 47.791 51.244  1.00 41.70  ? 36  TRP B CE2 1 
ATOM   3333 C CE3 . TRP B 2 36  ? -43.523 48.521 53.519  1.00 33.83  ? 36  TRP B CE3 1 
ATOM   3334 C CZ2 . TRP B 2 36  ? -42.088 48.667 51.084  1.00 38.65  ? 36  TRP B CZ2 1 
ATOM   3335 C CZ3 . TRP B 2 36  ? -42.464 49.388 53.360  1.00 39.76  ? 36  TRP B CZ3 1 
ATOM   3336 C CH2 . TRP B 2 36  ? -41.755 49.452 52.153  1.00 39.54  ? 36  TRP B CH2 1 
ATOM   3337 N N   . SER B 2 37  ? -46.041 44.608 56.316  1.00 34.35  ? 37  SER B N   1 
ATOM   3338 C CA  . SER B 2 37  ? -46.785 43.829 57.286  1.00 38.61  ? 37  SER B CA  1 
ATOM   3339 C C   . SER B 2 37  ? -47.294 44.723 58.405  1.00 32.26  ? 37  SER B C   1 
ATOM   3340 O O   . SER B 2 37  ? -46.900 45.887 58.545  1.00 33.16  ? 37  SER B O   1 
ATOM   3341 C CB  . SER B 2 37  ? -45.921 42.683 57.836  1.00 36.09  ? 37  SER B CB  1 
ATOM   3342 O OG  . SER B 2 37  ? -44.796 43.185 58.519  1.00 43.15  ? 37  SER B OG  1 
ATOM   3343 N N   . TRP B 2 38  ? -48.216 44.160 59.181  1.00 34.32  ? 38  TRP B N   1 
ATOM   3344 C CA  . TRP B 2 38  ? -48.780 44.797 60.362  1.00 31.35  ? 38  TRP B CA  1 
ATOM   3345 C C   . TRP B 2 38  ? -48.422 43.961 61.579  1.00 32.96  ? 38  TRP B C   1 
ATOM   3346 O O   . TRP B 2 38  ? -48.558 42.731 61.554  1.00 31.82  ? 38  TRP B O   1 
ATOM   3347 C CB  . TRP B 2 38  ? -50.300 44.939 60.243  1.00 32.16  ? 38  TRP B CB  1 
ATOM   3348 C CG  . TRP B 2 38  ? -50.694 45.820 59.112  1.00 37.46  ? 38  TRP B CG  1 
ATOM   3349 C CD1 . TRP B 2 38  ? -50.946 45.442 57.825  1.00 33.44  ? 38  TRP B CD1 1 
ATOM   3350 C CD2 . TRP B 2 38  ? -50.855 47.242 59.155  1.00 33.53  ? 38  TRP B CD2 1 
ATOM   3351 N NE1 . TRP B 2 38  ? -51.268 46.540 57.066  1.00 35.97  ? 38  TRP B NE1 1 
ATOM   3352 C CE2 . TRP B 2 38  ? -51.218 47.659 57.857  1.00 36.77  ? 38  TRP B CE2 1 
ATOM   3353 C CE3 . TRP B 2 38  ? -50.735 48.201 60.166  1.00 31.23  ? 38  TRP B CE3 1 
ATOM   3354 C CZ2 . TRP B 2 38  ? -51.461 49.001 57.542  1.00 38.16  ? 38  TRP B CZ2 1 
ATOM   3355 C CZ3 . TRP B 2 38  ? -50.974 49.532 59.855  1.00 42.21  ? 38  TRP B CZ3 1 
ATOM   3356 C CH2 . TRP B 2 38  ? -51.336 49.920 58.552  1.00 38.60  ? 38  TRP B CH2 1 
ATOM   3357 N N   . ILE B 2 39  ? -47.952 44.629 62.627  1.00 28.18  ? 39  ILE B N   1 
ATOM   3358 C CA  . ILE B 2 39  ? -47.606 44.003 63.893  1.00 27.06  ? 39  ILE B CA  1 
ATOM   3359 C C   . ILE B 2 39  ? -48.256 44.826 64.993  1.00 35.21  ? 39  ILE B C   1 
ATOM   3360 O O   . ILE B 2 39  ? -48.311 46.058 64.905  1.00 36.27  ? 39  ILE B O   1 
ATOM   3361 C CB  . ILE B 2 39  ? -46.076 43.918 64.083  1.00 29.83  ? 39  ILE B CB  1 
ATOM   3362 C CG1 . ILE B 2 39  ? -45.445 43.101 62.955  1.00 33.02  ? 39  ILE B CG1 1 
ATOM   3363 C CG2 . ILE B 2 39  ? -45.720 43.306 65.434  1.00 31.91  ? 39  ILE B CG2 1 
ATOM   3364 C CD1 . ILE B 2 39  ? -44.064 43.570 62.549  1.00 27.90  ? 39  ILE B CD1 1 
ATOM   3365 N N   . ARG B 2 40  ? -48.770 44.155 66.021  1.00 30.01  ? 40  ARG B N   1 
ATOM   3366 C CA  . ARG B 2 40  ? -49.537 44.844 67.044  1.00 33.73  ? 40  ARG B CA  1 
ATOM   3367 C C   . ARG B 2 40  ? -49.028 44.473 68.427  1.00 34.71  ? 40  ARG B C   1 
ATOM   3368 O O   . ARG B 2 40  ? -48.396 43.432 68.630  1.00 33.11  ? 40  ARG B O   1 
ATOM   3369 C CB  . ARG B 2 40  ? -51.042 44.549 66.920  1.00 30.10  ? 40  ARG B CB  1 
ATOM   3370 C CG  . ARG B 2 40  ? -51.473 43.222 67.483  1.00 31.65  ? 40  ARG B CG  1 
ATOM   3371 C CD  . ARG B 2 40  ? -52.973 43.053 67.342  1.00 32.32  ? 40  ARG B CD  1 
ATOM   3372 N NE  . ARG B 2 40  ? -53.396 41.688 67.623  1.00 35.01  ? 40  ARG B NE  1 
ATOM   3373 C CZ  . ARG B 2 40  ? -54.652 41.266 67.567  1.00 36.85  ? 40  ARG B CZ  1 
ATOM   3374 N NH1 . ARG B 2 40  ? -55.643 42.086 67.243  1.00 31.61  ? 40  ARG B NH1 1 
ATOM   3375 N NH2 . ARG B 2 40  ? -54.920 39.991 67.838  1.00 31.52  ? 40  ARG B NH2 1 
ATOM   3376 N N   . GLN B 2 41  ? -49.312 45.363 69.377  1.00 32.45  ? 41  GLN B N   1 
ATOM   3377 C CA  . GLN B 2 41  ? -48.800 45.261 70.740  1.00 33.44  ? 41  GLN B CA  1 
ATOM   3378 C C   . GLN B 2 41  ? -49.868 45.769 71.699  1.00 34.14  ? 41  GLN B C   1 
ATOM   3379 O O   . GLN B 2 41  ? -50.076 46.987 71.813  1.00 35.90  ? 41  GLN B O   1 
ATOM   3380 C CB  . GLN B 2 41  ? -47.506 46.055 70.894  1.00 35.39  ? 41  GLN B CB  1 
ATOM   3381 C CG  . GLN B 2 41  ? -46.915 46.046 72.295  1.00 32.24  ? 41  GLN B CG  1 
ATOM   3382 C CD  . GLN B 2 41  ? -45.507 46.606 72.320  1.00 36.87  ? 41  GLN B CD  1 
ATOM   3383 O OE1 . GLN B 2 41  ? -44.609 46.028 72.939  1.00 42.45  ? 41  GLN B OE1 1 
ATOM   3384 N NE2 . GLN B 2 41  ? -45.300 47.727 71.633  1.00 28.99  ? 41  GLN B NE2 1 
ATOM   3385 N N   . PRO B 2 42  ? -50.574 44.872 72.388  1.00 34.90  ? 42  PRO B N   1 
ATOM   3386 C CA  . PRO B 2 42  ? -51.501 45.324 73.419  1.00 35.72  ? 42  PRO B CA  1 
ATOM   3387 C C   . PRO B 2 42  ? -50.751 46.052 74.518  1.00 37.54  ? 42  PRO B C   1 
ATOM   3388 O O   . PRO B 2 42  ? -49.563 45.781 74.764  1.00 38.82  ? 42  PRO B O   1 
ATOM   3389 C CB  . PRO B 2 42  ? -52.124 44.015 73.929  1.00 33.82  ? 42  PRO B CB  1 
ATOM   3390 C CG  . PRO B 2 42  ? -51.938 43.038 72.823  1.00 32.49  ? 42  PRO B CG  1 
ATOM   3391 C CD  . PRO B 2 42  ? -50.626 43.416 72.189  1.00 38.86  ? 42  PRO B CD  1 
ATOM   3392 N N   . PRO B 2 43  ? -51.405 47.001 75.188  1.00 43.04  ? 43  PRO B N   1 
ATOM   3393 C CA  . PRO B 2 43  ? -50.713 47.796 76.214  1.00 40.56  ? 43  PRO B CA  1 
ATOM   3394 C C   . PRO B 2 43  ? -50.030 46.926 77.259  1.00 44.55  ? 43  PRO B C   1 
ATOM   3395 O O   . PRO B 2 43  ? -50.609 45.970 77.782  1.00 43.12  ? 43  PRO B O   1 
ATOM   3396 C CB  . PRO B 2 43  ? -51.840 48.639 76.831  1.00 42.13  ? 43  PRO B CB  1 
ATOM   3397 C CG  . PRO B 2 43  ? -53.133 48.071 76.278  1.00 46.17  ? 43  PRO B CG  1 
ATOM   3398 C CD  . PRO B 2 43  ? -52.780 47.471 74.963  1.00 41.31  ? 43  PRO B CD  1 
ATOM   3399 N N   . GLY B 2 44  ? -48.775 47.262 77.554  1.00 44.06  ? 44  GLY B N   1 
ATOM   3400 C CA  . GLY B 2 44  ? -47.987 46.501 78.498  1.00 39.80  ? 44  GLY B CA  1 
ATOM   3401 C C   . GLY B 2 44  ? -47.635 45.092 78.078  1.00 44.67  ? 44  GLY B C   1 
ATOM   3402 O O   . GLY B 2 44  ? -47.210 44.305 78.929  1.00 47.32  ? 44  GLY B O   1 
ATOM   3403 N N   . GLN B 2 45  ? -47.770 44.751 76.794  1.00 40.86  ? 45  GLN B N   1 
ATOM   3404 C CA  . GLN B 2 45  ? -47.563 43.377 76.348  1.00 42.40  ? 45  GLN B CA  1 
ATOM   3405 C C   . GLN B 2 45  ? -46.538 43.256 75.227  1.00 38.82  ? 45  GLN B C   1 
ATOM   3406 O O   . GLN B 2 45  ? -45.809 44.207 74.924  1.00 40.48  ? 45  GLN B O   1 
ATOM   3407 C CB  . GLN B 2 45  ? -48.888 42.767 75.888  1.00 41.09  ? 45  GLN B CB  1 
ATOM   3408 C CG  . GLN B 2 45  ? -49.902 42.577 76.993  1.00 46.04  ? 45  GLN B CG  1 
ATOM   3409 C CD  . GLN B 2 45  ? -50.725 41.327 76.790  1.00 59.94  ? 45  GLN B CD  1 
ATOM   3410 O OE1 . GLN B 2 45  ? -51.924 41.396 76.517  1.00 59.63  ? 45  GLN B OE1 1 
ATOM   3411 N NE2 . GLN B 2 45  ? -50.081 40.170 76.908  1.00 70.20  ? 45  GLN B NE2 1 
ATOM   3412 N N   . GLY B 2 46  ? -46.491 42.081 74.606  1.00 30.79  ? 46  GLY B N   1 
ATOM   3413 C CA  . GLY B 2 46  ? -45.505 41.756 73.606  1.00 27.19  ? 46  GLY B CA  1 
ATOM   3414 C C   . GLY B 2 46  ? -45.998 42.029 72.202  1.00 36.58  ? 46  GLY B C   1 
ATOM   3415 O O   . GLY B 2 46  ? -46.975 42.754 71.984  1.00 40.65  ? 46  GLY B O   1 
ATOM   3416 N N   . LEU B 2 47  ? -45.314 41.430 71.233  1.00 31.80  ? 47  LEU B N   1 
ATOM   3417 C CA  . LEU B 2 47  ? -45.536 41.720 69.826  1.00 35.27  ? 47  LEU B CA  1 
ATOM   3418 C C   . LEU B 2 47  ? -46.208 40.543 69.134  1.00 37.46  ? 47  LEU B C   1 
ATOM   3419 O O   . LEU B 2 47  ? -45.877 39.381 69.397  1.00 37.23  ? 47  LEU B O   1 
ATOM   3420 C CB  . LEU B 2 47  ? -44.216 42.063 69.130  1.00 33.62  ? 47  LEU B CB  1 
ATOM   3421 C CG  . LEU B 2 47  ? -43.620 43.365 69.670  1.00 30.59  ? 47  LEU B CG  1 
ATOM   3422 C CD1 . LEU B 2 47  ? -42.104 43.396 69.537  1.00 29.39  ? 47  LEU B CD1 1 
ATOM   3423 C CD2 . LEU B 2 47  ? -44.256 44.557 68.971  1.00 35.92  ? 47  LEU B CD2 1 
ATOM   3424 N N   . GLU B 2 48  ? -47.153 40.855 68.246  1.00 34.74  ? 48  GLU B N   1 
ATOM   3425 C CA  . GLU B 2 48  ? -47.871 39.852 67.470  1.00 34.61  ? 48  GLU B CA  1 
ATOM   3426 C C   . GLU B 2 48  ? -47.940 40.294 66.015  1.00 33.61  ? 48  GLU B C   1 
ATOM   3427 O O   . GLU B 2 48  ? -48.517 41.343 65.703  1.00 35.00  ? 48  GLU B O   1 
ATOM   3428 C CB  . GLU B 2 48  ? -49.280 39.619 68.027  1.00 30.97  ? 48  GLU B CB  1 
ATOM   3429 C CG  . GLU B 2 48  ? -50.028 38.504 67.315  1.00 34.22  ? 48  GLU B CG  1 
ATOM   3430 C CD  . GLU B 2 48  ? -51.448 38.323 67.818  1.00 40.97  ? 48  GLU B CD  1 
ATOM   3431 O OE1 . GLU B 2 48  ? -52.065 39.322 68.244  1.00 37.71  ? 48  GLU B OE1 1 
ATOM   3432 O OE2 . GLU B 2 48  ? -51.944 37.177 67.791  1.00 45.13  ? 48  GLU B OE2 1 
ATOM   3433 N N   . TRP B 2 49  ? -47.353 39.494 65.134  1.00 32.25  ? 49  TRP B N   1 
ATOM   3434 C CA  . TRP B 2 49  ? -47.466 39.732 63.702  1.00 32.30  ? 49  TRP B CA  1 
ATOM   3435 C C   . TRP B 2 49  ? -48.869 39.372 63.226  1.00 34.77  ? 49  TRP B C   1 
ATOM   3436 O O   . TRP B 2 49  ? -49.411 38.323 63.591  1.00 35.37  ? 49  TRP B O   1 
ATOM   3437 C CB  . TRP B 2 49  ? -46.413 38.910 62.966  1.00 29.45  ? 49  TRP B CB  1 
ATOM   3438 C CG  . TRP B 2 49  ? -46.421 39.023 61.473  1.00 33.43  ? 49  TRP B CG  1 
ATOM   3439 C CD1 . TRP B 2 49  ? -45.918 40.050 60.722  1.00 32.09  ? 49  TRP B CD1 1 
ATOM   3440 C CD2 . TRP B 2 49  ? -46.925 38.055 60.543  1.00 33.06  ? 49  TRP B CD2 1 
ATOM   3441 N NE1 . TRP B 2 49  ? -46.089 39.782 59.382  1.00 31.85  ? 49  TRP B NE1 1 
ATOM   3442 C CE2 . TRP B 2 49  ? -46.701 38.563 59.246  1.00 33.53  ? 49  TRP B CE2 1 
ATOM   3443 C CE3 . TRP B 2 49  ? -47.547 36.809 60.681  1.00 33.67  ? 49  TRP B CE3 1 
ATOM   3444 C CZ2 . TRP B 2 49  ? -47.074 37.866 58.096  1.00 35.48  ? 49  TRP B CZ2 1 
ATOM   3445 C CZ3 . TRP B 2 49  ? -47.912 36.115 59.539  1.00 33.00  ? 49  TRP B CZ3 1 
ATOM   3446 C CH2 . TRP B 2 49  ? -47.682 36.649 58.263  1.00 33.54  ? 49  TRP B CH2 1 
ATOM   3447 N N   . ILE B 2 50  ? -49.461 40.243 62.414  1.00 33.81  ? 50  ILE B N   1 
ATOM   3448 C CA  . ILE B 2 50  ? -50.825 40.059 61.936  1.00 31.38  ? 50  ILE B CA  1 
ATOM   3449 C C   . ILE B 2 50  ? -50.855 39.455 60.537  1.00 34.46  ? 50  ILE B C   1 
ATOM   3450 O O   . ILE B 2 50  ? -51.619 38.527 60.275  1.00 35.99  ? 50  ILE B O   1 
ATOM   3451 C CB  . ILE B 2 50  ? -51.589 41.401 61.983  1.00 34.21  ? 50  ILE B CB  1 
ATOM   3452 C CG1 . ILE B 2 50  ? -51.709 41.897 63.427  1.00 30.59  ? 50  ILE B CG1 1 
ATOM   3453 C CG2 . ILE B 2 50  ? -52.968 41.269 61.330  1.00 31.32  ? 50  ILE B CG2 1 
ATOM   3454 C CD1 . ILE B 2 50  ? -52.031 43.363 63.546  1.00 29.65  ? 50  ILE B CD1 1 
ATOM   3455 N N   . GLY B 2 51  ? -50.016 39.952 59.645  1.00 35.40  ? 51  GLY B N   1 
ATOM   3456 C CA  . GLY B 2 51  ? -50.019 39.522 58.262  1.00 35.42  ? 51  GLY B CA  1 
ATOM   3457 C C   . GLY B 2 51  ? -49.314 40.559 57.417  1.00 35.97  ? 51  GLY B C   1 
ATOM   3458 O O   . GLY B 2 51  ? -48.905 41.612 57.905  1.00 34.66  ? 51  GLY B O   1 
ATOM   3459 N N   . ASP B 2 52  ? -49.180 40.245 56.128  1.00 36.08  ? 52  ASP B N   1 
ATOM   3460 C CA  . ASP B 2 52  ? -48.499 41.157 55.216  1.00 38.36  ? 52  ASP B CA  1 
ATOM   3461 C C   . ASP B 2 52  ? -49.246 41.244 53.890  1.00 35.79  ? 52  ASP B C   1 
ATOM   3462 O O   . ASP B 2 52  ? -50.304 40.637 53.699  1.00 35.48  ? 52  ASP B O   1 
ATOM   3463 C CB  . ASP B 2 52  ? -47.030 40.748 55.003  1.00 36.31  ? 52  ASP B CB  1 
ATOM   3464 C CG  . ASP B 2 52  ? -46.865 39.439 54.225  1.00 37.50  ? 52  ASP B CG  1 
ATOM   3465 O OD1 . ASP B 2 52  ? -47.747 39.051 53.424  1.00 36.51  ? 52  ASP B OD1 1 
ATOM   3466 O OD2 . ASP B 2 52  ? -45.809 38.798 54.405  1.00 36.64  ? 52  ASP B OD2 1 
ATOM   3467 N N   . ILE B 2 53  ? -48.666 42.019 52.975  1.00 33.97  ? 53  ILE B N   1 
ATOM   3468 C CA  . ILE B 2 53  ? -49.087 42.099 51.583  1.00 40.35  ? 53  ILE B CA  1 
ATOM   3469 C C   . ILE B 2 53  ? -47.828 42.278 50.742  1.00 42.38  ? 53  ILE B C   1 
ATOM   3470 O O   . ILE B 2 53  ? -46.862 42.920 51.169  1.00 41.01  ? 53  ILE B O   1 
ATOM   3471 C CB  . ILE B 2 53  ? -50.092 43.253 51.343  1.00 41.61  ? 53  ILE B CB  1 
ATOM   3472 C CG1 . ILE B 2 53  ? -50.628 43.227 49.910  1.00 37.64  ? 53  ILE B CG1 1 
ATOM   3473 C CG2 . ILE B 2 53  ? -49.455 44.601 51.646  1.00 39.29  ? 53  ILE B CG2 1 
ATOM   3474 C CD1 . ILE B 2 53  ? -51.630 42.117 49.650  1.00 35.34  ? 53  ILE B CD1 1 
ATOM   3475 N N   . TYR B 2 54  ? -47.826 41.673 49.556  1.00 40.30  ? 54  TYR B N   1 
ATOM   3476 C CA  . TYR B 2 54  ? -46.732 41.806 48.607  1.00 42.01  ? 54  TYR B CA  1 
ATOM   3477 C C   . TYR B 2 54  ? -47.202 42.630 47.417  1.00 41.00  ? 54  TYR B C   1 
ATOM   3478 O O   . TYR B 2 54  ? -48.398 42.677 47.117  1.00 44.10  ? 54  TYR B O   1 
ATOM   3479 C CB  . TYR B 2 54  ? -46.233 40.437 48.136  1.00 41.06  ? 54  TYR B CB  1 
ATOM   3480 C CG  . TYR B 2 54  ? -44.841 40.474 47.547  1.00 40.91  ? 54  TYR B CG  1 
ATOM   3481 C CD1 . TYR B 2 54  ? -43.826 41.185 48.167  1.00 40.19  ? 54  TYR B CD1 1 
ATOM   3482 C CD2 . TYR B 2 54  ? -44.547 39.803 46.366  1.00 45.61  ? 54  TYR B CD2 1 
ATOM   3483 C CE1 . TYR B 2 54  ? -42.549 41.223 47.633  1.00 44.74  ? 54  TYR B CE1 1 
ATOM   3484 C CE2 . TYR B 2 54  ? -43.273 39.833 45.822  1.00 45.75  ? 54  TYR B CE2 1 
ATOM   3485 C CZ  . TYR B 2 54  ? -42.280 40.547 46.458  1.00 46.66  ? 54  TYR B CZ  1 
ATOM   3486 O OH  . TYR B 2 54  ? -41.011 40.587 45.929  1.00 42.82  ? 54  TYR B OH  1 
ATOM   3487 N N   . TYR B 2 55  ? -46.255 43.289 46.741  1.00 37.24  ? 55  TYR B N   1 
ATOM   3488 C CA  . TYR B 2 55  ? -46.650 44.217 45.684  1.00 44.60  ? 55  TYR B CA  1 
ATOM   3489 C C   . TYR B 2 55  ? -47.307 43.493 44.515  1.00 44.51  ? 55  TYR B C   1 
ATOM   3490 O O   . TYR B 2 55  ? -48.171 44.068 43.846  1.00 42.12  ? 55  TYR B O   1 
ATOM   3491 C CB  . TYR B 2 55  ? -45.451 45.048 45.217  1.00 46.80  ? 55  TYR B CB  1 
ATOM   3492 C CG  . TYR B 2 55  ? -44.494 44.349 44.278  1.00 51.78  ? 55  TYR B CG  1 
ATOM   3493 C CD1 . TYR B 2 55  ? -43.450 43.570 44.768  1.00 48.78  ? 55  TYR B CD1 1 
ATOM   3494 C CD2 . TYR B 2 55  ? -44.616 44.492 42.900  1.00 49.04  ? 55  TYR B CD2 1 
ATOM   3495 C CE1 . TYR B 2 55  ? -42.568 42.939 43.911  1.00 51.43  ? 55  TYR B CE1 1 
ATOM   3496 C CE2 . TYR B 2 55  ? -43.739 43.869 42.037  1.00 50.62  ? 55  TYR B CE2 1 
ATOM   3497 C CZ  . TYR B 2 55  ? -42.718 43.092 42.546  1.00 55.40  ? 55  TYR B CZ  1 
ATOM   3498 O OH  . TYR B 2 55  ? -41.845 42.464 41.688  1.00 54.64  ? 55  TYR B OH  1 
ATOM   3499 N N   . ARG B 2 56  ? -46.941 42.230 44.271  1.00 48.81  ? 56  ARG B N   1 
ATOM   3500 C CA  . ARG B 2 56  ? -47.626 41.451 43.242  1.00 48.26  ? 56  ARG B CA  1 
ATOM   3501 C C   . ARG B 2 56  ? -49.064 41.122 43.628  1.00 52.04  ? 56  ARG B C   1 
ATOM   3502 O O   . ARG B 2 56  ? -49.869 40.800 42.748  1.00 54.60  ? 56  ARG B O   1 
ATOM   3503 C CB  . ARG B 2 56  ? -46.873 40.149 42.940  1.00 51.60  ? 56  ARG B CB  1 
ATOM   3504 C CG  . ARG B 2 56  ? -45.365 40.277 42.721  1.00 54.74  ? 56  ARG B CG  1 
ATOM   3505 C CD  . ARG B 2 56  ? -45.000 40.783 41.327  1.00 61.08  ? 56  ARG B CD  1 
ATOM   3506 N NE  . ARG B 2 56  ? -43.821 40.101 40.797  1.00 67.90  ? 56  ARG B NE  1 
ATOM   3507 C CZ  . ARG B 2 56  ? -43.409 40.166 39.536  1.00 66.14  ? 56  ARG B CZ  1 
ATOM   3508 N NH1 . ARG B 2 56  ? -43.993 40.962 38.655  1.00 64.47  ? 56  ARG B NH1 1 
ATOM   3509 N NH2 . ARG B 2 56  ? -42.371 39.426 39.154  1.00 61.22  ? 56  ARG B NH2 1 
ATOM   3510 N N   . GLY B 2 57  ? -49.405 41.184 44.913  1.00 50.49  ? 57  GLY B N   1 
ATOM   3511 C CA  . GLY B 2 57  ? -50.774 40.999 45.366  1.00 42.58  ? 57  GLY B CA  1 
ATOM   3512 C C   . GLY B 2 57  ? -50.989 39.855 46.336  1.00 43.89  ? 57  GLY B C   1 
ATOM   3513 O O   . GLY B 2 57  ? -52.097 39.727 46.878  1.00 41.27  ? 57  GLY B O   1 
ATOM   3514 N N   . SER B 2 58  ? -49.989 39.013 46.584  1.00 44.51  ? 58  SER B N   1 
ATOM   3515 C CA  . SER B 2 58  ? -50.142 37.907 47.518  1.00 40.11  ? 58  SER B CA  1 
ATOM   3516 C C   . SER B 2 58  ? -49.987 38.395 48.960  1.00 40.50  ? 58  SER B C   1 
ATOM   3517 O O   . SER B 2 58  ? -49.396 39.445 49.231  1.00 37.63  ? 58  SER B O   1 
ATOM   3518 C CB  . SER B 2 58  ? -49.118 36.817 47.217  1.00 39.48  ? 58  SER B CB  1 
ATOM   3519 O OG  . SER B 2 58  ? -47.842 37.390 46.975  1.00 51.14  ? 58  SER B OG  1 
ATOM   3520 N N   . SER B 2 59  ? -50.526 37.613 49.895  1.00 38.75  ? 59  SER B N   1 
ATOM   3521 C CA  . SER B 2 59  ? -50.508 38.022 51.293  1.00 41.40  ? 59  SER B CA  1 
ATOM   3522 C C   . SER B 2 59  ? -50.452 36.807 52.205  1.00 40.10  ? 59  SER B C   1 
ATOM   3523 O O   . SER B 2 59  ? -51.193 35.840 52.009  1.00 39.50  ? 59  SER B O   1 
ATOM   3524 C CB  . SER B 2 59  ? -51.735 38.876 51.628  1.00 41.11  ? 59  SER B CB  1 
ATOM   3525 O OG  . SER B 2 59  ? -52.925 38.133 51.480  1.00 50.48  ? 59  SER B OG  1 
ATOM   3526 N N   . ASN B 2 60  ? -49.568 36.866 53.195  1.00 41.60  ? 60  ASN B N   1 
ATOM   3527 C CA  . ASN B 2 60  ? -49.525 35.902 54.282  1.00 42.47  ? 60  ASN B CA  1 
ATOM   3528 C C   . ASN B 2 60  ? -50.219 36.502 55.498  1.00 43.22  ? 60  ASN B C   1 
ATOM   3529 O O   . ASN B 2 60  ? -50.243 37.723 55.676  1.00 44.36  ? 60  ASN B O   1 
ATOM   3530 C CB  . ASN B 2 60  ? -48.079 35.530 54.632  1.00 39.46  ? 60  ASN B CB  1 
ATOM   3531 C CG  . ASN B 2 60  ? -47.240 35.214 53.400  1.00 45.71  ? 60  ASN B CG  1 
ATOM   3532 O OD1 . ASN B 2 60  ? -47.458 34.197 52.743  1.00 46.62  ? 60  ASN B OD1 1 
ATOM   3533 N ND2 . ASN B 2 60  ? -46.285 36.093 53.073  1.00 41.23  ? 60  ASN B ND2 1 
ATOM   3534 N N   . GLN B 2 61  ? -50.787 35.637 56.337  1.00 38.46  ? 61  GLN B N   1 
ATOM   3535 C CA  . GLN B 2 61  ? -51.491 36.078 57.533  1.00 40.76  ? 61  GLN B CA  1 
ATOM   3536 C C   . GLN B 2 61  ? -51.151 35.162 58.697  1.00 38.31  ? 61  GLN B C   1 
ATOM   3537 O O   . GLN B 2 61  ? -50.848 33.981 58.511  1.00 39.12  ? 61  GLN B O   1 
ATOM   3538 C CB  . GLN B 2 61  ? -53.013 36.095 57.339  1.00 43.35  ? 61  GLN B CB  1 
ATOM   3539 C CG  . GLN B 2 61  ? -53.492 37.004 56.228  1.00 49.80  ? 61  GLN B CG  1 
ATOM   3540 C CD  . GLN B 2 61  ? -54.253 36.255 55.153  1.00 55.73  ? 61  GLN B CD  1 
ATOM   3541 O OE1 . GLN B 2 61  ? -53.657 35.597 54.294  1.00 50.67  ? 61  GLN B OE1 1 
ATOM   3542 N NE2 . GLN B 2 61  ? -55.581 36.340 55.201  1.00 61.40  ? 61  GLN B NE2 1 
ATOM   3543 N N   . ASN B 2 62  ? -51.200 35.724 59.898  1.00 42.54  ? 62  ASN B N   1 
ATOM   3544 C CA  . ASN B 2 62  ? -51.056 34.930 61.108  1.00 40.40  ? 62  ASN B CA  1 
ATOM   3545 C C   . ASN B 2 62  ? -52.180 33.902 61.136  1.00 45.83  ? 62  ASN B C   1 
ATOM   3546 O O   . ASN B 2 62  ? -53.361 34.288 61.177  1.00 43.28  ? 62  ASN B O   1 
ATOM   3547 C CB  . ASN B 2 62  ? -51.095 35.820 62.350  1.00 37.24  ? 62  ASN B CB  1 
ATOM   3548 C CG  . ASN B 2 62  ? -50.841 35.050 63.647  1.00 43.46  ? 62  ASN B CG  1 
ATOM   3549 O OD1 . ASN B 2 62  ? -51.256 33.899 63.806  1.00 42.91  ? 62  ASN B OD1 1 
ATOM   3550 N ND2 . ASN B 2 62  ? -50.154 35.694 64.581  1.00 45.66  ? 62  ASN B ND2 1 
ATOM   3551 N N   . PRO B 2 63  ? -51.868 32.602 61.109  1.00 45.40  ? 63  PRO B N   1 
ATOM   3552 C CA  . PRO B 2 63  ? -52.927 31.589 60.957  1.00 45.12  ? 63  PRO B CA  1 
ATOM   3553 C C   . PRO B 2 63  ? -54.015 31.660 62.012  1.00 44.84  ? 63  PRO B C   1 
ATOM   3554 O O   . PRO B 2 63  ? -55.133 31.199 61.751  1.00 52.34  ? 63  PRO B O   1 
ATOM   3555 C CB  . PRO B 2 63  ? -52.157 30.259 61.031  1.00 48.47  ? 63  PRO B CB  1 
ATOM   3556 C CG  . PRO B 2 63  ? -50.808 30.604 61.594  1.00 44.96  ? 63  PRO B CG  1 
ATOM   3557 C CD  . PRO B 2 63  ? -50.527 32.001 61.152  1.00 42.95  ? 63  PRO B CD  1 
ATOM   3558 N N   . SER B 2 64  ? -53.737 32.235 63.184  1.00 46.54  ? 64  SER B N   1 
ATOM   3559 C CA  . SER B 2 64  ? -54.742 32.365 64.232  1.00 47.74  ? 64  SER B CA  1 
ATOM   3560 C C   . SER B 2 64  ? -55.642 33.585 64.053  1.00 52.24  ? 64  SER B C   1 
ATOM   3561 O O   . SER B 2 64  ? -56.578 33.764 64.838  1.00 55.30  ? 64  SER B O   1 
ATOM   3562 C CB  . SER B 2 64  ? -54.062 32.416 65.602  1.00 45.62  ? 64  SER B CB  1 
ATOM   3563 O OG  . SER B 2 64  ? -53.151 33.495 65.682  1.00 54.20  ? 64  SER B OG  1 
ATOM   3564 N N   . LEU B 2 65  ? -55.384 34.429 63.055  1.00 48.03  ? 65  LEU B N   1 
ATOM   3565 C CA  . LEU B 2 65  ? -56.258 35.547 62.736  1.00 46.81  ? 65  LEU B CA  1 
ATOM   3566 C C   . LEU B 2 65  ? -56.717 35.541 61.285  1.00 46.87  ? 65  LEU B C   1 
ATOM   3567 O O   . LEU B 2 65  ? -57.447 36.458 60.885  1.00 46.21  ? 65  LEU B O   1 
ATOM   3568 C CB  . LEU B 2 65  ? -55.558 36.883 63.030  1.00 40.75  ? 65  LEU B CB  1 
ATOM   3569 C CG  . LEU B 2 65  ? -54.879 37.093 64.383  1.00 44.99  ? 65  LEU B CG  1 
ATOM   3570 C CD1 . LEU B 2 65  ? -53.808 38.171 64.266  1.00 40.04  ? 65  LEU B CD1 1 
ATOM   3571 C CD2 . LEU B 2 65  ? -55.891 37.461 65.453  1.00 34.55  ? 65  LEU B CD2 1 
ATOM   3572 N N   . LYS B 2 66  ? -56.325 34.529 60.498  1.00 43.05  ? 66  LYS B N   1 
ATOM   3573 C CA  . LYS B 2 66  ? -56.503 34.559 59.046  1.00 49.34  ? 66  LYS B CA  1 
ATOM   3574 C C   . LYS B 2 66  ? -57.928 34.917 58.636  1.00 47.05  ? 66  LYS B C   1 
ATOM   3575 O O   . LYS B 2 66  ? -58.134 35.721 57.718  1.00 47.28  ? 66  LYS B O   1 
ATOM   3576 C CB  . LYS B 2 66  ? -56.112 33.209 58.442  1.00 45.45  ? 66  LYS B CB  1 
ATOM   3577 C CG  . LYS B 2 66  ? -55.760 33.282 56.959  1.00 50.47  ? 66  LYS B CG  1 
ATOM   3578 C CD  . LYS B 2 66  ? -56.214 32.037 56.208  1.00 51.03  ? 66  LYS B CD  1 
ATOM   3579 C CE  . LYS B 2 66  ? -55.333 31.768 54.995  1.00 52.41  ? 66  LYS B CE  1 
ATOM   3580 N NZ  . LYS B 2 66  ? -55.911 32.317 53.738  1.00 55.38  ? 66  LYS B NZ  1 
ATOM   3581 N N   . SER B 2 67  ? -58.923 34.337 59.308  1.00 37.86  ? 67  SER B N   1 
ATOM   3582 C CA  . SER B 2 67  ? -60.310 34.558 58.916  1.00 43.00  ? 67  SER B CA  1 
ATOM   3583 C C   . SER B 2 67  ? -60.751 36.008 59.094  1.00 43.17  ? 67  SER B C   1 
ATOM   3584 O O   . SER B 2 67  ? -61.732 36.425 58.467  1.00 46.08  ? 67  SER B O   1 
ATOM   3585 C CB  . SER B 2 67  ? -61.228 33.631 59.715  1.00 40.37  ? 67  SER B CB  1 
ATOM   3586 O OG  . SER B 2 67  ? -60.994 33.761 61.106  1.00 48.63  ? 67  SER B OG  1 
ATOM   3587 N N   . ARG B 2 68  ? -60.057 36.786 59.924  1.00 39.53  ? 68  ARG B N   1 
ATOM   3588 C CA  . ARG B 2 68  ? -60.451 38.161 60.196  1.00 37.44  ? 68  ARG B CA  1 
ATOM   3589 C C   . ARG B 2 68  ? -59.560 39.190 59.517  1.00 37.93  ? 68  ARG B C   1 
ATOM   3590 O O   . ARG B 2 68  ? -59.830 40.390 59.627  1.00 38.61  ? 68  ARG B O   1 
ATOM   3591 C CB  . ARG B 2 68  ? -60.463 38.425 61.709  1.00 34.85  ? 68  ARG B CB  1 
ATOM   3592 C CG  . ARG B 2 68  ? -61.231 37.401 62.527  1.00 35.48  ? 68  ARG B CG  1 
ATOM   3593 C CD  . ARG B 2 68  ? -61.654 37.971 63.885  1.00 38.65  ? 68  ARG B CD  1 
ATOM   3594 N NE  . ARG B 2 68  ? -60.528 38.176 64.793  1.00 36.39  ? 68  ARG B NE  1 
ATOM   3595 C CZ  . ARG B 2 68  ? -60.253 39.318 65.409  1.00 36.39  ? 68  ARG B CZ  1 
ATOM   3596 N NH1 . ARG B 2 68  ? -60.983 40.403 65.215  1.00 40.02  ? 68  ARG B NH1 1 
ATOM   3597 N NH2 . ARG B 2 68  ? -59.220 39.371 66.246  1.00 41.21  ? 68  ARG B NH2 1 
ATOM   3598 N N   . VAL B 2 69  ? -58.511 38.767 58.819  1.00 40.51  ? 69  VAL B N   1 
ATOM   3599 C CA  . VAL B 2 69  ? -57.486 39.676 58.325  1.00 35.43  ? 69  VAL B CA  1 
ATOM   3600 C C   . VAL B 2 69  ? -57.635 39.817 56.819  1.00 34.19  ? 69  VAL B C   1 
ATOM   3601 O O   . VAL B 2 69  ? -57.812 38.822 56.107  1.00 37.01  ? 69  VAL B O   1 
ATOM   3602 C CB  . VAL B 2 69  ? -56.075 39.190 58.698  1.00 32.91  ? 69  VAL B CB  1 
ATOM   3603 C CG1 . VAL B 2 69  ? -55.021 40.023 57.989  1.00 35.30  ? 69  VAL B CG1 1 
ATOM   3604 C CG2 . VAL B 2 69  ? -55.880 39.261 60.198  1.00 40.49  ? 69  VAL B CG2 1 
ATOM   3605 N N   . THR B 2 70  ? -57.577 41.057 56.341  1.00 32.70  ? 70  THR B N   1 
ATOM   3606 C CA  . THR B 2 70  ? -57.450 41.349 54.921  1.00 36.72  ? 70  THR B CA  1 
ATOM   3607 C C   . THR B 2 70  ? -56.421 42.455 54.768  1.00 39.51  ? 70  THR B C   1 
ATOM   3608 O O   . THR B 2 70  ? -56.544 43.510 55.399  1.00 43.47  ? 70  THR B O   1 
ATOM   3609 C CB  . THR B 2 70  ? -58.782 41.787 54.294  1.00 42.63  ? 70  THR B CB  1 
ATOM   3610 O OG1 . THR B 2 70  ? -59.733 40.718 54.370  1.00 44.07  ? 70  THR B OG1 1 
ATOM   3611 C CG2 . THR B 2 70  ? -58.574 42.162 52.831  1.00 39.64  ? 70  THR B CG2 1 
ATOM   3612 N N   . THR B 2 71  ? -55.401 42.209 53.957  1.00 35.61  ? 71  THR B N   1 
ATOM   3613 C CA  . THR B 2 71  ? -54.440 43.235 53.599  1.00 37.03  ? 71  THR B CA  1 
ATOM   3614 C C   . THR B 2 71  ? -54.592 43.566 52.124  1.00 35.67  ? 71  THR B C   1 
ATOM   3615 O O   . THR B 2 71  ? -55.167 42.804 51.345  1.00 40.74  ? 71  THR B O   1 
ATOM   3616 C CB  . THR B 2 71  ? -52.997 42.801 53.892  1.00 38.33  ? 71  THR B CB  1 
ATOM   3617 O OG1 . THR B 2 71  ? -52.701 41.597 53.175  1.00 35.89  ? 71  THR B OG1 1 
ATOM   3618 C CG2 . THR B 2 71  ? -52.791 42.576 55.385  1.00 28.98  ? 71  THR B CG2 1 
ATOM   3619 N N   . SER B 2 72  ? -54.072 44.727 51.751  1.00 40.64  ? 72  SER B N   1 
ATOM   3620 C CA  . SER B 2 72  ? -54.126 45.175 50.370  1.00 41.70  ? 72  SER B CA  1 
ATOM   3621 C C   . SER B 2 72  ? -52.987 46.156 50.164  1.00 33.54  ? 72  SER B C   1 
ATOM   3622 O O   . SER B 2 72  ? -52.430 46.694 51.122  1.00 34.92  ? 72  SER B O   1 
ATOM   3623 C CB  . SER B 2 72  ? -55.477 45.822 50.035  1.00 39.91  ? 72  SER B CB  1 
ATOM   3624 O OG  . SER B 2 72  ? -55.522 47.171 50.477  1.00 46.13  ? 72  SER B OG  1 
ATOM   3625 N N   . VAL B 2 73  ? -52.647 46.383 48.903  1.00 37.10  ? 73  VAL B N   1 
ATOM   3626 C CA  . VAL B 2 73  ? -51.587 47.313 48.543  1.00 38.98  ? 73  VAL B CA  1 
ATOM   3627 C C   . VAL B 2 73  ? -52.073 48.174 47.388  1.00 39.40  ? 73  VAL B C   1 
ATOM   3628 O O   . VAL B 2 73  ? -52.774 47.693 46.491  1.00 40.65  ? 73  VAL B O   1 
ATOM   3629 C CB  . VAL B 2 73  ? -50.276 46.580 48.178  1.00 39.43  ? 73  VAL B CB  1 
ATOM   3630 C CG1 . VAL B 2 73  ? -50.483 45.645 46.991  1.00 34.11  ? 73  VAL B CG1 1 
ATOM   3631 C CG2 . VAL B 2 73  ? -49.160 47.581 47.897  1.00 39.34  ? 73  VAL B CG2 1 
ATOM   3632 N N   . ASP B 2 74  ? -51.717 49.451 47.428  1.00 43.49  ? 74  ASP B N   1 
ATOM   3633 C CA  . ASP B 2 74  ? -52.009 50.406 46.366  1.00 43.88  ? 74  ASP B CA  1 
ATOM   3634 C C   . ASP B 2 74  ? -50.670 50.826 45.769  1.00 47.54  ? 74  ASP B C   1 
ATOM   3635 O O   . ASP B 2 74  ? -49.960 51.660 46.339  1.00 46.90  ? 74  ASP B O   1 
ATOM   3636 C CB  . ASP B 2 74  ? -52.788 51.597 46.911  1.00 43.07  ? 74  ASP B CB  1 
ATOM   3637 C CG  . ASP B 2 74  ? -53.411 52.440 45.815  1.00 51.37  ? 74  ASP B CG  1 
ATOM   3638 O OD1 . ASP B 2 74  ? -52.677 52.823 44.873  1.00 48.05  ? 74  ASP B OD1 1 
ATOM   3639 O OD2 . ASP B 2 74  ? -54.629 52.725 45.903  1.00 49.65  ? 74  ASP B OD2 1 
ATOM   3640 N N   . THR B 2 75  ? -50.319 50.239 44.621  1.00 47.88  ? 75  THR B N   1 
ATOM   3641 C CA  . THR B 2 75  ? -49.033 50.561 44.013  1.00 52.13  ? 75  THR B CA  1 
ATOM   3642 C C   . THR B 2 75  ? -49.008 51.983 43.468  1.00 46.14  ? 75  THR B C   1 
ATOM   3643 O O   . THR B 2 75  ? -47.935 52.586 43.362  1.00 48.96  ? 75  THR B O   1 
ATOM   3644 C CB  . THR B 2 75  ? -48.698 49.560 42.903  1.00 52.71  ? 75  THR B CB  1 
ATOM   3645 O OG1 . THR B 2 75  ? -49.890 49.199 42.199  1.00 59.84  ? 75  THR B OG1 1 
ATOM   3646 C CG2 . THR B 2 75  ? -48.071 48.307 43.498  1.00 54.30  ? 75  THR B CG2 1 
ATOM   3647 N N   . ALA B 2 76  ? -50.171 52.545 43.140  1.00 49.93  ? 76  ALA B N   1 
ATOM   3648 C CA  . ALA B 2 76  ? -50.203 53.905 42.611  1.00 50.59  ? 76  ALA B CA  1 
ATOM   3649 C C   . ALA B 2 76  ? -49.996 54.948 43.708  1.00 49.80  ? 76  ALA B C   1 
ATOM   3650 O O   . ALA B 2 76  ? -49.310 55.953 43.489  1.00 52.29  ? 76  ALA B O   1 
ATOM   3651 C CB  . ALA B 2 76  ? -51.522 54.149 41.878  1.00 44.35  ? 76  ALA B CB  1 
ATOM   3652 N N   . THR B 2 77  ? -50.570 54.732 44.889  1.00 44.46  ? 77  THR B N   1 
ATOM   3653 C CA  . THR B 2 77  ? -50.465 55.691 45.979  1.00 47.02  ? 77  THR B CA  1 
ATOM   3654 C C   . THR B 2 77  ? -49.373 55.343 46.984  1.00 46.90  ? 77  THR B C   1 
ATOM   3655 O O   . THR B 2 77  ? -49.162 56.108 47.930  1.00 49.33  ? 77  THR B O   1 
ATOM   3656 C CB  . THR B 2 77  ? -51.808 55.820 46.706  1.00 50.19  ? 77  THR B CB  1 
ATOM   3657 O OG1 . THR B 2 77  ? -52.085 54.615 47.431  1.00 49.15  ? 77  THR B OG1 1 
ATOM   3658 C CG2 . THR B 2 77  ? -52.934 56.088 45.711  1.00 48.91  ? 77  THR B CG2 1 
ATOM   3659 N N   . ASN B 2 78  ? -48.684 54.212 46.807  1.00 46.85  ? 78  ASN B N   1 
ATOM   3660 C CA  . ASN B 2 78  ? -47.595 53.797 47.698  1.00 49.75  ? 78  ASN B CA  1 
ATOM   3661 C C   . ASN B 2 78  ? -48.082 53.588 49.132  1.00 46.05  ? 78  ASN B C   1 
ATOM   3662 O O   . ASN B 2 78  ? -47.448 54.026 50.097  1.00 40.65  ? 78  ASN B O   1 
ATOM   3663 C CB  . ASN B 2 78  ? -46.442 54.800 47.667  1.00 49.66  ? 78  ASN B CB  1 
ATOM   3664 C CG  . ASN B 2 78  ? -45.111 54.139 47.449  1.00 54.29  ? 78  ASN B CG  1 
ATOM   3665 O OD1 . ASN B 2 78  ? -44.961 53.290 46.565  1.00 55.23  ? 78  ASN B OD1 1 
ATOM   3666 N ND2 . ASN B 2 78  ? -44.129 54.514 48.261  1.00 56.53  ? 78  ASN B ND2 1 
ATOM   3667 N N   . GLN B 2 79  ? -49.216 52.913 49.272  1.00 42.80  ? 79  GLN B N   1 
ATOM   3668 C CA  . GLN B 2 79  ? -49.803 52.636 50.570  1.00 44.05  ? 79  GLN B CA  1 
ATOM   3669 C C   . GLN B 2 79  ? -50.201 51.172 50.634  1.00 41.29  ? 79  GLN B C   1 
ATOM   3670 O O   . GLN B 2 79  ? -50.397 50.515 49.609  1.00 39.13  ? 79  GLN B O   1 
ATOM   3671 C CB  . GLN B 2 79  ? -51.031 53.519 50.839  1.00 40.52  ? 79  GLN B CB  1 
ATOM   3672 C CG  . GLN B 2 79  ? -50.768 55.012 50.729  1.00 44.97  ? 79  GLN B CG  1 
ATOM   3673 C CD  . GLN B 2 79  ? -52.045 55.822 50.673  1.00 43.89  ? 79  GLN B CD  1 
ATOM   3674 O OE1 . GLN B 2 79  ? -52.842 55.676 49.750  1.00 49.90  ? 79  GLN B OE1 1 
ATOM   3675 N NE2 . GLN B 2 79  ? -52.253 56.674 51.670  1.00 44.22  ? 79  GLN B NE2 1 
ATOM   3676 N N   . PHE B 2 80  ? -50.311 50.663 51.857  1.00 36.87  ? 80  PHE B N   1 
ATOM   3677 C CA  . PHE B 2 80  ? -50.903 49.356 52.083  1.00 39.70  ? 80  PHE B CA  1 
ATOM   3678 C C   . PHE B 2 80  ? -51.801 49.453 53.306  1.00 39.28  ? 80  PHE B C   1 
ATOM   3679 O O   . PHE B 2 80  ? -51.680 50.374 54.118  1.00 40.24  ? 80  PHE B O   1 
ATOM   3680 C CB  . PHE B 2 80  ? -49.844 48.242 52.226  1.00 41.22  ? 80  PHE B CB  1 
ATOM   3681 C CG  . PHE B 2 80  ? -48.880 48.434 53.366  1.00 36.21  ? 80  PHE B CG  1 
ATOM   3682 C CD1 . PHE B 2 80  ? -47.818 49.319 53.253  1.00 33.58  ? 80  PHE B CD1 1 
ATOM   3683 C CD2 . PHE B 2 80  ? -49.021 47.700 54.539  1.00 38.38  ? 80  PHE B CD2 1 
ATOM   3684 C CE1 . PHE B 2 80  ? -46.924 49.490 54.296  1.00 35.38  ? 80  PHE B CE1 1 
ATOM   3685 C CE2 . PHE B 2 80  ? -48.132 47.857 55.587  1.00 33.93  ? 80  PHE B CE2 1 
ATOM   3686 C CZ  . PHE B 2 80  ? -47.079 48.758 55.467  1.00 37.92  ? 80  PHE B CZ  1 
ATOM   3687 N N   . SER B 2 81  ? -52.728 48.505 53.415  1.00 40.33  ? 81  SER B N   1 
ATOM   3688 C CA  . SER B 2 81  ? -53.840 48.625 54.342  1.00 41.25  ? 81  SER B CA  1 
ATOM   3689 C C   . SER B 2 81  ? -54.049 47.331 55.111  1.00 32.77  ? 81  SER B C   1 
ATOM   3690 O O   . SER B 2 81  ? -53.541 46.269 54.744  1.00 36.56  ? 81  SER B O   1 
ATOM   3691 C CB  . SER B 2 81  ? -55.133 49.007 53.608  1.00 38.03  ? 81  SER B CB  1 
ATOM   3692 O OG  . SER B 2 81  ? -55.131 50.391 53.301  1.00 49.57  ? 81  SER B OG  1 
ATOM   3693 N N   . LEU B 2 82  ? -54.821 47.444 56.188  1.00 35.94  ? 82  LEU B N   1 
ATOM   3694 C CA  . LEU B 2 82  ? -55.189 46.319 57.030  1.00 36.88  ? 82  LEU B CA  1 
ATOM   3695 C C   . LEU B 2 82  ? -56.670 46.423 57.359  1.00 34.70  ? 82  LEU B C   1 
ATOM   3696 O O   . LEU B 2 82  ? -57.175 47.511 57.653  1.00 39.46  ? 82  LEU B O   1 
ATOM   3697 C CB  . LEU B 2 82  ? -54.347 46.297 58.316  1.00 34.18  ? 82  LEU B CB  1 
ATOM   3698 C CG  . LEU B 2 82  ? -54.403 45.146 59.333  1.00 31.97  ? 82  LEU B CG  1 
ATOM   3699 C CD1 . LEU B 2 82  ? -55.264 45.508 60.519  1.00 39.06  ? 82  LEU B CD1 1 
ATOM   3700 C CD2 . LEU B 2 82  ? -54.864 43.831 58.719  1.00 35.40  ? 82  LEU B CD2 1 
ATOM   3701 N N   . ARG B 2 83  ? -57.366 45.293 57.286  1.00 33.72  ? 83  ARG B N   1 
ATOM   3702 C CA  . ARG B 2 83  ? -58.749 45.194 57.736  1.00 40.60  ? 83  ARG B CA  1 
ATOM   3703 C C   . ARG B 2 83  ? -58.854 44.017 58.693  1.00 40.78  ? 83  ARG B C   1 
ATOM   3704 O O   . ARG B 2 83  ? -58.568 42.874 58.316  1.00 37.44  ? 83  ARG B O   1 
ATOM   3705 C CB  . ARG B 2 83  ? -59.716 45.036 56.556  1.00 34.18  ? 83  ARG B CB  1 
ATOM   3706 C CG  . ARG B 2 83  ? -60.184 46.368 55.975  1.00 38.53  ? 83  ARG B CG  1 
ATOM   3707 C CD  . ARG B 2 83  ? -60.467 46.262 54.485  1.00 49.36  ? 83  ARG B CD  1 
ATOM   3708 N N   . LEU B 2 84  ? -59.232 44.306 59.934  1.00 36.09  ? 84  LEU B N   1 
ATOM   3709 C CA  . LEU B 2 84  ? -59.459 43.299 60.960  1.00 36.23  ? 84  LEU B CA  1 
ATOM   3710 C C   . LEU B 2 84  ? -60.917 43.384 61.382  1.00 40.23  ? 84  LEU B C   1 
ATOM   3711 O O   . LEU B 2 84  ? -61.343 44.401 61.939  1.00 41.64  ? 84  LEU B O   1 
ATOM   3712 C CB  . LEU B 2 84  ? -58.530 43.519 62.156  1.00 34.51  ? 84  LEU B CB  1 
ATOM   3713 C CG  . LEU B 2 84  ? -58.612 42.485 63.279  1.00 39.63  ? 84  LEU B CG  1 
ATOM   3714 C CD1 . LEU B 2 84  ? -57.971 41.165 62.852  1.00 33.08  ? 84  LEU B CD1 1 
ATOM   3715 C CD2 . LEU B 2 84  ? -57.970 43.030 64.552  1.00 40.21  ? 84  LEU B CD2 1 
ATOM   3716 N N   . SER B 2 85  ? -61.680 42.330 61.113  1.00 37.28  ? 85  SER B N   1 
ATOM   3717 C CA  . SER B 2 85  ? -63.116 42.355 61.354  1.00 41.14  ? 85  SER B CA  1 
ATOM   3718 C C   . SER B 2 85  ? -63.450 41.763 62.718  1.00 40.73  ? 85  SER B C   1 
ATOM   3719 O O   . SER B 2 85  ? -62.636 41.076 63.340  1.00 37.49  ? 85  SER B O   1 
ATOM   3720 C CB  . SER B 2 85  ? -63.866 41.597 60.257  1.00 34.07  ? 85  SER B CB  1 
ATOM   3721 O OG  . SER B 2 85  ? -63.303 40.314 60.059  1.00 37.49  ? 85  SER B OG  1 
ATOM   3722 N N   . SER B 2 86  ? -64.670 42.058 63.175  1.00 37.86  ? 86  SER B N   1 
ATOM   3723 C CA  . SER B 2 86  ? -65.235 41.511 64.410  1.00 40.05  ? 86  SER B CA  1 
ATOM   3724 C C   . SER B 2 86  ? -64.278 41.691 65.589  1.00 39.17  ? 86  SER B C   1 
ATOM   3725 O O   . SER B 2 86  ? -63.884 40.736 66.260  1.00 39.48  ? 86  SER B O   1 
ATOM   3726 C CB  . SER B 2 86  ? -65.607 40.036 64.230  1.00 34.88  ? 86  SER B CB  1 
ATOM   3727 O OG  . SER B 2 86  ? -66.114 39.797 62.928  1.00 42.77  ? 86  SER B OG  1 
ATOM   3728 N N   . VAL B 2 87  ? -63.905 42.939 65.833  1.00 38.06  ? 87  VAL B N   1 
ATOM   3729 C CA  . VAL B 2 87  ? -62.936 43.223 66.882  1.00 39.79  ? 87  VAL B CA  1 
ATOM   3730 C C   . VAL B 2 87  ? -63.609 43.114 68.241  1.00 45.01  ? 87  VAL B C   1 
ATOM   3731 O O   . VAL B 2 87  ? -64.801 43.407 68.405  1.00 42.33  ? 87  VAL B O   1 
ATOM   3732 C CB  . VAL B 2 87  ? -62.280 44.606 66.692  1.00 40.65  ? 87  VAL B CB  1 
ATOM   3733 C CG1 . VAL B 2 87  ? -61.561 44.674 65.353  1.00 34.44  ? 87  VAL B CG1 1 
ATOM   3734 C CG2 . VAL B 2 87  ? -63.315 45.722 66.833  1.00 42.09  ? 87  VAL B CG2 1 
ATOM   3735 N N   . THR B 2 88  ? -62.832 42.660 69.216  1.00 41.99  ? 88  THR B N   1 
ATOM   3736 C CA  . THR B 2 88  ? -63.180 42.658 70.625  1.00 37.79  ? 88  THR B CA  1 
ATOM   3737 C C   . THR B 2 88  ? -62.137 43.477 71.377  1.00 41.74  ? 88  THR B C   1 
ATOM   3738 O O   . THR B 2 88  ? -61.165 43.965 70.792  1.00 41.25  ? 88  THR B O   1 
ATOM   3739 C CB  . THR B 2 88  ? -63.256 41.228 71.170  1.00 39.47  ? 88  THR B CB  1 
ATOM   3740 O OG1 . THR B 2 88  ? -61.930 40.701 71.310  1.00 38.28  ? 88  THR B OG1 1 
ATOM   3741 C CG2 . THR B 2 88  ? -64.058 40.332 70.229  1.00 31.30  ? 88  THR B CG2 1 
ATOM   3742 N N   . ALA B 2 89  ? -62.336 43.615 72.691  1.00 36.23  ? 89  ALA B N   1 
ATOM   3743 C CA  . ALA B 2 89  ? -61.368 44.346 73.502  1.00 40.60  ? 89  ALA B CA  1 
ATOM   3744 C C   . ALA B 2 89  ? -59.981 43.725 73.409  1.00 38.76  ? 89  ALA B C   1 
ATOM   3745 O O   . ALA B 2 89  ? -58.977 44.416 73.613  1.00 41.24  ? 89  ALA B O   1 
ATOM   3746 C CB  . ALA B 2 89  ? -61.826 44.403 74.960  1.00 42.58  ? 89  ALA B CB  1 
ATOM   3747 N N   . ALA B 2 90  ? -59.903 42.431 73.090  1.00 38.16  ? 90  ALA B N   1 
ATOM   3748 C CA  . ALA B 2 90  ? -58.617 41.769 72.898  1.00 38.08  ? 90  ALA B CA  1 
ATOM   3749 C C   . ALA B 2 90  ? -57.822 42.341 71.729  1.00 41.54  ? 90  ALA B C   1 
ATOM   3750 O O   . ALA B 2 90  ? -56.621 42.073 71.634  1.00 40.09  ? 90  ALA B O   1 
ATOM   3751 C CB  . ALA B 2 90  ? -58.831 40.271 72.690  1.00 34.60  ? 90  ALA B CB  1 
ATOM   3752 N N   . ASP B 2 91  ? -58.452 43.112 70.843  1.00 37.97  ? 91  ASP B N   1 
ATOM   3753 C CA  . ASP B 2 91  ? -57.772 43.713 69.705  1.00 37.76  ? 91  ASP B CA  1 
ATOM   3754 C C   . ASP B 2 91  ? -57.301 45.132 69.990  1.00 37.25  ? 91  ASP B C   1 
ATOM   3755 O O   . ASP B 2 91  ? -56.679 45.754 69.121  1.00 33.92  ? 91  ASP B O   1 
ATOM   3756 C CB  . ASP B 2 91  ? -58.687 43.696 68.475  1.00 37.48  ? 91  ASP B CB  1 
ATOM   3757 C CG  . ASP B 2 91  ? -59.062 42.285 68.052  1.00 41.99  ? 91  ASP B CG  1 
ATOM   3758 O OD1 . ASP B 2 91  ? -58.143 41.502 67.729  1.00 40.67  ? 91  ASP B OD1 1 
ATOM   3759 O OD2 . ASP B 2 91  ? -60.269 41.956 68.045  1.00 41.13  ? 91  ASP B OD2 1 
ATOM   3760 N N   . THR B 2 92  ? -57.591 45.661 71.176  1.00 36.55  ? 92  THR B N   1 
ATOM   3761 C CA  . THR B 2 92  ? -57.040 46.947 71.578  1.00 36.83  ? 92  THR B CA  1 
ATOM   3762 C C   . THR B 2 92  ? -55.527 46.844 71.658  1.00 33.18  ? 92  THR B C   1 
ATOM   3763 O O   . THR B 2 92  ? -54.995 46.045 72.432  1.00 38.40  ? 92  THR B O   1 
ATOM   3764 C CB  . THR B 2 92  ? -57.620 47.370 72.927  1.00 36.06  ? 92  THR B CB  1 
ATOM   3765 O OG1 . THR B 2 92  ? -58.997 47.724 72.759  1.00 40.40  ? 92  THR B OG1 1 
ATOM   3766 C CG2 . THR B 2 92  ? -56.858 48.563 73.497  1.00 30.06  ? 92  THR B CG2 1 
ATOM   3767 N N   . ALA B 2 93  ? -54.833 47.650 70.862  1.00 35.87  ? 93  ALA B N   1 
ATOM   3768 C CA  . ALA B 2 93  ? -53.386 47.525 70.751  1.00 32.47  ? 93  ALA B CA  1 
ATOM   3769 C C   . ALA B 2 93  ? -52.838 48.733 70.009  1.00 36.82  ? 93  ALA B C   1 
ATOM   3770 O O   . ALA B 2 93  ? -53.580 49.504 69.395  1.00 33.20  ? 93  ALA B O   1 
ATOM   3771 C CB  . ALA B 2 93  ? -52.992 46.235 70.026  1.00 31.05  ? 93  ALA B CB  1 
ATOM   3772 N N   . VAL B 2 94  ? -51.520 48.891 70.092  1.00 34.07  ? 94  VAL B N   1 
ATOM   3773 C CA  . VAL B 2 94  ? -50.788 49.757 69.178  1.00 32.24  ? 94  VAL B CA  1 
ATOM   3774 C C   . VAL B 2 94  ? -50.494 48.954 67.922  1.00 33.92  ? 94  VAL B C   1 
ATOM   3775 O O   . VAL B 2 94  ? -49.927 47.858 67.995  1.00 35.99  ? 94  VAL B O   1 
ATOM   3776 C CB  . VAL B 2 94  ? -49.489 50.269 69.825  1.00 34.87  ? 94  VAL B CB  1 
ATOM   3777 C CG1 . VAL B 2 94  ? -48.638 51.013 68.803  1.00 33.98  ? 94  VAL B CG1 1 
ATOM   3778 C CG2 . VAL B 2 94  ? -49.796 51.155 71.018  1.00 35.07  ? 94  VAL B CG2 1 
ATOM   3779 N N   . TYR B 2 95  ? -50.897 49.474 66.772  1.00 33.83  ? 95  TYR B N   1 
ATOM   3780 C CA  . TYR B 2 95  ? -50.710 48.777 65.507  1.00 34.07  ? 95  TYR B CA  1 
ATOM   3781 C C   . TYR B 2 95  ? -49.576 49.443 64.736  1.00 37.45  ? 95  TYR B C   1 
ATOM   3782 O O   . TYR B 2 95  ? -49.664 50.627 64.393  1.00 35.17  ? 95  TYR B O   1 
ATOM   3783 C CB  . TYR B 2 95  ? -52.004 48.767 64.692  1.00 34.45  ? 95  TYR B CB  1 
ATOM   3784 C CG  . TYR B 2 95  ? -53.051 47.818 65.237  1.00 34.60  ? 95  TYR B CG  1 
ATOM   3785 C CD1 . TYR B 2 95  ? -53.708 48.089 66.435  1.00 34.36  ? 95  TYR B CD1 1 
ATOM   3786 C CD2 . TYR B 2 95  ? -53.371 46.645 64.565  1.00 34.23  ? 95  TYR B CD2 1 
ATOM   3787 C CE1 . TYR B 2 95  ? -54.656 47.222 66.941  1.00 34.31  ? 95  TYR B CE1 1 
ATOM   3788 C CE2 . TYR B 2 95  ? -54.319 45.769 65.067  1.00 29.19  ? 95  TYR B CE2 1 
ATOM   3789 C CZ  . TYR B 2 95  ? -54.953 46.063 66.252  1.00 33.47  ? 95  TYR B CZ  1 
ATOM   3790 O OH  . TYR B 2 95  ? -55.892 45.201 66.756  1.00 37.28  ? 95  TYR B OH  1 
ATOM   3791 N N   . PHE B 2 96  ? -48.509 48.686 64.491  1.00 35.09  ? 96  PHE B N   1 
ATOM   3792 C CA  . PHE B 2 96  ? -47.379 49.138 63.694  1.00 34.74  ? 96  PHE B CA  1 
ATOM   3793 C C   . PHE B 2 96  ? -47.514 48.608 62.274  1.00 37.07  ? 96  PHE B C   1 
ATOM   3794 O O   . PHE B 2 96  ? -47.879 47.446 62.065  1.00 32.19  ? 96  PHE B O   1 
ATOM   3795 C CB  . PHE B 2 96  ? -46.045 48.650 64.273  1.00 32.51  ? 96  PHE B CB  1 
ATOM   3796 C CG  . PHE B 2 96  ? -45.781 49.082 65.692  1.00 37.10  ? 96  PHE B CG  1 
ATOM   3797 C CD1 . PHE B 2 96  ? -45.224 50.327 65.963  1.00 38.11  ? 96  PHE B CD1 1 
ATOM   3798 C CD2 . PHE B 2 96  ? -46.058 48.226 66.754  1.00 31.83  ? 96  PHE B CD2 1 
ATOM   3799 C CE1 . PHE B 2 96  ? -44.967 50.721 67.269  1.00 38.44  ? 96  PHE B CE1 1 
ATOM   3800 C CE2 . PHE B 2 96  ? -45.800 48.609 68.062  1.00 33.22  ? 96  PHE B CE2 1 
ATOM   3801 C CZ  . PHE B 2 96  ? -45.259 49.858 68.322  1.00 35.38  ? 96  PHE B CZ  1 
ATOM   3802 N N   . CYS B 2 97  ? -47.214 49.454 61.299  1.00 35.51  ? 97  CYS B N   1 
ATOM   3803 C CA  . CYS B 2 97  ? -46.886 48.963 59.973  1.00 35.43  ? 97  CYS B CA  1 
ATOM   3804 C C   . CYS B 2 97  ? -45.368 48.891 59.857  1.00 36.24  ? 97  CYS B C   1 
ATOM   3805 O O   . CYS B 2 97  ? -44.639 49.637 60.519  1.00 35.91  ? 97  CYS B O   1 
ATOM   3806 C CB  . CYS B 2 97  ? -47.489 49.843 58.871  1.00 37.25  ? 97  CYS B CB  1 
ATOM   3807 S SG  . CYS B 2 97  ? -46.969 51.586 58.812  1.00 42.30  ? 97  CYS B SG  1 
ATOM   3808 N N   . ALA B 2 98  ? -44.889 47.959 59.041  1.00 34.52  ? 98  ALA B N   1 
ATOM   3809 C CA  . ALA B 2 98  ? -43.454 47.717 59.015  1.00 37.98  ? 98  ALA B CA  1 
ATOM   3810 C C   . ALA B 2 98  ? -43.067 47.107 57.683  1.00 38.24  ? 98  ALA B C   1 
ATOM   3811 O O   . ALA B 2 98  ? -43.825 46.330 57.094  1.00 39.32  ? 98  ALA B O   1 
ATOM   3812 C CB  . ALA B 2 98  ? -43.013 46.799 60.161  1.00 39.52  ? 98  ALA B CB  1 
ATOM   3813 N N   . ARG B 2 99  ? -41.882 47.480 57.212  1.00 40.70  ? 99  ARG B N   1 
ATOM   3814 C CA  . ARG B 2 99  ? -41.287 46.812 56.068  1.00 38.75  ? 99  ARG B CA  1 
ATOM   3815 C C   . ARG B 2 99  ? -40.623 45.526 56.537  1.00 38.08  ? 99  ARG B C   1 
ATOM   3816 O O   . ARG B 2 99  ? -39.911 45.515 57.546  1.00 32.25  ? 99  ARG B O   1 
ATOM   3817 C CB  . ARG B 2 99  ? -40.269 47.713 55.374  1.00 38.95  ? 99  ARG B CB  1 
ATOM   3818 C CG  . ARG B 2 99  ? -39.828 47.171 54.018  1.00 43.10  ? 99  ARG B CG  1 
ATOM   3819 C CD  . ARG B 2 99  ? -38.808 48.076 53.353  1.00 38.02  ? 99  ARG B CD  1 
ATOM   3820 N NE  . ARG B 2 99  ? -37.478 47.894 53.916  1.00 39.17  ? 99  ARG B NE  1 
ATOM   3821 C CZ  . ARG B 2 99  ? -36.374 48.410 53.397  1.00 39.78  ? 99  ARG B CZ  1 
ATOM   3822 N NH1 . ARG B 2 99  ? -36.411 49.159 52.308  1.00 42.16  ? 99  ARG B NH1 1 
ATOM   3823 N NH2 . ARG B 2 99  ? -35.206 48.169 53.985  1.00 35.83  ? 99  ARG B NH2 1 
ATOM   3824 N N   . SER B 2 100 ? -40.866 44.439 55.814  1.00 38.90  ? 100 SER B N   1 
ATOM   3825 C CA  . SER B 2 100 ? -40.321 43.136 56.157  1.00 38.48  ? 100 SER B CA  1 
ATOM   3826 C C   . SER B 2 100 ? -39.391 42.675 55.050  1.00 37.08  ? 100 SER B C   1 
ATOM   3827 O O   . SER B 2 100 ? -39.785 42.626 53.879  1.00 35.87  ? 100 SER B O   1 
ATOM   3828 C CB  . SER B 2 100 ? -41.432 42.115 56.383  1.00 33.90  ? 100 SER B CB  1 
ATOM   3829 O OG  . SER B 2 100 ? -42.643 42.777 56.688  1.00 37.31  ? 100 SER B OG  1 
ATOM   3830 N N   . ARG B 2 101 ? -38.155 42.359 55.423  1.00 35.41  ? 101 ARG B N   1 
ATOM   3831 C CA  . ARG B 2 101 ? -37.195 41.773 54.498  1.00 37.76  ? 101 ARG B CA  1 
ATOM   3832 C C   . ARG B 2 101 ? -37.545 40.298 54.331  1.00 32.71  ? 101 ARG B C   1 
ATOM   3833 O O   . ARG B 2 101 ? -37.297 39.491 55.232  1.00 36.80  ? 101 ARG B O   1 
ATOM   3834 C CB  . ARG B 2 101 ? -35.775 41.964 55.029  1.00 36.83  ? 101 ARG B CB  1 
ATOM   3835 C CG  . ARG B 2 101 ? -34.703 41.327 54.171  1.00 35.62  ? 101 ARG B CG  1 
ATOM   3836 C CD  . ARG B 2 101 ? -34.600 41.981 52.799  1.00 31.46  ? 101 ARG B CD  1 
ATOM   3837 N NE  . ARG B 2 101 ? -33.554 41.334 52.019  1.00 36.72  ? 101 ARG B NE  1 
ATOM   3838 C CZ  . ARG B 2 101 ? -33.746 40.313 51.195  1.00 36.32  ? 101 ARG B CZ  1 
ATOM   3839 N NH1 . ARG B 2 101 ? -34.961 39.865 50.913  1.00 36.50  ? 101 ARG B NH1 1 
ATOM   3840 N NH2 . ARG B 2 101 ? -32.693 39.724 50.640  1.00 38.85  ? 101 ARG B NH2 1 
ATOM   3841 N N   . GLY B 2 102 ? -38.130 39.942 53.190  1.00 32.36  ? 102 GLY B N   1 
ATOM   3842 C CA  . GLY B 2 102 ? -38.634 38.595 52.993  1.00 32.96  ? 102 GLY B CA  1 
ATOM   3843 C C   . GLY B 2 102 ? -37.975 37.828 51.862  1.00 38.61  ? 102 GLY B C   1 
ATOM   3844 O O   . GLY B 2 102 ? -37.767 38.362 50.768  1.00 37.21  ? 102 GLY B O   1 
ATOM   3845 N N   . GLU B 2 103 ? -37.646 36.564 52.118  1.00 35.63  ? 103 GLU B N   1 
ATOM   3846 C CA  . GLU B 2 103 ? -37.028 35.724 51.100  1.00 29.78  ? 103 GLU B CA  1 
ATOM   3847 C C   . GLU B 2 103 ? -37.227 34.266 51.481  1.00 31.94  ? 103 GLU B C   1 
ATOM   3848 O O   . GLU B 2 103 ? -36.765 33.830 52.541  1.00 35.88  ? 103 GLU B O   1 
ATOM   3849 C CB  . GLU B 2 103 ? -35.548 36.055 50.957  1.00 35.38  ? 103 GLU B CB  1 
ATOM   3850 C CG  . GLU B 2 103 ? -35.012 35.867 49.552  1.00 34.09  ? 103 GLU B CG  1 
ATOM   3851 C CD  . GLU B 2 103 ? -33.618 36.436 49.397  1.00 36.08  ? 103 GLU B CD  1 
ATOM   3852 O OE1 . GLU B 2 103 ? -33.469 37.656 49.596  1.00 35.97  ? 103 GLU B OE1 1 
ATOM   3853 O OE2 . GLU B 2 103 ? -32.678 35.682 49.069  1.00 35.04  ? 103 GLU B OE2 1 
ATOM   3854 N N   . GLY B 2 104 ? -37.921 33.520 50.629  1.00 31.54  ? 104 GLY B N   1 
ATOM   3855 C CA  . GLY B 2 104 ? -38.110 32.103 50.854  1.00 31.75  ? 104 GLY B CA  1 
ATOM   3856 C C   . GLY B 2 104 ? -37.634 31.287 49.673  1.00 35.09  ? 104 GLY B C   1 
ATOM   3857 O O   . GLY B 2 104 ? -37.554 31.800 48.552  1.00 32.85  ? 104 GLY B O   1 
ATOM   3858 N N   . TYR B 2 105 ? -37.316 30.017 49.904  1.00 31.20  ? 105 TYR B N   1 
ATOM   3859 C CA  . TYR B 2 105 ? -36.833 29.147 48.843  1.00 37.29  ? 105 TYR B CA  1 
ATOM   3860 C C   . TYR B 2 105 ? -37.555 27.811 48.918  1.00 37.26  ? 105 TYR B C   1 
ATOM   3861 O O   . TYR B 2 105 ? -37.713 27.241 50.003  1.00 33.48  ? 105 TYR B O   1 
ATOM   3862 C CB  . TYR B 2 105 ? -35.311 28.966 48.936  1.00 31.70  ? 105 TYR B CB  1 
ATOM   3863 C CG  . TYR B 2 105 ? -34.582 30.212 48.519  1.00 32.31  ? 105 TYR B CG  1 
ATOM   3864 C CD1 . TYR B 2 105 ? -34.372 30.500 47.172  1.00 35.79  ? 105 TYR B CD1 1 
ATOM   3865 C CD2 . TYR B 2 105 ? -34.141 31.128 49.465  1.00 31.94  ? 105 TYR B CD2 1 
ATOM   3866 C CE1 . TYR B 2 105 ? -33.718 31.660 46.780  1.00 33.17  ? 105 TYR B CE1 1 
ATOM   3867 C CE2 . TYR B 2 105 ? -33.490 32.290 49.086  1.00 35.55  ? 105 TYR B CE2 1 
ATOM   3868 C CZ  . TYR B 2 105 ? -33.284 32.553 47.742  1.00 37.31  ? 105 TYR B CZ  1 
ATOM   3869 O OH  . TYR B 2 105 ? -32.637 33.709 47.360  1.00 35.51  ? 105 TYR B OH  1 
ATOM   3870 N N   . CYS B 2 106 ? -37.997 27.319 47.760  1.00 36.98  ? 106 CYS B N   1 
ATOM   3871 C CA  . CYS B 2 106 ? -38.847 26.139 47.688  1.00 38.59  ? 106 CYS B CA  1 
ATOM   3872 C C   . CYS B 2 106 ? -38.248 25.115 46.739  1.00 35.26  ? 106 CYS B C   1 
ATOM   3873 O O   . CYS B 2 106 ? -37.766 25.460 45.655  1.00 32.26  ? 106 CYS B O   1 
ATOM   3874 C CB  . CYS B 2 106 ? -40.269 26.492 47.223  1.00 30.94  ? 106 CYS B CB  1 
ATOM   3875 S SG  . CYS B 2 106 ? -40.976 27.969 47.998  1.00 41.43  ? 106 CYS B SG  1 
ATOM   3876 N N   . SER B 2 107 ? -38.289 23.854 47.160  1.00 35.46  ? 107 SER B N   1 
ATOM   3877 C CA  . SER B 2 107 ? -37.904 22.733 46.321  1.00 36.18  ? 107 SER B CA  1 
ATOM   3878 C C   . SER B 2 107 ? -38.666 21.503 46.788  1.00 34.57  ? 107 SER B C   1 
ATOM   3879 O O   . SER B 2 107 ? -38.883 21.318 47.991  1.00 34.54  ? 107 SER B O   1 
ATOM   3880 C CB  . SER B 2 107 ? -36.390 22.489 46.368  1.00 36.85  ? 107 SER B CB  1 
ATOM   3881 O OG  . SER B 2 107 ? -35.993 21.968 47.623  1.00 37.01  ? 107 SER B OG  1 
ATOM   3882 N N   . PHE B 2 108 ? -39.093 20.687 45.824  1.00 36.89  ? 108 PHE B N   1 
ATOM   3883 C CA  . PHE B 2 108 ? -39.756 19.407 46.093  1.00 39.45  ? 108 PHE B CA  1 
ATOM   3884 C C   . PHE B 2 108 ? -41.001 19.581 46.960  1.00 38.52  ? 108 PHE B C   1 
ATOM   3885 O O   . PHE B 2 108 ? -41.301 18.746 47.817  1.00 39.72  ? 108 PHE B O   1 
ATOM   3886 C CB  . PHE B 2 108 ? -38.785 18.413 46.734  1.00 39.91  ? 108 PHE B CB  1 
ATOM   3887 C CG  . PHE B 2 108 ? -37.572 18.136 45.899  1.00 40.70  ? 108 PHE B CG  1 
ATOM   3888 C CD1 . PHE B 2 108 ? -36.460 18.955 45.982  1.00 38.03  ? 108 PHE B CD1 1 
ATOM   3889 C CD2 . PHE B 2 108 ? -37.545 17.062 45.024  1.00 40.00  ? 108 PHE B CD2 1 
ATOM   3890 C CE1 . PHE B 2 108 ? -35.337 18.707 45.206  1.00 40.55  ? 108 PHE B CE1 1 
ATOM   3891 C CE2 . PHE B 2 108 ? -36.427 16.807 44.246  1.00 44.67  ? 108 PHE B CE2 1 
ATOM   3892 C CZ  . PHE B 2 108 ? -35.318 17.631 44.340  1.00 40.62  ? 108 PHE B CZ  1 
ATOM   3893 N N   . GLY B 2 109 ? -41.726 20.679 46.744  1.00 37.07  ? 109 GLY B N   1 
ATOM   3894 C CA  . GLY B 2 109 ? -43.000 20.891 47.409  1.00 44.73  ? 109 GLY B CA  1 
ATOM   3895 C C   . GLY B 2 109 ? -42.946 21.470 48.807  1.00 40.89  ? 109 GLY B C   1 
ATOM   3896 O O   . GLY B 2 109 ? -43.972 21.466 49.496  1.00 45.49  ? 109 GLY B O   1 
ATOM   3897 N N   . THR B 2 110 ? -41.796 21.968 49.251  1.00 38.29  ? 110 THR B N   1 
ATOM   3898 C CA  . THR B 2 110 ? -41.660 22.561 50.573  1.00 40.80  ? 110 THR B CA  1 
ATOM   3899 C C   . THR B 2 110 ? -40.837 23.834 50.465  1.00 39.29  ? 110 THR B C   1 
ATOM   3900 O O   . THR B 2 110 ? -39.835 23.873 49.747  1.00 38.46  ? 110 THR B O   1 
ATOM   3901 C CB  . THR B 2 110 ? -40.993 21.592 51.557  1.00 38.02  ? 110 THR B CB  1 
ATOM   3902 O OG1 . THR B 2 110 ? -41.758 20.384 51.614  1.00 44.20  ? 110 THR B OG1 1 
ATOM   3903 C CG2 . THR B 2 110 ? -40.905 22.209 52.954  1.00 32.71  ? 110 THR B CG2 1 
ATOM   3904 N N   . CYS B 2 111 ? -41.267 24.874 51.172  1.00 37.98  ? 111 CYS B N   1 
ATOM   3905 C CA  . CYS B 2 111 ? -40.554 26.139 51.207  1.00 38.67  ? 111 CYS B CA  1 
ATOM   3906 C C   . CYS B 2 111 ? -39.859 26.326 52.549  1.00 37.88  ? 111 CYS B C   1 
ATOM   3907 O O   . CYS B 2 111 ? -40.309 25.821 53.582  1.00 40.05  ? 111 CYS B O   1 
ATOM   3908 C CB  . CYS B 2 111 ? -41.501 27.309 50.944  1.00 36.18  ? 111 CYS B CB  1 
ATOM   3909 S SG  . CYS B 2 111 ? -42.323 27.231 49.346  1.00 44.52  ? 111 CYS B SG  1 
ATOM   3910 N N   . TYR B 2 112 ? -38.755 27.065 52.519  1.00 38.30  ? 112 TYR B N   1 
ATOM   3911 C CA  . TYR B 2 112 ? -37.933 27.316 53.691  1.00 27.60  ? 112 TYR B CA  1 
ATOM   3912 C C   . TYR B 2 112 ? -37.543 28.782 53.689  1.00 34.92  ? 112 TYR B C   1 
ATOM   3913 O O   . TYR B 2 112 ? -37.205 29.336 52.637  1.00 35.00  ? 112 TYR B O   1 
ATOM   3914 C CB  . TYR B 2 112 ? -36.680 26.434 53.692  1.00 33.38  ? 112 TYR B CB  1 
ATOM   3915 C CG  . TYR B 2 112 ? -36.941 24.971 53.398  1.00 35.60  ? 112 TYR B CG  1 
ATOM   3916 C CD1 . TYR B 2 112 ? -36.979 24.501 52.088  1.00 35.55  ? 112 TYR B CD1 1 
ATOM   3917 C CD2 . TYR B 2 112 ? -37.136 24.057 54.429  1.00 33.88  ? 112 TYR B CD2 1 
ATOM   3918 C CE1 . TYR B 2 112 ? -37.208 23.163 51.811  1.00 38.26  ? 112 TYR B CE1 1 
ATOM   3919 C CE2 . TYR B 2 112 ? -37.363 22.716 54.164  1.00 37.57  ? 112 TYR B CE2 1 
ATOM   3920 C CZ  . TYR B 2 112 ? -37.397 22.276 52.853  1.00 42.15  ? 112 TYR B CZ  1 
ATOM   3921 O OH  . TYR B 2 112 ? -37.622 20.947 52.580  1.00 42.88  ? 112 TYR B OH  1 
ATOM   3922 N N   . THR B 2 113 ? -37.600 29.409 54.861  1.00 33.96  ? 113 THR B N   1 
ATOM   3923 C CA  . THR B 2 113 ? -37.361 30.842 54.959  1.00 34.39  ? 113 THR B CA  1 
ATOM   3924 C C   . THR B 2 113 ? -35.870 31.133 55.037  1.00 34.41  ? 113 THR B C   1 
ATOM   3925 O O   . THR B 2 113 ? -35.144 30.497 55.807  1.00 34.05  ? 113 THR B O   1 
ATOM   3926 C CB  . THR B 2 113 ? -38.052 31.423 56.190  1.00 36.74  ? 113 THR B CB  1 
ATOM   3927 O OG1 . THR B 2 113 ? -39.443 31.086 56.163  1.00 40.40  ? 113 THR B OG1 1 
ATOM   3928 C CG2 . THR B 2 113 ? -37.893 32.944 56.227  1.00 31.10  ? 113 THR B CG2 1 
ATOM   3929 N N   . LEU B 2 114 ? -35.416 32.100 54.247  1.00 32.65  ? 114 LEU B N   1 
ATOM   3930 C CA  . LEU B 2 114 ? -34.100 32.679 54.466  1.00 32.58  ? 114 LEU B CA  1 
ATOM   3931 C C   . LEU B 2 114 ? -34.161 33.970 55.276  1.00 32.86  ? 114 LEU B C   1 
ATOM   3932 O O   . LEU B 2 114 ? -33.376 34.136 56.217  1.00 30.10  ? 114 LEU B O   1 
ATOM   3933 C CB  . LEU B 2 114 ? -33.393 32.931 53.131  1.00 29.81  ? 114 LEU B CB  1 
ATOM   3934 C CG  . LEU B 2 114 ? -31.922 33.330 53.280  1.00 34.91  ? 114 LEU B CG  1 
ATOM   3935 C CD1 . LEU B 2 114 ? -31.139 32.186 53.898  1.00 30.33  ? 114 LEU B CD1 1 
ATOM   3936 C CD2 . LEU B 2 114 ? -31.319 33.742 51.938  1.00 31.03  ? 114 LEU B CD2 1 
ATOM   3937 N N   . PHE B 2 115 ? -35.086 34.877 54.951  1.00 29.32  ? 115 PHE B N   1 
ATOM   3938 C CA  . PHE B 2 115 ? -35.267 36.119 55.696  1.00 29.62  ? 115 PHE B CA  1 
ATOM   3939 C C   . PHE B 2 115 ? -36.746 36.394 55.912  1.00 36.00  ? 115 PHE B C   1 
ATOM   3940 O O   . PHE B 2 115 ? -37.535 36.341 54.962  1.00 33.20  ? 115 PHE B O   1 
ATOM   3941 C CB  . PHE B 2 115 ? -34.667 37.325 54.962  1.00 30.51  ? 115 PHE B CB  1 
ATOM   3942 C CG  . PHE B 2 115 ? -33.204 37.214 54.681  1.00 32.64  ? 115 PHE B CG  1 
ATOM   3943 C CD1 . PHE B 2 115 ? -32.294 37.104 55.713  1.00 27.79  ? 115 PHE B CD1 1 
ATOM   3944 C CD2 . PHE B 2 115 ? -32.733 37.261 53.373  1.00 33.53  ? 115 PHE B CD2 1 
ATOM   3945 C CE1 . PHE B 2 115 ? -30.944 37.025 55.449  1.00 29.03  ? 115 PHE B CE1 1 
ATOM   3946 C CE2 . PHE B 2 115 ? -31.380 37.177 53.105  1.00 31.18  ? 115 PHE B CE2 1 
ATOM   3947 C CZ  . PHE B 2 115 ? -30.486 37.061 54.149  1.00 27.79  ? 115 PHE B CZ  1 
ATOM   3948 N N   . TYR B 2 116 ? -37.119 36.722 57.157  1.00 34.82  ? 116 TYR B N   1 
ATOM   3949 C CA  . TYR B 2 116 ? -38.399 37.401 57.375  1.00 30.93  ? 116 TYR B CA  1 
ATOM   3950 C C   . TYR B 2 116 ? -38.289 38.209 58.672  1.00 30.19  ? 116 TYR B C   1 
ATOM   3951 O O   . TYR B 2 116 ? -38.767 37.814 59.741  1.00 29.72  ? 116 TYR B O   1 
ATOM   3952 C CB  . TYR B 2 116 ? -39.595 36.452 57.411  1.00 29.77  ? 116 TYR B CB  1 
ATOM   3953 C CG  . TYR B 2 116 ? -40.874 37.203 57.127  1.00 31.25  ? 116 TYR B CG  1 
ATOM   3954 C CD1 . TYR B 2 116 ? -41.282 37.441 55.820  1.00 30.61  ? 116 TYR B CD1 1 
ATOM   3955 C CD2 . TYR B 2 116 ? -41.645 37.724 58.163  1.00 31.48  ? 116 TYR B CD2 1 
ATOM   3956 C CE1 . TYR B 2 116 ? -42.438 38.148 55.548  1.00 32.51  ? 116 TYR B CE1 1 
ATOM   3957 C CE2 . TYR B 2 116 ? -42.803 38.439 57.900  1.00 34.62  ? 116 TYR B CE2 1 
ATOM   3958 C CZ  . TYR B 2 116 ? -43.188 38.646 56.587  1.00 33.35  ? 116 TYR B CZ  1 
ATOM   3959 O OH  . TYR B 2 116 ? -44.333 39.345 56.311  1.00 38.21  ? 116 TYR B OH  1 
ATOM   3960 N N   . TYR B 2 117 ? -37.661 39.376 58.561  1.00 30.70  ? 117 TYR B N   1 
ATOM   3961 C CA  . TYR B 2 117 ? -37.458 40.264 59.693  1.00 33.45  ? 117 TYR B CA  1 
ATOM   3962 C C   . TYR B 2 117 ? -37.930 41.663 59.325  1.00 36.11  ? 117 TYR B C   1 
ATOM   3963 O O   . TYR B 2 117 ? -38.153 41.982 58.153  1.00 36.00  ? 117 TYR B O   1 
ATOM   3964 C CB  . TYR B 2 117 ? -35.984 40.278 60.155  1.00 30.39  ? 117 TYR B CB  1 
ATOM   3965 C CG  . TYR B 2 117 ? -34.966 40.756 59.137  1.00 30.04  ? 117 TYR B CG  1 
ATOM   3966 C CD1 . TYR B 2 117 ? -34.666 42.100 59.007  1.00 32.46  ? 117 TYR B CD1 1 
ATOM   3967 C CD2 . TYR B 2 117 ? -34.285 39.855 58.328  1.00 33.00  ? 117 TYR B CD2 1 
ATOM   3968 C CE1 . TYR B 2 117 ? -33.727 42.542 58.096  1.00 33.50  ? 117 TYR B CE1 1 
ATOM   3969 C CE2 . TYR B 2 117 ? -33.340 40.289 57.406  1.00 34.64  ? 117 TYR B CE2 1 
ATOM   3970 C CZ  . TYR B 2 117 ? -33.066 41.636 57.295  1.00 37.02  ? 117 TYR B CZ  1 
ATOM   3971 O OH  . TYR B 2 117 ? -32.130 42.084 56.382  1.00 34.79  ? 117 TYR B OH  1 
ATOM   3972 N N   . PHE B 2 118 ? -38.081 42.499 60.348  1.00 32.21  ? 118 PHE B N   1 
ATOM   3973 C CA  . PHE B 2 118 ? -38.714 43.808 60.214  1.00 35.92  ? 118 PHE B CA  1 
ATOM   3974 C C   . PHE B 2 118 ? -37.659 44.894 60.412  1.00 39.13  ? 118 PHE B C   1 
ATOM   3975 O O   . PHE B 2 118 ? -37.264 45.195 61.544  1.00 37.88  ? 118 PHE B O   1 
ATOM   3976 C CB  . PHE B 2 118 ? -39.869 43.920 61.205  1.00 35.80  ? 118 PHE B CB  1 
ATOM   3977 C CG  . PHE B 2 118 ? -40.765 42.709 61.203  1.00 36.24  ? 118 PHE B CG  1 
ATOM   3978 C CD1 . PHE B 2 118 ? -41.618 42.471 60.134  1.00 30.47  ? 118 PHE B CD1 1 
ATOM   3979 C CD2 . PHE B 2 118 ? -40.726 41.791 62.244  1.00 28.31  ? 118 PHE B CD2 1 
ATOM   3980 C CE1 . PHE B 2 118 ? -42.429 41.352 60.115  1.00 32.65  ? 118 PHE B CE1 1 
ATOM   3981 C CE2 . PHE B 2 118 ? -41.536 40.668 62.231  1.00 32.23  ? 118 PHE B CE2 1 
ATOM   3982 C CZ  . PHE B 2 118 ? -42.388 40.448 61.168  1.00 32.49  ? 118 PHE B CZ  1 
ATOM   3983 N N   . ASP B 2 119 ? -37.220 45.497 59.304  1.00 37.59  ? 119 ASP B N   1 
ATOM   3984 C CA  . ASP B 2 119 ? -36.096 46.423 59.355  1.00 39.88  ? 119 ASP B CA  1 
ATOM   3985 C C   . ASP B 2 119 ? -36.510 47.883 59.495  1.00 37.95  ? 119 ASP B C   1 
ATOM   3986 O O   . ASP B 2 119 ? -35.694 48.694 59.942  1.00 47.85  ? 119 ASP B O   1 
ATOM   3987 C CB  . ASP B 2 119 ? -35.198 46.248 58.119  1.00 38.62  ? 119 ASP B CB  1 
ATOM   3988 C CG  . ASP B 2 119 ? -35.935 46.459 56.804  1.00 38.93  ? 119 ASP B CG  1 
ATOM   3989 O OD1 . ASP B 2 119 ? -37.111 46.878 56.804  1.00 43.02  ? 119 ASP B OD1 1 
ATOM   3990 O OD2 . ASP B 2 119 ? -35.323 46.210 55.751  1.00 40.94  ? 119 ASP B OD2 1 
ATOM   3991 N N   . TYR B 2 120 ? -37.744 48.243 59.146  1.00 36.43  ? 120 TYR B N   1 
ATOM   3992 C CA  . TYR B 2 120 ? -38.205 49.618 59.303  1.00 39.19  ? 120 TYR B CA  1 
ATOM   3993 C C   . TYR B 2 120 ? -39.661 49.610 59.738  1.00 40.99  ? 120 TYR B C   1 
ATOM   3994 O O   . TYR B 2 120 ? -40.490 48.932 59.124  1.00 42.05  ? 120 TYR B O   1 
ATOM   3995 C CB  . TYR B 2 120 ? -38.038 50.421 58.006  1.00 44.24  ? 120 TYR B CB  1 
ATOM   3996 C CG  . TYR B 2 120 ? -36.591 50.731 57.681  1.00 51.90  ? 120 TYR B CG  1 
ATOM   3997 C CD1 . TYR B 2 120 ? -35.823 49.853 56.919  1.00 49.40  ? 120 TYR B CD1 1 
ATOM   3998 C CD2 . TYR B 2 120 ? -35.986 51.895 58.151  1.00 58.95  ? 120 TYR B CD2 1 
ATOM   3999 C CE1 . TYR B 2 120 ? -34.493 50.129 56.627  1.00 52.03  ? 120 TYR B CE1 1 
ATOM   4000 C CE2 . TYR B 2 120 ? -34.657 52.180 57.865  1.00 57.78  ? 120 TYR B CE2 1 
ATOM   4001 C CZ  . TYR B 2 120 ? -33.918 51.293 57.104  1.00 55.51  ? 120 TYR B CZ  1 
ATOM   4002 O OH  . TYR B 2 120 ? -32.602 51.570 56.818  1.00 50.68  ? 120 TYR B OH  1 
ATOM   4003 N N   . TRP B 2 121 ? -39.965 50.364 60.793  1.00 37.28  ? 121 TRP B N   1 
ATOM   4004 C CA  . TRP B 2 121 ? -41.290 50.390 61.391  1.00 39.94  ? 121 TRP B CA  1 
ATOM   4005 C C   . TRP B 2 121 ? -41.855 51.804 61.372  1.00 42.35  ? 121 TRP B C   1 
ATOM   4006 O O   . TRP B 2 121 ? -41.111 52.788 61.419  1.00 47.41  ? 121 TRP B O   1 
ATOM   4007 C CB  . TRP B 2 121 ? -41.268 49.897 62.847  1.00 37.79  ? 121 TRP B CB  1 
ATOM   4008 C CG  . TRP B 2 121 ? -40.665 48.538 63.081  1.00 37.38  ? 121 TRP B CG  1 
ATOM   4009 C CD1 . TRP B 2 121 ? -39.442 48.097 62.671  1.00 36.13  ? 121 TRP B CD1 1 
ATOM   4010 C CD2 . TRP B 2 121 ? -41.257 47.452 63.814  1.00 39.65  ? 121 TRP B CD2 1 
ATOM   4011 N NE1 . TRP B 2 121 ? -39.233 46.805 63.097  1.00 37.35  ? 121 TRP B NE1 1 
ATOM   4012 C CE2 . TRP B 2 121 ? -40.332 46.386 63.801  1.00 38.15  ? 121 TRP B CE2 1 
ATOM   4013 C CE3 . TRP B 2 121 ? -42.480 47.279 64.477  1.00 36.29  ? 121 TRP B CE3 1 
ATOM   4014 C CZ2 . TRP B 2 121 ? -40.591 45.161 64.423  1.00 31.85  ? 121 TRP B CZ2 1 
ATOM   4015 C CZ3 . TRP B 2 121 ? -42.738 46.061 65.092  1.00 36.21  ? 121 TRP B CZ3 1 
ATOM   4016 C CH2 . TRP B 2 121 ? -41.794 45.017 65.061  1.00 32.93  ? 121 TRP B CH2 1 
ATOM   4017 N N   . GLY B 2 122 ? -43.180 51.898 61.322  1.00 41.85  ? 122 GLY B N   1 
ATOM   4018 C CA  . GLY B 2 122 ? -43.853 53.149 61.582  1.00 36.93  ? 122 GLY B CA  1 
ATOM   4019 C C   . GLY B 2 122 ? -43.781 53.505 63.061  1.00 38.88  ? 122 GLY B C   1 
ATOM   4020 O O   . GLY B 2 122 ? -43.098 52.868 63.863  1.00 36.65  ? 122 GLY B O   1 
ATOM   4021 N N   . GLN B 2 123 ? -44.517 54.554 63.422  1.00 39.52  ? 123 GLN B N   1 
ATOM   4022 C CA  . GLN B 2 123 ? -44.533 55.023 64.803  1.00 40.49  ? 123 GLN B CA  1 
ATOM   4023 C C   . GLN B 2 123 ? -45.542 54.287 65.670  1.00 38.78  ? 123 GLN B C   1 
ATOM   4024 O O   . GLN B 2 123 ? -45.420 54.314 66.898  1.00 39.15  ? 123 GLN B O   1 
ATOM   4025 C CB  . GLN B 2 123 ? -44.832 56.525 64.852  1.00 41.10  ? 123 GLN B CB  1 
ATOM   4026 N N   . GLY B 2 124 ? -46.529 53.635 65.066  1.00 39.70  ? 124 GLY B N   1 
ATOM   4027 C CA  . GLY B 2 124 ? -47.563 52.973 65.832  1.00 35.99  ? 124 GLY B CA  1 
ATOM   4028 C C   . GLY B 2 124 ? -48.782 53.848 66.026  1.00 35.57  ? 124 GLY B C   1 
ATOM   4029 O O   . GLY B 2 124 ? -48.660 55.053 66.266  1.00 38.52  ? 124 GLY B O   1 
ATOM   4030 N N   . THR B 2 125 ? -49.965 53.257 65.906  1.00 39.02  ? 125 THR B N   1 
ATOM   4031 C CA  . THR B 2 125 ? -51.218 53.958 66.140  1.00 38.50  ? 125 THR B CA  1 
ATOM   4032 C C   . THR B 2 125 ? -52.043 53.151 67.133  1.00 35.04  ? 125 THR B C   1 
ATOM   4033 O O   . THR B 2 125 ? -52.252 51.948 66.947  1.00 32.77  ? 125 THR B O   1 
ATOM   4034 C CB  . THR B 2 125 ? -51.978 54.198 64.820  1.00 40.56  ? 125 THR B CB  1 
ATOM   4035 O OG1 . THR B 2 125 ? -53.127 55.018 65.060  1.00 43.98  ? 125 THR B OG1 1 
ATOM   4036 C CG2 . THR B 2 125 ? -52.403 52.893 64.147  1.00 37.68  ? 125 THR B CG2 1 
ATOM   4037 N N   . LEU B 2 126 ? -52.469 53.799 68.213  1.00 35.54  ? 126 LEU B N   1 
ATOM   4038 C CA  . LEU B 2 126 ? -53.232 53.108 69.242  1.00 33.17  ? 126 LEU B CA  1 
ATOM   4039 C C   . LEU B 2 126 ? -54.683 53.001 68.797  1.00 37.35  ? 126 LEU B C   1 
ATOM   4040 O O   . LEU B 2 126 ? -55.341 54.016 68.544  1.00 36.62  ? 126 LEU B O   1 
ATOM   4041 C CB  . LEU B 2 126 ? -53.134 53.828 70.582  1.00 33.81  ? 126 LEU B CB  1 
ATOM   4042 C CG  . LEU B 2 126 ? -53.972 53.189 71.697  1.00 37.97  ? 126 LEU B CG  1 
ATOM   4043 C CD1 . LEU B 2 126 ? -53.625 51.711 71.845  1.00 37.34  ? 126 LEU B CD1 1 
ATOM   4044 C CD2 . LEU B 2 126 ? -53.778 53.920 73.018  1.00 34.10  ? 126 LEU B CD2 1 
ATOM   4045 N N   . VAL B 2 127 ? -55.173 51.771 68.694  1.00 34.42  ? 127 VAL B N   1 
ATOM   4046 C CA  . VAL B 2 127 ? -56.572 51.496 68.404  1.00 36.86  ? 127 VAL B CA  1 
ATOM   4047 C C   . VAL B 2 127 ? -57.226 50.992 69.680  1.00 36.56  ? 127 VAL B C   1 
ATOM   4048 O O   . VAL B 2 127 ? -56.757 50.019 70.283  1.00 36.36  ? 127 VAL B O   1 
ATOM   4049 C CB  . VAL B 2 127 ? -56.727 50.473 67.268  1.00 41.00  ? 127 VAL B CB  1 
ATOM   4050 C CG1 . VAL B 2 127 ? -58.205 50.119 67.078  1.00 31.85  ? 127 VAL B CG1 1 
ATOM   4051 C CG2 . VAL B 2 127 ? -56.108 51.017 65.983  1.00 35.53  ? 127 VAL B CG2 1 
ATOM   4052 N N   . THR B 2 128 ? -58.304 51.649 70.088  1.00 35.51  ? 128 THR B N   1 
ATOM   4053 C CA  . THR B 2 128 ? -59.047 51.269 71.281  1.00 40.01  ? 128 THR B CA  1 
ATOM   4054 C C   . THR B 2 128 ? -60.400 50.723 70.851  1.00 38.27  ? 128 THR B C   1 
ATOM   4055 O O   . THR B 2 128 ? -61.189 51.436 70.224  1.00 39.93  ? 128 THR B O   1 
ATOM   4056 C CB  . THR B 2 128 ? -59.225 52.458 72.228  1.00 37.04  ? 128 THR B CB  1 
ATOM   4057 O OG1 . THR B 2 128 ? -57.941 52.943 72.637  1.00 38.60  ? 128 THR B OG1 1 
ATOM   4058 C CG2 . THR B 2 128 ? -60.006 52.043 73.464  1.00 38.59  ? 128 THR B CG2 1 
ATOM   4059 N N   . VAL B 2 129 ? -60.658 49.461 71.177  1.00 34.46  ? 129 VAL B N   1 
ATOM   4060 C CA  . VAL B 2 129 ? -61.974 48.873 70.961  1.00 39.56  ? 129 VAL B CA  1 
ATOM   4061 C C   . VAL B 2 129 ? -62.846 49.231 72.154  1.00 45.67  ? 129 VAL B C   1 
ATOM   4062 O O   . VAL B 2 129 ? -62.547 48.844 73.289  1.00 44.45  ? 129 VAL B O   1 
ATOM   4063 C CB  . VAL B 2 129 ? -61.885 47.354 70.773  1.00 40.73  ? 129 VAL B CB  1 
ATOM   4064 C CG1 . VAL B 2 129 ? -63.279 46.772 70.531  1.00 36.32  ? 129 VAL B CG1 1 
ATOM   4065 C CG2 . VAL B 2 129 ? -60.946 47.021 69.626  1.00 35.83  ? 129 VAL B CG2 1 
ATOM   4066 N N   . SER B 2 130 ? -63.914 49.986 71.906  1.00 44.21  ? 130 SER B N   1 
ATOM   4067 C CA  . SER B 2 130 ? -64.773 50.453 72.985  1.00 41.18  ? 130 SER B CA  1 
ATOM   4068 C C   . SER B 2 130 ? -66.085 50.943 72.394  1.00 47.60  ? 130 SER B C   1 
ATOM   4069 O O   . SER B 2 130 ? -66.157 51.316 71.220  1.00 48.01  ? 130 SER B O   1 
ATOM   4070 C CB  . SER B 2 130 ? -64.101 51.567 73.796  1.00 43.86  ? 130 SER B CB  1 
ATOM   4071 O OG  . SER B 2 130 ? -65.045 52.248 74.606  1.00 46.29  ? 130 SER B OG  1 
ATOM   4072 N N   . SER B 2 131 ? -67.125 50.929 73.227  1.00 53.06  ? 131 SER B N   1 
ATOM   4073 C CA  . SER B 2 131 ? -68.414 51.494 72.849  1.00 48.61  ? 131 SER B CA  1 
ATOM   4074 C C   . SER B 2 131 ? -68.528 52.974 73.179  1.00 44.98  ? 131 SER B C   1 
ATOM   4075 O O   . SER B 2 131 ? -69.361 53.664 72.583  1.00 46.85  ? 131 SER B O   1 
ATOM   4076 C CB  . SER B 2 131 ? -69.550 50.735 73.538  1.00 44.41  ? 131 SER B CB  1 
ATOM   4077 O OG  . SER B 2 131 ? -69.852 49.541 72.836  1.00 56.24  ? 131 SER B OG  1 
ATOM   4078 N N   . ALA B 2 132 ? -67.709 53.473 74.100  1.00 42.94  ? 132 ALA B N   1 
ATOM   4079 C CA  . ALA B 2 132 ? -67.761 54.876 74.477  1.00 45.50  ? 132 ALA B CA  1 
ATOM   4080 C C   . ALA B 2 132 ? -67.373 55.771 73.301  1.00 44.35  ? 132 ALA B C   1 
ATOM   4081 O O   . ALA B 2 132 ? -66.688 55.356 72.361  1.00 51.61  ? 132 ALA B O   1 
ATOM   4082 C CB  . ALA B 2 132 ? -66.840 55.142 75.670  1.00 37.85  ? 132 ALA B CB  1 
ATOM   4083 N N   . SER B 2 133 ? -67.833 57.014 73.359  1.00 45.85  ? 133 SER B N   1 
ATOM   4084 C CA  . SER B 2 133 ? -67.495 58.017 72.361  1.00 52.73  ? 133 SER B CA  1 
ATOM   4085 C C   . SER B 2 133 ? -66.313 58.850 72.840  1.00 50.77  ? 133 SER B C   1 
ATOM   4086 O O   . SER B 2 133 ? -65.880 58.763 73.991  1.00 53.13  ? 133 SER B O   1 
ATOM   4087 C CB  . SER B 2 133 ? -68.700 58.918 72.055  1.00 60.44  ? 133 SER B CB  1 
ATOM   4088 O OG  . SER B 2 133 ? -69.455 59.190 73.225  1.00 68.56  ? 133 SER B OG  1 
ATOM   4089 N N   . THR B 2 134 ? -65.794 59.670 71.937  1.00 51.25  ? 134 THR B N   1 
ATOM   4090 C CA  . THR B 2 134 ? -64.609 60.449 72.245  1.00 51.49  ? 134 THR B CA  1 
ATOM   4091 C C   . THR B 2 134 ? -64.975 61.691 73.049  1.00 48.78  ? 134 THR B C   1 
ATOM   4092 O O   . THR B 2 134 ? -66.089 62.216 72.958  1.00 54.56  ? 134 THR B O   1 
ATOM   4093 C CB  . THR B 2 134 ? -63.874 60.848 70.961  1.00 53.82  ? 134 THR B CB  1 
ATOM   4094 O OG1 . THR B 2 134 ? -62.889 61.843 71.260  1.00 58.35  ? 134 THR B OG1 1 
ATOM   4095 C CG2 . THR B 2 134 ? -64.846 61.411 69.937  1.00 54.54  ? 134 THR B CG2 1 
ATOM   4096 N N   . LYS B 2 135 ? -64.021 62.144 73.858  1.00 47.57  ? 135 LYS B N   1 
ATOM   4097 C CA  . LYS B 2 135 ? -64.120 63.388 74.606  1.00 50.11  ? 135 LYS B CA  1 
ATOM   4098 C C   . LYS B 2 135 ? -62.735 64.017 74.636  1.00 49.55  ? 135 LYS B C   1 
ATOM   4099 O O   . LYS B 2 135 ? -61.764 63.360 75.025  1.00 47.57  ? 135 LYS B O   1 
ATOM   4100 C CB  . LYS B 2 135 ? -64.636 63.147 76.031  1.00 54.50  ? 135 LYS B CB  1 
ATOM   4101 C CG  . LYS B 2 135 ? -65.319 64.350 76.673  1.00 59.98  ? 135 LYS B CG  1 
ATOM   4102 C CD  . LYS B 2 135 ? -64.326 65.212 77.425  1.00 59.90  ? 135 LYS B CD  1 
ATOM   4103 C CE  . LYS B 2 135 ? -64.957 65.987 78.581  1.00 63.78  ? 135 LYS B CE  1 
ATOM   4104 N NZ  . LYS B 2 135 ? -63.945 66.882 79.240  1.00 61.91  ? 135 LYS B NZ  1 
ATOM   4105 N N   . GLY B 2 136 ? -62.641 65.272 74.203  1.00 46.31  ? 136 GLY B N   1 
ATOM   4106 C CA  . GLY B 2 136 ? -61.388 65.987 74.209  1.00 45.36  ? 136 GLY B CA  1 
ATOM   4107 C C   . GLY B 2 136 ? -61.062 66.502 75.594  1.00 50.66  ? 136 GLY B C   1 
ATOM   4108 O O   . GLY B 2 136 ? -61.951 66.714 76.422  1.00 47.64  ? 136 GLY B O   1 
ATOM   4109 N N   . PRO B 2 137 ? -59.782 66.723 75.876  1.00 53.56  ? 137 PRO B N   1 
ATOM   4110 C CA  . PRO B 2 137 ? -59.377 67.129 77.222  1.00 52.20  ? 137 PRO B CA  1 
ATOM   4111 C C   . PRO B 2 137 ? -59.467 68.633 77.446  1.00 52.29  ? 137 PRO B C   1 
ATOM   4112 O O   . PRO B 2 137 ? -59.527 69.435 76.512  1.00 48.77  ? 137 PRO B O   1 
ATOM   4113 C CB  . PRO B 2 137 ? -57.916 66.667 77.290  1.00 49.45  ? 137 PRO B CB  1 
ATOM   4114 C CG  . PRO B 2 137 ? -57.429 66.799 75.876  1.00 48.44  ? 137 PRO B CG  1 
ATOM   4115 C CD  . PRO B 2 137 ? -58.631 66.632 74.960  1.00 47.57  ? 137 PRO B CD  1 
ATOM   4116 N N   . SER B 2 138 ? -59.494 68.994 78.724  1.00 51.07  ? 138 SER B N   1 
ATOM   4117 C CA  . SER B 2 138 ? -59.180 70.343 79.156  1.00 50.40  ? 138 SER B CA  1 
ATOM   4118 C C   . SER B 2 138 ? -57.700 70.415 79.511  1.00 54.02  ? 138 SER B C   1 
ATOM   4119 O O   . SER B 2 138 ? -57.104 69.439 79.982  1.00 52.43  ? 138 SER B O   1 
ATOM   4120 C CB  . SER B 2 138 ? -60.035 70.755 80.357  1.00 54.52  ? 138 SER B CB  1 
ATOM   4121 O OG  . SER B 2 138 ? -61.313 71.210 79.947  1.00 60.83  ? 138 SER B OG  1 
ATOM   4122 N N   . VAL B 2 139 ? -57.102 71.575 79.262  1.00 50.04  ? 139 VAL B N   1 
ATOM   4123 C CA  . VAL B 2 139 ? -55.673 71.778 79.465  1.00 51.32  ? 139 VAL B CA  1 
ATOM   4124 C C   . VAL B 2 139 ? -55.497 72.914 80.463  1.00 49.29  ? 139 VAL B C   1 
ATOM   4125 O O   . VAL B 2 139 ? -55.836 74.068 80.170  1.00 54.83  ? 139 VAL B O   1 
ATOM   4126 C CB  . VAL B 2 139 ? -54.942 72.073 78.149  1.00 49.73  ? 139 VAL B CB  1 
ATOM   4127 C CG1 . VAL B 2 139 ? -53.435 72.078 78.371  1.00 48.24  ? 139 VAL B CG1 1 
ATOM   4128 C CG2 . VAL B 2 139 ? -55.325 71.047 77.085  1.00 42.70  ? 139 VAL B CG2 1 
ATOM   4129 N N   . PHE B 2 140 ? -54.968 72.589 81.643  1.00 45.91  ? 140 PHE B N   1 
ATOM   4130 C CA  . PHE B 2 140 ? -54.743 73.583 82.679  1.00 49.94  ? 140 PHE B CA  1 
ATOM   4131 C C   . PHE B 2 140 ? -53.253 73.788 82.915  1.00 51.22  ? 140 PHE B C   1 
ATOM   4132 O O   . PHE B 2 140 ? -52.474 72.828 82.846  1.00 47.20  ? 140 PHE B O   1 
ATOM   4133 C CB  . PHE B 2 140 ? -55.401 73.178 84.004  1.00 49.82  ? 140 PHE B CB  1 
ATOM   4134 C CG  . PHE B 2 140 ? -56.837 72.784 83.869  1.00 53.07  ? 140 PHE B CG  1 
ATOM   4135 C CD1 . PHE B 2 140 ? -57.794 73.720 83.521  1.00 54.17  ? 140 PHE B CD1 1 
ATOM   4136 C CD2 . PHE B 2 140 ? -57.231 71.479 84.093  1.00 49.60  ? 140 PHE B CD2 1 
ATOM   4137 C CE1 . PHE B 2 140 ? -59.119 73.361 83.391  1.00 54.25  ? 140 PHE B CE1 1 
ATOM   4138 C CE2 . PHE B 2 140 ? -58.553 71.114 83.965  1.00 51.06  ? 140 PHE B CE2 1 
ATOM   4139 C CZ  . PHE B 2 140 ? -59.500 72.058 83.616  1.00 51.09  ? 140 PHE B CZ  1 
ATOM   4140 N N   . PRO B 2 141 ? -52.831 75.017 83.198  1.00 52.46  ? 141 PRO B N   1 
ATOM   4141 C CA  . PRO B 2 141 ? -51.420 75.253 83.503  1.00 48.17  ? 141 PRO B CA  1 
ATOM   4142 C C   . PRO B 2 141 ? -51.066 74.734 84.883  1.00 48.91  ? 141 PRO B C   1 
ATOM   4143 O O   . PRO B 2 141 ? -51.895 74.704 85.795  1.00 46.72  ? 141 PRO B O   1 
ATOM   4144 C CB  . PRO B 2 141 ? -51.298 76.779 83.438  1.00 50.40  ? 141 PRO B CB  1 
ATOM   4145 C CG  . PRO B 2 141 ? -52.652 77.260 83.826  1.00 48.88  ? 141 PRO B CG  1 
ATOM   4146 C CD  . PRO B 2 141 ? -53.616 76.265 83.228  1.00 53.30  ? 141 PRO B CD  1 
ATOM   4147 N N   . LEU B 2 142 ? -49.817 74.302 85.020  1.00 48.58  ? 142 LEU B N   1 
ATOM   4148 C CA  . LEU B 2 142 ? -49.210 73.991 86.311  1.00 49.05  ? 142 LEU B CA  1 
ATOM   4149 C C   . LEU B 2 142 ? -48.164 75.082 86.525  1.00 50.92  ? 142 LEU B C   1 
ATOM   4150 O O   . LEU B 2 142 ? -47.013 74.948 86.109  1.00 49.77  ? 142 LEU B O   1 
ATOM   4151 C CB  . LEU B 2 142 ? -48.604 72.581 86.335  1.00 45.70  ? 142 LEU B CB  1 
ATOM   4152 C CG  . LEU B 2 142 ? -49.575 71.413 86.113  1.00 46.72  ? 142 LEU B CG  1 
ATOM   4153 C CD1 . LEU B 2 142 ? -48.834 70.085 86.093  1.00 45.81  ? 142 LEU B CD1 1 
ATOM   4154 C CD2 . LEU B 2 142 ? -50.678 71.393 87.165  1.00 45.19  ? 142 LEU B CD2 1 
ATOM   4155 N N   . ALA B 2 143 ? -48.581 76.166 87.177  1.00 54.68  ? 143 ALA B N   1 
ATOM   4156 C CA  . ALA B 2 143 ? -47.807 77.402 87.157  1.00 61.28  ? 143 ALA B CA  1 
ATOM   4157 C C   . ALA B 2 143 ? -46.556 77.286 88.026  1.00 62.52  ? 143 ALA B C   1 
ATOM   4158 O O   . ALA B 2 143 ? -46.600 76.692 89.109  1.00 61.56  ? 143 ALA B O   1 
ATOM   4159 C CB  . ALA B 2 143 ? -48.664 78.575 87.634  1.00 62.33  ? 143 ALA B CB  1 
ATOM   4160 N N   . PRO B 2 144 ? -45.428 77.847 87.583  1.00 65.24  ? 144 PRO B N   1 
ATOM   4161 C CA  . PRO B 2 144 ? -44.221 77.833 88.420  1.00 66.49  ? 144 PRO B CA  1 
ATOM   4162 C C   . PRO B 2 144 ? -44.325 78.841 89.556  1.00 68.06  ? 144 PRO B C   1 
ATOM   4163 O O   . PRO B 2 144 ? -44.914 79.915 89.406  1.00 67.45  ? 144 PRO B O   1 
ATOM   4164 C CB  . PRO B 2 144 ? -43.102 78.201 87.437  1.00 62.09  ? 144 PRO B CB  1 
ATOM   4165 C CG  . PRO B 2 144 ? -43.783 78.995 86.370  1.00 61.62  ? 144 PRO B CG  1 
ATOM   4166 C CD  . PRO B 2 144 ? -45.187 78.452 86.260  1.00 61.80  ? 144 PRO B CD  1 
ATOM   4167 N N   . SER B 2 145 ? -43.750 78.479 90.700  1.00 73.63  ? 145 SER B N   1 
ATOM   4168 C CA  . SER B 2 145 ? -43.818 79.295 91.909  1.00 74.28  ? 145 SER B CA  1 
ATOM   4169 C C   . SER B 2 145 ? -42.801 78.757 92.910  1.00 80.23  ? 145 SER B C   1 
ATOM   4170 O O   . SER B 2 145 ? -42.023 77.846 92.608  1.00 80.86  ? 145 SER B O   1 
ATOM   4171 C CB  . SER B 2 145 ? -45.227 79.299 92.504  1.00 76.18  ? 145 SER B CB  1 
ATOM   4172 O OG  . SER B 2 145 ? -45.422 78.180 93.354  1.00 79.98  ? 145 SER B OG  1 
ATOM   4173 N N   . SER B 2 146 ? -42.815 79.338 94.114  1.00 86.02  ? 146 SER B N   1 
ATOM   4174 C CA  . SER B 2 146 ? -41.929 78.874 95.178  1.00 84.36  ? 146 SER B CA  1 
ATOM   4175 C C   . SER B 2 146 ? -42.267 77.449 95.593  1.00 79.39  ? 146 SER B C   1 
ATOM   4176 O O   . SER B 2 146 ? -41.369 76.649 95.885  1.00 81.20  ? 146 SER B O   1 
ATOM   4177 C CB  . SER B 2 146 ? -42.013 79.813 96.382  1.00 85.40  ? 146 SER B CB  1 
ATOM   4178 O OG  . SER B 2 146 ? -41.606 79.153 97.571  1.00 87.42  ? 146 SER B OG  1 
ATOM   4179 N N   . LYS B 2 147 ? -43.560 77.114 95.633  1.00 78.56  ? 147 LYS B N   1 
ATOM   4180 C CA  . LYS B 2 147 ? -43.966 75.733 95.872  1.00 82.80  ? 147 LYS B CA  1 
ATOM   4181 C C   . LYS B 2 147 ? -43.467 74.798 94.778  1.00 74.07  ? 147 LYS B C   1 
ATOM   4182 O O   . LYS B 2 147 ? -43.408 73.581 94.991  1.00 62.97  ? 147 LYS B O   1 
ATOM   4183 C CB  . LYS B 2 147 ? -45.490 75.652 95.989  1.00 72.10  ? 147 LYS B CB  1 
ATOM   4184 N N   . SER B 2 148 ? -43.096 75.345 93.620  1.00 80.03  ? 148 SER B N   1 
ATOM   4185 C CA  . SER B 2 148 ? -42.556 74.587 92.499  1.00 71.78  ? 148 SER B CA  1 
ATOM   4186 C C   . SER B 2 148 ? -41.065 74.851 92.309  1.00 75.93  ? 148 SER B C   1 
ATOM   4187 O O   . SER B 2 148 ? -40.545 74.731 91.196  1.00 73.83  ? 148 SER B O   1 
ATOM   4188 C CB  . SER B 2 148 ? -43.319 74.930 91.220  1.00 66.57  ? 148 SER B CB  1 
ATOM   4189 O OG  . SER B 2 148 ? -44.707 74.697 91.375  1.00 73.39  ? 148 SER B OG  1 
ATOM   4190 N N   . THR B 2 149 ? -40.369 75.230 93.380  1.00 75.57  ? 149 THR B N   1 
ATOM   4191 C CA  . THR B 2 149 ? -38.944 75.528 93.320  1.00 78.60  ? 149 THR B CA  1 
ATOM   4192 C C   . THR B 2 149 ? -38.212 74.723 94.383  1.00 79.71  ? 149 THR B C   1 
ATOM   4193 O O   . THR B 2 149 ? -38.592 74.747 95.558  1.00 80.06  ? 149 THR B O   1 
ATOM   4194 C CB  . THR B 2 149 ? -38.674 77.027 93.509  1.00 78.98  ? 149 THR B CB  1 
ATOM   4195 O OG1 . THR B 2 149 ? -39.289 77.762 92.443  1.00 76.68  ? 149 THR B OG1 1 
ATOM   4196 C CG2 . THR B 2 149 ? -37.174 77.303 93.514  1.00 73.37  ? 149 THR B CG2 1 
ATOM   4197 N N   . SER B 2 150 ? -37.168 74.012 93.964  1.00 72.84  ? 150 SER B N   1 
ATOM   4198 C CA  . SER B 2 150 ? -36.378 73.183 94.869  1.00 69.59  ? 150 SER B CA  1 
ATOM   4199 C C   . SER B 2 150 ? -34.935 73.235 94.392  1.00 74.95  ? 150 SER B C   1 
ATOM   4200 O O   . SER B 2 150 ? -34.621 72.731 93.309  1.00 65.94  ? 150 SER B O   1 
ATOM   4201 C CB  . SER B 2 150 ? -36.901 71.748 94.900  1.00 71.18  ? 150 SER B CB  1 
ATOM   4202 O OG  . SER B 2 150 ? -35.871 70.831 95.230  1.00 74.16  ? 150 SER B OG  1 
ATOM   4203 N N   . GLY B 2 151 ? -34.061 73.838 95.198  1.00 80.65  ? 151 GLY B N   1 
ATOM   4204 C CA  . GLY B 2 151 ? -32.704 74.065 94.747  1.00 73.15  ? 151 GLY B CA  1 
ATOM   4205 C C   . GLY B 2 151 ? -32.675 75.078 93.614  1.00 75.45  ? 151 GLY B C   1 
ATOM   4206 O O   . GLY B 2 151 ? -33.506 75.989 93.526  1.00 69.47  ? 151 GLY B O   1 
ATOM   4207 N N   . GLY B 2 152 ? -31.701 74.910 92.726  1.00 75.59  ? 152 GLY B N   1 
ATOM   4208 C CA  . GLY B 2 152 ? -31.613 75.755 91.558  1.00 70.20  ? 152 GLY B CA  1 
ATOM   4209 C C   . GLY B 2 152 ? -32.555 75.403 90.432  1.00 68.08  ? 152 GLY B C   1 
ATOM   4210 O O   . GLY B 2 152 ? -32.412 75.949 89.335  1.00 73.40  ? 152 GLY B O   1 
ATOM   4211 N N   . THR B 2 153 ? -33.517 74.510 90.655  1.00 64.67  ? 153 THR B N   1 
ATOM   4212 C CA  . THR B 2 153 ? -34.449 74.098 89.616  1.00 65.76  ? 153 THR B CA  1 
ATOM   4213 C C   . THR B 2 153 ? -35.864 74.535 89.968  1.00 66.55  ? 153 THR B C   1 
ATOM   4214 O O   . THR B 2 153 ? -36.257 74.537 91.141  1.00 61.08  ? 153 THR B O   1 
ATOM   4215 C CB  . THR B 2 153 ? -34.424 72.579 89.397  1.00 60.32  ? 153 THR B CB  1 
ATOM   4216 O OG1 . THR B 2 153 ? -34.864 71.913 90.583  1.00 66.98  ? 153 THR B OG1 1 
ATOM   4217 C CG2 . THR B 2 153 ? -33.021 72.109 89.050  1.00 56.65  ? 153 THR B CG2 1 
ATOM   4218 N N   . ALA B 2 154 ? -36.616 74.916 88.940  1.00 62.69  ? 154 ALA B N   1 
ATOM   4219 C CA  . ALA B 2 154 ? -38.032 75.221 89.048  1.00 59.08  ? 154 ALA B CA  1 
ATOM   4220 C C   . ALA B 2 154 ? -38.808 74.267 88.152  1.00 57.21  ? 154 ALA B C   1 
ATOM   4221 O O   . ALA B 2 154 ? -38.274 73.742 87.171  1.00 55.60  ? 154 ALA B O   1 
ATOM   4222 C CB  . ALA B 2 154 ? -38.328 76.671 88.651  1.00 52.95  ? 154 ALA B CB  1 
ATOM   4223 N N   . ALA B 2 155 ? -40.074 74.046 88.490  1.00 55.89  ? 155 ALA B N   1 
ATOM   4224 C CA  . ALA B 2 155 ? -40.920 73.143 87.730  1.00 56.45  ? 155 ALA B CA  1 
ATOM   4225 C C   . ALA B 2 155 ? -42.196 73.851 87.307  1.00 55.38  ? 155 ALA B C   1 
ATOM   4226 O O   . ALA B 2 155 ? -42.737 74.681 88.043  1.00 59.34  ? 155 ALA B O   1 
ATOM   4227 C CB  . ALA B 2 155 ? -41.267 71.881 88.534  1.00 54.42  ? 155 ALA B CB  1 
ATOM   4228 N N   . LEU B 2 156 ? -42.661 73.516 86.107  1.00 51.17  ? 156 LEU B N   1 
ATOM   4229 C CA  . LEU B 2 156 ? -43.948 73.958 85.590  1.00 52.00  ? 156 LEU B CA  1 
ATOM   4230 C C   . LEU B 2 156 ? -44.449 72.860 84.664  1.00 43.18  ? 156 LEU B C   1 
ATOM   4231 O O   . LEU B 2 156 ? -43.706 71.942 84.309  1.00 48.52  ? 156 LEU B O   1 
ATOM   4232 C CB  . LEU B 2 156 ? -43.835 75.304 84.864  1.00 53.69  ? 156 LEU B CB  1 
ATOM   4233 C CG  . LEU B 2 156 ? -42.894 75.340 83.655  1.00 55.99  ? 156 LEU B CG  1 
ATOM   4234 C CD1 . LEU B 2 156 ? -43.680 75.398 82.354  1.00 56.51  ? 156 LEU B CD1 1 
ATOM   4235 C CD2 . LEU B 2 156 ? -41.935 76.511 83.760  1.00 56.54  ? 156 LEU B CD2 1 
ATOM   4236 N N   . GLY B 2 157 ? -45.712 72.946 84.274  1.00 47.32  ? 157 GLY B N   1 
ATOM   4237 C CA  . GLY B 2 157 ? -46.238 71.898 83.428  1.00 45.42  ? 157 GLY B CA  1 
ATOM   4238 C C   . GLY B 2 157 ? -47.654 72.172 82.983  1.00 45.58  ? 157 GLY B C   1 
ATOM   4239 O O   . GLY B 2 157 ? -48.165 73.289 83.094  1.00 45.09  ? 157 GLY B O   1 
ATOM   4240 N N   . CYS B 2 158 ? -48.276 71.116 82.460  1.00 45.57  ? 158 CYS B N   1 
ATOM   4241 C CA  . CYS B 2 158 ? -49.623 71.177 81.911  1.00 51.46  ? 158 CYS B CA  1 
ATOM   4242 C C   . CYS B 2 158 ? -50.392 69.951 82.370  1.00 51.12  ? 158 CYS B C   1 
ATOM   4243 O O   . CYS B 2 158 ? -49.873 68.831 82.306  1.00 44.08  ? 158 CYS B O   1 
ATOM   4244 C CB  . CYS B 2 158 ? -49.596 71.236 80.377  1.00 47.32  ? 158 CYS B CB  1 
ATOM   4245 S SG  . CYS B 2 158 ? -49.683 72.907 79.688  1.00 60.24  ? 158 CYS B SG  1 
ATOM   4246 N N   . LEU B 2 159 ? -51.620 70.165 82.831  1.00 47.02  ? 159 LEU B N   1 
ATOM   4247 C CA  . LEU B 2 159 ? -52.518 69.083 83.210  1.00 45.36  ? 159 LEU B CA  1 
ATOM   4248 C C   . LEU B 2 159 ? -53.510 68.862 82.076  1.00 46.26  ? 159 LEU B C   1 
ATOM   4249 O O   . LEU B 2 159 ? -54.268 69.774 81.725  1.00 42.89  ? 159 LEU B O   1 
ATOM   4250 C CB  . LEU B 2 159 ? -53.249 69.403 84.514  1.00 47.41  ? 159 LEU B CB  1 
ATOM   4251 C CG  . LEU B 2 159 ? -54.070 68.265 85.129  1.00 48.81  ? 159 LEU B CG  1 
ATOM   4252 C CD1 . LEU B 2 159 ? -53.160 67.205 85.723  1.00 41.66  ? 159 LEU B CD1 1 
ATOM   4253 C CD2 . LEU B 2 159 ? -55.034 68.803 86.179  1.00 49.30  ? 159 LEU B CD2 1 
ATOM   4254 N N   . VAL B 2 160 ? -53.494 67.662 81.501  1.00 40.41  ? 160 VAL B N   1 
ATOM   4255 C CA  . VAL B 2 160 ? -54.366 67.289 80.393  1.00 43.29  ? 160 VAL B CA  1 
ATOM   4256 C C   . VAL B 2 160 ? -55.394 66.316 80.957  1.00 46.44  ? 160 VAL B C   1 
ATOM   4257 O O   . VAL B 2 160 ? -55.097 65.136 81.175  1.00 47.51  ? 160 VAL B O   1 
ATOM   4258 C CB  . VAL B 2 160 ? -53.577 66.678 79.231  1.00 44.47  ? 160 VAL B CB  1 
ATOM   4259 C CG1 . VAL B 2 160 ? -54.490 66.406 78.048  1.00 41.11  ? 160 VAL B CG1 1 
ATOM   4260 C CG2 . VAL B 2 160 ? -52.439 67.603 78.831  1.00 38.36  ? 160 VAL B CG2 1 
ATOM   4261 N N   . LYS B 2 161 ? -56.612 66.803 81.188  1.00 47.70  ? 161 LYS B N   1 
ATOM   4262 C CA  . LYS B 2 161 ? -57.568 66.132 82.059  1.00 50.48  ? 161 LYS B CA  1 
ATOM   4263 C C   . LYS B 2 161 ? -58.853 65.788 81.314  1.00 49.04  ? 161 LYS B C   1 
ATOM   4264 O O   . LYS B 2 161 ? -59.303 66.549 80.451  1.00 50.19  ? 161 LYS B O   1 
ATOM   4265 C CB  . LYS B 2 161 ? -57.879 67.015 83.281  1.00 49.71  ? 161 LYS B CB  1 
ATOM   4266 C CG  . LYS B 2 161 ? -58.988 66.488 84.169  1.00 54.36  ? 161 LYS B CG  1 
ATOM   4267 C CD  . LYS B 2 161 ? -58.711 66.664 85.653  1.00 57.81  ? 161 LYS B CD  1 
ATOM   4268 C CE  . LYS B 2 161 ? -60.015 66.607 86.455  1.00 55.22  ? 161 LYS B CE  1 
ATOM   4269 N NZ  . LYS B 2 161 ? -60.529 65.211 86.618  1.00 50.76  ? 161 LYS B NZ  1 
ATOM   4270 N N   . ASP B 2 162 ? -59.419 64.619 81.640  1.00 50.88  ? 162 ASP B N   1 
ATOM   4271 C CA  . ASP B 2 162 ? -60.771 64.209 81.243  1.00 49.32  ? 162 ASP B CA  1 
ATOM   4272 C C   . ASP B 2 162 ? -60.898 64.054 79.722  1.00 50.73  ? 162 ASP B C   1 
ATOM   4273 O O   . ASP B 2 162 ? -61.651 64.764 79.052  1.00 50.14  ? 162 ASP B O   1 
ATOM   4274 C CB  . ASP B 2 162 ? -61.816 65.196 81.781  1.00 49.73  ? 162 ASP B CB  1 
ATOM   4275 C CG  . ASP B 2 162 ? -61.917 65.178 83.296  1.00 55.06  ? 162 ASP B CG  1 
ATOM   4276 O OD1 . ASP B 2 162 ? -61.235 64.348 83.934  1.00 56.41  ? 162 ASP B OD1 1 
ATOM   4277 O OD2 . ASP B 2 162 ? -62.653 66.019 83.853  1.00 61.45  ? 162 ASP B OD2 1 
ATOM   4278 N N   . TYR B 2 163 ? -60.173 63.065 79.199  1.00 49.99  ? 163 TYR B N   1 
ATOM   4279 C CA  . TYR B 2 163 ? -60.223 62.757 77.777  1.00 46.61  ? 163 TYR B CA  1 
ATOM   4280 C C   . TYR B 2 163 ? -60.331 61.253 77.569  1.00 47.18  ? 163 TYR B C   1 
ATOM   4281 O O   . TYR B 2 163 ? -59.916 60.456 78.417  1.00 43.68  ? 163 TYR B O   1 
ATOM   4282 C CB  . TYR B 2 163 ? -58.998 63.313 77.027  1.00 47.75  ? 163 TYR B CB  1 
ATOM   4283 C CG  . TYR B 2 163 ? -57.673 62.666 77.377  1.00 47.39  ? 163 TYR B CG  1 
ATOM   4284 C CD1 . TYR B 2 163 ? -56.897 63.148 78.427  1.00 45.56  ? 163 TYR B CD1 1 
ATOM   4285 C CD2 . TYR B 2 163 ? -57.185 61.592 76.638  1.00 45.14  ? 163 TYR B CD2 1 
ATOM   4286 C CE1 . TYR B 2 163 ? -55.681 62.565 78.742  1.00 45.84  ? 163 TYR B CE1 1 
ATOM   4287 C CE2 . TYR B 2 163 ? -55.974 61.002 76.946  1.00 42.56  ? 163 TYR B CE2 1 
ATOM   4288 C CZ  . TYR B 2 163 ? -55.225 61.491 77.998  1.00 46.74  ? 163 TYR B CZ  1 
ATOM   4289 O OH  . TYR B 2 163 ? -54.014 60.906 78.304  1.00 41.79  ? 163 TYR B OH  1 
ATOM   4290 N N   . PHE B 2 164 ? -60.894 60.874 76.415  1.00 46.82  ? 164 PHE B N   1 
ATOM   4291 C CA  . PHE B 2 164 ? -61.048 59.478 76.034  1.00 40.47  ? 164 PHE B CA  1 
ATOM   4292 C C   . PHE B 2 164 ? -61.123 59.401 74.522  1.00 45.94  ? 164 PHE B C   1 
ATOM   4293 O O   . PHE B 2 164 ? -61.751 60.272 73.904  1.00 49.23  ? 164 PHE B O   1 
ATOM   4294 C CB  . PHE B 2 164 ? -62.306 58.855 76.654  1.00 42.37  ? 164 PHE B CB  1 
ATOM   4295 C CG  . PHE B 2 164 ? -62.452 57.381 76.379  1.00 42.46  ? 164 PHE B CG  1 
ATOM   4296 C CD1 . PHE B 2 164 ? -61.819 56.445 77.187  1.00 40.39  ? 164 PHE B CD1 1 
ATOM   4297 C CD2 . PHE B 2 164 ? -63.212 56.932 75.308  1.00 45.15  ? 164 PHE B CD2 1 
ATOM   4298 C CE1 . PHE B 2 164 ? -61.945 55.085 76.937  1.00 37.31  ? 164 PHE B CE1 1 
ATOM   4299 C CE2 . PHE B 2 164 ? -63.344 55.573 75.051  1.00 47.36  ? 164 PHE B CE2 1 
ATOM   4300 C CZ  . PHE B 2 164 ? -62.707 54.648 75.866  1.00 42.00  ? 164 PHE B CZ  1 
ATOM   4301 N N   . PRO B 2 165 ? -60.481 58.414 73.889  1.00 43.66  ? 165 PRO B N   1 
ATOM   4302 C CA  . PRO B 2 165 ? -59.576 57.422 74.472  1.00 40.68  ? 165 PRO B CA  1 
ATOM   4303 C C   . PRO B 2 165 ? -58.147 57.943 74.476  1.00 45.41  ? 165 PRO B C   1 
ATOM   4304 O O   . PRO B 2 165 ? -57.905 59.096 74.126  1.00 42.73  ? 165 PRO B O   1 
ATOM   4305 C CB  . PRO B 2 165 ? -59.748 56.226 73.536  1.00 43.24  ? 165 PRO B CB  1 
ATOM   4306 C CG  . PRO B 2 165 ? -60.014 56.861 72.171  1.00 43.41  ? 165 PRO B CG  1 
ATOM   4307 C CD  . PRO B 2 165 ? -60.601 58.241 72.430  1.00 44.06  ? 165 PRO B CD  1 
ATOM   4308 N N   . GLU B 2 166 ? -57.178 57.124 74.874  1.00 45.27  ? 166 GLU B N   1 
ATOM   4309 C CA  . GLU B 2 166 ? -55.787 57.453 74.636  1.00 41.20  ? 166 GLU B CA  1 
ATOM   4310 C C   . GLU B 2 166 ? -55.526 57.431 73.131  1.00 39.41  ? 166 GLU B C   1 
ATOM   4311 O O   . GLU B 2 166 ? -56.295 56.836 72.374  1.00 39.71  ? 166 GLU B O   1 
ATOM   4312 C CB  . GLU B 2 166 ? -54.882 56.462 75.360  1.00 40.41  ? 166 GLU B CB  1 
ATOM   4313 C CG  . GLU B 2 166 ? -54.780 56.685 76.865  1.00 42.60  ? 166 GLU B CG  1 
ATOM   4314 C CD  . GLU B 2 166 ? -53.452 57.302 77.282  1.00 52.56  ? 166 GLU B CD  1 
ATOM   4315 O OE1 . GLU B 2 166 ? -52.667 56.612 77.967  1.00 44.45  ? 166 GLU B OE1 1 
ATOM   4316 O OE2 . GLU B 2 166 ? -53.212 58.493 76.944  1.00 50.99  ? 166 GLU B OE2 1 
ATOM   4317 N N   . PRO B 2 167 ? -54.452 58.090 72.659  1.00 43.56  ? 167 PRO B N   1 
ATOM   4318 C CA  . PRO B 2 167 ? -53.429 58.849 73.376  1.00 39.43  ? 167 PRO B CA  1 
ATOM   4319 C C   . PRO B 2 167 ? -53.627 60.353 73.281  1.00 44.51  ? 167 PRO B C   1 
ATOM   4320 O O   . PRO B 2 167 ? -54.568 60.849 72.662  1.00 43.95  ? 167 PRO B O   1 
ATOM   4321 C CB  . PRO B 2 167 ? -52.149 58.428 72.648  1.00 35.35  ? 167 PRO B CB  1 
ATOM   4322 C CG  . PRO B 2 167 ? -52.609 58.170 71.196  1.00 34.02  ? 167 PRO B CG  1 
ATOM   4323 C CD  . PRO B 2 167 ? -54.126 58.039 71.224  1.00 34.44  ? 167 PRO B CD  1 
ATOM   4324 N N   . VAL B 2 168 ? -52.726 61.101 73.903  1.00 44.15  ? 168 VAL B N   1 
ATOM   4325 C CA  . VAL B 2 168 ? -52.593 62.530 73.670  1.00 47.62  ? 168 VAL B CA  1 
ATOM   4326 C C   . VAL B 2 168 ? -51.140 62.793 73.317  1.00 45.90  ? 168 VAL B C   1 
ATOM   4327 O O   . VAL B 2 168 ? -50.230 62.123 73.815  1.00 42.95  ? 168 VAL B O   1 
ATOM   4328 C CB  . VAL B 2 168 ? -53.011 63.387 74.886  1.00 46.15  ? 168 VAL B CB  1 
ATOM   4329 C CG1 . VAL B 2 168 ? -54.515 63.552 74.937  1.00 50.38  ? 168 VAL B CG1 1 
ATOM   4330 C CG2 . VAL B 2 168 ? -52.481 62.784 76.175  1.00 46.88  ? 168 VAL B CG2 1 
ATOM   4331 N N   . THR B 2 169 ? -50.930 63.761 72.436  1.00 44.72  ? 169 THR B N   1 
ATOM   4332 C CA  . THR B 2 169 ? -49.602 64.265 72.133  1.00 47.35  ? 169 THR B CA  1 
ATOM   4333 C C   . THR B 2 169 ? -49.367 65.524 72.952  1.00 45.99  ? 169 THR B C   1 
ATOM   4334 O O   . THR B 2 169 ? -50.193 66.443 72.936  1.00 43.19  ? 169 THR B O   1 
ATOM   4335 C CB  . THR B 2 169 ? -49.447 64.575 70.642  1.00 50.30  ? 169 THR B CB  1 
ATOM   4336 O OG1 . THR B 2 169 ? -49.224 63.357 69.922  1.00 57.22  ? 169 THR B OG1 1 
ATOM   4337 C CG2 . THR B 2 169 ? -48.257 65.514 70.414  1.00 52.96  ? 169 THR B CG2 1 
ATOM   4338 N N   . VAL B 2 170 ? -48.257 65.555 73.682  1.00 42.27  ? 170 VAL B N   1 
ATOM   4339 C CA  . VAL B 2 170 ? -47.817 66.752 74.384  1.00 41.92  ? 170 VAL B CA  1 
ATOM   4340 C C   . VAL B 2 170 ? -46.412 67.082 73.912  1.00 42.57  ? 170 VAL B C   1 
ATOM   4341 O O   . VAL B 2 170 ? -45.486 66.277 74.079  1.00 49.57  ? 170 VAL B O   1 
ATOM   4342 C CB  . VAL B 2 170 ? -47.852 66.586 75.912  1.00 40.28  ? 170 VAL B CB  1 
ATOM   4343 C CG1 . VAL B 2 170 ? -47.540 67.919 76.573  1.00 43.84  ? 170 VAL B CG1 1 
ATOM   4344 C CG2 . VAL B 2 170 ? -49.206 66.071 76.368  1.00 40.22  ? 170 VAL B CG2 1 
ATOM   4345 N N   . SER B 2 171 ? -46.256 68.252 73.312  1.00 45.08  ? 171 SER B N   1 
ATOM   4346 C CA  . SER B 2 171 ? -44.949 68.830 73.059  1.00 44.45  ? 171 SER B CA  1 
ATOM   4347 C C   . SER B 2 171 ? -44.873 70.172 73.772  1.00 43.19  ? 171 SER B C   1 
ATOM   4348 O O   . SER B 2 171 ? -45.868 70.684 74.294  1.00 43.66  ? 171 SER B O   1 
ATOM   4349 C CB  . SER B 2 171 ? -44.687 68.983 71.554  1.00 38.13  ? 171 SER B CB  1 
ATOM   4350 O OG  . SER B 2 171 ? -45.432 70.050 71.009  1.00 45.64  ? 171 SER B OG  1 
ATOM   4351 N N   . TRP B 2 172 ? -43.672 70.737 73.813  1.00 39.80  ? 172 TRP B N   1 
ATOM   4352 C CA  . TRP B 2 172 ? -43.461 72.048 74.405  1.00 42.28  ? 172 TRP B CA  1 
ATOM   4353 C C   . TRP B 2 172 ? -42.767 72.938 73.389  1.00 45.50  ? 172 TRP B C   1 
ATOM   4354 O O   . TRP B 2 172 ? -41.777 72.528 72.771  1.00 38.97  ? 172 TRP B O   1 
ATOM   4355 C CB  . TRP B 2 172 ? -42.645 71.949 75.695  1.00 41.89  ? 172 TRP B CB  1 
ATOM   4356 C CG  . TRP B 2 172 ? -43.419 71.338 76.826  1.00 43.27  ? 172 TRP B CG  1 
ATOM   4357 C CD1 . TRP B 2 172 ? -43.555 70.009 77.100  1.00 38.68  ? 172 TRP B CD1 1 
ATOM   4358 C CD2 . TRP B 2 172 ? -44.168 72.036 77.832  1.00 47.90  ? 172 TRP B CD2 1 
ATOM   4359 N NE1 . TRP B 2 172 ? -44.336 69.834 78.218  1.00 50.13  ? 172 TRP B NE1 1 
ATOM   4360 C CE2 . TRP B 2 172 ? -44.725 71.062 78.688  1.00 47.15  ? 172 TRP B CE2 1 
ATOM   4361 C CE3 . TRP B 2 172 ? -44.417 73.389 78.096  1.00 43.08  ? 172 TRP B CE3 1 
ATOM   4362 C CZ2 . TRP B 2 172 ? -45.517 71.397 79.790  1.00 43.77  ? 172 TRP B CZ2 1 
ATOM   4363 C CZ3 . TRP B 2 172 ? -45.203 73.720 79.194  1.00 47.40  ? 172 TRP B CZ3 1 
ATOM   4364 C CH2 . TRP B 2 172 ? -45.746 72.727 80.024  1.00 44.44  ? 172 TRP B CH2 1 
ATOM   4365 N N   . ASN B 2 173 ? -43.301 74.146 73.211  1.00 42.36  ? 173 ASN B N   1 
ATOM   4366 C CA  . ASN B 2 173 ? -42.801 75.093 72.221  1.00 41.92  ? 173 ASN B CA  1 
ATOM   4367 C C   . ASN B 2 173 ? -42.661 74.420 70.857  1.00 43.94  ? 173 ASN B C   1 
ATOM   4368 O O   . ASN B 2 173 ? -41.644 74.546 70.169  1.00 43.95  ? 173 ASN B O   1 
ATOM   4369 C CB  . ASN B 2 173 ? -41.484 75.719 72.683  1.00 45.26  ? 173 ASN B CB  1 
ATOM   4370 C CG  . ASN B 2 173 ? -41.661 76.594 73.911  1.00 42.28  ? 173 ASN B CG  1 
ATOM   4371 O OD1 . ASN B 2 173 ? -42.786 76.881 74.318  1.00 43.37  ? 173 ASN B OD1 1 
ATOM   4372 N ND2 . ASN B 2 173 ? -40.553 77.018 74.511  1.00 43.39  ? 173 ASN B ND2 1 
ATOM   4373 N N   . SER B 2 174 ? -43.705 73.669 70.488  1.00 46.03  ? 174 SER B N   1 
ATOM   4374 C CA  . SER B 2 174 ? -43.828 73.032 69.174  1.00 48.04  ? 174 SER B CA  1 
ATOM   4375 C C   . SER B 2 174 ? -42.672 72.078 68.880  1.00 45.72  ? 174 SER B C   1 
ATOM   4376 O O   . SER B 2 174 ? -42.324 71.854 67.719  1.00 50.42  ? 174 SER B O   1 
ATOM   4377 C CB  . SER B 2 174 ? -43.949 74.079 68.063  1.00 42.47  ? 174 SER B CB  1 
ATOM   4378 O OG  . SER B 2 174 ? -44.770 75.157 68.481  1.00 47.23  ? 174 SER B OG  1 
ATOM   4379 N N   . GLY B 2 175 ? -42.078 71.499 69.923  1.00 41.16  ? 175 GLY B N   1 
ATOM   4380 C CA  . GLY B 2 175 ? -40.965 70.587 69.777  1.00 38.87  ? 175 GLY B CA  1 
ATOM   4381 C C   . GLY B 2 175 ? -39.604 71.209 69.998  1.00 47.70  ? 175 GLY B C   1 
ATOM   4382 O O   . GLY B 2 175 ? -38.604 70.478 70.028  1.00 48.01  ? 175 GLY B O   1 
ATOM   4383 N N   . ALA B 2 176 ? -39.534 72.534 70.154  1.00 45.60  ? 176 ALA B N   1 
ATOM   4384 C CA  . ALA B 2 176 ? -38.249 73.188 70.365  1.00 41.29  ? 176 ALA B CA  1 
ATOM   4385 C C   . ALA B 2 176 ? -37.691 72.908 71.755  1.00 44.67  ? 176 ALA B C   1 
ATOM   4386 O O   . ALA B 2 176 ? -36.469 72.909 71.941  1.00 44.65  ? 176 ALA B O   1 
ATOM   4387 C CB  . ALA B 2 176 ? -38.385 74.695 70.141  1.00 39.98  ? 176 ALA B CB  1 
ATOM   4388 N N   . LEU B 2 177 ? -38.557 72.673 72.738  1.00 44.62  ? 177 LEU B N   1 
ATOM   4389 C CA  . LEU B 2 177 ? -38.136 72.398 74.108  1.00 48.36  ? 177 LEU B CA  1 
ATOM   4390 C C   . LEU B 2 177 ? -38.297 70.905 74.379  1.00 50.87  ? 177 LEU B C   1 
ATOM   4391 O O   . LEU B 2 177 ? -39.420 70.392 74.432  1.00 48.64  ? 177 LEU B O   1 
ATOM   4392 C CB  . LEU B 2 177 ? -38.944 73.228 75.104  1.00 50.91  ? 177 LEU B CB  1 
ATOM   4393 C CG  . LEU B 2 177 ? -38.653 72.960 76.583  1.00 47.22  ? 177 LEU B CG  1 
ATOM   4394 C CD1 . LEU B 2 177 ? -37.236 73.383 76.935  1.00 47.33  ? 177 LEU B CD1 1 
ATOM   4395 C CD2 . LEU B 2 177 ? -39.664 73.670 77.471  1.00 49.75  ? 177 LEU B CD2 1 
ATOM   4396 N N   . THR B 2 178 ? -37.172 70.213 74.538  1.00 51.67  ? 178 THR B N   1 
ATOM   4397 C CA  . THR B 2 178 ? -37.162 68.800 74.886  1.00 53.91  ? 178 THR B CA  1 
ATOM   4398 C C   . THR B 2 178 ? -36.400 68.494 76.163  1.00 51.40  ? 178 THR B C   1 
ATOM   4399 O O   . THR B 2 178 ? -36.734 67.521 76.843  1.00 54.22  ? 178 THR B O   1 
ATOM   4400 C CB  . THR B 2 178 ? -36.552 67.963 73.749  1.00 55.41  ? 178 THR B CB  1 
ATOM   4401 O OG1 . THR B 2 178 ? -35.363 68.602 73.266  1.00 55.99  ? 178 THR B OG1 1 
ATOM   4402 C CG2 . THR B 2 178 ? -37.546 67.807 72.612  1.00 52.48  ? 178 THR B CG2 1 
ATOM   4403 N N   . SER B 2 179 ? -35.395 69.295 76.508  1.00 53.28  ? 179 SER B N   1 
ATOM   4404 C CA  . SER B 2 179 ? -34.575 69.029 77.681  1.00 52.95  ? 179 SER B CA  1 
ATOM   4405 C C   . SER B 2 179 ? -35.339 69.388 78.950  1.00 50.86  ? 179 SER B C   1 
ATOM   4406 O O   . SER B 2 179 ? -35.916 70.475 79.054  1.00 52.85  ? 179 SER B O   1 
ATOM   4407 C CB  . SER B 2 179 ? -33.267 69.817 77.602  1.00 48.70  ? 179 SER B CB  1 
ATOM   4408 O OG  . SER B 2 179 ? -32.586 69.797 78.843  1.00 62.69  ? 179 SER B OG  1 
ATOM   4409 N N   . GLY B 2 180 ? -35.344 68.467 79.914  1.00 48.25  ? 180 GLY B N   1 
ATOM   4410 C CA  . GLY B 2 180 ? -36.040 68.667 81.169  1.00 42.75  ? 180 GLY B CA  1 
ATOM   4411 C C   . GLY B 2 180 ? -37.518 68.343 81.149  1.00 48.06  ? 180 GLY B C   1 
ATOM   4412 O O   . GLY B 2 180 ? -38.197 68.577 82.157  1.00 51.94  ? 180 GLY B O   1 
ATOM   4413 N N   . VAL B 2 181 ? -38.037 67.811 80.046  1.00 45.72  ? 181 VAL B N   1 
ATOM   4414 C CA  . VAL B 2 181 ? -39.461 67.537 79.906  1.00 46.56  ? 181 VAL B CA  1 
ATOM   4415 C C   . VAL B 2 181 ? -39.754 66.127 80.400  1.00 47.93  ? 181 VAL B C   1 
ATOM   4416 O O   . VAL B 2 181 ? -39.056 65.171 80.041  1.00 43.48  ? 181 VAL B O   1 
ATOM   4417 C CB  . VAL B 2 181 ? -39.917 67.709 78.447  1.00 48.94  ? 181 VAL B CB  1 
ATOM   4418 C CG1 . VAL B 2 181 ? -41.381 67.308 78.300  1.00 40.58  ? 181 VAL B CG1 1 
ATOM   4419 C CG2 . VAL B 2 181 ? -39.702 69.146 77.982  1.00 47.43  ? 181 VAL B CG2 1 
ATOM   4420 N N   . HIS B 2 182 ? -40.790 65.998 81.225  1.00 45.37  ? 182 HIS B N   1 
ATOM   4421 C CA  . HIS B 2 182 ? -41.312 64.703 81.640  1.00 45.71  ? 182 HIS B CA  1 
ATOM   4422 C C   . HIS B 2 182 ? -42.798 64.678 81.328  1.00 45.19  ? 182 HIS B C   1 
ATOM   4423 O O   . HIS B 2 182 ? -43.563 65.475 81.883  1.00 45.04  ? 182 HIS B O   1 
ATOM   4424 C CB  . HIS B 2 182 ? -41.079 64.450 83.135  1.00 47.10  ? 182 HIS B CB  1 
ATOM   4425 C CG  . HIS B 2 182 ? -39.636 64.363 83.520  1.00 50.29  ? 182 HIS B CG  1 
ATOM   4426 N ND1 . HIS B 2 182 ? -38.817 63.330 83.116  1.00 54.90  ? 182 HIS B ND1 1 
ATOM   4427 C CD2 . HIS B 2 182 ? -38.866 65.180 84.276  1.00 56.20  ? 182 HIS B CD2 1 
ATOM   4428 C CE1 . HIS B 2 182 ? -37.603 63.518 83.603  1.00 53.63  ? 182 HIS B CE1 1 
ATOM   4429 N NE2 . HIS B 2 182 ? -37.606 64.632 84.313  1.00 56.17  ? 182 HIS B NE2 1 
ATOM   4430 N N   . THR B 2 183 ? -43.206 63.781 80.437  1.00 43.07  ? 183 THR B N   1 
ATOM   4431 C CA  . THR B 2 183 ? -44.618 63.547 80.163  1.00 45.08  ? 183 THR B CA  1 
ATOM   4432 C C   . THR B 2 183 ? -44.991 62.200 80.761  1.00 45.33  ? 183 THR B C   1 
ATOM   4433 O O   . THR B 2 183 ? -44.429 61.168 80.378  1.00 46.78  ? 183 THR B O   1 
ATOM   4434 C CB  . THR B 2 183 ? -44.919 63.584 78.668  1.00 46.65  ? 183 THR B CB  1 
ATOM   4435 O OG1 . THR B 2 183 ? -44.612 64.887 78.156  1.00 52.99  ? 183 THR B OG1 1 
ATOM   4436 C CG2 . THR B 2 183 ? -46.393 63.296 78.423  1.00 41.18  ? 183 THR B CG2 1 
ATOM   4437 N N   . PHE B 2 184 ? -45.901 62.215 81.682  1.00 44.79  ? 184 PHE B N   1 
ATOM   4438 C CA  . PHE B 2 184 ? -46.140 61.009 82.451  1.00 46.14  ? 184 PHE B CA  1 
ATOM   4439 C C   . PHE B 2 184 ? -47.193 60.141 81.778  1.00 46.05  ? 184 PHE B C   1 
ATOM   4440 O O   . PHE B 2 184 ? -48.035 60.647 81.029  1.00 45.14  ? 184 PHE B O   1 
ATOM   4441 C CB  . PHE B 2 184 ? -46.597 61.363 83.862  1.00 44.37  ? 184 PHE B CB  1 
ATOM   4442 C CG  . PHE B 2 184 ? -45.528 62.007 84.695  1.00 49.03  ? 184 PHE B CG  1 
ATOM   4443 C CD1 . PHE B 2 184 ? -45.304 63.376 84.623  1.00 46.19  ? 184 PHE B CD1 1 
ATOM   4444 C CD2 . PHE B 2 184 ? -44.741 61.244 85.542  1.00 42.08  ? 184 PHE B CD2 1 
ATOM   4445 C CE1 . PHE B 2 184 ? -44.316 63.970 85.386  1.00 48.04  ? 184 PHE B CE1 1 
ATOM   4446 C CE2 . PHE B 2 184 ? -43.752 61.830 86.307  1.00 40.75  ? 184 PHE B CE2 1 
ATOM   4447 C CZ  . PHE B 2 184 ? -43.538 63.193 86.230  1.00 45.11  ? 184 PHE B CZ  1 
ATOM   4448 N N   . PRO B 2 185 ? -47.142 58.830 82.012  1.00 48.44  ? 185 PRO B N   1 
ATOM   4449 C CA  . PRO B 2 185 ? -48.248 57.972 81.583  1.00 42.05  ? 185 PRO B CA  1 
ATOM   4450 C C   . PRO B 2 185 ? -49.562 58.485 82.147  1.00 44.36  ? 185 PRO B C   1 
ATOM   4451 O O   . PRO B 2 185 ? -49.629 58.970 83.279  1.00 43.24  ? 185 PRO B O   1 
ATOM   4452 C CB  . PRO B 2 185 ? -47.888 56.594 82.155  1.00 40.70  ? 185 PRO B CB  1 
ATOM   4453 C CG  . PRO B 2 185 ? -46.575 56.754 82.873  1.00 42.54  ? 185 PRO B CG  1 
ATOM   4454 C CD  . PRO B 2 185 ? -45.979 58.057 82.476  1.00 47.30  ? 185 PRO B CD  1 
ATOM   4455 N N   . ALA B 2 186 ? -50.608 58.404 81.333  1.00 46.39  ? 186 ALA B N   1 
ATOM   4456 C CA  . ALA B 2 186 ? -51.926 58.802 81.797  1.00 45.02  ? 186 ALA B CA  1 
ATOM   4457 C C   . ALA B 2 186 ? -52.466 57.782 82.791  1.00 45.74  ? 186 ALA B C   1 
ATOM   4458 O O   . ALA B 2 186 ? -52.106 56.603 82.768  1.00 47.72  ? 186 ALA B O   1 
ATOM   4459 C CB  . ALA B 2 186 ? -52.887 58.944 80.618  1.00 43.68  ? 186 ALA B CB  1 
ATOM   4460 N N   . VAL B 2 187 ? -53.331 58.249 83.677  1.00 46.49  ? 187 VAL B N   1 
ATOM   4461 C CA  . VAL B 2 187 ? -54.066 57.369 84.572  1.00 45.82  ? 187 VAL B CA  1 
ATOM   4462 C C   . VAL B 2 187 ? -55.522 57.374 84.138  1.00 41.29  ? 187 VAL B C   1 
ATOM   4463 O O   . VAL B 2 187 ? -56.030 58.372 83.612  1.00 42.27  ? 187 VAL B O   1 
ATOM   4464 C CB  . VAL B 2 187 ? -53.934 57.782 86.056  1.00 42.24  ? 187 VAL B CB  1 
ATOM   4465 C CG1 . VAL B 2 187 ? -52.501 57.623 86.521  1.00 40.61  ? 187 VAL B CG1 1 
ATOM   4466 C CG2 . VAL B 2 187 ? -54.411 59.217 86.264  1.00 42.04  ? 187 VAL B CG2 1 
ATOM   4467 N N   . LEU B 2 188 ? -56.188 56.243 84.346  1.00 40.16  ? 188 LEU B N   1 
ATOM   4468 C CA  . LEU B 2 188 ? -57.623 56.129 84.122  1.00 48.48  ? 188 LEU B CA  1 
ATOM   4469 C C   . LEU B 2 188 ? -58.348 56.496 85.411  1.00 48.31  ? 188 LEU B C   1 
ATOM   4470 O O   . LEU B 2 188 ? -58.081 55.910 86.466  1.00 48.17  ? 188 LEU B O   1 
ATOM   4471 C CB  . LEU B 2 188 ? -57.992 54.714 83.676  1.00 48.75  ? 188 LEU B CB  1 
ATOM   4472 C CG  . LEU B 2 188 ? -59.436 54.490 83.217  1.00 50.12  ? 188 LEU B CG  1 
ATOM   4473 C CD1 . LEU B 2 188 ? -59.835 55.471 82.114  1.00 48.37  ? 188 LEU B CD1 1 
ATOM   4474 C CD2 . LEU B 2 188 ? -59.634 53.045 82.767  1.00 39.19  ? 188 LEU B CD2 1 
ATOM   4475 N N   . GLN B 2 189 ? -59.250 57.468 85.328  1.00 53.51  ? 189 GLN B N   1 
ATOM   4476 C CA  . GLN B 2 189 ? -60.015 57.911 86.483  1.00 49.12  ? 189 GLN B CA  1 
ATOM   4477 C C   . GLN B 2 189 ? -61.288 57.079 86.639  1.00 50.66  ? 189 GLN B C   1 
ATOM   4478 O O   . GLN B 2 189 ? -61.658 56.284 85.772  1.00 49.70  ? 189 GLN B O   1 
ATOM   4479 C CB  . GLN B 2 189 ? -60.365 59.395 86.358  1.00 42.75  ? 189 GLN B CB  1 
ATOM   4480 C CG  . GLN B 2 189 ? -59.166 60.321 86.258  1.00 50.47  ? 189 GLN B CG  1 
ATOM   4481 C CD  . GLN B 2 189 ? -59.500 61.625 85.559  1.00 54.83  ? 189 GLN B CD  1 
ATOM   4482 O OE1 . GLN B 2 189 ? -59.507 62.689 86.178  1.00 58.28  ? 189 GLN B OE1 1 
ATOM   4483 N NE2 . GLN B 2 189 ? -59.785 61.547 84.260  1.00 51.61  ? 189 GLN B NE2 1 
ATOM   4484 N N   . SER B 2 190 ? -61.966 57.286 87.772  1.00 52.60  ? 190 SER B N   1 
ATOM   4485 C CA  . SER B 2 190 ? -63.206 56.568 88.048  1.00 48.16  ? 190 SER B CA  1 
ATOM   4486 C C   . SER B 2 190 ? -64.263 56.846 86.990  1.00 51.06  ? 190 SER B C   1 
ATOM   4487 O O   . SER B 2 190 ? -65.078 55.970 86.678  1.00 55.65  ? 190 SER B O   1 
ATOM   4488 C CB  . SER B 2 190 ? -63.737 56.955 89.426  1.00 50.24  ? 190 SER B CB  1 
ATOM   4489 O OG  . SER B 2 190 ? -62.701 56.958 90.390  1.00 57.25  ? 190 SER B OG  1 
ATOM   4490 N N   . SER B 2 191 ? -64.267 58.055 86.429  1.00 48.94  ? 191 SER B N   1 
ATOM   4491 C CA  . SER B 2 191 ? -65.220 58.425 85.392  1.00 48.71  ? 191 SER B CA  1 
ATOM   4492 C C   . SER B 2 191 ? -65.004 57.675 84.086  1.00 49.53  ? 191 SER B C   1 
ATOM   4493 O O   . SER B 2 191 ? -65.823 57.815 83.171  1.00 49.94  ? 191 SER B O   1 
ATOM   4494 C CB  . SER B 2 191 ? -65.136 59.926 85.128  1.00 46.70  ? 191 SER B CB  1 
ATOM   4495 O OG  . SER B 2 191 ? -63.800 60.302 84.835  1.00 49.32  ? 191 SER B OG  1 
ATOM   4496 N N   . GLY B 2 192 ? -63.939 56.884 83.975  1.00 49.13  ? 192 GLY B N   1 
ATOM   4497 C CA  . GLY B 2 192 ? -63.573 56.283 82.713  1.00 47.34  ? 192 GLY B CA  1 
ATOM   4498 C C   . GLY B 2 192 ? -62.804 57.195 81.787  1.00 46.16  ? 192 GLY B C   1 
ATOM   4499 O O   . GLY B 2 192 ? -62.503 56.793 80.657  1.00 52.00  ? 192 GLY B O   1 
ATOM   4500 N N   . LEU B 2 193 ? -62.485 58.408 82.219  1.00 47.66  ? 193 LEU B N   1 
ATOM   4501 C CA  . LEU B 2 193 ? -61.682 59.329 81.434  1.00 49.37  ? 193 LEU B CA  1 
ATOM   4502 C C   . LEU B 2 193 ? -60.225 59.255 81.868  1.00 51.36  ? 193 LEU B C   1 
ATOM   4503 O O   . LEU B 2 193 ? -59.909 58.921 83.014  1.00 48.66  ? 193 LEU B O   1 
ATOM   4504 C CB  . LEU B 2 193 ? -62.199 60.763 81.572  1.00 45.90  ? 193 LEU B CB  1 
ATOM   4505 C CG  . LEU B 2 193 ? -63.667 60.925 81.175  1.00 46.54  ? 193 LEU B CG  1 
ATOM   4506 C CD1 . LEU B 2 193 ? -64.188 62.303 81.547  1.00 37.11  ? 193 LEU B CD1 1 
ATOM   4507 C CD2 . LEU B 2 193 ? -63.836 60.654 79.690  1.00 46.17  ? 193 LEU B CD2 1 
ATOM   4508 N N   . TYR B 2 194 ? -59.338 59.557 80.930  1.00 47.64  ? 194 TYR B N   1 
ATOM   4509 C CA  . TYR B 2 194 ? -57.914 59.578 81.209  1.00 47.93  ? 194 TYR B CA  1 
ATOM   4510 C C   . TYR B 2 194 ? -57.482 60.974 81.641  1.00 46.58  ? 194 TYR B C   1 
ATOM   4511 O O   . TYR B 2 194 ? -58.153 61.974 81.373  1.00 45.52  ? 194 TYR B O   1 
ATOM   4512 C CB  . TYR B 2 194 ? -57.122 59.122 79.982  1.00 41.11  ? 194 TYR B CB  1 
ATOM   4513 C CG  . TYR B 2 194 ? -57.293 57.648 79.697  1.00 43.69  ? 194 TYR B CG  1 
ATOM   4514 C CD1 . TYR B 2 194 ? -56.478 56.709 80.309  1.00 40.51  ? 194 TYR B CD1 1 
ATOM   4515 C CD2 . TYR B 2 194 ? -58.288 57.194 78.835  1.00 45.16  ? 194 TYR B CD2 1 
ATOM   4516 C CE1 . TYR B 2 194 ? -56.634 55.361 80.061  1.00 42.62  ? 194 TYR B CE1 1 
ATOM   4517 C CE2 . TYR B 2 194 ? -58.455 55.841 78.581  1.00 42.98  ? 194 TYR B CE2 1 
ATOM   4518 C CZ  . TYR B 2 194 ? -57.622 54.931 79.198  1.00 45.43  ? 194 TYR B CZ  1 
ATOM   4519 O OH  . TYR B 2 194 ? -57.773 53.586 78.955  1.00 49.17  ? 194 TYR B OH  1 
ATOM   4520 N N   . SER B 2 195 ? -56.353 61.028 82.341  1.00 45.77  ? 195 SER B N   1 
ATOM   4521 C CA  . SER B 2 195 ? -55.773 62.302 82.731  1.00 44.80  ? 195 SER B CA  1 
ATOM   4522 C C   . SER B 2 195 ? -54.262 62.165 82.773  1.00 45.04  ? 195 SER B C   1 
ATOM   4523 O O   . SER B 2 195 ? -53.728 61.147 83.223  1.00 44.25  ? 195 SER B O   1 
ATOM   4524 C CB  . SER B 2 195 ? -56.306 62.784 84.081  1.00 47.81  ? 195 SER B CB  1 
ATOM   4525 O OG  . SER B 2 195 ? -55.836 64.092 84.353  1.00 50.28  ? 195 SER B OG  1 
ATOM   4526 N N   . LEU B 2 196 ? -53.584 63.207 82.309  1.00 48.85  ? 196 LEU B N   1 
ATOM   4527 C CA  . LEU B 2 196 ? -52.148 63.173 82.104  1.00 49.70  ? 196 LEU B CA  1 
ATOM   4528 C C   . LEU B 2 196 ? -51.541 64.493 82.557  1.00 46.60  ? 196 LEU B C   1 
ATOM   4529 O O   . LEU B 2 196 ? -52.191 65.542 82.521  1.00 45.10  ? 196 LEU B O   1 
ATOM   4530 C CB  . LEU B 2 196 ? -51.828 62.901 80.624  1.00 43.86  ? 196 LEU B CB  1 
ATOM   4531 C CG  . LEU B 2 196 ? -50.392 62.953 80.107  1.00 48.01  ? 196 LEU B CG  1 
ATOM   4532 C CD1 . LEU B 2 196 ? -50.209 61.910 79.015  1.00 44.34  ? 196 LEU B CD1 1 
ATOM   4533 C CD2 . LEU B 2 196 ? -50.056 64.346 79.586  1.00 44.03  ? 196 LEU B CD2 1 
ATOM   4534 N N   . SER B 2 197 ? -50.288 64.431 82.987  1.00 46.00  ? 197 SER B N   1 
ATOM   4535 C CA  . SER B 2 197 ? -49.518 65.623 83.303  1.00 44.19  ? 197 SER B CA  1 
ATOM   4536 C C   . SER B 2 197 ? -48.230 65.601 82.497  1.00 41.82  ? 197 SER B C   1 
ATOM   4537 O O   . SER B 2 197 ? -47.632 64.541 82.298  1.00 44.44  ? 197 SER B O   1 
ATOM   4538 C CB  . SER B 2 197 ? -49.197 65.704 84.799  1.00 46.37  ? 197 SER B CB  1 
ATOM   4539 O OG  . SER B 2 197 ? -48.249 64.713 85.161  1.00 49.22  ? 197 SER B OG  1 
ATOM   4540 N N   . SER B 2 198 ? -47.816 66.767 82.022  1.00 35.32  ? 198 SER B N   1 
ATOM   4541 C CA  . SER B 2 198 ? -46.521 66.931 81.382  1.00 41.11  ? 198 SER B CA  1 
ATOM   4542 C C   . SER B 2 198 ? -45.829 68.113 82.030  1.00 44.32  ? 198 SER B C   1 
ATOM   4543 O O   . SER B 2 198 ? -46.409 69.199 82.113  1.00 47.03  ? 198 SER B O   1 
ATOM   4544 C CB  . SER B 2 198 ? -46.653 67.160 79.878  1.00 40.56  ? 198 SER B CB  1 
ATOM   4545 O OG  . SER B 2 198 ? -45.386 67.447 79.309  1.00 43.30  ? 198 SER B OG  1 
ATOM   4546 N N   . VAL B 2 199 ? -44.601 67.901 82.494  1.00 46.72  ? 199 VAL B N   1 
ATOM   4547 C CA  . VAL B 2 199 ? -43.873 68.906 83.253  1.00 44.36  ? 199 VAL B CA  1 
ATOM   4548 C C   . VAL B 2 199 ? -42.520 69.142 82.601  1.00 46.75  ? 199 VAL B C   1 
ATOM   4549 O O   . VAL B 2 199 ? -41.982 68.275 81.905  1.00 46.12  ? 199 VAL B O   1 
ATOM   4550 C CB  . VAL B 2 199 ? -43.697 68.487 84.732  1.00 46.10  ? 199 VAL B CB  1 
ATOM   4551 C CG1 . VAL B 2 199 ? -45.040 68.123 85.343  1.00 44.04  ? 199 VAL B CG1 1 
ATOM   4552 C CG2 . VAL B 2 199 ? -42.733 67.319 84.840  1.00 47.28  ? 199 VAL B CG2 1 
ATOM   4553 N N   . VAL B 2 200 ? -41.976 70.337 82.823  1.00 44.51  ? 200 VAL B N   1 
ATOM   4554 C CA  . VAL B 2 200 ? -40.616 70.671 82.423  1.00 48.67  ? 200 VAL B CA  1 
ATOM   4555 C C   . VAL B 2 200 ? -39.935 71.341 83.607  1.00 50.10  ? 200 VAL B C   1 
ATOM   4556 O O   . VAL B 2 200 ? -40.530 72.203 84.263  1.00 51.75  ? 200 VAL B O   1 
ATOM   4557 C CB  . VAL B 2 200 ? -40.575 71.576 81.173  1.00 46.25  ? 200 VAL B CB  1 
ATOM   4558 C CG1 . VAL B 2 200 ? -41.543 72.728 81.302  1.00 49.46  ? 200 VAL B CG1 1 
ATOM   4559 C CG2 . VAL B 2 200 ? -39.165 72.090 80.921  1.00 49.15  ? 200 VAL B CG2 1 
ATOM   4560 N N   . THR B 2 201 ? -38.709 70.915 83.904  1.00 52.91  ? 201 THR B N   1 
ATOM   4561 C CA  . THR B 2 201 ? -37.882 71.553 84.922  1.00 51.87  ? 201 THR B CA  1 
ATOM   4562 C C   . THR B 2 201 ? -36.846 72.432 84.236  1.00 53.68  ? 201 THR B C   1 
ATOM   4563 O O   . THR B 2 201 ? -36.163 71.986 83.308  1.00 48.59  ? 201 THR B O   1 
ATOM   4564 C CB  . THR B 2 201 ? -37.185 70.521 85.813  1.00 48.37  ? 201 THR B CB  1 
ATOM   4565 O OG1 . THR B 2 201 ? -36.668 69.456 85.005  1.00 53.78  ? 201 THR B OG1 1 
ATOM   4566 C CG2 . THR B 2 201 ? -38.156 69.953 86.839  1.00 52.81  ? 201 THR B CG2 1 
ATOM   4567 N N   . VAL B 2 202 ? -36.751 73.678 84.676  1.00 56.36  ? 202 VAL B N   1 
ATOM   4568 C CA  . VAL B 2 202 ? -35.750 74.612 84.169  1.00 54.32  ? 202 VAL B CA  1 
ATOM   4569 C C   . VAL B 2 202 ? -34.968 75.137 85.363  1.00 54.71  ? 202 VAL B C   1 
ATOM   4570 O O   . VAL B 2 202 ? -35.440 75.066 86.511  1.00 52.95  ? 202 VAL B O   1 
ATOM   4571 C CB  . VAL B 2 202 ? -36.393 75.764 83.362  1.00 51.43  ? 202 VAL B CB  1 
ATOM   4572 C CG1 . VAL B 2 202 ? -37.332 75.221 82.299  1.00 49.26  ? 202 VAL B CG1 1 
ATOM   4573 C CG2 . VAL B 2 202 ? -37.123 76.720 84.298  1.00 52.93  ? 202 VAL B CG2 1 
ATOM   4574 N N   . PRO B 2 203 ? -33.760 75.651 85.137  1.00 60.08  ? 203 PRO B N   1 
ATOM   4575 C CA  . PRO B 2 203 ? -33.056 76.354 86.219  1.00 60.08  ? 203 PRO B CA  1 
ATOM   4576 C C   . PRO B 2 203 ? -33.869 77.553 86.685  1.00 61.11  ? 203 PRO B C   1 
ATOM   4577 O O   . PRO B 2 203 ? -34.350 78.351 85.877  1.00 63.49  ? 203 PRO B O   1 
ATOM   4578 C CB  . PRO B 2 203 ? -31.729 76.776 85.574  1.00 50.11  ? 203 PRO B CB  1 
ATOM   4579 C CG  . PRO B 2 203 ? -31.563 75.871 84.395  1.00 52.03  ? 203 PRO B CG  1 
ATOM   4580 C CD  . PRO B 2 203 ? -32.945 75.551 83.912  1.00 51.13  ? 203 PRO B CD  1 
ATOM   4581 N N   . SER B 2 204 ? -34.038 77.663 88.006  1.00 58.88  ? 204 SER B N   1 
ATOM   4582 C CA  . SER B 2 204 ? -34.891 78.708 88.561  1.00 62.41  ? 204 SER B CA  1 
ATOM   4583 C C   . SER B 2 204 ? -34.341 80.104 88.307  1.00 63.54  ? 204 SER B C   1 
ATOM   4584 O O   . SER B 2 204 ? -35.102 81.075 88.371  1.00 62.24  ? 204 SER B O   1 
ATOM   4585 C CB  . SER B 2 204 ? -35.087 78.487 90.061  1.00 65.42  ? 204 SER B CB  1 
ATOM   4586 O OG  . SER B 2 204 ? -33.849 78.251 90.703  1.00 72.78  ? 204 SER B OG  1 
ATOM   4587 N N   . SER B 2 205 ? -33.043 80.227 88.018  1.00 65.18  ? 205 SER B N   1 
ATOM   4588 C CA  . SER B 2 205 ? -32.466 81.518 87.664  1.00 63.91  ? 205 SER B CA  1 
ATOM   4589 C C   . SER B 2 205 ? -32.828 81.957 86.252  1.00 67.30  ? 205 SER B C   1 
ATOM   4590 O O   . SER B 2 205 ? -32.500 83.085 85.870  1.00 67.10  ? 205 SER B O   1 
ATOM   4591 C CB  . SER B 2 205 ? -30.945 81.467 87.812  1.00 64.64  ? 205 SER B CB  1 
ATOM   4592 O OG  . SER B 2 205 ? -30.374 80.581 86.866  1.00 67.33  ? 205 SER B OG  1 
ATOM   4593 N N   . SER B 2 206 ? -33.493 81.101 85.473  1.00 62.61  ? 206 SER B N   1 
ATOM   4594 C CA  . SER B 2 206 ? -33.861 81.411 84.097  1.00 61.46  ? 206 SER B CA  1 
ATOM   4595 C C   . SER B 2 206 ? -35.370 81.374 83.882  1.00 63.59  ? 206 SER B C   1 
ATOM   4596 O O   . SER B 2 206 ? -35.823 81.299 82.734  1.00 64.83  ? 206 SER B O   1 
ATOM   4597 C CB  . SER B 2 206 ? -33.174 80.442 83.134  1.00 63.10  ? 206 SER B CB  1 
ATOM   4598 O OG  . SER B 2 206 ? -33.947 79.264 82.973  1.00 63.50  ? 206 SER B OG  1 
ATOM   4599 N N   . LEU B 2 207 ? -36.154 81.422 84.963  1.00 59.46  ? 207 LEU B N   1 
ATOM   4600 C CA  . LEU B 2 207 ? -37.604 81.281 84.854  1.00 60.05  ? 207 LEU B CA  1 
ATOM   4601 C C   . LEU B 2 207 ? -38.194 82.300 83.886  1.00 60.42  ? 207 LEU B C   1 
ATOM   4602 O O   . LEU B 2 207 ? -38.823 81.938 82.885  1.00 67.30  ? 207 LEU B O   1 
ATOM   4603 C CB  . LEU B 2 207 ? -38.248 81.413 86.236  1.00 59.38  ? 207 LEU B CB  1 
ATOM   4604 C CG  . LEU B 2 207 ? -38.953 80.163 86.765  1.00 56.32  ? 207 LEU B CG  1 
ATOM   4605 C CD1 . LEU B 2 207 ? -39.852 80.502 87.939  1.00 55.01  ? 207 LEU B CD1 1 
ATOM   4606 C CD2 . LEU B 2 207 ? -39.749 79.488 85.654  1.00 54.46  ? 207 LEU B CD2 1 
ATOM   4607 N N   . GLY B 2 208 ? -37.986 83.585 84.161  1.00 57.85  ? 208 GLY B N   1 
ATOM   4608 C CA  . GLY B 2 208 ? -38.580 84.631 83.349  1.00 56.15  ? 208 GLY B CA  1 
ATOM   4609 C C   . GLY B 2 208 ? -37.800 85.018 82.107  1.00 52.99  ? 208 GLY B C   1 
ATOM   4610 O O   . GLY B 2 208 ? -38.041 86.083 81.533  1.00 49.03  ? 208 GLY B O   1 
ATOM   4611 N N   . THR B 2 209 ? -36.862 84.173 81.676  1.00 46.12  ? 209 THR B N   1 
ATOM   4612 C CA  . THR B 2 209 ? -36.090 84.444 80.470  1.00 47.72  ? 209 THR B CA  1 
ATOM   4613 C C   . THR B 2 209 ? -36.658 83.764 79.230  1.00 47.11  ? 209 THR B C   1 
ATOM   4614 O O   . THR B 2 209 ? -36.273 84.126 78.114  1.00 46.06  ? 209 THR B O   1 
ATOM   4615 C CB  . THR B 2 209 ? -34.628 84.015 80.657  1.00 48.54  ? 209 THR B CB  1 
ATOM   4616 O OG1 . THR B 2 209 ? -34.529 82.588 80.575  1.00 51.26  ? 209 THR B OG1 1 
ATOM   4617 C CG2 . THR B 2 209 ? -34.100 84.483 82.008  1.00 51.04  ? 209 THR B CG2 1 
ATOM   4618 N N   . GLN B 2 210 ? -37.562 82.804 79.397  1.00 48.08  ? 210 GLN B N   1 
ATOM   4619 C CA  . GLN B 2 210 ? -38.138 82.060 78.291  1.00 46.02  ? 210 GLN B CA  1 
ATOM   4620 C C   . GLN B 2 210 ? -39.625 81.871 78.557  1.00 48.54  ? 210 GLN B C   1 
ATOM   4621 O O   . GLN B 2 210 ? -40.068 81.875 79.710  1.00 49.05  ? 210 GLN B O   1 
ATOM   4622 C CB  . GLN B 2 210 ? -37.422 80.707 78.113  1.00 46.83  ? 210 GLN B CB  1 
ATOM   4623 C CG  . GLN B 2 210 ? -37.995 79.792 77.039  1.00 42.82  ? 210 GLN B CG  1 
ATOM   4624 C CD  . GLN B 2 210 ? -37.933 80.403 75.647  1.00 49.71  ? 210 GLN B CD  1 
ATOM   4625 O OE1 . GLN B 2 210 ? -38.734 81.274 75.301  1.00 45.32  ? 210 GLN B OE1 1 
ATOM   4626 N NE2 . GLN B 2 210 ? -36.980 79.940 74.838  1.00 45.83  ? 210 GLN B NE2 1 
ATOM   4627 N N   . THR B 2 211 ? -40.397 81.745 77.480  1.00 40.25  ? 211 THR B N   1 
ATOM   4628 C CA  . THR B 2 211 ? -41.815 81.429 77.553  1.00 45.67  ? 211 THR B CA  1 
ATOM   4629 C C   . THR B 2 211 ? -42.022 79.949 77.246  1.00 46.26  ? 211 THR B C   1 
ATOM   4630 O O   . THR B 2 211 ? -41.284 79.354 76.455  1.00 44.64  ? 211 THR B O   1 
ATOM   4631 C CB  . THR B 2 211 ? -42.611 82.301 76.577  1.00 41.11  ? 211 THR B CB  1 
ATOM   4632 O OG1 . THR B 2 211 ? -42.423 83.678 76.919  1.00 45.52  ? 211 THR B OG1 1 
ATOM   4633 C CG2 . THR B 2 211 ? -44.100 81.979 76.628  1.00 42.56  ? 211 THR B CG2 1 
ATOM   4634 N N   . TYR B 2 212 ? -43.030 79.355 77.885  1.00 44.86  ? 212 TYR B N   1 
ATOM   4635 C CA  . TYR B 2 212 ? -43.270 77.915 77.823  1.00 48.99  ? 212 TYR B CA  1 
ATOM   4636 C C   . TYR B 2 212 ? -44.699 77.652 77.364  1.00 46.86  ? 212 TYR B C   1 
ATOM   4637 O O   . TYR B 2 212 ? -45.649 77.853 78.130  1.00 49.03  ? 212 TYR B O   1 
ATOM   4638 C CB  . TYR B 2 212 ? -43.006 77.274 79.184  1.00 48.71  ? 212 TYR B CB  1 
ATOM   4639 C CG  . TYR B 2 212 ? -41.647 77.621 79.758  1.00 52.97  ? 212 TYR B CG  1 
ATOM   4640 C CD1 . TYR B 2 212 ? -40.494 76.992 79.299  1.00 53.37  ? 212 TYR B CD1 1 
ATOM   4641 C CD2 . TYR B 2 212 ? -41.516 78.588 80.750  1.00 52.12  ? 212 TYR B CD2 1 
ATOM   4642 C CE1 . TYR B 2 212 ? -39.247 77.307 79.822  1.00 53.91  ? 212 TYR B CE1 1 
ATOM   4643 C CE2 . TYR B 2 212 ? -40.270 78.910 81.278  1.00 52.86  ? 212 TYR B CE2 1 
ATOM   4644 C CZ  . TYR B 2 212 ? -39.141 78.265 80.809  1.00 51.10  ? 212 TYR B CZ  1 
ATOM   4645 O OH  . TYR B 2 212 ? -37.902 78.579 81.327  1.00 61.03  ? 212 TYR B OH  1 
ATOM   4646 N N   . ILE B 2 213 ? -44.851 77.204 76.118  1.00 42.45  ? 213 ILE B N   1 
ATOM   4647 C CA  . ILE B 2 213 ? -46.145 76.806 75.569  1.00 46.71  ? 213 ILE B CA  1 
ATOM   4648 C C   . ILE B 2 213 ? -46.175 75.286 75.522  1.00 47.11  ? 213 ILE B C   1 
ATOM   4649 O O   . ILE B 2 213 ? -45.316 74.667 74.884  1.00 43.72  ? 213 ILE B O   1 
ATOM   4650 C CB  . ILE B 2 213 ? -46.386 77.367 74.155  1.00 47.61  ? 213 ILE B CB  1 
ATOM   4651 C CG1 . ILE B 2 213 ? -46.192 78.884 74.043  1.00 49.58  ? 213 ILE B CG1 1 
ATOM   4652 C CG2 . ILE B 2 213 ? -47.804 77.020 73.700  1.00 42.70  ? 213 ILE B CG2 1 
ATOM   4653 C CD1 . ILE B 2 213 ? -46.523 79.659 75.261  1.00 50.46  ? 213 ILE B CD1 1 
ATOM   4654 N N   . CYS B 2 214 ? -47.163 74.678 76.171  1.00 46.50  ? 214 CYS B N   1 
ATOM   4655 C CA  . CYS B 2 214 ? -47.419 73.258 75.979  1.00 47.29  ? 214 CYS B CA  1 
ATOM   4656 C C   . CYS B 2 214 ? -48.455 73.087 74.874  1.00 47.83  ? 214 CYS B C   1 
ATOM   4657 O O   . CYS B 2 214 ? -49.504 73.738 74.887  1.00 47.62  ? 214 CYS B O   1 
ATOM   4658 C CB  . CYS B 2 214 ? -47.871 72.591 77.281  1.00 43.01  ? 214 CYS B CB  1 
ATOM   4659 S SG  . CYS B 2 214 ? -49.625 72.642 77.669  1.00 50.40  ? 214 CYS B SG  1 
ATOM   4660 N N   . ASN B 2 215 ? -48.133 72.248 73.896  1.00 45.30  ? 215 ASN B N   1 
ATOM   4661 C CA  . ASN B 2 215 ? -49.009 71.973 72.763  1.00 46.70  ? 215 ASN B CA  1 
ATOM   4662 C C   . ASN B 2 215 ? -49.628 70.601 72.969  1.00 44.62  ? 215 ASN B C   1 
ATOM   4663 O O   . ASN B 2 215 ? -48.911 69.597 73.045  1.00 43.65  ? 215 ASN B O   1 
ATOM   4664 C CB  . ASN B 2 215 ? -48.237 72.028 71.443  1.00 44.49  ? 215 ASN B CB  1 
ATOM   4665 C CG  . ASN B 2 215 ? -47.229 73.162 71.406  1.00 48.84  ? 215 ASN B CG  1 
ATOM   4666 O OD1 . ASN B 2 215 ? -46.023 72.941 71.541  1.00 46.84  ? 215 ASN B OD1 1 
ATOM   4667 N ND2 . ASN B 2 215 ? -47.717 74.385 71.226  1.00 48.12  ? 215 ASN B ND2 1 
ATOM   4668 N N   . VAL B 2 216 ? -50.952 70.561 73.068  1.00 43.69  ? 216 VAL B N   1 
ATOM   4669 C CA  . VAL B 2 216 ? -51.682 69.333 73.346  1.00 46.17  ? 216 VAL B CA  1 
ATOM   4670 C C   . VAL B 2 216 ? -52.535 69.003 72.132  1.00 46.51  ? 216 VAL B C   1 
ATOM   4671 O O   . VAL B 2 216 ? -53.283 69.855 71.640  1.00 49.65  ? 216 VAL B O   1 
ATOM   4672 C CB  . VAL B 2 216 ? -52.547 69.456 74.615  1.00 44.59  ? 216 VAL B CB  1 
ATOM   4673 C CG1 . VAL B 2 216 ? -53.420 68.222 74.788  1.00 38.16  ? 216 VAL B CG1 1 
ATOM   4674 C CG2 . VAL B 2 216 ? -51.662 69.663 75.834  1.00 42.42  ? 216 VAL B CG2 1 
ATOM   4675 N N   . ASN B 2 217 ? -52.411 67.770 71.649  1.00 48.45  ? 217 ASN B N   1 
ATOM   4676 C CA  . ASN B 2 217 ? -53.180 67.284 70.512  1.00 48.24  ? 217 ASN B CA  1 
ATOM   4677 C C   . ASN B 2 217 ? -53.825 65.963 70.897  1.00 44.39  ? 217 ASN B C   1 
ATOM   4678 O O   . ASN B 2 217 ? -53.124 65.003 71.232  1.00 45.18  ? 217 ASN B O   1 
ATOM   4679 C CB  . ASN B 2 217 ? -52.292 67.111 69.275  1.00 45.45  ? 217 ASN B CB  1 
ATOM   4680 C CG  . ASN B 2 217 ? -53.098 66.930 67.999  1.00 55.62  ? 217 ASN B CG  1 
ATOM   4681 O OD1 . ASN B 2 217 ? -54.333 66.939 68.019  1.00 54.90  ? 217 ASN B OD1 1 
ATOM   4682 N ND2 . ASN B 2 217 ? -52.400 66.747 66.881  1.00 57.30  ? 217 ASN B ND2 1 
ATOM   4683 N N   . HIS B 2 218 ? -55.150 65.919 70.867  1.00 48.17  ? 218 HIS B N   1 
ATOM   4684 C CA  . HIS B 2 218 ? -55.906 64.685 71.063  1.00 49.14  ? 218 HIS B CA  1 
ATOM   4685 C C   . HIS B 2 218 ? -56.569 64.386 69.721  1.00 47.79  ? 218 HIS B C   1 
ATOM   4686 O O   . HIS B 2 218 ? -57.650 64.894 69.418  1.00 47.90  ? 218 HIS B O   1 
ATOM   4687 C CB  . HIS B 2 218 ? -56.926 64.818 72.191  1.00 47.49  ? 218 HIS B CB  1 
ATOM   4688 C CG  . HIS B 2 218 ? -57.661 63.550 72.498  1.00 48.31  ? 218 HIS B CG  1 
ATOM   4689 N ND1 . HIS B 2 218 ? -59.037 63.462 72.473  1.00 48.08  ? 218 HIS B ND1 1 
ATOM   4690 C CD2 . HIS B 2 218 ? -57.212 62.322 72.850  1.00 46.15  ? 218 HIS B CD2 1 
ATOM   4691 C CE1 . HIS B 2 218 ? -59.404 62.232 72.792  1.00 46.70  ? 218 HIS B CE1 1 
ATOM   4692 N NE2 . HIS B 2 218 ? -58.315 61.521 73.026  1.00 47.70  ? 218 HIS B NE2 1 
ATOM   4693 N N   . LYS B 2 219 ? -55.892 63.570 68.912  1.00 43.03  ? 219 LYS B N   1 
ATOM   4694 C CA  . LYS B 2 219 ? -56.389 63.270 67.571  1.00 47.65  ? 219 LYS B CA  1 
ATOM   4695 C C   . LYS B 2 219 ? -57.776 62.631 67.538  1.00 49.50  ? 219 LYS B C   1 
ATOM   4696 O O   . LYS B 2 219 ? -58.554 62.982 66.633  1.00 46.46  ? 219 LYS B O   1 
ATOM   4697 C CB  . LYS B 2 219 ? -55.373 62.390 66.833  1.00 40.56  ? 219 LYS B CB  1 
ATOM   4698 C CG  . LYS B 2 219 ? -54.205 63.172 66.273  1.00 47.19  ? 219 LYS B CG  1 
ATOM   4699 C CD  . LYS B 2 219 ? -52.899 62.399 66.366  1.00 48.40  ? 219 LYS B CD  1 
ATOM   4700 C CE  . LYS B 2 219 ? -51.901 62.913 65.338  1.00 53.17  ? 219 LYS B CE  1 
ATOM   4701 N NZ  . LYS B 2 219 ? -50.545 62.337 65.534  1.00 55.05  ? 219 LYS B NZ  1 
ATOM   4702 N N   . PRO B 2 220 ? -58.154 61.716 68.444  1.00 47.83  ? 220 PRO B N   1 
ATOM   4703 C CA  . PRO B 2 220 ? -59.500 61.123 68.341  1.00 49.63  ? 220 PRO B CA  1 
ATOM   4704 C C   . PRO B 2 220 ? -60.628 62.143 68.334  1.00 50.62  ? 220 PRO B C   1 
ATOM   4705 O O   . PRO B 2 220 ? -61.685 61.875 67.750  1.00 47.40  ? 220 PRO B O   1 
ATOM   4706 C CB  . PRO B 2 220 ? -59.573 60.209 69.571  1.00 48.81  ? 220 PRO B CB  1 
ATOM   4707 C CG  . PRO B 2 220 ? -58.160 59.823 69.821  1.00 47.42  ? 220 PRO B CG  1 
ATOM   4708 C CD  . PRO B 2 220 ? -57.354 61.049 69.491  1.00 43.65  ? 220 PRO B CD  1 
ATOM   4709 N N   . SER B 2 221 ? -60.439 63.305 68.958  1.00 51.40  ? 221 SER B N   1 
ATOM   4710 C CA  . SER B 2 221 ? -61.441 64.363 68.962  1.00 48.40  ? 221 SER B CA  1 
ATOM   4711 C C   . SER B 2 221 ? -60.975 65.613 68.230  1.00 49.74  ? 221 SER B C   1 
ATOM   4712 O O   . SER B 2 221 ? -61.672 66.633 68.271  1.00 52.29  ? 221 SER B O   1 
ATOM   4713 C CB  . SER B 2 221 ? -61.827 64.724 70.398  1.00 52.22  ? 221 SER B CB  1 
ATOM   4714 O OG  . SER B 2 221 ? -60.686 65.098 71.155  1.00 51.10  ? 221 SER B OG  1 
ATOM   4715 N N   . ASN B 2 222 ? -59.814 65.557 67.573  1.00 51.63  ? 222 ASN B N   1 
ATOM   4716 C CA  . ASN B 2 222 ? -59.212 66.700 66.882  1.00 53.64  ? 222 ASN B CA  1 
ATOM   4717 C C   . ASN B 2 222 ? -59.204 67.941 67.775  1.00 52.53  ? 222 ASN B C   1 
ATOM   4718 O O   . ASN B 2 222 ? -59.576 69.043 67.368  1.00 52.97  ? 222 ASN B O   1 
ATOM   4719 C CB  . ASN B 2 222 ? -59.914 66.977 65.548  1.00 56.75  ? 222 ASN B CB  1 
ATOM   4720 C CG  . ASN B 2 222 ? -59.220 68.069 64.730  1.00 68.09  ? 222 ASN B CG  1 
ATOM   4721 O OD1 . ASN B 2 222 ? -58.077 67.905 64.292  1.00 64.56  ? 222 ASN B OD1 1 
ATOM   4722 N ND2 . ASN B 2 222 ? -59.912 69.191 64.526  1.00 62.75  ? 222 ASN B ND2 1 
ATOM   4723 N N   . THR B 2 223 ? -58.784 67.747 69.022  1.00 50.47  ? 223 THR B N   1 
ATOM   4724 C CA  . THR B 2 223 ? -58.551 68.855 69.936  1.00 47.64  ? 223 THR B CA  1 
ATOM   4725 C C   . THR B 2 223 ? -57.077 69.234 69.871  1.00 54.16  ? 223 THR B C   1 
ATOM   4726 O O   . THR B 2 223 ? -56.202 68.393 70.109  1.00 54.86  ? 223 THR B O   1 
ATOM   4727 C CB  . THR B 2 223 ? -58.952 68.490 71.365  1.00 47.52  ? 223 THR B CB  1 
ATOM   4728 O OG1 . THR B 2 223 ? -60.221 67.822 71.356  1.00 51.22  ? 223 THR B OG1 1 
ATOM   4729 C CG2 . THR B 2 223 ? -59.050 69.742 72.224  1.00 43.31  ? 223 THR B CG2 1 
ATOM   4730 N N   . LYS B 2 224 ? -56.805 70.490 69.525  1.00 53.38  ? 224 LYS B N   1 
ATOM   4731 C CA  . LYS B 2 224 ? -55.451 71.036 69.500  1.00 52.76  ? 224 LYS B CA  1 
ATOM   4732 C C   . LYS B 2 224 ? -55.454 72.289 70.361  1.00 58.32  ? 224 LYS B C   1 
ATOM   4733 O O   . LYS B 2 224 ? -56.094 73.284 70.007  1.00 65.45  ? 224 LYS B O   1 
ATOM   4734 C CB  . LYS B 2 224 ? -54.998 71.359 68.075  1.00 52.31  ? 224 LYS B CB  1 
ATOM   4735 C CG  . LYS B 2 224 ? -54.786 70.148 67.187  1.00 57.35  ? 224 LYS B CG  1 
ATOM   4736 C CD  . LYS B 2 224 ? -54.330 70.562 65.796  1.00 55.59  ? 224 LYS B CD  1 
ATOM   4737 N N   . VAL B 2 225 ? -54.751 72.241 71.490  1.00 56.27  ? 225 VAL B N   1 
ATOM   4738 C CA  . VAL B 2 225 ? -54.740 73.332 72.456  1.00 53.15  ? 225 VAL B CA  1 
ATOM   4739 C C   . VAL B 2 225 ? -53.297 73.723 72.737  1.00 53.42  ? 225 VAL B C   1 
ATOM   4740 O O   . VAL B 2 225 ? -52.446 72.856 72.969  1.00 54.23  ? 225 VAL B O   1 
ATOM   4741 C CB  . VAL B 2 225 ? -55.456 72.945 73.766  1.00 54.53  ? 225 VAL B CB  1 
ATOM   4742 C CG1 . VAL B 2 225 ? -55.525 74.136 74.709  1.00 54.76  ? 225 VAL B CG1 1 
ATOM   4743 C CG2 . VAL B 2 225 ? -56.849 72.413 73.476  1.00 52.03  ? 225 VAL B CG2 1 
ATOM   4744 N N   . ASP B 2 226 ? -53.022 75.022 72.704  1.00 54.78  ? 226 ASP B N   1 
ATOM   4745 C CA  . ASP B 2 226 ? -51.756 75.583 73.153  1.00 50.69  ? 226 ASP B CA  1 
ATOM   4746 C C   . ASP B 2 226 ? -52.020 76.396 74.411  1.00 53.13  ? 226 ASP B C   1 
ATOM   4747 O O   . ASP B 2 226 ? -52.910 77.253 74.419  1.00 55.83  ? 226 ASP B O   1 
ATOM   4748 C CB  . ASP B 2 226 ? -51.125 76.461 72.071  1.00 47.18  ? 226 ASP B CB  1 
ATOM   4749 C CG  . ASP B 2 226 ? -50.782 75.688 70.816  1.00 51.88  ? 226 ASP B CG  1 
ATOM   4750 O OD1 . ASP B 2 226 ? -50.100 74.645 70.914  1.00 52.31  ? 226 ASP B OD1 1 
ATOM   4751 O OD2 . ASP B 2 226 ? -51.190 76.130 69.723  1.00 58.35  ? 226 ASP B OD2 1 
ATOM   4752 N N   . LYS B 2 227 ? -51.265 76.121 75.474  1.00 49.23  ? 227 LYS B N   1 
ATOM   4753 C CA  . LYS B 2 227 ? -51.485 76.764 76.764  1.00 53.25  ? 227 LYS B CA  1 
ATOM   4754 C C   . LYS B 2 227 ? -50.175 77.349 77.270  1.00 52.71  ? 227 LYS B C   1 
ATOM   4755 O O   . LYS B 2 227 ? -49.225 76.606 77.538  1.00 47.26  ? 227 LYS B O   1 
ATOM   4756 C CB  . LYS B 2 227 ? -52.067 75.775 77.781  1.00 54.94  ? 227 LYS B CB  1 
ATOM   4757 C CG  . LYS B 2 227 ? -51.946 76.218 79.236  1.00 54.66  ? 227 LYS B CG  1 
ATOM   4758 C CD  . LYS B 2 227 ? -52.995 77.270 79.603  1.00 56.52  ? 227 LYS B CD  1 
ATOM   4759 C CE  . LYS B 2 227 ? -54.382 76.890 79.106  1.00 61.44  ? 227 LYS B CE  1 
ATOM   4760 N NZ  . LYS B 2 227 ? -55.440 77.680 79.792  1.00 57.66  ? 227 LYS B NZ  1 
ATOM   4761 N N   . ARG B 2 228 ? -50.126 78.679 77.391  1.00 51.72  ? 228 ARG B N   1 
ATOM   4762 C CA  . ARG B 2 228 ? -48.989 79.354 78.006  1.00 52.53  ? 228 ARG B CA  1 
ATOM   4763 C C   . ARG B 2 228 ? -48.980 79.103 79.509  1.00 53.70  ? 228 ARG B C   1 
ATOM   4764 O O   . ARG B 2 228 ? -50.002 79.263 80.182  1.00 52.82  ? 228 ARG B O   1 
ATOM   4765 C CB  . ARG B 2 228 ? -49.052 80.858 77.726  1.00 53.37  ? 228 ARG B CB  1 
ATOM   4766 C CG  . ARG B 2 228 ? -47.711 81.575 77.707  1.00 55.54  ? 228 ARG B CG  1 
ATOM   4767 C CD  . ARG B 2 228 ? -47.853 83.037 77.334  1.00 55.57  ? 228 ARG B CD  1 
ATOM   4768 N NE  . ARG B 2 228 ? -47.753 83.259 75.895  1.00 68.01  ? 228 ARG B NE  1 
ATOM   4769 C CZ  . ARG B 2 228 ? -47.079 84.253 75.329  1.00 64.86  ? 228 ARG B CZ  1 
ATOM   4770 N NH1 . ARG B 2 228 ? -46.362 85.103 76.048  1.00 61.69  ? 228 ARG B NH1 1 
ATOM   4771 N NH2 . ARG B 2 228 ? -47.132 84.400 74.008  1.00 56.44  ? 228 ARG B NH2 1 
ATOM   4772 N N   . VAL B 2 229 ? -47.825 78.715 80.039  1.00 53.38  ? 229 VAL B N   1 
ATOM   4773 C CA  . VAL B 2 229 ? -47.657 78.484 81.468  1.00 51.11  ? 229 VAL B CA  1 
ATOM   4774 C C   . VAL B 2 229 ? -46.842 79.640 82.026  1.00 54.69  ? 229 VAL B C   1 
ATOM   4775 O O   . VAL B 2 229 ? -45.622 79.708 81.827  1.00 56.21  ? 229 VAL B O   1 
ATOM   4776 C CB  . VAL B 2 229 ? -46.987 77.137 81.759  1.00 53.91  ? 229 VAL B CB  1 
ATOM   4777 C CG1 . VAL B 2 229 ? -46.856 76.931 83.260  1.00 53.64  ? 229 VAL B CG1 1 
ATOM   4778 C CG2 . VAL B 2 229 ? -47.781 76.003 81.125  1.00 50.60  ? 229 VAL B CG2 1 
ATOM   4779 N N   . GLU B 2 230 ? -47.514 80.544 82.735  1.00 63.07  ? 230 GLU B N   1 
ATOM   4780 C CA  . GLU B 2 230 ? -47.091 81.799 83.339  1.00 61.71  ? 230 GLU B CA  1 
ATOM   4781 C C   . GLU B 2 230 ? -46.817 81.635 84.826  1.00 61.96  ? 230 GLU B C   1 
ATOM   4782 O O   . GLU B 2 230 ? -47.601 80.994 85.536  1.00 66.68  ? 230 GLU B O   1 
ATOM   4783 C CB  . GLU B 2 230 ? -48.165 82.868 83.149  1.00 66.12  ? 230 GLU B CB  1 
ATOM   4784 C CG  . GLU B 2 230 ? -48.610 83.064 81.717  1.00 63.81  ? 230 GLU B CG  1 
ATOM   4785 C CD  . GLU B 2 230 ? -47.687 83.982 80.949  1.00 73.86  ? 230 GLU B CD  1 
ATOM   4786 O OE1 . GLU B 2 230 ? -46.506 84.111 81.341  1.00 75.86  ? 230 GLU B OE1 1 
ATOM   4787 O OE2 . GLU B 2 230 ? -48.148 84.594 79.963  1.00 80.78  ? 230 GLU B OE2 1 
ATOM   4788 N N   . PRO B 2 231 ? -45.716 82.218 85.323  1.00 67.89  ? 231 PRO B N   1 
ATOM   4789 C CA  . PRO B 2 231 ? -45.409 82.269 86.758  1.00 75.15  ? 231 PRO B CA  1 
ATOM   4790 C C   . PRO B 2 231 ? -46.534 82.903 87.572  1.00 69.87  ? 231 PRO B C   1 
ATOM   4791 O O   . PRO B 2 231 ? -46.919 82.341 88.597  1.00 74.39  ? 231 PRO B O   1 
ATOM   4792 C CB  . PRO B 2 231 ? -44.145 83.132 86.813  1.00 71.71  ? 231 PRO B CB  1 
ATOM   4793 C CG  . PRO B 2 231 ? -43.489 82.907 85.496  1.00 76.32  ? 231 PRO B CG  1 
ATOM   4794 C CD  . PRO B 2 231 ? -44.615 82.753 84.504  1.00 75.25  ? 231 PRO B CD  1 
ATOM   4795 N N   . GLU C 3 1   ? -47.494 26.363 66.468  1.00 53.75  ? 1   GLU C N   1 
ATOM   4796 C CA  . GLU C 3 1   ? -46.576 27.476 66.270  1.00 49.49  ? 1   GLU C CA  1 
ATOM   4797 C C   . GLU C 3 1   ? -45.274 27.239 67.023  1.00 44.81  ? 1   GLU C C   1 
ATOM   4798 O O   . GLU C 3 1   ? -45.206 26.394 67.915  1.00 46.72  ? 1   GLU C O   1 
ATOM   4799 C CB  . GLU C 3 1   ? -47.212 28.789 66.734  1.00 49.10  ? 1   GLU C CB  1 
ATOM   4800 C CG  . GLU C 3 1   ? -46.952 29.100 68.200  1.00 51.42  ? 1   GLU C CG  1 
ATOM   4801 C CD  . GLU C 3 1   ? -47.790 30.244 68.718  1.00 57.82  ? 1   GLU C CD  1 
ATOM   4802 O OE1 . GLU C 3 1   ? -48.149 31.129 67.908  1.00 56.75  ? 1   GLU C OE1 1 
ATOM   4803 O OE2 . GLU C 3 1   ? -48.086 30.255 69.936  1.00 61.49  ? 1   GLU C OE2 1 
ATOM   4804 N N   . ILE C 3 2   ? -44.242 27.991 66.665  1.00 44.08  ? 2   ILE C N   1 
ATOM   4805 C CA  . ILE C 3 2   ? -42.981 27.965 67.394  1.00 40.78  ? 2   ILE C CA  1 
ATOM   4806 C C   . ILE C 3 2   ? -43.019 29.052 68.457  1.00 40.21  ? 2   ILE C C   1 
ATOM   4807 O O   . ILE C 3 2   ? -43.292 30.221 68.157  1.00 44.00  ? 2   ILE C O   1 
ATOM   4808 C CB  . ILE C 3 2   ? -41.789 28.152 66.443  1.00 38.17  ? 2   ILE C CB  1 
ATOM   4809 C CG1 . ILE C 3 2   ? -41.678 26.947 65.504  1.00 34.34  ? 2   ILE C CG1 1 
ATOM   4810 C CG2 . ILE C 3 2   ? -40.503 28.346 67.241  1.00 36.77  ? 2   ILE C CG2 1 
ATOM   4811 C CD1 . ILE C 3 2   ? -40.992 27.241 64.202  1.00 32.21  ? 2   ILE C CD1 1 
ATOM   4812 N N   . VAL C 3 3   ? -42.769 28.665 69.702  1.00 40.24  ? 3   VAL C N   1 
ATOM   4813 C CA  . VAL C 3 3   ? -42.839 29.568 70.841  1.00 37.90  ? 3   VAL C CA  1 
ATOM   4814 C C   . VAL C 3 3   ? -41.426 29.998 71.204  1.00 42.99  ? 3   VAL C C   1 
ATOM   4815 O O   . VAL C 3 3   ? -40.513 29.165 71.277  1.00 35.86  ? 3   VAL C O   1 
ATOM   4816 C CB  . VAL C 3 3   ? -43.543 28.903 72.036  1.00 44.83  ? 3   VAL C CB  1 
ATOM   4817 C CG1 . VAL C 3 3   ? -43.604 29.858 73.226  1.00 41.01  ? 3   VAL C CG1 1 
ATOM   4818 C CG2 . VAL C 3 3   ? -44.939 28.445 71.632  1.00 37.68  ? 3   VAL C CG2 1 
ATOM   4819 N N   . MET C 3 4   ? -41.245 31.300 71.408  1.00 42.21  ? 4   MET C N   1 
ATOM   4820 C CA  . MET C 3 4   ? -39.974 31.889 71.798  1.00 36.86  ? 4   MET C CA  1 
ATOM   4821 C C   . MET C 3 4   ? -40.083 32.344 73.244  1.00 34.89  ? 4   MET C C   1 
ATOM   4822 O O   . MET C 3 4   ? -41.000 33.093 73.595  1.00 39.36  ? 4   MET C O   1 
ATOM   4823 C CB  . MET C 3 4   ? -39.621 33.078 70.898  1.00 38.52  ? 4   MET C CB  1 
ATOM   4824 C CG  . MET C 3 4   ? -39.476 32.755 69.408  1.00 37.57  ? 4   MET C CG  1 
ATOM   4825 S SD  . MET C 3 4   ? -38.564 31.241 69.030  1.00 38.30  ? 4   MET C SD  1 
ATOM   4826 C CE  . MET C 3 4   ? -36.897 31.781 69.355  1.00 30.66  ? 4   MET C CE  1 
ATOM   4827 N N   . THR C 3 5   ? -39.156 31.893 74.082  1.00 39.70  ? 5   THR C N   1 
ATOM   4828 C CA  . THR C 3 5   ? -39.150 32.239 75.497  1.00 38.19  ? 5   THR C CA  1 
ATOM   4829 C C   . THR C 3 5   ? -37.879 33.010 75.826  1.00 37.48  ? 5   THR C C   1 
ATOM   4830 O O   . THR C 3 5   ? -36.770 32.544 75.541  1.00 39.89  ? 5   THR C O   1 
ATOM   4831 C CB  . THR C 3 5   ? -39.262 30.985 76.368  1.00 36.59  ? 5   THR C CB  1 
ATOM   4832 O OG1 . THR C 3 5   ? -40.458 30.278 76.025  1.00 35.41  ? 5   THR C OG1 1 
ATOM   4833 C CG2 . THR C 3 5   ? -39.310 31.358 77.835  1.00 35.69  ? 5   THR C CG2 1 
ATOM   4834 N N   . GLN C 3 6   ? -38.043 34.182 76.428  1.00 39.07  ? 6   GLN C N   1 
ATOM   4835 C CA  . GLN C 3 6   ? -36.928 35.064 76.737  1.00 38.90  ? 6   GLN C CA  1 
ATOM   4836 C C   . GLN C 3 6   ? -36.668 35.086 78.238  1.00 42.50  ? 6   GLN C C   1 
ATOM   4837 O O   . GLN C 3 6   ? -37.597 35.004 79.048  1.00 41.37  ? 6   GLN C O   1 
ATOM   4838 C CB  . GLN C 3 6   ? -37.200 36.480 76.223  1.00 36.14  ? 6   GLN C CB  1 
ATOM   4839 C CG  . GLN C 3 6   ? -36.755 36.682 74.779  1.00 37.68  ? 6   GLN C CG  1 
ATOM   4840 C CD  . GLN C 3 6   ? -37.037 38.073 74.264  1.00 37.01  ? 6   GLN C CD  1 
ATOM   4841 O OE1 . GLN C 3 6   ? -38.112 38.336 73.723  1.00 34.24  ? 6   GLN C OE1 1 
ATOM   4842 N NE2 . GLN C 3 6   ? -36.076 38.979 74.436  1.00 31.88  ? 6   GLN C NE2 1 
ATOM   4843 N N   . SER C 3 7   ? -35.388 35.205 78.600  1.00 42.01  ? 7   SER C N   1 
ATOM   4844 C CA  . SER C 3 7   ? -34.930 35.137 79.982  1.00 41.61  ? 7   SER C CA  1 
ATOM   4845 C C   . SER C 3 7   ? -33.725 36.043 80.171  1.00 41.85  ? 7   SER C C   1 
ATOM   4846 O O   . SER C 3 7   ? -32.908 36.169 79.247  1.00 41.71  ? 7   SER C O   1 
ATOM   4847 C CB  . SER C 3 7   ? -34.549 33.707 80.375  1.00 42.33  ? 7   SER C CB  1 
ATOM   4848 O OG  . SER C 3 7   ? -35.646 33.043 80.961  1.00 57.34  ? 7   SER C OG  1 
ATOM   4849 N N   . PRO C 3 8   ? -33.589 36.693 81.332  1.00 42.66  ? 8   PRO C N   1 
ATOM   4850 C CA  . PRO C 3 8   ? -34.572 36.804 82.418  1.00 41.21  ? 8   PRO C CA  1 
ATOM   4851 C C   . PRO C 3 8   ? -35.698 37.757 82.029  1.00 36.10  ? 8   PRO C C   1 
ATOM   4852 O O   . PRO C 3 8   ? -35.642 38.363 80.965  1.00 35.69  ? 8   PRO C O   1 
ATOM   4853 C CB  . PRO C 3 8   ? -33.731 37.338 83.591  1.00 40.00  ? 8   PRO C CB  1 
ATOM   4854 C CG  . PRO C 3 8   ? -32.617 38.095 82.930  1.00 38.58  ? 8   PRO C CG  1 
ATOM   4855 C CD  . PRO C 3 8   ? -32.291 37.280 81.710  1.00 36.99  ? 8   PRO C CD  1 
ATOM   4856 N N   . ALA C 3 9   ? -36.739 37.912 82.850  1.00 35.99  ? 9   ALA C N   1 
ATOM   4857 C CA  . ALA C 3 9   ? -37.790 38.866 82.514  1.00 37.18  ? 9   ALA C CA  1 
ATOM   4858 C C   . ALA C 3 9   ? -37.274 40.299 82.592  1.00 41.37  ? 9   ALA C C   1 
ATOM   4859 O O   . ALA C 3 9   ? -37.572 41.120 81.716  1.00 39.29  ? 9   ALA C O   1 
ATOM   4860 C CB  . ALA C 3 9   ? -38.998 38.674 83.429  1.00 24.44  ? 9   ALA C CB  1 
ATOM   4861 N N   . THR C 3 10  ? -36.499 40.615 83.629  1.00 42.29  ? 10  THR C N   1 
ATOM   4862 C CA  . THR C 3 10  ? -35.883 41.923 83.782  1.00 36.60  ? 10  THR C CA  1 
ATOM   4863 C C   . THR C 3 10  ? -34.408 41.745 84.100  1.00 43.06  ? 10  THR C C   1 
ATOM   4864 O O   . THR C 3 10  ? -34.004 40.760 84.721  1.00 46.46  ? 10  THR C O   1 
ATOM   4865 C CB  . THR C 3 10  ? -36.544 42.758 84.887  1.00 39.78  ? 10  THR C CB  1 
ATOM   4866 O OG1 . THR C 3 10  ? -36.409 42.079 86.138  1.00 54.34  ? 10  THR C OG1 1 
ATOM   4867 C CG2 . THR C 3 10  ? -38.018 42.967 84.594  1.00 42.03  ? 10  THR C CG2 1 
ATOM   4868 N N   . LEU C 3 11  ? -33.605 42.709 83.660  1.00 45.77  ? 11  LEU C N   1 
ATOM   4869 C CA  . LEU C 3 11  ? -32.162 42.688 83.853  1.00 43.14  ? 11  LEU C CA  1 
ATOM   4870 C C   . LEU C 3 11  ? -31.737 44.044 84.390  1.00 47.28  ? 11  LEU C C   1 
ATOM   4871 O O   . LEU C 3 11  ? -32.022 45.073 83.767  1.00 45.73  ? 11  LEU C O   1 
ATOM   4872 C CB  . LEU C 3 11  ? -31.437 42.378 82.539  1.00 40.70  ? 11  LEU C CB  1 
ATOM   4873 C CG  . LEU C 3 11  ? -30.039 41.769 82.639  1.00 52.10  ? 11  LEU C CG  1 
ATOM   4874 C CD1 . LEU C 3 11  ? -29.956 40.791 83.814  1.00 49.21  ? 11  LEU C CD1 1 
ATOM   4875 C CD2 . LEU C 3 11  ? -29.646 41.093 81.325  1.00 47.71  ? 11  LEU C CD2 1 
ATOM   4876 N N   . SER C 3 12  ? -31.052 44.048 85.534  1.00 44.13  ? 12  SER C N   1 
ATOM   4877 C CA  . SER C 3 12  ? -30.595 45.276 86.180  1.00 44.10  ? 12  SER C CA  1 
ATOM   4878 C C   . SER C 3 12  ? -29.075 45.241 86.265  1.00 46.24  ? 12  SER C C   1 
ATOM   4879 O O   . SER C 3 12  ? -28.508 44.415 86.987  1.00 43.88  ? 12  SER C O   1 
ATOM   4880 C CB  . SER C 3 12  ? -31.223 45.431 87.564  1.00 48.83  ? 12  SER C CB  1 
ATOM   4881 O OG  . SER C 3 12  ? -31.047 46.747 88.055  1.00 55.99  ? 12  SER C OG  1 
ATOM   4882 N N   . LEU C 3 13  ? -28.417 46.135 85.531  1.00 47.45  ? 13  LEU C N   1 
ATOM   4883 C CA  . LEU C 3 13  ? -26.965 46.150 85.452  1.00 44.09  ? 13  LEU C CA  1 
ATOM   4884 C C   . LEU C 3 13  ? -26.467 47.588 85.435  1.00 47.65  ? 13  LEU C C   1 
ATOM   4885 O O   . LEU C 3 13  ? -27.229 48.535 85.221  1.00 46.12  ? 13  LEU C O   1 
ATOM   4886 C CB  . LEU C 3 13  ? -26.464 45.396 84.216  1.00 42.25  ? 13  LEU C CB  1 
ATOM   4887 C CG  . LEU C 3 13  ? -26.619 43.878 84.252  1.00 44.36  ? 13  LEU C CG  1 
ATOM   4888 C CD1 . LEU C 3 13  ? -26.116 43.255 82.960  1.00 41.55  ? 13  LEU C CD1 1 
ATOM   4889 C CD2 . LEU C 3 13  ? -25.886 43.306 85.455  1.00 34.61  ? 13  LEU C CD2 1 
ATOM   4890 N N   . SER C 3 14  ? -25.169 47.739 85.665  1.00 43.88  ? 14  SER C N   1 
ATOM   4891 C CA  . SER C 3 14  ? -24.495 49.023 85.698  1.00 45.92  ? 14  SER C CA  1 
ATOM   4892 C C   . SER C 3 14  ? -23.849 49.328 84.352  1.00 43.53  ? 14  SER C C   1 
ATOM   4893 O O   . SER C 3 14  ? -23.419 48.414 83.642  1.00 39.23  ? 14  SER C O   1 
ATOM   4894 C CB  . SER C 3 14  ? -23.424 49.041 86.794  1.00 45.56  ? 14  SER C CB  1 
ATOM   4895 O OG  . SER C 3 14  ? -24.010 49.031 88.084  1.00 51.96  ? 14  SER C OG  1 
ATOM   4896 N N   . PRO C 3 15  ? -23.780 50.604 83.978  1.00 42.36  ? 15  PRO C N   1 
ATOM   4897 C CA  . PRO C 3 15  ? -23.091 50.973 82.736  1.00 44.33  ? 15  PRO C CA  1 
ATOM   4898 C C   . PRO C 3 15  ? -21.679 50.404 82.687  1.00 42.20  ? 15  PRO C C   1 
ATOM   4899 O O   . PRO C 3 15  ? -20.967 50.363 83.693  1.00 43.05  ? 15  PRO C O   1 
ATOM   4900 C CB  . PRO C 3 15  ? -23.082 52.505 82.778  1.00 44.03  ? 15  PRO C CB  1 
ATOM   4901 C CG  . PRO C 3 15  ? -24.258 52.864 83.631  1.00 42.53  ? 15  PRO C CG  1 
ATOM   4902 C CD  . PRO C 3 15  ? -24.394 51.764 84.647  1.00 39.36  ? 15  PRO C CD  1 
ATOM   4903 N N   . GLY C 3 16  ? -21.284 49.947 81.501  1.00 43.25  ? 16  GLY C N   1 
ATOM   4904 C CA  . GLY C 3 16  ? -19.994 49.327 81.302  1.00 36.72  ? 16  GLY C CA  1 
ATOM   4905 C C   . GLY C 3 16  ? -19.975 47.828 81.497  1.00 41.65  ? 16  GLY C C   1 
ATOM   4906 O O   . GLY C 3 16  ? -19.000 47.178 81.097  1.00 43.84  ? 16  GLY C O   1 
ATOM   4907 N N   . GLU C 3 17  ? -21.017 47.255 82.083  1.00 42.14  ? 17  GLU C N   1 
ATOM   4908 C CA  . GLU C 3 17  ? -21.051 45.823 82.329  1.00 43.37  ? 17  GLU C CA  1 
ATOM   4909 C C   . GLU C 3 17  ? -21.571 45.074 81.106  1.00 40.27  ? 17  GLU C C   1 
ATOM   4910 O O   . GLU C 3 17  ? -22.198 45.645 80.211  1.00 41.92  ? 17  GLU C O   1 
ATOM   4911 C CB  . GLU C 3 17  ? -21.911 45.511 83.552  1.00 39.50  ? 17  GLU C CB  1 
ATOM   4912 C CG  . GLU C 3 17  ? -21.210 45.816 84.864  1.00 43.46  ? 17  GLU C CG  1 
ATOM   4913 C CD  . GLU C 3 17  ? -22.122 45.681 86.070  1.00 54.90  ? 17  GLU C CD  1 
ATOM   4914 O OE1 . GLU C 3 17  ? -23.321 45.377 85.890  1.00 55.73  ? 17  GLU C OE1 1 
ATOM   4915 O OE2 . GLU C 3 17  ? -21.633 45.883 87.202  1.00 66.30  ? 17  GLU C OE2 1 
ATOM   4916 N N   . ARG C 3 18  ? -21.288 43.777 81.077  1.00 33.73  ? 18  ARG C N   1 
ATOM   4917 C CA  . ARG C 3 18  ? -21.676 42.916 79.971  1.00 38.57  ? 18  ARG C CA  1 
ATOM   4918 C C   . ARG C 3 18  ? -23.046 42.315 80.268  1.00 40.51  ? 18  ARG C C   1 
ATOM   4919 O O   . ARG C 3 18  ? -23.242 41.691 81.315  1.00 48.35  ? 18  ARG C O   1 
ATOM   4920 C CB  . ARG C 3 18  ? -20.622 41.831 79.760  1.00 36.17  ? 18  ARG C CB  1 
ATOM   4921 C CG  . ARG C 3 18  ? -20.885 40.865 78.616  1.00 44.08  ? 18  ARG C CG  1 
ATOM   4922 C CD  . ARG C 3 18  ? -19.932 39.685 78.714  1.00 44.42  ? 18  ARG C CD  1 
ATOM   4923 N NE  . ARG C 3 18  ? -19.918 38.857 77.514  1.00 55.87  ? 18  ARG C NE  1 
ATOM   4924 C CZ  . ARG C 3 18  ? -19.327 39.190 76.374  1.00 56.64  ? 18  ARG C CZ  1 
ATOM   4925 N NH1 . ARG C 3 18  ? -18.705 40.350 76.228  1.00 52.80  ? 18  ARG C NH1 1 
ATOM   4926 N NH2 . ARG C 3 18  ? -19.361 38.337 75.352  1.00 54.98  ? 18  ARG C NH2 1 
ATOM   4927 N N   . ALA C 3 19  ? -23.994 42.520 79.359  1.00 42.74  ? 19  ALA C N   1 
ATOM   4928 C CA  . ALA C 3 19  ? -25.349 42.006 79.502  1.00 40.49  ? 19  ALA C CA  1 
ATOM   4929 C C   . ALA C 3 19  ? -25.569 40.883 78.501  1.00 40.13  ? 19  ALA C C   1 
ATOM   4930 O O   . ALA C 3 19  ? -25.300 41.050 77.307  1.00 38.49  ? 19  ALA C O   1 
ATOM   4931 C CB  . ALA C 3 19  ? -26.384 43.114 79.292  1.00 40.36  ? 19  ALA C CB  1 
ATOM   4932 N N   . THR C 3 20  ? -26.047 39.742 78.987  1.00 39.38  ? 20  THR C N   1 
ATOM   4933 C CA  . THR C 3 20  ? -26.358 38.598 78.140  1.00 39.83  ? 20  THR C CA  1 
ATOM   4934 C C   . THR C 3 20  ? -27.833 38.275 78.307  1.00 40.86  ? 20  THR C C   1 
ATOM   4935 O O   . THR C 3 20  ? -28.291 38.014 79.424  1.00 42.33  ? 20  THR C O   1 
ATOM   4936 C CB  . THR C 3 20  ? -25.492 37.386 78.490  1.00 41.33  ? 20  THR C CB  1 
ATOM   4937 O OG1 . THR C 3 20  ? -24.120 37.686 78.209  1.00 48.86  ? 20  THR C OG1 1 
ATOM   4938 C CG2 . THR C 3 20  ? -25.908 36.180 77.665  1.00 38.80  ? 20  THR C CG2 1 
ATOM   4939 N N   . LEU C 3 21  ? -28.574 38.317 77.205  1.00 37.12  ? 21  LEU C N   1 
ATOM   4940 C CA  . LEU C 3 21  ? -30.007 38.070 77.197  1.00 33.70  ? 21  LEU C CA  1 
ATOM   4941 C C   . LEU C 3 21  ? -30.259 36.758 76.478  1.00 37.60  ? 21  LEU C C   1 
ATOM   4942 O O   . LEU C 3 21  ? -29.625 36.476 75.457  1.00 34.70  ? 21  LEU C O   1 
ATOM   4943 C CB  . LEU C 3 21  ? -30.765 39.203 76.499  1.00 35.56  ? 21  LEU C CB  1 
ATOM   4944 C CG  . LEU C 3 21  ? -30.888 40.553 77.211  1.00 37.53  ? 21  LEU C CG  1 
ATOM   4945 C CD1 . LEU C 3 21  ? -29.545 41.264 77.349  1.00 35.06  ? 21  LEU C CD1 1 
ATOM   4946 C CD2 . LEU C 3 21  ? -31.873 41.426 76.463  1.00 37.08  ? 21  LEU C CD2 1 
ATOM   4947 N N   . SER C 3 22  ? -31.170 35.951 77.013  1.00 37.84  ? 22  SER C N   1 
ATOM   4948 C CA  . SER C 3 22  ? -31.409 34.611 76.500  1.00 36.33  ? 22  SER C CA  1 
ATOM   4949 C C   . SER C 3 22  ? -32.733 34.542 75.753  1.00 39.40  ? 22  SER C C   1 
ATOM   4950 O O   . SER C 3 22  ? -33.717 35.181 76.140  1.00 34.95  ? 22  SER C O   1 
ATOM   4951 C CB  . SER C 3 22  ? -31.390 33.581 77.628  1.00 31.37  ? 22  SER C CB  1 
ATOM   4952 O OG  . SER C 3 22  ? -30.113 33.559 78.241  1.00 59.20  ? 22  SER C OG  1 
ATOM   4953 N N   . CYS C 3 23  ? -32.737 33.767 74.675  1.00 33.26  ? 23  CYS C N   1 
ATOM   4954 C CA  . CYS C 3 23  ? -33.934 33.503 73.893  1.00 38.61  ? 23  CYS C CA  1 
ATOM   4955 C C   . CYS C 3 23  ? -33.890 32.039 73.499  1.00 37.33  ? 23  CYS C C   1 
ATOM   4956 O O   . CYS C 3 23  ? -32.931 31.601 72.858  1.00 37.54  ? 23  CYS C O   1 
ATOM   4957 C CB  . CYS C 3 23  ? -33.998 34.407 72.655  1.00 36.67  ? 23  CYS C CB  1 
ATOM   4958 S SG  . CYS C 3 23  ? -35.258 33.984 71.430  1.00 40.41  ? 23  CYS C SG  1 
ATOM   4959 N N   . ARG C 3 24  ? -34.905 31.282 73.897  1.00 37.42  ? 24  ARG C N   1 
ATOM   4960 C CA  . ARG C 3 24  ? -34.983 29.868 73.569  1.00 40.48  ? 24  ARG C CA  1 
ATOM   4961 C C   . ARG C 3 24  ? -36.188 29.605 72.682  1.00 37.71  ? 24  ARG C C   1 
ATOM   4962 O O   . ARG C 3 24  ? -37.251 30.206 72.860  1.00 35.91  ? 24  ARG C O   1 
ATOM   4963 C CB  . ARG C 3 24  ? -35.054 29.006 74.831  1.00 41.33  ? 24  ARG C CB  1 
ATOM   4964 C CG  . ARG C 3 24  ? -33.903 29.240 75.788  1.00 46.57  ? 24  ARG C CG  1 
ATOM   4965 C CD  . ARG C 3 24  ? -32.902 28.096 75.737  1.00 54.80  ? 24  ARG C CD  1 
ATOM   4966 N NE  . ARG C 3 24  ? -33.297 26.990 76.602  1.00 62.32  ? 24  ARG C NE  1 
ATOM   4967 C CZ  . ARG C 3 24  ? -33.541 25.756 76.179  1.00 63.83  ? 24  ARG C CZ  1 
ATOM   4968 N NH1 . ARG C 3 24  ? -33.417 25.425 74.903  1.00 57.42  ? 24  ARG C NH1 1 
ATOM   4969 N NH2 . ARG C 3 24  ? -33.916 24.832 77.059  1.00 66.48  ? 24  ARG C NH2 1 
ATOM   4970 N N   . ALA C 3 25  ? -36.009 28.717 71.717  1.00 36.88  ? 25  ALA C N   1 
ATOM   4971 C CA  . ALA C 3 25  ? -37.087 28.288 70.843  1.00 40.82  ? 25  ALA C CA  1 
ATOM   4972 C C   . ALA C 3 25  ? -37.652 26.968 71.342  1.00 43.70  ? 25  ALA C C   1 
ATOM   4973 O O   . ALA C 3 25  ? -36.902 26.074 71.742  1.00 38.43  ? 25  ALA C O   1 
ATOM   4974 C CB  . ALA C 3 25  ? -36.588 28.132 69.408  1.00 36.47  ? 25  ALA C CB  1 
ATOM   4975 N N   . SER C 3 26  ? -38.980 26.842 71.310  1.00 42.78  ? 26  SER C N   1 
ATOM   4976 C CA  . SER C 3 26  ? -39.615 25.578 71.672  1.00 45.76  ? 26  SER C CA  1 
ATOM   4977 C C   . SER C 3 26  ? -39.234 24.443 70.731  1.00 41.63  ? 26  SER C C   1 
ATOM   4978 O O   . SER C 3 26  ? -39.600 23.291 70.992  1.00 45.97  ? 26  SER C O   1 
ATOM   4979 C CB  . SER C 3 26  ? -41.137 25.744 71.678  1.00 42.83  ? 26  SER C CB  1 
ATOM   4980 O OG  . SER C 3 26  ? -41.628 25.943 70.359  1.00 45.34  ? 26  SER C OG  1 
ATOM   4981 N N   . GLN C 3 27  ? -38.492 24.747 69.669  1.00 40.94  ? 27  GLN C N   1 
ATOM   4982 C CA  . GLN C 3 27  ? -38.329 23.871 68.521  1.00 43.69  ? 27  GLN C CA  1 
ATOM   4983 C C   . GLN C 3 27  ? -37.184 24.419 67.675  1.00 45.28  ? 27  GLN C C   1 
ATOM   4984 O O   . GLN C 3 27  ? -37.018 25.636 67.582  1.00 40.42  ? 27  GLN C O   1 
ATOM   4985 C CB  . GLN C 3 27  ? -39.649 23.817 67.739  1.00 42.01  ? 27  GLN C CB  1 
ATOM   4986 C CG  . GLN C 3 27  ? -39.810 22.773 66.664  1.00 49.42  ? 27  GLN C CG  1 
ATOM   4987 C CD  . GLN C 3 27  ? -41.276 22.636 66.268  1.00 55.47  ? 27  GLN C CD  1 
ATOM   4988 O OE1 . GLN C 3 27  ? -42.161 23.188 66.930  1.00 51.98  ? 27  GLN C OE1 1 
ATOM   4989 N NE2 . GLN C 3 27  ? -41.538 21.904 65.194  1.00 54.22  ? 27  GLN C NE2 1 
ATOM   4990 N N   . SER C 3 28  ? -36.387 23.526 67.087  1.00 40.59  ? 28  SER C N   1 
ATOM   4991 C CA  . SER C 3 28  ? -35.160 23.946 66.412  1.00 38.60  ? 28  SER C CA  1 
ATOM   4992 C C   . SER C 3 28  ? -35.461 24.822 65.196  1.00 37.74  ? 28  SER C C   1 
ATOM   4993 O O   . SER C 3 28  ? -36.261 24.450 64.335  1.00 42.29  ? 28  SER C O   1 
ATOM   4994 C CB  . SER C 3 28  ? -34.347 22.719 65.993  1.00 37.58  ? 28  SER C CB  1 
ATOM   4995 O OG  . SER C 3 28  ? -33.103 23.103 65.429  1.00 50.42  ? 28  SER C OG  1 
ATOM   4996 N N   . ILE C 3 29  ? -34.810 25.990 65.119  1.00 33.63  ? 29  ILE C N   1 
ATOM   4997 C CA  . ILE C 3 29  ? -35.116 26.963 64.067  1.00 33.06  ? 29  ILE C CA  1 
ATOM   4998 C C   . ILE C 3 29  ? -33.863 27.419 63.324  1.00 38.36  ? 29  ILE C C   1 
ATOM   4999 O O   . ILE C 3 29  ? -33.844 28.513 62.743  1.00 34.20  ? 29  ILE C O   1 
ATOM   5000 C CB  . ILE C 3 29  ? -35.856 28.186 64.641  1.00 35.76  ? 29  ILE C CB  1 
ATOM   5001 C CG1 . ILE C 3 29  ? -35.016 28.848 65.736  1.00 39.54  ? 29  ILE C CG1 1 
ATOM   5002 C CG2 . ILE C 3 29  ? -37.254 27.800 65.147  1.00 31.30  ? 29  ILE C CG2 1 
ATOM   5003 C CD1 . ILE C 3 29  ? -35.466 30.240 66.105  1.00 29.69  ? 29  ILE C CD1 1 
ATOM   5004 N N   . SER C 3 30  ? -32.818 26.587 63.324  1.00 37.93  ? 30  SER C N   1 
ATOM   5005 C CA  . SER C 3 30  ? -31.556 26.938 62.678  1.00 36.71  ? 30  SER C CA  1 
ATOM   5006 C C   . SER C 3 30  ? -31.044 28.290 63.166  1.00 35.88  ? 30  SER C C   1 
ATOM   5007 O O   . SER C 3 30  ? -30.699 28.446 64.343  1.00 40.28  ? 30  SER C O   1 
ATOM   5008 C CB  . SER C 3 30  ? -31.715 26.962 61.155  1.00 38.37  ? 30  SER C CB  1 
ATOM   5009 O OG  . SER C 3 30  ? -31.623 25.667 60.603  1.00 40.55  ? 30  SER C OG  1 
ATOM   5010 N N   . LYS C 3 31  ? -31.005 29.279 62.266  1.00 34.32  ? 31  LYS C N   1 
ATOM   5011 C CA  . LYS C 3 31  ? -30.555 30.623 62.611  1.00 34.15  ? 31  LYS C CA  1 
ATOM   5012 C C   . LYS C 3 31  ? -31.519 31.699 62.114  1.00 34.64  ? 31  LYS C C   1 
ATOM   5013 O O   . LYS C 3 31  ? -31.117 32.856 61.961  1.00 35.27  ? 31  LYS C O   1 
ATOM   5014 C CB  . LYS C 3 31  ? -29.152 30.884 62.058  1.00 34.72  ? 31  LYS C CB  1 
ATOM   5015 C CG  . LYS C 3 31  ? -28.008 30.565 63.019  1.00 39.37  ? 31  LYS C CG  1 
ATOM   5016 C CD  . LYS C 3 31  ? -26.750 30.162 62.264  1.00 35.22  ? 31  LYS C CD  1 
ATOM   5017 C CE  . LYS C 3 31  ? -25.891 31.379 61.965  1.00 46.36  ? 31  LYS C CE  1 
ATOM   5018 N NZ  . LYS C 3 31  ? -25.027 31.787 63.120  1.00 50.87  ? 31  LYS C NZ  1 
ATOM   5019 N N   . THR C 3 32  ? -32.783 31.349 61.866  1.00 34.62  ? 32  THR C N   1 
ATOM   5020 C CA  . THR C 3 32  ? -33.775 32.306 61.370  1.00 35.82  ? 32  THR C CA  1 
ATOM   5021 C C   . THR C 3 32  ? -34.379 33.044 62.563  1.00 34.74  ? 32  THR C C   1 
ATOM   5022 O O   . THR C 3 32  ? -35.510 32.800 62.989  1.00 31.78  ? 32  THR C O   1 
ATOM   5023 C CB  . THR C 3 32  ? -34.843 31.596 60.546  1.00 35.17  ? 32  THR C CB  1 
ATOM   5024 O OG1 . THR C 3 32  ? -35.538 30.657 61.377  1.00 33.59  ? 32  THR C OG1 1 
ATOM   5025 C CG2 . THR C 3 32  ? -34.206 30.874 59.361  1.00 30.22  ? 32  THR C CG2 1 
ATOM   5026 N N   . LEU C 3 33  ? -33.599 33.983 63.094  1.00 32.10  ? 33  LEU C N   1 
ATOM   5027 C CA  . LEU C 3 33  ? -33.885 34.632 64.367  1.00 27.91  ? 33  LEU C CA  1 
ATOM   5028 C C   . LEU C 3 33  ? -33.443 36.084 64.268  1.00 33.66  ? 33  LEU C C   1 
ATOM   5029 O O   . LEU C 3 33  ? -32.358 36.365 63.749  1.00 34.23  ? 33  LEU C O   1 
ATOM   5030 C CB  . LEU C 3 33  ? -33.151 33.905 65.508  1.00 30.78  ? 33  LEU C CB  1 
ATOM   5031 C CG  . LEU C 3 33  ? -33.447 34.092 67.006  1.00 36.78  ? 33  LEU C CG  1 
ATOM   5032 C CD1 . LEU C 3 33  ? -32.700 35.303 67.571  1.00 30.72  ? 33  LEU C CD1 1 
ATOM   5033 C CD2 . LEU C 3 33  ? -34.935 34.179 67.299  1.00 34.21  ? 33  LEU C CD2 1 
ATOM   5034 N N   . ALA C 3 34  ? -34.282 37.004 64.742  1.00 30.79  ? 34  ALA C N   1 
ATOM   5035 C CA  . ALA C 3 34  ? -33.940 38.419 64.769  1.00 30.72  ? 34  ALA C CA  1 
ATOM   5036 C C   . ALA C 3 34  ? -34.061 38.961 66.188  1.00 32.43  ? 34  ALA C C   1 
ATOM   5037 O O   . ALA C 3 34  ? -34.761 38.394 67.032  1.00 32.41  ? 34  ALA C O   1 
ATOM   5038 C CB  . ALA C 3 34  ? -34.826 39.232 63.813  1.00 30.39  ? 34  ALA C CB  1 
ATOM   5039 N N   . TRP C 3 35  ? -33.352 40.064 66.448  1.00 29.72  ? 35  TRP C N   1 
ATOM   5040 C CA  . TRP C 3 35  ? -33.388 40.750 67.734  1.00 27.97  ? 35  TRP C CA  1 
ATOM   5041 C C   . TRP C 3 35  ? -33.797 42.202 67.527  1.00 34.67  ? 35  TRP C C   1 
ATOM   5042 O O   . TRP C 3 35  ? -33.411 42.833 66.537  1.00 33.49  ? 35  TRP C O   1 
ATOM   5043 C CB  . TRP C 3 35  ? -32.029 40.705 68.449  1.00 29.29  ? 35  TRP C CB  1 
ATOM   5044 C CG  . TRP C 3 35  ? -31.668 39.383 69.080  1.00 31.68  ? 35  TRP C CG  1 
ATOM   5045 C CD1 . TRP C 3 35  ? -30.909 38.388 68.525  1.00 29.07  ? 35  TRP C CD1 1 
ATOM   5046 C CD2 . TRP C 3 35  ? -32.024 38.929 70.394  1.00 29.88  ? 35  TRP C CD2 1 
ATOM   5047 N NE1 . TRP C 3 35  ? -30.776 37.346 69.409  1.00 35.17  ? 35  TRP C NE1 1 
ATOM   5048 C CE2 . TRP C 3 35  ? -31.455 37.648 70.561  1.00 30.94  ? 35  TRP C CE2 1 
ATOM   5049 C CE3 . TRP C 3 35  ? -32.774 39.477 71.443  1.00 35.35  ? 35  TRP C CE3 1 
ATOM   5050 C CZ2 . TRP C 3 35  ? -31.611 36.905 71.735  1.00 32.95  ? 35  TRP C CZ2 1 
ATOM   5051 C CZ3 . TRP C 3 35  ? -32.928 38.739 72.614  1.00 32.84  ? 35  TRP C CZ3 1 
ATOM   5052 C CH2 . TRP C 3 35  ? -32.347 37.466 72.748  1.00 37.11  ? 35  TRP C CH2 1 
ATOM   5053 N N   . TYR C 3 36  ? -34.562 42.733 68.479  1.00 31.28  ? 36  TYR C N   1 
ATOM   5054 C CA  . TYR C 3 36  ? -35.073 44.092 68.403  1.00 31.61  ? 36  TYR C CA  1 
ATOM   5055 C C   . TYR C 3 36  ? -34.910 44.771 69.754  1.00 35.59  ? 36  TYR C C   1 
ATOM   5056 O O   . TYR C 3 36  ? -34.895 44.115 70.800  1.00 31.84  ? 36  TYR C O   1 
ATOM   5057 C CB  . TYR C 3 36  ? -36.555 44.125 67.989  1.00 33.66  ? 36  TYR C CB  1 
ATOM   5058 C CG  . TYR C 3 36  ? -36.838 43.461 66.658  1.00 33.45  ? 36  TYR C CG  1 
ATOM   5059 C CD1 . TYR C 3 36  ? -37.043 42.085 66.572  1.00 28.92  ? 36  TYR C CD1 1 
ATOM   5060 C CD2 . TYR C 3 36  ? -36.910 44.211 65.487  1.00 30.74  ? 36  TYR C CD2 1 
ATOM   5061 C CE1 . TYR C 3 36  ? -37.300 41.475 65.353  1.00 31.32  ? 36  TYR C CE1 1 
ATOM   5062 C CE2 . TYR C 3 36  ? -37.171 43.611 64.263  1.00 30.39  ? 36  TYR C CE2 1 
ATOM   5063 C CZ  . TYR C 3 36  ? -37.366 42.246 64.201  1.00 33.67  ? 36  TYR C CZ  1 
ATOM   5064 O OH  . TYR C 3 36  ? -37.622 41.647 62.985  1.00 33.11  ? 36  TYR C OH  1 
ATOM   5065 N N   . GLN C 3 37  ? -34.795 46.096 69.716  1.00 34.53  ? 37  GLN C N   1 
ATOM   5066 C CA  . GLN C 3 37  ? -34.725 46.937 70.902  1.00 33.49  ? 37  GLN C CA  1 
ATOM   5067 C C   . GLN C 3 37  ? -35.885 47.916 70.851  1.00 37.34  ? 37  GLN C C   1 
ATOM   5068 O O   . GLN C 3 37  ? -36.013 48.669 69.880  1.00 39.38  ? 37  GLN C O   1 
ATOM   5069 C CB  . GLN C 3 37  ? -33.396 47.692 70.962  1.00 37.53  ? 37  GLN C CB  1 
ATOM   5070 C CG  . GLN C 3 37  ? -33.361 48.832 71.977  1.00 36.87  ? 37  GLN C CG  1 
ATOM   5071 C CD  . GLN C 3 37  ? -32.234 49.820 71.706  1.00 39.82  ? 37  GLN C CD  1 
ATOM   5072 O OE1 . GLN C 3 37  ? -32.318 50.631 70.784  1.00 40.00  ? 37  GLN C OE1 1 
ATOM   5073 N NE2 . GLN C 3 37  ? -31.172 49.749 72.503  1.00 36.57  ? 37  GLN C NE2 1 
ATOM   5074 N N   . GLN C 3 38  ? -36.726 47.911 71.886  1.00 36.60  ? 38  GLN C N   1 
ATOM   5075 C CA  . GLN C 3 38  ? -37.864 48.821 71.960  1.00 37.09  ? 38  GLN C CA  1 
ATOM   5076 C C   . GLN C 3 38  ? -37.708 49.740 73.160  1.00 38.97  ? 38  GLN C C   1 
ATOM   5077 O O   . GLN C 3 38  ? -37.732 49.281 74.307  1.00 42.47  ? 38  GLN C O   1 
ATOM   5078 C CB  . GLN C 3 38  ? -39.197 48.072 72.043  1.00 39.10  ? 38  GLN C CB  1 
ATOM   5079 C CG  . GLN C 3 38  ? -40.381 49.032 71.895  1.00 39.83  ? 38  GLN C CG  1 
ATOM   5080 C CD  . GLN C 3 38  ? -41.736 48.349 71.875  1.00 41.36  ? 38  GLN C CD  1 
ATOM   5081 O OE1 . GLN C 3 38  ? -42.652 48.805 71.186  1.00 36.39  ? 38  GLN C OE1 1 
ATOM   5082 N NE2 . GLN C 3 38  ? -41.879 47.271 72.643  1.00 36.46  ? 38  GLN C NE2 1 
ATOM   5083 N N   . LYS C 3 39  ? -37.557 51.032 72.892  1.00 43.50  ? 39  LYS C N   1 
ATOM   5084 C CA  . LYS C 3 39  ? -37.534 52.061 73.917  1.00 44.06  ? 39  LYS C CA  1 
ATOM   5085 C C   . LYS C 3 39  ? -38.951 52.535 74.215  1.00 45.15  ? 39  LYS C C   1 
ATOM   5086 O O   . LYS C 3 39  ? -39.858 52.363 73.394  1.00 45.61  ? 39  LYS C O   1 
ATOM   5087 C CB  . LYS C 3 39  ? -36.651 53.224 73.468  1.00 36.84  ? 39  LYS C CB  1 
ATOM   5088 C CG  . LYS C 3 39  ? -35.208 53.080 73.924  1.00 41.25  ? 39  LYS C CG  1 
ATOM   5089 C CD  . LYS C 3 39  ? -34.217 53.491 72.853  1.00 39.96  ? 39  LYS C CD  1 
ATOM   5090 C CE  . LYS C 3 39  ? -32.826 52.941 73.155  1.00 40.87  ? 39  LYS C CE  1 
ATOM   5091 N NZ  . LYS C 3 39  ? -31.748 53.957 72.957  1.00 48.09  ? 39  LYS C NZ  1 
ATOM   5092 N N   . PRO C 3 40  ? -39.183 53.116 75.395  1.00 47.63  ? 40  PRO C N   1 
ATOM   5093 C CA  . PRO C 3 40  ? -40.552 53.498 75.769  1.00 46.52  ? 40  PRO C CA  1 
ATOM   5094 C C   . PRO C 3 40  ? -41.184 54.448 74.760  1.00 45.59  ? 40  PRO C C   1 
ATOM   5095 O O   . PRO C 3 40  ? -40.557 55.404 74.297  1.00 47.20  ? 40  PRO C O   1 
ATOM   5096 C CB  . PRO C 3 40  ? -40.370 54.171 77.135  1.00 48.94  ? 40  PRO C CB  1 
ATOM   5097 C CG  . PRO C 3 40  ? -39.100 53.616 77.665  1.00 50.61  ? 40  PRO C CG  1 
ATOM   5098 C CD  . PRO C 3 40  ? -38.219 53.399 76.474  1.00 44.17  ? 40  PRO C CD  1 
ATOM   5099 N N   . GLY C 3 41  ? -42.442 54.168 74.418  1.00 42.73  ? 41  GLY C N   1 
ATOM   5100 C CA  . GLY C 3 41  ? -43.196 54.983 73.488  1.00 42.80  ? 41  GLY C CA  1 
ATOM   5101 C C   . GLY C 3 41  ? -42.720 54.946 72.053  1.00 53.58  ? 41  GLY C C   1 
ATOM   5102 O O   . GLY C 3 41  ? -43.289 55.653 71.213  1.00 51.91  ? 41  GLY C O   1 
ATOM   5103 N N   . GLN C 3 42  ? -41.706 54.145 71.737  1.00 48.94  ? 42  GLN C N   1 
ATOM   5104 C CA  . GLN C 3 42  ? -41.141 54.079 70.400  1.00 44.69  ? 42  GLN C CA  1 
ATOM   5105 C C   . GLN C 3 42  ? -41.360 52.696 69.801  1.00 42.64  ? 42  GLN C C   1 
ATOM   5106 O O   . GLN C 3 42  ? -41.593 51.715 70.511  1.00 45.25  ? 42  GLN C O   1 
ATOM   5107 C CB  . GLN C 3 42  ? -39.645 54.403 70.422  1.00 45.53  ? 42  GLN C CB  1 
ATOM   5108 C CG  . GLN C 3 42  ? -39.330 55.881 70.574  1.00 50.82  ? 42  GLN C CG  1 
ATOM   5109 C CD  . GLN C 3 42  ? -37.837 56.159 70.543  1.00 54.42  ? 42  GLN C CD  1 
ATOM   5110 O OE1 . GLN C 3 42  ? -37.052 55.347 70.047  1.00 55.66  ? 42  GLN C OE1 1 
ATOM   5111 N NE2 . GLN C 3 42  ? -37.438 57.309 71.077  1.00 56.53  ? 42  GLN C NE2 1 
ATOM   5112 N N   . ALA C 3 43  ? -41.278 52.628 68.476  1.00 42.29  ? 43  ALA C N   1 
ATOM   5113 C CA  . ALA C 3 43  ? -41.379 51.354 67.790  1.00 39.03  ? 43  ALA C CA  1 
ATOM   5114 C C   . ALA C 3 43  ? -40.117 50.530 68.026  1.00 40.21  ? 43  ALA C C   1 
ATOM   5115 O O   . ALA C 3 43  ? -39.065 51.075 68.367  1.00 41.37  ? 43  ALA C O   1 
ATOM   5116 C CB  . ALA C 3 43  ? -41.588 51.570 66.295  1.00 32.72  ? 43  ALA C CB  1 
ATOM   5117 N N   . PRO C 3 44  ? -40.198 49.209 67.867  1.00 38.28  ? 44  PRO C N   1 
ATOM   5118 C CA  . PRO C 3 44  ? -38.982 48.390 67.911  1.00 36.89  ? 44  PRO C CA  1 
ATOM   5119 C C   . PRO C 3 44  ? -37.996 48.791 66.822  1.00 40.18  ? 44  PRO C C   1 
ATOM   5120 O O   . PRO C 3 44  ? -38.354 49.362 65.788  1.00 35.44  ? 44  PRO C O   1 
ATOM   5121 C CB  . PRO C 3 44  ? -39.500 46.963 67.694  1.00 34.57  ? 44  PRO C CB  1 
ATOM   5122 C CG  . PRO C 3 44  ? -40.915 47.004 68.164  1.00 40.57  ? 44  PRO C CG  1 
ATOM   5123 C CD  . PRO C 3 44  ? -41.421 48.387 67.836  1.00 38.36  ? 44  PRO C CD  1 
ATOM   5124 N N   . ARG C 3 45  ? -36.728 48.483 67.074  1.00 37.16  ? 45  ARG C N   1 
ATOM   5125 C CA  . ARG C 3 45  ? -35.643 48.778 66.152  1.00 37.22  ? 45  ARG C CA  1 
ATOM   5126 C C   . ARG C 3 45  ? -34.820 47.516 65.944  1.00 35.10  ? 45  ARG C C   1 
ATOM   5127 O O   . ARG C 3 45  ? -34.426 46.862 66.915  1.00 32.93  ? 45  ARG C O   1 
ATOM   5128 C CB  . ARG C 3 45  ? -34.765 49.910 66.686  1.00 34.49  ? 45  ARG C CB  1 
ATOM   5129 C CG  . ARG C 3 45  ? -33.370 49.931 66.104  1.00 45.60  ? 45  ARG C CG  1 
ATOM   5130 C CD  . ARG C 3 45  ? -32.941 51.346 65.769  1.00 55.98  ? 45  ARG C CD  1 
ATOM   5131 N NE  . ARG C 3 45  ? -31.514 51.549 65.991  1.00 59.21  ? 45  ARG C NE  1 
ATOM   5132 C CZ  . ARG C 3 45  ? -30.566 51.184 65.140  1.00 60.58  ? 45  ARG C CZ  1 
ATOM   5133 N NH1 . ARG C 3 45  ? -30.857 50.579 63.997  1.00 60.40  ? 45  ARG C NH1 1 
ATOM   5134 N NH2 . ARG C 3 45  ? -29.293 51.439 65.438  1.00 52.82  ? 45  ARG C NH2 1 
ATOM   5135 N N   . LEU C 3 46  ? -34.570 47.176 64.681  1.00 31.45  ? 46  LEU C N   1 
ATOM   5136 C CA  . LEU C 3 46  ? -33.832 45.965 64.352  1.00 31.16  ? 46  LEU C CA  1 
ATOM   5137 C C   . LEU C 3 46  ? -32.385 46.073 64.820  1.00 34.38  ? 46  LEU C C   1 
ATOM   5138 O O   . LEU C 3 46  ? -31.701 47.059 64.531  1.00 37.06  ? 46  LEU C O   1 
ATOM   5139 C CB  . LEU C 3 46  ? -33.880 45.720 62.845  1.00 30.52  ? 46  LEU C CB  1 
ATOM   5140 C CG  . LEU C 3 46  ? -33.013 44.585 62.303  1.00 30.31  ? 46  LEU C CG  1 
ATOM   5141 C CD1 . LEU C 3 46  ? -33.558 43.232 62.737  1.00 28.61  ? 46  LEU C CD1 1 
ATOM   5142 C CD2 . LEU C 3 46  ? -32.923 44.671 60.787  1.00 31.04  ? 46  LEU C CD2 1 
ATOM   5143 N N   . LEU C 3 47  ? -31.920 45.056 65.545  1.00 34.06  ? 47  LEU C N   1 
ATOM   5144 C CA  . LEU C 3 47  ? -30.524 44.944 65.958  1.00 35.66  ? 47  LEU C CA  1 
ATOM   5145 C C   . LEU C 3 47  ? -29.764 43.890 65.165  1.00 38.59  ? 47  LEU C C   1 
ATOM   5146 O O   . LEU C 3 47  ? -28.684 44.158 64.626  1.00 34.44  ? 47  LEU C O   1 
ATOM   5147 C CB  . LEU C 3 47  ? -30.442 44.597 67.450  1.00 30.82  ? 47  LEU C CB  1 
ATOM   5148 C CG  . LEU C 3 47  ? -31.119 45.550 68.427  1.00 35.96  ? 47  LEU C CG  1 
ATOM   5149 C CD1 . LEU C 3 47  ? -30.695 45.220 69.853  1.00 31.99  ? 47  LEU C CD1 1 
ATOM   5150 C CD2 . LEU C 3 47  ? -30.774 46.982 68.065  1.00 33.37  ? 47  LEU C CD2 1 
ATOM   5151 N N   . ILE C 3 48  ? -30.314 42.683 65.101  1.00 33.94  ? 48  ILE C N   1 
ATOM   5152 C CA  . ILE C 3 48  ? -29.620 41.516 64.581  1.00 32.52  ? 48  ILE C CA  1 
ATOM   5153 C C   . ILE C 3 48  ? -30.615 40.734 63.734  1.00 30.94  ? 48  ILE C C   1 
ATOM   5154 O O   . ILE C 3 48  ? -31.801 40.657 64.070  1.00 29.45  ? 48  ILE C O   1 
ATOM   5155 C CB  . ILE C 3 48  ? -29.075 40.631 65.728  1.00 35.98  ? 48  ILE C CB  1 
ATOM   5156 C CG1 . ILE C 3 48  ? -28.117 41.400 66.647  1.00 31.72  ? 48  ILE C CG1 1 
ATOM   5157 C CG2 . ILE C 3 48  ? -28.350 39.421 65.160  1.00 35.19  ? 48  ILE C CG2 1 
ATOM   5158 C CD1 . ILE C 3 48  ? -26.682 41.422 66.180  1.00 43.31  ? 48  ILE C CD1 1 
ATOM   5159 N N   . TYR C 3 49  ? -30.143 40.170 62.627  1.00 29.54  ? 49  TYR C N   1 
ATOM   5160 C CA  . TYR C 3 49  ? -30.890 39.156 61.899  1.00 33.20  ? 49  TYR C CA  1 
ATOM   5161 C C   . TYR C 3 49  ? -29.943 38.002 61.608  1.00 33.37  ? 49  TYR C C   1 
ATOM   5162 O O   . TYR C 3 49  ? -28.727 38.115 61.787  1.00 34.71  ? 49  TYR C O   1 
ATOM   5163 C CB  . TYR C 3 49  ? -31.535 39.712 60.613  1.00 27.40  ? 49  TYR C CB  1 
ATOM   5164 C CG  . TYR C 3 49  ? -30.584 40.371 59.648  1.00 27.86  ? 49  TYR C CG  1 
ATOM   5165 C CD1 . TYR C 3 49  ? -29.993 39.646 58.621  1.00 33.92  ? 49  TYR C CD1 1 
ATOM   5166 C CD2 . TYR C 3 49  ? -30.289 41.725 59.749  1.00 32.11  ? 49  TYR C CD2 1 
ATOM   5167 C CE1 . TYR C 3 49  ? -29.123 40.249 57.729  1.00 36.54  ? 49  TYR C CE1 1 
ATOM   5168 C CE2 . TYR C 3 49  ? -29.419 42.335 58.862  1.00 34.71  ? 49  TYR C CE2 1 
ATOM   5169 C CZ  . TYR C 3 49  ? -28.840 41.589 57.857  1.00 31.35  ? 49  TYR C CZ  1 
ATOM   5170 O OH  . TYR C 3 49  ? -27.975 42.176 56.970  1.00 33.34  ? 49  TYR C OH  1 
ATOM   5171 N N   . SER C 3 50  ? -30.513 36.867 61.191  1.00 32.94  ? 50  SER C N   1 
ATOM   5172 C CA  . SER C 3 50  ? -29.748 35.629 61.009  1.00 33.13  ? 50  SER C CA  1 
ATOM   5173 C C   . SER C 3 50  ? -28.994 35.243 62.282  1.00 30.40  ? 50  SER C C   1 
ATOM   5174 O O   . SER C 3 50  ? -27.902 34.673 62.223  1.00 32.60  ? 50  SER C O   1 
ATOM   5175 C CB  . SER C 3 50  ? -28.779 35.739 59.825  1.00 33.50  ? 50  SER C CB  1 
ATOM   5176 O OG  . SER C 3 50  ? -29.464 36.032 58.618  1.00 36.92  ? 50  SER C OG  1 
ATOM   5177 N N   . ALA C 3 51  ? -29.573 35.585 63.438  1.00 35.04  ? 51  ALA C N   1 
ATOM   5178 C CA  . ALA C 3 51  ? -29.053 35.268 64.771  1.00 34.51  ? 51  ALA C CA  1 
ATOM   5179 C C   . ALA C 3 51  ? -27.799 36.061 65.136  1.00 37.07  ? 51  ALA C C   1 
ATOM   5180 O O   . ALA C 3 51  ? -27.643 36.463 66.295  1.00 33.12  ? 51  ALA C O   1 
ATOM   5181 C CB  . ALA C 3 51  ? -28.778 33.764 64.910  1.00 28.68  ? 51  ALA C CB  1 
ATOM   5182 N N   . SER C 3 52  ? -26.896 36.296 64.175  1.00 36.09  ? 52  SER C N   1 
ATOM   5183 C CA  . SER C 3 52  ? -25.628 36.952 64.479  1.00 37.24  ? 52  SER C CA  1 
ATOM   5184 C C   . SER C 3 52  ? -25.245 38.093 63.543  1.00 39.30  ? 52  SER C C   1 
ATOM   5185 O O   . SER C 3 52  ? -24.237 38.758 63.809  1.00 36.88  ? 52  SER C O   1 
ATOM   5186 C CB  . SER C 3 52  ? -24.478 35.933 64.485  1.00 30.12  ? 52  SER C CB  1 
ATOM   5187 O OG  . SER C 3 52  ? -24.468 35.169 63.299  1.00 42.35  ? 52  SER C OG  1 
ATOM   5188 N N   . THR C 3 53  ? -26.000 38.349 62.475  1.00 33.02  ? 53  THR C N   1 
ATOM   5189 C CA  . THR C 3 53  ? -25.686 39.447 61.564  1.00 33.54  ? 53  THR C CA  1 
ATOM   5190 C C   . THR C 3 53  ? -26.215 40.753 62.145  1.00 39.38  ? 53  THR C C   1 
ATOM   5191 O O   . THR C 3 53  ? -27.431 40.953 62.241  1.00 34.20  ? 53  THR C O   1 
ATOM   5192 C CB  . THR C 3 53  ? -26.280 39.196 60.181  1.00 32.61  ? 53  THR C CB  1 
ATOM   5193 O OG1 . THR C 3 53  ? -25.818 37.937 59.671  1.00 38.94  ? 53  THR C OG1 1 
ATOM   5194 C CG2 . THR C 3 53  ? -25.887 40.304 59.231  1.00 33.75  ? 53  THR C CG2 1 
ATOM   5195 N N   . ARG C 3 54  ? -25.306 41.651 62.515  1.00 35.65  ? 54  ARG C N   1 
ATOM   5196 C CA  . ARG C 3 54  ? -25.701 42.938 63.072  1.00 37.66  ? 54  ARG C CA  1 
ATOM   5197 C C   . ARG C 3 54  ? -26.190 43.871 61.967  1.00 37.45  ? 54  ARG C C   1 
ATOM   5198 O O   . ARG C 3 54  ? -25.513 44.061 60.952  1.00 36.30  ? 54  ARG C O   1 
ATOM   5199 C CB  . ARG C 3 54  ? -24.536 43.567 63.833  1.00 33.55  ? 54  ARG C CB  1 
ATOM   5200 C CG  . ARG C 3 54  ? -24.899 44.856 64.544  1.00 42.25  ? 54  ARG C CG  1 
ATOM   5201 C CD  . ARG C 3 54  ? -23.815 45.271 65.524  1.00 39.04  ? 54  ARG C CD  1 
ATOM   5202 N NE  . ARG C 3 54  ? -22.753 45.990 64.836  1.00 48.21  ? 54  ARG C NE  1 
ATOM   5203 C CZ  . ARG C 3 54  ? -21.562 45.477 64.560  1.00 51.27  ? 54  ARG C CZ  1 
ATOM   5204 N NH1 . ARG C 3 54  ? -21.215 44.270 64.980  1.00 48.15  ? 54  ARG C NH1 1 
ATOM   5205 N NH2 . ARG C 3 54  ? -20.697 46.192 63.846  1.00 50.38  ? 54  ARG C NH2 1 
ATOM   5206 N N   . ALA C 3 55  ? -27.371 44.447 62.169  1.00 33.14  ? 55  ALA C N   1 
ATOM   5207 C CA  . ALA C 3 55  ? -27.974 45.308 61.167  1.00 39.64  ? 55  ALA C CA  1 
ATOM   5208 C C   . ALA C 3 55  ? -27.133 46.563 60.948  1.00 37.16  ? 55  ALA C C   1 
ATOM   5209 O O   . ALA C 3 55  ? -26.371 46.998 61.814  1.00 37.90  ? 55  ALA C O   1 
ATOM   5210 C CB  . ALA C 3 55  ? -29.396 45.695 61.579  1.00 29.26  ? 55  ALA C CB  1 
ATOM   5211 N N   . SER C 3 56  ? -27.290 47.150 59.766  1.00 37.98  ? 56  SER C N   1 
ATOM   5212 C CA  . SER C 3 56  ? -26.525 48.337 59.415  1.00 42.63  ? 56  SER C CA  1 
ATOM   5213 C C   . SER C 3 56  ? -26.879 49.493 60.340  1.00 40.67  ? 56  SER C C   1 
ATOM   5214 O O   . SER C 3 56  ? -28.055 49.811 60.535  1.00 44.60  ? 56  SER C O   1 
ATOM   5215 C CB  . SER C 3 56  ? -26.794 48.720 57.961  1.00 44.51  ? 56  SER C CB  1 
ATOM   5216 O OG  . SER C 3 56  ? -26.646 50.115 57.767  1.00 56.68  ? 56  SER C OG  1 
ATOM   5217 N N   . GLY C 3 57  ? -25.852 50.121 60.915  1.00 44.49  ? 57  GLY C N   1 
ATOM   5218 C CA  . GLY C 3 57  ? -26.034 51.259 61.787  1.00 39.66  ? 57  GLY C CA  1 
ATOM   5219 C C   . GLY C 3 57  ? -26.170 50.936 63.259  1.00 42.93  ? 57  GLY C C   1 
ATOM   5220 O O   . GLY C 3 57  ? -26.214 51.864 64.077  1.00 45.97  ? 57  GLY C O   1 
ATOM   5221 N N   . VAL C 3 58  ? -26.246 49.660 63.626  1.00 37.84  ? 58  VAL C N   1 
ATOM   5222 C CA  . VAL C 3 58  ? -26.355 49.268 65.030  1.00 42.98  ? 58  VAL C CA  1 
ATOM   5223 C C   . VAL C 3 58  ? -24.964 49.330 65.653  1.00 40.68  ? 58  VAL C C   1 
ATOM   5224 O O   . VAL C 3 58  ? -23.991 48.875 65.030  1.00 40.43  ? 58  VAL C O   1 
ATOM   5225 C CB  . VAL C 3 58  ? -26.983 47.868 65.172  1.00 43.23  ? 58  VAL C CB  1 
ATOM   5226 C CG1 . VAL C 3 58  ? -26.907 47.373 66.619  1.00 30.85  ? 58  VAL C CG1 1 
ATOM   5227 C CG2 . VAL C 3 58  ? -28.431 47.876 64.675  1.00 36.17  ? 58  VAL C CG2 1 
ATOM   5228 N N   . PRO C 3 59  ? -24.816 49.890 66.856  1.00 40.57  ? 59  PRO C N   1 
ATOM   5229 C CA  . PRO C 3 59  ? -23.492 49.941 67.489  1.00 37.81  ? 59  PRO C CA  1 
ATOM   5230 C C   . PRO C 3 59  ? -22.902 48.552 67.671  1.00 42.70  ? 59  PRO C C   1 
ATOM   5231 O O   . PRO C 3 59  ? -23.617 47.564 67.852  1.00 40.60  ? 59  PRO C O   1 
ATOM   5232 C CB  . PRO C 3 59  ? -23.764 50.613 68.841  1.00 41.16  ? 59  PRO C CB  1 
ATOM   5233 C CG  . PRO C 3 59  ? -25.028 51.389 68.639  1.00 33.77  ? 59  PRO C CG  1 
ATOM   5234 C CD  . PRO C 3 59  ? -25.839 50.598 67.646  1.00 40.41  ? 59  PRO C CD  1 
ATOM   5235 N N   . ALA C 3 60  ? -21.570 48.492 67.629  1.00 44.11  ? 60  ALA C N   1 
ATOM   5236 C CA  . ALA C 3 60  ? -20.871 47.214 67.657  1.00 40.93  ? 60  ALA C CA  1 
ATOM   5237 C C   . ALA C 3 60  ? -20.978 46.503 69.001  1.00 39.78  ? 60  ALA C C   1 
ATOM   5238 O O   . ALA C 3 60  ? -20.681 45.305 69.077  1.00 42.19  ? 60  ALA C O   1 
ATOM   5239 C CB  . ALA C 3 60  ? -19.398 47.419 67.300  1.00 41.18  ? 60  ALA C CB  1 
ATOM   5240 N N   . ARG C 3 61  ? -21.379 47.202 70.065  1.00 41.70  ? 61  ARG C N   1 
ATOM   5241 C CA  . ARG C 3 61  ? -21.479 46.550 71.364  1.00 38.64  ? 61  ARG C CA  1 
ATOM   5242 C C   . ARG C 3 61  ? -22.613 45.531 71.413  1.00 40.55  ? 61  ARG C C   1 
ATOM   5243 O O   . ARG C 3 61  ? -22.617 44.671 72.301  1.00 38.09  ? 61  ARG C O   1 
ATOM   5244 C CB  . ARG C 3 61  ? -21.651 47.596 72.467  1.00 35.74  ? 61  ARG C CB  1 
ATOM   5245 C CG  . ARG C 3 61  ? -22.978 48.328 72.452  1.00 39.59  ? 61  ARG C CG  1 
ATOM   5246 C CD  . ARG C 3 61  ? -23.079 49.291 73.640  1.00 37.99  ? 61  ARG C CD  1 
ATOM   5247 N NE  . ARG C 3 61  ? -24.254 50.155 73.571  1.00 33.18  ? 61  ARG C NE  1 
ATOM   5248 C CZ  . ARG C 3 61  ? -24.325 51.262 72.843  1.00 41.66  ? 61  ARG C CZ  1 
ATOM   5249 N NH1 . ARG C 3 61  ? -23.305 51.669 72.101  1.00 37.70  ? 61  ARG C NH1 1 
ATOM   5250 N NH2 . ARG C 3 61  ? -25.448 51.977 72.855  1.00 37.88  ? 61  ARG C NH2 1 
ATOM   5251 N N   . PHE C 3 62  ? -23.564 45.598 70.483  1.00 35.25  ? 62  PHE C N   1 
ATOM   5252 C CA  . PHE C 3 62  ? -24.617 44.596 70.376  1.00 37.35  ? 62  PHE C CA  1 
ATOM   5253 C C   . PHE C 3 62  ? -24.142 43.448 69.497  1.00 32.68  ? 62  PHE C C   1 
ATOM   5254 O O   . PHE C 3 62  ? -23.613 43.673 68.406  1.00 35.30  ? 62  PHE C O   1 
ATOM   5255 C CB  . PHE C 3 62  ? -25.895 45.196 69.786  1.00 30.89  ? 62  PHE C CB  1 
ATOM   5256 C CG  . PHE C 3 62  ? -26.504 46.280 70.621  1.00 34.53  ? 62  PHE C CG  1 
ATOM   5257 C CD1 . PHE C 3 62  ? -27.443 45.975 71.597  1.00 35.94  ? 62  PHE C CD1 1 
ATOM   5258 C CD2 . PHE C 3 62  ? -26.147 47.607 70.426  1.00 33.30  ? 62  PHE C CD2 1 
ATOM   5259 C CE1 . PHE C 3 62  ? -28.015 46.975 72.366  1.00 35.59  ? 62  PHE C CE1 1 
ATOM   5260 C CE2 . PHE C 3 62  ? -26.708 48.610 71.194  1.00 38.44  ? 62  PHE C CE2 1 
ATOM   5261 C CZ  . PHE C 3 62  ? -27.646 48.293 72.168  1.00 37.74  ? 62  PHE C CZ  1 
ATOM   5262 N N   . SER C 3 63  ? -24.338 42.221 69.969  1.00 35.01  ? 63  SER C N   1 
ATOM   5263 C CA  . SER C 3 63  ? -24.045 41.052 69.155  1.00 38.51  ? 63  SER C CA  1 
ATOM   5264 C C   . SER C 3 63  ? -24.953 39.909 69.581  1.00 36.58  ? 63  SER C C   1 
ATOM   5265 O O   . SER C 3 63  ? -25.407 39.847 70.728  1.00 39.63  ? 63  SER C O   1 
ATOM   5266 C CB  . SER C 3 63  ? -22.573 40.631 69.259  1.00 36.63  ? 63  SER C CB  1 
ATOM   5267 O OG  . SER C 3 63  ? -22.255 40.166 70.559  1.00 39.58  ? 63  SER C OG  1 
ATOM   5268 N N   . GLY C 3 64  ? -25.215 39.004 68.641  1.00 33.02  ? 64  GLY C N   1 
ATOM   5269 C CA  . GLY C 3 64  ? -26.029 37.845 68.915  1.00 36.38  ? 64  GLY C CA  1 
ATOM   5270 C C   . GLY C 3 64  ? -25.300 36.574 68.525  1.00 33.49  ? 64  GLY C C   1 
ATOM   5271 O O   . GLY C 3 64  ? -24.374 36.584 67.715  1.00 32.51  ? 64  GLY C O   1 
ATOM   5272 N N   . SER C 3 65  ? -25.733 35.470 69.128  1.00 40.40  ? 65  SER C N   1 
ATOM   5273 C CA  . SER C 3 65  ? -25.164 34.166 68.826  1.00 37.49  ? 65  SER C CA  1 
ATOM   5274 C C   . SER C 3 65  ? -26.207 33.102 69.115  1.00 36.19  ? 65  SER C C   1 
ATOM   5275 O O   . SER C 3 65  ? -27.271 33.374 69.676  1.00 38.49  ? 65  SER C O   1 
ATOM   5276 C CB  . SER C 3 65  ? -23.890 33.901 69.632  1.00 37.75  ? 65  SER C CB  1 
ATOM   5277 O OG  . SER C 3 65  ? -23.997 34.432 70.939  1.00 46.53  ? 65  SER C OG  1 
ATOM   5278 N N   . GLY C 3 66  ? -25.884 31.878 68.732  1.00 36.92  ? 66  GLY C N   1 
ATOM   5279 C CA  . GLY C 3 66  ? -26.734 30.733 68.984  1.00 35.58  ? 66  GLY C CA  1 
ATOM   5280 C C   . GLY C 3 66  ? -27.277 30.135 67.700  1.00 38.18  ? 66  GLY C C   1 
ATOM   5281 O O   . GLY C 3 66  ? -27.180 30.707 66.617  1.00 40.73  ? 66  GLY C O   1 
ATOM   5282 N N   . SER C 3 67  ? -27.843 28.941 67.856  1.00 39.76  ? 67  SER C N   1 
ATOM   5283 C CA  . SER C 3 67  ? -28.434 28.190 66.757  1.00 41.17  ? 67  SER C CA  1 
ATOM   5284 C C   . SER C 3 67  ? -29.412 27.197 67.360  1.00 39.29  ? 67  SER C C   1 
ATOM   5285 O O   . SER C 3 67  ? -29.459 27.015 68.577  1.00 36.47  ? 67  SER C O   1 
ATOM   5286 C CB  . SER C 3 67  ? -27.366 27.477 65.921  1.00 35.85  ? 67  SER C CB  1 
ATOM   5287 O OG  . SER C 3 67  ? -26.672 26.518 66.701  1.00 45.10  ? 67  SER C OG  1 
ATOM   5288 N N   . GLY C 3 68  ? -30.197 26.556 66.491  1.00 37.50  ? 68  GLY C N   1 
ATOM   5289 C CA  . GLY C 3 68  ? -31.146 25.549 66.928  1.00 32.93  ? 68  GLY C CA  1 
ATOM   5290 C C   . GLY C 3 68  ? -32.235 26.078 67.841  1.00 38.76  ? 68  GLY C C   1 
ATOM   5291 O O   . GLY C 3 68  ? -33.228 26.648 67.373  1.00 41.77  ? 68  GLY C O   1 
ATOM   5292 N N   . THR C 3 69  ? -32.064 25.900 69.154  1.00 36.26  ? 69  THR C N   1 
ATOM   5293 C CA  . THR C 3 69  ? -33.058 26.337 70.124  1.00 36.65  ? 69  THR C CA  1 
ATOM   5294 C C   . THR C 3 69  ? -32.524 27.326 71.147  1.00 37.58  ? 69  THR C C   1 
ATOM   5295 O O   . THR C 3 69  ? -33.308 27.812 71.969  1.00 38.72  ? 69  THR C O   1 
ATOM   5296 C CB  . THR C 3 69  ? -33.653 25.137 70.884  1.00 42.92  ? 69  THR C CB  1 
ATOM   5297 O OG1 . THR C 3 69  ? -32.631 24.498 71.657  1.00 43.21  ? 69  THR C OG1 1 
ATOM   5298 C CG2 . THR C 3 69  ? -34.284 24.134 69.927  1.00 40.18  ? 69  THR C CG2 1 
ATOM   5299 N N   . GLU C 3 70  ? -31.230 27.637 71.139  1.00 34.27  ? 70  GLU C N   1 
ATOM   5300 C CA  . GLU C 3 70  ? -30.631 28.496 72.153  1.00 38.01  ? 70  GLU C CA  1 
ATOM   5301 C C   . GLU C 3 70  ? -29.987 29.704 71.491  1.00 37.61  ? 70  GLU C C   1 
ATOM   5302 O O   . GLU C 3 70  ? -29.168 29.555 70.580  1.00 39.17  ? 70  GLU C O   1 
ATOM   5303 C CB  . GLU C 3 70  ? -29.598 27.726 72.978  1.00 42.01  ? 70  GLU C CB  1 
ATOM   5304 C CG  . GLU C 3 70  ? -30.055 26.329 73.361  1.00 52.75  ? 70  GLU C CG  1 
ATOM   5305 C CD  . GLU C 3 70  ? -29.797 26.010 74.818  1.00 68.00  ? 70  GLU C CD  1 
ATOM   5306 O OE1 . GLU C 3 70  ? -29.453 26.943 75.577  1.00 75.38  ? 70  GLU C OE1 1 
ATOM   5307 O OE2 . GLU C 3 70  ? -29.938 24.827 75.202  1.00 70.63  ? 70  GLU C OE2 1 
ATOM   5308 N N   . PHE C 3 71  ? -30.352 30.897 71.956  1.00 35.28  ? 71  PHE C N   1 
ATOM   5309 C CA  . PHE C 3 71  ? -29.876 32.133 71.356  1.00 36.55  ? 71  PHE C CA  1 
ATOM   5310 C C   . PHE C 3 71  ? -29.592 33.152 72.446  1.00 33.90  ? 71  PHE C C   1 
ATOM   5311 O O   . PHE C 3 71  ? -30.225 33.147 73.503  1.00 36.53  ? 71  PHE C O   1 
ATOM   5312 C CB  . PHE C 3 71  ? -30.894 32.695 70.357  1.00 31.75  ? 71  PHE C CB  1 
ATOM   5313 C CG  . PHE C 3 71  ? -31.185 31.766 69.223  1.00 36.76  ? 71  PHE C CG  1 
ATOM   5314 C CD1 . PHE C 3 71  ? -32.172 30.795 69.340  1.00 37.09  ? 71  PHE C CD1 1 
ATOM   5315 C CD2 . PHE C 3 71  ? -30.452 31.838 68.051  1.00 32.03  ? 71  PHE C CD2 1 
ATOM   5316 C CE1 . PHE C 3 71  ? -32.434 29.925 68.308  1.00 34.40  ? 71  PHE C CE1 1 
ATOM   5317 C CE2 . PHE C 3 71  ? -30.710 30.972 67.012  1.00 39.44  ? 71  PHE C CE2 1 
ATOM   5318 C CZ  . PHE C 3 71  ? -31.709 30.012 67.140  1.00 38.63  ? 71  PHE C CZ  1 
ATOM   5319 N N   . SER C 3 72  ? -28.637 34.035 72.170  1.00 34.53  ? 72  SER C N   1 
ATOM   5320 C CA  . SER C 3 72  ? -28.246 35.075 73.106  1.00 34.99  ? 72  SER C CA  1 
ATOM   5321 C C   . SER C 3 72  ? -28.067 36.388 72.363  1.00 36.53  ? 72  SER C C   1 
ATOM   5322 O O   . SER C 3 72  ? -27.644 36.410 71.204  1.00 36.85  ? 72  SER C O   1 
ATOM   5323 C CB  . SER C 3 72  ? -26.940 34.730 73.837  1.00 36.05  ? 72  SER C CB  1 
ATOM   5324 O OG  . SER C 3 72  ? -27.117 33.622 74.696  1.00 57.18  ? 72  SER C OG  1 
ATOM   5325 N N   . LEU C 3 73  ? -28.406 37.479 73.042  1.00 33.64  ? 73  LEU C N   1 
ATOM   5326 C CA  . LEU C 3 73  ? -28.003 38.820 72.649  1.00 33.96  ? 73  LEU C CA  1 
ATOM   5327 C C   . LEU C 3 73  ? -27.058 39.354 73.713  1.00 39.67  ? 73  LEU C C   1 
ATOM   5328 O O   . LEU C 3 73  ? -27.359 39.273 74.909  1.00 37.39  ? 73  LEU C O   1 
ATOM   5329 C CB  . LEU C 3 73  ? -29.207 39.751 72.494  1.00 33.74  ? 73  LEU C CB  1 
ATOM   5330 C CG  . LEU C 3 73  ? -28.832 41.192 72.133  1.00 37.69  ? 73  LEU C CG  1 
ATOM   5331 C CD1 . LEU C 3 73  ? -28.640 41.341 70.625  1.00 33.29  ? 73  LEU C CD1 1 
ATOM   5332 C CD2 . LEU C 3 73  ? -29.871 42.185 72.653  1.00 34.54  ? 73  LEU C CD2 1 
ATOM   5333 N N   . THR C 3 74  ? -25.915 39.879 73.285  1.00 37.84  ? 74  THR C N   1 
ATOM   5334 C CA  . THR C 3 74  ? -24.911 40.400 74.203  1.00 38.74  ? 74  THR C CA  1 
ATOM   5335 C C   . THR C 3 74  ? -24.705 41.882 73.946  1.00 40.88  ? 74  THR C C   1 
ATOM   5336 O O   . THR C 3 74  ? -24.508 42.294 72.797  1.00 39.36  ? 74  THR C O   1 
ATOM   5337 C CB  . THR C 3 74  ? -23.577 39.659 74.060  1.00 41.77  ? 74  THR C CB  1 
ATOM   5338 O OG1 . THR C 3 74  ? -23.747 38.284 74.424  1.00 41.27  ? 74  THR C OG1 1 
ATOM   5339 C CG2 . THR C 3 74  ? -22.520 40.290 74.955  1.00 44.36  ? 74  THR C CG2 1 
ATOM   5340 N N   . ILE C 3 75  ? -24.770 42.674 75.012  1.00 39.72  ? 75  ILE C N   1 
ATOM   5341 C CA  . ILE C 3 75  ? -24.326 44.062 75.013  1.00 36.88  ? 75  ILE C CA  1 
ATOM   5342 C C   . ILE C 3 75  ? -22.996 44.072 75.757  1.00 40.38  ? 75  ILE C C   1 
ATOM   5343 O O   . ILE C 3 75  ? -22.962 43.996 76.991  1.00 45.34  ? 75  ILE C O   1 
ATOM   5344 C CB  . ILE C 3 75  ? -25.348 45.000 75.665  1.00 39.73  ? 75  ILE C CB  1 
ATOM   5345 C CG1 . ILE C 3 75  ? -26.766 44.635 75.221  1.00 44.43  ? 75  ILE C CG1 1 
ATOM   5346 C CG2 . ILE C 3 75  ? -25.036 46.446 75.312  1.00 40.38  ? 75  ILE C CG2 1 
ATOM   5347 C CD1 . ILE C 3 75  ? -27.831 45.603 75.704  1.00 40.88  ? 75  ILE C CD1 1 
ATOM   5348 N N   . SER C 3 76  ? -21.894 44.150 75.008  1.00 42.71  ? 76  SER C N   1 
ATOM   5349 C CA  . SER C 3 76  ? -20.575 43.937 75.602  1.00 42.92  ? 76  SER C CA  1 
ATOM   5350 C C   . SER C 3 76  ? -20.236 44.996 76.643  1.00 42.32  ? 76  SER C C   1 
ATOM   5351 O O   . SER C 3 76  ? -19.509 44.712 77.598  1.00 45.99  ? 76  SER C O   1 
ATOM   5352 C CB  . SER C 3 76  ? -19.506 43.907 74.513  1.00 37.12  ? 76  SER C CB  1 
ATOM   5353 O OG  . SER C 3 76  ? -19.516 45.111 73.774  1.00 41.84  ? 76  SER C OG  1 
ATOM   5354 N N   . SER C 3 77  ? -20.748 46.213 76.486  1.00 43.82  ? 77  SER C N   1 
ATOM   5355 C CA  . SER C 3 77  ? -20.540 47.254 77.490  1.00 38.37  ? 77  SER C CA  1 
ATOM   5356 C C   . SER C 3 77  ? -21.822 48.080 77.545  1.00 40.02  ? 77  SER C C   1 
ATOM   5357 O O   . SER C 3 77  ? -22.056 48.925 76.676  1.00 36.79  ? 77  SER C O   1 
ATOM   5358 C CB  . SER C 3 77  ? -19.327 48.113 77.156  1.00 43.05  ? 77  SER C CB  1 
ATOM   5359 O OG  . SER C 3 77  ? -19.258 49.245 78.002  1.00 47.89  ? 77  SER C OG  1 
ATOM   5360 N N   . LEU C 3 78  ? -22.638 47.825 78.566  1.00 35.31  ? 78  LEU C N   1 
ATOM   5361 C CA  . LEU C 3 78  ? -23.945 48.459 78.678  1.00 38.65  ? 78  LEU C CA  1 
ATOM   5362 C C   . LEU C 3 78  ? -23.815 49.973 78.827  1.00 42.21  ? 78  LEU C C   1 
ATOM   5363 O O   . LEU C 3 78  ? -23.043 50.471 79.651  1.00 39.23  ? 78  LEU C O   1 
ATOM   5364 C CB  . LEU C 3 78  ? -24.694 47.861 79.869  1.00 43.06  ? 78  LEU C CB  1 
ATOM   5365 C CG  . LEU C 3 78  ? -26.187 48.123 80.042  1.00 44.89  ? 78  LEU C CG  1 
ATOM   5366 C CD1 . LEU C 3 78  ? -26.979 47.528 78.886  1.00 44.02  ? 78  LEU C CD1 1 
ATOM   5367 C CD2 . LEU C 3 78  ? -26.651 47.539 81.369  1.00 39.18  ? 78  LEU C CD2 1 
ATOM   5368 N N   . GLN C 3 79  ? -24.566 50.704 78.015  1.00 39.65  ? 79  GLN C N   1 
ATOM   5369 C CA  . GLN C 3 79  ? -24.660 52.151 78.128  1.00 37.33  ? 79  GLN C CA  1 
ATOM   5370 C C   . GLN C 3 79  ? -25.991 52.525 78.761  1.00 41.78  ? 79  GLN C C   1 
ATOM   5371 O O   . GLN C 3 79  ? -26.958 51.760 78.722  1.00 39.82  ? 79  GLN C O   1 
ATOM   5372 C CB  . GLN C 3 79  ? -24.522 52.815 76.756  1.00 38.06  ? 79  GLN C CB  1 
ATOM   5373 C CG  . GLN C 3 79  ? -23.230 52.455 76.046  1.00 36.33  ? 79  GLN C CG  1 
ATOM   5374 C CD  . GLN C 3 79  ? -22.019 52.639 76.945  1.00 41.34  ? 79  GLN C CD  1 
ATOM   5375 O OE1 . GLN C 3 79  ? -21.761 53.741 77.428  1.00 42.35  ? 79  GLN C OE1 1 
ATOM   5376 N NE2 . GLN C 3 79  ? -21.277 51.557 77.185  1.00 37.58  ? 79  GLN C NE2 1 
ATOM   5377 N N   . SER C 3 80  ? -26.032 53.720 79.355  1.00 44.37  ? 80  SER C N   1 
ATOM   5378 C CA  . SER C 3 80  ? -27.264 54.164 79.991  1.00 40.18  ? 80  SER C CA  1 
ATOM   5379 C C   . SER C 3 80  ? -28.383 54.378 78.981  1.00 41.00  ? 80  SER C C   1 
ATOM   5380 O O   . SER C 3 80  ? -29.559 54.318 79.355  1.00 46.84  ? 80  SER C O   1 
ATOM   5381 C CB  . SER C 3 80  ? -27.019 55.444 80.797  1.00 43.28  ? 80  SER C CB  1 
ATOM   5382 O OG  . SER C 3 80  ? -26.781 56.553 79.951  1.00 49.48  ? 80  SER C OG  1 
ATOM   5383 N N   . GLU C 3 81  ? -28.050 54.607 77.710  1.00 40.78  ? 81  GLU C N   1 
ATOM   5384 C CA  . GLU C 3 81  ? -29.071 54.711 76.677  1.00 46.94  ? 81  GLU C CA  1 
ATOM   5385 C C   . GLU C 3 81  ? -29.591 53.353 76.221  1.00 42.80  ? 81  GLU C C   1 
ATOM   5386 O O   . GLU C 3 81  ? -30.531 53.310 75.423  1.00 41.56  ? 81  GLU C O   1 
ATOM   5387 C CB  . GLU C 3 81  ? -28.534 55.487 75.468  1.00 45.09  ? 81  GLU C CB  1 
ATOM   5388 C CG  . GLU C 3 81  ? -27.300 54.880 74.815  1.00 49.56  ? 81  GLU C CG  1 
ATOM   5389 C CD  . GLU C 3 81  ? -26.960 55.539 73.490  1.00 53.77  ? 81  GLU C CD  1 
ATOM   5390 O OE1 . GLU C 3 81  ? -27.579 56.576 73.174  1.00 60.48  ? 81  GLU C OE1 1 
ATOM   5391 O OE2 . GLU C 3 81  ? -26.074 55.029 72.767  1.00 56.15  ? 81  GLU C OE2 1 
ATOM   5392 N N   . ASP C 3 82  ? -29.016 52.253 76.709  1.00 44.18  ? 82  ASP C N   1 
ATOM   5393 C CA  . ASP C 3 82  ? -29.452 50.916 76.322  1.00 41.41  ? 82  ASP C CA  1 
ATOM   5394 C C   . ASP C 3 82  ? -30.665 50.432 77.105  1.00 43.42  ? 82  ASP C C   1 
ATOM   5395 O O   . ASP C 3 82  ? -31.093 49.288 76.905  1.00 45.43  ? 82  ASP C O   1 
ATOM   5396 C CB  . ASP C 3 82  ? -28.306 49.919 76.492  1.00 40.32  ? 82  ASP C CB  1 
ATOM   5397 C CG  . ASP C 3 82  ? -27.161 50.180 75.540  1.00 38.77  ? 82  ASP C CG  1 
ATOM   5398 O OD1 . ASP C 3 82  ? -27.374 50.895 74.538  1.00 43.95  ? 82  ASP C OD1 1 
ATOM   5399 O OD2 . ASP C 3 82  ? -26.048 49.667 75.790  1.00 42.31  ? 82  ASP C OD2 1 
ATOM   5400 N N   . PHE C 3 83  ? -31.213 51.255 77.996  1.00 42.97  ? 83  PHE C N   1 
ATOM   5401 C CA  . PHE C 3 83  ? -32.443 50.905 78.696  1.00 45.25  ? 83  PHE C CA  1 
ATOM   5402 C C   . PHE C 3 83  ? -33.575 50.730 77.694  1.00 40.29  ? 83  PHE C C   1 
ATOM   5403 O O   . PHE C 3 83  ? -33.926 51.668 76.972  1.00 43.74  ? 83  PHE C O   1 
ATOM   5404 C CB  . PHE C 3 83  ? -32.789 51.988 79.719  1.00 43.34  ? 83  PHE C CB  1 
ATOM   5405 C CG  . PHE C 3 83  ? -34.225 51.970 80.164  1.00 48.45  ? 83  PHE C CG  1 
ATOM   5406 C CD1 . PHE C 3 83  ? -34.641 51.111 81.175  1.00 56.84  ? 83  PHE C CD1 1 
ATOM   5407 C CD2 . PHE C 3 83  ? -35.157 52.819 79.585  1.00 47.56  ? 83  PHE C CD2 1 
ATOM   5408 C CE1 . PHE C 3 83  ? -35.962 51.094 81.597  1.00 53.49  ? 83  PHE C CE1 1 
ATOM   5409 C CE2 . PHE C 3 83  ? -36.483 52.804 79.994  1.00 51.59  ? 83  PHE C CE2 1 
ATOM   5410 C CZ  . PHE C 3 83  ? -36.886 51.942 81.003  1.00 52.95  ? 83  PHE C CZ  1 
ATOM   5411 N N   . ALA C 3 84  ? -34.145 49.530 77.656  1.00 42.06  ? 84  ALA C N   1 
ATOM   5412 C CA  . ALA C 3 84  ? -35.196 49.198 76.701  1.00 44.05  ? 84  ALA C CA  1 
ATOM   5413 C C   . ALA C 3 84  ? -35.711 47.804 77.023  1.00 34.77  ? 84  ALA C C   1 
ATOM   5414 O O   . ALA C 3 84  ? -35.170 47.103 77.882  1.00 39.70  ? 84  ALA C O   1 
ATOM   5415 C CB  . ALA C 3 84  ? -34.686 49.262 75.257  1.00 36.82  ? 84  ALA C CB  1 
ATOM   5416 N N   . VAL C 3 85  ? -36.772 47.414 76.326  1.00 33.42  ? 85  VAL C N   1 
ATOM   5417 C CA  . VAL C 3 85  ? -37.196 46.022 76.256  1.00 37.85  ? 85  VAL C CA  1 
ATOM   5418 C C   . VAL C 3 85  ? -36.638 45.431 74.968  1.00 35.39  ? 85  VAL C C   1 
ATOM   5419 O O   . VAL C 3 85  ? -36.752 46.036 73.893  1.00 32.76  ? 85  VAL C O   1 
ATOM   5420 C CB  . VAL C 3 85  ? -38.728 45.889 76.311  1.00 37.47  ? 85  VAL C CB  1 
ATOM   5421 C CG1 . VAL C 3 85  ? -39.137 44.427 76.195  1.00 32.58  ? 85  VAL C CG1 1 
ATOM   5422 C CG2 . VAL C 3 85  ? -39.277 46.489 77.600  1.00 30.42  ? 85  VAL C CG2 1 
ATOM   5423 N N   . TYR C 3 86  ? -36.025 44.258 75.074  1.00 34.93  ? 86  TYR C N   1 
ATOM   5424 C CA  . TYR C 3 86  ? -35.426 43.579 73.935  1.00 33.34  ? 86  TYR C CA  1 
ATOM   5425 C C   . TYR C 3 86  ? -36.235 42.333 73.601  1.00 34.51  ? 86  TYR C C   1 
ATOM   5426 O O   . TYR C 3 86  ? -36.584 41.550 74.491  1.00 33.52  ? 86  TYR C O   1 
ATOM   5427 C CB  . TYR C 3 86  ? -33.964 43.225 74.223  1.00 35.36  ? 86  TYR C CB  1 
ATOM   5428 C CG  . TYR C 3 86  ? -33.085 44.447 74.370  1.00 36.53  ? 86  TYR C CG  1 
ATOM   5429 C CD1 . TYR C 3 86  ? -32.999 45.126 75.583  1.00 35.76  ? 86  TYR C CD1 1 
ATOM   5430 C CD2 . TYR C 3 86  ? -32.360 44.937 73.290  1.00 34.63  ? 86  TYR C CD2 1 
ATOM   5431 C CE1 . TYR C 3 86  ? -32.208 46.252 75.717  1.00 36.26  ? 86  TYR C CE1 1 
ATOM   5432 C CE2 . TYR C 3 86  ? -31.567 46.060 73.414  1.00 33.34  ? 86  TYR C CE2 1 
ATOM   5433 C CZ  . TYR C 3 86  ? -31.496 46.716 74.627  1.00 38.93  ? 86  TYR C CZ  1 
ATOM   5434 O OH  . TYR C 3 86  ? -30.707 47.841 74.751  1.00 41.02  ? 86  TYR C OH  1 
ATOM   5435 N N   . TYR C 3 87  ? -36.529 42.155 72.319  1.00 33.23  ? 87  TYR C N   1 
ATOM   5436 C CA  . TYR C 3 87  ? -37.358 41.064 71.837  1.00 31.11  ? 87  TYR C CA  1 
ATOM   5437 C C   . TYR C 3 87  ? -36.572 40.218 70.847  1.00 33.71  ? 87  TYR C C   1 
ATOM   5438 O O   . TYR C 3 87  ? -35.827 40.751 70.018  1.00 35.41  ? 87  TYR C O   1 
ATOM   5439 C CB  . TYR C 3 87  ? -38.619 41.599 71.145  1.00 30.84  ? 87  TYR C CB  1 
ATOM   5440 C CG  . TYR C 3 87  ? -39.620 42.277 72.050  1.00 32.41  ? 87  TYR C CG  1 
ATOM   5441 C CD1 . TYR C 3 87  ? -40.552 41.533 72.770  1.00 30.74  ? 87  TYR C CD1 1 
ATOM   5442 C CD2 . TYR C 3 87  ? -39.659 43.662 72.161  1.00 32.83  ? 87  TYR C CD2 1 
ATOM   5443 C CE1 . TYR C 3 87  ? -41.479 42.147 73.585  1.00 29.96  ? 87  TYR C CE1 1 
ATOM   5444 C CE2 . TYR C 3 87  ? -40.589 44.289 72.973  1.00 31.42  ? 87  TYR C CE2 1 
ATOM   5445 C CZ  . TYR C 3 87  ? -41.495 43.526 73.685  1.00 38.25  ? 87  TYR C CZ  1 
ATOM   5446 O OH  . TYR C 3 87  ? -42.420 44.143 74.499  1.00 38.22  ? 87  TYR C OH  1 
ATOM   5447 N N   . CYS C 3 88  ? -36.748 38.903 70.921  1.00 31.41  ? 88  CYS C N   1 
ATOM   5448 C CA  . CYS C 3 88  ? -36.326 38.036 69.832  1.00 32.55  ? 88  CYS C CA  1 
ATOM   5449 C C   . CYS C 3 88  ? -37.536 37.627 68.992  1.00 35.84  ? 88  CYS C C   1 
ATOM   5450 O O   . CYS C 3 88  ? -38.692 37.769 69.402  1.00 31.81  ? 88  CYS C O   1 
ATOM   5451 C CB  . CYS C 3 88  ? -35.578 36.802 70.350  1.00 29.54  ? 88  CYS C CB  1 
ATOM   5452 S SG  . CYS C 3 88  ? -36.505 35.625 71.360  1.00 39.58  ? 88  CYS C SG  1 
ATOM   5453 N N   . GLN C 3 89  ? -37.254 37.129 67.792  1.00 32.73  ? 89  GLN C N   1 
ATOM   5454 C CA  . GLN C 3 89  ? -38.311 36.843 66.827  1.00 31.96  ? 89  GLN C CA  1 
ATOM   5455 C C   . GLN C 3 89  ? -37.808 35.788 65.858  1.00 35.47  ? 89  GLN C C   1 
ATOM   5456 O O   . GLN C 3 89  ? -36.784 35.994 65.196  1.00 34.08  ? 89  GLN C O   1 
ATOM   5457 C CB  . GLN C 3 89  ? -38.717 38.118 66.085  1.00 30.72  ? 89  GLN C CB  1 
ATOM   5458 C CG  . GLN C 3 89  ? -39.776 37.925 65.024  1.00 30.80  ? 89  GLN C CG  1 
ATOM   5459 C CD  . GLN C 3 89  ? -39.256 38.201 63.623  1.00 36.45  ? 89  GLN C CD  1 
ATOM   5460 O OE1 . GLN C 3 89  ? -38.503 39.156 63.396  1.00 34.15  ? 89  GLN C OE1 1 
ATOM   5461 N NE2 . GLN C 3 89  ? -39.669 37.372 62.668  1.00 33.65  ? 89  GLN C NE2 1 
ATOM   5462 N N   . GLN C 3 90  ? -38.515 34.665 65.781  1.00 29.83  ? 90  GLN C N   1 
ATOM   5463 C CA  . GLN C 3 90  ? -38.176 33.602 64.850  1.00 31.43  ? 90  GLN C CA  1 
ATOM   5464 C C   . GLN C 3 90  ? -39.005 33.748 63.579  1.00 29.12  ? 90  GLN C C   1 
ATOM   5465 O O   . GLN C 3 90  ? -40.103 34.307 63.593  1.00 34.04  ? 90  GLN C O   1 
ATOM   5466 C CB  . GLN C 3 90  ? -38.403 32.222 65.481  1.00 26.49  ? 90  GLN C CB  1 
ATOM   5467 C CG  . GLN C 3 90  ? -39.857 31.910 65.843  1.00 27.76  ? 90  GLN C CG  1 
ATOM   5468 C CD  . GLN C 3 90  ? -40.638 31.287 64.693  1.00 33.02  ? 90  GLN C CD  1 
ATOM   5469 O OE1 . GLN C 3 90  ? -40.058 30.713 63.768  1.00 33.86  ? 90  GLN C OE1 1 
ATOM   5470 N NE2 . GLN C 3 90  ? -41.957 31.413 64.738  1.00 28.54  ? 90  GLN C NE2 1 
ATOM   5471 N N   . TYR C 3 91  ? -38.467 33.239 62.477  1.00 28.69  ? 91  TYR C N   1 
ATOM   5472 C CA  . TYR C 3 91  ? -39.171 33.263 61.199  1.00 32.90  ? 91  TYR C CA  1 
ATOM   5473 C C   . TYR C 3 91  ? -38.783 32.031 60.382  1.00 30.97  ? 91  TYR C C   1 
ATOM   5474 O O   . TYR C 3 91  ? -38.429 32.121 59.208  1.00 33.36  ? 91  TYR C O   1 
ATOM   5475 C CB  . TYR C 3 91  ? -38.879 34.556 60.435  1.00 28.96  ? 91  TYR C CB  1 
ATOM   5476 C CG  . TYR C 3 91  ? -37.416 34.965 60.389  1.00 30.67  ? 91  TYR C CG  1 
ATOM   5477 C CD1 . TYR C 3 91  ? -36.568 34.483 59.399  1.00 31.66  ? 91  TYR C CD1 1 
ATOM   5478 C CD2 . TYR C 3 91  ? -36.888 35.849 61.330  1.00 31.64  ? 91  TYR C CD2 1 
ATOM   5479 C CE1 . TYR C 3 91  ? -35.227 34.857 59.351  1.00 31.03  ? 91  TYR C CE1 1 
ATOM   5480 C CE2 . TYR C 3 91  ? -35.554 36.234 61.288  1.00 31.06  ? 91  TYR C CE2 1 
ATOM   5481 C CZ  . TYR C 3 91  ? -34.728 35.732 60.298  1.00 31.88  ? 91  TYR C CZ  1 
ATOM   5482 O OH  . TYR C 3 91  ? -33.403 36.103 60.256  1.00 34.64  ? 91  TYR C OH  1 
ATOM   5483 N N   . ASN C 3 92  ? -38.875 30.848 60.992  1.00 32.50  ? 92  ASN C N   1 
ATOM   5484 C CA  . ASN C 3 92  ? -38.285 29.663 60.378  1.00 33.22  ? 92  ASN C CA  1 
ATOM   5485 C C   . ASN C 3 92  ? -39.131 29.096 59.245  1.00 34.71  ? 92  ASN C C   1 
ATOM   5486 O O   . ASN C 3 92  ? -38.584 28.593 58.255  1.00 30.25  ? 92  ASN C O   1 
ATOM   5487 C CB  . ASN C 3 92  ? -38.047 28.584 61.433  1.00 34.17  ? 92  ASN C CB  1 
ATOM   5488 C CG  . ASN C 3 92  ? -37.262 27.417 60.885  1.00 31.79  ? 92  ASN C CG  1 
ATOM   5489 O OD1 . ASN C 3 92  ? -37.825 26.372 60.570  1.00 35.64  ? 92  ASN C OD1 1 
ATOM   5490 N ND2 . ASN C 3 92  ? -35.955 27.598 60.739  1.00 33.22  ? 92  ASN C ND2 1 
ATOM   5491 N N   . GLU C 3 93  ? -40.453 29.141 59.373  1.00 31.35  ? 93  GLU C N   1 
ATOM   5492 C CA  . GLU C 3 93  ? -41.327 28.489 58.411  1.00 33.59  ? 93  GLU C CA  1 
ATOM   5493 C C   . GLU C 3 93  ? -41.688 29.436 57.273  1.00 36.55  ? 93  GLU C C   1 
ATOM   5494 O O   . GLU C 3 93  ? -41.714 30.662 57.436  1.00 35.00  ? 93  GLU C O   1 
ATOM   5495 C CB  . GLU C 3 93  ? -42.591 27.974 59.109  1.00 33.32  ? 93  GLU C CB  1 
ATOM   5496 C CG  . GLU C 3 93  ? -42.291 27.409 60.491  1.00 42.39  ? 93  GLU C CG  1 
ATOM   5497 C CD  . GLU C 3 93  ? -43.526 27.146 61.310  1.00 41.70  ? 93  GLU C CD  1 
ATOM   5498 O OE1 . GLU C 3 93  ? -44.049 28.114 61.894  1.00 48.89  ? 93  GLU C OE1 1 
ATOM   5499 O OE2 . GLU C 3 93  ? -43.959 25.976 61.393  1.00 53.81  ? 93  GLU C OE2 1 
ATOM   5500 N N   . TRP C 3 94  ? -41.934 28.851 56.102  1.00 34.26  ? 94  TRP C N   1 
ATOM   5501 C CA  . TRP C 3 94  ? -42.420 29.593 54.951  1.00 35.74  ? 94  TRP C CA  1 
ATOM   5502 C C   . TRP C 3 94  ? -43.605 28.843 54.354  1.00 37.17  ? 94  TRP C C   1 
ATOM   5503 O O   . TRP C 3 94  ? -43.501 27.629 54.104  1.00 39.06  ? 94  TRP C O   1 
ATOM   5504 C CB  . TRP C 3 94  ? -41.334 29.796 53.892  1.00 33.52  ? 94  TRP C CB  1 
ATOM   5505 C CG  . TRP C 3 94  ? -41.780 30.738 52.831  1.00 35.02  ? 94  TRP C CG  1 
ATOM   5506 C CD1 . TRP C 3 94  ? -42.567 30.448 51.752  1.00 37.73  ? 94  TRP C CD1 1 
ATOM   5507 C CD2 . TRP C 3 94  ? -41.497 32.138 52.757  1.00 31.62  ? 94  TRP C CD2 1 
ATOM   5508 N NE1 . TRP C 3 94  ? -42.781 31.579 51.006  1.00 37.04  ? 94  TRP C NE1 1 
ATOM   5509 C CE2 . TRP C 3 94  ? -42.136 32.631 51.602  1.00 31.44  ? 94  TRP C CE2 1 
ATOM   5510 C CE3 . TRP C 3 94  ? -40.763 33.022 53.553  1.00 34.06  ? 94  TRP C CE3 1 
ATOM   5511 C CZ2 . TRP C 3 94  ? -42.062 33.963 51.222  1.00 33.57  ? 94  TRP C CZ2 1 
ATOM   5512 C CZ3 . TRP C 3 94  ? -40.690 34.349 53.174  1.00 34.50  ? 94  TRP C CZ3 1 
ATOM   5513 C CH2 . TRP C 3 94  ? -41.338 34.808 52.019  1.00 37.02  ? 94  TRP C CH2 1 
ATOM   5514 N N   . PRO C 3 95  ? -44.746 29.515 54.092  1.00 36.96  ? 95  PRO C N   1 
ATOM   5515 C CA  . PRO C 3 95  ? -45.068 30.945 54.285  1.00 39.01  ? 95  PRO C CA  1 
ATOM   5516 C C   . PRO C 3 95  ? -44.850 31.461 55.709  1.00 33.62  ? 95  PRO C C   1 
ATOM   5517 O O   . PRO C 3 95  ? -45.089 30.751 56.679  1.00 36.58  ? 95  PRO C O   1 
ATOM   5518 C CB  . PRO C 3 95  ? -46.553 31.013 53.892  1.00 36.98  ? 95  PRO C CB  1 
ATOM   5519 C CG  . PRO C 3 95  ? -46.716 29.919 52.896  1.00 37.38  ? 95  PRO C CG  1 
ATOM   5520 C CD  . PRO C 3 95  ? -45.853 28.807 53.427  1.00 38.37  ? 95  PRO C CD  1 
ATOM   5521 N N   . PRO C 3 96  ? -44.382 32.702 55.827  1.00 35.68  ? 96  PRO C N   1 
ATOM   5522 C CA  . PRO C 3 96  ? -43.983 33.234 57.139  1.00 38.72  ? 96  PRO C CA  1 
ATOM   5523 C C   . PRO C 3 96  ? -45.064 33.087 58.202  1.00 36.18  ? 96  PRO C C   1 
ATOM   5524 O O   . PRO C 3 96  ? -46.237 33.383 57.973  1.00 37.05  ? 96  PRO C O   1 
ATOM   5525 C CB  . PRO C 3 96  ? -43.683 34.713 56.847  1.00 37.41  ? 96  PRO C CB  1 
ATOM   5526 C CG  . PRO C 3 96  ? -44.039 34.948 55.393  1.00 40.20  ? 96  PRO C CG  1 
ATOM   5527 C CD  . PRO C 3 96  ? -44.034 33.615 54.726  1.00 33.25  ? 96  PRO C CD  1 
ATOM   5528 N N   . ARG C 3 97  ? -44.656 32.608 59.376  1.00 38.40  ? 97  ARG C N   1 
ATOM   5529 C CA  . ARG C 3 97  ? -45.509 32.567 60.566  1.00 39.96  ? 97  ARG C CA  1 
ATOM   5530 C C   . ARG C 3 97  ? -44.721 33.070 61.770  1.00 37.24  ? 97  ARG C C   1 
ATOM   5531 O O   . ARG C 3 97  ? -44.584 32.365 62.775  1.00 36.08  ? 97  ARG C O   1 
ATOM   5532 C CB  . ARG C 3 97  ? -46.021 31.150 60.821  1.00 43.23  ? 97  ARG C CB  1 
ATOM   5533 C CG  . ARG C 3 97  ? -47.221 30.757 59.994  1.00 52.30  ? 97  ARG C CG  1 
ATOM   5534 C CD  . ARG C 3 97  ? -47.159 29.285 59.631  1.00 48.15  ? 97  ARG C CD  1 
ATOM   5535 N NE  . ARG C 3 97  ? -48.435 28.803 59.114  1.00 60.96  ? 97  ARG C NE  1 
ATOM   5536 C CZ  . ARG C 3 97  ? -49.146 27.825 59.659  1.00 63.34  ? 97  ARG C CZ  1 
ATOM   5537 N NH1 . ARG C 3 97  ? -48.728 27.187 60.743  1.00 62.90  ? 97  ARG C NH1 1 
ATOM   5538 N NH2 . ARG C 3 97  ? -50.306 27.480 59.106  1.00 62.33  ? 97  ARG C NH2 1 
ATOM   5539 N N   . PRO C 3 98  ? -44.197 34.295 61.707  1.00 40.35  ? 98  PRO C N   1 
ATOM   5540 C CA  . PRO C 3 98  ? -43.275 34.753 62.757  1.00 34.21  ? 98  PRO C CA  1 
ATOM   5541 C C   . PRO C 3 98  ? -43.952 34.860 64.118  1.00 38.19  ? 98  PRO C C   1 
ATOM   5542 O O   . PRO C 3 98  ? -45.157 35.105 64.223  1.00 33.50  ? 98  PRO C O   1 
ATOM   5543 C CB  . PRO C 3 98  ? -42.815 36.130 62.259  1.00 33.15  ? 98  PRO C CB  1 
ATOM   5544 C CG  . PRO C 3 98  ? -43.452 36.344 60.922  1.00 38.99  ? 98  PRO C CG  1 
ATOM   5545 C CD  . PRO C 3 98  ? -44.575 35.380 60.789  1.00 34.67  ? 98  PRO C CD  1 
ATOM   5546 N N   . THR C 3 99  ? -43.154 34.660 65.167  1.00 32.37  ? 99  THR C N   1 
ATOM   5547 C CA  . THR C 3 99  ? -43.574 34.904 66.540  1.00 36.88  ? 99  THR C CA  1 
ATOM   5548 C C   . THR C 3 99  ? -42.430 35.564 67.298  1.00 33.34  ? 99  THR C C   1 
ATOM   5549 O O   . THR C 3 99  ? -41.260 35.425 66.939  1.00 33.86  ? 99  THR C O   1 
ATOM   5550 C CB  . THR C 3 99  ? -43.997 33.618 67.268  1.00 35.11  ? 99  THR C CB  1 
ATOM   5551 O OG1 . THR C 3 99  ? -42.893 32.703 67.316  1.00 35.09  ? 99  THR C OG1 1 
ATOM   5552 C CG2 . THR C 3 99  ? -45.183 32.966 66.578  1.00 28.86  ? 99  THR C CG2 1 
ATOM   5553 N N   . PHE C 3 100 ? -42.783 36.287 68.356  1.00 37.73  ? 100 PHE C N   1 
ATOM   5554 C CA  . PHE C 3 100 ? -41.821 36.996 69.188  1.00 30.77  ? 100 PHE C CA  1 
ATOM   5555 C C   . PHE C 3 100 ? -41.736 36.355 70.566  1.00 35.34  ? 100 PHE C C   1 
ATOM   5556 O O   . PHE C 3 100 ? -42.713 35.793 71.071  1.00 36.27  ? 100 PHE C O   1 
ATOM   5557 C CB  . PHE C 3 100 ? -42.210 38.467 69.378  1.00 29.39  ? 100 PHE C CB  1 
ATOM   5558 C CG  . PHE C 3 100 ? -42.189 39.286 68.121  1.00 32.32  ? 100 PHE C CG  1 
ATOM   5559 C CD1 . PHE C 3 100 ? -43.216 39.194 67.196  1.00 32.23  ? 100 PHE C CD1 1 
ATOM   5560 C CD2 . PHE C 3 100 ? -41.162 40.182 67.885  1.00 31.11  ? 100 PHE C CD2 1 
ATOM   5561 C CE1 . PHE C 3 100 ? -43.203 39.963 66.050  1.00 32.81  ? 100 PHE C CE1 1 
ATOM   5562 C CE2 . PHE C 3 100 ? -41.144 40.954 66.738  1.00 30.58  ? 100 PHE C CE2 1 
ATOM   5563 C CZ  . PHE C 3 100 ? -42.168 40.849 65.822  1.00 25.87  ? 100 PHE C CZ  1 
ATOM   5564 N N   . GLY C 3 101 ? -40.568 36.470 71.186  1.00 35.65  ? 101 GLY C N   1 
ATOM   5565 C CA  . GLY C 3 101 ? -40.467 36.222 72.606  1.00 35.24  ? 101 GLY C CA  1 
ATOM   5566 C C   . GLY C 3 101 ? -41.184 37.295 73.404  1.00 33.25  ? 101 GLY C C   1 
ATOM   5567 O O   . GLY C 3 101 ? -41.585 38.342 72.891  1.00 35.50  ? 101 GLY C O   1 
ATOM   5568 N N   . GLY C 3 102 ? -41.349 37.022 74.697  1.00 33.38  ? 102 GLY C N   1 
ATOM   5569 C CA  . GLY C 3 102 ? -42.059 37.932 75.577  1.00 31.29  ? 102 GLY C CA  1 
ATOM   5570 C C   . GLY C 3 102 ? -41.286 39.159 76.008  1.00 36.64  ? 102 GLY C C   1 
ATOM   5571 O O   . GLY C 3 102 ? -41.862 40.032 76.665  1.00 38.98  ? 102 GLY C O   1 
ATOM   5572 N N   . GLY C 3 103 ? -40.008 39.241 75.673  1.00 34.88  ? 103 GLY C N   1 
ATOM   5573 C CA  . GLY C 3 103 ? -39.216 40.423 75.946  1.00 34.48  ? 103 GLY C CA  1 
ATOM   5574 C C   . GLY C 3 103 ? -38.426 40.326 77.242  1.00 36.99  ? 103 GLY C C   1 
ATOM   5575 O O   . GLY C 3 103 ? -38.839 39.684 78.214  1.00 34.88  ? 103 GLY C O   1 
ATOM   5576 N N   . THR C 3 104 ? -37.260 40.974 77.252  1.00 38.97  ? 104 THR C N   1 
ATOM   5577 C CA  . THR C 3 104 ? -36.440 41.148 78.444  1.00 34.18  ? 104 THR C CA  1 
ATOM   5578 C C   . THR C 3 104 ? -36.261 42.640 78.670  1.00 39.50  ? 104 THR C C   1 
ATOM   5579 O O   . THR C 3 104 ? -35.820 43.358 77.764  1.00 35.18  ? 104 THR C O   1 
ATOM   5580 C CB  . THR C 3 104 ? -35.076 40.467 78.301  1.00 34.39  ? 104 THR C CB  1 
ATOM   5581 O OG1 . THR C 3 104 ? -35.240 39.044 78.297  1.00 36.74  ? 104 THR C OG1 1 
ATOM   5582 C CG2 . THR C 3 104 ? -34.165 40.869 79.456  1.00 34.67  ? 104 THR C CG2 1 
ATOM   5583 N N   . LYS C 3 105 ? -36.621 43.110 79.862  1.00 40.77  ? 105 LYS C N   1 
ATOM   5584 C CA  . LYS C 3 105 ? -36.461 44.515 80.213  1.00 41.11  ? 105 LYS C CA  1 
ATOM   5585 C C   . LYS C 3 105 ? -35.077 44.716 80.814  1.00 45.05  ? 105 LYS C C   1 
ATOM   5586 O O   . LYS C 3 105 ? -34.720 44.057 81.797  1.00 41.17  ? 105 LYS C O   1 
ATOM   5587 C CB  . LYS C 3 105 ? -37.542 44.973 81.191  1.00 41.70  ? 105 LYS C CB  1 
ATOM   5588 C CG  . LYS C 3 105 ? -37.606 46.490 81.354  1.00 43.97  ? 105 LYS C CG  1 
ATOM   5589 C CD  . LYS C 3 105 ? -38.851 46.921 82.108  1.00 52.92  ? 105 LYS C CD  1 
ATOM   5590 C CE  . LYS C 3 105 ? -38.909 48.432 82.267  1.00 55.50  ? 105 LYS C CE  1 
ATOM   5591 N NZ  . LYS C 3 105 ? -40.129 49.009 81.635  1.00 57.30  ? 105 LYS C NZ  1 
ATOM   5592 N N   . VAL C 3 106 ? -34.300 45.619 80.222  1.00 40.90  ? 106 VAL C N   1 
ATOM   5593 C CA  . VAL C 3 106 ? -32.960 45.941 80.696  1.00 43.94  ? 106 VAL C CA  1 
ATOM   5594 C C   . VAL C 3 106 ? -33.030 47.300 81.377  1.00 42.14  ? 106 VAL C C   1 
ATOM   5595 O O   . VAL C 3 106 ? -33.269 48.325 80.725  1.00 45.98  ? 106 VAL C O   1 
ATOM   5596 C CB  . VAL C 3 106 ? -31.931 45.937 79.557  1.00 43.08  ? 106 VAL C CB  1 
ATOM   5597 C CG1 . VAL C 3 106 ? -30.586 46.429 80.060  1.00 37.26  ? 106 VAL C CG1 1 
ATOM   5598 C CG2 . VAL C 3 106 ? -31.805 44.545 78.969  1.00 33.87  ? 106 VAL C CG2 1 
ATOM   5599 N N   . GLU C 3 107 ? -32.830 47.310 82.689  1.00 46.28  ? 107 GLU C N   1 
ATOM   5600 C CA  . GLU C 3 107 ? -32.788 48.533 83.474  1.00 46.73  ? 107 GLU C CA  1 
ATOM   5601 C C   . GLU C 3 107 ? -31.355 48.806 83.915  1.00 44.18  ? 107 GLU C C   1 
ATOM   5602 O O   . GLU C 3 107 ? -30.533 47.890 84.022  1.00 43.52  ? 107 GLU C O   1 
ATOM   5603 C CB  . GLU C 3 107 ? -33.721 48.434 84.685  1.00 48.85  ? 107 GLU C CB  1 
ATOM   5604 C CG  . GLU C 3 107 ? -35.186 48.219 84.293  1.00 56.07  ? 107 GLU C CG  1 
ATOM   5605 C CD  . GLU C 3 107 ? -36.106 48.019 85.484  1.00 64.83  ? 107 GLU C CD  1 
ATOM   5606 O OE1 . GLU C 3 107 ? -36.910 48.934 85.770  1.00 74.04  ? 107 GLU C OE1 1 
ATOM   5607 O OE2 . GLU C 3 107 ? -36.027 46.945 86.126  1.00 59.59  ? 107 GLU C OE2 1 
ATOM   5608 N N   . ILE C 3 108 ? -31.049 50.074 84.152  1.00 45.35  ? 108 ILE C N   1 
ATOM   5609 C CA  . ILE C 3 108 ? -29.690 50.495 84.477  1.00 47.85  ? 108 ILE C CA  1 
ATOM   5610 C C   . ILE C 3 108 ? -29.592 50.743 85.978  1.00 45.94  ? 108 ILE C C   1 
ATOM   5611 O O   . ILE C 3 108 ? -30.392 51.497 86.548  1.00 44.26  ? 108 ILE C O   1 
ATOM   5612 C CB  . ILE C 3 108 ? -29.283 51.749 83.678  1.00 47.69  ? 108 ILE C CB  1 
ATOM   5613 C CG1 . ILE C 3 108 ? -28.759 51.397 82.276  1.00 47.07  ? 108 ILE C CG1 1 
ATOM   5614 C CG2 . ILE C 3 108 ? -28.198 52.516 84.413  1.00 49.99  ? 108 ILE C CG2 1 
ATOM   5615 C CD1 . ILE C 3 108 ? -29.575 50.403 81.484  1.00 45.21  ? 108 ILE C CD1 1 
ATOM   5616 N N   . LYS C 3 109 ? -28.620 50.106 86.624  1.00 47.14  ? 109 LYS C N   1 
ATOM   5617 C CA  . LYS C 3 109 ? -28.336 50.403 88.021  1.00 50.56  ? 109 LYS C CA  1 
ATOM   5618 C C   . LYS C 3 109 ? -27.595 51.728 88.137  1.00 48.46  ? 109 LYS C C   1 
ATOM   5619 O O   . LYS C 3 109 ? -26.777 52.085 87.283  1.00 46.65  ? 109 LYS C O   1 
ATOM   5620 C CB  . LYS C 3 109 ? -27.497 49.296 88.663  1.00 51.74  ? 109 LYS C CB  1 
ATOM   5621 C CG  . LYS C 3 109 ? -28.250 48.010 88.947  1.00 53.15  ? 109 LYS C CG  1 
ATOM   5622 C CD  . LYS C 3 109 ? -27.319 46.955 89.523  1.00 50.10  ? 109 LYS C CD  1 
ATOM   5623 C CE  . LYS C 3 109 ? -28.102 45.788 90.117  1.00 62.32  ? 109 LYS C CE  1 
ATOM   5624 N NZ  . LYS C 3 109 ? -29.423 46.231 90.670  1.00 58.69  ? 109 LYS C NZ  1 
ATOM   5625 N N   . ARG C 3 110 ? -27.888 52.459 89.208  1.00 45.20  ? 110 ARG C N   1 
ATOM   5626 C CA  . ARG C 3 110 ? -27.181 53.695 89.513  1.00 45.66  ? 110 ARG C CA  1 
ATOM   5627 C C   . ARG C 3 110 ? -27.256 53.937 91.015  1.00 44.32  ? 110 ARG C C   1 
ATOM   5628 O O   . ARG C 3 110 ? -27.902 53.187 91.753  1.00 47.64  ? 110 ARG C O   1 
ATOM   5629 C CB  . ARG C 3 110 ? -27.754 54.877 88.722  1.00 42.21  ? 110 ARG C CB  1 
ATOM   5630 C CG  . ARG C 3 110 ? -29.228 55.146 88.978  1.00 42.65  ? 110 ARG C CG  1 
ATOM   5631 C CD  . ARG C 3 110 ? -29.526 56.634 88.936  1.00 41.00  ? 110 ARG C CD  1 
ATOM   5632 N NE  . ARG C 3 110 ? -28.868 57.321 90.040  1.00 49.32  ? 110 ARG C NE  1 
ATOM   5633 C CZ  . ARG C 3 110 ? -28.324 58.528 89.960  1.00 45.49  ? 110 ARG C CZ  1 
ATOM   5634 N NH1 . ARG C 3 110 ? -28.364 59.232 88.841  1.00 43.78  ? 110 ARG C NH1 1 
ATOM   5635 N NH2 . ARG C 3 110 ? -27.729 59.042 91.032  1.00 51.91  ? 110 ARG C NH2 1 
ATOM   5636 N N   . THR C 3 111 ? -26.589 54.993 91.469  1.00 45.29  ? 111 THR C N   1 
ATOM   5637 C CA  . THR C 3 111 ? -26.590 55.307 92.887  1.00 43.79  ? 111 THR C CA  1 
ATOM   5638 C C   . THR C 3 111 ? -27.923 55.916 93.306  1.00 45.84  ? 111 THR C C   1 
ATOM   5639 O O   . THR C 3 111 ? -28.662 56.488 92.497  1.00 45.55  ? 111 THR C O   1 
ATOM   5640 C CB  . THR C 3 111 ? -25.460 56.270 93.238  1.00 38.75  ? 111 THR C CB  1 
ATOM   5641 O OG1 . THR C 3 111 ? -25.637 57.493 92.514  1.00 41.79  ? 111 THR C OG1 1 
ATOM   5642 C CG2 . THR C 3 111 ? -24.112 55.656 92.902  1.00 41.21  ? 111 THR C CG2 1 
ATOM   5643 N N   . VAL C 3 112 ? -28.222 55.776 94.599  1.00 44.42  ? 112 VAL C N   1 
ATOM   5644 C CA  . VAL C 3 112 ? -29.428 56.355 95.172  1.00 43.02  ? 112 VAL C CA  1 
ATOM   5645 C C   . VAL C 3 112 ? -29.460 57.850 94.898  1.00 46.23  ? 112 VAL C C   1 
ATOM   5646 O O   . VAL C 3 112 ? -28.435 58.536 94.961  1.00 43.77  ? 112 VAL C O   1 
ATOM   5647 C CB  . VAL C 3 112 ? -29.487 56.049 96.681  1.00 48.86  ? 112 VAL C CB  1 
ATOM   5648 C CG1 . VAL C 3 112 ? -30.632 56.802 97.354  1.00 49.88  ? 112 VAL C CG1 1 
ATOM   5649 C CG2 . VAL C 3 112 ? -29.617 54.548 96.909  1.00 43.71  ? 112 VAL C CG2 1 
ATOM   5650 N N   . ALA C 3 113 ? -30.645 58.358 94.567  1.00 46.74  ? 113 ALA C N   1 
ATOM   5651 C CA  . ALA C 3 113 ? -30.832 59.780 94.306  1.00 48.14  ? 113 ALA C CA  1 
ATOM   5652 C C   . ALA C 3 113 ? -32.159 60.218 94.905  1.00 50.85  ? 113 ALA C C   1 
ATOM   5653 O O   . ALA C 3 113 ? -33.196 59.607 94.631  1.00 50.38  ? 113 ALA C O   1 
ATOM   5654 C CB  . ALA C 3 113 ? -30.795 60.081 92.803  1.00 44.53  ? 113 ALA C CB  1 
ATOM   5655 N N   . ALA C 3 114 ? -32.122 61.264 95.722  1.00 56.17  ? 114 ALA C N   1 
ATOM   5656 C CA  . ALA C 3 114 ? -33.330 61.742 96.382  1.00 57.99  ? 114 ALA C CA  1 
ATOM   5657 C C   . ALA C 3 114 ? -34.178 62.560 95.408  1.00 56.50  ? 114 ALA C C   1 
ATOM   5658 O O   . ALA C 3 114 ? -33.638 63.268 94.553  1.00 53.33  ? 114 ALA C O   1 
ATOM   5659 C CB  . ALA C 3 114 ? -32.977 62.589 97.603  1.00 59.90  ? 114 ALA C CB  1 
ATOM   5660 N N   . PRO C 3 115 ? -35.501 62.477 95.507  1.00 57.64  ? 115 PRO C N   1 
ATOM   5661 C CA  . PRO C 3 115 ? -36.354 63.260 94.611  1.00 60.57  ? 115 PRO C CA  1 
ATOM   5662 C C   . PRO C 3 115 ? -36.414 64.723 95.014  1.00 57.58  ? 115 PRO C C   1 
ATOM   5663 O O   . PRO C 3 115 ? -36.365 65.079 96.193  1.00 63.52  ? 115 PRO C O   1 
ATOM   5664 C CB  . PRO C 3 115 ? -37.731 62.601 94.759  1.00 56.52  ? 115 PRO C CB  1 
ATOM   5665 C CG  . PRO C 3 115 ? -37.706 61.944 96.092  1.00 56.07  ? 115 PRO C CG  1 
ATOM   5666 C CD  . PRO C 3 115 ? -36.276 61.630 96.433  1.00 54.15  ? 115 PRO C CD  1 
ATOM   5667 N N   . SER C 3 116 ? -36.511 65.577 94.004  1.00 57.02  ? 116 SER C N   1 
ATOM   5668 C CA  . SER C 3 116 ? -36.879 66.969 94.206  1.00 61.36  ? 116 SER C CA  1 
ATOM   5669 C C   . SER C 3 116 ? -38.398 67.053 94.160  1.00 62.49  ? 116 SER C C   1 
ATOM   5670 O O   . SER C 3 116 ? -39.014 66.625 93.178  1.00 66.98  ? 116 SER C O   1 
ATOM   5671 C CB  . SER C 3 116 ? -36.249 67.867 93.142  1.00 62.10  ? 116 SER C CB  1 
ATOM   5672 O OG  . SER C 3 116 ? -34.895 67.515 92.914  1.00 71.99  ? 116 SER C OG  1 
ATOM   5673 N N   . VAL C 3 117 ? -39.001 67.580 95.218  1.00 60.27  ? 117 VAL C N   1 
ATOM   5674 C CA  . VAL C 3 117 ? -40.451 67.583 95.358  1.00 57.31  ? 117 VAL C CA  1 
ATOM   5675 C C   . VAL C 3 117 ? -40.984 68.969 95.029  1.00 58.64  ? 117 VAL C C   1 
ATOM   5676 O O   . VAL C 3 117 ? -40.398 69.989 95.417  1.00 55.64  ? 117 VAL C O   1 
ATOM   5677 C CB  . VAL C 3 117 ? -40.875 67.137 96.770  1.00 58.95  ? 117 VAL C CB  1 
ATOM   5678 C CG1 . VAL C 3 117 ? -42.390 67.070 96.876  1.00 53.54  ? 117 VAL C CG1 1 
ATOM   5679 C CG2 . VAL C 3 117 ? -40.260 65.781 97.095  1.00 55.27  ? 117 VAL C CG2 1 
ATOM   5680 N N   . PHE C 3 118 ? -42.085 69.001 94.282  1.00 56.32  ? 118 PHE C N   1 
ATOM   5681 C CA  . PHE C 3 118 ? -42.780 70.225 93.924  1.00 56.05  ? 118 PHE C CA  1 
ATOM   5682 C C   . PHE C 3 118 ? -44.272 69.979 94.076  1.00 55.76  ? 118 PHE C C   1 
ATOM   5683 O O   . PHE C 3 118 ? -44.754 68.880 93.791  1.00 55.17  ? 118 PHE C O   1 
ATOM   5684 C CB  . PHE C 3 118 ? -42.482 70.680 92.480  1.00 59.01  ? 118 PHE C CB  1 
ATOM   5685 C CG  . PHE C 3 118 ? -41.026 70.590 92.075  1.00 58.73  ? 118 PHE C CG  1 
ATOM   5686 C CD1 . PHE C 3 118 ? -40.403 69.366 91.864  1.00 57.60  ? 118 PHE C CD1 1 
ATOM   5687 C CD2 . PHE C 3 118 ? -40.286 71.745 91.891  1.00 62.03  ? 118 PHE C CD2 1 
ATOM   5688 C CE1 . PHE C 3 118 ? -39.072 69.304 91.493  1.00 61.68  ? 118 PHE C CE1 1 
ATOM   5689 C CE2 . PHE C 3 118 ? -38.958 71.693 91.517  1.00 65.66  ? 118 PHE C CE2 1 
ATOM   5690 C CZ  . PHE C 3 118 ? -38.348 70.471 91.319  1.00 66.86  ? 118 PHE C CZ  1 
ATOM   5691 N N   . ILE C 3 119 ? -45.003 70.998 94.514  1.00 57.24  ? 119 ILE C N   1 
ATOM   5692 C CA  . ILE C 3 119 ? -46.451 70.912 94.649  1.00 58.93  ? 119 ILE C CA  1 
ATOM   5693 C C   . ILE C 3 119 ? -47.083 72.004 93.797  1.00 56.44  ? 119 ILE C C   1 
ATOM   5694 O O   . ILE C 3 119 ? -46.594 73.139 93.755  1.00 60.26  ? 119 ILE C O   1 
ATOM   5695 C CB  . ILE C 3 119 ? -46.904 71.013 96.124  1.00 57.61  ? 119 ILE C CB  1 
ATOM   5696 C CG1 . ILE C 3 119 ? -48.417 70.819 96.239  1.00 56.48  ? 119 ILE C CG1 1 
ATOM   5697 C CG2 . ILE C 3 119 ? -46.482 72.333 96.743  1.00 63.49  ? 119 ILE C CG2 1 
ATOM   5698 C CD1 . ILE C 3 119 ? -48.828 69.923 97.384  1.00 64.27  ? 119 ILE C CD1 1 
ATOM   5699 N N   . PHE C 3 120 ? -48.154 71.647 93.094  1.00 54.54  ? 120 PHE C N   1 
ATOM   5700 C CA  . PHE C 3 120 ? -48.860 72.564 92.212  1.00 57.37  ? 120 PHE C CA  1 
ATOM   5701 C C   . PHE C 3 120 ? -50.286 72.731 92.712  1.00 60.01  ? 120 PHE C C   1 
ATOM   5702 O O   . PHE C 3 120 ? -51.041 71.741 92.755  1.00 60.50  ? 120 PHE C O   1 
ATOM   5703 C CB  . PHE C 3 120 ? -48.861 72.049 90.768  1.00 53.90  ? 120 PHE C CB  1 
ATOM   5704 C CG  . PHE C 3 120 ? -47.501 72.020 90.131  1.00 56.04  ? 120 PHE C CG  1 
ATOM   5705 C CD1 . PHE C 3 120 ? -47.005 73.137 89.474  1.00 53.46  ? 120 PHE C CD1 1 
ATOM   5706 C CD2 . PHE C 3 120 ? -46.723 70.874 90.179  1.00 49.90  ? 120 PHE C CD2 1 
ATOM   5707 C CE1 . PHE C 3 120 ? -45.758 73.115 88.878  1.00 50.37  ? 120 PHE C CE1 1 
ATOM   5708 C CE2 . PHE C 3 120 ? -45.473 70.848 89.587  1.00 57.00  ? 120 PHE C CE2 1 
ATOM   5709 C CZ  . PHE C 3 120 ? -44.990 71.972 88.935  1.00 51.76  ? 120 PHE C CZ  1 
ATOM   5710 N N   . PRO C 3 121 ? -50.708 73.934 93.088  1.00 61.58  ? 121 PRO C N   1 
ATOM   5711 C CA  . PRO C 3 121 ? -52.108 74.139 93.494  1.00 62.04  ? 121 PRO C CA  1 
ATOM   5712 C C   . PRO C 3 121 ? -53.025 74.041 92.288  1.00 56.20  ? 121 PRO C C   1 
ATOM   5713 O O   . PRO C 3 121 ? -52.553 74.058 91.140  1.00 59.33  ? 121 PRO C O   1 
ATOM   5714 C CB  . PRO C 3 121 ? -52.106 75.556 94.084  1.00 58.56  ? 121 PRO C CB  1 
ATOM   5715 C CG  . PRO C 3 121 ? -50.880 76.224 93.548  1.00 62.11  ? 121 PRO C CG  1 
ATOM   5716 C CD  . PRO C 3 121 ? -49.954 75.192 92.972  1.00 61.16  ? 121 PRO C CD  1 
ATOM   5717 N N   . PRO C 3 122 ? -54.336 73.923 92.492  1.00 59.03  ? 122 PRO C N   1 
ATOM   5718 C CA  . PRO C 3 122 ? -55.243 73.912 91.338  1.00 63.01  ? 122 PRO C CA  1 
ATOM   5719 C C   . PRO C 3 122 ? -55.203 75.247 90.614  1.00 62.00  ? 122 PRO C C   1 
ATOM   5720 O O   . PRO C 3 122 ? -55.095 76.308 91.232  1.00 65.00  ? 122 PRO C O   1 
ATOM   5721 C CB  . PRO C 3 122 ? -56.625 73.642 91.947  1.00 61.51  ? 122 PRO C CB  1 
ATOM   5722 C CG  . PRO C 3 122 ? -56.433 73.469 93.407  1.00 61.80  ? 122 PRO C CG  1 
ATOM   5723 C CD  . PRO C 3 122 ? -55.036 73.802 93.782  1.00 63.40  ? 122 PRO C CD  1 
ATOM   5724 N N   . SER C 3 123 ? -55.270 75.185 89.289  1.00 62.35  ? 123 SER C N   1 
ATOM   5725 C CA  . SER C 3 123 ? -55.308 76.403 88.495  1.00 59.28  ? 123 SER C CA  1 
ATOM   5726 C C   . SER C 3 123 ? -56.682 77.062 88.597  1.00 63.25  ? 123 SER C C   1 
ATOM   5727 O O   . SER C 3 123 ? -57.705 76.398 88.798  1.00 64.40  ? 123 SER C O   1 
ATOM   5728 C CB  . SER C 3 123 ? -54.957 76.097 87.037  1.00 50.64  ? 123 SER C CB  1 
ATOM   5729 O OG  . SER C 3 123 ? -56.087 75.650 86.315  1.00 53.19  ? 123 SER C OG  1 
ATOM   5730 N N   . ASP C 3 124 ? -56.696 78.392 88.473  1.00 62.66  ? 124 ASP C N   1 
ATOM   5731 C CA  . ASP C 3 124 ? -57.950 79.130 88.591  1.00 65.34  ? 124 ASP C CA  1 
ATOM   5732 C C   . ASP C 3 124 ? -58.891 78.829 87.431  1.00 60.60  ? 124 ASP C C   1 
ATOM   5733 O O   . ASP C 3 124 ? -60.112 78.953 87.576  1.00 66.02  ? 124 ASP C O   1 
ATOM   5734 C CB  . ASP C 3 124 ? -57.672 80.632 88.683  1.00 64.59  ? 124 ASP C CB  1 
ATOM   5735 N N   . GLU C 3 125 ? -58.349 78.435 86.279  1.00 56.55  ? 125 GLU C N   1 
ATOM   5736 C CA  . GLU C 3 125 ? -59.205 78.001 85.180  1.00 63.86  ? 125 GLU C CA  1 
ATOM   5737 C C   . GLU C 3 125 ? -59.949 76.723 85.540  1.00 63.93  ? 125 GLU C C   1 
ATOM   5738 O O   . GLU C 3 125 ? -61.156 76.610 85.295  1.00 65.98  ? 125 GLU C O   1 
ATOM   5739 C CB  . GLU C 3 125 ? -58.373 77.799 83.916  1.00 60.33  ? 125 GLU C CB  1 
ATOM   5740 C CG  . GLU C 3 125 ? -57.263 78.819 83.748  1.00 62.22  ? 125 GLU C CG  1 
ATOM   5741 C CD  . GLU C 3 125 ? -56.726 78.862 82.334  1.00 76.06  ? 125 GLU C CD  1 
ATOM   5742 O OE1 . GLU C 3 125 ? -55.621 79.416 82.133  1.00 75.61  ? 125 GLU C OE1 1 
ATOM   5743 O OE2 . GLU C 3 125 ? -57.412 78.340 81.425  1.00 74.10  ? 125 GLU C OE2 1 
ATOM   5744 N N   . GLN C 3 126 ? -59.246 75.750 86.126  1.00 61.59  ? 126 GLN C N   1 
ATOM   5745 C CA  . GLN C 3 126 ? -59.905 74.517 86.539  1.00 60.92  ? 126 GLN C CA  1 
ATOM   5746 C C   . GLN C 3 126 ? -60.967 74.788 87.594  1.00 66.56  ? 126 GLN C C   1 
ATOM   5747 O O   . GLN C 3 126 ? -62.058 74.207 87.551  1.00 66.71  ? 126 GLN C O   1 
ATOM   5748 C CB  . GLN C 3 126 ? -58.874 73.514 87.061  1.00 56.51  ? 126 GLN C CB  1 
ATOM   5749 C CG  . GLN C 3 126 ? -59.423 72.101 87.188  1.00 52.13  ? 126 GLN C CG  1 
ATOM   5750 C CD  . GLN C 3 126 ? -58.552 71.196 88.037  1.00 56.94  ? 126 GLN C CD  1 
ATOM   5751 O OE1 . GLN C 3 126 ? -57.559 71.632 88.620  1.00 61.00  ? 126 GLN C OE1 1 
ATOM   5752 N NE2 . GLN C 3 126 ? -58.919 69.923 88.106  1.00 53.74  ? 126 GLN C NE2 1 
ATOM   5753 N N   . LEU C 3 127 ? -60.669 75.678 88.544  1.00 68.40  ? 127 LEU C N   1 
ATOM   5754 C CA  . LEU C 3 127 ? -61.606 75.965 89.625  1.00 70.03  ? 127 LEU C CA  1 
ATOM   5755 C C   . LEU C 3 127 ? -62.882 76.634 89.132  1.00 68.49  ? 127 LEU C C   1 
ATOM   5756 O O   . LEU C 3 127 ? -63.905 76.565 89.822  1.00 70.85  ? 127 LEU C O   1 
ATOM   5757 C CB  . LEU C 3 127 ? -60.928 76.836 90.683  1.00 67.69  ? 127 LEU C CB  1 
ATOM   5758 C CG  . LEU C 3 127 ? -59.931 76.078 91.558  1.00 62.45  ? 127 LEU C CG  1 
ATOM   5759 C CD1 . LEU C 3 127 ? -58.968 77.035 92.238  1.00 60.88  ? 127 LEU C CD1 1 
ATOM   5760 C CD2 . LEU C 3 127 ? -60.676 75.238 92.577  1.00 60.34  ? 127 LEU C CD2 1 
ATOM   5761 N N   . LYS C 3 128 ? -62.848 77.286 87.967  1.00 65.01  ? 128 LYS C N   1 
ATOM   5762 C CA  . LYS C 3 128 ? -64.086 77.787 87.375  1.00 69.97  ? 128 LYS C CA  1 
ATOM   5763 C C   . LYS C 3 128 ? -65.058 76.644 87.108  1.00 75.22  ? 128 LYS C C   1 
ATOM   5764 O O   . LYS C 3 128 ? -66.260 76.764 87.374  1.00 78.40  ? 128 LYS C O   1 
ATOM   5765 C CB  . LYS C 3 128 ? -63.786 78.558 86.090  1.00 62.11  ? 128 LYS C CB  1 
ATOM   5766 C CG  . LYS C 3 128 ? -63.319 79.988 86.324  1.00 59.16  ? 128 LYS C CG  1 
ATOM   5767 N N   . SER C 3 129 ? -64.556 75.528 86.586  1.00 71.43  ? 129 SER C N   1 
ATOM   5768 C CA  . SER C 3 129 ? -65.326 74.297 86.578  1.00 68.89  ? 129 SER C CA  1 
ATOM   5769 C C   . SER C 3 129 ? -65.369 73.708 87.989  1.00 70.20  ? 129 SER C C   1 
ATOM   5770 O O   . SER C 3 129 ? -64.716 74.193 88.917  1.00 73.35  ? 129 SER C O   1 
ATOM   5771 C CB  . SER C 3 129 ? -64.733 73.300 85.582  1.00 72.81  ? 129 SER C CB  1 
ATOM   5772 O OG  . SER C 3 129 ? -63.519 72.751 86.067  1.00 69.14  ? 129 SER C OG  1 
ATOM   5773 N N   . GLY C 3 130 ? -66.144 72.644 88.151  1.00 62.28  ? 130 GLY C N   1 
ATOM   5774 C CA  . GLY C 3 130 ? -66.415 72.165 89.491  1.00 67.44  ? 130 GLY C CA  1 
ATOM   5775 C C   . GLY C 3 130 ? -65.331 71.370 90.185  1.00 66.14  ? 130 GLY C C   1 
ATOM   5776 O O   . GLY C 3 130 ? -65.590 70.836 91.266  1.00 62.78  ? 130 GLY C O   1 
ATOM   5777 N N   . THR C 3 131 ? -64.122 71.279 89.628  1.00 66.33  ? 131 THR C N   1 
ATOM   5778 C CA  . THR C 3 131 ? -63.111 70.363 90.140  1.00 64.84  ? 131 THR C CA  1 
ATOM   5779 C C   . THR C 3 131 ? -61.805 71.097 90.415  1.00 65.02  ? 131 THR C C   1 
ATOM   5780 O O   . THR C 3 131 ? -61.448 72.051 89.718  1.00 62.87  ? 131 THR C O   1 
ATOM   5781 C CB  . THR C 3 131 ? -62.868 69.205 89.152  1.00 60.16  ? 131 THR C CB  1 
ATOM   5782 O OG1 . THR C 3 131 ? -64.096 68.500 88.935  1.00 63.81  ? 131 THR C OG1 1 
ATOM   5783 C CG2 . THR C 3 131 ? -61.833 68.228 89.695  1.00 60.77  ? 131 THR C CG2 1 
ATOM   5784 N N   . ALA C 3 132 ? -61.107 70.648 91.458  1.00 61.35  ? 132 ALA C N   1 
ATOM   5785 C CA  . ALA C 3 132 ? -59.764 71.105 91.787  1.00 60.91  ? 132 ALA C CA  1 
ATOM   5786 C C   . ALA C 3 132 ? -58.815 69.913 91.801  1.00 60.24  ? 132 ALA C C   1 
ATOM   5787 O O   . ALA C 3 132 ? -59.090 68.904 92.460  1.00 59.94  ? 132 ALA C O   1 
ATOM   5788 C CB  . ALA C 3 132 ? -59.743 71.814 93.144  1.00 59.23  ? 132 ALA C CB  1 
ATOM   5789 N N   . SER C 3 133 ? -57.700 70.029 91.082  1.00 54.61  ? 133 SER C N   1 
ATOM   5790 C CA  . SER C 3 133 ? -56.669 68.999 91.066  1.00 50.67  ? 133 SER C CA  1 
ATOM   5791 C C   . SER C 3 133 ? -55.378 69.569 91.634  1.00 53.24  ? 133 SER C C   1 
ATOM   5792 O O   . SER C 3 133 ? -54.920 70.631 91.203  1.00 57.49  ? 133 SER C O   1 
ATOM   5793 C CB  . SER C 3 133 ? -56.430 68.467 89.651  1.00 49.67  ? 133 SER C CB  1 
ATOM   5794 O OG  . SER C 3 133 ? -57.617 67.926 89.096  1.00 52.98  ? 133 SER C OG  1 
ATOM   5795 N N   . VAL C 3 134 ? -54.800 68.865 92.601  1.00 52.83  ? 134 VAL C N   1 
ATOM   5796 C CA  . VAL C 3 134 ? -53.519 69.226 93.197  1.00 52.99  ? 134 VAL C CA  1 
ATOM   5797 C C   . VAL C 3 134 ? -52.485 68.232 92.694  1.00 48.86  ? 134 VAL C C   1 
ATOM   5798 O O   . VAL C 3 134 ? -52.721 67.019 92.726  1.00 49.32  ? 134 VAL C O   1 
ATOM   5799 C CB  . VAL C 3 134 ? -53.590 69.222 94.735  1.00 58.46  ? 134 VAL C CB  1 
ATOM   5800 C CG1 . VAL C 3 134 ? -52.329 69.836 95.327  1.00 57.95  ? 134 VAL C CG1 1 
ATOM   5801 C CG2 . VAL C 3 134 ? -54.836 69.957 95.214  1.00 51.81  ? 134 VAL C CG2 1 
ATOM   5802 N N   . VAL C 3 135 ? -51.345 68.739 92.228  1.00 49.08  ? 135 VAL C N   1 
ATOM   5803 C CA  . VAL C 3 135 ? -50.321 67.919 91.592  1.00 50.63  ? 135 VAL C CA  1 
ATOM   5804 C C   . VAL C 3 135 ? -49.047 67.977 92.426  1.00 52.76  ? 135 VAL C C   1 
ATOM   5805 O O   . VAL C 3 135 ? -48.571 69.065 92.769  1.00 48.80  ? 135 VAL C O   1 
ATOM   5806 C CB  . VAL C 3 135 ? -50.050 68.376 90.146  1.00 54.58  ? 135 VAL C CB  1 
ATOM   5807 C CG1 . VAL C 3 135 ? -49.005 67.485 89.491  1.00 47.54  ? 135 VAL C CG1 1 
ATOM   5808 C CG2 . VAL C 3 135 ? -51.343 68.377 89.336  1.00 47.33  ? 135 VAL C CG2 1 
ATOM   5809 N N   . CYS C 3 136 ? -48.497 66.805 92.741  1.00 51.12  ? 136 CYS C N   1 
ATOM   5810 C CA  . CYS C 3 136 ? -47.242 66.679 93.472  1.00 52.97  ? 136 CYS C CA  1 
ATOM   5811 C C   . CYS C 3 136 ? -46.239 65.963 92.581  1.00 54.05  ? 136 CYS C C   1 
ATOM   5812 O O   . CYS C 3 136 ? -46.488 64.833 92.147  1.00 53.80  ? 136 CYS C O   1 
ATOM   5813 C CB  . CYS C 3 136 ? -47.439 65.921 94.787  1.00 58.96  ? 136 CYS C CB  1 
ATOM   5814 S SG  . CYS C 3 136 ? -45.973 65.835 95.845  1.00 64.66  ? 136 CYS C SG  1 
ATOM   5815 N N   . LEU C 3 137 ? -45.111 66.616 92.315  1.00 51.49  ? 137 LEU C N   1 
ATOM   5816 C CA  . LEU C 3 137 ? -44.108 66.112 91.387  1.00 48.68  ? 137 LEU C CA  1 
ATOM   5817 C C   . LEU C 3 137 ? -42.853 65.687 92.139  1.00 53.95  ? 137 LEU C C   1 
ATOM   5818 O O   . LEU C 3 137 ? -42.308 66.454 92.941  1.00 53.15  ? 137 LEU C O   1 
ATOM   5819 C CB  . LEU C 3 137 ? -43.765 67.171 90.336  1.00 52.83  ? 137 LEU C CB  1 
ATOM   5820 C CG  . LEU C 3 137 ? -42.518 66.950 89.475  1.00 54.79  ? 137 LEU C CG  1 
ATOM   5821 C CD1 . LEU C 3 137 ? -42.652 65.704 88.602  1.00 46.03  ? 137 LEU C CD1 1 
ATOM   5822 C CD2 . LEU C 3 137 ? -42.243 68.181 88.619  1.00 49.07  ? 137 LEU C CD2 1 
ATOM   5823 N N   . LEU C 3 138 ? -42.408 64.462 91.875  1.00 46.57  ? 138 LEU C N   1 
ATOM   5824 C CA  . LEU C 3 138 ? -41.132 63.937 92.347  1.00 48.10  ? 138 LEU C CA  1 
ATOM   5825 C C   . LEU C 3 138 ? -40.316 63.627 91.104  1.00 52.29  ? 138 LEU C C   1 
ATOM   5826 O O   . LEU C 3 138 ? -40.652 62.698 90.364  1.00 56.41  ? 138 LEU C O   1 
ATOM   5827 C CB  . LEU C 3 138 ? -41.314 62.668 93.181  1.00 50.90  ? 138 LEU C CB  1 
ATOM   5828 C CG  . LEU C 3 138 ? -42.087 62.553 94.496  1.00 55.16  ? 138 LEU C CG  1 
ATOM   5829 C CD1 . LEU C 3 138 ? -43.534 63.019 94.388  1.00 54.73  ? 138 LEU C CD1 1 
ATOM   5830 C CD2 . LEU C 3 138 ? -42.050 61.094 94.902  1.00 52.66  ? 138 LEU C CD2 1 
ATOM   5831 N N   . ASN C 3 139 ? -39.258 64.390 90.852  1.00 54.40  ? 139 ASN C N   1 
ATOM   5832 C CA  . ASN C 3 139 ? -38.487 64.173 89.636  1.00 64.65  ? 139 ASN C CA  1 
ATOM   5833 C C   . ASN C 3 139 ? -37.035 63.847 89.963  1.00 58.23  ? 139 ASN C C   1 
ATOM   5834 O O   . ASN C 3 139 ? -36.467 64.365 90.930  1.00 54.34  ? 139 ASN C O   1 
ATOM   5835 C CB  . ASN C 3 139 ? -38.595 65.378 88.669  1.00 60.30  ? 139 ASN C CB  1 
ATOM   5836 C CG  . ASN C 3 139 ? -37.522 66.412 88.885  1.00 63.54  ? 139 ASN C CG  1 
ATOM   5837 O OD1 . ASN C 3 139 ? -37.286 66.856 90.006  1.00 69.51  ? 139 ASN C OD1 1 
ATOM   5838 N ND2 . ASN C 3 139 ? -36.856 66.803 87.802  1.00 65.47  ? 139 ASN C ND2 1 
ATOM   5839 N N   . ASN C 3 140 ? -36.476 62.928 89.173  1.00 53.90  ? 140 ASN C N   1 
ATOM   5840 C CA  . ASN C 3 140 ? -35.065 62.560 89.181  1.00 55.55  ? 140 ASN C CA  1 
ATOM   5841 C C   . ASN C 3 140 ? -34.646 61.851 90.464  1.00 51.04  ? 140 ASN C C   1 
ATOM   5842 O O   . ASN C 3 140 ? -33.689 62.261 91.127  1.00 50.97  ? 140 ASN C O   1 
ATOM   5843 C CB  . ASN C 3 140 ? -34.197 63.797 88.934  1.00 58.16  ? 140 ASN C CB  1 
ATOM   5844 C CG  . ASN C 3 140 ? -34.388 64.364 87.536  1.00 63.23  ? 140 ASN C CG  1 
ATOM   5845 O OD1 . ASN C 3 140 ? -35.036 63.747 86.687  1.00 57.27  ? 140 ASN C OD1 1 
ATOM   5846 N ND2 . ASN C 3 140 ? -33.825 65.541 87.291  1.00 70.06  ? 140 ASN C ND2 1 
ATOM   5847 N N   . PHE C 3 141 ? -35.330 60.761 90.801  1.00 49.04  ? 141 PHE C N   1 
ATOM   5848 C CA  . PHE C 3 141 ? -34.962 59.943 91.944  1.00 53.42  ? 141 PHE C CA  1 
ATOM   5849 C C   . PHE C 3 141 ? -34.646 58.519 91.499  1.00 51.30  ? 141 PHE C C   1 
ATOM   5850 O O   . PHE C 3 141 ? -35.052 58.074 90.421  1.00 44.39  ? 141 PHE C O   1 
ATOM   5851 C CB  . PHE C 3 141 ? -36.070 59.930 93.012  1.00 49.50  ? 141 PHE C CB  1 
ATOM   5852 C CG  . PHE C 3 141 ? -37.391 59.397 92.524  1.00 45.22  ? 141 PHE C CG  1 
ATOM   5853 C CD1 . PHE C 3 141 ? -38.328 60.246 91.956  1.00 48.19  ? 141 PHE C CD1 1 
ATOM   5854 C CD2 . PHE C 3 141 ? -37.704 58.052 92.654  1.00 44.89  ? 141 PHE C CD2 1 
ATOM   5855 C CE1 . PHE C 3 141 ? -39.551 59.762 91.511  1.00 49.73  ? 141 PHE C CE1 1 
ATOM   5856 C CE2 . PHE C 3 141 ? -38.923 57.560 92.212  1.00 47.52  ? 141 PHE C CE2 1 
ATOM   5857 C CZ  . PHE C 3 141 ? -39.849 58.418 91.641  1.00 45.41  ? 141 PHE C CZ  1 
ATOM   5858 N N   . TYR C 3 142 ? -33.900 57.811 92.358  1.00 46.53  ? 142 TYR C N   1 
ATOM   5859 C CA  . TYR C 3 142 ? -33.553 56.407 92.187  1.00 46.66  ? 142 TYR C CA  1 
ATOM   5860 C C   . TYR C 3 142 ? -33.287 55.788 93.556  1.00 53.35  ? 142 TYR C C   1 
ATOM   5861 O O   . TYR C 3 142 ? -32.583 56.391 94.381  1.00 48.00  ? 142 TYR C O   1 
ATOM   5862 C CB  . TYR C 3 142 ? -32.333 56.245 91.278  1.00 45.84  ? 142 TYR C CB  1 
ATOM   5863 C CG  . TYR C 3 142 ? -32.054 54.809 90.901  1.00 46.39  ? 142 TYR C CG  1 
ATOM   5864 C CD1 . TYR C 3 142 ? -32.688 54.222 89.814  1.00 50.00  ? 142 TYR C CD1 1 
ATOM   5865 C CD2 . TYR C 3 142 ? -31.177 54.029 91.648  1.00 49.02  ? 142 TYR C CD2 1 
ATOM   5866 C CE1 . TYR C 3 142 ? -32.445 52.903 89.469  1.00 48.46  ? 142 TYR C CE1 1 
ATOM   5867 C CE2 . TYR C 3 142 ? -30.928 52.707 91.310  1.00 45.59  ? 142 TYR C CE2 1 
ATOM   5868 C CZ  . TYR C 3 142 ? -31.568 52.152 90.221  1.00 46.79  ? 142 TYR C CZ  1 
ATOM   5869 O OH  . TYR C 3 142 ? -31.329 50.844 89.876  1.00 50.22  ? 142 TYR C OH  1 
ATOM   5870 N N   . PRO C 3 143 ? -33.803 54.579 93.838  1.00 52.89  ? 143 PRO C N   1 
ATOM   5871 C CA  . PRO C 3 143 ? -34.530 53.666 92.942  1.00 51.01  ? 143 PRO C CA  1 
ATOM   5872 C C   . PRO C 3 143 ? -35.994 54.038 92.734  1.00 49.04  ? 143 PRO C C   1 
ATOM   5873 O O   . PRO C 3 143 ? -36.457 55.084 93.182  1.00 50.82  ? 143 PRO C O   1 
ATOM   5874 C CB  . PRO C 3 143 ? -34.381 52.314 93.651  1.00 52.26  ? 143 PRO C CB  1 
ATOM   5875 C CG  . PRO C 3 143 ? -34.367 52.674 95.113  1.00 58.99  ? 143 PRO C CG  1 
ATOM   5876 C CD  . PRO C 3 143 ? -33.710 54.038 95.208  1.00 55.89  ? 143 PRO C CD  1 
ATOM   5877 N N   . ARG C 3 144 ? -36.734 53.163 92.047  1.00 50.24  ? 144 ARG C N   1 
ATOM   5878 C CA  . ARG C 3 144 ? -38.064 53.519 91.559  1.00 54.49  ? 144 ARG C CA  1 
ATOM   5879 C C   . ARG C 3 144 ? -39.096 53.567 92.679  1.00 56.03  ? 144 ARG C C   1 
ATOM   5880 O O   . ARG C 3 144 ? -40.067 54.328 92.592  1.00 50.63  ? 144 ARG C O   1 
ATOM   5881 C CB  . ARG C 3 144 ? -38.504 52.523 90.484  1.00 53.14  ? 144 ARG C CB  1 
ATOM   5882 C CG  . ARG C 3 144 ? -39.888 52.772 89.893  1.00 58.52  ? 144 ARG C CG  1 
ATOM   5883 C CD  . ARG C 3 144 ? -40.275 51.612 88.971  1.00 65.40  ? 144 ARG C CD  1 
ATOM   5884 N NE  . ARG C 3 144 ? -41.644 51.592 88.449  1.00 74.14  ? 144 ARG C NE  1 
ATOM   5885 C CZ  . ARG C 3 144 ? -42.762 51.874 89.114  1.00 71.22  ? 144 ARG C CZ  1 
ATOM   5886 N NH1 . ARG C 3 144 ? -42.751 52.230 90.391  1.00 66.46  ? 144 ARG C NH1 1 
ATOM   5887 N NH2 . ARG C 3 144 ? -43.929 51.779 88.482  1.00 72.76  ? 144 ARG C NH2 1 
ATOM   5888 N N   . GLU C 3 145 ? -38.907 52.776 93.732  1.00 59.50  ? 145 GLU C N   1 
ATOM   5889 C CA  . GLU C 3 145 ? -39.902 52.668 94.792  1.00 58.33  ? 145 GLU C CA  1 
ATOM   5890 C C   . GLU C 3 145 ? -39.933 53.943 95.625  1.00 55.21  ? 145 GLU C C   1 
ATOM   5891 O O   . GLU C 3 145 ? -38.941 54.305 96.265  1.00 56.05  ? 145 GLU C O   1 
ATOM   5892 C CB  . GLU C 3 145 ? -39.609 51.453 95.668  1.00 58.82  ? 145 GLU C CB  1 
ATOM   5893 C CG  . GLU C 3 145 ? -39.615 50.126 94.904  1.00 62.13  ? 145 GLU C CG  1 
ATOM   5894 C CD  . GLU C 3 145 ? -38.319 49.858 94.147  1.00 63.54  ? 145 GLU C CD  1 
ATOM   5895 O OE1 . GLU C 3 145 ? -37.425 50.732 94.150  1.00 60.72  ? 145 GLU C OE1 1 
ATOM   5896 O OE2 . GLU C 3 145 ? -38.200 48.772 93.539  1.00 63.47  ? 145 GLU C OE2 1 
ATOM   5897 N N   . ALA C 3 146 ? -41.076 54.625 95.605  1.00 56.81  ? 146 ALA C N   1 
ATOM   5898 C CA  . ALA C 3 146 ? -41.303 55.820 96.399  1.00 54.36  ? 146 ALA C CA  1 
ATOM   5899 C C   . ALA C 3 146 ? -42.746 55.809 96.883  1.00 55.61  ? 146 ALA C C   1 
ATOM   5900 O O   . ALA C 3 146 ? -43.594 55.095 96.343  1.00 57.05  ? 146 ALA C O   1 
ATOM   5901 C CB  . ALA C 3 146 ? -41.015 57.097 95.599  1.00 50.92  ? 146 ALA C CB  1 
ATOM   5902 N N   . LYS C 3 147 ? -43.021 56.602 97.915  1.00 51.50  ? 147 LYS C N   1 
ATOM   5903 C CA  . LYS C 3 147 ? -44.368 56.688 98.464  1.00 55.89  ? 147 LYS C CA  1 
ATOM   5904 C C   . LYS C 3 147 ? -44.716 58.144 98.705  1.00 54.35  ? 147 LYS C C   1 
ATOM   5905 O O   . LYS C 3 147 ? -43.987 58.853 99.406  1.00 60.32  ? 147 LYS C O   1 
ATOM   5906 C CB  . LYS C 3 147 ? -44.499 55.897 99.771  1.00 56.42  ? 147 LYS C CB  1 
ATOM   5907 N N   . VAL C 3 148 ? -45.822 58.587 98.119  1.00 53.72  ? 148 VAL C N   1 
ATOM   5908 C CA  . VAL C 3 148 ? -46.376 59.907 98.384  1.00 55.75  ? 148 VAL C CA  1 
ATOM   5909 C C   . VAL C 3 148 ? -47.674 59.718 99.156  1.00 58.28  ? 148 VAL C C   1 
ATOM   5910 O O   . VAL C 3 148 ? -48.446 58.788 98.887  1.00 59.97  ? 148 VAL C O   1 
ATOM   5911 C CB  . VAL C 3 148 ? -46.584 60.723 97.088  1.00 56.97  ? 148 VAL C CB  1 
ATOM   5912 C CG1 . VAL C 3 148 ? -45.509 60.377 96.069  1.00 51.48  ? 148 VAL C CG1 1 
ATOM   5913 C CG2 . VAL C 3 148 ? -47.975 60.517 96.494  1.00 58.94  ? 148 VAL C CG2 1 
ATOM   5914 N N   . GLN C 3 149 ? -47.884 60.571 100.155 1.00 59.22  ? 149 GLN C N   1 
ATOM   5915 C CA  . GLN C 3 149 ? -49.078 60.535 100.988 1.00 58.11  ? 149 GLN C CA  1 
ATOM   5916 C C   . GLN C 3 149 ? -49.677 61.928 100.993 1.00 57.17  ? 149 GLN C C   1 
ATOM   5917 O O   . GLN C 3 149 ? -48.994 62.895 101.345 1.00 61.14  ? 149 GLN C O   1 
ATOM   5918 C CB  . GLN C 3 149 ? -48.753 60.079 102.414 1.00 56.17  ? 149 GLN C CB  1 
ATOM   5919 N N   . TRP C 3 150 ? -50.937 62.035 100.588 1.00 54.94  ? 150 TRP C N   1 
ATOM   5920 C CA  . TRP C 3 150 ? -51.625 63.316 100.563 1.00 57.04  ? 150 TRP C CA  1 
ATOM   5921 C C   . TRP C 3 150 ? -52.233 63.585 101.934 1.00 64.81  ? 150 TRP C C   1 
ATOM   5922 O O   . TRP C 3 150 ? -52.985 62.758 102.461 1.00 62.09  ? 150 TRP C O   1 
ATOM   5923 C CB  . TRP C 3 150 ? -52.707 63.334 99.484  1.00 56.37  ? 150 TRP C CB  1 
ATOM   5924 C CG  . TRP C 3 150 ? -52.186 63.525 98.079  1.00 56.47  ? 150 TRP C CG  1 
ATOM   5925 C CD1 . TRP C 3 150 ? -52.071 62.567 97.114  1.00 52.60  ? 150 TRP C CD1 1 
ATOM   5926 C CD2 . TRP C 3 150 ? -51.723 64.749 97.484  1.00 52.41  ? 150 TRP C CD2 1 
ATOM   5927 N NE1 . TRP C 3 150 ? -51.563 63.114 95.960  1.00 57.33  ? 150 TRP C NE1 1 
ATOM   5928 C CE2 . TRP C 3 150 ? -51.341 64.451 96.160  1.00 55.56  ? 150 TRP C CE2 1 
ATOM   5929 C CE3 . TRP C 3 150 ? -51.592 66.065 97.944  1.00 56.45  ? 150 TRP C CE3 1 
ATOM   5930 C CZ2 . TRP C 3 150 ? -50.839 65.421 95.285  1.00 56.15  ? 150 TRP C CZ2 1 
ATOM   5931 C CZ3 . TRP C 3 150 ? -51.095 67.029 97.074  1.00 59.68  ? 150 TRP C CZ3 1 
ATOM   5932 C CH2 . TRP C 3 150 ? -50.723 66.701 95.760  1.00 55.49  ? 150 TRP C CH2 1 
ATOM   5933 N N   . LYS C 3 151 ? -51.888 64.732 102.513 1.00 64.93  ? 151 LYS C N   1 
ATOM   5934 C CA  . LYS C 3 151 ? -52.395 65.148 103.816 1.00 64.71  ? 151 LYS C CA  1 
ATOM   5935 C C   . LYS C 3 151 ? -53.105 66.482 103.639 1.00 67.99  ? 151 LYS C C   1 
ATOM   5936 O O   . LYS C 3 151 ? -52.457 67.516 103.441 1.00 65.73  ? 151 LYS C O   1 
ATOM   5937 C CB  . LYS C 3 151 ? -51.268 65.255 104.844 1.00 65.29  ? 151 LYS C CB  1 
ATOM   5938 N N   . VAL C 3 152 ? -54.431 66.455 103.691 1.00 74.09  ? 152 VAL C N   1 
ATOM   5939 C CA  . VAL C 3 152 ? -55.248 67.661 103.677 1.00 77.18  ? 152 VAL C CA  1 
ATOM   5940 C C   . VAL C 3 152 ? -55.630 67.953 105.121 1.00 76.92  ? 152 VAL C C   1 
ATOM   5941 O O   . VAL C 3 152 ? -56.394 67.200 105.735 1.00 78.94  ? 152 VAL C O   1 
ATOM   5942 C CB  . VAL C 3 152 ? -56.489 67.500 102.788 1.00 73.97  ? 152 VAL C CB  1 
ATOM   5943 C CG1 . VAL C 3 152 ? -57.419 68.699 102.951 1.00 70.62  ? 152 VAL C CG1 1 
ATOM   5944 C CG2 . VAL C 3 152 ? -56.082 67.316 101.333 1.00 63.56  ? 152 VAL C CG2 1 
ATOM   5945 N N   . ASP C 3 153 ? -55.083 69.038 105.671 1.00 76.76  ? 153 ASP C N   1 
ATOM   5946 C CA  . ASP C 3 153 ? -55.291 69.416 107.069 1.00 76.98  ? 153 ASP C CA  1 
ATOM   5947 C C   . ASP C 3 153 ? -54.842 68.298 108.014 1.00 81.42  ? 153 ASP C C   1 
ATOM   5948 O O   . ASP C 3 153 ? -55.608 67.792 108.838 1.00 84.33  ? 153 ASP C O   1 
ATOM   5949 C CB  . ASP C 3 153 ? -56.750 69.802 107.319 1.00 77.89  ? 153 ASP C CB  1 
ATOM   5950 C CG  . ASP C 3 153 ? -57.022 71.241 106.983 1.00 75.50  ? 153 ASP C CG  1 
ATOM   5951 O OD1 . ASP C 3 153 ? -56.090 72.064 107.116 1.00 72.48  ? 153 ASP C OD1 1 
ATOM   5952 O OD2 . ASP C 3 153 ? -58.161 71.561 106.582 1.00 72.76  ? 153 ASP C OD2 1 
ATOM   5953 N N   . ASN C 3 154 ? -53.576 67.905 107.859 1.00 79.15  ? 154 ASN C N   1 
ATOM   5954 C CA  . ASN C 3 154 ? -52.943 66.882 108.685 1.00 78.77  ? 154 ASN C CA  1 
ATOM   5955 C C   . ASN C 3 154 ? -53.721 65.571 108.686 1.00 79.17  ? 154 ASN C C   1 
ATOM   5956 O O   . ASN C 3 154 ? -53.393 64.654 109.446 1.00 82.11  ? 154 ASN C O   1 
ATOM   5957 C CB  . ASN C 3 154 ? -52.763 67.380 110.124 1.00 83.50  ? 154 ASN C CB  1 
ATOM   5958 C CG  . ASN C 3 154 ? -51.960 68.666 110.203 1.00 90.77  ? 154 ASN C CG  1 
ATOM   5959 O OD1 . ASN C 3 154 ? -52.082 69.430 111.162 1.00 94.00  ? 154 ASN C OD1 1 
ATOM   5960 N ND2 . ASN C 3 154 ? -51.132 68.911 109.191 1.00 88.47  ? 154 ASN C ND2 1 
ATOM   5961 N N   . ALA C 3 155 ? -54.741 65.466 107.839 1.00 77.09  ? 155 ALA C N   1 
ATOM   5962 C CA  . ALA C 3 155 ? -55.539 64.255 107.710 1.00 77.80  ? 155 ALA C CA  1 
ATOM   5963 C C   . ALA C 3 155 ? -55.110 63.523 106.446 1.00 74.44  ? 155 ALA C C   1 
ATOM   5964 O O   . ALA C 3 155 ? -55.237 64.062 105.340 1.00 74.17  ? 155 ALA C O   1 
ATOM   5965 C CB  . ALA C 3 155 ? -57.032 64.582 107.670 1.00 71.46  ? 155 ALA C CB  1 
ATOM   5966 N N   . LEU C 3 156 ? -54.590 62.310 106.614 1.00 70.47  ? 156 LEU C N   1 
ATOM   5967 C CA  . LEU C 3 156 ? -54.133 61.525 105.476 1.00 72.48  ? 156 LEU C CA  1 
ATOM   5968 C C   . LEU C 3 156 ? -55.312 61.132 104.595 1.00 70.92  ? 156 LEU C C   1 
ATOM   5969 O O   . LEU C 3 156 ? -56.368 60.724 105.087 1.00 69.14  ? 156 LEU C O   1 
ATOM   5970 C CB  . LEU C 3 156 ? -53.388 60.278 105.955 1.00 66.93  ? 156 LEU C CB  1 
ATOM   5971 N N   . GLN C 3 157 ? -55.125 61.260 103.286 1.00 62.59  ? 157 GLN C N   1 
ATOM   5972 C CA  . GLN C 3 157 ? -56.179 61.013 102.316 1.00 65.24  ? 157 GLN C CA  1 
ATOM   5973 C C   . GLN C 3 157 ? -56.008 59.647 101.662 1.00 61.01  ? 157 GLN C C   1 
ATOM   5974 O O   . GLN C 3 157 ? -54.921 59.065 101.650 1.00 68.24  ? 157 GLN C O   1 
ATOM   5975 C CB  . GLN C 3 157 ? -56.199 62.110 101.250 1.00 68.19  ? 157 GLN C CB  1 
ATOM   5976 C CG  . GLN C 3 157 ? -56.218 63.516 101.822 1.00 68.40  ? 157 GLN C CG  1 
ATOM   5977 C CD  . GLN C 3 157 ? -57.620 63.979 102.157 1.00 69.89  ? 157 GLN C CD  1 
ATOM   5978 O OE1 . GLN C 3 157 ? -58.409 64.300 101.269 1.00 70.92  ? 157 GLN C OE1 1 
ATOM   5979 N NE2 . GLN C 3 157 ? -57.941 64.007 103.444 1.00 69.81  ? 157 GLN C NE2 1 
ATOM   5980 N N   . SER C 3 158 ? -57.111 59.140 101.116 1.00 63.33  ? 158 SER C N   1 
ATOM   5981 C CA  . SER C 3 158 ? -57.119 57.842 100.458 1.00 63.22  ? 158 SER C CA  1 
ATOM   5982 C C   . SER C 3 158 ? -58.268 57.803 99.461  1.00 60.62  ? 158 SER C C   1 
ATOM   5983 O O   . SER C 3 158 ? -59.323 58.401 99.685  1.00 61.47  ? 158 SER C O   1 
ATOM   5984 C CB  . SER C 3 158 ? -57.249 56.700 101.472 1.00 67.84  ? 158 SER C CB  1 
ATOM   5985 O OG  . SER C 3 158 ? -57.796 55.543 100.865 1.00 77.49  ? 158 SER C OG  1 
ATOM   5986 N N   . GLY C 3 159 ? -58.043 57.098 98.353  1.00 62.76  ? 159 GLY C N   1 
ATOM   5987 C CA  . GLY C 3 159 ? -59.046 56.932 97.320  1.00 63.00  ? 159 GLY C CA  1 
ATOM   5988 C C   . GLY C 3 159 ? -59.304 58.140 96.447  1.00 58.58  ? 159 GLY C C   1 
ATOM   5989 O O   . GLY C 3 159 ? -60.072 58.028 95.485  1.00 59.13  ? 159 GLY C O   1 
ATOM   5990 N N   . ASN C 3 160 ? -58.697 59.291 96.741  1.00 58.70  ? 160 ASN C N   1 
ATOM   5991 C CA  . ASN C 3 160 ? -58.893 60.506 95.959  1.00 56.49  ? 160 ASN C CA  1 
ATOM   5992 C C   . ASN C 3 160 ? -57.629 60.925 95.216  1.00 58.58  ? 160 ASN C C   1 
ATOM   5993 O O   . ASN C 3 160 ? -57.487 62.099 94.851  1.00 51.61  ? 160 ASN C O   1 
ATOM   5994 C CB  . ASN C 3 160 ? -59.364 61.646 96.862  1.00 54.11  ? 160 ASN C CB  1 
ATOM   5995 C CG  . ASN C 3 160 ? -58.569 61.730 98.151  1.00 60.64  ? 160 ASN C CG  1 
ATOM   5996 O OD1 . ASN C 3 160 ? -57.483 61.152 98.268  1.00 60.75  ? 160 ASN C OD1 1 
ATOM   5997 N ND2 . ASN C 3 160 ? -59.085 62.483 99.113  1.00 62.62  ? 160 ASN C ND2 1 
ATOM   5998 N N   . SER C 3 161 ? -56.704 59.994 94.993  1.00 55.79  ? 161 SER C N   1 
ATOM   5999 C CA  . SER C 3 161 ? -55.421 60.317 94.395  1.00 50.05  ? 161 SER C CA  1 
ATOM   6000 C C   . SER C 3 161 ? -55.009 59.220 93.426  1.00 54.18  ? 161 SER C C   1 
ATOM   6001 O O   . SER C 3 161 ? -55.338 58.046 93.613  1.00 54.23  ? 161 SER C O   1 
ATOM   6002 C CB  . SER C 3 161 ? -54.339 60.506 95.464  1.00 50.79  ? 161 SER C CB  1 
ATOM   6003 O OG  . SER C 3 161 ? -53.698 59.278 95.753  1.00 55.30  ? 161 SER C OG  1 
ATOM   6004 N N   . GLN C 3 162 ? -54.291 59.621 92.378  1.00 47.55  ? 162 GLN C N   1 
ATOM   6005 C CA  . GLN C 3 162 ? -53.705 58.689 91.428  1.00 48.47  ? 162 GLN C CA  1 
ATOM   6006 C C   . GLN C 3 162 ? -52.309 59.165 91.055  1.00 52.63  ? 162 GLN C C   1 
ATOM   6007 O O   . GLN C 3 162 ? -52.008 60.362 91.103  1.00 47.51  ? 162 GLN C O   1 
ATOM   6008 C CB  . GLN C 3 162 ? -54.560 58.545 90.165  1.00 47.04  ? 162 GLN C CB  1 
ATOM   6009 C CG  . GLN C 3 162 ? -55.995 58.143 90.422  1.00 46.49  ? 162 GLN C CG  1 
ATOM   6010 C CD  . GLN C 3 162 ? -56.600 57.397 89.257  1.00 50.83  ? 162 GLN C CD  1 
ATOM   6011 O OE1 . GLN C 3 162 ? -57.401 57.949 88.505  1.00 54.47  ? 162 GLN C OE1 1 
ATOM   6012 N NE2 . GLN C 3 162 ? -56.217 56.133 89.096  1.00 52.87  ? 162 GLN C NE2 1 
ATOM   6013 N N   . GLU C 3 163 ? -51.460 58.213 90.674  1.00 52.07  ? 163 GLU C N   1 
ATOM   6014 C CA  . GLU C 3 163 ? -50.075 58.515 90.352  1.00 49.12  ? 163 GLU C CA  1 
ATOM   6015 C C   . GLU C 3 163 ? -49.599 57.625 89.215  1.00 47.51  ? 163 GLU C C   1 
ATOM   6016 O O   . GLU C 3 163 ? -50.169 56.567 88.938  1.00 45.62  ? 163 GLU C O   1 
ATOM   6017 C CB  . GLU C 3 163 ? -49.166 58.342 91.572  1.00 45.84  ? 163 GLU C CB  1 
ATOM   6018 C CG  . GLU C 3 163 ? -49.091 56.912 92.078  1.00 52.84  ? 163 GLU C CG  1 
ATOM   6019 C CD  . GLU C 3 163 ? -48.061 56.742 93.177  1.00 50.68  ? 163 GLU C CD  1 
ATOM   6020 O OE1 . GLU C 3 163 ? -48.040 57.577 94.106  1.00 54.81  ? 163 GLU C OE1 1 
ATOM   6021 O OE2 . GLU C 3 163 ? -47.272 55.776 93.108  1.00 50.64  ? 163 GLU C OE2 1 
ATOM   6022 N N   . SER C 3 164 ? -48.541 58.081 88.551  1.00 43.02  ? 164 SER C N   1 
ATOM   6023 C CA  . SER C 3 164 ? -47.886 57.317 87.503  1.00 46.02  ? 164 SER C CA  1 
ATOM   6024 C C   . SER C 3 164 ? -46.415 57.710 87.482  1.00 44.29  ? 164 SER C C   1 
ATOM   6025 O O   . SER C 3 164 ? -46.031 58.778 87.968  1.00 44.24  ? 164 SER C O   1 
ATOM   6026 C CB  . SER C 3 164 ? -48.554 57.543 86.138  1.00 41.75  ? 164 SER C CB  1 
ATOM   6027 O OG  . SER C 3 164 ? -48.088 58.733 85.525  1.00 46.11  ? 164 SER C OG  1 
ATOM   6028 N N   . VAL C 3 165 ? -45.590 56.824 86.929  1.00 44.07  ? 165 VAL C N   1 
ATOM   6029 C CA  . VAL C 3 165 ? -44.140 56.961 86.980  1.00 43.91  ? 165 VAL C CA  1 
ATOM   6030 C C   . VAL C 3 165 ? -43.586 56.902 85.565  1.00 45.14  ? 165 VAL C C   1 
ATOM   6031 O O   . VAL C 3 165 ? -44.002 56.059 84.763  1.00 47.01  ? 165 VAL C O   1 
ATOM   6032 C CB  . VAL C 3 165 ? -43.501 55.859 87.853  1.00 49.28  ? 165 VAL C CB  1 
ATOM   6033 C CG1 . VAL C 3 165 ? -42.009 56.104 88.027  1.00 48.63  ? 165 VAL C CG1 1 
ATOM   6034 C CG2 . VAL C 3 165 ? -44.196 55.777 89.204  1.00 50.72  ? 165 VAL C CG2 1 
ATOM   6035 N N   . THR C 3 166 ? -42.644 57.792 85.259  1.00 46.30  ? 166 THR C N   1 
ATOM   6036 C CA  . THR C 3 166 ? -41.957 57.731 83.978  1.00 43.89  ? 166 THR C CA  1 
ATOM   6037 C C   . THR C 3 166 ? -41.023 56.528 83.933  1.00 50.74  ? 166 THR C C   1 
ATOM   6038 O O   . THR C 3 166 ? -40.633 55.964 84.961  1.00 51.46  ? 166 THR C O   1 
ATOM   6039 C CB  . THR C 3 166 ? -41.140 58.995 83.721  1.00 44.60  ? 166 THR C CB  1 
ATOM   6040 O OG1 . THR C 3 166 ? -40.135 59.123 84.732  1.00 49.39  ? 166 THR C OG1 1 
ATOM   6041 C CG2 . THR C 3 166 ? -42.018 60.229 83.724  1.00 48.14  ? 166 THR C CG2 1 
ATOM   6042 N N   . GLU C 3 167 ? -40.662 56.139 82.716  1.00 50.87  ? 167 GLU C N   1 
ATOM   6043 C CA  . GLU C 3 167 ? -39.634 55.131 82.549  1.00 48.73  ? 167 GLU C CA  1 
ATOM   6044 C C   . GLU C 3 167 ? -38.268 55.743 82.841  1.00 45.75  ? 167 GLU C C   1 
ATOM   6045 O O   . GLU C 3 167 ? -38.122 56.958 82.995  1.00 50.46  ? 167 GLU C O   1 
ATOM   6046 C CB  . GLU C 3 167 ? -39.687 54.543 81.140  1.00 51.92  ? 167 GLU C CB  1 
ATOM   6047 C CG  . GLU C 3 167 ? -40.944 53.729 80.863  1.00 53.48  ? 167 GLU C CG  1 
ATOM   6048 C CD  . GLU C 3 167 ? -40.901 52.345 81.486  1.00 62.03  ? 167 GLU C CD  1 
ATOM   6049 O OE1 . GLU C 3 167 ? -39.851 51.973 82.061  1.00 66.67  ? 167 GLU C OE1 1 
ATOM   6050 O OE2 . GLU C 3 167 ? -41.924 51.630 81.402  1.00 61.18  ? 167 GLU C OE2 1 
ATOM   6051 N N   . GLN C 3 168 ? -37.257 54.884 82.925  1.00 49.81  ? 168 GLN C N   1 
ATOM   6052 C CA  . GLN C 3 168 ? -35.921 55.346 83.273  1.00 54.15  ? 168 GLN C CA  1 
ATOM   6053 C C   . GLN C 3 168 ? -35.410 56.348 82.242  1.00 50.34  ? 168 GLN C C   1 
ATOM   6054 O O   . GLN C 3 168 ? -35.608 56.183 81.036  1.00 52.81  ? 168 GLN C O   1 
ATOM   6055 C CB  . GLN C 3 168 ? -34.963 54.159 83.386  1.00 51.33  ? 168 GLN C CB  1 
ATOM   6056 C CG  . GLN C 3 168 ? -33.915 54.337 84.465  1.00 48.21  ? 168 GLN C CG  1 
ATOM   6057 C CD  . GLN C 3 168 ? -33.250 53.040 84.874  1.00 49.62  ? 168 GLN C CD  1 
ATOM   6058 O OE1 . GLN C 3 168 ? -33.532 51.978 84.320  1.00 56.48  ? 168 GLN C OE1 1 
ATOM   6059 N NE2 . GLN C 3 168 ? -32.358 53.120 85.854  1.00 50.70  ? 168 GLN C NE2 1 
ATOM   6060 N N   . ASP C 3 169 ? -34.764 57.402 82.728  1.00 48.12  ? 169 ASP C N   1 
ATOM   6061 C CA  . ASP C 3 169 ? -34.229 58.417 81.836  1.00 52.45  ? 169 ASP C CA  1 
ATOM   6062 C C   . ASP C 3 169 ? -32.974 57.904 81.134  1.00 58.35  ? 169 ASP C C   1 
ATOM   6063 O O   . ASP C 3 169 ? -32.206 57.108 81.684  1.00 54.57  ? 169 ASP C O   1 
ATOM   6064 C CB  . ASP C 3 169 ? -33.922 59.699 82.608  1.00 53.38  ? 169 ASP C CB  1 
ATOM   6065 C CG  . ASP C 3 169 ? -33.354 60.794 81.722  1.00 62.39  ? 169 ASP C CG  1 
ATOM   6066 O OD1 . ASP C 3 169 ? -34.130 61.375 80.930  1.00 63.81  ? 169 ASP C OD1 1 
ATOM   6067 O OD2 . ASP C 3 169 ? -32.136 61.070 81.814  1.00 60.41  ? 169 ASP C OD2 1 
ATOM   6068 N N   . SER C 3 170 ? -32.770 58.378 79.900  1.00 60.61  ? 170 SER C N   1 
ATOM   6069 C CA  . SER C 3 170 ? -31.710 57.829 79.059  1.00 56.47  ? 170 SER C CA  1 
ATOM   6070 C C   . SER C 3 170 ? -30.323 58.266 79.516  1.00 51.91  ? 170 SER C C   1 
ATOM   6071 O O   . SER C 3 170 ? -29.347 57.540 79.293  1.00 48.29  ? 170 SER C O   1 
ATOM   6072 C CB  . SER C 3 170 ? -31.941 58.226 77.598  1.00 42.65  ? 170 SER C CB  1 
ATOM   6073 N N   . LYS C 3 171 ? -30.207 59.429 80.158  1.00 51.63  ? 171 LYS C N   1 
ATOM   6074 C CA  . LYS C 3 171 ? -28.903 59.955 80.556  1.00 51.27  ? 171 LYS C CA  1 
ATOM   6075 C C   . LYS C 3 171 ? -28.556 59.662 82.012  1.00 53.60  ? 171 LYS C C   1 
ATOM   6076 O O   . LYS C 3 171 ? -27.494 59.098 82.287  1.00 55.33  ? 171 LYS C O   1 
ATOM   6077 C CB  . LYS C 3 171 ? -28.839 61.466 80.298  1.00 54.64  ? 171 LYS C CB  1 
ATOM   6078 N N   . ASP C 3 172 ? -29.427 60.024 82.955  1.00 51.66  ? 172 ASP C N   1 
ATOM   6079 C CA  . ASP C 3 172 ? -29.101 59.896 84.370  1.00 53.15  ? 172 ASP C CA  1 
ATOM   6080 C C   . ASP C 3 172 ? -29.730 58.675 85.035  1.00 53.35  ? 172 ASP C C   1 
ATOM   6081 O O   . ASP C 3 172 ? -29.454 58.423 86.214  1.00 53.80  ? 172 ASP C O   1 
ATOM   6082 C CB  . ASP C 3 172 ? -29.494 61.180 85.122  1.00 52.28  ? 172 ASP C CB  1 
ATOM   6083 C CG  . ASP C 3 172 ? -30.987 61.486 85.059  1.00 60.79  ? 172 ASP C CG  1 
ATOM   6084 O OD1 . ASP C 3 172 ? -31.777 60.623 84.620  1.00 60.77  ? 172 ASP C OD1 1 
ATOM   6085 O OD2 . ASP C 3 172 ? -31.375 62.609 85.454  1.00 61.80  ? 172 ASP C OD2 1 
ATOM   6086 N N   . SER C 3 173 ? -30.566 57.921 84.317  1.00 51.27  ? 173 SER C N   1 
ATOM   6087 C CA  . SER C 3 173 ? -31.159 56.671 84.796  1.00 46.39  ? 173 SER C CA  1 
ATOM   6088 C C   . SER C 3 173 ? -32.098 56.871 85.985  1.00 48.29  ? 173 SER C C   1 
ATOM   6089 O O   . SER C 3 173 ? -32.341 55.933 86.755  1.00 44.00  ? 173 SER C O   1 
ATOM   6090 C CB  . SER C 3 173 ? -30.079 55.644 85.154  1.00 41.20  ? 173 SER C CB  1 
ATOM   6091 O OG  . SER C 3 173 ? -29.101 55.559 84.134  1.00 50.67  ? 173 SER C OG  1 
ATOM   6092 N N   . THR C 3 174 ? -32.646 58.067 86.154  1.00 48.38  ? 174 THR C N   1 
ATOM   6093 C CA  . THR C 3 174 ? -33.558 58.314 87.257  1.00 50.61  ? 174 THR C CA  1 
ATOM   6094 C C   . THR C 3 174 ? -35.005 58.131 86.811  1.00 50.56  ? 174 THR C C   1 
ATOM   6095 O O   . THR C 3 174 ? -35.308 57.928 85.632  1.00 50.29  ? 174 THR C O   1 
ATOM   6096 C CB  . THR C 3 174 ? -33.362 59.720 87.826  1.00 50.74  ? 174 THR C CB  1 
ATOM   6097 O OG1 . THR C 3 174 ? -33.417 60.677 86.762  1.00 54.20  ? 174 THR C OG1 1 
ATOM   6098 C CG2 . THR C 3 174 ? -32.023 59.830 88.542  1.00 51.46  ? 174 THR C CG2 1 
ATOM   6099 N N   . TYR C 3 175 ? -35.902 58.194 87.785  1.00 45.71  ? 175 TYR C N   1 
ATOM   6100 C CA  . TYR C 3 175 ? -37.332 58.148 87.548  1.00 46.35  ? 175 TYR C CA  1 
ATOM   6101 C C   . TYR C 3 175 ? -37.962 59.447 88.020  1.00 48.11  ? 175 TYR C C   1 
ATOM   6102 O O   . TYR C 3 175 ? -37.407 60.170 88.855  1.00 45.98  ? 175 TYR C O   1 
ATOM   6103 C CB  . TYR C 3 175 ? -37.988 56.970 88.278  1.00 46.93  ? 175 TYR C CB  1 
ATOM   6104 C CG  . TYR C 3 175 ? -37.437 55.624 87.883  1.00 48.39  ? 175 TYR C CG  1 
ATOM   6105 C CD1 . TYR C 3 175 ? -37.947 54.938 86.790  1.00 50.94  ? 175 TYR C CD1 1 
ATOM   6106 C CD2 . TYR C 3 175 ? -36.407 55.039 88.603  1.00 46.94  ? 175 TYR C CD2 1 
ATOM   6107 C CE1 . TYR C 3 175 ? -37.445 53.705 86.426  1.00 53.44  ? 175 TYR C CE1 1 
ATOM   6108 C CE2 . TYR C 3 175 ? -35.898 53.808 88.247  1.00 52.27  ? 175 TYR C CE2 1 
ATOM   6109 C CZ  . TYR C 3 175 ? -36.421 53.146 87.158  1.00 52.32  ? 175 TYR C CZ  1 
ATOM   6110 O OH  . TYR C 3 175 ? -35.918 51.918 86.798  1.00 53.01  ? 175 TYR C OH  1 
ATOM   6111 N N   . SER C 3 176 ? -39.137 59.732 87.476  1.00 49.32  ? 176 SER C N   1 
ATOM   6112 C CA  . SER C 3 176 ? -39.975 60.810 87.968  1.00 48.00  ? 176 SER C CA  1 
ATOM   6113 C C   . SER C 3 176 ? -41.367 60.259 88.232  1.00 45.94  ? 176 SER C C   1 
ATOM   6114 O O   . SER C 3 176 ? -41.812 59.313 87.578  1.00 45.90  ? 176 SER C O   1 
ATOM   6115 C CB  . SER C 3 176 ? -40.037 61.982 86.980  1.00 48.41  ? 176 SER C CB  1 
ATOM   6116 O OG  . SER C 3 176 ? -38.783 62.636 86.901  1.00 48.76  ? 176 SER C OG  1 
ATOM   6117 N N   . LEU C 3 177 ? -42.042 60.850 89.212  1.00 49.98  ? 177 LEU C N   1 
ATOM   6118 C CA  . LEU C 3 177 ? -43.378 60.435 89.608  1.00 44.71  ? 177 LEU C CA  1 
ATOM   6119 C C   . LEU C 3 177 ? -44.277 61.657 89.675  1.00 47.91  ? 177 LEU C C   1 
ATOM   6120 O O   . LEU C 3 177 ? -43.850 62.729 90.114  1.00 46.18  ? 177 LEU C O   1 
ATOM   6121 C CB  . LEU C 3 177 ? -43.366 59.721 90.968  1.00 48.94  ? 177 LEU C CB  1 
ATOM   6122 C CG  . LEU C 3 177 ? -44.683 59.104 91.451  1.00 47.55  ? 177 LEU C CG  1 
ATOM   6123 C CD1 . LEU C 3 177 ? -44.418 57.808 92.195  1.00 44.30  ? 177 LEU C CD1 1 
ATOM   6124 C CD2 . LEU C 3 177 ? -45.461 60.075 92.328  1.00 43.84  ? 177 LEU C CD2 1 
ATOM   6125 N N   . SER C 3 178 ? -45.522 61.486 89.242  1.00 46.58  ? 178 SER C N   1 
ATOM   6126 C CA  . SER C 3 178 ? -46.529 62.534 89.318  1.00 48.41  ? 178 SER C CA  1 
ATOM   6127 C C   . SER C 3 178 ? -47.762 61.975 90.010  1.00 48.94  ? 178 SER C C   1 
ATOM   6128 O O   . SER C 3 178 ? -48.247 60.898 89.646  1.00 41.83  ? 178 SER C O   1 
ATOM   6129 C CB  . SER C 3 178 ? -46.893 63.065 87.926  1.00 45.81  ? 178 SER C CB  1 
ATOM   6130 O OG  . SER C 3 178 ? -47.894 64.067 88.009  1.00 39.88  ? 178 SER C OG  1 
ATOM   6131 N N   . SER C 3 179 ? -48.260 62.704 91.007  1.00 46.51  ? 179 SER C N   1 
ATOM   6132 C CA  . SER C 3 179 ? -49.465 62.321 91.728  1.00 49.42  ? 179 SER C CA  1 
ATOM   6133 C C   . SER C 3 179 ? -50.470 63.463 91.682  1.00 50.90  ? 179 SER C C   1 
ATOM   6134 O O   . SER C 3 179 ? -50.095 64.637 91.772  1.00 53.43  ? 179 SER C O   1 
ATOM   6135 C CB  . SER C 3 179 ? -49.154 61.948 93.181  1.00 48.32  ? 179 SER C CB  1 
ATOM   6136 O OG  . SER C 3 179 ? -50.348 61.668 93.892  1.00 54.37  ? 179 SER C OG  1 
ATOM   6137 N N   . THR C 3 180 ? -51.747 63.115 91.541  1.00 46.68  ? 180 THR C N   1 
ATOM   6138 C CA  . THR C 3 180 ? -52.822 64.094 91.451  1.00 48.33  ? 180 THR C CA  1 
ATOM   6139 C C   . THR C 3 180 ? -53.834 63.844 92.558  1.00 49.00  ? 180 THR C C   1 
ATOM   6140 O O   . THR C 3 180 ? -54.418 62.758 92.635  1.00 49.26  ? 180 THR C O   1 
ATOM   6141 C CB  . THR C 3 180 ? -53.509 64.044 90.085  1.00 46.46  ? 180 THR C CB  1 
ATOM   6142 O OG1 . THR C 3 180 ? -52.545 64.289 89.055  1.00 50.47  ? 180 THR C OG1 1 
ATOM   6143 C CG2 . THR C 3 180 ? -54.608 65.100 90.009  1.00 43.70  ? 180 THR C CG2 1 
ATOM   6144 N N   . LEU C 3 181 ? -54.038 64.851 93.406  1.00 52.90  ? 181 LEU C N   1 
ATOM   6145 C CA  . LEU C 3 181 ? -55.097 64.856 94.409  1.00 51.39  ? 181 LEU C CA  1 
ATOM   6146 C C   . LEU C 3 181 ? -56.277 65.627 93.825  1.00 51.93  ? 181 LEU C C   1 
ATOM   6147 O O   . LEU C 3 181 ? -56.171 66.832 93.570  1.00 52.78  ? 181 LEU C O   1 
ATOM   6148 C CB  . LEU C 3 181 ? -54.602 65.492 95.708  1.00 52.36  ? 181 LEU C CB  1 
ATOM   6149 C CG  . LEU C 3 181 ? -55.492 65.531 96.957  1.00 55.00  ? 181 LEU C CG  1 
ATOM   6150 C CD1 . LEU C 3 181 ? -56.311 66.806 96.993  1.00 59.77  ? 181 LEU C CD1 1 
ATOM   6151 C CD2 . LEU C 3 181 ? -56.392 64.306 97.058  1.00 51.85  ? 181 LEU C CD2 1 
ATOM   6152 N N   . THR C 3 182 ? -57.395 64.937 93.607  1.00 50.70  ? 182 THR C N   1 
ATOM   6153 C CA  . THR C 3 182 ? -58.555 65.519 92.941  1.00 54.98  ? 182 THR C CA  1 
ATOM   6154 C C   . THR C 3 182 ? -59.716 65.590 93.927  1.00 57.10  ? 182 THR C C   1 
ATOM   6155 O O   . THR C 3 182 ? -60.225 64.557 94.377  1.00 60.90  ? 182 THR C O   1 
ATOM   6156 C CB  . THR C 3 182 ? -58.934 64.712 91.699  1.00 57.76  ? 182 THR C CB  1 
ATOM   6157 O OG1 . THR C 3 182 ? -57.997 64.995 90.653  1.00 60.14  ? 182 THR C OG1 1 
ATOM   6158 C CG2 . THR C 3 182 ? -60.327 65.090 91.215  1.00 55.02  ? 182 THR C CG2 1 
ATOM   6159 N N   . LEU C 3 183 ? -60.123 66.809 94.266  1.00 56.91  ? 183 LEU C N   1 
ATOM   6160 C CA  . LEU C 3 183 ? -61.302 67.067 95.078  1.00 61.65  ? 183 LEU C CA  1 
ATOM   6161 C C   . LEU C 3 183 ? -62.326 67.839 94.257  1.00 63.15  ? 183 LEU C C   1 
ATOM   6162 O O   . LEU C 3 183 ? -62.032 68.353 93.175  1.00 63.58  ? 183 LEU C O   1 
ATOM   6163 C CB  . LEU C 3 183 ? -60.957 67.866 96.342  1.00 61.82  ? 183 LEU C CB  1 
ATOM   6164 C CG  . LEU C 3 183 ? -59.866 67.368 97.285  1.00 61.28  ? 183 LEU C CG  1 
ATOM   6165 C CD1 . LEU C 3 183 ? -59.358 68.520 98.143  1.00 60.94  ? 183 LEU C CD1 1 
ATOM   6166 C CD2 . LEU C 3 183 ? -60.390 66.239 98.153  1.00 63.97  ? 183 LEU C CD2 1 
ATOM   6167 N N   . SER C 3 184 ? -63.542 67.917 94.789  1.00 57.94  ? 184 SER C N   1 
ATOM   6168 C CA  . SER C 3 184 ? -64.526 68.826 94.228  1.00 61.27  ? 184 SER C CA  1 
ATOM   6169 C C   . SER C 3 184 ? -64.132 70.268 94.531  1.00 66.41  ? 184 SER C C   1 
ATOM   6170 O O   . SER C 3 184 ? -63.332 70.546 95.430  1.00 65.94  ? 184 SER C O   1 
ATOM   6171 C CB  . SER C 3 184 ? -65.914 68.535 94.793  1.00 62.92  ? 184 SER C CB  1 
ATOM   6172 O OG  . SER C 3 184 ? -66.035 69.051 96.109  1.00 66.67  ? 184 SER C OG  1 
ATOM   6173 N N   . LYS C 3 185 ? -64.698 71.196 93.754  1.00 67.47  ? 185 LYS C N   1 
ATOM   6174 C CA  . LYS C 3 185 ? -64.510 72.609 94.064  1.00 65.22  ? 185 LYS C CA  1 
ATOM   6175 C C   . LYS C 3 185 ? -64.977 72.917 95.480  1.00 73.55  ? 185 LYS C C   1 
ATOM   6176 O O   . LYS C 3 185 ? -64.301 73.638 96.222  1.00 73.94  ? 185 LYS C O   1 
ATOM   6177 C CB  . LYS C 3 185 ? -65.254 73.479 93.052  1.00 64.59  ? 185 LYS C CB  1 
ATOM   6178 N N   . ALA C 3 186 ? -66.117 72.348 95.883  1.00 74.50  ? 186 ALA C N   1 
ATOM   6179 C CA  . ALA C 3 186 ? -66.662 72.617 97.211  1.00 73.29  ? 186 ALA C CA  1 
ATOM   6180 C C   . ALA C 3 186 ? -65.747 72.080 98.307  1.00 73.77  ? 186 ALA C C   1 
ATOM   6181 O O   . ALA C 3 186 ? -65.408 72.799 99.255  1.00 77.78  ? 186 ALA C O   1 
ATOM   6182 C CB  . ALA C 3 186 ? -68.061 72.013 97.333  1.00 69.39  ? 186 ALA C CB  1 
ATOM   6183 N N   . ASP C 3 187 ? -65.340 70.811 98.195  1.00 70.74  ? 187 ASP C N   1 
ATOM   6184 C CA  . ASP C 3 187 ? -64.476 70.216 99.211  1.00 70.31  ? 187 ASP C CA  1 
ATOM   6185 C C   . ASP C 3 187 ? -63.146 70.951 99.323  1.00 74.42  ? 187 ASP C C   1 
ATOM   6186 O O   . ASP C 3 187 ? -62.585 71.054 100.420 1.00 73.92  ? 187 ASP C O   1 
ATOM   6187 C CB  . ASP C 3 187 ? -64.229 68.738 98.901  1.00 68.12  ? 187 ASP C CB  1 
ATOM   6188 C CG  . ASP C 3 187 ? -65.422 67.860 99.228  1.00 69.47  ? 187 ASP C CG  1 
ATOM   6189 O OD1 . ASP C 3 187 ? -66.543 68.392 99.366  1.00 74.85  ? 187 ASP C OD1 1 
ATOM   6190 O OD2 . ASP C 3 187 ? -65.235 66.632 99.347  1.00 63.71  ? 187 ASP C OD2 1 
ATOM   6191 N N   . TYR C 3 188 ? -62.635 71.476 98.205  1.00 69.81  ? 188 TYR C N   1 
ATOM   6192 C CA  . TYR C 3 188 ? -61.317 72.103 98.210  1.00 68.55  ? 188 TYR C CA  1 
ATOM   6193 C C   . TYR C 3 188 ? -61.324 73.418 98.981  1.00 70.58  ? 188 TYR C C   1 
ATOM   6194 O O   . TYR C 3 188 ? -60.394 73.699 99.746  1.00 68.62  ? 188 TYR C O   1 
ATOM   6195 C CB  . TYR C 3 188 ? -60.839 72.316 96.771  1.00 69.25  ? 188 TYR C CB  1 
ATOM   6196 C CG  . TYR C 3 188 ? -59.642 73.235 96.628  1.00 62.66  ? 188 TYR C CG  1 
ATOM   6197 C CD1 . TYR C 3 188 ? -58.392 72.867 97.107  1.00 63.90  ? 188 TYR C CD1 1 
ATOM   6198 C CD2 . TYR C 3 188 ? -59.763 74.464 95.997  1.00 61.81  ? 188 TYR C CD2 1 
ATOM   6199 C CE1 . TYR C 3 188 ? -57.297 73.705 96.973  1.00 63.53  ? 188 TYR C CE1 1 
ATOM   6200 C CE2 . TYR C 3 188 ? -58.677 75.306 95.859  1.00 66.26  ? 188 TYR C CE2 1 
ATOM   6201 C CZ  . TYR C 3 188 ? -57.447 74.923 96.349  1.00 66.05  ? 188 TYR C CZ  1 
ATOM   6202 O OH  . TYR C 3 188 ? -56.365 75.762 96.209  1.00 66.53  ? 188 TYR C OH  1 
ATOM   6203 N N   . GLU C 3 189 ? -62.360 74.235 98.797  1.00 75.08  ? 189 GLU C N   1 
ATOM   6204 C CA  . GLU C 3 189 ? -62.433 75.527 99.472  1.00 75.73  ? 189 GLU C CA  1 
ATOM   6205 C C   . GLU C 3 189 ? -62.848 75.416 100.933 1.00 75.90  ? 189 GLU C C   1 
ATOM   6206 O O   . GLU C 3 189 ? -62.893 76.439 101.622 1.00 73.96  ? 189 GLU C O   1 
ATOM   6207 C CB  . GLU C 3 189 ? -63.395 76.456 98.728  1.00 71.99  ? 189 GLU C CB  1 
ATOM   6208 C CG  . GLU C 3 189 ? -63.324 76.315 97.220  1.00 75.10  ? 189 GLU C CG  1 
ATOM   6209 C CD  . GLU C 3 189 ? -63.690 77.586 96.487  1.00 84.88  ? 189 GLU C CD  1 
ATOM   6210 O OE1 . GLU C 3 189 ? -64.877 77.975 96.530  1.00 84.21  ? 189 GLU C OE1 1 
ATOM   6211 O OE2 . GLU C 3 189 ? -62.789 78.191 95.863  1.00 88.61  ? 189 GLU C OE2 1 
ATOM   6212 N N   . LYS C 3 190 ? -63.149 74.210 101.421 1.00 76.05  ? 190 LYS C N   1 
ATOM   6213 C CA  . LYS C 3 190 ? -63.451 74.036 102.836 1.00 75.10  ? 190 LYS C CA  1 
ATOM   6214 C C   . LYS C 3 190 ? -62.188 74.001 103.692 1.00 76.50  ? 190 LYS C C   1 
ATOM   6215 O O   . LYS C 3 190 ? -62.222 74.419 104.856 1.00 71.99  ? 190 LYS C O   1 
ATOM   6216 C CB  . LYS C 3 190 ? -64.264 72.757 103.044 1.00 69.94  ? 190 LYS C CB  1 
ATOM   6217 N N   . HIS C 3 191 ? -61.076 73.524 103.139 1.00 76.37  ? 191 HIS C N   1 
ATOM   6218 C CA  . HIS C 3 191 ? -59.812 73.380 103.848 1.00 71.28  ? 191 HIS C CA  1 
ATOM   6219 C C   . HIS C 3 191 ? -58.788 74.359 103.288 1.00 71.47  ? 191 HIS C C   1 
ATOM   6220 O O   . HIS C 3 191 ? -58.999 74.977 102.244 1.00 76.85  ? 191 HIS C O   1 
ATOM   6221 C CB  . HIS C 3 191 ? -59.297 71.941 103.739 1.00 71.49  ? 191 HIS C CB  1 
ATOM   6222 C CG  . HIS C 3 191 ? -60.338 70.903 104.027 1.00 78.01  ? 191 HIS C CG  1 
ATOM   6223 N ND1 . HIS C 3 191 ? -61.348 70.591 103.140 1.00 72.04  ? 191 HIS C ND1 1 
ATOM   6224 C CD2 . HIS C 3 191 ? -60.523 70.102 105.103 1.00 75.79  ? 191 HIS C CD2 1 
ATOM   6225 C CE1 . HIS C 3 191 ? -62.108 69.643 103.657 1.00 72.92  ? 191 HIS C CE1 1 
ATOM   6226 N NE2 . HIS C 3 191 ? -61.630 69.329 104.848 1.00 72.78  ? 191 HIS C NE2 1 
ATOM   6227 N N   . LYS C 3 192 ? -57.665 74.498 103.994 1.00 71.17  ? 192 LYS C N   1 
ATOM   6228 C CA  . LYS C 3 192 ? -56.642 75.469 103.615 1.00 72.63  ? 192 LYS C CA  1 
ATOM   6229 C C   . LYS C 3 192 ? -55.300 74.830 103.298 1.00 72.80  ? 192 LYS C C   1 
ATOM   6230 O O   . LYS C 3 192 ? -54.732 75.107 102.235 1.00 74.15  ? 192 LYS C O   1 
ATOM   6231 C CB  . LYS C 3 192 ? -56.468 76.522 104.723 1.00 67.49  ? 192 LYS C CB  1 
ATOM   6232 N N   . VAL C 3 193 ? -54.763 73.984 104.179 1.00 67.63  ? 193 VAL C N   1 
ATOM   6233 C CA  . VAL C 3 193 ? -53.424 73.435 103.981 1.00 69.62  ? 193 VAL C CA  1 
ATOM   6234 C C   . VAL C 3 193 ? -53.507 72.154 103.156 1.00 68.00  ? 193 VAL C C   1 
ATOM   6235 O O   . VAL C 3 193 ? -54.369 71.294 103.386 1.00 68.51  ? 193 VAL C O   1 
ATOM   6236 C CB  . VAL C 3 193 ? -52.701 73.212 105.326 1.00 67.04  ? 193 VAL C CB  1 
ATOM   6237 C CG1 . VAL C 3 193 ? -53.060 71.885 105.962 1.00 67.36  ? 193 VAL C CG1 1 
ATOM   6238 C CG2 . VAL C 3 193 ? -51.196 73.304 105.133 1.00 63.58  ? 193 VAL C CG2 1 
ATOM   6239 N N   . TYR C 3 194 ? -52.629 72.050 102.161 1.00 68.99  ? 194 TYR C N   1 
ATOM   6240 C CA  . TYR C 3 194 ? -52.572 70.908 101.258 1.00 66.58  ? 194 TYR C CA  1 
ATOM   6241 C C   . TYR C 3 194 ? -51.117 70.504 101.114 1.00 62.64  ? 194 TYR C C   1 
ATOM   6242 O O   . TYR C 3 194 ? -50.284 71.318 100.702 1.00 63.57  ? 194 TYR C O   1 
ATOM   6243 C CB  . TYR C 3 194 ? -53.180 71.246 99.895  1.00 64.67  ? 194 TYR C CB  1 
ATOM   6244 C CG  . TYR C 3 194 ? -54.671 71.451 99.952  1.00 67.70  ? 194 TYR C CG  1 
ATOM   6245 C CD1 . TYR C 3 194 ? -55.540 70.379 99.827  1.00 66.29  ? 194 TYR C CD1 1 
ATOM   6246 C CD2 . TYR C 3 194 ? -55.210 72.715 100.153 1.00 69.78  ? 194 TYR C CD2 1 
ATOM   6247 C CE1 . TYR C 3 194 ? -56.904 70.555 99.889  1.00 69.86  ? 194 TYR C CE1 1 
ATOM   6248 C CE2 . TYR C 3 194 ? -56.577 72.904 100.218 1.00 68.06  ? 194 TYR C CE2 1 
ATOM   6249 C CZ  . TYR C 3 194 ? -57.419 71.820 100.085 1.00 70.44  ? 194 TYR C CZ  1 
ATOM   6250 O OH  . TYR C 3 194 ? -58.782 71.996 100.145 1.00 67.35  ? 194 TYR C OH  1 
ATOM   6251 N N   . ALA C 3 195 ? -50.814 69.255 101.449 1.00 60.19  ? 195 ALA C N   1 
ATOM   6252 C CA  . ALA C 3 195 ? -49.442 68.786 101.528 1.00 62.81  ? 195 ALA C CA  1 
ATOM   6253 C C   . ALA C 3 195 ? -49.327 67.399 100.922 1.00 62.87  ? 195 ALA C C   1 
ATOM   6254 O O   . ALA C 3 195 ? -50.238 66.578 101.056 1.00 60.42  ? 195 ALA C O   1 
ATOM   6255 C CB  . ALA C 3 195 ? -48.958 68.752 102.983 1.00 56.39  ? 195 ALA C CB  1 
ATOM   6256 N N   . CYS C 3 196 ? -48.204 67.142 100.258 1.00 61.59  ? 196 CYS C N   1 
ATOM   6257 C CA  . CYS C 3 196 ? -47.821 65.786 99.889  1.00 60.61  ? 196 CYS C CA  1 
ATOM   6258 C C   . CYS C 3 196 ? -46.547 65.430 100.639 1.00 58.99  ? 196 CYS C C   1 
ATOM   6259 O O   . CYS C 3 196 ? -45.554 66.162 100.572 1.00 64.20  ? 196 CYS C O   1 
ATOM   6260 C CB  . CYS C 3 196 ? -47.629 65.628 98.373  1.00 67.02  ? 196 CYS C CB  1 
ATOM   6261 S SG  . CYS C 3 196 ? -46.504 66.789 97.562  1.00 70.43  ? 196 CYS C SG  1 
ATOM   6262 N N   . GLU C 3 197 ? -46.595 64.328 101.378 1.00 61.09  ? 197 GLU C N   1 
ATOM   6263 C CA  . GLU C 3 197 ? -45.447 63.824 102.115 1.00 61.54  ? 197 GLU C CA  1 
ATOM   6264 C C   . GLU C 3 197 ? -44.815 62.701 101.311 1.00 60.95  ? 197 GLU C C   1 
ATOM   6265 O O   . GLU C 3 197 ? -45.513 61.787 100.859 1.00 58.34  ? 197 GLU C O   1 
ATOM   6266 C CB  . GLU C 3 197 ? -45.853 63.319 103.499 1.00 69.61  ? 197 GLU C CB  1 
ATOM   6267 C CG  . GLU C 3 197 ? -44.678 62.901 104.368 1.00 70.66  ? 197 GLU C CG  1 
ATOM   6268 C CD  . GLU C 3 197 ? -45.116 62.248 105.665 1.00 76.01  ? 197 GLU C CD  1 
ATOM   6269 O OE1 . GLU C 3 197 ? -46.033 61.399 105.623 1.00 71.04  ? 197 GLU C OE1 1 
ATOM   6270 O OE2 . GLU C 3 197 ? -44.543 62.584 106.724 1.00 77.91  ? 197 GLU C OE2 1 
ATOM   6271 N N   . VAL C 3 198 ? -43.501 62.775 101.136 1.00 61.55  ? 198 VAL C N   1 
ATOM   6272 C CA  . VAL C 3 198 ? -42.764 61.864 100.273 1.00 58.47  ? 198 VAL C CA  1 
ATOM   6273 C C   . VAL C 3 198 ? -41.743 61.116 101.114 1.00 62.97  ? 198 VAL C C   1 
ATOM   6274 O O   . VAL C 3 198 ? -40.961 61.734 101.847 1.00 66.04  ? 198 VAL C O   1 
ATOM   6275 C CB  . VAL C 3 198 ? -42.071 62.616 99.123  1.00 59.74  ? 198 VAL C CB  1 
ATOM   6276 C CG1 . VAL C 3 198 ? -41.291 61.645 98.259  1.00 58.55  ? 198 VAL C CG1 1 
ATOM   6277 C CG2 . VAL C 3 198 ? -43.094 63.390 98.297  1.00 55.62  ? 198 VAL C CG2 1 
ATOM   6278 N N   . THR C 3 199 ? -41.749 59.793 101.005 1.00 56.97  ? 199 THR C N   1 
ATOM   6279 C CA  . THR C 3 199 ? -40.757 58.946 101.646 1.00 62.62  ? 199 THR C CA  1 
ATOM   6280 C C   . THR C 3 199 ? -39.926 58.261 100.569 1.00 62.09  ? 199 THR C C   1 
ATOM   6281 O O   . THR C 3 199 ? -40.475 57.738 99.593  1.00 60.28  ? 199 THR C O   1 
ATOM   6282 C CB  . THR C 3 199 ? -41.417 57.906 102.562 1.00 65.26  ? 199 THR C CB  1 
ATOM   6283 O OG1 . THR C 3 199 ? -41.788 56.746 101.805 1.00 61.86  ? 199 THR C OG1 1 
ATOM   6284 C CG2 . THR C 3 199 ? -42.657 58.491 103.227 1.00 62.00  ? 199 THR C CG2 1 
ATOM   6285 N N   . HIS C 3 200 ? -38.607 58.276 100.747 1.00 65.77  ? 200 HIS C N   1 
ATOM   6286 C CA  . HIS C 3 200 ? -37.695 57.664 99.790  1.00 67.53  ? 200 HIS C CA  1 
ATOM   6287 C C   . HIS C 3 200 ? -36.403 57.302 100.504 1.00 66.07  ? 200 HIS C C   1 
ATOM   6288 O O   . HIS C 3 200 ? -36.022 57.948 101.486 1.00 68.36  ? 200 HIS C O   1 
ATOM   6289 C CB  . HIS C 3 200 ? -37.407 58.599 98.609  1.00 63.62  ? 200 HIS C CB  1 
ATOM   6290 C CG  . HIS C 3 200 ? -36.779 57.912 97.437  1.00 58.77  ? 200 HIS C CG  1 
ATOM   6291 N ND1 . HIS C 3 200 ? -35.430 57.988 97.166  1.00 58.83  ? 200 HIS C ND1 1 
ATOM   6292 C CD2 . HIS C 3 200 ? -37.316 57.136 96.466  1.00 56.57  ? 200 HIS C CD2 1 
ATOM   6293 C CE1 . HIS C 3 200 ? -35.162 57.286 96.079  1.00 58.88  ? 200 HIS C CE1 1 
ATOM   6294 N NE2 . HIS C 3 200 ? -36.289 56.759 95.634  1.00 52.42  ? 200 HIS C NE2 1 
ATOM   6295 N N   . GLN C 3 201 ? -35.730 56.267 99.988  1.00 66.47  ? 201 GLN C N   1 
ATOM   6296 C CA  . GLN C 3 201 ? -34.471 55.814 100.577 1.00 64.23  ? 201 GLN C CA  1 
ATOM   6297 C C   . GLN C 3 201 ? -33.465 56.950 100.688 1.00 65.51  ? 201 GLN C C   1 
ATOM   6298 O O   . GLN C 3 201 ? -32.733 57.048 101.679 1.00 76.50  ? 201 GLN C O   1 
ATOM   6299 C CB  . GLN C 3 201 ? -33.880 54.676 99.745  1.00 59.54  ? 201 GLN C CB  1 
ATOM   6300 C CG  . GLN C 3 201 ? -34.883 53.627 99.312  1.00 68.62  ? 201 GLN C CG  1 
ATOM   6301 C CD  . GLN C 3 201 ? -34.217 52.461 98.609  1.00 74.52  ? 201 GLN C CD  1 
ATOM   6302 O OE1 . GLN C 3 201 ? -32.993 52.431 98.461  1.00 72.36  ? 201 GLN C OE1 1 
ATOM   6303 N NE2 . GLN C 3 201 ? -35.018 51.495 98.164  1.00 70.04  ? 201 GLN C NE2 1 
ATOM   6304 N N   . GLY C 3 202 ? -33.414 57.820 99.682  1.00 64.91  ? 202 GLY C N   1 
ATOM   6305 C CA  . GLY C 3 202 ? -32.498 58.943 99.711  1.00 66.78  ? 202 GLY C CA  1 
ATOM   6306 C C   . GLY C 3 202 ? -32.902 60.084 100.616 1.00 72.78  ? 202 GLY C C   1 
ATOM   6307 O O   . GLY C 3 202 ? -32.086 60.977 100.864 1.00 79.79  ? 202 GLY C O   1 
ATOM   6308 N N   . LEU C 3 203 ? -34.137 60.081 101.112 1.00 68.89  ? 203 LEU C N   1 
ATOM   6309 C CA  . LEU C 3 203 ? -34.614 61.118 102.018 1.00 73.02  ? 203 LEU C CA  1 
ATOM   6310 C C   . LEU C 3 203 ? -34.274 60.722 103.450 1.00 76.69  ? 203 LEU C C   1 
ATOM   6311 O O   . LEU C 3 203 ? -34.712 59.666 103.924 1.00 73.46  ? 203 LEU C O   1 
ATOM   6312 C CB  . LEU C 3 203 ? -36.121 61.317 101.852 1.00 68.81  ? 203 LEU C CB  1 
ATOM   6313 C CG  . LEU C 3 203 ? -36.558 62.252 100.725 1.00 68.03  ? 203 LEU C CG  1 
ATOM   6314 C CD1 . LEU C 3 203 ? -37.970 62.766 100.967 1.00 71.11  ? 203 LEU C CD1 1 
ATOM   6315 C CD2 . LEU C 3 203 ? -35.574 63.410 100.561 1.00 64.85  ? 203 LEU C CD2 1 
ATOM   6316 N N   . SER C 3 204 ? -33.486 61.559 104.134 1.00 75.30  ? 204 SER C N   1 
ATOM   6317 C CA  . SER C 3 204 ? -33.146 61.281 105.528 1.00 80.38  ? 204 SER C CA  1 
ATOM   6318 C C   . SER C 3 204 ? -34.400 61.232 106.391 1.00 75.74  ? 204 SER C C   1 
ATOM   6319 O O   . SER C 3 204 ? -34.588 60.305 107.188 1.00 78.02  ? 204 SER C O   1 
ATOM   6320 C CB  . SER C 3 204 ? -32.163 62.330 106.053 1.00 75.82  ? 204 SER C CB  1 
ATOM   6321 O OG  . SER C 3 204 ? -32.720 63.632 105.985 1.00 82.41  ? 204 SER C OG  1 
ATOM   6322 N N   . SER C 3 205 ? -35.274 62.219 106.236 1.00 75.61  ? 205 SER C N   1 
ATOM   6323 C CA  . SER C 3 205 ? -36.602 62.220 106.824 1.00 75.21  ? 205 SER C CA  1 
ATOM   6324 C C   . SER C 3 205 ? -37.613 62.577 105.745 1.00 76.26  ? 205 SER C C   1 
ATOM   6325 O O   . SER C 3 205 ? -37.269 63.264 104.776 1.00 72.76  ? 205 SER C O   1 
ATOM   6326 C CB  . SER C 3 205 ? -36.702 63.216 107.988 1.00 68.41  ? 205 SER C CB  1 
ATOM   6327 O OG  . SER C 3 205 ? -37.044 64.513 107.526 1.00 75.59  ? 205 SER C OG  1 
ATOM   6328 N N   . PRO C 3 206 ? -38.852 62.102 105.868 1.00 71.80  ? 206 PRO C N   1 
ATOM   6329 C CA  . PRO C 3 206 ? -39.877 62.449 104.876 1.00 71.10  ? 206 PRO C CA  1 
ATOM   6330 C C   . PRO C 3 206 ? -39.994 63.955 104.698 1.00 72.22  ? 206 PRO C C   1 
ATOM   6331 O O   . PRO C 3 206 ? -40.069 64.713 105.669 1.00 77.33  ? 206 PRO C O   1 
ATOM   6332 C CB  . PRO C 3 206 ? -41.161 61.843 105.459 1.00 68.20  ? 206 PRO C CB  1 
ATOM   6333 C CG  . PRO C 3 206 ? -40.801 61.346 106.835 1.00 70.76  ? 206 PRO C CG  1 
ATOM   6334 C CD  . PRO C 3 206 ? -39.337 61.095 106.822 1.00 68.85  ? 206 PRO C CD  1 
ATOM   6335 N N   . VAL C 3 207 ? -39.977 64.388 103.441 1.00 73.44  ? 207 VAL C N   1 
ATOM   6336 C CA  . VAL C 3 207 ? -40.102 65.795 103.083 1.00 69.61  ? 207 VAL C CA  1 
ATOM   6337 C C   . VAL C 3 207 ? -41.546 66.062 102.690 1.00 68.39  ? 207 VAL C C   1 
ATOM   6338 O O   . VAL C 3 207 ? -42.228 65.211 102.103 1.00 70.93  ? 207 VAL C O   1 
ATOM   6339 C CB  . VAL C 3 207 ? -39.121 66.179 101.952 1.00 70.18  ? 207 VAL C CB  1 
ATOM   6340 C CG1 . VAL C 3 207 ? -39.317 67.624 101.526 1.00 67.08  ? 207 VAL C CG1 1 
ATOM   6341 C CG2 . VAL C 3 207 ? -37.688 65.966 102.405 1.00 72.20  ? 207 VAL C CG2 1 
ATOM   6342 N N   . THR C 3 208 ? -42.024 67.257 103.028 1.00 68.74  ? 208 THR C N   1 
ATOM   6343 C CA  . THR C 3 208 ? -43.424 67.622 102.839 1.00 67.88  ? 208 THR C CA  1 
ATOM   6344 C C   . THR C 3 208 ? -43.481 69.018 102.235 1.00 69.33  ? 208 THR C C   1 
ATOM   6345 O O   . THR C 3 208 ? -43.153 69.999 102.909 1.00 75.04  ? 208 THR C O   1 
ATOM   6346 C CB  . THR C 3 208 ? -44.183 67.572 104.166 1.00 71.18  ? 208 THR C CB  1 
ATOM   6347 O OG1 . THR C 3 208 ? -44.300 66.211 104.604 1.00 74.44  ? 208 THR C OG1 1 
ATOM   6348 C CG2 . THR C 3 208 ? -45.570 68.180 104.019 1.00 68.17  ? 208 THR C CG2 1 
ATOM   6349 N N   . LYS C 3 209 ? -43.886 69.109 100.971 1.00 62.26  ? 209 LYS C N   1 
ATOM   6350 C CA  . LYS C 3 209 ? -44.190 70.393 100.359 1.00 65.28  ? 209 LYS C CA  1 
ATOM   6351 C C   . LYS C 3 209 ? -45.678 70.678 100.515 1.00 65.93  ? 209 LYS C C   1 
ATOM   6352 O O   . LYS C 3 209 ? -46.512 69.779 100.366 1.00 67.10  ? 209 LYS C O   1 
ATOM   6353 C CB  . LYS C 3 209 ? -43.792 70.406 98.881  1.00 63.16  ? 209 LYS C CB  1 
ATOM   6354 C CG  . LYS C 3 209 ? -42.295 70.277 98.643  1.00 60.92  ? 209 LYS C CG  1 
ATOM   6355 C CD  . LYS C 3 209 ? -41.619 71.637 98.583  1.00 61.64  ? 209 LYS C CD  1 
ATOM   6356 N N   . SER C 3 210 ? -46.010 71.928 100.825 1.00 60.71  ? 210 SER C N   1 
ATOM   6357 C CA  . SER C 3 210 ? -47.381 72.264 101.172 1.00 59.42  ? 210 SER C CA  1 
ATOM   6358 C C   . SER C 3 210 ? -47.664 73.719 100.838 1.00 65.99  ? 210 SER C C   1 
ATOM   6359 O O   . SER C 3 210 ? -46.755 74.512 100.580 1.00 62.07  ? 210 SER C O   1 
ATOM   6360 C CB  . SER C 3 210 ? -47.659 71.993 102.654 1.00 67.14  ? 210 SER C CB  1 
ATOM   6361 O OG  . SER C 3 210 ? -46.478 72.129 103.425 1.00 73.84  ? 210 SER C OG  1 
ATOM   6362 N N   . PHE C 3 211 ? -48.954 74.058 100.854 1.00 70.11  ? 211 PHE C N   1 
ATOM   6363 C CA  . PHE C 3 211 ? -49.411 75.420 100.622 1.00 67.93  ? 211 PHE C CA  1 
ATOM   6364 C C   . PHE C 3 211 ? -50.762 75.609 101.295 1.00 68.38  ? 211 PHE C C   1 
ATOM   6365 O O   . PHE C 3 211 ? -51.432 74.643 101.671 1.00 67.13  ? 211 PHE C O   1 
ATOM   6366 C CB  . PHE C 3 211 ? -49.505 75.741 99.121  1.00 65.70  ? 211 PHE C CB  1 
ATOM   6367 C CG  . PHE C 3 211 ? -50.620 75.018 98.404  1.00 66.79  ? 211 PHE C CG  1 
ATOM   6368 C CD1 . PHE C 3 211 ? -51.878 75.596 98.280  1.00 65.56  ? 211 PHE C CD1 1 
ATOM   6369 C CD2 . PHE C 3 211 ? -50.405 73.769 97.841  1.00 68.33  ? 211 PHE C CD2 1 
ATOM   6370 C CE1 . PHE C 3 211 ? -52.900 74.938 97.621  1.00 64.86  ? 211 PHE C CE1 1 
ATOM   6371 C CE2 . PHE C 3 211 ? -51.423 73.105 97.177  1.00 67.49  ? 211 PHE C CE2 1 
ATOM   6372 C CZ  . PHE C 3 211 ? -52.673 73.691 97.067  1.00 66.98  ? 211 PHE C CZ  1 
ATOM   6373 N N   . ASN C 3 212 ? -51.154 76.872 101.446 1.00 68.59  ? 212 ASN C N   1 
ATOM   6374 C CA  . ASN C 3 212 ? -52.483 77.241 101.912 1.00 71.82  ? 212 ASN C CA  1 
ATOM   6375 C C   . ASN C 3 212 ? -53.173 78.068 100.837 1.00 71.99  ? 212 ASN C C   1 
ATOM   6376 O O   . ASN C 3 212 ? -52.546 78.935 100.219 1.00 68.73  ? 212 ASN C O   1 
ATOM   6377 C CB  . ASN C 3 212 ? -52.430 78.042 103.223 1.00 74.04  ? 212 ASN C CB  1 
ATOM   6378 C CG  . ASN C 3 212 ? -51.278 77.631 104.117 1.00 69.84  ? 212 ASN C CG  1 
ATOM   6379 O OD1 . ASN C 3 212 ? -51.169 76.472 104.517 1.00 69.96  ? 212 ASN C OD1 1 
ATOM   6380 N ND2 . ASN C 3 212 ? -50.411 78.585 104.438 1.00 66.88  ? 212 ASN C ND2 1 
ATOM   6381 N N   . ARG C 3 213 ? -54.460 77.793 100.609 1.00 74.20  ? 213 ARG C N   1 
ATOM   6382 C CA  . ARG C 3 213 ? -55.240 78.579 99.658  1.00 77.75  ? 213 ARG C CA  1 
ATOM   6383 C C   . ARG C 3 213 ? -55.171 80.055 100.014 1.00 79.07  ? 213 ARG C C   1 
ATOM   6384 O O   . ARG C 3 213 ? -55.524 80.452 101.129 1.00 83.65  ? 213 ARG C O   1 
ATOM   6385 C CB  . ARG C 3 213 ? -56.700 78.123 99.640  1.00 74.40  ? 213 ARG C CB  1 
ATOM   6386 C CG  . ARG C 3 213 ? -56.937 76.647 99.419  1.00 75.71  ? 213 ARG C CG  1 
ATOM   6387 C CD  . ARG C 3 213 ? -58.438 76.343 99.359  1.00 77.81  ? 213 ARG C CD  1 
ATOM   6388 N NE  . ARG C 3 213 ? -59.068 76.503 100.668 1.00 80.03  ? 213 ARG C NE  1 
ATOM   6389 C CZ  . ARG C 3 213 ? -59.631 77.620 101.113 1.00 78.86  ? 213 ARG C CZ  1 
ATOM   6390 N NH1 . ARG C 3 213 ? -59.781 78.680 100.332 1.00 78.45  ? 213 ARG C NH1 1 
ATOM   6391 N NH2 . ARG C 3 213 ? -60.066 77.669 102.370 1.00 82.10  ? 213 ARG C NH2 1 
ATOM   6392 N N   . GLY C 3 214 ? -54.716 80.863 99.063  1.00 79.81  ? 214 GLY C N   1 
ATOM   6393 C CA  . GLY C 3 214 ? -54.564 82.289 99.279  1.00 76.71  ? 214 GLY C CA  1 
ATOM   6394 C C   . GLY C 3 214 ? -53.111 82.723 99.322  1.00 77.69  ? 214 GLY C C   1 
ATOM   6395 O O   . GLY C 3 214 ? -52.234 81.962 99.734  1.00 72.21  ? 214 GLY C O   1 
HETATM 6396 O O   . HOH D 4 .   ? -26.642 13.339 61.212  1.00 62.21  ? 501 HOH A O   1 
HETATM 6397 O O   . HOH D 4 .   ? -36.274 20.079 49.172  1.00 48.07  ? 502 HOH A O   1 
HETATM 6398 O O   . HOH D 4 .   ? 7.934   19.216 24.534  1.00 45.81  ? 503 HOH A O   1 
HETATM 6399 O O   . HOH D 4 .   ? -37.001 44.438 39.125  1.00 46.01  ? 504 HOH A O   1 
HETATM 6400 O O   . HOH D 4 .   ? 12.769  30.857 30.528  1.00 54.12  ? 505 HOH A O   1 
HETATM 6401 O O   . HOH D 4 .   ? -3.332  22.064 44.651  1.00 51.55  ? 506 HOH A O   1 
HETATM 6402 O O   . HOH D 4 .   ? -30.854 25.670 30.170  1.00 51.11  ? 507 HOH A O   1 
HETATM 6403 O O   . HOH D 4 .   ? -13.029 9.406  27.752  1.00 38.11  ? 508 HOH A O   1 
HETATM 6404 O O   . HOH D 4 .   ? 0.338   7.250  9.190   1.00 49.52  ? 509 HOH A O   1 
HETATM 6405 O O   . HOH D 4 .   ? 1.862   14.361 13.524  1.00 44.97  ? 510 HOH A O   1 
HETATM 6406 O O   . HOH D 4 .   ? -20.974 31.811 40.299  1.00 30.57  ? 511 HOH A O   1 
HETATM 6407 O O   . HOH D 4 .   ? -23.882 9.569  46.224  1.00 41.81  ? 512 HOH A O   1 
HETATM 6408 O O   . HOH D 4 .   ? -2.401  11.023 9.550   1.00 46.10  ? 513 HOH A O   1 
HETATM 6409 O O   . HOH D 4 .   ? -10.935 -1.109 22.881  1.00 50.40  ? 514 HOH A O   1 
HETATM 6410 O O   . HOH D 4 .   ? -17.481 13.241 44.669  1.00 38.96  ? 515 HOH A O   1 
HETATM 6411 O O   . HOH D 4 .   ? -25.825 14.122 30.033  1.00 42.28  ? 516 HOH A O   1 
HETATM 6412 O O   . HOH D 4 .   ? -27.023 38.252 54.595  1.00 34.09  ? 517 HOH A O   1 
HETATM 6413 O O   . HOH D 4 .   ? -1.809  1.517  29.378  1.00 45.35  ? 518 HOH A O   1 
HETATM 6414 O O   . HOH D 4 .   ? -39.535 39.378 35.800  1.00 50.74  ? 519 HOH A O   1 
HETATM 6415 O O   . HOH D 4 .   ? -26.721 36.722 40.195  1.00 42.31  ? 520 HOH A O   1 
HETATM 6416 O O   . HOH D 4 .   ? -9.216  16.596 45.507  1.00 44.98  ? 521 HOH A O   1 
HETATM 6417 O O   . HOH D 4 .   ? -10.207 22.522 48.424  1.00 38.85  ? 522 HOH A O   1 
HETATM 6418 O O   . HOH D 4 .   ? -34.951 40.886 41.035  1.00 44.49  ? 523 HOH A O   1 
HETATM 6419 O O   . HOH D 4 .   ? -15.088 21.702 21.912  1.00 37.75  ? 524 HOH A O   1 
HETATM 6420 O O   . HOH D 4 .   ? -25.921 17.277 38.226  1.00 37.73  ? 525 HOH A O   1 
HETATM 6421 O O   . HOH D 4 .   ? -7.487  24.283 42.995  1.00 34.79  ? 526 HOH A O   1 
HETATM 6422 O O   . HOH D 4 .   ? -21.710 44.457 53.710  1.00 47.65  ? 527 HOH A O   1 
HETATM 6423 O O   . HOH D 4 .   ? -11.370 16.936 44.566  1.00 42.21  ? 528 HOH A O   1 
HETATM 6424 O O   . HOH D 4 .   ? -2.558  7.015  19.728  1.00 43.76  ? 529 HOH A O   1 
HETATM 6425 O O   . HOH D 4 .   ? -10.907 13.415 32.185  1.00 37.87  ? 530 HOH A O   1 
HETATM 6426 O O   . HOH D 4 .   ? -15.763 18.578 33.577  1.00 33.34  ? 531 HOH A O   1 
HETATM 6427 O O   . HOH D 4 .   ? -2.154  13.961 5.502   1.00 49.81  ? 532 HOH A O   1 
HETATM 6428 O O   . HOH D 4 .   ? -19.331 26.096 34.945  1.00 33.02  ? 533 HOH A O   1 
HETATM 6429 O O   . HOH D 4 .   ? -20.337 33.541 42.127  1.00 32.94  ? 534 HOH A O   1 
HETATM 6430 O O   . HOH D 4 .   ? -24.343 29.884 26.779  1.00 42.37  ? 535 HOH A O   1 
HETATM 6431 O O   . HOH D 4 .   ? -26.156 28.330 37.540  1.00 32.52  ? 536 HOH A O   1 
HETATM 6432 O O   . HOH D 4 .   ? -21.459 30.721 26.863  1.00 39.59  ? 537 HOH A O   1 
HETATM 6433 O O   . HOH D 4 .   ? 3.635   -3.674 20.282  1.00 41.12  ? 538 HOH A O   1 
HETATM 6434 O O   . HOH D 4 .   ? -31.383 27.329 42.862  1.00 33.35  ? 539 HOH A O   1 
HETATM 6435 O O   . HOH D 4 .   ? -27.526 10.074 46.031  1.00 44.99  ? 540 HOH A O   1 
HETATM 6436 O O   . HOH D 4 .   ? -11.644 0.065  19.935  1.00 53.31  ? 541 HOH A O   1 
HETATM 6437 O O   . HOH D 4 .   ? -9.708  15.076 13.249  1.00 47.23  ? 542 HOH A O   1 
HETATM 6438 O O   . HOH D 4 .   ? -10.889 9.953  29.074  1.00 41.40  ? 543 HOH A O   1 
HETATM 6439 O O   . HOH D 4 .   ? -23.647 38.964 40.671  1.00 43.60  ? 544 HOH A O   1 
HETATM 6440 O O   . HOH D 4 .   ? -16.647 23.119 52.872  1.00 39.40  ? 545 HOH A O   1 
HETATM 6441 O O   . HOH D 4 .   ? -21.094 28.463 52.927  1.00 31.50  ? 546 HOH A O   1 
HETATM 6442 O O   . HOH D 4 .   ? -17.153 27.440 35.381  1.00 37.86  ? 547 HOH A O   1 
HETATM 6443 O O   . HOH D 4 .   ? -11.689 32.621 48.301  1.00 36.09  ? 548 HOH A O   1 
HETATM 6444 O O   . HOH D 4 .   ? -4.109  -1.595 19.838  1.00 39.87  ? 549 HOH A O   1 
HETATM 6445 O O   . HOH D 4 .   ? -13.501 16.036 21.187  1.00 38.34  ? 550 HOH A O   1 
HETATM 6446 O O   . HOH D 4 .   ? -18.667 37.952 36.853  1.00 36.59  ? 551 HOH A O   1 
HETATM 6447 O O   . HOH D 4 .   ? -8.072  14.206 44.453  1.00 46.11  ? 552 HOH A O   1 
HETATM 6448 O O   . HOH D 4 .   ? -25.397 20.034 56.942  1.00 40.87  ? 553 HOH A O   1 
HETATM 6449 O O   . HOH D 4 .   ? -19.433 39.132 50.825  1.00 29.81  ? 554 HOH A O   1 
HETATM 6450 O O   . HOH D 4 .   ? 2.530   -8.217 14.794  1.00 55.85  ? 555 HOH A O   1 
HETATM 6451 O O   . HOH D 4 .   ? -4.468  23.692 38.432  1.00 41.81  ? 556 HOH A O   1 
HETATM 6452 O O   . HOH D 4 .   ? -10.342 31.520 25.498  1.00 44.07  ? 557 HOH A O   1 
HETATM 6453 O O   . HOH D 4 .   ? -0.348  17.368 19.792  1.00 34.61  ? 558 HOH A O   1 
HETATM 6454 O O   . HOH D 4 .   ? -17.978 13.015 48.003  1.00 42.21  ? 559 HOH A O   1 
HETATM 6455 O O   . HOH D 4 .   ? -21.713 25.310 22.210  1.00 48.08  ? 560 HOH A O   1 
HETATM 6456 O O   . HOH D 4 .   ? -23.962 28.759 52.617  1.00 30.14  ? 561 HOH A O   1 
HETATM 6457 O O   . HOH D 4 .   ? -14.169 32.712 23.502  1.00 53.10  ? 562 HOH A O   1 
HETATM 6458 O O   . HOH D 4 .   ? -30.130 32.225 28.217  1.00 48.97  ? 563 HOH A O   1 
HETATM 6459 O O   . HOH D 4 .   ? -35.805 34.069 33.202  1.00 45.59  ? 564 HOH A O   1 
HETATM 6460 O O   . HOH D 4 .   ? -19.512 13.406 26.574  1.00 44.36  ? 565 HOH A O   1 
HETATM 6461 O O   . HOH D 4 .   ? -29.177 28.891 54.628  1.00 35.67  ? 566 HOH A O   1 
HETATM 6462 O O   . HOH D 4 .   ? -33.357 25.807 34.257  1.00 53.22  ? 567 HOH A O   1 
HETATM 6463 O O   . HOH D 4 .   ? -31.308 15.676 39.088  1.00 40.01  ? 568 HOH A O   1 
HETATM 6464 O O   . HOH D 4 .   ? -16.521 10.622 26.133  1.00 41.34  ? 569 HOH A O   1 
HETATM 6465 O O   . HOH D 4 .   ? -15.004 11.980 34.023  1.00 34.03  ? 570 HOH A O   1 
HETATM 6466 O O   . HOH D 4 .   ? -18.954 9.572  49.661  1.00 47.36  ? 571 HOH A O   1 
HETATM 6467 O O   . HOH D 4 .   ? -13.777 5.516  21.547  1.00 37.70  ? 572 HOH A O   1 
HETATM 6468 O O   . HOH D 4 .   ? -20.111 23.981 36.302  1.00 34.54  ? 573 HOH A O   1 
HETATM 6469 O O   . HOH D 4 .   ? -26.194 33.108 42.183  1.00 38.46  ? 574 HOH A O   1 
HETATM 6470 O O   . HOH D 4 .   ? -19.267 16.141 55.906  1.00 44.56  ? 575 HOH A O   1 
HETATM 6471 O O   . HOH D 4 .   ? -17.058 41.236 59.603  1.00 48.28  ? 576 HOH A O   1 
HETATM 6472 O O   . HOH D 4 .   ? 4.931   6.280  32.456  1.00 51.62  ? 577 HOH A O   1 
HETATM 6473 O O   . HOH D 4 .   ? -11.800 19.168 42.620  1.00 33.01  ? 578 HOH A O   1 
HETATM 6474 O O   . HOH D 4 .   ? -8.556  1.262  -0.390  1.00 61.35  ? 579 HOH A O   1 
HETATM 6475 O O   . HOH D 4 .   ? 1.670   24.264 40.636  1.00 49.25  ? 580 HOH A O   1 
HETATM 6476 O O   . HOH D 4 .   ? -26.405 24.302 40.916  1.00 35.60  ? 581 HOH A O   1 
HETATM 6477 O O   . HOH D 4 .   ? -42.767 33.758 38.758  1.00 54.69  ? 582 HOH A O   1 
HETATM 6478 O O   . HOH D 4 .   ? -18.436 19.501 17.650  1.00 53.41  ? 583 HOH A O   1 
HETATM 6479 O O   . HOH D 4 .   ? -9.484  7.250  8.564   1.00 56.02  ? 584 HOH A O   1 
HETATM 6480 O O   . HOH D 4 .   ? -22.183 8.314  38.605  1.00 51.75  ? 585 HOH A O   1 
HETATM 6481 O O   . HOH D 4 .   ? -27.370 10.192 56.162  1.00 46.47  ? 586 HOH A O   1 
HETATM 6482 O O   . HOH D 4 .   ? -32.842 38.629 42.761  1.00 35.39  ? 587 HOH A O   1 
HETATM 6483 O O   . HOH D 4 .   ? -13.495 42.287 35.478  1.00 51.31  ? 588 HOH A O   1 
HETATM 6484 O O   . HOH D 4 .   ? 3.208   25.581 17.262  1.00 58.20  ? 589 HOH A O   1 
HETATM 6485 O O   . HOH D 4 .   ? -0.433  8.395  16.798  1.00 41.09  ? 590 HOH A O   1 
HETATM 6486 O O   . HOH D 4 .   ? -10.941 19.928 15.610  1.00 42.50  ? 591 HOH A O   1 
HETATM 6487 O O   . HOH D 4 .   ? -25.508 10.752 39.278  1.00 38.12  ? 592 HOH A O   1 
HETATM 6488 O O   . HOH D 4 .   ? -4.275  7.924  30.088  1.00 47.48  ? 593 HOH A O   1 
HETATM 6489 O O   . HOH D 4 .   ? 3.645   -2.988 26.197  1.00 51.59  ? 594 HOH A O   1 
HETATM 6490 O O   . HOH D 4 .   ? 1.022   18.786 39.556  1.00 43.54  ? 595 HOH A O   1 
HETATM 6491 O O   . HOH D 4 .   ? -34.484 42.967 49.153  1.00 39.79  ? 596 HOH A O   1 
HETATM 6492 O O   . HOH D 4 .   ? -21.839 8.229  48.612  1.00 51.89  ? 597 HOH A O   1 
HETATM 6493 O O   . HOH D 4 .   ? -12.985 33.288 25.955  1.00 47.37  ? 598 HOH A O   1 
HETATM 6494 O O   . HOH D 4 .   ? -13.089 26.128 20.758  1.00 41.07  ? 599 HOH A O   1 
HETATM 6495 O O   . HOH D 4 .   ? -21.253 14.444 55.366  1.00 44.35  ? 600 HOH A O   1 
HETATM 6496 O O   . HOH D 4 .   ? 4.438   29.340 21.270  1.00 51.85  ? 601 HOH A O   1 
HETATM 6497 O O   . HOH D 4 .   ? -28.520 15.889 34.017  1.00 41.60  ? 602 HOH A O   1 
HETATM 6498 O O   . HOH D 4 .   ? -11.988 11.369 34.096  1.00 42.54  ? 603 HOH A O   1 
HETATM 6499 O O   . HOH D 4 .   ? -27.068 6.123  48.678  1.00 57.56  ? 604 HOH A O   1 
HETATM 6500 O O   . HOH D 4 .   ? -23.550 8.485  36.470  1.00 49.23  ? 605 HOH A O   1 
HETATM 6501 O O   . HOH D 4 .   ? 0.554   -2.960 24.702  1.00 52.61  ? 606 HOH A O   1 
HETATM 6502 O O   . HOH D 4 .   ? -28.918 18.204 34.194  1.00 48.73  ? 607 HOH A O   1 
HETATM 6503 O O   . HOH D 4 .   ? -6.388  44.474 43.100  1.00 54.31  ? 608 HOH A O   1 
HETATM 6504 O O   . HOH D 4 .   ? -19.325 12.584 43.089  1.00 42.66  ? 609 HOH A O   1 
HETATM 6505 O O   . HOH D 4 .   ? -41.002 44.706 39.261  1.00 56.53  ? 610 HOH A O   1 
HETATM 6506 O O   . HOH D 4 .   ? -6.808  7.023  29.641  1.00 46.67  ? 611 HOH A O   1 
HETATM 6507 O O   . HOH D 4 .   ? -9.410  7.408  30.400  1.00 47.95  ? 612 HOH A O   1 
HETATM 6508 O O   . HOH D 4 .   ? -20.142 9.733  44.123  1.00 45.15  ? 613 HOH A O   1 
HETATM 6509 O O   . HOH D 4 .   ? -29.474 46.134 57.533  1.00 43.20  ? 614 HOH A O   1 
HETATM 6510 O O   . HOH D 4 .   ? -3.454  32.812 24.746  1.00 49.83  ? 615 HOH A O   1 
HETATM 6511 O O   . HOH D 4 .   ? 1.303   19.727 21.663  1.00 40.41  ? 616 HOH A O   1 
HETATM 6512 O O   . HOH D 4 .   ? -18.153 21.501 18.703  1.00 53.28  ? 617 HOH A O   1 
HETATM 6513 O O   . HOH D 4 .   ? 3.488   16.951 37.479  1.00 43.14  ? 618 HOH A O   1 
HETATM 6514 O O   . HOH D 4 .   ? 10.079  -2.345 12.862  1.00 53.99  ? 619 HOH A O   1 
HETATM 6515 O O   . HOH D 4 .   ? 4.732   26.671 19.200  1.00 51.03  ? 620 HOH A O   1 
HETATM 6516 O O   . HOH D 4 .   ? -27.191 8.910  38.005  1.00 48.48  ? 621 HOH A O   1 
HETATM 6517 O O   . HOH D 4 .   ? 12.256  3.303  18.530  1.00 55.82  ? 622 HOH A O   1 
HETATM 6518 O O   . HOH D 4 .   ? 4.000   19.098 21.611  1.00 45.90  ? 623 HOH A O   1 
HETATM 6519 O O   . HOH D 4 .   ? -19.100 10.326 26.221  1.00 48.81  ? 624 HOH A O   1 
HETATM 6520 O O   . HOH D 4 .   ? -20.833 28.367 55.613  1.00 45.04  ? 625 HOH A O   1 
HETATM 6521 O O   . HOH D 4 .   ? -13.391 27.703 18.630  1.00 53.35  ? 626 HOH A O   1 
HETATM 6522 O O   . HOH D 4 .   ? -2.139  32.707 27.116  1.00 49.96  ? 627 HOH A O   1 
HETATM 6523 O O   . HOH D 4 .   ? 0.031   33.364 27.664  1.00 60.40  ? 628 HOH A O   1 
HETATM 6524 O O   . HOH D 4 .   ? -32.920 23.778 35.973  1.00 51.66  ? 629 HOH A O   1 
HETATM 6525 O O   . HOH D 4 .   ? -33.339 13.508 40.013  1.00 49.09  ? 630 HOH A O   1 
HETATM 6526 O O   . HOH E 4 .   ? -47.625 76.527 91.099  1.00 63.86  ? 301 HOH B O   1 
HETATM 6527 O O   . HOH E 4 .   ? -46.784 49.447 71.676  1.00 40.87  ? 302 HOH B O   1 
HETATM 6528 O O   . HOH E 4 .   ? -63.193 62.459 85.446  1.00 49.41  ? 303 HOH B O   1 
HETATM 6529 O O   . HOH E 4 .   ? -51.234 59.515 75.830  1.00 46.70  ? 304 HOH B O   1 
HETATM 6530 O O   . HOH E 4 .   ? -64.993 43.480 57.674  1.00 44.74  ? 305 HOH B O   1 
HETATM 6531 O O   . HOH E 4 .   ? -44.028 80.609 80.100  1.00 53.59  ? 306 HOH B O   1 
HETATM 6532 O O   . HOH E 4 .   ? -56.714 55.196 61.494  1.00 51.42  ? 307 HOH B O   1 
HETATM 6533 O O   . HOH E 4 .   ? -50.405 57.720 78.323  1.00 47.77  ? 308 HOH B O   1 
HETATM 6534 O O   . HOH E 4 .   ? -68.403 50.403 61.297  1.00 45.37  ? 309 HOH B O   1 
HETATM 6535 O O   . HOH E 4 .   ? -45.538 76.627 70.443  1.00 39.57  ? 310 HOH B O   1 
HETATM 6536 O O   . HOH E 4 .   ? -40.107 83.047 74.011  1.00 34.14  ? 311 HOH B O   1 
HETATM 6537 O O   . HOH E 4 .   ? -55.584 59.539 60.512  1.00 54.09  ? 312 HOH B O   1 
HETATM 6538 O O   . HOH E 4 .   ? -51.518 56.682 56.126  1.00 49.19  ? 313 HOH B O   1 
HETATM 6539 O O   . HOH E 4 .   ? -60.818 39.669 69.147  1.00 41.08  ? 314 HOH B O   1 
HETATM 6540 O O   . HOH E 4 .   ? -58.678 32.647 61.671  1.00 49.82  ? 315 HOH B O   1 
HETATM 6541 O O   . HOH E 4 .   ? -66.673 43.514 61.372  1.00 41.64  ? 316 HOH B O   1 
HETATM 6542 O O   . HOH E 4 .   ? -37.615 37.903 48.145  1.00 39.58  ? 317 HOH B O   1 
HETATM 6543 O O   . HOH E 4 .   ? -44.095 86.494 76.292  1.00 50.70  ? 318 HOH B O   1 
HETATM 6544 O O   . HOH E 4 .   ? -54.299 36.344 68.838  1.00 48.22  ? 319 HOH B O   1 
HETATM 6545 O O   . HOH E 4 .   ? -51.976 40.427 70.716  1.00 45.16  ? 320 HOH B O   1 
HETATM 6546 O O   . HOH E 4 .   ? -41.046 25.698 56.204  1.00 37.83  ? 321 HOH B O   1 
HETATM 6547 O O   . HOH E 4 .   ? -34.863 86.396 77.547  1.00 37.79  ? 322 HOH B O   1 
HETATM 6548 O O   . HOH E 4 .   ? -47.374 38.048 50.897  1.00 41.98  ? 323 HOH B O   1 
HETATM 6549 O O   . HOH E 4 .   ? -36.112 49.455 48.407  1.00 52.01  ? 324 HOH B O   1 
HETATM 6550 O O   . HOH E 4 .   ? -57.269 54.809 70.692  1.00 34.14  ? 325 HOH B O   1 
HETATM 6551 O O   . HOH E 4 .   ? -44.064 44.419 48.040  1.00 40.33  ? 326 HOH B O   1 
HETATM 6552 O O   . HOH E 4 .   ? -41.472 68.995 73.165  1.00 45.50  ? 327 HOH B O   1 
HETATM 6553 O O   . HOH E 4 .   ? -54.430 49.652 49.762  1.00 47.30  ? 328 HOH B O   1 
HETATM 6554 O O   . HOH E 4 .   ? -66.133 51.449 64.743  1.00 42.94  ? 329 HOH B O   1 
HETATM 6555 O O   . HOH E 4 .   ? -56.088 66.500 65.753  1.00 47.06  ? 330 HOH B O   1 
HETATM 6556 O O   . HOH E 4 .   ? -50.606 34.689 67.210  1.00 46.16  ? 331 HOH B O   1 
HETATM 6557 O O   . HOH E 4 .   ? -71.378 45.279 63.686  1.00 47.36  ? 332 HOH B O   1 
HETATM 6558 O O   . HOH E 4 .   ? -45.793 36.607 68.624  1.00 37.53  ? 333 HOH B O   1 
HETATM 6559 O O   . HOH E 4 .   ? -44.605 58.511 55.135  1.00 51.91  ? 334 HOH B O   1 
HETATM 6560 O O   . HOH E 4 .   ? -51.195 56.390 68.670  1.00 36.15  ? 335 HOH B O   1 
HETATM 6561 O O   . HOH E 4 .   ? -48.715 49.093 73.316  1.00 36.47  ? 336 HOH B O   1 
HETATM 6562 O O   . HOH E 4 .   ? -63.021 73.117 81.491  1.00 63.05  ? 337 HOH B O   1 
HETATM 6563 O O   . HOH E 4 .   ? -49.840 61.615 84.711  1.00 47.95  ? 338 HOH B O   1 
HETATM 6564 O O   . HOH E 4 .   ? -55.387 76.787 72.054  1.00 49.25  ? 339 HOH B O   1 
HETATM 6565 O O   . HOH E 4 .   ? -66.970 49.021 75.584  1.00 53.16  ? 340 HOH B O   1 
HETATM 6566 O O   . HOH E 4 .   ? -58.591 73.817 77.847  1.00 55.25  ? 341 HOH B O   1 
HETATM 6567 O O   . HOH E 4 .   ? -37.818 76.656 73.231  1.00 47.63  ? 342 HOH B O   1 
HETATM 6568 O O   . HOH E 4 .   ? -62.344 39.023 57.003  1.00 47.15  ? 343 HOH B O   1 
HETATM 6569 O O   . HOH E 4 .   ? -31.272 44.993 56.762  1.00 46.35  ? 344 HOH B O   1 
HETATM 6570 O O   . HOH E 4 .   ? -73.227 47.796 63.983  1.00 49.17  ? 345 HOH B O   1 
HETATM 6571 O O   . HOH E 4 .   ? -39.224 35.497 48.481  1.00 40.47  ? 346 HOH B O   1 
HETATM 6572 O O   . HOH E 4 .   ? -60.459 51.858 62.570  1.00 52.60  ? 347 HOH B O   1 
HETATM 6573 O O   . HOH E 4 .   ? -37.469 52.197 61.607  1.00 48.39  ? 348 HOH B O   1 
HETATM 6574 O O   . HOH E 4 .   ? -38.642 49.864 50.099  1.00 45.55  ? 349 HOH B O   1 
HETATM 6575 O O   . HOH E 4 .   ? -59.094 55.235 64.439  1.00 56.65  ? 350 HOH B O   1 
HETATM 6576 O O   . HOH E 4 .   ? -41.132 23.185 44.725  1.00 50.87  ? 351 HOH B O   1 
HETATM 6577 O O   . HOH E 4 .   ? -51.662 61.967 85.733  1.00 49.28  ? 352 HOH B O   1 
HETATM 6578 O O   . HOH E 4 .   ? -58.992 53.969 62.668  1.00 57.33  ? 353 HOH B O   1 
HETATM 6579 O O   . HOH E 4 .   ? -35.927 76.642 74.212  1.00 53.65  ? 354 HOH B O   1 
HETATM 6580 O O   . HOH E 4 .   ? -70.487 41.363 63.217  1.00 55.51  ? 355 HOH B O   1 
HETATM 6581 O O   . HOH E 4 .   ? -59.739 31.966 64.196  1.00 51.25  ? 356 HOH B O   1 
HETATM 6582 O O   . HOH E 4 .   ? -39.675 46.657 40.195  1.00 55.73  ? 357 HOH B O   1 
HETATM 6583 O O   . HOH E 4 .   ? -41.441 66.606 73.928  1.00 51.20  ? 358 HOH B O   1 
HETATM 6584 O O   . HOH E 4 .   ? -40.466 23.252 56.870  1.00 54.24  ? 359 HOH B O   1 
HETATM 6585 O O   . HOH E 4 .   ? -31.411 47.451 57.257  1.00 47.31  ? 360 HOH B O   1 
HETATM 6586 O O   . HOH F 4 .   ? -31.674 49.196 62.424  1.00 46.18  ? 301 HOH C O   1 
HETATM 6587 O O   . HOH F 4 .   ? -57.063 73.832 106.093 1.00 65.71  ? 302 HOH C O   1 
HETATM 6588 O O   . HOH F 4 .   ? -45.939 28.575 56.898  1.00 42.87  ? 303 HOH C O   1 
HETATM 6589 O O   . HOH F 4 .   ? -19.972 43.435 70.381  1.00 49.31  ? 304 HOH C O   1 
HETATM 6590 O O   . HOH F 4 .   ? -25.133 32.044 65.544  1.00 44.45  ? 305 HOH C O   1 
HETATM 6591 O O   . HOH F 4 .   ? -32.220 23.515 63.138  1.00 43.25  ? 306 HOH C O   1 
HETATM 6592 O O   . HOH F 4 .   ? -31.777 35.029 58.273  1.00 29.50  ? 307 HOH C O   1 
HETATM 6593 O O   . HOH F 4 .   ? -30.651 55.084 81.746  1.00 46.74  ? 308 HOH C O   1 
HETATM 6594 O O   . HOH F 4 .   ? -67.881 71.694 94.076  1.00 63.90  ? 309 HOH C O   1 
HETATM 6595 O O   . HOH F 4 .   ? -43.355 33.501 74.650  1.00 47.80  ? 310 HOH C O   1 
HETATM 6596 O O   . HOH F 4 .   ? -37.328 51.765 70.221  1.00 40.84  ? 311 HOH C O   1 
HETATM 6597 O O   . HOH F 4 .   ? -33.893 37.815 76.273  1.00 31.90  ? 312 HOH C O   1 
HETATM 6598 O O   . HOH F 4 .   ? -35.428 48.801 62.754  1.00 36.75  ? 313 HOH C O   1 
HETATM 6599 O O   . HOH F 4 .   ? -29.005 35.378 68.327  1.00 27.73  ? 314 HOH C O   1 
HETATM 6600 O O   . HOH F 4 .   ? -26.441 55.770 84.344  1.00 50.94  ? 315 HOH C O   1 
HETATM 6601 O O   . HOH F 4 .   ? -37.446 26.444 57.134  1.00 37.59  ? 316 HOH C O   1 
HETATM 6602 O O   . HOH F 4 .   ? -46.642 36.814 65.678  1.00 30.62  ? 317 HOH C O   1 
HETATM 6603 O O   . HOH F 4 .   ? -43.455 33.220 70.781  1.00 35.31  ? 318 HOH C O   1 
HETATM 6604 O O   . HOH F 4 .   ? -43.365 24.021 69.198  1.00 48.65  ? 319 HOH C O   1 
HETATM 6605 O O   . HOH F 4 .   ? -23.574 39.832 66.196  1.00 42.53  ? 320 HOH C O   1 
HETATM 6606 O O   . HOH F 4 .   ? -44.598 29.498 64.435  1.00 41.00  ? 321 HOH C O   1 
HETATM 6607 O O   . HOH F 4 .   ? -24.924 56.906 89.929  1.00 45.80  ? 322 HOH C O   1 
HETATM 6608 O O   . HOH F 4 .   ? -60.899 65.022 102.192 1.00 56.04  ? 323 HOH C O   1 
HETATM 6609 O O   . HOH F 4 .   ? -37.633 51.066 63.750  1.00 43.14  ? 324 HOH C O   1 
HETATM 6610 O O   . HOH F 4 .   ? -55.502 72.850 87.251  1.00 50.47  ? 325 HOH C O   1 
HETATM 6611 O O   . HOH F 4 .   ? -41.954 47.110 75.395  1.00 41.82  ? 326 HOH C O   1 
HETATM 6612 O O   . HOH F 4 .   ? -40.313 37.404 78.702  1.00 35.82  ? 327 HOH C O   1 
HETATM 6613 O O   . HOH F 4 .   ? -21.475 42.137 72.327  1.00 42.19  ? 328 HOH C O   1 
HETATM 6614 O O   . HOH F 4 .   ? -41.415 57.454 80.398  1.00 55.92  ? 329 HOH C O   1 
HETATM 6615 O O   . HOH F 4 .   ? -40.584 35.243 76.895  1.00 35.75  ? 330 HOH C O   1 
HETATM 6616 O O   . HOH F 4 .   ? -44.276 38.669 72.213  1.00 37.93  ? 331 HOH C O   1 
HETATM 6617 O O   . HOH F 4 .   ? -50.630 58.954 94.537  1.00 56.53  ? 332 HOH C O   1 
HETATM 6618 O O   . HOH F 4 .   ? -37.571 59.814 83.832  1.00 50.39  ? 333 HOH C O   1 
HETATM 6619 O O   . HOH F 4 .   ? -47.619 56.251 96.555  1.00 55.54  ? 334 HOH C O   1 
HETATM 6620 O O   . HOH F 4 .   ? -31.905 56.515 74.128  1.00 46.45  ? 335 HOH C O   1 
HETATM 6621 O O   . HOH F 4 .   ? -43.844 25.161 52.787  1.00 41.39  ? 336 HOH C O   1 
HETATM 6622 O O   . HOH F 4 .   ? -41.818 30.243 61.595  1.00 32.10  ? 337 HOH C O   1 
HETATM 6623 O O   . HOH F 4 .   ? -25.157 54.276 86.458  1.00 46.44  ? 338 HOH C O   1 
HETATM 6624 O O   . HOH F 4 .   ? -47.599 34.306 62.993  1.00 38.33  ? 339 HOH C O   1 
HETATM 6625 O O   . HOH F 4 .   ? -41.835 32.010 59.943  1.00 31.43  ? 340 HOH C O   1 
HETATM 6626 O O   . HOH F 4 .   ? -29.084 52.063 72.564  1.00 44.09  ? 341 HOH C O   1 
HETATM 6627 O O   . HOH F 4 .   ? -27.256 37.140 57.153  1.00 23.22  ? 342 HOH C O   1 
HETATM 6628 O O   . HOH F 4 .   ? -25.704 56.293 77.210  1.00 45.02  ? 343 HOH C O   1 
HETATM 6629 O O   . HOH F 4 .   ? -34.417 25.319 59.677  1.00 40.25  ? 344 HOH C O   1 
HETATM 6630 O O   . HOH F 4 .   ? -41.044 54.777 66.472  1.00 41.89  ? 345 HOH C O   1 
HETATM 6631 O O   . HOH F 4 .   ? -18.919 39.495 72.658  1.00 57.08  ? 346 HOH C O   1 
HETATM 6632 O O   . HOH F 4 .   ? -36.893 20.655 66.534  1.00 45.80  ? 347 HOH C O   1 
HETATM 6633 O O   . HOH F 4 .   ? -34.087 49.804 87.800  1.00 55.19  ? 348 HOH C O   1 
HETATM 6634 O O   . HOH F 4 .   ? -52.577 55.445 90.780  1.00 49.52  ? 349 HOH C O   1 
HETATM 6635 O O   . HOH F 4 .   ? -23.629 54.565 71.112  1.00 50.20  ? 350 HOH C O   1 
HETATM 6636 O O   . HOH F 4 .   ? -46.954 54.305 86.063  1.00 46.05  ? 351 HOH C O   1 
HETATM 6637 O O   . HOH F 4 .   ? -26.263 39.075 81.898  1.00 50.44  ? 352 HOH C O   1 
HETATM 6638 O O   . HOH F 4 .   ? -35.479 22.617 78.384  1.00 57.48  ? 353 HOH C O   1 
HETATM 6639 O O   . HOH F 4 .   ? -29.783 51.381 69.238  1.00 53.90  ? 354 HOH C O   1 
HETATM 6640 O O   . HOH F 4 .   ? -45.363 36.660 72.359  1.00 46.19  ? 355 HOH C O   1 
HETATM 6641 O O   . HOH F 4 .   ? -30.956 41.415 87.174  1.00 53.95  ? 356 HOH C O   1 
HETATM 6642 O O   . HOH F 4 .   ? -20.784 50.283 70.828  1.00 43.13  ? 357 HOH C O   1 
HETATM 6643 O O   . HOH F 4 .   ? -32.624 39.270 87.167  1.00 52.05  ? 358 HOH C O   1 
HETATM 6644 O O   . HOH F 4 .   ? -50.697 62.016 87.768  1.00 45.17  ? 359 HOH C O   1 
HETATM 6645 O O   . HOH F 4 .   ? -35.516 50.531 90.630  1.00 53.92  ? 360 HOH C O   1 
HETATM 6646 O O   . HOH F 4 .   ? -22.079 41.067 62.312  1.00 45.95  ? 361 HOH C O   1 
HETATM 6647 O O   . HOH F 4 .   ? -40.609 41.880 80.508  1.00 45.07  ? 362 HOH C O   1 
HETATM 6648 O O   . HOH F 4 .   ? -41.936 49.553 75.423  1.00 43.65  ? 363 HOH C O   1 
HETATM 6649 O O   . HOH F 4 .   ? -28.237 52.978 70.496  1.00 49.73  ? 364 HOH C O   1 
HETATM 6650 O O   . HOH F 4 .   ? -53.030 53.938 88.713  1.00 60.03  ? 365 HOH C O   1 
HETATM 6651 O O   . HOH F 4 .   ? -42.198 43.225 79.143  1.00 53.46  ? 366 HOH C O   1 
HETATM 6652 O O   . HOH F 4 .   ? -48.014 35.105 68.699  1.00 52.45  ? 367 HOH C O   1 
HETATM 6653 O O   . HOH F 4 .   ? -40.913 43.142 82.937  1.00 58.17  ? 368 HOH C O   1 
HETATM 6654 O O   . HOH F 4 .   ? -42.621 33.522 77.440  1.00 43.00  ? 369 HOH C O   1 
# 
