data_9BTP
# 
_entry.id   9BTP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BTP         pdb_00009btp 10.2210/pdb9btp/pdb 
WWPDB D_1000283966 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-05-07 ? 
3 'Structure model' 1 2 2025-05-21 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
4 3 '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_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.title'                   
7  2 'Structure model' '_citation.year'                    
8  3 'Structure model' '_citation.pdbx_database_id_DOI'    
9  3 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 3 'Structure model' '_citation.title'                   
11 3 'Structure model' '_citation_author.identifier_ORCID' 
12 3 '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                        9BTP 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_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           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 zachary.hauseman@novartis.com Zachary Hauseman J 'principal investigator/group leader' 0000-0002-0260-2326 
3 dan.king@novartis.com         Daniel  King     A 'principal investigator/group leader' 0000-0002-2581-2318 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dhembi, A.'     1 0000-0002-4698-9008 
'Hauseman, Z.J.' 2 0000-0002-0260-2326 
'King, D.'       3 0000-0002-2581-2318 
# 
_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            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Targeting the SHOC2-RAS interaction in RAS-mutant cancers.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-025-08931-1 
_citation.pdbx_database_id_PubMed   40335703 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hauseman, Z.J.'        1  ?                   
primary 'Stauffer, F.'          2  ?                   
primary 'Beyer, K.S.'           3  0000-0002-3047-304X 
primary 'Molle, S.'             4  0009-0000-3288-7513 
primary 'Cavicchioli, E.'       5  ?                   
primary 'Marchand, J.R.'        6  0000-0002-8002-9457 
primary 'Fodor, M.'             7  ?                   
primary 'Viscomi, J.'           8  ?                   
primary 'Dhembi, A.'            9  ?                   
primary 'Katz, S.'              10 0009-0006-8730-9351 
primary 'Faggion, B.'           11 ?                   
primary 'Lanter, M.'            12 ?                   
primary 'Kerr, G.'              13 0009-0004-4231-518X 
primary 'Schildknecht, D.'      14 ?                   
primary 'Handl, C.'             15 ?                   
primary 'Maddalo, D.'           16 ?                   
primary 'Pissot Soldermann, C.' 17 ?                   
primary 'Brady, J.'             18 ?                   
primary 'Shrestha, O.'          19 ?                   
primary 'Nguyen, Z.'            20 ?                   
primary 'Leder, L.'             21 0009-0002-4378-6739 
primary 'Cremosnik, G.'         22 ?                   
primary 'Lopez Romero, S.'      23 ?                   
primary 'Hassiepen, U.'         24 ?                   
primary 'Stams, T.'             25 ?                   
primary 'Linder, M.'            26 ?                   
primary 'Galli, G.G.'           27 0000-0002-9401-060X 
primary 'Guthy, D.A.'           28 0000-0001-5324-8585 
primary 'King, D.A.'            29 ?                   
primary 'Maira, S.M.'           30 ?                   
primary 'Thoma, C.R.'           31 ?                   
primary 'Ehmke, V.'             32 ?                   
primary 'Tordella, L.'          33 0000-0002-0542-7834 
# 
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 'Leucine-rich repeat protein SHOC-2' 56737.582 1   ? ? 'residues 80-582' ? 
2 non-polymer syn 
;(2S)-{2-[(4-chloro[1,1'-biphenyl]-3-yl)methoxy]phenyl}[(2-oxo-2,3-dihydro-1,3-benzoxazol-5-yl)amino]acetic acid
;
500.930   1   ? ? ?                 ? 
3 non-polymer syn 'POTASSIUM ION' 39.098    1   ? ? ?                 ? 
4 water       nat water 18.015    148 ? ? ?                 ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Protein soc-2 homolog,Protein sur-8 homolog' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENS
LTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGEL
CNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENN
NISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLD
FGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLV
LTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLP
PQIVAGGPSFIIQFLKMQGPYRAMV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENS
LTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGEL
CNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENN
NISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLD
FGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLV
LTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLP
PQIVAGGPSFIIQFLKMQGPYRAMV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(2S)-{2-[(4-chloro[1,1'-biphenyl]-3-yl)methoxy]phenyl}[(2-oxo-2,3-dihydro-1,3-benzoxazol-5-yl)amino]acetic acid
;
A1ATZ 
3 'POTASSIUM ION'                                                                                                   K     
4 water                                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   THR n 
1 5   ARG n 
1 6   LYS n 
1 7   LYS n 
1 8   SER n 
1 9   SER n 
1 10  ASN n 
1 11  ALA n 
1 12  GLU n 
1 13  VAL n 
1 14  ILE n 
1 15  LYS n 
1 16  GLU n 
1 17  LEU n 
1 18  ASN n 
1 19  LYS n 
1 20  CYS n 
1 21  ARG n 
1 22  GLU n 
1 23  GLU n 
1 24  ASN n 
1 25  SER n 
1 26  MET n 
1 27  ARG n 
1 28  LEU n 
1 29  ASP n 
1 30  LEU n 
1 31  SER n 
1 32  LYS n 
1 33  ARG n 
1 34  SER n 
1 35  ILE n 
1 36  HIS n 
1 37  ILE n 
1 38  LEU n 
1 39  PRO n 
1 40  SER n 
1 41  SER n 
1 42  ILE n 
1 43  LYS n 
1 44  GLU n 
1 45  LEU n 
1 46  THR n 
1 47  GLN n 
1 48  LEU n 
1 49  THR n 
1 50  GLU n 
1 51  LEU n 
1 52  TYR n 
1 53  LEU n 
1 54  TYR n 
1 55  SER n 
1 56  ASN n 
1 57  LYS n 
1 58  LEU n 
1 59  GLN n 
1 60  SER n 
1 61  LEU n 
1 62  PRO n 
1 63  ALA n 
1 64  GLU n 
1 65  VAL n 
1 66  GLY n 
1 67  CYS n 
1 68  LEU n 
1 69  VAL n 
1 70  ASN n 
1 71  LEU n 
1 72  MET n 
1 73  THR n 
1 74  LEU n 
1 75  ALA n 
1 76  LEU n 
1 77  SER n 
1 78  GLU n 
1 79  ASN n 
1 80  SER n 
1 81  LEU n 
1 82  THR n 
1 83  SER n 
1 84  LEU n 
1 85  PRO n 
1 86  ASP n 
1 87  SER n 
1 88  LEU n 
1 89  ASP n 
1 90  ASN n 
1 91  LEU n 
1 92  LYS n 
1 93  LYS n 
1 94  LEU n 
1 95  ARG n 
1 96  MET n 
1 97  LEU n 
1 98  ASP n 
1 99  LEU n 
1 100 ARG n 
1 101 HIS n 
1 102 ASN n 
1 103 LYS n 
1 104 LEU n 
1 105 ARG n 
1 106 GLU n 
1 107 ILE n 
1 108 PRO n 
1 109 SER n 
1 110 VAL n 
1 111 VAL n 
1 112 TYR n 
1 113 ARG n 
1 114 LEU n 
1 115 ASP n 
1 116 SER n 
1 117 LEU n 
1 118 THR n 
1 119 THR n 
1 120 LEU n 
1 121 TYR n 
1 122 LEU n 
1 123 ARG n 
1 124 PHE n 
1 125 ASN n 
1 126 ARG n 
1 127 ILE n 
1 128 THR n 
1 129 THR n 
1 130 VAL n 
1 131 GLU n 
1 132 LYS n 
1 133 ASP n 
1 134 ILE n 
1 135 LYS n 
1 136 ASN n 
1 137 LEU n 
1 138 SER n 
1 139 LYS n 
1 140 LEU n 
1 141 SER n 
1 142 MET n 
1 143 LEU n 
1 144 SER n 
1 145 ILE n 
1 146 ARG n 
1 147 GLU n 
1 148 ASN n 
1 149 LYS n 
1 150 ILE n 
1 151 LYS n 
1 152 GLN n 
1 153 LEU n 
1 154 PRO n 
1 155 ALA n 
1 156 GLU n 
1 157 ILE n 
1 158 GLY n 
1 159 GLU n 
1 160 LEU n 
1 161 CYS n 
1 162 ASN n 
1 163 LEU n 
1 164 ILE n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 VAL n 
1 169 ALA n 
1 170 HIS n 
1 171 ASN n 
1 172 GLN n 
1 173 LEU n 
1 174 GLU n 
1 175 HIS n 
1 176 LEU n 
1 177 PRO n 
1 178 LYS n 
1 179 GLU n 
1 180 ILE n 
1 181 GLY n 
1 182 ASN n 
1 183 CYS n 
1 184 THR n 
1 185 GLN n 
1 186 ILE n 
1 187 THR n 
1 188 ASN n 
1 189 LEU n 
1 190 ASP n 
1 191 LEU n 
1 192 GLN n 
1 193 HIS n 
1 194 ASN n 
1 195 GLU n 
1 196 LEU n 
1 197 LEU n 
1 198 ASP n 
1 199 LEU n 
1 200 PRO n 
1 201 ASP n 
1 202 THR n 
1 203 ILE n 
1 204 GLY n 
1 205 ASN n 
1 206 LEU n 
1 207 SER n 
1 208 SER n 
1 209 LEU n 
1 210 SER n 
1 211 ARG n 
1 212 LEU n 
1 213 GLY n 
1 214 LEU n 
1 215 ARG n 
1 216 TYR n 
1 217 ASN n 
1 218 ARG n 
1 219 LEU n 
1 220 SER n 
1 221 ALA n 
1 222 ILE n 
1 223 PRO n 
1 224 ARG n 
1 225 SER n 
1 226 LEU n 
1 227 ALA n 
1 228 LYS n 
1 229 CYS n 
1 230 SER n 
1 231 ALA n 
1 232 LEU n 
1 233 GLU n 
1 234 GLU n 
1 235 LEU n 
1 236 ASN n 
1 237 LEU n 
1 238 GLU n 
1 239 ASN n 
1 240 ASN n 
1 241 ASN n 
1 242 ILE n 
1 243 SER n 
1 244 THR n 
1 245 LEU n 
1 246 PRO n 
1 247 GLU n 
1 248 SER n 
1 249 LEU n 
1 250 LEU n 
1 251 SER n 
1 252 SER n 
1 253 LEU n 
1 254 VAL n 
1 255 LYS n 
1 256 LEU n 
1 257 ASN n 
1 258 SER n 
1 259 LEU n 
1 260 THR n 
1 261 LEU n 
1 262 ALA n 
1 263 ARG n 
1 264 ASN n 
1 265 CYS n 
1 266 PHE n 
1 267 GLN n 
1 268 LEU n 
1 269 TYR n 
1 270 PRO n 
1 271 VAL n 
1 272 GLY n 
1 273 GLY n 
1 274 PRO n 
1 275 SER n 
1 276 GLN n 
1 277 PHE n 
1 278 SER n 
1 279 THR n 
1 280 ILE n 
1 281 TYR n 
1 282 SER n 
1 283 LEU n 
1 284 ASN n 
1 285 MET n 
1 286 GLU n 
1 287 HIS n 
1 288 ASN n 
1 289 ARG n 
1 290 ILE n 
1 291 ASN n 
1 292 LYS n 
1 293 ILE n 
1 294 PRO n 
1 295 PHE n 
1 296 GLY n 
1 297 ILE n 
1 298 PHE n 
1 299 SER n 
1 300 ARG n 
1 301 ALA n 
1 302 LYS n 
1 303 VAL n 
1 304 LEU n 
1 305 SER n 
1 306 LYS n 
1 307 LEU n 
1 308 ASN n 
1 309 MET n 
1 310 LYS n 
1 311 ASP n 
1 312 ASN n 
1 313 GLN n 
1 314 LEU n 
1 315 THR n 
1 316 SER n 
1 317 LEU n 
1 318 PRO n 
1 319 LEU n 
1 320 ASP n 
1 321 PHE n 
1 322 GLY n 
1 323 THR n 
1 324 TRP n 
1 325 THR n 
1 326 SER n 
1 327 MET n 
1 328 VAL n 
1 329 GLU n 
1 330 LEU n 
1 331 ASN n 
1 332 LEU n 
1 333 ALA n 
1 334 THR n 
1 335 ASN n 
1 336 GLN n 
1 337 LEU n 
1 338 THR n 
1 339 LYS n 
1 340 ILE n 
1 341 PRO n 
1 342 GLU n 
1 343 ASP n 
1 344 VAL n 
1 345 SER n 
1 346 GLY n 
1 347 LEU n 
1 348 VAL n 
1 349 SER n 
1 350 LEU n 
1 351 GLU n 
1 352 VAL n 
1 353 LEU n 
1 354 ILE n 
1 355 LEU n 
1 356 SER n 
1 357 ASN n 
1 358 ASN n 
1 359 LEU n 
1 360 LEU n 
1 361 LYS n 
1 362 LYS n 
1 363 LEU n 
1 364 PRO n 
1 365 HIS n 
1 366 GLY n 
1 367 LEU n 
1 368 GLY n 
1 369 ASN n 
1 370 LEU n 
1 371 ARG n 
1 372 LYS n 
1 373 LEU n 
1 374 ARG n 
1 375 GLU n 
1 376 LEU n 
1 377 ASP n 
1 378 LEU n 
1 379 GLU n 
1 380 GLU n 
1 381 ASN n 
1 382 LYS n 
1 383 LEU n 
1 384 GLU n 
1 385 SER n 
1 386 LEU n 
1 387 PRO n 
1 388 ASN n 
1 389 GLU n 
1 390 ILE n 
1 391 ALA n 
1 392 TYR n 
1 393 LEU n 
1 394 LYS n 
1 395 ASP n 
1 396 LEU n 
1 397 GLN n 
1 398 LYS n 
1 399 LEU n 
1 400 VAL n 
1 401 LEU n 
1 402 THR n 
1 403 ASN n 
1 404 ASN n 
1 405 GLN n 
1 406 LEU n 
1 407 THR n 
1 408 THR n 
1 409 LEU n 
1 410 PRO n 
1 411 ARG n 
1 412 GLY n 
1 413 ILE n 
1 414 GLY n 
1 415 HIS n 
1 416 LEU n 
1 417 THR n 
1 418 ASN n 
1 419 LEU n 
1 420 THR n 
1 421 HIS n 
1 422 LEU n 
1 423 GLY n 
1 424 LEU n 
1 425 GLY n 
1 426 GLU n 
1 427 ASN n 
1 428 LEU n 
1 429 LEU n 
1 430 THR n 
1 431 HIS n 
1 432 LEU n 
1 433 PRO n 
1 434 GLU n 
1 435 GLU n 
1 436 ILE n 
1 437 GLY n 
1 438 THR n 
1 439 LEU n 
1 440 GLU n 
1 441 ASN n 
1 442 LEU n 
1 443 GLU n 
1 444 GLU n 
1 445 LEU n 
1 446 TYR n 
1 447 LEU n 
1 448 ASN n 
1 449 ASP n 
1 450 ASN n 
1 451 PRO n 
1 452 ASN n 
1 453 LEU n 
1 454 HIS n 
1 455 SER n 
1 456 LEU n 
1 457 PRO n 
1 458 PHE n 
1 459 GLU n 
1 460 LEU n 
1 461 ALA n 
1 462 LEU n 
1 463 CYS n 
1 464 SER n 
1 465 LYS n 
1 466 LEU n 
1 467 SER n 
1 468 ILE n 
1 469 MET n 
1 470 SER n 
1 471 ILE n 
1 472 GLU n 
1 473 ASN n 
1 474 CYS n 
1 475 PRO n 
1 476 LEU n 
1 477 SER n 
1 478 HIS n 
1 479 LEU n 
1 480 PRO n 
1 481 PRO n 
1 482 GLN n 
1 483 ILE n 
1 484 VAL n 
1 485 ALA n 
1 486 GLY n 
1 487 GLY n 
1 488 PRO n 
1 489 SER n 
1 490 PHE n 
1 491 ILE n 
1 492 ILE n 
1 493 GLN n 
1 494 PHE n 
1 495 LEU n 
1 496 LYS n 
1 497 MET n 
1 498 GLN n 
1 499 GLY n 
1 500 PRO n 
1 501 TYR n 
1 502 ARG n 
1 503 ALA n 
1 504 MET n 
1 505 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   505 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SHOC2, KIAA0862' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            Sf21 
_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                       pFastBac1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ATZ non-polymer         . 
;(2S)-{2-[(4-chloro[1,1'-biphenyl]-3-yl)methoxy]phenyl}[(2-oxo-2,3-dihydro-1,3-benzoxazol-5-yl)amino]acetic acid
;
? 'C28 H21 Cl N2 O5' 500.930 
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 
K     non-polymer         . 'POTASSIUM ION' ? 'K 1'              39.098  
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   GLY 1   78  ?   ?   ?   A . n 
A 1 2   PRO 2   79  ?   ?   ?   A . n 
A 1 3   GLY 3   80  ?   ?   ?   A . n 
A 1 4   THR 4   81  ?   ?   ?   A . n 
A 1 5   ARG 5   82  ?   ?   ?   A . n 
A 1 6   LYS 6   83  ?   ?   ?   A . n 
A 1 7   LYS 7   84  84  LYS LYS A . n 
A 1 8   SER 8   85  85  SER SER A . n 
A 1 9   SER 9   86  86  SER SER A . n 
A 1 10  ASN 10  87  87  ASN ASN A . n 
A 1 11  ALA 11  88  88  ALA ALA A . n 
A 1 12  GLU 12  89  89  GLU GLU A . n 
A 1 13  VAL 13  90  90  VAL VAL A . n 
A 1 14  ILE 14  91  91  ILE ILE A . n 
A 1 15  LYS 15  92  92  LYS LYS A . n 
A 1 16  GLU 16  93  93  GLU GLU A . n 
A 1 17  LEU 17  94  94  LEU LEU A . n 
A 1 18  ASN 18  95  95  ASN ASN A . n 
A 1 19  LYS 19  96  96  LYS LYS A . n 
A 1 20  CYS 20  97  97  CYS CYS A . n 
A 1 21  ARG 21  98  98  ARG ARG A . n 
A 1 22  GLU 22  99  99  GLU GLU A . n 
A 1 23  GLU 23  100 100 GLU GLU A . n 
A 1 24  ASN 24  101 101 ASN ASN A . n 
A 1 25  SER 25  102 102 SER SER A . n 
A 1 26  MET 26  103 103 MET MET A . n 
A 1 27  ARG 27  104 104 ARG ARG A . n 
A 1 28  LEU 28  105 105 LEU LEU A . n 
A 1 29  ASP 29  106 106 ASP ASP A . n 
A 1 30  LEU 30  107 107 LEU LEU A . n 
A 1 31  SER 31  108 108 SER SER A . n 
A 1 32  LYS 32  109 109 LYS LYS A . n 
A 1 33  ARG 33  110 110 ARG ARG A . n 
A 1 34  SER 34  111 111 SER SER A . n 
A 1 35  ILE 35  112 112 ILE ILE A . n 
A 1 36  HIS 36  113 113 HIS HIS A . n 
A 1 37  ILE 37  114 114 ILE ILE A . n 
A 1 38  LEU 38  115 115 LEU LEU A . n 
A 1 39  PRO 39  116 116 PRO PRO A . n 
A 1 40  SER 40  117 117 SER SER A . n 
A 1 41  SER 41  118 118 SER SER A . n 
A 1 42  ILE 42  119 119 ILE ILE A . n 
A 1 43  LYS 43  120 120 LYS LYS A . n 
A 1 44  GLU 44  121 121 GLU GLU A . n 
A 1 45  LEU 45  122 122 LEU LEU A . n 
A 1 46  THR 46  123 123 THR THR A . n 
A 1 47  GLN 47  124 124 GLN GLN A . n 
A 1 48  LEU 48  125 125 LEU LEU A . n 
A 1 49  THR 49  126 126 THR THR A . n 
A 1 50  GLU 50  127 127 GLU GLU A . n 
A 1 51  LEU 51  128 128 LEU LEU A . n 
A 1 52  TYR 52  129 129 TYR TYR A . n 
A 1 53  LEU 53  130 130 LEU LEU A . n 
A 1 54  TYR 54  131 131 TYR TYR A . n 
A 1 55  SER 55  132 132 SER SER A . n 
A 1 56  ASN 56  133 133 ASN ASN A . n 
A 1 57  LYS 57  134 134 LYS LYS A . n 
A 1 58  LEU 58  135 135 LEU LEU A . n 
A 1 59  GLN 59  136 136 GLN GLN A . n 
A 1 60  SER 60  137 137 SER SER A . n 
A 1 61  LEU 61  138 138 LEU LEU A . n 
A 1 62  PRO 62  139 139 PRO PRO A . n 
A 1 63  ALA 63  140 140 ALA ALA A . n 
A 1 64  GLU 64  141 141 GLU GLU A . n 
A 1 65  VAL 65  142 142 VAL VAL A . n 
A 1 66  GLY 66  143 143 GLY GLY A . n 
A 1 67  CYS 67  144 144 CYS CYS A . n 
A 1 68  LEU 68  145 145 LEU LEU A . n 
A 1 69  VAL 69  146 146 VAL VAL A . n 
A 1 70  ASN 70  147 147 ASN ASN A . n 
A 1 71  LEU 71  148 148 LEU LEU A . n 
A 1 72  MET 72  149 149 MET MET A . n 
A 1 73  THR 73  150 150 THR THR A . n 
A 1 74  LEU 74  151 151 LEU LEU A . n 
A 1 75  ALA 75  152 152 ALA ALA A . n 
A 1 76  LEU 76  153 153 LEU LEU A . n 
A 1 77  SER 77  154 154 SER SER A . n 
A 1 78  GLU 78  155 155 GLU GLU A . n 
A 1 79  ASN 79  156 156 ASN ASN A . n 
A 1 80  SER 80  157 157 SER SER A . n 
A 1 81  LEU 81  158 158 LEU LEU A . n 
A 1 82  THR 82  159 159 THR THR A . n 
A 1 83  SER 83  160 160 SER SER A . n 
A 1 84  LEU 84  161 161 LEU LEU A . n 
A 1 85  PRO 85  162 162 PRO PRO A . n 
A 1 86  ASP 86  163 163 ASP ASP A . n 
A 1 87  SER 87  164 164 SER SER A . n 
A 1 88  LEU 88  165 165 LEU LEU A . n 
A 1 89  ASP 89  166 166 ASP ASP A . n 
A 1 90  ASN 90  167 167 ASN ASN A . n 
A 1 91  LEU 91  168 168 LEU LEU A . n 
A 1 92  LYS 92  169 169 LYS LYS A . n 
A 1 93  LYS 93  170 170 LYS LYS A . n 
A 1 94  LEU 94  171 171 LEU LEU A . n 
A 1 95  ARG 95  172 172 ARG ARG A . n 
A 1 96  MET 96  173 173 MET MET A . n 
A 1 97  LEU 97  174 174 LEU LEU A . n 
A 1 98  ASP 98  175 175 ASP ASP A . n 
A 1 99  LEU 99  176 176 LEU LEU A . n 
A 1 100 ARG 100 177 177 ARG ARG A . n 
A 1 101 HIS 101 178 178 HIS HIS A . n 
A 1 102 ASN 102 179 179 ASN ASN A . n 
A 1 103 LYS 103 180 180 LYS LYS A . n 
A 1 104 LEU 104 181 181 LEU LEU A . n 
A 1 105 ARG 105 182 182 ARG ARG A . n 
A 1 106 GLU 106 183 183 GLU GLU A . n 
A 1 107 ILE 107 184 184 ILE ILE A . n 
A 1 108 PRO 108 185 185 PRO PRO A . n 
A 1 109 SER 109 186 186 SER SER A . n 
A 1 110 VAL 110 187 187 VAL VAL A . n 
A 1 111 VAL 111 188 188 VAL VAL A . n 
A 1 112 TYR 112 189 189 TYR TYR A . n 
A 1 113 ARG 113 190 190 ARG ARG A . n 
A 1 114 LEU 114 191 191 LEU LEU A . n 
A 1 115 ASP 115 192 192 ASP ASP A . n 
A 1 116 SER 116 193 193 SER SER A . n 
A 1 117 LEU 117 194 194 LEU LEU A . n 
A 1 118 THR 118 195 195 THR THR A . n 
A 1 119 THR 119 196 196 THR THR A . n 
A 1 120 LEU 120 197 197 LEU LEU A . n 
A 1 121 TYR 121 198 198 TYR TYR A . n 
A 1 122 LEU 122 199 199 LEU LEU A . n 
A 1 123 ARG 123 200 200 ARG ARG A . n 
A 1 124 PHE 124 201 201 PHE PHE A . n 
A 1 125 ASN 125 202 202 ASN ASN A . n 
A 1 126 ARG 126 203 203 ARG ARG A . n 
A 1 127 ILE 127 204 204 ILE ILE A . n 
A 1 128 THR 128 205 205 THR THR A . n 
A 1 129 THR 129 206 206 THR THR A . n 
A 1 130 VAL 130 207 207 VAL VAL A . n 
A 1 131 GLU 131 208 208 GLU GLU A . n 
A 1 132 LYS 132 209 209 LYS LYS A . n 
A 1 133 ASP 133 210 210 ASP ASP A . n 
A 1 134 ILE 134 211 211 ILE ILE A . n 
A 1 135 LYS 135 212 212 LYS LYS A . n 
A 1 136 ASN 136 213 213 ASN ASN A . n 
A 1 137 LEU 137 214 214 LEU LEU A . n 
A 1 138 SER 138 215 215 SER SER A . n 
A 1 139 LYS 139 216 216 LYS LYS A . n 
A 1 140 LEU 140 217 217 LEU LEU A . n 
A 1 141 SER 141 218 218 SER SER A . n 
A 1 142 MET 142 219 219 MET MET A . n 
A 1 143 LEU 143 220 220 LEU LEU A . n 
A 1 144 SER 144 221 221 SER SER A . n 
A 1 145 ILE 145 222 222 ILE ILE A . n 
A 1 146 ARG 146 223 223 ARG ARG A . n 
A 1 147 GLU 147 224 224 GLU GLU A . n 
A 1 148 ASN 148 225 225 ASN ASN A . n 
A 1 149 LYS 149 226 226 LYS LYS A . n 
A 1 150 ILE 150 227 227 ILE ILE A . n 
A 1 151 LYS 151 228 228 LYS LYS A . n 
A 1 152 GLN 152 229 229 GLN GLN A . n 
A 1 153 LEU 153 230 230 LEU LEU A . n 
A 1 154 PRO 154 231 231 PRO PRO A . n 
A 1 155 ALA 155 232 232 ALA ALA A . n 
A 1 156 GLU 156 233 233 GLU GLU A . n 
A 1 157 ILE 157 234 234 ILE ILE A . n 
A 1 158 GLY 158 235 235 GLY GLY A . n 
A 1 159 GLU 159 236 236 GLU GLU A . n 
A 1 160 LEU 160 237 237 LEU LEU A . n 
A 1 161 CYS 161 238 238 CYS CYS A . n 
A 1 162 ASN 162 239 239 ASN ASN A . n 
A 1 163 LEU 163 240 240 LEU LEU A . n 
A 1 164 ILE 164 241 241 ILE ILE A . n 
A 1 165 THR 165 242 242 THR THR A . n 
A 1 166 LEU 166 243 243 LEU LEU A . n 
A 1 167 ASP 167 244 244 ASP ASP A . n 
A 1 168 VAL 168 245 245 VAL VAL A . n 
A 1 169 ALA 169 246 246 ALA ALA A . n 
A 1 170 HIS 170 247 247 HIS HIS A . n 
A 1 171 ASN 171 248 248 ASN ASN A . n 
A 1 172 GLN 172 249 249 GLN GLN A . n 
A 1 173 LEU 173 250 250 LEU LEU A . n 
A 1 174 GLU 174 251 251 GLU GLU A . n 
A 1 175 HIS 175 252 252 HIS HIS A . n 
A 1 176 LEU 176 253 253 LEU LEU A . n 
A 1 177 PRO 177 254 254 PRO PRO A . n 
A 1 178 LYS 178 255 255 LYS LYS A . n 
A 1 179 GLU 179 256 256 GLU GLU A . n 
A 1 180 ILE 180 257 257 ILE ILE A . n 
A 1 181 GLY 181 258 258 GLY GLY A . n 
A 1 182 ASN 182 259 259 ASN ASN A . n 
A 1 183 CYS 183 260 260 CYS CYS A . n 
A 1 184 THR 184 261 261 THR THR A . n 
A 1 185 GLN 185 262 262 GLN GLN A . n 
A 1 186 ILE 186 263 263 ILE ILE A . n 
A 1 187 THR 187 264 264 THR THR A . n 
A 1 188 ASN 188 265 265 ASN ASN A . n 
A 1 189 LEU 189 266 266 LEU LEU A . n 
A 1 190 ASP 190 267 267 ASP ASP A . n 
A 1 191 LEU 191 268 268 LEU LEU A . n 
A 1 192 GLN 192 269 269 GLN GLN A . n 
A 1 193 HIS 193 270 270 HIS HIS A . n 
A 1 194 ASN 194 271 271 ASN ASN A . n 
A 1 195 GLU 195 272 272 GLU GLU A . n 
A 1 196 LEU 196 273 273 LEU LEU A . n 
A 1 197 LEU 197 274 274 LEU LEU A . n 
A 1 198 ASP 198 275 275 ASP ASP A . n 
A 1 199 LEU 199 276 276 LEU LEU A . n 
A 1 200 PRO 200 277 277 PRO PRO A . n 
A 1 201 ASP 201 278 278 ASP ASP A . n 
A 1 202 THR 202 279 279 THR THR A . n 
A 1 203 ILE 203 280 280 ILE ILE A . n 
A 1 204 GLY 204 281 281 GLY GLY A . n 
A 1 205 ASN 205 282 282 ASN ASN A . n 
A 1 206 LEU 206 283 283 LEU LEU A . n 
A 1 207 SER 207 284 284 SER SER A . n 
A 1 208 SER 208 285 285 SER SER A . n 
A 1 209 LEU 209 286 286 LEU LEU A . n 
A 1 210 SER 210 287 287 SER SER A . n 
A 1 211 ARG 211 288 288 ARG ARG A . n 
A 1 212 LEU 212 289 289 LEU LEU A . n 
A 1 213 GLY 213 290 290 GLY GLY A . n 
A 1 214 LEU 214 291 291 LEU LEU A . n 
A 1 215 ARG 215 292 292 ARG ARG A . n 
A 1 216 TYR 216 293 293 TYR TYR A . n 
A 1 217 ASN 217 294 294 ASN ASN A . n 
A 1 218 ARG 218 295 295 ARG ARG A . n 
A 1 219 LEU 219 296 296 LEU LEU A . n 
A 1 220 SER 220 297 297 SER SER A . n 
A 1 221 ALA 221 298 298 ALA ALA A . n 
A 1 222 ILE 222 299 299 ILE ILE A . n 
A 1 223 PRO 223 300 300 PRO PRO A . n 
A 1 224 ARG 224 301 301 ARG ARG A . n 
A 1 225 SER 225 302 302 SER SER A . n 
A 1 226 LEU 226 303 303 LEU LEU A . n 
A 1 227 ALA 227 304 304 ALA ALA A . n 
A 1 228 LYS 228 305 305 LYS LYS A . n 
A 1 229 CYS 229 306 306 CYS CYS A . n 
A 1 230 SER 230 307 307 SER SER A . n 
A 1 231 ALA 231 308 308 ALA ALA A . n 
A 1 232 LEU 232 309 309 LEU LEU A . n 
A 1 233 GLU 233 310 310 GLU GLU A . n 
A 1 234 GLU 234 311 311 GLU GLU A . n 
A 1 235 LEU 235 312 312 LEU LEU A . n 
A 1 236 ASN 236 313 313 ASN ASN A . n 
A 1 237 LEU 237 314 314 LEU LEU A . n 
A 1 238 GLU 238 315 315 GLU GLU A . n 
A 1 239 ASN 239 316 316 ASN ASN A . n 
A 1 240 ASN 240 317 317 ASN ASN A . n 
A 1 241 ASN 241 318 318 ASN ASN A . n 
A 1 242 ILE 242 319 319 ILE ILE A . n 
A 1 243 SER 243 320 320 SER SER A . n 
A 1 244 THR 244 321 321 THR THR A . n 
A 1 245 LEU 245 322 322 LEU LEU A . n 
A 1 246 PRO 246 323 323 PRO PRO A . n 
A 1 247 GLU 247 324 324 GLU GLU A . n 
A 1 248 SER 248 325 325 SER SER A . n 
A 1 249 LEU 249 326 326 LEU LEU A . n 
A 1 250 LEU 250 327 327 LEU LEU A . n 
A 1 251 SER 251 328 328 SER SER A . n 
A 1 252 SER 252 329 329 SER SER A . n 
A 1 253 LEU 253 330 330 LEU LEU A . n 
A 1 254 VAL 254 331 331 VAL VAL A . n 
A 1 255 LYS 255 332 332 LYS LYS A . n 
A 1 256 LEU 256 333 333 LEU LEU A . n 
A 1 257 ASN 257 334 334 ASN ASN A . n 
A 1 258 SER 258 335 335 SER SER A . n 
A 1 259 LEU 259 336 336 LEU LEU A . n 
A 1 260 THR 260 337 337 THR THR A . n 
A 1 261 LEU 261 338 338 LEU LEU A . n 
A 1 262 ALA 262 339 339 ALA ALA A . n 
A 1 263 ARG 263 340 340 ARG ARG A . n 
A 1 264 ASN 264 341 341 ASN ASN A . n 
A 1 265 CYS 265 342 342 CYS CYS A . n 
A 1 266 PHE 266 343 343 PHE PHE A . n 
A 1 267 GLN 267 344 344 GLN GLN A . n 
A 1 268 LEU 268 345 345 LEU LEU A . n 
A 1 269 TYR 269 346 346 TYR TYR A . n 
A 1 270 PRO 270 347 347 PRO PRO A . n 
A 1 271 VAL 271 348 348 VAL VAL A . n 
A 1 272 GLY 272 349 349 GLY GLY A . n 
A 1 273 GLY 273 350 350 GLY GLY A . n 
A 1 274 PRO 274 351 351 PRO PRO A . n 
A 1 275 SER 275 352 352 SER SER A . n 
A 1 276 GLN 276 353 353 GLN GLN A . n 
A 1 277 PHE 277 354 354 PHE PHE A . n 
A 1 278 SER 278 355 355 SER SER A . n 
A 1 279 THR 279 356 356 THR THR A . n 
A 1 280 ILE 280 357 357 ILE ILE A . n 
A 1 281 TYR 281 358 358 TYR TYR A . n 
A 1 282 SER 282 359 359 SER SER A . n 
A 1 283 LEU 283 360 360 LEU LEU A . n 
A 1 284 ASN 284 361 361 ASN ASN A . n 
A 1 285 MET 285 362 362 MET MET A . n 
A 1 286 GLU 286 363 363 GLU GLU A . n 
A 1 287 HIS 287 364 364 HIS HIS A . n 
A 1 288 ASN 288 365 365 ASN ASN A . n 
A 1 289 ARG 289 366 366 ARG ARG A . n 
A 1 290 ILE 290 367 367 ILE ILE A . n 
A 1 291 ASN 291 368 368 ASN ASN A . n 
A 1 292 LYS 292 369 369 LYS LYS A . n 
A 1 293 ILE 293 370 370 ILE ILE A . n 
A 1 294 PRO 294 371 371 PRO PRO A . n 
A 1 295 PHE 295 372 372 PHE PHE A . n 
A 1 296 GLY 296 373 373 GLY GLY A . n 
A 1 297 ILE 297 374 374 ILE ILE A . n 
A 1 298 PHE 298 375 375 PHE PHE A . n 
A 1 299 SER 299 376 376 SER SER A . n 
A 1 300 ARG 300 377 377 ARG ARG A . n 
A 1 301 ALA 301 378 378 ALA ALA A . n 
A 1 302 LYS 302 379 379 LYS LYS A . n 
A 1 303 VAL 303 380 380 VAL VAL A . n 
A 1 304 LEU 304 381 381 LEU LEU A . n 
A 1 305 SER 305 382 382 SER SER A . n 
A 1 306 LYS 306 383 383 LYS LYS A . n 
A 1 307 LEU 307 384 384 LEU LEU A . n 
A 1 308 ASN 308 385 385 ASN ASN A . n 
A 1 309 MET 309 386 386 MET MET A . n 
A 1 310 LYS 310 387 387 LYS LYS A . n 
A 1 311 ASP 311 388 388 ASP ASP A . n 
A 1 312 ASN 312 389 389 ASN ASN A . n 
A 1 313 GLN 313 390 390 GLN GLN A . n 
A 1 314 LEU 314 391 391 LEU LEU A . n 
A 1 315 THR 315 392 392 THR THR A . n 
A 1 316 SER 316 393 393 SER SER A . n 
A 1 317 LEU 317 394 394 LEU LEU A . n 
A 1 318 PRO 318 395 395 PRO PRO A . n 
A 1 319 LEU 319 396 396 LEU LEU A . n 
A 1 320 ASP 320 397 397 ASP ASP A . n 
A 1 321 PHE 321 398 398 PHE PHE A . n 
A 1 322 GLY 322 399 399 GLY GLY A . n 
A 1 323 THR 323 400 400 THR THR A . n 
A 1 324 TRP 324 401 401 TRP TRP A . n 
A 1 325 THR 325 402 402 THR THR A . n 
A 1 326 SER 326 403 403 SER SER A . n 
A 1 327 MET 327 404 404 MET MET A . n 
A 1 328 VAL 328 405 405 VAL VAL A . n 
A 1 329 GLU 329 406 406 GLU GLU A . n 
A 1 330 LEU 330 407 407 LEU LEU A . n 
A 1 331 ASN 331 408 408 ASN ASN A . n 
A 1 332 LEU 332 409 409 LEU LEU A . n 
A 1 333 ALA 333 410 410 ALA ALA A . n 
A 1 334 THR 334 411 411 THR THR A . n 
A 1 335 ASN 335 412 412 ASN ASN A . n 
A 1 336 GLN 336 413 413 GLN GLN A . n 
A 1 337 LEU 337 414 414 LEU LEU A . n 
A 1 338 THR 338 415 415 THR THR A . n 
A 1 339 LYS 339 416 416 LYS LYS A . n 
A 1 340 ILE 340 417 417 ILE ILE A . n 
A 1 341 PRO 341 418 418 PRO PRO A . n 
A 1 342 GLU 342 419 419 GLU GLU A . n 
A 1 343 ASP 343 420 420 ASP ASP A . n 
A 1 344 VAL 344 421 421 VAL VAL A . n 
A 1 345 SER 345 422 422 SER SER A . n 
A 1 346 GLY 346 423 423 GLY GLY A . n 
A 1 347 LEU 347 424 424 LEU LEU A . n 
A 1 348 VAL 348 425 425 VAL VAL A . n 
A 1 349 SER 349 426 426 SER SER A . n 
A 1 350 LEU 350 427 427 LEU LEU A . n 
A 1 351 GLU 351 428 428 GLU GLU A . n 
A 1 352 VAL 352 429 429 VAL VAL A . n 
A 1 353 LEU 353 430 430 LEU LEU A . n 
A 1 354 ILE 354 431 431 ILE ILE A . n 
A 1 355 LEU 355 432 432 LEU LEU A . n 
A 1 356 SER 356 433 433 SER SER A . n 
A 1 357 ASN 357 434 434 ASN ASN A . n 
A 1 358 ASN 358 435 435 ASN ASN A . n 
A 1 359 LEU 359 436 436 LEU LEU A . n 
A 1 360 LEU 360 437 437 LEU LEU A . n 
A 1 361 LYS 361 438 438 LYS LYS A . n 
A 1 362 LYS 362 439 439 LYS LYS A . n 
A 1 363 LEU 363 440 440 LEU LEU A . n 
A 1 364 PRO 364 441 441 PRO PRO A . n 
A 1 365 HIS 365 442 442 HIS HIS A . n 
A 1 366 GLY 366 443 443 GLY GLY A . n 
A 1 367 LEU 367 444 444 LEU LEU A . n 
A 1 368 GLY 368 445 445 GLY GLY A . n 
A 1 369 ASN 369 446 446 ASN ASN A . n 
A 1 370 LEU 370 447 447 LEU LEU A . n 
A 1 371 ARG 371 448 448 ARG ARG A . n 
A 1 372 LYS 372 449 449 LYS LYS A . n 
A 1 373 LEU 373 450 450 LEU LEU A . n 
A 1 374 ARG 374 451 451 ARG ARG A . n 
A 1 375 GLU 375 452 452 GLU GLU A . n 
A 1 376 LEU 376 453 453 LEU LEU A . n 
A 1 377 ASP 377 454 454 ASP ASP A . n 
A 1 378 LEU 378 455 455 LEU LEU A . n 
A 1 379 GLU 379 456 456 GLU GLU A . n 
A 1 380 GLU 380 457 457 GLU GLU A . n 
A 1 381 ASN 381 458 458 ASN ASN A . n 
A 1 382 LYS 382 459 459 LYS LYS A . n 
A 1 383 LEU 383 460 460 LEU LEU A . n 
A 1 384 GLU 384 461 461 GLU GLU A . n 
A 1 385 SER 385 462 462 SER SER A . n 
A 1 386 LEU 386 463 463 LEU LEU A . n 
A 1 387 PRO 387 464 464 PRO PRO A . n 
A 1 388 ASN 388 465 465 ASN ASN A . n 
A 1 389 GLU 389 466 466 GLU GLU A . n 
A 1 390 ILE 390 467 467 ILE ILE A . n 
A 1 391 ALA 391 468 468 ALA ALA A . n 
A 1 392 TYR 392 469 469 TYR TYR A . n 
A 1 393 LEU 393 470 470 LEU LEU A . n 
A 1 394 LYS 394 471 471 LYS LYS A . n 
A 1 395 ASP 395 472 472 ASP ASP A . n 
A 1 396 LEU 396 473 473 LEU LEU A . n 
A 1 397 GLN 397 474 474 GLN GLN A . n 
A 1 398 LYS 398 475 475 LYS LYS A . n 
A 1 399 LEU 399 476 476 LEU LEU A . n 
A 1 400 VAL 400 477 477 VAL VAL A . n 
A 1 401 LEU 401 478 478 LEU LEU A . n 
A 1 402 THR 402 479 479 THR THR A . n 
A 1 403 ASN 403 480 480 ASN ASN A . n 
A 1 404 ASN 404 481 481 ASN ASN A . n 
A 1 405 GLN 405 482 482 GLN GLN A . n 
A 1 406 LEU 406 483 483 LEU LEU A . n 
A 1 407 THR 407 484 484 THR THR A . n 
A 1 408 THR 408 485 485 THR THR A . n 
A 1 409 LEU 409 486 486 LEU LEU A . n 
A 1 410 PRO 410 487 487 PRO PRO A . n 
A 1 411 ARG 411 488 488 ARG ARG A . n 
A 1 412 GLY 412 489 489 GLY GLY A . n 
A 1 413 ILE 413 490 490 ILE ILE A . n 
A 1 414 GLY 414 491 491 GLY GLY A . n 
A 1 415 HIS 415 492 492 HIS HIS A . n 
A 1 416 LEU 416 493 493 LEU LEU A . n 
A 1 417 THR 417 494 494 THR THR A . n 
A 1 418 ASN 418 495 495 ASN ASN A . n 
A 1 419 LEU 419 496 496 LEU LEU A . n 
A 1 420 THR 420 497 497 THR THR A . n 
A 1 421 HIS 421 498 498 HIS HIS A . n 
A 1 422 LEU 422 499 499 LEU LEU A . n 
A 1 423 GLY 423 500 500 GLY GLY A . n 
A 1 424 LEU 424 501 501 LEU LEU A . n 
A 1 425 GLY 425 502 502 GLY GLY A . n 
A 1 426 GLU 426 503 503 GLU GLU A . n 
A 1 427 ASN 427 504 504 ASN ASN A . n 
A 1 428 LEU 428 505 505 LEU LEU A . n 
A 1 429 LEU 429 506 506 LEU LEU A . n 
A 1 430 THR 430 507 507 THR THR A . n 
A 1 431 HIS 431 508 508 HIS HIS A . n 
A 1 432 LEU 432 509 509 LEU LEU A . n 
A 1 433 PRO 433 510 510 PRO PRO A . n 
A 1 434 GLU 434 511 511 GLU GLU A . n 
A 1 435 GLU 435 512 512 GLU GLU A . n 
A 1 436 ILE 436 513 513 ILE ILE A . n 
A 1 437 GLY 437 514 514 GLY GLY A . n 
A 1 438 THR 438 515 515 THR THR A . n 
A 1 439 LEU 439 516 516 LEU LEU A . n 
A 1 440 GLU 440 517 517 GLU GLU A . n 
A 1 441 ASN 441 518 518 ASN ASN A . n 
A 1 442 LEU 442 519 519 LEU LEU A . n 
A 1 443 GLU 443 520 520 GLU GLU A . n 
A 1 444 GLU 444 521 521 GLU GLU A . n 
A 1 445 LEU 445 522 522 LEU LEU A . n 
A 1 446 TYR 446 523 523 TYR TYR A . n 
A 1 447 LEU 447 524 524 LEU LEU A . n 
A 1 448 ASN 448 525 525 ASN ASN A . n 
A 1 449 ASP 449 526 526 ASP ASP A . n 
A 1 450 ASN 450 527 527 ASN ASN A . n 
A 1 451 PRO 451 528 528 PRO PRO A . n 
A 1 452 ASN 452 529 529 ASN ASN A . n 
A 1 453 LEU 453 530 530 LEU LEU A . n 
A 1 454 HIS 454 531 531 HIS HIS A . n 
A 1 455 SER 455 532 532 SER SER A . n 
A 1 456 LEU 456 533 533 LEU LEU A . n 
A 1 457 PRO 457 534 534 PRO PRO A . n 
A 1 458 PHE 458 535 535 PHE PHE A . n 
A 1 459 GLU 459 536 536 GLU GLU A . n 
A 1 460 LEU 460 537 537 LEU LEU A . n 
A 1 461 ALA 461 538 538 ALA ALA A . n 
A 1 462 LEU 462 539 539 LEU LEU A . n 
A 1 463 CYS 463 540 540 CYS CYS A . n 
A 1 464 SER 464 541 541 SER SER A . n 
A 1 465 LYS 465 542 542 LYS LYS A . n 
A 1 466 LEU 466 543 543 LEU LEU A . n 
A 1 467 SER 467 544 544 SER SER A . n 
A 1 468 ILE 468 545 545 ILE ILE A . n 
A 1 469 MET 469 546 546 MET MET A . n 
A 1 470 SER 470 547 547 SER SER A . n 
A 1 471 ILE 471 548 548 ILE ILE A . n 
A 1 472 GLU 472 549 549 GLU GLU A . n 
A 1 473 ASN 473 550 550 ASN ASN A . n 
A 1 474 CYS 474 551 551 CYS CYS A . n 
A 1 475 PRO 475 552 552 PRO PRO A . n 
A 1 476 LEU 476 553 553 LEU LEU A . n 
A 1 477 SER 477 554 554 SER SER A . n 
A 1 478 HIS 478 555 555 HIS HIS A . n 
A 1 479 LEU 479 556 556 LEU LEU A . n 
A 1 480 PRO 480 557 557 PRO PRO A . n 
A 1 481 PRO 481 558 558 PRO PRO A . n 
A 1 482 GLN 482 559 559 GLN GLN A . n 
A 1 483 ILE 483 560 560 ILE ILE A . n 
A 1 484 VAL 484 561 561 VAL VAL A . n 
A 1 485 ALA 485 562 562 ALA ALA A . n 
A 1 486 GLY 486 563 563 GLY GLY A . n 
A 1 487 GLY 487 564 564 GLY GLY A . n 
A 1 488 PRO 488 565 565 PRO PRO A . n 
A 1 489 SER 489 566 566 SER SER A . n 
A 1 490 PHE 490 567 567 PHE PHE A . n 
A 1 491 ILE 491 568 568 ILE ILE A . n 
A 1 492 ILE 492 569 569 ILE ILE A . n 
A 1 493 GLN 493 570 570 GLN GLN A . n 
A 1 494 PHE 494 571 571 PHE PHE A . n 
A 1 495 LEU 495 572 572 LEU LEU A . n 
A 1 496 LYS 496 573 573 LYS LYS A . n 
A 1 497 MET 497 574 574 MET MET A . n 
A 1 498 GLN 498 575 575 GLN GLN A . n 
A 1 499 GLY 499 576 576 GLY GLY A . n 
A 1 500 PRO 500 577 577 PRO PRO A . n 
A 1 501 TYR 501 578 578 TYR TYR A . n 
A 1 502 ARG 502 579 579 ARG ARG A . n 
A 1 503 ALA 503 580 580 ALA ALA A . n 
A 1 504 MET 504 581 581 MET MET A . n 
A 1 505 VAL 505 582 582 VAL VAL A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ATZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATZ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1ATZ 1   601 1   A1ATZ LI1 A . 
C 3 K     1   602 1   K     K   A . 
D 4 HOH   1   701 117 HOH   HOH A . 
D 4 HOH   2   702 39  HOH   HOH A . 
D 4 HOH   3   703 102 HOH   HOH A . 
D 4 HOH   4   704 12  HOH   HOH A . 
D 4 HOH   5   705 27  HOH   HOH A . 
D 4 HOH   6   706 174 HOH   HOH A . 
D 4 HOH   7   707 100 HOH   HOH A . 
D 4 HOH   8   708 141 HOH   HOH A . 
D 4 HOH   9   709 65  HOH   HOH A . 
D 4 HOH   10  710 191 HOH   HOH A . 
D 4 HOH   11  711 62  HOH   HOH A . 
D 4 HOH   12  712 40  HOH   HOH A . 
D 4 HOH   13  713 69  HOH   HOH A . 
D 4 HOH   14  714 32  HOH   HOH A . 
D 4 HOH   15  715 68  HOH   HOH A . 
D 4 HOH   16  716 48  HOH   HOH A . 
D 4 HOH   17  717 172 HOH   HOH A . 
D 4 HOH   18  718 171 HOH   HOH A . 
D 4 HOH   19  719 14  HOH   HOH A . 
D 4 HOH   20  720 19  HOH   HOH A . 
D 4 HOH   21  721 180 HOH   HOH A . 
D 4 HOH   22  722 61  HOH   HOH A . 
D 4 HOH   23  723 71  HOH   HOH A . 
D 4 HOH   24  724 52  HOH   HOH A . 
D 4 HOH   25  725 89  HOH   HOH A . 
D 4 HOH   26  726 30  HOH   HOH A . 
D 4 HOH   27  727 94  HOH   HOH A . 
D 4 HOH   28  728 45  HOH   HOH A . 
D 4 HOH   29  729 8   HOH   HOH A . 
D 4 HOH   30  730 72  HOH   HOH A . 
D 4 HOH   31  731 93  HOH   HOH A . 
D 4 HOH   32  732 51  HOH   HOH A . 
D 4 HOH   33  733 79  HOH   HOH A . 
D 4 HOH   34  734 74  HOH   HOH A . 
D 4 HOH   35  735 104 HOH   HOH A . 
D 4 HOH   36  736 95  HOH   HOH A . 
D 4 HOH   37  737 44  HOH   HOH A . 
D 4 HOH   38  738 119 HOH   HOH A . 
D 4 HOH   39  739 18  HOH   HOH A . 
D 4 HOH   40  740 6   HOH   HOH A . 
D 4 HOH   41  741 60  HOH   HOH A . 
D 4 HOH   42  742 16  HOH   HOH A . 
D 4 HOH   43  743 25  HOH   HOH A . 
D 4 HOH   44  744 178 HOH   HOH A . 
D 4 HOH   45  745 13  HOH   HOH A . 
D 4 HOH   46  746 138 HOH   HOH A . 
D 4 HOH   47  747 36  HOH   HOH A . 
D 4 HOH   48  748 31  HOH   HOH A . 
D 4 HOH   49  749 166 HOH   HOH A . 
D 4 HOH   50  750 106 HOH   HOH A . 
D 4 HOH   51  751 159 HOH   HOH A . 
D 4 HOH   52  752 58  HOH   HOH A . 
D 4 HOH   53  753 22  HOH   HOH A . 
D 4 HOH   54  754 4   HOH   HOH A . 
D 4 HOH   55  755 76  HOH   HOH A . 
D 4 HOH   56  756 73  HOH   HOH A . 
D 4 HOH   57  757 24  HOH   HOH A . 
D 4 HOH   58  758 59  HOH   HOH A . 
D 4 HOH   59  759 10  HOH   HOH A . 
D 4 HOH   60  760 28  HOH   HOH A . 
D 4 HOH   61  761 97  HOH   HOH A . 
D 4 HOH   62  762 29  HOH   HOH A . 
D 4 HOH   63  763 88  HOH   HOH A . 
D 4 HOH   64  764 21  HOH   HOH A . 
D 4 HOH   65  765 190 HOH   HOH A . 
D 4 HOH   66  766 86  HOH   HOH A . 
D 4 HOH   67  767 181 HOH   HOH A . 
D 4 HOH   68  768 101 HOH   HOH A . 
D 4 HOH   69  769 196 HOH   HOH A . 
D 4 HOH   70  770 164 HOH   HOH A . 
D 4 HOH   71  771 120 HOH   HOH A . 
D 4 HOH   72  772 7   HOH   HOH A . 
D 4 HOH   73  773 192 HOH   HOH A . 
D 4 HOH   74  774 136 HOH   HOH A . 
D 4 HOH   75  775 33  HOH   HOH A . 
D 4 HOH   76  776 63  HOH   HOH A . 
D 4 HOH   77  777 161 HOH   HOH A . 
D 4 HOH   78  778 11  HOH   HOH A . 
D 4 HOH   79  779 17  HOH   HOH A . 
D 4 HOH   80  780 145 HOH   HOH A . 
D 4 HOH   81  781 53  HOH   HOH A . 
D 4 HOH   82  782 54  HOH   HOH A . 
D 4 HOH   83  783 9   HOH   HOH A . 
D 4 HOH   84  784 49  HOH   HOH A . 
D 4 HOH   85  785 47  HOH   HOH A . 
D 4 HOH   86  786 23  HOH   HOH A . 
D 4 HOH   87  787 75  HOH   HOH A . 
D 4 HOH   88  788 123 HOH   HOH A . 
D 4 HOH   89  789 173 HOH   HOH A . 
D 4 HOH   90  790 103 HOH   HOH A . 
D 4 HOH   91  791 179 HOH   HOH A . 
D 4 HOH   92  792 157 HOH   HOH A . 
D 4 HOH   93  793 92  HOH   HOH A . 
D 4 HOH   94  794 110 HOH   HOH A . 
D 4 HOH   95  795 43  HOH   HOH A . 
D 4 HOH   96  796 98  HOH   HOH A . 
D 4 HOH   97  797 82  HOH   HOH A . 
D 4 HOH   98  798 139 HOH   HOH A . 
D 4 HOH   99  799 114 HOH   HOH A . 
D 4 HOH   100 800 131 HOH   HOH A . 
D 4 HOH   101 801 147 HOH   HOH A . 
D 4 HOH   102 802 42  HOH   HOH A . 
D 4 HOH   103 803 46  HOH   HOH A . 
D 4 HOH   104 804 90  HOH   HOH A . 
D 4 HOH   105 805 121 HOH   HOH A . 
D 4 HOH   106 806 80  HOH   HOH A . 
D 4 HOH   107 807 57  HOH   HOH A . 
D 4 HOH   108 808 183 HOH   HOH A . 
D 4 HOH   109 809 38  HOH   HOH A . 
D 4 HOH   110 810 194 HOH   HOH A . 
D 4 HOH   111 811 124 HOH   HOH A . 
D 4 HOH   112 812 37  HOH   HOH A . 
D 4 HOH   113 813 83  HOH   HOH A . 
D 4 HOH   114 814 70  HOH   HOH A . 
D 4 HOH   115 815 132 HOH   HOH A . 
D 4 HOH   116 816 111 HOH   HOH A . 
D 4 HOH   117 817 34  HOH   HOH A . 
D 4 HOH   118 818 134 HOH   HOH A . 
D 4 HOH   119 819 109 HOH   HOH A . 
D 4 HOH   120 820 163 HOH   HOH A . 
D 4 HOH   121 821 127 HOH   HOH A . 
D 4 HOH   122 822 151 HOH   HOH A . 
D 4 HOH   123 823 137 HOH   HOH A . 
D 4 HOH   124 824 156 HOH   HOH A . 
D 4 HOH   125 825 167 HOH   HOH A . 
D 4 HOH   126 826 177 HOH   HOH A . 
D 4 HOH   127 827 175 HOH   HOH A . 
D 4 HOH   128 828 144 HOH   HOH A . 
D 4 HOH   129 829 96  HOH   HOH A . 
D 4 HOH   130 830 64  HOH   HOH A . 
D 4 HOH   131 831 158 HOH   HOH A . 
D 4 HOH   132 832 105 HOH   HOH A . 
D 4 HOH   133 833 185 HOH   HOH A . 
D 4 HOH   134 834 108 HOH   HOH A . 
D 4 HOH   135 835 142 HOH   HOH A . 
D 4 HOH   136 836 129 HOH   HOH A . 
D 4 HOH   137 837 91  HOH   HOH A . 
D 4 HOH   138 838 165 HOH   HOH A . 
D 4 HOH   139 839 160 HOH   HOH A . 
D 4 HOH   140 840 133 HOH   HOH A . 
D 4 HOH   141 841 118 HOH   HOH A . 
D 4 HOH   142 842 3   HOH   HOH A . 
D 4 HOH   143 843 195 HOH   HOH A . 
D 4 HOH   144 844 200 HOH   HOH A . 
D 4 HOH   145 845 87  HOH   HOH A . 
D 4 HOH   146 846 188 HOH   HOH A . 
D 4 HOH   147 847 130 HOH   HOH A . 
D 4 HOH   148 848 168 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE   ? ? ? .           3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BTP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.768 
_cell.length_a_esd                 ? 
_cell.length_b                     69.717 
_cell.length_b_esd                 ? 
_cell.length_c                     198.266 
_cell.length_c_esd                 ? 
_cell.volume                       522048.585 
_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                         9BTP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BTP 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.53 
_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              7.5 
_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    
;See reference. Crystals of apo SHOC2 in space group p212121 were incubated with compound and harvested. 50 mM Tris pH 7.0, 200 mM KCl, 40% PP 5/4 PO/OH
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-05 
_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   1 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          31.23 
_reflns.entry_id                                       9BTP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.369 
_reflns.d_resolution_low                               65.769 
_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                                     22184 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.279 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.369 
_reflns_shell.d_res_low                                     2.377 
_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                             210 
_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                               13.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.679 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.648 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.84 
_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                                 9BTP 
_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                            2.37 
_refine.ls_d_res_low                             57.03 
_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                     22174 
_refine.ls_number_reflns_R_free                  1101 
_refine.ls_number_reflns_R_work                  21073 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1940 
_refine.ls_R_factor_R_free                       0.2626 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1904 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.9531 
_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                            0.2852 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.37 
_refine_hist.d_res_low                        57.03 
_refine_hist.number_atoms_solvent             148 
_refine_hist.number_atoms_total               4117 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3932 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078  ? 4029 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0259  ? 5461 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0506  ? 659  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0072  ? 694  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.0166 ? 1557 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.37 2.48  . . 144 2557 99.96  . . . . 0.2352 . . . . . . . . . . . 0.2929 
'X-RAY DIFFRACTION' 2.48 2.61  . . 122 2574 100.00 . . . . 0.2282 . . . . . . . . . . . 0.3264 
'X-RAY DIFFRACTION' 2.61 2.77  . . 139 2600 99.93  . . . . 0.2176 . . . . . . . . . . . 0.2888 
'X-RAY DIFFRACTION' 2.77 2.98  . . 140 2579 99.96  . . . . 0.2176 . . . . . . . . . . . 0.3213 
'X-RAY DIFFRACTION' 2.98 3.29  . . 133 2634 99.96  . . . . 0.2204 . . . . . . . . . . . 0.2954 
'X-RAY DIFFRACTION' 3.29 3.76  . . 129 2654 100.00 . . . . 0.1852 . . . . . . . . . . . 0.2637 
'X-RAY DIFFRACTION' 3.76 4.73  . . 145 2667 100.00 . . . . 0.1525 . . . . . . . . . . . 0.2256 
'X-RAY DIFFRACTION' 4.74 57.03 . . 149 2808 99.80  . . . . 0.1765 . . . . . . . . . . . 0.2274 
# 
_struct.entry_id                     9BTP 
_struct.title                        'Structure of human SHOC2 in complex with a small molecule inhibitor (R)-5' 
_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        9BTP 
_struct_keywords.text            'SHOC2, RAS, PP1C, MAPK, Inhibitor, Complex, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SHOC2_HUMAN 
_struct_ref.pdbx_db_accession          Q9UQ13 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLT
SLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCN
LITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI
STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFG
TWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLT
NNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ
IVAGGPSFIIQFLKMQGPYRAMV
;
_struct_ref.pdbx_align_begin           80 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BTP 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 505 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9UQ13 
_struct_ref_seq.db_align_beg                  80 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  582 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       80 
_struct_ref_seq.pdbx_auth_seq_align_end       582 
# 
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 9BTP GLY A 1 ? UNP Q9UQ13 ? ? 'expression tag' 78 1 
1 9BTP PRO A 2 ? UNP Q9UQ13 ? ? 'expression tag' 79 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 9   ? ASN A 24  ? SER A 86  ASN A 101 1 ? 16 
HELX_P HELX_P2  AA2 PRO A 39  ? LEU A 45  ? PRO A 116 LEU A 122 5 ? 7  
HELX_P HELX_P3  AA3 PRO A 62  ? LEU A 68  ? PRO A 139 LEU A 145 5 ? 7  
HELX_P HELX_P4  AA4 PRO A 85  ? LEU A 91  ? PRO A 162 LEU A 168 5 ? 7  
HELX_P HELX_P5  AA5 PRO A 108 ? LEU A 114 ? PRO A 185 LEU A 191 5 ? 7  
HELX_P HELX_P6  AA6 GLU A 131 ? LEU A 137 ? GLU A 208 LEU A 214 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 154 ? LEU A 160 ? PRO A 231 LEU A 237 5 ? 7  
HELX_P HELX_P8  AA8 PRO A 177 ? CYS A 183 ? PRO A 254 CYS A 260 5 ? 7  
HELX_P HELX_P9  AA9 PRO A 200 ? LEU A 206 ? PRO A 277 LEU A 283 5 ? 7  
HELX_P HELX_P10 AB1 PRO A 223 ? CYS A 229 ? PRO A 300 CYS A 306 5 ? 7  
HELX_P HELX_P11 AB2 GLY A 273 ? SER A 278 ? GLY A 350 SER A 355 5 ? 6  
HELX_P HELX_P12 AB3 ASP A 320 ? TRP A 324 ? ASP A 397 TRP A 401 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 341 ? LEU A 347 ? PRO A 418 LEU A 424 5 ? 7  
HELX_P HELX_P14 AB5 PRO A 364 ? LEU A 370 ? PRO A 441 LEU A 447 5 ? 7  
HELX_P HELX_P15 AB6 PRO A 387 ? LEU A 393 ? PRO A 464 LEU A 470 5 ? 7  
HELX_P HELX_P16 AB7 PRO A 410 ? LEU A 416 ? PRO A 487 LEU A 493 5 ? 7  
HELX_P HELX_P17 AB8 PRO A 433 ? LEU A 439 ? PRO A 510 LEU A 516 5 ? 7  
HELX_P HELX_P18 AB9 PRO A 457 ? CYS A 463 ? PRO A 534 CYS A 540 5 ? 7  
HELX_P HELX_P19 AC1 PRO A 480 ? GLY A 486 ? PRO A 557 GLY A 563 1 ? 7  
HELX_P HELX_P20 AC2 GLY A 487 ? GLN A 498 ? GLY A 564 GLN A 575 1 ? 12 
HELX_P HELX_P21 AC3 TYR A 501 ? VAL A 505 ? TYR A 578 VAL A 582 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A ASN 239 OD1 ? ? ? 1_555 C K   . K ? ? A ASN 316 A K   602 1_555 ? ? ? ? ? ? ? 2.797 ? ? 
metalc2 metalc ? ? A ASN 240 O   ? ? ? 1_555 C K   . K ? ? A ASN 317 A K   602 1_555 ? ? ? ? ? ? ? 2.659 ? ? 
metalc3 metalc ? ? A ARG 263 O   ? ? ? 1_555 C K   . K ? ? A ARG 340 A K   602 1_555 ? ? ? ? ? ? ? 2.617 ? ? 
metalc4 metalc ? ? C K   .   K   ? ? ? 1_555 D HOH . O ? ? A K   602 A HOH 765 1_555 ? ? ? ? ? ? ? 2.761 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OD1 ? A ASN 239 ? A ASN 316 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? A ASN 240 ? A ASN 317 ? 1_555 112.2 ? 
2 OD1 ? A ASN 239 ? A ASN 316 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? A ARG 263 ? A ARG 340 ? 1_555 92.6  ? 
3 O   ? A ASN 240 ? A ASN 317 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? A ARG 263 ? A ARG 340 ? 1_555 73.9  ? 
4 OD1 ? A ASN 239 ? A ASN 316 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? D HOH .   ? A HOH 765 ? 1_555 73.8  ? 
5 O   ? A ASN 240 ? A ASN 317 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? D HOH .   ? A HOH 765 ? 1_555 80.8  ? 
6 O   ? A ARG 263 ? A ARG 340 ? 1_555 K ? C K . ? A K 602 ? 1_555 O ? D HOH .   ? A HOH 765 ? 1_555 144.1 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   20 
_struct_sheet.details          ? 
# 
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  ? parallel 
AA1 2  3  ? parallel 
AA1 3  4  ? parallel 
AA1 4  5  ? parallel 
AA1 5  6  ? parallel 
AA1 6  7  ? parallel 
AA1 7  8  ? parallel 
AA1 8  9  ? parallel 
AA1 9  10 ? parallel 
AA1 10 11 ? parallel 
AA1 11 12 ? parallel 
AA1 12 13 ? parallel 
AA1 13 14 ? parallel 
AA1 14 15 ? parallel 
AA1 15 16 ? parallel 
AA1 16 17 ? parallel 
AA1 17 18 ? parallel 
AA1 18 19 ? parallel 
AA1 19 20 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ARG A 27  ? ASP A 29  ? ARG A 104 ASP A 106 
AA1 2  GLU A 50  ? TYR A 52  ? GLU A 127 TYR A 129 
AA1 3  THR A 73  ? ALA A 75  ? THR A 150 ALA A 152 
AA1 4  MET A 96  ? ASP A 98  ? MET A 173 ASP A 175 
AA1 5  THR A 119 ? TYR A 121 ? THR A 196 TYR A 198 
AA1 6  MET A 142 ? SER A 144 ? MET A 219 SER A 221 
AA1 7  THR A 165 ? ASP A 167 ? THR A 242 ASP A 244 
AA1 8  ASN A 188 ? ASP A 190 ? ASN A 265 ASP A 267 
AA1 9  ARG A 211 ? GLY A 213 ? ARG A 288 GLY A 290 
AA1 10 GLU A 234 ? ASN A 236 ? GLU A 311 ASN A 313 
AA1 11 SER A 258 ? THR A 260 ? SER A 335 THR A 337 
AA1 12 SER A 282 ? ASN A 284 ? SER A 359 ASN A 361 
AA1 13 LYS A 306 ? ASN A 308 ? LYS A 383 ASN A 385 
AA1 14 GLU A 329 ? ASN A 331 ? GLU A 406 ASN A 408 
AA1 15 VAL A 352 ? ILE A 354 ? VAL A 429 ILE A 431 
AA1 16 GLU A 375 ? ASP A 377 ? GLU A 452 ASP A 454 
AA1 17 LYS A 398 ? VAL A 400 ? LYS A 475 VAL A 477 
AA1 18 HIS A 421 ? GLY A 423 ? HIS A 498 GLY A 500 
AA1 19 GLU A 444 ? TYR A 446 ? GLU A 521 TYR A 523 
AA1 20 ILE A 468 ? SER A 470 ? ILE A 545 SER A 547 
# 
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 LEU A 28  ? N LEU A 105 O TYR A 52  ? O TYR A 129 
AA1 2  3  N LEU A 51  ? N LEU A 128 O ALA A 75  ? O ALA A 152 
AA1 3  4  N LEU A 74  ? N LEU A 151 O MET A 96  ? O MET A 173 
AA1 4  5  N LEU A 97  ? N LEU A 174 O THR A 119 ? O THR A 196 
AA1 5  6  N LEU A 120 ? N LEU A 197 O SER A 144 ? O SER A 221 
AA1 6  7  N LEU A 143 ? N LEU A 220 O THR A 165 ? O THR A 242 
AA1 7  8  N LEU A 166 ? N LEU A 243 O ASN A 188 ? O ASN A 265 
AA1 8  9  N LEU A 189 ? N LEU A 266 O ARG A 211 ? O ARG A 288 
AA1 9  10 N LEU A 212 ? N LEU A 289 O GLU A 234 ? O GLU A 311 
AA1 10 11 N LEU A 235 ? N LEU A 312 O SER A 258 ? O SER A 335 
AA1 11 12 N LEU A 259 ? N LEU A 336 O SER A 282 ? O SER A 359 
AA1 12 13 N LEU A 283 ? N LEU A 360 O LYS A 306 ? O LYS A 383 
AA1 13 14 N LEU A 307 ? N LEU A 384 O ASN A 331 ? O ASN A 408 
AA1 14 15 N LEU A 330 ? N LEU A 407 O ILE A 354 ? O ILE A 431 
AA1 15 16 N LEU A 353 ? N LEU A 430 O ASP A 377 ? O ASP A 454 
AA1 16 17 N LEU A 376 ? N LEU A 453 O VAL A 400 ? O VAL A 477 
AA1 17 18 N LEU A 399 ? N LEU A 476 O GLY A 423 ? O GLY A 500 
AA1 18 19 N LEU A 422 ? N LEU A 499 O GLU A 444 ? O GLU A 521 
AA1 19 20 N LEU A 445 ? N LEU A 522 O ILE A 468 ? O ILE A 545 
# 
_pdbx_entry_details.entry_id                   9BTP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 110 ? ? -141.61 -1.62   
2  1 ASP A 166 ? ? -33.06  -38.71  
3  1 ASN A 179 ? ? -125.81 -159.13 
4  1 PHE A 201 ? ? 59.50   71.39   
5  1 LEU A 214 ? ? -94.10  53.30   
6  1 ASN A 225 ? ? -132.39 -151.29 
7  1 ASN A 248 ? ? -123.71 -153.50 
8  1 ASN A 271 ? ? -124.35 -147.79 
9  1 TYR A 293 ? ? 68.16   61.45   
10 1 ASN A 316 ? ? 60.00   63.27   
11 1 ASN A 317 ? ? -123.55 -159.01 
12 1 ASN A 341 ? ? -115.72 -146.26 
13 1 ASN A 365 ? ? -132.74 -158.78 
14 1 ASN A 389 ? ? -120.42 -148.96 
15 1 ASN A 412 ? ? -108.95 -167.40 
16 1 ASN A 435 ? ? -97.03  -150.47 
17 1 ASN A 458 ? ? -103.18 -156.10 
18 1 ASN A 481 ? ? -115.82 -164.40 
19 1 ASN A 504 ? ? -115.45 -164.11 
20 1 ILE A 548 ? ? -145.05 18.81   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         4.2237248115 
_pdbx_refine_tls.origin_y         -8.21995320894 
_pdbx_refine_tls.origin_z         -31.3825079299 
_pdbx_refine_tls.T[1][1]          0.267325339502 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0269755882946 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0156517277402 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.242844806576 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0150570216297 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.272991691224 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.116895490924 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.129621169331 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0435874285771 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.377622377259 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.323620997022 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.537697395379 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.00859990046397 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0174016690227 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          7.24472077676e-05 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0121648899098 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0092727638914 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.00707379437539 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.067431246948 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0205082791118 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.00386953211437 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    L 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    B 
_pdbx_refine_tls_group.end_auth_seq_id     1 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 GLY 78 ? A GLY 1 
2 1 Y 1 A PRO 79 ? A PRO 2 
3 1 Y 1 A GLY 80 ? A GLY 3 
4 1 Y 1 A THR 81 ? A THR 4 
5 1 Y 1 A ARG 82 ? A ARG 5 
6 1 Y 1 A LYS 83 ? A LYS 6 
# 
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 
A1ATZ C1   C  N N 1   
A1ATZ C2   C  N S 2   
A1ATZ C3   C  Y N 3   
A1ATZ O1   O  N N 4   
A1ATZ O2   O  N N 5   
A1ATZ O3   O  N N 6   
A1ATZ C11  C  Y N 7   
A1ATZ C12  C  Y N 8   
A1ATZ C13  C  Y N 9   
A1ATZ C14  C  Y N 10  
A1ATZ C15  C  Y N 11  
A1ATZ C16  C  N N 12  
A1ATZ C17  C  Y N 13  
A1ATZ C18  C  Y N 14  
A1ATZ C19  C  Y N 15  
A1ATZ C20  C  Y N 16  
A1ATZ C21  C  Y N 17  
A1ATZ C22  C  Y N 18  
A1ATZ C23  C  Y N 19  
A1ATZ C24  C  Y N 20  
A1ATZ C25  C  Y N 21  
A1ATZ C26  C  Y N 22  
A1ATZ C27  C  Y N 23  
A1ATZ C28  C  Y N 24  
A1ATZ C10  C  Y N 25  
A1ATZ C4   C  Y N 26  
A1ATZ C5   C  Y N 27  
A1ATZ C6   C  Y N 28  
A1ATZ C7   C  N N 29  
A1ATZ C8   C  Y N 30  
A1ATZ C9   C  Y N 31  
A1ATZ N1   N  N N 32  
A1ATZ N2   N  N N 33  
A1ATZ O4   O  N N 34  
A1ATZ O5   O  N N 35  
A1ATZ CL1  CL N N 36  
A1ATZ H2   H  N N 37  
A1ATZ H1   H  N N 38  
A1ATZ H8   H  N N 39  
A1ATZ H9   H  N N 40  
A1ATZ H10  H  N N 41  
A1ATZ H11  H  N N 42  
A1ATZ H12  H  N N 43  
A1ATZ H13  H  N N 44  
A1ATZ H14  H  N N 45  
A1ATZ H15  H  N N 46  
A1ATZ H16  H  N N 47  
A1ATZ H17  H  N N 48  
A1ATZ H18  H  N N 49  
A1ATZ H19  H  N N 50  
A1ATZ H20  H  N N 51  
A1ATZ H21  H  N N 52  
A1ATZ H4   H  N N 53  
A1ATZ H5   H  N N 54  
A1ATZ H7   H  N N 55  
A1ATZ H3   H  N N 56  
A1ATZ H6   H  N N 57  
ALA   N    N  N N 58  
ALA   CA   C  N S 59  
ALA   C    C  N N 60  
ALA   O    O  N N 61  
ALA   CB   C  N N 62  
ALA   OXT  O  N N 63  
ALA   H    H  N N 64  
ALA   H2   H  N N 65  
ALA   HA   H  N N 66  
ALA   HB1  H  N N 67  
ALA   HB2  H  N N 68  
ALA   HB3  H  N N 69  
ALA   HXT  H  N N 70  
ARG   N    N  N N 71  
ARG   CA   C  N S 72  
ARG   C    C  N N 73  
ARG   O    O  N N 74  
ARG   CB   C  N N 75  
ARG   CG   C  N N 76  
ARG   CD   C  N N 77  
ARG   NE   N  N N 78  
ARG   CZ   C  N N 79  
ARG   NH1  N  N N 80  
ARG   NH2  N  N N 81  
ARG   OXT  O  N N 82  
ARG   H    H  N N 83  
ARG   H2   H  N N 84  
ARG   HA   H  N N 85  
ARG   HB2  H  N N 86  
ARG   HB3  H  N N 87  
ARG   HG2  H  N N 88  
ARG   HG3  H  N N 89  
ARG   HD2  H  N N 90  
ARG   HD3  H  N N 91  
ARG   HE   H  N N 92  
ARG   HH11 H  N N 93  
ARG   HH12 H  N N 94  
ARG   HH21 H  N N 95  
ARG   HH22 H  N N 96  
ARG   HXT  H  N N 97  
ASN   N    N  N N 98  
ASN   CA   C  N S 99  
ASN   C    C  N N 100 
ASN   O    O  N N 101 
ASN   CB   C  N N 102 
ASN   CG   C  N N 103 
ASN   OD1  O  N N 104 
ASN   ND2  N  N N 105 
ASN   OXT  O  N N 106 
ASN   H    H  N N 107 
ASN   H2   H  N N 108 
ASN   HA   H  N N 109 
ASN   HB2  H  N N 110 
ASN   HB3  H  N N 111 
ASN   HD21 H  N N 112 
ASN   HD22 H  N N 113 
ASN   HXT  H  N N 114 
ASP   N    N  N N 115 
ASP   CA   C  N S 116 
ASP   C    C  N N 117 
ASP   O    O  N N 118 
ASP   CB   C  N N 119 
ASP   CG   C  N N 120 
ASP   OD1  O  N N 121 
ASP   OD2  O  N N 122 
ASP   OXT  O  N N 123 
ASP   H    H  N N 124 
ASP   H2   H  N N 125 
ASP   HA   H  N N 126 
ASP   HB2  H  N N 127 
ASP   HB3  H  N N 128 
ASP   HD2  H  N N 129 
ASP   HXT  H  N N 130 
CYS   N    N  N N 131 
CYS   CA   C  N R 132 
CYS   C    C  N N 133 
CYS   O    O  N N 134 
CYS   CB   C  N N 135 
CYS   SG   S  N N 136 
CYS   OXT  O  N N 137 
CYS   H    H  N N 138 
CYS   H2   H  N N 139 
CYS   HA   H  N N 140 
CYS   HB2  H  N N 141 
CYS   HB3  H  N N 142 
CYS   HG   H  N N 143 
CYS   HXT  H  N N 144 
GLN   N    N  N N 145 
GLN   CA   C  N S 146 
GLN   C    C  N N 147 
GLN   O    O  N N 148 
GLN   CB   C  N N 149 
GLN   CG   C  N N 150 
GLN   CD   C  N N 151 
GLN   OE1  O  N N 152 
GLN   NE2  N  N N 153 
GLN   OXT  O  N N 154 
GLN   H    H  N N 155 
GLN   H2   H  N N 156 
GLN   HA   H  N N 157 
GLN   HB2  H  N N 158 
GLN   HB3  H  N N 159 
GLN   HG2  H  N N 160 
GLN   HG3  H  N N 161 
GLN   HE21 H  N N 162 
GLN   HE22 H  N N 163 
GLN   HXT  H  N N 164 
GLU   N    N  N N 165 
GLU   CA   C  N S 166 
GLU   C    C  N N 167 
GLU   O    O  N N 168 
GLU   CB   C  N N 169 
GLU   CG   C  N N 170 
GLU   CD   C  N N 171 
GLU   OE1  O  N N 172 
GLU   OE2  O  N N 173 
GLU   OXT  O  N N 174 
GLU   H    H  N N 175 
GLU   H2   H  N N 176 
GLU   HA   H  N N 177 
GLU   HB2  H  N N 178 
GLU   HB3  H  N N 179 
GLU   HG2  H  N N 180 
GLU   HG3  H  N N 181 
GLU   HE2  H  N N 182 
GLU   HXT  H  N N 183 
GLY   N    N  N N 184 
GLY   CA   C  N N 185 
GLY   C    C  N N 186 
GLY   O    O  N N 187 
GLY   OXT  O  N N 188 
GLY   H    H  N N 189 
GLY   H2   H  N N 190 
GLY   HA2  H  N N 191 
GLY   HA3  H  N N 192 
GLY   HXT  H  N N 193 
HIS   N    N  N N 194 
HIS   CA   C  N S 195 
HIS   C    C  N N 196 
HIS   O    O  N N 197 
HIS   CB   C  N N 198 
HIS   CG   C  Y N 199 
HIS   ND1  N  Y N 200 
HIS   CD2  C  Y N 201 
HIS   CE1  C  Y N 202 
HIS   NE2  N  Y N 203 
HIS   OXT  O  N N 204 
HIS   H    H  N N 205 
HIS   H2   H  N N 206 
HIS   HA   H  N N 207 
HIS   HB2  H  N N 208 
HIS   HB3  H  N N 209 
HIS   HD1  H  N N 210 
HIS   HD2  H  N N 211 
HIS   HE1  H  N N 212 
HIS   HE2  H  N N 213 
HIS   HXT  H  N N 214 
HOH   O    O  N N 215 
HOH   H1   H  N N 216 
HOH   H2   H  N N 217 
ILE   N    N  N N 218 
ILE   CA   C  N S 219 
ILE   C    C  N N 220 
ILE   O    O  N N 221 
ILE   CB   C  N S 222 
ILE   CG1  C  N N 223 
ILE   CG2  C  N N 224 
ILE   CD1  C  N N 225 
ILE   OXT  O  N N 226 
ILE   H    H  N N 227 
ILE   H2   H  N N 228 
ILE   HA   H  N N 229 
ILE   HB   H  N N 230 
ILE   HG12 H  N N 231 
ILE   HG13 H  N N 232 
ILE   HG21 H  N N 233 
ILE   HG22 H  N N 234 
ILE   HG23 H  N N 235 
ILE   HD11 H  N N 236 
ILE   HD12 H  N N 237 
ILE   HD13 H  N N 238 
ILE   HXT  H  N N 239 
K     K    K  N N 240 
LEU   N    N  N N 241 
LEU   CA   C  N S 242 
LEU   C    C  N N 243 
LEU   O    O  N N 244 
LEU   CB   C  N N 245 
LEU   CG   C  N N 246 
LEU   CD1  C  N N 247 
LEU   CD2  C  N N 248 
LEU   OXT  O  N N 249 
LEU   H    H  N N 250 
LEU   H2   H  N N 251 
LEU   HA   H  N N 252 
LEU   HB2  H  N N 253 
LEU   HB3  H  N N 254 
LEU   HG   H  N N 255 
LEU   HD11 H  N N 256 
LEU   HD12 H  N N 257 
LEU   HD13 H  N N 258 
LEU   HD21 H  N N 259 
LEU   HD22 H  N N 260 
LEU   HD23 H  N N 261 
LEU   HXT  H  N N 262 
LYS   N    N  N N 263 
LYS   CA   C  N S 264 
LYS   C    C  N N 265 
LYS   O    O  N N 266 
LYS   CB   C  N N 267 
LYS   CG   C  N N 268 
LYS   CD   C  N N 269 
LYS   CE   C  N N 270 
LYS   NZ   N  N N 271 
LYS   OXT  O  N N 272 
LYS   H    H  N N 273 
LYS   H2   H  N N 274 
LYS   HA   H  N N 275 
LYS   HB2  H  N N 276 
LYS   HB3  H  N N 277 
LYS   HG2  H  N N 278 
LYS   HG3  H  N N 279 
LYS   HD2  H  N N 280 
LYS   HD3  H  N N 281 
LYS   HE2  H  N N 282 
LYS   HE3  H  N N 283 
LYS   HZ1  H  N N 284 
LYS   HZ2  H  N N 285 
LYS   HZ3  H  N N 286 
LYS   HXT  H  N N 287 
MET   N    N  N N 288 
MET   CA   C  N S 289 
MET   C    C  N N 290 
MET   O    O  N N 291 
MET   CB   C  N N 292 
MET   CG   C  N N 293 
MET   SD   S  N N 294 
MET   CE   C  N N 295 
MET   OXT  O  N N 296 
MET   H    H  N N 297 
MET   H2   H  N N 298 
MET   HA   H  N N 299 
MET   HB2  H  N N 300 
MET   HB3  H  N N 301 
MET   HG2  H  N N 302 
MET   HG3  H  N N 303 
MET   HE1  H  N N 304 
MET   HE2  H  N N 305 
MET   HE3  H  N N 306 
MET   HXT  H  N N 307 
PHE   N    N  N N 308 
PHE   CA   C  N S 309 
PHE   C    C  N N 310 
PHE   O    O  N N 311 
PHE   CB   C  N N 312 
PHE   CG   C  Y N 313 
PHE   CD1  C  Y N 314 
PHE   CD2  C  Y N 315 
PHE   CE1  C  Y N 316 
PHE   CE2  C  Y N 317 
PHE   CZ   C  Y N 318 
PHE   OXT  O  N N 319 
PHE   H    H  N N 320 
PHE   H2   H  N N 321 
PHE   HA   H  N N 322 
PHE   HB2  H  N N 323 
PHE   HB3  H  N N 324 
PHE   HD1  H  N N 325 
PHE   HD2  H  N N 326 
PHE   HE1  H  N N 327 
PHE   HE2  H  N N 328 
PHE   HZ   H  N N 329 
PHE   HXT  H  N N 330 
PRO   N    N  N N 331 
PRO   CA   C  N S 332 
PRO   C    C  N N 333 
PRO   O    O  N N 334 
PRO   CB   C  N N 335 
PRO   CG   C  N N 336 
PRO   CD   C  N N 337 
PRO   OXT  O  N N 338 
PRO   H    H  N N 339 
PRO   HA   H  N N 340 
PRO   HB2  H  N N 341 
PRO   HB3  H  N N 342 
PRO   HG2  H  N N 343 
PRO   HG3  H  N N 344 
PRO   HD2  H  N N 345 
PRO   HD3  H  N N 346 
PRO   HXT  H  N N 347 
SER   N    N  N N 348 
SER   CA   C  N S 349 
SER   C    C  N N 350 
SER   O    O  N N 351 
SER   CB   C  N N 352 
SER   OG   O  N N 353 
SER   OXT  O  N N 354 
SER   H    H  N N 355 
SER   H2   H  N N 356 
SER   HA   H  N N 357 
SER   HB2  H  N N 358 
SER   HB3  H  N N 359 
SER   HG   H  N N 360 
SER   HXT  H  N N 361 
THR   N    N  N N 362 
THR   CA   C  N S 363 
THR   C    C  N N 364 
THR   O    O  N N 365 
THR   CB   C  N R 366 
THR   OG1  O  N N 367 
THR   CG2  C  N N 368 
THR   OXT  O  N N 369 
THR   H    H  N N 370 
THR   H2   H  N N 371 
THR   HA   H  N N 372 
THR   HB   H  N N 373 
THR   HG1  H  N N 374 
THR   HG21 H  N N 375 
THR   HG22 H  N N 376 
THR   HG23 H  N N 377 
THR   HXT  H  N N 378 
TRP   N    N  N N 379 
TRP   CA   C  N S 380 
TRP   C    C  N N 381 
TRP   O    O  N N 382 
TRP   CB   C  N N 383 
TRP   CG   C  Y N 384 
TRP   CD1  C  Y N 385 
TRP   CD2  C  Y N 386 
TRP   NE1  N  Y N 387 
TRP   CE2  C  Y N 388 
TRP   CE3  C  Y N 389 
TRP   CZ2  C  Y N 390 
TRP   CZ3  C  Y N 391 
TRP   CH2  C  Y N 392 
TRP   OXT  O  N N 393 
TRP   H    H  N N 394 
TRP   H2   H  N N 395 
TRP   HA   H  N N 396 
TRP   HB2  H  N N 397 
TRP   HB3  H  N N 398 
TRP   HD1  H  N N 399 
TRP   HE1  H  N N 400 
TRP   HE3  H  N N 401 
TRP   HZ2  H  N N 402 
TRP   HZ3  H  N N 403 
TRP   HH2  H  N N 404 
TRP   HXT  H  N N 405 
TYR   N    N  N N 406 
TYR   CA   C  N S 407 
TYR   C    C  N N 408 
TYR   O    O  N N 409 
TYR   CB   C  N N 410 
TYR   CG   C  Y N 411 
TYR   CD1  C  Y N 412 
TYR   CD2  C  Y N 413 
TYR   CE1  C  Y N 414 
TYR   CE2  C  Y N 415 
TYR   CZ   C  Y N 416 
TYR   OH   O  N N 417 
TYR   OXT  O  N N 418 
TYR   H    H  N N 419 
TYR   H2   H  N N 420 
TYR   HA   H  N N 421 
TYR   HB2  H  N N 422 
TYR   HB3  H  N N 423 
TYR   HD1  H  N N 424 
TYR   HD2  H  N N 425 
TYR   HE1  H  N N 426 
TYR   HE2  H  N N 427 
TYR   HH   H  N N 428 
TYR   HXT  H  N N 429 
VAL   N    N  N N 430 
VAL   CA   C  N S 431 
VAL   C    C  N N 432 
VAL   O    O  N N 433 
VAL   CB   C  N N 434 
VAL   CG1  C  N N 435 
VAL   CG2  C  N N 436 
VAL   OXT  O  N N 437 
VAL   H    H  N N 438 
VAL   H2   H  N N 439 
VAL   HA   H  N N 440 
VAL   HB   H  N N 441 
VAL   HG11 H  N N 442 
VAL   HG12 H  N N 443 
VAL   HG13 H  N N 444 
VAL   HG21 H  N N 445 
VAL   HG22 H  N N 446 
VAL   HG23 H  N N 447 
VAL   HXT  H  N N 448 
# 
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 
A1ATZ O1  C1   doub N N 1   
A1ATZ C1  O2   sing N N 2   
A1ATZ C1  C2   sing N N 3   
A1ATZ C2  N1   sing N N 4   
A1ATZ C2  C10  sing N N 5   
A1ATZ N1  C3   sing N N 6   
A1ATZ C3  C4   doub Y N 7   
A1ATZ C3  C9   sing Y N 8   
A1ATZ C4  C5   sing Y N 9   
A1ATZ C5  C6   doub Y N 10  
A1ATZ C6  O3   sing N N 11  
A1ATZ C6  C8   sing Y N 12  
A1ATZ O3  C7   sing N N 13  
A1ATZ C7  O4   doub N N 14  
A1ATZ C7  N2   sing N N 15  
A1ATZ N2  C8   sing N N 16  
A1ATZ C8  C9   doub Y N 17  
A1ATZ C10 C11  doub Y N 18  
A1ATZ C10 C15  sing Y N 19  
A1ATZ C11 C12  sing Y N 20  
A1ATZ C12 C13  doub Y N 21  
A1ATZ C13 C14  sing Y N 22  
A1ATZ C14 C15  doub Y N 23  
A1ATZ C15 O5   sing N N 24  
A1ATZ O5  C16  sing N N 25  
A1ATZ C16 C17  sing N N 26  
A1ATZ C17 C18  doub Y N 27  
A1ATZ C17 C28  sing Y N 28  
A1ATZ C18 C19  sing Y N 29  
A1ATZ C19 C20  sing N N 30  
A1ATZ C19 C26  doub Y N 31  
A1ATZ C20 C21  doub Y N 32  
A1ATZ C20 C25  sing Y N 33  
A1ATZ C21 C22  sing Y N 34  
A1ATZ C22 C23  doub Y N 35  
A1ATZ C23 C24  sing Y N 36  
A1ATZ C24 C25  doub Y N 37  
A1ATZ C26 C27  sing Y N 38  
A1ATZ C27 C28  doub Y N 39  
A1ATZ C28 CL1  sing N N 40  
A1ATZ C2  H2   sing N N 41  
A1ATZ O2  H1   sing N N 42  
A1ATZ C11 H8   sing N N 43  
A1ATZ C12 H9   sing N N 44  
A1ATZ C13 H10  sing N N 45  
A1ATZ C14 H11  sing N N 46  
A1ATZ C16 H12  sing N N 47  
A1ATZ C16 H13  sing N N 48  
A1ATZ C18 H14  sing N N 49  
A1ATZ C21 H15  sing N N 50  
A1ATZ C22 H16  sing N N 51  
A1ATZ C23 H17  sing N N 52  
A1ATZ C24 H18  sing N N 53  
A1ATZ C25 H19  sing N N 54  
A1ATZ C26 H20  sing N N 55  
A1ATZ C27 H21  sing N N 56  
A1ATZ C4  H4   sing N N 57  
A1ATZ C5  H5   sing N N 58  
A1ATZ C9  H7   sing N N 59  
A1ATZ N1  H3   sing N N 60  
A1ATZ N2  H6   sing N N 61  
ALA   N   CA   sing N N 62  
ALA   N   H    sing N N 63  
ALA   N   H2   sing N N 64  
ALA   CA  C    sing N N 65  
ALA   CA  CB   sing N N 66  
ALA   CA  HA   sing N N 67  
ALA   C   O    doub N N 68  
ALA   C   OXT  sing N N 69  
ALA   CB  HB1  sing N N 70  
ALA   CB  HB2  sing N N 71  
ALA   CB  HB3  sing N N 72  
ALA   OXT HXT  sing N N 73  
ARG   N   CA   sing N N 74  
ARG   N   H    sing N N 75  
ARG   N   H2   sing N N 76  
ARG   CA  C    sing N N 77  
ARG   CA  CB   sing N N 78  
ARG   CA  HA   sing N N 79  
ARG   C   O    doub N N 80  
ARG   C   OXT  sing N N 81  
ARG   CB  CG   sing N N 82  
ARG   CB  HB2  sing N N 83  
ARG   CB  HB3  sing N N 84  
ARG   CG  CD   sing N N 85  
ARG   CG  HG2  sing N N 86  
ARG   CG  HG3  sing N N 87  
ARG   CD  NE   sing N N 88  
ARG   CD  HD2  sing N N 89  
ARG   CD  HD3  sing N N 90  
ARG   NE  CZ   sing N N 91  
ARG   NE  HE   sing N N 92  
ARG   CZ  NH1  sing N N 93  
ARG   CZ  NH2  doub N N 94  
ARG   NH1 HH11 sing N N 95  
ARG   NH1 HH12 sing N N 96  
ARG   NH2 HH21 sing N N 97  
ARG   NH2 HH22 sing N N 98  
ARG   OXT HXT  sing N N 99  
ASN   N   CA   sing N N 100 
ASN   N   H    sing N N 101 
ASN   N   H2   sing N N 102 
ASN   CA  C    sing N N 103 
ASN   CA  CB   sing N N 104 
ASN   CA  HA   sing N N 105 
ASN   C   O    doub N N 106 
ASN   C   OXT  sing N N 107 
ASN   CB  CG   sing N N 108 
ASN   CB  HB2  sing N N 109 
ASN   CB  HB3  sing N N 110 
ASN   CG  OD1  doub N N 111 
ASN   CG  ND2  sing N N 112 
ASN   ND2 HD21 sing N N 113 
ASN   ND2 HD22 sing N N 114 
ASN   OXT HXT  sing N N 115 
ASP   N   CA   sing N N 116 
ASP   N   H    sing N N 117 
ASP   N   H2   sing N N 118 
ASP   CA  C    sing N N 119 
ASP   CA  CB   sing N N 120 
ASP   CA  HA   sing N N 121 
ASP   C   O    doub N N 122 
ASP   C   OXT  sing N N 123 
ASP   CB  CG   sing N N 124 
ASP   CB  HB2  sing N N 125 
ASP   CB  HB3  sing N N 126 
ASP   CG  OD1  doub N N 127 
ASP   CG  OD2  sing N N 128 
ASP   OD2 HD2  sing N N 129 
ASP   OXT HXT  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
GLN   N   CA   sing N N 144 
GLN   N   H    sing N N 145 
GLN   N   H2   sing N N 146 
GLN   CA  C    sing N N 147 
GLN   CA  CB   sing N N 148 
GLN   CA  HA   sing N N 149 
GLN   C   O    doub N N 150 
GLN   C   OXT  sing N N 151 
GLN   CB  CG   sing N N 152 
GLN   CB  HB2  sing N N 153 
GLN   CB  HB3  sing N N 154 
GLN   CG  CD   sing N N 155 
GLN   CG  HG2  sing N N 156 
GLN   CG  HG3  sing N N 157 
GLN   CD  OE1  doub N N 158 
GLN   CD  NE2  sing N N 159 
GLN   NE2 HE21 sing N N 160 
GLN   NE2 HE22 sing N N 161 
GLN   OXT HXT  sing N N 162 
GLU   N   CA   sing N N 163 
GLU   N   H    sing N N 164 
GLU   N   H2   sing N N 165 
GLU   CA  C    sing N N 166 
GLU   CA  CB   sing N N 167 
GLU   CA  HA   sing N N 168 
GLU   C   O    doub N N 169 
GLU   C   OXT  sing N N 170 
GLU   CB  CG   sing N N 171 
GLU   CB  HB2  sing N N 172 
GLU   CB  HB3  sing N N 173 
GLU   CG  CD   sing N N 174 
GLU   CG  HG2  sing N N 175 
GLU   CG  HG3  sing N N 176 
GLU   CD  OE1  doub N N 177 
GLU   CD  OE2  sing N N 178 
GLU   OE2 HE2  sing N N 179 
GLU   OXT HXT  sing N N 180 
GLY   N   CA   sing N N 181 
GLY   N   H    sing N N 182 
GLY   N   H2   sing N N 183 
GLY   CA  C    sing N N 184 
GLY   CA  HA2  sing N N 185 
GLY   CA  HA3  sing N N 186 
GLY   C   O    doub N N 187 
GLY   C   OXT  sing N N 188 
GLY   OXT HXT  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
HOH   O   H1   sing N N 211 
HOH   O   H2   sing N N 212 
ILE   N   CA   sing N N 213 
ILE   N   H    sing N N 214 
ILE   N   H2   sing N N 215 
ILE   CA  C    sing N N 216 
ILE   CA  CB   sing N N 217 
ILE   CA  HA   sing N N 218 
ILE   C   O    doub N N 219 
ILE   C   OXT  sing N N 220 
ILE   CB  CG1  sing N N 221 
ILE   CB  CG2  sing N N 222 
ILE   CB  HB   sing N N 223 
ILE   CG1 CD1  sing N N 224 
ILE   CG1 HG12 sing N N 225 
ILE   CG1 HG13 sing N N 226 
ILE   CG2 HG21 sing N N 227 
ILE   CG2 HG22 sing N N 228 
ILE   CG2 HG23 sing N N 229 
ILE   CD1 HD11 sing N N 230 
ILE   CD1 HD12 sing N N 231 
ILE   CD1 HD13 sing N N 232 
ILE   OXT HXT  sing N N 233 
LEU   N   CA   sing N N 234 
LEU   N   H    sing N N 235 
LEU   N   H2   sing N N 236 
LEU   CA  C    sing N N 237 
LEU   CA  CB   sing N N 238 
LEU   CA  HA   sing N N 239 
LEU   C   O    doub N N 240 
LEU   C   OXT  sing N N 241 
LEU   CB  CG   sing N N 242 
LEU   CB  HB2  sing N N 243 
LEU   CB  HB3  sing N N 244 
LEU   CG  CD1  sing N N 245 
LEU   CG  CD2  sing N N 246 
LEU   CG  HG   sing N N 247 
LEU   CD1 HD11 sing N N 248 
LEU   CD1 HD12 sing N N 249 
LEU   CD1 HD13 sing N N 250 
LEU   CD2 HD21 sing N N 251 
LEU   CD2 HD22 sing N N 252 
LEU   CD2 HD23 sing N N 253 
LEU   OXT HXT  sing N N 254 
LYS   N   CA   sing N N 255 
LYS   N   H    sing N N 256 
LYS   N   H2   sing N N 257 
LYS   CA  C    sing N N 258 
LYS   CA  CB   sing N N 259 
LYS   CA  HA   sing N N 260 
LYS   C   O    doub N N 261 
LYS   C   OXT  sing N N 262 
LYS   CB  CG   sing N N 263 
LYS   CB  HB2  sing N N 264 
LYS   CB  HB3  sing N N 265 
LYS   CG  CD   sing N N 266 
LYS   CG  HG2  sing N N 267 
LYS   CG  HG3  sing N N 268 
LYS   CD  CE   sing N N 269 
LYS   CD  HD2  sing N N 270 
LYS   CD  HD3  sing N N 271 
LYS   CE  NZ   sing N N 272 
LYS   CE  HE2  sing N N 273 
LYS   CE  HE3  sing N N 274 
LYS   NZ  HZ1  sing N N 275 
LYS   NZ  HZ2  sing N N 276 
LYS   NZ  HZ3  sing N N 277 
LYS   OXT HXT  sing N N 278 
MET   N   CA   sing N N 279 
MET   N   H    sing N N 280 
MET   N   H2   sing N N 281 
MET   CA  C    sing N N 282 
MET   CA  CB   sing N N 283 
MET   CA  HA   sing N N 284 
MET   C   O    doub N N 285 
MET   C   OXT  sing N N 286 
MET   CB  CG   sing N N 287 
MET   CB  HB2  sing N N 288 
MET   CB  HB3  sing N N 289 
MET   CG  SD   sing N N 290 
MET   CG  HG2  sing N N 291 
MET   CG  HG3  sing N N 292 
MET   SD  CE   sing N N 293 
MET   CE  HE1  sing N N 294 
MET   CE  HE2  sing N N 295 
MET   CE  HE3  sing N N 296 
MET   OXT HXT  sing N N 297 
PHE   N   CA   sing N N 298 
PHE   N   H    sing N N 299 
PHE   N   H2   sing N N 300 
PHE   CA  C    sing N N 301 
PHE   CA  CB   sing N N 302 
PHE   CA  HA   sing N N 303 
PHE   C   O    doub N N 304 
PHE   C   OXT  sing N N 305 
PHE   CB  CG   sing N N 306 
PHE   CB  HB2  sing N N 307 
PHE   CB  HB3  sing N N 308 
PHE   CG  CD1  doub Y N 309 
PHE   CG  CD2  sing Y N 310 
PHE   CD1 CE1  sing Y N 311 
PHE   CD1 HD1  sing N N 312 
PHE   CD2 CE2  doub Y N 313 
PHE   CD2 HD2  sing N N 314 
PHE   CE1 CZ   doub Y N 315 
PHE   CE1 HE1  sing N N 316 
PHE   CE2 CZ   sing Y N 317 
PHE   CE2 HE2  sing N N 318 
PHE   CZ  HZ   sing N N 319 
PHE   OXT HXT  sing N N 320 
PRO   N   CA   sing N N 321 
PRO   N   CD   sing N N 322 
PRO   N   H    sing N N 323 
PRO   CA  C    sing N N 324 
PRO   CA  CB   sing N N 325 
PRO   CA  HA   sing N N 326 
PRO   C   O    doub N N 327 
PRO   C   OXT  sing N N 328 
PRO   CB  CG   sing N N 329 
PRO   CB  HB2  sing N N 330 
PRO   CB  HB3  sing N N 331 
PRO   CG  CD   sing N N 332 
PRO   CG  HG2  sing N N 333 
PRO   CG  HG3  sing N N 334 
PRO   CD  HD2  sing N N 335 
PRO   CD  HD3  sing N N 336 
PRO   OXT HXT  sing N N 337 
SER   N   CA   sing N N 338 
SER   N   H    sing N N 339 
SER   N   H2   sing N N 340 
SER   CA  C    sing N N 341 
SER   CA  CB   sing N N 342 
SER   CA  HA   sing N N 343 
SER   C   O    doub N N 344 
SER   C   OXT  sing N N 345 
SER   CB  OG   sing N N 346 
SER   CB  HB2  sing N N 347 
SER   CB  HB3  sing N N 348 
SER   OG  HG   sing N N 349 
SER   OXT HXT  sing N N 350 
THR   N   CA   sing N N 351 
THR   N   H    sing N N 352 
THR   N   H2   sing N N 353 
THR   CA  C    sing N N 354 
THR   CA  CB   sing N N 355 
THR   CA  HA   sing N N 356 
THR   C   O    doub N N 357 
THR   C   OXT  sing N N 358 
THR   CB  OG1  sing N N 359 
THR   CB  CG2  sing N N 360 
THR   CB  HB   sing N N 361 
THR   OG1 HG1  sing N N 362 
THR   CG2 HG21 sing N N 363 
THR   CG2 HG22 sing N N 364 
THR   CG2 HG23 sing N N 365 
THR   OXT HXT  sing N N 366 
TRP   N   CA   sing N N 367 
TRP   N   H    sing N N 368 
TRP   N   H2   sing N N 369 
TRP   CA  C    sing N N 370 
TRP   CA  CB   sing N N 371 
TRP   CA  HA   sing N N 372 
TRP   C   O    doub N N 373 
TRP   C   OXT  sing N N 374 
TRP   CB  CG   sing N N 375 
TRP   CB  HB2  sing N N 376 
TRP   CB  HB3  sing N N 377 
TRP   CG  CD1  doub Y N 378 
TRP   CG  CD2  sing Y N 379 
TRP   CD1 NE1  sing Y N 380 
TRP   CD1 HD1  sing N N 381 
TRP   CD2 CE2  doub Y N 382 
TRP   CD2 CE3  sing Y N 383 
TRP   NE1 CE2  sing Y N 384 
TRP   NE1 HE1  sing N N 385 
TRP   CE2 CZ2  sing Y N 386 
TRP   CE3 CZ3  doub Y N 387 
TRP   CE3 HE3  sing N N 388 
TRP   CZ2 CH2  doub Y N 389 
TRP   CZ2 HZ2  sing N N 390 
TRP   CZ3 CH2  sing Y N 391 
TRP   CZ3 HZ3  sing N N 392 
TRP   CH2 HH2  sing N N 393 
TRP   OXT HXT  sing N N 394 
TYR   N   CA   sing N N 395 
TYR   N   H    sing N N 396 
TYR   N   H2   sing N N 397 
TYR   CA  C    sing N N 398 
TYR   CA  CB   sing N N 399 
TYR   CA  HA   sing N N 400 
TYR   C   O    doub N N 401 
TYR   C   OXT  sing N N 402 
TYR   CB  CG   sing N N 403 
TYR   CB  HB2  sing N N 404 
TYR   CB  HB3  sing N N 405 
TYR   CG  CD1  doub Y N 406 
TYR   CG  CD2  sing Y N 407 
TYR   CD1 CE1  sing Y N 408 
TYR   CD1 HD1  sing N N 409 
TYR   CD2 CE2  doub Y N 410 
TYR   CD2 HD2  sing N N 411 
TYR   CE1 CZ   doub Y N 412 
TYR   CE1 HE1  sing N N 413 
TYR   CE2 CZ   sing Y N 414 
TYR   CE2 HE2  sing N N 415 
TYR   CZ  OH   sing N N 416 
TYR   OH  HH   sing N N 417 
TYR   OXT HXT  sing N N 418 
VAL   N   CA   sing N N 419 
VAL   N   H    sing N N 420 
VAL   N   H2   sing N N 421 
VAL   CA  C    sing N N 422 
VAL   CA  CB   sing N N 423 
VAL   CA  HA   sing N N 424 
VAL   C   O    doub N N 425 
VAL   C   OXT  sing N N 426 
VAL   CB  CG1  sing N N 427 
VAL   CB  CG2  sing N N 428 
VAL   CB  HB   sing N N 429 
VAL   CG1 HG11 sing N N 430 
VAL   CG1 HG12 sing N N 431 
VAL   CG1 HG13 sing N N 432 
VAL   CG2 HG21 sing N N 433 
VAL   CG2 HG22 sing N N 434 
VAL   CG2 HG23 sing N N 435 
VAL   OXT HXT  sing N N 436 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7TYG 
_pdbx_initial_refinement_model.details          'SHOC2 apo' 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BTP 
_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]   0.026477 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014344 
_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]   0.005044 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL  ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K   ? ? 16.37977 2.54835 ? ? 4.54127  84.28225 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LYS   A 1 7   ? -11.40909 -4.29405  -63.69648 1.000 41.49626 ?  84  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 7   ? -10.49485 -4.19537  -64.83968 1.000 46.78792 ?  84  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 7   ? -11.01194 -3.27898  -65.97085 1.000 49.68979 ?  84  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 7   ? -11.90579 -3.66536  -66.73182 1.000 50.73746 ?  84  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 7   ? -10.22811 -5.58788  -65.40101 1.000 48.45955 ?  84  LYS   A CB  1 
ATOM   6    C  CG  . LYS   A 1 7   ? -8.87562  -5.73090  -66.06342 1.000 52.90869 ?  84  LYS   A CG  1 
ATOM   7    C  CD  . LYS   A 1 7   ? -8.59441  -4.60092  -67.04315 1.000 48.19301 ?  84  LYS   A CD  1 
ATOM   8    C  CE  . LYS   A 1 7   ? -7.10135  -4.37999  -67.17813 1.000 48.47739 ?  84  LYS   A CE  1 
ATOM   9    N  NZ  . LYS   A 1 7   ? -6.77766  -3.07779  -67.82534 1.000 50.63835 ?  84  LYS   A NZ  1 
ATOM   10   N  N   . SER   A 1 8   ? -10.42244 -2.08977  -66.11181 1.000 45.27750 ?  85  SER   A N   1 
ATOM   11   C  CA  . SER   A 1 8   ? -10.93832 -1.05949  -67.00670 1.000 39.76052 ?  85  SER   A CA  1 
ATOM   12   C  C   . SER   A 1 8   ? -10.12061 -0.98496  -68.28815 1.000 42.03488 ?  85  SER   A C   1 
ATOM   13   O  O   . SER   A 1 8   ? -8.88663  -0.94251  -68.24806 1.000 42.82964 ?  85  SER   A O   1 
ATOM   14   C  CB  . SER   A 1 8   ? -10.93096 0.31141   -66.32730 1.000 42.72645 ?  85  SER   A CB  1 
ATOM   15   O  OG  . SER   A 1 8   ? -11.89851 0.39595   -65.29296 1.000 45.85740 ?  85  SER   A OG  1 
ATOM   16   N  N   . SER   A 1 9   ? -10.81014 -0.93122  -69.41930 1.000 40.20568 ?  86  SER   A N   1 
ATOM   17   C  CA  . SER   A 1 9   ? -10.13654 -0.63164  -70.66705 1.000 37.83865 ?  86  SER   A CA  1 
ATOM   18   C  C   . SER   A 1 9   ? -9.83289  0.86508   -70.76280 1.000 37.97797 ?  86  SER   A C   1 
ATOM   19   O  O   . SER   A 1 9   ? -10.37184 1.68877   -70.02456 1.000 38.49943 ?  86  SER   A O   1 
ATOM   20   C  CB  . SER   A 1 9   ? -10.98605 -1.06937  -71.85584 1.000 37.65220 ?  86  SER   A CB  1 
ATOM   21   O  OG  . SER   A 1 9   ? -12.16433 -0.28507  -71.93799 1.000 39.78723 ?  86  SER   A OG  1 
ATOM   22   N  N   . ASN   A 1 10  ? -8.95241  1.20535   -71.70390 1.000 37.15867 ?  87  ASN   A N   1 
ATOM   23   C  CA  . ASN   A 1 10  ? -8.62743  2.59588   -71.98809 1.000 34.27936 ?  87  ASN   A CA  1 
ATOM   24   C  C   . ASN   A 1 10  ? -9.88941  3.43177   -72.17221 1.000 34.74361 ?  87  ASN   A C   1 
ATOM   25   O  O   . ASN   A 1 10  ? -10.00575 4.53375   -71.62562 1.000 33.42309 ?  87  ASN   A O   1 
ATOM   26   C  CB  . ASN   A 1 10  ? -7.74018  2.64729   -73.23506 1.000 32.18930 ?  87  ASN   A CB  1 
ATOM   27   C  CG  . ASN   A 1 10  ? -7.21636  4.03644   -73.53476 1.000 35.18888 ?  87  ASN   A CG  1 
ATOM   28   O  OD1 . ASN   A 1 10  ? -6.30913  4.52306   -72.86276 1.000 34.97797 ?  87  ASN   A OD1 1 
ATOM   29   N  ND2 . ASN   A 1 10  ? -7.76646  4.67406   -74.57729 1.000 34.21929 ?  87  ASN   A ND2 1 
ATOM   30   N  N   . ALA   A 1 11  ? -10.84750 2.91807   -72.94327 1.000 32.53206 ?  88  ALA   A N   1 
ATOM   31   C  CA  . ALA   A 1 11  ? -12.07322 3.66482   -73.20707 1.000 33.18512 ?  88  ALA   A CA  1 
ATOM   32   C  C   . ALA   A 1 11  ? -12.88903 3.86127   -71.93633 1.000 36.06789 ?  88  ALA   A C   1 
ATOM   33   O  O   . ALA   A 1 11  ? -13.48590 4.92531   -71.73376 1.000 36.15282 ?  88  ALA   A O   1 
ATOM   34   C  CB  . ALA   A 1 11  ? -12.90849 2.95058   -74.27021 1.000 32.41141 ?  88  ALA   A CB  1 
ATOM   35   N  N   . GLU   A 1 12  ? -12.94343 2.84739   -71.07554 1.000 33.07402 ?  89  GLU   A N   1 
ATOM   36   C  CA  . GLU   A 1 12  ? -13.59100 3.02985   -69.78373 1.000 36.94741 ?  89  GLU   A CA  1 
ATOM   37   C  C   . GLU   A 1 12  ? -12.87713 4.08806   -68.95303 1.000 32.96960 ?  89  GLU   A C   1 
ATOM   38   O  O   . GLU   A 1 12  ? -13.51953 4.89699   -68.27753 1.000 36.75455 ?  89  GLU   A O   1 
ATOM   39   C  CB  . GLU   A 1 12  ? -13.64094 1.70607   -69.02188 1.000 38.83525 ?  89  GLU   A CB  1 
ATOM   40   C  CG  . GLU   A 1 12  ? -14.43639 0.61248   -69.71324 1.000 41.32026 ?  89  GLU   A CG  1 
ATOM   41   C  CD  . GLU   A 1 12  ? -14.55534 -0.62529  -68.84289 1.000 50.27374 ?  89  GLU   A CD  1 
ATOM   42   O  OE1 . GLU   A 1 12  ? -15.29647 -0.56150  -67.83628 1.000 50.48155 ?  89  GLU   A OE1 1 
ATOM   43   O  OE2 . GLU   A 1 12  ? -13.88766 -1.64705  -69.14189 1.000 51.76628 ?  89  GLU   A OE2 1 
ATOM   44   N  N   . VAL   A 1 13  ? -11.54884 4.08976   -68.96771 1.000 32.94365 ?  90  VAL   A N   1 
ATOM   45   C  CA  . VAL   A 1 13  ? -10.82757 5.11711   -68.22661 1.000 34.34172 ?  90  VAL   A CA  1 
ATOM   46   C  C   . VAL   A 1 13  ? -11.17854 6.48743   -68.77357 1.000 34.57006 ?  90  VAL   A C   1 
ATOM   47   O  O   . VAL   A 1 13  ? -11.43578 7.43236   -68.01554 1.000 36.00215 ?  90  VAL   A O   1 
ATOM   48   C  CB  . VAL   A 1 13  ? -9.31392  4.86134   -68.28449 1.000 34.13554 ?  90  VAL   A CB  1 
ATOM   49   C  CG1 . VAL   A 1 13  ? -8.56640  6.05359   -67.69869 1.000 32.14894 ?  90  VAL   A CG1 1 
ATOM   50   C  CG2 . VAL   A 1 13  ? -8.97080  3.57971   -67.55464 1.000 32.92505 ?  90  VAL   A CG2 1 
ATOM   51   N  N   . ILE   A 1 14  ? -11.22275 6.60659   -70.10170 1.000 31.79798 ?  91  ILE   A N   1 
ATOM   52   C  CA  . ILE   A 1 14  ? -11.64864 7.84858   -70.73285 1.000 33.69467 ?  91  ILE   A CA  1 
ATOM   53   C  C   . ILE   A 1 14  ? -13.05596 8.21846   -70.29168 1.000 31.72913 ?  91  ILE   A C   1 
ATOM   54   O  O   . ILE   A 1 14  ? -13.32160 9.36632   -69.92489 1.000 32.97119 ?  91  ILE   A O   1 
ATOM   55   C  CB  . ILE   A 1 14  ? -11.55416 7.72614   -72.25988 1.000 32.29898 ?  91  ILE   A CB  1 
ATOM   56   C  CG1 . ILE   A 1 14  ? -10.09788 7.57272   -72.66800 1.000 35.56074 ?  91  ILE   A CG1 1 
ATOM   57   C  CG2 . ILE   A 1 14  ? -12.18329 8.93716   -72.91295 1.000 30.17918 ?  91  ILE   A CG2 1 
ATOM   58   C  CD1 . ILE   A 1 14  ? -9.91379  7.14138   -74.11360 1.000 38.26405 ?  91  ILE   A CD1 1 
ATOM   59   N  N   . LYS   A 1 15  ? -13.98486 7.25992   -70.33914 1.000 31.22788 ?  92  LYS   A N   1 
ATOM   60   C  CA  . LYS   A 1 15  ? -15.34528 7.55557   -69.90436 1.000 33.24099 ?  92  LYS   A CA  1 
ATOM   61   C  C   . LYS   A 1 15  ? -15.35125 8.14330   -68.50017 1.000 34.64684 ?  92  LYS   A C   1 
ATOM   62   O  O   . LYS   A 1 15  ? -16.17356 9.00951   -68.19295 1.000 33.82791 ?  92  LYS   A O   1 
ATOM   63   C  CB  . LYS   A 1 15  ? -16.22999 6.29466   -69.93836 1.000 34.00286 ?  92  LYS   A CB  1 
ATOM   64   C  CG  . LYS   A 1 15  ? -16.36517 5.57985   -71.30981 1.000 44.96932 ?  92  LYS   A CG  1 
ATOM   65   C  CD  . LYS   A 1 15  ? -17.46231 4.44627   -71.30631 1.000 45.16815 ?  92  LYS   A CD  1 
ATOM   66   C  CE  . LYS   A 1 15  ? -16.97524 3.07419   -71.85198 1.000 39.79988 ?  92  LYS   A CE  1 
ATOM   67   N  NZ  . LYS   A 1 15  ? -16.62284 3.05443   -73.31866 1.000 42.85381 ?  92  LYS   A NZ  1 
ATOM   68   N  N   . GLU   A 1 16  ? -14.43608 7.69740   -67.63978 1.000 32.30301 ?  93  GLU   A N   1 
ATOM   69   C  CA  . GLU   A 1 16  ? -14.44844 8.13718   -66.24981 1.000 35.23329 ?  93  GLU   A CA  1 
ATOM   70   C  C   . GLU   A 1 16  ? -13.86589 9.54055   -66.09850 1.000 34.53482 ?  93  GLU   A C   1 
ATOM   71   O  O   . GLU   A 1 16  ? -14.37172 10.34472  -65.30881 1.000 33.17632 ?  93  GLU   A O   1 
ATOM   72   C  CB  . GLU   A 1 16  ? -13.68490 7.12804   -65.38437 1.000 34.02976 ?  93  GLU   A CB  1 
ATOM   73   C  CG  . GLU   A 1 16  ? -13.65984 7.45644   -63.90373 1.000 40.92311 ?  93  GLU   A CG  1 
ATOM   74   C  CD  . GLU   A 1 16  ? -15.04109 7.39370   -63.25106 1.000 46.35077 ?  93  GLU   A CD  1 
ATOM   75   O  OE1 . GLU   A 1 16  ? -15.91949 6.66608   -63.78441 1.000 41.86951 ?  93  GLU   A OE1 1 
ATOM   76   O  OE2 . GLU   A 1 16  ? -15.23965 8.06977   -62.20429 1.000 49.94091 ?  93  GLU   A OE2 1 
ATOM   77   N  N   . LEU   A 1 17  ? -12.80069 9.84468   -66.83834 1.000 33.10533 ?  94  LEU   A N   1 
ATOM   78   C  CA  . LEU   A 1 17  ? -12.28116 11.20554  -66.86368 1.000 33.91840 ?  94  LEU   A CA  1 
ATOM   79   C  C   . LEU   A 1 17  ? -13.32198 12.17172  -67.39764 1.000 33.78427 ?  94  LEU   A C   1 
ATOM   80   O  O   . LEU   A 1 17  ? -13.51959 13.26378  -66.85308 1.000 37.11533 ?  94  LEU   A O   1 
ATOM   81   C  CB  . LEU   A 1 17  ? -11.03842 11.27690  -67.73526 1.000 33.63083 ?  94  LEU   A CB  1 
ATOM   82   C  CG  . LEU   A 1 17  ? -9.93378  10.28533  -67.48988 1.000 34.43435 ?  94  LEU   A CG  1 
ATOM   83   C  CD1 . LEU   A 1 17  ? -8.95641  10.50877  -68.62501 1.000 36.42858 ?  94  LEU   A CD1 1 
ATOM   84   C  CD2 . LEU   A 1 17  ? -9.29642  10.55772  -66.12743 1.000 36.55704 ?  94  LEU   A CD2 1 
ATOM   85   N  N   . ASN   A 1 18  ? -13.97718 11.80197  -68.49199 1.000 32.71328 ?  95  ASN   A N   1 
ATOM   86   C  CA  . ASN   A 1 18  ? -14.99376 12.68684  -69.03982 1.000 36.29664 ?  95  ASN   A CA  1 
ATOM   87   C  C   . ASN   A 1 18  ? -16.15656 12.87218  -68.06854 1.000 35.06088 ?  95  ASN   A C   1 
ATOM   88   O  O   . ASN   A 1 18  ? -16.73850 13.95522  -67.99283 1.000 37.09605 ?  95  ASN   A O   1 
ATOM   89   C  CB  . ASN   A 1 18  ? -15.48335 12.15758  -70.38101 1.000 33.45886 ?  95  ASN   A CB  1 
ATOM   90   C  CG  . ASN   A 1 18  ? -16.29027 13.18146  -71.12318 1.000 41.49224 ?  95  ASN   A CG  1 
ATOM   91   O  OD1 . ASN   A 1 18  ? -15.73151 14.11876  -71.69394 1.000 46.32417 ?  95  ASN   A OD1 1 
ATOM   92   N  ND2 . ASN   A 1 18  ? -17.61662 13.02715  -71.11456 1.000 38.01804 ?  95  ASN   A ND2 1 
ATOM   93   N  N   . LYS   A 1 19  ? -16.50464 11.84185  -67.30810 1.000 34.00454 ?  96  LYS   A N   1 
ATOM   94   C  CA  . LYS   A 1 19  ? -17.54585 12.01181  -66.30777 1.000 36.72306 ?  96  LYS   A CA  1 
ATOM   95   C  C   . LYS   A 1 19  ? -17.09778 13.00396  -65.24302 1.000 36.72765 ?  96  LYS   A C   1 
ATOM   96   O  O   . LYS   A 1 19  ? -17.82541 13.94141  -64.89751 1.000 36.61452 ?  96  LYS   A O   1 
ATOM   97   C  CB  . LYS   A 1 19  ? -17.89562 10.65875  -65.69234 1.000 34.92449 ?  96  LYS   A CB  1 
ATOM   98   C  CG  . LYS   A 1 19  ? -19.06793 10.69119  -64.73265 1.000 35.80319 ?  96  LYS   A CG  1 
ATOM   99   C  CD  . LYS   A 1 19  ? -18.91043 9.62131   -63.66597 1.000 37.29721 ?  96  LYS   A CD  1 
ATOM   100  C  CE  . LYS   A 1 19  ? -20.08312 9.62569   -62.69564 1.000 38.62128 ?  96  LYS   A CE  1 
ATOM   101  N  NZ  . LYS   A 1 19  ? -19.70291 9.07941   -61.36503 1.000 41.67132 ?  96  LYS   A NZ  1 
ATOM   102  N  N   . CYS   A 1 20  ? -15.87145 12.83844  -64.75314 1.000 34.34444 ?  97  CYS   A N   1 
ATOM   103  C  CA  . CYS   A 1 20  ? -15.38534 13.66396  -63.66274 1.000 31.08356 ?  97  CYS   A CA  1 
ATOM   104  C  C   . CYS   A 1 20  ? -15.24863 15.12892  -64.07845 1.000 36.55066 ?  97  CYS   A C   1 
ATOM   105  O  O   . CYS   A 1 20  ? -15.58770 16.03086  -63.30515 1.000 39.22849 ?  97  CYS   A O   1 
ATOM   106  C  CB  . CYS   A 1 20  ? -14.06717 13.08930  -63.16254 1.000 36.80771 ?  97  CYS   A CB  1 
ATOM   107  S  SG  . CYS   A 1 20  ? -13.17744 14.14963  -62.03826 1.000 45.62606 ?  97  CYS   A SG  1 
ATOM   108  N  N   . ARG   A 1 21  ? -14.78711 15.40815  -65.29548 1.000 37.42011 ?  98  ARG   A N   1 
ATOM   109  C  CA  . ARG   A 1 21  ? -14.70325 16.81287  -65.67959 1.000 34.63469 ?  98  ARG   A CA  1 
ATOM   110  C  C   . ARG   A 1 21  ? -16.08684 17.39166  -65.94433 1.000 34.88660 ?  98  ARG   A C   1 
ATOM   111  O  O   . ARG   A 1 21  ? -16.36904 18.54112  -65.57642 1.000 35.66269 ?  98  ARG   A O   1 
ATOM   112  C  CB  . ARG   A 1 21  ? -13.79162 16.99463  -66.88821 1.000 36.39393 ?  98  ARG   A CB  1 
ATOM   113  C  CG  . ARG   A 1 21  ? -14.32428 16.46605  -68.17428 1.000 41.30233 ?  98  ARG   A CG  1 
ATOM   114  C  CD  . ARG   A 1 21  ? -13.73407 17.22363  -69.34970 1.000 36.19827 ?  98  ARG   A CD  1 
ATOM   115  N  NE  . ARG   A 1 21  ? -14.75848 18.10305  -69.87883 1.000 40.92544 ?  98  ARG   A NE  1 
ATOM   116  C  CZ  . ARG   A 1 21  ? -15.73451 17.68802  -70.66957 1.000 39.50226 ?  98  ARG   A CZ  1 
ATOM   117  N  NH1 . ARG   A 1 21  ? -15.79313 16.43604  -71.08359 1.000 35.96061 ?  98  ARG   A NH1 1 
ATOM   118  N  NH2 . ARG   A 1 21  ? -16.67208 18.55266  -71.05645 1.000 40.09296 ?  98  ARG   A NH2 1 
ATOM   119  N  N   . GLU   A 1 22  ? -16.97181 16.60389  -66.55353 1.000 36.39032 ?  99  GLU   A N   1 
ATOM   120  C  CA  . GLU   A 1 22  ? -18.35678 17.03369  -66.72627 1.000 35.82527 ?  99  GLU   A CA  1 
ATOM   121  C  C   . GLU   A 1 22  ? -18.94519 17.51368  -65.40735 1.000 35.37720 ?  99  GLU   A C   1 
ATOM   122  O  O   . GLU   A 1 22  ? -19.48304 18.61977  -65.31950 1.000 35.39513 ?  99  GLU   A O   1 
ATOM   123  C  CB  . GLU   A 1 22  ? -19.19965 15.88699  -67.28515 1.000 35.32108 ?  99  GLU   A CB  1 
ATOM   124  C  CG  . GLU   A 1 22  ? -20.02232 16.23887  -68.48810 1.000 38.49379 ?  99  GLU   A CG  1 
ATOM   125  C  CD  . GLU   A 1 22  ? -19.25697 16.03750  -69.78897 1.000 48.52484 ?  99  GLU   A CD  1 
ATOM   126  O  OE1 . GLU   A 1 22  ? -18.98285 14.86550  -70.12420 1.000 46.28864 ?  99  GLU   A OE1 1 
ATOM   127  O  OE2 . GLU   A 1 22  ? -18.92412 17.04157  -70.47639 1.000 53.74405 ?  99  GLU   A OE2 1 
ATOM   128  N  N   . GLU   A 1 23  ? -18.85234 16.68411  -64.36842 1.000 32.79386 ?  100 GLU   A N   1 
ATOM   129  C  CA  . GLU   A 1 23  ? -19.46830 16.96686  -63.07971 1.000 37.49144 ?  100 GLU   A CA  1 
ATOM   130  C  C   . GLU   A 1 23  ? -18.66498 17.94776  -62.22983 1.000 38.09434 ?  100 GLU   A C   1 
ATOM   131  O  O   . GLU   A 1 23  ? -19.12288 18.31069  -61.13987 1.000 36.63230 ?  100 GLU   A O   1 
ATOM   132  C  CB  . GLU   A 1 23  ? -19.68950 15.64974  -62.32300 1.000 33.81296 ?  100 GLU   A CB  1 
ATOM   133  C  CG  . GLU   A 1 23  ? -20.42821 14.62586  -63.17703 1.000 38.48705 ?  100 GLU   A CG  1 
ATOM   134  C  CD  . GLU   A 1 23  ? -20.93010 13.41875  -62.39938 1.000 38.56922 ?  100 GLU   A CD  1 
ATOM   135  O  OE1 . GLU   A 1 23  ? -20.13226 12.82576  -61.65374 1.000 39.83266 ?  100 GLU   A OE1 1 
ATOM   136  O  OE2 . GLU   A 1 23  ? -22.12504 13.06499  -62.53909 1.000 36.34665 ?  100 GLU   A OE2 1 
ATOM   137  N  N   . ASN   A 1 24  ? -17.49875 18.39339  -62.70536 1.000 37.05008 ?  101 ASN   A N   1 
ATOM   138  C  CA  . ASN   A 1 24  ? -16.63462 19.31094  -61.96090 1.000 38.48397 ?  101 ASN   A CA  1 
ATOM   139  C  C   . ASN   A 1 24  ? -16.25238 18.72550  -60.60222 1.000 38.14352 ?  101 ASN   A C   1 
ATOM   140  O  O   . ASN   A 1 24  ? -16.06118 19.44912  -59.62092 1.000 39.82878 ?  101 ASN   A O   1 
ATOM   141  C  CB  . ASN   A 1 24  ? -17.28927 20.69380  -61.82127 1.000 37.77353 ?  101 ASN   A CB  1 
ATOM   142  C  CG  . ASN   A 1 24  ? -17.54499 21.35930  -63.19016 1.000 37.60507 ?  101 ASN   A CG  1 
ATOM   143  O  OD1 . ASN   A 1 24  ? -16.64038 21.45266  -64.01313 1.000 38.24060 ?  101 ASN   A OD1 1 
ATOM   144  N  ND2 . ASN   A 1 24  ? -18.78543 21.78127  -63.44021 1.000 32.56443 ?  101 ASN   A ND2 1 
ATOM   145  N  N   . SER   A 1 25  ? -16.12596 17.40439  -60.55695 1.000 34.50742 ?  102 SER   A N   1 
ATOM   146  C  CA  . SER   A 1 25  ? -15.76546 16.69519  -59.34285 1.000 34.47848 ?  102 SER   A CA  1 
ATOM   147  C  C   . SER   A 1 25  ? -14.33916 17.03465  -58.90697 1.000 39.87031 ?  102 SER   A C   1 
ATOM   148  O  O   . SER   A 1 25  ? -13.46112 17.31202  -59.72715 1.000 39.51067 ?  102 SER   A O   1 
ATOM   149  C  CB  . SER   A 1 25  ? -15.92228 15.19659  -59.57627 1.000 35.13501 ?  102 SER   A CB  1 
ATOM   150  O  OG  . SER   A 1 25  ? -14.91121 14.46572  -58.91138 1.000 46.26872 ?  102 SER   A OG  1 
ATOM   151  N  N   . MET   A 1 26  ? -14.11134 17.02246  -57.59175 1.000 38.92527 ?  103 MET   A N   1 
ATOM   152  C  CA  . MET   A 1 26  ? -12.80917 17.36237  -57.03635 1.000 35.02900 ?  103 MET   A CA  1 
ATOM   153  C  C   . MET   A 1 26  ? -11.98147 16.14321  -56.67756 1.000 37.40811 ?  103 MET   A C   1 
ATOM   154  O  O   . MET   A 1 26  ? -10.79987 16.28600  -56.33741 1.000 37.55456 ?  103 MET   A O   1 
ATOM   155  C  CB  . MET   A 1 26  ? -12.97314 18.23676  -55.79552 1.000 37.38617 ?  103 MET   A CB  1 
ATOM   156  C  CG  . MET   A 1 26  ? -13.79374 19.48310  -56.06171 1.000 50.37873 ?  103 MET   A CG  1 
ATOM   157  S  SD  . MET   A 1 26  ? -13.39091 20.92596  -55.04600 1.000 61.62006 ?  103 MET   A SD  1 
ATOM   158  C  CE  . MET   A 1 26  ? -14.09446 22.23990  -56.06664 1.000 46.77612 ?  103 MET   A CE  1 
ATOM   159  N  N   . ARG   A 1 27  ? -12.56888 14.95946  -56.73182 1.000 40.45840 ?  104 ARG   A N   1 
ATOM   160  C  CA  . ARG   A 1 27  ? -11.86861 13.72142  -56.44623 1.000 41.74195 ?  104 ARG   A CA  1 
ATOM   161  C  C   . ARG   A 1 27  ? -12.12484 12.77087  -57.60458 1.000 45.69034 ?  104 ARG   A C   1 
ATOM   162  O  O   . ARG   A 1 27  ? -13.27759 12.56764  -58.00226 1.000 47.57517 ?  104 ARG   A O   1 
ATOM   163  C  CB  . ARG   A 1 27  ? -12.33468 13.10757  -55.11619 1.000 41.37860 ?  104 ARG   A CB  1 
ATOM   164  C  CG  . ARG   A 1 27  ? -12.58734 11.61459  -55.20078 1.000 46.84931 ?  104 ARG   A CG  1 
ATOM   165  C  CD  . ARG   A 1 27  ? -13.25077 11.05002  -53.94095 1.000 52.53389 ?  104 ARG   A CD  1 
ATOM   166  N  NE  . ARG   A 1 27  ? -12.31457 10.90221  -52.83253 1.000 56.11997 ?  104 ARG   A NE  1 
ATOM   167  C  CZ  . ARG   A 1 27  ? -12.38885 11.56675  -51.68520 1.000 56.42211 ?  104 ARG   A CZ  1 
ATOM   168  N  NH1 . ARG   A 1 27  ? -13.37421 12.41654  -51.43935 1.000 51.72278 ?  104 ARG   A NH1 1 
ATOM   169  N  NH2 . ARG   A 1 27  ? -11.45443 11.36521  -50.75665 1.000 52.58241 ?  104 ARG   A NH2 1 
ATOM   170  N  N   . LEU   A 1 28  ? -11.05069 12.22912  -58.17085 1.000 39.55720 ?  105 LEU   A N   1 
ATOM   171  C  CA  . LEU   A 1 28  ? -11.12754 11.19012  -59.18609 1.000 33.45450 ?  105 LEU   A CA  1 
ATOM   172  C  C   . LEU   A 1 28  ? -10.46304 9.94475   -58.61993 1.000 37.39542 ?  105 LEU   A C   1 
ATOM   173  O  O   . LEU   A 1 28  ? -9.28245  9.97751   -58.25563 1.000 33.19745 ?  105 LEU   A O   1 
ATOM   174  C  CB  . LEU   A 1 28  ? -10.44610 11.63600  -60.47568 1.000 36.16574 ?  105 LEU   A CB  1 
ATOM   175  C  CG  . LEU   A 1 28  ? -10.20989 10.60096  -61.57382 1.000 33.26041 ?  105 LEU   A CG  1 
ATOM   176  C  CD1 . LEU   A 1 28  ? -11.50225 10.24123  -62.27713 1.000 35.18274 ?  105 LEU   A CD1 1 
ATOM   177  C  CD2 . LEU   A 1 28  ? -9.18306  11.12844  -62.56114 1.000 35.30117 ?  105 LEU   A CD2 1 
ATOM   178  N  N   . ASP   A 1 29  ? -11.22451 8.86112   -58.51542 1.000 36.83474 ?  106 ASP   A N   1 
ATOM   179  C  CA  . ASP   A 1 29  ? -10.70739 7.59139   -58.02642 1.000 37.95002 ?  106 ASP   A CA  1 
ATOM   180  C  C   . ASP   A 1 29  ? -10.67481 6.61090   -59.19211 1.000 34.68440 ?  106 ASP   A C   1 
ATOM   181  O  O   . ASP   A 1 29  ? -11.72583 6.17688   -59.66866 1.000 37.36891 ?  106 ASP   A O   1 
ATOM   182  C  CB  . ASP   A 1 29  ? -11.55535 7.05518   -56.87497 1.000 37.77238 ?  106 ASP   A CB  1 
ATOM   183  C  CG  . ASP   A 1 29  ? -10.94421 5.81261   -56.23058 1.000 39.04531 ?  106 ASP   A CG  1 
ATOM   184  O  OD1 . ASP   A 1 29  ? -10.18904 5.08867   -56.91271 1.000 35.47842 ?  106 ASP   A OD1 1 
ATOM   185  O  OD2 . ASP   A 1 29  ? -11.20787 5.56848   -55.02951 1.000 46.67971 ?  106 ASP   A OD2 1 
ATOM   186  N  N   . LEU   A 1 30  ? -9.46854  6.27296   -59.65400 1.000 36.66469 ?  107 LEU   A N   1 
ATOM   187  C  CA  . LEU   A 1 30  ? -9.26458  5.24697   -60.67354 1.000 37.09914 ?  107 LEU   A CA  1 
ATOM   188  C  C   . LEU   A 1 30  ? -8.42756  4.08983   -60.13206 1.000 33.53986 ?  107 LEU   A C   1 
ATOM   189  O  O   . LEU   A 1 30  ? -7.68808  3.45362   -60.87762 1.000 34.35135 ?  107 LEU   A O   1 
ATOM   190  C  CB  . LEU   A 1 30  ? -8.60009  5.82608   -61.92531 1.000 38.85189 ?  107 LEU   A CB  1 
ATOM   191  C  CG  . LEU   A 1 30  ? -9.21219  6.91310   -62.82011 1.000 34.68765 ?  107 LEU   A CG  1 
ATOM   192  C  CD1 . LEU   A 1 30  ? -8.13063  7.48579   -63.72450 1.000 34.25662 ?  107 LEU   A CD1 1 
ATOM   193  C  CD2 . LEU   A 1 30  ? -10.32374 6.37522   -63.66435 1.000 33.34544 ?  107 LEU   A CD2 1 
ATOM   194  N  N   . SER   A 1 31  ? -8.52311  3.81195   -58.83709 1.000 33.07662 ?  108 SER   A N   1 
ATOM   195  C  CA  . SER   A 1 31  ? -7.73091  2.74966   -58.23346 1.000 32.24886 ?  108 SER   A CA  1 
ATOM   196  C  C   . SER   A 1 31  ? -8.33327  1.37858   -58.52798 1.000 32.64395 ?  108 SER   A C   1 
ATOM   197  O  O   . SER   A 1 31  ? -9.51080  1.24530   -58.86759 1.000 35.15839 ?  108 SER   A O   1 
ATOM   198  C  CB  . SER   A 1 31  ? -7.63570  2.94623   -56.72524 1.000 33.37867 ?  108 SER   A CB  1 
ATOM   199  O  OG  . SER   A 1 31  ? -8.93873  3.02075   -56.17296 1.000 36.01139 ?  108 SER   A OG  1 
ATOM   200  N  N   . LYS   A 1 32  ? -7.49806  0.35024   -58.40410 1.000 30.37940 ?  109 LYS   A N   1 
ATOM   201  C  CA  . LYS   A 1 32  ? -7.96192  -1.03064  -58.41736 1.000 32.23817 ?  109 LYS   A CA  1 
ATOM   202  C  C   . LYS   A 1 32  ? -8.67436  -1.34266  -59.73092 1.000 37.10261 ?  109 LYS   A C   1 
ATOM   203  O  O   . LYS   A 1 32  ? -9.82068  -1.79917  -59.75347 1.000 40.98010 ?  109 LYS   A O   1 
ATOM   204  C  CB  . LYS   A 1 32  ? -8.85930  -1.30606  -57.20500 1.000 29.59283 ?  109 LYS   A CB  1 
ATOM   205  C  CG  . LYS   A 1 32  ? -8.16404  -0.99752  -55.87873 1.000 32.55236 ?  109 LYS   A CG  1 
ATOM   206  C  CD  . LYS   A 1 32  ? -8.99007  -1.41016  -54.65734 1.000 30.02281 ?  109 LYS   A CD  1 
ATOM   207  C  CE  . LYS   A 1 32  ? -10.32256 -0.68763  -54.62955 1.000 37.48952 ?  109 LYS   A CE  1 
ATOM   208  N  NZ  . LYS   A 1 32  ? -10.19328 0.77539   -54.35277 1.000 37.12384 ?  109 LYS   A NZ  1 
ATOM   209  N  N   . ARG   A 1 33  ? -7.96796  -1.08912  -60.83787 1.000 33.47190 ?  110 ARG   A N   1 
ATOM   210  C  CA  . ARG   A 1 33  ? -8.54539  -1.15750  -62.16719 1.000 32.81664 ?  110 ARG   A CA  1 
ATOM   211  C  C   . ARG   A 1 33  ? -7.60721  -1.74199  -63.20700 1.000 34.34769 ?  110 ARG   A C   1 
ATOM   212  O  O   . ARG   A 1 33  ? -8.00261  -1.84491  -64.37302 1.000 38.63566 ?  110 ARG   A O   1 
ATOM   213  C  CB  . ARG   A 1 33  ? -8.97141  0.23862   -62.63063 1.000 35.66249 ?  110 ARG   A CB  1 
ATOM   214  C  CG  . ARG   A 1 33  ? -10.35619 0.64817   -62.23400 1.000 36.60305 ?  110 ARG   A CG  1 
ATOM   215  C  CD  . ARG   A 1 33  ? -10.64739 2.01404   -62.81597 1.000 36.73323 ?  110 ARG   A CD  1 
ATOM   216  N  NE  . ARG   A 1 33  ? -11.79631 2.63571   -62.17563 1.000 37.52778 ?  110 ARG   A NE  1 
ATOM   217  C  CZ  . ARG   A 1 33  ? -12.92689 2.93237   -62.79790 1.000 42.80332 ?  110 ARG   A CZ  1 
ATOM   218  N  NH1 . ARG   A 1 33  ? -13.08555 2.70076   -64.09174 1.000 41.43255 ?  110 ARG   A NH1 1 
ATOM   219  N  NH2 . ARG   A 1 33  ? -13.92026 3.48503   -62.10817 1.000 44.19956 ?  110 ARG   A NH2 1 
ATOM   220  N  N   . SER   A 1 34  ? -6.37776  -2.09651  -62.84261 1.000 30.54093 ?  111 SER   A N   1 
ATOM   221  C  CA  . SER   A 1 34  ? -5.42444  -2.69110  -63.78400 1.000 37.80475 ?  111 SER   A CA  1 
ATOM   222  C  C   . SER   A 1 34  ? -5.12054  -1.77454  -64.96252 1.000 37.39113 ?  111 SER   A C   1 
ATOM   223  O  O   . SER   A 1 34  ? -4.90848  -2.24729  -66.08026 1.000 40.98322 ?  111 SER   A O   1 
ATOM   224  C  CB  . SER   A 1 34  ? -5.91723  -4.03553  -64.32135 1.000 40.01193 ?  111 SER   A CB  1 
ATOM   225  O  OG  . SER   A 1 34  ? -6.36846  -4.86966  -63.28103 1.000 45.99612 ?  111 SER   A OG  1 
ATOM   226  N  N   . ILE   A 1 35  ? -5.10564  -0.46209  -64.74399 1.000 36.01859 ?  112 ILE   A N   1 
ATOM   227  C  CA  . ILE   A 1 35  ? -4.78039  0.46238   -65.82216 1.000 32.54918 ?  112 ILE   A CA  1 
ATOM   228  C  C   . ILE   A 1 35  ? -3.28975  0.37843   -66.10775 1.000 33.57336 ?  112 ILE   A C   1 
ATOM   229  O  O   . ILE   A 1 35  ? -2.47054  0.36465   -65.18091 1.000 35.42907 ?  112 ILE   A O   1 
ATOM   230  C  CB  . ILE   A 1 35  ? -5.19534  1.89116   -65.44728 1.000 32.38885 ?  112 ILE   A CB  1 
ATOM   231  C  CG1 . ILE   A 1 35  ? -6.71016  1.97213   -65.25994 1.000 32.91685 ?  112 ILE   A CG1 1 
ATOM   232  C  CG2 . ILE   A 1 35  ? -4.69008  2.89475   -66.47851 1.000 30.44993 ?  112 ILE   A CG2 1 
ATOM   233  C  CD1 . ILE   A 1 35  ? -7.15829  3.31697   -64.71612 1.000 35.36354 ?  112 ILE   A CD1 1 
ATOM   234  N  N   . HIS   A 1 36  ? -2.93272  0.29858   -67.39465 1.000 33.22869 ?  113 HIS   A N   1 
ATOM   235  C  CA  . HIS   A 1 36  ? -1.54167  0.27316   -67.83604 1.000 32.81256 ?  113 HIS   A CA  1 
ATOM   236  C  C   . HIS   A 1 36  ? -1.02671  1.65374   -68.22826 1.000 37.04444 ?  113 HIS   A C   1 
ATOM   237  O  O   . HIS   A 1 36  ? 0.16709   1.94072   -68.05992 1.000 35.62926 ?  113 HIS   A O   1 
ATOM   238  C  CB  . HIS   A 1 36  ? -1.37214  -0.67472  -69.03707 1.000 34.96833 ?  113 HIS   A CB  1 
ATOM   239  C  CG  . HIS   A 1 36  ? -1.17709  -2.11724  -68.66971 1.000 32.27537 ?  113 HIS   A CG  1 
ATOM   240  N  ND1 . HIS   A 1 36  ? -2.20248  -3.04050  -68.69814 1.000 32.37604 ?  113 HIS   A ND1 1 
ATOM   241  C  CD2 . HIS   A 1 36  ? -0.06913  -2.79814  -68.29049 1.000 33.26294 ?  113 HIS   A CD2 1 
ATOM   242  C  CE1 . HIS   A 1 36  ? -1.73898  -4.22349  -68.33664 1.000 34.33243 ?  113 HIS   A CE1 1 
ATOM   243  N  NE2 . HIS   A 1 36  ? -0.44772  -4.10403  -68.08215 1.000 37.31318 ?  113 HIS   A NE2 1 
ATOM   244  N  N   . ILE   A 1 37  ? -1.88685  2.51070   -68.76937 1.000 34.91743 ?  114 ILE   A N   1 
ATOM   245  C  CA  . ILE   A 1 37  ? -1.48359  3.84872   -69.16600 1.000 35.23784 ?  114 ILE   A CA  1 
ATOM   246  C  C   . ILE   A 1 37  ? -2.62837  4.79775   -68.85201 1.000 38.95622 ?  114 ILE   A C   1 
ATOM   247  O  O   . ILE   A 1 37  ? -3.80642  4.44612   -68.97210 1.000 40.29790 ?  114 ILE   A O   1 
ATOM   248  C  CB  . ILE   A 1 37  ? -1.06543  3.90818   -70.65510 1.000 37.74584 ?  114 ILE   A CB  1 
ATOM   249  C  CG1 . ILE   A 1 37  ? -0.50758  5.28497   -70.99406 1.000 42.23985 ?  114 ILE   A CG1 1 
ATOM   250  C  CG2 . ILE   A 1 37  ? -2.22186  3.56036   -71.59279 1.000 34.04610 ?  114 ILE   A CG2 1 
ATOM   251  C  CD1 . ILE   A 1 37  ? -0.05264  5.40547   -72.44925 1.000 44.00143 ?  114 ILE   A CD1 1 
ATOM   252  N  N   . LEU   A 1 38  ? -2.27877  5.98412   -68.39275 1.000 39.00186 ?  115 LEU   A N   1 
ATOM   253  C  CA  . LEU   A 1 38  ? -3.26119  6.99905   -68.08584 1.000 38.81152 ?  115 LEU   A CA  1 
ATOM   254  C  C   . LEU   A 1 38  ? -3.33822  7.94271   -69.27412 1.000 39.53275 ?  115 LEU   A C   1 
ATOM   255  O  O   . LEU   A 1 38  ? -2.31131  8.53971   -69.62867 1.000 41.59779 ?  115 LEU   A O   1 
ATOM   256  C  CB  . LEU   A 1 38  ? -2.84851  7.74587   -66.82352 1.000 38.06881 ?  115 LEU   A CB  1 
ATOM   257  C  CG  . LEU   A 1 38  ? -3.81885  8.74224   -66.21712 1.000 38.62187 ?  115 LEU   A CG  1 
ATOM   258  C  CD1 . LEU   A 1 38  ? -5.07733  8.02861   -65.73263 1.000 37.92466 ?  115 LEU   A CD1 1 
ATOM   259  C  CD2 . LEU   A 1 38  ? -3.12000  9.46419   -65.08605 1.000 38.18739 ?  115 LEU   A CD2 1 
ATOM   260  N  N   . PRO   A 1 39  ? -4.47840  8.08027   -69.94992 1.000 40.27432 ?  116 PRO   A N   1 
ATOM   261  C  CA  . PRO   A 1 39  ? -4.50708  8.90242   -71.16751 1.000 40.11957 ?  116 PRO   A CA  1 
ATOM   262  C  C   . PRO   A 1 39  ? -4.17119  10.35974  -70.88427 1.000 39.64738 ?  116 PRO   A C   1 
ATOM   263  O  O   . PRO   A 1 39  ? -4.38384  10.87283  -69.78081 1.000 36.58010 ?  116 PRO   A O   1 
ATOM   264  C  CB  . PRO   A 1 39  ? -5.94745  8.75180   -71.66952 1.000 39.17293 ?  116 PRO   A CB  1 
ATOM   265  C  CG  . PRO   A 1 39  ? -6.71330  8.30419   -70.47687 1.000 39.47850 ?  116 PRO   A CG  1 
ATOM   266  C  CD  . PRO   A 1 39  ? -5.77524  7.43961   -69.69387 1.000 36.02877 ?  116 PRO   A CD  1 
ATOM   267  N  N   . SER   A 1 40  ? -3.64271  11.02662  -71.91781 1.000 40.90669 ?  117 SER   A N   1 
ATOM   268  C  CA  . SER   A 1 40  ? -3.31335  12.44797  -71.82045 1.000 41.08316 ?  117 SER   A CA  1 
ATOM   269  C  C   . SER   A 1 40  ? -4.51291  13.29925  -71.42989 1.000 35.95013 ?  117 SER   A C   1 
ATOM   270  O  O   . SER   A 1 40  ? -4.34043  14.34092  -70.79331 1.000 38.03691 ?  117 SER   A O   1 
ATOM   271  C  CB  . SER   A 1 40  ? -2.74006  12.95312  -73.14647 1.000 38.97802 ?  117 SER   A CB  1 
ATOM   272  O  OG  . SER   A 1 40  ? -1.35232  12.69967  -73.20629 1.000 45.92239 ?  117 SER   A OG  1 
ATOM   273  N  N   . SER   A 1 41  ? -5.72679  12.88350  -71.79698 1.000 36.76771 ?  118 SER   A N   1 
ATOM   274  C  CA  . SER   A 1 41  ? -6.90807  13.71636  -71.59074 1.000 36.49419 ?  118 SER   A CA  1 
ATOM   275  C  C   . SER   A 1 41  ? -7.12114  14.10622  -70.13724 1.000 35.70879 ?  118 SER   A C   1 
ATOM   276  O  O   . SER   A 1 41  ? -7.94097  14.98749  -69.87435 1.000 36.17127 ?  118 SER   A O   1 
ATOM   277  C  CB  . SER   A 1 41  ? -8.15130  12.99907  -72.09942 1.000 37.04796 ?  118 SER   A CB  1 
ATOM   278  O  OG  . SER   A 1 41  ? -7.80705  12.14687  -73.17635 1.000 51.11839 ?  118 SER   A OG  1 
ATOM   279  N  N   . ILE   A 1 42  ? -6.42715  13.47589  -69.18863 1.000 35.45539 ?  119 ILE   A N   1 
ATOM   280  C  CA  . ILE   A 1 42  ? -6.56769  13.86187  -67.78971 1.000 36.93075 ?  119 ILE   A CA  1 
ATOM   281  C  C   . ILE   A 1 42  ? -6.12163  15.29329  -67.53801 1.000 33.47767 ?  119 ILE   A C   1 
ATOM   282  O  O   . ILE   A 1 42  ? -6.38844  15.83786  -66.46926 1.000 31.08411 ?  119 ILE   A O   1 
ATOM   283  C  CB  . ILE   A 1 42  ? -5.77472  12.90954  -66.86174 1.000 37.49601 ?  119 ILE   A CB  1 
ATOM   284  C  CG1 . ILE   A 1 42  ? -6.32574  13.00178  -65.42768 1.000 37.05588 ?  119 ILE   A CG1 1 
ATOM   285  C  CG2 . ILE   A 1 42  ? -4.28108  13.22602  -66.92932 1.000 33.27398 ?  119 ILE   A CG2 1 
ATOM   286  C  CD1 . ILE   A 1 42  ? -5.32123  12.68240  -64.35334 1.000 35.24316 ?  119 ILE   A CD1 1 
ATOM   287  N  N   . LYS   A 1 43  ? -5.42443  15.91121  -68.48969 1.000 35.99426 ?  120 LYS   A N   1 
ATOM   288  C  CA  . LYS   A 1 43  ? -4.98157  17.27878  -68.27740 1.000 36.73349 ?  120 LYS   A CA  1 
ATOM   289  C  C   . LYS   A 1 43  ? -6.15249  18.24578  -68.18753 1.000 36.78616 ?  120 LYS   A C   1 
ATOM   290  O  O   . LYS   A 1 43  ? -5.98504  19.33403  -67.62812 1.000 35.56651 ?  120 LYS   A O   1 
ATOM   291  C  CB  . LYS   A 1 43  ? -4.01228  17.71814  -69.38502 1.000 37.71688 ?  120 LYS   A CB  1 
ATOM   292  C  CG  . LYS   A 1 43  ? -4.63472  18.06855  -70.73070 1.000 37.02132 ?  120 LYS   A CG  1 
ATOM   293  C  CD  . LYS   A 1 43  ? -3.69026  19.01449  -71.49233 1.000 46.95050 ?  120 LYS   A CD  1 
ATOM   294  C  CE  . LYS   A 1 43  ? -3.48368  20.33691  -70.69851 1.000 50.10093 ?  120 LYS   A CE  1 
ATOM   295  N  NZ  . LYS   A 1 43  ? -2.29031  21.17671  -71.06258 1.000 44.43468 ?  120 LYS   A NZ  1 
ATOM   296  N  N   . GLU   A 1 44  ? -7.33416  17.87068  -68.70582 1.000 33.25855 ?  121 GLU   A N   1 
ATOM   297  C  CA  . GLU   A 1 44  ? -8.51041  18.73981  -68.62385 1.000 34.50000 ?  121 GLU   A CA  1 
ATOM   298  C  C   . GLU   A 1 44  ? -9.08303  18.86359  -67.21089 1.000 37.12447 ?  121 GLU   A C   1 
ATOM   299  O  O   . GLU   A 1 44  ? -9.83695  19.80740  -66.95024 1.000 38.38966 ?  121 GLU   A O   1 
ATOM   300  C  CB  . GLU   A 1 44  ? -9.61796  18.22887  -69.54119 1.000 33.73934 ?  121 GLU   A CB  1 
ATOM   301  C  CG  . GLU   A 1 44  ? -9.32929  18.36642  -71.00862 1.000 34.85617 ?  121 GLU   A CG  1 
ATOM   302  C  CD  . GLU   A 1 44  ? -10.50423 17.94190  -71.85252 1.000 33.93717 ?  121 GLU   A CD  1 
ATOM   303  O  OE1 . GLU   A 1 44  ? -10.88694 16.76901  -71.77783 1.000 39.12506 ?  121 GLU   A OE1 1 
ATOM   304  O  OE2 . GLU   A 1 44  ? -11.06982 18.78330  -72.57827 1.000 38.33386 ?  121 GLU   A OE2 1 
ATOM   305  N  N   . LEU   A 1 45  ? -8.76651  17.92982  -66.30849 1.000 32.25132 ?  122 LEU   A N   1 
ATOM   306  C  CA  . LEU   A 1 45  ? -9.40220  17.84655  -64.99834 1.000 34.89054 ?  122 LEU   A CA  1 
ATOM   307  C  C   . LEU   A 1 45  ? -8.74107  18.76497  -63.97362 1.000 34.86370 ?  122 LEU   A C   1 
ATOM   308  O  O   . LEU   A 1 45  ? -8.36191  18.33083  -62.88054 1.000 34.27808 ?  122 LEU   A O   1 
ATOM   309  C  CB  . LEU   A 1 45  ? -9.38323  16.39314  -64.51055 1.000 33.84406 ?  122 LEU   A CB  1 
ATOM   310  C  CG  . LEU   A 1 45  ? -10.55474 15.49299  -64.92524 1.000 35.48048 ?  122 LEU   A CG  1 
ATOM   311  C  CD1 . LEU   A 1 45  ? -10.81678 15.56004  -66.41273 1.000 37.97268 ?  122 LEU   A CD1 1 
ATOM   312  C  CD2 . LEU   A 1 45  ? -10.27353 14.06531  -64.52606 1.000 36.50370 ?  122 LEU   A CD2 1 
ATOM   313  N  N   . THR   A 1 46  ? -8.61605  20.04327  -64.31630 1.000 35.39852 ?  123 THR   A N   1 
ATOM   314  C  CA  . THR   A 1 46  ? -7.94659  21.01491  -63.46185 1.000 35.94944 ?  123 THR   A CA  1 
ATOM   315  C  C   . THR   A 1 46  ? -8.70362  21.32089  -62.17141 1.000 32.37927 ?  123 THR   A C   1 
ATOM   316  O  O   . THR   A 1 46  ? -8.11895  21.93460  -61.27682 1.000 32.64980 ?  123 THR   A O   1 
ATOM   317  C  CB  . THR   A 1 46  ? -7.72227  22.31137  -64.24664 1.000 35.65791 ?  123 THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 46  ? -8.97634  22.74673  -64.79208 1.000 34.17301 ?  123 THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 46  ? -6.70148  22.09257  -65.37677 1.000 28.62186 ?  123 THR   A CG2 1 
ATOM   320  N  N   . GLN   A 1 47  ? -9.97911  20.94498  -62.05554 1.000 33.37613 ?  124 GLN   A N   1 
ATOM   321  C  CA  . GLN   A 1 47  ? -10.70114 21.09992  -60.79547 1.000 34.15946 ?  124 GLN   A CA  1 
ATOM   322  C  C   . GLN   A 1 47  ? -10.29817 20.06416  -59.74738 1.000 34.65153 ?  124 GLN   A C   1 
ATOM   323  O  O   . GLN   A 1 47  ? -10.80714 20.12417  -58.62255 1.000 36.92534 ?  124 GLN   A O   1 
ATOM   324  C  CB  . GLN   A 1 47  ? -12.21554 20.99102  -61.00964 1.000 34.88103 ?  124 GLN   A CB  1 
ATOM   325  C  CG  . GLN   A 1 47  ? -12.81281 21.95497  -61.98032 1.000 38.19325 ?  124 GLN   A CG  1 
ATOM   326  C  CD  . GLN   A 1 47  ? -12.69126 23.39562  -61.51827 1.000 41.66389 ?  124 GLN   A CD  1 
ATOM   327  O  OE1 . GLN   A 1 47  ? -11.95069 24.18213  -62.11343 1.000 37.10788 ?  124 GLN   A OE1 1 
ATOM   328  N  NE2 . GLN   A 1 47  ? -13.41871 23.74984  -60.45492 1.000 41.67285 ?  124 GLN   A NE2 1 
ATOM   329  N  N   . LEU   A 1 48  ? -9.41814  19.11944  -60.08196 1.000 33.31929 ?  125 LEU   A N   1 
ATOM   330  C  CA  . LEU   A 1 48  ? -9.11640  18.01590  -59.17794 1.000 32.82815 ?  125 LEU   A CA  1 
ATOM   331  C  C   . LEU   A 1 48  ? -8.26828  18.48099  -58.00220 1.000 33.12100 ?  125 LEU   A C   1 
ATOM   332  O  O   . LEU   A 1 48  ? -7.24777  19.15097  -58.18509 1.000 29.86049 ?  125 LEU   A O   1 
ATOM   333  C  CB  . LEU   A 1 48  ? -8.39170  16.90601  -59.92745 1.000 27.25102 ?  125 LEU   A CB  1 
ATOM   334  C  CG  . LEU   A 1 48  ? -9.29420  15.96376  -60.71067 1.000 34.41699 ?  125 LEU   A CG  1 
ATOM   335  C  CD1 . LEU   A 1 48  ? -8.46924  14.94581  -61.51980 1.000 33.33145 ?  125 LEU   A CD1 1 
ATOM   336  C  CD2 . LEU   A 1 48  ? -10.24963 15.26174  -59.75607 1.000 32.53635 ?  125 LEU   A CD2 1 
ATOM   337  N  N   . THR   A 1 49  ? -8.68791  18.11441  -56.78942 1.000 33.42564 ?  126 THR   A N   1 
ATOM   338  C  CA  . THR   A 1 49  ? -7.83918  18.25732  -55.61281 1.000 35.16165 ?  126 THR   A CA  1 
ATOM   339  C  C   . THR   A 1 49  ? -7.38617  16.91749  -55.06807 1.000 32.90371 ?  126 THR   A C   1 
ATOM   340  O  O   . THR   A 1 49  ? -6.50606  16.88085  -54.20478 1.000 31.86934 ?  126 THR   A O   1 
ATOM   341  C  CB  . THR   A 1 49  ? -8.54279  19.04598  -54.48903 1.000 34.96251 ?  126 THR   A CB  1 
ATOM   342  O  OG1 . THR   A 1 49  ? -9.72506  18.35987  -54.07310 1.000 36.22117 ?  126 THR   A OG1 1 
ATOM   343  C  CG2 . THR   A 1 49  ? -8.91233  20.43030  -54.95751 1.000 31.30941 ?  126 THR   A CG2 1 
ATOM   344  N  N   . GLU   A 1 50  ? -7.93858  15.81948  -55.56355 1.000 34.47933 ?  127 GLU   A N   1 
ATOM   345  C  CA  . GLU   A 1 50  ? -7.49815  14.50816  -55.12005 1.000 33.24678 ?  127 GLU   A CA  1 
ATOM   346  C  C   . GLU   A 1 50  ? -7.57233  13.54826  -56.29174 1.000 35.61803 ?  127 GLU   A C   1 
ATOM   347  O  O   . GLU   A 1 50  ? -8.60184  13.45629  -56.96721 1.000 35.78761 ?  127 GLU   A O   1 
ATOM   348  C  CB  . GLU   A 1 50  ? -8.34200  14.01859  -53.94468 1.000 34.32267 ?  127 GLU   A CB  1 
ATOM   349  C  CG  . GLU   A 1 50  ? -8.25626  14.97277  -52.76561 1.000 35.33484 ?  127 GLU   A CG  1 
ATOM   350  C  CD  . GLU   A 1 50  ? -9.29520  14.72218  -51.72786 1.000 38.36000 ?  127 GLU   A CD  1 
ATOM   351  O  OE1 . GLU   A 1 50  ? -9.60861  13.55517  -51.47029 1.000 40.09077 ?  127 GLU   A OE1 1 
ATOM   352  O  OE2 . GLU   A 1 50  ? -9.81136  15.71035  -51.16759 1.000 55.00762 ?  127 GLU   A OE2 1 
ATOM   353  N  N   . LEU   A 1 51  ? -6.46559  12.85117  -56.52423 1.000 36.12786 ?  128 LEU   A N   1 
ATOM   354  C  CA  . LEU   A 1 51  ? -6.33993  11.86419  -57.58450 1.000 34.23447 ?  128 LEU   A CA  1 
ATOM   355  C  C   . LEU   A 1 51  ? -5.82641  10.58629  -56.95307 1.000 32.15756 ?  128 LEU   A C   1 
ATOM   356  O  O   . LEU   A 1 51  ? -4.71316  10.56755  -56.41833 1.000 31.67903 ?  128 LEU   A O   1 
ATOM   357  C  CB  . LEU   A 1 51  ? -5.37936  12.34900  -58.66933 1.000 31.40733 ?  128 LEU   A CB  1 
ATOM   358  C  CG  . LEU   A 1 51  ? -5.20553  11.46348  -59.88468 1.000 31.21613 ?  128 LEU   A CG  1 
ATOM   359  C  CD1 . LEU   A 1 51  ? -6.54073  11.25207  -60.59022 1.000 32.52999 ?  128 LEU   A CD1 1 
ATOM   360  C  CD2 . LEU   A 1 51  ? -4.18237  12.11114  -60.80422 1.000 29.09117 ?  128 LEU   A CD2 1 
ATOM   361  N  N   . TYR   A 1 52  ? -6.64130  9.53498   -56.99389 1.000 34.15641 ?  129 TYR   A N   1 
ATOM   362  C  CA  . TYR   A 1 52  ? -6.26203  8.21581   -56.51177 1.000 30.75843 ?  129 TYR   A CA  1 
ATOM   363  C  C   . TYR   A 1 52  ? -6.03507  7.32236   -57.71527 1.000 31.28708 ?  129 TYR   A C   1 
ATOM   364  O  O   . TYR   A 1 52  ? -6.95227  7.12116   -58.51373 1.000 34.18062 ?  129 TYR   A O   1 
ATOM   365  C  CB  . TYR   A 1 52  ? -7.33966  7.63781   -55.60069 1.000 33.43821 ?  129 TYR   A CB  1 
ATOM   366  C  CG  . TYR   A 1 52  ? -7.61971  8.52777   -54.42160 1.000 37.08968 ?  129 TYR   A CG  1 
ATOM   367  C  CD1 . TYR   A 1 52  ? -6.88815  8.41557   -53.24173 1.000 35.98368 ?  129 TYR   A CD1 1 
ATOM   368  C  CD2 . TYR   A 1 52  ? -8.59295  9.50090   -54.49482 1.000 36.71982 ?  129 TYR   A CD2 1 
ATOM   369  C  CE1 . TYR   A 1 52  ? -7.14112  9.24181   -52.17005 1.000 33.76481 ?  129 TYR   A CE1 1 
ATOM   370  C  CE2 . TYR   A 1 52  ? -8.84613  10.33315  -53.43512 1.000 39.83725 ?  129 TYR   A CE2 1 
ATOM   371  C  CZ  . TYR   A 1 52  ? -8.12134  10.20512  -52.27920 1.000 40.16050 ?  129 TYR   A CZ  1 
ATOM   372  O  OH  . TYR   A 1 52  ? -8.40355  11.05211  -51.23562 1.000 43.22859 ?  129 TYR   A OH  1 
ATOM   373  N  N   . LEU   A 1 53  ? -4.80715  6.80356   -57.84461 1.000 33.22794 ?  130 LEU   A N   1 
ATOM   374  C  CA  . LEU   A 1 53  ? -4.39999  5.90530   -58.92375 1.000 33.02971 ?  130 LEU   A CA  1 
ATOM   375  C  C   . LEU   A 1 53  ? -3.73530  4.64397   -58.37406 1.000 30.62529 ?  130 LEU   A C   1 
ATOM   376  O  O   . LEU   A 1 53  ? -2.98540  3.97527   -59.08983 1.000 28.72971 ?  130 LEU   A O   1 
ATOM   377  C  CB  . LEU   A 1 53  ? -3.45242  6.62798   -59.89337 1.000 29.12467 ?  130 LEU   A CB  1 
ATOM   378  C  CG  . LEU   A 1 53  ? -4.06703  7.84430   -60.58899 1.000 30.45124 ?  130 LEU   A CG  1 
ATOM   379  C  CD1 . LEU   A 1 53  ? -3.04122  8.71054   -61.29582 1.000 31.18579 ?  130 LEU   A CD1 1 
ATOM   380  C  CD2 . LEU   A 1 53  ? -5.09696  7.35796   -61.57885 1.000 35.72304 ?  130 LEU   A CD2 1 
ATOM   381  N  N   . TYR   A 1 54  ? -3.98334  4.31330   -57.11427 1.000 29.34537 ?  131 TYR   A N   1 
ATOM   382  C  CA  . TYR   A 1 54  ? -3.28937  3.20942   -56.48178 1.000 29.82794 ?  131 TYR   A CA  1 
ATOM   383  C  C   . TYR   A 1 54  ? -3.83346  1.86926   -56.97721 1.000 29.69832 ?  131 TYR   A C   1 
ATOM   384  O  O   . TYR   A 1 54  ? -4.97070  1.76739   -57.43913 1.000 27.51143 ?  131 TYR   A O   1 
ATOM   385  C  CB  . TYR   A 1 54  ? -3.40648  3.31788   -54.95993 1.000 30.88746 ?  131 TYR   A CB  1 
ATOM   386  C  CG  . TYR   A 1 54  ? -4.80429  3.14024   -54.38094 1.000 33.18353 ?  131 TYR   A CG  1 
ATOM   387  C  CD1 . TYR   A 1 54  ? -5.40114  1.88245   -54.30338 1.000 34.04726 ?  131 TYR   A CD1 1 
ATOM   388  C  CD2 . TYR   A 1 54  ? -5.50143  4.21869   -53.86072 1.000 32.32664 ?  131 TYR   A CD2 1 
ATOM   389  C  CE1 . TYR   A 1 54  ? -6.66440  1.72244   -53.75689 1.000 34.04927 ?  131 TYR   A CE1 1 
ATOM   390  C  CE2 . TYR   A 1 54  ? -6.75582  4.06400   -53.31290 1.000 31.32913 ?  131 TYR   A CE2 1 
ATOM   391  C  CZ  . TYR   A 1 54  ? -7.33148  2.81859   -53.26746 1.000 35.01524 ?  131 TYR   A CZ  1 
ATOM   392  O  OH  . TYR   A 1 54  ? -8.58380  2.67242   -52.72674 1.000 40.34046 ?  131 TYR   A OH  1 
ATOM   393  N  N   . SER   A 1 55  ? -2.99435  0.83398   -56.86454 1.000 30.62029 ?  132 SER   A N   1 
ATOM   394  C  CA  . SER   A 1 55  ? -3.29834  -0.53661  -57.29763 1.000 33.38858 ?  132 SER   A CA  1 
ATOM   395  C  C   . SER   A 1 55  ? -3.70405  -0.57194  -58.77463 1.000 29.43691 ?  132 SER   A C   1 
ATOM   396  O  O   . SER   A 1 55  ? -4.84844  -0.82881  -59.14668 1.000 29.68013 ?  132 SER   A O   1 
ATOM   397  C  CB  . SER   A 1 55  ? -4.38222  -1.17454  -56.42363 1.000 31.71399 ?  132 SER   A CB  1 
ATOM   398  O  OG  . SER   A 1 55  ? -3.98454  -1.11679  -55.07320 1.000 39.31095 ?  132 SER   A OG  1 
ATOM   399  N  N   . ASN   A 1 56  ? -2.71580  -0.28953  -59.60942 1.000 30.49397 ?  133 ASN   A N   1 
ATOM   400  C  CA  . ASN   A 1 56  ? -2.86762  -0.37821  -61.05569 1.000 29.12649 ?  133 ASN   A CA  1 
ATOM   401  C  C   . ASN   A 1 56  ? -1.58361  -1.00624  -61.58349 1.000 30.72498 ?  133 ASN   A C   1 
ATOM   402  O  O   . ASN   A 1 56  ? -0.79734  -1.58565  -60.82634 1.000 30.36019 ?  133 ASN   A O   1 
ATOM   403  C  CB  . ASN   A 1 56  ? -3.18636  1.00452   -61.65332 1.000 30.45534 ?  133 ASN   A CB  1 
ATOM   404  C  CG  . ASN   A 1 56  ? -4.66192  1.34468   -61.56894 1.000 32.67997 ?  133 ASN   A CG  1 
ATOM   405  O  OD1 . ASN   A 1 56  ? -5.51418  0.59090   -62.05392 1.000 32.90169 ?  133 ASN   A OD1 1 
ATOM   406  N  ND2 . ASN   A 1 56  ? -4.97876  2.46582   -60.91649 1.000 29.91796 ?  133 ASN   A ND2 1 
ATOM   407  N  N   . LYS   A 1 57  ? -1.35162  -0.88896  -62.88560 1.000 33.15809 ?  134 LYS   A N   1 
ATOM   408  C  CA  . LYS   A 1 57  ? -0.15543  -1.42804  -63.51872 1.000 31.74597 ?  134 LYS   A CA  1 
ATOM   409  C  C   . LYS   A 1 57  ? 0.65556   -0.31122  -64.16024 1.000 32.59437 ?  134 LYS   A C   1 
ATOM   410  O  O   . LYS   A 1 57  ? 1.29663   -0.50199  -65.19915 1.000 31.57218 ?  134 LYS   A O   1 
ATOM   411  C  CB  . LYS   A 1 57  ? -0.52928  -2.50029  -64.54035 1.000 31.77588 ?  134 LYS   A CB  1 
ATOM   412  C  CG  . LYS   A 1 57  ? -1.22506  -3.68599  -63.89675 1.000 32.83208 ?  134 LYS   A CG  1 
ATOM   413  C  CD  . LYS   A 1 57  ? -1.55933  -4.73843  -64.90364 1.000 37.76862 ?  134 LYS   A CD  1 
ATOM   414  C  CE  . LYS   A 1 57  ? -2.29919  -5.89861  -64.25643 1.000 39.98526 ?  134 LYS   A CE  1 
ATOM   415  N  NZ  . LYS   A 1 57  ? -1.51185  -6.47976  -63.13987 1.000 43.87837 ?  134 LYS   A NZ  1 
ATOM   416  N  N   . LEU   A 1 58  ? 0.62329   0.86441   -63.54565 1.000 29.82921 ?  135 LEU   A N   1 
ATOM   417  C  CA  . LEU   A 1 58  ? 1.26811   2.02719   -64.13616 1.000 31.96266 ?  135 LEU   A CA  1 
ATOM   418  C  C   . LEU   A 1 58  ? 2.77750   1.89660   -64.00366 1.000 29.89554 ?  135 LEU   A C   1 
ATOM   419  O  O   . LEU   A 1 58  ? 3.30348   1.63157   -62.91908 1.000 29.08975 ?  135 LEU   A O   1 
ATOM   420  C  CB  . LEU   A 1 58  ? 0.77434   3.31659   -63.46923 1.000 29.45981 ?  135 LEU   A CB  1 
ATOM   421  C  CG  . LEU   A 1 58  ? -0.70840  3.68287   -63.58885 1.000 27.35385 ?  135 LEU   A CG  1 
ATOM   422  C  CD1 . LEU   A 1 58  ? -1.00850  4.93728   -62.76702 1.000 28.03413 ?  135 LEU   A CD1 1 
ATOM   423  C  CD2 . LEU   A 1 58  ? -1.13199  3.86484   -65.05554 1.000 29.20978 ?  135 LEU   A CD2 1 
ATOM   424  N  N   . GLN   A 1 59  ? 3.47258   2.05899   -65.11494 1.000 29.63282 ?  136 GLN   A N   1 
ATOM   425  C  CA  . GLN   A 1 59  ? 4.92154   2.10994   -65.10218 1.000 31.48489 ?  136 GLN   A CA  1 
ATOM   426  C  C   . GLN   A 1 59  ? 5.44369   3.50023   -65.40880 1.000 34.23379 ?  136 GLN   A C   1 
ATOM   427  O  O   . GLN   A 1 59  ? 6.66260   3.70462   -65.41059 1.000 33.47419 ?  136 GLN   A O   1 
ATOM   428  C  CB  . GLN   A 1 59  ? 5.49077   1.10591   -66.10061 1.000 31.81768 ?  136 GLN   A CB  1 
ATOM   429  C  CG  . GLN   A 1 59  ? 4.92102   -0.28116  -65.94494 1.000 26.66325 ?  136 GLN   A CG  1 
ATOM   430  C  CD  . GLN   A 1 59  ? 5.52416   -1.22432  -66.92727 1.000 27.51912 ?  136 GLN   A CD  1 
ATOM   431  O  OE1 . GLN   A 1 59  ? 6.74201   -1.38006  -66.96579 1.000 28.38196 ?  136 GLN   A OE1 1 
ATOM   432  N  NE2 . GLN   A 1 59  ? 4.68750   -1.84302  -67.76003 1.000 25.81701 ?  136 GLN   A NE2 1 
ATOM   433  N  N   . SER   A 1 60  ? 4.55268   4.45852   -65.66258 1.000 33.61440 ?  137 SER   A N   1 
ATOM   434  C  CA  . SER   A 1 60  ? 4.94625   5.83874   -65.87935 1.000 33.76165 ?  137 SER   A CA  1 
ATOM   435  C  C   . SER   A 1 60  ? 3.73367   6.72535   -65.65161 1.000 33.98863 ?  137 SER   A C   1 
ATOM   436  O  O   . SER   A 1 60  ? 2.59704   6.33430   -65.92865 1.000 35.22743 ?  137 SER   A O   1 
ATOM   437  C  CB  . SER   A 1 60  ? 5.50309   6.05685   -67.29010 1.000 34.25491 ?  137 SER   A CB  1 
ATOM   438  O  OG  . SER   A 1 60  ? 4.48461   6.50918   -68.16797 1.000 36.56867 ?  137 SER   A OG  1 
ATOM   439  N  N   . LEU   A 1 61  ? 3.99468   7.92576   -65.15629 1.000 32.64630 ?  138 LEU   A N   1 
ATOM   440  C  CA  . LEU   A 1 61  ? 2.95704   8.89995   -64.89983 1.000 33.48943 ?  138 LEU   A CA  1 
ATOM   441  C  C   . LEU   A 1 61  ? 3.07440   10.01496  -65.92849 1.000 32.89012 ?  138 LEU   A C   1 
ATOM   442  O  O   . LEU   A 1 61  ? 4.14012   10.64194  -66.03236 1.000 33.83328 ?  138 LEU   A O   1 
ATOM   443  C  CB  . LEU   A 1 61  ? 3.09435   9.44761   -63.48198 1.000 32.67505 ?  138 LEU   A CB  1 
ATOM   444  C  CG  . LEU   A 1 61  ? 1.91648   10.26504  -62.97476 1.000 31.16540 ?  138 LEU   A CG  1 
ATOM   445  C  CD1 . LEU   A 1 61  ? 0.79352   9.32943   -62.57529 1.000 32.61008 ?  138 LEU   A CD1 1 
ATOM   446  C  CD2 . LEU   A 1 61  ? 2.33805   11.15575  -61.82855 1.000 33.09194 ?  138 LEU   A CD2 1 
ATOM   447  N  N   . PRO   A 1 62  ? 2.04714   10.29072  -66.72401 1.000 32.82408 ?  139 PRO   A N   1 
ATOM   448  C  CA  . PRO   A 1 62  ? 2.21974   11.25943  -67.81735 1.000 33.91206 ?  139 PRO   A CA  1 
ATOM   449  C  C   . PRO   A 1 62  ? 2.48439   12.65970  -67.28863 1.000 31.54700 ?  139 PRO   A C   1 
ATOM   450  O  O   . PRO   A 1 62  ? 1.91702   13.08325  -66.28049 1.000 32.27326 ?  139 PRO   A O   1 
ATOM   451  C  CB  . PRO   A 1 62  ? 0.89078   11.19020  -68.58123 1.000 34.42072 ?  139 PRO   A CB  1 
ATOM   452  C  CG  . PRO   A 1 62  ? -0.09088  10.58316  -67.63659 1.000 34.99879 ?  139 PRO   A CG  1 
ATOM   453  C  CD  . PRO   A 1 62  ? 0.68889   9.72264   -66.67116 1.000 34.90997 ?  139 PRO   A CD  1 
ATOM   454  N  N   . ALA   A 1 63  ? 3.34746   13.38800  -67.99276 1.000 30.96976 ?  140 ALA   A N   1 
ATOM   455  C  CA  . ALA   A 1 63  ? 3.63737   14.76320  -67.60426 1.000 33.37868 ?  140 ALA   A CA  1 
ATOM   456  C  C   . ALA   A 1 63  ? 2.37674   15.62296  -67.51790 1.000 32.23146 ?  140 ALA   A C   1 
ATOM   457  O  O   . ALA   A 1 63  ? 2.38961   16.65593  -66.84590 1.000 30.58415 ?  140 ALA   A O   1 
ATOM   458  C  CB  . ALA   A 1 63  ? 4.63999   15.37582  -68.57721 1.000 33.76442 ?  140 ALA   A CB  1 
ATOM   459  N  N   . GLU   A 1 64  ? 1.27665   15.19669  -68.14059 1.000 35.67206 ?  141 GLU   A N   1 
ATOM   460  C  CA  . GLU   A 1 64  ? 0.03912   15.97213  -68.09390 1.000 36.02643 ?  141 GLU   A CA  1 
ATOM   461  C  C   . GLU   A 1 64  ? -0.50735  16.11552  -66.67771 1.000 35.99222 ?  141 GLU   A C   1 
ATOM   462  O  O   . GLU   A 1 64  ? -1.19950  17.10168  -66.38384 1.000 34.49250 ?  141 GLU   A O   1 
ATOM   463  C  CB  . GLU   A 1 64  ? -1.01068  15.32434  -68.99218 1.000 38.45308 ?  141 GLU   A CB  1 
ATOM   464  C  CG  . GLU   A 1 64  ? -0.91355  15.73710  -70.45908 1.000 43.60849 ?  141 GLU   A CG  1 
ATOM   465  C  CD  . GLU   A 1 64  ? 0.13451   14.95137  -71.24190 1.000 41.57771 ?  141 GLU   A CD  1 
ATOM   466  O  OE1 . GLU   A 1 64  ? 0.75464   14.01961  -70.67331 1.000 39.50962 ?  141 GLU   A OE1 1 
ATOM   467  O  OE2 . GLU   A 1 64  ? 0.33320   15.27814  -72.43252 1.000 47.23992 ?  141 GLU   A OE2 1 
ATOM   468  N  N   . VAL   A 1 65  ? -0.23373  15.14002  -65.79681 1.000 33.08378 ?  142 VAL   A N   1 
ATOM   469  C  CA  . VAL   A 1 65  ? -0.65922  15.23865  -64.39581 1.000 33.84711 ?  142 VAL   A CA  1 
ATOM   470  C  C   . VAL   A 1 65  ? -0.17284  16.54082  -63.76196 1.000 33.13321 ?  142 VAL   A C   1 
ATOM   471  O  O   . VAL   A 1 65  ? -0.79562  17.05940  -62.82496 1.000 31.99728 ?  142 VAL   A O   1 
ATOM   472  C  CB  . VAL   A 1 65  ? -0.17425  14.00831  -63.58933 1.000 33.24826 ?  142 VAL   A CB  1 
ATOM   473  C  CG1 . VAL   A 1 65  ? -0.47556  14.17946  -62.10491 1.000 30.66061 ?  142 VAL   A CG1 1 
ATOM   474  C  CG2 . VAL   A 1 65  ? -0.81468  12.73878  -64.10312 1.000 34.05034 ?  142 VAL   A CG2 1 
ATOM   475  N  N   . GLY   A 1 66  ? 0.93790   17.09021  -64.25507 1.000 33.81736 ?  143 GLY   A N   1 
ATOM   476  C  CA  . GLY   A 1 66  ? 1.43745   18.36764  -63.77579 1.000 31.51318 ?  143 GLY   A CA  1 
ATOM   477  C  C   . GLY   A 1 66  ? 0.52677   19.54316  -64.05903 1.000 35.89278 ?  143 GLY   A C   1 
ATOM   478  O  O   . GLY   A 1 66  ? 0.76081   20.62985  -63.51548 1.000 37.82560 ?  143 GLY   A O   1 
ATOM   479  N  N   . CYS   A 1 67  ? -0.48724  19.35748  -64.90711 1.000 32.37935 ?  144 CYS   A N   1 
ATOM   480  C  CA  . CYS   A 1 67  ? -1.49261  20.38534  -65.12791 1.000 32.80978 ?  144 CYS   A CA  1 
ATOM   481  C  C   . CYS   A 1 67  ? -2.53021  20.44266  -64.01093 1.000 35.44813 ?  144 CYS   A C   1 
ATOM   482  O  O   . CYS   A 1 67  ? -3.23368  21.45020  -63.89455 1.000 33.60885 ?  144 CYS   A O   1 
ATOM   483  C  CB  . CYS   A 1 67  ? -2.20721  20.14659  -66.46741 1.000 37.90851 ?  144 CYS   A CB  1 
ATOM   484  S  SG  . CYS   A 1 67  ? -1.19613  20.39551  -67.96412 1.000 43.46861 ?  144 CYS   A SG  1 
ATOM   485  N  N   . LEU   A 1 68  ? -2.66719  19.37784  -63.20800 1.000 35.75648 ?  145 LEU   A N   1 
ATOM   486  C  CA  . LEU   A 1 68  ? -3.62944  19.37372  -62.10999 1.000 33.55251 ?  145 LEU   A CA  1 
ATOM   487  C  C   . LEU   A 1 68  ? -3.11095  20.26435  -60.98763 1.000 34.42573 ?  145 LEU   A C   1 
ATOM   488  O  O   . LEU   A 1 68  ? -2.68454  19.80051  -59.92037 1.000 36.25319 ?  145 LEU   A O   1 
ATOM   489  C  CB  . LEU   A 1 68  ? -3.89674  17.95188  -61.64433 1.000 31.30886 ?  145 LEU   A CB  1 
ATOM   490  C  CG  . LEU   A 1 68  ? -4.16677  17.06043  -62.85894 1.000 31.58118 ?  145 LEU   A CG  1 
ATOM   491  C  CD1 . LEU   A 1 68  ? -4.44767  15.60998  -62.45139 1.000 27.27321 ?  145 LEU   A CD1 1 
ATOM   492  C  CD2 . LEU   A 1 68  ? -5.29299  17.64293  -63.70428 1.000 29.58786 ?  145 LEU   A CD2 1 
ATOM   493  N  N   . VAL   A 1 69  ? -3.15145  21.56429  -61.26808 1.000 30.73330 ?  146 VAL   A N   1 
ATOM   494  C  CA  . VAL   A 1 69  ? -2.56245  22.61654  -60.45942 1.000 34.66414 ?  146 VAL   A CA  1 
ATOM   495  C  C   . VAL   A 1 69  ? -3.10491  22.66214  -59.03120 1.000 34.23081 ?  146 VAL   A C   1 
ATOM   496  O  O   . VAL   A 1 69  ? -2.45079  23.21138  -58.13997 1.000 31.32755 ?  146 VAL   A O   1 
ATOM   497  C  CB  . VAL   A 1 69  ? -2.80317  23.94432  -61.21754 1.000 33.02832 ?  146 VAL   A CB  1 
ATOM   498  C  CG1 . VAL   A 1 69  ? -2.96380  25.08515  -60.26180 1.000 34.66960 ?  146 VAL   A CG1 1 
ATOM   499  C  CG2 . VAL   A 1 69  ? -1.67568  24.19350  -62.20665 1.000 32.41444 ?  146 VAL   A CG2 1 
ATOM   500  N  N   . ASN   A 1 70  ? -4.28244  22.09123  -58.78410 1.000 36.01209 ?  147 ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 70  ? -4.91720  22.16586  -57.47280 1.000 36.94160 ?  147 ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 70  ? -4.83058  20.86261  -56.68899 1.000 33.12243 ?  147 ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 70  ? -5.50779  20.72305  -55.66307 1.000 31.09661 ?  147 ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 70  ? -6.37855  22.59289  -57.62029 1.000 33.35885 ?  147 ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 70  ? -6.51010  24.03352  -58.08457 1.000 38.77318 ?  147 ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 70  ? -5.85668  24.93434  -57.54993 1.000 38.38365 ?  147 ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 70  ? -7.33781  24.25506  -59.10241 1.000 35.39336 ?  147 ASN   A ND2 1 
ATOM   508  N  N   . LEU   A 1 71  ? -4.01375  19.90982  -57.13244 1.000 32.29268 ?  148 LEU   A N   1 
ATOM   509  C  CA  . LEU   A 1 71  ? -3.92322  18.64432  -56.41734 1.000 30.66967 ?  148 LEU   A CA  1 
ATOM   510  C  C   . LEU   A 1 71  ? -3.41837  18.86370  -54.99942 1.000 31.50313 ?  148 LEU   A C   1 
ATOM   511  O  O   . LEU   A 1 71  ? -2.34261  19.43088  -54.78602 1.000 35.16796 ?  148 LEU   A O   1 
ATOM   512  C  CB  . LEU   A 1 71  ? -3.00868  17.67293  -57.15649 1.000 31.45932 ?  148 LEU   A CB  1 
ATOM   513  C  CG  . LEU   A 1 71  ? -3.67605  16.80912  -58.21653 1.000 30.04672 ?  148 LEU   A CG  1 
ATOM   514  C  CD1 . LEU   A 1 71  ? -2.75147  15.65108  -58.56397 1.000 29.90621 ?  148 LEU   A CD1 1 
ATOM   515  C  CD2 . LEU   A 1 71  ? -5.04969  16.33116  -57.73162 1.000 28.05160 ?  148 LEU   A CD2 1 
ATOM   516  N  N   . MET   A 1 72  ? -4.19602  18.42186  -54.02672 1.000 31.71916 ?  149 MET   A N   1 
ATOM   517  C  CA  . MET   A 1 72  ? -3.69714  18.35161  -52.66525 1.000 33.86246 ?  149 MET   A CA  1 
ATOM   518  C  C   . MET   A 1 72  ? -3.17370  16.97369  -52.32025 1.000 31.25758 ?  149 MET   A C   1 
ATOM   519  O  O   . MET   A 1 72  ? -2.23642  16.86169  -51.52568 1.000 35.41238 ?  149 MET   A O   1 
ATOM   520  C  CB  . MET   A 1 72  ? -4.79425  18.76427  -51.67490 1.000 35.15497 ?  149 MET   A CB  1 
ATOM   521  C  CG  . MET   A 1 72  ? -5.24504  20.22480  -51.89083 1.000 41.68474 ?  149 MET   A CG  1 
ATOM   522  S  SD  . MET   A 1 72  ? -6.50345  20.85651  -50.74874 1.000 54.73679 ?  149 MET   A SD  1 
ATOM   523  C  CE  . MET   A 1 72  ? -7.37782  19.31426  -50.35772 1.000 44.17285 ?  149 MET   A CE  1 
ATOM   524  N  N   . THR   A 1 73  ? -3.72415  15.93297  -52.94058 1.000 33.45117 ?  150 THR   A N   1 
ATOM   525  C  CA  . THR   A 1 73  ? -3.38858  14.54421  -52.64228 1.000 33.61840 ?  150 THR   A CA  1 
ATOM   526  C  C   . THR   A 1 73  ? -3.19302  13.77016  -53.93432 1.000 30.16487 ?  150 THR   A C   1 
ATOM   527  O  O   . THR   A 1 73  ? -4.04130  13.82105  -54.83248 1.000 29.17372 ?  150 THR   A O   1 
ATOM   528  C  CB  . THR   A 1 73  ? -4.47865  13.85522  -51.80548 1.000 30.35992 ?  150 THR   A CB  1 
ATOM   529  O  OG1 . THR   A 1 73  ? -4.29548  14.18364  -50.43288 1.000 34.91495 ?  150 THR   A OG1 1 
ATOM   530  C  CG2 . THR   A 1 73  ? -4.37594  12.34827  -51.94901 1.000 32.04907 ?  150 THR   A CG2 1 
ATOM   531  N  N   . LEU   A 1 74  ? -2.09285  13.02755  -54.00219 1.000 30.85528 ?  151 LEU   A N   1 
ATOM   532  C  CA  . LEU   A 1 74  ? -1.77182  12.18104  -55.14498 1.000 31.36825 ?  151 LEU   A CA  1 
ATOM   533  C  C   . LEU   A 1 74  ? -1.42488  10.80221  -54.60645 1.000 29.57388 ?  151 LEU   A C   1 
ATOM   534  O  O   . LEU   A 1 74  ? -0.39487  10.63944  -53.94587 1.000 33.39155 ?  151 LEU   A O   1 
ATOM   535  C  CB  . LEU   A 1 74  ? -0.61383  12.77856  -55.94633 1.000 31.58355 ?  151 LEU   A CB  1 
ATOM   536  C  CG  . LEU   A 1 74  ? -0.19056  12.01890  -57.19825 1.000 27.24059 ?  151 LEU   A CG  1 
ATOM   537  C  CD1 . LEU   A 1 74  ? -1.38803  11.81706  -58.12718 1.000 28.20950 ?  151 LEU   A CD1 1 
ATOM   538  C  CD2 . LEU   A 1 74  ? 0.91048   12.77122  -57.89613 1.000 24.81826 ?  151 LEU   A CD2 1 
ATOM   539  N  N   . ALA   A 1 75  ? -2.28120  9.81356   -54.85667 1.000 27.49276 ?  152 ALA   A N   1 
ATOM   540  C  CA  . ALA   A 1 75  ? -2.11054  8.48087   -54.27831 1.000 29.59050 ?  152 ALA   A CA  1 
ATOM   541  C  C   . ALA   A 1 75  ? -1.70787  7.48227   -55.36580 1.000 31.82550 ?  152 ALA   A C   1 
ATOM   542  O  O   . ALA   A 1 75  ? -2.53214  7.10761   -56.21052 1.000 31.63900 ?  152 ALA   A O   1 
ATOM   543  C  CB  . ALA   A 1 75  ? -3.39015  8.04080   -53.58003 1.000 31.96964 ?  152 ALA   A CB  1 
ATOM   544  N  N   . LEU   A 1 76  ? -0.45322  7.01771   -55.31997 1.000 31.03309 ?  153 LEU   A N   1 
ATOM   545  C  CA  . LEU   A 1 76  ? 0.11462   6.20123   -56.39091 1.000 30.68239 ?  153 LEU   A CA  1 
ATOM   546  C  C   . LEU   A 1 76  ? 0.63392   4.83917   -55.94097 1.000 29.66323 ?  153 LEU   A C   1 
ATOM   547  O  O   . LEU   A 1 76  ? 1.39203   4.20728   -56.69101 1.000 27.72701 ?  153 LEU   A O   1 
ATOM   548  C  CB  . LEU   A 1 76  ? 1.26002   6.95720   -57.06283 1.000 28.48062 ?  153 LEU   A CB  1 
ATOM   549  C  CG  . LEU   A 1 76  ? 0.84669   8.25976   -57.71416 1.000 29.55791 ?  153 LEU   A CG  1 
ATOM   550  C  CD1 . LEU   A 1 76  ? 2.09234   9.05372   -58.07194 1.000 28.24407 ?  153 LEU   A CD1 1 
ATOM   551  C  CD2 . LEU   A 1 76  ? 0.01651   7.93094   -58.93844 1.000 31.46697 ?  153 LEU   A CD2 1 
ATOM   552  N  N   . SER   A 1 77  ? 0.26424   4.36707   -54.75313 1.000 29.83901 ?  154 SER   A N   1 
ATOM   553  C  CA  . SER   A 1 77  ? 0.86405   3.14188   -54.23791 1.000 31.22562 ?  154 SER   A CA  1 
ATOM   554  C  C   . SER   A 1 77  ? 0.46110   1.93760   -55.08851 1.000 28.32210 ?  154 SER   A C   1 
ATOM   555  O  O   . SER   A 1 77  ? -0.52861  1.96662   -55.81725 1.000 28.37344 ?  154 SER   A O   1 
ATOM   556  C  CB  . SER   A 1 77  ? 0.44516   2.92150   -52.79207 1.000 28.56138 ?  154 SER   A CB  1 
ATOM   557  O  OG  . SER   A 1 77  ? -0.96577  2.86942   -52.74864 1.000 32.72403 ?  154 SER   A OG  1 
ATOM   558  N  N   . GLU   A 1 78  ? 1.26023   0.87030   -54.99083 1.000 30.77201 ?  155 GLU   A N   1 
ATOM   559  C  CA  . GLU   A 1 78  ? 1.00870   -0.39307  -55.68522 1.000 28.29312 ?  155 GLU   A CA  1 
ATOM   560  C  C   . GLU   A 1 78  ? 0.87264   -0.18429  -57.19416 1.000 28.60385 ?  155 GLU   A C   1 
ATOM   561  O  O   . GLU   A 1 78  ? -0.16475  -0.46465  -57.80358 1.000 27.38350 ?  155 GLU   A O   1 
ATOM   562  C  CB  . GLU   A 1 78  ? -0.23458  -1.09727  -55.14190 1.000 33.30132 ?  155 GLU   A CB  1 
ATOM   563  C  CG  . GLU   A 1 78  ? -0.16337  -1.56693  -53.70653 1.000 35.48802 ?  155 GLU   A CG  1 
ATOM   564  C  CD  . GLU   A 1 78  ? -1.33849  -2.48852  -53.35724 1.000 50.93198 ?  155 GLU   A CD  1 
ATOM   565  O  OE1 . GLU   A 1 78  ? -1.80908  -3.23969  -54.25687 1.000 47.99134 ?  155 GLU   A OE1 1 
ATOM   566  O  OE2 . GLU   A 1 78  ? -1.80105  -2.45369  -52.19060 1.000 58.75432 ?  155 GLU   A OE2 1 
ATOM   567  N  N   . ASN   A 1 79  ? 1.95100   0.31460   -57.78317 1.000 27.86307 ?  156 ASN   A N   1 
ATOM   568  C  CA  . ASN   A 1 79  ? 2.10955   0.40343   -59.22697 1.000 27.65031 ?  156 ASN   A CA  1 
ATOM   569  C  C   . ASN   A 1 79  ? 3.53110   -0.06059  -59.52519 1.000 27.42081 ?  156 ASN   A C   1 
ATOM   570  O  O   . ASN   A 1 79  ? 4.21298   -0.62583  -58.66827 1.000 28.18243 ?  156 ASN   A O   1 
ATOM   571  C  CB  . ASN   A 1 79  ? 1.81686   1.83384   -59.71585 1.000 27.83910 ?  156 ASN   A CB  1 
ATOM   572  C  CG  . ASN   A 1 79  ? 0.33665   2.17475   -59.69988 1.000 28.48642 ?  156 ASN   A CG  1 
ATOM   573  O  OD1 . ASN   A 1 79  ? -0.43670  1.68042   -60.52396 1.000 28.53683 ?  156 ASN   A OD1 1 
ATOM   574  N  ND2 . ASN   A 1 79  ? -0.06656  3.02395   -58.76282 1.000 28.95060 ?  156 ASN   A ND2 1 
ATOM   575  N  N   . SER   A 1 80  ? 4.02651   0.21163   -60.72116 1.000 29.49132 ?  157 SER   A N   1 
ATOM   576  C  CA  . SER   A 1 80  ? 5.41595   -0.07114  -61.05209 1.000 29.05566 ?  157 SER   A CA  1 
ATOM   577  C  C   . SER   A 1 80  ? 6.16250   1.19963   -61.44624 1.000 30.15069 ?  157 SER   A C   1 
ATOM   578  O  O   . SER   A 1 80  ? 6.95074   1.20434   -62.38552 1.000 31.24718 ?  157 SER   A O   1 
ATOM   579  C  CB  . SER   A 1 80  ? 5.50011   -1.10683  -62.16539 1.000 30.04190 ?  157 SER   A CB  1 
ATOM   580  O  OG  . SER   A 1 80  ? 4.62521   -2.19332  -61.89375 1.000 41.46495 ?  157 SER   A OG  1 
ATOM   581  N  N   . LEU   A 1 81  ? 5.92821   2.30146   -60.74087 1.000 28.98393 ?  158 LEU   A N   1 
ATOM   582  C  CA  . LEU   A 1 81  ? 6.61399   3.53766   -61.08848 1.000 30.99924 ?  158 LEU   A CA  1 
ATOM   583  C  C   . LEU   A 1 81  ? 8.08825   3.44570   -60.72630 1.000 31.91156 ?  158 LEU   A C   1 
ATOM   584  O  O   . LEU   A 1 81  ? 8.44782   2.93606   -59.66335 1.000 27.77160 ?  158 LEU   A O   1 
ATOM   585  C  CB  . LEU   A 1 81  ? 5.98907   4.72864   -60.36483 1.000 28.29646 ?  158 LEU   A CB  1 
ATOM   586  C  CG  . LEU   A 1 81  ? 4.52920   4.97750   -60.68045 1.000 26.34244 ?  158 LEU   A CG  1 
ATOM   587  C  CD1 . LEU   A 1 81  ? 4.04662   6.11822   -59.85274 1.000 30.29691 ?  158 LEU   A CD1 1 
ATOM   588  C  CD2 . LEU   A 1 81  ? 4.38712   5.26569   -62.14622 1.000 27.56400 ?  158 LEU   A CD2 1 
ATOM   589  N  N   . THR   A 1 82  ? 8.94467   3.95124   -61.61931 1.000 32.32558 ?  159 THR   A N   1 
ATOM   590  C  CA  . THR   A 1 82  ? 10.35693  4.15335   -61.31855 1.000 29.98826 ?  159 THR   A CA  1 
ATOM   591  C  C   . THR   A 1 82  ? 10.75995  5.61803   -61.43734 1.000 30.90349 ?  159 THR   A C   1 
ATOM   592  O  O   . THR   A 1 82  ? 11.95141  5.93431   -61.38228 1.000 31.27673 ?  159 THR   A O   1 
ATOM   593  C  CB  . THR   A 1 82  ? 11.23768  3.31589   -62.24403 1.000 33.27826 ?  159 THR   A CB  1 
ATOM   594  O  OG1 . THR   A 1 82  ? 11.01285  3.73835   -63.58766 1.000 36.06359 ?  159 THR   A OG1 1 
ATOM   595  C  CG2 . THR   A 1 82  ? 10.92356  1.83091   -62.13066 1.000 32.02355 ?  159 THR   A CG2 1 
ATOM   596  N  N   . SER   A 1 83  ? 9.80828   6.52099   -61.62043 1.000 31.98094 ?  160 SER   A N   1 
ATOM   597  C  CA  . SER   A 1 83  ? 10.17506  7.90981   -61.82984 1.000 29.23066 ?  160 SER   A CA  1 
ATOM   598  C  C   . SER   A 1 83  ? 8.91524   8.75378   -61.87292 1.000 28.81654 ?  160 SER   A C   1 
ATOM   599  O  O   . SER   A 1 83  ? 7.80293   8.24278   -62.04234 1.000 29.83976 ?  160 SER   A O   1 
ATOM   600  C  CB  . SER   A 1 83  ? 10.96634  8.07555   -63.12118 1.000 29.13096 ?  160 SER   A CB  1 
ATOM   601  O  OG  . SER   A 1 83  ? 10.17847  7.63626   -64.20725 1.000 30.77050 ?  160 SER   A OG  1 
ATOM   602  N  N   . LEU   A 1 84  ? 9.10722   10.05467  -61.73631 1.000 27.11868 ?  161 LEU   A N   1 
ATOM   603  C  CA  . LEU   A 1 84  ? 7.98937   10.96691  -61.85445 1.000 28.52376 ?  161 LEU   A CA  1 
ATOM   604  C  C   . LEU   A 1 84  ? 8.35628   12.10876  -62.79006 1.000 31.35204 ?  161 LEU   A C   1 
ATOM   605  O  O   . LEU   A 1 84  ? 9.51008   12.56106  -62.81331 1.000 31.44122 ?  161 LEU   A O   1 
ATOM   606  C  CB  . LEU   A 1 84  ? 7.57675   11.52240  -60.48214 1.000 28.45069 ?  161 LEU   A CB  1 
ATOM   607  C  CG  . LEU   A 1 84  ? 7.00784   10.52118  -59.46475 1.000 27.43831 ?  161 LEU   A CG  1 
ATOM   608  C  CD1 . LEU   A 1 84  ? 6.92558   11.16135  -58.12626 1.000 27.12054 ?  161 LEU   A CD1 1 
ATOM   609  C  CD2 . LEU   A 1 84  ? 5.62225   10.01484  -59.87846 1.000 27.48423 ?  161 LEU   A CD2 1 
ATOM   610  N  N   . PRO   A 1 85  ? 7.39505   12.58830  -63.57159 1.000 27.63326 ?  162 PRO   A N   1 
ATOM   611  C  CA  . PRO   A 1 85  ? 7.67952   13.67655  -64.50696 1.000 31.80959 ?  162 PRO   A CA  1 
ATOM   612  C  C   . PRO   A 1 85  ? 8.04209   14.97225  -63.79043 1.000 31.52609 ?  162 PRO   A C   1 
ATOM   613  O  O   . PRO   A 1 85  ? 7.55307   15.27906  -62.70302 1.000 31.77484 ?  162 PRO   A O   1 
ATOM   614  C  CB  . PRO   A 1 85  ? 6.36652   13.82045  -65.28525 1.000 29.30825 ?  162 PRO   A CB  1 
ATOM   615  C  CG  . PRO   A 1 85  ? 5.32730   13.31437  -64.35922 1.000 30.05074 ?  162 PRO   A CG  1 
ATOM   616  C  CD  . PRO   A 1 85  ? 5.98092   12.18496  -63.60836 1.000 30.71122 ?  162 PRO   A CD  1 
ATOM   617  N  N   . ASP   A 1 86  ? 8.91179   15.74431  -64.43578 1.000 33.50980 ?  163 ASP   A N   1 
ATOM   618  C  CA  . ASP   A 1 86  ? 9.35671   17.01588  -63.87793 1.000 36.83651 ?  163 ASP   A CA  1 
ATOM   619  C  C   . ASP   A 1 86  ? 8.24372   18.05043  -63.82903 1.000 36.18749 ?  163 ASP   A C   1 
ATOM   620  O  O   . ASP   A 1 86  ? 8.27530   18.95315  -62.98305 1.000 35.02404 ?  163 ASP   A O   1 
ATOM   621  C  CB  . ASP   A 1 86  ? 10.52738  17.53815  -64.69286 1.000 34.73959 ?  163 ASP   A CB  1 
ATOM   622  C  CG  . ASP   A 1 86  ? 11.82837  17.07892  -64.13106 1.000 40.90449 ?  163 ASP   A CG  1 
ATOM   623  O  OD1 . ASP   A 1 86  ? 11.96785  17.18352  -62.89318 1.000 40.38534 ?  163 ASP   A OD1 1 
ATOM   624  O  OD2 . ASP   A 1 86  ? 12.67963  16.58513  -64.90232 1.000 44.14879 ?  163 ASP   A OD2 1 
ATOM   625  N  N   . SER   A 1 87  ? 7.25274   17.92952  -64.71284 1.000 34.52065 ?  164 SER   A N   1 
ATOM   626  C  CA  . SER   A 1 87  ? 6.11908   18.83916  -64.69248 1.000 33.25170 ?  164 SER   A CA  1 
ATOM   627  C  C   . SER   A 1 87  ? 5.39494   18.85670  -63.34976 1.000 34.40461 ?  164 SER   A C   1 
ATOM   628  O  O   . SER   A 1 87  ? 4.58979   19.75834  -63.11836 1.000 36.22665 ?  164 SER   A O   1 
ATOM   629  C  CB  . SER   A 1 87  ? 5.14384   18.45889  -65.80146 1.000 32.75287 ?  164 SER   A CB  1 
ATOM   630  O  OG  . SER   A 1 87  ? 4.65855   17.13641  -65.62110 1.000 31.25790 ?  164 SER   A OG  1 
ATOM   631  N  N   . LEU   A 1 88  ? 5.63390   17.87898  -62.46888 1.000 35.06406 ?  165 LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 88  ? 4.96462   17.87597  -61.16622 1.000 36.87620 ?  165 LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 88  ? 5.38160   19.04919  -60.28147 1.000 34.37907 ?  165 LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 88  ? 4.72888   19.27811  -59.25609 1.000 35.34064 ?  165 LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 88  ? 5.20915   16.54569  -60.44380 1.000 34.47035 ?  165 LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 88  ? 4.55032   15.31201  -61.07026 1.000 29.22544 ?  165 LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 88  ? 4.86891   14.08278  -60.25369 1.000 31.29117 ?  165 LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 88  ? 3.06705   15.49354  -61.17523 1.000 31.56586 ?  165 LEU   A CD2 1 
ATOM   639  N  N   . ASP   A 1 89  ? 6.45285   19.77135  -60.65212 1.000 35.64014 ?  166 ASP   A N   1 
ATOM   640  C  CA  . ASP   A 1 89  ? 6.78633   21.14904  -60.25586 1.000 39.72487 ?  166 ASP   A CA  1 
ATOM   641  C  C   . ASP   A 1 89  ? 5.60300   22.08090  -60.02823 1.000 35.00366 ?  166 ASP   A C   1 
ATOM   642  O  O   . ASP   A 1 89  ? 5.65482   22.97006  -59.17411 1.000 32.05000 ?  166 ASP   A O   1 
ATOM   643  C  CB  . ASP   A 1 89  ? 7.61829   21.82305  -61.35389 1.000 38.73143 ?  166 ASP   A CB  1 
ATOM   644  C  CG  . ASP   A 1 89  ? 9.08699   21.63698  -61.16648 1.000 44.33872 ?  166 ASP   A CG  1 
ATOM   645  O  OD1 . ASP   A 1 89  ? 9.50344   21.44391  -60.00571 1.000 49.07892 ?  166 ASP   A OD1 1 
ATOM   646  O  OD2 . ASP   A 1 89  ? 9.81970   21.69087  -62.17589 1.000 47.24202 ?  166 ASP   A OD2 1 
ATOM   647  N  N   . ASN   A 1 90  ? 4.58868   21.94340  -60.87166 1.000 31.99746 ?  167 ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 90  ? 3.43908   22.82953  -60.90899 1.000 37.12526 ?  167 ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 90  ? 2.44856   22.56254  -59.79130 1.000 37.96989 ?  167 ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 90  ? 1.57793   23.40651  -59.53553 1.000 36.76789 ?  167 ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 90  ? 2.75604   22.68086  -62.26177 1.000 36.21042 ?  167 ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 90  ? 3.71497   22.90373  -63.39862 1.000 40.01650 ?  167 ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 90  ? 4.50993   23.84118  -63.37178 1.000 42.94260 ?  167 ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 90  ? 3.67232   22.03123  -64.39447 1.000 44.81806 ?  167 ASN   A ND2 1 
ATOM   655  N  N   . LEU   A 1 91  ? 2.56918   21.41741  -59.11746 1.000 36.00216 ?  168 LEU   A N   1 
ATOM   656  C  CA  . LEU   A 1 91  ? 1.68255   21.05682  -58.01647 1.000 35.63963 ?  168 LEU   A CA  1 
ATOM   657  C  C   . LEU   A 1 91  ? 2.08134   21.83045  -56.75776 1.000 35.25152 ?  168 LEU   A C   1 
ATOM   658  O  O   . LEU   A 1 91  ? 2.56589   21.27628  -55.76732 1.000 34.79129 ?  168 LEU   A O   1 
ATOM   659  C  CB  . LEU   A 1 91  ? 1.72851   19.55280  -57.80588 1.000 35.01390 ?  168 LEU   A CB  1 
ATOM   660  C  CG  . LEU   A 1 91  ? 0.75696   18.76003  -58.66380 1.000 31.45063 ?  168 LEU   A CG  1 
ATOM   661  C  CD1 . LEU   A 1 91  ? 0.44387   19.49619  -59.96431 1.000 34.44651 ?  168 LEU   A CD1 1 
ATOM   662  C  CD2 . LEU   A 1 91  ? 1.30302   17.38239  -58.92781 1.000 30.89331 ?  168 LEU   A CD2 1 
ATOM   663  N  N   . LYS   A 1 92  ? 1.83868   23.14833  -56.80242 1.000 34.37526 ?  169 LYS   A N   1 
ATOM   664  C  CA  . LYS   A 1 92  ? 2.27821   24.02833  -55.71681 1.000 35.50470 ?  169 LYS   A CA  1 
ATOM   665  C  C   . LYS   A 1 92  ? 1.49403   23.83042  -54.42941 1.000 32.34657 ?  169 LYS   A C   1 
ATOM   666  O  O   . LYS   A 1 92  ? 1.92256   24.33267  -53.38276 1.000 33.90889 ?  169 LYS   A O   1 
ATOM   667  C  CB  . LYS   A 1 92  ? 2.18957   25.50134  -56.13601 1.000 37.16840 ?  169 LYS   A CB  1 
ATOM   668  C  CG  . LYS   A 1 92  ? 3.29216   25.94767  -57.09269 1.000 40.94888 ?  169 LYS   A CG  1 
ATOM   669  C  CD  . LYS   A 1 92  ? 4.67096   25.63123  -56.52372 1.000 41.02592 ?  169 LYS   A CD  1 
ATOM   670  C  CE  . LYS   A 1 92  ? 5.77517   26.52166  -57.12485 1.000 51.97119 ?  169 LYS   A CE  1 
ATOM   671  N  NZ  . LYS   A 1 92  ? 6.01315   27.82400  -56.36380 1.000 52.62720 ?  169 LYS   A NZ  1 
ATOM   672  N  N   . LYS   A 1 93  ? 0.37480   23.10914  -54.47314 1.000 33.13712 ?  170 LYS   A N   1 
ATOM   673  C  CA  . LYS   A 1 93  ? -0.44650  22.86643  -53.29391 1.000 35.26054 ?  170 LYS   A CA  1 
ATOM   674  C  C   . LYS   A 1 93  ? -0.42731  21.41391  -52.83578 1.000 34.25667 ?  170 LYS   A C   1 
ATOM   675  O  O   . LYS   A 1 93  ? -1.20581  21.05423  -51.94892 1.000 36.60641 ?  170 LYS   A O   1 
ATOM   676  C  CB  . LYS   A 1 93  ? -1.89421  23.28606  -53.55863 1.000 34.23089 ?  170 LYS   A CB  1 
ATOM   677  C  CG  . LYS   A 1 93  ? -2.06432  24.66746  -54.14300 1.000 36.38524 ?  170 LYS   A CG  1 
ATOM   678  C  CD  . LYS   A 1 93  ? -3.53018  25.02185  -54.09715 1.000 39.25552 ?  170 LYS   A CD  1 
ATOM   679  C  CE  . LYS   A 1 93  ? -3.97906  25.75236  -55.33182 1.000 42.43628 ?  170 LYS   A CE  1 
ATOM   680  N  NZ  . LYS   A 1 93  ? -5.44104  26.04443  -55.23279 1.000 46.02216 ?  170 LYS   A NZ  1 
ATOM   681  N  N   . LEU   A 1 94  ? 0.41760   20.56742  -53.42214 1.000 32.46879 ?  171 LEU   A N   1 
ATOM   682  C  CA  . LEU   A 1 94  ? 0.36880   19.13417  -53.13197 1.000 33.94845 ?  171 LEU   A CA  1 
ATOM   683  C  C   . LEU   A 1 94  ? 0.76611   18.88048  -51.68286 1.000 33.67753 ?  171 LEU   A C   1 
ATOM   684  O  O   . LEU   A 1 94  ? 1.91162   19.11880  -51.29113 1.000 34.30418 ?  171 LEU   A O   1 
ATOM   685  C  CB  . LEU   A 1 94  ? 1.28344   18.36254  -54.08054 1.000 32.17442 ?  171 LEU   A CB  1 
ATOM   686  C  CG  . LEU   A 1 94  ? 1.15894   16.84572  -53.95774 1.000 30.70010 ?  171 LEU   A CG  1 
ATOM   687  C  CD1 . LEU   A 1 94  ? -0.19468  16.38220  -54.47740 1.000 30.28361 ?  171 LEU   A CD1 1 
ATOM   688  C  CD2 . LEU   A 1 94  ? 2.30102   16.13828  -54.66920 1.000 27.97320 ?  171 LEU   A CD2 1 
ATOM   689  N  N   . ARG   A 1 95  ? -0.16514  18.37925  -50.88150 1.000 35.06050 ?  172 ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 95  ? 0.12866   18.16806  -49.47051 1.000 34.24734 ?  172 ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 95  ? 0.57509   16.75179  -49.17303 1.000 35.69778 ?  172 ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 95  ? 1.34260   16.52935  -48.22784 1.000 35.24465 ?  172 ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 95  ? -1.09021  18.49014  -48.61549 1.000 34.36137 ?  172 ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 95  ? -1.22777  19.95134  -48.26318 1.000 37.74202 ?  172 ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 95  ? -2.35403  20.11332  -47.27726 1.000 48.01367 ?  172 ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 95  ? -3.05766  21.37454  -47.45288 1.000 62.09326 ?  172 ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 95  ? -4.27630  21.61707  -46.98949 1.000 71.78019 ?  172 ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 95  ? -4.96661  20.68901  -46.34086 1.000 69.32441 ?  172 ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 95  ? -4.81634  22.81971  -47.18148 1.000 77.30808 ?  172 ARG   A NH2 1 
ATOM   700  N  N   . MET   A 1 96  ? 0.12811   15.78510  -49.96065 1.000 33.82198 ?  173 MET   A N   1 
ATOM   701  C  CA  . MET   A 1 96  ? 0.38990   14.40359  -49.61837 1.000 31.45511 ?  173 MET   A CA  1 
ATOM   702  C  C   . MET   A 1 96  ? 0.67184   13.60756  -50.87796 1.000 28.74035 ?  173 MET   A C   1 
ATOM   703  O  O   . MET   A 1 96  ? -0.06714  13.70146  -51.86103 1.000 29.18132 ?  173 MET   A O   1 
ATOM   704  C  CB  . MET   A 1 96  ? -0.79033  13.83155  -48.84001 1.000 33.60785 ?  173 MET   A CB  1 
ATOM   705  C  CG  . MET   A 1 96  ? -1.53203  12.78949  -49.55826 1.000 36.56678 ?  173 MET   A CG  1 
ATOM   706  S  SD  . MET   A 1 96  ? -0.82155  11.23193  -49.08443 1.000 45.75542 ?  173 MET   A SD  1 
ATOM   707  C  CE  . MET   A 1 96  ? -1.60263  10.15345  -50.29140 1.000 32.76638 ?  173 MET   A CE  1 
ATOM   708  N  N   . LEU   A 1 97  ? 1.75503   12.83849  -50.84041 1.000 30.03261 ?  174 LEU   A N   1 
ATOM   709  C  CA  . LEU   A 1 97  ? 2.20731   12.02837  -51.96290 1.000 31.72438 ?  174 LEU   A CA  1 
ATOM   710  C  C   . LEU   A 1 97  ? 2.50508   10.62192  -51.45305 1.000 32.38640 ?  174 LEU   A C   1 
ATOM   711  O  O   . LEU   A 1 97  ? 3.29193   10.45629  -50.51084 1.000 27.60775 ?  174 LEU   A O   1 
ATOM   712  C  CB  . LEU   A 1 97  ? 3.44616   12.65988  -52.61243 1.000 27.10131 ?  174 LEU   A CB  1 
ATOM   713  C  CG  . LEU   A 1 97  ? 4.08750   11.96026  -53.79555 1.000 26.05093 ?  174 LEU   A CG  1 
ATOM   714  C  CD1 . LEU   A 1 97  ? 3.04397   11.70584  -54.85361 1.000 26.54723 ?  174 LEU   A CD1 1 
ATOM   715  C  CD2 . LEU   A 1 97  ? 5.20746   12.82361  -54.32710 1.000 25.27580 ?  174 LEU   A CD2 1 
ATOM   716  N  N   . ASP   A 1 98  ? 1.87815   9.61469   -52.07991 1.000 30.34328 ?  175 ASP   A N   1 
ATOM   717  C  CA  . ASP   A 1 98  ? 1.93249   8.22104   -51.63357 1.000 29.53717 ?  175 ASP   A CA  1 
ATOM   718  C  C   . ASP   A 1 98  ? 2.52859   7.36669   -52.74849 1.000 28.46408 ?  175 ASP   A C   1 
ATOM   719  O  O   . ASP   A 1 98  ? 1.88723   7.13777   -53.78122 1.000 26.25614 ?  175 ASP   A O   1 
ATOM   720  C  CB  . ASP   A 1 98  ? 0.53829   7.72360   -51.22724 1.000 31.24532 ?  175 ASP   A CB  1 
ATOM   721  C  CG  . ASP   A 1 98  ? 0.53690   6.27112   -50.73976 1.000 34.25354 ?  175 ASP   A CG  1 
ATOM   722  O  OD1 . ASP   A 1 98  ? 1.58239   5.58134   -50.85797 1.000 34.12155 ?  175 ASP   A OD1 1 
ATOM   723  O  OD2 . ASP   A 1 98  ? -0.51730  5.81032   -50.23235 1.000 34.96741 ?  175 ASP   A OD2 1 
ATOM   724  N  N   . LEU   A 1 99  ? 3.75408   6.88011   -52.52873 1.000 30.46641 ?  176 LEU   A N   1 
ATOM   725  C  CA  . LEU   A 1 99  ? 4.49980   6.15252   -53.54704 1.000 29.73379 ?  176 LEU   A CA  1 
ATOM   726  C  C   . LEU   A 1 99  ? 4.93458   4.77312   -53.06960 1.000 28.63626 ?  176 LEU   A C   1 
ATOM   727  O  O   . LEU   A 1 99  ? 5.87167   4.19530   -53.62763 1.000 27.69438 ?  176 LEU   A O   1 
ATOM   728  C  CB  . LEU   A 1 99  ? 5.71975   6.96367   -53.99341 1.000 27.51278 ?  176 LEU   A CB  1 
ATOM   729  C  CG  . LEU   A 1 99  ? 5.46420   8.19924   -54.87046 1.000 30.55215 ?  176 LEU   A CG  1 
ATOM   730  C  CD1 . LEU   A 1 99  ? 6.63857   9.19438   -54.82570 1.000 26.99534 ?  176 LEU   A CD1 1 
ATOM   731  C  CD2 . LEU   A 1 99  ? 5.21102   7.77686   -56.30633 1.000 28.89178 ?  176 LEU   A CD2 1 
ATOM   732  N  N   . ARG   A 1 100 ? 4.28350   4.21847   -52.05725 1.000 29.77167 ?  177 ARG   A N   1 
ATOM   733  C  CA  . ARG   A 1 100 ? 4.82089   2.95601   -51.57579 1.000 33.10214 ?  177 ARG   A CA  1 
ATOM   734  C  C   . ARG   A 1 100 ? 4.42413   1.80746   -52.50529 1.000 32.09099 ?  177 ARG   A C   1 
ATOM   735  O  O   . ARG   A 1 100 ? 3.53064   1.92836   -53.34568 1.000 32.21828 ?  177 ARG   A O   1 
ATOM   736  C  CB  . ARG   A 1 100 ? 4.38964   2.69203   -50.12664 1.000 34.00835 ?  177 ARG   A CB  1 
ATOM   737  C  CG  . ARG   A 1 100 ? 2.94543   2.82092   -49.88855 1.000 35.27699 ?  177 ARG   A CG  1 
ATOM   738  C  CD  . ARG   A 1 100 ? 2.60299   3.20014   -48.46374 1.000 28.58450 ?  177 ARG   A CD  1 
ATOM   739  N  NE  . ARG   A 1 100 ? 1.23046   3.66659   -48.53220 1.000 34.31139 ?  177 ARG   A NE  1 
ATOM   740  C  CZ  . ARG   A 1 100 ? 0.16090   2.93405   -48.26755 1.000 36.01699 ?  177 ARG   A CZ  1 
ATOM   741  N  NH1 . ARG   A 1 100 ? 0.25831   1.75424   -47.68696 1.000 42.58624 ?  177 ARG   A NH1 1 
ATOM   742  N  NH2 . ARG   A 1 100 ? -1.03924  3.40044   -48.59506 1.000 37.29000 ?  177 ARG   A NH2 1 
ATOM   743  N  N   . HIS   A 1 101 ? 5.14197   0.69433   -52.37031 1.000 33.05280 ?  178 HIS   A N   1 
ATOM   744  C  CA  . HIS   A 1 101 ? 4.95634   -0.48156  -53.21175 1.000 33.00558 ?  178 HIS   A CA  1 
ATOM   745  C  C   . HIS   A 1 101 ? 5.01140   -0.09785  -54.68789 1.000 29.67137 ?  178 HIS   A C   1 
ATOM   746  O  O   . HIS   A 1 101 ? 4.08313   -0.33378  -55.46099 1.000 30.06598 ?  178 HIS   A O   1 
ATOM   747  C  CB  . HIS   A 1 101 ? 3.64995   -1.20543  -52.88265 1.000 32.06376 ?  178 HIS   A CB  1 
ATOM   748  C  CG  . HIS   A 1 101 ? 3.69981   -1.99653  -51.61757 1.000 42.84654 ?  178 HIS   A CG  1 
ATOM   749  N  ND1 . HIS   A 1 101 ? 3.65808   -1.40989  -50.36943 1.000 48.32706 ?  178 HIS   A ND1 1 
ATOM   750  C  CD2 . HIS   A 1 101 ? 3.77942   -3.33295  -51.40298 1.000 47.55761 ?  178 HIS   A CD2 1 
ATOM   751  C  CE1 . HIS   A 1 101 ? 3.71128   -2.35006  -49.44042 1.000 47.87165 ?  178 HIS   A CE1 1 
ATOM   752  N  NE2 . HIS   A 1 101 ? 3.78462   -3.52560  -50.04132 1.000 49.39290 ?  178 HIS   A NE2 1 
ATOM   753  N  N   . ASN   A 1 102 ? 6.12622   0.51839   -55.05782 1.000 27.77573 ?  179 ASN   A N   1 
ATOM   754  C  CA  . ASN   A 1 102 ? 6.46081   0.75945   -56.45293 1.000 28.92105 ?  179 ASN   A CA  1 
ATOM   755  C  C   . ASN   A 1 102 ? 7.84886   0.16700   -56.66570 1.000 28.68277 ?  179 ASN   A C   1 
ATOM   756  O  O   . ASN   A 1 102 ? 8.32741   -0.67176  -55.89705 1.000 29.39451 ?  179 ASN   A O   1 
ATOM   757  C  CB  . ASN   A 1 102 ? 6.39159   2.25345   -56.80794 1.000 29.54254 ?  179 ASN   A CB  1 
ATOM   758  C  CG  . ASN   A 1 102 ? 5.00615   2.68328   -57.26875 1.000 31.24165 ?  179 ASN   A CG  1 
ATOM   759  O  OD1 . ASN   A 1 102 ? 4.69311   2.64096   -58.47028 1.000 30.97887 ?  179 ASN   A OD1 1 
ATOM   760  N  ND2 . ASN   A 1 102 ? 4.16809   3.10359   -56.32036 1.000 27.59519 ?  179 ASN   A ND2 1 
ATOM   761  N  N   . LYS   A 1 103 ? 8.53066   0.62657   -57.70590 1.000 28.82818 ?  180 LYS   A N   1 
ATOM   762  C  CA  . LYS   A 1 103 ? 9.85791   0.11834   -58.01362 1.000 30.24411 ?  180 LYS   A CA  1 
ATOM   763  C  C   . LYS   A 1 103 ? 10.87376  1.26276   -58.08694 1.000 29.02401 ?  180 LYS   A C   1 
ATOM   764  O  O   . LYS   A 1 103 ? 11.68738  1.33843   -59.01469 1.000 30.65933 ?  180 LYS   A O   1 
ATOM   765  C  CB  . LYS   A 1 103 ? 9.78610   -0.69160  -59.31439 1.000 31.41940 ?  180 LYS   A CB  1 
ATOM   766  C  CG  . LYS   A 1 103 ? 8.82920   -1.88487  -59.21989 1.000 31.29138 ?  180 LYS   A CG  1 
ATOM   767  C  CD  . LYS   A 1 103 ? 8.58831   -2.57013  -60.56992 1.000 37.80429 ?  180 LYS   A CD  1 
ATOM   768  C  CE  . LYS   A 1 103 ? 7.62125   -3.77137  -60.41982 1.000 48.85509 ?  180 LYS   A CE  1 
ATOM   769  N  NZ  . LYS   A 1 103 ? 7.31789   -4.52296  -61.68912 1.000 43.76588 ?  180 LYS   A NZ  1 
ATOM   770  N  N   . LEU   A 1 104 ? 10.84071  2.15312   -57.09977 1.000 30.36903 ?  181 LEU   A N   1 
ATOM   771  C  CA  . LEU   A 1 104 ? 11.72801  3.31138   -57.08616 1.000 31.75463 ?  181 LEU   A CA  1 
ATOM   772  C  C   . LEU   A 1 104 ? 13.11788  2.91220   -56.61770 1.000 31.45181 ?  181 LEU   A C   1 
ATOM   773  O  O   . LEU   A 1 104 ? 13.27032  2.29907   -55.55974 1.000 33.03867 ?  181 LEU   A O   1 
ATOM   774  C  CB  . LEU   A 1 104 ? 11.17462  4.39454   -56.16153 1.000 30.56392 ?  181 LEU   A CB  1 
ATOM   775  C  CG  . LEU   A 1 104 ? 9.77590   4.93610   -56.42445 1.000 27.68819 ?  181 LEU   A CG  1 
ATOM   776  C  CD1 . LEU   A 1 104 ? 9.34738   5.70604   -55.22070 1.000 30.45382 ?  181 LEU   A CD1 1 
ATOM   777  C  CD2 . LEU   A 1 104 ? 9.79875   5.84075   -57.64444 1.000 28.58684 ?  181 LEU   A CD2 1 
ATOM   778  N  N   . ARG   A 1 105 ? 14.13192  3.27273   -57.38527 1.000 33.51532 ?  182 ARG   A N   1 
ATOM   779  C  CA  . ARG   A 1 105 ? 15.49834  3.12526   -56.91179 1.000 34.49702 ?  182 ARG   A CA  1 
ATOM   780  C  C   . ARG   A 1 105 ? 15.98621  4.37422   -56.19734 1.000 36.10730 ?  182 ARG   A C   1 
ATOM   781  O  O   . ARG   A 1 105 ? 17.14662  4.42066   -55.76553 1.000 34.91046 ?  182 ARG   A O   1 
ATOM   782  C  CB  . ARG   A 1 105 ? 16.42632  2.76337   -58.07319 1.000 34.54404 ?  182 ARG   A CB  1 
ATOM   783  C  CG  . ARG   A 1 105 ? 16.25182  1.31930   -58.51268 1.000 40.94910 ?  182 ARG   A CG  1 
ATOM   784  C  CD  . ARG   A 1 105 ? 17.04155  1.00876   -59.75798 1.000 45.54041 ?  182 ARG   A CD  1 
ATOM   785  N  NE  . ARG   A 1 105 ? 16.48808  1.71437   -60.90845 1.000 50.62351 ?  182 ARG   A NE  1 
ATOM   786  C  CZ  . ARG   A 1 105 ? 15.28597  1.47256   -61.42015 1.000 53.40710 ?  182 ARG   A CZ  1 
ATOM   787  N  NH1 . ARG   A 1 105 ? 14.46027  0.58829   -60.86782 1.000 56.92907 ?  182 ARG   A NH1 1 
ATOM   788  N  NH2 . ARG   A 1 105 ? 14.89794  2.13340   -62.50748 1.000 43.21481 ?  182 ARG   A NH2 1 
ATOM   789  N  N   . GLU   A 1 106 ? 15.10965  5.36572   -56.03088 1.000 35.76835 ?  183 GLU   A N   1 
ATOM   790  C  CA  . GLU   A 1 106 ? 15.45437  6.66465   -55.47072 1.000 31.86084 ?  183 GLU   A CA  1 
ATOM   791  C  C   . GLU   A 1 106 ? 14.17389  7.46254   -55.34282 1.000 32.26866 ?  183 GLU   A C   1 
ATOM   792  O  O   . GLU   A 1 106 ? 13.14700  7.12273   -55.94127 1.000 31.74928 ?  183 GLU   A O   1 
ATOM   793  C  CB  . GLU   A 1 106 ? 16.42481  7.42509   -56.35947 1.000 32.30227 ?  183 GLU   A CB  1 
ATOM   794  C  CG  . GLU   A 1 106 ? 15.72145  7.97845   -57.57694 1.000 34.02881 ?  183 GLU   A CG  1 
ATOM   795  C  CD  . GLU   A 1 106 ? 16.68026  8.43315   -58.64965 1.000 40.11336 ?  183 GLU   A CD  1 
ATOM   796  O  OE1 . GLU   A 1 106 ? 17.90358  8.22823   -58.46250 1.000 46.72125 ?  183 GLU   A OE1 1 
ATOM   797  O  OE2 . GLU   A 1 106 ? 16.21090  8.98104   -59.67844 1.000 38.80863 ?  183 GLU   A OE2 1 
ATOM   798  N  N   . ILE   A 1 107 ? 14.25353  8.54222   -54.57312 1.000 32.07940 ?  184 ILE   A N   1 
ATOM   799  C  CA  . ILE   A 1 107 ? 13.19065  9.53696   -54.54893 1.000 29.57345 ?  184 ILE   A CA  1 
ATOM   800  C  C   . ILE   A 1 107 ? 13.29972  10.31914  -55.84850 1.000 29.14595 ?  184 ILE   A C   1 
ATOM   801  O  O   . ILE   A 1 107 ? 14.35668  10.88769  -56.13713 1.000 27.59899 ?  184 ILE   A O   1 
ATOM   802  C  CB  . ILE   A 1 107 ? 13.30481  10.43752  -53.31678 1.000 28.88229 ?  184 ILE   A CB  1 
ATOM   803  C  CG1 . ILE   A 1 107 ? 13.23034  9.56150   -52.06329 1.000 30.69609 ?  184 ILE   A CG1 1 
ATOM   804  C  CG2 . ILE   A 1 107 ? 12.23930  11.50884  -53.34376 1.000 24.34339 ?  184 ILE   A CG2 1 
ATOM   805  C  CD1 . ILE   A 1 107 ? 13.43137  10.28193  -50.74997 1.000 31.05771 ?  184 ILE   A CD1 1 
ATOM   806  N  N   . PRO   A 1 108 ? 12.27480  10.32232  -56.68960 1.000 30.23670 ?  185 PRO   A N   1 
ATOM   807  C  CA  . PRO   A 1 108 ? 12.36990  11.08467  -57.93811 1.000 28.56962 ?  185 PRO   A CA  1 
ATOM   808  C  C   . PRO   A 1 108 ? 12.74423  12.52607  -57.63215 1.000 31.61559 ?  185 PRO   A C   1 
ATOM   809  O  O   . PRO   A 1 108 ? 12.26382  13.11866  -56.66259 1.000 29.67705 ?  185 PRO   A O   1 
ATOM   810  C  CB  . PRO   A 1 108 ? 10.96624  10.96513  -58.53700 1.000 27.78227 ?  185 PRO   A CB  1 
ATOM   811  C  CG  . PRO   A 1 108 ? 10.44315  9.64079   -57.98607 1.000 28.65346 ?  185 PRO   A CG  1 
ATOM   812  C  CD  . PRO   A 1 108 ? 11.01461  9.55908   -56.57775 1.000 27.72230 ?  185 PRO   A CD  1 
ATOM   813  N  N   . SER   A 1 109 ? 13.62417  13.09601  -58.45910 1.000 30.41079 ?  186 SER   A N   1 
ATOM   814  C  CA  . SER   A 1 109 ? 14.20055  14.38468  -58.09034 1.000 33.12594 ?  186 SER   A CA  1 
ATOM   815  C  C   . SER   A 1 109 ? 13.14931  15.49270  -58.03570 1.000 33.07311 ?  186 SER   A C   1 
ATOM   816  O  O   . SER   A 1 109 ? 13.33149  16.47359  -57.30779 1.000 33.91061 ?  186 SER   A O   1 
ATOM   817  C  CB  . SER   A 1 109 ? 15.32672  14.76441  -59.04840 1.000 28.29063 ?  186 SER   A CB  1 
ATOM   818  O  OG  . SER   A 1 109 ? 14.80365  14.98677  -60.32503 1.000 36.22185 ?  186 SER   A OG  1 
ATOM   819  N  N   . VAL   A 1 110 ? 12.04797  15.36677  -58.78157 1.000 33.47909 ?  187 VAL   A N   1 
ATOM   820  C  CA  . VAL   A 1 110 ? 11.00042  16.38554  -58.68528 1.000 32.52050 ?  187 VAL   A CA  1 
ATOM   821  C  C   . VAL   A 1 110 ? 10.39518  16.41104  -57.29714 1.000 30.15754 ?  187 VAL   A C   1 
ATOM   822  O  O   . VAL   A 1 110 ? 9.96388   17.46982  -56.82494 1.000 30.47810 ?  187 VAL   A O   1 
ATOM   823  C  CB  . VAL   A 1 110 ? 9.89346   16.16567  -59.73011 1.000 34.32925 ?  187 VAL   A CB  1 
ATOM   824  C  CG1 . VAL   A 1 110 ? 9.14437   14.87773  -59.44337 1.000 26.81463 ?  187 VAL   A CG1 1 
ATOM   825  C  CG2 . VAL   A 1 110 ? 8.93782   17.35465  -59.71847 1.000 33.53461 ?  187 VAL   A CG2 1 
ATOM   826  N  N   . VAL   A 1 111 ? 10.33645  15.25642  -56.62442 1.000 26.84788 ?  188 VAL   A N   1 
ATOM   827  C  CA  . VAL   A 1 111 ? 9.69809   15.20042  -55.31335 1.000 27.04996 ?  188 VAL   A CA  1 
ATOM   828  C  C   . VAL   A 1 111 ? 10.37849  16.16131  -54.35047 1.000 28.08167 ?  188 VAL   A C   1 
ATOM   829  O  O   . VAL   A 1 111 ? 9.71401   16.76220  -53.49459 1.000 26.92342 ?  188 VAL   A O   1 
ATOM   830  C  CB  . VAL   A 1 111 ? 9.67510   13.75458  -54.76863 1.000 26.96209 ?  188 VAL   A CB  1 
ATOM   831  C  CG1 . VAL   A 1 111 ? 9.28889   13.73699  -53.31069 1.000 27.47531 ?  188 VAL   A CG1 1 
ATOM   832  C  CG2 . VAL   A 1 111 ? 8.68601   12.90717  -55.53785 1.000 25.25500 ?  188 VAL   A CG2 1 
ATOM   833  N  N   . TYR   A 1 112 ? 11.69813  16.35172  -54.48862 1.000 28.38858 ?  189 TYR   A N   1 
ATOM   834  C  CA  . TYR   A 1 112 ? 12.43704  17.29583  -53.65040 1.000 30.60389 ?  189 TYR   A CA  1 
ATOM   835  C  C   . TYR   A 1 112 ? 12.11418  18.75671  -53.94774 1.000 30.12979 ?  189 TYR   A C   1 
ATOM   836  O  O   . TYR   A 1 112 ? 12.63433  19.63417  -53.25064 1.000 28.69579 ?  189 TYR   A O   1 
ATOM   837  C  CB  . TYR   A 1 112 ? 13.94844  17.12259  -53.80538 1.000 33.31998 ?  189 TYR   A CB  1 
ATOM   838  C  CG  . TYR   A 1 112 ? 14.54795  15.81311  -53.33940 1.000 30.07751 ?  189 TYR   A CG  1 
ATOM   839  C  CD1 . TYR   A 1 112 ? 14.82116  15.58375  -51.99896 1.000 32.33581 ?  189 TYR   A CD1 1 
ATOM   840  C  CD2 . TYR   A 1 112 ? 14.90314  14.83065  -54.25627 1.000 30.45843 ?  189 TYR   A CD2 1 
ATOM   841  C  CE1 . TYR   A 1 112 ? 15.40445  14.38542  -51.57592 1.000 31.66547 ?  189 TYR   A CE1 1 
ATOM   842  C  CE2 . TYR   A 1 112 ? 15.49607  13.64359  -53.85304 1.000 30.60764 ?  189 TYR   A CE2 1 
ATOM   843  C  CZ  . TYR   A 1 112 ? 15.74384  13.42444  -52.51272 1.000 33.23252 ?  189 TYR   A CZ  1 
ATOM   844  O  OH  . TYR   A 1 112 ? 16.31113  12.23783  -52.12069 1.000 32.50080 ?  189 TYR   A OH  1 
ATOM   845  N  N   . ARG   A 1 113 ? 11.30742  19.04345  -54.96795 1.000 31.73107 ?  190 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 113 ? 10.83762  20.39820  -55.23818 1.000 30.74363 ?  190 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 113 ? 9.38188   20.60603  -54.83950 1.000 31.05074 ?  190 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 113 ? 8.86457   21.71529  -54.99922 1.000 31.58652 ?  190 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 113 ? 11.01632  20.75218  -56.72655 1.000 30.64624 ?  190 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 113 ? 12.44008  20.63630  -57.21868 1.000 32.36116 ?  190 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 113 ? 12.63535  21.37004  -58.50333 1.000 34.92316 ?  190 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 113 ? 11.94379  20.73504  -59.61326 1.000 38.84094 ?  190 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 113 ? 12.40283  19.67266  -60.25742 1.000 41.19489 ?  190 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 113 ? 13.54902  19.10352  -59.91482 1.000 37.77811 ?  190 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 113 ? 11.69443  19.16807  -61.26750 1.000 39.56646 ?  190 ARG   A NH2 1 
ATOM   856  N  N   . LEU   A 1 114 ? 8.71182   19.57981  -54.31622 1.000 29.68842 ?  191 LEU   A N   1 
ATOM   857  C  CA  . LEU   A 1 114 ? 7.32339   19.71765  -53.86525 1.000 31.15270 ?  191 LEU   A CA  1 
ATOM   858  C  C   . LEU   A 1 114 ? 7.29729   20.19941  -52.40949 1.000 34.28204 ?  191 LEU   A C   1 
ATOM   859  O  O   . LEU   A 1 114 ? 6.94614   19.47021  -51.47031 1.000 34.53253 ?  191 LEU   A O   1 
ATOM   860  C  CB  . LEU   A 1 114 ? 6.58225   18.40176  -54.04473 1.000 26.21867 ?  191 LEU   A CB  1 
ATOM   861  C  CG  . LEU   A 1 114 ? 6.75353   17.84932  -55.46317 1.000 34.34080 ?  191 LEU   A CG  1 
ATOM   862  C  CD1 . LEU   A 1 114 ? 6.13710   16.48731  -55.60803 1.000 29.84905 ?  191 LEU   A CD1 1 
ATOM   863  C  CD2 . LEU   A 1 114 ? 6.16293   18.82719  -56.51059 1.000 36.48264 ?  191 LEU   A CD2 1 
ATOM   864  N  N   . ASP   A 1 115 ? 7.67476   21.46929  -52.23126 1.000 28.27901 ?  192 ASP   A N   1 
ATOM   865  C  CA  . ASP   A 1 115 ? 7.94613   21.96902  -50.88321 1.000 36.26957 ?  192 ASP   A CA  1 
ATOM   866  C  C   . ASP   A 1 115 ? 6.68434   22.31166  -50.09070 1.000 36.50199 ?  192 ASP   A C   1 
ATOM   867  O  O   . ASP   A 1 115 ? 6.79498   22.82103  -48.97198 1.000 36.15197 ?  192 ASP   A O   1 
ATOM   868  C  CB  . ASP   A 1 115 ? 8.87209   23.18820  -50.93360 1.000 33.85976 ?  192 ASP   A CB  1 
ATOM   869  C  CG  . ASP   A 1 115 ? 8.21137   24.39576  -51.53290 1.000 40.23493 ?  192 ASP   A CG  1 
ATOM   870  O  OD1 . ASP   A 1 115 ? 7.33886   24.98484  -50.85822 1.000 46.97236 ?  192 ASP   A OD1 1 
ATOM   871  O  OD2 . ASP   A 1 115 ? 8.56513   24.76445  -52.67835 1.000 45.50737 ?  192 ASP   A OD2 1 
ATOM   872  N  N   . SER   A 1 116 ? 5.50156   22.05070  -50.63202 1.000 32.68642 ?  193 SER   A N   1 
ATOM   873  C  CA  . SER   A 1 116 ? 4.28216   22.10006  -49.84855 1.000 34.03151 ?  193 SER   A CA  1 
ATOM   874  C  C   . SER   A 1 116 ? 3.94292   20.75679  -49.19313 1.000 32.14251 ?  193 SER   A C   1 
ATOM   875  O  O   . SER   A 1 116 ? 3.03748   20.70765  -48.35359 1.000 34.23090 ?  193 SER   A O   1 
ATOM   876  C  CB  . SER   A 1 116 ? 3.11918   22.57878  -50.73423 1.000 31.86920 ?  193 SER   A CB  1 
ATOM   877  O  OG  . SER   A 1 116 ? 2.98535   21.77757  -51.90524 1.000 38.44175 ?  193 SER   A OG  1 
ATOM   878  N  N   . LEU   A 1 117 ? 4.65484   19.67851  -49.53080 1.000 32.56769 ?  194 LEU   A N   1 
ATOM   879  C  CA  . LEU   A 1 117 ? 4.35311   18.36735  -48.96186 1.000 33.32724 ?  194 LEU   A CA  1 
ATOM   880  C  C   . LEU   A 1 117 ? 4.44745   18.37883  -47.44374 1.000 33.09034 ?  194 LEU   A C   1 
ATOM   881  O  O   . LEU   A 1 117 ? 5.38138   18.94208  -46.86100 1.000 30.80120 ?  194 LEU   A O   1 
ATOM   882  C  CB  . LEU   A 1 117 ? 5.30639   17.30743  -49.49514 1.000 31.54873 ?  194 LEU   A CB  1 
ATOM   883  C  CG  . LEU   A 1 117 ? 5.11398   16.74399  -50.89079 1.000 32.28231 ?  194 LEU   A CG  1 
ATOM   884  C  CD1 . LEU   A 1 117 ? 6.21306   15.75188  -51.10772 1.000 32.52911 ?  194 LEU   A CD1 1 
ATOM   885  C  CD2 . LEU   A 1 117 ? 3.75992   16.06297  -51.02666 1.000 32.50316 ?  194 LEU   A CD2 1 
ATOM   886  N  N   . THR   A 1 118 ? 3.46624   17.73988  -46.80845 1.000 31.69784 ?  195 THR   A N   1 
ATOM   887  C  CA  . THR   A 1 118 ? 3.51651   17.42519  -45.38995 1.000 32.79421 ?  195 THR   A CA  1 
ATOM   888  C  C   . THR   A 1 118 ? 3.46206   15.92562  -45.10942 1.000 32.99031 ?  195 THR   A C   1 
ATOM   889  O  O   . THR   A 1 118 ? 3.65178   15.52210  -43.95742 1.000 29.93094 ?  195 THR   A O   1 
ATOM   890  C  CB  . THR   A 1 118 ? 2.37077   18.12246  -44.64327 1.000 33.34197 ?  195 THR   A CB  1 
ATOM   891  O  OG1 . THR   A 1 118 ? 1.12308   17.75446  -45.24049 1.000 37.64261 ?  195 THR   A OG1 1 
ATOM   892  C  CG2 . THR   A 1 118 ? 2.52522   19.63260  -44.71686 1.000 30.03782 ?  195 THR   A CG2 1 
ATOM   893  N  N   . THR   A 1 119 ? 3.24992   15.09237  -46.12615 1.000 31.26667 ?  196 THR   A N   1 
ATOM   894  C  CA  . THR   A 1 119 ? 3.12931   13.65362  -45.92649 1.000 34.06414 ?  196 THR   A CA  1 
ATOM   895  C  C   . THR   A 1 119 ? 3.71022   12.93551  -47.13092 1.000 32.89355 ?  196 THR   A C   1 
ATOM   896  O  O   . THR   A 1 119 ? 3.16898   13.04209  -48.23248 1.000 32.10267 ?  196 THR   A O   1 
ATOM   897  C  CB  . THR   A 1 119 ? 1.66787   13.25343  -45.72577 1.000 35.43789 ?  196 THR   A CB  1 
ATOM   898  O  OG1 . THR   A 1 119 ? 1.12057   14.01080  -44.64420 1.000 38.95311 ?  196 THR   A OG1 1 
ATOM   899  C  CG2 . THR   A 1 119 ? 1.55995   11.77868  -45.40684 1.000 35.19926 ?  196 THR   A CG2 1 
ATOM   900  N  N   . LEU   A 1 120 ? 4.78674   12.18501  -46.91429 1.000 34.60837 ?  197 LEU   A N   1 
ATOM   901  C  CA  . LEU   A 1 120 ? 5.47240   11.46691  -47.97875 1.000 30.55648 ?  197 LEU   A CA  1 
ATOM   902  C  C   . LEU   A 1 120 ? 5.63893   10.01119  -47.55874 1.000 32.12243 ?  197 LEU   A C   1 
ATOM   903  O  O   . LEU   A 1 120 ? 6.31303   9.72572   -46.56075 1.000 29.56184 ?  197 LEU   A O   1 
ATOM   904  C  CB  . LEU   A 1 120 ? 6.82487   12.11244  -48.27256 1.000 27.20329 ?  197 LEU   A CB  1 
ATOM   905  C  CG  . LEU   A 1 120 ? 7.56909   11.52719  -49.45924 1.000 29.66067 ?  197 LEU   A CG  1 
ATOM   906  C  CD1 . LEU   A 1 120 ? 6.68081   11.56329  -50.67461 1.000 27.84147 ?  197 LEU   A CD1 1 
ATOM   907  C  CD2 . LEU   A 1 120 ? 8.87029   12.28334  -49.70283 1.000 26.52919 ?  197 LEU   A CD2 1 
ATOM   908  N  N   . TYR   A 1 121 ? 5.01855   9.09525   -48.32191 1.000 30.38111 ?  198 TYR   A N   1 
ATOM   909  C  CA  . TYR   A 1 121 ? 5.04764   7.65689   -48.05801 1.000 29.48809 ?  198 TYR   A CA  1 
ATOM   910  C  C   . TYR   A 1 121 ? 5.84797   6.96867   -49.15018 1.000 28.06140 ?  198 TYR   A C   1 
ATOM   911  O  O   . TYR   A 1 121 ? 5.41340   6.93355   -50.30389 1.000 31.45160 ?  198 TYR   A O   1 
ATOM   912  C  CB  . TYR   A 1 121 ? 3.64285   7.06684   -48.01548 1.000 29.99892 ?  198 TYR   A CB  1 
ATOM   913  C  CG  . TYR   A 1 121 ? 2.75063   7.61117   -46.93408 1.000 36.62181 ?  198 TYR   A CG  1 
ATOM   914  C  CD1 . TYR   A 1 121 ? 3.00009   7.32377   -45.59933 1.000 34.57914 ?  198 TYR   A CD1 1 
ATOM   915  C  CD2 . TYR   A 1 121 ? 1.64352   8.40632   -47.24594 1.000 34.51486 ?  198 TYR   A CD2 1 
ATOM   916  C  CE1 . TYR   A 1 121 ? 2.18469   7.81362   -44.60346 1.000 36.04502 ?  198 TYR   A CE1 1 
ATOM   917  C  CE2 . TYR   A 1 121 ? 0.81750   8.90067   -46.24797 1.000 36.09947 ?  198 TYR   A CE2 1 
ATOM   918  C  CZ  . TYR   A 1 121 ? 1.09743   8.59445   -44.92523 1.000 37.20813 ?  198 TYR   A CZ  1 
ATOM   919  O  OH  . TYR   A 1 121 ? 0.29822   9.05755   -43.90775 1.000 39.13133 ?  198 TYR   A OH  1 
ATOM   920  N  N   . LEU   A 1 122 ? 6.98644   6.37745   -48.78285 1.000 25.63597 ?  199 LEU   A N   1 
ATOM   921  C  CA  . LEU   A 1 122 ? 7.82487   5.66736   -49.74036 1.000 29.25223 ?  199 LEU   A CA  1 
ATOM   922  C  C   . LEU   A 1 122 ? 8.07467   4.21609   -49.34098 1.000 29.51098 ?  199 LEU   A C   1 
ATOM   923  O  O   . LEU   A 1 122 ? 9.01610   3.59568   -49.84271 1.000 27.92405 ?  199 LEU   A O   1 
ATOM   924  C  CB  . LEU   A 1 122 ? 9.14733   6.40884   -49.92019 1.000 25.95657 ?  199 LEU   A CB  1 
ATOM   925  C  CG  . LEU   A 1 122 ? 8.90667   7.84195   -50.39573 1.000 26.91944 ?  199 LEU   A CG  1 
ATOM   926  C  CD1 . LEU   A 1 122 ? 9.89533   8.80505   -49.74516 1.000 27.98244 ?  199 LEU   A CD1 1 
ATOM   927  C  CD2 . LEU   A 1 122 ? 8.97938   7.93547   -51.88687 1.000 27.99329 ?  199 LEU   A CD2 1 
ATOM   928  N  N   . ARG   A 1 123 ? 7.25354   3.65959   -48.45439 1.000 28.64712 ?  200 ARG   A N   1 
ATOM   929  C  CA  . ARG   A 1 123 ? 7.50693   2.31912   -47.95408 1.000 31.19139 ?  200 ARG   A CA  1 
ATOM   930  C  C   . ARG   A 1 123 ? 7.57911   1.31370   -49.10489 1.000 32.16162 ?  200 ARG   A C   1 
ATOM   931  O  O   . ARG   A 1 123 ? 6.88551   1.43737   -50.11452 1.000 32.50722 ?  200 ARG   A O   1 
ATOM   932  C  CB  . ARG   A 1 123 ? 6.41637   1.90760   -46.95756 1.000 33.19771 ?  200 ARG   A CB  1 
ATOM   933  C  CG  . ARG   A 1 123 ? 6.55224   0.47564   -46.44007 1.000 37.40936 ?  200 ARG   A CG  1 
ATOM   934  C  CD  . ARG   A 1 123 ? 5.26789   0.01988   -45.76141 1.000 43.08142 ?  200 ARG   A CD  1 
ATOM   935  N  NE  . ARG   A 1 123 ? 5.37876   -1.31979  -45.19624 1.000 44.57857 ?  200 ARG   A NE  1 
ATOM   936  C  CZ  . ARG   A 1 123 ? 4.78432   -1.69718  -44.07085 1.000 46.46958 ?  200 ARG   A CZ  1 
ATOM   937  N  NH1 . ARG   A 1 123 ? 4.05924   -0.85247  -43.35226 1.000 46.83164 ?  200 ARG   A NH1 1 
ATOM   938  N  NH2 . ARG   A 1 123 ? 4.91220   -2.95257  -43.65832 1.000 44.21977 ?  200 ARG   A NH2 1 
ATOM   939  N  N   . PHE   A 1 124 ? 8.44531   0.31467   -48.94118 1.000 29.50255 ?  201 PHE   A N   1 
ATOM   940  C  CA  . PHE   A 1 124 ? 8.56842   -0.82947  -49.84257 1.000 30.72030 ?  201 PHE   A CA  1 
ATOM   941  C  C   . PHE   A 1 124 ? 8.91905   -0.37482  -51.26220 1.000 30.65016 ?  201 PHE   A C   1 
ATOM   942  O  O   . PHE   A 1 124 ? 8.12283   -0.44269  -52.19725 1.000 30.89857 ?  201 PHE   A O   1 
ATOM   943  C  CB  . PHE   A 1 124 ? 7.29959   -1.69439  -49.82911 1.000 34.65240 ?  201 PHE   A CB  1 
ATOM   944  C  CG  . PHE   A 1 124 ? 7.54458   -3.12429  -50.25565 1.000 36.12086 ?  201 PHE   A CG  1 
ATOM   945  C  CD1 . PHE   A 1 124 ? 7.93285   -4.08271  -49.33290 1.000 36.69986 ?  201 PHE   A CD1 1 
ATOM   946  C  CD2 . PHE   A 1 124 ? 7.41805   -3.50554  -51.58419 1.000 36.49357 ?  201 PHE   A CD2 1 
ATOM   947  C  CE1 . PHE   A 1 124 ? 8.18765   -5.39487  -49.73386 1.000 33.95974 ?  201 PHE   A CE1 1 
ATOM   948  C  CE2 . PHE   A 1 124 ? 7.66289   -4.81855  -51.98848 1.000 33.16945 ?  201 PHE   A CE2 1 
ATOM   949  C  CZ  . PHE   A 1 124 ? 8.04851   -5.75783  -51.06297 1.000 33.09711 ?  201 PHE   A CZ  1 
ATOM   950  N  N   . ASN   A 1 125 ? 10.15939  0.07484   -51.38851 1.000 29.05758 ?  202 ASN   A N   1 
ATOM   951  C  CA  . ASN   A 1 125 ? 10.76026  0.40012   -52.67139 1.000 27.51930 ?  202 ASN   A CA  1 
ATOM   952  C  C   . ASN   A 1 125 ? 12.19661  -0.10587  -52.61092 1.000 32.12240 ?  202 ASN   A C   1 
ATOM   953  O  O   . ASN   A 1 125 ? 12.55856  -0.91215  -51.74643 1.000 32.79203 ?  202 ASN   A O   1 
ATOM   954  C  CB  . ASN   A 1 125 ? 10.64723  1.91136   -52.95555 1.000 31.34778 ?  202 ASN   A CB  1 
ATOM   955  C  CG  . ASN   A 1 125 ? 9.29282   2.30177   -53.57706 1.000 31.89482 ?  202 ASN   A CG  1 
ATOM   956  O  OD1 . ASN   A 1 125 ? 8.99887   1.95991   -54.72444 1.000 28.74976 ?  202 ASN   A OD1 1 
ATOM   957  N  ND2 . ASN   A 1 125 ? 8.47565   3.02189   -52.81768 1.000 30.48689 ?  202 ASN   A ND2 1 
ATOM   958  N  N   . ARG   A 1 126 ? 13.04357  0.36993   -53.51019 1.000 30.24582 ?  203 ARG   A N   1 
ATOM   959  C  CA  . ARG   A 1 126 ? 14.45642  0.02112   -53.49211 1.000 33.33247 ?  203 ARG   A CA  1 
ATOM   960  C  C   . ARG   A 1 126 ? 15.31433  1.27515   -53.39174 1.000 32.00964 ?  203 ARG   A C   1 
ATOM   961  O  O   . ARG   A 1 126 ? 16.39476  1.36260   -53.96975 1.000 33.38871 ?  203 ARG   A O   1 
ATOM   962  C  CB  . ARG   A 1 126 ? 14.81946  -0.80517  -54.72433 1.000 37.74436 ?  203 ARG   A CB  1 
ATOM   963  C  CG  . ARG   A 1 126 ? 13.93361  -2.04378  -54.89745 1.000 47.48903 ?  203 ARG   A CG  1 
ATOM   964  C  CD  . ARG   A 1 126 ? 14.17397  -2.77911  -56.22790 1.000 59.37995 ?  203 ARG   A CD  1 
ATOM   965  N  NE  . ARG   A 1 126 ? 15.56954  -3.18201  -56.40275 1.000 61.91449 ?  203 ARG   A NE  1 
ATOM   966  C  CZ  . ARG   A 1 126 ? 16.15035  -4.18825  -55.76037 1.000 58.73690 ?  203 ARG   A CZ  1 
ATOM   967  N  NH1 . ARG   A 1 126 ? 15.48560  -4.92882  -54.88627 1.000 53.75386 ?  203 ARG   A NH1 1 
ATOM   968  N  NH2 . ARG   A 1 126 ? 17.43466  -4.44939  -55.99170 1.000 59.94826 ?  203 ARG   A NH2 1 
ATOM   969  N  N   . ILE   A 1 127 ? 14.83887  2.26504   -52.64020 1.000 33.12579 ?  204 ILE   A N   1 
ATOM   970  C  CA  . ILE   A 1 127 ? 15.52484  3.54936   -52.56066 1.000 30.94763 ?  204 ILE   A CA  1 
ATOM   971  C  C   . ILE   A 1 127 ? 16.82580  3.38362   -51.78971 1.000 32.63248 ?  204 ILE   A C   1 
ATOM   972  O  O   . ILE   A 1 127 ? 16.84891  2.81820   -50.68590 1.000 30.24305 ?  204 ILE   A O   1 
ATOM   973  C  CB  . ILE   A 1 127 ? 14.61127  4.59593   -51.90699 1.000 31.82924 ?  204 ILE   A CB  1 
ATOM   974  C  CG1 . ILE   A 1 127 ? 13.37749  4.85416   -52.78170 1.000 29.25610 ?  204 ILE   A CG1 1 
ATOM   975  C  CG2 . ILE   A 1 127 ? 15.38526  5.87789   -51.62827 1.000 31.21684 ?  204 ILE   A CG2 1 
ATOM   976  C  CD1 . ILE   A 1 127 ? 12.29442  5.64733   -52.07783 1.000 28.38403 ?  204 ILE   A CD1 1 
ATOM   977  N  N   . THR   A 1 128 ? 17.92477  3.86800   -52.36808 1.000 33.24349 ?  205 THR   A N   1 
ATOM   978  C  CA  . THR   A 1 128 ? 19.21998  3.71200   -51.71802 1.000 33.50816 ?  205 THR   A CA  1 
ATOM   979  C  C   . THR   A 1 128 ? 19.72042  4.98879   -51.05683 1.000 35.13529 ?  205 THR   A C   1 
ATOM   980  O  O   . THR   A 1 128 ? 20.58223  4.91488   -50.17027 1.000 37.10875 ?  205 THR   A O   1 
ATOM   981  C  CB  . THR   A 1 128 ? 20.27346  3.20872   -52.71848 1.000 36.96132 ?  205 THR   A CB  1 
ATOM   982  O  OG1 . THR   A 1 128 ? 20.57199  4.23195   -53.66809 1.000 37.73004 ?  205 THR   A OG1 1 
ATOM   983  C  CG2 . THR   A 1 128 ? 19.77551  1.98542   -53.47116 1.000 30.25606 ?  205 THR   A CG2 1 
ATOM   984  N  N   . THR   A 1 129 ? 19.17269  6.14266   -51.42103 1.000 33.89320 ?  206 THR   A N   1 
ATOM   985  C  CA  . THR   A 1 129 ? 19.70407  7.41814   -50.97168 1.000 34.65428 ?  206 THR   A CA  1 
ATOM   986  C  C   . THR   A 1 129 ? 18.57915  8.36688   -50.59555 1.000 34.37156 ?  206 THR   A C   1 
ATOM   987  O  O   . THR   A 1 129 ? 17.46212  8.27522   -51.11001 1.000 35.25215 ?  206 THR   A O   1 
ATOM   988  C  CB  . THR   A 1 129 ? 20.55757  8.05440   -52.06619 1.000 37.24893 ?  206 THR   A CB  1 
ATOM   989  O  OG1 . THR   A 1 129 ? 21.66846  7.19553   -52.33430 1.000 41.82003 ?  206 THR   A OG1 1 
ATOM   990  C  CG2 . THR   A 1 129 ? 21.05614  9.41575   -51.63897 1.000 39.18908 ?  206 THR   A CG2 1 
ATOM   991  N  N   . VAL   A 1 130 ? 18.89194  9.28250   -49.68819 1.000 35.67490 ?  207 VAL   A N   1 
ATOM   992  C  CA  . VAL   A 1 130 ? 18.06655  10.45121  -49.42124 1.000 33.30630 ?  207 VAL   A CA  1 
ATOM   993  C  C   . VAL   A 1 130 ? 18.95983  11.66614  -49.60071 1.000 32.97056 ?  207 VAL   A C   1 
ATOM   994  O  O   . VAL   A 1 130 ? 19.94652  11.82141  -48.87748 1.000 34.35729 ?  207 VAL   A O   1 
ATOM   995  C  CB  . VAL   A 1 130 ? 17.45654  10.42148  -48.01626 1.000 31.56071 ?  207 VAL   A CB  1 
ATOM   996  C  CG1 . VAL   A 1 130 ? 16.75712  11.75781  -47.72029 1.000 27.23449 ?  207 VAL   A CG1 1 
ATOM   997  C  CG2 . VAL   A 1 130 ? 16.50183  9.24305   -47.87407 1.000 27.27734 ?  207 VAL   A CG2 1 
ATOM   998  N  N   . GLU   A 1 131 ? 18.62151  12.51815  -50.56021 1.000 31.59378 ?  208 GLU   A N   1 
ATOM   999  C  CA  . GLU   A 1 131 ? 19.51783  13.58768  -50.97212 1.000 31.43940 ?  208 GLU   A CA  1 
ATOM   1000 C  C   . GLU   A 1 131 ? 19.54317  14.72728  -49.95909 1.000 30.51747 ?  208 GLU   A C   1 
ATOM   1001 O  O   . GLU   A 1 131 ? 18.58192  14.96724  -49.22427 1.000 27.31536 ?  208 GLU   A O   1 
ATOM   1002 C  CB  . GLU   A 1 131 ? 19.08745  14.12448  -52.33586 1.000 35.67811 ?  208 GLU   A CB  1 
ATOM   1003 C  CG  . GLU   A 1 131 ? 19.07340  13.06344  -53.41274 1.000 32.03715 ?  208 GLU   A CG  1 
ATOM   1004 C  CD  . GLU   A 1 131 ? 20.47234  12.54190  -53.68439 1.000 38.77594 ?  208 GLU   A CD  1 
ATOM   1005 O  OE1 . GLU   A 1 131 ? 21.42722  13.34752  -53.68405 1.000 42.05413 ?  208 GLU   A OE1 1 
ATOM   1006 O  OE2 . GLU   A 1 131 ? 20.63198  11.32336  -53.87142 1.000 44.33739 ?  208 GLU   A OE2 1 
ATOM   1007 N  N   . LYS   A 1 132 ? 20.66738  15.44211  -49.93884 1.000 31.01190 ?  209 LYS   A N   1 
ATOM   1008 C  CA  . LYS   A 1 132 ? 20.74550  16.69536  -49.19829 1.000 33.51628 ?  209 LYS   A CA  1 
ATOM   1009 C  C   . LYS   A 1 132 ? 19.53376  17.59703  -49.44153 1.000 34.25888 ?  209 LYS   A C   1 
ATOM   1010 O  O   . LYS   A 1 132 ? 19.12076  18.33864  -48.54255 1.000 35.29474 ?  209 LYS   A O   1 
ATOM   1011 C  CB  . LYS   A 1 132 ? 22.03089  17.42622  -49.57388 1.000 35.14946 ?  209 LYS   A CB  1 
ATOM   1012 C  CG  . LYS   A 1 132 ? 23.30181  16.73981  -49.08632 1.000 32.47192 ?  209 LYS   A CG  1 
ATOM   1013 C  CD  . LYS   A 1 132 ? 24.39469  17.77139  -48.84773 1.000 38.28576 ?  209 LYS   A CD  1 
ATOM   1014 C  CE  . LYS   A 1 132 ? 25.76693  17.22374  -49.23341 1.000 48.81732 ?  209 LYS   A CE  1 
ATOM   1015 N  NZ  . LYS   A 1 132 ? 26.01586  15.88740  -48.61233 1.000 43.65559 ?  209 LYS   A NZ  1 
ATOM   1016 N  N   . ASP   A 1 133 ? 18.94463  17.54154  -50.63858 1.000 32.92185 ?  210 ASP   A N   1 
ATOM   1017 C  CA  . ASP   A 1 133 ? 17.79317  18.37175  -50.97954 1.000 33.36946 ?  210 ASP   A CA  1 
ATOM   1018 C  C   . ASP   A 1 133 ? 16.57102  18.10301  -50.11498 1.000 33.32767 ?  210 ASP   A C   1 
ATOM   1019 O  O   . ASP   A 1 133 ? 15.59013  18.84577  -50.22387 1.000 34.22952 ?  210 ASP   A O   1 
ATOM   1020 C  CB  . ASP   A 1 133 ? 17.39438  18.15942  -52.44562 1.000 37.76040 ?  210 ASP   A CB  1 
ATOM   1021 C  CG  . ASP   A 1 133 ? 18.46579  18.61432  -53.42893 1.000 44.46578 ?  210 ASP   A CG  1 
ATOM   1022 O  OD1 . ASP   A 1 133 ? 18.89778  19.79193  -53.35374 1.000 46.34177 ?  210 ASP   A OD1 1 
ATOM   1023 O  OD2 . ASP   A 1 133 ? 18.86431  17.78550  -54.28366 1.000 50.61315 ?  210 ASP   A OD2 1 
ATOM   1024 N  N   . ILE   A 1 134 ? 16.58005  17.05750  -49.28645 1.000 30.70305 ?  211 ILE   A N   1 
ATOM   1025 C  CA  . ILE   A 1 134 ? 15.42122  16.79184  -48.44310 1.000 32.99943 ?  211 ILE   A CA  1 
ATOM   1026 C  C   . ILE   A 1 134 ? 15.06234  18.00717  -47.58821 1.000 32.58825 ?  211 ILE   A C   1 
ATOM   1027 O  O   . ILE   A 1 134 ? 13.96085  18.06512  -47.03390 1.000 35.21558 ?  211 ILE   A O   1 
ATOM   1028 C  CB  . ILE   A 1 134 ? 15.65721  15.54094  -47.55646 1.000 30.80012 ?  211 ILE   A CB  1 
ATOM   1029 C  CG1 . ILE   A 1 134 ? 14.37037  15.11294  -46.84556 1.000 29.80515 ?  211 ILE   A CG1 1 
ATOM   1030 C  CG2 . ILE   A 1 134 ? 16.75406  15.79189  -46.51515 1.000 27.42893 ?  211 ILE   A CG2 1 
ATOM   1031 C  CD1 . ILE   A 1 134 ? 13.41045  14.33034  -47.69455 1.000 29.64321 ?  211 ILE   A CD1 1 
ATOM   1032 N  N   . LYS   A 1 135 ? 15.96636  18.98301  -47.46062 1.000 31.14531 ?  212 LYS   A N   1 
ATOM   1033 C  CA  . LYS   A 1 135 ? 15.67732  20.16720  -46.65218 1.000 34.04520 ?  212 LYS   A CA  1 
ATOM   1034 C  C   . LYS   A 1 135 ? 14.66548  21.09267  -47.31273 1.000 35.91666 ?  212 LYS   A C   1 
ATOM   1035 O  O   . LYS   A 1 135 ? 14.01266  21.87565  -46.61248 1.000 34.33212 ?  212 LYS   A O   1 
ATOM   1036 C  CB  . LYS   A 1 135 ? 16.95839  20.93342  -46.36751 1.000 34.16890 ?  212 LYS   A CB  1 
ATOM   1037 C  CG  . LYS   A 1 135 ? 17.72808  21.29662  -47.60076 1.000 34.51727 ?  212 LYS   A CG  1 
ATOM   1038 C  CD  . LYS   A 1 135 ? 19.06523  21.84000  -47.20449 1.000 40.85904 ?  212 LYS   A CD  1 
ATOM   1039 C  CE  . LYS   A 1 135 ? 19.59894  22.79757  -48.25220 1.000 41.35131 ?  212 LYS   A CE  1 
ATOM   1040 N  NZ  . LYS   A 1 135 ? 20.81790  23.50028  -47.75427 1.000 42.59530 ?  212 LYS   A NZ  1 
ATOM   1041 N  N   . ASN   A 1 136 ? 14.51755  21.01424  -48.63775 1.000 31.37332 ?  213 ASN   A N   1 
ATOM   1042 C  CA  . ASN   A 1 136 ? 13.43324  21.72332  -49.30299 1.000 31.49793 ?  213 ASN   A CA  1 
ATOM   1043 C  C   . ASN   A 1 136 ? 12.07566  21.37402  -48.71787 1.000 33.59506 ?  213 ASN   A C   1 
ATOM   1044 O  O   . ASN   A 1 136 ? 11.14106  22.17449  -48.81444 1.000 35.87643 ?  213 ASN   A O   1 
ATOM   1045 C  CB  . ASN   A 1 136 ? 13.41854  21.40693  -50.79815 1.000 33.73812 ?  213 ASN   A CB  1 
ATOM   1046 C  CG  . ASN   A 1 136 ? 14.63281  21.92077  -51.51012 1.000 35.49986 ?  213 ASN   A CG  1 
ATOM   1047 O  OD1 . ASN   A 1 136 ? 15.36807  22.74479  -50.97358 1.000 36.40100 ?  213 ASN   A OD1 1 
ATOM   1048 N  ND2 . ASN   A 1 136 ? 14.85350  21.44671  -52.73878 1.000 36.80440 ?  213 ASN   A ND2 1 
ATOM   1049 N  N   . LEU   A 1 137 ? 11.92318  20.17647  -48.16149 1.000 34.00768 ?  214 LEU   A N   1 
ATOM   1050 C  CA  . LEU   A 1 137 ? 10.60947  19.71215  -47.71392 1.000 32.59071 ?  214 LEU   A CA  1 
ATOM   1051 C  C   . LEU   A 1 137 ? 10.38901  20.01221  -46.23553 1.000 35.02879 ?  214 LEU   A C   1 
ATOM   1052 O  O   . LEU   A 1 137 ? 10.05460  19.12962  -45.44477 1.000 32.38112 ?  214 LEU   A O   1 
ATOM   1053 C  CB  . LEU   A 1 137 ? 10.45755  18.22547  -48.01080 1.000 34.69554 ?  214 LEU   A CB  1 
ATOM   1054 C  CG  . LEU   A 1 137 ? 10.66794  17.76972  -49.46825 1.000 31.89224 ?  214 LEU   A CG  1 
ATOM   1055 C  CD1 . LEU   A 1 137 ? 10.48774  16.28467  -49.55282 1.000 30.91093 ?  214 LEU   A CD1 1 
ATOM   1056 C  CD2 . LEU   A 1 137 ? 9.71752   18.46937  -50.43508 1.000 29.77508 ?  214 LEU   A CD2 1 
ATOM   1057 N  N   . SER   A 1 138 ? 10.57593  21.28760  -45.85834 1.000 34.59921 ?  215 SER   A N   1 
ATOM   1058 C  CA  . SER   A 1 138 ? 10.58254  21.66833  -44.44861 1.000 34.83718 ?  215 SER   A CA  1 
ATOM   1059 C  C   . SER   A 1 138 ? 9.20425   21.58478  -43.80799 1.000 35.64737 ?  215 SER   A C   1 
ATOM   1060 O  O   . SER   A 1 138 ? 9.10166   21.67648  -42.57451 1.000 34.18332 ?  215 SER   A O   1 
ATOM   1061 C  CB  . SER   A 1 138 ? 11.16689  23.07596  -44.27985 1.000 35.99452 ?  215 SER   A CB  1 
ATOM   1062 O  OG  . SER   A 1 138 ? 10.58307  24.00598  -45.16998 1.000 34.10222 ?  215 SER   A OG  1 
ATOM   1063 N  N   . LYS   A 1 139 ? 8.15324   21.38887  -44.60098 1.000 34.25675 ?  216 LYS   A N   1 
ATOM   1064 C  CA  . LYS   A 1 139 ? 6.81289   21.22541  -44.05951 1.000 36.10727 ?  216 LYS   A CA  1 
ATOM   1065 C  C   . LYS   A 1 139 ? 6.46291   19.76951  -43.75220 1.000 33.76072 ?  216 LYS   A C   1 
ATOM   1066 O  O   . LYS   A 1 139 ? 5.37066   19.51021  -43.22731 1.000 34.06846 ?  216 LYS   A O   1 
ATOM   1067 C  CB  . LYS   A 1 139 ? 5.77124   21.81897  -45.02061 1.000 30.92983 ?  216 LYS   A CB  1 
ATOM   1068 C  CG  . LYS   A 1 139 ? 5.80639   23.32796  -45.11533 1.000 34.32691 ?  216 LYS   A CG  1 
ATOM   1069 C  CD  . LYS   A 1 139 ? 4.56271   23.87003  -45.79414 1.000 35.03666 ?  216 LYS   A CD  1 
ATOM   1070 C  CE  . LYS   A 1 139 ? 4.54139   25.38187  -45.75738 1.000 45.64737 ?  216 LYS   A CE  1 
ATOM   1071 N  NZ  . LYS   A 1 139 ? 5.71374   25.97091  -46.47429 1.000 49.49005 ?  216 LYS   A NZ  1 
ATOM   1072 N  N   . LEU   A 1 140 ? 7.34258   18.81883  -44.05779 1.000 29.29111 ?  217 LEU   A N   1 
ATOM   1073 C  CA  . LEU   A 1 140 ? 7.00395   17.42631  -43.80846 1.000 31.12126 ?  217 LEU   A CA  1 
ATOM   1074 C  C   . LEU   A 1 140 ? 6.75499   17.23743  -42.32856 1.000 32.00024 ?  217 LEU   A C   1 
ATOM   1075 O  O   . LEU   A 1 140 ? 7.56121   17.66643  -41.49922 1.000 35.34216 ?  217 LEU   A O   1 
ATOM   1076 C  CB  . LEU   A 1 140 ? 8.12924   16.49330  -44.24409 1.000 34.83587 ?  217 LEU   A CB  1 
ATOM   1077 C  CG  . LEU   A 1 140 ? 8.39213   16.10928  -45.68375 1.000 34.53423 ?  217 LEU   A CG  1 
ATOM   1078 C  CD1 . LEU   A 1 140 ? 9.78082   15.53871  -45.72724 1.000 34.28666 ?  217 LEU   A CD1 1 
ATOM   1079 C  CD2 . LEU   A 1 140 ? 7.37397   15.07570  -46.17838 1.000 35.42781 ?  217 LEU   A CD2 1 
ATOM   1080 N  N   . SER   A 1 141 ? 5.63793   16.59808  -41.99324 1.000 30.51579 ?  218 SER   A N   1 
ATOM   1081 C  CA  . SER   A 1 141 ? 5.41143   16.16143  -40.62882 1.000 30.81326 ?  218 SER   A CA  1 
ATOM   1082 C  C   . SER   A 1 141 ? 5.35518   14.65206  -40.50702 1.000 35.62523 ?  218 SER   A C   1 
ATOM   1083 O  O   . SER   A 1 141 ? 5.55223   14.12394  -39.40545 1.000 33.95682 ?  218 SER   A O   1 
ATOM   1084 C  CB  . SER   A 1 141 ? 4.11383   16.76761  -40.07645 1.000 33.59146 ?  218 SER   A CB  1 
ATOM   1085 O  OG  . SER   A 1 141 ? 3.00430   16.34919  -40.84838 1.000 37.09525 ?  218 SER   A OG  1 
ATOM   1086 N  N   . MET   A 1 142 ? 5.10073   13.95335  -41.60831 1.000 33.41137 ?  219 MET   A N   1 
ATOM   1087 C  CA  . MET   A 1 142 ? 5.12480   12.49883  -41.65181 1.000 30.99896 ?  219 MET   A CA  1 
ATOM   1088 C  C   . MET   A 1 142 ? 6.01739   12.08952  -42.81499 1.000 30.64820 ?  219 MET   A C   1 
ATOM   1089 O  O   . MET   A 1 142 ? 5.69977   12.37286  -43.97371 1.000 33.37010 ?  219 MET   A O   1 
ATOM   1090 C  CB  . MET   A 1 142 ? 3.71380   11.93853  -41.80706 1.000 32.59929 ?  219 MET   A CB  1 
ATOM   1091 C  CG  . MET   A 1 142 ? 3.65334   10.59742  -42.54269 1.000 37.50728 ?  219 MET   A CG  1 
ATOM   1092 S  SD  . MET   A 1 142 ? 4.15332   9.15575   -41.55659 1.000 36.90270 ?  219 MET   A SD  1 
ATOM   1093 C  CE  . MET   A 1 142 ? 2.80905   9.08126   -40.35812 1.000 33.05720 ?  219 MET   A CE  1 
ATOM   1094 N  N   . LEU   A 1 143 ? 7.14290   11.45026  -42.51891 1.000 27.82464 ?  220 LEU   A N   1 
ATOM   1095 C  CA  . LEU   A 1 143 ? 8.01144   10.90181  -43.55417 1.000 30.09168 ?  220 LEU   A CA  1 
ATOM   1096 C  C   . LEU   A 1 143 ? 8.18417   9.40555   -43.29145 1.000 29.84071 ?  220 LEU   A C   1 
ATOM   1097 O  O   . LEU   A 1 143 ? 8.64168   9.01113   -42.21410 1.000 31.07928 ?  220 LEU   A O   1 
ATOM   1098 C  CB  . LEU   A 1 143 ? 9.35307   11.64738  -43.57303 1.000 27.90920 ?  220 LEU   A CB  1 
ATOM   1099 C  CG  . LEU   A 1 143 ? 10.47504  11.09884  -44.47083 1.000 34.17892 ?  220 LEU   A CG  1 
ATOM   1100 C  CD1 . LEU   A 1 143 ? 10.13843  11.16228  -45.97937 1.000 31.30320 ?  220 LEU   A CD1 1 
ATOM   1101 C  CD2 . LEU   A 1 143 ? 11.80544  11.78912  -44.17541 1.000 28.40073 ?  220 LEU   A CD2 1 
ATOM   1102 N  N   . SER   A 1 144 ? 7.79825   8.56665   -44.25130 1.000 29.69658 ?  221 SER   A N   1 
ATOM   1103 C  CA  . SER   A 1 144 ? 7.95239   7.12069   -44.10260 1.000 29.23514 ?  221 SER   A CA  1 
ATOM   1104 C  C   . SER   A 1 144 ? 8.76683   6.55691   -45.25635 1.000 29.03783 ?  221 SER   A C   1 
ATOM   1105 O  O   . SER   A 1 144 ? 8.32630   6.59195   -46.40962 1.000 31.58014 ?  221 SER   A O   1 
ATOM   1106 C  CB  . SER   A 1 144 ? 6.59852   6.41375   -44.01895 1.000 31.31485 ?  221 SER   A CB  1 
ATOM   1107 O  OG  . SER   A 1 144 ? 6.76859   5.00250   -43.96237 1.000 32.25083 ?  221 SER   A OG  1 
ATOM   1108 N  N   . ILE   A 1 145 ? 9.93534   6.00701   -44.94095 1.000 28.79686 ?  222 ILE   A N   1 
ATOM   1109 C  CA  . ILE   A 1 145 ? 10.79813  5.40181   -45.94858 1.000 29.16645 ?  222 ILE   A CA  1 
ATOM   1110 C  C   . ILE   A 1 145 ? 11.17298  3.99150   -45.52447 1.000 29.54759 ?  222 ILE   A C   1 
ATOM   1111 O  O   . ILE   A 1 145 ? 12.25077  3.49276   -45.87662 1.000 29.31548 ?  222 ILE   A O   1 
ATOM   1112 C  CB  . ILE   A 1 145 ? 12.06867  6.23926   -46.17149 1.000 30.88744 ?  222 ILE   A CB  1 
ATOM   1113 C  CG1 . ILE   A 1 145 ? 12.70673  6.54299   -44.82140 1.000 30.45599 ?  222 ILE   A CG1 1 
ATOM   1114 C  CG2 . ILE   A 1 145 ? 11.75383  7.52087   -46.90686 1.000 33.30685 ?  222 ILE   A CG2 1 
ATOM   1115 C  CD1 . ILE   A 1 145 ? 13.80359  7.54776   -44.89765 1.000 34.38611 ?  222 ILE   A CD1 1 
ATOM   1116 N  N   . ARG   A 1 146 ? 10.30810  3.33949   -44.75812 1.000 29.43391 ?  223 ARG   A N   1 
ATOM   1117 C  CA  . ARG   A 1 146 ? 10.68380  2.02929   -44.27262 1.000 28.70384 ?  223 ARG   A CA  1 
ATOM   1118 C  C   . ARG   A 1 146 ? 10.71633  1.04503   -45.43719 1.000 29.48254 ?  223 ARG   A C   1 
ATOM   1119 O  O   . ARG   A 1 146 ? 10.10700  1.26509   -46.48179 1.000 31.43879 ?  223 ARG   A O   1 
ATOM   1120 C  CB  . ARG   A 1 146 ? 9.72468   1.57428   -43.17333 1.000 33.37661 ?  223 ARG   A CB  1 
ATOM   1121 C  CG  . ARG   A 1 146 ? 8.46891   0.90521   -43.65655 1.000 36.14734 ?  223 ARG   A CG  1 
ATOM   1122 C  CD  . ARG   A 1 146 ? 8.36826   -0.54024  -43.13701 1.000 39.92835 ?  223 ARG   A CD  1 
ATOM   1123 N  NE  . ARG   A 1 146 ? 7.79982   -0.61468  -41.79327 1.000 43.42977 ?  223 ARG   A NE  1 
ATOM   1124 C  CZ  . ARG   A 1 146 ? 7.33589   -1.72118  -41.21697 1.000 41.32953 ?  223 ARG   A CZ  1 
ATOM   1125 N  NH1 . ARG   A 1 146 ? 7.33610   -2.88393  -41.84425 1.000 41.08889 ?  223 ARG   A NH1 1 
ATOM   1126 N  NH2 . ARG   A 1 146 ? 6.84944   -1.65469  -39.97879 1.000 39.44580 ?  223 ARG   A NH2 1 
ATOM   1127 N  N   . GLU   A 1 147 ? 11.45725  -0.04632  -45.25192 1.000 31.97308 ?  224 GLU   A N   1 
ATOM   1128 C  CA  . GLU   A 1 147 ? 11.61217  -1.09743  -46.26437 1.000 31.95822 ?  224 GLU   A CA  1 
ATOM   1129 C  C   . GLU   A 1 147 ? 12.14795  -0.51814  -47.57805 1.000 31.62468 ?  224 GLU   A C   1 
ATOM   1130 O  O   . GLU   A 1 147 ? 11.53897  -0.63277  -48.65377 1.000 29.52923 ?  224 GLU   A O   1 
ATOM   1131 C  CB  . GLU   A 1 147 ? 10.29870  -1.86694  -46.47758 1.000 31.87703 ?  224 GLU   A CB  1 
ATOM   1132 C  CG  . GLU   A 1 147 ? 9.88001   -2.69589  -45.25425 1.000 35.41209 ?  224 GLU   A CG  1 
ATOM   1133 C  CD  . GLU   A 1 147 ? 8.49145   -3.30560  -45.37820 1.000 41.13722 ?  224 GLU   A CD  1 
ATOM   1134 O  OE1 . GLU   A 1 147 ? 8.27990   -4.08972  -46.32645 1.000 46.08404 ?  224 GLU   A OE1 1 
ATOM   1135 O  OE2 . GLU   A 1 147 ? 7.61449   -3.00623  -44.53047 1.000 41.53061 ?  224 GLU   A OE2 1 
ATOM   1136 N  N   . ASN   A 1 148 ? 13.31563  0.11818   -47.46316 1.000 26.75753 ?  225 ASN   A N   1 
ATOM   1137 C  CA  . ASN   A 1 148 ? 14.10556  0.47750   -48.62660 1.000 28.24007 ?  225 ASN   A CA  1 
ATOM   1138 C  C   . ASN   A 1 148 ? 15.55415  0.06196   -48.39590 1.000 31.65921 ?  225 ASN   A C   1 
ATOM   1139 O  O   . ASN   A 1 148 ? 15.81142  -0.91714  -47.69333 1.000 32.03031 ?  225 ASN   A O   1 
ATOM   1140 C  CB  . ASN   A 1 148 ? 13.95753  1.96305   -48.92548 1.000 28.98107 ?  225 ASN   A CB  1 
ATOM   1141 C  CG  . ASN   A 1 148 ? 12.62801  2.27891   -49.61458 1.000 30.86113 ?  225 ASN   A CG  1 
ATOM   1142 O  OD1 . ASN   A 1 148 ? 12.51182  2.14197   -50.83580 1.000 30.33803 ?  225 ASN   A OD1 1 
ATOM   1143 N  ND2 . ASN   A 1 148 ? 11.61896  2.68135   -48.83563 1.000 25.05577 ?  225 ASN   A ND2 1 
ATOM   1144 N  N   . LYS   A 1 149 ? 16.50695  0.75756   -48.99602 1.000 32.82584 ?  226 LYS   A N   1 
ATOM   1145 C  CA  . LYS   A 1 149 ? 17.90193  0.36869   -48.88111 1.000 33.84111 ?  226 LYS   A CA  1 
ATOM   1146 C  C   . LYS   A 1 149 ? 18.76580  1.55884   -48.52295 1.000 34.48084 ?  226 LYS   A C   1 
ATOM   1147 O  O   . LYS   A 1 149 ? 19.84965  1.75320   -49.08607 1.000 36.21095 ?  226 LYS   A O   1 
ATOM   1148 C  CB  . LYS   A 1 149 ? 18.39151  -0.27740  -50.17150 1.000 36.62783 ?  226 LYS   A CB  1 
ATOM   1149 C  CG  . LYS   A 1 149 ? 17.86239  -1.68167  -50.37336 1.000 35.85509 ?  226 LYS   A CG  1 
ATOM   1150 C  CD  . LYS   A 1 149 ? 17.80982  -2.03530  -51.84625 1.000 41.14208 ?  226 LYS   A CD  1 
ATOM   1151 C  CE  . LYS   A 1 149 ? 17.30045  -3.44389  -52.04069 1.000 51.00017 ?  226 LYS   A CE  1 
ATOM   1152 N  NZ  . LYS   A 1 149 ? 17.71858  -3.97273  -53.36297 1.000 53.86419 ?  226 LYS   A NZ  1 
ATOM   1153 N  N   . ILE   A 1 150 ? 18.30547  2.36884   -47.57410 1.000 31.29542 ?  227 ILE   A N   1 
ATOM   1154 C  CA  . ILE   A 1 150 ? 19.03332  3.56698   -47.18622 1.000 29.36552 ?  227 ILE   A CA  1 
ATOM   1155 C  C   . ILE   A 1 150 ? 20.16840  3.17590   -46.25491 1.000 30.89066 ?  227 ILE   A C   1 
ATOM   1156 O  O   . ILE   A 1 150 ? 19.95502  2.49135   -45.24829 1.000 28.62053 ?  227 ILE   A O   1 
ATOM   1157 C  CB  . ILE   A 1 150 ? 18.09069  4.58474   -46.52866 1.000 31.13939 ?  227 ILE   A CB  1 
ATOM   1158 C  CG1 . ILE   A 1 150 ? 17.19376  5.23075   -47.59039 1.000 32.03013 ?  227 ILE   A CG1 1 
ATOM   1159 C  CG2 . ILE   A 1 150 ? 18.88511  5.65792   -45.83751 1.000 29.86375 ?  227 ILE   A CG2 1 
ATOM   1160 C  CD1 . ILE   A 1 150 ? 15.72710  5.22763   -47.23671 1.000 28.82768 ?  227 ILE   A CD1 1 
ATOM   1161 N  N   . LYS   A 1 151 ? 21.38603  3.60352   -46.59127 1.000 32.88863 ?  228 LYS   A N   1 
ATOM   1162 C  CA  . LYS   A 1 151 ? 22.53719  3.38587   -45.72253 1.000 32.40391 ?  228 LYS   A CA  1 
ATOM   1163 C  C   . LYS   A 1 151 ? 22.85200  4.58189   -44.82568 1.000 34.77300 ?  228 LYS   A C   1 
ATOM   1164 O  O   . LYS   A 1 151 ? 23.53878  4.41321   -43.80162 1.000 31.10786 ?  228 LYS   A O   1 
ATOM   1165 C  CB  . LYS   A 1 151 ? 23.76998  3.03038   -46.56423 1.000 32.43943 ?  228 LYS   A CB  1 
ATOM   1166 C  CG  . LYS   A 1 151 ? 23.64996  1.65691   -47.22018 1.000 38.83132 ?  228 LYS   A CG  1 
ATOM   1167 C  CD  . LYS   A 1 151 ? 24.56712  1.48393   -48.41271 1.000 39.76259 ?  228 LYS   A CD  1 
ATOM   1168 C  CE  . LYS   A 1 151 ? 24.25154  0.17428   -49.14414 1.000 46.98473 ?  228 LYS   A CE  1 
ATOM   1169 N  NZ  . LYS   A 1 151 ? 22.80998  0.06916   -49.55678 1.000 40.35975 ?  228 LYS   A NZ  1 
ATOM   1170 N  N   . GLN   A 1 152 ? 22.33360  5.76598   -45.15669 1.000 33.08672 ?  229 GLN   A N   1 
ATOM   1171 C  CA  . GLN   A 1 152 ? 22.69464  6.98278   -44.44665 1.000 29.67192 ?  229 GLN   A CA  1 
ATOM   1172 C  C   . GLN   A 1 152 ? 21.59455  8.02280   -44.61115 1.000 29.75970 ?  229 GLN   A C   1 
ATOM   1173 O  O   . GLN   A 1 152 ? 20.98687  8.12762   -45.67690 1.000 32.27343 ?  229 GLN   A O   1 
ATOM   1174 C  CB  . GLN   A 1 152 ? 24.02489  7.52044   -44.96632 1.000 32.41307 ?  229 GLN   A CB  1 
ATOM   1175 C  CG  . GLN   A 1 152 ? 24.52737  8.76778   -44.26543 1.000 34.83824 ?  229 GLN   A CG  1 
ATOM   1176 C  CD  . GLN   A 1 152 ? 26.01845  8.95825   -44.47522 1.000 41.32847 ?  229 GLN   A CD  1 
ATOM   1177 O  OE1 . GLN   A 1 152 ? 26.65516  8.18393   -45.19204 1.000 44.78589 ?  229 GLN   A OE1 1 
ATOM   1178 N  NE2 . GLN   A 1 152 ? 26.58962  9.97545   -43.83365 1.000 46.62467 ?  229 GLN   A NE2 1 
ATOM   1179 N  N   . LEU   A 1 153 ? 21.31758  8.75585   -43.53118 1.000 31.59075 ?  230 LEU   A N   1 
ATOM   1180 C  CA  . LEU   A 1 153 ? 20.48201  9.94506   -43.56248 1.000 31.25660 ?  230 LEU   A CA  1 
ATOM   1181 C  C   . LEU   A 1 153 ? 21.37376  11.16008  -43.57514 1.000 29.64256 ?  230 LEU   A C   1 
ATOM   1182 O  O   . LEU   A 1 153 ? 22.34635  11.20154  -42.81649 1.000 31.81474 ?  230 LEU   A O   1 
ATOM   1183 C  CB  . LEU   A 1 153 ? 19.54899  10.00525  -42.35975 1.000 30.26954 ?  230 LEU   A CB  1 
ATOM   1184 C  CG  . LEU   A 1 153 ? 18.49073  8.90770   -42.40162 1.000 35.34884 ?  230 LEU   A CG  1 
ATOM   1185 C  CD1 . LEU   A 1 153 ? 17.38480  9.12053   -41.36192 1.000 28.41712 ?  230 LEU   A CD1 1 
ATOM   1186 C  CD2 . LEU   A 1 153 ? 17.93286  8.82384   -43.81408 1.000 32.22801 ?  230 LEU   A CD2 1 
ATOM   1187 N  N   . PRO   A 1 154 ? 21.10987  12.14394  -44.42698 1.000 32.72217 ?  231 PRO   A N   1 
ATOM   1188 C  CA  . PRO   A 1 154 ? 21.97590  13.32208  -44.47133 1.000 33.14257 ?  231 PRO   A CA  1 
ATOM   1189 C  C   . PRO   A 1 154 ? 21.74445  14.19132  -43.24897 1.000 30.91774 ?  231 PRO   A C   1 
ATOM   1190 O  O   . PRO   A 1 154 ? 20.69503  14.13985  -42.60778 1.000 32.52996 ?  231 PRO   A O   1 
ATOM   1191 C  CB  . PRO   A 1 154 ? 21.53710  14.03672  -45.75587 1.000 33.76967 ?  231 PRO   A CB  1 
ATOM   1192 C  CG  . PRO   A 1 154 ? 20.06477  13.69344  -45.85215 1.000 32.17555 ?  231 PRO   A CG  1 
ATOM   1193 C  CD  . PRO   A 1 154 ? 19.98485  12.24703  -45.37397 1.000 33.14871 ?  231 PRO   A CD  1 
ATOM   1194 N  N   . ALA   A 1 155 ? 22.75061  15.00149  -42.93061 1.000 31.77838 ?  232 ALA   A N   1 
ATOM   1195 C  CA  . ALA   A 1 155 ? 22.58453  16.00369  -41.88128 1.000 37.03124 ?  232 ALA   A CA  1 
ATOM   1196 C  C   . ALA   A 1 155 ? 21.43509  16.95562  -42.17941 1.000 35.32593 ?  232 ALA   A C   1 
ATOM   1197 O  O   . ALA   A 1 155 ? 20.86462  17.54063  -41.25122 1.000 36.47222 ?  232 ALA   A O   1 
ATOM   1198 C  CB  . ALA   A 1 155 ? 23.87726  16.80412  -41.68551 1.000 29.98492 ?  232 ALA   A CB  1 
ATOM   1199 N  N   . GLU   A 1 156 ? 21.07246  17.12176  -43.44856 1.000 35.98170 ?  233 GLU   A N   1 
ATOM   1200 C  CA  . GLU   A 1 156 ? 19.98680  18.03700  -43.77869 1.000 35.74405 ?  233 GLU   A CA  1 
ATOM   1201 C  C   . GLU   A 1 156 ? 18.64887  17.59368  -43.19669 1.000 35.72432 ?  233 GLU   A C   1 
ATOM   1202 O  O   . GLU   A 1 156 ? 17.67959  18.36232  -43.26157 1.000 35.71044 ?  233 GLU   A O   1 
ATOM   1203 C  CB  . GLU   A 1 156 ? 19.88483  18.18810  -45.29580 1.000 35.89341 ?  233 GLU   A CB  1 
ATOM   1204 C  CG  . GLU   A 1 156 ? 20.90551  19.14632  -45.90864 1.000 36.54004 ?  233 GLU   A CG  1 
ATOM   1205 C  CD  . GLU   A 1 156 ? 22.34294  18.65188  -45.79906 1.000 35.97462 ?  233 GLU   A CD  1 
ATOM   1206 O  OE1 . GLU   A 1 156 ? 22.56184  17.54101  -45.27984 1.000 38.73534 ?  233 GLU   A OE1 1 
ATOM   1207 O  OE2 . GLU   A 1 156 ? 23.26410  19.38472  -46.22808 1.000 44.63019 ?  233 GLU   A OE2 1 
ATOM   1208 N  N   . ILE   A 1 157 ? 18.57510  16.38496  -42.62909 1.000 32.06326 ?  234 ILE   A N   1 
ATOM   1209 C  CA  . ILE   A 1 157 ? 17.33195  15.91031  -42.03019 1.000 33.98975 ?  234 ILE   A CA  1 
ATOM   1210 C  C   . ILE   A 1 157 ? 16.94252  16.79487  -40.85541 1.000 33.37713 ?  234 ILE   A C   1 
ATOM   1211 O  O   . ILE   A 1 157 ? 15.75127  16.99374  -40.58040 1.000 32.56187 ?  234 ILE   A O   1 
ATOM   1212 C  CB  . ILE   A 1 157 ? 17.46488  14.42117  -41.62800 1.000 34.48949 ?  234 ILE   A CB  1 
ATOM   1213 C  CG1 . ILE   A 1 157 ? 16.12748  13.69691  -41.75092 1.000 35.58423 ?  234 ILE   A CG1 1 
ATOM   1214 C  CG2 . ILE   A 1 157 ? 17.97213  14.26015  -40.20863 1.000 35.53742 ?  234 ILE   A CG2 1 
ATOM   1215 C  CD1 . ILE   A 1 157 ? 15.96439  12.98067  -43.06368 1.000 33.71923 ?  234 ILE   A CD1 1 
ATOM   1216 N  N   . GLY   A 1 158 ? 17.92951  17.38132  -40.18014 1.000 34.55564 ?  235 GLY   A N   1 
ATOM   1217 C  CA  . GLY   A 1 158 ? 17.68979  18.29439  -39.07844 1.000 35.42943 ?  235 GLY   A CA  1 
ATOM   1218 C  C   . GLY   A 1 158 ? 17.00637  19.60034  -39.43775 1.000 38.55708 ?  235 GLY   A C   1 
ATOM   1219 O  O   . GLY   A 1 158 ? 16.76882  20.41411  -38.53781 1.000 37.04006 ?  235 GLY   A O   1 
ATOM   1220 N  N   . GLU   A 1 159 ? 16.68961  19.83536  -40.71320 1.000 39.02484 ?  236 GLU   A N   1 
ATOM   1221 C  CA  . GLU   A 1 159 ? 15.93801  21.01838  -41.11622 1.000 41.70139 ?  236 GLU   A CA  1 
ATOM   1222 C  C   . GLU   A 1 159 ? 14.44394  20.74777  -41.26520 1.000 41.67133 ?  236 GLU   A C   1 
ATOM   1223 O  O   . GLU   A 1 159 ? 13.69894  21.64429  -41.67948 1.000 43.29305 ?  236 GLU   A O   1 
ATOM   1224 C  CB  . GLU   A 1 159 ? 16.51268  21.59884  -42.41113 1.000 38.82379 ?  236 GLU   A CB  1 
ATOM   1225 C  CG  . GLU   A 1 159 ? 17.90214  22.17565  -42.19367 1.000 43.20253 ?  236 GLU   A CG  1 
ATOM   1226 C  CD  . GLU   A 1 159 ? 18.40372  23.00021  -43.36079 1.000 52.81146 ?  236 GLU   A CD  1 
ATOM   1227 O  OE1 . GLU   A 1 159 ? 17.75712  24.01856  -43.71207 1.000 54.69646 ?  236 GLU   A OE1 1 
ATOM   1228 O  OE2 . GLU   A 1 159 ? 19.45452  22.62604  -43.92832 1.000 52.31829 ?  236 GLU   A OE2 1 
ATOM   1229 N  N   . LEU   A 1 160 ? 13.99049  19.54343  -40.91652 1.000 39.07640 ?  237 LEU   A N   1 
ATOM   1230 C  CA  . LEU   A 1 160 ? 12.56976  19.20831  -40.92637 1.000 36.83855 ?  237 LEU   A CA  1 
ATOM   1231 C  C   . LEU   A 1 160 ? 11.99148  19.39682  -39.52085 1.000 36.53550 ?  237 LEU   A C   1 
ATOM   1232 O  O   . LEU   A 1 160 ? 11.55589  18.45868  -38.84769 1.000 33.87299 ?  237 LEU   A O   1 
ATOM   1233 C  CB  . LEU   A 1 160 ? 12.37401  17.78080  -41.43416 1.000 33.25825 ?  237 LEU   A CB  1 
ATOM   1234 C  CG  . LEU   A 1 160 ? 13.15759  17.39088  -42.68762 1.000 34.51353 ?  237 LEU   A CG  1 
ATOM   1235 C  CD1 . LEU   A 1 160 ? 12.97218  15.91519  -43.01942 1.000 28.79894 ?  237 LEU   A CD1 1 
ATOM   1236 C  CD2 . LEU   A 1 160 ? 12.75702  18.27735  -43.87632 1.000 33.65989 ?  237 LEU   A CD2 1 
ATOM   1237 N  N   . CYS   A 1 161 ? 11.97861  20.64904  -39.07852 1.000 32.62098 ?  238 CYS   A N   1 
ATOM   1238 C  CA  . CYS   A 1 161 ? 11.57917  20.90641  -37.70133 1.000 37.46986 ?  238 CYS   A CA  1 
ATOM   1239 C  C   . CYS   A 1 161 ? 10.09873  20.63078  -37.43223 1.000 36.38735 ?  238 CYS   A C   1 
ATOM   1240 O  O   . CYS   A 1 161 ? 9.68921   20.66824  -36.26494 1.000 36.87514 ?  238 CYS   A O   1 
ATOM   1241 C  CB  . CYS   A 1 161 ? 11.93240  22.34933  -37.31162 1.000 42.97928 ?  238 CYS   A CB  1 
ATOM   1242 S  SG  . CYS   A 1 161 ? 11.96402  23.50135  -38.69563 1.000 53.20579 ?  238 CYS   A SG  1 
ATOM   1243 N  N   . ASN   A 1 162 ? 9.28924   20.33914  -38.44993 1.000 32.89546 ?  239 ASN   A N   1 
ATOM   1244 C  CA  . ASN   A 1 162 ? 7.90683   19.94336  -38.21042 1.000 32.61563 ?  239 ASN   A CA  1 
ATOM   1245 C  C   . ASN   A 1 162 ? 7.68512   18.43200  -38.24329 1.000 33.98657 ?  239 ASN   A C   1 
ATOM   1246 O  O   . ASN   A 1 162 ? 6.54231   17.98608  -38.11634 1.000 31.29651 ?  239 ASN   A O   1 
ATOM   1247 C  CB  . ASN   A 1 162 ? 6.98260   20.61740  -39.21576 1.000 32.58793 ?  239 ASN   A CB  1 
ATOM   1248 C  CG  . ASN   A 1 162 ? 7.17708   22.10728  -39.25223 1.000 38.24430 ?  239 ASN   A CG  1 
ATOM   1249 O  OD1 . ASN   A 1 162 ? 6.90487   22.80944  -38.27787 1.000 38.98003 ?  239 ASN   A OD1 1 
ATOM   1250 N  ND2 . ASN   A 1 162 ? 7.67393   22.60376  -40.37877 1.000 39.29699 ?  239 ASN   A ND2 1 
ATOM   1251 N  N   . LEU   A 1 163 ? 8.73934   17.63647  -38.39468 1.000 35.28426 ?  240 LEU   A N   1 
ATOM   1252 C  CA  . LEU   A 1 163 ? 8.58442   16.18831  -38.40329 1.000 32.71931 ?  240 LEU   A CA  1 
ATOM   1253 C  C   . LEU   A 1 163 ? 7.91163   15.70491  -37.12535 1.000 33.91521 ?  240 LEU   A C   1 
ATOM   1254 O  O   . LEU   A 1 163 ? 8.34389   16.04111  -36.01789 1.000 32.81382 ?  240 LEU   A O   1 
ATOM   1255 C  CB  . LEU   A 1 163 ? 9.94376   15.52034  -38.53708 1.000 31.18327 ?  240 LEU   A CB  1 
ATOM   1256 C  CG  . LEU   A 1 163 ? 10.34586  14.91964  -39.85901 1.000 31.95251 ?  240 LEU   A CG  1 
ATOM   1257 C  CD1 . LEU   A 1 163 ? 11.46204  13.91978  -39.58137 1.000 32.73366 ?  240 LEU   A CD1 1 
ATOM   1258 C  CD2 . LEU   A 1 163 ? 9.16125   14.24573  -40.50452 1.000 32.26839 ?  240 LEU   A CD2 1 
ATOM   1259 N  N   . ILE   A 1 164 ? 6.86257   14.89737  -37.28899 1.000 32.05003 ?  241 ILE   A N   1 
ATOM   1260 C  CA  . ILE   A 1 164 ? 6.17981   14.24551  -36.18093 1.000 33.10992 ?  241 ILE   A CA  1 
ATOM   1261 C  C   . ILE   A 1 164 ? 6.43307   12.74317  -36.17679 1.000 32.92562 ?  241 ILE   A C   1 
ATOM   1262 O  O   . ILE   A 1 164 ? 6.55706   12.13118  -35.11368 1.000 32.28569 ?  241 ILE   A O   1 
ATOM   1263 C  CB  . ILE   A 1 164 ? 4.66071   14.53125  -36.21979 1.000 34.03597 ?  241 ILE   A CB  1 
ATOM   1264 C  CG1 . ILE   A 1 164 ? 4.36256   16.03873  -36.33457 1.000 34.17475 ?  241 ILE   A CG1 1 
ATOM   1265 C  CG2 . ILE   A 1 164 ? 4.00238   13.93184  -35.00496 1.000 31.58911 ?  241 ILE   A CG2 1 
ATOM   1266 C  CD1 . ILE   A 1 164 ? 4.38372   16.76581  -35.04992 1.000 32.26171 ?  241 ILE   A CD1 1 
ATOM   1267 N  N   . THR   A 1 165 ? 6.47807   12.13384  -37.35757 1.000 31.72257 ?  242 THR   A N   1 
ATOM   1268 C  CA  . THR   A 1 165 ? 6.66298   10.69991  -37.51333 1.000 33.71780 ?  242 THR   A CA  1 
ATOM   1269 C  C   . THR   A 1 165 ? 7.74931   10.45378  -38.54624 1.000 31.58576 ?  242 THR   A C   1 
ATOM   1270 O  O   . THR   A 1 165 ? 7.58005   10.77869  -39.72835 1.000 30.89905 ?  242 THR   A O   1 
ATOM   1271 C  CB  . THR   A 1 165 ? 5.36959   10.00610  -37.94205 1.000 34.69111 ?  242 THR   A CB  1 
ATOM   1272 O  OG1 . THR   A 1 165 ? 4.33169   10.32885  -37.01864 1.000 36.25138 ?  242 THR   A OG1 1 
ATOM   1273 C  CG2 . THR   A 1 165 ? 5.56406   8.49409   -37.94859 1.000 33.14297 ?  242 THR   A CG2 1 
ATOM   1274 N  N   . LEU   A 1 166 ? 8.85485   9.87926   -38.09666 1.000 30.21991 ?  243 LEU   A N   1 
ATOM   1275 C  CA  . LEU   A 1 166 ? 9.93165   9.44492   -38.96641 1.000 29.54284 ?  243 LEU   A CA  1 
ATOM   1276 C  C   . LEU   A 1 166 ? 10.02830  7.93682   -38.82451 1.000 29.98865 ?  243 LEU   A C   1 
ATOM   1277 O  O   . LEU   A 1 166 ? 10.28958  7.43038   -37.72801 1.000 30.24960 ?  243 LEU   A O   1 
ATOM   1278 C  CB  . LEU   A 1 166 ? 11.24643  10.13001  -38.59336 1.000 28.80021 ?  243 LEU   A CB  1 
ATOM   1279 C  CG  . LEU   A 1 166 ? 12.47003  9.78801   -39.43223 1.000 28.99310 ?  243 LEU   A CG  1 
ATOM   1280 C  CD1 . LEU   A 1 166 ? 12.12185  9.87935   -40.89021 1.000 29.70684 ?  243 LEU   A CD1 1 
ATOM   1281 C  CD2 . LEU   A 1 166 ? 13.57852  10.74697  -39.08848 1.000 28.57867 ?  243 LEU   A CD2 1 
ATOM   1282 N  N   . ASP   A 1 167 ? 9.78230   7.22338   -39.91840 1.000 31.61179 ?  244 ASP   A N   1 
ATOM   1283 C  CA  . ASP   A 1 167 ? 9.80988   5.76191   -39.94488 1.000 28.94542 ?  244 ASP   A CA  1 
ATOM   1284 C  C   . ASP   A 1 167 ? 10.89444  5.31729   -40.92517 1.000 28.67203 ?  244 ASP   A C   1 
ATOM   1285 O  O   . ASP   A 1 167 ? 10.75604  5.51690   -42.13602 1.000 29.20778 ?  244 ASP   A O   1 
ATOM   1286 C  CB  . ASP   A 1 167 ? 8.42829   5.23956   -40.34372 1.000 31.86458 ?  244 ASP   A CB  1 
ATOM   1287 C  CG  . ASP   A 1 167 ? 8.34692   3.72364   -40.40619 1.000 37.91948 ?  244 ASP   A CG  1 
ATOM   1288 O  OD1 . ASP   A 1 167 ? 9.34860   3.03224   -40.10398 1.000 36.47950 ?  244 ASP   A OD1 1 
ATOM   1289 O  OD2 . ASP   A 1 167 ? 7.25971   3.22386   -40.77938 1.000 42.00869 ?  244 ASP   A OD2 1 
ATOM   1290 N  N   . VAL   A 1 168 ? 11.98047  4.72742   -40.41860 1.000 25.08750 ?  245 VAL   A N   1 
ATOM   1291 C  CA  . VAL   A 1 168 ? 13.01069  4.22036   -41.31641 1.000 27.52710 ?  245 VAL   A CA  1 
ATOM   1292 C  C   . VAL   A 1 168 ? 13.27995  2.75406   -41.01555 1.000 29.31306 ?  245 VAL   A C   1 
ATOM   1293 O  O   . VAL   A 1 168 ? 14.38699  2.25439   -41.25149 1.000 29.78702 ?  245 VAL   A O   1 
ATOM   1294 C  CB  . VAL   A 1 168 ? 14.30978  5.04098   -41.22937 1.000 32.74969 ?  245 VAL   A CB  1 
ATOM   1295 C  CG1 . VAL   A 1 168 ? 14.02806  6.52152   -41.38691 1.000 31.39154 ?  245 VAL   A CG1 1 
ATOM   1296 C  CG2 . VAL   A 1 168 ? 14.98296  4.79685   -39.91714 1.000 35.92274 ?  245 VAL   A CG2 1 
ATOM   1297 N  N   . ALA   A 1 169 ? 12.27041  2.05739   -40.49554 1.000 27.90691 ?  246 ALA   A N   1 
ATOM   1298 C  CA  . ALA   A 1 169 ? 12.38333  0.62764   -40.24547 1.000 29.43353 ?  246 ALA   A CA  1 
ATOM   1299 C  C   . ALA   A 1 169 ? 12.90092  -0.09930  -41.48248 1.000 29.38240 ?  246 ALA   A C   1 
ATOM   1300 O  O   . ALA   A 1 169 ? 12.64544  0.30386   -42.61679 1.000 31.87441 ?  246 ALA   A O   1 
ATOM   1301 C  CB  . ALA   A 1 169 ? 11.01953  0.05811   -39.83971 1.000 30.44899 ?  246 ALA   A CB  1 
ATOM   1302 N  N   . HIS   A 1 170 ? 13.63314  -1.18685  -41.26330 1.000 27.66889 ?  247 HIS   A N   1 
ATOM   1303 C  CA  . HIS   A 1 170 ? 14.01848  -2.07837  -42.34841 1.000 27.65682 ?  247 HIS   A CA  1 
ATOM   1304 C  C   . HIS   A 1 170 ? 14.78851  -1.33471  -43.44357 1.000 30.52594 ?  247 HIS   A C   1 
ATOM   1305 O  O   . HIS   A 1 170 ? 14.46768  -1.42147  -44.63400 1.000 29.75626 ?  247 HIS   A O   1 
ATOM   1306 C  CB  . HIS   A 1 170 ? 12.78520  -2.77683  -42.92717 1.000 30.10060 ?  247 HIS   A CB  1 
ATOM   1307 C  CG  . HIS   A 1 170 ? 12.16189  -3.78768  -42.01004 1.000 30.71431 ?  247 HIS   A CG  1 
ATOM   1308 N  ND1 . HIS   A 1 170 ? 12.68363  -5.05192  -41.82445 1.000 29.31498 ?  247 HIS   A ND1 1 
ATOM   1309 C  CD2 . HIS   A 1 170 ? 11.04067  -3.72979  -41.24839 1.000 34.24847 ?  247 HIS   A CD2 1 
ATOM   1310 C  CE1 . HIS   A 1 170 ? 11.91797  -5.72496  -40.98182 1.000 29.56674 ?  247 HIS   A CE1 1 
ATOM   1311 N  NE2 . HIS   A 1 170 ? 10.91370  -4.94472  -40.61538 1.000 32.17545 ?  247 HIS   A NE2 1 
ATOM   1312 N  N   . ASN   A 1 171 ? 15.81002  -0.58160  -43.02840 1.000 28.88565 ?  248 ASN   A N   1 
ATOM   1313 C  CA  . ASN   A 1 171 ? 16.81541  -0.07338  -43.95391 1.000 28.43902 ?  248 ASN   A CA  1 
ATOM   1314 C  C   . ASN   A 1 171 ? 18.18533  -0.53279  -43.48351 1.000 31.07070 ?  248 ASN   A C   1 
ATOM   1315 O  O   . ASN   A 1 171 ? 18.29533  -1.55153  -42.78981 1.000 33.06238 ?  248 ASN   A O   1 
ATOM   1316 C  CB  . ASN   A 1 171 ? 16.76255  1.45450   -44.06054 1.000 30.54523 ?  248 ASN   A CB  1 
ATOM   1317 C  CG  . ASN   A 1 171 ? 15.64990  1.92985   -44.95480 1.000 29.27962 ?  248 ASN   A CG  1 
ATOM   1318 O  OD1 . ASN   A 1 171 ? 15.82065  2.07488   -46.17625 1.000 29.72550 ?  248 ASN   A OD1 1 
ATOM   1319 N  ND2 . ASN   A 1 171 ? 14.49212  2.15113   -44.36450 1.000 25.80725 ?  248 ASN   A ND2 1 
ATOM   1320 N  N   . GLN   A 1 172 ? 19.23553  0.21678   -43.82201 1.000 28.93888 ?  249 GLN   A N   1 
ATOM   1321 C  CA  . GLN   A 1 172 ? 20.59200  -0.21750  -43.51700 1.000 29.15928 ?  249 GLN   A CA  1 
ATOM   1322 C  C   . GLN   A 1 172 ? 21.36401  0.84591   -42.76159 1.000 29.28085 ?  249 GLN   A C   1 
ATOM   1323 O  O   . GLN   A 1 172 ? 22.58089  0.94415   -42.90228 1.000 31.56468 ?  249 GLN   A O   1 
ATOM   1324 C  CB  . GLN   A 1 172 ? 21.34452  -0.60666  -44.79014 1.000 33.85096 ?  249 GLN   A CB  1 
ATOM   1325 C  CG  . GLN   A 1 172 ? 20.91744  -1.94155  -45.37775 1.000 31.20162 ?  249 GLN   A CG  1 
ATOM   1326 C  CD  . GLN   A 1 172 ? 20.95914  -1.93468  -46.89849 1.000 39.91915 ?  249 GLN   A CD  1 
ATOM   1327 O  OE1 . GLN   A 1 172 ? 21.98917  -1.62219  -47.50850 1.000 41.36207 ?  249 GLN   A OE1 1 
ATOM   1328 N  NE2 . GLN   A 1 172 ? 19.83083  -2.26962  -47.52029 1.000 42.31916 ?  249 GLN   A NE2 1 
ATOM   1329 N  N   . LEU   A 1 173 ? 20.68696  1.63698   -41.94027 1.000 28.87029 ?  250 LEU   A N   1 
ATOM   1330 C  CA  . LEU   A 1 173 ? 21.38468  2.71658   -41.26583 1.000 30.99924 ?  250 LEU   A CA  1 
ATOM   1331 C  C   . LEU   A 1 173 ? 22.37025  2.13857   -40.27037 1.000 30.76068 ?  250 LEU   A C   1 
ATOM   1332 O  O   . LEU   A 1 173 ? 22.02239  1.26339   -39.47644 1.000 30.52522 ?  250 LEU   A O   1 
ATOM   1333 C  CB  . LEU   A 1 173 ? 20.40728  3.64547   -40.55064 1.000 29.10383 ?  250 LEU   A CB  1 
ATOM   1334 C  CG  . LEU   A 1 173 ? 19.40851  4.45611   -41.37064 1.000 31.37971 ?  250 LEU   A CG  1 
ATOM   1335 C  CD1 . LEU   A 1 173 ? 18.62451  5.35736   -40.42908 1.000 30.25614 ?  250 LEU   A CD1 1 
ATOM   1336 C  CD2 . LEU   A 1 173 ? 20.12308  5.26893   -42.46360 1.000 31.15236 ?  250 LEU   A CD2 1 
ATOM   1337 N  N   . GLU   A 1 174 ? 23.59870  2.64284   -40.30271 1.000 32.32419 ?  251 GLU   A N   1 
ATOM   1338 C  CA  . GLU   A 1 174 ? 24.57079  2.33445   -39.26731 1.000 31.59777 ?  251 GLU   A CA  1 
ATOM   1339 C  C   . GLU   A 1 174 ? 24.72831  3.44128   -38.24314 1.000 33.76289 ?  251 GLU   A C   1 
ATOM   1340 O  O   . GLU   A 1 174 ? 25.14347  3.15224   -37.11876 1.000 33.72136 ?  251 GLU   A O   1 
ATOM   1341 C  CB  . GLU   A 1 174 ? 25.92813  2.03499   -39.89296 1.000 36.50708 ?  251 GLU   A CB  1 
ATOM   1342 C  CG  . GLU   A 1 174 ? 25.87725  0.84257   -40.82948 1.000 37.92109 ?  251 GLU   A CG  1 
ATOM   1343 C  CD  . GLU   A 1 174 ? 27.21301  0.52968   -41.44123 1.000 45.33561 ?  251 GLU   A CD  1 
ATOM   1344 O  OE1 . GLU   A 1 174 ? 28.23836  0.66183   -40.73075 1.000 44.37268 ?  251 GLU   A OE1 1 
ATOM   1345 O  OE2 . GLU   A 1 174 ? 27.23275  0.16565   -42.64027 1.000 53.58029 ?  251 GLU   A OE2 1 
ATOM   1346 N  N   . HIS   A 1 175 ? 24.41426  4.69344   -38.59719 1.000 34.85182 ?  252 HIS   A N   1 
ATOM   1347 C  CA  . HIS   A 1 175 ? 24.40116  5.78559   -37.63847 1.000 30.29829 ?  252 HIS   A CA  1 
ATOM   1348 C  C   . HIS   A 1 175 ? 23.23139  6.70327   -37.93637 1.000 34.41179 ?  252 HIS   A C   1 
ATOM   1349 O  O   . HIS   A 1 175 ? 22.57947  6.59857   -38.97663 1.000 34.91473 ?  252 HIS   A O   1 
ATOM   1350 C  CB  . HIS   A 1 175 ? 25.69786  6.59205   -37.67057 1.000 32.61529 ?  252 HIS   A CB  1 
ATOM   1351 C  CG  . HIS   A 1 175 ? 26.92613  5.75705   -37.54153 1.000 32.60444 ?  252 HIS   A CG  1 
ATOM   1352 N  ND1 . HIS   A 1 175 ? 27.50589  5.47136   -36.32585 1.000 31.06719 ?  252 HIS   A ND1 1 
ATOM   1353 C  CD2 . HIS   A 1 175 ? 27.67497  5.12750   -38.47450 1.000 31.27476 ?  252 HIS   A CD2 1 
ATOM   1354 C  CE1 . HIS   A 1 175 ? 28.56819  4.71100   -36.51578 1.000 32.68872 ?  252 HIS   A CE1 1 
ATOM   1355 N  NE2 . HIS   A 1 175 ? 28.69451  4.48932   -37.81120 1.000 35.58770 ?  252 HIS   A NE2 1 
ATOM   1356 N  N   . LEU   A 1 176 ? 22.97602  7.61871   -37.00869 1.000 32.71057 ?  253 LEU   A N   1 
ATOM   1357 C  CA  . LEU   A 1 176 ? 22.08169  8.71652   -37.31499 1.000 32.57428 ?  253 LEU   A CA  1 
ATOM   1358 C  C   . LEU   A 1 176 ? 22.84807  10.02506  -37.28220 1.000 33.25282 ?  253 LEU   A C   1 
ATOM   1359 O  O   . LEU   A 1 176 ? 23.75469  10.19186  -36.45941 1.000 35.42378 ?  253 LEU   A O   1 
ATOM   1360 C  CB  . LEU   A 1 176 ? 20.92733  8.82170   -36.32026 1.000 34.19196 ?  253 LEU   A CB  1 
ATOM   1361 C  CG  . LEU   A 1 176 ? 19.87443  7.74014   -36.17573 1.000 33.32058 ?  253 LEU   A CG  1 
ATOM   1362 C  CD1 . LEU   A 1 176 ? 18.90121  8.23399   -35.11051 1.000 34.20120 ?  253 LEU   A CD1 1 
ATOM   1363 C  CD2 . LEU   A 1 176 ? 19.18191  7.52708   -37.48625 1.000 32.76653 ?  253 LEU   A CD2 1 
ATOM   1364 N  N   . PRO   A 1 177 ? 22.49962  10.97925  -38.13085 1.000 31.32207 ?  254 PRO   A N   1 
ATOM   1365 C  CA  . PRO   A 1 177 ? 23.13413  12.29531  -38.02786 1.000 33.16291 ?  254 PRO   A CA  1 
ATOM   1366 C  C   . PRO   A 1 177 ? 22.76899  12.93140  -36.69685 1.000 32.10020 ?  254 PRO   A C   1 
ATOM   1367 O  O   . PRO   A 1 177 ? 21.62960  12.82919  -36.23783 1.000 31.21635 ?  254 PRO   A O   1 
ATOM   1368 C  CB  . PRO   A 1 177 ? 22.55255  13.07077  -39.21624 1.000 33.86834 ?  254 PRO   A CB  1 
ATOM   1369 C  CG  . PRO   A 1 177 ? 21.27050  12.38983  -39.54241 1.000 33.01479 ?  254 PRO   A CG  1 
ATOM   1370 C  CD  . PRO   A 1 177 ? 21.39393  10.94716  -39.10020 1.000 32.13385 ?  254 PRO   A CD  1 
ATOM   1371 N  N   . LYS   A 1 178 ? 23.75099  13.56728  -36.05282 1.000 30.03848 ?  255 LYS   A N   1 
ATOM   1372 C  CA  . LYS   A 1 178 ? 23.43746  14.22311  -34.78553 1.000 35.52330 ?  255 LYS   A CA  1 
ATOM   1373 C  C   . LYS   A 1 178 ? 22.39111  15.31701  -34.97893 1.000 36.56865 ?  255 LYS   A C   1 
ATOM   1374 O  O   . LYS   A 1 178 ? 21.61638  15.60609  -34.05688 1.000 32.29034 ?  255 LYS   A O   1 
ATOM   1375 C  CB  . LYS   A 1 178 ? 24.70171  14.78526  -34.12318 1.000 32.53691 ?  255 LYS   A CB  1 
ATOM   1376 C  CG  . LYS   A 1 178 ? 25.32910  15.98383  -34.79288 1.000 35.20219 ?  255 LYS   A CG  1 
ATOM   1377 C  CD  . LYS   A 1 178 ? 26.59029  16.41866  -34.03808 1.000 38.99107 ?  255 LYS   A CD  1 
ATOM   1378 C  CE  . LYS   A 1 178 ? 27.21486  17.67315  -34.64883 1.000 36.21784 ?  255 LYS   A CE  1 
ATOM   1379 N  NZ  . LYS   A 1 178 ? 27.04517  17.68291  -36.12905 1.000 34.39532 ?  255 LYS   A NZ  1 
ATOM   1380 N  N   . GLU   A 1 179 ? 22.31649  15.89915  -36.18319 1.000 31.99233 ?  256 GLU   A N   1 
ATOM   1381 C  CA  . GLU   A 1 179 ? 21.33379  16.94033  -36.43589 1.000 33.23761 ?  256 GLU   A CA  1 
ATOM   1382 C  C   . GLU   A 1 179 ? 19.89725  16.43038  -36.36365 1.000 34.29261 ?  256 GLU   A C   1 
ATOM   1383 O  O   . GLU   A 1 179 ? 18.96957  17.24610  -36.41596 1.000 34.42806 ?  256 GLU   A O   1 
ATOM   1384 C  CB  . GLU   A 1 179 ? 21.59886  17.59802  -37.79591 1.000 35.94760 ?  256 GLU   A CB  1 
ATOM   1385 C  CG  . GLU   A 1 179 ? 22.93029  18.34992  -37.89670 1.000 35.32538 ?  256 GLU   A CG  1 
ATOM   1386 C  CD  . GLU   A 1 179 ? 24.11330  17.42522  -38.17539 1.000 38.42453 ?  256 GLU   A CD  1 
ATOM   1387 O  OE1 . GLU   A 1 179 ? 23.90375  16.19160  -38.29405 1.000 36.21631 ?  256 GLU   A OE1 1 
ATOM   1388 O  OE2 . GLU   A 1 179 ? 25.25170  17.94013  -38.28512 1.000 41.57099 ?  256 GLU   A OE2 1 
ATOM   1389 N  N   . ILE   A 1 180 ? 19.68453  15.11654  -36.23200 1.000 33.55781 ?  257 ILE   A N   1 
ATOM   1390 C  CA  . ILE   A 1 180 ? 18.32506  14.62079  -36.03848 1.000 32.67789 ?  257 ILE   A CA  1 
ATOM   1391 C  C   . ILE   A 1 180 ? 17.72578  15.19948  -34.77100 1.000 33.27845 ?  257 ILE   A C   1 
ATOM   1392 O  O   . ILE   A 1 180 ? 16.50044  15.31592  -34.64736 1.000 35.33373 ?  257 ILE   A O   1 
ATOM   1393 C  CB  . ILE   A 1 180 ? 18.28664  13.08932  -36.00389 1.000 30.08433 ?  257 ILE   A CB  1 
ATOM   1394 C  CG1 . ILE   A 1 180 ? 16.83419  12.64154  -35.98451 1.000 33.23203 ?  257 ILE   A CG1 1 
ATOM   1395 C  CG2 . ILE   A 1 180 ? 18.95589  12.56557  -34.73003 1.000 34.88796 ?  257 ILE   A CG2 1 
ATOM   1396 C  CD1 . ILE   A 1 180 ? 16.13157  12.79662  -37.31030 1.000 40.62579 ?  257 ILE   A CD1 1 
ATOM   1397 N  N   . GLY   A 1 181 ? 18.57085  15.57456  -33.81368 1.000 33.62317 ?  258 GLY   A N   1 
ATOM   1398 C  CA  . GLY   A 1 181 ? 18.11829  16.22758  -32.59686 1.000 34.48726 ?  258 GLY   A CA  1 
ATOM   1399 C  C   . GLY   A 1 181 ? 17.48669  17.58881  -32.80371 1.000 33.56144 ?  258 GLY   A C   1 
ATOM   1400 O  O   . GLY   A 1 181 ? 16.88067  18.11122  -31.86229 1.000 34.84048 ?  258 GLY   A O   1 
ATOM   1401 N  N   . ASN   A 1 182 ? 17.62195  18.18688  -33.98985 1.000 32.79709 ?  259 ASN   A N   1 
ATOM   1402 C  CA  . ASN   A 1 182 ? 16.91619  19.43190  -34.25562 1.000 30.55261 ?  259 ASN   A CA  1 
ATOM   1403 C  C   . ASN   A 1 182 ? 15.45038  19.21117  -34.55877 1.000 34.30564 ?  259 ASN   A C   1 
ATOM   1404 O  O   . ASN   A 1 182 ? 14.70952  20.18714  -34.66723 1.000 36.37652 ?  259 ASN   A O   1 
ATOM   1405 C  CB  . ASN   A 1 182 ? 17.53467  20.18094  -35.43265 1.000 33.06929 ?  259 ASN   A CB  1 
ATOM   1406 C  CG  . ASN   A 1 182 ? 18.95400  20.62342  -35.16714 1.000 36.43157 ?  259 ASN   A CG  1 
ATOM   1407 O  OD1 . ASN   A 1 182 ? 19.41716  20.59537  -34.03444 1.000 36.04982 ?  259 ASN   A OD1 1 
ATOM   1408 N  ND2 . ASN   A 1 182 ? 19.64941  21.05225  -36.21656 1.000 36.92810 ?  259 ASN   A ND2 1 
ATOM   1409 N  N   . CYS   A 1 183 ? 15.02158  17.96302  -34.74005 1.000 38.08429 ?  260 CYS   A N   1 
ATOM   1410 C  CA  . CYS   A 1 183 ? 13.63066  17.65965  -35.07648 1.000 34.72002 ?  260 CYS   A CA  1 
ATOM   1411 C  C   . CYS   A 1 183 ? 12.81994  17.44795  -33.79565 1.000 35.96478 ?  260 CYS   A C   1 
ATOM   1412 O  O   . CYS   A 1 183 ? 12.23533  16.39513  -33.54861 1.000 34.95999 ?  260 CYS   A O   1 
ATOM   1413 C  CB  . CYS   A 1 183 ? 13.56809  16.44375  -35.99346 1.000 37.20287 ?  260 CYS   A CB  1 
ATOM   1414 S  SG  . CYS   A 1 183 ? 14.64609  16.52466  -37.47217 1.000 34.53819 ?  260 CYS   A SG  1 
ATOM   1415 N  N   . THR   A 1 184 ? 12.77765  18.50623  -32.98928 1.000 33.33721 ?  261 THR   A N   1 
ATOM   1416 C  CA  . THR   A 1 184 ? 12.22392  18.47964  -31.64556 1.000 34.88771 ?  261 THR   A CA  1 
ATOM   1417 C  C   . THR   A 1 184 ? 10.73087  18.18204  -31.59318 1.000 34.61508 ?  261 THR   A C   1 
ATOM   1418 O  O   . THR   A 1 184 ? 10.21318  18.06200  -30.48783 1.000 35.76374 ?  261 THR   A O   1 
ATOM   1419 C  CB  . THR   A 1 184 ? 12.51175  19.81740  -30.95551 1.000 38.40271 ?  261 THR   A CB  1 
ATOM   1420 O  OG1 . THR   A 1 184 ? 12.30705  20.88243  -31.89335 1.000 39.08290 ?  261 THR   A OG1 1 
ATOM   1421 C  CG2 . THR   A 1 184 ? 13.96659  19.86602  -30.47902 1.000 37.33404 ?  261 THR   A CG2 1 
ATOM   1422 N  N   . GLN   A 1 185 ? 10.01689  18.05054  -32.70875 1.000 35.90284 ?  262 GLN   A N   1 
ATOM   1423 C  CA  . GLN   A 1 185 ? 8.60905   17.67588  -32.62077 1.000 34.94914 ?  262 GLN   A CA  1 
ATOM   1424 C  C   . GLN   A 1 185 ? 8.36982   16.17741  -32.78396 1.000 33.72579 ?  262 GLN   A C   1 
ATOM   1425 O  O   . GLN   A 1 185 ? 7.22895   15.73356  -32.63184 1.000 34.89342 ?  262 GLN   A O   1 
ATOM   1426 C  CB  . GLN   A 1 185 ? 7.77900   18.42205  -33.66693 1.000 32.60810 ?  262 GLN   A CB  1 
ATOM   1427 C  CG  . GLN   A 1 185 ? 7.77460   19.93946  -33.51877 1.000 37.52689 ?  262 GLN   A CG  1 
ATOM   1428 C  CD  . GLN   A 1 185 ? 6.94988   20.38465  -32.34073 1.000 45.20152 ?  262 GLN   A CD  1 
ATOM   1429 O  OE1 . GLN   A 1 185 ? 7.48077   20.93978  -31.37377 1.000 51.51950 ?  262 GLN   A OE1 1 
ATOM   1430 N  NE2 . GLN   A 1 185 ? 5.63458   20.14544  -32.40714 1.000 46.14179 ?  262 GLN   A NE2 1 
ATOM   1431 N  N   . ILE   A 1 186 ? 9.40124   15.39035  -33.08937 1.000 31.19705 ?  263 ILE   A N   1 
ATOM   1432 C  CA  . ILE   A 1 186 ? 9.19315   13.96628  -33.35730 1.000 34.43100 ?  263 ILE   A CA  1 
ATOM   1433 C  C   . ILE   A 1 186 ? 8.55603   13.28514  -32.15325 1.000 31.89908 ?  263 ILE   A C   1 
ATOM   1434 O  O   . ILE   A 1 186 ? 9.05784   13.37384  -31.02636 1.000 34.50493 ?  263 ILE   A O   1 
ATOM   1435 C  CB  . ILE   A 1 186 ? 10.51862  13.28705  -33.73865 1.000 31.38904 ?  263 ILE   A CB  1 
ATOM   1436 C  CG1 . ILE   A 1 186 ? 10.99118  13.72960  -35.13374 1.000 32.03771 ?  263 ILE   A CG1 1 
ATOM   1437 C  CG2 . ILE   A 1 186 ? 10.37319  11.77212  -33.70117 1.000 31.87774 ?  263 ILE   A CG2 1 
ATOM   1438 C  CD1 . ILE   A 1 186 ? 12.32490  13.08712  -35.56105 1.000 29.55670 ?  263 ILE   A CD1 1 
ATOM   1439 N  N   . THR   A 1 187 ? 7.44921   12.58074  -32.38805 1.000 29.26688 ?  264 THR   A N   1 
ATOM   1440 C  CA  . THR   A 1 187 ? 6.85245   11.75435  -31.34944 1.000 33.45171 ?  264 THR   A CA  1 
ATOM   1441 C  C   . THR   A 1 187 ? 6.90922   10.25482  -31.63716 1.000 32.18070 ?  264 THR   A C   1 
ATOM   1442 O  O   . THR   A 1 187 ? 6.81977   9.46046   -30.69441 1.000 32.31641 ?  264 THR   A O   1 
ATOM   1443 C  CB  . THR   A 1 187 ? 5.39074   12.16363  -31.11264 1.000 33.46715 ?  264 THR   A CB  1 
ATOM   1444 O  OG1 . THR   A 1 187 ? 4.60035   11.73916  -32.22743 1.000 39.86392 ?  264 THR   A OG1 1 
ATOM   1445 C  CG2 . THR   A 1 187 ? 5.29067   13.65923  -31.00728 1.000 31.53057 ?  264 THR   A CG2 1 
ATOM   1446 N  N   . ASN   A 1 188 ? 7.05531   9.84611   -32.89804 1.000 31.50497 ?  265 ASN   A N   1 
ATOM   1447 C  CA  . ASN   A 1 188 ? 7.17761   8.43897   -33.25690 1.000 29.01505 ?  265 ASN   A CA  1 
ATOM   1448 C  C   . ASN   A 1 188 ? 8.39042   8.26340   -34.15410 1.000 29.84145 ?  265 ASN   A C   1 
ATOM   1449 O  O   . ASN   A 1 188 ? 8.38312   8.69841   -35.30924 1.000 32.81795 ?  265 ASN   A O   1 
ATOM   1450 C  CB  . ASN   A 1 188 ? 5.92530   7.93802   -33.95647 1.000 31.93870 ?  265 ASN   A CB  1 
ATOM   1451 C  CG  . ASN   A 1 188 ? 4.67802   8.41905   -33.30182 1.000 34.28252 ?  265 ASN   A CG  1 
ATOM   1452 O  OD1 . ASN   A 1 188 ? 4.33708   7.98667   -32.20165 1.000 38.32257 ?  265 ASN   A OD1 1 
ATOM   1453 N  ND2 . ASN   A 1 188 ? 3.97437   9.33001   -33.97002 1.000 36.48224 ?  265 ASN   A ND2 1 
ATOM   1454 N  N   . LEU   A 1 189 ? 9.41994   7.60821   -33.64062 1.000 27.21709 ?  266 LEU   A N   1 
ATOM   1455 C  CA  . LEU   A 1 189 ? 10.61730  7.31723   -34.41452 1.000 29.55950 ?  266 LEU   A CA  1 
ATOM   1456 C  C   . LEU   A 1 189 ? 10.79227  5.79965   -34.44706 1.000 26.68625 ?  266 LEU   A C   1 
ATOM   1457 O  O   . LEU   A 1 189 ? 10.99819  5.17427   -33.40418 1.000 29.58964 ?  266 LEU   A O   1 
ATOM   1458 C  CB  . LEU   A 1 189 ? 11.82423  8.03250   -33.80490 1.000 27.47718 ?  266 LEU   A CB  1 
ATOM   1459 C  CG  . LEU   A 1 189 ? 13.15536  7.92807   -34.55201 1.000 28.38642 ?  266 LEU   A CG  1 
ATOM   1460 C  CD1 . LEU   A 1 189 ? 13.04442  8.45435   -35.99518 1.000 25.17931 ?  266 LEU   A CD1 1 
ATOM   1461 C  CD2 . LEU   A 1 189 ? 14.21456  8.68472   -33.77981 1.000 27.71577 ?  266 LEU   A CD2 1 
ATOM   1462 N  N   . ASP   A 1 190 ? 10.67460  5.19247   -35.62554 1.000 26.83092 ?  267 ASP   A N   1 
ATOM   1463 C  CA  . ASP   A 1 190 ? 10.86738  3.75132   -35.76847 1.000 28.25733 ?  267 ASP   A CA  1 
ATOM   1464 C  C   . ASP   A 1 190 ? 12.15849  3.50285   -36.53647 1.000 29.70438 ?  267 ASP   A C   1 
ATOM   1465 O  O   . ASP   A 1 190 ? 12.27940  3.89413   -37.70115 1.000 29.25235 ?  267 ASP   A O   1 
ATOM   1466 C  CB  . ASP   A 1 190 ? 9.69356   3.05655   -36.46746 1.000 28.24766 ?  267 ASP   A CB  1 
ATOM   1467 C  CG  . ASP   A 1 190 ? 9.79621   1.51196   -36.37399 1.000 36.34583 ?  267 ASP   A CG  1 
ATOM   1468 O  OD1 . ASP   A 1 190 ? 10.78104  1.02801   -35.75032 1.000 31.29919 ?  267 ASP   A OD1 1 
ATOM   1469 O  OD2 . ASP   A 1 190 ? 8.91905   0.78297   -36.91530 1.000 35.09233 ?  267 ASP   A OD2 1 
ATOM   1470 N  N   . LEU   A 1 191 ? 13.10869  2.83363   -35.88380 1.000 27.23103 ?  268 LEU   A N   1 
ATOM   1471 C  CA  . LEU   A 1 191 ? 14.40751  2.52206   -36.46205 1.000 27.88056 ?  268 LEU   A CA  1 
ATOM   1472 C  C   . LEU   A 1 191 ? 14.69439  1.02109   -36.44352 1.000 30.80592 ?  268 LEU   A C   1 
ATOM   1473 O  O   . LEU   A 1 191 ? 15.84924  0.61338   -36.62198 1.000 26.87711 ?  268 LEU   A O   1 
ATOM   1474 C  CB  . LEU   A 1 191 ? 15.50200  3.29295   -35.72051 1.000 27.46539 ?  268 LEU   A CB  1 
ATOM   1475 C  CG  . LEU   A 1 191 ? 15.43830  4.83163   -35.76073 1.000 23.34737 ?  268 LEU   A CG  1 
ATOM   1476 C  CD1 . LEU   A 1 191 ? 16.36321  5.45751   -34.74706 1.000 23.70287 ?  268 LEU   A CD1 1 
ATOM   1477 C  CD2 . LEU   A 1 191 ? 15.83113  5.29022   -37.11209 1.000 27.11684 ?  268 LEU   A CD2 1 
ATOM   1478 N  N   . GLN   A 1 192 ? 13.66159  0.19590   -36.24532 1.000 29.19573 ?  269 GLN   A N   1 
ATOM   1479 C  CA  . GLN   A 1 192 ? 13.83450  -1.24723  -36.15770 1.000 28.25906 ?  269 GLN   A CA  1 
ATOM   1480 C  C   . GLN   A 1 192 ? 14.46082  -1.80461  -37.42634 1.000 29.05808 ?  269 GLN   A C   1 
ATOM   1481 O  O   . GLN   A 1 192 ? 14.30311  -1.25794  -38.51987 1.000 28.16737 ?  269 GLN   A O   1 
ATOM   1482 C  CB  . GLN   A 1 192 ? 12.49554  -1.93678  -35.92251 1.000 27.49521 ?  269 GLN   A CB  1 
ATOM   1483 C  CG  . GLN   A 1 192 ? 11.49961  -1.75601  -37.04249 1.000 28.52041 ?  269 GLN   A CG  1 
ATOM   1484 C  CD  . GLN   A 1 192 ? 10.24028  -2.59188  -36.83826 1.000 35.39644 ?  269 GLN   A CD  1 
ATOM   1485 O  OE1 . GLN   A 1 192 ? 10.31584  -3.73347  -36.37781 1.000 34.48702 ?  269 GLN   A OE1 1 
ATOM   1486 N  NE2 . GLN   A 1 192 ? 9.07582   -2.02987  -37.18758 1.000 34.27616 ?  269 GLN   A NE2 1 
ATOM   1487 N  N   . HIS   A 1 193 ? 15.17019  -2.91599  -37.26295 1.000 28.70403 ?  270 HIS   A N   1 
ATOM   1488 C  CA  . HIS   A 1 193 ? 15.75495  -3.66579  -38.36847 1.000 29.26981 ?  270 HIS   A CA  1 
ATOM   1489 C  C   . HIS   A 1 193 ? 16.57834  -2.75165  -39.28011 1.000 30.03816 ?  270 HIS   A C   1 
ATOM   1490 O  O   . HIS   A 1 193 ? 16.28448  -2.55955  -40.46036 1.000 31.85193 ?  270 HIS   A O   1 
ATOM   1491 C  CB  . HIS   A 1 193 ? 14.66553  -4.41808  -39.14886 1.000 31.16827 ?  270 HIS   A CB  1 
ATOM   1492 C  CG  . HIS   A 1 193 ? 14.08611  -5.59288  -38.41159 1.000 31.13871 ?  270 HIS   A CG  1 
ATOM   1493 N  ND1 . HIS   A 1 193 ? 12.95726  -5.49916  -37.61986 1.000 30.74635 ?  270 HIS   A ND1 1 
ATOM   1494 C  CD2 . HIS   A 1 193 ? 14.47712  -6.88874  -38.35486 1.000 27.61986 ?  270 HIS   A CD2 1 
ATOM   1495 C  CE1 . HIS   A 1 193 ? 12.67776  -6.68577  -37.11000 1.000 30.93188 ?  270 HIS   A CE1 1 
ATOM   1496 N  NE2 . HIS   A 1 193 ? 13.58930  -7.54423  -37.53440 1.000 31.59734 ?  270 HIS   A NE2 1 
ATOM   1497 N  N   . ASN   A 1 194 ? 17.62047  -2.17123  -38.68619 1.000 29.80580 ?  271 ASN   A N   1 
ATOM   1498 C  CA  . ASN   A 1 194 ? 18.70094  -1.50962  -39.40700 1.000 29.45712 ?  271 ASN   A CA  1 
ATOM   1499 C  C   . ASN   A 1 194 ? 20.01744  -2.14339  -38.98143 1.000 30.70760 ?  271 ASN   A C   1 
ATOM   1500 O  O   . ASN   A 1 194 ? 20.04582  -3.33252  -38.66188 1.000 31.73296 ?  271 ASN   A O   1 
ATOM   1501 C  CB  . ASN   A 1 194 ? 18.72177  -0.00605  -39.12886 1.000 29.30777 ?  271 ASN   A CB  1 
ATOM   1502 C  CG  . ASN   A 1 194 ? 17.77011  0.75588   -40.00211 1.000 30.58000 ?  271 ASN   A CG  1 
ATOM   1503 O  OD1 . ASN   A 1 194 ? 18.09451  1.08629   -41.15439 1.000 30.69530 ?  271 ASN   A OD1 1 
ATOM   1504 N  ND2 . ASN   A 1 194 ? 16.58394  1.04302   -39.47432 1.000 26.89177 ?  271 ASN   A ND2 1 
ATOM   1505 N  N   . GLU   A 1 195 ? 21.10153  -1.36883  -38.95487 1.000 27.96973 ?  272 GLU   A N   1 
ATOM   1506 C  CA  . GLU   A 1 195 ? 22.39530  -1.85056  -38.48795 1.000 31.04686 ?  272 GLU   A CA  1 
ATOM   1507 C  C   . GLU   A 1 195 ? 23.03059  -0.83893  -37.54191 1.000 31.08797 ?  272 GLU   A C   1 
ATOM   1508 O  O   . GLU   A 1 195 ? 24.25193  -0.66489  -37.52356 1.000 31.82569 ?  272 GLU   A O   1 
ATOM   1509 C  CB  . GLU   A 1 195 ? 23.33445  -2.15581  -39.66062 1.000 34.19317 ?  272 GLU   A CB  1 
ATOM   1510 C  CG  . GLU   A 1 195 ? 22.83686  -3.21296  -40.66264 1.000 35.81389 ?  272 GLU   A CG  1 
ATOM   1511 C  CD  . GLU   A 1 195 ? 23.01875  -4.66533  -40.18119 1.000 46.79245 ?  272 GLU   A CD  1 
ATOM   1512 O  OE1 . GLU   A 1 195 ? 23.77179  -4.90065  -39.20659 1.000 45.03240 ?  272 GLU   A OE1 1 
ATOM   1513 O  OE2 . GLU   A 1 195 ? 22.40987  -5.58639  -40.78892 1.000 53.69347 ?  272 GLU   A OE2 1 
ATOM   1514 N  N   . LEU   A 1 196 ? 22.20866  -0.17694  -36.72383 1.000 28.39579 ?  273 LEU   A N   1 
ATOM   1515 C  CA  . LEU   A 1 196 ? 22.66055  0.96851   -35.93850 1.000 29.09435 ?  273 LEU   A CA  1 
ATOM   1516 C  C   . LEU   A 1 196 ? 23.72556  0.57365   -34.93316 1.000 30.25287 ?  273 LEU   A C   1 
ATOM   1517 O  O   . LEU   A 1 196 ? 23.52185  -0.31844  -34.10904 1.000 28.03974 ?  273 LEU   A O   1 
ATOM   1518 C  CB  . LEU   A 1 196 ? 21.48210  1.60906   -35.21561 1.000 27.32820 ?  273 LEU   A CB  1 
ATOM   1519 C  CG  . LEU   A 1 196 ? 20.59240  2.37031   -36.19948 1.000 31.67766 ?  273 LEU   A CG  1 
ATOM   1520 C  CD1 . LEU   A 1 196 ? 19.33897  2.87605   -35.49528 1.000 27.01501 ?  273 LEU   A CD1 1 
ATOM   1521 C  CD2 . LEU   A 1 196 ? 21.38654  3.50709   -36.88371 1.000 26.29344 ?  273 LEU   A CD2 1 
ATOM   1522 N  N   . LEU   A 1 197 ? 24.86548  1.24861   -34.99569 1.000 28.37974 ?  274 LEU   A N   1 
ATOM   1523 C  CA  . LEU   A 1 197 ? 25.93531  0.95431   -34.05724 1.000 31.33572 ?  274 LEU   A CA  1 
ATOM   1524 C  C   . LEU   A 1 197 ? 25.85054  1.80220   -32.80351 1.000 31.99988 ?  274 LEU   A C   1 
ATOM   1525 O  O   . LEU   A 1 197 ? 26.42850  1.43345   -31.77491 1.000 31.03696 ?  274 LEU   A O   1 
ATOM   1526 C  CB  . LEU   A 1 197 ? 27.29437  1.16755   -34.72255 1.000 32.74458 ?  274 LEU   A CB  1 
ATOM   1527 C  CG  . LEU   A 1 197 ? 27.72775  0.12462   -35.74653 1.000 34.05202 ?  274 LEU   A CG  1 
ATOM   1528 C  CD1 . LEU   A 1 197 ? 28.86464  0.67905   -36.59838 1.000 31.94920 ?  274 LEU   A CD1 1 
ATOM   1529 C  CD2 . LEU   A 1 197 ? 28.13194  -1.16327  -35.06323 1.000 26.91672 ?  274 LEU   A CD2 1 
ATOM   1530 N  N   . ASP   A 1 198 ? 25.13061  2.91212   -32.86481 1.000 31.08992 ?  275 ASP   A N   1 
ATOM   1531 C  CA  . ASP   A 1 198 ? 24.98842  3.80567   -31.72912 1.000 31.29141 ?  275 ASP   A CA  1 
ATOM   1532 C  C   . ASP   A 1 198 ? 23.93473  4.83797   -32.08243 1.000 32.95233 ?  275 ASP   A C   1 
ATOM   1533 O  O   . ASP   A 1 198 ? 23.45820  4.91175   -33.21893 1.000 33.80017 ?  275 ASP   A O   1 
ATOM   1534 C  CB  . ASP   A 1 198 ? 26.30784  4.48584   -31.37991 1.000 30.68250 ?  275 ASP   A CB  1 
ATOM   1535 C  CG  . ASP   A 1 198 ? 26.99192  5.07730   -32.59811 1.000 35.31435 ?  275 ASP   A CG  1 
ATOM   1536 O  OD1 . ASP   A 1 198 ? 26.29211  5.63380   -33.48077 1.000 36.55863 ?  275 ASP   A OD1 1 
ATOM   1537 O  OD2 . ASP   A 1 198 ? 28.23402  4.98796   -32.67572 1.000 39.11963 ?  275 ASP   A OD2 1 
ATOM   1538 N  N   . LEU   A 1 199 ? 23.57831  5.62762   -31.09036 1.000 30.12202 ?  276 LEU   A N   1 
ATOM   1539 C  CA  . LEU   A 1 199 ? 22.67288  6.73545   -31.23694 1.000 32.14242 ?  276 LEU   A CA  1 
ATOM   1540 C  C   . LEU   A 1 199 ? 23.41751  8.02341   -30.91875 1.000 35.46706 ?  276 LEU   A C   1 
ATOM   1541 O  O   . LEU   A 1 199 ? 24.33728  8.01983   -30.09127 1.000 34.17620 ?  276 LEU   A O   1 
ATOM   1542 C  CB  . LEU   A 1 199 ? 21.47606  6.58362   -30.29488 1.000 32.65058 ?  276 LEU   A CB  1 
ATOM   1543 C  CG  . LEU   A 1 199 ? 20.59311  5.36745   -30.55793 1.000 33.42443 ?  276 LEU   A CG  1 
ATOM   1544 C  CD1 . LEU   A 1 199 ? 19.72883  5.09881   -29.34410 1.000 28.60464 ?  276 LEU   A CD1 1 
ATOM   1545 C  CD2 . LEU   A 1 199 ? 19.72470  5.64484   -31.76769 1.000 34.34246 ?  276 LEU   A CD2 1 
ATOM   1546 N  N   . PRO   A 1 200 ? 23.05714  9.13518   -31.55419 1.000 32.58586 ?  277 PRO   A N   1 
ATOM   1547 C  CA  . PRO   A 1 200 ? 23.71081  10.39896  -31.22027 1.000 34.01393 ?  277 PRO   A CA  1 
ATOM   1548 C  C   . PRO   A 1 200 ? 23.20840  10.89893  -29.87655 1.000 34.12988 ?  277 PRO   A C   1 
ATOM   1549 O  O   . PRO   A 1 200 ? 22.10547  10.56475  -29.43728 1.000 37.20577 ?  277 PRO   A O   1 
ATOM   1550 C  CB  . PRO   A 1 200 ? 23.29651  11.32228  -32.36572 1.000 35.31140 ?  277 PRO   A CB  1 
ATOM   1551 C  CG  . PRO   A 1 200 ? 21.95876  10.76928  -32.82632 1.000 33.27360 ?  277 PRO   A CG  1 
ATOM   1552 C  CD  . PRO   A 1 200 ? 21.89495  9.31975   -32.44258 1.000 32.50399 ?  277 PRO   A CD  1 
ATOM   1553 N  N   . ASP   A 1 201 ? 24.04618  11.68029  -29.20237 1.000 36.10562 ?  278 ASP   A N   1 
ATOM   1554 C  CA  . ASP   A 1 201 ? 23.69555  12.21026  -27.88889 1.000 35.95452 ?  278 ASP   A CA  1 
ATOM   1555 C  C   . ASP   A 1 201 ? 22.69642  13.35461  -27.95305 1.000 34.02997 ?  278 ASP   A C   1 
ATOM   1556 O  O   . ASP   A 1 201 ? 22.12962  13.71986  -26.92087 1.000 34.88390 ?  278 ASP   A O   1 
ATOM   1557 C  CB  . ASP   A 1 201 ? 24.95503  12.66889  -27.17347 1.000 37.36102 ?  278 ASP   A CB  1 
ATOM   1558 C  CG  . ASP   A 1 201 ? 25.88391  11.52655  -26.87585 1.000 40.52372 ?  278 ASP   A CG  1 
ATOM   1559 O  OD1 . ASP   A 1 201 ? 25.47662  10.62401  -26.10733 1.000 36.90695 ?  278 ASP   A OD1 1 
ATOM   1560 O  OD2 . ASP   A 1 201 ? 27.00921  11.52615  -27.42413 1.000 43.24985 ?  278 ASP   A OD2 1 
ATOM   1561 N  N   . THR   A 1 202 ? 22.49058  13.93765  -29.12976 1.000 32.48016 ?  279 THR   A N   1 
ATOM   1562 C  CA  . THR   A 1 202 ? 21.42793  14.89819  -29.34203 1.000 31.18363 ?  279 THR   A CA  1 
ATOM   1563 C  C   . THR   A 1 202 ? 20.04812  14.27290  -29.22517 1.000 35.62921 ?  279 THR   A C   1 
ATOM   1564 O  O   . THR   A 1 202 ? 19.05474  15.01146  -29.25006 1.000 33.90630 ?  279 THR   A O   1 
ATOM   1565 C  CB  . THR   A 1 202 ? 21.58437  15.53218  -30.72474 1.000 36.78065 ?  279 THR   A CB  1 
ATOM   1566 O  OG1 . THR   A 1 202 ? 21.66223  14.49638  -31.70244 1.000 33.46214 ?  279 THR   A OG1 1 
ATOM   1567 C  CG2 . THR   A 1 202 ? 22.85351  16.38136  -30.80751 1.000 32.25880 ?  279 THR   A CG2 1 
ATOM   1568 N  N   . ILE   A 1 203 ? 19.96519  12.93916  -29.09391 1.000 34.84483 ?  280 ILE   A N   1 
ATOM   1569 C  CA  . ILE   A 1 203 ? 18.67297  12.25624  -29.04929 1.000 32.31812 ?  280 ILE   A CA  1 
ATOM   1570 C  C   . ILE   A 1 203 ? 17.81984  12.77251  -27.89896 1.000 32.94277 ?  280 ILE   A C   1 
ATOM   1571 O  O   . ILE   A 1 203 ? 16.58591  12.80262  -27.99552 1.000 32.28110 ?  280 ILE   A O   1 
ATOM   1572 C  CB  . ILE   A 1 203 ? 18.87537  10.72448  -28.96441 1.000 35.31140 ?  280 ILE   A CB  1 
ATOM   1573 C  CG1 . ILE   A 1 203 ? 17.55707  10.00152  -29.19782 1.000 33.60704 ?  280 ILE   A CG1 1 
ATOM   1574 C  CG2 . ILE   A 1 203 ? 19.42762  10.31170  -27.61683 1.000 32.73652 ?  280 ILE   A CG2 1 
ATOM   1575 C  CD1 . ILE   A 1 203 ? 16.95257  10.28646  -30.54004 1.000 38.70766 ?  280 ILE   A CD1 1 
ATOM   1576 N  N   . GLY   A 1 204 ? 18.45149  13.19458  -26.80075 1.000 34.05483 ?  281 GLY   A N   1 
ATOM   1577 C  CA  . GLY   A 1 204 ? 17.71726  13.71895  -25.65810 1.000 33.24199 ?  281 GLY   A CA  1 
ATOM   1578 C  C   . GLY   A 1 204 ? 16.99786  15.02855  -25.92625 1.000 34.73778 ?  281 GLY   A C   1 
ATOM   1579 O  O   . GLY   A 1 204 ? 16.14550  15.43309  -25.12419 1.000 32.11058 ?  281 GLY   A O   1 
ATOM   1580 N  N   . ASN   A 1 205 ? 17.32565  15.70973  -27.03098 1.000 33.83032 ?  282 ASN   A N   1 
ATOM   1581 C  CA  . ASN   A 1 205 ? 16.59152  16.91357  -27.41680 1.000 34.25127 ?  282 ASN   A CA  1 
ATOM   1582 C  C   . ASN   A 1 205 ? 15.13580  16.62604  -27.77535 1.000 37.98437 ?  282 ASN   A C   1 
ATOM   1583 O  O   . ASN   A 1 205 ? 14.31723  17.54882  -27.74575 1.000 37.55727 ?  282 ASN   A O   1 
ATOM   1584 C  CB  . ASN   A 1 205 ? 17.24792  17.60026  -28.62040 1.000 36.20783 ?  282 ASN   A CB  1 
ATOM   1585 C  CG  . ASN   A 1 205 ? 18.67328  18.02669  -28.35369 1.000 36.02229 ?  282 ASN   A CG  1 
ATOM   1586 O  OD1 . ASN   A 1 205 ? 19.14333  18.00302  -27.21866 1.000 39.24164 ?  282 ASN   A OD1 1 
ATOM   1587 N  ND2 . ASN   A 1 205 ? 19.36426  18.43719  -29.40053 1.000 34.95616 ?  282 ASN   A ND2 1 
ATOM   1588 N  N   . LEU   A 1 206 ? 14.79357  15.38343  -28.13537 1.000 34.16489 ?  283 LEU   A N   1 
ATOM   1589 C  CA  . LEU   A 1 206 ? 13.45206  15.07366  -28.63412 1.000 34.80233 ?  283 LEU   A CA  1 
ATOM   1590 C  C   . LEU   A 1 206 ? 12.52552  14.88293  -27.44288 1.000 34.03400 ?  283 LEU   A C   1 
ATOM   1591 O  O   . LEU   A 1 206 ? 12.14584  13.76415  -27.07462 1.000 32.74628 ?  283 LEU   A O   1 
ATOM   1592 C  CB  . LEU   A 1 206 ? 13.46015  13.83518  -29.52095 1.000 33.54425 ?  283 LEU   A CB  1 
ATOM   1593 C  CG  . LEU   A 1 206 ? 14.43991  13.75561  -30.69394 1.000 37.25007 ?  283 LEU   A CG  1 
ATOM   1594 C  CD1 . LEU   A 1 206 ? 14.09285  12.54520  -31.56107 1.000 30.77829 ?  283 LEU   A CD1 1 
ATOM   1595 C  CD2 . LEU   A 1 206 ? 14.44985  15.04237  -31.51573 1.000 32.39767 ?  283 LEU   A CD2 1 
ATOM   1596 N  N   . SER   A 1 207 ? 12.13405  16.00621  -26.84693 1.000 31.32845 ?  284 SER   A N   1 
ATOM   1597 C  CA  . SER   A 1 207 ? 11.36944  15.93385  -25.61029 1.000 34.02279 ?  284 SER   A CA  1 
ATOM   1598 C  C   . SER   A 1 207 ? 9.90586   15.57342  -25.82856 1.000 35.27543 ?  284 SER   A C   1 
ATOM   1599 O  O   . SER   A 1 207 ? 9.15722   15.50531  -24.85043 1.000 34.71041 ?  284 SER   A O   1 
ATOM   1600 C  CB  . SER   A 1 207 ? 11.46935  17.24928  -24.85400 1.000 32.36778 ?  284 SER   A CB  1 
ATOM   1601 O  OG  . SER   A 1 207 ? 11.07564  18.30873  -25.68709 1.000 35.40761 ?  284 SER   A OG  1 
ATOM   1602 N  N   . SER   A 1 208 ? 9.47919   15.34004  -27.06949 1.000 32.34268 ?  285 SER   A N   1 
ATOM   1603 C  CA  . SER   A 1 208 ? 8.12796   14.88466  -27.33928 1.000 31.07987 ?  285 SER   A CA  1 
ATOM   1604 C  C   . SER   A 1 208 ? 8.07439   13.44347  -27.81302 1.000 31.79972 ?  285 SER   A C   1 
ATOM   1605 O  O   . SER   A 1 208 ? 6.97483   12.90908  -27.96658 1.000 30.84439 ?  285 SER   A O   1 
ATOM   1606 C  CB  . SER   A 1 208 ? 7.45987   15.78182  -28.39263 1.000 33.25845 ?  285 SER   A CB  1 
ATOM   1607 O  OG  . SER   A 1 208 ? 7.47654   17.13772  -27.98262 1.000 40.06833 ?  285 SER   A OG  1 
ATOM   1608 N  N   . LEU   A 1 209 ? 9.22684   12.82801  -28.08852 1.000 34.54098 ?  286 LEU   A N   1 
ATOM   1609 C  CA  . LEU   A 1 209 ? 9.31852   11.42492  -28.48138 1.000 32.14863 ?  286 LEU   A CA  1 
ATOM   1610 C  C   . LEU   A 1 209 ? 8.62316   10.54536  -27.47081 1.000 30.43819 ?  286 LEU   A C   1 
ATOM   1611 O  O   . LEU   A 1 209 ? 9.00359   10.51949  -26.30017 1.000 30.53829 ?  286 LEU   A O   1 
ATOM   1612 C  CB  . LEU   A 1 209 ? 10.78928  11.01401  -28.58990 1.000 30.80764 ?  286 LEU   A CB  1 
ATOM   1613 C  CG  . LEU   A 1 209 ? 11.13590  9.60074   -29.06950 1.000 29.55948 ?  286 LEU   A CG  1 
ATOM   1614 C  CD1 . LEU   A 1 209 ? 10.68463  9.34718   -30.50594 1.000 31.25550 ?  286 LEU   A CD1 1 
ATOM   1615 C  CD2 . LEU   A 1 209 ? 12.62711  9.33257   -28.92619 1.000 28.65023 ?  286 LEU   A CD2 1 
ATOM   1616 N  N   . SER   A 1 210 ? 7.59623   9.81801   -27.91213 1.000 30.76052 ?  287 SER   A N   1 
ATOM   1617 C  CA  . SER   A 1 210 ? 6.91932   8.89701   -27.01197 1.000 32.83170 ?  287 SER   A CA  1 
ATOM   1618 C  C   . SER   A 1 210 ? 7.05005   7.43096   -27.39975 1.000 32.24481 ?  287 SER   A C   1 
ATOM   1619 O  O   . SER   A 1 210 ? 6.85031   6.56803   -26.53303 1.000 32.50679 ?  287 SER   A O   1 
ATOM   1620 C  CB  . SER   A 1 210 ? 5.43000   9.25223   -26.88871 1.000 34.51794 ?  287 SER   A CB  1 
ATOM   1621 O  OG  . SER   A 1 210 ? 4.85506   9.41898   -28.15777 1.000 40.71510 ?  287 SER   A OG  1 
ATOM   1622 N  N   . ARG   A 1 211 ? 7.37850   7.12573   -28.65635 1.000 31.46406 ?  288 ARG   A N   1 
ATOM   1623 C  CA  . ARG   A 1 211 ? 7.59228   5.76144   -29.12838 1.000 33.01127 ?  288 ARG   A CA  1 
ATOM   1624 C  C   . ARG   A 1 211 ? 8.91047   5.71814   -29.88586 1.000 31.19858 ?  288 ARG   A C   1 
ATOM   1625 O  O   . ARG   A 1 211 ? 9.07701   6.42661   -30.88317 1.000 28.94662 ?  288 ARG   A O   1 
ATOM   1626 C  CB  . ARG   A 1 211 ? 6.44641   5.28898   -30.02645 1.000 34.97034 ?  288 ARG   A CB  1 
ATOM   1627 C  CG  . ARG   A 1 211 ? 5.25420   4.76009   -29.27838 1.000 41.03274 ?  288 ARG   A CG  1 
ATOM   1628 C  CD  . ARG   A 1 211 ? 4.13329   4.41191   -30.22440 1.000 44.15811 ?  288 ARG   A CD  1 
ATOM   1629 N  NE  . ARG   A 1 211 ? 3.18666   5.51470   -30.32755 1.000 51.43095 ?  288 ARG   A NE  1 
ATOM   1630 C  CZ  . ARG   A 1 211 ? 2.06241   5.59590   -29.62780 1.000 58.22210 ?  288 ARG   A CZ  1 
ATOM   1631 N  NH1 . ARG   A 1 211 ? 1.69921   4.63575   -28.78641 1.000 54.80367 ?  288 ARG   A NH1 1 
ATOM   1632 N  NH2 . ARG   A 1 211 ? 1.28343   6.66507   -29.77419 1.000 60.47734 ?  288 ARG   A NH2 1 
ATOM   1633 N  N   . LEU   A 1 212 ? 9.83738   4.88940   -29.41163 1.000 28.98362 ?  289 LEU   A N   1 
ATOM   1634 C  CA  . LEU   A 1 212 ? 11.17110  4.77153   -29.98521 1.000 29.35340 ?  289 LEU   A CA  1 
ATOM   1635 C  C   . LEU   A 1 212 ? 11.44669  3.29579   -30.25928 1.000 32.01157 ?  289 LEU   A C   1 
ATOM   1636 O  O   . LEU   A 1 212 ? 11.66837  2.51331   -29.32302 1.000 31.68381 ?  289 LEU   A O   1 
ATOM   1637 C  CB  . LEU   A 1 212 ? 12.21807  5.36983   -29.04306 1.000 26.34441 ?  289 LEU   A CB  1 
ATOM   1638 C  CG  . LEU   A 1 212 ? 13.67504  5.18759   -29.48258 1.000 29.26971 ?  289 LEU   A CG  1 
ATOM   1639 C  CD1 . LEU   A 1 212 ? 13.91301  5.75026   -30.89208 1.000 25.07261 ?  289 LEU   A CD1 1 
ATOM   1640 C  CD2 . LEU   A 1 212 ? 14.65852  5.78323   -28.47406 1.000 24.70651 ?  289 LEU   A CD2 1 
ATOM   1641 N  N   . GLY   A 1 213 ? 11.42791  2.90966   -31.53869 1.000 31.57162 ?  290 GLY   A N   1 
ATOM   1642 C  CA  . GLY   A 1 213 ? 11.68799  1.52650   -31.90865 1.000 26.94457 ?  290 GLY   A CA  1 
ATOM   1643 C  C   . GLY   A 1 213 ? 13.10319  1.28158   -32.39734 1.000 25.60479 ?  290 GLY   A C   1 
ATOM   1644 O  O   . GLY   A 1 213 ? 13.50032  1.77802   -33.44641 1.000 28.27976 ?  290 GLY   A O   1 
ATOM   1645 N  N   . LEU   A 1 214 ? 13.88072  0.51075   -31.65087 1.000 26.85660 ?  291 LEU   A N   1 
ATOM   1646 C  CA  . LEU   A 1 214 ? 15.27295  0.24390   -31.98921 1.000 25.92947 ?  291 LEU   A CA  1 
ATOM   1647 C  C   . LEU   A 1 214 ? 15.54360  -1.25243  -32.09302 1.000 27.92150 ?  291 LEU   A C   1 
ATOM   1648 O  O   . LEU   A 1 214 ? 16.70301  -1.68127  -32.07898 1.000 27.50932 ?  291 LEU   A O   1 
ATOM   1649 C  CB  . LEU   A 1 214 ? 16.19734  0.89214   -30.96087 1.000 26.87959 ?  291 LEU   A CB  1 
ATOM   1650 C  CG  . LEU   A 1 214 ? 16.08816  2.42296   -30.85396 1.000 26.25462 ?  291 LEU   A CG  1 
ATOM   1651 C  CD1 . LEU   A 1 214 ? 16.71627  2.94000   -29.58180 1.000 24.19558 ?  291 LEU   A CD1 1 
ATOM   1652 C  CD2 . LEU   A 1 214 ? 16.77974  3.05299   -32.04086 1.000 27.05387 ?  291 LEU   A CD2 1 
ATOM   1653 N  N   . ARG   A 1 215 ? 14.49179  -2.05321  -32.21409 1.000 26.63101 ?  292 ARG   A N   1 
ATOM   1654 C  CA  . ARG   A 1 215 ? 14.65125  -3.49683  -32.20841 1.000 27.22535 ?  292 ARG   A CA  1 
ATOM   1655 C  C   . ARG   A 1 215 ? 15.43668  -3.95494  -33.43919 1.000 27.73904 ?  292 ARG   A C   1 
ATOM   1656 O  O   . ARG   A 1 215 ? 15.25571  -3.43394  -34.54462 1.000 29.05969 ?  292 ARG   A O   1 
ATOM   1657 C  CB  . ARG   A 1 215 ? 13.26199  -4.16069  -32.14054 1.000 29.27965 ?  292 ARG   A CB  1 
ATOM   1658 C  CG  . ARG   A 1 215 ? 12.77343  -4.70101  -33.47115 1.000 33.85410 ?  292 ARG   A CG  1 
ATOM   1659 C  CD  . ARG   A 1 215 ? 11.34768  -4.35088  -33.81153 1.000 30.68949 ?  292 ARG   A CD  1 
ATOM   1660 N  NE  . ARG   A 1 215 ? 10.37939  -5.07428  -33.00773 1.000 31.66704 ?  292 ARG   A NE  1 
ATOM   1661 C  CZ  . ARG   A 1 215 ? 9.14600   -5.35489  -33.40911 1.000 33.13356 ?  292 ARG   A CZ  1 
ATOM   1662 N  NH1 . ARG   A 1 215 ? 8.72838   -5.04434  -34.62182 1.000 31.48437 ?  292 ARG   A NH1 1 
ATOM   1663 N  NH2 . ARG   A 1 215 ? 8.31481   -5.97869  -32.57678 1.000 36.24173 ?  292 ARG   A NH2 1 
ATOM   1664 N  N   . TYR   A 1 216 ? 16.32861  -4.92987  -33.23522 1.000 27.39198 ?  293 TYR   A N   1 
ATOM   1665 C  CA  . TYR   A 1 216 ? 17.12333  -5.52718  -34.30792 1.000 28.10644 ?  293 TYR   A CA  1 
ATOM   1666 C  C   . TYR   A 1 216 ? 18.14519  -4.55355  -34.89229 1.000 28.92648 ?  293 TYR   A C   1 
ATOM   1667 O  O   . TYR   A 1 216 ? 18.11418  -4.23655  -36.08878 1.000 29.01211 ?  293 TYR   A O   1 
ATOM   1668 C  CB  . TYR   A 1 216 ? 16.22175  -6.07151  -35.41630 1.000 27.04071 ?  293 TYR   A CB  1 
ATOM   1669 C  CG  . TYR   A 1 216 ? 15.67067  -7.45401  -35.13603 1.000 31.74096 ?  293 TYR   A CG  1 
ATOM   1670 C  CD1 . TYR   A 1 216 ? 14.65629  -7.64276  -34.20818 1.000 31.58071 ?  293 TYR   A CD1 1 
ATOM   1671 C  CD2 . TYR   A 1 216 ? 16.16371  -8.57073  -35.80834 1.000 32.24889 ?  293 TYR   A CD2 1 
ATOM   1672 C  CE1 . TYR   A 1 216 ? 14.14561  -8.90418  -33.94716 1.000 34.51971 ?  293 TYR   A CE1 1 
ATOM   1673 C  CE2 . TYR   A 1 216 ? 15.65694  -9.83189  -35.55820 1.000 35.52892 ?  293 TYR   A CE2 1 
ATOM   1674 C  CZ  . TYR   A 1 216 ? 14.64406  -9.99474  -34.62886 1.000 37.35241 ?  293 TYR   A CZ  1 
ATOM   1675 O  OH  . TYR   A 1 216 ? 14.13374  -11.25319 -34.38417 1.000 37.29785 ?  293 TYR   A OH  1 
ATOM   1676 N  N   . ASN   A 1 217 ? 19.06762  -4.09801  -34.05147 1.000 27.47266 ?  294 ASN   A N   1 
ATOM   1677 C  CA  . ASN   A 1 217 ? 20.17109  -3.24778  -34.46205 1.000 28.79598 ?  294 ASN   A CA  1 
ATOM   1678 C  C   . ASN   A 1 217 ? 21.43666  -3.77374  -33.78954 1.000 31.01597 ?  294 ASN   A C   1 
ATOM   1679 O  O   . ASN   A 1 217 ? 21.45834  -4.87002  -33.21820 1.000 30.62716 ?  294 ASN   A O   1 
ATOM   1680 C  CB  . ASN   A 1 217 ? 19.85169  -1.78441  -34.13857 1.000 26.36509 ?  294 ASN   A CB  1 
ATOM   1681 C  CG  . ASN   A 1 217 ? 18.89359  -1.17865  -35.14320 1.000 26.76712 ?  294 ASN   A CG  1 
ATOM   1682 O  OD1 . ASN   A 1 217 ? 19.21834  -1.06357  -36.31930 1.000 27.22522 ?  294 ASN   A OD1 1 
ATOM   1683 N  ND2 . ASN   A 1 217 ? 17.70861  -0.80702  -34.69465 1.000 24.12994 ?  294 ASN   A ND2 1 
ATOM   1684 N  N   . ARG   A 1 218 ? 22.51745  -3.00891  -33.87854 1.000 31.02157 ?  295 ARG   A N   1 
ATOM   1685 C  CA  . ARG   A 1 218 ? 23.78558  -3.43626  -33.30574 1.000 29.88469 ?  295 ARG   A CA  1 
ATOM   1686 C  C   . ARG   A 1 218 ? 24.21208  -2.54099  -32.15295 1.000 27.39766 ?  295 ARG   A C   1 
ATOM   1687 O  O   . ARG   A 1 218 ? 25.40312  -2.38660  -31.89620 1.000 30.30575 ?  295 ARG   A O   1 
ATOM   1688 C  CB  . ARG   A 1 218 ? 24.87372  -3.49852  -34.37611 1.000 29.85727 ?  295 ARG   A CB  1 
ATOM   1689 C  CG  . ARG   A 1 218 ? 24.63204  -4.56345  -35.45471 1.000 33.68803 ?  295 ARG   A CG  1 
ATOM   1690 C  CD  . ARG   A 1 218 ? 25.82316  -4.68761  -36.42322 1.000 33.56585 ?  295 ARG   A CD  1 
ATOM   1691 N  NE  . ARG   A 1 218 ? 25.95648  -3.49698  -37.25670 1.000 45.77515 ?  295 ARG   A NE  1 
ATOM   1692 C  CZ  . ARG   A 1 218 ? 26.96466  -3.25487  -38.09262 1.000 44.49325 ?  295 ARG   A CZ  1 
ATOM   1693 N  NH1 . ARG   A 1 218 ? 27.98314  -4.09714  -38.21559 1.000 35.23607 ?  295 ARG   A NH1 1 
ATOM   1694 N  NH2 . ARG   A 1 218 ? 26.95066  -2.13612  -38.82156 1.000 37.36465 ?  295 ARG   A NH2 1 
ATOM   1695 N  N   . LEU   A 1 219 ? 23.24295  -1.94469  -31.45914 1.000 30.06496 ?  296 LEU   A N   1 
ATOM   1696 C  CA  . LEU   A 1 219 ? 23.53476  -1.03339  -30.35795 1.000 30.23326 ?  296 LEU   A CA  1 
ATOM   1697 C  C   . LEU   A 1 219 ? 24.25456  -1.76742  -29.23325 1.000 30.30766 ?  296 LEU   A C   1 
ATOM   1698 O  O   . LEU   A 1 219 ? 23.85440  -2.86345  -28.83465 1.000 34.38010 ?  296 LEU   A O   1 
ATOM   1699 C  CB  . LEU   A 1 219 ? 22.24028  -0.40498  -29.83122 1.000 26.80442 ?  296 LEU   A CB  1 
ATOM   1700 C  CG  . LEU   A 1 219 ? 21.38242  0.45114   -30.76677 1.000 28.80734 ?  296 LEU   A CG  1 
ATOM   1701 C  CD1 . LEU   A 1 219 ? 20.12411  0.92451   -30.05573 1.000 27.94803 ?  296 LEU   A CD1 1 
ATOM   1702 C  CD2 . LEU   A 1 219 ? 22.14894  1.64392   -31.33250 1.000 27.83058 ?  296 LEU   A CD2 1 
ATOM   1703 N  N   . SER   A 1 220 ? 25.32515  -1.16594  -28.72362 1.000 30.35563 ?  297 SER   A N   1 
ATOM   1704 C  CA  . SER   A 1 220 ? 26.05855  -1.72991  -27.59754 1.000 34.80399 ?  297 SER   A CA  1 
ATOM   1705 C  C   . SER   A 1 220 ? 25.94577  -0.87370  -26.34816 1.000 33.23265 ?  297 SER   A C   1 
ATOM   1706 O  O   . SER   A 1 220 ? 26.41603  -1.27621  -25.28333 1.000 36.45215 ?  297 SER   A O   1 
ATOM   1707 C  CB  . SER   A 1 220 ? 27.53274  -1.93583  -27.96254 1.000 34.34790 ?  297 SER   A CB  1 
ATOM   1708 O  OG  . SER   A 1 220 ? 28.12348  -0.71887  -28.36410 1.000 40.51651 ?  297 SER   A OG  1 
ATOM   1709 N  N   . ALA   A 1 221 ? 25.28667  0.26854   -26.44067 1.000 35.75037 ?  298 ALA   A N   1 
ATOM   1710 C  CA  . ALA   A 1 221 ? 25.13272  1.16239   -25.31117 1.000 32.03818 ?  298 ALA   A CA  1 
ATOM   1711 C  C   . ALA   A 1 221 ? 24.00138  2.12580   -25.63689 1.000 34.39006 ?  298 ALA   A C   1 
ATOM   1712 O  O   . ALA   A 1 221 ? 23.67269  2.34973   -26.80459 1.000 33.36907 ?  298 ALA   A O   1 
ATOM   1713 C  CB  . ALA   A 1 221 ? 26.43536  1.91049   -25.03350 1.000 32.62556 ?  298 ALA   A CB  1 
ATOM   1714 N  N   . ILE   A 1 222 ? 23.39467  2.67434   -24.59358 1.000 32.11631 ?  299 ILE   A N   1 
ATOM   1715 C  CA  . ILE   A 1 222 ? 22.39237  3.71624   -24.77011 1.000 33.38358 ?  299 ILE   A CA  1 
ATOM   1716 C  C   . ILE   A 1 222 ? 22.98215  5.03806   -24.28758 1.000 37.82459 ?  299 ILE   A C   1 
ATOM   1717 O  O   . ILE   A 1 222 ? 23.71181  5.08198   -23.27793 1.000 35.47952 ?  299 ILE   A O   1 
ATOM   1718 C  CB  . ILE   A 1 222 ? 21.08817  3.38846   -24.02972 1.000 33.21536 ?  299 ILE   A CB  1 
ATOM   1719 C  CG1 . ILE   A 1 222 ? 20.53151  2.03362   -24.48430 1.000 36.72434 ?  299 ILE   A CG1 1 
ATOM   1720 C  CG2 . ILE   A 1 222 ? 20.08184  4.48696   -24.26963 1.000 35.51216 ?  299 ILE   A CG2 1 
ATOM   1721 C  CD1 . ILE   A 1 222 ? 20.17996  1.94745   -26.00557 1.000 32.89313 ?  299 ILE   A CD1 1 
ATOM   1722 N  N   . PRO   A 1 223 ? 22.71498  6.13510   -24.98700 1.000 35.63391 ?  300 PRO   A N   1 
ATOM   1723 C  CA  . PRO   A 1 223 ? 23.20781  7.43494   -24.51894 1.000 34.31768 ?  300 PRO   A CA  1 
ATOM   1724 C  C   . PRO   A 1 223 ? 22.45394  7.85962   -23.26742 1.000 36.77094 ?  300 PRO   A C   1 
ATOM   1725 O  O   . PRO   A 1 223 ? 21.22419  7.80226   -23.21184 1.000 35.27756 ?  300 PRO   A O   1 
ATOM   1726 C  CB  . PRO   A 1 223 ? 22.92687  8.37394   -25.69521 1.000 33.39178 ?  300 PRO   A CB  1 
ATOM   1727 C  CG  . PRO   A 1 223 ? 22.51991  7.48635   -26.84486 1.000 36.14621 ?  300 PRO   A CG  1 
ATOM   1728 C  CD  . PRO   A 1 223 ? 21.95303  6.24153   -26.23819 1.000 32.65075 ?  300 PRO   A CD  1 
ATOM   1729 N  N   . ARG   A 1 224 ? 23.20777  8.27366   -22.25159 1.000 38.30520 ?  301 ARG   A N   1 
ATOM   1730 C  CA  . ARG   A 1 224 ? 22.59129  8.81330   -21.04971 1.000 39.80026 ?  301 ARG   A CA  1 
ATOM   1731 C  C   . ARG   A 1 224 ? 21.62428  9.93973   -21.38307 1.000 34.65687 ?  301 ARG   A C   1 
ATOM   1732 O  O   . ARG   A 1 224 ? 20.66699  10.17169  -20.64426 1.000 38.68114 ?  301 ARG   A O   1 
ATOM   1733 C  CB  . ARG   A 1 224 ? 23.68788  9.27247   -20.09607 1.000 42.67222 ?  301 ARG   A CB  1 
ATOM   1734 C  CG  . ARG   A 1 224 ? 23.28948  10.31877  -19.11982 1.000 48.51424 ?  301 ARG   A CG  1 
ATOM   1735 C  CD  . ARG   A 1 224 ? 24.54003  11.07482  -18.69372 1.000 61.65039 ?  301 ARG   A CD  1 
ATOM   1736 N  NE  . ARG   A 1 224 ? 24.25599  12.11208  -17.70941 1.000 69.60740 ?  301 ARG   A NE  1 
ATOM   1737 C  CZ  . ARG   A 1 224 ? 23.95593  11.86268  -16.44346 1.000 63.77525 ?  301 ARG   A CZ  1 
ATOM   1738 N  NH1 . ARG   A 1 224 ? 23.87167  10.62359  -15.98839 1.000 63.35622 ?  301 ARG   A NH1 1 
ATOM   1739 N  NH2 . ARG   A 1 224 ? 23.72368  12.87993  -15.61936 1.000 67.47352 ?  301 ARG   A NH2 1 
ATOM   1740 N  N   . SER   A 1 225 ? 21.82918  10.61755  -22.50949 1.000 34.98121 ?  302 SER   A N   1 
ATOM   1741 C  CA  . SER   A 1 225 ? 20.89719  11.65093  -22.95353 1.000 36.97952 ?  302 SER   A CA  1 
ATOM   1742 C  C   . SER   A 1 225 ? 19.48004  11.13139  -23.16157 1.000 35.81560 ?  302 SER   A C   1 
ATOM   1743 O  O   . SER   A 1 225 ? 18.53380  11.92969  -23.12717 1.000 33.90035 ?  302 SER   A O   1 
ATOM   1744 C  CB  . SER   A 1 225 ? 21.38670  12.27760  -24.25949 1.000 33.70824 ?  302 SER   A CB  1 
ATOM   1745 O  OG  . SER   A 1 225 ? 22.65982  12.86648  -24.07522 1.000 38.01128 ?  302 SER   A OG  1 
ATOM   1746 N  N   . LEU   A 1 226 ? 19.30266  9.83069   -23.41960 1.000 33.54496 ?  303 LEU   A N   1 
ATOM   1747 C  CA  . LEU   A 1 226 ? 17.94989  9.34518   -23.63520 1.000 31.54628 ?  303 LEU   A CA  1 
ATOM   1748 C  C   . LEU   A 1 226 ? 17.07759  9.60662   -22.41846 1.000 33.42181 ?  303 LEU   A C   1 
ATOM   1749 O  O   . LEU   A 1 226 ? 15.85051  9.65378   -22.54768 1.000 31.37372 ?  303 LEU   A O   1 
ATOM   1750 C  CB  . LEU   A 1 226 ? 17.95729  7.85922   -23.99298 1.000 31.75686 ?  303 LEU   A CB  1 
ATOM   1751 C  CG  . LEU   A 1 226 ? 16.62562  7.34579   -24.57196 1.000 31.68620 ?  303 LEU   A CG  1 
ATOM   1752 C  CD1 . LEU   A 1 226 ? 16.38363  7.88168   -25.96119 1.000 30.79300 ?  303 LEU   A CD1 1 
ATOM   1753 C  CD2 . LEU   A 1 226 ? 16.53860  5.82306   -24.57794 1.000 27.99960 ?  303 LEU   A CD2 1 
ATOM   1754 N  N   . ALA   A 1 227 ? 17.69184  9.82629   -21.24994 1.000 28.82252 ?  304 ALA   A N   1 
ATOM   1755 C  CA  . ALA   A 1 227 ? 16.93737  10.15308  -20.04876 1.000 32.15376 ?  304 ALA   A CA  1 
ATOM   1756 C  C   . ALA   A 1 227 ? 16.09267  11.41230  -20.20735 1.000 35.24874 ?  304 ALA   A C   1 
ATOM   1757 O  O   . ALA   A 1 227 ? 15.10616  11.57572  -19.48129 1.000 38.53937 ?  304 ALA   A O   1 
ATOM   1758 C  CB  . ALA   A 1 227 ? 17.88893  10.31273  -18.86377 1.000 31.18182 ?  304 ALA   A CB  1 
ATOM   1759 N  N   . LYS   A 1 228 ? 16.44862  12.30445  -21.13248 1.000 33.81948 ?  305 LYS   A N   1 
ATOM   1760 C  CA  . LYS   A 1 228 ? 15.71023  13.54370  -21.32226 1.000 30.29787 ?  305 LYS   A CA  1 
ATOM   1761 C  C   . LYS   A 1 228 ? 14.48647  13.40633  -22.22207 1.000 32.42630 ?  305 LYS   A C   1 
ATOM   1762 O  O   . LYS   A 1 228 ? 13.74568  14.37906  -22.37826 1.000 31.20406 ?  305 LYS   A O   1 
ATOM   1763 C  CB  . LYS   A 1 228 ? 16.64393  14.60811  -21.88154 1.000 34.57008 ?  305 LYS   A CB  1 
ATOM   1764 C  CG  . LYS   A 1 228 ? 17.60469  15.13530  -20.85855 1.000 33.49639 ?  305 LYS   A CG  1 
ATOM   1765 C  CD  . LYS   A 1 228 ? 16.84458  15.52533  -19.61257 1.000 30.82688 ?  305 LYS   A CD  1 
ATOM   1766 C  CE  . LYS   A 1 228 ? 17.78944  15.89224  -18.48930 1.000 36.47690 ?  305 LYS   A CE  1 
ATOM   1767 N  NZ  . LYS   A 1 228 ? 18.70844  14.75085  -18.18869 1.000 47.12370 ?  305 LYS   A NZ  1 
ATOM   1768 N  N   . CYS   A 1 229 ? 14.25480  12.24502  -22.83575 1.000 35.28906 ?  306 CYS   A N   1 
ATOM   1769 C  CA  . CYS   A 1 229 ? 13.04803  12.04226  -23.63390 1.000 33.00806 ?  306 CYS   A CA  1 
ATOM   1770 C  C   . CYS   A 1 229 ? 11.93435  11.64718  -22.67034 1.000 31.27949 ?  306 CYS   A C   1 
ATOM   1771 O  O   . CYS   A 1 229 ? 11.42049  10.52608  -22.66291 1.000 32.20788 ?  306 CYS   A O   1 
ATOM   1772 C  CB  . CYS   A 1 229 ? 13.27905  10.99813  -24.71632 1.000 29.48394 ?  306 CYS   A CB  1 
ATOM   1773 S  SG  . CYS   A 1 229 ? 14.72864  11.34498  -25.73098 1.000 35.45760 ?  306 CYS   A SG  1 
ATOM   1774 N  N   . SER   A 1 230 ? 11.58521  12.59992  -21.81351 1.000 29.04947 ?  307 SER   A N   1 
ATOM   1775 C  CA  . SER   A 1 230 ? 10.69794  12.27713  -20.70899 1.000 32.09968 ?  307 SER   A CA  1 
ATOM   1776 C  C   . SER   A 1 230 ? 9.28039   11.97383  -21.15596 1.000 31.84870 ?  307 SER   A C   1 
ATOM   1777 O  O   . SER   A 1 230 ? 8.49499   11.49357  -20.33436 1.000 33.11883 ?  307 SER   A O   1 
ATOM   1778 C  CB  . SER   A 1 230 ? 10.70097  13.40956  -19.68332 1.000 35.46087 ?  307 SER   A CB  1 
ATOM   1779 O  OG  . SER   A 1 230 ? 10.74233  14.65456  -20.34050 1.000 36.86062 ?  307 SER   A OG  1 
ATOM   1780 N  N   . ALA   A 1 231 ? 8.93957   12.20968  -22.42379 1.000 29.78722 ?  308 ALA   A N   1 
ATOM   1781 C  CA  . ALA   A 1 231 ? 7.65646   11.77238  -22.95135 1.000 29.77187 ?  308 ALA   A CA  1 
ATOM   1782 C  C   . ALA   A 1 231 ? 7.62107   10.29175  -23.33342 1.000 33.70856 ?  308 ALA   A C   1 
ATOM   1783 O  O   . ALA   A 1 231 ? 6.55130   9.80095   -23.72482 1.000 33.58637 ?  308 ALA   A O   1 
ATOM   1784 C  CB  . ALA   A 1 231 ? 7.28322   12.60420  -24.17504 1.000 30.80037 ?  308 ALA   A CB  1 
ATOM   1785 N  N   . LEU   A 1 232 ? 8.73648   9.56227   -23.24103 1.000 31.07415 ?  309 LEU   A N   1 
ATOM   1786 C  CA  . LEU   A 1 232 ? 8.75012   8.20077   -23.76734 1.000 32.28501 ?  309 LEU   A CA  1 
ATOM   1787 C  C   . LEU   A 1 232 ? 7.69454   7.34855   -23.08401 1.000 29.43290 ?  309 LEU   A C   1 
ATOM   1788 O  O   . LEU   A 1 232 ? 7.60105   7.32117   -21.85528 1.000 30.83683 ?  309 LEU   A O   1 
ATOM   1789 C  CB  . LEU   A 1 232 ? 10.11861  7.56350   -23.59798 1.000 30.37854 ?  309 LEU   A CB  1 
ATOM   1790 C  CG  . LEU   A 1 232 ? 11.06297  7.81219   -24.75721 1.000 29.25144 ?  309 LEU   A CG  1 
ATOM   1791 C  CD1 . LEU   A 1 232 ? 12.41407  7.24727   -24.40858 1.000 29.27684 ?  309 LEU   A CD1 1 
ATOM   1792 C  CD2 . LEU   A 1 232 ? 10.50856  7.18729   -26.03748 1.000 29.13308 ?  309 LEU   A CD2 1 
ATOM   1793 N  N   . GLU   A 1 233 ? 6.86935   6.68159   -23.89260 1.000 30.78667 ?  310 GLU   A N   1 
ATOM   1794 C  CA  . GLU   A 1 233 ? 5.88374   5.74344   -23.37439 1.000 32.79799 ?  310 GLU   A CA  1 
ATOM   1795 C  C   . GLU   A 1 233 ? 6.20839   4.29734   -23.69341 1.000 31.88636 ?  310 GLU   A C   1 
ATOM   1796 O  O   . GLU   A 1 233 ? 5.75150   3.40776   -22.96905 1.000 29.82021 ?  310 GLU   A O   1 
ATOM   1797 C  CB  . GLU   A 1 233 ? 4.48251   6.07011   -23.91431 1.000 31.93658 ?  310 GLU   A CB  1 
ATOM   1798 C  CG  . GLU   A 1 233 ? 3.92763   7.39513   -23.37549 1.000 36.20433 ?  310 GLU   A CG  1 
ATOM   1799 C  CD  . GLU   A 1 233 ? 2.56171   7.74976   -23.92710 1.000 39.56984 ?  310 GLU   A CD  1 
ATOM   1800 O  OE1 . GLU   A 1 233 ? 1.71075   6.84557   -24.03123 1.000 43.17171 ?  310 GLU   A OE1 1 
ATOM   1801 O  OE2 . GLU   A 1 233 ? 2.33599   8.93773   -24.26083 1.000 48.99099 ?  310 GLU   A OE2 1 
ATOM   1802 N  N   . GLU   A 1 234 ? 6.98576   4.05110   -24.74850 1.000 32.51071 ?  311 GLU   A N   1 
ATOM   1803 C  CA  . GLU   A 1 234 ? 7.29853   2.71442   -25.22151 1.000 29.53325 ?  311 GLU   A CA  1 
ATOM   1804 C  C   . GLU   A 1 234 ? 8.66856   2.74919   -25.88180 1.000 30.65460 ?  311 GLU   A C   1 
ATOM   1805 O  O   . GLU   A 1 234 ? 8.91392   3.55928   -26.77876 1.000 33.34980 ?  311 GLU   A O   1 
ATOM   1806 C  CB  . GLU   A 1 234 ? 6.24488   2.21901   -26.20753 1.000 33.13090 ?  311 GLU   A CB  1 
ATOM   1807 C  CG  . GLU   A 1 234 ? 4.81432   2.62531   -25.89219 1.000 37.21169 ?  311 GLU   A CG  1 
ATOM   1808 C  CD  . GLU   A 1 234 ? 3.86271   2.24355   -27.02321 1.000 47.59857 ?  311 GLU   A CD  1 
ATOM   1809 O  OE1 . GLU   A 1 234 ? 4.13053   1.20582   -27.66762 1.000 49.35408 ?  311 GLU   A OE1 1 
ATOM   1810 O  OE2 . GLU   A 1 234 ? 2.87069   2.97799   -27.28102 1.000 53.45821 ?  311 GLU   A OE2 1 
ATOM   1811 N  N   . LEU   A 1 235 ? 9.55661   1.88130   -25.41741 1.000 28.86503 ?  312 LEU   A N   1 
ATOM   1812 C  CA  . LEU   A 1 235 ? 10.93959  1.84002   -25.85855 1.000 28.83421 ?  312 LEU   A CA  1 
ATOM   1813 C  C   . LEU   A 1 235 ? 11.28332  0.37958   -26.09334 1.000 32.75799 ?  312 LEU   A C   1 
ATOM   1814 O  O   . LEU   A 1 235 ? 11.23215  -0.42688  -25.15761 1.000 30.36593 ?  312 LEU   A O   1 
ATOM   1815 C  CB  . LEU   A 1 235 ? 11.85432  2.45994   -24.80341 1.000 31.15225 ?  312 LEU   A CB  1 
ATOM   1816 C  CG  . LEU   A 1 235 ? 13.36332  2.29608   -24.93162 1.000 27.81780 ?  312 LEU   A CG  1 
ATOM   1817 C  CD1 . LEU   A 1 235 ? 13.84827  3.03909   -26.13717 1.000 28.21474 ?  312 LEU   A CD1 1 
ATOM   1818 C  CD2 . LEU   A 1 235 ? 14.03294  2.81629   -23.67797 1.000 27.30843 ?  312 LEU   A CD2 1 
ATOM   1819 N  N   . ASN   A 1 236 ? 11.57668  0.02605   -27.34088 1.000 31.88042 ?  313 ASN   A N   1 
ATOM   1820 C  CA  . ASN   A 1 236 ? 11.85066  -1.35700  -27.70963 1.000 29.54587 ?  313 ASN   A CA  1 
ATOM   1821 C  C   . ASN   A 1 236 ? 13.30248  -1.44750  -28.15625 1.000 27.79755 ?  313 ASN   A C   1 
ATOM   1822 O  O   . ASN   A 1 236 ? 13.67101  -0.90351  -29.19830 1.000 28.83684 ?  313 ASN   A O   1 
ATOM   1823 C  CB  . ASN   A 1 236 ? 10.89691  -1.84687  -28.80001 1.000 28.62083 ?  313 ASN   A CB  1 
ATOM   1824 C  CG  . ASN   A 1 236 ? 10.98659  -3.34331  -29.01494 1.000 27.06910 ?  313 ASN   A CG  1 
ATOM   1825 O  OD1 . ASN   A 1 236 ? 12.05937  -3.92052  -28.90374 1.000 28.40767 ?  313 ASN   A OD1 1 
ATOM   1826 N  ND2 . ASN   A 1 236 ? 9.85969   -3.97983  -29.32314 1.000 29.08245 ?  313 ASN   A ND2 1 
ATOM   1827 N  N   . LEU   A 1 237 ? 14.12292  -2.13748  -27.36764 1.000 26.39950 ?  314 LEU   A N   1 
ATOM   1828 C  CA  . LEU   A 1 237 ? 15.50781  -2.39350  -27.71811 1.000 25.34119 ?  314 LEU   A CA  1 
ATOM   1829 C  C   . LEU   A 1 237 ? 15.77374  -3.88297  -27.96367 1.000 27.78764 ?  314 LEU   A C   1 
ATOM   1830 O  O   . LEU   A 1 237 ? 16.91916  -4.34119  -27.84236 1.000 24.72124 ?  314 LEU   A O   1 
ATOM   1831 C  CB  . LEU   A 1 237 ? 16.42109  -1.85480  -26.62379 1.000 24.77863 ?  314 LEU   A CB  1 
ATOM   1832 C  CG  . LEU   A 1 237 ? 16.29658  -0.41977  -26.11087 1.000 28.44420 ?  314 LEU   A CG  1 
ATOM   1833 C  CD1 . LEU   A 1 237 ? 17.15033  -0.28314  -24.85743 1.000 30.82426 ?  314 LEU   A CD1 1 
ATOM   1834 C  CD2 . LEU   A 1 237 ? 16.73437  0.60219   -27.14766 1.000 27.06060 ?  314 LEU   A CD2 1 
ATOM   1835 N  N   . GLU   A 1 238 ? 14.74491  -4.64834  -28.32090 1.000 25.61991 ?  315 GLU   A N   1 
ATOM   1836 C  CA  . GLU   A 1 238 ? 14.93500  -6.08183  -28.47909 1.000 27.49833 ?  315 GLU   A CA  1 
ATOM   1837 C  C   . GLU   A 1 238 ? 16.04685  -6.36356  -29.49040 1.000 28.94506 ?  315 GLU   A C   1 
ATOM   1838 O  O   . GLU   A 1 238 ? 16.16074  -5.68495  -30.51929 1.000 30.04658 ?  315 GLU   A O   1 
ATOM   1839 C  CB  . GLU   A 1 238 ? 13.62360  -6.74158  -28.90296 1.000 28.56587 ?  315 GLU   A CB  1 
ATOM   1840 C  CG  . GLU   A 1 238 ? 13.72072  -8.25147  -29.04873 1.000 29.15960 ?  315 GLU   A CG  1 
ATOM   1841 C  CD  . GLU   A 1 238 ? 12.55837  -8.84264  -29.84419 1.000 41.85800 ?  315 GLU   A CD  1 
ATOM   1842 O  OE1 . GLU   A 1 238 ? 12.09600  -8.18668  -30.81766 1.000 34.68461 ?  315 GLU   A OE1 1 
ATOM   1843 O  OE2 . GLU   A 1 238 ? 12.10809  -9.97317  -29.49795 1.000 46.47768 ?  315 GLU   A OE2 1 
ATOM   1844 N  N   . ASN   A 1 239 ? 16.90431  -7.33637  -29.15493 1.000 25.82814 ?  316 ASN   A N   1 
ATOM   1845 C  CA  . ASN   A 1 239 ? 17.94919  -7.86764  -30.03324 1.000 24.45094 ?  316 ASN   A CA  1 
ATOM   1846 C  C   . ASN   A 1 239 ? 18.94662  -6.78956  -30.46379 1.000 29.45837 ?  316 ASN   A C   1 
ATOM   1847 O  O   . ASN   A 1 239 ? 19.10176  -6.46301  -31.65200 1.000 27.42782 ?  316 ASN   A O   1 
ATOM   1848 C  CB  . ASN   A 1 239 ? 17.34386  -8.56790  -31.25211 1.000 29.82474 ?  316 ASN   A CB  1 
ATOM   1849 C  CG  . ASN   A 1 239 ? 18.34294  -9.47248  -31.96203 1.000 32.41397 ?  316 ASN   A CG  1 
ATOM   1850 O  OD1 . ASN   A 1 239 ? 19.39572  -9.82198  -31.41472 1.000 29.80426 ?  316 ASN   A OD1 1 
ATOM   1851 N  ND2 . ASN   A 1 239 ? 18.01199  -9.86107  -33.18294 1.000 32.56054 ?  316 ASN   A ND2 1 
ATOM   1852 N  N   . ASN   A 1 240 ? 19.64303  -6.25394  -29.46515 1.000 27.45948 ?  317 ASN   A N   1 
ATOM   1853 C  CA  . ASN   A 1 240 ? 20.86318  -5.49879  -29.69948 1.000 28.84122 ?  317 ASN   A CA  1 
ATOM   1854 C  C   . ASN   A 1 240 ? 21.97049  -6.15832  -28.88904 1.000 28.44014 ?  317 ASN   A C   1 
ATOM   1855 O  O   . ASN   A 1 240 ? 21.84492  -7.33268  -28.52958 1.000 28.32598 ?  317 ASN   A O   1 
ATOM   1856 C  CB  . ASN   A 1 240 ? 20.67640  -4.02047  -29.33481 1.000 27.79503 ?  317 ASN   A CB  1 
ATOM   1857 C  CG  . ASN   A 1 240 ? 19.86854  -3.25542  -30.38139 1.000 29.46491 ?  317 ASN   A CG  1 
ATOM   1858 O  OD1 . ASN   A 1 240 ? 20.42292  -2.75437  -31.35877 1.000 31.14727 ?  317 ASN   A OD1 1 
ATOM   1859 N  ND2 . ASN   A 1 240 ? 18.56033  -3.16605  -30.18044 1.000 26.64246 ?  317 ASN   A ND2 1 
ATOM   1860 N  N   . ASN   A 1 241 ? 23.05283  -5.43694  -28.59448 1.000 28.61877 ?  318 ASN   A N   1 
ATOM   1861 C  CA  . ASN   A 1 241 ? 24.14880  -5.97183  -27.79071 1.000 29.94045 ?  318 ASN   A CA  1 
ATOM   1862 C  C   . ASN   A 1 241 ? 24.37534  -5.12868  -26.54954 1.000 30.07614 ?  318 ASN   A C   1 
ATOM   1863 O  O   . ASN   A 1 241 ? 25.51051  -4.80887  -26.18170 1.000 31.61031 ?  318 ASN   A O   1 
ATOM   1864 C  CB  . ASN   A 1 241 ? 25.42867  -6.07669  -28.60782 1.000 30.37075 ?  318 ASN   A CB  1 
ATOM   1865 C  CG  . ASN   A 1 241 ? 25.19379  -6.73592  -29.92016 1.000 32.12274 ?  318 ASN   A CG  1 
ATOM   1866 O  OD1 . ASN   A 1 241 ? 24.51757  -7.76703  -29.99383 1.000 38.29248 ?  318 ASN   A OD1 1 
ATOM   1867 N  ND2 . ASN   A 1 241 ? 25.69665  -6.13032  -30.98264 1.000 31.73939 ?  318 ASN   A ND2 1 
ATOM   1868 N  N   . ILE   A 1 242 ? 23.29110  -4.77454  -25.88278 1.000 31.03819 ?  319 ILE   A N   1 
ATOM   1869 C  CA  . ILE   A 1 242 ? 23.34070  -3.85125  -24.76008 1.000 30.76944 ?  319 ILE   A CA  1 
ATOM   1870 C  C   . ILE   A 1 242 ? 23.54853  -4.66193  -23.50088 1.000 31.27479 ?  319 ILE   A C   1 
ATOM   1871 O  O   . ILE   A 1 242 ? 22.80651  -5.61814  -23.24532 1.000 32.91156 ?  319 ILE   A O   1 
ATOM   1872 C  CB  . ILE   A 1 242 ? 22.05104  -3.01905  -24.68048 1.000 28.04896 ?  319 ILE   A CB  1 
ATOM   1873 C  CG1 . ILE   A 1 242 ? 21.87103  -2.22984  -25.97618 1.000 28.71836 ?  319 ILE   A CG1 1 
ATOM   1874 C  CG2 . ILE   A 1 242 ? 22.09169  -2.09608  -23.49074 1.000 28.38852 ?  319 ILE   A CG2 1 
ATOM   1875 C  CD1 . ILE   A 1 242 ? 20.47594  -1.74949  -26.20326 1.000 26.75609 ?  319 ILE   A CD1 1 
ATOM   1876 N  N   . SER   A 1 243 ? 24.56220  -4.30234  -22.71283 1.000 27.67686 ?  320 SER   A N   1 
ATOM   1877 C  CA  . SER   A 1 243 ? 24.75280  -4.99863  -21.45692 1.000 28.56807 ?  320 SER   A CA  1 
ATOM   1878 C  C   . SER   A 1 243 ? 24.36834  -4.18252  -20.23053 1.000 31.45943 ?  320 SER   A C   1 
ATOM   1879 O  O   . SER   A 1 243 ? 24.16094  -4.77929  -19.17695 1.000 31.12621 ?  320 SER   A O   1 
ATOM   1880 C  CB  . SER   A 1 243 ? 26.20055  -5.47117  -21.32758 1.000 31.24251 ?  320 SER   A CB  1 
ATOM   1881 O  OG  . SER   A 1 243 ? 27.05650  -4.38460  -21.13943 1.000 31.73599 ?  320 SER   A OG  1 
ATOM   1882 N  N   . THR   A 1 244 ? 24.24431  -2.85395  -20.34402 1.000 29.15408 ?  321 THR   A N   1 
ATOM   1883 C  CA  . THR   A 1 244 ? 23.74441  -1.99623  -19.27118 1.000 29.10357 ?  321 THR   A CA  1 
ATOM   1884 C  C   . THR   A 1 244 ? 23.16694  -0.71018  -19.86109 1.000 32.90462 ?  321 THR   A C   1 
ATOM   1885 O  O   . THR   A 1 244 ? 23.51718  -0.28893  -20.97191 1.000 34.13231 ?  321 THR   A O   1 
ATOM   1886 C  CB  . THR   A 1 244 ? 24.83405  -1.60043  -18.26052 1.000 27.52632 ?  321 THR   A CB  1 
ATOM   1887 O  OG1 . THR   A 1 244 ? 25.84799  -0.84226  -18.93824 1.000 30.93571 ?  321 THR   A OG1 1 
ATOM   1888 C  CG2 . THR   A 1 244 ? 25.45919  -2.80189  -17.59142 1.000 27.47651 ?  321 THR   A CG2 1 
ATOM   1889 N  N   . LEU   A 1 245 ? 22.32477  -0.05199  -19.05971 1.000 30.24133 ?  322 LEU   A N   1 
ATOM   1890 C  CA  . LEU   A 1 245 ? 21.69545  1.24645   -19.21338 1.000 35.37440 ?  322 LEU   A CA  1 
ATOM   1891 C  C   . LEU   A 1 245 ? 22.37328  2.26995   -18.31231 1.000 38.11080 ?  322 LEU   A C   1 
ATOM   1892 O  O   . LEU   A 1 245 ? 22.81830  1.92952   -17.21170 1.000 37.65098 ?  322 LEU   A O   1 
ATOM   1893 C  CB  . LEU   A 1 245 ? 20.20537  1.17611   -18.85453 1.000 37.50535 ?  322 LEU   A CB  1 
ATOM   1894 C  CG  . LEU   A 1 245 ? 19.29756  0.33030   -19.74610 1.000 35.15970 ?  322 LEU   A CG  1 
ATOM   1895 C  CD1 . LEU   A 1 245 ? 17.83966  0.65019   -19.44190 1.000 32.87395 ?  322 LEU   A CD1 1 
ATOM   1896 C  CD2 . LEU   A 1 245 ? 19.62184  0.55491   -21.21815 1.000 31.59411 ?  322 LEU   A CD2 1 
ATOM   1897 N  N   . PRO   A 1 246 ? 22.48692  3.53783   -18.71989 1.000 39.41359 ?  323 PRO   A N   1 
ATOM   1898 C  CA  . PRO   A 1 246 ? 23.00763  4.54257   -17.78236 1.000 42.20270 ?  323 PRO   A CA  1 
ATOM   1899 C  C   . PRO   A 1 246 ? 22.13066  4.55339   -16.54331 1.000 45.03790 ?  323 PRO   A C   1 
ATOM   1900 O  O   . PRO   A 1 246 ? 20.91159  4.40153   -16.62731 1.000 48.45221 ?  323 PRO   A O   1 
ATOM   1901 C  CB  . PRO   A 1 246 ? 22.91832  5.85551   -18.56606 1.000 42.12217 ?  323 PRO   A CB  1 
ATOM   1902 C  CG  . PRO   A 1 246 ? 22.76572  5.43843   -20.01246 1.000 37.45536 ?  323 PRO   A CG  1 
ATOM   1903 C  CD  . PRO   A 1 246 ? 22.03183  4.13984   -19.98352 1.000 34.58903 ?  323 PRO   A CD  1 
ATOM   1904 N  N   . GLU   A 1 247 ? 22.75482  4.67778   -15.38067 1.000 50.17512 ?  324 GLU   A N   1 
ATOM   1905 C  CA  . GLU   A 1 247 ? 22.00529  4.50096   -14.14305 1.000 54.01323 ?  324 GLU   A CA  1 
ATOM   1906 C  C   . GLU   A 1 247 ? 20.88245  5.52698   -14.02977 1.000 51.31213 ?  324 GLU   A C   1 
ATOM   1907 O  O   . GLU   A 1 247 ? 21.05509  6.70609   -14.34909 1.000 45.23322 ?  324 GLU   A O   1 
ATOM   1908 C  CB  . GLU   A 1 247 ? 22.93771  4.60034   -12.94265 1.000 61.47427 ?  324 GLU   A CB  1 
ATOM   1909 C  CG  . GLU   A 1 247 ? 24.38598  4.35045   -13.30351 1.000 70.95956 ?  324 GLU   A CG  1 
ATOM   1910 C  CD  . GLU   A 1 247 ? 25.29010  4.35852   -12.09099 1.000 84.37494 ?  324 GLU   A CD  1 
ATOM   1911 O  OE1 . GLU   A 1 247 ? 25.07450  3.51857   -11.18804 1.000 77.08483 ?  324 GLU   A OE1 1 
ATOM   1912 O  OE2 . GLU   A 1 247 ? 26.20606  5.21396   -12.03942 1.000 93.13337 ?  324 GLU   A OE2 1 
ATOM   1913 N  N   . SER   A 1 248 ? 19.71654  5.05146   -13.58828 1.000 58.88058 ?  325 SER   A N   1 
ATOM   1914 C  CA  . SER   A 1 248 ? 18.51387  5.85663   -13.38137 1.000 55.51993 ?  325 SER   A CA  1 
ATOM   1915 C  C   . SER   A 1 248 ? 18.02200  6.53026   -14.66826 1.000 53.01124 ?  325 SER   A C   1 
ATOM   1916 O  O   . SER   A 1 248 ? 17.26447  7.50291   -14.61781 1.000 54.27918 ?  325 SER   A O   1 
ATOM   1917 C  CB  . SER   A 1 248 ? 18.73148  6.89047   -12.26367 1.000 57.63738 ?  325 SER   A CB  1 
ATOM   1918 O  OG  . SER   A 1 248 ? 18.77160  6.26911   -10.98028 1.000 56.95828 ?  325 SER   A OG  1 
ATOM   1919 N  N   . LEU   A 1 249 ? 18.42876  6.02695   -15.83585 1.000 46.92256 ?  326 LEU   A N   1 
ATOM   1920 C  CA  . LEU   A 1 249 ? 17.78686  6.43674   -17.08078 1.000 38.75322 ?  326 LEU   A CA  1 
ATOM   1921 C  C   . LEU   A 1 249 ? 16.27057  6.25190   -17.01280 1.000 38.11262 ?  326 LEU   A C   1 
ATOM   1922 O  O   . LEU   A 1 249 ? 15.50799  7.13245   -17.41932 1.000 38.38171 ?  326 LEU   A O   1 
ATOM   1923 C  CB  . LEU   A 1 249 ? 18.36062  5.63746   -18.25278 1.000 39.14942 ?  326 LEU   A CB  1 
ATOM   1924 C  CG  . LEU   A 1 249 ? 17.60992  5.87044   -19.56485 1.000 36.76178 ?  326 LEU   A CG  1 
ATOM   1925 C  CD1 . LEU   A 1 249 ? 18.20238  7.06313   -20.24695 1.000 37.11133 ?  326 LEU   A CD1 1 
ATOM   1926 C  CD2 . LEU   A 1 249 ? 17.66367  4.65915   -20.46471 1.000 38.16867 ?  326 LEU   A CD2 1 
ATOM   1927 N  N   . LEU   A 1 250 ? 15.81272  5.09733   -16.51440 1.000 36.45705 ?  327 LEU   A N   1 
ATOM   1928 C  CA  . LEU   A 1 250 ? 14.38350  4.80111   -16.51548 1.000 35.24660 ?  327 LEU   A CA  1 
ATOM   1929 C  C   . LEU   A 1 250 ? 13.64837  5.55362   -15.41923 1.000 37.44819 ?  327 LEU   A C   1 
ATOM   1930 O  O   . LEU   A 1 250 ? 12.44080  5.80652   -15.53998 1.000 36.49911 ?  327 LEU   A O   1 
ATOM   1931 C  CB  . LEU   A 1 250 ? 14.15129  3.29524   -16.35095 1.000 36.81377 ?  327 LEU   A CB  1 
ATOM   1932 C  CG  . LEU   A 1 250 ? 14.73099  2.36256   -17.41583 1.000 28.93471 ?  327 LEU   A CG  1 
ATOM   1933 C  CD1 . LEU   A 1 250 ? 14.50238  0.92370   -17.01979 1.000 35.50723 ?  327 LEU   A CD1 1 
ATOM   1934 C  CD2 . LEU   A 1 250 ? 14.11659  2.64086   -18.76486 1.000 31.91187 ?  327 LEU   A CD2 1 
ATOM   1935 N  N   . SER   A 1 251 ? 14.34653  5.88818   -14.33378 1.000 36.13608 ?  328 SER   A N   1 
ATOM   1936 C  CA  . SER   A 1 251 ? 13.75677  6.77552   -13.34606 1.000 37.33391 ?  328 SER   A CA  1 
ATOM   1937 C  C   . SER   A 1 251 ? 13.33219  8.09384   -13.98180 1.000 37.90649 ?  328 SER   A C   1 
ATOM   1938 O  O   . SER   A 1 251 ? 12.31944  8.67689   -13.58064 1.000 32.79949 ?  328 SER   A O   1 
ATOM   1939 C  CB  . SER   A 1 251 ? 14.74523  7.02129   -12.20701 1.000 41.95735 ?  328 SER   A CB  1 
ATOM   1940 O  OG  . SER   A 1 251 ? 14.75929  5.94768   -11.28432 1.000 44.35783 ?  328 SER   A OG  1 
ATOM   1941 N  N   . SER   A 1 252 ? 14.07579  8.56625   -14.99067 1.000 36.87836 ?  329 SER   A N   1 
ATOM   1942 C  CA  . SER   A 1 252 ? 13.74267  9.82079   -15.65717 1.000 34.68022 ?  329 SER   A CA  1 
ATOM   1943 C  C   . SER   A 1 252 ? 12.57599  9.69025   -16.63632 1.000 37.32736 ?  329 SER   A C   1 
ATOM   1944 O  O   . SER   A 1 252 ? 12.07193  10.71108  -17.11534 1.000 36.51443 ?  329 SER   A O   1 
ATOM   1945 C  CB  . SER   A 1 252 ? 14.97278  10.37070  -16.39245 1.000 36.45815 ?  329 SER   A CB  1 
ATOM   1946 O  OG  . SER   A 1 252 ? 16.04478  10.62835  -15.49775 1.000 34.64975 ?  329 SER   A OG  1 
ATOM   1947 N  N   . LEU   A 1 253 ? 12.11094  8.47597   -16.93056 1.000 36.61281 ?  330 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 253 ? 11.09658  8.27538   -17.96143 1.000 33.13164 ?  330 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 253 ? 9.74936   8.09562   -17.26623 1.000 30.92107 ?  330 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 253 ? 9.24132   6.98945   -17.09668 1.000 35.12308 ?  330 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 253 ? 11.47619  7.09338   -18.85730 1.000 31.68488 ?  330 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 253 ? 12.74184  7.25262   -19.72001 1.000 34.24876 ?  330 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 253 ? 12.93520  6.08200   -20.67629 1.000 33.49973 ?  330 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 253 ? 12.74354  8.55666   -20.50742 1.000 31.94587 ?  330 LEU   A CD2 1 
ATOM   1955 N  N   . VAL   A 1 254 ? 9.14516   9.22973   -16.90160 1.000 33.87348 ?  331 VAL   A N   1 
ATOM   1956 C  CA  . VAL   A 1 254 ? 8.03296   9.26139   -15.95306 1.000 34.19527 ?  331 VAL   A CA  1 
ATOM   1957 C  C   . VAL   A 1 254 ? 6.70944   8.74719   -16.50689 1.000 33.08803 ?  331 VAL   A C   1 
ATOM   1958 O  O   . VAL   A 1 254 ? 5.74994   8.58750   -15.73382 1.000 33.06005 ?  331 VAL   A O   1 
ATOM   1959 C  CB  . VAL   A 1 254 ? 7.82531   10.69916  -15.43407 1.000 33.37291 ?  331 VAL   A CB  1 
ATOM   1960 C  CG1 . VAL   A 1 254 ? 9.01752   11.15022  -14.60361 1.000 32.89532 ?  331 VAL   A CG1 1 
ATOM   1961 C  CG2 . VAL   A 1 254 ? 7.61852   11.63841  -16.59511 1.000 33.20670 ?  331 VAL   A CG2 1 
ATOM   1962 N  N   . LYS   A 1 255 ? 6.60766   8.49133   -17.80979 1.000 28.84819 ?  332 LYS   A N   1 
ATOM   1963 C  CA  . LYS   A 1 255 ? 5.41263   7.85059   -18.35381 1.000 33.48860 ?  332 LYS   A CA  1 
ATOM   1964 C  C   . LYS   A 1 255 ? 5.70800   6.51844   -19.04541 1.000 30.87417 ?  332 LYS   A C   1 
ATOM   1965 O  O   . LYS   A 1 255 ? 4.83432   5.99517   -19.74714 1.000 29.60237 ?  332 LYS   A O   1 
ATOM   1966 C  CB  . LYS   A 1 255 ? 4.68554   8.78542   -19.33412 1.000 33.76006 ?  332 LYS   A CB  1 
ATOM   1967 C  CG  . LYS   A 1 255 ? 5.29964   10.15655  -19.49523 1.000 37.18612 ?  332 LYS   A CG  1 
ATOM   1968 C  CD  . LYS   A 1 255 ? 4.65752   10.94026  -20.64448 1.000 42.43228 ?  332 LYS   A CD  1 
ATOM   1969 C  CE  . LYS   A 1 255 ? 3.14938   11.07399  -20.47366 1.000 46.78409 ?  332 LYS   A CE  1 
ATOM   1970 N  NZ  . LYS   A 1 255 ? 2.53940   11.86399  -21.59087 1.000 48.09453 ?  332 LYS   A NZ  1 
ATOM   1971 N  N   . LEU   A 1 256 ? 6.91057   5.96467   -18.88946 1.000 32.49466 ?  333 LEU   A N   1 
ATOM   1972 C  CA  . LEU   A 1 256 ? 7.27337   4.77149   -19.64560 1.000 30.50263 ?  333 LEU   A CA  1 
ATOM   1973 C  C   . LEU   A 1 256 ? 6.37666   3.63191   -19.21517 1.000 27.58305 ?  333 LEU   A C   1 
ATOM   1974 O  O   . LEU   A 1 256 ? 6.28401   3.32109   -18.03054 1.000 32.17638 ?  333 LEU   A O   1 
ATOM   1975 C  CB  . LEU   A 1 256 ? 8.74464   4.40919   -19.42752 1.000 30.92453 ?  333 LEU   A CB  1 
ATOM   1976 C  CG  . LEU   A 1 256 ? 9.26199   3.29837   -20.36074 1.000 30.81025 ?  333 LEU   A CG  1 
ATOM   1977 C  CD1 . LEU   A 1 256 ? 9.52045   3.84015   -21.77273 1.000 31.34541 ?  333 LEU   A CD1 1 
ATOM   1978 C  CD2 . LEU   A 1 256 ? 10.49803  2.59651   -19.83218 1.000 28.29590 ?  333 LEU   A CD2 1 
ATOM   1979 N  N   . ASN   A 1 257 ? 5.68302   3.02619   -20.14920 1.000 26.08040 ?  334 ASN   A N   1 
ATOM   1980 C  CA  . ASN   A 1 257 ? 4.78733   1.96278   -19.76488 1.000 30.09310 ?  334 ASN   A CA  1 
ATOM   1981 C  C   . ASN   A 1 257 ? 5.04931   0.64156   -20.46638 1.000 29.79306 ?  334 ASN   A C   1 
ATOM   1982 O  O   . ASN   A 1 257 ? 4.53166   -0.38601  -20.01456 1.000 31.05381 ?  334 ASN   A O   1 
ATOM   1983 C  CB  . ASN   A 1 257 ? 3.32775   2.38355   -19.98300 1.000 32.31964 ?  334 ASN   A CB  1 
ATOM   1984 C  CG  . ASN   A 1 257 ? 3.02067   2.70765   -21.41479 1.000 31.80996 ?  334 ASN   A CG  1 
ATOM   1985 O  OD1 . ASN   A 1 257 ? 3.18247   1.86931   -22.28823 1.000 30.79996 ?  334 ASN   A OD1 1 
ATOM   1986 N  ND2 . ASN   A 1 257 ? 2.53039   3.92245   -21.66205 1.000 32.08429 ?  334 ASN   A ND2 1 
ATOM   1987 N  N   . SER   A 1 258 ? 5.84326   0.62307   -21.53003 1.000 29.89645 ?  335 SER   A N   1 
ATOM   1988 C  CA  . SER   A 1 258 ? 6.18139   -0.61655  -22.21439 1.000 26.81718 ?  335 SER   A CA  1 
ATOM   1989 C  C   . SER   A 1 258 ? 7.66008   -0.58845  -22.56960 1.000 30.41118 ?  335 SER   A C   1 
ATOM   1990 O  O   . SER   A 1 258 ? 8.09536   0.26465   -23.35073 1.000 32.18903 ?  335 SER   A O   1 
ATOM   1991 C  CB  . SER   A 1 258 ? 5.32211   -0.79120  -23.45622 1.000 28.64065 ?  335 SER   A CB  1 
ATOM   1992 O  OG  . SER   A 1 258 ? 6.03969   -1.49643  -24.44705 1.000 35.40507 ?  335 SER   A OG  1 
ATOM   1993 N  N   . LEU   A 1 259 ? 8.43086   -1.50283  -21.98316 1.000 28.82669 ?  336 LEU   A N   1 
ATOM   1994 C  CA  . LEU   A 1 259 ? 9.87826   -1.57081  -22.16472 1.000 28.90245 ?  336 LEU   A CA  1 
ATOM   1995 C  C   . LEU   A 1 259 ? 10.25620  -2.98487  -22.57594 1.000 27.12070 ?  336 LEU   A C   1 
ATOM   1996 O  O   . LEU   A 1 259 ? 9.77449   -3.94470  -21.96696 1.000 28.82529 ?  336 LEU   A O   1 
ATOM   1997 C  CB  . LEU   A 1 259 ? 10.61498  -1.19888  -20.87355 1.000 24.79839 ?  336 LEU   A CB  1 
ATOM   1998 C  CG  . LEU   A 1 259 ? 12.12388  -1.41113  -20.92841 1.000 24.45631 ?  336 LEU   A CG  1 
ATOM   1999 C  CD1 . LEU   A 1 259 ? 12.73315  -0.49739  -22.00308 1.000 24.76210 ?  336 LEU   A CD1 1 
ATOM   2000 C  CD2 . LEU   A 1 259 ? 12.74893  -1.13168  -19.58039 1.000 23.30180 ?  336 LEU   A CD2 1 
ATOM   2001 N  N   . THR   A 1 260 ? 11.10352  -3.11832  -23.60447 1.000 27.45448 ?  337 THR   A N   1 
ATOM   2002 C  CA  . THR   A 1 260 ? 11.62888  -4.41246  -24.05215 1.000 26.52541 ?  337 THR   A CA  1 
ATOM   2003 C  C   . THR   A 1 260 ? 13.14900  -4.35856  -24.05962 1.000 27.14037 ?  337 THR   A C   1 
ATOM   2004 O  O   . THR   A 1 260 ? 13.73449  -3.54009  -24.77363 1.000 27.48882 ?  337 THR   A O   1 
ATOM   2005 C  CB  . THR   A 1 260 ? 11.13885  -4.79245  -25.45509 1.000 29.12499 ?  337 THR   A CB  1 
ATOM   2006 O  OG1 . THR   A 1 260 ? 9.70815   -4.86904  -25.47766 1.000 31.95132 ?  337 THR   A OG1 1 
ATOM   2007 C  CG2 . THR   A 1 260 ? 11.73523  -6.15743  -25.87962 1.000 26.20922 ?  337 THR   A CG2 1 
ATOM   2008 N  N   . LEU   A 1 261 ? 13.78168  -5.22690  -23.26828 1.000 24.47110 ?  338 LEU   A N   1 
ATOM   2009 C  CA  . LEU   A 1 261 ? 15.22956  -5.39949  -23.27319 1.000 26.27069 ?  338 LEU   A CA  1 
ATOM   2010 C  C   . LEU   A 1 261 ? 15.63441  -6.79891  -23.72618 1.000 25.76756 ?  338 LEU   A C   1 
ATOM   2011 O  O   . LEU   A 1 261 ? 16.79963  -7.17975  -23.56448 1.000 23.15938 ?  338 LEU   A O   1 
ATOM   2012 C  CB  . LEU   A 1 261 ? 15.81377  -5.11902  -21.88590 1.000 25.43622 ?  338 LEU   A CB  1 
ATOM   2013 C  CG  . LEU   A 1 261 ? 15.47779  -3.75276  -21.29828 1.000 29.51806 ?  338 LEU   A CG  1 
ATOM   2014 C  CD1 . LEU   A 1 261 ? 15.97437  -3.67985  -19.87000 1.000 31.33820 ?  338 LEU   A CD1 1 
ATOM   2015 C  CD2 . LEU   A 1 261 ? 16.09456  -2.64857  -22.12507 1.000 28.96879 ?  338 LEU   A CD2 1 
ATOM   2016 N  N   . ALA   A 1 262 ? 14.69789  -7.56372  -24.28164 1.000 24.35234 ?  339 ALA   A N   1 
ATOM   2017 C  CA  . ALA   A 1 262 ? 14.93715  -8.94592  -24.66762 1.000 27.46291 ?  339 ALA   A CA  1 
ATOM   2018 C  C   . ALA   A 1 262 ? 16.13047  -9.06958  -25.60952 1.000 30.99811 ?  339 ALA   A C   1 
ATOM   2019 O  O   . ALA   A 1 262 ? 16.43299  -8.16287  -26.39938 1.000 28.09661 ?  339 ALA   A O   1 
ATOM   2020 C  CB  . ALA   A 1 262 ? 13.68972  -9.52490  -25.33866 1.000 25.92347 ?  339 ALA   A CB  1 
ATOM   2021 N  N   . ARG   A 1 263 ? 16.81900  -10.21451 -25.50425 1.000 30.09450 ?  340 ARG   A N   1 
ATOM   2022 C  CA  . ARG   A 1 263 ? 17.85359  -10.61092 -26.45748 1.000 27.93734 ?  340 ARG   A CA  1 
ATOM   2023 C  C   . ARG   A 1 263 ? 18.98843  -9.59633  -26.48887 1.000 27.90164 ?  340 ARG   A C   1 
ATOM   2024 O  O   . ARG   A 1 263 ? 19.50593  -9.23327  -27.54535 1.000 27.39291 ?  340 ARG   A O   1 
ATOM   2025 C  CB  . ARG   A 1 263 ? 17.25767  -10.81216 -27.84732 1.000 31.08792 ?  340 ARG   A CB  1 
ATOM   2026 C  CG  . ARG   A 1 263 ? 16.34636  -12.02789 -27.94372 1.000 36.81946 ?  340 ARG   A CG  1 
ATOM   2027 C  CD  . ARG   A 1 263 ? 15.23384  -11.80985 -28.94693 1.000 37.31414 ?  340 ARG   A CD  1 
ATOM   2028 N  NE  . ARG   A 1 263 ? 15.48997  -12.20363 -30.33404 1.000 37.12408 ?  340 ARG   A NE  1 
ATOM   2029 C  CZ  . ARG   A 1 263 ? 16.67103  -12.43124 -30.89455 1.000 41.66257 ?  340 ARG   A CZ  1 
ATOM   2030 N  NH1 . ARG   A 1 263 ? 17.79826  -12.38637 -30.19764 1.000 43.94133 ?  340 ARG   A NH1 1 
ATOM   2031 N  NH2 . ARG   A 1 263 ? 16.72198  -12.73347 -32.19216 1.000 38.72005 ?  340 ARG   A NH2 1 
ATOM   2032 N  N   . ASN   A 1 264 ? 19.38121  -9.13718  -25.31401 1.000 31.26250 ?  341 ASN   A N   1 
ATOM   2033 C  CA  . ASN   A 1 264 ? 20.56928  -8.30703  -25.19268 1.000 30.35029 ?  341 ASN   A CA  1 
ATOM   2034 C  C   . ASN   A 1 264 ? 21.62403  -9.02950  -24.36327 1.000 30.35385 ?  341 ASN   A C   1 
ATOM   2035 O  O   . ASN   A 1 264 ? 21.71453  -10.25881 -24.41787 1.000 30.01191 ?  341 ASN   A O   1 
ATOM   2036 C  CB  . ASN   A 1 264 ? 20.19804  -6.93925  -24.60937 1.000 26.27771 ?  341 ASN   A CB  1 
ATOM   2037 C  CG  . ASN   A 1 264 ? 19.80384  -5.95059  -25.69993 1.000 28.84187 ?  341 ASN   A CG  1 
ATOM   2038 O  OD1 . ASN   A 1 264 ? 20.66614  -5.28679  -26.29357 1.000 27.59265 ?  341 ASN   A OD1 1 
ATOM   2039 N  ND2 . ASN   A 1 264 ? 18.51145  -5.88583  -26.00445 1.000 24.06363 ?  341 ASN   A ND2 1 
ATOM   2040 N  N   . CYS   A 1 265 ? 22.41389  -8.28687  -23.58800 1.000 29.45704 ?  342 CYS   A N   1 
ATOM   2041 C  CA  . CYS   A 1 265 ? 23.56118  -8.84284  -22.88846 1.000 28.49025 ?  342 CYS   A CA  1 
ATOM   2042 C  C   . CYS   A 1 265 ? 23.50804  -8.55454  -21.39710 1.000 27.35321 ?  342 CYS   A C   1 
ATOM   2043 O  O   . CYS   A 1 265 ? 24.55078  -8.45030  -20.75993 1.000 27.09338 ?  342 CYS   A O   1 
ATOM   2044 C  CB  . CYS   A 1 265 ? 24.86296  -8.29898  -23.47303 1.000 30.39784 ?  342 CYS   A CB  1 
ATOM   2045 S  SG  . CYS   A 1 265 ? 25.20874  -8.82712  -25.15613 1.000 34.32806 ?  342 CYS   A SG  1 
ATOM   2046 N  N   . PHE   A 1 266 ? 22.31167  -8.41507  -20.82676 1.000 26.62925 ?  343 PHE   A N   1 
ATOM   2047 C  CA  . PHE   A 1 266 ? 22.18022  -7.97021  -19.44386 1.000 26.60188 ?  343 PHE   A CA  1 
ATOM   2048 C  C   . PHE   A 1 266 ? 22.45490  -9.10627  -18.46482 1.000 27.74059 ?  343 PHE   A C   1 
ATOM   2049 O  O   . PHE   A 1 266 ? 21.86579  -10.18620 -18.56827 1.000 24.29300 ?  343 PHE   A O   1 
ATOM   2050 C  CB  . PHE   A 1 266 ? 20.77856  -7.42372  -19.18044 1.000 29.15458 ?  343 PHE   A CB  1 
ATOM   2051 C  CG  . PHE   A 1 266 ? 20.51590  -6.05761  -19.75289 1.000 30.67957 ?  343 PHE   A CG  1 
ATOM   2052 C  CD1 . PHE   A 1 266 ? 20.74609  -4.92276  -18.99279 1.000 29.39616 ?  343 PHE   A CD1 1 
ATOM   2053 C  CD2 . PHE   A 1 266 ? 19.98210  -5.91190  -21.03771 1.000 27.53675 ?  343 PHE   A CD2 1 
ATOM   2054 C  CE1 . PHE   A 1 266 ? 20.46791  -3.66615  -19.51250 1.000 31.62868 ?  343 PHE   A CE1 1 
ATOM   2055 C  CE2 . PHE   A 1 266 ? 19.71231  -4.66160  -21.56329 1.000 29.29556 ?  343 PHE   A CE2 1 
ATOM   2056 C  CZ  . PHE   A 1 266 ? 19.96594  -3.53314  -20.79881 1.000 29.99924 ?  343 PHE   A CZ  1 
ATOM   2057 N  N   . GLN   A 1 267 ? 23.30932  -8.84047  -17.48029 1.000 26.78526 ?  344 GLN   A N   1 
ATOM   2058 C  CA  . GLN   A 1 267 ? 23.51401  -9.77373  -16.38577 1.000 26.96250 ?  344 GLN   A CA  1 
ATOM   2059 C  C   . GLN   A 1 267 ? 22.73892  -9.40119  -15.13145 1.000 29.09792 ?  344 GLN   A C   1 
ATOM   2060 O  O   . GLN   A 1 267 ? 22.60283  -10.23549 -14.23040 1.000 28.01109 ?  344 GLN   A O   1 
ATOM   2061 C  CB  . GLN   A 1 267 ? 25.00234  -9.86934  -16.04611 1.000 28.67290 ?  344 GLN   A CB  1 
ATOM   2062 C  CG  . GLN   A 1 267 ? 25.87030  -10.22284 -17.23660 1.000 33.58114 ?  344 GLN   A CG  1 
ATOM   2063 C  CD  . GLN   A 1 267 ? 27.23603  -10.75123 -16.84381 1.000 41.40707 ?  344 GLN   A CD  1 
ATOM   2064 O  OE1 . GLN   A 1 267 ? 27.53613  -10.92863 -15.66349 1.000 47.56241 ?  344 GLN   A OE1 1 
ATOM   2065 N  NE2 . GLN   A 1 267 ? 28.06920  -11.02551 -17.84040 1.000 50.26958 ?  344 GLN   A NE2 1 
ATOM   2066 N  N   . LEU   A 1 268 ? 22.23120  -8.17614  -15.05166 1.000 29.45560 ?  345 LEU   A N   1 
ATOM   2067 C  CA  . LEU   A 1 268 ? 21.50223  -7.70202  -13.89183 1.000 26.40285 ?  345 LEU   A CA  1 
ATOM   2068 C  C   . LEU   A 1 268 ? 20.34257  -6.86546  -14.39743 1.000 29.30061 ?  345 LEU   A C   1 
ATOM   2069 O  O   . LEU   A 1 268 ? 20.25747  -6.55518  -15.58603 1.000 30.90734 ?  345 LEU   A O   1 
ATOM   2070 C  CB  . LEU   A 1 268 ? 22.40384  -6.87448  -12.96695 1.000 28.30007 ?  345 LEU   A CB  1 
ATOM   2071 C  CG  . LEU   A 1 268 ? 23.49235  -7.56871  -12.13662 1.000 32.99020 ?  345 LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   A 1 268 ? 24.37731  -6.54923  -11.42732 1.000 30.03564 ?  345 LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   A 1 268 ? 22.89979  -8.53474  -11.10632 1.000 35.21011 ?  345 LEU   A CD2 1 
ATOM   2074 N  N   . TYR   A 1 269 ? 19.44454  -6.49174  -13.48928 1.000 29.31794 ?  346 TYR   A N   1 
ATOM   2075 C  CA  . TYR   A 1 269 ? 18.45318  -5.48714  -13.81903 1.000 30.19246 ?  346 TYR   A CA  1 
ATOM   2076 C  C   . TYR   A 1 269 ? 19.14317  -4.12971  -13.97382 1.000 34.62005 ?  346 TYR   A C   1 
ATOM   2077 O  O   . TYR   A 1 269 ? 20.20798  -3.88947  -13.39330 1.000 32.67239 ?  346 TYR   A O   1 
ATOM   2078 C  CB  . TYR   A 1 269 ? 17.37976  -5.40234  -12.73183 1.000 28.63570 ?  346 TYR   A CB  1 
ATOM   2079 C  CG  . TYR   A 1 269 ? 16.10592  -6.13511  -13.04666 1.000 30.26074 ?  346 TYR   A CG  1 
ATOM   2080 C  CD1 . TYR   A 1 269 ? 16.10047  -7.52198  -13.23207 1.000 29.73080 ?  346 TYR   A CD1 1 
ATOM   2081 C  CD2 . TYR   A 1 269 ? 14.89531  -5.45576  -13.13330 1.000 31.92243 ?  346 TYR   A CD2 1 
ATOM   2082 C  CE1 . TYR   A 1 269 ? 14.92360  -8.21243  -13.52070 1.000 29.37774 ?  346 TYR   A CE1 1 
ATOM   2083 C  CE2 . TYR   A 1 269 ? 13.70869  -6.13526  -13.42630 1.000 33.64920 ?  346 TYR   A CE2 1 
ATOM   2084 C  CZ  . TYR   A 1 269 ? 13.72894  -7.51725  -13.62396 1.000 33.58672 ?  346 TYR   A CZ  1 
ATOM   2085 O  OH  . TYR   A 1 269 ? 12.55462  -8.20421  -13.91070 1.000 31.67286 ?  346 TYR   A OH  1 
ATOM   2086 N  N   . PRO   A 1 270 ? 18.57332  -3.23036  -14.76782 1.000 36.56167 ?  347 PRO   A N   1 
ATOM   2087 C  CA  . PRO   A 1 270 ? 19.06368  -1.84686  -14.76259 1.000 35.32234 ?  347 PRO   A CA  1 
ATOM   2088 C  C   . PRO   A 1 270 ? 18.99327  -1.26035  -13.35652 1.000 37.25409 ?  347 PRO   A C   1 
ATOM   2089 O  O   . PRO   A 1 270 ? 17.97875  -1.37303  -12.66830 1.000 37.13779 ?  347 PRO   A O   1 
ATOM   2090 C  CB  . PRO   A 1 270 ? 18.12175  -1.13391  -15.74268 1.000 34.64794 ?  347 PRO   A CB  1 
ATOM   2091 C  CG  . PRO   A 1 270 ? 16.98136  -2.09356  -15.97973 1.000 35.38679 ?  347 PRO   A CG  1 
ATOM   2092 C  CD  . PRO   A 1 270 ? 17.54266  -3.45431  -15.79244 1.000 32.38580 ?  347 PRO   A CD  1 
ATOM   2093 N  N   . VAL   A 1 271 ? 20.08357  -0.63081  -12.93001 1.000 40.21509 ?  348 VAL   A N   1 
ATOM   2094 C  CA  . VAL   A 1 271 ? 20.20312  -0.15137  -11.55571 1.000 42.61801 ?  348 VAL   A CA  1 
ATOM   2095 C  C   . VAL   A 1 271 ? 19.50294  1.19371   -11.39965 1.000 47.29802 ?  348 VAL   A C   1 
ATOM   2096 O  O   . VAL   A 1 271 ? 19.59737  2.07073   -12.26741 1.000 46.35378 ?  348 VAL   A O   1 
ATOM   2097 C  CB  . VAL   A 1 271 ? 21.68595  -0.06208  -11.15031 1.000 44.42179 ?  348 VAL   A CB  1 
ATOM   2098 C  CG1 . VAL   A 1 271 ? 22.37827  -1.38671  -11.42101 1.000 42.91546 ?  348 VAL   A CG1 1 
ATOM   2099 C  CG2 . VAL   A 1 271 ? 22.37544  1.03840   -11.89921 1.000 47.69710 ?  348 VAL   A CG2 1 
ATOM   2100 N  N   . GLY   A 1 272 ? 18.79240  1.36747   -10.28791 1.000 55.17306 ?  349 GLY   A N   1 
ATOM   2101 C  CA  . GLY   A 1 272 ? 18.20315  2.66305   -10.03516 1.000 58.57183 ?  349 GLY   A CA  1 
ATOM   2102 C  C   . GLY   A 1 272 ? 16.93337  2.71644   -9.21025  1.000 62.09495 ?  349 GLY   A C   1 
ATOM   2103 O  O   . GLY   A 1 272 ? 16.27514  3.76410   -9.18483  1.000 67.03127 ?  349 GLY   A O   1 
ATOM   2104 N  N   . GLY   A 1 273 ? 16.56624  1.62642   -8.53739  1.000 46.92078 ?  350 GLY   A N   1 
ATOM   2105 C  CA  . GLY   A 1 273 ? 15.45504  1.66284   -7.61162  1.000 45.49481 ?  350 GLY   A CA  1 
ATOM   2106 C  C   . GLY   A 1 273 ? 14.08668  1.64559   -8.26926  1.000 43.76118 ?  350 GLY   A C   1 
ATOM   2107 O  O   . GLY   A 1 273 ? 13.95715  1.73212   -9.49381  1.000 40.28181 ?  350 GLY   A O   1 
ATOM   2108 N  N   . PRO   A 1 274 ? 13.03017  1.55270   -7.45013  1.000 40.18476 ?  351 PRO   A N   1 
ATOM   2109 C  CA  . PRO   A 1 274 ? 11.67747  1.30535   -7.99913  1.000 40.66288 ?  351 PRO   A CA  1 
ATOM   2110 C  C   . PRO   A 1 274 ? 11.10478  2.45366   -8.83827  1.000 41.25009 ?  351 PRO   A C   1 
ATOM   2111 O  O   . PRO   A 1 274 ? 10.13378  2.23390   -9.58155  1.000 38.70487 ?  351 PRO   A O   1 
ATOM   2112 C  CB  . PRO   A 1 274 ? 10.83044  1.06432   -6.73705  1.000 38.16519 ?  351 PRO   A CB  1 
ATOM   2113 C  CG  . PRO   A 1 274 ? 11.54982  1.82100   -5.66183  1.000 39.64440 ?  351 PRO   A CG  1 
ATOM   2114 C  CD  . PRO   A 1 274 ? 13.02130  1.64742   -5.98268  1.000 36.97598 ?  351 PRO   A CD  1 
ATOM   2115 N  N   . SER   A 1 275 ? 11.65116  3.66689   -8.73426  1.000 38.02438 ?  352 SER   A N   1 
ATOM   2116 C  CA  . SER   A 1 275 ? 11.21186  4.74868   -9.60612  1.000 37.84876 ?  352 SER   A CA  1 
ATOM   2117 C  C   . SER   A 1 275 ? 11.25947  4.36323   -11.07335 1.000 38.02722 ?  352 SER   A C   1 
ATOM   2118 O  O   . SER   A 1 275 ? 10.58068  4.99087   -11.88657 1.000 39.18960 ?  352 SER   A O   1 
ATOM   2119 C  CB  . SER   A 1 275 ? 12.08351  5.99033   -9.38635  1.000 38.21411 ?  352 SER   A CB  1 
ATOM   2120 O  OG  . SER   A 1 275 ? 13.32005  5.62152   -8.77998  1.000 49.04468 ?  352 SER   A OG  1 
ATOM   2121 N  N   . GLN   A 1 276 ? 12.05692  3.35953   -11.43688 1.000 37.07030 ?  353 GLN   A N   1 
ATOM   2122 C  CA  . GLN   A 1 276 ? 12.23422  3.02692   -12.84105 1.000 35.78182 ?  353 GLN   A CA  1 
ATOM   2123 C  C   . GLN   A 1 276 ? 10.99422  2.41345   -13.45638 1.000 32.09828 ?  353 GLN   A C   1 
ATOM   2124 O  O   . GLN   A 1 276 ? 10.81052  2.50081   -14.67366 1.000 32.47616 ?  353 GLN   A O   1 
ATOM   2125 C  CB  . GLN   A 1 276 ? 13.38428  2.04847   -13.00896 1.000 36.41109 ?  353 GLN   A CB  1 
ATOM   2126 C  CG  . GLN   A 1 276 ? 14.62625  2.38620   -12.24490 1.000 40.84897 ?  353 GLN   A CG  1 
ATOM   2127 C  CD  . GLN   A 1 276 ? 15.71140  1.38517   -12.54738 1.000 43.27055 ?  353 GLN   A CD  1 
ATOM   2128 O  OE1 . GLN   A 1 276 ? 16.21237  1.32584   -13.66986 1.000 41.72794 ?  353 GLN   A OE1 1 
ATOM   2129 N  NE2 . GLN   A 1 276 ? 16.05808  0.56966   -11.56316 1.000 42.37169 ?  353 GLN   A NE2 1 
ATOM   2130 N  N   . PHE   A 1 277 ? 10.15882  1.76832   -12.65308 1.000 32.22997 ?  354 PHE   A N   1 
ATOM   2131 C  CA  . PHE   A 1 277 ? 9.10465   0.91924   -13.18596 1.000 35.02238 ?  354 PHE   A CA  1 
ATOM   2132 C  C   . PHE   A 1 277 ? 7.74158   1.32071   -12.66030 1.000 33.34857 ?  354 PHE   A C   1 
ATOM   2133 O  O   . PHE   A 1 277 ? 6.79342   0.54348   -12.76869 1.000 35.03262 ?  354 PHE   A O   1 
ATOM   2134 C  CB  . PHE   A 1 277 ? 9.40001   -0.54974  -12.87423 1.000 30.74305 ?  354 PHE   A CB  1 
ATOM   2135 C  CG  . PHE   A 1 277 ? 10.64444  -1.05382  -13.53529 1.000 31.47235 ?  354 PHE   A CG  1 
ATOM   2136 C  CD1 . PHE   A 1 277 ? 10.68710  -1.21955  -14.91615 1.000 33.41277 ?  354 PHE   A CD1 1 
ATOM   2137 C  CD2 . PHE   A 1 277 ? 11.77876  -1.33768  -12.79439 1.000 32.28525 ?  354 PHE   A CD2 1 
ATOM   2138 C  CE1 . PHE   A 1 277 ? 11.82878  -1.67287  -15.55193 1.000 29.77621 ?  354 PHE   A CE1 1 
ATOM   2139 C  CE2 . PHE   A 1 277 ? 12.93501  -1.79250  -13.42207 1.000 32.64631 ?  354 PHE   A CE2 1 
ATOM   2140 C  CZ  . PHE   A 1 277 ? 12.95590  -1.96178  -14.80259 1.000 33.44932 ?  354 PHE   A CZ  1 
ATOM   2141 N  N   . SER   A 1 278 ? 7.62159   2.54019   -12.13332 1.000 32.73224 ?  355 SER   A N   1 
ATOM   2142 C  CA  . SER   A 1 278 ? 6.39302   2.93839   -11.45540 1.000 33.84513 ?  355 SER   A CA  1 
ATOM   2143 C  C   . SER   A 1 278 ? 5.19802   2.96144   -12.40423 1.000 32.61144 ?  355 SER   A C   1 
ATOM   2144 O  O   . SER   A 1 278 ? 4.10605   2.51989   -12.03468 1.000 35.58423 ?  355 SER   A O   1 
ATOM   2145 C  CB  . SER   A 1 278 ? 6.58990   4.29721   -10.78723 1.000 32.91037 ?  355 SER   A CB  1 
ATOM   2146 O  OG  . SER   A 1 278 ? 7.08130   5.21089   -11.73859 1.000 44.05195 ?  355 SER   A OG  1 
ATOM   2147 N  N   . THR   A 1 279 ? 5.36839   3.46041   -13.62715 1.000 32.05966 ?  356 THR   A N   1 
ATOM   2148 C  CA  . THR   A 1 279 ? 4.26308   3.46437   -14.57775 1.000 32.69489 ?  356 THR   A CA  1 
ATOM   2149 C  C   . THR   A 1 279 ? 4.32133   2.29429   -15.53442 1.000 32.88544 ?  356 THR   A C   1 
ATOM   2150 O  O   . THR   A 1 279 ? 3.50635   2.21344   -16.45922 1.000 31.34548 ?  356 THR   A O   1 
ATOM   2151 C  CB  . THR   A 1 279 ? 4.22152   4.76907   -15.36824 1.000 32.90242 ?  356 THR   A CB  1 
ATOM   2152 O  OG1 . THR   A 1 279 ? 5.50589   5.02110   -15.95301 1.000 33.27684 ?  356 THR   A OG1 1 
ATOM   2153 C  CG2 . THR   A 1 279 ? 3.82866   5.91494   -14.45003 1.000 26.11084 ?  356 THR   A CG2 1 
ATOM   2154 N  N   . ILE   A 1 280 ? 5.25669   1.37749   -15.31967 1.000 30.73684 ?  357 ILE   A N   1 
ATOM   2155 C  CA  . ILE   A 1 280 ? 5.49329   0.32200   -16.28367 1.000 30.81579 ?  357 ILE   A CA  1 
ATOM   2156 C  C   . ILE   A 1 280 ? 4.31225   -0.63710  -16.28169 1.000 31.16114 ?  357 ILE   A C   1 
ATOM   2157 O  O   . ILE   A 1 280 ? 3.78131   -1.00819  -15.22101 1.000 30.57171 ?  357 ILE   A O   1 
ATOM   2158 C  CB  . ILE   A 1 280 ? 6.81525   -0.39330  -15.96353 1.000 30.69416 ?  357 ILE   A CB  1 
ATOM   2159 C  CG1 . ILE   A 1 280 ? 7.75664   -0.32172  -17.16560 1.000 29.78262 ?  357 ILE   A CG1 1 
ATOM   2160 C  CG2 . ILE   A 1 280 ? 6.55172   -1.82633  -15.56346 1.000 31.46317 ?  357 ILE   A CG2 1 
ATOM   2161 C  CD1 . ILE   A 1 280 ? 7.40213   -1.30676  -18.24473 1.000 31.58939 ?  357 ILE   A CD1 1 
ATOM   2162 N  N   . TYR   A 1 281 ? 3.87062   -1.00781  -17.47626 1.000 25.65234 ?  358 TYR   A N   1 
ATOM   2163 C  CA  . TYR   A 1 281 ? 2.77807   -1.95056  -17.66635 1.000 30.29985 ?  358 TYR   A CA  1 
ATOM   2164 C  C   . TYR   A 1 281 ? 3.23660   -3.26325  -18.28168 1.000 30.25587 ?  358 TYR   A C   1 
ATOM   2165 O  O   . TYR   A 1 281 ? 2.77442   -4.33375  -17.88094 1.000 30.61779 ?  358 TYR   A O   1 
ATOM   2166 C  CB  . TYR   A 1 281 ? 1.70238   -1.31638  -18.54739 1.000 28.89608 ?  358 TYR   A CB  1 
ATOM   2167 C  CG  . TYR   A 1 281 ? 0.63690   -2.26671  -19.03229 1.000 32.69493 ?  358 TYR   A CG  1 
ATOM   2168 C  CD1 . TYR   A 1 281 ? 0.79520   -2.97012  -20.23125 1.000 32.08514 ?  358 TYR   A CD1 1 
ATOM   2169 C  CD2 . TYR   A 1 281 ? -0.54349  -2.44910  -18.31071 1.000 30.09699 ?  358 TYR   A CD2 1 
ATOM   2170 C  CE1 . TYR   A 1 281 ? -0.18915  -3.84266  -20.69165 1.000 34.51475 ?  358 TYR   A CE1 1 
ATOM   2171 C  CE2 . TYR   A 1 281 ? -1.53805  -3.31761  -18.76374 1.000 32.96530 ?  358 TYR   A CE2 1 
ATOM   2172 C  CZ  . TYR   A 1 281 ? -1.34995  -4.01453  -19.95280 1.000 38.09907 ?  358 TYR   A CZ  1 
ATOM   2173 O  OH  . TYR   A 1 281 ? -2.32706  -4.87840  -20.40728 1.000 44.84281 ?  358 TYR   A OH  1 
ATOM   2174 N  N   . SER   A 1 282 ? 4.15966   -3.19857  -19.22861 1.000 29.29816 ?  359 SER   A N   1 
ATOM   2175 C  CA  . SER   A 1 282 ? 4.67658   -4.36227  -19.92240 1.000 30.24692 ?  359 SER   A CA  1 
ATOM   2176 C  C   . SER   A 1 282 ? 6.19047   -4.30094  -19.88453 1.000 28.80177 ?  359 SER   A C   1 
ATOM   2177 O  O   . SER   A 1 282 ? 6.78162   -3.28692  -20.26467 1.000 32.43907 ?  359 SER   A O   1 
ATOM   2178 C  CB  . SER   A 1 282 ? 4.17533   -4.40744  -21.36248 1.000 28.73304 ?  359 SER   A CB  1 
ATOM   2179 O  OG  . SER   A 1 282 ? 4.93655   -5.33693  -22.09170 1.000 39.19625 ?  359 SER   A OG  1 
ATOM   2180 N  N   . LEU   A 1 283 ? 6.81070   -5.37258  -19.40063 1.000 31.80962 ?  360 LEU   A N   1 
ATOM   2181 C  CA  . LEU   A 1 283 ? 8.25724   -5.45098  -19.22498 1.000 29.65211 ?  360 LEU   A CA  1 
ATOM   2182 C  C   . LEU   A 1 283 ? 8.74980   -6.77964  -19.79747 1.000 32.01285 ?  360 LEU   A C   1 
ATOM   2183 O  O   . LEU   A 1 283 ? 8.36301   -7.85187  -19.30972 1.000 28.73822 ?  360 LEU   A O   1 
ATOM   2184 C  CB  . LEU   A 1 283 ? 8.62718   -5.31862  -17.74430 1.000 28.11453 ?  360 LEU   A CB  1 
ATOM   2185 C  CG  . LEU   A 1 283 ? 10.10830  -5.34858  -17.38186 1.000 27.90909 ?  360 LEU   A CG  1 
ATOM   2186 C  CD1 . LEU   A 1 283 ? 10.87435  -4.36350  -18.26623 1.000 25.27102 ?  360 LEU   A CD1 1 
ATOM   2187 C  CD2 . LEU   A 1 283 ? 10.29619  -5.03789  -15.89866 1.000 30.09861 ?  360 LEU   A CD2 1 
ATOM   2188 N  N   . ASN   A 1 284 ? 9.60724   -6.70305  -20.82108 1.000 26.44640 ?  361 ASN   A N   1 
ATOM   2189 C  CA  . ASN   A 1 284 ? 10.09180  -7.86025  -21.56587 1.000 26.21825 ?  361 ASN   A CA  1 
ATOM   2190 C  C   . ASN   A 1 284 ? 11.60282  -7.91623  -21.43765 1.000 27.58871 ?  361 ASN   A C   1 
ATOM   2191 O  O   . ASN   A 1 284 ? 12.30754  -7.10110  -22.03552 1.000 27.34951 ?  361 ASN   A O   1 
ATOM   2192 C  CB  . ASN   A 1 284 ? 9.70838   -7.77897  -23.03968 1.000 25.90613 ?  361 ASN   A CB  1 
ATOM   2193 C  CG  . ASN   A 1 284 ? 8.39191   -8.42530  -23.33150 1.000 32.17814 ?  361 ASN   A CG  1 
ATOM   2194 O  OD1 . ASN   A 1 284 ? 7.34072   -7.86189  -23.03427 1.000 31.94976 ?  361 ASN   A OD1 1 
ATOM   2195 N  ND2 . ASN   A 1 284 ? 8.43081   -9.62147  -23.93273 1.000 32.84792 ?  361 ASN   A ND2 1 
ATOM   2196 N  N   . MET   A 1 285 ? 12.10938  -8.89507  -20.69235 1.000 30.80400 ?  362 MET   A N   1 
ATOM   2197 C  CA  . MET   A 1 285 ? 13.54896  -9.00189  -20.50242 1.000 27.90149 ?  362 MET   A CA  1 
ATOM   2198 C  C   . MET   A 1 285 ? 14.07668  -10.38288 -20.87057 1.000 26.62932 ?  362 MET   A C   1 
ATOM   2199 O  O   . MET   A 1 285 ? 15.15969  -10.76240 -20.41301 1.000 28.11487 ?  362 MET   A O   1 
ATOM   2200 C  CB  . MET   A 1 285 ? 13.91419  -8.64654  -19.06373 1.000 28.94277 ?  362 MET   A CB  1 
ATOM   2201 C  CG  . MET   A 1 285 ? 13.48664  -7.24287  -18.67502 1.000 28.78958 ?  362 MET   A CG  1 
ATOM   2202 S  SD  . MET   A 1 285 ? 14.07696  -6.98966  -17.02061 1.000 44.18875 ?  362 MET   A SD  1 
ATOM   2203 C  CE  . MET   A 1 285 ? 15.59755  -6.13455  -17.40567 1.000 35.17112 ?  362 MET   A CE  1 
ATOM   2204 N  N   . GLU   A 1 286 ? 13.35462  -11.11649 -21.71658 1.000 24.40216 ?  363 GLU   A N   1 
ATOM   2205 C  CA  . GLU   A 1 286 ? 13.70218  -12.49276 -22.02508 1.000 27.92255 ?  363 GLU   A CA  1 
ATOM   2206 C  C   . GLU   A 1 286 ? 14.99441  -12.56574 -22.84322 1.000 30.02866 ?  363 GLU   A C   1 
ATOM   2207 O  O   . GLU   A 1 286 ? 15.39501  -11.61534 -23.51917 1.000 28.16202 ?  363 GLU   A O   1 
ATOM   2208 C  CB  . GLU   A 1 286 ? 12.54041  -13.19278 -22.74894 1.000 25.61580 ?  363 GLU   A CB  1 
ATOM   2209 C  CG  . GLU   A 1 286 ? 12.13563  -12.62187 -24.10954 1.000 28.42135 ?  363 GLU   A CG  1 
ATOM   2210 C  CD  . GLU   A 1 286 ? 11.08385  -11.50061 -24.03319 1.000 32.94792 ?  363 GLU   A CD  1 
ATOM   2211 O  OE1 . GLU   A 1 286 ? 10.83641  -10.95339 -22.92012 1.000 30.05730 ?  363 GLU   A OE1 1 
ATOM   2212 O  OE2 . GLU   A 1 286 ? 10.51789  -11.15439 -25.10470 1.000 31.33446 ?  363 GLU   A OE2 1 
ATOM   2213 N  N   . HIS   A 1 287 ? 15.66026  -13.71919 -22.74257 1.000 28.99464 ?  364 HIS   A N   1 
ATOM   2214 C  CA  . HIS   A 1 287 ? 16.89612  -14.01935 -23.46711 1.000 29.95581 ?  364 HIS   A CA  1 
ATOM   2215 C  C   . HIS   A 1 287 ? 18.01855  -13.04828 -23.08944 1.000 30.43866 ?  364 HIS   A C   1 
ATOM   2216 O  O   . HIS   A 1 287 ? 18.61803  -12.37369 -23.93137 1.000 30.68766 ?  364 HIS   A O   1 
ATOM   2217 C  CB  . HIS   A 1 287 ? 16.65350  -14.04273 -24.98174 1.000 30.83666 ?  364 HIS   A CB  1 
ATOM   2218 C  CG  . HIS   A 1 287 ? 15.50399  -14.90870 -25.38270 1.000 31.74059 ?  364 HIS   A CG  1 
ATOM   2219 N  ND1 . HIS   A 1 287 ? 15.50895  -16.27568 -25.20876 1.000 29.97509 ?  364 HIS   A ND1 1 
ATOM   2220 C  CD2 . HIS   A 1 287 ? 14.29924  -14.60148 -25.91709 1.000 30.92255 ?  364 HIS   A CD2 1 
ATOM   2221 C  CE1 . HIS   A 1 287 ? 14.35958  -16.77380 -25.62510 1.000 28.34980 ?  364 HIS   A CE1 1 
ATOM   2222 N  NE2 . HIS   A 1 287 ? 13.60812  -15.77950 -26.05942 1.000 29.36588 ?  364 HIS   A NE2 1 
ATOM   2223 N  N   . ASN   A 1 288 ? 18.31469  -13.01209 -21.79563 1.000 28.51658 ?  365 ASN   A N   1 
ATOM   2224 C  CA  . ASN   A 1 288 ? 19.50484  -12.33952 -21.29413 1.000 28.20221 ?  365 ASN   A CA  1 
ATOM   2225 C  C   . ASN   A 1 288 ? 20.16032  -13.31628 -20.32234 1.000 28.63895 ?  365 ASN   A C   1 
ATOM   2226 O  O   . ASN   A 1 288 ? 19.89960  -14.52254 -20.34393 1.000 29.58586 ?  365 ASN   A O   1 
ATOM   2227 C  CB  . ASN   A 1 288 ? 19.16438  -10.99392 -20.64086 1.000 29.11843 ?  365 ASN   A CB  1 
ATOM   2228 C  CG  . ASN   A 1 288 ? 18.90475  -9.88835  -21.64888 1.000 29.24029 ?  365 ASN   A CG  1 
ATOM   2229 O  OD1 . ASN   A 1 288 ? 19.83553  -9.34121  -22.23774 1.000 29.48243 ?  365 ASN   A OD1 1 
ATOM   2230 N  ND2 . ASN   A 1 288 ? 17.64438  -9.52320  -21.81456 1.000 27.28651 ?  365 ASN   A ND2 1 
ATOM   2231 N  N   . ARG   A 1 289 ? 20.98976  -12.79553 -19.42742 1.000 27.43224 ?  366 ARG   A N   1 
ATOM   2232 C  CA  . ARG   A 1 289 ? 21.61896  -13.57680 -18.37571 1.000 26.23881 ?  366 ARG   A CA  1 
ATOM   2233 C  C   . ARG   A 1 289 ? 21.38070  -12.93446 -17.02706 1.000 26.21607 ?  366 ARG   A C   1 
ATOM   2234 O  O   . ARG   A 1 289 ? 22.27820  -12.86466 -16.18601 1.000 28.21047 ?  366 ARG   A O   1 
ATOM   2235 C  CB  . ARG   A 1 289 ? 23.11753  -13.73944 -18.62959 1.000 31.46288 ?  366 ARG   A CB  1 
ATOM   2236 C  CG  . ARG   A 1 289 ? 23.45870  -14.42344 -19.94578 1.000 31.32196 ?  366 ARG   A CG  1 
ATOM   2237 C  CD  . ARG   A 1 289 ? 24.89751  -14.84514 -19.97504 1.000 28.85315 ?  366 ARG   A CD  1 
ATOM   2238 N  NE  . ARG   A 1 289 ? 25.06735  -16.11236 -19.27179 1.000 39.76482 ?  366 ARG   A NE  1 
ATOM   2239 C  CZ  . ARG   A 1 289 ? 25.79728  -16.25926 -18.18050 1.000 37.87243 ?  366 ARG   A CZ  1 
ATOM   2240 N  NH1 . ARG   A 1 289 ? 26.48890  -15.24646 -17.67437 1.000 45.97508 ?  366 ARG   A NH1 1 
ATOM   2241 N  NH2 . ARG   A 1 289 ? 25.82795  -17.44305 -17.57572 1.000 36.03727 ?  366 ARG   A NH2 1 
ATOM   2242 N  N   . ILE   A 1 290 ? 20.16444  -12.44289 -16.80042 1.000 30.60673 ?  367 ILE   A N   1 
ATOM   2243 C  CA  . ILE   A 1 290 ? 19.84608  -11.74080 -15.55745 1.000 28.64083 ?  367 ILE   A CA  1 
ATOM   2244 C  C   . ILE   A 1 290 ? 19.81649  -12.75010 -14.42133 1.000 27.57779 ?  367 ILE   A C   1 
ATOM   2245 O  O   . ILE   A 1 290 ? 19.02951  -13.70134 -14.44939 1.000 27.34343 ?  367 ILE   A O   1 
ATOM   2246 C  CB  . ILE   A 1 290 ? 18.50556  -11.00606 -15.68705 1.000 27.65693 ?  367 ILE   A CB  1 
ATOM   2247 C  CG1 . ILE   A 1 290 ? 18.66834  -9.81523  -16.62059 1.000 26.48434 ?  367 ILE   A CG1 1 
ATOM   2248 C  CG2 . ILE   A 1 290 ? 17.96089  -10.60514 -14.31677 1.000 27.61610 ?  367 ILE   A CG2 1 
ATOM   2249 C  CD1 . ILE   A 1 290 ? 17.42079  -9.38997  -17.28921 1.000 26.58089 ?  367 ILE   A CD1 1 
ATOM   2250 N  N   . ASN   A 1 291 ? 20.65565  -12.54908 -13.40633 1.000 27.40397 ?  368 ASN   A N   1 
ATOM   2251 C  CA  . ASN   A 1 291 ? 20.74024  -13.58478 -12.38008 1.000 28.51720 ?  368 ASN   A CA  1 
ATOM   2252 C  C   . ASN   A 1 291 ? 19.81700  -13.35242 -11.19658 1.000 30.24938 ?  368 ASN   A C   1 
ATOM   2253 O  O   . ASN   A 1 291 ? 19.78874  -14.19055 -10.29183 1.000 30.67636 ?  368 ASN   A O   1 
ATOM   2254 C  CB  . ASN   A 1 291 ? 22.17692  -13.76253 -11.86728 1.000 29.52442 ?  368 ASN   A CB  1 
ATOM   2255 C  CG  . ASN   A 1 291 ? 22.78093  -12.47977 -11.34078 1.000 36.18304 ?  368 ASN   A CG  1 
ATOM   2256 O  OD1 . ASN   A 1 291 ? 22.36923  -11.95132 -10.29285 1.000 35.46149 ?  368 ASN   A OD1 1 
ATOM   2257 N  ND2 . ASN   A 1 291 ? 23.79760  -11.98017 -12.05151 1.000 37.12552 ?  368 ASN   A ND2 1 
ATOM   2258 N  N   . LYS   A 1 292 ? 19.04448  -12.27175 -11.17168 1.000 29.20755 ?  369 LYS   A N   1 
ATOM   2259 C  CA  . LYS   A 1 292 ? 18.10226  -12.12521 -10.06905 1.000 28.07761 ?  369 LYS   A CA  1 
ATOM   2260 C  C   . LYS   A 1 292 ? 17.14245  -10.98758 -10.38073 1.000 29.95677 ?  369 LYS   A C   1 
ATOM   2261 O  O   . LYS   A 1 292 ? 17.44288  -10.10791 -11.18376 1.000 31.93563 ?  369 LYS   A O   1 
ATOM   2262 C  CB  . LYS   A 1 292 ? 18.83340  -11.86948 -8.74513  1.000 31.97776 ?  369 LYS   A CB  1 
ATOM   2263 C  CG  . LYS   A 1 292 ? 19.38908  -10.46735 -8.58245  1.000 31.03474 ?  369 LYS   A CG  1 
ATOM   2264 C  CD  . LYS   A 1 292 ? 20.07177  -10.27344 -7.22324  1.000 30.45118 ?  369 LYS   A CD  1 
ATOM   2265 C  CE  . LYS   A 1 292 ? 19.14799  -10.69902 -6.08279  1.000 41.96292 ?  369 LYS   A CE  1 
ATOM   2266 N  NZ  . LYS   A 1 292 ? 19.46067  -10.12274 -4.70396  1.000 48.83105 ?  369 LYS   A NZ  1 
ATOM   2267 N  N   . ILE   A 1 293 ? 15.97849  -11.02377 -9.74769  1.000 29.58702 ?  370 ILE   A N   1 
ATOM   2268 C  CA  . ILE   A 1 293 ? 15.05941  -9.89004  -9.71563  1.000 30.54839 ?  370 ILE   A CA  1 
ATOM   2269 C  C   . ILE   A 1 293 ? 15.30355  -9.14463  -8.40876  1.000 29.69296 ?  370 ILE   A C   1 
ATOM   2270 O  O   . ILE   A 1 293 ? 15.05359  -9.71342  -7.33608  1.000 30.07282 ?  370 ILE   A O   1 
ATOM   2271 C  CB  . ILE   A 1 293 ? 13.59691  -10.34626 -9.82774  1.000 28.36258 ?  370 ILE   A CB  1 
ATOM   2272 C  CG1 . ILE   A 1 293 ? 13.38299  -11.17058 -11.09207 1.000 29.13468 ?  370 ILE   A CG1 1 
ATOM   2273 C  CG2 . ILE   A 1 293 ? 12.65590  -9.14932  -9.82017  1.000 29.88982 ?  370 ILE   A CG2 1 
ATOM   2274 C  CD1 . ILE   A 1 293 ? 12.00818  -11.82321 -11.15430 1.000 28.20890 ?  370 ILE   A CD1 1 
ATOM   2275 N  N   . PRO   A 1 294 ? 15.78385  -7.89395  -8.44310  1.000 27.35805 ?  371 PRO   A N   1 
ATOM   2276 C  CA  . PRO   A 1 294 ? 16.11419  -7.17594  -7.20120  1.000 31.75553 ?  371 PRO   A CA  1 
ATOM   2277 C  C   . PRO   A 1 294 ? 14.92354  -7.05009  -6.25697  1.000 31.24410 ?  371 PRO   A C   1 
ATOM   2278 O  O   . PRO   A 1 294 ? 13.78702  -6.83923  -6.68466  1.000 31.30402 ?  371 PRO   A O   1 
ATOM   2279 C  CB  . PRO   A 1 294 ? 16.55641  -5.78911  -7.69799  1.000 28.80375 ?  371 PRO   A CB  1 
ATOM   2280 C  CG  . PRO   A 1 294 ? 16.87346  -5.94798  -9.11268  1.000 27.76182 ?  371 PRO   A CG  1 
ATOM   2281 C  CD  . PRO   A 1 294 ? 16.04714  -7.07448  -9.63560  1.000 30.26962 ?  371 PRO   A CD  1 
ATOM   2282 N  N   . PHE   A 1 295 ? 15.19723  -7.15198  -4.95621  1.000 30.60743 ?  372 PHE   A N   1 
ATOM   2283 C  CA  . PHE   A 1 295 ? 14.16319  -6.88220  -3.95917  1.000 30.67013 ?  372 PHE   A CA  1 
ATOM   2284 C  C   . PHE   A 1 295 ? 13.71542  -5.43379  -4.07331  1.000 27.20319 ?  372 PHE   A C   1 
ATOM   2285 O  O   . PHE   A 1 295 ? 14.53912  -4.51789  -3.98730  1.000 29.87769 ?  372 PHE   A O   1 
ATOM   2286 C  CB  . PHE   A 1 295 ? 14.69665  -7.17094  -2.55203  1.000 30.05428 ?  372 PHE   A CB  1 
ATOM   2287 C  CG  . PHE   A 1 295 ? 13.69755  -6.91890  -1.44911  1.000 28.63486 ?  372 PHE   A CG  1 
ATOM   2288 C  CD1 . PHE   A 1 295 ? 12.79124  -7.89581  -1.07906  1.000 30.75972 ?  372 PHE   A CD1 1 
ATOM   2289 C  CD2 . PHE   A 1 295 ? 13.66296  -5.69877  -0.78605  1.000 31.27064 ?  372 PHE   A CD2 1 
ATOM   2290 C  CE1 . PHE   A 1 295 ? 11.86494  -7.67281  -0.06283  1.000 28.84367 ?  372 PHE   A CE1 1 
ATOM   2291 C  CE2 . PHE   A 1 295 ? 12.74778  -5.47052  0.23187   1.000 32.06821 ?  372 PHE   A CE2 1 
ATOM   2292 C  CZ  . PHE   A 1 295 ? 11.84993  -6.46291  0.59350   1.000 30.34458 ?  372 PHE   A CZ  1 
ATOM   2293 N  N   . GLY   A 1 296 ? 12.42360  -5.21642  -4.30087  1.000 28.10405 ?  373 GLY   A N   1 
ATOM   2294 C  CA  . GLY   A 1 296 ? 11.87938  -3.86890  -4.32233  1.000 27.27992 ?  373 GLY   A CA  1 
ATOM   2295 C  C   . GLY   A 1 296 ? 11.62561  -3.21797  -5.67907  1.000 32.73136 ?  373 GLY   A C   1 
ATOM   2296 O  O   . GLY   A 1 296 ? 10.94298  -2.18174  -5.70582  1.000 32.53712 ?  373 GLY   A O   1 
ATOM   2297 N  N   . ILE   A 1 297 ? 12.12816  -3.76180  -6.80291  1.000 28.69890 ?  374 ILE   A N   1 
ATOM   2298 C  CA  . ILE   A 1 297 ? 12.06007  -2.97371  -8.04451  1.000 32.06247 ?  374 ILE   A CA  1 
ATOM   2299 C  C   . ILE   A 1 297 ? 10.62425  -2.69457  -8.46029  1.000 33.26834 ?  374 ILE   A C   1 
ATOM   2300 O  O   . ILE   A 1 297 ? 10.36729  -1.72312  -9.18638  1.000 34.50558 ?  374 ILE   A O   1 
ATOM   2301 C  CB  . ILE   A 1 297 ? 12.79982  -3.61863  -9.24445  1.000 30.45236 ?  374 ILE   A CB  1 
ATOM   2302 C  CG1 . ILE   A 1 297 ? 13.03371  -5.11977  -9.04333  1.000 32.31097 ?  374 ILE   A CG1 1 
ATOM   2303 C  CG2 . ILE   A 1 297 ? 14.03003  -2.80454  -9.64321  1.000 31.47674 ?  374 ILE   A CG2 1 
ATOM   2304 C  CD1 . ILE   A 1 297 ? 11.77485  -5.94614  -9.14138  1.000 29.26238 ?  374 ILE   A CD1 1 
ATOM   2305 N  N   . PHE   A 1 298 ? 9.67307   -3.55203  -8.07516  1.000 30.63816 ?  375 PHE   A N   1 
ATOM   2306 C  CA  . PHE   A 1 298 ? 8.29214   -3.37629  -8.52055  1.000 31.84276 ?  375 PHE   A CA  1 
ATOM   2307 C  C   . PHE   A 1 298 ? 7.38235   -2.87549  -7.40526  1.000 32.20715 ?  375 PHE   A C   1 
ATOM   2308 O  O   . PHE   A 1 298 ? 6.15434   -2.98050  -7.52063  1.000 33.92827 ?  375 PHE   A O   1 
ATOM   2309 C  CB  . PHE   A 1 298 ? 7.73206   -4.67354  -9.11387  1.000 29.46184 ?  375 PHE   A CB  1 
ATOM   2310 C  CG  . PHE   A 1 298 ? 8.50902   -5.18995  -10.27563 1.000 27.68303 ?  375 PHE   A CG  1 
ATOM   2311 C  CD1 . PHE   A 1 298 ? 9.05872   -4.31446  -11.20752 1.000 30.37651 ?  375 PHE   A CD1 1 
ATOM   2312 C  CD2 . PHE   A 1 298 ? 8.71378   -6.55383  -10.43498 1.000 28.04606 ?  375 PHE   A CD2 1 
ATOM   2313 C  CE1 . PHE   A 1 298 ? 9.79324   -4.79870  -12.29722 1.000 30.00427 ?  375 PHE   A CE1 1 
ATOM   2314 C  CE2 . PHE   A 1 298 ? 9.44624   -7.04650  -11.51122 1.000 28.95912 ?  375 PHE   A CE2 1 
ATOM   2315 C  CZ  . PHE   A 1 298 ? 9.98842   -6.16864  -12.44245 1.000 28.07619 ?  375 PHE   A CZ  1 
ATOM   2316 N  N   . SER   A 1 299 ? 7.95802   -2.32836  -6.33002  1.000 31.39845 ?  376 SER   A N   1 
ATOM   2317 C  CA  . SER   A 1 299 ? 7.15069   -1.89175  -5.19527  1.000 31.16878 ?  376 SER   A CA  1 
ATOM   2318 C  C   . SER   A 1 299 ? 6.28786   -0.68461  -5.52273  1.000 32.54941 ?  376 SER   A C   1 
ATOM   2319 O  O   . SER   A 1 299 ? 5.28153   -0.45975  -4.84498  1.000 30.56850 ?  376 SER   A O   1 
ATOM   2320 C  CB  . SER   A 1 299 ? 8.04637   -1.56528  -4.01747  1.000 28.34570 ?  376 SER   A CB  1 
ATOM   2321 O  OG  . SER   A 1 299 ? 9.09818   -0.75268  -4.46907  1.000 36.06797 ?  376 SER   A OG  1 
ATOM   2322 N  N   . ARG   A 1 300 ? 6.65186   0.09124   -6.54155  1.000 33.09467 ?  377 ARG   A N   1 
ATOM   2323 C  CA  . ARG   A 1 300 ? 5.82564   1.19592   -7.00105  1.000 31.37700 ?  377 ARG   A CA  1 
ATOM   2324 C  C   . ARG   A 1 300 ? 5.08798   0.88051   -8.28932  1.000 31.64043 ?  377 ARG   A C   1 
ATOM   2325 O  O   . ARG   A 1 300 ? 4.29703   1.70623   -8.74685  1.000 28.98374 ?  377 ARG   A O   1 
ATOM   2326 C  CB  . ARG   A 1 300 ? 6.67746   2.45014   -7.19349  1.000 30.99901 ?  377 ARG   A CB  1 
ATOM   2327 C  CG  . ARG   A 1 300 ? 7.43153   2.82525   -5.94326  1.000 35.29706 ?  377 ARG   A CG  1 
ATOM   2328 C  CD  . ARG   A 1 300 ? 8.13293   4.15409   -6.08043  1.000 45.18893 ?  377 ARG   A CD  1 
ATOM   2329 N  NE  . ARG   A 1 300 ? 9.19930   4.26540   -5.09568  1.000 46.68230 ?  377 ARG   A NE  1 
ATOM   2330 C  CZ  . ARG   A 1 300 ? 10.04673  5.28174   -5.01233  1.000 49.39706 ?  377 ARG   A CZ  1 
ATOM   2331 N  NH1 . ARG   A 1 300 ? 9.93804   6.34444   -5.80085  1.000 49.29722 ?  377 ARG   A NH1 1 
ATOM   2332 N  NH2 . ARG   A 1 300 ? 11.03818  5.22490   -4.12594  1.000 48.44749 ?  377 ARG   A NH2 1 
ATOM   2333 N  N   . ALA   A 1 301 ? 5.32255   -0.28711  -8.89064  1.000 29.26385 ?  378 ALA   A N   1 
ATOM   2334 C  CA  . ALA   A 1 301 ? 4.78703   -0.54898  -10.22691 1.000 33.28859 ?  378 ALA   A CA  1 
ATOM   2335 C  C   . ALA   A 1 301 ? 3.30839   -0.90453  -10.09371 1.000 32.56358 ?  378 ALA   A C   1 
ATOM   2336 O  O   . ALA   A 1 301 ? 2.89293   -2.06013  -10.19251 1.000 28.33064 ?  378 ALA   A O   1 
ATOM   2337 C  CB  . ALA   A 1 301 ? 5.58153   -1.63563  -10.93118 1.000 29.58683 ?  378 ALA   A CB  1 
ATOM   2338 N  N   . LYS   A 1 302 ? 2.49716   0.13654   -9.89885  1.000 31.35305 ?  379 LYS   A N   1 
ATOM   2339 C  CA  . LYS   A 1 302 ? 1.08305   -0.06204  -9.60027  1.000 34.46264 ?  379 LYS   A CA  1 
ATOM   2340 C  C   . LYS   A 1 302 ? 0.35735   -0.82961  -10.70151 1.000 35.34609 ?  379 LYS   A C   1 
ATOM   2341 O  O   . LYS   A 1 302 ? -0.61366  -1.54503  -10.41902 1.000 34.57817 ?  379 LYS   A O   1 
ATOM   2342 C  CB  . LYS   A 1 302 ? 0.40952   1.28802   -9.37834  1.000 36.23040 ?  379 LYS   A CB  1 
ATOM   2343 C  CG  . LYS   A 1 302 ? 0.00070   1.55466   -7.97416  1.000 39.45009 ?  379 LYS   A CG  1 
ATOM   2344 C  CD  . LYS   A 1 302 ? 1.09274   2.23535   -7.19202  1.000 47.49371 ?  379 LYS   A CD  1 
ATOM   2345 C  CE  . LYS   A 1 302 ? 0.47634   2.94442   -5.99111  1.000 48.41354 ?  379 LYS   A CE  1 
ATOM   2346 N  NZ  . LYS   A 1 302 ? -0.71725  3.71207   -6.45764  1.000 56.99926 ?  379 LYS   A NZ  1 
ATOM   2347 N  N   . VAL   A 1 303 ? 0.80045   -0.70480  -11.95114 1.000 32.39043 ?  380 VAL   A N   1 
ATOM   2348 C  CA  . VAL   A 1 303 ? 0.08335   -1.32781  -13.05388 1.000 32.72202 ?  380 VAL   A CA  1 
ATOM   2349 C  C   . VAL   A 1 303 ? 0.95957   -2.30739  -13.83457 1.000 28.94140 ?  380 VAL   A C   1 
ATOM   2350 O  O   . VAL   A 1 303 ? 0.64850   -2.63674  -14.95838 1.000 32.41415 ?  380 VAL   A O   1 
ATOM   2351 C  CB  . VAL   A 1 303 ? -0.52427  -0.26173  -13.98250 1.000 32.75375 ?  380 VAL   A CB  1 
ATOM   2352 C  CG1 . VAL   A 1 303 ? -1.38085  0.72625   -13.15702 1.000 29.22345 ?  380 VAL   A CG1 1 
ATOM   2353 C  CG2 . VAL   A 1 303 ? 0.57346   0.44737   -14.74556 1.000 29.87819 ?  380 VAL   A CG2 1 
ATOM   2354 N  N   . LEU   A 1 304 ? 2.05268   -2.77962  -13.25262 1.000 29.28129 ?  381 LEU   A N   1 
ATOM   2355 C  CA  . LEU   A 1 304 ? 2.78628   -3.87936  -13.86361 1.000 27.39029 ?  381 LEU   A CA  1 
ATOM   2356 C  C   . LEU   A 1 304 ? 1.86134   -5.07816  -14.00603 1.000 28.53906 ?  381 LEU   A C   1 
ATOM   2357 O  O   . LEU   A 1 304 ? 1.27774   -5.54122  -13.02525 1.000 28.32079 ?  381 LEU   A O   1 
ATOM   2358 C  CB  . LEU   A 1 304 ? 4.00102   -4.24942  -13.01599 1.000 28.25572 ?  381 LEU   A CB  1 
ATOM   2359 C  CG  . LEU   A 1 304 ? 4.85270   -5.40005  -13.56033 1.000 29.56566 ?  381 LEU   A CG  1 
ATOM   2360 C  CD1 . LEU   A 1 304 ? 5.52248   -4.93693  -14.84321 1.000 31.85639 ?  381 LEU   A CD1 1 
ATOM   2361 C  CD2 . LEU   A 1 304 ? 5.88797   -5.80265  -12.54818 1.000 29.11198 ?  381 LEU   A CD2 1 
ATOM   2362 N  N   . SER   A 1 305 ? 1.70062   -5.57352  -15.22471 1.000 29.78679 ?  382 SER   A N   1 
ATOM   2363 C  CA  . SER   A 1 305 ? 0.84881   -6.73992  -15.38975 1.000 30.57606 ?  382 SER   A CA  1 
ATOM   2364 C  C   . SER   A 1 305 ? 1.36170   -7.77938  -16.37646 1.000 26.74202 ?  382 SER   A C   1 
ATOM   2365 O  O   . SER   A 1 305 ? 0.76410   -8.85341  -16.44557 1.000 24.39390 ?  382 SER   A O   1 
ATOM   2366 C  CB  . SER   A 1 305 ? -0.55980  -6.30362  -15.80083 1.000 30.16604 ?  382 SER   A CB  1 
ATOM   2367 O  OG  . SER   A 1 305 ? -0.48803  -5.48786  -16.92563 1.000 31.93116 ?  382 SER   A OG  1 
ATOM   2368 N  N   . LYS   A 1 306 ? 2.43475   -7.51706  -17.12456 1.000 26.19035 ?  383 LYS   A N   1 
ATOM   2369 C  CA  . LYS   A 1 306 ? 3.07898   -8.51311  -17.97619 1.000 26.49659 ?  383 LYS   A CA  1 
ATOM   2370 C  C   . LYS   A 1 306 ? 4.57996   -8.41380  -17.77238 1.000 28.00913 ?  383 LYS   A C   1 
ATOM   2371 O  O   . LYS   A 1 306 ? 5.18923   -7.38731  -18.09134 1.000 27.88551 ?  383 LYS   A O   1 
ATOM   2372 C  CB  . LYS   A 1 306 ? 2.75235   -8.32477  -19.45994 1.000 26.06488 ?  383 LYS   A CB  1 
ATOM   2373 C  CG  . LYS   A 1 306 ? 1.28234   -8.28598  -19.80170 1.000 33.28332 ?  383 LYS   A CG  1 
ATOM   2374 C  CD  . LYS   A 1 306 ? 1.09333   -8.11447  -21.32319 1.000 40.95902 ?  383 LYS   A CD  1 
ATOM   2375 C  CE  . LYS   A 1 306 ? -0.31840  -7.65214  -21.66536 1.000 47.75028 ?  383 LYS   A CE  1 
ATOM   2376 N  NZ  . LYS   A 1 306 ? -0.50378  -7.54744  -23.13631 1.000 50.40150 ?  383 LYS   A NZ  1 
ATOM   2377 N  N   . LEU   A 1 307 ? 5.17102   -9.47517  -17.23985 1.000 26.20937 ?  384 LEU   A N   1 
ATOM   2378 C  CA  . LEU   A 1 307 ? 6.60654   -9.55243  -17.05085 1.000 25.42661 ?  384 LEU   A CA  1 
ATOM   2379 C  C   . LEU   A 1 307 ? 7.07936   -10.82378 -17.73682 1.000 28.74359 ?  384 LEU   A C   1 
ATOM   2380 O  O   . LEU   A 1 307 ? 6.58385   -11.91502 -17.43216 1.000 29.59939 ?  384 LEU   A O   1 
ATOM   2381 C  CB  . LEU   A 1 307 ? 6.95970   -9.54446  -15.56433 1.000 22.81815 ?  384 LEU   A CB  1 
ATOM   2382 C  CG  . LEU   A 1 307 ? 8.42412   -9.81078  -15.21637 1.000 27.91647 ?  384 LEU   A CG  1 
ATOM   2383 C  CD1 . LEU   A 1 307 ? 9.31610   -8.77514  -15.87970 1.000 25.41401 ?  384 LEU   A CD1 1 
ATOM   2384 C  CD2 . LEU   A 1 307 ? 8.65842   -9.86920  -13.69507 1.000 24.22361 ?  384 LEU   A CD2 1 
ATOM   2385 N  N   . ASN   A 1 308 ? 8.01321   -10.68560 -18.67584 1.000 25.42151 ?  385 ASN   A N   1 
ATOM   2386 C  CA  . ASN   A 1 308 ? 8.59870   -11.82472 -19.37544 1.000 23.69287 ?  385 ASN   A CA  1 
ATOM   2387 C  C   . ASN   A 1 308 ? 10.07468  -11.89438 -19.00934 1.000 23.90888 ?  385 ASN   A C   1 
ATOM   2388 O  O   . ASN   A 1 308 ? 10.86874  -11.04591 -19.43792 1.000 26.28383 ?  385 ASN   A O   1 
ATOM   2389 C  CB  . ASN   A 1 308 ? 8.39890   -11.70669 -20.88986 1.000 26.71395 ?  385 ASN   A CB  1 
ATOM   2390 C  CG  . ASN   A 1 308 ? 8.71369   -13.00984 -21.62539 1.000 26.32237 ?  385 ASN   A CG  1 
ATOM   2391 O  OD1 . ASN   A 1 308 ? 9.47168   -13.83508 -21.13450 1.000 24.42149 ?  385 ASN   A OD1 1 
ATOM   2392 N  ND2 . ASN   A 1 308 ? 8.13804   -13.18181 -22.80819 1.000 24.39407 ?  385 ASN   A ND2 1 
ATOM   2393 N  N   . MET   A 1 309 ? 10.42584  -12.88297 -18.18600 1.000 27.26412 ?  386 MET   A N   1 
ATOM   2394 C  CA  . MET   A 1 309 ? 11.79494  -13.16709 -17.77413 1.000 26.15782 ?  386 MET   A CA  1 
ATOM   2395 C  C   . MET   A 1 309 ? 12.29787  -14.49009 -18.34247 1.000 29.06238 ?  386 MET   A C   1 
ATOM   2396 O  O   . MET   A 1 309 ? 13.24572  -15.06871 -17.79912 1.000 28.97343 ?  386 MET   A O   1 
ATOM   2397 C  CB  . MET   A 1 309 ? 11.90849  -13.19560 -16.25070 1.000 24.75633 ?  386 MET   A CB  1 
ATOM   2398 C  CG  . MET   A 1 309 ? 11.64386  -11.86086 -15.55635 1.000 28.56495 ?  386 MET   A CG  1 
ATOM   2399 S  SD  . MET   A 1 309 ? 13.04226  -10.73852 -15.63056 1.000 30.03632 ?  386 MET   A SD  1 
ATOM   2400 C  CE  . MET   A 1 309 ? 14.39042  -11.74687 -15.02713 1.000 29.24936 ?  386 MET   A CE  1 
ATOM   2401 N  N   . LYS   A 1 310 ? 11.68404  -14.97345 -19.42397 1.000 26.26816 ?  387 LYS   A N   1 
ATOM   2402 C  CA  . LYS   A 1 310 ? 12.07632  -16.24627 -20.02261 1.000 26.40164 ?  387 LYS   A CA  1 
ATOM   2403 C  C   . LYS   A 1 310 ? 13.54943  -16.24973 -20.42561 1.000 26.88573 ?  387 LYS   A C   1 
ATOM   2404 O  O   . LYS   A 1 310 ? 14.07775  -15.26129 -20.94409 1.000 26.16189 ?  387 LYS   A O   1 
ATOM   2405 C  CB  . LYS   A 1 310 ? 11.19984  -16.55677 -21.24447 1.000 23.61723 ?  387 LYS   A CB  1 
ATOM   2406 C  CG  . LYS   A 1 310 ? 11.52541  -17.89559 -21.89312 1.000 28.15714 ?  387 LYS   A CG  1 
ATOM   2407 C  CD  . LYS   A 1 310 ? 10.86642  -18.08968 -23.26207 1.000 27.49744 ?  387 LYS   A CD  1 
ATOM   2408 C  CE  . LYS   A 1 310 ? 11.02716  -19.52631 -23.73474 1.000 34.42471 ?  387 LYS   A CE  1 
ATOM   2409 N  NZ  . LYS   A 1 310 ? 10.43666  -19.76175 -25.08134 1.000 39.24702 ?  387 LYS   A NZ  1 
ATOM   2410 N  N   . ASP   A 1 311 ? 14.21382  -17.37915 -20.16539 1.000 27.39249 ?  388 ASP   A N   1 
ATOM   2411 C  CA  . ASP   A 1 311 ? 15.55773  -17.65492 -20.67036 1.000 26.97546 ?  388 ASP   A CA  1 
ATOM   2412 C  C   . ASP   A 1 311 ? 16.58451  -16.66601 -20.10749 1.000 27.34032 ?  388 ASP   A C   1 
ATOM   2413 O  O   . ASP   A 1 311 ? 17.33194  -16.01083 -20.84253 1.000 29.52744 ?  388 ASP   A O   1 
ATOM   2414 C  CB  . ASP   A 1 311 ? 15.56091  -17.66961 -22.20238 1.000 24.68479 ?  388 ASP   A CB  1 
ATOM   2415 C  CG  . ASP   A 1 311 ? 16.91549  -18.02761 -22.78541 1.000 27.32797 ?  388 ASP   A CG  1 
ATOM   2416 O  OD1 . ASP   A 1 311 ? 17.77579  -18.53264 -22.03785 1.000 29.65985 ?  388 ASP   A OD1 1 
ATOM   2417 O  OD2 . ASP   A 1 311 ? 17.14357  -17.77408 -23.99216 1.000 31.22121 ?  388 ASP   A OD2 1 
ATOM   2418 N  N   . ASN   A 1 312 ? 16.61948  -16.56810 -18.78160 1.000 23.01235 ?  389 ASN   A N   1 
ATOM   2419 C  CA  . ASN   A 1 312 ? 17.66883  -15.83195 -18.08970 1.000 25.88030 ?  389 ASN   A CA  1 
ATOM   2420 C  C   . ASN   A 1 312 ? 18.41565  -16.77395 -17.15010 1.000 28.49155 ?  389 ASN   A C   1 
ATOM   2421 O  O   . ASN   A 1 312 ? 18.52166  -17.96855 -17.43767 1.000 31.73366 ?  389 ASN   A O   1 
ATOM   2422 C  CB  . ASN   A 1 312 ? 17.08246  -14.63403 -17.33126 1.000 29.40867 ?  389 ASN   A CB  1 
ATOM   2423 C  CG  . ASN   A 1 312 ? 16.85995  -13.44126 -18.22808 1.000 26.84725 ?  389 ASN   A CG  1 
ATOM   2424 O  OD1 . ASN   A 1 312 ? 17.80129  -12.71726 -18.53358 1.000 27.65315 ?  389 ASN   A OD1 1 
ATOM   2425 N  ND2 . ASN   A 1 312 ? 15.62376  -13.24126 -18.67288 1.000 24.70372 ?  389 ASN   A ND2 1 
ATOM   2426 N  N   . GLN   A 1 313 ? 18.93001  -16.26645 -16.02960 1.000 24.28837 ?  390 GLN   A N   1 
ATOM   2427 C  CA  . GLN   A 1 313 ? 19.72922  -17.06297 -15.11104 1.000 27.44311 ?  390 GLN   A CA  1 
ATOM   2428 C  C   . GLN   A 1 313 ? 19.13343  -17.07950 -13.70238 1.000 28.87591 ?  390 GLN   A C   1 
ATOM   2429 O  O   . GLN   A 1 313 ? 19.87162  -17.14540 -12.71509 1.000 28.13611 ?  390 GLN   A O   1 
ATOM   2430 C  CB  . GLN   A 1 313 ? 21.17275  -16.55760 -15.07048 1.000 28.55459 ?  390 GLN   A CB  1 
ATOM   2431 C  CG  . GLN   A 1 313 ? 21.95823  -16.70831 -16.37220 1.000 29.03295 ?  390 GLN   A CG  1 
ATOM   2432 C  CD  . GLN   A 1 313 ? 22.36893  -18.13701 -16.66009 1.000 32.48431 ?  390 GLN   A CD  1 
ATOM   2433 O  OE1 . GLN   A 1 313 ? 23.23949  -18.68643 -15.99005 1.000 37.18206 ?  390 GLN   A OE1 1 
ATOM   2434 N  NE2 . GLN   A 1 313 ? 21.73098  -18.75239 -17.64663 1.000 32.72765 ?  390 GLN   A NE2 1 
ATOM   2435 N  N   . LEU   A 1 314 ? 17.80423  -17.04185 -13.59381 1.000 24.17225 ?  391 LEU   A N   1 
ATOM   2436 C  CA  . LEU   A 1 314 ? 17.14936  -17.02967 -12.29135 1.000 27.11576 ?  391 LEU   A CA  1 
ATOM   2437 C  C   . LEU   A 1 314 ? 17.29384  -18.37766 -11.59395 1.000 30.89767 ?  391 LEU   A C   1 
ATOM   2438 O  O   . LEU   A 1 314 ? 16.91444  -19.42017 -12.14874 1.000 32.23646 ?  391 LEU   A O   1 
ATOM   2439 C  CB  . LEU   A 1 314 ? 15.67154  -16.67391 -12.44065 1.000 26.21000 ?  391 LEU   A CB  1 
ATOM   2440 C  CG  . LEU   A 1 314 ? 15.36944  -15.30831 -13.06205 1.000 28.29300 ?  391 LEU   A CG  1 
ATOM   2441 C  CD1 . LEU   A 1 314 ? 13.88772  -14.97342 -12.91645 1.000 28.66396 ?  391 LEU   A CD1 1 
ATOM   2442 C  CD2 . LEU   A 1 314 ? 16.24405  -14.21433 -12.45182 1.000 28.50204 ?  391 LEU   A CD2 1 
ATOM   2443 N  N   . THR   A 1 315 ? 17.83103  -18.35984 -10.37152 1.000 28.23024 ?  392 THR   A N   1 
ATOM   2444 C  CA  . THR   A 1 315 ? 17.84908  -19.54252 -9.52388  1.000 30.39836 ?  392 THR   A CA  1 
ATOM   2445 C  C   . THR   A 1 315 ? 16.85339  -19.45806 -8.37776  1.000 33.12291 ?  392 THR   A C   1 
ATOM   2446 O  O   . THR   A 1 315 ? 16.60773  -20.46891 -7.71634  1.000 34.99224 ?  392 THR   A O   1 
ATOM   2447 C  CB  . THR   A 1 315 ? 19.25129  -19.79117 -8.94708  1.000 27.01902 ?  392 THR   A CB  1 
ATOM   2448 O  OG1 . THR   A 1 315 ? 19.78066  -18.55978 -8.45187  1.000 35.20774 ?  392 THR   A OG1 1 
ATOM   2449 C  CG2 . THR   A 1 315 ? 20.18337  -20.32574 -9.99957  1.000 24.62735 ?  392 THR   A CG2 1 
ATOM   2450 N  N   . SER   A 1 316 ? 16.28458  -18.28921 -8.11408  1.000 34.15170 ?  393 SER   A N   1 
ATOM   2451 C  CA  . SER   A 1 316 ? 15.15650  -18.19112 -7.19681  1.000 34.46965 ?  393 SER   A CA  1 
ATOM   2452 C  C   . SER   A 1 316 ? 14.40712  -16.90506 -7.50365  1.000 31.55396 ?  393 SER   A C   1 
ATOM   2453 O  O   . SER   A 1 316 ? 14.78303  -16.14228 -8.39567  1.000 31.58216 ?  393 SER   A O   1 
ATOM   2454 C  CB  . SER   A 1 316 ? 15.60285  -18.22379 -5.73784  1.000 32.04267 ?  393 SER   A CB  1 
ATOM   2455 O  OG  . SER   A 1 316 ? 16.25528  -17.01422 -5.40391  1.000 38.71427 ?  393 SER   A OG  1 
ATOM   2456 N  N   . LEU   A 1 317 ? 13.35394  -16.66382 -6.73006  1.000 32.45343 ?  394 LEU   A N   1 
ATOM   2457 C  CA  . LEU   A 1 317 ? 12.50498  -15.50571 -6.84805  1.000 29.09584 ?  394 LEU   A CA  1 
ATOM   2458 C  C   . LEU   A 1 317 ? 12.62223  -14.64581 -5.59557  1.000 31.53484 ?  394 LEU   A C   1 
ATOM   2459 O  O   . LEU   A 1 317 ? 12.84647  -15.16609 -4.50495  1.000 33.66361 ?  394 LEU   A O   1 
ATOM   2460 C  CB  . LEU   A 1 317 ? 11.05306  -15.93237 -7.07318  1.000 29.91991 ?  394 LEU   A CB  1 
ATOM   2461 C  CG  . LEU   A 1 317 ? 10.89172  -16.66422 -8.41712  1.000 34.56612 ?  394 LEU   A CG  1 
ATOM   2462 C  CD1 . LEU   A 1 317 ? 9.53900   -17.32948 -8.54964  1.000 28.92424 ?  394 LEU   A CD1 1 
ATOM   2463 C  CD2 . LEU   A 1 317 ? 11.11939  -15.69922 -9.57318  1.000 28.05204 ?  394 LEU   A CD2 1 
ATOM   2464 N  N   . PRO   A 1 318 ? 12.47730  -13.32985 -5.72434  1.000 33.04301 ?  395 PRO   A N   1 
ATOM   2465 C  CA  . PRO   A 1 318 ? 12.73444  -12.43469 -4.59120  1.000 30.06916 ?  395 PRO   A CA  1 
ATOM   2466 C  C   . PRO   A 1 318 ? 11.69471  -12.57329 -3.48718  1.000 28.36005 ?  395 PRO   A C   1 
ATOM   2467 O  O   . PRO   A 1 318 ? 10.57644  -13.03843 -3.70321  1.000 25.84520 ?  395 PRO   A O   1 
ATOM   2468 C  CB  . PRO   A 1 318 ? 12.66097  -11.05423 -5.23626  1.000 29.73919 ?  395 PRO   A CB  1 
ATOM   2469 C  CG  . PRO   A 1 318 ? 11.68618  -11.25453 -6.36469  1.000 26.77949 ?  395 PRO   A CG  1 
ATOM   2470 C  CD  . PRO   A 1 318 ? 12.00551  -12.59648 -6.91253  1.000 26.51339 ?  395 PRO   A CD  1 
ATOM   2471 N  N   . LEU   A 1 319 ? 12.07696  -12.10665 -2.28702  1.000 31.49642 ?  396 LEU   A N   1 
ATOM   2472 C  CA  . LEU   A 1 319 ? 11.23287  -12.25131 -1.09814  1.000 30.38645 ?  396 LEU   A CA  1 
ATOM   2473 C  C   . LEU   A 1 319 ? 9.86552   -11.60313 -1.26518  1.000 31.53918 ?  396 LEU   A C   1 
ATOM   2474 O  O   . LEU   A 1 319 ? 8.88486   -12.06004 -0.65309  1.000 30.62955 ?  396 LEU   A O   1 
ATOM   2475 C  CB  . LEU   A 1 319 ? 11.91562  -11.63081 0.11435   1.000 32.17282 ?  396 LEU   A CB  1 
ATOM   2476 C  CG  . LEU   A 1 319 ? 12.87339  -12.39667 1.01679   1.000 33.67259 ?  396 LEU   A CG  1 
ATOM   2477 C  CD1 . LEU   A 1 319 ? 13.46337  -11.37209 1.98382   1.000 30.89668 ?  396 LEU   A CD1 1 
ATOM   2478 C  CD2 . LEU   A 1 319 ? 12.15413  -13.54148 1.76993   1.000 32.36406 ?  396 LEU   A CD2 1 
ATOM   2479 N  N   . ASP   A 1 320 ? 9.79208   -10.51690 -2.04349  1.000 29.72381 ?  397 ASP   A N   1 
ATOM   2480 C  CA  . ASP   A 1 320 ? 8.59097   -9.69808  -2.20242  1.000 29.68579 ?  397 ASP   A CA  1 
ATOM   2481 C  C   . ASP   A 1 320 ? 7.80678   -10.08544 -3.44382  1.000 29.52098 ?  397 ASP   A C   1 
ATOM   2482 O  O   . ASP   A 1 320 ? 6.90479   -9.36066  -3.87287  1.000 32.18541 ?  397 ASP   A O   1 
ATOM   2483 C  CB  . ASP   A 1 320 ? 8.97043   -8.21694  -2.25111  1.000 25.41907 ?  397 ASP   A CB  1 
ATOM   2484 C  CG  . ASP   A 1 320 ? 9.98175   -7.91137  -3.33795  1.000 30.06339 ?  397 ASP   A CG  1 
ATOM   2485 O  OD1 . ASP   A 1 320 ? 10.50868  -8.86839  -3.95593  1.000 28.08447 ?  397 ASP   A OD1 1 
ATOM   2486 O  OD2 . ASP   A 1 320 ? 10.25149  -6.70597  -3.58564  1.000 32.84231 ?  397 ASP   A OD2 1 
ATOM   2487 N  N   . PHE   A 1 321 ? 8.14543   -11.22367 -4.02273  1.000 31.36163 ?  398 PHE   A N   1 
ATOM   2488 C  CA  . PHE   A 1 321 ? 7.50248   -11.70141 -5.23393  1.000 31.51101 ?  398 PHE   A CA  1 
ATOM   2489 C  C   . PHE   A 1 321 ? 5.98015   -11.74369 -5.09843  1.000 32.47311 ?  398 PHE   A C   1 
ATOM   2490 O  O   . PHE   A 1 321 ? 5.26065   -11.43245 -6.05388  1.000 34.52688 ?  398 PHE   A O   1 
ATOM   2491 C  CB  . PHE   A 1 321 ? 8.13488   -13.05487 -5.54106  1.000 31.47003 ?  398 PHE   A CB  1 
ATOM   2492 C  CG  . PHE   A 1 321 ? 7.31934   -13.96288 -6.37506  1.000 34.72749 ?  398 PHE   A CG  1 
ATOM   2493 C  CD1 . PHE   A 1 321 ? 7.06891   -13.67791 -7.71489  1.000 34.97111 ?  398 PHE   A CD1 1 
ATOM   2494 C  CD2 . PHE   A 1 321 ? 6.87370   -15.16379 -5.84357  1.000 31.77741 ?  398 PHE   A CD2 1 
ATOM   2495 C  CE1 . PHE   A 1 321 ? 6.33464   -14.57450 -8.51137  1.000 36.04785 ?  398 PHE   A CE1 1 
ATOM   2496 C  CE2 . PHE   A 1 321 ? 6.14041   -16.05127 -6.61920  1.000 34.09416 ?  398 PHE   A CE2 1 
ATOM   2497 C  CZ  . PHE   A 1 321 ? 5.86991   -15.75321 -7.96034  1.000 35.80804 ?  398 PHE   A CZ  1 
ATOM   2498 N  N   . GLY   A 1 322 ? 5.46909   -12.08141 -3.92592  1.000 32.55971 ?  399 GLY   A N   1 
ATOM   2499 C  CA  . GLY   A 1 322 ? 4.03296   -12.13969 -3.76294  1.000 31.10081 ?  399 GLY   A CA  1 
ATOM   2500 C  C   . GLY   A 1 322 ? 3.33606   -10.80654 -3.66881  1.000 32.99044 ?  399 GLY   A C   1 
ATOM   2501 O  O   . GLY   A 1 322 ? 2.11444   -10.78608 -3.49071  1.000 35.97105 ?  399 GLY   A O   1 
ATOM   2502 N  N   . THR   A 1 323 ? 4.06400   -9.69135  -3.76746  1.000 32.89392 ?  400 THR   A N   1 
ATOM   2503 C  CA  . THR   A 1 323 ? 3.43759   -8.37465  -3.75481  1.000 31.33927 ?  400 THR   A CA  1 
ATOM   2504 C  C   . THR   A 1 323 ? 3.00516   -7.90631  -5.13691  1.000 31.09086 ?  400 THR   A C   1 
ATOM   2505 O  O   . THR   A 1 323 ? 2.37151   -6.85005  -5.24168  1.000 32.41638 ?  400 THR   A O   1 
ATOM   2506 C  CB  . THR   A 1 323 ? 4.38227   -7.32417  -3.14461  1.000 31.58138 ?  400 THR   A CB  1 
ATOM   2507 O  OG1 . THR   A 1 323 ? 5.54192   -7.14998  -3.97283  1.000 29.31592 ?  400 THR   A OG1 1 
ATOM   2508 C  CG2 . THR   A 1 323 ? 4.82762   -7.76620  -1.77303  1.000 28.23669 ?  400 THR   A CG2 1 
ATOM   2509 N  N   . TRP   A 1 324 ? 3.32951   -8.65740  -6.19035  1.000 29.33535 ?  401 TRP   A N   1 
ATOM   2510 C  CA  . TRP   A 1 324 ? 3.00498   -8.26965  -7.56343  1.000 32.61124 ?  401 TRP   A CA  1 
ATOM   2511 C  C   . TRP   A 1 324 ? 1.51943   -8.52891  -7.86056  1.000 33.84411 ?  401 TRP   A C   1 
ATOM   2512 O  O   . TRP   A 1 324 ? 1.14045   -9.32904  -8.72828  1.000 27.70168 ?  401 TRP   A O   1 
ATOM   2513 C  CB  . TRP   A 1 324 ? 3.90229   -9.02094  -8.53734  1.000 29.85483 ?  401 TRP   A CB  1 
ATOM   2514 C  CG  . TRP   A 1 324 ? 5.38487   -8.89900  -8.27532  1.000 31.77623 ?  401 TRP   A CG  1 
ATOM   2515 C  CD1 . TRP   A 1 324 ? 6.01644   -8.00852  -7.44891  1.000 33.76104 ?  401 TRP   A CD1 1 
ATOM   2516 C  CD2 . TRP   A 1 324 ? 6.41527   -9.70462  -8.85422  1.000 30.83486 ?  401 TRP   A CD2 1 
ATOM   2517 N  NE1 . TRP   A 1 324 ? 7.38158   -8.21231  -7.48175  1.000 30.54610 ?  401 TRP   A NE1 1 
ATOM   2518 C  CE2 . TRP   A 1 324 ? 7.64941   -9.24246  -8.34212  1.000 28.76023 ?  401 TRP   A CE2 1 
ATOM   2519 C  CE3 . TRP   A 1 324 ? 6.41440   -10.76998 -9.76823  1.000 31.31684 ?  401 TRP   A CE3 1 
ATOM   2520 C  CZ2 . TRP   A 1 324 ? 8.86712   -9.81325  -8.70120  1.000 30.99689 ?  401 TRP   A CZ2 1 
ATOM   2521 C  CZ3 . TRP   A 1 324 ? 7.62909   -11.33376 -10.13401 1.000 31.26788 ?  401 TRP   A CZ3 1 
ATOM   2522 C  CH2 . TRP   A 1 324 ? 8.83984   -10.85593 -9.59930  1.000 32.98172 ?  401 TRP   A CH2 1 
ATOM   2523 N  N   . THR   A 1 325 ? 0.66643   -7.80203  -7.13310  1.000 27.42184 ?  402 THR   A N   1 
ATOM   2524 C  CA  . THR   A 1 325 ? -0.74783  -8.14150  -7.09226  1.000 28.82289 ?  402 THR   A CA  1 
ATOM   2525 C  C   . THR   A 1 325 ? -1.54741  -7.65901  -8.30012  1.000 29.15743 ?  402 THR   A C   1 
ATOM   2526 O  O   . THR   A 1 325 ? -2.73929  -7.96353  -8.37693  1.000 31.60091 ?  402 THR   A O   1 
ATOM   2527 C  CB  . THR   A 1 325 ? -1.38389  -7.60346  -5.80917  1.000 29.00349 ?  402 THR   A CB  1 
ATOM   2528 O  OG1 . THR   A 1 325 ? -1.20290  -6.18855  -5.73317  1.000 25.46897 ?  402 THR   A OG1 1 
ATOM   2529 C  CG2 . THR   A 1 325 ? -0.74598  -8.23785  -4.61054  1.000 29.25124 ?  402 THR   A CG2 1 
ATOM   2530 N  N   . SER   A 1 326 ? -0.96324  -6.94245  -9.25858  1.000 29.24439 ?  403 SER   A N   1 
ATOM   2531 C  CA  . SER   A 1 326 ? -1.71242  -6.63949  -10.47750 1.000 29.36337 ?  403 SER   A CA  1 
ATOM   2532 C  C   . SER   A 1 326 ? -1.15964  -7.36933  -11.69779 1.000 31.24740 ?  403 SER   A C   1 
ATOM   2533 O  O   . SER   A 1 326 ? -1.60802  -7.11413  -12.82677 1.000 33.53092 ?  403 SER   A O   1 
ATOM   2534 C  CB  . SER   A 1 326 ? -1.79555  -5.12211  -10.72193 1.000 31.21455 ?  403 SER   A CB  1 
ATOM   2535 O  OG  . SER   A 1 326 ? -0.54069  -4.48508  -10.66136 1.000 34.46834 ?  403 SER   A OG  1 
ATOM   2536 N  N   . MET   A 1 327 ? -0.24903  -8.31857  -11.49698 1.000 28.74854 ?  404 MET   A N   1 
ATOM   2537 C  CA  . MET   A 1 327 ? 0.30832   -9.05486  -12.61812 1.000 26.20143 ?  404 MET   A CA  1 
ATOM   2538 C  C   . MET   A 1 327 ? -0.71341  -10.01376 -13.22238 1.000 29.45223 ?  404 MET   A C   1 
ATOM   2539 O  O   . MET   A 1 327 ? -1.45132  -10.70257 -12.50974 1.000 30.42487 ?  404 MET   A O   1 
ATOM   2540 C  CB  . MET   A 1 327 ? 1.54468   -9.82686  -12.18363 1.000 25.47217 ?  404 MET   A CB  1 
ATOM   2541 C  CG  . MET   A 1 327 ? 2.32059   -10.32056 -13.36870 1.000 29.93201 ?  404 MET   A CG  1 
ATOM   2542 S  SD  . MET   A 1 327 ? 4.05842   -10.43489 -13.01714 1.000 38.41858 ?  404 MET   A SD  1 
ATOM   2543 C  CE  . MET   A 1 327 ? 4.48045   -8.74321  -12.70265 1.000 29.19120 ?  404 MET   A CE  1 
ATOM   2544 N  N   . VAL   A 1 328 ? -0.73976  -10.06441 -14.55166 1.000 26.22871 ?  405 VAL   A N   1 
ATOM   2545 C  CA  . VAL   A 1 328 ? -1.66841  -10.90177 -15.28969 1.000 27.68184 ?  405 VAL   A CA  1 
ATOM   2546 C  C   . VAL   A 1 328 ? -0.94556  -12.02286 -16.02751 1.000 27.36644 ?  405 VAL   A C   1 
ATOM   2547 O  O   . VAL   A 1 328 ? -1.43962  -13.15084 -16.08997 1.000 26.14619 ?  405 VAL   A O   1 
ATOM   2548 C  CB  . VAL   A 1 328 ? -2.51632  -10.04970 -16.26718 1.000 26.76150 ?  405 VAL   A CB  1 
ATOM   2549 C  CG1 . VAL   A 1 328 ? -3.41001  -10.92863 -17.11256 1.000 25.18178 ?  405 VAL   A CG1 1 
ATOM   2550 C  CG2 . VAL   A 1 328 ? -3.35563  -9.03471  -15.49548 1.000 24.50419 ?  405 VAL   A CG2 1 
ATOM   2551 N  N   . GLU   A 1 329 ? 0.22273   -11.73423 -16.58805 1.000 26.95143 ?  406 GLU   A N   1 
ATOM   2552 C  CA  . GLU   A 1 329 ? 1.00429   -12.72141 -17.32072 1.000 26.84397 ?  406 GLU   A CA  1 
ATOM   2553 C  C   . GLU   A 1 329 ? 2.43351   -12.68559 -16.80165 1.000 27.83230 ?  406 GLU   A C   1 
ATOM   2554 O  O   . GLU   A 1 329 ? 3.07297   -11.62407 -16.79464 1.000 23.55667 ?  406 GLU   A O   1 
ATOM   2555 C  CB  . GLU   A 1 329 ? 0.96326   -12.45454 -18.82606 1.000 26.03537 ?  406 GLU   A CB  1 
ATOM   2556 C  CG  . GLU   A 1 329 ? -0.44530  -12.20092 -19.36071 1.000 33.20050 ?  406 GLU   A CG  1 
ATOM   2557 C  CD  . GLU   A 1 329 ? -0.51429  -12.09656 -20.89227 1.000 44.86484 ?  406 GLU   A CD  1 
ATOM   2558 O  OE1 . GLU   A 1 329 ? 0.24191   -12.82349 -21.59104 1.000 42.39800 ?  406 GLU   A OE1 1 
ATOM   2559 O  OE2 . GLU   A 1 329 ? -1.34342  -11.28970 -21.38941 1.000 47.40970 ?  406 GLU   A OE2 1 
ATOM   2560 N  N   . LEU   A 1 330 ? 2.91976   -13.84181 -16.35749 1.000 22.48771 ?  407 LEU   A N   1 
ATOM   2561 C  CA  . LEU   A 1 330 ? 4.25362   -13.99104 -15.79848 1.000 25.46246 ?  407 LEU   A CA  1 
ATOM   2562 C  C   . LEU   A 1 330 ? 4.91562   -15.14801 -16.51599 1.000 24.62233 ?  407 LEU   A C   1 
ATOM   2563 O  O   . LEU   A 1 330 ? 4.45869   -16.28920 -16.39938 1.000 26.05659 ?  407 LEU   A O   1 
ATOM   2564 C  CB  . LEU   A 1 330 ? 4.20012   -14.25969 -14.28516 1.000 24.77088 ?  407 LEU   A CB  1 
ATOM   2565 C  CG  . LEU   A 1 330 ? 5.51031   -14.55720 -13.54128 1.000 24.38939 ?  407 LEU   A CG  1 
ATOM   2566 C  CD1 . LEU   A 1 330 ? 6.53819   -13.46515 -13.79782 1.000 26.68238 ?  407 LEU   A CD1 1 
ATOM   2567 C  CD2 . LEU   A 1 330 ? 5.26753   -14.70856 -12.05056 1.000 21.59385 ?  407 LEU   A CD2 1 
ATOM   2568 N  N   . ASN   A 1 331 ? 5.98557   -14.86967 -17.23876 1.000 23.85224 ?  408 ASN   A N   1 
ATOM   2569 C  CA  . ASN   A 1 331 ? 6.72751   -15.91411 -17.94197 1.000 26.27078 ?  408 ASN   A CA  1 
ATOM   2570 C  C   . ASN   A 1 331 ? 8.09203   -16.08942 -17.27069 1.000 25.59120 ?  408 ASN   A C   1 
ATOM   2571 O  O   . ASN   A 1 331 ? 8.93751   -15.18219 -17.29301 1.000 22.49450 ?  408 ASN   A O   1 
ATOM   2572 C  CB  . ASN   A 1 331 ? 6.85964   -15.57617 -19.42824 1.000 23.16568 ?  408 ASN   A CB  1 
ATOM   2573 C  CG  . ASN   A 1 331 ? 7.39863   -16.74312 -20.25064 1.000 26.72656 ?  408 ASN   A CG  1 
ATOM   2574 O  OD1 . ASN   A 1 331 ? 8.24339   -17.50697 -19.77742 1.000 25.70018 ?  408 ASN   A OD1 1 
ATOM   2575 N  ND2 . ASN   A 1 331 ? 6.90775   -16.88506 -21.48729 1.000 20.91500 ?  408 ASN   A ND2 1 
ATOM   2576 N  N   . LEU   A 1 332 ? 8.30690   -17.26486 -16.67792 1.000 27.72355 ?  409 LEU   A N   1 
ATOM   2577 C  CA  . LEU   A 1 332 ? 9.57728   -17.59559 -16.04338 1.000 23.55217 ?  409 LEU   A CA  1 
ATOM   2578 C  C   . LEU   A 1 332 ? 10.22414  -18.82238 -16.67705 1.000 26.41867 ?  409 LEU   A C   1 
ATOM   2579 O  O   . LEU   A 1 332 ? 11.11513  -19.43044 -16.07922 1.000 25.92020 ?  409 LEU   A O   1 
ATOM   2580 C  CB  . LEU   A 1 332 ? 9.37836   -17.79717 -14.54407 1.000 23.35297 ?  409 LEU   A CB  1 
ATOM   2581 C  CG  . LEU   A 1 332 ? 9.06647   -16.52662 -13.73646 1.000 26.01063 ?  409 LEU   A CG  1 
ATOM   2582 C  CD1 . LEU   A 1 332 ? 8.54166   -16.90017 -12.36161 1.000 24.68182 ?  409 LEU   A CD1 1 
ATOM   2583 C  CD2 . LEU   A 1 332 ? 10.28990  -15.63664 -13.60685 1.000 23.50543 ?  409 LEU   A CD2 1 
ATOM   2584 N  N   . ALA   A 1 333 ? 9.81771   -19.18030 -17.89147 1.000 26.02418 ?  410 ALA   A N   1 
ATOM   2585 C  CA  . ALA   A 1 333 ? 10.35305  -20.37328 -18.53496 1.000 28.54403 ?  410 ALA   A CA  1 
ATOM   2586 C  C   . ALA   A 1 333 ? 11.85419  -20.24615 -18.77845 1.000 27.30617 ?  410 ALA   A C   1 
ATOM   2587 O  O   . ALA   A 1 333 ? 12.41245  -19.15164 -18.83180 1.000 30.24031 ?  410 ALA   A O   1 
ATOM   2588 C  CB  . ALA   A 1 333 ? 9.62626   -20.64385 -19.85851 1.000 24.34520 ?  410 ALA   A CB  1 
ATOM   2589 N  N   . THR   A 1 334 ? 12.50394  -21.40311 -18.91331 1.000 27.10646 ?  411 THR   A N   1 
ATOM   2590 C  CA  . THR   A 1 334 ? 13.91074  -21.51603 -19.30546 1.000 27.53763 ?  411 THR   A CA  1 
ATOM   2591 C  C   . THR   A 1 334 ? 14.84241  -20.78159 -18.33818 1.000 27.92029 ?  411 THR   A C   1 
ATOM   2592 O  O   . THR   A 1 334 ? 15.86177  -20.20515 -18.73530 1.000 27.78685 ?  411 THR   A O   1 
ATOM   2593 C  CB  . THR   A 1 334 ? 14.13254  -21.04608 -20.74799 1.000 31.45309 ?  411 THR   A CB  1 
ATOM   2594 O  OG1 . THR   A 1 334 ? 13.16797  -21.66796 -21.61296 1.000 34.00581 ?  411 THR   A OG1 1 
ATOM   2595 C  CG2 . THR   A 1 334 ? 15.54976  -21.42751 -21.22781 1.000 27.02827 ?  411 THR   A CG2 1 
ATOM   2596 N  N   . ASN   A 1 335 ? 14.51950  -20.83862 -17.05609 1.000 24.38194 ?  412 ASN   A N   1 
ATOM   2597 C  CA  . ASN   A 1 335 ? 15.46364  -20.47989 -16.01273 1.000 28.99348 ?  412 ASN   A CA  1 
ATOM   2598 C  C   . ASN   A 1 335 ? 15.90174  -21.75645 -15.27151 1.000 29.63276 ?  412 ASN   A C   1 
ATOM   2599 O  O   . ASN   A 1 335 ? 15.68746  -22.88444 -15.74199 1.000 33.81681 ?  412 ASN   A O   1 
ATOM   2600 C  CB  . ASN   A 1 335 ? 14.85047  -19.41146 -15.08992 1.000 27.84251 ?  412 ASN   A CB  1 
ATOM   2601 C  CG  . ASN   A 1 335 ? 14.85893  -18.01464 -15.72069 1.000 29.05909 ?  412 ASN   A CG  1 
ATOM   2602 O  OD1 . ASN   A 1 335 ? 15.88265  -17.34734 -15.72763 1.000 29.07977 ?  412 ASN   A OD1 1 
ATOM   2603 N  ND2 . ASN   A 1 335 ? 13.71464  -17.57485 -16.24945 1.000 28.19818 ?  412 ASN   A ND2 1 
ATOM   2604 N  N   . GLN   A 1 336 ? 16.55966  -21.58333 -14.12770 1.000 29.68564 ?  413 GLN   A N   1 
ATOM   2605 C  CA  . GLN   A 1 336 ? 17.05339  -22.70079 -13.32516 1.000 30.47867 ?  413 GLN   A CA  1 
ATOM   2606 C  C   . GLN   A 1 336 ? 16.33931  -22.76790 -11.97629 1.000 28.77920 ?  413 GLN   A C   1 
ATOM   2607 O  O   . GLN   A 1 336 ? 16.93948  -23.07603 -10.95215 1.000 28.01953 ?  413 GLN   A O   1 
ATOM   2608 C  CB  . GLN   A 1 336 ? 18.56329  -22.60413 -13.12167 1.000 27.38590 ?  413 GLN   A CB  1 
ATOM   2609 C  CG  . GLN   A 1 336 ? 19.38215  -22.55849 -14.41116 1.000 31.40544 ?  413 GLN   A CG  1 
ATOM   2610 C  CD  . GLN   A 1 336 ? 19.40866  -21.16095 -15.02717 1.000 35.17301 ?  413 GLN   A CD  1 
ATOM   2611 O  OE1 . GLN   A 1 336 ? 19.58022  -20.17321 -14.31406 1.000 34.20879 ?  413 GLN   A OE1 1 
ATOM   2612 N  NE2 . GLN   A 1 336 ? 19.22298  -21.07034 -16.35326 1.000 33.51539 ?  413 GLN   A NE2 1 
ATOM   2613 N  N   . LEU   A 1 337 ? 15.05387  -22.44688 -11.95512 1.000 27.35386 ?  414 LEU   A N   1 
ATOM   2614 C  CA  . LEU   A 1 337 ? 14.33264  -22.43713 -10.69684 1.000 29.34089 ?  414 LEU   A CA  1 
ATOM   2615 C  C   . LEU   A 1 337 ? 14.14903  -23.86619 -10.20389 1.000 32.65772 ?  414 LEU   A C   1 
ATOM   2616 O  O   . LEU   A 1 337 ? 13.72767  -24.75145 -10.96054 1.000 27.28602 ?  414 LEU   A O   1 
ATOM   2617 C  CB  . LEU   A 1 337 ? 12.98023  -21.74482 -10.85245 1.000 27.70163 ?  414 LEU   A CB  1 
ATOM   2618 C  CG  . LEU   A 1 337 ? 12.92405  -20.28416 -11.32033 1.000 29.48754 ?  414 LEU   A CG  1 
ATOM   2619 C  CD1 . LEU   A 1 337 ? 11.49081  -19.83307 -11.45400 1.000 27.26305 ?  414 LEU   A CD1 1 
ATOM   2620 C  CD2 . LEU   A 1 337 ? 13.65924  -19.36051 -10.38368 1.000 29.97720 ?  414 LEU   A CD2 1 
ATOM   2621 N  N   . THR   A 1 338 ? 14.45925  -24.07875 -8.92292  1.000 31.95634 ?  415 THR   A N   1 
ATOM   2622 C  CA  . THR   A 1 338 ? 14.29016  -25.36358 -8.25714  1.000 33.09273 ?  415 THR   A CA  1 
ATOM   2623 C  C   . THR   A 1 338 ? 13.02598  -25.44657 -7.40629  1.000 33.87166 ?  415 THR   A C   1 
ATOM   2624 O  O   . THR   A 1 338 ? 12.55508  -26.55621 -7.13896  1.000 35.66984 ?  415 THR   A O   1 
ATOM   2625 C  CB  . THR   A 1 338 ? 15.50879  -25.65203 -7.37747  1.000 33.29888 ?  415 THR   A CB  1 
ATOM   2626 O  OG1 . THR   A 1 338 ? 16.06466  -24.40254 -6.91753  1.000 39.00058 ?  415 THR   A OG1 1 
ATOM   2627 C  CG2 . THR   A 1 338 ? 16.55063  -26.42105 -8.16900  1.000 28.37451 ?  415 THR   A CG2 1 
ATOM   2628 N  N   . LYS   A 1 339 ? 12.47244  -24.31486 -6.97134  1.000 34.56336 ?  416 LYS   A N   1 
ATOM   2629 C  CA  . LYS   A 1 339 ? 11.16188  -24.31254 -6.33816  1.000 35.08445 ?  416 LYS   A CA  1 
ATOM   2630 C  C   . LYS   A 1 339 ? 10.52488  -22.94113 -6.50291  1.000 32.80558 ?  416 LYS   A C   1 
ATOM   2631 O  O   . LYS   A 1 339 ? 11.20767  -21.94656 -6.74592  1.000 34.48880 ?  416 LYS   A O   1 
ATOM   2632 C  CB  . LYS   A 1 339 ? 11.24509  -24.69598 -4.86065  1.000 35.23406 ?  416 LYS   A CB  1 
ATOM   2633 C  CG  . LYS   A 1 339 ? 12.23022  -23.89818 -4.04361  1.000 39.43821 ?  416 LYS   A CG  1 
ATOM   2634 C  CD  . LYS   A 1 339 ? 12.37154  -24.55804 -2.67488  1.000 43.93822 ?  416 LYS   A CD  1 
ATOM   2635 C  CE  . LYS   A 1 339 ? 12.57382  -26.08479 -2.83760  1.000 53.04448 ?  416 LYS   A CE  1 
ATOM   2636 N  NZ  . LYS   A 1 339 ? 12.60202  -26.86571 -1.55258  1.000 55.23311 ?  416 LYS   A NZ  1 
ATOM   2637 N  N   . ILE   A 1 340 ? 9.20583   -22.90925 -6.38309  1.000 31.91113 ?  417 ILE   A N   1 
ATOM   2638 C  CA  . ILE   A 1 340 ? 8.43499   -21.66851 -6.38452  1.000 32.78749 ?  417 ILE   A CA  1 
ATOM   2639 C  C   . ILE   A 1 340 ? 8.03943   -21.35190 -4.95142  1.000 32.21983 ?  417 ILE   A C   1 
ATOM   2640 O  O   . ILE   A 1 340 ? 7.48172   -22.22907 -4.26589  1.000 29.99429 ?  417 ILE   A O   1 
ATOM   2641 C  CB  . ILE   A 1 340 ? 7.19151   -21.76726 -7.28799  1.000 35.16525 ?  417 ILE   A CB  1 
ATOM   2642 C  CG1 . ILE   A 1 340 ? 7.58894   -22.22504 -8.70121  1.000 32.68076 ?  417 ILE   A CG1 1 
ATOM   2643 C  CG2 . ILE   A 1 340 ? 6.47358   -20.41965 -7.35569  1.000 28.77959 ?  417 ILE   A CG2 1 
ATOM   2644 C  CD1 . ILE   A 1 340 ? 8.59245   -21.31075 -9.38152  1.000 28.76816 ?  417 ILE   A CD1 1 
ATOM   2645 N  N   . PRO   A 1 341 ? 8.29791   -20.14008 -4.45926  1.000 31.39577 ?  418 PRO   A N   1 
ATOM   2646 C  CA  . PRO   A 1 341 ? 8.02462   -19.83508 -3.05519  1.000 29.27507 ?  418 PRO   A CA  1 
ATOM   2647 C  C   . PRO   A 1 341 ? 6.53979   -19.89264 -2.75960  1.000 31.12649 ?  418 PRO   A C   1 
ATOM   2648 O  O   . PRO   A 1 341 ? 5.69349   -19.65778 -3.62400  1.000 32.66414 ?  418 PRO   A O   1 
ATOM   2649 C  CB  . PRO   A 1 341 ? 8.56085   -18.40733 -2.87570  1.000 28.72887 ?  418 PRO   A CB  1 
ATOM   2650 C  CG  . PRO   A 1 341 ? 9.38120   -18.11965 -4.06564  1.000 31.76845 ?  418 PRO   A CG  1 
ATOM   2651 C  CD  . PRO   A 1 341 ? 8.81559   -18.97131 -5.18289  1.000 34.05879 ?  418 PRO   A CD  1 
ATOM   2652 N  N   . GLU   A 1 342 ? 6.22510   -20.19096 -1.50502  1.000 32.54710 ?  419 GLU   A N   1 
ATOM   2653 C  CA  . GLU   A 1 342 ? 4.82383   -20.23054 -1.10941  1.000 32.60167 ?  419 GLU   A CA  1 
ATOM   2654 C  C   . GLU   A 1 342 ? 4.13005   -18.89026 -1.35230  1.000 33.26424 ?  419 GLU   A C   1 
ATOM   2655 O  O   . GLU   A 1 342 ? 2.91083   -18.85799 -1.55587  1.000 31.50183 ?  419 GLU   A O   1 
ATOM   2656 C  CB  . GLU   A 1 342 ? 4.71955   -20.66422 0.34984   1.000 31.85100 ?  419 GLU   A CB  1 
ATOM   2657 C  CG  . GLU   A 1 342 ? 5.08362   -22.12654 0.56899   1.000 28.54277 ?  419 GLU   A CG  1 
ATOM   2658 C  CD  . GLU   A 1 342 ? 3.99843   -23.06722 0.04936   1.000 36.84736 ?  419 GLU   A CD  1 
ATOM   2659 O  OE1 . GLU   A 1 342 ? 2.82151   -22.64060 0.00872   1.000 38.40649 ?  419 GLU   A OE1 1 
ATOM   2660 O  OE2 . GLU   A 1 342 ? 4.30861   -24.22627 -0.32281  1.000 39.54000 ?  419 GLU   A OE2 1 
ATOM   2661 N  N   . ASP   A 1 343 ? 4.88968   -17.78500 -1.39153  1.000 31.60633 ?  420 ASP   A N   1 
ATOM   2662 C  CA  . ASP   A 1 343 ? 4.32887   -16.45390 -1.62313  1.000 30.34957 ?  420 ASP   A CA  1 
ATOM   2663 C  C   . ASP   A 1 343 ? 3.71439   -16.24858 -3.00315  1.000 32.86732 ?  420 ASP   A C   1 
ATOM   2664 O  O   . ASP   A 1 343 ? 3.18791   -15.16524 -3.29316  1.000 32.02889 ?  420 ASP   A O   1 
ATOM   2665 C  CB  . ASP   A 1 343 ? 5.39744   -15.38405 -1.42454  1.000 36.30974 ?  420 ASP   A CB  1 
ATOM   2666 C  CG  . ASP   A 1 343 ? 5.98740   -15.41550 -0.04759  1.000 48.34561 ?  420 ASP   A CG  1 
ATOM   2667 O  OD1 . ASP   A 1 343 ? 6.75060   -16.38673 0.22389   1.000 52.29949 ?  420 ASP   A OD1 1 
ATOM   2668 O  OD2 . ASP   A 1 343 ? 5.68836   -14.48530 0.75281   1.000 41.83019 ?  420 ASP   A OD2 1 
ATOM   2669 N  N   . VAL   A 1 344 ? 3.80917   -17.25243 -3.87805  1.000 32.20795 ?  421 VAL   A N   1 
ATOM   2670 C  CA  . VAL   A 1 344 ? 3.15295   -17.15133 -5.17493  1.000 29.31506 ?  421 VAL   A CA  1 
ATOM   2671 C  C   . VAL   A 1 344 ? 1.67290   -16.88988 -4.99854  1.000 31.02939 ?  421 VAL   A C   1 
ATOM   2672 O  O   . VAL   A 1 344 ? 1.02368   -16.35036 -5.90129  1.000 31.08738 ?  421 VAL   A O   1 
ATOM   2673 C  CB  . VAL   A 1 344 ? 3.38164   -18.42883 -6.00570  1.000 33.29002 ?  421 VAL   A CB  1 
ATOM   2674 C  CG1 . VAL   A 1 344 ? 2.57480   -19.60080 -5.43725  1.000 27.03442 ?  421 VAL   A CG1 1 
ATOM   2675 C  CG2 . VAL   A 1 344 ? 3.00689   -18.17006 -7.45588  1.000 32.90016 ?  421 VAL   A CG2 1 
ATOM   2676 N  N   . SER   A 1 345 ? 1.12570   -17.26670 -3.83981  1.000 27.81206 ?  422 SER   A N   1 
ATOM   2677 C  CA  . SER   A 1 345 ? -0.28173  -17.07944 -3.52993  1.000 30.61598 ?  422 SER   A CA  1 
ATOM   2678 C  C   . SER   A 1 345 ? -0.69885  -15.61647 -3.50161  1.000 31.75037 ?  422 SER   A C   1 
ATOM   2679 O  O   . SER   A 1 345 ? -1.89931  -15.32860 -3.52962  1.000 33.98895 ?  422 SER   A O   1 
ATOM   2680 C  CB  . SER   A 1 345 ? -0.57277  -17.70119 -2.17138  1.000 31.80370 ?  422 SER   A CB  1 
ATOM   2681 O  OG  . SER   A 1 345 ? 0.25528   -17.07418 -1.21598  1.000 28.31236 ?  422 SER   A OG  1 
ATOM   2682 N  N   . GLY   A 1 346 ? 0.25214   -14.68503 -3.40861  1.000 32.46441 ?  423 GLY   A N   1 
ATOM   2683 C  CA  . GLY   A 1 346 ? -0.09492  -13.27373 -3.42792  1.000 29.11593 ?  423 GLY   A CA  1 
ATOM   2684 C  C   . GLY   A 1 346 ? -0.55917  -12.75328 -4.77798  1.000 30.30891 ?  423 GLY   A C   1 
ATOM   2685 O  O   . GLY   A 1 346 ? -1.22276  -11.71214 -4.82645  1.000 35.43246 ?  423 GLY   A O   1 
ATOM   2686 N  N   . LEU   A 1 347 ? -0.22851  -13.44857 -5.87268  1.000 31.68470 ?  424 LEU   A N   1 
ATOM   2687 C  CA  . LEU   A 1 347 ? -0.48455  -12.95896 -7.23456  1.000 29.95163 ?  424 LEU   A CA  1 
ATOM   2688 C  C   . LEU   A 1 347 ? -1.94511  -13.19747 -7.61893  1.000 30.30342 ?  424 LEU   A C   1 
ATOM   2689 O  O   . LEU   A 1 347 ? -2.27362  -14.02026 -8.47159  1.000 30.25111 ?  424 LEU   A O   1 
ATOM   2690 C  CB  . LEU   A 1 347 ? 0.44266   -13.64044 -8.22619  1.000 27.13435 ?  424 LEU   A CB  1 
ATOM   2691 C  CG  . LEU   A 1 347 ? 1.93455   -13.71690 -7.90160  1.000 31.20011 ?  424 LEU   A CG  1 
ATOM   2692 C  CD1 . LEU   A 1 347 ? 2.66992   -14.36078 -9.05109  1.000 35.06775 ?  424 LEU   A CD1 1 
ATOM   2693 C  CD2 . LEU   A 1 347 ? 2.50840   -12.35533 -7.65806  1.000 33.91336 ?  424 LEU   A CD2 1 
ATOM   2694 N  N   . VAL   A 1 348 ? -2.83817  -12.43578 -6.98300  1.000 28.11645 ?  425 VAL   A N   1 
ATOM   2695 C  CA  . VAL   A 1 348 ? -4.25724  -12.72712 -7.13825  1.000 30.56923 ?  425 VAL   A CA  1 
ATOM   2696 C  C   . VAL   A 1 348 ? -4.76645  -12.34025 -8.51505  1.000 29.29933 ?  425 VAL   A C   1 
ATOM   2697 O  O   . VAL   A 1 348 ? -5.84206  -12.78902 -8.92178  1.000 32.86904 ?  425 VAL   A O   1 
ATOM   2698 C  CB  . VAL   A 1 348 ? -5.07866  -12.03881 -6.03112  1.000 27.32245 ?  425 VAL   A CB  1 
ATOM   2699 C  CG1 . VAL   A 1 348 ? -4.82656  -12.74585 -4.70165  1.000 31.42335 ?  425 VAL   A CG1 1 
ATOM   2700 C  CG2 . VAL   A 1 348 ? -4.70716  -10.57713 -5.93854  1.000 28.42264 ?  425 VAL   A CG2 1 
ATOM   2701 N  N   . SER   A 1 349 ? -4.02311  -11.53884 -9.25621  1.000 26.76479 ?  426 SER   A N   1 
ATOM   2702 C  CA  . SER   A 1 349 ? -4.44776  -11.18540 -10.60152 1.000 30.88838 ?  426 SER   A CA  1 
ATOM   2703 C  C   . SER   A 1 349 ? -3.95510  -12.15189 -11.67734 1.000 27.10309 ?  426 SER   A C   1 
ATOM   2704 O  O   . SER   A 1 349 ? -4.34711  -12.00365 -12.83752 1.000 30.02107 ?  426 SER   A O   1 
ATOM   2705 C  CB  . SER   A 1 349 ? -3.97066  -9.77175  -10.93271 1.000 25.57587 ?  426 SER   A CB  1 
ATOM   2706 O  OG  . SER   A 1 349 ? -4.60818  -8.84812  -10.08108 1.000 29.41118 ?  426 SER   A OG  1 
ATOM   2707 N  N   . LEU   A 1 350 ? -3.12620  -13.13375 -11.33463 1.000 27.60406 ?  427 LEU   A N   1 
ATOM   2708 C  CA  . LEU   A 1 350 ? -2.41145  -13.89483 -12.35737 1.000 27.88915 ?  427 LEU   A CA  1 
ATOM   2709 C  C   . LEU   A 1 350 ? -3.38474  -14.71903 -13.19435 1.000 29.17809 ?  427 LEU   A C   1 
ATOM   2710 O  O   . LEU   A 1 350 ? -4.17261  -15.50848 -12.65566 1.000 28.15016 ?  427 LEU   A O   1 
ATOM   2711 C  CB  . LEU   A 1 350 ? -1.35297  -14.78847 -11.71540 1.000 25.27272 ?  427 LEU   A CB  1 
ATOM   2712 C  CG  . LEU   A 1 350 ? -0.15722  -15.19796 -12.59160 1.000 26.91861 ?  427 LEU   A CG  1 
ATOM   2713 C  CD1 . LEU   A 1 350 ? 0.59819   -13.99118 -13.13742 1.000 27.07845 ?  427 LEU   A CD1 1 
ATOM   2714 C  CD2 . LEU   A 1 350 ? 0.78311   -16.09928 -11.83585 1.000 25.11372 ?  427 LEU   A CD2 1 
ATOM   2715 N  N   . GLU   A 1 351 ? -3.33960  -14.51777 -14.52012 1.000 29.84540 ?  428 GLU   A N   1 
ATOM   2716 C  CA  . GLU   A 1 351 ? -4.08215  -15.34716 -15.45629 1.000 26.48005 ?  428 GLU   A CA  1 
ATOM   2717 C  C   . GLU   A 1 351 ? -3.21166  -16.32839 -16.21806 1.000 26.42374 ?  428 GLU   A C   1 
ATOM   2718 O  O   . GLU   A 1 351 ? -3.72270  -17.36217 -16.66492 1.000 28.86465 ?  428 GLU   A O   1 
ATOM   2719 C  CB  . GLU   A 1 351 ? -4.85470  -14.46795 -16.45384 1.000 26.57757 ?  428 GLU   A CB  1 
ATOM   2720 C  CG  . GLU   A 1 351 ? -5.96378  -13.67812 -15.76174 1.000 30.00193 ?  428 GLU   A CG  1 
ATOM   2721 C  CD  . GLU   A 1 351 ? -6.81896  -12.79161 -16.66401 1.000 35.26726 ?  428 GLU   A CD  1 
ATOM   2722 O  OE1 . GLU   A 1 351 ? -7.13929  -13.16515 -17.81248 1.000 42.18262 ?  428 GLU   A OE1 1 
ATOM   2723 O  OE2 . GLU   A 1 351 ? -7.20471  -11.69871 -16.19308 1.000 43.70706 ?  428 GLU   A OE2 1 
ATOM   2724 N  N   . VAL   A 1 352 ? -1.91866  -16.04829 -16.37204 1.000 26.41316 ?  429 VAL   A N   1 
ATOM   2725 C  CA  . VAL   A 1 352 ? -1.03458  -16.88710 -17.17511 1.000 25.39582 ?  429 VAL   A CA  1 
ATOM   2726 C  C   . VAL   A 1 352 ? 0.25961   -17.08753 -16.40866 1.000 26.15585 ?  429 VAL   A C   1 
ATOM   2727 O  O   . VAL   A 1 352 ? 0.94226   -16.11665 -16.07619 1.000 24.81131 ?  429 VAL   A O   1 
ATOM   2728 C  CB  . VAL   A 1 352 ? -0.74015  -16.28218 -18.55902 1.000 27.45812 ?  429 VAL   A CB  1 
ATOM   2729 C  CG1 . VAL   A 1 352 ? 0.41465   -17.01926 -19.25133 1.000 22.34670 ?  429 VAL   A CG1 1 
ATOM   2730 C  CG2 . VAL   A 1 352 ? -1.98740  -16.32830 -19.41525 1.000 29.10523 ?  429 VAL   A CG2 1 
ATOM   2731 N  N   . LEU   A 1 353 ? 0.61035   -18.33884 -16.14415 1.000 23.02327 ?  430 LEU   A N   1 
ATOM   2732 C  CA  . LEU   A 1 353 ? 1.86867   -18.65193 -15.49183 1.000 22.70370 ?  430 LEU   A CA  1 
ATOM   2733 C  C   . LEU   A 1 353 ? 2.61776   -19.60836 -16.39516 1.000 23.56547 ?  430 LEU   A C   1 
ATOM   2734 O  O   . LEU   A 1 353 ? 2.11659   -20.69137 -16.70930 1.000 28.59730 ?  430 LEU   A O   1 
ATOM   2735 C  CB  . LEU   A 1 353 ? 1.63913   -19.24437 -14.09841 1.000 22.85659 ?  430 LEU   A CB  1 
ATOM   2736 C  CG  . LEU   A 1 353 ? 2.87969   -19.42692 -13.22575 1.000 21.03363 ?  430 LEU   A CG  1 
ATOM   2737 C  CD1 . LEU   A 1 353 ? 3.77632   -18.19808 -13.26715 1.000 22.24435 ?  430 LEU   A CD1 1 
ATOM   2738 C  CD2 . LEU   A 1 353 ? 2.48279   -19.76790 -11.79716 1.000 21.12404 ?  430 LEU   A CD2 1 
ATOM   2739 N  N   . ILE   A 1 354 ? 3.79159   -19.19701 -16.84780 1.000 23.35107 ?  431 ILE   A N   1 
ATOM   2740 C  CA  . ILE   A 1 354 ? 4.63211   -20.02649 -17.69220 1.000 23.66760 ?  431 ILE   A CA  1 
ATOM   2741 C  C   . ILE   A 1 354 ? 5.88412   -20.35853 -16.89333 1.000 26.58934 ?  431 ILE   A C   1 
ATOM   2742 O  O   . ILE   A 1 354 ? 6.64793   -19.45858 -16.51906 1.000 26.79994 ?  431 ILE   A O   1 
ATOM   2743 C  CB  . ILE   A 1 354 ? 4.98522   -19.32605 -19.01264 1.000 25.65390 ?  431 ILE   A CB  1 
ATOM   2744 C  CG1 . ILE   A 1 354 ? 3.75266   -18.66904 -19.64832 1.000 27.19777 ?  431 ILE   A CG1 1 
ATOM   2745 C  CG2 . ILE   A 1 354 ? 5.60466   -20.31673 -19.97135 1.000 25.64087 ?  431 ILE   A CG2 1 
ATOM   2746 C  CD1 . ILE   A 1 354 ? 2.68599   -19.64374 -20.05225 1.000 28.70190 ?  431 ILE   A CD1 1 
ATOM   2747 N  N   . LEU   A 1 355 ? 6.09319   -21.65142 -16.63198 1.000 26.82376 ?  432 LEU   A N   1 
ATOM   2748 C  CA  . LEU   A 1 355 ? 7.21658   -22.12619 -15.83326 1.000 26.32172 ?  432 LEU   A CA  1 
ATOM   2749 C  C   . LEU   A 1 355 ? 7.94926   -23.25733 -16.53576 1.000 28.46207 ?  432 LEU   A C   1 
ATOM   2750 O  O   . LEU   A 1 355 ? 8.66194   -24.02684 -15.88383 1.000 28.20507 ?  432 LEU   A O   1 
ATOM   2751 C  CB  . LEU   A 1 355 ? 6.74623   -22.58868 -14.45324 1.000 23.21039 ?  432 LEU   A CB  1 
ATOM   2752 C  CG  . LEU   A 1 355 ? 6.35419   -21.43393 -13.53570 1.000 27.31975 ?  432 LEU   A CG  1 
ATOM   2753 C  CD1 . LEU   A 1 355 ? 5.37821   -21.85920 -12.43512 1.000 23.27886 ?  432 LEU   A CD1 1 
ATOM   2754 C  CD2 . LEU   A 1 355 ? 7.61842   -20.83953 -12.95214 1.000 28.01037 ?  432 LEU   A CD2 1 
ATOM   2755 N  N   . SER   A 1 356 ? 7.78552   -23.37464 -17.84682 1.000 28.31210 ?  433 SER   A N   1 
ATOM   2756 C  CA  . SER   A 1 356 ? 8.29877   -24.53855 -18.55004 1.000 29.14034 ?  433 SER   A CA  1 
ATOM   2757 C  C   . SER   A 1 356 ? 9.82390   -24.54703 -18.56966 1.000 31.35241 ?  433 SER   A C   1 
ATOM   2758 O  O   . SER   A 1 356 ? 10.47187  -23.49970 -18.64984 1.000 29.75378 ?  433 SER   A O   1 
ATOM   2759 C  CB  . SER   A 1 356 ? 7.75097   -24.58846 -19.97252 1.000 30.04850 ?  433 SER   A CB  1 
ATOM   2760 O  OG  . SER   A 1 356 ? 7.55239   -23.30228 -20.50121 1.000 32.69709 ?  433 SER   A OG  1 
ATOM   2761 N  N   . ASN   A 1 357 ? 10.39244  -25.74948 -18.45075 1.000 29.23788 ?  434 ASN   A N   1 
ATOM   2762 C  CA  . ASN   A 1 357 ? 11.80941  -25.97007 -18.68251 1.000 29.55281 ?  434 ASN   A CA  1 
ATOM   2763 C  C   . ASN   A 1 357 ? 12.67429  -25.32386 -17.59905 1.000 32.05560 ?  434 ASN   A C   1 
ATOM   2764 O  O   . ASN   A 1 357 ? 13.75640  -24.79048 -17.87343 1.000 32.98426 ?  434 ASN   A O   1 
ATOM   2765 C  CB  . ASN   A 1 357 ? 12.19473  -25.47622 -20.07242 1.000 29.74780 ?  434 ASN   A CB  1 
ATOM   2766 C  CG  . ASN   A 1 357 ? 13.53434  -25.97622 -20.49615 1.000 34.24694 ?  434 ASN   A CG  1 
ATOM   2767 O  OD1 . ASN   A 1 357 ? 14.10736  -26.86623 -19.86126 1.000 30.06893 ?  434 ASN   A OD1 1 
ATOM   2768 N  ND2 . ASN   A 1 357 ? 14.05483  -25.41144 -21.58074 1.000 36.55587 ?  434 ASN   A ND2 1 
ATOM   2769 N  N   . ASN   A 1 358 ? 12.17524  -25.34506 -16.36104 1.000 29.50766 ?  435 ASN   A N   1 
ATOM   2770 C  CA  . ASN   A 1 358 ? 13.00772  -25.11226 -15.18937 1.000 28.29235 ?  435 ASN   A CA  1 
ATOM   2771 C  C   . ASN   A 1 358 ? 13.42117  -26.46643 -14.60199 1.000 30.71008 ?  435 ASN   A C   1 
ATOM   2772 O  O   . ASN   A 1 358 ? 13.53702  -27.44990 -15.33506 1.000 32.51267 ?  435 ASN   A O   1 
ATOM   2773 C  CB  . ASN   A 1 358 ? 12.26032  -24.24108 -14.17319 1.000 27.08190 ?  435 ASN   A CB  1 
ATOM   2774 C  CG  . ASN   A 1 358 ? 12.27100  -22.75846 -14.55203 1.000 27.98445 ?  435 ASN   A CG  1 
ATOM   2775 O  OD1 . ASN   A 1 358 ? 13.20167  -22.01872 -14.20568 1.000 27.32203 ?  435 ASN   A OD1 1 
ATOM   2776 N  ND2 . ASN   A 1 358 ? 11.23739  -22.31997 -15.25808 1.000 25.33988 ?  435 ASN   A ND2 1 
ATOM   2777 N  N   . LEU   A 1 359 ? 13.64087  -26.53620 -13.29074 1.000 32.56265 ?  436 LEU   A N   1 
ATOM   2778 C  CA  . LEU   A 1 359 ? 14.12949  -27.72582 -12.59146 1.000 30.51550 ?  436 LEU   A CA  1 
ATOM   2779 C  C   . LEU   A 1 359 ? 13.23202  -28.07175 -11.40789 1.000 31.25593 ?  436 LEU   A C   1 
ATOM   2780 O  O   . LEU   A 1 359 ? 13.71201  -28.41962 -10.32745 1.000 32.46926 ?  436 LEU   A O   1 
ATOM   2781 C  CB  . LEU   A 1 359 ? 15.55990  -27.52156 -12.09136 1.000 32.69055 ?  436 LEU   A CB  1 
ATOM   2782 C  CG  . LEU   A 1 359 ? 16.81758  -27.62757 -12.95509 1.000 34.10780 ?  436 LEU   A CG  1 
ATOM   2783 C  CD1 . LEU   A 1 359 ? 16.49272  -27.74208 -14.41587 1.000 39.78224 ?  436 LEU   A CD1 1 
ATOM   2784 C  CD2 . LEU   A 1 359 ? 17.70525  -26.43008 -12.69019 1.000 30.30501 ?  436 LEU   A CD2 1 
ATOM   2785 N  N   . LEU   A 1 360 ? 11.92059  -27.95895 -11.57089 1.000 28.44690 ?  437 LEU   A N   1 
ATOM   2786 C  CA  . LEU   A 1 360 ? 11.00907  -28.07962 -10.44303 1.000 32.14334 ?  437 LEU   A CA  1 
ATOM   2787 C  C   . LEU   A 1 360 ? 10.64187  -29.54131 -10.19179 1.000 28.88616 ?  437 LEU   A C   1 
ATOM   2788 O  O   . LEU   A 1 360 ? 10.24844  -30.25155 -11.11346 1.000 26.34227 ?  437 LEU   A O   1 
ATOM   2789 C  CB  . LEU   A 1 360 ? 9.75051   -27.24852 -10.69627 1.000 28.97901 ?  437 LEU   A CB  1 
ATOM   2790 C  CG  . LEU   A 1 360 ? 9.96506   -25.74364 -10.85093 1.000 32.59958 ?  437 LEU   A CG  1 
ATOM   2791 C  CD1 . LEU   A 1 360 ? 8.70024   -25.08513 -11.38141 1.000 29.50471 ?  437 LEU   A CD1 1 
ATOM   2792 C  CD2 . LEU   A 1 360 ? 10.37031  -25.09849 -9.52536  1.000 32.37605 ?  437 LEU   A CD2 1 
ATOM   2793 N  N   . LYS   A 1 361 ? 10.76305  -29.98209 -8.93847  1.000 33.42726 ?  438 LYS   A N   1 
ATOM   2794 C  CA  . LYS   A 1 361 ? 10.31898  -31.31609 -8.53906  1.000 33.58638 ?  438 LYS   A CA  1 
ATOM   2795 C  C   . LYS   A 1 361 ? 8.96020   -31.30919 -7.86567  1.000 31.42879 ?  438 LYS   A C   1 
ATOM   2796 O  O   . LYS   A 1 361 ? 8.27935   -32.34217 -7.87761  1.000 32.03463 ?  438 LYS   A O   1 
ATOM   2797 C  CB  . LYS   A 1 361 ? 11.32602  -31.97380 -7.58374  1.000 31.64403 ?  438 LYS   A CB  1 
ATOM   2798 C  CG  . LYS   A 1 361 ? 12.66101  -32.25471 -8.21541  1.000 35.90357 ?  438 LYS   A CG  1 
ATOM   2799 C  CD  . LYS   A 1 361 ? 13.51220  -33.16355 -7.35252  1.000 45.13402 ?  438 LYS   A CD  1 
ATOM   2800 C  CE  . LYS   A 1 361 ? 14.95713  -33.19254 -7.85547  1.000 47.00937 ?  438 LYS   A CE  1 
ATOM   2801 N  NZ  . LYS   A 1 361 ? 15.84464  -33.94399 -6.91877  1.000 53.36395 ?  438 LYS   A NZ  1 
ATOM   2802 N  N   . LYS   A 1 362 ? 8.56742   -30.18198 -7.27369  1.000 30.11347 ?  439 LYS   A N   1 
ATOM   2803 C  CA  . LYS   A 1 362 ? 7.27930   -30.03651 -6.60816  1.000 34.18052 ?  439 LYS   A CA  1 
ATOM   2804 C  C   . LYS   A 1 362 ? 6.82781   -28.58426 -6.73368  1.000 32.33288 ?  439 LYS   A C   1 
ATOM   2805 O  O   . LYS   A 1 362 ? 7.63611   -27.68724 -6.97802  1.000 32.43205 ?  439 LYS   A O   1 
ATOM   2806 C  CB  . LYS   A 1 362 ? 7.36677   -30.46279 -5.13612  1.000 32.18501 ?  439 LYS   A CB  1 
ATOM   2807 C  CG  . LYS   A 1 362 ? 8.25914   -29.54929 -4.32093  1.000 39.39109 ?  439 LYS   A CG  1 
ATOM   2808 C  CD  . LYS   A 1 362 ? 8.48969   -30.07399 -2.90477  1.000 49.80759 ?  439 LYS   A CD  1 
ATOM   2809 C  CE  . LYS   A 1 362 ? 9.05894   -28.98542 -1.99079  1.000 52.99461 ?  439 LYS   A CE  1 
ATOM   2810 N  NZ  . LYS   A 1 362 ? 10.13517  -28.16655 -2.64233  1.000 50.94071 ?  439 LYS   A NZ  1 
ATOM   2811 N  N   . LEU   A 1 363 ? 5.52367   -28.35897 -6.59072  1.000 31.46447 ?  440 LEU   A N   1 
ATOM   2812 C  CA  . LEU   A 1 363 ? 4.96600   -27.01325 -6.55388  1.000 32.65179 ?  440 LEU   A CA  1 
ATOM   2813 C  C   . LEU   A 1 363 ? 4.55258   -26.65555 -5.14034  1.000 32.19458 ?  440 LEU   A C   1 
ATOM   2814 O  O   . LEU   A 1 363 ? 4.27178   -27.53661 -4.32315  1.000 31.78869 ?  440 LEU   A O   1 
ATOM   2815 C  CB  . LEU   A 1 363 ? 3.74622   -26.88171 -7.47679  1.000 32.11881 ?  440 LEU   A CB  1 
ATOM   2816 C  CG  . LEU   A 1 363 ? 4.03764   -27.28183 -8.92125  1.000 33.67058 ?  440 LEU   A CG  1 
ATOM   2817 C  CD1 . LEU   A 1 363 ? 2.77108   -27.43235 -9.72587  1.000 31.56920 ?  440 LEU   A CD1 1 
ATOM   2818 C  CD2 . LEU   A 1 363 ? 4.96635   -26.27280 -9.56322  1.000 28.53104 ?  440 LEU   A CD2 1 
ATOM   2819 N  N   . PRO   A 1 364 ? 4.48076   -25.36983 -4.81799  1.000 33.47285 ?  441 PRO   A N   1 
ATOM   2820 C  CA  . PRO   A 1 364 ? 4.07409   -24.96202 -3.46924  1.000 32.60787 ?  441 PRO   A CA  1 
ATOM   2821 C  C   . PRO   A 1 364 ? 2.57507   -25.11325 -3.24896  1.000 32.91087 ?  441 PRO   A C   1 
ATOM   2822 O  O   . PRO   A 1 364 ? 1.78103   -25.12094 -4.18589  1.000 35.11103 ?  441 PRO   A O   1 
ATOM   2823 C  CB  . PRO   A 1 364 ? 4.48590   -23.48944 -3.42468  1.000 33.81383 ?  441 PRO   A CB  1 
ATOM   2824 C  CG  . PRO   A 1 364 ? 4.38860   -23.05721 -4.84340  1.000 32.82266 ?  441 PRO   A CG  1 
ATOM   2825 C  CD  . PRO   A 1 364 ? 4.87009   -24.21913 -5.64553  1.000 32.25726 ?  441 PRO   A CD  1 
ATOM   2826 N  N   . HIS   A 1 365 ? 2.18886   -25.21305 -1.97223  1.000 34.46495 ?  442 HIS   A N   1 
ATOM   2827 C  CA  . HIS   A 1 365 ? 0.76319   -25.21884 -1.64393  1.000 34.81019 ?  442 HIS   A CA  1 
ATOM   2828 C  C   . HIS   A 1 365 ? 0.07791   -23.94738 -2.13367  1.000 34.83415 ?  442 HIS   A C   1 
ATOM   2829 O  O   . HIS   A 1 365 ? -1.03771  -24.00377 -2.66210  1.000 33.27991 ?  442 HIS   A O   1 
ATOM   2830 C  CB  . HIS   A 1 365 ? 0.54997   -25.37023 -0.13747  1.000 36.74985 ?  442 HIS   A CB  1 
ATOM   2831 C  CG  . HIS   A 1 365 ? 1.16225   -26.60697 0.44579   1.000 38.15992 ?  442 HIS   A CG  1 
ATOM   2832 N  ND1 . HIS   A 1 365 ? 0.56585   -27.84726 0.35737   1.000 41.10744 ?  442 HIS   A ND1 1 
ATOM   2833 C  CD2 . HIS   A 1 365 ? 2.31453   -26.79155 1.13046   1.000 36.65935 ?  442 HIS   A CD2 1 
ATOM   2834 C  CE1 . HIS   A 1 365 ? 1.33316   -28.74532 0.94802   1.000 42.16153 ?  442 HIS   A CE1 1 
ATOM   2835 N  NE2 . HIS   A 1 365 ? 2.39926   -28.13089 1.42721   1.000 42.92097 ?  442 HIS   A NE2 1 
ATOM   2836 N  N   . GLY   A 1 366 ? 0.73356   -22.79238 -1.96180  1.000 34.42509 ?  443 GLY   A N   1 
ATOM   2837 C  CA  . GLY   A 1 366 ? 0.21633   -21.48067 -2.33938  1.000 30.90326 ?  443 GLY   A CA  1 
ATOM   2838 C  C   . GLY   A 1 366 ? -0.21828  -21.36096 -3.78543  1.000 30.10566 ?  443 GLY   A C   1 
ATOM   2839 O  O   . GLY   A 1 366 ? -0.93710  -20.41297 -4.12675  1.000 30.04361 ?  443 GLY   A O   1 
ATOM   2840 N  N   . LEU   A 1 367 ? 0.19925   -22.28936 -4.64336  1.000 33.23624 ?  444 LEU   A N   1 
ATOM   2841 C  CA  . LEU   A 1 367 ? -0.25783  -22.24661 -6.01999  1.000 31.03220 ?  444 LEU   A CA  1 
ATOM   2842 C  C   . LEU   A 1 367 ? -1.77943  -22.26107 -6.09247  1.000 30.67408 ?  444 LEU   A C   1 
ATOM   2843 O  O   . LEU   A 1 367 ? -2.36152  -21.65845 -6.99596  1.000 32.87069 ?  444 LEU   A O   1 
ATOM   2844 C  CB  . LEU   A 1 367 ? 0.35909   -23.41037 -6.79495  1.000 31.99045 ?  444 LEU   A CB  1 
ATOM   2845 C  CG  . LEU   A 1 367 ? -0.02885  -23.49598 -8.27345  1.000 37.77613 ?  444 LEU   A CG  1 
ATOM   2846 C  CD1 . LEU   A 1 367 ? 0.51936   -22.29569 -9.04542  1.000 30.59158 ?  444 LEU   A CD1 1 
ATOM   2847 C  CD2 . LEU   A 1 367 ? 0.43364   -24.82973 -8.88192  1.000 30.75042 ?  444 LEU   A CD2 1 
ATOM   2848 N  N   . GLY   A 1 368 ? -2.44504  -22.90000 -5.13031  1.000 30.32213 ?  445 GLY   A N   1 
ATOM   2849 C  CA  . GLY   A 1 368 ? -3.89169  -23.01688 -5.18749  1.000 29.34782 ?  445 GLY   A CA  1 
ATOM   2850 C  C   . GLY   A 1 368 ? -4.65272  -21.72048 -4.96372  1.000 31.75017 ?  445 GLY   A C   1 
ATOM   2851 O  O   . GLY   A 1 368 ? -5.85876  -21.68381 -5.22749  1.000 32.42471 ?  445 GLY   A O   1 
ATOM   2852 N  N   . ASN   A 1 369 ? -3.99315  -20.66779 -4.48657  1.000 31.45459 ?  446 ASN   A N   1 
ATOM   2853 C  CA  . ASN   A 1 369 ? -4.66263  -19.39274 -4.26972  1.000 31.31357 ?  446 ASN   A CA  1 
ATOM   2854 C  C   . ASN   A 1 369 ? -4.81739  -18.55420 -5.54101  1.000 32.49507 ?  446 ASN   A C   1 
ATOM   2855 O  O   . ASN   A 1 369 ? -5.43091  -17.48269 -5.48146  1.000 33.87884 ?  446 ASN   A O   1 
ATOM   2856 C  CB  . ASN   A 1 369 ? -3.90283  -18.58208 -3.22148  1.000 31.71120 ?  446 ASN   A CB  1 
ATOM   2857 C  CG  . ASN   A 1 369 ? -4.74125  -17.47083 -2.63253  1.000 36.28694 ?  446 ASN   A CG  1 
ATOM   2858 O  OD1 . ASN   A 1 369 ? -5.91013  -17.68153 -2.32072  1.000 38.17417 ?  446 ASN   A OD1 1 
ATOM   2859 N  ND2 . ASN   A 1 369 ? -4.15441  -16.26918 -2.48556  1.000 33.98499 ?  446 ASN   A ND2 1 
ATOM   2860 N  N   . LEU   A 1 370 ? -4.27849  -18.99242 -6.68015  1.000 30.31930 ?  447 LEU   A N   1 
ATOM   2861 C  CA  . LEU   A 1 370 ? -4.32193  -18.19524 -7.90677  1.000 30.13404 ?  447 LEU   A CA  1 
ATOM   2862 C  C   . LEU   A 1 370 ? -5.66178  -18.45155 -8.58459  1.000 31.75870 ?  447 LEU   A C   1 
ATOM   2863 O  O   . LEU   A 1 370 ? -5.78410  -19.19453 -9.56155  1.000 34.16330 ?  447 LEU   A O   1 
ATOM   2864 C  CB  . LEU   A 1 370 ? -3.15316  -18.53855 -8.81282  1.000 27.94158 ?  447 LEU   A CB  1 
ATOM   2865 C  CG  . LEU   A 1 370 ? -1.78816  -18.26441 -8.18008  1.000 30.43371 ?  447 LEU   A CG  1 
ATOM   2866 C  CD1 . LEU   A 1 370 ? -0.67406  -18.20250 -9.23762  1.000 32.13022 ?  447 LEU   A CD1 1 
ATOM   2867 C  CD2 . LEU   A 1 370 ? -1.83970  -16.97839 -7.39555  1.000 30.31398 ?  447 LEU   A CD2 1 
ATOM   2868 N  N   . ARG   A 1 371 ? -6.68662  -17.81772 -8.03750  1.000 28.68150 ?  448 ARG   A N   1 
ATOM   2869 C  CA  . ARG   A 1 371 ? -8.06181  -18.13722 -8.38275  1.000 30.67803 ?  448 ARG   A CA  1 
ATOM   2870 C  C   . ARG   A 1 371 ? -8.42908  -17.67670 -9.79249  1.000 34.39941 ?  448 ARG   A C   1 
ATOM   2871 O  O   . ARG   A 1 371 ? -9.44564  -18.13074 -10.33131 1.000 33.52244 ?  448 ARG   A O   1 
ATOM   2872 C  CB  . ARG   A 1 371 ? -8.97049  -17.51399 -7.30673  1.000 30.58803 ?  448 ARG   A CB  1 
ATOM   2873 C  CG  . ARG   A 1 371 ? -10.45905 -17.84763 -7.34733  1.000 38.48573 ?  448 ARG   A CG  1 
ATOM   2874 C  CD  . ARG   A 1 371 ? -10.77910 -19.26148 -7.83607  1.000 41.89356 ?  448 ARG   A CD  1 
ATOM   2875 N  NE  . ARG   A 1 371 ? -11.40330 -19.24623 -9.16401  1.000 44.50123 ?  448 ARG   A NE  1 
ATOM   2876 C  CZ  . ARG   A 1 371 ? -12.71152 -19.28722 -9.41179  1.000 41.82164 ?  448 ARG   A CZ  1 
ATOM   2877 N  NH1 . ARG   A 1 371 ? -13.60407 -19.41804 -8.44292  1.000 37.14407 ?  448 ARG   A NH1 1 
ATOM   2878 N  NH2 . ARG   A 1 371 ? -13.13436 -19.19003 -10.66927 1.000 43.80765 ?  448 ARG   A NH2 1 
ATOM   2879 N  N   . LYS   A 1 372 ? -7.62953  -16.79333 -10.40123 1.000 30.40642 ?  449 LYS   A N   1 
ATOM   2880 C  CA  . LYS   A 1 372 ? -7.86951  -16.30072 -11.75312 1.000 30.07845 ?  449 LYS   A CA  1 
ATOM   2881 C  C   . LYS   A 1 372 ? -7.00327  -16.99872 -12.79396 1.000 30.08169 ?  449 LYS   A C   1 
ATOM   2882 O  O   . LYS   A 1 372 ? -7.11536  -16.68810 -13.98579 1.000 28.24633 ?  449 LYS   A O   1 
ATOM   2883 C  CB  . LYS   A 1 372 ? -7.60355  -14.78841 -11.83189 1.000 30.46434 ?  449 LYS   A CB  1 
ATOM   2884 C  CG  . LYS   A 1 372 ? -8.48114  -13.90645 -10.97534 1.000 36.51899 ?  449 LYS   A CG  1 
ATOM   2885 C  CD  . LYS   A 1 372 ? -9.72388  -13.43691 -11.73028 1.000 42.17923 ?  449 LYS   A CD  1 
ATOM   2886 C  CE  . LYS   A 1 372 ? -9.38474  -12.57465 -12.95467 1.000 41.18918 ?  449 LYS   A CE  1 
ATOM   2887 N  NZ  . LYS   A 1 372 ? -8.86702  -11.21895 -12.57304 1.000 44.74389 ?  449 LYS   A NZ  1 
ATOM   2888 N  N   . LEU   A 1 373 ? -6.11322  -17.89389 -12.37078 1.000 27.70913 ?  450 LEU   A N   1 
ATOM   2889 C  CA  . LEU   A 1 373 ? -5.19306  -18.54538 -13.29402 1.000 27.30357 ?  450 LEU   A CA  1 
ATOM   2890 C  C   . LEU   A 1 373 ? -5.95877  -19.32779 -14.36549 1.000 27.26690 ?  450 LEU   A C   1 
ATOM   2891 O  O   . LEU   A 1 373 ? -6.73396  -20.24228 -14.05187 1.000 23.91202 ?  450 LEU   A O   1 
ATOM   2892 C  CB  . LEU   A 1 373 ? -4.25605  -19.46326 -12.51449 1.000 26.48005 ?  450 LEU   A CB  1 
ATOM   2893 C  CG  . LEU   A 1 373 ? -2.99083  -19.94816 -13.20800 1.000 23.89632 ?  450 LEU   A CG  1 
ATOM   2894 C  CD1 . LEU   A 1 373 ? -2.13882  -18.77200 -13.69984 1.000 25.17764 ?  450 LEU   A CD1 1 
ATOM   2895 C  CD2 . LEU   A 1 373 ? -2.20731  -20.77038 -12.23763 1.000 25.16431 ?  450 LEU   A CD2 1 
ATOM   2896 N  N   . ARG   A 1 374 ? -5.73007  -18.96380 -15.63150 1.000 24.80552 ?  451 ARG   A N   1 
ATOM   2897 C  CA  . ARG   A 1 374 ? -6.34207  -19.62304 -16.77857 1.000 25.30499 ?  451 ARG   A CA  1 
ATOM   2898 C  C   . ARG   A 1 374 ? -5.38985  -20.57170 -17.49588 1.000 25.64476 ?  451 ARG   A C   1 
ATOM   2899 O  O   . ARG   A 1 374 ? -5.83229  -21.60560 -18.01030 1.000 27.48944 ?  451 ARG   A O   1 
ATOM   2900 C  CB  . ARG   A 1 374 ? -6.85422  -18.58652 -17.79429 1.000 27.01572 ?  451 ARG   A CB  1 
ATOM   2901 C  CG  . ARG   A 1 374 ? -7.95881  -17.64967 -17.30558 1.000 31.14370 ?  451 ARG   A CG  1 
ATOM   2902 C  CD  . ARG   A 1 374 ? -8.26915  -16.51934 -18.33325 1.000 33.90898 ?  451 ARG   A CD  1 
ATOM   2903 N  NE  . ARG   A 1 374 ? -8.92048  -17.01404 -19.54157 1.000 35.75703 ?  451 ARG   A NE  1 
ATOM   2904 C  CZ  . ARG   A 1 374 ? -9.38175  -16.25616 -20.53279 1.000 38.07712 ?  451 ARG   A CZ  1 
ATOM   2905 N  NH1 . ARG   A 1 374 ? -9.26506  -14.93970 -20.51338 1.000 37.95323 ?  451 ARG   A NH1 1 
ATOM   2906 N  NH2 . ARG   A 1 374 ? -9.98228  -16.83727 -21.57176 1.000 36.93576 ?  451 ARG   A NH2 1 
ATOM   2907 N  N   . GLU   A 1 375 ? -4.09664  -20.25314 -17.53954 1.000 25.47356 ?  452 GLU   A N   1 
ATOM   2908 C  CA  . GLU   A 1 375 ? -3.09953  -21.02935 -18.27313 1.000 26.95280 ?  452 GLU   A CA  1 
ATOM   2909 C  C   . GLU   A 1 375 ? -1.92279  -21.34740 -17.35834 1.000 23.10453 ?  452 GLU   A C   1 
ATOM   2910 O  O   . GLU   A 1 375 ? -1.32434  -20.43895 -16.78338 1.000 26.24891 ?  452 GLU   A O   1 
ATOM   2911 C  CB  . GLU   A 1 375 ? -2.62417  -20.24718 -19.50737 1.000 25.62192 ?  452 GLU   A CB  1 
ATOM   2912 C  CG  . GLU   A 1 375 ? -1.63389  -20.97139 -20.41348 1.000 33.91683 ?  452 GLU   A CG  1 
ATOM   2913 C  CD  . GLU   A 1 375 ? -1.16347  -20.11333 -21.61359 1.000 40.21467 ?  452 GLU   A CD  1 
ATOM   2914 O  OE1 . GLU   A 1 375 ? -1.97051  -19.31467 -22.15184 1.000 40.05861 ?  452 GLU   A OE1 1 
ATOM   2915 O  OE2 . GLU   A 1 375 ? 0.02025   -20.24900 -22.02565 1.000 44.28473 ?  452 GLU   A OE2 1 
ATOM   2916 N  N   . LEU   A 1 376 ? -1.57325  -22.62161 -17.22765 1.000 24.56341 ?  453 LEU   A N   1 
ATOM   2917 C  CA  . LEU   A 1 376 ? -0.43419  -23.02179 -16.39760 1.000 25.93790 ?  453 LEU   A CA  1 
ATOM   2918 C  C   . LEU   A 1 376 ? 0.48441   -23.93072 -17.20241 1.000 25.34768 ?  453 LEU   A C   1 
ATOM   2919 O  O   . LEU   A 1 376 ? 0.12458   -25.07637 -17.49670 1.000 26.96168 ?  453 LEU   A O   1 
ATOM   2920 C  CB  . LEU   A 1 376 ? -0.91335  -23.71523 -15.12055 1.000 23.77809 ?  453 LEU   A CB  1 
ATOM   2921 C  CG  . LEU   A 1 376 ? 0.10085   -24.26747 -14.12230 1.000 22.74744 ?  453 LEU   A CG  1 
ATOM   2922 C  CD1 . LEU   A 1 376 ? 1.13321   -23.22570 -13.70937 1.000 22.81431 ?  453 LEU   A CD1 1 
ATOM   2923 C  CD2 . LEU   A 1 376 ? -0.65417  -24.77582 -12.91072 1.000 23.08875 ?  453 LEU   A CD2 1 
ATOM   2924 N  N   . ASP   A 1 377 ? 1.67592   -23.43969 -17.54862 1.000 27.66149 ?  454 ASP   A N   1 
ATOM   2925 C  CA  . ASP   A 1 377 ? 2.60581   -24.17868 -18.40719 1.000 26.01989 ?  454 ASP   A CA  1 
ATOM   2926 C  C   . ASP   A 1 377 ? 3.77720   -24.66133 -17.56456 1.000 28.44253 ?  454 ASP   A C   1 
ATOM   2927 O  O   . ASP   A 1 377 ? 4.63423   -23.86407 -17.17235 1.000 29.36085 ?  454 ASP   A O   1 
ATOM   2928 C  CB  . ASP   A 1 377 ? 3.08922   -23.32295 -19.58071 1.000 26.61897 ?  454 ASP   A CB  1 
ATOM   2929 C  CG  . ASP   A 1 377 ? 3.84267   -24.14742 -20.66318 1.000 40.40694 ?  454 ASP   A CG  1 
ATOM   2930 O  OD1 . ASP   A 1 377 ? 3.94017   -25.40271 -20.51680 1.000 37.70897 ?  454 ASP   A OD1 1 
ATOM   2931 O  OD2 . ASP   A 1 377 ? 4.34030   -23.53834 -21.66197 1.000 41.83189 ?  454 ASP   A OD2 1 
ATOM   2932 N  N   . LEU   A 1 378 ? 3.82634   -25.97793 -17.31604 1.000 30.89733 ?  455 LEU   A N   1 
ATOM   2933 C  CA  . LEU   A 1 378 ? 4.83810   -26.59669 -16.46923 1.000 26.15235 ?  455 LEU   A CA  1 
ATOM   2934 C  C   . LEU   A 1 378 ? 5.63211   -27.65344 -17.22029 1.000 26.96382 ?  455 LEU   A C   1 
ATOM   2935 O  O   . LEU   A 1 378 ? 6.18970   -28.56224 -16.60159 1.000 26.21175 ?  455 LEU   A O   1 
ATOM   2936 C  CB  . LEU   A 1 378 ? 4.18804   -27.20902 -15.22404 1.000 28.31091 ?  455 LEU   A CB  1 
ATOM   2937 C  CG  . LEU   A 1 378 ? 3.73845   -26.22488 -14.13413 1.000 27.32382 ?  455 LEU   A CG  1 
ATOM   2938 C  CD1 . LEU   A 1 378 ? 2.64686   -26.79449 -13.24384 1.000 22.94743 ?  455 LEU   A CD1 1 
ATOM   2939 C  CD2 . LEU   A 1 378 ? 4.93271   -25.82481 -13.30030 1.000 26.49955 ?  455 LEU   A CD2 1 
ATOM   2940 N  N   . GLU   A 1 379 ? 5.70063   -27.55683 -18.53869 1.000 28.78527 ?  456 GLU   A N   1 
ATOM   2941 C  CA  . GLU   A 1 379 ? 6.34407   -28.61175 -19.30612 1.000 29.78604 ?  456 GLU   A CA  1 
ATOM   2942 C  C   . GLU   A 1 379 ? 7.84680   -28.61446 -19.06097 1.000 27.34789 ?  456 GLU   A C   1 
ATOM   2943 O  O   . GLU   A 1 379 ? 8.44555   -27.58961 -18.74559 1.000 30.11641 ?  456 GLU   A O   1 
ATOM   2944 C  CB  . GLU   A 1 379 ? 6.03565   -28.44621 -20.79909 1.000 29.25776 ?  456 GLU   A CB  1 
ATOM   2945 C  CG  . GLU   A 1 379 ? 6.76972   -27.31507 -21.48938 1.000 31.52849 ?  456 GLU   A CG  1 
ATOM   2946 C  CD  . GLU   A 1 379 ? 6.11472   -26.87287 -22.81318 1.000 39.64997 ?  456 GLU   A CD  1 
ATOM   2947 O  OE1 . GLU   A 1 379 ? 5.06078   -26.18754 -22.77896 1.000 44.85237 ?  456 GLU   A OE1 1 
ATOM   2948 O  OE2 . GLU   A 1 379 ? 6.65726   -27.19484 -23.89685 1.000 41.80296 ?  456 GLU   A OE2 1 
ATOM   2949 N  N   . GLU   A 1 380 ? 8.45587   -29.79413 -19.20111 1.000 29.05940 ?  457 GLU   A N   1 
ATOM   2950 C  CA  . GLU   A 1 380 ? 9.91094   -29.96395 -19.17298 1.000 28.12549 ?  457 GLU   A CA  1 
ATOM   2951 C  C   . GLU   A 1 380 ? 10.51153  -29.62353 -17.81283 1.000 31.72423 ?  457 GLU   A C   1 
ATOM   2952 O  O   . GLU   A 1 380 ? 11.62809  -29.09251 -17.73024 1.000 32.47012 ?  457 GLU   A O   1 
ATOM   2953 C  CB  . GLU   A 1 380 ? 10.60668  -29.13797 -20.25994 1.000 28.09712 ?  457 GLU   A CB  1 
ATOM   2954 C  CG  . GLU   A 1 380 ? 10.10785  -29.37431 -21.67255 1.000 28.14957 ?  457 GLU   A CG  1 
ATOM   2955 C  CD  . GLU   A 1 380 ? 10.25841  -30.81193 -22.12708 1.000 35.64298 ?  457 GLU   A CD  1 
ATOM   2956 O  OE1 . GLU   A 1 380 ? 11.14171  -31.54030 -21.59311 1.000 35.05896 ?  457 GLU   A OE1 1 
ATOM   2957 O  OE2 . GLU   A 1 380 ? 9.47788   -31.21396 -23.02820 1.000 36.56797 ?  457 GLU   A OE2 1 
ATOM   2958 N  N   . ASN   A 1 381 ? 9.78730   -29.90862 -16.74267 1.000 28.54240 ?  458 ASN   A N   1 
ATOM   2959 C  CA  . ASN   A 1 381 ? 10.36370  -29.85205 -15.42047 1.000 28.08098 ?  458 ASN   A CA  1 
ATOM   2960 C  C   . ASN   A 1 381 ? 10.64216  -31.28478 -14.95763 1.000 31.46183 ?  458 ASN   A C   1 
ATOM   2961 O  O   . ASN   A 1 381 ? 10.83106  -32.18773 -15.78227 1.000 33.62159 ?  458 ASN   A O   1 
ATOM   2962 C  CB  . ASN   A 1 381 ? 9.43516   -29.06608 -14.48965 1.000 27.71174 ?  458 ASN   A CB  1 
ATOM   2963 C  CG  . ASN   A 1 381 ? 9.57015   -27.56460 -14.67271 1.000 29.37126 ?  458 ASN   A CG  1 
ATOM   2964 O  OD1 . ASN   A 1 381 ? 10.44010  -26.93220 -14.07230 1.000 26.71943 ?  458 ASN   A OD1 1 
ATOM   2965 N  ND2 . ASN   A 1 381 ? 8.71912   -26.99088 -15.51573 1.000 26.84431 ?  458 ASN   A ND2 1 
ATOM   2966 N  N   . LYS   A 1 382 ? 10.70324  -31.49349 -13.64452 1.000 27.43801 ?  459 LYS   A N   1 
ATOM   2967 C  CA  . LYS   A 1 382 ? 10.91000  -32.80182 -13.04912 1.000 29.44575 ?  459 LYS   A CA  1 
ATOM   2968 C  C   . LYS   A 1 382 ? 9.79198   -33.12406 -12.06681 1.000 29.08222 ?  459 LYS   A C   1 
ATOM   2969 O  O   . LYS   A 1 382 ? 9.99593   -33.86746 -11.11521 1.000 29.70827 ?  459 LYS   A O   1 
ATOM   2970 C  CB  . LYS   A 1 382 ? 12.26645  -32.86361 -12.34887 1.000 33.47643 ?  459 LYS   A CB  1 
ATOM   2971 C  CG  . LYS   A 1 382 ? 13.41464  -32.27566 -13.13881 1.000 35.29553 ?  459 LYS   A CG  1 
ATOM   2972 C  CD  . LYS   A 1 382 ? 14.44935  -31.63267 -12.19890 1.000 39.37251 ?  459 LYS   A CD  1 
ATOM   2973 C  CE  . LYS   A 1 382 ? 15.71049  -32.48010 -12.04328 1.000 45.10262 ?  459 LYS   A CE  1 
ATOM   2974 N  NZ  . LYS   A 1 382 ? 16.52902  -32.49113 -13.30625 1.000 49.30526 ?  459 LYS   A NZ  1 
ATOM   2975 N  N   . LEU   A 1 383 ? 8.61536   -32.53901 -12.26288 1.000 27.44709 ?  460 LEU   A N   1 
ATOM   2976 C  CA  . LEU   A 1 383 ? 7.52865   -32.72633 -11.31249 1.000 28.23037 ?  460 LEU   A CA  1 
ATOM   2977 C  C   . LEU   A 1 383 ? 7.29959   -34.20196 -11.04400 1.000 29.18789 ?  460 LEU   A C   1 
ATOM   2978 O  O   . LEU   A 1 383 ? 7.18302   -35.00673 -11.97204 1.000 29.57901 ?  460 LEU   A O   1 
ATOM   2979 C  CB  . LEU   A 1 383 ? 6.24203   -32.08722 -11.83394 1.000 27.75536 ?  460 LEU   A CB  1 
ATOM   2980 C  CG  . LEU   A 1 383 ? 6.33405   -30.56495 -11.83875 1.000 30.00386 ?  460 LEU   A CG  1 
ATOM   2981 C  CD1 . LEU   A 1 383 ? 5.11789   -29.93665 -12.49388 1.000 25.73479 ?  460 LEU   A CD1 1 
ATOM   2982 C  CD2 . LEU   A 1 383 ? 6.53584   -30.07227 -10.40868 1.000 26.19694 ?  460 LEU   A CD2 1 
ATOM   2983 N  N   . GLU   A 1 384 ? 7.23931   -34.54627 -9.76431  1.000 29.68363 ?  461 GLU   A N   1 
ATOM   2984 C  CA  . GLU   A 1 384 ? 6.93888   -35.89628 -9.31991  1.000 31.83759 ?  461 GLU   A CA  1 
ATOM   2985 C  C   . GLU   A 1 384 ? 5.54637   -36.01747 -8.72022  1.000 32.51860 ?  461 GLU   A C   1 
ATOM   2986 O  O   . GLU   A 1 384 ? 5.05678   -37.14315 -8.56003  1.000 31.60415 ?  461 GLU   A O   1 
ATOM   2987 C  CB  . GLU   A 1 384 ? 8.00263   -36.36203 -8.31202  1.000 28.99168 ?  461 GLU   A CB  1 
ATOM   2988 C  CG  . GLU   A 1 384 ? 9.38807   -36.49882 -8.96690  1.000 35.41961 ?  461 GLU   A CG  1 
ATOM   2989 C  CD  . GLU   A 1 384 ? 10.54952  -36.59567 -7.97523  1.000 49.45617 ?  461 GLU   A CD  1 
ATOM   2990 O  OE1 . GLU   A 1 384 ? 10.40177  -36.12915 -6.81960  1.000 47.67246 ?  461 GLU   A OE1 1 
ATOM   2991 O  OE2 . GLU   A 1 384 ? 11.61662  -37.13939 -8.36125  1.000 50.54688 ?  461 GLU   A OE2 1 
ATOM   2992 N  N   . SER   A 1 385 ? 4.88332   -34.89451 -8.43155  1.000 29.44178 ?  462 SER   A N   1 
ATOM   2993 C  CA  . SER   A 1 385 ? 3.50147   -34.90343 -7.97155  1.000 32.30234 ?  462 SER   A CA  1 
ATOM   2994 C  C   . SER   A 1 385 ? 2.93464   -33.49324 -8.07934  1.000 32.75866 ?  462 SER   A C   1 
ATOM   2995 O  O   . SER   A 1 385 ? 3.67585   -32.50775 -8.13655  1.000 33.56396 ?  462 SER   A O   1 
ATOM   2996 C  CB  . SER   A 1 385 ? 3.39871   -35.39654 -6.53510  1.000 29.63384 ?  462 SER   A CB  1 
ATOM   2997 O  OG  . SER   A 1 385 ? 3.93136   -34.40191 -5.68698  1.000 33.20711 ?  462 SER   A OG  1 
ATOM   2998 N  N   . LEU   A 1 386 ? 1.60994   -33.41070 -8.09909  1.000 32.01146 ?  463 LEU   A N   1 
ATOM   2999 C  CA  . LEU   A 1 386 ? 0.90654   -32.13794 -8.07934  1.000 32.13673 ?  463 LEU   A CA  1 
ATOM   3000 C  C   . LEU   A 1 386 ? 0.29738   -31.90475 -6.70736  1.000 32.42551 ?  463 LEU   A C   1 
ATOM   3001 O  O   . LEU   A 1 386 ? -0.34169  -32.80936 -6.16618  1.000 33.71110 ?  463 LEU   A O   1 
ATOM   3002 C  CB  . LEU   A 1 386 ? -0.18761  -32.12206 -9.13431  1.000 28.78444 ?  463 LEU   A CB  1 
ATOM   3003 C  CG  . LEU   A 1 386 ? 0.34598   -32.23549 -10.56147 1.000 33.34426 ?  463 LEU   A CG  1 
ATOM   3004 C  CD1 . LEU   A 1 386 ? -0.78027  -32.06890 -11.59498 1.000 25.15800 ?  463 LEU   A CD1 1 
ATOM   3005 C  CD2 . LEU   A 1 386 ? 1.47643   -31.22850 -10.77695 1.000 26.21675 ?  463 LEU   A CD2 1 
ATOM   3006 N  N   . PRO   A 1 387 ? 0.44361   -30.72863 -6.11396  1.000 34.28404 ?  464 PRO   A N   1 
ATOM   3007 C  CA  . PRO   A 1 387 ? -0.13978  -30.51548 -4.78282  1.000 33.80740 ?  464 PRO   A CA  1 
ATOM   3008 C  C   . PRO   A 1 387 ? -1.64231  -30.74788 -4.81671  1.000 32.07154 ?  464 PRO   A C   1 
ATOM   3009 O  O   . PRO   A 1 387 ? -2.28364  -30.61920 -5.85891  1.000 34.89907 ?  464 PRO   A O   1 
ATOM   3010 C  CB  . PRO   A 1 387 ? 0.19706   -29.04830 -4.47856  1.000 32.30984 ?  464 PRO   A CB  1 
ATOM   3011 C  CG  . PRO   A 1 387 ? 0.35122   -28.41438 -5.82435  1.000 31.17920 ?  464 PRO   A CG  1 
ATOM   3012 C  CD  . PRO   A 1 387 ? 0.93034   -29.47716 -6.72119  1.000 30.95664 ?  464 PRO   A CD  1 
ATOM   3013 N  N   . ASN   A 1 388 ? -2.21769  -31.08707 -3.66453  1.000 29.93141 ?  465 ASN   A N   1 
ATOM   3014 C  CA  . ASN   A 1 388 ? -3.66905  -31.21337 -3.64261  1.000 31.51228 ?  465 ASN   A CA  1 
ATOM   3015 C  C   . ASN   A 1 388 ? -4.36707  -29.86594 -3.79211  1.000 32.53419 ?  465 ASN   A C   1 
ATOM   3016 O  O   . ASN   A 1 388 ? -5.56583  -29.81477 -4.08600  1.000 32.28997 ?  465 ASN   A O   1 
ATOM   3017 C  CB  . ASN   A 1 388 ? -4.12693  -31.89082 -2.35637  1.000 32.15106 ?  465 ASN   A CB  1 
ATOM   3018 C  CG  . ASN   A 1 388 ? -3.79977  -33.37741 -2.32643  1.000 37.68992 ?  465 ASN   A CG  1 
ATOM   3019 O  OD1 . ASN   A 1 388 ? -4.08680  -34.11905 -3.27503  1.000 40.70837 ?  465 ASN   A OD1 1 
ATOM   3020 N  ND2 . ASN   A 1 388 ? -3.19382  -33.81811 -1.23556  1.000 33.64842 ?  465 ASN   A ND2 1 
ATOM   3021 N  N   . GLU   A 1 389 ? -3.65546  -28.76889 -3.59995  1.000 33.01242 ?  466 GLU   A N   1 
ATOM   3022 C  CA  . GLU   A 1 389 ? -4.32890  -27.48604 -3.65612  1.000 28.84854 ?  466 GLU   A CA  1 
ATOM   3023 C  C   . GLU   A 1 389 ? -4.69805  -27.08358 -5.07709  1.000 30.38364 ?  466 GLU   A C   1 
ATOM   3024 O  O   . GLU   A 1 389 ? -5.37487  -26.06666 -5.25293  1.000 31.42457 ?  466 GLU   A O   1 
ATOM   3025 C  CB  . GLU   A 1 389 ? -3.45051  -26.42710 -2.97792  1.000 28.78429 ?  466 GLU   A CB  1 
ATOM   3026 C  CG  . GLU   A 1 389 ? -3.36385  -26.56913 -1.43398  1.000 29.55133 ?  466 GLU   A CG  1 
ATOM   3027 C  CD  . GLU   A 1 389 ? -2.33453  -27.61810 -0.94790  1.000 37.22530 ?  466 GLU   A CD  1 
ATOM   3028 O  OE1 . GLU   A 1 389 ? -1.71120  -28.32532 -1.78570  1.000 35.77239 ?  466 GLU   A OE1 1 
ATOM   3029 O  OE2 . GLU   A 1 389 ? -2.14846  -27.73867 0.29096   1.000 36.28172 ?  466 GLU   A OE2 1 
ATOM   3030 N  N   . ILE   A 1 390 ? -4.29394  -27.84579 -6.09910  1.000 30.25456 ?  467 ILE   A N   1 
ATOM   3031 C  CA  . ILE   A 1 390 ? -4.67642  -27.45210 -7.44880  1.000 31.82732 ?  467 ILE   A CA  1 
ATOM   3032 C  C   . ILE   A 1 390 ? -6.18230  -27.51008 -7.62625  1.000 30.04780 ?  467 ILE   A C   1 
ATOM   3033 O  O   . ILE   A 1 390 ? -6.71360  -26.92686 -8.57474  1.000 31.83814 ?  467 ILE   A O   1 
ATOM   3034 C  CB  . ILE   A 1 390 ? -4.00030  -28.31354 -8.53077  1.000 33.58087 ?  467 ILE   A CB  1 
ATOM   3035 C  CG1 . ILE   A 1 390 ? -4.62626  -29.70393 -8.54534  1.000 31.31751 ?  467 ILE   A CG1 1 
ATOM   3036 C  CG2 . ILE   A 1 390 ? -2.50939  -28.39297 -8.30292  1.000 35.26650 ?  467 ILE   A CG2 1 
ATOM   3037 C  CD1 . ILE   A 1 390 ? -4.54606  -30.35094 -9.88900  1.000 34.50304 ?  467 ILE   A CD1 1 
ATOM   3038 N  N   . ALA   A 1 391 ? -6.89413  -28.20211 -6.73814  1.000 28.03410 ?  468 ALA   A N   1 
ATOM   3039 C  CA  . ALA   A 1 391 ? -8.35497  -28.21600 -6.82755  1.000 32.72041 ?  468 ALA   A CA  1 
ATOM   3040 C  C   . ALA   A 1 391 ? -8.96256  -26.81520 -6.80792  1.000 30.52150 ?  468 ALA   A C   1 
ATOM   3041 O  O   . ALA   A 1 391 ? -10.10634 -26.65110 -7.23899  1.000 30.09583 ?  468 ALA   A O   1 
ATOM   3042 C  CB  . ALA   A 1 391 ? -8.96351  -29.03767 -5.69129  1.000 30.22879 ?  468 ALA   A CB  1 
ATOM   3043 N  N   . TYR   A 1 392 ? -8.23489  -25.80654 -6.32437  1.000 30.48192 ?  469 TYR   A N   1 
ATOM   3044 C  CA  . TYR   A 1 392 ? -8.77890  -24.45745 -6.19115  1.000 31.38994 ?  469 TYR   A CA  1 
ATOM   3045 C  C   . TYR   A 1 392 ? -8.44907  -23.55964 -7.38069  1.000 29.92387 ?  469 TYR   A C   1 
ATOM   3046 O  O   . TYR   A 1 392 ? -8.80698  -22.38650 -7.36775  1.000 25.47422 ?  469 TYR   A O   1 
ATOM   3047 C  CB  . TYR   A 1 392 ? -8.31250  -23.83885 -4.87181  1.000 30.77733 ?  469 TYR   A CB  1 
ATOM   3048 C  CG  . TYR   A 1 392 ? -9.14714  -24.36568 -3.71968  1.000 32.06914 ?  469 TYR   A CG  1 
ATOM   3049 C  CD1 . TYR   A 1 392 ? -8.94172  -25.64512 -3.21603  1.000 28.65805 ?  469 TYR   A CD1 1 
ATOM   3050 C  CD2 . TYR   A 1 392 ? -10.18755 -23.60419 -3.17787  1.000 30.45809 ?  469 TYR   A CD2 1 
ATOM   3051 C  CE1 . TYR   A 1 392 ? -9.73918  -26.14767 -2.19023  1.000 27.37324 ?  469 TYR   A CE1 1 
ATOM   3052 C  CE2 . TYR   A 1 392 ? -10.97821 -24.09232 -2.15190  1.000 27.13940 ?  469 TYR   A CE2 1 
ATOM   3053 C  CZ  . TYR   A 1 392 ? -10.74787 -25.36847 -1.66343  1.000 33.45377 ?  469 TYR   A CZ  1 
ATOM   3054 O  OH  . TYR   A 1 392 ? -11.53668 -25.87059 -0.64767  1.000 35.67843 ?  469 TYR   A OH  1 
ATOM   3055 N  N   . LEU   A 1 393 ? -7.81303  -24.09718 -8.42932  1.000 31.85301 ?  470 LEU   A N   1 
ATOM   3056 C  CA  . LEU   A 1 393 ? -7.59764  -23.34949 -9.66747  1.000 28.42932 ?  470 LEU   A CA  1 
ATOM   3057 C  C   . LEU   A 1 393 ? -8.86168  -23.38203 -10.53561 1.000 29.28463 ?  470 LEU   A C   1 
ATOM   3058 O  O   . LEU   A 1 393 ? -8.90229  -23.91071 -11.64272 1.000 30.65484 ?  470 LEU   A O   1 
ATOM   3059 C  CB  . LEU   A 1 393 ? -6.38550  -23.89817 -10.39928 1.000 25.36560 ?  470 LEU   A CB  1 
ATOM   3060 C  CG  . LEU   A 1 393 ? -5.10054  -23.86078 -9.56728  1.000 28.08561 ?  470 LEU   A CG  1 
ATOM   3061 C  CD1 . LEU   A 1 393 ? -3.99264  -24.56450 -10.30317 1.000 26.58342 ?  470 LEU   A CD1 1 
ATOM   3062 C  CD2 . LEU   A 1 393 ? -4.66935  -22.43094 -9.22956  1.000 30.38017 ?  470 LEU   A CD2 1 
ATOM   3063 N  N   . LYS   A 1 394 ? -9.91821  -22.77354 -10.01083 1.000 29.91360 ?  471 LYS   A N   1 
ATOM   3064 C  CA  . LYS   A 1 394 ? -11.23412 -22.94926 -10.61230 1.000 31.00924 ?  471 LYS   A CA  1 
ATOM   3065 C  C   . LYS   A 1 394 ? -11.32283 -22.35316 -12.01314 1.000 34.33720 ?  471 LYS   A C   1 
ATOM   3066 O  O   . LYS   A 1 394 ? -12.17273 -22.77780 -12.80367 1.000 35.77334 ?  471 LYS   A O   1 
ATOM   3067 C  CB  . LYS   A 1 394 ? -12.30559 -22.33612 -9.69438  1.000 36.67325 ?  471 LYS   A CB  1 
ATOM   3068 C  CG  . LYS   A 1 394 ? -13.43933 -23.30287 -9.27821  1.000 47.08002 ?  471 LYS   A CG  1 
ATOM   3069 C  CD  . LYS   A 1 394 ? -12.91250 -24.60035 -8.60741  1.000 42.98747 ?  471 LYS   A CD  1 
ATOM   3070 C  CE  . LYS   A 1 394 ? -14.05714 -25.58009 -8.31280  1.000 39.36299 ?  471 LYS   A CE  1 
ATOM   3071 N  NZ  . LYS   A 1 394 ? -14.73878 -26.07626 -9.54410  1.000 31.34197 ?  471 LYS   A NZ  1 
ATOM   3072 N  N   . ASP   A 1 395 ? -10.48108 -21.38150 -12.34526 1.000 31.31144 ?  472 ASP   A N   1 
ATOM   3073 C  CA  . ASP   A 1 395 ? -10.50495 -20.79834 -13.67539 1.000 32.48885 ?  472 ASP   A CA  1 
ATOM   3074 C  C   . ASP   A 1 395 ? -9.56755  -21.49570 -14.64346 1.000 32.14366 ?  472 ASP   A C   1 
ATOM   3075 O  O   . ASP   A 1 395 ? -9.39530  -21.00868 -15.76528 1.000 33.96484 ?  472 ASP   A O   1 
ATOM   3076 C  CB  . ASP   A 1 395 ? -10.15087 -19.30467 -13.62070 1.000 33.56252 ?  472 ASP   A CB  1 
ATOM   3077 C  CG  . ASP   A 1 395 ? -11.35905 -18.42475 -13.30490 1.000 38.20797 ?  472 ASP   A CG  1 
ATOM   3078 O  OD1 . ASP   A 1 395 ? -12.47171 -18.98965 -13.15260 1.000 38.92450 ?  472 ASP   A OD1 1 
ATOM   3079 O  OD2 . ASP   A 1 395 ? -11.19645 -17.17728 -13.21637 1.000 38.74351 ?  472 ASP   A OD2 1 
ATOM   3080 N  N   . LEU   A 1 396 ? -8.94818  -22.60268 -14.24794 1.000 25.74395 ?  473 LEU   A N   1 
ATOM   3081 C  CA  . LEU   A 1 396 ? -7.88149  -23.14697 -15.06981 1.000 26.95870 ?  473 LEU   A CA  1 
ATOM   3082 C  C   . LEU   A 1 396 ? -8.45942  -23.75114 -16.34414 1.000 28.70544 ?  473 LEU   A C   1 
ATOM   3083 O  O   . LEU   A 1 396 ? -9.37604  -24.57694 -16.30575 1.000 25.56696 ?  473 LEU   A O   1 
ATOM   3084 C  CB  . LEU   A 1 396 ? -7.07281  -24.17996 -14.29882 1.000 25.84897 ?  473 LEU   A CB  1 
ATOM   3085 C  CG  . LEU   A 1 396 ? -5.71829  -24.48171 -14.95078 1.000 28.71851 ?  473 LEU   A CG  1 
ATOM   3086 C  CD1 . LEU   A 1 396 ? -4.80127  -23.24572 -14.95405 1.000 24.77832 ?  473 LEU   A CD1 1 
ATOM   3087 C  CD2 . LEU   A 1 396 ? -5.04234  -25.63732 -14.25525 1.000 24.15386 ?  473 LEU   A CD2 1 
ATOM   3088 N  N   . GLN   A 1 397 ? -7.92575  -23.32980 -17.48133 1.000 27.94019 ?  474 GLN   A N   1 
ATOM   3089 C  CA  . GLN   A 1 397 ? -8.40801  -23.81619 -18.76100 1.000 28.71406 ?  474 GLN   A CA  1 
ATOM   3090 C  C   . GLN   A 1 397 ? -7.38943  -24.63507 -19.52917 1.000 26.48470 ?  474 GLN   A C   1 
ATOM   3091 O  O   . GLN   A 1 397 ? -7.77737  -25.49300 -20.31192 1.000 27.91238 ?  474 GLN   A O   1 
ATOM   3092 C  CB  . GLN   A 1 397 ? -8.85809  -22.63819 -19.61665 1.000 26.88445 ?  474 GLN   A CB  1 
ATOM   3093 C  CG  . GLN   A 1 397 ? -9.91141  -21.84681 -18.88842 1.000 31.29141 ?  474 GLN   A CG  1 
ATOM   3094 C  CD  . GLN   A 1 397 ? -10.44382 -20.71105 -19.71446 1.000 33.81192 ?  474 GLN   A CD  1 
ATOM   3095 O  OE1 . GLN   A 1 397 ? -9.68627  -19.97588 -20.34087 1.000 29.25670 ?  474 GLN   A OE1 1 
ATOM   3096 N  NE2 . GLN   A 1 397 ? -11.76492 -20.55823 -19.71657 1.000 42.47296 ?  474 GLN   A NE2 1 
ATOM   3097 N  N   . LYS   A 1 398 ? -6.10555  -24.39336 -19.32178 1.000 27.72990 ?  475 LYS   A N   1 
ATOM   3098 C  CA  . LYS   A 1 398 ? -5.04132  -25.10697 -20.00673 1.000 29.10930 ?  475 LYS   A CA  1 
ATOM   3099 C  C   . LYS   A 1 398 ? -3.99872  -25.47135 -18.96716 1.000 26.77590 ?  475 LYS   A C   1 
ATOM   3100 O  O   . LYS   A 1 398 ? -3.56722  -24.60771 -18.19690 1.000 29.68683 ?  475 LYS   A O   1 
ATOM   3101 C  CB  . LYS   A 1 398 ? -4.42157  -24.25119 -21.12260 1.000 26.66531 ?  475 LYS   A CB  1 
ATOM   3102 C  CG  . LYS   A 1 398 ? -3.35954  -24.98529 -21.94007 1.000 31.03801 ?  475 LYS   A CG  1 
ATOM   3103 C  CD  . LYS   A 1 398 ? -2.59964  -24.03908 -22.88625 1.000 30.79400 ?  475 LYS   A CD  1 
ATOM   3104 C  CE  . LYS   A 1 398 ? -1.99656  -24.82808 -24.03332 1.000 34.85696 ?  475 LYS   A CE  1 
ATOM   3105 N  NZ  . LYS   A 1 398 ? -0.94266  -24.08762 -24.75513 1.000 41.18176 ?  475 LYS   A NZ  1 
ATOM   3106 N  N   . LEU   A 1 399 ? -3.62024  -26.74735 -18.92627 1.000 28.60825 ?  476 LEU   A N   1 
ATOM   3107 C  CA  . LEU   A 1 399 ? -2.63219  -27.25927 -17.98103 1.000 25.34898 ?  476 LEU   A CA  1 
ATOM   3108 C  C   . LEU   A 1 399 ? -1.67867  -28.15869 -18.74867 1.000 26.54743 ?  476 LEU   A C   1 
ATOM   3109 O  O   . LEU   A 1 399 ? -2.09198  -29.18941 -19.27906 1.000 28.48979 ?  476 LEU   A O   1 
ATOM   3110 C  CB  . LEU   A 1 399 ? -3.30952  -28.02469 -16.84570 1.000 24.67582 ?  476 LEU   A CB  1 
ATOM   3111 C  CG  . LEU   A 1 399 ? -2.42672  -28.66835 -15.76548 1.000 28.15359 ?  476 LEU   A CG  1 
ATOM   3112 C  CD1 . LEU   A 1 399 ? -1.51177  -27.64875 -15.09051 1.000 23.64486 ?  476 LEU   A CD1 1 
ATOM   3113 C  CD2 . LEU   A 1 399 ? -3.29054  -29.42148 -14.72327 1.000 24.73332 ?  476 LEU   A CD2 1 
ATOM   3114 N  N   . VAL   A 1 400 ? -0.41386  -27.76890 -18.82449 1.000 27.28235 ?  477 VAL   A N   1 
ATOM   3115 C  CA  . VAL   A 1 400 ? 0.56655   -28.44376 -19.66777 1.000 27.89873 ?  477 VAL   A CA  1 
ATOM   3116 C  C   . VAL   A 1 400 ? 1.62398   -29.05990 -18.75842 1.000 30.26522 ?  477 VAL   A C   1 
ATOM   3117 O  O   . VAL   A 1 400 ? 2.27939   -28.34753 -17.98515 1.000 28.48490 ?  477 VAL   A O   1 
ATOM   3118 C  CB  . VAL   A 1 400 ? 1.19762   -27.48335 -20.69680 1.000 29.23256 ?  477 VAL   A CB  1 
ATOM   3119 C  CG1 . VAL   A 1 400 ? 2.14734   -28.22086 -21.63851 1.000 25.12755 ?  477 VAL   A CG1 1 
ATOM   3120 C  CG2 . VAL   A 1 400 ? 0.11498   -26.77842 -21.50058 1.000 29.48714 ?  477 VAL   A CG2 1 
ATOM   3121 N  N   . LEU   A 1 401 ? 1.80130   -30.38752 -18.86678 1.000 29.48910 ?  478 LEU   A N   1 
ATOM   3122 C  CA  . LEU   A 1 401 ? 2.69711   -31.12696 -17.99047 1.000 28.05397 ?  478 LEU   A CA  1 
ATOM   3123 C  C   . LEU   A 1 401 ? 3.64514   -32.02671 -18.77388 1.000 27.96649 ?  478 LEU   A C   1 
ATOM   3124 O  O   . LEU   A 1 401 ? 4.28582   -32.90314 -18.19211 1.000 28.00207 ?  478 LEU   A O   1 
ATOM   3125 C  CB  . LEU   A 1 401 ? 1.88165   -31.92523 -16.97712 1.000 29.27473 ?  478 LEU   A CB  1 
ATOM   3126 C  CG  . LEU   A 1 401 ? 1.25963   -30.98449 -15.93925 1.000 28.11613 ?  478 LEU   A CG  1 
ATOM   3127 C  CD1 . LEU   A 1 401 ? 0.08543   -31.62327 -15.24598 1.000 26.72768 ?  478 LEU   A CD1 1 
ATOM   3128 C  CD2 . LEU   A 1 401 ? 2.33177   -30.58294 -14.92965 1.000 26.96324 ?  478 LEU   A CD2 1 
ATOM   3129 N  N   . THR   A 1 402 ? 3.78927   -31.76939 -20.06662 1.000 29.11708 ?  479 THR   A N   1 
ATOM   3130 C  CA  . THR   A 1 402 ? 4.55084   -32.62583 -20.96272 1.000 29.41711 ?  479 THR   A CA  1 
ATOM   3131 C  C   . THR   A 1 402 ? 5.95553   -32.89343 -20.43392 1.000 29.35217 ?  479 THR   A C   1 
ATOM   3132 O  O   . THR   A 1 402 ? 6.70509   -31.96585 -20.11677 1.000 30.03470 ?  479 THR   A O   1 
ATOM   3133 C  CB  . THR   A 1 402 ? 4.61174   -31.94751 -22.33209 1.000 28.01732 ?  479 THR   A CB  1 
ATOM   3134 O  OG1 . THR   A 1 402 ? 3.31268   -31.43111 -22.64199 1.000 25.59723 ?  479 THR   A OG1 1 
ATOM   3135 C  CG2 . THR   A 1 402 ? 5.03307   -32.93386 -23.41318 1.000 28.03006 ?  479 THR   A CG2 1 
ATOM   3136 N  N   . ASN   A 1 403 ? 6.31756   -34.17058 -20.34823 1.000 30.00143 ?  480 ASN   A N   1 
ATOM   3137 C  CA  . ASN   A 1 403 ? 7.67663   -34.55754 -19.98349 1.000 28.42397 ?  480 ASN   A CA  1 
ATOM   3138 C  C   . ASN   A 1 403 ? 8.02183   -34.08274 -18.57017 1.000 30.79676 ?  480 ASN   A C   1 
ATOM   3139 O  O   . ASN   A 1 403 ? 8.94227   -33.29129 -18.35084 1.000 33.71542 ?  480 ASN   A O   1 
ATOM   3140 C  CB  . ASN   A 1 403 ? 8.67627   -34.00708 -21.00327 1.000 32.67289 ?  480 ASN   A CB  1 
ATOM   3141 C  CG  . ASN   A 1 403 ? 10.07294  -34.55048 -20.79462 1.000 33.67171 ?  480 ASN   A CG  1 
ATOM   3142 O  OD1 . ASN   A 1 403 ? 10.24603  -35.63374 -20.23368 1.000 34.98222 ?  480 ASN   A OD1 1 
ATOM   3143 N  ND2 . ASN   A 1 403 ? 11.07982  -33.79826 -21.23998 1.000 31.09658 ?  480 ASN   A ND2 1 
ATOM   3144 N  N   . ASN   A 1 404 ? 7.21773   -34.53413 -17.61391 1.000 30.62837 ?  481 ASN   A N   1 
ATOM   3145 C  CA  . ASN   A 1 404 ? 7.59307   -34.50079 -16.20863 1.000 26.58848 ?  481 ASN   A CA  1 
ATOM   3146 C  C   . ASN   A 1 404 ? 7.68886   -35.94186 -15.72614 1.000 29.47188 ?  481 ASN   A C   1 
ATOM   3147 O  O   . ASN   A 1 404 ? 7.71675   -36.85705 -16.55008 1.000 30.01036 ?  481 ASN   A O   1 
ATOM   3148 C  CB  . ASN   A 1 404 ? 6.58544   -33.69582 -15.38948 1.000 26.88349 ?  481 ASN   A CB  1 
ATOM   3149 C  CG  . ASN   A 1 404 ? 6.78157   -32.18251 -15.53753 1.000 31.86726 ?  481 ASN   A CG  1 
ATOM   3150 O  OD1 . ASN   A 1 404 ? 7.70554   -31.60160 -14.95324 1.000 30.36895 ?  481 ASN   A OD1 1 
ATOM   3151 N  ND2 . ASN   A 1 404 ? 5.91311   -31.54440 -16.31966 1.000 26.71064 ?  481 ASN   A ND2 1 
ATOM   3152 N  N   . GLN   A 1 405 ? 7.70616   -36.15314 -14.40959 1.000 28.02790 ?  482 GLN   A N   1 
ATOM   3153 C  CA  . GLN   A 1 405 ? 7.81730   -37.46985 -13.80051 1.000 27.27712 ?  482 GLN   A CA  1 
ATOM   3154 C  C   . GLN   A 1 405 ? 6.55410   -37.87986 -13.05609 1.000 28.14752 ?  482 GLN   A C   1 
ATOM   3155 O  O   . GLN   A 1 405 ? 6.63374   -38.54497 -12.02562 1.000 25.83427 ?  482 GLN   A O   1 
ATOM   3156 C  CB  . GLN   A 1 405 ? 8.97083   -37.50759 -12.80653 1.000 32.69555 ?  482 GLN   A CB  1 
ATOM   3157 C  CG  . GLN   A 1 405 ? 10.13312  -36.68507 -13.16593 1.000 32.00497 ?  482 GLN   A CG  1 
ATOM   3158 C  CD  . GLN   A 1 405 ? 11.07239  -37.45637 -13.98015 1.000 41.06566 ?  482 GLN   A CD  1 
ATOM   3159 O  OE1 . GLN   A 1 405 ? 10.66179  -38.13264 -14.92789 1.000 43.12917 ?  482 GLN   A OE1 1 
ATOM   3160 N  NE2 . GLN   A 1 405 ? 12.35645  -37.40627 -13.61862 1.000 45.20878 ?  482 GLN   A NE2 1 
ATOM   3161 N  N   . LEU   A 1 406 ? 5.38825   -37.45154 -13.50705 1.000 30.22474 ?  483 LEU   A N   1 
ATOM   3162 C  CA  . LEU   A 1 406 ? 4.19624   -37.72646 -12.72598 1.000 30.42491 ?  483 LEU   A CA  1 
ATOM   3163 C  C   . LEU   A 1 406 ? 3.86093   -39.21174 -12.82011 1.000 31.31119 ?  483 LEU   A C   1 
ATOM   3164 O  O   . LEU   A 1 406 ? 3.90559   -39.79762 -13.90759 1.000 29.48909 ?  483 LEU   A O   1 
ATOM   3165 C  CB  . LEU   A 1 406 ? 3.03785   -36.86997 -13.22094 1.000 29.63720 ?  483 LEU   A CB  1 
ATOM   3166 C  CG  . LEU   A 1 406 ? 3.25388   -35.35717 -13.23259 1.000 31.14531 ?  483 LEU   A CG  1 
ATOM   3167 C  CD1 . LEU   A 1 406 ? 2.12158   -34.67655 -13.97981 1.000 29.71428 ?  483 LEU   A CD1 1 
ATOM   3168 C  CD2 . LEU   A 1 406 ? 3.37008   -34.81485 -11.83232 1.000 28.10370 ?  483 LEU   A CD2 1 
ATOM   3169 N  N   . THR   A 1 407 ? 3.55036   -39.83532 -11.68130 1.000 29.87928 ?  484 THR   A N   1 
ATOM   3170 C  CA  . THR   A 1 407 ? 3.03025   -41.19539 -11.73058 1.000 34.23588 ?  484 THR   A CA  1 
ATOM   3171 C  C   . THR   A 1 407 ? 1.52028   -41.24239 -11.56841 1.000 35.84486 ?  484 THR   A C   1 
ATOM   3172 O  O   . THR   A 1 407 ? 0.89474   -42.17018 -12.08255 1.000 37.41475 ?  484 THR   A O   1 
ATOM   3173 C  CB  . THR   A 1 407 ? 3.70794   -42.09799 -10.68626 1.000 33.13291 ?  484 THR   A CB  1 
ATOM   3174 O  OG1 . THR   A 1 407 ? 3.65764   -41.48780 -9.39117  1.000 38.86029 ?  484 THR   A OG1 1 
ATOM   3175 C  CG2 . THR   A 1 407 ? 5.17812   -42.37697 -11.06640 1.000 26.09724 ?  484 THR   A CG2 1 
ATOM   3176 N  N   . THR   A 1 408 ? 0.91463   -40.24278 -10.92978 1.000 45.96895 ?  485 THR   A N   1 
ATOM   3177 C  CA  . THR   A 1 408 ? -0.53169  -40.06764 -10.99472 1.000 49.15096 ?  485 THR   A CA  1 
ATOM   3178 C  C   . THR   A 1 408 ? -0.87404  -38.59503 -10.80677 1.000 49.42441 ?  485 THR   A C   1 
ATOM   3179 O  O   . THR   A 1 408 ? 0.00588   -37.74591 -10.66256 1.000 54.99734 ?  485 THR   A O   1 
ATOM   3180 C  CB  . THR   A 1 408 ? -1.25336  -40.90521 -9.94510  1.000 54.41168 ?  485 THR   A CB  1 
ATOM   3181 O  OG1 . THR   A 1 408 ? -2.67140  -40.81035 -10.16880 1.000 52.88288 ?  485 THR   A OG1 1 
ATOM   3182 C  CG2 . THR   A 1 408 ? -0.89790  -40.39929 -8.53602  1.000 48.63437 ?  485 THR   A CG2 1 
ATOM   3183 N  N   . LEU   A 1 409 ? -2.17283  -38.30004 -10.79329 1.000 39.99734 ?  486 LEU   A N   1 
ATOM   3184 C  CA  . LEU   A 1 409 ? -2.74028  -36.98760 -10.53812 1.000 38.73673 ?  486 LEU   A CA  1 
ATOM   3185 C  C   . LEU   A 1 409 ? -3.46452  -36.95455 -9.19820  1.000 37.00446 ?  486 LEU   A C   1 
ATOM   3186 O  O   . LEU   A 1 409 ? -3.97166  -37.97735 -8.74090  1.000 35.91258 ?  486 LEU   A O   1 
ATOM   3187 C  CB  . LEU   A 1 409 ? -3.73917  -36.59334 -11.62586 1.000 33.89497 ?  486 LEU   A CB  1 
ATOM   3188 C  CG  . LEU   A 1 409 ? -3.23572  -36.55455 -13.05741 1.000 35.49453 ?  486 LEU   A CG  1 
ATOM   3189 C  CD1 . LEU   A 1 409 ? -4.38671  -36.13420 -13.93713 1.000 34.00104 ?  486 LEU   A CD1 1 
ATOM   3190 C  CD2 . LEU   A 1 409 ? -2.07992  -35.58924 -13.18843 1.000 33.77693 ?  486 LEU   A CD2 1 
ATOM   3191 N  N   . PRO   A 1 410 ? -3.54132  -35.79226 -8.54854  1.000 36.83540 ?  487 PRO   A N   1 
ATOM   3192 C  CA  . PRO   A 1 410 ? -4.38216  -35.67309 -7.34699  1.000 31.68906 ?  487 PRO   A CA  1 
ATOM   3193 C  C   . PRO   A 1 410 ? -5.85122  -35.84658 -7.69009  1.000 32.50602 ?  487 PRO   A C   1 
ATOM   3194 O  O   . PRO   A 1 410 ? -6.31404  -35.42397 -8.75163  1.000 32.62228 ?  487 PRO   A O   1 
ATOM   3195 C  CB  . PRO   A 1 410 ? -4.09562  -34.25097 -6.85094  1.000 32.40898 ?  487 PRO   A CB  1 
ATOM   3196 C  CG  . PRO   A 1 410 ? -2.77617  -33.90450 -7.43711  1.000 34.82128 ?  487 PRO   A CG  1 
ATOM   3197 C  CD  . PRO   A 1 410 ? -2.70111  -34.60257 -8.76262  1.000 33.31791 ?  487 PRO   A CD  1 
ATOM   3198 N  N   . ARG   A 1 411 ? -6.59176  -36.47784 -6.77915  1.000 33.84139 ?  488 ARG   A N   1 
ATOM   3199 C  CA  . ARG   A 1 411 ? -8.02150  -36.64661 -7.01091  1.000 32.43820 ?  488 ARG   A CA  1 
ATOM   3200 C  C   . ARG   A 1 411 ? -8.71677  -35.30762 -7.13921  1.000 30.46146 ?  488 ARG   A C   1 
ATOM   3201 O  O   . ARG   A 1 411 ? -9.74177  -35.21232 -7.81976  1.000 30.74913 ?  488 ARG   A O   1 
ATOM   3202 C  CB  . ARG   A 1 411 ? -8.67279  -37.44845 -5.88519  1.000 36.74093 ?  488 ARG   A CB  1 
ATOM   3203 C  CG  . ARG   A 1 411 ? -8.26088  -38.90839 -5.79193  1.000 40.56496 ?  488 ARG   A CG  1 
ATOM   3204 C  CD  . ARG   A 1 411 ? -9.16928  -39.62151 -4.80211  1.000 45.14457 ?  488 ARG   A CD  1 
ATOM   3205 N  NE  . ARG   A 1 411 ? -8.72708  -40.97258 -4.49533  1.000 46.24704 ?  488 ARG   A NE  1 
ATOM   3206 C  CZ  . ARG   A 1 411 ? -8.93720  -42.02533 -5.27567  1.000 50.79325 ?  488 ARG   A CZ  1 
ATOM   3207 N  NH1 . ARG   A 1 411 ? -9.57792  -41.91561 -6.43397  1.000 51.13421 ?  488 ARG   A NH1 1 
ATOM   3208 N  NH2 . ARG   A 1 411 ? -8.48258  -43.21599 -4.89176  1.000 44.47814 ?  488 ARG   A NH2 1 
ATOM   3209 N  N   . GLY   A 1 412 ? -8.18796  -34.26802 -6.48545  1.000 30.08219 ?  489 GLY   A N   1 
ATOM   3210 C  CA  . GLY   A 1 412 ? -8.75981  -32.92380 -6.59035  1.000 31.26066 ?  489 GLY   A CA  1 
ATOM   3211 C  C   . GLY   A 1 412 ? -8.76980  -32.36266 -8.00340  1.000 32.07849 ?  489 GLY   A C   1 
ATOM   3212 O  O   . GLY   A 1 412 ? -9.47333  -31.38178 -8.26733  1.000 32.24415 ?  489 GLY   A O   1 
ATOM   3213 N  N   . ILE   A 1 413 ? -8.01774  -32.97229 -8.91710  1.000 30.58285 ?  490 ILE   A N   1 
ATOM   3214 C  CA  . ILE   A 1 413 ? -7.96219  -32.49654 -10.28375 1.000 30.73598 ?  490 ILE   A CA  1 
ATOM   3215 C  C   . ILE   A 1 413 ? -9.35363  -32.44979 -10.90090 1.000 33.10094 ?  490 ILE   A C   1 
ATOM   3216 O  O   . ILE   A 1 413 ? -9.59246  -31.67632 -11.83241 1.000 34.88730 ?  490 ILE   A O   1 
ATOM   3217 C  CB  . ILE   A 1 413 ? -6.97812  -33.38896 -11.07164 1.000 31.69213 ?  490 ILE   A CB  1 
ATOM   3218 C  CG1 . ILE   A 1 413 ? -6.33039  -32.61414 -12.19805 1.000 33.46491 ?  490 ILE   A CG1 1 
ATOM   3219 C  CG2 . ILE   A 1 413 ? -7.67135  -34.63919 -11.60333 1.000 31.23071 ?  490 ILE   A CG2 1 
ATOM   3220 C  CD1 . ILE   A 1 413 ? -7.27799  -32.32341 -13.31287 1.000 35.07930 ?  490 ILE   A CD1 1 
ATOM   3221 N  N   . GLY   A 1 414 ? -10.30066 -33.23012 -10.37602 1.000 34.12765 ?  491 GLY   A N   1 
ATOM   3222 C  CA  . GLY   A 1 414 ? -11.65594 -33.21855 -10.90806 1.000 30.09143 ?  491 GLY   A CA  1 
ATOM   3223 C  C   . GLY   A 1 414 ? -12.47154 -32.00483 -10.52912 1.000 31.22850 ?  491 GLY   A C   1 
ATOM   3224 O  O   . GLY   A 1 414 ? -13.60921 -31.87083 -10.99570 1.000 34.22467 ?  491 GLY   A O   1 
ATOM   3225 N  N   . HIS   A 1 415 ? -11.94198 -31.12715 -9.68611  1.000 29.64154 ?  492 HIS   A N   1 
ATOM   3226 C  CA  . HIS   A 1 415 ? -12.65624 -29.87911 -9.45359  1.000 33.56625 ?  492 HIS   A CA  1 
ATOM   3227 C  C   . HIS   A 1 415 ? -12.39999 -28.84266 -10.53189 1.000 32.11911 ?  492 HIS   A C   1 
ATOM   3228 O  O   . HIS   A 1 415 ? -13.11116 -27.83292 -10.57250 1.000 35.32261 ?  492 HIS   A O   1 
ATOM   3229 C  CB  . HIS   A 1 415 ? -12.29956 -29.28999 -8.09346  1.000 31.29367 ?  492 HIS   A CB  1 
ATOM   3230 C  CG  . HIS   A 1 415 ? -13.02971 -29.94434 -6.96940  1.000 36.27115 ?  492 HIS   A CG  1 
ATOM   3231 N  ND1 . HIS   A 1 415 ? -12.40118 -30.73683 -6.02843  1.000 38.60847 ?  492 HIS   A ND1 1 
ATOM   3232 C  CD2 . HIS   A 1 415 ? -14.34553 -29.95004 -6.65157  1.000 34.29350 ?  492 HIS   A CD2 1 
ATOM   3233 C  CE1 . HIS   A 1 415 ? -13.29915 -31.19512 -5.17336  1.000 35.48701 ?  492 HIS   A CE1 1 
ATOM   3234 N  NE2 . HIS   A 1 415 ? -14.48532 -30.73095 -5.52884  1.000 39.32308 ?  492 HIS   A NE2 1 
ATOM   3235 N  N   . LEU   A 1 416 ? -11.42418 -29.07579 -11.40752 1.000 28.71194 ?  493 LEU   A N   1 
ATOM   3236 C  CA  . LEU   A 1 416 ? -11.06258 -28.11557 -12.44244 1.000 30.79468 ?  493 LEU   A CA  1 
ATOM   3237 C  C   . LEU   A 1 416 ? -12.07267 -28.20242 -13.58285 1.000 30.51396 ?  493 LEU   A C   1 
ATOM   3238 O  O   . LEU   A 1 416 ? -11.79193 -28.71392 -14.67019 1.000 30.45727 ?  493 LEU   A O   1 
ATOM   3239 C  CB  . LEU   A 1 416 ? -9.64672  -28.37150 -12.93017 1.000 27.65126 ?  493 LEU   A CB  1 
ATOM   3240 C  CG  . LEU   A 1 416 ? -8.52687  -28.25978 -11.90356 1.000 31.44578 ?  493 LEU   A CG  1 
ATOM   3241 C  CD1 . LEU   A 1 416 ? -7.18540  -28.28325 -12.62639 1.000 29.54819 ?  493 LEU   A CD1 1 
ATOM   3242 C  CD2 . LEU   A 1 416 ? -8.65737  -27.02309 -11.01665 1.000 27.26940 ?  493 LEU   A CD2 1 
ATOM   3243 N  N   . THR   A 1 417 ? -13.26247 -27.64733 -13.33554 1.000 28.43240 ?  494 THR   A N   1 
ATOM   3244 C  CA  . THR   A 1 417 ? -14.37037 -27.79607 -14.27136 1.000 30.33265 ?  494 THR   A CA  1 
ATOM   3245 C  C   . THR   A 1 417 ? -14.25068 -26.90969 -15.50790 1.000 33.05197 ?  494 THR   A C   1 
ATOM   3246 O  O   . THR   A 1 417 ? -14.96603 -27.15515 -16.49016 1.000 37.73820 ?  494 THR   A O   1 
ATOM   3247 C  CB  . THR   A 1 417 ? -15.70353 -27.49529 -13.57672 1.000 30.61424 ?  494 THR   A CB  1 
ATOM   3248 O  OG1 . THR   A 1 417 ? -15.76022 -26.10672 -13.23409 1.000 30.17393 ?  494 THR   A OG1 1 
ATOM   3249 C  CG2 . THR   A 1 417 ? -15.84432 -28.32892 -12.31809 1.000 27.29993 ?  494 THR   A CG2 1 
ATOM   3250 N  N   . ASN   A 1 418 ? -13.39727 -25.88548 -15.49413 1.000 26.87042 ?  495 ASN   A N   1 
ATOM   3251 C  CA  . ASN   A 1 418 ? -13.16634 -25.10096 -16.70194 1.000 30.23469 ?  495 ASN   A CA  1 
ATOM   3252 C  C   . ASN   A 1 418 ? -12.03308 -25.66375 -17.54913 1.000 30.58375 ?  495 ASN   A C   1 
ATOM   3253 O  O   . ASN   A 1 418 ? -11.70171 -25.08928 -18.58858 1.000 28.49336 ?  495 ASN   A O   1 
ATOM   3254 C  CB  . ASN   A 1 418 ? -12.88008 -23.62755 -16.35677 1.000 28.64977 ?  495 ASN   A CB  1 
ATOM   3255 C  CG  . ASN   A 1 418 ? -14.15405 -22.85425 -15.95637 1.000 36.01225 ?  495 ASN   A CG  1 
ATOM   3256 O  OD1 . ASN   A 1 418 ? -15.18397 -22.93107 -16.63470 1.000 34.52211 ?  495 ASN   A OD1 1 
ATOM   3257 N  ND2 . ASN   A 1 418 ? -14.08396 -22.12447 -14.84268 1.000 29.70819 ?  495 ASN   A ND2 1 
ATOM   3258 N  N   . LEU   A 1 419 ? -11.44408 -26.77703 -17.14635 1.000 30.27143 ?  496 LEU   A N   1 
ATOM   3259 C  CA  . LEU   A 1 419 ? -10.25001 -27.25452 -17.82382 1.000 30.87689 ?  496 LEU   A CA  1 
ATOM   3260 C  C   . LEU   A 1 419 ? -10.63196 -27.80744 -19.19257 1.000 29.86050 ?  496 LEU   A C   1 
ATOM   3261 O  O   . LEU   A 1 419 ? -11.49702 -28.68253 -19.29096 1.000 30.41577 ?  496 LEU   A O   1 
ATOM   3262 C  CB  . LEU   A 1 419 ? -9.55493  -28.30166 -16.96248 1.000 27.46762 ?  496 LEU   A CB  1 
ATOM   3263 C  CG  . LEU   A 1 419 ? -8.17085  -28.71463 -17.42480 1.000 29.19368 ?  496 LEU   A CG  1 
ATOM   3264 C  CD1 . LEU   A 1 419 ? -7.22987  -27.54239 -17.30253 1.000 25.14272 ?  496 LEU   A CD1 1 
ATOM   3265 C  CD2 . LEU   A 1 419 ? -7.68052  -29.91901 -16.62869 1.000 25.04385 ?  496 LEU   A CD2 1 
ATOM   3266 N  N   . THR   A 1 420 ? -10.02673 -27.26502 -20.25531 1.000 26.96773 ?  497 THR   A N   1 
ATOM   3267 C  CA  . THR   A 1 420 ? -10.29051 -27.74116 -21.60751 1.000 28.99330 ?  497 THR   A CA  1 
ATOM   3268 C  C   . THR   A 1 420 ? -9.13826  -28.52708 -22.20139 1.000 30.30299 ?  497 THR   A C   1 
ATOM   3269 O  O   . THR   A 1 420 ? -9.36057  -29.36260 -23.07624 1.000 31.09096 ?  497 THR   A O   1 
ATOM   3270 C  CB  . THR   A 1 420 ? -10.60669 -26.57608 -22.55543 1.000 30.22350 ?  497 THR   A CB  1 
ATOM   3271 O  OG1 . THR   A 1 420 ? -9.40718  -25.85008 -22.81952 1.000 30.49572 ?  497 THR   A OG1 1 
ATOM   3272 C  CG2 . THR   A 1 420 ? -11.64777 -25.61641 -21.96534 1.000 30.41248 ?  497 THR   A CG2 1 
ATOM   3273 N  N   . HIS   A 1 421 ? -7.91743  -28.28167 -21.74908 1.000 28.65717 ?  498 HIS   A N   1 
ATOM   3274 C  CA  . HIS   A 1 421 ? -6.72595  -28.85703 -22.35372 1.000 29.46516 ?  498 HIS   A CA  1 
ATOM   3275 C  C   . HIS   A 1 421 ? -5.84873  -29.36525 -21.22095 1.000 29.74131 ?  498 HIS   A C   1 
ATOM   3276 O  O   . HIS   A 1 421 ? -5.42820  -28.58558 -20.35546 1.000 28.03357 ?  498 HIS   A O   1 
ATOM   3277 C  CB  . HIS   A 1 421 ? -6.00615  -27.81006 -23.22035 1.000 29.55143 ?  498 HIS   A CB  1 
ATOM   3278 C  CG  . HIS   A 1 421 ? -4.68805  -28.25353 -23.78825 1.000 32.13408 ?  498 HIS   A CG  1 
ATOM   3279 N  ND1 . HIS   A 1 421 ? -3.63977  -28.69955 -23.00587 1.000 32.92562 ?  498 HIS   A ND1 1 
ATOM   3280 C  CD2 . HIS   A 1 421 ? -4.23004  -28.25942 -25.06351 1.000 31.23930 ?  498 HIS   A CD2 1 
ATOM   3281 C  CE1 . HIS   A 1 421 ? -2.60358  -28.98177 -23.77725 1.000 32.55547 ?  498 HIS   A CE1 1 
ATOM   3282 N  NE2 . HIS   A 1 421 ? -2.93583  -28.71962 -25.02888 1.000 34.18108 ?  498 HIS   A NE2 1 
ATOM   3283 N  N   . LEU   A 1 422 ? -5.60838  -30.67231 -21.21351 1.000 28.03998 ?  499 LEU   A N   1 
ATOM   3284 C  CA  . LEU   A 1 422 ? -4.77718  -31.34146 -20.22288 1.000 25.08219 ?  499 LEU   A CA  1 
ATOM   3285 C  C   . LEU   A 1 422 ? -3.66052  -32.03025 -20.98742 1.000 29.61917 ?  499 LEU   A C   1 
ATOM   3286 O  O   . LEU   A 1 422 ? -3.91464  -33.01037 -21.69543 1.000 32.52317 ?  499 LEU   A O   1 
ATOM   3287 C  CB  . LEU   A 1 422 ? -5.60327  -32.34529 -19.42729 1.000 23.99802 ?  499 LEU   A CB  1 
ATOM   3288 C  CG  . LEU   A 1 422 ? -4.94106  -32.97761 -18.22266 1.000 27.13574 ?  499 LEU   A CG  1 
ATOM   3289 C  CD1 . LEU   A 1 422 ? -4.07486  -31.95552 -17.45710 1.000 25.70284 ?  499 LEU   A CD1 1 
ATOM   3290 C  CD2 . LEU   A 1 422 ? -6.02727  -33.52964 -17.33048 1.000 30.69234 ?  499 LEU   A CD2 1 
ATOM   3291 N  N   . GLY   A 1 423 ? -2.43539  -31.50678 -20.88092 1.000 27.14446 ?  500 GLY   A N   1 
ATOM   3292 C  CA  . GLY   A 1 423 ? -1.31425  -32.08138 -21.60714 1.000 25.61415 ?  500 GLY   A CA  1 
ATOM   3293 C  C   . GLY   A 1 423 ? -0.41314  -32.90596 -20.71033 1.000 28.29030 ?  500 GLY   A C   1 
ATOM   3294 O  O   . GLY   A 1 423 ? 0.40925   -32.34856 -19.97838 1.000 27.07116 ?  500 GLY   A O   1 
ATOM   3295 N  N   . LEU   A 1 424 ? -0.55678  -34.23559 -20.75940 1.000 28.90499 ?  501 LEU   A N   1 
ATOM   3296 C  CA  . LEU   A 1 424 ? 0.15031   -35.14329 -19.86546 1.000 27.08918 ?  501 LEU   A CA  1 
ATOM   3297 C  C   . LEU   A 1 424 ? 1.18818   -36.00307 -20.57911 1.000 28.43234 ?  501 LEU   A C   1 
ATOM   3298 O  O   . LEU   A 1 424 ? 1.73655   -36.93081 -19.97386 1.000 26.77277 ?  501 LEU   A O   1 
ATOM   3299 C  CB  . LEU   A 1 424 ? -0.85830  -36.02892 -19.13552 1.000 23.79293 ?  501 LEU   A CB  1 
ATOM   3300 C  CG  . LEU   A 1 424 ? -1.65346  -35.28726 -18.06475 1.000 26.53103 ?  501 LEU   A CG  1 
ATOM   3301 C  CD1 . LEU   A 1 424 ? -2.83990  -36.08970 -17.64296 1.000 28.41360 ?  501 LEU   A CD1 1 
ATOM   3302 C  CD2 . LEU   A 1 424 ? -0.77951  -35.00500 -16.86137 1.000 29.83976 ?  501 LEU   A CD2 1 
ATOM   3303 N  N   . GLY   A 1 425 ? 1.48763   -35.71262 -21.83928 1.000 27.62208 ?  502 GLY   A N   1 
ATOM   3304 C  CA  . GLY   A 1 425 ? 2.38108   -36.57516 -22.58661 1.000 26.11159 ?  502 GLY   A CA  1 
ATOM   3305 C  C   . GLY   A 1 425 ? 3.76557   -36.65409 -21.97405 1.000 25.33262 ?  502 GLY   A C   1 
ATOM   3306 O  O   . GLY   A 1 425 ? 4.23114   -35.74235 -21.30160 1.000 27.76268 ?  502 GLY   A O   1 
ATOM   3307 N  N   . GLU   A 1 426 ? 4.42808   -37.77508 -22.21637 1.000 28.15072 ?  503 GLU   A N   1 
ATOM   3308 C  CA  . GLU   A 1 426 ? 5.81648   -37.97086 -21.81067 1.000 26.76678 ?  503 GLU   A CA  1 
ATOM   3309 C  C   . GLU   A 1 426 ? 5.98874   -37.93242 -20.29748 1.000 25.35083 ?  503 GLU   A C   1 
ATOM   3310 O  O   . GLU   A 1 426 ? 6.94206   -37.35288 -19.78591 1.000 30.65449 ?  503 GLU   A O   1 
ATOM   3311 C  CB  . GLU   A 1 426 ? 6.73060   -36.95034 -22.49082 1.000 30.27934 ?  503 GLU   A CB  1 
ATOM   3312 C  CG  . GLU   A 1 426 ? 6.74459   -37.05926 -24.03100 1.000 29.10436 ?  503 GLU   A CG  1 
ATOM   3313 C  CD  . GLU   A 1 426 ? 7.64828   -36.02387 -24.71575 1.000 36.72461 ?  503 GLU   A CD  1 
ATOM   3314 O  OE1 . GLU   A 1 426 ? 8.66559   -35.59496 -24.10807 1.000 37.98406 ?  503 GLU   A OE1 1 
ATOM   3315 O  OE2 . GLU   A 1 426 ? 7.33087   -35.62820 -25.86323 1.000 36.91411 ?  503 GLU   A OE2 1 
ATOM   3316 N  N   . ASN   A 1 427 ? 5.09259   -38.58990 -19.57036 1.000 26.14268 ?  504 ASN   A N   1 
ATOM   3317 C  CA  . ASN   A 1 427 ? 5.22534   -38.71302 -18.12203 1.000 27.72499 ?  504 ASN   A CA  1 
ATOM   3318 C  C   . ASN   A 1 427 ? 5.42931   -40.18525 -17.72018 1.000 32.05067 ?  504 ASN   A C   1 
ATOM   3319 O  O   . ASN   A 1 427 ? 5.74686   -41.04174 -18.56631 1.000 30.81740 ?  504 ASN   A O   1 
ATOM   3320 C  CB  . ASN   A 1 427 ? 4.00634   -38.07672 -17.44555 1.000 25.04283 ?  504 ASN   A CB  1 
ATOM   3321 C  CG  . ASN   A 1 427 ? 4.13941   -36.57276 -17.30526 1.000 30.72821 ?  504 ASN   A CG  1 
ATOM   3322 O  OD1 . ASN   A 1 427 ? 4.68831   -36.07598 -16.31995 1.000 30.21080 ?  504 ASN   A OD1 1 
ATOM   3323 N  ND2 . ASN   A 1 427 ? 3.63990   -35.83771 -18.28910 1.000 28.56510 ?  504 ASN   A ND2 1 
ATOM   3324 N  N   . LEU   A 1 428 ? 5.23718   -40.47747 -16.43040 1.000 28.84073 ?  505 LEU   A N   1 
ATOM   3325 C  CA  . LEU   A 1 428 ? 5.33660   -41.83212 -15.89977 1.000 30.07513 ?  505 LEU   A CA  1 
ATOM   3326 C  C   . LEU   A 1 428 ? 4.01869   -42.28198 -15.27727 1.000 29.57515 ?  505 LEU   A C   1 
ATOM   3327 O  O   . LEU   A 1 428 ? 4.01453   -42.98534 -14.26680 1.000 29.48468 ?  505 LEU   A O   1 
ATOM   3328 C  CB  . LEU   A 1 428 ? 6.46250   -41.93000 -14.87062 1.000 26.96463 ?  505 LEU   A CB  1 
ATOM   3329 C  CG  . LEU   A 1 428 ? 7.84041   -41.60812 -15.44394 1.000 30.73528 ?  505 LEU   A CG  1 
ATOM   3330 C  CD1 . LEU   A 1 428 ? 8.90608   -41.54114 -14.36976 1.000 27.99963 ?  505 LEU   A CD1 1 
ATOM   3331 C  CD2 . LEU   A 1 428 ? 8.21304   -42.64758 -16.47998 1.000 34.72629 ?  505 LEU   A CD2 1 
ATOM   3332 N  N   . LEU   A 1 429 ? 2.89900   -41.85224 -15.84840 1.000 27.03368 ?  506 LEU   A N   1 
ATOM   3333 C  CA  . LEU   A 1 429 ? 1.59739   -42.13521 -15.26077 1.000 31.17702 ?  506 LEU   A CA  1 
ATOM   3334 C  C   . LEU   A 1 429 ? 1.32165   -43.63727 -15.25506 1.000 35.54286 ?  506 LEU   A C   1 
ATOM   3335 O  O   . LEU   A 1 429 ? 1.56833   -44.33348 -16.24812 1.000 30.75361 ?  506 LEU   A O   1 
ATOM   3336 C  CB  . LEU   A 1 429 ? 0.50050   -41.40481 -16.04104 1.000 28.15731 ?  506 LEU   A CB  1 
ATOM   3337 C  CG  . LEU   A 1 429 ? 0.51460   -39.87059 -16.03782 1.000 27.49554 ?  506 LEU   A CG  1 
ATOM   3338 C  CD1 . LEU   A 1 429 ? -0.50869  -39.32350 -16.99692 1.000 25.17938 ?  506 LEU   A CD1 1 
ATOM   3339 C  CD2 . LEU   A 1 429 ? 0.25985   -39.33027 -14.65255 1.000 30.93394 ?  506 LEU   A CD2 1 
ATOM   3340 N  N   . THR   A 1 430 ? 0.80677   -44.14256 -14.12316 1.000 32.50421 ?  507 THR   A N   1 
ATOM   3341 C  CA  . THR   A 1 430 ? 0.28108   -45.50410 -14.09244 1.000 37.24832 ?  507 THR   A CA  1 
ATOM   3342 C  C   . THR   A 1 430 ? -1.23215  -45.56288 -14.24911 1.000 36.43245 ?  507 THR   A C   1 
ATOM   3343 O  O   . THR   A 1 430 ? -1.75005  -46.57553 -14.73328 1.000 38.17283 ?  507 THR   A O   1 
ATOM   3344 C  CB  . THR   A 1 430 ? 0.68569   -46.22828 -12.79468 1.000 36.19971 ?  507 THR   A CB  1 
ATOM   3345 O  OG1 . THR   A 1 430 ? 0.35406   -45.41839 -11.65898 1.000 39.34293 ?  507 THR   A OG1 1 
ATOM   3346 C  CG2 . THR   A 1 430 ? 2.18529   -46.51418 -12.79103 1.000 26.95387 ?  507 THR   A CG2 1 
ATOM   3347 N  N   . HIS   A 1 431 ? -1.94340  -44.49827 -13.89778 1.000 36.30333 ?  508 HIS   A N   1 
ATOM   3348 C  CA  . HIS   A 1 431 ? -3.39806  -44.49890 -13.96950 1.000 39.25667 ?  508 HIS   A CA  1 
ATOM   3349 C  C   . HIS   A 1 431 ? -3.88534  -43.06632 -13.79703 1.000 35.86054 ?  508 HIS   A C   1 
ATOM   3350 O  O   . HIS   A 1 431 ? -3.19269  -42.22912 -13.21903 1.000 34.18978 ?  508 HIS   A O   1 
ATOM   3351 C  CB  . HIS   A 1 431 ? -4.00795  -45.40404 -12.88812 1.000 37.50935 ?  508 HIS   A CB  1 
ATOM   3352 C  CG  . HIS   A 1 431 ? -3.71779  -44.94076 -11.49232 1.000 40.28876 ?  508 HIS   A CG  1 
ATOM   3353 N  ND1 . HIS   A 1 431 ? -2.44846  -44.95452 -10.95355 1.000 41.45763 ?  508 HIS   A ND1 1 
ATOM   3354 C  CD2 . HIS   A 1 431 ? -4.52568  -44.42371 -10.53565 1.000 43.49566 ?  508 HIS   A CD2 1 
ATOM   3355 C  CE1 . HIS   A 1 431 ? -2.48601  -44.46783 -9.72580  1.000 42.69357 ?  508 HIS   A CE1 1 
ATOM   3356 N  NE2 . HIS   A 1 431 ? -3.73498  -44.13801 -9.44742  1.000 43.98132 ?  508 HIS   A NE2 1 
ATOM   3357 N  N   . LEU   A 1 432 ? -5.10429  -42.79739 -14.30028 1.000 34.25557 ?  509 LEU   A N   1 
ATOM   3358 C  CA  . LEU   A 1 432 ? -5.70829  -41.51862 -13.97337 1.000 36.44328 ?  509 LEU   A CA  1 
ATOM   3359 C  C   . LEU   A 1 432 ? -6.76189  -41.69309 -12.88258 1.000 35.81877 ?  509 LEU   A C   1 
ATOM   3360 O  O   . LEU   A 1 432 ? -7.39656  -42.74534 -12.79440 1.000 38.31999 ?  509 LEU   A O   1 
ATOM   3361 C  CB  . LEU   A 1 432 ? -6.35018  -40.89703 -15.21633 1.000 33.01594 ?  509 LEU   A CB  1 
ATOM   3362 C  CG  . LEU   A 1 432 ? -5.43652  -40.84619 -16.43511 1.000 32.97211 ?  509 LEU   A CG  1 
ATOM   3363 C  CD1 . LEU   A 1 432 ? -6.22721  -40.39467 -17.65128 1.000 34.69616 ?  509 LEU   A CD1 1 
ATOM   3364 C  CD2 . LEU   A 1 432 ? -4.25836  -39.93535 -16.17260 1.000 27.38766 ?  509 LEU   A CD2 1 
ATOM   3365 N  N   . PRO   A 1 433 ? -6.98249  -40.68840 -12.03297 1.000 37.80847 ?  510 PRO   A N   1 
ATOM   3366 C  CA  . PRO   A 1 433 ? -8.01188  -40.81152 -10.99426 1.000 34.01672 ?  510 PRO   A CA  1 
ATOM   3367 C  C   . PRO   A 1 433 ? -9.40216  -40.93689 -11.59318 1.000 36.15289 ?  510 PRO   A C   1 
ATOM   3368 O  O   . PRO   A 1 433 ? -9.66757  -40.51020 -12.71948 1.000 37.53503 ?  510 PRO   A O   1 
ATOM   3369 C  CB  . PRO   A 1 433 ? -7.86938  -39.51008 -10.20066 1.000 31.74550 ?  510 PRO   A CB  1 
ATOM   3370 C  CG  . PRO   A 1 433 ? -7.28627  -38.57171 -11.14012 1.000 31.39588 ?  510 PRO   A CG  1 
ATOM   3371 C  CD  . PRO   A 1 433 ? -6.35840  -39.35752 -12.01920 1.000 34.91533 ?  510 PRO   A CD  1 
ATOM   3372 N  N   . GLU   A 1 434 ? -10.30655 -41.54223 -10.82077 1.000 38.74631 ?  511 GLU   A N   1 
ATOM   3373 C  CA  . GLU   A 1 434 ? -11.69743 -41.62368 -11.26178 1.000 41.05543 ?  511 GLU   A CA  1 
ATOM   3374 C  C   . GLU   A 1 434 ? -12.35258 -40.24856 -11.31199 1.000 40.38197 ?  511 GLU   A C   1 
ATOM   3375 O  O   . GLU   A 1 434 ? -13.33144 -40.06475 -12.04541 1.000 37.82026 ?  511 GLU   A O   1 
ATOM   3376 C  CB  . GLU   A 1 434 ? -12.49905 -42.55504 -10.34999 1.000 41.04909 ?  511 GLU   A CB  1 
ATOM   3377 C  CG  . GLU   A 1 434 ? -11.69178 -43.13946 -9.20663  1.000 44.80008 ?  511 GLU   A CG  1 
ATOM   3378 C  CD  . GLU   A 1 434 ? -11.32455 -44.58361 -9.45346  1.000 46.87750 ?  511 GLU   A CD  1 
ATOM   3379 O  OE1 . GLU   A 1 434 ? -12.13567 -45.28498 -10.08954 1.000 52.65240 ?  511 GLU   A OE1 1 
ATOM   3380 O  OE2 . GLU   A 1 434 ? -10.23267 -45.02305 -9.02530  1.000 48.52177 ?  511 GLU   A OE2 1 
ATOM   3381 N  N   . GLU   A 1 435 ? -11.81442 -39.28074 -10.56410 1.000 37.92496 ?  512 GLU   A N   1 
ATOM   3382 C  CA  . GLU   A 1 435 ? -12.29961 -37.90481 -10.56589 1.000 38.98595 ?  512 GLU   A CA  1 
ATOM   3383 C  C   . GLU   A 1 435 ? -12.02825 -37.17488 -11.87682 1.000 36.62867 ?  512 GLU   A C   1 
ATOM   3384 O  O   . GLU   A 1 435 ? -12.45087 -36.02644 -12.02056 1.000 33.70769 ?  512 GLU   A O   1 
ATOM   3385 C  CB  . GLU   A 1 435 ? -11.65407 -37.12675 -9.41739  1.000 38.91184 ?  512 GLU   A CB  1 
ATOM   3386 C  CG  . GLU   A 1 435 ? -10.97568 -38.00943 -8.37322  1.000 41.38603 ?  512 GLU   A CG  1 
ATOM   3387 C  CD  . GLU   A 1 435 ? -11.94447 -38.93940 -7.69377  1.000 45.25578 ?  512 GLU   A CD  1 
ATOM   3388 O  OE1 . GLU   A 1 435 ? -13.01631 -39.19101 -8.27987  1.000 53.75260 ?  512 GLU   A OE1 1 
ATOM   3389 O  OE2 . GLU   A 1 435 ? -11.64928 -39.41561 -6.57862  1.000 48.56647 ?  512 GLU   A OE2 1 
ATOM   3390 N  N   . ILE   A 1 436 ? -11.34470 -37.80596 -12.82985 1.000 38.30497 ?  513 ILE   A N   1 
ATOM   3391 C  CA  . ILE   A 1 436 ? -11.12991 -37.24053 -14.15771 1.000 34.62154 ?  513 ILE   A CA  1 
ATOM   3392 C  C   . ILE   A 1 436 ? -12.48905 -36.92467 -14.75962 1.000 34.55210 ?  513 ILE   A C   1 
ATOM   3393 O  O   . ILE   A 1 436 ? -12.61419 -36.05493 -15.62901 1.000 34.81122 ?  513 ILE   A O   1 
ATOM   3394 C  CB  . ILE   A 1 436 ? -10.33678 -38.21656 -15.05525 1.000 37.40885 ?  513 ILE   A CB  1 
ATOM   3395 C  CG1 . ILE   A 1 436 ? -9.50088  -37.45646 -16.07397 1.000 37.30428 ?  513 ILE   A CG1 1 
ATOM   3396 C  CG2 . ILE   A 1 436 ? -11.26945 -39.19790 -15.79740 1.000 34.10076 ?  513 ILE   A CG2 1 
ATOM   3397 C  CD1 . ILE   A 1 436 ? -8.28183  -36.79590 -15.44946 1.000 37.29885 ?  513 ILE   A CD1 1 
ATOM   3398 N  N   . GLY   A 1 437 ? -13.51624 -37.64269 -14.30345 1.000 34.82948 ?  514 GLY   A N   1 
ATOM   3399 C  CA  . GLY   A 1 437 ? -14.82033 -37.63623 -14.94758 1.000 34.92234 ?  514 GLY   A CA  1 
ATOM   3400 C  C   . GLY   A 1 437 ? -15.66072 -36.39717 -14.74741 1.000 33.23733 ?  514 GLY   A C   1 
ATOM   3401 O  O   . GLY   A 1 437 ? -16.66008 -36.22033 -15.45246 1.000 33.13617 ?  514 GLY   A O   1 
ATOM   3402 N  N   . THR   A 1 438 ? -15.31229 -35.54277 -13.79518 1.000 33.22045 ?  515 THR   A N   1 
ATOM   3403 C  CA  . THR   A 1 438 ? -16.04904 -34.29665 -13.63294 1.000 35.99390 ?  515 THR   A CA  1 
ATOM   3404 C  C   . THR   A 1 438 ? -15.42786 -33.14070 -14.41691 1.000 36.32505 ?  515 THR   A C   1 
ATOM   3405 O  O   . THR   A 1 438 ? -15.90250 -32.00590 -14.30527 1.000 35.23281 ?  515 THR   A O   1 
ATOM   3406 C  CB  . THR   A 1 438 ? -16.16666 -33.93991 -12.14725 1.000 35.27632 ?  515 THR   A CB  1 
ATOM   3407 O  OG1 . THR   A 1 438 ? -14.92737 -34.20935 -11.48657 1.000 34.84338 ?  515 THR   A OG1 1 
ATOM   3408 C  CG2 . THR   A 1 438 ? -17.25264 -34.76056 -11.49554 1.000 36.23961 ?  515 THR   A CG2 1 
ATOM   3409 N  N   . LEU   A 1 439 ? -14.38213 -33.39951 -15.20571 1.000 32.48750 ?  516 LEU   A N   1 
ATOM   3410 C  CA  . LEU   A 1 439 ? -13.79337 -32.37820 -16.06636 1.000 31.03671 ?  516 LEU   A CA  1 
ATOM   3411 C  C   . LEU   A 1 439 ? -14.75861 -32.14240 -17.21976 1.000 34.61189 ?  516 LEU   A C   1 
ATOM   3412 O  O   . LEU   A 1 439 ? -14.58717 -32.64513 -18.33244 1.000 31.74151 ?  516 LEU   A O   1 
ATOM   3413 C  CB  . LEU   A 1 439 ? -12.41779 -32.80190 -16.55145 1.000 34.69331 ?  516 LEU   A CB  1 
ATOM   3414 C  CG  . LEU   A 1 439 ? -11.36864 -32.95722 -15.44692 1.000 34.05915 ?  516 LEU   A CG  1 
ATOM   3415 C  CD1 . LEU   A 1 439 ? -9.99412  -33.29060 -16.03056 1.000 32.17866 ?  516 LEU   A CD1 1 
ATOM   3416 C  CD2 . LEU   A 1 439 ? -11.30241 -31.71062 -14.58186 1.000 33.93508 ?  516 LEU   A CD2 1 
ATOM   3417 N  N   . GLU   A 1 440 ? -15.79409 -31.34217 -16.93227 1.000 39.12217 ?  517 GLU   A N   1 
ATOM   3418 C  CA  . GLU   A 1 440 ? -16.93964 -31.23720 -17.83253 1.000 43.41019 ?  517 GLU   A CA  1 
ATOM   3419 C  C   . GLU   A 1 440 ? -16.53889 -30.68054 -19.18725 1.000 38.68827 ?  517 GLU   A C   1 
ATOM   3420 O  O   . GLU   A 1 440 ? -17.08386 -31.09037 -20.21651 1.000 37.78390 ?  517 GLU   A O   1 
ATOM   3421 C  CB  . GLU   A 1 440 ? -18.03644 -30.36551 -17.20704 1.000 46.79089 ?  517 GLU   A CB  1 
ATOM   3422 C  CG  . GLU   A 1 440 ? -19.26197 -31.16806 -16.73095 1.000 55.37526 ?  517 GLU   A CG  1 
ATOM   3423 C  CD  . GLU   A 1 440 ? -20.56169 -30.36276 -16.76347 1.000 61.64141 ?  517 GLU   A CD  1 
ATOM   3424 O  OE1 . GLU   A 1 440 ? -20.56930 -29.28029 -17.40612 1.000 58.92062 ?  517 GLU   A OE1 1 
ATOM   3425 O  OE2 . GLU   A 1 440 ? -21.56793 -30.81897 -16.15002 1.000 58.47713 ?  517 GLU   A OE2 1 
ATOM   3426 N  N   . ASN   A 1 441 ? -15.59999 -29.73918 -19.20673 1.000 35.70443 ?  518 ASN   A N   1 
ATOM   3427 C  CA  . ASN   A 1 441 ? -15.23406 -29.03033 -20.42337 1.000 34.38401 ?  518 ASN   A CA  1 
ATOM   3428 C  C   . ASN   A 1 441 ? -13.95676 -29.57004 -21.06276 1.000 33.28679 ?  518 ASN   A C   1 
ATOM   3429 O  O   . ASN   A 1 441 ? -13.38528 -28.91335 -21.94077 1.000 35.04906 ?  518 ASN   A O   1 
ATOM   3430 C  CB  . ASN   A 1 441 ? -15.09483 -27.53689 -20.12686 1.000 31.74965 ?  518 ASN   A CB  1 
ATOM   3431 C  CG  . ASN   A 1 441 ? -16.41004 -26.90237 -19.70343 1.000 39.11091 ?  518 ASN   A CG  1 
ATOM   3432 O  OD1 . ASN   A 1 441 ? -17.33595 -26.79231 -20.50403 1.000 41.75327 ?  518 ASN   A OD1 1 
ATOM   3433 N  ND2 . ASN   A 1 441 ? -16.50022 -26.48620 -18.44232 1.000 35.16113 ?  518 ASN   A ND2 1 
ATOM   3434 N  N   . LEU   A 1 442 ? -13.49364 -30.74326 -20.65108 1.000 31.07843 ?  519 LEU   A N   1 
ATOM   3435 C  CA  . LEU   A 1 442 ? -12.26697 -31.27971 -21.22499 1.000 34.11411 ?  519 LEU   A CA  1 
ATOM   3436 C  C   . LEU   A 1 442 ? -12.44466 -31.55017 -22.71863 1.000 31.69108 ?  519 LEU   A C   1 
ATOM   3437 O  O   . LEU   A 1 442 ? -13.31750 -32.31722 -23.13260 1.000 32.98177 ?  519 LEU   A O   1 
ATOM   3438 C  CB  . LEU   A 1 442 ? -11.84845 -32.55338 -20.49126 1.000 29.74425 ?  519 LEU   A CB  1 
ATOM   3439 C  CG  . LEU   A 1 442 ? -10.50093 -33.13186 -20.91724 1.000 29.72839 ?  519 LEU   A CG  1 
ATOM   3440 C  CD1 . LEU   A 1 442 ? -9.37074  -32.15785 -20.60476 1.000 29.73025 ?  519 LEU   A CD1 1 
ATOM   3441 C  CD2 . LEU   A 1 442 ? -10.26705 -34.46767 -20.21527 1.000 32.73453 ?  519 LEU   A CD2 1 
ATOM   3442 N  N   . GLU   A 1 443 ? -11.61403 -30.91897 -23.53220 1.000 32.26081 ?  520 GLU   A N   1 
ATOM   3443 C  CA  . GLU   A 1 443 ? -11.64990 -31.14197 -24.96709 1.000 32.17565 ?  520 GLU   A CA  1 
ATOM   3444 C  C   . GLU   A 1 443 ? -10.43815 -31.87679 -25.47950 1.000 31.29951 ?  520 GLU   A C   1 
ATOM   3445 O  O   . GLU   A 1 443 ? -10.55964 -32.66036 -26.42316 1.000 32.85692 ?  520 GLU   A O   1 
ATOM   3446 C  CB  . GLU   A 1 443 ? -11.76623 -29.80700 -25.71081 1.000 32.81826 ?  520 GLU   A CB  1 
ATOM   3447 C  CG  . GLU   A 1 443 ? -12.97382 -28.97052 -25.25530 1.000 38.04056 ?  520 GLU   A CG  1 
ATOM   3448 C  CD  . GLU   A 1 443 ? -12.96488 -27.57272 -25.83199 1.000 44.49054 ?  520 GLU   A CD  1 
ATOM   3449 O  OE1 . GLU   A 1 443 ? -12.15577 -27.32637 -26.75381 1.000 50.31763 ?  520 GLU   A OE1 1 
ATOM   3450 O  OE2 . GLU   A 1 443 ? -13.75914 -26.72488 -25.36435 1.000 45.86369 ?  520 GLU   A OE2 1 
ATOM   3451 N  N   . GLU   A 1 444 ? -9.28104  -31.64815 -24.86997 1.000 29.70904 ?  521 GLU   A N   1 
ATOM   3452 C  CA  . GLU   A 1 444 ? -8.01982  -32.16520 -25.36521 1.000 28.91868 ?  521 GLU   A CA  1 
ATOM   3453 C  C   . GLU   A 1 444 ? -7.30029  -32.83856 -24.21267 1.000 31.03390 ?  521 GLU   A C   1 
ATOM   3454 O  O   . GLU   A 1 444 ? -7.04077  -32.20853 -23.18301 1.000 28.99599 ?  521 GLU   A O   1 
ATOM   3455 C  CB  . GLU   A 1 444 ? -7.17620  -31.04685 -25.96982 1.000 31.04916 ?  521 GLU   A CB  1 
ATOM   3456 C  CG  . GLU   A 1 444 ? -8.03420  -30.02953 -26.71464 1.000 35.41363 ?  521 GLU   A CG  1 
ATOM   3457 C  CD  . GLU   A 1 444 ? -7.23970  -28.88139 -27.29650 1.000 41.62837 ?  521 GLU   A CD  1 
ATOM   3458 O  OE1 . GLU   A 1 444 ? -5.99427  -28.99522 -27.37425 1.000 42.53118 ?  521 GLU   A OE1 1 
ATOM   3459 O  OE2 . GLU   A 1 444 ? -7.86729  -27.86485 -27.68257 1.000 50.79797 ?  521 GLU   A OE2 1 
ATOM   3460 N  N   . LEU   A 1 445 ? -7.00180  -34.12480 -24.38399 1.000 31.63903 ?  522 LEU   A N   1 
ATOM   3461 C  CA  . LEU   A 1 445 ? -6.25659  -34.90738 -23.41192 1.000 28.98160 ?  522 LEU   A CA  1 
ATOM   3462 C  C   . LEU   A 1 445 ? -5.09490  -35.56303 -24.14720 1.000 31.84441 ?  522 LEU   A C   1 
ATOM   3463 O  O   . LEU   A 1 445 ? -5.31183  -36.41450 -25.01787 1.000 33.22666 ?  522 LEU   A O   1 
ATOM   3464 C  CB  . LEU   A 1 445 ? -7.16942  -35.94235 -22.76525 1.000 29.43574 ?  522 LEU   A CB  1 
ATOM   3465 C  CG  . LEU   A 1 445 ? -6.55358  -36.92503 -21.77387 1.000 28.71043 ?  522 LEU   A CG  1 
ATOM   3466 C  CD1 . LEU   A 1 445 ? -5.90334  -36.13846 -20.65837 1.000 27.67457 ?  522 LEU   A CD1 1 
ATOM   3467 C  CD2 . LEU   A 1 445 ? -7.63585  -37.84290 -21.23500 1.000 25.15584 ?  522 LEU   A CD2 1 
ATOM   3468 N  N   . TYR   A 1 446 ? -3.86589  -35.16661 -23.83027 1.000 26.91184 ?  523 TYR   A N   1 
ATOM   3469 C  CA  . TYR   A 1 446 ? -2.70137  -35.77249 -24.46332 1.000 30.68317 ?  523 TYR   A CA  1 
ATOM   3470 C  C   . TYR   A 1 446 ? -2.02867  -36.72193 -23.47786 1.000 30.21497 ?  523 TYR   A C   1 
ATOM   3471 O  O   . TYR   A 1 446 ? -1.53579  -36.29256 -22.42785 1.000 25.99850 ?  523 TYR   A O   1 
ATOM   3472 C  CB  . TYR   A 1 446 ? -1.71858  -34.71986 -24.98193 1.000 27.57720 ?  523 TYR   A CB  1 
ATOM   3473 C  CG  . TYR   A 1 446 ? -2.31849  -33.83293 -26.04269 1.000 28.44139 ?  523 TYR   A CG  1 
ATOM   3474 C  CD1 . TYR   A 1 446 ? -2.26256  -34.17186 -27.39448 1.000 31.31744 ?  523 TYR   A CD1 1 
ATOM   3475 C  CD2 . TYR   A 1 446 ? -2.96129  -32.65613 -25.69389 1.000 30.81726 ?  523 TYR   A CD2 1 
ATOM   3476 C  CE1 . TYR   A 1 446 ? -2.83247  -33.33537 -28.36333 1.000 33.29291 ?  523 TYR   A CE1 1 
ATOM   3477 C  CE2 . TYR   A 1 446 ? -3.52717  -31.83421 -26.64253 1.000 28.82114 ?  523 TYR   A CE2 1 
ATOM   3478 C  CZ  . TYR   A 1 446 ? -3.46124  -32.16745 -27.96221 1.000 30.46637 ?  523 TYR   A CZ  1 
ATOM   3479 O  OH  . TYR   A 1 446 ? -4.03913  -31.31968 -28.87154 1.000 38.49710 ?  523 TYR   A OH  1 
ATOM   3480 N  N   . LEU   A 1 447 ? -2.01168  -38.01320 -23.83201 1.000 30.44164 ?  524 LEU   A N   1 
ATOM   3481 C  CA  . LEU   A 1 447 ? -1.45733  -39.06123 -22.99048 1.000 31.88819 ?  524 LEU   A CA  1 
ATOM   3482 C  C   . LEU   A 1 447 ? -0.30648  -39.79838 -23.65208 1.000 31.00117 ?  524 LEU   A C   1 
ATOM   3483 O  O   . LEU   A 1 447 ? 0.21334   -40.74613 -23.06261 1.000 32.60082 ?  524 LEU   A O   1 
ATOM   3484 C  CB  . LEU   A 1 447 ? -2.55613  -40.06098 -22.58778 1.000 29.67507 ?  524 LEU   A CB  1 
ATOM   3485 C  CG  . LEU   A 1 447 ? -3.64783  -39.52440 -21.64260 1.000 28.12387 ?  524 LEU   A CG  1 
ATOM   3486 C  CD1 . LEU   A 1 447 ? -4.77350  -40.52553 -21.46030 1.000 28.91281 ?  524 LEU   A CD1 1 
ATOM   3487 C  CD2 . LEU   A 1 447 ? -3.04349  -39.13921 -20.29765 1.000 29.88232 ?  524 LEU   A CD2 1 
ATOM   3488 N  N   . ASN   A 1 448 ? 0.12904   -39.36621 -24.83335 1.000 30.41964 ?  525 ASN   A N   1 
ATOM   3489 C  CA  . ASN   A 1 448 ? 1.11995   -40.10797 -25.60111 1.000 29.86555 ?  525 ASN   A CA  1 
ATOM   3490 C  C   . ASN   A 1 448 ? 2.42933   -40.26104 -24.83548 1.000 34.26720 ?  525 ASN   A C   1 
ATOM   3491 O  O   . ASN   A 1 448 ? 2.85662   -39.36947 -24.09315 1.000 32.35700 ?  525 ASN   A O   1 
ATOM   3492 C  CB  . ASN   A 1 448 ? 1.36997   -39.42261 -26.94760 1.000 29.56919 ?  525 ASN   A CB  1 
ATOM   3493 C  CG  . ASN   A 1 448 ? 1.91112   -38.01373 -26.80042 1.000 29.65155 ?  525 ASN   A CG  1 
ATOM   3494 O  OD1 . ASN   A 1 448 ? 1.15332   -37.04690 -26.68262 1.000 27.11595 ?  525 ASN   A OD1 1 
ATOM   3495 N  ND2 . ASN   A 1 448 ? 3.22671   -37.88810 -26.81496 1.000 30.55680 ?  525 ASN   A ND2 1 
ATOM   3496 N  N   . ASP   A 1 449 ? 3.06760   -41.41763 -25.01520 1.000 33.30510 ?  526 ASP   A N   1 
ATOM   3497 C  CA  . ASP   A 1 449 ? 4.38416   -41.67506 -24.44112 1.000 32.20608 ?  526 ASP   A CA  1 
ATOM   3498 C  C   . ASP   A 1 449 ? 4.33470   -41.71847 -22.91945 1.000 31.36508 ?  526 ASP   A C   1 
ATOM   3499 O  O   . ASP   A 1 449 ? 5.11164   -41.05859 -22.23895 1.000 34.38558 ?  526 ASP   A O   1 
ATOM   3500 C  CB  . ASP   A 1 449 ? 5.38403   -40.63875 -24.93486 1.000 31.39474 ?  526 ASP   A CB  1 
ATOM   3501 C  CG  . ASP   A 1 449 ? 5.68439   -40.81778 -26.38495 1.000 35.22911 ?  526 ASP   A CG  1 
ATOM   3502 O  OD1 . ASP   A 1 449 ? 6.18796   -41.90627 -26.73887 1.000 39.27295 ?  526 ASP   A OD1 1 
ATOM   3503 O  OD2 . ASP   A 1 449 ? 5.35600   -39.91547 -27.17811 1.000 36.77002 ?  526 ASP   A OD2 1 
ATOM   3504 N  N   . ASN   A 1 450 ? 3.38273   -42.48959 -22.39500 1.000 35.28418 ?  527 ASN   A N   1 
ATOM   3505 C  CA  . ASN   A 1 450 ? 3.29603   -42.86095 -20.98329 1.000 34.14177 ?  527 ASN   A CA  1 
ATOM   3506 C  C   . ASN   A 1 450 ? 3.45382   -44.37557 -20.91215 1.000 35.02407 ?  527 ASN   A C   1 
ATOM   3507 O  O   . ASN   A 1 450 ? 2.46649   -45.12421 -20.83439 1.000 33.55864 ?  527 ASN   A O   1 
ATOM   3508 C  CB  . ASN   A 1 450 ? 1.98940   -42.39599 -20.35684 1.000 28.03985 ?  527 ASN   A CB  1 
ATOM   3509 C  CG  . ASN   A 1 450 ? 2.09654   -41.00774 -19.82942 1.000 33.11849 ?  527 ASN   A CG  1 
ATOM   3510 O  OD1 . ASN   A 1 450 ? 2.75561   -40.77953 -18.80574 1.000 28.88501 ?  527 ASN   A OD1 1 
ATOM   3511 N  ND2 . ASN   A 1 450 ? 1.48650   -40.04728 -20.53652 1.000 29.37422 ?  527 ASN   A ND2 1 
ATOM   3512 N  N   . PRO   A 1 451 ? 4.69320   -44.85961 -20.93637 1.000 35.32853 ?  528 PRO   A N   1 
ATOM   3513 C  CA  . PRO   A 1 451 ? 4.92717   -46.30966 -21.09488 1.000 36.41053 ?  528 PRO   A CA  1 
ATOM   3514 C  C   . PRO   A 1 451 ? 4.42752   -47.14998 -19.93602 1.000 36.02811 ?  528 PRO   A C   1 
ATOM   3515 O  O   . PRO   A 1 451 ? 4.42521   -48.38217 -20.04734 1.000 33.50595 ?  528 PRO   A O   1 
ATOM   3516 C  CB  . PRO   A 1 451 ? 6.45101   -46.41040 -21.23004 1.000 36.48737 ?  528 PRO   A CB  1 
ATOM   3517 C  CG  . PRO   A 1 451 ? 6.99233   -45.07268 -20.67338 1.000 40.20077 ?  528 PRO   A CG  1 
ATOM   3518 C  CD  . PRO   A 1 451 ? 5.92784   -44.05238 -20.91503 1.000 33.58849 ?  528 PRO   A CD  1 
ATOM   3519 N  N   . ASN   A 1 452 ? 4.00788   -46.53788 -18.83261 1.000 35.66540 ?  529 ASN   A N   1 
ATOM   3520 C  CA  . ASN   A 1 452 ? 3.52842   -47.27810 -17.67527 1.000 33.49997 ?  529 ASN   A CA  1 
ATOM   3521 C  C   . ASN   A 1 452 ? 2.02061   -47.17881 -17.49389 1.000 35.01683 ?  529 ASN   A C   1 
ATOM   3522 O  O   . ASN   A 1 452 ? 1.50179   -47.67813 -16.49387 1.000 36.50505 ?  529 ASN   A O   1 
ATOM   3523 C  CB  . ASN   A 1 452 ? 4.23405   -46.79748 -16.40182 1.000 35.53188 ?  529 ASN   A CB  1 
ATOM   3524 C  CG  . ASN   A 1 452 ? 5.69162   -47.25737 -16.32472 1.000 38.50251 ?  529 ASN   A CG  1 
ATOM   3525 O  OD1 . ASN   A 1 452 ? 6.05957   -48.28392 -16.88853 1.000 36.09281 ?  529 ASN   A OD1 1 
ATOM   3526 N  ND2 . ASN   A 1 452 ? 6.52573   -46.48257 -15.63474 1.000 39.54287 ?  529 ASN   A ND2 1 
ATOM   3527 N  N   . LEU   A 1 453 ? 1.30030   -46.55985 -18.43125 1.000 33.94886 ?  530 LEU   A N   1 
ATOM   3528 C  CA  . LEU   A 1 453 ? -0.13991  -46.34062 -18.28093 1.000 34.38890 ?  530 LEU   A CA  1 
ATOM   3529 C  C   . LEU   A 1 453 ? -0.87530  -47.55299 -18.85252 1.000 35.39168 ?  530 LEU   A C   1 
ATOM   3530 O  O   . LEU   A 1 453 ? -1.00674  -47.69758 -20.06816 1.000 36.23712 ?  530 LEU   A O   1 
ATOM   3531 C  CB  . LEU   A 1 453 ? -0.54657  -45.03855 -18.96805 1.000 34.47590 ?  530 LEU   A CB  1 
ATOM   3532 C  CG  . LEU   A 1 453 ? -2.01136  -44.60382 -18.98410 1.000 32.97044 ?  530 LEU   A CG  1 
ATOM   3533 C  CD1 . LEU   A 1 453 ? -2.52332  -44.32204 -17.58346 1.000 32.24347 ?  530 LEU   A CD1 1 
ATOM   3534 C  CD2 . LEU   A 1 453 ? -2.18245  -43.40332 -19.86588 1.000 31.65624 ?  530 LEU   A CD2 1 
ATOM   3535 N  N   . HIS   A 1 454 ? -1.35109  -48.44107 -17.97874 1.000 36.81628 ?  531 HIS   A N   1 
ATOM   3536 C  CA  . HIS   A 1 454 ? -2.03764  -49.64986 -18.41741 1.000 34.37023 ?  531 HIS   A CA  1 
ATOM   3537 C  C   . HIS   A 1 454 ? -3.54617  -49.56384 -18.29589 1.000 34.82757 ?  531 HIS   A C   1 
ATOM   3538 O  O   . HIS   A 1 454 ? -4.23685  -50.49241 -18.72069 1.000 35.96428 ?  531 HIS   A O   1 
ATOM   3539 C  CB  . HIS   A 1 454 ? -1.53326  -50.85531 -17.63187 1.000 37.62388 ?  531 HIS   A CB  1 
ATOM   3540 C  CG  . HIS   A 1 454 ? -0.10598  -51.17835 -17.90825 1.000 35.78509 ?  531 HIS   A CG  1 
ATOM   3541 N  ND1 . HIS   A 1 454 ? 0.28061   -51.97303 -18.96536 1.000 37.44366 ?  531 HIS   A ND1 1 
ATOM   3542 C  CD2 . HIS   A 1 454 ? 1.03364   -50.78030 -17.29665 1.000 33.51081 ?  531 HIS   A CD2 1 
ATOM   3543 C  CE1 . HIS   A 1 454 ? 1.59908   -52.06843 -18.98115 1.000 36.37184 ?  531 HIS   A CE1 1 
ATOM   3544 N  NE2 . HIS   A 1 454 ? 2.08038   -51.35603 -17.97848 1.000 36.37371 ?  531 HIS   A NE2 1 
ATOM   3545 N  N   . SER   A 1 455 ? -4.06868  -48.47136 -17.74159 1.000 38.34927 ?  532 SER   A N   1 
ATOM   3546 C  CA  . SER   A 1 455 ? -5.49443  -48.30411 -17.50731 1.000 37.65056 ?  532 SER   A CA  1 
ATOM   3547 C  C   . SER   A 1 455 ? -5.93908  -46.90350 -17.89501 1.000 36.60406 ?  532 SER   A C   1 
ATOM   3548 O  O   . SER   A 1 455 ? -5.17389  -45.93893 -17.82498 1.000 38.86541 ?  532 SER   A O   1 
ATOM   3549 C  CB  . SER   A 1 455 ? -5.86692  -48.52801 -16.03520 1.000 38.73462 ?  532 SER   A CB  1 
ATOM   3550 O  OG  . SER   A 1 455 ? -6.23559  -49.86657 -15.81623 1.000 47.38152 ?  532 SER   A OG  1 
ATOM   3551 N  N   . LEU   A 1 456 ? -7.19440  -46.81430 -18.30085 1.000 33.53044 ?  533 LEU   A N   1 
ATOM   3552 C  CA  . LEU   A 1 456 ? -7.95270  -45.59841 -18.37767 1.000 32.55226 ?  533 LEU   A CA  1 
ATOM   3553 C  C   . LEU   A 1 456 ? -9.20232  -45.78269 -17.53022 1.000 35.99218 ?  533 LEU   A C   1 
ATOM   3554 O  O   . LEU   A 1 456 ? -9.82121  -46.84692 -17.59273 1.000 30.42620 ?  533 LEU   A O   1 
ATOM   3555 C  CB  . LEU   A 1 456 ? -8.35047  -45.29143 -19.82444 1.000 31.52462 ?  533 LEU   A CB  1 
ATOM   3556 C  CG  . LEU   A 1 456 ? -7.57418  -44.32277 -20.71172 1.000 34.45445 ?  533 LEU   A CG  1 
ATOM   3557 C  CD1 . LEU   A 1 456 ? -6.18085  -44.07350 -20.20953 1.000 33.11189 ?  533 LEU   A CD1 1 
ATOM   3558 C  CD2 . LEU   A 1 456 ? -7.55494  -44.84384 -22.15521 1.000 32.30331 ?  533 LEU   A CD2 1 
ATOM   3559 N  N   . PRO   A 1 457 ? -9.59384  -44.79826 -16.72198 1.000 36.17693 ?  534 PRO   A N   1 
ATOM   3560 C  CA  . PRO   A 1 457 ? -10.80778 -44.96871 -15.92420 1.000 33.27359 ?  534 PRO   A CA  1 
ATOM   3561 C  C   . PRO   A 1 457 ? -12.04262 -44.90764 -16.80070 1.000 31.82888 ?  534 PRO   A C   1 
ATOM   3562 O  O   . PRO   A 1 457 ? -12.10065 -44.18321 -17.79638 1.000 29.69307 ?  534 PRO   A O   1 
ATOM   3563 C  CB  . PRO   A 1 457 ? -10.76427 -43.79072 -14.94860 1.000 34.21536 ?  534 PRO   A CB  1 
ATOM   3564 C  CG  . PRO   A 1 457 ? -10.02566 -42.73999 -15.68881 1.000 34.74524 ?  534 PRO   A CG  1 
ATOM   3565 C  CD  . PRO   A 1 457 ? -9.01825  -43.45083 -16.56733 1.000 33.27667 ?  534 PRO   A CD  1 
ATOM   3566 N  N   . PHE   A 1 458 ? -13.05383 -45.66808 -16.39528 1.000 33.03092 ?  535 PHE   A N   1 
ATOM   3567 C  CA  . PHE   A 1 458 ? -14.32833 -45.63428 -17.10095 1.000 32.97902 ?  535 PHE   A CA  1 
ATOM   3568 C  C   . PHE   A 1 458 ? -14.96661 -44.24494 -17.09655 1.000 33.56073 ?  535 PHE   A C   1 
ATOM   3569 O  O   . PHE   A 1 458 ? -15.69625 -43.90176 -18.03725 1.000 33.17271 ?  535 PHE   A O   1 
ATOM   3570 C  CB  . PHE   A 1 458 ? -15.26553 -46.66203 -16.48195 1.000 33.65245 ?  535 PHE   A CB  1 
ATOM   3571 C  CG  . PHE   A 1 458 ? -15.07193 -48.04646 -17.02240 1.000 34.36217 ?  535 PHE   A CG  1 
ATOM   3572 C  CD1 . PHE   A 1 458 ? -15.20806 -48.29359 -18.37286 1.000 33.89357 ?  535 PHE   A CD1 1 
ATOM   3573 C  CD2 . PHE   A 1 458 ? -14.78008 -49.09490 -16.18912 1.000 35.76736 ?  535 PHE   A CD2 1 
ATOM   3574 C  CE1 . PHE   A 1 458 ? -15.04525 -49.55279 -18.87859 1.000 33.85491 ?  535 PHE   A CE1 1 
ATOM   3575 C  CE2 . PHE   A 1 458 ? -14.62408 -50.37118 -16.69875 1.000 36.56653 ?  535 PHE   A CE2 1 
ATOM   3576 C  CZ  . PHE   A 1 458 ? -14.75448 -50.59449 -18.04288 1.000 30.91036 ?  535 PHE   A CZ  1 
ATOM   3577 N  N   . GLU   A 1 459 ? -14.72705 -43.43376 -16.05206 1.000 34.29323 ?  536 GLU   A N   1 
ATOM   3578 C  CA  . GLU   A 1 459 ? -15.38501 -42.12729 -15.99186 1.000 34.28612 ?  536 GLU   A CA  1 
ATOM   3579 C  C   . GLU   A 1 459 ? -14.90068 -41.16954 -17.07186 1.000 32.32826 ?  536 GLU   A C   1 
ATOM   3580 O  O   . GLU   A 1 459 ? -15.52234 -40.11732 -17.26027 1.000 31.59828 ?  536 GLU   A O   1 
ATOM   3581 C  CB  . GLU   A 1 459 ? -15.21775 -41.46107 -14.62173 1.000 30.72886 ?  536 GLU   A CB  1 
ATOM   3582 C  CG  . GLU   A 1 459 ? -14.21781 -42.09612 -13.73056 1.000 39.72754 ?  536 GLU   A CG  1 
ATOM   3583 C  CD  . GLU   A 1 459 ? -14.71132 -43.39126 -13.11925 1.000 39.87721 ?  536 GLU   A CD  1 
ATOM   3584 O  OE1 . GLU   A 1 459 ? -15.84030 -43.41244 -12.58819 1.000 39.68959 ?  536 GLU   A OE1 1 
ATOM   3585 O  OE2 . GLU   A 1 459 ? -13.95855 -44.38536 -13.17250 1.000 41.09002 ?  536 GLU   A OE2 1 
ATOM   3586 N  N   . LEU   A 1 460 ? -13.82133 -41.50173 -17.78276 1.000 32.09128 ?  537 LEU   A N   1 
ATOM   3587 C  CA  . LEU   A 1 460 ? -13.45036 -40.71397 -18.95134 1.000 31.68892 ?  537 LEU   A CA  1 
ATOM   3588 C  C   . LEU   A 1 460 ? -14.57955 -40.67450 -19.97419 1.000 32.50347 ?  537 LEU   A C   1 
ATOM   3589 O  O   . LEU   A 1 460 ? -14.62882 -39.75579 -20.80081 1.000 32.30163 ?  537 LEU   A O   1 
ATOM   3590 C  CB  . LEU   A 1 460 ? -12.16286 -41.27692 -19.56915 1.000 33.42554 ?  537 LEU   A CB  1 
ATOM   3591 C  CG  . LEU   A 1 460 ? -11.36418 -40.43804 -20.57890 1.000 38.28701 ?  537 LEU   A CG  1 
ATOM   3592 C  CD1 . LEU   A 1 460 ? -11.12815 -39.00864 -20.04497 1.000 30.64745 ?  537 LEU   A CD1 1 
ATOM   3593 C  CD2 . LEU   A 1 460 ? -10.03938 -41.12758 -20.93380 1.000 28.83154 ?  537 LEU   A CD2 1 
ATOM   3594 N  N   . ALA   A 1 461 ? -15.50337 -41.63870 -19.92456 1.000 31.69230 ?  538 ALA   A N   1 
ATOM   3595 C  CA  . ALA   A 1 461 ? -16.69619 -41.56954 -20.77117 1.000 35.21551 ?  538 ALA   A CA  1 
ATOM   3596 C  C   . ALA   A 1 461 ? -17.60365 -40.39897 -20.40135 1.000 32.06671 ?  538 ALA   A C   1 
ATOM   3597 O  O   . ALA   A 1 461 ? -18.43012 -39.98546 -21.21732 1.000 31.35746 ?  538 ALA   A O   1 
ATOM   3598 C  CB  . ALA   A 1 461 ? -17.48286 -42.88433 -20.68404 1.000 32.82862 ?  538 ALA   A CB  1 
ATOM   3599 N  N   . LEU   A 1 462 ? -17.47996 -39.86791 -19.18810 1.000 31.79984 ?  539 LEU   A N   1 
ATOM   3600 C  CA  . LEU   A 1 462 ? -18.29038 -38.74027 -18.76079 1.000 34.11710 ?  539 LEU   A CA  1 
ATOM   3601 C  C   . LEU   A 1 462 ? -17.80854 -37.41857 -19.33567 1.000 34.46261 ?  539 LEU   A C   1 
ATOM   3602 O  O   . LEU   A 1 462 ? -18.44837 -36.39607 -19.08071 1.000 32.73085 ?  539 LEU   A O   1 
ATOM   3603 C  CB  . LEU   A 1 462 ? -18.30858 -38.63925 -17.23360 1.000 30.66499 ?  539 LEU   A CB  1 
ATOM   3604 C  CG  . LEU   A 1 462 ? -18.85449 -39.82555 -16.43788 1.000 33.28174 ?  539 LEU   A CG  1 
ATOM   3605 C  CD1 . LEU   A 1 462 ? -18.70743 -39.55427 -14.95014 1.000 30.83761 ?  539 LEU   A CD1 1 
ATOM   3606 C  CD2 . LEU   A 1 462 ? -20.30065 -40.09926 -16.80768 1.000 27.42861 ?  539 LEU   A CD2 1 
ATOM   3607 N  N   . CYS   A 1 463 ? -16.70374 -37.40868 -20.09114 1.000 33.91626 ?  540 CYS   A N   1 
ATOM   3608 C  CA  . CYS   A 1 463 ? -16.14671 -36.16994 -20.64256 1.000 31.22215 ?  540 CYS   A CA  1 
ATOM   3609 C  C   . CYS   A 1 463 ? -16.75335 -35.93810 -22.01890 1.000 33.60761 ?  540 CYS   A C   1 
ATOM   3610 O  O   . CYS   A 1 463 ? -16.16822 -36.23394 -23.06201 1.000 36.58103 ?  540 CYS   A O   1 
ATOM   3611 C  CB  . CYS   A 1 463 ? -14.62738 -36.23343 -20.68933 1.000 29.37897 ?  540 CYS   A CB  1 
ATOM   3612 S  SG  . CYS   A 1 463 ? -13.87979 -36.35792 -19.04407 1.000 34.43619 ?  540 CYS   A SG  1 
ATOM   3613 N  N   . SER   A 1 464 ? -17.95062 -35.36472 -22.00880 1.000 33.52021 ?  541 SER   A N   1 
ATOM   3614 C  CA  . SER   A 1 464 ? -18.76615 -35.27605 -23.21055 1.000 35.65014 ?  541 SER   A CA  1 
ATOM   3615 C  C   . SER   A 1 464 ? -18.24237 -34.27507 -24.23947 1.000 35.81211 ?  541 SER   A C   1 
ATOM   3616 O  O   . SER   A 1 464 ? -18.75412 -34.24968 -25.36298 1.000 37.08437 ?  541 SER   A O   1 
ATOM   3617 C  CB  . SER   A 1 464 ? -20.18736 -34.90775 -22.81044 1.000 35.81881 ?  541 SER   A CB  1 
ATOM   3618 O  OG  . SER   A 1 464 ? -20.16766 -33.66554 -22.13244 1.000 39.87795 ?  541 SER   A OG  1 
ATOM   3619 N  N   . LYS   A 1 465 ? -17.25695 -33.44651 -23.90484 1.000 34.86951 ?  542 LYS   A N   1 
ATOM   3620 C  CA  . LYS   A 1 465 ? -16.66758 -32.55838 -24.89983 1.000 32.99744 ?  542 LYS   A CA  1 
ATOM   3621 C  C   . LYS   A 1 465 ? -15.31626 -33.05030 -25.39877 1.000 30.42379 ?  542 LYS   A C   1 
ATOM   3622 O  O   . LYS   A 1 465 ? -14.68100 -32.36571 -26.20464 1.000 30.23179 ?  542 LYS   A O   1 
ATOM   3623 C  CB  . LYS   A 1 465 ? -16.54444 -31.13878 -24.33969 1.000 31.71466 ?  542 LYS   A CB  1 
ATOM   3624 C  CG  . LYS   A 1 465 ? -17.86780 -30.52405 -23.92912 1.000 36.41976 ?  542 LYS   A CG  1 
ATOM   3625 C  CD  . LYS   A 1 465 ? -17.86085 -29.00545 -24.15501 1.000 42.13079 ?  542 LYS   A CD  1 
ATOM   3626 C  CE  . LYS   A 1 465 ? -18.20931 -28.22302 -22.89990 1.000 40.48829 ?  542 LYS   A CE  1 
ATOM   3627 N  NZ  . LYS   A 1 465 ? -19.55461 -28.60575 -22.35498 1.000 48.00800 ?  542 LYS   A NZ  1 
ATOM   3628 N  N   . LEU   A 1 466 ? -14.88498 -34.23791 -24.96745 1.000 35.39111 ?  543 LEU   A N   1 
ATOM   3629 C  CA  . LEU   A 1 466 ? -13.57712 -34.77370 -25.32966 1.000 31.81016 ?  543 LEU   A CA  1 
ATOM   3630 C  C   . LEU   A 1 466 ? -13.56497 -35.13309 -26.80781 1.000 30.41560 ?  543 LEU   A C   1 
ATOM   3631 O  O   . LEU   A 1 466 ? -14.20502 -36.10946 -27.21493 1.000 34.35692 ?  543 LEU   A O   1 
ATOM   3632 C  CB  . LEU   A 1 466 ? -13.24728 -35.98936 -24.46921 1.000 30.08708 ?  543 LEU   A CB  1 
ATOM   3633 C  CG  . LEU   A 1 466 ? -11.82329 -36.54823 -24.62685 1.000 31.91161 ?  543 LEU   A CG  1 
ATOM   3634 C  CD1 . LEU   A 1 466 ? -10.79152 -35.49446 -24.27289 1.000 30.63495 ?  543 LEU   A CD1 1 
ATOM   3635 C  CD2 . LEU   A 1 466 ? -11.58525 -37.81940 -23.80751 1.000 29.83285 ?  543 LEU   A CD2 1 
ATOM   3636 N  N   . SER   A 1 467 ? -12.82818 -34.34857 -27.61161 1.000 29.79817 ?  544 SER   A N   1 
ATOM   3637 C  CA  . SER   A 1 467 ? -12.68580 -34.59536 -29.04392 1.000 32.63169 ?  544 SER   A CA  1 
ATOM   3638 C  C   . SER   A 1 467 ? -11.26086 -34.90719 -29.48416 1.000 32.17152 ?  544 SER   A C   1 
ATOM   3639 O  O   . SER   A 1 467 ? -11.07620 -35.41878 -30.59017 1.000 35.47772 ?  544 SER   A O   1 
ATOM   3640 C  CB  . SER   A 1 467 ? -13.20836 -33.39393 -29.85338 1.000 33.22734 ?  544 SER   A CB  1 
ATOM   3641 O  OG  . SER   A 1 467 ? -12.54372 -32.19227 -29.49782 1.000 35.57517 ?  544 SER   A OG  1 
ATOM   3642 N  N   . ILE   A 1 468 ? -10.25894 -34.64945 -28.65005 1.000 32.59256 ?  545 ILE   A N   1 
ATOM   3643 C  CA  . ILE   A 1 468 ? -8.86244  -34.91610 -28.96691 1.000 30.87678 ?  545 ILE   A CA  1 
ATOM   3644 C  C   . ILE   A 1 468 ? -8.25540  -35.73076 -27.83767 1.000 29.98871 ?  545 ILE   A C   1 
ATOM   3645 O  O   . ILE   A 1 468 ? -8.34336  -35.34529 -26.66898 1.000 30.68545 ?  545 ILE   A O   1 
ATOM   3646 C  CB  . ILE   A 1 468 ? -8.05362  -33.61963 -29.15568 1.000 31.72882 ?  545 ILE   A CB  1 
ATOM   3647 C  CG1 . ILE   A 1 468 ? -8.41399  -32.93359 -30.47165 1.000 32.91024 ?  545 ILE   A CG1 1 
ATOM   3648 C  CG2 . ILE   A 1 468 ? -6.55860  -33.91639 -29.06089 1.000 29.89926 ?  545 ILE   A CG2 1 
ATOM   3649 C  CD1 . ILE   A 1 468 ? -8.01221  -31.44868 -30.51488 1.000 33.35014 ?  545 ILE   A CD1 1 
ATOM   3650 N  N   . MET   A 1 469 ? -7.60562  -36.82929 -28.18879 1.000 33.85247 ?  546 MET   A N   1 
ATOM   3651 C  CA  . MET   A 1 469 ? -6.84697  -37.62104 -27.23204 1.000 35.30825 ?  546 MET   A CA  1 
ATOM   3652 C  C   . MET   A 1 469 ? -5.72221  -38.30560 -27.99530 1.000 35.39947 ?  546 MET   A C   1 
ATOM   3653 O  O   . MET   A 1 469 ? -5.93883  -38.81393 -29.10006 1.000 37.57178 ?  546 MET   A O   1 
ATOM   3654 C  CB  . MET   A 1 469 ? -7.73932  -38.65286 -26.51525 1.000 35.34164 ?  546 MET   A CB  1 
ATOM   3655 C  CG  . MET   A 1 469 ? -7.02847  -39.46064 -25.43556 1.000 37.30778 ?  546 MET   A CG  1 
ATOM   3656 S  SD  . MET   A 1 469 ? -8.03466  -40.70749 -24.57100 1.000 43.30216 ?  546 MET   A SD  1 
ATOM   3657 C  CE  . MET   A 1 469 ? -8.28152  -41.93130 -25.86133 1.000 34.60386 ?  546 MET   A CE  1 
ATOM   3658 N  N   . SER   A 1 470 ? -4.52175  -38.29318 -27.42860 1.000 34.33615 ?  547 SER   A N   1 
ATOM   3659 C  CA  . SER   A 1 470 ? -3.43661  -39.12446 -27.93405 1.000 36.20621 ?  547 SER   A CA  1 
ATOM   3660 C  C   . SER   A 1 470 ? -3.08050  -40.14838 -26.87159 1.000 32.94566 ?  547 SER   A C   1 
ATOM   3661 O  O   . SER   A 1 470 ? -3.12449  -39.84752 -25.67532 1.000 31.99610 ?  547 SER   A O   1 
ATOM   3662 C  CB  . SER   A 1 470 ? -2.20532  -38.29831 -28.30188 1.000 31.29687 ?  547 SER   A CB  1 
ATOM   3663 O  OG  . SER   A 1 470 ? -1.70122  -37.64001 -27.15254 1.000 31.64295 ?  547 SER   A OG  1 
ATOM   3664 N  N   . ILE   A 1 471 ? -2.75881  -41.36480 -27.31250 1.000 37.17710 ?  548 ILE   A N   1 
ATOM   3665 C  CA  . ILE   A 1 471 ? -2.37132  -42.43895 -26.40357 1.000 36.77306 ?  548 ILE   A CA  1 
ATOM   3666 C  C   . ILE   A 1 471 ? -1.31123  -43.30980 -27.05920 1.000 35.59699 ?  548 ILE   A C   1 
ATOM   3667 O  O   . ILE   A 1 471 ? -1.08323  -44.44693 -26.63221 1.000 35.56483 ?  548 ILE   A O   1 
ATOM   3668 C  CB  . ILE   A 1 471 ? -3.57634  -43.29537 -25.97230 1.000 33.10716 ?  548 ILE   A CB  1 
ATOM   3669 C  CG1 . ILE   A 1 471 ? -4.55432  -43.44217 -27.13374 1.000 36.52752 ?  548 ILE   A CG1 1 
ATOM   3670 C  CG2 . ILE   A 1 471 ? -4.21038  -42.76119 -24.68053 1.000 33.54745 ?  548 ILE   A CG2 1 
ATOM   3671 C  CD1 . ILE   A 1 471 ? -3.98734  -44.25339 -28.30684 1.000 34.29032 ?  548 ILE   A CD1 1 
ATOM   3672 N  N   . GLU   A 1 472 ? -0.65255  -42.78793 -28.08778 1.000 33.42929 ?  549 GLU   A N   1 
ATOM   3673 C  CA  . GLU   A 1 472 ? 0.42163   -43.53741 -28.73008 1.000 38.28287 ?  549 GLU   A CA  1 
ATOM   3674 C  C   . GLU   A 1 472 ? 1.50845   -43.90085 -27.72552 1.000 38.73176 ?  549 GLU   A C   1 
ATOM   3675 O  O   . GLU   A 1 472 ? 1.92805   -43.07017 -26.91758 1.000 38.85986 ?  549 GLU   A O   1 
ATOM   3676 C  CB  . GLU   A 1 472 ? 1.01709   -42.71949 -29.86597 1.000 39.19466 ?  549 GLU   A CB  1 
ATOM   3677 C  CG  . GLU   A 1 472 ? 2.17498   -43.38680 -30.57016 1.000 43.63058 ?  549 GLU   A CG  1 
ATOM   3678 C  CD  . GLU   A 1 472 ? 2.75365   -42.50546 -31.66383 1.000 49.51631 ?  549 GLU   A CD  1 
ATOM   3679 O  OE1 . GLU   A 1 472 ? 3.22528   -41.38691 -31.34170 1.000 49.89404 ?  549 GLU   A OE1 1 
ATOM   3680 O  OE2 . GLU   A 1 472 ? 2.71401   -42.92018 -32.84393 1.000 48.49163 ?  549 GLU   A OE2 1 
ATOM   3681 N  N   . ASN   A 1 473 ? 1.95783   -45.15269 -27.77199 1.000 42.57882 ?  550 ASN   A N   1 
ATOM   3682 C  CA  . ASN   A 1 473 ? 3.05061   -45.64795 -26.92872 1.000 43.49654 ?  550 ASN   A CA  1 
ATOM   3683 C  C   . ASN   A 1 473 ? 2.64839   -45.74761 -25.45788 1.000 41.20262 ?  550 ASN   A C   1 
ATOM   3684 O  O   . ASN   A 1 473 ? 3.48564   -45.60910 -24.56683 1.000 41.39212 ?  550 ASN   A O   1 
ATOM   3685 C  CB  . ASN   A 1 473 ? 4.31559   -44.79258 -27.08042 1.000 41.47683 ?  550 ASN   A CB  1 
ATOM   3686 C  CG  . ASN   A 1 473 ? 4.99288   -44.97406 -28.43746 1.000 46.90763 ?  550 ASN   A CG  1 
ATOM   3687 O  OD1 . ASN   A 1 473 ? 4.97004   -46.06171 -29.01988 1.000 54.28681 ?  550 ASN   A OD1 1 
ATOM   3688 N  ND2 . ASN   A 1 473 ? 5.60113   -43.90455 -28.94395 1.000 45.54072 ?  550 ASN   A ND2 1 
ATOM   3689 N  N   . CYS   A 1 474 ? 1.36755   -45.96892 -25.19445 1.000 36.97016 ?  551 CYS   A N   1 
ATOM   3690 C  CA  . CYS   A 1 474 ? 0.89998   -46.36307 -23.87946 1.000 35.09427 ?  551 CYS   A CA  1 
ATOM   3691 C  C   . CYS   A 1 474 ? 0.44900   -47.80978 -23.93175 1.000 36.30977 ?  551 CYS   A C   1 
ATOM   3692 O  O   . CYS   A 1 474 ? -0.36537  -48.17005 -24.79600 1.000 39.02312 ?  551 CYS   A O   1 
ATOM   3693 C  CB  . CYS   A 1 474 ? -0.25635  -45.48576 -23.41147 1.000 32.07762 ?  551 CYS   A CB  1 
ATOM   3694 S  SG  . CYS   A 1 474 ? 0.10565   -43.72810 -23.38279 1.000 38.18888 ?  551 CYS   A SG  1 
ATOM   3695 N  N   . PRO   A 1 475 ? 0.94520   -48.65655 -23.03188 1.000 33.71786 ?  552 PRO   A N   1 
ATOM   3696 C  CA  . PRO   A 1 475 ? 0.58977   -50.08645 -23.10135 1.000 32.61620 ?  552 PRO   A CA  1 
ATOM   3697 C  C   . PRO   A 1 475 ? -0.90072  -50.32751 -23.06839 1.000 32.67090 ?  552 PRO   A C   1 
ATOM   3698 O  O   . PRO   A 1 475 ? -1.42506  -51.03251 -23.93165 1.000 33.63379 ?  552 PRO   A O   1 
ATOM   3699 C  CB  . PRO   A 1 475 ? 1.27808   -50.67482 -21.86654 1.000 34.91968 ?  552 PRO   A CB  1 
ATOM   3700 C  CG  . PRO   A 1 475 ? 2.33602   -49.68706 -21.50485 1.000 38.07147 ?  552 PRO   A CG  1 
ATOM   3701 C  CD  . PRO   A 1 475 ? 1.83002   -48.34145 -21.90047 1.000 33.18169 ?  552 PRO   A CD  1 
ATOM   3702 N  N   . LEU   A 1 476 ? -1.59852  -49.74891 -22.08904 1.000 37.02870 ?  553 LEU   A N   1 
ATOM   3703 C  CA  . LEU   A 1 476 ? -3.03870  -49.94446 -21.90281 1.000 36.97211 ?  553 LEU   A CA  1 
ATOM   3704 C  C   . LEU   A 1 476 ? -3.39683  -51.43070 -21.92759 1.000 35.16789 ?  553 LEU   A C   1 
ATOM   3705 O  O   . LEU   A 1 476 ? -4.35060  -51.86014 -22.57624 1.000 35.81437 ?  553 LEU   A O   1 
ATOM   3706 C  CB  . LEU   A 1 476 ? -3.83334  -49.16835 -22.95021 1.000 34.32929 ?  553 LEU   A CB  1 
ATOM   3707 C  CG  . LEU   A 1 476 ? -3.71331  -47.64809 -22.83512 1.000 35.22163 ?  553 LEU   A CG  1 
ATOM   3708 C  CD1 . LEU   A 1 476 ? -4.39866  -46.99237 -24.00181 1.000 28.99478 ?  553 LEU   A CD1 1 
ATOM   3709 C  CD2 . LEU   A 1 476 ? -4.32154  -47.18580 -21.53571 1.000 29.80183 ?  553 LEU   A CD2 1 
ATOM   3710 N  N   . SER   A 1 477 ? -2.62904  -52.22557 -21.18900 1.000 34.86080 ?  554 SER   A N   1 
ATOM   3711 C  CA  . SER   A 1 477 ? -2.77953  -53.67109 -21.30351 1.000 37.36766 ?  554 SER   A CA  1 
ATOM   3712 C  C   . SER   A 1 477 ? -3.92948  -54.23007 -20.47951 1.000 34.68728 ?  554 SER   A C   1 
ATOM   3713 O  O   . SER   A 1 477 ? -4.20383  -55.41979 -20.59827 1.000 39.92191 ?  554 SER   A O   1 
ATOM   3714 C  CB  . SER   A 1 477 ? -1.48292  -54.37550 -20.91504 1.000 33.37320 ?  554 SER   A CB  1 
ATOM   3715 O  OG  . SER   A 1 477 ? -1.16656  -54.14120 -19.55807 1.000 40.12204 ?  554 SER   A OG  1 
ATOM   3716 N  N   . HIS   A 1 478 ? -4.59316  -53.42086 -19.65252 1.000 36.68045 ?  555 HIS   A N   1 
ATOM   3717 C  CA  . HIS   A 1 478 ? -5.87117  -53.78948 -19.04828 1.000 35.96841 ?  555 HIS   A CA  1 
ATOM   3718 C  C   . HIS   A 1 478 ? -7.05618  -53.56877 -19.98619 1.000 36.56898 ?  555 HIS   A C   1 
ATOM   3719 O  O   . HIS   A 1 478 ? -8.19271  -53.86278 -19.61227 1.000 36.34013 ?  555 HIS   A O   1 
ATOM   3720 C  CB  . HIS   A 1 478 ? -6.09777  -52.99395 -17.76058 1.000 38.49173 ?  555 HIS   A CB  1 
ATOM   3721 C  CG  . HIS   A 1 478 ? -5.05759  -53.23451 -16.71240 1.000 43.06804 ?  555 HIS   A CG  1 
ATOM   3722 N  ND1 . HIS   A 1 478 ? -5.06510  -52.58785 -15.49320 1.000 42.08929 ?  555 HIS   A ND1 1 
ATOM   3723 C  CD2 . HIS   A 1 478 ? -3.97479  -54.05029 -16.70139 1.000 40.22693 ?  555 HIS   A CD2 1 
ATOM   3724 C  CE1 . HIS   A 1 478 ? -4.03038  -52.99207 -14.77767 1.000 44.76614 ?  555 HIS   A CE1 1 
ATOM   3725 N  NE2 . HIS   A 1 478 ? -3.35377  -53.88056 -15.48809 1.000 49.16763 ?  555 HIS   A NE2 1 
ATOM   3726 N  N   . LEU   A 1 479 ? -6.83630  -53.05581 -21.13472 1.000 39.71518 ?  556 LEU   A N   1 
ATOM   3727 C  CA  . LEU   A 1 479 ? -7.85130  -52.93544 -22.16669 1.000 39.85791 ?  556 LEU   A CA  1 
ATOM   3728 C  C   . LEU   A 1 479 ? -7.64471  -54.00693 -23.23176 1.000 37.63341 ?  556 LEU   A C   1 
ATOM   3729 O  O   . LEU   A 1 479 ? -6.50979  -54.42822 -23.47813 1.000 39.77524 ?  556 LEU   A O   1 
ATOM   3730 C  CB  . LEU   A 1 479 ? -7.79204  -51.54905 -22.81366 1.000 35.12651 ?  556 LEU   A CB  1 
ATOM   3731 C  CG  . LEU   A 1 479 ? -8.36239  -50.42047 -21.96210 1.000 41.13210 ?  556 LEU   A CG  1 
ATOM   3732 C  CD1 . LEU   A 1 479 ? -7.78032  -49.06360 -22.36197 1.000 36.21721 ?  556 LEU   A CD1 1 
ATOM   3733 C  CD2 . LEU   A 1 479 ? -9.85973  -50.41076 -22.14219 1.000 41.06675 ?  556 LEU   A CD2 1 
ATOM   3734 N  N   . PRO   A 1 480 ? -8.70306  -54.47061 -23.89340 1.000 37.68434 ?  557 PRO   A N   1 
ATOM   3735 C  CA  . PRO   A 1 480 ? -8.53857  -55.51744 -24.91131 1.000 38.73111 ?  557 PRO   A CA  1 
ATOM   3736 C  C   . PRO   A 1 480 ? -7.57542  -55.05698 -25.98861 1.000 40.42052 ?  557 PRO   A C   1 
ATOM   3737 O  O   . PRO   A 1 480 ? -7.68593  -53.92689 -26.48317 1.000 40.23572 ?  557 PRO   A O   1 
ATOM   3738 C  CB  . PRO   A 1 480 ? -9.95826  -55.70123 -25.47304 1.000 35.98785 ?  557 PRO   A CB  1 
ATOM   3739 C  CG  . PRO   A 1 480 ? -10.86288 -55.14584 -24.41514 1.000 38.80097 ?  557 PRO   A CG  1 
ATOM   3740 C  CD  . PRO   A 1 480 ? -10.09975 -54.01819 -23.79041 1.000 38.90809 ?  557 PRO   A CD  1 
ATOM   3741 N  N   . PRO   A 1 481 ? -6.61406  -55.89780 -26.37455 1.000 42.79562 ?  558 PRO   A N   1 
ATOM   3742 C  CA  . PRO   A 1 481 ? -5.62639  -55.46605 -27.37968 1.000 36.31634 ?  558 PRO   A CA  1 
ATOM   3743 C  C   . PRO   A 1 481 ? -6.22388  -54.87324 -28.64665 1.000 38.93430 ?  558 PRO   A C   1 
ATOM   3744 O  O   . PRO   A 1 481 ? -5.68265  -53.87888 -29.14561 1.000 39.19912 ?  558 PRO   A O   1 
ATOM   3745 C  CB  . PRO   A 1 481 ? -4.84079  -56.75173 -27.67240 1.000 35.18723 ?  558 PRO   A CB  1 
ATOM   3746 C  CG  . PRO   A 1 481 ? -4.98096  -57.57938 -26.42725 1.000 40.58943 ?  558 PRO   A CG  1 
ATOM   3747 C  CD  . PRO   A 1 481 ? -6.28722  -57.20654 -25.77461 1.000 40.69032 ?  558 PRO   A CD  1 
ATOM   3748 N  N   . GLN   A 1 482 ? -7.29553  -55.44658 -29.21013 1.000 40.62216 ?  559 GLN   A N   1 
ATOM   3749 C  CA  . GLN   A 1 482 ? -7.77767  -54.90091 -30.47653 1.000 39.96463 ?  559 GLN   A CA  1 
ATOM   3750 C  C   . GLN   A 1 482 ? -8.54014  -53.59751 -30.29297 1.000 37.14759 ?  559 GLN   A C   1 
ATOM   3751 O  O   . GLN   A 1 482 ? -8.62051  -52.80478 -31.23612 1.000 36.15033 ?  559 GLN   A O   1 
ATOM   3752 C  CB  . GLN   A 1 482 ? -8.66151  -55.90592 -31.22527 1.000 41.96017 ?  559 GLN   A CB  1 
ATOM   3753 C  CG  . GLN   A 1 482 ? -9.99689  -56.15059 -30.56623 1.000 43.17211 ?  559 GLN   A CG  1 
ATOM   3754 C  CD  . GLN   A 1 482 ? -11.04049 -56.72149 -31.50881 1.000 41.63990 ?  559 GLN   A CD  1 
ATOM   3755 O  OE1 . GLN   A 1 482 ? -10.73032 -57.27226 -32.57385 1.000 47.35004 ?  559 GLN   A OE1 1 
ATOM   3756 N  NE2 . GLN   A 1 482 ? -12.29566 -56.59838 -31.11335 1.000 40.65935 ?  559 GLN   A NE2 1 
ATOM   3757 N  N   . ILE   A 1 483 ? -9.10498  -53.36107 -29.11060 1.000 38.66451 ?  560 ILE   A N   1 
ATOM   3758 C  CA  . ILE   A 1 483 ? -9.66195  -52.04612 -28.81177 1.000 36.48278 ?  560 ILE   A CA  1 
ATOM   3759 C  C   . ILE   A 1 483 ? -8.56830  -50.98757 -28.89634 1.000 39.54482 ?  560 ILE   A C   1 
ATOM   3760 O  O   . ILE   A 1 483 ? -8.64066  -50.05694 -29.70735 1.000 36.29727 ?  560 ILE   A O   1 
ATOM   3761 C  CB  . ILE   A 1 483 ? -10.33060 -52.03195 -27.42890 1.000 35.41851 ?  560 ILE   A CB  1 
ATOM   3762 C  CG1 . ILE   A 1 483 ? -11.40400 -53.12466 -27.30109 1.000 39.73294 ?  560 ILE   A CG1 1 
ATOM   3763 C  CG2 . ILE   A 1 483 ? -10.89580 -50.63770 -27.14501 1.000 37.40730 ?  560 ILE   A CG2 1 
ATOM   3764 C  CD1 . ILE   A 1 483 ? -12.71556 -52.81979 -27.96119 1.000 34.07438 ?  560 ILE   A CD1 1 
ATOM   3765 N  N   . VAL   A 1 484 ? -7.53079  -51.11523 -28.06027 1.000 36.42174 ?  561 VAL   A N   1 
ATOM   3766 C  CA  . VAL   A 1 484 ? -6.52174  -50.06251 -28.03714 1.000 37.38811 ?  561 VAL   A CA  1 
ATOM   3767 C  C   . VAL   A 1 484 ? -5.74278  -50.01365 -29.34014 1.000 36.35476 ?  561 VAL   A C   1 
ATOM   3768 O  O   . VAL   A 1 484 ? -5.14801  -48.97982 -29.65397 1.000 41.05027 ?  561 VAL   A O   1 
ATOM   3769 C  CB  . VAL   A 1 484 ? -5.56320  -50.18998 -26.83101 1.000 37.79996 ?  561 VAL   A CB  1 
ATOM   3770 C  CG1 . VAL   A 1 484 ? -5.94254  -51.34922 -25.97560 1.000 38.45817 ?  561 VAL   A CG1 1 
ATOM   3771 C  CG2 . VAL   A 1 484 ? -4.11445  -50.29784 -27.28648 1.000 36.76813 ?  561 VAL   A CG2 1 
ATOM   3772 N  N   . ALA   A 1 485 ? -5.74281  -51.09120 -30.12823 1.000 38.80910 ?  562 ALA   A N   1 
ATOM   3773 C  CA  . ALA   A 1 485 ? -5.12327  -51.00936 -31.44651 1.000 38.02979 ?  562 ALA   A CA  1 
ATOM   3774 C  C   . ALA   A 1 485 ? -5.91717  -50.09703 -32.35874 1.000 36.25332 ?  562 ALA   A C   1 
ATOM   3775 O  O   . ALA   A 1 485 ? -5.33818  -49.41951 -33.20802 1.000 40.15906 ?  562 ALA   A O   1 
ATOM   3776 C  CB  . ALA   A 1 485 ? -4.98391  -52.39944 -32.06851 1.000 35.52332 ?  562 ALA   A CB  1 
ATOM   3777 N  N   . GLY   A 1 486 ? -7.23488  -50.04634 -32.18337 1.000 37.60882 ?  563 GLY   A N   1 
ATOM   3778 C  CA  . GLY   A 1 486 ? -8.06703  -49.13279 -32.93884 1.000 33.72617 ?  563 GLY   A CA  1 
ATOM   3779 C  C   . GLY   A 1 486 ? -7.91517  -47.66912 -32.58756 1.000 37.07119 ?  563 GLY   A C   1 
ATOM   3780 O  O   . GLY   A 1 486 ? -8.55006  -46.83295 -33.23805 1.000 40.80761 ?  563 GLY   A O   1 
ATOM   3781 N  N   . GLY   A 1 487 ? -7.12229  -47.32394 -31.57521 1.000 33.91225 ?  564 GLY   A N   1 
ATOM   3782 C  CA  . GLY   A 1 487 ? -6.85457  -45.93607 -31.28540 1.000 34.07048 ?  564 GLY   A CA  1 
ATOM   3783 C  C   . GLY   A 1 487 ? -7.93098  -45.28192 -30.44289 1.000 38.04040 ?  564 GLY   A C   1 
ATOM   3784 O  O   . GLY   A 1 487 ? -8.76874  -45.95195 -29.83448 1.000 42.13815 ?  564 GLY   A O   1 
ATOM   3785 N  N   . PRO   A 1 488 ? -7.92639  -43.94607 -30.40433 1.000 37.54089 ?  565 PRO   A N   1 
ATOM   3786 C  CA  . PRO   A 1 488 ? -8.78469  -43.22425 -29.43916 1.000 37.77569 ?  565 PRO   A CA  1 
ATOM   3787 C  C   . PRO   A 1 488 ? -10.27852 -43.36963 -29.68382 1.000 33.55974 ?  565 PRO   A C   1 
ATOM   3788 O  O   . PRO   A 1 488 ? -11.05593 -43.37103 -28.72482 1.000 31.78900 ?  565 PRO   A O   1 
ATOM   3789 C  CB  . PRO   A 1 488 ? -8.34729  -41.75720 -29.60447 1.000 34.88747 ?  565 PRO   A CB  1 
ATOM   3790 C  CG  . PRO   A 1 488 ? -7.03769  -41.80115 -30.35565 1.000 36.37264 ?  565 PRO   A CG  1 
ATOM   3791 C  CD  . PRO   A 1 488 ? -7.05168  -43.04989 -31.17501 1.000 38.40336 ?  565 PRO   A CD  1 
ATOM   3792 N  N   . SER   A 1 489 ? -10.71675 -43.43047 -30.94037 1.000 36.59028 ?  566 SER   A N   1 
ATOM   3793 C  CA  . SER   A 1 489 ? -12.14106 -43.62026 -31.21186 1.000 34.59217 ?  566 SER   A CA  1 
ATOM   3794 C  C   . SER   A 1 489 ? -12.66885 -44.88486 -30.54286 1.000 33.35155 ?  566 SER   A C   1 
ATOM   3795 O  O   . SER   A 1 489 ? -13.70787 -44.85836 -29.87418 1.000 35.61330 ?  566 SER   A O   1 
ATOM   3796 C  CB  . SER   A 1 489 ? -12.39059 -43.66239 -32.72135 1.000 35.88238 ?  566 SER   A CB  1 
ATOM   3797 O  OG  . SER   A 1 489 ? -12.33884 -42.35142 -33.27840 1.000 44.98787 ?  566 SER   A OG  1 
ATOM   3798 N  N   . PHE   A 1 490 ? -11.96141 -46.00430 -30.69921 1.000 30.67374 ?  567 PHE   A N   1 
ATOM   3799 C  CA  . PHE   A 1 490 ? -12.44094 -47.24700 -30.10244 1.000 33.60998 ?  567 PHE   A CA  1 
ATOM   3800 C  C   . PHE   A 1 490 ? -12.26463 -47.24617 -28.59602 1.000 30.35398 ?  567 PHE   A C   1 
ATOM   3801 O  O   . PHE   A 1 490 ? -13.11602 -47.76179 -27.86604 1.000 29.62097 ?  567 PHE   A O   1 
ATOM   3802 C  CB  . PHE   A 1 490 ? -11.73609 -48.44925 -30.73620 1.000 34.26406 ?  567 PHE   A CB  1 
ATOM   3803 C  CG  . PHE   A 1 490 ? -12.33401 -48.84245 -32.03740 1.000 30.61660 ?  567 PHE   A CG  1 
ATOM   3804 C  CD1 . PHE   A 1 490 ? -11.90985 -48.26289 -33.21140 1.000 32.42332 ?  567 PHE   A CD1 1 
ATOM   3805 C  CD2 . PHE   A 1 490 ? -13.37883 -49.73714 -32.08543 1.000 35.14582 ?  567 PHE   A CD2 1 
ATOM   3806 C  CE1 . PHE   A 1 490 ? -12.49339 -48.61022 -34.42141 1.000 32.84164 ?  567 PHE   A CE1 1 
ATOM   3807 C  CE2 . PHE   A 1 490 ? -13.96187 -50.08022 -33.29688 1.000 35.57839 ?  567 PHE   A CE2 1 
ATOM   3808 C  CZ  . PHE   A 1 490 ? -13.51347 -49.51544 -34.45980 1.000 32.36033 ?  567 PHE   A CZ  1 
ATOM   3809 N  N   . ILE   A 1 491 ? -11.17557 -46.66360 -28.10460 1.000 32.50055 ?  568 ILE   A N   1 
ATOM   3810 C  CA  . ILE   A 1 491 ? -10.95119 -46.65899 -26.66528 1.000 31.66557 ?  568 ILE   A CA  1 
ATOM   3811 C  C   . ILE   A 1 491 ? -12.08507 -45.91211 -25.96475 1.000 31.17110 ?  568 ILE   A C   1 
ATOM   3812 O  O   . ILE   A 1 491 ? -12.70393 -46.42785 -25.02785 1.000 29.78533 ?  568 ILE   A O   1 
ATOM   3813 C  CB  . ILE   A 1 491 ? -9.56177  -46.07231 -26.34555 1.000 36.35100 ?  568 ILE   A CB  1 
ATOM   3814 C  CG1 . ILE   A 1 491 ? -8.46391  -46.93186 -26.98158 1.000 32.81463 ?  568 ILE   A CG1 1 
ATOM   3815 C  CG2 . ILE   A 1 491 ? -9.34308  -45.95634 -24.84041 1.000 34.08468 ?  568 ILE   A CG2 1 
ATOM   3816 C  CD1 . ILE   A 1 491 ? -7.11960  -46.25416 -27.04973 1.000 34.39834 ?  568 ILE   A CD1 1 
ATOM   3817 N  N   . ILE   A 1 492 ? -12.40621 -44.70386 -26.43890 1.000 31.80717 ?  569 ILE   A N   1 
ATOM   3818 C  CA  . ILE   A 1 492 ? -13.51492 -43.94409 -25.85475 1.000 32.14955 ?  569 ILE   A CA  1 
ATOM   3819 C  C   . ILE   A 1 492 ? -14.83851 -44.67685 -26.05761 1.000 32.96514 ?  569 ILE   A C   1 
ATOM   3820 O  O   . ILE   A 1 492 ? -15.66489 -44.77662 -25.14001 1.000 31.60594 ?  569 ILE   A O   1 
ATOM   3821 C  CB  . ILE   A 1 492 ? -13.57217 -42.52201 -26.43870 1.000 30.34148 ?  569 ILE   A CB  1 
ATOM   3822 C  CG1 . ILE   A 1 492 ? -12.41358 -41.67934 -25.91036 1.000 32.80689 ?  569 ILE   A CG1 1 
ATOM   3823 C  CG2 . ILE   A 1 492 ? -14.88059 -41.87759 -26.06455 1.000 32.71177 ?  569 ILE   A CG2 1 
ATOM   3824 C  CD1 . ILE   A 1 492 ? -12.28712 -41.68931 -24.39163 1.000 32.72131 ?  569 ILE   A CD1 1 
ATOM   3825 N  N   . GLN   A 1 493 ? -15.07512 -45.18497 -27.26756 1.000 31.41078 ?  570 GLN   A N   1 
ATOM   3826 C  CA  . GLN   A 1 493 ? -16.28774 -45.96753 -27.47835 1.000 32.62534 ?  570 GLN   A CA  1 
ATOM   3827 C  C   . GLN   A 1 493 ? -16.36734 -47.12246 -26.48787 1.000 34.40749 ?  570 GLN   A C   1 
ATOM   3828 O  O   . GLN   A 1 493 ? -17.43676 -47.40850 -25.93143 1.000 35.84406 ?  570 GLN   A O   1 
ATOM   3829 C  CB  . GLN   A 1 493 ? -16.34989 -46.49819 -28.91168 1.000 36.08661 ?  570 GLN   A CB  1 
ATOM   3830 C  CG  . GLN   A 1 493 ? -17.46852 -47.52905 -29.08938 1.000 41.88859 ?  570 GLN   A CG  1 
ATOM   3831 C  CD  . GLN   A 1 493 ? -17.42471 -48.24569 -30.42889 1.000 40.33446 ?  570 GLN   A CD  1 
ATOM   3832 O  OE1 . GLN   A 1 493 ? -18.26845 -47.99964 -31.28633 1.000 41.43821 ?  570 GLN   A OE1 1 
ATOM   3833 N  NE2 . GLN   A 1 493 ? -16.46045 -49.15630 -30.60163 1.000 34.23602 ?  570 GLN   A NE2 1 
ATOM   3834 N  N   . PHE   A 1 494 ? -15.24107 -47.79190 -26.24521 1.000 31.53541 ?  571 PHE   A N   1 
ATOM   3835 C  CA  . PHE   A 1 494 ? -15.26316 -48.93051 -25.33912 1.000 34.65392 ?  571 PHE   A CA  1 
ATOM   3836 C  C   . PHE   A 1 494 ? -15.54687 -48.48631 -23.91041 1.000 34.10006 ?  571 PHE   A C   1 
ATOM   3837 O  O   . PHE   A 1 494 ? -16.29018 -49.15466 -23.18009 1.000 31.12381 ?  571 PHE   A O   1 
ATOM   3838 C  CB  . PHE   A 1 494 ? -13.94511 -49.69071 -25.43275 1.000 33.72855 ?  571 PHE   A CB  1 
ATOM   3839 C  CG  . PHE   A 1 494 ? -13.72403 -50.64970 -24.30696 1.000 39.24828 ?  571 PHE   A CG  1 
ATOM   3840 C  CD1 . PHE   A 1 494 ? -14.20072 -51.95103 -24.38547 1.000 38.56040 ?  571 PHE   A CD1 1 
ATOM   3841 C  CD2 . PHE   A 1 494 ? -13.03546 -50.25583 -23.17335 1.000 34.04412 ?  571 PHE   A CD2 1 
ATOM   3842 C  CE1 . PHE   A 1 494 ? -14.00087 -52.82779 -23.35642 1.000 35.39483 ?  571 PHE   A CE1 1 
ATOM   3843 C  CE2 . PHE   A 1 494 ? -12.83805 -51.13362 -22.14304 1.000 34.35327 ?  571 PHE   A CE2 1 
ATOM   3844 C  CZ  . PHE   A 1 494 ? -13.31700 -52.42300 -22.23810 1.000 37.04261 ?  571 PHE   A CZ  1 
ATOM   3845 N  N   . LEU   A 1 495 ? -14.98669 -47.34430 -23.50761 1.000 33.12655 ?  572 LEU   A N   1 
ATOM   3846 C  CA  . LEU   A 1 495 ? -15.20140 -46.84918 -22.15095 1.000 36.89274 ?  572 LEU   A CA  1 
ATOM   3847 C  C   . LEU   A 1 495 ? -16.65238 -46.43960 -21.92391 1.000 34.07477 ?  572 LEU   A C   1 
ATOM   3848 O  O   . LEU   A 1 495 ? -17.18120 -46.61234 -20.82158 1.000 35.38710 ?  572 LEU   A O   1 
ATOM   3849 C  CB  . LEU   A 1 495 ? -14.26870 -45.66966 -21.86276 1.000 33.62176 ?  572 LEU   A CB  1 
ATOM   3850 C  CG  . LEU   A 1 495 ? -12.76764 -45.93631 -21.74333 1.000 33.04473 ?  572 LEU   A CG  1 
ATOM   3851 C  CD1 . LEU   A 1 495 ? -12.05429 -44.61118 -21.47606 1.000 29.10286 ?  572 LEU   A CD1 1 
ATOM   3852 C  CD2 . LEU   A 1 495 ? -12.47327 -46.95190 -20.63186 1.000 26.14716 ?  572 LEU   A CD2 1 
ATOM   3853 N  N   . LYS   A 1 496 ? -17.30373 -45.87584 -22.94267 1.000 32.51742 ?  573 LYS   A N   1 
ATOM   3854 C  CA  . LYS   A 1 496 ? -18.68088 -45.42321 -22.78631 1.000 34.36890 ?  573 LYS   A CA  1 
ATOM   3855 C  C   . LYS   A 1 496 ? -19.65941 -46.58903 -22.78489 1.000 35.34151 ?  573 LYS   A C   1 
ATOM   3856 O  O   . LYS   A 1 496 ? -20.48345 -46.70906 -21.86951 1.000 36.16000 ?  573 LYS   A O   1 
ATOM   3857 C  CB  . LYS   A 1 496 ? -19.05226 -44.44330 -23.89861 1.000 35.45902 ?  573 LYS   A CB  1 
ATOM   3858 C  CG  . LYS   A 1 496 ? -18.14592 -43.27812 -23.99829 1.000 36.49194 ?  573 LYS   A CG  1 
ATOM   3859 C  CD  . LYS   A 1 496 ? -18.24587 -42.64768 -25.36002 1.000 36.45972 ?  573 LYS   A CD  1 
ATOM   3860 C  CE  . LYS   A 1 496 ? -19.67622 -42.32729 -25.70385 1.000 39.54002 ?  573 LYS   A CE  1 
ATOM   3861 N  NZ  . LYS   A 1 496 ? -19.74728 -41.25582 -26.75361 1.000 41.40960 ?  573 LYS   A NZ  1 
ATOM   3862 N  N   . MET   A 1 497 ? -19.58965 -47.45589 -23.80537 1.000 35.77072 ?  574 MET   A N   1 
ATOM   3863 C  CA  . MET   A 1 497 ? -20.58745 -48.51314 -23.94581 1.000 38.87672 ?  574 MET   A CA  1 
ATOM   3864 C  C   . MET   A 1 497 ? -20.34375 -49.70248 -23.02407 1.000 38.46093 ?  574 MET   A C   1 
ATOM   3865 O  O   . MET   A 1 497 ? -21.28339 -50.44479 -22.73077 1.000 39.68790 ?  574 MET   A O   1 
ATOM   3866 C  CB  . MET   A 1 497 ? -20.64753 -48.99442 -25.39371 1.000 37.81185 ?  574 MET   A CB  1 
ATOM   3867 C  CG  . MET   A 1 497 ? -21.06805 -47.92456 -26.38397 1.000 41.50137 ?  574 MET   A CG  1 
ATOM   3868 S  SD  . MET   A 1 497 ? -21.25444 -48.62661 -28.03852 1.000 64.90549 ?  574 MET   A SD  1 
ATOM   3869 C  CE  . MET   A 1 497 ? -21.01263 -47.20282 -29.11527 1.000 51.65110 ?  574 MET   A CE  1 
ATOM   3870 N  N   . GLN   A 1 498 ? -19.11819 -49.90638 -22.55272 1.000 41.41672 ?  575 GLN   A N   1 
ATOM   3871 C  CA  . GLN   A 1 498 ? -18.80724 -51.07437 -21.73649 1.000 38.48961 ?  575 GLN   A CA  1 
ATOM   3872 C  C   . GLN   A 1 498 ? -18.38473 -50.69425 -20.31921 1.000 40.09553 ?  575 GLN   A C   1 
ATOM   3873 O  O   . GLN   A 1 498 ? -17.73013 -51.49029 -19.64001 1.000 40.93940 ?  575 GLN   A O   1 
ATOM   3874 C  CB  . GLN   A 1 498 ? -17.72689 -51.91376 -22.41626 1.000 37.81930 ?  575 GLN   A CB  1 
ATOM   3875 C  CG  . GLN   A 1 498 ? -18.12184 -52.43624 -23.80161 1.000 37.24576 ?  575 GLN   A CG  1 
ATOM   3876 C  CD  . GLN   A 1 498 ? -17.31006 -53.65938 -24.18953 1.000 41.54538 ?  575 GLN   A CD  1 
ATOM   3877 O  OE1 . GLN   A 1 498 ? -16.76828 -54.34935 -23.32400 1.000 45.18076 ?  575 GLN   A OE1 1 
ATOM   3878 N  NE2 . GLN   A 1 498 ? -17.21171 -53.93143 -25.48327 1.000 38.82422 ?  575 GLN   A NE2 1 
ATOM   3879 N  N   . GLY   A 1 499 ? -18.74497 -49.48709 -19.86261 1.000 38.50868 ?  576 GLY   A N   1 
ATOM   3880 C  CA  . GLY   A 1 499 ? -18.52239 -49.06078 -18.49815 1.000 33.90326 ?  576 GLY   A CA  1 
ATOM   3881 C  C   . GLY   A 1 499 ? -19.84312 -48.90233 -17.76871 1.000 33.87717 ?  576 GLY   A C   1 
ATOM   3882 O  O   . GLY   A 1 499 ? -20.89671 -49.25513 -18.29220 1.000 35.95913 ?  576 GLY   A O   1 
ATOM   3883 N  N   . PRO   A 1 500 ? -19.81569 -48.39243 -16.53582 1.000 32.97933 ?  577 PRO   A N   1 
ATOM   3884 C  CA  . PRO   A 1 500 ? -21.06679 -48.21946 -15.77151 1.000 34.10034 ?  577 PRO   A CA  1 
ATOM   3885 C  C   . PRO   A 1 500 ? -21.87066 -46.97075 -16.11128 1.000 34.66408 ?  577 PRO   A C   1 
ATOM   3886 O  O   . PRO   A 1 500 ? -22.91235 -46.74813 -15.48732 1.000 33.26860 ?  577 PRO   A O   1 
ATOM   3887 C  CB  . PRO   A 1 500 ? -20.58933 -48.16302 -14.30856 1.000 32.13967 ?  577 PRO   A CB  1 
ATOM   3888 C  CG  . PRO   A 1 500 ? -19.13706 -47.79842 -14.37811 1.000 35.86334 ?  577 PRO   A CG  1 
ATOM   3889 C  CD  . PRO   A 1 500 ? -18.60654 -48.32311 -15.69277 1.000 30.95317 ?  577 PRO   A CD  1 
ATOM   3890 N  N   . TYR   A 1 501 ? -21.44682 -46.15579 -17.07276 1.000 30.30209 ?  578 TYR   A N   1 
ATOM   3891 C  CA  . TYR   A 1 501 ? -22.17016 -44.94080 -17.41637 1.000 35.90373 ?  578 TYR   A CA  1 
ATOM   3892 C  C   . TYR   A 1 501 ? -22.87128 -45.07196 -18.75539 1.000 35.61116 ?  578 TYR   A C   1 
ATOM   3893 O  O   . TYR   A 1 501 ? -23.26380 -44.06701 -19.35854 1.000 36.30852 ?  578 TYR   A O   1 
ATOM   3894 C  CB  . TYR   A 1 501 ? -21.20851 -43.74953 -17.39483 1.000 34.99481 ?  578 TYR   A CB  1 
ATOM   3895 C  CG  . TYR   A 1 501 ? -20.40904 -43.75721 -16.11283 1.000 33.59020 ?  578 TYR   A CG  1 
ATOM   3896 C  CD1 . TYR   A 1 501 ? -21.04069 -43.56694 -14.88363 1.000 31.82802 ?  578 TYR   A CD1 1 
ATOM   3897 C  CD2 . TYR   A 1 501 ? -19.04236 -44.00936 -16.11602 1.000 32.45824 ?  578 TYR   A CD2 1 
ATOM   3898 C  CE1 . TYR   A 1 501 ? -20.32410 -43.59591 -13.69830 1.000 33.26294 ?  578 TYR   A CE1 1 
ATOM   3899 C  CE2 . TYR   A 1 501 ? -18.31737 -44.04545 -14.92767 1.000 30.71813 ?  578 TYR   A CE2 1 
ATOM   3900 C  CZ  . TYR   A 1 501 ? -18.96666 -43.84092 -13.73007 1.000 31.92556 ?  578 TYR   A CZ  1 
ATOM   3901 O  OH  . TYR   A 1 501 ? -18.26702 -43.87024 -12.55398 1.000 39.89673 ?  578 TYR   A OH  1 
ATOM   3902 N  N   . ARG   A 1 502 ? -23.02800 -46.30732 -19.22713 1.000 36.48566 ?  579 ARG   A N   1 
ATOM   3903 C  CA  . ARG   A 1 502 ? -23.61828 -46.54310 -20.53808 1.000 37.09292 ?  579 ARG   A CA  1 
ATOM   3904 C  C   . ARG   A 1 502 ? -24.94756 -45.81415 -20.68114 1.000 36.94472 ?  579 ARG   A C   1 
ATOM   3905 O  O   . ARG   A 1 502 ? -25.26183 -45.27382 -21.74638 1.000 35.96942 ?  579 ARG   A O   1 
ATOM   3906 C  CB  . ARG   A 1 502 ? -23.78956 -48.04608 -20.74378 1.000 32.94010 ?  579 ARG   A CB  1 
ATOM   3907 C  CG  . ARG   A 1 502 ? -24.33174 -48.46112 -22.09421 1.000 38.86419 ?  579 ARG   A CG  1 
ATOM   3908 C  CD  . ARG   A 1 502 ? -24.39709 -49.98905 -22.19864 1.000 38.56363 ?  579 ARG   A CD  1 
ATOM   3909 N  NE  . ARG   A 1 502 ? -25.05290 -50.59005 -21.04097 1.000 33.47757 ?  579 ARG   A NE  1 
ATOM   3910 C  CZ  . ARG   A 1 502 ? -25.39551 -51.87015 -20.95808 1.000 38.39040 ?  579 ARG   A CZ  1 
ATOM   3911 N  NH1 . ARG   A 1 502 ? -25.10648 -52.72815 -21.92804 1.000 33.52301 ?  579 ARG   A NH1 1 
ATOM   3912 N  NH2 . ARG   A 1 502 ? -26.05401 -52.29964 -19.88056 1.000 36.17162 ?  579 ARG   A NH2 1 
ATOM   3913 N  N   . ALA   A 1 503 ? -25.72163 -45.75866 -19.60045 1.000 36.20057 ?  580 ALA   A N   1 
ATOM   3914 C  CA  . ALA   A 1 503 ? -27.05874 -45.19116 -19.63988 1.000 38.47928 ?  580 ALA   A CA  1 
ATOM   3915 C  C   . ALA   A 1 503 ? -27.06628 -43.66287 -19.66806 1.000 38.67882 ?  580 ALA   A C   1 
ATOM   3916 O  O   . ALA   A 1 503 ? -28.06694 -43.07961 -20.09424 1.000 36.87647 ?  580 ALA   A O   1 
ATOM   3917 C  CB  . ALA   A 1 503 ? -27.87248 -45.69598 -18.43876 1.000 36.58621 ?  580 ALA   A CB  1 
ATOM   3918 N  N   . MET   A 1 504 ? -25.99115 -42.99494 -19.24663 1.000 34.44144 ?  581 MET   A N   1 
ATOM   3919 C  CA  . MET   A 1 504 ? -26.02494 -41.54092 -19.15899 1.000 39.81847 ?  581 MET   A CA  1 
ATOM   3920 C  C   . MET   A 1 504 ? -25.05409 -40.83809 -20.10057 1.000 40.84867 ?  581 MET   A C   1 
ATOM   3921 O  O   . MET   A 1 504 ? -24.87897 -39.62282 -19.97906 1.000 47.39053 ?  581 MET   A O   1 
ATOM   3922 C  CB  . MET   A 1 504 ? -25.78930 -41.08078 -17.71431 1.000 37.04023 ?  581 MET   A CB  1 
ATOM   3923 C  CG  . MET   A 1 504 ? -24.43466 -41.39136 -17.14494 1.000 38.29693 ?  581 MET   A CG  1 
ATOM   3924 S  SD  . MET   A 1 504 ? -24.40503 -41.20816 -15.35174 1.000 43.29911 ?  581 MET   A SD  1 
ATOM   3925 C  CE  . MET   A 1 504 ? -25.24635 -42.70760 -14.81618 1.000 44.20827 ?  581 MET   A CE  1 
ATOM   3926 N  N   . VAL   A 1 505 ? -24.45504 -41.53879 -21.05769 1.000 40.84756 ?  582 VAL   A N   1 
ATOM   3927 C  CA  . VAL   A 1 505 ? -23.54295 -40.88237 -21.99787 1.000 41.54695 ?  582 VAL   A CA  1 
ATOM   3928 C  C   . VAL   A 1 505 ? -23.97297 -41.07611 -23.45187 1.000 43.86319 ?  582 VAL   A C   1 
ATOM   3929 O  O   . VAL   A 1 505 ? -24.76856 -41.95529 -23.77354 1.000 43.32047 ?  582 VAL   A O   1 
ATOM   3930 C  CB  . VAL   A 1 505 ? -22.11313 -41.38380 -21.81992 1.000 41.23615 ?  582 VAL   A CB  1 
ATOM   3931 C  CG1 . VAL   A 1 505 ? -21.68408 -41.26438 -20.36590 1.000 37.38359 ?  582 VAL   A CG1 1 
ATOM   3932 C  CG2 . VAL   A 1 505 ? -22.01746 -42.82528 -22.31395 1.000 39.27583 ?  582 VAL   A CG2 1 
HETATM 3933 C  C1  . A1ATZ B 2 .   ? 3.19123   -3.11805  -34.85511 1.000 51.29295 ?  601 A1ATZ A C1  1 
HETATM 3934 C  C2  . A1ATZ B 2 .   ? 3.34061   -1.52841  -34.90091 1.000 50.60469 ?  601 A1ATZ A C2  1 
HETATM 3935 C  C3  . A1ATZ B 2 .   ? 5.89346   -1.50786  -34.41824 1.000 40.59899 ?  601 A1ATZ A C3  1 
HETATM 3936 O  O1  . A1ATZ B 2 .   ? 2.29569   -3.67891  -34.09692 1.000 53.88270 ?  601 A1ATZ A O1  1 
HETATM 3937 O  O2  . A1ATZ B 2 .   ? 4.13924   -3.80698  -35.67173 1.000 45.47039 -1 601 A1ATZ A O2  1 
HETATM 3938 O  O3  . A1ATZ B 2 .   ? 9.40053   -2.12356  -31.93675 1.000 36.27444 ?  601 A1ATZ A O3  1 
HETATM 3939 C  C11 . A1ATZ B 2 .   ? 1.36477   -1.77610  -36.74129 1.000 58.23698 ?  601 A1ATZ A C11 1 
HETATM 3940 C  C12 . A1ATZ B 2 .   ? 0.50574   -1.16923  -37.78357 1.000 60.09018 ?  601 A1ATZ A C12 1 
HETATM 3941 C  C13 . A1ATZ B 2 .   ? 0.65374   0.26684   -38.11620 1.000 65.76028 ?  601 A1ATZ A C13 1 
HETATM 3942 C  C14 . A1ATZ B 2 .   ? 1.66274   1.09232   -37.41839 1.000 57.45081 ?  601 A1ATZ A C14 1 
HETATM 3943 C  C15 . A1ATZ B 2 .   ? 2.52074   0.47482   -36.37172 1.000 56.13576 ?  601 A1ATZ A C15 1 
HETATM 3944 C  C16 . A1ATZ B 2 .   ? 4.12481   2.42018   -36.19985 1.000 49.56591 ?  601 A1ATZ A C16 1 
HETATM 3945 C  C17 . A1ATZ B 2 .   ? 5.30327   2.93457   -35.26087 1.000 40.36317 ?  601 A1ATZ A C17 1 
HETATM 3946 C  C18 . A1ATZ B 2 .   ? 5.59146   2.22741   -34.00683 1.000 37.51805 ?  601 A1ATZ A C18 1 
HETATM 3947 C  C19 . A1ATZ B 2 .   ? 6.66310   2.67195   -33.10911 1.000 33.04070 ?  601 A1ATZ A C19 1 
HETATM 3948 C  C20 . A1ATZ B 2 .   ? 6.93116   1.89749   -31.82379 1.000 35.53351 ?  601 A1ATZ A C20 1 
HETATM 3949 C  C21 . A1ATZ B 2 .   ? 5.82581   1.24467   -31.08903 1.000 39.99558 ?  601 A1ATZ A C21 1 
HETATM 3950 C  C22 . A1ATZ B 2 .   ? 6.09435   0.48107   -29.85542 1.000 37.85411 ?  601 A1ATZ A C22 1 
HETATM 3951 C  C23 . A1ATZ B 2 .   ? 7.47256   0.36371   -29.35289 1.000 36.29050 ?  601 A1ATZ A C23 1 
HETATM 3952 C  C24 . A1ATZ B 2 .   ? 8.57606   1.00557   -30.09107 1.000 32.79198 ?  601 A1ATZ A C24 1 
HETATM 3953 C  C25 . A1ATZ B 2 .   ? 8.30672   1.76774   -31.32484 1.000 33.96626 ?  601 A1ATZ A C25 1 
HETATM 3954 C  C26 . A1ATZ B 2 .   ? 7.47707   3.83727   -33.47198 1.000 35.90468 ?  601 A1ATZ A C26 1 
HETATM 3955 C  C27 . A1ATZ B 2 .   ? 7.19635   4.56895   -34.71883 1.000 35.50255 ?  601 A1ATZ A C27 1 
HETATM 3956 C  C28 . A1ATZ B 2 .   ? 6.11639   4.11126   -35.61699 1.000 43.36097 ?  601 A1ATZ A C28 1 
HETATM 3957 C  C10 . A1ATZ B 2 .   ? 2.38370   -0.96299  -36.01653 1.000 57.00061 ?  601 A1ATZ A C10 1 
HETATM 3958 C  C4  . A1ATZ B 2 .   ? 5.69799   -2.28705  -33.15901 1.000 37.77472 ?  601 A1ATZ A C4  1 
HETATM 3959 C  C5  . A1ATZ B 2 .   ? 6.82566   -2.55513  -32.24297 1.000 34.03016 ?  601 A1ATZ A C5  1 
HETATM 3960 C  C6  . A1ATZ B 2 .   ? 8.14318   -2.01915  -32.62163 1.000 35.04950 ?  601 A1ATZ A C6  1 
HETATM 3961 C  C7  . A1ATZ B 2 .   ? 10.39519  -1.43407  -32.68938 1.000 30.41020 ?  601 A1ATZ A C7  1 
HETATM 3962 C  C8  . A1ATZ B 2 .   ? 8.32514   -1.25551  -33.82806 1.000 32.31265 ?  601 A1ATZ A C8  1 
HETATM 3963 C  C9  . A1ATZ B 2 .   ? 7.23181   -0.96667  -34.76533 1.000 38.31081 ?  601 A1ATZ A C9  1 
HETATM 3964 N  N1  . A1ATZ B 2 .   ? 4.77836   -1.23557  -35.32025 1.000 44.85971 ?  601 A1ATZ A N1  1 
HETATM 3965 N  N2  . A1ATZ B 2 .   ? 9.73002   -0.90425  -33.86025 1.000 33.66554 ?  601 A1ATZ A N2  1 
HETATM 3966 O  O4  . A1ATZ B 2 .   ? 11.62817  -1.34431  -32.37667 1.000 30.81904 ?  601 A1ATZ A O4  1 
HETATM 3967 O  O5  . A1ATZ B 2 .   ? 3.53899   1.17873   -35.62607 1.000 52.53300 ?  601 A1ATZ A O5  1 
HETATM 3968 CL CL1 . A1ATZ B 2 .   ? 5.78447   5.01326   -37.16116 1.000 69.35579 ?  601 A1ATZ A CL1 1 
HETATM 3969 H  H2  . A1ATZ B 2 .   ? 2.97730   -1.13189  -33.89120 1.000 60.65307 ?  601 A1ATZ A H2  1 
HETATM 3970 H  H8  . A1ATZ B 2 .   ? 1.24508   -2.87668  -36.49104 1.000 69.81181 ?  601 A1ATZ A H8  1 
HETATM 3971 H  H9  . A1ATZ B 2 .   ? -0.26366  -1.80376  -38.32543 1.000 72.03565 ?  601 A1ATZ A H9  1 
HETATM 3972 H  H10 . A1ATZ B 2 .   ? -0.00906  0.73447   -38.90865 1.000 78.83978 ?  601 A1ATZ A H10 1 
HETATM 3973 H  H11 . A1ATZ B 2 .   ? 1.76027   2.18564   -37.69913 1.000 68.86841 ?  601 A1ATZ A H11 1 
HETATM 3974 H  H12 . A1ATZ B 2 .   ? 3.35085   3.26179   -36.27727 1.000 59.40652 ?  601 A1ATZ A H12 1 
HETATM 3975 H  H13 . A1ATZ B 2 .   ? 4.56511   2.24252   -37.24287 1.000 59.40652 ?  601 A1ATZ A H13 1 
HETATM 3976 H  H14 . A1ATZ B 2 .   ? 4.97689   1.31932   -33.72159 1.000 44.94909 ?  601 A1ATZ A H14 1 
HETATM 3977 H  H15 . A1ATZ B 2 .   ? 4.76044   1.32604   -31.46891 1.000 47.92213 ?  601 A1ATZ A H15 1 
HETATM 3978 H  H16 . A1ATZ B 2 .   ? 5.24144   -0.01503  -29.29446 1.000 45.35237 ?  601 A1ATZ A H16 1 
HETATM 3979 H  H17 . A1ATZ B 2 .   ? 7.68223   -0.21862  -28.40149 1.000 43.47603 ?  601 A1ATZ A H17 1 
HETATM 3980 H  H18 . A1ATZ B 2 .   ? 9.63913   0.91249   -29.70743 1.000 39.27781 ?  601 A1ATZ A H18 1 
HETATM 3981 H  H19 . A1ATZ B 2 .   ? 9.16820   2.25059   -31.88221 1.000 40.68695 ?  601 A1ATZ A H19 1 
HETATM 3982 H  H20 . A1ATZ B 2 .   ? 8.32244   4.17921   -32.79790 1.000 43.01306 ?  601 A1ATZ A H20 1 
HETATM 3983 H  H21 . A1ATZ B 2 .   ? 7.80837   5.48401   -34.99095 1.000 42.53050 ?  601 A1ATZ A H21 1 
HETATM 3984 H  H4  . A1ATZ B 2 .   ? 4.67174   -2.68625  -32.88806 1.000 45.25710 ?  601 A1ATZ A H4  1 
HETATM 3985 H  H5  . A1ATZ B 2 .   ? 6.68414   -3.14897  -31.28731 1.000 40.76363 ?  601 A1ATZ A H5  1 
HETATM 3986 H  H7  . A1ATZ B 2 .   ? 7.40888   -0.35914  -35.70635 1.000 45.90041 ?  601 A1ATZ A H7  1 
HETATM 3987 H  H3  . A1ATZ B 2 .   ? 4.89364   -1.58072  -36.32115 1.000 53.75909 ?  601 A1ATZ A H3  1 
HETATM 3988 H  H6  . A1ATZ B 2 .   ? 10.24005  -0.34887  -34.60096 1.000 40.32608 ?  601 A1ATZ A H6  1 
HETATM 3989 K  K   . K     C 3 .   ? 21.29959  -9.79732  -29.36571 1.000 36.09572 ?  602 K     A K   1 
HETATM 3990 O  O   . HOH   D 4 .   ? 5.50551   -45.22297 -14.03441 1.000 30.37810 ?  701 HOH   A O   1 
HETATM 3991 O  O   . HOH   D 4 .   ? -18.61064 19.87431  -70.66365 1.000 34.32098 ?  702 HOH   A O   1 
HETATM 3992 O  O   . HOH   D 4 .   ? 7.09173   -5.27148  -23.09809 1.000 32.47834 ?  703 HOH   A O   1 
HETATM 3993 O  O   . HOH   D 4 .   ? -13.13119 -29.25438 -17.62081 1.000 29.64022 ?  704 HOH   A O   1 
HETATM 3994 O  O   . HOH   D 4 .   ? 8.60299   -0.08797  -8.93542  1.000 33.64229 ?  705 HOH   A O   1 
HETATM 3995 O  O   . HOH   D 4 .   ? -2.02141  5.05452   -52.46320 1.000 36.50287 ?  706 HOH   A O   1 
HETATM 3996 O  O   . HOH   D 4 .   ? 2.21002   3.19774   -67.58326 1.000 34.14029 ?  707 HOH   A O   1 
HETATM 3997 O  O   . HOH   D 4 .   ? 26.99137  9.18483   -24.82743 1.000 41.28424 ?  708 HOH   A O   1 
HETATM 3998 O  O   . HOH   D 4 .   ? 3.71699   20.58262  -41.73748 1.000 33.97421 ?  709 HOH   A O   1 
HETATM 3999 O  O   . HOH   D 4 .   ? 9.07107   2.81911   -3.09089  1.000 43.16257 ?  710 HOH   A O   1 
HETATM 4000 O  O   . HOH   D 4 .   ? 24.67618  11.18172  -23.82170 1.000 34.93461 ?  711 HOH   A O   1 
HETATM 4001 O  O   . HOH   D 4 .   ? 0.30858   -9.90332  -2.01970  1.000 33.18353 ?  712 HOH   A O   1 
HETATM 4002 O  O   . HOH   D 4 .   ? -9.37291  -15.78052 -14.59639 1.000 33.42925 ?  713 HOH   A O   1 
HETATM 4003 O  O   . HOH   D 4 .   ? 9.24886   18.89581  -28.32180 1.000 37.56263 ?  714 HOH   A O   1 
HETATM 4004 O  O   . HOH   D 4 .   ? 24.69501  5.00214   -41.64145 1.000 32.79506 ?  715 HOH   A O   1 
HETATM 4005 O  O   . HOH   D 4 .   ? 7.88708   16.96083  -66.95578 1.000 30.93129 ?  716 HOH   A O   1 
HETATM 4006 O  O   . HOH   D 4 .   ? 11.94875  -32.57458 -18.03141 1.000 31.91239 ?  717 HOH   A O   1 
HETATM 4007 O  O   . HOH   D 4 .   ? -6.22378  20.45954  -60.12610 1.000 35.72246 ?  718 HOH   A O   1 
HETATM 4008 O  O   . HOH   D 4 .   ? 25.91017  -19.82775 -16.65347 1.000 32.50370 ?  719 HOH   A O   1 
HETATM 4009 O  O   . HOH   D 4 .   ? 8.42675   8.80762   -19.93573 1.000 33.00617 ?  720 HOH   A O   1 
HETATM 4010 O  O   . HOH   D 4 .   ? 2.58741   11.98671  -37.91218 1.000 35.91754 ?  721 HOH   A O   1 
HETATM 4011 O  O   . HOH   D 4 .   ? 8.93183   2.50920   -65.29660 1.000 35.34195 ?  722 HOH   A O   1 
HETATM 4012 O  O   . HOH   D 4 .   ? 16.00651  -10.94697 -5.28182  1.000 31.41418 ?  723 HOH   A O   1 
HETATM 4013 O  O   . HOH   D 4 .   ? 22.29914  5.79249   -48.44691 1.000 33.09638 ?  724 HOH   A O   1 
HETATM 4014 O  O   . HOH   D 4 .   ? 6.24639   -22.54281 -23.09953 1.000 38.06789 ?  725 HOH   A O   1 
HETATM 4015 O  O   . HOH   D 4 .   ? 1.80122   -34.72169 -25.70641 1.000 29.52344 ?  726 HOH   A O   1 
HETATM 4016 O  O   . HOH   D 4 .   ? 9.28646   21.81923  -64.72271 1.000 49.82228 ?  727 HOH   A O   1 
HETATM 4017 O  O   . HOH   D 4 .   ? 12.40404  -11.77463 -27.63239 1.000 34.86221 ?  728 HOH   A O   1 
HETATM 4018 O  O   . HOH   D 4 .   ? 9.55934   19.33147  -41.22170 1.000 34.07844 ?  729 HOH   A O   1 
HETATM 4019 O  O   . HOH   D 4 .   ? 23.93263  7.31399   -34.14859 1.000 31.49089 ?  730 HOH   A O   1 
HETATM 4020 O  O   . HOH   D 4 .   ? 16.40131  -1.98145  -58.58060 1.000 50.76967 ?  731 HOH   A O   1 
HETATM 4021 O  O   . HOH   D 4 .   ? 26.18814  1.62027   -29.16796 1.000 34.05910 ?  732 HOH   A O   1 
HETATM 4022 O  O   . HOH   D 4 .   ? 7.89673   5.45859   -63.87457 1.000 32.25745 ?  733 HOH   A O   1 
HETATM 4023 O  O   . HOH   D 4 .   ? 1.18081   3.27419   -17.12614 1.000 35.51440 ?  734 HOH   A O   1 
HETATM 4024 O  O   . HOH   D 4 .   ? 10.94503  22.04395  -34.39102 1.000 38.11638 ?  735 HOH   A O   1 
HETATM 4025 O  O   . HOH   D 4 .   ? 4.62761   19.59500  -37.23957 1.000 35.40114 ?  736 HOH   A O   1 
HETATM 4026 O  O   . HOH   D 4 .   ? 6.43877   8.59502   -64.36264 1.000 31.79358 ?  737 HOH   A O   1 
HETATM 4027 O  O   . HOH   D 4 .   ? 9.95490   7.66769   -12.91303 1.000 35.33770 ?  738 HOH   A O   1 
HETATM 4028 O  O   . HOH   D 4 .   ? 3.97891   -30.66339 -6.24603  1.000 32.49107 ?  739 HOH   A O   1 
HETATM 4029 O  O   . HOH   D 4 .   ? 3.22586   0.00086   -12.82384 1.000 29.96556 ?  740 HOH   A O   1 
HETATM 4030 O  O   . HOH   D 4 .   ? 5.46638   -40.01373 -29.83865 1.000 45.24907 ?  741 HOH   A O   1 
HETATM 4031 O  O   . HOH   D 4 .   ? -5.12285  -15.91782 -10.10098 1.000 28.97124 ?  742 HOH   A O   1 
HETATM 4032 O  O   . HOH   D 4 .   ? 19.33250  -7.98577  -11.27057 1.000 27.83533 ?  743 HOH   A O   1 
HETATM 4033 O  O   . HOH   D 4 .   ? 1.79072   18.73687  -40.91853 1.000 38.74518 ?  744 HOH   A O   1 
HETATM 4034 O  O   . HOH   D 4 .   ? 17.74980  -4.16472  -42.55998 1.000 26.98274 ?  745 HOH   A O   1 
HETATM 4035 O  O   . HOH   D 4 .   ? -4.85073  13.15867  -48.01576 1.000 36.43471 ?  746 HOH   A O   1 
HETATM 4036 O  O   . HOH   D 4 .   ? 10.44704  15.48219  -29.56923 1.000 35.02616 ?  747 HOH   A O   1 
HETATM 4037 O  O   . HOH   D 4 .   ? -15.44186 -32.93490 -21.28593 1.000 30.43654 ?  748 HOH   A O   1 
HETATM 4038 O  O   . HOH   D 4 .   ? -1.49831  -47.07050 -27.08995 1.000 35.47195 ?  749 HOH   A O   1 
HETATM 4039 O  O   . HOH   D 4 .   ? 18.04286  -15.84554 -9.07079  1.000 31.12825 ?  750 HOH   A O   1 
HETATM 4040 O  O   . HOH   D 4 .   ? -4.00840  -6.15602  -13.61864 1.000 34.44209 ?  751 HOH   A O   1 
HETATM 4041 O  O   . HOH   D 4 .   ? 5.42461   -49.66522 -22.20848 1.000 35.54556 ?  752 HOH   A O   1 
HETATM 4042 O  O   . HOH   D 4 .   ? 3.74933   -43.94977 -18.08709 1.000 29.96880 ?  753 HOH   A O   1 
HETATM 4043 O  O   . HOH   D 4 .   ? -10.92681 -25.17139 -14.16263 1.000 25.74484 ?  754 HOH   A O   1 
HETATM 4044 O  O   . HOH   D 4 .   ? 13.48219  24.34690  -41.75615 1.000 43.07374 ?  755 HOH   A O   1 
HETATM 4045 O  O   . HOH   D 4 .   ? 24.16201  4.45457   -28.45157 1.000 29.78598 ?  756 HOH   A O   1 
HETATM 4046 O  O   . HOH   D 4 .   ? 20.61986  18.66076  -32.54995 1.000 34.31961 ?  757 HOH   A O   1 
HETATM 4047 O  O   . HOH   D 4 .   ? 2.69948   -38.18707 -9.43677  1.000 37.54348 ?  758 HOH   A O   1 
HETATM 4048 O  O   . HOH   D 4 .   ? -1.36212  -11.03566 -9.80607  1.000 30.02161 ?  759 HOH   A O   1 
HETATM 4049 O  O   . HOH   D 4 .   ? 11.25829  -7.84353  -6.51965  1.000 26.81833 ?  760 HOH   A O   1 
HETATM 4050 O  O   . HOH   D 4 .   ? -0.43072  -3.31711  -58.74704 1.000 29.54361 ?  761 HOH   A O   1 
HETATM 4051 O  O   . HOH   D 4 .   ? -22.99731 -52.21389 -23.93327 1.000 37.22523 ?  762 HOH   A O   1 
HETATM 4052 O  O   . HOH   D 4 .   ? -22.74933 11.43035  -60.42634 1.000 35.49477 ?  763 HOH   A O   1 
HETATM 4053 O  O   . HOH   D 4 .   ? -1.02914  21.58726  -56.44167 1.000 32.71564 ?  764 HOH   A O   1 
HETATM 4054 O  O   . HOH   D 4 .   ? 22.57795  -8.83757  -31.61748 1.000 30.25390 ?  765 HOH   A O   1 
HETATM 4055 O  O   . HOH   D 4 .   ? -0.79046  -31.28121 -1.32283  1.000 35.99626 ?  766 HOH   A O   1 
HETATM 4056 O  O   . HOH   D 4 .   ? 10.22107  14.76373  -66.65063 1.000 39.99806 ?  767 HOH   A O   1 
HETATM 4057 O  O   . HOH   D 4 .   ? 8.19498   -23.70944 -2.05438  1.000 32.69805 ?  768 HOH   A O   1 
HETATM 4058 O  O   . HOH   D 4 .   ? 9.24935   -46.91847 -15.72842 1.000 42.89238 ?  769 HOH   A O   1 
HETATM 4059 O  O   . HOH   D 4 .   ? -18.53612 9.69721   -69.44920 1.000 33.83158 ?  770 HOH   A O   1 
HETATM 4060 O  O   . HOH   D 4 .   ? 20.75475  -12.55472 -25.68170 1.000 38.80314 ?  771 HOH   A O   1 
HETATM 4061 O  O   . HOH   D 4 .   ? -7.70556  -20.78346 -11.51589 1.000 25.42924 ?  772 HOH   A O   1 
HETATM 4062 O  O   . HOH   D 4 .   ? 8.71302   15.42020  -22.06719 1.000 37.05701 ?  773 HOH   A O   1 
HETATM 4063 O  O   . HOH   D 4 .   ? -2.22636  -10.55542 -2.50537  1.000 36.76246 ?  774 HOH   A O   1 
HETATM 4064 O  O   . HOH   D 4 .   ? 10.87996  -33.90917 -24.03808 1.000 33.95160 ?  775 HOH   A O   1 
HETATM 4065 O  O   . HOH   D 4 .   ? 28.02003  -0.80147  -31.29999 1.000 32.03539 ?  776 HOH   A O   1 
HETATM 4066 O  O   . HOH   D 4 .   ? 16.52994  9.79347   -53.55751 1.000 33.65719 ?  777 HOH   A O   1 
HETATM 4067 O  O   . HOH   D 4 .   ? 11.48212  12.01857  -64.71568 1.000 25.54058 ?  778 HOH   A O   1 
HETATM 4068 O  O   . HOH   D 4 .   ? 1.15729   -33.39711 -23.37429 1.000 28.85050 ?  779 HOH   A O   1 
HETATM 4069 O  O   . HOH   D 4 .   ? 14.22966  -21.84198 -7.17142  1.000 35.36777 ?  780 HOH   A O   1 
HETATM 4070 O  O   . HOH   D 4 .   ? 0.34953   -35.97942 -8.51759  1.000 34.52223 ?  781 HOH   A O   1 
HETATM 4071 O  O   . HOH   D 4 .   ? 17.93261  -7.84331  -4.13065  1.000 34.15647 ?  782 HOH   A O   1 
HETATM 4072 O  O   . HOH   D 4 .   ? 21.01859  -7.63053  -33.45931 1.000 23.48453 ?  783 HOH   A O   1 
HETATM 4073 O  O   . HOH   D 4 .   ? 22.97030  8.37908   -41.11489 1.000 32.54453 ?  784 HOH   A O   1 
HETATM 4074 O  O   . HOH   D 4 .   ? -19.32430 -46.14269 -18.91879 1.000 33.01878 ?  785 HOH   A O   1 
HETATM 4075 O  O   . HOH   D 4 .   ? 18.60304  -19.87737 -19.51804 1.000 27.92238 ?  786 HOH   A O   1 
HETATM 4076 O  O   . HOH   D 4 .   ? 15.35952  -13.36262 -8.27445  1.000 28.93662 ?  787 HOH   A O   1 
HETATM 4077 O  O   . HOH   D 4 .   ? 13.35855  -22.97266 -24.12029 1.000 32.08963 ?  788 HOH   A O   1 
HETATM 4078 O  O   . HOH   D 4 .   ? 17.79098  3.05830   -15.26313 1.000 41.35924 ?  789 HOH   A O   1 
HETATM 4079 O  O   . HOH   D 4 .   ? -0.14040  9.10797   -71.35998 1.000 38.67646 ?  790 HOH   A O   1 
HETATM 4080 O  O   . HOH   D 4 .   ? 12.62574  -19.60123 -6.00785  1.000 33.54910 ?  791 HOH   A O   1 
HETATM 4081 O  O   . HOH   D 4 .   ? 21.36408  -7.98670  -39.69016 1.000 38.97334 ?  792 HOH   A O   1 
HETATM 4082 O  O   . HOH   D 4 .   ? -13.89580 8.98528   -59.47962 1.000 37.67530 ?  793 HOH   A O   1 
HETATM 4083 O  O   . HOH   D 4 .   ? 8.24237   -2.21711  -26.09389 1.000 34.41945 ?  794 HOH   A O   1 
HETATM 4084 O  O   . HOH   D 4 .   ? -11.00746 -14.72043 -23.16939 1.000 36.52516 ?  795 HOH   A O   1 
HETATM 4085 O  O   . HOH   D 4 .   ? 8.26855   -25.48433 -5.29516  1.000 40.14348 ?  796 HOH   A O   1 
HETATM 4086 O  O   . HOH   D 4 .   ? -15.43805 -27.08290 -23.06486 1.000 39.18986 ?  797 HOH   A O   1 
HETATM 4087 O  O   . HOH   D 4 .   ? 15.71023  -29.80341 -8.80115  1.000 37.78590 ?  798 HOH   A O   1 
HETATM 4088 O  O   . HOH   D 4 .   ? 10.59508  17.78036  -35.62046 1.000 33.09076 ?  799 HOH   A O   1 
HETATM 4089 O  O   . HOH   D 4 .   ? -13.24213 -29.47154 -28.89477 1.000 43.51752 ?  800 HOH   A O   1 
HETATM 4090 O  O   . HOH   D 4 .   ? 1.57381   -3.02213  -60.07170 1.000 31.59283 ?  801 HOH   A O   1 
HETATM 4091 O  O   . HOH   D 4 .   ? 11.48389  13.63699  -61.02088 1.000 34.07871 ?  802 HOH   A O   1 
HETATM 4092 O  O   . HOH   D 4 .   ? 6.56560   -3.47933  -37.35419 1.000 37.76436 ?  803 HOH   A O   1 
HETATM 4093 O  O   . HOH   D 4 .   ? -5.37419  -37.80516 -4.50032  1.000 33.38169 ?  804 HOH   A O   1 
HETATM 4094 O  O   . HOH   D 4 .   ? 2.25960   -19.75395 -23.81751 1.000 38.78409 ?  805 HOH   A O   1 
HETATM 4095 O  O   . HOH   D 4 .   ? 13.60847  8.28386   -60.91323 1.000 31.57713 ?  806 HOH   A O   1 
HETATM 4096 O  O   . HOH   D 4 .   ? 9.64728   -6.85969  -29.90489 1.000 31.80325 ?  807 HOH   A O   1 
HETATM 4097 O  O   . HOH   D 4 .   ? -20.79576 -38.33298 -21.73154 1.000 37.71902 ?  808 HOH   A O   1 
HETATM 4098 O  O   . HOH   D 4 .   ? 9.00877   -6.01972  -6.37657  1.000 31.61402 ?  809 HOH   A O   1 
HETATM 4099 O  O   . HOH   D 4 .   ? -12.43555 -47.05699 -13.87222 1.000 36.58650 ?  810 HOH   A O   1 
HETATM 4100 O  O   . HOH   D 4 .   ? 13.02210  13.75579  -64.12885 1.000 37.94714 ?  811 HOH   A O   1 
HETATM 4101 O  O   . HOH   D 4 .   ? 1.93228   -6.00952  -10.08154 1.000 31.65461 ?  812 HOH   A O   1 
HETATM 4102 O  O   . HOH   D 4 .   ? 3.36094   -4.54692  -8.62753  1.000 31.98925 ?  813 HOH   A O   1 
HETATM 4103 O  O   . HOH   D 4 .   ? 7.22037   -3.06983  -28.27172 1.000 32.68290 ?  814 HOH   A O   1 
HETATM 4104 O  O   . HOH   D 4 .   ? 8.98425   -5.53200  -38.41537 1.000 37.61425 ?  815 HOH   A O   1 
HETATM 4105 O  O   . HOH   D 4 .   ? 5.94763   -11.26628 -24.21303 1.000 37.58700 ?  816 HOH   A O   1 
HETATM 4106 O  O   . HOH   D 4 .   ? -2.66079  -41.50408 -30.30933 1.000 29.96340 ?  817 HOH   A O   1 
HETATM 4107 O  O   . HOH   D 4 .   ? 26.52753  10.23265  -37.63342 1.000 33.42594 ?  818 HOH   A O   1 
HETATM 4108 O  O   . HOH   D 4 .   ? 6.67481   10.67798  -67.70069 1.000 34.61699 ?  819 HOH   A O   1 
HETATM 4109 O  O   . HOH   D 4 .   ? 27.45457  -9.34002  -20.46923 1.000 47.32212 ?  820 HOH   A O   1 
HETATM 4110 O  O   . HOH   D 4 .   ? 20.24281  20.32827  -39.99215 1.000 37.35325 ?  821 HOH   A O   1 
HETATM 4111 O  O   . HOH   D 4 .   ? 25.94472  -7.35981  -33.84785 1.000 34.69359 ?  822 HOH   A O   1 
HETATM 4112 O  O   . HOH   D 4 .   ? 2.85217   -32.03466 -3.90453  1.000 37.28412 ?  823 HOH   A O   1 
HETATM 4113 O  O   . HOH   D 4 .   ? 27.42872  -11.73191 -20.85143 1.000 38.53381 ?  824 HOH   A O   1 
HETATM 4114 O  O   . HOH   D 4 .   ? 23.06149  -12.26015 -22.37047 1.000 39.56084 ?  825 HOH   A O   1 
HETATM 4115 O  O   . HOH   D 4 .   ? 7.94702   8.26435   -11.76804 1.000 38.74209 ?  826 HOH   A O   1 
HETATM 4116 O  O   . HOH   D 4 .   ? 9.63583   -9.01041  -32.64859 1.000 41.23226 ?  827 HOH   A O   1 
HETATM 4117 O  O   . HOH   D 4 .   ? -11.12088 20.02294  -51.75445 1.000 42.51157 ?  828 HOH   A O   1 
HETATM 4118 O  O   . HOH   D 4 .   ? 2.04273   0.72777   -45.23611 1.000 34.21505 ?  829 HOH   A O   1 
HETATM 4119 O  O   . HOH   D 4 .   ? -11.61059 -29.05459 -0.56968  1.000 41.44445 ?  830 HOH   A O   1 
HETATM 4120 O  O   . HOH   D 4 .   ? -5.66948  -13.70137 -1.19850  1.000 36.80143 ?  831 HOH   A O   1 
HETATM 4121 O  O   . HOH   D 4 .   ? 10.73165  -2.64026  -54.94134 1.000 34.52431 ?  832 HOH   A O   1 
HETATM 4122 O  O   . HOH   D 4 .   ? 8.96740   10.38657  -65.47916 1.000 25.41573 ?  833 HOH   A O   1 
HETATM 4123 O  O   . HOH   D 4 .   ? -15.92260 -51.29008 -27.88738 1.000 49.66272 ?  834 HOH   A O   1 
HETATM 4124 O  O   . HOH   D 4 .   ? -19.36969 -33.41717 -15.21397 1.000 51.35544 ?  835 HOH   A O   1 
HETATM 4125 O  O   . HOH   D 4 .   ? 24.90549  9.58661   -40.32112 1.000 37.31492 ?  836 HOH   A O   1 
HETATM 4126 O  O   . HOH   D 4 .   ? 16.65530  -13.52300 -5.84780  1.000 33.64686 ?  837 HOH   A O   1 
HETATM 4127 O  O   . HOH   D 4 .   ? 6.33085   -10.63775 -26.63371 1.000 38.33032 ?  838 HOH   A O   1 
HETATM 4128 O  O   . HOH   D 4 .   ? 19.14949  -14.86680 -5.50190  1.000 43.24114 ?  839 HOH   A O   1 
HETATM 4129 O  O   . HOH   D 4 .   ? 1.80931   -39.75629 -6.79808  1.000 42.11149 ?  840 HOH   A O   1 
HETATM 4130 O  O   . HOH   D 4 .   ? 19.81909  -7.45482  -35.53813 1.000 28.67873 ?  841 HOH   A O   1 
HETATM 4131 O  O   . HOH   D 4 .   ? 2.41025   -2.54448  -6.35994  1.000 28.49791 ?  842 HOH   A O   1 
HETATM 4132 O  O   . HOH   D 4 .   ? 1.12255   13.84136  -38.59528 1.000 38.74637 ?  843 HOH   A O   1 
HETATM 4133 O  O   . HOH   D 4 .   ? -17.02161 -41.15213 -9.61172  1.000 49.67816 ?  844 HOH   A O   1 
HETATM 4134 O  O   . HOH   D 4 .   ? 3.12496   2.99328   -44.35738 1.000 34.84745 ?  845 HOH   A O   1 
HETATM 4135 O  O   . HOH   D 4 .   ? -17.99096 -39.63378 -11.03520 1.000 37.93761 ?  846 HOH   A O   1 
HETATM 4136 O  O   . HOH   D 4 .   ? 13.20694  -35.36349 -24.92643 1.000 41.12784 ?  847 HOH   A O   1 
HETATM 4137 O  O   . HOH   D 4 .   ? 19.74009  -9.36909  -37.80193 1.000 37.88323 ?  848 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . LYS   A 7   ? 0.55102 0.53245 0.49320 -0.02524 -0.03336 0.03283  84  LYS   A N   
2    C  CA  . LYS   A 7   ? 0.62402 0.59761 0.55610 -0.02796 -0.03244 0.03003  84  LYS   A CA  
3    C  C   . LYS   A 7   ? 0.66068 0.63605 0.59125 -0.03066 -0.03578 0.03462  84  LYS   A C   
4    O  O   . LYS   A 7   ? 0.67471 0.65130 0.60177 -0.03602 -0.04036 0.03844  84  LYS   A O   
5    C  CB  . LYS   A 7   ? 0.65142 0.61738 0.57245 -0.03309 -0.03296 0.02697  84  LYS   A CB  
6    C  CG  . LYS   A 7   ? 0.71402 0.67075 0.62551 -0.03347 -0.02931 0.02183  84  LYS   A CG  
7    C  CD  . LYS   A 7   ? 0.65532 0.61130 0.56450 -0.03407 -0.02965 0.02332  84  LYS   A CD  
8    C  CE  . LYS   A 7   ? 0.66229 0.61230 0.56734 -0.03151 -0.02457 0.01831  84  LYS   A CE  
9    N  NZ  . LYS   A 7   ? 0.68925 0.64001 0.59476 -0.03076 -0.02439 0.01983  84  LYS   A NZ  
10   N  N   . SER   A 8   ? 0.60422 0.57934 0.53678 -0.02738 -0.03367 0.03431  85  SER   A N   
11   C  CA  . SER   A 8   ? 0.53336 0.51103 0.46633 -0.02882 -0.03656 0.03905  85  SER   A CA  
12   C  C   . SER   A 8   ? 0.56842 0.53839 0.49033 -0.03264 -0.03626 0.03677  85  SER   A C   
13   O  O   . SER   A 8   ? 0.58165 0.54597 0.49970 -0.03082 -0.03209 0.03177  85  SER   A O   
14   C  CB  . SER   A 8   ? 0.56630 0.54850 0.50861 -0.02263 -0.03461 0.04083  85  SER   A CB  
15   O  OG  . SER   A 8   ? 0.59999 0.58989 0.55250 -0.01922 -0.03529 0.04426  85  SER   A OG  
16   N  N   . SER   A 9   ? 0.54682 0.51694 0.46387 -0.03794 -0.04067 0.04078  86  SER   A N   
17   C  CA  . SER   A 9   ? 0.52236 0.48582 0.42952 -0.04133 -0.04056 0.03947  86  SER   A CA  
18   C  C   . SER   A 9   ? 0.52181 0.48744 0.43375 -0.03758 -0.03936 0.04108  86  SER   A C   
19   O  O   . SER   A 9   ? 0.52275 0.49506 0.44499 -0.03313 -0.03954 0.04429  86  SER   A O   
20   C  CB  . SER   A 9   ? 0.52289 0.48528 0.42245 -0.04877 -0.04597 0.04339  86  SER   A CB  
21   O  OG  . SER   A 9   ? 0.54437 0.51548 0.45189 -0.04882 -0.05027 0.05046  86  SER   A OG  
22   N  N   . ASN   A 10  ? 0.51629 0.47560 0.41997 -0.03950 -0.03797 0.03884  87  ASN   A N   
23   C  CA  . ASN   A 10  ? 0.47870 0.43885 0.38491 -0.03705 -0.03722 0.04042  87  ASN   A CA  
24   C  C   . ASN   A 10  ? 0.47995 0.44728 0.39287 -0.03706 -0.04168 0.04756  87  ASN   A C   
25   O  O   . ASN   A 10  ? 0.45928 0.43043 0.38021 -0.03215 -0.04068 0.04965  87  ASN   A O   
26   C  CB  . ASN   A 10  ? 0.45861 0.41113 0.35331 -0.04097 -0.03631 0.03802  87  ASN   A CB  
27   C  CG  . ASN   A 10  ? 0.49613 0.44849 0.39240 -0.03867 -0.03507 0.03893  87  ASN   A CG  
28   O  OD1 . ASN   A 10  ? 0.49264 0.44417 0.39219 -0.03426 -0.03097 0.03583  87  ASN   A OD1 
29   N  ND2 . ASN   A 10  ? 0.48465 0.43752 0.37801 -0.04206 -0.03880 0.04334  87  ASN   A ND2 
30   N  N   . ALA   A 11  ? 0.45253 0.42154 0.36200 -0.04262 -0.04661 0.05160  88  ALA   A N   
31   C  CA  . ALA   A 11  ? 0.45611 0.43269 0.37209 -0.04299 -0.05114 0.05914  88  ALA   A CA  
32   C  C   . ALA   A 11  ? 0.48543 0.47058 0.41440 -0.03754 -0.05089 0.06215  88  ALA   A C   
33   O  O   . ALA   A 11  ? 0.48189 0.47274 0.41901 -0.03386 -0.05169 0.06702  88  ALA   A O   
34   C  CB  . ALA   A 11  ? 0.44853 0.42528 0.35767 -0.05083 -0.05678 0.06296  88  ALA   A CB  
35   N  N   . GLU   A 12  ? 0.44663 0.43256 0.37747 -0.03683 -0.04964 0.05950  89  GLU   A N   
36   C  CA  . GLU   A 12  ? 0.48922 0.48261 0.43200 -0.03121 -0.04858 0.06166  89  GLU   A CA  
37   C  C   . GLU   A 12  ? 0.43743 0.42973 0.38553 -0.02404 -0.04378 0.05922  89  GLU   A C   
38   O  O   . GLU   A 12  ? 0.48031 0.47840 0.43779 -0.01907 -0.04340 0.06310  89  GLU   A O   
39   C  CB  . GLU   A 12  ? 0.51318 0.50653 0.45586 -0.03203 -0.04785 0.05857  89  GLU   A CB  
40   C  CG  . GLU   A 12  ? 0.54612 0.54036 0.48350 -0.03930 -0.05279 0.06125  89  GLU   A CG  
41   C  CD  . GLU   A 12  ? 0.65916 0.65366 0.59735 -0.03958 -0.05201 0.05860  89  GLU   A CD  
42   O  OE1 . GLU   A 12  ? 0.65570 0.65805 0.60432 -0.03585 -0.05200 0.06151  89  GLU   A OE1 
43   O  OE2 . GLU   A 12  ? 0.68401 0.67057 0.61230 -0.04320 -0.05109 0.05360  89  GLU   A OE2 
44   N  N   . VAL   A 13  ? 0.44164 0.42638 0.38368 -0.02342 -0.03996 0.05298  90  VAL   A N   
45   C  CA  . VAL   A 13  ? 0.45854 0.44168 0.40461 -0.01746 -0.03580 0.05082  90  VAL   A CA  
46   C  C   . VAL   A 13  ? 0.46024 0.44481 0.40845 -0.01607 -0.03718 0.05550  90  VAL   A C   
47   O  O   . VAL   A 13  ? 0.47517 0.46218 0.43056 -0.01055 -0.03555 0.05752  90  VAL   A O   
48   C  CB  . VAL   A 13  ? 0.46090 0.43630 0.39980 -0.01786 -0.03190 0.04395  90  VAL   A CB  
49   C  CG1 . VAL   A 13  ? 0.43536 0.40882 0.37734 -0.01283 -0.02837 0.04245  90  VAL   A CG1 
50   C  CG2 . VAL   A 13  ? 0.44620 0.42045 0.38434 -0.01798 -0.03001 0.03956  90  VAL   A CG2 
51   N  N   . ILE   A 14  ? 0.42802 0.41062 0.36954 -0.02109 -0.04021 0.05743  91  ILE   A N   
52   C  CA  . ILE   A 14  ? 0.45094 0.43513 0.39418 -0.02036 -0.04214 0.06252  91  ILE   A CA  
53   C  C   . ILE   A 14  ? 0.41974 0.41272 0.37311 -0.01747 -0.04461 0.06951  91  ILE   A C   
54   O  O   . ILE   A 14  ? 0.43293 0.42765 0.39217 -0.01243 -0.04346 0.07257  91  ILE   A O   
55   C  CB  . ILE   A 14  ? 0.43748 0.41841 0.37133 -0.02711 -0.04549 0.06366  91  ILE   A CB  
56   C  CG1 . ILE   A 14  ? 0.48477 0.45710 0.40927 -0.02883 -0.04218 0.05709  91  ILE   A CG1 
57   C  CG2 . ILE   A 14  ? 0.40883 0.39255 0.34529 -0.02661 -0.04822 0.06991  91  ILE   A CG2 
58   C  CD1 . ILE   A 14  ? 0.52417 0.49204 0.43765 -0.03592 -0.04481 0.05702  91  ILE   A CD1 
59   N  N   . LYS   A 15  ? 0.41089 0.40941 0.36622 -0.02066 -0.04797 0.07244  92  LYS   A N   
60   C  CA  . LYS   A 15  ? 0.42973 0.43780 0.39548 -0.01790 -0.05023 0.07964  92  LYS   A CA  
61   C  C   . LYS   A 15  ? 0.44405 0.45388 0.41849 -0.00976 -0.04577 0.07890  92  LYS   A C   
62   O  O   . LYS   A 15  ? 0.42919 0.44444 0.41168 -0.00524 -0.04591 0.08459  92  LYS   A O   
63   C  CB  . LYS   A 15  ? 0.43715 0.45089 0.40391 -0.02250 -0.05398 0.08210  92  LYS   A CB  
64   C  CG  . LYS   A 15  ? 0.57997 0.59156 0.53710 -0.03141 -0.05892 0.08325  92  LYS   A CG  
65   C  CD  . LYS   A 15  ? 0.57963 0.59787 0.53869 -0.03616 -0.06341 0.08728  92  LYS   A CD  
66   C  CE  . LYS   A 15  ? 0.51804 0.52910 0.46507 -0.04345 -0.06473 0.08238  92  LYS   A CE  
67   N  NZ  . LYS   A 15  ? 0.56293 0.56739 0.49793 -0.05029 -0.06756 0.08212  92  LYS   A NZ  
68   N  N   . GLU   A 16  ? 0.41658 0.42157 0.38921 -0.00774 -0.04168 0.07212  93  GLU   A N   
69   C  CA  . GLU   A 16  ? 0.45089 0.45699 0.43082 -0.00061 -0.03756 0.07115  93  GLU   A CA  
70   C  C   . GLU   A 16  ? 0.44381 0.44486 0.42350 0.00405  -0.03449 0.07052  93  GLU   A C   
71   O  O   . GLU   A 16  ? 0.42362 0.42685 0.41009 0.01007  -0.03247 0.07341  93  GLU   A O   
72   C  CB  . GLU   A 16  ? 0.43741 0.44026 0.41531 -0.00056 -0.03465 0.06443  93  GLU   A CB  
73   C  CG  . GLU   A 16  ? 0.52231 0.52579 0.50679 0.00615  -0.03050 0.06301  93  GLU   A CG  
74   C  CD  . GLU   A 16  ? 0.58481 0.59729 0.57902 0.00925  -0.03154 0.06892  93  GLU   A CD  
75   O  OE1 . GLU   A 16  ? 0.52547 0.54418 0.52120 0.00518  -0.03563 0.07293  93  GLU   A OE1 
76   O  OE2 . GLU   A 16  ? 0.62815 0.64126 0.62811 0.01561  -0.02821 0.06967  93  GLU   A OE2 
77   N  N   . LEU   A 17  ? 0.43081 0.42471 0.40233 0.00134  -0.03393 0.06681  94  LEU   A N   
78   C  CA  . LEU   A 17  ? 0.44318 0.43205 0.41352 0.00474  -0.03174 0.06680  94  LEU   A CA  
79   C  C   . LEU   A 17  ? 0.43867 0.43167 0.41331 0.00640  -0.03425 0.07434  94  LEU   A C   
80   O  O   . LEU   A 17  ? 0.47995 0.47181 0.45846 0.01207  -0.03201 0.07652  94  LEU   A O   
81   C  CB  . LEU   A 17  ? 0.44514 0.42676 0.40592 0.00057  -0.03135 0.06232  94  LEU   A CB  
82   C  CG  . LEU   A 17  ? 0.45838 0.43598 0.41399 -0.00181 -0.02914 0.05537  94  LEU   A CG  
83   C  CD1 . LEU   A 17  ? 0.48854 0.46037 0.43521 -0.00606 -0.02937 0.05301  94  LEU   A CD1 
84   C  CD2 . LEU   A 17  ? 0.48517 0.46009 0.44375 0.00327  -0.02468 0.05151  94  LEU   A CD2 
85   N  N   . ASN   A 18  ? 0.42407 0.42138 0.39750 0.00140  -0.03892 0.07853  95  ASN   A N   
86   C  CA  . ASN   A 18  ? 0.46631 0.46844 0.44435 0.00278  -0.04165 0.08635  95  ASN   A CA  
87   C  C   . ASN   A 18  ? 0.44442 0.45425 0.43348 0.00869  -0.04085 0.09159  95  ASN   A C   
88   O  O   . ASN   A 18  ? 0.46798 0.47951 0.46199 0.01347  -0.04029 0.09679  95  ASN   A O   
89   C  CB  . ASN   A 18  ? 0.43045 0.43604 0.40479 -0.00445 -0.04721 0.09002  95  ASN   A CB  
90   C  CG  . ASN   A 18  ? 0.52990 0.53918 0.50744 -0.00367 -0.05012 0.09772  95  ASN   A CG  
91   O  OD1 . ASN   A 18  ? 0.59451 0.59810 0.56750 -0.00345 -0.04956 0.09732  95  ASN   A OD1 
92   N  ND2 . ASN   A 18  ? 0.47988 0.49906 0.46557 -0.00319 -0.05328 0.10516  95  ASN   A ND2 
93   N  N   . LYS   A 19  ? 0.42824 0.44260 0.42118 0.00871  -0.04052 0.09043  96  LYS   A N   
94   C  CA  . LYS   A 19  ? 0.45679 0.47835 0.46017 0.01466  -0.03912 0.09510  96  LYS   A CA  
95   C  C   . LYS   A 19  ? 0.45826 0.47399 0.46323 0.02225  -0.03354 0.09265  96  LYS   A C   
96   O  O   . LYS   A 19  ? 0.45395 0.47215 0.46508 0.02814  -0.03210 0.09793  96  LYS   A O   
97   C  CB  . LYS   A 19  ? 0.43131 0.45810 0.43756 0.01266  -0.03978 0.09369  96  LYS   A CB  
98   C  CG  . LYS   A 19  ? 0.43577 0.47145 0.45314 0.01805  -0.03875 0.09914  96  LYS   A CG  
99   C  CD  . LYS   A 19  ? 0.45399 0.49041 0.47273 0.01836  -0.03672 0.09463  96  LYS   A CD  
100  C  CE  . LYS   A 19  ? 0.46403 0.50959 0.49381 0.02368  -0.03548 0.10014  96  LYS   A CE  
101  N  NZ  . LYS   A 19  ? 0.50306 0.54635 0.53391 0.02676  -0.03140 0.09481  96  LYS   A NZ  
102  N  N   . CYS   A 20  ? 0.43289 0.44032 0.43173 0.02206  -0.03033 0.08482  97  CYS   A N   
103  C  CA  . CYS   A 20  ? 0.39355 0.39471 0.39277 0.02841  -0.02522 0.08198  97  CYS   A CA  
104  C  C   . CYS   A 20  ? 0.46535 0.46104 0.46237 0.03137  -0.02427 0.08443  97  CYS   A C   
105  O  O   . CYS   A 20  ? 0.49881 0.49246 0.49923 0.03796  -0.02099 0.08652  97  CYS   A O   
106  C  CB  . CYS   A 20  ? 0.47045 0.46468 0.46339 0.02644  -0.02275 0.07350  97  CYS   A CB  
107  S  SG  . CYS   A 20  ? 0.58628 0.57070 0.57660 0.03218  -0.01720 0.06926  97  CYS   A SG  
108  N  N   . ARG   A 21  ? 0.47933 0.47214 0.47032 0.02672  -0.02696 0.08444  98  ARG   A N   
109  C  CA  . ARG   A 21  ? 0.44648 0.43405 0.43544 0.02955  -0.02618 0.08711  98  ARG   A CA  
110  C  C   . ARG   A 21  ? 0.44469 0.43948 0.44136 0.03308  -0.02794 0.09605  98  ARG   A C   
111  O  O   . ARG   A 21  ? 0.45498 0.44647 0.45358 0.03913  -0.02535 0.09905  98  ARG   A O   
112  C  CB  . ARG   A 21  ? 0.47342 0.45574 0.45364 0.02368  -0.02836 0.08468  98  ARG   A CB  
113  C  CG  . ARG   A 21  ? 0.53378 0.52210 0.51342 0.01778  -0.03358 0.08855  98  ARG   A CG  
114  C  CD  . ARG   A 21  ? 0.47339 0.45622 0.44576 0.01438  -0.03526 0.08878  98  ARG   A CD  
115  N  NE  . ARG   A 21  ? 0.53047 0.51720 0.50731 0.01665  -0.03754 0.09678  98  ARG   A NE  
116  C  CZ  . ARG   A 21  ? 0.50855 0.50356 0.48880 0.01341  -0.04217 0.10273  98  ARG   A CZ  
117  N  NH1 . ARG   A 21  ? 0.46293 0.46203 0.44137 0.00735  -0.04513 0.10129  98  ARG   A NH1 
118  N  NH2 . ARG   A 21  ? 0.51301 0.51204 0.49830 0.01622  -0.04395 0.11052  98  ARG   A NH2 
119  N  N   . GLU   A 22  ? 0.45901 0.46356 0.46009 0.02945  -0.03225 0.10064  99  GLU   A N   
120  C  CA  . GLU   A 22  ? 0.44595 0.45936 0.45589 0.03279  -0.03406 0.10987  99  GLU   A CA  
121  C  C   . GLU   A 22  ? 0.43744 0.45200 0.45474 0.04150  -0.02935 0.11192  99  GLU   A C   
122  O  O   . GLU   A 22  ? 0.43671 0.45065 0.45749 0.04738  -0.02763 0.11708  99  GLU   A O   
123  C  CB  . GLU   A 22  ? 0.43456 0.45890 0.44858 0.02729  -0.03914 0.11385  99  GLU   A CB  
124  C  CG  . GLU   A 22  ? 0.47189 0.50255 0.48815 0.02446  -0.04415 0.12188  99  GLU   A CG  
125  C  CD  . GLU   A 22  ? 0.60398 0.62964 0.61010 0.01643  -0.04782 0.11898  99  GLU   A CD  
126  O  OE1 . GLU   A 22  ? 0.57685 0.60332 0.57858 0.00984  -0.05029 0.11552  99  GLU   A OE1 
127  O  OE2 . GLU   A 22  ? 0.67317 0.69361 0.67525 0.01671  -0.04808 0.12013  99  GLU   A OE2 
128  N  N   . GLU   A 23  ? 0.40361 0.41943 0.42297 0.04255  -0.02704 0.10797  100 GLU   A N   
129  C  CA  . GLU   A 23  ? 0.46022 0.47779 0.48649 0.05037  -0.02258 0.10986  100 GLU   A CA  
130  C  C   . GLU   A 23  ? 0.47366 0.47902 0.49473 0.05581  -0.01701 0.10518  100 GLU   A C   
131  O  O   . GLU   A 23  ? 0.45390 0.45873 0.47924 0.06272  -0.01273 0.10649  100 GLU   A O   
132  C  CB  . GLU   A 23  ? 0.41031 0.43403 0.44040 0.04879  -0.02258 0.10754  100 GLU   A CB  
133  C  CG  . GLU   A 23  ? 0.46462 0.49932 0.49839 0.04244  -0.02842 0.11184  100 GLU   A CG  
134  C  CD  . GLU   A 23  ? 0.46138 0.50355 0.50053 0.04167  -0.02856 0.11149  100 GLU   A CD  
135  O  OE1 . GLU   A 23  ? 0.48049 0.51731 0.51566 0.04110  -0.02608 0.10423  100 GLU   A OE1 
136  O  OE2 . GLU   A 23  ? 0.42661 0.48028 0.47412 0.04149  -0.03128 0.11879  100 GLU   A OE2 
137  N  N   . ASN   A 24  ? 0.46688 0.46231 0.47855 0.05273  -0.01698 0.10004  101 ASN   A N   
138  C  CA  . ASN   A 24  ? 0.49122 0.47434 0.49665 0.05665  -0.01227 0.09540  101 ASN   A CA  
139  C  C   . ASN   A 24  ? 0.48774 0.46839 0.49315 0.05867  -0.00855 0.08993  101 ASN   A C   
140  O  O   . ASN   A 24  ? 0.51231 0.48525 0.51575 0.06410  -0.00397 0.08832  101 ASN   A O   
141  C  CB  . ASN   A 24  ? 0.48270 0.46238 0.49014 0.06387  -0.00968 0.10111  101 ASN   A CB  
142  C  CG  . ASN   A 24  ? 0.48042 0.46140 0.48700 0.06168  -0.01341 0.10629  101 ASN   A CG  
143  O  OD1 . ASN   A 24  ? 0.49264 0.46856 0.49177 0.05619  -0.01561 0.10287  101 ASN   A OD1 
144  N  ND2 . ASN   A 24  ? 0.41147 0.39986 0.42597 0.06586  -0.01418 0.11483  101 ASN   A ND2 
145  N  N   . SER   A 25  ? 0.43921 0.42580 0.44612 0.05405  -0.01057 0.08704  102 SER   A N   
146  C  CA  . SER   A 25  ? 0.43919 0.42448 0.44635 0.05516  -0.00766 0.08195  102 SER   A CA  
147  C  C   . SER   A 25  ? 0.51436 0.48797 0.51256 0.05410  -0.00505 0.07455  102 SER   A C   
148  O  O   . SER   A 25  ? 0.51364 0.48230 0.50529 0.04992  -0.00663 0.07205  102 SER   A O   
149  C  CB  . SER   A 25  ? 0.44371 0.43757 0.45370 0.04975  -0.01097 0.08080  102 SER   A CB  
150  O  OG  . SER   A 25  ? 0.58763 0.57707 0.59330 0.04750  -0.00937 0.07344  102 SER   A OG  
151  N  N   . MET   A 26  ? 0.50391 0.47328 0.50179 0.05779  -0.00104 0.07128  103 MET   A N   
152  C  CA  . MET   A 26  ? 0.46084 0.41948 0.45062 0.05689  0.00144  0.06480  103 MET   A CA  
153  C  C   . MET   A 26  ? 0.49099 0.45103 0.47932 0.05239  0.00090  0.05882  103 MET   A C   
154  O  O   . MET   A 26  ? 0.49749 0.45000 0.47942 0.05054  0.00231  0.05353  103 MET   A O   
155  C  CB  . MET   A 26  ? 0.49361 0.44469 0.48220 0.06354  0.00633  0.06479  103 MET   A CB  
156  C  CG  . MET   A 26  ? 0.65863 0.60722 0.64831 0.06891  0.00761  0.07079  103 MET   A CG  
157  S  SD  . MET   A 26  ? 0.80885 0.74184 0.79060 0.07470  0.01306  0.06919  103 MET   A SD  
158  C  CE  . MET   A 26  ? 0.62145 0.55249 0.60334 0.07807  0.01243  0.07616  103 MET   A CE  
159  N  N   . ARG   A 27  ? 0.52460 0.49401 0.51862 0.05057  -0.00111 0.05980  104 ARG   A N   
160  C  CA  . ARG   A 27  ? 0.54070 0.51173 0.53357 0.04645  -0.00171 0.05457  104 ARG   A CA  
161  C  C   . ARG   A 27  ? 0.58782 0.56619 0.58202 0.04099  -0.00610 0.05594  104 ARG   A C   
162  O  O   . ARG   A 27  ? 0.60720 0.59331 0.60713 0.04147  -0.00831 0.06138  104 ARG   A O   
163  C  CB  . ARG   A 27  ? 0.53357 0.50743 0.53120 0.04981  0.00071  0.05384  104 ARG   A CB  
164  C  CG  . ARG   A 27  ? 0.59894 0.58089 0.60023 0.04611  -0.00171 0.05300  104 ARG   A CG  
165  C  CD  . ARG   A 27  ? 0.66775 0.65364 0.67466 0.04965  0.00043  0.05341  104 ARG   A CD  
166  N  NE  . ARG   A 27  ? 0.71653 0.69600 0.71977 0.05039  0.00349  0.04768  104 ARG   A NE  
167  C  CZ  . ARG   A 27  ? 0.72210 0.69661 0.72507 0.05543  0.00737  0.04729  104 ARG   A CZ  
168  N  NH1 . ARG   A 27  ? 0.66127 0.63632 0.66763 0.06086  0.00923  0.05221  104 ARG   A NH1 
169  N  NH2 . ARG   A 27  ? 0.67675 0.64544 0.67571 0.05503  0.00952  0.04201  104 ARG   A NH2 
170  N  N   . LEU   A 28  ? 0.51292 0.48861 0.50146 0.03575  -0.00732 0.05135  105 LEU   A N   
171  C  CA  . LEU   A 28  ? 0.43416 0.41493 0.42203 0.03014  -0.01100 0.05147  105 LEU   A CA  
172  C  C   . LEU   A 28  ? 0.48442 0.46532 0.47111 0.02779  -0.01022 0.04616  105 LEU   A C   
173  O  O   . LEU   A 28  ? 0.43467 0.40976 0.41692 0.02719  -0.00808 0.04115  105 LEU   A O   
174  C  CB  . LEU   A 28  ? 0.47190 0.44888 0.45336 0.02609  -0.01285 0.05097  105 LEU   A CB  
175  C  CG  . LEU   A 28  ? 0.43551 0.41487 0.41337 0.01973  -0.01603 0.04978  105 LEU   A CG  
176  C  CD1 . LEU   A 28  ? 0.45601 0.44293 0.43785 0.01806  -0.01990 0.05559  105 LEU   A CD1 
177  C  CD2 . LEU   A 28  ? 0.46579 0.43931 0.43619 0.01646  -0.01634 0.04768  105 LEU   A CD2 
178  N  N   . ASP   A 29  ? 0.47372 0.46132 0.46451 0.02649  -0.01198 0.04757  106 ASP   A N   
179  C  CA  . ASP   A 29  ? 0.48808 0.47600 0.47784 0.02421  -0.01150 0.04301  106 ASP   A CA  
180  C  C   . ASP   A 29  ? 0.44730 0.43718 0.43337 0.01816  -0.01494 0.04276  106 ASP   A C   
181  O  O   . ASP   A 29  ? 0.47834 0.47419 0.46731 0.01637  -0.01807 0.04702  106 ASP   A O   
182  C  CB  . ASP   A 29  ? 0.48191 0.47489 0.47837 0.02737  -0.01052 0.04437  106 ASP   A CB  
183  C  CG  . ASP   A 29  ? 0.49863 0.49105 0.49386 0.02551  -0.00964 0.03941  106 ASP   A CG  
184  O  OD1 . ASP   A 29  ? 0.45593 0.44616 0.44593 0.02106  -0.01078 0.03617  106 ASP   A OD1 
185  O  OD2 . ASP   A 29  ? 0.59350 0.58735 0.59277 0.02871  -0.00759 0.03880  106 ASP   A OD2 
186  N  N   . LEU   A 30  ? 0.47635 0.46102 0.45572 0.01494  -0.01430 0.03799  107 LEU   A N   
187  C  CA  . LEU   A 30  ? 0.48359 0.46820 0.45781 0.00933  -0.01671 0.03672  107 LEU   A CA  
188  C  C   . LEU   A 30  ? 0.44008 0.42242 0.41187 0.00814  -0.01486 0.03133  107 LEU   A C   
189  O  O   . LEU   A 30  ? 0.45358 0.43258 0.41903 0.00438  -0.01506 0.02843  107 LEU   A O   
190  C  CB  . LEU   A 30  ? 0.50944 0.48975 0.47701 0.00632  -0.01753 0.03637  107 LEU   A CB  
191  C  CG  . LEU   A 30  ? 0.45632 0.43763 0.42402 0.00613  -0.01981 0.04136  107 LEU   A CG  
192  C  CD1 . LEU   A 30  ? 0.45524 0.43061 0.41575 0.00382  -0.01917 0.03910  107 LEU   A CD1 
193  C  CD2 . LEU   A 30  ? 0.43742 0.42385 0.40571 0.00253  -0.02412 0.04589  107 LEU   A CD2 
194  N  N   . SER   A 31  ? 0.43211 0.41598 0.40867 0.01148  -0.01285 0.03005  108 SER   A N   
195  C  CA  . SER   A 31  ? 0.42286 0.40475 0.39770 0.01077  -0.01101 0.02523  108 SER   A CA  
196  C  C   . SER   A 31  ? 0.42725 0.41184 0.40123 0.00729  -0.01340 0.02559  108 SER   A C   
197  O  O   . SER   A 31  ? 0.45666 0.44597 0.43323 0.00603  -0.01642 0.02996  108 SER   A O   
198  C  CB  . SER   A 31  ? 0.43538 0.41766 0.41519 0.01530  -0.00819 0.02387  108 SER   A CB  
199  O  OG  . SER   A 31  ? 0.46480 0.45250 0.45097 0.01768  -0.00921 0.02795  108 SER   A OG  
200  N  N   . LYS   A 32  ? 0.40093 0.38233 0.37102 0.00561  -0.01204 0.02118  109 LYS   A N   
201  C  CA  . LYS   A 32  ? 0.42447 0.40712 0.39332 0.00277  -0.01368 0.02078  109 LYS   A CA  
202  C  C   . LYS   A 32  ? 0.48738 0.47056 0.45180 -0.00212 -0.01754 0.02379  109 LYS   A C   
203  O  O   . LYS   A 32  ? 0.53410 0.52186 0.50110 -0.00382 -0.02057 0.02735  109 LYS   A O   
204  C  CB  . LYS   A 32  ? 0.38670 0.37465 0.36305 0.00551  -0.01378 0.02258  109 LYS   A CB  
205  C  CG  . LYS   A 32  ? 0.42337 0.41018 0.40329 0.01001  -0.01007 0.01961  109 LYS   A CG  
206  C  CD  . LYS   A 32  ? 0.38761 0.37906 0.37407 0.01248  -0.00988 0.02094  109 LYS   A CD  
207  C  CE  . LYS   A 32  ? 0.47827 0.47558 0.47058 0.01425  -0.01161 0.02664  109 LYS   A CE  
208  N  NZ  . LYS   A 32  ? 0.47328 0.46943 0.46782 0.01839  -0.00960 0.02785  109 LYS   A NZ  
209  N  N   . ARG   A 33  ? 0.44529 0.42375 0.40274 -0.00467 -0.01749 0.02250  110 ARG   A N   
210  C  CA  . ARG   A 33  ? 0.43882 0.41692 0.39114 -0.00943 -0.02111 0.02544  110 ARG   A CA  
211  C  C   . ARG   A 33  ? 0.46407 0.43497 0.40601 -0.01331 -0.02035 0.02192  110 ARG   A C   
212  O  O   . ARG   A 33  ? 0.52084 0.49022 0.45692 -0.01780 -0.02328 0.02399  110 ARG   A O   
213  C  CB  . ARG   A 33  ? 0.47301 0.45374 0.42826 -0.00819 -0.02243 0.02960  110 ARG   A CB  
214  C  CG  . ARG   A 33  ? 0.47971 0.46798 0.44306 -0.00653 -0.02497 0.03532  110 ARG   A CG  
215  C  CD  . ARG   A 33  ? 0.48032 0.46998 0.44540 -0.00528 -0.02597 0.03924  110 ARG   A CD  
216  N  NE  . ARG   A 33  ? 0.48498 0.48169 0.45922 -0.00160 -0.02688 0.04449  110 ARG   A NE  
217  C  CZ  . ARG   A 33  ? 0.54900 0.55123 0.52610 -0.00314 -0.03059 0.05068  110 ARG   A CZ  
218  N  NH1 . ARG   A 33  ? 0.53399 0.53520 0.50506 -0.00871 -0.03414 0.05242  110 ARG   A NH1 
219  N  NH2 . ARG   A 33  ? 0.56146 0.57036 0.54756 0.00105  -0.03066 0.05548  110 ARG   A NH2 
220  N  N   . SER   A 34  ? 0.41818 0.38467 0.35757 -0.01169 -0.01644 0.01697  111 SER   A N   
221  C  CA  . SER   A 34  ? 0.51576 0.47528 0.44536 -0.01470 -0.01490 0.01360  111 SER   A CA  
222  C  C   . SER   A 34  ? 0.51284 0.47010 0.43774 -0.01658 -0.01548 0.01482  111 SER   A C   
223  O  O   . SER   A 34  ? 0.56306 0.51526 0.47886 -0.02068 -0.01608 0.01405  111 SER   A O   
224  C  CB  . SER   A 34  ? 0.54713 0.50339 0.46975 -0.01930 -0.01700 0.01329  111 SER   A CB  
225  O  OG  . SER   A 34  ? 0.62063 0.57937 0.54764 -0.01806 -0.01714 0.01284  111 SER   A OG  
226  N  N   . ILE   A 35  ? 0.49264 0.45295 0.42295 -0.01375 -0.01526 0.01677  112 ILE   A N   
227  C  CA  . ILE   A 35  ? 0.45087 0.40897 0.37688 -0.01542 -0.01575 0.01798  112 ILE   A CA  
228  C  C   . ILE   A 35  ? 0.46737 0.42027 0.38799 -0.01521 -0.01173 0.01365  112 ILE   A C   
229  O  O   . ILE   A 35  ? 0.48958 0.44274 0.41381 -0.01182 -0.00841 0.01088  112 ILE   A O   
230  C  CB  . ILE   A 35  ? 0.44512 0.40731 0.37820 -0.01221 -0.01651 0.02137  112 ILE   A CB  
231  C  CG1 . ILE   A 35  ? 0.44800 0.41600 0.38669 -0.01223 -0.02031 0.02637  112 ILE   A CG1 
232  C  CG2 . ILE   A 35  ? 0.42300 0.38237 0.35159 -0.01363 -0.01657 0.02221  112 ILE   A CG2 
233  C  CD1 . ILE   A 35  ? 0.47529 0.44697 0.42139 -0.00802 -0.02034 0.02970  112 ILE   A CD1 
234  N  N   . HIS   A 36  ? 0.46744 0.41578 0.37931 -0.01897 -0.01199 0.01329  113 HIS   A N   
235  C  CA  . HIS   A 36  ? 0.46554 0.40927 0.37192 -0.01897 -0.00806 0.00982  113 HIS   A CA  
236  C  C   . HIS   A 36  ? 0.51875 0.46289 0.42588 -0.01824 -0.00753 0.01108  113 HIS   A C   
237  O  O   . HIS   A 36  ? 0.50128 0.44420 0.40827 -0.01653 -0.00395 0.00869  113 HIS   A O   
238  C  CB  . HIS   A 36  ? 0.49871 0.43613 0.39380 -0.02346 -0.00801 0.00840  113 HIS   A CB  
239  C  CG  . HIS   A 36  ? 0.46671 0.40095 0.35865 -0.02355 -0.00616 0.00527  113 HIS   A CG  
240  N  ND1 . HIS   A 36  ? 0.46901 0.40250 0.35863 -0.02628 -0.00924 0.00631  113 HIS   A ND1 
241  C  CD2 . HIS   A 36  ? 0.48064 0.41209 0.37112 -0.02134 -0.00157 0.00140  113 HIS   A CD2 
242  C  CE1 . HIS   A 36  ? 0.49611 0.42581 0.38256 -0.02569 -0.00658 0.00295  113 HIS   A CE1 
243  N  NE2 . HIS   A 36  ? 0.53403 0.46255 0.42115 -0.02248 -0.00182 -0.00002 113 HIS   A NE2 
244  N  N   . ILE   A 37  ? 0.49100 0.43688 0.39883 -0.01966 -0.01108 0.01505  114 ILE   A N   
245  C  CA  . ILE   A 37  ? 0.49500 0.44075 0.40313 -0.01913 -0.01089 0.01654  114 ILE   A CA  
246  C  C   . ILE   A 37  ? 0.53848 0.48854 0.45315 -0.01759 -0.01422 0.02107  114 ILE   A C   
247  O  O   . ILE   A 37  ? 0.55412 0.50682 0.47020 -0.01895 -0.01761 0.02402  114 ILE   A O   
248  C  CB  . ILE   A 37  ? 0.53153 0.47267 0.42997 -0.02344 -0.01112 0.01653  114 ILE   A CB  
249  C  CG1 . ILE   A 37  ? 0.58843 0.52928 0.48722 -0.02280 -0.01055 0.01778  114 ILE   A CG1 
250  C  CG2 . ILE   A 37  ? 0.48638 0.42699 0.38022 -0.02778 -0.01557 0.01966  114 ILE   A CG2 
251  C  CD1 . ILE   A 37  ? 0.61540 0.55180 0.50465 -0.02699 -0.01057 0.01783  114 ILE   A CD1 
252  N  N   . LEU   A 38  ? 0.53746 0.48822 0.45622 -0.01461 -0.01309 0.02179  115 LEU   A N   
253  C  CA  . LEU   A 38  ? 0.53208 0.48597 0.45662 -0.01241 -0.01547 0.02609  115 LEU   A CA  
254  C  C   . LEU   A 38  ? 0.54326 0.49533 0.46348 -0.01488 -0.01745 0.02897  115 LEU   A C   
255  O  O   . LEU   A 38  ? 0.57176 0.52045 0.48832 -0.01535 -0.01545 0.02730  115 LEU   A O   
256  C  CB  . LEU   A 38  ? 0.52053 0.47488 0.45103 -0.00766 -0.01292 0.02508  115 LEU   A CB  
257  C  CG  . LEU   A 38  ? 0.52460 0.48142 0.46144 -0.00411 -0.01428 0.02903  115 LEU   A CG  
258  C  CD1 . LEU   A 38  ? 0.51235 0.47416 0.45446 -0.00310 -0.01627 0.03133  115 LEU   A CD1 
259  C  CD2 . LEU   A 38  ? 0.51875 0.47365 0.45855 -0.00026 -0.01123 0.02712  115 LEU   A CD2 
260  N  N   . PRO   A 39  ? 0.55188 0.50621 0.47215 -0.01682 -0.02140 0.03342  116 PRO   A N   
261  C  CA  . PRO   A 39  ? 0.55223 0.50454 0.46760 -0.01968 -0.02344 0.03615  116 PRO   A CA  
262  C  C   . PRO   A 39  ? 0.54574 0.49687 0.46381 -0.01648 -0.02228 0.03742  116 PRO   A C   
263  O  O   . PRO   A 39  ? 0.50417 0.45687 0.42884 -0.01190 -0.02106 0.03794  116 PRO   A O   
264  C  CB  . PRO   A 39  ? 0.53830 0.49472 0.45537 -0.02169 -0.02816 0.04140  116 PRO   A CB  
265  C  CG  . PRO   A 39  ? 0.53778 0.49913 0.46309 -0.01819 -0.02816 0.04219  116 PRO   A CG  
266  C  CD  . PRO   A 39  ? 0.49509 0.45423 0.41961 -0.01702 -0.02439 0.03644  116 PRO   A CD  
267  N  N   . SER   A 40  ? 0.56484 0.51251 0.47692 -0.01917 -0.02265 0.03796  117 SER   A N   
268  C  CA  . SER   A 40  ? 0.56743 0.51298 0.48057 -0.01694 -0.02193 0.03943  117 SER   A CA  
269  C  C   . SER   A 40  ? 0.49930 0.44773 0.41891 -0.01353 -0.02416 0.04454  117 SER   A C   
270  O  O   . SER   A 40  ? 0.52546 0.47197 0.44779 -0.00988 -0.02267 0.04514  117 SER   A O   
271  C  CB  . SER   A 40  ? 0.54459 0.48644 0.44995 -0.02103 -0.02267 0.03993  117 SER   A CB  
272  O  OG  . SER   A 40  ? 0.63512 0.57376 0.53596 -0.02224 -0.01917 0.03536  117 SER   A OG  
273  N  N   . SER   A 41  ? 0.50743 0.46024 0.42934 -0.01468 -0.02765 0.04847  118 SER   A N   
274  C  CA  . SER   A 41  ? 0.50071 0.45699 0.42891 -0.01148 -0.02984 0.05426  118 SER   A CA  
275  C  C   . SER   A 41  ? 0.48798 0.44524 0.42355 -0.00525 -0.02722 0.05402  118 SER   A C   
276  O  O   . SER   A 41  ? 0.49170 0.45052 0.43212 -0.00157 -0.02795 0.05856  118 SER   A O   
277  C  CB  . SER   A 41  ? 0.50508 0.46721 0.43537 -0.01401 -0.03397 0.05853  118 SER   A CB  
278  O  OG  . SER   A 41  ? 0.68656 0.64687 0.60884 -0.02022 -0.03560 0.05678  118 SER   A OG  
279  N  N   . ILE   A 42  ? 0.48486 0.44108 0.42120 -0.00385 -0.02409 0.04909  119 ILE   A N   
280  C  CA  . ILE   A 42  ? 0.50155 0.45782 0.44384 0.00177  -0.02148 0.04861  119 ILE   A CA  
281  C  C   . ILE   A 42  ? 0.46005 0.41083 0.40112 0.00465  -0.01971 0.04916  119 ILE   A C   
282  O  O   . ILE   A 42  ? 0.42875 0.37844 0.37387 0.00951  -0.01774 0.04970  119 ILE   A O   
283  C  CB  . ILE   A 42  ? 0.50880 0.46454 0.45134 0.00213  -0.01857 0.04303  119 ILE   A CB  
284  C  CG1 . ILE   A 42  ? 0.50031 0.45785 0.44980 0.00751  -0.01676 0.04345  119 ILE   A CG1 
285  C  CG2 . ILE   A 42  ? 0.45906 0.40919 0.39602 0.00070  -0.01598 0.03866  119 ILE   A CG2 
286  C  CD1 . ILE   A 42  ? 0.47836 0.43313 0.42759 0.00889  -0.01330 0.03827  119 ILE   A CD1 
287  N  N   . LYS   A 43  ? 0.49535 0.44202 0.43025 0.00163  -0.02024 0.04893  120 LYS   A N   
288  C  CA  . LYS   A 43  ? 0.50733 0.44810 0.44028 0.00390  -0.01875 0.04952  120 LYS   A CA  
289  C  C   . LYS   A 43  ? 0.50646 0.44776 0.44348 0.00797  -0.01996 0.05525  120 LYS   A C   
290  O  O   . LYS   A 43  ? 0.49303 0.42890 0.42944 0.01142  -0.01808 0.05577  120 LYS   A O   
291  C  CB  . LYS   A 43  ? 0.52366 0.46032 0.44909 -0.00056 -0.01925 0.04842  120 LYS   A CB  
292  C  CG  . LYS   A 43  ? 0.51526 0.45306 0.43831 -0.00335 -0.02278 0.05286  120 LYS   A CG  
293  C  CD  . LYS   A 43  ? 0.64526 0.57721 0.56143 -0.00596 -0.02250 0.05236  120 LYS   A CD  
294  C  CE  . LYS   A 43  ? 0.68697 0.61313 0.60351 -0.00186 -0.02057 0.05305  120 LYS   A CE  
295  N  NZ  . LYS   A 43  ? 0.61954 0.53935 0.52942 -0.00430 -0.01944 0.05126  120 LYS   A NZ  
296  N  N   . GLU   A 44  ? 0.45838 0.40593 0.39937 0.00767  -0.02298 0.05979  121 GLU   A N   
297  C  CA  . GLU   A 44  ? 0.47187 0.42115 0.41782 0.01198  -0.02402 0.06599  121 GLU   A CA  
298  C  C   . GLU   A 44  ? 0.50269 0.45280 0.45507 0.01835  -0.02124 0.06652  121 GLU   A C   
299  O  O   . GLU   A 44  ? 0.51793 0.46719 0.47352 0.02312  -0.02070 0.07103  121 GLU   A O   
300  C  CB  . GLU   A 44  ? 0.45867 0.41557 0.40770 0.00950  -0.02827 0.07116  121 GLU   A CB  
301  C  CG  . GLU   A 44  ? 0.47532 0.43103 0.41802 0.00383  -0.03137 0.07233  121 GLU   A CG  
302  C  CD  . GLU   A 44  ? 0.46023 0.42331 0.40592 0.00131  -0.03590 0.07812  121 GLU   A CD  
303  O  OE1 . GLU   A 44  ? 0.52352 0.49184 0.47121 -0.00094 -0.03725 0.07753  121 GLU   A OE1 
304  O  OE2 . GLU   A 44  ? 0.51560 0.47927 0.46165 0.00145  -0.03828 0.08357  121 GLU   A OE2 
305  N  N   . LEU   A 45  ? 0.43989 0.39148 0.39403 0.01867  -0.01934 0.06226  122 LEU   A N   
306  C  CA  . LEU   A 45  ? 0.47064 0.42404 0.43101 0.02420  -0.01695 0.06284  122 LEU   A CA  
307  C  C   . LEU   A 45  ? 0.47403 0.41891 0.43172 0.02813  -0.01301 0.06014  122 LEU   A C   
308  O  O   . LEU   A 45  ? 0.46676 0.41038 0.42527 0.02969  -0.01043 0.05635  122 LEU   A O   
309  C  CB  . LEU   A 45  ? 0.45470 0.41341 0.41781 0.02242  -0.01695 0.05963  122 LEU   A CB  
310  C  CG  . LEU   A 45  ? 0.47048 0.43852 0.43910 0.02101  -0.02020 0.06370  122 LEU   A CG  
311  C  CD1 . LEU   A 45  ? 0.50229 0.47243 0.46807 0.01634  -0.02427 0.06711  122 LEU   A CD1 
312  C  CD2 . LEU   A 45  ? 0.48227 0.45338 0.45132 0.01838  -0.02009 0.05952  122 LEU   A CD2 
313  N  N   . THR   A 46  ? 0.48414 0.42270 0.43815 0.02953  -0.01266 0.06225  123 THR   A N   
314  C  CA  . THR   A 46  ? 0.49578 0.42470 0.44544 0.03245  -0.00928 0.05989  123 THR   A CA  
315  C  C   . THR   A 46  ? 0.44961 0.37716 0.40350 0.03918  -0.00618 0.06136  123 THR   A C   
316  O  O   . THR   A 46  ? 0.45724 0.37637 0.40694 0.04130  -0.00314 0.05862  123 THR   A O   
317  C  CB  . THR   A 46  ? 0.49615 0.41834 0.44035 0.03207  -0.00998 0.06233  123 THR   A CB  
318  O  OG1 . THR   A 46  ? 0.47449 0.40067 0.42326 0.03499  -0.01169 0.06896  123 THR   A OG1 
319  C  CG2 . THR   A 46  ? 0.40910 0.33083 0.34757 0.02527  -0.01220 0.05982  123 THR   A CG2 
320  N  N   . GLN   A 47  ? 0.45707 0.39237 0.41871 0.04245  -0.00682 0.06582  124 GLN   A N   
321  C  CA  . GLN   A 47  ? 0.46568 0.40051 0.43171 0.04891  -0.00349 0.06710  124 GLN   A CA  
322  C  C   . GLN   A 47  ? 0.47088 0.40743 0.43828 0.04834  -0.00180 0.06212  124 GLN   A C   
323  O  O   . GLN   A 47  ? 0.49895 0.43469 0.46935 0.05339  0.00121  0.06257  124 GLN   A O   
324  C  CB  . GLN   A 47  ? 0.46887 0.41279 0.44366 0.05258  -0.00469 0.07406  124 GLN   A CB  
325  C  CG  . GLN   A 47  ? 0.51075 0.45455 0.48587 0.05388  -0.00643 0.08009  124 GLN   A CG  
326  C  CD  . GLN   A 47  ? 0.56006 0.49256 0.53041 0.05910  -0.00293 0.08101  124 GLN   A CD  
327  O  OE1 . GLN   A 47  ? 0.50734 0.43213 0.47046 0.05677  -0.00353 0.07985  124 GLN   A OE1 
328  N  NE2 . GLN   A 47  ? 0.55952 0.49049 0.53337 0.06615  0.00088  0.08315  124 GLN   A NE2 
329  N  N   . LEU   A 48  ? 0.45401 0.39276 0.41921 0.04259  -0.00345 0.05761  125 LEU   A N   
330  C  CA  . LEU   A 48  ? 0.44616 0.38773 0.41343 0.04190  -0.00226 0.05343  125 LEU   A CA  
331  C  C   . LEU   A 48  ? 0.45438 0.38705 0.41701 0.04373  0.00132  0.04917  125 LEU   A C   
332  O  O   . LEU   A 48  ? 0.41789 0.34303 0.37365 0.04153  0.00175  0.04670  125 LEU   A O   
333  C  CB  . LEU   A 48  ? 0.37467 0.32039 0.34035 0.03550  -0.00478 0.05008  125 LEU   A CB  
334  C  CG  . LEU   A 48  ? 0.46054 0.41592 0.43123 0.03329  -0.00813 0.05324  125 LEU   A CG  
335  C  CD1 . LEU   A 48  ? 0.44743 0.40460 0.41442 0.02688  -0.01018 0.04956  125 LEU   A CD1 
336  C  CD2 . LEU   A 48  ? 0.43227 0.39376 0.41021 0.03670  -0.00724 0.05470  125 LEU   A CD2 
337  N  N   . THR   A 49  ? 0.45676 0.39035 0.42291 0.04742  0.00375  0.04846  126 THR   A N   
338  C  CA  . THR   A 49  ? 0.48267 0.40887 0.44444 0.04809  0.00671  0.04389  126 THR   A CA  
339  C  C   . THR   A 49  ? 0.45161 0.38281 0.41577 0.04548  0.00654  0.03981  126 THR   A C   
340  O  O   . THR   A 49  ? 0.44146 0.36751 0.40193 0.04475  0.00835  0.03573  126 THR   A O   
341  C  CB  . THR   A 49  ? 0.48195 0.40257 0.44390 0.05467  0.01036  0.04581  126 THR   A CB  
342  O  OG1 . THR   A 49  ? 0.49238 0.42134 0.46252 0.05816  0.01080  0.04870  126 THR   A OG1 
343  C  CG2 . THR   A 49  ? 0.43896 0.35304 0.39762 0.05767  0.01102  0.04968  126 THR   A CG2 
344  N  N   . GLU   A 50  ? 0.46651 0.40725 0.43630 0.04375  0.00426  0.04094  127 GLU   A N   
345  C  CA  . GLU   A 50  ? 0.44887 0.39390 0.42046 0.04116  0.00403  0.03712  127 GLU   A CA  
346  C  C   . GLU   A 50  ? 0.47598 0.42813 0.44921 0.03663  0.00064  0.03757  127 GLU   A C   
347  O  O   . GLU   A 50  ? 0.47497 0.43274 0.45206 0.03700  -0.00147 0.04194  127 GLU   A O   
348  C  CB  . GLU   A 50  ? 0.45957 0.40791 0.43663 0.04523  0.00587  0.03788  127 GLU   A CB  
349  C  CG  . GLU   A 50  ? 0.47613 0.41616 0.45027 0.04966  0.00955  0.03724  127 GLU   A CG  
350  C  CD  . GLU   A 50  ? 0.51167 0.45469 0.49115 0.05456  0.01170  0.03921  127 GLU   A CD  
351  O  OE1 . GLU   A 50  ? 0.52950 0.47984 0.51392 0.05354  0.01084  0.03859  127 GLU   A OE1 
352  O  OE2 . GLU   A 50  ? 0.72465 0.66231 0.70308 0.05957  0.01446  0.04150  127 GLU   A OE2 
353  N  N   . LEU   A 51  ? 0.48373 0.43532 0.45364 0.03233  0.00021  0.03325  128 LEU   A N   
354  C  CA  . LEU   A 51  ? 0.45820 0.41472 0.42783 0.02774  -0.00244 0.03273  128 LEU   A CA  
355  C  C   . LEU   A 51  ? 0.43081 0.38958 0.40145 0.02624  -0.00168 0.02868  128 LEU   A C   
356  O  O   . LEU   A 51  ? 0.42700 0.38190 0.39475 0.02552  0.00017  0.02482  128 LEU   A O   
357  C  CB  . LEU   A 51  ? 0.42572 0.37840 0.38922 0.02400  -0.00331 0.03160  128 LEU   A CB  
358  C  CG  . LEU   A 51  ? 0.42278 0.37897 0.38432 0.01920  -0.00573 0.03114  128 LEU   A CG  
359  C  CD1 . LEU   A 51  ? 0.43645 0.39818 0.40136 0.01899  -0.00869 0.03590  128 LEU   A CD1 
360  C  CD2 . LEU   A 51  ? 0.39947 0.35111 0.35475 0.01614  -0.00585 0.03000  128 LEU   A CD2 
361  N  N   . TYR   A 52  ? 0.45268 0.41771 0.42740 0.02570  -0.00318 0.02986  129 TYR   A N   
362  C  CA  . TYR   A 52  ? 0.40862 0.37592 0.38414 0.02407  -0.00279 0.02638  129 TYR   A CA  
363  C  C   . TYR   A 52  ? 0.41570 0.38493 0.38813 0.01924  -0.00508 0.02565  129 TYR   A C   
364  O  O   . TYR   A 52  ? 0.45075 0.42372 0.42423 0.01775  -0.00779 0.02908  129 TYR   A O   
365  C  CB  . TYR   A 52  ? 0.43887 0.41107 0.42056 0.02683  -0.00267 0.02813  129 TYR   A CB  
366  C  CG  . TYR   A 52  ? 0.48521 0.45481 0.46922 0.03186  -0.00002 0.02898  129 TYR   A CG  
367  C  CD1 . TYR   A 52  ? 0.47267 0.43873 0.45582 0.03321  0.00261  0.02526  129 TYR   A CD1 
368  C  CD2 . TYR   A 52  ? 0.47950 0.44965 0.46603 0.03527  -0.00001 0.03362  129 TYR   A CD2 
369  C  CE1 . TYR   A 52  ? 0.44550 0.40797 0.42944 0.03756  0.00515  0.02592  129 TYR   A CE1 
370  C  CE2 . TYR   A 52  ? 0.51983 0.48638 0.50742 0.04013  0.00288  0.03435  129 TYR   A CE2 
371  C  CZ  . TYR   A 52  ? 0.52592 0.48824 0.51175 0.04112  0.00546  0.03036  129 TYR   A CZ  
372  O  OH  . TYR   A 52  ? 0.56637 0.52404 0.55208 0.04579  0.00843  0.03110  129 TYR   A OH  
373  N  N   . LEU   A 53  ? 0.44255 0.40906 0.41090 0.01677  -0.00390 0.02141  130 LEU   A N   
374  C  CA  . LEU   A 53  ? 0.44137 0.40816 0.40544 0.01241  -0.00519 0.01995  130 LEU   A CA  
375  C  C   . LEU   A 53  ? 0.41097 0.37794 0.37470 0.01159  -0.00368 0.01595  130 LEU   A C   
376  O  O   . LEU   A 53  ? 0.38903 0.35439 0.34818 0.00862  -0.00339 0.01364  130 LEU   A O   
377  C  CB  . LEU   A 53  ? 0.39513 0.35789 0.35358 0.01021  -0.00487 0.01919  130 LEU   A CB  
378  C  CG  . LEU   A 53  ? 0.41231 0.37441 0.37029 0.01059  -0.00658 0.02323  130 LEU   A CG  
379  C  CD1 . LEU   A 53  ? 0.42487 0.38246 0.37760 0.00891  -0.00583 0.02231  130 LEU   A CD1 
380  C  CD2 . LEU   A 53  ? 0.47797 0.44360 0.43574 0.00807  -0.00990 0.02645  130 LEU   A CD2 
381  N  N   . TYR   A 54  ? 0.39271 0.36132 0.36096 0.01434  -0.00250 0.01519  131 TYR   A N   
382  C  CA  . TYR   A 54  ? 0.39886 0.36739 0.36708 0.01397  -0.00089 0.01151  131 TYR   A CA  
383  C  C   . TYR   A 54  ? 0.39681 0.36755 0.36403 0.01138  -0.00263 0.01146  131 TYR   A C   
384  O  O   . TYR   A 54  ? 0.36778 0.34136 0.33616 0.01042  -0.00525 0.01469  131 TYR   A O   
385  C  CB  . TYR   A 54  ? 0.41047 0.37970 0.38341 0.01753  0.00079  0.01085  131 TYR   A CB  
386  C  CG  . TYR   A 54  ? 0.43648 0.40976 0.41458 0.01962  -0.00040 0.01375  131 TYR   A CG  
387  C  CD1 . TYR   A 54  ? 0.44572 0.42247 0.42546 0.01835  -0.00166 0.01375  131 TYR   A CD1 
388  C  CD2 . TYR   A 54  ? 0.42456 0.39799 0.40572 0.02301  0.00001  0.01658  131 TYR   A CD2 
389  C  CE1 . TYR   A 54  ? 0.44254 0.42375 0.42743 0.02011  -0.00272 0.01677  131 TYR   A CE1 
390  C  CE2 . TYR   A 54  ? 0.40876 0.38648 0.39512 0.02528  -0.00065 0.01957  131 TYR   A CE2 
391  C  CZ  . TYR   A 54  ? 0.45328 0.43535 0.44178 0.02371  -0.00210 0.01976  131 TYR   A CZ  
392  O  OH  . TYR   A 54  ? 0.51720 0.50429 0.51127 0.02581  -0.00278 0.02315  131 TYR   A OH  
393  N  N   . SER   A 55  ? 0.40978 0.37902 0.37463 0.01018  -0.00115 0.00795  132 SER   A N   
394  C  CA  . SER   A 55  ? 0.44562 0.41511 0.40788 0.00754  -0.00229 0.00714  132 SER   A CA  
395  C  C   . SER   A 55  ? 0.39776 0.36607 0.35464 0.00379  -0.00472 0.00896  132 SER   A C   
396  O  O   . SER   A 55  ? 0.39986 0.37060 0.35725 0.00211  -0.00771 0.01190  132 SER   A O   
397  C  CB  . SER   A 55  ? 0.42149 0.39481 0.38869 0.00866  -0.00357 0.00852  132 SER   A CB  
398  O  OG  . SER   A 55  ? 0.51607 0.48999 0.48758 0.01194  -0.00129 0.00679  132 SER   A OG  
399  N  N   . ASN   A 56  ? 0.41412 0.37878 0.36572 0.00233  -0.00340 0.00737  133 ASN   A N   
400  C  CA  . ASN   A 56  ? 0.39980 0.36211 0.34476 -0.00154 -0.00519 0.00842  133 ASN   A CA  
401  C  C   . ASN   A 56  ? 0.42368 0.38140 0.36233 -0.00290 -0.00234 0.00473  133 ASN   A C   
402  O  O   . ASN   A 56  ? 0.41878 0.37598 0.35879 -0.00106 0.00042  0.00184  133 ASN   A O   
403  C  CB  . ASN   A 56  ? 0.41622 0.37926 0.36168 -0.00155 -0.00672 0.01162  133 ASN   A CB  
404  C  CG  . ASN   A 56  ? 0.44143 0.40885 0.39141 -0.00124 -0.01007 0.01613  133 ASN   A CG  
405  O  OD1 . ASN   A 56  ? 0.44432 0.41310 0.39269 -0.00410 -0.01281 0.01787  133 ASN   A OD1 
406  N  ND2 . ASN   A 56  ? 0.40386 0.37345 0.35943 0.00226  -0.00978 0.01825  133 ASN   A ND2 
407  N  N   . LYS   A 57  ? 0.45790 0.41235 0.38961 -0.00600 -0.00284 0.00501  134 LYS   A N   
408  C  CA  . LYS   A 57  ? 0.44372 0.39362 0.36886 -0.00716 0.00023  0.00190  134 LYS   A CA  
409  C  C   . LYS   A 57  ? 0.45541 0.40431 0.37872 -0.00732 0.00147  0.00225  134 LYS   A C   
410  O  O   . LYS   A 57  ? 0.44611 0.39118 0.36231 -0.00954 0.00284  0.00117  134 LYS   A O   
411  C  CB  . LYS   A 57  ? 0.44842 0.39390 0.36502 -0.01111 -0.00096 0.00146  134 LYS   A CB  
412  C  CG  . LYS   A 57  ? 0.46134 0.40714 0.37899 -0.01130 -0.00204 0.00091  134 LYS   A CG  
413  C  CD  . LYS   A 57  ? 0.52897 0.46916 0.43690 -0.01564 -0.00326 0.00041  134 LYS   A CD  
414  C  CE  . LYS   A 57  ? 0.55675 0.49706 0.46544 -0.01624 -0.00470 0.00014  134 LYS   A CE  
415  N  NZ  . LYS   A 57  ? 0.60462 0.54523 0.51733 -0.01240 -0.00108 -0.00295 134 LYS   A NZ  
416  N  N   . LEU   A 58  ? 0.41744 0.36932 0.34662 -0.00503 0.00111  0.00381  135 LEU   A N   
417  C  CA  . LEU   A 58  ? 0.44537 0.39623 0.37283 -0.00548 0.00173  0.00462  135 LEU   A CA  
418  C  C   . LEU   A 58  ? 0.41995 0.36968 0.34626 -0.00466 0.00573  0.00182  135 LEU   A C   
419  O  O   . LEU   A 58  ? 0.40763 0.35913 0.33852 -0.00215 0.00768  0.00023  135 LEU   A O   
420  C  CB  . LEU   A 58  ? 0.41090 0.36422 0.34422 -0.00322 0.00028  0.00714  135 LEU   A CB  
421  C  CG  . LEU   A 58  ? 0.38275 0.33815 0.31842 -0.00334 -0.00342 0.01084  135 LEU   A CG  
422  C  CD1 . LEU   A 58  ? 0.38901 0.34588 0.33028 -0.00011 -0.00365 0.01287  135 LEU   A CD1 
423  C  CD2 . LEU   A 58  ? 0.40879 0.36253 0.33851 -0.00709 -0.00587 0.01302  135 LEU   A CD2 
424  N  N   . GLN   A 59  ? 0.41954 0.36659 0.33978 -0.00686 0.00696  0.00148  136 GLN   A N   
425  C  CA  . GLN   A 59  ? 0.44329 0.39014 0.36285 -0.00616 0.01076  -0.00033 136 GLN   A CA  
426  C  C   . GLN   A 59  ? 0.47792 0.42516 0.39766 -0.00671 0.01066  0.00128  136 GLN   A C   
427  O  O   . GLN   A 59  ? 0.46813 0.41596 0.38778 -0.00646 0.01353  0.00040  136 GLN   A O   
428  C  CB  . GLN   A 59  ? 0.45119 0.39446 0.36328 -0.00792 0.01323  -0.00217 136 GLN   A CB  
429  C  CG  . GLN   A 59  ? 0.38722 0.32856 0.29730 -0.00796 0.01310  -0.00369 136 GLN   A CG  
430  C  CD  . GLN   A 59  ? 0.40256 0.33895 0.30409 -0.00949 0.01598  -0.00559 136 GLN   A CD  
431  O  OE1 . GLN   A 59  ? 0.41366 0.35003 0.31469 -0.00809 0.02008  -0.00697 136 GLN   A OE1 
432  N  NE2 . GLN   A 59  ? 0.38488 0.31683 0.27921 -0.01250 0.01396  -0.00542 136 GLN   A NE2 
433  N  N   . SER   A 60  ? 0.47002 0.41706 0.39011 -0.00746 0.00743  0.00388  137 SER   A N   
434  C  CA  . SER   A 60  ? 0.47200 0.41870 0.39209 -0.00790 0.00704  0.00558  137 SER   A CA  
435  C  C   . SER   A 60  ? 0.47387 0.42084 0.39670 -0.00713 0.00359  0.00846  137 SER   A C   
436  O  O   . SER   A 60  ? 0.48952 0.43685 0.41211 -0.00765 0.00111  0.00982  137 SER   A O   
437  C  CB  . SER   A 60  ? 0.48142 0.42565 0.39446 -0.01101 0.00774  0.00591  137 SER   A CB  
438  O  OG  . SER   A 60  ? 0.51236 0.45494 0.42214 -0.01305 0.00439  0.00838  137 SER   A OG  
439  N  N   . LEU   A 61  ? 0.45620 0.40284 0.38137 -0.00595 0.00351  0.00963  138 LEU   A N   
440  C  CA  . LEU   A 61  ? 0.46623 0.41243 0.39379 -0.00458 0.00092  0.01252  138 LEU   A CA  
441  C  C   . LEU   A 61  ? 0.46091 0.40457 0.38419 -0.00666 -0.00028 0.01473  138 LEU   A C   
442  O  O   . LEU   A 61  ? 0.47403 0.41616 0.39531 -0.00762 0.00130  0.01411  138 LEU   A O   
443  C  CB  . LEU   A 61  ? 0.45425 0.40053 0.38673 -0.00147 0.00185  0.01217  138 LEU   A CB  
444  C  CG  . LEU   A 61  ? 0.43430 0.37998 0.36986 0.00107  -0.00010 0.01496  138 LEU   A CG  
445  C  CD1 . LEU   A 61  ? 0.45022 0.39915 0.38966 0.00262  -0.00124 0.01539  138 LEU   A CD1 
446  C  CD2 . LEU   A 61  ? 0.45888 0.40217 0.39630 0.00331  0.00118  0.01465  138 LEU   A CD2 
447  N  N   . PRO   A 62  ? 0.46070 0.40404 0.38242 -0.00768 -0.00312 0.01757  139 PRO   A N   
448  C  CA  . PRO   A 62  ? 0.47692 0.41770 0.39389 -0.01007 -0.00427 0.01963  139 PRO   A CA  
449  C  C   . PRO   A 62  ? 0.44735 0.38570 0.36559 -0.00841 -0.00407 0.02097  139 PRO   A C   
450  O  O   . PRO   A 62  ? 0.45511 0.39338 0.37774 -0.00515 -0.00435 0.02188  139 PRO   A O   
451  C  CB  . PRO   A 62  ? 0.48329 0.42498 0.39956 -0.01112 -0.00775 0.02287  139 PRO   A CB  
452  C  CG  . PRO   A 62  ? 0.48756 0.43245 0.40978 -0.00835 -0.00857 0.02331  139 PRO   A CG  
453  C  CD  . PRO   A 62  ? 0.48544 0.43118 0.40980 -0.00695 -0.00558 0.01937  139 PRO   A CD  
454  N  N   . ALA   A 63  ? 0.44239 0.37822 0.35610 -0.01079 -0.00351 0.02116  140 ALA   A N   
455  C  CA  . ALA   A 63  ? 0.47412 0.40653 0.38759 -0.00990 -0.00354 0.02256  140 ALA   A CA  
456  C  C   . ALA   A 63  ? 0.45958 0.39033 0.37474 -0.00760 -0.00600 0.02615  140 ALA   A C   
457  O  O   . ALA   A 63  ? 0.43971 0.36693 0.35542 -0.00559 -0.00574 0.02714  140 ALA   A O   
458  C  CB  . ALA   A 63  ? 0.48160 0.41185 0.38945 -0.01341 -0.00303 0.02276  140 ALA   A CB  
459  N  N   . GLU   A 64  ? 0.50211 0.43522 0.41804 -0.00777 -0.00831 0.02829  141 GLU   A N   
460  C  CA  . GLU   A 64  ? 0.50594 0.43856 0.42434 -0.00529 -0.01057 0.03237  141 GLU   A CA  
461  C  C   . GLU   A 64  ? 0.50356 0.43635 0.42763 -0.00054 -0.00953 0.03247  141 GLU   A C   
462  O  O   . GLU   A 64  ? 0.48487 0.41531 0.41038 0.00239  -0.01015 0.03551  141 GLU   A O   
463  C  CB  . GLU   A 64  ? 0.53534 0.47167 0.45403 -0.00687 -0.01344 0.03487  141 GLU   A CB  
464  C  CG  . GLU   A 64  ? 0.60314 0.53787 0.51591 -0.01086 -0.01542 0.03687  141 GLU   A CG  
465  C  CD  . GLU   A 64  ? 0.57950 0.51373 0.48653 -0.01509 -0.01410 0.03355  141 GLU   A CD  
466  O  OE1 . GLU   A 64  ? 0.55257 0.48806 0.46055 -0.01480 -0.01169 0.02985  141 GLU   A OE1 
467  O  OE2 . GLU   A 64  ? 0.65369 0.58611 0.55510 -0.01855 -0.01532 0.03482  141 GLU   A OE2 
468  N  N   . VAL   A 65  ? 0.46490 0.40015 0.39198 0.00044  -0.00780 0.02933  142 VAL   A N   
469  C  CA  . VAL   A 65  ? 0.47303 0.40809 0.40492 0.00474  -0.00651 0.02908  142 VAL   A CA  
470  C  C   . VAL   A 65  ? 0.46675 0.39559 0.39657 0.00643  -0.00515 0.02926  142 VAL   A C   
471  O  O   . VAL   A 65  ? 0.45223 0.37895 0.38457 0.01039  -0.00445 0.03049  142 VAL   A O   
472  C  CB  . VAL   A 65  ? 0.46360 0.40165 0.39803 0.00484  -0.00473 0.02526  142 VAL   A CB  
473  C  CG1 . VAL   A 65  ? 0.42977 0.36690 0.36830 0.00895  -0.00320 0.02475  142 VAL   A CG1 
474  C  CG2 . VAL   A 65  ? 0.47153 0.41465 0.40758 0.00349  -0.00614 0.02531  142 VAL   A CG2 
475  N  N   . GLY   A 66  ? 0.47824 0.40369 0.40298 0.00339  -0.00466 0.02816  143 GLY   A N   
476  C  CA  . GLY   A 66  ? 0.45239 0.37112 0.37384 0.00408  -0.00378 0.02856  143 GLY   A CA  
477  C  C   . GLY   A 66  ? 0.50966 0.42417 0.42993 0.00637  -0.00505 0.03256  143 GLY   A C   
478  O  O   . GLY   A 66  ? 0.53745 0.44510 0.45465 0.00768  -0.00416 0.03306  143 GLY   A O   
479  N  N   . CYS   A 67  ? 0.46331 0.38143 0.38553 0.00671  -0.00716 0.03561  144 CYS   A N   
480  C  CA  . CYS   A 67  ? 0.46964 0.38490 0.39208 0.00961  -0.00833 0.04006  144 CYS   A CA  
481  C  C   . CYS   A 67  ? 0.50126 0.41674 0.42887 0.01521  -0.00720 0.04159  144 CYS   A C   
482  O  O   . CYS   A 67  ? 0.47933 0.39083 0.40683 0.01868  -0.00712 0.04504  144 CYS   A O   
483  C  CB  . CYS   A 67  ? 0.53255 0.45233 0.45547 0.00758  -0.01131 0.04333  144 CYS   A CB  
484  S  SG  . CYS   A 67  ? 0.60594 0.52404 0.52163 0.00144  -0.01270 0.04280  144 CYS   A SG  
485  N  N   . LEU   A 68  ? 0.50214 0.42219 0.43424 0.01633  -0.00618 0.03931  145 LEU   A N   
486  C  CA  . LEU   A 68  ? 0.47238 0.39302 0.40944 0.02161  -0.00483 0.04068  145 LEU   A CA  
487  C  C   . LEU   A 68  ? 0.48744 0.39956 0.42102 0.02405  -0.00210 0.03904  145 LEU   A C   
488  O  O   . LEU   A 68  ? 0.51055 0.42205 0.44486 0.02471  -0.00023 0.03582  145 LEU   A O   
489  C  CB  . LEU   A 68  ? 0.43978 0.36767 0.38214 0.02155  -0.00476 0.03875  145 LEU   A CB  
490  C  CG  . LEU   A 68  ? 0.44067 0.37523 0.38404 0.01777  -0.00759 0.03972  145 LEU   A CG  
491  C  CD1 . LEU   A 68  ? 0.38247 0.32352 0.33027 0.01735  -0.00769 0.03787  145 LEU   A CD1 
492  C  CD2 . LEU   A 68  ? 0.41425 0.35072 0.35923 0.01884  -0.01000 0.04529  145 LEU   A CD2 
493  N  N   . VAL   A 69  ? 0.44452 0.34952 0.37368 0.02512  -0.00204 0.04142  146 VAL   A N   
494  C  CA  . VAL   A 69  ? 0.49968 0.39443 0.42297 0.02634  0.00010  0.04020  146 VAL   A CA  
495  C  C   . VAL   A 69  ? 0.49457 0.38628 0.41976 0.03142  0.00285  0.03979  146 VAL   A C   
496  O  O   . VAL   A 69  ? 0.46225 0.34581 0.38225 0.03158  0.00477  0.03754  146 VAL   A O   
497  C  CB  . VAL   A 69  ? 0.48265 0.37093 0.40135 0.02699  -0.00071 0.04385  146 VAL   A CB  
498  C  CG1 . VAL   A 69  ? 0.50854 0.38601 0.42274 0.03111  0.00182  0.04456  146 VAL   A CG1 
499  C  CG2 . VAL   A 69  ? 0.47720 0.36399 0.39041 0.02108  -0.00237 0.04253  146 VAL   A CG2 
500  N  N   . ASN   A 70  ? 0.51267 0.41072 0.44491 0.03532  0.00304  0.04204  147 ASN   A N   
501  C  CA  . ASN   A 70  ? 0.52465 0.42007 0.45889 0.04063  0.00592  0.04219  147 ASN   A CA  
502  C  C   . ASN   A 70  ? 0.47251 0.37443 0.41155 0.04014  0.00649  0.03907  147 ASN   A C   
503  O  O   . ASN   A 70  ? 0.44590 0.34770 0.38792 0.04454  0.00868  0.03950  147 ASN   A O   
504  C  CB  . ASN   A 70  ? 0.47701 0.37450 0.41598 0.04625  0.00630  0.04768  147 ASN   A CB  
505  C  CG  . ASN   A 70  ? 0.55030 0.43905 0.48385 0.04813  0.00666  0.05085  147 ASN   A CG  
506  O  OD1 . ASN   A 70  ? 0.55169 0.42923 0.47749 0.04835  0.00855  0.04906  147 ASN   A OD1 
507  N  ND2 . ASN   A 70  ? 0.50470 0.39823 0.44186 0.04912  0.00463  0.05571  147 ASN   A ND2 
508  N  N   . LEU   A 71  ? 0.46002 0.36730 0.39966 0.03511  0.00482  0.03602  148 LEU   A N   
509  C  CA  . LEU   A 71  ? 0.43603 0.34922 0.38006 0.03468  0.00533  0.03317  148 LEU   A CA  
510  C  C   . LEU   A 71  ? 0.44972 0.35642 0.39084 0.03622  0.00806  0.03028  148 LEU   A C   
511  O  O   . LEU   A 71  ? 0.50050 0.40038 0.43534 0.03366  0.00858  0.02800  148 LEU   A O   
512  C  CB  . LEU   A 71  ? 0.44427 0.36279 0.38825 0.02919  0.00352  0.03035  148 LEU   A CB  
513  C  CG  . LEU   A 71  ? 0.42206 0.34918 0.37040 0.02766  0.00101  0.03227  148 LEU   A CG  
514  C  CD1 . LEU   A 71  ? 0.41900 0.35031 0.36700 0.02314  0.00034  0.02861  148 LEU   A CD1 
515  C  CD2 . LEU   A 71  ? 0.39272 0.32526 0.34785 0.03170  0.00107  0.03501  148 LEU   A CD2 
516  N  N   . MET   A 72  ? 0.45033 0.35912 0.39574 0.04012  0.00971  0.03058  149 MET   A N   
517  C  CA  . MET   A 72  ? 0.47991 0.38381 0.42291 0.04090  0.01204  0.02744  149 MET   A CA  
518  C  C   . MET   A 72  ? 0.44337 0.35420 0.39008 0.03815  0.01145  0.02411  149 MET   A C   
519  O  O   . MET   A 72  ? 0.49823 0.40551 0.44177 0.03628  0.01239  0.02086  149 MET   A O   
520  C  CB  . MET   A 72  ? 0.49688 0.39754 0.44131 0.04709  0.01479  0.02957  149 MET   A CB  
521  C  CG  . MET   A 72  ? 0.58410 0.47598 0.52376 0.05045  0.01605  0.03282  149 MET   A CG  
522  S  SD  . MET   A 72  ? 0.75100 0.63751 0.69125 0.05851  0.02019  0.03568  149 MET   A SD  
523  C  CE  . MET   A 72  ? 0.60900 0.50912 0.56024 0.06003  0.01987  0.03612  149 MET   A CE  
524  N  N   . THR   A 73  ? 0.46592 0.38624 0.41883 0.03752  0.00974  0.02501  150 THR   A N   
525  C  CA  . THR   A 73  ? 0.46461 0.39148 0.42126 0.03543  0.00928  0.02220  150 THR   A CA  
526  C  C   . THR   A 73  ? 0.41819 0.35155 0.37639 0.03160  0.00673  0.02221  150 THR   A C   
527  O  O   . THR   A 73  ? 0.40372 0.34064 0.36410 0.03201  0.00506  0.02544  150 THR   A O   
528  C  CB  . THR   A 73  ? 0.41982 0.35129 0.38243 0.03915  0.01024  0.02325  150 THR   A CB  
529  O  OG1 . THR   A 73  ? 0.48016 0.40582 0.44062 0.04152  0.01287  0.02159  150 THR   A OG1 
530  C  CG2 . THR   A 73  ? 0.43710 0.37660 0.40401 0.03660  0.00887  0.02141  150 THR   A CG2 
531  N  N   . LEU   A 74  ? 0.42685 0.36169 0.38382 0.02794  0.00654  0.01880  151 LEU   A N   
532  C  CA  . LEU   A 74  ? 0.43150 0.37147 0.38888 0.02427  0.00474  0.01818  151 LEU   A CA  
533  C  C   . LEU   A 74  ? 0.40635 0.35073 0.36659 0.02330  0.00521  0.01525  151 LEU   A C   
534  O  O   . LEU   A 74  ? 0.45577 0.39835 0.41461 0.02224  0.00655  0.01242  151 LEU   A O   
535  C  CB  . LEU   A 74  ? 0.43717 0.37369 0.38918 0.02076  0.00445  0.01723  151 LEU   A CB  
536  C  CG  . LEU   A 74  ? 0.38112 0.32169 0.33221 0.01700  0.00308  0.01657  151 LEU   A CG  
537  C  CD1 . LEU   A 74  ? 0.39157 0.33575 0.34451 0.01725  0.00091  0.01969  151 LEU   A CD1 
538  C  CD2 . LEU   A 74  ? 0.35338 0.29034 0.29927 0.01400  0.00316  0.01607  151 LEU   A CD2 
539  N  N   . ALA   A 75  ? 0.37680 0.32686 0.34095 0.02352  0.00403  0.01615  152 ALA   A N   
540  C  CA  . ALA   A 75  ? 0.40121 0.35501 0.36808 0.02300  0.00449  0.01365  152 ALA   A CA  
541  C  C   . ALA   A 75  ? 0.42903 0.38582 0.39438 0.01934  0.00327  0.01244  152 ALA   A C   
542  O  O   . ALA   A 75  ? 0.42548 0.38523 0.39142 0.01832  0.00128  0.01451  152 ALA   A O   
543  C  CB  . ALA   A 75  ? 0.42842 0.38583 0.40044 0.02599  0.00428  0.01547  152 ALA   A CB  
544  N  N   . LEU   A 76  ? 0.41998 0.37592 0.38321 0.01735  0.00454  0.00930  153 LEU   A N   
545  C  CA  . LEU   A 76  ? 0.41600 0.37331 0.37649 0.01412  0.00415  0.00799  153 LEU   A CA  
546  C  C   . LEU   A 76  ? 0.40199 0.36140 0.36367 0.01362  0.00533  0.00511  153 LEU   A C   
547  O  O   . LEU   A 76  ? 0.37845 0.33787 0.33718 0.01134  0.00595  0.00354  153 LEU   A O   
548  C  CB  . LEU   A 76  ? 0.39053 0.34490 0.34670 0.01204  0.00490  0.00742  153 LEU   A CB  
549  C  CG  . LEU   A 76  ? 0.40579 0.35752 0.35975 0.01200  0.00363  0.01022  153 LEU   A CG  
550  C  CD1 . LEU   A 76  ? 0.39152 0.34011 0.34152 0.01004  0.00463  0.00945  153 LEU   A CD1 
551  C  CD2 . LEU   A 76  ? 0.42975 0.38338 0.38247 0.01037  0.00143  0.01223  153 LEU   A CD2 
552  N  N   . SER   A 77  ? 0.40242 0.36329 0.36804 0.01580  0.00588  0.00444  154 SER   A N   
553  C  CA  . SER   A 77  ? 0.41910 0.38152 0.38581 0.01550  0.00715  0.00174  154 SER   A CA  
554  C  C   . SER   A 77  ? 0.38231 0.34632 0.34748 0.01364  0.00615  0.00140  154 SER   A C   
555  O  O   . SER   A 77  ? 0.38294 0.34774 0.34738 0.01276  0.00405  0.00356  154 SER   A O   
556  C  CB  . SER   A 77  ? 0.38358 0.34705 0.35457 0.01810  0.00771  0.00135  154 SER   A CB  
557  O  OG  . SER   A 77  ? 0.43482 0.40025 0.40829 0.01939  0.00612  0.00367  154 SER   A OG  
558  N  N   . GLU   A 78  ? 0.41356 0.37774 0.37789 0.01293  0.00768  -0.00115 155 GLU   A N   
559  C  CA  . GLU   A 78  ? 0.38304 0.34725 0.34472 0.01116  0.00721  -0.00200 155 GLU   A CA  
560  C  C   . GLU   A 78  ? 0.38938 0.35176 0.34568 0.00843  0.00603  -0.00090 155 GLU   A C   
561  O  O   . GLU   A 78  ? 0.37429 0.33702 0.32915 0.00691  0.00364  0.00079  155 GLU   A O   
562  C  CB  . GLU   A 78  ? 0.44477 0.41114 0.40939 0.01180  0.00545  -0.00105 155 GLU   A CB  
563  C  CG  . GLU   A 78  ? 0.47040 0.43836 0.43962 0.01414  0.00659  -0.00233 155 GLU   A CG  
564  C  CD  . GLU   A 78  ? 0.66458 0.63472 0.63588 0.01410  0.00488  -0.00147 155 GLU   A CD  
565  O  OE1 . GLU   A 78  ? 0.62869 0.59824 0.59652 0.01160  0.00336  -0.00107 155 GLU   A OE1 
566  O  OE2 . GLU   A 78  ? 0.76141 0.73361 0.73737 0.01632  0.00501  -0.00106 155 GLU   A OE2 
567  N  N   . ASN   A 79  ? 0.38159 0.34221 0.33487 0.00756  0.00766  -0.00167 156 ASN   A N   
568  C  CA  . ASN   A 79  ? 0.38166 0.33999 0.32893 0.00482  0.00726  -0.00121 156 ASN   A CA  
569  C  C   . ASN   A 79  ? 0.38018 0.33711 0.32458 0.00443  0.01053  -0.00359 156 ASN   A C   
570  O  O   . ASN   A 79  ? 0.38850 0.34658 0.33572 0.00612  0.01263  -0.00533 156 ASN   A O   
571  C  CB  . ASN   A 79  ? 0.38429 0.34227 0.33119 0.00437  0.00569  0.00134  156 ASN   A CB  
572  C  CG  . ASN   A 79  ? 0.39122 0.35076 0.34038 0.00468  0.00255  0.00431  156 ASN   A CG  
573  O  OD1 . ASN   A 79  ? 0.39279 0.35230 0.33918 0.00248  0.00044  0.00557  156 ASN   A OD1 
574  N  ND2 . ASN   A 79  ? 0.39506 0.35589 0.34904 0.00735  0.00226  0.00570  156 ASN   A ND2 
575  N  N   . SER   A 80  ? 0.40892 0.36366 0.34796 0.00234  0.01116  -0.00343 157 SER   A N   
576  C  CA  . SER   A 80  ? 0.40444 0.35842 0.34113 0.00226  0.01464  -0.00511 157 SER   A CA  
577  C  C   . SER   A 80  ? 0.41833 0.37268 0.35458 0.00153  0.01516  -0.00391 157 SER   A C   
578  O  O   . SER   A 80  ? 0.43415 0.38713 0.36598 0.00012  0.01704  -0.00422 157 SER   A O   
579  C  CB  . SER   A 80  ? 0.42055 0.37086 0.35004 0.00041  0.01582  -0.00635 157 SER   A CB  
580  O  OG  . SER   A 80  ? 0.56580 0.51498 0.49469 0.00036  0.01456  -0.00707 157 SER   A OG  
581  N  N   . LEU   A 81  ? 0.40174 0.35748 0.34204 0.00243  0.01363  -0.00246 158 LEU   A N   
582  C  CA  . LEU   A 81  ? 0.42771 0.38311 0.36701 0.00141  0.01388  -0.00121 158 LEU   A CA  
583  C  C   . LEU   A 81  ? 0.43811 0.39547 0.37892 0.00175  0.01696  -0.00222 158 LEU   A C   
584  O  O   . LEU   A 81  ? 0.38354 0.34306 0.32860 0.00350  0.01808  -0.00325 158 LEU   A O   
585  C  CB  . LEU   A 81  ? 0.39252 0.34770 0.33491 0.00242  0.01169  0.00057  158 LEU   A CB  
586  C  CG  . LEU   A 81  ? 0.36822 0.32244 0.31023 0.00249  0.00871  0.00241  158 LEU   A CG  
587  C  CD1 . LEU   A 81  ? 0.41748 0.37108 0.36258 0.00427  0.00747  0.00407  158 LEU   A CD1 
588  C  CD2 . LEU   A 81  ? 0.38615 0.33850 0.32266 -0.00017 0.00768  0.00365  158 LEU   A CD2 
589  N  N   . THR   A 82  ? 0.44458 0.40158 0.38206 -0.00006 0.01826  -0.00160 159 THR   A N   
590  C  CA  . THR   A 82  ? 0.41341 0.37315 0.35286 -0.00013 0.02080  -0.00156 159 THR   A CA  
591  C  C   . THR   A 82  ? 0.42535 0.38467 0.36417 -0.00189 0.01969  0.00038  159 THR   A C   
592  O  O   . THR   A 82  ? 0.42895 0.39070 0.36873 -0.00279 0.02145  0.00102  159 THR   A O   
593  C  CB  . THR   A 82  ? 0.45597 0.41627 0.39219 -0.00057 0.02420  -0.00239 159 THR   A CB  
594  O  OG1 . THR   A 82  ? 0.49427 0.45162 0.42436 -0.00283 0.02368  -0.00166 159 THR   A OG1 
595  C  CG2 . THR   A 82  ? 0.44045 0.40002 0.37627 0.00114  0.02561  -0.00440 159 THR   A CG2 
596  N  N   . SER   A 83  ? 0.44055 0.39687 0.37771 -0.00246 0.01683  0.00161  160 SER   A N   
597  C  CA  . SER   A 83  ? 0.40678 0.36160 0.34226 -0.00425 0.01582  0.00346  160 SER   A CA  
598  C  C   . SER   A 83  ? 0.40314 0.35435 0.33741 -0.00389 0.01276  0.00484  160 SER   A C   
599  O  O   . SER   A 83  ? 0.41627 0.36690 0.35060 -0.00281 0.01144  0.00472  160 SER   A O   
600  C  CB  . SER   A 83  ? 0.40692 0.36190 0.33802 -0.00670 0.01728  0.00409  160 SER   A CB  
601  O  OG  . SER   A 83  ? 0.42982 0.38264 0.35668 -0.00730 0.01660  0.00389  160 SER   A OG  
602  N  N   . LEU   A 84  ? 0.38285 0.33163 0.31591 -0.00486 0.01168  0.00644  161 LEU   A N   
603  C  CA  . LEU   A 84  ? 0.40238 0.34739 0.33400 -0.00424 0.00915  0.00819  161 LEU   A CA  
604  C  C   . LEU   A 84  ? 0.44067 0.38291 0.36766 -0.00680 0.00839  0.01005  161 LEU   A C   
605  O  O   . LEU   A 84  ? 0.44209 0.38467 0.36787 -0.00883 0.00951  0.01021  161 LEU   A O   
606  C  CB  . LEU   A 84  ? 0.40123 0.34414 0.33563 -0.00199 0.00845  0.00839  161 LEU   A CB  
607  C  CG  . LEU   A 84  ? 0.38611 0.33129 0.32513 0.00076  0.00885  0.00688  161 LEU   A CG  
608  C  CD1 . LEU   A 84  ? 0.38243 0.32500 0.32302 0.00239  0.00873  0.00696  161 LEU   A CD1 
609  C  CD2 . LEU   A 84  ? 0.38621 0.33198 0.32608 0.00228  0.00736  0.00754  161 LEU   A CD2 
610  N  N   . PRO   A 85  ? 0.39520 0.33502 0.31971 -0.00693 0.00637  0.01179  162 PRO   A N   
611  C  CA  . PRO   A 85  ? 0.45064 0.38752 0.37046 -0.00940 0.00547  0.01371  162 PRO   A CA  
612  C  C   . PRO   A 85  ? 0.44867 0.38156 0.36762 -0.00951 0.00502  0.01483  162 PRO   A C   
613  O  O   . PRO   A 85  ? 0.45182 0.38254 0.37294 -0.00708 0.00462  0.01484  162 PRO   A O   
614  C  CB  . PRO   A 85  ? 0.41990 0.35536 0.33831 -0.00890 0.00308  0.01562  162 PRO   A CB  
615  C  CG  . PRO   A 85  ? 0.42739 0.36396 0.35044 -0.00556 0.00243  0.01537  162 PRO   A CG  
616  C  CD  . PRO   A 85  ? 0.43359 0.37357 0.35973 -0.00491 0.00462  0.01249  162 PRO   A CD  
617  N  N   . ASP   A 86  ? 0.47559 0.40699 0.39064 -0.01256 0.00515  0.01584  163 ASP   A N   
618  C  CA  . ASP   A 86  ? 0.52004 0.44676 0.43282 -0.01354 0.00456  0.01703  163 ASP   A CA  
619  C  C   . ASP   A 86  ? 0.51455 0.43519 0.42523 -0.01173 0.00254  0.01905  163 ASP   A C   
620  O  O   . ASP   A 86  ? 0.50206 0.41747 0.41123 -0.01110 0.00223  0.01962  163 ASP   A O   
621  C  CB  . ASP   A 86  ? 0.49461 0.42169 0.40365 -0.01759 0.00507  0.01793  163 ASP   A CB  
622  C  CG  . ASP   A 86  ? 0.57047 0.50188 0.48183 -0.01912 0.00705  0.01680  163 ASP   A CG  
623  O  OD1 . ASP   A 86  ? 0.56353 0.49392 0.47701 -0.01815 0.00705  0.01621  163 ASP   A OD1 
624  O  OD2 . ASP   A 86  ? 0.61014 0.54602 0.52129 -0.02114 0.00869  0.01667  163 ASP   A OD2 
625  N  N   . SER   A 87  ? 0.49346 0.41443 0.40374 -0.01087 0.00121  0.02035  164 SER   A N   
626  C  CA  . SER   A 87  ? 0.47935 0.39548 0.38859 -0.00857 -0.00056 0.02281  164 SER   A CA  
627  C  C   . SER   A 87  ? 0.49344 0.40770 0.40609 -0.00448 -0.00017 0.02247  164 SER   A C   
628  O  O   . SER   A 87  ? 0.51856 0.42781 0.43008 -0.00208 -0.00098 0.02458  164 SER   A O   
629  C  CB  . SER   A 87  ? 0.47214 0.39071 0.38161 -0.00840 -0.00219 0.02445  164 SER   A CB  
630  O  OG  . SER   A 87  ? 0.45001 0.37389 0.36376 -0.00703 -0.00182 0.02296  164 SER   A OG  
631  N  N   . LEU   A 88  ? 0.49921 0.41720 0.41587 -0.00342 0.00122  0.02002  165 LEU   A N   
632  C  CA  . LEU   A 88  ? 0.52181 0.43792 0.44139 0.00036  0.00177  0.01964  165 LEU   A CA  
633  C  C   . LEU   A 88  ? 0.49398 0.40254 0.40973 0.00048  0.00224  0.01992  165 LEU   A C   
634  O  O   . LEU   A 88  ? 0.50697 0.41212 0.42369 0.00385  0.00282  0.02000  165 LEU   A O   
635  C  CB  . LEU   A 88  ? 0.48790 0.40959 0.41223 0.00105  0.00307  0.01694  165 LEU   A CB  
636  C  CG  . LEU   A 88  ? 0.41828 0.34608 0.34608 0.00160  0.00263  0.01659  165 LEU   A CG  
637  C  CD1 . LEU   A 88  ? 0.44164 0.37377 0.37351 0.00236  0.00407  0.01391  165 LEU   A CD1 
638  C  CD2 . LEU   A 88  ? 0.44740 0.37485 0.37711 0.00457  0.00117  0.01900  165 LEU   A CD2 
639  N  N   . ASP   A 89  ? 0.51249 0.41816 0.42351 -0.00327 0.00207  0.02013  166 ASP   A N   
640  C  CA  . ASP   A 89  ? 0.56916 0.46600 0.47421 -0.00424 0.00180  0.02127  166 ASP   A CA  
641  C  C   . ASP   A 89  ? 0.51250 0.40209 0.41539 -0.00038 0.00143  0.02340  166 ASP   A C   
642  O  O   . ASP   A 89  ? 0.47930 0.36061 0.37785 0.00042  0.00196  0.02360  166 ASP   A O   
643  C  CB  . ASP   A 89  ? 0.55852 0.45422 0.45888 -0.00861 0.00087  0.02252  166 ASP   A CB  
644  C  CG  . ASP   A 89  ? 0.62891 0.52726 0.52850 -0.01287 0.00150  0.02124  166 ASP   A CG  
645  O  OD1 . ASP   A 89  ? 0.68881 0.58658 0.58939 -0.01276 0.00227  0.01984  166 ASP   A OD1 
646  O  OD2 . ASP   A 89  ? 0.66525 0.56646 0.56327 -0.01635 0.00124  0.02190  166 ASP   A OD2 
647  N  N   . ASN   A 90  ? 0.47277 0.36500 0.37799 0.00168  0.00050  0.02532  167 ASN   A N   
648  C  CA  . ASN   A 90  ? 0.54001 0.42668 0.44390 0.00545  0.00010  0.02822  167 ASN   A CA  
649  C  C   . ASN   A 90  ? 0.54963 0.43571 0.45734 0.01063  0.00143  0.02819  167 ASN   A C   
650  O  O   . ASN   A 90  ? 0.53690 0.41703 0.44308 0.01444  0.00187  0.03057  167 ASN   A O   
651  C  CB  . ASN   A 90  ? 0.52634 0.41751 0.43198 0.00525  -0.00169 0.03069  167 ASN   A CB  
652  C  CG  . ASN   A 90  ? 0.57567 0.46748 0.47729 0.00017  -0.00278 0.03071  167 ASN   A CG  
653  O  OD1 . ASN   A 90  ? 0.61668 0.50230 0.51264 -0.00225 -0.00272 0.03082  167 ASN   A OD1 
654  N  ND2 . ASN   A 90  ? 0.63330 0.53228 0.53730 -0.00174 -0.00370 0.03061  167 ASN   A ND2 
655  N  N   . LEU   A 91  ? 0.52114 0.41311 0.43367 0.01102  0.00229  0.02569  168 LEU   A N   
656  C  CA  . LEU   A 91  ? 0.51520 0.40734 0.43160 0.01565  0.00367  0.02549  168 LEU   A CA  
657  C  C   . LEU   A 91  ? 0.51503 0.39796 0.42641 0.01654  0.00537  0.02434  168 LEU   A C   
658  O  O   . LEU   A 91  ? 0.50864 0.39231 0.42096 0.01607  0.00642  0.02177  168 LEU   A O   
659  C  CB  . LEU   A 91  ? 0.50214 0.40344 0.42480 0.01524  0.00380  0.02325  168 LEU   A CB  
660  C  CG  . LEU   A 91  ? 0.45270 0.36165 0.38063 0.01629  0.00243  0.02494  168 LEU   A CG  
661  C  CD1 . LEU   A 91  ? 0.49189 0.39966 0.41726 0.01519  0.00064  0.02801  168 LEU   A CD1 
662  C  CD2 . LEU   A 91  ? 0.44206 0.35861 0.37313 0.01356  0.00219  0.02237  168 LEU   A CD2 
663  N  N   . LYS   A 92  ? 0.50906 0.38254 0.41450 0.01783  0.00562  0.02643  169 LYS   A N   
664  C  CA  . LYS   A 92  ? 0.52936 0.39192 0.42774 0.01796  0.00709  0.02545  169 LYS   A CA  
665  C  C   . LYS   A 92  ? 0.48966 0.34966 0.38971 0.02287  0.00937  0.02492  169 LYS   A C   
666  O  O   . LYS   A 92  ? 0.51430 0.36566 0.40842 0.02257  0.01071  0.02348  169 LYS   A O   
667  C  CB  . LYS   A 92  ? 0.55657 0.40848 0.44718 0.01818  0.00691  0.02789  169 LYS   A CB  
668  C  CG  . LYS   A 92  ? 0.60617 0.45739 0.49231 0.01228  0.00495  0.02793  169 LYS   A CG  
669  C  CD  . LYS   A 92  ? 0.60772 0.45947 0.49161 0.00715  0.00476  0.02501  169 LYS   A CD  
670  C  CE  . LYS   A 92  ? 0.75040 0.59716 0.62710 0.00156  0.00330  0.02559  169 LYS   A CE  
671  N  NZ  . LYS   A 92  ? 0.76696 0.59921 0.63342 0.00092  0.00382  0.02599  169 LYS   A NZ  
672  N  N   . LYS   A 93  ? 0.49478 0.36194 0.40235 0.02704  0.00979  0.02615  170 LYS   A N   
673  C  CA  . LYS   A 93  ? 0.52135 0.38714 0.43125 0.03196  0.01213  0.02597  170 LYS   A CA  
674  C  C   . LYS   A 93  ? 0.50290 0.37863 0.42006 0.03154  0.01205  0.02370  170 LYS   A C   
675  O  O   . LYS   A 93  ? 0.53134 0.40783 0.45171 0.03562  0.01382  0.02378  170 LYS   A O   
676  C  CB  . LYS   A 93  ? 0.50731 0.37303 0.42028 0.03787  0.01303  0.02996  170 LYS   A CB  
677  C  CG  . LYS   A 93  ? 0.53971 0.39637 0.44639 0.03895  0.01308  0.03282  170 LYS   A CG  
678  C  CD  . LYS   A 93  ? 0.57485 0.43144 0.48524 0.04580  0.01471  0.03691  170 LYS   A CD  
679  C  CE  . LYS   A 93  ? 0.61525 0.47171 0.52542 0.04637  0.01312  0.04093  170 LYS   A CE  
680  N  NZ  . LYS   A 93  ? 0.65869 0.51632 0.57362 0.05343  0.01484  0.04551  170 LYS   A NZ  
681  N  N   . LEU   A 94  ? 0.47693 0.36009 0.39664 0.02695  0.01027  0.02184  171 LEU   A N   
682  C  CA  . LEU   A 94  ? 0.49020 0.38285 0.41684 0.02673  0.01013  0.01997  171 LEU   A CA  
683  C  C   . LEU   A 94  ? 0.48824 0.37771 0.41365 0.02714  0.01183  0.01738  171 LEU   A C   
684  O  O   . LEU   A 94  ? 0.49901 0.38459 0.41980 0.02351  0.01175  0.01543  171 LEU   A O   
685  C  CB  . LEU   A 94  ? 0.46479 0.36455 0.39315 0.02189  0.00834  0.01855  171 LEU   A CB  
686  C  CG  . LEU   A 94  ? 0.44072 0.34991 0.37584 0.02180  0.00817  0.01688  171 LEU   A CG  
687  C  CD1 . LEU   A 94  ? 0.43182 0.34654 0.37227 0.02480  0.00742  0.01931  171 LEU   A CD1 
688  C  CD2 . LEU   A 94  ? 0.40443 0.31865 0.33977 0.01716  0.00725  0.01499  171 LEU   A CD2 
689  N  N   . ARG   A 95  ? 0.50369 0.39518 0.43327 0.03126  0.01325  0.01758  172 ARG   A N   
690  C  CA  . ARG   A 95  ? 0.49512 0.38304 0.42308 0.03181  0.01494  0.01528  172 ARG   A CA  
691  C  C   . ARG   A 95  ? 0.50869 0.40540 0.44227 0.02981  0.01433  0.01282  172 ARG   A C   
692  O  O   . ARG   A 95  ? 0.50434 0.39891 0.43588 0.02799  0.01489  0.01051  172 ARG   A O   
693  C  CB  . ARG   A 95  ? 0.49770 0.38170 0.42617 0.03765  0.01736  0.01683  172 ARG   A CB  
694  C  CG  . ARG   A 95  ? 0.54760 0.41878 0.46765 0.03972  0.01911  0.01811  172 ARG   A CG  
695  C  CD  . ARG   A 95  ? 0.67866 0.54629 0.59935 0.04576  0.02215  0.01933  172 ARG   A CD  
696  N  NE  . ARG   A 95  ? 0.86147 0.72030 0.77749 0.04984  0.02391  0.02233  172 ARG   A NE  
697  C  CZ  . ARG   A 95  ? 0.98398 0.84130 0.90204 0.05620  0.02669  0.02486  172 ARG   A CZ  
698  N  NH1 . ARG   A 95  ? 0.94824 0.81266 0.87311 0.05898  0.02785  0.02483  172 ARG   A NH1 
699  N  NH2 . ARG   A 95  ? 1.05854 0.90707 0.97174 0.05997  0.02848  0.02770  172 ARG   A NH2 
700  N  N   . MET   A 96  ? 0.47959 0.38575 0.41974 0.02989  0.01312  0.01339  173 MET   A N   
701  C  CA  . MET   A 96  ? 0.44539 0.35909 0.39068 0.02874  0.01286  0.01122  173 MET   A CA  
702  C  C   . MET   A 96  ? 0.40742 0.32873 0.35585 0.02594  0.01103  0.01114  173 MET   A C   
703  O  O   . MET   A 96  ? 0.41165 0.33548 0.36163 0.02671  0.00994  0.01340  173 MET   A O   
704  C  CB  . MET   A 96  ? 0.47010 0.38663 0.42022 0.03299  0.01401  0.01190  173 MET   A CB  
705  C  CG  . MET   A 96  ? 0.50236 0.42802 0.45899 0.03342  0.01269  0.01295  173 MET   A CG  
706  S  SD  . MET   A 96  ? 0.61544 0.54740 0.57566 0.03094  0.01243  0.00960  173 MET   A SD  
707  C  CE  . MET   A 96  ? 0.44618 0.38709 0.41170 0.03032  0.01041  0.01102  173 MET   A CE  
708  N  N   . LEU   A 97  ? 0.42249 0.34712 0.37150 0.02268  0.01080  0.00871  174 LEU   A N   
709  C  CA  . LEU   A 97  ? 0.44124 0.37203 0.39211 0.01993  0.00966  0.00819  174 LEU   A CA  
710  C  C   . LEU   A 97  ? 0.44633 0.38280 0.40140 0.01953  0.01011  0.00594  174 LEU   A C   
711  O  O   . LEU   A 97  ? 0.38624 0.32173 0.34100 0.01874  0.01099  0.00422  174 LEU   A O   
712  C  CB  . LEU   A 97  ? 0.38495 0.31341 0.33137 0.01616  0.00931  0.00789  174 LEU   A CB  
713  C  CG  . LEU   A 97  ? 0.36966 0.30338 0.31677 0.01322  0.00871  0.00734  174 LEU   A CG  
714  C  CD1 . LEU   A 97  ? 0.37461 0.31100 0.32306 0.01413  0.00749  0.00902  174 LEU   A CD1 
715  C  CD2 . LEU   A 97  ? 0.36235 0.29314 0.30488 0.00990  0.00856  0.00766  174 LEU   A CD2 
716  N  N   . ASP   A 98  ? 0.41741 0.35948 0.37602 0.01986  0.00936  0.00614  175 ASP   A N   
717  C  CA  . ASP   A 98  ? 0.40429 0.35126 0.36673 0.01993  0.00973  0.00427  175 ASP   A CA  
718  C  C   . ASP   A 98  ? 0.38957 0.34028 0.35166 0.01721  0.00932  0.00333  175 ASP   A C   
719  O  O   . ASP   A 98  ? 0.36111 0.31356 0.32294 0.01669  0.00810  0.00456  175 ASP   A O   
720  C  CB  . ASP   A 98  ? 0.42377 0.37324 0.39017 0.02286  0.00935  0.00544  175 ASP   A CB  
721  C  CG  . ASP   A 98  ? 0.45916 0.41318 0.42913 0.02281  0.00960  0.00358  175 ASP   A CG  
722  O  OD1 . ASP   A 98  ? 0.45719 0.41262 0.42666 0.02071  0.01012  0.00147  175 ASP   A OD1 
723  O  OD2 . ASP   A 98  ? 0.46631 0.42260 0.43970 0.02498  0.00938  0.00445  175 ASP   A OD2 
724  N  N   . LEU   A 99  ? 0.41461 0.36647 0.37651 0.01549  0.01043  0.00135  176 LEU   A N   
725  C  CA  . LEU   A 99  ? 0.40477 0.35934 0.36564 0.01321  0.01080  0.00044  176 LEU   A CA  
726  C  C   . LEU   A 99  ? 0.38878 0.34684 0.35243 0.01343  0.01195  -0.00161 176 LEU   A C   
727  O  O   . LEU   A 99  ? 0.37655 0.33636 0.33935 0.01192  0.01311  -0.00259 176 LEU   A O   
728  C  CB  . LEU   A 99  ? 0.37822 0.33120 0.33595 0.01082  0.01138  0.00065  176 LEU   A CB  
729  C  CG  . LEU   A 99  ? 0.41912 0.36867 0.37305 0.00984  0.01026  0.00264  176 LEU   A CG  
730  C  CD1 . LEU   A 99  ? 0.37587 0.32294 0.32689 0.00763  0.01072  0.00300  176 LEU   A CD1 
731  C  CD2 . LEU   A 99  ? 0.39817 0.34933 0.35026 0.00847  0.00966  0.00312  176 LEU   A CD2 
732  N  N   . ARG   A 100 ? 0.40178 0.36078 0.36863 0.01544  0.01188  -0.00214 177 ARG   A N   
733  C  CA  . ARG   A 100 ? 0.44222 0.40409 0.41142 0.01556  0.01304  -0.00403 177 ARG   A CA  
734  C  C   . ARG   A 100 ? 0.42907 0.39268 0.39757 0.01502  0.01287  -0.00460 177 ARG   A C   
735  O  O   . ARG   A 100 ? 0.43142 0.39447 0.39825 0.01457  0.01142  -0.00339 177 ARG   A O   
736  C  CB  . ARG   A 100 ? 0.45250 0.41464 0.42502 0.01757  0.01312  -0.00455 177 ARG   A CB  
737  C  CG  . ARG   A 100 ? 0.46827 0.43000 0.44209 0.01947  0.01196  -0.00334 177 ARG   A CG  
738  C  CD  . ARG   A 100 ? 0.38342 0.34362 0.35904 0.02150  0.01235  -0.00330 177 ARG   A CD  
739  N  NE  . ARG   A 100 ? 0.45590 0.41552 0.43225 0.02345  0.01148  -0.00130 177 ARG   A NE  
740  C  CZ  . ARG   A 100 ? 0.47553 0.43795 0.45500 0.02493  0.01093  -0.00071 177 ARG   A CZ  
741  N  NH1 . ARG   A 100 ? 0.55709 0.52207 0.53892 0.02493  0.01125  -0.00228 177 ARG   A NH1 
742  N  NH2 . ARG   A 100 ? 0.49118 0.45407 0.47160 0.02642  0.01001  0.00182  177 ARG   A NH2 
743  N  N   . HIS   A 101 ? 0.44039 0.40576 0.40971 0.01490  0.01436  -0.00629 178 HIS   A N   
744  C  CA  . HIS   A 101 ? 0.44035 0.40602 0.40770 0.01423  0.01467  -0.00719 178 HIS   A CA  
745  C  C   . HIS   A 101 ? 0.40025 0.36426 0.36286 0.01224  0.01437  -0.00643 178 HIS   A C   
746  O  O   . HIS   A 101 ? 0.40640 0.36940 0.36657 0.01131  0.01279  -0.00574 178 HIS   A O   
747  C  CB  . HIS   A 101 ? 0.42779 0.39392 0.39656 0.01504  0.01307  -0.00706 178 HIS   A CB  
748  C  CG  . HIS   A 101 ? 0.56258 0.53026 0.53513 0.01667  0.01377  -0.00826 178 HIS   A CG  
749  N  ND1 . HIS   A 101 ? 0.63064 0.59893 0.60664 0.01818  0.01371  -0.00795 178 HIS   A ND1 
750  C  CD2 . HIS   A 101 ? 0.62197 0.59015 0.59486 0.01695  0.01454  -0.00974 178 HIS   A CD2 
751  C  CE1 . HIS   A 101 ? 0.62355 0.59317 0.60219 0.01922  0.01431  -0.00913 178 HIS   A CE1 
752  N  NE2 . HIS   A 101 ? 0.64334 0.61301 0.62036 0.01858  0.01479  -0.01020 178 HIS   A NE2 
753  N  N   . ASN   A 102 ? 0.37672 0.34063 0.33799 0.01133  0.01577  -0.00632 179 ASN   A N   
754  C  CA  . ASN   A 102 ? 0.39331 0.35576 0.34980 0.00936  0.01617  -0.00588 179 ASN   A CA  
755  C  C   . ASN   A 102 ? 0.39005 0.35376 0.34600 0.00922  0.01927  -0.00702 179 ASN   A C   
756  O  O   . ASN   A 102 ? 0.39749 0.36299 0.35637 0.01066  0.02082  -0.00816 179 ASN   A O   
757  C  CB  . ASN   A 102 ? 0.40204 0.36320 0.35724 0.00833  0.01482  -0.00400 179 ASN   A CB  
758  C  CG  . ASN   A 102 ? 0.42448 0.38413 0.37842 0.00812  0.01211  -0.00238 179 ASN   A CG  
759  O  OD1 . ASN   A 102 ? 0.42295 0.38130 0.37280 0.00634  0.01131  -0.00171 179 ASN   A OD1 
760  N  ND2 . ASN   A 102 ? 0.37708 0.33696 0.33445 0.00993  0.01076  -0.00148 179 ASN   A ND2 
761  N  N   . LYS   A 103 ? 0.39330 0.35634 0.34571 0.00762  0.02034  -0.00645 180 LYS   A N   
762  C  CA  . LYS   A 103 ? 0.41082 0.37551 0.36281 0.00771  0.02368  -0.00702 180 LYS   A CA  
763  C  C   . LYS   A 103 ? 0.39445 0.36106 0.34728 0.00647  0.02426  -0.00546 180 LYS   A C   
764  O  O   . LYS   A 103 ? 0.41595 0.38294 0.36602 0.00539  0.02628  -0.00502 180 LYS   A O   
765  C  CB  . LYS   A 103 ? 0.42871 0.39047 0.37461 0.00689  0.02515  -0.00792 180 LYS   A CB  
766  C  CG  . LYS   A 103 ? 0.42841 0.38776 0.37276 0.00757  0.02443  -0.00938 180 LYS   A CG  
767  C  CD  . LYS   A 103 ? 0.51501 0.46984 0.45154 0.00599  0.02525  -0.01015 180 LYS   A CD  
768  C  CE  . LYS   A 103 ? 0.65661 0.60859 0.59106 0.00612  0.02415  -0.01144 180 LYS   A CE  
769  N  NZ  . LYS   A 103 ? 0.59704 0.54333 0.52253 0.00406  0.02466  -0.01228 180 LYS   A NZ  
770  N  N   . LEU   A 104 ? 0.41008 0.37756 0.36625 0.00646  0.02256  -0.00454 181 LEU   A N   
771  C  CA  . LEU   A 104 ? 0.42720 0.39577 0.38356 0.00472  0.02255  -0.00288 181 LEU   A CA  
772  C  C   . LEU   A 104 ? 0.42062 0.39386 0.38055 0.00489  0.02503  -0.00248 181 LEU   A C   
773  O  O   . LEU   A 104 ? 0.43863 0.41401 0.40268 0.00638  0.02538  -0.00304 181 LEU   A O   
774  C  CB  . LEU   A 104 ? 0.41243 0.37895 0.36991 0.00453  0.01992  -0.00206 181 LEU   A CB  
775  C  CG  . LEU   A 104 ? 0.37812 0.34065 0.33326 0.00490  0.01747  -0.00176 181 LEU   A CG  
776  C  CD1 . LEU   A 104 ? 0.41319 0.37381 0.37011 0.00572  0.01592  -0.00127 181 LEU   A CD1 
777  C  CD2 . LEU   A 104 ? 0.39172 0.35209 0.34236 0.00284  0.01681  -0.00039 181 LEU   A CD2 
778  N  N   . ARG   A 105 ? 0.44652 0.42174 0.40517 0.00333  0.02671  -0.00118 182 ARG   A N   
779  C  CA  . ARG   A 105 ? 0.45576 0.43643 0.41853 0.00314  0.02875  0.00016  182 ARG   A CA  
780  C  C   . ARG   A 105 ? 0.47540 0.45695 0.43956 0.00071  0.02670  0.00212  182 ARG   A C   
781  O  O   . ARG   A 105 ? 0.45740 0.44394 0.42510 -0.00023 0.02776  0.00388  182 ARG   A O   
782  C  CB  . ARG   A 105 ? 0.45608 0.43923 0.41720 0.00293  0.03215  0.00091  182 ARG   A CB  
783  C  CG  . ARG   A 105 ? 0.53784 0.52021 0.49784 0.00562  0.03498  -0.00097 182 ARG   A CG  
784  C  CD  . ARG   A 105 ? 0.59675 0.57999 0.55358 0.00560  0.03868  -0.00040 182 ARG   A CD  
785  N  NE  . ARG   A 105 ? 0.66472 0.64356 0.61518 0.00341  0.03744  -0.00052 182 ARG   A NE  
786  C  CZ  . ARG   A 105 ? 0.70349 0.67669 0.64904 0.00329  0.03576  -0.00227 182 ARG   A CZ  
787  N  NH1 . ARG   A 105 ? 0.74857 0.71971 0.69476 0.00508  0.03494  -0.00410 182 ARG   A NH1 
788  N  NH2 . ARG   A 105 ? 0.57742 0.54721 0.51733 0.00109  0.03468  -0.00190 182 ARG   A NH2 
789  N  N   . GLU   A 106 ? 0.47371 0.45031 0.43502 -0.00033 0.02378  0.00204  183 GLU   A N   
790  C  CA  . GLU   A 106 ? 0.42495 0.40013 0.38548 -0.00292 0.02172  0.00374  183 GLU   A CA  
791  C  C   . GLU   A 106 ? 0.43350 0.40205 0.39051 -0.00261 0.01914  0.00312  183 GLU   A C   
792  O  O   . GLU   A 106 ? 0.42828 0.39447 0.38358 -0.00099 0.01887  0.00198  183 GLU   A O   
793  C  CB  . GLU   A 106 ? 0.43066 0.40756 0.38912 -0.00586 0.02237  0.00587  183 GLU   A CB  
794  C  CG  . GLU   A 106 ? 0.45577 0.42827 0.40890 -0.00646 0.02170  0.00567  183 GLU   A CG  
795  C  CD  . GLU   A 106 ? 0.53274 0.50757 0.48382 -0.00896 0.02305  0.00750  183 GLU   A CD  
796  O  OE1 . GLU   A 106 ? 0.61339 0.59401 0.56780 -0.00994 0.02480  0.00904  183 GLU   A OE1 
797  O  OE2 . GLU   A 106 ? 0.51897 0.49023 0.46535 -0.00995 0.02238  0.00765  183 GLU   A OE2 
798  N  N   . ILE   A 107 ? 0.43262 0.39800 0.38825 -0.00428 0.01727  0.00415  184 ILE   A N   
799  C  CA  . ILE   A 107 ? 0.40451 0.36305 0.35610 -0.00404 0.01521  0.00418  184 ILE   A CA  
800  C  C   . ILE   A 107 ? 0.40106 0.35788 0.34847 -0.00599 0.01492  0.00545  184 ILE   A C   
801  O  O   . ILE   A 107 ? 0.38137 0.33966 0.32761 -0.00897 0.01514  0.00703  184 ILE   A O   
802  C  CB  . ILE   A 107 ? 0.39760 0.35202 0.34778 -0.00523 0.01369  0.00480  184 ILE   A CB  
803  C  CG1 . ILE   A 107 ? 0.41848 0.37503 0.37280 -0.00341 0.01407  0.00354  184 ILE   A CG1 
804  C  CG2 . ILE   A 107 ? 0.34423 0.29093 0.28977 -0.00451 0.01211  0.00507  184 ILE   A CG2 
805  C  CD1 . ILE   A 107 ? 0.42499 0.37748 0.37758 -0.00482 0.01276  0.00400  184 ILE   A CD1 
806  N  N   . PRO   A 108 ? 0.41644 0.37074 0.36168 -0.00467 0.01439  0.00508  185 PRO   A N   
807  C  CA  . PRO   A 108 ? 0.39736 0.34983 0.33832 -0.00671 0.01396  0.00642  185 PRO   A CA  
808  C  C   . PRO   A 108 ? 0.43860 0.38658 0.37607 -0.00917 0.01247  0.00813  185 PRO   A C   
809  O  O   . PRO   A 108 ? 0.41589 0.35924 0.35247 -0.00837 0.01123  0.00813  185 PRO   A O   
810  C  CB  . PRO   A 108 ? 0.38882 0.33848 0.32830 -0.00469 0.01285  0.00606  185 PRO   A CB  
811  C  CG  . PRO   A 108 ? 0.39753 0.35008 0.34109 -0.00196 0.01364  0.00421  185 PRO   A CG  
812  C  CD  . PRO   A 108 ? 0.38429 0.33796 0.33107 -0.00155 0.01407  0.00369  185 PRO   A CD  
813  N  N   . SER   A 109 ? 0.42389 0.37277 0.35881 -0.01228 0.01272  0.00964  186 SER   A N   
814  C  CA  . SER   A 109 ? 0.46075 0.40569 0.39220 -0.01535 0.01132  0.01137  186 SER   A CA  
815  C  C   . SER   A 109 ? 0.46450 0.40093 0.39120 -0.01458 0.00934  0.01188  186 SER   A C   
816  O  O   . SER   A 109 ? 0.47804 0.40899 0.40142 -0.01609 0.00814  0.01272  186 SER   A O   
817  C  CB  . SER   A 109 ? 0.39905 0.34706 0.32880 -0.01898 0.01197  0.01316  186 SER   A CB  
818  O  OG  . SER   A 109 ? 0.50117 0.44740 0.42770 -0.01894 0.01184  0.01347  186 SER   A OG  
819  N  N   . VAL   A 110 ? 0.47039 0.40528 0.39638 -0.01228 0.00897  0.01163  187 VAL   A N   
820  C  CA  . VAL   A 110 ? 0.46200 0.38933 0.38430 -0.01088 0.00735  0.01256  187 VAL   A CA  
821  C  C   . VAL   A 110 ? 0.43284 0.35668 0.35633 -0.00819 0.00721  0.01168  187 VAL   A C   
822  O  O   . VAL   A 110 ? 0.44077 0.35706 0.36020 -0.00768 0.00635  0.01257  187 VAL   A O   
823  C  CB  . VAL   A 110 ? 0.48489 0.41240 0.40707 -0.00894 0.00678  0.01297  187 VAL   A CB  
824  C  CG1 . VAL   A 110 ? 0.38664 0.31844 0.31376 -0.00582 0.00744  0.01135  187 VAL   A CG1 
825  C  CG2 . VAL   A 110 ? 0.47857 0.39858 0.39701 -0.00755 0.00524  0.01468  187 VAL   A CG2 
826  N  N   . VAL   A 111 ? 0.38762 0.31629 0.31618 -0.00633 0.00824  0.00995  188 VAL   A N   
827  C  CA  . VAL   A 111 ? 0.39080 0.31642 0.32055 -0.00364 0.00827  0.00907  188 VAL   A CA  
828  C  C   . VAL   A 111 ? 0.40716 0.32700 0.33281 -0.00587 0.00780  0.00955  188 VAL   A C   
829  O  O   . VAL   A 111 ? 0.39565 0.30869 0.31863 -0.00400 0.00759  0.00954  188 VAL   A O   
830  C  CB  . VAL   A 111 ? 0.38553 0.31764 0.32127 -0.00184 0.00940  0.00720  188 VAL   A CB  
831  C  CG1 . VAL   A 111 ? 0.39274 0.32186 0.32933 0.00014  0.00952  0.00633  188 VAL   A CG1 
832  C  CG2 . VAL   A 111 ? 0.36187 0.29735 0.30035 0.00062  0.00949  0.00679  188 VAL   A CG2 
833  N  N   . TYR   A 112 ? 0.41065 0.33274 0.33525 -0.01001 0.00768  0.01020  189 TYR   A N   
834  C  CA  . TYR   A 112 ? 0.44213 0.35865 0.36203 -0.01321 0.00678  0.01102  189 TYR   A CA  
835  C  C   . TYR   A 112 ? 0.44190 0.34871 0.35418 -0.01426 0.00562  0.01249  189 TYR   A C   
836  O  O   . TYR   A 112 ? 0.42774 0.32802 0.33455 -0.01711 0.00473  0.01318  189 TYR   A O   
837  C  CB  . TYR   A 112 ? 0.47404 0.39663 0.39534 -0.01772 0.00674  0.01203  189 TYR   A CB  
838  C  CG  . TYR   A 112 ? 0.42766 0.35925 0.35590 -0.01725 0.00794  0.01111  189 TYR   A CG  
839  C  CD1 . TYR   A 112 ? 0.45606 0.38720 0.38536 -0.01763 0.00765  0.01061  189 TYR   A CD1 
840  C  CD2 . TYR   A 112 ? 0.42801 0.36809 0.36117 -0.01661 0.00947  0.01093  189 TYR   A CD2 
841  C  CE1 . TYR   A 112 ? 0.44258 0.38213 0.37844 -0.01716 0.00871  0.01008  189 TYR   A CE1 
842  C  CE2 . TYR   A 112 ? 0.42528 0.37315 0.36452 -0.01592 0.01085  0.01031  189 TYR   A CE2 
843  C  CZ  . TYR   A 112 ? 0.45796 0.40584 0.39889 -0.01614 0.01039  0.00999  189 TYR   A CZ  
844  O  OH  . TYR   A 112 ? 0.44403 0.39966 0.39119 -0.01524 0.01174  0.00961  189 TYR   A OH  
845  N  N   . ARG   A 113 ? 0.46296 0.36836 0.37432 -0.01235 0.00549  0.01317  190 ARG   A N   
846  C  CA  . ARG   A 113 ? 0.45600 0.35174 0.36038 -0.01246 0.00456  0.01469  190 ARG   A CA  
847  C  C   . ARG   A 113 ? 0.46187 0.35210 0.36582 -0.00727 0.00504  0.01457  190 ARG   A C   
848  O  O   . ARG   A 113 ? 0.47338 0.35506 0.37170 -0.00642 0.00462  0.01600  190 ARG   A O   
849  C  CB  . ARG   A 113 ? 0.45459 0.35219 0.35763 -0.01436 0.00390  0.01624  190 ARG   A CB  
850  C  CG  . ARG   A 113 ? 0.47436 0.37752 0.37769 -0.01933 0.00375  0.01684  190 ARG   A CG  
851  C  CD  . ARG   A 113 ? 0.50852 0.41033 0.40807 -0.02172 0.00295  0.01866  190 ARG   A CD  
852  N  NE  . ARG   A 113 ? 0.55551 0.46206 0.45821 -0.01941 0.00339  0.01852  190 ARG   A NE  
853  C  CZ  . ARG   A 113 ? 0.58089 0.49624 0.48809 -0.01994 0.00454  0.01779  190 ARG   A CZ  
854  N  NH1 . ARG   A 113 ? 0.53468 0.45595 0.44476 -0.02218 0.00559  0.01734  190 ARG   A NH1 
855  N  NH2 . ARG   A 113 ? 0.55892 0.47696 0.46747 -0.01820 0.00470  0.01771  190 ARG   A NH2 
856  N  N   . LEU   A 114 ? 0.44113 0.33601 0.35088 -0.00369 0.00600  0.01316  191 LEU   A N   
857  C  CA  . LEU   A 114 ? 0.46090 0.35166 0.37110 0.00141  0.00668  0.01341  191 LEU   A CA  
858  C  C   . LEU   A 114 ? 0.50455 0.38732 0.41070 0.00229  0.00748  0.01263  191 LEU   A C   
859  O  O   . LEU   A 114 ? 0.50588 0.39070 0.41551 0.00462  0.00846  0.01123  191 LEU   A O   
860  C  CB  . LEU   A 114 ? 0.39290 0.29240 0.31089 0.00446  0.00718  0.01255  191 LEU   A CB  
861  C  CG  . LEU   A 114 ? 0.49248 0.39913 0.41318 0.00282  0.00644  0.01303  191 LEU   A CG  
862  C  CD1 . LEU   A 114 ? 0.43078 0.34530 0.35805 0.00504  0.00680  0.01203  191 LEU   A CD1 
863  C  CD2 . LEU   A 114 ? 0.52218 0.42471 0.43929 0.00316  0.00540  0.01548  191 LEU   A CD2 
864  N  N   . ASP   A 115 ? 0.43459 0.30740 0.33249 0.00016  0.00704  0.01360  192 ASP   A N   
865  C  CA  . ASP   A 115 ? 0.54060 0.40478 0.43270 -0.00058 0.00757  0.01275  192 ASP   A CA  
866  C  C   . ASP   A 115 ? 0.54674 0.40337 0.43680 0.00498  0.00938  0.01279  192 ASP   A C   
867  O  O   . ASP   A 115 ? 0.54741 0.39500 0.43120 0.00474  0.01014  0.01209  192 ASP   A O   
868  C  CB  . ASP   A 115 ? 0.51610 0.37145 0.39897 -0.00553 0.00634  0.01378  192 ASP   A CB  
869  C  CG  . ASP   A 115 ? 0.60206 0.44803 0.47865 -0.00379 0.00640  0.01564  192 ASP   A CG  
870  O  OD1 . ASP   A 115 ? 0.69205 0.52851 0.56417 0.00015  0.00788  0.01581  192 ASP   A OD1 
871  O  OD2 . ASP   A 115 ? 0.66842 0.51629 0.54437 -0.00622 0.00515  0.01706  192 ASP   A OD2 
872  N  N   . SER   A 116 ? 0.49566 0.35570 0.39058 0.00984  0.01012  0.01381  193 SER   A N   
873  C  CA  . SER   A 116 ? 0.51389 0.36985 0.40931 0.01560  0.01216  0.01406  193 SER   A CA  
874  C  C   . SER   A 116 ? 0.48443 0.34910 0.38774 0.01766  0.01292  0.01241  193 SER   A C   
875  O  O   . SER   A 116 ? 0.51169 0.37341 0.41552 0.02209  0.01479  0.01241  193 SER   A O   
876  C  CB  . SER   A 116 ? 0.48622 0.34159 0.38308 0.01988  0.01249  0.01677  193 SER   A CB  
877  O  OG  . SER   A 116 ? 0.56323 0.42991 0.46747 0.01922  0.01098  0.01743  193 SER   A OG  
878  N  N   . LEU   A 117 ? 0.48447 0.35936 0.39359 0.01466  0.01172  0.01109  194 LEU   A N   
879  C  CA  . LEU   A 117 ? 0.48899 0.37193 0.40536 0.01645  0.01233  0.00957  194 LEU   A CA  
880  C  C   . LEU   A 117 ? 0.48882 0.36624 0.40222 0.01707  0.01362  0.00808  194 LEU   A C   
881  O  O   . LEU   A 117 ? 0.46402 0.33517 0.37111 0.01346  0.01323  0.00739  194 LEU   A O   
882  C  CB  . LEU   A 117 ? 0.46144 0.35438 0.38289 0.01281  0.01112  0.00835  194 LEU   A CB  
883  C  CG  . LEU   A 117 ? 0.46650 0.36742 0.39267 0.01259  0.01018  0.00914  194 LEU   A CG  
884  C  CD1 . LEU   A 117 ? 0.46587 0.37455 0.39554 0.00918  0.00975  0.00764  194 LEU   A CD1 
885  C  CD2 . LEU   A 117 ? 0.46593 0.37133 0.39772 0.01700  0.01059  0.00978  194 LEU   A CD2 
886  N  N   . THR   A 118 ? 0.46890 0.34877 0.38671 0.02138  0.01504  0.00775  195 THR   A N   
887  C  CA  . THR   A 118 ? 0.48416 0.36113 0.40074 0.02201  0.01628  0.00610  195 THR   A CA  
888  C  C   . THR   A 118 ? 0.48031 0.36788 0.40530 0.02245  0.01611  0.00468  195 THR   A C   
889  O  O   . THR   A 118 ? 0.44208 0.32851 0.36665 0.02231  0.01682  0.00320  195 THR   A O   
890  C  CB  . THR   A 118 ? 0.49522 0.36356 0.40807 0.02713  0.01873  0.00703  195 THR   A CB  
891  O  OG1 . THR   A 118 ? 0.54543 0.41982 0.46500 0.03180  0.01936  0.00884  195 THR   A OG1 
892  C  CG2 . THR   A 118 ? 0.46095 0.31657 0.36377 0.02659  0.01921  0.00816  195 THR   A CG2 
893  N  N   . THR   A 119 ? 0.45298 0.35017 0.38485 0.02266  0.01514  0.00507  196 THR   A N   
894  C  CA  . THR   A 119 ? 0.48287 0.38931 0.42210 0.02319  0.01503  0.00381  196 THR   A CA  
895  C  C   . THR   A 119 ? 0.46403 0.37858 0.40719 0.02053  0.01356  0.00365  196 THR   A C   
896  O  O   . THR   A 119 ? 0.45282 0.36962 0.39731 0.02133  0.01292  0.00511  196 THR   A O   
897  C  CB  . THR   A 119 ? 0.49798 0.40684 0.44166 0.02811  0.01609  0.00483  196 THR   A CB  
898  O  OG1 . THR   A 119 ? 0.54671 0.44725 0.48608 0.03102  0.01801  0.00516  196 THR   A OG1 
899  C  CG2 . THR   A 119 ? 0.48990 0.40724 0.44027 0.02833  0.01591  0.00344  196 THR   A CG2 
900  N  N   . LEU   A 120 ? 0.48372 0.40260 0.42864 0.01752  0.01316  0.00208  197 LEU   A N   
901  C  CA  . LEU   A 120 ? 0.42900 0.35497 0.37703 0.01512  0.01236  0.00180  197 LEU   A CA  
902  C  C   . LEU   A 120 ? 0.44463 0.37759 0.39828 0.01544  0.01273  0.00020  197 LEU   A C   
903  O  O   . LEU   A 120 ? 0.41212 0.34509 0.36601 0.01433  0.01304  -0.00085 197 LEU   A O   
904  C  CB  . LEU   A 120 ? 0.38840 0.31263 0.33257 0.01087  0.01177  0.00205  197 LEU   A CB  
905  C  CG  . LEU   A 120 ? 0.41649 0.34737 0.36311 0.00859  0.01143  0.00209  197 LEU   A CG  
906  C  CD1 . LEU   A 120 ? 0.39295 0.32488 0.34002 0.01010  0.01104  0.00307  197 LEU   A CD1 
907  C  CD2 . LEU   A 120 ? 0.37859 0.30790 0.32150 0.00441  0.01091  0.00288  197 LEU   A CD2 
908  N  N   . TYR   A 121 ? 0.41938 0.35787 0.37710 0.01676  0.01256  0.00015  198 TYR   A N   
909  C  CA  . TYR   A 121 ? 0.40444 0.34896 0.36701 0.01727  0.01292  -0.00129 198 TYR   A CA  
910  C  C   . TYR   A 121 ? 0.38445 0.33373 0.34803 0.01509  0.01290  -0.00174 198 TYR   A C   
911  O  O   . TYR   A 121 ? 0.42722 0.37757 0.39023 0.01499  0.01237  -0.00100 198 TYR   A O   
912  C  CB  . TYR   A 121 ? 0.40920 0.35568 0.37494 0.02033  0.01277  -0.00091 198 TYR   A CB  
913  C  CG  . TYR   A 121 ? 0.49453 0.43703 0.45990 0.02317  0.01335  -0.00029 198 TYR   A CG  
914  C  CD1 . TYR   A 121 ? 0.46886 0.41024 0.43474 0.02364  0.01417  -0.00157 198 TYR   A CD1 
915  C  CD2 . TYR   A 121 ? 0.46905 0.40887 0.43349 0.02557  0.01324  0.00180  198 TYR   A CD2 
916  C  CE1 . TYR   A 121 ? 0.48917 0.42634 0.45404 0.02637  0.01510  -0.00107 198 TYR   A CE1 
917  C  CE2 . TYR   A 121 ? 0.49054 0.42653 0.45455 0.02871  0.01435  0.00255  198 TYR   A CE2 
918  C  CZ  . TYR   A 121 ? 0.50512 0.43955 0.46907 0.02908  0.01539  0.00097  198 TYR   A CZ  
919  O  OH  . TYR   A 121 ? 0.53127 0.46139 0.49415 0.03226  0.01687  0.00159  198 TYR   A OH  
920  N  N   . LEU   A 122 ? 0.35227 0.30447 0.31731 0.01348  0.01359  -0.00276 199 LEU   A N   
921  C  CA  . LEU   A 122 ? 0.39627 0.35290 0.36228 0.01190  0.01424  -0.00311 199 LEU   A CA  
922  C  C   . LEU   A 122 ? 0.39668 0.35789 0.36671 0.01280  0.01524  -0.00454 199 LEU   A C   
923  O  O   . LEU   A 122 ? 0.37511 0.33978 0.34609 0.01175  0.01638  -0.00483 199 LEU   A O   
924  C  CB  . LEU   A 122 ? 0.35529 0.31170 0.31925 0.00896  0.01445  -0.00225 199 LEU   A CB  
925  C  CG  . LEU   A 122 ? 0.37080 0.32195 0.33007 0.00788  0.01342  -0.00082 199 LEU   A CG  
926  C  CD1 . LEU   A 122 ? 0.38609 0.33443 0.34269 0.00522  0.01304  0.00003  199 LEU   A CD1 
927  C  CD2 . LEU   A 122 ? 0.38456 0.33691 0.34215 0.00682  0.01344  -0.00014 199 LEU   A CD2 
928  N  N   . ARG   A 123 ? 0.38498 0.34618 0.35730 0.01487  0.01503  -0.00530 200 ARG   A N   
929  C  CA  . ARG   A 123 ? 0.41479 0.37971 0.39064 0.01568  0.01588  -0.00659 200 ARG   A CA  
930  C  C   . ARG   A 123 ? 0.42619 0.39371 0.40210 0.01561  0.01667  -0.00720 200 ARG   A C   
931  O  O   . ARG   A 123 ? 0.43168 0.39806 0.40538 0.01548  0.01603  -0.00681 200 ARG   A O   
932  C  CB  . ARG   A 123 ? 0.43976 0.40399 0.41761 0.01787  0.01538  -0.00713 200 ARG   A CB  
933  C  CG  . ARG   A 123 ? 0.49083 0.45847 0.47209 0.01875  0.01609  -0.00845 200 ARG   A CG  
934  C  CD  . ARG   A 123 ? 0.56220 0.52951 0.54518 0.02076  0.01545  -0.00874 200 ARG   A CD  
935  N  NE  . ARG   A 123 ? 0.57931 0.54931 0.56517 0.02145  0.01598  -0.00995 200 ARG   A NE  
936  C  CZ  . ARG   A 123 ? 0.60253 0.57262 0.59048 0.02278  0.01576  -0.01031 200 ARG   A CZ  
937  N  NH1 . ARG   A 123 ? 0.60812 0.57571 0.59556 0.02378  0.01532  -0.00960 200 ARG   A NH1 
938  N  NH2 . ARG   A 123 ? 0.57250 0.54487 0.56279 0.02326  0.01618  -0.01135 200 ARG   A NH2 
939  N  N   . PHE   A 124 ? 0.39075 0.36141 0.36880 0.01565  0.01813  -0.00802 201 PHE   A N   
940  C  CA  . PHE   A 124 ? 0.40585 0.37799 0.38339 0.01598  0.01943  -0.00891 201 PHE   A CA  
941  C  C   . PHE   A 124 ? 0.40646 0.37780 0.38031 0.01448  0.01996  -0.00828 201 PHE   A C   
942  O  O   . PHE   A 124 ? 0.41124 0.38066 0.38210 0.01417  0.01923  -0.00834 201 PHE   A O   
943  C  CB  . PHE   A 124 ? 0.45597 0.42714 0.43352 0.01724  0.01854  -0.00981 201 PHE   A CB  
944  C  CG  . PHE   A 124 ? 0.47446 0.44640 0.45157 0.01775  0.02007  -0.01110 201 PHE   A CG  
945  C  CD1 . PHE   A 124 ? 0.48017 0.45386 0.46040 0.01904  0.02109  -0.01197 201 PHE   A CD1 
946  C  CD2 . PHE   A 124 ? 0.48114 0.45138 0.45406 0.01688  0.02059  -0.01140 201 PHE   A CD2 
947  C  CE1 . PHE   A 124 ? 0.44589 0.41935 0.42507 0.01975  0.02279  -0.01311 201 PHE   A CE1 
948  C  CE2 . PHE   A 124 ? 0.43986 0.40936 0.41106 0.01737  0.02232  -0.01269 201 PHE   A CE2 
949  C  CZ  . PHE   A 124 ? 0.43741 0.40838 0.41175 0.01896  0.02351  -0.01355 201 PHE   A CZ  
950  N  N   . ASN   A 125 ? 0.38558 0.35875 0.35973 0.01330  0.02118  -0.00744 202 ASN   A N   
951  C  CA  . ASN   A 125 ? 0.36712 0.34032 0.33816 0.01187  0.02228  -0.00677 202 ASN   A CA  
952  C  C   . ASN   A 125 ? 0.42324 0.40058 0.39669 0.01189  0.02487  -0.00632 202 ASN   A C   
953  O  O   . ASN   A 125 ? 0.42965 0.40948 0.40681 0.01326  0.02576  -0.00673 202 ASN   A O   
954  C  CB  . ASN   A 125 ? 0.41718 0.38811 0.38578 0.01005  0.02061  -0.00532 202 ASN   A CB  
955  C  CG  . ASN   A 125 ? 0.42634 0.39364 0.39188 0.01017  0.01870  -0.00526 202 ASN   A CG  
956  O  OD1 . ASN   A 125 ? 0.38781 0.35425 0.35030 0.00966  0.01895  -0.00544 202 ASN   A OD1 
957  N  ND2 . ASN   A 125 ? 0.40904 0.37413 0.37519 0.01085  0.01689  -0.00475 202 ASN   A ND2 
958  N  N   . ARG   A 126 ? 0.39966 0.37818 0.37137 0.01044  0.02616  -0.00516 203 ARG   A N   
959  C  CA  . ARG   A 126 ? 0.43617 0.41956 0.41075 0.01049  0.02877  -0.00399 203 ARG   A CA  
960  C  C   . ARG   A 126 ? 0.41853 0.40398 0.39371 0.00785  0.02797  -0.00169 203 ARG   A C   
961  O  O   . ARG   A 126 ? 0.43459 0.42366 0.41037 0.00699  0.02998  -0.00010 203 ARG   A O   
962  C  CB  . ARG   A 126 ? 0.49294 0.47635 0.46482 0.01143  0.03191  -0.00451 203 ARG   A CB  
963  C  CG  . ARG   A 126 ? 0.61818 0.59823 0.58796 0.01345  0.03247  -0.00681 203 ARG   A CG  
964  C  CD  . ARG   A 126 ? 0.77114 0.74905 0.73598 0.01399  0.03552  -0.00755 203 ARG   A CD  
965  N  NE  . ARG   A 126 ? 0.80107 0.78320 0.76820 0.01520  0.03941  -0.00632 203 ARG   A NE  
966  C  CZ  . ARG   A 126 ? 0.75864 0.74347 0.72963 0.01773  0.04173  -0.00633 203 ARG   A CZ  
967  N  NH1 . ARG   A 126 ? 0.69543 0.67887 0.66810 0.01911  0.04050  -0.00776 203 ARG   A NH1 
968  N  NH2 . ARG   A 126 ? 0.77166 0.76098 0.74512 0.01896  0.04542  -0.00458 203 ARG   A NH2 
969  N  N   . ILE   A 127 ? 0.43368 0.41657 0.40838 0.00649  0.02512  -0.00135 204 ILE   A N   
970  C  CA  . ILE   A 127 ? 0.40632 0.38948 0.38008 0.00348  0.02391  0.00076  204 ILE   A CA  
971  C  C   . ILE   A 127 ? 0.42415 0.41318 0.40255 0.00246  0.02471  0.00267  204 ILE   A C   
972  O  O   . ILE   A 127 ? 0.39221 0.38280 0.37409 0.00350  0.02438  0.00234  204 ILE   A O   
973  C  CB  . ILE   A 127 ? 0.42027 0.39776 0.39134 0.00264  0.02095  0.00048  204 ILE   A CB  
974  C  CG1 . ILE   A 127 ? 0.39062 0.36332 0.35766 0.00354  0.02012  -0.00057 204 ILE   A CG1 
975  C  CG2 . ILE   A 127 ? 0.41329 0.39009 0.38272 -0.00078 0.01958  0.00262  204 ILE   A CG2 
976  C  CD1 . ILE   A 127 ? 0.38199 0.34931 0.34716 0.00400  0.01781  -0.00086 204 ILE   A CD1 
977  N  N   . THR   A 128 ? 0.43056 0.42331 0.40924 0.00027  0.02568  0.00501  205 THR   A N   
978  C  CA  . THR   A 128 ? 0.42996 0.42953 0.41367 -0.00095 0.02638  0.00759  205 THR   A CA  
979  C  C   . THR   A 128 ? 0.45113 0.45012 0.43373 -0.00516 0.02357  0.00984  205 THR   A C   
980  O  O   . THR   A 128 ? 0.47323 0.47696 0.45978 -0.00667 0.02303  0.01197  205 THR   A O   
981  C  CB  . THR   A 128 ? 0.47089 0.47665 0.45682 -0.00037 0.02987  0.00935  205 THR   A CB  
982  O  OG1 . THR   A 128 ? 0.48214 0.48703 0.46440 -0.00312 0.02960  0.01073  205 THR   A OG1 
983  C  CG2 . THR   A 128 ? 0.38663 0.39119 0.37178 0.00351  0.03284  0.00697  205 THR   A CG2 
984  N  N   . THR   A 129 ? 0.43934 0.43215 0.41630 -0.00718 0.02161  0.00952  206 THR   A N   
985  C  CA  . THR   A 129 ? 0.45041 0.44149 0.42481 -0.01157 0.01912  0.01175  206 THR   A CA  
986  C  C   . THR   A 129 ? 0.45204 0.43351 0.42042 -0.01202 0.01659  0.01011  206 THR   A C   
987  O  O   . THR   A 129 ? 0.46549 0.44248 0.43145 -0.00942 0.01684  0.00793  206 THR   A O   
988  C  CB  . THR   A 129 ? 0.48273 0.47672 0.45585 -0.01428 0.01987  0.01417  206 THR   A CB  
989  O  OG1 . THR   A 129 ? 0.53549 0.53887 0.51461 -0.01360 0.02260  0.01618  206 THR   A OG1 
990  C  CG2 . THR   A 129 ? 0.50944 0.50066 0.47891 -0.01930 0.01700  0.01649  206 THR   A CG2 
991  N  N   . VAL   A 130 ? 0.47051 0.44872 0.43625 -0.01540 0.01421  0.01144  207 VAL   A N   
992  C  CA  . VAL   A 130 ? 0.44614 0.41445 0.40490 -0.01647 0.01210  0.01063  207 VAL   A CA  
993  C  C   . VAL   A 130 ? 0.44375 0.41055 0.39843 -0.02163 0.01046  0.01338  207 VAL   A C   
994  O  O   . VAL   A 130 ? 0.45990 0.42978 0.41574 -0.02517 0.00931  0.01559  207 VAL   A O   
995  C  CB  . VAL   A 130 ? 0.42607 0.38943 0.38366 -0.01559 0.01085  0.00926  207 VAL   A CB  
996  C  CG1 . VAL   A 130 ? 0.37762 0.33003 0.32713 -0.01686 0.00905  0.00890  207 VAL   A CG1 
997  C  CG2 . VAL   A 130 ? 0.37006 0.33483 0.33152 -0.01065 0.01233  0.00667  207 VAL   A CG2 
998  N  N   . GLU   A 131 ? 0.42946 0.39165 0.37931 -0.02234 0.01017  0.01350  208 GLU   A N   
999  C  CA  . GLU   A 131 ? 0.42894 0.39050 0.37511 -0.02729 0.00887  0.01626  208 GLU   A CA  
1000 C  C   . GLU   A 131 ? 0.42238 0.37530 0.36185 -0.03096 0.00611  0.01701  208 GLU   A C   
1001 O  O   . GLU   A 131 ? 0.38577 0.33059 0.32150 -0.02901 0.00547  0.01502  208 GLU   A O   
1002 C  CB  . GLU   A 131 ? 0.48472 0.44349 0.42741 -0.02679 0.00940  0.01608  208 GLU   A CB  
1003 C  CG  . GLU   A 131 ? 0.43458 0.40050 0.38218 -0.02370 0.01214  0.01533  208 GLU   A CG  
1004 C  CD  . GLU   A 131 ? 0.51477 0.49088 0.46766 -0.02565 0.01370  0.01782  208 GLU   A CD  
1005 O  OE1 . GLU   A 131 ? 0.55631 0.53383 0.50772 -0.03024 0.01248  0.02074  208 GLU   A OE1 
1006 O  OE2 . GLU   A 131 ? 0.58115 0.56385 0.53963 -0.02260 0.01620  0.01712  208 GLU   A OE2 
1007 N  N   . LYS   A 132 ? 0.42877 0.38322 0.36631 -0.03647 0.00456  0.02008  209 LYS   A N   
1008 C  CA  . LYS   A 132 ? 0.46660 0.41121 0.39565 -0.04088 0.00178  0.02103  209 LYS   A CA  
1009 C  C   . LYS   A 132 ? 0.48277 0.41502 0.40390 -0.03882 0.00148  0.01901  209 LYS   A C   
1010 O  O   . LYS   A 132 ? 0.50171 0.42359 0.41574 -0.03989 0.00005  0.01838  209 LYS   A O   
1011 C  CB  . LYS   A 132 ? 0.48668 0.43466 0.41418 -0.04723 0.00022  0.02486  209 LYS   A CB  
1012 C  CG  . LYS   A 132 ? 0.44652 0.40606 0.38121 -0.05010 -0.00003 0.02781  209 LYS   A CG  
1013 C  CD  . LYS   A 132 ? 0.52193 0.48065 0.45210 -0.05778 -0.00299 0.03176  209 LYS   A CD  
1014 C  CE  . LYS   A 132 ? 0.64753 0.62102 0.58628 -0.06034 -0.00234 0.03590  209 LYS   A CE  
1015 N  NZ  . LYS   A 132 ? 0.57585 0.55895 0.52392 -0.05717 -0.00080 0.03587  209 LYS   A NZ  
1016 N  N   . ASP   A 133 ? 0.46533 0.39825 0.38730 -0.03579 0.00291  0.01815  210 ASP   A N   
1017 C  CA  . ASP   A 133 ? 0.47669 0.39908 0.39212 -0.03353 0.00270  0.01682  210 ASP   A CA  
1018 C  C   . ASP   A 133 ? 0.47840 0.39482 0.39308 -0.02888 0.00328  0.01424  210 ASP   A C   
1019 O  O   . ASP   A 133 ? 0.49471 0.40194 0.40392 -0.02674 0.00321  0.01351  210 ASP   A O   
1020 C  CB  . ASP   A 133 ? 0.53036 0.45633 0.44803 -0.03110 0.00407  0.01659  210 ASP   A CB  
1021 C  CG  . ASP   A 133 ? 0.61406 0.54435 0.53109 -0.03549 0.00371  0.01918  210 ASP   A CG  
1022 O  OD1 . ASP   A 133 ? 0.64217 0.56613 0.55247 -0.03990 0.00181  0.02098  210 ASP   A OD1 
1023 O  OD2 . ASP   A 133 ? 0.68686 0.62649 0.60972 -0.03453 0.00547  0.01945  210 ASP   A OD2 
1024 N  N   . ILE   A 134 ? 0.44158 0.36318 0.36182 -0.02703 0.00401  0.01307  211 ILE   A N   
1025 C  CA  . ILE   A 134 ? 0.47264 0.38892 0.39227 -0.02270 0.00466  0.01080  211 ILE   A CA  
1026 C  C   . ILE   A 134 ? 0.47501 0.37814 0.38505 -0.02408 0.00351  0.01082  211 ILE   A C   
1027 O  O   . ILE   A 134 ? 0.51110 0.40785 0.41908 -0.02012 0.00438  0.00922  211 ILE   A O   
1028 C  CB  . ILE   A 134 ? 0.44013 0.36362 0.36651 -0.02143 0.00532  0.00983  211 ILE   A CB  
1029 C  CG1 . ILE   A 134 ? 0.42870 0.34819 0.35557 -0.01646 0.00633  0.00747  211 ILE   A CG1 
1030 C  CG2 . ILE   A 134 ? 0.39816 0.32144 0.32258 -0.02645 0.00364  0.01136  211 ILE   A CG2 
1031 C  CD1 . ILE   A 134 ? 0.42353 0.34733 0.35545 -0.01160 0.00788  0.00616  211 ILE   A CD1 
1032 N  N   . LYS   A 135 ? 0.46037 0.35893 0.36408 -0.02967 0.00169  0.01273  212 LYS   A N   
1033 C  CA  . LYS   A 135 ? 0.50537 0.38983 0.39836 -0.03137 0.00068  0.01272  212 LYS   A CA  
1034 C  C   . LYS   A 135 ? 0.53414 0.40920 0.42133 -0.02839 0.00139  0.01242  212 LYS   A C   
1035 O  O   . LYS   A 135 ? 0.52087 0.38360 0.40000 -0.02720 0.00165  0.01177  212 LYS   A O   
1036 C  CB  . LYS   A 135 ? 0.50963 0.39169 0.39695 -0.03884 -0.00178 0.01511  212 LYS   A CB  
1037 C  CG  . LYS   A 135 ? 0.51192 0.39922 0.40036 -0.04215 -0.00256 0.01736  212 LYS   A CG  
1038 C  CD  . LYS   A 135 ? 0.59346 0.48091 0.47809 -0.04981 -0.00514 0.02012  212 LYS   A CD  
1039 C  CE  . LYS   A 135 ? 0.60170 0.48744 0.48203 -0.05379 -0.00630 0.02242  212 LYS   A CE  
1040 N  NZ  . LYS   A 135 ? 0.61993 0.50375 0.49475 -0.06192 -0.00925 0.02540  212 LYS   A NZ  
1041 N  N   . ASN   A 136 ? 0.47360 0.35396 0.36448 -0.02706 0.00184  0.01303  213 ASN   A N   
1042 C  CA  . ASN   A 136 ? 0.47889 0.35196 0.36594 -0.02344 0.00257  0.01295  213 ASN   A CA  
1043 C  C   . ASN   A 136 ? 0.50611 0.37580 0.39455 -0.01715 0.00434  0.01120  213 ASN   A C   
1044 O  O   . ASN   A 136 ? 0.53976 0.40033 0.42306 -0.01412 0.00503  0.01143  213 ASN   A O   
1045 C  CB  . ASN   A 136 ? 0.50280 0.38402 0.39507 -0.02266 0.00282  0.01371  213 ASN   A CB  
1046 C  CG  . ASN   A 136 ? 0.52502 0.40864 0.41518 -0.02846 0.00138  0.01577  213 ASN   A CG  
1047 O  OD1 . ASN   A 136 ? 0.54070 0.41815 0.42422 -0.03321 -0.00014 0.01695  213 ASN   A OD1 
1048 N  ND2 . ASN   A 136 ? 0.53690 0.42926 0.43224 -0.02836 0.00183  0.01637  213 ASN   A ND2 
1049 N  N   . LEU   A 137 ? 0.50639 0.38368 0.40206 -0.01488 0.00522  0.00973  214 LEU   A N   
1050 C  CA  . LEU   A 137 ? 0.48796 0.36403 0.38631 -0.00885 0.00694  0.00833  214 LEU   A CA  
1051 C  C   . LEU   A 137 ? 0.52362 0.39083 0.41649 -0.00838 0.00748  0.00736  214 LEU   A C   
1052 O  O   . LEU   A 137 ? 0.48741 0.35823 0.38469 -0.00603 0.00839  0.00597  214 LEU   A O   
1053 C  CB  . LEU   A 137 ? 0.50693 0.39563 0.41571 -0.00650 0.00763  0.00729  214 LEU   A CB  
1054 C  CG  . LEU   A 137 ? 0.46684 0.36423 0.38069 -0.00689 0.00742  0.00798  214 LEU   A CG  
1055 C  CD1 . LEU   A 137 ? 0.44808 0.35577 0.37062 -0.00455 0.00831  0.00669  214 LEU   A CD1 
1056 C  CD2 . LEU   A 137 ? 0.44222 0.33543 0.35366 -0.00438 0.00750  0.00903  214 LEU   A CD2 
1057 N  N   . SER   A 138 ? 0.52586 0.38054 0.40821 -0.01079 0.00697  0.00809  215 SER   A N   
1058 C  CA  . SER   A 138 ? 0.53464 0.37938 0.40964 -0.01162 0.00731  0.00723  215 SER   A CA  
1059 C  C   . SER   A 138 ? 0.54680 0.38623 0.42141 -0.00507 0.00991  0.00609  215 SER   A C   
1060 O  O   . SER   A 138 ? 0.53233 0.36460 0.40188 -0.00498 0.01069  0.00505  215 SER   A O   
1061 C  CB  . SER   A 138 ? 0.55782 0.38942 0.42038 -0.01635 0.00605  0.00837  215 SER   A CB  
1062 O  OG  . SER   A 138 ? 0.53739 0.36254 0.39580 -0.01427 0.00659  0.00948  215 SER   A OG  
1063 N  N   . LYS   A 139 ? 0.52619 0.36931 0.40610 0.00024  0.01124  0.00650  216 LYS   A N   
1064 C  CA  . LYS   A 139 ? 0.55018 0.39037 0.43136 0.00670  0.01377  0.00600  216 LYS   A CA  
1065 C  C   . LYS   A 139 ? 0.51311 0.36500 0.40464 0.00920  0.01431  0.00475  216 LYS   A C   
1066 O  O   . LYS   A 139 ? 0.51672 0.36754 0.41019 0.01435  0.01638  0.00445  216 LYS   A O   
1067 C  CB  . LYS   A 139 ? 0.48521 0.32324 0.36674 0.01122  0.01481  0.00773  216 LYS   A CB  
1068 C  CG  . LYS   A 139 ? 0.53675 0.36057 0.40695 0.01037  0.01506  0.00897  216 LYS   A CG  
1069 C  CD  . LYS   A 139 ? 0.54645 0.36746 0.41732 0.01623  0.01670  0.01091  216 LYS   A CD  
1070 C  CE  . LYS   A 139 ? 0.69012 0.49540 0.54887 0.01601  0.01740  0.01211  216 LYS   A CE  
1071 N  NZ  . LYS   A 139 ? 0.74094 0.54456 0.59491 0.00942  0.01464  0.01263  216 LYS   A NZ  
1072 N  N   . LEU   A 140 ? 0.45068 0.31348 0.34876 0.00587  0.01270  0.00419  217 LEU   A N   
1073 C  CA  . LEU   A 140 ? 0.46732 0.34048 0.37467 0.00826  0.01324  0.00303  217 LEU   A CA  
1074 C  C   . LEU   A 140 ? 0.48092 0.34921 0.38573 0.00944  0.01442  0.00173  217 LEU   A C   
1075 O  O   . LEU   A 140 ? 0.52747 0.38956 0.42581 0.00555  0.01370  0.00134  217 LEU   A O   
1076 C  CB  . LEU   A 140 ? 0.50869 0.39276 0.42215 0.00438  0.01165  0.00270  217 LEU   A CB  
1077 C  CG  . LEU   A 140 ? 0.50024 0.39291 0.41900 0.00363  0.01088  0.00348  217 LEU   A CG  
1078 C  CD1 . LEU   A 140 ? 0.49382 0.39354 0.41538 -0.00096 0.00972  0.00342  217 LEU   A CD1 
1079 C  CD2 . LEU   A 140 ? 0.50643 0.40672 0.43294 0.00805  0.01176  0.00302  217 LEU   A CD2 
1080 N  N   . SER   A 141 ? 0.45958 0.33067 0.36922 0.01452  0.01614  0.00126  218 SER   A N   
1081 C  CA  . SER   A 141 ? 0.46439 0.33314 0.37324 0.01569  0.01731  -0.00009 218 SER   A CA  
1082 C  C   . SER   A 141 ? 0.51808 0.39878 0.43674 0.01657  0.01704  -0.00110 218 SER   A C   
1083 O  O   . SER   A 141 ? 0.49697 0.37759 0.41564 0.01594  0.01730  -0.00229 218 SER   A O   
1084 C  CB  . SER   A 141 ? 0.50375 0.36393 0.40864 0.02113  0.02008  0.00033  218 SER   A CB  
1085 O  OG  . SER   A 141 ? 0.54338 0.41038 0.45570 0.02589  0.02094  0.00149  218 SER   A OG  
1086 N  N   . MET   A 142 ? 0.48431 0.37457 0.41060 0.01778  0.01649  -0.00062 219 MET   A N   
1087 C  CA  . MET   A 142 ? 0.44724 0.34839 0.38219 0.01822  0.01612  -0.00155 219 MET   A CA  
1088 C  C   . MET   A 142 ? 0.43910 0.34772 0.37767 0.01514  0.01457  -0.00127 219 MET   A C   
1089 O  O   . MET   A 142 ? 0.47285 0.38288 0.41218 0.01583  0.01428  -0.00022 219 MET   A O   
1090 C  CB  . MET   A 142 ? 0.46449 0.36938 0.40475 0.02327  0.01734  -0.00116 219 MET   A CB  
1091 C  CG  . MET   A 142 ? 0.52015 0.43622 0.46874 0.02339  0.01649  -0.00152 219 MET   A CG  
1092 S  SD  . MET   A 142 ? 0.50880 0.43107 0.46226 0.02240  0.01639  -0.00344 219 MET   A SD  
1093 C  CE  . MET   A 142 ? 0.46118 0.38008 0.41477 0.02689  0.01825  -0.00348 219 MET   A CE  
1094 N  N   . LEU   A 143 ? 0.40109 0.31439 0.34173 0.01178  0.01370  -0.00197 220 LEU   A N   
1095 C  CA  . LEU   A 143 ? 0.42583 0.34697 0.37055 0.00939  0.01282  -0.00166 220 LEU   A CA  
1096 C  C   . LEU   A 143 ? 0.41743 0.34715 0.36923 0.01012  0.01310  -0.00277 220 LEU   A C   
1097 O  O   . LEU   A 143 ? 0.43282 0.36290 0.38514 0.00908  0.01301  -0.00337 220 LEU   A O   
1098 C  CB  . LEU   A 143 ? 0.40034 0.31930 0.34078 0.00445  0.01164  -0.00072 220 LEU   A CB  
1099 C  CG  . LEU   A 143 ? 0.47555 0.40293 0.42016 0.00166  0.01109  -0.00007 220 LEU   A CG  
1100 C  CD1 . LEU   A 143 ? 0.43786 0.36782 0.38370 0.00271  0.01133  0.00047  220 LEU   A CD1 
1101 C  CD2 . LEU   A 143 ? 0.40414 0.32993 0.34502 -0.00347 0.00980  0.00129  220 LEU   A CD2 
1102 N  N   . SER   A 144 ? 0.41188 0.34788 0.36857 0.01181  0.01339  -0.00298 221 SER   A N   
1103 C  CA  . SER   A 144 ? 0.40160 0.34490 0.36430 0.01257  0.01379  -0.00405 221 SER   A CA  
1104 C  C   . SER   A 144 ? 0.39621 0.34559 0.36151 0.01101  0.01388  -0.00381 221 SER   A C   
1105 O  O   . SER   A 144 ? 0.42817 0.37841 0.39333 0.01170  0.01391  -0.00348 221 SER   A O   
1106 C  CB  . SER   A 144 ? 0.42647 0.37112 0.39223 0.01630  0.01430  -0.00469 221 SER   A CB  
1107 O  OG  . SER   A 144 ? 0.43452 0.38552 0.40534 0.01678  0.01461  -0.00573 221 SER   A OG  
1108 N  N   . ILE   A 145 ? 0.39094 0.34462 0.35860 0.00902  0.01405  -0.00378 222 ILE   A N   
1109 C  CA  . ILE   A 145 ? 0.39277 0.35238 0.36304 0.00794  0.01476  -0.00340 222 ILE   A CA  
1110 C  C   . ILE   A 145 ? 0.39394 0.35933 0.36940 0.00902  0.01571  -0.00422 222 ILE   A C   
1111 O  O   . ILE   A 145 ? 0.38848 0.35892 0.36645 0.00789  0.01659  -0.00353 222 ILE   A O   
1112 C  CB  . ILE   A 145 ? 0.41515 0.37506 0.38336 0.00424  0.01431  -0.00169 222 ILE   A CB  
1113 C  CG1 . ILE   A 145 ? 0.41036 0.36891 0.37791 0.00213  0.01338  -0.00109 222 ILE   A CG1 
1114 C  CG2 . ILE   A 145 ? 0.44934 0.40386 0.41231 0.00316  0.01355  -0.00085 222 ILE   A CG2 
1115 C  CD1 . ILE   A 145 ? 0.46149 0.41908 0.42595 -0.00209 0.01236  0.00093  222 ILE   A CD1 
1116 N  N   . ARG   A 146 ? 0.39215 0.35691 0.36930 0.01134  0.01571  -0.00547 223 ARG   A N   
1117 C  CA  . ARG   A 146 ? 0.37978 0.34937 0.36146 0.01228  0.01652  -0.00616 223 ARG   A CA  
1118 C  C   . ARG   A 146 ? 0.38781 0.36108 0.37131 0.01347  0.01786  -0.00671 223 ARG   A C   
1119 O  O   . ARG   A 146 ? 0.41385 0.38554 0.39513 0.01388  0.01784  -0.00687 223 ARG   A O   
1120 C  CB  . ARG   A 146 ? 0.43921 0.40703 0.42192 0.01429  0.01616  -0.00729 223 ARG   A CB  
1121 C  CG  . ARG   A 146 ? 0.47403 0.44182 0.45759 0.01687  0.01639  -0.00834 223 ARG   A CG  
1122 C  CD  . ARG   A 146 ? 0.51948 0.49071 0.50691 0.01835  0.01697  -0.00943 223 ARG   A CD  
1123 N  NE  . ARG   A 146 ? 0.56415 0.53370 0.55229 0.01928  0.01647  -0.00986 223 ARG   A NE  
1124 C  CZ  . ARG   A 146 ? 0.53602 0.50739 0.52693 0.02079  0.01667  -0.01078 223 ARG   A CZ  
1125 N  NH1 . ARG   A 146 ? 0.53131 0.50567 0.52421 0.02158  0.01730  -0.01145 223 ARG   A NH1 
1126 N  NH2 . ARG   A 146 ? 0.51272 0.48226 0.50378 0.02145  0.01630  -0.01103 223 ARG   A NH2 
1127 N  N   . GLU   A 147 ? 0.41663 0.39444 0.40376 0.01398  0.01908  -0.00685 224 GLU   A N   
1128 C  CA  . GLU   A 147 ? 0.41525 0.39567 0.40335 0.01526  0.02085  -0.00748 224 GLU   A CA  
1129 C  C   . GLU   A 147 ? 0.41176 0.39246 0.39737 0.01390  0.02164  -0.00657 224 GLU   A C   
1130 O  O   . GLU   A 147 ? 0.38675 0.36560 0.36963 0.01436  0.02193  -0.00725 224 GLU   A O   
1131 C  CB  . GLU   A 147 ? 0.41517 0.39348 0.40253 0.01726  0.02060  -0.00913 224 GLU   A CB  
1132 C  CG  . GLU   A 147 ? 0.45880 0.43766 0.44904 0.01871  0.02025  -0.01001 224 GLU   A CG  
1133 C  CD  . GLU   A 147 ? 0.53222 0.50911 0.52170 0.02019  0.01956  -0.01120 224 GLU   A CD  
1134 O  OE1 . GLU   A 147 ? 0.59532 0.57217 0.58349 0.02062  0.02032  -0.01188 224 GLU   A OE1 
1135 O  OE2 . GLU   A 147 ? 0.53760 0.51288 0.52750 0.02080  0.01832  -0.01129 224 GLU   A OE2 
1136 N  N   . ASN   A 148 ? 0.34902 0.33219 0.33546 0.01187  0.02183  -0.00478 225 ASN   A N   
1137 C  CA  . ASN   A 148 ? 0.36765 0.35260 0.35274 0.01058  0.02310  -0.00358 225 ASN   A CA  
1138 C  C   . ASN   A 148 ? 0.40749 0.39865 0.39676 0.01006  0.02476  -0.00174 225 ASN   A C   
1139 O  O   . ASN   A 148 ? 0.40995 0.40401 0.40305 0.01166  0.02562  -0.00192 225 ASN   A O   
1140 C  CB  . ASN   A 148 ? 0.37952 0.36093 0.36070 0.00817  0.02135  -0.00261 225 ASN   A CB  
1141 C  CG  . ASN   A 148 ? 0.40628 0.38270 0.38360 0.00908  0.02040  -0.00383 225 ASN   A CG  
1142 O  OD1 . ASN   A 148 ? 0.40044 0.37665 0.37562 0.00914  0.02127  -0.00400 225 ASN   A OD1 
1143 N  ND2 . ASN   A 148 ? 0.33434 0.30689 0.31078 0.00983  0.01871  -0.00444 225 ASN   A ND2 
1144 N  N   . LYS   A 149 ? 0.42156 0.41523 0.41044 0.00792  0.02530  0.00032  226 LYS   A N   
1145 C  CA  . LYS   A 149 ? 0.43055 0.43123 0.42403 0.00752  0.02709  0.00273  226 LYS   A CA  
1146 C  C   . LYS   A 149 ? 0.43794 0.44061 0.43157 0.00361  0.02534  0.00554  226 LYS   A C   
1147 O  O   . LYS   A 149 ? 0.45756 0.46534 0.45295 0.00225  0.02671  0.00807  226 LYS   A O   
1148 C  CB  . LYS   A 149 ? 0.46502 0.46824 0.45842 0.00917  0.03054  0.00294  226 LYS   A CB  
1149 C  CG  . LYS   A 149 ? 0.45561 0.45752 0.44920 0.01284  0.03267  0.00067  226 LYS   A CG  
1150 C  CD  . LYS   A 149 ? 0.52449 0.52458 0.51414 0.01395  0.03536  -0.00018 226 LYS   A CD  
1151 C  CE  . LYS   A 149 ? 0.65051 0.64813 0.63913 0.01718  0.03741  -0.00244 226 LYS   A CE  
1152 N  NZ  . LYS   A 149 ? 0.68814 0.68504 0.67342 0.01845  0.04111  -0.00259 226 LYS   A NZ  
1153 N  N   . ILE   A 150 ? 0.39974 0.39817 0.39117 0.00164  0.02237  0.00529  227 ILE   A N   
1154 C  CA  . ILE   A 150 ? 0.37576 0.37429 0.36571 -0.00265 0.02029  0.00781  227 ILE   A CA  
1155 C  C   . ILE   A 150 ? 0.39099 0.39637 0.38634 -0.00410 0.02008  0.01051  227 ILE   A C   
1156 O  O   . ILE   A 150 ? 0.36124 0.36709 0.35912 -0.00276 0.01964  0.00978  227 ILE   A O   
1157 C  CB  . ILE   A 150 ? 0.40293 0.39295 0.38727 -0.00406 0.01752  0.00647  227 ILE   A CB  
1158 C  CG1 . ILE   A 150 ? 0.41780 0.40213 0.39707 -0.00338 0.01754  0.00503  227 ILE   A CG1 
1159 C  CG2 . ILE   A 150 ? 0.38772 0.37697 0.37000 -0.00876 0.01520  0.00899  227 ILE   A CG2 
1160 C  CD1 . ILE   A 150 ? 0.38034 0.35808 0.35690 -0.00088 0.01674  0.00243  227 ILE   A CD1 
1161 N  N   . LYS   A 151 ? 0.41370 0.42487 0.41105 -0.00696 0.02030  0.01397  228 LYS   A N   
1162 C  CA  . LYS   A 151 ? 0.40334 0.42183 0.40602 -0.00909 0.01961  0.01746  228 LYS   A CA  
1163 C  C   . LYS   A 151 ? 0.43553 0.45105 0.43463 -0.01456 0.01581  0.01936  228 LYS   A C   
1164 O  O   . LYS   A 151 ? 0.38662 0.40633 0.38901 -0.01673 0.01429  0.02180  228 LYS   A O   
1165 C  CB  . LYS   A 151 ? 0.39884 0.42687 0.40684 -0.00892 0.02233  0.02088  228 LYS   A CB  
1166 C  CG  . LYS   A 151 ? 0.47753 0.50864 0.48924 -0.00341 0.02644  0.01941  228 LYS   A CG  
1167 C  CD  . LYS   A 151 ? 0.48633 0.52386 0.50060 -0.00257 0.02989  0.02182  228 LYS   A CD  
1168 C  CE  . LYS   A 151 ? 0.57746 0.61494 0.59281 0.00300  0.03415  0.01956  228 LYS   A CE  
1169 N  NZ  . LYS   A 151 ? 0.49888 0.52678 0.50783 0.00483  0.03373  0.01475  228 LYS   A NZ  
1170 N  N   . GLN   A 152 ? 0.41916 0.42691 0.41107 -0.01688 0.01416  0.01833  229 GLN   A N   
1171 C  CA  . GLN   A 152 ? 0.37891 0.38257 0.36591 -0.02244 0.01075  0.02023  229 GLN   A CA  
1172 C  C   . GLN   A 152 ? 0.38685 0.37880 0.36508 -0.02277 0.00948  0.01749  229 GLN   A C   
1173 O  O   . GLN   A 152 ? 0.42009 0.40962 0.39653 -0.02037 0.01099  0.01576  229 GLN   A O   
1174 C  CB  . GLN   A 152 ? 0.41064 0.42130 0.39961 -0.02671 0.01036  0.02468  229 GLN   A CB  
1175 C  CG  . GLN   A 152 ? 0.44453 0.45117 0.42799 -0.03334 0.00656  0.02717  229 GLN   A CG  
1176 C  CD  . GLN   A 152 ? 0.52179 0.53861 0.50988 -0.03771 0.00597  0.03256  229 GLN   A CD  
1177 O  OE1 . GLN   A 152 ? 0.55975 0.58660 0.55531 -0.03524 0.00885  0.03439  229 GLN   A OE1 
1178 N  NE2 . GLN   A 152 ? 0.59127 0.60549 0.57477 -0.04429 0.00232  0.03535  229 GLN   A NE2 
1179 N  N   . LEU   A 153 ? 0.41444 0.39886 0.38701 -0.02558 0.00684  0.01718  230 LEU   A N   
1180 C  CA  . LEU   A 153 ? 0.41711 0.38991 0.38059 -0.02663 0.00553  0.01549  230 LEU   A CA  
1181 C  C   . LEU   A 153 ? 0.39906 0.36971 0.35750 -0.03290 0.00314  0.01856  230 LEU   A C   
1182 O  O   . LEU   A 153 ? 0.42487 0.39936 0.38458 -0.03717 0.00128  0.02143  230 LEU   A O   
1183 C  CB  . LEU   A 153 ? 0.40883 0.37322 0.36805 -0.02543 0.00460  0.01308  230 LEU   A CB  
1184 C  CG  . LEU   A 153 ? 0.47142 0.43690 0.43478 -0.01932 0.00679  0.00997  230 LEU   A CG  
1185 C  CD1 . LEU   A 153 ? 0.38835 0.34462 0.34675 -0.01768 0.00626  0.00753  230 LEU   A CD1 
1186 C  CD2 . LEU   A 153 ? 0.43137 0.39759 0.39555 -0.01614 0.00870  0.00876  230 LEU   A CD2 
1187 N  N   . PRO   A 154 ? 0.44186 0.40679 0.39464 -0.03392 0.00295  0.01838  231 PRO   A N   
1188 C  CA  . PRO   A 154 ? 0.44980 0.41226 0.39721 -0.04030 0.00054  0.02144  231 PRO   A CA  
1189 C  C   . PRO   A 154 ? 0.42831 0.37961 0.36681 -0.04381 -0.00213 0.02111  231 PRO   A C   
1190 O  O   . PRO   A 154 ? 0.45255 0.39593 0.38751 -0.04065 -0.00168 0.01810  231 PRO   A O   
1191 C  CB  . PRO   A 154 ? 0.46038 0.41876 0.40396 -0.03938 0.00141  0.02073  231 PRO   A CB  
1192 C  CG  . PRO   A 154 ? 0.44251 0.39497 0.38504 -0.03332 0.00311  0.01674  231 PRO   A CG  
1193 C  CD  . PRO   A 154 ? 0.44953 0.40973 0.40025 -0.02956 0.00469  0.01561  231 PRO   A CD  
1194 N  N   . ALA   A 155 ? 0.44081 0.39135 0.37527 -0.05062 -0.00487 0.02445  232 ALA   A N   
1195 C  CA  . ALA   A 155 ? 0.51519 0.45304 0.43879 -0.05485 -0.00752 0.02427  232 ALA   A CA  
1196 C  C   . ALA   A 155 ? 0.50143 0.42526 0.41553 -0.05257 -0.00684 0.02138  232 ALA   A C   
1197 O  O   . ALA   A 155 ? 0.52295 0.43462 0.42820 -0.05325 -0.00769 0.01984  232 ALA   A O   
1198 C  CB  . ALA   A 155 ? 0.42675 0.36579 0.34675 -0.06326 -0.01084 0.02870  232 ALA   A CB  
1199 N  N   . GLU   A 156 ? 0.50887 0.43389 0.42439 -0.04974 -0.00518 0.02076  233 GLU   A N   
1200 C  CA  . GLU   A 156 ? 0.51289 0.42523 0.41999 -0.04738 -0.00455 0.01854  233 GLU   A CA  
1201 C  C   . GLU   A 156 ? 0.51463 0.42137 0.42137 -0.04121 -0.00268 0.01500  233 GLU   A C   
1202 O  O   . GLU   A 156 ? 0.52057 0.41614 0.42013 -0.03888 -0.00202 0.01340  233 GLU   A O   
1203 C  CB  . GLU   A 156 ? 0.51265 0.42881 0.42233 -0.04559 -0.00326 0.01887  233 GLU   A CB  
1204 C  CG  . GLU   A 156 ? 0.52218 0.43832 0.42786 -0.05186 -0.00519 0.02213  233 GLU   A CG  
1205 C  CD  . GLU   A 156 ? 0.50867 0.43723 0.42098 -0.05653 -0.00636 0.02565  233 GLU   A CD  
1206 O  OE1 . GLU   A 156 ? 0.53811 0.47533 0.45832 -0.05462 -0.00554 0.02553  233 GLU   A OE1 
1207 O  OE2 . GLU   A 156 ? 0.61872 0.54857 0.52845 -0.06217 -0.00810 0.02884  233 GLU   A OE2 
1208 N  N   . ILE   A 157 ? 0.46321 0.37750 0.37755 -0.03846 -0.00173 0.01402  234 ILE   A N   
1209 C  CA  . ILE   A 157 ? 0.48906 0.39888 0.40352 -0.03288 -0.00002 0.01094  234 ILE   A CA  
1210 C  C   . ILE   A 157 ? 0.48953 0.38544 0.39321 -0.03462 -0.00097 0.01016  234 ILE   A C   
1211 O  O   . ILE   A 157 ? 0.48316 0.37091 0.38313 -0.03016 0.00066  0.00793  234 ILE   A O   
1212 C  CB  . ILE   A 157 ? 0.48837 0.40920 0.41287 -0.03031 0.00094  0.01034  234 ILE   A CB  
1213 C  CG1 . ILE   A 157 ? 0.50111 0.42178 0.42915 -0.02344 0.00332  0.00740  234 ILE   A CG1 
1214 C  CG2 . ILE   A 157 ? 0.50271 0.42217 0.42538 -0.03360 -0.00070 0.01097  234 ILE   A CG2 
1215 C  CD1 . ILE   A 157 ? 0.47213 0.40152 0.40753 -0.02014 0.00496  0.00712  234 ILE   A CD1 
1216 N  N   . GLY   A 158 ? 0.50745 0.40007 0.40543 -0.04123 -0.00354 0.01223  235 GLY   A N   
1217 C  CA  . GLY   A 158 ? 0.52742 0.40544 0.41330 -0.04386 -0.00459 0.01165  235 GLY   A CA  
1218 C  C   . GLY   A 158 ? 0.57538 0.43917 0.45044 -0.04320 -0.00400 0.01092  235 GLY   A C   
1219 O  O   . GLY   A 158 ? 0.56461 0.41452 0.42823 -0.04509 -0.00446 0.01032  235 GLY   A O   
1220 N  N   . GLU   A 159 ? 0.57963 0.44581 0.45733 -0.04061 -0.00294 0.01104  236 GLU   A N   
1221 C  CA  . GLU   A 159 ? 0.62100 0.47414 0.48932 -0.03906 -0.00212 0.01048  236 GLU   A CA  
1222 C  C   . GLU   A 159 ? 0.62075 0.47127 0.49130 -0.03093 0.00098  0.00810  236 GLU   A C   
1223 O  O   . GLU   A 159 ? 0.64660 0.48748 0.51085 -0.02849 0.00207  0.00786  236 GLU   A O   
1224 C  CB  . GLU   A 159 ? 0.58345 0.43964 0.45203 -0.04182 -0.00318 0.01253  236 GLU   A CB  
1225 C  CG  . GLU   A 159 ? 0.64063 0.49646 0.50441 -0.05040 -0.00640 0.01535  236 GLU   A CG  
1226 C  CD  . GLU   A 159 ? 0.76321 0.61887 0.62451 -0.05362 -0.00749 0.01746  236 GLU   A CD  
1227 O  OE1 . GLU   A 159 ? 0.79394 0.63762 0.64665 -0.05238 -0.00695 0.01693  236 GLU   A OE1 
1228 O  OE2 . GLU   A 159 ? 0.75072 0.61837 0.61877 -0.05727 -0.00875 0.01984  236 GLU   A OE2 
1229 N  N   . LEU   A 160 ? 0.58217 0.44104 0.46151 -0.02679 0.00236  0.00663  237 LEU   A N   
1230 C  CA  . LEU   A 160 ? 0.55351 0.41075 0.43544 -0.01945 0.00510  0.00474  237 LEU   A CA  
1231 C  C   . LEU   A 160 ? 0.55545 0.40226 0.43048 -0.01805 0.00620  0.00330  237 LEU   A C   
1232 O  O   . LEU   A 160 ? 0.51848 0.36977 0.39876 -0.01507 0.00731  0.00196  237 LEU   A O   
1233 C  CB  . LEU   A 160 ? 0.49890 0.37090 0.39386 -0.01594 0.00595  0.00407  237 LEU   A CB  
1234 C  CG  . LEU   A 160 ? 0.50876 0.39196 0.41064 -0.01790 0.00503  0.00544  237 LEU   A CG  
1235 C  CD1 . LEU   A 160 ? 0.42831 0.32433 0.34159 -0.01450 0.00611  0.00453  237 LEU   A CD1 
1236 C  CD2 . LEU   A 160 ? 0.50040 0.37952 0.39901 -0.01695 0.00527  0.00624  237 LEU   A CD2 
1237 N  N   . CYS   A 161 ? 0.51505 0.34697 0.37742 -0.02026 0.00604  0.00358  238 CYS   A N   
1238 C  CA  . CYS   A 161 ? 0.58307 0.40361 0.43701 -0.01978 0.00712  0.00228  238 CYS   A CA  
1239 C  C   . CYS   A 161 ? 0.56956 0.38750 0.42550 -0.01176 0.01068  0.00070  238 CYS   A C   
1240 O  O   . CYS   A 161 ? 0.58033 0.39021 0.43055 -0.01057 0.01211  -0.00051 238 CYS   A O   
1241 C  CB  . CYS   A 161 ? 0.66369 0.46729 0.50203 -0.02426 0.00625  0.00295  238 CYS   A CB  
1242 S  SG  . CYS   A 161 ? 0.79615 0.59508 0.63035 -0.02487 0.00581  0.00460  238 CYS   A SG  
1243 N  N   . ASN   A 162 ? 0.52046 0.34516 0.38425 -0.00646 0.01212  0.00089  239 ASN   A N   
1244 C  CA  . ASN   A 162 ? 0.51566 0.34042 0.38316 0.00089  0.01521  -0.00004 239 ASN   A CA  
1245 C  C   . ASN   A 162 ? 0.52375 0.36339 0.40419 0.00330  0.01530  -0.00082 239 ASN   A C   
1246 O  O   . ASN   A 162 ? 0.48755 0.32917 0.37240 0.00911  0.01757  -0.00130 239 ASN   A O   
1247 C  CB  . ASN   A 162 ? 0.51634 0.33817 0.38368 0.00553  0.01679  0.00107  239 ASN   A CB  
1248 C  CG  . ASN   A 162 ? 0.59735 0.40402 0.45174 0.00344  0.01682  0.00193  239 ASN   A CG  
1249 O  OD1 . ASN   A 162 ? 0.61477 0.40768 0.45862 0.00402  0.01849  0.00133  239 ASN   A OD1 
1250 N  ND2 . ASN   A 162 ? 0.61007 0.41855 0.46448 0.00082  0.01505  0.00332  239 ASN   A ND2 
1251 N  N   . LEU   A 163 ? 0.53473 0.38470 0.42121 -0.00094 0.01299  -0.00075 240 LEU   A N   
1252 C  CA  . LEU   A 163 ? 0.49410 0.35712 0.39196 0.00121  0.01314  -0.00152 240 LEU   A CA  
1253 C  C   . LEU   A 163 ? 0.51040 0.37055 0.40768 0.00402  0.01480  -0.00292 240 LEU   A C   
1254 O  O   . LEU   A 163 ? 0.50146 0.35394 0.39138 0.00104  0.01442  -0.00337 240 LEU   A O   
1255 C  CB  . LEU   A 163 ? 0.46988 0.34238 0.37257 -0.00400 0.01070  -0.00099 240 LEU   A CB  
1256 C  CG  . LEU   A 163 ? 0.47286 0.35707 0.38412 -0.00419 0.00997  -0.00021 240 LEU   A CG  
1257 C  CD1 . LEU   A 163 ? 0.47734 0.37157 0.39482 -0.00755 0.00856  0.00009  240 LEU   A CD1 
1258 C  CD2 . LEU   A 163 ? 0.47281 0.36232 0.39092 0.00168  0.01169  -0.00092 240 LEU   A CD2 
1259 N  N   . ILE   A 164 ? 0.48215 0.34859 0.38701 0.00942  0.01650  -0.00345 241 ILE   A N   
1260 C  CA  . ILE   A 164 ? 0.49522 0.36135 0.40146 0.01238  0.01813  -0.00463 241 ILE   A CA  
1261 C  C   . ILE   A 164 ? 0.48503 0.36426 0.40173 0.01225  0.01719  -0.00527 241 ILE   A C   
1262 O  O   . ILE   A 164 ? 0.47658 0.35641 0.39372 0.01165  0.01725  -0.00620 241 ILE   A O   
1263 C  CB  . ILE   A 164 ? 0.50823 0.37053 0.41445 0.01894  0.02109  -0.00434 241 ILE   A CB  
1264 C  CG1 . ILE   A 164 ? 0.51786 0.36683 0.41379 0.01982  0.02241  -0.00345 241 ILE   A CG1 
1265 C  CG2 . ILE   A 164 ? 0.47733 0.33872 0.38420 0.02171  0.02295  -0.00540 241 ILE   A CG2 
1266 C  CD1 . ILE   A 164 ? 0.50192 0.33726 0.38662 0.01908  0.02387  -0.00425 241 ILE   A CD1 
1267 N  N   . THR   A 165 ? 0.46384 0.35300 0.38847 0.01292  0.01645  -0.00479 242 THR   A N   
1268 C  CA  . THR   A 165 ? 0.48205 0.38294 0.41614 0.01322  0.01585  -0.00537 242 THR   A CA  
1269 C  C   . THR   A 165 ? 0.45147 0.35950 0.38915 0.00983  0.01413  -0.00465 242 THR   A C   
1270 O  O   . THR   A 165 ? 0.44196 0.35149 0.38057 0.01050  0.01407  -0.00389 242 THR   A O   
1271 C  CB  . THR   A 165 ? 0.49057 0.39654 0.43099 0.01836  0.01724  -0.00550 242 THR   A CB  
1272 O  OG1 . THR   A 165 ? 0.51358 0.41305 0.45075 0.02183  0.01920  -0.00572 242 THR   A OG1 
1273 C  CG2 . THR   A 165 ? 0.46469 0.38112 0.41348 0.01842  0.01667  -0.00630 242 THR   A CG2 
1274 N  N   . LEU   A 166 ? 0.43197 0.34454 0.37171 0.00631  0.01287  -0.00465 243 LEU   A N   
1275 C  CA  . LEU   A 166 ? 0.41912 0.33990 0.36347 0.00356  0.01171  -0.00376 243 LEU   A CA  
1276 C  C   . LEU   A 166 ? 0.41886 0.34910 0.37147 0.00499  0.01202  -0.00448 243 LEU   A C   
1277 O  O   . LEU   A 166 ? 0.42172 0.35256 0.37507 0.00419  0.01171  -0.00486 243 LEU   A O   
1278 C  CB  . LEU   A 166 ? 0.41206 0.33040 0.35182 -0.00202 0.00996  -0.00239 243 LEU   A CB  
1279 C  CG  . LEU   A 166 ? 0.41005 0.33708 0.35448 -0.00508 0.00896  -0.00087 243 LEU   A CG  
1280 C  CD1 . LEU   A 166 ? 0.41750 0.34720 0.36402 -0.00313 0.00975  -0.00076 243 LEU   A CD1 
1281 C  CD2 . LEU   A 166 ? 0.40805 0.33117 0.34663 -0.01078 0.00705  0.00097  243 LEU   A CD2 
1282 N  N   . ASP   A 167 ? 0.43535 0.37225 0.39351 0.00706  0.01262  -0.00466 244 ASP   A N   
1283 C  CA  . ASP   A 167 ? 0.39647 0.34152 0.36181 0.00868  0.01313  -0.00542 244 ASP   A CA  
1284 C  C   . ASP   A 167 ? 0.38943 0.34153 0.35845 0.00686  0.01304  -0.00450 244 ASP   A C   
1285 O  O   . ASP   A 167 ? 0.39588 0.34900 0.36488 0.00735  0.01340  -0.00424 244 ASP   A O   
1286 C  CB  . ASP   A 167 ? 0.43241 0.37813 0.40016 0.01288  0.01413  -0.00643 244 ASP   A CB  
1287 C  CG  . ASP   A 167 ? 0.50459 0.45748 0.47869 0.01448  0.01461  -0.00731 244 ASP   A CG  
1288 O  OD1 . ASP   A 167 ? 0.48388 0.44127 0.46090 0.01290  0.01446  -0.00719 244 ASP   A OD1 
1289 O  OD2 . ASP   A 167 ? 0.55537 0.50932 0.53145 0.01730  0.01510  -0.00789 244 ASP   A OD2 
1290 N  N   . VAL   A 168 ? 0.34134 0.29838 0.31349 0.00482  0.01268  -0.00377 245 VAL   A N   
1291 C  CA  . VAL   A 168 ? 0.36846 0.33275 0.34469 0.00372  0.01317  -0.00263 245 VAL   A CA  
1292 C  C   . VAL   A 168 ? 0.38676 0.35774 0.36927 0.00546  0.01410  -0.00305 245 VAL   A C   
1293 O  O   . VAL   A 168 ? 0.38940 0.36665 0.37572 0.00432  0.01458  -0.00161 245 VAL   A O   
1294 C  CB  . VAL   A 168 ? 0.43501 0.39997 0.40936 -0.00078 0.01198  -0.00029 245 VAL   A CB  
1295 C  CG1 . VAL   A 168 ? 0.42296 0.37980 0.38998 -0.00272 0.01094  0.00007  245 VAL   A CG1 
1296 C  CG2 . VAL   A 168 ? 0.47441 0.44069 0.44981 -0.00297 0.01084  0.00066  245 VAL   A CG2 
1297 N  N   . ALA   A 169 ? 0.36899 0.33871 0.35264 0.00832  0.01448  -0.00480 246 ALA   A N   
1298 C  CA  . ALA   A 169 ? 0.38476 0.35983 0.37375 0.01021  0.01538  -0.00540 246 ALA   A CA  
1299 C  C   . ALA   A 169 ? 0.38133 0.36165 0.37342 0.01117  0.01695  -0.00512 246 ALA   A C   
1300 O  O   . ALA   A 169 ? 0.41398 0.39312 0.40399 0.01137  0.01742  -0.00528 246 ALA   A O   
1301 C  CB  . ALA   A 169 ? 0.39841 0.37097 0.38754 0.01321  0.01561  -0.00732 246 ALA   A CB  
1302 N  N   . HIS   A 170 ? 0.35626 0.34204 0.35300 0.01186  0.01793  -0.00462 247 HIS   A N   
1303 C  CA  . HIS   A 170 ? 0.35394 0.34375 0.35314 0.01355  0.02004  -0.00466 247 HIS   A CA  
1304 C  C   . HIS   A 170 ? 0.39024 0.38151 0.38810 0.01185  0.02069  -0.00315 247 HIS   A C   
1305 O  O   . HIS   A 170 ? 0.38140 0.37176 0.37745 0.01286  0.02186  -0.00393 247 HIS   A O   
1306 C  CB  . HIS   A 170 ? 0.38624 0.37332 0.38413 0.01624  0.02070  -0.00696 247 HIS   A CB  
1307 C  CG  . HIS   A 170 ? 0.39337 0.38029 0.39334 0.01808  0.02053  -0.00823 247 HIS   A CG  
1308 N  ND1 . HIS   A 170 ? 0.37326 0.36376 0.37681 0.01960  0.02193  -0.00822 247 HIS   A ND1 
1309 C  CD2 . HIS   A 170 ? 0.43963 0.42317 0.43849 0.01878  0.01928  -0.00940 247 HIS   A CD2 
1310 C  CE1 . HIS   A 170 ? 0.37661 0.36579 0.38100 0.02084  0.02129  -0.00943 247 HIS   A CE1 
1311 N  NE2 . HIS   A 170 ? 0.41184 0.39710 0.41358 0.02035  0.01972  -0.01013 247 HIS   A NE2 
1312 N  N   . ASN   A 171 ? 0.36854 0.36201 0.36697 0.00887  0.01975  -0.00081 248 ASN   A N   
1313 C  CA  . ASN   A 171 ? 0.36169 0.35856 0.36030 0.00708  0.02059  0.00128  248 ASN   A CA  
1314 C  C   . ASN   A 171 ? 0.39071 0.39509 0.39475 0.00610  0.02121  0.00415  248 ASN   A C   
1315 O  O   . ASN   A 171 ? 0.41367 0.42089 0.42167 0.00791  0.02180  0.00407  248 ASN   A O   
1316 C  CB  . ASN   A 171 ? 0.39152 0.38394 0.38512 0.00379  0.01862  0.00205  248 ASN   A CB  
1317 C  CG  . ASN   A 171 ? 0.37891 0.36565 0.36793 0.00498  0.01864  0.00014  248 ASN   A CG  
1318 O  OD1 . ASN   A 171 ? 0.38463 0.37225 0.37255 0.00500  0.01980  0.00042  248 ASN   A OD1 
1319 N  ND2 . ASN   A 171 ? 0.33767 0.31880 0.32409 0.00606  0.01746  -0.00160 248 ASN   A ND2 
1320 N  N   . GLN   A 172 ? 0.36237 0.37031 0.36687 0.00312  0.02096  0.00702  249 GLN   A N   
1321 C  CA  . GLN   A 172 ? 0.36030 0.37680 0.37082 0.00223  0.02173  0.01052  249 GLN   A CA  
1322 C  C   . GLN   A 172 ? 0.36165 0.37938 0.37150 -0.00286 0.01881  0.01356  249 GLN   A C   
1323 O  O   . GLN   A 172 ? 0.38681 0.41189 0.40062 -0.00486 0.01913  0.01732  249 GLN   A O   
1324 C  CB  . GLN   A 172 ? 0.41703 0.43899 0.43016 0.00382  0.02502  0.01198  249 GLN   A CB  
1325 C  CG  . GLN   A 172 ? 0.38305 0.40494 0.39754 0.00874  0.02830  0.00975  249 GLN   A CG  
1326 C  CD  . GLN   A 172 ? 0.49447 0.51581 0.50646 0.01003  0.03106  0.00921  249 GLN   A CD  
1327 O  OE1 . GLN   A 172 ? 0.51034 0.53697 0.52426 0.00892  0.03256  0.01208  249 GLN   A OE1 
1328 N  NE2 . GLN   A 172 ? 0.52848 0.54348 0.53598 0.01212  0.03165  0.00573  249 GLN   A NE2 
1329 N  N   . LEU   A 173 ? 0.36059 0.37112 0.36523 -0.00510 0.01600  0.01221  250 LEU   A N   
1330 C  CA  . LEU   A 173 ? 0.38856 0.39852 0.39075 -0.01050 0.01307  0.01495  250 LEU   A CA  
1331 C  C   . LEU   A 173 ? 0.38120 0.39846 0.38911 -0.01210 0.01214  0.01813  250 LEU   A C   
1332 O  O   . LEU   A 173 ? 0.37729 0.39485 0.38768 -0.00985 0.01228  0.01696  250 LEU   A O   
1333 C  CB  . LEU   A 173 ? 0.37072 0.37003 0.36507 -0.01216 0.01070  0.01265  250 LEU   A CB  
1334 C  CG  . LEU   A 173 ? 0.40430 0.39562 0.39237 -0.01115 0.01102  0.01014  250 LEU   A CG  
1335 C  CD1 . LEU   A 173 ? 0.39588 0.37711 0.37660 -0.01279 0.00890  0.00866  250 LEU   A CD1 
1336 C  CD2 . LEU   A 173 ? 0.40122 0.39445 0.38797 -0.01373 0.01115  0.01225  250 LEU   A CD2 
1337 N  N   . GLU   A 174 ? 0.39824 0.42162 0.40832 -0.01622 0.01102  0.02245  251 GLU   A N   
1338 C  CA  . GLU   A 174 ? 0.38518 0.41534 0.40005 -0.01900 0.00924  0.02628  251 GLU   A CA  
1339 C  C   . GLU   A 174 ? 0.41649 0.44122 0.42513 -0.02528 0.00502  0.02762  251 GLU   A C   
1340 O  O   . GLU   A 174 ? 0.41449 0.44170 0.42507 -0.02750 0.00298  0.02960  251 GLU   A O   
1341 C  CB  . GLU   A 174 ? 0.44079 0.48298 0.46333 -0.01953 0.01077  0.03113  251 GLU   A CB  
1342 C  CG  . GLU   A 174 ? 0.45515 0.50229 0.48339 -0.01317 0.01537  0.03005  251 GLU   A CG  
1343 C  CD  . GLU   A 174 ? 0.54258 0.60154 0.57843 -0.01305 0.01754  0.03504  251 GLU   A CD  
1344 O  OE1 . GLU   A 174 ? 0.52637 0.59283 0.56676 -0.01670 0.01550  0.03993  251 GLU   A OE1 
1345 O  OE2 . GLU   A 174 ? 0.64599 0.70673 0.68309 -0.00941 0.02130  0.03426  251 GLU   A OE2 
1346 N  N   . HIS   A 175 ? 0.43557 0.45241 0.43623 -0.02832 0.00363  0.02667  252 HIS   A N   
1347 C  CA  . HIS   A 175 ? 0.38328 0.39211 0.37580 -0.03406 -0.00012 0.02723  252 HIS   A CA  
1348 C  C   . HIS   A 175 ? 0.44282 0.43885 0.42583 -0.03327 -0.00005 0.02320  252 HIS   A C   
1349 O  O   . HIS   A 175 ? 0.44953 0.44427 0.43280 -0.02916 0.00243  0.02075  252 HIS   A O   
1350 C  CB  . HIS   A 175 ? 0.41102 0.42477 0.40345 -0.04075 -0.00267 0.03240  252 HIS   A CB  
1351 C  CG  . HIS   A 175 ? 0.40270 0.43060 0.40552 -0.04137 -0.00248 0.03728  252 HIS   A CG  
1352 N  ND1 . HIS   A 175 ? 0.38130 0.41279 0.38631 -0.04472 -0.00516 0.04022  252 HIS   A ND1 
1353 C  CD2 . HIS   A 175 ? 0.37909 0.41845 0.39076 -0.03879 0.00030  0.03994  252 HIS   A CD2 
1354 C  CE1 . HIS   A 175 ? 0.39382 0.43899 0.40921 -0.04410 -0.00415 0.04478  252 HIS   A CE1 
1355 N  NE2 . HIS   A 175 ? 0.42754 0.47757 0.44707 -0.04035 -0.00064 0.04466  252 HIS   A NE2 
1356 N  N   . LEU   A 176 ? 0.42747 0.41370 0.40168 -0.03732 -0.00277 0.02275  253 LEU   A N   
1357 C  CA  . LEU   A 176 ? 0.43303 0.40705 0.39760 -0.03740 -0.00285 0.02001  253 LEU   A CA  
1358 C  C   . LEU   A 176 ? 0.44538 0.41521 0.40287 -0.04440 -0.00574 0.02290  253 LEU   A C   
1359 O  O   . LEU   A 176 ? 0.47233 0.44444 0.42918 -0.04992 -0.00855 0.02617  253 LEU   A O   
1360 C  CB  . LEU   A 176 ? 0.45936 0.42242 0.41736 -0.03558 -0.00297 0.01649  253 LEU   A CB  
1361 C  CG  . LEU   A 176 ? 0.44666 0.41043 0.40894 -0.02907 -0.00050 0.01311  253 LEU   A CG  
1362 C  CD1 . LEU   A 176 ? 0.46473 0.41635 0.41841 -0.02892 -0.00107 0.01055  253 LEU   A CD1 
1363 C  CD2 . LEU   A 176 ? 0.43833 0.40339 0.40327 -0.02414 0.00219  0.01108  253 LEU   A CD2 
1364 N  N   . PRO   A 177 ? 0.42502 0.38838 0.37669 -0.04469 -0.00536 0.02197  254 PRO   A N   
1365 C  CA  . PRO   A 177 ? 0.45316 0.41046 0.39643 -0.05164 -0.00829 0.02446  254 PRO   A CA  
1366 C  C   . PRO   A 177 ? 0.44730 0.39215 0.38022 -0.05492 -0.01053 0.02340  254 PRO   A C   
1367 O  O   . PRO   A 177 ? 0.44015 0.37668 0.36925 -0.05078 -0.00908 0.01967  254 PRO   A O   
1368 C  CB  . PRO   A 177 ? 0.46542 0.41700 0.40442 -0.04974 -0.00685 0.02281  254 PRO   A CB  
1369 C  CG  . PRO   A 177 ? 0.45432 0.40415 0.39594 -0.04215 -0.00374 0.01865  254 PRO   A CG  
1370 C  CD  . PRO   A 177 ? 0.43666 0.39635 0.38792 -0.03891 -0.00255 0.01848  254 PRO   A CD  
1371 N  N   . LYS   A 178 ? 0.42315 0.36680 0.35137 -0.06255 -0.01407 0.02692  255 LYS   A N   
1372 C  CA  . LYS   A 178 ? 0.50091 0.43124 0.41757 -0.06624 -0.01622 0.02590  255 LYS   A CA  
1373 C  C   . LYS   A 178 ? 0.52354 0.43763 0.42827 -0.06469 -0.01513 0.02254  255 LYS   A C   
1374 O  O   . LYS   A 178 ? 0.47626 0.37824 0.37238 -0.06391 -0.01489 0.01995  255 LYS   A O   
1375 C  CB  . LYS   A 178 ? 0.46416 0.39537 0.37672 -0.07559 -0.02062 0.03060  255 LYS   A CB  
1376 C  CG  . LYS   A 178 ? 0.50125 0.42887 0.40741 -0.08140 -0.02262 0.03319  255 LYS   A CG  
1377 C  CD  . LYS   A 178 ? 0.54975 0.47930 0.45244 -0.09116 -0.02738 0.03830  255 LYS   A CD  
1378 C  CE  . LYS   A 178 ? 0.51865 0.44365 0.41380 -0.09773 -0.02973 0.04105  255 LYS   A CE  
1379 N  NZ  . LYS   A 178 ? 0.49160 0.42237 0.39289 -0.09308 -0.02678 0.04037  255 LYS   A NZ  
1380 N  N   . GLU   A 179 ? 0.46587 0.37955 0.37014 -0.06374 -0.01414 0.02258  256 GLU   A N   
1381 C  CA  . GLU   A 179 ? 0.49019 0.38896 0.38373 -0.06190 -0.01298 0.01982  256 GLU   A CA  
1382 C  C   . GLU   A 179 ? 0.50444 0.39918 0.39935 -0.05368 -0.00954 0.01553  256 GLU   A C   
1383 O  O   . GLU   A 179 ? 0.51332 0.39533 0.39947 -0.05141 -0.00827 0.01333  256 GLU   A O   
1384 C  CB  . GLU   A 179 ? 0.52387 0.42436 0.41762 -0.06263 -0.01277 0.02111  256 GLU   A CB  
1385 C  CG  . GLU   A 179 ? 0.51652 0.41882 0.40686 -0.07129 -0.01628 0.02552  256 GLU   A CG  
1386 C  CD  . GLU   A 179 ? 0.54542 0.46599 0.44854 -0.07323 -0.01707 0.02929  256 GLU   A CD  
1387 O  OE1 . GLU   A 179 ? 0.51034 0.44131 0.42440 -0.06769 -0.01476 0.02822  256 GLU   A OE1 
1388 O  OE2 . GLU   A 179 ? 0.58433 0.50875 0.48643 -0.08026 -0.01992 0.03353  256 GLU   A OE2 
1389 N  N   . ILE   A 180 ? 0.48817 0.39324 0.39364 -0.04919 -0.00798 0.01456  257 ILE   A N   
1390 C  CA  . ILE   A 180 ? 0.47796 0.37924 0.38442 -0.04207 -0.00508 0.01085  257 ILE   A CA  
1391 C  C   . ILE   A 180 ? 0.49398 0.38108 0.38937 -0.04292 -0.00532 0.00920  257 ILE   A C   
1392 O  O   . ILE   A 180 ? 0.52362 0.40310 0.41580 -0.03765 -0.00285 0.00640  257 ILE   A O   
1393 C  CB  . ILE   A 180 ? 0.43667 0.35088 0.35551 -0.03797 -0.00374 0.01032  257 ILE   A CB  
1394 C  CG1 . ILE   A 180 ? 0.47737 0.38803 0.39727 -0.03083 -0.00084 0.00678  257 ILE   A CG1 
1395 C  CG2 . ILE   A 180 ? 0.49633 0.41323 0.41602 -0.04157 -0.00571 0.01168  257 ILE   A CG2 
1396 C  CD1 . ILE   A 180 ? 0.56999 0.48146 0.49215 -0.02648 0.00116  0.00571  257 ILE   A CD1 
1397 N  N   . GLY   A 181 ? 0.50169 0.38498 0.39086 -0.04961 -0.00821 0.01111  258 GLY   A N   
1398 C  CA  . GLY   A 181 ? 0.52186 0.39005 0.39845 -0.05139 -0.00855 0.00969  258 GLY   A CA  
1399 C  C   . GLY   A 181 ? 0.51983 0.37184 0.38351 -0.05123 -0.00760 0.00844  258 GLY   A C   
1400 O  O   . GLY   A 181 ? 0.54430 0.38239 0.39709 -0.05103 -0.00678 0.00672  258 GLY   A O   
1401 N  N   . ASN   A 182 ? 0.50970 0.36264 0.37381 -0.05129 -0.00754 0.00936  259 ASN   A N   
1402 C  CA  . ASN   A 182 ? 0.49022 0.32789 0.34274 -0.05013 -0.00625 0.00816  259 ASN   A CA  
1403 C  C   . ASN   A 182 ? 0.53778 0.37287 0.39281 -0.04123 -0.00225 0.00526  259 ASN   A C   
1404 O  O   . ASN   A 182 ? 0.57148 0.39349 0.41718 -0.03909 -0.00061 0.00424  259 ASN   A O   
1405 C  CB  . ASN   A 182 ? 0.52181 0.36104 0.37363 -0.05332 -0.00764 0.01030  259 ASN   A CB  
1406 C  CG  . ASN   A 182 ? 0.56541 0.40567 0.41315 -0.06271 -0.01175 0.01370  259 ASN   A CG  
1407 O  OD1 . ASN   A 182 ? 0.56353 0.40008 0.40612 -0.06739 -0.01378 0.01441  259 ASN   A OD1 
1408 N  ND2 . ASN   A 182 ? 0.56932 0.41466 0.41911 -0.06580 -0.01312 0.01607  259 ASN   A ND2 
1409 N  N   . CYS   A 183 ? 0.57741 0.42478 0.44485 -0.03607 -0.00067 0.00421  260 CYS   A N   
1410 C  CA  . CYS   A 183 ? 0.53378 0.38056 0.40486 -0.02793 0.00281  0.00196  260 CYS   A CA  
1411 C  C   . CYS   A 183 ? 0.55358 0.39271 0.42021 -0.02508 0.00461  -0.00002 260 CYS   A C   
1412 O  O   . CYS   A 183 ? 0.53567 0.38217 0.41048 -0.02066 0.00612  -0.00127 260 CYS   A O   
1413 C  CB  . CYS   A 183 ? 0.55486 0.41803 0.44065 -0.02424 0.00347  0.00196  260 CYS   A CB  
1414 S  SG  . CYS   A 183 ? 0.51565 0.38926 0.40738 -0.02770 0.00167  0.00442  260 CYS   A SG  
1415 N  N   . THR   A 184 ? 0.53026 0.35354 0.38286 -0.02778 0.00456  -0.00029 261 THR   A N   
1416 C  CA  . THR   A 184 ? 0.55546 0.36918 0.40093 -0.02660 0.00605  -0.00192 261 THR   A CA  
1417 C  C   . THR   A 184 ? 0.55161 0.36368 0.39993 -0.01800 0.01021  -0.00387 261 THR   A C   
1418 O  O   . THR   A 184 ? 0.57009 0.37529 0.41348 -0.01642 0.01187  -0.00522 261 THR   A O   
1419 C  CB  . THR   A 184 ? 0.61196 0.40719 0.43997 -0.03152 0.00531  -0.00170 261 THR   A CB  
1420 O  OG1 . THR   A 184 ? 0.62471 0.41282 0.44744 -0.03073 0.00597  -0.00113 261 THR   A OG1 
1421 C  CG2 . THR   A 184 ? 0.59894 0.39590 0.42369 -0.04088 0.00084  0.00033  261 THR   A CG2 
1422 N  N   . GLN   A 185 ? 0.56334 0.38153 0.41928 -0.01261 0.01189  -0.00385 262 GLN   A N   
1423 C  CA  . GLN   A 185 ? 0.54991 0.36826 0.40973 -0.00477 0.01552  -0.00511 262 GLN   A CA  
1424 C  C   . GLN   A 185 ? 0.52435 0.35861 0.39847 -0.00182 0.01557  -0.00559 262 GLN   A C   
1425 O  O   . GLN   A 185 ? 0.53730 0.37305 0.41544 0.00417  0.01825  -0.00641 262 GLN   A O   
1426 C  CB  . GLN   A 185 ? 0.52160 0.33649 0.38086 -0.00014 0.01748  -0.00451 262 GLN   A CB  
1427 C  CG  . GLN   A 185 ? 0.59463 0.39210 0.43912 -0.00163 0.01823  -0.00413 262 GLN   A CG  
1428 C  CD  . GLN   A 185 ? 0.69975 0.48334 0.53435 0.00164  0.02154  -0.00532 262 GLN   A CD  
1429 O  OE1 . GLN   A 185 ? 0.78777 0.55939 0.61035 -0.00286 0.02093  -0.00586 262 GLN   A OE1 
1430 N  NE2 . GLN   A 185 ? 0.70964 0.49461 0.54893 0.00941  0.02516  -0.00555 262 GLN   A NE2 
1431 N  N   . ILE   A 186 ? 0.48588 0.33185 0.36762 -0.00577 0.01281  -0.00488 263 ILE   A N   
1432 C  CA  . ILE   A 186 ? 0.51768 0.37806 0.41248 -0.00286 0.01298  -0.00531 263 ILE   A CA  
1433 C  C   . ILE   A 186 ? 0.48585 0.34510 0.38107 -0.00031 0.01449  -0.00670 263 ILE   A C   
1434 O  O   . ILE   A 186 ? 0.52273 0.37649 0.41181 -0.00393 0.01358  -0.00695 263 ILE   A O   
1435 C  CB  . ILE   A 186 ? 0.47311 0.34483 0.37469 -0.00766 0.01008  -0.00410 263 ILE   A CB  
1436 C  CG1 . ILE   A 186 ? 0.47932 0.35492 0.38304 -0.00897 0.00914  -0.00274 263 ILE   A CG1 
1437 C  CG2 . ILE   A 186 ? 0.47127 0.35559 0.38436 -0.00502 0.01040  -0.00473 263 ILE   A CG2 
1438 C  CD1 . ILE   A 186 ? 0.44176 0.32889 0.35237 -0.01332 0.00679  -0.00116 263 ILE   A CD1 
1439 N  N   . THR   A 187 ? 0.44829 0.31299 0.35072 0.00562  0.01665  -0.00743 264 THR   A N   
1440 C  CA  . THR   A 187 ? 0.50010 0.36610 0.40481 0.00810  0.01799  -0.00857 264 THR   A CA  
1441 C  C   . THR   A 187 ? 0.47508 0.35548 0.39216 0.00928  0.01720  -0.00879 264 THR   A C   
1442 O  O   . THR   A 187 ? 0.47541 0.35798 0.39448 0.00950  0.01736  -0.00955 264 THR   A O   
1443 C  CB  . THR   A 187 ? 0.50353 0.36271 0.40536 0.01422  0.02154  -0.00903 264 THR   A CB  
1444 O  OG1 . THR   A 187 ? 0.57871 0.44643 0.48950 0.01865  0.02236  -0.00843 264 THR   A OG1 
1445 C  CG2 . THR   A 187 ? 0.48795 0.33250 0.37757 0.01379  0.02274  -0.00870 264 THR   A CG2 
1446 N  N   . ASN   A 188 ? 0.46093 0.35047 0.38564 0.00997  0.01644  -0.00816 265 ASN   A N   
1447 C  CA  . ASN   A 188 ? 0.42169 0.32375 0.35701 0.01088  0.01580  -0.00838 265 ASN   A CA  
1448 C  C   . ASN   A 188 ? 0.42862 0.33762 0.36760 0.00723  0.01375  -0.00735 265 ASN   A C   
1449 O  O   . ASN   A 188 ? 0.46572 0.37584 0.40537 0.00761  0.01371  -0.00670 265 ASN   A O   
1450 C  CB  . ASN   A 188 ? 0.45519 0.36182 0.39651 0.01621  0.01746  -0.00862 265 ASN   A CB  
1451 C  CG  . ASN   A 188 ? 0.48866 0.38798 0.42594 0.02021  0.01986  -0.00890 265 ASN   A CG  
1452 O  OD1 . ASN   A 188 ? 0.54053 0.43837 0.47719 0.02115  0.02076  -0.00967 265 ASN   A OD1 
1453 N  ND2 . ASN   A 188 ? 0.51899 0.41369 0.45348 0.02279  0.02111  -0.00806 265 ASN   A ND2 
1454 N  N   . LEU   A 189 ? 0.39281 0.30685 0.33446 0.00386  0.01217  -0.00697 266 LEU   A N   
1455 C  CA  . LEU   A 189 ? 0.41838 0.34023 0.36452 0.00074  0.01060  -0.00560 266 LEU   A CA  
1456 C  C   . LEU   A 189 ? 0.37533 0.30778 0.33084 0.00228  0.01073  -0.00589 266 LEU   A C   
1457 O  O   . LEU   A 189 ? 0.41129 0.34500 0.36798 0.00153  0.01026  -0.00607 266 LEU   A O   
1458 C  CB  . LEU   A 189 ? 0.39511 0.31332 0.33558 -0.00516 0.00848  -0.00407 266 LEU   A CB  
1459 C  CG  . LEU   A 189 ? 0.40265 0.32872 0.34719 -0.00888 0.00686  -0.00194 266 LEU   A CG  
1460 C  CD1 . LEU   A 189 ? 0.36158 0.28853 0.30659 -0.00783 0.00749  -0.00161 266 LEU   A CD1 
1461 C  CD2 . LEU   A 189 ? 0.39768 0.31947 0.33592 -0.01508 0.00447  -0.00009 266 LEU   A CD2 
1462 N  N   . ASP   A 190 ? 0.37284 0.31220 0.33441 0.00448  0.01142  -0.00596 267 ASP   A N   
1463 C  CA  . ASP   A 190 ? 0.38521 0.33364 0.35480 0.00602  0.01178  -0.00625 267 ASP   A CA  
1464 C  C   . ASP   A 190 ? 0.39993 0.35538 0.37332 0.00360  0.01120  -0.00460 267 ASP   A C   
1465 O  O   . ASP   A 190 ? 0.39390 0.35035 0.36720 0.00360  0.01156  -0.00415 267 ASP   A O   
1466 C  CB  . ASP   A 190 ? 0.38310 0.33382 0.35636 0.01047  0.01322  -0.00760 267 ASP   A CB  
1467 C  CG  . ASP   A 190 ? 0.48088 0.43907 0.46102 0.01201  0.01362  -0.00816 267 ASP   A CG  
1468 O  OD1 . ASP   A 190 ? 0.41506 0.37674 0.39742 0.00998  0.01294  -0.00736 267 ASP   A OD1 
1469 O  OD2 . ASP   A 190 ? 0.46327 0.42370 0.44638 0.01504  0.01451  -0.00914 267 ASP   A OD2 
1470 N  N   . LEU   A 191 ? 0.36572 0.32629 0.34265 0.00168  0.01043  -0.00348 268 LEU   A N   
1471 C  CA  . LEU   A 191 ? 0.36992 0.33811 0.35130 -0.00038 0.01015  -0.00135 268 LEU   A CA  
1472 C  C   . LEU   A 191 ? 0.40176 0.37800 0.39073 0.00191  0.01118  -0.00133 268 LEU   A C   
1473 O  O   . LEU   A 191 ? 0.34822 0.33137 0.34162 0.00048  0.01114  0.00085  268 LEU   A O   
1474 C  CB  . LEU   A 191 ? 0.36604 0.33319 0.34433 -0.00559 0.00800  0.00106  268 LEU   A CB  
1475 C  CG  . LEU   A 191 ? 0.31962 0.27811 0.28936 -0.00866 0.00684  0.00141  268 LEU   A CG  
1476 C  CD1 . LEU   A 191 ? 0.32632 0.28240 0.29189 -0.01416 0.00438  0.00356  268 LEU   A CD1 
1477 C  CD2 . LEU   A 191 ? 0.36630 0.32731 0.33671 -0.00913 0.00732  0.00240  268 LEU   A CD2 
1478 N  N   . GLN   A 192 ? 0.38111 0.35656 0.37163 0.00550  0.01219  -0.00349 269 GLN   A N   
1479 C  CA  . GLN   A 192 ? 0.36513 0.34674 0.36184 0.00775  0.01317  -0.00368 269 GLN   A CA  
1480 C  C   . GLN   A 192 ? 0.37195 0.35946 0.37266 0.00893  0.01477  -0.00293 269 GLN   A C   
1481 O  O   . GLN   A 192 ? 0.36176 0.34802 0.36045 0.00909  0.01540  -0.00317 269 GLN   A O   
1482 C  CB  . GLN   A 192 ? 0.35627 0.33534 0.35309 0.01116  0.01392  -0.00612 269 GLN   A CB  
1483 C  CG  . GLN   A 192 ? 0.37056 0.34731 0.36577 0.01344  0.01491  -0.00755 269 GLN   A CG  
1484 C  CD  . GLN   A 192 ? 0.45761 0.43338 0.45391 0.01650  0.01547  -0.00938 269 GLN   A CD  
1485 O  OE1 . GLN   A 192 ? 0.44388 0.42277 0.44370 0.01759  0.01578  -0.00974 269 GLN   A OE1 
1486 N  NE2 . GLN   A 192 ? 0.44576 0.41741 0.43917 0.01786  0.01556  -0.01024 269 GLN   A NE2 
1487 N  N   . HIS   A 193 ? 0.36360 0.35726 0.36976 0.00991  0.01561  -0.00193 270 HIS   A N   
1488 C  CA  . HIS   A 193 ? 0.36776 0.36667 0.37769 0.01179  0.01780  -0.00130 270 HIS   A CA  
1489 C  C   . HIS   A 193 ? 0.37722 0.37793 0.38616 0.00961  0.01802  0.00059  270 HIS   A C   
1490 O  O   . HIS   A 193 ? 0.40123 0.40069 0.40831 0.01063  0.01926  -0.00029 270 HIS   A O   
1491 C  CB  . HIS   A 193 ? 0.39293 0.38936 0.40197 0.01525  0.01936  -0.00401 270 HIS   A CB  
1492 C  CG  . HIS   A 193 ? 0.39189 0.38822 0.40302 0.01751  0.01957  -0.00537 270 HIS   A CG  
1493 N  ND1 . HIS   A 193 ? 0.38914 0.38104 0.39804 0.01784  0.01830  -0.00705 270 HIS   A ND1 
1494 C  CD2 . HIS   A 193 ? 0.34482 0.34474 0.35987 0.01962  0.02105  -0.00517 270 HIS   A CD2 
1495 C  CE1 . HIS   A 193 ? 0.39027 0.38330 0.40170 0.01973  0.01875  -0.00784 270 HIS   A CE1 
1496 N  NE2 . HIS   A 193 ? 0.39600 0.39356 0.41100 0.02083  0.02036  -0.00678 270 HIS   A NE2 
1497 N  N   . ASN   A 194 ? 0.37294 0.37663 0.38292 0.00618  0.01655  0.00344  271 ASN   A N   
1498 C  CA  . ASN   A 194 ? 0.36692 0.37466 0.37766 0.00375  0.01676  0.00621  271 ASN   A CA  
1499 C  C   . ASN   A 194 ? 0.37763 0.39414 0.39498 0.00303  0.01709  0.00976  271 ASN   A C   
1500 O  O   . ASN   A 194 ? 0.38810 0.40779 0.40982 0.00594  0.01841  0.00955  271 ASN   A O   
1501 C  CB  . ASN   A 194 ? 0.36861 0.37135 0.37360 -0.00057 0.01423  0.00694  271 ASN   A CB  
1502 C  CG  . ASN   A 194 ? 0.38878 0.38488 0.38824 0.00020  0.01454  0.00465  271 ASN   A CG  
1503 O  OD1 . ASN   A 194 ? 0.38981 0.38752 0.38895 0.00002  0.01563  0.00533  271 ASN   A OD1 
1504 N  ND2 . ASN   A 194 ? 0.34593 0.33474 0.34109 0.00115  0.01371  0.00217  271 ASN   A ND2 
1505 N  N   . GLU   A 195 ? 0.34133 0.36187 0.35952 -0.00089 0.01583  0.01331  272 GLU   A N   
1506 C  CA  . GLU   A 195 ? 0.37496 0.40476 0.39992 -0.00210 0.01575  0.01757  272 GLU   A CA  
1507 C  C   . GLU   A 195 ? 0.37615 0.40600 0.39906 -0.00809 0.01201  0.02053  272 GLU   A C   
1508 O  O   . GLU   A 195 ? 0.38148 0.41913 0.40862 -0.01092 0.01136  0.02505  272 GLU   A O   
1509 C  CB  . GLU   A 195 ? 0.41062 0.44814 0.44042 -0.00053 0.01873  0.02012  272 GLU   A CB  
1510 C  CG  . GLU   A 195 ? 0.43093 0.46794 0.46189 0.00515  0.02272  0.01746  272 GLU   A CG  
1511 C  CD  . GLU   A 195 ? 0.56670 0.60781 0.60339 0.00905  0.02461  0.01782  272 GLU   A CD  
1512 O  OE1 . GLU   A 195 ? 0.54092 0.58768 0.58243 0.00760  0.02324  0.02105  272 GLU   A OE1 
1513 O  OE2 . GLU   A 195 ? 0.65522 0.69362 0.69126 0.01342  0.02739  0.01501  272 GLU   A OE2 
1514 N  N   . LEU   A 196 ? 0.34725 0.36826 0.36340 -0.01018 0.00956  0.01822  273 LEU   A N   
1515 C  CA  . LEU   A 196 ? 0.35871 0.37672 0.37002 -0.01632 0.00600  0.02037  273 LEU   A CA  
1516 C  C   . LEU   A 196 ? 0.36926 0.39465 0.38557 -0.01936 0.00402  0.02460  273 LEU   A C   
1517 O  O   . LEU   A 196 ? 0.33987 0.36645 0.35907 -0.01751 0.00398  0.02407  273 LEU   A O   
1518 C  CB  . LEU   A 196 ? 0.34317 0.34933 0.34584 -0.01700 0.00450  0.01677  273 LEU   A CB  
1519 C  CG  . LEU   A 196 ? 0.40256 0.40148 0.39956 -0.01544 0.00569  0.01382  273 LEU   A CG  
1520 C  CD1 . LEU   A 196 ? 0.34979 0.33751 0.33915 -0.01491 0.00494  0.01041  273 LEU   A CD1 
1521 C  CD2 . LEU   A 196 ? 0.33512 0.33453 0.32938 -0.01970 0.00461  0.01643  273 LEU   A CD2 
1522 N  N   . LEU   A 197 ? 0.34346 0.37403 0.36082 -0.02430 0.00218  0.02909  274 LEU   A N   
1523 C  CA  . LEU   A 197 ? 0.37664 0.41502 0.39895 -0.02788 -0.00017 0.03391  274 LEU   A CA  
1524 C  C   . LEU   A 197 ? 0.39018 0.42105 0.40462 -0.03398 -0.00444 0.03427  274 LEU   A C   
1525 O  O   . LEU   A 197 ? 0.37566 0.41075 0.39285 -0.03670 -0.00672 0.03728  274 LEU   A O   
1526 C  CB  . LEU   A 197 ? 0.38878 0.43816 0.41721 -0.03040 -0.00009 0.03947  274 LEU   A CB  
1527 C  CG  . LEU   A 197 ? 0.39892 0.45815 0.43675 -0.02459 0.00431  0.04067  274 LEU   A CG  
1528 C  CD1 . LEU   A 197 ? 0.36828 0.43593 0.40972 -0.02729 0.00468  0.04545  274 LEU   A CD1 
1529 C  CD2 . LEU   A 197 ? 0.30319 0.37019 0.34934 -0.02169 0.00513  0.04280  274 LEU   A CD2 
1530 N  N   . ASP   A 198 ? 0.38587 0.40523 0.39017 -0.03608 -0.00545 0.03132  275 ASP   A N   
1531 C  CA  . ASP   A 198 ? 0.39471 0.40470 0.38952 -0.04180 -0.00908 0.03125  275 ASP   A CA  
1532 C  C   . ASP   A 198 ? 0.42364 0.42037 0.40803 -0.04137 -0.00852 0.02700  275 ASP   A C   
1533 O  O   . ASP   A 198 ? 0.43429 0.43047 0.41949 -0.03749 -0.00589 0.02485  275 ASP   A O   
1534 C  CB  . ASP   A 198 ? 0.38548 0.40034 0.37997 -0.04953 -0.01280 0.03699  275 ASP   A CB  
1535 C  CG  . ASP   A 198 ? 0.44171 0.46176 0.43832 -0.05090 -0.01215 0.03950  275 ASP   A CG  
1536 O  OD1 . ASP   A 198 ? 0.46126 0.47462 0.45319 -0.04860 -0.01027 0.03614  275 ASP   A OD1 
1537 O  OD2 . ASP   A 198 ? 0.48399 0.51521 0.48717 -0.05433 -0.01351 0.04513  275 ASP   A OD2 
1538 N  N   . LEU   A 199 ? 0.39481 0.38058 0.36911 -0.04536 -0.01094 0.02596  276 LEU   A N   
1539 C  CA  . LEU   A 199 ? 0.42863 0.40076 0.39188 -0.04562 -0.01067 0.02261  276 LEU   A CA  
1540 C  C   . LEU   A 199 ? 0.47558 0.44199 0.43002 -0.05362 -0.01419 0.02547  276 LEU   A C   
1541 O  O   . LEU   A 199 ? 0.45806 0.42791 0.41257 -0.05932 -0.01739 0.02919  276 LEU   A O   
1542 C  CB  . LEU   A 199 ? 0.44042 0.40241 0.39774 -0.04291 -0.00989 0.01855  276 LEU   A CB  
1543 C  CG  . LEU   A 199 ? 0.44637 0.41252 0.41109 -0.03535 -0.00663 0.01551  276 LEU   A CG  
1544 C  CD1 . LEU   A 199 ? 0.38937 0.34801 0.34946 -0.03414 -0.00662 0.01292  276 LEU   A CD1 
1545 C  CD2 . LEU   A 199 ? 0.45920 0.42233 0.42332 -0.03066 -0.00383 0.01263  276 LEU   A CD2 
1546 N  N   . PRO   A 200 ? 0.44466 0.40225 0.39121 -0.05453 -0.01389 0.02409  277 PRO   A N   
1547 C  CA  . PRO   A 200 ? 0.46846 0.41884 0.40508 -0.06245 -0.01734 0.02662  277 PRO   A CA  
1548 C  C   . PRO   A 200 ? 0.47847 0.41508 0.40323 -0.06542 -0.01900 0.02486  277 PRO   A C   
1549 O  O   . PRO   A 200 ? 0.52036 0.45045 0.44283 -0.06048 -0.01677 0.02088  277 PRO   A O   
1550 C  CB  . PRO   A 200 ? 0.48842 0.43285 0.42040 -0.06114 -0.01585 0.02505  277 PRO   A CB  
1551 C  CG  . PRO   A 200 ? 0.46256 0.40459 0.39710 -0.05260 -0.01186 0.02029  277 PRO   A CG  
1552 C  CD  . PRO   A 200 ? 0.44613 0.39795 0.39092 -0.04849 -0.01059 0.01993  277 PRO   A CD  
1553 N  N   . ASP   A 201 ? 0.50750 0.43983 0.42453 -0.07379 -0.02296 0.02808  278 ASP   A N   
1554 C  CA  . ASP   A 201 ? 0.51456 0.43282 0.41873 -0.07764 -0.02477 0.02676  278 ASP   A CA  
1555 C  C   . ASP   A 201 ? 0.50084 0.40108 0.39106 -0.07653 -0.02318 0.02291  278 ASP   A C   
1556 O  O   . ASP   A 201 ? 0.51975 0.40676 0.39892 -0.07765 -0.02333 0.02077  278 ASP   A O   
1557 C  CB  . ASP   A 201 ? 0.53346 0.45281 0.43328 -0.08761 -0.02984 0.03181  278 ASP   A CB  
1558 C  CG  . ASP   A 201 ? 0.56347 0.49978 0.47647 -0.08865 -0.03147 0.03595  278 ASP   A CG  
1559 O  OD1 . ASP   A 201 ? 0.51600 0.45392 0.43238 -0.08549 -0.03064 0.03445  278 ASP   A OD1 
1560 O  OD2 . ASP   A 201 ? 0.59165 0.53983 0.51183 -0.09239 -0.03341 0.04088  278 ASP   A OD2 
1561 N  N   . THR   A 202 ? 0.48157 0.38077 0.37175 -0.07437 -0.02158 0.02221  279 THR   A N   
1562 C  CA  . THR   A 202 ? 0.47408 0.35764 0.35312 -0.07158 -0.01934 0.01855  279 THR   A CA  
1563 C  C   . THR   A 202 ? 0.53048 0.41128 0.41199 -0.06286 -0.01524 0.01410  279 THR   A C   
1564 O  O   . THR   A 202 ? 0.51609 0.38368 0.38851 -0.05985 -0.01303 0.01116  279 THR   A O   
1565 C  CB  . THR   A 202 ? 0.54383 0.42934 0.42432 -0.07105 -0.01869 0.01930  279 THR   A CB  
1566 O  OG1 . THR   A 202 ? 0.49144 0.39287 0.38711 -0.06582 -0.01671 0.01963  279 THR   A OG1 
1567 C  CG2 . THR   A 202 ? 0.48821 0.37376 0.36372 -0.08026 -0.02279 0.02370  279 THR   A CG2 
1568 N  N   . ILE   A 203 ? 0.51253 0.40540 0.40602 -0.05879 -0.01417 0.01380  280 ILE   A N   
1569 C  CA  . ILE   A 203 ? 0.47972 0.37154 0.37668 -0.05072 -0.01046 0.00995  280 ILE   A CA  
1570 C  C   . ILE   A 203 ? 0.49695 0.37317 0.38156 -0.05049 -0.00961 0.00737  280 ILE   A C   
1571 O  O   . ILE   A 203 ? 0.49115 0.36134 0.37405 -0.04425 -0.00624 0.00420  280 ILE   A O   
1572 C  CB  . ILE   A 203 ? 0.50805 0.41479 0.41883 -0.04760 -0.01000 0.01048  280 ILE   A CB  
1573 C  CG1 . ILE   A 203 ? 0.48474 0.39194 0.40023 -0.03930 -0.00625 0.00682  280 ILE   A CG1 
1574 C  CG2 . ILE   A 203 ? 0.47584 0.38298 0.38502 -0.05201 -0.01252 0.01203  280 ILE   A CG2 
1575 C  CD1 . ILE   A 203 ? 0.54833 0.45613 0.46625 -0.03477 -0.00389 0.00549  280 ILE   A CD1 
1576 N  N   . GLY   A 204 ? 0.51634 0.38568 0.39191 -0.05733 -0.01254 0.00890  281 GLY   A N   
1577 C  CA  . GLY   A 204 ? 0.51581 0.36911 0.37813 -0.05761 -0.01160 0.00654  281 GLY   A CA  
1578 C  C   . GLY   A 204 ? 0.54448 0.38147 0.39392 -0.05646 -0.00963 0.00459  281 GLY   A C   
1579 O  O   . GLY   A 204 ? 0.51926 0.34251 0.35828 -0.05453 -0.00749 0.00213  281 GLY   A O   
1580 N  N   . ASN   A 205 ? 0.53262 0.37050 0.38228 -0.05747 -0.01011 0.00578  282 ASN   A N   
1581 C  CA  . ASN   A 205 ? 0.54658 0.36969 0.38513 -0.05551 -0.00795 0.00406  282 ASN   A CA  
1582 C  C   . ASN   A 205 ? 0.59299 0.41485 0.43539 -0.04588 -0.00319 0.00088  282 ASN   A C   
1583 O  O   . ASN   A 205 ? 0.59574 0.40344 0.42782 -0.04325 -0.00072 -0.00078 282 ASN   A O   
1584 C  CB  . ASN   A 205 ? 0.57003 0.39612 0.40959 -0.05833 -0.00950 0.00618  282 ASN   A CB  
1585 C  CG  . ASN   A 205 ? 0.56878 0.39586 0.40405 -0.06822 -0.01429 0.00986  282 ASN   A CG  
1586 O  OD1 . ASN   A 205 ? 0.61309 0.43585 0.44206 -0.07361 -0.01667 0.01081  282 ASN   A OD1 
1587 N  ND2 . ASN   A 205 ? 0.55232 0.38511 0.39074 -0.07092 -0.01584 0.01221  282 ASN   A ND2 
1588 N  N   . LEU   A 206 ? 0.53504 0.37122 0.39185 -0.04061 -0.00185 0.00027  283 LEU   A N   
1589 C  CA  . LEU   A 206 ? 0.54118 0.37817 0.40297 -0.03194 0.00220  -0.00212 283 LEU   A CA  
1590 C  C   . LEU   A 206 ? 0.53607 0.36464 0.39243 -0.02875 0.00461  -0.00431 283 LEU   A C   
1591 O  O   . LEU   A 206 ? 0.51417 0.35105 0.37898 -0.02544 0.00554  -0.00516 283 LEU   A O   
1592 C  CB  . LEU   A 206 ? 0.51389 0.36857 0.39207 -0.02811 0.00253  -0.00184 283 LEU   A CB  
1593 C  CG  . LEU   A 206 ? 0.55474 0.42030 0.44030 -0.03081 0.00051  0.00044  283 LEU   A CG  
1594 C  CD1 . LEU   A 206 ? 0.46323 0.34314 0.36306 -0.02536 0.00203  -0.00009 283 LEU   A CD1 
1595 C  CD2 . LEU   A 206 ? 0.49854 0.35584 0.37658 -0.03213 0.00048  0.00099  283 LEU   A CD2 
1596 N  N   . SER   A 207 ? 0.51252 0.32377 0.35405 -0.02962 0.00588  -0.00520 284 SER   A N   
1597 C  CA  . SER   A 207 ? 0.55226 0.35386 0.38659 -0.02738 0.00826  -0.00708 284 SER   A CA  
1598 C  C   . SER   A 207 ? 0.56598 0.36872 0.40561 -0.01819 0.01283  -0.00892 284 SER   A C   
1599 O  O   . SER   A 207 ? 0.56313 0.35830 0.39740 -0.01545 0.01543  -0.01040 284 SER   A O   
1600 C  CB  . SER   A 207 ? 0.54431 0.32577 0.35974 -0.03148 0.00838  -0.00740 284 SER   A CB  
1601 O  OG  . SER   A 207 ? 0.58742 0.36061 0.39730 -0.02927 0.01007  -0.00744 284 SER   A OG  
1602 N  N   . SER   A 208 ? 0.52233 0.33440 0.37214 -0.01359 0.01383  -0.00864 285 SER   A N   
1603 C  CA  . SER   A 208 ? 0.50296 0.31848 0.35945 -0.00537 0.01759  -0.00977 285 SER   A CA  
1604 C  C   . SER   A 208 ? 0.50085 0.33412 0.37327 -0.00297 0.01687  -0.00967 285 SER   A C   
1605 O  O   . SER   A 208 ? 0.48527 0.32271 0.36397 0.00324  0.01954  -0.01039 285 SER   A O   
1606 C  CB  . SER   A 208 ? 0.53262 0.34363 0.38743 -0.00134 0.01963  -0.00938 285 SER   A CB  
1607 O  OG  . SER   A 208 ? 0.62987 0.42331 0.46923 -0.00319 0.02059  -0.00948 285 SER   A OG  
1608 N  N   . LEU   A 209 ? 0.52998 0.37358 0.40885 -0.00770 0.01344  -0.00855 286 LEU   A N   
1609 C  CA  . LEU   A 209 ? 0.48971 0.34917 0.38262 -0.00590 0.01274  -0.00843 286 LEU   A CA  
1610 C  C   . LEU   A 209 ? 0.46683 0.32755 0.36213 -0.00294 0.01429  -0.00972 286 LEU   A C   
1611 O  O   . LEU   A 209 ? 0.47176 0.32738 0.36118 -0.00629 0.01340  -0.00991 286 LEU   A O   
1612 C  CB  . LEU   A 209 ? 0.46860 0.33640 0.36555 -0.01202 0.00905  -0.00670 286 LEU   A CB  
1613 C  CG  . LEU   A 209 ? 0.44283 0.32665 0.35364 -0.01077 0.00823  -0.00621 286 LEU   A CG  
1614 C  CD1 . LEU   A 209 ? 0.45920 0.35043 0.37794 -0.00657 0.00947  -0.00632 286 LEU   A CD1 
1615 C  CD2 . LEU   A 209 ? 0.42834 0.31869 0.34155 -0.01697 0.00487  -0.00399 286 LEU   A CD2 
1616 N  N   . SER   A 210 ? 0.46587 0.33334 0.36955 0.00304  0.01645  -0.01045 287 SER   A N   
1617 C  CA  . SER   A 210 ? 0.49021 0.36011 0.39713 0.00585  0.01785  -0.01149 287 SER   A CA  
1618 C  C   . SER   A 210 ? 0.47361 0.35814 0.39340 0.00700  0.01678  -0.01139 287 SER   A C   
1619 O  O   . SER   A 210 ? 0.47518 0.36241 0.39752 0.00758  0.01698  -0.01200 287 SER   A O   
1620 C  CB  . SER   A 210 ? 0.51436 0.37827 0.41890 0.01207  0.02171  -0.01226 287 SER   A CB  
1621 O  OG  . SER   A 210 ? 0.58963 0.45787 0.49948 0.01572  0.02260  -0.01165 287 SER   A OG  
1622 N  N   . ARG   A 211 ? 0.45832 0.35161 0.38556 0.00729  0.01579  -0.01066 288 ARG   A N   
1623 C  CA  . ARG   A 211 ? 0.46992 0.37604 0.40832 0.00822  0.01492  -0.01056 288 ARG   A CA  
1624 C  C   . ARG   A 211 ? 0.44390 0.35609 0.38541 0.00425  0.01256  -0.00918 288 ARG   A C   
1625 O  O   . ARG   A 211 ? 0.41606 0.32738 0.35640 0.00388  0.01244  -0.00855 288 ARG   A O   
1626 C  CB  . ARG   A 211 ? 0.49090 0.40206 0.43576 0.01357  0.01672  -0.01101 288 ARG   A CB  
1627 C  CG  . ARG   A 211 ? 0.56751 0.47795 0.51360 0.01752  0.01872  -0.01190 288 ARG   A CG  
1628 C  CD  . ARG   A 211 ? 0.60345 0.51885 0.55550 0.02215  0.02010  -0.01175 288 ARG   A CD  
1629 N  NE  . ARG   A 211 ? 0.69991 0.60757 0.64666 0.02516  0.02225  -0.01133 288 ARG   A NE  
1630 C  CZ  . ARG   A 211 ? 0.78765 0.69167 0.73285 0.02885  0.02468  -0.01139 288 ARG   A CZ  
1631 N  NH1 . ARG   A 211 ? 0.74212 0.64958 0.69059 0.02979  0.02511  -0.01198 288 ARG   A NH1 
1632 N  NH2 . ARG   A 211 ? 0.82026 0.71705 0.76055 0.03182  0.02688  -0.01065 288 ARG   A NH2 
1633 N  N   . LEU   A 212 ? 0.41235 0.33090 0.35799 0.00142  0.01080  -0.00846 289 LEU   A N   
1634 C  CA  . LEU   A 212 ? 0.41360 0.33886 0.36283 -0.00235 0.00875  -0.00661 289 LEU   A CA  
1635 C  C   . LEU   A 212 ? 0.43995 0.37676 0.39958 -0.00064 0.00871  -0.00641 289 LEU   A C   
1636 O  O   . LEU   A 212 ? 0.43421 0.37359 0.39605 -0.00133 0.00806  -0.00629 289 LEU   A O   
1637 C  CB  . LEU   A 212 ? 0.37907 0.29993 0.32197 -0.00830 0.00639  -0.00508 289 LEU   A CB  
1638 C  CG  . LEU   A 212 ? 0.41185 0.34097 0.35930 -0.01255 0.00410  -0.00242 289 LEU   A CG  
1639 C  CD1 . LEU   A 212 ? 0.35756 0.28880 0.30628 -0.01232 0.00444  -0.00173 289 LEU   A CD1 
1640 C  CD2 . LEU   A 212 ? 0.35765 0.28250 0.29858 -0.01902 0.00133  -0.00045 289 LEU   A CD2 
1641 N  N   . GLY   A 213 ? 0.43032 0.37349 0.39577 0.00156  0.00948  -0.00636 290 GLY   A N   
1642 C  CA  . GLY   A 213 ? 0.36552 0.31844 0.33981 0.00339  0.00982  -0.00625 290 GLY   A CA  
1643 C  C   . GLY   A 213 ? 0.34468 0.30494 0.32324 0.00060  0.00874  -0.00399 290 GLY   A C   
1644 O  O   . GLY   A 213 ? 0.37805 0.33975 0.35671 -0.00007 0.00889  -0.00318 290 GLY   A O   
1645 N  N   . LEU   A 214 ? 0.35757 0.32290 0.33996 -0.00096 0.00775  -0.00267 291 LEU   A N   
1646 C  CA  . LEU   A 214 ? 0.34160 0.31480 0.32880 -0.00347 0.00685  0.00014  291 LEU   A CA  
1647 C  C   . LEU   A 214 ? 0.36120 0.34291 0.35678 -0.00070 0.00790  0.00047  291 LEU   A C   
1648 O  O   . LEU   A 214 ? 0.35194 0.34085 0.35244 -0.00230 0.00734  0.00318  291 LEU   A O   
1649 C  CB  . LEU   A 214 ? 0.35546 0.32691 0.33893 -0.00894 0.00424  0.00254  291 LEU   A CB  
1650 C  CG  . LEU   A 214 ? 0.35390 0.31585 0.32781 -0.01235 0.00310  0.00248  291 LEU   A CG  
1651 C  CD1 . LEU   A 214 ? 0.33102 0.28890 0.29941 -0.01773 0.00044  0.00421  291 LEU   A CD1 
1652 C  CD2 . LEU   A 214 ? 0.36281 0.32768 0.33743 -0.01392 0.00302  0.00415  291 LEU   A CD2 
1653 N  N   . ARG   A 215 ? 0.34454 0.32553 0.34178 0.00345  0.00947  -0.00200 292 ARG   A N   
1654 C  CA  . ARG   A 215 ? 0.34771 0.33508 0.35165 0.00608  0.01047  -0.00195 292 ARG   A CA  
1655 C  C   . ARG   A 215 ? 0.35035 0.34438 0.35923 0.00728  0.01195  -0.00065 292 ARG   A C   
1656 O  O   . ARG   A 215 ? 0.36802 0.36088 0.37523 0.00786  0.01288  -0.00123 292 ARG   A O   
1657 C  CB  . ARG   A 215 ? 0.37487 0.35915 0.37847 0.00981  0.01166  -0.00485 292 ARG   A CB  
1658 C  CG  . ARG   A 215 ? 0.43148 0.41756 0.43726 0.01306  0.01354  -0.00614 292 ARG   A CG  
1659 C  CD  . ARG   A 215 ? 0.39433 0.37513 0.39660 0.01505  0.01408  -0.00835 292 ARG   A CD  
1660 N  NE  . ARG   A 215 ? 0.40705 0.38636 0.40979 0.01689  0.01415  -0.00977 292 ARG   A NE  
1661 C  CZ  . ARG   A 215 ? 0.42635 0.40392 0.42865 0.01938  0.01489  -0.01132 292 ARG   A CZ  
1662 N  NH1 . ARG   A 215 ? 0.40592 0.38301 0.40734 0.02037  0.01553  -0.01171 292 ARG   A NH1 
1663 N  NH2 . ARG   A 215 ? 0.46586 0.44247 0.46869 0.02069  0.01486  -0.01223 292 ARG   A NH2 
1664 N  N   . TYR   A 216 ? 0.34167 0.34259 0.35651 0.00776  0.01232  0.00129  293 TYR   A N   
1665 C  CA  . TYR   A 216 ? 0.34691 0.35429 0.36671 0.00954  0.01435  0.00274  293 TYR   A CA  
1666 C  C   . TYR   A 216 ? 0.35639 0.36667 0.37602 0.00651  0.01390  0.00543  293 TYR   A C   
1667 O  O   . TYR   A 216 ? 0.35784 0.36799 0.37650 0.00743  0.01537  0.00494  293 TYR   A O   
1668 C  CB  . TYR   A 216 ? 0.33440 0.33957 0.35346 0.01337  0.01664  -0.00007 293 TYR   A CB  
1669 C  CG  . TYR   A 216 ? 0.39301 0.39846 0.41454 0.01668  0.01776  -0.00163 293 TYR   A CG  
1670 C  CD1 . TYR   A 216 ? 0.39307 0.39429 0.41256 0.01700  0.01660  -0.00352 293 TYR   A CD1 
1671 C  CD2 . TYR   A 216 ? 0.39677 0.40630 0.42224 0.01953  0.02017  -0.00112 293 TYR   A CD2 
1672 C  CE1 . TYR   A 216 ? 0.42957 0.43095 0.45108 0.01968  0.01744  -0.00481 293 TYR   A CE1 
1673 C  CE2 . TYR   A 216 ? 0.43808 0.44690 0.46496 0.02235  0.02113  -0.00255 293 TYR   A CE2 
1674 C  CZ  . TYR   A 216 ? 0.46311 0.46801 0.48810 0.02223  0.01958  -0.00437 293 TYR   A CZ  
1675 O  OH  . TYR   A 216 ? 0.46228 0.46641 0.48846 0.02471  0.02037  -0.00567 293 TYR   A OH  
1676 N  N   . ASN   A 217 ? 0.33677 0.34983 0.35723 0.00261  0.01172  0.00851  294 ASN   A N   
1677 C  CA  . ASN   A 217 ? 0.35206 0.36903 0.37303 -0.00093 0.01089  0.01185  294 ASN   A CA  
1678 C  C   . ASN   A 217 ? 0.37511 0.40081 0.40254 -0.00266 0.00997  0.01622  294 ASN   A C   
1679 O  O   . ASN   A 217 ? 0.36770 0.39648 0.39952 -0.00032 0.01054  0.01644  294 ASN   A O   
1680 C  CB  . ASN   A 217 ? 0.32645 0.33582 0.33948 -0.00515 0.00845  0.01129  294 ASN   A CB  
1681 C  CG  . ASN   A 217 ? 0.33526 0.33835 0.34342 -0.00332 0.00975  0.00824  294 ASN   A CG  
1682 O  OD1 . ASN   A 217 ? 0.33960 0.34561 0.34923 -0.00246 0.01129  0.00880  294 ASN   A OD1 
1683 N  ND2 . ASN   A 217 ? 0.30653 0.30124 0.30906 -0.00259 0.00927  0.00525  294 ASN   A ND2 
1684 N  N   . ARG   A 218 ? 0.37340 0.40355 0.40173 -0.00683 0.00850  0.02009  295 ARG   A N   
1685 C  CA  . ARG   A 218 ? 0.35354 0.39324 0.38869 -0.00880 0.00744  0.02512  295 ARG   A CA  
1686 C  C   . ARG   A 218 ? 0.32398 0.36180 0.35521 -0.01538 0.00313  0.02757  295 ARG   A C   
1687 O  O   . ARG   A 218 ? 0.35679 0.40245 0.39223 -0.01901 0.00143  0.03265  295 ARG   A O   
1688 C  CB  . ARG   A 218 ? 0.34812 0.39702 0.38930 -0.00812 0.00953  0.02877  295 ARG   A CB  
1689 C  CG  . ARG   A 218 ? 0.39455 0.44572 0.43972 -0.00157 0.01412  0.02692  295 ARG   A CG  
1690 C  CD  . ARG   A 218 ? 0.38768 0.44852 0.43914 -0.00067 0.01664  0.03108  295 ARG   A CD  
1691 N  NE  . ARG   A 218 ? 0.54430 0.60337 0.59158 -0.00368 0.01618  0.03130  295 ARG   A NE  
1692 C  CZ  . ARG   A 218 ? 0.52421 0.59086 0.57547 -0.00426 0.01777  0.03505  295 ARG   A CZ  
1693 N  NH1 . ARG   A 218 ? 0.40059 0.47768 0.46054 -0.00184 0.02015  0.03927  295 ARG   A NH1 
1694 N  NH2 . ARG   A 218 ? 0.43651 0.50023 0.48295 -0.00719 0.01711  0.03476  295 ARG   A NH2 
1695 N  N   . LEU   A 219 ? 0.36405 0.39135 0.38693 -0.01703 0.00140  0.02418  296 LEU   A N   
1696 C  CA  . LEU   A 219 ? 0.36963 0.39261 0.38648 -0.02346 -0.00256 0.02592  296 LEU   A CA  
1697 C  C   . LEU   A 219 ? 0.36676 0.39616 0.38863 -0.02536 -0.00457 0.02942  296 LEU   A C   
1698 O  O   . LEU   A 219 ? 0.41655 0.44743 0.44230 -0.02143 -0.00329 0.02806  296 LEU   A O   
1699 C  CB  . LEU   A 219 ? 0.33397 0.34371 0.34077 -0.02358 -0.00309 0.02124  296 LEU   A CB  
1700 C  CG  . LEU   A 219 ? 0.36402 0.36588 0.36465 -0.02201 -0.00154 0.01783  296 LEU   A CG  
1701 C  CD1 . LEU   A 219 ? 0.36011 0.34986 0.35193 -0.02155 -0.00179 0.01387  296 LEU   A CD1 
1702 C  CD2 . LEU   A 219 ? 0.35281 0.35451 0.35012 -0.02672 -0.00302 0.02040  296 LEU   A CD2 
1703 N  N   . SER   A 220 ? 0.36612 0.39941 0.38785 -0.03165 -0.00791 0.03421  297 SER   A N   
1704 C  CA  . SER   A 220 ? 0.41902 0.45840 0.44497 -0.03448 -0.01050 0.03821  297 SER   A CA  
1705 C  C   . SER   A 220 ? 0.40530 0.43592 0.42147 -0.04120 -0.01470 0.03834  297 SER   A C   
1706 O  O   . SER   A 220 ? 0.44443 0.47826 0.46233 -0.04414 -0.01730 0.04124  297 SER   A O   
1707 C  CB  . SER   A 220 ? 0.40541 0.45877 0.44089 -0.03637 -0.01109 0.04489  297 SER   A CB  
1708 O  OG  . SER   A 220 ? 0.48501 0.53794 0.51649 -0.04191 -0.01309 0.04734  297 SER   A OG  
1709 N  N   . ALA   A 221 ? 0.44467 0.46360 0.45008 -0.04346 -0.01524 0.03515  298 ALA   A N   
1710 C  CA  . ALA   A 221 ? 0.40484 0.41338 0.39908 -0.04974 -0.01876 0.03489  298 ALA   A CA  
1711 C  C   . ALA   A 221 ? 0.44289 0.43750 0.42627 -0.04861 -0.01730 0.02972  298 ALA   A C   
1712 O  O   . ALA   A 221 ? 0.42951 0.42417 0.41419 -0.04504 -0.01469 0.02788  298 ALA   A O   
1713 C  CB  . ALA   A 221 ? 0.41120 0.42408 0.40434 -0.05797 -0.02295 0.04079  298 ALA   A CB  
1714 N  N   . ILE   A 222 ? 0.42171 0.40427 0.39429 -0.05144 -0.01881 0.02753  299 ILE   A N   
1715 C  CA  . ILE   A 222 ? 0.44622 0.41471 0.40749 -0.05088 -0.01756 0.02331  299 ILE   A CA  
1716 C  C   . ILE   A 222 ? 0.50894 0.46920 0.45902 -0.05915 -0.02115 0.02551  299 ILE   A C   
1717 O  O   . ILE   A 222 ? 0.47994 0.44069 0.42743 -0.06530 -0.02476 0.02875  299 ILE   A O   
1718 C  CB  . ILE   A 222 ? 0.44877 0.40814 0.40512 -0.04688 -0.01563 0.01868  299 ILE   A CB  
1719 C  CG1 . ILE   A 222 ? 0.48689 0.45443 0.45404 -0.03933 -0.01248 0.01680  299 ILE   A CG1 
1720 C  CG2 . ILE   A 222 ? 0.48614 0.43166 0.43150 -0.04578 -0.01396 0.01490  299 ILE   A CG2 
1721 C  CD1 . ILE   A 222 ? 0.43527 0.40671 0.40781 -0.03402 -0.00932 0.01518  299 ILE   A CD1 
1722 N  N   . PRO   A 223 ? 0.48620 0.43861 0.42911 -0.05989 -0.02049 0.02409  300 PRO   A N   
1723 C  CA  . PRO   A 223 ? 0.47691 0.41951 0.40750 -0.06792 -0.02385 0.02589  300 PRO   A CA  
1724 C  C   . PRO   A 223 ? 0.51739 0.44480 0.43494 -0.06970 -0.02433 0.02305  300 PRO   A C   
1725 O  O   . PRO   A 223 ? 0.50230 0.42172 0.41637 -0.06400 -0.02100 0.01845  300 PRO   A O   
1726 C  CB  . PRO   A 223 ? 0.46798 0.40581 0.39494 -0.06660 -0.02217 0.02443  300 PRO   A CB  
1727 C  CG  . PRO   A 223 ? 0.49546 0.44337 0.43456 -0.05861 -0.01841 0.02281  300 PRO   A CG  
1728 C  CD  . PRO   A 223 ? 0.44786 0.39961 0.39311 -0.05369 -0.01680 0.02094  300 PRO   A CD  
1729 N  N   . ARG   A 224 ? 0.54051 0.46413 0.45078 -0.07778 -0.02847 0.02609  301 ARG   A N   
1730 C  CA  . ARG   A 224 ? 0.56968 0.47718 0.46537 -0.08047 -0.02904 0.02362  301 ARG   A CA  
1731 C  C   . ARG   A 224 ? 0.51404 0.40541 0.39736 -0.07839 -0.02638 0.01952  301 ARG   A C   
1732 O  O   . ARG   A 224 ? 0.57258 0.45097 0.44616 -0.07642 -0.02446 0.01595  301 ARG   A O   
1733 C  CB  . ARG   A 224 ? 0.60918 0.51454 0.49763 -0.09079 -0.03443 0.02809  301 ARG   A CB  
1734 C  CG  . ARG   A 224 ? 0.69615 0.58172 0.56545 -0.09582 -0.03554 0.02615  301 ARG   A CG  
1735 C  CD  . ARG   A 224 ? 0.86551 0.74948 0.72745 -0.10703 -0.04125 0.03126  301 ARG   A CD  
1736 N  NE  . ARG   A 224 ? 0.97985 0.84337 0.82154 -0.11293 -0.04267 0.02965  301 ARG   A NE  
1737 C  CZ  . ARG   A 224 ? 0.91120 0.76682 0.74515 -0.11486 -0.04338 0.02853  301 ARG   A CZ  
1738 N  NH1 . ARG   A 224 ? 0.89865 0.76508 0.74352 -0.11136 -0.04294 0.02881  301 ARG   A NH1 
1739 N  NH2 . ARG   A 224 ? 0.97124 0.80700 0.78544 -0.12036 -0.04439 0.02703  301 ARG   A NH2 
1740 N  N   . SER   A 225 ? 0.51766 0.40988 0.40159 -0.07830 -0.02593 0.02008  302 SER   A N   
1741 C  CA  . SER   A 225 ? 0.55122 0.42913 0.42471 -0.07554 -0.02315 0.01645  302 SER   A CA  
1742 C  C   . SER   A 225 ? 0.53609 0.41188 0.41285 -0.06597 -0.01820 0.01177  302 SER   A C   
1743 O  O   . SER   A 225 ? 0.51995 0.38173 0.38637 -0.06343 -0.01567 0.00864  302 SER   A O   
1744 C  CB  . SER   A 225 ? 0.50746 0.38953 0.38377 -0.07640 -0.02344 0.01813  302 SER   A CB  
1745 O  OG  . SER   A 225 ? 0.56283 0.44617 0.43525 -0.08566 -0.02808 0.02272  302 SER   A OG  
1746 N  N   . LEU   A 226 ? 0.49814 0.38744 0.38897 -0.06055 -0.01668 0.01146  303 LEU   A N   
1747 C  CA  . LEU   A 226 ? 0.47241 0.35997 0.36623 -0.05203 -0.01232 0.00738  303 LEU   A CA  
1748 C  C   . LEU   A 226 ? 0.50455 0.37824 0.38709 -0.05151 -0.01103 0.00468  303 LEU   A C   
1749 O  O   . LEU   A 226 ? 0.48112 0.34898 0.36196 -0.04520 -0.00726 0.00138  303 LEU   A O   
1750 C  CB  . LEU   A 226 ? 0.46458 0.36793 0.37410 -0.04716 -0.01127 0.00764  303 LEU   A CB  
1751 C  CG  . LEU   A 226 ? 0.46188 0.36578 0.37627 -0.03850 -0.00701 0.00397  303 LEU   A CG  
1752 C  CD1 . LEU   A 226 ? 0.44969 0.35438 0.36592 -0.03568 -0.00537 0.00341  303 LEU   A CD1 
1753 C  CD2 . LEU   A 226 ? 0.40674 0.32324 0.33388 -0.03435 -0.00616 0.00390  303 LEU   A CD2 
1754 N  N   . ALA   A 227 ? 0.45093 0.31894 0.32525 -0.05824 -0.01408 0.00628  304 ALA   A N   
1755 C  CA  . ALA   A 227 ? 0.50214 0.35557 0.36398 -0.05840 -0.01280 0.00382  304 ALA   A CA  
1756 C  C   . ALA   A 227 ? 0.55142 0.38798 0.39989 -0.05659 -0.00998 0.00117  304 ALA   A C   
1757 O  O   . ALA   A 227 ? 0.59951 0.42490 0.43991 -0.05340 -0.00702 -0.00163 304 ALA   A O   
1758 C  CB  . ALA   A 227 ? 0.49383 0.34327 0.34766 -0.06726 -0.01715 0.00647  304 ALA   A CB  
1759 N  N   . LYS   A 228 ? 0.53491 0.36928 0.38080 -0.05835 -0.01062 0.00214  305 LYS   A N   
1760 C  CA  . LYS   A 228 ? 0.50006 0.31809 0.33303 -0.05671 -0.00802 -0.00001 305 LYS   A CA  
1761 C  C   . LYS   A 228 ? 0.52425 0.34417 0.36363 -0.04727 -0.00333 -0.00263 305 LYS   A C   
1762 O  O   . LYS   A 228 ? 0.51642 0.32319 0.34600 -0.04473 -0.00062 -0.00433 305 LYS   A O   
1763 C  CB  . LYS   A 228 ? 0.55770 0.37168 0.38413 -0.06329 -0.01104 0.00240  305 LYS   A CB  
1764 C  CG  . LYS   A 228 ? 0.55087 0.35660 0.36525 -0.07312 -0.01532 0.00466  305 LYS   A CG  
1765 C  CD  . LYS   A 228 ? 0.52796 0.31606 0.32726 -0.07296 -0.01330 0.00197  305 LYS   A CD  
1766 C  CE  . LYS   A 228 ? 0.60616 0.38639 0.39340 -0.08315 -0.01785 0.00424  305 LYS   A CE  
1767 N  NZ  . LYS   A 228 ? 0.73093 0.52856 0.53100 -0.08664 -0.02169 0.00744  305 LYS   A NZ  
1768 N  N   . CYS   A 229 ? 0.55002 0.38560 0.40520 -0.04210 -0.00233 -0.00276 306 CYS   A N   
1769 C  CA  . CYS   A 229 ? 0.51838 0.35613 0.37964 -0.03356 0.00178  -0.00497 306 CYS   A CA  
1770 C  C   . CYS   A 229 ? 0.49934 0.33135 0.35779 -0.02894 0.00493  -0.00738 306 CYS   A C   
1771 O  O   . CYS   A 229 ? 0.50431 0.34618 0.37326 -0.02438 0.00624  -0.00815 306 CYS   A O   
1772 C  CB  . CYS   A 229 ? 0.46225 0.31789 0.34011 -0.03055 0.00143  -0.00406 306 CYS   A CB  
1773 S  SG  . CYS   A 229 ? 0.53389 0.39766 0.41567 -0.03640 -0.00221 -0.00074 306 CYS   A SG  
1774 N  N   . SER   A 230 ? 0.48181 0.29691 0.32503 -0.03043 0.00620  -0.00847 307 SER   A N   
1775 C  CA  . SER   A 230 ? 0.52409 0.33268 0.36287 -0.02726 0.00898  -0.01041 307 SER   A CA  
1776 C  C   . SER   A 230 ? 0.51812 0.32892 0.36307 -0.01809 0.01366  -0.01221 307 SER   A C   
1777 O  O   . SER   A 230 ? 0.53510 0.34383 0.37943 -0.01471 0.01614  -0.01355 307 SER   A O   
1778 C  CB  . SER   A 230 ? 0.57970 0.36836 0.39929 -0.03122 0.00950  -0.01112 307 SER   A CB  
1779 O  OG  . SER   A 230 ? 0.60363 0.38226 0.41465 -0.03201 0.01001  -0.01093 307 SER   A OG  
1780 N  N   . ALA   A 231 ? 0.48838 0.30389 0.33951 -0.01423 0.01478  -0.01198 308 ALA   A N   
1781 C  CA  . ALA   A 231 ? 0.48380 0.30437 0.34302 -0.00599 0.01852  -0.01301 308 ALA   A CA  
1782 C  C   . ALA   A 231 ? 0.52252 0.36056 0.39769 -0.00369 0.01759  -0.01278 308 ALA   A C   
1783 O  O   . ALA   A 231 ? 0.51687 0.36004 0.39922 0.00262  0.02028  -0.01342 308 ALA   A O   
1784 C  CB  . ALA   A 231 ? 0.49745 0.31608 0.35674 -0.00298 0.01986  -0.01261 308 ALA   A CB  
1785 N  N   . LEU   A 232 ? 0.48422 0.33142 0.36504 -0.00855 0.01393  -0.01165 309 LEU   A N   
1786 C  CA  . LEU   A 232 ? 0.48935 0.35244 0.38489 -0.00613 0.01325  -0.01135 309 LEU   A CA  
1787 C  C   . LEU   A 232 ? 0.45146 0.31635 0.35051 -0.00139 0.01572  -0.01273 309 LEU   A C   
1788 O  O   . LEU   A 232 ? 0.47363 0.33191 0.36612 -0.00285 0.01609  -0.01334 309 LEU   A O   
1789 C  CB  . LEU   A 232 ? 0.46080 0.33242 0.36103 -0.01183 0.00933  -0.00962 309 LEU   A CB  
1790 C  CG  . LEU   A 232 ? 0.44287 0.32105 0.34750 -0.01445 0.00719  -0.00785 309 LEU   A CG  
1791 C  CD1 . LEU   A 232 ? 0.43929 0.32526 0.34784 -0.02011 0.00357  -0.00560 309 LEU   A CD1 
1792 C  CD2 . LEU   A 232 ? 0.43435 0.32256 0.35002 -0.00900 0.00878  -0.00829 309 LEU   A CD2 
1793 N  N   . GLU   A 233 ? 0.46248 0.33593 0.37135 0.00408  0.01742  -0.01311 310 GLU   A N   
1794 C  CA  . GLU   A 233 ? 0.48498 0.36229 0.39890 0.00840  0.01943  -0.01403 310 GLU   A CA  
1795 C  C   . GLU   A 233 ? 0.46473 0.35599 0.39082 0.00858  0.01769  -0.01369 310 GLU   A C   
1796 O  O   . GLU   A 233 ? 0.43652 0.33075 0.36576 0.01012  0.01833  -0.01425 310 GLU   A O   
1797 C  CB  . GLU   A 233 ? 0.47430 0.34980 0.38934 0.01481  0.02299  -0.01445 310 GLU   A CB  
1798 C  CG  . GLU   A 233 ? 0.53749 0.39805 0.44006 0.01604  0.02579  -0.01485 310 GLU   A CG  
1799 C  CD  . GLU   A 233 ? 0.57986 0.43936 0.48425 0.02268  0.02942  -0.01461 310 GLU   A CD  
1800 O  OE1 . GLU   A 233 ? 0.61978 0.48769 0.53285 0.02667  0.03061  -0.01447 310 GLU   A OE1 
1801 O  OE2 . GLU   A 233 ? 0.70466 0.55498 0.60180 0.02384  0.03102  -0.01428 310 GLU   A OE2 
1802 N  N   . GLU   A 234 ? 0.46783 0.36713 0.40030 0.00709  0.01571  -0.01273 311 GLU   A N   
1803 C  CA  . GLU   A 234 ? 0.42226 0.33405 0.36582 0.00775  0.01450  -0.01238 311 GLU   A CA  
1804 C  C   . GLU   A 234 ? 0.43380 0.35088 0.38006 0.00371  0.01191  -0.01084 311 GLU   A C   
1805 O  O   . GLU   A 234 ? 0.46908 0.38455 0.41351 0.00307  0.01177  -0.01031 311 GLU   A O   
1806 C  CB  . GLU   A 234 ? 0.46364 0.38102 0.41417 0.01298  0.01632  -0.01293 311 GLU   A CB  
1807 C  CG  . GLU   A 234 ? 0.51838 0.42988 0.46561 0.01734  0.01926  -0.01371 311 GLU   A CG  
1808 C  CD  . GLU   A 234 ? 0.64554 0.56322 0.59977 0.02171  0.02045  -0.01357 311 GLU   A CD  
1809 O  OE1 . GLU   A 234 ? 0.66209 0.58896 0.62418 0.02172  0.01921  -0.01346 311 GLU   A OE1 
1810 O  OE2 . GLU   A 234 ? 0.72213 0.63531 0.67373 0.02504  0.02259  -0.01337 311 GLU   A OE2 
1811 N  N   . LEU   A 235 ? 0.40753 0.33102 0.35819 0.00106  0.00994  -0.00987 312 LEU   A N   
1812 C  CA  . LEU   A 235 ? 0.40416 0.33352 0.35789 -0.00292 0.00755  -0.00781 312 LEU   A CA  
1813 C  C   . LEU   A 235 ? 0.44657 0.38730 0.41079 -0.00139 0.00719  -0.00726 312 LEU   A C   
1814 O  O   . LEU   A 235 ? 0.41514 0.35752 0.38110 -0.00142 0.00679  -0.00737 312 LEU   A O   
1815 C  CB  . LEU   A 235 ? 0.43775 0.36170 0.38420 -0.00882 0.00518  -0.00636 312 LEU   A CB  
1816 C  CG  . LEU   A 235 ? 0.39190 0.32301 0.34204 -0.01366 0.00226  -0.00341 312 LEU   A CG  
1817 C  CD1 . LEU   A 235 ? 0.39641 0.32883 0.34679 -0.01461 0.00204  -0.00239 312 LEU   A CD1 
1818 C  CD2 . LEU   A 235 ? 0.39015 0.31511 0.33234 -0.01958 -0.00025 -0.00201 312 LEU   A CD2 
1819 N  N   . ASN   A 236 ? 0.43094 0.37878 0.40158 0.00016  0.00756  -0.00677 313 ASN   A N   
1820 C  CA  . ASN   A 236 ? 0.39507 0.35262 0.37492 0.00220  0.00777  -0.00641 313 ASN   A CA  
1821 C  C   . ASN   A 236 ? 0.36932 0.33369 0.35317 -0.00080 0.00630  -0.00374 313 ASN   A C   
1822 O  O   . ASN   A 236 ? 0.38196 0.34763 0.36607 -0.00120 0.00654  -0.00307 313 ASN   A O   
1823 C  CB  . ASN   A 236 ? 0.38124 0.34120 0.36502 0.00689  0.00981  -0.00805 313 ASN   A CB  
1824 C  CG  . ASN   A 236 ? 0.35640 0.32414 0.34796 0.00918  0.01028  -0.00811 313 ASN   A CG  
1825 O  OD1 . ASN   A 236 ? 0.37010 0.34350 0.36576 0.00762  0.00939  -0.00640 313 ASN   A OD1 
1826 N  ND2 . ASN   A 236 ? 0.38119 0.34915 0.37466 0.01284  0.01168  -0.00983 313 ASN   A ND2 
1827 N  N   . LEU   A 237 ? 0.34892 0.31801 0.33613 -0.00285 0.00484  -0.00194 314 LEU   A N   
1828 C  CA  . LEU   A 237 ? 0.33103 0.30825 0.32357 -0.00519 0.00367  0.00122  314 LEU   A CA  
1829 C  C   . LEU   A 237 ? 0.35607 0.34209 0.35765 -0.00199 0.00473  0.00178  314 LEU   A C   
1830 O  O   . LEU   A 237 ? 0.31310 0.30635 0.31985 -0.00363 0.00377  0.00484  314 LEU   A O   
1831 C  CB  . LEU   A 237 ? 0.32557 0.30143 0.31447 -0.01088 0.00076  0.00384  314 LEU   A CB  
1832 C  CG  . LEU   A 237 ? 0.37894 0.34458 0.35723 -0.01501 -0.00066 0.00357  314 LEU   A CG  
1833 C  CD1 . LEU   A 237 ? 0.41025 0.37531 0.38562 -0.02060 -0.00374 0.00619  314 LEU   A CD1 
1834 C  CD2 . LEU   A 237 ? 0.36241 0.32726 0.33851 -0.01673 -0.00077 0.00451  314 LEU   A CD2 
1835 N  N   . GLU   A 238 ? 0.32817 0.31365 0.33163 0.00251  0.00673  -0.00085 315 GLU   A N   
1836 C  CA  . GLU   A 238 ? 0.34734 0.33947 0.35800 0.00547  0.00779  -0.00054 315 GLU   A CA  
1837 C  C   . GLU   A 238 ? 0.36132 0.36093 0.37754 0.00582  0.00861  0.00180  315 GLU   A C   
1838 O  O   . GLU   A 238 ? 0.37580 0.37508 0.39075 0.00572  0.00936  0.00176  315 GLU   A O   
1839 C  CB  . GLU   A 238 ? 0.36161 0.35134 0.37242 0.00975  0.00968  -0.00366 315 GLU   A CB  
1840 C  CG  . GLU   A 238 ? 0.36537 0.36030 0.38226 0.01273  0.01082  -0.00365 315 GLU   A CG  
1841 C  CD  . GLU   A 238 ? 0.52686 0.51988 0.54367 0.01642  0.01261  -0.00634 315 GLU   A CD  
1842 O  OE1 . GLU   A 238 ? 0.43759 0.42832 0.45195 0.01703  0.01338  -0.00740 315 GLU   A OE1 
1843 O  OE2 . GLU   A 238 ? 0.58438 0.57816 0.60340 0.01844  0.01307  -0.00721 315 GLU   A OE2 
1844 N  N   . ASN   A 239 ? 0.31754 0.32394 0.33987 0.00620  0.00854  0.00416  316 ASN   A N   
1845 C  CA  . ASN   A 239 ? 0.29540 0.30961 0.32402 0.00758  0.01003  0.00665  316 ASN   A CA  
1846 C  C   . ASN   A 239 ? 0.35805 0.37499 0.38625 0.00402  0.00906  0.00951  316 ASN   A C   
1847 O  O   . ASN   A 239 ? 0.33189 0.34994 0.36030 0.00504  0.01068  0.00939  316 ASN   A O   
1848 C  CB  . ASN   A 239 ? 0.36319 0.37701 0.39301 0.01220  0.01305  0.00421  316 ASN   A CB  
1849 C  CG  . ASN   A 239 ? 0.39137 0.41255 0.42766 0.01467  0.01529  0.00655  316 ASN   A CG  
1850 O  OD1 . ASN   A 239 ? 0.35458 0.38202 0.39583 0.01373  0.01470  0.01008  316 ASN   A OD1 
1851 N  ND2 . ASN   A 239 ? 0.39360 0.41391 0.42965 0.01788  0.01796  0.00480  316 ASN   A ND2 
1852 N  N   . ASN   A 240 ? 0.33266 0.35068 0.36000 -0.00055 0.00622  0.01228  317 ASN   A N   
1853 C  CA  . ASN   A 240 ? 0.34801 0.37105 0.37677 -0.00446 0.00488  0.01629  317 ASN   A CA  
1854 C  C   . ASN   A 240 ? 0.33801 0.36937 0.37322 -0.00610 0.00342  0.02077  317 ASN   A C   
1855 O  O   . ASN   A 240 ? 0.33419 0.36821 0.37386 -0.00284 0.00447  0.02056  317 ASN   A O   
1856 C  CB  . ASN   A 240 ? 0.34008 0.35569 0.36031 -0.00945 0.00237  0.01586  317 ASN   A CB  
1857 C  CG  . ASN   A 240 ? 0.36497 0.37438 0.38017 -0.00790 0.00396  0.01270  317 ASN   A CG  
1858 O  OD1 . ASN   A 240 ? 0.38500 0.39730 0.40115 -0.00859 0.00459  0.01412  317 ASN   A OD1 
1859 N  ND2 . ASN   A 240 ? 0.33364 0.33491 0.34374 -0.00579 0.00461  0.00873  317 ASN   A ND2 
1860 N  N   . ASN   A 241 ? 0.33865 0.37427 0.37446 -0.01122 0.00090  0.02510  318 ASN   A N   
1861 C  CA  . ASN   A 241 ? 0.35038 0.39465 0.39257 -0.01341 -0.00097 0.03016  318 ASN   A CA  
1862 C  C   . ASN   A 241 ? 0.35536 0.39578 0.39162 -0.02028 -0.00542 0.03189  318 ASN   A C   
1863 O  O   . ASN   A 241 ? 0.37170 0.41867 0.41068 -0.02503 -0.00808 0.03711  318 ASN   A O   
1864 C  CB  . ASN   A 241 ? 0.34944 0.40490 0.39961 -0.01324 0.00015  0.03511  318 ASN   A CB  
1865 C  CG  . ASN   A 241 ? 0.36973 0.42715 0.42364 -0.00692 0.00474  0.03310  318 ASN   A CG  
1866 O  OD1 . ASN   A 241 ? 0.44807 0.50351 0.50337 -0.00187 0.00711  0.03017  318 ASN   A OD1 
1867 N  ND2 . ASN   A 241 ? 0.36363 0.42405 0.41827 -0.00738 0.00601  0.03447  318 ASN   A ND2 
1868 N  N   . ILE   A 242 ? 0.37395 0.40358 0.40178 -0.02096 -0.00623 0.02773  319 ILE   A N   
1869 C  CA  . ILE   A 242 ? 0.37552 0.39851 0.39507 -0.02743 -0.01002 0.02847  319 ILE   A CA  
1870 C  C   . ILE   A 242 ? 0.38027 0.40579 0.40223 -0.02860 -0.01196 0.03029  319 ILE   A C   
1871 O  O   . ILE   A 242 ? 0.40074 0.42508 0.42467 -0.02409 -0.01017 0.02757  319 ILE   A O   
1872 C  CB  . ILE   A 242 ? 0.34918 0.35866 0.35790 -0.02716 -0.00939 0.02318  319 ILE   A CB  
1873 C  CG1 . ILE   A 242 ? 0.35899 0.36642 0.36576 -0.02593 -0.00757 0.02173  319 ILE   A CG1 
1874 C  CG2 . ILE   A 242 ? 0.35952 0.36069 0.35843 -0.03363 -0.01287 0.02376  319 ILE   A CG2 
1875 C  CD1 . ILE   A 242 ? 0.34028 0.33676 0.33957 -0.02311 -0.00571 0.01650  319 ILE   A CD1 
1876 N  N   . SER   A 243 ? 0.33355 0.36272 0.35533 -0.03492 -0.01579 0.03513  320 SER   A N   
1877 C  CA  . SER   A 243 ? 0.34374 0.37474 0.36698 -0.03667 -0.01804 0.03705  320 SER   A CA  
1878 C  C   . SER   A 243 ? 0.38799 0.40793 0.39939 -0.04263 -0.02131 0.03584  320 SER   A C   
1879 O  O   . SER   A 243 ? 0.38445 0.40306 0.39514 -0.04319 -0.02255 0.03582  320 SER   A O   
1880 C  CB  . SER   A 243 ? 0.36977 0.41443 0.40287 -0.03905 -0.02006 0.04413  320 SER   A CB  
1881 O  OG  . SER   A 243 ? 0.37705 0.42243 0.40634 -0.04653 -0.02372 0.04812  320 SER   A OG  
1882 N  N   . THR   A 244 ? 0.36497 0.37624 0.36651 -0.04693 -0.02251 0.03474  321 THR   A N   
1883 C  CA  . THR   A 244 ? 0.37312 0.37131 0.36137 -0.05200 -0.02481 0.03281  321 THR   A CA  
1884 C  C   . THR   A 244 ? 0.42823 0.41548 0.40651 -0.05281 -0.02372 0.02952  321 THR   A C   
1885 O  O   . THR   A 244 ? 0.44152 0.43255 0.42281 -0.05206 -0.02273 0.03034  321 THR   A O   
1886 C  CB  . THR   A 244 ? 0.35359 0.35353 0.33875 -0.06070 -0.02998 0.03816  321 THR   A CB  
1887 O  OG1 . THR   A 244 ? 0.39451 0.39972 0.38118 -0.06499 -0.03179 0.04226  321 THR   A OG1 
1888 C  CG2 . THR   A 244 ? 0.34618 0.35690 0.34090 -0.06047 -0.03150 0.04209  321 THR   A CG2 
1889 N  N   . LEU   A 245 ? 0.40330 0.37659 0.36915 -0.05463 -0.02396 0.02611  322 LEU   A N   
1890 C  CA  . LEU   A 245 ? 0.47700 0.43668 0.43038 -0.05620 -0.02327 0.02303  322 LEU   A CA  
1891 C  C   . LEU   A 245 ? 0.51802 0.46999 0.46003 -0.06535 -0.02755 0.02569  322 LEU   A C   
1892 O  O   . LEU   A 245 ? 0.51240 0.46517 0.45299 -0.06969 -0.03051 0.02810  322 LEU   A O   
1893 C  CB  . LEU   A 245 ? 0.50965 0.45858 0.45680 -0.05120 -0.02000 0.01745  322 LEU   A CB  
1894 C  CG  . LEU   A 245 ? 0.47549 0.42919 0.43123 -0.04252 -0.01579 0.01421  322 LEU   A CG  
1895 C  CD1 . LEU   A 245 ? 0.45329 0.39495 0.40082 -0.03879 -0.01287 0.00931  322 LEU   A CD1 
1896 C  CD2 . LEU   A 245 ? 0.42622 0.38621 0.38800 -0.04028 -0.01444 0.01485  322 LEU   A CD2 
1897 N  N   . PRO   A 246 ? 0.54020 0.48409 0.47325 -0.06895 -0.02822 0.02553  323 PRO   A N   
1898 C  CA  . PRO   A 246 ? 0.58328 0.51715 0.50308 -0.07800 -0.03225 0.02757  323 PRO   A CA  
1899 C  C   . PRO   A 246 ? 0.62711 0.54806 0.53607 -0.07817 -0.03168 0.02423  323 PRO   A C   
1900 O  O   . PRO   A 246 ? 0.67311 0.58769 0.58017 -0.07163 -0.02759 0.01940  323 PRO   A O   
1901 C  CB  . PRO   A 246 ? 0.58802 0.51310 0.49933 -0.07966 -0.03170 0.02644  323 PRO   A CB  
1902 C  CG  . PRO   A 246 ? 0.52144 0.45681 0.44488 -0.07271 -0.02841 0.02562  323 PRO   A CG  
1903 C  CD  . PRO   A 246 ? 0.47988 0.42151 0.41284 -0.06503 -0.02528 0.02311  323 PRO   A CD  
1904 N  N   . GLU   A 247 ? 0.69546 0.61322 0.59774 -0.08567 -0.03579 0.02710  324 GLU   A N   
1905 C  CA  . GLU   A 247 ? 0.75066 0.65776 0.64383 -0.08580 -0.03524 0.02433  324 GLU   A CA  
1906 C  C   . GLU   A 247 ? 0.72773 0.61614 0.60576 -0.08403 -0.03203 0.01922  324 GLU   A C   
1907 O  O   . GLU   A 247 ? 0.65709 0.53630 0.52527 -0.08773 -0.03271 0.01924  324 GLU   A O   
1908 C  CB  . GLU   A 247 ? 0.84773 0.75343 0.73459 -0.09527 -0.04065 0.02861  324 GLU   A CB  
1909 C  CG  . GLU   A 247 ? 0.95911 0.88043 0.85661 -0.10026 -0.04497 0.03525  324 GLU   A CG  
1910 C  CD  . GLU   A 247 ? 1.13077 1.05202 1.02307 -0.10972 -0.05065 0.04003  324 GLU   A CD  
1911 O  OE1 . GLU   A 247 ? 1.03740 0.96007 0.93141 -0.10891 -0.05102 0.03990  324 GLU   A OE1 
1912 O  OE2 . GLU   A 247 ? 1.24430 1.16390 1.13045 -0.11825 -0.05491 0.04407  324 GLU   A OE2 
1913 N  N   . SER   A 248 ? 0.82585 0.70894 0.70240 -0.07805 -0.02832 0.01505  325 SER   A N   
1914 C  CA  . SER   A 248 ? 0.79330 0.65947 0.65673 -0.07496 -0.02444 0.01027  325 SER   A CA  
1915 C  C   . SER   A 248 ? 0.76180 0.62610 0.62629 -0.07013 -0.02127 0.00819  325 SER   A C   
1916 O  O   . SER   A 248 ? 0.78692 0.63634 0.63910 -0.06896 -0.01868 0.00525  325 SER   A O   
1917 C  CB  . SER   A 248 ? 0.83222 0.68128 0.67645 -0.08299 -0.02678 0.01053  325 SER   A CB  
1918 O  OG  . SER   A 248 ? 0.82514 0.67273 0.66629 -0.08584 -0.02841 0.01110  325 SER   A OG  
1919 N  N   . LEU   A 249 ? 0.67504 0.55395 0.55385 -0.06709 -0.02123 0.00975  326 LEU   A N   
1920 C  CA  . LEU   A 249 ? 0.57080 0.44929 0.45235 -0.06124 -0.01775 0.00742  326 LEU   A CA  
1921 C  C   . LEU   A 249 ? 0.56545 0.43736 0.44529 -0.05340 -0.01279 0.00283  326 LEU   A C   
1922 O  O   . LEU   A 249 ? 0.57470 0.43644 0.44719 -0.05061 -0.00995 0.00039  326 LEU   A O   
1923 C  CB  . LEU   A 249 ? 0.56439 0.46051 0.46259 -0.05833 -0.01798 0.00954  326 LEU   A CB  
1924 C  CG  . LEU   A 249 ? 0.53258 0.42943 0.43477 -0.05172 -0.01428 0.00701  326 LEU   A CG  
1925 C  CD1 . LEU   A 249 ? 0.54041 0.43295 0.43671 -0.05591 -0.01572 0.00851  326 LEU   A CD1 
1926 C  CD2 . LEU   A 249 ? 0.53969 0.45237 0.45817 -0.04625 -0.01296 0.00747  326 LEU   A CD2 
1927 N  N   . LEU   A 250 ? 0.54006 0.41812 0.42702 -0.04969 -0.01166 0.00192  327 LEU   A N   
1928 C  CA  . LEU   A 250 ? 0.52588 0.40010 0.41323 -0.04214 -0.00706 -0.00187 327 LEU   A CA  
1929 C  C   . LEU   A 250 ? 0.56460 0.42185 0.43641 -0.04310 -0.00532 -0.00411 327 LEU   A C   
1930 O  O   . LEU   A 250 ? 0.55582 0.40640 0.42457 -0.03723 -0.00106 -0.00704 327 LEU   A O   
1931 C  CB  . LEU   A 250 ? 0.53753 0.42385 0.43738 -0.03817 -0.00656 -0.00193 327 LEU   A CB  
1932 C  CG  . LEU   A 250 ? 0.42708 0.32980 0.34251 -0.03588 -0.00736 -0.00010 327 LEU   A CG  
1933 C  CD1 . LEU   A 250 ? 0.50411 0.41590 0.42911 -0.03271 -0.00699 -0.00019 327 LEU   A CD1 
1934 C  CD2 . LEU   A 250 ? 0.46286 0.36724 0.38240 -0.03050 -0.00448 -0.00179 327 LEU   A CD2 
1935 N  N   . SER   A 251 ? 0.55363 0.40385 0.41552 -0.05038 -0.00844 -0.00258 328 SER   A N   
1936 C  CA  . SER   A 251 ? 0.58064 0.41253 0.42534 -0.05204 -0.00673 -0.00465 328 SER   A CA  
1937 C  C   . SER   A 251 ? 0.59511 0.41498 0.43018 -0.05070 -0.00431 -0.00619 328 SER   A C   
1938 O  O   . SER   A 251 ? 0.53833 0.34482 0.36308 -0.04727 -0.00032 -0.00892 328 SER   A O   
1939 C  CB  . SER   A 251 ? 0.64451 0.47051 0.47917 -0.06140 -0.01123 -0.00228 328 SER   A CB  
1940 O  OG  . SER   A 251 ? 0.67155 0.50323 0.51062 -0.06182 -0.01227 -0.00177 328 SER   A OG  
1941 N  N   . SER   A 252 ? 0.57937 0.40396 0.41787 -0.05301 -0.00642 -0.00432 329 SER   A N   
1942 C  CA  . SER   A 252 ? 0.55814 0.37172 0.38783 -0.05201 -0.00444 -0.00548 329 SER   A CA  
1943 C  C   . SER   A 252 ? 0.58799 0.40493 0.42535 -0.04260 0.00031  -0.00784 329 SER   A C   
1944 O  O   . SER   A 252 ? 0.58360 0.39040 0.41338 -0.04048 0.00274  -0.00906 329 SER   A O   
1945 C  CB  . SER   A 252 ? 0.57893 0.39672 0.40959 -0.05819 -0.00855 -0.00239 329 SER   A CB  
1946 O  OG  . SER   A 252 ? 0.56010 0.37393 0.38250 -0.06758 -0.01324 0.00027  329 SER   A OG  
1947 N  N   . LEU   A 253 ? 0.56971 0.40006 0.42136 -0.03705 0.00164  -0.00834 330 LEU   A N   
1948 C  CA  . LEU   A 253 ? 0.52110 0.35653 0.38122 -0.02892 0.00539  -0.00996 330 LEU   A CA  
1949 C  C   . LEU   A 253 ? 0.49650 0.32524 0.35312 -0.02315 0.00976  -0.01247 330 LEU   A C   
1950 O  O   . LEU   A 253 ? 0.54363 0.38128 0.40961 -0.01934 0.01081  -0.01302 330 LEU   A O   
1951 C  CB  . LEU   A 253 ? 0.49077 0.34485 0.36826 -0.02683 0.00397  -0.00870 330 LEU   A CB  
1952 C  CG  . LEU   A 253 ? 0.51891 0.38101 0.40138 -0.03137 0.00043  -0.00599 330 LEU   A CG  
1953 C  CD1 . LEU   A 253 ? 0.49825 0.37740 0.39719 -0.02790 0.00021  -0.00516 330 LEU   A CD1 
1954 C  CD2 . LEU   A 253 ? 0.49496 0.34876 0.37008 -0.03209 0.00101  -0.00608 330 LEU   A CD2 
1955 N  N   . VAL   A 254 ? 0.54392 0.35646 0.38666 -0.02231 0.01259  -0.01386 331 VAL   A N   
1956 C  CA  . VAL   A 254 ? 0.55356 0.35653 0.38918 -0.01826 0.01674  -0.01584 331 VAL   A CA  
1957 C  C   . VAL   A 254 ? 0.53412 0.34363 0.37945 -0.00931 0.02101  -0.01697 331 VAL   A C   
1958 O  O   . VAL   A 254 ? 0.53663 0.34098 0.37852 -0.00544 0.02458  -0.01824 331 VAL   A O   
1959 C  CB  . VAL   A 254 ? 0.55627 0.33870 0.37305 -0.01988 0.01888  -0.01681 331 VAL   A CB  
1960 C  CG1 . VAL   A 254 ? 0.55696 0.33101 0.36190 -0.02940 0.01465  -0.01573 331 VAL   A CG1 
1961 C  CG2 . VAL   A 254 ? 0.55549 0.33480 0.37142 -0.01726 0.02026  -0.01669 331 VAL   A CG2 
1962 N  N   . LYS   A 255 ? 0.47284 0.29342 0.32984 -0.00605 0.02080  -0.01635 332 LYS   A N   
1963 C  CA  . LYS   A 255 ? 0.52545 0.35413 0.39283 0.00162  0.02405  -0.01694 332 LYS   A CA  
1964 C  C   . LYS   A 255 ? 0.48104 0.32753 0.36451 0.00229  0.02165  -0.01616 332 LYS   A C   
1965 O  O   . LYS   A 255 ? 0.45925 0.31353 0.35198 0.00788  0.02359  -0.01634 332 LYS   A O   
1966 C  CB  . LYS   A 255 ? 0.53084 0.35512 0.39676 0.00630  0.02693  -0.01699 332 LYS   A CB  
1967 C  CG  . LYS   A 255 ? 0.58252 0.39422 0.43616 0.00244  0.02619  -0.01673 332 LYS   A CG  
1968 C  CD  . LYS   A 255 ? 0.64921 0.45916 0.50386 0.00715  0.02853  -0.01641 332 LYS   A CD  
1969 C  CE  . LYS   A 255 ? 0.70576 0.51179 0.56003 0.01499  0.03385  -0.01697 332 LYS   A CE  
1970 N  NZ  . LYS   A 255 ? 0.72250 0.52701 0.57786 0.01948  0.03593  -0.01619 332 LYS   A NZ  
1971 N  N   . LEU   A 256 ? 0.49830 0.35124 0.38511 -0.00323 0.01755  -0.01508 333 LEU   A N   
1972 C  CA  . LEU   A 256 ? 0.46295 0.33178 0.36423 -0.00241 0.01559  -0.01422 333 LEU   A CA  
1973 C  C   . LEU   A 256 ? 0.42165 0.29651 0.32987 0.00188  0.01736  -0.01508 333 LEU   A C   
1974 O  O   . LEU   A 256 ? 0.48247 0.35359 0.38649 0.00056  0.01751  -0.01551 333 LEU   A O   
1975 C  CB  . LEU   A 256 ? 0.46585 0.34008 0.36905 -0.00892 0.01120  -0.01244 333 LEU   A CB  
1976 C  CG  . LEU   A 256 ? 0.45444 0.34430 0.37191 -0.00798 0.00948  -0.01129 333 LEU   A CG  
1977 C  CD1 . LEU   A 256 ? 0.45914 0.35209 0.37975 -0.00724 0.00936  -0.01069 333 LEU   A CD1 
1978 C  CD2 . LEU   A 256 ? 0.41914 0.31576 0.34022 -0.01307 0.00585  -0.00930 333 LEU   A CD2 
1979 N  N   . ASN   A 257 ? 0.39639 0.28003 0.31452 0.00676  0.01867  -0.01526 334 ASN   A N   
1980 C  CA  . ASN   A 257 ? 0.44329 0.33245 0.36766 0.01056  0.02024  -0.01588 334 ASN   A CA  
1981 C  C   . ASN   A 257 ? 0.43067 0.33361 0.36772 0.01135  0.01846  -0.01535 334 ASN   A C   
1982 O  O   . ASN   A 257 ? 0.44336 0.35116 0.38538 0.01324  0.01896  -0.01569 334 ASN   A O   
1983 C  CB  . ASN   A 257 ? 0.47308 0.35852 0.39640 0.01651  0.02428  -0.01651 334 ASN   A CB  
1984 C  CG  . ASN   A 257 ? 0.46352 0.35316 0.39195 0.01934  0.02475  -0.01599 334 ASN   A CG  
1985 O  OD1 . ASN   A 257 ? 0.44397 0.34420 0.38209 0.01992  0.02325  -0.01558 334 ASN   A OD1 
1986 N  ND2 . ASN   A 257 ? 0.47226 0.35306 0.39374 0.02128  0.02703  -0.01597 334 ASN   A ND2 
1987 N  N   . SER   A 258 ? 0.42839 0.33725 0.37029 0.00992  0.01655  -0.01451 335 SER   A N   
1988 C  CA  . SER   A 258 ? 0.38178 0.30255 0.33460 0.01064  0.01514  -0.01401 335 SER   A CA  
1989 C  C   . SER   A 258 ? 0.42545 0.35014 0.37990 0.00621  0.01225  -0.01254 335 SER   A C   
1990 O  O   . SER   A 258 ? 0.44926 0.37222 0.40156 0.00498  0.01184  -0.01198 335 SER   A O   
1991 C  CB  . SER   A 258 ? 0.40137 0.32680 0.36005 0.01509  0.01672  -0.01436 335 SER   A CB  
1992 O  OG  . SER   A 258 ? 0.48156 0.41585 0.44782 0.01451  0.01513  -0.01371 335 SER   A OG  
1993 N  N   . LEU   A 259 ? 0.40228 0.33239 0.36061 0.00383  0.01028  -0.01162 336 LEU   A N   
1994 C  CA  . LEU   A 259 ? 0.40084 0.33579 0.36154 -0.00040 0.00754  -0.00954 336 LEU   A CA  
1995 C  C   . LEU   A 259 ? 0.37104 0.31710 0.34232 0.00117  0.00697  -0.00881 336 LEU   A C   
1996 O  O   . LEU   A 259 ? 0.39096 0.33913 0.36514 0.00290  0.00738  -0.00945 336 LEU   A O   
1997 C  CB  . LEU   A 259 ? 0.35285 0.28266 0.30671 -0.00565 0.00539  -0.00837 336 LEU   A CB  
1998 C  CG  . LEU   A 259 ? 0.34507 0.28154 0.30262 -0.01023 0.00225  -0.00547 336 LEU   A CG  
1999 C  CD1 . LEU   A 259 ? 0.34914 0.28584 0.30586 -0.01180 0.00175  -0.00441 336 LEU   A CD1 
2000 C  CD2 . LEU   A 259 ? 0.33436 0.26591 0.28509 -0.01570 -0.00020 -0.00408 336 LEU   A CD2 
2001 N  N   . THR   A 260 ? 0.37128 0.32397 0.34790 0.00069  0.00623  -0.00742 337 THR   A N   
2002 C  CA  . THR   A 260 ? 0.35310 0.31567 0.33907 0.00215  0.00597  -0.00644 337 THR   A CA  
2003 C  C   . THR   A 260 ? 0.35832 0.32609 0.34679 -0.00178 0.00379  -0.00338 337 THR   A C   
2004 O  O   . THR   A 260 ? 0.36315 0.33098 0.35032 -0.00358 0.00336  -0.00229 337 THR   A O   
2005 C  CB  . THR   A 260 ? 0.38309 0.34957 0.37396 0.00618  0.00783  -0.00753 337 THR   A CB  
2006 O  OG1 . THR   A 260 ? 0.42066 0.38340 0.40995 0.00964  0.00962  -0.00980 337 THR   A OG1 
2007 C  CG2 . THR   A 260 ? 0.34038 0.31574 0.33971 0.00772  0.00789  -0.00655 337 THR   A CG2 
2008 N  N   . LEU   A 261 ? 0.32168 0.29416 0.31396 -0.00313 0.00237  -0.00168 338 LEU   A N   
2009 C  CA  . LEU   A 261 ? 0.34063 0.32020 0.33733 -0.00630 0.00039  0.00194  338 LEU   A CA  
2010 C  C   . LEU   A 261 ? 0.32788 0.31684 0.33433 -0.00308 0.00129  0.00303  338 LEU   A C   
2011 O  O   . LEU   A 261 ? 0.29089 0.28678 0.30228 -0.00499 -0.00010 0.00644  338 LEU   A O   
2012 C  CB  . LEU   A 261 ? 0.33232 0.30942 0.32472 -0.01143 -0.00247 0.00395  338 LEU   A CB  
2013 C  CG  . LEU   A 261 ? 0.39142 0.35760 0.37254 -0.01505 -0.00333 0.00294  338 LEU   A CG  
2014 C  CD1 . LEU   A 261 ? 0.41695 0.38032 0.39344 -0.02007 -0.00612 0.00473  338 LEU   A CD1 
2015 C  CD2 . LEU   A 261 ? 0.38562 0.35090 0.36416 -0.01761 -0.00395 0.00420  338 LEU   A CD2 
2016 N  N   . ALA   A 262 ? 0.30906 0.29816 0.31806 0.00169  0.00360  0.00045  339 ALA   A N   
2017 C  CA  . ALA   A 262 ? 0.34360 0.33957 0.36029 0.00500  0.00475  0.00101  339 ALA   A CA  
2018 C  C   . ALA   A 262 ? 0.38405 0.38738 0.40635 0.00510  0.00520  0.00374  339 ALA   A C   
2019 O  O   . ALA   A 262 ? 0.34798 0.35097 0.36859 0.00394  0.00540  0.00415  339 ALA   A O   
2020 C  CB  . ALA   A 262 ? 0.32478 0.31848 0.34171 0.00946  0.00706  -0.00228 339 ALA   A CB  
2021 N  N   . ARG   A 263 ? 0.36813 0.37816 0.39716 0.00664  0.00553  0.00583  340 ARG   A N   
2022 C  CA  . ARG   A 263 ? 0.33623 0.35372 0.37154 0.00817  0.00692  0.00839  340 ARG   A CA  
2023 C  C   . ARG   A 263 ? 0.33454 0.35556 0.37003 0.00391  0.00517  0.01193  340 ARG   A C   
2024 O  O   . ARG   A 263 ? 0.32649 0.35061 0.36371 0.00438  0.00643  0.01297  340 ARG   A O   
2025 C  CB  . ARG   A 263 ? 0.37665 0.39271 0.41184 0.01208  0.00985  0.00576  340 ARG   A CB  
2026 C  CG  . ARG   A 263 ? 0.44962 0.46367 0.48568 0.01616  0.01156  0.00310  340 ARG   A CG  
2027 C  CD  . ARG   A 263 ? 0.45882 0.46787 0.49107 0.01826  0.01315  -0.00039 340 ARG   A CD  
2028 N  NE  . ARG   A 263 ? 0.45508 0.46620 0.48926 0.02101  0.01569  -0.00059 340 ARG   A NE  
2029 C  CZ  . ARG   A 263 ? 0.50921 0.52607 0.54771 0.02169  0.01699  0.00211  340 ARG   A CZ  
2030 N  NH1 . ARG   A 263 ? 0.53485 0.55730 0.57741 0.01981  0.01581  0.00576  340 ARG   A NH1 
2031 N  NH2 . ARG   A 263 ? 0.47178 0.48891 0.51050 0.02430  0.01961  0.00136  340 ARG   A NH2 
2032 N  N   . ASN   A 264 ? 0.37806 0.39844 0.41133 -0.00060 0.00214  0.01395  341 ASN   A N   
2033 C  CA  . ASN   A 264 ? 0.36493 0.38948 0.39876 -0.00541 -0.00011 0.01812  341 ASN   A CA  
2034 C  C   . ASN   A 264 ? 0.36018 0.39275 0.40038 -0.00701 -0.00190 0.02277  341 ASN   A C   
2035 O  O   . ASN   A 264 ? 0.35218 0.38944 0.39870 -0.00295 -0.00021 0.02330  341 ASN   A O   
2036 C  CB  . ASN   A 264 ? 0.31939 0.33539 0.34365 -0.01034 -0.00250 0.01694  341 ASN   A CB  
2037 C  CG  . ASN   A 264 ? 0.35475 0.36638 0.37473 -0.00991 -0.00114 0.01483  341 ASN   A CG  
2038 O  OD1 . ASN   A 264 ? 0.33741 0.35264 0.35834 -0.01238 -0.00174 0.01747  341 ASN   A OD1 
2039 N  ND2 . ASN   A 264 ? 0.29801 0.30252 0.31378 -0.00670 0.00072  0.01039  341 ASN   A ND2 
2040 N  N   . CYS   A 265 ? 0.34902 0.38291 0.38730 -0.01301 -0.00539 0.02632  342 CYS   A N   
2041 C  CA  . CYS   A 265 ? 0.33154 0.37446 0.37650 -0.01521 -0.00750 0.03180  342 CYS   A CA  
2042 C  C   . CYS   A 265 ? 0.32044 0.35899 0.35987 -0.02053 -0.01137 0.03264  342 CYS   A C   
2043 O  O   . CYS   A 265 ? 0.31425 0.35882 0.35636 -0.02512 -0.01448 0.03780  342 CYS   A O   
2044 C  CB  . CYS   A 265 ? 0.35125 0.40283 0.40090 -0.01804 -0.00836 0.03697  342 CYS   A CB  
2045 S  SG  . CYS   A 265 ? 0.39601 0.45476 0.45354 -0.01172 -0.00357 0.03727  342 CYS   A SG  
2046 N  N   . PHE   A 266 ? 0.31731 0.34556 0.34892 -0.02015 -0.01121 0.02792  343 PHE   A N   
2047 C  CA  . PHE   A 266 ? 0.32150 0.34356 0.34569 -0.02551 -0.01458 0.02821  343 PHE   A CA  
2048 C  C   . PHE   A 266 ? 0.33263 0.35952 0.36187 -0.02520 -0.01588 0.03051  343 PHE   A C   
2049 O  O   . PHE   A 266 ? 0.28729 0.31512 0.32062 -0.01983 -0.01348 0.02836  343 PHE   A O   
2050 C  CB  . PHE   A 266 ? 0.36146 0.37077 0.37552 -0.02468 -0.01340 0.02252  343 PHE   A CB  
2051 C  CG  . PHE   A 266 ? 0.38575 0.38788 0.39205 -0.02672 -0.01316 0.02070  343 PHE   A CG  
2052 C  CD1 . PHE   A 266 ? 0.37509 0.37001 0.37182 -0.03322 -0.01609 0.02161  343 PHE   A CD1 
2053 C  CD2 . PHE   A 266 ? 0.34564 0.34726 0.35337 -0.02219 -0.00998 0.01795  343 PHE   A CD2 
2054 C  CE1 . PHE   A 266 ? 0.40852 0.39579 0.39744 -0.03488 -0.01570 0.01985  343 PHE   A CE1 
2055 C  CE2 . PHE   A 266 ? 0.37256 0.36737 0.37316 -0.02388 -0.00974 0.01638  343 PHE   A CE2 
2056 C  CZ  . PHE   A 266 ? 0.38701 0.37458 0.37825 -0.03012 -0.01254 0.01735  343 PHE   A CZ  
2057 N  N   . GLN   A 267 ? 0.32008 0.34937 0.34827 -0.03133 -0.01989 0.03490  344 GLN   A N   
2058 C  CA  . GLN   A 267 ? 0.32023 0.35270 0.35153 -0.03203 -0.02172 0.03713  344 GLN   A CA  
2059 C  C   . GLN   A 267 ? 0.35453 0.37603 0.37503 -0.03571 -0.02364 0.03443  344 GLN   A C   
2060 O  O   . GLN   A 267 ? 0.34007 0.36227 0.36196 -0.03545 -0.02457 0.03497  344 GLN   A O   
2061 C  CB  . GLN   A 267 ? 0.33594 0.37943 0.37406 -0.03642 -0.02512 0.04453  344 GLN   A CB  
2062 C  CG  . GLN   A 267 ? 0.39060 0.44564 0.43969 -0.03281 -0.02298 0.04794  344 GLN   A CG  
2063 C  CD  . GLN   A 267 ? 0.48218 0.55016 0.54094 -0.03504 -0.02549 0.05565  344 GLN   A CD  
2064 O  OE1 . GLN   A 267 ? 0.56028 0.62895 0.61793 -0.03937 -0.02912 0.05855  344 GLN   A OE1 
2065 N  NE2 . GLN   A 267 ? 0.58766 0.66622 0.65614 -0.03192 -0.02342 0.05926  344 GLN   A NE2 
2066 N  N   . LEU   A 268 ? 0.36621 0.37726 0.37570 -0.03899 -0.02406 0.03160  345 LEU   A N   
2067 C  CA  . LEU   A 268 ? 0.33529 0.33470 0.33320 -0.04246 -0.02539 0.02900  345 LEU   A CA  
2068 C  C   . LEU   A 268 ? 0.37847 0.36689 0.36793 -0.04004 -0.02239 0.02344  345 LEU   A C   
2069 O  O   . LEU   A 268 ? 0.39732 0.38747 0.38954 -0.03696 -0.02016 0.02226  345 LEU   A O   
2070 C  CB  . LEU   A 268 ? 0.36229 0.35956 0.35342 -0.05138 -0.03022 0.03308  345 LEU   A CB  
2071 C  CG  . LEU   A 268 ? 0.41652 0.42314 0.41382 -0.05534 -0.03412 0.03909  345 LEU   A CG  
2072 C  CD1 . LEU   A 268 ? 0.38256 0.38653 0.37213 -0.06489 -0.03909 0.04321  345 LEU   A CD1 
2073 C  CD2 . LEU   A 268 ? 0.44547 0.44994 0.44241 -0.05373 -0.03409 0.03771  345 LEU   A CD2 
2074 N  N   . TYR   A 269 ? 0.38596 0.36300 0.36499 -0.04135 -0.02221 0.02023  346 TYR   A N   
2075 C  CA  . TYR   A 269 ? 0.40393 0.36970 0.37355 -0.04005 -0.01975 0.01582  346 TYR   A CA  
2076 C  C   . TYR   A 269 ? 0.46407 0.42518 0.42615 -0.04599 -0.02196 0.01761  346 TYR   A C   
2077 O  O   . TYR   A 269 ? 0.43904 0.40259 0.39977 -0.05249 -0.02594 0.02186  346 TYR   A O   
2078 C  CB  . TYR   A 269 ? 0.39114 0.34578 0.35110 -0.04003 -0.01875 0.01245  346 TYR   A CB  
2079 C  CG  . TYR   A 269 ? 0.41073 0.36488 0.37416 -0.03279 -0.01478 0.00845  346 TYR   A CG  
2080 C  CD1 . TYR   A 269 ? 0.39718 0.36091 0.37154 -0.02870 -0.01412 0.00905  346 TYR   A CD1 
2081 C  CD2 . TYR   A 269 ? 0.43777 0.38177 0.39336 -0.03012 -0.01170 0.00434  346 TYR   A CD2 
2082 C  CE1 . TYR   A 269 ? 0.39196 0.35515 0.36911 -0.02264 -0.01081 0.00561  346 TYR   A CE1 
2083 C  CE2 . TYR   A 269 ? 0.45828 0.40271 0.41752 -0.02379 -0.00830 0.00120  346 TYR   A CE2 
2084 C  CZ  . TYR   A 269 ? 0.45074 0.40478 0.42063 -0.02035 -0.00804 0.00182  346 TYR   A CZ  
2085 O  OH  . TYR   A 269 ? 0.42533 0.37968 0.39841 -0.01471 -0.00502 -0.00105 346 TYR   A OH  
2086 N  N   . PRO   A 270 ? 0.49247 0.44708 0.44963 -0.04411 -0.01964 0.01474  347 PRO   A N   
2087 C  CA  . PRO   A 270 ? 0.48255 0.42969 0.42984 -0.05007 -0.02164 0.01585  347 PRO   A CA  
2088 C  C   . PRO   A 270 ? 0.51537 0.45080 0.44932 -0.05610 -0.02391 0.01578  347 PRO   A C   
2089 O  O   . PRO   A 270 ? 0.51876 0.44576 0.44654 -0.05383 -0.02184 0.01239  347 PRO   A O   
2090 C  CB  . PRO   A 270 ? 0.47736 0.41792 0.42118 -0.04548 -0.01792 0.01186  347 PRO   A CB  
2091 C  CG  . PRO   A 270 ? 0.48407 0.42669 0.43378 -0.03783 -0.01420 0.00840  347 PRO   A CG  
2092 C  CD  . PRO   A 270 ? 0.43829 0.39293 0.39929 -0.03672 -0.01535 0.01088  347 PRO   A CD  
2093 N  N   . VAL   A 271 ? 0.55466 0.48951 0.48383 -0.06403 -0.02818 0.01974  348 VAL   A N   
2094 C  CA  . VAL   A 271 ? 0.59289 0.51720 0.50920 -0.07090 -0.03105 0.02042  348 VAL   A CA  
2095 C  C   . VAL   A 271 ? 0.66349 0.57019 0.56342 -0.07253 -0.02945 0.01689  348 VAL   A C   
2096 O  O   . VAL   A 271 ? 0.65328 0.55722 0.55073 -0.07269 -0.02878 0.01651  348 VAL   A O   
2097 C  CB  . VAL   A 271 ? 0.61288 0.54419 0.53075 -0.07932 -0.03671 0.02667  348 VAL   A CB  
2098 C  CG1 . VAL   A 271 ? 0.58211 0.53136 0.51712 -0.07665 -0.03763 0.03044  348 VAL   A CG1 
2099 C  CG2 . VAL   A 271 ? 0.65585 0.58606 0.57036 -0.08355 -0.03831 0.02867  348 VAL   A CG2 
2100 N  N   . GLY   A 272 ? 0.77125 0.66552 0.65956 -0.07361 -0.02863 0.01436  349 GLY   A N   
2101 C  CA  . GLY   A 272 ? 0.82584 0.70226 0.69736 -0.07545 -0.02703 0.01140  349 GLY   A CA  
2102 C  C   . GLY   A 272 ? 0.87808 0.74157 0.73967 -0.07199 -0.02323 0.00701  349 GLY   A C   
2103 O  O   . GLY   A 272 ? 0.94975 0.79857 0.79856 -0.07144 -0.02059 0.00414  349 GLY   A O   
2104 N  N   . GLY   A 273 ? 0.68248 0.55084 0.54946 -0.06950 -0.02267 0.00657  350 GLY   A N   
2105 C  CA  . GLY   A 273 ? 0.67175 0.52807 0.52877 -0.06712 -0.01938 0.00300  350 GLY   A CA  
2106 C  C   . GLY   A 273 ? 0.64962 0.50378 0.50933 -0.05790 -0.01345 -0.00120 350 GLY   A C   
2107 O  O   . GLY   A 273 ? 0.60075 0.46117 0.46861 -0.05355 -0.01188 -0.00166 350 GLY   A O   
2108 N  N   . PRO   A 274 ? 0.60969 0.45487 0.46228 -0.05495 -0.01005 -0.00409 351 PRO   A N   
2109 C  CA  . PRO   A 274 ? 0.61388 0.45971 0.47141 -0.04586 -0.00455 -0.00741 351 PRO   A CA  
2110 C  C   . PRO   A 274 ? 0.62601 0.46347 0.47784 -0.04256 -0.00119 -0.00940 351 PRO   A C   
2111 O  O   . PRO   A 274 ? 0.59020 0.43140 0.44901 -0.03514 0.00269  -0.01129 351 PRO   A O   
2112 C  CB  . PRO   A 274 ? 0.58800 0.42496 0.43715 -0.04493 -0.00211 -0.00935 351 PRO   A CB  
2113 C  CG  . PRO   A 274 ? 0.61618 0.44058 0.44955 -0.05344 -0.00508 -0.00821 351 PRO   A CG  
2114 C  CD  . PRO   A 274 ? 0.57691 0.41130 0.41671 -0.05988 -0.01106 -0.00419 351 PRO   A CD  
2115 N  N   . SER   A 275 ? 0.59321 0.41923 0.43232 -0.04796 -0.00262 -0.00886 352 SER   A N   
2116 C  CA  . SER   A 275 ? 0.59503 0.41370 0.42935 -0.04500 0.00022  -0.01037 352 SER   A CA  
2117 C  C   . SER   A 275 ? 0.58743 0.42023 0.43720 -0.04041 0.00042  -0.00979 352 SER   A C   
2118 O  O   . SER   A 275 ? 0.60359 0.43280 0.45263 -0.03572 0.00367  -0.01137 352 SER   A O   
2119 C  CB  . SER   A 275 ? 0.60847 0.41505 0.42844 -0.05281 -0.00264 -0.00910 352 SER   A CB  
2120 O  OG  . SER   A 275 ? 0.74388 0.55538 0.56422 -0.06095 -0.00832 -0.00584 352 SER   A OG  
2121 N  N   . GLN   A 276 ? 0.56560 0.41399 0.42891 -0.04164 -0.00289 -0.00742 353 GLN   A N   
2122 C  CA  . GLN   A 276 ? 0.54062 0.40158 0.41734 -0.03800 -0.00284 -0.00671 353 GLN   A CA  
2123 C  C   . GLN   A 276 ? 0.48946 0.35540 0.37473 -0.02937 0.00144  -0.00911 353 GLN   A C   
2124 O  O   . GLN   A 276 ? 0.49008 0.36155 0.38232 -0.02564 0.00265  -0.00937 353 GLN   A O   
2125 C  CB  . GLN   A 276 ? 0.53964 0.41552 0.42830 -0.04105 -0.00693 -0.00342 353 GLN   A CB  
2126 C  CG  . GLN   A 276 ? 0.59867 0.47240 0.48101 -0.04989 -0.01172 -0.00022 353 GLN   A CG  
2127 C  CD  . GLN   A 276 ? 0.61930 0.50940 0.51538 -0.05167 -0.01518 0.00348  353 GLN   A CD  
2128 O  OE1 . GLN   A 276 ? 0.59369 0.49304 0.49874 -0.05039 -0.01558 0.00491  353 GLN   A OE1 
2129 N  NE2 . GLN   A 276 ? 0.60605 0.49987 0.50402 -0.05426 -0.01742 0.00513  353 GLN   A NE2 
2130 N  N   . PHE   A 277 ? 0.49166 0.35623 0.37670 -0.02643 0.00354  -0.01060 354 PHE   A N   
2131 C  CA  . PHE   A 277 ? 0.52106 0.39328 0.41635 -0.01906 0.00669  -0.01212 354 PHE   A CA  
2132 C  C   . PHE   A 277 ? 0.50577 0.36784 0.39349 -0.01462 0.01129  -0.01456 354 PHE   A C   
2133 O  O   . PHE   A 277 ? 0.52285 0.39047 0.41776 -0.00924 0.01376  -0.01554 354 PHE   A O   
2134 C  CB  . PHE   A 277 ? 0.45929 0.34346 0.36535 -0.01899 0.00478  -0.01101 354 PHE   A CB  
2135 C  CG  . PHE   A 277 ? 0.46154 0.35724 0.37703 -0.02182 0.00109  -0.00836 354 PHE   A CG  
2136 C  CD1 . PHE   A 277 ? 0.48021 0.38427 0.40506 -0.01841 0.00171  -0.00821 354 PHE   A CD1 
2137 C  CD2 . PHE   A 277 ? 0.47121 0.36941 0.38608 -0.02788 -0.00289 -0.00575 354 PHE   A CD2 
2138 C  CE1 . PHE   A 277 ? 0.42781 0.34234 0.36121 -0.02055 -0.00111 -0.00566 354 PHE   A CE1 
2139 C  CE2 . PHE   A 277 ? 0.46889 0.37841 0.39311 -0.03004 -0.00594 -0.00281 354 PHE   A CE2 
2140 C  CZ  . PHE   A 277 ? 0.47331 0.39087 0.40674 -0.02617 -0.00481 -0.00285 354 PHE   A CZ  
2141 N  N   . SER   A 278 ? 0.50778 0.35494 0.38095 -0.01670 0.01263  -0.01536 355 SER   A N   
2142 C  CA  . SER   A 278 ? 0.52830 0.36469 0.39296 -0.01264 0.01735  -0.01738 355 SER   A CA  
2143 C  C   . SER   A 278 ? 0.50918 0.34922 0.38069 -0.00474 0.02149  -0.01839 355 SER   A C   
2144 O  O   . SER   A 278 ? 0.54601 0.38655 0.41947 0.00013  0.02490  -0.01931 355 SER   A O   
2145 C  CB  . SER   A 278 ? 0.52841 0.34694 0.37509 -0.01654 0.01807  -0.01797 355 SER   A CB  
2146 O  OG  . SER   A 278 ? 0.67088 0.48718 0.51571 -0.01788 0.01705  -0.01739 355 SER   A OG  
2147 N  N   . THR   A 279 ? 0.49991 0.34291 0.37531 -0.00349 0.02118  -0.01796 356 THR   A N   
2148 C  CA  . THR   A 279 ? 0.50424 0.35145 0.38657 0.00361  0.02463  -0.01849 356 THR   A CA  
2149 C  C   . THR   A 279 ? 0.49588 0.35950 0.39412 0.00570  0.02290  -0.01775 356 THR   A C   
2150 O  O   . THR   A 279 ? 0.47245 0.34108 0.37745 0.01085  0.02497  -0.01785 356 THR   A O   
2151 C  CB  . THR   A 279 ? 0.51152 0.35092 0.38771 0.00445  0.02593  -0.01854 356 THR   A CB  
2152 O  OG1 . THR   A 279 ? 0.51504 0.35728 0.39205 -0.00093 0.02175  -0.01739 356 THR   A OG1 
2153 C  CG2 . THR   A 279 ? 0.43687 0.25853 0.29670 0.00417  0.02902  -0.01955 356 THR   A CG2 
2154 N  N   . ILE   A 280 ? 0.46405 0.33578 0.36804 0.00182  0.01920  -0.01684 357 ILE   A N   
2155 C  CA  . ILE   A 280 ? 0.45568 0.34170 0.37348 0.00333  0.01749  -0.01608 357 ILE   A CA  
2156 C  C   . ILE   A 280 ? 0.45556 0.34764 0.38078 0.00868  0.01988  -0.01679 357 ILE   A C   
2157 O  O   . ILE   A 280 ? 0.45004 0.33919 0.37236 0.00924  0.02118  -0.01733 357 ILE   A O   
2158 C  CB  . ILE   A 280 ? 0.45074 0.34323 0.37227 -0.00194 0.01326  -0.01458 357 ILE   A CB  
2159 C  CG1 . ILE   A 280 ? 0.43469 0.33444 0.36247 -0.00344 0.01097  -0.01322 357 ILE   A CG1 
2160 C  CG2 . ILE   A 280 ? 0.45477 0.35594 0.38475 -0.00028 0.01292  -0.01454 357 ILE   A CG2 
2161 C  CD1 . ILE   A 280 ? 0.44960 0.36089 0.38976 0.00093  0.01156  -0.01330 357 ILE   A CD1 
2162 N  N   . TYR   A 281 ? 0.38008 0.28026 0.31433 0.01241  0.02047  -0.01666 358 TYR   A N   
2163 C  CA  . TYR   A 281 ? 0.43405 0.34110 0.37611 0.01702  0.02222  -0.01694 358 TYR   A CA  
2164 C  C   . TYR   A 281 ? 0.42586 0.34485 0.37887 0.01671  0.01979  -0.01640 358 TYR   A C   
2165 O  O   . TYR   A 281 ? 0.42718 0.35111 0.38505 0.01804  0.01991  -0.01650 358 TYR   A O   
2166 C  CB  . TYR   A 281 ? 0.41631 0.32235 0.35925 0.02183  0.02513  -0.01699 358 TYR   A CB  
2167 C  CG  . TYR   A 281 ? 0.45848 0.37318 0.41060 0.02608  0.02629  -0.01670 358 TYR   A CG  
2168 C  CD1 . TYR   A 281 ? 0.44459 0.36877 0.40573 0.02668  0.02458  -0.01627 358 TYR   A CD1 
2169 C  CD2 . TYR   A 281 ? 0.42633 0.33953 0.37769 0.02934  0.02915  -0.01669 358 TYR   A CD2 
2170 C  CE1 . TYR   A 281 ? 0.47040 0.40192 0.43908 0.02995  0.02531  -0.01586 358 TYR   A CE1 
2171 C  CE2 . TYR   A 281 ? 0.45705 0.37861 0.41687 0.03275  0.02991  -0.01601 358 TYR   A CE2 
2172 C  CZ  . TYR   A 281 ? 0.51630 0.44678 0.48450 0.03279  0.02778  -0.01561 358 TYR   A CZ  
2173 O  OH  . TYR   A 281 ? 0.59667 0.53480 0.57235 0.03550  0.02817  -0.01482 358 TYR   A OH  
2174 N  N   . SER   A 282 ? 0.41118 0.33438 0.36763 0.01495  0.01773  -0.01576 359 SER   A N   
2175 C  CA  . SER   A 282 ? 0.41658 0.35010 0.38257 0.01492  0.01585  -0.01519 359 SER   A CA  
2176 C  C   . SER   A 282 ? 0.39778 0.33295 0.36361 0.01036  0.01298  -0.01397 359 SER   A C   
2177 O  O   . SER   A 282 ? 0.44649 0.37797 0.40808 0.00825  0.01239  -0.01348 359 SER   A O   
2178 C  CB  . SER   A 282 ? 0.39398 0.33225 0.36549 0.01815  0.01673  -0.01530 359 SER   A CB  
2179 O  OG  . SER   A 282 ? 0.52137 0.46779 0.50011 0.01745  0.01496  -0.01474 359 SER   A OG  
2180 N  N   . LEU   A 283 ? 0.43247 0.37324 0.40291 0.00879  0.01118  -0.01319 360 LEU   A N   
2181 C  CA  . LEU   A 283 ? 0.40387 0.34755 0.37523 0.00450  0.00837  -0.01134 360 LEU   A CA  
2182 C  C   . LEU   A 283 ? 0.42705 0.38092 0.40837 0.00576  0.00747  -0.01044 360 LEU   A C   
2183 O  O   . LEU   A 283 ? 0.38341 0.34022 0.36829 0.00722  0.00761  -0.01076 360 LEU   A O   
2184 C  CB  . LEU   A 283 ? 0.38818 0.32677 0.35327 0.00062  0.00694  -0.01072 360 LEU   A CB  
2185 C  CG  . LEU   A 283 ? 0.38445 0.32599 0.34999 -0.00451 0.00363  -0.00817 360 LEU   A CG  
2186 C  CD1 . LEU   A 283 ? 0.35165 0.29281 0.31572 -0.00659 0.00279  -0.00708 360 LEU   A CD1 
2187 C  CD2 . LEU   A 283 ? 0.41729 0.35180 0.37452 -0.00869 0.00225  -0.00772 360 LEU   A CD2 
2188 N  N   . ASN   A 284 ? 0.35358 0.31234 0.33892 0.00524  0.00673  -0.00925 361 ASN   A N   
2189 C  CA  . ASN   A 284 ? 0.34485 0.31239 0.33894 0.00700  0.00655  -0.00843 361 ASN   A CA  
2190 C  C   . ASN   A 284 ? 0.35979 0.33201 0.35644 0.00353  0.00436  -0.00557 361 ASN   A C   
2191 O  O   . ASN   A 284 ? 0.35701 0.32954 0.35260 0.00163  0.00378  -0.00439 361 ASN   A O   
2192 C  CB  . ASN   A 284 ? 0.33924 0.30889 0.33619 0.01006  0.00816  -0.00937 361 ASN   A CB  
2193 C  CG  . ASN   A 284 ? 0.41812 0.38770 0.41681 0.01393  0.00990  -0.01130 361 ASN   A CG  
2194 O  OD1 . ASN   A 284 ? 0.41835 0.38278 0.41281 0.01504  0.01103  -0.01255 361 ASN   A OD1 
2195 N  ND2 . ASN   A 284 ? 0.42270 0.39790 0.42746 0.01603  0.01023  -0.01133 361 ASN   A ND2 
2196 N  N   . MET   A 285 ? 0.39785 0.37426 0.39830 0.00275  0.00311  -0.00412 362 MET   A N   
2197 C  CA  . MET   A 285 ? 0.35815 0.34007 0.36190 -0.00048 0.00094  -0.00071 362 MET   A CA  
2198 C  C   . MET   A 285 ? 0.33621 0.32662 0.34896 0.00209  0.00131  0.00074  362 MET   A C   
2199 O  O   . MET   A 285 ? 0.35203 0.34770 0.36850 -0.00006 -0.00045 0.00394  362 MET   A O   
2200 C  CB  . MET   A 285 ? 0.37431 0.35256 0.37282 -0.00513 -0.00151 0.00069  362 MET   A CB  
2201 C  CG  . MET   A 285 ? 0.37904 0.34752 0.36731 -0.00787 -0.00168 -0.00062 362 MET   A CG  
2202 S  SD  . MET   A 285 ? 0.57755 0.54195 0.55947 -0.01386 -0.00480 0.00138  362 MET   A SD  
2203 C  CE  . MET   A 285 ? 0.46224 0.43000 0.44411 -0.01917 -0.00762 0.00521  362 MET   A CE  
2204 N  N   . GLU   A 286 ? 0.30651 0.29814 0.32252 0.00657  0.00358  -0.00131 363 GLU   A N   
2205 C  CA  . GLU   A 286 ? 0.34671 0.34442 0.36979 0.00939  0.00435  -0.00040 363 GLU   A CA  
2206 C  C   . GLU   A 286 ? 0.36932 0.37384 0.39779 0.00940  0.00453  0.00249  363 GLU   A C   
2207 O  O   . GLU   A 286 ? 0.34610 0.35073 0.37319 0.00806  0.00457  0.00307  363 GLU   A O   
2208 C  CB  . GLU   A 286 ? 0.31787 0.31386 0.34155 0.01360  0.00658  -0.00340 363 GLU   A CB  
2209 C  CG  . GLU   A 286 ? 0.35418 0.34894 0.37676 0.01534  0.00827  -0.00498 363 GLU   A CG  
2210 C  CD  . GLU   A 286 ? 0.41575 0.40407 0.43206 0.01469  0.00844  -0.00708 363 GLU   A CD  
2211 O  OE1 . GLU   A 286 ? 0.38194 0.36620 0.39390 0.01246  0.00736  -0.00717 363 GLU   A OE1 
2212 O  OE2 . GLU   A 286 ? 0.39601 0.38309 0.41147 0.01648  0.00980  -0.00850 363 GLU   A OE2 
2213 N  N   . HIS   A 287 ? 0.35224 0.36251 0.38691 0.01103  0.00476  0.00457  364 HIS   A N   
2214 C  CA  . HIS   A 287 ? 0.35990 0.37751 0.40078 0.01195  0.00552  0.00777  364 HIS   A CA  
2215 C  C   . HIS   A 287 ? 0.36482 0.38584 0.40587 0.00733  0.00317  0.01145  364 HIS   A C   
2216 O  O   . HIS   A 287 ? 0.36685 0.39041 0.40873 0.00664  0.00366  0.01273  364 HIS   A O   
2217 C  CB  . HIS   A 287 ? 0.37090 0.38837 0.41238 0.01532  0.00838  0.00598  364 HIS   A CB  
2218 C  CG  . HIS   A 287 ? 0.38407 0.39759 0.42434 0.01902  0.01025  0.00251  364 HIS   A CG  
2219 N  ND1 . HIS   A 287 ? 0.36006 0.37510 0.40376 0.02183  0.01122  0.00273  364 HIS   A ND1 
2220 C  CD2 . HIS   A 287 ? 0.37702 0.38506 0.41284 0.02008  0.01112  -0.00098 364 HIS   A CD2 
2221 C  CE1 . HIS   A 287 ? 0.34190 0.35234 0.38292 0.02411  0.01247  -0.00057 364 HIS   A CE1 
2222 N  NE2 . HIS   A 287 ? 0.35753 0.36414 0.39411 0.02309  0.01237  -0.00270 364 HIS   A NE2 
2223 N  N   . ASN   A 288 ? 0.34078 0.36188 0.38084 0.00384  0.00042  0.01336  365 ASN   A N   
2224 C  CA  . ASN   A 288 ? 0.33505 0.36047 0.37604 -0.00103 -0.00235 0.01775  365 ASN   A CA  
2225 C  C   . ASN   A 288 ? 0.33700 0.36793 0.38323 -0.00156 -0.00395 0.02123  365 ASN   A C   
2226 O  O   . ASN   A 288 ? 0.34707 0.37963 0.39742 0.00258  -0.00230 0.02058  365 ASN   A O   
2227 C  CB  . ASN   A 288 ? 0.35218 0.37012 0.38407 -0.00616 -0.00468 0.01663  365 ASN   A CB  
2228 C  CG  . ASN   A 288 ? 0.35634 0.37057 0.38409 -0.00634 -0.00353 0.01477  365 ASN   A CG  
2229 O  OD1 . ASN   A 288 ? 0.35716 0.37594 0.38709 -0.00822 -0.00403 0.01756  365 ASN   A OD1 
2230 N  ND2 . ASN   A 288 ? 0.33628 0.34242 0.35807 -0.00458 -0.00208 0.01037  365 ASN   A ND2 
2231 N  N   . ARG   A 289 ? 0.32115 0.35447 0.36669 -0.00696 -0.00739 0.02504  366 ARG   A N   
2232 C  CA  . ARG   A 289 ? 0.30294 0.34127 0.35274 -0.00843 -0.00960 0.02880  366 ARG   A CA  
2233 C  C   . ARG   A 289 ? 0.30733 0.33950 0.34926 -0.01428 -0.01315 0.02870  366 ARG   A C   
2234 O  O   . ARG   A 289 ? 0.33072 0.36713 0.37402 -0.01884 -0.01649 0.03324  366 ARG   A O   
2235 C  CB  . ARG   A 289 ? 0.36242 0.41214 0.42088 -0.00942 -0.01051 0.03513  366 ARG   A CB  
2236 C  CG  . ARG   A 289 ? 0.35604 0.41187 0.42218 -0.00337 -0.00653 0.03565  366 ARG   A CG  
2237 C  CD  . ARG   A 289 ? 0.31757 0.38536 0.39336 -0.00349 -0.00709 0.04246  366 ARG   A CD  
2238 N  NE  . ARG   A 289 ? 0.45277 0.52415 0.53396 -0.00097 -0.00713 0.04453  366 ARG   A NE  
2239 C  CZ  . ARG   A 289 ? 0.42610 0.50266 0.51022 -0.00480 -0.01067 0.04944  366 ARG   A CZ  
2240 N  NH1 . ARG   A 289 ? 0.52847 0.60761 0.61076 -0.01159 -0.01457 0.05308  366 ARG   A NH1 
2241 N  NH2 . ARG   A 289 ? 0.40063 0.47948 0.48915 -0.00206 -0.01048 0.05084  366 ARG   A NH2 
2242 N  N   . ILE   A 290 ? 0.36923 0.39118 0.40251 -0.01429 -0.01241 0.02372  367 ILE   A N   
2243 C  CA  . ILE   A 290 ? 0.34996 0.36422 0.37405 -0.01960 -0.01516 0.02310  367 ILE   A CA  
2244 C  C   . ILE   A 290 ? 0.33542 0.35105 0.36136 -0.01989 -0.01660 0.02434  367 ILE   A C   
2245 O  O   . ILE   A 290 ? 0.33203 0.34675 0.36014 -0.01528 -0.01445 0.02172  367 ILE   A O   
2246 C  CB  . ILE   A 290 ? 0.34421 0.34745 0.35918 -0.01846 -0.01319 0.01760  367 ILE   A CB  
2247 C  CG1 . ILE   A 290 ? 0.33112 0.33226 0.34291 -0.01960 -0.01261 0.01708  367 ILE   A CG1 
2248 C  CG2 . ILE   A 290 ? 0.34977 0.34423 0.35528 -0.02236 -0.01497 0.01633  367 ILE   A CG2 
2249 C  CD1 . ILE   A 290 ? 0.33630 0.33019 0.34347 -0.01596 -0.00956 0.01217  367 ILE   A CD1 
2250 N  N   . ASN   A 291 ? 0.33297 0.35057 0.35769 -0.02561 -0.02044 0.02845  368 ASN   A N   
2251 C  CA  . ASN   A 291 ? 0.34530 0.36538 0.37284 -0.02580 -0.02195 0.03025  368 ASN   A CA  
2252 C  C   . ASN   A 291 ? 0.37400 0.38386 0.39148 -0.02847 -0.02292 0.02722  368 ASN   A C   
2253 O  O   . ASN   A 291 ? 0.37855 0.38956 0.39744 -0.02882 -0.02418 0.02837  368 ASN   A O   
2254 C  CB  . ASN   A 291 ? 0.35300 0.38243 0.38636 -0.03010 -0.02569 0.03713  368 ASN   A CB  
2255 C  CG  . ASN   A 291 ? 0.44083 0.46722 0.46674 -0.03803 -0.02947 0.03957  368 ASN   A CG  
2256 O  OD1 . ASN   A 291 ? 0.43803 0.45556 0.45379 -0.04277 -0.03159 0.03820  368 ASN   A OD1 
2257 N  ND2 . ASN   A 291 ? 0.44883 0.48240 0.47938 -0.03978 -0.03036 0.04345  368 ASN   A ND2 
2258 N  N   . LYS   A 292 ? 0.36756 0.36731 0.37489 -0.03006 -0.02210 0.02345  369 LYS   A N   
2259 C  CA  . LYS   A 292 ? 0.35969 0.34958 0.35755 -0.03172 -0.02223 0.02049  369 LYS   A CA  
2260 C  C   . LYS   A 292 ? 0.39023 0.36955 0.37844 -0.03132 -0.01995 0.01603  369 LYS   A C   
2261 O  O   . LYS   A 292 ? 0.41586 0.39469 0.40286 -0.03204 -0.01962 0.01610  369 LYS   A O   
2262 C  CB  . LYS   A 292 ? 0.41134 0.39969 0.40398 -0.03898 -0.02662 0.02409  369 LYS   A CB  
2263 C  CG  . LYS   A 292 ? 0.40413 0.38710 0.38795 -0.04553 -0.02906 0.02547  369 LYS   A CG  
2264 C  CD  . LYS   A 292 ? 0.39950 0.38030 0.37721 -0.05328 -0.03372 0.02912  369 LYS   A CD  
2265 C  CE  . LYS   A 292 ? 0.55017 0.52313 0.52110 -0.05320 -0.03316 0.02634  369 LYS   A CE  
2266 N  NZ  . LYS   A 292 ? 0.64368 0.60876 0.60292 -0.06135 -0.03700 0.02811  369 LYS   A NZ  
2267 N  N   . ILE   A 293 ? 0.39050 0.36159 0.37208 -0.02995 -0.01820 0.01236  370 ILE   A N   
2268 C  CA  . ILE   A 293 ? 0.41007 0.36978 0.38085 -0.03017 -0.01617 0.00866  370 ILE   A CA  
2269 C  C   . ILE   A 293 ? 0.40606 0.35697 0.36517 -0.03687 -0.01876 0.00960  370 ILE   A C   
2270 O  O   . ILE   A 293 ? 0.41235 0.36124 0.36904 -0.03811 -0.01957 0.00968  370 ILE   A O   
2271 C  CB  . ILE   A 293 ? 0.38366 0.33980 0.35418 -0.02441 -0.01232 0.00443  370 ILE   A CB  
2272 C  CG1 . ILE   A 293 ? 0.38706 0.35150 0.36843 -0.01843 -0.01017 0.00371  370 ILE   A CG1 
2273 C  CG2 . ILE   A 293 ? 0.41030 0.35515 0.37023 -0.02407 -0.00985 0.00110  370 ILE   A CG2 
2274 C  CD1 . ILE   A 293 ? 0.37566 0.33820 0.35795 -0.01332 -0.00705 0.00033  370 ILE   A CD1 
2275 N  N   . PRO   A 294 ? 0.38114 0.32614 0.33221 -0.04154 -0.02017 0.01035  371 PRO   A N   
2276 C  CA  . PRO   A 294 ? 0.44399 0.37980 0.38277 -0.04874 -0.02300 0.01152  371 PRO   A CA  
2277 C  C   . PRO   A 294 ? 0.44481 0.36904 0.37329 -0.04774 -0.02054 0.00781  371 PRO   A C   
2278 O  O   . PRO   A 294 ? 0.44779 0.36719 0.37443 -0.04246 -0.01634 0.00394  371 PRO   A O   
2279 C  CB  . PRO   A 294 ? 0.41100 0.34098 0.34243 -0.05242 -0.02376 0.01187  371 PRO   A CB  
2280 C  CG  . PRO   A 294 ? 0.39089 0.33061 0.33333 -0.04840 -0.02264 0.01252  371 PRO   A CG  
2281 C  CD  . PRO   A 294 ? 0.41735 0.36323 0.36953 -0.04070 -0.01930 0.01018  371 PRO   A CD  
2282 N  N   . PHE   A 295 ? 0.44054 0.36034 0.36207 -0.05302 -0.02318 0.00930  372 PHE   A N   
2283 C  CA  . PHE   A 295 ? 0.44943 0.35678 0.35911 -0.05298 -0.02085 0.00606  372 PHE   A CA  
2284 C  C   . PHE   A 295 ? 0.41451 0.30822 0.31087 -0.05405 -0.01867 0.00346  372 PHE   A C   
2285 O  O   . PHE   A 295 ? 0.45240 0.34140 0.34142 -0.06013 -0.02149 0.00535  372 PHE   A O   
2286 C  CB  . PHE   A 295 ? 0.44458 0.34919 0.34815 -0.05950 -0.02459 0.00855  372 PHE   A CB  
2287 C  CG  . PHE   A 295 ? 0.43530 0.32676 0.32593 -0.05985 -0.02215 0.00544  372 PHE   A CG  
2288 C  CD1 . PHE   A 295 ? 0.46010 0.35374 0.35489 -0.05511 -0.01961 0.00359  372 PHE   A CD1 
2289 C  CD2 . PHE   A 295 ? 0.47933 0.35575 0.35306 -0.06494 -0.02222 0.00443  372 PHE   A CD2 
2290 C  CE1 . PHE   A 295 ? 0.44362 0.32558 0.32672 -0.05522 -0.01702 0.00094  372 PHE   A CE1 
2291 C  CE2 . PHE   A 295 ? 0.49777 0.36159 0.35908 -0.06492 -0.01946 0.00161  372 PHE   A CE2 
2292 C  CZ  . PHE   A 295 ? 0.47317 0.34023 0.33956 -0.05996 -0.01678 -0.00006 372 PHE   A CZ  
2293 N  N   . GLY   A 296 ? 0.42898 0.31650 0.32234 -0.04816 -0.01366 -0.00058 373 GLY   A N   
2294 C  CA  . GLY   A 296 ? 0.42766 0.30112 0.30773 -0.04839 -0.01093 -0.00312 373 GLY   A CA  
2295 C  C   . GLY   A 296 ? 0.49512 0.36975 0.37877 -0.04416 -0.00853 -0.00444 373 GLY   A C   
2296 O  O   . GLY   A 296 ? 0.50015 0.36284 0.37328 -0.04285 -0.00535 -0.00689 373 GLY   A O   
2297 N  N   . ILE   A 297 ? 0.43504 0.32290 0.33249 -0.04183 -0.00968 -0.00290 374 ILE   A N   
2298 C  CA  . ILE   A 297 ? 0.47722 0.36493 0.37608 -0.03930 -0.00806 -0.00376 374 ILE   A CA  
2299 C  C   . ILE   A 297 ? 0.49486 0.37720 0.39198 -0.03237 -0.00273 -0.00744 374 ILE   A C   
2300 O  O   . ILE   A 297 ? 0.51362 0.39066 0.40677 -0.03085 -0.00086 -0.00861 374 ILE   A O   
2301 C  CB  . ILE   A 297 ? 0.44691 0.34950 0.36064 -0.03755 -0.00969 -0.00160 374 ILE   A CB  
2302 C  CG1 . ILE   A 297 ? 0.46252 0.37707 0.38807 -0.03597 -0.01102 -0.00002 374 ILE   A CG1 
2303 C  CG2 . ILE   A 297 ? 0.46037 0.36358 0.37202 -0.04322 -0.01308 0.00126  374 ILE   A CG2 
2304 C  CD1 . ILE   A 297 ? 0.42171 0.33802 0.35211 -0.02923 -0.00733 -0.00286 374 ILE   A CD1 
2305 N  N   . PHE   A 298 ? 0.45961 0.34407 0.36043 -0.02796 -0.00027 -0.00899 375 PHE   A N   
2306 C  CA  . PHE   A 298 ? 0.47583 0.35726 0.37679 -0.02118 0.00468  -0.01181 375 PHE   A CA  
2307 C  C   . PHE   A 298 ? 0.48892 0.35742 0.37738 -0.02077 0.00782  -0.01373 375 PHE   A C   
2308 O  O   . PHE   A 298 ? 0.51069 0.37809 0.40034 -0.01496 0.01203  -0.01556 375 PHE   A O   
2309 C  CB  . PHE   A 298 ? 0.43690 0.33067 0.35184 -0.01574 0.00572  -0.01208 375 PHE   A CB  
2310 C  CG  . PHE   A 298 ? 0.40652 0.31210 0.33321 -0.01522 0.00352  -0.01049 375 PHE   A CG  
2311 C  CD1 . PHE   A 298 ? 0.44105 0.34607 0.36705 -0.01623 0.00291  -0.00996 375 PHE   A CD1 
2312 C  CD2 . PHE   A 298 ? 0.40361 0.32042 0.34159 -0.01373 0.00220  -0.00944 375 PHE   A CD2 
2313 C  CE1 . PHE   A 298 ? 0.42913 0.34507 0.36582 -0.01561 0.00121  -0.00840 375 PHE   A CE1 
2314 C  CE2 . PHE   A 298 ? 0.40836 0.33538 0.35657 -0.01292 0.00065  -0.00794 375 PHE   A CE2 
2315 C  CZ  . PHE   A 298 ? 0.39745 0.32422 0.34510 -0.01383 0.00024  -0.00741 375 PHE   A CZ  
2316 N  N   . SER   A 299 ? 0.48606 0.34466 0.36228 -0.02691 0.00594  -0.01313 376 SER   A N   
2317 C  CA  . SER   A 299 ? 0.49187 0.33731 0.35509 -0.02677 0.00910  -0.01494 376 SER   A CA  
2318 C  C   . SER   A 299 ? 0.51625 0.35011 0.37037 -0.02302 0.01384  -0.01706 376 SER   A C   
2319 O  O   . SER   A 299 ? 0.49658 0.32174 0.34314 -0.01998 0.01812  -0.01877 376 SER   A O   
2320 C  CB  . SER   A 299 ? 0.46294 0.29983 0.31424 -0.03491 0.00562  -0.01366 376 SER   A CB  
2321 O  OG  . SER   A 299 ? 0.56267 0.39742 0.41032 -0.03999 0.00232  -0.01209 376 SER   A OG  
2322 N  N   . ARG   A 300 ? 0.52304 0.35664 0.37776 -0.02296 0.01336  -0.01680 377 ARG   A N   
2323 C  CA  . ARG   A 300 ? 0.50691 0.33071 0.35457 -0.01873 0.01787  -0.01853 377 ARG   A CA  
2324 C  C   . ARG   A 300 ? 0.50242 0.33660 0.36317 -0.01161 0.02020  -0.01890 377 ARG   A C   
2325 O  O   . ARG   A 300 ? 0.47223 0.29999 0.32904 -0.00722 0.02413  -0.02000 377 ARG   A O   
2326 C  CB  . ARG   A 300 ? 0.50911 0.32286 0.34586 -0.02395 0.01591  -0.01802 377 ARG   A CB  
2327 C  CG  . ARG   A 300 ? 0.57197 0.37460 0.39456 -0.03182 0.01319  -0.01742 377 ARG   A CG  
2328 C  CD  . ARG   A 300 ? 0.70556 0.49612 0.51529 -0.03706 0.01166  -0.01703 377 ARG   A CD  
2329 N  NE  . ARG   A 300 ? 0.72953 0.51450 0.52968 -0.04626 0.00694  -0.01534 377 ARG   A NE  
2330 C  CZ  . ARG   A 300 ? 0.77118 0.54621 0.55947 -0.05314 0.00409  -0.01430 377 ARG   A CZ  
2331 N  NH1 . ARG   A 300 ? 0.77395 0.54193 0.55718 -0.05177 0.00580  -0.01506 377 ARG   A NH1 
2332 N  NH2 . ARG   A 300 ? 0.76237 0.53466 0.54375 -0.06188 -0.00083 -0.01218 377 ARG   A NH2 
2333 N  N   . ALA   A 301 ? 0.46218 0.31179 0.33793 -0.01038 0.01792  -0.01786 378 ALA   A N   
2334 C  CA  . ALA   A 301 ? 0.50605 0.36527 0.39350 -0.00474 0.01937  -0.01799 378 ALA   A CA  
2335 C  C   . ALA   A 301 ? 0.49577 0.35560 0.38590 0.00185  0.02399  -0.01916 378 ALA   A C   
2336 O  O   . ALA   A 301 ? 0.43528 0.30541 0.33574 0.00439  0.02388  -0.01892 378 ALA   A O   
2337 C  CB  . ALA   A 301 ? 0.44966 0.32372 0.35078 -0.00586 0.01557  -0.01648 378 ALA   A CB  
2338 N  N   . LYS   A 302 ? 0.48744 0.33589 0.36795 0.00473  0.02823  -0.02022 379 LYS   A N   
2339 C  CA  . LYS   A 302 ? 0.52673 0.37450 0.40820 0.01080  0.03305  -0.02087 379 LYS   A CA  
2340 C  C   . LYS   A 302 ? 0.52850 0.38979 0.42470 0.01608  0.03372  -0.02026 379 LYS   A C   
2341 O  O   . LYS   A 302 ? 0.51550 0.38156 0.41676 0.01982  0.03598  -0.02015 379 LYS   A O   
2342 C  CB  . LYS   A 302 ? 0.55807 0.39142 0.42710 0.01352  0.03775  -0.02171 379 LYS   A CB  
2343 C  CG  . LYS   A 302 ? 0.60699 0.42833 0.46361 0.01298  0.04075  -0.02260 379 LYS   A CG  
2344 C  CD  . LYS   A 302 ? 0.71765 0.52670 0.56020 0.00574  0.03815  -0.02305 379 LYS   A CD  
2345 C  CE  . LYS   A 302 ? 0.74009 0.53271 0.56669 0.00648  0.04277  -0.02426 379 LYS   A CE  
2346 N  NZ  . LYS   A 302 ? 0.85106 0.63867 0.67598 0.01406  0.04889  -0.02459 379 LYS   A NZ  
2347 N  N   . VAL   A 303 ? 0.48681 0.35426 0.38962 0.01618  0.03172  -0.01972 380 VAL   A N   
2348 C  CA  . VAL   A 303 ? 0.48307 0.36191 0.39831 0.02088  0.03238  -0.01913 380 VAL   A CA  
2349 C  C   . VAL   A 303 ? 0.42767 0.31841 0.35357 0.01850  0.02805  -0.01850 380 VAL   A C   
2350 O  O   . VAL   A 303 ? 0.46606 0.36485 0.40068 0.02125  0.02791  -0.01806 380 VAL   A O   
2351 C  CB  . VAL   A 303 ? 0.48519 0.36040 0.39891 0.02483  0.03515  -0.01895 380 VAL   A CB  
2352 C  CG1 . VAL   A 303 ? 0.44849 0.31092 0.35095 0.02769  0.04002  -0.01941 380 VAL   A CG1 
2353 C  CG2 . VAL   A 303 ? 0.45020 0.32339 0.36165 0.02130  0.03237  -0.01888 380 VAL   A CG2 
2354 N  N   . LEU   A 304 ? 0.43190 0.32368 0.35697 0.01345  0.02461  -0.01825 381 LEU   A N   
2355 C  CA  . LEU   A 304 ? 0.40054 0.30395 0.33622 0.01203  0.02116  -0.01743 381 LEU   A CA  
2356 C  C   . LEU   A 304 ? 0.40920 0.32117 0.35399 0.01583  0.02218  -0.01745 381 LEU   A C   
2357 O  O   . LEU   A 304 ? 0.40749 0.31800 0.35058 0.01642  0.02342  -0.01770 381 LEU   A O   
2358 C  CB  . LEU   A 304 ? 0.41234 0.31555 0.34569 0.00635  0.01763  -0.01665 381 LEU   A CB  
2359 C  CG  . LEU   A 304 ? 0.42148 0.33634 0.36554 0.00506  0.01433  -0.01545 381 LEU   A CG  
2360 C  CD1 . LEU   A 304 ? 0.44818 0.36648 0.39573 0.00477  0.01318  -0.01483 381 LEU   A CD1 
2361 C  CD2 . LEU   A 304 ? 0.41650 0.33126 0.35836 -0.00008 0.01118  -0.01422 381 LEU   A CD2 
2362 N  N   . SER   A 305 ? 0.41915 0.33960 0.37301 0.01819  0.02169  -0.01713 382 SER   A N   
2363 C  CA  . SER   A 305 ? 0.42388 0.35209 0.38578 0.02115  0.02226  -0.01700 382 SER   A CA  
2364 C  C   . SER   A 305 ? 0.36893 0.30686 0.34029 0.02097  0.01980  -0.01655 382 SER   A C   
2365 O  O   . SER   A 305 ? 0.33525 0.27904 0.31256 0.02267  0.01981  -0.01642 382 SER   A O   
2366 C  CB  . SER   A 305 ? 0.41875 0.34625 0.38118 0.02593  0.02571  -0.01695 382 SER   A CB  
2367 O  OG  . SER   A 305 ? 0.44117 0.36818 0.40389 0.02708  0.02601  -0.01680 382 SER   A OG  
2368 N  N   . LYS   A 306 ? 0.36101 0.30053 0.33357 0.01894  0.01783  -0.01620 383 LYS   A N   
2369 C  CA  . LYS   A 306 ? 0.35944 0.30728 0.34003 0.01866  0.01578  -0.01570 383 LYS   A CA  
2370 C  C   . LYS   A 306 ? 0.37881 0.32694 0.35847 0.01463  0.01321  -0.01477 383 LYS   A C   
2371 O  O   . LYS   A 306 ? 0.37969 0.32439 0.35544 0.01288  0.01281  -0.01446 383 LYS   A O   
2372 C  CB  . LYS   A 306 ? 0.35149 0.30274 0.33611 0.02113  0.01643  -0.01580 383 LYS   A CB  
2373 C  CG  . LYS   A 306 ? 0.44237 0.39400 0.42825 0.02489  0.01871  -0.01607 383 LYS   A CG  
2374 C  CD  . LYS   A 306 ? 0.53714 0.49231 0.52681 0.02663  0.01879  -0.01589 383 LYS   A CD  
2375 C  CE  . LYS   A 306 ? 0.62338 0.57785 0.61305 0.03006  0.02105  -0.01556 383 LYS   A CE  
2376 N  NZ  . LYS   A 306 ? 0.65455 0.61265 0.64782 0.03133  0.02075  -0.01518 383 LYS   A NZ  
2377 N  N   . LEU   A 307 ? 0.35336 0.30578 0.33670 0.01311  0.01143  -0.01403 384 LEU   A N   
2378 C  CA  . LEU   A 307 ? 0.34247 0.29704 0.32659 0.00947  0.00885  -0.01244 384 LEU   A CA  
2379 C  C   . LEU   A 307 ? 0.37870 0.34179 0.37164 0.01079  0.00794  -0.01166 384 LEU   A C   
2380 O  O   . LEU   A 307 ? 0.38750 0.35327 0.38387 0.01235  0.00814  -0.01199 384 LEU   A O   
2381 C  CB  . LEU   A 307 ? 0.31245 0.26307 0.29146 0.00602  0.00751  -0.01176 384 LEU   A CB  
2382 C  CG  . LEU   A 307 ? 0.37523 0.32941 0.35605 0.00198  0.00441  -0.00941 384 LEU   A CG  
2383 C  CD1 . LEU   A 307 ? 0.34446 0.29783 0.32332 -0.00035 0.00344  -0.00834 384 LEU   A CD1 
2384 C  CD2 . LEU   A 307 ? 0.33164 0.28172 0.30702 -0.00167 0.00288  -0.00864 384 LEU   A CD2 
2385 N  N   . ASN   A 308 ? 0.33426 0.30117 0.33048 0.01026  0.00716  -0.01061 385 ASN   A N   
2386 C  CA  . ASN   A 308 ? 0.30738 0.28161 0.31123 0.01166  0.00672  -0.00970 385 ASN   A CA  
2387 C  C   . ASN   A 308 ? 0.30832 0.28603 0.31408 0.00849  0.00455  -0.00704 385 ASN   A C   
2388 O  O   . ASN   A 308 ? 0.33868 0.31664 0.34334 0.00651  0.00387  -0.00584 385 ASN   A O   
2389 C  CB  . ASN   A 308 ? 0.34401 0.32040 0.35060 0.01424  0.00810  -0.01046 385 ASN   A CB  
2390 C  CG  . ASN   A 308 ? 0.33487 0.31716 0.34810 0.01643  0.00837  -0.01008 385 ASN   A CG  
2391 O  OD1 . ASN   A 308 ? 0.30856 0.29426 0.32509 0.01575  0.00736  -0.00859 385 ASN   A OD1 
2392 N  ND2 . ASN   A 308 ? 0.30969 0.29276 0.32442 0.01900  0.00978  -0.01129 385 ASN   A ND2 
2393 N  N   . MET   A 309 ? 0.34893 0.32946 0.35751 0.00784  0.00336  -0.00581 386 MET   A N   
2394 C  CA  . MET   A 309 ? 0.33229 0.31752 0.34407 0.00515  0.00119  -0.00265 386 MET   A CA  
2395 C  C   . MET   A 309 ? 0.36403 0.35628 0.38392 0.00793  0.00163  -0.00141 386 MET   A C   
2396 O  O   . MET   A 309 ? 0.36020 0.35687 0.38378 0.00656  0.00006  0.00141  386 MET   A O   
2397 C  CB  . MET   A 309 ? 0.31672 0.29920 0.32470 0.00175  -0.00079 -0.00165 386 MET   A CB  
2398 C  CG  . MET   A 309 ? 0.37073 0.34523 0.36938 -0.00167 -0.00133 -0.00242 386 MET   A CG  
2399 S  SD  . MET   A 309 ? 0.39000 0.36500 0.38624 -0.00674 -0.00379 0.00055  386 MET   A SD  
2400 C  CE  . MET   A 309 ? 0.37481 0.35847 0.37807 -0.00914 -0.00672 0.00490  386 MET   A CE  
2401 N  N   . LYS   A 310 ? 0.32759 0.32058 0.34990 0.01177  0.00378  -0.00327 387 LYS   A N   
2402 C  CA  . LYS   A 310 ? 0.32553 0.32348 0.35413 0.01471  0.00468  -0.00246 387 LYS   A CA  
2403 C  C   . LYS   A 310 ? 0.32805 0.33205 0.36144 0.01408  0.00422  0.00084  387 LYS   A C   
2404 O  O   . LYS   A 310 ? 0.31894 0.32367 0.35142 0.01254  0.00406  0.00167  387 LYS   A O   
2405 C  CB  . LYS   A 310 ? 0.29063 0.28727 0.31944 0.01820  0.00695  -0.00502 387 LYS   A CB  
2406 C  CG  . LYS   A 310 ? 0.34543 0.34534 0.37907 0.02129  0.00820  -0.00454 387 LYS   A CG  
2407 C  CD  . LYS   A 310 ? 0.33778 0.33617 0.37083 0.02404  0.01026  -0.00671 387 LYS   A CD  
2408 C  CE  . LYS   A 310 ? 0.42414 0.42368 0.46016 0.02694  0.01158  -0.00660 387 LYS   A CE  
2409 N  NZ  . LYS   A 310 ? 0.48646 0.48382 0.52092 0.02911  0.01342  -0.00860 387 LYS   A NZ  
2410 N  N   . ASP   A 311 ? 0.33122 0.33972 0.36986 0.01533  0.00407  0.00302  388 ASP   A N   
2411 C  CA  . ASP   A 311 ? 0.32167 0.33696 0.36631 0.01603  0.00438  0.00651  388 ASP   A CA  
2412 C  C   . ASP   A 311 ? 0.32529 0.34362 0.36990 0.01154  0.00191  0.00985  388 ASP   A C   
2413 O  O   . ASP   A 311 ? 0.35137 0.37297 0.39757 0.01086  0.00223  0.01151  388 ASP   A O   
2414 C  CB  . ASP   A 311 ? 0.29197 0.30797 0.33796 0.01926  0.00715  0.00532  388 ASP   A CB  
2415 C  CG  . ASP   A 311 ? 0.32096 0.34406 0.37332 0.02070  0.00821  0.00900  388 ASP   A CG  
2416 O  OD1 . ASP   A 311 ? 0.34741 0.37535 0.40419 0.02004  0.00701  0.01254  388 ASP   A OD1 
2417 O  OD2 . ASP   A 311 ? 0.36969 0.39382 0.42275 0.02247  0.01028  0.00865  388 ASP   A OD2 
2418 N  N   . ASN   A 312 ? 0.27163 0.28870 0.31403 0.00812  -0.00069 0.01098  389 ASN   A N   
2419 C  CA  . ASN   A 312 ? 0.30697 0.32709 0.34928 0.00324  -0.00359 0.01479  389 ASN   A CA  
2420 C  C   . ASN   A 312 ? 0.33661 0.36202 0.38393 0.00249  -0.00540 0.01857  389 ASN   A C   
2421 O  O   . ASN   A 312 ? 0.37463 0.40351 0.42760 0.00659  -0.00375 0.01916  389 ASN   A O   
2422 C  CB  . ASN   A 312 ? 0.35719 0.36974 0.39046 -0.00115 -0.00537 0.01295  389 ASN   A CB  
2423 C  CG  . ASN   A 312 ? 0.32723 0.33641 0.35643 -0.00163 -0.00434 0.01116  389 ASN   A CG  
2424 O  OD1 . ASN   A 312 ? 0.33612 0.34848 0.36609 -0.00435 -0.00550 0.01385  389 ASN   A OD1 
2425 N  ND2 . ASN   A 312 ? 0.30345 0.30659 0.32858 0.00095  -0.00224 0.00695  389 ASN   A ND2 
2426 N  N   . GLN   A 313 ? 0.28413 0.30972 0.32899 -0.00278 -0.00880 0.02124  390 GLN   A N   
2427 C  CA  . GLN   A 313 ? 0.32057 0.35182 0.37032 -0.00414 -0.01102 0.02554  390 GLN   A CA  
2428 C  C   . GLN   A 313 ? 0.34273 0.36815 0.38627 -0.00753 -0.01337 0.02447  390 GLN   A C   
2429 O  O   . GLN   A 313 ? 0.33208 0.36054 0.37642 -0.01154 -0.01656 0.02838  390 GLN   A O   
2430 C  CB  . GLN   A 313 ? 0.33059 0.36973 0.38462 -0.00788 -0.01343 0.03129  390 GLN   A CB  
2431 C  CG  . GLN   A 313 ? 0.33158 0.37829 0.39325 -0.00433 -0.01100 0.03348  390 GLN   A CG  
2432 C  CD  . GLN   A 313 ? 0.37019 0.42333 0.44073 0.00110  -0.00884 0.03566  390 GLN   A CD  
2433 O  OE1 . GLN   A 313 ? 0.42555 0.48543 0.50176 0.00007  -0.01069 0.04063  390 GLN   A OE1 
2434 N  NE2 . GLN   A 313 ? 0.37385 0.42447 0.44519 0.00682  -0.00494 0.03208  390 GLN   A NE2 
2435 N  N   . LEU   A 314 ? 0.28788 0.30522 0.32533 -0.00600 -0.01179 0.01950  391 LEU   A N   
2436 C  CA  . LEU   A 314 ? 0.32936 0.34059 0.36033 -0.00887 -0.01344 0.01820  391 LEU   A CA  
2437 C  C   . LEU   A 314 ? 0.37442 0.38926 0.41029 -0.00749 -0.01420 0.02007  391 LEU   A C   
2438 O  O   . LEU   A 314 ? 0.38925 0.40578 0.42981 -0.00248 -0.01187 0.01879  391 LEU   A O   
2439 C  CB  . LEU   A 314 ? 0.32301 0.32566 0.34719 -0.00695 -0.01106 0.01281  391 LEU   A CB  
2440 C  CG  . LEU   A 314 ? 0.35295 0.35071 0.37134 -0.00804 -0.01012 0.01068  391 LEU   A CG  
2441 C  CD1 . LEU   A 314 ? 0.36275 0.35210 0.37425 -0.00645 -0.00803 0.00611  391 LEU   A CD1 
2442 C  CD2 . LEU   A 314 ? 0.35766 0.35409 0.37120 -0.01420 -0.01314 0.01341  391 LEU   A CD2 
2443 N  N   . THR   A 315 ? 0.34099 0.35646 0.37517 -0.01215 -0.01757 0.02316  392 THR   A N   
2444 C  CA  . THR   A 315 ? 0.36672 0.38425 0.40403 -0.01150 -0.01863 0.02476  392 THR   A CA  
2445 C  C   . THR   A 315 ? 0.40675 0.41612 0.43565 -0.01390 -0.01939 0.02198  392 THR   A C   
2446 O  O   . THR   A 315 ? 0.42972 0.43951 0.46031 -0.01291 -0.01981 0.02237  392 THR   A O   
2447 C  CB  . THR   A 315 ? 0.31938 0.34496 0.36227 -0.01475 -0.02202 0.03114  392 THR   A CB  
2448 O  OG1 . THR   A 315 ? 0.42555 0.44946 0.46273 -0.02122 -0.02503 0.03300  392 THR   A OG1 
2449 C  CG2 . THR   A 315 ? 0.28255 0.31742 0.33575 -0.01076 -0.02054 0.03438  392 THR   A CG2 
2450 N  N   . SER   A 316 ? 0.42541 0.42711 0.44509 -0.01691 -0.01939 0.01933  393 SER   A N   
2451 C  CA  . SER   A 316 ? 0.43501 0.42826 0.44642 -0.01797 -0.01891 0.01604  393 SER   A CA  
2452 C  C   . SER   A 316 ? 0.40353 0.38883 0.40654 -0.01860 -0.01710 0.01243  393 SER   A C   
2453 O  O   . SER   A 316 ? 0.40332 0.38969 0.40697 -0.01846 -0.01656 0.01251  393 SER   A O   
2454 C  CB  . SER   A 316 ? 0.40624 0.39790 0.41334 -0.02352 -0.02246 0.01878  393 SER   A CB  
2455 O  OG  . SER   A 316 ? 0.49379 0.48260 0.49458 -0.02924 -0.02484 0.02048  393 SER   A OG  
2456 N  N   . LEU   A 317 ? 0.42030 0.39751 0.41527 -0.01923 -0.01606 0.00947  394 LEU   A N   
2457 C  CA  . LEU   A 317 ? 0.38353 0.35218 0.36980 -0.01936 -0.01392 0.00609  394 LEU   A CA  
2458 C  C   . LEU   A 317 ? 0.42086 0.38130 0.39602 -0.02522 -0.01579 0.00654  394 LEU   A C   
2459 O  O   . LEU   A 317 ? 0.44846 0.40862 0.42198 -0.02815 -0.01794 0.00822  394 LEU   A O   
2460 C  CB  . LEU   A 317 ? 0.39499 0.36080 0.38104 -0.01447 -0.01038 0.00228  394 LEU   A CB  
2461 C  CG  . LEU   A 317 ? 0.44849 0.42097 0.44389 -0.00914 -0.00854 0.00159  394 LEU   A CG  
2462 C  CD1 . LEU   A 317 ? 0.37725 0.34831 0.37343 -0.00500 -0.00585 -0.00130 394 LEU   A CD1 
2463 C  CD2 . LEU   A 317 ? 0.36593 0.33848 0.36144 -0.00826 -0.00745 0.00096  394 LEU   A CD2 
2464 N  N   . PRO   A 318 ? 0.44523 0.39827 0.41199 -0.02714 -0.01501 0.00510  395 PRO   A N   
2465 C  CA  . PRO   A 318 ? 0.41449 0.35863 0.36937 -0.03333 -0.01696 0.00575  395 PRO   A CA  
2466 C  C   . PRO   A 318 ? 0.39821 0.33424 0.34510 -0.03329 -0.01529 0.00337  395 PRO   A C   
2467 O  O   . PRO   A 318 ? 0.36572 0.30149 0.31478 -0.02821 -0.01195 0.00062  395 PRO   A O   
2468 C  CB  . PRO   A 318 ? 0.41462 0.35238 0.36295 -0.03393 -0.01560 0.00420  395 PRO   A CB  
2469 C  CG  . PRO   A 318 ? 0.37449 0.31451 0.32850 -0.02693 -0.01156 0.00115  395 PRO   A CG  
2470 C  CD  . PRO   A 318 ? 0.36298 0.31451 0.32990 -0.02366 -0.01215 0.00269  395 PRO   A CD  
2471 N  N   . LEU   A 319 ? 0.44361 0.37263 0.38048 -0.03940 -0.01768 0.00462  396 LEU   A N   
2472 C  CA  . LEU   A 319 ? 0.43505 0.35607 0.36343 -0.04017 -0.01637 0.00284  396 LEU   A CA  
2473 C  C   . LEU   A 319 ? 0.45478 0.36712 0.37645 -0.03593 -0.01127 -0.00141 396 LEU   A C   
2474 O  O   . LEU   A 319 ? 0.44498 0.35437 0.36444 -0.03363 -0.00884 -0.00322 396 LEU   A O   
2475 C  CB  . LEU   A 319 ? 0.46420 0.37736 0.38086 -0.04801 -0.01971 0.00477  396 LEU   A CB  
2476 C  CG  . LEU   A 319 ? 0.48071 0.39896 0.39973 -0.05318 -0.02455 0.00887  396 LEU   A CG  
2477 C  CD1 . LEU   A 319 ? 0.45375 0.36172 0.35846 -0.06136 -0.02748 0.01027  396 LEU   A CD1 
2478 C  CD2 . LEU   A 319 ? 0.46290 0.38254 0.38425 -0.05085 -0.02353 0.00808  396 LEU   A CD2 
2479 N  N   . ASP   A 320 ? 0.43437 0.34248 0.35252 -0.03501 -0.00959 -0.00275 397 ASP   A N   
2480 C  CA  . ASP   A 320 ? 0.43936 0.33840 0.35017 -0.03129 -0.00478 -0.00625 397 ASP   A CA  
2481 C  C   . ASP   A 320 ? 0.43148 0.33759 0.35260 -0.02419 -0.00168 -0.00787 397 ASP   A C   
2482 O  O   . ASP   A 320 ? 0.46827 0.36900 0.38563 -0.02059 0.00212  -0.01019 397 ASP   A O   
2483 C  CB  . ASP   A 320 ? 0.39253 0.28132 0.29195 -0.03484 -0.00486 -0.00659 397 ASP   A CB  
2484 C  CG  . ASP   A 320 ? 0.44694 0.34245 0.35288 -0.03604 -0.00740 -0.00469 397 ASP   A CG  
2485 O  OD1 . ASP   A 320 ? 0.41340 0.32139 0.33229 -0.03453 -0.00928 -0.00281 397 ASP   A OD1 
2486 O  OD2 . ASP   A 320 ? 0.48738 0.37532 0.38516 -0.03841 -0.00733 -0.00501 397 ASP   A OD2 
2487 N  N   . PHE   A 321 ? 0.44669 0.36449 0.38041 -0.02221 -0.00328 -0.00649 398 PHE   A N   
2488 C  CA  . PHE   A 321 ? 0.44302 0.36779 0.38646 -0.01616 -0.00092 -0.00774 398 PHE   A CA  
2489 C  C   . PHE   A 321 ? 0.45718 0.37821 0.39844 -0.01162 0.00335  -0.01035 398 PHE   A C   
2490 O  O   . PHE   A 321 ? 0.48196 0.40392 0.42599 -0.00729 0.00609  -0.01180 398 PHE   A O   
2491 C  CB  . PHE   A 321 ? 0.43488 0.37086 0.38998 -0.01553 -0.00342 -0.00568 398 PHE   A CB  
2492 C  CG  . PHE   A 321 ? 0.47107 0.41338 0.43504 -0.00992 -0.00127 -0.00694 398 PHE   A CG  
2493 C  CD1 . PHE   A 321 ? 0.47168 0.41687 0.44020 -0.00630 0.00045  -0.00799 398 PHE   A CD1 
2494 C  CD2 . PHE   A 321 ? 0.43132 0.37694 0.39914 -0.00868 -0.00136 -0.00681 398 PHE   A CD2 
2495 C  CE1 . PHE   A 321 ? 0.48082 0.43171 0.45712 -0.00166 0.00207  -0.00895 398 PHE   A CE1 
2496 C  CE2 . PHE   A 321 ? 0.45628 0.40739 0.43176 -0.00406 0.00028  -0.00779 398 PHE   A CE2 
2497 C  CZ  . PHE   A 321 ? 0.47579 0.42943 0.45532 -0.00066 0.00194  -0.00885 398 PHE   A CZ  
2498 N  N   . GLY   A 322 ? 0.46133 0.37824 0.39755 -0.01261 0.00402  -0.01071 399 GLY   A N   
2499 C  CA  . GLY   A 322 ? 0.44427 0.35848 0.37894 -0.00830 0.00820  -0.01267 399 GLY   A CA  
2500 C  C   . GLY   A 322 ? 0.47500 0.37889 0.39960 -0.00702 0.01192  -0.01440 399 GLY   A C   
2501 O  O   . GLY   A 322 ? 0.51395 0.41563 0.43715 -0.00318 0.01580  -0.01565 399 GLY   A O   
2502 N  N   . THR   A 323 ? 0.47837 0.37572 0.39573 -0.01010 0.01098  -0.01429 400 THR   A N   
2503 C  CA  . THR   A 323 ? 0.46567 0.35221 0.37287 -0.00862 0.01470  -0.01592 400 THR   A CA  
2504 C  C   . THR   A 323 ? 0.45954 0.34941 0.37236 -0.00398 0.01676  -0.01661 400 THR   A C   
2505 O  O   . THR   A 323 ? 0.48149 0.36312 0.38707 -0.00176 0.02027  -0.01781 400 THR   A O   
2506 C  CB  . THR   A 323 ? 0.47637 0.35242 0.37116 -0.01462 0.01274  -0.01552 400 THR   A CB  
2507 O  OG1 . THR   A 323 ? 0.44434 0.32561 0.34392 -0.01736 0.00901  -0.01400 400 THR   A OG1 
2508 C  CG2 . THR   A 323 ? 0.43722 0.30976 0.32589 -0.01974 0.01038  -0.01459 400 THR   A CG2 
2509 N  N   . TRP   A 324 ? 0.42948 0.33066 0.35447 -0.00243 0.01479  -0.01580 401 TRP   A N   
2510 C  CA  . TRP   A 324 ? 0.46792 0.37274 0.39842 0.00146  0.01625  -0.01627 401 TRP   A CA  
2511 C  C   . TRP   A 324 ? 0.48154 0.38856 0.41583 0.00732  0.02023  -0.01719 401 TRP   A C   
2512 O  O   . TRP   A 324 ? 0.39727 0.31351 0.34175 0.01033  0.02008  -0.01693 401 TRP   A O   
2513 C  CB  . TRP   A 324 ? 0.42587 0.34135 0.36713 0.00083  0.01289  -0.01502 401 TRP   A CB  
2514 C  CG  . TRP   A 324 ? 0.45071 0.36636 0.39028 -0.00475 0.00884  -0.01333 401 TRP   A CG  
2515 C  CD1 . TRP   A 324 ? 0.48237 0.38914 0.41126 -0.00965 0.00757  -0.01289 401 TRP   A CD1 
2516 C  CD2 . TRP   A 324 ? 0.43245 0.35781 0.38132 -0.00603 0.00555  -0.01150 401 TRP   A CD2 
2517 N  NE1 . TRP   A 324 ? 0.43920 0.35053 0.37088 -0.01420 0.00335  -0.01058 401 TRP   A NE1 
2518 C  CE2 . TRP   A 324 ? 0.40854 0.33147 0.35275 -0.01173 0.00229  -0.00964 401 TRP   A CE2 
2519 C  CE3 . TRP   A 324 ? 0.43135 0.36688 0.39167 -0.00290 0.00518  -0.01110 401 TRP   A CE3 
2520 C  CZ2 . TRP   A 324 ? 0.43159 0.36295 0.38320 -0.01400 -0.00113 -0.00709 401 TRP   A CZ2 
2521 C  CZ3 . TRP   A 324 ? 0.42614 0.36891 0.39298 -0.00489 0.00211  -0.00894 401 TRP   A CZ3 
2522 C  CH2 . TRP   A 324 ? 0.44965 0.39085 0.41266 -0.01020 -0.00092 -0.00681 401 TRP   A CH2 
2523 N  N   . THR   A 325 ? 0.40616 0.30417 0.33158 0.00884  0.02394  -0.01808 402 THR   A N   
2524 C  CA  . THR   A 325 ? 0.42209 0.32240 0.35065 0.01387  0.02772  -0.01832 402 THR   A CA  
2525 C  C   . THR   A 325 ? 0.42376 0.32700 0.35709 0.01882  0.03026  -0.01831 402 THR   A C   
2526 O  O   . THR   A 325 ? 0.45226 0.35893 0.38950 0.02301  0.03316  -0.01795 402 THR   A O   
2527 C  CB  . THR   A 325 ? 0.43154 0.32144 0.34902 0.01405  0.03123  -0.01895 402 THR   A CB  
2528 O  OG1 . THR   A 325 ? 0.39432 0.27263 0.30076 0.01349  0.03313  -0.01972 402 THR   A OG1 
2529 C  CG2 . THR   A 325 ? 0.43659 0.32464 0.35018 0.00929  0.02868  -0.01876 402 THR   A CG2 
2530 N  N   . SER   A 326 ? 0.42501 0.32762 0.35853 0.01842  0.02919  -0.01839 403 SER   A N   
2531 C  CA  . SER   A 326 ? 0.42319 0.33000 0.36248 0.02295  0.03109  -0.01811 403 SER   A CA  
2532 C  C   . SER   A 326 ? 0.44016 0.35724 0.38986 0.02254  0.02779  -0.01762 403 SER   A C   
2533 O  O   . SER   A 326 ? 0.46632 0.38702 0.42068 0.02551  0.02866  -0.01732 403 SER   A O   
2534 C  CB  . SER   A 326 ? 0.45269 0.34982 0.38350 0.02412  0.03361  -0.01856 403 SER   A CB  
2535 O  OG  . SER   A 326 ? 0.49792 0.38931 0.42241 0.01945  0.03097  -0.01896 403 SER   A OG  
2536 N  N   . MET   A 327 ? 0.40563 0.32755 0.35914 0.01918  0.02424  -0.01736 404 MET   A N   
2537 C  CA  . MET   A 327 ? 0.36732 0.29820 0.33001 0.01904  0.02157  -0.01689 404 MET   A CA  
2538 C  C   . MET   A 327 ? 0.40305 0.34183 0.37418 0.02256  0.02241  -0.01658 404 MET   A C   
2539 O  O   . MET   A 327 ? 0.41455 0.35475 0.38671 0.02347  0.02335  -0.01639 404 MET   A O   
2540 C  CB  . MET   A 327 ? 0.35653 0.29030 0.32100 0.01494  0.01794  -0.01632 404 MET   A CB  
2541 C  CG  . MET   A 327 ? 0.40799 0.34915 0.38014 0.01476  0.01566  -0.01575 404 MET   A CG  
2542 S  SD  . MET   A 327 ? 0.51537 0.45738 0.48697 0.00970  0.01189  -0.01446 404 MET   A SD  
2543 C  CE  . MET   A 327 ? 0.40546 0.33742 0.36626 0.00694  0.01230  -0.01465 404 MET   A CE  
2544 N  N   . VAL   A 328 ? 0.35864 0.30246 0.33548 0.02419  0.02190  -0.01639 405 VAL   A N   
2545 C  CA  . VAL   A 328 ? 0.37221 0.32314 0.35643 0.02696  0.02229  -0.01591 405 VAL   A CA  
2546 C  C   . VAL   A 328 ? 0.36377 0.32138 0.35464 0.02570  0.01941  -0.01581 405 VAL   A C   
2547 O  O   . VAL   A 328 ? 0.34506 0.30761 0.34076 0.02637  0.01884  -0.01550 405 VAL   A O   
2548 C  CB  . VAL   A 328 ? 0.36035 0.31124 0.34523 0.03022  0.02442  -0.01553 405 VAL   A CB  
2549 C  CG1 . VAL   A 328 ? 0.33526 0.29386 0.32768 0.03230  0.02420  -0.01468 405 VAL   A CG1 
2550 C  CG2 . VAL   A 328 ? 0.33610 0.28033 0.31462 0.03230  0.02793  -0.01535 405 VAL   A CG2 
2551 N  N   . GLU   A 329 ? 0.35853 0.31609 0.34941 0.02391  0.01772  -0.01593 406 GLU   A N   
2552 C  CA  . GLU   A 329 ? 0.35334 0.31659 0.35001 0.02311  0.01553  -0.01571 406 GLU   A CA  
2553 C  C   . GLU   A 329 ? 0.36673 0.32895 0.36182 0.01987  0.01352  -0.01524 406 GLU   A C   
2554 O  O   . GLU   A 329 ? 0.31526 0.27367 0.30612 0.01827  0.01336  -0.01513 406 GLU   A O   
2555 C  CB  . GLU   A 329 ? 0.34123 0.30710 0.34090 0.02467  0.01569  -0.01578 406 GLU   A CB  
2556 C  CG  . GLU   A 329 ? 0.43143 0.39801 0.43202 0.02756  0.01755  -0.01570 406 GLU   A CG  
2557 C  CD  . GLU   A 329 ? 0.57711 0.54671 0.58083 0.02875  0.01733  -0.01562 406 GLU   A CD  
2558 O  OE1 . GLU   A 329 ? 0.54377 0.51653 0.55063 0.02791  0.01583  -0.01577 406 GLU   A OE1 
2559 O  OE2 . GLU   A 329 ? 0.60997 0.57859 0.61280 0.03066  0.01880  -0.01524 406 GLU   A OE2 
2560 N  N   . LEU   A 330 ? 0.29679 0.26241 0.29523 0.01877  0.01191  -0.01471 407 LEU   A N   
2561 C  CA  . LEU   A 330 ? 0.33442 0.30046 0.33258 0.01573  0.00978  -0.01360 407 LEU   A CA  
2562 C  C   . LEU   A 330 ? 0.31945 0.29167 0.32442 0.01642  0.00857  -0.01288 407 LEU   A C   
2563 O  O   . LEU   A 330 ? 0.33574 0.31040 0.34390 0.01762  0.00851  -0.01301 407 LEU   A O   
2564 C  CB  . LEU   A 330 ? 0.32777 0.29100 0.32242 0.01368  0.00915  -0.01326 407 LEU   A CB  
2565 C  CG  . LEU   A 330 ? 0.32259 0.28684 0.31726 0.01017  0.00653  -0.01158 407 LEU   A CG  
2566 C  CD1 . LEU   A 330 ? 0.35320 0.31565 0.34496 0.00764  0.00550  -0.01069 407 LEU   A CD1 
2567 C  CD2 . LEU   A 330 ? 0.29001 0.25047 0.27999 0.00807  0.00610  -0.01141 407 LEU   A CD2 
2568 N  N   . ASN   A 331 ? 0.30833 0.28275 0.31520 0.01568  0.00777  -0.01199 408 ASN   A N   
2569 C  CA  . ASN   A 331 ? 0.33514 0.31496 0.34807 0.01667  0.00713  -0.01109 408 ASN   A CA  
2570 C  C   . ASN   A 331 ? 0.32532 0.30740 0.33963 0.01405  0.00516  -0.00880 408 ASN   A C   
2571 O  O   . ASN   A 331 ? 0.28675 0.26853 0.29941 0.01182  0.00431  -0.00763 408 ASN   A O   
2572 C  CB  . ASN   A 331 ? 0.29463 0.27611 0.30946 0.01837  0.00813  -0.01153 408 ASN   A CB  
2573 C  CG  . ASN   A 331 ? 0.33646 0.32238 0.35666 0.02013  0.00824  -0.01098 408 ASN   A CG  
2574 O  OD1 . ASN   A 331 ? 0.32161 0.31020 0.34468 0.01958  0.00728  -0.00943 408 ASN   A OD1 
2575 N  ND2 . ASN   A 331 ? 0.26238 0.24872 0.28357 0.02230  0.00951  -0.01211 408 ASN   A ND2 
2576 N  N   . LEU   A 332 ? 0.35048 0.33501 0.36788 0.01418  0.00429  -0.00787 409 LEU   A N   
2577 C  CA  . LEU   A 332 ? 0.29578 0.28351 0.31558 0.01199  0.00231  -0.00514 409 LEU   A CA  
2578 C  C   . LEU   A 332 ? 0.32812 0.32110 0.35457 0.01437  0.00255  -0.00382 409 LEU   A C   
2579 O  O   . LEU   A 332 ? 0.31967 0.31594 0.34924 0.01339  0.00113  -0.00130 409 LEU   A O   
2580 C  CB  . LEU   A 332 ? 0.29511 0.28040 0.31180 0.00956  0.00089  -0.00465 409 LEU   A CB  
2581 C  CG  . LEU   A 332 ? 0.33332 0.31263 0.34233 0.00656  0.00056  -0.00532 409 LEU   A CG  
2582 C  CD1 . LEU   A 332 ? 0.31874 0.29487 0.32419 0.00502  -0.00009 -0.00551 409 LEU   A CD1 
2583 C  CD2 . LEU   A 332 ? 0.30197 0.28172 0.30941 0.00296  -0.00130 -0.00310 409 LEU   A CD2 
2584 N  N   . ALA   A 333 ? 0.32230 0.31585 0.35065 0.01749  0.00440  -0.00529 410 ALA   A N   
2585 C  CA  . ALA   A 333 ? 0.35140 0.34838 0.38477 0.02010  0.00516  -0.00434 410 ALA   A CA  
2586 C  C   . ALA   A 333 ? 0.33269 0.33464 0.37018 0.01966  0.00473  -0.00125 410 ALA   A C   
2587 O  O   . ALA   A 333 ? 0.36990 0.37274 0.40636 0.01747  0.00402  -0.00023 410 ALA   A O   
2588 C  CB  . ALA   A 333 ? 0.29876 0.29433 0.33191 0.02298  0.00721  -0.00658 410 ALA   A CB  
2589 N  N   . THR   A 334 ? 0.32753 0.33270 0.36969 0.02180  0.00523  0.00050  411 THR   A N   
2590 C  CA  . THR   A 334 ? 0.32935 0.34023 0.37673 0.02250  0.00551  0.00387  411 THR   A CA  
2591 C  C   . THR   A 334 ? 0.33274 0.34706 0.38104 0.01856  0.00289  0.00715  411 THR   A C   
2592 O  O   . THR   A 334 ? 0.32867 0.34742 0.37968 0.01766  0.00270  0.00972  411 THR   A O   
2593 C  CB  . THR   A 334 ? 0.37851 0.39018 0.42639 0.02436  0.00767  0.00314  411 THR   A CB  
2594 O  OG1 . THR   A 334 ? 0.41289 0.42050 0.45868 0.02728  0.00971  0.00001  411 THR   A OG1 
2595 C  CG2 . THR   A 334 ? 0.31832 0.33631 0.37232 0.02608  0.00870  0.00683  411 THR   A CG2 
2596 N  N   . ASN   A 335 ? 0.28940 0.30174 0.33527 0.01594  0.00077  0.00732  412 ASN   A N   
2597 C  CA  . ASN   A 335 ? 0.34638 0.36199 0.39325 0.01206  -0.00206 0.01097  412 ASN   A CA  
2598 C  C   . ASN   A 335 ? 0.35191 0.37073 0.40327 0.01304  -0.00293 0.01358  412 ASN   A C   
2599 O  O   . ASN   A 335 ? 0.40389 0.42285 0.45814 0.01710  -0.00100 0.01289  412 ASN   A O   
2600 C  CB  . ASN   A 335 ? 0.33612 0.34622 0.37555 0.00774  -0.00389 0.00941  412 ASN   A CB  
2601 C  CG  . ASN   A 335 ? 0.35348 0.36151 0.38912 0.00607  -0.00357 0.00837  412 ASN   A CG  
2602 O  OD1 . ASN   A 335 ? 0.35228 0.36364 0.38898 0.00330  -0.00506 0.01128  412 ASN   A OD1 
2603 N  ND2 . ASN   A 335 ? 0.34581 0.34848 0.37711 0.00765  -0.00172 0.00450  412 ASN   A ND2 
2604 N  N   . GLN   A 336 ? 0.35171 0.37285 0.40336 0.00918  -0.00591 0.01681  413 GLN   A N   
2605 C  CA  . GLN   A 336 ? 0.35916 0.38374 0.41515 0.00962  -0.00718 0.01990  413 GLN   A CA  
2606 C  C   . GLN   A 336 ? 0.34102 0.36080 0.39166 0.00644  -0.00934 0.01875  413 GLN   A C   
2607 O  O   . GLN   A 336 ? 0.33002 0.35245 0.38214 0.00384  -0.01194 0.02213  413 GLN   A O   
2608 C  CB  . GLN   A 336 ? 0.31519 0.34803 0.37731 0.00784  -0.00905 0.02574  413 GLN   A CB  
2609 C  CG  . GLN   A 336 ? 0.36225 0.40075 0.43026 0.01107  -0.00669 0.02756  413 GLN   A CG  
2610 C  CD  . GLN   A 336 ? 0.41153 0.44892 0.47596 0.00859  -0.00671 0.02631  413 GLN   A CD  
2611 O  OE1 . GLN   A 336 ? 0.40105 0.43735 0.46138 0.00329  -0.00958 0.02726  413 GLN   A OE1 
2612 N  NE2 . GLN   A 336 ? 0.39043 0.42735 0.45566 0.01223  -0.00353 0.02414  413 GLN   A NE2 
2613 N  N   . LEU   A 337 ? 0.32737 0.34024 0.37171 0.00652  -0.00825 0.01424  414 LEU   A N   
2614 C  CA  . LEU   A 337 ? 0.35600 0.36405 0.39476 0.00365  -0.00983 0.01306  414 LEU   A CA  
2615 C  C   . LEU   A 337 ? 0.39669 0.40561 0.43855 0.00569  -0.00994 0.01376  414 LEU   A C   
2616 O  O   . LEU   A 337 ? 0.32780 0.33658 0.37236 0.00995  -0.00771 0.01222  414 LEU   A O   
2617 C  CB  . LEU   A 337 ? 0.33985 0.34093 0.37175 0.00383  -0.00815 0.00845  414 LEU   A CB  
2618 C  CG  . LEU   A 337 ? 0.36486 0.36325 0.39228 0.00210  -0.00770 0.00713  414 LEU   A CG  
2619 C  CD1 . LEU   A 337 ? 0.34073 0.33271 0.36243 0.00330  -0.00565 0.00294  414 LEU   A CD1 
2620 C  CD2 . LEU   A 337 ? 0.37275 0.37019 0.39606 -0.00331 -0.01050 0.00950  414 LEU   A CD2 
2621 N  N   . THR   A 338 ? 0.38806 0.39729 0.42884 0.00234  -0.01265 0.01612  415 THR   A N   
2622 C  CA  . THR   A 338 ? 0.40164 0.41119 0.44454 0.00352  -0.01323 0.01704  415 THR   A CA  
2623 C  C   . THR   A 338 ? 0.41585 0.41894 0.45217 0.00212  -0.01326 0.01390  415 THR   A C   
2624 O  O   . THR   A 338 ? 0.43850 0.44075 0.47603 0.00398  -0.01291 0.01346  415 THR   A O   
2625 C  CB  . THR   A 338 ? 0.40121 0.41608 0.44791 0.00077  -0.01638 0.02234  415 THR   A CB  
2626 O  OG1 . THR   A 338 ? 0.47452 0.48965 0.51767 -0.00435 -0.01871 0.02395  415 THR   A OG1 
2627 C  CG2 . THR   A 338 ? 0.33348 0.35544 0.38918 0.00461  -0.01543 0.02583  415 THR   A CG2 
2628 N  N   . LYS   A 339 ? 0.42858 0.42689 0.45778 -0.00100 -0.01349 0.01187  416 LYS   A N   
2629 C  CA  . LYS   A 339 ? 0.43925 0.43150 0.46230 -0.00150 -0.01260 0.00867  416 LYS   A CA  
2630 C  C   . LYS   A 339 ? 0.41428 0.40151 0.43067 -0.00277 -0.01127 0.00591  416 LYS   A C   
2631 O  O   . LYS   A 339 ? 0.43592 0.42349 0.45101 -0.00475 -0.01196 0.00687  416 LYS   A O   
2632 C  CB  . LYS   A 339 ? 0.44260 0.43340 0.46273 -0.00505 -0.01506 0.01043  416 LYS   A CB  
2633 C  CG  . LYS   A 339 ? 0.49671 0.48785 0.51392 -0.01020 -0.01806 0.01343  416 LYS   A CG  
2634 C  CD  . LYS   A 339 ? 0.55446 0.54502 0.56997 -0.01329 -0.02064 0.01561  416 LYS   A CD  
2635 C  CE  . LYS   A 339 ? 0.66558 0.66097 0.68890 -0.00983 -0.02073 0.01735  416 LYS   A CE  
2636 N  NZ  . LYS   A 339 ? 0.69392 0.68871 0.71598 -0.01232 -0.02308 0.01936  416 LYS   A NZ  
2637 N  N   . ILE   A 340 ? 0.40584 0.38850 0.41814 -0.00152 -0.00927 0.00273  417 ILE   A N   
2638 C  CA  . ILE   A 340 ? 0.42107 0.39819 0.42651 -0.00228 -0.00759 0.00019  417 ILE   A CA  
2639 C  C   . ILE   A 340 ? 0.41823 0.38988 0.41609 -0.00577 -0.00832 0.00003  417 ILE   A C   
2640 O  O   . ILE   A 340 ? 0.39016 0.36144 0.38804 -0.00553 -0.00838 -0.00011 417 ILE   A O   
2641 C  CB  . ILE   A 340 ? 0.45122 0.42742 0.45748 0.00176  -0.00454 -0.00284 417 ILE   A CB  
2642 C  CG1 . ILE   A 340 ? 0.41586 0.39687 0.42899 0.00505  -0.00387 -0.00269 417 ILE   A CG1 
2643 C  CG2 . ILE   A 340 ? 0.37428 0.34516 0.37405 0.00146  -0.00259 -0.00497 417 ILE   A CG2 
2644 C  CD1 . ILE   A 340 ? 0.36544 0.34814 0.37947 0.00426  -0.00432 -0.00161 417 ILE   A CD1 
2645 N  N   . PRO   A 341 ? 0.41181 0.37858 0.40250 -0.00917 -0.00880 0.00004  418 PRO   A N   
2646 C  CA  . PRO   A 341 ? 0.38980 0.35041 0.37211 -0.01288 -0.00949 0.00002  418 PRO   A CA  
2647 C  C   . PRO   A 341 ? 0.41599 0.37223 0.39444 -0.01052 -0.00633 -0.00283 418 PRO   A C   
2648 O  O   . PRO   A 341 ? 0.43498 0.39123 0.41488 -0.00680 -0.00351 -0.00496 418 PRO   A O   
2649 C  CB  . PRO   A 341 ? 0.38720 0.34246 0.36191 -0.01656 -0.01015 0.00023  418 PRO   A CB  
2650 C  CG  . PRO   A 341 ? 0.42200 0.38242 0.40263 -0.01547 -0.01074 0.00129  418 PRO   A CG  
2651 C  CD  . PRO   A 341 ? 0.44641 0.41222 0.43545 -0.00989 -0.00860 -0.00004 418 PRO   A CD  
2652 N  N   . GLU   A 342 ? 0.43684 0.38953 0.41028 -0.01288 -0.00685 -0.00257 419 GLU   A N   
2653 C  CA  . GLU   A 342 ? 0.44011 0.38890 0.40970 -0.01084 -0.00370 -0.00484 419 GLU   A CA  
2654 C  C   . GLU   A 342 ? 0.45291 0.39532 0.41566 -0.00970 -0.00043 -0.00707 419 GLU   A C   
2655 O  O   . GLU   A 342 ? 0.43099 0.37244 0.39350 -0.00632 0.00288  -0.00882 419 GLU   A O   
2656 C  CB  . GLU   A 342 ? 0.43351 0.37890 0.39778 -0.01411 -0.00483 -0.00400 419 GLU   A CB  
2657 C  CG  . GLU   A 342 ? 0.38716 0.33875 0.35858 -0.01419 -0.00736 -0.00203 419 GLU   A CG  
2658 C  CD  . GLU   A 342 ? 0.48929 0.44442 0.46632 -0.00991 -0.00525 -0.00335 419 GLU   A CD  
2659 O  OE1 . GLU   A 342 ? 0.51112 0.46326 0.48489 -0.00788 -0.00196 -0.00541 419 GLU   A OE1 
2660 O  OE2 . GLU   A 342 ? 0.51906 0.47977 0.50351 -0.00861 -0.00681 -0.00212 419 GLU   A OE2 
2661 N  N   . ASP   A 343 ? 0.43503 0.37333 0.39254 -0.01237 -0.00130 -0.00675 420 ASP   A N   
2662 C  CA  . ASP   A 343 ? 0.42390 0.35511 0.37413 -0.01137 0.00177  -0.00872 420 ASP   A CA  
2663 C  C   . ASP   A 343 ? 0.45263 0.38745 0.40872 -0.00642 0.00426  -0.01011 420 ASP   A C   
2664 O  O   . ASP   A 343 ? 0.44554 0.37498 0.39643 -0.00496 0.00702  -0.01157 420 ASP   A O   
2665 C  CB  . ASP   A 343 ? 0.50337 0.42946 0.44677 -0.01586 -0.00030 -0.00779 420 ASP   A CB  
2666 C  CG  . ASP   A 343 ? 0.65987 0.58122 0.59582 -0.02144 -0.00291 -0.00629 420 ASP   A CG  
2667 O  OD1 . ASP   A 343 ? 0.70585 0.63358 0.64772 -0.02344 -0.00638 -0.00389 420 ASP   A OD1 
2668 O  OD2 . ASP   A 343 ? 0.58480 0.49580 0.50876 -0.02377 -0.00143 -0.00739 420 ASP   A OD2 
2669 N  N   . VAL   A 344 ? 0.43802 0.38137 0.40437 -0.00394 0.00331  -0.00954 421 VAL   A N   
2670 C  CA  . VAL   A 344 ? 0.39852 0.34523 0.37009 0.00045  0.00551  -0.01078 421 VAL   A CA  
2671 C  C   . VAL   A 344 ? 0.42224 0.36589 0.39085 0.00341  0.00926  -0.01233 421 VAL   A C   
2672 O  O   . VAL   A 344 ? 0.42239 0.36642 0.39237 0.00659  0.01157  -0.01329 421 VAL   A O   
2673 C  CB  . VAL   A 344 ? 0.44266 0.39782 0.42439 0.00242  0.00405  -0.01000 421 VAL   A CB  
2674 C  CG1 . VAL   A 344 ? 0.36199 0.31919 0.34600 0.00338  0.00436  -0.00999 421 VAL   A CG1 
2675 C  CG2 . VAL   A 344 ? 0.43525 0.39335 0.42146 0.00595  0.00565  -0.01101 421 VAL   A CG2 
2676 N  N   . SER   A 345 ? 0.38368 0.32463 0.34842 0.00244  0.00996  -0.01230 422 SER   A N   
2677 C  CA  . SER   A 345 ? 0.42087 0.35944 0.38296 0.00524  0.01374  -0.01326 422 SER   A CA  
2678 C  C   . SER   A 345 ? 0.44044 0.37135 0.39458 0.00633  0.01701  -0.01436 422 SER   A C   
2679 O  O   . SER   A 345 ? 0.46944 0.39932 0.42267 0.00972  0.02071  -0.01488 422 SER   A O   
2680 C  CB  . SER   A 345 ? 0.43788 0.37429 0.39623 0.00325  0.01364  -0.01281 422 SER   A CB  
2681 O  OG  . SER   A 345 ? 0.39891 0.32825 0.34858 -0.00093 0.01235  -0.01260 422 SER   A OG  
2682 N  N   . GLY   A 346 ? 0.45337 0.37868 0.40145 0.00349  0.01581  -0.01448 423 GLY   A N   
2683 C  CA  . GLY   A 346 ? 0.41654 0.33347 0.35626 0.00449  0.01891  -0.01556 423 GLY   A CA  
2684 C  C   . GLY   A 346 ? 0.42908 0.34895 0.37357 0.00857  0.02077  -0.01606 423 GLY   A C   
2685 O  O   . GLY   A 346 ? 0.49793 0.41165 0.43669 0.01088  0.02431  -0.01683 423 GLY   A O   
2686 N  N   . LEU   A 347 ? 0.44026 0.36894 0.39467 0.00959  0.01859  -0.01554 424 LEU   A N   
2687 C  CA  . LEU   A 347 ? 0.41589 0.34746 0.37468 0.01273  0.01967  -0.01587 424 LEU   A CA  
2688 C  C   . LEU   A 347 ? 0.41782 0.35286 0.38071 0.01730  0.02283  -0.01590 424 LEU   A C   
2689 O  O   . LEU   A 347 ? 0.41174 0.35457 0.38309 0.01909  0.02201  -0.01546 424 LEU   A O   
2690 C  CB  . LEU   A 347 ? 0.37499 0.31403 0.34196 0.01191  0.01633  -0.01524 424 LEU   A CB  
2691 C  CG  . LEU   A 347 ? 0.42697 0.36570 0.39279 0.00749  0.01273  -0.01433 424 LEU   A CG  
2692 C  CD1 . LEU   A 347 ? 0.47042 0.41697 0.44503 0.00802  0.01051  -0.01360 424 LEU   A CD1 
2693 C  CD2 . LEU   A 347 ? 0.46690 0.39768 0.42398 0.00500  0.01285  -0.01456 424 LEU   A CD2 
2694 N  N   . VAL   A 348 ? 0.39434 0.32323 0.35072 0.01915  0.02662  -0.01621 425 VAL   A N   
2695 C  CA  . VAL   A 348 ? 0.42271 0.35561 0.38317 0.02326  0.02967  -0.01557 425 VAL   A CA  
2696 C  C   . VAL   A 348 ? 0.40332 0.34055 0.36937 0.02670  0.03067  -0.01518 425 VAL   A C   
2697 O  O   . VAL   A 348 ? 0.44457 0.38780 0.41651 0.02965  0.03208  -0.01412 425 VAL   A O   
2698 C  CB  . VAL   A 348 ? 0.38695 0.31220 0.33897 0.02472  0.03396  -0.01567 425 VAL   A CB  
2699 C  CG1 . VAL   A 348 ? 0.44088 0.36396 0.38911 0.02151  0.03290  -0.01574 425 VAL   A CG1 
2700 C  CG2 . VAL   A 348 ? 0.40754 0.32249 0.34990 0.02458  0.03585  -0.01661 425 VAL   A CG2 
2701 N  N   . SER   A 349 ? 0.37260 0.30728 0.33705 0.02612  0.02975  -0.01577 426 SER   A N   
2702 C  CA  . SER   A 349 ? 0.42173 0.36052 0.39137 0.02908  0.03039  -0.01534 426 SER   A CA  
2703 C  C   . SER   A 349 ? 0.36811 0.31527 0.34642 0.02818  0.02693  -0.01513 426 SER   A C   
2704 O  O   . SER   A 349 ? 0.40221 0.35335 0.38511 0.03034  0.02716  -0.01468 426 SER   A O   
2705 C  CB  . SER   A 349 ? 0.35907 0.29046 0.32224 0.02914  0.03145  -0.01601 426 SER   A CB  
2706 O  OG  . SER   A 349 ? 0.41321 0.33622 0.36806 0.03085  0.03538  -0.01614 426 SER   A OG  
2707 N  N   . LEU   A 350 ? 0.37295 0.32257 0.35330 0.02518  0.02388  -0.01531 427 LEU   A N   
2708 C  CA  . LEU   A 350 ? 0.37238 0.32800 0.35929 0.02430  0.02090  -0.01526 427 LEU   A CA  
2709 C  C   . LEU   A 350 ? 0.38406 0.34658 0.37800 0.02663  0.02106  -0.01458 427 LEU   A C   
2710 O  O   . LEU   A 350 ? 0.36957 0.33463 0.36538 0.02707  0.02148  -0.01396 427 LEU   A O   
2711 C  CB  . LEU   A 350 ? 0.33873 0.29528 0.32624 0.02101  0.01798  -0.01520 427 LEU   A CB  
2712 C  CG  . LEU   A 350 ? 0.35693 0.31713 0.34873 0.01967  0.01522  -0.01506 427 LEU   A CG  
2713 C  CD1 . LEU   A 350 ? 0.36109 0.31803 0.34974 0.01896  0.01520  -0.01531 427 LEU   A CD1 
2714 C  CD2 . LEU   A 350 ? 0.33335 0.29478 0.32607 0.01690  0.01269  -0.01444 427 LEU   A CD2 
2715 N  N   . GLU   A 351 ? 0.39040 0.35577 0.38781 0.02782  0.02061  -0.01455 428 GLU   A N   
2716 C  CA  . GLU   A 351 ? 0.34365 0.31526 0.34721 0.02917  0.02004  -0.01385 428 GLU   A CA  
2717 C  C   . GLU   A 351 ? 0.34055 0.31546 0.34797 0.02769  0.01728  -0.01425 428 GLU   A C   
2718 O  O   . GLU   A 351 ? 0.36877 0.34780 0.38015 0.02787  0.01635  -0.01380 428 GLU   A O   
2719 C  CB  . GLU   A 351 ? 0.34426 0.31678 0.34879 0.03175  0.02171  -0.01321 428 GLU   A CB  
2720 C  CG  . GLU   A 351 ? 0.38928 0.35956 0.39110 0.03412  0.02498  -0.01226 428 GLU   A CG  
2721 C  CD  . GLU   A 351 ? 0.45512 0.42660 0.45827 0.03711  0.02689  -0.01105 428 GLU   A CD  
2722 O  OE1 . GLU   A 351 ? 0.53934 0.51601 0.54739 0.03750  0.02558  -0.01026 428 GLU   A OE1 
2723 O  OE2 . GLU   A 351 ? 0.56505 0.53179 0.56383 0.03913  0.02984  -0.01074 428 GLU   A OE2 
2724 N  N   . VAL   A 352 ? 0.34148 0.31450 0.34760 0.02620  0.01606  -0.01490 429 VAL   A N   
2725 C  CA  . VAL   A 352 ? 0.32641 0.30239 0.33613 0.02540  0.01405  -0.01506 429 VAL   A CA  
2726 C  C   . VAL   A 352 ? 0.33690 0.31149 0.34542 0.02315  0.01258  -0.01499 429 VAL   A C   
2727 O  O   . VAL   A 352 ? 0.32210 0.29350 0.32711 0.02195  0.01264  -0.01501 429 VAL   A O   
2728 C  CB  . VAL   A 352 ? 0.35193 0.32866 0.36269 0.02630  0.01416  -0.01532 429 VAL   A CB  
2729 C  CG1 . VAL   A 352 ? 0.28559 0.26440 0.29907 0.02550  0.01257  -0.01544 429 VAL   A CG1 
2730 C  CG2 . VAL   A 352 ? 0.37131 0.35045 0.38411 0.02817  0.01500  -0.01496 429 VAL   A CG2 
2731 N  N   . LEU   A 353 ? 0.29554 0.27243 0.30681 0.02241  0.01114  -0.01466 430 LEU   A N   
2732 C  CA  . LEU   A 353 ? 0.29156 0.26827 0.30281 0.02042  0.00953  -0.01401 430 LEU   A CA  
2733 C  C   . LEU   A 353 ? 0.29987 0.27993 0.31559 0.02104  0.00852  -0.01367 430 LEU   A C   
2734 O  O   . LEU   A 353 ? 0.36229 0.34393 0.38035 0.02201  0.00837  -0.01384 430 LEU   A O   
2735 C  CB  . LEU   A 353 ? 0.29436 0.26998 0.30411 0.01904  0.00896  -0.01357 430 LEU   A CB  
2736 C  CG  . LEU   A 353 ? 0.27163 0.24684 0.28072 0.01653  0.00710  -0.01246 430 LEU   A CG  
2737 C  CD1 . LEU   A 353 ? 0.28866 0.26174 0.29478 0.01493  0.00681  -0.01211 430 LEU   A CD1 
2738 C  CD2 . LEU   A 353 ? 0.27443 0.24755 0.28064 0.01497  0.00679  -0.01215 430 LEU   A CD2 
2739 N  N   . ILE   A 354 ? 0.29661 0.27746 0.31316 0.02050  0.00799  -0.01310 431 ILE   A N   
2740 C  CA  . ILE   A 354 ? 0.29830 0.28210 0.31886 0.02143  0.00754  -0.01253 431 ILE   A CA  
2741 C  C   . ILE   A 354 ? 0.33433 0.31961 0.35634 0.01982  0.00606  -0.01072 431 ILE   A C   
2742 O  O   . ILE   A 354 ? 0.33758 0.32257 0.35812 0.01791  0.00537  -0.00976 431 ILE   A O   
2743 C  CB  . ILE   A 354 ? 0.32303 0.30755 0.34415 0.02244  0.00839  -0.01288 431 ILE   A CB  
2744 C  CG1 . ILE   A 354 ? 0.34379 0.32670 0.36290 0.02354  0.00962  -0.01422 431 ILE   A CG1 
2745 C  CG2 . ILE   A 354 ? 0.32092 0.30777 0.34555 0.02399  0.00860  -0.01256 431 ILE   A CG2 
2746 C  CD1 . ILE   A 354 ? 0.36227 0.34576 0.38251 0.02483  0.00989  -0.01489 431 ILE   A CD1 
2747 N  N   . LEU   A 355 ? 0.33589 0.32267 0.36062 0.02042  0.00545  -0.01001 432 LEU   A N   
2748 C  CA  . LEU   A 355 ? 0.32815 0.31696 0.35500 0.01913  0.00395  -0.00781 432 LEU   A CA  
2749 C  C   . LEU   A 355 ? 0.35287 0.34435 0.38421 0.02133  0.00429  -0.00675 432 LEU   A C   
2750 O  O   . LEU   A 355 ? 0.34820 0.34146 0.38200 0.02105  0.00326  -0.00479 432 LEU   A O   
2751 C  CB  . LEU   A 355 ? 0.28988 0.27712 0.31489 0.01751  0.00284  -0.00755 432 LEU   A CB  
2752 C  CG  . LEU   A 355 ? 0.34468 0.32876 0.36458 0.01505  0.00258  -0.00800 432 LEU   A CG  
2753 C  CD1 . LEU   A 355 ? 0.29522 0.27688 0.31240 0.01427  0.00248  -0.00862 432 LEU   A CD1 
2754 C  CD2 . LEU   A 355 ? 0.35329 0.33826 0.37272 0.01227  0.00087  -0.00587 432 LEU   A CD2 
2755 N  N   . SER   A 356 ? 0.35075 0.34215 0.38283 0.02356  0.00585  -0.00788 433 SER   A N   
2756 C  CA  . SER   A 356 ? 0.35998 0.35228 0.39494 0.02603  0.00675  -0.00728 433 SER   A CA  
2757 C  C   . SER   A 356 ? 0.38530 0.38163 0.42432 0.02643  0.00666  -0.00447 433 SER   A C   
2758 O  O   . SER   A 356 ? 0.36413 0.36270 0.40368 0.02510  0.00632  -0.00344 433 SER   A O   
2759 C  CB  . SER   A 356 ? 0.37251 0.36301 0.40618 0.02795  0.00847  -0.00920 433 SER   A CB  
2760 O  OG  . SER   A 356 ? 0.40652 0.39716 0.43866 0.02722  0.00884  -0.01004 433 SER   A OG  
2761 N  N   . ASN   A 357 ? 0.35724 0.35452 0.39914 0.02821  0.00693  -0.00292 434 ASN   A N   
2762 C  CA  . ASN   A 357 ? 0.35820 0.35983 0.40484 0.02962  0.00749  0.00014  434 ASN   A CA  
2763 C  C   . ASN   A 357 ? 0.38774 0.39361 0.43661 0.02667  0.00522  0.00315  434 ASN   A C   
2764 O  O   . ASN   A 357 ? 0.39692 0.40729 0.44904 0.02642  0.00523  0.00566  434 ASN   A O   
2765 C  CB  . ASN   A 357 ? 0.36020 0.36272 0.40737 0.03143  0.00961  -0.00033 434 ASN   A CB  
2766 C  CG  . ASN   A 357 ? 0.41412 0.42081 0.46630 0.03395  0.01107  0.00278  434 ASN   A CG  
2767 O  OD1 . ASN   A 357 ? 0.35954 0.36803 0.41491 0.03500  0.01075  0.00520  434 ASN   A OD1 
2768 N  ND2 . ASN   A 357 ? 0.44246 0.45094 0.49556 0.03513  0.01282  0.00299  434 ASN   A ND2 
2769 N  N   . ASN   A 358 ? 0.35671 0.36102 0.40343 0.02410  0.00316  0.00302  435 ASN   A N   
2770 C  CA  . ASN   A 358 ? 0.33963 0.34727 0.38809 0.02119  0.00070  0.00625  435 ASN   A CA  
2771 C  C   . ASN   A 358 ? 0.36856 0.37772 0.42056 0.02267  0.00022  0.00854  435 ASN   A C   
2772 O  O   . ASN   A 358 ? 0.39071 0.39960 0.44502 0.02642  0.00222  0.00852  435 ASN   A O   
2773 C  CB  . ASN   A 358 ? 0.32724 0.33151 0.37024 0.01731  -0.00109 0.00481  435 ASN   A CB  
2774 C  CG  . ASN   A 358 ? 0.33996 0.34342 0.37990 0.01533  -0.00105 0.00390  435 ASN   A CG  
2775 O  OD1 . ASN   A 358 ? 0.33051 0.33662 0.37098 0.01258  -0.00264 0.00641  435 ASN   A OD1 
2776 N  ND2 . ASN   A 358 ? 0.30881 0.30857 0.34542 0.01654  0.00062  0.00058  435 ASN   A ND2 
2777 N  N   . LEU   A 359 ? 0.39174 0.40188 0.44362 0.01974  -0.00234 0.01055  436 LEU   A N   
2778 C  CA  . LEU   A 359 ? 0.36399 0.37604 0.41941 0.02066  -0.00325 0.01335  436 LEU   A CA  
2779 C  C   . LEU   A 359 ? 0.37606 0.38415 0.42737 0.01831  -0.00497 0.01205  436 LEU   A C   
2780 O  O   . LEU   A 359 ? 0.39036 0.40035 0.44297 0.01631  -0.00722 0.01488  436 LEU   A O   
2781 C  CB  . LEU   A 359 ? 0.38756 0.40641 0.44813 0.01906  -0.00515 0.01849  436 LEU   A CB  
2782 C  CG  . LEU   A 359 ? 0.40115 0.42634 0.46845 0.02185  -0.00370 0.02199  436 LEU   A CG  
2783 C  CD1 . LEU   A 359 ? 0.47388 0.49682 0.54084 0.02597  -0.00010 0.01916  436 LEU   A CD1 
2784 C  CD2 . LEU   A 359 ? 0.35087 0.38112 0.41946 0.01789  -0.00586 0.02498  436 LEU   A CD2 
2785 N  N   . LEU   A 360 ? 0.34385 0.34676 0.39024 0.01835  -0.00399 0.00806  437 LEU   A N   
2786 C  CA  . LEU   A 360 ? 0.39328 0.39267 0.43536 0.01584  -0.00536 0.00681  437 LEU   A CA  
2787 C  C   . LEU   A 360 ? 0.35224 0.34998 0.39532 0.01772  -0.00524 0.00689  437 LEU   A C   
2788 O  O   . LEU   A 360 ? 0.32048 0.31635 0.36405 0.02086  -0.00333 0.00534  437 LEU   A O   
2789 C  CB  . LEU   A 360 ? 0.35634 0.35161 0.39312 0.01511  -0.00423 0.00304  437 LEU   A CB  
2790 C  CG  . LEU   A 360 ? 0.40296 0.39833 0.43735 0.01308  -0.00430 0.00264  437 LEU   A CG  
2791 C  CD1 . LEU   A 360 ? 0.36641 0.35799 0.39664 0.01373  -0.00250 -0.00090 437 LEU   A CD1 
2792 C  CD2 . LEU   A 360 ? 0.40126 0.39624 0.43265 0.00875  -0.00670 0.00440  437 LEU   A CD2 
2793 N  N   . LYS   A 361 ? 0.40983 0.40771 0.45255 0.01550  -0.00737 0.00873  438 LYS   A N   
2794 C  CA  . LYS   A 361 ? 0.41256 0.40822 0.45535 0.01668  -0.00755 0.00877  438 LYS   A CA  
2795 C  C   . LYS   A 361 ? 0.38842 0.37985 0.42588 0.01463  -0.00785 0.00612  438 LYS   A C   
2796 O  O   . LYS   A 361 ? 0.39724 0.38601 0.43391 0.01584  -0.00743 0.00516  438 LYS   A O   
2797 C  CB  . LYS   A 361 ? 0.38577 0.38453 0.43204 0.01581  -0.00972 0.01295  438 LYS   A CB  
2798 C  CG  . LYS   A 361 ? 0.43598 0.43959 0.48860 0.01857  -0.00913 0.01633  438 LYS   A CG  
2799 C  CD  . LYS   A 361 ? 0.55057 0.55712 0.60720 0.01858  -0.01098 0.02069  438 LYS   A CD  
2800 C  CE  . LYS   A 361 ? 0.56981 0.58282 0.63350 0.02090  -0.01053 0.02500  438 LYS   A CE  
2801 N  NZ  . LYS   A 361 ? 0.64748 0.66445 0.71566 0.02054  -0.01269 0.03003  438 LYS   A NZ  
2802 N  N   . LYS   A 362 ? 0.37336 0.36390 0.40691 0.01159  -0.00843 0.00511  439 LYS   A N   
2803 C  CA  . LYS   A 362 ? 0.42778 0.41466 0.45626 0.00986  -0.00823 0.00286  439 LYS   A CA  
2804 C  C   . LYS   A 362 ? 0.40614 0.39162 0.43075 0.00854  -0.00723 0.00096  439 LYS   A C   
2805 O  O   . LYS   A 362 ? 0.40673 0.39373 0.43181 0.00778  -0.00754 0.00183  439 LYS   A O   
2806 C  CB  . LYS   A 362 ? 0.40333 0.38953 0.43002 0.00692  -0.01041 0.00465  439 LYS   A CB  
2807 C  CG  . LYS   A 362 ? 0.49469 0.48206 0.51993 0.00350  -0.01232 0.00674  439 LYS   A CG  
2808 C  CD  . LYS   A 362 ? 0.62730 0.61420 0.65096 0.00043  -0.01481 0.00900  439 LYS   A CD  
2809 C  CE  . LYS   A 362 ? 0.66927 0.65550 0.68878 -0.00402 -0.01670 0.01042  439 LYS   A CE  
2810 N  NZ  . LYS   A 362 ? 0.64127 0.63080 0.66344 -0.00425 -0.01718 0.01201  439 LYS   A NZ  
2811 N  N   . LEU   A 363 ? 0.39736 0.37996 0.41819 0.00839  -0.00593 -0.00141 440 LEU   A N   
2812 C  CA  . LEU   A 363 ? 0.41457 0.39500 0.43105 0.00741  -0.00465 -0.00308 440 LEU   A CA  
2813 C  C   . LEU   A 363 ? 0.41162 0.38896 0.42267 0.00438  -0.00519 -0.00297 440 LEU   A C   
2814 O  O   . LEU   A 363 ? 0.40674 0.38366 0.41742 0.00345  -0.00611 -0.00227 440 LEU   A O   
2815 C  CB  . LEU   A 363 ? 0.40817 0.38786 0.42434 0.00978  -0.00234 -0.00550 440 LEU   A CB  
2816 C  CG  . LEU   A 363 ? 0.42570 0.40750 0.44613 0.01261  -0.00167 -0.00587 440 LEU   A CG  
2817 C  CD1 . LEU   A 363 ? 0.39940 0.38059 0.41949 0.01434  -0.00003 -0.00776 440 LEU   A CD1 
2818 C  CD2 . LEU   A 363 ? 0.35992 0.34293 0.38120 0.01279  -0.00147 -0.00554 440 LEU   A CD2 
2819 N  N   . PRO   A 364 ? 0.43043 0.40488 0.43651 0.00276  -0.00449 -0.00370 441 PRO   A N   
2820 C  CA  . PRO   A 364 ? 0.42306 0.39331 0.42259 -0.00012 -0.00458 -0.00376 441 PRO   A CA  
2821 C  C   . PRO   A 364 ? 0.42829 0.39667 0.42551 0.00126  -0.00220 -0.00552 441 PRO   A C   
2822 O  O   . PRO   A 364 ? 0.45489 0.42468 0.45449 0.00410  -0.00031 -0.00686 441 PRO   A O   
2823 C  CB  . PRO   A 364 ? 0.44114 0.40804 0.43559 -0.00185 -0.00418 -0.00413 441 PRO   A CB  
2824 C  CG  . PRO   A 364 ? 0.42675 0.39568 0.42467 0.00120  -0.00260 -0.00534 441 PRO   A CG  
2825 C  CD  . PRO   A 364 ? 0.41528 0.38952 0.42084 0.00328  -0.00363 -0.00434 441 PRO   A CD  
2826 N  N   . HIS   A 365 ? 0.45059 0.41593 0.44299 -0.00100 -0.00232 -0.00523 442 HIS   A N   
2827 C  CA  . HIS   A 365 ? 0.45638 0.42008 0.44617 0.00016  0.00028  -0.00652 442 HIS   A CA  
2828 C  C   . HIS   A 365 ? 0.45857 0.41979 0.44518 0.00196  0.00339  -0.00817 442 HIS   A C   
2829 O  O   . HIS   A 365 ? 0.43772 0.40057 0.42619 0.00460  0.00564  -0.00900 442 HIS   A O   
2830 C  CB  . HIS   A 365 ? 0.48406 0.44417 0.46810 -0.00274 -0.00006 -0.00590 442 HIS   A CB  
2831 C  CG  . HIS   A 365 ? 0.50029 0.46255 0.48707 -0.00461 -0.00313 -0.00405 442 HIS   A CG  
2832 N  ND1 . HIS   A 365 ? 0.53529 0.50045 0.52615 -0.00342 -0.00341 -0.00373 442 HIS   A ND1 
2833 C  CD2 . HIS   A 365 ? 0.48170 0.44356 0.46762 -0.00768 -0.00614 -0.00213 442 HIS   A CD2 
2834 C  CE1 . HIS   A 365 ? 0.54783 0.51393 0.54019 -0.00533 -0.00627 -0.00186 442 HIS   A CE1 
2835 N  NE2 . HIS   A 365 ? 0.55883 0.52337 0.54860 -0.00786 -0.00799 -0.00072 442 HIS   A NE2 
2836 N  N   . GLY   A 366 ? 0.45636 0.41358 0.43806 0.00043  0.00343  -0.00839 443 GLY   A N   
2837 C  CA  . GLY   A 366 ? 0.41436 0.36793 0.39190 0.00196  0.00636  -0.00982 443 GLY   A CA  
2838 C  C   . GLY   A 366 ? 0.40107 0.35857 0.38424 0.00557  0.00769  -0.01061 443 GLY   A C   
2839 O  O   . GLY   A 366 ? 0.40191 0.35710 0.38251 0.00755  0.01052  -0.01162 443 GLY   A O   
2840 N  N   . LEU   A 367 ? 0.43652 0.39944 0.42687 0.00651  0.00583  -0.01007 444 LEU   A N   
2841 C  CA  . LEU   A 367 ? 0.40593 0.37218 0.40097 0.00959  0.00697  -0.01080 444 LEU   A CA  
2842 C  C   . LEU   A 367 ? 0.40113 0.36810 0.39625 0.01180  0.00961  -0.01131 444 LEU   A C   
2843 O  O   . LEU   A 367 ? 0.42823 0.39614 0.42457 0.01413  0.01139  -0.01188 444 LEU   A O   
2844 C  CB  . LEU   A 367 ? 0.41434 0.38522 0.41593 0.01013  0.00479  -0.01013 444 LEU   A CB  
2845 C  CG  . LEU   A 367 ? 0.48516 0.45906 0.49109 0.01289  0.00565  -0.01085 444 LEU   A CG  
2846 C  CD1 . LEU   A 367 ? 0.39480 0.36771 0.39983 0.01350  0.00633  -0.01141 444 LEU   A CD1 
2847 C  CD2 . LEU   A 367 ? 0.39344 0.37050 0.40444 0.01343  0.00389  -0.01027 444 LEU   A CD2 
2848 N  N   . GLY   A 368 ? 0.39715 0.36394 0.39101 0.01102  0.00993  -0.01081 445 GLY   A N   
2849 C  CA  . GLY   A 368 ? 0.38384 0.35255 0.37869 0.01299  0.01231  -0.01069 445 GLY   A CA  
2850 C  C   . GLY   A 368 ? 0.41690 0.38229 0.40717 0.01468  0.01591  -0.01111 445 GLY   A C   
2851 O  O   . GLY   A 368 ? 0.42391 0.39197 0.41611 0.01693  0.01816  -0.01058 445 GLY   A O   
2852 N  N   . ASN   A 369 ? 0.41716 0.37670 0.40127 0.01363  0.01653  -0.01180 446 ASN   A N   
2853 C  CA  . ASN   A 369 ? 0.41874 0.37365 0.39738 0.01546  0.02027  -0.01229 446 ASN   A CA  
2854 C  C   . ASN   A 369 ? 0.43257 0.38858 0.41351 0.01816  0.02149  -0.01270 446 ASN   A C   
2855 O  O   . ASN   A 369 ? 0.45270 0.40498 0.42956 0.02027  0.02484  -0.01291 446 ASN   A O   
2856 C  CB  . ASN   A 369 ? 0.42953 0.37626 0.39909 0.01279  0.02039  -0.01290 446 ASN   A CB  
2857 C  CG  . ASN   A 369 ? 0.49212 0.43242 0.45420 0.01459  0.02483  -0.01334 446 ASN   A CG  
2858 O  OD1 . ASN   A 369 ? 0.51518 0.45719 0.47807 0.01685  0.02766  -0.01271 446 ASN   A OD1 
2859 N  ND2 . ASN   A 369 ? 0.46804 0.40068 0.42255 0.01364  0.02563  -0.01425 446 ASN   A ND2 
2860 N  N   . LEU   A 370 ? 0.40152 0.36207 0.38841 0.01827  0.01908  -0.01274 447 LEU   A N   
2861 C  CA  . LEU   A 370 ? 0.39828 0.35967 0.38701 0.02044  0.01994  -0.01312 447 LEU   A CA  
2862 C  C   . LEU   A 370 ? 0.41549 0.38207 0.40913 0.02339  0.02165  -0.01221 447 LEU   A C   
2863 O  O   . LEU   A 370 ? 0.44217 0.41412 0.44176 0.02379  0.02000  -0.01184 447 LEU   A O   
2864 C  CB  . LEU   A 370 ? 0.36849 0.33223 0.36093 0.01923  0.01687  -0.01343 447 LEU   A CB  
2865 C  CG  . LEU   A 370 ? 0.40271 0.36250 0.39113 0.01611  0.01490  -0.01363 447 LEU   A CG  
2866 C  CD1 . LEU   A 370 ? 0.42232 0.38434 0.41414 0.01566  0.01283  -0.01366 447 LEU   A CD1 
2867 C  CD2 . LEU   A 370 ? 0.40647 0.35883 0.38649 0.01547  0.01698  -0.01414 447 LEU   A CD2 
2868 N  N   . ARG   A 371 ? 0.37810 0.34284 0.36883 0.02538  0.02511  -0.01163 448 ARG   A N   
2869 C  CA  . ARG   A 371 ? 0.39993 0.37033 0.39537 0.02785  0.02684  -0.01000 448 ARG   A CA  
2870 C  C   . ARG   A 371 ? 0.44443 0.41842 0.44418 0.03015  0.02712  -0.00948 448 ARG   A C   
2871 O  O   . ARG   A 371 ? 0.42951 0.40966 0.43453 0.03149  0.02740  -0.00778 448 ARG   A O   
2872 C  CB  . ARG   A 371 ? 0.40145 0.36856 0.39220 0.02963  0.03096  -0.00924 448 ARG   A CB  
2873 C  CG  . ARG   A 371 ? 0.49784 0.47120 0.49324 0.03210  0.03322  -0.00688 448 ARG   A CG  
2874 C  CD  . ARG   A 371 ? 0.53599 0.51720 0.53858 0.03049  0.03006  -0.00575 448 ARG   A CD  
2875 N  NE  . ARG   A 371 ? 0.56494 0.55225 0.57365 0.03215  0.02960  -0.00435 448 ARG   A NE  
2876 C  CZ  . ARG   A 371 ? 0.52751 0.52092 0.54060 0.03416  0.03135  -0.00163 448 ARG   A CZ  
2877 N  NH1 . ARG   A 371 ? 0.46789 0.46284 0.48058 0.03506  0.03394  0.00010  448 ARG   A NH1 
2878 N  NH2 . ARG   A 371 ? 0.54937 0.54773 0.56739 0.03520  0.03047  -0.00036 448 ARG   A NH2 
2879 N  N   . LYS   A 372 ? 0.39578 0.36621 0.39331 0.03033  0.02685  -0.01066 449 LYS   A N   
2880 C  CA  . LYS   A 372 ? 0.38952 0.36277 0.39055 0.03226  0.02695  -0.01024 449 LYS   A CA  
2881 C  C   . LYS   A 372 ? 0.38730 0.36347 0.39220 0.03049  0.02340  -0.01101 449 LYS   A C   
2882 O  O   . LYS   A 372 ? 0.36238 0.34084 0.37001 0.03165  0.02310  -0.01076 449 LYS   A O   
2883 C  CB  . LYS   A 372 ? 0.39828 0.36528 0.39394 0.03383  0.02928  -0.01093 449 LYS   A CB  
2884 C  CG  . LYS   A 372 ? 0.47794 0.44075 0.46887 0.03642  0.03359  -0.01017 449 LYS   A CG  
2885 C  CD  . LYS   A 372 ? 0.54678 0.51398 0.54186 0.04034  0.03614  -0.00805 449 LYS   A CD  
2886 C  CE  . LYS   A 372 ? 0.53430 0.50073 0.52997 0.04147  0.03575  -0.00834 449 LYS   A CE  
2887 N  NZ  . LYS   A 372 ? 0.58527 0.54214 0.57265 0.04221  0.03804  -0.00961 449 LYS   A NZ  
2888 N  N   . LEU   A 373 ? 0.35739 0.33317 0.36226 0.02784  0.02089  -0.01182 450 LEU   A N   
2889 C  CA  . LEU   A 373 ? 0.35055 0.32834 0.35853 0.02654  0.01804  -0.01247 450 LEU   A CA  
2890 C  C   . LEU   A 373 ? 0.34653 0.32978 0.35971 0.02726  0.01713  -0.01161 450 LEU   A C   
2891 O  O   . LEU   A 373 ? 0.30234 0.28860 0.31762 0.02682  0.01673  -0.01062 450 LEU   A O   
2892 C  CB  . LEU   A 373 ? 0.34063 0.31745 0.34804 0.02401  0.01587  -0.01291 450 LEU   A CB  
2893 C  CG  . LEU   A 373 ? 0.30700 0.28451 0.31645 0.02285  0.01347  -0.01347 450 LEU   A CG  
2894 C  CD1 . LEU   A 373 ? 0.32481 0.29972 0.33211 0.02295  0.01379  -0.01409 450 LEU   A CD1 
2895 C  CD2 . LEU   A 373 ? 0.32353 0.30020 0.33240 0.02070  0.01173  -0.01331 450 LEU   A CD2 
2896 N  N   . ARG   A 374 ? 0.31450 0.29874 0.32926 0.02801  0.01668  -0.01189 451 ARG   A N   
2897 C  CA  . ARG   A 374 ? 0.31811 0.30662 0.33674 0.02820  0.01554  -0.01113 451 ARG   A CA  
2898 C  C   . ARG   A 374 ? 0.32204 0.31053 0.34181 0.02675  0.01317  -0.01212 451 ARG   A C   
2899 O  O   . ARG   A 374 ? 0.34399 0.33475 0.36573 0.02596  0.01179  -0.01164 451 ARG   A O   
2900 C  CB  . ARG   A 374 ? 0.33919 0.32876 0.35853 0.03009  0.01675  -0.01050 451 ARG   A CB  
2901 C  CG  . ARG   A 374 ? 0.39147 0.38156 0.41030 0.03233  0.01954  -0.00899 451 ARG   A CG  
2902 C  CD  . ARG   A 374 ? 0.42624 0.41666 0.44549 0.03438  0.02071  -0.00833 451 ARG   A CD  
2903 N  NE  . ARG   A 374 ? 0.44661 0.44209 0.46991 0.03416  0.01919  -0.00697 451 ARG   A NE  
2904 C  CZ  . ARG   A 374 ? 0.47499 0.47215 0.49962 0.03563  0.01971  -0.00580 451 ARG   A CZ  
2905 N  NH1 . ARG   A 374 ? 0.47525 0.46924 0.49756 0.03778  0.02189  -0.00591 451 ARG   A NH1 
2906 N  NH2 . ARG   A 374 ? 0.45793 0.45965 0.48581 0.03473  0.01788  -0.00438 451 ARG   A NH2 
2907 N  N   . GLU   A 375 ? 0.32126 0.30704 0.33958 0.02636  0.01277  -0.01329 452 GLU   A N   
2908 C  CA  . GLU   A 375 ? 0.33963 0.32535 0.35911 0.02563  0.01116  -0.01401 452 GLU   A CA  
2909 C  C   . GLU   A 375 ? 0.29178 0.27568 0.31040 0.02449  0.01039  -0.01432 452 GLU   A C   
2910 O  O   . GLU   A 375 ? 0.33296 0.31488 0.34949 0.02416  0.01091  -0.01446 452 GLU   A O   
2911 C  CB  . GLU   A 375 ? 0.32285 0.30831 0.34235 0.02649  0.01149  -0.01451 452 GLU   A CB  
2912 C  CG  . GLU   A 375 ? 0.42763 0.41295 0.44811 0.02622  0.01044  -0.01513 452 GLU   A CG  
2913 C  CD  . GLU   A 375 ? 0.50755 0.49264 0.52778 0.02699  0.01097  -0.01555 452 GLU   A CD  
2914 O  OE1 . GLU   A 375 ? 0.50548 0.49118 0.52538 0.02773  0.01169  -0.01525 452 GLU   A OE1 
2915 O  OE2 . GLU   A 375 ? 0.55917 0.54373 0.57972 0.02694  0.01074  -0.01593 452 GLU   A OE2 
2916 N  N   . LEU   A 376 ? 0.30970 0.29399 0.32961 0.02375  0.00906  -0.01423 453 LEU   A N   
2917 C  CA  . LEU   A 376 ? 0.32748 0.31075 0.34730 0.02275  0.00813  -0.01401 453 LEU   A CA  
2918 C  C   . LEU   A 376 ? 0.31924 0.30283 0.34102 0.02320  0.00731  -0.01406 453 LEU   A C   
2919 O  O   . LEU   A 376 ? 0.33951 0.32298 0.36193 0.02329  0.00674  -0.01408 453 LEU   A O   
2920 C  CB  . LEU   A 376 ? 0.30044 0.28342 0.31960 0.02160  0.00759  -0.01346 453 LEU   A CB  
2921 C  CG  . LEU   A 376 ? 0.28767 0.26986 0.30678 0.02028  0.00632  -0.01282 453 LEU   A CG  
2922 C  CD1 . LEU   A 376 ? 0.28938 0.27048 0.30699 0.01945  0.00628  -0.01256 453 LEU   A CD1 
2923 C  CD2 . LEU   A 376 ? 0.29257 0.27431 0.31039 0.01912  0.00608  -0.01235 453 LEU   A CD2 
2924 N  N   . ASP   A 377 ? 0.34828 0.33202 0.37072 0.02347  0.00737  -0.01391 454 ASP   A N   
2925 C  CA  . ASP   A 377 ? 0.32671 0.31086 0.35107 0.02449  0.00726  -0.01374 454 ASP   A CA  
2926 C  C   . ASP   A 377 ? 0.35662 0.34148 0.38259 0.02396  0.00637  -0.01238 454 ASP   A C   
2927 O  O   . ASP   A 377 ? 0.36781 0.35367 0.39409 0.02311  0.00608  -0.01151 454 ASP   A O   
2928 C  CB  . ASP   A 377 ? 0.33406 0.31871 0.35862 0.02542  0.00819  -0.01414 454 ASP   A CB  
2929 C  CG  . ASP   A 377 ? 0.50826 0.49283 0.53419 0.02692  0.00870  -0.01412 454 ASP   A CG  
2930 O  OD1 . ASP   A 377 ? 0.47427 0.45783 0.50067 0.02739  0.00842  -0.01387 454 ASP   A OD1 
2931 O  OD2 . ASP   A 377 ? 0.52607 0.51115 0.55221 0.02772  0.00959  -0.01433 454 ASP   A OD2 
2932 N  N   . LEU   A 378 ? 0.38760 0.37188 0.41448 0.02431  0.00581  -0.01194 455 LEU   A N   
2933 C  CA  . LEU   A 378 ? 0.32656 0.31175 0.35536 0.02398  0.00486  -0.01024 455 LEU   A CA  
2934 C  C   . LEU   A 378 ? 0.33622 0.32120 0.36708 0.02611  0.00547  -0.00959 455 LEU   A C   
2935 O  O   . LEU   A 378 ? 0.32613 0.31124 0.35855 0.02638  0.00482  -0.00815 455 LEU   A O   
2936 C  CB  . LEU   A 378 ? 0.35462 0.33882 0.38225 0.02248  0.00371  -0.00996 455 LEU   A CB  
2937 C  CG  . LEU   A 378 ? 0.34292 0.32699 0.36827 0.02038  0.00328  -0.01000 455 LEU   A CG  
2938 C  CD1 . LEU   A 378 ? 0.28850 0.27132 0.31208 0.01933  0.00286  -0.01027 455 LEU   A CD1 
2939 C  CD2 . LEU   A 378 ? 0.33186 0.31712 0.35788 0.01890  0.00213  -0.00825 455 LEU   A CD2 
2940 N  N   . GLU   A 379 ? 0.35959 0.34391 0.39020 0.02774  0.00687  -0.01050 456 GLU   A N   
2941 C  CA  . GLU   A 379 ? 0.37249 0.35534 0.40390 0.03008  0.00800  -0.01010 456 GLU   A CA  
2942 C  C   . GLU   A 379 ? 0.33920 0.32530 0.37459 0.03121  0.00829  -0.00765 456 GLU   A C   
2943 O  O   . GLU   A 379 ? 0.37251 0.36207 0.40971 0.03008  0.00776  -0.00656 456 GLU   A O   
2944 C  CB  . GLU   A 379 ? 0.36716 0.34801 0.39649 0.03131  0.00955  -0.01171 456 GLU   A CB  
2945 C  CG  . GLU   A 379 ? 0.39452 0.37808 0.42534 0.03185  0.01053  -0.01142 456 GLU   A CG  
2946 C  CD  . GLU   A 379 ? 0.49895 0.48060 0.52697 0.03216  0.01153  -0.01325 456 GLU   A CD  
2947 O  OE1 . GLU   A 379 ? 0.56544 0.54700 0.59175 0.03062  0.01076  -0.01432 456 GLU   A OE1 
2948 O  OE2 . GLU   A 379 ? 0.52688 0.50712 0.55432 0.03401  0.01321  -0.01343 456 GLU   A OE2 
2949 N  N   . GLU   A 380 ? 0.36088 0.34574 0.39750 0.03342  0.00914  -0.00652 457 GLU   A N   
2950 C  CA  . GLU   A 380 ? 0.34639 0.33477 0.38748 0.03531  0.00993  -0.00366 457 GLU   A CA  
2951 C  C   . GLU   A 380 ? 0.38944 0.38218 0.43376 0.03322  0.00775  -0.00109 457 GLU   A C   
2952 O  O   . GLU   A 380 ? 0.39600 0.39354 0.44418 0.03325  0.00765  0.00147  457 GLU   A O   
2953 C  CB  . GLU   A 380 ? 0.34476 0.33555 0.38725 0.03656  0.01165  -0.00344 457 GLU   A CB  
2954 C  CG  . GLU   A 380 ? 0.34810 0.33451 0.38694 0.03835  0.01381  -0.00584 457 GLU   A CG  
2955 C  CD  . GLU   A 380 ? 0.44510 0.42683 0.48234 0.04129  0.01564  -0.00583 457 GLU   A CD  
2956 O  OE1 . GLU   A 380 ? 0.43610 0.41932 0.47667 0.04312  0.01607  -0.00329 457 GLU   A OE1 
2957 O  OE2 . GLU   A 380 ? 0.46032 0.43652 0.49259 0.04167  0.01662  -0.00824 457 GLU   A OE2 
2958 N  N   . ASN   A 381 ? 0.35024 0.34145 0.39280 0.03111  0.00590  -0.00152 458 ASN   A N   
2959 C  CA  . ASN   A 381 ? 0.34258 0.33691 0.38746 0.02913  0.00378  0.00106  458 ASN   A CA  
2960 C  C   . ASN   A 381 ? 0.38529 0.37842 0.43170 0.03079  0.00364  0.00271  458 ASN   A C   
2961 O  O   . ASN   A 381 ? 0.41336 0.40411 0.46000 0.03404  0.00563  0.00258  458 ASN   A O   
2962 C  CB  . ASN   A 381 ? 0.33942 0.33268 0.38082 0.02556  0.00202  -0.00037 458 ASN   A CB  
2963 C  CG  . ASN   A 381 ? 0.36018 0.35513 0.40066 0.02380  0.00190  -0.00080 458 ASN   A CG  
2964 O  OD1 . ASN   A 381 ? 0.32506 0.32311 0.36705 0.02187  0.00055  0.00145  458 ASN   A OD1 
2965 N  ND2 . ASN   A 381 ? 0.32981 0.32258 0.36757 0.02426  0.00317  -0.00346 458 ASN   A ND2 
2966 N  N   . LYS   A 382 ? 0.33377 0.32802 0.38073 0.02857  0.00140  0.00436  459 LYS   A N   
2967 C  CA  . LYS   A 382 ? 0.35920 0.35221 0.40739 0.02974  0.00090  0.00609  459 LYS   A CA  
2968 C  C   . LYS   A 382 ? 0.35697 0.34672 0.40131 0.02708  -0.00082 0.00459  459 LYS   A C   
2969 O  O   . LYS   A 382 ? 0.36459 0.35437 0.40982 0.02644  -0.00228 0.00651  459 LYS   A O   
2970 C  CB  . LYS   A 382 ? 0.40662 0.40515 0.46018 0.02969  -0.00034 0.01059  459 LYS   A CB  
2971 C  CG  . LYS   A 382 ? 0.42653 0.43002 0.48452 0.03145  0.00098  0.01272  459 LYS   A CG  
2972 C  CD  . LYS   A 382 ? 0.47465 0.48468 0.53664 0.02865  -0.00155 0.01681  459 LYS   A CD  
2973 C  CE  . LYS   A 382 ? 0.54345 0.55824 0.61200 0.03131  -0.00132 0.02173  459 LYS   A CE  
2974 N  NZ  . LYS   A 382 ? 0.59443 0.61201 0.66694 0.03546  0.00180  0.02298  459 LYS   A NZ  
2975 N  N   . LEU   A 383 ? 0.33842 0.32575 0.37870 0.02550  -0.00064 0.00149  460 LEU   A N   
2976 C  CA  . LEU   A 383 ? 0.35024 0.33526 0.38713 0.02295  -0.00201 0.00033  460 LEU   A CA  
2977 C  C   . LEU   A 383 ? 0.36360 0.34546 0.39995 0.02392  -0.00233 0.00084  460 LEU   A C   
2978 O  O   . LEU   A 383 ? 0.36986 0.34854 0.40546 0.02637  -0.00087 -0.00001 460 LEU   A O   
2979 C  CB  . LEU   A 383 ? 0.34610 0.32912 0.37936 0.02215  -0.00114 -0.00277 460 LEU   A CB  
2980 C  CG  . LEU   A 383 ? 0.37397 0.35924 0.40680 0.02077  -0.00101 -0.00326 460 LEU   A CG  
2981 C  CD1 . LEU   A 383 ? 0.32141 0.30506 0.35134 0.02068  0.00016  -0.00591 460 LEU   A CD1 
2982 C  CD2 . LEU   A 383 ? 0.32572 0.31206 0.35759 0.01774  -0.00281 -0.00189 460 LEU   A CD2 
2983 N  N   . GLU   A 384 ? 0.36989 0.35201 0.40594 0.02179  -0.00424 0.00223  461 GLU   A N   
2984 C  CA  . GLU   A 384 ? 0.39858 0.37749 0.43362 0.02210  -0.00490 0.00281  461 GLU   A CA  
2985 C  C   . GLU   A 384 ? 0.40940 0.38584 0.44031 0.01945  -0.00571 0.00098  461 GLU   A C   
2986 O  O   . GLU   A 384 ? 0.39954 0.37256 0.42871 0.01950  -0.00611 0.00092  461 GLU   A O   
2987 C  CB  . GLU   A 384 ? 0.36065 0.34197 0.39893 0.02183  -0.00656 0.00640  461 GLU   A CB  
2988 C  CG  . GLU   A 384 ? 0.43947 0.42365 0.48266 0.02511  -0.00545 0.00893  461 GLU   A CG  
2989 C  CD  . GLU   A 384 ? 0.61429 0.60302 0.66180 0.02437  -0.00738 0.01322  461 GLU   A CD  
2990 O  OE1 . GLU   A 384 ? 0.59160 0.58183 0.63791 0.02059  -0.00974 0.01396  461 GLU   A OE1 
2991 O  OE2 . GLU   A 384 ? 0.62593 0.61671 0.67791 0.02760  -0.00645 0.01607  461 GLU   A OE2 
2992 N  N   . SER   A 385 ? 0.37054 0.34843 0.39969 0.01731  -0.00574 -0.00040 462 SER   A N   
2993 C  CA  . SER   A 385 ? 0.40846 0.38475 0.43413 0.01524  -0.00594 -0.00194 462 SER   A CA  
2994 C  C   . SER   A 385 ? 0.41418 0.39205 0.43845 0.01427  -0.00498 -0.00347 462 SER   A C   
2995 O  O   . SER   A 385 ? 0.42340 0.40319 0.44869 0.01430  -0.00477 -0.00310 462 SER   A O   
2996 C  CB  . SER   A 385 ? 0.37515 0.35110 0.39971 0.01286  -0.00771 -0.00048 462 SER   A CB  
2997 O  OG  . SER   A 385 ? 0.41970 0.39785 0.44417 0.01102  -0.00843 0.00047  462 SER   A OG  
2998 N  N   . LEU   A 386 ? 0.40578 0.38284 0.42767 0.01340  -0.00438 -0.00491 463 LEU   A N   
2999 C  CA  . LEU   A 386 ? 0.40752 0.38572 0.42781 0.01276  -0.00317 -0.00610 463 LEU   A CA  
3000 C  C   . LEU   A 386 ? 0.41216 0.39009 0.42978 0.01041  -0.00349 -0.00569 463 LEU   A C   
3001 O  O   . LEU   A 386 ? 0.42897 0.40615 0.44575 0.00937  -0.00417 -0.00525 463 LEU   A O   
3002 C  CB  . LEU   A 386 ? 0.36519 0.34339 0.38510 0.01370  -0.00198 -0.00753 463 LEU   A CB  
3003 C  CG  . LEU   A 386 ? 0.42255 0.40034 0.44405 0.01587  -0.00140 -0.00819 463 LEU   A CG  
3004 C  CD1 . LEU   A 386 ? 0.31911 0.29702 0.33976 0.01625  -0.00048 -0.00942 463 LEU   A CD1 
3005 C  CD2 . LEU   A 386 ? 0.33130 0.31052 0.35429 0.01677  -0.00090 -0.00800 463 LEU   A CD2 
3006 N  N   . PRO   A 387 ? 0.43636 0.41432 0.45196 0.00942  -0.00291 -0.00582 464 PRO   A N   
3007 C  CA  . PRO   A 387 ? 0.43190 0.40868 0.44395 0.00724  -0.00285 -0.00550 464 PRO   A CA  
3008 C  C   . PRO   A 387 ? 0.41005 0.38729 0.42123 0.00745  -0.00149 -0.00616 464 PRO   A C   
3009 O  O   . PRO   A 387 ? 0.44491 0.42347 0.45762 0.00906  -0.00039 -0.00698 464 PRO   A O   
3010 C  CB  . PRO   A 387 ? 0.41431 0.38993 0.42339 0.00658  -0.00187 -0.00595 464 PRO   A CB  
3011 C  CG  . PRO   A 387 ? 0.39887 0.37569 0.41011 0.00880  -0.00076 -0.00698 464 PRO   A CG  
3012 C  CD  . PRO   A 387 ? 0.39408 0.37249 0.40964 0.01025  -0.00189 -0.00652 464 PRO   A CD  
3013 N  N   . ASN   A 388 ? 0.38400 0.36048 0.39278 0.00565  -0.00163 -0.00550 465 ASN   A N   
3014 C  CA  . ASN   A 388 ? 0.40374 0.38154 0.41205 0.00579  -0.00015 -0.00565 465 ASN   A CA  
3015 C  C   . ASN   A 388 ? 0.41710 0.39529 0.42376 0.00701  0.00265  -0.00644 465 ASN   A C   
3016 O  O   . ASN   A 388 ? 0.41298 0.39341 0.42048 0.00783  0.00419  -0.00627 465 ASN   A O   
3017 C  CB  . ASN   A 388 ? 0.41282 0.38988 0.41889 0.00360  -0.00073 -0.00459 465 ASN   A CB  
3018 C  CG  . ASN   A 388 ? 0.48248 0.45924 0.49032 0.00265  -0.00325 -0.00364 465 ASN   A CG  
3019 O  OD1 . ASN   A 388 ? 0.51967 0.49721 0.52985 0.00350  -0.00382 -0.00375 465 ASN   A OD1 
3020 N  ND2 . ASN   A 388 ? 0.43242 0.40748 0.43859 0.00077  -0.00480 -0.00260 465 ASN   A ND2 
3021 N  N   . GLU   A 389 ? 0.42469 0.40071 0.42893 0.00710  0.00334  -0.00705 466 GLU   A N   
3022 C  CA  . GLU   A 389 ? 0.37301 0.34829 0.37481 0.00841  0.00625  -0.00775 466 GLU   A CA  
3023 C  C   . GLU   A 389 ? 0.39051 0.36829 0.39564 0.01086  0.00723  -0.00835 466 GLU   A C   
3024 O  O   . GLU   A 389 ? 0.40417 0.38184 0.40798 0.01241  0.00977  -0.00867 466 GLU   A O   
3025 C  CB  . GLU   A 389 ? 0.37525 0.34626 0.37217 0.00728  0.00654  -0.00820 466 GLU   A CB  
3026 C  CG  . GLU   A 389 ? 0.38774 0.35547 0.37960 0.00461  0.00621  -0.00756 466 GLU   A CG  
3027 C  CD  . GLU   A 389 ? 0.48437 0.45239 0.47763 0.00225  0.00271  -0.00643 466 GLU   A CD  
3028 O  OE1 . GLU   A 389 ? 0.46340 0.43410 0.46168 0.00301  0.00079  -0.00609 466 GLU   A OE1 
3029 O  OE2 . GLU   A 389 ? 0.47473 0.44004 0.46377 -0.00030 0.00200  -0.00574 466 GLU   A OE2 
3030 N  N   . ILE   A 390 ? 0.38694 0.36660 0.39599 0.01134  0.00544  -0.00843 467 ILE   A N   
3031 C  CA  . ILE   A 390 ? 0.40534 0.38705 0.41691 0.01332  0.00629  -0.00896 467 ILE   A CA  
3032 C  C   . ILE   A 390 ? 0.38142 0.36613 0.39413 0.01401  0.00775  -0.00819 467 ILE   A C   
3033 O  O   . ILE   A 390 ? 0.40292 0.38956 0.41722 0.01563  0.00889  -0.00825 467 ILE   A O   
3034 C  CB  . ILE   A 390 ? 0.42632 0.40867 0.44093 0.01366  0.00435  -0.00921 467 ILE   A CB  
3035 C  CG1 . ILE   A 390 ? 0.39690 0.38026 0.41277 0.01266  0.00300  -0.00846 467 ILE   A CG1 
3036 C  CG2 . ILE   A 390 ? 0.44833 0.42883 0.46281 0.01314  0.00295  -0.00927 467 ILE   A CG2 
3037 C  CD1 . ILE   A 390 ? 0.43652 0.42013 0.45431 0.01338  0.00207  -0.00883 467 ILE   A CD1 
3038 N  N   . ALA   A 391 ? 0.35581 0.34139 0.36797 0.01271  0.00768  -0.00713 468 ALA   A N   
3039 C  CA  . ALA   A 391 ? 0.41339 0.40277 0.42707 0.01324  0.00918  -0.00580 468 ALA   A CA  
3040 C  C   . ALA   A 391 ? 0.38573 0.37558 0.39837 0.01549  0.01250  -0.00566 468 ALA   A C   
3041 O  O   . ALA   A 391 ? 0.37814 0.37211 0.39325 0.01664  0.01386  -0.00425 468 ALA   A O   
3042 C  CB  . ALA   A 391 ? 0.38191 0.37200 0.39465 0.01141  0.00894  -0.00454 468 ALA   A CB  
3043 N  N   . TYR   A 392 ? 0.38789 0.37352 0.39676 0.01606  0.01379  -0.00684 469 TYR   A N   
3044 C  CA  . TYR   A 392 ? 0.40054 0.38503 0.40711 0.01832  0.01727  -0.00678 469 TYR   A CA  
3045 C  C   . TYR   A 392 ? 0.38166 0.36596 0.38935 0.02018  0.01767  -0.00759 469 TYR   A C   
3046 O  O   . TYR   A 392 ? 0.32657 0.30923 0.33210 0.02225  0.02052  -0.00761 469 TYR   A O   
3047 C  CB  . TYR   A 392 ? 0.39683 0.37556 0.39701 0.01749  0.01870  -0.00750 469 TYR   A CB  
3048 C  CG  . TYR   A 392 ? 0.41344 0.39289 0.41216 0.01668  0.01993  -0.00626 469 TYR   A CG  
3049 C  CD1 . TYR   A 392 ? 0.36948 0.35009 0.36931 0.01409  0.01725  -0.00579 469 TYR   A CD1 
3050 C  CD2 . TYR   A 392 ? 0.39392 0.37305 0.39031 0.01875  0.02401  -0.00534 469 TYR   A CD2 
3051 C  CE1 . TYR   A 392 ? 0.35330 0.33486 0.35189 0.01320  0.01835  -0.00453 469 TYR   A CE1 
3052 C  CE2 . TYR   A 392 ? 0.35190 0.33213 0.34714 0.01814  0.02543  -0.00400 469 TYR   A CE2 
3053 C  CZ  . TYR   A 392 ? 0.43105 0.41261 0.42742 0.01517  0.02244  -0.00363 469 TYR   A CZ  
3054 O  OH  . TYR   A 392 ? 0.45921 0.44200 0.45440 0.01435  0.02377  -0.00221 469 TYR   A OH  
3055 N  N   . LEU   A 393 ? 0.40459 0.39029 0.41538 0.01963  0.01508  -0.00818 470 LEU   A N   
3056 C  CA  . LEU   A 393 ? 0.36059 0.34675 0.37284 0.02128  0.01535  -0.00877 470 LEU   A CA  
3057 C  C   . LEU   A 393 ? 0.36843 0.35970 0.38455 0.02273  0.01615  -0.00723 470 LEU   A C   
3058 O  O   . LEU   A 393 ? 0.38392 0.37773 0.40309 0.02242  0.01437  -0.00708 470 LEU   A O   
3059 C  CB  . LEU   A 393 ? 0.32164 0.30697 0.33516 0.02021  0.01263  -0.00988 470 LEU   A CB  
3060 C  CG  . LEU   A 393 ? 0.35840 0.33979 0.36893 0.01865  0.01157  -0.01070 470 LEU   A CG  
3061 C  CD1 . LEU   A 393 ? 0.33850 0.32020 0.35135 0.01803  0.00916  -0.01117 470 LEU   A CD1 
3062 C  CD2 . LEU   A 393 ? 0.39017 0.36765 0.39649 0.01914  0.01329  -0.01140 470 LEU   A CD2 
3063 N  N   . LYS   A 394 ? 0.37606 0.36875 0.39177 0.02434  0.01901  -0.00583 471 LYS   A N   
3064 C  CA  . LYS   A 394 ? 0.38645 0.38526 0.40650 0.02535  0.01962  -0.00349 471 LYS   A CA  
3065 C  C   . LYS   A 394 ? 0.42715 0.42786 0.44964 0.02681  0.01943  -0.00331 471 LYS   A C   
3066 O  O   . LYS   A 394 ? 0.44224 0.44826 0.46873 0.02658  0.01847  -0.00141 471 LYS   A O   
3067 C  CB  . LYS   A 394 ? 0.45800 0.45813 0.47728 0.02733  0.02332  -0.00166 471 LYS   A CB  
3068 C  CG  . LYS   A 394 ? 0.58675 0.59272 0.60935 0.02625  0.02309  0.00094  471 LYS   A CG  
3069 C  CD  . LYS   A 394 ? 0.53583 0.54028 0.55722 0.02287  0.02027  0.00006  471 LYS   A CD  
3070 C  CE  . LYS   A 394 ? 0.48687 0.49722 0.51153 0.02141  0.01970  0.00281  471 LYS   A CE  
3071 N  NZ  . LYS   A 394 ? 0.38175 0.39787 0.41123 0.02058  0.01760  0.00469  471 LYS   A NZ  
3072 N  N   . ASP   A 395 ? 0.39105 0.38760 0.41104 0.02797  0.02013  -0.00502 472 ASP   A N   
3073 C  CA  . ASP   A 395 ? 0.40481 0.40282 0.42679 0.02923  0.01990  -0.00490 472 ASP   A CA  
3074 C  C   . ASP   A 395 ? 0.40040 0.39773 0.42318 0.02739  0.01675  -0.00639 472 ASP   A C   
3075 O  O   . ASP   A 395 ? 0.42304 0.42075 0.44672 0.02817  0.01643  -0.00664 472 ASP   A O   
3076 C  CB  . ASP   A 395 ? 0.42098 0.41467 0.43958 0.03155  0.02250  -0.00576 472 ASP   A CB  
3077 C  CG  . ASP   A 395 ? 0.47914 0.47451 0.49808 0.03460  0.02614  -0.00361 472 ASP   A CG  
3078 O  OD1 . ASP   A 395 ? 0.48512 0.48611 0.50772 0.03483  0.02653  -0.00118 472 ASP   A OD1 
3079 O  OD2 . ASP   A 395 ? 0.48851 0.47957 0.50400 0.03678  0.02869  -0.00414 472 ASP   A OD2 
3080 N  N   . LEU   A 396 ? 0.31994 0.31602 0.34220 0.02518  0.01464  -0.00728 473 LEU   A N   
3081 C  CA  . LEU   A 396 ? 0.33592 0.33020 0.35819 0.02407  0.01239  -0.00879 473 LEU   A CA  
3082 C  C   . LEU   A 396 ? 0.35620 0.35354 0.38093 0.02348  0.01084  -0.00797 473 LEU   A C   
3083 O  O   . LEU   A 396 ? 0.31495 0.31527 0.34120 0.02221  0.00989  -0.00644 473 LEU   A O   
3084 C  CB  . LEU   A 396 ? 0.32301 0.31501 0.34413 0.02224  0.01078  -0.00961 473 LEU   A CB  
3085 C  CG  . LEU   A 396 ? 0.36029 0.34979 0.38109 0.02188  0.00930  -0.01108 473 LEU   A CG  
3086 C  CD1 . LEU   A 396 ? 0.31173 0.29886 0.33087 0.02288  0.01040  -0.01204 473 LEU   A CD1 
3087 C  CD2 . LEU   A 396 ? 0.30316 0.29104 0.32353 0.02036  0.00769  -0.01130 473 LEU   A CD2 
3088 N  N   . GLN   A 397 ? 0.34684 0.34324 0.37153 0.02409  0.01049  -0.00885 474 GLN   A N   
3089 C  CA  . GLN   A 397 ? 0.35555 0.35393 0.38152 0.02326  0.00899  -0.00817 474 GLN   A CA  
3090 C  C   . GLN   A 397 ? 0.32890 0.32401 0.35338 0.02220  0.00732  -0.00982 474 GLN   A C   
3091 O  O   . GLN   A 397 ? 0.34702 0.34234 0.37119 0.02067  0.00570  -0.00939 474 GLN   A O   
3092 C  CB  . GLN   A 397 ? 0.33140 0.33169 0.35840 0.02493  0.01016  -0.00739 474 GLN   A CB  
3093 C  CG  . GLN   A 397 ? 0.38569 0.38906 0.41418 0.02655  0.01229  -0.00544 474 GLN   A CG  
3094 C  CD  . GLN   A 397 ? 0.41648 0.42192 0.44630 0.02849  0.01354  -0.00420 474 GLN   A CD  
3095 O  OE1 . GLN   A 397 ? 0.36017 0.36290 0.38855 0.02938  0.01387  -0.00560 474 GLN   A OE1 
3096 N  NE2 . GLN   A 397 ? 0.52345 0.53407 0.55626 0.02918  0.01425  -0.00125 474 GLN   A NE2 
3097 N  N   . LYS   A 398 ? 0.34611 0.33809 0.36941 0.02292  0.00775  -0.01145 475 LYS   A N   
3098 C  CA  . LYS   A 398 ? 0.36492 0.35397 0.38713 0.02258  0.00678  -0.01274 475 LYS   A CA  
3099 C  C   . LYS   A 398 ? 0.33616 0.32319 0.35801 0.02254  0.00673  -0.01336 475 LYS   A C   
3100 O  O   . LYS   A 398 ? 0.37309 0.36002 0.39485 0.02312  0.00767  -0.01348 475 LYS   A O   
3101 C  CB  . LYS   A 398 ? 0.33431 0.32264 0.35621 0.02376  0.00746  -0.01356 475 LYS   A CB  
3102 C  CG  . LYS   A 398 ? 0.39106 0.37648 0.41177 0.02377  0.00696  -0.01469 475 LYS   A CG  
3103 C  CD  . LYS   A 398 ? 0.38818 0.37315 0.40870 0.02499  0.00791  -0.01540 475 LYS   A CD  
3104 C  CE  . LYS   A 398 ? 0.44109 0.42338 0.45994 0.02502  0.00768  -0.01621 475 LYS   A CE  
3105 N  NZ  . LYS   A 398 ? 0.52134 0.50314 0.54023 0.02628  0.00878  -0.01685 475 LYS   A NZ  
3106 N  N   . LEU   A 399 ? 0.36021 0.34531 0.38147 0.02172  0.00557  -0.01357 476 LEU   A N   
3107 C  CA  . LEU   A 399 ? 0.31943 0.30295 0.34076 0.02165  0.00526  -0.01369 476 LEU   A CA  
3108 C  C   . LEU   A 399 ? 0.33570 0.31649 0.35649 0.02224  0.00489  -0.01426 476 LEU   A C   
3109 O  O   . LEU   A 399 ? 0.36150 0.34025 0.38073 0.02157  0.00415  -0.01434 476 LEU   A O   
3110 C  CB  . LEU   A 399 ? 0.31086 0.29472 0.33198 0.02023  0.00445  -0.01286 476 LEU   A CB  
3111 C  CG  . LEU   A 399 ? 0.35541 0.33777 0.37653 0.01982  0.00379  -0.01262 476 LEU   A CG  
3112 C  CD1 . LEU   A 399 ? 0.29806 0.28079 0.31955 0.02028  0.00445  -0.01263 476 LEU   A CD1 
3113 C  CD2 . LEU   A 399 ? 0.31214 0.29488 0.33273 0.01819  0.00297  -0.01174 476 LEU   A CD2 
3114 N  N   . VAL   A 400 ? 0.34478 0.32529 0.36653 0.02344  0.00552  -0.01446 477 VAL   A N   
3115 C  CA  . VAL   A 400 ? 0.35340 0.33169 0.37494 0.02470  0.00590  -0.01477 477 VAL   A CA  
3116 C  C   . VAL   A 400 ? 0.38297 0.36097 0.40600 0.02512  0.00557  -0.01383 477 VAL   A C   
3117 O  O   . VAL   A 400 ? 0.35913 0.33929 0.38388 0.02494  0.00550  -0.01310 477 VAL   A O   
3118 C  CB  . VAL   A 400 ? 0.36988 0.34893 0.39189 0.02596  0.00708  -0.01526 477 VAL   A CB  
3119 C  CG1 . VAL   A 400 ? 0.31889 0.29547 0.34037 0.02757  0.00797  -0.01549 477 VAL   A CG1 
3120 C  CG2 . VAL   A 400 ? 0.37328 0.35302 0.39407 0.02546  0.00722  -0.01584 477 VAL   A CG2 
3121 N  N   . LEU   A 401 ? 0.37449 0.34947 0.39649 0.02555  0.00532  -0.01368 478 LEU   A N   
3122 C  CA  . LEU   A 401 ? 0.35590 0.33056 0.37946 0.02607  0.00491  -0.01241 478 LEU   A CA  
3123 C  C   . LEU   A 401 ? 0.35585 0.32756 0.37919 0.02842  0.00608  -0.01215 478 LEU   A C   
3124 O  O   . LEU   A 401 ? 0.35633 0.32698 0.38065 0.02925  0.00589  -0.01091 478 LEU   A O   
3125 C  CB  . LEU   A 401 ? 0.37212 0.34570 0.39450 0.02430  0.00348  -0.01205 478 LEU   A CB  
3126 C  CG  . LEU   A 401 ? 0.35616 0.33292 0.37920 0.02251  0.00284  -0.01182 478 LEU   A CG  
3127 C  CD1 . LEU   A 401 ? 0.33933 0.31542 0.36077 0.02064  0.00180  -0.01169 478 LEU   A CD1 
3128 C  CD2 . LEU   A 401 ? 0.34020 0.31891 0.36537 0.02241  0.00245  -0.01053 478 LEU   A CD2 
3129 N  N   . THR   A 402 ? 0.37129 0.34168 0.39335 0.02968  0.00749  -0.01312 479 THR   A N   
3130 C  CA  . THR   A 402 ? 0.37685 0.34336 0.39750 0.03214  0.00918  -0.01312 479 THR   A CA  
3131 C  C   . THR   A 402 ? 0.37403 0.34258 0.39864 0.03434  0.00997  -0.01103 479 THR   A C   
3132 O  O   . THR   A 402 ? 0.37967 0.35329 0.40822 0.03448  0.00997  -0.00983 479 THR   A O   
3133 C  CB  . THR   A 402 ? 0.35976 0.32580 0.37896 0.03297  0.01067  -0.01429 479 THR   A CB  
3134 O  OG1 . THR   A 402 ? 0.32987 0.29596 0.34675 0.03063  0.00953  -0.01557 479 THR   A OG1 
3135 C  CG2 . THR   A 402 ? 0.36315 0.32323 0.37863 0.03513  0.01264  -0.01483 479 THR   A CG2 
3136 N  N   . ASN   A 403 ? 0.38398 0.34851 0.40742 0.03597  0.01059  -0.01033 480 ASN   A N   
3137 C  CA  . ASN   A 403 ? 0.36201 0.32848 0.38949 0.03865  0.01166  -0.00784 480 ASN   A CA  
3138 C  C   . ASN   A 403 ? 0.38858 0.36087 0.42068 0.03698  0.00957  -0.00582 480 ASN   A C   
3139 O  O   . ASN   A 403 ? 0.42229 0.40000 0.45875 0.03728  0.00961  -0.00404 480 ASN   A O   
3140 C  CB  . ASN   A 403 ? 0.41449 0.38296 0.44397 0.04128  0.01412  -0.00729 480 ASN   A CB  
3141 C  CG  . ASN   A 403 ? 0.42501 0.39552 0.45884 0.04461  0.01572  -0.00426 480 ASN   A CG  
3142 O  OD1 . ASN   A 403 ? 0.44253 0.41040 0.47624 0.04580  0.01567  -0.00305 480 ASN   A OD1 
3143 N  ND2 . ASN   A 403 ? 0.38937 0.36490 0.42727 0.04615  0.01714  -0.00270 480 ASN   A ND2 
3144 N  N   . ASN   A 404 ? 0.38742 0.35834 0.41798 0.03474  0.00759  -0.00609 481 ASN   A N   
3145 C  CA  . ASN   A 404 ? 0.33398 0.30853 0.36773 0.03335  0.00570  -0.00396 481 ASN   A CA  
3146 C  C   . ASN   A 404 ? 0.37206 0.34279 0.40495 0.03441  0.00544  -0.00284 481 ASN   A C   
3147 O  O   . ASN   A 404 ? 0.38154 0.34699 0.41173 0.03672  0.00714  -0.00347 481 ASN   A O   
3148 C  CB  . ASN   A 404 ? 0.33756 0.31386 0.37003 0.02977  0.00377  -0.00506 481 ASN   A CB  
3149 C  CG  . ASN   A 404 ? 0.39884 0.37926 0.43272 0.02877  0.00385  -0.00533 481 ASN   A CG  
3150 O  OD1 . ASN   A 404 ? 0.37752 0.36187 0.41448 0.02826  0.00319  -0.00336 481 ASN   A OD1 
3151 N  ND2 . ASN   A 404 ? 0.33470 0.31407 0.36611 0.02829  0.00451  -0.00755 481 ASN   A ND2 
3152 N  N   . GLN   A 405 ? 0.35265 0.32524 0.38704 0.03261  0.00338  -0.00125 482 GLN   A N   
3153 C  CA  . GLN   A 405 ? 0.34443 0.31373 0.37825 0.03334  0.00282  0.00014  482 GLN   A CA  
3154 C  C   . GLN   A 405 ? 0.35764 0.32415 0.38769 0.03020  0.00091  -0.00119 482 GLN   A C   
3155 O  O   . GLN   A 405 ? 0.32829 0.29447 0.35882 0.02933  -0.00057 0.00041  482 GLN   A O   
3156 C  CB  . GLN   A 405 ? 0.40973 0.38381 0.44874 0.03376  0.00177  0.00377  482 GLN   A CB  
3157 C  CG  . GLN   A 405 ? 0.39751 0.37720 0.44133 0.03525  0.00269  0.00569  482 GLN   A CG  
3158 C  CD  . GLN   A 405 ? 0.51203 0.49041 0.55786 0.03980  0.00529  0.00734  482 GLN   A CD  
3159 O  OE1 . GLN   A 405 ? 0.54160 0.51374 0.58338 0.04192  0.00736  0.00531  482 GLN   A OE1 
3160 N  NE2 . GLN   A 405 ? 0.56063 0.54464 0.61247 0.04137  0.00531  0.01131  482 GLN   A NE2 
3161 N  N   . LEU   A 406 ? 0.38552 0.35069 0.41219 0.02834  0.00083  -0.00374 483 LEU   A N   
3162 C  CA  . LEU   A 406 ? 0.38936 0.35333 0.41331 0.02523  -0.00093 -0.00448 483 LEU   A CA  
3163 C  C   . LEU   A 406 ? 0.40390 0.36153 0.42426 0.02556  -0.00115 -0.00447 483 LEU   A C   
3164 O  O   . LEU   A 406 ? 0.38343 0.33610 0.40092 0.02737  0.00029  -0.00542 483 LEU   A O   
3165 C  CB  . LEU   A 406 ? 0.37972 0.34469 0.40166 0.02340  -0.00082 -0.00662 483 LEU   A CB  
3166 C  CG  . LEU   A 406 ? 0.39634 0.36632 0.42072 0.02313  -0.00038 -0.00690 483 LEU   A CG  
3167 C  CD1 . LEU   A 406 ? 0.37885 0.34901 0.40115 0.02214  0.00013  -0.00883 483 LEU   A CD1 
3168 C  CD2 . LEU   A 406 ? 0.35621 0.32953 0.38207 0.02114  -0.00172 -0.00568 483 LEU   A CD2 
3169 N  N   . THR   A 407 ? 0.38610 0.34320 0.40597 0.02370  -0.00291 -0.00338 484 THR   A N   
3170 C  CA  . THR   A 407 ? 0.44488 0.39548 0.46045 0.02327  -0.00341 -0.00354 484 THR   A CA  
3171 C  C   . THR   A 407 ? 0.46667 0.41652 0.47875 0.01964  -0.00478 -0.00486 484 THR   A C   
3172 O  O   . THR   A 407 ? 0.49004 0.43409 0.49746 0.01884  -0.00504 -0.00558 484 THR   A O   
3173 C  CB  . THR   A 407 ? 0.43082 0.38035 0.44773 0.02384  -0.00442 -0.00112 484 THR   A CB  
3174 O  OG1 . THR   A 407 ? 0.50060 0.45560 0.52031 0.02145  -0.00616 0.00005  484 THR   A OG1 
3175 C  CG2 . THR   A 407 ? 0.34076 0.29000 0.36082 0.02809  -0.00271 0.00071  484 THR   A CG2 
3176 N  N   . THR   A 408 ? 0.59245 0.54780 0.60636 0.01745  -0.00551 -0.00506 485 THR   A N   
3177 C  CA  . THR   A 408 ? 0.63331 0.58935 0.64486 0.01457  -0.00621 -0.00607 485 THR   A CA  
3178 C  C   . THR   A 408 ? 0.63390 0.59598 0.64801 0.01399  -0.00564 -0.00657 485 THR   A C   
3179 O  O   . THR   A 408 ? 0.70259 0.66753 0.71954 0.01543  -0.00490 -0.00635 485 THR   A O   
3180 C  CB  . THR   A 408 ? 0.70094 0.65581 0.71065 0.01184  -0.00798 -0.00507 485 THR   A CB  
3181 O  OG1 . THR   A 408 ? 0.68190 0.63780 0.68960 0.00916  -0.00854 -0.00563 485 THR   A OG1 
3182 C  CG2 . THR   A 408 ? 0.62542 0.58451 0.63796 0.01109  -0.00860 -0.00379 485 THR   A CG2 
3183 N  N   . LEU   A 409 ? 0.51428 0.47821 0.52722 0.01180  -0.00595 -0.00700 486 LEU   A N   
3184 C  CA  . LEU   A 409 ? 0.49606 0.46505 0.51072 0.01127  -0.00516 -0.00729 486 LEU   A CA  
3185 C  C   . LEU   A 409 ? 0.47341 0.44468 0.48791 0.00905  -0.00580 -0.00629 486 LEU   A C   
3186 O  O   . LEU   A 409 ? 0.46073 0.43022 0.47356 0.00726  -0.00706 -0.00550 486 LEU   A O   
3187 C  CB  . LEU   A 409 ? 0.43462 0.40471 0.44853 0.01087  -0.00464 -0.00808 486 LEU   A CB  
3188 C  CG  . LEU   A 409 ? 0.45593 0.42357 0.46913 0.01267  -0.00390 -0.00921 486 LEU   A CG  
3189 C  CD1 . LEU   A 409 ? 0.43667 0.40610 0.44911 0.01155  -0.00383 -0.00953 486 LEU   A CD1 
3190 C  CD2 . LEU   A 409 ? 0.43277 0.40207 0.44853 0.01510  -0.00257 -0.00966 486 LEU   A CD2 
3191 N  N   . PRO   A 410 ? 0.46977 0.44443 0.48538 0.00904  -0.00481 -0.00629 487 PRO   A N   
3192 C  CA  . PRO   A 410 ? 0.40423 0.38080 0.41901 0.00708  -0.00483 -0.00543 487 PRO   A CA  
3193 C  C   . PRO   A 410 ? 0.41401 0.39264 0.42843 0.00580  -0.00465 -0.00503 487 PRO   A C   
3194 O  O   . PRO   A 410 ? 0.41478 0.39478 0.42994 0.00656  -0.00398 -0.00553 487 PRO   A O   
3195 C  CB  . PRO   A 410 ? 0.41259 0.39114 0.42767 0.00780  -0.00330 -0.00581 487 PRO   A CB  
3196 C  CG  . PRO   A 410 ? 0.44307 0.42057 0.45941 0.00954  -0.00334 -0.00638 487 PRO   A CG  
3197 C  CD  . PRO   A 410 ? 0.42428 0.40031 0.44134 0.01075  -0.00363 -0.00693 487 PRO   A CD  
3198 N  N   . ARG   A 411 ? 0.43107 0.41027 0.44447 0.00365  -0.00537 -0.00382 488 ARG   A N   
3199 C  CA  . ARG   A 411 ? 0.41224 0.39445 0.42582 0.00211  -0.00530 -0.00280 488 ARG   A CA  
3200 C  C   . ARG   A 411 ? 0.38514 0.37185 0.40040 0.00336  -0.00300 -0.00271 488 ARG   A C   
3201 O  O   . ARG   A 411 ? 0.38731 0.37722 0.40379 0.00294  -0.00277 -0.00183 488 ARG   A O   
3202 C  CB  . ARG   A 411 ? 0.46698 0.44964 0.47937 -0.00044 -0.00622 -0.00126 488 ARG   A CB  
3203 C  CG  . ARG   A 411 ? 0.51764 0.49566 0.52798 -0.00202 -0.00863 -0.00095 488 ARG   A CG  
3204 C  CD  . ARG   A 411 ? 0.57559 0.55488 0.58482 -0.00492 -0.00950 0.00081  488 ARG   A CD  
3205 N  NE  . ARG   A 411 ? 0.59201 0.56633 0.59883 -0.00645 -0.01174 0.00122  488 ARG   A NE  
3206 C  CZ  . ARG   A 411 ? 0.65151 0.62217 0.65623 -0.00777 -0.01346 0.00139  488 ARG   A CZ  
3207 N  NH1 . ARG   A 411 ? 0.65553 0.62713 0.66021 -0.00815 -0.01351 0.00122  488 ARG   A NH1 
3208 N  NH2 . ARG   A 411 ? 0.57416 0.53957 0.57625 -0.00886 -0.01522 0.00181  488 ARG   A NH2 
3209 N  N   . GLY   A 412 ? 0.38039 0.36716 0.39544 0.00478  -0.00131 -0.00337 489 GLY   A N   
3210 C  CA  . GLY   A 412 ? 0.39401 0.38384 0.40991 0.00642  0.00126  -0.00339 489 GLY   A CA  
3211 C  C   . GLY   A 412 ? 0.40343 0.39434 0.42107 0.00809  0.00166  -0.00409 489 GLY   A C   
3212 O  O   . GLY   A 412 ? 0.40413 0.39808 0.42292 0.00944  0.00363  -0.00365 489 GLY   A O   
3213 N  N   . ILE   A 413 ? 0.38536 0.37363 0.40302 0.00817  -0.00000 -0.00504 490 ILE   A N   
3214 C  CA  . ILE   A 413 ? 0.38678 0.37554 0.40551 0.00954  0.00029  -0.00577 490 ILE   A CA  
3215 C  C   . ILE   A 413 ? 0.41489 0.40776 0.43504 0.00879  0.00041  -0.00430 490 ILE   A C   
3216 O  O   . ILE   A 413 ? 0.43649 0.43119 0.45788 0.01008  0.00125  -0.00443 490 ILE   A O   
3217 C  CB  . ILE   A 413 ? 0.40061 0.38517 0.41837 0.00958  -0.00136 -0.00683 490 ILE   A CB  
3218 C  CG1 . ILE   A 413 ? 0.42303 0.40705 0.44144 0.01162  -0.00052 -0.00809 490 ILE   A CG1 
3219 C  CG2 . ILE   A 413 ? 0.39561 0.37894 0.41207 0.00747  -0.00320 -0.00608 490 ILE   A CG2 
3220 C  CD1 . ILE   A 413 ? 0.44252 0.42882 0.46151 0.01147  -0.00038 -0.00773 490 ILE   A CD1 
3221 N  N   . GLY   A 414 ? 0.42722 0.42207 0.44741 0.00660  -0.00047 -0.00257 491 GLY   A N   
3222 C  CA  . GLY   A 414 ? 0.37382 0.37362 0.39590 0.00550  -0.00061 -0.00046 491 GLY   A CA  
3223 C  C   . GLY   A 414 ? 0.38565 0.39068 0.41022 0.00733  0.00216  0.00091  491 GLY   A C   
3224 O  O   . GLY   A 414 ? 0.42103 0.43128 0.44807 0.00682  0.00228  0.00320  491 GLY   A O   
3225 N  N   . HIS   A 415 ? 0.36630 0.36992 0.39002 0.00937  0.00442  -0.00015 492 HIS   A N   
3226 C  CA  . HIS   A 415 ? 0.41430 0.42154 0.43952 0.01168  0.00754  0.00094  492 HIS   A CA  
3227 C  C   . HIS   A 415 ? 0.39564 0.40293 0.42181 0.01398  0.00850  0.00008  492 HIS   A C   
3228 O  O   . HIS   A 415 ? 0.43462 0.44513 0.46235 0.01610  0.01102  0.00135  492 HIS   A O   
3229 C  CB  . HIS   A 415 ? 0.38724 0.39194 0.40984 0.01271  0.00983  0.00022  492 HIS   A CB  
3230 C  CG  . HIS   A 415 ? 0.44975 0.45636 0.47203 0.01108  0.01012  0.00194  492 HIS   A CG  
3231 N  ND1 . HIS   A 415 ? 0.48146 0.48444 0.50105 0.00913  0.00871  0.00115  492 HIS   A ND1 
3232 C  CD2 . HIS   A 415 ? 0.42209 0.43426 0.44664 0.01106  0.01163  0.00473  492 HIS   A CD2 
3233 C  CE1 . HIS   A 415 ? 0.44091 0.44672 0.46071 0.00785  0.00933  0.00312  492 HIS   A CE1 
3234 N  NE2 . HIS   A 415 ? 0.48654 0.49811 0.50944 0.00902  0.01119  0.00536  492 HIS   A NE2 
3235 N  N   . LEU   A 416 ? 0.35396 0.35776 0.37920 0.01376  0.00673  -0.00184 493 LEU   A N   
3236 C  CA  . LEU   A 416 ? 0.38029 0.38370 0.40607 0.01575  0.00751  -0.00279 493 LEU   A CA  
3237 C  C   . LEU   A 416 ? 0.37437 0.38225 0.40277 0.01523  0.00667  -0.00091 493 LEU   A C   
3238 O  O   . LEU   A 416 ? 0.37426 0.38076 0.40221 0.01409  0.00464  -0.00153 493 LEU   A O   
3239 C  CB  . LEU   A 416 ? 0.34274 0.34120 0.36668 0.01570  0.00613  -0.00522 493 LEU   A CB  
3240 C  CG  . LEU   A 416 ? 0.39284 0.38738 0.41457 0.01591  0.00648  -0.00665 493 LEU   A CG  
3241 C  CD1 . LEU   A 416 ? 0.37014 0.36132 0.39123 0.01644  0.00552  -0.00841 493 LEU   A CD1 
3242 C  CD2 . LEU   A 416 ? 0.34041 0.33481 0.36089 0.01741  0.00914  -0.00661 493 LEU   A CD2 
3243 N  N   . THR   A 417 ? 0.34535 0.35860 0.37635 0.01614  0.00843  0.00164  494 THR   A N   
3244 C  CA  . THR   A 417 ? 0.36652 0.38535 0.40063 0.01516  0.00736  0.00436  494 THR   A CA  
3245 C  C   . THR   A 417 ? 0.40050 0.41979 0.43554 0.01680  0.00765  0.00409  494 THR   A C   
3246 O  O   . THR   A 417 ? 0.45800 0.48096 0.49492 0.01534  0.00595  0.00608  494 THR   A O   
3247 C  CB  . THR   A 417 ? 0.36676 0.39226 0.40418 0.01588  0.00935  0.00786  494 THR   A CB  
3248 O  OG1 . THR   A 417 ? 0.36092 0.38673 0.39882 0.01975  0.01309  0.00788  494 THR   A OG1 
3249 C  CG2 . THR   A 417 ? 0.32529 0.35039 0.36159 0.01420  0.00924  0.00822  494 THR   A CG2 
3250 N  N   . ASN   A 418 ? 0.32391 0.33960 0.35745 0.01945  0.00957  0.00191  495 ASN   A N   
3251 C  CA  . ASN   A 418 ? 0.36644 0.38192 0.40042 0.02077  0.00962  0.00144  495 ASN   A CA  
3252 C  C   . ASN   A 418 ? 0.37339 0.38391 0.40475 0.01941  0.00741  -0.00119 495 ASN   A C   
3253 O  O   . ASN   A 418 ? 0.34725 0.35694 0.37842 0.02025  0.00733  -0.00189 495 ASN   A O   
3254 C  CB  . ASN   A 418 ? 0.34708 0.36103 0.38045 0.02426  0.01289  0.00071  495 ASN   A CB  
3255 C  CG  . ASN   A 418 ? 0.43760 0.45681 0.47389 0.02653  0.01565  0.00386  495 ASN   A CG  
3256 O  OD1 . ASN   A 418 ? 0.41550 0.44068 0.45550 0.02623  0.01500  0.00685  495 ASN   A OD1 
3257 N  ND2 . ASN   A 418 ? 0.35918 0.37606 0.39354 0.02875  0.01880  0.00342  495 ASN   A ND2 
3258 N  N   . LEU   A 419 ? 0.37124 0.37840 0.40053 0.01749  0.00579  -0.00249 496 LEU   A N   
3259 C  CA  . LEU   A 419 ? 0.38148 0.38349 0.40821 0.01698  0.00445  -0.00493 496 LEU   A CA  
3260 C  C   . LEU   A 419 ? 0.36877 0.37095 0.39485 0.01516  0.00240  -0.00436 496 LEU   A C   
3261 O  O   . LEU   A 419 ? 0.37520 0.37917 0.40128 0.01259  0.00061  -0.00262 496 LEU   A O   
3262 C  CB  . LEU   A 419 ? 0.34014 0.33853 0.36497 0.01578  0.00352  -0.00606 496 LEU   A CB  
3263 C  CG  . LEU   A 419 ? 0.36447 0.35765 0.38710 0.01610  0.00287  -0.00832 496 LEU   A CG  
3264 C  CD1 . LEU   A 419 ? 0.31340 0.30562 0.33629 0.01841  0.00462  -0.00962 496 LEU   A CD1 
3265 C  CD2 . LEU   A 419 ? 0.31345 0.30355 0.33456 0.01481  0.00171  -0.00873 496 LEU   A CD2 
3266 N  N   . THR   A 420 ? 0.33307 0.33333 0.35825 0.01620  0.00260  -0.00563 497 THR   A N   
3267 C  CA  . THR   A 420 ? 0.35960 0.35894 0.38307 0.01433  0.00074  -0.00532 497 THR   A CA  
3268 C  C   . THR   A 420 ? 0.37969 0.37247 0.39922 0.01390  0.00002  -0.00776 497 THR   A C   
3269 O  O   . THR   A 420 ? 0.39158 0.38172 0.40801 0.01163  -0.00175 -0.00767 497 THR   A O   
3270 C  CB  . THR   A 420 ? 0.37374 0.37586 0.39875 0.01564  0.00147  -0.00455 497 THR   A CB  
3271 O  OG1 . THR   A 420 ? 0.37864 0.37742 0.40264 0.01791  0.00295  -0.00690 497 THR   A OG1 
3272 C  CG2 . THR   A 420 ? 0.37268 0.38104 0.40181 0.01713  0.00298  -0.00201 497 THR   A CG2 
3273 N  N   . HIS   A 421 ? 0.35986 0.34982 0.37917 0.01598  0.00142  -0.00971 498 HIS   A N   
3274 C  CA  . HIS   A 421 ? 0.37291 0.35736 0.38927 0.01642  0.00140  -0.01169 498 HIS   A CA  
3275 C  C   . HIS   A 421 ? 0.37700 0.35942 0.39361 0.01721  0.00184  -0.01246 498 HIS   A C   
3276 O  O   . HIS   A 421 ? 0.35402 0.33830 0.37282 0.01866  0.00303  -0.01256 498 HIS   A O   
3277 C  CB  . HIS   A 421 ? 0.37401 0.35819 0.39062 0.01838  0.00274  -0.01274 498 HIS   A CB  
3278 C  CG  . HIS   A 421 ? 0.40910 0.38845 0.42340 0.01944  0.00334  -0.01449 498 HIS   A CG  
3279 N  ND1 . HIS   A 421 ? 0.41965 0.39703 0.43435 0.02057  0.00395  -0.01519 498 HIS   A ND1 
3280 C  CD2 . HIS   A 421 ? 0.39959 0.37601 0.41135 0.01975  0.00367  -0.01542 498 HIS   A CD2 
3281 C  CE1 . HIS   A 421 ? 0.41672 0.39056 0.42968 0.02178  0.00478  -0.01627 498 HIS   A CE1 
3282 N  NE2 . HIS   A 421 ? 0.43831 0.41123 0.44919 0.02134  0.00475  -0.01659 498 HIS   A NE2 
3283 N  N   . LEU   A 422 ? 0.35775 0.33599 0.37165 0.01606  0.00079  -0.01281 499 LEU   A N   
3284 C  CA  . LEU   A 422 ? 0.32101 0.29701 0.33499 0.01669  0.00093  -0.01321 499 LEU   A CA  
3285 C  C   . LEU   A 422 ? 0.38117 0.35173 0.39249 0.01789  0.00142  -0.01446 499 LEU   A C   
3286 O  O   . LEU   A 422 ? 0.42080 0.38684 0.42810 0.01661  0.00061  -0.01472 499 LEU   A O   
3287 C  CB  . LEU   A 422 ? 0.30764 0.28345 0.32073 0.01438  -0.00059 -0.01210 499 LEU   A CB  
3288 C  CG  . LEU   A 422 ? 0.34774 0.32203 0.36126 0.01473  -0.00067 -0.01208 499 LEU   A CG  
3289 C  CD1 . LEU   A 422 ? 0.32776 0.30454 0.34429 0.01676  0.00072  -0.01234 499 LEU   A CD1 
3290 C  CD2 . LEU   A 422 ? 0.39215 0.36830 0.40572 0.01235  -0.00195 -0.01065 499 LEU   A CD2 
3291 N  N   . GLY   A 423 ? 0.34914 0.31990 0.36233 0.02026  0.00285  -0.01504 500 GLY   A N   
3292 C  CA  . GLY   A 423 ? 0.33183 0.29819 0.34319 0.02200  0.00387  -0.01584 500 GLY   A CA  
3293 C  C   . GLY   A 423 ? 0.36604 0.33062 0.37824 0.02307  0.00400  -0.01535 500 GLY   A C   
3294 O  O   . GLY   A 423 ? 0.34843 0.31604 0.36411 0.02428  0.00451  -0.01477 500 GLY   A O   
3295 N  N   . LEU   A 424 ? 0.37671 0.33614 0.38541 0.02245  0.00341  -0.01536 501 LEU   A N   
3296 C  CA  . LEU   A 424 ? 0.35418 0.31162 0.36347 0.02336  0.00334  -0.01459 501 LEU   A CA  
3297 C  C   . LEU   A 424 ? 0.37391 0.32562 0.38077 0.02592  0.00497  -0.01485 501 LEU   A C   
3298 O  O   . LEU   A 424 ? 0.35383 0.30286 0.36056 0.02693  0.00503  -0.01402 501 LEU   A O   
3299 C  CB  . LEU   A 424 ? 0.31367 0.26951 0.32084 0.02068  0.00142  -0.01406 501 LEU   A CB  
3300 C  CG  . LEU   A 424 ? 0.34528 0.30712 0.35565 0.01887  0.00033  -0.01328 501 LEU   A CG  
3301 C  CD1 . LEU   A 424 ? 0.37027 0.33103 0.37830 0.01593  -0.00145 -0.01266 501 LEU   A CD1 
3302 C  CD2 . LEU   A 424 ? 0.38506 0.34965 0.39906 0.01997  0.00053  -0.01241 501 LEU   A CD2 
3303 N  N   . GLY   A 425 ? 0.36500 0.31465 0.36987 0.02720  0.00651  -0.01584 502 GLY   A N   
3304 C  CA  . GLY   A 425 ? 0.34906 0.29238 0.35068 0.02985  0.00858  -0.01612 502 GLY   A CA  
3305 C  C   . GLY   A 425 ? 0.33686 0.28247 0.34319 0.03311  0.01004  -0.01458 502 GLY   A C   
3306 O  O   . GLY   A 425 ? 0.36345 0.31592 0.37548 0.03337  0.00971  -0.01354 502 GLY   A O   
3307 N  N   . GLU   A 426 ? 0.37551 0.31500 0.37909 0.03554  0.01167  -0.01420 503 GLU   A N   
3308 C  CA  . GLU   A 426 ? 0.35579 0.29731 0.36392 0.03919  0.01344  -0.01221 503 GLU   A CA  
3309 C  C   . GLU   A 426 ? 0.33431 0.28120 0.34771 0.03826  0.01143  -0.01028 503 GLU   A C   
3310 O  O   . GLU   A 426 ? 0.39745 0.35048 0.41681 0.03963  0.01172  -0.00839 503 GLU   A O   
3311 C  CB  . GLU   A 426 ? 0.39742 0.34369 0.40936 0.04140  0.01546  -0.01181 503 GLU   A CB  
3312 C  CG  . GLU   A 426 ? 0.38633 0.32676 0.39275 0.04280  0.01793  -0.01351 503 GLU   A CG  
3313 C  CD  . GLU   A 426 ? 0.47988 0.42534 0.49015 0.04487  0.01996  -0.01299 503 GLU   A CD  
3314 O  OE1 . GLU   A 426 ? 0.49139 0.44342 0.50841 0.04656  0.02038  -0.01068 503 GLU   A OE1 
3315 O  OE2 . GLU   A 426 ? 0.48440 0.42736 0.49080 0.04447  0.02094  -0.01470 503 GLU   A OE2 
3316 N  N   . ASN   A 427 ? 0.34600 0.29041 0.35689 0.03570  0.00931  -0.01054 504 ASN   A N   
3317 C  CA  . ASN   A 427 ? 0.36344 0.31174 0.37825 0.03469  0.00745  -0.00873 504 ASN   A CA  
3318 C  C   . ASN   A 427 ? 0.42116 0.36327 0.43335 0.03585  0.00751  -0.00772 504 ASN   A C   
3319 O  O   . ASN   A 427 ? 0.40933 0.34431 0.41727 0.03830  0.00958  -0.00814 504 ASN   A O   
3320 C  CB  . ASN   A 427 ? 0.32830 0.28009 0.34312 0.03066  0.00496  -0.00956 504 ASN   A CB  
3321 C  CG  . ASN   A 427 ? 0.39654 0.35546 0.41554 0.03003  0.00482  -0.00957 504 ASN   A CG  
3322 O  OD1 . ASN   A 427 ? 0.38703 0.35073 0.41012 0.02974  0.00405  -0.00805 504 ASN   A OD1 
3323 N  ND2 . ASN   A 427 ? 0.36956 0.32876 0.38703 0.02961  0.00548  -0.01117 504 ASN   A ND2 
3324 N  N   . LEU   A 428 ? 0.37916 0.32338 0.39327 0.03410  0.00538  -0.00639 505 LEU   A N   
3325 C  CA  . LEU   A 428 ? 0.39746 0.33609 0.40917 0.03474  0.00501  -0.00526 505 LEU   A CA  
3326 C  C   . LEU   A 428 ? 0.39314 0.32951 0.40106 0.03061  0.00243  -0.00614 505 LEU   A C   
3327 O  O   . LEU   A 428 ? 0.39218 0.32771 0.40039 0.02982  0.00102  -0.00472 505 LEU   A O   
3328 C  CB  . LEU   A 428 ? 0.35454 0.29773 0.37226 0.03660  0.00477  -0.00215 505 LEU   A CB  
3329 C  CG  . LEU   A 428 ? 0.39986 0.34594 0.42200 0.04083  0.00736  -0.00047 505 LEU   A CG  
3330 C  CD1 . LEU   A 428 ? 0.36085 0.31322 0.38979 0.04189  0.00652  0.00318  505 LEU   A CD1 
3331 C  CD2 . LEU   A 428 ? 0.45474 0.39234 0.47237 0.04463  0.01038  -0.00083 505 LEU   A CD2 
3332 N  N   . LEU   A 429 ? 0.36213 0.29814 0.36689 0.02787  0.00173  -0.00815 506 LEU   A N   
3333 C  CA  . LEU   A 429 ? 0.41562 0.35121 0.41776 0.02376  -0.00070 -0.00854 506 LEU   A CA  
3334 C  C   . LEU   A 429 ? 0.47584 0.40264 0.47198 0.02313  -0.00127 -0.00838 506 LEU   A C   
3335 O  O   . LEU   A 429 ? 0.41949 0.33854 0.41047 0.02477  0.00026  -0.00921 506 LEU   A O   
3336 C  CB  . LEU   A 429 ? 0.37747 0.31467 0.37771 0.02131  -0.00113 -0.01020 506 LEU   A CB  
3337 C  CG  . LEU   A 429 ? 0.36475 0.30999 0.36997 0.02142  -0.00074 -0.01049 506 LEU   A CG  
3338 C  CD1 . LEU   A 429 ? 0.33605 0.28173 0.33893 0.01956  -0.00092 -0.01185 506 LEU   A CD1 
3339 C  CD2 . LEU   A 429 ? 0.40496 0.35627 0.41412 0.01976  -0.00210 -0.00939 506 LEU   A CD2 
3340 N  N   . THR   A 430 ? 0.43715 0.36453 0.43332 0.02065  -0.00339 -0.00731 507 THR   A N   
3341 C  CA  . THR   A 430 ? 0.50218 0.42119 0.49190 0.01897  -0.00445 -0.00724 507 THR   A CA  
3342 C  C   . THR   A 430 ? 0.49327 0.41192 0.47908 0.01417  -0.00655 -0.00805 507 THR   A C   
3343 O  O   . THR   A 430 ? 0.52039 0.43086 0.49915 0.01235  -0.00727 -0.00848 507 THR   A O   
3344 C  CB  . THR   A 430 ? 0.48839 0.40719 0.47985 0.01914  -0.00556 -0.00523 507 THR   A CB  
3345 O  OG1 . THR   A 430 ? 0.52356 0.45105 0.52025 0.01702  -0.00712 -0.00437 507 THR   A OG1 
3346 C  CG2 . THR   A 430 ? 0.37082 0.28823 0.36508 0.02404  -0.00349 -0.00384 507 THR   A CG2 
3347 N  N   . HIS   A 431 ? 0.48747 0.41450 0.47739 0.01210  -0.00744 -0.00806 508 HIS   A N   
3348 C  CA  . HIS   A 431 ? 0.52524 0.45360 0.51274 0.00771  -0.00936 -0.00811 508 HIS   A CA  
3349 C  C   . HIS   A 431 ? 0.47721 0.41515 0.47018 0.00721  -0.00914 -0.00815 508 HIS   A C   
3350 O  O   . HIS   A 431 ? 0.45263 0.39572 0.45071 0.00935  -0.00812 -0.00795 508 HIS   A O   
3351 C  CB  . HIS   A 431 ? 0.50409 0.43116 0.48993 0.00470  -0.01149 -0.00671 508 HIS   A CB  
3352 C  CG  . HIS   A 431 ? 0.53524 0.46884 0.52671 0.00514  -0.01171 -0.00550 508 HIS   A CG  
3353 N  ND1 . HIS   A 431 ? 0.54905 0.48264 0.54351 0.00838  -0.01073 -0.00492 508 HIS   A ND1 
3354 C  CD2 . HIS   A 431 ? 0.57267 0.51293 0.56704 0.00269  -0.01272 -0.00458 508 HIS   A CD2 
3355 C  CE1 . HIS   A 431 ? 0.56141 0.50093 0.55983 0.00748  -0.01142 -0.00383 508 HIS   A CE1 
3356 N  NE2 . HIS   A 431 ? 0.57655 0.51983 0.57472 0.00421  -0.01241 -0.00376 508 HIS   A NE2 
3357 N  N   . LEU   A 432 ? 0.45663 0.39671 0.44822 0.00420  -0.01017 -0.00816 509 LEU   A N   
3358 C  CA  . LEU   A 432 ? 0.47968 0.42867 0.47633 0.00376  -0.00988 -0.00777 509 LEU   A CA  
3359 C  C   . LEU   A 432 ? 0.47003 0.42314 0.46778 0.00063  -0.01138 -0.00611 509 LEU   A C   
3360 O  O   . LEU   A 432 ? 0.50418 0.45370 0.49811 -0.00233 -0.01317 -0.00528 509 LEU   A O   
3361 C  CB  . LEU   A 432 ? 0.43606 0.38652 0.43188 0.00303  -0.00970 -0.00834 509 LEU   A CB  
3362 C  CG  . LEU   A 432 ? 0.43794 0.38342 0.43143 0.00562  -0.00824 -0.00998 509 LEU   A CG  
3363 C  CD1 . LEU   A 432 ? 0.46014 0.40639 0.45177 0.00400  -0.00862 -0.01029 509 LEU   A CD1 
3364 C  CD2 . LEU   A 432 ? 0.36453 0.31327 0.36281 0.00949  -0.00618 -0.01058 509 LEU   A CD2 
3365 N  N   . PRO   A 433 ? 0.49131 0.45153 0.49371 0.00109  -0.01058 -0.00553 510 PRO   A N   
3366 C  CA  . PRO   A 433 ? 0.44158 0.40593 0.44497 -0.00163 -0.01153 -0.00383 510 PRO   A CA  
3367 C  C   . PRO   A 433 ? 0.46815 0.43497 0.47052 -0.00475 -0.01271 -0.00259 510 PRO   A C   
3368 O  O   . PRO   A 433 ? 0.48555 0.45296 0.48765 -0.00460 -0.01252 -0.00301 510 PRO   A O   
3369 C  CB  . PRO   A 433 ? 0.40931 0.37979 0.41708 0.00016  -0.00973 -0.00381 510 PRO   A CB  
3370 C  CG  . PRO   A 433 ? 0.40423 0.37528 0.41339 0.00280  -0.00827 -0.00520 510 PRO   A CG  
3371 C  CD  . PRO   A 433 ? 0.45194 0.41638 0.45831 0.00397  -0.00865 -0.00633 510 PRO   A CD  
3372 N  N   . GLU   A 434 ? 0.50057 0.46918 0.50244 -0.00786 -0.01409 -0.00074 511 GLU   A N   
3373 C  CA  . GLU   A 434 ? 0.52851 0.50110 0.53031 -0.01120 -0.01537 0.00122  511 GLU   A CA  
3374 C  C   . GLU   A 434 ? 0.51539 0.49661 0.52233 -0.00985 -0.01357 0.00210  511 GLU   A C   
3375 O  O   . GLU   A 434 ? 0.48142 0.46645 0.48913 -0.01169 -0.01433 0.00368  511 GLU   A O   
3376 C  CB  . GLU   A 434 ? 0.52862 0.50190 0.52916 -0.01487 -0.01715 0.00336  511 GLU   A CB  
3377 C  CG  . GLU   A 434 ? 0.57776 0.54720 0.57724 -0.01408 -0.01711 0.00278  511 GLU   A CG  
3378 C  CD  . GLU   A 434 ? 0.60907 0.56941 0.60265 -0.01594 -0.01923 0.00243  511 GLU   A CD  
3379 O  OE1 . GLU   A 434 ? 0.68411 0.64235 0.67410 -0.01955 -0.02126 0.00350  511 GLU   A OE1 
3380 O  OE2 . GLU   A 434 ? 0.63210 0.58714 0.62437 -0.01391 -0.01891 0.00130  511 GLU   A OE2 
3381 N  N   . GLU   A 435 ? 0.48229 0.46627 0.49241 -0.00673 -0.01123 0.00128  512 GLU   A N   
3382 C  CA  . GLU   A 435 ? 0.49210 0.48285 0.50635 -0.00478 -0.00900 0.00186  512 GLU   A CA  
3383 C  C   . GLU   A 435 ? 0.46212 0.45269 0.47691 -0.00297 -0.00840 0.00069  512 GLU   A C   
3384 O  O   . GLU   A 435 ? 0.42233 0.41808 0.44032 -0.00126 -0.00661 0.00126  512 GLU   A O   
3385 C  CB  . GLU   A 435 ? 0.49040 0.48196 0.50612 -0.00226 -0.00679 0.00098  512 GLU   A CB  
3386 C  CG  . GLU   A 435 ? 0.52389 0.51120 0.53739 -0.00314 -0.00777 0.00059  512 GLU   A CG  
3387 C  CD  . GLU   A 435 ? 0.57269 0.56148 0.58534 -0.00648 -0.00920 0.00274  512 GLU   A CD  
3388 O  OE1 . GLU   A 435 ? 0.67909 0.67100 0.69226 -0.00862 -0.01016 0.00448  512 GLU   A OE1 
3389 O  OE2 . GLU   A 435 ? 0.61557 0.60267 0.62706 -0.00723 -0.00951 0.00295  512 GLU   A OE2 
3390 N  N   . ILE   A 436 ? 0.48652 0.47093 0.49796 -0.00317 -0.00966 -0.00085 513 ILE   A N   
3391 C  CA  . ILE   A 436 ? 0.44019 0.42388 0.45139 -0.00193 -0.00929 -0.00188 513 ILE   A CA  
3392 C  C   . ILE   A 436 ? 0.43681 0.42632 0.44970 -0.00403 -0.01006 0.00049  513 ILE   A C   
3393 O  O   . ILE   A 436 ? 0.43875 0.43071 0.45321 -0.00275 -0.00929 0.00041  513 ILE   A O   
3394 C  CB  . ILE   A 436 ? 0.47999 0.45526 0.48611 -0.00237 -0.01052 -0.00356 513 ILE   A CB  
3395 C  CG1 . ILE   A 436 ? 0.47919 0.45280 0.48541 0.00050  -0.00908 -0.00546 513 ILE   A CG1 
3396 C  CG2 . ILE   A 436 ? 0.44026 0.41314 0.44227 -0.00655 -0.01313 -0.00223 513 ILE   A CG2 
3397 C  CD1 . ILE   A 436 ? 0.47832 0.45188 0.48698 0.00408  -0.00706 -0.00691 513 ILE   A CD1 
3398 N  N   . GLY   A 437 ? 0.43952 0.43158 0.45227 -0.00741 -0.01171 0.00293  514 GLY   A N   
3399 C  CA  . GLY   A 437 ? 0.43851 0.43590 0.45247 -0.01036 -0.01323 0.00585  514 GLY   A CA  
3400 C  C   . GLY   A 437 ? 0.41202 0.41883 0.43201 -0.00859 -0.01123 0.00808  514 GLY   A C   
3401 O  O   . GLY   A 437 ? 0.40840 0.42040 0.43022 -0.01047 -0.01233 0.01077  514 GLY   A O   
3402 N  N   . THR   A 438 ? 0.41014 0.41912 0.43297 -0.00513 -0.00831 0.00731  515 THR   A N   
3403 C  CA  . THR   A 438 ? 0.44103 0.45772 0.46885 -0.00278 -0.00581 0.00925  515 THR   A CA  
3404 C  C   . THR   A 438 ? 0.44527 0.46105 0.47387 0.00063  -0.00409 0.00740  515 THR   A C   
3405 O  O   . THR   A 438 ? 0.42852 0.44947 0.46070 0.00320  -0.00166 0.00867  515 THR   A O   
3406 C  CB  . THR   A 438 ? 0.43057 0.44967 0.46010 -0.00110 -0.00329 0.00972  515 THR   A CB  
3407 O  OG1 . THR   A 438 ? 0.42843 0.44071 0.45475 -0.00012 -0.00302 0.00662  515 THR   A OG1 
3408 C  CG2 . THR   A 438 ? 0.44091 0.46448 0.47155 -0.00432 -0.00446 0.01296  515 THR   A CG2 
3409 N  N   . LEU   A 439 ? 0.40002 0.40918 0.42518 0.00085  -0.00511 0.00457  516 LEU   A N   
3410 C  CA  . LEU   A 439 ? 0.38179 0.39004 0.40743 0.00361  -0.00378 0.00296  516 LEU   A CA  
3411 C  C   . LEU   A 439 ? 0.42510 0.43773 0.45227 0.00216  -0.00500 0.00531  516 LEU   A C   
3412 O  O   . LEU   A 439 ? 0.39093 0.40005 0.41505 0.00024  -0.00707 0.00468  516 LEU   A O   
3413 C  CB  . LEU   A 439 ? 0.43202 0.43242 0.45375 0.00422  -0.00436 -0.00032 516 LEU   A CB  
3414 C  CG  . LEU   A 439 ? 0.42554 0.42222 0.44633 0.00573  -0.00331 -0.00223 516 LEU   A CG  
3415 C  CD1 . LEU   A 439 ? 0.40490 0.39494 0.42280 0.00683  -0.00358 -0.00488 516 LEU   A CD1 
3416 C  CD2 . LEU   A 439 ? 0.42199 0.42192 0.44546 0.00849  -0.00058 -0.00223 516 LEU   A CD2 
3417 N  N   . GLU   A 440 ? 0.47809 0.49846 0.50991 0.00320  -0.00353 0.00826  517 GLU   A N   
3418 C  CA  . GLU   A 440 ? 0.52954 0.55598 0.56386 0.00127  -0.00503 0.01173  517 GLU   A CA  
3419 C  C   . GLU   A 440 ? 0.47081 0.49519 0.50397 0.00199  -0.00552 0.01056  517 GLU   A C   
3420 O  O   . GLU   A 440 ? 0.45936 0.48475 0.49150 -0.00114 -0.00818 0.01227  517 GLU   A O   
3421 C  CB  . GLU   A 440 ? 0.56739 0.60286 0.60759 0.00328  -0.00262 0.01536  517 GLU   A CB  
3422 C  CG  . GLU   A 440 ? 0.67321 0.71500 0.71579 -0.00011 -0.00418 0.01948  517 GLU   A CG  
3423 C  CD  . GLU   A 440 ? 0.74688 0.79922 0.79599 0.00120  -0.00265 0.02439  517 GLU   A CD  
3424 O  OE1 . GLU   A 440 ? 0.71104 0.76531 0.76236 0.00416  -0.00107 0.02469  517 GLU   A OE1 
3425 O  OE2 . GLU   A 440 ? 0.70362 0.76246 0.75579 -0.00066 -0.00296 0.02817  517 GLU   A OE2 
3426 N  N   . ASN   A 441 ? 0.43408 0.45549 0.46704 0.00576  -0.00311 0.00783  518 ASN   A N   
3427 C  CA  . ASN   A 441 ? 0.41799 0.43810 0.45034 0.00689  -0.00309 0.00688  518 ASN   A CA  
3428 C  C   . ASN   A 441 ? 0.40868 0.42026 0.43580 0.00643  -0.00405 0.00316  518 ASN   A C   
3429 O  O   . ASN   A 441 ? 0.43197 0.44153 0.45821 0.00794  -0.00346 0.00171  518 ASN   A O   
3430 C  CB  . ASN   A 441 ? 0.38277 0.40535 0.41823 0.01131  0.00029  0.00670  518 ASN   A CB  
3431 C  CG  . ASN   A 441 ? 0.47145 0.50247 0.51211 0.01243  0.00174  0.01078  518 ASN   A CG  
3432 O  OD1 . ASN   A 441 ? 0.50226 0.53867 0.54550 0.01115  0.00042  0.01399  518 ASN   A OD1 
3433 N  ND2 . ASN   A 441 ? 0.42056 0.45276 0.46264 0.01483  0.00455  0.01092  518 ASN   A ND2 
3434 N  N   . LEU   A 442 ? 0.38354 0.39010 0.40721 0.00459  -0.00530 0.00176  519 LEU   A N   
3435 C  CA  . LEU   A 442 ? 0.42626 0.42475 0.44516 0.00473  -0.00570 -0.00145 519 LEU   A CA  
3436 C  C   . LEU   A 442 ? 0.39757 0.39354 0.41300 0.00250  -0.00758 -0.00133 519 LEU   A C   
3437 O  O   . LEU   A 442 ? 0.41444 0.41084 0.42788 -0.00134 -0.01014 0.00065  519 LEU   A O   
3438 C  CB  . LEU   A 442 ? 0.37359 0.36715 0.38941 0.00324  -0.00667 -0.00245 519 LEU   A CB  
3439 C  CG  . LEU   A 442 ? 0.37762 0.36291 0.38901 0.00420  -0.00645 -0.00549 519 LEU   A CG  
3440 C  CD1 . LEU   A 442 ? 0.37694 0.36211 0.39057 0.00816  -0.00391 -0.00740 519 LEU   A CD1 
3441 C  CD2 . LEU   A 442 ? 0.41830 0.39884 0.42662 0.00256  -0.00759 -0.00586 519 LEU   A CD2 
3442 N  N   . GLU   A 443 ? 0.40612 0.39926 0.42038 0.00460  -0.00643 -0.00332 520 GLU   A N   
3443 C  CA  . GLU   A 443 ? 0.40758 0.39730 0.41765 0.00263  -0.00793 -0.00356 520 GLU   A CA  
3444 C  C   . GLU   A 443 ? 0.40144 0.38207 0.40573 0.00306  -0.00756 -0.00665 520 GLU   A C   
3445 O  O   . GLU   A 443 ? 0.42488 0.40018 0.42336 0.00026  -0.00924 -0.00688 520 GLU   A O   
3446 C  CB  . GLU   A 443 ? 0.41342 0.40718 0.42635 0.00451  -0.00688 -0.00300 520 GLU   A CB  
3447 C  CG  . GLU   A 443 ? 0.47448 0.47741 0.49348 0.00487  -0.00669 0.00043  520 GLU   A CG  
3448 C  CD  . GLU   A 443 ? 0.55408 0.56036 0.57599 0.00753  -0.00515 0.00084  520 GLU   A CD  
3449 O  OE1 . GLU   A 443 ? 0.63036 0.63222 0.64926 0.00819  -0.00486 -0.00126 520 GLU   A OE1 
3450 O  OE2 . GLU   A 443 ? 0.56751 0.58059 0.59451 0.00910  -0.00404 0.00335  520 GLU   A OE2 
3451 N  N   . GLU   A 444 ? 0.38156 0.36019 0.38706 0.00642  -0.00534 -0.00879 521 GLU   A N   
3452 C  CA  . GLU   A 444 ? 0.37548 0.34660 0.37670 0.00781  -0.00431 -0.01136 521 GLU   A CA  
3453 C  C   . GLU   A 444 ? 0.40286 0.37169 0.40460 0.00910  -0.00358 -0.01220 521 GLU   A C   
3454 O  O   . GLU   A 444 ? 0.37413 0.34711 0.38048 0.01106  -0.00243 -0.01203 521 GLU   A O   
3455 C  CB  . GLU   A 444 ? 0.40169 0.37353 0.40451 0.01082  -0.00227 -0.01266 521 GLU   A CB  
3456 C  CG  . GLU   A 444 ? 0.45469 0.43147 0.45939 0.01010  -0.00282 -0.01119 521 GLU   A CG  
3457 C  CD  . GLU   A 444 ? 0.53273 0.51013 0.53883 0.01287  -0.00090 -0.01236 521 GLU   A CD  
3458 O  OE1 . GLU   A 444 ? 0.54593 0.51936 0.55071 0.01493  0.00068  -0.01432 521 GLU   A OE1 
3459 O  OE2 . GLU   A 444 ? 0.64646 0.62853 0.65510 0.01301  -0.00097 -0.01105 521 GLU   A OE2 
3460 N  N   . LEU   A 445 ? 0.41465 0.37638 0.41111 0.00786  -0.00429 -0.01297 522 LEU   A N   
3461 C  CA  . LEU   A 445 ? 0.38207 0.34069 0.37840 0.00912  -0.00371 -0.01360 522 LEU   A CA  
3462 C  C   . LEU   A 445 ? 0.42259 0.37316 0.41419 0.01094  -0.00229 -0.01543 522 LEU   A C   
3463 O  O   . LEU   A 445 ? 0.44459 0.38832 0.42955 0.00903  -0.00306 -0.01590 522 LEU   A O   
3464 C  CB  . LEU   A 445 ? 0.38877 0.34647 0.38318 0.00580  -0.00590 -0.01223 522 LEU   A CB  
3465 C  CG  . LEU   A 445 ? 0.38119 0.33500 0.37468 0.00649  -0.00575 -0.01258 522 LEU   A CG  
3466 C  CD1 . LEU   A 445 ? 0.36428 0.32334 0.36389 0.00937  -0.00424 -0.01258 522 LEU   A CD1 
3467 C  CD2 . LEU   A 445 ? 0.33696 0.29044 0.32841 0.00262  -0.00819 -0.01097 522 LEU   A CD2 
3468 N  N   . TYR   A 446 ? 0.35893 0.31005 0.35355 0.01455  -0.00015 -0.01626 523 TYR   A N   
3469 C  CA  . TYR   A 446 ? 0.41017 0.35447 0.40119 0.01694  0.00171  -0.01755 523 TYR   A CA  
3470 C  C   . TYR   A 446 ? 0.40509 0.34655 0.39639 0.01828  0.00207  -0.01725 523 TYR   A C   
3471 O  O   . TYR   A 446 ? 0.34820 0.29461 0.34502 0.01978  0.00242  -0.01656 523 TYR   A O   
3472 C  CB  . TYR   A 446 ? 0.36890 0.31588 0.36303 0.02005  0.00394  -0.01822 523 TYR   A CB  
3473 C  CG  . TYR   A 446 ? 0.37947 0.32841 0.37276 0.01887  0.00365  -0.01849 523 TYR   A CG  
3474 C  CD1 . TYR   A 446 ? 0.41995 0.36283 0.40714 0.01838  0.00418  -0.01949 523 TYR   A CD1 
3475 C  CD2 . TYR   A 446 ? 0.40545 0.36187 0.40360 0.01824  0.00293  -0.01764 523 TYR   A CD2 
3476 C  CE1 . TYR   A 446 ? 0.44451 0.38948 0.43099 0.01705  0.00366  -0.01950 523 TYR   A CE1 
3477 C  CE2 . TYR   A 446 ? 0.37962 0.33810 0.37735 0.01731  0.00261  -0.01755 523 TYR   A CE2 
3478 C  CZ  . TYR   A 446 ? 0.40410 0.35722 0.39627 0.01660  0.00281  -0.01841 523 TYR   A CZ  
3479 O  OH  . TYR   A 446 ? 0.50507 0.46062 0.49703 0.01549  0.00227  -0.01807 523 TYR   A OH  
3480 N  N   . LEU   A 447 ? 0.41297 0.34592 0.39776 0.01757  0.00193  -0.01768 524 LEU   A N   
3481 C  CA  . LEU   A 447 ? 0.43282 0.36187 0.41692 0.01874  0.00218  -0.01723 524 LEU   A CA  
3482 C  C   . LEU   A 447 ? 0.42559 0.34670 0.40560 0.02210  0.00482  -0.01801 524 LEU   A C   
3483 O  O   . LEU   A 447 ? 0.44760 0.36454 0.42655 0.02353  0.00532  -0.01747 524 LEU   A O   
3484 C  CB  . LEU   A 447 ? 0.40744 0.33293 0.38716 0.01479  -0.00042 -0.01663 524 LEU   A CB  
3485 C  CG  . LEU   A 447 ? 0.38348 0.31718 0.36792 0.01191  -0.00271 -0.01528 524 LEU   A CG  
3486 C  CD1 . LEU   A 447 ? 0.39624 0.32644 0.37588 0.00759  -0.00532 -0.01443 524 LEU   A CD1 
3487 C  CD2 . LEU   A 447 ? 0.40164 0.34103 0.39273 0.01397  -0.00218 -0.01448 524 LEU   A CD2 
3488 N  N   . ASN   A 448 ? 0.41961 0.33870 0.39750 0.02367  0.00674  -0.01907 525 ASN   A N   
3489 C  CA  . ASN   A 448 ? 0.41708 0.32771 0.38996 0.02692  0.00971  -0.01980 525 ASN   A CA  
3490 C  C   . ASN   A 448 ? 0.47021 0.38313 0.44866 0.03135  0.01182  -0.01855 525 ASN   A C   
3491 O  O   . ASN   A 448 ? 0.44027 0.36227 0.42688 0.03238  0.01160  -0.01745 525 ASN   A O   
3492 C  CB  . ASN   A 448 ? 0.41444 0.32404 0.38501 0.02784  0.01153  -0.02099 525 ASN   A CB  
3493 C  CG  . ASN   A 448 ? 0.40927 0.32899 0.38837 0.02967  0.01228  -0.02046 525 ASN   A CG  
3494 O  OD1 . ASN   A 448 ? 0.37384 0.30017 0.35628 0.02729  0.01035  -0.02034 525 ASN   A OD1 
3495 N  ND2 . ASN   A 448 ? 0.41922 0.34008 0.40173 0.03392  0.01514  -0.01990 525 ASN   A ND2 
3496 N  N   . ASP   A 449 ? 0.46254 0.36677 0.43614 0.03388  0.01387  -0.01849 526 ASP   A N   
3497 C  CA  . ASP   A 449 ? 0.44639 0.35228 0.42501 0.03855  0.01622  -0.01681 526 ASP   A CA  
3498 C  C   . ASP   A 449 ? 0.43154 0.34368 0.41651 0.03765  0.01391  -0.01504 526 ASP   A C   
3499 O  O   . ASP   A 449 ? 0.46441 0.38470 0.45738 0.03949  0.01419  -0.01341 526 ASP   A O   
3500 C  CB  . ASP   A 449 ? 0.43213 0.34432 0.41641 0.04176  0.01867  -0.01634 526 ASP   A CB  
3501 C  CG  . ASP   A 449 ? 0.48540 0.39016 0.46299 0.04362  0.02175  -0.01778 526 ASP   A CG  
3502 O  OD1 . ASP   A 449 ? 0.54156 0.43712 0.51352 0.04644  0.02436  -0.01776 526 ASP   A OD1 
3503 O  OD2 . ASP   A 449 ? 0.50423 0.41149 0.48137 0.04216  0.02157  -0.01896 526 ASP   A OD2 
3504 N  N   . ASN   A 450 ? 0.48385 0.39202 0.46477 0.03435  0.01144  -0.01527 527 ASN   A N   
3505 C  CA  . ASN   A 450 ? 0.46700 0.37843 0.45180 0.03342  0.00942  -0.01365 527 ASN   A CA  
3506 C  C   . ASN   A 450 ? 0.48381 0.38477 0.46218 0.03449  0.01011  -0.01333 527 ASN   A C   
3507 O  O   . ASN   A 450 ? 0.46928 0.36438 0.44142 0.03094  0.00807  -0.01401 527 ASN   A O   
3508 C  CB  . ASN   A 450 ? 0.38766 0.30414 0.37359 0.02852  0.00597  -0.01392 527 ASN   A CB  
3509 C  CG  . ASN   A 450 ? 0.44571 0.37305 0.43958 0.02837  0.00541  -0.01336 527 ASN   A CG  
3510 O  OD1 . ASN   A 450 ? 0.38844 0.32097 0.38809 0.02962  0.00522  -0.01179 527 ASN   A OD1 
3511 N  ND2 . ASN   A 450 ? 0.39723 0.32775 0.39111 0.02680  0.00514  -0.01451 527 ASN   A ND2 
3512 N  N   . PRO   A 451 ? 0.48807 0.38647 0.46778 0.03939  0.01304  -0.01204 528 PRO   A N   
3513 C  CA  . PRO   A 451 ? 0.50819 0.39474 0.48050 0.04127  0.01456  -0.01187 528 PRO   A CA  
3514 C  C   . PRO   A 451 ? 0.50420 0.38897 0.47574 0.03891  0.01185  -0.01079 528 PRO   A C   
3515 O  O   . PRO   A 451 ? 0.47832 0.35224 0.44251 0.03965  0.01263  -0.01082 528 PRO   A O   
3516 C  CB  . PRO   A 451 ? 0.50748 0.39478 0.48410 0.04764  0.01848  -0.00996 528 PRO   A CB  
3517 C  CG  . PRO   A 451 ? 0.54601 0.44750 0.53393 0.04807  0.01774  -0.00845 528 PRO   A CG  
3518 C  CD  . PRO   A 451 ? 0.46074 0.36691 0.44855 0.04343  0.01525  -0.01050 528 PRO   A CD  
3519 N  N   . ASN   A 452 ? 0.49418 0.38854 0.47240 0.03611  0.00885  -0.00984 529 ASN   A N   
3520 C  CA  . ASN   A 452 ? 0.46721 0.36061 0.44503 0.03368  0.00624  -0.00868 529 ASN   A CA  
3521 C  C   . ASN   A 452 ? 0.48730 0.38135 0.46184 0.02771  0.00286  -0.00989 529 ASN   A C   
3522 O  O   . ASN   A 452 ? 0.50601 0.40043 0.48058 0.02511  0.00048  -0.00891 529 ASN   A O   
3523 C  CB  . ASN   A 452 ? 0.48647 0.38970 0.47388 0.03496  0.00543  -0.00620 529 ASN   A CB  
3524 C  CG  . ASN   A 452 ? 0.52337 0.42551 0.51404 0.04058  0.00821  -0.00390 529 ASN   A CG  
3525 O  OD1 . ASN   A 452 ? 0.49803 0.39036 0.48297 0.04347  0.01050  -0.00389 529 ASN   A OD1 
3526 N  ND2 . ASN   A 452 ? 0.53022 0.44233 0.52990 0.04211  0.00809  -0.00172 529 ASN   A ND2 
3527 N  N   . LEU   A 453 ? 0.47449 0.36901 0.44640 0.02544  0.00259  -0.01168 530 LEU   A N   
3528 C  CA  . LEU   A 453 ? 0.47981 0.37683 0.44998 0.01991  -0.00056 -0.01221 530 LEU   A CA  
3529 C  C   . LEU   A 453 ? 0.49994 0.38532 0.45946 0.01694  -0.00159 -0.01298 530 LEU   A C   
3530 O  O   . LEU   A 453 ? 0.51516 0.39372 0.46796 0.01662  -0.00059 -0.01445 530 LEU   A O   
3531 C  CB  . LEU   A 453 ? 0.47761 0.38156 0.45076 0.01895  -0.00051 -0.01323 530 LEU   A CB  
3532 C  CG  . LEU   A 453 ? 0.45736 0.36548 0.42989 0.01385  -0.00330 -0.01337 530 LEU   A CG  
3533 C  CD1 . LEU   A 453 ? 0.44360 0.35963 0.42188 0.01191  -0.00528 -0.01189 530 LEU   A CD1 
3534 C  CD2 . LEU   A 453 ? 0.43826 0.35148 0.41305 0.01401  -0.00257 -0.01430 530 LEU   A CD2 
3535 N  N   . HIS   A 454 ? 0.51968 0.40220 0.47697 0.01446  -0.00370 -0.01192 531 HIS   A N   
3536 C  CA  . HIS   A 454 ? 0.49615 0.36701 0.44275 0.01114  -0.00501 -0.01240 531 HIS   A CA  
3537 C  C   . HIS   A 454 ? 0.50146 0.37552 0.44631 0.00467  -0.00867 -0.01204 531 HIS   A C   
3538 O  O   . HIS   A 454 ? 0.52199 0.38688 0.45761 0.00087  -0.01031 -0.01224 531 HIS   A O   
3539 C  CB  . HIS   A 454 ? 0.54063 0.40436 0.48455 0.01264  -0.00483 -0.01126 531 HIS   A CB  
3540 C  CG  . HIS   A 454 ? 0.51902 0.37760 0.46305 0.01905  -0.00101 -0.01119 531 HIS   A CG  
3541 N  ND1 . HIS   A 454 ? 0.54760 0.39303 0.48205 0.02110  0.00149  -0.01239 531 HIS   A ND1 
3542 C  CD2 . HIS   A 454 ? 0.48519 0.35029 0.43779 0.02389  0.00087  -0.00978 531 HIS   A CD2 
3543 C  CE1 . HIS   A 454 ? 0.53332 0.37771 0.47094 0.02740  0.00507  -0.01162 531 HIS   A CE1 
3544 N  NE2 . HIS   A 454 ? 0.52550 0.38213 0.47441 0.02903  0.00455  -0.00987 531 HIS   A NE2 
3545 N  N   . SER   A 455 ? 0.53910 0.42571 0.49229 0.00331  -0.00990 -0.01131 532 SER   A N   
3546 C  CA  . SER   A 455 ? 0.52853 0.42021 0.48181 -0.00230 -0.01306 -0.01032 532 SER   A CA  
3547 C  C   . SER   A 455 ? 0.50982 0.41180 0.46917 -0.00256 -0.01293 -0.01046 532 SER   A C   
3548 O  O   . SER   A 455 ? 0.53437 0.44222 0.50012 0.00134  -0.01083 -0.01098 532 SER   A O   
3549 C  CB  . SER   A 455 ? 0.53902 0.43606 0.49666 -0.00395 -0.01481 -0.00852 532 SER   A CB  
3550 O  OG  . SER   A 455 ? 0.65400 0.54208 0.60420 -0.00692 -0.01659 -0.00788 532 SER   A OG  
3551 N  N   . LEU   A 456 ? 0.47093 0.37498 0.42809 -0.00736 -0.01530 -0.00970 533 LEU   A N   
3552 C  CA  . LEU   A 456 ? 0.45280 0.36781 0.41623 -0.00853 -0.01584 -0.00891 533 LEU   A CA  
3553 C  C   . LEU   A 456 ? 0.49378 0.41463 0.45913 -0.01304 -0.01854 -0.00655 533 LEU   A C   
3554 O  O   . LEU   A 456 ? 0.42743 0.34229 0.38634 -0.01717 -0.02084 -0.00568 533 LEU   A O   
3555 C  CB  . LEU   A 456 ? 0.44200 0.35465 0.40114 -0.01017 -0.01614 -0.00960 533 LEU   A CB  
3556 C  CG  . LEU   A 456 ? 0.47798 0.39189 0.43924 -0.00628 -0.01357 -0.01127 533 LEU   A CG  
3557 C  CD1 . LEU   A 456 ? 0.45951 0.37360 0.42500 -0.00068 -0.01063 -0.01237 533 LEU   A CD1 
3558 C  CD2 . LEU   A 456 ? 0.45729 0.36106 0.40903 -0.00775 -0.01361 -0.01255 533 LEU   A CD2 
3559 N  N   . PRO   A 457 ? 0.48966 0.42166 0.46324 -0.01242 -0.01822 -0.00538 534 PRO   A N   
3560 C  CA  . PRO   A 457 ? 0.45023 0.38820 0.42581 -0.01647 -0.02038 -0.00285 534 PRO   A CA  
3561 C  C   . PRO   A 457 ? 0.43183 0.37218 0.40534 -0.02095 -0.02257 -0.00120 534 PRO   A C   
3562 O  O   . PRO   A 457 ? 0.40404 0.34609 0.37807 -0.02027 -0.02202 -0.00171 534 PRO   A O   
3563 C  CB  . PRO   A 457 ? 0.45577 0.40414 0.44013 -0.01372 -0.01862 -0.00233 534 PRO   A CB  
3564 C  CG  . PRO   A 457 ? 0.46117 0.41093 0.44806 -0.00985 -0.01637 -0.00409 534 PRO   A CG  
3565 C  CD  . PRO   A 457 ? 0.44806 0.38742 0.42889 -0.00826 -0.01579 -0.00614 534 PRO   A CD  
3566 N  N   . PHE   A 458 ? 0.44756 0.38852 0.41894 -0.02583 -0.02525 0.00115  535 PHE   A N   
3567 C  CA  . PHE   A 458 ? 0.44602 0.39079 0.41624 -0.03078 -0.02781 0.00362  535 PHE   A CA  
3568 C  C   . PHE   A 458 ? 0.44621 0.40377 0.42518 -0.02943 -0.02673 0.00528  535 PHE   A C   
3569 O  O   . PHE   A 458 ? 0.44037 0.40098 0.41906 -0.03190 -0.02809 0.00677  535 PHE   A O   
3570 C  CB  . PHE   A 458 ? 0.45560 0.40003 0.42301 -0.03622 -0.03082 0.00629  535 PHE   A CB  
3571 C  CG  . PHE   A 458 ? 0.47282 0.40366 0.42913 -0.03964 -0.03294 0.00540  535 PHE   A CG  
3572 C  CD1 . PHE   A 458 ? 0.47162 0.39558 0.42060 -0.04225 -0.03432 0.00485  535 PHE   A CD1 
3573 C  CD2 . PHE   A 458 ? 0.49402 0.41840 0.44658 -0.04040 -0.03354 0.00521  535 PHE   A CD2 
3574 C  CE1 . PHE   A 458 ? 0.47954 0.38973 0.41706 -0.04546 -0.03604 0.00395  535 PHE   A CE1 
3575 C  CE2 . PHE   A 458 ? 0.51235 0.42317 0.45384 -0.04347 -0.03532 0.00443  535 PHE   A CE2 
3576 C  CZ  . PHE   A 458 ? 0.44579 0.34918 0.37948 -0.04597 -0.03646 0.00372  535 PHE   A CZ  
3577 N  N   . GLU   A 459 ? 0.45062 0.41541 0.43696 -0.02567 -0.02431 0.00523  536 GLU   A N   
3578 C  CA  . GLU   A 459 ? 0.44419 0.42033 0.43820 -0.02419 -0.02295 0.00696  536 GLU   A CA  
3579 C  C   . GLU   A 459 ? 0.41910 0.39523 0.41399 -0.02124 -0.02145 0.00527  536 GLU   A C   
3580 O  O   . GLU   A 459 ? 0.40519 0.38986 0.40554 -0.02034 -0.02060 0.00691  536 GLU   A O   
3581 C  CB  . GLU   A 459 ? 0.39499 0.37734 0.39523 -0.02090 -0.02044 0.00710  536 GLU   A CB  
3582 C  CG  . GLU   A 459 ? 0.51179 0.48787 0.50980 -0.01930 -0.01981 0.00510  536 GLU   A CG  
3583 C  CD  . GLU   A 459 ? 0.51596 0.48894 0.51025 -0.02348 -0.02226 0.00667  536 GLU   A CD  
3584 O  OE1 . GLU   A 459 ? 0.51032 0.49034 0.50737 -0.02632 -0.02318 0.00972  536 GLU   A OE1 
3585 O  OE2 . GLU   A 459 ? 0.53638 0.49985 0.52500 -0.02377 -0.02311 0.00502  536 GLU   A OE2 
3586 N  N   . LEU   A 460 ? 0.42093 0.38777 0.41063 -0.01959 -0.02094 0.00224  537 LEU   A N   
3587 C  CA  . LEU   A 460 ? 0.41608 0.38235 0.40560 -0.01762 -0.01990 0.00087  537 LEU   A CA  
3588 C  C   . LEU   A 460 ? 0.42599 0.39502 0.41397 -0.02187 -0.02237 0.00327  537 LEU   A C   
3589 O  O   . LEU   A 460 ? 0.42167 0.39393 0.41171 -0.02055 -0.02165 0.00323  537 LEU   A O   
3590 C  CB  . LEU   A 460 ? 0.44385 0.39902 0.42715 -0.01556 -0.01894 -0.00242 537 LEU   A CB  
3591 C  CG  . LEU   A 460 ? 0.50587 0.45958 0.48929 -0.01216 -0.01693 -0.00453 537 LEU   A CG  
3592 C  CD1 . LEU   A 460 ? 0.40336 0.36598 0.39512 -0.00817 -0.01452 -0.00457 537 LEU   A CD1 
3593 C  CD2 . LEU   A 460 ? 0.39151 0.33461 0.36935 -0.00965 -0.01549 -0.00736 537 LEU   A CD2 
3594 N  N   . ALA   A 461 ? 0.41720 0.38532 0.40165 -0.02722 -0.02548 0.00567  538 ALA   A N   
3595 C  CA  . ALA   A 461 ? 0.46053 0.43306 0.44444 -0.03191 -0.02828 0.00889  538 ALA   A CA  
3596 C  C   . ALA   A 461 ? 0.41275 0.39921 0.40643 -0.03073 -0.02740 0.01213  538 ALA   A C   
3597 O  O   . ALA   A 461 ? 0.40155 0.39326 0.39664 -0.03312 -0.02899 0.01479  538 ALA   A O   
3598 C  CB  . ALA   A 461 ? 0.43354 0.40229 0.41151 -0.03835 -0.03201 0.01113  538 ALA   A CB  
3599 N  N   . LEU   A 462 ? 0.40531 0.39755 0.40539 -0.02712 -0.02483 0.01216  539 LEU   A N   
3600 C  CA  . LEU   A 462 ? 0.42770 0.43212 0.43648 -0.02525 -0.02324 0.01509  539 LEU   A CA  
3601 C  C   . LEU   A 462 ? 0.43019 0.43687 0.44236 -0.02067 -0.02065 0.01359  539 LEU   A C   
3602 O  O   . LEU   A 462 ? 0.40290 0.41888 0.42184 -0.01860 -0.01899 0.01596  539 LEU   A O   
3603 C  CB  . LEU   A 462 ? 0.38118 0.38966 0.39429 -0.02306 -0.02112 0.01546  539 LEU   A CB  
3604 C  CG  . LEU   A 462 ? 0.41525 0.42307 0.42624 -0.02723 -0.02328 0.01734  539 LEU   A CG  
3605 C  CD1 . LEU   A 462 ? 0.38179 0.39306 0.39684 -0.02432 -0.02063 0.01718  539 LEU   A CD1 
3606 C  CD2 . LEU   A 462 ? 0.33806 0.35332 0.35078 -0.03234 -0.02616 0.02233  539 LEU   A CD2 
3607 N  N   . CYS   A 463 ? 0.42758 0.42593 0.43516 -0.01888 -0.02007 0.00990  540 CYS   A N   
3608 C  CA  . CYS   A 463 ? 0.39203 0.39190 0.40237 -0.01465 -0.01766 0.00830  540 CYS   A CA  
3609 C  C   . CYS   A 463 ? 0.42221 0.42352 0.43120 -0.01722 -0.01966 0.01002  540 CYS   A C   
3610 O  O   . CYS   A 463 ? 0.46434 0.45814 0.46743 -0.01807 -0.02050 0.00789  540 CYS   A O   
3611 C  CB  . CYS   A 463 ? 0.37274 0.36396 0.37957 -0.01131 -0.01582 0.00388  540 CYS   A CB  
3612 S  SG  . CYS   A 463 ? 0.43630 0.42678 0.44534 -0.00831 -0.01364 0.00233  540 CYS   A SG  
3613 N  N   . SER   A 464 ? 0.41585 0.42724 0.43053 -0.01833 -0.02024 0.01417  541 SER   A N   
3614 C  CA  . SER   A 464 ? 0.44212 0.45640 0.45601 -0.02189 -0.02294 0.01702  541 SER   A CA  
3615 C  C   . SER   A 464 ? 0.44449 0.45774 0.45847 -0.01909 -0.02165 0.01540  541 SER   A C   
3616 O  O   . SER   A 464 ? 0.46102 0.47499 0.47303 -0.02222 -0.02406 0.01727  541 SER   A O   
3617 C  CB  . SER   A 464 ? 0.43769 0.46436 0.45890 -0.02336 -0.02364 0.02257  541 SER   A CB  
3618 O  OG  . SER   A 464 ? 0.48441 0.51783 0.51294 -0.01777 -0.01976 0.02285  541 SER   A OG  
3619 N  N   . LYS   A 465 ? 0.43243 0.44406 0.44840 -0.01367 -0.01814 0.01221  542 LYS   A N   
3620 C  CA  . LYS   A 465 ? 0.40953 0.41932 0.42490 -0.01124 -0.01699 0.01046  542 LYS   A CA  
3621 C  C   . LYS   A 465 ? 0.38294 0.38164 0.39138 -0.01039 -0.01643 0.00587  542 LYS   A C   
3622 O  O   . LYS   A 465 ? 0.38159 0.37803 0.38906 -0.00826 -0.01525 0.00408  542 LYS   A O   
3623 C  CB  . LYS   A 465 ? 0.38894 0.40488 0.41119 -0.00593 -0.01348 0.01054  542 LYS   A CB  
3624 C  CG  . LYS   A 465 ? 0.44250 0.46945 0.47183 -0.00583 -0.01326 0.01531  542 LYS   A CG  
3625 C  CD  . LYS   A 465 ? 0.51172 0.54325 0.54582 -0.00137 -0.01051 0.01582  542 LYS   A CD  
3626 C  CE  . LYS   A 465 ? 0.48704 0.52440 0.52693 0.00256  -0.00713 0.01714  542 LYS   A CE  
3627 N  NZ  . LYS   A 465 ? 0.57799 0.62381 0.62228 0.00043  -0.00808 0.02199  542 LYS   A NZ  
3628 N  N   . LEU   A 466 ? 0.44979 0.44157 0.45334 -0.01198 -0.01720 0.00421  543 LEU   A N   
3629 C  CA  . LEU   A 466 ? 0.40998 0.39134 0.40733 -0.01057 -0.01618 0.00021  543 LEU   A CA  
3630 C  C   . LEU   A 466 ? 0.39679 0.37185 0.38702 -0.01347 -0.01794 -0.00032 543 LEU   A C   
3631 O  O   . LEU   A 466 ? 0.44980 0.42119 0.43441 -0.01841 -0.02090 0.00103  543 LEU   A O   
3632 C  CB  . LEU   A 466 ? 0.39113 0.36690 0.38514 -0.01158 -0.01661 -0.00082 543 LEU   A CB  
3633 C  CG  . LEU   A 466 ? 0.41934 0.38504 0.40812 -0.00914 -0.01494 -0.00457 543 LEU   A CG  
3634 C  CD1 . LEU   A 466 ? 0.40072 0.36882 0.39445 -0.00378 -0.01168 -0.00648 543 LEU   A CD1 
3635 C  CD2 . LEU   A 466 ? 0.39611 0.35606 0.38134 -0.01031 -0.01560 -0.00512 543 LEU   A CD2 
3636 N  N   . SER   A 467 ? 0.38968 0.36300 0.37951 -0.01067 -0.01616 -0.00224 544 SER   A N   
3637 C  CA  . SER   A 467 ? 0.43022 0.39687 0.41276 -0.01296 -0.01731 -0.00311 544 SER   A CA  
3638 C  C   . SER   A 467 ? 0.42951 0.38634 0.40652 -0.01010 -0.01489 -0.00706 544 SER   A C   
3639 O  O   . SER   A 467 ? 0.47675 0.42557 0.44567 -0.01223 -0.01562 -0.00813 544 SER   A O   
3640 C  CB  . SER   A 467 ? 0.43427 0.40766 0.42056 -0.01281 -0.01762 -0.00128 544 SER   A CB  
3641 O  OG  . SER   A 467 ? 0.46049 0.43819 0.45301 -0.00756 -0.01448 -0.00251 544 SER   A OG  
3642 N  N   . ILE   A 468 ? 0.43349 0.39057 0.41431 -0.00550 -0.01203 -0.00900 545 ILE   A N   
3643 C  CA  . ILE   A 468 ? 0.41566 0.36488 0.39264 -0.00230 -0.00945 -0.01215 545 ILE   A CA  
3644 C  C   . ILE   A 468 ? 0.40527 0.35155 0.38261 -0.00067 -0.00850 -0.01306 545 ILE   A C   
3645 O  O   . ILE   A 468 ? 0.40975 0.36248 0.39368 0.00083  -0.00808 -0.01223 545 ILE   A O   
3646 C  CB  . ILE   A 468 ? 0.42342 0.37669 0.40543 0.00199  -0.00679 -0.01325 545 ILE   A CB  
3647 C  CG1 . ILE   A 468 ? 0.43884 0.39273 0.41887 0.00066  -0.00744 -0.01281 545 ILE   A CG1 
3648 C  CG2 . ILE   A 468 ? 0.40272 0.35017 0.38315 0.00580  -0.00392 -0.01582 545 ILE   A CG2 
3649 C  CD1 . ILE   A 468 ? 0.44015 0.40046 0.42654 0.00415  -0.00550 -0.01295 545 ILE   A CD1 
3650 N  N   . MET   A 469 ? 0.46004 0.39620 0.43000 -0.00076 -0.00795 -0.01474 546 MET   A N   
3651 C  CA  . MET   A 469 ? 0.47970 0.41218 0.44967 0.00139  -0.00672 -0.01562 546 MET   A CA  
3652 C  C   . MET   A 469 ? 0.48669 0.40864 0.44969 0.00360  -0.00445 -0.01785 546 MET   A C   
3653 O  O   . MET   A 469 ? 0.51956 0.43380 0.47420 0.00126  -0.00502 -0.01849 546 MET   A O   
3654 C  CB  . MET   A 469 ? 0.48135 0.41244 0.44903 -0.00243 -0.00936 -0.01413 546 MET   A CB  
3655 C  CG  . MET   A 469 ? 0.50722 0.43501 0.47530 -0.00036 -0.00835 -0.01472 546 MET   A CG  
3656 S  SD  . MET   A 469 ? 0.58489 0.51054 0.54986 -0.00499 -0.01146 -0.01295 546 MET   A SD  
3657 C  CE  . MET   A 469 ? 0.48365 0.39578 0.43536 -0.00894 -0.01292 -0.01375 546 MET   A CE  
3658 N  N   . SER   A 470 ? 0.47223 0.39387 0.43851 0.00809  -0.00178 -0.01880 547 SER   A N   
3659 C  CA  . SER   A 470 ? 0.50122 0.41298 0.46147 0.01075  0.00075  -0.02038 547 SER   A CA  
3660 C  C   . SER   A 470 ? 0.46107 0.36953 0.42119 0.01175  0.00088  -0.02004 547 SER   A C   
3661 O  O   . SER   A 470 ? 0.44424 0.35995 0.41151 0.01234  0.00020  -0.01894 547 SER   A O   
3662 C  CB  . SER   A 470 ? 0.43695 0.35106 0.40113 0.01548  0.00404  -0.02129 547 SER   A CB  
3663 O  OG  . SER   A 470 ? 0.43544 0.35803 0.40882 0.01803  0.00459  -0.02044 547 SER   A OG  
3664 N  N   . ILE   A 471 ? 0.52143 0.41834 0.47278 0.01182  0.00176  -0.02093 548 ILE   A N   
3665 C  CA  . ILE   A 471 ? 0.51824 0.41053 0.46845 0.01299  0.00205  -0.02054 548 ILE   A CA  
3666 C  C   . ILE   A 471 ? 0.50954 0.39036 0.45262 0.01652  0.00540  -0.02178 548 ILE   A C   
3667 O  O   . ILE   A 471 ? 0.51314 0.38635 0.45182 0.01710  0.00576  -0.02163 548 ILE   A O   
3668 C  CB  . ILE   A 471 ? 0.47431 0.36365 0.41996 0.00773  -0.00149 -0.01961 548 ILE   A CB  
3669 C  CG1 . ILE   A 471 ? 0.52209 0.40634 0.45945 0.00290  -0.00351 -0.01994 548 ILE   A CG1 
3670 C  CG2 . ILE   A 471 ? 0.47310 0.37378 0.42777 0.00633  -0.00368 -0.01786 548 ILE   A CG2 
3671 C  CD1 . ILE   A 471 ? 0.50234 0.37242 0.42811 0.00370  -0.00137 -0.02176 548 ILE   A CD1 
3672 N  N   . GLU   A 472 ? 0.48301 0.36234 0.42481 0.01912  0.00810  -0.02288 549 GLU   A N   
3673 C  CA  . GLU   A 472 ? 0.55007 0.41897 0.48554 0.02323  0.01203  -0.02387 549 GLU   A CA  
3674 C  C   . GLU   A 472 ? 0.55308 0.42395 0.49461 0.02812  0.01418  -0.02268 549 GLU   A C   
3675 O  O   . GLU   A 472 ? 0.54744 0.42949 0.49957 0.02994  0.01404  -0.02145 549 GLU   A O   
3676 C  CB  . GLU   A 472 ? 0.56145 0.43105 0.49672 0.02559  0.01476  -0.02488 549 GLU   A CB  
3677 C  CG  . GLU   A 472 ? 0.62293 0.48258 0.55226 0.03044  0.01950  -0.02569 549 GLU   A CG  
3678 C  CD  . GLU   A 472 ? 0.69677 0.55815 0.62648 0.03264  0.02223  -0.02651 549 GLU   A CD  
3679 O  OE1 . GLU   A 472 ? 0.69417 0.56725 0.63432 0.03461  0.02256  -0.02560 549 GLU   A OE1 
3680 O  OE2 . GLU   A 472 ? 0.69092 0.54158 0.60996 0.03207  0.02392  -0.02805 549 GLU   A OE2 
3681 N  N   . ASN   A 473 ? 0.60797 0.46753 0.54230 0.03009  0.01611  -0.02285 550 ASN   A N   
3682 C  CA  . ASN   A 473 ? 0.61779 0.47790 0.55699 0.03512  0.01846  -0.02135 550 ASN   A CA  
3683 C  C   . ASN   A 473 ? 0.58416 0.45130 0.53005 0.03322  0.01523  -0.01973 550 ASN   A C   
3684 O  O   . ASN   A 473 ? 0.58171 0.45521 0.53580 0.03663  0.01615  -0.01799 550 ASN   A O   
3685 C  CB  . ASN   A 473 ? 0.58689 0.45460 0.53445 0.04049  0.02187  -0.02049 550 ASN   A CB  
3686 C  CG  . ASN   A 473 ? 0.66089 0.51998 0.60140 0.04381  0.02623  -0.02171 550 ASN   A CG  
3687 O  OD1 . ASN   A 473 ? 0.76255 0.60801 0.69209 0.04432  0.02803  -0.02274 550 ASN   A OD1 
3688 N  ND2 . ASN   A 473 ? 0.63921 0.50570 0.58543 0.04601  0.02805  -0.02159 550 ASN   A ND2 
3689 N  N   . CYS   A 474 ? 0.53192 0.39834 0.47443 0.02759  0.01137  -0.02003 551 CYS   A N   
3690 C  CA  . CYS   A 474 ? 0.50579 0.37577 0.45185 0.02547  0.00854  -0.01862 551 CYS   A CA  
3691 C  C   . CYS   A 474 ? 0.52911 0.38604 0.46446 0.02328  0.00772  -0.01893 551 CYS   A C   
3692 O  O   . CYS   A 474 ? 0.56921 0.41835 0.49514 0.01935  0.00649  -0.02018 551 CYS   A O   
3693 C  CB  . CYS   A 474 ? 0.46248 0.34268 0.41365 0.02071  0.00482  -0.01823 551 CYS   A CB  
3694 S  SG  . CYS   A 474 ? 0.53154 0.42575 0.49371 0.02258  0.00553  -0.01802 551 CYS   A SG  
3695 N  N   . PRO   A 475 ? 0.49701 0.35099 0.43312 0.02542  0.00818  -0.01768 552 PRO   A N   
3696 C  CA  . PRO   A 475 ? 0.49140 0.33149 0.41638 0.02360  0.00766  -0.01797 552 PRO   A CA  
3697 C  C   . PRO   A 475 ? 0.49434 0.33301 0.41399 0.01626  0.00324  -0.01824 552 PRO   A C   
3698 O  O   . PRO   A 475 ? 0.51437 0.34130 0.42227 0.01320  0.00275  -0.01942 552 PRO   A O   
3699 C  CB  . PRO   A 475 ? 0.51844 0.35987 0.44848 0.02674  0.00810  -0.01600 552 PRO   A CB  
3700 C  CG  . PRO   A 475 ? 0.55055 0.40358 0.49241 0.03156  0.01018  -0.01483 552 PRO   A CG  
3701 C  CD  . PRO   A 475 ? 0.48366 0.34666 0.43044 0.02920  0.00893  -0.01573 552 PRO   A CD  
3702 N  N   . LEU   A 476 ? 0.54291 0.39328 0.47073 0.01324  0.00004  -0.01695 553 LEU   A N   
3703 C  CA  . LEU   A 476 ? 0.54298 0.39423 0.46756 0.00636  -0.00420 -0.01646 553 LEU   A CA  
3704 C  C   . LEU   A 476 ? 0.52867 0.36591 0.44164 0.00352  -0.00539 -0.01646 553 LEU   A C   
3705 O  O   . LEU   A 476 ? 0.54200 0.37273 0.44606 -0.00186 -0.00774 -0.01683 553 LEU   A O   
3706 C  CB  . LEU   A 476 ? 0.50918 0.36323 0.43194 0.00292  -0.00542 -0.01727 553 LEU   A CB  
3707 C  CG  . LEU   A 476 ? 0.51194 0.38029 0.44603 0.00478  -0.00489 -0.01704 553 LEU   A CG  
3708 C  CD1 . LEU   A 476 ? 0.43372 0.30306 0.36489 0.00186  -0.00577 -0.01777 553 LEU   A CD1 
3709 C  CD2 . LEU   A 476 ? 0.43648 0.31641 0.37944 0.00293  -0.00728 -0.01527 553 LEU   A CD2 
3710 N  N   . SER   A 477 ? 0.52636 0.35887 0.43932 0.00696  -0.00393 -0.01578 554 SER   A N   
3711 C  CA  . SER   A 477 ? 0.56727 0.38440 0.46813 0.00524  -0.00431 -0.01596 554 SER   A CA  
3712 C  C   . SER   A 477 ? 0.53362 0.35161 0.43273 -0.00107 -0.00878 -0.01453 554 SER   A C   
3713 O  O   . SER   A 477 ? 0.60793 0.41283 0.49609 -0.00360 -0.00970 -0.01461 554 SER   A O   
3714 C  CB  . SER   A 477 ? 0.51884 0.32948 0.41970 0.01178  -0.00070 -0.01552 554 SER   A CB  
3715 O  OG  . SER   A 477 ? 0.59718 0.41835 0.50893 0.01350  -0.00153 -0.01356 554 SER   A OG  
3716 N  N   . HIS   A 478 ? 0.55073 0.38317 0.45980 -0.00360 -0.01138 -0.01316 555 HIS   A N   
3717 C  CA  . HIS   A 478 ? 0.54140 0.37622 0.44901 -0.01030 -0.01568 -0.01163 555 HIS   A CA  
3718 C  C   . HIS   A 478 ? 0.55087 0.38546 0.45312 -0.01645 -0.01838 -0.01172 555 HIS   A C   
3719 O  O   . HIS   A 478 ? 0.54764 0.38463 0.44849 -0.02250 -0.02209 -0.01006 555 HIS   A O   
3720 C  CB  . HIS   A 478 ? 0.56396 0.41429 0.48426 -0.01016 -0.01688 -0.00993 555 HIS   A CB  
3721 C  CG  . HIS   A 478 ? 0.61980 0.47119 0.54540 -0.00530 -0.01511 -0.00928 555 HIS   A CG  
3722 N  ND1 . HIS   A 478 ? 0.59987 0.46351 0.53582 -0.00473 -0.01583 -0.00786 555 HIS   A ND1 
3723 C  CD2 . HIS   A 478 ? 0.58830 0.42999 0.51015 -0.00081 -0.01263 -0.00957 555 HIS   A CD2 
3724 C  CE1 . HIS   A 478 ? 0.63359 0.49532 0.57200 -0.00050 -0.01424 -0.00724 555 HIS   A CE1 
3725 N  NE2 . HIS   A 478 ? 0.69626 0.54517 0.62672 0.00214  -0.01225 -0.00811 555 HIS   A NE2 
3726 N  N   . LEU   A 479 ? 0.59223 0.42480 0.49197 -0.01525 -0.01677 -0.01325 556 LEU   A N   
3727 C  CA  . LEU   A 479 ? 0.59688 0.42743 0.49010 -0.02103 -0.01926 -0.01326 556 LEU   A CA  
3728 C  C   . LEU   A 479 ? 0.58022 0.39203 0.45765 -0.02235 -0.01851 -0.01489 556 LEU   A C   
3729 O  O   . LEU   A 479 ? 0.61179 0.41417 0.48531 -0.01681 -0.01464 -0.01654 556 LEU   A O   
3730 C  CB  . LEU   A 479 ? 0.53109 0.37193 0.43163 -0.01914 -0.01806 -0.01384 556 LEU   A CB  
3731 C  CG  . LEU   A 479 ? 0.59677 0.45533 0.51073 -0.01958 -0.01945 -0.01203 556 LEU   A CG  
3732 C  CD1 . LEU   A 479 ? 0.52882 0.39624 0.45103 -0.01504 -0.01684 -0.01302 556 LEU   A CD1 
3733 C  CD2 . LEU   A 479 ? 0.59512 0.45788 0.50735 -0.02692 -0.02370 -0.00992 556 LEU   A CD2 
3734 N  N   . PRO   A 480 ? 0.58616 0.39183 0.45385 -0.02959 -0.02200 -0.01431 557 PRO   A N   
3735 C  CA  . PRO   A 480 ? 0.61155 0.39768 0.46237 -0.03141 -0.02137 -0.01597 557 PRO   A CA  
3736 C  C   . PRO   A 480 ? 0.63551 0.41656 0.48373 -0.02609 -0.01700 -0.01847 557 PRO   A C   
3737 O  O   . PRO   A 480 ? 0.62749 0.41876 0.48253 -0.02556 -0.01680 -0.01859 557 PRO   A O   
3738 C  CB  . PRO   A 480 ? 0.57959 0.36462 0.42316 -0.04087 -0.02652 -0.01438 557 PRO   A CB  
3739 C  CG  . PRO   A 480 ? 0.60522 0.40762 0.46142 -0.04382 -0.02987 -0.01141 557 PRO   A CG  
3740 C  CD  . PRO   A 480 ? 0.59684 0.41321 0.46828 -0.03653 -0.02662 -0.01186 557 PRO   A CD  
3741 N  N   . PRO   A 481 ? 0.67406 0.43943 0.51254 -0.02187 -0.01320 -0.02035 558 PRO   A N   
3742 C  CA  . PRO   A 481 ? 0.59424 0.35503 0.43059 -0.01623 -0.00846 -0.02256 558 PRO   A CA  
3743 C  C   . PRO   A 481 ? 0.62937 0.38959 0.46036 -0.02050 -0.00983 -0.02334 558 PRO   A C   
3744 O  O   . PRO   A 481 ? 0.62817 0.39552 0.46570 -0.01646 -0.00723 -0.02422 558 PRO   A O   
3745 C  CB  . PRO   A 481 ? 0.59122 0.33184 0.41390 -0.01303 -0.00493 -0.02403 558 PRO   A CB  
3746 C  CG  . PRO   A 481 ? 0.65934 0.39922 0.48365 -0.01371 -0.00669 -0.02242 558 PRO   A CG  
3747 C  CD  . PRO   A 481 ? 0.65418 0.40683 0.48504 -0.02099 -0.01255 -0.02026 558 PRO   A CD  
3748 N  N   . GLN   A 482 ? 0.65754 0.40934 0.47658 -0.02870 -0.01389 -0.02288 559 GLN   A N   
3749 C  CA  . GLN   A 482 ? 0.65154 0.40207 0.46486 -0.03264 -0.01508 -0.02348 559 GLN   A CA  
3750 C  C   . GLN   A 482 ? 0.60442 0.37519 0.43183 -0.03499 -0.01816 -0.02147 559 GLN   A C   
3751 O  O   . GLN   A 482 ? 0.59075 0.36454 0.41825 -0.03552 -0.01791 -0.02201 559 GLN   A O   
3752 C  CB  . GLN   A 482 ? 0.68822 0.42275 0.48332 -0.04118 -0.01867 -0.02338 559 GLN   A CB  
3753 C  CG  . GLN   A 482 ? 0.70058 0.44209 0.49768 -0.04939 -0.02496 -0.02026 559 GLN   A CG  
3754 C  CD  . GLN   A 482 ? 0.68999 0.42057 0.47157 -0.05919 -0.02953 -0.01944 559 GLN   A CD  
3755 O  OE1 . GLN   A 482 ? 0.77357 0.48644 0.53907 -0.06023 -0.02792 -0.02162 559 GLN   A OE1 
3756 N  NE2 . GLN   A 482 ? 0.67258 0.41366 0.45863 -0.06664 -0.03528 -0.01604 559 GLN   A NE2 
3757 N  N   . ILE   A 483 ? 0.61532 0.39955 0.45421 -0.03630 -0.02087 -0.01910 560 ILE   A N   
3758 C  CA  . ILE   A 483 ? 0.57627 0.38008 0.42983 -0.03672 -0.02261 -0.01725 560 ILE   A CA  
3759 C  C   . ILE   A 483 ? 0.60926 0.42057 0.47269 -0.02874 -0.01804 -0.01887 560 ILE   A C   
3760 O  O   . ILE   A 483 ? 0.56561 0.38210 0.43142 -0.02864 -0.01772 -0.01919 560 ILE   A O   
3761 C  CB  . ILE   A 483 ? 0.55540 0.37122 0.41912 -0.03853 -0.02540 -0.01458 560 ILE   A CB  
3762 C  CG1 . ILE   A 483 ? 0.61564 0.42430 0.46972 -0.04671 -0.03005 -0.01265 560 ILE   A CG1 
3763 C  CG2 . ILE   A 483 ? 0.56928 0.40449 0.44753 -0.03842 -0.02659 -0.01268 560 ILE   A CG2 
3764 C  CD1 . ILE   A 483 ? 0.54301 0.35665 0.39501 -0.05466 -0.03477 -0.01015 560 ILE   A CD1 
3765 N  N   . VAL   A 484 ? 0.56751 0.37959 0.43676 -0.02215 -0.01461 -0.01967 561 VAL   A N   
3766 C  CA  . VAL   A 484 ? 0.57339 0.39416 0.45303 -0.01513 -0.01074 -0.02066 561 VAL   A CA  
3767 C  C   . VAL   A 484 ? 0.56632 0.37710 0.43790 -0.01222 -0.00717 -0.02299 561 VAL   A C   
3768 O  O   . VAL   A 484 ? 0.62076 0.43922 0.49974 -0.00810 -0.00473 -0.02361 561 VAL   A O   
3769 C  CB  . VAL   A 484 ? 0.57452 0.39913 0.46258 -0.00907 -0.00816 -0.02048 561 VAL   A CB  
3770 C  CG1 . VAL   A 484 ? 0.58630 0.40493 0.47001 -0.01176 -0.01024 -0.01943 561 VAL   A CG1 
3771 C  CG2 . VAL   A 484 ? 0.56445 0.38194 0.45064 -0.00190 -0.00286 -0.02231 561 VAL   A CG2 
3772 N  N   . ALA   A 485 ? 0.60840 0.40178 0.46439 -0.01444 -0.00672 -0.02427 562 ALA   A N   
3773 C  CA  . ALA   A 485 ? 0.60474 0.38825 0.45197 -0.01229 -0.00335 -0.02645 562 ALA   A CA  
3774 C  C   . ALA   A 485 ? 0.58017 0.36974 0.42754 -0.01691 -0.00597 -0.02610 562 ALA   A C   
3775 O  O   . ALA   A 485 ? 0.62948 0.41934 0.47705 -0.01383 -0.00313 -0.02743 562 ALA   A O   
3776 C  CB  . ALA   A 485 ? 0.58626 0.34823 0.41523 -0.01383 -0.00214 -0.02795 562 ALA   A CB  
3777 N  N   . GLY   A 486 ? 0.59532 0.39047 0.44317 -0.02419 -0.01135 -0.02400 563 GLY   A N   
3778 C  CA  . GLY   A 486 ? 0.54290 0.34587 0.39267 -0.02862 -0.01424 -0.02291 563 GLY   A CA  
3779 C  C   . GLY   A 486 ? 0.57381 0.39487 0.43985 -0.02481 -0.01343 -0.02209 563 GLY   A C   
3780 O  O   . GLY   A 486 ? 0.61810 0.44603 0.48637 -0.02780 -0.01547 -0.02108 563 GLY   A O   
3781 N  N   . GLY   A 487 ? 0.52750 0.35634 0.40467 -0.01860 -0.01071 -0.02229 564 GLY   A N   
3782 C  CA  . GLY   A 487 ? 0.51980 0.36386 0.41087 -0.01480 -0.00955 -0.02180 564 GLY   A CA  
3783 C  C   . GLY   A 487 ? 0.56168 0.42048 0.46320 -0.01798 -0.01324 -0.01905 564 GLY   A C   
3784 O  O   . GLY   A 487 ? 0.61414 0.47282 0.51410 -0.02234 -0.01642 -0.01736 564 GLY   A O   
3785 N  N   . PRO   A 488 ? 0.54758 0.41910 0.45970 -0.01574 -0.01269 -0.01845 565 PRO   A N   
3786 C  CA  . PRO   A 488 ? 0.54196 0.42802 0.46532 -0.01713 -0.01507 -0.01589 565 PRO   A CA  
3787 C  C   . PRO   A 488 ? 0.48834 0.37743 0.40935 -0.02429 -0.01971 -0.01313 565 PRO   A C   
3788 O  O   . PRO   A 488 ? 0.46118 0.35840 0.38826 -0.02630 -0.02185 -0.01078 565 PRO   A O   
3789 C  CB  . PRO   A 488 ? 0.49887 0.39506 0.43163 -0.01296 -0.01295 -0.01621 565 PRO   A CB  
3790 C  CG  . PRO   A 488 ? 0.52194 0.40985 0.45020 -0.00846 -0.00907 -0.01896 565 PRO   A CG  
3791 C  CD  . PRO   A 488 ? 0.55741 0.43011 0.47163 -0.01135 -0.00942 -0.02011 565 PRO   A CD  
3792 N  N   . SER   A 489 ? 0.53127 0.41489 0.44411 -0.02829 -0.02136 -0.01303 566 SER   A N   
3793 C  CA  . SER   A 489 ? 0.50576 0.39243 0.41616 -0.03568 -0.02618 -0.00984 566 SER   A CA  
3794 C  C   . SER   A 489 ? 0.49374 0.37479 0.39867 -0.03995 -0.02873 -0.00868 566 SER   A C   
3795 O  O   . SER   A 489 ? 0.51752 0.40768 0.42794 -0.04358 -0.03181 -0.00542 566 SER   A O   
3796 C  CB  . SER   A 489 ? 0.52808 0.40707 0.42822 -0.03971 -0.02761 -0.01012 566 SER   A CB  
3797 O  OG  . SER   A 489 ? 0.63814 0.52601 0.54519 -0.03741 -0.02664 -0.00982 566 SER   A OG  
3798 N  N   . PHE   A 490 ? 0.46846 0.33445 0.36255 -0.03942 -0.02730 -0.01116 567 PHE   A N   
3799 C  CA  . PHE   A 490 ? 0.50998 0.36928 0.39776 -0.04367 -0.02978 -0.01013 567 PHE   A CA  
3800 C  C   . PHE   A 490 ? 0.46266 0.33004 0.36061 -0.04025 -0.02881 -0.00946 567 PHE   A C   
3801 O  O   . PHE   A 490 ? 0.45202 0.32254 0.35090 -0.04450 -0.03188 -0.00700 567 PHE   A O   
3802 C  CB  . PHE   A 490 ? 0.53001 0.36959 0.40228 -0.04386 -0.02825 -0.01294 567 PHE   A CB  
3803 C  CG  . PHE   A 490 ? 0.49158 0.32116 0.35055 -0.05040 -0.03097 -0.01269 567 PHE   A CG  
3804 C  CD1 . PHE   A 490 ? 0.51686 0.34305 0.37203 -0.04896 -0.02914 -0.01438 567 PHE   A CD1 
3805 C  CD2 . PHE   A 490 ? 0.55355 0.37788 0.40396 -0.05856 -0.03570 -0.01043 567 PHE   A CD2 
3806 C  CE1 . PHE   A 490 ? 0.52962 0.34636 0.37186 -0.05554 -0.03191 -0.01400 567 PHE   A CE1 
3807 C  CE2 . PHE   A 490 ? 0.56644 0.38144 0.40394 -0.06537 -0.03866 -0.00991 567 PHE   A CE2 
3808 C  CZ  . PHE   A 490 ? 0.52840 0.33945 0.36170 -0.06382 -0.03674 -0.01176 567 PHE   A CZ  
3809 N  N   . ILE   A 491 ? 0.48610 0.35712 0.39165 -0.03290 -0.02471 -0.01140 568 ILE   A N   
3810 C  CA  . ILE   A 491 ? 0.47019 0.34825 0.38471 -0.02983 -0.02384 -0.01079 568 ILE   A CA  
3811 C  C   . ILE   A 491 ? 0.45538 0.34880 0.38017 -0.03245 -0.02640 -0.00750 568 ILE   A C   
3812 O  O   . ILE   A 491 ? 0.43623 0.33264 0.36284 -0.03511 -0.02841 -0.00555 568 ILE   A O   
3813 C  CB  . ILE   A 491 ? 0.52689 0.40661 0.44767 -0.02192 -0.01924 -0.01310 568 ILE   A CB  
3814 C  CG1 . ILE   A 491 ? 0.49055 0.35503 0.40123 -0.01906 -0.01638 -0.01581 568 ILE   A CG1 
3815 C  CG2 . ILE   A 491 ? 0.49238 0.38008 0.42260 -0.01911 -0.01860 -0.01225 568 ILE   A CG2 
3816 C  CD1 . ILE   A 491 ? 0.50820 0.37449 0.42429 -0.01179 -0.01191 -0.01770 568 ILE   A CD1 
3817 N  N   . ILE   A 492 ? 0.45805 0.36115 0.38932 -0.03178 -0.02628 -0.00665 569 ILE   A N   
3818 C  CA  . ILE   A 492 ? 0.45434 0.37195 0.39525 -0.03380 -0.02825 -0.00323 569 ILE   A CA  
3819 C  C   . ILE   A 492 ? 0.46640 0.38374 0.40238 -0.04156 -0.03285 0.00005  569 ILE   A C   
3820 O  O   . ILE   A 492 ? 0.44471 0.37010 0.38607 -0.04384 -0.03461 0.00294  569 ILE   A O   
3821 C  CB  . ILE   A 492 ? 0.42609 0.35281 0.37394 -0.03137 -0.02706 -0.00289 569 ILE   A CB  
3822 C  CG1 . ILE   A 492 ? 0.45386 0.38385 0.40880 -0.02413 -0.02289 -0.00529 569 ILE   A CG1 
3823 C  CG2 . ILE   A 492 ? 0.44896 0.38912 0.40482 -0.03420 -0.02933 0.00120  569 ILE   A CG2 
3824 C  CD1 . ILE   A 492 ? 0.44856 0.38418 0.41052 -0.02175 -0.02190 -0.00479 569 ILE   A CD1 
3825 N  N   . GLN   A 493 ? 0.45327 0.36147 0.37873 -0.04603 -0.03493 -0.00011 570 GLN   A N   
3826 C  CA  . GLN   A 493 ? 0.47103 0.37794 0.39064 -0.05416 -0.03971 0.00319  570 GLN   A CA  
3827 C  C   . GLN   A 493 ? 0.49641 0.39823 0.41269 -0.05608 -0.04076 0.00351  570 GLN   A C   
3828 O  O   . GLN   A 493 ? 0.51148 0.42003 0.43040 -0.06094 -0.04399 0.00720  570 GLN   A O   
3829 C  CB  . GLN   A 493 ? 0.52349 0.41798 0.42966 -0.05884 -0.04165 0.00237  570 GLN   A CB  
3830 C  CG  . GLN   A 493 ? 0.60125 0.49142 0.49890 -0.06791 -0.04684 0.00555  570 GLN   A CG  
3831 C  CD  . GLN   A 493 ? 0.59215 0.46666 0.47372 -0.07294 -0.04869 0.00427  570 GLN   A CD  
3832 O  OE1 . GLN   A 493 ? 0.60603 0.48335 0.48508 -0.07863 -0.05218 0.00700  570 GLN   A OE1 
3833 N  NE2 . GLN   A 493 ? 0.52429 0.38198 0.39454 -0.07097 -0.04634 0.00035  570 GLN   A NE2 
3834 N  N   . PHE   A 494 ? 0.46569 0.35602 0.37649 -0.05220 -0.03799 -0.00005 571 PHE   A N   
3835 C  CA  . PHE   A 494 ? 0.50847 0.39284 0.41538 -0.05391 -0.03896 0.00020  571 PHE   A CA  
3836 C  C   . PHE   A 494 ? 0.49278 0.39063 0.41223 -0.05171 -0.03848 0.00212  571 PHE   A C   
3837 O  O   . PHE   A 494 ? 0.45462 0.35420 0.37375 -0.05594 -0.04110 0.00459  571 PHE   A O   
3838 C  CB  . PHE   A 494 ? 0.50448 0.37381 0.40324 -0.04953 -0.03571 -0.00376 571 PHE   A CB  
3839 C  CG  . PHE   A 494 ? 0.57624 0.44121 0.47381 -0.04912 -0.03570 -0.00375 571 PHE   A CG  
3840 C  CD1 . PHE   A 494 ? 0.57525 0.42867 0.46120 -0.05500 -0.03864 -0.00297 571 PHE   A CD1 
3841 C  CD2 . PHE   A 494 ? 0.50470 0.37662 0.41221 -0.04317 -0.03290 -0.00440 571 PHE   A CD2 
3842 C  CE1 . PHE   A 494 ? 0.53694 0.38620 0.42170 -0.05464 -0.03867 -0.00286 571 PHE   A CE1 
3843 C  CE2 . PHE   A 494 ? 0.51028 0.37831 0.41667 -0.04296 -0.03305 -0.00419 571 PHE   A CE2 
3844 C  CZ  . PHE   A 494 ? 0.55185 0.40858 0.44702 -0.04853 -0.03587 -0.00344 571 PHE   A CZ  
3845 N  N   . LEU   A 495 ? 0.47378 0.38104 0.40384 -0.04542 -0.03519 0.00111  572 LEU   A N   
3846 C  CA  . LEU   A 495 ? 0.51381 0.43299 0.45496 -0.04307 -0.03432 0.00268  572 LEU   A CA  
3847 C  C   . LEU   A 495 ? 0.47188 0.40370 0.41910 -0.04768 -0.03719 0.00714  572 LEU   A C   
3848 O  O   . LEU   A 495 ? 0.48468 0.42304 0.43683 -0.04872 -0.03787 0.00932  572 LEU   A O   
3849 C  CB  . LEU   A 495 ? 0.46743 0.39275 0.41728 -0.03575 -0.03025 0.00061  572 LEU   A CB  
3850 C  CG  . LEU   A 495 ? 0.46394 0.38036 0.41125 -0.03020 -0.02695 -0.00304 572 LEU   A CG  
3851 C  CD1 . LEU   A 495 ? 0.40808 0.33287 0.36482 -0.02415 -0.02365 -0.00422 572 LEU   A CD1 
3852 C  CD2 . LEU   A 495 ? 0.37873 0.29047 0.32428 -0.03013 -0.02712 -0.00310 572 LEU   A CD2 
3853 N  N   . LYS   A 496 ? 0.45078 0.38665 0.39809 -0.05030 -0.03876 0.00882  573 LYS   A N   
3854 C  CA  . LYS   A 496 ? 0.46761 0.41661 0.42164 -0.05427 -0.04130 0.01367  573 LYS   A CA  
3855 C  C   . LYS   A 496 ? 0.48318 0.42905 0.43059 -0.06226 -0.04584 0.01684  573 LYS   A C   
3856 O  O   . LYS   A 496 ? 0.48872 0.44344 0.44176 -0.06444 -0.04710 0.02026  573 LYS   A O   
3857 C  CB  . LYS   A 496 ? 0.47874 0.43333 0.43520 -0.05454 -0.04170 0.01488  573 LYS   A CB  
3858 C  CG  . LYS   A 496 ? 0.48895 0.44633 0.45124 -0.04734 -0.03757 0.01202  573 LYS   A CG  
3859 C  CD  . LYS   A 496 ? 0.48927 0.44649 0.44954 -0.04818 -0.03823 0.01212  573 LYS   A CD  
3860 C  CE  . LYS   A 496 ? 0.52341 0.49128 0.48765 -0.05330 -0.04164 0.01745  573 LYS   A CE  
3861 N  NZ  . LYS   A 496 ? 0.54479 0.51699 0.51160 -0.05202 -0.04125 0.01794  573 LYS   A NZ  
3862 N  N   . MET   A 497 ? 0.49706 0.43006 0.43201 -0.06689 -0.04831 0.01584  574 MET   A N   
3863 C  CA  . MET   A 497 ? 0.53998 0.46959 0.46757 -0.07548 -0.05318 0.01919  574 MET   A CA  
3864 C  C   . MET   A 497 ? 0.53925 0.46056 0.46153 -0.07671 -0.05359 0.01828  574 MET   A C   
3865 O  O   . MET   A 497 ? 0.55528 0.47776 0.47492 -0.08335 -0.05738 0.02181  574 MET   A O   
3866 C  CB  . MET   A 497 ? 0.53466 0.45252 0.44950 -0.08062 -0.05585 0.01856  574 MET   A CB  
3867 C  CG  . MET   A 497 ? 0.57723 0.50329 0.49634 -0.08097 -0.05645 0.02029  574 MET   A CG  
3868 S  SD  . MET   A 497 ? 0.88413 0.79546 0.78653 -0.08849 -0.06029 0.02001  574 MET   A SD  
3869 C  CE  . MET   A 497 ? 0.71233 0.63011 0.62007 -0.08460 -0.05838 0.01933  574 MET   A CE  
3870 N  N   . GLN   A 498 ? 0.57982 0.49315 0.50067 -0.07064 -0.04993 0.01398  575 GLN   A N   
3871 C  CA  . GLN   A 498 ? 0.54770 0.45193 0.46280 -0.07153 -0.05026 0.01305  575 GLN   A CA  
3872 C  C   . GLN   A 498 ? 0.56184 0.47424 0.48737 -0.06589 -0.04728 0.01260  575 GLN   A C   
3873 O  O   . GLN   A 498 ? 0.57653 0.48071 0.49827 -0.06424 -0.04632 0.01079  575 GLN   A O   
3874 C  CB  . GLN   A 498 ? 0.54986 0.43511 0.45199 -0.07001 -0.04887 0.00879  575 GLN   A CB  
3875 C  CG  . GLN   A 498 ? 0.55055 0.42490 0.43972 -0.07622 -0.05185 0.00898  575 GLN   A CG  
3876 C  CD  . GLN   A 498 ? 0.61696 0.47058 0.49099 -0.07636 -0.05108 0.00564  575 GLN   A CD  
3877 O  OE1 . GLN   A 498 ? 0.66528 0.51331 0.53808 -0.07388 -0.04969 0.00442  575 GLN   A OE1 
3878 N  NE2 . GLN   A 498 ? 0.59042 0.43216 0.45256 -0.07909 -0.05180 0.00423  575 GLN   A NE2 
3879 N  N   . GLY   A 499 ? 0.53235 0.46031 0.47049 -0.06291 -0.04577 0.01431  576 GLY   A N   
3880 C  CA  . GLY   A 499 ? 0.46806 0.40445 0.41566 -0.05849 -0.04326 0.01441  576 GLY   A CA  
3881 C  C   . GLY   A 499 ? 0.46100 0.41056 0.41563 -0.06242 -0.04527 0.01928  576 GLY   A C   
3882 O  O   . GLY   A 499 ? 0.48754 0.43927 0.43947 -0.06891 -0.04895 0.02277  576 GLY   A O   
3883 N  N   . PRO   A 500 ? 0.44371 0.40218 0.40717 -0.05876 -0.04290 0.01984  577 PRO   A N   
3884 C  CA  . PRO   A 500 ? 0.45124 0.42267 0.42176 -0.06192 -0.04416 0.02465  577 PRO   A CA  
3885 C  C   . PRO   A 500 ? 0.45065 0.43609 0.43034 -0.06090 -0.04333 0.02766  577 PRO   A C   
3886 O  O   . PRO   A 500 ? 0.42688 0.42395 0.41323 -0.06282 -0.04380 0.03200  577 PRO   A O   
3887 C  CB  . PRO   A 500 ? 0.42408 0.39782 0.39926 -0.05788 -0.04143 0.02357  577 PRO   A CB  
3888 C  CG  . PRO   A 500 ? 0.47404 0.44043 0.44817 -0.05143 -0.03819 0.01865  577 PRO   A CG  
3889 C  CD  . PRO   A 500 ? 0.41895 0.37327 0.38385 -0.05271 -0.03953 0.01627  577 PRO   A CD  
3890 N  N   . TYR   A 501 ? 0.39537 0.38026 0.37571 -0.05787 -0.04199 0.02581  578 TYR   A N   
3891 C  CA  . TYR   A 501 ? 0.45916 0.45688 0.44814 -0.05648 -0.04104 0.02870  578 TYR   A CA  
3892 C  C   . TYR   A 501 ? 0.45675 0.45438 0.44193 -0.06182 -0.04467 0.03121  578 TYR   A C   
3893 O  O   . TYR   A 501 ? 0.46098 0.46680 0.45178 -0.06039 -0.04403 0.03297  578 TYR   A O   
3894 C  CB  . TYR   A 501 ? 0.44575 0.44444 0.43945 -0.04880 -0.03661 0.02513  578 TYR   A CB  
3895 C  CG  . TYR   A 501 ? 0.42796 0.42475 0.42357 -0.04438 -0.03361 0.02252  578 TYR   A CG  
3896 C  CD1 . TYR   A 501 ? 0.40052 0.40632 0.40247 -0.04397 -0.03244 0.02517  578 TYR   A CD1 
3897 C  CD2 . TYR   A 501 ? 0.41881 0.40481 0.40964 -0.04091 -0.03204 0.01775  578 TYR   A CD2 
3898 C  CE1 . TYR   A 501 ? 0.41907 0.42273 0.42204 -0.04047 -0.02997 0.02293  578 TYR   A CE1 
3899 C  CE2 . TYR   A 501 ? 0.39665 0.38125 0.38924 -0.03737 -0.02973 0.01584  578 TYR   A CE2 
3900 C  CZ  . TYR   A 501 ? 0.40719 0.40034 0.40550 -0.03739 -0.02886 0.01835  578 TYR   A CZ  
3901 O  OH  . TYR   A 501 ? 0.50830 0.49983 0.50776 -0.03434 -0.02679 0.01659  578 TYR   A OH  
3902 N  N   . ARG   A 502 ? 0.47442 0.46232 0.44955 -0.06815 -0.04857 0.03147  579 ARG   A N   
3903 C  CA  . ARG   A 502 ? 0.48480 0.47040 0.45416 -0.07405 -0.05244 0.03358  579 ARG   A CA  
3904 C  C   . ARG   A 502 ? 0.47442 0.47632 0.45299 -0.07661 -0.05400 0.03977  579 ARG   A C   
3905 O  O   . ARG   A 502 ? 0.46104 0.46572 0.43991 -0.07793 -0.05529 0.04125  579 ARG   A O   
3906 C  CB  . ARG   A 502 ? 0.44024 0.41385 0.39749 -0.08132 -0.05659 0.03384  579 ARG   A CB  
3907 C  CG  . ARG   A 502 ? 0.51993 0.48826 0.46847 -0.08842 -0.06103 0.03572  579 ARG   A CG  
3908 C  CD  . ARG   A 502 ? 0.52533 0.47956 0.46035 -0.09539 -0.06478 0.03544  579 ARG   A CD  
3909 N  NE  . ARG   A 502 ? 0.45797 0.41779 0.39624 -0.09836 -0.06619 0.03865  579 ARG   A NE  
3910 C  CZ  . ARG   A 502 ? 0.52650 0.47730 0.45486 -0.10537 -0.06999 0.03986  579 ARG   A CZ  
3911 N  NH1 . ARG   A 502 ? 0.47519 0.40966 0.38887 -0.10995 -0.07255 0.03783  579 ARG   A NH1 
3912 N  NH2 . ARG   A 502 ? 0.49461 0.45245 0.42730 -0.10796 -0.07117 0.04324  579 ARG   A NH2 
3913 N  N   . ALA   A 503 ? 0.45860 0.47175 0.44511 -0.07697 -0.05362 0.04362  580 ALA   A N   
3914 C  CA  . ALA   A 503 ? 0.47902 0.50835 0.47467 -0.07954 -0.05502 0.05034  580 ALA   A CA  
3915 C  C   . ALA   A 503 ? 0.47431 0.51460 0.48071 -0.07259 -0.05093 0.05084  580 ALA   A C   
3916 O  O   . ALA   A 503 ? 0.44524 0.49758 0.45832 -0.07431 -0.05215 0.05620  580 ALA   A O   
3917 C  CB  . ALA   A 503 ? 0.45084 0.48823 0.45105 -0.08211 -0.05561 0.05443  580 ALA   A CB  
3918 N  N   . MET   A 504 ? 0.42135 0.45780 0.42946 -0.06497 -0.04625 0.04572  581 MET   A N   
3919 C  CA  . MET   A 504 ? 0.48294 0.52924 0.50074 -0.05844 -0.04221 0.04628  581 MET   A CA  
3920 C  C   . MET   A 504 ? 0.49917 0.53867 0.51423 -0.05441 -0.04059 0.04182  581 MET   A C   
3921 O  O   . MET   A 504 ? 0.57772 0.62322 0.59969 -0.04845 -0.03689 0.04135  581 MET   A O   
3922 C  CB  . MET   A 504 ? 0.44416 0.49494 0.46826 -0.05272 -0.03764 0.04524  581 MET   A CB  
3923 C  CG  . MET   A 504 ? 0.46585 0.50471 0.48454 -0.04908 -0.03543 0.03892  581 MET   A CG  
3924 S  SD  . MET   A 504 ? 0.52570 0.56950 0.54997 -0.04509 -0.03155 0.03890  581 MET   A SD  
3925 C  CE  . MET   A 504 ? 0.53840 0.58222 0.55910 -0.05276 -0.03571 0.04252  581 MET   A CE  
3926 N  N   . VAL   A 505 ? 0.50664 0.53378 0.51160 -0.05753 -0.04312 0.03878  582 VAL   A N   
3927 C  CA  . VAL   A 505 ? 0.51848 0.53938 0.52073 -0.05385 -0.04150 0.03478  582 VAL   A CA  
3928 C  C   . VAL   A 505 ? 0.55054 0.56887 0.54719 -0.05928 -0.04545 0.03658  582 VAL   A C   
3929 O  O   . VAL   A 505 ? 0.54538 0.56311 0.53749 -0.06653 -0.04987 0.03996  582 VAL   A O   
3930 C  CB  . VAL   A 505 ? 0.52166 0.52855 0.51658 -0.05077 -0.03958 0.02842  582 VAL   A CB  
3931 C  CG1 . VAL   A 505 ? 0.47055 0.47958 0.47028 -0.04619 -0.03622 0.02689  582 VAL   A CG1 
3932 C  CG2 . VAL   A 505 ? 0.50490 0.49939 0.48801 -0.05694 -0.04332 0.02747  582 VAL   A CG2 
3933 C  C1  . A1ATZ B .   ? 0.66327 0.62816 0.65747 0.02772  0.01676  -0.01273 601 A1ATZ A C1  
3934 C  C2  . A1ATZ B .   ? 0.65807 0.61737 0.64731 0.02720  0.01709  -0.01206 601 A1ATZ A C2  
3935 C  C3  . A1ATZ B .   ? 0.53137 0.49164 0.51957 0.02213  0.01587  -0.01207 601 A1ATZ A C3  
3936 O  O1  . A1ATZ B .   ? 0.69537 0.66084 0.69109 0.02926  0.01707  -0.01288 601 A1ATZ A O1  
3937 O  O2  . A1ATZ B .   ? 0.58761 0.55620 0.58385 0.02638  0.01632  -0.01303 601 A1ATZ A O2  
3938 O  O3  . A1ATZ B .   ? 0.47488 0.43920 0.46418 0.01402  0.01304  -0.01008 601 A1ATZ A O3  
3939 C  C11 . A1ATZ B .   ? 0.75226 0.71556 0.74492 0.03054  0.01705  -0.01070 601 A1ATZ A C11 
3940 C  C12 . A1ATZ B .   ? 0.77584 0.73911 0.76820 0.03175  0.01693  -0.00930 601 A1ATZ A C12 
3941 C  C13 . A1ATZ B .   ? 0.85056 0.80910 0.83893 0.03180  0.01734  -0.00845 601 A1ATZ A C13 
3942 C  C14 . A1ATZ B .   ? 0.74843 0.70190 0.73254 0.03023  0.01773  -0.00909 601 A1ATZ A C14 
3943 C  C15 . A1ATZ B .   ? 0.73153 0.68541 0.71596 0.02860  0.01761  -0.01034 601 A1ATZ A C15 
3944 C  C16 . A1ATZ B .   ? 0.65416 0.59927 0.62984 0.02468  0.01727  -0.00998 601 A1ATZ A C16 
3945 C  C17 . A1ATZ B .   ? 0.54039 0.48146 0.51177 0.02134  0.01668  -0.01015 601 A1ATZ A C17 
3946 C  C18 . A1ATZ B .   ? 0.50381 0.44562 0.47608 0.02055  0.01650  -0.01081 601 A1ATZ A C18 
3947 C  C19 . A1ATZ B .   ? 0.44965 0.38796 0.41779 0.01694  0.01555  -0.01059 601 A1ATZ A C19 
3948 C  C20 . A1ATZ B .   ? 0.48053 0.41990 0.44968 0.01599  0.01515  -0.01104 601 A1ATZ A C20 
3949 C  C21 . A1ATZ B .   ? 0.53654 0.47583 0.50728 0.01904  0.01633  -0.01193 601 A1ATZ A C21 
3950 C  C22 . A1ATZ B .   ? 0.50883 0.44908 0.48038 0.01797  0.01587  -0.01232 601 A1ATZ A C22 
3951 C  C23 . A1ATZ B .   ? 0.48872 0.43034 0.45981 0.01383  0.01406  -0.01158 601 A1ATZ A C23 
3952 C  C24 . A1ATZ B .   ? 0.44449 0.38691 0.41455 0.01079  0.01284  -0.01037 601 A1ATZ A C24 
3953 C  C25 . A1ATZ B .   ? 0.46015 0.40131 0.42911 0.01187  0.01346  -0.01022 601 A1ATZ A C25 
3954 C  C26 . A1ATZ B .   ? 0.48909 0.42308 0.45205 0.01389  0.01474  -0.00968 601 A1ATZ A C26 
3955 C  C27 . A1ATZ B .   ? 0.48470 0.41761 0.44663 0.01482  0.01508  -0.00916 601 A1ATZ A C27 
3956 C  C28 . A1ATZ B .   ? 0.58157 0.51813 0.54782 0.01861  0.01606  -0.00939 601 A1ATZ A C28 
3957 C  C10 . A1ATZ B .   ? 0.73927 0.69825 0.72824 0.02893  0.01733  -0.01112 601 A1ATZ A C10 
3958 C  C4  . A1ATZ B .   ? 0.49496 0.45575 0.48456 0.02251  0.01587  -0.01263 601 A1ATZ A C4  
3959 C  C5  . A1ATZ B .   ? 0.44721 0.40884 0.43694 0.02000  0.01503  -0.01233 601 A1ATZ A C5  
3960 C  C6  . A1ATZ B .   ? 0.46013 0.42262 0.44897 0.01707  0.01420  -0.01122 601 A1ATZ A C6  
3961 C  C7  . A1ATZ B .   ? 0.40051 0.36592 0.38902 0.01168  0.01250  -0.00873 601 A1ATZ A C7  
3962 C  C8  . A1ATZ B .   ? 0.42608 0.38810 0.41356 0.01672  0.01436  -0.01074 601 A1ATZ A C8  
3963 C  C9  . A1ATZ B .   ? 0.50271 0.46333 0.48960 0.01920  0.01518  -0.01125 601 A1ATZ A C9  
3964 N  N1  . A1ATZ B .   ? 0.58552 0.54525 0.57369 0.02438  0.01642  -0.01196 601 A1ATZ A N1  
3965 N  N2  . A1ATZ B .   ? 0.44274 0.40646 0.42993 0.01339  0.01339  -0.00932 601 A1ATZ A N2  
3966 O  O4  . A1ATZ B .   ? 0.40460 0.37257 0.39381 0.00855  0.01134  -0.00700 601 A1ATZ A O4  
3967 O  O5  . A1ATZ B .   ? 0.68879 0.63820 0.66902 0.02633  0.01752  -0.01065 601 A1ATZ A O5  
3968 CL CL1 . A1ATZ B .   ? 0.91167 0.84703 0.87650 0.01941  0.01617  -0.00843 601 A1ATZ A CL1 
3989 K  K   . K     C .   ? 0.42843 0.46637 0.47667 0.00771  0.01016  0.01800  602 K     A K   
3990 O  O   . HOH   D .   ? 0.40779 0.33267 0.41377 0.03552  0.00307  -0.00157 701 HOH   A O   
3991 O  O   . HOH   D .   ? 0.43176 0.44032 0.43196 0.02643  -0.04379 0.12419  702 HOH   A O   
3992 O  O   . HOH   D .   ? 0.43309 0.38546 0.41547 0.01320  0.01194  -0.01291 703 HOH   A O   
3993 O  O   . HOH   D .   ? 0.36195 0.37291 0.39134 0.01075  0.00066  0.00125  704 HOH   A O   
3994 O  O   . HOH   D .   ? 0.51598 0.37124 0.39104 -0.02593 0.00634  -0.01306 705 HOH   A O   
3995 O  O   . HOH   D .   ? 0.48337 0.44583 0.45774 0.02292  0.00574  0.00803  706 HOH   A O   
3996 O  O   . HOH   D .   ? 0.48131 0.42454 0.39133 -0.01313 0.00142  0.00641  707 HOH   A O   
3997 O  O   . HOH   D .   ? 0.56051 0.51794 0.49016 -0.09092 -0.03529 0.04184  708 HOH   A O   
3998 O  O   . HOH   D .   ? 0.52490 0.35754 0.40843 0.02209  0.02110  0.00466  709 HOH   A O   
3999 O  O   . HOH   D .   ? 0.68523 0.47142 0.48333 -0.04954 0.00556  -0.01500 710 HOH   A O   
4000 O  O   . HOH   D .   ? 0.50608 0.42027 0.40100 -0.09084 -0.03306 0.03123  711 HOH   A O   
4001 O  O   . HOH   D .   ? 0.48885 0.37549 0.39649 -0.00011 0.02329  -0.01764 712 HOH   A O   
4002 O  O   . HOH   D .   ? 0.42500 0.40876 0.43639 0.03667  0.02729  -0.00737 713 HOH   A O   
4003 O  O   . HOH   D .   ? 0.60859 0.38773 0.43089 -0.01491 0.01580  -0.00762 714 HOH   A O   
4004 O  O   . HOH   D .   ? 0.40685 0.42931 0.40990 -0.02463 0.00884  0.02678  715 HOH   A O   
4005 O  O   . HOH   D .   ? 0.44739 0.37397 0.35389 -0.01559 0.00170  0.02012  716 HOH   A O   
4006 O  O   . HOH   D .   ? 0.39138 0.38129 0.43985 0.04036  0.01071  0.00290  717 HOH   A O   
4007 O  O   . HOH   D .   ? 0.49764 0.41588 0.44377 0.03577  -0.00125 0.04783  718 HOH   A O   
4008 O  O   . HOH   D .   ? 0.35146 0.43455 0.44898 0.00446  -0.00927 0.05357  719 HOH   A O   
4009 O  O   . HOH   D .   ? 0.51736 0.35184 0.38488 -0.01186 0.01466  -0.01342 720 HOH   A O   
4010 O  O   . HOH   D .   ? 0.51416 0.40416 0.44638 0.02814  0.02184  -0.00337 721 HOH   A O   
4011 O  O   . HOH   D .   ? 0.49134 0.44091 0.41059 -0.00494 0.02087  -0.00277 722 HOH   A O   
4012 O  O   . HOH   D .   ? 0.42781 0.38086 0.38493 -0.04507 -0.02537 0.01492  723 HOH   A O   
4013 O  O   . HOH   D .   ? 0.41892 0.42919 0.40941 -0.01339 0.01954  0.01754  724 HOH   A O   
4014 O  O   . HOH   D .   ? 0.47684 0.46443 0.50513 0.02910  0.01119  -0.01339 725 HOH   A O   
4015 O  O   . HOH   D .   ? 0.39410 0.33706 0.39060 0.02911  0.01044  -0.01899 726 HOH   A O   
4016 O  O   . HOH   D .   ? 0.69792 0.60186 0.59323 -0.01820 -0.00029 0.02449  727 HOH   A O   
4017 O  O   . HOH   D .   ? 0.43456 0.43165 0.45840 0.01881  0.01194  -0.00605 728 HOH   A O   
4018 O  O   . HOH   D .   ? 0.52081 0.37015 0.40387 -0.00522 0.01047  0.00268  729 HOH   A O   
4019 O  O   . HOH   D .   ? 0.41258 0.39901 0.38492 -0.04542 -0.00844 0.02669  730 HOH   A O   
4020 O  O   . HOH   D .   ? 0.66253 0.64397 0.62251 0.01215  0.04171  -0.00444 731 HOH   A O   
4021 O  O   . HOH   D .   ? 0.42012 0.44568 0.42829 -0.04377 -0.01268 0.03758  732 HOH   A O   
4022 O  O   . HOH   D .   ? 0.44866 0.40032 0.37666 -0.00436 0.01449  0.00155  733 HOH   A O   
4023 O  O   . HOH   D .   ? 0.52817 0.39001 0.43121 0.02180  0.03279  -0.01828 734 HOH   A O   
4024 O  O   . HOH   D .   ? 0.61196 0.39824 0.43805 -0.02130 0.00962  -0.00050 735 HOH   A O   
4025 O  O   . HOH   D .   ? 0.55169 0.37071 0.42268 0.01757  0.02314  -0.00096 736 HOH   A O   
4026 O  O   . HOH   D .   ? 0.44489 0.39196 0.37117 -0.00585 0.00817  0.00733  737 HOH   A O   
4027 O  O   . HOH   D .   ? 0.56953 0.37459 0.39855 -0.03393 0.00814  -0.01350 738 HOH   A O   
4028 O  O   . HOH   D .   ? 0.41088 0.39150 0.43214 0.00971  -0.00593 -0.00217 739 HOH   A O   
4029 O  O   . HOH   D .   ? 0.45683 0.32429 0.35744 0.00696  0.02457  -0.01871 740 HOH   A O   
4030 O  O   . HOH   D .   ? 0.62073 0.51460 0.58393 0.04325  0.02596  -0.02200 741 HOH   A O   
4031 O  O   . HOH   D .   ? 0.38358 0.34422 0.37298 0.02621  0.02405  -0.01341 742 HOH   A O   
4032 O  O   . HOH   D .   ? 0.36712 0.34455 0.34594 -0.04373 -0.02512 0.02190  743 HOH   A O   
4033 O  O   . HOH   D .   ? 0.57576 0.42195 0.47443 0.03144  0.02437  0.00424  744 HOH   A O   
4034 O  O   . HOH   D .   ? 0.33412 0.34359 0.34751 0.01468  0.02513  0.00149  745 HOH   A O   
4035 O  O   . HOH   D .   ? 0.49767 0.42431 0.46238 0.04588  0.01638  0.01920  746 HOH   A O   
4036 O  O   . HOH   D .   ? 0.54666 0.37487 0.40931 -0.01537 0.01070  -0.00601 747 HOH   A O   
4037 O  O   . HOH   D .   ? 0.37607 0.38439 0.39599 -0.00493 -0.01166 0.00673  748 HOH   A O   
4038 O  O   . HOH   D .   ? 0.52772 0.37506 0.44499 0.01377  0.00533  -0.02261 749 HOH   A O   
4039 O  O   . HOH   D .   ? 0.38727 0.39155 0.40392 -0.02405 -0.02212 0.02346  750 HOH   A O   
4040 O  O   . HOH   D .   ? 0.47723 0.39789 0.43353 0.03464  0.03549  -0.01605 751 HOH   A O   
4041 O  O   . HOH   D .   ? 0.51664 0.36857 0.46536 0.04633  0.01996  -0.01267 752 HOH   A O   
4042 O  O   . HOH   D .   ? 0.41015 0.32610 0.40243 0.03335  0.00642  -0.00954 753 HOH   A O   
4043 O  O   . HOH   D .   ? 0.31553 0.31993 0.34273 0.02132  0.01138  -0.00355 754 HOH   A O   
4044 O  O   . HOH   D .   ? 0.66149 0.47352 0.50160 -0.03202 0.00154  0.00914  755 HOH   A O   
4045 O  O   . HOH   D .   ? 0.38868 0.37796 0.36509 -0.04993 -0.01522 0.02907  756 HOH   A O   
4046 O  O   . HOH   D .   ? 0.53034 0.38678 0.38687 -0.07152 -0.01686 0.01697  757 HOH   A O   
4047 O  O   . HOH   D .   ? 0.47937 0.44550 0.50161 0.01818  -0.00558 -0.00273 758 HOH   A O   
4048 O  O   . HOH   D .   ? 0.41590 0.34739 0.37740 0.01956  0.02380  -0.01664 759 HOH   A O   
4049 O  O   . HOH   D .   ? 0.39157 0.30736 0.32004 -0.03140 -0.00887 -0.00234 760 HOH   A O   
4050 O  O   . HOH   D .   ? 0.40584 0.36470 0.35198 0.00263  0.00332  -0.00210 761 HOH   A O   
4051 O  O   . HOH   D .   ? 0.53443 0.44550 0.43445 -0.10157 -0.06755 0.02766  762 HOH   A O   
4052 O  O   . HOH   D .   ? 0.40993 0.47211 0.46660 0.04460  -0.02759 0.11628  763 HOH   A O   
4053 O  O   . HOH   D .   ? 0.47803 0.36538 0.39964 0.02810  0.00658  0.02971  764 HOH   A O   
4054 O  O   . HOH   D .   ? 0.35096 0.39628 0.40227 0.00795  0.01332  0.02113  765 HOH   A O   
4055 O  O   . HOH   D .   ? 0.46346 0.43656 0.46767 0.00120  -0.00456 -0.00329 766 HOH   A O   
4056 O  O   . HOH   D .   ? 0.55750 0.49439 0.46786 -0.01738 0.00766  0.01524  767 HOH   A O   
4057 O  O   . HOH   D .   ? 0.42435 0.39653 0.42150 -0.01064 -0.01304 0.00404  768 HOH   A O   
4058 O  O   . HOH   D .   ? 0.56865 0.48361 0.57745 0.05250  0.01339  0.00379  769 HOH   A O   
4059 O  O   . HOH   D .   ? 0.42065 0.45164 0.41316 -0.00755 -0.05447 0.10146  770 HOH   A O   
4060 O  O   . HOH   D .   ? 0.46095 0.49910 0.51429 0.00879  0.00634  0.01898  771 HOH   A O   
4061 O  O   . HOH   D .   ? 0.32306 0.30814 0.33500 0.02586  0.01872  -0.00940 772 HOH   A O   
4062 O  O   . HOH   D .   ? 0.60527 0.38131 0.42141 -0.01753 0.01766  -0.01272 773 HOH   A O   
4063 O  O   . HOH   D .   ? 0.52820 0.42284 0.44577 0.01026  0.03048  -0.01797 774 HOH   A O   
4064 O  O   . HOH   D .   ? 0.43129 0.39784 0.46088 0.04961  0.02232  -0.00643 775 HOH   A O   
4065 O  O   . HOH   D .   ? 0.37348 0.43215 0.41157 -0.03283 -0.00526 0.04486  776 HOH   A O   
4066 O  O   . HOH   D .   ? 0.45120 0.42013 0.40748 -0.01056 0.01634  0.00801  777 HOH   A O   
4067 O  O   . HOH   D .   ? 0.36730 0.31465 0.28848 -0.01354 0.01318  0.01010  778 HOH   A O   
4068 O  O   . HOH   D .   ? 0.37778 0.33382 0.38459 0.02702  0.00750  -0.01713 779 HOH   A O   
4069 O  O   . HOH   D .   ? 0.43906 0.43972 0.46503 -0.00780 -0.01633 0.01550  780 HOH   A O   
4070 O  O   . HOH   D .   ? 0.43999 0.41198 0.45972 0.01324  -0.00543 -0.00503 781 HOH   A O   
4071 O  O   . HOH   D .   ? 0.47715 0.41315 0.40749 -0.06493 -0.03365 0.02025  782 HOH   A O   
4072 O  O   . HOH   D .   ? 0.27274 0.30615 0.31341 0.00931  0.01542  0.01438  783 HOH   A O   
4073 O  O   . HOH   D .   ? 0.42261 0.41444 0.39950 -0.03257 0.00276  0.02231  784 HOH   A O   
4074 O  O   . HOH   D .   ? 0.44107 0.40446 0.40904 -0.05282 -0.03997 0.01737  785 HOH   A O   
4075 O  O   . HOH   D .   ? 0.32181 0.35504 0.38407 0.01744  0.00276  0.01815  786 HOH   A O   
4076 O  O   . HOH   D .   ? 0.37859 0.35417 0.36669 -0.02699 -0.01857 0.01266  787 HOH   A O   
4077 O  O   . HOH   D .   ? 0.38878 0.39478 0.43570 0.03411  0.01509  -0.00151 788 HOH   A O   
4078 O  O   . HOH   D .   ? 0.58935 0.49005 0.49206 -0.05735 -0.01903 0.00898  789 HOH   A O   
4079 O  O   . HOH   D .   ? 0.54174 0.48282 0.44497 -0.02034 -0.01207 0.02394  790 HOH   A O   
4080 O  O   . HOH   D .   ? 0.42837 0.41231 0.43404 -0.01370 -0.01562 0.00984  791 HOH   A O   
4081 O  O   . HOH   D .   ? 0.46899 0.50404 0.50778 0.01999  0.02898  0.01136  792 HOH   A O   
4082 O  O   . HOH   D .   ? 0.47580 0.47827 0.47741 0.02703  -0.01764 0.06088  793 HOH   A O   
4083 O  O   . HOH   D .   ? 0.46133 0.40897 0.43749 0.01088  0.01189  -0.01156 794 HOH   A O   
4084 O  O   . HOH   D .   ? 0.45117 0.45553 0.48109 0.03883  0.02005  -0.00117 795 HOH   A O   
4085 O  O   . HOH   D .   ? 0.50862 0.49215 0.52450 0.00040  -0.00990 0.00311  796 HOH   A O   
4086 O  O   . HOH   D .   ? 0.47715 0.50055 0.51133 0.00900  -0.00303 0.00811  797 HOH   A O   
4087 O  O   . HOH   D .   ? 0.45151 0.47054 0.51365 0.01551  -0.01102 0.02425  798 HOH   A O   
4088 O  O   . HOH   D .   ? 0.51535 0.35411 0.38784 -0.01222 0.00982  -0.00139 799 HOH   A O   
4089 O  O   . HOH   D .   ? 0.55012 0.54536 0.55799 -0.00169 -0.01157 0.00076  800 HOH   A O   
4090 O  O   . HOH   D .   ? 0.43616 0.38993 0.37429 0.00143  0.00756  -0.00472 801 HOH   A O   
4091 O  O   . HOH   D .   ? 0.47491 0.41739 0.40253 -0.01101 0.01067  0.01054  802 HOH   A O   
4092 O  O   . HOH   D .   ? 0.48903 0.46083 0.48502 0.02291  0.01624  -0.01235 803 HOH   A O   
4093 O  O   . HOH   D .   ? 0.42748 0.40230 0.43857 0.00143  -0.00782 -0.00230 804 HOH   A O   
4094 O  O   . HOH   D .   ? 0.48925 0.47381 0.51056 0.02771  0.01134  -0.01631 805 HOH   A O   
4095 O  O   . HOH   D .   ? 0.43205 0.39520 0.37253 -0.00678 0.02057  0.00466  806 HOH   A O   
4096 O  O   . HOH   D .   ? 0.40815 0.38698 0.41325 0.01753  0.01296  -0.01066 807 HOH   A O   
4097 O  O   . HOH   D .   ? 0.46936 0.48538 0.47841 -0.03523 -0.03033 0.02396  808 HOH   A O   
4098 O  O   . HOH   D .   ? 0.46605 0.35963 0.37551 -0.02618 -0.00071 -0.00871 809 HOH   A O   
4099 O  O   . HOH   D .   ? 0.49369 0.43101 0.46542 -0.02527 -0.02540 0.00170  810 HOH   A O   
4100 O  O   . HOH   D .   ? 0.52498 0.47152 0.44532 -0.01708 0.01295  0.01250  811 HOH   A O   
4101 O  O   . HOH   D .   ? 0.45761 0.35775 0.38737 0.00934  0.02185  -0.01783 812 HOH   A O   
4102 O  O   . HOH   D .   ? 0.47439 0.35695 0.38411 0.00048  0.01958  -0.01776 813 HOH   A O   
4103 O  O   . HOH   D .   ? 0.43363 0.38941 0.41875 0.01659  0.01374  -0.01250 814 HOH   A O   
4104 O  O   . HOH   D .   ? 0.48189 0.46318 0.48410 0.02211  0.01782  -0.01199 815 HOH   A O   
4105 O  O   . HOH   D .   ? 0.48131 0.45735 0.48948 0.02170  0.01234  -0.01406 816 HOH   A O   
4106 O  O   . HOH   D .   ? 0.44118 0.32207 0.37521 0.01028  0.00394  -0.02375 817 HOH   A O   
4107 O  O   . HOH   D .   ? 0.43471 0.43086 0.40447 -0.05761 -0.01033 0.03660  818 HOH   A O   
4108 O  O   . HOH   D .   ? 0.48741 0.42837 0.39951 -0.01312 0.00555  0.01206  819 HOH   A O   
4109 O  O   . HOH   D .   ? 0.55485 0.62624 0.61693 -0.02864 -0.01785 0.05261  820 HOH   A O   
4110 O  O   . HOH   D .   ? 0.55604 0.43216 0.43106 -0.06038 -0.01084 0.01894  821 HOH   A O   
4111 O  O   . HOH   D .   ? 0.39616 0.46341 0.45863 0.00388  0.01571  0.03320  822 HOH   A O   
4112 O  O   . HOH   D .   ? 0.47406 0.45176 0.49082 0.00578  -0.00794 -0.00100 823 HOH   A O   
4113 O  O   . HOH   D .   ? 0.43564 0.51632 0.51215 -0.01699 -0.01243 0.05302  824 HOH   A O   
4114 O  O   . HOH   D .   ? 0.46489 0.51479 0.52345 -0.00355 -0.00327 0.03097  825 HOH   A O   
4115 O  O   . HOH   D .   ? 0.62469 0.40923 0.43810 -0.02616 0.01664  -0.01751 826 HOH   A O   
4116 O  O   . HOH   D .   ? 0.52241 0.50916 0.53506 0.02258  0.01581  -0.01172 827 HOH   A O   
4117 O  O   . HOH   D .   ? 0.57686 0.49264 0.54574 0.07270  0.01997  0.05268  828 HOH   A O   
4118 O  O   . HOH   D .   ? 0.45033 0.41519 0.43449 0.02495  0.01368  -0.00637 829 HOH   A O   
4119 O  O   . HOH   D .   ? 0.52764 0.51725 0.52981 0.00855  0.01634  -0.00024 830 HOH   A O   
4120 O  O   . HOH   D .   ? 0.51681 0.43044 0.45105 0.01794  0.03614  -0.01545 831 HOH   A O   
4121 O  O   . HOH   D .   ? 0.45885 0.42982 0.42310 0.01367  0.02723  -0.00988 832 HOH   A O   
4122 O  O   . HOH   D .   ? 0.36659 0.31234 0.28675 -0.01062 0.01088  0.00871  833 HOH   A O   
4123 O  O   . HOH   D .   ? 0.72316 0.57151 0.59229 -0.06865 -0.04521 -0.00057 834 HOH   A O   
4124 O  O   . HOH   D .   ? 0.62508 0.66294 0.66325 -0.00596 -0.00720 0.01960  835 HOH   A O   
4125 O  O   . HOH   D .   ? 0.48251 0.47840 0.45688 -0.04409 -0.00229 0.02960  836 HOH   A O   
4126 O  O   . HOH   D .   ? 0.44080 0.41540 0.42223 -0.03816 -0.02586 0.01892  837 HOH   A O   
4127 O  O   . HOH   D .   ? 0.48945 0.46778 0.49914 0.02299  0.01326  -0.01412 838 HOH   A O   
4128 O  O   . HOH   D .   ? 0.54965 0.54502 0.54830 -0.04228 -0.03249 0.03014  839 HOH   A O   
4129 O  O   . HOH   D .   ? 0.53892 0.50291 0.55821 0.01325  -0.00932 -0.00026 840 HOH   A O   
4130 O  O   . HOH   D .   ? 0.34271 0.36916 0.37779 0.01344  0.01912  0.00926  841 HOH   A O   
4131 O  O   . HOH   D .   ? 0.45105 0.30241 0.32933 -0.00118 0.02600  -0.02007 842 HOH   A O   
4132 O  O   . HOH   D .   ? 0.55603 0.43453 0.48163 0.03404  0.02460  -0.00048 843 HOH   A O   
4133 O  O   . HOH   D .   ? 0.62379 0.62687 0.63688 -0.02122 -0.01676 0.01370  844 HOH   A O   
4134 O  O   . HOH   D .   ? 0.46272 0.41975 0.44158 0.02420  0.01454  -0.00580 845 HOH   A O   
4135 O  O   . HOH   D .   ? 0.46987 0.48276 0.48883 -0.01959 -0.01543 0.01582  846 HOH   A O   
4136 O  O   . HOH   D .   ? 0.52178 0.48628 0.55460 0.05901  0.02942  -0.00203 847 HOH   A O   
4137 O  O   . HOH   D .   ? 0.45797 0.48578 0.49564 0.02214  0.02652  0.00707  848 HOH   A O   
# 
